data_9JC9
# 
_entry.id   9JC9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9JC9         pdb_00009jc9 10.2210/pdb9jc9/pdb 
WWPDB D_1300050865 ?            ?                   
# 
_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       2025-04-02 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9JC9 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              wenshanyew@nus.edu.sg 
_pdbx_contact_author.name_first         'Wen Shan' 
_pdbx_contact_author.name_last          Yew 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3021-0469 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xue, B.'    1 0000-0002-5172-2519 
'Ling, L.H.' 2 0000-0003-1310-0046 
'Jia, X.'    3 0000-0003-0133-8321 
'Yew, W.S.'  4 0000-0002-3021-0469 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Sustain Chem Eng' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2168-0485 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            13 
_citation.language                  ? 
_citation.page_first                2830 
_citation.page_last                 2844 
_citation.title                     
'Sustainable Biosynthesis of Diverse Fatty Acid Esters of Hydroxy Fatty Acids (FAHFAs) for Industrial Production' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acssuschemeng.4c08793 
_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 'Ling, L.H.'     1  ? 
primary 'Chua, E.T.'     2  ? 
primary 'Xue, B.'        3  ? 
primary 'Jia, X.'        4  ? 
primary 'Chow, J.Y.'     5  ? 
primary 'Yang, R.L.'     6  ? 
primary 'Lim, Y.P.'      7  ? 
primary 'Han, P.'        8  ? 
primary 'Xie, H.'        9  ? 
primary 'Tan, C.H.'      10 ? 
primary 'Nguyen, G.K.T.' 11 ? 
primary 'Yew, W.S.'      12 ? 
# 
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 Lipase                                                                                    48347.188 1   3.1.1.3 
S200A ? ? 
2 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   1   ?       
?     ? ? 
3 non-polymer syn 'PALMITIC ACID'                                                                           256.424   1   ?       
?     ? ? 
4 water       nat water                                                                                     18.015    185 ?       
?     ? ? 
# 
_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       
;VMHHHHHHVPMERRAPFPDPNDDPFYKTPSNIGTYANGQVIQSRKAPTDIGNQNGADSFQLSYRTTNTQKEAQANVATVF
IPSKPASPPKIFSYQVYEDSTQLNCAPSYSYLTGFDEPNKVTTVLDTPIIISWALQQGYYVVSSDHEGPRSAFIAGYEEG
MAILDGIRAFKNFKNLPEDIGVGFYGYAGGAHATAWAVSLAEGYAPEIKIDGAAYGGTPASAKDTFTFLNKGFFAGFAVA
GVSGLALAHPDMEAFLEPRLNAKGKQVFEQIRSRGFCLPSVVLHNNFVDVFSLVNDTNLLIEEPIAGILKQETLVQAEAS
YTVPVPKFPRFMWHALPDEIVPFQPAANYVKEQCQKGANINWNVYPIAEHVTAEIFGLVPGLDFLSKAFKGQTPKVACGS
GVPAIPGINSPSTQNVLGSDLANQLNSLKGQQSAFGKPFGSVSPPL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;VMHHHHHHVPMERRAPFPDPNDDPFYKTPSNIGTYANGQVIQSRKAPTDIGNQNGADSFQLSYRTTNTQKEAQANVATVF
IPSKPASPPKIFSYQVYEDSTQLNCAPSYSYLTGFDEPNKVTTVLDTPIIISWALQQGYYVVSSDHEGPRSAFIAGYEEG
MAILDGIRAFKNFKNLPEDIGVGFYGYAGGAHATAWAVSLAEGYAPEIKIDGAAYGGTPASAKDTFTFLNKGFFAGFAVA
GVSGLALAHPDMEAFLEPRLNAKGKQVFEQIRSRGFCLPSVVLHNNFVDVFSLVNDTNLLIEEPIAGILKQETLVQAEAS
YTVPVPKFPRFMWHALPDEIVPFQPAANYVKEQCQKGANINWNVYPIAEHVTAEIFGLVPGLDFLSKAFKGQTPKVACGS
GVPAIPGINSPSTQNVLGSDLANQLNSLKGQQSAFGKPFGSVSPPL
;
_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 
3 'PALMITIC ACID' PLM 
4 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   VAL n 
1 2   MET n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   VAL n 
1 10  PRO n 
1 11  MET n 
1 12  GLU n 
1 13  ARG n 
1 14  ARG n 
1 15  ALA n 
1 16  PRO n 
1 17  PHE n 
1 18  PRO n 
1 19  ASP n 
1 20  PRO n 
1 21  ASN n 
1 22  ASP n 
1 23  ASP n 
1 24  PRO n 
1 25  PHE n 
1 26  TYR n 
1 27  LYS n 
1 28  THR n 
1 29  PRO n 
1 30  SER n 
1 31  ASN n 
1 32  ILE n 
1 33  GLY n 
1 34  THR n 
1 35  TYR n 
1 36  ALA n 
1 37  ASN n 
1 38  GLY n 
1 39  GLN n 
1 40  VAL n 
1 41  ILE n 
1 42  GLN n 
1 43  SER n 
1 44  ARG n 
1 45  LYS n 
1 46  ALA n 
1 47  PRO n 
1 48  THR n 
1 49  ASP n 
1 50  ILE n 
1 51  GLY n 
1 52  ASN n 
1 53  GLN n 
1 54  ASN n 
1 55  GLY n 
1 56  ALA n 
1 57  ASP n 
1 58  SER n 
1 59  PHE n 
1 60  GLN n 
1 61  LEU n 
1 62  SER n 
1 63  TYR n 
1 64  ARG n 
1 65  THR n 
1 66  THR n 
1 67  ASN n 
1 68  THR n 
1 69  GLN n 
1 70  LYS n 
1 71  GLU n 
1 72  ALA n 
1 73  GLN n 
1 74  ALA n 
1 75  ASN n 
1 76  VAL n 
1 77  ALA n 
1 78  THR n 
1 79  VAL n 
1 80  PHE n 
1 81  ILE n 
1 82  PRO n 
1 83  SER n 
1 84  LYS n 
1 85  PRO n 
1 86  ALA n 
1 87  SER n 
1 88  PRO n 
1 89  PRO n 
1 90  LYS n 
1 91  ILE n 
1 92  PHE n 
1 93  SER n 
1 94  TYR n 
1 95  GLN n 
1 96  VAL n 
1 97  TYR n 
1 98  GLU n 
1 99  ASP n 
1 100 SER n 
1 101 THR n 
1 102 GLN n 
1 103 LEU n 
1 104 ASN n 
1 105 CYS n 
1 106 ALA n 
1 107 PRO n 
1 108 SER n 
1 109 TYR n 
1 110 SER n 
1 111 TYR n 
1 112 LEU n 
1 113 THR n 
1 114 GLY n 
1 115 PHE n 
1 116 ASP n 
1 117 GLU n 
1 118 PRO n 
1 119 ASN n 
1 120 LYS n 
1 121 VAL n 
1 122 THR n 
1 123 THR n 
1 124 VAL n 
1 125 LEU n 
1 126 ASP n 
1 127 THR n 
1 128 PRO n 
1 129 ILE n 
1 130 ILE n 
1 131 ILE n 
1 132 SER n 
1 133 TRP n 
1 134 ALA n 
1 135 LEU n 
1 136 GLN n 
1 137 GLN n 
1 138 GLY n 
1 139 TYR n 
1 140 TYR n 
1 141 VAL n 
1 142 VAL n 
1 143 SER n 
1 144 SER n 
1 145 ASP n 
1 146 HIS n 
1 147 GLU n 
1 148 GLY n 
1 149 PRO n 
1 150 ARG n 
1 151 SER n 
1 152 ALA n 
1 153 PHE n 
1 154 ILE n 
1 155 ALA n 
1 156 GLY n 
1 157 TYR n 
1 158 GLU n 
1 159 GLU n 
1 160 GLY n 
1 161 MET n 
1 162 ALA n 
1 163 ILE n 
1 164 LEU n 
1 165 ASP n 
1 166 GLY n 
1 167 ILE n 
1 168 ARG n 
1 169 ALA n 
1 170 PHE n 
1 171 LYS n 
1 172 ASN n 
1 173 PHE n 
1 174 LYS n 
1 175 ASN n 
1 176 LEU n 
1 177 PRO n 
1 178 GLU n 
1 179 ASP n 
1 180 ILE n 
1 181 GLY n 
1 182 VAL n 
1 183 GLY n 
1 184 PHE n 
1 185 TYR n 
1 186 GLY n 
1 187 TYR n 
1 188 ALA n 
1 189 GLY n 
1 190 GLY n 
1 191 ALA n 
1 192 HIS n 
1 193 ALA n 
1 194 THR n 
1 195 ALA n 
1 196 TRP n 
1 197 ALA n 
1 198 VAL n 
1 199 SER n 
1 200 LEU n 
1 201 ALA n 
1 202 GLU n 
1 203 GLY n 
1 204 TYR n 
1 205 ALA n 
1 206 PRO n 
1 207 GLU n 
1 208 ILE n 
1 209 LYS n 
1 210 ILE n 
1 211 ASP n 
1 212 GLY n 
1 213 ALA n 
1 214 ALA n 
1 215 TYR n 
1 216 GLY n 
1 217 GLY n 
1 218 THR n 
1 219 PRO n 
1 220 ALA n 
1 221 SER n 
1 222 ALA n 
1 223 LYS n 
1 224 ASP n 
1 225 THR n 
1 226 PHE n 
1 227 THR n 
1 228 PHE n 
1 229 LEU n 
1 230 ASN n 
1 231 LYS n 
1 232 GLY n 
1 233 PHE n 
1 234 PHE n 
1 235 ALA n 
1 236 GLY n 
1 237 PHE n 
1 238 ALA n 
1 239 VAL n 
1 240 ALA n 
1 241 GLY n 
1 242 VAL n 
1 243 SER n 
1 244 GLY n 
1 245 LEU n 
1 246 ALA n 
1 247 LEU n 
1 248 ALA n 
1 249 HIS n 
1 250 PRO n 
1 251 ASP n 
1 252 MET n 
1 253 GLU n 
1 254 ALA n 
1 255 PHE n 
1 256 LEU n 
1 257 GLU n 
1 258 PRO n 
1 259 ARG n 
1 260 LEU n 
1 261 ASN n 
1 262 ALA n 
1 263 LYS n 
1 264 GLY n 
1 265 LYS n 
1 266 GLN n 
1 267 VAL n 
1 268 PHE n 
1 269 GLU n 
1 270 GLN n 
1 271 ILE n 
1 272 ARG n 
1 273 SER n 
1 274 ARG n 
1 275 GLY n 
1 276 PHE n 
1 277 CYS n 
1 278 LEU n 
1 279 PRO n 
1 280 SER n 
1 281 VAL n 
1 282 VAL n 
1 283 LEU n 
1 284 HIS n 
1 285 ASN n 
1 286 ASN n 
1 287 PHE n 
1 288 VAL n 
1 289 ASP n 
1 290 VAL n 
1 291 PHE n 
1 292 SER n 
1 293 LEU n 
1 294 VAL n 
1 295 ASN n 
1 296 ASP n 
1 297 THR n 
1 298 ASN n 
1 299 LEU n 
1 300 LEU n 
1 301 ILE n 
1 302 GLU n 
1 303 GLU n 
1 304 PRO n 
1 305 ILE n 
1 306 ALA n 
1 307 GLY n 
1 308 ILE n 
1 309 LEU n 
1 310 LYS n 
1 311 GLN n 
1 312 GLU n 
1 313 THR n 
1 314 LEU n 
1 315 VAL n 
1 316 GLN n 
1 317 ALA n 
1 318 GLU n 
1 319 ALA n 
1 320 SER n 
1 321 TYR n 
1 322 THR n 
1 323 VAL n 
1 324 PRO n 
1 325 VAL n 
1 326 PRO n 
1 327 LYS n 
1 328 PHE n 
1 329 PRO n 
1 330 ARG n 
1 331 PHE n 
1 332 MET n 
1 333 TRP n 
1 334 HIS n 
1 335 ALA n 
1 336 LEU n 
1 337 PRO n 
1 338 ASP n 
1 339 GLU n 
1 340 ILE n 
1 341 VAL n 
1 342 PRO n 
1 343 PHE n 
1 344 GLN n 
1 345 PRO n 
1 346 ALA n 
1 347 ALA n 
1 348 ASN n 
1 349 TYR n 
1 350 VAL n 
1 351 LYS n 
1 352 GLU n 
1 353 GLN n 
1 354 CYS n 
1 355 GLN n 
1 356 LYS n 
1 357 GLY n 
1 358 ALA n 
1 359 ASN n 
1 360 ILE n 
1 361 ASN n 
1 362 TRP n 
1 363 ASN n 
1 364 VAL n 
1 365 TYR n 
1 366 PRO n 
1 367 ILE n 
1 368 ALA n 
1 369 GLU n 
1 370 HIS n 
1 371 VAL n 
1 372 THR n 
1 373 ALA n 
1 374 GLU n 
1 375 ILE n 
1 376 PHE n 
1 377 GLY n 
1 378 LEU n 
1 379 VAL n 
1 380 PRO n 
1 381 GLY n 
1 382 LEU n 
1 383 ASP n 
1 384 PHE n 
1 385 LEU n 
1 386 SER n 
1 387 LYS n 
1 388 ALA n 
1 389 PHE n 
1 390 LYS n 
1 391 GLY n 
1 392 GLN n 
1 393 THR n 
1 394 PRO n 
1 395 LYS n 
1 396 VAL n 
1 397 ALA n 
1 398 CYS n 
1 399 GLY n 
1 400 SER n 
1 401 GLY n 
1 402 VAL n 
1 403 PRO n 
1 404 ALA n 
1 405 ILE n 
1 406 PRO n 
1 407 GLY n 
1 408 ILE n 
1 409 ASN n 
1 410 SER n 
1 411 PRO n 
1 412 SER n 
1 413 THR n 
1 414 GLN n 
1 415 ASN n 
1 416 VAL n 
1 417 LEU n 
1 418 GLY n 
1 419 SER n 
1 420 ASP n 
1 421 LEU n 
1 422 ALA n 
1 423 ASN n 
1 424 GLN n 
1 425 LEU n 
1 426 ASN n 
1 427 SER n 
1 428 LEU n 
1 429 LYS n 
1 430 GLY n 
1 431 GLN n 
1 432 GLN n 
1 433 SER n 
1 434 ALA n 
1 435 PHE n 
1 436 GLY n 
1 437 LYS n 
1 438 PRO n 
1 439 PHE n 
1 440 GLY n 
1 441 SER n 
1 442 VAL n 
1 443 SER n 
1 444 PRO n 
1 445 PRO n 
1 446 LEU 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                   446 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 UTRI_04204_B 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    'Ustilago trichophora' 
_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      'Ustilago trichophora' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     86804 
_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      'Komagataella pastoris' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4922 
_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               GS115 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pFAi2 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DGlcpNAcb1-4DGlcpNAcb1-ROH                            'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1' WURCS                       PDB2Glycan 1.1.0 
3 2 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'       LINUCS                      PDB-CARE   ?     
