data_8XU9
# 
_entry.id   8XU9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8XU9         pdb_00008xu9 10.2210/pdb8xu9/pdb 
WWPDB D_1300044220 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8XU9 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gfyang@mail.ccnu.edu.cn 
_pdbx_contact_author.name_first         Guang-Fu 
_pdbx_contact_author.name_last          Yang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4384-2593 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dong, J.'    1 ? 
'Lin, H.-Y.'  2 ? 
'Yang, G.-F.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of AtHPPD-YH20531 complex' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dong, J.'    1 ? 
primary 'Lin, H.-Y.'  2 ? 
primary 'Yang, G.-F.' 3 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '4-hydroxyphenylpyruvate dioxygenase'                                                            45952.727 1   
1.13.11.27 ? ? ? 
2 non-polymer syn 'COBALT (II) ION'                                                                                58.933    1   ? 
? ? ? 
3 non-polymer nat '2-fluoranyl-~{N}-(5-methyl-1,3,4-oxadiazol-2-yl)-3-propylsulfinyl-4-(trifluoromethyl)benzamide' 379.330   1   ? 
? ? ? 
4 water       nat water                                                                                            18.015    173 ? 
? ? ? 
# 
_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 '2-fluoranyl-~{N}-(5-methyl-1,3,4-oxadiazol-2-yl)-3-propylsulfinyl-4-(trifluoromethyl)benzamide' A1LW4 
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 
A1LW4 non-polymer         . '2-fluoranyl-~{N}-(5-methyl-1,3,4-oxadiazol-2-yl)-3-propylsulfinyl-4-(trifluoromethyl)benzamide' ? 
'C14 H13 F4 N3 O3 S' 379.330 
ALA   'L-peptide linking' y ALANINE                                                                                          ? 
'C3 H7 N O2'         89.093  
ARG   'L-peptide linking' y ARGININE                                                                                         ? 
'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                       ? 
'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                  ? 
'C4 H7 N O4'         133.103 
CO    non-polymer         . 'COBALT (II) ION'                                                                                ? 
'Co 2'               58.933  
CYS   'L-peptide linking' y CYSTEINE                                                                                         ? 
'C3 H7 N O2 S'       121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                        ? 
'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                  ? 
'C5 H9 N O4'         147.129 
GLY   'peptide linking'   y GLYCINE                                                                                          ? 
'C2 H5 N O2'         75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                        ? 
'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer         . WATER                                                                                            ? 
'H2 O'               18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                       ? 
'C6 H13 N O2'        131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                          ? 
'C6 H13 N O2'        131.173 
LYS   'L-peptide linking' y LYSINE                                                                                           ? 
'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking' y METHIONINE                                                                                       ? 
'C5 H11 N O2 S'      149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                    ? 
'C9 H11 N O2'        165.189 
PRO   'L-peptide linking' y PROLINE                                                                                          ? 
'C5 H9 N O2'         115.130 
SER   'L-peptide linking' y SERINE                                                                                           ? 
'C3 H7 N O3'         105.093 
THR   'L-peptide linking' y THREONINE                                                                                        ? 
'C4 H9 N O3'         119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                       ? 
'C11 H12 N2 O2'      204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                         ? 
'C9 H11 N O3'        181.189 
VAL   'L-peptide linking' y VALINE                                                                                           ? 
'C5 H11 N O2'        117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   29  ?   ?   ?   A . n 
A 1 2   SER 2   30  ?   ?   ?   A . n 
A 1 3   HIS 3   31  ?   ?   ?   A . n 
A 1 4   MET 4   32  ?   ?   ?   A . n 
A 1 5   VAL 5   33  ?   ?   ?   A . n 
A 1 6   ARG 6   34  ?   ?   ?   A . n 
A 1 7   LYS 7   35  35  LYS LYS A . n 
A 1 8   ASN 8   36  36  ASN ASN A . n 
A 1 9   PRO 9   37  37  PRO PRO A . n 
A 1 10  LYS 10  38  38  LYS LYS A . n 
A 1 11  SER 11  39  39  SER SER A . n 
A 1 12  ASP 12  40  40  ASP ASP A . n 
A 1 13  LYS 13  41  41  LYS LYS A . n 
A 1 14  PHE 14  42  42  PHE PHE A . n 
A 1 15  LYS 15  43  43  LYS LYS A . n 
A 1 16  VAL 16  44  44  VAL VAL A . n 
A 1 17  LYS 17  45  45  LYS LYS A . n 
A 1 18  ARG 18  46  46  ARG ARG A . n 
A 1 19  PHE 19  47  47  PHE PHE A . n 
A 1 20  HIS 20  48  48  HIS HIS A . n 
A 1 21  HIS 21  49  49  HIS HIS A . n 
A 1 22  ILE 22  50  50  ILE ILE A . n 
A 1 23  GLU 23  51  51  GLU GLU A . n 
A 1 24  PHE 24  52  52  PHE PHE A . n 
A 1 25  TRP 25  53  53  TRP TRP A . n 
A 1 26  CYS 26  54  54  CYS CYS A . n 
A 1 27  GLY 27  55  55  GLY GLY A . n 
A 1 28  ASP 28  56  56  ASP ASP A . n 
A 1 29  ALA 29  57  57  ALA ALA A . n 
A 1 30  THR 30  58  58  THR THR A . n 
A 1 31  ASN 31  59  59  ASN ASN A . n 
A 1 32  VAL 32  60  60  VAL VAL A . n 
A 1 33  ALA 33  61  61  ALA ALA A . n 
A 1 34  ARG 34  62  62  ARG ARG A . n 
A 1 35  ARG 35  63  63  ARG ARG A . n 
A 1 36  PHE 36  64  64  PHE PHE A . n 
A 1 37  SER 37  65  65  SER SER A . n 
A 1 38  TRP 38  66  66  TRP TRP A . n 
A 1 39  GLY 39  67  67  GLY GLY A . n 
A 1 40  LEU 40  68  68  LEU LEU A . n 
A 1 41  GLY 41  69  69  GLY GLY A . n 
A 1 42  MET 42  70  70  MET MET A . n 
A 1 43  ARG 43  71  71  ARG ARG A . n 
A 1 44  PHE 44  72  72  PHE PHE A . n 
A 1 45  SER 45  73  73  SER SER A . n 
A 1 46  ALA 46  74  74  ALA ALA A . n 
A 1 47  LYS 47  75  75  LYS LYS A . n 
A 1 48  SER 48  76  76  SER SER A . n 
A 1 49  ASP 49  77  77  ASP ASP A . n 
A 1 50  LEU 50  78  78  LEU LEU A . n 
A 1 51  SER 51  79  79  SER SER A . n 
A 1 52  THR 52  80  80  THR THR A . n 
A 1 53  GLY 53  81  81  GLY GLY A . n 
A 1 54  ASN 54  82  82  ASN ASN A . n 
A 1 55  MET 55  83  83  MET MET A . n 
A 1 56  VAL 56  84  84  VAL VAL A . n 
A 1 57  HIS 57  85  85  HIS HIS A . n 
A 1 58  ALA 58  86  86  ALA ALA A . n 
A 1 59  SER 59  87  87  SER SER A . n 
A 1 60  TYR 60  88  88  TYR TYR A . n 
A 1 61  LEU 61  89  89  LEU LEU A . n 
A 1 62  LEU 62  90  90  LEU LEU A . n 
A 1 63  THR 63  91  91  THR THR A . n 
A 1 64  SER 64  92  92  SER SER A . n 
A 1 65  GLY 65  93  93  GLY GLY A . n 
A 1 66  ASP 66  94  94  ASP ASP A . n 
A 1 67  LEU 67  95  95  LEU LEU A . n 
A 1 68  ARG 68  96  96  ARG ARG A . n 
A 1 69  PHE 69  97  97  PHE PHE A . n 
A 1 70  LEU 70  98  98  LEU LEU A . n 
A 1 71  PHE 71  99  99  PHE PHE A . n 
A 1 72  THR 72  100 100 THR THR A . n 
A 1 73  ALA 73  101 101 ALA ALA A . n 
A 1 74  PRO 74  102 102 PRO PRO A . n 
A 1 75  TYR 75  103 103 TYR TYR A . n 
A 1 76  SER 76  104 104 SER SER A . n 
A 1 77  PRO 77  105 105 PRO PRO A . n 
A 1 78  SER 78  106 106 SER SER A . n 
A 1 79  LEU 79  107 107 LEU LEU A . n 
A 1 80  SER 80  108 108 SER SER A . n 
A 1 81  ALA 81  109 109 ALA ALA A . n 
A 1 82  GLY 82  110 110 GLY GLY A . n 
A 1 83  GLU 83  111 111 GLU GLU A . n 
A 1 84  ILE 84  112 112 ILE ILE A . n 
A 1 85  LYS 85  113 113 LYS LYS A . n 
A 1 86  PRO 86  114 114 PRO PRO A . n 
A 1 87  THR 87  115 115 THR THR A . n 
A 1 88  THR 88  116 116 THR THR A . n 
A 1 89  THR 89  117 117 THR THR A . n 
A 1 90  ALA 90  118 118 ALA ALA A . n 
A 1 91  SER 91  119 119 SER SER A . n 
A 1 92  ILE 92  120 120 ILE ILE A . n 
A 1 93  PRO 93  121 121 PRO PRO A . n 
A 1 94  SER 94  122 122 SER SER A . n 
A 1 95  PHE 95  123 123 PHE PHE A . n 
A 1 96  ASP 96  124 124 ASP ASP A . n 
A 1 97  HIS 97  125 125 HIS HIS A . n 
A 1 98  GLY 98  126 126 GLY GLY A . n 
A 1 99  SER 99  127 127 SER SER A . n 
A 1 100 CYS 100 128 128 CYS CYS A . n 
A 1 101 ARG 101 129 129 ARG ARG A . n 
A 1 102 SER 102 130 130 SER SER A . n 
A 1 103 PHE 103 131 131 PHE PHE A . n 
A 1 104 PHE 104 132 132 PHE PHE A . n 
A 1 105 SER 105 133 133 SER SER A . n 
A 1 106 SER 106 134 134 SER SER A . n 
A 1 107 HIS 107 135 135 HIS HIS A . n 
A 1 108 GLY 108 136 136 GLY GLY A . n 
A 1 109 LEU 109 137 137 LEU LEU A . n 
A 1 110 GLY 110 138 138 GLY GLY A . n 
A 1 111 VAL 111 139 139 VAL VAL A . n 
A 1 112 ARG 112 140 140 ARG ARG A . n 
A 1 113 ALA 113 141 141 ALA ALA A . n 
A 1 114 VAL 114 142 142 VAL VAL A . n 
A 1 115 ALA 115 143 143 ALA ALA A . n 
A 1 116 ILE 116 144 144 ILE ILE A . n 
A 1 117 GLU 117 145 145 GLU GLU A . n 
A 1 118 VAL 118 146 146 VAL VAL A . n 
A 1 119 GLU 119 147 147 GLU GLU A . n 
A 1 120 ASP 120 148 148 ASP ASP A . n 
A 1 121 ALA 121 149 149 ALA ALA A . n 
A 1 122 GLU 122 150 150 GLU GLU A . n 
A 1 123 SER 123 151 151 SER SER A . n 
A 1 124 ALA 124 152 152 ALA ALA A . n 
A 1 125 PHE 125 153 153 PHE PHE A . n 
A 1 126 SER 126 154 154 SER SER A . n 
A 1 127 ILE 127 155 155 ILE ILE A . n 
A 1 128 SER 128 156 156 SER SER A . n 
A 1 129 VAL 129 157 157 VAL VAL A . n 
A 1 130 ALA 130 158 158 ALA ALA A . n 
A 1 131 ASN 131 159 159 ASN ASN A . n 
A 1 132 GLY 132 160 160 GLY GLY A . n 
A 1 133 ALA 133 161 161 ALA ALA A . n 
A 1 134 ILE 134 162 162 ILE ILE A . n 
A 1 135 PRO 135 163 163 PRO PRO A . n 
A 1 136 SER 136 164 164 SER SER A . n 
A 1 137 SER 137 165 165 SER SER A . n 
A 1 138 PRO 138 166 166 PRO PRO A . n 
A 1 139 PRO 139 167 167 PRO PRO A . n 
A 1 140 ILE 140 168 168 ILE ILE A . n 
A 1 141 VAL 141 169 169 VAL VAL A . n 
A 1 142 LEU 142 170 170 LEU LEU A . n 
A 1 143 ASN 143 171 171 ASN ASN A . n 
A 1 144 GLU 144 172 172 GLU GLU A . n 
A 1 145 ALA 145 173 173 ALA ALA A . n 
A 1 146 VAL 146 174 174 VAL VAL A . n 
A 1 147 THR 147 175 175 THR THR A . n 
A 1 148 ILE 148 176 176 ILE ILE A . n 
A 1 149 ALA 149 177 177 ALA ALA A . n 
A 1 150 GLU 150 178 178 GLU GLU A . n 
A 1 151 VAL 151 179 179 VAL VAL A . n 
A 1 152 LYS 152 180 180 LYS LYS A . n 
A 1 153 LEU 153 181 181 LEU LEU A . n 
A 1 154 TYR 154 182 182 TYR TYR A . n 
A 1 155 GLY 155 183 183 GLY GLY A . n 
A 1 156 ASP 156 184 184 ASP ASP A . n 
A 1 157 VAL 157 185 185 VAL VAL A . n 
A 1 158 VAL 158 186 186 VAL VAL A . n 
A 1 159 LEU 159 187 187 LEU LEU A . n 
A 1 160 ARG 160 188 188 ARG ARG A . n 
A 1 161 TYR 161 189 189 TYR TYR A . n 
A 1 162 VAL 162 190 190 VAL VAL A . n 
A 1 163 SER 163 191 191 SER SER A . n 
A 1 164 TYR 164 192 192 TYR TYR A . n 
A 1 165 LYS 165 193 193 LYS LYS A . n 
A 1 166 ALA 166 194 194 ALA ALA A . n 
A 1 167 GLU 167 195 ?   ?   ?   A . n 
A 1 168 ASP 168 196 ?   ?   ?   A . n 
A 1 169 THR 169 197 ?   ?   ?   A . n 
A 1 170 GLU 170 198 ?   ?   ?   A . n 
A 1 171 LYS 171 199 ?   ?   ?   A . n 
A 1 172 SER 172 200 ?   ?   ?   A . n 
A 1 173 GLU 173 201 ?   ?   ?   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 ?   ?   ?   A . n 
A 1 225 PHE 225 253 ?   ?   ?   A . n 
A 1 226 THR 226 254 ?   ?   ?   A . n 
A 1 227 ALA 227 255 ?   ?   ?   A . n 
A 1 228 ASP 228 256 ?   ?   ?   A . n 
A 1 229 ASP 229 257 ?   ?   ?   A . n 
A 1 230 VAL 230 258 ?   ?   ?   A . n 
A 1 231 GLY 231 259 ?   ?   ?   A . n 
A 1 232 THR 232 260 ?   ?   ?   A . n 
A 1 233 ALA 233 261 ?   ?   ?   A . n 
A 1 234 GLU 234 262 262 GLU GLU A . n 
A 1 235 SER 235 263 263 SER SER A . n 
A 1 236 GLY 236 264 264 GLY GLY A . n 
A 1 237 LEU 237 265 265 LEU LEU A . n 
A 1 238 ASN 238 266 266 ASN ASN A . n 
A 1 239 SER 239 267 267 SER SER A . n 
A 1 240 ALA 240 268 268 ALA ALA A . n 
A 1 241 VAL 241 269 269 VAL VAL A . n 
A 1 242 LEU 242 270 270 LEU LEU A . n 
A 1 243 ALA 243 271 271 ALA ALA A . n 
A 1 244 SER 244 272 272 SER SER A . n 
A 1 245 ASN 245 273 273 ASN ASN A . n 
A 1 246 ASP 246 274 274 ASP ASP A . n 
A 1 247 GLU 247 275 275 GLU GLU A . n 
A 1 248 MET 248 276 276 MET MET A . n 
A 1 249 VAL 249 277 277 VAL VAL A . n 
A 1 250 LEU 250 278 278 LEU LEU A . n 
A 1 251 LEU 251 279 279 LEU LEU A . n 
A 1 252 PRO 252 280 280 PRO PRO A . n 
A 1 253 ILE 253 281 281 ILE ILE A . n 
A 1 254 ASN 254 282 282 ASN ASN A . n 
A 1 255 GLU 255 283 283 GLU GLU A . n 
A 1 256 PRO 256 284 284 PRO PRO A . n 
A 1 257 VAL 257 285 285 VAL VAL A . n 
A 1 258 HIS 258 286 286 HIS HIS A . n 
A 1 259 GLY 259 287 287 GLY GLY A . n 
A 1 260 THR 260 288 288 THR THR A . n 
A 1 261 LYS 261 289 289 LYS LYS A . n 
A 1 262 ARG 262 290 290 ARG ARG A . n 
A 1 263 LYS 263 291 291 LYS LYS A . n 
A 1 264 SER 264 292 292 SER SER A . n 
A 1 265 GLN 265 293 293 GLN GLN A . n 
A 1 266 ILE 266 294 294 ILE ILE A . n 
A 1 267 GLN 267 295 295 GLN GLN A . n 
A 1 268 THR 268 296 296 THR THR A . n 
A 1 269 TYR 269 297 297 TYR TYR A . n 
A 1 270 LEU 270 298 298 LEU LEU A . n 
A 1 271 GLU 271 299 299 GLU GLU A . n 
A 1 272 HIS 272 300 300 HIS HIS A . n 
A 1 273 ASN 273 301 301 ASN ASN A . n 
A 1 274 GLU 274 302 302 GLU GLU A . n 
A 1 275 GLY 275 303 303 GLY GLY A . n 
A 1 276 ALA 276 304 304 ALA ALA A . n 
A 1 277 GLY 277 305 305 GLY GLY A . n 
A 1 278 LEU 278 306 306 LEU LEU A . n 
A 1 279 GLN 279 307 307 GLN GLN A . n 
A 1 280 HIS 280 308 308 HIS HIS A . n 
A 1 281 LEU 281 309 309 LEU LEU A . n 
A 1 282 ALA 282 310 310 ALA ALA A . n 
A 1 283 LEU 283 311 311 LEU LEU A . n 
A 1 284 MET 284 312 312 MET MET A . n 
A 1 285 SER 285 313 313 SER SER A . n 
A 1 286 GLU 286 314 314 GLU GLU A . n 
A 1 287 ASP 287 315 315 ASP ASP A . n 
A 1 288 ILE 288 316 316 ILE ILE A . n 
A 1 289 PHE 289 317 317 PHE PHE A . n 
A 1 290 ARG 290 318 318 ARG ARG A . n 
A 1 291 THR 291 319 319 THR THR A . n 
A 1 292 LEU 292 320 320 LEU LEU A . n 
A 1 293 ARG 293 321 321 ARG ARG A . n 
A 1 294 GLU 294 322 322 GLU GLU A . n 
A 1 295 MET 295 323 323 MET MET A . n 
A 1 296 ARG 296 324 324 ARG ARG A . n 
A 1 297 LYS 297 325 325 LYS LYS A . n 
A 1 298 ARG 298 326 326 ARG ARG A . n 
A 1 299 SER 299 327 327 SER SER A . n 
A 1 300 SER 300 328 328 SER SER A . n 
A 1 301 ILE 301 329 329 ILE ILE A . n 
A 1 302 GLY 302 330 330 GLY GLY A . n 
A 1 303 GLY 303 331 331 GLY GLY A . n 
A 1 304 PHE 304 332 332 PHE PHE A . n 
A 1 305 ASP 305 333 333 ASP ASP A . n 
A 1 306 PHE 306 334 334 PHE PHE A . n 
A 1 307 MET 307 335 335 MET MET A . n 
A 1 308 PRO 308 336 336 PRO PRO A . n 
A 1 309 SER 309 337 337 SER SER A . n 
A 1 310 PRO 310 338 338 PRO PRO A . n 
A 1 311 PRO 311 339 339 PRO PRO A . n 
A 1 312 PRO 312 340 340 PRO PRO A . n 
A 1 313 THR 313 341 341 THR THR A . n 
A 1 314 TYR 314 342 342 TYR TYR A . n 
A 1 315 TYR 315 343 343 TYR TYR A . n 
A 1 316 GLN 316 344 344 GLN GLN A . n 
A 1 317 ASN 317 345 345 ASN ASN A . n 
A 1 318 LEU 318 346 346 LEU LEU A . n 
A 1 319 LYS 319 347 347 LYS LYS A . n 
A 1 320 LYS 320 348 348 LYS LYS A . n 
A 1 321 ARG 321 349 349 ARG ARG A . n 
A 1 322 VAL 322 350 350 VAL VAL A . n 
A 1 323 GLY 323 351 351 GLY GLY A . n 
A 1 324 ASP 324 352 352 ASP ASP A . n 
A 1 325 VAL 325 353 353 VAL VAL A . n 
A 1 326 LEU 326 354 354 LEU LEU A . n 
A 1 327 SER 327 355 355 SER SER A . n 
A 1 328 ASP 328 356 356 ASP ASP A . n 
A 1 329 ASP 329 357 357 ASP ASP A . n 
A 1 330 GLN 330 358 358 GLN GLN A . n 
A 1 331 ILE 331 359 359 ILE ILE A . n 
A 1 332 LYS 332 360 360 LYS LYS A . n 
A 1 333 GLU 333 361 361 GLU GLU A . n 
A 1 334 CYS 334 362 362 CYS CYS A . n 
A 1 335 GLU 335 363 363 GLU GLU A . n 
A 1 336 GLU 336 364 364 GLU GLU A . n 
A 1 337 LEU 337 365 365 LEU LEU A . n 
A 1 338 GLY 338 366 366 GLY GLY A . n 
A 1 339 ILE 339 367 367 ILE ILE A . n 
A 1 340 LEU 340 368 368 LEU LEU A . n 
A 1 341 VAL 341 369 369 VAL VAL A . n 
A 1 342 ASP 342 370 370 ASP ASP A . n 
A 1 343 ARG 343 371 371 ARG ARG A . n 
A 1 344 ASP 344 372 372 ASP ASP A . n 
A 1 345 ASP 345 373 373 ASP ASP A . n 
A 1 346 GLN 346 374 374 GLN GLN A . n 
A 1 347 GLY 347 375 375 GLY GLY A . n 
A 1 348 THR 348 376 376 THR THR A . n 
A 1 349 LEU 349 377 377 LEU LEU A . n 
A 1 350 LEU 350 378 378 LEU LEU A . n 
A 1 351 GLN 351 379 379 GLN GLN A . n 
A 1 352 ILE 352 380 380 ILE ILE A . n 
A 1 353 PHE 353 381 381 PHE PHE A . n 
A 1 354 THR 354 382 382 THR THR A . n 
A 1 355 LYS 355 383 383 LYS LYS A . n 
A 1 356 PRO 356 384 384 PRO PRO A . n 
A 1 357 LEU 357 385 385 LEU LEU A . n 
A 1 358 GLY 358 386 386 GLY GLY A . n 
A 1 359 ASP 359 387 387 ASP ASP A . n 
A 1 360 ARG 360 388 388 ARG ARG A . n 
A 1 361 PRO 361 389 389 PRO PRO A . n 
A 1 362 THR 362 390 390 THR THR A . n 
A 1 363 ILE 363 391 391 ILE ILE A . n 
A 1 364 PHE 364 392 392 PHE PHE A . n 
A 1 365 ILE 365 393 393 ILE ILE A . n 
A 1 366 GLU 366 394 394 GLU GLU A . n 
A 1 367 ILE 367 395 395 ILE ILE A . n 
A 1 368 ILE 368 396 396 ILE ILE A . n 
A 1 369 GLN 369 397 397 GLN GLN A . n 
A 1 370 ARG 370 398 398 ARG ARG A . n 
A 1 371 VAL 371 399 399 VAL VAL A . n 
A 1 372 GLY 372 400 400 GLY GLY A . n 
A 1 373 CYS 373 401 401 CYS CYS A . n 
A 1 374 MET 374 402 402 MET MET A . n 
A 1 375 MET 375 403 403 MET MET A . n 
A 1 376 LYS 376 404 ?   ?   ?   A . n 
A 1 377 ASP 377 405 ?   ?   ?   A . n 
A 1 378 GLU 378 406 ?   ?   ?   A . n 
A 1 379 GLU 379 407 ?   ?   ?   A . n 
A 1 380 GLY 380 408 ?   ?   ?   A . n 
A 1 381 LYS 381 409 ?   ?   ?   A . n 
A 1 382 ALA 382 410 ?   ?   ?   A . n 
A 1 383 TYR 383 411 411 TYR TYR A . n 
A 1 384 GLN 384 412 412 GLN GLN A . n 
A 1 385 SER 385 413 413 SER SER A . n 
A 1 386 GLY 386 414 414 GLY GLY A . n 
A 1 387 GLY 387 415 415 GLY GLY A . n 
A 1 388 CYS 388 416 416 CYS CYS A . n 
A 1 389 GLY 389 417 417 GLY GLY A . n 
A 1 390 GLY 390 418 418 GLY GLY A . n 
A 1 391 PHE 391 419 419 PHE PHE A . n 
A 1 392 GLY 392 420 420 GLY GLY A . n 
A 1 393 LYS 393 421 421 LYS LYS A . n 
A 1 394 GLY 394 422 422 GLY GLY A . n 
A 1 395 ASN 395 423 423 ASN ASN A . n 
A 1 396 PHE 396 424 424 PHE PHE A . n 
A 1 397 SER 397 425 425 SER SER A . n 
A 1 398 GLU 398 426 426 GLU GLU A . n 
A 1 399 LEU 399 427 427 LEU LEU A . n 
A 1 400 PHE 400 428 428 PHE PHE A . n 
A 1 401 LYS 401 429 429 LYS LYS A . n 
A 1 402 SER 402 430 430 SER SER A . n 
A 1 403 ILE 403 431 431 ILE ILE A . n 
A 1 404 GLU 404 432 432 GLU GLU A . n 
A 1 405 GLU 405 433 433 GLU GLU A . n 
A 1 406 TYR 406 434 434 TYR TYR A . n 
A 1 407 GLU 407 435 435 GLU GLU A . n 
A 1 408 LYS 408 436 436 LYS LYS A . n 
A 1 409 THR 409 437 ?   ?   ?   A . n 
A 1 410 LEU 410 438 ?   ?   ?   A . n 
A 1 411 GLU 411 439 ?   ?   ?   A . n 
A 1 412 ALA 412 440 ?   ?   ?   A . n 
A 1 413 LYS 413 441 ?   ?   ?   A . n 
A 1 414 GLN 414 442 ?   ?   ?   A . n 
A 1 415 LEU 415 443 ?   ?   ?   A . n 
A 1 416 VAL 416 444 ?   ?   ?   A . n 
A 1 417 GLY 417 445 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CO    1   501 1   CO    CO  A . 
C 3 A1LW4 1   502 501 A1LW4 LIG A . 
D 4 HOH   1   601 148 HOH   HOH A . 
D 4 HOH   2   602 26  HOH   HOH A . 
D 4 HOH   3   603 54  HOH   HOH A . 
D 4 HOH   4   604 53  HOH   HOH A . 
D 4 HOH   5   605 170 HOH   HOH A . 
D 4 HOH   6   606 131 HOH   HOH A . 
D 4 HOH   7   607 94  HOH   HOH A . 
D 4 HOH   8   608 135 HOH   HOH A . 
D 4 HOH   9   609 25  HOH   HOH A . 
D 4 HOH   10  610 168 HOH   HOH A . 
D 4 HOH   11  611 41  HOH   HOH A . 
D 4 HOH   12  612 138 HOH   HOH A . 
D 4 HOH   13  613 161 HOH   HOH A . 
D 4 HOH   14  614 89  HOH   HOH A . 
D 4 HOH   15  615 82  HOH   HOH A . 
D 4 HOH   16  616 153 HOH   HOH A . 
D 4 HOH   17  617 8   HOH   HOH A . 
D 4 HOH   18  618 85  HOH   HOH A . 
D 4 HOH   19  619 21  HOH   HOH A . 
D 4 HOH   20  620 7   HOH   HOH A . 
D 4 HOH   21  621 127 HOH   HOH A . 
D 4 HOH   22  622 35  HOH   HOH A . 
D 4 HOH   23  623 63  HOH   HOH A . 
D 4 HOH   24  624 57  HOH   HOH A . 
D 4 HOH   25  625 157 HOH   HOH A . 
D 4 HOH   26  626 90  HOH   HOH A . 
D 4 HOH   27  627 43  HOH   HOH A . 
D 4 HOH   28  628 150 HOH   HOH A . 
D 4 HOH   29  629 59  HOH   HOH A . 
D 4 HOH   30  630 36  HOH   HOH A . 
D 4 HOH   31  631 111 HOH   HOH A . 
D 4 HOH   32  632 37  HOH   HOH A . 
D 4 HOH   33  633 18  HOH   HOH A . 
D 4 HOH   34  634 13  HOH   HOH A . 
D 4 HOH   35  635 70  HOH   HOH A . 
D 4 HOH   36  636 1   HOH   HOH A . 
D 4 HOH   37  637 9   HOH   HOH A . 
D 4 HOH   38  638 3   HOH   HOH A . 
D 4 HOH   39  639 31  HOH   HOH A . 
D 4 HOH   40  640 101 HOH   HOH A . 
D 4 HOH   41  641 112 HOH   HOH A . 
D 4 HOH   42  642 141 HOH   HOH A . 
D 4 HOH   43  643 67  HOH   HOH A . 
D 4 HOH   44  644 5   HOH   HOH A . 
D 4 HOH   45  645 38  HOH   HOH A . 
D 4 HOH   46  646 86  HOH   HOH A . 
D 4 HOH   47  647 32  HOH   HOH A . 
D 4 HOH   48  648 73  HOH   HOH A . 
D 4 HOH   49  649 171 HOH   HOH A . 
D 4 HOH   50  650 46  HOH   HOH A . 
D 4 HOH   51  651 60  HOH   HOH A . 
D 4 HOH   52  652 48  HOH   HOH A . 
D 4 HOH   53  653 92  HOH   HOH A . 
D 4 HOH   54  654 56  HOH   HOH A . 
D 4 HOH   55  655 12  HOH   HOH A . 
D 4 HOH   56  656 20  HOH   HOH A . 
D 4 HOH   57  657 106 HOH   HOH A . 
D 4 HOH   58  658 40  HOH   HOH A . 
D 4 HOH   59  659 52  HOH   HOH A . 
D 4 HOH   60  660 64  HOH   HOH A . 
D 4 HOH   61  661 62  HOH   HOH A . 
D 4 HOH   62  662 144 HOH   HOH A . 
D 4 HOH   63  663 42  HOH   HOH A . 
D 4 HOH   64  664 69  HOH   HOH A . 
D 4 HOH   65  665 93  HOH   HOH A . 
D 4 HOH   66  666 11  HOH   HOH A . 
D 4 HOH   67  667 142 HOH   HOH A . 
D 4 HOH   68  668 109 HOH   HOH A . 
D 4 HOH   69  669 80  HOH   HOH A . 
D 4 HOH   70  670 72  HOH   HOH A . 
D 4 HOH   71  671 107 HOH   HOH A . 
D 4 HOH   72  672 103 HOH   HOH A . 
D 4 HOH   73  673 165 HOH   HOH A . 
D 4 HOH   74  674 139 HOH   HOH A . 
D 4 HOH   75  675 45  HOH   HOH A . 
D 4 HOH   76  676 24  HOH   HOH A . 
D 4 HOH   77  677 28  HOH   HOH A . 
D 4 HOH   78  678 27  HOH   HOH A . 
D 4 HOH   79  679 156 HOH   HOH A . 
D 4 HOH   80  680 117 HOH   HOH A . 
D 4 HOH   81  681 160 HOH   HOH A . 
D 4 HOH   82  682 29  HOH   HOH A . 
D 4 HOH   83  683 10  HOH   HOH A . 
D 4 HOH   84  684 71  HOH   HOH A . 
D 4 HOH   85  685 162 HOH   HOH A . 
D 4 HOH   86  686 129 HOH   HOH A . 
D 4 HOH   87  687 137 HOH   HOH A . 
D 4 HOH   88  688 146 HOH   HOH A . 
D 4 HOH   89  689 105 HOH   HOH A . 
D 4 HOH   90  690 96  HOH   HOH A . 
D 4 HOH   91  691 84  HOH   HOH A . 
D 4 HOH   92  692 68  HOH   HOH A . 
D 4 HOH   93  693 4   HOH   HOH A . 
D 4 HOH   94  694 22  HOH   HOH A . 
D 4 HOH   95  695 91  HOH   HOH A . 
D 4 HOH   96  696 61  HOH   HOH A . 
D 4 HOH   97  697 108 HOH   HOH A . 
D 4 HOH   98  698 16  HOH   HOH A . 
D 4 HOH   99  699 78  HOH   HOH A . 
D 4 HOH   100 700 49  HOH   HOH A . 
D 4 HOH   101 701 79  HOH   HOH A . 
D 4 HOH   102 702 140 HOH   HOH A . 
D 4 HOH   103 703 17  HOH   HOH A . 
D 4 HOH   104 704 66  HOH   HOH A . 
D 4 HOH   105 705 58  HOH   HOH A . 
D 4 HOH   106 706 51  HOH   HOH A . 
D 4 HOH   107 707 163 HOH   HOH A . 
D 4 HOH   108 708 14  HOH   HOH A . 
D 4 HOH   109 709 172 HOH   HOH A . 
D 4 HOH   110 710 81  HOH   HOH A . 
D 4 HOH   111 711 119 HOH   HOH A . 
D 4 HOH   112 712 125 HOH   HOH A . 
D 4 HOH   113 713 88  HOH   HOH A . 
D 4 HOH   114 714 33  HOH   HOH A . 
D 4 HOH   115 715 47  HOH   HOH A . 
D 4 HOH   116 716 164 HOH   HOH A . 
D 4 HOH   117 717 39  HOH   HOH A . 
D 4 HOH   118 718 87  HOH   HOH A . 
D 4 HOH   119 719 151 HOH   HOH A . 
D 4 HOH   120 720 113 HOH   HOH A . 
D 4 HOH   121 721 83  HOH   HOH A . 
D 4 HOH   122 722 74  HOH   HOH A . 
D 4 HOH   123 723 44  HOH   HOH A . 
D 4 HOH   124 724 130 HOH   HOH A . 
D 4 HOH   125 725 121 HOH   HOH A . 
D 4 HOH   126 726 169 HOH   HOH A . 
D 4 HOH   127 727 98  HOH   HOH A . 
D 4 HOH   128 728 34  HOH   HOH A . 
D 4 HOH   129 729 19  HOH   HOH A . 
D 4 HOH   130 730 122 HOH   HOH A . 
D 4 HOH   131 731 76  HOH   HOH A . 
D 4 HOH   132 732 149 HOH   HOH A . 
D 4 HOH   133 733 6   HOH   HOH A . 
D 4 HOH   134 734 15  HOH   HOH A . 
D 4 HOH   135 735 30  HOH   HOH A . 
D 4 HOH   136 736 132 HOH   HOH A . 
D 4 HOH   137 737 55  HOH   HOH A . 
D 4 HOH   138 738 110 HOH   HOH A . 
D 4 HOH   139 739 133 HOH   HOH A . 
D 4 HOH   140 740 154 HOH   HOH A . 
D 4 HOH   141 741 99  HOH   HOH A . 
D 4 HOH   142 742 118 HOH   HOH A . 
D 4 HOH   143 743 97  HOH   HOH A . 
D 4 HOH   144 744 136 HOH   HOH A . 
D 4 HOH   145 745 75  HOH   HOH A . 
D 4 HOH   146 746 126 HOH   HOH A . 
D 4 HOH   147 747 115 HOH   HOH A . 
D 4 HOH   148 748 50  HOH   HOH A . 
D 4 HOH   149 749 95  HOH   HOH A . 
D 4 HOH   150 750 102 HOH   HOH A . 
D 4 HOH   151 751 2   HOH   HOH A . 
D 4 HOH   152 752 128 HOH   HOH A . 
D 4 HOH   153 753 159 HOH   HOH A . 
D 4 HOH   154 754 114 HOH   HOH A . 
D 4 HOH   155 755 155 HOH   HOH A . 
D 4 HOH   156 756 124 HOH   HOH A . 
D 4 HOH   157 757 143 HOH   HOH A . 
D 4 HOH   158 758 104 HOH   HOH A . 
D 4 HOH   159 759 123 HOH   HOH A . 
D 4 HOH   160 760 158 HOH   HOH A . 
D 4 HOH   161 761 145 HOH   HOH A . 
D 4 HOH   162 762 100 HOH   HOH A . 
D 4 HOH   163 763 134 HOH   HOH A . 
D 4 HOH   164 764 173 HOH   HOH A . 
D 4 HOH   165 765 167 HOH   HOH A . 
D 4 HOH   166 766 166 HOH   HOH A . 
D 4 HOH   167 767 147 HOH   HOH A . 
D 4 HOH   168 768 152 HOH   HOH A . 
D 4 HOH   169 769 23  HOH   HOH A . 
D 4 HOH   170 770 77  HOH   HOH A . 
D 4 HOH   171 771 65  HOH   HOH A . 
D 4 HOH   172 772 116 HOH   HOH A . 
D 4 HOH   173 773 120 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 35  ? CG  ? A LYS 7   CG  
2  1 Y 1 A LYS 35  ? CD  ? A LYS 7   CD  
3  1 Y 1 A LYS 35  ? CE  ? A LYS 7   CE  
4  1 Y 1 A LYS 35  ? NZ  ? A LYS 7   NZ  
5  1 Y 1 A LYS 193 ? CG  ? A LYS 165 CG  
6  1 Y 1 A LYS 193 ? CD  ? A LYS 165 CD  
7  1 Y 1 A LYS 193 ? CE  ? A LYS 165 CE  
8  1 Y 1 A LYS 193 ? NZ  ? A LYS 165 NZ  
9  1 Y 1 A ARG 208 ? CG  ? A ARG 180 CG  
10 1 Y 1 A ARG 208 ? CD  ? A ARG 180 CD  
11 1 Y 1 A ARG 208 ? NE  ? A ARG 180 NE  
12 1 Y 1 A ARG 208 ? CZ  ? A ARG 180 CZ  
13 1 Y 1 A ARG 208 ? NH1 ? A ARG 180 NH1 
14 1 Y 1 A ARG 208 ? NH2 ? A ARG 180 NH2 
15 1 Y 1 A GLU 210 ? CG  ? A GLU 182 CG  
16 1 Y 1 A GLU 210 ? CD  ? A GLU 182 CD  
17 1 Y 1 A GLU 210 ? OE1 ? A GLU 182 OE1 
18 1 Y 1 A GLU 210 ? OE2 ? A GLU 182 OE2 
19 1 Y 1 A GLU 262 ? CG  ? A GLU 234 CG  
20 1 Y 1 A GLU 262 ? CD  ? A GLU 234 CD  
21 1 Y 1 A GLU 262 ? OE1 ? A GLU 234 OE1 
22 1 Y 1 A GLU 262 ? OE2 ? A GLU 234 OE2 
23 1 Y 1 A LYS 289 ? CG  ? A LYS 261 CG  
24 1 Y 1 A LYS 289 ? CD  ? A LYS 261 CD  
25 1 Y 1 A LYS 289 ? CE  ? A LYS 261 CE  
26 1 Y 1 A LYS 289 ? NZ  ? A LYS 261 NZ  
27 1 Y 1 A ARG 290 ? CG  ? A ARG 262 CG  
28 1 Y 1 A ARG 290 ? CD  ? A ARG 262 CD  
29 1 Y 1 A ARG 290 ? NE  ? A ARG 262 NE  
30 1 Y 1 A ARG 290 ? CZ  ? A ARG 262 CZ  
31 1 Y 1 A ARG 290 ? NH1 ? A ARG 262 NH1 
32 1 Y 1 A ARG 290 ? NH2 ? A ARG 262 NH2 
33 1 Y 1 A GLN 344 ? CG  ? A GLN 316 CG  
34 1 Y 1 A GLN 344 ? CD  ? A GLN 316 CD  
35 1 Y 1 A GLN 344 ? OE1 ? A GLN 316 OE1 
36 1 Y 1 A GLN 344 ? NE2 ? A GLN 316 NE2 
37 1 Y 1 A LYS 347 ? CG  ? A LYS 319 CG  
38 1 Y 1 A LYS 347 ? CD  ? A LYS 319 CD  
39 1 Y 1 A LYS 347 ? CE  ? A LYS 319 CE  
40 1 Y 1 A LYS 347 ? NZ  ? A LYS 319 NZ  
41 1 Y 1 A LYS 348 ? CG  ? A LYS 320 CG  
42 1 Y 1 A LYS 348 ? CD  ? A LYS 320 CD  
43 1 Y 1 A LYS 348 ? CE  ? A LYS 320 CE  
44 1 Y 1 A LYS 348 ? NZ  ? A LYS 320 NZ  
45 1 Y 1 A LYS 360 ? CG  ? A LYS 332 CG  
46 1 Y 1 A LYS 360 ? CD  ? A LYS 332 CD  
47 1 Y 1 A LYS 360 ? CE  ? A LYS 332 CE  
48 1 Y 1 A LYS 360 ? NZ  ? A LYS 332 NZ  
49 1 Y 1 A GLN 374 ? CG  ? A GLN 346 CG  
50 1 Y 1 A GLN 374 ? CD  ? A GLN 346 CD  
51 1 Y 1 A GLN 374 ? OE1 ? A GLN 346 OE1 
52 1 Y 1 A GLN 374 ? NE2 ? A GLN 346 NE2 
53 1 Y 1 A PHE 428 ? CG  ? A PHE 400 CG  
54 1 Y 1 A PHE 428 ? CD1 ? A PHE 400 CD1 
55 1 Y 1 A PHE 428 ? CD2 ? A PHE 400 CD2 
56 1 Y 1 A PHE 428 ? CE1 ? A PHE 400 CE1 
57 1 Y 1 A PHE 428 ? CE2 ? A PHE 400 CE2 
58 1 Y 1 A PHE 428 ? CZ  ? A PHE 400 CZ  
59 1 Y 1 A ILE 431 ? CG1 ? A ILE 403 CG1 
60 1 Y 1 A ILE 431 ? CG2 ? A ILE 403 CG2 
61 1 Y 1 A ILE 431 ? CD1 ? A ILE 403 CD1 
62 1 Y 1 A GLU 432 ? CG  ? A GLU 404 CG  
63 1 Y 1 A GLU 432 ? CD  ? A GLU 404 CD  
64 1 Y 1 A GLU 432 ? OE1 ? A GLU 404 OE1 
65 1 Y 1 A GLU 432 ? OE2 ? A GLU 404 OE2 
66 1 Y 1 A GLU 435 ? CG  ? A GLU 407 CG  
67 1 Y 1 A GLU 435 ? CD  ? A GLU 407 CD  
68 1 Y 1 A GLU 435 ? OE1 ? A GLU 407 OE1 
69 1 Y 1 A GLU 435 ? OE2 ? A GLU 407 OE2 
70 1 Y 1 A LYS 436 ? CG  ? A LYS 408 CG  
71 1 Y 1 A LYS 436 ? CD  ? A LYS 408 CD  
72 1 Y 1 A LYS 436 ? CE  ? A LYS 408 CE  
73 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                   101.13 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XU9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.718 
_cell.length_a_esd                 ? 
_cell.length_b                     83.810 
_cell.length_b_esd                 ? 
_cell.length_c                     62.201 
_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                         8XU9 
_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                   8XU9 
_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             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.39 
_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         2022-06-20 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.987 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XU9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.217 
_reflns.d_resolution_low                               29.586 
_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                                     19057 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.10 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.94 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.63 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.22 
_reflns_shell.d_res_low                                     2.35 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5739 
_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                                  0.944 
_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                                 8XU9 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.217 
_refine.ls_d_res_low                             29.586 
_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                     19057 
_refine.ls_number_reflns_R_free                  954 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.10 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1706 
_refine.ls_R_factor_R_free                       0.2012 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1689 
_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                          1.36 
_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                 21.12 
_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                       2.217 
_refine_hist.d_res_low                        29.586 
_refine_hist.number_atoms_solvent             173 
_refine_hist.number_atoms_total               3065 
_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        2866 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_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  ? 2970 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.945  ? 4026 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.875 ? 1754 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053  ? 439  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 526  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.2170 2.3338 . . 132 2506 97.00  . . . . 0.1807 . . . . . . . . . . . 0.2220 
'X-RAY DIFFRACTION' 2.3338 2.4799 . . 138 2610 99.00  . . . . 0.1948 . . . . . . . . . . . 0.2729 
'X-RAY DIFFRACTION' 2.4799 2.6713 . . 134 2558 100.00 . . . . 0.1837 . . . . . . . . . . . 0.2536 
'X-RAY DIFFRACTION' 2.6713 2.9399 . . 137 2588 100.00 . . . . 0.1845 . . . . . . . . . . . 0.2254 
'X-RAY DIFFRACTION' 2.9399 3.3648 . . 137 2600 100.00 . . . . 0.1719 . . . . . . . . . . . 0.2004 
'X-RAY DIFFRACTION' 3.3648 4.2373 . . 136 2597 99.00  . . . . 0.1494 . . . . . . . . . . . 0.1524 
'X-RAY DIFFRACTION' 4.2373 8      . . 140 2644 99.00  . . . . 0.1605 . . . . . . . . . . . 0.1902 
# 
_struct.entry_id                     8XU9 
_struct.title                        'Crystal structure of AtHPPD-YH20531 complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8XU9 
_struct_keywords.text            'Complex, Inhibitor, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HPPD_ARATH 
_struct_ref.pdbx_db_accession          P93836 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VRKNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVHASYLLTSGDLRFLFTAPYSPSLSAGEI
KPTTTASIPSFDHGSCRSFFSSHGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDVVLRYVSY
KAEDTEKSEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVAGFTGFHQFAEFTADDVGTAESGLNSAVLAS
NDEMVLLPINEPVHGTKRKSQIQTYLEHNEGAGLQHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKKRVGD
VLSDDQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGCMMKDEEGKAYQSGGCGGFGKGNFSELFKSIE
EYEKTLEAKQLVG
;
_struct_ref.pdbx_align_begin           33 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8XU9 
_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 8XU9 GLY A 1 ? UNP P93836 ? ? 'expression tag' 29 1 
1 8XU9 SER A 2 ? UNP P93836 ? ? 'expression tag' 30 2 
1 8XU9 HIS A 3 ? UNP P93836 ? ? 'expression tag' 31 3 
1 8XU9 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)' 3550  ? 
1 MORE         -35   ? 
1 'SSA (A^2)'  28210 ? 
# 
_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 -24.0140325939 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 122.0622130005 
# 
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 182 ? SER A 186 ? GLU A 210 SER A 214 5 ? 5  
HELX_P HELX_P8  AA8 GLU A 205 ? GLY A 218 ? GLU A 233 GLY A 246 1 ? 14 
HELX_P HELX_P9  AA9 SER A 264 ? GLU A 274 ? SER A 292 GLU A 302 1 ? 11 
HELX_P HELX_P10 AB1 ASP A 287 ? ARG A 298 ? ASP A 315 ARG A 326 1 ? 12 
HELX_P HELX_P11 AB2 PRO A 311 ? ASN A 317 ? PRO A 339 ASN A 345 1 ? 7  
HELX_P HELX_P12 AB3 LEU A 318 ? GLY A 323 ? LEU A 346 GLY A 351 1 ? 6  
HELX_P HELX_P13 AB4 SER A 327 ? GLY A 338 ? SER A 355 GLY A 366 1 ? 12 
HELX_P HELX_P14 AB5 LYS A 393 ? LYS A 408 ? LYS A 421 LYS A 436 1 ? 16 
# 
_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 ? ? ? ? ? ? ? 2.026 ? ? 
metalc1 metalc ? ? A HIS 198 NE2 ? ? ? 1_555 B CO    .   CO  ? ? A HIS 226 A CO    501 1_555 ? ? ? ? ? ? ? 2.366 ? ? 
metalc2 metalc ? ? A HIS 280 NE2 ? ? ? 1_555 B CO    .   CO  ? ? A HIS 308 A CO    501 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
metalc3 metalc ? ? A GLU 366 OE1 ? ? ? 1_555 B CO    .   CO  ? ? A GLU 394 A CO    501 1_555 ? ? ? ? ? ? ? 2.186 ? ? 
metalc4 metalc ? ? B CO  .   CO  ? ? ? 1_555 C A1LW4 .   O08 ? ? A CO  501 A A1LW4 502 1_555 ? ? ? ? ? ? ? 2.161 ? ? 
metalc5 metalc ? ? B CO  .   CO  ? ? ? 1_555 C A1LW4 .   N11 ? ? A CO  501 A A1LW4 502 1_555 ? ? ? ? ? ? ? 2.311 ? ? 
metalc6 metalc ? ? B CO  .   CO  ? ? ? 1_555 D HOH   .   O   ? ? A CO  501 A HOH   636 1_555 ? ? ? ? ? ? ? 2.368 ? ? 
# 
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 99.3  ? 
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 96.5  ? 
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 83.6  ? 
4  NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O08 ? C A1LW4 .   ? A A1LW4 502 ? 1_555 166.4 ? 
5  NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O08 ? C A1LW4 .   ? A A1LW4 502 ? 1_555 93.9  ? 
6  OE1 ? A GLU   366 ? A GLU   394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O08 ? C A1LW4 .   ? A A1LW4 502 ? 1_555 88.2  ? 
7  NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 N11 ? C A1LW4 .   ? A A1LW4 502 ? 1_555 95.6  ? 
8  NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 N11 ? C A1LW4 .   ? A A1LW4 502 ? 1_555 99.5  ? 
9  OE1 ? A GLU   366 ? A GLU   394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 N11 ? C A1LW4 .   ? A A1LW4 502 ? 1_555 166.9 ? 
10 O08 ? C A1LW4 .   ? A A1LW4 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 N11 ? C A1LW4 .   ? A A1LW4 502 ? 1_555 78.9  ? 
