data_8XUG
# 
_entry.id   8XUG 
# 
_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   8XUG         pdb_00008xug 10.2210/pdb8xug/pdb 
WWPDB D_1300044224 ?            ?                   
# 
_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                        8XUG 
_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-YH21831 complex' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dong, J.'    1 ? 
primary 'Lin, H.-Y.'  2 ? 
primary 'Yang, G.-F.' 3 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '4-hydroxyphenylpyruvate dioxygenase' 45952.727 1  1.13.11.27 ? ? ? 
2 non-polymer syn 'COBALT (II) ION' 58.933    1  ?          ? ? ? 
3 non-polymer syn 
'1-methyl-6-nitro-7-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-3-[2,2,2-tris(fluoranyl)ethyl]quinazoline-2,4-dione' 
441.315   1  ?          ? ? ? 
4 water       nat water 18.015    99 ?          ? ? ? 
# 
_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 '1-methyl-6-nitro-7-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-3-[2,2,2-tris(fluoranyl)ethyl]quinazoline-2,4-dione' 
A1LW7 
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 
A1LW7 non-polymer         . 
'1-methyl-6-nitro-7-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-3-[2,2,2-tris(fluoranyl)ethyl]quinazoline-2,4-dione' ? 
'C18 H14 F3 N3 O7' 441.315 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'       133.103 
CO    non-polymer         . 'COBALT (II) ION' ? 'Co 2'             58.933  
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'       75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER ? 'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   29  ?   ?   ?   A . n 
A 1 2   SER 2   30  ?   ?   ?   A . n 
A 1 3   HIS 3   31  ?   ?   ?   A . n 
A 1 4   MET 4   32  ?   ?   ?   A . n 
A 1 5   VAL 5   33  ?   ?   ?   A . n 
A 1 6   ARG 6   34  ?   ?   ?   A . n 
A 1 7   LYS 7   35  35  LYS LYS A . n 
A 1 8   ASN 8   36  36  ASN ASN A . n 
A 1 9   PRO 9   37  37  PRO PRO A . n 
A 1 10  LYS 10  38  38  LYS LYS A . n 
A 1 11  SER 11  39  39  SER SER A . n 
A 1 12  ASP 12  40  40  ASP ASP A . n 
A 1 13  LYS 13  41  41  LYS LYS A . n 
A 1 14  PHE 14  42  42  PHE PHE A . n 
A 1 15  LYS 15  43  43  LYS LYS A . n 
A 1 16  VAL 16  44  44  VAL VAL A . n 
A 1 17  LYS 17  45  45  LYS LYS A . n 
A 1 18  ARG 18  46  46  ARG ARG A . n 
A 1 19  PHE 19  47  47  PHE PHE A . n 
A 1 20  HIS 20  48  48  HIS HIS A . n 
A 1 21  HIS 21  49  49  HIS HIS A . n 
A 1 22  ILE 22  50  50  ILE ILE A . n 
A 1 23  GLU 23  51  51  GLU GLU A . n 
A 1 24  PHE 24  52  52  PHE PHE A . n 
A 1 25  TRP 25  53  53  TRP TRP A . n 
A 1 26  CYS 26  54  54  CYS CYS A . n 
A 1 27  GLY 27  55  55  GLY GLY A . n 
A 1 28  ASP 28  56  56  ASP ASP A . n 
A 1 29  ALA 29  57  57  ALA ALA A . n 
A 1 30  THR 30  58  58  THR THR A . n 
A 1 31  ASN 31  59  59  ASN ASN A . n 
A 1 32  VAL 32  60  60  VAL VAL A . n 
A 1 33  ALA 33  61  61  ALA ALA A . n 
A 1 34  ARG 34  62  62  ARG ARG A . n 
A 1 35  ARG 35  63  63  ARG ARG A . n 
A 1 36  PHE 36  64  64  PHE PHE A . n 
A 1 37  SER 37  65  65  SER SER A . n 
A 1 38  TRP 38  66  66  TRP TRP A . n 
A 1 39  GLY 39  67  67  GLY GLY A . n 
A 1 40  LEU 40  68  68  LEU LEU A . n 
A 1 41  GLY 41  69  69  GLY GLY A . n 
A 1 42  MET 42  70  70  MET MET A . n 
A 1 43  ARG 43  71  71  ARG ARG A . n 
A 1 44  PHE 44  72  72  PHE PHE A . n 
A 1 45  SER 45  73  73  SER SER A . n 
A 1 46  ALA 46  74  74  ALA ALA A . n 
A 1 47  LYS 47  75  75  LYS LYS A . n 
A 1 48  SER 48  76  76  SER SER A . n 
A 1 49  ASP 49  77  77  ASP ASP A . n 
A 1 50  LEU 50  78  78  LEU LEU A . n 
A 1 51  SER 51  79  79  SER SER A . n 
A 1 52  THR 52  80  80  THR THR A . n 
A 1 53  GLY 53  81  81  GLY GLY A . n 
A 1 54  ASN 54  82  82  ASN ASN A . n 
A 1 55  MET 55  83  83  MET MET A . n 
A 1 56  VAL 56  84  84  VAL VAL A . n 
A 1 57  HIS 57  85  85  HIS HIS A . n 
A 1 58  ALA 58  86  86  ALA ALA A . n 
A 1 59  SER 59  87  87  SER SER A . n 
A 1 60  TYR 60  88  88  TYR TYR A . n 
A 1 61  LEU 61  89  89  LEU LEU A . n 
A 1 62  LEU 62  90  90  LEU LEU A . n 
A 1 63  THR 63  91  91  THR THR A . n 
A 1 64  SER 64  92  92  SER SER A . n 
A 1 65  GLY 65  93  93  GLY GLY A . n 
A 1 66  ASP 66  94  94  ASP ASP A . n 
A 1 67  LEU 67  95  95  LEU LEU A . n 
A 1 68  ARG 68  96  96  ARG ARG A . n 
A 1 69  PHE 69  97  97  PHE PHE A . n 
A 1 70  LEU 70  98  98  LEU LEU A . n 
A 1 71  PHE 71  99  99  PHE PHE A . n 
A 1 72  THR 72  100 100 THR THR A . n 
A 1 73  ALA 73  101 101 ALA ALA A . n 
A 1 74  PRO 74  102 102 PRO PRO A . n 
A 1 75  TYR 75  103 103 TYR TYR A . n 
A 1 76  SER 76  104 104 SER SER A . n 
A 1 77  PRO 77  105 105 PRO PRO A . n 
A 1 78  SER 78  106 106 SER SER A . n 
A 1 79  LEU 79  107 107 LEU LEU A . n 
A 1 80  SER 80  108 108 SER SER A . n 
A 1 81  ALA 81  109 109 ALA ALA A . n 
A 1 82  GLY 82  110 110 GLY GLY A . n 
A 1 83  GLU 83  111 111 GLU GLU A . n 
A 1 84  ILE 84  112 112 ILE ILE A . n 
A 1 85  LYS 85  113 113 LYS LYS A . n 
A 1 86  PRO 86  114 114 PRO PRO A . n 
A 1 87  THR 87  115 115 THR THR A . n 
A 1 88  THR 88  116 116 THR THR A . n 
A 1 89  THR 89  117 117 THR THR A . n 
A 1 90  ALA 90  118 118 ALA ALA A . n 
A 1 91  SER 91  119 119 SER SER A . n 
A 1 92  ILE 92  120 120 ILE ILE A . n 
A 1 93  PRO 93  121 121 PRO PRO A . n 
A 1 94  SER 94  122 122 SER SER A . n 
A 1 95  PHE 95  123 123 PHE PHE A . n 
A 1 96  ASP 96  124 124 ASP ASP A . n 
A 1 97  HIS 97  125 125 HIS HIS A . n 
A 1 98  GLY 98  126 126 GLY GLY A . n 
A 1 99  SER 99  127 127 SER SER A . n 
A 1 100 CYS 100 128 128 CYS CYS A . n 
A 1 101 ARG 101 129 129 ARG ARG A . n 
A 1 102 SER 102 130 130 SER SER A . n 
A 1 103 PHE 103 131 131 PHE PHE A . n 
A 1 104 PHE 104 132 132 PHE PHE A . n 
A 1 105 SER 105 133 133 SER SER A . n 
A 1 106 SER 106 134 134 SER SER A . n 
A 1 107 HIS 107 135 135 HIS HIS A . n 
A 1 108 GLY 108 136 136 GLY GLY A . n 
A 1 109 LEU 109 137 137 LEU LEU A . n 
A 1 110 GLY 110 138 138 GLY GLY A . n 
A 1 111 VAL 111 139 139 VAL VAL A . n 
A 1 112 ARG 112 140 140 ARG ARG A . n 
A 1 113 ALA 113 141 141 ALA ALA A . n 
A 1 114 VAL 114 142 142 VAL VAL A . n 
A 1 115 ALA 115 143 143 ALA ALA A . n 
A 1 116 ILE 116 144 144 ILE ILE A . n 
A 1 117 GLU 117 145 145 GLU GLU A . n 
A 1 118 VAL 118 146 146 VAL VAL A . n 
A 1 119 GLU 119 147 147 GLU GLU A . n 
A 1 120 ASP 120 148 148 ASP ASP A . n 
A 1 121 ALA 121 149 149 ALA ALA A . n 
A 1 122 GLU 122 150 150 GLU GLU A . n 
A 1 123 SER 123 151 151 SER SER A . n 
A 1 124 ALA 124 152 152 ALA ALA A . n 
A 1 125 PHE 125 153 153 PHE PHE A . n 
A 1 126 SER 126 154 154 SER SER A . n 
A 1 127 ILE 127 155 155 ILE ILE A . n 
A 1 128 SER 128 156 156 SER SER A . n 
A 1 129 VAL 129 157 157 VAL VAL A . n 
A 1 130 ALA 130 158 158 ALA ALA A . n 
A 1 131 ASN 131 159 159 ASN ASN A . n 
A 1 132 GLY 132 160 160 GLY GLY A . n 
A 1 133 ALA 133 161 161 ALA ALA A . n 
A 1 134 ILE 134 162 162 ILE ILE A . n 
A 1 135 PRO 135 163 163 PRO PRO A . n 
A 1 136 SER 136 164 164 SER SER A . n 
A 1 137 SER 137 165 165 SER SER A . n 
A 1 138 PRO 138 166 166 PRO PRO A . n 
A 1 139 PRO 139 167 167 PRO PRO A . n 
A 1 140 ILE 140 168 168 ILE ILE A . n 
A 1 141 VAL 141 169 169 VAL VAL A . n 
A 1 142 LEU 142 170 170 LEU LEU A . n 
A 1 143 ASN 143 171 171 ASN ASN A . n 
A 1 144 GLU 144 172 172 GLU GLU A . n 
A 1 145 ALA 145 173 173 ALA ALA A . n 
A 1 146 VAL 146 174 174 VAL VAL A . n 
A 1 147 THR 147 175 175 THR THR A . n 
A 1 148 ILE 148 176 176 ILE ILE A . n 
A 1 149 ALA 149 177 177 ALA ALA A . n 
A 1 150 GLU 150 178 178 GLU GLU A . n 
A 1 151 VAL 151 179 179 VAL VAL A . n 
A 1 152 LYS 152 180 180 LYS LYS A . n 
A 1 153 LEU 153 181 181 LEU LEU A . n 
A 1 154 TYR 154 182 182 TYR TYR A . n 
A 1 155 GLY 155 183 183 GLY GLY A . n 
A 1 156 ASP 156 184 184 ASP ASP A . n 
A 1 157 VAL 157 185 185 VAL VAL A . n 
A 1 158 VAL 158 186 186 VAL VAL A . n 
A 1 159 LEU 159 187 187 LEU LEU A . n 
A 1 160 ARG 160 188 188 ARG ARG A . n 
A 1 161 TYR 161 189 189 TYR TYR A . n 
A 1 162 VAL 162 190 190 VAL VAL A . n 
A 1 163 SER 163 191 191 SER SER A . n 
A 1 164 TYR 164 192 192 TYR TYR A . n 
A 1 165 LYS 165 193 193 LYS LYS A . n 
A 1 166 ALA 166 194 194 ALA ALA A . n 
A 1 167 GLU 167 195 ?   ?   ?   A . n 
A 1 168 ASP 168 196 ?   ?   ?   A . n 
A 1 169 THR 169 197 ?   ?   ?   A . n 
A 1 170 GLU 170 198 ?   ?   ?   A . n 
A 1 171 LYS 171 199 ?   ?   ?   A . n 
A 1 172 SER 172 200 ?   ?   ?   A . n 
A 1 173 GLU 173 201 201 GLU GLU A . n 
A 1 174 PHE 174 202 202 PHE PHE A . n 
A 1 175 LEU 175 203 203 LEU LEU A . n 
A 1 176 PRO 176 204 204 PRO PRO A . n 
A 1 177 GLY 177 205 205 GLY GLY A . n 
A 1 178 PHE 178 206 206 PHE PHE A . n 
A 1 179 GLU 179 207 207 GLU GLU A . n 
A 1 180 ARG 180 208 208 ARG ARG A . n 
A 1 181 VAL 181 209 209 VAL VAL A . n 
A 1 182 GLU 182 210 210 GLU GLU A . n 
A 1 183 ASP 183 211 211 ASP ASP A . n 
A 1 184 ALA 184 212 212 ALA ALA A . n 
A 1 185 SER 185 213 213 SER SER A . n 
A 1 186 SER 186 214 214 SER SER A . n 
A 1 187 PHE 187 215 215 PHE PHE A . n 
A 1 188 PRO 188 216 216 PRO PRO A . n 
A 1 189 LEU 189 217 217 LEU LEU A . n 
A 1 190 ASP 190 218 218 ASP ASP A . n 
A 1 191 TYR 191 219 219 TYR TYR A . n 
A 1 192 GLY 192 220 220 GLY GLY A . n 
A 1 193 ILE 193 221 221 ILE ILE A . n 
A 1 194 ARG 194 222 222 ARG ARG A . n 
A 1 195 ARG 195 223 223 ARG ARG A . n 
A 1 196 LEU 196 224 224 LEU LEU A . n 
A 1 197 ASP 197 225 225 ASP ASP A . n 
A 1 198 HIS 198 226 226 HIS HIS A . n 
A 1 199 ALA 199 227 227 ALA ALA A . n 
A 1 200 VAL 200 228 228 VAL VAL A . n 
A 1 201 GLY 201 229 229 GLY GLY A . n 
A 1 202 ASN 202 230 230 ASN ASN A . n 
A 1 203 VAL 203 231 231 VAL VAL A . n 
A 1 204 PRO 204 232 232 PRO PRO A . n 
A 1 205 GLU 205 233 233 GLU GLU A . n 
A 1 206 LEU 206 234 234 LEU LEU A . n 
A 1 207 GLY 207 235 235 GLY GLY A . n 
A 1 208 PRO 208 236 236 PRO PRO A . n 
A 1 209 ALA 209 237 237 ALA ALA A . n 
A 1 210 LEU 210 238 238 LEU LEU A . n 
A 1 211 THR 211 239 239 THR THR A . n 
A 1 212 TYR 212 240 240 TYR TYR A . n 
A 1 213 VAL 213 241 241 VAL VAL A . n 
A 1 214 ALA 214 242 242 ALA ALA A . n 
A 1 215 GLY 215 243 243 GLY GLY A . n 
A 1 216 PHE 216 244 244 PHE PHE A . n 
A 1 217 THR 217 245 245 THR THR A . n 
A 1 218 GLY 218 246 246 GLY GLY A . n 
A 1 219 PHE 219 247 247 PHE PHE A . n 
A 1 220 HIS 220 248 248 HIS HIS A . n 
A 1 221 GLN 221 249 249 GLN GLN A . n 
A 1 222 PHE 222 250 250 PHE PHE A . n 
A 1 223 ALA 223 251 251 ALA ALA A . n 
A 1 224 GLU 224 252 252 GLU GLU A . n 
A 1 225 PHE 225 253 253 PHE PHE A . n 
A 1 226 THR 226 254 ?   ?   ?   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 A1LW7 1  502 1  A1LW7 LIG A . 
D 4 HOH   1  601 11 HOH   HOH A . 
D 4 HOH   2  602 95 HOH   HOH A . 
D 4 HOH   3  603 46 HOH   HOH A . 
D 4 HOH   4  604 83 HOH   HOH A . 
D 4 HOH   5  605 76 HOH   HOH A . 
D 4 HOH   6  606 48 HOH   HOH A . 
D 4 HOH   7  607 55 HOH   HOH A . 
D 4 HOH   8  608 70 HOH   HOH A . 
D 4 HOH   9  609 54 HOH   HOH A . 
D 4 HOH   10 610 88 HOH   HOH A . 
D 4 HOH   11 611 3  HOH   HOH A . 
D 4 HOH   12 612 44 HOH   HOH A . 
D 4 HOH   13 613 4  HOH   HOH A . 
D 4 HOH   14 614 36 HOH   HOH A . 
D 4 HOH   15 615 64 HOH   HOH A . 
D 4 HOH   16 616 32 HOH   HOH A . 
D 4 HOH   17 617 52 HOH   HOH A . 
D 4 HOH   18 618 79 HOH   HOH A . 
D 4 HOH   19 619 12 HOH   HOH A . 
D 4 HOH   20 620 9  HOH   HOH A . 
D 4 HOH   21 621 26 HOH   HOH A . 
D 4 HOH   22 622 5  HOH   HOH A . 
D 4 HOH   23 623 10 HOH   HOH A . 
D 4 HOH   24 624 25 HOH   HOH A . 
D 4 HOH   25 625 16 HOH   HOH A . 
D 4 HOH   26 626 34 HOH   HOH A . 
D 4 HOH   27 627 92 HOH   HOH A . 
D 4 HOH   28 628 6  HOH   HOH A . 
D 4 HOH   29 629 1  HOH   HOH A . 
D 4 HOH   30 630 73 HOH   HOH A . 
D 4 HOH   31 631 68 HOH   HOH A . 
D 4 HOH   32 632 86 HOH   HOH A . 
D 4 HOH   33 633 38 HOH   HOH A . 
D 4 HOH   34 634 18 HOH   HOH A . 
D 4 HOH   35 635 13 HOH   HOH A . 
D 4 HOH   36 636 50 HOH   HOH A . 
D 4 HOH   37 637 67 HOH   HOH A . 
D 4 HOH   38 638 77 HOH   HOH A . 
D 4 HOH   39 639 43 HOH   HOH A . 
D 4 HOH   40 640 87 HOH   HOH A . 
D 4 HOH   41 641 98 HOH   HOH A . 
D 4 HOH   42 642 20 HOH   HOH A . 
D 4 HOH   43 643 24 HOH   HOH A . 
D 4 HOH   44 644 19 HOH   HOH A . 
D 4 HOH   45 645 56 HOH   HOH A . 
D 4 HOH   46 646 69 HOH   HOH A . 
D 4 HOH   47 647 35 HOH   HOH A . 
D 4 HOH   48 648 21 HOH   HOH A . 
D 4 HOH   49 649 75 HOH   HOH A . 
D 4 HOH   50 650 28 HOH   HOH A . 
D 4 HOH   51 651 23 HOH   HOH A . 
D 4 HOH   52 652 47 HOH   HOH A . 
D 4 HOH   53 653 29 HOH   HOH A . 
D 4 HOH   54 654 84 HOH   HOH A . 
D 4 HOH   55 655 49 HOH   HOH A . 
D 4 HOH   56 656 45 HOH   HOH A . 
D 4 HOH   57 657 31 HOH   HOH A . 
D 4 HOH   58 658 71 HOH   HOH A . 
D 4 HOH   59 659 63 HOH   HOH A . 
D 4 HOH   60 660 65 HOH   HOH A . 
D 4 HOH   61 661 57 HOH   HOH A . 
D 4 HOH   62 662 30 HOH   HOH A . 
D 4 HOH   63 663 96 HOH   HOH A . 
D 4 HOH   64 664 97 HOH   HOH A . 
D 4 HOH   65 665 66 HOH   HOH A . 
D 4 HOH   66 666 22 HOH   HOH A . 
D 4 HOH   67 667 14 HOH   HOH A . 
D 4 HOH   68 668 17 HOH   HOH A . 
D 4 HOH   69 669 8  HOH   HOH A . 
D 4 HOH   70 670 33 HOH   HOH A . 
D 4 HOH   71 671 42 HOH   HOH A . 
D 4 HOH   72 672 7  HOH   HOH A . 
D 4 HOH   73 673 58 HOH   HOH A . 
D 4 HOH   74 674 41 HOH   HOH A . 
D 4 HOH   75 675 15 HOH   HOH A . 
D 4 HOH   76 676 80 HOH   HOH A . 
D 4 HOH   77 677 51 HOH   HOH A . 
D 4 HOH   78 678 40 HOH   HOH A . 
D 4 HOH   79 679 37 HOH   HOH A . 
D 4 HOH   80 680 78 HOH   HOH A . 
D 4 HOH   81 681 39 HOH   HOH A . 
D 4 HOH   82 682 94 HOH   HOH A . 
D 4 HOH   83 683 53 HOH   HOH A . 
D 4 HOH   84 684 82 HOH   HOH A . 
D 4 HOH   85 685 81 HOH   HOH A . 
D 4 HOH   86 686 59 HOH   HOH A . 
D 4 HOH   87 687 27 HOH   HOH A . 
D 4 HOH   88 688 61 HOH   HOH A . 
D 4 HOH   89 689 89 HOH   HOH A . 
D 4 HOH   90 690 72 HOH   HOH A . 
D 4 HOH   91 691 2  HOH   HOH A . 
D 4 HOH   92 692 74 HOH   HOH A . 
D 4 HOH   93 693 62 HOH   HOH A . 
D 4 HOH   94 694 85 HOH   HOH A . 
D 4 HOH   95 695 60 HOH   HOH A . 
D 4 HOH   96 696 90 HOH   HOH A . 
D 4 HOH   97 697 91 HOH   HOH A . 
D 4 HOH   98 698 99 HOH   HOH A . 
D 4 HOH   99 699 93 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 35  ? CG  ? A LYS 7   CG  
2  1 Y 1 A LYS 35  ? CD  ? A LYS 7   CD  
3  1 Y 1 A LYS 35  ? CE  ? A LYS 7   CE  
4  1 Y 1 A LYS 35  ? NZ  ? A LYS 7   NZ  
5  1 Y 1 A LYS 43  ? CG  ? A LYS 15  CG  
6  1 Y 1 A LYS 43  ? CD  ? A LYS 15  CD  
7  1 Y 1 A LYS 43  ? CE  ? A LYS 15  CE  
8  1 Y 1 A LYS 43  ? NZ  ? A LYS 15  NZ  
9  1 Y 1 A LYS 193 ? CG  ? A LYS 165 CG  
10 1 Y 1 A LYS 193 ? CD  ? A LYS 165 CD  
11 1 Y 1 A LYS 193 ? CE  ? A LYS 165 CE  
12 1 Y 1 A LYS 193 ? NZ  ? A LYS 165 NZ  
13 1 Y 1 A GLU 201 ? CG  ? A GLU 173 CG  
14 1 Y 1 A GLU 201 ? CD  ? A GLU 173 CD  
15 1 Y 1 A GLU 201 ? OE1 ? A GLU 173 OE1 
16 1 Y 1 A GLU 201 ? OE2 ? A GLU 173 OE2 
17 1 Y 1 A GLU 210 ? CG  ? A GLU 182 CG  
18 1 Y 1 A GLU 210 ? CD  ? A GLU 182 CD  
19 1 Y 1 A GLU 210 ? OE1 ? A GLU 182 OE1 
20 1 Y 1 A GLU 210 ? OE2 ? A GLU 182 OE2 
21 1 Y 1 A ASP 211 ? CG  ? A ASP 183 CG  
22 1 Y 1 A ASP 211 ? OD1 ? A ASP 183 OD1 
23 1 Y 1 A ASP 211 ? OD2 ? A ASP 183 OD2 
24 1 Y 1 A PHE 253 ? CG  ? A PHE 225 CG  
25 1 Y 1 A PHE 253 ? CD1 ? A PHE 225 CD1 
26 1 Y 1 A PHE 253 ? CD2 ? A PHE 225 CD2 
27 1 Y 1 A PHE 253 ? CE1 ? A PHE 225 CE1 
28 1 Y 1 A PHE 253 ? CE2 ? A PHE 225 CE2 
29 1 Y 1 A PHE 253 ? CZ  ? A PHE 225 CZ  
30 1 Y 1 A GLU 262 ? CG  ? A GLU 234 CG  
31 1 Y 1 A GLU 262 ? CD  ? A GLU 234 CD  
32 1 Y 1 A GLU 262 ? OE1 ? A GLU 234 OE1 
33 1 Y 1 A GLU 262 ? OE2 ? A GLU 234 OE2 
34 1 Y 1 A LYS 289 ? CG  ? A LYS 261 CG  
35 1 Y 1 A LYS 289 ? CD  ? A LYS 261 CD  
36 1 Y 1 A LYS 289 ? CE  ? A LYS 261 CE  
37 1 Y 1 A LYS 289 ? NZ  ? A LYS 261 NZ  
38 1 Y 1 A ARG 290 ? CG  ? A ARG 262 CG  
39 1 Y 1 A ARG 290 ? CD  ? A ARG 262 CD  
40 1 Y 1 A ARG 290 ? NE  ? A ARG 262 NE  
41 1 Y 1 A ARG 290 ? CZ  ? A ARG 262 CZ  
42 1 Y 1 A ARG 290 ? NH1 ? A ARG 262 NH1 
43 1 Y 1 A ARG 290 ? NH2 ? A ARG 262 NH2 
44 1 Y 1 A GLN 344 ? CG  ? A GLN 316 CG  
45 1 Y 1 A GLN 344 ? CD  ? A GLN 316 CD  
46 1 Y 1 A GLN 344 ? OE1 ? A GLN 316 OE1 
47 1 Y 1 A GLN 344 ? NE2 ? A GLN 316 NE2 
48 1 Y 1 A LYS 347 ? CG  ? A LYS 319 CG  
49 1 Y 1 A LYS 347 ? CD  ? A LYS 319 CD  
50 1 Y 1 A LYS 347 ? CE  ? A LYS 319 CE  
51 1 Y 1 A LYS 347 ? NZ  ? A LYS 319 NZ  
52 1 Y 1 A LYS 348 ? CG  ? A LYS 320 CG  
53 1 Y 1 A LYS 348 ? CD  ? A LYS 320 CD  
54 1 Y 1 A LYS 348 ? CE  ? A LYS 320 CE  
55 1 Y 1 A LYS 348 ? NZ  ? A LYS 320 NZ  
56 1 Y 1 A ASP 357 ? CG  ? A ASP 329 CG  
57 1 Y 1 A ASP 357 ? OD1 ? A ASP 329 OD1 
58 1 Y 1 A ASP 357 ? OD2 ? A ASP 329 OD2 
59 1 Y 1 A LYS 360 ? CG  ? A LYS 332 CG  
60 1 Y 1 A LYS 360 ? CD  ? A LYS 332 CD  
61 1 Y 1 A LYS 360 ? CE  ? A LYS 332 CE  
62 1 Y 1 A LYS 360 ? NZ  ? A LYS 332 NZ  
63 1 Y 1 A GLU 364 ? CG  ? A GLU 336 CG  
64 1 Y 1 A GLU 364 ? CD  ? A GLU 336 CD  
65 1 Y 1 A GLU 364 ? OE1 ? A GLU 336 OE1 
66 1 Y 1 A GLU 364 ? OE2 ? A GLU 336 OE2 
67 1 Y 1 A PHE 428 ? CG  ? A PHE 400 CG  
68 1 Y 1 A PHE 428 ? CD1 ? A PHE 400 CD1 
69 1 Y 1 A PHE 428 ? CD2 ? A PHE 400 CD2 
70 1 Y 1 A PHE 428 ? CE1 ? A PHE 400 CE1 
71 1 Y 1 A PHE 428 ? CE2 ? A PHE 400 CE2 
72 1 Y 1 A PHE 428 ? CZ  ? A PHE 400 CZ  
73 1 Y 1 A ILE 431 ? CG1 ? A ILE 403 CG1 
74 1 Y 1 A ILE 431 ? CG2 ? A ILE 403 CG2 
75 1 Y 1 A ILE 431 ? CD1 ? A ILE 403 CD1 
76 1 Y 1 A GLU 432 ? CG  ? A GLU 404 CG  
77 1 Y 1 A GLU 432 ? CD  ? A GLU 404 CD  
78 1 Y 1 A GLU 432 ? OE1 ? A GLU 404 OE1 
79 1 Y 1 A GLU 432 ? OE2 ? A GLU 404 OE2 
80 1 Y 1 A GLU 433 ? CG  ? A GLU 405 CG  
81 1 Y 1 A GLU 433 ? CD  ? A GLU 405 CD  
82 1 Y 1 A GLU 433 ? OE1 ? A GLU 405 OE1 
83 1 Y 1 A GLU 433 ? OE2 ? A GLU 405 OE2 
84 1 Y 1 A GLU 435 ? CG  ? A GLU 407 CG  
85 1 Y 1 A GLU 435 ? CD  ? A GLU 407 CD  
86 1 Y 1 A GLU 435 ? OE1 ? A GLU 407 OE1 
87 1 Y 1 A GLU 435 ? OE2 ? A GLU 407 OE2 
88 1 Y 1 A LYS 436 ? CG  ? A LYS 408 CG  
89 1 Y 1 A LYS 436 ? CD  ? A LYS 408 CD  
90 1 Y 1 A LYS 436 ? CE  ? A LYS 408 CE  
91 1 Y 1 A LYS 436 ? NZ  ? A LYS 408 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.10.1_2155: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   100.43 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XUG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.602 
_cell.length_a_esd                 ? 
_cell.length_b                     84.076 
_cell.length_b_esd                 ? 
_cell.length_c                     64.749 
_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                         8XUG 
_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                   8XUG 
_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             2.46 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.07 
_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         2022-05-10 
_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                                       8XUG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.893 
_reflns.d_resolution_low                               45.396 
_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                                     31881 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.81 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.12 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.04 
_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                                   0.988 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.893 
_reflns_shell.d_res_low                                     2.01 
_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                             8889 
_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                                  0.939 
_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                                 8XUG 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.893 
_refine.ls_d_res_low                             45.396 
_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                     31881 
_refine.ls_number_reflns_R_free                  1595 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.81 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2209 
_refine.ls_R_factor_R_free                       0.2494 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2194 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 37.99 
_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                            0.24 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.893 
_refine_hist.d_res_low                        45.396 
_refine_hist.number_atoms_solvent             99 
_refine_hist.number_atoms_total               3008 
_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        2877 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_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  ? 2977 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.962  ? 4042 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.181 ? 1750 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 441  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 527  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.8932 1.9543 . . 139 2627 94.00  . . . . 0.3899 . . . . . . . . . . . 0.4338 
'X-RAY DIFFRACTION' 1.9543 2.0242 . . 140 2672 95.00  . . . . 0.3272 . . . . . . . . . . . 0.3352 
'X-RAY DIFFRACTION' 2.0242 2.1052 . . 141 2693 97.00  . . . . 0.2906 . . . . . . . . . . . 0.3538 
'X-RAY DIFFRACTION' 2.1052 2.2010 . . 144 2732 97.00  . . . . 0.2783 . . . . . . . . . . . 0.3553 
'X-RAY DIFFRACTION' 2.2010 2.3171 . . 145 2737 98.00  . . . . 0.2587 . . . . . . . . . . . 0.3195 
'X-RAY DIFFRACTION' 2.3171 2.4622 . . 146 2767 99.00  . . . . 0.2297 . . . . . . . . . . . 0.2864 
'X-RAY DIFFRACTION' 2.4622 2.6523 . . 145 2769 99.00  . . . . 0.2255 . . . . . . . . . . . 0.2255 
'X-RAY DIFFRACTION' 2.6523 2.9192 . . 146 2785 99.00  . . . . 0.2365 . . . . . . . . . . . 0.2699 
'X-RAY DIFFRACTION' 2.9192 3.3415 . . 149 2819 99.00  . . . . 0.2205 . . . . . . . . . . . 0.2549 
'X-RAY DIFFRACTION' 3.3415 4.2095 . . 148 2817 100.00 . . . . 0.1877 . . . . . . . . . . . 0.2187 
'X-RAY DIFFRACTION' 4.2095 8      . . 152 2868 99.00  . . . . 0.1840 . . . . . . . . . . . 0.2034 
# 
_struct.entry_id                     8XUG 
_struct.title                        'Crystal structure of AtHPPD-YH21831 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        8XUG 
_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              8XUG 
_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 8XUG GLY A 1 ? UNP P93836 ? ? 'expression tag' 29 1 
1 8XUG SER A 2 ? UNP P93836 ? ? 'expression tag' 30 2 
1 8XUG HIS A 3 ? UNP P93836 ? ? 'expression tag' 31 3 
1 8XUG 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         -37   ? 
1 'SSA (A^2)'  28370 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 2_557 -x,y,-z+2 -1.0000000000 0.0000000000 0.0000000000 -23.4435561221 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 127.3582807687 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 28  ? GLY A 41  ? ASP A 56  GLY A 69  1 ? 14 
HELX_P HELX_P2  AA2 ASP A 49  ? GLY A 53  ? ASP A 77  GLY A 81  5 ? 5  
HELX_P HELX_P3  AA3 SER A 76  ? ALA A 81  ? SER A 104 ALA A 109 5 ? 6  
HELX_P HELX_P4  AA4 ILE A 84  ? THR A 88  ? ILE A 112 THR A 116 5 ? 5  
HELX_P HELX_P5  AA5 ASP A 96  ? GLY A 108 ? ASP A 124 GLY A 136 1 ? 13 
HELX_P HELX_P6  AA6 ASP A 120 ? ASN A 131 ? ASP A 148 ASN A 159 1 ? 12 
HELX_P HELX_P7  AA7 GLU A 205 ? GLY A 218 ? GLU A 233 GLY A 246 1 ? 14 
HELX_P HELX_P8  AA8 SER A 264 ? ASN A 273 ? SER A 292 ASN A 301 1 ? 10 
HELX_P HELX_P9  AA9 ASP A 287 ? ARG A 298 ? ASP A 315 ARG A 326 1 ? 12 
HELX_P HELX_P10 AB1 SER A 299 ? GLY A 302 ? SER A 327 GLY A 330 5 ? 4  
HELX_P HELX_P11 AB2 PRO A 311 ? GLN A 316 ? PRO A 339 GLN A 344 1 ? 6  
HELX_P HELX_P12 AB3 LEU A 318 ? GLY A 323 ? LEU A 346 GLY A 351 1 ? 6  
HELX_P HELX_P13 AB4 SER A 327 ? GLY A 338 ? SER A 355 GLY A 366 1 ? 12 
HELX_P HELX_P14 AB5 GLY A 394 ? LYS A 408 ? GLY A 422 LYS A 436 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 373 SG  ? ? ? 1_555 A CYS   388 SG  ? ? A CYS 401 A CYS   416 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc1 metalc ? ? A HIS 198 NE2 ? ? ? 1_555 B CO    .   CO  ? ? A HIS 226 A CO    501 1_555 ? ? ? ? ? ? ? 2.456 ? ? 
metalc2 metalc ? ? A HIS 280 NE2 ? ? ? 1_555 B CO    .   CO  ? ? A HIS 308 A CO    501 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc3 metalc ? ? A GLU 366 OE1 ? ? ? 1_555 B CO    .   CO  ? ? A GLU 394 A CO    501 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc4 metalc ? ? B CO  .   CO  ? ? ? 1_555 C A1LW7 .   O09 ? ? A CO  501 A A1LW7 502 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc5 metalc ? ? B CO  .   CO  ? ? ? 1_555 C A1LW7 .   O15 ? ? A CO  501 A A1LW7 502 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
metalc6 metalc ? ? B CO  .   CO  ? ? ? 1_555 D HOH   .   O   ? ? A CO  501 A HOH   629 1_555 ? ? ? ? ? ? ? 2.313 ? ? 
# 
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 96.7  ? 
2  NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 OE1 ? A GLU   366 ? A GLU   394 ? 1_555 87.9  ? 
3  NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 OE1 ? A GLU   366 ? A GLU   394 ? 1_555 86.7  ? 
4  NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O09 ? C A1LW7 .   ? A A1LW7 502 ? 1_555 163.2 ? 
5  NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O09 ? C A1LW7 .   ? A A1LW7 502 ? 1_555 91.9  ? 
6  OE1 ? A GLU   366 ? A GLU   394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O09 ? C A1LW7 .   ? A A1LW7 502 ? 1_555 107.0 ? 
7  NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O15 ? C A1LW7 .   ? A A1LW7 502 ? 1_555 91.4  ? 
8  NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O15 ? C A1LW7 .   ? A A1LW7 502 ? 1_555 94.3  ? 
9  OE1 ? A GLU   366 ? A GLU   394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O15 ? C A1LW7 .   ? A A1LW7 502 ? 1_555 178.9 ? 
10 O09 ? C A1LW7 .   ? A A1LW7 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O15 ? C A1LW7 .   ? A A1LW7 502 ? 1_555 73.6  ? 
11 NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   629 ? 1_555 90.4  ? 
12 NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   629 ? 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   629 ? 1_555 85.5  ? 
14 O09 ? C A1LW7 .   ? A A1LW7 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   629 ? 1_555 83.3  ? 
15 O15 ? C A1LW7 .   ? A A1LW7 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   629 ? 1_555 93.6  ? 
# 
_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 ALA A 115 ? O ALA A 143 N HIS A 20  ? N HIS A 48  
AA1 5 6 N PHE A 24  ? N PHE A 52  O LEU A 70  ? O LEU A 98  
AA1 6 7 O PHE A 69  ? O PHE A 97  N LEU A 62  ? N LEU A 90  
AA1 7 8 O LEU A 61  ? O LEU A 89  N ALA A 46  ? N ALA A 74  
AA1 8 9 N LYS A 47  ? N LYS A 75  O GLU A 179 ? O GLU A 207 
AA2 1 2 N HIS A 220 ? N HIS A 248 O ALA A 243 ? O ALA A 271 
AA2 2 3 N LEU A 242 ? N LEU A 270 O LEU A 251 ? O LEU A 279 
AA2 3 4 O ASN A 254 ? O ASN A 282 N GLY A 201 ? N GLY A 229 
AA2 4 5 N ARG A 194 ? N ARG A 222 O MET A 284 ? O MET A 312 
AA2 5 6 N LEU A 281 ? N LEU A 309 O GLU A 366 ? O GLU A 394 
AA2 6 7 O GLN A 369 ? O GLN A 397 N LEU A 350 ? N LEU A 378 
AA2 7 8 O GLN A 351 ? O GLN A 379 N LEU A 340 ? N LEU A 368 
# 
_pdbx_entry_details.entry_id                   8XUG 
_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  ? ? -99.38  -89.37  
2  1 ASP A 77  ? ? -165.74 -168.76 
3  1 GLU A 172 ? ? 55.06   18.09   
4  1 LEU A 181 ? ? -102.63 -60.71  
5  1 PRO A 216 ? ? -74.32  49.81   
6  1 ASP A 218 ? ? -163.94 116.79  
7  1 ALA A 251 ? ? 73.04   142.45  
8  1 GLU A 252 ? ? -108.14 -134.72 
9  1 ASP A 315 ? ? -162.03 82.23   
10 1 MET A 335 ? ? -47.80  156.04  
11 1 THR A 390 ? ? -126.13 -96.69  
# 
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 THR 254 ? A THR 226 
14 1 Y 1 A ALA 255 ? A ALA 227 
15 1 Y 1 A ASP 256 ? A ASP 228 
16 1 Y 1 A ASP 257 ? A ASP 229 
17 1 Y 1 A VAL 258 ? A VAL 230 
18 1 Y 1 A GLY 259 ? A GLY 231 
19 1 Y 1 A THR 260 ? A THR 232 
20 1 Y 1 A ALA 261 ? A ALA 233 
21 1 Y 1 A LYS 404 ? A LYS 376 
22 1 Y 1 A ASP 405 ? A ASP 377 
23 1 Y 1 A GLU 406 ? A GLU 378 
24 1 Y 1 A GLU 407 ? A GLU 379 
25 1 Y 1 A GLY 408 ? A GLY 380 
26 1 Y 1 A LYS 409 ? A LYS 381 
27 1 Y 1 A ALA 410 ? A ALA 382 
28 1 Y 1 A THR 437 ? A THR 409 
29 1 Y 1 A LEU 438 ? A LEU 410 
30 1 Y 1 A GLU 439 ? A GLU 411 
31 1 Y 1 A ALA 440 ? A ALA 412 
32 1 Y 1 A LYS 441 ? A LYS 413 
33 1 Y 1 A GLN 442 ? A GLN 414 
34 1 Y 1 A LEU 443 ? A LEU 415 
35 1 Y 1 A VAL 444 ? A VAL 416 
36 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 
A1LW7 C10  C  N N 1   
A1LW7 C13  C  N N 2   
A1LW7 C20  C  N N 3   
A1LW7 C24  C  N N 4   
A1LW7 C28  C  N N 5   
A1LW7 C01  C  Y N 6   
A1LW7 C02  C  Y N 7   
A1LW7 C03  C  Y N 8   
A1LW7 C04  C  Y N 9   
A1LW7 C05  C  Y N 10  
A1LW7 C06  C  Y N 11  
A1LW7 C07  C  N N 12  
A1LW7 C08  C  N N 13  
A1LW7 C11  C  N N 14  
A1LW7 C12  C  N N 15  
A1LW7 C14  C  N N 16  
A1LW7 C18  C  N N 17  
A1LW7 C23  C  N N 18  
A1LW7 F29  F  N N 19  
A1LW7 F30  F  N N 20  
A1LW7 F31  F  N N 21  
A1LW7 N17  N  N N 22  
A1LW7 N19  N  N N 23  
A1LW7 N25  N  N N 24  
A1LW7 O09  O  N N 25  
A1LW7 O15  O  N N 26  
A1LW7 O16  O  N N 27  
A1LW7 O21  O  N N 28  
A1LW7 O22  O  N N 29  
A1LW7 O26  O  N N 30  
A1LW7 O27  O  N N 31  
A1LW7 H1   H  N N 32  
A1LW7 H2   H  N N 33  
A1LW7 H3   H  N N 34  
A1LW7 H4   H  N N 35  
A1LW7 H5   H  N N 36  
A1LW7 H6   H  N N 37  
A1LW7 H7   H  N N 38  
A1LW7 H8   H  N N 39  
A1LW7 H9   H  N N 40  
A1LW7 H10  H  N N 41  
A1LW7 H11  H  N N 42  
A1LW7 H12  H  N N 43  
A1LW7 H13  H  N N 44  
A1LW7 H14  H  N N 45  
ALA   N    N  N N 46  
ALA   CA   C  N S 47  
ALA   C    C  N N 48  
ALA   O    O  N N 49  
ALA   CB   C  N N 50  
ALA   OXT  O  N N 51  
ALA   H    H  N N 52  
ALA   H2   H  N N 53  
ALA   HA   H  N N 54  
ALA   HB1  H  N N 55  
ALA   HB2  H  N N 56  
ALA   HB3  H  N N 57  
ALA   HXT  H  N N 58  
ARG   N    N  N N 59  
ARG   CA   C  N S 60  
ARG   C    C  N N 61  
ARG   O    O  N N 62  
ARG   CB   C  N N 63  
ARG   CG   C  N N 64  
ARG   CD   C  N N 65  
ARG   NE   N  N N 66  
ARG   CZ   C  N N 67  
ARG   NH1  N  N N 68  
ARG   NH2  N  N N 69  
ARG   OXT  O  N N 70  
ARG   H    H  N N 71  
ARG   H2   H  N N 72  
ARG   HA   H  N N 73  
ARG   HB2  H  N N 74  
ARG   HB3  H  N N 75  
ARG   HG2  H  N N 76  
ARG   HG3  H  N N 77  
ARG   HD2  H  N N 78  
ARG   HD3  H  N N 79  
ARG   HE   H  N N 80  
ARG   HH11 H  N N 81  
ARG   HH12 H  N N 82  
ARG   HH21 H  N N 83  
ARG   HH22 H  N N 84  
ARG   HXT  H  N N 85  
ASN   N    N  N N 86  
ASN   CA   C  N S 87  
ASN   C    C  N N 88  
ASN   O    O  N N 89  
ASN   CB   C  N N 90  
ASN   CG   C  N N 91  
ASN   OD1  O  N N 92  
ASN   ND2  N  N N 93  
ASN   OXT  O  N N 94  
ASN   H    H  N N 95  
ASN   H2   H  N N 96  
ASN   HA   H  N N 97  
ASN   HB2  H  N N 98  
ASN   HB3  H  N N 99  
ASN   HD21 H  N N 100 
ASN   HD22 H  N N 101 
ASN   HXT  H  N N 102 
ASP   N    N  N N 103 
ASP   CA   C  N S 104 
ASP   C    C  N N 105 
ASP   O    O  N N 106 
ASP   CB   C  N N 107 
ASP   CG   C  N N 108 
ASP   OD1  O  N N 109 
ASP   OD2  O  N N 110 
ASP   OXT  O  N N 111 
ASP   H    H  N N 112 
ASP   H2   H  N N 113 
ASP   HA   H  N N 114 
ASP   HB2  H  N N 115 
ASP   HB3  H  N N 116 
ASP   HD2  H  N N 117 
ASP   HXT  H  N N 118 
CO    CO   CO N N 119 
CYS   N    N  N N 120 
CYS   CA   C  N R 121 
CYS   C    C  N N 122 
CYS   O    O  N N 123 
CYS   CB   C  N N 124 
CYS   SG   S  N N 125 
CYS   OXT  O  N N 126 
CYS   H    H  N N 127 
CYS   H2   H  N N 128 
CYS   HA   H  N N 129 
CYS   HB2  H  N N 130 
CYS   HB3  H  N N 131 
CYS   HG   H  N N 132 
CYS   HXT  H  N N 133 
GLN   N    N  N N 134 
GLN   CA   C  N S 135 
GLN   C    C  N N 136 
GLN   O    O  N N 137 
GLN   CB   C  N N 138 
GLN   CG   C  N N 139 
GLN   CD   C  N N 140 
GLN   OE1  O  N N 141 
GLN   NE2  N  N N 142 
GLN   OXT  O  N N 143 
GLN   H    H  N N 144 
GLN   H2   H  N N 145 
GLN   HA   H  N N 146 
GLN   HB2  H  N N 147 
GLN   HB3  H  N N 148 
GLN   HG2  H  N N 149 
GLN   HG3  H  N N 150 
GLN   HE21 H  N N 151 
GLN   HE22 H  N N 152 
GLN   HXT  H  N N 153 
GLU   N    N  N N 154 
GLU   CA   C  N S 155 
GLU   C    C  N N 156 
GLU   O    O  N N 157 
GLU   CB   C  N N 158 
GLU   CG   C  N N 159 
GLU   CD   C  N N 160 
GLU   OE1  O  N N 161 
GLU   OE2  O  N N 162 
GLU   OXT  O  N N 163 
GLU   H    H  N N 164 
GLU   H2   H  N N 165 
GLU   HA   H  N N 166 
GLU   HB2  H  N N 167 
GLU   HB3  H  N N 168 
GLU   HG2  H  N N 169 
GLU   HG3  H  N N 170 
GLU   HE2  H  N N 171 
GLU   HXT  H  N N 172 
GLY   N    N  N N 173 
GLY   CA   C  N N 174 
GLY   C    C  N N 175 
GLY   O    O  N N 176 
GLY   OXT  O  N N 177 
GLY   H    H  N N 178 
GLY   H2   H  N N 179 
GLY   HA2  H  N N 180 
GLY   HA3  H  N N 181 
GLY   HXT  H  N N 182 
HIS   N    N  N N 183 
HIS   CA   C  N S 184 
HIS   C    C  N N 185 
HIS   O    O  N N 186 
HIS   CB   C  N N 187 
HIS   CG   C  Y N 188 
HIS   ND1  N  Y N 189 
HIS   CD2  C  Y N 190 
HIS   CE1  C  Y N 191 
HIS   NE2  N  Y N 192 
HIS   OXT  O  N N 193 
HIS   H    H  N N 194 
HIS   H2   H  N N 195 
HIS   HA   H  N N 196 
HIS   HB2  H  N N 197 
HIS   HB3  H  N N 198 
HIS   HD1  H  N N 199 
HIS   HD2  H  N N 200 
HIS   HE1  H  N N 201 
HIS   HE2  H  N N 202 
HIS   HXT  H  N N 203 
HOH   O    O  N N 204 
HOH   H1   H  N N 205 
HOH   H2   H  N N 206 
ILE   N    N  N N 207 
ILE   CA   C  N S 208 
ILE   C    C  N N 209 
ILE   O    O  N N 210 
ILE   CB   C  N S 211 
ILE   CG1  C  N N 212 
ILE   CG2  C  N N 213 
ILE   CD1  C  N N 214 
ILE   OXT  O  N N 215 
ILE   H    H  N N 216 
ILE   H2   H  N N 217 
ILE   HA   H  N N 218 
ILE   HB   H  N N 219 
ILE   HG12 H  N N 220 
ILE   HG13 H  N N 221 
ILE   HG21 H  N N 222 
ILE   HG22 H  N N 223 
ILE   HG23 H  N N 224 
ILE   HD11 H  N N 225 
ILE   HD12 H  N N 226 
ILE   HD13 H  N N 227 
ILE   HXT  H  N N 228 
LEU   N    N  N N 229 
LEU   CA   C  N S 230 
LEU   C    C  N N 231 
LEU   O    O  N N 232 
LEU   CB   C  N N 233 
LEU   CG   C  N N 234 
LEU   CD1  C  N N 235 
LEU   CD2  C  N N 236 
LEU   OXT  O  N N 237 
LEU   H    H  N N 238 
LEU   H2   H  N N 239 
LEU   HA   H  N N 240 
LEU   HB2  H  N N 241 
LEU   HB3  H  N N 242 
LEU   HG   H  N N 243 
LEU   HD11 H  N N 244 
LEU   HD12 H  N N 245 
LEU   HD13 H  N N 246 
LEU   HD21 H  N N 247 
LEU   HD22 H  N N 248 
LEU   HD23 H  N N 249 
LEU   HXT  H  N N 250 
LYS   N    N  N N 251 
LYS   CA   C  N S 252 
LYS   C    C  N N 253 
LYS   O    O  N N 254 
LYS   CB   C  N N 255 
LYS   CG   C  N N 256 
LYS   CD   C  N N 257 
LYS   CE   C  N N 258 
LYS   NZ   N  N N 259 
LYS   OXT  O  N N 260 
LYS   H    H  N N 261 
LYS   H2   H  N N 262 
LYS   HA   H  N N 263 
LYS   HB2  H  N N 264 
LYS   HB3  H  N N 265 
LYS   HG2  H  N N 266 
LYS   HG3  H  N N 267 
LYS   HD2  H  N N 268 
LYS   HD3  H  N N 269 
LYS   HE2  H  N N 270 
LYS   HE3  H  N N 271 
LYS   HZ1  H  N N 272 
LYS   HZ2  H  N N 273 
LYS   HZ3  H  N N 274 
LYS   HXT  H  N N 275 
MET   N    N  N N 276 
MET   CA   C  N S 277 
MET   C    C  N N 278 
MET   O    O  N N 279 
MET   CB   C  N N 280 
MET   CG   C  N N 281 
MET   SD   S  N N 282 
MET   CE   C  N N 283 
MET   OXT  O  N N 284 
MET   H    H  N N 285 
MET   H2   H  N N 286 
MET   HA   H  N N 287 
MET   HB2  H  N N 288 
MET   HB3  H  N N 289 
MET   HG2  H  N N 290 
MET   HG3  H  N N 291 
MET   HE1  H  N N 292 
MET   HE2  H  N N 293 
MET   HE3  H  N N 294 
MET   HXT  H  N N 295 
PHE   N    N  N N 296 
PHE   CA   C  N S 297 
PHE   C    C  N N 298 
PHE   O    O  N N 299 
PHE   CB   C  N N 300 
PHE   CG   C  Y N 301 
PHE   CD1  C  Y N 302 
PHE   CD2  C  Y N 303 
PHE   CE1  C  Y N 304 
PHE   CE2  C  Y N 305 
PHE   CZ   C  Y N 306 
PHE   OXT  O  N N 307 
PHE   H    H  N N 308 
PHE   H2   H  N N 309 
PHE   HA   H  N N 310 
PHE   HB2  H  N N 311 
PHE   HB3  H  N N 312 
PHE   HD1  H  N N 313 
PHE   HD2  H  N N 314 
PHE   HE1  H  N N 315 
PHE   HE2  H  N N 316 
PHE   HZ   H  N N 317 
PHE   HXT  H  N N 318 
PRO   N    N  N N 319 
PRO   CA   C  N S 320 
PRO   C    C  N N 321 
PRO   O    O  N N 322 
PRO   CB   C  N N 323 
PRO   CG   C  N N 324 
PRO   CD   C  N N 325 
PRO   OXT  O  N N 326 
PRO   H    H  N N 327 
PRO   HA   H  N N 328 
PRO   HB2  H  N N 329 
PRO   HB3  H  N N 330 
PRO   HG2  H  N N 331 
PRO   HG3  H  N N 332 
PRO   HD2  H  N N 333 
PRO   HD3  H  N N 334 
PRO   HXT  H  N N 335 
SER   N    N  N N 336 
SER   CA   C  N S 337 
SER   C    C  N N 338 
SER   O    O  N N 339 
SER   CB   C  N N 340 
SER   OG   O  N N 341 
SER   OXT  O  N N 342 
SER   H    H  N N 343 
SER   H2   H  N N 344 
SER   HA   H  N N 345 
SER   HB2  H  N N 346 
SER   HB3  H  N N 347 
SER   HG   H  N N 348 
SER   HXT  H  N N 349 
THR   N    N  N N 350 
THR   CA   C  N S 351 
THR   C    C  N N 352 
THR   O    O  N N 353 
THR   CB   C  N R 354 
THR   OG1  O  N N 355 
THR   CG2  C  N N 356 
THR   OXT  O  N N 357 
THR   H    H  N N 358 
THR   H2   H  N N 359 
THR   HA   H  N N 360 
THR   HB   H  N N 361 
THR   HG1  H  N N 362 
THR   HG21 H  N N 363 
THR   HG22 H  N N 364 
THR   HG23 H  N N 365 
THR   HXT  H  N N 366 
TRP   N    N  N N 367 
TRP   CA   C  N S 368 
TRP   C    C  N N 369 
TRP   O    O  N N 370 
TRP   CB   C  N N 371 
TRP   CG   C  Y N 372 
TRP   CD1  C  Y N 373 
TRP   CD2  C  Y N 374 
TRP   NE1  N  Y N 375 
TRP   CE2  C  Y N 376 
TRP   CE3  C  Y N 377 
TRP   CZ2  C  Y N 378 
TRP   CZ3  C  Y N 379 
TRP   CH2  C  Y N 380 
TRP   OXT  O  N N 381 
TRP   H    H  N N 382 
TRP   H2   H  N N 383 
TRP   HA   H  N N 384 
TRP   HB2  H  N N 385 
TRP   HB3  H  N N 386 
TRP   HD1  H  N N 387 
TRP   HE1  H  N N 388 
TRP   HE3  H  N N 389 
TRP   HZ2  H  N N 390 
TRP   HZ3  H  N N 391 
TRP   HH2  H  N N 392 
TRP   HXT  H  N N 393 
TYR   N    N  N N 394 
TYR   CA   C  N S 395 
TYR   C    C  N N 396 
TYR   O    O  N N 397 
TYR   CB   C  N N 398 
TYR   CG   C  Y N 399 
TYR   CD1  C  Y N 400 
TYR   CD2  C  Y N 401 
TYR   CE1  C  Y N 402 
TYR   CE2  C  Y N 403 
TYR   CZ   C  Y N 404 
TYR   OH   O  N N 405 
TYR   OXT  O  N N 406 
TYR   H    H  N N 407 
TYR   H2   H  N N 408 
TYR   HA   H  N N 409 
TYR   HB2  H  N N 410 
TYR   HB3  H  N N 411 
TYR   HD1  H  N N 412 
TYR   HD2  H  N N 413 
TYR   HE1  H  N N 414 
TYR   HE2  H  N N 415 
TYR   HH   H  N N 416 
TYR   HXT  H  N N 417 
VAL   N    N  N N 418 
VAL   CA   C  N S 419 
VAL   C    C  N N 420 
VAL   O    O  N N 421 
VAL   CB   C  N N 422 
VAL   CG1  C  N N 423 
VAL   CG2  C  N N 424 
VAL   OXT  O  N N 425 
VAL   H    H  N N 426 
VAL   H2   H  N N 427 
VAL   HA   H  N N 428 
VAL   HB   H  N N 429 
VAL   HG11 H  N N 430 
VAL   HG12 H  N N 431 
VAL   HG13 H  N N 432 
VAL   HG21 H  N N 433 
VAL   HG22 H  N N 434 
VAL   HG23 H  N N 435 
VAL   HXT  H  N N 436 
# 
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 
A1LW7 O15 C10  sing N N 1   
A1LW7 O09 C07  doub N N 2   
A1LW7 O26 N25  sing N N 3   
A1LW7 C10 C11  sing N N 4   
A1LW7 C10 C08  doub N N 5   
A1LW7 O27 N25  doub N N 6   
A1LW7 N25 C05  sing N N 7   
A1LW7 C11 C12  sing N N 8   
A1LW7 C07 C08  sing N N 9   
A1LW7 C07 C06  sing N N 10  
A1LW7 C08 C14  sing N N 11  
A1LW7 C05 C06  doub Y N 12  
A1LW7 C05 C04  sing Y N 13  
A1LW7 C06 C01  sing Y N 14  
A1LW7 C12 C13  sing N N 15  
A1LW7 C04 C03  doub Y N 16  
A1LW7 C01 C02  doub Y N 17  
A1LW7 C14 C13  sing N N 18  
A1LW7 C14 O16  doub N N 19  
A1LW7 C03 C02  sing Y N 20  
A1LW7 C03 C20  sing N N 21  
A1LW7 C02 N17  sing N N 22  
A1LW7 F31 C28  sing N N 23  
A1LW7 O21 C20  doub N N 24  
A1LW7 C20 N19  sing N N 25  
A1LW7 N17 C23  sing N N 26  
A1LW7 N17 C18  sing N N 27  
A1LW7 F29 C28  sing N N 28  
A1LW7 C28 F30  sing N N 29  
A1LW7 C28 C24  sing N N 30  
A1LW7 N19 C18  sing N N 31  
A1LW7 N19 C24  sing N N 32  
A1LW7 C18 O22  doub N N 33  
A1LW7 C13 H1   sing N N 34  
A1LW7 C13 H2   sing N N 35  
A1LW7 C24 H3   sing N N 36  
A1LW7 C24 H4   sing N N 37  
A1LW7 C01 H5   sing N N 38  
A1LW7 C04 H6   sing N N 39  
A1LW7 C11 H7   sing N N 40  
A1LW7 C11 H8   sing N N 41  
A1LW7 C12 H9   sing N N 42  
A1LW7 C12 H10  sing N N 43  
A1LW7 C23 H11  sing N N 44  
A1LW7 C23 H12  sing N N 45  
A1LW7 C23 H13  sing N N 46  
A1LW7 O15 H14  sing N N 47  
ALA   N   CA   sing N N 48  
ALA   N   H    sing N N 49  
ALA   N   H2   sing N N 50  
ALA   CA  C    sing N N 51  
ALA   CA  CB   sing N N 52  
ALA   CA  HA   sing N N 53  
ALA   C   O    doub N N 54  
ALA   C   OXT  sing N N 55  
ALA   CB  HB1  sing N N 56  
ALA   CB  HB2  sing N N 57  
ALA   CB  HB3  sing N N 58  
ALA   OXT HXT  sing N N 59  
ARG   N   CA   sing N N 60  
ARG   N   H    sing N N 61  
ARG   N   H2   sing N N 62  
ARG   CA  C    sing N N 63  
ARG   CA  CB   sing N N 64  
ARG   CA  HA   sing N N 65  
ARG   C   O    doub N N 66  
ARG   C   OXT  sing N N 67  
ARG   CB  CG   sing N N 68  
ARG   CB  HB2  sing N N 69  
ARG   CB  HB3  sing N N 70  
ARG   CG  CD   sing N N 71  
ARG   CG  HG2  sing N N 72  
ARG   CG  HG3  sing N N 73  
ARG   CD  NE   sing N N 74  
ARG   CD  HD2  sing N N 75  
ARG   CD  HD3  sing N N 76  
ARG   NE  CZ   sing N N 77  
ARG   NE  HE   sing N N 78  
ARG   CZ  NH1  sing N N 79  
ARG   CZ  NH2  doub N N 80  