# 
_pdbx_entity_branch_link.link_id                    1 
_pdbx_entity_branch_link.entity_id                  2 
_pdbx_entity_branch_link.entity_branch_list_num_1   2 
_pdbx_entity_branch_link.comp_id_1                  NAG 
_pdbx_entity_branch_link.atom_id_1                  C1 
_pdbx_entity_branch_link.leaving_atom_id_1          O1 
_pdbx_entity_branch_link.entity_branch_list_num_2   1 
_pdbx_entity_branch_link.comp_id_2                  NAG 
_pdbx_entity_branch_link.atom_id_2                  O4 
_pdbx_entity_branch_link.leaving_atom_id_2          HO4 
_pdbx_entity_branch_link.value_order                sing 
_pdbx_entity_branch_link.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PLM non-polymer                  . 'PALMITIC ACID'                          ? 'C16 H32 O2'     256.424 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   VAL 1   13  ?   ?   ?   A . n 
A 1 2   MET 2   14  ?   ?   ?   A . n 
A 1 3   HIS 3   15  ?   ?   ?   A . n 
A 1 4   HIS 4   16  ?   ?   ?   A . n 
A 1 5   HIS 5   17  ?   ?   ?   A . n 
A 1 6   HIS 6   18  ?   ?   ?   A . n 
A 1 7   HIS 7   19  ?   ?   ?   A . n 
A 1 8   HIS 8   20  ?   ?   ?   A . n 
A 1 9   VAL 9   21  ?   ?   ?   A . n 
A 1 10  PRO 10  22  ?   ?   ?   A . n 
A 1 11  MET 11  23  ?   ?   ?   A . n 
A 1 12  GLU 12  24  ?   ?   ?   A . n 
A 1 13  ARG 13  25  25  ARG ARG A . n 
A 1 14  ARG 14  26  26  ARG ARG A . n 
A 1 15  ALA 15  27  27  ALA ALA A . n 
A 1 16  PRO 16  28  28  PRO PRO A . n 
A 1 17  PHE 17  29  29  PHE PHE A . n 
A 1 18  PRO 18  30  30  PRO PRO A . n 
A 1 19  ASP 19  31  31  ASP ASP A . n 
A 1 20  PRO 20  32  32  PRO PRO A . n 
A 1 21  ASN 21  33  33  ASN ASN A . n 
A 1 22  ASP 22  34  34  ASP ASP A . n 
A 1 23  ASP 23  35  35  ASP ASP A . n 
A 1 24  PRO 24  36  36  PRO PRO A . n 
A 1 25  PHE 25  37  37  PHE PHE A . n 
A 1 26  TYR 26  38  38  TYR TYR A . n 
A 1 27  LYS 27  39  39  LYS LYS A . n 
A 1 28  THR 28  40  40  THR THR A . n 
A 1 29  PRO 29  41  41  PRO PRO A . n 
A 1 30  SER 30  42  42  SER SER A . n 
A 1 31  ASN 31  43  43  ASN ASN A . n 
A 1 32  ILE 32  44  44  ILE ILE A . n 
A 1 33  GLY 33  45  45  GLY GLY A . n 
A 1 34  THR 34  46  46  THR THR A . n 
A 1 35  TYR 35  47  47  TYR TYR A . n 
A 1 36  ALA 36  48  48  ALA ALA A . n 
A 1 37  ASN 37  49  49  ASN ASN A . n 
A 1 38  GLY 38  50  50  GLY GLY A . n 
A 1 39  GLN 39  51  51  GLN GLN A . n 
A 1 40  VAL 40  52  52  VAL VAL A . n 
A 1 41  ILE 41  53  53  ILE ILE A . n 
A 1 42  GLN 42  54  54  GLN GLN A . n 
A 1 43  SER 43  55  55  SER SER A . n 
A 1 44  ARG 44  56  56  ARG ARG A . n 
A 1 45  LYS 45  57  57  LYS LYS A . n 
A 1 46  ALA 46  58  58  ALA ALA A . n 
A 1 47  PRO 47  59  59  PRO PRO A . n 
A 1 48  THR 48  60  60  THR THR A . n 
A 1 49  ASP 49  61  61  ASP ASP A . n 
A 1 50  ILE 50  62  62  ILE ILE A . n 
A 1 51  GLY 51  63  63  GLY GLY A . n 
A 1 52  ASN 52  64  64  ASN ASN A . n 
A 1 53  GLN 53  65  65  GLN GLN A . n 
A 1 54  ASN 54  66  66  ASN ASN A . n 
A 1 55  GLY 55  67  67  GLY GLY A . n 
A 1 56  ALA 56  68  68  ALA ALA A . n 
A 1 57  ASP 57  69  69  ASP ASP A . n 
A 1 58  SER 58  70  70  SER SER A . n 
A 1 59  PHE 59  71  71  PHE PHE A . n 
A 1 60  GLN 60  72  72  GLN GLN A . n 
A 1 61  LEU 61  73  73  LEU LEU A . n 
A 1 62  SER 62  74  74  SER SER A . n 
A 1 63  TYR 63  75  75  TYR TYR A . n 
A 1 64  ARG 64  76  76  ARG ARG A . n 
A 1 65  THR 65  77  77  THR THR A . n 
A 1 66  THR 66  78  78  THR THR A . n 
A 1 67  ASN 67  79  79  ASN ASN A . n 
A 1 68  THR 68  80  80  THR THR A . n 
A 1 69  GLN 69  81  81  GLN GLN A . n 
A 1 70  LYS 70  82  82  LYS LYS A . n 
A 1 71  GLU 71  83  83  GLU GLU A . n 
A 1 72  ALA 72  84  84  ALA ALA A . n 
A 1 73  GLN 73  85  85  GLN GLN A . n 
A 1 74  ALA 74  86  86  ALA ALA A . n 
A 1 75  ASN 75  87  87  ASN ASN A . n 
A 1 76  VAL 76  88  88  VAL VAL A . n 
A 1 77  ALA 77  89  89  ALA ALA A . n 
A 1 78  THR 78  90  90  THR THR A . n 
A 1 79  VAL 79  91  91  VAL VAL A . n 
A 1 80  PHE 80  92  92  PHE PHE A . n 
A 1 81  ILE 81  93  93  ILE ILE A . n 
A 1 82  PRO 82  94  94  PRO PRO A . n 
A 1 83  SER 83  95  95  SER SER A . n 
A 1 84  LYS 84  96  96  LYS LYS A . n 
A 1 85  PRO 85  97  97  PRO PRO A . n 
A 1 86  ALA 86  98  98  ALA ALA A . n 
A 1 87  SER 87  99  99  SER SER A . n 
A 1 88  PRO 88  100 100 PRO PRO A . n 
A 1 89  PRO 89  101 101 PRO PRO A . n 
A 1 90  LYS 90  102 102 LYS LYS A . n 
A 1 91  ILE 91  103 103 ILE ILE A . n 
A 1 92  PHE 92  104 104 PHE PHE A . n 
A 1 93  SER 93  105 105 SER SER A . n 
A 1 94  TYR 94  106 106 TYR TYR A . n 
A 1 95  GLN 95  107 107 GLN GLN A . n 
A 1 96  VAL 96  108 108 VAL VAL A . n 
A 1 97  TYR 97  109 109 TYR TYR A . n 
A 1 98  GLU 98  110 110 GLU GLU A . n 
A 1 99  ASP 99  111 111 ASP ASP A . n 
A 1 100 SER 100 112 112 SER SER A . n 
A 1 101 THR 101 113 113 THR THR A . n 
A 1 102 GLN 102 114 114 GLN GLN A . n 
A 1 103 LEU 103 115 115 LEU LEU A . n 
A 1 104 ASN 104 116 116 ASN ASN A . n 
A 1 105 CYS 105 117 117 CYS CYS A . n 
A 1 106 ALA 106 118 118 ALA ALA A . n 
A 1 107 PRO 107 119 119 PRO PRO A . n 
A 1 108 SER 108 120 120 SER SER A . n 
A 1 109 TYR 109 121 121 TYR TYR A . n 
A 1 110 SER 110 122 122 SER SER A . n 
A 1 111 TYR 111 123 123 TYR TYR A . n 
A 1 112 LEU 112 124 124 LEU LEU A . n 
A 1 113 THR 113 125 125 THR THR A . n 
A 1 114 GLY 114 126 126 GLY GLY A . n 
A 1 115 PHE 115 127 127 PHE PHE A . n 
A 1 116 ASP 116 128 128 ASP ASP A . n 
A 1 117 GLU 117 129 129 GLU GLU A . n 
A 1 118 PRO 118 130 130 PRO PRO A . n 
A 1 119 ASN 119 131 131 ASN ASN A . n 
A 1 120 LYS 120 132 132 LYS LYS A . n 
A 1 121 VAL 121 133 133 VAL VAL A . n 
A 1 122 THR 122 134 134 THR THR A . n 
A 1 123 THR 123 135 135 THR THR A . n 
A 1 124 VAL 124 136 136 VAL VAL A . n 
A 1 125 LEU 125 137 137 LEU LEU A . n 
A 1 126 ASP 126 138 138 ASP ASP A . n 
A 1 127 THR 127 139 139 THR THR A . n 
A 1 128 PRO 128 140 140 PRO PRO A . n 
A 1 129 ILE 129 141 141 ILE ILE A . n 
A 1 130 ILE 130 142 142 ILE ILE A . n 
A 1 131 ILE 131 143 143 ILE ILE A . n 
A 1 132 SER 132 144 144 SER SER A . n 
A 1 133 TRP 133 145 145 TRP TRP A . n 
A 1 134 ALA 134 146 146 ALA ALA A . n 
A 1 135 LEU 135 147 147 LEU LEU A . n 
A 1 136 GLN 136 148 148 GLN GLN A . n 
A 1 137 GLN 137 149 149 GLN GLN A . n 
A 1 138 GLY 138 150 150 GLY GLY A . n 
A 1 139 TYR 139 151 151 TYR TYR A . n 
A 1 140 TYR 140 152 152 TYR TYR A . n 
A 1 141 VAL 141 153 153 VAL VAL A . n 
A 1 142 VAL 142 154 154 VAL VAL A . n 
A 1 143 SER 143 155 155 SER SER A . n 
A 1 144 SER 144 156 156 SER SER A . n 
A 1 145 ASP 145 157 157 ASP ASP A . n 
A 1 146 HIS 146 158 158 HIS HIS A . n 
A 1 147 GLU 147 159 159 GLU GLU A . n 
A 1 148 GLY 148 160 160 GLY GLY A . n 
A 1 149 PRO 149 161 161 PRO PRO A . n 
A 1 150 ARG 150 162 162 ARG ARG A . n 
A 1 151 SER 151 163 163 SER SER A . n 
A 1 152 ALA 152 164 164 ALA ALA A . n 
A 1 153 PHE 153 165 165 PHE PHE A . n 
A 1 154 ILE 154 166 166 ILE ILE A . n 
A 1 155 ALA 155 167 167 ALA ALA A . n 
A 1 156 GLY 156 168 168 GLY GLY A . n 
A 1 157 TYR 157 169 169 TYR TYR A . n 
A 1 158 GLU 158 170 170 GLU GLU A . n 
A 1 159 GLU 159 171 171 GLU GLU A . n 
A 1 160 GLY 160 172 172 GLY GLY A . n 
A 1 161 MET 161 173 173 MET MET A . n 
A 1 162 ALA 162 174 174 ALA ALA A . n 
A 1 163 ILE 163 175 175 ILE ILE A . n 
A 1 164 LEU 164 176 176 LEU LEU A . n 
A 1 165 ASP 165 177 177 ASP ASP A . n 
A 1 166 GLY 166 178 178 GLY GLY A . n 
A 1 167 ILE 167 179 179 ILE ILE A . n 
A 1 168 ARG 168 180 180 ARG ARG A . n 
A 1 169 ALA 169 181 181 ALA ALA A . n 
A 1 170 PHE 170 182 182 PHE PHE A . n 
A 1 171 LYS 171 183 183 LYS LYS A . n 
A 1 172 ASN 172 184 184 ASN ASN A . n 
A 1 173 PHE 173 185 185 PHE PHE A . n 
A 1 174 LYS 174 186 186 LYS LYS A . n 
A 1 175 ASN 175 187 187 ASN ASN A . n 
A 1 176 LEU 176 188 188 LEU LEU A . n 
A 1 177 PRO 177 189 189 PRO PRO A . n 
A 1 178 GLU 178 190 190 GLU GLU A . n 
A 1 179 ASP 179 191 191 ASP ASP A . n 
A 1 180 ILE 180 192 192 ILE ILE A . n 
A 1 181 GLY 181 193 193 GLY GLY A . n 
A 1 182 VAL 182 194 194 VAL VAL A . n 
A 1 183 GLY 183 195 195 GLY GLY A . n 
A 1 184 PHE 184 196 196 PHE PHE A . n 
A 1 185 TYR 185 197 197 TYR TYR A . n 
A 1 186 GLY 186 198 198 GLY GLY A . n 
A 1 187 TYR 187 199 199 TYR TYR A . n 
A 1 188 ALA 188 200 200 ALA ALA A . n 
A 1 189 GLY 189 201 201 GLY GLY A . n 
A 1 190 GLY 190 202 202 GLY GLY A . n 
A 1 191 ALA 191 203 203 ALA ALA A . n 
A 1 192 HIS 192 204 204 HIS HIS A . n 
A 1 193 ALA 193 205 205 ALA ALA A . n 
A 1 194 THR 194 206 206 THR THR A . n 
A 1 195 ALA 195 207 207 ALA ALA A . n 
A 1 196 TRP 196 208 208 TRP TRP A . n 
A 1 197 ALA 197 209 209 ALA ALA A . n 
A 1 198 VAL 198 210 210 VAL VAL A . n 
A 1 199 SER 199 211 211 SER SER A . n 
A 1 200 LEU 200 212 212 LEU LEU A . n 
A 1 201 ALA 201 213 213 ALA ALA A . n 
A 1 202 GLU 202 214 214 GLU GLU A . n 
A 1 203 GLY 203 215 215 GLY GLY A . n 
A 1 204 TYR 204 216 216 TYR TYR A . n 
A 1 205 ALA 205 217 217 ALA ALA A . n 
A 1 206 PRO 206 218 218 PRO PRO A . n 
A 1 207 GLU 207 219 219 GLU GLU A . n 
A 1 208 ILE 208 220 220 ILE ILE A . n 
A 1 209 LYS 209 221 221 LYS LYS A . n 
A 1 210 ILE 210 222 222 ILE ILE A . n 
A 1 211 ASP 211 223 223 ASP ASP A . n 
A 1 212 GLY 212 224 224 GLY GLY A . n 
A 1 213 ALA 213 225 225 ALA ALA A . n 
A 1 214 ALA 214 226 226 ALA ALA A . n 
A 1 215 TYR 215 227 227 TYR TYR A . n 
A 1 216 GLY 216 228 228 GLY GLY A . n 
A 1 217 GLY 217 229 229 GLY GLY A . n 
A 1 218 THR 218 230 230 THR THR A . n 
A 1 219 PRO 219 231 231 PRO PRO A . n 
A 1 220 ALA 220 232 232 ALA ALA A . n 
A 1 221 SER 221 233 233 SER SER A . n 