11 NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   636 ? 1_555 88.9  ? 
12 NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   636 ? 1_555 169.2 ? 
13 OE1 ? A GLU   366 ? A GLU   394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   636 ? 1_555 88.5  ? 
14 O08 ? C A1LW4 .   ? A A1LW4 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   636 ? 1_555 78.5  ? 
15 N11 ? C A1LW4 .   ? A A1LW4 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   636 ? 1_555 86.6  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       373 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      388 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       416 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA1 8 9 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PRO A 135 ? LEU A 142 ? PRO A 163 LEU A 170 
AA1 2 VAL A 146 ? TYR A 154 ? VAL A 174 TYR A 182 
AA1 3 VAL A 157 ? TYR A 164 ? VAL A 185 TYR A 192 
AA1 4 GLY A 110 ? VAL A 118 ? GLY A 138 VAL A 146 
AA1 5 VAL A 16  ? TRP A 25  ? VAL A 44  TRP A 53  
AA1 6 LEU A 67  ? PRO A 74  ? LEU A 95  PRO A 102 
AA1 7 HIS A 57  ? SER A 64  ? HIS A 85  SER A 92  
AA1 8 ARG A 43  ? SER A 48  ? ARG A 71  SER A 76  
AA1 9 GLU A 179 ? ARG A 180 ? GLU A 207 ARG A 208 
AA2 1 HIS A 220 ? GLN A 221 ? HIS A 248 GLN A 249 
AA2 2 LEU A 237 ? ALA A 243 ? LEU A 265 ALA A 271 
AA2 3 LEU A 250 ? PRO A 256 ? LEU A 278 PRO A 284 
AA2 4 ILE A 193 ? ASN A 202 ? ILE A 221 ASN A 230 
AA2 5 GLY A 277 ? SER A 285 ? GLY A 305 SER A 313 
AA2 6 PHE A 364 ? GLY A 372 ? PHE A 392 GLY A 400 
AA2 7 GLY A 347 ? PHE A 353 ? GLY A 375 PHE A 381 
AA2 8 LEU A 340 ? ARG A 343 ? LEU A 368 ARG A 371 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 142 ? N LEU A 170 O VAL A 146 ? O VAL A 174 
AA1 2 3 N ALA A 149 ? N ALA A 177 O TYR A 161 ? O TYR A 189 
AA1 3 4 O VAL A 162 ? O VAL A 190 N VAL A 118 ? N VAL A 146 
AA1 4 5 O GLU A 117 ? O GLU A 145 N 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 SER A 59  ? O SER A 87  N SER A 48  ? N SER A 76  
AA1 8 9 N LYS A 47  ? N LYS A 75  O GLU A 179 ? O GLU A 207 
AA2 1 2 N HIS A 220 ? N HIS A 248 O ALA A 243 ? O ALA A 271 
AA2 2 3 N LEU A 242 ? N LEU A 270 O LEU A 251 ? O LEU A 279 
AA2 3 4 O ASN A 254 ? O ASN A 282 N GLY A 201 ? N GLY A 229 
AA2 4 5 N 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 VAL A 371 ? O VAL A 399 N THR A 348 ? N THR A 376 
AA2 7 8 O GLN A 351 ? O GLN A 379 N LEU A 340 ? N LEU A 368 
# 
_pdbx_entry_details.entry_id                   8XU9 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 45  ? ? -96.02  -84.11  
2 1 GLU A 172 ? ? 54.60   19.31   
3 1 LEU A 181 ? ? -104.07 -61.37  
4 1 ASP A 218 ? ? -167.32 113.74  
5 1 THR A 288 ? ? -119.22 -134.32 
6 1 ASP A 315 ? ? -166.33 83.45   
7 1 THR A 390 ? ? -120.30 -92.05  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     687 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 GLU 201 ? A GLU 173 
14 1 Y 1 A GLU 252 ? A GLU 224 
15 1 Y 1 A PHE 253 ? A PHE 225 
16 1 Y 1 A THR 254 ? A THR 226 
17 1 Y 1 A ALA 255 ? A ALA 227 
18 1 Y 1 A ASP 256 ? A ASP 228 
19 1 Y 1 A ASP 257 ? A ASP 229 
20 1 Y 1 A VAL 258 ? A VAL 230 
21 1 Y 1 A GLY 259 ? A GLY 231 
22 1 Y 1 A THR 260 ? A THR 232 
23 1 Y 1 A ALA 261 ? A ALA 233 
24 1 Y 1 A LYS 404 ? A LYS 376 
25 1 Y 1 A ASP 405 ? A ASP 377 
26 1 Y 1 A GLU 406 ? A GLU 378 
27 1 Y 1 A GLU 407 ? A GLU 379 
28 1 Y 1 A GLY 408 ? A GLY 380 
29 1 Y 1 A LYS 409 ? A LYS 381 
30 1 Y 1 A ALA 410 ? A ALA 382 
31 1 Y 1 A THR 437 ? A THR 409 
32 1 Y 1 A LEU 438 ? A LEU 410 
33 1 Y 1 A GLU 439 ? A GLU 411 
34 1 Y 1 A ALA 440 ? A ALA 412 
35 1 Y 1 A LYS 441 ? A LYS 413 
36 1 Y 1 A GLN 442 ? A GLN 414 
37 1 Y 1 A LEU 443 ? A LEU 415 
38 1 Y 1 A VAL 444 ? A VAL 416 
39 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 
A1LW4 C10  C  Y N 1   
A1LW4 N12  N  Y N 2   
A1LW4 C13  C  Y N 3   
A1LW4 C15  C  N N 4   
A1LW4 C20  C  N N 5   
A1LW4 C21  C  N N 6   
A1LW4 C22  C  N N 7   
A1LW4 C01  C  Y N 8   
A1LW4 C02  C  Y N 9   
A1LW4 C03  C  Y N 10  
A1LW4 C04  C  Y N 11  
A1LW4 C05  C  Y N 12  
A1LW4 C06  C  Y N 13  
A1LW4 C07  C  N N 14  
A1LW4 O08  O  N N 15  
A1LW4 N09  N  N N 16  
A1LW4 N11  N  Y N 17  
A1LW4 O14  O  Y N 18  
A1LW4 F16  F  N N 19  
A1LW4 S17  S  N R 20  
A1LW4 O18  O  N N 21  
A1LW4 C19  C  N N 22  
A1LW4 F23  F  N N 23  
A1LW4 F24  F  N N 24  
A1LW4 F25  F  N N 25  
A1LW4 H1   H  N N 26  
A1LW4 H2   H  N N 27  
A1LW4 H3   H  N N 28  
A1LW4 H4   H  N N 29  
A1LW4 H5   H  N N 30  
A1LW4 H6   H  N N 31  
A1LW4 H7   H  N N 32  
A1LW4 H8   H  N N 33  
A1LW4 H9   H  N N 34  
A1LW4 H10  H  N N 35  
A1LW4 H11  H  N N 36  
A1LW4 H12  H  N N 37  
A1LW4 H13  H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CO    CO   CO N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
GLN   N    N  N N 127 
GLN   CA   C  N S 128 
GLN   C    C  N N 129 
GLN   O    O  N N 130 
GLN   CB   C  N N 131 
GLN   CG   C  N N 132 
GLN   CD   C  N N 133 
GLN   OE1  O  N N 134 
GLN   NE2  N  N N 135 
GLN   OXT  O  N N 136 
GLN   H    H  N N 137 
GLN   H2   H  N N 138 
GLN   HA   H  N N 139 
GLN   HB2  H  N N 140 
GLN   HB3  H  N N 141 
GLN   HG2  H  N N 142 
GLN   HG3  H  N N 143 
GLN   HE21 H  N N 144 
GLN   HE22 H  N N 145 
GLN   HXT  H  N N 146 
GLU   N    N  N N 147 
GLU   CA   C  N S 148 
GLU   C    C  N N 149 
GLU   O    O  N N 150 
GLU   CB   C  N N 151 
GLU   CG   C  N N 152 
GLU   CD   C  N N 153 
GLU   OE1  O  N N 154 
GLU   OE2  O  N N 155 
GLU   OXT  O  N N 156 
GLU   H    H  N N 157 
GLU   H2   H  N N 158 
GLU   HA   H  N N 159 
GLU   HB2  H  N N 160 
GLU   HB3  H  N N 161 
GLU   HG2  H  N N 162 
GLU   HG3  H  N N 163 
GLU   HE2  H  N N 164 
GLU   HXT  H  N N 165 
GLY   N    N  N N 166 
GLY   CA   C  N N 167 
GLY   C    C  N N 168 
GLY   O    O  N N 169 
GLY   OXT  O  N N 170 
GLY   H    H  N N 171 
GLY   H2   H  N N 172 
GLY   HA2  H  N N 173 
GLY   HA3  H  N N 174 
GLY   HXT  H  N N 175 
HIS   N    N  N N 176 
HIS   CA   C  N S 177 
HIS   C    C  N N 178 
HIS   O    O  N N 179 
HIS   CB   C  N N 180 
HIS   CG   C  Y N 181 
HIS   ND1  N  Y N 182 
HIS   CD2  C  Y N 183 
HIS   CE1  C  Y N 184 
HIS   NE2  N  Y N 185 
HIS   OXT  O  N N 186 
HIS   H    H  N N 187 
HIS   H2   H  N N 188 
HIS   HA   H  N N 189 
HIS   HB2  H  N N 190 
HIS   HB3  H  N N 191 
HIS   HD1  H  N N 192 
HIS   HD2  H  N N 193 
HIS   HE1  H  N N 194 
HIS   HE2  H  N N 195 
HIS   HXT  H  N N 196 
HOH   O    O  N N 197 
HOH   H1   H  N N 198 
HOH   H2   H  N N 199 
ILE   N    N  N N 200 
ILE   CA   C  N S 201 
ILE   C    C  N N 202 
ILE   O    O  N N 203 
ILE   CB   C  N S 204 
ILE   CG1  C  N N 205 
ILE   CG2  C  N N 206 
ILE   CD1  C  N N 207 
ILE   OXT  O  N N 208 
ILE   H    H  N N 209 
ILE   H2   H  N N 210 
ILE   HA   H  N N 211 
ILE   HB   H  N N 212 
ILE   HG12 H  N N 213 
ILE   HG13 H  N N 214 
ILE   HG21 H  N N 215 
ILE   HG22 H  N N 216 
ILE   HG23 H  N N 217 
ILE   HD11 H  N N 218 
ILE   HD12 H  N N 219 
ILE   HD13 H  N N 220 
ILE   HXT  H  N N 221 
LEU   N    N  N N 222 
LEU   CA   C  N S 223 
LEU   C    C  N N 224 
LEU   O    O  N N 225 
LEU   CB   C  N N 226 
LEU   CG   C  N N 227 
LEU   CD1  C  N N 228 
LEU   CD2  C  N N 229 
LEU   OXT  O  N N 230 
LEU   H    H  N N 231 
LEU   H2   H  N N 232 
LEU   HA   H  N N 233 
LEU   HB2  H  N N 234 
LEU   HB3  H  N N 235 
LEU   HG   H  N N 236 
LEU   HD11 H  N N 237 
LEU   HD12 H  N N 238 
LEU   HD13 H  N N 239 
LEU   HD21 H  N N 240 
LEU   HD22 H  N N 241 
LEU   HD23 H  N N 242 
LEU   HXT  H  N N 243 
LYS   N    N  N N 244 
LYS   CA   C  N S 245 
LYS   C    C  N N 246 
LYS   O    O  N N 247 
LYS   CB   C  N N 248 
LYS   CG   C  N N 249 
LYS   CD   C  N N 250 
LYS   CE   C  N N 251 
LYS   NZ   N  N N 252 
LYS   OXT  O  N N 253 
LYS   H    H  N N 254 
LYS   H2   H  N N 255 
LYS   HA   H  N N 256 
LYS   HB2  H  N N 257 
LYS   HB3  H  N N 258 
LYS   HG2  H  N N 259 
LYS   HG3  H  N N 260 
LYS   HD2  H  N N 261 
LYS   HD3  H  N N 262 
LYS   HE2  H  N N 263 
LYS   HE3  H  N N 264 
LYS   HZ1  H  N N 265 
LYS   HZ2  H  N N 266 
LYS   HZ3  H  N N 267 
LYS   HXT  H  N N 268 
MET   N    N  N N 269 
MET   CA   C  N S 270 
MET   C    C  N N 271 
MET   O    O  N N 272 
MET   CB   C  N N 273 
MET   CG   C  N N 274 
MET   SD   S  N N 275 
MET   CE   C  N N 276 
MET   OXT  O  N N 277 
MET   H    H  N N 278 
MET   H2   H  N N 279 
MET   HA   H  N N 280 
MET   HB2  H  N N 281 
MET   HB3  H  N N 282 
MET   HG2  H  N N 283 
MET   HG3  H  N N 284 
MET   HE1  H  N N 285 
MET   HE2  H  N N 286 
MET   HE3  H  N N 287 
MET   HXT  H  N N 288 
PHE   N    N  N N 289 
PHE   CA   C  N S 290 
PHE   C    C  N N 291 
PHE   O    O  N N 292 
PHE   CB   C  N N 293 
PHE   CG   C  Y N 294 
PHE   CD1  C  Y N 295 
PHE   CD2  C  Y N 296 
PHE   CE1  C  Y N 297 
PHE   CE2  C  Y N 298 
PHE   CZ   C  Y N 299 
PHE   OXT  O  N N 300 
PHE   H    H  N N 301 
PHE   H2   H  N N 302 
PHE   HA   H  N N 303 
PHE   HB2  H  N N 304 
PHE   HB3  H  N N 305 
PHE   HD1  H  N N 306 
PHE   HD2  H  N N 307 
PHE   HE1  H  N N 308 
PHE   HE2  H  N N 309 
PHE   HZ   H  N N 310 
PHE   HXT  H  N N 311 
PRO   N    N  N N 312 
PRO   CA   C  N S 313 
PRO   C    C  N N 314 
PRO   O    O  N N 315 
PRO   CB   C  N N 316 
PRO   CG   C  N N 317 
PRO   CD   C  N N 318 
PRO   OXT  O  N N 319 
PRO   H    H  N N 320 
PRO   HA   H  N N 321 
PRO   HB2  H  N N 322 
PRO   HB3  H  N N 323 
PRO   HG2  H  N N 324 
PRO   HG3  H  N N 325 
PRO   HD2  H  N N 326 
PRO   HD3  H  N N 327 
PRO   HXT  H  N N 328 
SER   N    N  N N 329 
SER   CA   C  N S 330 
SER   C    C  N N 331 
SER   O    O  N N 332 
SER   CB   C  N N 333 
SER   OG   O  N N 334 
SER   OXT  O  N N 335 
SER   H    H  N N 336 
SER   H2   H  N N 337 
SER   HA   H  N N 338 
SER   HB2  H  N N 339 
SER   HB3  H  N N 340 
SER   HG   H  N N 341 
SER   HXT  H  N N 342 
THR   N    N  N N 343 
THR   CA   C  N S 344 
THR   C    C  N N 345 
THR   O    O  N N 346 
THR   CB   C  N R 347 
THR   OG1  O  N N 348 
THR   CG2  C  N N 349 
THR   OXT  O  N N 350 
THR   H    H  N N 351 
THR   H2   H  N N 352 
THR   HA   H  N N 353 
THR   HB   H  N N 354 
THR   HG1  H  N N 355 
THR   HG21 H  N N 356 
THR   HG22 H  N N 357 
THR   HG23 H  N N 358 
THR   HXT  H  N N 359 
TRP   N    N  N N 360 
TRP   CA   C  N S 361 
TRP   C    C  N N 362 
TRP   O    O  N N 363 
TRP   CB   C  N N 364 
TRP   CG   C  Y N 365 
TRP   CD1  C  Y N 366 
TRP   CD2  C  Y N 367 
TRP   NE1  N  Y N 368 
TRP   CE2  C  Y N 369 
TRP   CE3  C  Y N 370 
TRP   CZ2  C  Y N 371 
TRP   CZ3  C  Y N 372 
TRP   CH2  C  Y N 373 
TRP   OXT  O  N N 374 
TRP   H    H  N N 375 
TRP   H2   H  N N 376 
TRP   HA   H  N N 377 
TRP   HB2  H  N N 378 
TRP   HB3  H  N N 379 
TRP   HD1  H  N N 380 
TRP   HE1  H  N N 381 
TRP   HE3  H  N N 382 
TRP   HZ2  H  N N 383 
TRP   HZ3  H  N N 384 
TRP   HH2  H  N N 385 
TRP   HXT  H  N N 386 
TYR   N    N  N N 387 
TYR   CA   C  N S 388 
TYR   C    C  N N 389 
TYR   O    O  N N 390 
TYR   CB   C  N N 391 
TYR   CG   C  Y N 392 
TYR   CD1  C  Y N 393 
TYR   CD2  C  Y N 394 
TYR   CE1  C  Y N 395 
TYR   CE2  C  Y N 396 
TYR   CZ   C  Y N 397 
TYR   OH   O  N N 398 
TYR   OXT  O  N N 399 
TYR   H    H  N N 400 
TYR   H2   H  N N 401 
TYR   HA   H  N N 402 
TYR   HB2  H  N N 403 
TYR   HB3  H  N N 404 
TYR   HD1  H  N N 405 
TYR   HD2  H  N N 406 
TYR   HE1  H  N N 407 
TYR   HE2  H  N N 408 
TYR   HH   H  N N 409 
TYR   HXT  H  N N 410 
VAL   N    N  N N 411 
VAL   CA   C  N S 412 
VAL   C    C  N N 413 
VAL   O    O  N N 414 
VAL   CB   C  N N 415 
VAL   CG1  C  N N 416 
VAL   CG2  C  N N 417 
VAL   OXT  O  N N 418 
VAL   H    H  N N 419 
VAL   H2   H  N N 420 
VAL   HA   H  N N 421 
VAL   HB   H  N N 422 
VAL   HG11 H  N N 423 
VAL   HG12 H  N N 424 
VAL   HG13 H  N N 425 
VAL   HG21 H  N N 426 
VAL   HG22 H  N N 427 
VAL   HG23 H  N N 428 
VAL   HXT  H  N N 429 
# 
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 
A1LW4 N12 N11  sing Y N 1   
A1LW4 N12 C13  doub Y N 2   
A1LW4 N11 C10  doub Y N 3   
A1LW4 O08 C07  doub N N 4   
A1LW4 C20 C19  sing N N 5   
A1LW4 C20 C21  sing N N 6   
A1LW4 F16 C06  sing N N 7   
A1LW4 C13 C15  sing N N 8   
A1LW4 C13 O14  sing Y N 9   
A1LW4 C07 N09  sing N N 10  
A1LW4 C07 C01  sing N N 11  
A1LW4 C10 N09  sing N N 12  
A1LW4 C10 O14  sing Y N 13  
A1LW4 C19 S17  sing N N 14  
A1LW4 C06 C01  doub Y N 15  
A1LW4 C06 C05  sing Y N 16  
A1LW4 C01 C02  sing Y N 17  
A1LW4 S17 C05  sing N N 18  
A1LW4 S17 O18  doub N N 19  
A1LW4 C05 C04  doub Y N 20  
A1LW4 C02 C03  doub Y N 21  
A1LW4 C04 C03  sing Y N 22  
A1LW4 C04 C22  sing N N 23  
A1LW4 F24 C22  sing N N 24  
A1LW4 C22 F25  sing N N 25  
A1LW4 C22 F23  sing N N 26  
A1LW4 C15 H1   sing N N 27  
A1LW4 C15 H2   sing N N 28  
A1LW4 C15 H3   sing N N 29  
A1LW4 C20 H4   sing N N 30  
A1LW4 C20 H5   sing N N 31  
A1LW4 C21 H6   sing N N 32  
A1LW4 C21 H7   sing N N 33  
A1LW4 C21 H8   sing N N 34  
A1LW4 C02 H9   sing N N 35  
A1LW4 C03 H10  sing N N 36  
A1LW4 N09 H11  sing N N 37  
A1LW4 C19 H12  sing N N 38  
A1LW4 C19 H13  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
THR   N   CA   sing N N 329 
THR   N   H    sing N N 330 
THR   N   H2   sing N N 331 
THR   CA  C    sing N N 332 
THR   CA  CB   sing N N 333 
THR   CA  HA   sing N N 334 
THR   C   O    doub N N 335 
THR   C   OXT  sing N N 336 
THR   CB  OG1  sing N N 337 
THR   CB  CG2  sing N N 338 
THR   CB  HB   sing N N 339 
THR   OG1 HG1  sing N N 340 
THR   CG2 HG21 sing N N 341 
THR   CG2 HG22 sing N N 342 
THR   CG2 HG23 sing N N 343 
THR   OXT HXT  sing N N 344 
TRP   N   CA   sing N N 345 
TRP   N   H    sing N N 346 
TRP   N   H2   sing N N 347 
TRP   CA  C    sing N N 348 
TRP   CA  CB   sing N N 349 
TRP   CA  HA   sing N N 350 
TRP   C   O    doub N N 351 
TRP   C   OXT  sing N N 352 
TRP   CB  CG   sing N N 353 
TRP   CB  HB2  sing N N 354 
TRP   CB  HB3  sing N N 355 
TRP   CG  CD1  doub Y N 356 
TRP   CG  CD2  sing Y N 357 
TRP   CD1 NE1  sing Y N 358 
TRP   CD1 HD1  sing N N 359 
TRP   CD2 CE2  doub Y N 360 
TRP   CD2 CE3  sing Y N 361 
TRP   NE1 CE2  sing Y N 362 
TRP   NE1 HE1  sing N N 363 
TRP   CE2 CZ2  sing Y N 364 
TRP   CE3 CZ3  doub Y N 365 
TRP   CE3 HE3  sing N N 366 
TRP   CZ2 CH2  doub Y N 367 
TRP   CZ2 HZ2  sing N N 368 
TRP   CZ3 CH2  sing Y N 369 
TRP   CZ3 HZ3  sing N N 370 
TRP   CH2 HH2  sing N N 371 
TRP   OXT HXT  sing N N 372 
TYR   N   CA   sing N N 373 
TYR   N   H    sing N N 374 
TYR   N   H2   sing N N 375 
TYR   CA  C    sing N N 376 
TYR   CA  CB   sing N N 377 
TYR   CA  HA   sing N N 378 
TYR   C   O    doub N N 379 
TYR   C   OXT  sing N N 380 
TYR   CB  CG   sing N N 381 
TYR   CB  HB2  sing N N 382 
TYR   CB  HB3  sing N N 383 
TYR   CG  CD1  doub Y N 384 
TYR   CG  CD2  sing Y N 385 
TYR   CD1 CE1  sing Y N 386 
TYR   CD1 HD1  sing N N 387 
TYR   CD2 CE2  doub Y N 388 
TYR   CD2 HD2  sing N N 389 
TYR   CE1 CZ   doub Y N 390 
TYR   CE1 HE1  sing N N 391 
TYR   CE2 CZ   sing Y N 392 
TYR   CE2 HE2  sing N N 393 
TYR   CZ  OH   sing N N 394 
TYR   OH  HH   sing N N 395 
TYR   OXT HXT  sing N N 396 
VAL   N   CA   sing N N 397 
VAL   N   H    sing N N 398 
VAL   N   H2   sing N N 399 
VAL   CA  C    sing N N 400 
VAL   CA  CB   sing N N 401 
VAL   CA  HA   sing N N 402 
VAL   C   O    doub N N 403 
VAL   C   OXT  sing N N 404 
VAL   CB  CG1  sing N N 405 
VAL   CB  CG2  sing N N 406 
VAL   CB  HB   sing N N 407 
VAL   CG1 HG11 sing N N 408 
VAL   CG1 HG12 sing N N 409 
VAL   CG1 HG13 sing N N 410 
VAL   CG2 HG21 sing N N 411 
VAL   CG2 HG22 sing N N 412 
VAL   CG2 HG23 sing N N 413 
VAL   OXT HXT  sing N N 414 
# 
_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                    8XU9 
_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]   0.013035 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002564 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011932 
_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]   0.016385 
_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   ? 22.263  -5.573  87.076  1.00 50.45 ? 35  LYS   A N   1 
ATOM   2    C  CA  . LYS   A 1 7   ? 23.356  -6.190  86.330  1.00 48.84 ? 35  LYS   A CA  1 
ATOM   3    C  C   . LYS   A 1 7   ? 22.883  -6.717  84.967  1.00 52.73 ? 35  LYS   A C   1 
ATOM   4    O  O   . LYS   A 1 7   ? 21.784  -7.269  84.843  1.00 52.20 ? 35  LYS   A O   1 
ATOM   5    C  CB  . LYS   A 1 7   ? 23.990  -7.322  87.148  1.00 52.13 ? 35  LYS   A CB  1 
ATOM   6    N  N   . ASN   A 1 8   ? 23.727  -6.542  83.952  1.00 49.80 ? 36  ASN   A N   1 
ATOM   7    C  CA  . ASN   A 1 8   ? 23.432  -6.953  82.580  1.00 43.93 ? 36  ASN   A CA  1 
ATOM   8    C  C   . ASN   A 1 8   ? 24.573  -7.844  82.105  1.00 40.75 ? 36  ASN   A C   1 
ATOM   9    O  O   . ASN   A 1 8   ? 25.614  -7.334  81.655  1.00 43.59 ? 36  ASN   A O   1 
ATOM   10   C  CB  . ASN   A 1 8   ? 23.254  -5.737  81.670  1.00 42.20 ? 36  ASN   A CB  1 
ATOM   11   C  CG  . ASN   A 1 8   ? 23.079  -6.107  80.193  1.00 41.99 ? 36  ASN   A CG  1 
ATOM   12   O  OD1 . ASN   A 1 8   ? 22.966  -7.282  79.839  1.00 38.43 ? 36  ASN   A OD1 1 
ATOM   13   N  ND2 . ASN   A 1 8   ? 23.041  -5.093  79.327  1.00 35.51 ? 36  ASN   A ND2 1 
ATOM   14   N  N   . PRO   A 1 9   ? 24.407  -9.171  82.159  1.00 40.07 ? 37  PRO   A N   1 
ATOM   15   C  CA  . PRO   A 1 9   ? 25.498  -10.075 81.759  1.00 35.09 ? 37  PRO   A CA  1 
ATOM   16   C  C   . PRO   A 1 9   ? 25.768  -10.101 80.269  1.00 37.46 ? 37  PRO   A C   1 
ATOM   17   O  O   . PRO   A 1 9   ? 26.754  -10.730 79.860  1.00 36.77 ? 37  PRO   A O   1 
ATOM   18   C  CB  . PRO   A 1 9   ? 25.011  -11.443 82.240  1.00 31.69 ? 37  PRO   A CB  1 
ATOM   19   C  CG  . PRO   A 1 9   ? 23.517  -11.323 82.187  1.00 38.05 ? 37  PRO   A CG  1 
ATOM   20   C  CD  . PRO   A 1 9   ? 23.197  -9.904  82.568  1.00 39.70 ? 37  PRO   A CD  1 
ATOM   21   N  N   . LYS   A 1 10  ? 24.919  -9.473  79.454  1.00 38.47 ? 38  LYS   A N   1 
ATOM   22   C  CA  . LYS   A 1 10  ? 25.082  -9.397  78.003  1.00 34.55 ? 38  LYS   A CA  1 
ATOM   23   C  C   . LYS   A 1 10  ? 25.359  -10.773 77.391  1.00 31.51 ? 38  LYS   A C   1 
ATOM   24   O  O   . LYS   A 1 10  ? 26.343  -10.994 76.683  1.00 33.97 ? 38  LYS   A O   1 
ATOM   25   C  CB  . LYS   A 1 10  ? 26.176  -8.396  77.633  1.00 36.38 ? 38  LYS   A CB  1 
ATOM   26   C  CG  . LYS   A 1 10  ? 25.873  -6.970  78.092  1.00 43.02 ? 38  LYS   A CG  1 
ATOM   27   C  CD  . LYS   A 1 10  ? 26.623  -5.946  77.252  1.00 43.94 ? 38  LYS   A CD  1 
ATOM   28   C  CE  . LYS   A 1 10  ? 25.918  -4.590  77.268  1.00 46.42 ? 38  LYS   A CE  1 
ATOM   29   N  NZ  . LYS   A 1 10  ? 26.719  -3.550  77.961  1.00 49.73 ? 38  LYS   A NZ  1 
ATOM   30   N  N   . SER   A 1 11  ? 24.436  -11.696 77.641  1.00 33.27 ? 39  SER   A N   1 
ATOM   31   C  CA  . SER   A 1 11  ? 24.610  -13.085 77.246  1.00 29.47 ? 39  SER   A CA  1 
ATOM   32   C  C   . SER   A 1 11  ? 23.813  -13.469 76.007  1.00 30.15 ? 39  SER   A C   1 
ATOM   33   O  O   . SER   A 1 11  ? 23.570  -14.662 75.796  1.00 27.30 ? 39  SER   A O   1 
ATOM   34   C  CB  . SER   A 1 11  ? 24.240  -13.997 78.406  1.00 26.93 ? 39  SER   A CB  1 
ATOM   35   O  OG  . SER   A 1 11  ? 23.041  -13.570 79.002  1.00 30.14 ? 39  SER   A OG  1 
ATOM   36   N  N   . ASP   A 1 12  ? 23.409  -12.499 75.176  1.00 28.69 ? 40  ASP   A N   1 
ATOM   37   C  CA  . ASP   A 1 12  ? 22.754  -12.831 73.907  1.00 28.88 ? 40  ASP   A CA  1 
ATOM   38   C  C   . ASP   A 1 12  ? 23.573  -13.878 73.160  1.00 29.77 ? 40  ASP   A C   1 
ATOM   39   O  O   . ASP   A 1 12  ? 24.789  -13.743 73.014  1.00 28.39 ? 40  ASP   A O   1 
ATOM   40   C  CB  . ASP   A 1 12  ? 22.590  -11.586 73.030  1.00 25.35 ? 40  ASP   A CB  1 
ATOM   41   C  CG  . ASP   A 1 12  ? 21.442  -10.679 73.478  1.00 26.95 ? 40  ASP   A CG  1 
ATOM   42   O  OD1 . ASP   A 1 12  ? 20.804  -10.949 74.524  1.00 25.23 ? 40  ASP   A OD1 1 
ATOM   43   O  OD2 . ASP   A 1 12  ? 21.218  -9.661  72.790  1.00 26.36 ? 40  ASP   A OD2 1 
ATOM   44   N  N   . LYS   A 1 13  ? 22.910  -14.941 72.724  1.00 23.66 ? 41  LYS   A N   1 
ATOM   45   C  CA  . LYS   A 1 13  ? 23.593  -15.998 71.998  1.00 31.39 ? 41  LYS   A CA  1 
ATOM   46   C  C   . LYS   A 1 13  ? 23.710  -15.686 70.518  1.00 30.19 ? 41  LYS   A C   1 
ATOM   47   O  O   . LYS   A 1 13  ? 24.411  -16.408 69.801  1.00 34.64 ? 41  LYS   A O   1 
ATOM   48   C  CB  . LYS   A 1 13  ? 22.873  -17.336 72.210  1.00 26.63 ? 41  LYS   A CB  1 
ATOM   49   C  CG  . LYS   A 1 13  ? 22.820  -17.748 73.676  1.00 26.16 ? 41  LYS   A CG  1 
ATOM   50   C  CD  . LYS   A 1 13  ? 22.103  -19.073 73.878  1.00 30.85 ? 41  LYS   A CD  1 
ATOM   51   C  CE  . LYS   A 1 13  ? 22.836  -19.936 74.908  1.00 31.32 ? 41  LYS   A CE  1 
ATOM   52   N  NZ  . LYS   A 1 13  ? 21.959  -20.382 76.021  1.00 31.47 ? 41  LYS   A NZ  1 
ATOM   53   N  N   . PHE   A 1 14  ? 23.051  -14.627 70.055  1.00 26.38 ? 42  PHE   A N   1 
ATOM   54   C  CA  . PHE   A 1 14  ? 23.207  -14.133 68.698  1.00 22.15 ? 42  PHE   A CA  1 
ATOM   55   C  C   . PHE   A 1 14  ? 22.993  -12.632 68.732  1.00 24.00 ? 42  PHE   A C   1 
ATOM   56   O  O   . PHE   A 1 14  ? 22.418  -12.091 69.679  1.00 29.26 ? 42  PHE   A O   1 
ATOM   57   C  CB  . PHE   A 1 14  ? 22.232  -14.806 67.716  1.00 27.45 ? 42  PHE   A CB  1 
ATOM   58   C  CG  . PHE   A 1 14  ? 20.871  -15.095 68.299  1.00 24.18 ? 42  PHE   A CG  1 
ATOM   59   C  CD1 . PHE   A 1 14  ? 19.846  -14.161 68.208  1.00 26.55 ? 42  PHE   A CD1 1 
ATOM   60   C  CD2 . PHE   A 1 14  ? 20.613  -16.307 68.925  1.00 25.07 ? 42  PHE   A CD2 1 
ATOM   61   C  CE1 . PHE   A 1 14  ? 18.583  -14.426 68.754  1.00 24.96 ? 42  PHE   A CE1 1 
ATOM   62   C  CE2 . PHE   A 1 14  ? 19.356  -16.587 69.464  1.00 26.94 ? 42  PHE   A CE2 1 
ATOM   63   C  CZ  . PHE   A 1 14  ? 18.338  -15.641 69.380  1.00 24.33 ? 42  PHE   A CZ  1 
ATOM   64   N  N   . LYS   A 1 15  ? 23.460  -11.962 67.689  1.00 23.89 ? 43  LYS   A N   1 
ATOM   65   C  CA  . LYS   A 1 15  ? 23.393  -10.509 67.631  1.00 31.12 ? 43  LYS   A CA  1 
ATOM   66   C  C   . LYS   A 1 15  ? 21.969  -10.070 67.284  1.00 27.41 ? 43  LYS   A C   1 
ATOM   67   O  O   . LYS   A 1 15  ? 21.465  -10.351 66.191  1.00 24.16 ? 43  LYS   A O   1 
ATOM   68   C  CB  . LYS   A 1 15  ? 24.409  -9.976  66.623  1.00 28.26 ? 43  LYS   A CB  1 
ATOM   69   C  CG  . LYS   A 1 15  ? 24.233  -8.510  66.254  1.00 36.02 ? 43  LYS   A CG  1 
ATOM   70   C  CD  . LYS   A 1 15  ? 24.229  -7.578  67.455  1.00 35.51 ? 43  LYS   A CD  1 
ATOM   71   C  CE  . LYS   A 1 15  ? 24.111  -6.126  66.996  1.00 34.74 ? 43  LYS   A CE  1 
ATOM   72   N  NZ  . LYS   A 1 15  ? 24.438  -5.157  68.075  1.00 48.33 ? 43  LYS   A NZ  1 
ATOM   73   N  N   . VAL   A 1 16  ? 21.329  -9.388  68.225  1.00 26.61 ? 44  VAL   A N   1 
ATOM   74   C  CA  . VAL   A 1 16  ? 19.969  -8.886  68.072  1.00 28.63 ? 44  VAL   A CA  1 
ATOM   75   C  C   . VAL   A 1 16  ? 20.046  -7.377  67.897  1.00 31.16 ? 44  VAL   A C   1 
ATOM   76   O  O   . VAL   A 1 16  ? 20.774  -6.701  68.635  1.00 28.44 ? 44  VAL   A O   1 
ATOM   77   C  CB  . VAL   A 1 16  ? 19.098  -9.257  69.285  1.00 26.47 ? 44  VAL   A CB  1 
ATOM   78   C  CG1 . VAL   A 1 16  ? 17.768  -8.475  69.277  1.00 27.14 ? 44  VAL   A CG1 1 
ATOM   79   C  CG2 . VAL   A 1 16  ? 18.899  -10.796 69.358  1.00 23.61 ? 44  VAL   A CG2 1 
ATOM   80   N  N   . LYS   A 1 17  ? 19.309  -6.851  66.915  1.00 29.15 ? 45  LYS   A N   1 
ATOM   81   C  CA  . LYS   A 1 17  ? 19.277  -5.411  66.699  1.00 28.10 ? 45  LYS   A CA  1 
ATOM   82   C  C   . LYS   A 1 17  ? 18.064  -4.796  67.394  1.00 29.87 ? 45  LYS   A C   1 
ATOM   83   O  O   . LYS   A 1 17  ? 18.180  -4.327  68.530  1.00 35.34 ? 45  LYS   A O   1 
ATOM   84   C  CB  . LYS   A 1 17  ? 19.314  -5.112  65.200  1.00 27.99 ? 45  LYS   A CB  1 
ATOM   85   C  CG  . LYS   A 1 17  ? 20.640  -5.552  64.587  1.00 30.58 ? 45  LYS   A CG  1 
ATOM   86   C  CD  . LYS   A 1 17  ? 20.692  -5.469  63.066  1.00 33.46 ? 45  LYS   A CD  1 
ATOM   87   C  CE  . LYS   A 1 17  ? 20.784  -4.033  62.579  1.00 36.26 ? 45  LYS   A CE  1 
ATOM   88   N  NZ  . LYS   A 1 17  ? 20.733  -3.981  61.088  1.00 42.73 ? 45  LYS   A NZ  1 
ATOM   89   N  N   . ARG   A 1 18  ? 16.897  -4.808  66.759  1.00 26.32 ? 46  ARG   A N   1 
ATOM   90   C  CA  . ARG   A 1 18  ? 15.733  -4.129  67.317  1.00 26.92 ? 46  ARG   A CA  1 
ATOM   91   C  C   . ARG   A 1 18  ? 14.470  -4.912  66.991  1.00 23.10 ? 46  ARG   A C   1 
ATOM   92   O  O   . ARG   A 1 18  ? 14.479  -5.828  66.162  1.00 19.02 ? 46  ARG   A O   1 
ATOM   93   C  CB  . ARG   A 1 18  ? 15.598  -2.708  66.765  1.00 28.00 ? 46  ARG   A CB  1 
ATOM   94   C  CG  . ARG   A 1 18  ? 16.661  -1.738  67.237  1.00 34.78 ? 46  ARG   A CG  1 
ATOM   95   C  CD  . ARG   A 1 18  ? 16.342  -1.174  68.613  1.00 32.49 ? 46  ARG   A CD  1 
ATOM   96   N  NE  . ARG   A 1 18  ? 17.295  -0.133  68.984  1.00 48.95 ? 46  ARG   A NE  1 
ATOM   97   C  CZ  . ARG   A 1 18  ? 18.531  -0.362  69.428  1.00 49.38 ? 46  ARG   A CZ  1 
ATOM   98   N  NH1 . ARG   A 1 18  ? 18.973  -1.616  69.587  1.00 37.59 ? 46  ARG   A NH1 1 
ATOM   99   N  NH2 . ARG   A 1 18  ? 19.320  0.669   69.732  1.00 45.06 ? 46  ARG   A NH2 1 
ATOM   100  N  N   . PHE   A 1 19  ? 13.374  -4.532  67.655  1.00 22.70 ? 47  PHE   A N   1 
ATOM   101  C  CA  . PHE   A 1 19  ? 12.052  -4.945  67.198  1.00 18.03 ? 47  PHE   A CA  1 
ATOM   102  C  C   . PHE   A 1 19  ? 11.872  -4.523  65.754  1.00 18.30 ? 47  PHE   A C   1 
ATOM   103  O  O   . PHE   A 1 19  ? 12.180  -3.388  65.387  1.00 17.47 ? 47  PHE   A O   1 
ATOM   104  C  CB  . PHE   A 1 19  ? 10.952  -4.331  68.055  1.00 15.84 ? 47  PHE   A CB  1 
ATOM   105  C  CG  . PHE   A 1 19  ? 10.697  -5.069  69.347  1.00 17.22 ? 47  PHE   A CG  1 
ATOM   106  C  CD1 . PHE   A 1 19  ? 10.332  -6.402  69.348  1.00 16.28 ? 47  PHE   A CD1 1 
ATOM   107  C  CD2 . PHE   A 1 19  ? 10.783  -4.412  70.555  1.00 18.15 ? 47  PHE   A CD2 1 
ATOM   108  C  CE1 . PHE   A 1 19  ? 10.092  -7.063  70.527  1.00 17.37 ? 47  PHE   A CE1 1 
ATOM   109  C  CE2 . PHE   A 1 19  ? 10.532  -5.072  71.739  1.00 17.51 ? 47  PHE   A CE2 1 
ATOM   110  C  CZ  . PHE   A 1 19  ? 10.190  -6.397  71.723  1.00 18.21 ? 47  PHE   A CZ  1 
ATOM   111  N  N   . HIS   A 1 20  ? 11.398  -5.448  64.924  1.00 18.63 ? 48  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 20  ? 11.211  -5.164  63.512  1.00 16.70 ? 48  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 20  ? 9.749   -5.015  63.120  1.00 21.29 ? 48  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 20  ? 9.394   -4.074  62.415  1.00 17.72 ? 48  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 20  ? 11.868  -6.251  62.662  1.00 15.85 ? 48  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 20  ? 11.899  -5.908  61.214  1.00 21.78 ? 48  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 20  ? 10.892  -6.264  60.345  1.00 24.69 ? 48  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 20  ? 12.786  -5.185  60.490  1.00 28.20 ? 48  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 20  ? 11.170  -5.799  59.140  1.00 28.78 ? 48  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 20  ? 12.314  -5.139  59.201  1.00 29.71 ? 48  HIS   A NE2 1 
ATOM   121  N  N   . HIS   A 1 21  ? 8.888   -5.942  63.524  1.00 17.90 ? 49  HIS   A N   1 
ATOM   122  C  CA  . HIS   A 1 21  ? 7.467   -5.763  63.277  1.00 19.89 ? 49  HIS   A CA  1 
ATOM   123  C  C   . HIS   A 1 21  ? 6.676   -6.719  64.160  1.00 18.27 ? 49  HIS   A C   1 
ATOM   124  O  O   . HIS   A 1 21  ? 7.227   -7.575  64.857  1.00 16.84 ? 49  HIS   A O   1 
ATOM   125  C  CB  . HIS   A 1 21  ? 7.098   -5.948  61.796  1.00 17.14 ? 49  HIS   A CB  1 
ATOM   126  C  CG  . HIS   A 1 21  ? 7.259   -7.347  61.281  1.00 19.72 ? 49  HIS   A CG  1 
ATOM   127  N  ND1 . HIS   A 1 21  ? 8.449   -7.821  60.764  1.00 16.41 ? 49  HIS   A ND1 1 
ATOM   128  C  CD2 . HIS   A 1 21  ? 6.367   -8.364  61.174  1.00 15.25 ? 49  HIS   A CD2 1 
ATOM   129  C  CE1 . HIS   A 1 21  ? 8.284   -9.072  60.367  1.00 19.61 ? 49  HIS   A CE1 1 
ATOM   130  N  NE2 . HIS   A 1 21  ? 7.033   -9.428  60.609  1.00 17.32 ? 49  HIS   A NE2 1 
ATOM   131  N  N   . ILE   A 1 22  ? 5.367   -6.506  64.152  1.00 17.59 ? 50  ILE   A N   1 
ATOM   132  C  CA  . ILE   A 1 22  ? 4.398   -7.321  64.863  1.00 17.24 ? 50  ILE   A CA  1 
ATOM   133  C  C   . ILE   A 1 22  ? 3.369   -7.741  63.825  1.00 16.82 ? 50  ILE   A C   1 
ATOM   134  O  O   . ILE   A 1 22  ? 2.856   -6.887  63.089  1.00 16.94 ? 50  ILE   A O   1 
ATOM   135  C  CB  . ILE   A 1 22  ? 3.743   -6.528  66.015  1.00 17.14 ? 50  ILE   A CB  1 
ATOM   136  C  CG1 . ILE   A 1 22  ? 4.783   -6.184  67.081  1.00 15.09 ? 50  ILE   A CG1 1 
ATOM   137  C  CG2 . ILE   A 1 22  ? 2.537   -7.282  66.594  1.00 12.73 ? 50  ILE   A CG2 1 
ATOM   138  C  CD1 . ILE   A 1 22  ? 5.427   -7.404  67.746  1.00 14.08 ? 50  ILE   A CD1 1 
ATOM   139  N  N   . GLU   A 1 23  ? 3.096   -9.045  63.726  1.00 13.75 ? 51  GLU   A N   1 
ATOM   140  C  CA  . GLU   A 1 23  ? 2.111   -9.539  62.769  1.00 14.26 ? 51  GLU   A CA  1 
ATOM   141  C  C   . GLU   A 1 23  ? 0.864   -10.033 63.493  1.00 16.53 ? 51  GLU   A C   1 
ATOM   142  O  O   . GLU   A 1 23  ? 0.947   -10.896 64.379  1.00 14.30 ? 51  GLU   A O   1 
ATOM   143  C  CB  . GLU   A 1 23  ? 2.653   -10.659 61.878  1.00 12.02 ? 51  GLU   A CB  1 
ATOM   144  C  CG  . GLU   A 1 23  ? 1.614   -11.098 60.848  1.00 9.83  ? 51  GLU   A CG  1 
ATOM   145  C  CD  . GLU   A 1 23  ? 2.129   -12.150 59.877  1.00 13.35 ? 51  GLU   A CD  1 
ATOM   146  O  OE1 . GLU   A 1 23  ? 3.194   -12.737 60.130  1.00 16.36 ? 51  GLU   A OE1 1 
ATOM   147  O  OE2 . GLU   A 1 23  ? 1.476   -12.372 58.841  1.00 14.14 ? 51  GLU   A OE2 1 
ATOM   148  N  N   . PHE   A 1 24  ? -0.286  -9.491  63.093  1.00 14.29 ? 52  PHE   A N   1 
ATOM   149  C  CA  . PHE   A 1 24  ? -1.591  -9.950  63.543  1.00 13.06 ? 52  PHE   A CA  1 
ATOM   150  C  C   . PHE   A 1 24  ? -2.122  -10.964 62.539  1.00 13.47 ? 52  PHE   A C   1 
ATOM   151  O  O   . PHE   A 1 24  ? -2.082  -10.723 61.328  1.00 12.75 ? 52  PHE   A O   1 
ATOM   152  C  CB  . PHE   A 1 24  ? -2.584  -8.790  63.650  1.00 13.40 ? 52  PHE   A CB  1 
ATOM   153  C  CG  . PHE   A 1 24  ? -2.311  -7.832  64.768  1.00 13.29 ? 52  PHE   A CG  1 
ATOM   154  C  CD1 . PHE   A 1 24  ? -1.394  -6.813  64.622  1.00 13.62 ? 52  PHE   A CD1 1 
ATOM   155  C  CD2 . PHE   A 1 24  ? -3.003  -7.936  65.966  1.00 15.38 ? 52  PHE   A CD2 1 
ATOM   156  C  CE1 . PHE   A 1 24  ? -1.155  -5.910  65.669  1.00 15.02 ? 52  PHE   A CE1 1 
ATOM   157  C  CE2 . PHE   A 1 24  ? -2.768  -7.039  67.004  1.00 16.34 ? 52  PHE   A CE2 1 
ATOM   158  C  CZ  . PHE   A 1 24  ? -1.838  -6.037  66.860  1.00 12.01 ? 52  PHE   A CZ  1 
ATOM   159  N  N   . TRP   A 1 25  ? -2.639  -12.080 63.037  1.00 12.15 ? 53  TRP   A N   1 
ATOM   160  C  CA  . TRP   A 1 25  ? -3.369  -13.009 62.193  1.00 13.47 ? 53  TRP   A CA  1 
ATOM   161  C  C   . TRP   A 1 25  ? -4.856  -12.709 62.329  1.00 12.11 ? 53  TRP   A C   1 
ATOM   162  O  O   . TRP   A 1 25  ? -5.383  -12.632 63.440  1.00 14.74 ? 53  TRP   A O   1 
ATOM   163  C  CB  . TRP   A 1 25  ? -3.022  -14.459 62.536  1.00 13.71 ? 53  TRP   A CB  1 
ATOM   164  C  CG  . TRP   A 1 25  ? -1.916  -15.011 61.622  1.00 17.48 ? 53  TRP   A CG  1 
ATOM   165  C  CD1 . TRP   A 1 25  ? -1.246  -14.327 60.634  1.00 14.38 ? 53  TRP   A CD1 1 
ATOM   166  C  CD2 . TRP   A 1 25  ? -1.387  -16.354 61.606  1.00 14.25 ? 53  TRP   A CD2 1 
ATOM   167  N  NE1 . TRP   A 1 25  ? -0.348  -15.164 59.997  1.00 15.68 ? 53  TRP   A NE1 1 
ATOM   168  C  CE2 . TRP   A 1 25  ? -0.409  -16.409 60.579  1.00 16.55 ? 53  TRP   A CE2 1 
ATOM   169  C  CE3 . TRP   A 1 25  ? -1.643  -17.510 62.361  1.00 14.93 ? 53  TRP   A CE3 1 
ATOM   170  C  CZ2 . TRP   A 1 25  ? 0.313   -17.578 60.290  1.00 15.13 ? 53  TRP   A CZ2 1 
ATOM   171  C  CZ3 . TRP   A 1 25  ? -0.917  -18.679 62.071  1.00 16.25 ? 53  TRP   A CZ3 1 
ATOM   172  C  CH2 . TRP   A 1 25  ? 0.044   -18.697 61.042  1.00 14.72 ? 53  TRP   A CH2 1 
ATOM   173  N  N   . CYS   A 1 26  ? -5.511  -12.489 61.195  1.00 16.01 ? 54  CYS   A N   1 
ATOM   174  C  CA  . CYS   A 1 26  ? -6.865  -11.954 61.122  1.00 15.32 ? 54  CYS   A CA  1 
ATOM   175  C  C   . CYS   A 1 26  ? -7.745  -12.882 60.310  1.00 15.27 ? 54  CYS   A C   1 
ATOM   176  O  O   . CYS   A 1 26  ? -7.265  -13.715 59.536  1.00 16.32 ? 54  CYS   A O   1 
ATOM   177  C  CB  . CYS   A 1 26  ? -6.904  -10.561 60.449  1.00 12.12 ? 54  CYS   A CB  1 
ATOM   178  S  SG  . CYS   A 1 26  ? -5.665  -9.412  60.987  1.00 20.70 ? 54  CYS   A SG  1 
ATOM   179  N  N   . GLY   A 1 27  ? -9.047  -12.680 60.454  1.00 15.55 ? 55  GLY   A N   1 
ATOM   180  C  CA  . GLY   A 1 27  ? -10.013 -13.237 59.537  1.00 15.43 ? 55  GLY   A CA  1 
ATOM   181  C  C   . GLY   A 1 27  ? -10.144 -12.403 58.279  1.00 17.95 ? 55  GLY   A C   1 
ATOM   182  O  O   . GLY   A 1 27  ? -10.184 -12.927 57.160  1.00 17.86 ? 55  GLY   A O   1 
ATOM   183  N  N   . ASP   A 1 28  ? -10.212 -11.089 58.441  1.00 17.16 ? 56  ASP   A N   1 
ATOM   184  C  CA  . ASP   A 1 28  ? -10.184 -10.177 57.306  1.00 15.10 ? 56  ASP   A CA  1 
ATOM   185  C  C   . ASP   A 1 28  ? -9.114  -9.131  57.586  1.00 13.96 ? 56  ASP   A C   1 
ATOM   186  O  O   . ASP   A 1 28  ? -9.244  -8.330  58.517  1.00 16.30 ? 56  ASP   A O   1 
ATOM   187  C  CB  . ASP   A 1 28  ? -11.562 -9.547  57.075  1.00 13.72 ? 56  ASP   A CB  1 
ATOM   188  C  CG  . ASP   A 1 28  ? -11.582 -8.668  55.851  1.00 15.79 ? 56  ASP   A CG  1 
ATOM   189  O  OD1 . ASP   A 1 28  ? -11.729 -9.220  54.738  1.00 16.40 ? 56  ASP   A OD1 1 
ATOM   190  O  OD2 . ASP   A 1 28  ? -11.443 -7.437  56.005  1.00 17.73 ? 56  ASP   A OD2 1 
ATOM   191  N  N   . ALA   A 1 29  ? -8.036  -9.145  56.808  1.00 15.68 ? 57  ALA   A N   1 
ATOM   192  C  CA  . ALA   A 1 29  ? -6.946  -8.236  57.137  1.00 13.02 ? 57  ALA   A CA  1 
ATOM   193  C  C   . ALA   A 1 29  ? -7.295  -6.802  56.770  1.00 13.86 ? 57  ALA   A C   1 
ATOM   194  O  O   . ALA   A 1 29  ? -6.845  -5.868  57.440  1.00 16.42 ? 57  ALA   A O   1 
ATOM   195  C  CB  . ALA   A 1 29  ? -5.652  -8.687  56.450  1.00 11.45 ? 57  ALA   A CB  1 
ATOM   196  N  N   . THR   A 1 30  ? -8.120  -6.619  55.737  1.00 16.25 ? 58  THR   A N   1 
ATOM   197  C  CA  . THR   A 1 30  ? -8.454  -5.285  55.251  1.00 14.81 ? 58  THR   A CA  1 
ATOM   198  C  C   . THR   A 1 30  ? -9.132  -4.455  56.335  1.00 12.62 ? 58  THR   A C   1 
ATOM   199  O  O   . THR   A 1 30  ? -8.743  -3.307  56.592  1.00 13.56 ? 58  THR   A O   1 
ATOM   200  C  CB  . THR   A 1 30  ? -9.342  -5.416  54.009  1.00 18.19 ? 58  THR   A CB  1 
ATOM   201  O  OG1 . THR   A 1 30  ? -8.557  -5.921  52.919  1.00 17.02 ? 58  THR   A OG1 1 
ATOM   202  C  CG2 . THR   A 1 30  ? -9.992  -4.070  53.601  1.00 16.21 ? 58  THR   A CG2 1 
ATOM   203  N  N   . ASN   A 1 31  ? -10.137 -5.029  57.004  1.00 12.55 ? 59  ASN   A N   1 
ATOM   204  C  CA  . ASN   A 1 31  ? -10.924 -4.243  57.954  1.00 12.77 ? 59  ASN   A CA  1 
ATOM   205  C  C   . ASN   A 1 31  ? -10.157 -3.993  59.241  1.00 15.01 ? 59  ASN   A C   1 
ATOM   206  O  O   . ASN   A 1 31  ? -10.264 -2.909  59.829  1.00 12.57 ? 59  ASN   A O   1 
ATOM   207  C  CB  . ASN   A 1 31  ? -12.253 -4.934  58.243  1.00 12.54 ? 59  ASN   A CB  1 
ATOM   208  C  CG  . ASN   A 1 31  ? -13.305 -4.637  57.178  1.00 11.66 ? 59  ASN   A CG  1 
ATOM   209  O  OD1 . ASN   A 1 31  ? -14.126 -3.738  57.352  1.00 9.57  ? 59  ASN   A OD1 1 
ATOM   210  N  ND2 . ASN   A 1 31  ? -13.267 -5.375  56.060  1.00 11.03 ? 59  ASN   A ND2 1 
ATOM   211  N  N   . VAL   A 1 32  ? -9.371  -4.969  59.701  1.00 13.18 ? 60  VAL   A N   1 
ATOM   212  C  CA  . VAL   A 1 32  ? -8.582  -4.711  60.904  1.00 12.65 ? 60  VAL   A CA  1 
ATOM   213  C  C   . VAL   A 1 32  ? -7.528  -3.649  60.626  1.00 12.23 ? 60  VAL   A C   1 
ATOM   214  O  O   . VAL   A 1 32  ? -7.363  -2.700  61.403  1.00 13.91 ? 60  VAL   A O   1 
ATOM   215  C  CB  . VAL   A 1 32  ? -7.947  -6.004  61.448  1.00 13.18 ? 60  VAL   A CB  1 
ATOM   216  C  CG1 . VAL   A 1 32  ? -7.132  -5.691  62.670  1.00 10.57 ? 60  VAL   A CG1 1 
ATOM   217  C  CG2 . VAL   A 1 32  ? -9.034  -7.045  61.784  1.00 13.27 ? 60  VAL   A CG2 1 
ATOM   218  N  N   . ALA   A 1 33  ? -6.814  -3.773  59.506  1.00 12.56 ? 61  ALA   A N   1 
ATOM   219  C  CA  . ALA   A 1 33  ? -5.785  -2.792  59.189  1.00 11.59 ? 61  ALA   A CA  1 
ATOM   220  C  C   . ALA   A 1 33  ? -6.375  -1.392  59.052  1.00 14.57 ? 61  ALA   A C   1 
ATOM   221  O  O   . ALA   A 1 33  ? -5.820  -0.428  59.583  1.00 13.69 ? 61  ALA   A O   1 
ATOM   222  C  CB  . ALA   A 1 33  ? -5.045  -3.190  57.913  1.00 10.80 ? 61  ALA   A CB  1 
ATOM   223  N  N   . ARG   A 1 34  ? -7.504  -1.257  58.353  1.00 14.21 ? 62  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 34  ? -8.085  0.068   58.193  1.00 13.67 ? 62  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 34  ? -8.531  0.631   59.535  1.00 17.53 ? 62  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 34  ? -8.317  1.821   59.815  1.00 14.43 ? 62  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 34  ? -9.228  0.013   57.175  1.00 17.20 ? 62  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 34  ? -8.658  0.101   55.763  1.00 18.46 ? 62  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 34  ? -9.668  0.192   54.645  1.00 17.44 ? 62  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 34  ? -8.960  0.145   53.370  1.00 19.24 ? 62  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 34  ? -9.147  0.993   52.366  1.00 22.47 ? 62  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 34  ? -8.443  0.858   51.253  1.00 19.38 ? 62  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 34  ? -10.068 1.950   52.453  1.00 23.48 ? 62  ARG   A NH2 1 
ATOM   234  N  N   . ARG   A 1 35  ? -9.074  -0.223  60.416  1.00 13.25 ? 63  ARG   A N   1 
ATOM   235  C  CA  . ARG   A 1 35  ? -9.464  0.260   61.736  1.00 13.55 ? 63  ARG   A CA  1 
ATOM   236  C  C   . ARG   A 1 35  ? -8.237  0.704   62.535  1.00 13.19 ? 63  ARG   A C   1 
ATOM   237  O  O   . ARG   A 1 35  ? -8.245  1.775   63.153  1.00 14.35 ? 63  ARG   A O   1 
ATOM   238  C  CB  . ARG   A 1 35  ? -10.275 -0.826  62.470  1.00 15.45 ? 63  ARG   A CB  1 
ATOM   239  C  CG  . ARG   A 1 35  ? -10.978 -0.424  63.794  1.00 12.36 ? 63  ARG   A CG  1 
ATOM   240  C  CD  . ARG   A 1 35  ? -9.965  -0.302  64.949  1.00 14.21 ? 63  ARG   A CD  1 
ATOM   241  N  NE  . ARG   A 1 35  ? -10.565 -0.004  66.249  1.00 14.93 ? 63  ARG   A NE  1 
ATOM   242  C  CZ  . ARG   A 1 35  ? -10.729 -0.899  67.211  1.00 13.92 ? 63  ARG   A CZ  1 
ATOM   243  N  NH1 . ARG   A 1 35  ? -11.277 -0.542  68.365  1.00 13.78 ? 63  ARG   A NH1 1 
ATOM   244  N  NH2 . ARG   A 1 35  ? -10.371 -2.163  67.004  1.00 11.97 ? 63  ARG   A NH2 1 
ATOM   245  N  N   . PHE   A 1 36  ? -7.179  -0.110  62.547  1.00 12.99 ? 64  PHE   A N   1 
ATOM   246  C  CA  . PHE   A 1 36  ? -5.974  0.241   63.303  1.00 14.55 ? 64  PHE   A CA  1 
ATOM   247  C  C   . PHE   A 1 36  ? -5.323  1.507   62.756  1.00 14.97 ? 64  PHE   A C   1 
ATOM   248  O  O   . PHE   A 1 36  ? -4.803  2.326   63.524  1.00 14.47 ? 64  PHE   A O   1 
ATOM   249  C  CB  . PHE   A 1 36  ? -4.964  -0.911  63.272  1.00 11.08 ? 64  PHE   A CB  1 
ATOM   250  C  CG  . PHE   A 1 36  ? -5.200  -1.966  64.314  1.00 13.71 ? 64  PHE   A CG  1 
ATOM   251  C  CD1 . PHE   A 1 36  ? -6.417  -2.633  64.396  1.00 12.86 ? 64  PHE   A CD1 1 
ATOM   252  C  CD2 . PHE   A 1 36  ? -4.191  -2.316  65.199  1.00 12.27 ? 64  PHE   A CD2 1 
ATOM   253  C  CE1 . PHE   A 1 36  ? -6.630  -3.612  65.363  1.00 11.76 ? 64  PHE   A CE1 1 
ATOM   254  C  CE2 . PHE   A 1 36  ? -4.388  -3.303  66.156  1.00 13.89 ? 64  PHE   A CE2 1 
ATOM   255  C  CZ  . PHE   A 1 36  ? -5.626  -3.962  66.233  1.00 12.45 ? 64  PHE   A CZ  1 
ATOM   256  N  N   . SER   A 1 37  ? -5.329  1.670   61.429  1.00 15.01 ? 65  SER   A N   1 
ATOM   257  C  CA  . SER   A 1 37  ? -4.761  2.855   60.793  1.00 16.43 ? 65  SER   A CA  1 
ATOM   258  C  C   . SER   A 1 37  ? -5.397  4.135   61.330  1.00 15.81 ? 65  SER   A C   1 
ATOM   259  O  O   . SER   A 1 37  ? -4.707  5.035   61.821  1.00 16.68 ? 65  SER   A O   1 
ATOM   260  C  CB  . SER   A 1 37  ? -4.942  2.765   59.279  1.00 15.51 ? 65  SER   A CB  1 
ATOM   261  O  OG  . SER   A 1 37  ? -4.262  3.835   58.627  1.00 19.40 ? 65  SER   A OG  1 
ATOM   262  N  N   . TRP   A 1 38  ? -6.722  4.226   61.232  1.00 14.00 ? 66  TRP   A N   1 
ATOM   263  C  CA  . TRP   A 1 38  ? -7.436  5.375   61.770  1.00 13.70 ? 66  TRP   A CA  1 
ATOM   264  C  C   . TRP   A 1 38  ? -7.212  5.522   63.269  1.00 15.43 ? 66  TRP   A C   1 
ATOM   265  O  O   . TRP   A 1 38  ? -6.942  6.628   63.756  1.00 13.54 ? 66  TRP   A O   1 
ATOM   266  C  CB  . TRP   A 1 38  ? -8.926  5.231   61.460  1.00 11.10 ? 66  TRP   A CB  1 
ATOM   267  C  CG  . TRP   A 1 38  ? -9.792  6.360   61.914  1.00 15.03 ? 66  TRP   A CG  1 
ATOM   268  C  CD1 . TRP   A 1 38  ? -10.924 6.270   62.672  1.00 14.84 ? 66  TRP   A CD1 1 
ATOM   269  C  CD2 . TRP   A 1 38  ? -9.616  7.758   61.618  1.00 14.13 ? 66  TRP   A CD2 1 
ATOM   270  N  NE1 . TRP   A 1 38  ? -11.463 7.528   62.872  1.00 16.52 ? 66  TRP   A NE1 1 
ATOM   271  C  CE2 . TRP   A 1 38  ? -10.689 8.454   62.224  1.00 15.02 ? 66  TRP   A CE2 1 
ATOM   272  C  CE3 . TRP   A 1 38  ? -8.671  8.481   60.885  1.00 13.45 ? 66  TRP   A CE3 1 
ATOM   273  C  CZ2 . TRP   A 1 38  ? -10.832 9.844   62.132  1.00 13.90 ? 66  TRP   A CZ2 1 
ATOM   274  C  CZ3 . TRP   A 1 38  ? -8.820  9.869   60.778  1.00 15.42 ? 66  TRP   A CZ3 1 
ATOM   275  C  CH2 . TRP   A 1 38  ? -9.895  10.533  61.403  1.00 13.52 ? 66  TRP   A CH2 1 
ATOM   276  N  N   . GLY   A 1 39  ? -7.307  4.408   64.015  1.00 13.47 ? 67  GLY   A N   1 
ATOM   277  C  CA  . GLY   A 1 39  ? -7.309  4.479   65.467  1.00 12.28 ? 67  GLY   A CA  1 
ATOM   278  C  C   . GLY   A 1 39  ? -5.964  4.840   66.069  1.00 16.64 ? 67  GLY   A C   1 
ATOM   279  O  O   . GLY   A 1 39  ? -5.907  5.499   67.113  1.00 16.53 ? 67  GLY   A O   1 
ATOM   280  N  N   . LEU   A 1 40  ? -4.868  4.426   65.431  1.00 13.65 ? 68  LEU   A N   1 
ATOM   281  C  CA  . LEU   A 1 40  ? -3.538  4.667   65.977  1.00 16.29 ? 68  LEU   A CA  1 
ATOM   282  C  C   . LEU   A 1 40  ? -2.722  5.662   65.174  1.00 15.96 ? 68  LEU   A C   1 
ATOM   283  O  O   . LEU   A 1 40  ? -1.641  6.046   65.622  1.00 18.44 ? 68  LEU   A O   1 
ATOM   284  C  CB  . LEU   A 1 40  ? -2.743  3.352   66.073  1.00 18.72 ? 68  LEU   A CB  1 
ATOM   285  C  CG  . LEU   A 1 40  ? -3.197  2.348   67.139  1.00 16.35 ? 68  LEU   A CG  1 
ATOM   286  C  CD1 . LEU   A 1 40  ? -2.982  0.896   66.669  1.00 11.28 ? 68  LEU   A CD1 1 
ATOM   287  C  CD2 . LEU   A 1 40  ? -2.438  2.634   68.441  1.00 14.67 ? 68  LEU   A CD2 1 
ATOM   288  N  N   . GLY   A 1 41  ? -3.194  6.081   64.005  1.00 17.36 ? 69  GLY   A N   1 
ATOM   289  C  CA  . GLY   A 1 41  ? -2.451  7.045   63.217  1.00 20.20 ? 69  GLY   A CA  1 
ATOM   290  C  C   . GLY   A 1 41  ? -1.254  6.422   62.535  1.00 18.43 ? 69  GLY   A C   1 
ATOM   291  O  O   . GLY   A 1 41  ? -0.149  6.968   62.582  1.00 18.49 ? 69  GLY   A O   1 
ATOM   292  N  N   . MET   A 1 42  ? -1.468  5.280   61.890  1.00 17.19 ? 70  MET   A N   1 
ATOM   293  C  CA  . MET   A 1 42  ? -0.415  4.558   61.189  1.00 19.46 ? 70  MET   A CA  1 