ARG   NH1 HH11 sing N N 81  
ARG   NH1 HH12 sing N N 82  
ARG   NH2 HH21 sing N N 83  
ARG   NH2 HH22 sing N N 84  
ARG   OXT HXT  sing N N 85  
ASN   N   CA   sing N N 86  
ASN   N   H    sing N N 87  
ASN   N   H2   sing N N 88  
ASN   CA  C    sing N N 89  
ASN   CA  CB   sing N N 90  
ASN   CA  HA   sing N N 91  
ASN   C   O    doub N N 92  
ASN   C   OXT  sing N N 93  
ASN   CB  CG   sing N N 94  
ASN   CB  HB2  sing N N 95  
ASN   CB  HB3  sing N N 96  
ASN   CG  OD1  doub N N 97  
ASN   CG  ND2  sing N N 98  
ASN   ND2 HD21 sing N N 99  
ASN   ND2 HD22 sing N N 100 
ASN   OXT HXT  sing N N 101 
ASP   N   CA   sing N N 102 
ASP   N   H    sing N N 103 
ASP   N   H2   sing N N 104 
ASP   CA  C    sing N N 105 
ASP   CA  CB   sing N N 106 
ASP   CA  HA   sing N N 107 
ASP   C   O    doub N N 108 
ASP   C   OXT  sing N N 109 
ASP   CB  CG   sing N N 110 
ASP   CB  HB2  sing N N 111 
ASP   CB  HB3  sing N N 112 
ASP   CG  OD1  doub N N 113 
ASP   CG  OD2  sing N N 114 
ASP   OD2 HD2  sing N N 115 
ASP   OXT HXT  sing N N 116 
CYS   N   CA   sing N N 117 
CYS   N   H    sing N N 118 
CYS   N   H2   sing N N 119 
CYS   CA  C    sing N N 120 
CYS   CA  CB   sing N N 121 
CYS   CA  HA   sing N N 122 
CYS   C   O    doub N N 123 
CYS   C   OXT  sing N N 124 
CYS   CB  SG   sing N N 125 
CYS   CB  HB2  sing N N 126 
CYS   CB  HB3  sing N N 127 
CYS   SG  HG   sing N N 128 
CYS   OXT HXT  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TRP   N   CA   sing N N 353 
TRP   N   H    sing N N 354 
TRP   N   H2   sing N N 355 
TRP   CA  C    sing N N 356 
TRP   CA  CB   sing N N 357 
TRP   CA  HA   sing N N 358 
TRP   C   O    doub N N 359 
TRP   C   OXT  sing N N 360 
TRP   CB  CG   sing N N 361 
TRP   CB  HB2  sing N N 362 
TRP   CB  HB3  sing N N 363 
TRP   CG  CD1  doub Y N 364 
TRP   CG  CD2  sing Y N 365 
TRP   CD1 NE1  sing Y N 366 
TRP   CD1 HD1  sing N N 367 
TRP   CD2 CE2  doub Y N 368 
TRP   CD2 CE3  sing Y N 369 
TRP   NE1 CE2  sing Y N 370 
TRP   NE1 HE1  sing N N 371 
TRP   CE2 CZ2  sing Y N 372 
TRP   CE3 CZ3  doub Y N 373 
TRP   CE3 HE3  sing N N 374 
TRP   CZ2 CH2  doub Y N 375 
TRP   CZ2 HZ2  sing N N 376 
TRP   CZ3 CH2  sing Y N 377 
TRP   CZ3 HZ3  sing N N 378 
TRP   CH2 HH2  sing N N 379 
TRP   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
_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                    8XUG 
_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]   0.012886 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002373 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011894 
_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]   0.015704 
_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   ? 22.306  -5.229  89.645  1.00 65.72  ? 35  LYS   A N   1 
ATOM   2    C  CA  . LYS   A 1 7   ? 23.249  -6.234  89.160  1.00 70.18  ? 35  LYS   A CA  1 
ATOM   3    C  C   . LYS   A 1 7   ? 22.906  -6.662  87.736  1.00 69.66  ? 35  LYS   A C   1 
ATOM   4    O  O   . LYS   A 1 7   ? 21.839  -7.241  87.483  1.00 63.74  ? 35  LYS   A O   1 
ATOM   5    C  CB  . LYS   A 1 7   ? 23.267  -7.457  90.088  1.00 69.89  ? 35  LYS   A CB  1 
ATOM   6    N  N   . ASN   A 1 8   ? 23.811  -6.370  86.805  1.00 65.85  ? 36  ASN   A N   1 
ATOM   7    C  CA  . ASN   A 1 8   ? 23.660  -6.806  85.420  1.00 64.17  ? 36  ASN   A CA  1 
ATOM   8    C  C   . ASN   A 1 8   ? 24.832  -7.691  85.042  1.00 59.52  ? 36  ASN   A C   1 
ATOM   9    O  O   . ASN   A 1 8   ? 25.900  -7.186  84.656  1.00 64.83  ? 36  ASN   A O   1 
ATOM   10   C  CB  . ASN   A 1 8   ? 23.569  -5.623  84.463  1.00 58.65  ? 36  ASN   A CB  1 
ATOM   11   C  CG  . ASN   A 1 8   ? 23.204  -6.055  83.045  1.00 59.78  ? 36  ASN   A CG  1 
ATOM   12   O  OD1 . ASN   A 1 8   ? 23.223  -7.253  82.720  1.00 56.18  ? 36  ASN   A OD1 1 
ATOM   13   N  ND2 . ASN   A 1 8   ? 22.855  -5.077  82.192  1.00 54.84  ? 36  ASN   A ND2 1 
ATOM   14   N  N   . PRO   A 1 9   ? 24.684  -9.015  85.108  1.00 62.45  ? 37  PRO   A N   1 
ATOM   15   C  CA  . PRO   A 1 9   ? 25.772  -9.910  84.643  1.00 60.41  ? 37  PRO   A CA  1 
ATOM   16   C  C   . PRO   A 1 9   ? 26.004  -9.904  83.137  1.00 60.06  ? 37  PRO   A C   1 
ATOM   17   O  O   . PRO   A 1 9   ? 27.041  -10.406 82.706  1.00 62.97  ? 37  PRO   A O   1 
ATOM   18   C  CB  . PRO   A 1 9   ? 25.300  -11.315 85.101  1.00 58.31  ? 37  PRO   A CB  1 
ATOM   19   C  CG  . PRO   A 1 9   ? 24.045  -11.107 85.903  1.00 66.01  ? 37  PRO   A CG  1 
ATOM   20   C  CD  . PRO   A 1 9   ? 23.497  -9.758  85.616  1.00 60.42  ? 37  PRO   A CD  1 
ATOM   21   N  N   . LYS   A 1 10  ? 25.084  -9.361  82.343  1.00 56.79  ? 38  LYS   A N   1 
ATOM   22   C  CA  . LYS   A 1 10  ? 25.209  -9.333  80.880  1.00 56.60  ? 38  LYS   A CA  1 
ATOM   23   C  C   . LYS   A 1 10  ? 25.435  -10.733 80.302  1.00 54.93  ? 38  LYS   A C   1 
ATOM   24   O  O   . LYS   A 1 10  ? 26.433  -11.010 79.640  1.00 51.43  ? 38  LYS   A O   1 
ATOM   25   C  CB  . LYS   A 1 10  ? 26.314  -8.374  80.434  1.00 56.02  ? 38  LYS   A CB  1 
ATOM   26   C  CG  . LYS   A 1 10  ? 26.158  -6.942  80.932  1.00 58.03  ? 38  LYS   A CG  1 
ATOM   27   C  CD  . LYS   A 1 10  ? 26.593  -5.943  79.868  1.00 56.37  ? 38  LYS   A CD  1 
ATOM   28   C  CE  . LYS   A 1 10  ? 27.022  -4.616  80.476  1.00 64.13  ? 38  LYS   A CE  1 
ATOM   29   N  NZ  . LYS   A 1 10  ? 26.136  -4.183  81.594  1.00 65.12  ? 38  LYS   A NZ  1 
ATOM   30   N  N   . SER   A 1 11  ? 24.458  -11.610 80.533  1.00 55.00  ? 39  SER   A N   1 
ATOM   31   C  CA  . SER   A 1 11  ? 24.616  -13.027 80.227  1.00 53.42  ? 39  SER   A CA  1 
ATOM   32   C  C   . SER   A 1 11  ? 23.924  -13.467 78.937  1.00 50.65  ? 39  SER   A C   1 
ATOM   33   O  O   . SER   A 1 11  ? 23.794  -14.675 78.715  1.00 47.15  ? 39  SER   A O   1 
ATOM   34   C  CB  . SER   A 1 11  ? 24.110  -13.879 81.397  1.00 56.26  ? 39  SER   A CB  1 
ATOM   35   O  OG  . SER   A 1 11  ? 22.837  -13.449 81.839  1.00 52.47  ? 39  SER   A OG  1 
ATOM   36   N  N   . ASP   A 1 12  ? 23.499  -12.532 78.081  1.00 52.04  ? 40  ASP   A N   1 
ATOM   37   C  CA  . ASP   A 1 12  ? 22.859  -12.888 76.810  1.00 50.73  ? 40  ASP   A CA  1 
ATOM   38   C  C   . ASP   A 1 12  ? 23.703  -13.918 76.072  1.00 52.14  ? 40  ASP   A C   1 
ATOM   39   O  O   . ASP   A 1 12  ? 24.906  -13.715 75.871  1.00 45.10  ? 40  ASP   A O   1 
ATOM   40   C  CB  . ASP   A 1 12  ? 22.685  -11.650 75.913  1.00 45.95  ? 40  ASP   A CB  1 
ATOM   41   C  CG  . ASP   A 1 12  ? 21.625  -10.694 76.410  1.00 48.51  ? 40  ASP   A CG  1 
ATOM   42   O  OD1 . ASP   A 1 12  ? 21.475  -9.609  75.792  1.00 48.48  ? 40  ASP   A OD1 1 
ATOM   43   O  OD2 . ASP   A 1 12  ? 20.951  -11.016 77.411  1.00 49.52  ? 40  ASP   A OD2 1 
ATOM   44   N  N   . LYS   A 1 13  ? 23.062  -15.024 75.670  1.00 46.94  ? 41  LYS   A N   1 
ATOM   45   C  CA  . LYS   A 1 13  ? 23.740  -16.107 74.966  1.00 49.65  ? 41  LYS   A CA  1 
ATOM   46   C  C   . LYS   A 1 13  ? 23.951  -15.819 73.486  1.00 50.15  ? 41  LYS   A C   1 
ATOM   47   O  O   . LYS   A 1 13  ? 24.632  -16.593 72.806  1.00 50.18  ? 41  LYS   A O   1 
ATOM   48   C  CB  . LYS   A 1 13  ? 22.955  -17.411 75.132  1.00 49.16  ? 41  LYS   A CB  1 
ATOM   49   C  CG  . LYS   A 1 13  ? 22.610  -17.710 76.582  1.00 49.74  ? 41  LYS   A CG  1 
ATOM   50   C  CD  . LYS   A 1 13  ? 22.383  -19.187 76.823  1.00 48.46  ? 41  LYS   A CD  1 
ATOM   51   C  CE  . LYS   A 1 13  ? 22.836  -19.588 78.228  1.00 55.24  ? 41  LYS   A CE  1 
ATOM   52   N  NZ  . LYS   A 1 13  ? 21.752  -19.411 79.230  1.00 57.74  ? 41  LYS   A NZ  1 
ATOM   53   N  N   . PHE   A 1 14  ? 23.381  -14.740 72.976  1.00 46.41  ? 42  PHE   A N   1 
ATOM   54   C  CA  . PHE   A 1 14  ? 23.573  -14.299 71.605  1.00 44.79  ? 42  PHE   A CA  1 
ATOM   55   C  C   . PHE   A 1 14  ? 23.268  -12.827 71.667  1.00 44.33  ? 42  PHE   A C   1 
ATOM   56   O  O   . PHE   A 1 14  ? 22.724  -12.348 72.665  1.00 49.06  ? 42  PHE   A O   1 
ATOM   57   C  CB  . PHE   A 1 14  ? 22.674  -15.052 70.620  1.00 48.02  ? 42  PHE   A CB  1 
ATOM   58   C  CG  . PHE   A 1 14  ? 21.252  -15.192 71.088  1.00 47.16  ? 42  PHE   A CG  1 
ATOM   59   C  CD1 . PHE   A 1 14  ? 20.334  -14.174 70.886  1.00 45.66  ? 42  PHE   A CD1 1 
ATOM   60   C  CD2 . PHE   A 1 14  ? 20.840  -16.341 71.741  1.00 46.87  ? 42  PHE   A CD2 1 
ATOM   61   C  CE1 . PHE   A 1 14  ? 19.030  -14.303 71.334  1.00 43.27  ? 42  PHE   A CE1 1 
ATOM   62   C  CE2 . PHE   A 1 14  ? 19.539  -16.479 72.182  1.00 46.83  ? 42  PHE   A CE2 1 
ATOM   63   C  CZ  . PHE   A 1 14  ? 18.632  -15.465 71.976  1.00 39.87  ? 42  PHE   A CZ  1 
ATOM   64   N  N   . LYS   A 1 15  ? 23.684  -12.082 70.655  1.00 46.61  ? 43  LYS   A N   1 
ATOM   65   C  CA  . LYS   A 1 15  ? 23.574  -10.645 70.822  1.00 47.37  ? 43  LYS   A CA  1 
ATOM   66   C  C   . LYS   A 1 15  ? 22.170  -10.236 70.389  1.00 43.60  ? 43  LYS   A C   1 
ATOM   67   O  O   . LYS   A 1 15  ? 21.683  -10.664 69.346  1.00 41.49  ? 43  LYS   A O   1 
ATOM   68   C  CB  . LYS   A 1 15  ? 24.644  -9.877  70.051  1.00 49.74  ? 43  LYS   A CB  1 
ATOM   69   N  N   . VAL   A 1 16  ? 21.569  -9.348  71.148  1.00 43.47  ? 44  VAL   A N   1 
ATOM   70   C  CA  . VAL   A 1 16  ? 20.202  -8.916  70.937  1.00 45.00  ? 44  VAL   A CA  1 
ATOM   71   C  C   . VAL   A 1 16  ? 20.253  -7.415  70.766  1.00 46.91  ? 44  VAL   A C   1 
ATOM   72   O  O   . VAL   A 1 16  ? 21.013  -6.735  71.463  1.00 46.65  ? 44  VAL   A O   1 
ATOM   73   C  CB  . VAL   A 1 16  ? 19.311  -9.328  72.122  1.00 44.51  ? 44  VAL   A CB  1 
ATOM   74   C  CG1 . VAL   A 1 16  ? 17.962  -8.603  72.079  1.00 42.99  ? 44  VAL   A CG1 1 
ATOM   75   C  CG2 . VAL   A 1 16  ? 19.112  -10.856 72.145  1.00 42.41  ? 44  VAL   A CG2 1 
ATOM   76   N  N   . LYS   A 1 17  ? 19.500  -6.900  69.803  1.00 43.69  ? 45  LYS   A N   1 
ATOM   77   C  CA  . LYS   A 1 17  ? 19.493  -5.455  69.667  1.00 44.86  ? 45  LYS   A CA  1 
ATOM   78   C  C   . LYS   A 1 17  ? 18.249  -4.902  70.338  1.00 48.94  ? 45  LYS   A C   1 
ATOM   79   O  O   . LYS   A 1 17  ? 18.300  -4.554  71.523  1.00 49.78  ? 45  LYS   A O   1 
ATOM   80   C  CB  . LYS   A 1 17  ? 19.597  -5.060  68.204  1.00 45.98  ? 45  LYS   A CB  1 
ATOM   81   C  CG  . LYS   A 1 17  ? 20.824  -5.677  67.572  1.00 50.05  ? 45  LYS   A CG  1 
ATOM   82   C  CD  . LYS   A 1 17  ? 20.672  -5.861  66.090  1.00 51.97  ? 45  LYS   A CD  1 
ATOM   83   C  CE  . LYS   A 1 17  ? 21.115  -4.624  65.349  1.00 57.48  ? 45  LYS   A CE  1 
ATOM   84   N  NZ  . LYS   A 1 17  ? 21.581  -4.987  63.983  1.00 65.06  ? 45  LYS   A NZ  1 
ATOM   85   N  N   . ARG   A 1 18  ? 17.159  -4.792  69.594  1.00 40.28  ? 46  ARG   A N   1 
ATOM   86   C  CA  . ARG   A 1 18  ? 15.913  -4.289  70.137  1.00 42.58  ? 46  ARG   A CA  1 
ATOM   87   C  C   . ARG   A 1 18  ? 14.660  -4.972  69.588  1.00 42.37  ? 46  ARG   A C   1 
ATOM   88   O  O   . ARG   A 1 18  ? 14.713  -5.718  68.650  1.00 38.87  ? 46  ARG   A O   1 
ATOM   89   C  CB  . ARG   A 1 18  ? 15.744  -2.820  69.775  1.00 46.58  ? 46  ARG   A CB  1 
ATOM   90   C  CG  . ARG   A 1 18  ? 16.905  -1.911  70.041  1.00 62.42  ? 46  ARG   A CG  1 
ATOM   91   C  CD  . ARG   A 1 18  ? 16.677  -1.103  71.294  1.00 67.36  ? 46  ARG   A CD  1 
ATOM   92   N  NE  . ARG   A 1 18  ? 17.763  -0.164  71.542  1.00 63.58  ? 46  ARG   A NE  1 
ATOM   93   C  CZ  . ARG   A 1 18  ? 18.942  -0.483  72.067  1.00 52.26  ? 46  ARG   A CZ  1 
ATOM   94   N  NH1 . ARG   A 1 18  ? 19.852  0.451   72.231  1.00 51.57  ? 46  ARG   A NH1 1 
ATOM   95   N  NH2 . ARG   A 1 18  ? 19.220  -1.727  72.420  1.00 55.46  ? 46  ARG   A NH2 1 
ATOM   96   N  N   . PHE   A 1 19  ? 13.538  -4.721  70.240  1.00 38.47  ? 47  PHE   A N   1 
ATOM   97   C  CA  . PHE   A 1 19  ? 12.253  -5.157  69.704  1.00 37.29  ? 47  PHE   A CA  1 
ATOM   98   C  C   . PHE   A 1 19  ? 12.168  -4.703  68.264  1.00 36.51  ? 47  PHE   A C   1 
ATOM   99   O  O   . PHE   A 1 19  ? 12.515  -3.568  67.941  1.00 40.78  ? 47  PHE   A O   1 
ATOM   100  C  CB  . PHE   A 1 19  ? 11.095  -4.548  70.507  1.00 42.61  ? 47  PHE   A CB  1 
ATOM   101  C  CG  . PHE   A 1 19  ? 10.910  -5.142  71.898  1.00 39.88  ? 47  PHE   A CG  1 
ATOM   102  C  CD1 . PHE   A 1 19  ? 10.563  -6.465  72.039  1.00 34.02  ? 47  PHE   A CD1 1 
ATOM   103  C  CD2 . PHE   A 1 19  ? 10.999  -4.340  73.042  1.00 35.58  ? 47  PHE   A CD2 1 
ATOM   104  C  CE1 . PHE   A 1 19  ? 10.346  -7.011  73.274  1.00 37.34  ? 47  PHE   A CE1 1 
ATOM   105  C  CE2 . PHE   A 1 19  ? 10.779  -4.894  74.308  1.00 36.38  ? 47  PHE   A CE2 1 
ATOM   106  C  CZ  . PHE   A 1 19  ? 10.470  -6.232  74.417  1.00 34.99  ? 47  PHE   A CZ  1 
ATOM   107  N  N   . HIS   A 1 20  ? 11.736  -5.608  67.400  1.00 38.58  ? 48  HIS   A N   1 
ATOM   108  C  CA  . HIS   A 1 20  ? 11.548  -5.326  65.990  1.00 36.87  ? 48  HIS   A CA  1 
ATOM   109  C  C   . HIS   A 1 20  ? 10.077  -5.118  65.637  1.00 35.04  ? 48  HIS   A C   1 
ATOM   110  O  O   . HIS   A 1 20  ? 9.721   -4.100  65.040  1.00 37.35  ? 48  HIS   A O   1 
ATOM   111  C  CB  . HIS   A 1 20  ? 12.147  -6.478  65.186  1.00 38.36  ? 48  HIS   A CB  1 
ATOM   112  C  CG  . HIS   A 1 20  ? 12.207  -6.207  63.727  1.00 40.26  ? 48  HIS   A CG  1 
ATOM   113  N  ND1 . HIS   A 1 20  ? 11.192  -6.566  62.868  1.00 42.51  ? 48  HIS   A ND1 1 
ATOM   114  C  CD2 . HIS   A 1 20  ? 13.137  -5.576  62.976  1.00 45.38  ? 48  HIS   A CD2 1 
ATOM   115  C  CE1 . HIS   A 1 20  ? 11.500  -6.178  61.645  1.00 43.31  ? 48  HIS   A CE1 1 
ATOM   116  N  NE2 . HIS   A 1 20  ? 12.683  -5.586  61.682  1.00 48.35  ? 48  HIS   A NE2 1 
ATOM   117  N  N   . HIS   A 1 21  ? 9.203   -6.058  66.000  1.00 34.66  ? 49  HIS   A N   1 
ATOM   118  C  CA  . HIS   A 1 21  ? 7.767   -5.860  65.800  1.00 34.36  ? 49  HIS   A CA  1 
ATOM   119  C  C   . HIS   A 1 21  ? 6.991   -6.821  66.689  1.00 37.19  ? 49  HIS   A C   1 
ATOM   120  O  O   . HIS   A 1 21  ? 7.539   -7.780  67.241  1.00 35.06  ? 49  HIS   A O   1 
ATOM   121  C  CB  . HIS   A 1 21  ? 7.355   -6.052  64.332  1.00 36.18  ? 49  HIS   A CB  1 
ATOM   122  C  CG  . HIS   A 1 21  ? 7.582   -7.446  63.819  1.00 37.80  ? 49  HIS   A CG  1 
ATOM   123  N  ND1 . HIS   A 1 21  ? 8.812   -7.875  63.368  1.00 34.59  ? 49  HIS   A ND1 1 
ATOM   124  C  CD2 . HIS   A 1 21  ? 6.739   -8.501  63.682  1.00 35.43  ? 49  HIS   A CD2 1 
ATOM   125  C  CE1 . HIS   A 1 21  ? 8.723   -9.139  62.983  1.00 38.24  ? 49  HIS   A CE1 1 
ATOM   126  N  NE2 . HIS   A 1 21  ? 7.481   -9.548  63.179  1.00 36.66  ? 49  HIS   A NE2 1 
ATOM   127  N  N   . ILE   A 1 22  ? 5.699   -6.537  66.814  1.00 35.50  ? 50  ILE   A N   1 
ATOM   128  C  CA  . ILE   A 1 22  ? 4.721   -7.385  67.480  1.00 32.45  ? 50  ILE   A CA  1 
ATOM   129  C  C   . ILE   A 1 22  ? 3.725   -7.822  66.418  1.00 34.99  ? 50  ILE   A C   1 
ATOM   130  O  O   . ILE   A 1 22  ? 3.200   -6.976  65.689  1.00 29.44  ? 50  ILE   A O   1 
ATOM   131  C  CB  . ILE   A 1 22  ? 3.983   -6.635  68.606  1.00 35.80  ? 50  ILE   A CB  1 
ATOM   132  C  CG1 . ILE   A 1 22  ? 4.940   -6.164  69.699  1.00 36.60  ? 50  ILE   A CG1 1 
ATOM   133  C  CG2 . ILE   A 1 22  ? 2.836   -7.481  69.163  1.00 32.41  ? 50  ILE   A CG2 1 
ATOM   134  C  CD1 . ILE   A 1 22  ? 5.578   -7.313  70.479  1.00 35.55  ? 50  ILE   A CD1 1 
ATOM   135  N  N   . GLU   A 1 23  ? 3.456   -9.125  66.323  1.00 32.33  ? 51  GLU   A N   1 
ATOM   136  C  CA  . GLU   A 1 23  ? 2.486   -9.625  65.347  1.00 29.47  ? 51  GLU   A CA  1 
ATOM   137  C  C   . GLU   A 1 23  ? 1.216   -10.119 66.028  1.00 32.51  ? 51  GLU   A C   1 
ATOM   138  O  O   . GLU   A 1 23  ? 1.262   -11.049 66.845  1.00 33.13  ? 51  GLU   A O   1 
ATOM   139  C  CB  . GLU   A 1 23  ? 3.045   -10.757 64.478  1.00 29.73  ? 51  GLU   A CB  1 
ATOM   140  C  CG  . GLU   A 1 23  ? 1.936   -11.234 63.472  1.00 26.36  ? 51  GLU   A CG  1 
ATOM   141  C  CD  . GLU   A 1 23  ? 2.441   -12.255 62.482  1.00 36.41  ? 51  GLU   A CD  1 
ATOM   142  O  OE1 . GLU   A 1 23  ? 3.571   -12.733 62.665  1.00 37.16  ? 51  GLU   A OE1 1 
ATOM   143  O  OE2 . GLU   A 1 23  ? 1.724   -12.567 61.510  1.00 37.39  ? 51  GLU   A OE2 1 
ATOM   144  N  N   . PHE   A 1 24  ? 0.077   -9.543  65.634  1.00 31.20  ? 52  PHE   A N   1 
ATOM   145  C  CA  . PHE   A 1 24  ? -1.223  -9.986  66.098  1.00 32.07  ? 52  PHE   A CA  1 
ATOM   146  C  C   . PHE   A 1 24  ? -1.769  -11.011 65.107  1.00 32.59  ? 52  PHE   A C   1 
ATOM   147  O  O   . PHE   A 1 24  ? -1.695  -10.809 63.889  1.00 31.89  ? 52  PHE   A O   1 
ATOM   148  C  CB  . PHE   A 1 24  ? -2.207  -8.804  66.193  1.00 31.52  ? 52  PHE   A CB  1 
ATOM   149  C  CG  . PHE   A 1 24  ? -1.896  -7.828  67.292  1.00 32.19  ? 52  PHE   A CG  1 
ATOM   150  C  CD1 . PHE   A 1 24  ? -0.930  -6.858  67.114  1.00 30.48  ? 52  PHE   A CD1 1 
ATOM   151  C  CD2 . PHE   A 1 24  ? -2.596  -7.857  68.492  1.00 33.10  ? 52  PHE   A CD2 1 
ATOM   152  C  CE1 . PHE   A 1 24  ? -0.644  -5.955  68.119  1.00 33.29  ? 52  PHE   A CE1 1 
ATOM   153  C  CE2 . PHE   A 1 24  ? -2.284  -6.948  69.511  1.00 31.66  ? 52  PHE   A CE2 1 
ATOM   154  C  CZ  . PHE   A 1 24  ? -1.334  -6.002  69.311  1.00 31.73  ? 52  PHE   A CZ  1 
ATOM   155  N  N   . TRP   A 1 25  ? -2.344  -12.094 65.626  1.00 29.08  ? 53  TRP   A N   1 
ATOM   156  C  CA  . TRP   A 1 25  ? -3.109  -13.005 64.791  1.00 29.65  ? 53  TRP   A CA  1 
ATOM   157  C  C   . TRP   A 1 25  ? -4.593  -12.718 64.966  1.00 35.44  ? 53  TRP   A C   1 
ATOM   158  O  O   . TRP   A 1 25  ? -5.094  -12.652 66.093  1.00 36.23  ? 53  TRP   A O   1 
ATOM   159  C  CB  . TRP   A 1 25  ? -2.783  -14.467 65.116  1.00 30.10  ? 53  TRP   A CB  1 
ATOM   160  C  CG  . TRP   A 1 25  ? -1.644  -14.988 64.278  1.00 33.57  ? 53  TRP   A CG  1 
ATOM   161  C  CD1 . TRP   A 1 25  ? -0.931  -14.301 63.334  1.00 33.43  ? 53  TRP   A CD1 1 
ATOM   162  C  CD2 . TRP   A 1 25  ? -1.105  -16.318 64.297  1.00 34.98  ? 53  TRP   A CD2 1 
ATOM   163  N  NE1 . TRP   A 1 25  ? 0.021   -15.125 62.768  1.00 33.78  ? 53  TRP   A NE1 1 
ATOM   164  C  CE2 . TRP   A 1 25  ? -0.065  -16.363 63.345  1.00 35.70  ? 53  TRP   A CE2 1 
ATOM   165  C  CE3 . TRP   A 1 25  ? -1.405  -17.474 65.023  1.00 33.70  ? 53  TRP   A CE3 1 
ATOM   166  C  CZ2 . TRP   A 1 25  ? 0.682   -17.527 63.103  1.00 39.08  ? 53  TRP   A CZ2 1 
ATOM   167  C  CZ3 . TRP   A 1 25  ? -0.663  -18.624 64.787  1.00 36.98  ? 53  TRP   A CZ3 1 
ATOM   168  C  CH2 . TRP   A 1 25  ? 0.368   -18.643 63.834  1.00 38.84  ? 53  TRP   A CH2 1 
ATOM   169  N  N   . CYS   A 1 26  ? -5.278  -12.507 63.847  1.00 36.13  ? 54  CYS   A N   1 
ATOM   170  C  CA  . CYS   A 1 26  ? -6.671  -12.081 63.858  1.00 35.65  ? 54  CYS   A CA  1 
ATOM   171  C  C   . CYS   A 1 26  ? -7.438  -12.858 62.806  1.00 34.07  ? 54  CYS   A C   1 
ATOM   172  O  O   . CYS   A 1 26  ? -6.884  -13.668 62.057  1.00 36.30  ? 54  CYS   A O   1 
ATOM   173  C  CB  . CYS   A 1 26  ? -6.861  -10.585 63.587  1.00 35.25  ? 54  CYS   A CB  1 
ATOM   174  S  SG  . CYS   A 1 26  ? -5.476  -9.475  63.626  1.00 46.70  ? 54  CYS   A SG  1 
ATOM   175  N  N   . GLY   A 1 27  ? -8.730  -12.591 62.743  1.00 38.29  ? 55  GLY   A N   1 
ATOM   176  C  CA  . GLY   A 1 27  ? -9.537  -13.279 61.782  1.00 36.01  ? 55  GLY   A CA  1 
ATOM   177  C  C   . GLY   A 1 27  ? -9.773  -12.390 60.590  1.00 37.94  ? 55  GLY   A C   1 
ATOM   178  O  O   . GLY   A 1 27  ? -9.919  -12.862 59.454  1.00 39.05  ? 55  GLY   A O   1 
ATOM   179  N  N   . ASP   A 1 28  ? -9.861  -11.091 60.854  1.00 34.74  ? 56  ASP   A N   1 
ATOM   180  C  CA  . ASP   A 1 28  ? -9.820  -10.081 59.805  1.00 35.17  ? 56  ASP   A CA  1 
ATOM   181  C  C   . ASP   A 1 28  ? -8.721  -9.079  60.153  1.00 34.81  ? 56  ASP   A C   1 
ATOM   182  O  O   . ASP   A 1 28  ? -8.834  -8.322  61.128  1.00 37.82  ? 56  ASP   A O   1 
ATOM   183  C  CB  . ASP   A 1 28  ? -11.188 -9.407  59.624  1.00 33.24  ? 56  ASP   A CB  1 
ATOM   184  C  CG  . ASP   A 1 28  ? -11.236 -8.570  58.377  1.00 33.54  ? 56  ASP   A CG  1 
ATOM   185  O  OD1 . ASP   A 1 28  ? -11.352 -9.153  57.282  1.00 36.32  ? 56  ASP   A OD1 1 
ATOM   186  O  OD2 . ASP   A 1 28  ? -11.118 -7.344  58.490  1.00 34.63  ? 56  ASP   A OD2 1 
ATOM   187  N  N   . ALA   A 1 29  ? -7.636  -9.084  59.373  1.00 32.62  ? 57  ALA   A N   1 
ATOM   188  C  CA  . ALA   A 1 29  ? -6.551  -8.149  59.652  1.00 32.87  ? 57  ALA   A CA  1 
ATOM   189  C  C   . ALA   A 1 29  ? -6.921  -6.714  59.278  1.00 34.19  ? 57  ALA   A C   1 
ATOM   190  O  O   . ALA   A 1 29  ? -6.409  -5.762  59.883  1.00 34.43  ? 57  ALA   A O   1 
ATOM   191  C  CB  . ALA   A 1 29  ? -5.282  -8.595  58.919  1.00 32.51  ? 57  ALA   A CB  1 
ATOM   192  N  N   . THR   A 1 30  ? -7.777  -6.529  58.280  1.00 33.52  ? 58  THR   A N   1 
ATOM   193  C  CA  . THR   A 1 30  ? -8.147  -5.170  57.877  1.00 34.63  ? 58  THR   A CA  1 
ATOM   194  C  C   . THR   A 1 30  ? -8.839  -4.419  59.012  1.00 31.40  ? 58  THR   A C   1 
ATOM   195  O  O   . THR   A 1 30  ? -8.463  -3.292  59.351  1.00 32.95  ? 58  THR   A O   1 
ATOM   196  C  CB  . THR   A 1 30  ? -9.039  -5.226  56.639  1.00 37.07  ? 58  THR   A CB  1 
ATOM   197  O  OG1 . THR   A 1 30  ? -8.299  -5.816  55.563  1.00 36.00  ? 58  THR   A OG1 1 
ATOM   198  C  CG2 . THR   A 1 30  ? -9.515  -3.816  56.233  1.00 37.14  ? 58  THR   A CG2 1 
ATOM   199  N  N   . ASN   A 1 31  ? -9.854  -5.020  59.624  1.00 28.74  ? 59  ASN   A N   1 
ATOM   200  C  CA  . ASN   A 1 31  ? -10.646 -4.233  60.564  1.00 33.34  ? 59  ASN   A CA  1 
ATOM   201  C  C   . ASN   A 1 31  ? -9.868  -3.938  61.841  1.00 31.87  ? 59  ASN   A C   1 
ATOM   202  O  O   . ASN   A 1 31  ? -9.915  -2.818  62.360  1.00 31.48  ? 59  ASN   A O   1 
ATOM   203  C  CB  . ASN   A 1 31  ? -11.971 -4.941  60.841  1.00 33.95  ? 59  ASN   A CB  1 
ATOM   204  C  CG  . ASN   A 1 31  ? -12.984 -4.617  59.798  1.00 34.57  ? 59  ASN   A CG  1 
ATOM   205  O  OD1 . ASN   A 1 31  ? -13.769 -3.686  59.962  1.00 31.18  ? 59  ASN   A OD1 1 
ATOM   206  N  ND2 . ASN   A 1 31  ? -12.944 -5.344  58.677  1.00 35.66  ? 59  ASN   A ND2 1 
ATOM   207  N  N   . VAL   A 1 32  ? -9.128  -4.921  62.346  1.00 30.32  ? 60  VAL   A N   1 
ATOM   208  C  CA  . VAL   A 1 32  ? -8.312  -4.691  63.531  1.00 32.61  ? 60  VAL   A CA  1 
ATOM   209  C  C   . VAL   A 1 32  ? -7.260  -3.617  63.253  1.00 32.14  ? 60  VAL   A C   1 
ATOM   210  O  O   . VAL   A 1 32  ? -7.104  -2.664  64.029  1.00 32.04  ? 60  VAL   A O   1 
ATOM   211  C  CB  . VAL   A 1 32  ? -7.674  -6.011  64.002  1.00 28.46  ? 60  VAL   A CB  1 
ATOM   212  C  CG1 . VAL   A 1 32  ? -6.831  -5.765  65.241  1.00 33.63  ? 60  VAL   A CG1 1 
ATOM   213  C  CG2 . VAL   A 1 32  ? -8.778  -7.102  64.209  1.00 33.26  ? 60  VAL   A CG2 1 
ATOM   214  N  N   . ALA   A 1 33  ? -6.556  -3.731  62.120  1.00 30.63  ? 61  ALA   A N   1 
ATOM   215  C  CA  . ALA   A 1 33  ? -5.510  -2.751  61.813  1.00 33.45  ? 61  ALA   A CA  1 
ATOM   216  C  C   . ALA   A 1 33  ? -6.082  -1.348  61.656  1.00 34.46  ? 61  ALA   A C   1 
ATOM   217  O  O   . ALA   A 1 33  ? -5.415  -0.364  61.996  1.00 33.60  ? 61  ALA   A O   1 
ATOM   218  C  CB  . ALA   A 1 33  ? -4.743  -3.144  60.550  1.00 33.28  ? 61  ALA   A CB  1 
ATOM   219  N  N   . ARG   A 1 34  ? -7.299  -1.216  61.140  1.00 31.98  ? 62  ARG   A N   1 
ATOM   220  C  CA  . ARG   A 1 34  ? -7.799  0.156   60.985  1.00 32.98  ? 62  ARG   A CA  1 
ATOM   221  C  C   . ARG   A 1 34  ? -8.256  0.737   62.320  1.00 35.84  ? 62  ARG   A C   1 
ATOM   222  O  O   . ARG   A 1 34  ? -8.033  1.929   62.595  1.00 32.09  ? 62  ARG   A O   1 
ATOM   223  C  CB  . ARG   A 1 34  ? -8.903  0.194   59.942  1.00 35.68  ? 62  ARG   A CB  1 
ATOM   224  C  CG  . ARG   A 1 34  ? -8.393  -0.180  58.563  1.00 40.86  ? 62  ARG   A CG  1 
ATOM   225  C  CD  . ARG   A 1 34  ? -9.316  0.290   57.434  1.00 38.67  ? 62  ARG   A CD  1 
ATOM   226  N  NE  . ARG   A 1 34  ? -8.617  0.228   56.151  1.00 42.27  ? 62  ARG   A NE  1 
ATOM   227  C  CZ  . ARG   A 1 34  ? -8.850  1.012   55.101  1.00 44.95  ? 62  ARG   A CZ  1 
ATOM   228  N  NH1 . ARG   A 1 34  ? -8.137  0.840   53.998  1.00 45.98  ? 62  ARG   A NH1 1 
ATOM   229  N  NH2 . ARG   A 1 34  ? -9.793  1.954   55.133  1.00 39.80  ? 62  ARG   A NH2 1 
ATOM   230  N  N   . ARG   A 1 35  ? -8.866  -0.097  63.167  1.00 32.05  ? 63  ARG   A N   1 
ATOM   231  C  CA  . ARG   A 1 35  ? -9.201  0.298   64.536  1.00 33.36  ? 63  ARG   A CA  1 
ATOM   232  C  C   . ARG   A 1 35  ? -7.958  0.723   65.318  1.00 35.92  ? 63  ARG   A C   1 
ATOM   233  O  O   . ARG   A 1 35  ? -7.946  1.786   65.963  1.00 33.65  ? 63  ARG   A O   1 
ATOM   234  C  CB  . ARG   A 1 35  ? -9.942  -0.863  65.230  1.00 31.27  ? 63  ARG   A CB  1 
ATOM   235  C  CG  . ARG   A 1 35  ? -10.715 -0.503  66.523  1.00 35.95  ? 63  ARG   A CG  1 
ATOM   236  C  CD  . ARG   A 1 35  ? -9.779  -0.236  67.705  1.00 32.14  ? 63  ARG   A CD  1 
ATOM   237  N  NE  . ARG   A 1 35  ? -10.459 -0.006  68.980  1.00 34.64  ? 63  ARG   A NE  1 
ATOM   238  C  CZ  . ARG   A 1 35  ? -10.577 -0.927  69.937  1.00 36.28  ? 63  ARG   A CZ  1 
ATOM   239  N  NH1 . ARG   A 1 35  ? -11.199 -0.635  71.077  1.00 34.11  ? 63  ARG   A NH1 1 
ATOM   240  N  NH2 . ARG   A 1 35  ? -10.073 -2.149  69.750  1.00 33.79  ? 63  ARG   A NH2 1 
ATOM   241  N  N   . PHE   A 1 36  ? -6.904  -0.099  65.290  1.00 32.17  ? 64  PHE   A N   1 
ATOM   242  C  CA  . PHE   A 1 36  ? -5.686  0.230   66.029  1.00 34.44  ? 64  PHE   A CA  1 
ATOM   243  C  C   . PHE   A 1 36  ? -5.051  1.490   65.481  1.00 34.82  ? 64  PHE   A C   1 
ATOM   244  O  O   . PHE   A 1 36  ? -4.563  2.328   66.248  1.00 37.01  ? 64  PHE   A O   1 
ATOM   245  C  CB  . PHE   A 1 36  ? -4.667  -0.923  65.979  1.00 31.19  ? 64  PHE   A CB  1 
ATOM   246  C  CG  . PHE   A 1 36  ? -4.885  -1.980  67.040  1.00 31.42  ? 64  PHE   A CG  1 
ATOM   247  C  CD1 . PHE   A 1 36  ? -6.109  -2.629  67.135  1.00 33.61  ? 64  PHE   A CD1 1 
ATOM   248  C  CD2 . PHE   A 1 36  ? -3.866  -2.322  67.931  1.00 33.96  ? 64  PHE   A CD2 1 
ATOM   249  C  CE1 . PHE   A 1 36  ? -6.341  -3.571  68.098  1.00 31.56  ? 64  PHE   A CE1 1 
ATOM   250  C  CE2 . PHE   A 1 36  ? -4.078  -3.293  68.900  1.00 33.44  ? 64  PHE   A CE2 1 
ATOM   251  C  CZ  . PHE   A 1 36  ? -5.321  -3.925  68.975  1.00 31.50  ? 64  PHE   A CZ  1 
ATOM   252  N  N   . SER   A 1 37  ? -5.060  1.652   64.155  1.00 32.43  ? 65  SER   A N   1 
ATOM   253  C  CA  . SER   A 1 37  ? -4.411  2.821   63.550  1.00 34.89  ? 65  SER   A CA  1 
ATOM   254  C  C   . SER   A 1 37  ? -5.042  4.122   64.035  1.00 38.55  ? 65  SER   A C   1 
ATOM   255  O  O   . SER   A 1 37  ? -4.343  5.078   64.406  1.00 34.79  ? 65  SER   A O   1 
ATOM   256  C  CB  . SER   A 1 37  ? -4.494  2.717   62.026  1.00 37.58  ? 65  SER   A CB  1 
ATOM   257  O  OG  . SER   A 1 37  ? -3.980  3.884   61.413  1.00 40.45  ? 65  SER   A OG  1 
ATOM   258  N  N   . TRP   A 1 38  ? -6.372  4.176   64.022  1.00 33.51  ? 66  TRP   A N   1 
ATOM   259  C  CA  . TRP   A 1 38  ? -7.096  5.352   64.487  1.00 35.66  ? 66  TRP   A CA  1 
ATOM   260  C  C   . TRP   A 1 38  ? -6.972  5.515   65.997  1.00 33.60  ? 66  TRP   A C   1 
ATOM   261  O  O   . TRP   A 1 38  ? -6.767  6.631   66.500  1.00 34.61  ? 66  TRP   A O   1 
ATOM   262  C  CB  . TRP   A 1 38  ? -8.557  5.216   64.050  1.00 35.50  ? 66  TRP   A CB  1 
ATOM   263  C  CG  . TRP   A 1 38  ? -9.518  6.275   64.512  1.00 35.08  ? 66  TRP   A CG  1 
ATOM   264  C  CD1 . TRP   A 1 38  ? -10.724 6.064   65.128  1.00 35.08  ? 66  TRP   A CD1 1 
ATOM   265  C  CD2 . TRP   A 1 38  ? -9.379  7.700   64.375  1.00 36.21  ? 66  TRP   A CD2 1 
ATOM   266  N  NE1 . TRP   A 1 38  ? -11.346 7.258   65.376  1.00 36.15  ? 66  TRP   A NE1 1 
ATOM   267  C  CE2 . TRP   A 1 38  ? -10.541 8.281   64.931  1.00 39.22  ? 66  TRP   A CE2 1 
ATOM   268  C  CE3 . TRP   A 1 38  ? -8.396  8.536   63.829  1.00 34.76  ? 66  TRP   A CE3 1 
ATOM   269  C  CZ2 . TRP   A 1 38  ? -10.740 9.653   64.971  1.00 35.06  ? 66  TRP   A CZ2 1 
ATOM   270  C  CZ3 . TRP   A 1 38  ? -8.593  9.919   63.870  1.00 36.87  ? 66  TRP   A CZ3 1 
ATOM   271  C  CH2 . TRP   A 1 38  ? -9.761  10.460  64.433  1.00 40.43  ? 66  TRP   A CH2 1 
ATOM   272  N  N   . GLY   A 1 39  ? -7.072  4.405   66.728  1.00 31.30  ? 67  GLY   A N   1 
ATOM   273  C  CA  . GLY   A 1 39  ? -7.060  4.447   68.178  1.00 34.08  ? 67  GLY   A CA  1 
ATOM   274  C  C   . GLY   A 1 39  ? -5.729  4.855   68.783  1.00 34.48  ? 67  GLY   A C   1 
ATOM   275  O  O   . GLY   A 1 39  ? -5.705  5.525   69.819  1.00 33.96  ? 67  GLY   A O   1 
ATOM   276  N  N   . LEU   A 1 40  ? -4.610  4.444   68.170  1.00 31.17  ? 68  LEU   A N   1 
ATOM   277  C  CA  . LEU   A 1 40  ? -3.280  4.696   68.714  1.00 30.67  ? 68  LEU   A CA  1 
ATOM   278  C  C   . LEU   A 1 40  ? -2.474  5.707   67.907  1.00 34.31  ? 68  LEU   A C   1 
ATOM   279  O  O   . LEU   A 1 40  ? -1.387  6.093   68.345  1.00 33.30  ? 68  LEU   A O   1 
ATOM   280  C  CB  . LEU   A 1 40  ? -2.476  3.385   68.809  1.00 34.15  ? 68  LEU   A CB  1 
ATOM   281  C  CG  . LEU   A 1 40  ? -2.978  2.308   69.781  1.00 33.64  ? 68  LEU   A CG  1 
ATOM   282  C  CD1 . LEU   A 1 40  ? -2.757  0.864   69.251  1.00 33.31  ? 68  LEU   A CD1 1 
ATOM   283  C  CD2 . LEU   A 1 40  ? -2.290  2.475   71.130  1.00 31.83  ? 68  LEU   A CD2 1 
ATOM   284  N  N   . GLY   A 1 41  ? -2.961  6.119   66.741  1.00 36.10  ? 69  GLY   A N   1 
ATOM   285  C  CA  . GLY   A 1 41  ? -2.246  7.046   65.889  1.00 35.97  ? 69  GLY   A CA  1 
ATOM   286  C  C   . GLY   A 1 41  ? -1.014  6.426   65.279  1.00 38.59  ? 69  GLY   A C   1 
ATOM   287  O  O   . GLY   A 1 41  ? 0.108   6.897   65.486  1.00 40.13  ? 69  GLY   A O   1 
ATOM   288  N  N   . MET   A 1 42  ? -1.217  5.367   64.511  1.00 37.55  ? 70  MET   A N   1 
ATOM   289  C  CA  . MET   A 1 42  ? -0.140  4.672   63.833  1.00 34.50  ? 70  MET   A CA  1 
ATOM   290  C  C   . MET   A 1 42  ? -0.449  4.666   62.348  1.00 36.19  ? 70  MET   A C   1 
ATOM   291  O  O   . MET   A 1 42  ? -1.588  4.412   61.944  1.00 42.70  ? 70  MET   A O   1 
ATOM   292  C  CB  . MET   A 1 42  ? 0.010   3.229   64.354  1.00 34.82  ? 70  MET   A CB  1 
ATOM   293  C  CG  . MET   A 1 42  ? 0.091   3.095   65.873  1.00 34.56  ? 70  MET   A CG  1 
ATOM   294  S  SD  . MET   A 1 42  ? 0.332   1.388   66.482  1.00 40.06  ? 70  MET   A SD  1 
ATOM   295  C  CE  . MET   A 1 42  ? 1.780   0.901   65.552  1.00 31.43  ? 70  MET   A CE  1 
ATOM   296  N  N   . ARG   A 1 43  ? 0.574   4.886   61.541  1.00 35.42  ? 71  ARG   A N   1 
ATOM   297  C  CA  . ARG   A 1 43  ? 0.413   4.965   60.098  1.00 42.48  ? 71  ARG   A CA  1 
ATOM   298  C  C   . ARG   A 1 43  ? 0.440   3.585   59.452  1.00 40.72  ? 71  ARG   A C   1 
ATOM   299  O  O   . ARG   A 1 43  ? 1.213   2.725   59.868  1.00 38.79  ? 71  ARG   A O   1 
ATOM   300  C  CB  . ARG   A 1 43  ? 1.544   5.795   59.515  1.00 47.89  ? 71  ARG   A CB  1 
ATOM   301  C  CG  . ARG   A 1 43  ? 1.312   6.152   58.085  1.00 51.51  ? 71  ARG   A CG  1 
ATOM   302  C  CD  . ARG   A 1 43  ? 2.456   7.008   57.577  1.00 55.21  ? 71  ARG   A CD  1 
ATOM   303  N  NE  . ARG   A 1 43  ? 1.995   7.873   56.504  1.00 60.23  ? 71  ARG   A NE  1 
ATOM   304  C  CZ  . ARG   A 1 43  ? 2.787   8.650   55.772  1.00 61.07  ? 71  ARG   A CZ  1 
ATOM   305  N  NH1 . ARG   A 1 43  ? 2.264   9.406   54.810  1.00 63.82  ? 71  ARG   A NH1 1 
ATOM   306  N  NH2 . ARG   A 1 43  ? 4.097   8.678   55.982  1.00 67.20  ? 71  ARG   A NH2 1 
ATOM   307  N  N   . PHE   A 1 44  ? -0.375  3.382   58.407  1.00 38.13  ? 72  PHE   A N   1 
ATOM   308  C  CA  . PHE   A 1 44  ? -0.234  2.172   57.580  1.00 43.62  ? 72  PHE   A CA  1 
ATOM   309  C  C   . PHE   A 1 44  ? 1.029   2.302   56.728  1.00 47.77  ? 72  PHE   A C   1 
ATOM   310  O  O   . PHE   A 1 44  ? 1.124   3.211   55.893  1.00 41.56  ? 72  PHE   A O   1 
ATOM   311  C  CB  . PHE   A 1 44  ? -1.438  1.971   56.659  1.00 45.91  ? 72  PHE   A CB  1 
ATOM   312  C  CG  . PHE   A 1 44  ? -2.600  1.223   57.271  1.00 47.53  ? 72  PHE   A CG  1 
ATOM   313  C  CD1 . PHE   A 1 44  ? -2.858  -0.095  56.924  1.00 54.05  ? 72  PHE   A CD1 1 
ATOM   314  C  CD2 . PHE   A 1 44  ? -3.483  1.863   58.135  1.00 49.76  ? 72  PHE   A CD2 1 
ATOM   315  C  CE1 . PHE   A 1 44  ? -3.960  -0.781  57.462  1.00 46.86  ? 72  PHE   A CE1 1 
ATOM   316  C  CE2 . PHE   A 1 44  ? -4.575  1.194   58.676  1.00 43.44  ? 72  PHE   A CE2 1 
ATOM   317  C  CZ  . PHE   A 1 44  ? -4.818  -0.130  58.339  1.00 43.58  ? 72  PHE   A CZ  1 
ATOM   318  N  N   . SER   A 1 45  ? 1.998   1.399   56.915  1.00 40.24  ? 73  SER   A N   1 
ATOM   319  C  CA  . SER   A 1 45  ? 3.280   1.559   56.234  1.00 42.78  ? 73  SER   A CA  1 
ATOM   320  C  C   . SER   A 1 45  ? 3.679   0.417   55.308  1.00 44.44  ? 73  SER   A C   1 
ATOM   321  O  O   . SER   A 1 45  ? 4.384   0.674   54.332  1.00 46.28  ? 73  SER   A O   1 
ATOM   322  C  CB  . SER   A 1 45  ? 4.406   1.784   57.252  1.00 45.99  ? 73  SER   A CB  1 
ATOM   323  O  OG  . SER   A 1 45  ? 4.414   0.729   58.179  1.00 51.57  ? 73  SER   A OG  1 
ATOM   324  N  N   . ALA   A 1 46  ? 3.271   -0.826  55.567  1.00 35.44  ? 74  ALA   A N   1 
ATOM   325  C  CA  . ALA   A 1 46  ? 3.583   -1.892  54.624  1.00 40.17  ? 74  ALA   A CA  1 
ATOM   326  C  C   . ALA   A 1 46  ? 2.448   -2.906  54.609  1.00 39.80  ? 74  ALA   A C   1 
ATOM   327  O  O   . ALA   A 1 46  ? 1.712   -3.032  55.589  1.00 38.55  ? 74  ALA   A O   1 
ATOM   328  C  CB  . ALA   A 1 46  ? 4.900   -2.595  54.964  1.00 41.76  ? 74  ALA   A CB  1 
ATOM   329  N  N   . LYS   A 1 47  ? 2.301   -3.603  53.477  1.00 37.72  ? 75  LYS   A N   1 
ATOM   330  C  CA  . LYS   A 1 47  ? 1.286   -4.638  53.319  1.00 40.92  ? 75  LYS   A CA  1 
ATOM   331  C  C   . LYS   A 1 47  ? 1.879   -5.845  52.606  1.00 42.18  ? 75  LYS   A C   1 
ATOM   332  O  O   . LYS   A 1 47  ? 2.843   -5.743  51.842  1.00 40.98  ? 75  LYS   A O   1 
ATOM   333  C  CB  . LYS   A 1 47  ? 0.045   -4.153  52.531  1.00 38.47  ? 75  LYS   A CB  1 
ATOM   334  C  CG  . LYS   A 1 47  ? 0.292   -3.841  51.051  1.00 42.55  ? 75  LYS   A CG  1 
ATOM   335  C  CD  . LYS   A 1 47  ? -0.990  -3.384  50.308  1.00 41.82  ? 75  LYS   A CD  1 
ATOM   336  C  CE  . LYS   A 1 47  ? -0.629  -2.768  48.951  1.00 47.93  ? 75  LYS   A CE  1 
ATOM   337  N  NZ  . LYS   A 1 47  ? -1.808  -2.512  48.077  1.00 51.11  ? 75  LYS   A NZ  1 
ATOM   338  N  N   . SER   A 1 48  ? 1.273   -6.995  52.874  1.00 35.31  ? 76  SER   A N   1 
ATOM   339  C  CA  . SER   A 1 48  ? 1.531   -8.206  52.110  1.00 40.56  ? 76  SER   A CA  1 
ATOM   340  C  C   . SER   A 1 48  ? 0.194   -8.936  52.052  1.00 39.81  ? 76  SER   A C   1 
ATOM   341  O  O   . SER   A 1 48  ? -0.336  -9.319  53.094  1.00 38.30  ? 76  SER   A O   1 
ATOM   342  C  CB  . SER   A 1 48  ? 2.612   -9.059  52.763  1.00 36.47  ? 76  SER   A CB  1 
ATOM   343  O  OG  . SER   A 1 48  ? 2.713   -10.309 52.106  1.00 41.12  ? 76  SER   A OG  1 
ATOM   344  N  N   . ASP   A 1 49  ? -0.374  -9.075  50.863  1.00 39.99  ? 77  ASP   A N   1 
ATOM   345  C  CA  . ASP   A 1 49  ? -1.734  -9.596  50.738  1.00 44.08  ? 77  ASP   A CA  1 
ATOM   346  C  C   . ASP   A 1 49  ? -1.970  -9.971  49.277  1.00 42.10  ? 77  ASP   A C   1 
ATOM   347  O  O   . ASP   A 1 49  ? -1.025  -10.042 48.483  1.00 46.19  ? 77  ASP   A O   1 
ATOM   348  C  CB  . ASP   A 1 49  ? -2.758  -8.601  51.299  1.00 39.10  ? 77  ASP   A CB  1 
ATOM   349  C  CG  . ASP   A 1 49  ? -2.835  -7.296  50.517  1.00 44.78  ? 77  ASP   A CG  1 
ATOM   350  O  OD1 . ASP   A 1 49  ? -2.252  -7.170  49.422  1.00 45.44  ? 77  ASP   A OD1 1 
ATOM   351  O  OD2 . ASP   A 1 49  ? -3.521  -6.388  51.021  1.00 40.75  ? 77  ASP   A OD2 1 
ATOM   352  N  N   . LEU   A 1 50  ? -3.231  -10.247 48.931  1.00 40.25  ? 78  LEU   A N   1 
ATOM   353  C  CA  . LEU   A 1 50  ? -3.585  -10.556 47.546  1.00 45.57  ? 78  LEU   A CA  1 
ATOM   354  C  C   . LEU   A 1 50  ? -2.969  -9.563  46.563  1.00 47.82  ? 78  LEU   A C   1 
ATOM   355  O  O   . LEU   A 1 50  ? -2.462  -9.960  45.506  1.00 46.44  ? 78  LEU   A O   1 
ATOM   356  C  CB  . LEU   A 1 50  ? -5.111  -10.579 47.379  1.00 42.30  ? 78  LEU   A CB  1 
ATOM   357  C  CG  . LEU   A 1 50  ? -5.862  -11.662 48.162  1.00 43.42  ? 78  LEU   A CG  1 
ATOM   358  C  CD1 . LEU   A 1 50  ? -7.414  -11.519 48.049  1.00 39.44  ? 78  LEU   A CD1 1 
ATOM   359  C  CD2 . LEU   A 1 50  ? -5.402  -13.038 47.723  1.00 41.01  ? 78  LEU   A CD2 1 
ATOM   360  N  N   . SER   A 1 51  ? -2.988  -8.270  46.905  1.00 42.43  ? 79  SER   A N   1 
ATOM   361  C  CA  . SER   A 1 51  ? -2.519  -7.246  45.981  1.00 47.54  ? 79  SER   A CA  1 
ATOM   362  C  C   . SER   A 1 51  ? -1.019  -7.325  45.743  1.00 52.52  ? 79  SER   A C   1 
ATOM   363  O  O   . SER   A 1 51  ? -0.535  -6.792  44.738  1.00 55.35  ? 79  SER   A O   1 
ATOM   364  C  CB  . SER   A 1 51  ? -2.876  -5.853  46.506  1.00 47.77  ? 79  SER   A CB  1 
ATOM   365  O  OG  . SER   A 1 51  ? -1.971  -5.461  47.531  1.00 47.57  ? 79  SER   A OG  1 
ATOM   366  N  N   . THR   A 1 52  ? -0.273  -7.948  46.655  1.00 49.36  ? 80  THR   A N   1 
ATOM   367  C  CA  . THR   A 1 52  ? 1.161   -8.126  46.497  1.00 48.66  ? 80  THR   A CA  1 
ATOM   368  C  C   . THR   A 1 52  ? 1.515   -9.554  46.111  1.00 50.67  ? 80  THR   A C   1 
ATOM   369  O  O   . THR   A 1 52  ? 2.697   -9.911  46.111  1.00 52.07  ? 80  THR   A O   1 
ATOM   370  C  CB  . THR   A 1 52  ? 1.898   -7.733  47.781  1.00 47.24  ? 80  THR   A CB  1 
ATOM   371  O  OG1 . THR   A 1 52  ? 1.640   -8.710  48.794  1.00 46.50  ? 80  THR   A OG1 1 
ATOM   372  C  CG2 . THR   A 1 52  ? 1.438   -6.364  48.273  1.00 47.90  ? 80  THR   A CG2 1 
ATOM   373  N  N   . GLY   A 1 53  ? 0.520   -10.370 45.776  1.00 51.67  ? 81  GLY   A N   1 
ATOM   374  C  CA  . GLY   A 1 53  ? 0.744   -11.736 45.355  1.00 50.98  ? 81  GLY   A CA  1 
ATOM   375  C  C   . GLY   A 1 53  ? 0.823   -12.757 46.468  1.00 53.29  ? 81  GLY   A C   1 
ATOM   376  O  O   . GLY   A 1 53  ? 1.247   -13.888 46.213  1.00 52.06  ? 81  GLY   A O   1 
ATOM   377  N  N   . ASN   A 1 54  ? 0.429   -12.400 47.687  1.00 51.80  ? 82  ASN   A N   1 
ATOM   378  C  CA  . ASN   A 1 54  ? 0.412   -13.323 48.819  1.00 45.77  ? 82  ASN   A CA  1 
ATOM   379  C  C   . ASN   A 1 54  ? -0.965  -13.985 48.879  1.00 44.67  ? 82  ASN   A C   1 
ATOM   380  O  O   . ASN   A 1 54  ? -1.947  -13.356 49.288  1.00 45.57  ? 82  ASN   A O   1 
ATOM   381  C  CB  . ASN   A 1 54  ? 0.750   -12.561 50.103  1.00 44.86  ? 82  ASN   A CB  1 
ATOM   382  C  CG  . ASN   A 1 54  ? 0.806   -13.449 51.332  1.00 42.15  ? 82  ASN   A CG  1 
ATOM   383  O  OD1 . ASN   A 1 54  ? 0.315   -14.571 51.330  1.00 41.38  ? 82  ASN   A OD1 1 
ATOM   384  N  ND2 . ASN   A 1 54  ? 1.370   -12.923 52.405  1.00 38.59  ? 82  ASN   A ND2 1 
ATOM   385  N  N   . MET   A 1 55  ? -1.036  -15.258 48.467  1.00 42.38  ? 83  MET   A N   1 
ATOM   386  C  CA  . MET   A 1 55  ? -2.274  -16.036 48.459  1.00 45.90  ? 83  MET   A CA  1 
ATOM   387  C  C   . MET   A 1 55  ? -2.551  -16.730 49.784  1.00 44.33  ? 83  MET   A C   1 
ATOM   388  O  O   . MET   A 1 55  ? -3.506  -17.511 49.867  1.00 38.80  ? 83  MET   A O   1 
ATOM   389  C  CB  . MET   A 1 55  ? -2.231  -17.118 47.365  1.00 44.20  ? 83  MET   A CB  1 
ATOM   390  C  CG  . MET   A 1 55  ? -1.842  -16.634 45.987  1.00 51.00  ? 83  MET   A CG  1 
ATOM   391  S  SD  . MET   A 1 55  ? -3.186  -15.725 45.203  1.00 69.62  ? 83  MET   A SD  1 
ATOM   392  C  CE  . MET   A 1 55  ? -2.650  -14.044 45.485  1.00 50.39  ? 83  MET   A CE  1 
ATOM   393  N  N   . VAL   A 1 56  ? -1.728  -16.505 50.806  1.00 39.82  ? 84  VAL   A N   1 
ATOM   394  C  CA  . VAL   A 1 56  ? -1.780  -17.290 52.035  1.00 43.29  ? 84  VAL   A CA  1 
ATOM   395  C  C   . VAL   A 1 56  ? -2.359  -16.481 53.182  1.00 35.88  ? 84  VAL   A C   1 
ATOM   396  O  O   . VAL   A 1 56  ? -3.310  -16.909 53.838  1.00 35.42  ? 84  VAL   A O   1 
ATOM   397  C  CB  . VAL   A 1 56  ? -0.388  -17.856 52.396  1.00 40.49  ? 84  VAL   A CB  1 
ATOM   398  C  CG1 . VAL   A 1 56  ? -0.446  -18.556 53.744  1.00 41.95  ? 84  VAL   A CG1 1 
ATOM   399  C  CG2 . VAL   A 1 56  ? 0.064   -18.831 51.318  1.00 41.09  ? 84  VAL   A CG2 1 
ATOM   400  N  N   . HIS   A 1 57  ? -1.766  -15.336 53.475  1.00 34.76  ? 85  HIS   A N   1 
ATOM   401  C  CA  . HIS   A 1 57  ? -2.212  -14.508 54.574  1.00 37.12  ? 85  HIS   A CA  1 
ATOM   402  C  C   . HIS   A 1 57  ? -2.249  -13.059 54.125  1.00 41.47  ? 85  HIS   A C   1 
ATOM   403  O  O   . HIS   A 1 57  ? -1.525  -12.643 53.214  1.00 42.84  ? 85  HIS   A O   1 
ATOM   404  C  CB  . HIS   A 1 57  ? -1.324  -14.651 55.818  1.00 35.63  ? 85  HIS   A CB  1 
ATOM   405  C  CG  . HIS   A 1 57  ? 0.141   -14.404 55.574  1.00 39.72  ? 85  HIS   A CG  1 