A 1 222 ALA 222 234 234 ALA ALA A . n 
A 1 223 LYS 223 235 235 LYS LYS A . n 
A 1 224 ASP 224 236 236 ASP ASP A . n 
A 1 225 THR 225 237 237 THR THR A . n 
A 1 226 PHE 226 238 238 PHE PHE A . n 
A 1 227 THR 227 239 239 THR THR A . n 
A 1 228 PHE 228 240 240 PHE PHE A . n 
A 1 229 LEU 229 241 241 LEU LEU A . n 
A 1 230 ASN 230 242 242 ASN ASN A . n 
A 1 231 LYS 231 243 243 LYS LYS A . n 
A 1 232 GLY 232 244 244 GLY GLY A . n 
A 1 233 PHE 233 245 245 PHE PHE A . n 
A 1 234 PHE 234 246 246 PHE PHE A . n 
A 1 235 ALA 235 247 247 ALA ALA A . n 
A 1 236 GLY 236 248 248 GLY GLY A . n 
A 1 237 PHE 237 249 249 PHE PHE A . n 
A 1 238 ALA 238 250 250 ALA ALA A . n 
A 1 239 VAL 239 251 251 VAL VAL A . n 
A 1 240 ALA 240 252 252 ALA ALA A . n 
A 1 241 GLY 241 253 253 GLY GLY A . n 
A 1 242 VAL 242 254 254 VAL VAL A . n 
A 1 243 SER 243 255 255 SER SER A . n 
A 1 244 GLY 244 256 256 GLY GLY A . n 
A 1 245 LEU 245 257 257 LEU LEU A . n 
A 1 246 ALA 246 258 258 ALA ALA A . n 
A 1 247 LEU 247 259 259 LEU LEU A . n 
A 1 248 ALA 248 260 260 ALA ALA A . n 
A 1 249 HIS 249 261 261 HIS HIS A . n 
A 1 250 PRO 250 262 262 PRO PRO A . n 
A 1 251 ASP 251 263 263 ASP ASP A . n 
A 1 252 MET 252 264 264 MET MET A . n 
A 1 253 GLU 253 265 265 GLU GLU A . n 
A 1 254 ALA 254 266 266 ALA ALA A . n 
A 1 255 PHE 255 267 267 PHE PHE A . n 
A 1 256 LEU 256 268 268 LEU LEU A . n 
A 1 257 GLU 257 269 269 GLU GLU A . n 
A 1 258 PRO 258 270 270 PRO PRO A . n 
A 1 259 ARG 259 271 271 ARG ARG A . n 
A 1 260 LEU 260 272 272 LEU LEU A . n 
A 1 261 ASN 261 273 273 ASN ASN A . n 
A 1 262 ALA 262 274 274 ALA ALA A . n 
A 1 263 LYS 263 275 275 LYS LYS A . n 
A 1 264 GLY 264 276 276 GLY GLY A . n 
A 1 265 LYS 265 277 277 LYS LYS A . n 
A 1 266 GLN 266 278 278 GLN GLN A . n 
A 1 267 VAL 267 279 279 VAL VAL A . n 
A 1 268 PHE 268 280 280 PHE PHE A . n 
A 1 269 GLU 269 281 281 GLU GLU A . n 
A 1 270 GLN 270 282 282 GLN GLN A . n 
A 1 271 ILE 271 283 283 ILE ILE A . n 
A 1 272 ARG 272 284 284 ARG ARG A . n 
A 1 273 SER 273 285 285 SER SER A . n 
A 1 274 ARG 274 286 286 ARG ARG A . n 
A 1 275 GLY 275 287 287 GLY GLY A . n 
A 1 276 PHE 276 288 288 PHE PHE A . n 
A 1 277 CYS 277 289 289 CYS CYS A . n 
A 1 278 LEU 278 290 290 LEU LEU A . n 
A 1 279 PRO 279 291 291 PRO PRO A . n 
A 1 280 SER 280 292 292 SER SER A . n 
A 1 281 VAL 281 293 293 VAL VAL A . n 
A 1 282 VAL 282 294 294 VAL VAL A . n 
A 1 283 LEU 283 295 295 LEU LEU A . n 
A 1 284 HIS 284 296 296 HIS HIS A . n 
A 1 285 ASN 285 297 297 ASN ASN A . n 
A 1 286 ASN 286 298 298 ASN ASN A . n 
A 1 287 PHE 287 299 299 PHE PHE A . n 
A 1 288 VAL 288 300 300 VAL VAL A . n 
A 1 289 ASP 289 301 301 ASP ASP A . n 
A 1 290 VAL 290 302 302 VAL VAL A . n 
A 1 291 PHE 291 303 303 PHE PHE A . n 
A 1 292 SER 292 304 304 SER SER A . n 
A 1 293 LEU 293 305 305 LEU LEU A . n 
A 1 294 VAL 294 306 306 VAL VAL A . n 
A 1 295 ASN 295 307 307 ASN ASN A . n 
A 1 296 ASP 296 308 308 ASP ASP A . n 
A 1 297 THR 297 309 309 THR THR A . n 
A 1 298 ASN 298 310 310 ASN ASN A . n 
A 1 299 LEU 299 311 311 LEU LEU A . n 
A 1 300 LEU 300 312 312 LEU LEU A . n 
A 1 301 ILE 301 313 313 ILE ILE A . n 
A 1 302 GLU 302 314 314 GLU GLU A . n 
A 1 303 GLU 303 315 315 GLU GLU A . n 
A 1 304 PRO 304 316 316 PRO PRO A . n 
A 1 305 ILE 305 317 317 ILE ILE A . n 
A 1 306 ALA 306 318 318 ALA ALA A . n 
A 1 307 GLY 307 319 319 GLY GLY A . n 
A 1 308 ILE 308 320 320 ILE ILE A . n 
A 1 309 LEU 309 321 321 LEU LEU A . n 
A 1 310 LYS 310 322 322 LYS LYS A . n 
A 1 311 GLN 311 323 323 GLN GLN A . n 
A 1 312 GLU 312 324 324 GLU GLU A . n 
A 1 313 THR 313 325 325 THR THR A . n 
A 1 314 LEU 314 326 326 LEU LEU A . n 
A 1 315 VAL 315 327 327 VAL VAL A . n 
A 1 316 GLN 316 328 328 GLN GLN A . n 
A 1 317 ALA 317 329 329 ALA ALA A . n 
A 1 318 GLU 318 330 330 GLU GLU A . n 
A 1 319 ALA 319 331 331 ALA ALA A . n 
A 1 320 SER 320 332 332 SER SER A . n 
A 1 321 TYR 321 333 333 TYR TYR A . n 
A 1 322 THR 322 334 334 THR THR A . n 
A 1 323 VAL 323 335 335 VAL VAL A . n 
A 1 324 PRO 324 336 336 PRO PRO A . n 
A 1 325 VAL 325 337 337 VAL VAL A . n 
A 1 326 PRO 326 338 338 PRO PRO A . n 
A 1 327 LYS 327 339 339 LYS LYS A . n 
A 1 328 PHE 328 340 340 PHE PHE A . n 
A 1 329 PRO 329 341 341 PRO PRO A . n 
A 1 330 ARG 330 342 342 ARG ARG A . n 
A 1 331 PHE 331 343 343 PHE PHE A . n 
A 1 332 MET 332 344 344 MET MET A . n 
A 1 333 TRP 333 345 345 TRP TRP A . n 
A 1 334 HIS 334 346 346 HIS HIS A . n 
A 1 335 ALA 335 347 347 ALA ALA A . n 
A 1 336 LEU 336 348 348 LEU LEU A . n 
A 1 337 PRO 337 349 349 PRO PRO A . n 
A 1 338 ASP 338 350 350 ASP ASP A . n 
A 1 339 GLU 339 351 351 GLU GLU A . n 
A 1 340 ILE 340 352 352 ILE ILE A . n 
A 1 341 VAL 341 353 353 VAL VAL A . n 
A 1 342 PRO 342 354 354 PRO PRO A . n 
A 1 343 PHE 343 355 355 PHE PHE A . n 
A 1 344 GLN 344 356 356 GLN GLN A . n 
A 1 345 PRO 345 357 357 PRO PRO A . n 
A 1 346 ALA 346 358 358 ALA ALA A . n 
A 1 347 ALA 347 359 359 ALA ALA A . n 
A 1 348 ASN 348 360 360 ASN ASN A . n 
A 1 349 TYR 349 361 361 TYR TYR A . n 
A 1 350 VAL 350 362 362 VAL VAL A . n 
A 1 351 LYS 351 363 363 LYS LYS A . n 
A 1 352 GLU 352 364 364 GLU GLU A . n 
A 1 353 GLN 353 365 365 GLN GLN A . n 
A 1 354 CYS 354 366 366 CYS CYS A . n 
A 1 355 GLN 355 367 367 GLN GLN A . n 
A 1 356 LYS 356 368 368 LYS LYS A . n 
A 1 357 GLY 357 369 369 GLY GLY A . n 
A 1 358 ALA 358 370 370 ALA ALA A . n 
A 1 359 ASN 359 371 371 ASN ASN A . n 
A 1 360 ILE 360 372 372 ILE ILE A . n 
A 1 361 ASN 361 373 373 ASN ASN A . n 
A 1 362 TRP 362 374 374 TRP TRP A . n 
A 1 363 ASN 363 375 375 ASN ASN A . n 
A 1 364 VAL 364 376 376 VAL VAL A . n 
A 1 365 TYR 365 377 377 TYR TYR A . n 
A 1 366 PRO 366 378 378 PRO PRO A . n 
A 1 367 ILE 367 379 379 ILE ILE A . n 
A 1 368 ALA 368 380 380 ALA ALA A . n 
A 1 369 GLU 369 381 381 GLU GLU A . n 
A 1 370 HIS 370 382 382 HIS HIS A . n 
A 1 371 VAL 371 383 383 VAL VAL A . n 
A 1 372 THR 372 384 384 THR THR A . n 
A 1 373 ALA 373 385 385 ALA ALA A . n 
A 1 374 GLU 374 386 386 GLU GLU A . n 
A 1 375 ILE 375 387 387 ILE ILE A . n 
A 1 376 PHE 376 388 388 PHE PHE A . n 
A 1 377 GLY 377 389 389 GLY GLY A . n 
A 1 378 LEU 378 390 390 LEU LEU A . n 
A 1 379 VAL 379 391 391 VAL VAL A . n 
A 1 380 PRO 380 392 392 PRO PRO A . n 
A 1 381 GLY 381 393 393 GLY GLY A . n 
A 1 382 LEU 382 394 394 LEU LEU A . n 
A 1 383 ASP 383 395 395 ASP ASP A . n 
A 1 384 PHE 384 396 396 PHE PHE A . n 
A 1 385 LEU 385 397 397 LEU LEU A . n 
A 1 386 SER 386 398 398 SER SER A . n 
A 1 387 LYS 387 399 399 LYS LYS A . n 
A 1 388 ALA 388 400 400 ALA ALA A . n 
A 1 389 PHE 389 401 401 PHE PHE A . n 
A 1 390 LYS 390 402 402 LYS LYS A . n 
A 1 391 GLY 391 403 403 GLY GLY A . n 
A 1 392 GLN 392 404 404 GLN GLN A . n 
A 1 393 THR 393 405 405 THR THR A . n 
A 1 394 PRO 394 406 406 PRO PRO A . n 
A 1 395 LYS 395 407 407 LYS LYS A . n 
A 1 396 VAL 396 408 408 VAL VAL A . n 
A 1 397 ALA 397 409 409 ALA ALA A . n 
A 1 398 CYS 398 410 410 CYS CYS A . n 
A 1 399 GLY 399 411 411 GLY GLY A . n 
A 1 400 SER 400 412 412 SER SER A . n 
A 1 401 GLY 401 413 413 GLY GLY A . n 
A 1 402 VAL 402 414 414 VAL VAL A . n 
A 1 403 PRO 403 415 415 PRO PRO A . n 
A 1 404 ALA 404 416 416 ALA ALA A . n 
A 1 405 ILE 405 417 417 ILE ILE A . n 
A 1 406 PRO 406 418 418 PRO PRO A . n 
A 1 407 GLY 407 419 419 GLY GLY A . n 
A 1 408 ILE 408 420 420 ILE ILE A . n 
A 1 409 ASN 409 421 421 ASN ASN A . n 
A 1 410 SER 410 422 422 SER SER A . n 
A 1 411 PRO 411 423 423 PRO PRO A . n 
A 1 412 SER 412 424 424 SER SER A . n 
A 1 413 THR 413 425 425 THR THR A . n 
A 1 414 GLN 414 426 426 GLN GLN A . n 
A 1 415 ASN 415 427 427 ASN ASN A . n 
A 1 416 VAL 416 428 428 VAL VAL A . n 
A 1 417 LEU 417 429 429 LEU LEU A . n 
A 1 418 GLY 418 430 430 GLY GLY A . n 
A 1 419 SER 419 431 431 SER SER A . n 
A 1 420 ASP 420 432 432 ASP ASP A . n 
A 1 421 LEU 421 433 433 LEU LEU A . n 
A 1 422 ALA 422 434 434 ALA ALA A . n 
A 1 423 ASN 423 435 435 ASN ASN A . n 
A 1 424 GLN 424 436 436 GLN GLN A . n 
A 1 425 LEU 425 437 437 LEU LEU A . n 
A 1 426 ASN 426 438 438 ASN ASN A . n 
A 1 427 SER 427 439 439 SER SER A . n 
A 1 428 LEU 428 440 440 LEU LEU A . n 
A 1 429 LYS 429 441 441 LYS LYS A . n 
A 1 430 GLY 430 442 442 GLY GLY A . n 
A 1 431 GLN 431 443 443 GLN GLN A . n 
A 1 432 GLN 432 444 444 GLN GLN A . n 
A 1 433 SER 433 445 445 SER SER A . n 
A 1 434 ALA 434 446 446 ALA ALA A . n 
A 1 435 PHE 435 447 447 PHE PHE A . n 
A 1 436 GLY 436 448 448 GLY GLY A . n 
A 1 437 LYS 437 449 449 LYS LYS A . n 
A 1 438 PRO 438 450 450 PRO PRO A . n 
A 1 439 PHE 439 451 451 PHE PHE A . n 
A 1 440 GLY 440 452 452 GLY GLY A . n 
A 1 441 SER 441 453 453 SER SER A . n 
A 1 442 VAL 442 454 454 VAL VAL A . n 
A 1 443 SER 443 455 455 SER SER A . n 
A 1 444 PRO 444 456 456 PRO PRO A . n 
A 1 445 PRO 445 457 457 PRO PRO A . n 
A 1 446 LEU 446 458 458 LEU LEU A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
B 2 NAG 1 B NAG 1 A NAG 501 n 
B 2 NAG 2 B NAG 2 A NAG 502 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        PLM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   PLM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
C 3 PLM 1   500 500 PLM PLM A . 
D 4 HOH 1   601 170 HOH HOH A . 
D 4 HOH 2   602 171 HOH HOH A . 
D 4 HOH 3   603 159 HOH HOH A . 
D 4 HOH 4   604 167 HOH HOH A . 
D 4 HOH 5   605 40  HOH HOH A . 
D 4 HOH 6   606 90  HOH HOH A . 
D 4 HOH 7   607 56  HOH HOH A . 
D 4 HOH 8   608 51  HOH HOH A . 
D 4 HOH 9   609 71  HOH HOH A . 
D 4 HOH 10  610 16  HOH HOH A . 
D 4 HOH 11  611 115 HOH HOH A . 
D 4 HOH 12  612 43  HOH HOH A . 