ATOM   294  C  C   . MET   A 1 42  ? -0.710  4.596   59.693  1.00 19.99 ? 70  MET   A C   1 
ATOM   295  O  O   . MET   A 1 42  ? -1.853  4.408   59.277  1.00 23.41 ? 70  MET   A O   1 
ATOM   296  C  CB  . MET   A 1 42  ? -0.304  3.122   61.714  1.00 17.49 ? 70  MET   A CB  1 
ATOM   297  C  CG  . MET   A 1 42  ? -0.069  3.027   63.238  1.00 16.83 ? 70  MET   A CG  1 
ATOM   298  S  SD  . MET   A 1 42  ? 0.090   1.322   63.897  1.00 17.61 ? 70  MET   A SD  1 
ATOM   299  C  CE  . MET   A 1 42  ? 1.648   0.782   63.149  1.00 14.14 ? 70  MET   A CE  1 
ATOM   300  N  N   . ARG   A 1 43  ? 0.314   4.900   58.906  1.00 16.61 ? 71  ARG   A N   1 
ATOM   301  C  CA  . ARG   A 1 43  ? 0.229   4.953   57.451  1.00 21.99 ? 71  ARG   A CA  1 
ATOM   302  C  C   . ARG   A 1 43  ? 0.108   3.557   56.847  1.00 19.94 ? 71  ARG   A C   1 
ATOM   303  O  O   . ARG   A 1 43  ? 0.769   2.626   57.302  1.00 19.06 ? 71  ARG   A O   1 
ATOM   304  C  CB  . ARG   A 1 43  ? 1.516   5.572   56.907  1.00 22.04 ? 71  ARG   A CB  1 
ATOM   305  C  CG  . ARG   A 1 43  ? 1.610   7.040   56.824  1.00 34.30 ? 71  ARG   A CG  1 
ATOM   306  C  CD  . ARG   A 1 43  ? 2.519   7.366   55.637  1.00 37.69 ? 71  ARG   A CD  1 
ATOM   307  N  NE  . ARG   A 1 43  ? 1.971   8.462   54.837  1.00 48.84 ? 71  ARG   A NE  1 
ATOM   308  C  CZ  . ARG   A 1 43  ? 2.620   9.071   53.852  1.00 46.05 ? 71  ARG   A CZ  1 
ATOM   309  N  NH1 . ARG   A 1 43  ? 2.033   10.059  53.192  1.00 51.08 ? 71  ARG   A NH1 1 
ATOM   310  N  NH2 . ARG   A 1 43  ? 3.849   8.688   53.527  1.00 43.48 ? 71  ARG   A NH2 1 
ATOM   311  N  N   . PHE   A 1 44  ? -0.657  3.428   55.761  1.00 17.09 ? 72  PHE   A N   1 
ATOM   312  C  CA  . PHE   A 1 44  ? -0.530  2.251   54.899  1.00 22.46 ? 72  PHE   A CA  1 
ATOM   313  C  C   . PHE   A 1 44  ? 0.775   2.332   54.099  1.00 27.81 ? 72  PHE   A C   1 
ATOM   314  O  O   . PHE   A 1 44  ? 0.946   3.242   53.282  1.00 22.14 ? 72  PHE   A O   1 
ATOM   315  C  CB  . PHE   A 1 44  ? -1.722  2.159   53.944  1.00 27.77 ? 72  PHE   A CB  1 
ATOM   316  C  CG  . PHE   A 1 44  ? -2.927  1.480   54.528  1.00 33.52 ? 72  PHE   A CG  1 
ATOM   317  C  CD1 . PHE   A 1 44  ? -2.982  0.098   54.629  1.00 34.53 ? 72  PHE   A CD1 1 
ATOM   318  C  CD2 . PHE   A 1 44  ? -4.017  2.226   54.980  1.00 36.13 ? 72  PHE   A CD2 1 
ATOM   319  C  CE1 . PHE   A 1 44  ? -4.117  -0.541  55.164  1.00 36.18 ? 72  PHE   A CE1 1 
ATOM   320  C  CE2 . PHE   A 1 44  ? -5.149  1.595   55.522  1.00 31.91 ? 72  PHE   A CE2 1 
ATOM   321  C  CZ  . PHE   A 1 44  ? -5.190  0.208   55.613  1.00 27.43 ? 72  PHE   A CZ  1 
ATOM   322  N  N   . SER   A 1 45  ? 1.687   1.377   54.304  1.00 23.31 ? 73  SER   A N   1 
ATOM   323  C  CA  . SER   A 1 45  ? 3.024   1.463   53.717  1.00 26.20 ? 73  SER   A CA  1 
ATOM   324  C  C   . SER   A 1 45  ? 3.307   0.421   52.648  1.00 25.95 ? 73  SER   A C   1 
ATOM   325  O  O   . SER   A 1 45  ? 4.002   0.720   51.679  1.00 23.03 ? 73  SER   A O   1 
ATOM   326  C  CB  . SER   A 1 45  ? 4.085   1.333   54.811  1.00 25.92 ? 73  SER   A CB  1 
ATOM   327  O  OG  . SER   A 1 45  ? 4.193   2.539   55.538  1.00 33.22 ? 73  SER   A OG  1 
ATOM   328  N  N   . ALA   A 1 46  ? 2.811   -0.803  52.802  1.00 21.80 ? 74  ALA   A N   1 
ATOM   329  C  CA  . ALA   A 1 46  ? 3.138   -1.861  51.858  1.00 23.77 ? 74  ALA   A CA  1 
ATOM   330  C  C   . ALA   A 1 46  ? 2.010   -2.879  51.844  1.00 22.54 ? 74  ALA   A C   1 
ATOM   331  O  O   . ALA   A 1 46  ? 1.243   -2.992  52.797  1.00 23.22 ? 74  ALA   A O   1 
ATOM   332  C  CB  . ALA   A 1 46  ? 4.478   -2.528  52.201  1.00 18.97 ? 74  ALA   A CB  1 
ATOM   333  N  N   . LYS   A 1 47  ? 1.912   -3.618  50.744  1.00 22.87 ? 75  LYS   A N   1 
ATOM   334  C  CA  . LYS   A 1 47  ? 0.881   -4.628  50.601  1.00 24.96 ? 75  LYS   A CA  1 
ATOM   335  C  C   . LYS   A 1 47  ? 1.461   -5.835  49.883  1.00 23.77 ? 75  LYS   A C   1 
ATOM   336  O  O   . LYS   A 1 47  ? 2.417   -5.721  49.119  1.00 21.86 ? 75  LYS   A O   1 
ATOM   337  C  CB  . LYS   A 1 47  ? -0.346  -4.095  49.837  1.00 22.94 ? 75  LYS   A CB  1 
ATOM   338  C  CG  . LYS   A 1 47  ? -0.070  -3.698  48.395  1.00 24.72 ? 75  LYS   A CG  1 
ATOM   339  C  CD  . LYS   A 1 47  ? -1.348  -3.306  47.658  1.00 23.47 ? 75  LYS   A CD  1 
ATOM   340  C  CE  . LYS   A 1 47  ? -1.080  -2.925  46.208  1.00 23.44 ? 75  LYS   A CE  1 
ATOM   341  N  NZ  . LYS   A 1 47  ? -2.346  -2.441  45.571  1.00 27.59 ? 75  LYS   A NZ  1 
ATOM   342  N  N   . SER   A 1 48  ? 0.883   -6.996  50.170  1.00 18.09 ? 76  SER   A N   1 
ATOM   343  C  CA  . SER   A 1 48  ? 1.106   -8.210  49.406  1.00 18.36 ? 76  SER   A CA  1 
ATOM   344  C  C   . SER   A 1 48  ? -0.237  -8.925  49.386  1.00 19.81 ? 76  SER   A C   1 
ATOM   345  O  O   . SER   A 1 48  ? -0.701  -9.388  50.430  1.00 21.79 ? 76  SER   A O   1 
ATOM   346  C  CB  . SER   A 1 48  ? 2.195   -9.079  50.030  1.00 18.05 ? 76  SER   A CB  1 
ATOM   347  O  OG  . SER   A 1 48  ? 2.184   -10.391 49.479  1.00 19.16 ? 76  SER   A OG  1 
ATOM   348  N  N   . ASP   A 1 49  ? -0.875  -8.981  48.223  1.00 19.06 ? 77  ASP   A N   1 
ATOM   349  C  CA  . ASP   A 1 49  ? -2.202  -9.577  48.101  1.00 19.82 ? 77  ASP   A CA  1 
ATOM   350  C  C   . ASP   A 1 49  ? -2.394  -9.997  46.645  1.00 22.47 ? 77  ASP   A C   1 
ATOM   351  O  O   . ASP   A 1 49  ? -1.423  -10.098 45.886  1.00 23.11 ? 77  ASP   A O   1 
ATOM   352  C  CB  . ASP   A 1 49  ? -3.276  -8.591  48.604  1.00 18.08 ? 77  ASP   A CB  1 
ATOM   353  C  CG  . ASP   A 1 49  ? -3.280  -7.281  47.841  1.00 21.90 ? 77  ASP   A CG  1 
ATOM   354  O  OD1 . ASP   A 1 49  ? -2.605  -7.192  46.790  1.00 22.40 ? 77  ASP   A OD1 1 
ATOM   355  O  OD2 . ASP   A 1 49  ? -3.970  -6.332  48.297  1.00 21.26 ? 77  ASP   A OD2 1 
ATOM   356  N  N   . LEU   A 1 50  ? -3.653  -10.208 46.248  1.00 17.98 ? 78  LEU   A N   1 
ATOM   357  C  CA  . LEU   A 1 50  ? -3.968  -10.568 44.868  1.00 20.63 ? 78  LEU   A CA  1 
ATOM   358  C  C   . LEU   A 1 50  ? -3.388  -9.573  43.874  1.00 19.71 ? 78  LEU   A C   1 
ATOM   359  O  O   . LEU   A 1 50  ? -2.900  -9.964  42.810  1.00 22.79 ? 78  LEU   A O   1 
ATOM   360  C  CB  . LEU   A 1 50  ? -5.482  -10.657 44.675  1.00 17.14 ? 78  LEU   A CB  1 
ATOM   361  C  CG  . LEU   A 1 50  ? -6.231  -11.785 45.357  1.00 22.31 ? 78  LEU   A CG  1 
ATOM   362  C  CD1 . LEU   A 1 50  ? -7.742  -11.491 45.285  1.00 20.92 ? 78  LEU   A CD1 1 
ATOM   363  C  CD2 . LEU   A 1 50  ? -5.886  -13.112 44.720  1.00 18.02 ? 78  LEU   A CD2 1 
ATOM   364  N  N   . SER   A 1 51  ? -3.451  -8.282  44.187  1.00 17.47 ? 79  SER   A N   1 
ATOM   365  C  CA  . SER   A 1 51  ? -2.975  -7.294  43.226  1.00 22.71 ? 79  SER   A CA  1 
ATOM   366  C  C   . SER   A 1 51  ? -1.463  -7.323  43.059  1.00 20.59 ? 79  SER   A C   1 
ATOM   367  O  O   . SER   A 1 51  ? -0.955  -6.703  42.125  1.00 28.51 ? 79  SER   A O   1 
ATOM   368  C  CB  . SER   A 1 51  ? -3.420  -5.879  43.633  1.00 21.41 ? 79  SER   A CB  1 
ATOM   369  O  OG  . SER   A 1 51  ? -2.610  -5.379  44.678  1.00 20.44 ? 79  SER   A OG  1 
ATOM   370  N  N   . THR   A 1 52  ? -0.733  -8.012  43.933  1.00 21.28 ? 80  THR   A N   1 
ATOM   371  C  CA  . THR   A 1 52  ? 0.703   -8.194  43.775  1.00 23.88 ? 80  THR   A CA  1 
ATOM   372  C  C   . THR   A 1 52  ? 1.070   -9.625  43.385  1.00 23.28 ? 80  THR   A C   1 
ATOM   373  O  O   . THR   A 1 52  ? 2.255   -9.978  43.407  1.00 28.18 ? 80  THR   A O   1 
ATOM   374  C  CB  . THR   A 1 52  ? 1.447   -7.793  45.054  1.00 24.21 ? 80  THR   A CB  1 
ATOM   375  O  OG1 . THR   A 1 52  ? 1.291   -8.813  46.051  1.00 22.40 ? 80  THR   A OG1 1 
ATOM   376  C  CG2 . THR   A 1 52  ? 0.936   -6.456  45.587  1.00 22.81 ? 80  THR   A CG2 1 
ATOM   377  N  N   . GLY   A 1 53  ? 0.092   -10.456 43.030  1.00 21.13 ? 81  GLY   A N   1 
ATOM   378  C  CA  . GLY   A 1 53  ? 0.362   -11.829 42.651  1.00 24.06 ? 81  GLY   A CA  1 
ATOM   379  C  C   . GLY   A 1 53  ? 0.332   -12.837 43.783  1.00 25.24 ? 81  GLY   A C   1 
ATOM   380  O  O   . GLY   A 1 53  ? 0.613   -14.018 43.550  1.00 25.11 ? 81  GLY   A O   1 
ATOM   381  N  N   . ASN   A 1 54  ? 0.006   -12.420 45.000  1.00 24.98 ? 82  ASN   A N   1 
ATOM   382  C  CA  . ASN   A 1 54  ? -0.066  -13.331 46.135  1.00 21.81 ? 82  ASN   A CA  1 
ATOM   383  C  C   . ASN   A 1 54  ? -1.457  -13.967 46.127  1.00 22.71 ? 82  ASN   A C   1 
ATOM   384  O  O   . ASN   A 1 54  ? -2.461  -13.284 46.367  1.00 18.32 ? 82  ASN   A O   1 
ATOM   385  C  CB  . ASN   A 1 54  ? 0.234   -12.578 47.434  1.00 19.85 ? 82  ASN   A CB  1 
ATOM   386  C  CG  . ASN   A 1 54  ? 0.373   -13.501 48.645  1.00 19.30 ? 82  ASN   A CG  1 
ATOM   387  O  OD1 . ASN   A 1 54  ? -0.084  -14.655 48.631  1.00 19.22 ? 82  ASN   A OD1 1 
ATOM   388  N  ND2 . ASN   A 1 54  ? 0.978   -12.984 49.710  1.00 17.46 ? 82  ASN   A ND2 1 
ATOM   389  N  N   . MET   A 1 55  ? -1.510  -15.271 45.817  1.00 22.60 ? 83  MET   A N   1 
ATOM   390  C  CA  . MET   A 1 55  ? -2.735  -16.069 45.798  1.00 21.10 ? 83  MET   A CA  1 
ATOM   391  C  C   . MET   A 1 55  ? -2.973  -16.797 47.110  1.00 20.88 ? 83  MET   A C   1 
ATOM   392  O  O   . MET   A 1 55  ? -3.975  -17.511 47.242  1.00 21.26 ? 83  MET   A O   1 
ATOM   393  C  CB  . MET   A 1 55  ? -2.687  -17.109 44.661  1.00 19.20 ? 83  MET   A CB  1 
ATOM   394  C  CG  . MET   A 1 55  ? -2.403  -16.533 43.271  1.00 23.07 ? 83  MET   A CG  1 
ATOM   395  S  SD  . MET   A 1 55  ? -3.742  -15.484 42.635  1.00 32.26 ? 83  MET   A SD  1 
ATOM   396  C  CE  . MET   A 1 55  ? -2.969  -13.890 42.575  1.00 25.16 ? 83  MET   A CE  1 
ATOM   397  N  N   . VAL   A 1 56  ? -2.075  -16.639 48.076  1.00 20.43 ? 84  VAL   A N   1 
ATOM   398  C  CA  . VAL   A 1 56  ? -2.159  -17.364 49.331  1.00 20.63 ? 84  VAL   A CA  1 
ATOM   399  C  C   . VAL   A 1 56  ? -2.760  -16.482 50.417  1.00 16.85 ? 84  VAL   A C   1 
ATOM   400  O  O   . VAL   A 1 56  ? -3.731  -16.865 51.069  1.00 17.35 ? 84  VAL   A O   1 
ATOM   401  C  CB  . VAL   A 1 56  ? -0.777  -17.889 49.763  1.00 20.01 ? 84  VAL   A CB  1 
ATOM   402  C  CG1 . VAL   A 1 56  ? -0.878  -18.504 51.134  1.00 20.60 ? 84  VAL   A CG1 1 
ATOM   403  C  CG2 . VAL   A 1 56  ? -0.255  -18.941 48.750  1.00 20.42 ? 84  VAL   A CG2 1 
ATOM   404  N  N   . HIS   A 1 57  ? -2.173  -15.320 50.662  1.00 15.33 ? 85  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 57  ? -2.620  -14.530 51.795  1.00 18.30 ? 85  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 57  ? -2.656  -13.054 51.428  1.00 19.96 ? 85  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 57  ? -1.945  -12.587 50.528  1.00 17.91 ? 85  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 57  ? -1.739  -14.759 53.041  1.00 15.24 ? 85  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 57  ? -0.276  -14.500 52.818  1.00 18.38 ? 85  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 57  ? 0.333   -13.305 53.153  1.00 19.17 ? 85  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 57  ? 0.700   -15.284 52.302  1.00 15.86 ? 85  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 57  ? 1.618   -13.366 52.854  1.00 17.20 ? 85  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 57  ? 1.865   -14.554 52.333  1.00 20.03 ? 85  HIS   A NE2 1 
ATOM   414  N  N   . ALA   A 1 58  ? -3.516  -12.336 52.138  1.00 16.91 ? 86  ALA   A N   1 
ATOM   415  C  CA  . ALA   A 1 58  ? -3.604  -10.892 52.062  1.00 16.61 ? 86  ALA   A CA  1 
ATOM   416  C  C   . ALA   A 1 58  ? -2.871  -10.320 53.261  1.00 15.12 ? 86  ALA   A C   1 
ATOM   417  O  O   . ALA   A 1 58  ? -3.240  -10.612 54.403  1.00 13.57 ? 86  ALA   A O   1 
ATOM   418  C  CB  . ALA   A 1 58  ? -5.062  -10.434 52.058  1.00 15.85 ? 86  ALA   A CB  1 
ATOM   419  N  N   . SER   A 1 59  ? -1.845  -9.505  53.002  1.00 14.87 ? 87  SER   A N   1 
ATOM   420  C  CA  . SER   A 1 59  ? -1.004  -8.923  54.041  1.00 18.03 ? 87  SER   A CA  1 
ATOM   421  C  C   . SER   A 1 59  ? -0.852  -7.428  53.807  1.00 18.53 ? 87  SER   A C   1 
ATOM   422  O  O   . SER   A 1 59  ? -0.444  -7.009  52.719  1.00 18.17 ? 87  SER   A O   1 
ATOM   423  C  CB  . SER   A 1 59  ? 0.389   -9.573  54.067  1.00 16.64 ? 87  SER   A CB  1 
ATOM   424  O  OG  . SER   A 1 59  ? 0.348   -10.775 54.793  1.00 19.63 ? 87  SER   A OG  1 
ATOM   425  N  N   . TYR   A 1 60  ? -1.142  -6.632  54.837  1.00 15.97 ? 88  TYR   A N   1 
ATOM   426  C  CA  . TYR   A 1 60  ? -1.077  -5.177  54.748  1.00 18.30 ? 88  TYR   A CA  1 
ATOM   427  C  C   . TYR   A 1 60  ? -0.236  -4.644  55.892  1.00 17.79 ? 88  TYR   A C   1 
ATOM   428  O  O   . TYR   A 1 60  ? -0.442  -5.023  57.051  1.00 16.51 ? 88  TYR   A O   1 
ATOM   429  C  CB  . TYR   A 1 60  ? -2.494  -4.551  54.758  1.00 15.51 ? 88  TYR   A CB  1 
ATOM   430  C  CG  . TYR   A 1 60  ? -3.324  -5.093  53.626  1.00 15.88 ? 88  TYR   A CG  1 
ATOM   431  C  CD1 . TYR   A 1 60  ? -2.961  -4.834  52.308  1.00 16.40 ? 88  TYR   A CD1 1 
ATOM   432  C  CD2 . TYR   A 1 60  ? -4.435  -5.918  53.862  1.00 15.46 ? 88  TYR   A CD2 1 
ATOM   433  C  CE1 . TYR   A 1 60  ? -3.681  -5.338  51.250  1.00 17.31 ? 88  TYR   A CE1 1 
ATOM   434  C  CE2 . TYR   A 1 60  ? -5.184  -6.433  52.800  1.00 14.94 ? 88  TYR   A CE2 1 
ATOM   435  C  CZ  . TYR   A 1 60  ? -4.787  -6.138  51.492  1.00 16.41 ? 88  TYR   A CZ  1 
ATOM   436  O  OH  . TYR   A 1 60  ? -5.487  -6.632  50.417  1.00 16.89 ? 88  TYR   A OH  1 
ATOM   437  N  N   . LEU   A 1 61  ? 0.710   -3.773  55.564  1.00 15.92 ? 89  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 61  ? 1.644   -3.231  56.533  1.00 14.74 ? 89  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 61  ? 1.283   -1.791  56.848  1.00 18.83 ? 89  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 61  ? 1.140   -0.970  55.930  1.00 16.28 ? 89  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 61  ? 3.078   -3.291  56.009  1.00 19.80 ? 89  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 61  ? 4.087   -2.686  56.983  1.00 20.10 ? 89  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 61  ? 4.306   -3.635  58.168  1.00 16.71 ? 89  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 61  ? 5.417   -2.342  56.298  1.00 20.17 ? 89  LEU   A CD2 1 
ATOM   445  N  N   . LEU   A 1 62  ? 1.145   -1.493  58.144  1.00 16.96 ? 90  LEU   A N   1 
ATOM   446  C  CA  . LEU   A 1 62  ? 1.012   -0.129  58.645  1.00 16.70 ? 90  LEU   A CA  1 
ATOM   447  C  C   . LEU   A 1 62  ? 2.309   0.262   59.332  1.00 17.01 ? 90  LEU   A C   1 
ATOM   448  O  O   . LEU   A 1 62  ? 2.930   -0.567  60.005  1.00 16.34 ? 90  LEU   A O   1 
ATOM   449  C  CB  . LEU   A 1 62  ? -0.133  0.012   59.655  1.00 15.90 ? 90  LEU   A CB  1 
ATOM   450  C  CG  . LEU   A 1 62  ? -1.533  -0.470  59.298  1.00 15.82 ? 90  LEU   A CG  1 
ATOM   451  C  CD1 . LEU   A 1 62  ? -2.510  -0.079  60.374  1.00 11.45 ? 90  LEU   A CD1 1 
ATOM   452  C  CD2 . LEU   A 1 62  ? -1.922  0.126   57.958  1.00 18.93 ? 90  LEU   A CD2 1 
ATOM   453  N  N   . THR   A 1 63  ? 2.718   1.521   59.169  1.00 18.68 ? 91  THR   A N   1 
ATOM   454  C  CA  . THR   A 1 63  ? 3.910   2.022   59.838  1.00 19.84 ? 91  THR   A CA  1 
ATOM   455  C  C   . THR   A 1 63  ? 3.596   3.319   60.564  1.00 20.05 ? 91  THR   A C   1 
ATOM   456  O  O   . THR   A 1 63  ? 2.730   4.091   60.147  1.00 18.89 ? 91  THR   A O   1 
ATOM   457  C  CB  . THR   A 1 63  ? 5.054   2.286   58.864  1.00 23.51 ? 91  THR   A CB  1 
ATOM   458  O  OG1 . THR   A 1 63  ? 4.631   3.261   57.906  1.00 26.46 ? 91  THR   A OG1 1 
ATOM   459  C  CG2 . THR   A 1 63  ? 5.447   1.010   58.135  1.00 18.62 ? 91  THR   A CG2 1 
ATOM   460  N  N   . SER   A 1 64  ? 4.328   3.557   61.650  1.00 21.33 ? 92  SER   A N   1 
ATOM   461  C  CA  . SER   A 1 64  ? 4.367   4.876   62.282  1.00 20.68 ? 92  SER   A CA  1 
ATOM   462  C  C   . SER   A 1 64  ? 5.762   5.020   62.878  1.00 18.53 ? 92  SER   A C   1 
ATOM   463  O  O   . SER   A 1 64  ? 6.092   4.320   63.840  1.00 20.95 ? 92  SER   A O   1 
ATOM   464  C  CB  . SER   A 1 64  ? 3.274   5.019   63.348  1.00 18.26 ? 92  SER   A CB  1 
ATOM   465  O  OG  . SER   A 1 64  ? 3.133   6.369   63.787  1.00 18.81 ? 92  SER   A OG  1 
ATOM   466  N  N   . GLY   A 1 65  ? 6.588   5.895   62.302  1.00 22.15 ? 93  GLY   A N   1 
ATOM   467  C  CA  . GLY   A 1 65  ? 7.994   5.913   62.688  1.00 17.53 ? 93  GLY   A CA  1 
ATOM   468  C  C   . GLY   A 1 65  ? 8.618   4.544   62.435  1.00 20.71 ? 93  GLY   A C   1 
ATOM   469  O  O   . GLY   A 1 65  ? 8.508   3.991   61.339  1.00 21.68 ? 93  GLY   A O   1 
ATOM   470  N  N   . ASP   A 1 66  ? 9.273   3.974   63.451  1.00 16.23 ? 94  ASP   A N   1 
ATOM   471  C  CA  . ASP   A 1 66  ? 9.840   2.635   63.310  1.00 19.41 ? 94  ASP   A CA  1 
ATOM   472  C  C   . ASP   A 1 66  ? 8.834   1.528   63.603  1.00 20.78 ? 94  ASP   A C   1 
ATOM   473  O  O   . ASP   A 1 66  ? 9.179   0.348   63.445  1.00 22.25 ? 94  ASP   A O   1 
ATOM   474  C  CB  . ASP   A 1 66  ? 11.051  2.448   64.238  1.00 19.37 ? 94  ASP   A CB  1 
ATOM   475  C  CG  . ASP   A 1 66  ? 12.222  3.336   63.870  1.00 30.93 ? 94  ASP   A CG  1 
ATOM   476  O  OD1 . ASP   A 1 66  ? 12.356  3.686   62.673  1.00 28.97 ? 94  ASP   A OD1 1 
ATOM   477  O  OD2 . ASP   A 1 66  ? 13.009  3.694   64.781  1.00 39.47 ? 94  ASP   A OD2 1 
ATOM   478  N  N   . LEU   A 1 67  ? 7.621   1.865   64.046  1.00 17.05 ? 95  LEU   A N   1 
ATOM   479  C  CA  . LEU   A 1 67  ? 6.643   0.847   64.410  1.00 17.19 ? 95  LEU   A CA  1 
ATOM   480  C  C   . LEU   A 1 67  ? 5.992   0.283   63.149  1.00 15.30 ? 95  LEU   A C   1 
ATOM   481  O  O   . LEU   A 1 67  ? 5.552   1.034   62.275  1.00 17.30 ? 95  LEU   A O   1 
ATOM   482  C  CB  . LEU   A 1 67  ? 5.593   1.419   65.366  1.00 14.07 ? 95  LEU   A CB  1 
ATOM   483  C  CG  . LEU   A 1 67  ? 4.522   0.392   65.791  1.00 17.05 ? 95  LEU   A CG  1 
ATOM   484  C  CD1 . LEU   A 1 67  ? 5.154   -0.778  66.512  1.00 10.21 ? 95  LEU   A CD1 1 
ATOM   485  C  CD2 . LEU   A 1 67  ? 3.446   1.040   66.660  1.00 13.02 ? 95  LEU   A CD2 1 
ATOM   486  N  N   . ARG   A 1 68  ? 5.979   -1.043  63.035  1.00 16.71 ? 96  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 68  ? 5.423   -1.733  61.877  1.00 16.11 ? 96  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 68  ? 4.421   -2.761  62.361  1.00 16.74 ? 96  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 68  ? 4.798   -3.711  63.057  1.00 17.74 ? 96  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 68  ? 6.500   -2.436  61.047  1.00 19.38 ? 96  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 68  ? 7.575   -1.533  60.507  1.00 23.07 ? 96  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 68  ? 8.584   -2.356  59.761  1.00 27.79 ? 96  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 68  ? 9.715   -1.548  59.352  1.00 36.91 ? 96  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 68  ? 10.876  -1.537  59.987  1.00 36.41 ? 96  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 68  ? 11.050  -2.309  61.047  1.00 31.96 ? 96  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 68  ? 11.860  -0.759  59.553  1.00 41.10 ? 96  ARG   A NH2 1 
ATOM   497  N  N   . PHE   A 1 69  ? 3.157   -2.574  61.979  1.00 16.06 ? 97  PHE   A N   1 
ATOM   498  C  CA  . PHE   A 1 69  ? 2.076   -3.526  62.237  1.00 16.46 ? 97  PHE   A CA  1 
ATOM   499  C  C   . PHE   A 1 69  ? 1.708   -4.209  60.927  1.00 15.08 ? 97  PHE   A C   1 
ATOM   500  O  O   . PHE   A 1 69  ? 1.317   -3.533  59.970  1.00 16.94 ? 97  PHE   A O   1 
ATOM   501  C  CB  . PHE   A 1 69  ? 0.850   -2.820  62.817  1.00 13.40 ? 97  PHE   A CB  1 
ATOM   502  C  CG  . PHE   A 1 69  ? 0.896   -2.637  64.303  1.00 17.59 ? 97  PHE   A CG  1 
ATOM   503  C  CD1 . PHE   A 1 69  ? 2.017   -3.032  65.040  1.00 14.60 ? 97  PHE   A CD1 1 
ATOM   504  C  CD2 . PHE   A 1 69  ? -0.186  -2.069  64.973  1.00 11.69 ? 97  PHE   A CD2 1 
ATOM   505  C  CE1 . PHE   A 1 69  ? 2.060   -2.871  66.421  1.00 14.06 ? 97  PHE   A CE1 1 
ATOM   506  C  CE2 . PHE   A 1 69  ? -0.155  -1.904  66.346  1.00 13.83 ? 97  PHE   A CE2 1 
ATOM   507  C  CZ  . PHE   A 1 69  ? 0.968   -2.300  67.079  1.00 17.37 ? 97  PHE   A CZ  1 
ATOM   508  N  N   . LEU   A 1 70  ? 1.829   -5.535  60.886  1.00 12.23 ? 98  LEU   A N   1 
ATOM   509  C  CA  . LEU   A 1 70  ? 1.435   -6.338  59.732  1.00 14.83 ? 98  LEU   A CA  1 
ATOM   510  C  C   . LEU   A 1 70  ? 0.137   -7.088  60.034  1.00 15.16 ? 98  LEU   A C   1 
ATOM   511  O  O   . LEU   A 1 70  ? 0.018   -7.727  61.083  1.00 13.85 ? 98  LEU   A O   1 
ATOM   512  C  CB  . LEU   A 1 70  ? 2.545   -7.327  59.363  1.00 12.25 ? 98  LEU   A CB  1 
ATOM   513  C  CG  . LEU   A 1 70  ? 2.388   -8.156  58.084  1.00 16.92 ? 98  LEU   A CG  1 
ATOM   514  C  CD1 . LEU   A 1 70  ? 2.354   -7.306  56.824  1.00 14.79 ? 98  LEU   A CD1 1 
ATOM   515  C  CD2 . LEU   A 1 70  ? 3.491   -9.242  57.978  1.00 14.22 ? 98  LEU   A CD2 1 
ATOM   516  N  N   . PHE   A 1 71  ? -0.819  -7.036  59.103  1.00 16.47 ? 99  PHE   A N   1 
ATOM   517  C  CA  . PHE   A 1 71  ? -2.114  -7.698  59.251  1.00 16.48 ? 99  PHE   A CA  1 
ATOM   518  C  C   . PHE   A 1 71  ? -2.276  -8.686  58.109  1.00 14.72 ? 99  PHE   A C   1 
ATOM   519  O  O   . PHE   A 1 71  ? -2.225  -8.298  56.941  1.00 16.36 ? 99  PHE   A O   1 
ATOM   520  C  CB  . PHE   A 1 71  ? -3.263  -6.676  59.266  1.00 15.21 ? 99  PHE   A CB  1 
ATOM   521  C  CG  . PHE   A 1 71  ? -3.100  -5.613  60.323  1.00 14.30 ? 99  PHE   A CG  1 
ATOM   522  C  CD1 . PHE   A 1 71  ? -2.309  -4.500  60.083  1.00 13.44 ? 99  PHE   A CD1 1 
ATOM   523  C  CD2 . PHE   A 1 71  ? -3.685  -5.761  61.573  1.00 12.54 ? 99  PHE   A CD2 1 
ATOM   524  C  CE1 . PHE   A 1 71  ? -2.142  -3.541  61.054  1.00 14.31 ? 99  PHE   A CE1 1 
ATOM   525  C  CE2 . PHE   A 1 71  ? -3.515  -4.808  62.558  1.00 11.05 ? 99  PHE   A CE2 1 
ATOM   526  C  CZ  . PHE   A 1 71  ? -2.755  -3.700  62.302  1.00 15.35 ? 99  PHE   A CZ  1 
ATOM   527  N  N   . THR   A 1 72  ? -2.455  -9.955  58.443  1.00 13.94 ? 100 THR   A N   1 
ATOM   528  C  CA  . THR   A 1 72  ? -2.489  -11.024 57.451  1.00 14.18 ? 100 THR   A CA  1 
ATOM   529  C  C   . THR   A 1 72  ? -3.723  -11.900 57.656  1.00 13.97 ? 100 THR   A C   1 
ATOM   530  O  O   . THR   A 1 72  ? -4.059  -12.239 58.790  1.00 15.45 ? 100 THR   A O   1 
ATOM   531  C  CB  . THR   A 1 72  ? -1.210  -11.877 57.544  1.00 13.11 ? 100 THR   A CB  1 
ATOM   532  O  OG1 . THR   A 1 72  ? -0.062  -11.064 57.223  1.00 12.77 ? 100 THR   A OG1 1 
ATOM   533  C  CG2 . THR   A 1 72  ? -1.290  -13.083 56.612  1.00 14.10 ? 100 THR   A CG2 1 
ATOM   534  N  N   . ALA   A 1 73  ? -4.382  -12.275 56.558  1.00 13.68 ? 101 ALA   A N   1 
ATOM   535  C  CA  . ALA   A 1 73  ? -5.503  -13.213 56.528  1.00 13.99 ? 101 ALA   A CA  1 
ATOM   536  C  C   . ALA   A 1 73  ? -5.338  -14.157 55.345  1.00 16.69 ? 101 ALA   A C   1 
ATOM   537  O  O   . ALA   A 1 73  ? -4.731  -13.780 54.335  1.00 15.79 ? 101 ALA   A O   1 
ATOM   538  C  CB  . ALA   A 1 73  ? -6.861  -12.496 56.398  1.00 13.03 ? 101 ALA   A CB  1 
ATOM   539  N  N   . PRO   A 1 74  ? -5.888  -15.376 55.424  1.00 18.51 ? 102 PRO   A N   1 
ATOM   540  C  CA  . PRO   A 1 74  ? -5.797  -16.299 54.281  1.00 18.43 ? 102 PRO   A CA  1 
ATOM   541  C  C   . PRO   A 1 74  ? -6.908  -16.086 53.266  1.00 18.01 ? 102 PRO   A C   1 
ATOM   542  O  O   . PRO   A 1 74  ? -8.052  -15.803 53.617  1.00 20.62 ? 102 PRO   A O   1 
ATOM   543  C  CB  . PRO   A 1 74  ? -5.929  -17.680 54.943  1.00 19.49 ? 102 PRO   A CB  1 
ATOM   544  C  CG  . PRO   A 1 74  ? -6.812  -17.446 56.150  1.00 20.30 ? 102 PRO   A CG  1 
ATOM   545  C  CD  . PRO   A 1 74  ? -6.532  -16.001 56.602  1.00 18.06 ? 102 PRO   A CD  1 
ATOM   546  N  N   . TYR   A 1 75  ? -6.561  -16.232 51.983  1.00 19.75 ? 103 TYR   A N   1 
ATOM   547  C  CA  . TYR   A 1 75  ? -7.542  -16.404 50.911  1.00 18.87 ? 103 TYR   A CA  1 
ATOM   548  C  C   . TYR   A 1 75  ? -8.115  -17.817 50.934  1.00 18.26 ? 103 TYR   A C   1 
ATOM   549  O  O   . TYR   A 1 75  ? -7.691  -18.673 51.712  1.00 20.30 ? 103 TYR   A O   1 
ATOM   550  C  CB  . TYR   A 1 75  ? -6.913  -16.139 49.542  1.00 19.76 ? 103 TYR   A CB  1 
ATOM   551  C  CG  . TYR   A 1 75  ? -6.525  -14.699 49.289  1.00 18.68 ? 103 TYR   A CG  1 
ATOM   552  C  CD1 . TYR   A 1 75  ? -7.422  -13.666 49.533  1.00 16.20 ? 103 TYR   A CD1 1 
ATOM   553  C  CD2 . TYR   A 1 75  ? -5.254  -14.374 48.801  1.00 18.78 ? 103 TYR   A CD2 1 
ATOM   554  C  CE1 . TYR   A 1 75  ? -7.074  -12.322 49.300  1.00 15.81 ? 103 TYR   A CE1 1 
ATOM   555  C  CE2 . TYR   A 1 75  ? -4.890  -13.048 48.569  1.00 18.19 ? 103 TYR   A CE2 1 
ATOM   556  C  CZ  . TYR   A 1 75  ? -5.811  -12.024 48.822  1.00 18.62 ? 103 TYR   A CZ  1 
ATOM   557  O  OH  . TYR   A 1 75  ? -5.461  -10.711 48.579  1.00 18.02 ? 103 TYR   A OH  1 
ATOM   558  N  N   . SER   A 1 76  ? -9.089  -18.078 50.065  1.00 20.54 ? 104 SER   A N   1 
ATOM   559  C  CA  . SER   A 1 76  ? -9.529  -19.457 49.846  1.00 20.58 ? 104 SER   A CA  1 
ATOM   560  C  C   . SER   A 1 76  ? -8.352  -20.331 49.410  1.00 21.20 ? 104 SER   A C   1 
ATOM   561  O  O   . SER   A 1 76  ? -7.604  -19.949 48.497  1.00 19.47 ? 104 SER   A O   1 
ATOM   562  C  CB  . SER   A 1 76  ? -10.625 -19.539 48.785  1.00 20.53 ? 104 SER   A CB  1 
ATOM   563  O  OG  . SER   A 1 76  ? -10.908 -20.908 48.498  1.00 20.92 ? 104 SER   A OG  1 
ATOM   564  N  N   . PRO   A 1 77  ? -8.152  -21.500 50.021  1.00 23.27 ? 105 PRO   A N   1 
ATOM   565  C  CA  . PRO   A 1 77  ? -7.069  -22.372 49.547  1.00 21.98 ? 105 PRO   A CA  1 
ATOM   566  C  C   . PRO   A 1 77  ? -7.200  -22.728 48.073  1.00 23.89 ? 105 PRO   A C   1 
ATOM   567  O  O   . PRO   A 1 77  ? -6.183  -22.975 47.411  1.00 21.53 ? 105 PRO   A O   1 
ATOM   568  C  CB  . PRO   A 1 77  ? -7.197  -23.603 50.459  1.00 23.15 ? 105 PRO   A CB  1 
ATOM   569  C  CG  . PRO   A 1 77  ? -7.790  -23.041 51.721  1.00 21.33 ? 105 PRO   A CG  1 
ATOM   570  C  CD  . PRO   A 1 77  ? -8.805  -22.039 51.225  1.00 19.51 ? 105 PRO   A CD  1 
ATOM   571  N  N   . SER   A 1 78  ? -8.422  -22.702 47.525  1.00 20.22 ? 106 SER   A N   1 
ATOM   572  C  CA  . SER   A 1 78  ? -8.624  -23.075 46.130  1.00 21.92 ? 106 SER   A CA  1 
ATOM   573  C  C   . SER   A 1 78  ? -7.839  -22.187 45.184  1.00 25.12 ? 106 SER   A C   1 
ATOM   574  O  O   . SER   A 1 78  ? -7.460  -22.640 44.096  1.00 26.81 ? 106 SER   A O   1 
ATOM   575  C  CB  . SER   A 1 78  ? -10.115 -23.043 45.775  1.00 23.28 ? 106 SER   A CB  1 
ATOM   576  O  OG  . SER   A 1 78  ? -10.657 -21.761 45.997  1.00 23.36 ? 106 SER   A OG  1 
ATOM   577  N  N   . LEU   A 1 79  ? -7.562  -20.934 45.575  1.00 20.15 ? 107 LEU   A N   1 
ATOM   578  C  CA  . LEU   A 1 79  ? -6.836  -20.045 44.670  1.00 21.02 ? 107 LEU   A CA  1 
ATOM   579  C  C   . LEU   A 1 79  ? -5.398  -20.500 44.450  1.00 22.00 ? 107 LEU   A C   1 
ATOM   580  O  O   . LEU   A 1 79  ? -4.804  -20.165 43.423  1.00 22.76 ? 107 LEU   A O   1 
ATOM   581  C  CB  . LEU   A 1 79  ? -6.822  -18.610 45.196  1.00 19.02 ? 107 LEU   A CB  1 
ATOM   582  C  CG  . LEU   A 1 79  ? -8.112  -17.913 45.578  1.00 18.98 ? 107 LEU   A CG  1 
ATOM   583  C  CD1 . LEU   A 1 79  ? -7.806  -16.424 45.813  1.00 14.96 ? 107 LEU   A CD1 1 
ATOM   584  C  CD2 . LEU   A 1 79  ? -9.146  -18.111 44.502  1.00 16.45 ? 107 LEU   A CD2 1 
ATOM   585  N  N   . SER   A 1 80  ? -4.815  -21.231 45.405  1.00 27.03 ? 108 SER   A N   1 
ATOM   586  C  CA  . SER   A 1 80  ? -3.429  -21.688 45.322  1.00 22.56 ? 108 SER   A CA  1 
ATOM   587  C  C   . SER   A 1 80  ? -3.327  -23.209 45.364  1.00 26.14 ? 108 SER   A C   1 
ATOM   588  O  O   . SER   A 1 80  ? -2.277  -23.743 45.723  1.00 27.41 ? 108 SER   A O   1 
ATOM   589  C  CB  . SER   A 1 80  ? -2.595  -21.082 46.453  1.00 20.73 ? 108 SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 80  ? -3.167  -21.422 47.712  1.00 22.26 ? 108 SER   A OG  1 
ATOM   591  N  N   . ALA   A 1 81  ? -4.401  -23.916 45.006  1.00 26.08 ? 109 ALA   A N   1 
ATOM   592  C  CA  . ALA   A 1 81  ? -4.422  -25.366 45.154  1.00 30.28 ? 109 ALA   A CA  1 
ATOM   593  C  C   . ALA   A 1 81  ? -3.361  -26.050 44.294  1.00 31.57 ? 109 ALA   A C   1 
ATOM   594  O  O   . ALA   A 1 81  ? -2.866  -27.121 44.664  1.00 31.33 ? 109 ALA   A O   1 
ATOM   595  C  CB  . ALA   A 1 81  ? -5.814  -25.906 44.811  1.00 24.23 ? 109 ALA   A CB  1 
ATOM   596  N  N   . GLY   A 1 82  ? -2.999  -25.455 43.156  1.00 29.50 ? 110 GLY   A N   1 
ATOM   597  C  CA  . GLY   A 1 82  ? -1.972  -26.033 42.315  1.00 31.75 ? 110 GLY   A CA  1 
ATOM   598  C  C   . GLY   A 1 82  ? -0.554  -25.699 42.719  1.00 35.29 ? 110 GLY   A C   1 
ATOM   599  O  O   . GLY   A 1 82  ? 0.394   -26.231 42.130  1.00 33.95 ? 110 GLY   A O   1 
ATOM   600  N  N   . GLU   A 1 83  ? -0.381  -24.834 43.709  1.00 29.61 ? 111 GLU   A N   1 
ATOM   601  C  CA  . GLU   A 1 83  ? 0.952   -24.446 44.136  1.00 27.44 ? 111 GLU   A CA  1 
ATOM   602  C  C   . GLU   A 1 83  ? 1.553   -25.505 45.056  1.00 27.88 ? 111 GLU   A C   1 
ATOM   603  O  O   . GLU   A 1 83  ? 0.844   -26.266 45.722  1.00 27.34 ? 111 GLU   A O   1 
ATOM   604  C  CB  . GLU   A 1 83  ? 0.924   -23.087 44.853  1.00 25.80 ? 111 GLU   A CB  1 
ATOM   605  C  CG  . GLU   A 1 83  ? 0.514   -21.907 43.966  1.00 22.22 ? 111 GLU   A CG  1 
ATOM   606  C  CD  . GLU   A 1 83  ? 0.491   -20.567 44.711  1.00 25.33 ? 111 GLU   A CD  1 
ATOM   607  O  OE1 . GLU   A 1 83  ? -0.090  -19.591 44.184  1.00 20.85 ? 111 GLU   A OE1 1 
ATOM   608  O  OE2 . GLU   A 1 83  ? 1.046   -20.493 45.827  1.00 22.85 ? 111 GLU   A OE2 1 
ATOM   609  N  N   . ILE   A 1 84  ? 2.883   -25.554 45.074  1.00 22.76 ? 112 ILE   A N   1 
ATOM   610  C  CA  . ILE   A 1 84  ? 3.626   -26.239 46.118  1.00 26.29 ? 112 ILE   A CA  1 
ATOM   611  C  C   . ILE   A 1 84  ? 4.602   -25.228 46.699  1.00 24.55 ? 112 ILE   A C   1 
ATOM   612  O  O   . ILE   A 1 84  ? 4.788   -24.137 46.156  1.00 26.44 ? 112 ILE   A O   1 
ATOM   613  C  CB  . ILE   A 1 84  ? 4.347   -27.499 45.601  1.00 26.37 ? 112 ILE   A CB  1 
ATOM   614  C  CG1 . ILE   A 1 84  ? 5.202   -27.172 44.363  1.00 26.15 ? 112 ILE   A CG1 1 
ATOM   615  C  CG2 . ILE   A 1 84  ? 3.317   -28.571 45.289  1.00 21.99 ? 112 ILE   A CG2 1 
ATOM   616  C  CD1 . ILE   A 1 84  ? 6.216   -28.291 43.978  1.00 26.42 ? 112 ILE   A CD1 1 
ATOM   617  N  N   . LYS   A 1 85  ? 5.208   -25.578 47.835  1.00 21.90 ? 113 LYS   A N   1 
ATOM   618  C  CA  . LYS   A 1 85  ? 6.120   -24.624 48.463  1.00 28.70 ? 113 LYS   A CA  1 
ATOM   619  C  C   . LYS   A 1 85  ? 7.195   -24.133 47.502  1.00 26.32 ? 113 LYS   A C   1 
ATOM   620  O  O   . LYS   A 1 85  ? 7.417   -22.915 47.446  1.00 24.71 ? 113 LYS   A O   1 
ATOM   621  C  CB  . LYS   A 1 85  ? 6.734   -25.231 49.735  1.00 24.69 ? 113 LYS   A CB  1 
ATOM   622  C  CG  . LYS   A 1 85  ? 5.804   -25.117 50.929  1.00 26.44 ? 113 LYS   A CG  1 
ATOM   623  C  CD  A LYS   A 1 85  ? 6.463   -25.682 52.177  0.19 31.11 ? 113 LYS   A CD  1 
ATOM   624  C  CD  B LYS   A 1 85  ? 6.434   -25.539 52.237  0.81 31.12 ? 113 LYS   A CD  1 
ATOM   625  C  CE  A LYS   A 1 85  ? 5.733   -25.248 53.437  0.19 31.23 ? 113 LYS   A CE  1 
ATOM   626  C  CE  B LYS   A 1 85  ? 5.394   -25.482 53.364  0.81 30.71 ? 113 LYS   A CE  1 
ATOM   627  N  NZ  A LYS   A 1 85  ? 5.859   -23.784 53.662  0.19 31.22 ? 113 LYS   A NZ  1 
ATOM   628  N  NZ  B LYS   A 1 85  ? 5.975   -25.807 54.699  0.81 33.75 ? 113 LYS   A NZ  1 
ATOM   629  N  N   . PRO   A 1 86  ? 7.847   -24.984 46.699  1.00 25.89 ? 114 PRO   A N   1 
ATOM   630  C  CA  . PRO   A 1 86  ? 8.776   -24.460 45.682  1.00 29.61 ? 114 PRO   A CA  1 
ATOM   631  C  C   . PRO   A 1 86  ? 8.166   -23.486 44.682  1.00 28.88 ? 114 PRO   A C   1 
ATOM   632  O  O   . PRO   A 1 86  ? 8.916   -22.679 44.118  1.00 31.33 ? 114 PRO   A O   1 
ATOM   633  C  CB  . PRO   A 1 86  ? 9.271   -25.735 44.980  1.00 27.68 ? 114 PRO   A CB  1 
ATOM   634  C  CG  . PRO   A 1 86  ? 9.193   -26.777 46.015  1.00 29.66 ? 114 PRO   A CG  1 
ATOM   635  C  CD  . PRO   A 1 86  ? 7.942   -26.453 46.804  1.00 25.68 ? 114 PRO   A CD  1 
ATOM   636  N  N   . THR   A 1 87  ? 6.852   -23.533 44.423  1.00 26.52 ? 115 THR   A N   1 
ATOM   637  C  CA  . THR   A 1 87  ? 6.232   -22.642 43.441  1.00 26.78 ? 115 THR   A CA  1 
ATOM   638  C  C   . THR   A 1 87  ? 5.289   -21.621 44.084  1.00 26.35 ? 115 THR   A C   1 
ATOM   639  O  O   . THR   A 1 87  ? 4.440   -21.044 43.391  1.00 26.13 ? 115 THR   A O   1 
ATOM   640  C  CB  . THR   A 1 87  ? 5.479   -23.443 42.365  1.00 24.73 ? 115 THR   A CB  1 
ATOM   641  O  OG1 . THR   A 1 87  ? 4.332   -24.090 42.933  1.00 22.79 ? 115 THR   A OG1 1 
ATOM   642  C  CG2 . THR   A 1 87  ? 6.383   -24.495 41.701  1.00 23.55 ? 115 THR   A CG2 1 
ATOM   643  N  N   . THR   A 1 88  ? 5.425   -21.377 45.388  1.00 24.32 ? 116 THR   A N   1 
ATOM   644  C  CA  . THR   A 1 88  ? 4.417   -20.617 46.121  1.00 25.25 ? 116 THR   A CA  1 
ATOM   645  C  C   . THR   A 1 88  ? 4.410   -19.151 45.692  1.00 23.05 ? 116 THR   A C   1 
ATOM   646  O  O   . THR   A 1 88  ? 5.441   -18.582 45.331  1.00 20.87 ? 116 THR   A O   1 
ATOM   647  C  CB  . THR   A 1 88  ? 4.661   -20.704 47.626  1.00 23.49 ? 116 THR   A CB  1 
ATOM   648  O  OG1 . THR   A 1 88  ? 3.569   -20.093 48.311  1.00 24.21 ? 116 THR   A OG1 1 
ATOM   649  C  CG2 . THR   A 1 88  ? 5.947   -19.975 48.012  1.00 24.40 ? 116 THR   A CG2 1 
ATOM   650  N  N   . THR   A 1 89  ? 3.219   -18.551 45.710  1.00 24.37 ? 117 THR   A N   1 
ATOM   651  C  CA  . THR   A 1 89  ? 3.052   -17.117 45.502  1.00 23.06 ? 117 THR   A CA  1 
ATOM   652  C  C   . THR   A 1 89  ? 2.943   -16.350 46.811  1.00 24.42 ? 117 THR   A C   1 
ATOM   653  O  O   . THR   A 1 89  ? 2.732   -15.131 46.785  1.00 22.30 ? 117 THR   A O   1 
ATOM   654  C  CB  . THR   A 1 89  ? 1.809   -16.827 44.657  1.00 25.08 ? 117 THR   A CB  1 
ATOM   655  O  OG1 . THR   A 1 89  ? 0.683   -17.508 45.218  1.00 19.76 ? 117 THR   A OG1 1 
ATOM   656  C  CG2 . THR   A 1 89  ? 2.010   -17.263 43.198  1.00 24.05 ? 117 THR   A CG2 1 
ATOM   657  N  N   . ALA   A 1 90  ? 3.047   -17.034 47.948  1.00 21.98 ? 118 ALA   A N   1 
ATOM   658  C  CA  . ALA   A 1 90  ? 2.987   -16.351 49.230  1.00 20.24 ? 118 ALA   A CA  1 
ATOM   659  C  C   . ALA   A 1 90  ? 4.261   -15.545 49.437  1.00 23.56 ? 118 ALA   A C   1 
ATOM   660  O  O   . ALA   A 1 90  ? 5.360   -16.005 49.129  1.00 24.54 ? 118 ALA   A O   1 
ATOM   661  C  CB  . ALA   A 1 90  ? 2.812   -17.363 50.357  1.00 20.10 ? 118 ALA   A CB  1 
ATOM   662  N  N   . SER   A 1 91  ? 4.120   -14.331 49.948  1.00 21.08 ? 119 SER   A N   1 
ATOM   663  C  CA  . SER   A 1 91  ? 5.307   -13.529 50.203  1.00 23.14 ? 119 SER   A CA  1 
ATOM   664  C  C   . SER   A 1 91  ? 5.930   -13.841 51.553  1.00 22.34 ? 119 SER   A C   1 
ATOM   665  O  O   . SER   A 1 91  ? 7.083   -13.469 51.792  1.00 21.04 ? 119 SER   A O   1 
ATOM   666  C  CB  . SER   A 1 91  ? 4.971   -12.034 50.110  1.00 21.08 ? 119 SER   A CB  1 
ATOM   667  O  OG  . SER   A 1 91  ? 3.732   -11.773 50.740  1.00 19.58 ? 119 SER   A OG  1 
ATOM   668  N  N   . ILE   A 1 92  ? 5.197   -14.508 52.432  1.00 19.51 ? 120 ILE   A N   1 
ATOM   669  C  CA  . ILE   A 1 92  ? 5.698   -14.941 53.728  1.00 20.99 ? 120 ILE   A CA  1 
ATOM   670  C  C   . ILE   A 1 92  ? 5.664   -16.463 53.758  1.00 21.72 ? 120 ILE   A C   1 
ATOM   671  O  O   . ILE   A 1 92  ? 4.601   -17.069 53.923  1.00 20.76 ? 120 ILE   A O   1 
ATOM   672  C  CB  . ILE   A 1 92  ? 4.884   -14.330 54.879  1.00 21.58 ? 120 ILE   A CB  1 
ATOM   673  C  CG1 . ILE   A 1 92  ? 5.007   -12.798 54.820  1.00 15.31 ? 120 ILE   A CG1 1 
ATOM   674  C  CG2 . ILE   A 1 92  ? 5.372   -14.871 56.235  1.00 19.86 ? 120 ILE   A CG2 1 
ATOM   675  C  CD1 . ILE   A 1 92  ? 4.194   -12.097 55.870  1.00 21.18 ? 120 ILE   A CD1 1 
ATOM   676  N  N   . PRO   A 1 93  ? 6.808   -17.118 53.563  1.00 23.34 ? 121 PRO   A N   1 
ATOM   677  C  CA  . PRO   A 1 93  ? 6.791   -18.569 53.304  1.00 23.14 ? 121 PRO   A CA  1 
ATOM   678  C  C   . PRO   A 1 93  ? 6.409   -19.405 54.510  1.00 24.32 ? 121 PRO   A C   1 
ATOM   679  O  O   . PRO   A 1 93  ? 5.960   -20.543 54.323  1.00 24.34 ? 121 PRO   A O   1 
ATOM   680  C  CB  . PRO   A 1 93  ? 8.226   -18.864 52.835  1.00 29.34 ? 121 PRO   A CB  1 
ATOM   681  C  CG  . PRO   A 1 93  ? 9.052   -17.677 53.291  1.00 25.24 ? 121 PRO   A CG  1 
ATOM   682  C  CD  . PRO   A 1 93  ? 8.123   -16.501 53.293  1.00 23.00 ? 121 PRO   A CD  1 
ATOM   683  N  N   . SER   A 1 94  ? 6.540   -18.877 55.732  1.00 21.04 ? 122 SER   A N   1 
ATOM   684  C  CA  . SER   A 1 94  ? 5.996   -19.559 56.901  1.00 21.59 ? 122 SER   A CA  1 
ATOM   685  C  C   . SER   A 1 94  ? 4.465   -19.619 56.928  1.00 19.97 ? 122 SER   A C   1 
ATOM   686  O  O   . SER   A 1 94  ? 3.913   -20.374 57.737  1.00 21.39 ? 122 SER   A O   1 
ATOM   687  C  CB  . SER   A 1 94  ? 6.494   -18.878 58.171  1.00 20.94 ? 122 SER   A CB  1 
ATOM   688  O  OG  . SER   A 1 94  ? 5.918   -17.585 58.294  1.00 24.20 ? 122 SER   A OG  1 
ATOM   689  N  N   . PHE   A 1 95  ? 3.758   -18.852 56.096  1.00 19.30 ? 123 PHE   A N   1 
ATOM   690  C  CA  . PHE   A 1 95  ? 2.303   -18.825 56.217  1.00 20.45 ? 123 PHE   A CA  1 
ATOM   691  C  C   . PHE   A 1 95  ? 1.676   -20.163 55.824  1.00 23.48 ? 123 PHE   A C   1 
ATOM   692  O  O   . PHE   A 1 95  ? 2.124   -20.852 54.899  1.00 23.76 ? 123 PHE   A O   1 
ATOM   693  C  CB  . PHE   A 1 95  ? 1.690   -17.718 55.362  1.00 15.79 ? 123 PHE   A CB  1 
ATOM   694  C  CG  . PHE   A 1 95  ? 0.184   -17.634 55.476  1.00 19.23 ? 123 PHE   A CG  1 
ATOM   695  C  CD1 . PHE   A 1 95  ? -0.406  -16.856 56.457  1.00 17.17 ? 123 PHE   A CD1 1 
ATOM   696  C  CD2 . PHE   A 1 95  ? -0.646  -18.359 54.611  1.00 21.97 ? 123 PHE   A CD2 1 
ATOM   697  C  CE1 . PHE   A 1 95  ? -1.806  -16.777 56.566  1.00 18.30 ? 123 PHE   A CE1 1 
ATOM   698  C  CE2 . PHE   A 1 95  ? -2.031  -18.297 54.717  1.00 21.29 ? 123 PHE   A CE2 1 
ATOM   699  C  CZ  . PHE   A 1 95  ? -2.616  -17.500 55.697  1.00 19.13 ? 123 PHE   A CZ  1 
ATOM   700  N  N   . ASP   A 1 96  ? 0.593   -20.508 56.513  1.00 21.61 ? 124 ASP   A N   1 
ATOM   701  C  CA  . ASP   A 1 96  ? -0.119  -21.752 56.231  1.00 23.79 ? 124 ASP   A CA  1 
ATOM   702  C  C   . ASP   A 1 96  ? -1.608  -21.556 56.487  1.00 20.75 ? 124 ASP   A C   1 
ATOM   703  O  O   . ASP   A 1 96  ? -1.983  -21.208 57.612  1.00 20.91 ? 124 ASP   A O   1 
ATOM   704  C  CB  . ASP   A 1 96  ? 0.444   -22.876 57.098  1.00 23.34 ? 124 ASP   A CB  1 
ATOM   705  C  CG  . ASP   A 1 96  ? -0.329  -24.164 56.949  1.00 25.75 ? 124 ASP   A CG  1 
ATOM   706  O  OD1 . ASP   A 1 96  ? -0.029  -24.930 56.007  1.00 34.74 ? 124 ASP   A OD1 1 
ATOM   707  O  OD2 . ASP   A 1 96  ? -1.220  -24.413 57.786  1.00 25.05 ? 124 ASP   A OD2 1 
ATOM   708  N  N   . HIS   A 1 97  ? -2.444  -21.753 55.452  1.00 20.16 ? 125 HIS   A N   1 
ATOM   709  C  CA  . HIS   A 1 97  ? -3.893  -21.560 55.607  1.00 24.48 ? 125 HIS   A CA  1 
ATOM   710  C  C   . HIS   A 1 97  ? -4.406  -22.244 56.869  1.00 22.00 ? 125 HIS   A C   1 
ATOM   711  O  O   . HIS   A 1 97  ? -5.096  -21.627 57.685  1.00 21.46 ? 125 HIS   A O   1 
ATOM   712  C  CB  . HIS   A 1 97  ? -4.680  -22.102 54.397  1.00 20.83 ? 125 HIS   A CB  1 
ATOM   713  C  CG  . HIS   A 1 97  ? -4.387  -21.417 53.100  1.00 27.24 ? 125 HIS   A CG  1 
ATOM   714  N  ND1 . HIS   A 1 97  ? -5.013  -20.247 52.715  1.00 26.49 ? 125 HIS   A ND1 1 
ATOM   715  C  CD2 . HIS   A 1 97  ? -3.583  -21.770 52.067  1.00 24.22 ? 125 HIS   A CD2 1 
ATOM   716  C  CE1 . HIS   A 1 97  ? -4.579  -19.890 51.520  1.00 22.25 ? 125 HIS   A CE1 1 
ATOM   717  N  NE2 . HIS   A 1 97  ? -3.710  -20.798 51.106  1.00 29.27 ? 125 HIS   A NE2 1 
ATOM   718  N  N   . GLY   A 1 98  ? -4.071  -23.529 57.041  1.00 20.87 ? 126 GLY   A N   1 
ATOM   719  C  CA  . GLY   A 1 98  ? -4.595  -24.283 58.171  1.00 19.02 ? 126 GLY   A CA  1 
ATOM   720  C  C   . GLY   A 1 98  ? -4.148  -23.727 59.511  1.00 20.60 ? 126 GLY   A C   1 
ATOM   721  O  O   . GLY   A 1 98  ? -4.963  -23.551 60.422  1.00 19.78 ? 126 GLY   A O   1 
ATOM   722  N  N   . SER   A 1 99  ? -2.845  -23.440 59.650  1.00 17.44 ? 127 SER   A N   1 
ATOM   723  C  CA  . SER   A 1 99  ? -2.355  -22.827 60.884  1.00 15.08 ? 127 SER   A CA  1 
ATOM   724  C  C   . SER   A 1 99  ? -3.050  -21.490 61.160  1.00 19.47 ? 127 SER   A C   1 
ATOM   725  O  O   . SER   A 1 99  ? -3.411  -21.191 62.306  1.00 19.11 ? 127 SER   A O   1 
ATOM   726  C  CB  . SER   A 1 99  ? -0.837  -22.621 60.819  1.00 22.59 ? 127 SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 99  ? -0.120  -23.831 60.647  1.00 24.53 ? 127 SER   A OG  1 
ATOM   728  N  N   . CYS   A 1 100 ? -3.243  -20.669 60.124  1.00 18.91 ? 128 CYS   A N   1 
ATOM   729  C  CA  . CYS   A 1 100 ? -3.826  -19.348 60.326  1.00 19.29 ? 128 CYS   A CA  1 
ATOM   730  C  C   . CYS   A 1 100 ? -5.300  -19.446 60.733  1.00 18.73 ? 128 CYS   A C   1 
ATOM   731  O  O   . CYS   A 1 100 ? -5.728  -18.815 61.707  1.00 16.43 ? 128 CYS   A O   1 
ATOM   732  C  CB  . CYS   A 1 100 ? -3.661  -18.505 59.059  1.00 16.81 ? 128 CYS   A CB  1 
ATOM   733  S  SG  . CYS   A 1 100 ? -4.268  -16.786 59.245  1.00 16.99 ? 128 CYS   A SG  1 
ATOM   734  N  N   . ARG   A 1 101 ? -6.095  -20.220 59.990  1.00 18.64 ? 129 ARG   A N   1 
ATOM   735  C  CA  . ARG   A 1 101 ? -7.493  -20.418 60.370  1.00 21.32 ? 129 ARG   A CA  1 
ATOM   736  C  C   . ARG   A 1 101 ? -7.610  -20.993 61.776  1.00 22.62 ? 129 ARG   A C   1 
ATOM   737  O  O   . ARG   A 1 101 ? -8.418  -20.520 62.578  1.00 21.07 ? 129 ARG   A O   1 
ATOM   738  C  CB  . ARG   A 1 101 ? -8.191  -21.329 59.359  1.00 22.21 ? 129 ARG   A CB  1 
ATOM   739  C  CG  . ARG   A 1 101 ? -8.327  -20.647 58.020  1.00 24.06 ? 129 ARG   A CG  1 
ATOM   740  C  CD  . ARG   A 1 101 ? -9.446  -21.217 57.157  1.00 30.17 ? 129 ARG   A CD  1 
ATOM   741  N  NE  . ARG   A 1 101 ? -9.850  -20.200 56.184  1.00 33.91 ? 129 ARG   A NE  1 
ATOM   742  C  CZ  . ARG   A 1 101 ? -9.250  -19.997 55.012  1.00 32.12 ? 129 ARG   A CZ  1 
ATOM   743  N  NH1 . ARG   A 1 101 ? -8.222  -20.755 54.628  1.00 32.72 ? 129 ARG   A NH1 1 
ATOM   744  N  NH2 . ARG   A 1 101 ? -9.675  -19.036 54.218  1.00 25.48 ? 129 ARG   A NH2 1 
ATOM   745  N  N   . SER   A 1 102 ? -6.777  -21.988 62.103  1.00 22.26 ? 130 SER   A N   1 
ATOM   746  C  CA  . SER   A 1 102 ? -6.814  -22.592 63.432  1.00 21.67 ? 130 SER   A CA  1 
ATOM   747  C  C   . SER   A 1 102 ? -6.456  -21.570 64.511  1.00 22.42 ? 130 SER   A C   1 
ATOM   748  O  O   . SER   A 1 102 ? -7.152  -21.459 65.528  1.00 21.99 ? 130 SER   A O   1 
ATOM   749  C  CB  . SER   A 1 102 ? -5.872  -23.802 63.468  1.00 23.68 ? 130 SER   A CB  1 
ATOM   750  O  OG  . SER   A 1 102 ? -5.881  -24.430 64.732  1.00 33.54 ? 130 SER   A OG  1 
ATOM   751  N  N   . PHE   A 1 103 ? -5.380  -20.800 64.298  1.00 21.65 ? 131 PHE   A N   1 
ATOM   752  C  CA  . PHE   A 1 103 ? -4.996  -19.767 65.260  1.00 17.47 ? 131 PHE   A CA  1 
ATOM   753  C  C   . PHE   A 1 103 ? -6.160  -18.831 65.548  1.00 18.13 ? 131 PHE   A C   1 
ATOM   754  O  O   . PHE   A 1 103 ? -6.516  -18.613 66.709  1.00 18.80 ? 131 PHE   A O   1 
ATOM   755  C  CB  . PHE   A 1 103 ? -3.786  -18.986 64.727  1.00 17.10 ? 131 PHE   A CB  1 