ATOM   406  N  ND1 . HIS   A 1 57  ? 0.746   -13.193 55.833  1.00 37.84  ? 85  HIS   A ND1 1 
ATOM   407  C  CD2 . HIS   A 1 57  ? 1.126   -15.225 55.132  1.00 35.81  ? 85  HIS   A CD2 1 
ATOM   408  C  CE1 . HIS   A 1 57  ? 2.038   -13.277 55.557  1.00 39.01  ? 85  HIS   A CE1 1 
ATOM   409  N  NE2 . HIS   A 1 57  ? 2.289   -14.493 55.108  1.00 40.68  ? 85  HIS   A NE2 1 
ATOM   410  N  N   . ALA   A 1 58  ? -3.118  -12.306 54.782  1.00 34.87  ? 86  ALA   A N   1 
ATOM   411  C  CA  . ALA   A 1 58  ? -3.136  -10.857 54.705  1.00 35.26  ? 86  ALA   A CA  1 
ATOM   412  C  C   . ALA   A 1 58  ? -2.433  -10.299 55.937  1.00 36.24  ? 86  ALA   A C   1 
ATOM   413  O  O   . ALA   A 1 58  ? -2.774  -10.670 57.062  1.00 33.22  ? 86  ALA   A O   1 
ATOM   414  C  CB  . ALA   A 1 58  ? -4.585  -10.359 54.619  1.00 36.08  ? 86  ALA   A CB  1 
ATOM   415  N  N   . SER   A 1 59  ? -1.439  -9.425  55.727  1.00 33.61  ? 87  SER   A N   1 
ATOM   416  C  CA  . SER   A 1 59  ? -0.644  -8.864  56.810  1.00 33.48  ? 87  SER   A CA  1 
ATOM   417  C  C   . SER   A 1 59  ? -0.466  -7.372  56.572  1.00 37.67  ? 87  SER   A C   1 
ATOM   418  O  O   . SER   A 1 59  ? 0.009   -6.964  55.506  1.00 37.90  ? 87  SER   A O   1 
ATOM   419  C  CB  . SER   A 1 59  ? 0.754   -9.519  56.929  1.00 35.35  ? 87  SER   A CB  1 
ATOM   420  O  OG  . SER   A 1 59  ? 0.690   -10.880 57.357  1.00 35.91  ? 87  SER   A OG  1 
ATOM   421  N  N   . TYR   A 1 60  ? -0.791  -6.569  57.581  1.00 35.42  ? 88  TYR   A N   1 
ATOM   422  C  CA  . TYR   A 1 60  ? -0.716  -5.115  57.474  1.00 34.05  ? 88  TYR   A CA  1 
ATOM   423  C  C   . TYR   A 1 60  ? 0.133   -4.597  58.620  1.00 33.97  ? 88  TYR   A C   1 
ATOM   424  O  O   . TYR   A 1 60  ? -0.054  -5.003  59.772  1.00 33.43  ? 88  TYR   A O   1 
ATOM   425  C  CB  . TYR   A 1 60  ? -2.132  -4.490  57.472  1.00 33.47  ? 88  TYR   A CB  1 
ATOM   426  C  CG  . TYR   A 1 60  ? -2.969  -5.029  56.334  1.00 35.50  ? 88  TYR   A CG  1 
ATOM   427  C  CD1 . TYR   A 1 60  ? -2.651  -4.724  55.021  1.00 36.31  ? 88  TYR   A CD1 1 
ATOM   428  C  CD2 . TYR   A 1 60  ? -4.043  -5.889  56.568  1.00 37.90  ? 88  TYR   A CD2 1 
ATOM   429  C  CE1 . TYR   A 1 60  ? -3.382  -5.241  53.969  1.00 38.48  ? 88  TYR   A CE1 1 
ATOM   430  C  CE2 . TYR   A 1 60  ? -4.792  -6.412  55.515  1.00 35.93  ? 88  TYR   A CE2 1 
ATOM   431  C  CZ  . TYR   A 1 60  ? -4.449  -6.083  54.219  1.00 38.19  ? 88  TYR   A CZ  1 
ATOM   432  O  OH  . TYR   A 1 60  ? -5.160  -6.579  53.156  1.00 38.76  ? 88  TYR   A OH  1 
ATOM   433  N  N   . LEU   A 1 61  ? 1.084   -3.724  58.299  1.00 33.75  ? 89  LEU   A N   1 
ATOM   434  C  CA  . LEU   A 1 61  ? 2.006   -3.183  59.282  1.00 32.59  ? 89  LEU   A CA  1 
ATOM   435  C  C   . LEU   A 1 61  ? 1.632   -1.747  59.603  1.00 32.60  ? 89  LEU   A C   1 
ATOM   436  O  O   . LEU   A 1 61  ? 1.414   -0.941  58.693  1.00 36.23  ? 89  LEU   A O   1 
ATOM   437  C  CB  . LEU   A 1 61  ? 3.452   -3.256  58.768  1.00 33.17  ? 89  LEU   A CB  1 
ATOM   438  C  CG  . LEU   A 1 61  ? 4.484   -2.825  59.785  1.00 37.94  ? 89  LEU   A CG  1 
ATOM   439  C  CD1 . LEU   A 1 61  ? 4.608   -3.927  60.827  1.00 39.53  ? 89  LEU   A CD1 1 
ATOM   440  C  CD2 . LEU   A 1 61  ? 5.822   -2.551  59.094  1.00 42.37  ? 89  LEU   A CD2 1 
ATOM   441  N  N   . LEU   A 1 62  ? 1.500   -1.451  60.890  1.00 31.77  ? 90  LEU   A N   1 
ATOM   442  C  CA  . LEU   A 1 62  ? 1.327   -0.086  61.363  1.00 38.30  ? 90  LEU   A CA  1 
ATOM   443  C  C   . LEU   A 1 62  ? 2.586   0.326   62.103  1.00 31.93  ? 90  LEU   A C   1 
ATOM   444  O  O   . LEU   A 1 62  ? 3.224   -0.498  62.766  1.00 33.43  ? 90  LEU   A O   1 
ATOM   445  C  CB  . LEU   A 1 62  ? 0.133   0.057   62.302  1.00 34.21  ? 90  LEU   A CB  1 
ATOM   446  C  CG  . LEU   A 1 62  ? -1.235  -0.465  61.871  1.00 35.19  ? 90  LEU   A CG  1 
ATOM   447  C  CD1 . LEU   A 1 62  ? -2.253  -0.037  62.901  1.00 36.58  ? 90  LEU   A CD1 1 
ATOM   448  C  CD2 . LEU   A 1 62  ? -1.599  0.077   60.506  1.00 39.01  ? 90  LEU   A CD2 1 
ATOM   449  N  N   . THR   A 1 63  ? 2.953   1.603   61.994  1.00 34.59  ? 91  THR   A N   1 
ATOM   450  C  CA  . THR   A 1 63  ? 4.183   2.064   62.631  1.00 38.39  ? 91  THR   A CA  1 
ATOM   451  C  C   . THR   A 1 63  ? 3.926   3.402   63.305  1.00 33.53  ? 91  THR   A C   1 
ATOM   452  O  O   . THR   A 1 63  ? 3.163   4.224   62.792  1.00 35.33  ? 91  THR   A O   1 
ATOM   453  C  CB  . THR   A 1 63  ? 5.341   2.227   61.638  1.00 36.86  ? 91  THR   A CB  1 
ATOM   454  O  OG1 . THR   A 1 63  ? 5.026   3.269   60.703  1.00 45.91  ? 91  THR   A OG1 1 
ATOM   455  C  CG2 . THR   A 1 63  ? 5.607   0.949   60.899  1.00 39.41  ? 91  THR   A CG2 1 
ATOM   456  N  N   . SER   A 1 64  ? 4.530   3.592   64.475  1.00 35.89  ? 92  SER   A N   1 
ATOM   457  C  CA  . SER   A 1 64  ? 4.579   4.900   65.138  1.00 36.77  ? 92  SER   A CA  1 
ATOM   458  C  C   . SER   A 1 64  ? 5.953   5.037   65.771  1.00 38.76  ? 92  SER   A C   1 
ATOM   459  O  O   . SER   A 1 64  ? 6.272   4.304   66.713  1.00 37.66  ? 92  SER   A O   1 
ATOM   460  C  CB  . SER   A 1 64  ? 3.481   5.042   66.200  1.00 38.77  ? 92  SER   A CB  1 
ATOM   461  O  OG  . SER   A 1 64  ? 3.285   6.407   66.562  1.00 39.54  ? 92  SER   A OG  1 
ATOM   462  N  N   . GLY   A 1 65  ? 6.758   5.970   65.266  1.00 40.70  ? 93  GLY   A N   1 
ATOM   463  C  CA  . GLY   A 1 65  ? 8.152   6.048   65.704  1.00 35.60  ? 93  GLY   A CA  1 
ATOM   464  C  C   . GLY   A 1 65  ? 8.854   4.738   65.365  1.00 40.32  ? 93  GLY   A C   1 
ATOM   465  O  O   . GLY   A 1 65  ? 8.884   4.303   64.209  1.00 41.69  ? 93  GLY   A O   1 
ATOM   466  N  N   . ASP   A 1 66  ? 9.413   4.070   66.366  1.00 37.25  ? 94  ASP   A N   1 
ATOM   467  C  CA  . ASP   A 1 66  ? 10.017  2.766   66.134  1.00 38.09  ? 94  ASP   A CA  1 
ATOM   468  C  C   . ASP   A 1 66  ? 9.060   1.609   66.385  1.00 37.26  ? 94  ASP   A C   1 
ATOM   469  O  O   . ASP   A 1 66  ? 9.468   0.448   66.244  1.00 35.91  ? 94  ASP   A O   1 
ATOM   470  C  CB  . ASP   A 1 66  ? 11.249  2.569   67.011  1.00 43.29  ? 94  ASP   A CB  1 
ATOM   471  C  CG  . ASP   A 1 66  ? 12.396  3.431   66.582  1.00 51.35  ? 94  ASP   A CG  1 
ATOM   472  O  OD1 . ASP   A 1 66  ? 12.528  3.681   65.364  1.00 51.52  ? 94  ASP   A OD1 1 
ATOM   473  O  OD2 . ASP   A 1 66  ? 13.158  3.859   67.467  1.00 63.84  ? 94  ASP   A OD2 1 
ATOM   474  N  N   . LEU   A 1 67  ? 7.829   1.881   66.801  1.00 34.64  ? 95  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 67  ? 6.907   0.796   67.111  1.00 35.82  ? 95  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 67  ? 6.377   0.200   65.812  1.00 34.32  ? 95  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 67  ? 5.960   0.930   64.911  1.00 34.18  ? 95  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 67  ? 5.752   1.311   67.977  1.00 36.54  ? 95  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 67  ? 4.720   0.286   68.473  1.00 32.32  ? 95  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 67  ? 5.360   -0.703  69.404  1.00 32.46  ? 95  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 67  ? 3.554   0.980   69.170  1.00 32.09  ? 95  LEU   A CD2 1 
ATOM   482  N  N   . ARG   A 1 68  ? 6.409   -1.123  65.696  1.00 34.96  ? 96  ARG   A N   1 
ATOM   483  C  CA  . ARG   A 1 68  ? 5.830   -1.792  64.535  1.00 33.79  ? 96  ARG   A CA  1 
ATOM   484  C  C   . ARG   A 1 68  ? 4.837   -2.836  65.030  1.00 36.17  ? 96  ARG   A C   1 
ATOM   485  O  O   . ARG   A 1 68  ? 5.234   -3.798  65.696  1.00 34.25  ? 96  ARG   A O   1 
ATOM   486  C  CB  . ARG   A 1 68  ? 6.887   -2.458  63.658  1.00 34.32  ? 96  ARG   A CB  1 
ATOM   487  C  CG  . ARG   A 1 68  ? 7.986   -1.583  63.062  1.00 40.92  ? 96  ARG   A CG  1 
ATOM   488  C  CD  . ARG   A 1 68  ? 8.901   -2.519  62.259  1.00 44.69  ? 96  ARG   A CD  1 
ATOM   489  N  NE  . ARG   A 1 68  ? 10.065  -1.849  61.708  1.00 51.72  ? 96  ARG   A NE  1 
ATOM   490  C  CZ  . ARG   A 1 68  ? 11.250  -1.808  62.307  1.00 54.25  ? 96  ARG   A CZ  1 
ATOM   491  N  NH1 . ARG   A 1 68  ? 11.428  -2.416  63.473  1.00 50.18  ? 96  ARG   A NH1 1 
ATOM   492  N  NH2 . ARG   A 1 68  ? 12.261  -1.163  61.738  1.00 58.42  ? 96  ARG   A NH2 1 
ATOM   493  N  N   . PHE   A 1 69  ? 3.559   -2.633  64.717  1.00 33.40  ? 97  PHE   A N   1 
ATOM   494  C  CA  . PHE   A 1 69  ? 2.500   -3.625  64.936  1.00 34.56  ? 97  PHE   A CA  1 
ATOM   495  C  C   . PHE   A 1 69  ? 2.135   -4.278  63.612  1.00 30.53  ? 97  PHE   A C   1 
ATOM   496  O  O   . PHE   A 1 69  ? 1.748   -3.581  62.668  1.00 32.18  ? 97  PHE   A O   1 
ATOM   497  C  CB  . PHE   A 1 69  ? 1.231   -2.990  65.525  1.00 30.00  ? 97  PHE   A CB  1 
ATOM   498  C  CG  . PHE   A 1 69  ? 1.275   -2.757  67.017  1.00 32.86  ? 97  PHE   A CG  1 
ATOM   499  C  CD1 . PHE   A 1 69  ? 2.395   -3.137  67.774  1.00 36.09  ? 97  PHE   A CD1 1 
ATOM   500  C  CD2 . PHE   A 1 69  ? 0.191   -2.141  67.664  1.00 33.60  ? 97  PHE   A CD2 1 
ATOM   501  C  CE1 . PHE   A 1 69  ? 2.435   -2.922  69.148  1.00 34.82  ? 97  PHE   A CE1 1 
ATOM   502  C  CE2 . PHE   A 1 69  ? 0.217   -1.920  69.036  1.00 37.39  ? 97  PHE   A CE2 1 
ATOM   503  C  CZ  . PHE   A 1 69  ? 1.342   -2.303  69.782  1.00 36.30  ? 97  PHE   A CZ  1 
ATOM   504  N  N   . LEU   A 1 70  ? 2.193   -5.611  63.564  1.00 31.18  ? 98  LEU   A N   1 
ATOM   505  C  CA  . LEU   A 1 70  ? 1.784   -6.392  62.401  1.00 29.44  ? 98  LEU   A CA  1 
ATOM   506  C  C   . LEU   A 1 70  ? 0.477   -7.124  62.700  1.00 32.37  ? 98  LEU   A C   1 
ATOM   507  O  O   . LEU   A 1 70  ? 0.353   -7.772  63.747  1.00 32.86  ? 98  LEU   A O   1 
ATOM   508  C  CB  . LEU   A 1 70  ? 2.873   -7.401  62.018  1.00 32.54  ? 98  LEU   A CB  1 
ATOM   509  C  CG  . LEU   A 1 70  ? 2.701   -8.178  60.717  1.00 34.34  ? 98  LEU   A CG  1 
ATOM   510  C  CD1 . LEU   A 1 70  ? 2.694   -7.238  59.517  1.00 34.61  ? 98  LEU   A CD1 1 
ATOM   511  C  CD2 . LEU   A 1 70  ? 3.808   -9.214  60.612  1.00 35.73  ? 98  LEU   A CD2 1 
ATOM   512  N  N   . PHE   A 1 71  ? -0.486  -7.032  61.779  1.00 29.10  ? 99  PHE   A N   1 
ATOM   513  C  CA  . PHE   A 1 71  ? -1.794  -7.673  61.909  1.00 29.03  ? 99  PHE   A CA  1 
ATOM   514  C  C   . PHE   A 1 71  ? -1.943  -8.666  60.766  1.00 32.72  ? 99  PHE   A C   1 
ATOM   515  O  O   . PHE   A 1 71  ? -1.864  -8.284  59.594  1.00 31.96  ? 99  PHE   A O   1 
ATOM   516  C  CB  . PHE   A 1 71  ? -2.938  -6.630  61.899  1.00 27.49  ? 99  PHE   A CB  1 
ATOM   517  C  CG  . PHE   A 1 71  ? -2.797  -5.590  62.980  1.00 32.40  ? 99  PHE   A CG  1 
ATOM   518  C  CD1 . PHE   A 1 71  ? -1.969  -4.492  62.792  1.00 30.58  ? 99  PHE   A CD1 1 
ATOM   519  C  CD2 . PHE   A 1 71  ? -3.412  -5.754  64.212  1.00 31.64  ? 99  PHE   A CD2 1 
ATOM   520  C  CE1 . PHE   A 1 71  ? -1.800  -3.541  63.794  1.00 27.86  ? 99  PHE   A CE1 1 
ATOM   521  C  CE2 . PHE   A 1 71  ? -3.223  -4.820  65.225  1.00 31.68  ? 99  PHE   A CE2 1 
ATOM   522  C  CZ  . PHE   A 1 71  ? -2.419  -3.718  65.011  1.00 30.88  ? 99  PHE   A CZ  1 
ATOM   523  N  N   . THR   A 1 72  ? -2.166  -9.939  61.103  1.00 32.71  ? 100 THR   A N   1 
ATOM   524  C  CA  . THR   A 1 72  ? -2.195  -10.996 60.101  1.00 30.96  ? 100 THR   A CA  1 
ATOM   525  C  C   . THR   A 1 72  ? -3.392  -11.903 60.313  1.00 30.54  ? 100 THR   A C   1 
ATOM   526  O  O   . THR   A 1 72  ? -3.684  -12.298 61.442  1.00 33.45  ? 100 THR   A O   1 
ATOM   527  C  CB  . THR   A 1 72  ? -0.920  -11.868 60.150  1.00 30.51  ? 100 THR   A CB  1 
ATOM   528  O  OG1 . THR   A 1 72  ? 0.224   -11.063 59.858  1.00 32.58  ? 100 THR   A OG1 1 
ATOM   529  C  CG2 . THR   A 1 72  ? -1.018  -12.983 59.131  1.00 32.04  ? 100 THR   A CG2 1 
ATOM   530  N  N   . ALA   A 1 73  ? -4.048  -12.256 59.217  1.00 29.33  ? 101 ALA   A N   1 
ATOM   531  C  CA  . ALA   A 1 73  ? -5.164  -13.193 59.217  1.00 30.76  ? 101 ALA   A CA  1 
ATOM   532  C  C   . ALA   A 1 73  ? -5.013  -14.112 58.017  1.00 36.14  ? 101 ALA   A C   1 
ATOM   533  O  O   . ALA   A 1 73  ? -4.397  -13.726 57.018  1.00 35.60  ? 101 ALA   A O   1 
ATOM   534  C  CB  . ALA   A 1 73  ? -6.511  -12.460 59.144  1.00 29.81  ? 101 ALA   A CB  1 
ATOM   535  N  N   . PRO   A 1 74  ? -5.563  -15.330 58.082  1.00 37.68  ? 102 PRO   A N   1 
ATOM   536  C  CA  . PRO   A 1 74  ? -5.468  -16.260 56.951  1.00 36.20  ? 102 PRO   A CA  1 
ATOM   537  C  C   . PRO   A 1 74  ? -6.552  -16.028 55.906  1.00 38.96  ? 102 PRO   A C   1 
ATOM   538  O  O   . PRO   A 1 74  ? -7.678  -15.643 56.217  1.00 39.36  ? 102 PRO   A O   1 
ATOM   539  C  CB  . PRO   A 1 74  ? -5.667  -17.626 57.629  1.00 38.88  ? 102 PRO   A CB  1 
ATOM   540  C  CG  . PRO   A 1 74  ? -6.631  -17.352 58.749  1.00 36.59  ? 102 PRO   A CG  1 
ATOM   541  C  CD  . PRO   A 1 74  ? -6.330  -15.901 59.206  1.00 37.82  ? 102 PRO   A CD  1 
ATOM   542  N  N   . TYR   A 1 75  ? -6.201  -16.270 54.641  1.00 38.05  ? 103 TYR   A N   1 
ATOM   543  C  CA  . TYR   A 1 75  ? -7.220  -16.391 53.598  1.00 36.24  ? 103 TYR   A CA  1 
ATOM   544  C  C   . TYR   A 1 75  ? -7.765  -17.818 53.580  1.00 38.44  ? 103 TYR   A C   1 
ATOM   545  O  O   . TYR   A 1 75  ? -7.300  -18.690 54.320  1.00 39.96  ? 103 TYR   A O   1 
ATOM   546  C  CB  . TYR   A 1 75  ? -6.654  -16.049 52.220  1.00 37.79  ? 103 TYR   A CB  1 
ATOM   547  C  CG  . TYR   A 1 75  ? -6.188  -14.610 52.031  1.00 39.07  ? 103 TYR   A CG  1 
ATOM   548  C  CD1 . TYR   A 1 75  ? -7.092  -13.552 52.098  1.00 38.52  ? 103 TYR   A CD1 1 
ATOM   549  C  CD2 . TYR   A 1 75  ? -4.866  -14.330 51.722  1.00 39.26  ? 103 TYR   A CD2 1 
ATOM   550  C  CE1 . TYR   A 1 75  ? -6.688  -12.254 51.896  1.00 37.10  ? 103 TYR   A CE1 1 
ATOM   551  C  CE2 . TYR   A 1 75  ? -4.440  -13.027 51.523  1.00 38.83  ? 103 TYR   A CE2 1 
ATOM   552  C  CZ  . TYR   A 1 75  ? -5.353  -11.999 51.617  1.00 42.76  ? 103 TYR   A CZ  1 
ATOM   553  O  OH  . TYR   A 1 75  ? -4.930  -10.709 51.417  1.00 43.51  ? 103 TYR   A OH  1 
ATOM   554  N  N   . SER   A 1 76  ? -8.738  -18.076 52.709  1.00 37.26  ? 104 SER   A N   1 
ATOM   555  C  CA  . SER   A 1 76  ? -9.178  -19.460 52.491  1.00 36.52  ? 104 SER   A CA  1 
ATOM   556  C  C   . SER   A 1 76  ? -7.991  -20.325 52.069  1.00 40.24  ? 104 SER   A C   1 
ATOM   557  O  O   . SER   A 1 76  ? -7.287  -19.972 51.113  1.00 38.73  ? 104 SER   A O   1 
ATOM   558  C  CB  . SER   A 1 76  ? -10.262 -19.542 51.417  1.00 41.96  ? 104 SER   A CB  1 
ATOM   559  O  OG  . SER   A 1 76  ? -10.438 -20.900 51.016  1.00 44.60  ? 104 SER   A OG  1 
ATOM   560  N  N   . PRO   A 1 77  ? -7.751  -21.478 52.726  1.00 41.25  ? 105 PRO   A N   1 
ATOM   561  C  CA  . PRO   A 1 77  ? -6.634  -22.343 52.296  1.00 43.33  ? 105 PRO   A CA  1 
ATOM   562  C  C   . PRO   A 1 77  ? -6.725  -22.693 50.819  1.00 44.77  ? 105 PRO   A C   1 
ATOM   563  O  O   . PRO   A 1 77  ? -5.701  -22.945 50.177  1.00 45.43  ? 105 PRO   A O   1 
ATOM   564  C  CB  . PRO   A 1 77  ? -6.778  -23.587 53.185  1.00 45.76  ? 105 PRO   A CB  1 
ATOM   565  C  CG  . PRO   A 1 77  ? -7.494  -23.103 54.399  1.00 47.80  ? 105 PRO   A CG  1 
ATOM   566  C  CD  . PRO   A 1 77  ? -8.440  -22.010 53.915  1.00 40.06  ? 105 PRO   A CD  1 
ATOM   567  N  N   . SER   A 1 78  ? -7.940  -22.645 50.258  1.00 44.18  ? 106 SER   A N   1 
ATOM   568  C  CA  . SER   A 1 78  ? -8.147  -23.022 48.863  1.00 47.76  ? 106 SER   A CA  1 
ATOM   569  C  C   . SER   A 1 78  ? -7.412  -22.108 47.890  1.00 45.49  ? 106 SER   A C   1 
ATOM   570  O  O   . SER   A 1 78  ? -7.148  -22.519 46.754  1.00 47.58  ? 106 SER   A O   1 
ATOM   571  C  CB  . SER   A 1 78  ? -9.649  -23.056 48.525  1.00 46.03  ? 106 SER   A CB  1 
ATOM   572  O  OG  . SER   A 1 78  ? -10.286 -21.810 48.754  1.00 50.41  ? 106 SER   A OG  1 
ATOM   573  N  N   . LEU   A 1 79  ? -7.038  -20.896 48.299  1.00 41.91  ? 107 LEU   A N   1 
ATOM   574  C  CA  . LEU   A 1 79  ? -6.326  -20.040 47.361  1.00 40.37  ? 107 LEU   A CA  1 
ATOM   575  C  C   . LEU   A 1 79  ? -4.897  -20.505 47.158  1.00 45.33  ? 107 LEU   A C   1 
ATOM   576  O  O   . LEU   A 1 79  ? -4.263  -20.125 46.166  1.00 47.03  ? 107 LEU   A O   1 
ATOM   577  C  CB  . LEU   A 1 79  ? -6.342  -18.585 47.838  1.00 41.88  ? 107 LEU   A CB  1 
ATOM   578  C  CG  . LEU   A 1 79  ? -7.705  -17.938 48.070  1.00 45.94  ? 107 LEU   A CG  1 
ATOM   579  C  CD1 . LEU   A 1 79  ? -7.546  -16.459 48.332  1.00 44.52  ? 107 LEU   A CD1 1 
ATOM   580  C  CD2 . LEU   A 1 79  ? -8.652  -18.164 46.888  1.00 45.38  ? 107 LEU   A CD2 1 
ATOM   581  N  N   . SER   A 1 80  ? -4.377  -21.310 48.082  1.00 43.15  ? 108 SER   A N   1 
ATOM   582  C  CA  . SER   A 1 80  ? -2.982  -21.723 48.051  1.00 46.00  ? 108 SER   A CA  1 
ATOM   583  C  C   . SER   A 1 80  ? -2.854  -23.237 48.106  1.00 47.04  ? 108 SER   A C   1 
ATOM   584  O  O   . SER   A 1 80  ? -1.809  -23.746 48.530  1.00 47.10  ? 108 SER   A O   1 
ATOM   585  C  CB  . SER   A 1 80  ? -2.201  -21.088 49.209  1.00 44.80  ? 108 SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 80  ? -2.716  -21.531 50.455  1.00 40.37  ? 108 SER   A OG  1 
ATOM   587  N  N   . ALA   A 1 81  ? -3.896  -23.956 47.681  1.00 44.66  ? 109 ALA   A N   1 
ATOM   588  C  CA  . ALA   A 1 81  ? -3.898  -25.410 47.796  1.00 50.97  ? 109 ALA   A CA  1 
ATOM   589  C  C   . ALA   A 1 81  ? -2.826  -26.050 46.925  1.00 48.56  ? 109 ALA   A C   1 
ATOM   590  O  O   . ALA   A 1 81  ? -2.346  -27.143 47.239  1.00 50.80  ? 109 ALA   A O   1 
ATOM   591  C  CB  . ALA   A 1 81  ? -5.281  -25.968 47.428  1.00 45.58  ? 109 ALA   A CB  1 
ATOM   592  N  N   . GLY   A 1 82  ? -2.451  -25.399 45.826  1.00 49.09  ? 110 GLY   A N   1 
ATOM   593  C  CA  . GLY   A 1 82  ? -1.478  -25.976 44.923  1.00 50.39  ? 110 GLY   A CA  1 
ATOM   594  C  C   . GLY   A 1 82  ? -0.044  -25.782 45.337  1.00 55.24  ? 110 GLY   A C   1 
ATOM   595  O  O   . GLY   A 1 82  ? 0.847   -26.396 44.740  1.00 55.75  ? 110 GLY   A O   1 
ATOM   596  N  N   . GLU   A 1 83  ? 0.192   -24.959 46.356  1.00 49.25  ? 111 GLU   A N   1 
ATOM   597  C  CA  . GLU   A 1 83  ? 1.525   -24.587 46.796  1.00 47.98  ? 111 GLU   A CA  1 
ATOM   598  C  C   . GLU   A 1 83  ? 2.102   -25.623 47.757  1.00 50.16  ? 111 GLU   A C   1 
ATOM   599  O  O   . GLU   A 1 83  ? 1.390   -26.361 48.443  1.00 45.99  ? 111 GLU   A O   1 
ATOM   600  C  CB  . GLU   A 1 83  ? 1.520   -23.206 47.473  1.00 43.79  ? 111 GLU   A CB  1 
ATOM   601  C  CG  . GLU   A 1 83  ? 1.054   -22.039 46.568  1.00 46.49  ? 111 GLU   A CG  1 
ATOM   602  C  CD  . GLU   A 1 83  ? 0.978   -20.699 47.298  1.00 51.58  ? 111 GLU   A CD  1 
ATOM   603  O  OE1 . GLU   A 1 83  ? 1.442   -20.627 48.458  1.00 51.30  ? 111 GLU   A OE1 1 
ATOM   604  O  OE2 . GLU   A 1 83  ? 0.472   -19.709 46.711  1.00 48.67  ? 111 GLU   A OE2 1 
ATOM   605  N  N   . ILE   A 1 84  ? 3.424   -25.662 47.793  1.00 50.56  ? 112 ILE   A N   1 
ATOM   606  C  CA  . ILE   A 1 84  ? 4.164   -26.360 48.827  1.00 49.92  ? 112 ILE   A CA  1 
ATOM   607  C  C   . ILE   A 1 84  ? 5.077   -25.322 49.467  1.00 49.46  ? 112 ILE   A C   1 
ATOM   608  O  O   . ILE   A 1 84  ? 5.218   -24.206 48.962  1.00 49.89  ? 112 ILE   A O   1 
ATOM   609  C  CB  . ILE   A 1 84  ? 4.943   -27.568 48.270  1.00 50.34  ? 112 ILE   A CB  1 
ATOM   610  C  CG1 . ILE   A 1 84  ? 5.771   -27.156 47.049  1.00 50.54  ? 112 ILE   A CG1 1 
ATOM   611  C  CG2 . ILE   A 1 84  ? 3.974   -28.672 47.876  1.00 50.32  ? 112 ILE   A CG2 1 
ATOM   612  C  CD1 . ILE   A 1 84  ? 6.709   -28.246 46.558  1.00 53.18  ? 112 ILE   A CD1 1 
ATOM   613  N  N   . LYS   A 1 85  ? 5.639   -25.665 50.626  1.00 42.30  ? 113 LYS   A N   1 
ATOM   614  C  CA  . LYS   A 1 85  ? 6.518   -24.715 51.308  1.00 48.39  ? 113 LYS   A CA  1 
ATOM   615  C  C   . LYS   A 1 85  ? 7.554   -24.087 50.381  1.00 47.95  ? 113 LYS   A C   1 
ATOM   616  O  O   . LYS   A 1 85  ? 7.725   -22.859 50.436  1.00 45.00  ? 113 LYS   A O   1 
ATOM   617  C  CB  . LYS   A 1 85  ? 7.201   -25.381 52.513  1.00 50.74  ? 113 LYS   A CB  1 
ATOM   618  C  CG  . LYS   A 1 85  ? 6.248   -25.792 53.611  1.00 52.78  ? 113 LYS   A CG  1 
ATOM   619  C  CD  . LYS   A 1 85  ? 6.681   -25.257 54.966  1.00 58.11  ? 113 LYS   A CD  1 
ATOM   620  C  CE  . LYS   A 1 85  ? 6.048   -26.073 56.084  1.00 57.79  ? 113 LYS   A CE  1 
ATOM   621  N  NZ  . LYS   A 1 85  ? 6.237   -25.459 57.424  1.00 62.63  ? 113 LYS   A NZ  1 
ATOM   622  N  N   . PRO   A 1 86  ? 8.260   -24.833 49.517  1.00 52.40  ? 114 PRO   A N   1 
ATOM   623  C  CA  . PRO   A 1 86  ? 9.225   -24.172 48.620  1.00 53.79  ? 114 PRO   A CA  1 
ATOM   624  C  C   . PRO   A 1 86  ? 8.587   -23.224 47.619  1.00 53.58  ? 114 PRO   A C   1 
ATOM   625  O  O   . PRO   A 1 86  ? 9.229   -22.243 47.225  1.00 52.68  ? 114 PRO   A O   1 
ATOM   626  C  CB  . PRO   A 1 86  ? 9.904   -25.349 47.905  1.00 53.37  ? 114 PRO   A CB  1 
ATOM   627  C  CG  . PRO   A 1 86  ? 9.715   -26.503 48.812  1.00 50.55  ? 114 PRO   A CG  1 
ATOM   628  C  CD  . PRO   A 1 86  ? 8.386   -26.306 49.452  1.00 48.97  ? 114 PRO   A CD  1 
ATOM   629  N  N   . THR   A 1 87  ? 7.358   -23.490 47.175  1.00 51.77  ? 115 THR   A N   1 
ATOM   630  C  CA  . THR   A 1 87  ? 6.688   -22.625 46.210  1.00 50.18  ? 115 THR   A CA  1 
ATOM   631  C  C   . THR   A 1 87  ? 5.718   -21.643 46.864  1.00 53.67  ? 115 THR   A C   1 
ATOM   632  O  O   . THR   A 1 87  ? 4.842   -21.100 46.177  1.00 50.18  ? 115 THR   A O   1 
ATOM   633  C  CB  . THR   A 1 87  ? 5.951   -23.470 45.161  1.00 55.19  ? 115 THR   A CB  1 
ATOM   634  O  OG1 . THR   A 1 87  ? 4.821   -24.126 45.756  1.00 50.31  ? 115 THR   A OG1 1 
ATOM   635  C  CG2 . THR   A 1 87  ? 6.877   -24.528 44.566  1.00 55.99  ? 115 THR   A CG2 1 
ATOM   636  N  N   . THR   A 1 88  ? 5.851   -21.382 48.164  1.00 48.80  ? 116 THR   A N   1 
ATOM   637  C  CA  . THR   A 1 88  ? 4.794   -20.635 48.843  1.00 47.00  ? 116 THR   A CA  1 
ATOM   638  C  C   . THR   A 1 88  ? 4.794   -19.159 48.441  1.00 48.06  ? 116 THR   A C   1 
ATOM   639  O  O   . THR   A 1 88  ? 5.825   -18.593 48.069  1.00 44.35  ? 116 THR   A O   1 
ATOM   640  C  CB  . THR   A 1 88  ? 4.937   -20.756 50.360  1.00 46.51  ? 116 THR   A CB  1 
ATOM   641  O  OG1 . THR   A 1 88  ? 3.821   -20.113 50.986  1.00 48.08  ? 116 THR   A OG1 1 
ATOM   642  C  CG2 . THR   A 1 88  ? 6.201   -20.086 50.833  1.00 43.80  ? 116 THR   A CG2 1 
ATOM   643  N  N   . THR   A 1 89  ? 3.611   -18.535 48.510  1.00 44.40  ? 117 THR   A N   1 
ATOM   644  C  CA  . THR   A 1 89  ? 3.496   -17.093 48.332  1.00 47.42  ? 117 THR   A CA  1 
ATOM   645  C  C   . THR   A 1 89  ? 3.325   -16.344 49.649  1.00 43.84  ? 117 THR   A C   1 
ATOM   646  O  O   . THR   A 1 89  ? 3.184   -15.122 49.632  1.00 45.72  ? 117 THR   A O   1 
ATOM   647  C  CB  . THR   A 1 89  ? 2.347   -16.737 47.382  1.00 47.03  ? 117 THR   A CB  1 
ATOM   648  O  OG1 . THR   A 1 89  ? 1.109   -17.297 47.851  1.00 44.63  ? 117 THR   A OG1 1 
ATOM   649  C  CG2 . THR   A 1 89  ? 2.646   -17.238 45.978  1.00 49.20  ? 117 THR   A CG2 1 
ATOM   650  N  N   . ALA   A 1 90  ? 3.379   -17.038 50.784  1.00 43.50  ? 118 ALA   A N   1 
ATOM   651  C  CA  . ALA   A 1 90  ? 3.378   -16.362 52.073  1.00 39.98  ? 118 ALA   A CA  1 
ATOM   652  C  C   . ALA   A 1 90  ? 4.647   -15.536 52.239  1.00 42.21  ? 118 ALA   A C   1 
ATOM   653  O  O   . ALA   A 1 90  ? 5.753   -15.987 51.928  1.00 43.75  ? 118 ALA   A O   1 
ATOM   654  C  CB  . ALA   A 1 90  ? 3.282   -17.370 53.215  1.00 41.23  ? 118 ALA   A CB  1 
ATOM   655  N  N   . SER   A 1 91  ? 4.488   -14.335 52.765  1.00 40.18  ? 119 SER   A N   1 
ATOM   656  C  CA  . SER   A 1 91  ? 5.650   -13.518 53.061  1.00 43.56  ? 119 SER   A CA  1 
ATOM   657  C  C   . SER   A 1 91  ? 6.226   -13.836 54.428  1.00 45.04  ? 119 SER   A C   1 
ATOM   658  O  O   . SER   A 1 91  ? 7.400   -13.511 54.697  1.00 39.08  ? 119 SER   A O   1 
ATOM   659  C  CB  . SER   A 1 91  ? 5.279   -12.042 52.969  1.00 42.75  ? 119 SER   A CB  1 
ATOM   660  O  OG  . SER   A 1 91  ? 4.227   -11.734 53.863  1.00 41.39  ? 119 SER   A OG  1 
ATOM   661  N  N   . ILE   A 1 92  ? 5.433   -14.459 55.295  1.00 38.56  ? 120 ILE   A N   1 
ATOM   662  C  CA  . ILE   A 1 92  ? 5.964   -14.934 56.569  1.00 42.30  ? 120 ILE   A CA  1 
ATOM   663  C  C   . ILE   A 1 92  ? 5.953   -16.454 56.518  1.00 41.34  ? 120 ILE   A C   1 
ATOM   664  O  O   . ILE   A 1 92  ? 4.901   -17.073 56.728  1.00 41.09  ? 120 ILE   A O   1 
ATOM   665  C  CB  . ILE   A 1 92  ? 5.170   -14.371 57.757  1.00 44.30  ? 120 ILE   A CB  1 
ATOM   666  C  CG1 . ILE   A 1 92  ? 5.322   -12.843 57.786  1.00 43.46  ? 120 ILE   A CG1 1 
ATOM   667  C  CG2 . ILE   A 1 92  ? 5.703   -14.941 59.066  1.00 45.14  ? 120 ILE   A CG2 1 
ATOM   668  C  CD1 . ILE   A 1 92  ? 4.269   -12.125 58.608  1.00 43.26  ? 120 ILE   A CD1 1 
ATOM   669  N  N   . PRO   A 1 93  ? 7.087   -17.089 56.201  1.00 43.41  ? 121 PRO   A N   1 
ATOM   670  C  CA  . PRO   A 1 93  ? 7.070   -18.540 55.957  1.00 45.14  ? 121 PRO   A CA  1 
ATOM   671  C  C   . PRO   A 1 93  ? 6.693   -19.359 57.179  1.00 44.17  ? 121 PRO   A C   1 
ATOM   672  O  O   . PRO   A 1 93  ? 6.257   -20.509 57.022  1.00 45.53  ? 121 PRO   A O   1 
ATOM   673  C  CB  . PRO   A 1 93  ? 8.503   -18.841 55.487  1.00 50.74  ? 121 PRO   A CB  1 
ATOM   674  C  CG  . PRO   A 1 93  ? 9.302   -17.605 55.786  1.00 50.37  ? 121 PRO   A CG  1 
ATOM   675  C  CD  . PRO   A 1 93  ? 8.345   -16.458 55.768  1.00 46.72  ? 121 PRO   A CD  1 
ATOM   676  N  N   . SER   A 1 94  ? 6.823   -18.809 58.390  1.00 38.33  ? 122 SER   A N   1 
ATOM   677  C  CA  . SER   A 1 94  ? 6.335   -19.535 59.555  1.00 41.96  ? 122 SER   A CA  1 
ATOM   678  C  C   . SER   A 1 94  ? 4.813   -19.645 59.598  1.00 42.88  ? 122 SER   A C   1 
ATOM   679  O  O   . SER   A 1 94  ? 4.288   -20.450 60.379  1.00 38.63  ? 122 SER   A O   1 
ATOM   680  C  CB  . SER   A 1 94  ? 6.848   -18.883 60.839  1.00 43.11  ? 122 SER   A CB  1 
ATOM   681  O  OG  . SER   A 1 94  ? 6.394   -17.545 60.969  1.00 40.68  ? 122 SER   A OG  1 
ATOM   682  N  N   . PHE   A 1 95  ? 4.090   -18.884 58.775  1.00 39.27  ? 123 PHE   A N   1 
ATOM   683  C  CA  . PHE   A 1 95  ? 2.637   -18.890 58.877  1.00 37.23  ? 123 PHE   A CA  1 
ATOM   684  C  C   . PHE   A 1 95  ? 2.048   -20.258 58.525  1.00 39.57  ? 123 PHE   A C   1 
ATOM   685  O  O   . PHE   A 1 95  ? 2.525   -20.955 57.623  1.00 43.95  ? 123 PHE   A O   1 
ATOM   686  C  CB  . PHE   A 1 95  ? 2.029   -17.825 57.968  1.00 34.63  ? 123 PHE   A CB  1 
ATOM   687  C  CG  . PHE   A 1 95  ? 0.539   -17.744 58.075  1.00 40.50  ? 123 PHE   A CG  1 
ATOM   688  C  CD1 . PHE   A 1 95  ? -0.052  -16.979 59.069  1.00 36.61  ? 123 PHE   A CD1 1 
ATOM   689  C  CD2 . PHE   A 1 95  ? -0.273  -18.454 57.199  1.00 38.98  ? 123 PHE   A CD2 1 
ATOM   690  C  CE1 . PHE   A 1 95  ? -1.421  -16.915 59.176  1.00 36.88  ? 123 PHE   A CE1 1 
ATOM   691  C  CE2 . PHE   A 1 95  ? -1.660  -18.400 57.300  1.00 41.59  ? 123 PHE   A CE2 1 
ATOM   692  C  CZ  . PHE   A 1 95  ? -2.236  -17.635 58.290  1.00 38.49  ? 123 PHE   A CZ  1 
ATOM   693  N  N   . ASP   A 1 96  ? 0.993   -20.629 59.242  1.00 36.78  ? 124 ASP   A N   1 
ATOM   694  C  CA  . ASP   A 1 96  ? 0.274   -21.879 59.027  1.00 40.23  ? 124 ASP   A CA  1 
ATOM   695  C  C   . ASP   A 1 96  ? -1.215  -21.614 59.198  1.00 39.31  ? 124 ASP   A C   1 
ATOM   696  O  O   . ASP   A 1 96  ? -1.618  -21.034 60.211  1.00 40.81  ? 124 ASP   A O   1 
ATOM   697  C  CB  . ASP   A 1 96  ? 0.747   -22.953 60.017  1.00 41.77  ? 124 ASP   A CB  1 
ATOM   698  C  CG  . ASP   A 1 96  ? 0.046   -24.267 59.825  1.00 44.99  ? 124 ASP   A CG  1 
ATOM   699  O  OD1 . ASP   A 1 96  ? 0.505   -25.068 58.982  1.00 54.49  ? 124 ASP   A OD1 1 
ATOM   700  O  OD2 . ASP   A 1 96  ? -0.964  -24.509 60.515  1.00 45.89  ? 124 ASP   A OD2 1 
ATOM   701  N  N   . HIS   A 1 97  ? -2.023  -22.037 58.211  1.00 42.34  ? 125 HIS   A N   1 
ATOM   702  C  CA  . HIS   A 1 97  ? -3.466  -21.793 58.262  1.00 43.81  ? 125 HIS   A CA  1 
ATOM   703  C  C   . HIS   A 1 97  ? -4.070  -22.381 59.528  1.00 45.02  ? 125 HIS   A C   1 
ATOM   704  O  O   . HIS   A 1 97  ? -4.826  -21.713 60.242  1.00 40.17  ? 125 HIS   A O   1 
ATOM   705  C  CB  . HIS   A 1 97  ? -4.168  -22.394 57.036  1.00 45.49  ? 125 HIS   A CB  1 
ATOM   706  C  CG  . HIS   A 1 97  ? -3.991  -21.613 55.772  1.00 44.70  ? 125 HIS   A CG  1 
ATOM   707  N  ND1 . HIS   A 1 97  ? -4.828  -20.574 55.412  1.00 48.93  ? 125 HIS   A ND1 1 
ATOM   708  C  CD2 . HIS   A 1 97  ? -3.095  -21.739 54.764  1.00 44.86  ? 125 HIS   A CD2 1 
ATOM   709  C  CE1 . HIS   A 1 97  ? -4.440  -20.081 54.248  1.00 42.54  ? 125 HIS   A CE1 1 
ATOM   710  N  NE2 . HIS   A 1 97  ? -3.389  -20.768 53.835  1.00 48.99  ? 125 HIS   A NE2 1 
ATOM   711  N  N   . GLY   A 1 98  ? -3.760  -23.646 59.813  1.00 41.33  ? 126 GLY   A N   1 
ATOM   712  C  CA  . GLY   A 1 98  ? -4.385  -24.310 60.945  1.00 42.37  ? 126 GLY   A CA  1 
ATOM   713  C  C   . GLY   A 1 98  ? -3.933  -23.730 62.270  1.00 40.86  ? 126 GLY   A C   1 
ATOM   714  O  O   . GLY   A 1 98  ? -4.746  -23.540 63.179  1.00 39.91  ? 126 GLY   A O   1 
ATOM   715  N  N   . SER   A 1 99  ? -2.634  -23.442 62.392  1.00 41.76  ? 127 SER   A N   1 
ATOM   716  C  CA  . SER   A 1 99  ? -2.096  -22.811 63.595  1.00 37.52  ? 127 SER   A CA  1 
ATOM   717  C  C   . SER   A 1 99  ? -2.781  -21.470 63.864  1.00 40.65  ? 127 SER   A C   1 
ATOM   718  O  O   . SER   A 1 99  ? -3.241  -21.202 64.982  1.00 38.53  ? 127 SER   A O   1 
ATOM   719  C  CB  . SER   A 1 99  ? -0.585  -22.626 63.448  1.00 41.69  ? 127 SER   A CB  1 
ATOM   720  O  OG  . SER   A 1 99  ? 0.107   -23.855 63.202  1.00 42.11  ? 127 SER   A OG  1 
ATOM   721  N  N   . CYS   A 1 100 ? -2.887  -20.629 62.835  1.00 37.43  ? 128 CYS   A N   1 
ATOM   722  C  CA  . CYS   A 1 100 ? -3.535  -19.329 63.002  1.00 38.42  ? 128 CYS   A CA  1 
ATOM   723  C  C   . CYS   A 1 100 ? -5.009  -19.488 63.368  1.00 39.75  ? 128 CYS   A C   1 
ATOM   724  O  O   . CYS   A 1 100 ? -5.488  -18.885 64.335  1.00 40.54  ? 128 CYS   A O   1 
ATOM   725  C  CB  . CYS   A 1 100 ? -3.372  -18.505 61.726  1.00 36.38  ? 128 CYS   A CB  1 
ATOM   726  S  SG  . CYS   A 1 100 ? -3.951  -16.793 61.912  1.00 39.93  ? 128 CYS   A SG  1 
ATOM   727  N  N   . ARG   A 1 101 ? -5.748  -20.302 62.605  1.00 37.26  ? 129 ARG   A N   1 
ATOM   728  C  CA  . ARG   A 1 101 ? -7.157  -20.517 62.913  1.00 40.19  ? 129 ARG   A CA  1 
ATOM   729  C  C   . ARG   A 1 101 ? -7.332  -21.083 64.318  1.00 41.43  ? 129 ARG   A C   1 
ATOM   730  O  O   . ARG   A 1 101 ? -8.228  -20.657 65.057  1.00 39.01  ? 129 ARG   A O   1 
ATOM   731  C  CB  . ARG   A 1 101 ? -7.789  -21.440 61.865  1.00 41.51  ? 129 ARG   A CB  1 
ATOM   732  C  CG  . ARG   A 1 101 ? -7.912  -20.742 60.498  1.00 45.75  ? 129 ARG   A CG  1 
ATOM   733  C  CD  . ARG   A 1 101 ? -9.020  -21.298 59.572  1.00 43.27  ? 129 ARG   A CD  1 
ATOM   734  N  NE  . ARG   A 1 101 ? -9.602  -20.210 58.776  1.00 47.24  ? 129 ARG   A NE  1 
ATOM   735  C  CZ  . ARG   A 1 101 ? -9.058  -19.706 57.665  1.00 45.11  ? 129 ARG   A CZ  1 
ATOM   736  N  NH1 . ARG   A 1 101 ? -7.923  -20.200 57.184  1.00 49.23  ? 129 ARG   A NH1 1 
ATOM   737  N  NH2 . ARG   A 1 101 ? -9.654  -18.717 57.026  1.00 43.28  ? 129 ARG   A NH2 1 
ATOM   738  N  N   . SER   A 1 102 ? -6.470  -22.031 64.713  1.00 39.07  ? 130 SER   A N   1 
ATOM   739  C  CA  . SER   A 1 102 ? -6.571  -22.608 66.050  1.00 38.05  ? 130 SER   A CA  1 
ATOM   740  C  C   . SER   A 1 102 ? -6.206  -21.584 67.125  1.00 44.22  ? 130 SER   A C   1 
ATOM   741  O  O   . SER   A 1 102 ? -6.849  -21.527 68.182  1.00 41.54  ? 130 SER   A O   1 
ATOM   742  C  CB  . SER   A 1 102 ? -5.686  -23.852 66.144  1.00 44.91  ? 130 SER   A CB  1 
ATOM   743  O  OG  . SER   A 1 102 ? -5.542  -24.300 67.481  1.00 54.19  ? 130 SER   A OG  1 
ATOM   744  N  N   . PHE   A 1 103 ? -5.181  -20.761 66.874  1.00 39.54  ? 131 PHE   A N   1 
ATOM   745  C  CA  . PHE   A 1 103 ? -4.828  -19.717 67.827  1.00 35.80  ? 131 PHE   A CA  1 
ATOM   746  C  C   . PHE   A 1 103 ? -6.009  -18.789 68.103  1.00 38.99  ? 131 PHE   A C   1 
ATOM   747  O  O   . PHE   A 1 103 ? -6.351  -18.543 69.264  1.00 38.88  ? 131 PHE   A O   1 
ATOM   748  C  CB  . PHE   A 1 103 ? -3.625  -18.935 67.295  1.00 40.26  ? 131 PHE   A CB  1 
ATOM   749  C  CG  . PHE   A 1 103 ? -3.175  -17.806 68.178  1.00 37.06  ? 131 PHE   A CG  1 
ATOM   750  C  CD1 . PHE   A 1 103 ? -3.854  -16.592 68.194  1.00 37.46  ? 131 PHE   A CD1 1 
ATOM   751  C  CD2 . PHE   A 1 103 ? -2.039  -17.942 68.957  1.00 35.67  ? 131 PHE   A CD2 1 
ATOM   752  C  CE1 . PHE   A 1 103 ? -3.400  -15.545 68.999  1.00 33.75  ? 131 PHE   A CE1 1 
ATOM   753  C  CE2 . PHE   A 1 103 ? -1.594  -16.905 69.759  1.00 37.29  ? 131 PHE   A CE2 1 
ATOM   754  C  CZ  . PHE   A 1 103 ? -2.272  -15.705 69.774  1.00 35.31  ? 131 PHE   A CZ  1 
ATOM   755  N  N   . PHE   A 1 104 ? -6.641  -18.253 67.040  1.00 37.72  ? 132 PHE   A N   1 
ATOM   756  C  CA  . PHE   A 1 104 ? -7.705  -17.268 67.215  1.00 43.02  ? 132 PHE   A CA  1 
ATOM   757  C  C   . PHE   A 1 104 ? -8.938  -17.895 67.858  1.00 41.20  ? 132 PHE   A C   1 
ATOM   758  O  O   . PHE   A 1 104 ? -9.553  -17.288 68.742  1.00 42.47  ? 132 PHE   A O   1 
ATOM   759  C  CB  . PHE   A 1 104 ? -8.067  -16.603 65.867  1.00 44.34  ? 132 PHE   A CB  1 
ATOM   760  C  CG  . PHE   A 1 104 ? -8.985  -15.374 65.986  1.00 45.92  ? 132 PHE   A CG  1 
ATOM   761  C  CD1 . PHE   A 1 104 ? -10.248 -15.457 66.552  1.00 45.43  ? 132 PHE   A CD1 1 
ATOM   762  C  CD2 . PHE   A 1 104 ? -8.580  -14.124 65.521  1.00 41.18  ? 132 PHE   A CD2 1 
ATOM   763  C  CE1 . PHE   A 1 104 ? -11.060 -14.306 66.664  1.00 44.11  ? 132 PHE   A CE1 1 
ATOM   764  C  CE2 . PHE   A 1 104 ? -9.444  -12.943 65.611  1.00 39.32  ? 132 PHE   A CE2 1 
ATOM   765  C  CZ  . PHE   A 1 104 ? -10.613 -13.028 66.193  1.00 35.66  ? 132 PHE   A CZ  1 
ATOM   766  N  N   . SER   A 1 105 ? -9.334  -19.093 67.423  1.00 36.99  ? 133 SER   A N   1 
ATOM   767  C  CA  . SER   A 1 105 ? -10.493 -19.717 68.057  1.00 41.88  ? 133 SER   A CA  1 
ATOM   768  C  C   . SER   A 1 105 ? -10.219 -20.038 69.522  1.00 41.45  ? 133 SER   A C   1 
ATOM   769  O  O   . SER   A 1 105 ? -11.144 -20.042 70.343  1.00 43.38  ? 133 SER   A O   1 
ATOM   770  C  CB  . SER   A 1 105 ? -10.909 -20.980 67.295  1.00 41.15  ? 133 SER   A CB  1 
ATOM   771  O  OG  . SER   A 1 105 ? -9.912  -21.954 67.385  1.00 47.82  ? 133 SER   A OG  1 
ATOM   772  N  N   . SER   A 1 106 ? -8.956  -20.275 69.880  1.00 39.68  ? 134 SER   A N   1 
ATOM   773  C  CA  . SER   A 1 106 ? -8.646  -20.556 71.274  1.00 40.63  ? 134 SER   A CA  1 
ATOM   774  C  C   . SER   A 1 106 ? -8.539  -19.283 72.112  1.00 42.79  ? 134 SER   A C   1 
ATOM   775  O  O   . SER   A 1 106 ? -9.080  -19.231 73.223  1.00 43.00  ? 134 SER   A O   1 
ATOM   776  C  CB  . SER   A 1 106 ? -7.349  -21.357 71.372  1.00 45.57  ? 134 SER   A CB  1 
ATOM   777  O  OG  . SER   A 1 106 ? -6.941  -21.445 72.722  1.00 47.72  ? 134 SER   A OG  1 
ATOM   778  N  N   . HIS   A 1 107 ? -7.855  -18.249 71.604  1.00 39.60  ? 135 HIS   A N   1 
ATOM   779  C  CA  . HIS   A 1 107 ? -7.564  -17.052 72.388  1.00 41.52  ? 135 HIS   A CA  1 
ATOM   780  C  C   . HIS   A 1 107 ? -8.342  -15.816 71.960  1.00 42.51  ? 135 HIS   A C   1 
ATOM   781  O  O   . HIS   A 1 107 ? -8.327  -14.817 72.692  1.00 40.96  ? 135 HIS   A O   1 
ATOM   782  C  CB  . HIS   A 1 107 ? -6.065  -16.721 72.321  1.00 39.68  ? 135 HIS   A CB  1 
ATOM   783  C  CG  . HIS   A 1 107 ? -5.186  -17.891 72.590  1.00 40.96  ? 135 HIS   A CG  1 
ATOM   784  N  ND1 . HIS   A 1 107 ? -5.217  -18.584 73.782  1.00 39.32  ? 135 HIS   A ND1 1 
ATOM   785  C  CD2 . HIS   A 1 107 ? -4.264  -18.510 71.815  1.00 38.43  ? 135 HIS   A CD2 1 
ATOM   786  C  CE1 . HIS   A 1 107 ? -4.342  -19.571 73.731  1.00 42.31  ? 135 HIS   A CE1 1 
ATOM   787  N  NE2 . HIS   A 1 107 ? -3.756  -19.550 72.547  1.00 41.18  ? 135 HIS   A NE2 1 
ATOM   788  N  N   . GLY   A 1 108 ? -9.007  -15.842 70.807  1.00 36.91  ? 136 GLY   A N   1 
ATOM   789  C  CA  . GLY   A 1 108 ? -9.451  -14.561 70.288  1.00 41.49  ? 136 GLY   A CA  1 
ATOM   790  C  C   . GLY   A 1 108 ? -8.266  -13.720 69.821  1.00 39.86  ? 136 GLY   A C   1 
ATOM   791  O  O   . GLY   A 1 108 ? -7.139  -14.195 69.685  1.00 37.49  ? 136 GLY   A O   1 
ATOM   792  N  N   . LEU   A 1 109 ? -8.540  -12.436 69.578  1.00 34.30  ? 137 LEU   A N   1 
ATOM   793  C  CA  . LEU   A 1 109 ? -7.494  -11.525 69.135  1.00 38.41  ? 137 LEU   A CA  1 
ATOM   794  C  C   . LEU   A 1 109 ? -6.364  -11.479 70.157  1.00 34.85  ? 137 LEU   A C   1 
ATOM   795  O  O   . LEU   A 1 109 ? -6.596  -11.236 71.343  1.00 38.89  ? 137 LEU   A O   1 
ATOM   796  C  CB  . LEU   A 1 109 ? -8.078  -10.126 68.924  1.00 34.22  ? 137 LEU   A CB  1 
ATOM   797  C  CG  . LEU   A 1 109 ? -7.072  -9.032  68.564  1.00 35.15  ? 137 LEU   A CG  1 
ATOM   798  C  CD1 . LEU   A 1 109 ? -6.466  -9.269  67.192  1.00 32.77  ? 137 LEU   A CD1 1 
ATOM   799  C  CD2 . LEU   A 1 109 ? -7.776  -7.682  68.626  1.00 35.37  ? 137 LEU   A CD2 1 
ATOM   800  N  N   . GLY   A 1 110 ? -5.139  -11.732 69.706  1.00 32.17  ? 138 GLY   A N   1 
ATOM   801  C  CA  . GLY   A 1 110 ? -4.023  -11.641 70.625  1.00 32.06  ? 138 GLY   A CA  1 
ATOM   802  C  C   . GLY   A 1 110 ? -2.701  -11.638 69.885  1.00 33.03  ? 138 GLY   A C   1 
ATOM   803  O  O   . GLY   A 1 110 ? -2.646  -11.771 68.658  1.00 32.84  ? 138 GLY   A O   1 
ATOM   804  N  N   . VAL   A 1 111 ? -1.629  -11.492 70.660  1.00 29.78  ? 139 VAL   A N   1 
ATOM   805  C  CA  . VAL   A 1 111 ? -0.283  -11.418 70.100  1.00 30.52  ? 139 VAL   A CA  1 
ATOM   806  C  C   . VAL   A 1 111 ? 0.218   -12.834 69.874  1.00 33.43  ? 139 VAL   A C   1 
ATOM   807  O  O   . VAL   A 1 111 ? 0.197   -13.663 70.793  1.00 32.92  ? 139 VAL   A O   1 
ATOM   808  C  CB  . VAL   A 1 111 ? 0.667   -10.648 71.033  1.00 29.42  ? 139 VAL   A CB  1 
ATOM   809  C  CG1 . VAL   A 1 111 ? 2.132   -10.855 70.620  1.00 29.91  ? 139 VAL   A CG1 1 
ATOM   810  C  CG2 . VAL   A 1 111 ? 0.328   -9.134  71.028  1.00 29.38  ? 139 VAL   A CG2 1 
ATOM   811  N  N   . ARG   A 1 112 ? 0.675   -13.110 68.654  1.00 35.77  ? 140 ARG   A N   1 
ATOM   812  C  CA  . ARG   A 1 112 ? 1.320   -14.381 68.329  1.00 33.24  ? 140 ARG   A CA  1 
ATOM   813  C  C   . ARG   A 1 112 ? 2.837   -14.319 68.487  1.00 35.34  ? 140 ARG   A C   1 
ATOM   814  O  O   . ARG   A 1 112 ? 3.440   -15.222 69.076  1.00 36.49  ? 140 ARG   A O   1 
ATOM   815  C  CB  . ARG   A 1 112 ? 0.964   -14.797 66.899  1.00 32.10  ? 140 ARG   A CB  1 
ATOM   816  C  CG  . ARG   A 1 112 ? 1.858   -15.913 66.311  1.00 31.52  ? 140 ARG   A CG  1 
ATOM   817  C  CD  . ARG   A 1 112 ? 1.685   -17.255 67.044  1.00 36.21  ? 140 ARG   A CD  1 
ATOM   818  N  NE  . ARG   A 1 112 ? 2.382   -18.343 66.332  1.00 38.82  ? 140 ARG   A NE  1 
ATOM   819  C  CZ  . ARG   A 1 112 ? 2.487   -19.604 66.751  1.00 40.25  ? 140 ARG   A CZ  1 
ATOM   820  N  NH1 . ARG   A 1 112 ? 1.962   -19.992 67.910  1.00 35.70  ? 140 ARG   A NH1 1 
ATOM   821  N  NH2 . ARG   A 1 112 ? 3.125   -20.487 65.995  1.00 37.38  ? 140 ARG   A NH2 1 
ATOM   822  N  N   . ALA   A 1 113 ? 3.483   -13.277 67.962  1.00 32.67  ? 141 ALA   A N   1 
ATOM   823  C  CA  . ALA   A 1 113 ? 4.940   -13.229 67.944  1.00 35.04  ? 141 ALA   A CA  1 
ATOM   824  C  C   . ALA   A 1 113 ? 5.416   -11.936 68.577  1.00 37.80  ? 141 ALA   A C   1 
ATOM   825  O  O   . ALA   A 1 113 ? 4.894   -10.859 68.270  1.00 34.57  ? 141 ALA   A O   1 
ATOM   826  C  CB  . ALA   A 1 113 ? 5.496   -13.339 66.522  1.00 35.32  ? 141 ALA   A CB  1 
ATOM   827  N  N   . VAL   A 1 114 ? 6.360   -12.061 69.493  1.00 32.42  ? 142 VAL   A N   1 
ATOM   828  C  CA  . VAL   A 1 114 ? 7.184   -10.950 69.959  1.00 34.41  ? 142 VAL   A CA  1 
ATOM   829  C  C   . VAL   A 1 114 ? 8.506   -11.049 69.216  1.00 36.16  ? 142 VAL   A C   1 
ATOM   830  O  O   . VAL   A 1 114 ? 9.304   -11.952 69.482  1.00 36.07  ? 142 VAL   A O   1 
ATOM   831  C  CB  . VAL   A 1 114 ? 7.383   -10.996 71.479  1.00 35.62  ? 142 VAL   A CB  1 
ATOM   832  C  CG1 . VAL   A 1 114 ? 8.272   -9.846  71.952  1.00 37.57  ? 142 VAL   A CG1 1 
ATOM   833  C  CG2 . VAL   A 1 114 ? 6.022   -11.000 72.207  1.00 34.40  ? 142 VAL   A CG2 1 
ATOM   834  N  N   . ALA   A 1 115 ? 8.751   -10.146 68.268  1.00 35.77  ? 143 ALA   A N   1 
ATOM   835  C  CA  . ALA   A 1 115 ? 9.940   -10.237 67.424  1.00 34.10  ? 143 ALA   A CA  1 
ATOM   836  C  C   . ALA   A 1 115 ? 11.027  -9.283  67.905  1.00 35.19  ? 143 ALA   A C   1 
ATOM   837  O  O   . ALA   A 1 115 ? 10.796  -8.073  68.015  1.00 33.86  ? 143 ALA   A O   1 
ATOM   838  C  CB  . ALA   A 1 115 ? 9.599   -9.935  65.966  1.00 32.34  ? 143 ALA   A CB  1 
ATOM   839  N  N   . ILE   A 1 116 ? 12.217  -9.824  68.164  1.00 35.58  ? 144 ILE   A N   1 