D 4 HOH 13  613 49  HOH HOH A . 
D 4 HOH 14  614 129 HOH HOH A . 
D 4 HOH 15  615 102 HOH HOH A . 
D 4 HOH 16  616 8   HOH HOH A . 
D 4 HOH 17  617 47  HOH HOH A . 
D 4 HOH 18  618 54  HOH HOH A . 
D 4 HOH 19  619 64  HOH HOH A . 
D 4 HOH 20  620 59  HOH HOH A . 
D 4 HOH 21  621 74  HOH HOH A . 
D 4 HOH 22  622 3   HOH HOH A . 
D 4 HOH 23  623 68  HOH HOH A . 
D 4 HOH 24  624 60  HOH HOH A . 
D 4 HOH 25  625 75  HOH HOH A . 
D 4 HOH 26  626 37  HOH HOH A . 
D 4 HOH 27  627 123 HOH HOH A . 
D 4 HOH 28  628 53  HOH HOH A . 
D 4 HOH 29  629 101 HOH HOH A . 
D 4 HOH 30  630 126 HOH HOH A . 
D 4 HOH 31  631 12  HOH HOH A . 
D 4 HOH 32  632 6   HOH HOH A . 
D 4 HOH 33  633 33  HOH HOH A . 
D 4 HOH 34  634 10  HOH HOH A . 
D 4 HOH 35  635 7   HOH HOH A . 
D 4 HOH 36  636 34  HOH HOH A . 
D 4 HOH 37  637 109 HOH HOH A . 
D 4 HOH 38  638 36  HOH HOH A . 
D 4 HOH 39  639 4   HOH HOH A . 
D 4 HOH 40  640 41  HOH HOH A . 
D 4 HOH 41  641 25  HOH HOH A . 
D 4 HOH 42  642 27  HOH HOH A . 
D 4 HOH 43  643 50  HOH HOH A . 
D 4 HOH 44  644 132 HOH HOH A . 
D 4 HOH 45  645 44  HOH HOH A . 
D 4 HOH 46  646 39  HOH HOH A . 
D 4 HOH 47  647 18  HOH HOH A . 
D 4 HOH 48  648 143 HOH HOH A . 
D 4 HOH 49  649 94  HOH HOH A . 
D 4 HOH 50  650 31  HOH HOH A . 
D 4 HOH 51  651 23  HOH HOH A . 
D 4 HOH 52  652 19  HOH HOH A . 
D 4 HOH 53  653 46  HOH HOH A . 
D 4 HOH 54  654 2   HOH HOH A . 
D 4 HOH 55  655 67  HOH HOH A . 
D 4 HOH 56  656 99  HOH HOH A . 
D 4 HOH 57  657 17  HOH HOH A . 
D 4 HOH 58  658 1   HOH HOH A . 
D 4 HOH 59  659 70  HOH HOH A . 
D 4 HOH 60  660 21  HOH HOH A . 
D 4 HOH 61  661 85  HOH HOH A . 
D 4 HOH 62  662 169 HOH HOH A . 
D 4 HOH 63  663 98  HOH HOH A . 
D 4 HOH 64  664 78  HOH HOH A . 
D 4 HOH 65  665 79  HOH HOH A . 
D 4 HOH 66  666 15  HOH HOH A . 
D 4 HOH 67  667 11  HOH HOH A . 
D 4 HOH 68  668 69  HOH HOH A . 
D 4 HOH 69  669 14  HOH HOH A . 
D 4 HOH 70  670 81  HOH HOH A . 
D 4 HOH 71  671 22  HOH HOH A . 
D 4 HOH 72  672 93  HOH HOH A . 
D 4 HOH 73  673 161 HOH HOH A . 
D 4 HOH 74  674 28  HOH HOH A . 
D 4 HOH 75  675 134 HOH HOH A . 
D 4 HOH 76  676 13  HOH HOH A . 
D 4 HOH 77  677 65  HOH HOH A . 
D 4 HOH 78  678 32  HOH HOH A . 
D 4 HOH 79  679 76  HOH HOH A . 
D 4 HOH 80  680 107 HOH HOH A . 
D 4 HOH 81  681 35  HOH HOH A . 
D 4 HOH 82  682 144 HOH HOH A . 
D 4 HOH 83  683 66  HOH HOH A . 
D 4 HOH 84  684 48  HOH HOH A . 
D 4 HOH 85  685 130 HOH HOH A . 
D 4 HOH 86  686 5   HOH HOH A . 
D 4 HOH 87  687 95  HOH HOH A . 
D 4 HOH 88  688 86  HOH HOH A . 
D 4 HOH 89  689 29  HOH HOH A . 
D 4 HOH 90  690 140 HOH HOH A . 
D 4 HOH 91  691 153 HOH HOH A . 
D 4 HOH 92  692 103 HOH HOH A . 
D 4 HOH 93  693 62  HOH HOH A . 
D 4 HOH 94  694 38  HOH HOH A . 
D 4 HOH 95  695 26  HOH HOH A . 
D 4 HOH 96  696 125 HOH HOH A . 
D 4 HOH 97  697 179 HOH HOH A . 
D 4 HOH 98  698 52  HOH HOH A . 
D 4 HOH 99  699 72  HOH HOH A . 
D 4 HOH 100 700 181 HOH HOH A . 
D 4 HOH 101 701 91  HOH HOH A . 
D 4 HOH 102 702 42  HOH HOH A . 
D 4 HOH 103 703 30  HOH HOH A . 
D 4 HOH 104 704 61  HOH HOH A . 
D 4 HOH 105 705 156 HOH HOH A . 
D 4 HOH 106 706 100 HOH HOH A . 
D 4 HOH 107 707 127 HOH HOH A . 
D 4 HOH 108 708 20  HOH HOH A . 
D 4 HOH 109 709 166 HOH HOH A . 
D 4 HOH 110 710 88  HOH HOH A . 
D 4 HOH 111 711 92  HOH HOH A . 
D 4 HOH 112 712 45  HOH HOH A . 
D 4 HOH 113 713 185 HOH HOH A . 
D 4 HOH 114 714 80  HOH HOH A . 
D 4 HOH 115 715 89  HOH HOH A . 
D 4 HOH 116 716 184 HOH HOH A . 
D 4 HOH 117 717 9   HOH HOH A . 
D 4 HOH 118 718 146 HOH HOH A . 
D 4 HOH 119 719 84  HOH HOH A . 
D 4 HOH 120 720 104 HOH HOH A . 
D 4 HOH 121 721 178 HOH HOH A . 
D 4 HOH 122 722 122 HOH HOH A . 
D 4 HOH 123 723 24  HOH HOH A . 
D 4 HOH 124 724 58  HOH HOH A . 
D 4 HOH 125 725 73  HOH HOH A . 
D 4 HOH 126 726 133 HOH HOH A . 
D 4 HOH 127 727 87  HOH HOH A . 
D 4 HOH 128 728 118 HOH HOH A . 
D 4 HOH 129 729 57  HOH HOH A . 
D 4 HOH 130 730 162 HOH HOH A . 
D 4 HOH 131 731 176 HOH HOH A . 
D 4 HOH 132 732 139 HOH HOH A . 
D 4 HOH 133 733 177 HOH HOH A . 
D 4 HOH 134 734 145 HOH HOH A . 
D 4 HOH 135 735 183 HOH HOH A . 
D 4 HOH 136 736 83  HOH HOH A . 
D 4 HOH 137 737 164 HOH HOH A . 
D 4 HOH 138 738 120 HOH HOH A . 
D 4 HOH 139 739 174 HOH HOH A . 
D 4 HOH 140 740 82  HOH HOH A . 
D 4 HOH 141 741 154 HOH HOH A . 
D 4 HOH 142 742 111 HOH HOH A . 
D 4 HOH 143 743 165 HOH HOH A . 
D 4 HOH 144 744 173 HOH HOH A . 
D 4 HOH 145 745 168 HOH HOH A . 
D 4 HOH 146 746 77  HOH HOH A . 
D 4 HOH 147 747 141 HOH HOH A . 
D 4 HOH 148 748 55  HOH HOH A . 
D 4 HOH 149 749 163 HOH HOH A . 
D 4 HOH 150 750 135 HOH HOH A . 
D 4 HOH 151 751 137 HOH HOH A . 
D 4 HOH 152 752 121 HOH HOH A . 
D 4 HOH 153 753 175 HOH HOH A . 
D 4 HOH 154 754 142 HOH HOH A . 
D 4 HOH 155 755 158 HOH HOH A . 
D 4 HOH 156 756 150 HOH HOH A . 
D 4 HOH 157 757 112 HOH HOH A . 
D 4 HOH 158 758 152 HOH HOH A . 
D 4 HOH 159 759 63  HOH HOH A . 
D 4 HOH 160 760 117 HOH HOH A . 
D 4 HOH 161 761 110 HOH HOH A . 
D 4 HOH 162 762 172 HOH HOH A . 
D 4 HOH 163 763 113 HOH HOH A . 
D 4 HOH 164 764 180 HOH HOH A . 
D 4 HOH 165 765 116 HOH HOH A . 
D 4 HOH 166 766 106 HOH HOH A . 
D 4 HOH 167 767 149 HOH HOH A . 
D 4 HOH 168 768 114 HOH HOH A . 
D 4 HOH 169 769 105 HOH HOH A . 
D 4 HOH 170 770 182 HOH HOH A . 
D 4 HOH 171 771 96  HOH HOH A . 
D 4 HOH 172 772 148 HOH HOH A . 
D 4 HOH 173 773 155 HOH HOH A . 
D 4 HOH 174 774 136 HOH HOH A . 
D 4 HOH 175 775 124 HOH HOH A . 
D 4 HOH 176 776 119 HOH HOH A . 
D 4 HOH 177 777 151 HOH HOH A . 
D 4 HOH 178 778 97  HOH HOH A . 
D 4 HOH 179 779 157 HOH HOH A . 
D 4 HOH 180 780 147 HOH HOH A . 
D 4 HOH 181 781 138 HOH HOH A . 
D 4 HOH 182 782 108 HOH HOH A . 
D 4 HOH 183 783 131 HOH HOH A . 
D 4 HOH 184 784 160 HOH HOH A . 
D 4 HOH 185 785 128 HOH HOH A . 
# 
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      ? ? ? 1.20.1_4487 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.28        2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .           3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .           4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JC9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     97.358 
_cell.length_a_esd                 ? 
_cell.length_b                     97.358 
_cell.length_b_esd                 ? 
_cell.length_c                     209.686 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9JC9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                178 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 61 2 2' 
_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                   9JC9 
_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             2.97 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.54 
_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          EVAPORATION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.5 
_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 NaOAc trihydrate pH 4.5, 30% v/v PEG 300' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-10-06 
_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   0.95372 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95372 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX1 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JC9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.37 
_reflns.d_resolution_low                               48.68 
_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                                     24575 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                39.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.96 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.2036 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.371 
_reflns_shell.d_res_low                                     2.456 
_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                             2321 
_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                                  0.849 
_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                                  1.574 
_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                                93.420 
_refine.B_iso_mean                               40.4586 
_refine.B_iso_min                                22.770 
_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                                 9JC9 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.3700 
_refine.ls_d_res_low                             48.6800 
_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                     24570 
_refine.ls_number_reflns_R_free                  1260 
_refine.ls_number_reflns_R_work                  23310 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.7200 
_refine.ls_percent_reflns_R_free                 5.1300 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1965 
_refine.ls_R_factor_R_free                       0.2353 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1944 
_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                          1.350 
_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               THROUGHOUT 
_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             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.2300 
_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                            0.3200 
_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                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.3700 
_refine_hist.d_res_low                        48.6800 
_refine_hist.number_atoms_solvent             185 
_refine_hist.number_atoms_total               3544 
_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       434 
_refine_hist.pdbx_B_iso_mean_ligand           51.34 
_refine_hist.pdbx_B_iso_mean_solvent          40.62 
_refine_hist.pdbx_number_atoms_protein        3313 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         46 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.3700 2.4700  2587 . 116 2471 97.0000  . . . 0.0000 0.2577 . . . . . . . 9 . . . 0.3207 
'X-RAY DIFFRACTION' 2.4700 2.5800  2672 . 152 2520 100.0000 . . . 0.0000 0.2475 . . . . . . . 9 . . . 0.3019 
'X-RAY DIFFRACTION' 2.5800 2.7100  2682 . 145 2537 100.0000 . . . 0.0000 0.2324 . . . . . . . 9 . . . 0.3451 
'X-RAY DIFFRACTION' 2.7100 2.8800  2686 . 132 2554 100.0000 . . . 0.0000 0.2407 . . . . . . . 9 . . . 0.2818 
'X-RAY DIFFRACTION' 2.8800 3.1100  2701 . 144 2557 100.0000 . . . 0.0000 0.2328 . . . . . . . 9 . . . 0.3161 
'X-RAY DIFFRACTION' 3.1100 3.4200  2718 . 145 2573 100.0000 . . . 0.0000 0.2130 . . . . . . . 9 . . . 0.2502 
'X-RAY DIFFRACTION' 3.4200 3.9100  2756 . 140 2616 100.0000 . . . 0.0000 0.1910 . . . . . . . 9 . . . 0.2206 
'X-RAY DIFFRACTION' 3.9100 4.9300  2791 . 144 2647 100.0000 . . . 0.0000 0.1502 . . . . . . . 9 . . . 0.1892 
'X-RAY DIFFRACTION' 4.9300 48.6800 2977 . 142 2835 100.0000 . . . 0.0000 0.1678 . . . . . . . 9 . . . 0.1833 
# 
_struct.entry_id                     9JC9 
_struct.title                        'CalA-like lipase from Ustilago trichophora (S200A mutant)' 
_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        9JC9 
_struct_keywords.text            'alpha/beta-Hydrolases, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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                    A0A5C3EAQ1_9BASI 
_struct_ref.pdbx_db_accession          A0A5C3EAQ1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VPMERRAPFPDPNDDPFYKTPSNIGTYANGQVIQSRKAPTDIGNQNGADSFQLSYRTTNTQKEAQANVATVFIPSKPASP
PKIFSYQVYEDSTQLNCAPSYSYLTGFDEPNKVTTVLDTPIIISWALQQGYYVVSSDHEGPRSAFIAGYEEGMAILDGIR
AFKNFKNLPEDIGVGFYGYSGGAHATAWAVSLAEGYAPEIKIDGAAYGGTPASAKDTFTFLNKGFFAGFAVAGVSGLALA
HPDMEAFLEPRLNAKGKQVFEQIRSRGFCLPSVVLHNNFVDVFSLVNDTNLLIEEPIAGILKQETLVQAEASYTVPVPKF
PRFMWHALPDEIVPFQPAANYVKEQCQKGANINWNVYPIAEHVTAEIFGLVPGLDFLSKAFKGQTPKVACGSGVPAIPGI
NSPSTQNVLGSDLANQLNSLKGQQSAFGKPFGSVSPPL
;
_struct_ref.pdbx_align_begin           21 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9JC9 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 9 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 446 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A5C3EAQ1 
_struct_ref_seq.db_align_beg                  21 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  458 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       21 
_struct_ref_seq.pdbx_auth_seq_align_end       458 
# 
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 9JC9 VAL A 1   ? UNP A0A5C3EAQ1 ?   ?   'expression tag'      13  1 
1 9JC9 MET A 2   ? UNP A0A5C3EAQ1 ?   ?   'expression tag'      14  2 
1 9JC9 HIS A 3   ? UNP A0A5C3EAQ1 ?   ?   'expression tag'      15  3 
1 9JC9 HIS A 4   ? UNP A0A5C3EAQ1 ?   ?   'expression tag'      16  4 
1 9JC9 HIS A 5   ? UNP A0A5C3EAQ1 ?   ?   'expression tag'      17  5 
1 9JC9 HIS A 6   ? UNP A0A5C3EAQ1 ?   ?   'expression tag'      18  6 
1 9JC9 HIS A 7   ? UNP A0A5C3EAQ1 ?   ?   'expression tag'      19  7 
1 9JC9 HIS A 8   ? UNP A0A5C3EAQ1 ?   ?   'expression tag'      20  8 
1 9JC9 ALA A 188 ? UNP A0A5C3EAQ1 SER 200 'engineered mutation' 200 9 
# 
_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)' 8490  ? 