ATOM   756  C  CG  . PHE   A 1 103 ? -3.355  -17.812 65.590  1.00 16.16 ? 131 PHE   A CG  1 
ATOM   757  C  CD1 . PHE   A 1 103 ? -4.050  -16.601 65.553  1.00 16.38 ? 131 PHE   A CD1 1 
ATOM   758  C  CD2 . PHE   A 1 103 ? -2.232  -17.906 66.392  1.00 15.60 ? 131 PHE   A CD2 1 
ATOM   759  C  CE1 . PHE   A 1 103 ? -3.647  -15.525 66.342  1.00 19.35 ? 131 PHE   A CE1 1 
ATOM   760  C  CE2 . PHE   A 1 103 ? -1.819  -16.839 67.175  1.00 15.60 ? 131 PHE   A CE2 1 
ATOM   761  C  CZ  . PHE   A 1 103 ? -2.521  -15.652 67.153  1.00 17.99 ? 131 PHE   A CZ  1 
ATOM   762  N  N   . PHE   A 1 104 ? -6.761  -18.261 64.498  1.00 18.22 ? 132 PHE   A N   1 
ATOM   763  C  CA  . PHE   A 1 104 ? -7.770  -17.221 64.692  1.00 18.89 ? 132 PHE   A CA  1 
ATOM   764  C  C   . PHE   A 1 104 ? -9.045  -17.796 65.294  1.00 23.86 ? 132 PHE   A C   1 
ATOM   765  O  O   . PHE   A 1 104 ? -9.699  -17.145 66.116  1.00 20.10 ? 132 PHE   A O   1 
ATOM   766  C  CB  . PHE   A 1 104 ? -8.086  -16.541 63.369  1.00 17.52 ? 132 PHE   A CB  1 
ATOM   767  C  CG  . PHE   A 1 104 ? -8.948  -15.300 63.492  1.00 21.01 ? 132 PHE   A CG  1 
ATOM   768  C  CD1 . PHE   A 1 104 ? -10.335 -15.391 63.576  1.00 24.73 ? 132 PHE   A CD1 1 
ATOM   769  C  CD2 . PHE   A 1 104 ? -8.374  -14.032 63.485  1.00 17.27 ? 132 PHE   A CD2 1 
ATOM   770  C  CE1 . PHE   A 1 104 ? -11.130 -14.218 63.675  1.00 28.40 ? 132 PHE   A CE1 1 
ATOM   771  C  CE2 . PHE   A 1 104 ? -9.177  -12.846 63.575  1.00 21.96 ? 132 PHE   A CE2 1 
ATOM   772  C  CZ  . PHE   A 1 104 ? -10.532 -12.923 63.642  1.00 12.72 ? 132 PHE   A CZ  1 
ATOM   773  N  N   . SER   A 1 105 ? -9.422  -19.002 64.878  1.00 18.86 ? 133 SER   A N   1 
ATOM   774  C  CA  . SER   A 1 105 ? -10.620 -19.624 65.422  1.00 24.26 ? 133 SER   A CA  1 
ATOM   775  C  C   . SER   A 1 105 ? -10.411 -20.027 66.873  1.00 21.18 ? 133 SER   A C   1 
ATOM   776  O  O   . SER   A 1 105 ? -11.363 -20.051 67.654  1.00 22.95 ? 133 SER   A O   1 
ATOM   777  C  CB  . SER   A 1 105 ? -11.005 -20.841 64.583  1.00 21.99 ? 133 SER   A CB  1 
ATOM   778  O  OG  . SER   A 1 105 ? -10.794 -22.007 65.345  1.00 29.90 ? 133 SER   A OG  1 
ATOM   779  N  N   . SER   A 1 106 ? -9.171  -20.311 67.260  1.00 19.85 ? 134 SER   A N   1 
ATOM   780  C  CA  . SER   A 1 106 ? -8.898  -20.650 68.649  1.00 22.02 ? 134 SER   A CA  1 
ATOM   781  C  C   . SER   A 1 106 ? -8.742  -19.406 69.529  1.00 19.93 ? 134 SER   A C   1 
ATOM   782  O  O   . SER   A 1 106 ? -9.250  -19.376 70.658  1.00 19.64 ? 134 SER   A O   1 
ATOM   783  C  CB  . SER   A 1 106 ? -7.645  -21.522 68.724  1.00 21.77 ? 134 SER   A CB  1 
ATOM   784  O  OG  . SER   A 1 106 ? -7.094  -21.476 70.022  1.00 23.55 ? 134 SER   A OG  1 
ATOM   785  N  N   . HIS   A 1 107 ? -8.048  -18.376 69.037  1.00 18.34 ? 135 HIS   A N   1 
ATOM   786  C  CA  . HIS   A 1 107 ? -7.684  -17.219 69.850  1.00 18.78 ? 135 HIS   A CA  1 
ATOM   787  C  C   . HIS   A 1 107 ? -8.426  -15.944 69.490  1.00 18.00 ? 135 HIS   A C   1 
ATOM   788  O  O   . HIS   A 1 107 ? -8.378  -14.990 70.267  1.00 21.91 ? 135 HIS   A O   1 
ATOM   789  C  CB  . HIS   A 1 107 ? -6.174  -16.926 69.743  1.00 17.33 ? 135 HIS   A CB  1 
ATOM   790  C  CG  . HIS   A 1 107 ? -5.301  -18.121 69.968  1.00 16.83 ? 135 HIS   A CG  1 
ATOM   791  N  ND1 . HIS   A 1 107 ? -5.213  -18.761 71.184  1.00 17.30 ? 135 HIS   A ND1 1 
ATOM   792  C  CD2 . HIS   A 1 107 ? -4.470  -18.786 69.132  1.00 19.06 ? 135 HIS   A CD2 1 
ATOM   793  C  CE1 . HIS   A 1 107 ? -4.375  -19.775 71.087  1.00 18.52 ? 135 HIS   A CE1 1 
ATOM   794  N  NE2 . HIS   A 1 107 ? -3.916  -19.819 69.848  1.00 18.53 ? 135 HIS   A NE2 1 
ATOM   795  N  N   . GLY   A 1 108 ? -9.096  -15.890 68.352  1.00 18.07 ? 136 GLY   A N   1 
ATOM   796  C  CA  . GLY   A 1 108 ? -9.587  -14.614 67.905  1.00 17.42 ? 136 GLY   A CA  1 
ATOM   797  C  C   . GLY   A 1 108 ? -8.425  -13.744 67.451  1.00 20.79 ? 136 GLY   A C   1 
ATOM   798  O  O   . GLY   A 1 108 ? -7.264  -14.169 67.375  1.00 19.22 ? 136 GLY   A O   1 
ATOM   799  N  N   . LEU   A 1 109 ? -8.764  -12.497 67.147  1.00 17.12 ? 137 LEU   A N   1 
ATOM   800  C  CA  . LEU   A 1 109 ? -7.791  -11.564 66.609  1.00 13.60 ? 137 LEU   A CA  1 
ATOM   801  C  C   . LEU   A 1 109 ? -6.624  -11.440 67.569  1.00 14.55 ? 137 LEU   A C   1 
ATOM   802  O  O   . LEU   A 1 109 ? -6.819  -11.224 68.769  1.00 19.46 ? 137 LEU   A O   1 
ATOM   803  C  CB  . LEU   A 1 109 ? -8.447  -10.192 66.391  1.00 16.85 ? 137 LEU   A CB  1 
ATOM   804  C  CG  . LEU   A 1 109 ? -7.475  -9.056  66.033  1.00 14.69 ? 137 LEU   A CG  1 
ATOM   805  C  CD1 . LEU   A 1 109 ? -6.823  -9.330  64.677  1.00 11.24 ? 137 LEU   A CD1 1 
ATOM   806  C  CD2 . LEU   A 1 109 ? -8.171  -7.694  66.043  1.00 11.88 ? 137 LEU   A CD2 1 
ATOM   807  N  N   . GLY   A 1 110 ? -5.409  -11.572 67.057  1.00 12.76 ? 138 GLY   A N   1 
ATOM   808  C  CA  . GLY   A 1 110 ? -4.279  -11.359 67.937  1.00 13.39 ? 138 GLY   A CA  1 
ATOM   809  C  C   . GLY   A 1 110 ? -2.960  -11.529 67.221  1.00 14.59 ? 138 GLY   A C   1 
ATOM   810  O  O   . GLY   A 1 110 ? -2.905  -11.785 66.015  1.00 11.91 ? 138 GLY   A O   1 
ATOM   811  N  N   . VAL   A 1 111 ? -1.893  -11.407 68.010  1.00 12.80 ? 139 VAL   A N   1 
ATOM   812  C  CA  . VAL   A 1 111 ? -0.533  -11.359 67.488  1.00 14.62 ? 139 VAL   A CA  1 
ATOM   813  C  C   . VAL   A 1 111 ? -0.040  -12.783 67.232  1.00 15.58 ? 139 VAL   A C   1 
ATOM   814  O  O   . VAL   A 1 111 ? 0.064   -13.597 68.155  1.00 15.00 ? 139 VAL   A O   1 
ATOM   815  C  CB  . VAL   A 1 111 ? 0.398   -10.609 68.454  1.00 13.78 ? 139 VAL   A CB  1 
ATOM   816  C  CG1 . VAL   A 1 111 ? 1.870   -10.767 68.042  1.00 12.21 ? 139 VAL   A CG1 1 
ATOM   817  C  CG2 . VAL   A 1 111 ? 0.043   -9.106  68.492  1.00 11.88 ? 139 VAL   A CG2 1 
ATOM   818  N  N   . ARG   A 1 112 ? 0.275   -13.081 65.977  1.00 15.00 ? 140 ARG   A N   1 
ATOM   819  C  CA  . ARG   A 1 112 ? 0.946   -14.334 65.637  1.00 15.99 ? 140 ARG   A CA  1 
ATOM   820  C  C   . ARG   A 1 112 ? 2.462   -14.251 65.814  1.00 16.64 ? 140 ARG   A C   1 
ATOM   821  O  O   . ARG   A 1 112 ? 3.081   -15.199 66.311  1.00 16.88 ? 140 ARG   A O   1 
ATOM   822  C  CB  . ARG   A 1 112 ? 0.613   -14.728 64.197  1.00 14.67 ? 140 ARG   A CB  1 
ATOM   823  C  CG  . ARG   A 1 112 ? 1.475   -15.846 63.590  1.00 15.81 ? 140 ARG   A CG  1 
ATOM   824  C  CD  . ARG   A 1 112 ? 1.503   -17.171 64.395  1.00 13.24 ? 140 ARG   A CD  1 
ATOM   825  N  NE  . ARG   A 1 112 ? 2.195   -18.199 63.614  1.00 17.87 ? 140 ARG   A NE  1 
ATOM   826  C  CZ  . ARG   A 1 112 ? 2.293   -19.489 63.948  1.00 20.31 ? 140 ARG   A CZ  1 
ATOM   827  N  NH1 . ARG   A 1 112 ? 1.772   -19.948 65.079  1.00 14.58 ? 140 ARG   A NH1 1 
ATOM   828  N  NH2 . ARG   A 1 112 ? 2.922   -20.327 63.136  1.00 18.50 ? 140 ARG   A NH2 1 
ATOM   829  N  N   . ALA   A 1 113 ? 3.092   -13.142 65.436  1.00 13.90 ? 141 ALA   A N   1 
ATOM   830  C  CA  . ALA   A 1 113 ? 4.547   -13.104 65.378  1.00 16.19 ? 141 ALA   A CA  1 
ATOM   831  C  C   . ALA   A 1 113 ? 5.066   -11.835 66.022  1.00 15.32 ? 141 ALA   A C   1 
ATOM   832  O  O   . ALA   A 1 113 ? 4.600   -10.734 65.708  1.00 15.95 ? 141 ALA   A O   1 
ATOM   833  C  CB  . ALA   A 1 113 ? 5.058   -13.211 63.932  1.00 14.75 ? 141 ALA   A CB  1 
ATOM   834  N  N   . VAL   A 1 114 ? 6.008   -12.001 66.941  1.00 18.06 ? 142 VAL   A N   1 
ATOM   835  C  CA  . VAL   A 1 114 ? 6.862   -10.919 67.415  1.00 16.46 ? 142 VAL   A CA  1 
ATOM   836  C  C   . VAL   A 1 114 ? 8.168   -11.050 66.642  1.00 19.72 ? 142 VAL   A C   1 
ATOM   837  O  O   . VAL   A 1 114 ? 8.890   -12.043 66.799  1.00 19.25 ? 142 VAL   A O   1 
ATOM   838  C  CB  . VAL   A 1 114 ? 7.094   -10.992 68.931  1.00 14.64 ? 142 VAL   A CB  1 
ATOM   839  C  CG1 . VAL   A 1 114 ? 8.022   -9.831  69.395  1.00 15.19 ? 142 VAL   A CG1 1 
ATOM   840  C  CG2 . VAL   A 1 114 ? 5.762   -10.965 69.680  1.00 14.69 ? 142 VAL   A CG2 1 
ATOM   841  N  N   . ALA   A 1 115 ? 8.462   -10.083 65.775  1.00 18.44 ? 143 ALA   A N   1 
ATOM   842  C  CA  . ALA   A 1 115 ? 9.625   -10.164 64.899  1.00 19.41 ? 143 ALA   A CA  1 
ATOM   843  C  C   . ALA   A 1 115 ? 10.697  -9.201  65.372  1.00 19.25 ? 143 ALA   A C   1 
ATOM   844  O  O   . ALA   A 1 115 ? 10.414  -8.020  65.631  1.00 17.57 ? 143 ALA   A O   1 
ATOM   845  C  CB  . ALA   A 1 115 ? 9.268   -9.866  63.443  1.00 16.92 ? 143 ALA   A CB  1 
ATOM   846  N  N   . ILE   A 1 116 ? 11.920  -9.719  65.499  1.00 17.26 ? 144 ILE   A N   1 
ATOM   847  C  CA  . ILE   A 1 116 ? 13.090  -8.925  65.848  1.00 19.96 ? 144 ILE   A CA  1 
ATOM   848  C  C   . ILE   A 1 116 ? 14.085  -9.001  64.699  1.00 20.90 ? 144 ILE   A C   1 
ATOM   849  O  O   . ILE   A 1 116 ? 14.209  -10.036 64.033  1.00 21.24 ? 144 ILE   A O   1 
ATOM   850  C  CB  . ILE   A 1 116 ? 13.728  -9.390  67.170  1.00 21.45 ? 144 ILE   A CB  1 
ATOM   851  C  CG1 . ILE   A 1 116 ? 13.960  -10.915 67.163  1.00 22.09 ? 144 ILE   A CG1 1 
ATOM   852  C  CG2 . ILE   A 1 116 ? 12.861  -8.936  68.344  1.00 17.18 ? 144 ILE   A CG2 1 
ATOM   853  C  CD1 . ILE   A 1 116 ? 14.967  -11.396 68.201  1.00 18.91 ? 144 ILE   A CD1 1 
ATOM   854  N  N   . GLU   A 1 117 ? 14.748  -7.888  64.422  1.00 20.33 ? 145 GLU   A N   1 
ATOM   855  C  CA  . GLU   A 1 117 ? 15.775  -7.912  63.398  1.00 24.01 ? 145 GLU   A CA  1 
ATOM   856  C  C   . GLU   A 1 117 ? 17.067  -8.403  64.023  1.00 24.68 ? 145 GLU   A C   1 
ATOM   857  O  O   . GLU   A 1 117 ? 17.457  -7.947  65.101  1.00 24.71 ? 145 GLU   A O   1 
ATOM   858  C  CB  . GLU   A 1 117 ? 15.986  -6.541  62.760  1.00 24.54 ? 145 GLU   A CB  1 
ATOM   859  C  CG  . GLU   A 1 117 ? 16.903  -6.647  61.548  1.00 31.68 ? 145 GLU   A CG  1 
ATOM   860  C  CD  . GLU   A 1 117 ? 17.367  -5.311  61.021  1.00 33.41 ? 145 GLU   A CD  1 
ATOM   861  O  OE1 . GLU   A 1 117 ? 18.172  -5.304  60.061  1.00 37.60 ? 145 GLU   A OE1 1 
ATOM   862  O  OE2 . GLU   A 1 117 ? 16.938  -4.276  61.570  1.00 35.85 ? 145 GLU   A OE2 1 
ATOM   863  N  N   . VAL   A 1 118 ? 17.711  -9.358  63.366  1.00 25.16 ? 146 VAL   A N   1 
ATOM   864  C  CA  . VAL   A 1 118 ? 18.958  -9.926  63.850  1.00 25.89 ? 146 VAL   A CA  1 
ATOM   865  C  C   . VAL   A 1 118 ? 20.012  -9.764  62.760  1.00 26.40 ? 146 VAL   A C   1 
ATOM   866  O  O   . VAL   A 1 118 ? 19.717  -9.399  61.618  1.00 20.47 ? 146 VAL   A O   1 
ATOM   867  C  CB  . VAL   A 1 118 ? 18.805  -11.404 64.245  1.00 24.12 ? 146 VAL   A CB  1 
ATOM   868  C  CG1 . VAL   A 1 118 ? 17.734  -11.561 65.339  1.00 23.56 ? 146 VAL   A CG1 1 
ATOM   869  C  CG2 . VAL   A 1 118 ? 18.458  -12.224 63.014  1.00 22.49 ? 146 VAL   A CG2 1 
ATOM   870  N  N   . GLU   A 1 119 ? 21.260  -10.058 63.127  1.00 26.75 ? 147 GLU   A N   1 
ATOM   871  C  CA  . GLU   A 1 119 ? 22.333  -9.954  62.149  1.00 28.63 ? 147 GLU   A CA  1 
ATOM   872  C  C   . GLU   A 1 119 ? 22.208  -11.050 61.097  1.00 22.57 ? 147 GLU   A C   1 
ATOM   873  O  O   . GLU   A 1 119 ? 22.410  -10.800 59.908  1.00 26.23 ? 147 GLU   A O   1 
ATOM   874  C  CB  . GLU   A 1 119 ? 23.688  -10.005 62.865  1.00 33.82 ? 147 GLU   A CB  1 
ATOM   875  C  CG  . GLU   A 1 119 ? 24.858  -9.405  62.104  1.00 38.27 ? 147 GLU   A CG  1 
ATOM   876  C  CD  . GLU   A 1 119 ? 26.113  -9.197  62.982  1.00 46.38 ? 147 GLU   A CD  1 
ATOM   877  O  OE1 . GLU   A 1 119 ? 27.080  -9.976  62.859  1.00 43.06 ? 147 GLU   A OE1 1 
ATOM   878  O  OE2 . GLU   A 1 119 ? 26.128  -8.258  63.811  1.00 50.49 ? 147 GLU   A OE2 1 
ATOM   879  N  N   . ASP   A 1 120 ? 21.831  -12.257 61.508  1.00 22.58 ? 148 ASP   A N   1 
ATOM   880  C  CA  . ASP   A 1 120 ? 21.775  -13.399 60.598  1.00 26.24 ? 148 ASP   A CA  1 
ATOM   881  C  C   . ASP   A 1 120 ? 20.683  -14.341 61.098  1.00 26.65 ? 148 ASP   A C   1 
ATOM   882  O  O   . ASP   A 1 120 ? 20.887  -15.058 62.083  1.00 25.88 ? 148 ASP   A O   1 
ATOM   883  C  CB  . ASP   A 1 120 ? 23.142  -14.092 60.531  1.00 28.47 ? 148 ASP   A CB  1 
ATOM   884  C  CG  . ASP   A 1 120 ? 23.136  -15.373 59.682  1.00 31.10 ? 148 ASP   A CG  1 
ATOM   885  O  OD1 . ASP   A 1 120 ? 22.152  -15.662 58.967  1.00 36.53 ? 148 ASP   A OD1 1 
ATOM   886  O  OD2 . ASP   A 1 120 ? 24.143  -16.109 59.740  1.00 39.96 ? 148 ASP   A OD2 1 
ATOM   887  N  N   . ALA   A 1 121 ? 19.530  -14.342 60.406  1.00 27.14 ? 149 ALA   A N   1 
ATOM   888  C  CA  . ALA   A 1 121 ? 18.373  -15.112 60.853  1.00 21.72 ? 149 ALA   A CA  1 
ATOM   889  C  C   . ALA   A 1 121 ? 18.622  -16.612 60.774  1.00 26.69 ? 149 ALA   A C   1 
ATOM   890  O  O   . ALA   A 1 121 ? 18.113  -17.364 61.613  1.00 24.51 ? 149 ALA   A O   1 
ATOM   891  C  CB  . ALA   A 1 121 ? 17.141  -14.731 60.032  1.00 21.09 ? 149 ALA   A CB  1 
ATOM   892  N  N   . GLU   A 1 122 ? 19.395  -17.073 59.786  1.00 27.84 ? 150 GLU   A N   1 
ATOM   893  C  CA  . GLU   A 1 122 ? 19.734  -18.496 59.742  1.00 29.29 ? 150 GLU   A CA  1 
ATOM   894  C  C   . GLU   A 1 122 ? 20.531  -18.905 60.973  1.00 27.58 ? 150 GLU   A C   1 
ATOM   895  O  O   . GLU   A 1 122 ? 20.187  -19.873 61.662  1.00 25.75 ? 150 GLU   A O   1 
ATOM   896  C  CB  . GLU   A 1 122 ? 20.516  -18.823 58.471  1.00 31.65 ? 150 GLU   A CB  1 
ATOM   897  C  CG  . GLU   A 1 122 ? 21.076  -20.258 58.473  1.00 31.16 ? 150 GLU   A CG  1 
ATOM   898  C  CD  . GLU   A 1 122 ? 21.431  -20.749 57.091  1.00 44.16 ? 150 GLU   A CD  1 
ATOM   899  O  OE1 . GLU   A 1 122 ? 22.072  -21.818 56.990  1.00 55.78 ? 150 GLU   A OE1 1 
ATOM   900  O  OE2 . GLU   A 1 122 ? 21.066  -20.072 56.098  1.00 52.27 ? 150 GLU   A OE2 1 
ATOM   901  N  N   . SER   A 1 123 ? 21.594  -18.156 61.272  1.00 26.47 ? 151 SER   A N   1 
ATOM   902  C  CA  . SER   A 1 123 ? 22.388  -18.402 62.468  1.00 26.58 ? 151 SER   A CA  1 
ATOM   903  C  C   . SER   A 1 123 ? 21.545  -18.291 63.735  1.00 28.04 ? 151 SER   A C   1 
ATOM   904  O  O   . SER   A 1 123 ? 21.603  -19.164 64.610  1.00 28.30 ? 151 SER   A O   1 
ATOM   905  C  CB  . SER   A 1 123 ? 23.558  -17.419 62.510  1.00 30.90 ? 151 SER   A CB  1 
ATOM   906  O  OG  . SER   A 1 123 ? 24.239  -17.525 63.745  1.00 39.49 ? 151 SER   A OG  1 
ATOM   907  N  N   . ALA   A 1 124 ? 20.764  -17.207 63.860  1.00 28.80 ? 152 ALA   A N   1 
ATOM   908  C  CA  . ALA   A 1 124 ? 19.900  -17.058 65.030  1.00 27.27 ? 152 ALA   A CA  1 
ATOM   909  C  C   . ALA   A 1 124 ? 18.978  -18.262 65.196  1.00 23.26 ? 152 ALA   A C   1 
ATOM   910  O  O   . ALA   A 1 124 ? 18.767  -18.736 66.318  1.00 25.04 ? 152 ALA   A O   1 
ATOM   911  C  CB  . ALA   A 1 124 ? 19.084  -15.768 64.936  1.00 24.98 ? 152 ALA   A CB  1 
ATOM   912  N  N   . PHE   A 1 125 ? 18.448  -18.790 64.088  1.00 23.64 ? 153 PHE   A N   1 
ATOM   913  C  CA  . PHE   A 1 125 ? 17.591  -19.973 64.156  1.00 25.71 ? 153 PHE   A CA  1 
ATOM   914  C  C   . PHE   A 1 125 ? 18.370  -21.189 64.647  1.00 24.36 ? 153 PHE   A C   1 
ATOM   915  O  O   . PHE   A 1 125 ? 17.948  -21.879 65.583  1.00 24.63 ? 153 PHE   A O   1 
ATOM   916  C  CB  . PHE   A 1 125 ? 16.965  -20.241 62.781  1.00 21.39 ? 153 PHE   A CB  1 
ATOM   917  C  CG  . PHE   A 1 125 ? 16.138  -21.505 62.720  1.00 27.80 ? 153 PHE   A CG  1 
ATOM   918  C  CD1 . PHE   A 1 125 ? 16.732  -22.732 62.387  1.00 23.87 ? 153 PHE   A CD1 1 
ATOM   919  C  CD2 . PHE   A 1 125 ? 14.771  -21.472 62.991  1.00 21.89 ? 153 PHE   A CD2 1 
ATOM   920  C  CE1 . PHE   A 1 125 ? 15.981  -23.893 62.327  1.00 26.21 ? 153 PHE   A CE1 1 
ATOM   921  C  CE2 . PHE   A 1 125 ? 14.001  -22.639 62.929  1.00 22.37 ? 153 PHE   A CE2 1 
ATOM   922  C  CZ  . PHE   A 1 125 ? 14.605  -23.852 62.594  1.00 24.02 ? 153 PHE   A CZ  1 
ATOM   923  N  N   . SER   A 1 126 ? 19.518  -21.462 64.023  1.00 28.84 ? 154 SER   A N   1 
ATOM   924  C  CA  . SER   A 1 126 ? 20.302  -22.648 64.365  1.00 28.43 ? 154 SER   A CA  1 
ATOM   925  C  C   . SER   A 1 126 ? 20.704  -22.632 65.830  1.00 25.75 ? 154 SER   A C   1 
ATOM   926  O  O   . SER   A 1 126 ? 20.482  -23.602 66.562  1.00 27.14 ? 154 SER   A O   1 
ATOM   927  C  CB  . SER   A 1 126 ? 21.546  -22.718 63.478  1.00 27.33 ? 154 SER   A CB  1 
ATOM   928  O  OG  . SER   A 1 126 ? 21.186  -23.089 62.165  1.00 34.22 ? 154 SER   A OG  1 
ATOM   929  N  N   . ILE   A 1 127 ? 21.293  -21.524 66.275  1.00 24.34 ? 155 ILE   A N   1 
ATOM   930  C  CA  . ILE   A 1 127 ? 21.722  -21.406 67.662  1.00 22.40 ? 155 ILE   A CA  1 
ATOM   931  C  C   . ILE   A 1 127 ? 20.534  -21.533 68.607  1.00 23.63 ? 155 ILE   A C   1 
ATOM   932  O  O   . ILE   A 1 127 ? 20.608  -22.234 69.625  1.00 27.62 ? 155 ILE   A O   1 
ATOM   933  C  CB  . ILE   A 1 127 ? 22.474  -20.077 67.845  1.00 29.43 ? 155 ILE   A CB  1 
ATOM   934  C  CG1 . ILE   A 1 127 ? 23.783  -20.108 67.037  1.00 28.93 ? 155 ILE   A CG1 1 
ATOM   935  C  CG2 . ILE   A 1 127 ? 22.693  -19.783 69.307  1.00 29.13 ? 155 ILE   A CG2 1 
ATOM   936  C  CD1 . ILE   A 1 127 ? 24.394  -18.731 66.772  1.00 30.38 ? 155 ILE   A CD1 1 
ATOM   937  N  N   . SER   A 1 128 ? 19.417  -20.866 68.282  1.00 25.97 ? 156 SER   A N   1 
ATOM   938  C  CA  . SER   A 1 128 ? 18.196  -20.990 69.079  1.00 24.88 ? 156 SER   A CA  1 
ATOM   939  C  C   . SER   A 1 128 ? 17.790  -22.442 69.235  1.00 22.38 ? 156 SER   A C   1 
ATOM   940  O  O   . SER   A 1 128 ? 17.517  -22.912 70.345  1.00 24.04 ? 156 SER   A O   1 
ATOM   941  C  CB  . SER   A 1 128 ? 17.042  -20.222 68.424  1.00 22.29 ? 156 SER   A CB  1 
ATOM   942  O  OG  . SER   A 1 128 ? 17.249  -18.841 68.449  1.00 20.04 ? 156 SER   A OG  1 
ATOM   943  N  N   . VAL   A 1 129 ? 17.684  -23.155 68.112  1.00 22.26 ? 157 VAL   A N   1 
ATOM   944  C  CA  . VAL   A 1 129 ? 17.241  -24.543 68.156  1.00 24.53 ? 157 VAL   A CA  1 
ATOM   945  C  C   . VAL   A 1 129 ? 18.258  -25.397 68.904  1.00 26.23 ? 157 VAL   A C   1 
ATOM   946  O  O   . VAL   A 1 129 ? 17.889  -26.224 69.749  1.00 23.84 ? 157 VAL   A O   1 
ATOM   947  C  CB  . VAL   A 1 129 ? 16.977  -25.058 66.727  1.00 27.06 ? 157 VAL   A CB  1 
ATOM   948  C  CG1 . VAL   A 1 129 ? 16.777  -26.584 66.706  1.00 22.41 ? 157 VAL   A CG1 1 
ATOM   949  C  CG2 . VAL   A 1 129 ? 15.762  -24.342 66.135  1.00 26.18 ? 157 VAL   A CG2 1 
ATOM   950  N  N   . ALA   A 1 130 ? 19.557  -25.173 68.652  1.00 23.66 ? 158 ALA   A N   1 
ATOM   951  C  CA  . ALA   A 1 130 ? 20.575  -25.912 69.396  1.00 28.27 ? 158 ALA   A CA  1 
ATOM   952  C  C   . ALA   A 1 130 ? 20.466  -25.656 70.891  1.00 29.27 ? 158 ALA   A C   1 
ATOM   953  O  O   . ALA   A 1 130 ? 20.912  -26.487 71.688  1.00 29.47 ? 158 ALA   A O   1 
ATOM   954  C  CB  . ALA   A 1 130 ? 21.982  -25.559 68.901  1.00 23.43 ? 158 ALA   A CB  1 
ATOM   955  N  N   . ASN   A 1 131 ? 19.844  -24.546 71.289  1.00 26.59 ? 159 ASN   A N   1 
ATOM   956  C  CA  . ASN   A 1 131 ? 19.699  -24.181 72.689  1.00 24.58 ? 159 ASN   A CA  1 
ATOM   957  C  C   . ASN   A 1 131 ? 18.261  -24.318 73.188  1.00 25.24 ? 159 ASN   A C   1 
ATOM   958  O  O   . ASN   A 1 131 ? 17.857  -23.620 74.121  1.00 28.05 ? 159 ASN   A O   1 
ATOM   959  C  CB  . ASN   A 1 131 ? 20.219  -22.761 72.902  1.00 25.86 ? 159 ASN   A CB  1 
ATOM   960  C  CG  . ASN   A 1 131 ? 21.736  -22.704 72.913  1.00 26.62 ? 159 ASN   A CG  1 
ATOM   961  O  OD1 . ASN   A 1 131 ? 22.354  -22.898 73.952  1.00 31.19 ? 159 ASN   A OD1 1 
ATOM   962  N  ND2 . ASN   A 1 131 ? 22.342  -22.473 71.753  1.00 21.87 ? 159 ASN   A ND2 1 
ATOM   963  N  N   . GLY   A 1 132 ? 17.467  -25.204 72.577  1.00 24.76 ? 160 GLY   A N   1 
ATOM   964  C  CA  . GLY   A 1 132 ? 16.183  -25.588 73.137  1.00 24.08 ? 160 GLY   A CA  1 
ATOM   965  C  C   . GLY   A 1 132 ? 14.950  -25.017 72.457  1.00 25.03 ? 160 GLY   A C   1 
ATOM   966  O  O   . GLY   A 1 132 ? 13.836  -25.448 72.781  1.00 23.69 ? 160 GLY   A O   1 
ATOM   967  N  N   . ALA   A 1 133 ? 15.101  -24.071 71.532  1.00 26.85 ? 161 ALA   A N   1 
ATOM   968  C  CA  . ALA   A 1 133 ? 13.938  -23.483 70.868  1.00 26.34 ? 161 ALA   A CA  1 
ATOM   969  C  C   . ALA   A 1 133 ? 13.197  -24.520 70.029  1.00 25.33 ? 161 ALA   A C   1 
ATOM   970  O  O   . ALA   A 1 133 ? 13.811  -25.312 69.302  1.00 25.21 ? 161 ALA   A O   1 
ATOM   971  C  CB  . ALA   A 1 133 ? 14.364  -22.322 69.974  1.00 21.65 ? 161 ALA   A CB  1 
ATOM   972  N  N   . ILE   A 1 134 ? 11.871  -24.509 70.125  1.00 25.81 ? 162 ILE   A N   1 
ATOM   973  C  CA  . ILE   A 1 134 ? 11.040  -25.372 69.288  1.00 23.04 ? 162 ILE   A CA  1 
ATOM   974  C  C   . ILE   A 1 134 ? 10.913  -24.735 67.914  1.00 24.73 ? 162 ILE   A C   1 
ATOM   975  O  O   . ILE   A 1 134 ? 10.397  -23.615 67.803  1.00 26.83 ? 162 ILE   A O   1 
ATOM   976  C  CB  . ILE   A 1 134 ? 9.648   -25.591 69.885  1.00 24.20 ? 162 ILE   A CB  1 
ATOM   977  C  CG1 . ILE   A 1 134 ? 9.737   -25.934 71.375  1.00 25.72 ? 162 ILE   A CG1 1 
ATOM   978  C  CG2 . ILE   A 1 134 ? 8.920   -26.667 69.078  1.00 25.56 ? 162 ILE   A CG2 1 
ATOM   979  C  CD1 . ILE   A 1 134 ? 10.171  -27.382 71.659  1.00 28.82 ? 162 ILE   A CD1 1 
ATOM   980  N  N   . PRO   A 1 135 ? 11.354  -25.397 66.849  1.00 23.35 ? 163 PRO   A N   1 
ATOM   981  C  CA  . PRO   A 1 135 ? 11.315  -24.761 65.529  1.00 23.40 ? 163 PRO   A CA  1 
ATOM   982  C  C   . PRO   A 1 135 ? 9.888   -24.608 65.025  1.00 21.59 ? 163 PRO   A C   1 
ATOM   983  O  O   . PRO   A 1 135 ? 9.041   -25.478 65.224  1.00 21.98 ? 163 PRO   A O   1 
ATOM   984  C  CB  . PRO   A 1 135 ? 12.139  -25.707 64.640  1.00 22.95 ? 163 PRO   A CB  1 
ATOM   985  C  CG  . PRO   A 1 135 ? 12.183  -27.000 65.367  1.00 25.69 ? 163 PRO   A CG  1 
ATOM   986  C  CD  . PRO   A 1 135 ? 12.046  -26.696 66.837  1.00 22.41 ? 163 PRO   A CD  1 
ATOM   987  N  N   . SER   A 1 136 ? 9.623   -23.478 64.369  1.00 21.19 ? 164 SER   A N   1 
ATOM   988  C  CA  . SER   A 1 136 ? 8.318   -23.258 63.757  1.00 20.01 ? 164 SER   A CA  1 
ATOM   989  C  C   . SER   A 1 136 ? 8.389   -23.107 62.246  1.00 18.52 ? 164 SER   A C   1 
ATOM   990  O  O   . SER   A 1 136 ? 7.560   -23.664 61.542  1.00 20.36 ? 164 SER   A O   1 
ATOM   991  C  CB  . SER   A 1 136 ? 7.630   -22.018 64.385  1.00 19.64 ? 164 SER   A CB  1 
ATOM   992  O  OG  . SER   A 1 136 ? 6.250   -21.959 64.026  1.00 23.32 ? 164 SER   A OG  1 
ATOM   993  N  N   . SER   A 1 137 ? 9.361   -22.367 61.716  1.00 19.46 ? 165 SER   A N   1 
ATOM   994  C  CA  . SER   A 1 137 ? 9.527   -22.310 60.283  1.00 17.95 ? 165 SER   A CA  1 
ATOM   995  C  C   . SER   A 1 137 ? 11.015  -22.114 60.019  1.00 19.73 ? 165 SER   A C   1 
ATOM   996  O  O   . SER   A 1 137 ? 11.633  -21.227 60.633  1.00 20.51 ? 165 SER   A O   1 
ATOM   997  C  CB  . SER   A 1 137 ? 8.729   -21.194 59.624  1.00 20.45 ? 165 SER   A CB  1 
ATOM   998  O  OG  . SER   A 1 137 ? 8.818   -21.285 58.210  1.00 27.86 ? 165 SER   A OG  1 
ATOM   999  N  N   . PRO   A 1 138 ? 11.608  -22.909 59.135  1.00 21.49 ? 166 PRO   A N   1 
ATOM   1000 C  CA  . PRO   A 1 138 ? 13.063  -22.892 58.975  1.00 23.15 ? 166 PRO   A CA  1 
ATOM   1001 C  C   . PRO   A 1 138 ? 13.525  -21.641 58.245  1.00 25.37 ? 166 PRO   A C   1 
ATOM   1002 O  O   . PRO   A 1 138 ? 12.707  -20.884 57.691  1.00 22.68 ? 166 PRO   A O   1 
ATOM   1003 C  CB  . PRO   A 1 138 ? 13.341  -24.175 58.165  1.00 23.01 ? 166 PRO   A CB  1 
ATOM   1004 C  CG  . PRO   A 1 138 ? 12.086  -24.443 57.428  1.00 25.76 ? 166 PRO   A CG  1 
ATOM   1005 C  CD  . PRO   A 1 138 ? 10.968  -23.969 58.335  1.00 21.01 ? 166 PRO   A CD  1 
ATOM   1006 N  N   . PRO   A 1 139 ? 14.828  -21.361 58.248  1.00 22.47 ? 167 PRO   A N   1 
ATOM   1007 C  CA  . PRO   A 1 139 ? 15.312  -20.161 57.551  1.00 21.15 ? 167 PRO   A CA  1 
ATOM   1008 C  C   . PRO   A 1 139 ? 15.036  -20.274 56.061  1.00 23.60 ? 167 PRO   A C   1 
ATOM   1009 O  O   . PRO   A 1 139 ? 15.274  -21.311 55.448  1.00 28.09 ? 167 PRO   A O   1 
ATOM   1010 C  CB  . PRO   A 1 139 ? 16.814  -20.136 57.861  1.00 23.42 ? 167 PRO   A CB  1 
ATOM   1011 C  CG  . PRO   A 1 139 ? 17.009  -21.058 59.012  1.00 26.41 ? 167 PRO   A CG  1 
ATOM   1012 C  CD  . PRO   A 1 139 ? 15.905  -22.083 58.942  1.00 22.28 ? 167 PRO   A CD  1 
ATOM   1013 N  N   . ILE   A 1 140 ? 14.470  -19.216 55.491  1.00 25.26 ? 168 ILE   A N   1 
ATOM   1014 C  CA  . ILE   A 1 140 ? 14.172  -19.162 54.069  1.00 24.09 ? 168 ILE   A CA  1 
ATOM   1015 C  C   . ILE   A 1 140 ? 14.715  -17.845 53.547  1.00 28.53 ? 168 ILE   A C   1 
ATOM   1016 O  O   . ILE   A 1 140 ? 14.481  -16.790 54.148  1.00 27.16 ? 168 ILE   A O   1 
ATOM   1017 C  CB  . ILE   A 1 140 ? 12.658  -19.292 53.786  1.00 30.22 ? 168 ILE   A CB  1 
ATOM   1018 C  CG1 . ILE   A 1 140 ? 12.155  -20.705 54.150  1.00 30.22 ? 168 ILE   A CG1 1 
ATOM   1019 C  CG2 . ILE   A 1 140 ? 12.365  -18.982 52.319  1.00 28.66 ? 168 ILE   A CG2 1 
ATOM   1020 C  CD1 . ILE   A 1 140 ? 10.926  -20.754 55.065  1.00 31.40 ? 168 ILE   A CD1 1 
ATOM   1021 N  N   . VAL   A 1 141 ? 15.469  -17.903 52.456  1.00 30.98 ? 169 VAL   A N   1 
ATOM   1022 C  CA  . VAL   A 1 141 ? 16.064  -16.712 51.861  1.00 28.56 ? 169 VAL   A CA  1 
ATOM   1023 C  C   . VAL   A 1 141 ? 15.125  -16.202 50.774  1.00 30.98 ? 169 VAL   A C   1 
ATOM   1024 O  O   . VAL   A 1 141 ? 14.765  -16.936 49.847  1.00 30.49 ? 169 VAL   A O   1 
ATOM   1025 C  CB  . VAL   A 1 141 ? 17.469  -16.997 51.314  1.00 30.33 ? 169 VAL   A CB  1 
ATOM   1026 C  CG1 . VAL   A 1 141 ? 18.159  -15.700 50.946  1.00 33.66 ? 169 VAL   A CG1 1 
ATOM   1027 C  CG2 . VAL   A 1 141 ? 18.277  -17.733 52.356  1.00 27.66 ? 169 VAL   A CG2 1 
ATOM   1028 N  N   . LEU   A 1 142 ? 14.717  -14.944 50.898  1.00 28.47 ? 170 LEU   A N   1 
ATOM   1029 C  CA  . LEU   A 1 142 ? 13.785  -14.316 49.973  1.00 30.14 ? 170 LEU   A CA  1 
ATOM   1030 C  C   . LEU   A 1 142 ? 14.573  -13.435 49.003  1.00 33.21 ? 170 LEU   A C   1 
ATOM   1031 O  O   . LEU   A 1 142 ? 15.218  -12.465 49.417  1.00 29.96 ? 170 LEU   A O   1 
ATOM   1032 C  CB  . LEU   A 1 142 ? 12.744  -13.504 50.740  1.00 28.33 ? 170 LEU   A CB  1 
ATOM   1033 C  CG  . LEU   A 1 142 ? 11.997  -14.280 51.825  1.00 27.51 ? 170 LEU   A CG  1 
ATOM   1034 C  CD1 . LEU   A 1 142 ? 11.270  -13.343 52.791  1.00 31.85 ? 170 LEU   A CD1 1 
ATOM   1035 C  CD2 . LEU   A 1 142 ? 11.030  -15.241 51.177  1.00 27.19 ? 170 LEU   A CD2 1 
ATOM   1036 N  N   . ASN   A 1 143 ? 14.524  -13.789 47.719  1.00 34.02 ? 171 ASN   A N   1 
ATOM   1037 C  CA  . ASN   A 1 143 ? 15.134  -13.012 46.637  1.00 40.25 ? 171 ASN   A CA  1 
ATOM   1038 C  C   . ASN   A 1 143 ? 16.599  -12.673 46.915  1.00 38.47 ? 171 ASN   A C   1 
ATOM   1039 O  O   . ASN   A 1 143 ? 17.072  -11.579 46.602  1.00 45.39 ? 171 ASN   A O   1 
ATOM   1040 C  CB  . ASN   A 1 143 ? 14.336  -11.737 46.365  1.00 38.74 ? 171 ASN   A CB  1 
ATOM   1041 C  CG  . ASN   A 1 143 ? 14.592  -11.181 44.974  1.00 46.94 ? 171 ASN   A CG  1 
ATOM   1042 O  OD1 . ASN   A 1 143 ? 14.990  -11.916 44.070  1.00 49.04 ? 171 ASN   A OD1 1 
ATOM   1043 N  ND2 . ASN   A 1 143 ? 14.383  -9.874  44.802  1.00 44.36 ? 171 ASN   A ND2 1 
ATOM   1044 N  N   . GLU   A 1 144 ? 17.325  -13.615 47.513  1.00 36.03 ? 172 GLU   A N   1 
ATOM   1045 C  CA  . GLU   A 1 144 ? 18.736  -13.438 47.858  1.00 43.81 ? 172 GLU   A CA  1 
ATOM   1046 C  C   . GLU   A 1 144 ? 18.981  -12.196 48.710  1.00 42.01 ? 172 GLU   A C   1 
ATOM   1047 O  O   . GLU   A 1 144 ? 20.115  -11.710 48.796  1.00 47.35 ? 172 GLU   A O   1 
ATOM   1048 C  CB  . GLU   A 1 144 ? 19.615  -13.384 46.599  1.00 45.03 ? 172 GLU   A CB  1 
ATOM   1049 C  CG  . GLU   A 1 144 ? 19.236  -14.402 45.535  1.00 52.27 ? 172 GLU   A CG  1 
ATOM   1050 C  CD  . GLU   A 1 144 ? 19.958  -14.177 44.214  1.00 60.67 ? 172 GLU   A CD  1 
ATOM   1051 O  OE1 . GLU   A 1 144 ? 21.182  -13.920 44.240  1.00 60.72 ? 172 GLU   A OE1 1 
ATOM   1052 O  OE2 . GLU   A 1 144 ? 19.306  -14.274 43.151  1.00 58.80 ? 172 GLU   A OE2 1 
ATOM   1053 N  N   . ALA   A 1 145 ? 17.955  -11.673 49.349  1.00 41.29 ? 173 ALA   A N   1 
ATOM   1054 C  CA  . ALA   A 1 145 ? 18.078  -10.372 49.993  1.00 36.56 ? 173 ALA   A CA  1 
ATOM   1055 C  C   . ALA   A 1 145 ? 17.720  -10.400 51.466  1.00 37.01 ? 173 ALA   A C   1 
ATOM   1056 O  O   . ALA   A 1 145 ? 18.372  -9.718  52.260  1.00 36.57 ? 173 ALA   A O   1 
ATOM   1057 C  CB  . ALA   A 1 145 ? 17.195  -9.337  49.268  1.00 31.36 ? 173 ALA   A CB  1 
ATOM   1058 N  N   . VAL   A 1 146 ? 16.696  -11.158 51.853  1.00 34.64 ? 174 VAL   A N   1 
ATOM   1059 C  CA  . VAL   A 1 146 ? 16.199  -11.158 53.222  1.00 33.36 ? 174 VAL   A CA  1 
ATOM   1060 C  C   . VAL   A 1 146 ? 16.026  -12.602 53.667  1.00 28.13 ? 174 VAL   A C   1 
ATOM   1061 O  O   . VAL   A 1 146 ? 15.509  -13.438 52.919  1.00 30.77 ? 174 VAL   A O   1 
ATOM   1062 C  CB  . VAL   A 1 146 ? 14.869  -10.373 53.353  1.00 32.18 ? 174 VAL   A CB  1 
ATOM   1063 C  CG1 . VAL   A 1 146 ? 14.503  -10.186 54.814  1.00 29.57 ? 174 VAL   A CG1 1 
ATOM   1064 C  CG2 . VAL   A 1 146 ? 14.972  -9.017  52.675  1.00 31.48 ? 174 VAL   A CG2 1 
ATOM   1065 N  N   . THR   A 1 147 ? 16.460  -12.898 54.884  1.00 25.36 ? 175 THR   A N   1 
ATOM   1066 C  CA  . THR   A 1 147 ? 16.285  -14.217 55.466  1.00 29.83 ? 175 THR   A CA  1 
ATOM   1067 C  C   . THR   A 1 147 ? 15.310  -14.136 56.634  1.00 26.47 ? 175 THR   A C   1 
ATOM   1068 O  O   . THR   A 1 147 ? 15.394  -13.227 57.467  1.00 24.44 ? 175 THR   A O   1 
ATOM   1069 C  CB  . THR   A 1 147 ? 17.624  -14.787 55.925  1.00 28.04 ? 175 THR   A CB  1 
ATOM   1070 O  OG1 . THR   A 1 147 ? 18.553  -14.714 54.834  1.00 29.35 ? 175 THR   A OG1 1 
ATOM   1071 C  CG2 . THR   A 1 147 ? 17.448  -16.230 56.344  1.00 25.46 ? 175 THR   A CG2 1 
ATOM   1072 N  N   . ILE   A 1 148 ? 14.382  -15.086 56.683  1.00 24.47 ? 176 ILE   A N   1 
ATOM   1073 C  CA  . ILE   A 1 148 ? 13.334  -15.116 57.693  1.00 23.75 ? 176 ILE   A CA  1 
ATOM   1074 C  C   . ILE   A 1 148 ? 13.265  -16.523 58.280  1.00 25.23 ? 176 ILE   A C   1 
ATOM   1075 O  O   . ILE   A 1 148 ? 13.403  -17.515 57.555  1.00 23.55 ? 176 ILE   A O   1 
ATOM   1076 C  CB  . ILE   A 1 148 ? 11.979  -14.680 57.089  1.00 26.33 ? 176 ILE   A CB  1 
ATOM   1077 C  CG1 . ILE   A 1 148 ? 10.873  -14.654 58.141  1.00 28.99 ? 176 ILE   A CG1 1 
ATOM   1078 C  CG2 . ILE   A 1 148 ? 11.564  -15.594 55.923  1.00 28.29 ? 176 ILE   A CG2 1 
ATOM   1079 C  CD1 . ILE   A 1 148 ? 9.598   -13.943 57.634  1.00 28.65 ? 176 ILE   A CD1 1 
ATOM   1080 N  N   . ALA   A 1 149 ? 13.075  -16.606 59.599  1.00 20.67 ? 177 ALA   A N   1 
ATOM   1081 C  CA  . ALA   A 1 149 ? 12.961  -17.875 60.302  1.00 21.81 ? 177 ALA   A CA  1 
ATOM   1082 C  C   . ALA   A 1 149 ? 12.143  -17.650 61.566  1.00 18.20 ? 177 ALA   A C   1 
ATOM   1083 O  O   . ALA   A 1 149 ? 12.051  -16.524 62.067  1.00 18.99 ? 177 ALA   A O   1 
ATOM   1084 C  CB  . ALA   A 1 149 ? 14.346  -18.454 60.636  1.00 20.51 ? 177 ALA   A CB  1 
ATOM   1085 N  N   . GLU   A 1 150 ? 11.543  -18.728 62.084  1.00 15.97 ? 178 GLU   A N   1 
ATOM   1086 C  CA  . GLU   A 1 150 ? 10.616  -18.622 63.208  1.00 18.11 ? 178 GLU   A CA  1 
ATOM   1087 C  C   . GLU   A 1 150 ? 10.793  -19.778 64.182  1.00 19.03 ? 178 GLU   A C   1 
ATOM   1088 O  O   . GLU   A 1 150 ? 10.968  -20.927 63.767  1.00 17.77 ? 178 GLU   A O   1 
ATOM   1089 C  CB  . GLU   A 1 150 ? 9.140   -18.582 62.725  1.00 15.49 ? 178 GLU   A CB  1 
ATOM   1090 C  CG  . GLU   A 1 150 ? 8.805   -17.332 61.906  1.00 17.35 ? 178 GLU   A CG  1 
ATOM   1091 C  CD  . GLU   A 1 150 ? 7.446   -17.395 61.218  1.00 19.41 ? 178 GLU   A CD  1 
ATOM   1092 O  OE1 . GLU   A 1 150 ? 6.566   -18.172 61.657  1.00 17.82 ? 178 GLU   A OE1 1 
ATOM   1093 O  OE2 . GLU   A 1 150 ? 7.261   -16.657 60.227  1.00 20.20 ? 178 GLU   A OE2 1 
ATOM   1094 N  N   . VAL   A 1 151 ? 10.709  -19.465 65.481  1.00 17.02 ? 179 VAL   A N   1 
ATOM   1095 C  CA  . VAL   A 1 151 ? 10.670  -20.458 66.549  1.00 20.96 ? 179 VAL   A CA  1 
ATOM   1096 C  C   . VAL   A 1 151 ? 9.493   -20.124 67.464  1.00 20.56 ? 179 VAL   A C   1 
ATOM   1097 O  O   . VAL   A 1 151 ? 8.998   -18.996 67.488  1.00 20.09 ? 179 VAL   A O   1 
ATOM   1098 C  CB  . VAL   A 1 151 ? 11.998  -20.520 67.354  1.00 22.58 ? 179 VAL   A CB  1 
ATOM   1099 C  CG1 . VAL   A 1 151 ? 13.132  -21.028 66.480  1.00 16.96 ? 179 VAL   A CG1 1 
ATOM   1100 C  CG2 . VAL   A 1 151 ? 12.365  -19.154 67.899  1.00 17.31 ? 179 VAL   A CG2 1 
ATOM   1101 N  N   . LYS   A 1 152 ? 9.039   -21.123 68.215  1.00 20.88 ? 180 LYS   A N   1 
ATOM   1102 C  CA  . LYS   A 1 152 ? 7.934   -20.911 69.143  1.00 20.55 ? 180 LYS   A CA  1 
ATOM   1103 C  C   . LYS   A 1 152 ? 8.367   -20.084 70.344  1.00 20.35 ? 180 LYS   A C   1 
ATOM   1104 O  O   . LYS   A 1 152 ? 9.433   -20.306 70.925  1.00 21.76 ? 180 LYS   A O   1 
ATOM   1105 C  CB  . LYS   A 1 152 ? 7.370   -22.246 69.625  1.00 21.27 ? 180 LYS   A CB  1 
ATOM   1106 C  CG  . LYS   A 1 152 ? 6.782   -23.084 68.516  1.00 21.66 ? 180 LYS   A CG  1 
ATOM   1107 C  CD  . LYS   A 1 152 ? 6.172   -24.356 69.077  1.00 28.03 ? 180 LYS   A CD  1 
ATOM   1108 C  CE  . LYS   A 1 152 ? 5.282   -25.054 68.048  1.00 31.71 ? 180 LYS   A CE  1 
ATOM   1109 N  NZ  . LYS   A 1 152 ? 4.495   -26.127 68.712  1.00 30.46 ? 180 LYS   A NZ  1 
ATOM   1110 N  N   . LEU   A 1 153 ? 7.516   -19.132 70.726  1.00 22.55 ? 181 LEU   A N   1 
ATOM   1111 C  CA  . LEU   A 1 153 ? 7.783   -18.242 71.855  1.00 22.95 ? 181 LEU   A CA  1 
ATOM   1112 C  C   . LEU   A 1 153 ? 6.963   -18.642 73.077  1.00 21.08 ? 181 LEU   A C   1 
ATOM   1113 O  O   . LEU   A 1 153 ? 7.521   -18.968 74.130  1.00 20.18 ? 181 LEU   A O   1 
ATOM   1114 C  CB  . LEU   A 1 153 ? 7.499   -16.780 71.442  1.00 18.28 ? 181 LEU   A CB  1 
ATOM   1115 C  CG  . LEU   A 1 153 ? 7.847   -15.637 72.414  1.00 23.29 ? 181 LEU   A CG  1 
ATOM   1116 C  CD1 . LEU   A 1 153 ? 9.328   -15.636 72.842  1.00 17.01 ? 181 LEU   A CD1 1 
ATOM   1117 C  CD2 . LEU   A 1 153 ? 7.430   -14.241 71.848  1.00 16.09 ? 181 LEU   A CD2 1 
ATOM   1118 N  N   . TYR   A 1 154 ? 5.639   -18.602 72.954  1.00 16.48 ? 182 TYR   A N   1 
ATOM   1119 C  CA  . TYR   A 1 154 ? 4.710   -19.125 73.945  1.00 18.45 ? 182 TYR   A CA  1 
ATOM   1120 C  C   . TYR   A 1 154 ? 3.364   -19.258 73.250  1.00 18.12 ? 182 TYR   A C   1 
ATOM   1121 O  O   . TYR   A 1 154 ? 3.053   -18.496 72.328  1.00 18.20 ? 182 TYR   A O   1 
ATOM   1122 C  CB  . TYR   A 1 154 ? 4.597   -18.235 75.205  1.00 20.33 ? 182 TYR   A CB  1 
ATOM   1123 C  CG  . TYR   A 1 154 ? 4.697   -16.730 74.965  1.00 18.49 ? 182 TYR   A CG  1 
ATOM   1124 C  CD1 . TYR   A 1 154 ? 3.742   -16.049 74.212  1.00 15.45 ? 182 TYR   A CD1 1 
ATOM   1125 C  CD2 . TYR   A 1 154 ? 5.746   -15.999 75.498  1.00 17.31 ? 182 TYR   A CD2 1 
ATOM   1126 C  CE1 . TYR   A 1 154 ? 3.846   -14.669 73.984  1.00 17.87 ? 182 TYR   A CE1 1 
ATOM   1127 C  CE2 . TYR   A 1 154 ? 5.861   -14.643 75.282  1.00 19.33 ? 182 TYR   A CE2 1 
ATOM   1128 C  CZ  . TYR   A 1 154 ? 4.912   -13.975 74.525  1.00 20.78 ? 182 TYR   A CZ  1 
ATOM   1129 O  OH  . TYR   A 1 154 ? 5.042   -12.613 74.332  1.00 18.74 ? 182 TYR   A OH  1 
ATOM   1130 N  N   . GLY   A 1 155 ? 2.587   -20.248 73.675  1.00 20.26 ? 183 GLY   A N   1 
ATOM   1131 C  CA  . GLY   A 1 155 ? 1.316   -20.510 73.017  1.00 21.74 ? 183 GLY   A CA  1 
ATOM   1132 C  C   . GLY   A 1 155 ? 1.527   -20.727 71.533  1.00 19.53 ? 183 GLY   A C   1 
ATOM   1133 O  O   . GLY   A 1 155 ? 2.447   -21.429 71.110  1.00 19.36 ? 183 GLY   A O   1 
ATOM   1134 N  N   . ASP   A 1 156 ? 0.697   -20.085 70.720  1.00 19.99 ? 184 ASP   A N   1 
ATOM   1135 C  CA  . ASP   A 1 156 ? 0.862   -20.106 69.276  1.00 17.25 ? 184 ASP   A CA  1 
ATOM   1136 C  C   . ASP   A 1 156 ? 1.544   -18.853 68.757  1.00 18.41 ? 184 ASP   A C   1 
ATOM   1137 O  O   . ASP   A 1 156 ? 1.428   -18.540 67.569  1.00 19.15 ? 184 ASP   A O   1 
ATOM   1138 C  CB  . ASP   A 1 156 ? -0.492  -20.290 68.603  1.00 21.16 ? 184 ASP   A CB  1 
ATOM   1139 C  CG  . ASP   A 1 156 ? -1.120  -21.625 68.949  1.00 24.68 ? 184 ASP   A CG  1 
ATOM   1140 O  OD1 . ASP   A 1 156 ? -0.376  -22.627 68.998  1.00 23.94 ? 184 ASP   A OD1 1 
ATOM   1141 O  OD2 . ASP   A 1 156 ? -2.337  -21.659 69.198  1.00 24.29 ? 184 ASP   A OD2 1 
ATOM   1142 N  N   . VAL   A 1 157 ? 2.235   -18.126 69.624  1.00 16.57 ? 185 VAL   A N   1 
ATOM   1143 C  CA  . VAL   A 1 157 ? 3.010   -16.963 69.218  1.00 18.80 ? 185 VAL   A CA  1 
ATOM   1144 C  C   . VAL   A 1 157 ? 4.417   -17.425 68.853  1.00 20.60 ? 185 VAL   A C   1 
ATOM   1145 O  O   . VAL   A 1 157 ? 5.022   -18.239 69.564  1.00 20.51 ? 185 VAL   A O   1 
ATOM   1146 C  CB  . VAL   A 1 157 ? 3.052   -15.902 70.337  1.00 18.58 ? 185 VAL   A CB  1 
ATOM   1147 C  CG1 . VAL   A 1 157 ? 3.741   -14.616 69.815  1.00 14.57 ? 185 VAL   A CG1 1 
ATOM   1148 C  CG2 . VAL   A 1 157 ? 1.655   -15.610 70.883  1.00 12.33 ? 185 VAL   A CG2 1 
ATOM   1149 N  N   . VAL   A 1 158 ? 4.936   -16.919 67.738  1.00 19.05 ? 186 VAL   A N   1 
ATOM   1150 C  CA  . VAL   A 1 158 ? 6.286   -17.230 67.289  1.00 17.06 ? 186 VAL   A CA  1 
ATOM   1151 C  C   . VAL   A 1 158 ? 7.159   -15.994 67.464  1.00 21.23 ? 186 VAL   A C   1 
ATOM   1152 O  O   . VAL   A 1 158 ? 6.693   -14.842 67.375  1.00 18.25 ? 186 VAL   A O   1 
ATOM   1153 C  CB  . VAL   A 1 158 ? 6.316   -17.731 65.824  1.00 19.92 ? 186 VAL   A CB  1 
ATOM   1154 C  CG1 . VAL   A 1 158 ? 5.462   -18.994 65.661  1.00 18.77 ? 186 VAL   A CG1 1 
ATOM   1155 C  CG2 . VAL   A 1 158 ? 5.870   -16.642 64.852  1.00 15.49 ? 186 VAL   A CG2 1 
ATOM   1156 N  N   . LEU   A 1 159 ? 8.434   -16.247 67.770  1.00 21.43 ? 187 LEU   A N   1 
ATOM   1157 C  CA  . LEU   A 1 159 ? 9.479   -15.237 67.683  1.00 19.89 ? 187 LEU   A CA  1 
ATOM   1158 C  C   . LEU   A 1 159 ? 10.107  -15.371 66.305  1.00 21.41 ? 187 LEU   A C   1 
ATOM   1159 O  O   . LEU   A 1 159 ? 10.619  -16.443 65.956  1.00 17.98 ? 187 LEU   A O   1 
ATOM   1160 C  CB  . LEU   A 1 159 ? 10.529  -15.420 68.776  1.00 19.61 ? 187 LEU   A CB  1 
ATOM   1161 C  CG  . LEU   A 1 159 ? 11.603  -14.341 68.852  1.00 16.55 ? 187 LEU   A CG  1 
ATOM   1162 C  CD1 . LEU   A 1 159 ? 10.994  -13.042 69.337  1.00 18.09 ? 187 LEU   A CD1 1 
ATOM   1163 C  CD2 . LEU   A 1 159 ? 12.771  -14.781 69.758  1.00 17.67 ? 187 LEU   A CD2 1 
ATOM   1164 N  N   . ARG   A 1 160 ? 10.026  -14.301 65.514  1.00 19.06 ? 188 ARG   A N   1 
ATOM   1165 C  CA  . ARG   A 1 160 ? 10.436  -14.310 64.117  1.00 19.37 ? 188 ARG   A CA  1 
ATOM   1166 C  C   . ARG   A 1 160 ? 11.748  -13.552 63.971  1.00 21.02 ? 188 ARG   A C   1 
ATOM   1167 O  O   . ARG   A 1 160 ? 11.852  -12.401 64.407  1.00 22.32 ? 188 ARG   A O   1 
ATOM   1168 C  CB  . ARG   A 1 160 ? 9.349   -13.690 63.239  1.00 21.29 ? 188 ARG   A CB  1 
ATOM   1169 C  CG  . ARG   A 1 160 ? 9.749   -13.471 61.802  1.00 19.96 ? 188 ARG   A CG  1 
ATOM   1170 C  CD  . ARG   A 1 160 ? 8.610   -12.845 60.988  1.00 18.39 ? 188 ARG   A CD  1 
ATOM   1171 N  NE  . ARG   A 1 160 ? 7.559   -13.806 60.673  1.00 18.49 ? 188 ARG   A NE  1 
ATOM   1172 C  CZ  . ARG   A 1 160 ? 6.305   -13.466 60.397  1.00 17.69 ? 188 ARG   A CZ  1 
ATOM   1173 N  NH1 . ARG   A 1 160 ? 5.950   -12.188 60.402  1.00 13.81 ? 188 ARG   A NH1 1 
ATOM   1174 N  NH2 . ARG   A 1 160 ? 5.407   -14.403 60.101  1.00 15.14 ? 188 ARG   A NH2 1 
ATOM   1175 N  N   . TYR   A 1 161 ? 12.743  -14.201 63.364  1.00 20.68 ? 189 TYR   A N   1 
ATOM   1176 C  CA  . TYR   A 1 161 ? 14.025  -13.571 63.051  1.00 19.69 ? 189 TYR   A CA  1 
ATOM   1177 C  C   . TYR   A 1 161 ? 14.011  -13.093 61.608  1.00 17.95 ? 189 TYR   A C   1 
ATOM   1178 O  O   . TYR   A 1 161 ? 13.615  -13.836 60.708  1.00 21.97 ? 189 TYR   A O   1 
ATOM   1179 C  CB  . TYR   A 1 161 ? 15.190  -14.552 63.255  1.00 17.72 ? 189 TYR   A CB  1 
ATOM   1180 C  CG  . TYR   A 1 161 ? 15.252  -15.163 64.634  1.00 18.20 ? 189 TYR   A CG  1 
ATOM   1181 C  CD1 . TYR   A 1 161 ? 15.079  -14.380 65.776  1.00 16.17 ? 189 TYR   A CD1 1 
ATOM   1182 C  CD2 . TYR   A 1 161 ? 15.445  -16.534 64.797  1.00 20.62 ? 189 TYR   A CD2 1 
ATOM   1183 C  CE1 . TYR   A 1 161 ? 15.116  -14.948 67.042  1.00 19.24 ? 189 TYR   A CE1 1 
ATOM   1184 C  CE2 . TYR   A 1 161 ? 15.478  -17.109 66.062  1.00 17.69 ? 189 TYR   A CE2 1 
ATOM   1185 C  CZ  . TYR   A 1 161 ? 15.320  -16.316 67.173  1.00 19.99 ? 189 TYR   A CZ  1 
ATOM   1186 O  OH  . TYR   A 1 161 ? 15.350  -16.894 68.424  1.00 23.27 ? 189 TYR   A OH  1 
ATOM   1187 N  N   . VAL   A 1 162 ? 14.446  -11.856 61.389  1.00 19.51 ? 190 VAL   A N   1 
ATOM   1188 C  CA  . VAL   A 1 162 ? 14.620  -11.324 60.049  1.00 23.34 ? 190 VAL   A CA  1 
ATOM   1189 C  C   . VAL   A 1 162 ? 15.996  -10.679 59.974  1.00 25.99 ? 190 VAL   A C   1 
ATOM   1190 O  O   . VAL   A 1 162 ? 16.420  -10.001 60.917  1.00 26.89 ? 190 VAL   A O   1 
ATOM   1191 C  CB  . VAL   A 1 162 ? 13.506  -10.322 59.693  1.00 27.58 ? 190 VAL   A CB  1 
ATOM   1192 C  CG1 . VAL   A 1 162 ? 13.368  -9.278  60.778  1.00 29.60 ? 190 VAL   A CG1 1 
ATOM   1193 C  CG2 . VAL   A 1 162 ? 13.785  -9.679  58.361  1.00 32.68 ? 190 VAL   A CG2 1 
ATOM   1194 N  N   . SER   A 1 163 ? 16.709  -10.922 58.871  1.00 24.20 ? 191 SER   A N   1 
ATOM   1195 C  CA  . SER   A 1 163 ? 17.990  -10.272 58.614  1.00 29.40 ? 191 SER   A CA  1 
ATOM   1196 C  C   . SER   A 1 163 ? 18.080  -9.867  57.147  1.00 27.17 ? 191 SER   A C   1 
ATOM   1197 O  O   . SER   A 1 163 ? 17.551  -10.544 56.263  1.00 29.17 ? 191 SER   A O   1 
ATOM   1198 C  CB  . SER   A 1 163 ? 19.176  -11.180 58.980  1.00 26.57 ? 191 SER   A CB  1 
ATOM   1199 O  OG  . SER   A 1 163 ? 19.107  -12.408 58.281  1.00 24.01 ? 191 SER   A OG  1 
ATOM   1200 N  N   . TYR   A 1 164 ? 18.754  -8.749  56.904  1.00 27.50 ? 192 TYR   A N   1 
ATOM   1201 C  CA  . TYR   A 1 164 ? 18.893  -8.144  55.584  1.00 31.67 ? 192 TYR   A CA  1 
ATOM   1202 C  C   . TYR   A 1 164 ? 20.361  -8.130  55.187  1.00 33.23 ? 192 TYR   A C   1 
ATOM   1203 O  O   . TYR   A 1 164 ? 21.210  -7.699  55.974  1.00 32.91 ? 192 TYR   A O   1 
ATOM   1204 C  CB  . TYR   A 1 164 ? 18.358  -6.698  55.582  1.00 34.35 ? 192 TYR   A CB  1 
ATOM   1205 C  CG  . TYR   A 1 164 ? 16.896  -6.592  55.923  1.00 32.26 ? 192 TYR   A CG  1 
ATOM   1206 C  CD1 . TYR   A 1 164 ? 16.457  -6.744  57.228  1.00 34.69 ? 192 TYR   A CD1 1 
ATOM   1207 C  CD2 . TYR   A 1 164 ? 15.951  -6.342  54.934  1.00 33.00 ? 192 TYR   A CD2 1 
ATOM   1208 C  CE1 . TYR   A 1 164 ? 15.117  -6.667  57.541  1.00 36.36 ? 192 TYR   A CE1 1 
ATOM   1209 C  CE2 . TYR   A 1 164 ? 14.609  -6.259  55.233  1.00 33.46 ? 192 TYR   A CE2 1 
ATOM   1210 C  CZ  . TYR   A 1 164 ? 14.197  -6.421  56.537  1.00 36.98 ? 192 TYR   A CZ  1 
ATOM   1211 O  OH  . TYR   A 1 164 ? 12.858  -6.341  56.833  1.00 41.40 ? 192 TYR   A OH  1 
ATOM   1212 N  N   . LYS   A 1 165 ? 20.660  -8.582  53.967  1.00 38.61 ? 193 LYS   A N   1 
ATOM   1213 C  CA  . LYS   A 1 165 ? 21.992  -8.338  53.416  1.00 41.37 ? 193 LYS   A CA  1 
ATOM   1214 C  C   . LYS   A 1 165 ? 22.257  -6.842  53.311  1.00 40.29 ? 193 LYS   A C   1 
ATOM   1215 O  O   . LYS   A 1 165 ? 23.297  -6.351  53.767  1.00 42.22 ? 193 LYS   A O   1 
ATOM   1216 C  CB  . LYS   A 1 165 ? 22.145  -9.013  52.050  1.00 37.42 ? 193 LYS   A CB  1 
ATOM   1217 N  N   . ALA   A 1 166 ? 21.306  -6.096  52.747  1.00 35.01 ? 194 ALA   A N   1 
ATOM   1218 C  CA  . ALA   A 1 166 ? 21.446  -4.652  52.578  1.00 47.45 ? 194 ALA   A CA  1 
ATOM   1219 C  C   . ALA   A 1 166 ? 21.122  -3.889  53.861  1.00 41.62 ? 194 ALA   A C   1 