ATOM   840  C  CA  . ILE   A 1 116 ? 13.372  -9.013  68.531  1.00 34.80  ? 144 ILE   A CA  1 
ATOM   841  C  C   . ILE   A 1 116 ? 14.422  -9.136  67.438  1.00 36.71  ? 144 ILE   A C   1 
ATOM   842  O  O   . ILE   A 1 116 ? 14.581  -10.197 66.824  1.00 37.19  ? 144 ILE   A O   1 
ATOM   843  C  CB  . ILE   A 1 116 ? 13.953  -9.410  69.903  1.00 33.40  ? 144 ILE   A CB  1 
ATOM   844  C  CG1 . ILE   A 1 116 ? 14.350  -10.888 69.923  1.00 38.87  ? 144 ILE   A CG1 1 
ATOM   845  C  CG2 . ILE   A 1 116 ? 12.972  -9.076  71.008  1.00 35.50  ? 144 ILE   A CG2 1 
ATOM   846  C  CD1 . ILE   A 1 116 ? 15.103  -11.325 71.175  1.00 41.57  ? 144 ILE   A CD1 1 
ATOM   847  N  N   . GLU   A 1 117 ? 15.118  -8.039  67.175  1.00 38.94  ? 145 GLU   A N   1 
ATOM   848  C  CA  . GLU   A 1 117 ? 16.168  -8.052  66.178  1.00 42.98  ? 145 GLU   A CA  1 
ATOM   849  C  C   . GLU   A 1 117 ? 17.446  -8.557  66.827  1.00 40.82  ? 145 GLU   A C   1 
ATOM   850  O  O   . GLU   A 1 117 ? 17.768  -8.175  67.955  1.00 39.10  ? 145 GLU   A O   1 
ATOM   851  C  CB  . GLU   A 1 117 ? 16.389  -6.656  65.590  1.00 43.66  ? 145 GLU   A CB  1 
ATOM   852  C  CG  . GLU   A 1 117 ? 17.483  -6.620  64.537  1.00 47.76  ? 145 GLU   A CG  1 
ATOM   853  C  CD  . GLU   A 1 117 ? 17.695  -5.227  63.977  1.00 52.82  ? 145 GLU   A CD  1 
ATOM   854  O  OE1 . GLU   A 1 117 ? 18.444  -5.081  62.987  1.00 52.76  ? 145 GLU   A OE1 1 
ATOM   855  O  OE2 . GLU   A 1 117 ? 17.103  -4.278  64.529  1.00 52.98  ? 145 GLU   A OE2 1 
ATOM   856  N  N   . VAL   A 1 118 ? 18.149  -9.446  66.122  1.00 40.41  ? 146 VAL   A N   1 
ATOM   857  C  CA  . VAL   A 1 118 ? 19.425  -10.002 66.565  1.00 42.83  ? 146 VAL   A CA  1 
ATOM   858  C  C   . VAL   A 1 118 ? 20.453  -9.862  65.433  1.00 42.87  ? 146 VAL   A C   1 
ATOM   859  O  O   . VAL   A 1 118 ? 20.109  -9.614  64.282  1.00 42.74  ? 146 VAL   A O   1 
ATOM   860  C  CB  . VAL   A 1 118 ? 19.277  -11.473 66.999  1.00 41.76  ? 146 VAL   A CB  1 
ATOM   861  C  CG1 . VAL   A 1 118 ? 18.295  -11.602 68.160  1.00 41.56  ? 146 VAL   A CG1 1 
ATOM   862  C  CG2 . VAL   A 1 118 ? 18.851  -12.319 65.827  1.00 39.54  ? 146 VAL   A CG2 1 
ATOM   863  N  N   . GLU   A 1 119 ? 21.746  -10.008 65.760  1.00 49.11  ? 147 GLU   A N   1 
ATOM   864  C  CA  . GLU   A 1 119 ? 22.758  -9.949  64.688  1.00 45.59  ? 147 GLU   A CA  1 
ATOM   865  C  C   . GLU   A 1 119 ? 22.669  -11.147 63.770  1.00 43.93  ? 147 GLU   A C   1 
ATOM   866  O  O   . GLU   A 1 119 ? 22.957  -11.025 62.576  1.00 41.79  ? 147 GLU   A O   1 
ATOM   867  C  CB  . GLU   A 1 119 ? 24.213  -9.842  65.204  1.00 51.78  ? 147 GLU   A CB  1 
ATOM   868  C  CG  . GLU   A 1 119 ? 24.651  -10.867 66.200  1.00 55.88  ? 147 GLU   A CG  1 
ATOM   869  C  CD  . GLU   A 1 119 ? 23.978  -10.559 67.479  1.00 61.59  ? 147 GLU   A CD  1 
ATOM   870  O  OE1 . GLU   A 1 119 ? 24.133  -9.372  67.894  1.00 65.36  ? 147 GLU   A OE1 1 
ATOM   871  O  OE2 . GLU   A 1 119 ? 23.262  -11.418 68.020  1.00 65.21  ? 147 GLU   A OE2 1 
ATOM   872  N  N   . ASP   A 1 120 ? 22.295  -12.307 64.298  1.00 41.70  ? 148 ASP   A N   1 
ATOM   873  C  CA  . ASP   A 1 120 ? 22.318  -13.536 63.505  1.00 47.07  ? 148 ASP   A CA  1 
ATOM   874  C  C   . ASP   A 1 120 ? 21.187  -14.436 64.003  1.00 45.98  ? 148 ASP   A C   1 
ATOM   875  O  O   . ASP   A 1 120 ? 21.350  -15.144 65.004  1.00 44.02  ? 148 ASP   A O   1 
ATOM   876  C  CB  . ASP   A 1 120 ? 23.681  -14.216 63.619  1.00 48.15  ? 148 ASP   A CB  1 
ATOM   877  C  CG  . ASP   A 1 120 ? 23.870  -15.319 62.594  1.00 52.95  ? 148 ASP   A CG  1 
ATOM   878  O  OD1 . ASP   A 1 120 ? 22.856  -15.870 62.126  1.00 53.32  ? 148 ASP   A OD1 1 
ATOM   879  O  OD2 . ASP   A 1 120 ? 25.030  -15.656 62.264  1.00 56.26  ? 148 ASP   A OD2 1 
ATOM   880  N  N   . ALA   A 1 121 ? 20.050  -14.410 63.286  1.00 48.81  ? 149 ALA   A N   1 
ATOM   881  C  CA  . ALA   A 1 121 ? 18.867  -15.163 63.702  1.00 45.33  ? 149 ALA   A CA  1 
ATOM   882  C  C   . ALA   A 1 121 ? 19.107  -16.669 63.700  1.00 47.81  ? 149 ALA   A C   1 
ATOM   883  O  O   . ALA   A 1 121 ? 18.498  -17.397 64.496  1.00 46.37  ? 149 ALA   A O   1 
ATOM   884  C  CB  . ALA   A 1 121 ? 17.687  -14.818 62.793  1.00 44.62  ? 149 ALA   A CB  1 
ATOM   885  N  N   . GLU   A 1 122 ? 19.963  -17.163 62.802  1.00 47.01  ? 150 GLU   A N   1 
ATOM   886  C  CA  . GLU   A 1 122 ? 20.253  -18.597 62.770  1.00 50.68  ? 150 GLU   A CA  1 
ATOM   887  C  C   . GLU   A 1 122 ? 21.019  -19.038 64.015  1.00 48.39  ? 150 GLU   A C   1 
ATOM   888  O  O   . GLU   A 1 122 ? 20.683  -20.054 64.639  1.00 47.91  ? 150 GLU   A O   1 
ATOM   889  C  CB  . GLU   A 1 122 ? 21.031  -18.945 61.502  1.00 54.24  ? 150 GLU   A CB  1 
ATOM   890  C  CG  . GLU   A 1 122 ? 21.928  -20.160 61.641  1.00 57.59  ? 150 GLU   A CG  1 
ATOM   891  C  CD  . GLU   A 1 122 ? 21.891  -21.027 60.400  1.00 66.57  ? 150 GLU   A CD  1 
ATOM   892  O  OE1 . GLU   A 1 122 ? 22.080  -22.249 60.525  1.00 73.15  ? 150 GLU   A OE1 1 
ATOM   893  O  OE2 . GLU   A 1 122 ? 21.653  -20.481 59.307  1.00 73.07  ? 150 GLU   A OE2 1 
ATOM   894  N  N   . SER   A 1 123 ? 22.054  -18.286 64.389  1.00 46.48  ? 151 SER   A N   1 
ATOM   895  C  CA  . SER   A 1 123 ? 22.768  -18.569 65.631  1.00 47.39  ? 151 SER   A CA  1 
ATOM   896  C  C   . SER   A 1 123 ? 21.850  -18.419 66.833  1.00 47.46  ? 151 SER   A C   1 
ATOM   897  O  O   . SER   A 1 123 ? 21.831  -19.278 67.720  1.00 44.06  ? 151 SER   A O   1 
ATOM   898  C  CB  . SER   A 1 123 ? 23.980  -17.650 65.765  1.00 51.52  ? 151 SER   A CB  1 
ATOM   899  O  OG  . SER   A 1 123 ? 24.798  -17.745 64.617  1.00 56.46  ? 151 SER   A OG  1 
ATOM   900  N  N   . ALA   A 1 124 ? 21.081  -17.326 66.883  1.00 46.02  ? 152 ALA   A N   1 
ATOM   901  C  CA  . ALA   A 1 124 ? 20.100  -17.157 67.950  1.00 45.74  ? 152 ALA   A CA  1 
ATOM   902  C  C   . ALA   A 1 124 ? 19.232  -18.397 68.089  1.00 42.52  ? 152 ALA   A C   1 
ATOM   903  O  O   . ALA   A 1 124 ? 19.040  -18.914 69.193  1.00 44.87  ? 152 ALA   A O   1 
ATOM   904  C  CB  . ALA   A 1 124 ? 19.228  -15.923 67.685  1.00 42.13  ? 152 ALA   A CB  1 
ATOM   905  N  N   . PHE   A 1 125 ? 18.718  -18.901 66.964  1.00 41.54  ? 153 PHE   A N   1 
ATOM   906  C  CA  . PHE   A 1 125 ? 17.878  -20.096 66.992  1.00 39.73  ? 153 PHE   A CA  1 
ATOM   907  C  C   . PHE   A 1 125 ? 18.663  -21.314 67.466  1.00 42.68  ? 153 PHE   A C   1 
ATOM   908  O  O   . PHE   A 1 125 ? 18.172  -22.111 68.275  1.00 41.32  ? 153 PHE   A O   1 
ATOM   909  C  CB  . PHE   A 1 125 ? 17.295  -20.350 65.601  1.00 39.95  ? 153 PHE   A CB  1 
ATOM   910  C  CG  . PHE   A 1 125 ? 16.435  -21.584 65.515  1.00 42.30  ? 153 PHE   A CG  1 
ATOM   911  C  CD1 . PHE   A 1 125 ? 16.987  -22.817 65.200  1.00 39.89  ? 153 PHE   A CD1 1 
ATOM   912  C  CD2 . PHE   A 1 125 ? 15.067  -21.506 65.739  1.00 40.94  ? 153 PHE   A CD2 1 
ATOM   913  C  CE1 . PHE   A 1 125 ? 16.190  -23.944 65.117  1.00 44.07  ? 153 PHE   A CE1 1 
ATOM   914  C  CE2 . PHE   A 1 125 ? 14.265  -22.620 65.656  1.00 40.89  ? 153 PHE   A CE2 1 
ATOM   915  C  CZ  . PHE   A 1 125 ? 14.827  -23.850 65.345  1.00 44.14  ? 153 PHE   A CZ  1 
ATOM   916  N  N   . SER   A 1 126 ? 19.877  -21.486 66.949  1.00 43.77  ? 154 SER   A N   1 
ATOM   917  C  CA  . SER   A 1 126 ? 20.675  -22.669 67.296  1.00 47.43  ? 154 SER   A CA  1 
ATOM   918  C  C   . SER   A 1 126 ? 21.052  -22.662 68.771  1.00 42.14  ? 154 SER   A C   1 
ATOM   919  O  O   . SER   A 1 126 ? 20.780  -23.623 69.503  1.00 41.97  ? 154 SER   A O   1 
ATOM   920  C  CB  . SER   A 1 126 ? 21.933  -22.718 66.431  1.00 49.42  ? 154 SER   A CB  1 
ATOM   921  O  OG  . SER   A 1 126 ? 21.676  -23.454 65.247  1.00 57.60  ? 154 SER   A OG  1 
ATOM   922  N  N   . ILE   A 1 127 ? 21.656  -21.562 69.222  1.00 39.88  ? 155 ILE   A N   1 
ATOM   923  C  CA  . ILE   A 1 127 ? 22.000  -21.400 70.633  1.00 44.32  ? 155 ILE   A CA  1 
ATOM   924  C  C   . ILE   A 1 127 ? 20.767  -21.587 71.511  1.00 44.29  ? 155 ILE   A C   1 
ATOM   925  O  O   . ILE   A 1 127 ? 20.792  -22.344 72.491  1.00 39.43  ? 155 ILE   A O   1 
ATOM   926  C  CB  . ILE   A 1 127 ? 22.663  -20.028 70.864  1.00 47.58  ? 155 ILE   A CB  1 
ATOM   927  C  CG1 . ILE   A 1 127 ? 23.950  -19.907 70.038  1.00 49.51  ? 155 ILE   A CG1 1 
ATOM   928  C  CG2 . ILE   A 1 127 ? 22.971  -19.822 72.337  1.00 52.21  ? 155 ILE   A CG2 1 
ATOM   929  C  CD1 . ILE   A 1 127 ? 24.415  -18.484 69.827  1.00 46.94  ? 155 ILE   A CD1 1 
ATOM   930  N  N   . SER   A 1 128 ? 19.659  -20.911 71.163  1.00 41.10  ? 156 SER   A N   1 
ATOM   931  C  CA  . SER   A 1 128 ? 18.442  -21.027 71.963  1.00 42.57  ? 156 SER   A CA  1 
ATOM   932  C  C   . SER   A 1 128 ? 18.030  -22.477 72.147  1.00 38.62  ? 156 SER   A C   1 
ATOM   933  O  O   . SER   A 1 128 ? 17.809  -22.931 73.275  1.00 42.76  ? 156 SER   A O   1 
ATOM   934  C  CB  . SER   A 1 128 ? 17.285  -20.246 71.318  1.00 40.40  ? 156 SER   A CB  1 
ATOM   935  O  OG  . SER   A 1 128 ? 17.516  -18.851 71.403  1.00 43.72  ? 156 SER   A OG  1 
ATOM   936  N  N   . VAL   A 1 129 ? 17.853  -23.207 71.044  1.00 38.47  ? 157 VAL   A N   1 
ATOM   937  C  CA  . VAL   A 1 129 ? 17.373  -24.580 71.143  1.00 39.87  ? 157 VAL   A CA  1 
ATOM   938  C  C   . VAL   A 1 129 ? 18.386  -25.444 71.883  1.00 42.66  ? 157 VAL   A C   1 
ATOM   939  O  O   . VAL   A 1 129 ? 18.020  -26.334 72.666  1.00 39.70  ? 157 VAL   A O   1 
ATOM   940  C  CB  . VAL   A 1 129 ? 17.065  -25.141 69.744  1.00 40.72  ? 157 VAL   A CB  1 
ATOM   941  C  CG1 . VAL   A 1 129 ? 16.725  -26.617 69.833  1.00 42.04  ? 157 VAL   A CG1 1 
ATOM   942  C  CG2 . VAL   A 1 129 ? 15.892  -24.363 69.108  1.00 41.21  ? 157 VAL   A CG2 1 
ATOM   943  N  N   . ALA   A 1 130 ? 19.669  -25.187 71.663  1.00 39.53  ? 158 ALA   A N   1 
ATOM   944  C  CA  . ALA   A 1 130 ? 20.690  -25.933 72.398  1.00 48.03  ? 158 ALA   A CA  1 
ATOM   945  C  C   . ALA   A 1 130 ? 20.622  -25.655 73.891  1.00 47.15  ? 158 ALA   A C   1 
ATOM   946  O  O   . ALA   A 1 130 ? 21.188  -26.413 74.684  1.00 48.72  ? 158 ALA   A O   1 
ATOM   947  C  CB  . ALA   A 1 130 ? 22.082  -25.594 71.866  1.00 42.76  ? 158 ALA   A CB  1 
ATOM   948  N  N   . ASN   A 1 131 ? 19.927  -24.595 74.297  1.00 48.43  ? 159 ASN   A N   1 
ATOM   949  C  CA  . ASN   A 1 131 ? 19.757  -24.288 75.707  1.00 46.04  ? 159 ASN   A CA  1 
ATOM   950  C  C   . ASN   A 1 131 ? 18.302  -24.436 76.144  1.00 41.21  ? 159 ASN   A C   1 
ATOM   951  O  O   . ASN   A 1 131 ? 17.853  -23.780 77.085  1.00 49.69  ? 159 ASN   A O   1 
ATOM   952  C  CB  . ASN   A 1 131 ? 20.322  -22.902 76.006  1.00 44.20  ? 159 ASN   A CB  1 
ATOM   953  C  CG  . ASN   A 1 131 ? 21.836  -22.918 76.069  1.00 47.41  ? 159 ASN   A CG  1 
ATOM   954  O  OD1 . ASN   A 1 131 ? 22.406  -23.377 77.059  1.00 46.85  ? 159 ASN   A OD1 1 
ATOM   955  N  ND2 . ASN   A 1 131 ? 22.497  -22.452 75.007  1.00 45.28  ? 159 ASN   A ND2 1 
ATOM   956  N  N   . GLY   A 1 132 ? 17.564  -25.313 75.477  1.00 38.93  ? 160 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 132 ? 16.262  -25.738 75.937  1.00 42.06  ? 160 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 132 ? 15.071  -25.075 75.261  1.00 37.13  ? 160 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 132 ? 13.939  -25.497 75.516  1.00 41.58  ? 160 GLY   A O   1 
ATOM   960  N  N   . ALA   A 1 133 ? 15.283  -24.074 74.406  1.00 38.19  ? 161 ALA   A N   1 
ATOM   961  C  CA  . ALA   A 1 133 ? 14.159  -23.475 73.683  1.00 41.97  ? 161 ALA   A CA  1 
ATOM   962  C  C   . ALA   A 1 133 ? 13.454  -24.524 72.835  1.00 42.25  ? 161 ALA   A C   1 
ATOM   963  O  O   . ALA   A 1 133 ? 14.096  -25.354 72.185  1.00 41.25  ? 161 ALA   A O   1 
ATOM   964  C  CB  . ALA   A 1 133 ? 14.631  -22.341 72.776  1.00 39.03  ? 161 ALA   A CB  1 
ATOM   965  N  N   . ILE   A 1 134 ? 12.123  -24.490 72.836  1.00 40.21  ? 162 ILE   A N   1 
ATOM   966  C  CA  . ILE   A 1 134 ? 11.320  -25.393 72.019  1.00 38.21  ? 162 ILE   A CA  1 
ATOM   967  C  C   . ILE   A 1 134 ? 11.205  -24.767 70.632  1.00 44.72  ? 162 ILE   A C   1 
ATOM   968  O  O   . ILE   A 1 134 ? 10.587  -23.686 70.500  1.00 39.79  ? 162 ILE   A O   1 
ATOM   969  C  CB  . ILE   A 1 134 ? 9.941   -25.647 72.640  1.00 42.06  ? 162 ILE   A CB  1 
ATOM   970  C  CG1 . ILE   A 1 134 ? 10.105  -26.083 74.095  1.00 42.27  ? 162 ILE   A CG1 1 
ATOM   971  C  CG2 . ILE   A 1 134 ? 9.148   -26.675 71.826  1.00 44.38  ? 162 ILE   A CG2 1 
ATOM   972  C  CD1 . ILE   A 1 134 ? 8.852   -26.712 74.675  1.00 50.06  ? 162 ILE   A CD1 1 
ATOM   973  N  N   . PRO   A 1 135 ? 11.796  -25.365 69.602  1.00 43.68  ? 163 PRO   A N   1 
ATOM   974  C  CA  . PRO   A 1 135 ? 11.688  -24.794 68.256  1.00 42.57  ? 163 PRO   A CA  1 
ATOM   975  C  C   . PRO   A 1 135 ? 10.238  -24.648 67.835  1.00 40.69  ? 163 PRO   A C   1 
ATOM   976  O  O   . PRO   A 1 135 ? 9.388   -25.487 68.137  1.00 39.88  ? 163 PRO   A O   1 
ATOM   977  C  CB  . PRO   A 1 135 ? 12.439  -25.801 67.381  1.00 46.88  ? 163 PRO   A CB  1 
ATOM   978  C  CG  . PRO   A 1 135 ? 12.482  -27.081 68.214  1.00 49.26  ? 163 PRO   A CG  1 
ATOM   979  C  CD  . PRO   A 1 135 ? 12.617  -26.585 69.619  1.00 46.23  ? 163 PRO   A CD  1 
ATOM   980  N  N   . SER   A 1 136 ? 9.946   -23.536 67.173  1.00 43.61  ? 164 SER   A N   1 
ATOM   981  C  CA  . SER   A 1 136 ? 8.636   -23.310 66.584  1.00 39.49  ? 164 SER   A CA  1 
ATOM   982  C  C   . SER   A 1 136 ? 8.719   -23.230 65.071  1.00 39.95  ? 164 SER   A C   1 
ATOM   983  O  O   . SER   A 1 136 ? 7.898   -23.816 64.378  1.00 43.91  ? 164 SER   A O   1 
ATOM   984  C  CB  . SER   A 1 136 ? 8.008   -22.019 67.138  1.00 37.56  ? 164 SER   A CB  1 
ATOM   985  O  OG  . SER   A 1 136 ? 6.621   -21.978 66.836  1.00 41.97  ? 164 SER   A OG  1 
ATOM   986  N  N   . SER   A 1 137 ? 9.703   -22.506 64.537  1.00 41.28  ? 165 SER   A N   1 
ATOM   987  C  CA  . SER   A 1 137 ? 9.852   -22.495 63.110  1.00 41.58  ? 165 SER   A CA  1 
ATOM   988  C  C   . SER   A 1 137 ? 11.336  -22.295 62.841  1.00 40.99  ? 165 SER   A C   1 
ATOM   989  O  O   . SER   A 1 137 ? 11.940  -21.373 63.413  1.00 41.41  ? 165 SER   A O   1 
ATOM   990  C  CB  . SER   A 1 137 ? 9.023   -21.401 62.433  1.00 43.46  ? 165 SER   A CB  1 
ATOM   991  O  OG  . SER   A 1 137 ? 9.505   -21.136 61.126  1.00 49.04  ? 165 SER   A OG  1 
ATOM   992  N  N   . PRO   A 1 138 ? 11.944  -23.127 62.002  1.00 40.80  ? 166 PRO   A N   1 
ATOM   993  C  CA  . PRO   A 1 138 ? 13.405  -23.105 61.861  1.00 42.39  ? 166 PRO   A CA  1 
ATOM   994  C  C   . PRO   A 1 138 ? 13.847  -21.872 61.093  1.00 44.55  ? 166 PRO   A C   1 
ATOM   995  O  O   . PRO   A 1 138 ? 13.023  -21.232 60.417  1.00 45.33  ? 166 PRO   A O   1 
ATOM   996  C  CB  . PRO   A 1 138 ? 13.712  -24.405 61.095  1.00 46.60  ? 166 PRO   A CB  1 
ATOM   997  C  CG  . PRO   A 1 138 ? 12.444  -24.725 60.342  1.00 49.89  ? 166 PRO   A CG  1 
ATOM   998  C  CD  . PRO   A 1 138 ? 11.284  -24.031 61.038  1.00 46.90  ? 166 PRO   A CD  1 
ATOM   999  N  N   . PRO   A 1 139 ? 15.123  -21.486 61.198  1.00 40.07  ? 167 PRO   A N   1 
ATOM   1000 C  CA  . PRO   A 1 139 ? 15.576  -20.272 60.506  1.00 41.28  ? 167 PRO   A CA  1 
ATOM   1001 C  C   . PRO   A 1 139 ? 15.372  -20.408 59.007  1.00 42.78  ? 167 PRO   A C   1 
ATOM   1002 O  O   . PRO   A 1 139 ? 15.591  -21.470 58.428  1.00 40.39  ? 167 PRO   A O   1 
ATOM   1003 C  CB  . PRO   A 1 139 ? 17.071  -20.181 60.866  1.00 43.04  ? 167 PRO   A CB  1 
ATOM   1004 C  CG  . PRO   A 1 139 ? 17.258  -21.052 62.066  1.00 42.18  ? 167 PRO   A CG  1 
ATOM   1005 C  CD  . PRO   A 1 139 ? 16.230  -22.163 61.904  1.00 42.34  ? 167 PRO   A CD  1 
ATOM   1006 N  N   . ILE   A 1 140 ? 14.922  -19.329 58.380  1.00 41.87  ? 168 ILE   A N   1 
ATOM   1007 C  CA  . ILE   A 1 140 ? 14.717  -19.311 56.938  1.00 45.68  ? 168 ILE   A CA  1 
ATOM   1008 C  C   . ILE   A 1 140 ? 15.202  -17.975 56.406  1.00 46.82  ? 168 ILE   A C   1 
ATOM   1009 O  O   . ILE   A 1 140 ? 14.854  -16.918 56.945  1.00 44.78  ? 168 ILE   A O   1 
ATOM   1010 C  CB  . ILE   A 1 140 ? 13.244  -19.561 56.552  1.00 49.12  ? 168 ILE   A CB  1 
ATOM   1011 C  CG1 . ILE   A 1 140 ? 13.051  -19.449 55.037  1.00 45.14  ? 168 ILE   A CG1 1 
ATOM   1012 C  CG2 . ILE   A 1 140 ? 12.327  -18.598 57.277  1.00 50.09  ? 168 ILE   A CG2 1 
ATOM   1013 C  CD1 . ILE   A 1 140 ? 11.931  -20.343 54.516  1.00 57.11  ? 168 ILE   A CD1 1 
ATOM   1014 N  N   . VAL   A 1 141 ? 16.023  -18.025 55.364  1.00 45.44  ? 169 VAL   A N   1 
ATOM   1015 C  CA  . VAL   A 1 141 ? 16.612  -16.824 54.787  1.00 52.83  ? 169 VAL   A CA  1 
ATOM   1016 C  C   . VAL   A 1 141 ? 15.665  -16.290 53.726  1.00 53.15  ? 169 VAL   A C   1 
ATOM   1017 O  O   . VAL   A 1 141 ? 15.224  -17.029 52.837  1.00 54.89  ? 169 VAL   A O   1 
ATOM   1018 C  CB  . VAL   A 1 141 ? 18.005  -17.118 54.209  1.00 52.07  ? 169 VAL   A CB  1 
ATOM   1019 C  CG1 . VAL   A 1 141 ? 18.662  -15.831 53.724  1.00 52.53  ? 169 VAL   A CG1 1 
ATOM   1020 C  CG2 . VAL   A 1 141 ? 18.845  -17.804 55.254  1.00 50.71  ? 169 VAL   A CG2 1 
ATOM   1021 N  N   . LEU   A 1 142 ? 15.331  -15.012 53.832  1.00 54.06  ? 170 LEU   A N   1 
ATOM   1022 C  CA  . LEU   A 1 142 ? 14.324  -14.388 52.988  1.00 54.31  ? 170 LEU   A CA  1 
ATOM   1023 C  C   . LEU   A 1 142 ? 15.021  -13.475 51.986  1.00 58.10  ? 170 LEU   A C   1 
ATOM   1024 O  O   . LEU   A 1 142 ? 15.605  -12.453 52.369  1.00 56.65  ? 170 LEU   A O   1 
ATOM   1025 C  CB  . LEU   A 1 142 ? 13.318  -13.625 53.845  1.00 54.61  ? 170 LEU   A CB  1 
ATOM   1026 C  CG  . LEU   A 1 142 ? 12.434  -14.523 54.720  1.00 54.38  ? 170 LEU   A CG  1 
ATOM   1027 C  CD1 . LEU   A 1 142 ? 11.667  -13.702 55.740  1.00 58.08  ? 170 LEU   A CD1 1 
ATOM   1028 C  CD2 . LEU   A 1 142 ? 11.464  -15.292 53.851  1.00 53.62  ? 170 LEU   A CD2 1 
ATOM   1029 N  N   . ASN   A 1 143 ? 14.964  -13.856 50.706  1.00 60.14  ? 171 ASN   A N   1 
ATOM   1030 C  CA  . ASN   A 1 143 ? 15.471  -13.035 49.604  1.00 60.94  ? 171 ASN   A CA  1 
ATOM   1031 C  C   . ASN   A 1 143 ? 16.944  -12.681 49.795  1.00 63.61  ? 171 ASN   A C   1 
ATOM   1032 O  O   . ASN   A 1 143 ? 17.380  -11.568 49.484  1.00 61.87  ? 171 ASN   A O   1 
ATOM   1033 C  CB  . ASN   A 1 143 ? 14.621  -11.773 49.431  1.00 63.06  ? 171 ASN   A CB  1 
ATOM   1034 C  CG  . ASN   A 1 143 ? 14.844  -11.100 48.094  1.00 66.62  ? 171 ASN   A CG  1 
ATOM   1035 O  OD1 . ASN   A 1 143 ? 15.372  -11.710 47.161  1.00 70.48  ? 171 ASN   A OD1 1 
ATOM   1036 N  ND2 . ASN   A 1 143 ? 14.452  -9.835  47.995  1.00 67.16  ? 171 ASN   A ND2 1 
ATOM   1037 N  N   . GLU   A 1 144 ? 17.714  -13.635 50.328  1.00 59.37  ? 172 GLU   A N   1 
ATOM   1038 C  CA  . GLU   A 1 144 ? 19.147  -13.469 50.596  1.00 62.71  ? 172 GLU   A CA  1 
ATOM   1039 C  C   . GLU   A 1 144 ? 19.438  -12.254 51.473  1.00 61.18  ? 172 GLU   A C   1 
ATOM   1040 O  O   . GLU   A 1 144 ? 20.579  -11.784 51.530  1.00 59.86  ? 172 GLU   A O   1 
ATOM   1041 C  CB  . GLU   A 1 144 ? 19.952  -13.375 49.294  1.00 65.39  ? 172 GLU   A CB  1 
ATOM   1042 C  CG  . GLU   A 1 144 ? 19.640  -14.471 48.286  1.00 69.37  ? 172 GLU   A CG  1 
ATOM   1043 C  CD  . GLU   A 1 144 ? 20.378  -14.288 46.970  1.00 75.06  ? 172 GLU   A CD  1 
ATOM   1044 O  OE1 . GLU   A 1 144 ? 21.555  -13.870 46.994  1.00 76.95  ? 172 GLU   A OE1 1 
ATOM   1045 O  OE2 . GLU   A 1 144 ? 19.776  -14.556 45.908  1.00 78.61  ? 172 GLU   A OE2 1 
ATOM   1046 N  N   . ALA   A 1 145 ? 18.432  -11.739 52.171  1.00 55.62  ? 173 ALA   A N   1 
ATOM   1047 C  CA  . ALA   A 1 145 ? 18.568  -10.471 52.878  1.00 57.08  ? 173 ALA   A CA  1 
ATOM   1048 C  C   . ALA   A 1 145 ? 18.230  -10.556 54.356  1.00 56.02  ? 173 ALA   A C   1 
ATOM   1049 O  O   . ALA   A 1 145 ? 18.887  -9.903  55.171  1.00 51.93  ? 173 ALA   A O   1 
ATOM   1050 C  CB  . ALA   A 1 145 ? 17.674  -9.410  52.221  1.00 54.29  ? 173 ALA   A CB  1 
ATOM   1051 N  N   . VAL   A 1 146 ? 17.211  -11.329 54.726  1.00 54.10  ? 174 VAL   A N   1 
ATOM   1052 C  CA  . VAL   A 1 146 ? 16.683  -11.332 56.083  1.00 50.52  ? 174 VAL   A CA  1 
ATOM   1053 C  C   . VAL   A 1 146 ? 16.509  -12.771 56.526  1.00 46.89  ? 174 VAL   A C   1 
ATOM   1054 O  O   . VAL   A 1 146 ? 16.049  -13.614 55.749  1.00 49.03  ? 174 VAL   A O   1 
ATOM   1055 C  CB  . VAL   A 1 146 ? 15.333  -10.586 56.183  1.00 50.66  ? 174 VAL   A CB  1 
ATOM   1056 C  CG1 . VAL   A 1 146 ? 14.944  -10.417 57.647  1.00 48.88  ? 174 VAL   A CG1 1 
ATOM   1057 C  CG2 . VAL   A 1 146 ? 15.391  -9.240  55.460  1.00 51.21  ? 174 VAL   A CG2 1 
ATOM   1058 N  N   . THR   A 1 147 ? 16.845  -13.045 57.780  1.00 43.07  ? 175 THR   A N   1 
ATOM   1059 C  CA  . THR   A 1 147 ? 16.648  -14.366 58.361  1.00 49.21  ? 175 THR   A CA  1 
ATOM   1060 C  C   . THR   A 1 147 ? 15.609  -14.292 59.473  1.00 44.31  ? 175 THR   A C   1 
ATOM   1061 O  O   . THR   A 1 147 ? 15.644  -13.381 60.308  1.00 43.20  ? 175 THR   A O   1 
ATOM   1062 C  CB  . THR   A 1 147 ? 17.974  -14.927 58.891  1.00 45.86  ? 175 THR   A CB  1 
ATOM   1063 O  OG1 . THR   A 1 147 ? 18.870  -15.103 57.791  1.00 45.91  ? 175 THR   A OG1 1 
ATOM   1064 C  CG2 . THR   A 1 147 ? 17.765  -16.257 59.564  1.00 47.38  ? 175 THR   A CG2 1 
ATOM   1065 N  N   . ILE   A 1 148 ? 14.683  -15.254 59.479  1.00 43.69  ? 176 ILE   A N   1 
ATOM   1066 C  CA  . ILE   A 1 148 ? 13.617  -15.312 60.471  1.00 42.96  ? 176 ILE   A CA  1 
ATOM   1067 C  C   . ILE   A 1 148 ? 13.584  -16.693 61.094  1.00 39.71  ? 176 ILE   A C   1 
ATOM   1068 O  O   . ILE   A 1 148 ? 13.665  -17.700 60.385  1.00 41.25  ? 176 ILE   A O   1 
ATOM   1069 C  CB  . ILE   A 1 148 ? 12.242  -14.991 59.864  1.00 46.42  ? 176 ILE   A CB  1 
ATOM   1070 C  CG1 . ILE   A 1 148 ? 12.273  -13.612 59.230  1.00 44.92  ? 176 ILE   A CG1 1 
ATOM   1071 C  CG2 . ILE   A 1 148 ? 11.168  -15.052 60.941  1.00 45.77  ? 176 ILE   A CG2 1 
ATOM   1072 C  CD1 . ILE   A 1 148 ? 12.525  -12.561 60.218  1.00 49.39  ? 176 ILE   A CD1 1 
ATOM   1073 N  N   . ALA   A 1 149 ? 13.406  -16.739 62.412  1.00 36.92  ? 177 ALA   A N   1 
ATOM   1074 C  CA  . ALA   A 1 149 ? 13.284  -17.993 63.136  1.00 39.26  ? 177 ALA   A CA  1 
ATOM   1075 C  C   . ALA   A 1 149 ? 12.447  -17.768 64.384  1.00 37.51  ? 177 ALA   A C   1 
ATOM   1076 O  O   . ALA   A 1 149 ? 12.447  -16.673 64.941  1.00 34.49  ? 177 ALA   A O   1 
ATOM   1077 C  CB  . ALA   A 1 149 ? 14.659  -18.542 63.526  1.00 40.14  ? 177 ALA   A CB  1 
ATOM   1078 N  N   . GLU   A 1 150 ? 11.776  -18.827 64.851  1.00 34.79  ? 178 GLU   A N   1 
ATOM   1079 C  CA  . GLU   A 1 150 ? 10.877  -18.702 65.994  1.00 40.27  ? 178 GLU   A CA  1 
ATOM   1080 C  C   . GLU   A 1 150 ? 11.072  -19.829 66.996  1.00 40.80  ? 178 GLU   A C   1 
ATOM   1081 O  O   . GLU   A 1 150 ? 11.209  -20.991 66.607  1.00 38.81  ? 178 GLU   A O   1 
ATOM   1082 C  CB  . GLU   A 1 150 ? 9.412   -18.691 65.522  1.00 38.27  ? 178 GLU   A CB  1 
ATOM   1083 C  CG  . GLU   A 1 150 ? 9.162   -17.517 64.601  1.00 37.22  ? 178 GLU   A CG  1 
ATOM   1084 C  CD  . GLU   A 1 150 ? 7.797   -17.533 63.951  1.00 39.38  ? 178 GLU   A CD  1 
ATOM   1085 O  OE1 . GLU   A 1 150 ? 6.960   -18.381 64.324  1.00 35.81  ? 178 GLU   A OE1 1 
ATOM   1086 O  OE2 . GLU   A 1 150 ? 7.575   -16.680 63.065  1.00 40.09  ? 178 GLU   A OE2 1 
ATOM   1087 N  N   . VAL   A 1 151 ? 11.051  -19.489 68.289  1.00 37.06  ? 179 VAL   A N   1 
ATOM   1088 C  CA  . VAL   A 1 151 ? 10.997  -20.492 69.348  1.00 38.34  ? 179 VAL   A CA  1 
ATOM   1089 C  C   . VAL   A 1 151 ? 9.796   -20.194 70.234  1.00 40.72  ? 179 VAL   A C   1 
ATOM   1090 O  O   . VAL   A 1 151 ? 9.258   -19.086 70.243  1.00 36.08  ? 179 VAL   A O   1 
ATOM   1091 C  CB  . VAL   A 1 151 ? 12.293  -20.537 70.184  1.00 41.62  ? 179 VAL   A CB  1 
ATOM   1092 C  CG1 . VAL   A 1 151 ? 13.462  -20.927 69.312  1.00 42.46  ? 179 VAL   A CG1 1 
ATOM   1093 C  CG2 . VAL   A 1 151 ? 12.551  -19.167 70.812  1.00 37.66  ? 179 VAL   A CG2 1 
ATOM   1094 N  N   . LYS   A 1 152 ? 9.338   -21.211 70.956  1.00 38.58  ? 180 LYS   A N   1 
ATOM   1095 C  CA  . LYS   A 1 152 ? 8.213   -20.986 71.850  1.00 38.39  ? 180 LYS   A CA  1 
ATOM   1096 C  C   . LYS   A 1 152 ? 8.621   -20.091 73.015  1.00 38.36  ? 180 LYS   A C   1 
ATOM   1097 O  O   . LYS   A 1 152 ? 9.712   -20.219 73.574  1.00 35.84  ? 180 LYS   A O   1 
ATOM   1098 C  CB  . LYS   A 1 152 ? 7.663   -22.312 72.349  1.00 36.68  ? 180 LYS   A CB  1 
ATOM   1099 C  CG  . LYS   A 1 152 ? 7.023   -23.125 71.247  1.00 38.06  ? 180 LYS   A CG  1 
ATOM   1100 C  CD  . LYS   A 1 152 ? 6.452   -24.411 71.817  1.00 42.35  ? 180 LYS   A CD  1 
ATOM   1101 C  CE  . LYS   A 1 152 ? 5.652   -25.180 70.779  1.00 48.10  ? 180 LYS   A CE  1 
ATOM   1102 N  NZ  . LYS   A 1 152 ? 4.881   -26.263 71.450  1.00 55.80  ? 180 LYS   A NZ  1 
ATOM   1103 N  N   . LEU   A 1 153 ? 7.755   -19.133 73.348  1.00 41.25  ? 181 LEU   A N   1 
ATOM   1104 C  CA  . LEU   A 1 153 ? 7.999   -18.227 74.467  1.00 37.10  ? 181 LEU   A CA  1 
ATOM   1105 C  C   . LEU   A 1 153 ? 7.168   -18.635 75.681  1.00 38.95  ? 181 LEU   A C   1 
ATOM   1106 O  O   . LEU   A 1 153 ? 7.712   -18.948 76.744  1.00 43.22  ? 181 LEU   A O   1 
ATOM   1107 C  CB  . LEU   A 1 153 ? 7.691   -16.775 74.044  1.00 36.78  ? 181 LEU   A CB  1 
ATOM   1108 C  CG  . LEU   A 1 153 ? 8.098   -15.632 74.979  1.00 40.27  ? 181 LEU   A CG  1 
ATOM   1109 C  CD1 . LEU   A 1 153 ? 9.556   -15.706 75.347  1.00 39.66  ? 181 LEU   A CD1 1 
ATOM   1110 C  CD2 . LEU   A 1 153 ? 7.782   -14.264 74.335  1.00 37.76  ? 181 LEU   A CD2 1 
ATOM   1111 N  N   . TYR   A 1 154 ? 5.845   -18.631 75.534  1.00 39.57  ? 182 TYR   A N   1 
ATOM   1112 C  CA  . TYR   A 1 154 ? 4.914   -19.114 76.543  1.00 38.89  ? 182 TYR   A CA  1 
ATOM   1113 C  C   . TYR   A 1 154 ? 3.546   -19.205 75.891  1.00 38.30  ? 182 TYR   A C   1 
ATOM   1114 O  O   . TYR   A 1 154 ? 3.241   -18.456 74.954  1.00 40.50  ? 182 TYR   A O   1 
ATOM   1115 C  CB  . TYR   A 1 154 ? 4.883   -18.219 77.797  1.00 41.21  ? 182 TYR   A CB  1 
ATOM   1116 C  CG  . TYR   A 1 154 ? 4.989   -16.728 77.542  1.00 40.72  ? 182 TYR   A CG  1 
ATOM   1117 C  CD1 . TYR   A 1 154 ? 4.030   -16.066 76.789  1.00 41.36  ? 182 TYR   A CD1 1 
ATOM   1118 C  CD2 . TYR   A 1 154 ? 6.036   -15.980 78.075  1.00 43.96  ? 182 TYR   A CD2 1 
ATOM   1119 C  CE1 . TYR   A 1 154 ? 4.114   -14.696 76.558  1.00 39.69  ? 182 TYR   A CE1 1 
ATOM   1120 C  CE2 . TYR   A 1 154 ? 6.130   -14.598 77.846  1.00 41.58  ? 182 TYR   A CE2 1 
ATOM   1121 C  CZ  . TYR   A 1 154 ? 5.162   -13.971 77.085  1.00 44.16  ? 182 TYR   A CZ  1 
ATOM   1122 O  OH  . TYR   A 1 154 ? 5.234   -12.609 76.847  1.00 38.70  ? 182 TYR   A OH  1 
ATOM   1123 N  N   . GLY   A 1 155 ? 2.742   -20.145 76.382  1.00 37.25  ? 183 GLY   A N   1 
ATOM   1124 C  CA  . GLY   A 1 155 ? 1.494   -20.479 75.726  1.00 40.52  ? 183 GLY   A CA  1 
ATOM   1125 C  C   . GLY   A 1 155 ? 1.701   -20.751 74.251  1.00 42.37  ? 183 GLY   A C   1 
ATOM   1126 O  O   . GLY   A 1 155 ? 2.564   -21.549 73.846  1.00 36.60  ? 183 GLY   A O   1 
ATOM   1127 N  N   . ASP   A 1 156 ? 0.893   -20.074 73.434  1.00 38.76  ? 184 ASP   A N   1 
ATOM   1128 C  CA  . ASP   A 1 156 ? 0.984   -20.122 71.983  1.00 38.51  ? 184 ASP   A CA  1 
ATOM   1129 C  C   . ASP   A 1 156 ? 1.671   -18.885 71.412  1.00 37.86  ? 184 ASP   A C   1 
ATOM   1130 O  O   . ASP   A 1 156 ? 1.532   -18.601 70.218  1.00 39.10  ? 184 ASP   A O   1 
ATOM   1131 C  CB  . ASP   A 1 156 ? -0.409  -20.281 71.375  1.00 41.30  ? 184 ASP   A CB  1 
ATOM   1132 C  CG  . ASP   A 1 156 ? -1.048  -21.610 71.725  1.00 45.11  ? 184 ASP   A CG  1 
ATOM   1133 O  OD1 . ASP   A 1 156 ? -0.328  -22.622 71.728  1.00 43.87  ? 184 ASP   A OD1 1 
ATOM   1134 O  OD2 . ASP   A 1 156 ? -2.267  -21.637 71.992  1.00 45.34  ? 184 ASP   A OD2 1 
ATOM   1135 N  N   . VAL   A 1 157 ? 2.378   -18.139 72.248  1.00 35.82  ? 185 VAL   A N   1 
ATOM   1136 C  CA  . VAL   A 1 157 ? 3.186   -16.987 71.849  1.00 34.23  ? 185 VAL   A CA  1 
ATOM   1137 C  C   . VAL   A 1 157 ? 4.594   -17.464 71.532  1.00 37.74  ? 185 VAL   A C   1 
ATOM   1138 O  O   . VAL   A 1 157 ? 5.160   -18.287 72.263  1.00 35.45  ? 185 VAL   A O   1 
ATOM   1139 C  CB  . VAL   A 1 157 ? 3.207   -15.933 72.968  1.00 37.69  ? 185 VAL   A CB  1 
ATOM   1140 C  CG1 . VAL   A 1 157 ? 4.064   -14.714 72.560  1.00 36.70  ? 185 VAL   A CG1 1 
ATOM   1141 C  CG2 . VAL   A 1 157 ? 1.782   -15.506 73.322  1.00 37.59  ? 185 VAL   A CG2 1 
ATOM   1142 N  N   . VAL   A 1 158 ? 5.179   -16.945 70.454  1.00 36.42  ? 186 VAL   A N   1 
ATOM   1143 C  CA  . VAL   A 1 158 ? 6.551   -17.296 70.102  1.00 36.71  ? 186 VAL   A CA  1 
ATOM   1144 C  C   . VAL   A 1 158 ? 7.442   -16.058 70.207  1.00 40.10  ? 186 VAL   A C   1 
ATOM   1145 O  O   . VAL   A 1 158 ? 6.990   -14.911 70.103  1.00 37.21  ? 186 VAL   A O   1 
ATOM   1146 C  CB  . VAL   A 1 158 ? 6.642   -17.930 68.688  1.00 35.03  ? 186 VAL   A CB  1 
ATOM   1147 C  CG1 . VAL   A 1 158 ? 5.702   -19.150 68.558  1.00 37.63  ? 186 VAL   A CG1 1 
ATOM   1148 C  CG2 . VAL   A 1 158 ? 6.345   -16.882 67.598  1.00 37.97  ? 186 VAL   A CG2 1 
ATOM   1149 N  N   . LEU   A 1 159 ? 8.723   -16.300 70.444  1.00 37.74  ? 187 LEU   A N   1 
ATOM   1150 C  CA  . LEU   A 1 159 ? 9.754   -15.270 70.334  1.00 38.43  ? 187 LEU   A CA  1 
ATOM   1151 C  C   . LEU   A 1 159 ? 10.388  -15.395 68.953  1.00 36.60  ? 187 LEU   A C   1 
ATOM   1152 O  O   . LEU   A 1 159 ? 10.970  -16.431 68.633  1.00 36.52  ? 187 LEU   A O   1 
ATOM   1153 C  CB  . LEU   A 1 159 ? 10.799  -15.424 71.437  1.00 40.06  ? 187 LEU   A CB  1 
ATOM   1154 C  CG  . LEU   A 1 159 ? 11.927  -14.401 71.550  1.00 38.83  ? 187 LEU   A CG  1 
ATOM   1155 C  CD1 . LEU   A 1 159 ? 11.386  -12.993 71.912  1.00 34.05  ? 187 LEU   A CD1 1 
ATOM   1156 C  CD2 . LEU   A 1 159 ? 12.925  -14.874 72.588  1.00 41.97  ? 187 LEU   A CD2 1 
ATOM   1157 N  N   . ARG   A 1 160 ? 10.237  -14.364 68.128  1.00 36.30  ? 188 ARG   A N   1 
ATOM   1158 C  CA  . ARG   A 1 160 ? 10.681  -14.377 66.737  1.00 33.93  ? 188 ARG   A CA  1 
ATOM   1159 C  C   . ARG   A 1 160 ? 12.004  -13.632 66.611  1.00 37.38  ? 188 ARG   A C   1 
ATOM   1160 O  O   . ARG   A 1 160 ? 12.057  -12.433 66.879  1.00 33.49  ? 188 ARG   A O   1 
ATOM   1161 C  CB  . ARG   A 1 160 ? 9.630   -13.727 65.837  1.00 35.48  ? 188 ARG   A CB  1 
ATOM   1162 C  CG  . ARG   A 1 160 ? 10.077  -13.526 64.402  1.00 37.03  ? 188 ARG   A CG  1 
ATOM   1163 C  CD  . ARG   A 1 160 ? 8.965   -12.922 63.576  1.00 30.46  ? 188 ARG   A CD  1 
ATOM   1164 N  NE  . ARG   A 1 160 ? 7.876   -13.894 63.392  1.00 36.04  ? 188 ARG   A NE  1 
ATOM   1165 C  CZ  . ARG   A 1 160 ? 6.604   -13.577 63.182  1.00 37.63  ? 188 ARG   A CZ  1 
ATOM   1166 N  NH1 . ARG   A 1 160 ? 6.230   -12.301 63.139  1.00 34.43  ? 188 ARG   A NH1 1 
ATOM   1167 N  NH2 . ARG   A 1 160 ? 5.694   -14.533 63.029  1.00 36.52  ? 188 ARG   A NH2 1 
ATOM   1168 N  N   . TYR   A 1 161 ? 13.066  -14.337 66.200  1.00 35.25  ? 189 TYR   A N   1 
ATOM   1169 C  CA  . TYR   A 1 161 ? 14.347  -13.696 65.918  1.00 38.80  ? 189 TYR   A CA  1 
ATOM   1170 C  C   . TYR   A 1 161 ? 14.370  -13.180 64.485  1.00 34.40  ? 189 TYR   A C   1 
ATOM   1171 O  O   . TYR   A 1 161 ? 13.967  -13.887 63.554  1.00 38.23  ? 189 TYR   A O   1 
ATOM   1172 C  CB  . TYR   A 1 161 ? 15.496  -14.683 66.133  1.00 39.62  ? 189 TYR   A CB  1 
ATOM   1173 C  CG  . TYR   A 1 161 ? 15.534  -15.270 67.520  1.00 38.42  ? 189 TYR   A CG  1 
ATOM   1174 C  CD1 . TYR   A 1 161 ? 15.379  -14.462 68.639  1.00 35.96  ? 189 TYR   A CD1 1 
ATOM   1175 C  CD2 . TYR   A 1 161 ? 15.711  -16.628 67.710  1.00 40.89  ? 189 TYR   A CD2 1 
ATOM   1176 C  CE1 . TYR   A 1 161 ? 15.403  -14.995 69.905  1.00 40.14  ? 189 TYR   A CE1 1 
ATOM   1177 C  CE2 . TYR   A 1 161 ? 15.746  -17.175 68.976  1.00 41.71  ? 189 TYR   A CE2 1 
ATOM   1178 C  CZ  . TYR   A 1 161 ? 15.601  -16.355 70.068  1.00 37.98  ? 189 TYR   A CZ  1 
ATOM   1179 O  OH  . TYR   A 1 161 ? 15.625  -16.898 71.325  1.00 39.81  ? 189 TYR   A OH  1 
ATOM   1180 N  N   . VAL   A 1 162 ? 14.832  -11.952 64.310  1.00 34.72  ? 190 VAL   A N   1 
ATOM   1181 C  CA  . VAL   A 1 162 ? 14.991  -11.344 62.995  1.00 37.47  ? 190 VAL   A CA  1 
ATOM   1182 C  C   . VAL   A 1 162 ? 16.402  -10.782 62.908  1.00 41.81  ? 190 VAL   A C   1 
ATOM   1183 O  O   . VAL   A 1 162 ? 16.829  -10.047 63.803  1.00 41.94  ? 190 VAL   A O   1 
ATOM   1184 C  CB  . VAL   A 1 162 ? 13.976  -10.211 62.740  1.00 41.01  ? 190 VAL   A CB  1 
ATOM   1185 C  CG1 . VAL   A 1 162 ? 14.116  -9.719  61.313  1.00 42.87  ? 190 VAL   A CG1 1 
ATOM   1186 C  CG2 . VAL   A 1 162 ? 12.543  -10.651 63.037  1.00 38.65  ? 190 VAL   A CG2 1 
ATOM   1187 N  N   . SER   A 1 163 ? 17.116  -11.115 61.834  1.00 41.40  ? 191 SER   A N   1 
ATOM   1188 C  CA  . SER   A 1 163 ? 18.420  -10.526 61.563  1.00 45.88  ? 191 SER   A CA  1 
ATOM   1189 C  C   . SER   A 1 163 ? 18.492  -10.090 60.106  1.00 46.37  ? 191 SER   A C   1 
ATOM   1190 O  O   . SER   A 1 163 ? 17.916  -10.722 59.220  1.00 44.22  ? 191 SER   A O   1 
ATOM   1191 C  CB  . SER   A 1 163 ? 19.574  -11.504 61.872  1.00 43.60  ? 191 SER   A CB  1 
ATOM   1192 O  OG  . SER   A 1 163 ? 19.598  -12.546 60.920  1.00 43.21  ? 191 SER   A OG  1 
ATOM   1193 N  N   . TYR   A 1 164 ? 19.221  -9.005  59.866  1.00 50.14  ? 192 TYR   A N   1 
ATOM   1194 C  CA  . TYR   A 1 164 ? 19.427  -8.468  58.528  1.00 54.22  ? 192 TYR   A CA  1 
ATOM   1195 C  C   . TYR   A 1 164 ? 20.905  -8.538  58.186  1.00 57.95  ? 192 TYR   A C   1 
ATOM   1196 O  O   . TYR   A 1 164 ? 21.749  -8.147  59.000  1.00 60.70  ? 192 TYR   A O   1 
ATOM   1197 C  CB  . TYR   A 1 164 ? 18.946  -7.014  58.433  1.00 56.97  ? 192 TYR   A CB  1 
ATOM   1198 C  CG  . TYR   A 1 164 ? 17.478  -6.858  58.742  1.00 55.06  ? 192 TYR   A CG  1 
ATOM   1199 C  CD1 . TYR   A 1 164 ? 16.532  -6.926  57.734  1.00 54.56  ? 192 TYR   A CD1 1 
ATOM   1200 C  CD2 . TYR   A 1 164 ? 17.039  -6.652  60.045  1.00 54.61  ? 192 TYR   A CD2 1 
ATOM   1201 C  CE1 . TYR   A 1 164 ? 15.188  -6.792  58.006  1.00 56.69  ? 192 TYR   A CE1 1 
ATOM   1202 C  CE2 . TYR   A 1 164 ? 15.701  -6.512  60.329  1.00 53.22  ? 192 TYR   A CE2 1 
ATOM   1203 C  CZ  . TYR   A 1 164 ? 14.774  -6.589  59.303  1.00 59.77  ? 192 TYR   A CZ  1 
ATOM   1204 O  OH  . TYR   A 1 164 ? 13.424  -6.458  59.557  1.00 59.97  ? 192 TYR   A OH  1 
ATOM   1205 N  N   . LYS   A 1 165 ? 21.220  -9.035  56.988  1.00 59.30  ? 193 LYS   A N   1 
ATOM   1206 C  CA  . LYS   A 1 165 ? 22.577  -8.884  56.475  1.00 64.38  ? 193 LYS   A CA  1 
ATOM   1207 C  C   . LYS   A 1 165 ? 22.926  -7.404  56.341  1.00 62.69  ? 193 LYS   A C   1 
ATOM   1208 O  O   . LYS   A 1 165 ? 23.895  -6.918  56.938  1.00 65.20  ? 193 LYS   A O   1 
ATOM   1209 C  CB  . LYS   A 1 165 ? 22.716  -9.613  55.136  1.00 62.27  ? 193 LYS   A CB  1 
ATOM   1210 N  N   . ALA   A 1 166 ? 22.116  -6.662  55.589  1.00 62.90  ? 194 ALA   A N   1 
ATOM   1211 C  CA  . ALA   A 1 166 ? 22.281  -5.212  55.480  1.00 65.82  ? 194 ALA   A CA  1 
ATOM   1212 C  C   . ALA   A 1 166 ? 21.772  -4.510  56.738  1.00 66.21  ? 194 ALA   A C   1 
ATOM   1213 O  O   . ALA   A 1 166 ? 22.365  -4.627  57.814  1.00 68.32  ? 194 ALA   A O   1 
ATOM   1214 C  CB  . ALA   A 1 166 ? 21.553  -4.681  54.246  1.00 60.33  ? 194 ALA   A CB  1 
ATOM   1215 N  N   . GLU   A 1 173 ? 10.157  -2.752  52.926  1.00 69.46  ? 201 GLU   A N   1 
ATOM   1216 C  CA  . GLU   A 1 173 ? 11.500  -3.065  53.416  1.00 66.11  ? 201 GLU   A CA  1 
ATOM   1217 C  C   . GLU   A 1 173 ? 11.451  -3.528  54.869  1.00 62.82  ? 201 GLU   A C   1 
ATOM   1218 O  O   . GLU   A 1 173 ? 12.486  -3.786  55.480  1.00 62.45  ? 201 GLU   A O   1 
ATOM   1219 C  CB  . GLU   A 1 173 ? 12.429  -1.853  53.278  1.00 71.69  ? 201 GLU   A CB  1 
ATOM   1220 N  N   . PHE   A 1 174 ? 10.239  -3.585  55.425  1.00 63.58  ? 202 PHE   A N   1 
ATOM   1221 C  CA  . PHE   A 1 174 ? 9.989   -4.282  56.681  1.00 55.96  ? 202 PHE   A CA  1 
ATOM   1222 C  C   . PHE   A 1 174 ? 10.559  -5.684  56.575  1.00 53.60  ? 202 PHE   A C   1 
ATOM   1223 O  O   . PHE   A 1 174 ? 11.526  -6.030  57.260  1.00 55.77  ? 202 PHE   A O   1 
ATOM   1224 C  CB  . PHE   A 1 174 ? 8.483   -4.319  56.965  1.00 50.42  ? 202 PHE   A CB  1 
ATOM   1225 C  CG  . PHE   A 1 174 ? 8.081   -5.246  58.076  1.00 44.58  ? 202 PHE   A CG  1 
ATOM   1226 C  CD1 . PHE   A 1 174 ? 8.533   -5.046  59.368  1.00 44.54  ? 202 PHE   A CD1 1 
ATOM   1227 C  CD2 . PHE   A 1 174 ? 7.202   -6.297  57.830  1.00 44.52  ? 202 PHE   A CD2 1 
ATOM   1228 C  CE1 . PHE   A 1 174 ? 8.145   -5.891  60.386  1.00 39.75  ? 202 PHE   A CE1 1 
ATOM   1229 C  CE2 . PHE   A 1 174 ? 6.817   -7.145  58.841  1.00 41.59  ? 202 PHE   A CE2 1 
ATOM   1230 C  CZ  . PHE   A 1 174 ? 7.274   -6.945  60.119  1.00 41.01  ? 202 PHE   A CZ  1 
ATOM   1231 N  N   . LEU   A 1 175 ? 9.954   -6.485  55.707  1.00 52.39  ? 203 LEU   A N   1 
ATOM   1232 C  CA  . LEU   A 1 175 ? 10.396  -7.816  55.333  1.00 50.97  ? 203 LEU   A CA  1 
ATOM   1233 C  C   . LEU   A 1 175 ? 10.280  -7.933  53.823  1.00 53.01  ? 203 LEU   A C   1 
ATOM   1234 O  O   . LEU   A 1 175 ? 9.489   -7.213  53.201  1.00 52.13  ? 203 LEU   A O   1 
ATOM   1235 C  CB  . LEU   A 1 175 ? 9.549   -8.910  56.007  1.00 49.32  ? 203 LEU   A CB  1 
ATOM   1236 C  CG  . LEU   A 1 175 ? 9.597   -9.054  57.530  1.00 48.35  ? 203 LEU   A CG  1 
ATOM   1237 C  CD1 . LEU   A 1 175 ? 8.711   -10.212 57.985  1.00 47.01  ? 203 LEU   A CD1 1 
ATOM   1238 C  CD2 . LEU   A 1 175 ? 11.036  -9.239  58.022  1.00 50.52  ? 203 LEU   A CD2 1 
ATOM   1239 N  N   . PRO   A 1 176 ? 11.057  -8.826  53.200  1.00 53.57  ? 204 PRO   A N   1 
ATOM   1240 C  CA  . PRO   A 1 176 ? 10.862  -9.094  51.769  1.00 54.23  ? 204 PRO   A CA  1 
ATOM   1241 C  C   . PRO   A 1 176 ? 9.429   -9.503  51.476  1.00 53.58  ? 204 PRO   A C   1 
ATOM   1242 O  O   . PRO   A 1 176 ? 8.768   -10.164 52.281  1.00 51.79  ? 204 PRO   A O   1 
ATOM   1243 C  CB  . PRO   A 1 176 ? 11.833  -10.246 51.481  1.00 52.87  ? 204 PRO   A CB  1 
ATOM   1244 C  CG  . PRO   A 1 176 ? 12.874  -10.127 52.528  1.00 55.04  ? 204 PRO   A CG  1 
ATOM   1245 C  CD  . PRO   A 1 176 ? 12.176  -9.605  53.757  1.00 54.42  ? 204 PRO   A CD  1 
ATOM   1246 N  N   . GLY   A 1 177 ? 8.955   -9.124  50.292  1.00 54.65  ? 205 GLY   A N   1 
ATOM   1247 C  CA  . GLY   A 1 177 ? 7.596   -9.420  49.896  1.00 52.14  ? 205 GLY   A CA  1 
ATOM   1248 C  C   . GLY   A 1 177 ? 6.563   -8.448  50.408  1.00 49.85  ? 205 GLY   A C   1 
ATOM   1249 O  O   . GLY   A 1 177 ? 5.443   -8.421  49.882  1.00 48.88  ? 205 GLY   A O   1 
ATOM   1250 N  N   . PHE   A 1 178 ? 6.890   -7.648  51.419  1.00 48.10  ? 206 PHE   A N   1 
ATOM   1251 C  CA  . PHE   A 1 178 ? 6.007   -6.556  51.796  1.00 46.06  ? 206 PHE   A CA  1 
ATOM   1252 C  C   . PHE   A 1 178 ? 6.226   -5.385  50.848  1.00 48.26  ? 206 PHE   A C   1 
ATOM   1253 O  O   . PHE   A 1 178 ? 7.331   -5.165  50.343  1.00 51.10  ? 206 PHE   A O   1 
ATOM   1254 C  CB  . PHE   A 1 178 ? 6.254   -6.127  53.246  1.00 44.84  ? 206 PHE   A CB  1 
ATOM   1255 C  CG  . PHE   A 1 178 ? 5.604   -7.026  54.275  1.00 42.81  ? 206 PHE   A CG  1 
ATOM   1256 C  CD1 . PHE   A 1 178 ? 6.182   -8.240  54.629  1.00 40.12  ? 206 PHE   A CD1 1 
ATOM   1257 C  CD2 . PHE   A 1 178 ? 4.424   -6.641  54.900  1.00 41.49  ? 206 PHE   A CD2 1 
ATOM   1258 C  CE1 . PHE   A 1 178 ? 5.591   -9.054  55.582  1.00 42.65  ? 206 PHE   A CE1 1 
ATOM   1259 C  CE2 . PHE   A 1 178 ? 3.809   -7.462  55.849  1.00 40.89  ? 206 PHE   A CE2 1 
ATOM   1260 C  CZ  . PHE   A 1 178 ? 4.387   -8.668  56.190  1.00 40.70  ? 206 PHE   A CZ  1 
ATOM   1261 N  N   . GLU   A 1 179 ? 5.160   -4.641  50.593  1.00 47.04  ? 207 GLU   A N   1 
ATOM   1262 C  CA  . GLU   A 1 179 ? 5.246   -3.425  49.798  1.00 47.87  ? 207 GLU   A CA  1 
ATOM   1263 C  C   . GLU   A 1 179 ? 4.869   -2.230  50.655  1.00 49.65  ? 207 GLU   A C   1 
ATOM   1264 O  O   . GLU   A 1 179 ? 4.043   -2.335  51.563  1.00 45.69  ? 207 GLU   A O   1 
ATOM   1265 C  CB  . GLU   A 1 179 ? 4.357   -3.499  48.553  1.00 48.90  ? 207 GLU   A CB  1 
ATOM   1266 C  CG  . GLU   A 1 179 ? 4.602   -4.761  47.746  1.00 55.35  ? 207 GLU   A CG  1 
ATOM   1267 C  CD  . GLU   A 1 179 ? 3.929   -4.720  46.391  1.00 62.87  ? 207 GLU   A CD  1 
ATOM   1268 O  OE1 . GLU   A 1 179 ? 3.151   -3.771  46.146  1.00 63.16  ? 207 GLU   A OE1 1 
ATOM   1269 O  OE2 . GLU   A 1 179 ? 4.169   -5.641  45.584  1.00 64.77  ? 207 GLU   A OE2 1 
ATOM   1270 N  N   . ARG   A 1 180 ? 5.511   -1.098  50.371  1.00 55.09  ? 208 ARG   A N   1 
ATOM   1271 C  CA  . ARG   A 1 180 ? 5.148   0.159   51.007  1.00 56.39  ? 208 ARG   A CA  1 
ATOM   1272 C  C   . ARG   A 1 180 ? 3.745   0.564   50.572  1.00 55.59  ? 208 ARG   A C   1 