1 MORE         -40   ? 
1 'SSA (A^2)'  29750 ? 
# 
_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   'gel filtration' 
_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' 10_554 -y,-x,-z-1/6 0.5000000000 -0.8660254038 0.0000000000 0.0000000000 -0.8660254038 
-0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -34.9476666667 
# 
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 19  ? LYS A 27  ? ASP A 31  LYS A 39  5 ? 9  
HELX_P HELX_P2  AA2 PRO A 29  ? TYR A 35  ? PRO A 41  TYR A 47  5 ? 7  
HELX_P HELX_P3  AA3 THR A 48  ? ASN A 54  ? THR A 60  ASN A 66  1 ? 7  
HELX_P HELX_P4  AA4 GLN A 102 ? CYS A 105 ? GLN A 114 CYS A 117 5 ? 4  
HELX_P HELX_P5  AA5 ALA A 106 ? LEU A 112 ? ALA A 118 LEU A 124 1 ? 7  
HELX_P HELX_P6  AA6 LYS A 120 ? LEU A 125 ? LYS A 132 LEU A 137 1 ? 6  
HELX_P HELX_P7  AA7 ASP A 126 ? GLN A 137 ? ASP A 138 GLN A 149 1 ? 12 
HELX_P HELX_P8  AA8 ALA A 155 ? LYS A 174 ? ALA A 167 LYS A 186 1 ? 20 
HELX_P HELX_P9  AA9 ALA A 188 ? ALA A 205 ? ALA A 200 ALA A 217 1 ? 18 
HELX_P HELX_P10 AB1 SER A 221 ? ASN A 230 ? SER A 233 ASN A 242 1 ? 10 
HELX_P HELX_P11 AB2 PHE A 234 ? HIS A 249 ? PHE A 246 HIS A 261 1 ? 16 
HELX_P HELX_P12 AB3 HIS A 249 ? GLU A 257 ? HIS A 261 GLU A 269 1 ? 9  
HELX_P HELX_P13 AB4 PRO A 258 ? LEU A 260 ? PRO A 270 LEU A 272 5 ? 3  
HELX_P HELX_P14 AB5 ASN A 261 ? ARG A 272 ? ASN A 273 ARG A 284 1 ? 12 
HELX_P HELX_P15 AB6 CYS A 277 ? VAL A 282 ? CYS A 289 VAL A 294 1 ? 6  
HELX_P HELX_P16 AB7 ASP A 289 ? VAL A 294 ? ASP A 301 VAL A 306 1 ? 6  
HELX_P HELX_P17 AB8 PRO A 304 ? GLU A 312 ? PRO A 316 GLU A 324 1 ? 9  
HELX_P HELX_P18 AB9 PRO A 342 ? LYS A 356 ? PRO A 354 LYS A 368 1 ? 15 
HELX_P HELX_P19 AC1 GLU A 369 ? GLY A 377 ? GLU A 381 GLY A 389 1 ? 9  
HELX_P HELX_P20 AC2 GLY A 377 ? LYS A 390 ? GLY A 389 LYS A 402 1 ? 14 
HELX_P HELX_P21 AC3 SER A 412 ? GLY A 418 ? SER A 424 GLY A 430 1 ? 7  
HELX_P HELX_P22 AC4 GLY A 418 ? SER A 427 ? GLY A 430 SER A 439 1 ? 10 
# 
_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 105 SG  ? ? ? 1_555 A CYS 277 SG ? ? A CYS 117 A CYS 289 1_555 ? ? ? ? ? ? ? 2.006 ? ?               
disulf2 disulf ?    ? A CYS 354 SG  ? ? ? 1_555 A CYS 398 SG ? ? A CYS 366 A CYS 410 1_555 ? ? ? ? ? ? ? 2.021 ? ?               
covale1 covale one  ? A ASN 295 ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 307 B NAG 1   1_555 ? ? ? ? ? ? ? 1.451 ? N-Glycosylation 
covale2 covale both ? B NAG .   O4  ? ? ? 1_555 B NAG .   C1 ? ? B NAG 1   B NAG 2   1_555 ? ? ? ? ? ? ? 1.397 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG B .   ? ASN A 295 ? NAG B 1   ? 1_555 ASN A 307 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 CYS A 105 ? CYS A 277 ? CYS A 117 ? 1_555 CYS A 289 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
3 CYS A 354 ? CYS A 398 ? CYS A 366 ? 1_555 CYS A 410 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 87  A . ? SER 99  A PRO 88  A ? PRO 100 A 1 -2.54 
2 GLU 303 A . ? GLU 315 A PRO 304 A ? PRO 316 A 1 5.27  
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   9 
_struct_sheet.details          ? 
# 
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 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? 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 VAL A 40  ? LYS A 45  ? VAL A 52  LYS A 57  
AA1 2 ASP A 57  ? THR A 66  ? ASP A 69  THR A 78  
AA1 3 ALA A 72  ? ILE A 81  ? ALA A 84  ILE A 93  
AA1 4 TYR A 140 ? SER A 144 ? TYR A 152 SER A 156 
AA1 5 LYS A 90  ? GLN A 95  ? LYS A 102 GLN A 107 
AA1 6 GLY A 181 ? TYR A 187 ? GLY A 193 TYR A 199 
AA1 7 LYS A 209 ? GLY A 216 ? LYS A 221 GLY A 228 
AA1 8 PRO A 329 ? ALA A 335 ? PRO A 341 ALA A 347 
AA1 9 ASN A 359 ? TYR A 365 ? ASN A 371 TYR A 377 
# 
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 GLN A 42  ? N GLN A 54  O SER A 62  ? O SER A 74  
AA1 2 3 N THR A 65  ? N THR A 77  O GLN A 73  ? O GLN A 85  
AA1 3 4 N PHE A 80  ? N PHE A 92  O VAL A 141 ? O VAL A 153 
AA1 4 5 O TYR A 140 ? O TYR A 152 N PHE A 92  ? N PHE A 104 
AA1 5 6 N SER A 93  ? N SER A 105 O GLY A 183 ? O GLY A 195 
AA1 6 7 N VAL A 182 ? N VAL A 194 O LYS A 209 ? O LYS A 221 
AA1 7 8 N ALA A 213 ? N ALA A 225 O PHE A 331 ? O PHE A 343 
AA1 8 9 N ARG A 330 ? N ARG A 342 O ASN A 361 ? O ASN A 373 
# 
_pdbx_entry_details.entry_id                   9JC9 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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 ALA A 27  ? ? -32.61  135.03  
2  1 LYS A 82  ? ? 73.15   32.42   
3  1 LEU A 137 ? ? -96.24  -89.49  
4  1 ILE A 166 ? ? 42.95   26.44   
5  1 ASN A 187 ? ? 34.99   65.02   
6  1 ALA A 200 ? ? 60.04   -127.61 
7  1 LYS A 243 ? ? 79.08   -3.47   
8  1 CYS A 289 ? ? -117.51 -161.13 
9  1 GLU A 324 ? ? -90.69  48.66   
10 1 PRO A 349 ? ? -89.55  33.49   
11 1 ASN A 421 ? ? -140.77 19.06   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 25 ? ? 0.279 'SIDE CHAIN' 
2 1 ARG A 26 ? ? 0.146 'SIDE CHAIN' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     724 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       785 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.31 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A VAL 13 ? A VAL 1  
2  1 Y 1 A MET 14 ? A MET 2  
3  1 Y 1 A HIS 15 ? A HIS 3  
4  1 Y 1 A HIS 16 ? A HIS 4  
5  1 Y 1 A HIS 17 ? A HIS 5  
6  1 Y 1 A HIS 18 ? A HIS 6  
7  1 Y 1 A HIS 19 ? A HIS 7  
8  1 Y 1 A HIS 20 ? A HIS 8  
9  1 Y 1 A VAL 21 ? A VAL 9  
10 1 Y 1 A PRO 22 ? A PRO 10 
11 1 Y 1 A MET 23 ? A MET 11 
12 1 Y 1 A GLU 24 ? A GLU 12 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
NAG C1   C N R 250 
NAG C2   C N R 251 
NAG C3   C N R 252 
NAG C4   C N S 253 
NAG C5   C N R 254 
NAG C6   C N N 255 
NAG C7   C N N 256 
NAG C8   C N N 257 
NAG N2   N N N 258 
NAG O1   O N N 259 
NAG O3   O N N 260 
NAG O4   O N N 261 
NAG O5   O N N 262 
NAG O6   O N N 263 
NAG O7   O N N 264 
NAG H1   H N N 265 
NAG H2   H N N 266 
NAG H3   H N N 267 
NAG H4   H N N 268 
NAG H5   H N N 269 
NAG H61  H N N 270 
NAG H62  H N N 271 
NAG H81  H N N 272 
NAG H82  H N N 273 
NAG H83  H N N 274 
NAG HN2  H N N 275 
NAG HO1  H N N 276 
NAG HO3  H N N 277 
NAG HO4  H N N 278 
NAG HO6  H N N 279 
PHE N    N N N 280 
PHE CA   C N S 281 
PHE C    C N N 282 
PHE O    O N N 283 
PHE CB   C N N 284 
PHE CG   C Y N 285 
PHE CD1  C Y N 286 
PHE CD2  C Y N 287 
PHE CE1  C Y N 288 
PHE CE2  C Y N 289 
PHE CZ   C Y N 290 
PHE OXT  O N N 291 
PHE H    H N N 292 
PHE H2   H N N 293 
PHE HA   H N N 294 
PHE HB2  H N N 295 
PHE HB3  H N N 296 
PHE HD1  H N N 297 
PHE HD2  H N N 298 
PHE HE1  H N N 299 
PHE HE2  H N N 300 
PHE HZ   H N N 301 
PHE HXT  H N N 302 
PLM C1   C N N 303 
PLM O1   O N N 304 
PLM O2   O N N 305 
PLM C2   C N N 306 
PLM C3   C N N 307 
PLM C4   C N N 308 
PLM C5   C N N 309 
PLM C6   C N N 310 
PLM C7   C N N 311 
PLM C8   C N N 312 
PLM C9   C N N 313 
PLM CA   C N N 314 
PLM CB   C N N 315 
PLM CC   C N N 316 
PLM CD   C N N 317 
PLM CE   C N N 318 
PLM CF   C N N 319 
PLM CG   C N N 320 
PLM H    H N N 321 
PLM H21  H N N 322 
PLM H22  H N N 323 
PLM H31  H N N 324 
PLM H32  H N N 325 
PLM H41  H N N 326 
PLM H42  H N N 327 
PLM H51  H N N 328 
PLM H52  H N N 329 
PLM H61  H N N 330 
PLM H62  H N N 331 
PLM H71  H N N 332 
PLM H72  H N N 333 
PLM H81  H N N 334 
PLM H82  H N N 335 
PLM H91  H N N 336 
PLM H92  H N N 337 
PLM HA1  H N N 338 
PLM HA2  H N N 339 
PLM HB1  H N N 340 
PLM HB2  H N N 341 
PLM HC1  H N N 342 
PLM HC2  H N N 343 
PLM HD1  H N N 344 
PLM HD2  H N N 345 
PLM HE1  H N N 346 
PLM HE2  H N N 347 
PLM HF1  H N N 348 
PLM HF2  H N N 349 
PLM HG1  H N N 350 
PLM HG2  H N N 351 
PLM HG3  H N N 352 
PRO N    N N N 353 
PRO CA   C N S 354 
PRO C    C N N 355 
PRO O    O N N 356 
PRO CB   C N N 357 
PRO CG   C N N 358 
PRO CD   C N N 359 
PRO OXT  O N N 360 
PRO H    H N N 361 
PRO HA   H N N 362 
PRO HB2  H N N 363 
PRO HB3  H N N 364 
PRO HG2  H N N 365 
PRO HG3  H N N 366 
PRO HD2  H N N 367 
PRO HD3  H N N 368 
PRO HXT  H N N 369 
SER N    N N N 370 
SER CA   C N S 371 
SER C    C N N 372 
SER O    O N N 373 
SER CB   C N N 374 
SER OG   O N N 375 
SER OXT  O N N 376 
SER H    H N N 377 
SER H2   H N N 378 
SER HA   H N N 379 
SER HB2  H N N 380 
SER HB3  H N N 381 
SER HG   H N N 382 
SER HXT  H N N 383 
THR N    N N N 384 
THR CA   C N S 385 
THR C    C N N 386 
THR O    O N N 387 
THR CB   C N R 388 
THR OG1  O N N 389 
THR CG2  C N N 390 
THR OXT  O N N 391 
THR H    H N N 392 
THR H2   H N N 393 
THR HA   H N N 394 
THR HB   H N N 395 
THR HG1  H N N 396 
THR HG21 H N N 397 
THR HG22 H N N 398 
THR HG23 H N N 399 
THR HXT  H N N 400 
TRP N    N N N 401 
TRP CA   C N S 402 
TRP C    C N N 403 
TRP O    O N N 404 
TRP CB   C N N 405 
TRP CG   C Y N 406 
TRP CD1  C Y N 407 
TRP CD2  C Y N 408 
TRP NE1  N Y N 409 
TRP CE2  C Y N 410 
TRP CE3  C Y N 411 
TRP CZ2  C Y N 412 
TRP CZ3  C Y N 413 
TRP CH2  C Y N 414 
TRP OXT  O N N 415 
TRP H    H N N 416 
TRP H2   H N N 417 
TRP HA   H N N 418 
TRP HB2  H N N 419 
TRP HB3  H N N 420 
TRP HD1  H N N 421 
TRP HE1  H N N 422 
TRP HE3  H N N 423 
TRP HZ2  H N N 424 
TRP HZ3  H N N 425 
TRP HH2  H N N 426 
TRP HXT  H N N 427 
TYR N    N N N 428 
TYR CA   C N S 429 
TYR C    C N N 430 
TYR O    O N N 431 
TYR CB   C N N 432 
TYR CG   C Y N 433 
TYR CD1  C Y N 434 
TYR CD2  C Y N 435 
TYR CE1  C Y N 436 
TYR CE2  C Y N 437 
TYR CZ   C Y N 438 
TYR OH   O N N 439 
TYR OXT  O N N 440 
TYR H    H N N 441 
TYR H2   H N N 442 
TYR HA   H N N 443 
TYR HB2  H N N 444 
TYR HB3  H N N 445 
TYR HD1  H N N 446 
TYR HD2  H N N 447 
TYR HE1  H N N 448 
TYR HE2  H N N 449 