ATOM   1220 O  O   . ALA   A 1 166 ? 21.896  -3.897  54.814  1.00 45.55 ? 194 ALA   A O   1 
ATOM   1221 C  CB  . ALA   A 1 166 ? 20.551  -4.165  51.440  1.00 53.05 ? 194 ALA   A CB  1 
ATOM   1222 N  N   . PHE   A 1 174 ? 10.103  -3.661  52.946  1.00 34.65 ? 202 PHE   A N   1 
ATOM   1223 C  CA  . PHE   A 1 174 ? 9.722   -4.490  54.087  1.00 31.83 ? 202 PHE   A CA  1 
ATOM   1224 C  C   . PHE   A 1 174 ? 10.174  -5.923  53.833  1.00 29.88 ? 202 PHE   A C   1 
ATOM   1225 O  O   . PHE   A 1 174 ? 11.038  -6.438  54.527  1.00 30.52 ? 202 PHE   A O   1 
ATOM   1226 C  CB  . PHE   A 1 174 ? 8.204   -4.429  54.343  1.00 28.43 ? 202 PHE   A CB  1 
ATOM   1227 C  CG  . PHE   A 1 174 ? 7.741   -5.332  55.456  1.00 28.41 ? 202 PHE   A CG  1 
ATOM   1228 C  CD1 . PHE   A 1 174 ? 8.104   -5.069  56.773  1.00 25.67 ? 202 PHE   A CD1 1 
ATOM   1229 C  CD2 . PHE   A 1 174 ? 6.943   -6.447  55.190  1.00 26.41 ? 202 PHE   A CD2 1 
ATOM   1230 C  CE1 . PHE   A 1 174 ? 7.682   -5.899  57.813  1.00 24.54 ? 202 PHE   A CE1 1 
ATOM   1231 C  CE2 . PHE   A 1 174 ? 6.518   -7.300  56.230  1.00 23.27 ? 202 PHE   A CE2 1 
ATOM   1232 C  CZ  . PHE   A 1 174 ? 6.895   -7.024  57.540  1.00 20.31 ? 202 PHE   A CZ  1 
ATOM   1233 N  N   . LEU   A 1 175 ? 9.586   -6.567  52.835  1.00 28.79 ? 203 LEU   A N   1 
ATOM   1234 C  CA  . LEU   A 1 175 ? 9.991   -7.902  52.437  1.00 29.48 ? 203 LEU   A CA  1 
ATOM   1235 C  C   . LEU   A 1 175 ? 9.884   -8.000  50.926  1.00 30.39 ? 203 LEU   A C   1 
ATOM   1236 O  O   . LEU   A 1 175 ? 9.070   -7.295  50.314  1.00 31.55 ? 203 LEU   A O   1 
ATOM   1237 C  CB  . LEU   A 1 175 ? 9.124   -8.999  53.082  1.00 29.68 ? 203 LEU   A CB  1 
ATOM   1238 C  CG  . LEU   A 1 175 ? 9.256   -9.286  54.582  1.00 27.78 ? 203 LEU   A CG  1 
ATOM   1239 C  CD1 . LEU   A 1 175 ? 8.277   -10.400 55.007  1.00 22.01 ? 203 LEU   A CD1 1 
ATOM   1240 C  CD2 . LEU   A 1 175 ? 10.700  -9.648  54.944  1.00 32.80 ? 203 LEU   A CD2 1 
ATOM   1241 N  N   . PRO   A 1 176 ? 10.703  -8.844  50.296  1.00 32.76 ? 204 PRO   A N   1 
ATOM   1242 C  CA  . PRO   A 1 176 ? 10.499  -9.128  48.873  1.00 31.51 ? 204 PRO   A CA  1 
ATOM   1243 C  C   . PRO   A 1 176 ? 9.078   -9.617  48.628  1.00 31.99 ? 204 PRO   A C   1 
ATOM   1244 O  O   . PRO   A 1 176 ? 8.516   -10.383 49.419  1.00 31.52 ? 204 PRO   A O   1 
ATOM   1245 C  CB  . PRO   A 1 176 ? 11.539  -10.218 48.575  1.00 31.38 ? 204 PRO   A CB  1 
ATOM   1246 C  CG  . PRO   A 1 176 ? 12.613  -9.997  49.599  1.00 30.84 ? 204 PRO   A CG  1 
ATOM   1247 C  CD  . PRO   A 1 176 ? 11.865  -9.570  50.841  1.00 33.38 ? 204 PRO   A CD  1 
ATOM   1248 N  N   . GLY   A 1 177 ? 8.494   -9.161  47.522  1.00 28.24 ? 205 GLY   A N   1 
ATOM   1249 C  CA  . GLY   A 1 177 ? 7.126   -9.493  47.195  1.00 30.29 ? 205 GLY   A CA  1 
ATOM   1250 C  C   . GLY   A 1 177 ? 6.095   -8.505  47.701  1.00 28.15 ? 205 GLY   A C   1 
ATOM   1251 O  O   . GLY   A 1 177 ? 4.937   -8.556  47.260  1.00 29.15 ? 205 GLY   A O   1 
ATOM   1252 N  N   . PHE   A 1 178 ? 6.467   -7.620  48.618  1.00 27.95 ? 206 PHE   A N   1 
ATOM   1253 C  CA  . PHE   A 1 178 ? 5.573   -6.554  49.047  1.00 27.25 ? 206 PHE   A CA  1 
ATOM   1254 C  C   . PHE   A 1 178 ? 5.775   -5.356  48.134  1.00 26.65 ? 206 PHE   A C   1 
ATOM   1255 O  O   . PHE   A 1 178 ? 6.902   -5.038  47.755  1.00 32.13 ? 206 PHE   A O   1 
ATOM   1256 C  CB  . PHE   A 1 178 ? 5.844   -6.162  50.502  1.00 25.05 ? 206 PHE   A CB  1 
ATOM   1257 C  CG  . PHE   A 1 178 ? 5.221   -7.087  51.521  1.00 24.13 ? 206 PHE   A CG  1 
ATOM   1258 C  CD1 . PHE   A 1 178 ? 5.758   -8.354  51.761  1.00 22.93 ? 206 PHE   A CD1 1 
ATOM   1259 C  CD2 . PHE   A 1 178 ? 4.111   -6.673  52.264  1.00 18.45 ? 206 PHE   A CD2 1 
ATOM   1260 C  CE1 . PHE   A 1 178 ? 5.198   -9.201  52.701  1.00 19.87 ? 206 PHE   A CE1 1 
ATOM   1261 C  CE2 . PHE   A 1 178 ? 3.541   -7.512  53.210  1.00 20.06 ? 206 PHE   A CE2 1 
ATOM   1262 C  CZ  . PHE   A 1 178 ? 4.080   -8.786  53.426  1.00 20.72 ? 206 PHE   A CZ  1 
ATOM   1263 N  N   . GLU   A 1 179 ? 4.686   -4.706  47.764  1.00 29.11 ? 207 GLU   A N   1 
ATOM   1264 C  CA  . GLU   A 1 179 ? 4.757   -3.464  47.004  1.00 31.66 ? 207 GLU   A CA  1 
ATOM   1265 C  C   . GLU   A 1 179 ? 4.473   -2.276  47.917  1.00 30.25 ? 207 GLU   A C   1 
ATOM   1266 O  O   . GLU   A 1 179 ? 3.606   -2.348  48.796  1.00 27.96 ? 207 GLU   A O   1 
ATOM   1267 C  CB  . GLU   A 1 179 ? 3.760   -3.483  45.847  1.00 32.29 ? 207 GLU   A CB  1 
ATOM   1268 C  CG  . GLU   A 1 179 ? 3.911   -4.710  44.953  1.00 39.83 ? 207 GLU   A CG  1 
ATOM   1269 C  CD  . GLU   A 1 179 ? 3.189   -4.571  43.624  1.00 40.65 ? 207 GLU   A CD  1 
ATOM   1270 O  OE1 . GLU   A 1 179 ? 2.411   -3.595  43.462  1.00 39.48 ? 207 GLU   A OE1 1 
ATOM   1271 O  OE2 . GLU   A 1 179 ? 3.391   -5.453  42.758  1.00 37.77 ? 207 GLU   A OE2 1 
ATOM   1272 N  N   . ARG   A 1 180 ? 5.223   -1.191  47.712  1.00 33.32 ? 208 ARG   A N   1 
ATOM   1273 C  CA  . ARG   A 1 180 ? 4.933   0.071   48.386  1.00 34.87 ? 208 ARG   A CA  1 
ATOM   1274 C  C   . ARG   A 1 180 ? 3.554   0.571   47.968  1.00 37.42 ? 208 ARG   A C   1 
ATOM   1275 O  O   . ARG   A 1 180 ? 3.121   0.377   46.829  1.00 42.81 ? 208 ARG   A O   1 
ATOM   1276 C  CB  . ARG   A 1 180 ? 6.009   1.112   48.056  1.00 34.21 ? 208 ARG   A CB  1 
ATOM   1277 N  N   . VAL   A 1 181 ? 2.848   1.201   48.895  1.00 39.77 ? 209 VAL   A N   1 
ATOM   1278 C  CA  . VAL   A 1 181 ? 1.441   1.511   48.679  1.00 36.87 ? 209 VAL   A CA  1 
ATOM   1279 C  C   . VAL   A 1 181 ? 1.317   2.846   47.954  1.00 51.27 ? 209 VAL   A C   1 
ATOM   1280 O  O   . VAL   A 1 181 ? 2.016   3.815   48.289  1.00 48.15 ? 209 VAL   A O   1 
ATOM   1281 C  CB  . VAL   A 1 181 ? 0.669   1.506   50.005  1.00 34.82 ? 209 VAL   A CB  1 
ATOM   1282 C  CG1 . VAL   A 1 181 ? -0.689  2.188   49.847  1.00 37.89 ? 209 VAL   A CG1 1 
ATOM   1283 C  CG2 . VAL   A 1 181 ? 0.481   0.069   50.456  1.00 30.89 ? 209 VAL   A CG2 1 
ATOM   1284 N  N   . GLU   A 1 182 ? 0.430   2.877   46.944  1.00 52.99 ? 210 GLU   A N   1 
ATOM   1285 C  CA  . GLU   A 1 182 ? 0.256   4.027   46.061  1.00 55.63 ? 210 GLU   A CA  1 
ATOM   1286 C  C   . GLU   A 1 182 ? -0.211  5.252   46.836  1.00 54.12 ? 210 GLU   A C   1 
ATOM   1287 O  O   . GLU   A 1 182 ? -1.188  5.187   47.587  1.00 53.65 ? 210 GLU   A O   1 
ATOM   1288 C  CB  . GLU   A 1 182 ? -0.752  3.686   44.963  1.00 53.76 ? 210 GLU   A CB  1 
ATOM   1289 N  N   . ASP   A 1 183 ? 0.473   6.380   46.612  1.00 58.25 ? 211 ASP   A N   1 
ATOM   1290 C  CA  . ASP   A 1 183 ? 0.346   7.546   47.488  1.00 59.09 ? 211 ASP   A CA  1 
ATOM   1291 C  C   . ASP   A 1 183 ? -1.105  7.911   47.777  1.00 55.03 ? 211 ASP   A C   1 
ATOM   1292 O  O   . ASP   A 1 183 ? -1.438  8.285   48.907  1.00 57.16 ? 211 ASP   A O   1 
ATOM   1293 C  CB  . ASP   A 1 183 ? 1.078   8.745   46.882  1.00 61.41 ? 211 ASP   A CB  1 
ATOM   1294 C  CG  . ASP   A 1 183 ? 2.586   8.614   46.978  1.00 69.69 ? 211 ASP   A CG  1 
ATOM   1295 O  OD1 . ASP   A 1 183 ? 3.220   8.253   45.960  1.00 69.44 ? 211 ASP   A OD1 1 
ATOM   1296 O  OD2 . ASP   A 1 183 ? 3.134   8.851   48.080  1.00 73.06 ? 211 ASP   A OD2 1 
ATOM   1297 N  N   . ALA   A 1 184 ? -1.984  7.815   46.774  1.00 53.55 ? 212 ALA   A N   1 
ATOM   1298 C  CA  . ALA   A 1 184 ? -3.389  8.164   46.989  1.00 57.85 ? 212 ALA   A CA  1 
ATOM   1299 C  C   . ALA   A 1 184 ? -4.019  7.286   48.068  1.00 52.21 ? 212 ALA   A C   1 
ATOM   1300 O  O   . ALA   A 1 184 ? -4.783  7.770   48.913  1.00 45.55 ? 212 ALA   A O   1 
ATOM   1301 C  CB  . ALA   A 1 184 ? -4.171  8.051   45.677  1.00 56.93 ? 212 ALA   A CB  1 
ATOM   1302 N  N   . SER   A 1 185 ? -3.700  5.992   48.063  1.00 53.68 ? 213 SER   A N   1 
ATOM   1303 C  CA  . SER   A 1 185 ? -4.154  5.089   49.112  1.00 50.06 ? 213 SER   A CA  1 
ATOM   1304 C  C   . SER   A 1 185 ? -3.420  5.298   50.432  1.00 46.44 ? 213 SER   A C   1 
ATOM   1305 O  O   . SER   A 1 185 ? -3.905  4.840   51.472  1.00 42.63 ? 213 SER   A O   1 
ATOM   1306 C  CB  . SER   A 1 185 ? -3.992  3.636   48.649  1.00 49.39 ? 213 SER   A CB  1 
ATOM   1307 O  OG  . SER   A 1 185 ? -4.685  3.423   47.428  1.00 54.20 ? 213 SER   A OG  1 
ATOM   1308 N  N   . SER   A 1 186 ? -2.286  5.993   50.425  1.00 45.31 ? 214 SER   A N   1 
ATOM   1309 C  CA  . SER   A 1 186 ? -1.449  6.153   51.607  1.00 38.27 ? 214 SER   A CA  1 
ATOM   1310 C  C   . SER   A 1 186 ? -1.574  7.577   52.149  1.00 37.74 ? 214 SER   A C   1 
ATOM   1311 O  O   . SER   A 1 186 ? -0.824  8.470   51.745  1.00 43.41 ? 214 SER   A O   1 
ATOM   1312 C  CB  . SER   A 1 186 ? -0.005  5.816   51.264  1.00 38.90 ? 214 SER   A CB  1 
ATOM   1313 O  OG  . SER   A 1 186 ? 0.797   5.816   52.432  1.00 35.17 ? 214 SER   A OG  1 
ATOM   1314 N  N   . PHE   A 1 187 ? -2.511  7.779   53.092  1.00 34.34 ? 215 PHE   A N   1 
ATOM   1315 C  CA  . PHE   A 1 187 ? -2.740  9.045   53.794  1.00 28.44 ? 215 PHE   A CA  1 
ATOM   1316 C  C   . PHE   A 1 187 ? -1.763  9.175   54.958  1.00 31.49 ? 215 PHE   A C   1 
ATOM   1317 O  O   . PHE   A 1 187 ? -1.712  8.286   55.819  1.00 25.56 ? 215 PHE   A O   1 
ATOM   1318 C  CB  . PHE   A 1 187 ? -4.166  9.132   54.320  1.00 23.13 ? 215 PHE   A CB  1 
ATOM   1319 C  CG  . PHE   A 1 187 ? -4.600  10.533  54.684  1.00 22.49 ? 215 PHE   A CG  1 
ATOM   1320 C  CD1 . PHE   A 1 187 ? -4.177  11.134  55.863  1.00 19.39 ? 215 PHE   A CD1 1 
ATOM   1321 C  CD2 . PHE   A 1 187 ? -5.435  11.250  53.837  1.00 26.78 ? 215 PHE   A CD2 1 
ATOM   1322 C  CE1 . PHE   A 1 187 ? -4.575  12.427  56.198  1.00 25.04 ? 215 PHE   A CE1 1 
ATOM   1323 C  CE2 . PHE   A 1 187 ? -5.848  12.537  54.166  1.00 26.80 ? 215 PHE   A CE2 1 
ATOM   1324 C  CZ  . PHE   A 1 187 ? -5.408  13.132  55.350  1.00 23.04 ? 215 PHE   A CZ  1 
ATOM   1325 N  N   . PRO   A 1 188 ? -0.994  10.278  55.041  1.00 27.70 ? 216 PRO   A N   1 
ATOM   1326 C  CA  . PRO   A 1 188 ? 0.116   10.342  56.008  1.00 28.27 ? 216 PRO   A CA  1 
ATOM   1327 C  C   . PRO   A 1 188 ? -0.355  10.651  57.427  1.00 25.20 ? 216 PRO   A C   1 
ATOM   1328 O  O   . PRO   A 1 188 ? 0.017   11.659  58.029  1.00 24.52 ? 216 PRO   A O   1 
ATOM   1329 C  CB  . PRO   A 1 188 ? 1.000   11.451  55.417  1.00 25.29 ? 216 PRO   A CB  1 
ATOM   1330 C  CG  . PRO   A 1 188 ? 0.049   12.350  54.712  1.00 24.09 ? 216 PRO   A CG  1 
ATOM   1331 C  CD  . PRO   A 1 188 ? -1.015  11.443  54.138  1.00 27.99 ? 216 PRO   A CD  1 
ATOM   1332 N  N   . LEU   A 1 189 ? -1.177  9.767   57.985  1.00 19.75 ? 217 LEU   A N   1 
ATOM   1333 C  CA  . LEU   A 1 189 ? -1.560  9.940   59.378  1.00 21.07 ? 217 LEU   A CA  1 
ATOM   1334 C  C   . LEU   A 1 189 ? -0.343  9.759   60.274  1.00 19.91 ? 217 LEU   A C   1 
ATOM   1335 O  O   . LEU   A 1 189 ? 0.582   9.012   59.958  1.00 24.49 ? 217 LEU   A O   1 
ATOM   1336 C  CB  . LEU   A 1 189 ? -2.639  8.937   59.785  1.00 20.54 ? 217 LEU   A CB  1 
ATOM   1337 C  CG  . LEU   A 1 189 ? -4.015  8.981   59.141  1.00 20.09 ? 217 LEU   A CG  1 
ATOM   1338 C  CD1 . LEU   A 1 189 ? -4.797  7.710   59.553  1.00 15.74 ? 217 LEU   A CD1 1 
ATOM   1339 C  CD2 . LEU   A 1 189 ? -4.764  10.279  59.496  1.00 14.71 ? 217 LEU   A CD2 1 
ATOM   1340 N  N   . ASP   A 1 190 ? -0.357  10.446  61.411  1.00 22.45 ? 218 ASP   A N   1 
ATOM   1341 C  CA  . ASP   A 1 190 ? 0.703   10.324  62.398  1.00 21.35 ? 218 ASP   A CA  1 
ATOM   1342 C  C   . ASP   A 1 190 ? 0.259   10.973  63.696  1.00 22.57 ? 218 ASP   A C   1 
ATOM   1343 O  O   . ASP   A 1 190 ? 0.095   12.194  63.730  1.00 25.57 ? 218 ASP   A O   1 
ATOM   1344 C  CB  . ASP   A 1 190 ? 1.982   10.980  61.880  1.00 23.28 ? 218 ASP   A CB  1 
ATOM   1345 C  CG  . ASP   A 1 190 ? 3.131   10.900  62.870  1.00 27.76 ? 218 ASP   A CG  1 
ATOM   1346 O  OD1 . ASP   A 1 190 ? 3.015   10.166  63.878  1.00 23.53 ? 218 ASP   A OD1 1 
ATOM   1347 O  OD2 . ASP   A 1 190 ? 4.162   11.571  62.634  1.00 31.59 ? 218 ASP   A OD2 1 
ATOM   1348 N  N   . TYR   A 1 191 ? 0.073   10.196  64.770  1.00 17.13 ? 219 TYR   A N   1 
ATOM   1349 C  CA  . TYR   A 1 191 ? -0.290  10.779  66.058  1.00 17.73 ? 219 TYR   A CA  1 
ATOM   1350 C  C   . TYR   A 1 191 ? 0.875   10.790  67.031  1.00 18.74 ? 219 TYR   A C   1 
ATOM   1351 O  O   . TYR   A 1 191 ? 0.666   11.010  68.228  1.00 20.87 ? 219 TYR   A O   1 
ATOM   1352 C  CB  . TYR   A 1 191 ? -1.493  10.060  66.703  1.00 18.67 ? 219 TYR   A CB  1 
ATOM   1353 C  CG  . TYR   A 1 191 ? -2.680  9.809   65.784  1.00 17.67 ? 219 TYR   A CG  1 
ATOM   1354 C  CD1 . TYR   A 1 191 ? -2.891  10.584  64.635  1.00 18.53 ? 219 TYR   A CD1 1 
ATOM   1355 C  CD2 . TYR   A 1 191 ? -3.587  8.783   66.061  1.00 16.73 ? 219 TYR   A CD2 1 
ATOM   1356 C  CE1 . TYR   A 1 191 ? -3.970  10.340  63.781  1.00 17.03 ? 219 TYR   A CE1 1 
ATOM   1357 C  CE2 . TYR   A 1 191 ? -4.669  8.534   65.227  1.00 17.54 ? 219 TYR   A CE2 1 
ATOM   1358 C  CZ  . TYR   A 1 191 ? -4.850  9.305   64.077  1.00 19.54 ? 219 TYR   A CZ  1 
ATOM   1359 O  OH  . TYR   A 1 191 ? -5.903  9.026   63.231  1.00 16.78 ? 219 TYR   A OH  1 
ATOM   1360 N  N   . GLY   A 1 192 ? 2.096   10.559  66.558  1.00 21.19 ? 220 GLY   A N   1 
ATOM   1361 C  CA  . GLY   A 1 192 ? 3.269   10.637  67.403  1.00 20.90 ? 220 GLY   A CA  1 
ATOM   1362 C  C   . GLY   A 1 192 ? 3.871   9.307   67.826  1.00 22.16 ? 220 GLY   A C   1 
ATOM   1363 O  O   . GLY   A 1 192 ? 4.904   9.316   68.516  1.00 22.48 ? 220 GLY   A O   1 
ATOM   1364 N  N   . ILE   A 1 193 ? 3.281   8.166   67.458  1.00 18.73 ? 221 ILE   A N   1 
ATOM   1365 C  CA  . ILE   A 1 193 ? 3.861   6.878   67.855  1.00 15.32 ? 221 ILE   A CA  1 
ATOM   1366 C  C   . ILE   A 1 193 ? 5.081   6.576   66.997  1.00 17.89 ? 221 ILE   A C   1 
ATOM   1367 O  O   . ILE   A 1 193 ? 5.083   6.809   65.777  1.00 16.84 ? 221 ILE   A O   1 
ATOM   1368 C  CB  . ILE   A 1 193 ? 2.820   5.750   67.754  1.00 17.24 ? 221 ILE   A CB  1 
ATOM   1369 C  CG1 . ILE   A 1 193 ? 1.697   5.997   68.757  1.00 17.67 ? 221 ILE   A CG1 1 
ATOM   1370 C  CG2 . ILE   A 1 193 ? 3.475   4.369   68.006  1.00 14.89 ? 221 ILE   A CG2 1 
ATOM   1371 C  CD1 . ILE   A 1 193 ? 0.425   5.192   68.500  1.00 11.15 ? 221 ILE   A CD1 1 
ATOM   1372 N  N   . ARG   A 1 194 ? 6.133   6.032   67.629  1.00 17.35 ? 222 ARG   A N   1 
ATOM   1373 C  CA  . ARG   A 1 194 ? 7.426   5.910   66.971  1.00 18.04 ? 222 ARG   A CA  1 
ATOM   1374 C  C   . ARG   A 1 194 ? 8.032   4.506   66.961  1.00 19.08 ? 222 ARG   A C   1 
ATOM   1375 O  O   . ARG   A 1 194 ? 8.736   4.178   65.998  1.00 21.22 ? 222 ARG   A O   1 
ATOM   1376 C  CB  . ARG   A 1 194 ? 8.431   6.890   67.608  1.00 20.04 ? 222 ARG   A CB  1 
ATOM   1377 C  CG  . ARG   A 1 194 ? 8.147   8.370   67.242  1.00 15.23 ? 222 ARG   A CG  1 
ATOM   1378 C  CD  . ARG   A 1 194 ? 8.211   8.609   65.717  1.00 18.32 ? 222 ARG   A CD  1 
ATOM   1379 N  NE  . ARG   A 1 194 ? 7.774   9.954   65.310  1.00 20.72 ? 222 ARG   A NE  1 
ATOM   1380 C  CZ  . ARG   A 1 194 ? 6.559   10.268  64.851  1.00 24.24 ? 222 ARG   A CZ  1 
ATOM   1381 N  NH1 . ARG   A 1 194 ? 5.612   9.337   64.700  1.00 18.04 ? 222 ARG   A NH1 1 
ATOM   1382 N  NH2 . ARG   A 1 194 ? 6.291   11.520  64.506  1.00 18.79 ? 222 ARG   A NH2 1 
ATOM   1383 N  N   . ARG   A 1 195 ? 7.808   3.668   67.974  1.00 18.71 ? 223 ARG   A N   1 
ATOM   1384 C  CA  . ARG   A 1 195 ? 8.428   2.342   67.949  1.00 17.75 ? 223 ARG   A CA  1 
ATOM   1385 C  C   . ARG   A 1 195 ? 7.778   1.445   68.997  1.00 16.80 ? 223 ARG   A C   1 
ATOM   1386 O  O   . ARG   A 1 195 ? 7.074   1.915   69.893  1.00 17.10 ? 223 ARG   A O   1 
ATOM   1387 C  CB  . ARG   A 1 195 ? 9.945   2.435   68.180  1.00 17.27 ? 223 ARG   A CB  1 
ATOM   1388 C  CG  . ARG   A 1 195 ? 10.341  2.796   69.599  1.00 21.28 ? 223 ARG   A CG  1 
ATOM   1389 C  CD  . ARG   A 1 195 ? 11.879  2.876   69.772  1.00 24.91 ? 223 ARG   A CD  1 
ATOM   1390 N  NE  . ARG   A 1 195 ? 12.250  3.157   71.161  1.00 28.83 ? 223 ARG   A NE  1 
ATOM   1391 C  CZ  . ARG   A 1 195 ? 12.459  2.217   72.088  1.00 31.51 ? 223 ARG   A CZ  1 
ATOM   1392 N  NH1 . ARG   A 1 195 ? 12.357  0.929   71.775  1.00 24.13 ? 223 ARG   A NH1 1 
ATOM   1393 N  NH2 . ARG   A 1 195 ? 12.784  2.558   73.331  1.00 29.97 ? 223 ARG   A NH2 1 
ATOM   1394 N  N   . LEU   A 1 196 ? 8.040   0.138   68.883  1.00 15.03 ? 224 LEU   A N   1 
ATOM   1395 C  CA  . LEU   A 1 196 ? 7.591   -0.812  69.896  1.00 14.05 ? 224 LEU   A CA  1 
ATOM   1396 C  C   . LEU   A 1 196 ? 8.541   -0.786  71.082  1.00 15.33 ? 224 LEU   A C   1 
ATOM   1397 O  O   . LEU   A 1 196 ? 9.748   -0.971  70.923  1.00 17.07 ? 224 LEU   A O   1 
ATOM   1398 C  CB  . LEU   A 1 196 ? 7.511   -2.231  69.332  1.00 15.34 ? 224 LEU   A CB  1 
ATOM   1399 C  CG  . LEU   A 1 196 ? 6.921   -3.312  70.248  1.00 18.07 ? 224 LEU   A CG  1 
ATOM   1400 C  CD1 . LEU   A 1 196 ? 5.407   -3.078  70.565  1.00 11.78 ? 224 LEU   A CD1 1 
ATOM   1401 C  CD2 . LEU   A 1 196 ? 7.144   -4.703  69.654  1.00 13.52 ? 224 LEU   A CD2 1 
ATOM   1402 N  N   . ASP   A 1 197 ? 8.002   -0.552  72.274  1.00 15.92 ? 225 ASP   A N   1 
ATOM   1403 C  CA  . ASP   A 1 197 ? 8.844   -0.510  73.456  1.00 17.56 ? 225 ASP   A CA  1 
ATOM   1404 C  C   . ASP   A 1 197 ? 8.968   -1.876  74.121  1.00 21.34 ? 225 ASP   A C   1 
ATOM   1405 O  O   . ASP   A 1 197 ? 10.082  -2.275  74.497  1.00 18.80 ? 225 ASP   A O   1 
ATOM   1406 C  CB  . ASP   A 1 197 ? 8.300   0.507   74.453  1.00 19.47 ? 225 ASP   A CB  1 
ATOM   1407 C  CG  . ASP   A 1 197 ? 9.189   0.664   75.653  1.00 20.27 ? 225 ASP   A CG  1 
ATOM   1408 O  OD1 . ASP   A 1 197 ? 10.120  1.518   75.608  1.00 18.26 ? 225 ASP   A OD1 1 
ATOM   1409 O  OD2 . ASP   A 1 197 ? 8.941   -0.057  76.645  1.00 21.21 ? 225 ASP   A OD2 1 
ATOM   1410 N  N   . HIS   A 1 198 ? 7.849   -2.593  74.283  1.00 16.69 ? 226 HIS   A N   1 
ATOM   1411 C  CA  . HIS   A 1 198 ? 7.911   -3.970  74.769  1.00 17.48 ? 226 HIS   A CA  1 
ATOM   1412 C  C   . HIS   A 1 198 ? 6.676   -4.750  74.337  1.00 19.82 ? 226 HIS   A C   1 
ATOM   1413 O  O   . HIS   A 1 198 ? 5.645   -4.177  73.965  1.00 18.54 ? 226 HIS   A O   1 
ATOM   1414 C  CB  . HIS   A 1 198 ? 8.086   -4.035  76.293  1.00 21.61 ? 226 HIS   A CB  1 
ATOM   1415 C  CG  . HIS   A 1 198 ? 7.078   -3.251  77.087  1.00 18.58 ? 226 HIS   A CG  1 
ATOM   1416 N  ND1 . HIS   A 1 198 ? 7.259   -1.924  77.421  1.00 20.19 ? 226 HIS   A ND1 1 
ATOM   1417 C  CD2 . HIS   A 1 198 ? 5.929   -3.633  77.691  1.00 18.97 ? 226 HIS   A CD2 1 
ATOM   1418 C  CE1 . HIS   A 1 198 ? 6.256   -1.521  78.183  1.00 19.84 ? 226 HIS   A CE1 1 
ATOM   1419 N  NE2 . HIS   A 1 198 ? 5.428   -2.537  78.352  1.00 20.71 ? 226 HIS   A NE2 1 
ATOM   1420 N  N   . ALA   A 1 199 ? 6.792   -6.077  74.404  1.00 19.00 ? 227 ALA   A N   1 
ATOM   1421 C  CA  . ALA   A 1 199 ? 5.716   -6.978  74.010  1.00 16.99 ? 227 ALA   A CA  1 
ATOM   1422 C  C   . ALA   A 1 199 ? 5.568   -8.052  75.081  1.00 18.25 ? 227 ALA   A C   1 
ATOM   1423 O  O   . ALA   A 1 199 ? 6.507   -8.815  75.344  1.00 18.76 ? 227 ALA   A O   1 
ATOM   1424 C  CB  . ALA   A 1 199 ? 5.987   -7.592  72.631  1.00 15.61 ? 227 ALA   A CB  1 
ATOM   1425 N  N   . VAL   A 1 200 ? 4.384   -8.122  75.677  1.00 17.03 ? 228 VAL   A N   1 
ATOM   1426 C  CA  . VAL   A 1 200 ? 4.151   -8.844  76.918  1.00 17.65 ? 228 VAL   A CA  1 
ATOM   1427 C  C   . VAL   A 1 200 ? 3.332   -10.099 76.635  1.00 20.90 ? 228 VAL   A C   1 
ATOM   1428 O  O   . VAL   A 1 200 ? 2.258   -10.028 76.020  1.00 17.54 ? 228 VAL   A O   1 
ATOM   1429 C  CB  . VAL   A 1 200 ? 3.440   -7.952  77.946  1.00 20.26 ? 228 VAL   A CB  1 
ATOM   1430 C  CG1 . VAL   A 1 200 ? 3.179   -8.746  79.224  1.00 21.78 ? 228 VAL   A CG1 1 
ATOM   1431 C  CG2 . VAL   A 1 200 ? 4.276   -6.702  78.228  1.00 17.01 ? 228 VAL   A CG2 1 
ATOM   1432 N  N   . GLY   A 1 201 ? 3.824   -11.242 77.112  1.00 19.42 ? 229 GLY   A N   1 
ATOM   1433 C  CA  . GLY   A 1 201 ? 3.105   -12.502 77.001  1.00 18.68 ? 229 GLY   A CA  1 
ATOM   1434 C  C   . GLY   A 1 201 ? 2.438   -12.894 78.312  1.00 22.87 ? 229 GLY   A C   1 
ATOM   1435 O  O   . GLY   A 1 201 ? 2.958   -12.615 79.392  1.00 23.60 ? 229 GLY   A O   1 
ATOM   1436 N  N   . ASN   A 1 202 ? 1.273   -13.530 78.203  1.00 19.75 ? 230 ASN   A N   1 
ATOM   1437 C  CA  . ASN   A 1 202 ? 0.625   -14.191 79.337  1.00 19.83 ? 230 ASN   A CA  1 
ATOM   1438 C  C   . ASN   A 1 202 ? 0.777   -15.696 79.159  1.00 21.24 ? 230 ASN   A C   1 
ATOM   1439 O  O   . ASN   A 1 202 ? 0.553   -16.200 78.056  1.00 20.28 ? 230 ASN   A O   1 
ATOM   1440 C  CB  . ASN   A 1 202 ? -0.863  -13.816 79.430  1.00 17.06 ? 230 ASN   A CB  1 
ATOM   1441 C  CG  . ASN   A 1 202 ? -1.086  -12.444 80.059  1.00 22.44 ? 230 ASN   A CG  1 
ATOM   1442 O  OD1 . ASN   A 1 202 ? -0.158  -11.832 80.603  1.00 20.70 ? 230 ASN   A OD1 1 
ATOM   1443 N  ND2 . ASN   A 1 202 ? -2.329  -11.970 80.019  1.00 20.42 ? 230 ASN   A ND2 1 
ATOM   1444 N  N   . VAL   A 1 203 ? 1.182   -16.406 80.215  1.00 22.00 ? 231 VAL   A N   1 
ATOM   1445 C  CA  . VAL   A 1 203 ? 1.334   -17.864 80.169  1.00 24.10 ? 231 VAL   A CA  1 
ATOM   1446 C  C   . VAL   A 1 203 ? 0.748   -18.456 81.444  1.00 23.84 ? 231 VAL   A C   1 
ATOM   1447 O  O   . VAL   A 1 203 ? 0.530   -17.742 82.441  1.00 26.21 ? 231 VAL   A O   1 
ATOM   1448 C  CB  . VAL   A 1 203 ? 2.815   -18.295 80.008  1.00 23.09 ? 231 VAL   A CB  1 
ATOM   1449 C  CG1 . VAL   A 1 203 ? 3.454   -17.658 78.780  1.00 19.54 ? 231 VAL   A CG1 1 
ATOM   1450 C  CG2 . VAL   A 1 203 ? 3.595   -17.978 81.287  1.00 22.18 ? 231 VAL   A CG2 1 
ATOM   1451 N  N   . PRO   A 1 204 ? 0.475   -19.768 81.449  1.00 24.11 ? 232 PRO   A N   1 
ATOM   1452 C  CA  . PRO   A 1 204 ? -0.047  -20.381 82.686  1.00 28.21 ? 232 PRO   A CA  1 
ATOM   1453 C  C   . PRO   A 1 204 ? 1.015   -20.534 83.767  1.00 29.40 ? 232 PRO   A C   1 
ATOM   1454 O  O   . PRO   A 1 204 ? 0.680   -20.457 84.955  1.00 29.52 ? 232 PRO   A O   1 
ATOM   1455 C  CB  . PRO   A 1 204 ? -0.590  -21.748 82.219  1.00 27.84 ? 232 PRO   A CB  1 
ATOM   1456 C  CG  . PRO   A 1 204 ? 0.180   -22.063 80.987  1.00 29.02 ? 232 PRO   A CG  1 
ATOM   1457 C  CD  . PRO   A 1 204 ? 0.449   -20.717 80.312  1.00 24.13 ? 232 PRO   A CD  1 
ATOM   1458 N  N   . GLU   A 1 205 ? 2.283   -20.733 83.394  1.00 26.68 ? 233 GLU   A N   1 
ATOM   1459 C  CA  . GLU   A 1 205 ? 3.367   -20.916 84.360  1.00 31.46 ? 233 GLU   A CA  1 
ATOM   1460 C  C   . GLU   A 1 205 ? 4.577   -20.106 83.913  1.00 27.71 ? 233 GLU   A C   1 
ATOM   1461 O  O   . GLU   A 1 205 ? 5.189   -20.418 82.885  1.00 27.85 ? 233 GLU   A O   1 
ATOM   1462 C  CB  . GLU   A 1 205 ? 3.748   -22.392 84.496  1.00 33.15 ? 233 GLU   A CB  1 
ATOM   1463 C  CG  . GLU   A 1 205 ? 2.568   -23.318 84.698  1.00 34.28 ? 233 GLU   A CG  1 
ATOM   1464 C  CD  . GLU   A 1 205 ? 2.995   -24.713 85.106  1.00 42.32 ? 233 GLU   A CD  1 
ATOM   1465 O  OE1 . GLU   A 1 205 ? 2.558   -25.164 86.182  1.00 42.62 ? 233 GLU   A OE1 1 
ATOM   1466 O  OE2 . GLU   A 1 205 ? 3.782   -25.345 84.368  1.00 44.53 ? 233 GLU   A OE2 1 
ATOM   1467 N  N   . LEU   A 1 206 ? 4.956   -19.114 84.719  1.00 27.09 ? 234 LEU   A N   1 
ATOM   1468 C  CA  . LEU   A 1 206 ? 6.058   -18.221 84.366  1.00 28.60 ? 234 LEU   A CA  1 
ATOM   1469 C  C   . LEU   A 1 206 ? 7.402   -18.942 84.340  1.00 29.62 ? 234 LEU   A C   1 
ATOM   1470 O  O   . LEU   A 1 206 ? 8.244   -18.662 83.478  1.00 30.60 ? 234 LEU   A O   1 
ATOM   1471 C  CB  . LEU   A 1 206 ? 6.097   -17.060 85.356  1.00 29.11 ? 234 LEU   A CB  1 
ATOM   1472 C  CG  . LEU   A 1 206 ? 7.182   -16.000 85.217  1.00 33.90 ? 234 LEU   A CG  1 
ATOM   1473 C  CD1 . LEU   A 1 206 ? 7.035   -15.278 83.879  1.00 30.09 ? 234 LEU   A CD1 1 
ATOM   1474 C  CD2 . LEU   A 1 206 ? 7.081   -15.004 86.372  1.00 31.71 ? 234 LEU   A CD2 1 
ATOM   1475 N  N   . GLY   A 1 207 ? 7.630   -19.854 85.286  1.00 30.63 ? 235 GLY   A N   1 
ATOM   1476 C  CA  . GLY   A 1 207 ? 8.910   -20.510 85.444  1.00 30.16 ? 235 GLY   A CA  1 
ATOM   1477 C  C   . GLY   A 1 207 ? 9.424   -21.181 84.186  1.00 27.74 ? 235 GLY   A C   1 
ATOM   1478 O  O   . GLY   A 1 207 ? 10.486  -20.835 83.665  1.00 29.08 ? 235 GLY   A O   1 
ATOM   1479 N  N   . PRO   A 1 208 ? 8.681   -22.168 83.680  1.00 25.80 ? 236 PRO   A N   1 
ATOM   1480 C  CA  . PRO   A 1 208 ? 9.125   -22.858 82.458  1.00 28.54 ? 236 PRO   A CA  1 
ATOM   1481 C  C   . PRO   A 1 208 ? 9.163   -21.964 81.231  1.00 29.50 ? 236 PRO   A C   1 
ATOM   1482 O  O   . PRO   A 1 208 ? 10.001  -22.185 80.347  1.00 27.21 ? 236 PRO   A O   1 
ATOM   1483 C  CB  . PRO   A 1 208 ? 8.099   -23.987 82.301  1.00 26.29 ? 236 PRO   A CB  1 
ATOM   1484 C  CG  . PRO   A 1 208 ? 7.541   -24.184 83.674  1.00 30.37 ? 236 PRO   A CG  1 
ATOM   1485 C  CD  . PRO   A 1 208 ? 7.528   -22.835 84.306  1.00 28.99 ? 236 PRO   A CD  1 
ATOM   1486 N  N   . ALA   A 1 209 ? 8.286   -20.960 81.147  1.00 28.05 ? 237 ALA   A N   1 
ATOM   1487 C  CA  . ALA   A 1 209 ? 8.341   -20.025 80.026  1.00 26.98 ? 237 ALA   A CA  1 
ATOM   1488 C  C   . ALA   A 1 209 ? 9.646   -19.229 80.035  1.00 27.05 ? 237 ALA   A C   1 
ATOM   1489 O  O   . ALA   A 1 209 ? 10.333  -19.123 79.011  1.00 26.40 ? 237 ALA   A O   1 
ATOM   1490 C  CB  . ALA   A 1 209 ? 7.134   -19.092 80.078  1.00 22.77 ? 237 ALA   A CB  1 
ATOM   1491 N  N   . LEU   A 1 210 ? 9.994   -18.643 81.182  1.00 27.65 ? 238 LEU   A N   1 
ATOM   1492 C  CA  . LEU   A 1 210 ? 11.266  -17.932 81.312  1.00 26.80 ? 238 LEU   A CA  1 
ATOM   1493 C  C   . LEU   A 1 210 ? 12.438  -18.820 80.929  1.00 25.05 ? 238 LEU   A C   1 
ATOM   1494 O  O   . LEU   A 1 210 ? 13.250  -18.471 80.063  1.00 27.16 ? 238 LEU   A O   1 
ATOM   1495 C  CB  . LEU   A 1 210 ? 11.452  -17.429 82.743  1.00 27.26 ? 238 LEU   A CB  1 
ATOM   1496 C  CG  . LEU   A 1 210 ? 10.773  -16.124 83.142  1.00 36.14 ? 238 LEU   A CG  1 
ATOM   1497 C  CD1 . LEU   A 1 210 ? 11.083  -15.816 84.591  1.00 35.15 ? 238 LEU   A CD1 1 
ATOM   1498 C  CD2 . LEU   A 1 210 ? 11.241  -15.001 82.241  1.00 23.67 ? 238 LEU   A CD2 1 
ATOM   1499 N  N   . THR   A 1 211 ? 12.551  -19.966 81.595  1.00 26.92 ? 239 THR   A N   1 
ATOM   1500 C  CA  . THR   A 1 211 ? 13.654  -20.884 81.343  1.00 27.52 ? 239 THR   A CA  1 
ATOM   1501 C  C   . THR   A 1 211 ? 13.767  -21.235 79.861  1.00 26.95 ? 239 THR   A C   1 
ATOM   1502 O  O   . THR   A 1 211 ? 14.863  -21.208 79.292  1.00 27.84 ? 239 THR   A O   1 
ATOM   1503 C  CB  . THR   A 1 211 ? 13.449  -22.134 82.199  1.00 30.12 ? 239 THR   A CB  1 
ATOM   1504 O  OG1 . THR   A 1 211 ? 13.339  -21.730 83.571  1.00 34.13 ? 239 THR   A OG1 1 
ATOM   1505 C  CG2 . THR   A 1 211 ? 14.604  -23.097 82.039  1.00 30.33 ? 239 THR   A CG2 1 
ATOM   1506 N  N   . TYR   A 1 212 ? 12.637  -21.531 79.212  1.00 27.83 ? 240 TYR   A N   1 
ATOM   1507 C  CA  . TYR   A 1 212 ? 12.630  -21.818 77.780  1.00 26.35 ? 240 TYR   A CA  1 
ATOM   1508 C  C   . TYR   A 1 212 ? 13.180  -20.647 76.969  1.00 26.32 ? 240 TYR   A C   1 
ATOM   1509 O  O   . TYR   A 1 212 ? 14.154  -20.789 76.217  1.00 24.61 ? 240 TYR   A O   1 
ATOM   1510 C  CB  . TYR   A 1 212 ? 11.203  -22.151 77.336  1.00 27.07 ? 240 TYR   A CB  1 
ATOM   1511 C  CG  . TYR   A 1 212 ? 11.041  -22.246 75.833  1.00 29.49 ? 240 TYR   A CG  1 
ATOM   1512 C  CD1 . TYR   A 1 212 ? 11.625  -23.294 75.125  1.00 28.35 ? 240 TYR   A CD1 1 
ATOM   1513 C  CD2 . TYR   A 1 212 ? 10.303  -21.295 75.117  1.00 24.23 ? 240 TYR   A CD2 1 
ATOM   1514 C  CE1 . TYR   A 1 212 ? 11.491  -23.398 73.747  1.00 27.87 ? 240 TYR   A CE1 1 
ATOM   1515 C  CE2 . TYR   A 1 212 ? 10.159  -21.393 73.729  1.00 23.57 ? 240 TYR   A CE2 1 
ATOM   1516 C  CZ  . TYR   A 1 212 ? 10.753  -22.459 73.049  1.00 23.34 ? 240 TYR   A CZ  1 
ATOM   1517 O  OH  . TYR   A 1 212 ? 10.647  -22.589 71.669  1.00 19.36 ? 240 TYR   A OH  1 
ATOM   1518 N  N   . VAL   A 1 213 ? 12.561  -19.473 77.104  1.00 24.80 ? 241 VAL   A N   1 
ATOM   1519 C  CA  . VAL   A 1 213 ? 12.910  -18.353 76.234  1.00 25.01 ? 241 VAL   A CA  1 
ATOM   1520 C  C   . VAL   A 1 213 ? 14.313  -17.842 76.552  1.00 23.71 ? 241 VAL   A C   1 
ATOM   1521 O  O   . VAL   A 1 213 ? 15.145  -17.647 75.651  1.00 21.27 ? 241 VAL   A O   1 
ATOM   1522 C  CB  . VAL   A 1 213 ? 11.854  -17.236 76.351  1.00 26.80 ? 241 VAL   A CB  1 
ATOM   1523 C  CG1 . VAL   A 1 213 ? 12.224  -16.070 75.458  1.00 22.25 ? 241 VAL   A CG1 1 
ATOM   1524 C  CG2 . VAL   A 1 213 ? 10.474  -17.783 76.004  1.00 24.07 ? 241 VAL   A CG2 1 
ATOM   1525 N  N   . ALA   A 1 214 ? 14.593  -17.586 77.831  1.00 22.90 ? 242 ALA   A N   1 
ATOM   1526 C  CA  . ALA   A 1 214 ? 15.966  -17.241 78.198  1.00 25.28 ? 242 ALA   A CA  1 
ATOM   1527 C  C   . ALA   A 1 214 ? 16.931  -18.338 77.771  1.00 24.08 ? 242 ALA   A C   1 
ATOM   1528 O  O   . ALA   A 1 214 ? 18.074  -18.053 77.381  1.00 25.41 ? 242 ALA   A O   1 
ATOM   1529 C  CB  . ALA   A 1 214 ? 16.069  -16.997 79.708  1.00 22.72 ? 242 ALA   A CB  1 
ATOM   1530 N  N   . GLY   A 1 215 ? 16.476  -19.594 77.834  1.00 27.60 ? 243 GLY   A N   1 
ATOM   1531 C  CA  . GLY   A 1 215 ? 17.307  -20.710 77.412  1.00 27.35 ? 243 GLY   A CA  1 
ATOM   1532 C  C   . GLY   A 1 215 ? 17.838  -20.559 76.003  1.00 26.75 ? 243 GLY   A C   1 
ATOM   1533 O  O   . GLY   A 1 215 ? 19.038  -20.715 75.762  1.00 29.33 ? 243 GLY   A O   1 
ATOM   1534 N  N   . PHE   A 1 216 ? 16.961  -20.237 75.043  1.00 21.78 ? 244 PHE   A N   1 
ATOM   1535 C  CA  . PHE   A 1 216 ? 17.413  -20.286 73.658  1.00 20.34 ? 244 PHE   A CA  1 
ATOM   1536 C  C   . PHE   A 1 216 ? 17.897  -18.944 73.117  1.00 26.47 ? 244 PHE   A C   1 
ATOM   1537 O  O   . PHE   A 1 216 ? 18.590  -18.933 72.096  1.00 21.19 ? 244 PHE   A O   1 
ATOM   1538 C  CB  . PHE   A 1 216 ? 16.325  -20.915 72.736  1.00 24.85 ? 244 PHE   A CB  1 
ATOM   1539 C  CG  . PHE   A 1 216 ? 15.152  -20.020 72.378  1.00 22.91 ? 244 PHE   A CG  1 
ATOM   1540 C  CD1 . PHE   A 1 216 ? 13.902  -20.232 72.955  1.00 25.55 ? 244 PHE   A CD1 1 
ATOM   1541 C  CD2 . PHE   A 1 216 ? 15.275  -19.020 71.411  1.00 23.92 ? 244 PHE   A CD2 1 
ATOM   1542 C  CE1 . PHE   A 1 216 ? 12.802  -19.431 72.614  1.00 24.00 ? 244 PHE   A CE1 1 
ATOM   1543 C  CE2 . PHE   A 1 216 ? 14.184  -18.212 71.058  1.00 23.83 ? 244 PHE   A CE2 1 
ATOM   1544 C  CZ  . PHE   A 1 216 ? 12.945  -18.418 71.657  1.00 20.83 ? 244 PHE   A CZ  1 
ATOM   1545 N  N   . THR   A 1 217 ? 17.587  -17.824 73.780  1.00 23.44 ? 245 THR   A N   1 
ATOM   1546 C  CA  . THR   A 1 217 ? 18.037  -16.523 73.298  1.00 25.97 ? 245 THR   A CA  1 
ATOM   1547 C  C   . THR   A 1 217 ? 19.318  -16.052 73.958  1.00 25.75 ? 245 THR   A C   1 
ATOM   1548 O  O   . THR   A 1 217 ? 20.136  -15.405 73.299  1.00 23.46 ? 245 THR   A O   1 
ATOM   1549 C  CB  . THR   A 1 217 ? 16.987  -15.422 73.530  1.00 23.66 ? 245 THR   A CB  1 
ATOM   1550 O  OG1 . THR   A 1 217 ? 16.759  -15.256 74.939  1.00 24.31 ? 245 THR   A OG1 1 
ATOM   1551 C  CG2 . THR   A 1 217 ? 15.662  -15.705 72.790  1.00 22.69 ? 245 THR   A CG2 1 
ATOM   1552 N  N   . GLY   A 1 218 ? 19.502  -16.359 75.236  1.00 26.60 ? 246 GLY   A N   1 
ATOM   1553 C  CA  . GLY   A 1 218 ? 20.527  -15.707 76.017  1.00 28.12 ? 246 GLY   A CA  1 
ATOM   1554 C  C   . GLY   A 1 218 ? 20.087  -14.393 76.610  1.00 28.37 ? 246 GLY   A C   1 
ATOM   1555 O  O   . GLY   A 1 218 ? 20.924  -13.679 77.173  1.00 30.09 ? 246 GLY   A O   1 
ATOM   1556 N  N   . PHE   A 1 219 ? 18.806  -14.041 76.472  1.00 26.95 ? 247 PHE   A N   1 
ATOM   1557 C  CA  . PHE   A 1 219 ? 18.292  -12.801 77.040  1.00 29.17 ? 247 PHE   A CA  1 
ATOM   1558 C  C   . PHE   A 1 219 ? 18.367  -12.869 78.557  1.00 29.33 ? 247 PHE   A C   1 
ATOM   1559 O  O   . PHE   A 1 219 ? 18.084  -13.908 79.157  1.00 29.48 ? 247 PHE   A O   1 
ATOM   1560 C  CB  . PHE   A 1 219 ? 16.834  -12.551 76.612  1.00 27.66 ? 247 PHE   A CB  1 
ATOM   1561 C  CG  . PHE   A 1 219 ? 16.664  -12.172 75.162  1.00 26.71 ? 247 PHE   A CG  1 
ATOM   1562 C  CD1 . PHE   A 1 219 ? 17.766  -11.846 74.370  1.00 24.89 ? 247 PHE   A CD1 1 
ATOM   1563 C  CD2 . PHE   A 1 219 ? 15.398  -12.129 74.596  1.00 24.06 ? 247 PHE   A CD2 1 
ATOM   1564 C  CE1 . PHE   A 1 219 ? 17.607  -11.495 73.046  1.00 23.34 ? 247 PHE   A CE1 1 
ATOM   1565 C  CE2 . PHE   A 1 219 ? 15.227  -11.775 73.271  1.00 26.26 ? 247 PHE   A CE2 1 
ATOM   1566 C  CZ  . PHE   A 1 219 ? 16.334  -11.453 72.493  1.00 26.87 ? 247 PHE   A CZ  1 
ATOM   1567 N  N   . HIS   A 1 220 ? 18.728  -11.752 79.176  1.00 29.15 ? 248 HIS   A N   1 
ATOM   1568 C  CA  . HIS   A 1 220 ? 18.871  -11.674 80.620  1.00 28.81 ? 248 HIS   A CA  1 
ATOM   1569 C  C   . HIS   A 1 220 ? 17.643  -11.042 81.264  1.00 29.02 ? 248 HIS   A C   1 
ATOM   1570 O  O   . HIS   A 1 220 ? 16.887  -10.305 80.629  1.00 30.24 ? 248 HIS   A O   1 
ATOM   1571 C  CB  . HIS   A 1 220 ? 20.122  -10.873 80.990  1.00 28.84 ? 248 HIS   A CB  1 
ATOM   1572 C  CG  . HIS   A 1 220 ? 20.064  -9.437  80.572  1.00 31.24 ? 248 HIS   A CG  1 
ATOM   1573 N  ND1 . HIS   A 1 220 ? 20.382  -9.021  79.297  1.00 30.25 ? 248 HIS   A ND1 1 
ATOM   1574 C  CD2 . HIS   A 1 220 ? 19.723  -8.320  81.259  1.00 29.57 ? 248 HIS   A CD2 1 
ATOM   1575 C  CE1 . HIS   A 1 220 ? 20.236  -7.710  79.215  1.00 30.08 ? 248 HIS   A CE1 1 
ATOM   1576 N  NE2 . HIS   A 1 220 ? 19.846  -7.260  80.394  1.00 31.12 ? 248 HIS   A NE2 1 
ATOM   1577 N  N   . GLN   A 1 221 ? 17.467  -11.330 82.552  1.00 26.68 ? 249 GLN   A N   1 
ATOM   1578 C  CA  . GLN   A 1 221 ? 16.393  -10.737 83.339  1.00 31.47 ? 249 GLN   A CA  1 
ATOM   1579 C  C   . GLN   A 1 221 ? 16.650  -9.248  83.560  1.00 34.01 ? 249 GLN   A C   1 
ATOM   1580 O  O   . GLN   A 1 221 ? 17.707  -8.858  84.068  1.00 37.95 ? 249 GLN   A O   1 
ATOM   1581 C  CB  . GLN   A 1 221 ? 16.265  -11.454 84.677  1.00 31.39 ? 249 GLN   A CB  1 
ATOM   1582 C  CG  . GLN   A 1 221 ? 15.200  -10.866 85.579  1.00 42.16 ? 249 GLN   A CG  1 
ATOM   1583 C  CD  . GLN   A 1 221 ? 14.448  -11.932 86.345  1.00 42.34 ? 249 GLN   A CD  1 
ATOM   1584 O  OE1 . GLN   A 1 221 ? 14.716  -13.123 86.193  1.00 40.83 ? 249 GLN   A OE1 1 
ATOM   1585 N  NE2 . GLN   A 1 221 ? 13.499  -11.510 87.171  1.00 43.62 ? 249 GLN   A NE2 1 
ATOM   1586 N  N   . PHE   A 1 222 ? 15.679  -8.417  83.186  1.00 34.20 ? 250 PHE   A N   1 
ATOM   1587 C  CA  . PHE   A 1 222 ? 15.877  -6.973  83.227  1.00 35.32 ? 250 PHE   A CA  1 
ATOM   1588 C  C   . PHE   A 1 222 ? 15.578  -6.407  84.612  1.00 39.86 ? 250 PHE   A C   1 
ATOM   1589 O  O   . PHE   A 1 222 ? 16.377  -5.634  85.156  1.00 46.22 ? 250 PHE   A O   1 
ATOM   1590 C  CB  . PHE   A 1 222 ? 15.019  -6.297  82.156  1.00 32.53 ? 250 PHE   A CB  1 
ATOM   1591 C  CG  . PHE   A 1 222 ? 15.087  -4.795  82.180  1.00 35.47 ? 250 PHE   A CG  1 
ATOM   1592 C  CD1 . PHE   A 1 222 ? 14.210  -4.054  82.961  1.00 38.02 ? 250 PHE   A CD1 1 
ATOM   1593 C  CD2 . PHE   A 1 222 ? 16.032  -4.121  81.426  1.00 36.40 ? 250 PHE   A CD2 1 
ATOM   1594 C  CE1 . PHE   A 1 222 ? 14.275  -2.676  82.990  1.00 36.45 ? 250 PHE   A CE1 1 
ATOM   1595 C  CE2 . PHE   A 1 222 ? 16.097  -2.734  81.449  1.00 38.37 ? 250 PHE   A CE2 1 
ATOM   1596 C  CZ  . PHE   A 1 222 ? 15.217  -2.013  82.238  1.00 34.89 ? 250 PHE   A CZ  1 
ATOM   1597 N  N   . ALA   A 1 223 ? 14.445  -6.783  85.197  1.00 39.17 ? 251 ALA   A N   1 
ATOM   1598 C  CA  . ALA   A 1 223 ? 14.041  -6.274  86.518  1.00 54.47 ? 251 ALA   A CA  1 
ATOM   1599 C  C   . ALA   A 1 223 ? 14.024  -4.739  86.585  1.00 53.55 ? 251 ALA   A C   1 
ATOM   1600 O  O   . ALA   A 1 223 ? 15.044  -4.094  86.853  1.00 54.28 ? 251 ALA   A O   1 
ATOM   1601 C  CB  . ALA   A 1 223 ? 14.954  -6.843  87.614  1.00 55.34 ? 251 ALA   A CB  1 
ATOM   1602 N  N   . GLU   A 1 234 ? -2.630  -8.826  95.279  1.00 51.33 ? 262 GLU   A N   1 
ATOM   1603 C  CA  . GLU   A 1 234 ? -3.196  -7.549  94.856  1.00 58.53 ? 262 GLU   A CA  1 
ATOM   1604 C  C   . GLU   A 1 234 ? -3.067  -7.350  93.344  1.00 60.52 ? 262 GLU   A C   1 
ATOM   1605 O  O   . GLU   A 1 234 ? -4.002  -6.896  92.684  1.00 62.82 ? 262 GLU   A O   1 
ATOM   1606 C  CB  . GLU   A 1 234 ? -2.521  -6.390  95.600  1.00 54.02 ? 262 GLU   A CB  1 
ATOM   1607 N  N   . SER   A 1 235 ? -1.902  -7.700  92.795  1.00 61.37 ? 263 SER   A N   1 
ATOM   1608 C  CA  . SER   A 1 235 ? -1.681  -7.531  91.361  1.00 61.02 ? 263 SER   A CA  1 
ATOM   1609 C  C   . SER   A 1 235 ? -2.477  -8.543  90.543  1.00 58.13 ? 263 SER   A C   1 
ATOM   1610 O  O   . SER   A 1 235 ? -3.049  -8.197  89.501  1.00 55.27 ? 263 SER   A O   1 
ATOM   1611 C  CB  . SER   A 1 235 ? -0.193  -7.659  91.040  1.00 58.47 ? 263 SER   A CB  1 
ATOM   1612 O  OG  . SER   A 1 235 ? 0.099   -7.092  89.777  1.00 60.16 ? 263 SER   A OG  1 
ATOM   1613 N  N   . GLY   A 1 236 ? -2.515  -9.797  90.995  1.00 48.89 ? 264 GLY   A N   1 
ATOM   1614 C  CA  . GLY   A 1 236 ? -3.043  -10.886 90.208  1.00 47.50 ? 264 GLY   A CA  1 
ATOM   1615 C  C   . GLY   A 1 236 ? -2.021  -11.605 89.354  1.00 42.20 ? 264 GLY   A C   1 
ATOM   1616 O  O   . GLY   A 1 236 ? -2.353  -12.642 88.762  1.00 40.97 ? 264 GLY   A O   1 
ATOM   1617 N  N   . LEU   A 1 237 ? -0.787  -11.104 89.287  1.00 41.30 ? 265 LEU   A N   1 
ATOM   1618 C  CA  . LEU   A 1 237 ? 0.227   -11.666 88.409  1.00 38.81 ? 265 LEU   A CA  1 
ATOM   1619 C  C   . LEU   A 1 237 ? 1.574   -11.736 89.115  1.00 36.10 ? 265 LEU   A C   1 
ATOM   1620 O  O   . LEU   A 1 237 ? 1.811   -11.076 90.125  1.00 38.45 ? 265 LEU   A O   1 
ATOM   1621 C  CB  . LEU   A 1 237 ? 0.363   -10.841 87.116  1.00 38.16 ? 265 LEU   A CB  1 
ATOM   1622 C  CG  . LEU   A 1 237 ? 0.827   -9.379  87.215  1.00 41.15 ? 265 LEU   A CG  1 
ATOM   1623 C  CD1 . LEU   A 1 237 ? 2.329   -9.242  86.999  1.00 39.09 ? 265 LEU   A CD1 1 
ATOM   1624 C  CD2 . LEU   A 1 237 ? 0.060   -8.484  86.253  1.00 36.08 ? 265 LEU   A CD2 1 
ATOM   1625 N  N   . ASN   A 1 238 ? 2.433   -12.591 88.578  1.00 35.48 ? 266 ASN   A N   1 
ATOM   1626 C  CA  . ASN   A 1 238 ? 3.875   -12.515 88.733  1.00 36.50 ? 266 ASN   A CA  1 
ATOM   1627 C  C   . ASN   A 1 238 ? 4.470   -12.356 87.345  1.00 37.64 ? 266 ASN   A C   1 
ATOM   1628 O  O   . ASN   A 1 238 ? 3.915   -12.859 86.359  1.00 35.49 ? 266 ASN   A O   1 
ATOM   1629 C  CB  . ASN   A 1 238 ? 4.467   -13.769 89.389  1.00 34.97 ? 266 ASN   A CB  1 
ATOM   1630 C  CG  . ASN   A 1 238 ? 3.928   -14.009 90.765  1.00 36.39 ? 266 ASN   A CG  1 
ATOM   1631 O  OD1 . ASN   A 1 238 ? 3.854   -13.087 91.574  1.00 43.43 ? 266 ASN   A OD1 1 
ATOM   1632 N  ND2 . ASN   A 1 238 ? 3.534   -15.245 91.042  1.00 33.30 ? 266 ASN   A ND2 1 
ATOM   1633 N  N   . SER   A 1 239 ? 5.603   -11.670 87.261  1.00 36.53 ? 267 SER   A N   1 
ATOM   1634 C  CA  . SER   A 1 239 ? 6.197   -11.431 85.960  1.00 35.33 ? 267 SER   A CA  1 
ATOM   1635 C  C   . SER   A 1 239 ? 7.713   -11.416 86.074  1.00 35.90 ? 267 SER   A C   1 
ATOM   1636 O  O   . SER   A 1 239 ? 8.290   -11.555 87.153  1.00 40.27 ? 267 SER   A O   1 
ATOM   1637 C  CB  . SER   A 1 239 ? 5.685   -10.126 85.352  1.00 31.64 ? 267 SER   A CB  1 
ATOM   1638 O  OG  . SER   A 1 239 ? 6.069   -9.018  86.145  1.00 43.47 ? 267 SER   A OG  1 
ATOM   1639 N  N   . ALA   A 1 240 ? 8.347   -11.255 84.925  1.00 33.05 ? 268 ALA   A N   1 
ATOM   1640 C  CA  . ALA   A 1 240 ? 9.774   -11.082 84.765  1.00 31.09 ? 268 ALA   A CA  1 
ATOM   1641 C  C   . ALA   A 1 240 ? 9.997   -10.652 83.326  1.00 27.24 ? 268 ALA   A C   1 
ATOM   1642 O  O   . ALA   A 1 240 ? 9.191   -10.959 82.438  1.00 28.47 ? 268 ALA   A O   1 
ATOM   1643 C  CB  . ALA   A 1 240 ? 10.547  -12.364 85.085  1.00 30.09 ? 268 ALA   A CB  1 
ATOM   1644 N  N   . VAL   A 1 241 ? 11.087  -9.933  83.106  1.00 28.68 ? 269 VAL   A N   1 
ATOM   1645 C  CA  . VAL   A 1 241 ? 11.368  -9.319  81.818  1.00 24.71 ? 269 VAL   A CA  1 
ATOM   1646 C  C   . VAL   A 1 241 ? 12.664  -9.888  81.285  1.00 26.62 ? 269 VAL   A C   1 
ATOM   1647 O  O   . VAL   A 1 241 ? 13.699  -9.811  81.956  1.00 28.63 ? 269 VAL   A O   1 
ATOM   1648 C  CB  . VAL   A 1 241 ? 11.483  -7.793  81.939  1.00 21.58 ? 269 VAL   A CB  1 
ATOM   1649 C  CG1 . VAL   A 1 241 ? 11.670  -7.180  80.565  1.00 20.41 ? 269 VAL   A CG1 1 
ATOM   1650 C  CG2 . VAL   A 1 241 ? 10.285  -7.263  82.658  1.00 21.73 ? 269 VAL   A CG2 1 
ATOM   1651 N  N   . LEU   A 1 242 ? 12.621  -10.416 80.074  1.00 25.23 ? 270 LEU   A N   1 
ATOM   1652 C  CA  . LEU   A 1 242 ? 13.834  -10.796 79.369  1.00 27.30 ? 270 LEU   A CA  1 
ATOM   1653 C  C   . LEU   A 1 242 ? 14.248  -9.667  78.436  1.00 26.76 ? 270 LEU   A C   1 
ATOM   1654 O  O   . LEU   A 1 242 ? 13.400  -8.969  77.881  1.00 26.96 ? 270 LEU   A O   1 
ATOM   1655 C  CB  . LEU   A 1 242 ? 13.603  -12.087 78.595  1.00 24.68 ? 270 LEU   A CB  1 
ATOM   1656 C  CG  . LEU   A 1 242 ? 13.281  -13.266 79.510  1.00 28.03 ? 270 LEU   A CG  1 
ATOM   1657 C  CD1 . LEU   A 1 242 ? 12.906  -14.497 78.691  1.00 26.33 ? 270 LEU   A CD1 1 
ATOM   1658 C  CD2 . LEU   A 1 242 ? 14.471  -13.574 80.429  1.00 26.08 ? 270 LEU   A CD2 1 
ATOM   1659 N  N   . ALA   A 1 243 ? 15.553  -9.480  78.270  1.00 28.00 ? 271 ALA   A N   1 
ATOM   1660 C  CA  . ALA   A 1 243 ? 16.045  -8.340  77.508  1.00 30.66 ? 271 ALA   A CA  1 
ATOM   1661 C  C   . ALA   A 1 243 ? 17.308  -8.721  76.755  1.00 27.64 ? 271 ALA   A C   1 
ATOM   1662 O  O   . ALA   A 1 243 ? 18.105  -9.539  77.219  1.00 28.81 ? 271 ALA   A O   1 
ATOM   1663 C  CB  . ALA   A 1 243 ? 16.318  -7.127  78.415  1.00 29.70 ? 271 ALA   A CB  1 
ATOM   1664 N  N   . SER   A 1 244 ? 17.475  -8.123  75.581  1.00 27.88 ? 272 SER   A N   1 
ATOM   1665 C  CA  . SER   A 1 244 ? 18.675  -8.331  74.789  1.00 29.04 ? 272 SER   A CA  1 
ATOM   1666 C  C   . SER   A 1 244 ? 19.838  -7.552  75.412  1.00 29.75 ? 272 SER   A C   1 
ATOM   1667 O  O   . SER   A 1 244 ? 19.688  -6.873  76.435  1.00 27.93 ? 272 SER   A O   1 
ATOM   1668 C  CB  . SER   A 1 244 ? 18.428  -7.921  73.338  1.00 25.94 ? 272 SER   A CB  1 
ATOM   1669 O  OG  . SER   A 1 244 ? 18.061  -6.548  73.248  1.00 22.66 ? 272 SER   A OG  1 
ATOM   1670 N  N   . ASN   A 1 245 ? 21.011  -7.643  74.772  1.00 25.75 ? 273 ASN   A N   1 
ATOM   1671 C  CA  . ASN   A 1 245 ? 22.237  -7.079  75.341  1.00 27.54 ? 273 ASN   A CA  1 
ATOM   1672 C  C   . ASN   A 1 245 ? 22.098  -5.581  75.626  1.00 31.10 ? 273 ASN   A C   1 
ATOM   1673 O  O   . ASN   A 1 245 ? 22.442  -5.111  76.719  1.00 31.96 ? 273 ASN   A O   1 
ATOM   1674 C  CB  . ASN   A 1 245 ? 23.409  -7.342  74.394  1.00 27.87 ? 273 ASN   A CB  1 
ATOM   1675 C  CG  . ASN   A 1 245 ? 23.973  -8.740  74.541  1.00 29.06 ? 273 ASN   A CG  1 
ATOM   1676 O  OD1 . ASN   A 1 245 ? 23.530  -9.519  75.393  1.00 25.83 ? 273 ASN   A OD1 1 
ATOM   1677 N  ND2 . ASN   A 1 245 ? 24.916  -9.084  73.678  1.00 25.39 ? 273 ASN   A ND2 1 
ATOM   1678 N  N   . ASP   A 1 246 ? 21.598  -4.814  74.660  1.00 25.30 ? 274 ASP   A N   1 
ATOM   1679 C  CA  . ASP   A 1 246 ? 21.443  -3.378  74.860  1.00 27.87 ? 274 ASP   A CA  1 
ATOM   1680 C  C   . ASP   A 1 246 ? 20.084  -3.018  75.461  1.00 32.14 ? 274 ASP   A C   1 
ATOM   1681 O  O   . ASP   A 1 246 ? 19.774  -1.827  75.615  1.00 29.56 ? 274 ASP   A O   1 
ATOM   1682 C  CB  . ASP   A 1 246 ? 21.688  -2.615  73.539  1.00 24.23 ? 274 ASP   A CB  1 
ATOM   1683 C  CG  . ASP   A 1 246 ? 20.684  -2.962  72.430  1.00 32.72 ? 274 ASP   A CG  1 