ATOM   1273 O  O   . ARG   A 1 180 ? 3.363   0.392   49.411  1.00 60.49  ? 208 ARG   A O   1 
ATOM   1274 C  CB  . ARG   A 1 180 ? 6.150   1.253   50.643  1.00 62.05  ? 208 ARG   A CB  1 
ATOM   1275 C  CG  . ARG   A 1 180 ? 7.570   0.988   51.119  1.00 68.28  ? 208 ARG   A CG  1 
ATOM   1276 C  CD  . ARG   A 1 180 ? 8.319   0.047   50.168  1.00 72.42  ? 208 ARG   A CD  1 
ATOM   1277 N  NE  . ARG   A 1 180 ? 9.751   0.315   50.117  1.00 77.21  ? 208 ARG   A NE  1 
ATOM   1278 C  CZ  . ARG   A 1 180 ? 10.289  1.371   49.514  1.00 80.56  ? 208 ARG   A CZ  1 
ATOM   1279 N  NH1 . ARG   A 1 180 ? 9.510   2.263   48.912  1.00 81.43  ? 208 ARG   A NH1 1 
ATOM   1280 N  NH2 . ARG   A 1 180 ? 11.606  1.537   49.513  1.00 83.73  ? 208 ARG   A NH2 1 
ATOM   1281 N  N   . VAL   A 1 181 ? 2.972   1.095   51.512  1.00 55.41  ? 209 VAL   A N   1 
ATOM   1282 C  CA  . VAL   A 1 181 ? 1.581   1.448   51.254  1.00 51.43  ? 209 VAL   A CA  1 
ATOM   1283 C  C   . VAL   A 1 181 ? 1.527   2.756   50.472  1.00 60.42  ? 209 VAL   A C   1 
ATOM   1284 O  O   . VAL   A 1 181 ? 2.311   3.678   50.721  1.00 56.98  ? 209 VAL   A O   1 
ATOM   1285 C  CB  . VAL   A 1 181 ? 0.805   1.535   52.582  1.00 52.47  ? 209 VAL   A CB  1 
ATOM   1286 C  CG1 . VAL   A 1 181 ? -0.468  2.368   52.435  1.00 55.05  ? 209 VAL   A CG1 1 
ATOM   1287 C  CG2 . VAL   A 1 181 ? 0.462   0.141   53.077  1.00 47.13  ? 209 VAL   A CG2 1 
ATOM   1288 N  N   . GLU   A 1 182 ? 0.598   2.830   49.513  1.00 61.16  ? 210 GLU   A N   1 
ATOM   1289 C  CA  . GLU   A 1 182 ? 0.458   3.988   48.636  1.00 65.64  ? 210 GLU   A CA  1 
ATOM   1290 C  C   . GLU   A 1 182 ? 0.217   5.266   49.435  1.00 66.26  ? 210 GLU   A C   1 
ATOM   1291 O  O   . GLU   A 1 182 ? -0.437  5.261   50.482  1.00 64.73  ? 210 GLU   A O   1 
ATOM   1292 C  CB  . GLU   A 1 182 ? -0.692  3.769   47.649  1.00 65.65  ? 210 GLU   A CB  1 
ATOM   1293 N  N   . ASP   A 1 183 ? 0.741   6.378   48.908  1.00 70.25  ? 211 ASP   A N   1 
ATOM   1294 C  CA  . ASP   A 1 183 ? 0.715   7.646   49.633  1.00 68.99  ? 211 ASP   A CA  1 
ATOM   1295 C  C   . ASP   A 1 183 ? -0.701  8.043   50.040  1.00 69.51  ? 211 ASP   A C   1 
ATOM   1296 O  O   . ASP   A 1 183 ? -0.928  8.482   51.174  1.00 70.85  ? 211 ASP   A O   1 
ATOM   1297 C  CB  . ASP   A 1 183 ? 1.354   8.743   48.779  1.00 74.28  ? 211 ASP   A CB  1 
ATOM   1298 N  N   . ALA   A 1 184 ? -1.669  7.884   49.135  1.00 69.75  ? 212 ALA   A N   1 
ATOM   1299 C  CA  . ALA   A 1 184 ? -3.039  8.293   49.435  1.00 72.17  ? 212 ALA   A CA  1 
ATOM   1300 C  C   . ALA   A 1 184 ? -3.663  7.426   50.525  1.00 71.45  ? 212 ALA   A C   1 
ATOM   1301 O  O   . ALA   A 1 184 ? -4.431  7.924   51.357  1.00 70.73  ? 212 ALA   A O   1 
ATOM   1302 C  CB  . ALA   A 1 184 ? -3.890  8.246   48.165  1.00 72.65  ? 212 ALA   A CB  1 
ATOM   1303 N  N   . SER   A 1 185 ? -3.356  6.126   50.532  1.00 70.05  ? 213 SER   A N   1 
ATOM   1304 C  CA  . SER   A 1 185 ? -3.912  5.179   51.492  1.00 66.95  ? 213 SER   A CA  1 
ATOM   1305 C  C   . SER   A 1 185 ? -3.121  5.131   52.792  1.00 66.73  ? 213 SER   A C   1 
ATOM   1306 O  O   . SER   A 1 185 ? -3.250  4.166   53.553  1.00 64.42  ? 213 SER   A O   1 
ATOM   1307 C  CB  . SER   A 1 185 ? -3.972  3.776   50.881  1.00 65.86  ? 213 SER   A CB  1 
ATOM   1308 O  OG  . SER   A 1 185 ? -4.780  3.737   49.718  1.00 73.05  ? 213 SER   A OG  1 
ATOM   1309 N  N   . SER   A 1 186 ? -2.284  6.130   53.049  1.00 67.36  ? 214 SER   A N   1 
ATOM   1310 C  CA  . SER   A 1 186 ? -1.432  6.145   54.235  1.00 61.35  ? 214 SER   A CA  1 
ATOM   1311 C  C   . SER   A 1 186 ? -1.476  7.546   54.825  1.00 60.66  ? 214 SER   A C   1 
ATOM   1312 O  O   . SER   A 1 186 ? -0.908  8.480   54.249  1.00 65.53  ? 214 SER   A O   1 
ATOM   1313 C  CB  . SER   A 1 186 ? 0.000   5.726   53.894  1.00 62.74  ? 214 SER   A CB  1 
ATOM   1314 O  OG  . SER   A 1 186 ? 0.432   6.321   52.681  1.00 69.08  ? 214 SER   A OG  1 
ATOM   1315 N  N   . PHE   A 1 187 ? -2.146  7.692   55.982  1.00 55.58  ? 215 PHE   A N   1 
ATOM   1316 C  CA  . PHE   A 1 187 ? -2.352  9.016   56.563  1.00 54.60  ? 215 PHE   A CA  1 
ATOM   1317 C  C   . PHE   A 1 187 ? -1.423  9.230   57.751  1.00 49.76  ? 215 PHE   A C   1 
ATOM   1318 O  O   . PHE   A 1 187 ? -1.319  8.345   58.615  1.00 43.18  ? 215 PHE   A O   1 
ATOM   1319 C  CB  . PHE   A 1 187 ? -3.795  9.184   57.013  1.00 49.72  ? 215 PHE   A CB  1 
ATOM   1320 C  CG  . PHE   A 1 187 ? -4.173  10.608  57.261  1.00 51.79  ? 215 PHE   A CG  1 
ATOM   1321 C  CD1 . PHE   A 1 187 ? -3.905  11.210  58.482  1.00 47.65  ? 215 PHE   A CD1 1 
ATOM   1322 C  CD2 . PHE   A 1 187 ? -4.801  11.347  56.270  1.00 49.68  ? 215 PHE   A CD2 1 
ATOM   1323 C  CE1 . PHE   A 1 187 ? -4.255  12.525  58.712  1.00 47.32  ? 215 PHE   A CE1 1 
ATOM   1324 C  CE2 . PHE   A 1 187 ? -5.146  12.663  56.495  1.00 51.06  ? 215 PHE   A CE2 1 
ATOM   1325 C  CZ  . PHE   A 1 187 ? -4.871  13.251  57.717  1.00 49.75  ? 215 PHE   A CZ  1 
ATOM   1326 N  N   . PRO   A 1 188 ? -0.741  10.403  57.842  1.00 50.44  ? 216 PRO   A N   1 
ATOM   1327 C  CA  . PRO   A 1 188 ? 0.365   10.600  58.796  1.00 49.91  ? 216 PRO   A CA  1 
ATOM   1328 C  C   . PRO   A 1 188 ? -0.058  10.770  60.260  1.00 50.46  ? 216 PRO   A C   1 
ATOM   1329 O  O   . PRO   A 1 188 ? 0.382   11.693  60.947  1.00 44.93  ? 216 PRO   A O   1 
ATOM   1330 C  CB  . PRO   A 1 188 ? 1.054   11.868  58.274  1.00 51.73  ? 216 PRO   A CB  1 
ATOM   1331 C  CG  . PRO   A 1 188 ? 0.325   12.327  57.043  1.00 49.89  ? 216 PRO   A CG  1 
ATOM   1332 C  CD  . PRO   A 1 188 ? -0.673  11.297  56.651  1.00 50.15  ? 216 PRO   A CD  1 
ATOM   1333 N  N   . LEU   A 1 189 ? -0.907  9.857   60.744  1.00 45.61  ? 217 LEU   A N   1 
ATOM   1334 C  CA  . LEU   A 1 189 ? -1.320  9.912   62.140  1.00 43.20  ? 217 LEU   A CA  1 
ATOM   1335 C  C   . LEU   A 1 189 ? -0.115  9.769   63.066  1.00 44.84  ? 217 LEU   A C   1 
ATOM   1336 O  O   . LEU   A 1 189 ? 0.836   9.038   62.779  1.00 48.02  ? 217 LEU   A O   1 
ATOM   1337 C  CB  . LEU   A 1 189 ? -2.347  8.819   62.453  1.00 40.57  ? 217 LEU   A CB  1 
ATOM   1338 C  CG  . LEU   A 1 189 ? -3.714  8.910   61.802  1.00 38.05  ? 217 LEU   A CG  1 
ATOM   1339 C  CD1 . LEU   A 1 189 ? -4.521  7.619   62.100  1.00 38.85  ? 217 LEU   A CD1 1 
ATOM   1340 C  CD2 . LEU   A 1 189 ? -4.478  10.168  62.267  1.00 37.03  ? 217 LEU   A CD2 1 
ATOM   1341 N  N   . ASP   A 1 190 ? -0.148  10.490  64.188  1.00 41.95  ? 218 ASP   A N   1 
ATOM   1342 C  CA  . ASP   A 1 190 ? 0.908   10.351  65.191  1.00 42.67  ? 218 ASP   A CA  1 
ATOM   1343 C  C   . ASP   A 1 190 ? 0.419   10.962  66.491  1.00 44.54  ? 218 ASP   A C   1 
ATOM   1344 O  O   . ASP   A 1 190 ? 0.184   12.174  66.543  1.00 41.55  ? 218 ASP   A O   1 
ATOM   1345 C  CB  . ASP   A 1 190 ? 2.201   11.043  64.718  1.00 44.21  ? 218 ASP   A CB  1 
ATOM   1346 C  CG  . ASP   A 1 190 ? 3.277   11.050  65.779  1.00 46.16  ? 218 ASP   A CG  1 
ATOM   1347 O  OD1 . ASP   A 1 190 ? 3.264   10.175  66.665  1.00 44.48  ? 218 ASP   A OD1 1 
ATOM   1348 O  OD2 . ASP   A 1 190 ? 4.153   11.941  65.715  1.00 51.97  ? 218 ASP   A OD2 1 
ATOM   1349 N  N   . TYR   A 1 191 ? 0.283   10.155  67.547  1.00 39.41  ? 219 TYR   A N   1 
ATOM   1350 C  CA  . TYR   A 1 191 ? -0.109  10.716  68.837  1.00 43.61  ? 219 TYR   A CA  1 
ATOM   1351 C  C   . TYR   A 1 191 ? 1.041   10.737  69.833  1.00 40.80  ? 219 TYR   A C   1 
ATOM   1352 O  O   . TYR   A 1 191 ? 0.801   10.938  71.026  1.00 41.73  ? 219 TYR   A O   1 
ATOM   1353 C  CB  . TYR   A 1 191 ? -1.305  9.978   69.452  1.00 35.23  ? 219 TYR   A CB  1 
ATOM   1354 C  CG  . TYR   A 1 191 ? -2.490  9.729   68.526  1.00 37.50  ? 219 TYR   A CG  1 
ATOM   1355 C  CD1 . TYR   A 1 191 ? -2.727  10.531  67.407  1.00 38.30  ? 219 TYR   A CD1 1 
ATOM   1356 C  CD2 . TYR   A 1 191 ? -3.373  8.689   68.780  1.00 34.98  ? 219 TYR   A CD2 1 
ATOM   1357 C  CE1 . TYR   A 1 191 ? -3.785  10.293  66.563  1.00 36.23  ? 219 TYR   A CE1 1 
ATOM   1358 C  CE2 . TYR   A 1 191 ? -4.449  8.443   67.947  1.00 35.03  ? 219 TYR   A CE2 1 
ATOM   1359 C  CZ  . TYR   A 1 191 ? -4.645  9.233   66.833  1.00 33.33  ? 219 TYR   A CZ  1 
ATOM   1360 O  OH  . TYR   A 1 191 ? -5.692  8.972   65.996  1.00 35.69  ? 219 TYR   A OH  1 
ATOM   1361 N  N   . GLY   A 1 192 ? 2.279   10.530  69.379  1.00 38.03  ? 220 GLY   A N   1 
ATOM   1362 C  CA  . GLY   A 1 192 ? 3.436   10.584  70.244  1.00 40.71  ? 220 GLY   A CA  1 
ATOM   1363 C  C   . GLY   A 1 192 ? 3.997   9.242   70.650  1.00 41.71  ? 220 GLY   A C   1 
ATOM   1364 O  O   . GLY   A 1 192 ? 5.007   9.201   71.359  1.00 35.88  ? 220 GLY   A O   1 
ATOM   1365 N  N   . ILE   A 1 193 ? 3.371   8.137   70.244  1.00 34.27  ? 221 ILE   A N   1 
ATOM   1366 C  CA  . ILE   A 1 193 ? 3.932   6.837   70.581  1.00 33.42  ? 221 ILE   A CA  1 
ATOM   1367 C  C   . ILE   A 1 193 ? 5.175   6.589   69.737  1.00 33.34  ? 221 ILE   A C   1 
ATOM   1368 O  O   . ILE   A 1 193 ? 5.187   6.857   68.528  1.00 36.43  ? 221 ILE   A O   1 
ATOM   1369 C  CB  . ILE   A 1 193 ? 2.878   5.736   70.387  1.00 33.12  ? 221 ILE   A CB  1 
ATOM   1370 C  CG1 . ILE   A 1 193 ? 1.714   6.000   71.332  1.00 31.22  ? 221 ILE   A CG1 1 
ATOM   1371 C  CG2 . ILE   A 1 193 ? 3.501   4.384   70.710  1.00 34.91  ? 221 ILE   A CG2 1 
ATOM   1372 C  CD1 . ILE   A 1 193 ? 0.521   5.038   71.198  1.00 31.43  ? 221 ILE   A CD1 1 
ATOM   1373 N  N   . ARG   A 1 194 ? 6.232   6.068   70.365  1.00 37.41  ? 222 ARG   A N   1 
ATOM   1374 C  CA  . ARG   A 1 194 ? 7.535   6.017   69.709  1.00 34.25  ? 222 ARG   A CA  1 
ATOM   1375 C  C   . ARG   A 1 194 ? 8.192   4.633   69.685  1.00 38.31  ? 222 ARG   A C   1 
ATOM   1376 O  O   . ARG   A 1 194 ? 8.909   4.308   68.730  1.00 39.81  ? 222 ARG   A O   1 
ATOM   1377 C  CB  . ARG   A 1 194 ? 8.479   7.037   70.360  1.00 41.32  ? 222 ARG   A CB  1 
ATOM   1378 C  CG  . ARG   A 1 194 ? 8.160   8.506   70.017  1.00 36.24  ? 222 ARG   A CG  1 
ATOM   1379 C  CD  . ARG   A 1 194 ? 8.426   8.801   68.536  1.00 39.40  ? 222 ARG   A CD  1 
ATOM   1380 N  NE  . ARG   A 1 194 ? 7.951   10.122  68.103  1.00 41.03  ? 222 ARG   A NE  1 
ATOM   1381 C  CZ  . ARG   A 1 194 ? 6.710   10.398  67.721  1.00 39.53  ? 222 ARG   A CZ  1 
ATOM   1382 N  NH1 . ARG   A 1 194 ? 5.783   9.439   67.715  1.00 41.33  ? 222 ARG   A NH1 1 
ATOM   1383 N  NH2 . ARG   A 1 194 ? 6.387   11.635  67.335  1.00 42.67  ? 222 ARG   A NH2 1 
ATOM   1384 N  N   . ARG   A 1 195 ? 8.003   3.812   70.717  1.00 38.39  ? 223 ARG   A N   1 
ATOM   1385 C  CA  . ARG   A 1 195 ? 8.656   2.506   70.695  1.00 36.32  ? 223 ARG   A CA  1 
ATOM   1386 C  C   . ARG   A 1 195 ? 8.021   1.584   71.724  1.00 37.19  ? 223 ARG   A C   1 
ATOM   1387 O  O   . ARG   A 1 195 ? 7.346   2.026   72.657  1.00 36.44  ? 223 ARG   A O   1 
ATOM   1388 C  CB  . ARG   A 1 195 ? 10.163  2.614   70.976  1.00 40.06  ? 223 ARG   A CB  1 
ATOM   1389 C  CG  . ARG   A 1 195 ? 10.495  2.929   72.421  1.00 40.07  ? 223 ARG   A CG  1 
ATOM   1390 C  CD  . ARG   A 1 195 ? 12.020  2.894   72.662  1.00 44.03  ? 223 ARG   A CD  1 
ATOM   1391 N  NE  . ARG   A 1 195 ? 12.391  3.106   74.060  1.00 48.67  ? 223 ARG   A NE  1 
ATOM   1392 C  CZ  . ARG   A 1 195 ? 12.589  2.130   74.950  1.00 51.08  ? 223 ARG   A CZ  1 
ATOM   1393 N  NH1 . ARG   A 1 195 ? 12.432  0.854   74.603  1.00 48.14  ? 223 ARG   A NH1 1 
ATOM   1394 N  NH2 . ARG   A 1 195 ? 12.948  2.429   76.198  1.00 48.58  ? 223 ARG   A NH2 1 
ATOM   1395 N  N   . LEU   A 1 196 ? 8.284   0.292   71.558  1.00 32.47  ? 224 LEU   A N   1 
ATOM   1396 C  CA  . LEU   A 1 196 ? 7.819   -0.701  72.518  1.00 35.48  ? 224 LEU   A CA  1 
ATOM   1397 C  C   . LEU   A 1 196 ? 8.778   -0.752  73.699  1.00 39.40  ? 224 LEU   A C   1 
ATOM   1398 O  O   . LEU   A 1 196 ? 9.988   -0.929  73.519  1.00 37.98  ? 224 LEU   A O   1 
ATOM   1399 C  CB  . LEU   A 1 196 ? 7.735   -2.084  71.867  1.00 33.91  ? 224 LEU   A CB  1 
ATOM   1400 C  CG  . LEU   A 1 196 ? 7.172   -3.205  72.744  1.00 36.11  ? 224 LEU   A CG  1 
ATOM   1401 C  CD1 . LEU   A 1 196 ? 5.691   -2.965  73.056  1.00 36.81  ? 224 LEU   A CD1 1 
ATOM   1402 C  CD2 . LEU   A 1 196 ? 7.350   -4.558  72.057  1.00 35.72  ? 224 LEU   A CD2 1 
ATOM   1403 N  N   . ASP   A 1 197 ? 8.239   -0.640  74.910  1.00 41.03  ? 225 ASP   A N   1 
ATOM   1404 C  CA  . ASP   A 1 197 ? 9.090   -0.619  76.096  1.00 40.35  ? 225 ASP   A CA  1 
ATOM   1405 C  C   . ASP   A 1 197 ? 9.195   -1.982  76.765  1.00 38.89  ? 225 ASP   A C   1 
ATOM   1406 O  O   . ASP   A 1 197 ? 10.305  -2.409  77.111  1.00 38.39  ? 225 ASP   A O   1 
ATOM   1407 C  CB  . ASP   A 1 197 ? 8.583   0.420   77.100  1.00 39.99  ? 225 ASP   A CB  1 
ATOM   1408 C  CG  . ASP   A 1 197 ? 9.444   0.497   78.345  1.00 41.57  ? 225 ASP   A CG  1 
ATOM   1409 O  OD1 . ASP   A 1 197 ? 10.363  1.346   78.369  1.00 44.78  ? 225 ASP   A OD1 1 
ATOM   1410 O  OD2 . ASP   A 1 197 ? 9.197   -0.278  79.299  1.00 40.34  ? 225 ASP   A OD2 1 
ATOM   1411 N  N   . HIS   A 1 198 ? 8.071   -2.676  76.960  1.00 35.95  ? 226 HIS   A N   1 
ATOM   1412 C  CA  . HIS   A 1 198 ? 8.113   -4.049  77.453  1.00 37.56  ? 226 HIS   A CA  1 
ATOM   1413 C  C   . HIS   A 1 198 ? 6.875   -4.815  76.985  1.00 35.69  ? 226 HIS   A C   1 
ATOM   1414 O  O   . HIS   A 1 198 ? 5.875   -4.223  76.572  1.00 35.27  ? 226 HIS   A O   1 
ATOM   1415 C  CB  . HIS   A 1 198 ? 8.263   -4.117  78.987  1.00 38.44  ? 226 HIS   A CB  1 
ATOM   1416 C  CG  . HIS   A 1 198 ? 7.241   -3.349  79.770  1.00 36.16  ? 226 HIS   A CG  1 
ATOM   1417 N  ND1 . HIS   A 1 198 ? 7.427   -2.036  80.149  1.00 41.11  ? 226 HIS   A ND1 1 
ATOM   1418 C  CD2 . HIS   A 1 198 ? 6.053   -3.727  80.305  1.00 38.90  ? 226 HIS   A CD2 1 
ATOM   1419 C  CE1 . HIS   A 1 198 ? 6.392   -1.631  80.865  1.00 37.43  ? 226 HIS   A CE1 1 
ATOM   1420 N  NE2 . HIS   A 1 198 ? 5.536   -2.633  80.962  1.00 41.65  ? 226 HIS   A NE2 1 
ATOM   1421 N  N   . ALA   A 1 199 ? 6.976   -6.146  77.027  1.00 34.83  ? 227 ALA   A N   1 
ATOM   1422 C  CA  . ALA   A 1 199 ? 5.893   -7.060  76.638  1.00 37.31  ? 227 ALA   A CA  1 
ATOM   1423 C  C   . ALA   A 1 199 ? 5.749   -8.124  77.714  1.00 37.58  ? 227 ALA   A C   1 
ATOM   1424 O  O   . ALA   A 1 199 ? 6.718   -8.813  78.034  1.00 38.72  ? 227 ALA   A O   1 
ATOM   1425 C  CB  . ALA   A 1 199 ? 6.173   -7.722  75.287  1.00 35.92  ? 227 ALA   A CB  1 
ATOM   1426 N  N   . VAL   A 1 200 ? 4.542   -8.279  78.251  1.00 38.24  ? 228 VAL   A N   1 
ATOM   1427 C  CA  . VAL   A 1 200 ? 4.321   -9.021  79.488  1.00 38.68  ? 228 VAL   A CA  1 
ATOM   1428 C  C   . VAL   A 1 200 ? 3.506   -10.276 79.204  1.00 40.12  ? 228 VAL   A C   1 
ATOM   1429 O  O   . VAL   A 1 200 ? 2.486   -10.223 78.501  1.00 40.69  ? 228 VAL   A O   1 
ATOM   1430 C  CB  . VAL   A 1 200 ? 3.621   -8.132  80.526  1.00 41.90  ? 228 VAL   A CB  1 
ATOM   1431 C  CG1 . VAL   A 1 200 ? 3.414   -8.895  81.823  1.00 42.11  ? 228 VAL   A CG1 1 
ATOM   1432 C  CG2 . VAL   A 1 200 ? 4.449   -6.837  80.739  1.00 36.85  ? 228 VAL   A CG2 1 
ATOM   1433 N  N   . GLY   A 1 201 ? 3.939   -11.398 79.769  1.00 40.04  ? 229 GLY   A N   1 
ATOM   1434 C  CA  . GLY   A 1 201 ? 3.220   -12.652 79.662  1.00 42.33  ? 229 GLY   A CA  1 
ATOM   1435 C  C   . GLY   A 1 201 ? 2.564   -13.013 80.982  1.00 44.21  ? 229 GLY   A C   1 
ATOM   1436 O  O   . GLY   A 1 201 ? 3.069   -12.676 82.054  1.00 45.42  ? 229 GLY   A O   1 
ATOM   1437 N  N   . ASN   A 1 202 ? 1.413   -13.664 80.897  1.00 40.59  ? 230 ASN   A N   1 
ATOM   1438 C  CA  . ASN   A 1 202 ? 0.731   -14.233 82.047  1.00 40.85  ? 230 ASN   A CA  1 
ATOM   1439 C  C   . ASN   A 1 202 ? 0.843   -15.742 81.940  1.00 44.28  ? 230 ASN   A C   1 
ATOM   1440 O  O   . ASN   A 1 202 ? 0.531   -16.311 80.889  1.00 44.23  ? 230 ASN   A O   1 
ATOM   1441 C  CB  . ASN   A 1 202 ? -0.749  -13.837 82.090  1.00 41.93  ? 230 ASN   A CB  1 
ATOM   1442 C  CG  . ASN   A 1 202 ? -0.974  -12.449 82.638  1.00 46.88  ? 230 ASN   A CG  1 
ATOM   1443 O  OD1 . ASN   A 1 202 ? -0.039  -11.785 83.089  1.00 42.86  ? 230 ASN   A OD1 1 
ATOM   1444 N  ND2 . ASN   A 1 202 ? -2.242  -12.002 82.612  1.00 44.68  ? 230 ASN   A ND2 1 
ATOM   1445 N  N   . VAL   A 1 203 ? 1.291   -16.387 83.012  1.00 43.47  ? 231 VAL   A N   1 
ATOM   1446 C  CA  . VAL   A 1 203 ? 1.409   -17.843 83.025  1.00 47.31  ? 231 VAL   A CA  1 
ATOM   1447 C  C   . VAL   A 1 203 ? 0.836   -18.368 84.330  1.00 50.94  ? 231 VAL   A C   1 
ATOM   1448 O  O   . VAL   A 1 203 ? 0.717   -17.628 85.317  1.00 48.70  ? 231 VAL   A O   1 
ATOM   1449 C  CB  . VAL   A 1 203 ? 2.872   -18.307 82.860  1.00 46.07  ? 231 VAL   A CB  1 
ATOM   1450 C  CG1 . VAL   A 1 203 ? 3.479   -17.735 81.581  1.00 46.25  ? 231 VAL   A CG1 1 
ATOM   1451 C  CG2 . VAL   A 1 203 ? 3.706   -17.902 84.074  1.00 44.53  ? 231 VAL   A CG2 1 
ATOM   1452 N  N   . PRO   A 1 204 ? 0.439   -19.648 84.352  1.00 51.29  ? 232 PRO   A N   1 
ATOM   1453 C  CA  . PRO   A 1 204 ? -0.057  -20.225 85.610  1.00 51.18  ? 232 PRO   A CA  1 
ATOM   1454 C  C   . PRO   A 1 204 ? 1.010   -20.328 86.687  1.00 52.51  ? 232 PRO   A C   1 
ATOM   1455 O  O   . PRO   A 1 204 ? 0.683   -20.132 87.865  1.00 50.96  ? 232 PRO   A O   1 
ATOM   1456 C  CB  . PRO   A 1 204 ? -0.585  -21.609 85.191  1.00 54.51  ? 232 PRO   A CB  1 
ATOM   1457 C  CG  . PRO   A 1 204 ? 0.017   -21.881 83.850  1.00 54.89  ? 232 PRO   A CG  1 
ATOM   1458 C  CD  . PRO   A 1 204 ? 0.199   -20.538 83.202  1.00 46.71  ? 232 PRO   A CD  1 
ATOM   1459 N  N   . GLU   A 1 205 ? 2.269   -20.610 86.324  1.00 51.19  ? 233 GLU   A N   1 
ATOM   1460 C  CA  . GLU   A 1 205 ? 3.359   -20.770 87.285  1.00 51.51  ? 233 GLU   A CA  1 
ATOM   1461 C  C   . GLU   A 1 205 ? 4.576   -20.000 86.801  1.00 47.24  ? 233 GLU   A C   1 
ATOM   1462 O  O   . GLU   A 1 205 ? 5.130   -20.318 85.744  1.00 45.15  ? 233 GLU   A O   1 
ATOM   1463 C  CB  . GLU   A 1 205 ? 3.736   -22.244 87.469  1.00 54.84  ? 233 GLU   A CB  1 
ATOM   1464 C  CG  . GLU   A 1 205 ? 2.601   -23.192 87.760  1.00 55.40  ? 233 GLU   A CG  1 
ATOM   1465 C  CD  . GLU   A 1 205 ? 3.127   -24.585 88.059  1.00 66.33  ? 233 GLU   A CD  1 
ATOM   1466 O  OE1 . GLU   A 1 205 ? 3.335   -24.894 89.253  1.00 70.39  ? 233 GLU   A OE1 1 
ATOM   1467 O  OE2 . GLU   A 1 205 ? 3.364   -25.355 87.101  1.00 70.70  ? 233 GLU   A OE2 1 
ATOM   1468 N  N   . LEU   A 1 206 ? 5.015   -19.018 87.591  1.00 49.80  ? 234 LEU   A N   1 
ATOM   1469 C  CA  . LEU   A 1 206 ? 6.090   -18.130 87.158  1.00 48.84  ? 234 LEU   A CA  1 
ATOM   1470 C  C   . LEU   A 1 206 ? 7.434   -18.849 87.115  1.00 49.99  ? 234 LEU   A C   1 
ATOM   1471 O  O   . LEU   A 1 206 ? 8.236   -18.623 86.200  1.00 48.68  ? 234 LEU   A O   1 
ATOM   1472 C  CB  . LEU   A 1 206 ? 6.157   -16.917 88.091  1.00 51.75  ? 234 LEU   A CB  1 
ATOM   1473 C  CG  . LEU   A 1 206 ? 7.292   -15.892 87.998  1.00 52.01  ? 234 LEU   A CG  1 
ATOM   1474 C  CD1 . LEU   A 1 206 ? 7.255   -15.126 86.686  1.00 52.02  ? 234 LEU   A CD1 1 
ATOM   1475 C  CD2 . LEU   A 1 206 ? 7.207   -14.935 89.173  1.00 51.29  ? 234 LEU   A CD2 1 
ATOM   1476 N  N   . GLY   A 1 207 ? 7.696   -19.714 88.094  1.00 48.41  ? 235 GLY   A N   1 
ATOM   1477 C  CA  . GLY   A 1 207 ? 8.981   -20.365 88.236  1.00 47.28  ? 235 GLY   A CA  1 
ATOM   1478 C  C   . GLY   A 1 207 ? 9.443   -21.099 86.991  1.00 47.75  ? 235 GLY   A C   1 
ATOM   1479 O  O   . GLY   A 1 207 ? 10.483  -20.777 86.403  1.00 51.23  ? 235 GLY   A O   1 
ATOM   1480 N  N   . PRO   A 1 208 ? 8.677   -22.107 86.566  1.00 47.05  ? 236 PRO   A N   1 
ATOM   1481 C  CA  . PRO   A 1 208 ? 9.054   -22.838 85.344  1.00 45.29  ? 236 PRO   A CA  1 
ATOM   1482 C  C   . PRO   A 1 208 ? 9.124   -21.950 84.112  1.00 48.10  ? 236 PRO   A C   1 
ATOM   1483 O  O   . PRO   A 1 208 ? 9.961   -22.179 83.230  1.00 44.73  ? 236 PRO   A O   1 
ATOM   1484 C  CB  . PRO   A 1 208 ? 7.949   -23.893 85.222  1.00 50.12  ? 236 PRO   A CB  1 
ATOM   1485 C  CG  . PRO   A 1 208 ? 7.385   -24.023 86.605  1.00 52.06  ? 236 PRO   A CG  1 
ATOM   1486 C  CD  . PRO   A 1 208 ? 7.464   -22.656 87.191  1.00 47.30  ? 236 PRO   A CD  1 
ATOM   1487 N  N   . ALA   A 1 209 ? 8.257   -20.937 84.016  1.00 46.59  ? 237 ALA   A N   1 
ATOM   1488 C  CA  . ALA   A 1 209 ? 8.295   -20.063 82.850  1.00 45.92  ? 237 ALA   A CA  1 
ATOM   1489 C  C   . ALA   A 1 209 ? 9.565   -19.227 82.831  1.00 43.18  ? 237 ALA   A C   1 
ATOM   1490 O  O   . ALA   A 1 209 ? 10.216  -19.096 81.787  1.00 47.41  ? 237 ALA   A O   1 
ATOM   1491 C  CB  . ALA   A 1 209 ? 7.057   -19.161 82.823  1.00 45.22  ? 237 ALA   A CB  1 
ATOM   1492 N  N   . LEU   A 1 210 ? 9.930   -18.643 83.972  1.00 44.30  ? 238 LEU   A N   1 
ATOM   1493 C  CA  . LEU   A 1 210 ? 11.175  -17.886 84.048  1.00 48.73  ? 238 LEU   A CA  1 
ATOM   1494 C  C   . LEU   A 1 210 ? 12.374  -18.769 83.727  1.00 49.64  ? 238 LEU   A C   1 
ATOM   1495 O  O   . LEU   A 1 210 ? 13.246  -18.392 82.934  1.00 46.43  ? 238 LEU   A O   1 
ATOM   1496 C  CB  . LEU   A 1 210 ? 11.348  -17.289 85.439  1.00 51.78  ? 238 LEU   A CB  1 
ATOM   1497 C  CG  . LEU   A 1 210 ? 10.817  -15.940 85.884  1.00 52.76  ? 238 LEU   A CG  1 
ATOM   1498 C  CD1 . LEU   A 1 210 ? 11.514  -15.636 87.203  1.00 52.86  ? 238 LEU   A CD1 1 
ATOM   1499 C  CD2 . LEU   A 1 210 ? 11.096  -14.846 84.859  1.00 53.89  ? 238 LEU   A CD2 1 
ATOM   1500 N  N   . THR   A 1 211 ? 12.446  -19.941 84.366  1.00 48.44  ? 239 THR   A N   1 
ATOM   1501 C  CA  . THR   A 1 211 ? 13.588  -20.835 84.170  1.00 51.06  ? 239 THR   A CA  1 
ATOM   1502 C  C   . THR   A 1 211 ? 13.749  -21.199 82.701  1.00 50.48  ? 239 THR   A C   1 
ATOM   1503 O  O   . THR   A 1 211 ? 14.871  -21.229 82.179  1.00 48.61  ? 239 THR   A O   1 
ATOM   1504 C  CB  . THR   A 1 211 ? 13.412  -22.101 85.012  1.00 51.56  ? 239 THR   A CB  1 
ATOM   1505 O  OG1 . THR   A 1 211 ? 13.194  -21.745 86.384  1.00 53.03  ? 239 THR   A OG1 1 
ATOM   1506 C  CG2 . THR   A 1 211 ? 14.636  -23.002 84.900  1.00 51.38  ? 239 THR   A CG2 1 
ATOM   1507 N  N   . TYR   A 1 212 ? 12.630  -21.446 82.011  1.00 47.51  ? 240 TYR   A N   1 
ATOM   1508 C  CA  . TYR   A 1 212 ? 12.681  -21.789 80.595  1.00 45.00  ? 240 TYR   A CA  1 
ATOM   1509 C  C   . TYR   A 1 212 ? 13.203  -20.622 79.760  1.00 46.18  ? 240 TYR   A C   1 
ATOM   1510 O  O   . TYR   A 1 212 ? 14.121  -20.788 78.947  1.00 41.93  ? 240 TYR   A O   1 
ATOM   1511 C  CB  . TYR   A 1 212 ? 11.292  -22.231 80.120  1.00 44.73  ? 240 TYR   A CB  1 
ATOM   1512 C  CG  . TYR   A 1 212 ? 11.141  -22.299 78.618  1.00 45.51  ? 240 TYR   A CG  1 
ATOM   1513 C  CD1 . TYR   A 1 212 ? 11.585  -23.406 77.904  1.00 45.68  ? 240 TYR   A CD1 1 
ATOM   1514 C  CD2 . TYR   A 1 212 ? 10.517  -21.265 77.912  1.00 45.22  ? 240 TYR   A CD2 1 
ATOM   1515 C  CE1 . TYR   A 1 212 ? 11.448  -23.476 76.527  1.00 43.28  ? 240 TYR   A CE1 1 
ATOM   1516 C  CE2 . TYR   A 1 212 ? 10.368  -21.327 76.536  1.00 42.70  ? 240 TYR   A CE2 1 
ATOM   1517 C  CZ  . TYR   A 1 212 ? 10.835  -22.432 75.845  1.00 43.69  ? 240 TYR   A CZ  1 
ATOM   1518 O  OH  . TYR   A 1 212 ? 10.696  -22.502 74.476  1.00 37.49  ? 240 TYR   A OH  1 
ATOM   1519 N  N   . VAL   A 1 213 ? 12.640  -19.425 79.952  1.00 43.34  ? 241 VAL   A N   1 
ATOM   1520 C  CA  . VAL   A 1 213 ? 13.007  -18.303 79.094  1.00 43.65  ? 241 VAL   A CA  1 
ATOM   1521 C  C   . VAL   A 1 213 ? 14.396  -17.781 79.449  1.00 43.21  ? 241 VAL   A C   1 
ATOM   1522 O  O   . VAL   A 1 213 ? 15.224  -17.520 78.566  1.00 42.11  ? 241 VAL   A O   1 
ATOM   1523 C  CB  . VAL   A 1 213 ? 11.952  -17.183 79.183  1.00 45.05  ? 241 VAL   A CB  1 
ATOM   1524 C  CG1 . VAL   A 1 213 ? 12.392  -16.000 78.332  1.00 42.95  ? 241 VAL   A CG1 1 
ATOM   1525 C  CG2 . VAL   A 1 213 ? 10.604  -17.702 78.745  1.00 43.17  ? 241 VAL   A CG2 1 
ATOM   1526 N  N   . ALA   A 1 214 ? 14.657  -17.568 80.742  1.00 44.93  ? 242 ALA   A N   1 
ATOM   1527 C  CA  . ALA   A 1 214 ? 16.015  -17.206 81.149  1.00 46.50  ? 242 ALA   A CA  1 
ATOM   1528 C  C   . ALA   A 1 214 ? 17.017  -18.254 80.692  1.00 45.23  ? 242 ALA   A C   1 
ATOM   1529 O  O   . ALA   A 1 214 ? 18.178  -17.930 80.410  1.00 47.14  ? 242 ALA   A O   1 
ATOM   1530 C  CB  . ALA   A 1 214 ? 16.096  -17.036 82.666  1.00 46.77  ? 242 ALA   A CB  1 
ATOM   1531 N  N   . GLY   A 1 215 ? 16.570  -19.505 80.575  1.00 48.79  ? 243 GLY   A N   1 
ATOM   1532 C  CA  . GLY   A 1 215 ? 17.486  -20.587 80.259  1.00 53.48  ? 243 GLY   A CA  1 
ATOM   1533 C  C   . GLY   A 1 215 ? 18.037  -20.526 78.847  1.00 51.33  ? 243 GLY   A C   1 
ATOM   1534 O  O   . GLY   A 1 215 ? 19.227  -20.781 78.634  1.00 46.69  ? 243 GLY   A O   1 
ATOM   1535 N  N   . PHE   A 1 216 ? 17.187  -20.209 77.860  1.00 43.78  ? 244 PHE   A N   1 
ATOM   1536 C  CA  . PHE   A 1 216 ? 17.637  -20.240 76.473  1.00 40.96  ? 244 PHE   A CA  1 
ATOM   1537 C  C   . PHE   A 1 216 ? 18.111  -18.883 75.953  1.00 43.42  ? 244 PHE   A C   1 
ATOM   1538 O  O   . PHE   A 1 216 ? 18.814  -18.841 74.934  1.00 44.47  ? 244 PHE   A O   1 
ATOM   1539 C  CB  . PHE   A 1 216 ? 16.543  -20.862 75.561  1.00 41.50  ? 244 PHE   A CB  1 
ATOM   1540 C  CG  . PHE   A 1 216 ? 15.356  -19.952 75.223  1.00 43.99  ? 244 PHE   A CG  1 
ATOM   1541 C  CD1 . PHE   A 1 216 ? 14.129  -20.124 75.858  1.00 39.99  ? 244 PHE   A CD1 1 
ATOM   1542 C  CD2 . PHE   A 1 216 ? 15.447  -18.999 74.214  1.00 40.70  ? 244 PHE   A CD2 1 
ATOM   1543 C  CE1 . PHE   A 1 216 ? 13.017  -19.331 75.520  1.00 42.29  ? 244 PHE   A CE1 1 
ATOM   1544 C  CE2 . PHE   A 1 216 ? 14.337  -18.202 73.875  1.00 45.90  ? 244 PHE   A CE2 1 
ATOM   1545 C  CZ  . PHE   A 1 216 ? 13.126  -18.377 74.536  1.00 41.74  ? 244 PHE   A CZ  1 
ATOM   1546 N  N   . THR   A 1 217 ? 17.812  -17.784 76.649  1.00 41.27  ? 245 THR   A N   1 
ATOM   1547 C  CA  . THR   A 1 217 ? 18.221  -16.456 76.200  1.00 44.12  ? 245 THR   A CA  1 
ATOM   1548 C  C   . THR   A 1 217 ? 19.455  -15.922 76.910  1.00 44.55  ? 245 THR   A C   1 
ATOM   1549 O  O   . THR   A 1 217 ? 20.205  -15.137 76.317  1.00 41.45  ? 245 THR   A O   1 
ATOM   1550 C  CB  . THR   A 1 217 ? 17.107  -15.425 76.420  1.00 42.32  ? 245 THR   A CB  1 
ATOM   1551 O  OG1 . THR   A 1 217 ? 16.775  -15.387 77.814  1.00 42.07  ? 245 THR   A OG1 1 
ATOM   1552 C  CG2 . THR   A 1 217 ? 15.856  -15.739 75.588  1.00 43.72  ? 245 THR   A CG2 1 
ATOM   1553 N  N   . GLY   A 1 218 ? 19.662  -16.300 78.168  1.00 44.78  ? 246 GLY   A N   1 
ATOM   1554 C  CA  . GLY   A 1 218 ? 20.647  -15.630 78.989  1.00 44.90  ? 246 GLY   A CA  1 
ATOM   1555 C  C   . GLY   A 1 218 ? 20.158  -14.345 79.608  1.00 45.87  ? 246 GLY   A C   1 
ATOM   1556 O  O   . GLY   A 1 218 ? 20.947  -13.660 80.272  1.00 46.10  ? 246 GLY   A O   1 
ATOM   1557 N  N   . PHE   A 1 219 ? 18.887  -13.987 79.401  1.00 43.07  ? 247 PHE   A N   1 
ATOM   1558 C  CA  . PHE   A 1 219 ? 18.348  -12.770 79.989  1.00 45.08  ? 247 PHE   A CA  1 
ATOM   1559 C  C   . PHE   A 1 219 ? 18.382  -12.863 81.508  1.00 41.49  ? 247 PHE   A C   1 
ATOM   1560 O  O   . PHE   A 1 219 ? 18.141  -13.924 82.083  1.00 42.42  ? 247 PHE   A O   1 
ATOM   1561 C  CB  . PHE   A 1 219 ? 16.899  -12.535 79.513  1.00 44.05  ? 247 PHE   A CB  1 
ATOM   1562 C  CG  . PHE   A 1 219 ? 16.781  -12.119 78.069  1.00 45.69  ? 247 PHE   A CG  1 
ATOM   1563 C  CD1 . PHE   A 1 219 ? 17.901  -11.769 77.326  1.00 44.80  ? 247 PHE   A CD1 1 
ATOM   1564 C  CD2 . PHE   A 1 219 ? 15.531  -12.057 77.457  1.00 48.27  ? 247 PHE   A CD2 1 
ATOM   1565 C  CE1 . PHE   A 1 219 ? 17.785  -11.380 75.999  1.00 45.83  ? 247 PHE   A CE1 1 
ATOM   1566 C  CE2 . PHE   A 1 219 ? 15.405  -11.659 76.135  1.00 45.66  ? 247 PHE   A CE2 1 
ATOM   1567 C  CZ  . PHE   A 1 219 ? 16.525  -11.324 75.402  1.00 47.70  ? 247 PHE   A CZ  1 
ATOM   1568 N  N   . HIS   A 1 220 ? 18.663  -11.740 82.159  1.00 44.80  ? 248 HIS   A N   1 
ATOM   1569 C  CA  . HIS   A 1 220 ? 18.821  -11.689 83.605  1.00 46.92  ? 248 HIS   A CA  1 
ATOM   1570 C  C   . HIS   A 1 220 ? 17.622  -11.015 84.256  1.00 50.07  ? 248 HIS   A C   1 
ATOM   1571 O  O   . HIS   A 1 220 ? 16.945  -10.188 83.646  1.00 46.11  ? 248 HIS   A O   1 
ATOM   1572 C  CB  . HIS   A 1 220 ? 20.094  -10.930 83.990  1.00 48.19  ? 248 HIS   A CB  1 
ATOM   1573 C  CG  . HIS   A 1 220 ? 20.118  -9.520  83.497  1.00 47.38  ? 248 HIS   A CG  1 
ATOM   1574 N  ND1 . HIS   A 1 220 ? 20.558  -9.184  82.234  1.00 46.57  ? 248 HIS   A ND1 1 
ATOM   1575 C  CD2 . HIS   A 1 220 ? 19.741  -8.359  84.086  1.00 46.00  ? 248 HIS   A CD2 1 
ATOM   1576 C  CE1 . HIS   A 1 220 ? 20.455  -7.879  82.068  1.00 46.80  ? 248 HIS   A CE1 1 
ATOM   1577 N  NE2 . HIS   A 1 220 ? 19.959  -7.355  83.175  1.00 48.91  ? 248 HIS   A NE2 1 
ATOM   1578 N  N   . GLN   A 1 221 ? 17.401  -11.351 85.525  1.00 50.84  ? 249 GLN   A N   1 
ATOM   1579 C  CA  . GLN   A 1 221 ? 16.328  -10.746 86.301  1.00 51.20  ? 249 GLN   A CA  1 
ATOM   1580 C  C   . GLN   A 1 221 ? 16.638  -9.284  86.619  1.00 56.12  ? 249 GLN   A C   1 
ATOM   1581 O  O   . GLN   A 1 221 ? 17.701  -8.960  87.164  1.00 56.02  ? 249 GLN   A O   1 
ATOM   1582 C  CB  . GLN   A 1 221 ? 16.104  -11.537 87.586  1.00 56.71  ? 249 GLN   A CB  1 
ATOM   1583 C  CG  . GLN   A 1 221 ? 15.013  -10.973 88.474  1.00 59.32  ? 249 GLN   A CG  1 
ATOM   1584 C  CD  . GLN   A 1 221 ? 14.143  -12.056 89.076  1.00 58.91  ? 249 GLN   A CD  1 
ATOM   1585 O  OE1 . GLN   A 1 221 ? 14.449  -13.238 88.965  1.00 57.50  ? 249 GLN   A OE1 1 
ATOM   1586 N  NE2 . GLN   A 1 221 ? 13.046  -11.654 89.713  1.00 59.90  ? 249 GLN   A NE2 1 
ATOM   1587 N  N   . PHE   A 1 222 ? 15.683  -8.403  86.296  1.00 55.07  ? 250 PHE   A N   1 
ATOM   1588 C  CA  . PHE   A 1 222 ? 15.885  -6.955  86.357  1.00 57.23  ? 250 PHE   A CA  1 
ATOM   1589 C  C   . PHE   A 1 222 ? 15.595  -6.387  87.747  1.00 59.29  ? 250 PHE   A C   1 
ATOM   1590 O  O   . PHE   A 1 222 ? 16.261  -5.437  88.177  1.00 65.30  ? 250 PHE   A O   1 
ATOM   1591 C  CB  . PHE   A 1 222 ? 15.007  -6.283  85.296  1.00 57.72  ? 250 PHE   A CB  1 
ATOM   1592 C  CG  . PHE   A 1 222 ? 15.155  -4.785  85.215  1.00 58.05  ? 250 PHE   A CG  1 
ATOM   1593 C  CD1 . PHE   A 1 222 ? 14.292  -3.951  85.911  1.00 57.64  ? 250 PHE   A CD1 1 
ATOM   1594 C  CD2 . PHE   A 1 222 ? 16.141  -4.213  84.424  1.00 58.77  ? 250 PHE   A CD2 1 
ATOM   1595 C  CE1 . PHE   A 1 222 ? 14.413  -2.567  85.828  1.00 58.47  ? 250 PHE   A CE1 1 
ATOM   1596 C  CE2 . PHE   A 1 222 ? 16.275  -2.837  84.343  1.00 61.00  ? 250 PHE   A CE2 1 
ATOM   1597 C  CZ  . PHE   A 1 222 ? 15.404  -2.010  85.045  1.00 58.78  ? 250 PHE   A CZ  1 
ATOM   1598 N  N   . ALA   A 1 223 ? 14.587  -6.926  88.440  1.00 62.87  ? 251 ALA   A N   1 
ATOM   1599 C  CA  . ALA   A 1 223 ? 14.284  -6.615  89.838  1.00 67.91  ? 251 ALA   A CA  1 
ATOM   1600 C  C   . ALA   A 1 223 ? 13.669  -5.231  90.035  1.00 70.96  ? 251 ALA   A C   1 
ATOM   1601 O  O   . ALA   A 1 223 ? 14.051  -4.256  89.373  1.00 65.90  ? 251 ALA   A O   1 
ATOM   1602 C  CB  . ALA   A 1 223 ? 15.532  -6.768  90.715  1.00 70.19  ? 251 ALA   A CB  1 
ATOM   1603 N  N   . GLU   A 1 224 ? 12.723  -5.143  90.961  1.00 70.74  ? 252 GLU   A N   1 
ATOM   1604 C  CA  . GLU   A 1 224 ? 11.897  -3.953  91.151  1.00 70.42  ? 252 GLU   A CA  1 
ATOM   1605 C  C   . GLU   A 1 224 ? 12.324  -3.260  92.449  1.00 74.86  ? 252 GLU   A C   1 
ATOM   1606 O  O   . GLU   A 1 224 ? 13.526  -3.090  92.651  1.00 78.53  ? 252 GLU   A O   1 
ATOM   1607 C  CB  . GLU   A 1 224 ? 10.419  -4.330  91.064  1.00 69.82  ? 252 GLU   A CB  1 
ATOM   1608 C  CG  . GLU   A 1 224 ? 9.917   -4.480  89.624  1.00 68.12  ? 252 GLU   A CG  1 
ATOM   1609 C  CD  . GLU   A 1 224 ? 8.521   -5.072  89.535  1.00 63.61  ? 252 GLU   A CD  1 
ATOM   1610 O  OE1 . GLU   A 1 224 ? 8.397   -6.308  89.644  1.00 66.68  ? 252 GLU   A OE1 1 
ATOM   1611 O  OE2 . GLU   A 1 224 ? 7.549   -4.303  89.354  1.00 61.38  ? 252 GLU   A OE2 1 
ATOM   1612 N  N   . PHE   A 1 225 ? 11.407  -2.829  93.313  1.00 78.69  ? 253 PHE   A N   1 
ATOM   1613 C  CA  . PHE   A 1 225 ? 11.750  -2.047  94.502  1.00 74.86  ? 253 PHE   A CA  1 
ATOM   1614 C  C   . PHE   A 1 225 ? 10.605  -2.050  95.514  1.00 77.56  ? 253 PHE   A C   1 
ATOM   1615 O  O   . PHE   A 1 225 ? 10.323  -3.068  96.150  1.00 78.91  ? 253 PHE   A O   1 
ATOM   1616 C  CB  . PHE   A 1 225 ? 12.100  -0.608  94.118  1.00 76.39  ? 253 PHE   A CB  1 
ATOM   1617 N  N   . GLU   A 1 234 ? -3.115  -8.271  98.682  1.00 84.90  ? 262 GLU   A N   1 
ATOM   1618 C  CA  . GLU   A 1 234 ? -2.523  -7.061  98.120  1.00 84.81  ? 262 GLU   A CA  1 
ATOM   1619 C  C   . GLU   A 1 234 ? -2.772  -6.996  96.617  1.00 81.50  ? 262 GLU   A C   1 
ATOM   1620 O  O   . GLU   A 1 234 ? -3.917  -6.986  96.166  1.00 80.51  ? 262 GLU   A O   1 
ATOM   1621 C  CB  . GLU   A 1 234 ? -1.020  -7.010  98.414  1.00 84.84  ? 262 GLU   A CB  1 
ATOM   1622 N  N   . SER   A 1 235 ? -1.697  -6.934  95.840  1.00 79.20  ? 263 SER   A N   1 
ATOM   1623 C  CA  . SER   A 1 235 ? -1.830  -7.112  94.405  1.00 75.19  ? 263 SER   A CA  1 
ATOM   1624 C  C   . SER   A 1 235 ? -2.123  -8.576  94.111  1.00 75.11  ? 263 SER   A C   1 
ATOM   1625 O  O   . SER   A 1 235 ? -1.669  -9.476  94.824  1.00 75.37  ? 263 SER   A O   1 
ATOM   1626 C  CB  . SER   A 1 235 ? -0.557  -6.684  93.682  1.00 71.15  ? 263 SER   A CB  1 
ATOM   1627 O  OG  . SER   A 1 235 ? 0.359   -7.763  93.631  1.00 70.96  ? 263 SER   A OG  1 
ATOM   1628 N  N   . GLY   A 1 236 ? -2.892  -8.814  93.054  1.00 69.50  ? 264 GLY   A N   1 
ATOM   1629 C  CA  . GLY   A 1 236 ? -3.225  -10.180 92.697  1.00 67.17  ? 264 GLY   A CA  1 
ATOM   1630 C  C   . GLY   A 1 236 ? -2.173  -10.872 91.853  1.00 63.39  ? 264 GLY   A C   1 
ATOM   1631 O  O   . GLY   A 1 236 ? -2.481  -11.848 91.159  1.00 59.53  ? 264 GLY   A O   1 
ATOM   1632 N  N   . LEU   A 1 237 ? -0.932  -10.376 91.902  1.00 64.02  ? 265 LEU   A N   1 
ATOM   1633 C  CA  . LEU   A 1 237 ? 0.153   -10.838 91.043  1.00 61.65  ? 265 LEU   A CA  1 
ATOM   1634 C  C   . LEU   A 1 237 ? 1.391   -11.154 91.867  1.00 61.50  ? 265 LEU   A C   1 
ATOM   1635 O  O   . LEU   A 1 237 ? 1.585   -10.632 92.968  1.00 63.23  ? 265 LEU   A O   1 
ATOM   1636 C  CB  . LEU   A 1 237 ? 0.606   -9.787  90.006  1.00 59.26  ? 265 LEU   A CB  1 
ATOM   1637 C  CG  . LEU   A 1 237 ? -0.290  -9.031  89.030  1.00 63.27  ? 265 LEU   A CG  1 
ATOM   1638 C  CD1 . LEU   A 1 237 ? 0.573   -8.395  87.940  1.00 58.16  ? 265 LEU   A CD1 1 
ATOM   1639 C  CD2 . LEU   A 1 237 ? -1.353  -9.917  88.442  1.00 62.98  ? 265 LEU   A CD2 1 
ATOM   1640 N  N   . ASN   A 1 238 ? 2.236   -12.010 91.292  1.00 58.44  ? 266 ASN   A N   1 
ATOM   1641 C  CA  . ASN   A 1 238 ? 3.672   -12.017 91.528  1.00 58.53  ? 266 ASN   A CA  1 
ATOM   1642 C  C   . ASN   A 1 238 ? 4.351   -12.067 90.169  1.00 56.09  ? 266 ASN   A C   1 
ATOM   1643 O  O   . ASN   A 1 238 ? 3.834   -12.667 89.223  1.00 52.26  ? 266 ASN   A O   1 
ATOM   1644 C  CB  . ASN   A 1 238 ? 4.147   -13.197 92.393  1.00 59.22  ? 266 ASN   A CB  1 
ATOM   1645 C  CG  . ASN   A 1 238 ? 3.398   -13.308 93.707  1.00 62.93  ? 266 ASN   A CG  1 
ATOM   1646 O  OD1 . ASN   A 1 238 ? 3.171   -12.313 94.401  1.00 70.95  ? 266 ASN   A OD1 1 
ATOM   1647 N  ND2 . ASN   A 1 238 ? 3.037   -14.533 94.074  1.00 62.59  ? 266 ASN   A ND2 1 
ATOM   1648 N  N   . SER   A 1 239 ? 5.504   -11.417 90.060  1.00 52.64  ? 267 SER   A N   1 
ATOM   1649 C  CA  . SER   A 1 239 ? 6.063   -11.209 88.736  1.00 55.52  ? 267 SER   A CA  1 
ATOM   1650 C  C   . SER   A 1 239 ? 7.572   -11.076 88.802  1.00 55.60  ? 267 SER   A C   1 
ATOM   1651 O  O   . SER   A 1 239 ? 8.156   -10.832 89.860  1.00 56.89  ? 267 SER   A O   1 
ATOM   1652 C  CB  . SER   A 1 239 ? 5.460   -9.970  88.073  1.00 54.04  ? 267 SER   A CB  1 
ATOM   1653 O  OG  . SER   A 1 239 ? 5.535   -8.865  88.949  1.00 64.94  ? 267 SER   A OG  1 
ATOM   1654 N  N   . ALA   A 1 240 ? 8.191   -11.241 87.638  1.00 53.48  ? 268 ALA   A N   1 
ATOM   1655 C  CA  . ALA   A 1 240 ? 9.617   -11.024 87.477  1.00 53.60  ? 268 ALA   A CA  1 
ATOM   1656 C  C   . ALA   A 1 240 ? 9.868   -10.530 86.061  1.00 52.68  ? 268 ALA   A C   1 
ATOM   1657 O  O   . ALA   A 1 240 ? 9.131   -10.874 85.128  1.00 47.71  ? 268 ALA   A O   1 
ATOM   1658 C  CB  . ALA   A 1 240 ? 10.410  -12.302 87.755  1.00 54.58  ? 268 ALA   A CB  1 
ATOM   1659 N  N   . VAL   A 1 241 ? 10.922  -9.729  85.913  1.00 46.30  ? 269 VAL   A N   1 
ATOM   1660 C  CA  . VAL   A 1 241 ? 11.276  -9.086  84.651  1.00 44.60  ? 269 VAL   A CA  1 
ATOM   1661 C  C   . VAL   A 1 241 ? 12.611  -9.642  84.176  1.00 50.61  ? 269 VAL   A C   1 
ATOM   1662 O  O   . VAL   A 1 241 ? 13.620  -9.560  84.893  1.00 51.02  ? 269 VAL   A O   1 
ATOM   1663 C  CB  . VAL   A 1 241 ? 11.346  -7.559  84.795  1.00 47.40  ? 269 VAL   A CB  1 
ATOM   1664 C  CG1 . VAL   A 1 241 ? 11.829  -6.923  83.495  1.00 48.08  ? 269 VAL   A CG1 1 
ATOM   1665 C  CG2 . VAL   A 1 241 ? 9.986   -7.003  85.198  1.00 46.80  ? 269 VAL   A CG2 1 
ATOM   1666 N  N   . LEU   A 1 242 ? 12.619  -10.191 82.964  1.00 44.78  ? 270 LEU   A N   1 
ATOM   1667 C  CA  . LEU   A 1 242 ? 13.841  -10.606 82.288  1.00 46.78  ? 270 LEU   A CA  1 
ATOM   1668 C  C   . LEU   A 1 242 ? 14.286  -9.511  81.325  1.00 46.78  ? 270 LEU   A C   1 
ATOM   1669 O  O   . LEU   A 1 242 ? 13.453  -8.825  80.723  1.00 43.74  ? 270 LEU   A O   1 
ATOM   1670 C  CB  . LEU   A 1 242 ? 13.623  -11.929 81.557  1.00 46.17  ? 270 LEU   A CB  1 
ATOM   1671 C  CG  . LEU   A 1 242 ? 13.300  -13.120 82.467  1.00 48.74  ? 270 LEU   A CG  1 
ATOM   1672 C  CD1 . LEU   A 1 242 ? 12.913  -14.342 81.629  1.00 46.29  ? 270 LEU   A CD1 1 
ATOM   1673 C  CD2 . LEU   A 1 242 ? 14.466  -13.428 83.455  1.00 45.19  ? 270 LEU   A CD2 1 
ATOM   1674 N  N   . ALA   A 1 243 ? 15.600  -9.310  81.211  1.00 45.85  ? 271 ALA   A N   1 
ATOM   1675 C  CA  . ALA   A 1 243 ? 16.127  -8.218  80.405  1.00 43.17  ? 271 ALA   A CA  1 
ATOM   1676 C  C   . ALA   A 1 243 ? 17.386  -8.654  79.671  1.00 46.00  ? 271 ALA   A C   1 
ATOM   1677 O  O   . ALA   A 1 243 ? 18.155  -9.480  80.165  1.00 45.91  ? 271 ALA   A O   1 
ATOM   1678 C  CB  . ALA   A 1 243 ? 16.436  -6.984  81.266  1.00 46.01  ? 271 ALA   A CB  1 
ATOM   1679 N  N   . SER   A 1 244 ? 17.604  -8.060  78.499  1.00 45.81  ? 272 SER   A N   1 
ATOM   1680 C  CA  . SER   A 1 244 ? 18.818  -8.282  77.725  1.00 44.62  ? 272 SER   A CA  1 
ATOM   1681 C  C   . SER   A 1 244 ? 19.978  -7.471  78.301  1.00 46.77  ? 272 SER   A C   1 
ATOM   1682 O  O   . SER   A 1 244 ? 19.833  -6.738  79.286  1.00 45.43  ? 272 SER   A O   1 
ATOM   1683 C  CB  . SER   A 1 244 ? 18.595  -7.905  76.264  1.00 41.94  ? 272 SER   A CB  1 
ATOM   1684 O  OG  . SER   A 1 244 ? 18.147  -6.564  76.169  1.00 45.28  ? 272 SER   A OG  1 
ATOM   1685 N  N   . ASN   A 1 245 ? 21.134  -7.570  77.630  1.00 47.57  ? 273 ASN   A N   1 
ATOM   1686 C  CA  . ASN   A 1 245 ? 22.386  -7.025  78.163  1.00 50.53  ? 273 ASN   A CA  1 
ATOM   1687 C  C   . ASN   A 1 245 ? 22.266  -5.546  78.494  1.00 50.05  ? 273 ASN   A C   1 
ATOM   1688 O  O   . ASN   A 1 245 ? 22.649  -5.110  79.587  1.00 51.90  ? 273 ASN   A O   1 
ATOM   1689 C  CB  . ASN   A 1 245 ? 23.526  -7.245  77.168  1.00 45.89  ? 273 ASN   A CB  1 
ATOM   1690 C  CG  . ASN   A 1 245 ? 24.066  -8.656  77.207  1.00 50.96  ? 273 ASN   A CG  1 
ATOM   1691 O  OD1 . ASN   A 1 245 ? 23.731  -9.439  78.102  1.00 50.64  ? 273 ASN   A OD1 1 
ATOM   1692 N  ND2 . ASN   A 1 245 ? 24.914  -8.993  76.236  1.00 51.76  ? 273 ASN   A ND2 1 
ATOM   1693 N  N   . ASP   A 1 246 ? 21.755  -4.754  77.553  1.00 47.70  ? 274 ASP   A N   1 
ATOM   1694 C  CA  . ASP   A 1 246 ? 21.534  -3.339  77.799  1.00 45.70  ? 274 ASP   A CA  1 
ATOM   1695 C  C   . ASP   A 1 246 ? 20.155  -3.066  78.373  1.00 48.42  ? 274 ASP   A C   1 
ATOM   1696 O  O   . ASP   A 1 246 ? 19.749  -1.909  78.482  1.00 44.52  ? 274 ASP   A O   1 
ATOM   1697 C  CB  . ASP   A 1 246 ? 21.773  -2.511  76.528  1.00 47.43  ? 274 ASP   A CB  1 
ATOM   1698 C  CG  . ASP   A 1 246 ? 20.925  -2.938  75.340  1.00 52.72  ? 274 ASP   A CG  1 
ATOM   1699 O  OD1 . ASP   A 1 246 ? 19.900  -3.649  75.505  1.00 47.76  ? 274 ASP   A OD1 1 
ATOM   1700 O  OD2 . ASP   A 1 246 ? 21.289  -2.509  74.219  1.00 52.66  ? 274 ASP   A OD2 1 
ATOM   1701 N  N   . GLU   A 1 247 ? 19.438  -4.107  78.765  1.00 50.98  ? 275 GLU   A N   1 
ATOM   1702 C  CA  . GLU   A 1 247 ? 18.128  -3.961  79.388  1.00 47.90  ? 275 GLU   A CA  1 
ATOM   1703 C  C   . GLU   A 1 247 ? 17.157  -3.144  78.528  1.00 50.64  ? 275 GLU   A C   1 
ATOM   1704 O  O   . GLU   A 1 247 ? 16.185  -2.564  79.022  1.00 46.31  ? 275 GLU   A O   1 
ATOM   1705 C  CB  . GLU   A 1 247 ? 18.284  -3.355  80.777  1.00 48.96  ? 275 GLU   A CB  1 
ATOM   1706 C  CG  . GLU   A 1 247 ? 19.432  -4.052  81.517  1.00 54.30  ? 275 GLU   A CG  1 