TYR HH   H N N 450 
TYR HXT  H N N 451 
VAL N    N N N 452 
VAL CA   C N S 453 
VAL C    C N N 454 
VAL O    O N N 455 
VAL CB   C N N 456 
VAL CG1  C N N 457 
VAL CG2  C N N 458 
VAL OXT  O N N 459 
VAL H    H N N 460 
VAL H2   H N N 461 
VAL HA   H N N 462 
VAL HB   H N N 463 
VAL HG11 H N N 464 
VAL HG12 H N N 465 
VAL HG13 H N N 466 
VAL HG21 H N N 467 
VAL HG22 H N N 468 
VAL HG23 H N N 469 
VAL HXT  H N N 470 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
NAG C1  C2   sing N N 237 
NAG C1  O1   sing N N 238 
NAG C1  O5   sing N N 239 
NAG C1  H1   sing N N 240 
NAG C2  C3   sing N N 241 
NAG C2  N2   sing N N 242 
NAG C2  H2   sing N N 243 
NAG C3  C4   sing N N 244 
NAG C3  O3   sing N N 245 
NAG C3  H3   sing N N 246 
NAG C4  C5   sing N N 247 
NAG C4  O4   sing N N 248 
NAG C4  H4   sing N N 249 
NAG C5  C6   sing N N 250 
NAG C5  O5   sing N N 251 
NAG C5  H5   sing N N 252 
NAG C6  O6   sing N N 253 
NAG C6  H61  sing N N 254 
NAG C6  H62  sing N N 255 
NAG C7  C8   sing N N 256 
NAG C7  N2   sing N N 257 
NAG C7  O7   doub N N 258 
NAG C8  H81  sing N N 259 
NAG C8  H82  sing N N 260 
NAG C8  H83  sing N N 261 
NAG N2  HN2  sing N N 262 
NAG O1  HO1  sing N N 263 
NAG O3  HO3  sing N N 264 
NAG O4  HO4  sing N N 265 
NAG O6  HO6  sing N N 266 
PHE N   CA   sing N N 267 
PHE N   H    sing N N 268 
PHE N   H2   sing N N 269 
PHE CA  C    sing N N 270 
PHE CA  CB   sing N N 271 
PHE CA  HA   sing N N 272 
PHE C   O    doub N N 273 
PHE C   OXT  sing N N 274 
PHE CB  CG   sing N N 275 
PHE CB  HB2  sing N N 276 
PHE CB  HB3  sing N N 277 
PHE CG  CD1  doub Y N 278 
PHE CG  CD2  sing Y N 279 
PHE CD1 CE1  sing Y N 280 
PHE CD1 HD1  sing N N 281 
PHE CD2 CE2  doub Y N 282 
PHE CD2 HD2  sing N N 283 
PHE CE1 CZ   doub Y N 284 
PHE CE1 HE1  sing N N 285 
PHE CE2 CZ   sing Y N 286 
PHE CE2 HE2  sing N N 287 
PHE CZ  HZ   sing N N 288 
PHE OXT HXT  sing N N 289 
PLM C1  O1   sing N N 290 
PLM C1  O2   doub N N 291 
PLM C1  C2   sing N N 292 
PLM O1  H    sing N N 293 
PLM C2  C3   sing N N 294 
PLM C2  H21  sing N N 295 
PLM C2  H22  sing N N 296 
PLM C3  C4   sing N N 297 
PLM C3  H31  sing N N 298 
PLM C3  H32  sing N N 299 
PLM C4  C5   sing N N 300 
PLM C4  H41  sing N N 301 
PLM C4  H42  sing N N 302 
PLM C5  C6   sing N N 303 
PLM C5  H51  sing N N 304 
PLM C5  H52  sing N N 305 
PLM C6  C7   sing N N 306 
PLM C6  H61  sing N N 307 
PLM C6  H62  sing N N 308 
PLM C7  C8   sing N N 309 
PLM C7  H71  sing N N 310 
PLM C7  H72  sing N N 311 
PLM C8  C9   sing N N 312 
PLM C8  H81  sing N N 313 
PLM C8  H82  sing N N 314 
PLM C9  CA   sing N N 315 
PLM C9  H91  sing N N 316 
PLM C9  H92  sing N N 317 
PLM CA  CB   sing N N 318 
PLM CA  HA1  sing N N 319 
PLM CA  HA2  sing N N 320 
PLM CB  CC   sing N N 321 
PLM CB  HB1  sing N N 322 
PLM CB  HB2  sing N N 323 
PLM CC  CD   sing N N 324 
PLM CC  HC1  sing N N 325 
PLM CC  HC2  sing N N 326 
PLM CD  CE   sing N N 327 
PLM CD  HD1  sing N N 328 
PLM CD  HD2  sing N N 329 
PLM CE  CF   sing N N 330 
PLM CE  HE1  sing N N 331 
PLM CE  HE2  sing N N 332 
PLM CF  CG   sing N N 333 
PLM CF  HF1  sing N N 334 
PLM CF  HF2  sing N N 335 
PLM CG  HG1  sing N N 336 
PLM CG  HG2  sing N N 337 
PLM CG  HG3  sing N N 338 
PRO N   CA   sing N N 339 
PRO N   CD   sing N N 340 
PRO N   H    sing N N 341 
PRO CA  C    sing N N 342 
PRO CA  CB   sing N N 343 
PRO CA  HA   sing N N 344 
PRO C   O    doub N N 345 
PRO C   OXT  sing N N 346 
PRO CB  CG   sing N N 347 
PRO CB  HB2  sing N N 348 
PRO CB  HB3  sing N N 349 
PRO CG  CD   sing N N 350 
PRO CG  HG2  sing N N 351 
PRO CG  HG3  sing N N 352 
PRO CD  HD2  sing N N 353 
PRO CD  HD3  sing N N 354 
PRO OXT HXT  sing N N 355 
SER N   CA   sing N N 356 
SER N   H    sing N N 357 
SER N   H2   sing N N 358 
SER CA  C    sing N N 359 
SER CA  CB   sing N N 360 
SER CA  HA   sing N N 361 
SER C   O    doub N N 362 
SER C   OXT  sing N N 363 
SER CB  OG   sing N N 364 
SER CB  HB2  sing N N 365 
SER CB  HB3  sing N N 366 
SER OG  HG   sing N N 367 
SER OXT HXT  sing N N 368 
THR N   CA   sing N N 369 
THR N   H    sing N N 370 
THR N   H2   sing N N 371 
THR CA  C    sing N N 372 
THR CA  CB   sing N N 373 
THR CA  HA   sing N N 374 
THR C   O    doub N N 375 
THR C   OXT  sing N N 376 
THR CB  OG1  sing N N 377 
THR CB  CG2  sing N N 378 
THR CB  HB   sing N N 379 
THR OG1 HG1  sing N N 380 
THR CG2 HG21 sing N N 381 
THR CG2 HG22 sing N N 382 
THR CG2 HG23 sing N N 383 
THR OXT HXT  sing N N 384 
TRP N   CA   sing N N 385 
TRP N   H    sing N N 386 
TRP N   H2   sing N N 387 
TRP CA  C    sing N N 388 
TRP CA  CB   sing N N 389 
TRP CA  HA   sing N N 390 
TRP C   O    doub N N 391 
TRP C   OXT  sing N N 392 
TRP CB  CG   sing N N 393 
TRP CB  HB2  sing N N 394 
TRP CB  HB3  sing N N 395 
TRP CG  CD1  doub Y N 396 
TRP CG  CD2  sing Y N 397 
TRP CD1 NE1  sing Y N 398 
TRP CD1 HD1  sing N N 399 
TRP CD2 CE2  doub Y N 400 
TRP CD2 CE3  sing Y N 401 
TRP NE1 CE2  sing Y N 402 
TRP NE1 HE1  sing N N 403 
TRP CE2 CZ2  sing Y N 404 
TRP CE3 CZ3  doub Y N 405 
TRP CE3 HE3  sing N N 406 
TRP CZ2 CH2  doub Y N 407 
TRP CZ2 HZ2  sing N N 408 
TRP CZ3 CH2  sing Y N 409 
TRP CZ3 HZ3  sing N N 410 
TRP CH2 HH2  sing N N 411 
TRP OXT HXT  sing N N 412 
TYR N   CA   sing N N 413 
TYR N   H    sing N N 414 
TYR N   H2   sing N N 415 
TYR CA  C    sing N N 416 
TYR CA  CB   sing N N 417 
TYR CA  HA   sing N N 418 
TYR C   O    doub N N 419 
TYR C   OXT  sing N N 420 
TYR CB  CG   sing N N 421 
TYR CB  HB2  sing N N 422 
TYR CB  HB3  sing N N 423 
TYR CG  CD1  doub Y N 424 
TYR CG  CD2  sing Y N 425 
TYR CD1 CE1  sing Y N 426 
TYR CD1 HD1  sing N N 427 
TYR CD2 CE2  doub Y N 428 
TYR CD2 HD2  sing N N 429 
TYR CE1 CZ   doub Y N 430 
TYR CE1 HE1  sing N N 431 
TYR CE2 CZ   sing Y N 432 
TYR CE2 HE2  sing N N 433 
TYR CZ  OH   sing N N 434 
TYR OH  HH   sing N N 435 
TYR OXT HXT  sing N N 436 
VAL N   CA   sing N N 437 
VAL N   H    sing N N 438 
VAL N   H2   sing N N 439 
VAL CA  C    sing N N 440 
VAL CA  CB   sing N N 441 
VAL CA  HA   sing N N 442 
VAL C   O    doub N N 443 
VAL C   OXT  sing N N 444 
VAL CB  CG1  sing N N 445 
VAL CB  CG2  sing N N 446 
VAL CB  HB   sing N N 447 
VAL CG1 HG11 sing N N 448 
VAL CG1 HG12 sing N N 449 
VAL CG1 HG13 sing N N 450 
VAL CG2 HG21 sing N N 451 
VAL CG2 HG22 sing N N 452 
VAL CG2 HG23 sing N N 453 
VAL OXT HXT  sing N N 454 
# 
_pdbx_audit_support.funding_organization   'National Research Foundation (NRF, Singapore)' 
_pdbx_audit_support.country                Singapore 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 NAG 2 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JC9 
_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]   0.010271 
_atom_sites.fract_transf_matrix[1][2]   0.005930 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011860 
_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]   0.004769 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
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   . ARG A 1 13  ? 23.173  -65.029 -19.930 1.00 55.87 ?  25  ARG A N   1 
ATOM   2    C CA  . ARG A 1 13  ? 22.483  -65.205 -18.625 1.00 59.32 ?  25  ARG A CA  1 
ATOM   3    C C   . ARG A 1 13  ? 21.393  -64.132 -18.463 1.00 60.94 ?  25  ARG A C   1 
ATOM   4    O O   . ARG A 1 13  ? 21.714  -62.946 -18.635 1.00 63.58 ?  25  ARG A O   1 
ATOM   5    C CB  . ARG A 1 13  ? 23.508  -65.158 -17.488 1.00 64.93 ?  25  ARG A CB  1 
ATOM   6    C CG  . ARG A 1 13  ? 22.956  -64.767 -16.124 1.00 71.67 ?  25  ARG A CG  1 
ATOM   7    C CD  . ARG A 1 13  ? 22.177  -65.895 -15.468 1.00 66.87 ?  25  ARG A CD  1 
ATOM   8    N NE  . ARG A 1 13  ? 22.725  -67.214 -15.800 1.00 79.27 ?  25  ARG A NE  1 
ATOM   9    C CZ  . ARG A 1 13  ? 23.230  -68.055 -14.910 1.00 81.45 ?  25  ARG A CZ  1 
ATOM   10   N NH1 . ARG A 1 13  ? 22.431  -68.672 -14.058 1.00 76.65 ?  25  ARG A NH1 1 
ATOM   11   N NH2 . ARG A 1 13  ? 24.532  -68.273 -14.875 1.00 74.06 ?  25  ARG A NH2 1 
ATOM   12   N N   . ARG A 1 14  ? 20.160  -64.543 -18.156 1.00 59.74 ?  26  ARG A N   1 
ATOM   13   C CA  . ARG A 1 14  ? 19.027  -63.599 -17.951 1.00 57.02 ?  26  ARG A CA  1 
ATOM   14   C C   . ARG A 1 14  ? 19.007  -63.030 -16.521 1.00 57.44 ?  26  ARG A C   1 
ATOM   15   O O   . ARG A 1 14  ? 19.628  -63.647 -15.632 1.00 55.07 ?  26  ARG A O   1 
ATOM   16   C CB  . ARG A 1 14  ? 17.686  -64.266 -18.276 1.00 56.15 ?  26  ARG A CB  1 
ATOM   17   C CG  . ARG A 1 14  ? 17.491  -64.583 -19.750 1.00 60.93 ?  26  ARG A CG  1 
ATOM   18   C CD  . ARG A 1 14  ? 16.024  -64.656 -20.130 1.00 55.26 ?  26  ARG A CD  1 
ATOM   19   N NE  . ARG A 1 14  ? 15.826  -64.450 -21.568 1.00 63.85 ?  26  ARG A NE  1 
ATOM   20   C CZ  . ARG A 1 14  ? 15.217  -63.399 -22.097 1.00 65.94 ?  26  ARG A CZ  1 
ATOM   21   N NH1 . ARG A 1 14  ? 14.261  -62.785 -21.426 1.00 65.11 ?  26  ARG A NH1 1 
ATOM   22   N NH2 . ARG A 1 14  ? 15.566  -62.963 -23.294 1.00 54.52 ?  26  ARG A NH2 1 
ATOM   23   N N   . ALA A 1 15  ? 18.355  -61.881 -16.321 1.00 54.07 ?  27  ALA A N   1 
ATOM   24   C CA  . ALA A 1 15  ? 18.192  -61.262 -14.980 1.00 53.20 ?  27  ALA A CA  1 
ATOM   25   C C   . ALA A 1 15  ? 18.086  -62.295 -13.855 1.00 56.87 ?  27  ALA A C   1 
ATOM   26   O O   . ALA A 1 15  ? 17.295  -63.254 -13.967 1.00 57.48 ?  27  ALA A O   1 
ATOM   27   C CB  . ALA A 1 15  ? 16.953  -60.401 -15.000 1.00 50.24 ?  27  ALA A CB  1 
ATOM   28   N N   . PRO A 1 16  ? 18.799  -62.096 -12.724 1.00 53.51 ?  28  PRO A N   1 
ATOM   29   C CA  . PRO A 1 16  ? 18.722  -63.012 -11.578 1.00 54.91 ?  28  PRO A CA  1 