ATOM   1684 O  OD1 . ASP   A 1 246 ? 19.614  -3.563  72.701  1.00 32.36 ? 274 ASP   A OD1 1 
ATOM   1685 O  OD2 . ASP   A 1 246 ? 20.968  -2.614  71.268  1.00 33.62 ? 274 ASP   A OD2 1 
ATOM   1686 N  N   . GLU   A 1 247 ? 19.277  -4.026  75.794  1.00 29.30 ? 275 GLU   A N   1 
ATOM   1687 C  CA  . GLU   A 1 247 ? 18.006  -3.866  76.503  1.00 26.86 ? 275 GLU   A CA  1 
ATOM   1688 C  C   . GLU   A 1 247 ? 16.998  -3.017  75.725  1.00 29.94 ? 275 GLU   A C   1 
ATOM   1689 O  O   . GLU   A 1 247 ? 16.158  -2.328  76.316  1.00 26.31 ? 275 GLU   A O   1 
ATOM   1690 C  CB  . GLU   A 1 247 ? 18.243  -3.314  77.907  1.00 30.19 ? 275 GLU   A CB  1 
ATOM   1691 C  CG  . GLU   A 1 247 ? 19.280  -4.140  78.664  1.00 32.24 ? 275 GLU   A CG  1 
ATOM   1692 C  CD  . GLU   A 1 247 ? 19.328  -3.800  80.128  1.00 34.90 ? 275 GLU   A CD  1 
ATOM   1693 O  OE1 . GLU   A 1 247 ? 19.389  -4.726  80.961  1.00 34.53 ? 275 GLU   A OE1 1 
ATOM   1694 O  OE2 . GLU   A 1 247 ? 19.305  -2.593  80.443  1.00 37.14 ? 275 GLU   A OE2 1 
ATOM   1695 N  N   . MET   A 1 248 ? 17.058  -3.085  74.390  1.00 26.82 ? 276 MET   A N   1 
ATOM   1696 C  CA  . MET   A 1 248 ? 16.041  -2.498  73.531  1.00 25.93 ? 276 MET   A CA  1 
ATOM   1697 C  C   . MET   A 1 248 ? 14.965  -3.489  73.102  1.00 25.83 ? 276 MET   A C   1 
ATOM   1698 O  O   . MET   A 1 248 ? 13.882  -3.064  72.687  1.00 26.44 ? 276 MET   A O   1 
ATOM   1699 C  CB  . MET   A 1 248 ? 16.686  -1.900  72.281  1.00 25.76 ? 276 MET   A CB  1 
ATOM   1700 C  CG  . MET   A 1 248 ? 17.669  -0.795  72.594  1.00 28.65 ? 276 MET   A CG  1 
ATOM   1701 S  SD  . MET   A 1 248 ? 16.831  0.684   73.173  1.00 35.86 ? 276 MET   A SD  1 
ATOM   1702 C  CE  . MET   A 1 248 ? 17.837  1.033   74.586  1.00 41.30 ? 276 MET   A CE  1 
ATOM   1703 N  N   . VAL   A 1 249 ? 15.236  -4.783  73.151  1.00 23.37 ? 277 VAL   A N   1 
ATOM   1704 C  CA  . VAL   A 1 249 ? 14.202  -5.788  72.957  1.00 25.81 ? 277 VAL   A CA  1 
ATOM   1705 C  C   . VAL   A 1 249 ? 13.800  -6.255  74.344  1.00 26.28 ? 277 VAL   A C   1 
ATOM   1706 O  O   . VAL   A 1 249 ? 14.606  -6.856  75.067  1.00 25.12 ? 277 VAL   A O   1 
ATOM   1707 C  CB  . VAL   A 1 249 ? 14.683  -6.943  72.074  1.00 23.12 ? 277 VAL   A CB  1 
ATOM   1708 C  CG1 . VAL   A 1 249 ? 13.609  -8.001  71.986  1.00 21.81 ? 277 VAL   A CG1 1 
ATOM   1709 C  CG2 . VAL   A 1 249 ? 15.046  -6.418  70.691  1.00 22.82 ? 277 VAL   A CG2 1 
ATOM   1710 N  N   . LEU   A 1 250 ? 12.571  -5.929  74.740  1.00 23.29 ? 278 LEU   A N   1 
ATOM   1711 C  CA  . LEU   A 1 250 ? 12.074  -6.190  76.086  1.00 21.82 ? 278 LEU   A CA  1 
ATOM   1712 C  C   . LEU   A 1 250 ? 10.859  -7.093  75.974  1.00 22.24 ? 278 LEU   A C   1 
ATOM   1713 O  O   . LEU   A 1 250 ? 9.891   -6.759  75.280  1.00 18.79 ? 278 LEU   A O   1 
ATOM   1714 C  CB  . LEU   A 1 250 ? 11.735  -4.888  76.822  1.00 22.45 ? 278 LEU   A CB  1 
ATOM   1715 C  CG  . LEU   A 1 250 ? 12.866  -3.857  76.866  1.00 22.99 ? 278 LEU   A CG  1 
ATOM   1716 C  CD1 . LEU   A 1 250 ? 12.394  -2.557  77.486  1.00 23.33 ? 278 LEU   A CD1 1 
ATOM   1717 C  CD2 . LEU   A 1 250 ? 14.054  -4.398  77.629  1.00 23.93 ? 278 LEU   A CD2 1 
ATOM   1718 N  N   . LEU   A 1 251 ? 10.921  -8.240  76.646  1.00 22.66 ? 279 LEU   A N   1 
ATOM   1719 C  CA  . LEU   A 1 251 ? 9.932   -9.300  76.503  1.00 21.44 ? 279 LEU   A CA  1 
ATOM   1720 C  C   . LEU   A 1 251 ? 9.445   -9.702  77.884  1.00 23.41 ? 279 LEU   A C   1 
ATOM   1721 O  O   . LEU   A 1 251 ? 9.888   -10.714 78.436  1.00 24.64 ? 279 LEU   A O   1 
ATOM   1722 C  CB  . LEU   A 1 251 ? 10.520  -10.502 75.760  1.00 24.10 ? 279 LEU   A CB  1 
ATOM   1723 C  CG  . LEU   A 1 251 ? 10.819  -10.287 74.274  1.00 24.31 ? 279 LEU   A CG  1 
ATOM   1724 C  CD1 . LEU   A 1 251 ? 11.459  -11.529 73.680  1.00 19.28 ? 279 LEU   A CD1 1 
ATOM   1725 C  CD2 . LEU   A 1 251 ? 9.525   -9.957  73.526  1.00 21.99 ? 279 LEU   A CD2 1 
ATOM   1726 N  N   . PRO   A 1 252 ? 8.528   -8.933  78.471  1.00 23.15 ? 280 PRO   A N   1 
ATOM   1727 C  CA  . PRO   A 1 252 ? 7.911   -9.367  79.729  1.00 21.76 ? 280 PRO   A CA  1 
ATOM   1728 C  C   . PRO   A 1 252 ? 7.001   -10.582 79.534  1.00 24.56 ? 280 PRO   A C   1 
ATOM   1729 O  O   . PRO   A 1 252 ? 6.388   -10.770 78.478  1.00 22.67 ? 280 PRO   A O   1 
ATOM   1730 C  CB  . PRO   A 1 252 ? 7.112   -8.138  80.173  1.00 25.44 ? 280 PRO   A CB  1 
ATOM   1731 C  CG  . PRO   A 1 252 ? 7.758   -6.947  79.438  1.00 21.01 ? 280 PRO   A CG  1 
ATOM   1732 C  CD  . PRO   A 1 252 ? 8.200   -7.532  78.127  1.00 21.60 ? 280 PRO   A CD  1 
ATOM   1733 N  N   . ILE   A 1 253 ? 6.921   -11.417 80.578  1.00 22.71 ? 281 ILE   A N   1 
ATOM   1734 C  CA  . ILE   A 1 253 ? 6.031   -12.578 80.617  1.00 23.02 ? 281 ILE   A CA  1 
ATOM   1735 C  C   . ILE   A 1 253 ? 5.312   -12.590 81.967  1.00 27.40 ? 281 ILE   A C   1 
ATOM   1736 O  O   . ILE   A 1 253 ? 5.952   -12.427 83.008  1.00 27.86 ? 281 ILE   A O   1 
ATOM   1737 C  CB  . ILE   A 1 253 ? 6.799   -13.901 80.401  1.00 24.50 ? 281 ILE   A CB  1 
ATOM   1738 C  CG1 . ILE   A 1 253 ? 7.610   -13.855 79.107  1.00 21.04 ? 281 ILE   A CG1 1 
ATOM   1739 C  CG2 . ILE   A 1 253 ? 5.835   -15.092 80.374  1.00 21.15 ? 281 ILE   A CG2 1 
ATOM   1740 C  CD1 . ILE   A 1 253 ? 8.419   -15.108 78.832  1.00 19.39 ? 281 ILE   A CD1 1 
ATOM   1741 N  N   . ASN   A 1 254 ? 3.986   -12.761 81.952  1.00 26.15 ? 282 ASN   A N   1 
ATOM   1742 C  CA  . ASN   A 1 254 ? 3.170   -12.856 83.158  1.00 23.97 ? 282 ASN   A CA  1 
ATOM   1743 C  C   . ASN   A 1 254 ? 2.643   -14.272 83.367  1.00 28.13 ? 282 ASN   A C   1 
ATOM   1744 O  O   . ASN   A 1 254 ? 2.407   -15.016 82.410  1.00 23.63 ? 282 ASN   A O   1 
ATOM   1745 C  CB  . ASN   A 1 254 ? 1.949   -11.936 83.106  1.00 26.20 ? 282 ASN   A CB  1 
ATOM   1746 C  CG  . ASN   A 1 254 ? 2.301   -10.483 82.901  1.00 25.68 ? 282 ASN   A CG  1 
ATOM   1747 O  OD1 . ASN   A 1 254 ? 3.336   -10.002 83.356  1.00 25.38 ? 282 ASN   A OD1 1 
ATOM   1748 N  ND2 . ASN   A 1 254 ? 1.419   -9.770  82.215  1.00 21.70 ? 282 ASN   A ND2 1 
ATOM   1749 N  N   . GLU   A 1 255 ? 2.422   -14.620 84.630  1.00 28.54 ? 283 GLU   A N   1 
ATOM   1750 C  CA  . GLU   A 1 255 ? 1.596   -15.745 85.030  1.00 28.87 ? 283 GLU   A CA  1 
ATOM   1751 C  C   . GLU   A 1 255 ? 0.569   -15.246 86.037  1.00 29.15 ? 283 GLU   A C   1 
ATOM   1752 O  O   . GLU   A 1 255 ? 0.789   -14.229 86.702  1.00 29.93 ? 283 GLU   A O   1 
ATOM   1753 C  CB  . GLU   A 1 255 ? 2.423   -16.885 85.646  1.00 29.60 ? 283 GLU   A CB  1 
ATOM   1754 C  CG  . GLU   A 1 255 ? 2.805   -16.653 87.096  1.00 31.79 ? 283 GLU   A CG  1 
ATOM   1755 C  CD  . GLU   A 1 255 ? 3.531   -17.833 87.701  1.00 34.93 ? 283 GLU   A CD  1 
ATOM   1756 O  OE1 . GLU   A 1 255 ? 4.018   -17.708 88.837  1.00 40.24 ? 283 GLU   A OE1 1 
ATOM   1757 O  OE2 . GLU   A 1 255 ? 3.611   -18.888 87.044  1.00 35.99 ? 283 GLU   A OE2 1 
ATOM   1758 N  N   . PRO   A 1 256 ? -0.568  -15.928 86.158  1.00 27.82 ? 284 PRO   A N   1 
ATOM   1759 C  CA  . PRO   A 1 256 ? -1.577  -15.516 87.146  1.00 34.36 ? 284 PRO   A CA  1 
ATOM   1760 C  C   . PRO   A 1 256 ? -1.171  -15.866 88.574  1.00 39.34 ? 284 PRO   A C   1 
ATOM   1761 O  O   . PRO   A 1 256 ? -0.323  -16.724 88.827  1.00 36.19 ? 284 PRO   A O   1 
ATOM   1762 C  CB  . PRO   A 1 256 ? -2.837  -16.299 86.740  1.00 30.65 ? 284 PRO   A CB  1 
ATOM   1763 C  CG  . PRO   A 1 256 ? -2.443  -17.169 85.580  1.00 33.55 ? 284 PRO   A CG  1 
ATOM   1764 C  CD  . PRO   A 1 256 ? -0.954  -17.154 85.441  1.00 26.33 ? 284 PRO   A CD  1 
ATOM   1765 N  N   . VAL   A 1 257 ? -1.790  -15.159 89.517  1.00 42.14 ? 285 VAL   A N   1 
ATOM   1766 C  CA  . VAL   A 1 257 ? -1.748  -15.514 90.931  1.00 46.33 ? 285 VAL   A CA  1 
ATOM   1767 C  C   . VAL   A 1 257 ? -3.157  -15.919 91.333  1.00 44.40 ? 285 VAL   A C   1 
ATOM   1768 O  O   . VAL   A 1 257 ? -4.093  -15.118 91.227  1.00 46.51 ? 285 VAL   A O   1 
ATOM   1769 C  CB  . VAL   A 1 257 ? -1.228  -14.363 91.803  1.00 44.95 ? 285 VAL   A CB  1 
ATOM   1770 C  CG1 . VAL   A 1 257 ? -1.415  -14.703 93.272  1.00 46.16 ? 285 VAL   A CG1 1 
ATOM   1771 C  CG2 . VAL   A 1 257 ? 0.239   -14.116 91.512  1.00 40.66 ? 285 VAL   A CG2 1 
ATOM   1772 N  N   . HIS   A 1 258 ? -3.312  -17.160 91.787  1.00 50.16 ? 286 HIS   A N   1 
ATOM   1773 C  CA  . HIS   A 1 258 ? -4.630  -17.740 92.003  1.00 54.33 ? 286 HIS   A CA  1 
ATOM   1774 C  C   . HIS   A 1 258 ? -5.122  -17.542 93.433  1.00 57.95 ? 286 HIS   A C   1 
ATOM   1775 O  O   . HIS   A 1 258 ? -4.339  -17.518 94.388  1.00 56.72 ? 286 HIS   A O   1 
ATOM   1776 C  CB  . HIS   A 1 258 ? -4.609  -19.231 91.667  1.00 49.56 ? 286 HIS   A CB  1 
ATOM   1777 C  CG  . HIS   A 1 258 ? -4.382  -19.509 90.218  1.00 49.20 ? 286 HIS   A CG  1 
ATOM   1778 N  ND1 . HIS   A 1 258 ? -3.423  -20.389 89.769  1.00 50.06 ? 286 HIS   A ND1 1 
ATOM   1779 C  CD2 . HIS   A 1 258 ? -4.983  -19.009 89.113  1.00 46.33 ? 286 HIS   A CD2 1 
ATOM   1780 C  CE1 . HIS   A 1 258 ? -3.447  -20.427 88.449  1.00 46.60 ? 286 HIS   A CE1 1 
ATOM   1781 N  NE2 . HIS   A 1 258 ? -4.386  -19.599 88.026  1.00 43.71 ? 286 HIS   A NE2 1 
ATOM   1782 N  N   . GLY   A 1 259 ? -6.443  -17.413 93.567  1.00 61.49 ? 287 GLY   A N   1 
ATOM   1783 C  CA  . GLY   A 1 259 ? -7.088  -17.307 94.863  1.00 62.46 ? 287 GLY   A CA  1 
ATOM   1784 C  C   . GLY   A 1 259 ? -6.898  -15.949 95.508  1.00 72.53 ? 287 GLY   A C   1 
ATOM   1785 O  O   . GLY   A 1 259 ? -6.111  -15.805 96.449  1.00 76.44 ? 287 GLY   A O   1 
ATOM   1786 N  N   . THR   A 1 260 ? -7.613  -14.941 95.006  1.00 71.86 ? 288 THR   A N   1 
ATOM   1787 C  CA  . THR   A 1 260 ? -7.507  -13.582 95.526  1.00 69.86 ? 288 THR   A CA  1 
ATOM   1788 C  C   . THR   A 1 260 ? -8.865  -13.141 96.057  1.00 74.47 ? 288 THR   A C   1 
ATOM   1789 O  O   . THR   A 1 260 ? -9.520  -13.877 96.801  1.00 76.15 ? 288 THR   A O   1 
ATOM   1790 C  CB  . THR   A 1 260 ? -7.023  -12.615 94.436  1.00 68.80 ? 288 THR   A CB  1 
ATOM   1791 O  OG1 . THR   A 1 260 ? -6.015  -13.196 93.682  1.00 66.07 ? 288 THR   A OG1 1 
ATOM   1792 C  CG2 . THR   A 1 260 ? -6.495  -11.346 95.028  1.00 71.39 ? 288 THR   A CG2 1 
ATOM   1793 N  N   . LYS   A 1 261 ? -9.271  -11.924 95.709  1.00 67.34 ? 289 LYS   A N   1 
ATOM   1794 C  CA  . LYS   A 1 261 ? -10.661 -11.500 95.783  1.00 71.18 ? 289 LYS   A CA  1 
ATOM   1795 C  C   . LYS   A 1 261 ? -11.153 -11.132 94.389  1.00 73.48 ? 289 LYS   A C   1 
ATOM   1796 O  O   . LYS   A 1 261 ? -12.130 -11.715 93.910  1.00 73.26 ? 289 LYS   A O   1 
ATOM   1797 C  CB  . LYS   A 1 261 ? -10.814 -10.328 96.767  1.00 69.18 ? 289 LYS   A CB  1 
ATOM   1798 N  N   . ARG   A 1 262 ? -10.481 -10.202 93.713  1.00 70.59 ? 290 ARG   A N   1 
ATOM   1799 C  CA  . ARG   A 1 262 ? -10.662 -10.020 92.276  1.00 63.81 ? 290 ARG   A CA  1 
ATOM   1800 C  C   . ARG   A 1 262 ? -9.892  -11.115 91.548  1.00 58.70 ? 290 ARG   A C   1 
ATOM   1801 O  O   . ARG   A 1 262 ? -8.694  -11.305 91.795  1.00 55.94 ? 290 ARG   A O   1 
ATOM   1802 C  CB  . ARG   A 1 262 ? -10.181 -8.640  91.831  1.00 58.68 ? 290 ARG   A CB  1 
ATOM   1803 N  N   . LYS   A 1 263 ? -10.584 -11.841 90.670  1.00 58.83 ? 291 LYS   A N   1 
ATOM   1804 C  CA  . LYS   A 1 263 ? -9.955  -12.891 89.875  1.00 51.69 ? 291 LYS   A CA  1 
ATOM   1805 C  C   . LYS   A 1 263 ? -8.850  -12.316 88.994  1.00 47.77 ? 291 LYS   A C   1 
ATOM   1806 O  O   . LYS   A 1 263 ? -8.969  -11.206 88.464  1.00 45.26 ? 291 LYS   A O   1 
ATOM   1807 C  CB  . LYS   A 1 263 ? -11.011 -13.583 89.016  1.00 49.79 ? 291 LYS   A CB  1 
ATOM   1808 C  CG  . LYS   A 1 263 ? -10.532 -14.778 88.213  1.00 45.67 ? 291 LYS   A CG  1 
ATOM   1809 C  CD  . LYS   A 1 263 ? -11.436 -14.959 87.003  1.00 43.13 ? 291 LYS   A CD  1 
ATOM   1810 C  CE  . LYS   A 1 263 ? -11.504 -16.405 86.546  1.00 42.29 ? 291 LYS   A CE  1 
ATOM   1811 N  NZ  . LYS   A 1 263 ? -12.419 -16.500 85.387  1.00 40.76 ? 291 LYS   A NZ  1 
ATOM   1812 N  N   . SER   A 1 264 ? -7.769  -13.083 88.844  1.00 41.00 ? 292 SER   A N   1 
ATOM   1813 C  CA  . SER   A 1 264 ? -6.620  -12.630 88.066  1.00 38.53 ? 292 SER   A CA  1 
ATOM   1814 C  C   . SER   A 1 264 ? -7.026  -12.319 86.626  1.00 34.93 ? 292 SER   A C   1 
ATOM   1815 O  O   . SER   A 1 264 ? -7.645  -13.143 85.944  1.00 31.38 ? 292 SER   A O   1 
ATOM   1816 C  CB  . SER   A 1 264 ? -5.524  -13.700 88.095  1.00 34.45 ? 292 SER   A CB  1 
ATOM   1817 O  OG  . SER   A 1 264 ? -4.384  -13.310 87.353  1.00 37.40 ? 292 SER   A OG  1 
ATOM   1818 N  N   . GLN   A 1 265 ? -6.683  -11.118 86.159  1.00 31.89 ? 293 GLN   A N   1 
ATOM   1819 C  CA  . GLN   A 1 265 ? -6.921  -10.816 84.754  1.00 32.52 ? 293 GLN   A CA  1 
ATOM   1820 C  C   . GLN   A 1 265 ? -5.989  -11.606 83.844  1.00 27.59 ? 293 GLN   A C   1 
ATOM   1821 O  O   . GLN   A 1 265 ? -6.289  -11.759 82.660  1.00 28.81 ? 293 GLN   A O   1 
ATOM   1822 C  CB  . GLN   A 1 265 ? -6.786  -9.311  84.485  1.00 32.53 ? 293 GLN   A CB  1 
ATOM   1823 C  CG  . GLN   A 1 265 ? -5.365  -8.813  84.236  1.00 35.94 ? 293 GLN   A CG  1 
ATOM   1824 C  CD  . GLN   A 1 265 ? -4.627  -8.507  85.514  1.00 45.73 ? 293 GLN   A CD  1 
ATOM   1825 O  OE1 . GLN   A 1 265 ? -5.150  -8.721  86.618  1.00 51.95 ? 293 GLN   A OE1 1 
ATOM   1826 N  NE2 . GLN   A 1 265 ? -3.411  -7.977  85.380  1.00 42.74 ? 293 GLN   A NE2 1 
ATOM   1827 N  N   . ILE   A 1 266 ? -4.870  -12.107 84.368  1.00 27.91 ? 294 ILE   A N   1 
ATOM   1828 C  CA  . ILE   A 1 266 ? -4.061  -13.057 83.612  1.00 27.59 ? 294 ILE   A CA  1 
ATOM   1829 C  C   . ILE   A 1 266 ? -4.835  -14.347 83.386  1.00 26.54 ? 294 ILE   A C   1 
ATOM   1830 O  O   . ILE   A 1 266 ? -4.863  -14.878 82.272  1.00 26.19 ? 294 ILE   A O   1 
ATOM   1831 C  CB  . ILE   A 1 266 ? -2.727  -13.317 84.334  1.00 28.54 ? 294 ILE   A CB  1 
ATOM   1832 C  CG1 . ILE   A 1 266 ? -2.076  -11.985 84.740  1.00 29.00 ? 294 ILE   A CG1 1 
ATOM   1833 C  CG2 . ILE   A 1 266 ? -1.800  -14.189 83.466  1.00 21.83 ? 294 ILE   A CG2 1 
ATOM   1834 C  CD1 . ILE   A 1 266 ? -1.761  -11.055 83.578  1.00 22.46 ? 294 ILE   A CD1 1 
ATOM   1835 N  N   . GLN   A 1 267 ? -5.488  -14.866 84.431  1.00 29.12 ? 295 GLN   A N   1 
ATOM   1836 C  CA  . GLN   A 1 267 ? -6.304  -16.071 84.275  1.00 27.70 ? 295 GLN   A CA  1 
ATOM   1837 C  C   . GLN   A 1 267 ? -7.500  -15.819 83.356  1.00 26.65 ? 295 GLN   A C   1 
ATOM   1838 O  O   . GLN   A 1 267 ? -7.832  -16.663 82.510  1.00 25.97 ? 295 GLN   A O   1 
ATOM   1839 C  CB  . GLN   A 1 267 ? -6.764  -16.573 85.648  1.00 29.63 ? 295 GLN   A CB  1 
ATOM   1840 C  CG  . GLN   A 1 267 ? -7.695  -17.798 85.604  1.00 29.97 ? 295 GLN   A CG  1 
ATOM   1841 C  CD  . GLN   A 1 267 ? -6.999  -19.059 85.140  1.00 27.31 ? 295 GLN   A CD  1 
ATOM   1842 O  OE1 . GLN   A 1 267 ? -5.797  -19.230 85.335  1.00 34.15 ? 295 GLN   A OE1 1 
ATOM   1843 N  NE2 . GLN   A 1 267 ? -7.746  -19.941 84.494  1.00 28.87 ? 295 GLN   A NE2 1 
ATOM   1844 N  N   . THR   A 1 268 ? -8.148  -14.656 83.491  1.00 28.41 ? 296 THR   A N   1 
ATOM   1845 C  CA  . THR   A 1 268 ? -9.232  -14.307 82.572  1.00 27.32 ? 296 THR   A CA  1 
ATOM   1846 C  C   . THR   A 1 268 ? -8.741  -14.300 81.130  1.00 25.14 ? 296 THR   A C   1 
ATOM   1847 O  O   . THR   A 1 268 ? -9.427  -14.798 80.225  1.00 23.85 ? 296 THR   A O   1 
ATOM   1848 C  CB  . THR   A 1 268 ? -9.833  -12.943 82.934  1.00 32.47 ? 296 THR   A CB  1 
ATOM   1849 O  OG1 . THR   A 1 268 ? -10.441 -13.009 84.233  1.00 33.57 ? 296 THR   A OG1 1 
ATOM   1850 C  CG2 . THR   A 1 268 ? -10.892 -12.525 81.911  1.00 25.87 ? 296 THR   A CG2 1 
ATOM   1851 N  N   . TYR   A 1 269 ? -7.537  -13.769 80.901  1.00 24.99 ? 297 TYR   A N   1 
ATOM   1852 C  CA  . TYR   A 1 269 ? -6.970  -13.784 79.557  1.00 21.47 ? 297 TYR   A CA  1 
ATOM   1853 C  C   . TYR   A 1 269 ? -6.844  -15.215 79.034  1.00 19.91 ? 297 TYR   A C   1 
ATOM   1854 O  O   . TYR   A 1 269 ? -7.305  -15.529 77.932  1.00 20.51 ? 297 TYR   A O   1 
ATOM   1855 C  CB  . TYR   A 1 269 ? -5.607  -13.080 79.556  1.00 20.97 ? 297 TYR   A CB  1 
ATOM   1856 C  CG  . TYR   A 1 269 ? -4.896  -13.142 78.224  1.00 18.84 ? 297 TYR   A CG  1 
ATOM   1857 C  CD1 . TYR   A 1 269 ? -4.270  -14.313 77.798  1.00 17.00 ? 297 TYR   A CD1 1 
ATOM   1858 C  CD2 . TYR   A 1 269 ? -4.844  -12.028 77.386  1.00 20.34 ? 297 TYR   A CD2 1 
ATOM   1859 C  CE1 . TYR   A 1 269 ? -3.629  -14.382 76.580  1.00 16.43 ? 297 TYR   A CE1 1 
ATOM   1860 C  CE2 . TYR   A 1 269 ? -4.196  -12.092 76.154  1.00 15.62 ? 297 TYR   A CE2 1 
ATOM   1861 C  CZ  . TYR   A 1 269 ? -3.598  -13.280 75.761  1.00 16.26 ? 297 TYR   A CZ  1 
ATOM   1862 O  OH  . TYR   A 1 269 ? -2.952  -13.378 74.545  1.00 15.98 ? 297 TYR   A OH  1 
ATOM   1863 N  N   . LEU   A 1 270 ? -6.199  -16.090 79.804  1.00 18.65 ? 298 LEU   A N   1 
ATOM   1864 C  CA  . LEU   A 1 270 ? -5.950  -17.453 79.334  1.00 23.01 ? 298 LEU   A CA  1 
ATOM   1865 C  C   . LEU   A 1 270 ? -7.249  -18.161 78.970  1.00 20.46 ? 298 LEU   A C   1 
ATOM   1866 O  O   . LEU   A 1 270 ? -7.317  -18.856 77.952  1.00 18.58 ? 298 LEU   A O   1 
ATOM   1867 C  CB  . LEU   A 1 270 ? -5.187  -18.244 80.397  1.00 19.09 ? 298 LEU   A CB  1 
ATOM   1868 C  CG  . LEU   A 1 270 ? -3.791  -17.756 80.770  1.00 21.86 ? 298 LEU   A CG  1 
ATOM   1869 C  CD1 . LEU   A 1 270 ? -3.318  -18.512 82.008  1.00 19.84 ? 298 LEU   A CD1 1 
ATOM   1870 C  CD2 . LEU   A 1 270 ? -2.800  -17.952 79.592  1.00 17.79 ? 298 LEU   A CD2 1 
ATOM   1871 N  N   . GLU   A 1 271 ? -8.307  -17.944 79.757  1.00 20.19 ? 299 GLU   A N   1 
ATOM   1872 C  CA  . GLU   A 1 271 ? -9.595  -18.577 79.469  1.00 28.65 ? 299 GLU   A CA  1 
ATOM   1873 C  C   . GLU   A 1 271 ? -10.189 -18.061 78.160  1.00 24.78 ? 299 GLU   A C   1 
ATOM   1874 O  O   . GLU   A 1 271 ? -10.549 -18.851 77.271  1.00 19.40 ? 299 GLU   A O   1 
ATOM   1875 C  CB  . GLU   A 1 271 ? -10.560 -18.360 80.651  1.00 26.79 ? 299 GLU   A CB  1 
ATOM   1876 C  CG  . GLU   A 1 271 ? -10.127 -19.158 81.908  1.00 32.94 ? 299 GLU   A CG  1 
ATOM   1877 C  CD  . GLU   A 1 271 ? -10.842 -18.773 83.188  1.00 33.19 ? 299 GLU   A CD  1 
ATOM   1878 O  OE1 . GLU   A 1 271 ? -11.718 -17.881 83.174  1.00 30.07 ? 299 GLU   A OE1 1 
ATOM   1879 O  OE2 . GLU   A 1 271 ? -10.493 -19.343 84.249  1.00 32.50 ? 299 GLU   A OE2 1 
ATOM   1880 N  N   . HIS   A 1 272 ? -10.271 -16.734 78.010  1.00 19.07 ? 300 HIS   A N   1 
ATOM   1881 C  CA  . HIS   A 1 272 ? -10.869 -16.170 76.804  1.00 19.64 ? 300 HIS   A CA  1 
ATOM   1882 C  C   . HIS   A 1 272 ? -9.971  -16.339 75.585  1.00 17.03 ? 300 HIS   A C   1 
ATOM   1883 O  O   . HIS   A 1 272 ? -10.478 -16.448 74.465  1.00 20.01 ? 300 HIS   A O   1 
ATOM   1884 C  CB  . HIS   A 1 272 ? -11.224 -14.694 77.025  1.00 20.30 ? 300 HIS   A CB  1 
ATOM   1885 C  CG  . HIS   A 1 272 ? -12.438 -14.488 77.881  1.00 18.55 ? 300 HIS   A CG  1 
ATOM   1886 N  ND1 . HIS   A 1 272 ? -13.686 -14.241 77.353  1.00 19.51 ? 300 HIS   A ND1 1 
ATOM   1887 C  CD2 . HIS   A 1 272 ? -12.597 -14.502 79.225  1.00 20.51 ? 300 HIS   A CD2 1 
ATOM   1888 C  CE1 . HIS   A 1 272 ? -14.560 -14.099 78.333  1.00 19.11 ? 300 HIS   A CE1 1 
ATOM   1889 N  NE2 . HIS   A 1 272 ? -13.925 -14.260 79.479  1.00 21.65 ? 300 HIS   A NE2 1 
ATOM   1890 N  N   . ASN   A 1 273 ? -8.657  -16.416 75.771  1.00 16.97 ? 301 ASN   A N   1 
ATOM   1891 C  CA  . ASN   A 1 273 ? -7.745  -16.580 74.646  1.00 17.53 ? 301 ASN   A CA  1 
ATOM   1892 C  C   . ASN   A 1 273 ? -7.528  -18.034 74.265  1.00 20.49 ? 301 ASN   A C   1 
ATOM   1893 O  O   . ASN   A 1 273 ? -6.790  -18.300 73.299  1.00 16.91 ? 301 ASN   A O   1 
ATOM   1894 C  CB  . ASN   A 1 273 ? -6.383  -15.947 74.964  1.00 17.31 ? 301 ASN   A CB  1 
ATOM   1895 C  CG  . ASN   A 1 273 ? -5.575  -15.667 73.729  1.00 16.71 ? 301 ASN   A CG  1 
ATOM   1896 O  OD1 . ASN   A 1 273 ? -5.967  -14.853 72.901  1.00 17.95 ? 301 ASN   A OD1 1 
ATOM   1897 N  ND2 . ASN   A 1 273 ? -4.433  -16.342 73.593  1.00 17.14 ? 301 ASN   A ND2 1 
ATOM   1898 N  N   . GLU   A 1 274 ? -8.143  -18.972 74.997  1.00 17.94 ? 302 GLU   A N   1 
ATOM   1899 C  CA  . GLU   A 1 274 ? -7.811  -20.391 74.896  1.00 18.03 ? 302 GLU   A CA  1 
ATOM   1900 C  C   . GLU   A 1 274 ? -6.303  -20.614 75.029  1.00 19.38 ? 302 GLU   A C   1 
ATOM   1901 O  O   . GLU   A 1 274 ? -5.660  -21.192 74.155  1.00 20.62 ? 302 GLU   A O   1 
ATOM   1902 C  CB  . GLU   A 1 274 ? -8.326  -20.987 73.589  1.00 19.06 ? 302 GLU   A CB  1 
ATOM   1903 C  CG  . GLU   A 1 274 ? -9.827  -21.174 73.538  1.00 22.11 ? 302 GLU   A CG  1 
ATOM   1904 C  CD  . GLU   A 1 274 ? -10.282 -21.894 72.285  1.00 19.76 ? 302 GLU   A CD  1 
ATOM   1905 O  OE1 . GLU   A 1 274 ? -9.435  -22.474 71.584  1.00 24.01 ? 302 GLU   A OE1 1 
ATOM   1906 O  OE2 . GLU   A 1 274 ? -11.490 -21.864 71.996  1.00 22.39 ? 302 GLU   A OE2 1 
ATOM   1907 N  N   . GLY   A 1 275 ? -5.730  -20.129 76.122  1.00 17.62 ? 303 GLY   A N   1 
ATOM   1908 C  CA  . GLY   A 1 275 ? -4.346  -20.422 76.454  1.00 16.48 ? 303 GLY   A CA  1 
ATOM   1909 C  C   . GLY   A 1 275 ? -3.425  -19.228 76.270  1.00 21.40 ? 303 GLY   A C   1 
ATOM   1910 O  O   . GLY   A 1 275 ? -3.850  -18.094 76.020  1.00 23.04 ? 303 GLY   A O   1 
ATOM   1911 N  N   . ALA   A 1 276 ? -2.130  -19.513 76.395  1.00 21.66 ? 304 ALA   A N   1 
ATOM   1912 C  CA  . ALA   A 1 276 ? -1.114  -18.475 76.392  1.00 17.97 ? 304 ALA   A CA  1 
ATOM   1913 C  C   . ALA   A 1 276 ? -1.146  -17.667 75.098  1.00 17.92 ? 304 ALA   A C   1 
ATOM   1914 O  O   . ALA   A 1 276 ? -1.513  -18.162 74.031  1.00 19.58 ? 304 ALA   A O   1 
ATOM   1915 C  CB  . ALA   A 1 276 ? 0.274   -19.090 76.587  1.00 21.32 ? 304 ALA   A CB  1 
ATOM   1916 N  N   . GLY   A 1 277 ? -0.754  -16.406 75.207  1.00 19.20 ? 305 GLY   A N   1 
ATOM   1917 C  CA  . GLY   A 1 277 ? -0.678  -15.539 74.049  1.00 16.01 ? 305 GLY   A CA  1 
ATOM   1918 C  C   . GLY   A 1 277 ? -0.119  -14.191 74.448  1.00 18.44 ? 305 GLY   A C   1 
ATOM   1919 O  O   . GLY   A 1 277 ? 0.251   -13.953 75.606  1.00 21.23 ? 305 GLY   A O   1 
ATOM   1920 N  N   . LEU   A 1 278 ? -0.061  -13.304 73.466  1.00 16.99 ? 306 LEU   A N   1 
ATOM   1921 C  CA  . LEU   A 1 278 ? 0.428   -11.960 73.709  1.00 17.23 ? 306 LEU   A CA  1 
ATOM   1922 C  C   . LEU   A 1 278 ? -0.651  -11.131 74.405  1.00 19.17 ? 306 LEU   A C   1 
ATOM   1923 O  O   . LEU   A 1 278 ? -1.798  -11.061 73.935  1.00 16.84 ? 306 LEU   A O   1 
ATOM   1924 C  CB  . LEU   A 1 278 ? 0.849   -11.327 72.388  1.00 16.20 ? 306 LEU   A CB  1 
ATOM   1925 C  CG  . LEU   A 1 278 ? 1.729   -10.096 72.565  1.00 22.00 ? 306 LEU   A CG  1 
ATOM   1926 C  CD1 . LEU   A 1 278 ? 2.877   -10.095 71.580  1.00 19.66 ? 306 LEU   A CD1 1 
ATOM   1927 C  CD2 . LEU   A 1 278 ? 0.882   -8.862  72.417  1.00 16.65 ? 306 LEU   A CD2 1 
ATOM   1928 N  N   . GLN   A 1 279 ? -0.288  -10.507 75.530  1.00 16.54 ? 307 GLN   A N   1 
ATOM   1929 C  CA  . GLN   A 1 279 ? -1.232  -9.714  76.314  1.00 18.04 ? 307 GLN   A CA  1 
ATOM   1930 C  C   . GLN   A 1 279 ? -1.285  -8.245  75.867  1.00 19.33 ? 307 GLN   A C   1 
ATOM   1931 O  O   . GLN   A 1 279 ? -2.372  -7.703  75.639  1.00 15.07 ? 307 GLN   A O   1 
ATOM   1932 C  CB  . GLN   A 1 279 ? -0.886  -9.774  77.805  1.00 18.41 ? 307 GLN   A CB  1 
ATOM   1933 C  CG  . GLN   A 1 279 ? -1.893  -8.997  78.672  1.00 21.54 ? 307 GLN   A CG  1 
ATOM   1934 C  CD  . GLN   A 1 279 ? -1.289  -8.385  79.932  1.00 19.84 ? 307 GLN   A CD  1 
ATOM   1935 O  OE1 . GLN   A 1 279 ? -0.143  -7.940  79.928  1.00 23.85 ? 307 GLN   A OE1 1 
ATOM   1936 N  NE2 . GLN   A 1 279 ? -2.070  -8.341  81.006  1.00 18.47 ? 307 GLN   A NE2 1 
ATOM   1937 N  N   . HIS   A 1 280 ? -0.140  -7.565  75.769  1.00 16.60 ? 308 HIS   A N   1 
ATOM   1938 C  CA  . HIS   A 1 280 ? -0.213  -6.203  75.270  1.00 19.14 ? 308 HIS   A CA  1 
ATOM   1939 C  C   . HIS   A 1 280 ? 1.069   -5.794  74.574  1.00 16.73 ? 308 HIS   A C   1 
ATOM   1940 O  O   . HIS   A 1 280 ? 2.151   -6.314  74.845  1.00 16.63 ? 308 HIS   A O   1 
ATOM   1941 C  CB  . HIS   A 1 280 ? -0.582  -5.192  76.374  1.00 16.88 ? 308 HIS   A CB  1 
ATOM   1942 C  CG  . HIS   A 1 280 ? 0.503   -4.900  77.363  1.00 19.71 ? 308 HIS   A CG  1 
ATOM   1943 N  ND1 . HIS   A 1 280 ? 0.718   -5.672  78.488  1.00 19.30 ? 308 HIS   A ND1 1 
ATOM   1944 C  CD2 . HIS   A 1 280 ? 1.389   -3.874  77.434  1.00 18.80 ? 308 HIS   A CD2 1 
ATOM   1945 C  CE1 . HIS   A 1 280 ? 1.695   -5.137  79.202  1.00 21.75 ? 308 HIS   A CE1 1 
ATOM   1946 N  NE2 . HIS   A 1 280 ? 2.130   -4.056  78.574  1.00 19.83 ? 308 HIS   A NE2 1 
ATOM   1947 N  N   . LEU   A 1 281 ? 0.911   -4.867  73.640  1.00 18.47 ? 309 LEU   A N   1 
ATOM   1948 C  CA  . LEU   A 1 281 ? 2.018   -4.217  72.962  1.00 14.97 ? 309 LEU   A CA  1 
ATOM   1949 C  C   . LEU   A 1 281 ? 2.114   -2.801  73.512  1.00 17.68 ? 309 LEU   A C   1 
ATOM   1950 O  O   . LEU   A 1 281 ? 1.105   -2.091  73.557  1.00 18.51 ? 309 LEU   A O   1 
ATOM   1951 C  CB  . LEU   A 1 281 ? 1.764   -4.189  71.454  1.00 14.23 ? 309 LEU   A CB  1 
ATOM   1952 C  CG  . LEU   A 1 281 ? 1.435   -5.519  70.770  1.00 18.17 ? 309 LEU   A CG  1 
ATOM   1953 C  CD1 . LEU   A 1 281 ? 0.663   -5.245  69.484  1.00 15.26 ? 309 LEU   A CD1 1 
ATOM   1954 C  CD2 . LEU   A 1 281 ? 2.702   -6.337  70.462  1.00 13.51 ? 309 LEU   A CD2 1 
ATOM   1955 N  N   . ALA   A 1 282 ? 3.301   -2.387  73.942  1.00 17.84 ? 310 ALA   A N   1 
ATOM   1956 C  CA  . ALA   A 1 282 ? 3.491   -1.022  74.434  1.00 16.26 ? 310 ALA   A CA  1 
ATOM   1957 C  C   . ALA   A 1 282 ? 4.228   -0.214  73.385  1.00 17.66 ? 310 ALA   A C   1 
ATOM   1958 O  O   . ALA   A 1 282 ? 5.342   -0.574  72.983  1.00 17.32 ? 310 ALA   A O   1 
ATOM   1959 C  CB  . ALA   A 1 282 ? 4.245   -0.985  75.755  1.00 16.49 ? 310 ALA   A CB  1 
ATOM   1960 N  N   . LEU   A 1 283 ? 3.608   0.881   72.962  1.00 18.49 ? 311 LEU   A N   1 
ATOM   1961 C  CA  . LEU   A 1 283 ? 4.041   1.665   71.817  1.00 17.33 ? 311 LEU   A CA  1 
ATOM   1962 C  C   . LEU   A 1 283 ? 4.584   2.993   72.327  1.00 18.18 ? 311 LEU   A C   1 
ATOM   1963 O  O   . LEU   A 1 283 ? 3.866   3.751   72.992  1.00 18.79 ? 311 LEU   A O   1 
ATOM   1964 C  CB  . LEU   A 1 283 ? 2.881   1.868   70.835  1.00 16.89 ? 311 LEU   A CB  1 
ATOM   1965 C  CG  . LEU   A 1 283 ? 1.974   0.638   70.584  1.00 16.54 ? 311 LEU   A CG  1 
ATOM   1966 C  CD1 . LEU   A 1 283 ? 0.828   0.957   69.618  1.00 13.54 ? 311 LEU   A CD1 1 
ATOM   1967 C  CD2 . LEU   A 1 283 ? 2.764   -0.526  70.065  1.00 11.78 ? 311 LEU   A CD2 1 
ATOM   1968 N  N   . MET   A 1 284 ? 5.853   3.269   72.032  1.00 19.59 ? 312 MET   A N   1 
ATOM   1969 C  CA  . MET   A 1 284 ? 6.460   4.508   72.489  1.00 21.57 ? 312 MET   A CA  1 
ATOM   1970 C  C   . MET   A 1 284 ? 5.946   5.667   71.644  1.00 19.93 ? 312 MET   A C   1 
ATOM   1971 O  O   . MET   A 1 284 ? 5.896   5.582   70.414  1.00 16.69 ? 312 MET   A O   1 
ATOM   1972 C  CB  A MET   A 1 284 ? 7.991   4.426   72.437  0.55 24.24 ? 312 MET   A CB  1 
ATOM   1973 C  CB  B MET   A 1 284 ? 7.990   4.437   72.408  0.45 21.58 ? 312 MET   A CB  1 
ATOM   1974 C  CG  A MET   A 1 284 ? 8.694   5.658   73.061  0.55 22.63 ? 312 MET   A CG  1 
ATOM   1975 C  CG  B MET   A 1 284 ? 8.709   5.760   72.782  0.45 22.69 ? 312 MET   A CG  1 
ATOM   1976 S  SD  A MET   A 1 284 ? 10.458  5.421   73.386  0.55 36.92 ? 312 MET   A SD  1 
ATOM   1977 S  SD  B MET   A 1 284 ? 9.107   6.804   71.351  0.45 25.86 ? 312 MET   A SD  1 
ATOM   1978 C  CE  A MET   A 1 284 ? 10.415  4.657   75.003  0.55 25.12 ? 312 MET   A CE  1 
ATOM   1979 C  CE  B MET   A 1 284 ? 9.730   8.306   72.132  0.45 20.07 ? 312 MET   A CE  1 
ATOM   1980 N  N   . SER   A 1 285 ? 5.559   6.747   72.311  1.00 19.51 ? 313 SER   A N   1 
ATOM   1981 C  CA  . SER   A 1 285 ? 5.206   7.990   71.640  1.00 22.86 ? 313 SER   A CA  1 
ATOM   1982 C  C   . SER   A 1 285 ? 6.270   9.049   71.924  1.00 21.63 ? 313 SER   A C   1 
ATOM   1983 O  O   . SER   A 1 285 ? 6.788   9.134   73.043  1.00 21.45 ? 313 SER   A O   1 
ATOM   1984 C  CB  . SER   A 1 285 ? 3.836   8.492   72.108  1.00 19.07 ? 313 SER   A CB  1 
ATOM   1985 O  OG  . SER   A 1 285 ? 3.569   9.788   71.611  1.00 20.99 ? 313 SER   A OG  1 
ATOM   1986 N  N   . GLU   A 1 286 ? 6.587   9.858   70.908  1.00 21.17 ? 314 GLU   A N   1 
ATOM   1987 C  CA  . GLU   A 1 286 ? 7.443   11.025  71.100  1.00 26.93 ? 314 GLU   A CA  1 
ATOM   1988 C  C   . GLU   A 1 286 ? 6.704   12.193  71.742  1.00 27.04 ? 314 GLU   A C   1 
ATOM   1989 O  O   . GLU   A 1 286 ? 7.330   13.223  72.025  1.00 27.20 ? 314 GLU   A O   1 
ATOM   1990 C  CB  . GLU   A 1 286 ? 8.045   11.488  69.764  1.00 24.85 ? 314 GLU   A CB  1 
ATOM   1991 C  CG  . GLU   A 1 286 ? 7.006   11.834  68.702  1.00 26.41 ? 314 GLU   A CG  1 
ATOM   1992 C  CD  . GLU   A 1 286 ? 7.506   12.882  67.703  1.00 35.14 ? 314 GLU   A CD  1 
ATOM   1993 O  OE1 . GLU   A 1 286 ? 8.724   12.911  67.420  1.00 38.91 ? 314 GLU   A OE1 1 
ATOM   1994 O  OE2 . GLU   A 1 286 ? 6.675   13.672  67.201  1.00 38.69 ? 314 GLU   A OE2 1 
ATOM   1995 N  N   . ASP   A 1 287 ? 5.399   12.060  71.977  1.00 22.65 ? 315 ASP   A N   1 
ATOM   1996 C  CA  . ASP   A 1 287 ? 4.597   13.136  72.550  1.00 23.48 ? 315 ASP   A CA  1 
ATOM   1997 C  C   . ASP   A 1 287 ? 3.277   12.527  72.985  1.00 22.03 ? 315 ASP   A C   1 
ATOM   1998 O  O   . ASP   A 1 287 ? 2.300   12.552  72.226  1.00 21.07 ? 315 ASP   A O   1 
ATOM   1999 C  CB  . ASP   A 1 287 ? 4.402   14.264  71.523  1.00 25.61 ? 315 ASP   A CB  1 
ATOM   2000 C  CG  . ASP   A 1 287 ? 3.581   15.452  72.057  1.00 27.90 ? 315 ASP   A CG  1 
ATOM   2001 O  OD1 . ASP   A 1 287 ? 3.063   15.417  73.202  1.00 21.08 ? 315 ASP   A OD1 1 
ATOM   2002 O  OD2 . ASP   A 1 287 ? 3.448   16.426  71.281  1.00 25.79 ? 315 ASP   A OD2 1 
ATOM   2003 N  N   . ILE   A 1 288 ? 3.260   11.936  74.186  1.00 22.90 ? 316 ILE   A N   1 
ATOM   2004 C  CA  . ILE   A 1 288 ? 2.130   11.116  74.592  1.00 21.18 ? 316 ILE   A CA  1 
ATOM   2005 C  C   . ILE   A 1 288 ? 0.872   11.955  74.751  1.00 23.56 ? 316 ILE   A C   1 
ATOM   2006 O  O   . ILE   A 1 288 ? -0.246  11.424  74.678  1.00 21.09 ? 316 ILE   A O   1 
ATOM   2007 C  CB  . ILE   A 1 288 ? 2.447   10.330  75.880  1.00 22.12 ? 316 ILE   A CB  1 
ATOM   2008 C  CG1 . ILE   A 1 288 ? 1.388   9.224   76.090  1.00 21.27 ? 316 ILE   A CG1 1 
ATOM   2009 C  CG2 . ILE   A 1 288 ? 2.539   11.274  77.091  1.00 23.26 ? 316 ILE   A CG2 1 
ATOM   2010 C  CD1 . ILE   A 1 288 ? 1.564   8.354   77.343  1.00 19.33 ? 316 ILE   A CD1 1 
ATOM   2011 N  N   . PHE   A 1 289 ? 1.024   13.268  74.931  1.00 27.29 ? 317 PHE   A N   1 
ATOM   2012 C  CA  . PHE   A 1 289 ? -0.146  14.124  75.085  1.00 25.40 ? 317 PHE   A CA  1 
ATOM   2013 C  C   . PHE   A 1 289 ? -0.874  14.293  73.758  1.00 21.96 ? 317 PHE   A C   1 
ATOM   2014 O  O   . PHE   A 1 289 ? -2.097  14.136  73.689  1.00 25.28 ? 317 PHE   A O   1 
ATOM   2015 C  CB  . PHE   A 1 289 ? 0.268   15.479  75.683  1.00 28.12 ? 317 PHE   A CB  1 
ATOM   2016 C  CG  . PHE   A 1 289 ? 0.673   15.389  77.122  1.00 32.22 ? 317 PHE   A CG  1 
ATOM   2017 C  CD1 . PHE   A 1 289 ? -0.146  14.761  78.039  1.00 36.42 ? 317 PHE   A CD1 1 
ATOM   2018 C  CD2 . PHE   A 1 289 ? 1.850   15.938  77.572  1.00 40.87 ? 317 PHE   A CD2 1 
ATOM   2019 C  CE1 . PHE   A 1 289 ? 0.216   14.666  79.376  1.00 39.72 ? 317 PHE   A CE1 1 
ATOM   2020 C  CE2 . PHE   A 1 289 ? 2.212   15.846  78.918  1.00 42.26 ? 317 PHE   A CE2 1 
ATOM   2021 C  CZ  . PHE   A 1 289 ? 1.394   15.202  79.813  1.00 33.18 ? 317 PHE   A CZ  1 
ATOM   2022 N  N   . ARG   A 1 290 ? -0.133  14.577  72.686  1.00 21.57 ? 318 ARG   A N   1 
ATOM   2023 C  CA  . ARG   A 1 290 ? -0.746  14.689  71.367  1.00 23.70 ? 318 ARG   A CA  1 
ATOM   2024 C  C   . ARG   A 1 290 ? -1.311  13.342  70.898  1.00 24.69 ? 318 ARG   A C   1 
ATOM   2025 O  O   . ARG   A 1 290 ? -2.431  13.280  70.361  1.00 19.69 ? 318 ARG   A O   1 
ATOM   2026 C  CB  . ARG   A 1 290 ? 0.277   15.241  70.368  1.00 20.04 ? 318 ARG   A CB  1 
ATOM   2027 C  CG  . ARG   A 1 290 ? -0.047  14.900  68.924  1.00 27.82 ? 318 ARG   A CG  1 
ATOM   2028 C  CD  . ARG   A 1 290 ? 0.835   15.607  67.880  1.00 25.71 ? 318 ARG   A CD  1 
ATOM   2029 N  NE  A ARG   A 1 290 ? 1.121   14.800  66.690  0.53 27.75 ? 318 ARG   A NE  1 
ATOM   2030 N  NE  B ARG   A 1 290 ? 0.515   15.032  66.565  0.47 28.50 ? 318 ARG   A NE  1 
ATOM   2031 C  CZ  A ARG   A 1 290 ? 2.249   14.130  66.485  0.53 24.86 ? 318 ARG   A CZ  1 
ATOM   2032 C  CZ  B ARG   A 1 290 ? -0.563  15.338  65.838  0.47 24.64 ? 318 ARG   A CZ  1 
ATOM   2033 N  NH1 A ARG   A 1 290 ? 3.221   14.153  67.390  0.53 30.28 ? 318 ARG   A NH1 1 
ATOM   2034 N  NH1 B ARG   A 1 290 ? -1.433  16.246  66.260  0.47 24.37 ? 318 ARG   A NH1 1 
ATOM   2035 N  NH2 A ARG   A 1 290 ? 2.413   13.445  65.364  0.53 24.47 ? 318 ARG   A NH2 1 
ATOM   2036 N  NH2 B ARG   A 1 290 ? -0.756  14.748  64.668  0.47 23.91 ? 318 ARG   A NH2 1 
ATOM   2037 N  N   . THR   A 1 291 ? -0.560  12.251  71.107  1.00 21.40 ? 319 THR   A N   1 
ATOM   2038 C  CA  . THR   A 1 291 ? -1.066  10.918  70.768  1.00 20.29 ? 319 THR   A CA  1 
ATOM   2039 C  C   . THR   A 1 291 ? -2.421  10.654  71.420  1.00 20.67 ? 319 THR   A C   1 
ATOM   2040 O  O   . THR   A 1 291 ? -3.371  10.206  70.767  1.00 18.76 ? 319 THR   A O   1 
ATOM   2041 C  CB  . THR   A 1 291 ? -0.068  9.850   71.207  1.00 17.71 ? 319 THR   A CB  1 
ATOM   2042 O  OG1 . THR   A 1 291 ? 1.161   10.037  70.509  1.00 19.76 ? 319 THR   A OG1 1 
ATOM   2043 C  CG2 . THR   A 1 291 ? -0.628  8.432   70.951  1.00 17.76 ? 319 THR   A CG2 1 
ATOM   2044 N  N   . LEU   A 1 292 ? -2.522  10.927  72.718  1.00 19.60 ? 320 LEU   A N   1 
ATOM   2045 C  CA  . LEU   A 1 292 ? -3.739  10.604  73.442  1.00 19.35 ? 320 LEU   A CA  1 
ATOM   2046 C  C   . LEU   A 1 292 ? -4.864  11.551  73.064  1.00 21.27 ? 320 LEU   A C   1 
ATOM   2047 O  O   . LEU   A 1 292 ? -6.022  11.135  72.979  1.00 20.31 ? 320 LEU   A O   1 
ATOM   2048 C  CB  . LEU   A 1 292 ? -3.476  10.627  74.943  1.00 21.39 ? 320 LEU   A CB  1 
ATOM   2049 C  CG  . LEU   A 1 292 ? -3.228  9.235   75.536  1.00 22.90 ? 320 LEU   A CG  1 
ATOM   2050 C  CD1 . LEU   A 1 292 ? -4.558  8.476   75.629  1.00 24.69 ? 320 LEU   A CD1 1 
ATOM   2051 C  CD2 . LEU   A 1 292 ? -2.235  8.455   74.691  1.00 18.70 ? 320 LEU   A CD2 1 
ATOM   2052 N  N   . ARG   A 1 293 ? -4.545  12.823  72.805  1.00 21.60 ? 321 ARG   A N   1 
ATOM   2053 C  CA  . ARG   A 1 293 ? -5.565  13.722  72.271  1.00 24.47 ? 321 ARG   A CA  1 
ATOM   2054 C  C   . ARG   A 1 293 ? -6.087  13.203  70.939  1.00 20.50 ? 321 ARG   A C   1 
ATOM   2055 O  O   . ARG   A 1 293 ? -7.299  13.139  70.709  1.00 18.94 ? 321 ARG   A O   1 
ATOM   2056 C  CB  . ARG   A 1 293 ? -5.013  15.148  72.110  1.00 25.85 ? 321 ARG   A CB  1 
ATOM   2057 C  CG  . ARG   A 1 293 ? -4.883  15.909  73.431  1.00 27.56 ? 321 ARG   A CG  1 
ATOM   2058 C  CD  . ARG   A 1 293 ? -4.628  17.415  73.229  1.00 25.76 ? 321 ARG   A CD  1 
ATOM   2059 N  NE  . ARG   A 1 293 ? -3.509  17.673  72.330  1.00 29.22 ? 321 ARG   A NE  1 
ATOM   2060 C  CZ  . ARG   A 1 293 ? -2.250  17.858  72.726  1.00 32.09 ? 321 ARG   A CZ  1 
ATOM   2061 N  NH1 . ARG   A 1 293 ? -1.933  17.806  74.018  1.00 34.19 ? 321 ARG   A NH1 1 
ATOM   2062 N  NH2 . ARG   A 1 293 ? -1.305  18.093  71.822  1.00 30.41 ? 321 ARG   A NH2 1 
ATOM   2063 N  N   . GLU   A 1 294 ? -5.173  12.828  70.043  1.00 19.41 ? 322 GLU   A N   1 
ATOM   2064 C  CA  . GLU   A 1 294 ? -5.591  12.353  68.735  1.00 20.75 ? 322 GLU   A CA  1 
ATOM   2065 C  C   . GLU   A 1 294 ? -6.337  11.023  68.838  1.00 18.86 ? 322 GLU   A C   1 
ATOM   2066 O  O   . GLU   A 1 294 ? -7.336  10.821  68.146  1.00 17.85 ? 322 GLU   A O   1 
ATOM   2067 C  CB  . GLU   A 1 294 ? -4.382  12.227  67.805  1.00 21.64 ? 322 GLU   A CB  1 
ATOM   2068 C  CG  . GLU   A 1 294 ? -3.716  13.558  67.425  1.00 24.70 ? 322 GLU   A CG  1 
ATOM   2069 C  CD  . GLU   A 1 294 ? -4.561  14.382  66.456  1.00 29.25 ? 322 GLU   A CD  1 
ATOM   2070 O  OE1 . GLU   A 1 294 ? -5.456  15.082  66.927  1.00 34.41 ? 322 GLU   A OE1 1 
ATOM   2071 O  OE2 . GLU   A 1 294 ? -4.364  14.299  65.220  1.00 40.35 ? 322 GLU   A OE2 1 
ATOM   2072 N  N   . MET   A 1 295 ? -5.875  10.106  69.700  1.00 18.99 ? 323 MET   A N   1 
ATOM   2073 C  CA  . MET   A 1 295 ? -6.541  8.809   69.800  1.00 17.20 ? 323 MET   A CA  1 
ATOM   2074 C  C   . MET   A 1 295 ? -7.923  8.946   70.440  1.00 18.95 ? 323 MET   A C   1 
ATOM   2075 O  O   . MET   A 1 295 ? -8.874  8.277   70.016  1.00 15.68 ? 323 MET   A O   1 
ATOM   2076 C  CB  . MET   A 1 295 ? -5.682  7.812   70.585  1.00 16.05 ? 323 MET   A CB  1 
ATOM   2077 C  CG  . MET   A 1 295 ? -4.394  7.363   69.866  1.00 17.40 ? 323 MET   A CG  1 
ATOM   2078 S  SD  . MET   A 1 295 ? -3.602  5.958   70.669  1.00 16.86 ? 323 MET   A SD  1 
ATOM   2079 C  CE  . MET   A 1 295 ? -4.768  4.618   70.334  1.00 12.77 ? 323 MET   A CE  1 
ATOM   2080 N  N   . ARG   A 1 296 ? -8.056  9.817   71.452  1.00 19.01 ? 324 ARG   A N   1 
ATOM   2081 C  CA  . ARG   A 1 296 ? -9.333  9.964   72.156  1.00 22.04 ? 324 ARG   A CA  1 
ATOM   2082 C  C   . ARG   A 1 296 ? -10.392 10.663  71.298  1.00 21.51 ? 324 ARG   A C   1 
ATOM   2083 O  O   . ARG   A 1 296 ? -11.579 10.340  71.399  1.00 22.96 ? 324 ARG   A O   1 
ATOM   2084 C  CB  . ARG   A 1 296 ? -9.129  10.722  73.465  1.00 23.34 ? 324 ARG   A CB  1 
ATOM   2085 C  CG  . ARG   A 1 296 ? -8.574  9.869   74.583  1.00 24.21 ? 324 ARG   A CG  1 
ATOM   2086 C  CD  . ARG   A 1 296 ? -8.595  10.646  75.876  1.00 30.17 ? 324 ARG   A CD  1 
ATOM   2087 N  NE  . ARG   A 1 296 ? -8.159  9.875   77.036  1.00 30.68 ? 324 ARG   A NE  1 
ATOM   2088 C  CZ  . ARG   A 1 296 ? -8.917  8.997   77.688  1.00 26.90 ? 324 ARG   A CZ  1 
ATOM   2089 N  NH1 . ARG   A 1 296 ? -10.152 8.746   77.293  1.00 25.89 ? 324 ARG   A NH1 1 
ATOM   2090 N  NH2 . ARG   A 1 296 ? -8.435  8.364   78.744  1.00 31.34 ? 324 ARG   A NH2 1 
ATOM   2091 N  N   . LYS   A 1 297 ? -9.995  11.630  70.462  1.00 18.83 ? 325 LYS   A N   1 
ATOM   2092 C  CA  . LYS   A 1 297 ? -10.953 12.218  69.524  1.00 18.94 ? 325 LYS   A CA  1 
ATOM   2093 C  C   . LYS   A 1 297 ? -11.581 11.160  68.625  1.00 21.39 ? 325 LYS   A C   1 
ATOM   2094 O  O   . LYS   A 1 297 ? -12.723 11.327  68.173  1.00 20.93 ? 325 LYS   A O   1 
ATOM   2095 C  CB  . LYS   A 1 297 ? -10.288 13.294  68.652  1.00 22.70 ? 325 LYS   A CB  1 
ATOM   2096 C  CG  . LYS   A 1 297 ? -9.783  14.503  69.395  1.00 31.09 ? 325 LYS   A CG  1 
ATOM   2097 C  CD  . LYS   A 1 297 ? -9.703  15.735  68.496  1.00 36.81 ? 325 LYS   A CD  1 
ATOM   2098 C  CE  . LYS   A 1 297 ? -8.410  15.760  67.702  1.00 34.40 ? 325 LYS   A CE  1 
ATOM   2099 N  NZ  . LYS   A 1 297 ? -7.628  17.008  67.939  1.00 41.85 ? 325 LYS   A NZ  1 
ATOM   2100 N  N   . ARG   A 1 298 ? -10.865 10.062  68.362  1.00 21.10 ? 326 ARG   A N   1 
ATOM   2101 C  CA  . ARG   A 1 298 ? -11.340 9.038   67.445  1.00 16.61 ? 326 ARG   A CA  1 
ATOM   2102 C  C   . ARG   A 1 298 ? -11.912 7.810   68.139  1.00 17.99 ? 326 ARG   A C   1 
ATOM   2103 O  O   . ARG   A 1 298 ? -12.324 6.880   67.448  1.00 16.91 ? 326 ARG   A O   1 
ATOM   2104 C  CB  . ARG   A 1 298 ? -10.211 8.620   66.501  1.00 18.45 ? 326 ARG   A CB  1 
ATOM   2105 C  CG  . ARG   A 1 298 ? -9.652  9.798   65.719  1.00 18.93 ? 326 ARG   A CG  1 
ATOM   2106 C  CD  . ARG   A 1 298 ? -8.325  9.471   65.098  1.00 17.44 ? 326 ARG   A CD  1 
ATOM   2107 N  NE  . ARG   A 1 298 ? -7.907  10.488  64.139  1.00 18.77 ? 326 ARG   A NE  1 
ATOM   2108 C  CZ  . ARG   A 1 298 ? -7.453  11.691  64.470  1.00 21.43 ? 326 ARG   A CZ  1 
ATOM   2109 N  NH1 . ARG   A 1 298 ? -7.371  12.047  65.743  1.00 24.06 ? 326 ARG   A NH1 1 
ATOM   2110 N  NH2 . ARG   A 1 298 ? -7.075  12.533  63.528  1.00 19.96 ? 326 ARG   A NH2 1 
ATOM   2111 N  N   . SER   A 1 299 ? -11.967 7.788   69.473  1.00 18.10 ? 327 SER   A N   1 
ATOM   2112 C  CA  . SER   A 1 299 ? -12.391 6.575   70.174  1.00 20.36 ? 327 SER   A CA  1 
ATOM   2113 C  C   . SER   A 1 299 ? -13.737 6.066   69.679  1.00 22.29 ? 327 SER   A C   1 
ATOM   2114 O  O   . SER   A 1 299 ? -13.918 4.862   69.452  1.00 23.89 ? 327 SER   A O   1 
ATOM   2115 C  CB  . SER   A 1 299 ? -12.462 6.838   71.676  1.00 19.52 ? 327 SER   A CB  1 
ATOM   2116 O  OG  . SER   A 1 299 ? -11.163 7.067   72.179  1.00 19.26 ? 327 SER   A OG  1 
ATOM   2117 N  N   . SER   A 1 300 ? -14.687 6.967   69.484  1.00 21.57 ? 328 SER   A N   1 
ATOM   2118 C  CA  . SER   A 1 300 ? -16.059 6.592   69.199  1.00 22.21 ? 328 SER   A CA  1 
ATOM   2119 C  C   . SER   A 1 300 ? -16.403 6.731   67.730  1.00 20.75 ? 328 SER   A C   1 
ATOM   2120 O  O   . SER   A 1 300 ? -17.576 6.596   67.361  1.00 19.86 ? 328 SER   A O   1 
ATOM   2121 C  CB  . SER   A 1 300 ? -17.004 7.427   70.063  1.00 29.45 ? 328 SER   A CB  1 
ATOM   2122 O  OG  . SER   A 1 300 ? -16.793 7.107   71.432  1.00 28.70 ? 328 SER   A OG  1 
ATOM   2123 N  N   . ILE   A 1 301 ? -15.404 6.975   66.880  1.00 17.32 ? 329 ILE   A N   1 
ATOM   2124 C  CA  . ILE   A 1 301 ? -15.632 7.065   65.446  1.00 14.63 ? 329 ILE   A CA  1 
ATOM   2125 C  C   . ILE   A 1 301 ? -14.639 6.155   64.737  1.00 14.24 ? 329 ILE   A C   1 
ATOM   2126 O  O   . ILE   A 1 301 ? -14.007 6.545   63.746  1.00 14.50 ? 329 ILE   A O   1 
ATOM   2127 C  CB  . ILE   A 1 301 ? -15.541 8.525   64.956  1.00 16.88 ? 329 ILE   A CB  1 
ATOM   2128 C  CG1 . ILE   A 1 301 ? -14.197 9.152   65.362  1.00 11.96 ? 329 ILE   A CG1 1 
ATOM   2129 C  CG2 . ILE   A 1 301 ? -16.754 9.353   65.502  1.00 14.70 ? 329 ILE   A CG2 1 
ATOM   2130 C  CD1 . ILE   A 1 301 ? -13.962 10.570  64.771  1.00 16.03 ? 329 ILE   A CD1 1 
ATOM   2131 N  N   . GLY   A 1 302 ? -14.507 4.928   65.240  1.00 17.71 ? 330 GLY   A N   1 
ATOM   2132 C  CA  . GLY   A 1 302 ? -13.751 3.874   64.590  1.00 15.52 ? 330 GLY   A CA  1 
ATOM   2133 C  C   . GLY   A 1 302 ? -12.431 3.535   65.255  1.00 17.34 ? 330 GLY   A C   1 
ATOM   2134 O  O   . GLY   A 1 302 ? -11.825 2.500   64.914  1.00 14.21 ? 330 GLY   A O   1 
ATOM   2135 N  N   . GLY   A 1 303 ? -11.971 4.346   66.202  1.00 15.13 ? 331 GLY   A N   1 
ATOM   2136 C  CA  . GLY   A 1 303 ? -10.688 4.129   66.860  1.00 13.54 ? 331 GLY   A CA  1 
ATOM   2137 C  C   . GLY   A 1 303 ? -10.741 3.209   68.066  1.00 18.54 ? 331 GLY   A C   1 
ATOM   2138 O  O   . GLY   A 1 303 ? -11.522 2.245   68.135  1.00 17.78 ? 331 GLY   A O   1 
ATOM   2139 N  N   . PHE   A 1 304 ? -9.889  3.510   69.036  1.00 17.88 ? 332 PHE   A N   1 
ATOM   2140 C  CA  . PHE   A 1 304 ? -9.723  2.677   70.213  1.00 18.31 ? 332 PHE   A CA  1 
ATOM   2141 C  C   . PHE   A 1 304 ? -10.255 3.394   71.444  1.00 19.56 ? 332 PHE   A C   1 
ATOM   2142 O  O   . PHE   A 1 304 ? -10.121 4.612   71.576  1.00 20.83 ? 332 PHE   A O   1 
ATOM   2143 C  CB  . PHE   A 1 304 ? -8.248  2.302   70.395  1.00 11.54 ? 332 PHE   A CB  1 
ATOM   2144 C  CG  . PHE   A 1 304 ? -7.725  1.403   69.311  1.00 14.94 ? 332 PHE   A CG  1 
ATOM   2145 C  CD1 . PHE   A 1 304 ? -7.918  0.023   69.378  1.00 13.41 ? 332 PHE   A CD1 1 
ATOM   2146 C  CD2 . PHE   A 1 304 ? -7.054  1.933   68.209  1.00 14.49 ? 332 PHE   A CD2 1 
ATOM   2147 C  CE1 . PHE   A 1 304 ? -7.438  -0.810  68.361  1.00 15.17 ? 332 PHE   A CE1 1 