ATOM   1707 C  CD  . GLU   A 1 247 ? 19.484  -3.734  82.974  1.00 53.40  ? 275 GLU   A CD  1 
ATOM   1708 O  OE1 . GLU   A 1 247 ? 19.608  -4.682  83.770  1.00 59.26  ? 275 GLU   A OE1 1 
ATOM   1709 O  OE2 . GLU   A 1 247 ? 19.402  -2.547  83.323  1.00 60.37  ? 275 GLU   A OE2 1 
ATOM   1710 N  N   . MET   A 1 248 ? 17.410  -3.076  77.228  1.00 47.45  ? 276 MET   A N   1 
ATOM   1711 C  CA  . MET   A 1 248 ? 16.411  -2.511  76.371  1.00 48.02  ? 276 MET   A CA  1 
ATOM   1712 C  C   . MET   A 1 248 ? 15.272  -3.522  76.206  1.00 47.94  ? 276 MET   A C   1 
ATOM   1713 O  O   . MET   A 1 248 ? 14.120  -3.148  76.508  1.00 47.30  ? 276 MET   A O   1 
ATOM   1714 C  CB  . MET   A 1 248 ? 17.070  -2.020  75.083  1.00 47.92  ? 276 MET   A CB  1 
ATOM   1715 C  CG  . MET   A 1 248 ? 17.910  -0.712  75.346  1.00 48.88  ? 276 MET   A CG  1 
ATOM   1716 S  SD  . MET   A 1 248 ? 16.885  0.674   75.959  1.00 56.60  ? 276 MET   A SD  1 
ATOM   1717 C  CE  . MET   A 1 248 ? 15.746  0.959   74.603  1.00 54.77  ? 276 MET   A CE  1 
ATOM   1718 N  N   . VAL   A 1 249 ? 15.556  -4.778  75.811  1.00 41.82  ? 277 VAL   A N   1 
ATOM   1719 C  CA  . VAL   A 1 249 ? 14.550  -5.822  75.666  1.00 41.80  ? 277 VAL   A CA  1 
ATOM   1720 C  C   . VAL   A 1 249 ? 14.114  -6.301  77.052  1.00 43.24  ? 277 VAL   A C   1 
ATOM   1721 O  O   . VAL   A 1 249 ? 14.886  -6.918  77.794  1.00 44.96  ? 277 VAL   A O   1 
ATOM   1722 C  CB  . VAL   A 1 249 ? 15.040  -6.996  74.801  1.00 45.77  ? 277 VAL   A CB  1 
ATOM   1723 C  CG1 . VAL   A 1 249 ? 14.126  -8.099  74.942  1.00 38.34  ? 277 VAL   A CG1 1 
ATOM   1724 C  CG2 . VAL   A 1 249 ? 15.125  -6.601  73.317  1.00 42.38  ? 277 VAL   A CG2 1 
ATOM   1725 N  N   . LEU   A 1 250 ? 12.851  -6.042  77.380  1.00 41.05  ? 278 LEU   A N   1 
ATOM   1726 C  CA  . LEU   A 1 250 ? 12.290  -6.262  78.700  1.00 37.70  ? 278 LEU   A CA  1 
ATOM   1727 C  C   . LEU   A 1 250 ? 11.074  -7.156  78.559  1.00 41.80  ? 278 LEU   A C   1 
ATOM   1728 O  O   . LEU   A 1 250 ? 10.094  -6.776  77.905  1.00 39.97  ? 278 LEU   A O   1 
ATOM   1729 C  CB  . LEU   A 1 250 ? 11.905  -4.927  79.349  1.00 40.83  ? 278 LEU   A CB  1 
ATOM   1730 C  CG  . LEU   A 1 250 ? 13.075  -3.947  79.518  1.00 42.27  ? 278 LEU   A CG  1 
ATOM   1731 C  CD1 . LEU   A 1 250 ? 12.591  -2.556  79.922  1.00 37.30  ? 278 LEU   A CD1 1 
ATOM   1732 C  CD2 . LEU   A 1 250 ? 14.046  -4.491  80.535  1.00 44.40  ? 278 LEU   A CD2 1 
ATOM   1733 N  N   . LEU   A 1 251 ? 11.124  -8.327  79.199  1.00 40.58  ? 279 LEU   A N   1 
ATOM   1734 C  CA  . LEU   A 1 251 ? 10.083  -9.345  79.077  1.00 43.83  ? 279 LEU   A CA  1 
ATOM   1735 C  C   . LEU   A 1 251 ? 9.624   -9.797  80.459  1.00 43.17  ? 279 LEU   A C   1 
ATOM   1736 O  O   . LEU   A 1 251 ? 10.077  -10.829 80.968  1.00 41.92  ? 279 LEU   A O   1 
ATOM   1737 C  CB  . LEU   A 1 251 ? 10.589  -10.529 78.250  1.00 41.55  ? 279 LEU   A CB  1 
ATOM   1738 C  CG  . LEU   A 1 251 ? 10.991  -10.247 76.798  1.00 39.20  ? 279 LEU   A CG  1 
ATOM   1739 C  CD1 . LEU   A 1 251 ? 11.513  -11.526 76.126  1.00 42.54  ? 279 LEU   A CD1 1 
ATOM   1740 C  CD2 . LEU   A 1 251 ? 9.815   -9.646  76.012  1.00 41.42  ? 279 LEU   A CD2 1 
ATOM   1741 N  N   . PRO   A 1 252 ? 8.718   -9.054  81.091  1.00 39.74  ? 280 PRO   A N   1 
ATOM   1742 C  CA  . PRO   A 1 252 ? 8.171   -9.487  82.384  1.00 41.98  ? 280 PRO   A CA  1 
ATOM   1743 C  C   . PRO   A 1 252 ? 7.186   -10.638 82.226  1.00 42.45  ? 280 PRO   A C   1 
ATOM   1744 O  O   . PRO   A 1 252 ? 6.580   -10.836 81.169  1.00 43.23  ? 280 PRO   A O   1 
ATOM   1745 C  CB  . PRO   A 1 252 ? 7.454   -8.236  82.910  1.00 42.64  ? 280 PRO   A CB  1 
ATOM   1746 C  CG  . PRO   A 1 252 ? 7.901   -7.098  82.017  1.00 44.40  ? 280 PRO   A CG  1 
ATOM   1747 C  CD  . PRO   A 1 252 ? 8.221   -7.731  80.697  1.00 39.76  ? 280 PRO   A CD  1 
ATOM   1748 N  N   . ILE   A 1 253 ? 7.008   -11.387 83.318  1.00 43.32  ? 281 ILE   A N   1 
ATOM   1749 C  CA  . ILE   A 1 253 ? 6.066   -12.506 83.371  1.00 44.11  ? 281 ILE   A CA  1 
ATOM   1750 C  C   . ILE   A 1 253 ? 5.310   -12.462 84.696  1.00 46.17  ? 281 ILE   A C   1 
ATOM   1751 O  O   . ILE   A 1 253 ? 5.919   -12.295 85.755  1.00 50.51  ? 281 ILE   A O   1 
ATOM   1752 C  CB  . ILE   A 1 253 ? 6.781   -13.862 83.206  1.00 45.89  ? 281 ILE   A CB  1 
ATOM   1753 C  CG1 . ILE   A 1 253 ? 7.609   -13.876 81.918  1.00 43.62  ? 281 ILE   A CG1 1 
ATOM   1754 C  CG2 . ILE   A 1 253 ? 5.762   -15.002 83.200  1.00 44.24  ? 281 ILE   A CG2 1 
ATOM   1755 C  CD1 . ILE   A 1 253 ? 8.315   -15.211 81.650  1.00 45.79  ? 281 ILE   A CD1 1 
ATOM   1756 N  N   . ASN   A 1 254 ? 3.990   -12.620 84.642  1.00 45.86  ? 282 ASN   A N   1 
ATOM   1757 C  CA  . ASN   A 1 254 ? 3.123   -12.599 85.815  1.00 46.65  ? 282 ASN   A CA  1 
ATOM   1758 C  C   . ASN   A 1 254 ? 2.563   -13.987 86.093  1.00 48.55  ? 282 ASN   A C   1 
ATOM   1759 O  O   . ASN   A 1 254 ? 2.386   -14.793 85.178  1.00 50.35  ? 282 ASN   A O   1 
ATOM   1760 C  CB  . ASN   A 1 254 ? 1.922   -11.657 85.626  1.00 47.33  ? 282 ASN   A CB  1 
ATOM   1761 C  CG  . ASN   A 1 254 ? 2.319   -10.229 85.349  1.00 48.59  ? 282 ASN   A CG  1 
ATOM   1762 O  OD1 . ASN   A 1 254 ? 3.284   -9.727  85.905  1.00 51.48  ? 282 ASN   A OD1 1 
ATOM   1763 N  ND2 . ASN   A 1 254 ? 1.548   -9.555  84.494  1.00 45.55  ? 282 ASN   A ND2 1 
ATOM   1764 N  N   . GLU   A 1 255 ? 2.233   -14.242 87.353  1.00 50.96  ? 283 GLU   A N   1 
ATOM   1765 C  CA  . GLU   A 1 255 ? 1.455   -15.405 87.749  1.00 50.65  ? 283 GLU   A CA  1 
ATOM   1766 C  C   . GLU   A 1 255 ? 0.425   -14.959 88.775  1.00 53.64  ? 283 GLU   A C   1 
ATOM   1767 O  O   . GLU   A 1 255 ? 0.579   -13.901 89.395  1.00 52.20  ? 283 GLU   A O   1 
ATOM   1768 C  CB  . GLU   A 1 255 ? 2.337   -16.522 88.328  1.00 52.72  ? 283 GLU   A CB  1 
ATOM   1769 C  CG  . GLU   A 1 255 ? 2.892   -16.226 89.695  1.00 56.97  ? 283 GLU   A CG  1 
ATOM   1770 C  CD  . GLU   A 1 255 ? 3.502   -17.455 90.358  1.00 57.50  ? 283 GLU   A CD  1 
ATOM   1771 O  OE1 . GLU   A 1 255 ? 3.769   -17.386 91.574  1.00 60.46  ? 283 GLU   A OE1 1 
ATOM   1772 O  OE2 . GLU   A 1 255 ? 3.702   -18.487 89.675  1.00 56.22  ? 283 GLU   A OE2 1 
ATOM   1773 N  N   . PRO   A 1 256 ? -0.647  -15.729 88.962  1.00 52.03  ? 284 PRO   A N   1 
ATOM   1774 C  CA  . PRO   A 1 256 ? -1.685  -15.322 89.914  1.00 55.47  ? 284 PRO   A CA  1 
ATOM   1775 C  C   . PRO   A 1 256 ? -1.260  -15.541 91.357  1.00 57.60  ? 284 PRO   A C   1 
ATOM   1776 O  O   . PRO   A 1 256 ? -0.413  -16.379 91.669  1.00 55.90  ? 284 PRO   A O   1 
ATOM   1777 C  CB  . PRO   A 1 256 ? -2.879  -16.222 89.560  1.00 57.95  ? 284 PRO   A CB  1 
ATOM   1778 C  CG  . PRO   A 1 256 ? -2.535  -16.891 88.257  1.00 54.55  ? 284 PRO   A CG  1 
ATOM   1779 C  CD  . PRO   A 1 256 ? -1.041  -16.924 88.194  1.00 53.49  ? 284 PRO   A CD  1 
ATOM   1780 N  N   . VAL   A 1 257 ? -1.860  -14.755 92.242  1.00 61.39  ? 285 VAL   A N   1 
ATOM   1781 C  CA  . VAL   A 1 257 ? -1.806  -14.988 93.679  1.00 64.13  ? 285 VAL   A CA  1 
ATOM   1782 C  C   . VAL   A 1 257 ? -3.207  -15.418 94.084  1.00 64.32  ? 285 VAL   A C   1 
ATOM   1783 O  O   . VAL   A 1 257 ? -4.114  -14.588 94.210  1.00 65.23  ? 285 VAL   A O   1 
ATOM   1784 C  CB  . VAL   A 1 257 ? -1.354  -13.750 94.462  1.00 62.80  ? 285 VAL   A CB  1 
ATOM   1785 C  CG1 . VAL   A 1 257 ? -1.341  -14.051 95.954  1.00 63.17  ? 285 VAL   A CG1 1 
ATOM   1786 C  CG2 . VAL   A 1 257 ? 0.007   -13.313 94.009  1.00 63.15  ? 285 VAL   A CG2 1 
ATOM   1787 N  N   . HIS   A 1 258 ? -3.399  -16.714 94.269  1.00 67.00  ? 286 HIS   A N   1 
ATOM   1788 C  CA  . HIS   A 1 258 ? -4.716  -17.198 94.637  1.00 68.27  ? 286 HIS   A CA  1 
ATOM   1789 C  C   . HIS   A 1 258 ? -4.975  -16.943 96.118  1.00 70.71  ? 286 HIS   A C   1 
ATOM   1790 O  O   . HIS   A 1 258 ? -4.055  -16.715 96.908  1.00 74.82  ? 286 HIS   A O   1 
ATOM   1791 C  CB  . HIS   A 1 258 ? -4.845  -18.682 94.306  1.00 67.58  ? 286 HIS   A CB  1 
ATOM   1792 C  CG  . HIS   A 1 258 ? -4.514  -19.006 92.881  1.00 69.96  ? 286 HIS   A CG  1 
ATOM   1793 N  ND1 . HIS   A 1 258 ? -3.278  -19.480 92.491  1.00 67.74  ? 286 HIS   A ND1 1 
ATOM   1794 C  CD2 . HIS   A 1 258 ? -5.253  -18.907 91.749  1.00 64.94  ? 286 HIS   A CD2 1 
ATOM   1795 C  CE1 . HIS   A 1 258 ? -3.275  -19.672 91.183  1.00 66.22  ? 286 HIS   A CE1 1 
ATOM   1796 N  NE2 . HIS   A 1 258 ? -4.461  -19.330 90.709  1.00 64.85  ? 286 HIS   A NE2 1 
ATOM   1797 N  N   . GLY   A 1 259 ? -6.253  -16.953 96.485  1.00 72.38  ? 287 GLY   A N   1 
ATOM   1798 C  CA  . GLY   A 1 259 ? -6.652  -16.757 97.859  1.00 74.43  ? 287 GLY   A CA  1 
ATOM   1799 C  C   . GLY   A 1 259 ? -6.857  -15.317 98.278  1.00 77.51  ? 287 GLY   A C   1 
ATOM   1800 O  O   . GLY   A 1 259 ? -7.310  -15.080 99.406  1.00 78.11  ? 287 GLY   A O   1 
ATOM   1801 N  N   . THR   A 1 260 ? -6.542  -14.349 97.418  1.00 76.08  ? 288 THR   A N   1 
ATOM   1802 C  CA  . THR   A 1 260 ? -6.743  -12.953 97.769  1.00 75.34  ? 288 THR   A CA  1 
ATOM   1803 C  C   . THR   A 1 260 ? -8.228  -12.599 97.742  1.00 76.37  ? 288 THR   A C   1 
ATOM   1804 O  O   . THR   A 1 260 ? -9.054  -13.302 97.153  1.00 75.06  ? 288 THR   A O   1 
ATOM   1805 C  CB  . THR   A 1 260 ? -5.972  -12.035 96.819  1.00 75.15  ? 288 THR   A CB  1 
ATOM   1806 O  OG1 . THR   A 1 260 ? -6.630  -11.993 95.547  1.00 74.45  ? 288 THR   A OG1 1 
ATOM   1807 C  CG2 . THR   A 1 260 ? -4.557  -12.545 96.631  1.00 75.69  ? 288 THR   A CG2 1 
ATOM   1808 N  N   . LYS   A 1 261 ? -8.558  -11.480 98.396  1.00 77.89  ? 289 LYS   A N   1 
ATOM   1809 C  CA  . LYS   A 1 261 ? -9.953  -11.061 98.519  1.00 77.36  ? 289 LYS   A CA  1 
ATOM   1810 C  C   . LYS   A 1 261 ? -10.579 -10.807 97.151  1.00 76.83  ? 289 LYS   A C   1 
ATOM   1811 O  O   . LYS   A 1 261 ? -11.634 -11.364 96.826  1.00 80.39  ? 289 LYS   A O   1 
ATOM   1812 C  CB  . LYS   A 1 261 ? -10.046 -9.812  99.399  1.00 75.99  ? 289 LYS   A CB  1 
ATOM   1813 N  N   . ARG   A 1 262 ? -9.949  -9.957  96.340  1.00 75.24  ? 290 ARG   A N   1 
ATOM   1814 C  CA  . ARG   A 1 262 ? -10.353 -9.769  94.953  1.00 72.02  ? 290 ARG   A CA  1 
ATOM   1815 C  C   . ARG   A 1 262 ? -9.679  -10.832 94.092  1.00 69.37  ? 290 ARG   A C   1 
ATOM   1816 O  O   . ARG   A 1 262 ? -8.474  -11.066 94.224  1.00 71.30  ? 290 ARG   A O   1 
ATOM   1817 C  CB  . ARG   A 1 262 ? -9.979  -8.371  94.461  1.00 68.51  ? 290 ARG   A CB  1 
ATOM   1818 N  N   . LYS   A 1 263 ? -10.459 -11.480 93.226  1.00 66.53  ? 291 LYS   A N   1 
ATOM   1819 C  CA  . LYS   A 1 263 ? -9.904  -12.514 92.361  1.00 65.87  ? 291 LYS   A CA  1 
ATOM   1820 C  C   . LYS   A 1 263 ? -8.779  -11.936 91.514  1.00 62.84  ? 291 LYS   A C   1 
ATOM   1821 O  O   . LYS   A 1 263 ? -8.875  -10.814 91.010  1.00 60.47  ? 291 LYS   A O   1 
ATOM   1822 C  CB  . LYS   A 1 263 ? -10.985 -13.106 91.455  1.00 60.02  ? 291 LYS   A CB  1 
ATOM   1823 C  CG  . LYS   A 1 263 ? -10.470 -14.235 90.566  1.00 60.06  ? 291 LYS   A CG  1 
ATOM   1824 C  CD  . LYS   A 1 263 ? -11.479 -14.620 89.503  1.00 60.23  ? 291 LYS   A CD  1 
ATOM   1825 C  CE  . LYS   A 1 263 ? -11.098 -15.922 88.818  1.00 59.03  ? 291 LYS   A CE  1 
ATOM   1826 N  NZ  . LYS   A 1 263 ? -12.120 -16.320 87.803  1.00 54.89  ? 291 LYS   A NZ  1 
ATOM   1827 N  N   . SER   A 1 264 ? -7.706  -12.710 91.368  1.00 62.97  ? 292 SER   A N   1 
ATOM   1828 C  CA  . SER   A 1 264 ? -6.538  -12.242 90.635  1.00 60.59  ? 292 SER   A CA  1 
ATOM   1829 C  C   . SER   A 1 264 ? -6.889  -11.934 89.186  1.00 56.50  ? 292 SER   A C   1 
ATOM   1830 O  O   . SER   A 1 264 ? -7.500  -12.755 88.498  1.00 54.20  ? 292 SER   A O   1 
ATOM   1831 C  CB  . SER   A 1 264 ? -5.431  -13.289 90.677  1.00 54.23  ? 292 SER   A CB  1 
ATOM   1832 O  OG  . SER   A 1 264 ? -4.365  -12.875 89.843  1.00 55.27  ? 292 SER   A OG  1 
ATOM   1833 N  N   . GLN   A 1 265 ? -6.480  -10.753 88.718  1.00 54.60  ? 293 GLN   A N   1 
ATOM   1834 C  CA  . GLN   A 1 265 ? -6.615  -10.426 87.301  1.00 54.84  ? 293 GLN   A CA  1 
ATOM   1835 C  C   . GLN   A 1 265 ? -5.866  -11.423 86.417  1.00 52.02  ? 293 GLN   A C   1 
ATOM   1836 O  O   . GLN   A 1 265 ? -6.299  -11.718 85.297  1.00 46.68  ? 293 GLN   A O   1 
ATOM   1837 C  CB  . GLN   A 1 265 ? -6.121  -9.002  87.038  1.00 56.93  ? 293 GLN   A CB  1 
ATOM   1838 C  CG  . GLN   A 1 265 ? -4.850  -8.617  87.790  1.00 59.51  ? 293 GLN   A CG  1 
ATOM   1839 C  CD  . GLN   A 1 265 ? -5.123  -8.027  89.174  1.00 67.22  ? 293 GLN   A CD  1 
ATOM   1840 O  OE1 . GLN   A 1 265 ? -5.542  -8.736  90.098  1.00 65.39  ? 293 GLN   A OE1 1 
ATOM   1841 N  NE2 . GLN   A 1 265 ? -4.873  -6.728  89.325  1.00 66.53  ? 293 GLN   A NE2 1 
ATOM   1842 N  N   . ILE   A 1 266 ? -4.718  -11.926 86.886  1.00 53.06  ? 294 ILE   A N   1 
ATOM   1843 C  CA  . ILE   A 1 266 ? -3.987  -12.917 86.094  1.00 50.35  ? 294 ILE   A CA  1 
ATOM   1844 C  C   . ILE   A 1 266 ? -4.814  -14.183 85.934  1.00 49.63  ? 294 ILE   A C   1 
ATOM   1845 O  O   . ILE   A 1 266 ? -4.844  -14.790 84.856  1.00 49.24  ? 294 ILE   A O   1 
ATOM   1846 C  CB  . ILE   A 1 266 ? -2.610  -13.242 86.704  1.00 50.50  ? 294 ILE   A CB  1 
ATOM   1847 C  CG1 . ILE   A 1 266 ? -1.776  -11.979 86.928  1.00 53.94  ? 294 ILE   A CG1 1 
ATOM   1848 C  CG2 . ILE   A 1 266 ? -1.854  -14.198 85.801  1.00 49.15  ? 294 ILE   A CG2 1 
ATOM   1849 C  CD1 . ILE   A 1 266 ? -1.741  -11.012 85.748  1.00 48.35  ? 294 ILE   A CD1 1 
ATOM   1850 N  N   . GLN   A 1 267 ? -5.496  -14.609 87.000  1.00 50.84  ? 295 GLN   A N   1 
ATOM   1851 C  CA  . GLN   A 1 267 ? -6.307  -15.816 86.894  1.00 50.91  ? 295 GLN   A CA  1 
ATOM   1852 C  C   . GLN   A 1 267 ? -7.491  -15.600 85.964  1.00 50.73  ? 295 GLN   A C   1 
ATOM   1853 O  O   . GLN   A 1 267 ? -7.834  -16.481 85.166  1.00 51.13  ? 295 GLN   A O   1 
ATOM   1854 C  CB  . GLN   A 1 267 ? -6.794  -16.264 88.272  1.00 56.33  ? 295 GLN   A CB  1 
ATOM   1855 C  CG  . GLN   A 1 267 ? -7.599  -17.568 88.236  1.00 50.98  ? 295 GLN   A CG  1 
ATOM   1856 C  CD  . GLN   A 1 267 ? -6.782  -18.732 87.702  1.00 54.72  ? 295 GLN   A CD  1 
ATOM   1857 O  OE1 . GLN   A 1 267 ? -5.559  -18.753 87.835  1.00 57.11  ? 295 GLN   A OE1 1 
ATOM   1858 N  NE2 . GLN   A 1 267 ? -7.452  -19.699 87.087  1.00 58.21  ? 295 GLN   A NE2 1 
ATOM   1859 N  N   . THR   A 1 268 ? -8.129  -14.435 86.049  1.00 50.00  ? 296 THR   A N   1 
ATOM   1860 C  CA  . THR   A 1 268 ? -9.185  -14.126 85.093  1.00 47.57  ? 296 THR   A CA  1 
ATOM   1861 C  C   . THR   A 1 268 ? -8.646  -14.167 83.670  1.00 45.63  ? 296 THR   A C   1 
ATOM   1862 O  O   . THR   A 1 268 ? -9.297  -14.710 82.771  1.00 45.77  ? 296 THR   A O   1 
ATOM   1863 C  CB  . THR   A 1 268 ? -9.805  -12.767 85.418  1.00 51.38  ? 296 THR   A CB  1 
ATOM   1864 O  OG1 . THR   A 1 268 ? -10.421 -12.833 86.711  1.00 54.34  ? 296 THR   A OG1 1 
ATOM   1865 C  CG2 . THR   A 1 268 ? -10.869 -12.391 84.383  1.00 51.41  ? 296 THR   A CG2 1 
ATOM   1866 N  N   . TYR   A 1 269 ? -7.429  -13.652 83.456  1.00 45.66  ? 297 TYR   A N   1 
ATOM   1867 C  CA  . TYR   A 1 269 ? -6.818  -13.725 82.132  1.00 43.92  ? 297 TYR   A CA  1 
ATOM   1868 C  C   . TYR   A 1 269 ? -6.711  -15.173 81.660  1.00 42.63  ? 297 TYR   A C   1 
ATOM   1869 O  O   . TYR   A 1 269 ? -7.204  -15.523 80.582  1.00 41.06  ? 297 TYR   A O   1 
ATOM   1870 C  CB  . TYR   A 1 269 ? -5.437  -13.050 82.133  1.00 43.35  ? 297 TYR   A CB  1 
ATOM   1871 C  CG  . TYR   A 1 269 ? -4.709  -13.165 80.798  1.00 40.74  ? 297 TYR   A CG  1 
ATOM   1872 C  CD1 . TYR   A 1 269 ? -4.061  -14.346 80.427  1.00 41.18  ? 297 TYR   A CD1 1 
ATOM   1873 C  CD2 . TYR   A 1 269 ? -4.679  -12.100 79.908  1.00 40.44  ? 297 TYR   A CD2 1 
ATOM   1874 C  CE1 . TYR   A 1 269 ? -3.413  -14.465 79.210  1.00 38.41  ? 297 TYR   A CE1 1 
ATOM   1875 C  CE2 . TYR   A 1 269 ? -4.022  -12.203 78.687  1.00 41.00  ? 297 TYR   A CE2 1 
ATOM   1876 C  CZ  . TYR   A 1 269 ? -3.388  -13.394 78.343  1.00 43.01  ? 297 TYR   A CZ  1 
ATOM   1877 O  OH  . TYR   A 1 269 ? -2.729  -13.525 77.133  1.00 38.21  ? 297 TYR   A OH  1 
ATOM   1878 N  N   . LEU   A 1 270 ? -6.060  -16.031 82.459  1.00 46.20  ? 298 LEU   A N   1 
ATOM   1879 C  CA  . LEU   A 1 270 ? -5.818  -17.415 82.045  1.00 42.52  ? 298 LEU   A CA  1 
ATOM   1880 C  C   . LEU   A 1 270 ? -7.109  -18.156 81.724  1.00 45.82  ? 298 LEU   A C   1 
ATOM   1881 O  O   . LEU   A 1 270 ? -7.122  -19.038 80.853  1.00 42.30  ? 298 LEU   A O   1 
ATOM   1882 C  CB  . LEU   A 1 270 ? -5.053  -18.171 83.135  1.00 48.84  ? 298 LEU   A CB  1 
ATOM   1883 C  CG  . LEU   A 1 270 ? -3.664  -17.655 83.524  1.00 47.36  ? 298 LEU   A CG  1 
ATOM   1884 C  CD1 . LEU   A 1 270 ? -3.122  -18.466 84.691  1.00 52.55  ? 298 LEU   A CD1 1 
ATOM   1885 C  CD2 . LEU   A 1 270 ? -2.704  -17.702 82.336  1.00 43.62  ? 298 LEU   A CD2 1 
ATOM   1886 N  N   . GLU   A 1 271 ? -8.199  -17.822 82.415  1.00 45.42  ? 299 GLU   A N   1 
ATOM   1887 C  CA  . GLU   A 1 271 ? -9.463  -18.497 82.162  1.00 48.78  ? 299 GLU   A CA  1 
ATOM   1888 C  C   . GLU   A 1 271 ? -10.074 -18.036 80.845  1.00 45.76  ? 299 GLU   A C   1 
ATOM   1889 O  O   . GLU   A 1 271 ? -10.518 -18.857 80.036  1.00 47.35  ? 299 GLU   A O   1 
ATOM   1890 C  CB  . GLU   A 1 271 ? -10.415 -18.267 83.339  1.00 52.30  ? 299 GLU   A CB  1 
ATOM   1891 C  CG  . GLU   A 1 271 ? -9.933  -18.970 84.618  1.00 56.19  ? 299 GLU   A CG  1 
ATOM   1892 C  CD  . GLU   A 1 271 ? -10.704 -18.565 85.866  1.00 59.81  ? 299 GLU   A CD  1 
ATOM   1893 O  OE1 . GLU   A 1 271 ? -10.643 -19.324 86.864  1.00 57.00  ? 299 GLU   A OE1 1 
ATOM   1894 O  OE2 . GLU   A 1 271 ? -11.356 -17.494 85.852  1.00 53.65  ? 299 GLU   A OE2 1 
ATOM   1895 N  N   . HIS   A 1 272 ? -10.073 -16.731 80.590  1.00 43.31  ? 300 HIS   A N   1 
ATOM   1896 C  CA  . HIS   A 1 272 ? -10.674 -16.232 79.360  1.00 43.30  ? 300 HIS   A CA  1 
ATOM   1897 C  C   . HIS   A 1 272 ? -9.767  -16.402 78.147  1.00 42.14  ? 300 HIS   A C   1 
ATOM   1898 O  O   . HIS   A 1 272 ? -10.274 -16.490 77.025  1.00 39.27  ? 300 HIS   A O   1 
ATOM   1899 C  CB  . HIS   A 1 272 ? -11.081 -14.766 79.539  1.00 41.57  ? 300 HIS   A CB  1 
ATOM   1900 C  CG  . HIS   A 1 272 ? -12.212 -14.576 80.502  1.00 42.76  ? 300 HIS   A CG  1 
ATOM   1901 N  ND1 . HIS   A 1 272 ? -13.490 -14.253 80.096  1.00 44.98  ? 300 HIS   A ND1 1 
ATOM   1902 C  CD2 . HIS   A 1 272 ? -12.263 -14.685 81.851  1.00 46.27  ? 300 HIS   A CD2 1 
ATOM   1903 C  CE1 . HIS   A 1 272 ? -14.279 -14.172 81.152  1.00 43.85  ? 300 HIS   A CE1 1 
ATOM   1904 N  NE2 . HIS   A 1 272 ? -13.559 -14.424 82.230  1.00 43.17  ? 300 HIS   A NE2 1 
ATOM   1905 N  N   . ASN   A 1 273 ? -8.449  -16.491 78.344  1.00 42.17  ? 301 ASN   A N   1 
ATOM   1906 C  CA  . ASN   A 1 273 ? -7.516  -16.677 77.239  1.00 39.54  ? 301 ASN   A CA  1 
ATOM   1907 C  C   . ASN   A 1 273 ? -7.337  -18.140 76.858  1.00 42.13  ? 301 ASN   A C   1 
ATOM   1908 O  O   . ASN   A 1 273 ? -6.642  -18.432 75.876  1.00 43.57  ? 301 ASN   A O   1 
ATOM   1909 C  CB  . ASN   A 1 273 ? -6.148  -16.092 77.605  1.00 40.31  ? 301 ASN   A CB  1 
ATOM   1910 C  CG  . ASN   A 1 273 ? -5.235  -15.932 76.401  1.00 41.75  ? 301 ASN   A CG  1 
ATOM   1911 O  OD1 . ASN   A 1 273 ? -5.552  -15.188 75.472  1.00 43.09  ? 301 ASN   A OD1 1 
ATOM   1912 N  ND2 . ASN   A 1 273 ? -4.087  -16.608 76.421  1.00 36.38  ? 301 ASN   A ND2 1 
ATOM   1913 N  N   . GLU   A 1 274 ? -7.908  -19.058 77.626  1.00 42.81  ? 302 GLU   A N   1 
ATOM   1914 C  CA  . GLU   A 1 274 ? -7.543  -20.475 77.552  1.00 43.61  ? 302 GLU   A CA  1 
ATOM   1915 C  C   . GLU   A 1 274 ? -6.033  -20.657 77.728  1.00 43.81  ? 302 GLU   A C   1 
ATOM   1916 O  O   . GLU   A 1 274 ? -5.337  -21.215 76.875  1.00 46.14  ? 302 GLU   A O   1 
ATOM   1917 C  CB  . GLU   A 1 274 ? -8.024  -21.099 76.239  1.00 43.15  ? 302 GLU   A CB  1 
ATOM   1918 C  CG  . GLU   A 1 274 ? -9.508  -20.963 76.017  1.00 44.05  ? 302 GLU   A CG  1 
ATOM   1919 C  CD  . GLU   A 1 274 ? -10.018 -21.809 74.859  1.00 42.51  ? 302 GLU   A CD  1 
ATOM   1920 O  OE1 . GLU   A 1 274 ? -9.206  -22.473 74.181  1.00 46.46  ? 302 GLU   A OE1 1 
ATOM   1921 O  OE2 . GLU   A 1 274 ? -11.239 -21.801 74.637  1.00 44.70  ? 302 GLU   A OE2 1 
ATOM   1922 N  N   . GLY   A 1 275 ? -5.524  -20.155 78.843  1.00 42.19  ? 303 GLY   A N   1 
ATOM   1923 C  CA  . GLY   A 1 275 ? -4.161  -20.445 79.246  1.00 40.91  ? 303 GLY   A CA  1 
ATOM   1924 C  C   . GLY   A 1 275 ? -3.230  -19.256 79.082  1.00 39.43  ? 303 GLY   A C   1 
ATOM   1925 O  O   . GLY   A 1 275 ? -3.650  -18.111 78.877  1.00 37.70  ? 303 GLY   A O   1 
ATOM   1926 N  N   . ALA   A 1 276 ? -1.934  -19.557 79.174  1.00 41.87  ? 304 ALA   A N   1 
ATOM   1927 C  CA  . ALA   A 1 276 ? -0.910  -18.522 79.172  1.00 38.72  ? 304 ALA   A CA  1 
ATOM   1928 C  C   . ALA   A 1 276 ? -0.888  -17.789 77.838  1.00 36.83  ? 304 ALA   A C   1 
ATOM   1929 O  O   . ALA   A 1 276 ? -1.341  -18.299 76.805  1.00 38.61  ? 304 ALA   A O   1 
ATOM   1930 C  CB  . ALA   A 1 276 ? 0.476   -19.120 79.456  1.00 39.34  ? 304 ALA   A CB  1 
ATOM   1931 N  N   . GLY   A 1 277 ? -0.346  -16.577 77.872  1.00 36.91  ? 305 GLY   A N   1 
ATOM   1932 C  CA  . GLY   A 1 277 ? -0.249  -15.756 76.684  1.00 37.15  ? 305 GLY   A CA  1 
ATOM   1933 C  C   . GLY   A 1 277 ? 0.162   -14.348 77.059  1.00 39.89  ? 305 GLY   A C   1 
ATOM   1934 O  O   . GLY   A 1 277 ? 0.434   -14.041 78.225  1.00 41.37  ? 305 GLY   A O   1 
ATOM   1935 N  N   . LEU   A 1 278 ? 0.187   -13.484 76.047  1.00 39.89  ? 306 LEU   A N   1 
ATOM   1936 C  CA  . LEU   A 1 278 ? 0.656   -12.121 76.249  1.00 38.88  ? 306 LEU   A CA  1 
ATOM   1937 C  C   . LEU   A 1 278 ? -0.430  -11.285 76.917  1.00 39.10  ? 306 LEU   A C   1 
ATOM   1938 O  O   . LEU   A 1 278 ? -1.560  -11.229 76.431  1.00 37.27  ? 306 LEU   A O   1 
ATOM   1939 C  CB  . LEU   A 1 278 ? 1.089   -11.494 74.922  1.00 35.85  ? 306 LEU   A CB  1 
ATOM   1940 C  CG  . LEU   A 1 278 ? 1.947   -10.231 75.147  1.00 38.20  ? 306 LEU   A CG  1 
ATOM   1941 C  CD1 . LEU   A 1 278 ? 3.129   -10.124 74.158  1.00 37.06  ? 306 LEU   A CD1 1 
ATOM   1942 C  CD2 . LEU   A 1 278 ? 1.123   -8.937  75.149  1.00 36.60  ? 306 LEU   A CD2 1 
ATOM   1943 N  N   . GLN   A 1 279 ? -0.076  -10.614 78.023  1.00 36.83  ? 307 GLN   A N   1 
ATOM   1944 C  CA  . GLN   A 1 279 ? -1.041  -9.811  78.777  1.00 37.37  ? 307 GLN   A CA  1 
ATOM   1945 C  C   . GLN   A 1 279 ? -1.083  -8.347  78.324  1.00 37.71  ? 307 GLN   A C   1 
ATOM   1946 O  O   . GLN   A 1 279 ? -2.150  -7.839  77.958  1.00 37.15  ? 307 GLN   A O   1 
ATOM   1947 C  CB  . GLN   A 1 279 ? -0.749  -9.863  80.281  1.00 41.39  ? 307 GLN   A CB  1 
ATOM   1948 C  CG  . GLN   A 1 279 ? -1.748  -9.029  81.085  1.00 42.04  ? 307 GLN   A CG  1 
ATOM   1949 C  CD  . GLN   A 1 279 ? -1.196  -8.510  82.400  1.00 43.87  ? 307 GLN   A CD  1 
ATOM   1950 O  OE1 . GLN   A 1 279 ? -0.110  -7.920  82.454  1.00 44.74  ? 307 GLN   A OE1 1 
ATOM   1951 N  NE2 . GLN   A 1 279 ? -1.946  -8.726  83.473  1.00 46.91  ? 307 GLN   A NE2 1 
ATOM   1952 N  N   . HIS   A 1 280 ? 0.045   -7.641  78.366  1.00 37.47  ? 308 HIS   A N   1 
ATOM   1953 C  CA  . HIS   A 1 280 ? 0.012   -6.263  77.898  1.00 37.10  ? 308 HIS   A CA  1 
ATOM   1954 C  C   . HIS   A 1 280 ? 1.303   -5.871  77.194  1.00 37.75  ? 308 HIS   A C   1 
ATOM   1955 O  O   . HIS   A 1 280 ? 2.369   -6.457  77.390  1.00 36.47  ? 308 HIS   A O   1 
ATOM   1956 C  CB  . HIS   A 1 280 ? -0.343  -5.255  79.024  1.00 36.19  ? 308 HIS   A CB  1 
ATOM   1957 C  CG  . HIS   A 1 280 ? 0.736   -5.015  80.038  1.00 40.57  ? 308 HIS   A CG  1 
ATOM   1958 N  ND1 . HIS   A 1 280 ? 0.935   -5.841  81.123  1.00 41.48  ? 308 HIS   A ND1 1 
ATOM   1959 C  CD2 . HIS   A 1 280 ? 1.619   -3.993  80.179  1.00 43.97  ? 308 HIS   A CD2 1 
ATOM   1960 C  CE1 . HIS   A 1 280 ? 1.919   -5.361  81.867  1.00 40.33  ? 308 HIS   A CE1 1 
ATOM   1961 N  NE2 . HIS   A 1 280 ? 2.368   -4.254  81.304  1.00 42.27  ? 308 HIS   A NE2 1 
ATOM   1962 N  N   . LEU   A 1 281 ? 1.148   -4.883  76.319  1.00 33.71  ? 309 LEU   A N   1 
ATOM   1963 C  CA  . LEU   A 1 281 ? 2.223   -4.231  75.600  1.00 32.73  ? 309 LEU   A CA  1 
ATOM   1964 C  C   . LEU   A 1 281 ? 2.315   -2.823  76.182  1.00 35.92  ? 309 LEU   A C   1 
ATOM   1965 O  O   . LEU   A 1 281 ? 1.293   -2.148  76.300  1.00 35.65  ? 309 LEU   A O   1 
ATOM   1966 C  CB  . LEU   A 1 281 ? 1.900   -4.183  74.101  1.00 32.25  ? 309 LEU   A CB  1 
ATOM   1967 C  CG  . LEU   A 1 281 ? 1.803   -5.544  73.393  1.00 34.26  ? 309 LEU   A CG  1 
ATOM   1968 C  CD1 . LEU   A 1 281 ? 1.117   -5.404  72.051  1.00 35.87  ? 309 LEU   A CD1 1 
ATOM   1969 C  CD2 . LEU   A 1 281 ? 3.201   -6.093  73.215  1.00 35.54  ? 309 LEU   A CD2 1 
ATOM   1970 N  N   . ALA   A 1 282 ? 3.499   -2.413  76.611  1.00 33.40  ? 310 ALA   A N   1 
ATOM   1971 C  CA  . ALA   A 1 282 ? 3.692   -1.051  77.113  1.00 37.73  ? 310 ALA   A CA  1 
ATOM   1972 C  C   . ALA   A 1 282 ? 4.447   -0.256  76.061  1.00 33.29  ? 310 ALA   A C   1 
ATOM   1973 O  O   . ALA   A 1 282 ? 5.557   -0.641  75.672  1.00 36.73  ? 310 ALA   A O   1 
ATOM   1974 C  CB  . ALA   A 1 282 ? 4.444   -1.038  78.437  1.00 34.33  ? 310 ALA   A CB  1 
ATOM   1975 N  N   . LEU   A 1 283 ? 3.839   0.834   75.606  1.00 34.06  ? 311 LEU   A N   1 
ATOM   1976 C  CA  . LEU   A 1 283 ? 4.346   1.657   74.520  1.00 33.14  ? 311 LEU   A CA  1 
ATOM   1977 C  C   . LEU   A 1 283 ? 4.849   2.973   75.093  1.00 37.16  ? 311 LEU   A C   1 
ATOM   1978 O  O   . LEU   A 1 283 ? 4.091   3.690   75.761  1.00 35.45  ? 311 LEU   A O   1 
ATOM   1979 C  CB  . LEU   A 1 283 ? 3.266   1.928   73.477  1.00 34.44  ? 311 LEU   A CB  1 
ATOM   1980 C  CG  . LEU   A 1 283 ? 2.375   0.711   73.130  1.00 28.29  ? 311 LEU   A CG  1 
ATOM   1981 C  CD1 . LEU   A 1 283 ? 1.267   1.123   72.182  1.00 30.41  ? 311 LEU   A CD1 1 
ATOM   1982 C  CD2 . LEU   A 1 283 ? 3.175   -0.452  72.564  1.00 30.99  ? 311 LEU   A CD2 1 
ATOM   1983 N  N   . MET   A 1 284 ? 6.117   3.277   74.815  1.00 35.08  ? 312 MET   A N   1 
ATOM   1984 C  CA  . MET   A 1 284 ? 6.733   4.549   75.168  1.00 37.73  ? 312 MET   A CA  1 
ATOM   1985 C  C   . MET   A 1 284 ? 6.204   5.702   74.324  1.00 37.28  ? 312 MET   A C   1 
ATOM   1986 O  O   . MET   A 1 284 ? 6.298   5.666   73.093  1.00 37.58  ? 312 MET   A O   1 
ATOM   1987 C  CB  . MET   A 1 284 ? 8.243   4.476   74.935  1.00 36.86  ? 312 MET   A CB  1 
ATOM   1988 C  CG  . MET   A 1 284 ? 8.899   5.847   75.067  1.00 47.01  ? 312 MET   A CG  1 
ATOM   1989 S  SD  . MET   A 1 284 ? 9.476   5.879   76.765  1.00 73.07  ? 312 MET   A SD  1 
ATOM   1990 C  CE  . MET   A 1 284 ? 11.211  5.446   76.523  1.00 59.16  ? 312 MET   A CE  1 
ATOM   1991 N  N   . SER   A 1 285 ? 5.752   6.760   74.990  1.00 34.90  ? 313 SER   A N   1 
ATOM   1992 C  CA  . SER   A 1 285 ? 5.411   8.009   74.334  1.00 35.60  ? 313 SER   A CA  1 
ATOM   1993 C  C   . SER   A 1 285 ? 6.460   9.078   74.637  1.00 44.54  ? 313 SER   A C   1 
ATOM   1994 O  O   . SER   A 1 285 ? 7.025   9.130   75.733  1.00 40.69  ? 313 SER   A O   1 
ATOM   1995 C  CB  . SER   A 1 285 ? 4.060   8.553   74.805  1.00 35.30  ? 313 SER   A CB  1 
ATOM   1996 O  OG  . SER   A 1 285 ? 3.813   9.846   74.248  1.00 38.64  ? 313 SER   A OG  1 
ATOM   1997 N  N   . GLU   A 1 286 ? 6.695   9.955   73.651  1.00 44.23  ? 314 GLU   A N   1 
ATOM   1998 C  CA  . GLU   A 1 286 ? 7.556   11.117  73.868  1.00 49.42  ? 314 GLU   A CA  1 
ATOM   1999 C  C   . GLU   A 1 286 ? 6.816   12.240  74.575  1.00 48.11  ? 314 GLU   A C   1 
ATOM   2000 O  O   . GLU   A 1 286 ? 7.441   13.229  74.965  1.00 48.32  ? 314 GLU   A O   1 
ATOM   2001 C  CB  . GLU   A 1 286 ? 8.106   11.630  72.535  1.00 43.18  ? 314 GLU   A CB  1 
ATOM   2002 C  CG  . GLU   A 1 286 ? 6.976   12.008  71.600  1.00 46.76  ? 314 GLU   A CG  1 
ATOM   2003 C  CD  . GLU   A 1 286 ? 7.391   12.903  70.453  1.00 51.89  ? 314 GLU   A CD  1 
ATOM   2004 O  OE1 . GLU   A 1 286 ? 8.555   12.814  69.994  1.00 52.89  ? 314 GLU   A OE1 1 
ATOM   2005 O  OE2 . GLU   A 1 286 ? 6.522   13.686  70.000  1.00 57.23  ? 314 GLU   A OE2 1 
ATOM   2006 N  N   . ASP   A 1 287 ? 5.508   12.102  74.762  1.00 46.02  ? 315 ASP   A N   1 
ATOM   2007 C  CA  . ASP   A 1 287 ? 4.695   13.129  75.404  1.00 47.77  ? 315 ASP   A CA  1 
ATOM   2008 C  C   . ASP   A 1 287 ? 3.393   12.471  75.848  1.00 40.78  ? 315 ASP   A C   1 
ATOM   2009 O  O   . ASP   A 1 287 ? 2.379   12.550  75.143  1.00 42.37  ? 315 ASP   A O   1 
ATOM   2010 C  CB  . ASP   A 1 287 ? 4.452   14.303  74.442  1.00 46.03  ? 315 ASP   A CB  1 
ATOM   2011 C  CG  . ASP   A 1 287 ? 3.743   15.483  75.095  1.00 47.69  ? 315 ASP   A CG  1 
ATOM   2012 O  OD1 . ASP   A 1 287 ? 3.285   15.384  76.255  1.00 47.35  ? 315 ASP   A OD1 1 
ATOM   2013 O  OD2 . ASP   A 1 287 ? 3.617   16.521  74.418  1.00 48.35  ? 315 ASP   A OD2 1 
ATOM   2014 N  N   . ILE   A 1 288 ? 3.425   11.805  77.011  1.00 44.06  ? 316 ILE   A N   1 
ATOM   2015 C  CA  . ILE   A 1 288 ? 2.276   11.025  77.457  1.00 44.36  ? 316 ILE   A CA  1 
ATOM   2016 C  C   . ILE   A 1 288 ? 1.045   11.904  77.628  1.00 41.43  ? 316 ILE   A C   1 
ATOM   2017 O  O   . ILE   A 1 288 ? -0.086  11.419  77.532  1.00 41.62  ? 316 ILE   A O   1 
ATOM   2018 C  CB  . ILE   A 1 288 ? 2.596   10.247  78.754  1.00 48.22  ? 316 ILE   A CB  1 
ATOM   2019 C  CG1 . ILE   A 1 288 ? 1.459   9.249   79.062  1.00 43.64  ? 316 ILE   A CG1 1 
ATOM   2020 C  CG2 . ILE   A 1 288 ? 2.827   11.202  79.915  1.00 44.67  ? 316 ILE   A CG2 1 
ATOM   2021 C  CD1 . ILE   A 1 288 ? 1.682   8.364   80.286  1.00 44.76  ? 316 ILE   A CD1 1 
ATOM   2022 N  N   . PHE   A 1 289 ? 1.226   13.199  77.886  1.00 42.75  ? 317 PHE   A N   1 
ATOM   2023 C  CA  . PHE   A 1 289 ? 0.058   14.067  77.963  1.00 47.43  ? 317 PHE   A CA  1 
ATOM   2024 C  C   . PHE   A 1 289 ? -0.582  14.236  76.592  1.00 43.23  ? 317 PHE   A C   1 
ATOM   2025 O  O   . PHE   A 1 289 ? -1.804  14.140  76.457  1.00 44.43  ? 317 PHE   A O   1 
ATOM   2026 C  CB  . PHE   A 1 289 ? 0.433   15.420  78.575  1.00 45.53  ? 317 PHE   A CB  1 
ATOM   2027 C  CG  . PHE   A 1 289 ? 0.954   15.304  79.980  1.00 52.37  ? 317 PHE   A CG  1 
ATOM   2028 C  CD1 . PHE   A 1 289 ? 0.083   15.121  81.043  1.00 52.54  ? 317 PHE   A CD1 1 
ATOM   2029 C  CD2 . PHE   A 1 289 ? 2.320   15.343  80.236  1.00 52.68  ? 317 PHE   A CD2 1 
ATOM   2030 C  CE1 . PHE   A 1 289 ? 0.559   15.002  82.339  1.00 57.16  ? 317 PHE   A CE1 1 
ATOM   2031 C  CE2 . PHE   A 1 289 ? 2.804   15.227  81.530  1.00 53.01  ? 317 PHE   A CE2 1 
ATOM   2032 C  CZ  . PHE   A 1 289 ? 1.925   15.052  82.583  1.00 55.10  ? 317 PHE   A CZ  1 
ATOM   2033 N  N   . ARG   A 1 290 ? 0.227   14.480  75.558  1.00 41.86  ? 318 ARG   A N   1 
ATOM   2034 C  CA  . ARG   A 1 290 ? -0.337  14.600  74.216  1.00 42.47  ? 318 ARG   A CA  1 
ATOM   2035 C  C   . ARG   A 1 290 ? -0.956  13.278  73.763  1.00 39.03  ? 318 ARG   A C   1 
ATOM   2036 O  O   . ARG   A 1 290 ? -2.046  13.254  73.178  1.00 41.07  ? 318 ARG   A O   1 
ATOM   2037 C  CB  . ARG   A 1 290 ? 0.744   15.051  73.235  1.00 45.74  ? 318 ARG   A CB  1 
ATOM   2038 C  CG  . ARG   A 1 290 ? 0.243   15.203  71.811  1.00 48.85  ? 318 ARG   A CG  1 
ATOM   2039 C  CD  . ARG   A 1 290 ? 1.354   15.734  70.915  1.00 56.35  ? 318 ARG   A CD  1 
ATOM   2040 N  NE  . ARG   A 1 290 ? 1.360   15.077  69.610  1.00 59.77  ? 318 ARG   A NE  1 
ATOM   2041 C  CZ  . ARG   A 1 290 ? 2.272   14.196  69.215  1.00 52.09  ? 318 ARG   A CZ  1 
ATOM   2042 N  NH1 . ARG   A 1 290 ? 3.276   13.859  70.018  1.00 52.48  ? 318 ARG   A NH1 1 
ATOM   2043 N  NH2 . ARG   A 1 290 ? 2.181   13.660  68.006  1.00 55.37  ? 318 ARG   A NH2 1 
ATOM   2044 N  N   . THR   A 1 291 ? -0.286  12.166  74.045  1.00 39.98  ? 319 THR   A N   1 
ATOM   2045 C  CA  . THR   A 1 291 ? -0.810  10.870  73.623  1.00 38.39  ? 319 THR   A CA  1 
ATOM   2046 C  C   . THR   A 1 291 ? -2.166  10.584  74.252  1.00 34.65  ? 319 THR   A C   1 
ATOM   2047 O  O   . THR   A 1 291 ? -3.100  10.154  73.569  1.00 36.02  ? 319 THR   A O   1 
ATOM   2048 C  CB  . THR   A 1 291 ? 0.188   9.774   73.976  1.00 35.71  ? 319 THR   A CB  1 
ATOM   2049 O  OG1 . THR   A 1 291 ? 1.378   9.977   73.215  1.00 37.55  ? 319 THR   A OG1 1 
ATOM   2050 C  CG2 . THR   A 1 291 ? -0.399  8.390   73.640  1.00 36.02  ? 319 THR   A CG2 1 
ATOM   2051 N  N   . LEU   A 1 292 ? -2.285  10.796  75.562  1.00 38.49  ? 320 LEU   A N   1 
ATOM   2052 C  CA  . LEU   A 1 292 ? -3.531  10.475  76.247  1.00 38.01  ? 320 LEU   A CA  1 
ATOM   2053 C  C   . LEU   A 1 292 ? -4.636  11.457  75.882  1.00 40.95  ? 320 LEU   A C   1 
ATOM   2054 O  O   . LEU   A 1 292 ? -5.817  11.091  75.893  1.00 36.84  ? 320 LEU   A O   1 
ATOM   2055 C  CB  . LEU   A 1 292 ? -3.303  10.446  77.761  1.00 41.10  ? 320 LEU   A CB  1 
ATOM   2056 C  CG  . LEU   A 1 292 ? -2.901  9.107   78.389  1.00 45.14  ? 320 LEU   A CG  1 
ATOM   2057 C  CD1 . LEU   A 1 292 ? -4.154  8.322   78.712  1.00 49.98  ? 320 LEU   A CD1 1 
ATOM   2058 C  CD2 . LEU   A 1 292 ? -2.049  8.280   77.455  1.00 44.44  ? 320 LEU   A CD2 1 
ATOM   2059 N  N   . ARG   A 1 293 ? -4.284  12.697  75.548  1.00 42.33  ? 321 ARG   A N   1 
ATOM   2060 C  CA  . ARG   A 1 293 ? -5.308  13.614  75.053  1.00 39.50  ? 321 ARG   A CA  1 
ATOM   2061 C  C   . ARG   A 1 293 ? -5.862  13.140  73.712  1.00 36.74  ? 321 ARG   A C   1 
ATOM   2062 O  O   . ARG   A 1 293 ? -7.080  13.124  73.501  1.00 36.78  ? 321 ARG   A O   1 
ATOM   2063 C  CB  . ARG   A 1 293 ? -4.742  15.032  74.939  1.00 42.12  ? 321 ARG   A CB  1 
ATOM   2064 C  CG  . ARG   A 1 293 ? -4.771  15.816  76.239  1.00 44.47  ? 321 ARG   A CG  1 
ATOM   2065 C  CD  . ARG   A 1 293 ? -4.569  17.339  75.989  1.00 45.74  ? 321 ARG   A CD  1 
ATOM   2066 N  NE  . ARG   A 1 293 ? -3.391  17.588  75.153  1.00 46.89  ? 321 ARG   A NE  1 
ATOM   2067 C  CZ  . ARG   A 1 293 ? -2.167  17.799  75.622  1.00 46.97  ? 321 ARG   A CZ  1 
ATOM   2068 N  NH1 . ARG   A 1 293 ? -1.942  17.827  76.933  1.00 50.70  ? 321 ARG   A NH1 1 
ATOM   2069 N  NH2 . ARG   A 1 293 ? -1.159  17.998  74.780  1.00 50.01  ? 321 ARG   A NH2 1 
ATOM   2070 N  N   . GLU   A 1 294 ? -4.978  12.743  72.794  1.00 41.22  ? 322 GLU   A N   1 
ATOM   2071 C  CA  . GLU   A 1 294 ? -5.414  12.275  71.481  1.00 38.97  ? 322 GLU   A CA  1 
ATOM   2072 C  C   . GLU   A 1 294 ? -6.177  10.955  71.575  1.00 37.47  ? 322 GLU   A C   1 
ATOM   2073 O  O   . GLU   A 1 294 ? -7.182  10.770  70.888  1.00 36.49  ? 322 GLU   A O   1 
ATOM   2074 C  CB  . GLU   A 1 294 ? -4.205  12.130  70.549  1.00 40.55  ? 322 GLU   A CB  1 
ATOM   2075 C  CG  . GLU   A 1 294 ? -3.524  13.461  70.181  1.00 41.21  ? 322 GLU   A CG  1 
ATOM   2076 C  CD  . GLU   A 1 294 ? -4.268  14.235  69.093  1.00 47.69  ? 322 GLU   A CD  1 
ATOM   2077 O  OE1 . GLU   A 1 294 ? -5.479  14.014  68.914  1.00 47.53  ? 322 GLU   A OE1 1 
ATOM   2078 O  OE2 . GLU   A 1 294 ? -3.646  15.086  68.420  1.00 56.66  ? 322 GLU   A OE2 1 
ATOM   2079 N  N   . MET   A 1 295 ? -5.702  10.017  72.402  1.00 36.82  ? 323 MET   A N   1 
ATOM   2080 C  CA  . MET   A 1 295 ? -6.377  8.722   72.513  1.00 35.40  ? 323 MET   A CA  1 
ATOM   2081 C  C   . MET   A 1 295 ? -7.731  8.848   73.205  1.00 39.44  ? 323 MET   A C   1 
ATOM   2082 O  O   . MET   A 1 295 ? -8.701  8.176   72.813  1.00 33.54  ? 323 MET   A O   1 
ATOM   2083 C  CB  . MET   A 1 295 ? -5.493  7.719   73.259  1.00 31.38  ? 323 MET   A CB  1 
ATOM   2084 C  CG  . MET   A 1 295 ? -4.260  7.301   72.498  1.00 31.87  ? 323 MET   A CG  1 
ATOM   2085 S  SD  . MET   A 1 295 ? -3.372  5.919   73.305  1.00 34.70  ? 323 MET   A SD  1 
ATOM   2086 C  CE  . MET   A 1 295 ? -4.535  4.573   73.003  1.00 34.68  ? 323 MET   A CE  1 
ATOM   2087 N  N   . ARG   A 1 296 ? -7.818  9.682   74.251  1.00 39.34  ? 324 ARG   A N   1 
ATOM   2088 C  CA  . ARG   A 1 296 ? -9.091  9.824   74.952  1.00 37.31  ? 324 ARG   A CA  1 
ATOM   2089 C  C   . ARG   A 1 296 ? -10.111 10.544  74.094  1.00 39.91  ? 324 ARG   A C   1 
ATOM   2090 O  O   . ARG   A 1 296 ? -11.305 10.217  74.153  1.00 36.28  ? 324 ARG   A O   1 
ATOM   2091 C  CB  . ARG   A 1 296 ? -8.912  10.562  76.276  1.00 44.31  ? 324 ARG   A CB  1 
ATOM   2092 C  CG  . ARG   A 1 296 ? -8.282  9.721   77.362  1.00 44.05  ? 324 ARG   A CG  1 
ATOM   2093 C  CD  . ARG   A 1 296 ? -8.467  10.375  78.708  1.00 47.87  ? 324 ARG   A CD  1 
ATOM   2094 N  NE  . ARG   A 1 296 ? -7.911  9.588   79.811  1.00 46.87  ? 324 ARG   A NE  1 
ATOM   2095 C  CZ  . ARG   A 1 296 ? -8.612  8.705   80.515  1.00 47.33  ? 324 ARG   A CZ  1 
ATOM   2096 N  NH1 . ARG   A 1 296 ? -9.885  8.470   80.209  1.00 49.89  ? 324 ARG   A NH1 1 
ATOM   2097 N  NH2 . ARG   A 1 296 ? -8.039  8.051   81.519  1.00 52.30  ? 324 ARG   A NH2 1 
ATOM   2098 N  N   . LYS   A 1 297 ? -9.649  11.493  73.273  1.00 37.58  ? 325 LYS   A N   1 
ATOM   2099 C  CA  . LYS   A 1 297 ? -10.509 12.138  72.285  1.00 40.64  ? 325 LYS   A CA  1 
ATOM   2100 C  C   . LYS   A 1 297 ? -11.241 11.130  71.425  1.00 37.49  ? 325 LYS   A C   1 
ATOM   2101 O  O   . LYS   A 1 297 ? -12.372 11.387  70.995  1.00 39.14  ? 325 LYS   A O   1 
ATOM   2102 C  CB  . LYS   A 1 297 ? -9.680  13.036  71.363  1.00 41.64  ? 325 LYS   A CB  1 
ATOM   2103 C  CG  . LYS   A 1 297 ? -9.648  14.491  71.725  1.00 51.02  ? 325 LYS   A CG  1 
ATOM   2104 C  CD  . LYS   A 1 297 ? -9.403  15.303  70.472  1.00 50.90  ? 325 LYS   A CD  1 
ATOM   2105 C  CE  . LYS   A 1 297 ? -7.939  15.491  70.206  1.00 46.75  ? 325 LYS   A CE  1 
ATOM   2106 N  NZ  . LYS   A 1 297 ? -7.401  16.639  71.001  1.00 52.65  ? 325 LYS   A NZ  1 
ATOM   2107 N  N   . ARG   A 1 298 ? -10.625 9.977   71.171  1.00 40.62  ? 326 ARG   A N   1 
ATOM   2108 C  CA  . ARG   A 1 298 ? -11.159 9.009   70.222  1.00 35.90  ? 326 ARG   A CA  1 
ATOM   2109 C  C   . ARG   A 1 298 ? -11.763 7.776   70.871  1.00 36.60  ? 326 ARG   A C   1 
ATOM   2110 O  O   . ARG   A 1 298 ? -12.225 6.889   70.146  1.00 35.02  ? 326 ARG   A O   1 
ATOM   2111 C  CB  . ARG   A 1 298 ? -10.060 8.597   69.235  1.00 35.13  ? 326 ARG   A CB  1 
ATOM   2112 C  CG  . ARG   A 1 298 ? -9.576  9.759   68.383  1.00 39.68  ? 326 ARG   A CG  1 
ATOM   2113 C  CD  . ARG   A 1 298 ? -8.192  9.515   67.817  1.00 36.75  ? 326 ARG   A CD  1 
ATOM   2114 N  NE  . ARG   A 1 298 ? -7.823  10.540  66.833  1.00 43.63  ? 326 ARG   A NE  1 
ATOM   2115 C  CZ  . ARG   A 1 298 ? -7.217  11.690  67.118  1.00 43.91  ? 326 ARG   A CZ  1 
ATOM   2116 N  NH1 . ARG   A 1 298 ? -6.915  11.995  68.375  1.00 40.94  ? 326 ARG   A NH1 1 
ATOM   2117 N  NH2 . ARG   A 1 298 ? -6.917  12.545  66.144  1.00 43.49  ? 326 ARG   A NH2 1 
ATOM   2118 N  N   . SER   A 1 299 ? -11.821 7.715   72.207  1.00 36.69  ? 327 SER   A N   1 
ATOM   2119 C  CA  . SER   A 1 299 ? -12.298 6.509   72.885  1.00 35.63  ? 327 SER   A CA  1 
ATOM   2120 C  C   . SER   A 1 299 ? -13.673 6.075   72.387  1.00 40.85  ? 327 SER   A C   1 
ATOM   2121 O  O   . SER   A 1 299 ? -13.908 4.887   72.142  1.00 40.28  ? 327 SER   A O   1 
ATOM   2122 C  CB  . SER   A 1 299 ? -12.332 6.729   74.401  1.00 37.77  ? 327 SER   A CB  1 
ATOM   2123 O  OG  . SER   A 1 299 ? -11.029 6.748   74.967  1.00 37.27  ? 327 SER   A OG  1 
ATOM   2124 N  N   . SER   A 1 300 ? -14.594 7.020   72.214  1.00 41.95  ? 328 SER   A N   1 
ATOM   2125 C  CA  . SER   A 1 300 ? -15.960 6.685   71.850  1.00 44.26  ? 328 SER   A CA  1 
ATOM   2126 C  C   . SER   A 1 300 ? -16.235 6.826   70.354  1.00 43.65  ? 328 SER   A C   1 
ATOM   2127 O  O   . SER   A 1 300 ? -17.387 6.665   69.930  1.00 39.77  ? 328 SER   A O   1 
ATOM   2128 C  CB  . SER   A 1 300 ? -16.932 7.543   72.663  1.00 52.25  ? 328 SER   A CB  1 
ATOM   2129 O  OG  . SER   A 1 300 ? -16.723 7.322   74.052  1.00 58.91  ? 328 SER   A OG  1 
ATOM   2130 N  N   . ILE   A 1 301 ? -15.212 7.104   69.542  1.00 37.11  ? 329 ILE   A N   1 
ATOM   2131 C  CA  . ILE   A 1 301 ? -15.401 7.140   68.091  1.00 34.34  ? 329 ILE   A CA  1 
ATOM   2132 C  C   . ILE   A 1 301 ? -14.391 6.214   67.418  1.00 35.41  ? 329 ILE   A C   1 
ATOM   2133 O  O   . ILE   A 1 301 ? -13.796 6.557   66.389  1.00 32.72  ? 329 ILE   A O   1 
ATOM   2134 C  CB  . ILE   A 1 301 ? -15.297 8.564   67.527  1.00 36.28  ? 329 ILE   A CB  1 
ATOM   2135 C  CG1 . ILE   A 1 301 ? -13.981 9.212   67.978  1.00 35.01  ? 329 ILE   A CG1 1 
ATOM   2136 C  CG2 . ILE   A 1 301 ? -16.532 9.395   67.909  1.00 36.59  ? 329 ILE   A CG2 1 
ATOM   2137 C  CD1 . ILE   A 1 301 ? -13.798 10.599  67.437  1.00 37.45  ? 329 ILE   A CD1 1 
ATOM   2138 N  N   . GLY   A 1 302 ? -14.229 5.021   67.975  1.00 34.31  ? 330 GLY   A N   1 
ATOM   2139 C  CA  . GLY   A 1 302 ? -13.507 3.943   67.323  1.00 35.16  ? 330 GLY   A CA  1 
ATOM   2140 C  C   . GLY   A 1 302 ? -12.201 3.575   67.978  1.00 37.02  ? 330 GLY   A C   1 