ATOM   30   C C   . PRO A 1 16  ? 17.475  -62.836 -10.726 1.00 49.07 ?  28  PRO A C   1 
ATOM   31   O O   . PRO A 1 16  ? 17.248  -63.654 -9.826  1.00 53.08 ?  28  PRO A O   1 
ATOM   32   C CB  . PRO A 1 16  ? 19.991  -62.673 -10.775 1.00 50.72 ?  28  PRO A CB  1 
ATOM   33   C CG  . PRO A 1 16  ? 20.255  -61.236 -11.085 1.00 49.64 ?  28  PRO A CG  1 
ATOM   34   C CD  . PRO A 1 16  ? 19.768  -61.005 -12.498 1.00 50.19 ?  28  PRO A CD  1 
ATOM   35   N N   . PHE A 1 17  ? 16.664  -61.818 -10.971 1.00 50.50 ?  29  PHE A N   1 
ATOM   36   C CA  . PHE A 1 17  ? 15.497  -61.530 -10.153 1.00 55.33 ?  29  PHE A CA  1 
ATOM   37   C C   . PHE A 1 17  ? 14.239  -61.535 -11.010 1.00 54.97 ?  29  PHE A C   1 
ATOM   38   O O   . PHE A 1 17  ? 14.310  -61.330 -12.228 1.00 58.32 ?  29  PHE A O   1 
ATOM   39   C CB  . PHE A 1 17  ? 15.626  -60.161 -9.463  1.00 56.64 ?  29  PHE A CB  1 
ATOM   40   C CG  . PHE A 1 17  ? 16.524  -60.158 -8.263  1.00 53.46 ?  29  PHE A CG  1 
ATOM   41   C CD1 . PHE A 1 17  ? 17.108  -61.326 -7.807  1.00 53.57 ?  29  PHE A CD1 1 
ATOM   42   C CD2 . PHE A 1 17  ? 16.787  -58.969 -7.589  1.00 54.53 ?  29  PHE A CD2 1 
ATOM   43   C CE1 . PHE A 1 17  ? 17.940  -61.319 -6.689  1.00 52.90 ?  29  PHE A CE1 1 
ATOM   44   C CE2 . PHE A 1 17  ? 17.613  -58.953 -6.471  1.00 58.47 ?  29  PHE A CE2 1 
ATOM   45   C CZ  . PHE A 1 17  ? 18.191  -60.134 -6.021  1.00 53.66 ?  29  PHE A CZ  1 
ATOM   46   N N   . PRO A 1 18  ? 13.066  -61.757 -10.410 1.00 49.25 ?  30  PRO A N   1 
ATOM   47   C CA  . PRO A 1 18  ? 11.819  -61.612 -11.169 1.00 53.94 ?  30  PRO A CA  1 
ATOM   48   C C   . PRO A 1 18  ? 11.643  -60.191 -11.685 1.00 51.19 ?  30  PRO A C   1 
ATOM   49   O O   . PRO A 1 18  ? 12.222  -59.233 -11.173 1.00 50.71 ?  30  PRO A O   1 
ATOM   50   C CB  . PRO A 1 18  ? 10.727  -61.965 -10.145 1.00 50.32 ?  30  PRO A CB  1 
ATOM   51   C CG  . PRO A 1 18  ? 11.376  -61.815 -8.813  1.00 48.06 ?  30  PRO A CG  1 
ATOM   52   C CD  . PRO A 1 18  ? 12.813  -62.203 -9.033  1.00 48.61 ?  30  PRO A CD  1 
ATOM   53   N N   . ASP A 1 19  ? 10.840  -60.069 -12.727 1.00 50.14 ?  31  ASP A N   1 
ATOM   54   C CA  . ASP A 1 19  ? 10.411  -58.761 -13.178 1.00 47.69 ?  31  ASP A CA  1 
ATOM   55   C C   . ASP A 1 19  ? 9.841   -57.985 -11.995 1.00 48.68 ?  31  ASP A C   1 
ATOM   56   O O   . ASP A 1 19  ? 9.026   -58.536 -11.241 1.00 49.45 ?  31  ASP A O   1 
ATOM   57   C CB  . ASP A 1 19  ? 9.349   -58.908 -14.267 1.00 49.26 ?  31  ASP A CB  1 
ATOM   58   C CG  . ASP A 1 19  ? 9.083   -57.619 -15.006 1.00 45.53 ?  31  ASP A CG  1 
ATOM   59   O OD1 . ASP A 1 19  ? 8.321   -56.775 -14.479 1.00 40.79 ?  31  ASP A OD1 1 
ATOM   60   O OD2 . ASP A 1 19  ? 9.630   -57.478 -16.123 1.00 51.12 ?  31  ASP A OD2 1 
ATOM   61   N N   . PRO A 1 20  ? 10.259  -56.729 -11.781 1.00 48.38 ?  32  PRO A N   1 
ATOM   62   C CA  . PRO A 1 20  ? 9.712   -55.948 -10.652 1.00 43.02 ?  32  PRO A CA  1 
ATOM   63   C C   . PRO A 1 20  ? 8.198   -55.981 -10.539 1.00 45.11 ?  32  PRO A C   1 
ATOM   64   O O   . PRO A 1 20  ? 7.672   -56.035 -9.414  1.00 40.58 ?  32  PRO A O   1 
ATOM   65   C CB  . PRO A 1 20  ? 10.234  -54.534 -10.939 1.00 36.74 ?  32  PRO A CB  1 
ATOM   66   C CG  . PRO A 1 20  ? 11.579  -54.783 -11.590 1.00 38.64 ?  32  PRO A CG  1 
ATOM   67   C CD  . PRO A 1 20  ? 11.442  -56.079 -12.386 1.00 44.31 ?  32  PRO A CD  1 
ATOM   68   N N   . ASN A 1 21  ? 7.485   -55.962 -11.678 1.00 45.21 ?  33  ASN A N   1 
ATOM   69   C CA  . ASN A 1 21  ? 6.021   -56.039 -11.663 1.00 44.84 ?  33  ASN A CA  1 
ATOM   70   C C   . ASN A 1 21  ? 5.524   -57.297 -10.950 1.00 42.40 ?  33  ASN A C   1 
ATOM   71   O O   . ASN A 1 21  ? 4.437   -57.283 -10.360 1.00 43.67 ?  33  ASN A O   1 
ATOM   72   C CB  . ASN A 1 21  ? 5.463   -56.018 -13.095 1.00 44.15 ?  33  ASN A CB  1 
ATOM   73   C CG  . ASN A 1 21  ? 5.620   -54.661 -13.795 1.00 46.97 ?  33  ASN A CG  1 
ATOM   74   O OD1 . ASN A 1 21  ? 4.842   -53.723 -13.569 1.00 37.59 ?  33  ASN A OD1 1 
ATOM   75   N ND2 . ASN A 1 21  ? 6.604   -54.575 -14.687 1.00 43.30 ?  33  ASN A ND2 1 
ATOM   76   N N   . ASP A 1 22  ? 6.297   -58.386 -11.011 1.00 39.50 ?  34  ASP A N   1 
ATOM   77   C CA  . ASP A 1 22  ? 5.940   -59.688 -10.450 1.00 47.29 ?  34  ASP A CA  1 
ATOM   78   C C   . ASP A 1 22  ? 6.594   -59.967 -9.100  1.00 54.66 ?  34  ASP A C   1 
ATOM   79   O O   . ASP A 1 22  ? 6.429   -61.072 -8.571  1.00 53.85 ?  34  ASP A O   1 
ATOM   80   C CB  . ASP A 1 22  ? 6.350   -60.822 -11.407 1.00 43.27 ?  34  ASP A CB  1 
ATOM   81   C CG  . ASP A 1 22  ? 5.842   -60.628 -12.827 1.00 45.38 ?  34  ASP A CG  1 
ATOM   82   O OD1 . ASP A 1 22  ? 4.723   -60.079 -13.010 1.00 39.94 ?  34  ASP A OD1 1 
ATOM   83   O OD2 . ASP A 1 22  ? 6.568   -61.069 -13.756 1.00 46.68 ?  34  ASP A OD2 1 
ATOM   84   N N   . ASP A 1 23  ? 7.367   -59.020 -8.558  1.00 50.03 ?  35  ASP A N   1 
ATOM   85   C CA  . ASP A 1 23  ? 8.200   -59.236 -7.381  1.00 48.83 ?  35  ASP A CA  1 
ATOM   86   C C   . ASP A 1 23  ? 7.570   -58.529 -6.193  1.00 54.99 ?  35  ASP A C   1 
ATOM   87   O O   . ASP A 1 23  ? 7.427   -57.297 -6.233  1.00 53.91 ?  35  ASP A O   1 
ATOM   88   C CB  . ASP A 1 23  ? 9.609   -58.704 -7.635  1.00 51.15 ?  35  ASP A CB  1 
ATOM   89   C CG  . ASP A 1 23  ? 10.605  -59.111 -6.563  1.00 48.43 ?  35  ASP A CG  1 
ATOM   90   O OD1 . ASP A 1 23  ? 10.187  -59.379 -5.411  1.00 51.10 ?  35  ASP A OD1 1 
ATOM   91   O OD2 . ASP A 1 23  ? 11.815  -59.147 -6.889  1.00 40.83 ?  35  ASP A OD2 1 
ATOM   92   N N   . PRO A 1 24  ? 7.175   -59.235 -5.125  1.00 56.40 ?  36  PRO A N   1 
ATOM   93   C CA  . PRO A 1 24  ? 6.525   -58.544 -4.002  1.00 53.28 ?  36  PRO A CA  1 
ATOM   94   C C   . PRO A 1 24  ? 7.465   -57.606 -3.271  1.00 51.20 ?  36  PRO A C   1 
ATOM   95   O O   . PRO A 1 24  ? 6.989   -56.768 -2.493  1.00 50.28 ?  36  PRO A O   1 
ATOM   96   C CB  . PRO A 1 24  ? 6.048   -59.694 -3.094  1.00 51.32 ?  36  PRO A CB  1 
ATOM   97   C CG  . PRO A 1 24  ? 6.228   -60.946 -3.895  1.00 51.58 ?  36  PRO A CG  1 
ATOM   98   C CD  . PRO A 1 24  ? 7.369   -60.663 -4.836  1.00 57.06 ?  36  PRO A CD  1 
ATOM   99   N N   . PHE A 1 25  ? 8.775   -57.704 -3.528  1.00 48.48 ?  37  PHE A N   1 
ATOM   100  C CA  . PHE A 1 25  ? 9.730   -56.753 -2.967  1.00 47.99 ?  37  PHE A CA  1 
ATOM   101  C C   . PHE A 1 25  ? 9.368   -55.312 -3.317  1.00 48.98 ?  37  PHE A C   1 
ATOM   102  O O   . PHE A 1 25  ? 9.631   -54.397 -2.525  1.00 45.90 ?  37  PHE A O   1 
ATOM   103  C CB  . PHE A 1 25  ? 11.138  -57.103 -3.455  1.00 44.18 ?  37  PHE A CB  1 
ATOM   104  C CG  . PHE A 1 25  ? 12.247  -56.373 -2.728  1.00 55.47 ?  37  PHE A CG  1 
ATOM   105  C CD1 . PHE A 1 25  ? 12.729  -56.844 -1.509  1.00 53.41 ?  37  PHE A CD1 1 
ATOM   106  C CD2 . PHE A 1 25  ? 12.827  -55.225 -3.277  1.00 52.09 ?  37  PHE A CD2 1 
ATOM   107  C CE1 . PHE A 1 25  ? 13.767  -56.182 -0.842  1.00 52.34 ?  37  PHE A CE1 1 
ATOM   108  C CE2 . PHE A 1 25  ? 13.868  -54.562 -2.630  1.00 48.34 ?  37  PHE A CE2 1 
ATOM   109  C CZ  . PHE A 1 25  ? 14.338  -55.041 -1.404  1.00 54.15 ?  37  PHE A CZ  1 
ATOM   110  N N   . TYR A 1 26  ? 8.744   -55.091 -4.476  1.00 43.97 ?  38  TYR A N   1 
ATOM   111  C CA  . TYR A 1 26  ? 8.389   -53.753 -4.927  1.00 40.62 ?  38  TYR A CA  1 
ATOM   112  C C   . TYR A 1 26  ? 7.011   -53.310 -4.460  1.00 42.26 ?  38  TYR A C   1 
ATOM   113  O O   . TYR A 1 26  ? 6.634   -52.157 -4.698  1.00 43.38 ?  38  TYR A O   1 
ATOM   114  C CB  . TYR A 1 26  ? 8.463   -53.679 -6.465  1.00 39.78 ?  38  TYR A CB  1 
ATOM   115  C CG  . TYR A 1 26  ? 9.876   -53.710 -7.030  1.00 36.44 ?  38  TYR A CG  1 
ATOM   116  C CD1 . TYR A 1 26  ? 10.618  -54.881 -7.034  1.00 39.59 ?  38  TYR A CD1 1 
ATOM   117  C CD2 . TYR A 1 26  ? 10.470  -52.555 -7.551  1.00 36.23 ?  38  TYR A CD2 1 
ATOM   118  C CE1 . TYR A 1 26  ? 11.919  -54.915 -7.544  1.00 38.92 ?  38  TYR A CE1 1 
ATOM   119  C CE2 . TYR A 1 26  ? 11.772  -52.573 -8.062  1.00 31.07 ?  38  TYR A CE2 1 
ATOM   120  C CZ  . TYR A 1 26  ? 12.487  -53.760 -8.061  1.00 34.70 ?  38  TYR A CZ  1 
ATOM   121  O OH  . TYR A 1 26  ? 13.772  -53.803 -8.563  1.00 34.45 ?  38  TYR A OH  1 
ATOM   122  N N   . LYS A 1 27  ? 6.245   -54.182 -3.812  1.00 47.01 ?  39  LYS A N   1 
ATOM   123  C CA  . LYS A 1 27  ? 4.904   -53.791 -3.405  1.00 45.46 ?  39  LYS A CA  1 
ATOM   124  C C   . LYS A 1 27  ? 4.965   -52.962 -2.126  1.00 47.57 ?  39  LYS A C   1 
ATOM   125  O O   . LYS A 1 27  ? 5.915   -53.038 -1.344  1.00 48.24 ?  39  LYS A O   1 
ATOM   126  C CB  . LYS A 1 27  ? 3.995   -55.013 -3.197  1.00 44.20 ?  39  LYS A CB  1 
ATOM   127  C CG  . LYS A 1 27  ? 4.056   -56.117 -4.281  1.00 53.10 ?  39  LYS A CG  1 
ATOM   128  C CD  . LYS A 1 27  ? 3.322   -55.765 -5.608  1.00 59.94 ?  39  LYS A CD  1 
ATOM   129  C CE  . LYS A 1 27  ? 4.079   -56.202 -6.910  1.00 53.25 ?  39  LYS A CE  1 
ATOM   130  N NZ  . LYS A 1 27  ? 5.462   -55.639 -7.111  1.00 51.33 ?  39  LYS A NZ  1 
ATOM   131  N N   . THR A 1 28  ? 3.934   -52.155 -1.926  1.00 48.17 ?  40  THR A N   1 
ATOM   132  C CA  . THR A 1 28  ? 3.863   -51.286 -0.767  1.00 49.18 ?  40  THR A CA  1 
ATOM   133  C C   . THR A 1 28  ? 2.966   -51.924 0.283   1.00 52.68 ?  40  THR A C   1 
ATOM   134  O O   . THR A 1 28  ? 1.760   -52.081 0.035   1.00 52.68 ?  40  THR A O   1 
ATOM   135  C CB  . THR A 1 28  ? 3.327   -49.918 -1.176  1.00 47.38 ?  40  THR A CB  1 
ATOM   136  O OG1 . THR A 1 28  ? 4.309   -49.256 -1.981  1.00 48.58 ?  40  THR A OG1 1 