ATOM   2148 C  CE2 . PHE   A 1 304 ? -6.565  1.112   67.200  1.00 13.76 ? 332 PHE   A CE2 1 
ATOM   2149 C  CZ  . PHE   A 1 304 ? -6.758  -0.257  67.267  1.00 14.05 ? 332 PHE   A CZ  1 
ATOM   2150 N  N   . ASP   A 1 305 ? -10.880 2.628   72.324  1.00 20.87 ? 333 ASP   A N   1 
ATOM   2151 C  CA  . ASP   A 1 305 ? -11.337 3.093   73.620  1.00 21.24 ? 333 ASP   A CA  1 
ATOM   2152 C  C   . ASP   A 1 305 ? -10.224 2.910   74.629  1.00 21.31 ? 333 ASP   A C   1 
ATOM   2153 O  O   . ASP   A 1 305 ? -9.377  2.027   74.487  1.00 20.90 ? 333 ASP   A O   1 
ATOM   2154 C  CB  . ASP   A 1 305 ? -12.564 2.306   74.095  1.00 20.77 ? 333 ASP   A CB  1 
ATOM   2155 C  CG  . ASP   A 1 305 ? -13.727 2.426   73.160  1.00 19.14 ? 333 ASP   A CG  1 
ATOM   2156 O  OD1 . ASP   A 1 305 ? -13.767 3.384   72.364  1.00 24.42 ? 333 ASP   A OD1 1 
ATOM   2157 O  OD2 . ASP   A 1 305 ? -14.613 1.566   73.219  1.00 20.64 ? 333 ASP   A OD2 1 
ATOM   2158 N  N   . PHE   A 1 306 ? -10.241 3.739   75.661  1.00 21.20 ? 334 PHE   A N   1 
ATOM   2159 C  CA  . PHE   A 1 306 ? -9.239  3.683   76.710  1.00 21.99 ? 334 PHE   A CA  1 
ATOM   2160 C  C   . PHE   A 1 306 ? -9.899  3.176   77.979  1.00 24.06 ? 334 PHE   A C   1 
ATOM   2161 O  O   . PHE   A 1 306 ? -11.108 3.326   78.153  1.00 23.90 ? 334 PHE   A O   1 
ATOM   2162 C  CB  . PHE   A 1 306 ? -8.587  5.061   76.902  1.00 22.67 ? 334 PHE   A CB  1 
ATOM   2163 C  CG  . PHE   A 1 306 ? -7.661  5.421   75.771  1.00 20.57 ? 334 PHE   A CG  1 
ATOM   2164 C  CD1 . PHE   A 1 306 ? -6.344  4.982   75.780  1.00 20.01 ? 334 PHE   A CD1 1 
ATOM   2165 C  CD2 . PHE   A 1 306 ? -8.124  6.118   74.667  1.00 21.50 ? 334 PHE   A CD2 1 
ATOM   2166 C  CE1 . PHE   A 1 306 ? -5.488  5.256   74.717  1.00 16.72 ? 334 PHE   A CE1 1 
ATOM   2167 C  CE2 . PHE   A 1 306 ? -7.275  6.410   73.612  1.00 19.59 ? 334 PHE   A CE2 1 
ATOM   2168 C  CZ  . PHE   A 1 306 ? -5.953  5.965   73.640  1.00 21.73 ? 334 PHE   A CZ  1 
ATOM   2169 N  N   . MET   A 1 307 ? -9.107  2.522   78.838  1.00 24.63 ? 335 MET   A N   1 
ATOM   2170 C  CA  . MET   A 1 307 ? -9.617  2.075   80.131  1.00 29.75 ? 335 MET   A CA  1 
ATOM   2171 C  C   . MET   A 1 307 ? -10.127 3.278   80.930  1.00 32.52 ? 335 MET   A C   1 
ATOM   2172 O  O   . MET   A 1 307 ? -9.835  4.428   80.596  1.00 29.60 ? 335 MET   A O   1 
ATOM   2173 C  CB  . MET   A 1 307 ? -8.530  1.332   80.918  1.00 29.91 ? 335 MET   A CB  1 
ATOM   2174 C  CG  . MET   A 1 307 ? -8.119  -0.039  80.352  1.00 26.75 ? 335 MET   A CG  1 
ATOM   2175 S  SD  . MET   A 1 307 ? -9.458  -1.253  80.291  1.00 33.71 ? 335 MET   A SD  1 
ATOM   2176 C  CE  . MET   A 1 307 ? -9.778  -1.433  82.042  1.00 35.88 ? 335 MET   A CE  1 
ATOM   2177 N  N   . PRO   A 1 308 ? -10.932 3.046   81.967  1.00 36.60 ? 336 PRO   A N   1 
ATOM   2178 C  CA  . PRO   A 1 308 ? -11.442 4.181   82.752  1.00 36.62 ? 336 PRO   A CA  1 
ATOM   2179 C  C   . PRO   A 1 308 ? -10.324 4.969   83.438  1.00 37.23 ? 336 PRO   A C   1 
ATOM   2180 O  O   . PRO   A 1 308 ? -9.322  4.418   83.903  1.00 36.53 ? 336 PRO   A O   1 
ATOM   2181 C  CB  . PRO   A 1 308 ? -12.390 3.524   83.767  1.00 35.01 ? 336 PRO   A CB  1 
ATOM   2182 C  CG  . PRO   A 1 308 ? -12.228 2.044   83.607  1.00 38.56 ? 336 PRO   A CG  1 
ATOM   2183 C  CD  . PRO   A 1 308 ? -11.665 1.801   82.245  1.00 34.44 ? 336 PRO   A CD  1 
ATOM   2184 N  N   . SER   A 1 309 ? -10.498 6.285   83.469  1.00 39.27 ? 337 SER   A N   1 
ATOM   2185 C  CA  . SER   A 1 309 ? -9.491  7.157   84.050  1.00 39.38 ? 337 SER   A CA  1 
ATOM   2186 C  C   . SER   A 1 309 ? -9.392  6.937   85.559  1.00 34.45 ? 337 SER   A C   1 
ATOM   2187 O  O   . SER   A 1 309 ? -10.389 6.638   86.218  1.00 37.93 ? 337 SER   A O   1 
ATOM   2188 C  CB  . SER   A 1 309 ? -9.826  8.616   83.766  1.00 38.60 ? 337 SER   A CB  1 
ATOM   2189 O  OG  . SER   A 1 309 ? -9.633  8.930   82.402  1.00 34.36 ? 337 SER   A OG  1 
ATOM   2190 N  N   . PRO   A 1 310 ? -8.200  7.074   86.130  1.00 40.32 ? 338 PRO   A N   1 
ATOM   2191 C  CA  . PRO   A 1 310 ? -8.068  7.000   87.592  1.00 43.06 ? 338 PRO   A CA  1 
ATOM   2192 C  C   . PRO   A 1 310 ? -8.780  8.169   88.251  1.00 46.06 ? 338 PRO   A C   1 
ATOM   2193 O  O   . PRO   A 1 310 ? -9.047  9.186   87.592  1.00 38.12 ? 338 PRO   A O   1 
ATOM   2194 C  CB  . PRO   A 1 310 ? -6.551  7.061   87.815  1.00 39.24 ? 338 PRO   A CB  1 
ATOM   2195 C  CG  . PRO   A 1 310 ? -6.005  7.690   86.594  1.00 41.26 ? 338 PRO   A CG  1 
ATOM   2196 C  CD  . PRO   A 1 310 ? -6.904  7.286   85.463  1.00 38.10 ? 338 PRO   A CD  1 
ATOM   2197 N  N   . PRO   A 1 311 ? -9.115  8.061   89.539  1.00 45.72 ? 339 PRO   A N   1 
ATOM   2198 C  CA  . PRO   A 1 311 ? -9.848  9.139   90.214  1.00 46.18 ? 339 PRO   A CA  1 
ATOM   2199 C  C   . PRO   A 1 311 ? -8.983  10.377  90.365  1.00 46.86 ? 339 PRO   A C   1 
ATOM   2200 O  O   . PRO   A 1 311 ? -7.747  10.298  90.280  1.00 42.50 ? 339 PRO   A O   1 
ATOM   2201 C  CB  . PRO   A 1 311 ? -10.187 8.531   91.581  1.00 47.42 ? 339 PRO   A CB  1 
ATOM   2202 C  CG  . PRO   A 1 311 ? -9.140  7.520   91.803  1.00 47.57 ? 339 PRO   A CG  1 
ATOM   2203 C  CD  . PRO   A 1 311 ? -8.816  6.948   90.456  1.00 47.33 ? 339 PRO   A CD  1 
ATOM   2204 N  N   . PRO   A 1 312 ? -9.592  11.546  90.590  1.00 47.10 ? 340 PRO   A N   1 
ATOM   2205 C  CA  . PRO   A 1 312 ? -8.784  12.759  90.783  1.00 48.47 ? 340 PRO   A CA  1 
ATOM   2206 C  C   . PRO   A 1 312 ? -7.838  12.667  91.961  1.00 44.67 ? 340 PRO   A C   1 
ATOM   2207 O  O   . PRO   A 1 312 ? -6.828  13.387  91.979  1.00 44.66 ? 340 PRO   A O   1 
ATOM   2208 C  CB  . PRO   A 1 312 ? -9.836  13.861  90.979  1.00 45.88 ? 340 PRO   A CB  1 
ATOM   2209 C  CG  . PRO   A 1 312 ? -11.062 13.150  91.382  1.00 47.21 ? 340 PRO   A CG  1 
ATOM   2210 C  CD  . PRO   A 1 312 ? -11.034 11.823  90.707  1.00 49.19 ? 340 PRO   A CD  1 
ATOM   2211 N  N   . THR   A 1 313 ? -8.129  11.802  92.937  1.00 44.52 ? 341 THR   A N   1 
ATOM   2212 C  CA  . THR   A 1 313 ? -7.179  11.542  94.013  1.00 47.80 ? 341 THR   A CA  1 
ATOM   2213 C  C   . THR   A 1 313 ? -5.832  11.082  93.464  1.00 48.56 ? 341 THR   A C   1 
ATOM   2214 O  O   . THR   A 1 313 ? -4.777  11.514  93.949  1.00 43.58 ? 341 THR   A O   1 
ATOM   2215 C  CB  . THR   A 1 313 ? -7.756  10.505  94.976  1.00 52.12 ? 341 THR   A CB  1 
ATOM   2216 O  OG1 . THR   A 1 313 ? -8.343  9.429   94.233  1.00 49.41 ? 341 THR   A OG1 1 
ATOM   2217 C  CG2 . THR   A 1 313 ? -8.830  11.145  95.835  1.00 55.97 ? 341 THR   A CG2 1 
ATOM   2218 N  N   . TYR   A 1 314 ? -5.852  10.225  92.432  1.00 44.59 ? 342 TYR   A N   1 
ATOM   2219 C  CA  . TYR   A 1 314 ? -4.613  9.780   91.804  1.00 41.57 ? 342 TYR   A CA  1 
ATOM   2220 C  C   . TYR   A 1 314 ? -3.800  10.967  91.312  1.00 43.57 ? 342 TYR   A C   1 
ATOM   2221 O  O   . TYR   A 1 314 ? -2.571  10.982  91.432  1.00 41.00 ? 342 TYR   A O   1 
ATOM   2222 C  CB  . TYR   A 1 314 ? -4.918  8.826   90.643  1.00 40.14 ? 342 TYR   A CB  1 
ATOM   2223 C  CG  . TYR   A 1 314 ? -3.687  8.336   89.902  1.00 41.36 ? 342 TYR   A CG  1 
ATOM   2224 C  CD1 . TYR   A 1 314 ? -3.031  7.169   90.296  1.00 41.80 ? 342 TYR   A CD1 1 
ATOM   2225 C  CD2 . TYR   A 1 314 ? -3.174  9.035   88.816  1.00 38.48 ? 342 TYR   A CD2 1 
ATOM   2226 C  CE1 . TYR   A 1 314 ? -1.901  6.718   89.630  1.00 37.73 ? 342 TYR   A CE1 1 
ATOM   2227 C  CE2 . TYR   A 1 314 ? -2.047  8.593   88.150  1.00 37.81 ? 342 TYR   A CE2 1 
ATOM   2228 C  CZ  . TYR   A 1 314 ? -1.419  7.434   88.555  1.00 35.53 ? 342 TYR   A CZ  1 
ATOM   2229 O  OH  . TYR   A 1 314 ? -0.301  7.000   87.884  1.00 33.36 ? 342 TYR   A OH  1 
ATOM   2230 N  N   . TYR   A 1 315 ? -4.469  11.972  90.751  1.00 39.80 ? 343 TYR   A N   1 
ATOM   2231 C  CA  . TYR   A 1 315 ? -3.749  13.121  90.224  1.00 44.92 ? 343 TYR   A CA  1 
ATOM   2232 C  C   . TYR   A 1 315 ? -3.375  14.115  91.314  1.00 44.63 ? 343 TYR   A C   1 
ATOM   2233 O  O   . TYR   A 1 315 ? -2.319  14.751  91.219  1.00 44.44 ? 343 TYR   A O   1 
ATOM   2234 C  CB  . TYR   A 1 315 ? -4.574  13.775  89.116  1.00 46.75 ? 343 TYR   A CB  1 
ATOM   2235 C  CG  . TYR   A 1 315 ? -4.687  12.843  87.940  1.00 45.72 ? 343 TYR   A CG  1 
ATOM   2236 C  CD1 . TYR   A 1 315 ? -5.791  12.019  87.783  1.00 43.87 ? 343 TYR   A CD1 1 
ATOM   2237 C  CD2 . TYR   A 1 315 ? -3.650  12.735  87.023  1.00 45.20 ? 343 TYR   A CD2 1 
ATOM   2238 C  CE1 . TYR   A 1 315 ? -5.873  11.146  86.719  1.00 42.62 ? 343 TYR   A CE1 1 
ATOM   2239 C  CE2 . TYR   A 1 315 ? -3.716  11.861  85.964  1.00 38.88 ? 343 TYR   A CE2 1 
ATOM   2240 C  CZ  . TYR   A 1 315 ? -4.828  11.072  85.815  1.00 39.75 ? 343 TYR   A CZ  1 
ATOM   2241 O  OH  . TYR   A 1 315 ? -4.902  10.204  84.759  1.00 36.52 ? 343 TYR   A OH  1 
ATOM   2242 N  N   . GLN   A 1 316 ? -4.204  14.250  92.354  1.00 45.61 ? 344 GLN   A N   1 
ATOM   2243 C  CA  . GLN   A 1 316 ? -3.802  15.018  93.526  1.00 47.00 ? 344 GLN   A CA  1 
ATOM   2244 C  C   . GLN   A 1 316 ? -2.548  14.448  94.172  1.00 51.50 ? 344 GLN   A C   1 
ATOM   2245 O  O   . GLN   A 1 316 ? -1.780  15.204  94.775  1.00 55.35 ? 344 GLN   A O   1 
ATOM   2246 C  CB  . GLN   A 1 316 ? -4.937  15.070  94.550  1.00 46.54 ? 344 GLN   A CB  1 
ATOM   2247 N  N   . ASN   A 1 317 ? -2.311  13.139  94.047  1.00 46.96 ? 345 ASN   A N   1 
ATOM   2248 C  CA  . ASN   A 1 317 ? -1.116  12.519  94.601  1.00 44.89 ? 345 ASN   A CA  1 
ATOM   2249 C  C   . ASN   A 1 317 ? 0.078   12.555  93.659  1.00 44.11 ? 345 ASN   A C   1 
ATOM   2250 O  O   . ASN   A 1 317 ? 1.180   12.190  94.074  1.00 46.42 ? 345 ASN   A O   1 
ATOM   2251 C  CB  . ASN   A 1 317 ? -1.400  11.070  95.004  1.00 45.35 ? 345 ASN   A CB  1 
ATOM   2252 C  CG  . ASN   A 1 317 ? -2.526  10.960  96.001  1.00 47.93 ? 345 ASN   A CG  1 
ATOM   2253 O  OD1 . ASN   A 1 317 ? -2.877  11.935  96.664  1.00 53.20 ? 345 ASN   A OD1 1 
ATOM   2254 N  ND2 . ASN   A 1 317 ? -3.095  9.768   96.124  1.00 48.94 ? 345 ASN   A ND2 1 
ATOM   2255 N  N   . LEU   A 1 318 ? -0.096  13.003  92.416  1.00 45.52 ? 346 LEU   A N   1 
ATOM   2256 C  CA  . LEU   A 1 318 ? 1.037   13.039  91.496  1.00 46.72 ? 346 LEU   A CA  1 
ATOM   2257 C  C   . LEU   A 1 318 ? 2.033   14.131  91.853  1.00 48.33 ? 346 LEU   A C   1 
ATOM   2258 O  O   . LEU   A 1 318 ? 3.233   13.967  91.602  1.00 44.37 ? 346 LEU   A O   1 
ATOM   2259 C  CB  . LEU   A 1 318 ? 0.568   13.237  90.057  1.00 45.03 ? 346 LEU   A CB  1 
ATOM   2260 C  CG  . LEU   A 1 318 ? -0.130  12.075  89.365  1.00 47.61 ? 346 LEU   A CG  1 
ATOM   2261 C  CD1 . LEU   A 1 318 ? -0.454  12.490  87.952  1.00 42.67 ? 346 LEU   A CD1 1 
ATOM   2262 C  CD2 . LEU   A 1 318 ? 0.764   10.845  89.381  1.00 44.28 ? 346 LEU   A CD2 1 
ATOM   2263 N  N   . LYS   A 1 319 ? 1.561   15.254  92.406  1.00 46.75 ? 347 LYS   A N   1 
ATOM   2264 C  CA  . LYS   A 1 319 ? 2.476   16.329  92.781  1.00 52.17 ? 347 LYS   A CA  1 
ATOM   2265 C  C   . LYS   A 1 319 ? 3.549   15.824  93.740  1.00 48.39 ? 347 LYS   A C   1 
ATOM   2266 O  O   . LYS   A 1 319 ? 4.739   16.096  93.544  1.00 42.59 ? 347 LYS   A O   1 
ATOM   2267 C  CB  . LYS   A 1 319 ? 1.703   17.502  93.397  1.00 46.83 ? 347 LYS   A CB  1 
ATOM   2268 N  N   . LYS   A 1 320 ? 3.148   15.057  94.762  1.00 45.81 ? 348 LYS   A N   1 
ATOM   2269 C  CA  . LYS   A 1 320 ? 4.076   14.537  95.760  1.00 47.12 ? 348 LYS   A CA  1 
ATOM   2270 C  C   . LYS   A 1 320 ? 5.033   13.498  95.201  1.00 50.85 ? 348 LYS   A C   1 
ATOM   2271 O  O   . LYS   A 1 320 ? 6.032   13.190  95.857  1.00 52.23 ? 348 LYS   A O   1 
ATOM   2272 C  CB  . LYS   A 1 320 ? 3.311   13.922  96.939  1.00 44.91 ? 348 LYS   A CB  1 
ATOM   2273 N  N   . ARG   A 1 321 ? 4.752   12.932  94.031  1.00 49.84 ? 349 ARG   A N   1 
ATOM   2274 C  CA  . ARG   A 1 321 ? 5.588   11.868  93.493  1.00 49.09 ? 349 ARG   A CA  1 
ATOM   2275 C  C   . ARG   A 1 321 ? 6.429   12.293  92.304  1.00 45.89 ? 349 ARG   A C   1 
ATOM   2276 O  O   . ARG   A 1 321 ? 7.561   11.829  92.167  1.00 43.49 ? 349 ARG   A O   1 
ATOM   2277 C  CB  . ARG   A 1 321 ? 4.727   10.667  93.078  1.00 49.33 ? 349 ARG   A CB  1 
ATOM   2278 C  CG  . ARG   A 1 321 ? 3.736   10.178  94.121  1.00 49.17 ? 349 ARG   A CG  1 
ATOM   2279 C  CD  . ARG   A 1 321 ? 2.626   9.325   93.464  1.00 52.98 ? 349 ARG   A CD  1 
ATOM   2280 N  NE  . ARG   A 1 321 ? 3.252   8.240   92.720  1.00 54.55 ? 349 ARG   A NE  1 
ATOM   2281 C  CZ  . ARG   A 1 321 ? 2.771   7.742   91.586  1.00 49.27 ? 349 ARG   A CZ  1 
ATOM   2282 N  NH1 . ARG   A 1 321 ? 1.652   8.227   91.043  1.00 43.77 ? 349 ARG   A NH1 1 
ATOM   2283 N  NH2 . ARG   A 1 321 ? 3.409   6.751   90.985  1.00 44.60 ? 349 ARG   A NH2 1 
ATOM   2284 N  N   . VAL   A 1 322 ? 5.905   13.158  91.441  1.00 44.33 ? 350 VAL   A N   1 
ATOM   2285 C  CA  . VAL   A 1 322 ? 6.581   13.496  90.194  1.00 47.74 ? 350 VAL   A CA  1 
ATOM   2286 C  C   . VAL   A 1 322 ? 6.569   15.008  89.999  1.00 50.01 ? 350 VAL   A C   1 
ATOM   2287 O  O   . VAL   A 1 322 ? 6.779   15.502  88.883  1.00 48.61 ? 350 VAL   A O   1 
ATOM   2288 C  CB  . VAL   A 1 322 ? 5.930   12.770  89.000  1.00 50.83 ? 350 VAL   A CB  1 
ATOM   2289 C  CG1 . VAL   A 1 322 ? 6.008   11.246  89.180  1.00 42.61 ? 350 VAL   A CG1 1 
ATOM   2290 C  CG2 . VAL   A 1 322 ? 4.481   13.223  88.828  1.00 47.54 ? 350 VAL   A CG2 1 
ATOM   2291 N  N   . GLY   A 1 323 ? 6.343   15.752  91.089  1.00 49.93 ? 351 GLY   A N   1 
ATOM   2292 C  CA  . GLY   A 1 323 ? 6.304   17.205  91.029  1.00 46.43 ? 351 GLY   A CA  1 
ATOM   2293 C  C   . GLY   A 1 323 ? 7.587   17.847  90.543  1.00 44.77 ? 351 GLY   A C   1 
ATOM   2294 O  O   . GLY   A 1 323 ? 7.561   18.992  90.086  1.00 47.38 ? 351 GLY   A O   1 
ATOM   2295 N  N   . ASP   A 1 324 ? 8.706   17.134  90.623  1.00 48.05 ? 352 ASP   A N   1 
ATOM   2296 C  CA  . ASP   A 1 324 ? 10.000  17.621  90.163  1.00 52.34 ? 352 ASP   A CA  1 
ATOM   2297 C  C   . ASP   A 1 324 ? 10.305  17.248  88.717  1.00 53.56 ? 352 ASP   A C   1 
ATOM   2298 O  O   . ASP   A 1 324 ? 11.260  17.781  88.141  1.00 50.61 ? 352 ASP   A O   1 
ATOM   2299 C  CB  . ASP   A 1 324 ? 11.102  17.065  91.054  1.00 52.24 ? 352 ASP   A CB  1 
ATOM   2300 C  CG  . ASP   A 1 324 ? 11.107  15.555  91.082  1.00 54.61 ? 352 ASP   A CG  1 
ATOM   2301 O  OD1 . ASP   A 1 324 ? 12.074  14.947  90.579  1.00 61.08 ? 352 ASP   A OD1 1 
ATOM   2302 O  OD2 . ASP   A 1 324 ? 10.124  14.976  91.581  1.00 54.37 ? 352 ASP   A OD2 1 
ATOM   2303 N  N   . VAL   A 1 325 ? 9.544   16.330  88.136  1.00 54.90 ? 353 VAL   A N   1 
ATOM   2304 C  CA  . VAL   A 1 325 ? 9.698   15.948  86.742  1.00 49.77 ? 353 VAL   A CA  1 
ATOM   2305 C  C   . VAL   A 1 325 ? 8.681   16.646  85.855  1.00 42.26 ? 353 VAL   A C   1 
ATOM   2306 O  O   . VAL   A 1 325 ? 9.009   17.073  84.750  1.00 46.27 ? 353 VAL   A O   1 
ATOM   2307 C  CB  . VAL   A 1 325 ? 9.597   14.416  86.603  1.00 51.43 ? 353 VAL   A CB  1 
ATOM   2308 C  CG1 . VAL   A 1 325 ? 10.070  13.962  85.237  1.00 51.11 ? 353 VAL   A CG1 1 
ATOM   2309 C  CG2 . VAL   A 1 325 ? 10.419  13.736  87.688  1.00 49.63 ? 353 VAL   A CG2 1 
ATOM   2310 N  N   . LEU   A 1 326 ? 7.458   16.804  86.338  1.00 41.21 ? 354 LEU   A N   1 
ATOM   2311 C  CA  . LEU   A 1 326 ? 6.376   17.388  85.558  1.00 41.50 ? 354 LEU   A CA  1 
ATOM   2312 C  C   . LEU   A 1 326 ? 5.810   18.603  86.280  1.00 44.55 ? 354 LEU   A C   1 
ATOM   2313 O  O   . LEU   A 1 326 ? 5.536   18.554  87.486  1.00 45.26 ? 354 LEU   A O   1 
ATOM   2314 C  CB  . LEU   A 1 326 ? 5.257   16.366  85.314  1.00 45.28 ? 354 LEU   A CB  1 
ATOM   2315 C  CG  . LEU   A 1 326 ? 5.606   15.018  84.669  1.00 43.49 ? 354 LEU   A CG  1 
ATOM   2316 C  CD1 . LEU   A 1 326 ? 4.358   14.162  84.576  1.00 38.47 ? 354 LEU   A CD1 1 
ATOM   2317 C  CD2 . LEU   A 1 326 ? 6.215   15.205  83.288  1.00 43.02 ? 354 LEU   A CD2 1 
ATOM   2318 N  N   . SER   A 1 327 ? 5.624   19.684  85.537  1.00 40.89 ? 355 SER   A N   1 
ATOM   2319 C  CA  . SER   A 1 327 ? 4.974   20.868  86.066  1.00 46.83 ? 355 SER   A CA  1 
ATOM   2320 C  C   . SER   A 1 327 ? 3.517   20.569  86.426  1.00 47.02 ? 355 SER   A C   1 
ATOM   2321 O  O   . SER   A 1 327 ? 2.955   19.529  86.065  1.00 44.10 ? 355 SER   A O   1 
ATOM   2322 C  CB  . SER   A 1 327 ? 5.044   21.998  85.047  1.00 44.03 ? 355 SER   A CB  1 
ATOM   2323 O  OG  . SER   A 1 327 ? 4.153   21.737  83.981  1.00 41.84 ? 355 SER   A OG  1 
ATOM   2324 N  N   . ASP   A 1 328 ? 2.902   21.508  87.157  1.00 43.02 ? 356 ASP   A N   1 
ATOM   2325 C  CA  . ASP   A 1 328 ? 1.491   21.370  87.498  1.00 44.22 ? 356 ASP   A CA  1 
ATOM   2326 C  C   . ASP   A 1 328 ? 0.621   21.386  86.253  1.00 46.79 ? 356 ASP   A C   1 
ATOM   2327 O  O   . ASP   A 1 328 ? -0.429  20.732  86.217  1.00 43.71 ? 356 ASP   A O   1 
ATOM   2328 C  CB  . ASP   A 1 328 ? 1.051   22.486  88.452  1.00 45.07 ? 356 ASP   A CB  1 
ATOM   2329 C  CG  . ASP   A 1 328 ? 1.688   22.375  89.834  1.00 58.24 ? 356 ASP   A CG  1 
ATOM   2330 O  OD1 . ASP   A 1 328 ? 2.512   21.464  90.061  1.00 57.86 ? 356 ASP   A OD1 1 
ATOM   2331 O  OD2 . ASP   A 1 328 ? 1.369   23.219  90.703  1.00 58.68 ? 356 ASP   A OD2 1 
ATOM   2332 N  N   . ASP   A 1 329 ? 1.029   22.136  85.226  1.00 45.38 ? 357 ASP   A N   1 
ATOM   2333 C  CA  . ASP   A 1 329 ? 0.269   22.136  83.979  1.00 46.96 ? 357 ASP   A CA  1 
ATOM   2334 C  C   . ASP   A 1 329 ? 0.388   20.795  83.265  1.00 42.38 ? 357 ASP   A C   1 
ATOM   2335 O  O   . ASP   A 1 329 ? -0.609  20.262  82.764  1.00 36.15 ? 357 ASP   A O   1 
ATOM   2336 C  CB  . ASP   A 1 329 ? 0.736   23.274  83.074  1.00 44.74 ? 357 ASP   A CB  1 
ATOM   2337 C  CG  . ASP   A 1 329 ? 0.567   24.633  83.726  1.00 57.76 ? 357 ASP   A CG  1 
ATOM   2338 O  OD1 . ASP   A 1 329 ? -0.553  25.186  83.649  1.00 57.34 ? 357 ASP   A OD1 1 
ATOM   2339 O  OD2 . ASP   A 1 329 ? 1.549   25.152  84.310  1.00 58.62 ? 357 ASP   A OD2 1 
ATOM   2340 N  N   . GLN   A 1 330 ? 1.602   20.237  83.213  1.00 42.44 ? 358 GLN   A N   1 
ATOM   2341 C  CA  . GLN   A 1 330 ? 1.789   18.906  82.643  1.00 43.12 ? 358 GLN   A CA  1 
ATOM   2342 C  C   . GLN   A 1 330 ? 1.064   17.840  83.452  1.00 42.32 ? 358 GLN   A C   1 
ATOM   2343 O  O   . GLN   A 1 330 ? 0.576   16.854  82.884  1.00 41.20 ? 358 GLN   A O   1 
ATOM   2344 C  CB  . GLN   A 1 330 ? 3.282   18.594  82.541  1.00 36.27 ? 358 GLN   A CB  1 
ATOM   2345 C  CG  . GLN   A 1 330 ? 3.956   19.447  81.506  1.00 37.19 ? 358 GLN   A CG  1 
ATOM   2346 C  CD  . GLN   A 1 330 ? 5.402   19.774  81.838  1.00 45.83 ? 358 GLN   A CD  1 
ATOM   2347 O  OE1 . GLN   A 1 330 ? 6.063   19.071  82.616  1.00 42.26 ? 358 GLN   A OE1 1 
ATOM   2348 N  NE2 . GLN   A 1 330 ? 5.904   20.858  81.242  1.00 39.84 ? 358 GLN   A NE2 1 
ATOM   2349 N  N   . ILE   A 1 331 ? 0.977   18.015  84.772  1.00 43.24 ? 359 ILE   A N   1 
ATOM   2350 C  CA  . ILE   A 1 331 ? 0.188   17.089  85.577  1.00 40.60 ? 359 ILE   A CA  1 
ATOM   2351 C  C   . ILE   A 1 331 ? -1.292  17.253  85.265  1.00 42.07 ? 359 ILE   A C   1 
ATOM   2352 O  O   . ILE   A 1 331 ? -2.017  16.262  85.101  1.00 39.09 ? 359 ILE   A O   1 
ATOM   2353 C  CB  . ILE   A 1 331 ? 0.492   17.272  87.078  1.00 42.34 ? 359 ILE   A CB  1 
ATOM   2354 C  CG1 . ILE   A 1 331 ? 1.889   16.719  87.402  1.00 44.77 ? 359 ILE   A CG1 1 
ATOM   2355 C  CG2 . ILE   A 1 331 ? -0.566  16.592  87.938  1.00 48.46 ? 359 ILE   A CG2 1 
ATOM   2356 C  CD1 . ILE   A 1 331 ? 2.402   17.071  88.796  1.00 48.59 ? 359 ILE   A CD1 1 
ATOM   2357 N  N   . LYS   A 1 332 ? -1.763  18.500  85.154  1.00 40.64 ? 360 LYS   A N   1 
ATOM   2358 C  CA  . LYS   A 1 332 ? -3.157  18.719  84.775  1.00 41.44 ? 360 LYS   A CA  1 
ATOM   2359 C  C   . LYS   A 1 332 ? -3.436  18.149  83.392  1.00 37.52 ? 360 LYS   A C   1 
ATOM   2360 O  O   . LYS   A 1 332 ? -4.538  17.658  83.126  1.00 35.88 ? 360 LYS   A O   1 
ATOM   2361 C  CB  . LYS   A 1 332 ? -3.504  20.213  84.820  1.00 39.33 ? 360 LYS   A CB  1 
ATOM   2362 N  N   . GLU   A 1 333 ? -2.440  18.187  82.503  1.00 40.38 ? 361 GLU   A N   1 
ATOM   2363 C  CA  . GLU   A 1 333 ? -2.627  17.619  81.172  1.00 40.65 ? 361 GLU   A CA  1 
ATOM   2364 C  C   . GLU   A 1 333 ? -2.732  16.094  81.233  1.00 39.04 ? 361 GLU   A C   1 
ATOM   2365 O  O   . GLU   A 1 333 ? -3.554  15.499  80.527  1.00 37.06 ? 361 GLU   A O   1 
ATOM   2366 C  CB  . GLU   A 1 333 ? -1.495  18.073  80.250  1.00 40.31 ? 361 GLU   A CB  1 
ATOM   2367 C  CG  . GLU   A 1 333 ? -1.833  17.994  78.772  1.00 39.51 ? 361 GLU   A CG  1 
ATOM   2368 C  CD  . GLU   A 1 333 ? -0.959  18.908  77.934  1.00 47.13 ? 361 GLU   A CD  1 
ATOM   2369 O  OE1 . GLU   A 1 333 ? -1.080  18.860  76.689  1.00 46.04 ? 361 GLU   A OE1 1 
ATOM   2370 O  OE2 . GLU   A 1 333 ? -0.156  19.680  78.516  1.00 40.23 ? 361 GLU   A OE2 1 
ATOM   2371 N  N   . CYS   A 1 334 ? -1.926  15.445  82.087  1.00 39.70 ? 362 CYS   A N   1 
ATOM   2372 C  CA  . CYS   A 1 334 ? -2.118  14.018  82.353  1.00 37.38 ? 362 CYS   A CA  1 
ATOM   2373 C  C   . CYS   A 1 334 ? -3.526  13.737  82.843  1.00 39.03 ? 362 CYS   A C   1 
ATOM   2374 O  O   . CYS   A 1 334 ? -4.108  12.696  82.510  1.00 36.93 ? 362 CYS   A O   1 
ATOM   2375 C  CB  . CYS   A 1 334 ? -1.111  13.505  83.392  1.00 27.01 ? 362 CYS   A CB  1 
ATOM   2376 S  SG  . CYS   A 1 334 ? 0.602   13.489  82.820  1.00 35.63 ? 362 CYS   A SG  1 
ATOM   2377 N  N   . GLU   A 1 335 ? -4.100  14.657  83.619  1.00 40.93 ? 363 GLU   A N   1 
ATOM   2378 C  CA  . GLU   A 1 335 ? -5.403  14.390  84.212  1.00 41.29 ? 363 GLU   A CA  1 
ATOM   2379 C  C   . GLU   A 1 335 ? -6.528  14.478  83.187  1.00 36.01 ? 363 GLU   A C   1 
ATOM   2380 O  O   . GLU   A 1 335 ? -7.470  13.681  83.238  1.00 38.06 ? 363 GLU   A O   1 
ATOM   2381 C  CB  . GLU   A 1 335 ? -5.658  15.346  85.376  1.00 44.34 ? 363 GLU   A CB  1 
ATOM   2382 C  CG  . GLU   A 1 335 ? -6.979  15.098  86.091  1.00 39.44 ? 363 GLU   A CG  1 
ATOM   2383 C  CD  . GLU   A 1 335 ? -7.112  15.919  87.364  1.00 48.81 ? 363 GLU   A CD  1 
ATOM   2384 O  OE1 . GLU   A 1 335 ? -8.061  15.662  88.138  1.00 48.96 ? 363 GLU   A OE1 1 
ATOM   2385 O  OE2 . GLU   A 1 335 ? -6.267  16.815  87.591  1.00 50.11 ? 363 GLU   A OE2 1 
ATOM   2386 N  N   . GLU   A 1 336 ? -6.468  15.429  82.251  1.00 36.83 ? 364 GLU   A N   1 
ATOM   2387 C  CA  . GLU   A 1 336 ? -7.552  15.500  81.273  1.00 42.40 ? 364 GLU   A CA  1 
ATOM   2388 C  C   . GLU   A 1 336 ? -7.524  14.301  80.337  1.00 39.94 ? 364 GLU   A C   1 
ATOM   2389 O  O   . GLU   A 1 336 ? -8.577  13.848  79.874  1.00 43.83 ? 364 GLU   A O   1 
ATOM   2390 C  CB  . GLU   A 1 336 ? -7.484  16.794  80.459  1.00 45.40 ? 364 GLU   A CB  1 
ATOM   2391 C  CG  . GLU   A 1 336 ? -6.087  17.285  80.183  1.00 44.90 ? 364 GLU   A CG  1 
ATOM   2392 C  CD  . GLU   A 1 336 ? -6.065  18.643  79.510  1.00 54.50 ? 364 GLU   A CD  1 
ATOM   2393 O  OE1 . GLU   A 1 336 ? -6.107  18.677  78.257  1.00 63.44 ? 364 GLU   A OE1 1 
ATOM   2394 O  OE2 . GLU   A 1 336 ? -5.994  19.676  80.217  1.00 50.88 ? 364 GLU   A OE2 1 
ATOM   2395 N  N   . LEU   A 1 337 ? -6.338  13.762  80.075  1.00 36.37 ? 365 LEU   A N   1 
ATOM   2396 C  CA  . LEU   A 1 337 ? -6.152  12.660  79.143  1.00 34.26 ? 365 LEU   A CA  1 
ATOM   2397 C  C   . LEU   A 1 337 ? -6.240  11.281  79.782  1.00 30.47 ? 365 LEU   A C   1 
ATOM   2398 O  O   . LEU   A 1 337 ? -6.333  10.292  79.051  1.00 32.87 ? 365 LEU   A O   1 
ATOM   2399 C  CB  . LEU   A 1 337 ? -4.803  12.819  78.437  1.00 32.80 ? 365 LEU   A CB  1 
ATOM   2400 C  CG  . LEU   A 1 337 ? -4.706  14.109  77.611  1.00 33.16 ? 365 LEU   A CG  1 
ATOM   2401 C  CD1 . LEU   A 1 337 ? -3.354  14.232  76.991  1.00 33.15 ? 365 LEU   A CD1 1 
ATOM   2402 C  CD2 . LEU   A 1 337 ? -5.742  14.083  76.521  1.00 26.40 ? 365 LEU   A CD2 1 
ATOM   2403 N  N   . GLY   A 1 338 ? -6.237  11.185  81.107  1.00 33.93 ? 366 GLY   A N   1 
ATOM   2404 C  CA  . GLY   A 1 338 ? -6.296  9.887   81.753  1.00 30.57 ? 366 GLY   A CA  1 
ATOM   2405 C  C   . GLY   A 1 338 ? -4.970  9.172   81.865  1.00 28.63 ? 366 GLY   A C   1 
ATOM   2406 O  O   . GLY   A 1 338 ? -4.945  7.956   82.091  1.00 27.78 ? 366 GLY   A O   1 
ATOM   2407 N  N   . ILE   A 1 339 ? -3.861  9.896   81.747  1.00 27.44 ? 367 ILE   A N   1 
ATOM   2408 C  CA  . ILE   A 1 339 ? -2.531  9.297   81.711  1.00 30.41 ? 367 ILE   A CA  1 
ATOM   2409 C  C   . ILE   A 1 339 ? -2.079  8.897   83.115  1.00 34.47 ? 367 ILE   A C   1 
ATOM   2410 O  O   . ILE   A 1 339 ? -2.358  9.589   84.104  1.00 37.09 ? 367 ILE   A O   1 
ATOM   2411 C  CB  . ILE   A 1 339 ? -1.553  10.277  81.040  1.00 30.82 ? 367 ILE   A CB  1 
ATOM   2412 C  CG1 . ILE   A 1 339 ? -1.994  10.515  79.585  1.00 26.16 ? 367 ILE   A CG1 1 
ATOM   2413 C  CG2 . ILE   A 1 339 ? -0.103  9.806   81.141  1.00 27.14 ? 367 ILE   A CG2 1 
ATOM   2414 C  CD1 . ILE   A 1 339 ? -1.145  11.514  78.836  1.00 30.52 ? 367 ILE   A CD1 1 
ATOM   2415 N  N   . LEU   A 1 340 ? -1.394  7.756   83.201  1.00 29.84 ? 368 LEU   A N   1 
ATOM   2416 C  CA  . LEU   A 1 340 ? -0.763  7.254   84.415  1.00 30.35 ? 368 LEU   A CA  1 
ATOM   2417 C  C   . LEU   A 1 340 ? 0.713   7.626   84.429  1.00 28.94 ? 368 LEU   A C   1 
ATOM   2418 O  O   . LEU   A 1 340 ? 1.348   7.770   83.377  1.00 26.94 ? 368 LEU   A O   1 
ATOM   2419 C  CB  . LEU   A 1 340 ? -0.886  5.728   84.529  1.00 32.95 ? 368 LEU   A CB  1 
ATOM   2420 C  CG  . LEU   A 1 340 ? -2.242  5.037   84.674  1.00 34.46 ? 368 LEU   A CG  1 
ATOM   2421 C  CD1 . LEU   A 1 340 ? -3.075  5.792   85.682  1.00 40.84 ? 368 LEU   A CD1 1 
ATOM   2422 C  CD2 . LEU   A 1 340 ? -2.974  4.923   83.347  1.00 31.96 ? 368 LEU   A CD2 1 
ATOM   2423 N  N   . VAL   A 1 341 ? 1.259   7.783   85.632  1.00 29.56 ? 369 VAL   A N   1 
ATOM   2424 C  CA  . VAL   A 1 341 ? 2.668   8.118   85.810  1.00 31.34 ? 369 VAL   A CA  1 
ATOM   2425 C  C   . VAL   A 1 341 ? 3.249   7.187   86.860  1.00 32.11 ? 369 VAL   A C   1 
ATOM   2426 O  O   . VAL   A 1 341 ? 2.623   6.936   87.895  1.00 30.79 ? 369 VAL   A O   1 
ATOM   2427 C  CB  . VAL   A 1 341 ? 2.881   9.598   86.222  1.00 35.22 ? 369 VAL   A CB  1 
ATOM   2428 C  CG1 . VAL   A 1 341 ? 4.351   9.988   86.085  1.00 27.24 ? 369 VAL   A CG1 1 
ATOM   2429 C  CG2 . VAL   A 1 341 ? 1.998   10.536  85.399  1.00 30.67 ? 369 VAL   A CG2 1 
ATOM   2430 N  N   . ASP   A 1 342 ? 4.434   6.657   86.581  1.00 29.94 ? 370 ASP   A N   1 
ATOM   2431 C  CA  . ASP   A 1 342 ? 5.196   5.930   87.582  1.00 33.90 ? 370 ASP   A CA  1 
ATOM   2432 C  C   . ASP   A 1 342 ? 6.652   6.335   87.432  1.00 33.20 ? 370 ASP   A C   1 
ATOM   2433 O  O   . ASP   A 1 342 ? 7.041   6.973   86.447  1.00 30.95 ? 370 ASP   A O   1 
ATOM   2434 C  CB  . ASP   A 1 342 ? 5.029   4.410   87.450  1.00 34.01 ? 370 ASP   A CB  1 
ATOM   2435 C  CG  . ASP   A 1 342 ? 5.420   3.666   88.720  1.00 35.02 ? 370 ASP   A CG  1 
ATOM   2436 O  OD1 . ASP   A 1 342 ? 5.534   4.318   89.779  1.00 37.42 ? 370 ASP   A OD1 1 
ATOM   2437 O  OD2 . ASP   A 1 342 ? 5.585   2.429   88.668  1.00 32.43 ? 370 ASP   A OD2 1 
ATOM   2438 N  N   . ARG   A 1 343 ? 7.465   5.938   88.407  1.00 32.22 ? 371 ARG   A N   1 
ATOM   2439 C  CA  . ARG   A 1 343 ? 8.844   6.386   88.446  1.00 34.86 ? 371 ARG   A CA  1 
ATOM   2440 C  C   . ARG   A 1 343 ? 9.757   5.315   89.034  1.00 39.29 ? 371 ARG   A C   1 
ATOM   2441 O  O   . ARG   A 1 343 ? 9.402   4.643   90.005  1.00 41.67 ? 371 ARG   A O   1 
ATOM   2442 C  CB  . ARG   A 1 343 ? 8.940   7.666   89.263  1.00 38.24 ? 371 ARG   A CB  1 
ATOM   2443 C  CG  . ARG   A 1 343 ? 10.290  8.282   89.274  1.00 40.79 ? 371 ARG   A CG  1 
ATOM   2444 C  CD  . ARG   A 1 343 ? 10.243  9.502   90.144  1.00 43.53 ? 371 ARG   A CD  1 
ATOM   2445 N  NE  . ARG   A 1 343 ? 11.433  10.315  89.974  1.00 50.55 ? 371 ARG   A NE  1 
ATOM   2446 C  CZ  . ARG   A 1 343 ? 11.516  11.570  90.382  1.00 51.92 ? 371 ARG   A CZ  1 
ATOM   2447 N  NH1 . ARG   A 1 343 ? 10.468  12.136  90.972  1.00 53.64 ? 371 ARG   A NH1 1 
ATOM   2448 N  NH2 . ARG   A 1 343 ? 12.633  12.255  90.194  1.00 58.08 ? 371 ARG   A NH2 1 
ATOM   2449 N  N   . ASP   A 1 344 ? 10.939  5.184   88.431  1.00 42.86 ? 372 ASP   A N   1 
ATOM   2450 C  CA  . ASP   A 1 344 ? 12.040  4.330   88.859  1.00 44.36 ? 372 ASP   A CA  1 
ATOM   2451 C  C   . ASP   A 1 344 ? 12.932  5.078   89.846  1.00 48.44 ? 372 ASP   A C   1 
ATOM   2452 O  O   . ASP   A 1 344 ? 12.562  6.121   90.387  1.00 43.40 ? 372 ASP   A O   1 
ATOM   2453 C  CB  . ASP   A 1 344 ? 12.895  3.922   87.651  1.00 37.33 ? 372 ASP   A CB  1 
ATOM   2454 C  CG  . ASP   A 1 344 ? 12.796  2.465   87.329  1.00 44.20 ? 372 ASP   A CG  1 
ATOM   2455 O  OD1 . ASP   A 1 344 ? 12.095  1.739   88.059  1.00 51.86 ? 372 ASP   A OD1 1 
ATOM   2456 O  OD2 . ASP   A 1 344 ? 13.420  2.034   86.333  1.00 47.41 ? 372 ASP   A OD2 1 
ATOM   2457 N  N   . ASP   A 1 345 ? 14.132  4.544   90.063  1.00 55.76 ? 373 ASP   A N   1 
ATOM   2458 C  CA  . ASP   A 1 345 ? 15.282  5.298   90.540  1.00 52.63 ? 373 ASP   A CA  1 
ATOM   2459 C  C   . ASP   A 1 345 ? 16.035  5.972   89.401  1.00 54.94 ? 373 ASP   A C   1 
ATOM   2460 O  O   . ASP   A 1 345 ? 16.815  6.899   89.645  1.00 58.19 ? 373 ASP   A O   1 
ATOM   2461 C  CB  . ASP   A 1 345 ? 16.242  4.367   91.295  1.00 54.58 ? 373 ASP   A CB  1 
ATOM   2462 C  CG  . ASP   A 1 345 ? 16.542  3.080   90.528  1.00 58.31 ? 373 ASP   A CG  1 
ATOM   2463 O  OD1 . ASP   A 1 345 ? 15.741  2.708   89.638  1.00 57.50 ? 373 ASP   A OD1 1 
ATOM   2464 O  OD2 . ASP   A 1 345 ? 17.582  2.442   90.812  1.00 64.49 ? 373 ASP   A OD2 1 
ATOM   2465 N  N   . GLN   A 1 346 ? 15.814  5.528   88.165  1.00 51.77 ? 374 GLN   A N   1 
ATOM   2466 C  CA  . GLN   A 1 346 ? 16.542  6.024   87.008  1.00 48.80 ? 374 GLN   A CA  1 
ATOM   2467 C  C   . GLN   A 1 346 ? 15.734  6.982   86.148  1.00 48.62 ? 374 GLN   A C   1 
ATOM   2468 O  O   . GLN   A 1 346 ? 16.326  7.819   85.458  1.00 48.01 ? 374 GLN   A O   1 
ATOM   2469 C  CB  . GLN   A 1 346 ? 17.012  4.846   86.146  1.00 50.16 ? 374 GLN   A CB  1 
ATOM   2470 N  N   . GLY   A 1 347 ? 14.406  6.883   86.167  1.00 44.77 ? 375 GLY   A N   1 
ATOM   2471 C  CA  . GLY   A 1 347 ? 13.611  7.658   85.232  1.00 38.18 ? 375 GLY   A CA  1 
ATOM   2472 C  C   . GLY   A 1 347 ? 12.140  7.658   85.578  1.00 35.60 ? 375 GLY   A C   1 
ATOM   2473 O  O   . GLY   A 1 347 ? 11.696  7.025   86.540  1.00 34.10 ? 375 GLY   A O   1 
ATOM   2474 N  N   . THR   A 1 348 ? 11.384  8.387   84.759  1.00 32.85 ? 376 THR   A N   1 
ATOM   2475 C  CA  . THR   A 1 348 ? 9.944   8.530   84.917  1.00 34.19 ? 376 THR   A CA  1 
ATOM   2476 C  C   . THR   A 1 348 ? 9.245   8.026   83.659  1.00 30.22 ? 376 THR   A C   1 
ATOM   2477 O  O   . THR   A 1 348 ? 9.789   8.084   82.551  1.00 30.15 ? 376 THR   A O   1 
ATOM   2478 C  CB  . THR   A 1 348 ? 9.544   10.008  85.203  1.00 34.71 ? 376 THR   A CB  1 
ATOM   2479 O  OG1 . THR   A 1 348 ? 10.241  10.480  86.361  1.00 39.11 ? 376 THR   A OG1 1 
ATOM   2480 C  CG2 . THR   A 1 348 ? 8.054   10.145  85.457  1.00 31.89 ? 376 THR   A CG2 1 
ATOM   2481 N  N   . LEU   A 1 349 ? 8.018   7.559   83.842  1.00 26.50 ? 377 LEU   A N   1 
ATOM   2482 C  CA  . LEU   A 1 349 ? 7.256   6.909   82.794  1.00 27.45 ? 377 LEU   A CA  1 
ATOM   2483 C  C   . LEU   A 1 349 ? 5.828   7.437   82.788  1.00 25.96 ? 377 LEU   A C   1 
ATOM   2484 O  O   . LEU   A 1 349 ? 5.169   7.466   83.831  1.00 27.94 ? 377 LEU   A O   1 
ATOM   2485 C  CB  . LEU   A 1 349 ? 7.291   5.404   83.046  1.00 27.70 ? 377 LEU   A CB  1 
ATOM   2486 C  CG  . LEU   A 1 349 ? 6.420   4.349   82.427  1.00 31.60 ? 377 LEU   A CG  1 
ATOM   2487 C  CD1 . LEU   A 1 349 ? 7.077   3.072   82.849  1.00 30.83 ? 377 LEU   A CD1 1 
ATOM   2488 C  CD2 . LEU   A 1 349 ? 5.022   4.386   82.965  1.00 31.64 ? 377 LEU   A CD2 1 
ATOM   2489 N  N   . LEU   A 1 350 ? 5.346   7.821   81.613  1.00 25.52 ? 378 LEU   A N   1 
ATOM   2490 C  CA  . LEU   A 1 350 ? 3.932   8.101   81.391  1.00 23.23 ? 378 LEU   A CA  1 
ATOM   2491 C  C   . LEU   A 1 350 ? 3.318   6.936   80.608  1.00 24.09 ? 378 LEU   A C   1 
ATOM   2492 O  O   . LEU   A 1 350 ? 3.894   6.490   79.613  1.00 24.89 ? 378 LEU   A O   1 
ATOM   2493 C  CB  . LEU   A 1 350 ? 3.766   9.419   80.631  1.00 22.46 ? 378 LEU   A CB  1 
ATOM   2494 C  CG  . LEU   A 1 350 ? 4.686   10.592  81.031  1.00 30.18 ? 378 LEU   A CG  1 
ATOM   2495 C  CD1 . LEU   A 1 350 ? 4.368   11.877  80.268  1.00 29.56 ? 378 LEU   A CD1 1 
ATOM   2496 C  CD2 . LEU   A 1 350 ? 4.610   10.864  82.522  1.00 34.02 ? 378 LEU   A CD2 1 
ATOM   2497 N  N   . GLN   A 1 351 ? 2.154   6.446   81.041  1.00 22.54 ? 379 GLN   A N   1 
ATOM   2498 C  CA  . GLN   A 1 351 ? 1.526   5.325   80.347  1.00 23.79 ? 379 GLN   A CA  1 
ATOM   2499 C  C   . GLN   A 1 351 ? 0.005   5.443   80.385  1.00 25.52 ? 379 GLN   A C   1 
ATOM   2500 O  O   . GLN   A 1 351 ? -0.572  6.057   81.283  1.00 23.50 ? 379 GLN   A O   1 
ATOM   2501 C  CB  . GLN   A 1 351 ? 1.948   3.980   80.960  1.00 23.40 ? 379 GLN   A CB  1 
ATOM   2502 C  CG  . GLN   A 1 351 ? 1.616   3.878   82.439  1.00 25.04 ? 379 GLN   A CG  1 
ATOM   2503 C  CD  . GLN   A 1 351 ? 2.103   2.597   83.086  1.00 26.86 ? 379 GLN   A CD  1 
ATOM   2504 O  OE1 . GLN   A 1 351 ? 2.018   2.437   84.303  1.00 26.20 ? 379 GLN   A OE1 1 
ATOM   2505 N  NE2 . GLN   A 1 351 ? 2.600   1.672   82.275  1.00 24.09 ? 379 GLN   A NE2 1 
ATOM   2506 N  N   . ILE   A 1 352 ? -0.644  4.806   79.407  1.00 20.56 ? 380 ILE   A N   1 
ATOM   2507 C  CA  . ILE   A 1 352 ? -2.090  4.635   79.414  1.00 20.36 ? 380 ILE   A CA  1 
ATOM   2508 C  C   . ILE   A 1 352 ? -2.415  3.370   78.625  1.00 20.94 ? 380 ILE   A C   1 
ATOM   2509 O  O   . ILE   A 1 352 ? -1.632  2.925   77.785  1.00 22.82 ? 380 ILE   A O   1 
ATOM   2510 C  CB  . ILE   A 1 352 ? -2.818  5.868   78.829  1.00 20.80 ? 380 ILE   A CB  1 
ATOM   2511 C  CG1 . ILE   A 1 352 ? -4.328  5.789   79.098  1.00 19.50 ? 380 ILE   A CG1 1 
ATOM   2512 C  CG2 . ILE   A 1 352 ? -2.496  6.036   77.335  1.00 15.91 ? 380 ILE   A CG2 1 
ATOM   2513 C  CD1 . ILE   A 1 352 ? -5.083  7.094   78.792  1.00 19.44 ? 380 ILE   A CD1 1 
ATOM   2514 N  N   . PHE   A 1 353 ? -3.585  2.791   78.897  1.00 19.25 ? 381 PHE   A N   1 
ATOM   2515 C  CA  . PHE   A 1 353 ? -3.989  1.505   78.347  1.00 19.76 ? 381 PHE   A CA  1 
ATOM   2516 C  C   . PHE   A 1 353 ? -5.302  1.604   77.589  1.00 19.77 ? 381 PHE   A C   1 
ATOM   2517 O  O   . PHE   A 1 353 ? -6.275  2.187   78.078  1.00 23.01 ? 381 PHE   A O   1 
ATOM   2518 C  CB  . PHE   A 1 353 ? -4.123  0.476   79.469  1.00 21.94 ? 381 PHE   A CB  1 
ATOM   2519 C  CG  . PHE   A 1 353 ? -2.878  0.317   80.257  1.00 23.74 ? 381 PHE   A CG  1 
ATOM   2520 C  CD1 . PHE   A 1 353 ? -2.715  0.993   81.452  1.00 25.57 ? 381 PHE   A CD1 1 
ATOM   2521 C  CD2 . PHE   A 1 353 ? -1.841  -0.471  79.781  1.00 23.65 ? 381 PHE   A CD2 1 
ATOM   2522 C  CE1 . PHE   A 1 353 ? -1.547  0.874   82.171  1.00 23.15 ? 381 PHE   A CE1 1 
ATOM   2523 C  CE2 . PHE   A 1 353 ? -0.677  -0.596  80.497  1.00 23.83 ? 381 PHE   A CE2 1 
ATOM   2524 C  CZ  . PHE   A 1 353 ? -0.531  0.087   81.691  1.00 25.70 ? 381 PHE   A CZ  1 
ATOM   2525 N  N   . THR   A 1 354 ? -5.336  1.007   76.404  1.00 18.04 ? 382 THR   A N   1 
ATOM   2526 C  CA  . THR   A 1 354 ? -6.593  0.885   75.683  1.00 17.83 ? 382 THR   A CA  1 
ATOM   2527 C  C   . THR   A 1 354 ? -7.431  -0.255  76.250  1.00 20.31 ? 382 THR   A C   1 
ATOM   2528 O  O   . THR   A 1 354 ? -6.931  -1.158  76.935  1.00 17.62 ? 382 THR   A O   1 
ATOM   2529 C  CB  . THR   A 1 354 ? -6.359  0.618   74.193  1.00 17.28 ? 382 THR   A CB  1 
ATOM   2530 O  OG1 . THR   A 1 354 ? -5.977  -0.756  74.023  1.00 16.42 ? 382 THR   A OG1 1 
ATOM   2531 C  CG2 . THR   A 1 354 ? -5.273  1.545   73.634  1.00 16.00 ? 382 THR   A CG2 1 
ATOM   2532 N  N   . LYS   A 1 355 ? -8.726  -0.206  75.944  1.00 18.29 ? 383 LYS   A N   1 
ATOM   2533 C  CA  . LYS   A 1 355 ? -9.576  -1.379  76.095  1.00 18.90 ? 383 LYS   A CA  1 
ATOM   2534 C  C   . LYS   A 1 355 ? -9.120  -2.458  75.116  1.00 16.42 ? 383 LYS   A C   1 
ATOM   2535 O  O   . LYS   A 1 355 ? -8.341  -2.167  74.199  1.00 18.60 ? 383 LYS   A O   1 
ATOM   2536 C  CB  . LYS   A 1 355 ? -11.043 -1.010  75.868  1.00 18.92 ? 383 LYS   A CB  1 
ATOM   2537 C  CG  . LYS   A 1 355 ? -11.605 -0.147  76.997  1.00 25.10 ? 383 LYS   A CG  1 
ATOM   2538 C  CD  . LYS   A 1 355 ? -13.120 -0.180  77.033  1.00 26.99 ? 383 LYS   A CD  1 
ATOM   2539 C  CE  . LYS   A 1 355 ? -13.674 0.779   78.081  1.00 33.57 ? 383 LYS   A CE  1 
ATOM   2540 N  NZ  . LYS   A 1 355 ? -15.162 0.946   77.942  1.00 37.23 ? 383 LYS   A NZ  1 
ATOM   2541 N  N   . PRO   A 1 356 ? -9.565  -3.704  75.273  1.00 18.18 ? 384 PRO   A N   1 
ATOM   2542 C  CA  . PRO   A 1 356 ? -9.168  -4.753  74.325  1.00 20.80 ? 384 PRO   A CA  1 
ATOM   2543 C  C   . PRO   A 1 356 ? -9.362  -4.333  72.872  1.00 17.47 ? 384 PRO   A C   1 
ATOM   2544 O  O   . PRO   A 1 356 ? -10.304 -3.610  72.530  1.00 18.99 ? 384 PRO   A O   1 
ATOM   2545 C  CB  . PRO   A 1 356 ? -10.073 -5.922  74.710  1.00 19.37 ? 384 PRO   A CB  1 
ATOM   2546 C  CG  . PRO   A 1 356 ? -10.254 -5.727  76.170  1.00 20.77 ? 384 PRO   A CG  1 
ATOM   2547 C  CD  . PRO   A 1 356 ? -10.368 -4.253  76.377  1.00 17.08 ? 384 PRO   A CD  1 
ATOM   2548 N  N   . LEU   A 1 357 ? -8.440  -4.782  72.014  1.00 15.14 ? 385 LEU   A N   1 
ATOM   2549 C  CA  . LEU   A 1 357 ? -8.441  -4.343  70.625  1.00 17.79 ? 385 LEU   A CA  1 
ATOM   2550 C  C   . LEU   A 1 357 ? -9.558  -4.974  69.812  1.00 14.50 ? 385 LEU   A C   1 
ATOM   2551 O  O   . LEU   A 1 357 ? -9.924  -4.431  68.769  1.00 17.39 ? 385 LEU   A O   1 
ATOM   2552 C  CB  . LEU   A 1 357 ? -7.095  -4.660  69.971  1.00 15.39 ? 385 LEU   A CB  1 
ATOM   2553 C  CG  . LEU   A 1 357 ? -5.837  -4.307  70.766  1.00 14.89 ? 385 LEU   A CG  1 
ATOM   2554 C  CD1 . LEU   A 1 357 ? -4.566  -4.605  69.937  1.00 12.74 ? 385 LEU   A CD1 1 
ATOM   2555 C  CD2 . LEU   A 1 357 ? -5.871  -2.834  71.171  1.00 15.17 ? 385 LEU   A CD2 1 
ATOM   2556 N  N   . GLY   A 1 358 ? -10.077 -6.118  70.238  1.00 15.84 ? 386 GLY   A N   1 
ATOM   2557 C  CA  . GLY   A 1 358 ? -11.073 -6.848  69.482  1.00 16.47 ? 386 GLY   A CA  1 
ATOM   2558 C  C   . GLY   A 1 358 ? -12.180 -7.367  70.376  1.00 14.60 ? 386 GLY   A C   1 
ATOM   2559 O  O   . GLY   A 1 358 ? -12.332 -6.883  71.498  1.00 17.03 ? 386 GLY   A O   1 
ATOM   2560 N  N   . ASP   A 1 359 ? -12.932 -8.362  69.894  1.00 17.24 ? 387 ASP   A N   1 
ATOM   2561 C  CA  . ASP   A 1 359 ? -14.082 -8.899  70.629  1.00 17.95 ? 387 ASP   A CA  1 
ATOM   2562 C  C   . ASP   A 1 359 ? -13.698 -9.437  72.005  1.00 17.08 ? 387 ASP   A C   1 
ATOM   2563 O  O   . ASP   A 1 359 ? -14.476 -9.326  72.959  1.00 14.90 ? 387 ASP   A O   1 
ATOM   2564 C  CB  . ASP   A 1 359 ? -14.746 -10.029 69.834  1.00 16.28 ? 387 ASP   A CB  1 
ATOM   2565 C  CG  . ASP   A 1 359 ? -15.418 -9.560  68.577  1.00 15.50 ? 387 ASP   A CG  1 
ATOM   2566 O  OD1 . ASP   A 1 359 ? -15.832 -8.385  68.492  1.00 15.38 ? 387 ASP   A OD1 1 
ATOM   2567 O  OD2 . ASP   A 1 359 ? -15.539 -10.394 67.659  1.00 15.49 ? 387 ASP   A OD2 1 
ATOM   2568 N  N   . ARG   A 1 360 ? -12.495 -10.089 72.123  1.00 17.56 ? 388 ARG   A N   1 
ATOM   2569 C  CA  . ARG   A 1 360 ? -12.284 -10.778 73.388  1.00 17.95 ? 388 ARG   A CA  1 
ATOM   2570 C  C   . ARG   A 1 360 ? -11.482 -9.920  74.351  1.00 16.92 ? 388 ARG   A C   1 
ATOM   2571 O  O   . ARG   A 1 360 ? -10.667 -9.102  73.925  1.00 17.88 ? 388 ARG   A O   1 
ATOM   2572 C  CB  . ARG   A 1 360 ? -11.543 -12.099 73.177  1.00 16.46 ? 388 ARG   A CB  1 
ATOM   2573 C  CG  . ARG   A 1 360 ? -11.991 -12.919 72.000  1.00 16.92 ? 388 ARG   A CG  1 
ATOM   2574 C  CD  . ARG   A 1 360 ? -11.336 -14.305 72.028  1.00 18.93 ? 388 ARG   A CD  1 
ATOM   2575 N  NE  . ARG   A 1 360 ? -11.878 -15.142 70.966  1.00 19.07 ? 388 ARG   A NE  1 
ATOM   2576 C  CZ  . ARG   A 1 360 ? -11.576 -16.419 70.783  1.00 19.12 ? 388 ARG   A CZ  1 
ATOM   2577 N  NH1 . ARG   A 1 360 ? -12.110 -17.076 69.764  1.00 19.88 ? 388 ARG   A NH1 1 
ATOM   2578 N  NH2 . ARG   A 1 360 ? -10.737 -17.034 71.614  1.00 17.84 ? 388 ARG   A NH2 1 
ATOM   2579 N  N   . PRO   A 1 361 ? -11.691 -10.124 75.659  1.00 18.27 ? 389 PRO   A N   1 
ATOM   2580 C  CA  . PRO   A 1 361 ? -10.917 -9.377  76.664  1.00 20.70 ? 389 PRO   A CA  1 
ATOM   2581 C  C   . PRO   A 1 361 ? -9.503  -9.927  76.808  1.00 21.14 ? 389 PRO   A C   1 
ATOM   2582 O  O   . PRO   A 1 361 ? -9.098  -10.410 77.868  1.00 21.55 ? 389 PRO   A O   1 
ATOM   2583 C  CB  . PRO   A 1 361 ? -11.738 -9.573  77.943  1.00 20.52 ? 389 PRO   A CB  1 
ATOM   2584 C  CG  . PRO   A 1 361 ? -12.333 -10.982 77.749  1.00 17.58 ? 389 PRO   A CG  1 
ATOM   2585 C  CD  . PRO   A 1 361 ? -12.655 -11.064 76.276  1.00 17.62 ? 389 PRO   A CD  1 
ATOM   2586 N  N   . THR   A 1 362 ? -8.739  -9.858  75.727  1.00 20.14 ? 390 THR   A N   1 
ATOM   2587 C  CA  . THR   A 1 362 ? -7.416  -10.456 75.688  1.00 19.47 ? 390 THR   A CA  1 
ATOM   2588 C  C   . THR   A 1 362 ? -6.343  -9.401  75.407  1.00 16.77 ? 390 THR   A C   1 
ATOM   2589 O  O   . THR   A 1 362 ? -5.826  -8.778  76.336  1.00 17.41 ? 390 THR   A O   1 
ATOM   2590 C  CB  . THR   A 1 362 ? -7.383  -11.565 74.638  1.00 16.17 ? 390 THR   A CB  1 
ATOM   2591 O  OG1 . THR   A 1 362 ? -7.936  -11.067 73.412  1.00 15.66 ? 390 THR   A OG1 1 
ATOM   2592 C  CG2 . THR   A 1 362 ? -8.181  -12.769 75.119  1.00 16.89 ? 390 THR   A CG2 1 
ATOM   2593 N  N   . ILE   A 1 363 ? -6.000  -9.192  74.150  1.00 14.23 ? 391 ILE   A N   1 
ATOM   2594 C  CA  . ILE   A 1 363 ? -4.909  -8.282  73.810  1.00 18.32 ? 391 ILE   A CA  1 
ATOM   2595 C  C   . ILE   A 1 363 ? -5.380  -6.834  73.914  1.00 15.07 ? 391 ILE   A C   1 
ATOM   2596 O  O   . ILE   A 1 363 ? -6.505  -6.502  73.526  1.00 14.92 ? 391 ILE   A O   1 
ATOM   2597 C  CB  . ILE   A 1 363 ? -4.355  -8.601  72.403  1.00 14.87 ? 391 ILE   A CB  1 
ATOM   2598 C  CG1 . ILE   A 1 363 ? -3.183  -7.667  72.071  1.00 18.16 ? 391 ILE   A CG1 1 
ATOM   2599 C  CG2 . ILE   A 1 363 ? -5.465  -8.540  71.330  1.00 13.42 ? 391 ILE   A CG2 1 
ATOM   2600 C  CD1 . ILE   A 1 363 ? -2.438  -8.031  70.798  1.00 15.19 ? 391 ILE   A CD1 1 
ATOM   2601 N  N   . PHE   A 1 364 ? -4.517  -5.968  74.447  1.00 16.80 ? 392 PHE   A N   1 
ATOM   2602 C  CA  . PHE   A 1 364 ? -4.735  -4.517  74.448  1.00 17.20 ? 392 PHE   A CA  1 
ATOM   2603 C  C   . PHE   A 1 364 ? -3.414  -3.830  74.126  1.00 17.64 ? 392 PHE   A C   1 
ATOM   2604 O  O   . PHE   A 1 364 ? -2.376  -4.477  73.972  1.00 19.96 ? 392 PHE   A O   1 
ATOM   2605 C  CB  . PHE   A 1 364 ? -5.297  -4.004  75.787  1.00 16.49 ? 392 PHE   A CB  1 
ATOM   2606 C  CG  . PHE   A 1 364 ? -4.474  -4.397  77.001  1.00 18.36 ? 392 PHE   A CG  1 
ATOM   2607 C  CD1 . PHE   A 1 364 ? -4.665  -5.629  77.620  1.00 18.81 ? 392 PHE   A CD1 1 
ATOM   2608 C  CD2 . PHE   A 1 364 ? -3.532  -3.530  77.532  1.00 18.43 ? 392 PHE   A CD2 1 
ATOM   2609 C  CE1 . PHE   A 1 364 ? -3.918  -5.983  78.737  1.00 21.12 ? 392 PHE   A CE1 1 
ATOM   2610 C  CE2 . PHE   A 1 364 ? -2.779  -3.884  78.648  1.00 20.76 ? 392 PHE   A CE2 1 
ATOM   2611 C  CZ  . PHE   A 1 364 ? -2.972  -5.105  79.252  1.00 16.45 ? 392 PHE   A CZ  1 
ATOM   2612 N  N   . ILE   A 1 365 ? -3.456  -2.508  74.034  1.00 17.92 ? 393 ILE   A N   1 