ATOM   2141 O  O   . GLY   A 1 302 ? -11.609 2.546   67.606  1.00 31.80  ? 330 GLY   A O   1 
ATOM   2142 N  N   . GLY   A 1 303 ? -11.725 4.376   68.932  1.00 35.10  ? 331 GLY   A N   1 
ATOM   2143 C  CA  . GLY   A 1 303 ? -10.437 4.135   69.553  1.00 32.44  ? 331 GLY   A CA  1 
ATOM   2144 C  C   . GLY   A 1 303 ? -10.482 3.218   70.759  1.00 35.86  ? 331 GLY   A C   1 
ATOM   2145 O  O   . GLY   A 1 303 ? -11.213 2.220   70.760  1.00 39.57  ? 331 GLY   A O   1 
ATOM   2146 N  N   . PHE   A 1 304 ? -9.707  3.534   71.796  1.00 33.46  ? 332 PHE   A N   1 
ATOM   2147 C  CA  . PHE   A 1 304 ? -9.545  2.662   72.951  1.00 36.96  ? 332 PHE   A CA  1 
ATOM   2148 C  C   . PHE   A 1 304 ? -10.080 3.337   74.209  1.00 38.99  ? 332 PHE   A C   1 
ATOM   2149 O  O   . PHE   A 1 304 ? -9.936  4.546   74.383  1.00 38.72  ? 332 PHE   A O   1 
ATOM   2150 C  CB  . PHE   A 1 304 ? -8.062  2.276   73.120  1.00 36.13  ? 332 PHE   A CB  1 
ATOM   2151 C  CG  . PHE   A 1 304 ? -7.543  1.415   72.002  1.00 36.48  ? 332 PHE   A CG  1 
ATOM   2152 C  CD1 . PHE   A 1 304 ? -7.865  0.058   71.944  1.00 36.06  ? 332 PHE   A CD1 1 
ATOM   2153 C  CD2 . PHE   A 1 304 ? -6.761  1.953   70.995  1.00 34.97  ? 332 PHE   A CD2 1 
ATOM   2154 C  CE1 . PHE   A 1 304 ? -7.393  -0.738  70.905  1.00 36.62  ? 332 PHE   A CE1 1 
ATOM   2155 C  CE2 . PHE   A 1 304 ? -6.276  1.165   69.955  1.00 34.27  ? 332 PHE   A CE2 1 
ATOM   2156 C  CZ  . PHE   A 1 304 ? -6.591  -0.181  69.908  1.00 36.45  ? 332 PHE   A CZ  1 
ATOM   2157 N  N   . ASP   A 1 305 ? -10.718 2.557   75.072  1.00 40.64  ? 333 ASP   A N   1 
ATOM   2158 C  CA  . ASP   A 1 305 ? -11.143 3.053   76.371  1.00 41.76  ? 333 ASP   A CA  1 
ATOM   2159 C  C   . ASP   A 1 305 ? -10.015 2.881   77.364  1.00 44.93  ? 333 ASP   A C   1 
ATOM   2160 O  O   . ASP   A 1 305 ? -9.130  2.045   77.184  1.00 39.98  ? 333 ASP   A O   1 
ATOM   2161 C  CB  . ASP   A 1 305 ? -12.373 2.306   76.879  1.00 43.94  ? 333 ASP   A CB  1 
ATOM   2162 C  CG  . ASP   A 1 305 ? -13.536 2.422   75.939  1.00 44.76  ? 333 ASP   A CG  1 
ATOM   2163 O  OD1 . ASP   A 1 305 ? -13.536 3.387   75.149  1.00 41.83  ? 333 ASP   A OD1 1 
ATOM   2164 O  OD2 . ASP   A 1 305 ? -14.431 1.558   75.994  1.00 44.53  ? 333 ASP   A OD2 1 
ATOM   2165 N  N   . PHE   A 1 306 ? -10.057 3.670   78.432  1.00 41.45  ? 334 PHE   A N   1 
ATOM   2166 C  CA  . PHE   A 1 306 ? -9.030  3.565   79.456  1.00 40.89  ? 334 PHE   A CA  1 
ATOM   2167 C  C   . PHE   A 1 306 ? -9.624  3.069   80.769  1.00 44.55  ? 334 PHE   A C   1 
ATOM   2168 O  O   . PHE   A 1 306 ? -10.835 3.138   80.999  1.00 44.87  ? 334 PHE   A O   1 
ATOM   2169 C  CB  . PHE   A 1 306 ? -8.318  4.908   79.646  1.00 41.60  ? 334 PHE   A CB  1 
ATOM   2170 C  CG  . PHE   A 1 306 ? -7.404  5.259   78.508  1.00 39.40  ? 334 PHE   A CG  1 
ATOM   2171 C  CD1 . PHE   A 1 306 ? -6.089  4.829   78.508  1.00 37.44  ? 334 PHE   A CD1 1 
ATOM   2172 C  CD2 . PHE   A 1 306 ? -7.870  5.974   77.416  1.00 41.08  ? 334 PHE   A CD2 1 
ATOM   2173 C  CE1 . PHE   A 1 306 ? -5.242  5.132   77.459  1.00 35.28  ? 334 PHE   A CE1 1 
ATOM   2174 C  CE2 . PHE   A 1 306 ? -7.020  6.291   76.367  1.00 39.67  ? 334 PHE   A CE2 1 
ATOM   2175 C  CZ  . PHE   A 1 306 ? -5.704  5.866   76.390  1.00 36.86  ? 334 PHE   A CZ  1 
ATOM   2176 N  N   . MET   A 1 307 ? -8.743  2.545   81.621  1.00 45.88  ? 335 MET   A N   1 
ATOM   2177 C  CA  . MET   A 1 307 ? -9.043  2.080   82.971  1.00 48.11  ? 335 MET   A CA  1 
ATOM   2178 C  C   . MET   A 1 307 ? -9.864  3.107   83.740  1.00 54.49  ? 335 MET   A C   1 
ATOM   2179 O  O   . MET   A 1 307 ? -9.801  4.307   83.431  1.00 51.22  ? 335 MET   A O   1 
ATOM   2180 C  CB  . MET   A 1 307 ? -7.740  1.818   83.722  1.00 51.76  ? 335 MET   A CB  1 
ATOM   2181 C  CG  . MET   A 1 307 ? -6.986  3.111   84.001  1.00 46.35  ? 335 MET   A CG  1 
ATOM   2182 S  SD  . MET   A 1 307 ? -5.397  2.871   84.803  1.00 51.10  ? 335 MET   A SD  1 
ATOM   2183 C  CE  . MET   A 1 307 ? -5.918  1.933   86.243  1.00 46.73  ? 335 MET   A CE  1 
ATOM   2184 N  N   . PRO   A 1 308 ? -10.622 2.691   84.758  1.00 55.71  ? 336 PRO   A N   1 
ATOM   2185 C  CA  . PRO   A 1 308 ? -11.376 3.667   85.554  1.00 58.66  ? 336 PRO   A CA  1 
ATOM   2186 C  C   . PRO   A 1 308 ? -10.434 4.623   86.275  1.00 62.15  ? 336 PRO   A C   1 
ATOM   2187 O  O   . PRO   A 1 308 ? -9.286  4.290   86.583  1.00 59.34  ? 336 PRO   A O   1 
ATOM   2188 C  CB  . PRO   A 1 308 ? -12.165 2.794   86.540  1.00 58.48  ? 336 PRO   A CB  1 
ATOM   2189 C  CG  . PRO   A 1 308 ? -12.178 1.421   85.915  1.00 61.20  ? 336 PRO   A CG  1 
ATOM   2190 C  CD  . PRO   A 1 308 ? -10.864 1.309   85.206  1.00 56.00  ? 336 PRO   A CD  1 
ATOM   2191 N  N   . SER   A 1 309 ? -10.941 5.805   86.540  1.00 65.46  ? 337 SER   A N   1 
ATOM   2192 C  CA  . SER   A 1 309 ? -10.204 6.844   87.212  1.00 66.11  ? 337 SER   A CA  1 
ATOM   2193 C  C   . SER   A 1 309 ? -9.910  6.496   88.653  1.00 66.96  ? 337 SER   A C   1 
ATOM   2194 O  O   . SER   A 1 309 ? -10.664 5.811   89.300  1.00 65.38  ? 337 SER   A O   1 
ATOM   2195 C  CB  . SER   A 1 309 ? -10.995 8.155   87.143  1.00 65.46  ? 337 SER   A CB  1 
ATOM   2196 O  OG  . SER   A 1 309 ? -11.845 8.218   86.011  1.00 65.27  ? 337 SER   A OG  1 
ATOM   2197 N  N   . PRO   A 1 310 ? -8.775  6.964   89.161  1.00 70.31  ? 338 PRO   A N   1 
ATOM   2198 C  CA  . PRO   A 1 310 ? -8.415  6.772   90.555  1.00 71.43  ? 338 PRO   A CA  1 
ATOM   2199 C  C   . PRO   A 1 310 ? -9.067  7.892   91.370  1.00 76.63  ? 338 PRO   A C   1 
ATOM   2200 O  O   . PRO   A 1 310 ? -9.472  8.890   90.820  1.00 75.51  ? 338 PRO   A O   1 
ATOM   2201 C  CB  . PRO   A 1 310 ? -6.913  6.908   90.549  1.00 69.86  ? 338 PRO   A CB  1 
ATOM   2202 C  CG  . PRO   A 1 310 ? -6.546  7.475   89.245  1.00 69.23  ? 338 PRO   A CG  1 
ATOM   2203 C  CD  . PRO   A 1 310 ? -7.767  7.739   88.456  1.00 66.43  ? 338 PRO   A CD  1 
ATOM   2204 N  N   . PRO   A 1 311 ? -9.162  7.732   92.672  1.00 78.59  ? 339 PRO   A N   1 
ATOM   2205 C  CA  . PRO   A 1 311 ? -9.841  8.791   93.423  1.00 78.60  ? 339 PRO   A CA  1 
ATOM   2206 C  C   . PRO   A 1 311 ? -9.063  10.084  93.525  1.00 77.10  ? 339 PRO   A C   1 
ATOM   2207 O  O   . PRO   A 1 311 ? -7.889  10.139  93.235  1.00 77.79  ? 339 PRO   A O   1 
ATOM   2208 C  CB  . PRO   A 1 311 ? -10.080 8.165   94.779  1.00 79.79  ? 339 PRO   A CB  1 
ATOM   2209 C  CG  . PRO   A 1 311 ? -9.084  7.083   94.889  1.00 79.70  ? 339 PRO   A CG  1 
ATOM   2210 C  CD  . PRO   A 1 311 ? -8.780  6.599   93.514  1.00 76.39  ? 339 PRO   A CD  1 
ATOM   2211 N  N   . PRO   A 1 312 ? -9.722  11.155  93.947  1.00 79.49  ? 340 PRO   A N   1 
ATOM   2212 C  CA  . PRO   A 1 312 ? -8.940  12.401  94.004  1.00 78.31  ? 340 PRO   A CA  1 
ATOM   2213 C  C   . PRO   A 1 312 ? -7.916  12.393  95.116  1.00 77.38  ? 340 PRO   A C   1 
ATOM   2214 O  O   . PRO   A 1 312 ? -6.880  13.060  95.001  1.00 78.57  ? 340 PRO   A O   1 
ATOM   2215 C  CB  . PRO   A 1 312 ? -10.014 13.479  94.220  1.00 79.34  ? 340 PRO   A CB  1 
ATOM   2216 C  CG  . PRO   A 1 312 ? -11.085 12.762  94.971  1.00 80.81  ? 340 PRO   A CG  1 
ATOM   2217 C  CD  . PRO   A 1 312 ? -11.109 11.356  94.416  1.00 81.81  ? 340 PRO   A CD  1 
ATOM   2218 N  N   . THR   A 1 313 ? -8.189  11.644  96.187  1.00 80.12  ? 341 THR   A N   1 
ATOM   2219 C  CA  . THR   A 1 313 ? -7.198  11.414  97.230  1.00 78.05  ? 341 THR   A CA  1 
ATOM   2220 C  C   . THR   A 1 313 ? -5.863  10.983  96.640  1.00 79.07  ? 341 THR   A C   1 
ATOM   2221 O  O   . THR   A 1 313 ? -4.801  11.397  97.122  1.00 79.00  ? 341 THR   A O   1 
ATOM   2222 C  CB  . THR   A 1 313 ? -7.725  10.361  98.207  1.00 81.74  ? 341 THR   A CB  1 
ATOM   2223 O  OG1 . THR   A 1 313 ? -8.262  9.256   97.468  1.00 81.27  ? 341 THR   A OG1 1 
ATOM   2224 C  CG2 . THR   A 1 313 ? -8.825  10.945  99.083  1.00 83.76  ? 341 THR   A CG2 1 
ATOM   2225 N  N   . TYR   A 1 314 ? -5.894  10.162  95.585  1.00 78.11  ? 342 TYR   A N   1 
ATOM   2226 C  CA  . TYR   A 1 314 ? -4.653  9.760   94.929  1.00 76.61  ? 342 TYR   A CA  1 
ATOM   2227 C  C   . TYR   A 1 314 ? -3.910  10.972  94.388  1.00 75.16  ? 342 TYR   A C   1 
ATOM   2228 O  O   . TYR   A 1 314 ? -2.704  11.130  94.612  1.00 75.41  ? 342 TYR   A O   1 
ATOM   2229 C  CB  . TYR   A 1 314 ? -4.932  8.761   93.801  1.00 74.51  ? 342 TYR   A CB  1 
ATOM   2230 C  CG  . TYR   A 1 314 ? -3.680  8.362   93.029  1.00 69.80  ? 342 TYR   A CG  1 
ATOM   2231 C  CD1 . TYR   A 1 314 ? -2.920  7.264   93.415  1.00 69.87  ? 342 TYR   A CD1 1 
ATOM   2232 C  CD2 . TYR   A 1 314 ? -3.261  9.085   91.916  1.00 65.64  ? 342 TYR   A CD2 1 
ATOM   2233 C  CE1 . TYR   A 1 314 ? -1.781  6.899   92.715  1.00 63.24  ? 342 TYR   A CE1 1 
ATOM   2234 C  CE2 . TYR   A 1 314 ? -2.127  8.730   91.215  1.00 62.71  ? 342 TYR   A CE2 1 
ATOM   2235 C  CZ  . TYR   A 1 314 ? -1.389  7.631   91.619  1.00 61.84  ? 342 TYR   A CZ  1 
ATOM   2236 O  OH  . TYR   A 1 314 ? -0.255  7.273   90.928  1.00 58.01  ? 342 TYR   A OH  1 
ATOM   2237 N  N   . TYR   A 1 315 ? -4.613  11.839  93.666  1.00 72.60  ? 343 TYR   A N   1 
ATOM   2238 C  CA  . TYR   A 1 315 ? -3.954  13.006  93.100  1.00 75.05  ? 343 TYR   A CA  1 
ATOM   2239 C  C   . TYR   A 1 315 ? -3.698  14.094  94.137  1.00 78.15  ? 343 TYR   A C   1 
ATOM   2240 O  O   . TYR   A 1 315 ? -2.862  14.974  93.896  1.00 73.12  ? 343 TYR   A O   1 
ATOM   2241 C  CB  . TYR   A 1 315 ? -4.774  13.533  91.920  1.00 74.06  ? 343 TYR   A CB  1 
ATOM   2242 C  CG  . TYR   A 1 315 ? -4.734  12.560  90.770  1.00 71.29  ? 343 TYR   A CG  1 
ATOM   2243 C  CD1 . TYR   A 1 315 ? -5.755  11.638  90.571  1.00 73.36  ? 343 TYR   A CD1 1 
ATOM   2244 C  CD2 . TYR   A 1 315 ? -3.640  12.522  89.917  1.00 70.70  ? 343 TYR   A CD2 1 
ATOM   2245 C  CE1 . TYR   A 1 315 ? -5.697  10.724  89.529  1.00 70.58  ? 343 TYR   A CE1 1 
ATOM   2246 C  CE2 . TYR   A 1 315 ? -3.570  11.617  88.878  1.00 66.39  ? 343 TYR   A CE2 1 
ATOM   2247 C  CZ  . TYR   A 1 315 ? -4.597  10.720  88.687  1.00 67.90  ? 343 TYR   A CZ  1 
ATOM   2248 O  OH  . TYR   A 1 315 ? -4.522  9.816   87.652  1.00 62.06  ? 343 TYR   A OH  1 
ATOM   2249 N  N   . GLN   A 1 316 ? -4.369  14.036  95.290  1.00 78.67  ? 344 GLN   A N   1 
ATOM   2250 C  CA  . GLN   A 1 316 ? -4.085  14.943  96.396  1.00 79.40  ? 344 GLN   A CA  1 
ATOM   2251 C  C   . GLN   A 1 316 ? -2.915  14.479  97.255  1.00 79.28  ? 344 GLN   A C   1 
ATOM   2252 O  O   . GLN   A 1 316 ? -2.560  15.172  98.215  1.00 82.41  ? 344 GLN   A O   1 
ATOM   2253 C  CB  . GLN   A 1 316 ? -5.328  15.120  97.275  1.00 79.72  ? 344 GLN   A CB  1 
ATOM   2254 N  N   . ASN   A 1 317 ? -2.323  13.326  96.948  1.00 76.31  ? 345 ASN   A N   1 
ATOM   2255 C  CA  . ASN   A 1 317 ? -1.074  12.895  97.560  1.00 77.12  ? 345 ASN   A CA  1 
ATOM   2256 C  C   . ASN   A 1 317 ? 0.077   12.901  96.567  1.00 75.93  ? 345 ASN   A C   1 
ATOM   2257 O  O   . ASN   A 1 317 ? 1.194   12.509  96.924  1.00 78.17  ? 345 ASN   A O   1 
ATOM   2258 C  CB  . ASN   A 1 317 ? -1.229  11.492  98.162  1.00 77.45  ? 345 ASN   A CB  1 
ATOM   2259 C  CG  . ASN   A 1 317 ? -2.438  11.379  99.065  1.00 79.72  ? 345 ASN   A CG  1 
ATOM   2260 O  OD1 . ASN   A 1 317 ? -2.853  12.358  99.685  1.00 83.57  ? 345 ASN   A OD1 1 
ATOM   2261 N  ND2 . ASN   A 1 317 ? -3.019  10.184  99.137  1.00 78.92  ? 345 ASN   A ND2 1 
ATOM   2262 N  N   . LEU   A 1 318 ? -0.167  13.351  95.336  1.00 73.86  ? 346 LEU   A N   1 
ATOM   2263 C  CA  . LEU   A 1 318 ? 0.821   13.247  94.270  1.00 74.46  ? 346 LEU   A CA  1 
ATOM   2264 C  C   . LEU   A 1 318 ? 1.942   14.268  94.434  1.00 75.27  ? 346 LEU   A C   1 
ATOM   2265 O  O   . LEU   A 1 318 ? 3.106   13.963  94.149  1.00 73.66  ? 346 LEU   A O   1 
ATOM   2266 C  CB  . LEU   A 1 318 ? 0.128   13.416  92.917  1.00 74.74  ? 346 LEU   A CB  1 
ATOM   2267 C  CG  . LEU   A 1 318 ? 0.811   12.835  91.680  1.00 72.86  ? 346 LEU   A CG  1 
ATOM   2268 C  CD1 . LEU   A 1 318 ? 1.338   11.442  91.969  1.00 67.72  ? 346 LEU   A CD1 1 
ATOM   2269 C  CD2 . LEU   A 1 318 ? -0.167  12.804  90.516  1.00 69.57  ? 346 LEU   A CD2 1 
ATOM   2270 N  N   . LYS   A 1 319 ? 1.607   15.481  94.887  1.00 75.78  ? 347 LYS   A N   1 
ATOM   2271 C  CA  . LYS   A 1 319 ? 2.622   16.512  95.097  1.00 77.46  ? 347 LYS   A CA  1 
ATOM   2272 C  C   . LYS   A 1 319 ? 3.659   16.067  96.124  1.00 76.42  ? 347 LYS   A C   1 
ATOM   2273 O  O   . LYS   A 1 319 ? 4.869   16.172  95.888  1.00 75.66  ? 347 LYS   A O   1 
ATOM   2274 C  CB  . LYS   A 1 319 ? 1.957   17.818  95.533  1.00 74.97  ? 347 LYS   A CB  1 
ATOM   2275 N  N   . LYS   A 1 320 ? 3.202   15.551  97.270  1.00 76.79  ? 348 LYS   A N   1 
ATOM   2276 C  CA  . LYS   A 1 320 ? 4.094   15.057  98.315  1.00 75.57  ? 348 LYS   A CA  1 
ATOM   2277 C  C   . LYS   A 1 320 ? 4.955   13.881  97.866  1.00 79.08  ? 348 LYS   A C   1 
ATOM   2278 O  O   . LYS   A 1 320 ? 5.811   13.438  98.643  1.00 76.54  ? 348 LYS   A O   1 
ATOM   2279 C  CB  . LYS   A 1 320 ? 3.282   14.659  99.552  1.00 74.22  ? 348 LYS   A CB  1 
ATOM   2280 N  N   . ARG   A 1 321 ? 4.756   13.364  96.650  1.00 76.70  ? 349 ARG   A N   1 
ATOM   2281 C  CA  . ARG   A 1 321 ? 5.557   12.270  96.112  1.00 76.12  ? 349 ARG   A CA  1 
ATOM   2282 C  C   . ARG   A 1 321 ? 6.439   12.688  94.943  1.00 74.06  ? 349 ARG   A C   1 
ATOM   2283 O  O   . ARG   A 1 321 ? 7.616   12.321  94.901  1.00 73.29  ? 349 ARG   A O   1 
ATOM   2284 C  CB  . ARG   A 1 321 ? 4.642   11.110  95.674  1.00 74.65  ? 349 ARG   A CB  1 
ATOM   2285 C  CG  . ARG   A 1 321 ? 4.078   10.292  96.826  1.00 75.44  ? 349 ARG   A CG  1 
ATOM   2286 C  CD  . ARG   A 1 321 ? 3.643   8.897   96.384  1.00 75.18  ? 349 ARG   A CD  1 
ATOM   2287 N  NE  . ARG   A 1 321 ? 2.503   8.904   95.470  1.00 74.41  ? 349 ARG   A NE  1 
ATOM   2288 C  CZ  . ARG   A 1 321 ? 2.570   8.554   94.188  1.00 73.46  ? 349 ARG   A CZ  1 
ATOM   2289 N  NH1 . ARG   A 1 321 ? 3.729   8.175   93.658  1.00 67.36  ? 349 ARG   A NH1 1 
ATOM   2290 N  NH2 . ARG   A 1 321 ? 1.479   8.578   93.436  1.00 69.06  ? 349 ARG   A NH2 1 
ATOM   2291 N  N   . VAL   A 1 322 ? 5.906   13.438  93.978  1.00 75.33  ? 350 VAL   A N   1 
ATOM   2292 C  CA  . VAL   A 1 322 ? 6.621   13.654  92.723  1.00 75.79  ? 350 VAL   A CA  1 
ATOM   2293 C  C   . VAL   A 1 322 ? 6.720   15.133  92.380  1.00 74.32  ? 350 VAL   A C   1 
ATOM   2294 O  O   . VAL   A 1 322 ? 7.188   15.496  91.293  1.00 72.13  ? 350 VAL   A O   1 
ATOM   2295 C  CB  . VAL   A 1 322 ? 5.948   12.890  91.568  1.00 73.44  ? 350 VAL   A CB  1 
ATOM   2296 C  CG1 . VAL   A 1 322 ? 5.832   11.409  91.904  1.00 71.35  ? 350 VAL   A CG1 1 
ATOM   2297 C  CG2 . VAL   A 1 322 ? 4.588   13.500  91.253  1.00 72.59  ? 350 VAL   A CG2 1 
ATOM   2298 N  N   . GLY   A 1 323 ? 6.291   15.995  93.302  1.00 76.85  ? 351 GLY   A N   1 
ATOM   2299 C  CA  . GLY   A 1 323 ? 6.298   17.433  93.065  1.00 77.09  ? 351 GLY   A CA  1 
ATOM   2300 C  C   . GLY   A 1 323 ? 7.648   18.009  92.675  1.00 75.31  ? 351 GLY   A C   1 
ATOM   2301 O  O   . GLY   A 1 323 ? 7.701   19.155  92.211  1.00 76.64  ? 351 GLY   A O   1 
ATOM   2302 N  N   . ASP   A 1 324 ? 8.735   17.256  92.852  1.00 75.62  ? 352 ASP   A N   1 
ATOM   2303 C  CA  . ASP   A 1 324 ? 10.052  17.686  92.399  1.00 75.50  ? 352 ASP   A CA  1 
ATOM   2304 C  C   . ASP   A 1 324 ? 10.303  17.374  90.928  1.00 75.76  ? 352 ASP   A C   1 
ATOM   2305 O  O   . ASP   A 1 324 ? 11.248  17.922  90.350  1.00 76.07  ? 352 ASP   A O   1 
ATOM   2306 C  CB  . ASP   A 1 324 ? 11.141  17.031  93.254  1.00 77.00  ? 352 ASP   A CB  1 
ATOM   2307 C  CG  . ASP   A 1 324 ? 11.324  15.558  92.941  1.00 79.19  ? 352 ASP   A CG  1 
ATOM   2308 O  OD1 . ASP   A 1 324 ? 12.485  15.130  92.762  1.00 79.77  ? 352 ASP   A OD1 1 
ATOM   2309 O  OD2 . ASP   A 1 324 ? 10.307  14.831  92.865  1.00 79.68  ? 352 ASP   A OD2 1 
ATOM   2310 N  N   . VAL   A 1 325 ? 9.487   16.514  90.314  1.00 73.78  ? 353 VAL   A N   1 
ATOM   2311 C  CA  . VAL   A 1 325 ? 9.631   16.180  88.907  1.00 71.63  ? 353 VAL   A CA  1 
ATOM   2312 C  C   . VAL   A 1 325 ? 8.591   16.867  88.023  1.00 70.95  ? 353 VAL   A C   1 
ATOM   2313 O  O   . VAL   A 1 325 ? 8.906   17.210  86.876  1.00 69.86  ? 353 VAL   A O   1 
ATOM   2314 C  CB  . VAL   A 1 325 ? 9.596   14.649  88.708  1.00 74.46  ? 353 VAL   A CB  1 
ATOM   2315 C  CG1 . VAL   A 1 325 ? 9.949   14.279  87.266  1.00 68.85  ? 353 VAL   A CG1 1 
ATOM   2316 C  CG2 . VAL   A 1 325 ? 10.542  13.976  89.685  1.00 73.34  ? 353 VAL   A CG2 1 
ATOM   2317 N  N   . LEU   A 1 326 ? 7.366   17.075  88.507  1.00 69.57  ? 354 LEU   A N   1 
ATOM   2318 C  CA  . LEU   A 1 326 ? 6.315   17.652  87.680  1.00 70.42  ? 354 LEU   A CA  1 
ATOM   2319 C  C   . LEU   A 1 326 ? 5.625   18.806  88.395  1.00 70.49  ? 354 LEU   A C   1 
ATOM   2320 O  O   . LEU   A 1 326 ? 5.348   18.736  89.598  1.00 70.44  ? 354 LEU   A O   1 
ATOM   2321 C  CB  . LEU   A 1 326 ? 5.279   16.593  87.274  1.00 70.83  ? 354 LEU   A CB  1 
ATOM   2322 C  CG  . LEU   A 1 326 ? 5.881   15.318  86.688  1.00 67.41  ? 354 LEU   A CG  1 
ATOM   2323 C  CD1 . LEU   A 1 326 ? 5.700   14.156  87.656  1.00 70.77  ? 354 LEU   A CD1 1 
ATOM   2324 C  CD2 . LEU   A 1 326 ? 5.305   15.020  85.316  1.00 63.69  ? 354 LEU   A CD2 1 
ATOM   2325 N  N   . SER   A 1 327 ? 5.338   19.860  87.634  1.00 71.57  ? 355 SER   A N   1 
ATOM   2326 C  CA  . SER   A 1 327 ? 4.695   21.049  88.167  1.00 71.94  ? 355 SER   A CA  1 
ATOM   2327 C  C   . SER   A 1 327 ? 3.280   20.725  88.634  1.00 72.50  ? 355 SER   A C   1 
ATOM   2328 O  O   . SER   A 1 327 ? 2.711   19.680  88.306  1.00 73.00  ? 355 SER   A O   1 
ATOM   2329 C  CB  . SER   A 1 327 ? 4.649   22.151  87.113  1.00 71.44  ? 355 SER   A CB  1 
ATOM   2330 O  OG  . SER   A 1 327 ? 3.650   21.876  86.145  1.00 73.87  ? 355 SER   A OG  1 
ATOM   2331 N  N   . ASP   A 1 328 ? 2.707   21.643  89.415  1.00 72.33  ? 356 ASP   A N   1 
ATOM   2332 C  CA  . ASP   A 1 328 ? 1.338   21.444  89.866  1.00 75.02  ? 356 ASP   A CA  1 
ATOM   2333 C  C   . ASP   A 1 328 ? 0.350   21.546  88.709  1.00 74.27  ? 356 ASP   A C   1 
ATOM   2334 O  O   . ASP   A 1 328 ? -0.740  20.966  88.774  1.00 72.71  ? 356 ASP   A O   1 
ATOM   2335 C  CB  . ASP   A 1 328 ? 1.009   22.431  90.981  1.00 77.00  ? 356 ASP   A CB  1 
ATOM   2336 C  CG  . ASP   A 1 328 ? 1.568   21.986  92.323  1.00 81.48  ? 356 ASP   A CG  1 
ATOM   2337 O  OD1 . ASP   A 1 328 ? 2.798   22.061  92.514  1.00 82.04  ? 356 ASP   A OD1 1 
ATOM   2338 O  OD2 . ASP   A 1 328 ? 0.775   21.540  93.178  1.00 84.29  ? 356 ASP   A OD2 1 
ATOM   2339 N  N   . ASP   A 1 329 ? 0.723   22.251  87.637  1.00 72.84  ? 357 ASP   A N   1 
ATOM   2340 C  CA  . ASP   A 1 329 ? -0.065  22.212  86.407  1.00 71.42  ? 357 ASP   A CA  1 
ATOM   2341 C  C   . ASP   A 1 329 ? -0.042  20.815  85.790  1.00 72.07  ? 357 ASP   A C   1 
ATOM   2342 O  O   . ASP   A 1 329 ? -1.084  20.282  85.387  1.00 70.88  ? 357 ASP   A O   1 
ATOM   2343 C  CB  . ASP   A 1 329 ? 0.462   23.252  85.414  1.00 71.76  ? 357 ASP   A CB  1 
ATOM   2344 N  N   . GLN   A 1 330 ? 1.143   20.201  85.721  1.00 70.69  ? 358 GLN   A N   1 
ATOM   2345 C  CA  . GLN   A 1 330 ? 1.254   18.852  85.177  1.00 69.99  ? 358 GLN   A CA  1 
ATOM   2346 C  C   . GLN   A 1 330 ? 0.571   17.826  86.070  1.00 71.25  ? 358 GLN   A C   1 
ATOM   2347 O  O   . GLN   A 1 330 ? 0.025   16.838  85.564  1.00 71.41  ? 358 GLN   A O   1 
ATOM   2348 C  CB  . GLN   A 1 330 ? 2.723   18.489  84.966  1.00 68.97  ? 358 GLN   A CB  1 
ATOM   2349 C  CG  . GLN   A 1 330 ? 3.329   19.125  83.728  1.00 69.61  ? 358 GLN   A CG  1 
ATOM   2350 C  CD  . GLN   A 1 330 ? 4.750   19.581  83.944  1.00 68.38  ? 358 GLN   A CD  1 
ATOM   2351 O  OE1 . GLN   A 1 330 ? 5.457   19.054  84.799  1.00 72.78  ? 358 GLN   A OE1 1 
ATOM   2352 N  NE2 . GLN   A 1 330 ? 5.177   20.580  83.175  1.00 70.19  ? 358 GLN   A NE2 1 
ATOM   2353 N  N   . ILE   A 1 331 ? 0.573   18.039  87.389  1.00 71.04  ? 359 ILE   A N   1 
ATOM   2354 C  CA  . ILE   A 1 331 ? -0.116  17.109  88.280  1.00 69.88  ? 359 ILE   A CA  1 
ATOM   2355 C  C   . ILE   A 1 331 ? -1.626  17.219  88.103  1.00 69.17  ? 359 ILE   A C   1 
ATOM   2356 O  O   . ILE   A 1 331 ? -2.344  16.211  88.136  1.00 69.01  ? 359 ILE   A O   1 
ATOM   2357 C  CB  . ILE   A 1 331 ? 0.313   17.341  89.740  1.00 71.19  ? 359 ILE   A CB  1 
ATOM   2358 C  CG1 . ILE   A 1 331 ? 1.803   17.028  89.902  1.00 72.46  ? 359 ILE   A CG1 1 
ATOM   2359 C  CG2 . ILE   A 1 331 ? -0.512  16.483  90.687  1.00 70.29  ? 359 ILE   A CG2 1 
ATOM   2360 C  CD1 . ILE   A 1 331 ? 2.345   17.276  91.298  1.00 75.18  ? 359 ILE   A CD1 1 
ATOM   2361 N  N   . LYS   A 1 332 ? -2.137  18.438  87.904  1.00 69.44  ? 360 LYS   A N   1 
ATOM   2362 C  CA  . LYS   A 1 332 ? -3.545  18.589  87.552  1.00 66.62  ? 360 LYS   A CA  1 
ATOM   2363 C  C   . LYS   A 1 332 ? -3.850  17.904  86.222  1.00 65.48  ? 360 LYS   A C   1 
ATOM   2364 O  O   . LYS   A 1 332 ? -4.904  17.273  86.061  1.00 64.09  ? 360 LYS   A O   1 
ATOM   2365 C  CB  . LYS   A 1 332 ? -3.917  20.073  87.496  1.00 66.95  ? 360 LYS   A CB  1 
ATOM   2366 N  N   . GLU   A 1 333 ? -2.931  18.018  85.259  1.00 66.02  ? 361 GLU   A N   1 
ATOM   2367 C  CA  . GLU   A 1 333 ? -3.087  17.351  83.970  1.00 62.85  ? 361 GLU   A CA  1 
ATOM   2368 C  C   . GLU   A 1 333 ? -3.146  15.833  84.136  1.00 64.26  ? 361 GLU   A C   1 
ATOM   2369 O  O   . GLU   A 1 333 ? -3.872  15.146  83.406  1.00 60.77  ? 361 GLU   A O   1 
ATOM   2370 C  CB  . GLU   A 1 333 ? -1.930  17.760  83.058  1.00 64.79  ? 361 GLU   A CB  1 
ATOM   2371 C  CG  . GLU   A 1 333 ? -2.216  17.725  81.576  1.00 62.97  ? 361 GLU   A CG  1 
ATOM   2372 C  CD  . GLU   A 1 333 ? -1.129  18.420  80.778  1.00 64.48  ? 361 GLU   A CD  1 
ATOM   2373 O  OE1 . GLU   A 1 333 ? -1.215  18.432  79.532  1.00 63.71  ? 361 GLU   A OE1 1 
ATOM   2374 O  OE2 . GLU   A 1 333 ? -0.189  18.959  81.403  1.00 68.48  ? 361 GLU   A OE2 1 
ATOM   2375 N  N   . CYS   A 1 334 ? -2.389  15.294  85.097  1.00 64.68  ? 362 CYS   A N   1 
ATOM   2376 C  CA  . CYS   A 1 334 ? -2.457  13.865  85.389  1.00 61.09  ? 362 CYS   A CA  1 
ATOM   2377 C  C   . CYS   A 1 334 ? -3.824  13.477  85.938  1.00 64.94  ? 362 CYS   A C   1 
ATOM   2378 O  O   . CYS   A 1 334 ? -4.364  12.415  85.592  1.00 58.65  ? 362 CYS   A O   1 
ATOM   2379 C  CB  . CYS   A 1 334 ? -1.363  13.478  86.382  1.00 64.70  ? 362 CYS   A CB  1 
ATOM   2380 S  SG  . CYS   A 1 334 ? 0.334   13.569  85.751  1.00 62.09  ? 362 CYS   A SG  1 
ATOM   2381 N  N   . GLU   A 1 335 ? -4.395  14.313  86.809  1.00 61.99  ? 363 GLU   A N   1 
ATOM   2382 C  CA  . GLU   A 1 335 ? -5.713  13.995  87.343  1.00 65.76  ? 363 GLU   A CA  1 
ATOM   2383 C  C   . GLU   A 1 335 ? -6.777  14.060  86.259  1.00 62.14  ? 363 GLU   A C   1 
ATOM   2384 O  O   . GLU   A 1 335 ? -7.740  13.288  86.289  1.00 61.64  ? 363 GLU   A O   1 
ATOM   2385 C  CB  . GLU   A 1 335 ? -6.077  14.935  88.491  1.00 71.14  ? 363 GLU   A CB  1 
ATOM   2386 C  CG  . GLU   A 1 335 ? -7.298  14.469  89.262  1.00 71.97  ? 363 GLU   A CG  1 
ATOM   2387 C  CD  . GLU   A 1 335 ? -7.840  15.518  90.203  1.00 75.82  ? 363 GLU   A CD  1 
ATOM   2388 O  OE1 . GLU   A 1 335 ? -8.654  15.157  91.081  1.00 77.10  ? 363 GLU   A OE1 1 
ATOM   2389 O  OE2 . GLU   A 1 335 ? -7.459  16.700  90.060  1.00 76.33  ? 363 GLU   A OE2 1 
ATOM   2390 N  N   . GLU   A 1 336 ? -6.612  14.960  85.290  1.00 61.14  ? 364 GLU   A N   1 
ATOM   2391 C  CA  . GLU   A 1 336 ? -7.567  15.043  84.191  1.00 62.08  ? 364 GLU   A CA  1 
ATOM   2392 C  C   . GLU   A 1 336 ? -7.485  13.808  83.302  1.00 56.94  ? 364 GLU   A C   1 
ATOM   2393 O  O   . GLU   A 1 336 ? -8.506  13.185  82.989  1.00 59.39  ? 364 GLU   A O   1 
ATOM   2394 C  CB  . GLU   A 1 336 ? -7.318  16.314  83.379  1.00 57.75  ? 364 GLU   A CB  1 
ATOM   2395 N  N   . LEU   A 1 337 ? -6.272  13.430  82.900  1.00 59.22  ? 365 LEU   A N   1 
ATOM   2396 C  CA  . LEU   A 1 337 ? -6.058  12.313  81.989  1.00 55.08  ? 365 LEU   A CA  1 
ATOM   2397 C  C   . LEU   A 1 337 ? -6.061  10.952  82.679  1.00 56.85  ? 365 LEU   A C   1 
ATOM   2398 O  O   . LEU   A 1 337 ? -6.141  9.929   81.988  1.00 55.64  ? 365 LEU   A O   1 
ATOM   2399 C  CB  . LEU   A 1 337 ? -4.743  12.522  81.234  1.00 52.05  ? 365 LEU   A CB  1 
ATOM   2400 C  CG  . LEU   A 1 337 ? -4.790  13.743  80.315  1.00 53.18  ? 365 LEU   A CG  1 
ATOM   2401 C  CD1 . LEU   A 1 337 ? -3.431  14.041  79.714  1.00 50.29  ? 365 LEU   A CD1 1 
ATOM   2402 C  CD2 . LEU   A 1 337 ? -5.848  13.540  79.227  1.00 47.35  ? 365 LEU   A CD2 1 
ATOM   2403 N  N   . GLY   A 1 338 ? -6.023  10.907  84.008  1.00 54.07  ? 366 GLY   A N   1 
ATOM   2404 C  CA  . GLY   A 1 338 ? -5.988  9.650   84.722  1.00 51.83  ? 366 GLY   A CA  1 
ATOM   2405 C  C   . GLY   A 1 338 ? -4.620  9.006   84.812  1.00 55.81  ? 366 GLY   A C   1 
ATOM   2406 O  O   . GLY   A 1 338 ? -4.526  7.840   85.213  1.00 53.44  ? 366 GLY   A O   1 
ATOM   2407 N  N   . ILE   A 1 339 ? -3.559  9.735   84.457  1.00 52.80  ? 367 ILE   A N   1 
ATOM   2408 C  CA  . ILE   A 1 339 ? -2.205  9.199   84.502  1.00 57.02  ? 367 ILE   A CA  1 
ATOM   2409 C  C   . ILE   A 1 339 ? -1.841  8.816   85.932  1.00 56.76  ? 367 ILE   A C   1 
ATOM   2410 O  O   . ILE   A 1 339 ? -2.155  9.534   86.892  1.00 59.29  ? 367 ILE   A O   1 
ATOM   2411 C  CB  . ILE   A 1 339 ? -1.223  10.239  83.935  1.00 55.98  ? 367 ILE   A CB  1 
ATOM   2412 C  CG1 . ILE   A 1 339 ? -1.458  10.455  82.431  1.00 57.65  ? 367 ILE   A CG1 1 
ATOM   2413 C  CG2 . ILE   A 1 339 ? 0.216   9.853   84.225  1.00 54.97  ? 367 ILE   A CG2 1 
ATOM   2414 C  CD1 . ILE   A 1 339 ? -0.393  11.324  81.754  1.00 52.65  ? 367 ILE   A CD1 1 
ATOM   2415 N  N   . LEU   A 1 340 ? -1.181  7.670   86.081  1.00 51.76  ? 368 LEU   A N   1 
ATOM   2416 C  CA  . LEU   A 1 340 ? -0.579  7.271   87.344  1.00 54.52  ? 368 LEU   A CA  1 
ATOM   2417 C  C   . LEU   A 1 340 ? 0.918   7.558   87.313  1.00 54.74  ? 368 LEU   A C   1 
ATOM   2418 O  O   . LEU   A 1 340 ? 1.535   7.607   86.245  1.00 53.94  ? 368 LEU   A O   1 
ATOM   2419 C  CB  . LEU   A 1 340 ? -0.820  5.789   87.627  1.00 53.94  ? 368 LEU   A CB  1 
ATOM   2420 C  CG  . LEU   A 1 340 ? -2.293  5.373   87.694  1.00 56.74  ? 368 LEU   A CG  1 
ATOM   2421 C  CD1 . LEU   A 1 340 ? -2.392  3.875   87.839  1.00 57.76  ? 368 LEU   A CD1 1 
ATOM   2422 C  CD2 . LEU   A 1 340 ? -3.014  6.075   88.840  1.00 61.41  ? 368 LEU   A CD2 1 
ATOM   2423 N  N   . VAL   A 1 341 ? 1.498   7.761   88.496  1.00 56.88  ? 369 VAL   A N   1 
ATOM   2424 C  CA  . VAL   A 1 341 ? 2.902   8.148   88.628  1.00 53.45  ? 369 VAL   A CA  1 
ATOM   2425 C  C   . VAL   A 1 341 ? 3.528   7.342   89.756  1.00 57.33  ? 369 VAL   A C   1 
ATOM   2426 O  O   . VAL   A 1 341 ? 2.959   7.240   90.849  1.00 60.15  ? 369 VAL   A O   1 
ATOM   2427 C  CB  . VAL   A 1 341 ? 3.077   9.656   88.903  1.00 56.73  ? 369 VAL   A CB  1 
ATOM   2428 C  CG1 . VAL   A 1 341 ? 4.544   10.050  88.765  1.00 50.98  ? 369 VAL   A CG1 1 
ATOM   2429 C  CG2 . VAL   A 1 341 ? 2.219   10.493  87.971  1.00 57.16  ? 369 VAL   A CG2 1 
ATOM   2430 N  N   . ASP   A 1 342 ? 4.694   6.763   89.492  1.00 53.94  ? 370 ASP   A N   1 
ATOM   2431 C  CA  . ASP   A 1 342 ? 5.465   6.077   90.517  1.00 58.47  ? 370 ASP   A CA  1 
ATOM   2432 C  C   . ASP   A 1 342 ? 6.926   6.467   90.363  1.00 58.18  ? 370 ASP   A C   1 
ATOM   2433 O  O   . ASP   A 1 342 ? 7.341   7.020   89.340  1.00 54.77  ? 370 ASP   A O   1 
ATOM   2434 C  CB  . ASP   A 1 342 ? 5.293   4.554   90.437  1.00 58.12  ? 370 ASP   A CB  1 
ATOM   2435 C  CG  . ASP   A 1 342 ? 5.880   3.839   91.640  1.00 60.53  ? 370 ASP   A CG  1 
ATOM   2436 O  OD1 . ASP   A 1 342 ? 6.259   4.539   92.604  1.00 65.44  ? 370 ASP   A OD1 1 
ATOM   2437 O  OD2 . ASP   A 1 342 ? 5.966   2.589   91.624  1.00 57.52  ? 370 ASP   A OD2 1 
ATOM   2438 N  N   . ARG   A 1 343 ? 7.712   6.156   91.395  1.00 64.26  ? 371 ARG   A N   1 
ATOM   2439 C  CA  . ARG   A 1 343 ? 9.105   6.563   91.479  1.00 62.79  ? 371 ARG   A CA  1 
ATOM   2440 C  C   . ARG   A 1 343 ? 10.000  5.389   91.844  1.00 65.68  ? 371 ARG   A C   1 
ATOM   2441 O  O   . ARG   A 1 343 ? 9.698   4.623   92.764  1.00 67.58  ? 371 ARG   A O   1 
ATOM   2442 C  CB  . ARG   A 1 343 ? 9.297   7.659   92.513  1.00 68.43  ? 371 ARG   A CB  1 
ATOM   2443 C  CG  . ARG   A 1 343 ? 10.760  7.938   92.789  1.00 71.32  ? 371 ARG   A CG  1 
ATOM   2444 C  CD  . ARG   A 1 343 ? 11.177  9.242   92.168  1.00 69.89  ? 371 ARG   A CD  1 
ATOM   2445 N  NE  . ARG   A 1 343 ? 10.739  10.357  92.995  1.00 75.49  ? 371 ARG   A NE  1 
ATOM   2446 C  CZ  . ARG   A 1 343 ? 11.055  11.624  92.765  1.00 79.25  ? 371 ARG   A CZ  1 
ATOM   2447 N  NH1 . ARG   A 1 343 ? 10.612  12.577  93.576  1.00 80.40  ? 371 ARG   A NH1 1 
ATOM   2448 N  NH2 . ARG   A 1 343 ? 11.820  11.936  91.729  1.00 78.89  ? 371 ARG   A NH2 1 
ATOM   2449 N  N   . ASP   A 1 344 ? 11.125  5.293   91.140  1.00 66.83  ? 372 ASP   A N   1 
ATOM   2450 C  CA  . ASP   A 1 344 ? 12.121  4.244   91.283  1.00 67.32  ? 372 ASP   A CA  1 
ATOM   2451 C  C   . ASP   A 1 344 ? 13.192  4.628   92.297  1.00 75.05  ? 372 ASP   A C   1 
ATOM   2452 O  O   . ASP   A 1 344 ? 13.151  5.687   92.933  1.00 72.09  ? 372 ASP   A O   1 
ATOM   2453 C  CB  . ASP   A 1 344 ? 12.795  3.995   89.939  1.00 67.20  ? 372 ASP   A CB  1 
ATOM   2454 C  CG  . ASP   A 1 344 ? 13.068  2.542   89.675  1.00 68.81  ? 372 ASP   A CG  1 
ATOM   2455 O  OD1 . ASP   A 1 344 ? 12.715  1.700   90.529  1.00 72.77  ? 372 ASP   A OD1 1 
ATOM   2456 O  OD2 . ASP   A 1 344 ? 13.630  2.242   88.597  1.00 68.59  ? 372 ASP   A OD2 1 
ATOM   2457 N  N   . ASP   A 1 345 ? 14.184  3.743   92.426  1.00 76.00  ? 373 ASP   A N   1 
ATOM   2458 C  CA  . ASP   A 1 345 ? 15.488  4.143   92.939  1.00 80.89  ? 373 ASP   A CA  1 
ATOM   2459 C  C   . ASP   A 1 345 ? 16.086  5.265   92.098  1.00 79.45  ? 373 ASP   A C   1 
ATOM   2460 O  O   . ASP   A 1 345 ? 16.772  6.149   92.629  1.00 78.16  ? 373 ASP   A O   1 
ATOM   2461 C  CB  . ASP   A 1 345 ? 16.426  2.929   92.940  1.00 80.61  ? 373 ASP   A CB  1 
ATOM   2462 C  CG  . ASP   A 1 345 ? 17.305  2.859   94.174  1.00 88.74  ? 373 ASP   A CG  1 
ATOM   2463 O  OD1 . ASP   A 1 345 ? 16.862  3.322   95.247  1.00 89.71  ? 373 ASP   A OD1 1 
ATOM   2464 O  OD2 . ASP   A 1 345 ? 18.435  2.328   94.075  1.00 91.69  ? 373 ASP   A OD2 1 
ATOM   2465 N  N   . GLN   A 1 346 ? 15.815  5.257   90.791  1.00 74.07  ? 374 GLN   A N   1 
ATOM   2466 C  CA  . GLN   A 1 346 ? 16.568  6.032   89.816  1.00 75.17  ? 374 GLN   A CA  1 
ATOM   2467 C  C   . GLN   A 1 346 ? 15.733  7.013   89.007  1.00 70.46  ? 374 GLN   A C   1 
ATOM   2468 O  O   . GLN   A 1 346 ? 16.265  8.042   88.582  1.00 68.32  ? 374 GLN   A O   1 
ATOM   2469 C  CB  . GLN   A 1 346 ? 17.279  5.080   88.840  1.00 76.15  ? 374 GLN   A CB  1 
ATOM   2470 C  CG  . GLN   A 1 346 ? 17.838  3.825   89.493  1.00 77.75  ? 374 GLN   A CG  1 
ATOM   2471 C  CD  . GLN   A 1 346 ? 17.657  2.598   88.629  1.00 78.86  ? 374 GLN   A CD  1 
ATOM   2472 O  OE1 . GLN   A 1 346 ? 16.539  2.112   88.445  1.00 80.10  ? 374 GLN   A OE1 1 
ATOM   2473 N  NE2 . GLN   A 1 346 ? 18.757  2.085   88.092  1.00 81.88  ? 374 GLN   A NE2 1 
ATOM   2474 N  N   . GLY   A 1 347 ? 14.458  6.724   88.765  1.00 66.42  ? 375 GLY   A N   1 
ATOM   2475 C  CA  . GLY   A 1 347 ? 13.665  7.598   87.921  1.00 61.41  ? 375 GLY   A CA  1 
ATOM   2476 C  C   . GLY   A 1 347 ? 12.187  7.606   88.241  1.00 59.79  ? 375 GLY   A C   1 
ATOM   2477 O  O   . GLY   A 1 347 ? 11.750  7.009   89.229  1.00 59.49  ? 375 GLY   A O   1 
ATOM   2478 N  N   . THR   A 1 348 ? 11.406  8.282   87.401  1.00 54.92  ? 376 THR   A N   1 
ATOM   2479 C  CA  . THR   A 1 348 ? 9.970   8.422   87.597  1.00 57.37  ? 376 THR   A CA  1 
ATOM   2480 C  C   . THR   A 1 348 ? 9.228   7.792   86.420  1.00 51.44  ? 376 THR   A C   1 
ATOM   2481 O  O   . THR   A 1 348 ? 9.671   7.882   85.269  1.00 50.77  ? 376 THR   A O   1 
ATOM   2482 C  CB  . THR   A 1 348 ? 9.584   9.901   87.739  1.00 55.79  ? 376 THR   A CB  1 
ATOM   2483 O  OG1 . THR   A 1 348 ? 10.529  10.555  88.602  1.00 64.28  ? 376 THR   A OG1 1 
ATOM   2484 C  CG2 . THR   A 1 348 ? 8.178   10.059  88.337  1.00 59.49  ? 376 THR   A CG2 1 
ATOM   2485 N  N   . LEU   A 1 349 ? 8.093   7.165   86.698  1.00 51.31  ? 377 LEU   A N   1 
ATOM   2486 C  CA  . LEU   A 1 349 ? 7.310   6.500   85.658  1.00 50.15  ? 377 LEU   A CA  1 
ATOM   2487 C  C   . LEU   A 1 349 ? 5.901   7.070   85.627  1.00 47.85  ? 377 LEU   A C   1 
ATOM   2488 O  O   . LEU   A 1 349 ? 5.184   7.017   86.632  1.00 49.92  ? 377 LEU   A O   1 
ATOM   2489 C  CB  . LEU   A 1 349 ? 7.273   4.989   85.883  1.00 47.19  ? 377 LEU   A CB  1 
ATOM   2490 C  CG  . LEU   A 1 349 ? 6.316   4.190   84.989  1.00 51.24  ? 377 LEU   A CG  1 
ATOM   2491 C  CD1 . LEU   A 1 349 ? 6.817   4.101   83.553  1.00 48.03  ? 377 LEU   A CD1 1 
ATOM   2492 C  CD2 . LEU   A 1 349 ? 6.104   2.803   85.564  1.00 47.92  ? 377 LEU   A CD2 1 
ATOM   2493 N  N   . LEU   A 1 350 ? 5.508   7.605   84.475  1.00 46.18  ? 378 LEU   A N   1 
ATOM   2494 C  CA  . LEU   A 1 350 ? 4.118   7.945   84.189  1.00 46.40  ? 378 LEU   A CA  1 
ATOM   2495 C  C   . LEU   A 1 350 ? 3.495   6.790   83.410  1.00 45.35  ? 378 LEU   A C   1 
ATOM   2496 O  O   . LEU   A 1 350 ? 4.117   6.277   82.480  1.00 45.22  ? 378 LEU   A O   1 
ATOM   2497 C  CB  . LEU   A 1 350 ? 4.032   9.238   83.377  1.00 45.93  ? 378 LEU   A CB  1 
ATOM   2498 C  CG  . LEU   A 1 350 ? 5.014   10.310  83.878  1.00 54.74  ? 378 LEU   A CG  1 
ATOM   2499 C  CD1 . LEU   A 1 350 ? 5.198   11.437  82.865  1.00 52.34  ? 378 LEU   A CD1 1 
ATOM   2500 C  CD2 . LEU   A 1 350 ? 4.520   10.852  85.204  1.00 55.61  ? 378 LEU   A CD2 1 
ATOM   2501 N  N   . GLN   A 1 351 ? 2.273   6.392   83.778  1.00 47.37  ? 379 GLN   A N   1 
ATOM   2502 C  CA  . GLN   A 1 351 ? 1.674   5.186   83.213  1.00 41.59  ? 379 GLN   A CA  1 
ATOM   2503 C  C   . GLN   A 1 351 ? 0.154   5.232   83.301  1.00 49.06  ? 379 GLN   A C   1 
ATOM   2504 O  O   . GLN   A 1 351 ? -0.415  5.807   84.232  1.00 49.69  ? 379 GLN   A O   1 
ATOM   2505 C  CB  . GLN   A 1 351 ? 2.175   3.919   83.934  1.00 46.01  ? 379 GLN   A CB  1 
ATOM   2506 C  CG  . GLN   A 1 351 ? 1.698   3.812   85.383  1.00 48.32  ? 379 GLN   A CG  1 
ATOM   2507 C  CD  . GLN   A 1 351 ? 2.201   2.577   86.110  1.00 51.60  ? 379 GLN   A CD  1 
ATOM   2508 O  OE1 . GLN   A 1 351 ? 2.201   2.535   87.341  1.00 53.79  ? 379 GLN   A OE1 1 
ATOM   2509 N  NE2 . GLN   A 1 351 ? 2.624   1.560   85.357  1.00 48.39  ? 379 GLN   A NE2 1 
ATOM   2510 N  N   . ILE   A 1 352 ? -0.495  4.574   82.337  1.00 41.70  ? 380 ILE   A N   1 
ATOM   2511 C  CA  . ILE   A 1 352 ? -1.941  4.390   82.341  1.00 41.32  ? 380 ILE   A CA  1 
ATOM   2512 C  C   . ILE   A 1 352 ? -2.230  3.155   81.502  1.00 43.00  ? 380 ILE   A C   1 
ATOM   2513 O  O   . ILE   A 1 352 ? -1.466  2.816   80.593  1.00 41.95  ? 380 ILE   A O   1 
ATOM   2514 C  CB  . ILE   A 1 352 ? -2.685  5.644   81.809  1.00 43.89  ? 380 ILE   A CB  1 
ATOM   2515 C  CG1 . ILE   A 1 352 ? -4.195  5.499   82.008  1.00 43.32  ? 380 ILE   A CG1 1 
ATOM   2516 C  CG2 . ILE   A 1 352 ? -2.341  5.891   80.355  1.00 41.21  ? 380 ILE   A CG2 1 
ATOM   2517 C  CD1 . ILE   A 1 352 ? -4.981  6.772   81.764  1.00 48.41  ? 380 ILE   A CD1 1 
ATOM   2518 N  N   . PHE   A 1 353 ? -3.319  2.466   81.829  1.00 41.74  ? 381 PHE   A N   1 
ATOM   2519 C  CA  . PHE   A 1 353 ? -3.709  1.230   81.165  1.00 41.73  ? 381 PHE   A CA  1 
ATOM   2520 C  C   . PHE   A 1 353 ? -5.000  1.422   80.379  1.00 43.26  ? 381 PHE   A C   1 
ATOM   2521 O  O   . PHE   A 1 353 ? -5.926  2.091   80.846  1.00 43.56  ? 381 PHE   A O   1 
ATOM   2522 C  CB  . PHE   A 1 353 ? -3.892  0.110   82.193  1.00 40.44  ? 381 PHE   A CB  1 
ATOM   2523 C  CG  . PHE   A 1 353 ? -2.670  -0.137  83.022  1.00 45.24  ? 381 PHE   A CG  1 
ATOM   2524 C  CD1 . PHE   A 1 353 ? -2.499  0.506   84.234  1.00 49.13  ? 381 PHE   A CD1 1 
ATOM   2525 C  CD2 . PHE   A 1 353 ? -1.679  -0.994  82.574  1.00 47.21  ? 381 PHE   A CD2 1 
ATOM   2526 C  CE1 . PHE   A 1 353 ? -1.365  0.295   84.993  1.00 50.32  ? 381 PHE   A CE1 1 
ATOM   2527 C  CE2 . PHE   A 1 353 ? -0.530  -1.211  83.330  1.00 45.14  ? 381 PHE   A CE2 1 
ATOM   2528 C  CZ  . PHE   A 1 353 ? -0.379  -0.562  84.539  1.00 48.17  ? 381 PHE   A CZ  1 
ATOM   2529 N  N   . THR   A 1 354 ? -5.073  0.803   79.198  1.00 42.11  ? 382 THR   A N   1 
ATOM   2530 C  CA  . THR   A 1 354 ? -6.337  0.748   78.482  1.00 38.44  ? 382 THR   A CA  1 
ATOM   2531 C  C   . THR   A 1 354 ? -7.232  -0.336  79.072  1.00 39.81  ? 382 THR   A C   1 
ATOM   2532 O  O   . THR   A 1 354 ? -6.804  -1.190  79.852  1.00 39.01  ? 382 THR   A O   1 
ATOM   2533 C  CB  . THR   A 1 354 ? -6.132  0.472   76.987  1.00 37.08  ? 382 THR   A CB  1 
ATOM   2534 O  OG1 . THR   A 1 354 ? -5.769  -0.906  76.785  1.00 36.85  ? 382 THR   A OG1 1 
ATOM   2535 C  CG2 . THR   A 1 354 ? -5.045  1.374   76.407  1.00 38.09  ? 382 THR   A CG2 1 
ATOM   2536 N  N   . LYS   A 1 355 ? -8.501  -0.282  78.694  1.00 38.77  ? 383 LYS   A N   1 
ATOM   2537 C  CA  . LYS   A 1 355 ? -9.370  -1.436  78.828  1.00 38.84  ? 383 LYS   A CA  1 
ATOM   2538 C  C   . LYS   A 1 355 ? -8.934  -2.468  77.788  1.00 40.34  ? 383 LYS   A C   1 
ATOM   2539 O  O   . LYS   A 1 355 ? -8.133  -2.159  76.902  1.00 38.76  ? 383 LYS   A O   1 
ATOM   2540 C  CB  . LYS   A 1 355 ? -10.832 -1.011  78.667  1.00 39.71  ? 383 LYS   A CB  1 
ATOM   2541 C  CG  . LYS   A 1 355 ? -11.390 -0.341  79.916  1.00 44.98  ? 383 LYS   A CG  1 
ATOM   2542 C  CD  . LYS   A 1 355 ? -12.886 -0.059  79.782  1.00 50.49  ? 383 LYS   A CD  1 
ATOM   2543 C  CE  . LYS   A 1 355 ? -13.466 0.471   81.090  1.00 58.52  ? 383 LYS   A CE  1 
ATOM   2544 N  NZ  . LYS   A 1 355 ? -13.914 -0.642  81.978  1.00 58.52  ? 383 LYS   A NZ  1 
ATOM   2545 N  N   . PRO   A 1 356 ? -9.424  -3.713  77.870  1.00 42.10  ? 384 PRO   A N   1 
ATOM   2546 C  CA  . PRO   A 1 356 ? -8.907  -4.749  76.963  1.00 39.49  ? 384 PRO   A CA  1 
ATOM   2547 C  C   . PRO   A 1 356 ? -9.128  -4.357  75.510  1.00 36.23  ? 384 PRO   A C   1 
ATOM   2548 O  O   . PRO   A 1 356 ? -10.096 -3.680  75.173  1.00 37.54  ? 384 PRO   A O   1 
ATOM   2549 C  CB  . PRO   A 1 356 ? -9.711  -5.996  77.348  1.00 41.63  ? 384 PRO   A CB  1 
ATOM   2550 C  CG  . PRO   A 1 356 ? -10.118 -5.749  78.770  1.00 45.08  ? 384 PRO   A CG  1 
ATOM   2551 C  CD  . PRO   A 1 356 ? -10.410 -4.266  78.817  1.00 41.76  ? 384 PRO   A CD  1 
ATOM   2552 N  N   . LEU   A 1 357 ? -8.194  -4.775  74.650  1.00 36.08  ? 385 LEU   A N   1 
ATOM   2553 C  CA  . LEU   A 1 357 ? -8.215  -4.341  73.254  1.00 33.63  ? 385 LEU   A CA  1 
ATOM   2554 C  C   . LEU   A 1 357 ? -9.341  -4.991  72.460  1.00 33.31  ? 385 LEU   A C   1 
ATOM   2555 O  O   . LEU   A 1 357 ? -9.718  -4.466  71.412  1.00 34.59  ? 385 LEU   A O   1 
ATOM   2556 C  CB  . LEU   A 1 357 ? -6.883  -4.675  72.575  1.00 30.92  ? 385 LEU   A CB  1 
ATOM   2557 C  CG  . LEU   A 1 357 ? -5.620  -4.267  73.324  1.00 33.80  ? 385 LEU   A CG  1 
ATOM   2558 C  CD1 . LEU   A 1 357 ? -4.433  -4.578  72.443  1.00 32.60  ? 385 LEU   A CD1 1 
ATOM   2559 C  CD2 . LEU   A 1 357 ? -5.684  -2.768  73.681  1.00 31.31  ? 385 LEU   A CD2 1 
ATOM   2560 N  N   . GLY   A 1 358 ? -9.831  -6.150  72.895  1.00 34.34  ? 386 GLY   A N   1 
ATOM   2561 C  CA  . GLY   A 1 358 ? -10.926 -6.808  72.196  1.00 35.27  ? 386 GLY   A CA  1 
ATOM   2562 C  C   . GLY   A 1 358 ? -12.031 -7.311  73.109  1.00 38.56  ? 386 GLY   A C   1 
ATOM   2563 O  O   . GLY   A 1 358 ? -12.211 -6.786  74.210  1.00 34.92  ? 386 GLY   A O   1 
ATOM   2564 N  N   . ASP   A 1 359 ? -12.774 -8.337  72.649  1.00 35.68  ? 387 ASP   A N   1 
ATOM   2565 C  CA  . ASP   A 1 359 ? -13.960 -8.824  73.361  1.00 37.13  ? 387 ASP   A CA  1 
ATOM   2566 C  C   . ASP   A 1 359 ? -13.626 -9.379  74.742  1.00 36.45  ? 387 ASP   A C   1 
ATOM   2567 O  O   . ASP   A 1 359 ? -14.419 -9.240  75.679  1.00 34.30  ? 387 ASP   A O   1 
ATOM   2568 C  CB  . ASP   A 1 359 ? -14.651 -9.933  72.554  1.00 33.07  ? 387 ASP   A CB  1 
ATOM   2569 C  CG  . ASP   A 1 359 ? -15.257 -9.439  71.266  1.00 34.69  ? 387 ASP   A CG  1 
ATOM   2570 O  OD1 . ASP   A 1 359 ? -15.573 -8.236  71.169  1.00 34.54  ? 387 ASP   A OD1 1 
ATOM   2571 O  OD2 . ASP   A 1 359 ? -15.438 -10.260 70.341  1.00 37.52  ? 387 ASP   A OD2 1 
ATOM   2572 N  N   . ARG   A 1 360 ? -12.501 -10.058 74.871  1.00 32.24  ? 388 ARG   A N   1 
ATOM   2573 C  CA  . ARG   A 1 360 ? -12.159 -10.817 76.067  1.00 38.91  ? 388 ARG   A CA  1 
ATOM   2574 C  C   . ARG   A 1 360 ? -11.341 -9.974  77.037  1.00 39.50  ? 388 ARG   A C   1 
ATOM   2575 O  O   . ARG   A 1 360 ? -10.580 -9.100  76.619  1.00 41.49  ? 388 ARG   A O   1 
ATOM   2576 C  CB  . ARG   A 1 360 ? -11.353 -12.058 75.705  1.00 34.28  ? 388 ARG   A CB  1 
ATOM   2577 C  CG  . ARG   A 1 360 ? -11.952 -12.899 74.600  1.00 41.67  ? 388 ARG   A CG  1 
ATOM   2578 C  CD  . ARG   A 1 360 ? -11.226 -14.255 74.496  1.00 38.41  ? 388 ARG   A CD  1 
ATOM   2579 N  NE  . ARG   A 1 360 ? -11.844 -15.073 73.458  1.00 36.76  ? 388 ARG   A NE  1 
ATOM   2580 C  CZ  . ARG   A 1 360 ? -11.579 -16.357 73.249  1.00 42.46  ? 388 ARG   A CZ  1 
ATOM   2581 N  NH1 . ARG   A 1 360 ? -12.211 -17.002 72.271  1.00 43.70  ? 388 ARG   A NH1 1 
ATOM   2582 N  NH2 . ARG   A 1 360 ? -10.705 -17.000 74.017  1.00 38.91  ? 388 ARG   A NH2 1 
ATOM   2583 N  N   . PRO   A 1 361 ? -11.475 -10.239 78.385  1.00 40.49  ? 389 PRO   A N   1 
ATOM   2584 C  CA  . PRO   A 1 361 ? -10.656 -9.506  79.372  1.00 42.72  ? 389 PRO   A CA  1 
ATOM   2585 C  C   . PRO   A 1 361 ? -9.248  -10.080 79.421  1.00 40.76  ? 389 PRO   A C   1 
ATOM   2586 O  O   . PRO   A 1 361 ? -8.822  -10.715 80.390  1.00 44.11  ? 389 PRO   A O   1 
ATOM   2587 C  CB  . PRO   A 1 361 ? -11.432 -9.719  80.674  1.00 43.05  ? 389 PRO   A CB  1 
ATOM   2588 C  CG  . PRO   A 1 361 ? -12.132 -11.040 80.482  1.00 42.19  ? 389 PRO   A CG  1 
ATOM   2589 C  CD  . PRO   A 1 361 ? -12.478 -11.117 79.021  1.00 38.75  ? 389 PRO   A CD  1 
ATOM   2590 N  N   . THR   A 1 362 ? -8.511  -9.883  78.328  1.00 36.82  ? 390 THR   A N   1 
ATOM   2591 C  CA  . THR   A 1 362 ? -7.199  -10.511 78.197  1.00 38.41  ? 390 THR   A CA  1 
ATOM   2592 C  C   . THR   A 1 362 ? -6.141  -9.461  77.889  1.00 37.04  ? 390 THR   A C   1 
ATOM   2593 O  O   . THR   A 1 362 ? -5.656  -8.788  78.801  1.00 39.94  ? 390 THR   A O   1 
ATOM   2594 C  CB  . THR   A 1 362 ? -7.221  -11.605 77.120  1.00 36.32  ? 390 THR   A CB  1 
ATOM   2595 O  OG1 . THR   A 1 362 ? -7.674  -11.054 75.874  1.00 36.13  ? 390 THR   A OG1 1 
ATOM   2596 C  CG2 . THR   A 1 362 ? -8.169  -12.757 77.531  1.00 37.64  ? 390 THR   A CG2 1 
ATOM   2597 N  N   . ILE   A 1 363 ? -5.803  -9.284  76.612  1.00 36.54  ? 391 ILE   A N   1 
ATOM   2598 C  CA  . ILE   A 1 363 ? -4.743  -8.348  76.242  1.00 33.96  ? 391 ILE   A CA  1 
ATOM   2599 C  C   . ILE   A 1 363 ? -5.205  -6.913  76.454  1.00 38.42  ? 391 ILE   A C   1 
ATOM   2600 O  O   . ILE   A 1 363 ? -6.361  -6.560  76.160  1.00 36.85  ? 391 ILE   A O   1 
ATOM   2601 C  CB  . ILE   A 1 363 ? -4.311  -8.578  74.783  1.00 35.22  ? 391 ILE   A CB  1 
ATOM   2602 C  CG1 . ILE   A 1 363 ? -3.171  -7.633  74.402  1.00 36.27  ? 391 ILE   A CG1 1 
ATOM   2603 C  CG2 . ILE   A 1 363 ? -5.492  -8.370  73.834  1.00 33.86  ? 391 ILE   A CG2 1 
ATOM   2604 C  CD1 . ILE   A 1 363 ? -2.283  -8.149  73.289  1.00 32.33  ? 391 ILE   A CD1 1 
ATOM   2605 N  N   . PHE   A 1 364 ? -4.301  -6.070  76.974  1.00 34.22  ? 392 PHE   A N   1 
ATOM   2606 C  CA  . PHE   A 1 364 ? -4.528  -4.625  77.023  1.00 39.52  ? 392 PHE   A CA  1 
ATOM   2607 C  C   . PHE   A 1 364 ? -3.221  -3.900  76.716  1.00 36.90  ? 392 PHE   A C   1 
ATOM   2608 O  O   . PHE   A 1 364 ? -2.151  -4.514  76.594  1.00 36.39  ? 392 PHE   A O   1 
ATOM   2609 C  CB  . PHE   A 1 364 ? -5.099  -4.161  78.380  1.00 39.88  ? 392 PHE   A CB  1 
ATOM   2610 C  CG  . PHE   A 1 364 ? -4.273  -4.578  79.587  1.00 40.07  ? 392 PHE   A CG  1 
ATOM   2611 C  CD1 . PHE   A 1 364 ? -4.458  -5.824  80.174  1.00 37.62  ? 392 PHE   A CD1 1 
ATOM   2612 C  CD2 . PHE   A 1 364 ? -3.341  -3.710  80.151  1.00 39.39  ? 392 PHE   A CD2 1 
ATOM   2613 C  CE1 . PHE   A 1 364 ? -3.718  -6.194  81.284  1.00 44.91  ? 392 PHE   A CE1 1 
ATOM   2614 C  CE2 . PHE   A 1 364 ? -2.610  -4.076  81.265  1.00 41.35  ? 392 PHE   A CE2 1 
ATOM   2615 C  CZ  . PHE   A 1 364 ? -2.789  -5.324  81.827  1.00 40.65  ? 392 PHE   A CZ  1 
ATOM   2616 N  N   . ILE   A 1 365 ? -3.303  -2.572  76.592  1.00 34.69  ? 393 ILE   A N   1 
ATOM   2617 C  CA  . ILE   A 1 365 ? -2.139  -1.752  76.271  1.00 35.29  ? 393 ILE   A CA  1 
ATOM   2618 C  C   . ILE   A 1 365 ? -1.863  -0.788  77.424  1.00 36.71  ? 393 ILE   A C   1 
ATOM   2619 O  O   . ILE   A 1 365 ? -2.790  -0.322  78.092  1.00 36.11  ? 393 ILE   A O   1 
ATOM   2620 C  CB  . ILE   A 1 365 ? -2.337  -0.999  74.936  1.00 38.56  ? 393 ILE   A CB  1 
ATOM   2621 C  CG1 . ILE   A 1 365 ? -1.986  -1.925  73.765  1.00 34.86  ? 393 ILE   A CG1 1 
ATOM   2622 C  CG2 . ILE   A 1 365 ? -1.474  0.283   74.878  1.00 31.47  ? 393 ILE   A CG2 1 
ATOM   2623 C  CD1 . ILE   A 1 365 ? -2.227  -1.301  72.397  1.00 34.98  ? 393 ILE   A CD1 1 
ATOM   2624 N  N   . GLU   A 1 366 ? -0.582  -0.536  77.686  1.00 39.15  ? 394 GLU   A N   1 
ATOM   2625 C  CA  . GLU   A 1 366 ? -0.130  0.446   78.670  1.00 40.08  ? 394 GLU   A CA  1 
ATOM   2626 C  C   . GLU   A 1 366 ? 0.601   1.562   77.938  1.00 36.57  ? 394 GLU   A C   1 
ATOM   2627 O  O   . GLU   A 1 366 ? 1.438   1.295   77.071  1.00 36.53  ? 394 GLU   A O   1 
ATOM   2628 C  CB  . GLU   A 1 366 ? 0.789   -0.224  79.712  1.00 39.02  ? 394 GLU   A CB  1 
ATOM   2629 C  CG  . GLU   A 1 366 ? 1.428   0.713   80.756  1.00 38.52  ? 394 GLU   A CG  1 
ATOM   2630 C  CD  . GLU   A 1 366 ? 2.430   0.003   81.659  1.00 43.72  ? 394 GLU   A CD  1 
ATOM   2631 O  OE1 . GLU   A 1 366 ? 2.704   -1.196  81.427  1.00 37.53  ? 394 GLU   A OE1 1 
ATOM   2632 O  OE2 . GLU   A 1 366 ? 2.952   0.643   82.604  1.00 43.95  ? 394 GLU   A OE2 1 
ATOM   2633 N  N   . ILE   A 1 367 ? 0.287   2.816   78.265  1.00 35.82  ? 395 ILE   A N   1 
ATOM   2634 C  CA  . ILE   A 1 367 ? 1.058   3.938   77.754  1.00 37.13  ? 395 ILE   A CA  1 
ATOM   2635 C  C   . ILE   A 1 367 ? 1.945   4.419   78.887  1.00 40.55  ? 395 ILE   A C   1 
ATOM   2636 O  O   . ILE   A 1 367 ? 1.517   4.449   80.049  1.00 41.48  ? 395 ILE   A O   1 
ATOM   2637 C  CB  . ILE   A 1 367 ? 0.151   5.073   77.228  1.00 38.12  ? 395 ILE   A CB  1 
ATOM   2638 C  CG1 . ILE   A 1 367 ? -0.929  4.505   76.307  1.00 38.25  ? 395 ILE   A CG1 1 
ATOM   2639 C  CG2 . ILE   A 1 367 ? 0.981   6.105   76.476  1.00 36.65  ? 395 ILE   A CG2 1 
ATOM   2640 C  CD1 . ILE   A 1 367 ? -0.410  3.858   75.038  1.00 36.88  ? 395 ILE   A CD1 1 
ATOM   2641 N  N   . ILE   A 1 368 ? 3.196   4.752   78.566  1.00 38.04  ? 396 ILE   A N   1 
ATOM   2642 C  CA  . ILE   A 1 368 ? 4.185   5.118   79.573  1.00 39.97  ? 396 ILE   A CA  1 
ATOM   2643 C  C   . ILE   A 1 368 ? 5.094   6.209   79.036  1.00 43.56  ? 396 ILE   A C   1 
ATOM   2644 O  O   . ILE   A 1 368 ? 5.279   6.377   77.826  1.00 40.45  ? 396 ILE   A O   1 
ATOM   2645 C  CB  . ILE   A 1 368 ? 5.086   3.952   80.042  1.00 42.21  ? 396 ILE   A CB  1 
ATOM   2646 C  CG1 . ILE   A 1 368 ? 6.048   3.553   78.927  1.00 43.18  ? 396 ILE   A CG1 1 
ATOM   2647 C  CG2 . ILE   A 1 368 ? 4.277   2.729   80.481  1.00 42.42  ? 396 ILE   A CG2 1 
ATOM   2648 C  CD1 . ILE   A 1 368 ? 7.178   2.695   79.406  1.00 44.04  ? 396 ILE   A CD1 1 
ATOM   2649 N  N   . GLN   A 1 369 ? 5.667   6.945   79.982  1.00 41.55  ? 397 GLN   A N   1 
ATOM   2650 C  CA  . GLN   A 1 369 ? 6.822   7.789   79.751  1.00 46.41  ? 397 GLN   A CA  1 
ATOM   2651 C  C   . GLN   A 1 369 ? 7.651   7.736   81.023  1.00 46.50  ? 397 GLN   A C   1 
ATOM   2652 O  O   . GLN   A 1 369 ? 7.104   7.757   82.132  1.00 45.80  ? 397 GLN   A O   1 
ATOM   2653 C  CB  . GLN   A 1 369 ? 6.416   9.229   79.408  1.00 42.20  ? 397 GLN   A CB  1 
ATOM   2654 C  CG  . GLN   A 1 369 ? 7.587   10.118  79.020  1.00 46.57  ? 397 GLN   A CG  1 
ATOM   2655 C  CD  . GLN   A 1 369 ? 7.139   11.289  78.178  1.00 47.93  ? 397 GLN   A CD  1 
ATOM   2656 O  OE1 . GLN   A 1 369 ? 6.029   11.800  78.341  1.00 45.80  ? 397 GLN   A OE1 1 
ATOM   2657 N  NE2 . GLN   A 1 369 ? 7.994   11.714  77.258  1.00 49.94  ? 397 GLN   A NE2 1 
ATOM   2658 N  N   . ARG   A 1 370 ? 8.962   7.611   80.865  1.00 43.24  ? 398 ARG   A N   1 
ATOM   2659 C  CA  . ARG   A 1 370 ? 9.868   7.582   82.004  1.00 48.57  ? 398 ARG   A CA  1 
ATOM   2660 C  C   . ARG   A 1 370 ? 10.771  8.805   81.996  1.00 48.61  ? 398 ARG   A C   1 
ATOM   2661 O  O   . ARG   A 1 370 ? 11.218  9.255   80.935  1.00 48.92  ? 398 ARG   A O   1 
ATOM   2662 C  CB  . ARG   A 1 370 ? 10.715  6.325   82.027  1.00 50.25  ? 398 ARG   A CB  1 
ATOM   2663 C  CG  . ARG   A 1 370 ? 10.054  5.053   81.510  1.00 50.07  ? 398 ARG   A CG  1 
ATOM   2664 C  CD  . ARG   A 1 370 ? 11.129  3.997   81.295  1.00 46.68  ? 398 ARG   A CD  1 
ATOM   2665 N  NE  . ARG   A 1 370 ? 10.564  2.677   81.116  1.00 47.66  ? 398 ARG   A NE  1 
ATOM   2666 C  CZ  . ARG   A 1 370 ? 10.209  1.882   82.123  1.00 45.72  ? 398 ARG   A CZ  1 
ATOM   2667 N  NH1 . ARG   A 1 370 ? 10.376  2.244   83.397  1.00 47.77  ? 398 ARG   A NH1 1 
ATOM   2668 N  NH2 . ARG   A 1 370 ? 9.667   0.697   81.844  1.00 41.76  ? 398 ARG   A NH2 1 
ATOM   2669 N  N   . VAL   A 1 371 ? 11.037  9.325   83.190  1.00 52.23  ? 399 VAL   A N   1 
ATOM   2670 C  CA  . VAL   A 1 371 ? 11.852  10.520  83.389  1.00 50.87  ? 399 VAL   A CA  1 
ATOM   2671 C  C   . VAL   A 1 371 ? 13.041  10.126  84.254  1.00 53.58  ? 399 VAL   A C   1 
ATOM   2672 O  O   . VAL   A 1 371 ? 12.856  9.643   85.377  1.00 53.17  ? 399 VAL   A O   1 
ATOM   2673 C  CB  . VAL   A 1 371 ? 11.036  11.644  84.044  1.00 54.86  ? 399 VAL   A CB  1 
ATOM   2674 C  CG1 . VAL   A 1 371 ? 11.679  13.014  83.794  1.00 56.49  ? 399 VAL   A CG1 1 
ATOM   2675 C  CG2 . VAL   A 1 371 ? 9.580   11.597  83.556  1.00 55.33  ? 399 VAL   A CG2 1 
ATOM   2676 N  N   . GLY   A 1 372 ? 14.250  10.299  83.728  1.00 55.53  ? 400 GLY   A N   1 
ATOM   2677 C  CA  . GLY   A 1 372 ? 15.467  10.141  84.503  1.00 63.86  ? 400 GLY   A CA  1 
ATOM   2678 C  C   . GLY   A 1 372 ? 16.449  9.209   83.826  1.00 63.13  ? 400 GLY   A C   1 
ATOM   2679 O  O   . GLY   A 1 372 ? 16.321  8.882   82.641  1.00 64.58  ? 400 GLY   A O   1 
ATOM   2680 N  N   . CYS   A 1 373 ? 17.454  8.787   84.596  1.00 60.31  ? 401 CYS   A N   1 
ATOM   2681 C  CA  . CYS   A 1 373 ? 18.414  7.751   84.204  1.00 65.40  ? 401 CYS   A CA  1 
ATOM   2682 C  C   . CYS   A 1 373 ? 18.990  7.998   82.809  1.00 65.83  ? 401 CYS   A C   1 
ATOM   2683 O  O   . CYS   A 1 373 ? 18.880  7.170   81.905  1.00 65.87  ? 401 CYS   A O   1 
ATOM   2684 C  CB  . CYS   A 1 373 ? 17.774  6.361   84.270  1.00 65.80  ? 401 CYS   A CB  1 
ATOM   2685 S  SG  . CYS   A 1 373 ? 16.567  6.125   85.594  1.00 71.65  ? 401 CYS   A SG  1 
ATOM   2686 N  N   . MET   A 1 374 ? 19.618  9.158   82.641  1.00 69.70  ? 402 MET   A N   1 
ATOM   2687 C  CA  . MET   A 1 374 ? 20.179  9.554   81.358  1.00 70.58  ? 402 MET   A CA  1 
ATOM   2688 C  C   . MET   A 1 374 ? 21.696  9.400   81.371  1.00 74.02  ? 402 MET   A C   1 
ATOM   2689 O  O   . MET   A 1 374 ? 22.360  9.746   82.355  1.00 71.29  ? 402 MET   A O   1 
ATOM   2690 C  CB  . MET   A 1 374 ? 19.789  10.994  81.018  1.00 69.61  ? 402 MET   A CB  1 
ATOM   2691 C  CG  . MET   A 1 374 ? 18.281  11.203  80.875  1.00 68.05  ? 402 MET   A CG  1 
ATOM   2692 S  SD  . MET   A 1 374 ? 17.723  10.791  79.218  1.00 73.72  ? 402 MET   A SD  1 
ATOM   2693 C  CE  . MET   A 1 374 ? 19.027  11.560  78.249  1.00 69.27  ? 402 MET   A CE  1 
ATOM   2694 N  N   . MET   A 1 375 ? 22.237  8.868   80.276  1.00 75.61  ? 403 MET   A N   1 
ATOM   2695 C  CA  . MET   A 1 375 ? 23.672  8.620   80.158  1.00 76.54  ? 403 MET   A CA  1 
ATOM   2696 C  C   . MET   A 1 375 ? 24.281  9.462   79.041  1.00 76.96  ? 403 MET   A C   1 
ATOM   2697 O  O   . MET   A 1 375 ? 23.725  9.548   77.944  1.00 78.58  ? 403 MET   A O   1 
ATOM   2698 C  CB  . MET   A 1 375 ? 23.947  7.135   79.896  1.00 75.66  ? 403 MET   A CB  1 
ATOM   2699 C  CG  . MET   A 1 375 ? 23.154  6.172   80.770  1.00 75.92  ? 403 MET   A CG  1 
ATOM   2700 S  SD  . MET   A 1 375 ? 23.617  6.205   82.513  1.00 85.87  ? 403 MET   A SD  1 
ATOM   2701 C  CE  . MET   A 1 375 ? 25.363  5.815   82.417  1.00 78.86  ? 403 MET   A CE  1 
ATOM   2702 N  N   . TYR   A 1 383 ? 21.278  9.209   75.991  1.00 72.20  ? 411 TYR   A N   1 
ATOM   2703 C  CA  . TYR   A 1 383 ? 20.191  8.237   75.942  1.00 68.70  ? 411 TYR   A CA  1 
ATOM   2704 C  C   . TYR   A 1 383 ? 19.695  7.908   77.347  1.00 70.24  ? 411 TYR   A C   1 
ATOM   2705 O  O   . TYR   A 1 383 ? 20.331  8.268   78.336  1.00 68.59  ? 411 TYR   A O   1 
ATOM   2706 C  CB  . TYR   A 1 383 ? 20.639  6.956   75.229  1.00 74.19  ? 411 TYR   A CB  1 
ATOM   2707 C  CG  . TYR   A 1 383 ? 21.647  6.137   76.012  1.00 74.29  ? 411 TYR   A CG  1 
ATOM   2708 C  CD1 . TYR   A 1 383 ? 21.239  5.092   76.837  1.00 71.76  ? 411 TYR   A CD1 1 
ATOM   2709 C  CD2 . TYR   A 1 383 ? 23.008  6.417   75.934  1.00 76.51  ? 411 TYR   A CD2 1 
ATOM   2710 C  CE1 . TYR   A 1 383 ? 22.163  4.350   77.559  1.00 75.65  ? 411 TYR   A CE1 1 
ATOM   2711 C  CE2 . TYR   A 1 383 ? 23.937  5.680   76.650  1.00 74.53  ? 411 TYR   A CE2 1 
ATOM   2712 C  CZ  . TYR   A 1 383 ? 23.510  4.650   77.461  1.00 76.06  ? 411 TYR   A CZ  1 
ATOM   2713 O  OH  . TYR   A 1 383 ? 24.440  3.918   78.170  1.00 82.24  ? 411 TYR   A OH  1 
ATOM   2714 N  N   . GLN   A 1 384 ? 18.564  7.209   77.429  1.00 68.65  ? 412 GLN   A N   1 
ATOM   2715 C  CA  . GLN   A 1 384 ? 17.966  6.817   78.698  1.00 66.54  ? 412 GLN   A CA  1 
ATOM   2716 C  C   . GLN   A 1 384 ? 18.165  5.323   78.924  1.00 66.09  ? 412 GLN   A C   1 
ATOM   2717 O  O   . GLN   A 1 384 ? 17.962  4.516   78.010  1.00 68.27  ? 412 GLN   A O   1 
ATOM   2718 C  CB  . GLN   A 1 384 ? 16.473  7.160   78.726  1.00 61.77  ? 412 GLN   A CB  1 
ATOM   2719 C  CG  . GLN   A 1 384 ? 15.799  6.937   80.073  1.00 61.66  ? 412 GLN   A CG  1 
ATOM   2720 C  CD  . GLN   A 1 384 ? 14.348  7.390   80.079  1.00 60.79  ? 412 GLN   A CD  1 
ATOM   2721 O  OE1 . GLN   A 1 384 ? 13.527  6.898   79.303  1.00 52.87  ? 412 GLN   A OE1 1 
ATOM   2722 N  NE2 . GLN   A 1 384 ? 14.030  8.352   80.948  1.00 61.19  ? 412 GLN   A NE2 1 
ATOM   2723 N  N   . SER   A 1 385 ? 18.555  4.952   80.141  1.00 61.91  ? 413 SER   A N   1 
ATOM   2724 C  CA  . SER   A 1 385 ? 18.745  3.539   80.445  1.00 62.04  ? 413 SER   A CA  1 
ATOM   2725 C  C   . SER   A 1 385 ? 17.389  2.851   80.592  1.00 58.69  ? 413 SER   A C   1 
ATOM   2726 O  O   . SER   A 1 385 ? 16.425  3.441   81.087  1.00 53.94  ? 413 SER   A O   1 
ATOM   2727 C  CB  . SER   A 1 385 ? 19.582  3.365   81.715  1.00 62.43  ? 413 SER   A CB  1 
ATOM   2728 O  OG  . SER   A 1 385 ? 18.819  3.610   82.883  1.00 64.72  ? 413 SER   A OG  1 
ATOM   2729 N  N   . GLY   A 1 386 ? 17.317  1.594   80.153  1.00 57.46  ? 414 GLY   A N   1 
ATOM   2730 C  CA  . GLY   A 1 386 ? 16.040  0.907   80.108  1.00 51.35  ? 414 GLY   A CA  1 
ATOM   2731 C  C   . GLY   A 1 386 ? 15.485  0.627   81.493  1.00 54.25  ? 414 GLY   A C   1 
ATOM   2732 O  O   . GLY   A 1 386 ? 16.218  0.461   82.468  1.00 53.00  ? 414 GLY   A O   1 
ATOM   2733 N  N   . GLY   A 1 387 ? 14.156  0.563   81.571  1.00 50.59  ? 415 GLY   A N   1 
ATOM   2734 C  CA  . GLY   A 1 387 ? 13.495  0.287   82.830  1.00 52.08  ? 415 GLY   A CA  1 
ATOM   2735 C  C   . GLY   A 1 387 ? 13.531  1.415   83.833  1.00 49.81  ? 415 GLY   A C   1 
ATOM   2736 O  O   . GLY   A 1 387 ? 13.213  1.193   85.004  1.00 51.62  ? 415 GLY   A O   1 
ATOM   2737 N  N   . CYS   A 1 388 ? 13.904  2.619   83.410  1.00 50.56  ? 416 CYS   A N   1 
ATOM   2738 C  CA  . CYS   A 1 388 ? 14.063  3.752   84.313  1.00 55.92  ? 416 CYS   A CA  1 
ATOM   2739 C  C   . CYS   A 1 388 ? 12.743  4.122   84.974  1.00 55.02  ? 416 CYS   A C   1 
ATOM   2740 O  O   . CYS   A 1 388 ? 11.835  4.622   84.309  1.00 52.46  ? 416 CYS   A O   1 
ATOM   2741 C  CB  . CYS   A 1 388 ? 14.614  4.951   83.544  1.00 55.37  ? 416 CYS   A CB  1 
ATOM   2742 S  SG  . CYS   A 1 388 ? 14.737  6.472   84.506  1.00 64.49  ? 416 CYS   A SG  1 
ATOM   2743 N  N   . GLY   A 1 389 ? 12.623  3.901   86.276  1.00 55.50  ? 417 GLY   A N   1 
ATOM   2744 C  CA  . GLY   A 1 389 ? 11.373  4.137   86.966  1.00 55.93  ? 417 GLY   A CA  1 
ATOM   2745 C  C   . GLY   A 1 389 ? 10.660  2.871   87.365  1.00 55.17  ? 417 GLY   A C   1 
ATOM   2746 O  O   . GLY   A 1 389 ? 9.745   2.924   88.195  1.00 58.85  ? 417 GLY   A O   1 
ATOM   2747 N  N   . GLY   A 1 390 ? 11.064  1.734   86.812  1.00 52.77  ? 418 GLY   A N   1 
ATOM   2748 C  CA  . GLY   A 1 390 ? 10.398  0.490   87.118  1.00 52.81  ? 418 GLY   A CA  1 
ATOM   2749 C  C   . GLY   A 1 390 ? 9.146   0.311   86.278  1.00 50.13  ? 418 GLY   A C   1 
ATOM   2750 O  O   . GLY   A 1 390 ? 9.049   0.793   85.143  1.00 48.59  ? 418 GLY   A O   1 
ATOM   2751 N  N   . PHE   A 1 391 ? 8.163   -0.365  86.872  1.00 48.55  ? 419 PHE   A N   1 
ATOM   2752 C  CA  . PHE   A 1 391 ? 6.935   -0.749  86.192  1.00 47.41  ? 419 PHE   A CA  1 
ATOM   2753 C  C   . PHE   A 1 391 ? 5.694   -0.343  86.986  1.00 52.11  ? 419 PHE   A C   1 
ATOM   2754 O  O   . PHE   A 1 391 ? 4.578   -0.744  86.628  1.00 52.28  ? 419 PHE   A O   1 
ATOM   2755 C  CB  . PHE   A 1 391 ? 6.962   -2.261  85.908  1.00 49.87  ? 419 PHE   A CB  1 
ATOM   2756 C  CG  . PHE   A 1 391 ? 8.196   -2.703  85.135  1.00 48.07  ? 419 PHE   A CG  1 
ATOM   2757 C  CD1 . PHE   A 1 391 ? 9.382   -3.007  85.798  1.00 52.06  ? 419 PHE   A CD1 1 
ATOM   2758 C  CD2 . PHE   A 1 391 ? 8.182   -2.763  83.746  1.00 45.04  ? 419 PHE   A CD2 1 
ATOM   2759 C  CE1 . PHE   A 1 391 ? 10.529  -3.382  85.091  1.00 47.45  ? 419 PHE   A CE1 1 
ATOM   2760 C  CE2 . PHE   A 1 391 ? 9.322   -3.139  83.033  1.00 46.97  ? 419 PHE   A CE2 1 
ATOM   2761 C  CZ  . PHE   A 1 391 ? 10.499  -3.450  83.712  1.00 47.30  ? 419 PHE   A CZ  1 
ATOM   2762 N  N   . GLY   A 1 392 ? 5.854   0.477   88.025  1.00 53.81  ? 420 GLY   A N   1 
ATOM   2763 C  CA  . GLY   A 1 392 ? 4.728   1.013   88.766  1.00 53.65  ? 420 GLY   A CA  1 
ATOM   2764 C  C   . GLY   A 1 392 ? 4.332   0.228   89.994  1.00 58.05  ? 420 GLY   A C   1 
ATOM   2765 O  O   . GLY   A 1 392 ? 3.224   0.424   90.505  1.00 57.70  ? 420 GLY   A O   1 
ATOM   2766 N  N   . LYS   A 1 393 ? 5.216   -0.641  90.491  1.00 55.10  ? 421 LYS   A N   1 
ATOM   2767 C  CA  . LYS   A 1 393 ? 4.907   -1.512  91.623  1.00 59.19  ? 421 LYS   A CA  1 
ATOM   2768 C  C   . LYS   A 1 393 ? 4.311   -0.750  92.806  1.00 63.41  ? 421 LYS   A C   1 
ATOM   2769 O  O   . LYS   A 1 393 ? 3.424   -1.262  93.500  1.00 65.93  ? 421 LYS   A O   1 
ATOM   2770 C  CB  . LYS   A 1 393 ? 6.180   -2.250  92.044  1.00 58.24  ? 421 LYS   A CB  1 
ATOM   2771 C  CG  . LYS   A 1 393 ? 5.976   -3.389  93.023  1.00 65.63  ? 421 LYS   A CG  1 
ATOM   2772 C  CD  . LYS   A 1 393 ? 7.318   -3.995  93.424  1.00 63.87  ? 421 LYS   A CD  1 
ATOM   2773 C  CE  . LYS   A 1 393 ? 7.176   -5.456  93.822  1.00 68.07  ? 421 LYS   A CE  1 
ATOM   2774 N  NZ  . LYS   A 1 393 ? 6.140   -5.653  94.875  1.00 72.96  ? 421 LYS   A NZ  1 
ATOM   2775 N  N   . GLY   A 1 394 ? 4.780   0.476   93.055  1.00 59.88  ? 422 GLY   A N   1 
ATOM   2776 C  CA  . GLY   A 1 394 ? 4.280   1.235   94.189  1.00 61.51  ? 422 GLY   A CA  1 
ATOM   2777 C  C   . GLY   A 1 394 ? 2.848   1.707   94.041  1.00 65.68  ? 422 GLY   A C   1 
ATOM   2778 O  O   . GLY   A 1 394 ? 2.176   1.941   95.052  1.00 68.18  ? 422 GLY   A O   1 
ATOM   2779 N  N   . ASN   A 1 395 ? 2.363   1.846   92.806  1.00 63.34  ? 423 ASN   A N   1 
ATOM   2780 C  CA  . ASN   A 1 395 ? 0.993   2.288   92.582  1.00 65.76  ? 423 ASN   A CA  1 
ATOM   2781 C  C   . ASN   A 1 395 ? -0.041  1.298   93.111  1.00 68.11  ? 423 ASN   A C   1 
ATOM   2782 O  O   . ASN   A 1 395 ? -1.213  1.663   93.249  1.00 67.09  ? 423 ASN   A O   1 
ATOM   2783 C  CB  . ASN   A 1 395 ? 0.773   2.547   91.090  1.00 62.33  ? 423 ASN   A CB  1 
ATOM   2784 C  CG  . ASN   A 1 395 ? 1.190   3.945   90.679  1.00 61.41  ? 423 ASN   A CG  1 
ATOM   2785 O  OD1 . ASN   A 1 395 ? 0.914   4.914   91.386  1.00 63.73  ? 423 ASN   A OD1 1 
ATOM   2786 N  ND2 . ASN   A 1 395 ? 1.867   4.057   89.542  1.00 59.60  ? 423 ASN   A ND2 1 
ATOM   2787 N  N   . PHE   A 1 396 ? 0.359   0.061   93.415  1.00 67.06  ? 424 PHE   A N   1 
ATOM   2788 C  CA  . PHE   A 1 396 ? -0.576  -0.880  94.028  1.00 68.40  ? 424 PHE   A CA  1 
ATOM   2789 C  C   . PHE   A 1 396 ? -0.972  -0.425  95.430  1.00 73.07  ? 424 PHE   A C   1 
ATOM   2790 O  O   . PHE   A 1 396 ? -2.161  -0.400  95.774  1.00 75.13  ? 424 PHE   A O   1 
ATOM   2791 C  CB  . PHE   A 1 396 ? 0.031   -2.281  94.073  1.00 67.90  ? 424 PHE   A CB  1 
ATOM   2792 C  CG  . PHE   A 1 396 ? -0.039  -3.025  92.766  1.00 67.34  ? 424 PHE   A CG  1 
ATOM   2793 C  CD1 . PHE   A 1 396 ? 1.118   -3.328  92.063  1.00 64.86  ? 424 PHE   A CD1 1 
ATOM   2794 C  CD2 . PHE   A 1 396 ? -1.259  -3.432  92.248  1.00 65.89  ? 424 PHE   A CD2 1 
ATOM   2795 C  CE1 . PHE   A 1 396 ? 1.060   -4.017  90.863  1.00 61.35  ? 424 PHE   A CE1 1 
ATOM   2796 C  CE2 . PHE   A 1 396 ? -1.323  -4.123  91.051  1.00 63.22  ? 424 PHE   A CE2 1 
ATOM   2797 C  CZ  . PHE   A 1 396 ? -0.158  -4.415  90.358  1.00 60.70  ? 424 PHE   A CZ  1 
ATOM   2798 N  N   . SER   A 1 397 ? 0.015   -0.058  96.254  1.00 74.20  ? 425 SER   A N   1 
ATOM   2799 C  CA  . SER   A 1 397 ? -0.259  0.342   97.631  1.00 75.90  ? 425 SER   A CA  1 
ATOM   2800 C  C   . SER   A 1 397 ? -0.713  1.792   97.723  1.00 76.97  ? 425 SER   A C   1 
ATOM   2801 O  O   . SER   A 1 397 ? -1.447  2.149   98.651  1.00 79.51  ? 425 SER   A O   1 
ATOM   2802 C  CB  . SER   A 1 397 ? 0.984   0.124   98.500  1.00 78.71  ? 425 SER   A CB  1 
ATOM   2803 O  OG  . SER   A 1 397 ? 0.651   0.108   99.878  1.00 79.61  ? 425 SER   A OG  1 
ATOM   2804 N  N   . GLU   A 1 398 ? -0.292  2.635   96.776  1.00 75.80  ? 426 GLU   A N   1 
ATOM   2805 C  CA  . GLU   A 1 398 ? -0.764  4.016   96.743  1.00 77.39  ? 426 GLU   A CA  1 
ATOM   2806 C  C   . GLU   A 1 398 ? -2.234  4.105   96.358  1.00 77.34  ? 426 GLU   A C   1 
ATOM   2807 O  O   . GLU   A 1 398 ? -2.949  4.987   96.850  1.00 78.88  ? 426 GLU   A O   1 
ATOM   2808 C  CB  . GLU   A 1 398 ? 0.087   4.835   95.771  1.00 74.96  ? 426 GLU   A CB  1 
ATOM   2809 C  CG  . GLU   A 1 398 ? -0.287  6.303   95.672  1.00 77.57  ? 426 GLU   A CG  1 
ATOM   2810 C  CD  . GLU   A 1 398 ? 0.067   7.113   96.920  1.00 81.27  ? 426 GLU   A CD  1 
ATOM   2811 O  OE1 . GLU   A 1 398 ? -0.213  8.325   96.913  1.00 83.43  ? 426 GLU   A OE1 1 
ATOM   2812 O  OE2 . GLU   A 1 398 ? 0.619   6.554   97.887  1.00 83.16  ? 426 GLU   A OE2 1 
ATOM   2813 N  N   . LEU   A 1 399 ? -2.702  3.212   95.483  1.00 77.07  ? 427 LEU   A N   1 
ATOM   2814 C  CA  . LEU   A 1 399 ? -4.108  3.213   95.089  1.00 75.90  ? 427 LEU   A CA  1 
ATOM   2815 C  C   . LEU   A 1 399 ? -4.996  2.615   96.173  1.00 78.39  ? 427 LEU   A C   1 
ATOM   2816 O  O   . LEU   A 1 399 ? -6.100  3.114   96.416  1.00 79.68  ? 427 LEU   A O   1 
ATOM   2817 C  CB  . LEU   A 1 399 ? -4.279  2.458   93.771  1.00 73.88  ? 427 LEU   A CB  1 
ATOM   2818 C  CG  . LEU   A 1 399 ? -3.921  3.287   92.538  1.00 70.76  ? 427 LEU   A CG  1 
ATOM   2819 C  CD1 . LEU   A 1 399 ? -3.714  2.402   91.321  1.00 66.27  ? 427 LEU   A CD1 1 
ATOM   2820 C  CD2 . LEU   A 1 399 ? -5.010  4.317   92.278  1.00 72.10  ? 427 LEU   A CD2 1 
ATOM   2821 N  N   . PHE   A 1 400 ? -4.528  1.555   96.839  1.00 76.99  ? 428 PHE   A N   1 
ATOM   2822 C  CA  . PHE   A 1 400 ? -5.283  0.982   97.951  1.00 77.40  ? 428 PHE   A CA  1 
ATOM   2823 C  C   . PHE   A 1 400 ? -5.549  2.020   99.036  1.00 81.88  ? 428 PHE   A C   1 
ATOM   2824 O  O   . PHE   A 1 400 ? -6.666  2.103   99.562  1.00 81.82  ? 428 PHE   A O   1 
ATOM   2825 C  CB  . PHE   A 1 400 ? -4.529  -0.213  98.531  1.00 75.68  ? 428 PHE   A CB  1 
ATOM   2826 N  N   . LYS   A 1 401 ? -4.536  2.827   99.373  1.00 83.01  ? 429 LYS   A N   1 
ATOM   2827 C  CA  . LYS   A 1 401 ? -4.692  3.823   100.428 1.00 82.74  ? 429 LYS   A CA  1 
ATOM   2828 C  C   . LYS   A 1 401 ? -5.701  4.894   100.039 1.00 85.12  ? 429 LYS   A C   1 
ATOM   2829 O  O   . LYS   A 1 401 ? -6.624  5.200   100.804 1.00 88.77  ? 429 LYS   A O   1 
ATOM   2830 C  CB  . LYS   A 1 401 ? -3.340  4.448   100.775 1.00 82.79  ? 429 LYS   A CB  1 
ATOM   2831 C  CG  . LYS   A 1 401 ? -2.361  3.441   101.340 1.00 80.44  ? 429 LYS   A CG  1 
ATOM   2832 C  CD  . LYS   A 1 401 ? -1.390  4.070   102.331 1.00 82.93  ? 429 LYS   A CD  1 
ATOM   2833 C  CE  . LYS   A 1 401 ? -0.150  4.614   101.646 1.00 81.32  ? 429 LYS   A CE  1 
ATOM   2834 N  NZ  . LYS   A 1 401 ? 1.012   4.633   102.575 1.00 82.00  ? 429 LYS   A NZ  1 
ATOM   2835 N  N   . SER   A 1 402 ? -5.540  5.476   98.850  1.00 84.11  ? 430 SER   A N   1 
ATOM   2836 C  CA  . SER   A 1 402 ? -6.465  6.510   98.395  1.00 85.09  ? 430 SER   A CA  1 
ATOM   2837 C  C   . SER   A 1 402 ? -7.903  6.009   98.347  1.00 86.66  ? 430 SER   A C   1 
ATOM   2838 O  O   . SER   A 1 402 ? -8.840  6.792   98.539  1.00 89.86  ? 430 SER   A O   1 
ATOM   2839 C  CB  . SER   A 1 402 ? -6.038  7.028   97.016  1.00 82.25  ? 430 SER   A CB  1 
ATOM   2840 O  OG  . SER   A 1 402 ? -4.651  7.306   96.984  1.00 80.54  ? 430 SER   A OG  1 
ATOM   2841 N  N   . ILE   A 1 403 ? -8.098  4.715   98.092  1.00 86.27  ? 431 ILE   A N   1 
ATOM   2842 C  CA  . ILE   A 1 403 ? -9.442  4.142   98.141  1.00 89.64  ? 431 ILE   A CA  1 
ATOM   2843 C  C   . ILE   A 1 403 ? -10.015 4.263   99.548  1.00 92.26  ? 431 ILE   A C   1 
ATOM   2844 O  O   . ILE   A 1 403 ? -11.155 4.704   99.738  1.00 94.78  ? 431 ILE   A O   1 
ATOM   2845 C  CB  . ILE   A 1 403 ? -9.423  2.678   97.662  1.00 85.22  ? 431 ILE   A CB  1 
ATOM   2846 N  N   . GLU   A 1 404 ? -9.227  3.881   100.557 1.00 90.30  ? 432 GLU   A N   1 
ATOM   2847 C  CA  . GLU   A 1 404 ? -9.664  4.049   101.940 1.00 91.40  ? 432 GLU   A CA  1 
ATOM   2848 C  C   . GLU   A 1 404 ? -9.813  5.524   102.300 1.00 93.89  ? 432 GLU   A C   1 
ATOM   2849 O  O   . GLU   A 1 404 ? -10.794 5.917   102.943 1.00 96.06  ? 432 GLU   A O   1 
ATOM   2850 C  CB  . GLU   A 1 404 ? -8.681  3.360   102.885 1.00 90.98  ? 432 GLU   A CB  1 
ATOM   2851 N  N   . GLU   A 1 405 ? -8.855  6.359   101.881 1.00 92.83  ? 433 GLU   A N   1 
ATOM   2852 C  CA  . GLU   A 1 405 ? -8.891  7.777   102.232 1.00 92.28  ? 433 GLU   A CA  1 
ATOM   2853 C  C   . GLU   A 1 405 ? -10.086 8.496   101.615 1.00 94.91  ? 433 GLU   A C   1 
ATOM   2854 O  O   . GLU   A 1 405 ? -10.571 9.482   102.183 1.00 96.74  ? 433 GLU   A O   1 
ATOM   2855 C  CB  . GLU   A 1 405 ? -7.594  8.460   101.800 1.00 88.90  ? 433 GLU   A CB  1 
ATOM   2856 N  N   . TYR   A 1 406 ? -10.574 8.034   100.461 1.00 94.45  ? 434 TYR   A N   1 
ATOM   2857 C  CA  . TYR   A 1 406 ? -11.707 8.716   99.843  1.00 93.08  ? 434 TYR   A CA  1 
ATOM   2858 C  C   . TYR   A 1 406 ? -13.017 8.362   100.536 1.00 96.46  ? 434 TYR   A C   1 
ATOM   2859 O  O   . TYR   A 1 406 ? -13.892 9.222   100.687 1.00 97.54  ? 434 TYR   A O   1 
ATOM   2860 C  CB  . TYR   A 1 406 ? -11.785 8.390   98.352  1.00 90.48  ? 434 TYR   A CB  1 
ATOM   2861 C  CG  . TYR   A 1 406 ? -12.700 9.331   97.605  1.00 90.41  ? 434 TYR   A CG  1 
ATOM   2862 C  CD1 . TYR   A 1 406 ? -12.591 10.704  97.778  1.00 88.73  ? 434 TYR   A CD1 1 
ATOM   2863 C  CD2 . TYR   A 1 406 ? -13.673 8.855   96.732  1.00 90.55  ? 434 TYR   A CD2 1 
ATOM   2864 C  CE1 . TYR   A 1 406 ? -13.421 11.579  97.113  1.00 88.96  ? 434 TYR   A CE1 1 
ATOM   2865 C  CE2 . TYR   A 1 406 ? -14.513 9.728   96.052  1.00 88.28  ? 434 TYR   A CE2 1 
ATOM   2866 C  CZ  . TYR   A 1 406 ? -14.377 11.093  96.247  1.00 91.16  ? 434 TYR   A CZ  1 
ATOM   2867 O  OH  . TYR   A 1 406 ? -15.195 11.985  95.586  1.00 89.38  ? 434 TYR   A OH  1 
ATOM   2868 N  N   . GLU   A 1 407 ? -13.169 7.108   100.969 1.00 96.23  ? 435 GLU   A N   1 
ATOM   2869 C  CA  . GLU   A 1 407 ? -14.362 6.716   101.708 1.00 99.56  ? 435 GLU   A CA  1 
ATOM   2870 C  C   . GLU   A 1 407 ? -14.437 7.363   103.085 1.00 100.65 ? 435 GLU   A C   1 
ATOM   2871 O  O   . GLU   A 1 407 ? -15.488 7.283   103.731 1.00 103.71 ? 435 GLU   A O   1 
ATOM   2872 C  CB  . GLU   A 1 407 ? -14.423 5.193   101.844 1.00 99.40  ? 435 GLU   A CB  1 
ATOM   2873 N  N   . LYS   A 1 408 ? -13.359 7.989   103.547 1.00 98.36  ? 436 LYS   A N   1 
ATOM   2874 C  CA  . LYS   A 1 408 ? -13.387 8.747   104.790 1.00 99.29  ? 436 LYS   A CA  1 
ATOM   2875 C  C   . LYS   A 1 408 ? -14.278 9.975   104.635 1.00 99.34  ? 436 LYS   A C   1 
ATOM   2876 O  O   . LYS   A 1 408 ? -14.382 10.543  103.548 1.00 99.98  ? 436 LYS   A O   1 
ATOM   2877 C  CB  . LYS   A 1 408 ? -11.974 9.165   105.200 1.00 98.91  ? 436 LYS   A CB  1 
HETATM 2878 CO CO  . CO    B 2 .   ? 3.663   -2.773  82.544  1.00 42.94  ? 501 CO    A CO  1 
HETATM 2879 C  C10 . A1LW7 C 3 .   ? 4.531   -4.943  84.818  1.00 44.94  ? 502 A1LW7 A C10 1 
HETATM 2880 C  C13 . A1LW7 C 3 .   ? 4.295   -6.700  87.149  1.00 48.28  ? 502 A1LW7 A C13 1 
HETATM 2881 C  C20 . A1LW7 C 3 .   ? -2.251  -2.786  88.220  1.00 58.03  ? 502 A1LW7 A C20 1 
HETATM 2882 C  C24 . A1LW7 C 3 .   ? -3.453  -1.346  89.753  1.00 59.60  ? 502 A1LW7 A C24 1 
HETATM 2883 C  C28 . A1LW7 C 3 .   ? -4.392  -0.476  88.908  1.00 61.30  ? 502 A1LW7 A C28 1 
HETATM 2884 C  C01 . A1LW7 C 3 .   ? 1.054   -2.502  86.784  1.00 51.57  ? 502 A1LW7 A C01 1 
HETATM 2885 C  C02 . A1LW7 C 3 .   ? -0.084  -2.229  87.522  1.00 55.42  ? 502 A1LW7 A C02 1 
HETATM 2886 C  C03 . A1LW7 C 3 .   ? -1.145  -3.078  87.482  1.00 55.17  ? 502 A1LW7 A C03 1 
HETATM 2887 C  C04 . A1LW7 C 3 .   ? -1.075  -4.231  86.698  1.00 54.03  ? 502 A1LW7 A C04 1 
HETATM 2888 C  C05 . A1LW7 C 3 .   ? 0.052   -4.508  85.945  1.00 52.54  ? 502 A1LW7 A C05 1 
HETATM 2889 C  C06 . A1LW7 C 3 .   ? 1.129   -3.633  86.013  1.00 50.65  ? 502 A1LW7 A C06 1 
HETATM 2890 C  C07 . A1LW7 C 3 .   ? 2.428   -3.757  85.237  1.00 47.63  ? 502 A1LW7 A C07 1 
HETATM 2891 C  C08 . A1LW7 C 3 .   ? 3.580   -4.646  85.688  1.00 43.83  ? 502 A1LW7 A C08 1 
HETATM 2892 C  C11 . A1LW7 C 3 .   ? 5.638   -5.944  85.157  1.00 47.22  ? 502 A1LW7 A C11 1 
HETATM 2893 C  C12 . A1LW7 C 3 .   ? 5.672   -6.320  86.635  1.00 52.84  ? 502 A1LW7 A C12 1 
HETATM 2894 C  C14 . A1LW7 C 3 .   ? 3.441   -5.451  86.984  1.00 51.38  ? 502 A1LW7 A C14 1 
HETATM 2895 C  C18 . A1LW7 C 3 .   ? -1.222  -0.844  88.986  1.00 60.68  ? 502 A1LW7 A C18 1 
HETATM 2896 C  C23 . A1LW7 C 3 .   ? 0.995   -0.220  88.301  1.00 57.55  ? 502 A1LW7 A C23 1 
HETATM 2897 F  F29 . A1LW7 C 3 .   ? -3.766  0.660   88.469  1.00 59.59  ? 502 A1LW7 A F29 1 
HETATM 2898 F  F30 . A1LW7 C 3 .   ? -5.460  -0.117  89.681  1.00 62.58  ? 502 A1LW7 A F30 1 
HETATM 2899 F  F31 . A1LW7 C 3 .   ? -4.815  -1.184  87.814  1.00 63.66  ? 502 A1LW7 A F31 1 
HETATM 2900 N  N17 . A1LW7 C 3 .   ? -0.127  -1.132  88.258  1.00 60.37  ? 502 A1LW7 A N17 1 
HETATM 2901 N  N19 . A1LW7 C 3 .   ? -2.285  -1.682  88.963  1.00 56.57  ? 502 A1LW7 A N19 1 
HETATM 2902 N  N25 . A1LW7 C 3 .   ? 0.075   -5.734  85.150  1.00 52.65  ? 502 A1LW7 A N25 1 
HETATM 2903 O  O09 . A1LW7 C 3 .   ? 2.515   -3.094  84.253  1.00 44.77  ? 502 A1LW7 A O09 1 
HETATM 2904 O  O15 . A1LW7 C 3 .   ? 4.604   -4.245  83.605  1.00 40.25  ? 502 A1LW7 A O15 1 
HETATM 2905 O  O16 . A1LW7 C 3 .   ? 2.710   -5.115  87.854  1.00 52.60  ? 502 A1LW7 A O16 1 
HETATM 2906 O  O21 . A1LW7 C 3 .   ? -3.186  -3.516  88.208  1.00 57.64  ? 502 A1LW7 A O21 1 
HETATM 2907 O  O22 . A1LW7 C 3 .   ? -1.231  0.143   89.644  1.00 60.22  ? 502 A1LW7 A O22 1 
HETATM 2908 O  O26 . A1LW7 C 3 .   ? 1.053   -6.049  84.577  1.00 54.99  ? 502 A1LW7 A O26 1 
HETATM 2909 O  O27 . A1LW7 C 3 .   ? -1.037  -6.596  85.104  1.00 53.05  ? 502 A1LW7 A O27 1 
HETATM 2910 O  O   . HOH   D 4 .   ? 22.593  -13.039 66.685  1.00 50.74  ? 601 HOH   A O   1 
HETATM 2911 O  O   . HOH   D 4 .   ? 8.209   -1.594  88.747  1.00 62.47  ? 602 HOH   A O   1 
HETATM 2912 O  O   . HOH   D 4 .   ? 19.260  -0.428  82.581  1.00 50.43  ? 603 HOH   A O   1 
HETATM 2913 O  O   . HOH   D 4 .   ? 19.162  -5.453  74.238  1.00 46.07  ? 604 HOH   A O   1 
HETATM 2914 O  O   . HOH   D 4 .   ? -13.548 -5.731  75.798  1.00 50.33  ? 605 HOH   A O   1 
HETATM 2915 O  O   . HOH   D 4 .   ? 26.280  -16.158 71.191  1.00 53.96  ? 606 HOH   A O   1 
HETATM 2916 O  O   . HOH   D 4 .   ? 3.781   -21.727 84.375  1.00 47.81  ? 607 HOH   A O   1 
HETATM 2917 O  O   . HOH   D 4 .   ? 19.954  -13.116 57.029  1.00 49.12  ? 608 HOH   A O   1 
HETATM 2918 O  O   . HOH   D 4 .   ? 9.337   -12.374 53.069  1.00 58.46  ? 609 HOH   A O   1 
HETATM 2919 O  O   . HOH   D 4 .   ? -2.170  5.595   57.251  1.00 44.69  ? 610 HOH   A O   1 
HETATM 2920 O  O   . HOH   D 4 .   ? 12.629  -1.183  76.653  1.00 37.76  ? 611 HOH   A O   1 
HETATM 2921 O  O   . HOH   D 4 .   ? -1.488  -21.003 88.688  1.00 57.43  ? 612 HOH   A O   1 
HETATM 2922 O  O   . HOH   D 4 .   ? 7.160   -11.315 78.802  1.00 42.80  ? 613 HOH   A O   1 
HETATM 2923 O  O   . HOH   D 4 .   ? 26.195  -11.876 77.014  1.00 50.21  ? 614 HOH   A O   1 
HETATM 2924 O  O   . HOH   D 4 .   ? 17.096  -3.221  66.820  1.00 48.21  ? 615 HOH   A O   1 
HETATM 2925 O  O   . HOH   D 4 .   ? 21.455  -10.453 80.236  1.00 50.71  ? 616 HOH   A O   1 
HETATM 2926 O  O   . HOH   D 4 .   ? 19.629  -7.561  54.451  1.00 54.93  ? 617 HOH   A O   1 
HETATM 2927 O  O   . HOH   D 4 .   ? 0.157   -27.590 42.575  1.00 67.61  ? 618 HOH   A O   1 
HETATM 2928 O  O   . HOH   D 4 .   ? -7.596  -12.640 73.854  1.00 40.52  ? 619 HOH   A O   1 
HETATM 2929 O  O   . HOH   D 4 .   ? 2.491   -14.717 60.326  1.00 37.09  ? 620 HOH   A O   1 
HETATM 2930 O  O   . HOH   D 4 .   ? 4.483   -13.123 48.632  1.00 46.85  ? 621 HOH   A O   1 
HETATM 2931 O  O   . HOH   D 4 .   ? -6.423  -8.648  51.880  1.00 41.47  ? 622 HOH   A O   1 
HETATM 2932 O  O   . HOH   D 4 .   ? -4.458  -19.457 51.298  1.00 38.94  ? 623 HOH   A O   1 
HETATM 2933 O  O   . HOH   D 4 .   ? 3.744   -10.343 49.445  1.00 45.66  ? 624 HOH   A O   1 
HETATM 2934 O  O   . HOH   D 4 .   ? -11.557 -2.170  73.158  1.00 37.17  ? 625 HOH   A O   1 
HETATM 2935 O  O   . HOH   D 4 .   ? 0.987   -14.975 43.844  1.00 51.66  ? 626 HOH   A O   1 
HETATM 2936 O  O   . HOH   D 4 .   ? 4.833   -23.389 68.172  1.00 53.40  ? 627 HOH   A O   1 
HETATM 2937 O  O   . HOH   D 4 .   ? 1.028   7.668   68.079  1.00 36.17  ? 628 HOH   A O   1 
HETATM 2938 O  O   . HOH   D 4 .   ? 4.584   -1.070  83.810  1.00 39.08  ? 629 HOH   A O   1 
HETATM 2939 O  O   . HOH   D 4 .   ? -7.478  -4.310  53.527  1.00 57.76  ? 630 HOH   A O   1 
HETATM 2940 O  O   . HOH   D 4 .   ? 7.752   1.825   89.587  1.00 57.28  ? 631 HOH   A O   1 
HETATM 2941 O  O   . HOH   D 4 .   ? 2.671   -23.380 63.771  1.00 55.14  ? 632 HOH   A O   1 
HETATM 2942 O  O   . HOH   D 4 .   ? -12.295 -11.620 56.853  1.00 39.60  ? 633 HOH   A O   1 
HETATM 2943 O  O   . HOH   D 4 .   ? 3.903   -16.813 61.630  1.00 38.06  ? 634 HOH   A O   1 
HETATM 2944 O  O   . HOH   D 4 .   ? -0.998  -18.280 74.067  1.00 37.63  ? 635 HOH   A O   1 
HETATM 2945 O  O   . HOH   D 4 .   ? 2.764   7.978   64.317  1.00 47.81  ? 636 HOH   A O   1 
HETATM 2946 O  O   . HOH   D 4 .   ? -11.200 7.924   77.375  1.00 45.17  ? 637 HOH   A O   1 
HETATM 2947 O  O   . HOH   D 4 .   ? 14.675  11.644  81.442  1.00 57.79  ? 638 HOH   A O   1 
HETATM 2948 O  O   . HOH   D 4 .   ? -10.037 -12.610 56.781  1.00 47.91  ? 639 HOH   A O   1 
HETATM 2949 O  O   . HOH   D 4 .   ? -7.121  -22.063 85.846  1.00 64.28  ? 640 HOH   A O   1 
HETATM 2950 O  O   . HOH   D 4 .   ? -9.106  -14.921 95.002  1.00 70.51  ? 641 HOH   A O   1 
HETATM 2951 O  O   . HOH   D 4 .   ? -14.003 -14.135 77.442  1.00 41.81  ? 642 HOH   A O   1 
HETATM 2952 O  O   . HOH   D 4 .   ? 12.978  0.813   78.840  1.00 46.75  ? 643 HOH   A O   1 
HETATM 2953 O  O   . HOH   D 4 .   ? -8.777  -8.035  74.896  1.00 40.02  ? 644 HOH   A O   1 
HETATM 2954 O  O   . HOH   D 4 .   ? -8.308  6.613   83.816  1.00 52.15  ? 645 HOH   A O   1 
HETATM 2955 O  O   . HOH   D 4 .   ? -4.394  -9.960  83.518  1.00 61.07  ? 646 HOH   A O   1 
HETATM 2956 O  O   . HOH   D 4 .   ? -8.034  5.974   71.319  1.00 38.26  ? 647 HOH   A O   1 
HETATM 2957 O  O   . HOH   D 4 .   ? 20.278  -7.852  62.125  1.00 46.85  ? 648 HOH   A O   1 
HETATM 2958 O  O   . HOH   D 4 .   ? 11.214  10.188  78.346  1.00 56.18  ? 649 HOH   A O   1 
HETATM 2959 O  O   . HOH   D 4 .   ? 1.777   -21.967 50.909  1.00 45.80  ? 650 HOH   A O   1 
HETATM 2960 O  O   . HOH   D 4 .   ? -2.707  -20.896 76.091  1.00 43.95  ? 651 HOH   A O   1 
HETATM 2961 O  O   . HOH   D 4 .   ? -12.553 -21.624 47.183  1.00 57.81  ? 652 HOH   A O   1 
HETATM 2962 O  O   . HOH   D 4 .   ? -6.326  -8.849  81.495  1.00 48.30  ? 653 HOH   A O   1 
HETATM 2963 O  O   . HOH   D 4 .   ? -3.826  -20.771 87.030  1.00 56.12  ? 654 HOH   A O   1 
HETATM 2964 O  O   . HOH   D 4 .   ? 4.213   -12.204 46.547  1.00 55.58  ? 655 HOH   A O   1 
HETATM 2965 O  O   . HOH   D 4 .   ? -12.099 5.518   78.865  1.00 47.46  ? 656 HOH   A O   1 
HETATM 2966 O  O   . HOH   D 4 .   ? 12.227  -0.831  71.852  1.00 42.79  ? 657 HOH   A O   1 
HETATM 2967 O  O   . HOH   D 4 .   ? -12.561 -3.340  76.458  1.00 45.59  ? 658 HOH   A O   1 
HETATM 2968 O  O   . HOH   D 4 .   ? -3.482  14.240  65.744  1.00 53.87  ? 659 HOH   A O   1 
HETATM 2969 O  O   . HOH   D 4 .   ? -14.392 9.780   72.726  1.00 49.56  ? 660 HOH   A O   1 
HETATM 2970 O  O   . HOH   D 4 .   ? -8.190  -10.046 83.059  1.00 55.78  ? 661 HOH   A O   1 
HETATM 2971 O  O   . HOH   D 4 .   ? 10.168  13.709  75.577  1.00 48.35  ? 662 HOH   A O   1 
HETATM 2972 O  O   . HOH   D 4 .   ? 10.829  -20.979 58.617  1.00 67.96  ? 663 HOH   A O   1 
HETATM 2973 O  O   . HOH   D 4 .   ? 8.802   -16.707 59.714  1.00 55.23  ? 664 HOH   A O   1 
HETATM 2974 O  O   . HOH   D 4 .   ? 15.539  -23.308 78.685  1.00 44.06  ? 665 HOH   A O   1 
HETATM 2975 O  O   . HOH   D 4 .   ? 4.528   -21.035 71.797  1.00 37.21  ? 666 HOH   A O   1 
HETATM 2976 O  O   . HOH   D 4 .   ? 9.645   -0.673  69.235  1.00 36.88  ? 667 HOH   A O   1 
HETATM 2977 O  O   . HOH   D 4 .   ? 4.147   -18.192 63.828  1.00 38.55  ? 668 HOH   A O   1 
HETATM 2978 O  O   . HOH   D 4 .   ? -0.992  -13.928 73.410  1.00 32.97  ? 669 HOH   A O   1 
HETATM 2979 O  O   . HOH   D 4 .   ? -9.709  -0.137  74.807  1.00 43.13  ? 670 HOH   A O   1 
HETATM 2980 O  O   . HOH   D 4 .   ? 10.949  -24.899 83.353  1.00 50.95  ? 671 HOH   A O   1 
HETATM 2981 O  O   . HOH   D 4 .   ? -10.058 -16.254 50.811  1.00 39.69  ? 672 HOH   A O   1 
HETATM 2982 O  O   . HOH   D 4 .   ? -1.052  -17.952 95.553  1.00 61.68  ? 673 HOH   A O   1 
HETATM 2983 O  O   . HOH   D 4 .   ? 10.832  -18.594 60.228  1.00 46.96  ? 674 HOH   A O   1 
HETATM 2984 O  O   . HOH   D 4 .   ? -2.794  -15.983 73.815  1.00 35.14  ? 675 HOH   A O   1 
HETATM 2985 O  O   . HOH   D 4 .   ? 4.367   -23.226 58.179  1.00 58.67  ? 676 HOH   A O   1 
HETATM 2986 O  O   . HOH   D 4 .   ? 14.182  -2.595  65.641  1.00 51.61  ? 677 HOH   A O   1 
HETATM 2987 O  O   . HOH   D 4 .   ? -7.519  -16.562 62.550  1.00 42.10  ? 678 HOH   A O   1 
HETATM 2988 O  O   . HOH   D 4 .   ? -2.493  -11.692 73.549  1.00 34.93  ? 679 HOH   A O   1 
HETATM 2989 O  O   . HOH   D 4 .   ? 21.365  -12.078 58.507  1.00 52.28  ? 680 HOH   A O   1 
HETATM 2990 O  O   . HOH   D 4 .   ? -3.916  -22.854 69.755  1.00 57.25  ? 681 HOH   A O   1 
HETATM 2991 O  O   . HOH   D 4 .   ? -2.338  0.199   49.381  1.00 52.23  ? 682 HOH   A O   1 
HETATM 2992 O  O   . HOH   D 4 .   ? 27.353  -15.178 77.038  1.00 63.78  ? 683 HOH   A O   1 
HETATM 2993 O  O   . HOH   D 4 .   ? 21.893  -5.822  74.503  1.00 48.98  ? 684 HOH   A O   1 
HETATM 2994 O  O   . HOH   D 4 .   ? -2.213  12.837  64.379  1.00 46.52  ? 685 HOH   A O   1 
HETATM 2995 O  O   . HOH   D 4 .   ? -10.389 -24.218 51.549  1.00 48.89  ? 686 HOH   A O   1 
HETATM 2996 O  O   . HOH   D 4 .   ? -5.075  -12.358 73.917  1.00 50.42  ? 687 HOH   A O   1 
HETATM 2997 O  O   . HOH   D 4 .   ? -10.197 -10.723 72.732  1.00 52.11  ? 688 HOH   A O   1 
HETATM 2998 O  O   . HOH   D 4 .   ? 3.575   -22.411 69.742  1.00 49.83  ? 689 HOH   A O   1 
HETATM 2999 O  O   . HOH   D 4 .   ? -8.768  -26.054 50.323  1.00 58.80  ? 690 HOH   A O   1 
HETATM 3000 O  O   . HOH   D 4 .   ? 8.221   -3.008  68.064  1.00 13.73  ? 691 HOH   A O   1 
HETATM 3001 O  O   . HOH   D 4 .   ? -9.732  -2.144  52.992  1.00 54.20  ? 692 HOH   A O   1 
HETATM 3002 O  O   . HOH   D 4 .   ? -6.787  -3.359  82.717  1.00 57.76  ? 693 HOH   A O   1 
HETATM 3003 O  O   . HOH   D 4 .   ? 4.271   -24.474 60.388  1.00 55.71  ? 694 HOH   A O   1 
HETATM 3004 O  O   . HOH   D 4 .   ? -5.734  -3.388  84.903  1.00 61.43  ? 695 HOH   A O   1 
HETATM 3005 O  O   . HOH   D 4 .   ? -10.268 -8.963  84.700  1.00 57.96  ? 696 HOH   A O   1 
HETATM 3006 O  O   . HOH   D 4 .   ? -4.244  -22.231 85.277  1.00 60.80  ? 697 HOH   A O   1 
HETATM 3007 O  O   . HOH   D 4 .   ? -9.770  -7.217  83.318  1.00 63.11  ? 698 HOH   A O   1 
HETATM 3008 O  O   . HOH   D 4 .   ? 1.441   -22.777 80.646  1.00 46.52  ? 699 HOH   A O   1 
# 