ATOM   2613 C  CA  . ILE   A 1 365 ? -2.306  -1.691  73.682  1.00 16.83 ? 393 ILE   A CA  1 
ATOM   2614 C  C   . ILE   A 1 365 ? -2.042  -0.714  74.824  1.00 17.51 ? 393 ILE   A C   1 
ATOM   2615 O  O   . ILE   A 1 365 ? -2.958  -0.291  75.542  1.00 20.13 ? 393 ILE   A O   1 
ATOM   2616 C  CB  . ILE   A 1 365 ? -2.551  -0.975  72.321  1.00 16.84 ? 393 ILE   A CB  1 
ATOM   2617 C  CG1 . ILE   A 1 365 ? -2.169  -1.914  71.163  1.00 13.37 ? 393 ILE   A CG1 1 
ATOM   2618 C  CG2 . ILE   A 1 365 ? -1.783  0.333   72.200  1.00 14.10 ? 393 ILE   A CG2 1 
ATOM   2619 C  CD1 . ILE   A 1 365 ? -2.448  -1.370  69.786  1.00 10.39 ? 393 ILE   A CD1 1 
ATOM   2620 N  N   . GLU   A 1 366 ? -0.766  -0.411  75.030  1.00 18.27 ? 394 GLU   A N   1 
ATOM   2621 C  CA  . GLU   A 1 366 ? -0.305  0.603   75.970  1.00 18.40 ? 394 GLU   A CA  1 
ATOM   2622 C  C   . GLU   A 1 366 ? 0.436   1.683   75.193  1.00 19.70 ? 394 GLU   A C   1 
ATOM   2623 O  O   . GLU   A 1 366 ? 1.219   1.373   74.283  1.00 19.81 ? 394 GLU   A O   1 
ATOM   2624 C  CB  . GLU   A 1 366 ? 0.616   -0.024  77.034  1.00 19.42 ? 394 GLU   A CB  1 
ATOM   2625 C  CG  . GLU   A 1 366 ? 1.280   0.933   78.006  1.00 21.94 ? 394 GLU   A CG  1 
ATOM   2626 C  CD  . GLU   A 1 366 ? 2.313   0.223   78.873  1.00 20.93 ? 394 GLU   A CD  1 
ATOM   2627 O  OE1 . GLU   A 1 366 ? 2.422   -1.007  78.758  1.00 20.87 ? 394 GLU   A OE1 1 
ATOM   2628 O  OE2 . GLU   A 1 366 ? 3.002   0.875   79.677  1.00 22.90 ? 394 GLU   A OE2 1 
ATOM   2629 N  N   . ILE   A 1 367 ? 0.168   2.948   75.512  1.00 18.38 ? 395 ILE   A N   1 
ATOM   2630 C  CA  . ILE   A 1 367 ? 0.961   4.062   74.992  1.00 19.32 ? 395 ILE   A CA  1 
ATOM   2631 C  C   . ILE   A 1 367 ? 1.885   4.535   76.105  1.00 21.66 ? 395 ILE   A C   1 
ATOM   2632 O  O   . ILE   A 1 367 ? 1.457   4.684   77.257  1.00 26.03 ? 395 ILE   A O   1 
ATOM   2633 C  CB  . ILE   A 1 367 ? 0.079   5.218   74.484  1.00 20.06 ? 395 ILE   A CB  1 
ATOM   2634 C  CG1 . ILE   A 1 367 ? -1.070  4.691   73.598  1.00 20.33 ? 395 ILE   A CG1 1 
ATOM   2635 C  CG2 . ILE   A 1 367 ? 0.959   6.297   73.788  1.00 15.21 ? 395 ILE   A CG2 1 
ATOM   2636 C  CD1 . ILE   A 1 367 ? -0.647  3.965   72.316  1.00 14.95 ? 395 ILE   A CD1 1 
ATOM   2637 N  N   . ILE   A 1 368 ? 3.153   4.758   75.778  1.00 21.99 ? 396 ILE   A N   1 
ATOM   2638 C  CA  . ILE   A 1 368 ? 4.152   5.015   76.806  1.00 22.29 ? 396 ILE   A CA  1 
ATOM   2639 C  C   . ILE   A 1 368 ? 5.118   6.087   76.317  1.00 23.08 ? 396 ILE   A C   1 
ATOM   2640 O  O   . ILE   A 1 368 ? 5.343   6.258   75.112  1.00 20.85 ? 396 ILE   A O   1 
ATOM   2641 C  CB  . ILE   A 1 368 ? 4.908   3.718   77.200  1.00 23.03 ? 396 ILE   A CB  1 
ATOM   2642 C  CG1 . ILE   A 1 368 ? 5.535   3.849   78.586  1.00 28.32 ? 396 ILE   A CG1 1 
ATOM   2643 C  CG2 . ILE   A 1 368 ? 5.994   3.361   76.189  1.00 21.40 ? 396 ILE   A CG2 1 
ATOM   2644 C  CD1 . ILE   A 1 368 ? 6.392   2.640   78.977  1.00 26.74 ? 396 ILE   A CD1 1 
ATOM   2645 N  N   . GLN   A 1 369 ? 5.675   6.828   77.271  1.00 24.27 ? 397 GLN   A N   1 
ATOM   2646 C  CA  . GLN   A 1 369 ? 6.754   7.758   76.984  1.00 21.28 ? 397 GLN   A CA  1 
ATOM   2647 C  C   . GLN   A 1 369 ? 7.644   7.829   78.207  1.00 23.15 ? 397 GLN   A C   1 
ATOM   2648 O  O   . GLN   A 1 369 ? 7.158   7.911   79.339  1.00 26.25 ? 397 GLN   A O   1 
ATOM   2649 C  CB  . GLN   A 1 369 ? 6.261   9.165   76.611  1.00 22.63 ? 397 GLN   A CB  1 
ATOM   2650 C  CG  . GLN   A 1 369 ? 7.413   10.063  76.131  1.00 24.38 ? 397 GLN   A CG  1 
ATOM   2651 C  CD  . GLN   A 1 369 ? 6.961   11.327  75.390  1.00 26.01 ? 397 GLN   A CD  1 
ATOM   2652 O  OE1 . GLN   A 1 369 ? 5.833   11.797  75.549  1.00 23.64 ? 397 GLN   A OE1 1 
ATOM   2653 N  NE2 . GLN   A 1 369 ? 7.856   11.880  74.578  1.00 24.47 ? 397 GLN   A NE2 1 
ATOM   2654 N  N   . ARG   A 1 370 ? 8.943   7.785   77.969  1.00 21.18 ? 398 ARG   A N   1 
ATOM   2655 C  CA  . ARG   A 1 370 ? 9.924   7.708   79.030  1.00 28.51 ? 398 ARG   A CA  1 
ATOM   2656 C  C   . ARG   A 1 370 ? 10.710  9.009   79.091  1.00 24.17 ? 398 ARG   A C   1 
ATOM   2657 O  O   . ARG   A 1 370 ? 11.090  9.563   78.058  1.00 25.39 ? 398 ARG   A O   1 
ATOM   2658 C  CB  . ARG   A 1 370 ? 10.854  6.516   78.793  1.00 27.91 ? 398 ARG   A CB  1 
ATOM   2659 C  CG  . ARG   A 1 370 ? 10.106  5.179   78.662  1.00 25.02 ? 398 ARG   A CG  1 
ATOM   2660 C  CD  . ARG   A 1 370 ? 11.083  4.014   78.551  1.00 22.49 ? 398 ARG   A CD  1 
ATOM   2661 N  NE  . ARG   A 1 370 ? 10.412  2.730   78.498  1.00 21.81 ? 398 ARG   A NE  1 
ATOM   2662 C  CZ  . ARG   A 1 370 ? 10.049  2.023   79.563  1.00 24.13 ? 398 ARG   A CZ  1 
ATOM   2663 N  NH1 . ARG   A 1 370 ? 10.304  2.467   80.784  1.00 23.05 ? 398 ARG   A NH1 1 
ATOM   2664 N  NH2 . ARG   A 1 370 ? 9.435   0.858   79.402  1.00 22.33 ? 398 ARG   A NH2 1 
ATOM   2665 N  N   . VAL   A 1 371 ? 10.931  9.508   80.301  1.00 30.20 ? 399 VAL   A N   1 
ATOM   2666 C  CA  . VAL   A 1 371 ? 11.813  10.651  80.522  1.00 33.87 ? 399 VAL   A CA  1 
ATOM   2667 C  C   . VAL   A 1 371 ? 12.895  10.245  81.525  1.00 34.05 ? 399 VAL   A C   1 
ATOM   2668 O  O   . VAL   A 1 371 ? 12.590  9.745   82.619  1.00 37.18 ? 399 VAL   A O   1 
ATOM   2669 C  CB  . VAL   A 1 371 ? 11.032  11.903  80.972  1.00 33.94 ? 399 VAL   A CB  1 
ATOM   2670 C  CG1 . VAL   A 1 371 ? 10.103  11.599  82.109  1.00 34.02 ? 399 VAL   A CG1 1 
ATOM   2671 C  CG2 . VAL   A 1 371 ? 11.994  13.032  81.355  1.00 37.49 ? 399 VAL   A CG2 1 
ATOM   2672 N  N   . GLY   A 1 372 ? 14.162  10.419  81.126  1.00 37.02 ? 400 GLY   A N   1 
ATOM   2673 C  CA  . GLY   A 1 372 ? 15.355  10.157  81.911  1.00 40.05 ? 400 GLY   A CA  1 
ATOM   2674 C  C   . GLY   A 1 372 ? 16.347  9.280   81.159  1.00 45.25 ? 400 GLY   A C   1 
ATOM   2675 O  O   . GLY   A 1 372 ? 16.231  9.052   79.947  1.00 42.04 ? 400 GLY   A O   1 
ATOM   2676 N  N   . CYS   A 1 373 ? 17.346  8.788   81.899  1.00 43.99 ? 401 CYS   A N   1 
ATOM   2677 C  CA  . CYS   A 1 373 ? 18.299  7.782   81.415  1.00 46.28 ? 401 CYS   A CA  1 
ATOM   2678 C  C   . CYS   A 1 373 ? 18.958  8.185   80.098  1.00 50.48 ? 401 CYS   A C   1 
ATOM   2679 O  O   . CYS   A 1 373 ? 19.106  7.378   79.176  1.00 48.45 ? 401 CYS   A O   1 
ATOM   2680 C  CB  . CYS   A 1 373 ? 17.627  6.415   81.269  1.00 41.89 ? 401 CYS   A CB  1 
ATOM   2681 S  SG  . CYS   A 1 373 ? 16.528  5.955   82.620  1.00 37.19 ? 401 CYS   A SG  1 
ATOM   2682 N  N   . MET   A 1 374 ? 19.365  9.450   80.009  1.00 53.64 ? 402 MET   A N   1 
ATOM   2683 C  CA  . MET   A 1 374 ? 20.077  9.915   78.828  1.00 53.19 ? 402 MET   A CA  1 
ATOM   2684 C  C   . MET   A 1 374 ? 21.559  9.563   78.937  1.00 55.81 ? 402 MET   A C   1 
ATOM   2685 O  O   . MET   A 1 374 ? 22.171  9.727   79.998  1.00 55.27 ? 402 MET   A O   1 
ATOM   2686 C  CB  . MET   A 1 374 ? 19.886  11.419  78.646  1.00 52.61 ? 402 MET   A CB  1 
ATOM   2687 C  CG  . MET   A 1 374 ? 18.436  11.827  78.402  1.00 50.82 ? 402 MET   A CG  1 
ATOM   2688 S  SD  . MET   A 1 374 ? 17.689  10.928  77.023  1.00 55.12 ? 402 MET   A SD  1 
ATOM   2689 C  CE  . MET   A 1 374 ? 18.809  11.330  75.681  1.00 47.93 ? 402 MET   A CE  1 
ATOM   2690 N  N   . MET   A 1 375 ? 22.121  9.048   77.848  1.00 55.13 ? 403 MET   A N   1 
ATOM   2691 C  CA  . MET   A 1 375 ? 23.543  8.731   77.779  1.00 61.29 ? 403 MET   A CA  1 
ATOM   2692 C  C   . MET   A 1 375 ? 24.149  9.460   76.589  1.00 62.07 ? 403 MET   A C   1 
ATOM   2693 O  O   . MET   A 1 375 ? 23.436  9.821   75.651  1.00 61.05 ? 403 MET   A O   1 
ATOM   2694 C  CB  . MET   A 1 375 ? 23.781  7.219   77.648  1.00 62.25 ? 403 MET   A CB  1 
ATOM   2695 C  CG  . MET   A 1 375 ? 22.823  6.324   78.430  1.00 57.06 ? 403 MET   A CG  1 
ATOM   2696 S  SD  . MET   A 1 375 ? 23.163  6.223   80.204  1.00 73.79 ? 403 MET   A SD  1 
ATOM   2697 C  CE  . MET   A 1 375 ? 24.786  5.461   80.218  1.00 63.58 ? 403 MET   A CE  1 
ATOM   2698 N  N   . TYR   A 1 383 ? 21.159  9.245   73.353  1.00 57.95 ? 411 TYR   A N   1 
ATOM   2699 C  CA  . TYR   A 1 383 ? 20.133  8.209   73.267  1.00 52.22 ? 411 TYR   A CA  1 
ATOM   2700 C  C   . TYR   A 1 383 ? 19.550  7.914   74.650  1.00 55.39 ? 411 TYR   A C   1 
ATOM   2701 O  O   . TYR   A 1 383 ? 20.141  8.283   75.668  1.00 55.58 ? 411 TYR   A O   1 
ATOM   2702 C  CB  . TYR   A 1 383 ? 20.713  6.932   72.649  1.00 56.72 ? 411 TYR   A CB  1 
ATOM   2703 C  CG  . TYR   A 1 383 ? 21.684  6.208   73.554  1.00 60.91 ? 411 TYR   A CG  1 
ATOM   2704 C  CD1 . TYR   A 1 383 ? 21.259  5.160   74.370  1.00 55.60 ? 411 TYR   A CD1 1 
ATOM   2705 C  CD2 . TYR   A 1 383 ? 23.024  6.585   73.611  1.00 60.03 ? 411 TYR   A CD2 1 
ATOM   2706 C  CE1 . TYR   A 1 383 ? 22.144  4.501   75.207  1.00 58.92 ? 411 TYR   A CE1 1 
ATOM   2707 C  CE2 . TYR   A 1 383 ? 23.916  5.929   74.442  1.00 61.97 ? 411 TYR   A CE2 1 
ATOM   2708 C  CZ  . TYR   A 1 383 ? 23.471  4.886   75.238  1.00 62.18 ? 411 TYR   A CZ  1 
ATOM   2709 O  OH  . TYR   A 1 383 ? 24.351  4.228   76.074  1.00 67.65 ? 411 TYR   A OH  1 
ATOM   2710 N  N   . GLN   A 1 384 ? 18.391  7.253   74.683  1.00 55.31 ? 412 GLN   A N   1 
ATOM   2711 C  CA  . GLN   A 1 384 ? 17.767  6.828   75.929  1.00 48.53 ? 412 GLN   A CA  1 
ATOM   2712 C  C   . GLN   A 1 384 ? 17.957  5.329   76.120  1.00 47.55 ? 412 GLN   A C   1 
ATOM   2713 O  O   . GLN   A 1 384 ? 17.772  4.546   75.183  1.00 50.93 ? 412 GLN   A O   1 
ATOM   2714 C  CB  . GLN   A 1 384 ? 16.275  7.160   75.946  1.00 41.43 ? 412 GLN   A CB  1 
ATOM   2715 C  CG  . GLN   A 1 384 ? 15.666  7.089   77.331  1.00 41.41 ? 412 GLN   A CG  1 
ATOM   2716 C  CD  . GLN   A 1 384 ? 14.199  7.477   77.347  1.00 42.51 ? 412 GLN   A CD  1 
ATOM   2717 O  OE1 . GLN   A 1 384 ? 13.378  6.895   76.628  1.00 39.00 ? 412 GLN   A OE1 1 
ATOM   2718 N  NE2 . GLN   A 1 384 ? 13.862  8.490   78.154  1.00 35.89 ? 412 GLN   A NE2 1 
ATOM   2719 N  N   . SER   A 1 385 ? 18.319  4.929   77.336  1.00 42.83 ? 413 SER   A N   1 
ATOM   2720 C  CA  . SER   A 1 385 ? 18.477  3.508   77.610  1.00 43.65 ? 413 SER   A CA  1 
ATOM   2721 C  C   . SER   A 1 385 ? 17.109  2.863   77.803  1.00 37.04 ? 413 SER   A C   1 
ATOM   2722 O  O   . SER   A 1 385 ? 16.149  3.505   78.243  1.00 35.73 ? 413 SER   A O   1 
ATOM   2723 C  CB  . SER   A 1 385 ? 19.376  3.268   78.834  1.00 45.17 ? 413 SER   A CB  1 
ATOM   2724 O  OG  . SER   A 1 385 ? 18.843  3.816   80.026  1.00 47.94 ? 413 SER   A OG  1 
ATOM   2725 N  N   . GLY   A 1 386 ? 17.029  1.577   77.463  1.00 35.26 ? 414 GLY   A N   1 
ATOM   2726 C  CA  . GLY   A 1 386 ? 15.751  0.899   77.412  1.00 29.31 ? 414 GLY   A CA  1 
ATOM   2727 C  C   . GLY   A 1 386 ? 15.187  0.592   78.787  1.00 31.94 ? 414 GLY   A C   1 
ATOM   2728 O  O   . GLY   A 1 386 ? 15.909  0.339   79.750  1.00 29.24 ? 414 GLY   A O   1 
ATOM   2729 N  N   . GLY   A 1 387 ? 13.859  0.602   78.863  1.00 29.70 ? 415 GLY   A N   1 
ATOM   2730 C  CA  . GLY   A 1 387 ? 13.191  0.389   80.124  1.00 30.37 ? 415 GLY   A CA  1 
ATOM   2731 C  C   . GLY   A 1 387 ? 13.244  1.553   81.085  1.00 26.56 ? 415 GLY   A C   1 
ATOM   2732 O  O   . GLY   A 1 387 ? 12.827  1.399   82.237  1.00 27.78 ? 415 GLY   A O   1 
ATOM   2733 N  N   . CYS   A 1 388 ? 13.721  2.715   80.648  1.00 27.63 ? 416 CYS   A N   1 
ATOM   2734 C  CA  . CYS   A 1 388 ? 13.871  3.863   81.540  1.00 27.52 ? 416 CYS   A CA  1 
ATOM   2735 C  C   . CYS   A 1 388 ? 12.593  4.207   82.289  1.00 27.23 ? 416 CYS   A C   1 
ATOM   2736 O  O   . CYS   A 1 388 ? 11.620  4.673   81.693  1.00 31.74 ? 416 CYS   A O   1 
ATOM   2737 C  CB  . CYS   A 1 388 ? 14.328  5.099   80.769  1.00 31.37 ? 416 CYS   A CB  1 
ATOM   2738 S  SG  . CYS   A 1 388 ? 14.714  6.483   81.889  1.00 38.16 ? 416 CYS   A SG  1 
ATOM   2739 N  N   . GLY   A 1 389 ? 12.592  4.014   83.600  1.00 31.76 ? 417 GLY   A N   1 
ATOM   2740 C  CA  . GLY   A 1 389 ? 11.422  4.281   84.403  1.00 31.15 ? 417 GLY   A CA  1 
ATOM   2741 C  C   . GLY   A 1 389 ? 10.631  3.050   84.759  1.00 30.49 ? 417 GLY   A C   1 
ATOM   2742 O  O   . GLY   A 1 389 ? 9.706   3.144   85.577  1.00 29.39 ? 417 GLY   A O   1 
ATOM   2743 N  N   . GLY   A 1 390 ? 10.969  1.899   84.173  1.00 31.56 ? 418 GLY   A N   1 
ATOM   2744 C  CA  . GLY   A 1 390 ? 10.290  0.647   84.471  1.00 30.84 ? 418 GLY   A CA  1 
ATOM   2745 C  C   . GLY   A 1 390 ? 9.077   0.371   83.601  1.00 25.97 ? 418 GLY   A C   1 
ATOM   2746 O  O   . GLY   A 1 390 ? 9.068   0.691   82.409  1.00 23.90 ? 418 GLY   A O   1 
ATOM   2747 N  N   . PHE   A 1 391 ? 8.040   -0.229  84.188  1.00 25.98 ? 419 PHE   A N   1 
ATOM   2748 C  CA  . PHE   A 1 391 ? 6.866   -0.608  83.414  1.00 24.41 ? 419 PHE   A CA  1 
ATOM   2749 C  C   . PHE   A 1 391 ? 5.571   -0.231  84.122  1.00 27.40 ? 419 PHE   A C   1 
ATOM   2750 O  O   . PHE   A 1 391 ? 4.488   -0.648  83.678  1.00 24.27 ? 419 PHE   A O   1 
ATOM   2751 C  CB  . PHE   A 1 391 ? 6.915   -2.115  83.093  1.00 21.33 ? 419 PHE   A CB  1 
ATOM   2752 C  CG  . PHE   A 1 391 ? 8.158   -2.526  82.330  1.00 24.92 ? 419 PHE   A CG  1 
ATOM   2753 C  CD1 . PHE   A 1 391 ? 9.312   -2.930  83.002  1.00 22.58 ? 419 PHE   A CD1 1 
ATOM   2754 C  CD2 . PHE   A 1 391 ? 8.189   -2.467  80.940  1.00 22.56 ? 419 PHE   A CD2 1 
ATOM   2755 C  CE1 . PHE   A 1 391 ? 10.455  -3.293  82.301  1.00 22.80 ? 419 PHE   A CE1 1 
ATOM   2756 C  CE2 . PHE   A 1 391 ? 9.334   -2.821  80.232  1.00 23.29 ? 419 PHE   A CE2 1 
ATOM   2757 C  CZ  . PHE   A 1 391 ? 10.472  -3.237  80.916  1.00 24.11 ? 419 PHE   A CZ  1 
ATOM   2758 N  N   . GLY   A 1 392 ? 5.650   0.573   85.180  1.00 28.69 ? 420 GLY   A N   1 
ATOM   2759 C  CA  . GLY   A 1 392 ? 4.480   1.054   85.876  1.00 28.00 ? 420 GLY   A CA  1 
ATOM   2760 C  C   . GLY   A 1 392 ? 3.971   0.142   86.958  1.00 32.44 ? 420 GLY   A C   1 
ATOM   2761 O  O   . GLY   A 1 392 ? 2.791   0.237   87.314  1.00 33.79 ? 420 GLY   A O   1 
ATOM   2762 N  N   . LYS   A 1 393 ? 4.820   -0.738  87.501  1.00 34.81 ? 421 LYS   A N   1 
ATOM   2763 C  CA  . LYS   A 1 393 ? 4.350   -1.659  88.533  1.00 40.82 ? 421 LYS   A CA  1 
ATOM   2764 C  C   . LYS   A 1 393 ? 3.872   -0.906  89.767  1.00 38.85 ? 421 LYS   A C   1 
ATOM   2765 O  O   . LYS   A 1 393 ? 2.956   -1.363  90.459  1.00 38.95 ? 421 LYS   A O   1 
ATOM   2766 C  CB  . LYS   A 1 393 ? 5.452   -2.667  88.903  1.00 40.17 ? 421 LYS   A CB  1 
ATOM   2767 C  CG  . LYS   A 1 393 ? 5.026   -3.716  89.960  1.00 50.37 ? 421 LYS   A CG  1 
ATOM   2768 C  CD  . LYS   A 1 393 ? 4.967   -5.153  89.398  1.00 56.74 ? 421 LYS   A CD  1 
ATOM   2769 C  CE  . LYS   A 1 393 ? 4.628   -6.181  90.487  1.00 54.81 ? 421 LYS   A CE  1 
ATOM   2770 N  NZ  . LYS   A 1 393 ? 3.832   -7.359  89.981  1.00 53.97 ? 421 LYS   A NZ  1 
ATOM   2771 N  N   . GLY   A 1 394 ? 4.462   0.259   90.045  1.00 36.64 ? 422 GLY   A N   1 
ATOM   2772 C  CA  . GLY   A 1 394 ? 4.016   1.061   91.165  1.00 35.27 ? 422 GLY   A CA  1 
ATOM   2773 C  C   . GLY   A 1 394 ? 2.594   1.556   91.029  1.00 40.71 ? 422 GLY   A C   1 
ATOM   2774 O  O   . GLY   A 1 394 ? 1.984   1.938   92.032  1.00 40.44 ? 422 GLY   A O   1 
ATOM   2775 N  N   . ASN   A 1 395 ? 2.046   1.547   89.810  1.00 40.24 ? 423 ASN   A N   1 
ATOM   2776 C  CA  . ASN   A 1 395 ? 0.708   2.077   89.577  1.00 38.04 ? 423 ASN   A CA  1 
ATOM   2777 C  C   . ASN   A 1 395 ? -0.392  1.150   90.076  1.00 41.04 ? 423 ASN   A C   1 
ATOM   2778 O  O   . ASN   A 1 395 ? -1.523  1.609   90.255  1.00 42.93 ? 423 ASN   A O   1 
ATOM   2779 C  CB  . ASN   A 1 395 ? 0.503   2.362   88.089  1.00 34.66 ? 423 ASN   A CB  1 
ATOM   2780 C  CG  . ASN   A 1 395 ? 0.852   3.796   87.711  1.00 34.77 ? 423 ASN   A CG  1 
ATOM   2781 O  OD1 . ASN   A 1 395 ? 0.525   4.740   88.429  1.00 35.01 ? 423 ASN   A OD1 1 
ATOM   2782 N  ND2 . ASN   A 1 395 ? 1.513   3.962   86.573  1.00 34.03 ? 423 ASN   A ND2 1 
ATOM   2783 N  N   . PHE   A 1 396 ? -0.100  -0.136  90.295  1.00 38.00 ? 424 PHE   A N   1 
ATOM   2784 C  CA  . PHE   A 1 396 ? -1.088  -1.020  90.913  1.00 43.98 ? 424 PHE   A CA  1 
ATOM   2785 C  C   . PHE   A 1 396 ? -1.394  -0.568  92.337  1.00 48.94 ? 424 PHE   A C   1 
ATOM   2786 O  O   . PHE   A 1 396 ? -2.552  -0.323  92.699  1.00 47.86 ? 424 PHE   A O   1 
ATOM   2787 C  CB  . PHE   A 1 396 ? -0.591  -2.470  90.908  1.00 44.64 ? 424 PHE   A CB  1 
ATOM   2788 C  CG  . PHE   A 1 396 ? -0.610  -3.131  89.548  1.00 43.16 ? 424 PHE   A CG  1 
ATOM   2789 C  CD1 . PHE   A 1 396 ? 0.538   -3.171  88.768  1.00 42.96 ? 424 PHE   A CD1 1 
ATOM   2790 C  CD2 . PHE   A 1 396 ? -1.757  -3.737  89.065  1.00 42.76 ? 424 PHE   A CD2 1 
ATOM   2791 C  CE1 . PHE   A 1 396 ? 0.539   -3.790  87.528  1.00 39.21 ? 424 PHE   A CE1 1 
ATOM   2792 C  CE2 . PHE   A 1 396 ? -1.763  -4.360  87.820  1.00 43.43 ? 424 PHE   A CE2 1 
ATOM   2793 C  CZ  . PHE   A 1 396 ? -0.612  -4.388  87.052  1.00 36.52 ? 424 PHE   A CZ  1 
ATOM   2794 N  N   . SER   A 1 397 ? -0.354  -0.456  93.162  1.00 50.92 ? 425 SER   A N   1 
ATOM   2795 C  CA  . SER   A 1 397 ? -0.512  0.081   94.508  1.00 54.48 ? 425 SER   A CA  1 
ATOM   2796 C  C   . SER   A 1 397 ? -1.098  1.491   94.482  1.00 52.56 ? 425 SER   A C   1 
ATOM   2797 O  O   . SER   A 1 397 ? -2.025  1.806   95.232  1.00 50.78 ? 425 SER   A O   1 
ATOM   2798 C  CB  . SER   A 1 397 ? 0.839   0.062   95.229  1.00 60.66 ? 425 SER   A CB  1 
ATOM   2799 O  OG  . SER   A 1 397 ? 1.735   1.012   94.668  1.00 65.60 ? 425 SER   A OG  1 
ATOM   2800 N  N   . GLU   A 1 398 ? -0.581  2.352   93.604  1.00 55.21 ? 426 GLU   A N   1 
ATOM   2801 C  CA  . GLU   A 1 398 ? -1.028  3.741   93.593  1.00 52.63 ? 426 GLU   A CA  1 
ATOM   2802 C  C   . GLU   A 1 398 ? -2.492  3.848   93.179  1.00 56.51 ? 426 GLU   A C   1 
ATOM   2803 O  O   . GLU   A 1 398 ? -3.224  4.707   93.686  1.00 55.14 ? 426 GLU   A O   1 
ATOM   2804 C  CB  . GLU   A 1 398 ? -0.133  4.573   92.673  1.00 49.20 ? 426 GLU   A CB  1 
ATOM   2805 C  CG  . GLU   A 1 398 ? 1.247   4.910   93.253  1.00 51.53 ? 426 GLU   A CG  1 
ATOM   2806 C  CD  . GLU   A 1 398 ? 1.167   5.728   94.534  1.00 54.20 ? 426 GLU   A CD  1 
ATOM   2807 O  OE1 . GLU   A 1 398 ? 1.832   5.351   95.526  1.00 53.41 ? 426 GLU   A OE1 1 
ATOM   2808 O  OE2 . GLU   A 1 398 ? 0.429   6.740   94.548  1.00 50.90 ? 426 GLU   A OE2 1 
ATOM   2809 N  N   . LEU   A 1 399 ? -2.944  2.974   92.273  1.00 53.45 ? 427 LEU   A N   1 
ATOM   2810 C  CA  . LEU   A 1 399 ? -4.328  3.040   91.809  1.00 54.86 ? 427 LEU   A CA  1 
ATOM   2811 C  C   . LEU   A 1 399 ? -5.297  2.594   92.894  1.00 57.13 ? 427 LEU   A C   1 
ATOM   2812 O  O   . LEU   A 1 399 ? -6.305  3.263   93.150  1.00 59.39 ? 427 LEU   A O   1 
ATOM   2813 C  CB  . LEU   A 1 399 ? -4.514  2.186   90.559  1.00 49.28 ? 427 LEU   A CB  1 
ATOM   2814 C  CG  . LEU   A 1 399 ? -4.407  2.883   89.210  1.00 50.55 ? 427 LEU   A CG  1 
ATOM   2815 C  CD1 . LEU   A 1 399 ? -4.612  1.857   88.098  1.00 42.31 ? 427 LEU   A CD1 1 
ATOM   2816 C  CD2 . LEU   A 1 399 ? -5.417  4.026   89.110  1.00 45.83 ? 427 LEU   A CD2 1 
ATOM   2817 N  N   . PHE   A 1 400 ? -5.029  1.446   93.518  1.00 56.43 ? 428 PHE   A N   1 
ATOM   2818 C  CA  . PHE   A 1 400 ? -5.854  1.003   94.636  1.00 58.05 ? 428 PHE   A CA  1 
ATOM   2819 C  C   . PHE   A 1 400 ? -5.948  2.089   95.704  1.00 61.39 ? 428 PHE   A C   1 
ATOM   2820 O  O   . PHE   A 1 400 ? -7.037  2.410   96.192  1.00 60.27 ? 428 PHE   A O   1 
ATOM   2821 C  CB  . PHE   A 1 400 ? -5.283  -0.289  95.222  1.00 50.08 ? 428 PHE   A CB  1 
ATOM   2822 N  N   . LYS   A 1 401 ? -4.814  2.697   96.042  1.00 58.06 ? 429 LYS   A N   1 
ATOM   2823 C  CA  . LYS   A 1 401 ? -4.787  3.662   97.131  1.00 61.71 ? 429 LYS   A CA  1 
ATOM   2824 C  C   . LYS   A 1 401 ? -5.414  4.993   96.727  1.00 64.65 ? 429 LYS   A C   1 
ATOM   2825 O  O   . LYS   A 1 401 ? -5.784  5.790   97.596  1.00 67.25 ? 429 LYS   A O   1 
ATOM   2826 C  CB  . LYS   A 1 401 ? -3.348  3.856   97.592  1.00 57.15 ? 429 LYS   A CB  1 
ATOM   2827 C  CG  . LYS   A 1 401 ? -3.107  5.064   98.482  1.00 61.84 ? 429 LYS   A CG  1 
ATOM   2828 C  CD  . LYS   A 1 401 ? -1.720  5.611   98.263  1.00 63.02 ? 429 LYS   A CD  1 
ATOM   2829 C  CE  . LYS   A 1 401 ? -0.762  4.468   98.208  1.00 62.44 ? 429 LYS   A CE  1 
ATOM   2830 N  NZ  . LYS   A 1 401 ? 0.619   4.851   98.575  1.00 62.56 ? 429 LYS   A NZ  1 
ATOM   2831 N  N   . SER   A 1 402 ? -5.570  5.255   95.432  1.00 61.20 ? 430 SER   A N   1 
ATOM   2832 C  CA  . SER   A 1 402 ? -6.365  6.415   95.049  1.00 62.94 ? 430 SER   A CA  1 
ATOM   2833 C  C   . SER   A 1 402 ? -7.844  6.067   95.009  1.00 64.31 ? 430 SER   A C   1 
ATOM   2834 O  O   . SER   A 1 402 ? -8.698  6.942   95.185  1.00 60.40 ? 430 SER   A O   1 
ATOM   2835 C  CB  . SER   A 1 402 ? -5.903  6.966   93.704  1.00 53.45 ? 430 SER   A CB  1 
ATOM   2836 O  OG  . SER   A 1 402 ? -4.821  6.222   93.189  1.00 55.81 ? 430 SER   A OG  1 
ATOM   2837 N  N   . ILE   A 1 403 ? -8.164  4.787   94.824  1.00 62.42 ? 431 ILE   A N   1 
ATOM   2838 C  CA  . ILE   A 1 403 ? -9.560  4.399   94.664  1.00 64.93 ? 431 ILE   A CA  1 
ATOM   2839 C  C   . ILE   A 1 403 ? -10.312 4.527   95.985  1.00 71.06 ? 431 ILE   A C   1 
ATOM   2840 O  O   . ILE   A 1 403 ? -11.358 5.183   96.054  1.00 70.71 ? 431 ILE   A O   1 
ATOM   2841 C  CB  . ILE   A 1 403 ? -9.666  2.977   94.088  1.00 59.79 ? 431 ILE   A CB  1 
ATOM   2842 N  N   . GLU   A 1 404 ? -9.815  3.874   97.043  1.00 70.69 ? 432 GLU   A N   1 
ATOM   2843 C  CA  . GLU   A 1 404 ? -10.515 3.920   98.322  1.00 71.40 ? 432 GLU   A CA  1 
ATOM   2844 C  C   . GLU   A 1 404 ? -10.413 5.299   98.960  1.00 72.32 ? 432 GLU   A C   1 
ATOM   2845 O  O   . GLU   A 1 404 ? -11.341 5.727   99.652  1.00 79.25 ? 432 GLU   A O   1 
ATOM   2846 C  CB  . GLU   A 1 404 ? -9.967  2.838   99.268  1.00 73.68 ? 432 GLU   A CB  1 
ATOM   2847 N  N   . GLU   A 1 405 ? -9.324  6.032   98.712  1.00 71.06 ? 433 GLU   A N   1 
ATOM   2848 C  CA  . GLU   A 1 405 ? -9.264  7.388   99.252  1.00 74.07 ? 433 GLU   A CA  1 
ATOM   2849 C  C   . GLU   A 1 405 ? -10.092 8.373   98.437  1.00 74.05 ? 433 GLU   A C   1 
ATOM   2850 O  O   . GLU   A 1 405 ? -10.385 9.468   98.935  1.00 74.63 ? 433 GLU   A O   1 
ATOM   2851 C  CB  . GLU   A 1 405 ? -7.813  7.908   99.383  1.00 67.17 ? 433 GLU   A CB  1 
ATOM   2852 C  CG  . GLU   A 1 405 ? -7.122  8.392   98.106  1.00 65.61 ? 433 GLU   A CG  1 
ATOM   2853 C  CD  . GLU   A 1 405 ? -5.615  8.649   98.295  1.00 67.29 ? 433 GLU   A CD  1 
ATOM   2854 O  OE1 . GLU   A 1 405 ? -5.009  8.082   99.228  1.00 69.32 ? 433 GLU   A OE1 1 
ATOM   2855 O  OE2 . GLU   A 1 405 ? -5.029  9.407   97.490  1.00 63.99 ? 433 GLU   A OE2 1 
ATOM   2856 N  N   . TYR   A 1 406 ? -10.501 8.004   97.220  1.00 73.22 ? 434 TYR   A N   1 
ATOM   2857 C  CA  . TYR   A 1 406 ? -11.474 8.813   96.500  1.00 69.65 ? 434 TYR   A CA  1 
ATOM   2858 C  C   . TYR   A 1 406 ? -12.894 8.541   96.968  1.00 76.43 ? 434 TYR   A C   1 
ATOM   2859 O  O   . TYR   A 1 406 ? -13.738 9.443   96.916  1.00 77.08 ? 434 TYR   A O   1 
ATOM   2860 C  CB  . TYR   A 1 406 ? -11.380 8.567   94.998  1.00 63.21 ? 434 TYR   A CB  1 
ATOM   2861 C  CG  . TYR   A 1 406 ? -12.414 9.338   94.218  1.00 58.29 ? 434 TYR   A CG  1 
ATOM   2862 C  CD1 . TYR   A 1 406 ? -12.317 10.718  94.073  1.00 58.36 ? 434 TYR   A CD1 1 
ATOM   2863 C  CD2 . TYR   A 1 406 ? -13.501 8.691   93.644  1.00 60.66 ? 434 TYR   A CD2 1 
ATOM   2864 C  CE1 . TYR   A 1 406 ? -13.268 11.429  93.363  1.00 56.65 ? 434 TYR   A CE1 1 
ATOM   2865 C  CE2 . TYR   A 1 406 ? -14.457 9.394   92.930  1.00 56.85 ? 434 TYR   A CE2 1 
ATOM   2866 C  CZ  . TYR   A 1 406 ? -14.333 10.759  92.791  1.00 56.80 ? 434 TYR   A CZ  1 
ATOM   2867 O  OH  . TYR   A 1 406 ? -15.283 11.455  92.081  1.00 66.41 ? 434 TYR   A OH  1 
ATOM   2868 N  N   . GLU   A 1 407 ? -13.182 7.310   97.401  1.00 77.42 ? 435 GLU   A N   1 
ATOM   2869 C  CA  . GLU   A 1 407 ? -14.430 7.055   98.112  1.00 73.58 ? 435 GLU   A CA  1 
ATOM   2870 C  C   . GLU   A 1 407 ? -14.573 8.009   99.293  1.00 78.31 ? 435 GLU   A C   1 
ATOM   2871 O  O   . GLU   A 1 407 ? -15.676 8.483   99.590  1.00 80.26 ? 435 GLU   A O   1 
ATOM   2872 C  CB  . GLU   A 1 407 ? -14.481 5.598   98.573  1.00 71.57 ? 435 GLU   A CB  1 
ATOM   2873 N  N   . LYS   A 1 408 ? -13.460 8.304   99.967  1.00 79.85 ? 436 LYS   A N   1 
ATOM   2874 C  CA  . LYS   A 1 408 ? -13.332 9.418   100.910 1.00 80.07 ? 436 LYS   A CA  1 
ATOM   2875 C  C   . LYS   A 1 408 ? -14.467 9.500   101.923 1.00 84.75 ? 436 LYS   A C   1 
ATOM   2876 O  O   . LYS   A 1 408 ? -14.848 10.591  102.345 1.00 87.91 ? 436 LYS   A O   1 
ATOM   2877 C  CB  . LYS   A 1 408 ? -13.233 10.745  100.144 1.00 68.76 ? 436 LYS   A CB  1 
HETATM 2878 CO CO  . CO    B 2 .   ? 3.559   -2.555  79.802  1.00 27.85 ? 501 CO    A CO  1 
HETATM 2879 C  C10 . A1LW4 C 3 .   ? 4.061   -4.248  82.557  1.00 25.54 ? 502 A1LW4 A C10 1 
HETATM 2880 N  N12 . A1LW4 C 3 .   ? 5.673   -4.657  81.209  1.00 25.23 ? 502 A1LW4 A N12 1 
HETATM 2881 C  C13 . A1LW4 C 3 .   ? 5.981   -5.177  82.406  1.00 25.19 ? 502 A1LW4 A C13 1 
HETATM 2882 C  C15 . A1LW4 C 3 .   ? 7.251   -5.958  82.813  1.00 22.63 ? 502 A1LW4 A C15 1 
HETATM 2883 C  C20 . A1LW4 C 3 .   ? -5.198  -2.902  82.029  1.00 30.76 ? 502 A1LW4 A C20 1 
HETATM 2884 C  C21 . A1LW4 C 3 .   ? -6.277  -3.472  82.962  1.00 36.11 ? 502 A1LW4 A C21 1 
HETATM 2885 C  C22 . A1LW4 C 3 .   ? -2.287  -0.591  86.053  1.00 30.58 ? 502 A1LW4 A C22 1 
HETATM 2886 C  C01 . A1LW4 C 3 .   ? 0.971   -2.245  83.411  1.00 27.89 ? 502 A1LW4 A C01 1 
HETATM 2887 C  C02 . A1LW4 C 3 .   ? 1.319   -1.166  84.424  1.00 31.89 ? 502 A1LW4 A C02 1 
HETATM 2888 C  C03 . A1LW4 C 3 .   ? 0.208   -0.599  85.325  1.00 31.88 ? 502 A1LW4 A C03 1 
HETATM 2889 C  C04 . A1LW4 C 3 .   ? -1.180  -1.168  85.159  1.00 35.22 ? 502 A1LW4 A C04 1 
HETATM 2890 C  C05 . A1LW4 C 3 .   ? -1.483  -2.253  84.143  1.00 32.11 ? 502 A1LW4 A C05 1 
HETATM 2891 C  C06 . A1LW4 C 3 .   ? -0.396  -2.798  83.246  1.00 27.14 ? 502 A1LW4 A C06 1 
HETATM 2892 C  C07 . A1LW4 C 3 .   ? 2.056   -2.756  82.552  1.00 27.36 ? 502 A1LW4 A C07 1 
HETATM 2893 O  O08 . A1LW4 C 3 .   ? 2.180   -2.358  81.454  1.00 26.84 ? 502 A1LW4 A O08 1 
HETATM 2894 N  N09 . A1LW4 C 3 .   ? 2.899   -3.744  83.208  1.00 26.98 ? 502 A1LW4 A N09 1 
HETATM 2895 N  N11 . A1LW4 C 3 .   ? 4.464   -4.047  81.317  1.00 23.05 ? 502 A1LW4 A N11 1 
HETATM 2896 O  O14 . A1LW4 C 3 .   ? 4.995   -4.917  83.255  1.00 27.67 ? 502 A1LW4 A O14 1 
HETATM 2897 F  F16 . A1LW4 C 3 .   ? -0.675  -3.793  82.319  1.00 27.57 ? 502 A1LW4 A F16 1 
HETATM 2898 S  S17 . A1LW4 C 3 .   ? -3.074  -3.018  83.823  1.00 30.24 ? 502 A1LW4 A S17 1 
HETATM 2899 O  O18 . A1LW4 C 3 .   ? -3.229  -4.437  84.215  1.00 36.89 ? 502 A1LW4 A O18 1 
HETATM 2900 C  C19 . A1LW4 C 3 .   ? -4.320  -2.015  82.910  1.00 37.19 ? 502 A1LW4 A C19 1 
HETATM 2901 F  F23 . A1LW4 C 3 .   ? -2.682  -1.494  86.955  1.00 32.63 ? 502 A1LW4 A F23 1 
HETATM 2902 F  F24 . A1LW4 C 3 .   ? -3.319  -0.189  85.240  1.00 32.64 ? 502 A1LW4 A F24 1 
HETATM 2903 F  F25 . A1LW4 C 3 .   ? -1.695  0.509   86.649  1.00 36.30 ? 502 A1LW4 A F25 1 
HETATM 2904 O  O   . HOH   D 4 .   ? 1.870   23.174  92.847  1.00 50.82 ? 601 HOH   A O   1 
HETATM 2905 O  O   . HOH   D 4 .   ? 4.581   -22.767 55.232  1.00 24.72 ? 602 HOH   A O   1 
HETATM 2906 O  O   . HOH   D 4 .   ? -9.032  6.562   80.504  1.00 39.55 ? 603 HOH   A O   1 
HETATM 2907 O  O   . HOH   D 4 .   ? 8.893   -12.558 49.998  1.00 28.94 ? 604 HOH   A O   1 
HETATM 2908 O  O   . HOH   D 4 .   ? -2.123  9.986   50.338  1.00 52.39 ? 605 HOH   A O   1 
HETATM 2909 O  O   . HOH   D 4 .   ? -10.157 -23.582 66.971  1.00 37.96 ? 606 HOH   A O   1 
HETATM 2910 O  O   . HOH   D 4 .   ? 8.717   -3.224  51.086  1.00 49.36 ? 607 HOH   A O   1 
HETATM 2911 O  O   . HOH   D 4 .   ? 1.742   -27.212 87.099  1.00 45.47 ? 608 HOH   A O   1 
HETATM 2912 O  O   . HOH   D 4 .   ? 1.697   -21.582 48.383  1.00 21.95 ? 609 HOH   A O   1 
HETATM 2913 O  O   . HOH   D 4 .   ? 15.152  2.028   84.681  1.00 45.60 ? 610 HOH   A O   1 
HETATM 2914 O  O   . HOH   D 4 .   ? -10.093 -12.570 54.792  1.00 20.87 ? 611 HOH   A O   1 
HETATM 2915 O  O   . HOH   D 4 .   ? -1.919  7.206   94.343  1.00 50.16 ? 612 HOH   A O   1 
HETATM 2916 O  O   . HOH   D 4 .   ? 11.360  -3.035  50.974  1.00 54.48 ? 613 HOH   A O   1 
HETATM 2917 O  O   . HOH   D 4 .   ? 21.298  -10.734 77.851  1.00 30.90 ? 614 HOH   A O   1 
HETATM 2918 O  O   . HOH   D 4 .   ? -15.926 1.868   75.235  1.00 37.53 ? 615 HOH   A O   1 
HETATM 2919 O  O   . HOH   D 4 .   ? 26.482  -12.103 63.869  1.00 46.66 ? 616 HOH   A O   1 
HETATM 2920 O  O   . HOH   D 4 .   ? -8.169  -12.696 71.068  1.00 19.61 ? 617 HOH   A O   1 
HETATM 2921 O  O   . HOH   D 4 .   ? 1.993   -1.344  44.430  1.00 41.14 ? 618 HOH   A O   1 
HETATM 2922 O  O   . HOH   D 4 .   ? 22.478  -8.845  70.793  1.00 24.96 ? 619 HOH   A O   1 
HETATM 2923 O  O   . HOH   D 4 .   ? 12.503  0.885   76.082  1.00 22.88 ? 620 HOH   A O   1 
HETATM 2924 O  O   . HOH   D 4 .   ? 18.669  3.075   69.248  1.00 44.05 ? 621 HOH   A O   1 
HETATM 2925 O  O   . HOH   D 4 .   ? 18.783  -0.213  79.693  1.00 32.13 ? 622 HOH   A O   1 
HETATM 2926 O  O   . HOH   D 4 .   ? -0.539  8.963   92.130  1.00 39.89 ? 623 HOH   A O   1 
HETATM 2927 O  O   . HOH   D 4 .   ? -1.474  -21.193 86.119  1.00 28.10 ? 624 HOH   A O   1 
HETATM 2928 O  O   . HOH   D 4 .   ? 7.770   -16.680 49.672  1.00 38.90 ? 625 HOH   A O   1 
HETATM 2929 O  O   . HOH   D 4 .   ? 7.119   -22.078 52.198  1.00 46.30 ? 626 HOH   A O   1 
HETATM 2930 O  O   . HOH   D 4 .   ? 15.649  -27.484 69.941  1.00 26.46 ? 627 HOH   A O   1 
HETATM 2931 O  O   . HOH   D 4 .   ? -9.636  -15.147 55.971  1.00 35.05 ? 628 HOH   A O   1 
HETATM 2932 O  O   . HOH   D 4 .   ? 4.810   -6.769  86.150  1.00 44.07 ? 629 HOH   A O   1 
HETATM 2933 O  O   . HOH   D 4 .   ? 3.523   -16.807 58.889  1.00 18.09 ? 630 HOH   A O   1 
HETATM 2934 O  O   . HOH   D 4 .   ? 0.618   19.376  74.798  1.00 41.22 ? 631 HOH   A O   1 
HETATM 2935 O  O   . HOH   D 4 .   ? 13.748  -2.968  69.695  1.00 27.10 ? 632 HOH   A O   1 
HETATM 2936 O  O   . HOH   D 4 .   ? -6.844  -8.675  49.417  1.00 16.14 ? 633 HOH   A O   1 
HETATM 2937 O  O   . HOH   D 4 .   ? 3.205   -10.464 46.895  1.00 22.58 ? 634 HOH   A O   1 
HETATM 2938 O  O   . HOH   D 4 .   ? -18.768 4.737   65.974  1.00 28.18 ? 635 HOH   A O   1 
HETATM 2939 O  O   . HOH   D 4 .   ? 4.591   -0.849  81.079  1.00 23.68 ? 636 HOH   A O   1 
HETATM 2940 O  O   . HOH   D 4 .   ? 6.957   -11.355 75.987  1.00 18.27 ? 637 HOH   A O   1 
HETATM 2941 O  O   . HOH   D 4 .   ? -5.001  -19.546 48.538  1.00 17.85 ? 638 HOH   A O   1 
HETATM 2942 O  O   . HOH   D 4 .   ? 5.980   -20.729 61.710  1.00 21.65 ? 639 HOH   A O   1 
HETATM 2943 O  O   . HOH   D 4 .   ? 20.040  -7.686  59.648  1.00 28.07 ? 640 HOH   A O   1 
HETATM 2944 O  O   . HOH   D 4 .   ? 4.125   16.309  68.741  1.00 27.71 ? 641 HOH   A O   1 
HETATM 2945 O  O   . HOH   D 4 .   ? 12.597  -3.516  53.774  1.00 43.60 ? 642 HOH   A O   1 
HETATM 2946 O  O   . HOH   D 4 .   ? 16.151  -3.090  63.791  1.00 33.26 ? 643 HOH   A O   1 
HETATM 2947 O  O   . HOH   D 4 .   ? -1.303  -18.200 71.387  1.00 20.91 ? 644 HOH   A O   1 
HETATM 2948 O  O   . HOH   D 4 .   ? -14.087 -13.941 74.737  1.00 15.05 ? 645 HOH   A O   1 
HETATM 2949 O  O   . HOH   D 4 .   ? -4.790  -4.228  46.881  1.00 30.99 ? 646 HOH   A O   1 
HETATM 2950 O  O   . HOH   D 4 .   ? -12.570 -11.744 54.519  1.00 17.15 ? 647 HOH   A O   1 
HETATM 2951 O  O   . HOH   D 4 .   ? -10.949 -21.456 77.703  1.00 28.69 ? 648 HOH   A O   1 
HETATM 2952 O  O   . HOH   D 4 .   ? -7.217  -15.365 90.124  1.00 52.16 ? 649 HOH   A O   1 
HETATM 2953 O  O   . HOH   D 4 .   ? 26.347  -11.577 74.073  1.00 26.86 ? 650 HOH   A O   1 
HETATM 2954 O  O   . HOH   D 4 .   ? 19.604  -12.544 53.658  1.00 33.97 ? 651 HOH   A O   1 
HETATM 2955 O  O   . HOH   D 4 .   ? 18.921  -5.424  70.892  1.00 29.15 ? 652 HOH   A O   1 
HETATM 2956 O  O   . HOH   D 4 .   ? 6.237   -20.570 87.469  1.00 29.24 ? 653 HOH   A O   1 
HETATM 2957 O  O   . HOH   D 4 .   ? 7.629   1.816   86.653  1.00 29.29 ? 654 HOH   A O   1 
HETATM 2958 O  O   . HOH   D 4 .   ? 1.998   -14.658 57.522  1.00 18.28 ? 655 HOH   A O   1 
HETATM 2959 O  O   . HOH   D 4 .   ? 12.457  -1.050  74.158  1.00 22.96 ? 656 HOH   A O   1 
HETATM 2960 O  O   . HOH   D 4 .   ? 1.426   -5.636  84.456  1.00 31.88 ? 657 HOH   A O   1 
HETATM 2961 O  O   . HOH   D 4 .   ? 21.795  -4.225  69.010  1.00 29.96 ? 658 HOH   A O   1 
HETATM 2962 O  O   . HOH   D 4 .   ? 4.134   -12.921 46.099  1.00 24.81 ? 659 HOH   A O   1 
HETATM 2963 O  O   . HOH   D 4 .   ? 18.548  -7.051  51.770  1.00 35.90 ? 660 HOH   A O   1 
HETATM 2964 O  O   . HOH   D 4 .   ? -16.354 4.175   72.092  1.00 29.98 ? 661 HOH   A O   1 
HETATM 2965 O  O   . HOH   D 4 .   ? 11.673  -0.863  87.390  1.00 45.99 ? 662 HOH   A O   1 
HETATM 2966 O  O   . HOH   D 4 .   ? -14.595 9.684   69.339  1.00 23.32 ? 663 HOH   A O   1 
HETATM 2967 O  O   . HOH   D 4 .   ? -3.484  -23.073 41.928  1.00 35.40 ? 664 HOH   A O   1 
HETATM 2968 O  O   . HOH   D 4 .   ? -13.473 -14.193 68.957  1.00 27.20 ? 665 HOH   A O   1 
HETATM 2969 O  O   . HOH   D 4 .   ? 3.864   -17.905 61.282  1.00 13.22 ? 666 HOH   A O   1 
HETATM 2970 O  O   . HOH   D 4 .   ? -6.181  3.518   52.238  1.00 31.83 ? 667 HOH   A O   1 
HETATM 2971 O  O   . HOH   D 4 .   ? 2.921   -25.472 41.031  1.00 31.68 ? 668 HOH   A O   1 
HETATM 2972 O  O   . HOH   D 4 .   ? -1.303  -6.807  83.152  1.00 32.53 ? 669 HOH   A O   1 
HETATM 2973 O  O   . HOH   D 4 .   ? -3.049  -0.054  46.740  1.00 27.96 ? 670 HOH   A O   1 
HETATM 2974 O  O   . HOH   D 4 .   ? -1.753  -27.070 58.254  1.00 39.81 ? 671 HOH   A O   1 
HETATM 2975 O  O   . HOH   D 4 .   ? 4.175   -7.455  82.583  1.00 33.52 ? 672 HOH   A O   1 
HETATM 2976 O  O   . HOH   D 4 .   ? -0.714  -28.791 45.047  1.00 38.85 ? 673 HOH   A O   1 
HETATM 2977 O  O   . HOH   D 4 .   ? 1.471   -21.572 52.305  1.00 41.00 ? 674 HOH   A O   1 
HETATM 2978 O  O   . HOH   D 4 .   ? 4.423   -20.908 69.125  1.00 23.54 ? 675 HOH   A O   1 
HETATM 2979 O  O   . HOH   D 4 .   ? -11.756 -2.230  70.608  1.00 19.03 ? 676 HOH   A O   1 
HETATM 2980 O  O   . HOH   D 4 .   ? -1.237  -13.749 70.612  1.00 15.01 ? 677 HOH   A O   1 
HETATM 2981 O  O   . HOH   D 4 .   ? 22.139  -12.852 64.214  1.00 26.76 ? 678 HOH   A O   1 
HETATM 2982 O  O   . HOH   D 4 .   ? 23.878  -2.041  55.486  1.00 53.15 ? 679 HOH   A O   1 
HETATM 2983 O  O   . HOH   D 4 .   ? 3.883   13.982  61.237  1.00 46.99 ? 680 HOH   A O   1 
HETATM 2984 O  O   . HOH   D 4 .   ? -11.293 6.525   79.443  1.00 48.52 ? 681 HOH   A O   1 
HETATM 2985 O  O   . HOH   D 4 .   ? -8.825  -7.992  72.126  1.00 16.60 ? 682 HOH   A O   1 
HETATM 2986 O  O   . HOH   D 4 .   ? 9.493   -0.631  66.608  1.00 14.56 ? 683 HOH   A O   1 
HETATM 2987 O  O   . HOH   D 4 .   ? -6.518  -8.684  79.063  1.00 28.27 ? 684 HOH   A O   1 
HETATM 2988 O  O   . HOH   D 4 .   ? 13.681  -3.294  57.569  1.00 47.97 ? 685 HOH   A O   1 
HETATM 2989 O  O   . HOH   D 4 .   ? -6.699  5.743   82.079  1.00 29.45 ? 686 HOH   A O   1 
HETATM 2990 O  O   . HOH   D 4 .   ? 26.349  -14.906 61.030  0.50 41.52 ? 687 HOH   A O   1 
HETATM 2991 O  O   . HOH   D 4 .   ? 0.696   -15.013 40.905  1.00 41.47 ? 688 HOH   A O   1 
HETATM 2992 O  O   . HOH   D 4 .   ? 8.021   -1.708  86.599  1.00 32.45 ? 689 HOH   A O   1 
HETATM 2993 O  O   . HOH   D 4 .   ? 2.748   7.668   61.184  1.00 24.53 ? 690 HOH   A O   1 
HETATM 2994 O  O   . HOH   D 4 .   ? 20.268  -9.654  85.086  1.00 42.06 ? 691 HOH   A O   1 
HETATM 2995 O  O   . HOH   D 4 .   ? 12.264  -0.803  66.556  1.00 23.00 ? 692 HOH   A O   1 
HETATM 2996 O  O   . HOH   D 4 .   ? -8.289  5.827   68.664  1.00 12.58 ? 693 HOH   A O   1 
HETATM 2997 O  O   . HOH   D 4 .   ? -15.637 3.672   67.524  1.00 20.55 ? 694 HOH   A O   1 
HETATM 2998 O  O   . HOH   D 4 .   ? -14.108 -6.030  73.548  1.00 29.42 ? 695 HOH   A O   1 
HETATM 2999 O  O   . HOH   D 4 .   ? 15.475  -23.287 75.880  1.00 27.37 ? 696 HOH   A O   1 
HETATM 3000 O  O   . HOH   D 4 .   ? -14.276 13.726  68.283  1.00 35.59 ? 697 HOH   A O   1 
HETATM 3001 O  O   . HOH   D 4 .   ? 0.851   7.536   65.517  1.00 16.00 ? 698 HOH   A O   1 
HETATM 3002 O  O   . HOH   D 4 .   ? -12.230 5.799   75.888  1.00 26.55 ? 699 HOH   A O   1 
HETATM 3003 O  O   . HOH   D 4 .   ? 10.098  13.721  72.614  1.00 25.41 ? 700 HOH   A O   1 
HETATM 3004 O  O   . HOH   D 4 .   ? -7.532  -3.412  78.619  1.00 27.28 ? 701 HOH   A O   1 
HETATM 3005 O  O   . HOH   D 4 .   ? 11.182  -24.776 79.918  1.00 43.10 ? 702 HOH   A O   1 
HETATM 3006 O  O   . HOH   D 4 .   ? -4.542  -9.839  81.055  1.00 23.01 ? 703 HOH   A O   1 
HETATM 3007 O  O   . HOH   D 4 .   ? 3.300   -23.047 64.079  1.00 35.68 ? 704 HOH   A O   1 
HETATM 3008 O  O   . HOH   D 4 .   ? 1.841   -6.896  82.279  1.00 32.21 ? 705 HOH   A O   1 
HETATM 3009 O  O   . HOH   D 4 .   ? -2.515  -20.822 73.421  1.00 26.63 ? 706 HOH   A O   1 
HETATM 3010 O  O   . HOH   D 4 .   ? -8.396  -10.114 80.688  1.00 38.25 ? 707 HOH   A O   1 
HETATM 3011 O  O   . HOH   D 4 .   ? -10.457 -16.308 48.183  1.00 16.48 ? 708 HOH   A O   1 
HETATM 3012 O  O   . HOH   D 4 .   ? -2.959  -25.443 55.123  1.00 39.87 ? 709 HOH   A O   1 
HETATM 3013 O  O   . HOH   D 4 .   ? -12.842 -3.435  73.993  1.00 26.82 ? 710 HOH   A O   1 
HETATM 3014 O  O   . HOH   D 4 .   ? -11.655 8.274   74.810  1.00 27.19 ? 711 HOH   A O   1 
HETATM 3015 O  O   . HOH   D 4 .   ? 12.726  11.689  85.326  1.00 45.94 ? 712 HOH   A O   1 
HETATM 3016 O  O   . HOH   D 4 .   ? -8.635  1.618   84.574  1.00 42.15 ? 713 HOH   A O   1 
HETATM 3017 O  O   . HOH   D 4 .   ? -5.593  3.184   81.043  1.00 25.80 ? 714 HOH   A O   1 
HETATM 3018 O  O   . HOH   D 4 .   ? -1.441  -22.269 77.277  1.00 24.11 ? 715 HOH   A O   1 
HETATM 3019 O  O   . HOH   D 4 .   ? -3.847  17.526  69.375  1.00 35.14 ? 716 HOH   A O   1 
HETATM 3020 O  O   . HOH   D 4 .   ? -2.683  5.559   55.116  1.00 23.74 ? 717 HOH   A O   1 
HETATM 3021 O  O   . HOH   D 4 .   ? 26.206  -18.500 70.943  1.00 34.80 ? 718 HOH   A O   1 
HETATM 3022 O  O   . HOH   D 4 .   ? -12.591 -16.648 66.679  1.00 46.25 ? 719 HOH   A O   1 
HETATM 3023 O  O   . HOH   D 4 .   ? 10.598  -18.541 57.401  1.00 26.59 ? 720 HOH   A O   1 
HETATM 3024 O  O   . HOH   D 4 .   ? -8.484  -8.887  69.616  1.00 19.73 ? 721 HOH   A O   1 
HETATM 3025 O  O   . HOH   D 4 .   ? -3.728  -24.270 48.567  1.00 24.48 ? 722 HOH   A O   1 
HETATM 3026 O  O   . HOH   D 4 .   ? -10.317 -10.742 70.154  1.00 18.77 ? 723 HOH   A O   1 
HETATM 3027 O  O   . HOH   D 4 .   ? 3.973   -3.658  86.027  1.00 35.66 ? 724 HOH   A O   1 
HETATM 3028 O  O   . HOH   D 4 .   ? 3.757   -21.707 80.561  1.00 33.58 ? 725 HOH   A O   1 
HETATM 3029 O  O   . HOH   D 4 .   ? -6.653  -22.331 82.989  1.00 50.16 ? 726 HOH   A O   1 
HETATM 3030 O  O   . HOH   D 4 .   ? 11.934  -0.468  68.885  1.00 27.01 ? 727 HOH   A O   1 
HETATM 3031 O  O   . HOH   D 4 .   ? -5.112  -12.289 71.521  1.00 19.93 ? 728 HOH   A O   1 
HETATM 3032 O  O   . HOH   D 4 .   ? -7.615  -16.707 59.947  1.00 18.62 ? 729 HOH   A O   1 
HETATM 3033 O  O   . HOH   D 4 .   ? 25.554  -8.183  70.845  1.00 39.34 ? 730 HOH   A O   1 
HETATM 3034 O  O   . HOH   D 4 .   ? 2.990   -21.904 76.203  1.00 38.17 ? 731 HOH   A O   1 
HETATM 3035 O  O   . HOH   D 4 .   ? -7.804  -4.369  50.402  1.00 49.11 ? 732 HOH   A O   1 
HETATM 3036 O  O   . HOH   D 4 .   ? -2.854  -15.772 71.042  1.00 15.07 ? 733 HOH   A O   1 
HETATM 3037 O  O   . HOH   D 4 .   ? -2.582  -11.653 70.989  1.00 14.21 ? 734 HOH   A O   1 
HETATM 3038 O  O   . HOH   D 4 .   ? -10.103 -0.353  72.378  1.00 19.17 ? 735 HOH   A O   1 
HETATM 3039 O  O   . HOH   D 4 .   ? -0.863  -22.878 53.032  1.00 32.10 ? 736 HOH   A O   1 
HETATM 3040 O  O   . HOH   D 4 .   ? 21.327  -6.080  71.832  1.00 28.19 ? 737 HOH   A O   1 
HETATM 3041 O  O   . HOH   D 4 .   ? -1.388  -25.878 47.861  1.00 41.20 ? 738 HOH   A O   1 
HETATM 3042 O  O   . HOH   D 4 .   ? 8.570   -16.767 56.808  1.00 29.20 ? 739 HOH   A O   1 
HETATM 3043 O  O   . HOH   D 4 .   ? 16.011  -20.764 51.316  1.00 41.08 ? 740 HOH   A O   1 
HETATM 3044 O  O   . HOH   D 4 .   ? 7.082   -1.421  45.193  1.00 34.76 ? 741 HOH   A O   1 
HETATM 3045 O  O   . HOH   D 4 .   ? 2.966   -23.093 60.642  1.00 30.50 ? 742 HOH   A O   1 
HETATM 3046 O  O   . HOH   D 4 .   ? 3.423   -22.110 66.748  1.00 31.57 ? 743 HOH   A O   1 
HETATM 3047 O  O   . HOH   D 4 .   ? -2.364  12.929  61.340  1.00 24.72 ? 744 HOH   A O   1 
HETATM 3048 O  O   . HOH   D 4 .   ? 10.172  -19.839 43.366  1.00 44.57 ? 745 HOH   A O   1 
HETATM 3049 O  O   . HOH   D 4 .   ? 5.611   -19.742 90.718  1.00 46.57 ? 746 HOH   A O   1 
HETATM 3050 O  O   . HOH   D 4 .   ? 21.222  -11.504 56.020  1.00 36.09 ? 747 HOH   A O   1 
HETATM 3051 O  O   . HOH   D 4 .   ? -4.709  -14.126 69.345  1.00 20.38 ? 748 HOH   A O   1 
HETATM 3052 O  O   . HOH   D 4 .   ? 3.813   -12.880 43.381  1.00 37.32 ? 749 HOH   A O   1 
HETATM 3053 O  O   . HOH   D 4 .   ? -0.562  -22.761 49.297  1.00 32.41 ? 750 HOH   A O   1 
HETATM 3054 O  O   . HOH   D 4 .   ? 7.909   -2.830  65.163  1.00 13.83 ? 751 HOH   A O   1 
HETATM 3055 O  O   . HOH   D 4 .   ? 2.329   -22.511 50.401  1.00 47.02 ? 752 HOH   A O   1 
HETATM 3056 O  O   . HOH   D 4 .   ? -9.993  -2.129  50.558  1.00 44.69 ? 753 HOH   A O   1 
HETATM 3057 O  O   . HOH   D 4 .   ? 9.407   -0.441  88.580  1.00 34.70 ? 754 HOH   A O   1 
HETATM 3058 O  O   . HOH   D 4 .   ? 23.534  -11.763 56.729  1.00 47.53 ? 755 HOH   A O   1 
HETATM 3059 O  O   . HOH   D 4 .   ? -5.975  -25.238 54.423  1.00 37.97 ? 756 HOH   A O   1 
HETATM 3060 O  O   . HOH   D 4 .   ? 2.026   -23.998 48.742  1.00 42.48 ? 757 HOH   A O   1 
HETATM 3061 O  O   . HOH   D 4 .   ? -6.429  2.150   84.375  1.00 38.06 ? 758 HOH   A O   1 
HETATM 3062 O  O   . HOH   D 4 .   ? 21.294  -13.562 52.567  1.00 53.42 ? 759 HOH   A O   1 
HETATM 3063 O  O   . HOH   D 4 .   ? 6.966   -13.350 46.838  1.00 43.54 ? 760 HOH   A O   1 
HETATM 3064 O  O   . HOH   D 4 .   ? 0.254   12.255  50.564  1.00 45.05 ? 761 HOH   A O   1 
HETATM 3065 O  O   . HOH   D 4 .   ? 4.257   -24.204 58.444  1.00 45.69 ? 762 HOH   A O   1 
HETATM 3066 O  O   . HOH   D 4 .   ? 1.113   15.131  61.252  1.00 30.39 ? 763 HOH   A O   1 
HETATM 3067 O  O   . HOH   D 4 .   ? 18.269  -1.051  63.364  1.00 41.01 ? 764 HOH   A O   1 
HETATM 3068 O  O   . HOH   D 4 .   ? -9.795  -7.126  80.010  1.00 54.49 ? 765 HOH   A O   1 
HETATM 3069 O  O   . HOH   D 4 .   ? 4.621   -8.958  93.595  1.00 55.39 ? 766 HOH   A O   1 
HETATM 3070 O  O   . HOH   D 4 .   ? -18.722 11.718  102.907 1.00 54.33 ? 767 HOH   A O   1 
HETATM 3071 O  O   . HOH   D 4 .   ? 7.022   -10.962 93.633  1.00 58.91 ? 768 HOH   A O   1 
HETATM 3072 O  O   . HOH   D 4 .   ? -3.706  -22.070 79.613  1.00 26.23 ? 769 HOH   A O   1 
HETATM 3073 O  O   . HOH   D 4 .   ? 5.470   -21.164 77.501  1.00 36.98 ? 770 HOH   A O   1 
HETATM 3074 O  O   . HOH   D 4 .   ? -4.164  -22.617 82.515  1.00 33.04 ? 771 HOH   A O   1 
HETATM 3075 O  O   . HOH   D 4 .   ? -7.770  -5.898  79.742  1.00 42.73 ? 772 HOH   A O   1 
HETATM 3076 O  O   . HOH   D 4 .   ? 9.233   -2.286  90.796  1.00 46.69 ? 773 HOH   A O   1 
# 