ATOM   137  C CG2 . THR A 1 28  ? 2.999   -49.065 0.047   1.00 45.23 ?  40  THR A CG2 1 
ATOM   138  N N   . PRO A 1 29  ? 3.486   -52.291 1.456   1.00 56.73 ?  41  PRO A N   1 
ATOM   139  C CA  . PRO A 1 29  ? 2.671   -53.012 2.444   1.00 51.32 ?  41  PRO A CA  1 
ATOM   140  C C   . PRO A 1 29  ? 1.592   -52.122 3.043   1.00 57.30 ?  41  PRO A C   1 
ATOM   141  O O   . PRO A 1 29  ? 1.659   -50.889 2.996   1.00 55.04 ?  41  PRO A O   1 
ATOM   142  C CB  . PRO A 1 29  ? 3.695   -53.421 3.502   1.00 54.80 ?  41  PRO A CB  1 
ATOM   143  C CG  . PRO A 1 29  ? 4.705   -52.316 3.457   1.00 53.67 ?  41  PRO A CG  1 
ATOM   144  C CD  . PRO A 1 29  ? 4.796   -51.902 2.003   1.00 50.68 ?  41  PRO A CD  1 
ATOM   145  N N   . SER A 1 30  ? 0.572   -52.769 3.622   1.00 59.48 ?  42  SER A N   1 
ATOM   146  C CA  . SER A 1 30  ? -0.562  -52.003 4.141   1.00 60.16 ?  42  SER A CA  1 
ATOM   147  C C   . SER A 1 30  ? -0.168  -51.158 5.346   1.00 54.51 ?  42  SER A C   1 
ATOM   148  O O   . SER A 1 30  ? -0.778  -50.113 5.592   1.00 54.96 ?  42  SER A O   1 
ATOM   149  C CB  . SER A 1 30  ? -1.731  -52.932 4.492   1.00 61.37 ?  42  SER A CB  1 
ATOM   150  O OG  . SER A 1 30  ? -1.278  -54.186 4.973   1.00 72.34 ?  42  SER A OG  1 
ATOM   151  N N   . ASN A 1 31  ? 0.851   -51.582 6.094   1.00 56.36 ?  43  ASN A N   1 
ATOM   152  C CA  . ASN A 1 31  ? 1.347   -50.846 7.249   1.00 53.02 ?  43  ASN A CA  1 
ATOM   153  C C   . ASN A 1 31  ? 2.380   -49.778 6.864   1.00 53.77 ?  43  ASN A C   1 
ATOM   154  O O   . ASN A 1 31  ? 3.100   -49.282 7.740   1.00 49.24 ?  43  ASN A O   1 
ATOM   155  C CB  . ASN A 1 31  ? 1.934   -51.827 8.273   1.00 42.63 ?  43  ASN A CB  1 
ATOM   156  C CG  . ASN A 1 31  ? 3.156   -52.568 7.741   1.00 52.97 ?  43  ASN A CG  1 
ATOM   157  O OD1 . ASN A 1 31  ? 3.474   -52.489 6.554   1.00 56.98 ?  43  ASN A OD1 1 
ATOM   158  N ND2 . ASN A 1 31  ? 3.845   -53.288 8.616   1.00 49.63 ?  43  ASN A ND2 1 
ATOM   159  N N   . ILE A 1 32  ? 2.451   -49.408 5.576   1.00 53.44 ?  44  ILE A N   1 
ATOM   160  C CA  . ILE A 1 32  ? 3.466   -48.458 5.116   1.00 54.75 ?  44  ILE A CA  1 
ATOM   161  C C   . ILE A 1 32  ? 3.393   -47.160 5.918   1.00 48.61 ?  44  ILE A C   1 
ATOM   162  O O   . ILE A 1 32  ? 4.421   -46.569 6.258   1.00 48.94 ?  44  ILE A O   1 
ATOM   163  C CB  . ILE A 1 32  ? 3.332   -48.203 3.596   1.00 47.24 ?  44  ILE A CB  1 
ATOM   164  C CG1 . ILE A 1 32  ? 4.519   -47.385 3.066   1.00 37.83 ?  44  ILE A CG1 1 
ATOM   165  C CG2 . ILE A 1 32  ? 2.030   -47.489 3.259   1.00 42.24 ?  44  ILE A CG2 1 
ATOM   166  C CD1 . ILE A 1 32  ? 5.802   -48.171 2.966   1.00 40.71 ?  44  ILE A CD1 1 
ATOM   167  N N   . GLY A 1 33  ? 2.182   -46.721 6.268   1.00 52.96 ?  45  GLY A N   1 
ATOM   168  C CA  . GLY A 1 33  ? 2.008   -45.474 6.998   1.00 51.72 ?  45  GLY A CA  1 
ATOM   169  C C   . GLY A 1 33  ? 2.726   -45.403 8.337   1.00 55.46 ?  45  GLY A C   1 
ATOM   170  O O   . GLY A 1 33  ? 2.947   -44.296 8.846   1.00 54.31 ?  45  GLY A O   1 
ATOM   171  N N   . THR A 1 34  ? 3.096   -46.552 8.918   1.00 51.22 ?  46  THR A N   1 
ATOM   172  C CA  . THR A 1 34  ? 3.777   -46.603 10.210  1.00 54.13 ?  46  THR A CA  1 
ATOM   173  C C   . THR A 1 34  ? 5.298   -46.579 10.098  1.00 51.54 ?  46  THR A C   1 
ATOM   174  O O   . THR A 1 34  ? 5.974   -46.578 11.131  1.00 53.73 ?  46  THR A O   1 
ATOM   175  C CB  . THR A 1 34  ? 3.372   -47.860 11.007  1.00 50.30 ?  46  THR A CB  1 
ATOM   176  O OG1 . THR A 1 34  ? 4.026   -49.022 10.469  1.00 43.44 ?  46  THR A OG1 1 
ATOM   177  C CG2 . THR A 1 34  ? 1.851   -48.051 11.012  1.00 51.53 ?  46  THR A CG2 1 
ATOM   178  N N   . TYR A 1 35  ? 5.857   -46.602 8.891   1.00 48.68 ?  47  TYR A N   1 
ATOM   179  C CA  . TYR A 1 35  ? 7.293   -46.420 8.716   1.00 47.74 ?  47  TYR A CA  1 
ATOM   180  C C   . TYR A 1 35  ? 7.585   -44.930 8.556   1.00 52.17 ?  47  TYR A C   1 
ATOM   181  O O   . TYR A 1 35  ? 6.795   -44.196 7.953   1.00 50.38 ?  47  TYR A O   1 
ATOM   182  C CB  . TYR A 1 35  ? 7.804   -47.181 7.493   1.00 46.46 ?  47  TYR A CB  1 
ATOM   183  C CG  . TYR A 1 35  ? 7.859   -48.703 7.582   1.00 49.63 ?  47  TYR A CG  1 
ATOM   184  C CD1 . TYR A 1 35  ? 6.701   -49.481 7.472   1.00 49.33 ?  47  TYR A CD1 1 
ATOM   185  C CD2 . TYR A 1 35  ? 9.080   -49.360 7.703   1.00 46.99 ?  47  TYR A CD2 1 
ATOM   186  C CE1 . TYR A 1 35  ? 6.760   -50.877 7.519   1.00 47.47 ?  47  TYR A CE1 1 
ATOM   187  C CE2 . TYR A 1 35  ? 9.153   -50.743 7.745   1.00 50.42 ?  47  TYR A CE2 1 
ATOM   188  C CZ  . TYR A 1 35  ? 7.992   -51.501 7.656   1.00 52.07 ?  47  TYR A CZ  1 
ATOM   189  O OH  . TYR A 1 35  ? 8.084   -52.884 7.708   1.00 45.80 ?  47  TYR A OH  1 
ATOM   190  N N   . ALA A 1 36  ? 8.708   -44.479 9.115   1.00 49.69 ?  48  ALA A N   1 
ATOM   191  C CA  . ALA A 1 36  ? 9.118   -43.099 8.902   1.00 44.71 ?  48  ALA A CA  1 
ATOM   192  C C   . ALA A 1 36  ? 9.779   -42.958 7.536   1.00 48.29 ?  48  ALA A C   1 
ATOM   193  O O   . ALA A 1 36  ? 10.282  -43.932 6.957   1.00 46.39 ?  48  ALA A O   1 
ATOM   194  C CB  . ALA A 1 36  ? 10.084  -42.634 9.989   1.00 41.38 ?  48  ALA A CB  1 
ATOM   195  N N   . ASN A 1 37  ? 9.778   -41.727 7.019   1.00 44.20 ?  49  ASN A N   1 
ATOM   196  C CA  . ASN A 1 37  ? 10.487  -41.465 5.771   1.00 44.82 ?  49  ASN A CA  1 
ATOM   197  C C   . ASN A 1 37  ? 11.934  -41.926 5.914   1.00 41.53 ?  49  ASN A C   1 
ATOM   198  O O   . ASN A 1 37  ? 12.609  -41.590 6.889   1.00 49.89 ?  49  ASN A O   1 
ATOM   199  C CB  . ASN A 1 37  ? 10.410  -39.972 5.414   1.00 37.87 ?  49  ASN A CB  1 
ATOM   200  C CG  . ASN A 1 37  ? 9.031   -39.557 4.881   1.00 44.41 ?  49  ASN A CG  1 
ATOM   201  O OD1 . ASN A 1 37  ? 8.409   -40.271 4.070   1.00 44.26 ?  49  ASN A OD1 1 
ATOM   202  N ND2 . ASN A 1 37  ? 8.541   -38.402 5.342   1.00 37.82 ?  49  ASN A ND2 1 
ATOM   203  N N   . GLY A 1 38  ? 12.388  -42.754 4.980   1.00 40.69 ?  50  GLY A N   1 
ATOM   204  C CA  . GLY A 1 38  ? 13.738  -43.270 5.021   1.00 38.98 ?  50  GLY A CA  1 
ATOM   205  C C   . GLY A 1 38  ? 13.910  -44.597 5.735   1.00 40.99 ?  50  GLY A C   1 
ATOM   206  O O   . GLY A 1 38  ? 14.925  -45.275 5.515   1.00 42.31 ?  50  GLY A O   1 
ATOM   207  N N   . GLN A 1 39  ? 12.950  -45.000 6.569   1.00 43.94 ?  51  GLN A N   1 
ATOM   208  C CA  . GLN A 1 39  ? 13.081  -46.259 7.298   1.00 46.99 ?  51  GLN A CA  1 
ATOM   209  C C   . GLN A 1 39  ? 13.118  -47.454 6.347   1.00 45.99 ?  51  GLN A C   1 
ATOM   210  O O   . GLN A 1 39  ? 12.374  -47.513 5.366   1.00 46.24 ?  51  GLN A O   1 
ATOM   211  C CB  . GLN A 1 39  ? 11.927  -46.421 8.284   1.00 47.78 ?  51  GLN A CB  1 
ATOM   212  C CG  . GLN A 1 39  ? 12.237  -47.409 9.407   1.00 51.38 ?  51  GLN A CG  1 
ATOM   213  C CD  . GLN A 1 39  ? 11.025  -47.722 10.266  1.00 53.23 ?  51  GLN A CD  1 
ATOM   214  O OE1 . GLN A 1 39  ? 10.206  -46.837 10.571  1.00 53.69 ?  51  GLN A OE1 1 
ATOM   215  N NE2 . GLN A 1 39  ? 10.900  -48.990 10.666  1.00 49.89 ?  51  GLN A NE2 1 
ATOM   216  N N   . VAL A 1 40  ? 13.978  -48.419 6.658   1.00 41.30 ?  52  VAL A N   1 
ATOM   217  C CA  . VAL A 1 40  ? 14.174  -49.595 5.817   1.00 43.14 ?  52  VAL A CA  1 
ATOM   218  C C   . VAL A 1 40  ? 13.077  -50.625 6.088   1.00 51.91 ?  52  VAL A C   1 
ATOM   219  O O   . VAL A 1 40  ? 12.914  -51.090 7.221   1.00 51.42 ?  52  VAL A O   1 
ATOM   220  C CB  . VAL A 1 40  ? 15.557  -50.208 6.055   1.00 41.05 ?  52  VAL A CB  1 
ATOM   221  C CG1 . VAL A 1 40  ? 15.629  -51.569 5.405   1.00 45.04 ?  52  VAL A CG1 1 
ATOM   222  C CG2 . VAL A 1 40  ? 16.639  -49.302 5.502   1.00 42.66 ?  52  VAL A CG2 1 
ATOM   223  N N   . ILE A 1 41  ? 12.332  -51.000 5.041   1.00 51.22 ?  53  ILE A N   1 
ATOM   224  C CA  . ILE A 1 41  ? 11.319  -52.050 5.170   1.00 48.86 ?  53  ILE A CA  1 
ATOM   225  C C   . ILE A 1 41  ? 11.960  -53.432 5.084   1.00 44.79 ?  53  ILE A C   1 
ATOM   226  O O   . ILE A 1 41  ? 11.608  -54.338 5.845   1.00 44.80 ?  53  ILE A O   1 
ATOM   227  C CB  . ILE A 1 41  ? 10.209  -51.873 4.111   1.00 52.91 ?  53  ILE A CB  1 
ATOM   228  C CG1 . ILE A 1 41  ? 9.620   -50.460 4.182   1.00 49.83 ?  53  ILE A CG1 1 
ATOM   229  C CG2 . ILE A 1 41  ? 9.079   -52.898 4.315   1.00 46.73 ?  53  ILE A CG2 1 
ATOM   230  C CD1 . ILE A 1 41  ? 8.862   -50.061 2.943   1.00 47.55 ?  53  ILE A CD1 1 
ATOM   231  N N   . GLN A 1 42  ? 12.900  -53.615 4.163   1.00 44.35 ?  54  GLN A N   1 
ATOM   232  C CA  . GLN A 1 42  ? 13.670  -54.849 4.045   1.00 47.21 ?  54  GLN A CA  1 
ATOM   233  C C   . GLN A 1 42  ? 14.795  -54.599 3.054   1.00 44.25 ?  54  GLN A C   1 
ATOM   234  O O   . GLN A 1 42  ? 14.831  -53.575 2.364   1.00 45.96 ?  54  GLN A O   1 
ATOM   235  C CB  . GLN A 1 42  ? 12.816  -56.042 3.592   1.00 53.18 ?  54  GLN A CB  1 
ATOM   236  C CG  . GLN A 1 42  ? 11.884  -55.736 2.423   1.00 51.74 ?  54  GLN A CG  1 
ATOM   237  C CD  . GLN A 1 42  ? 11.483  -56.977 1.640   1.00 60.14 ?  54  GLN A CD  1 
ATOM   238  O OE1 . GLN A 1 42  ? 12.219  -57.973 1.597   1.00 62.43 ?  54  GLN A OE1 1 
ATOM   239  N NE2 . GLN A 1 42  ? 10.319  -56.913 0.995   1.00 53.70 ?  54  GLN A NE2 1 
ATOM   240  N N   . SER A 1 43  ? 15.703  -55.562 2.982   1.00 45.81 ?  55  SER A N   1 
ATOM   241  C CA  . SER A 1 43  ? 16.893  -55.464 2.161   1.00 43.64 ?  55  SER A CA  1 
ATOM   242  C C   . SER A 1 43  ? 17.204  -56.838 1.587   1.00 47.13 ?  55  SER A C   1 
ATOM   243  O O   . SER A 1 43  ? 16.631  -57.848 2.001   1.00 51.30 ?  55  SER A O   1 
ATOM   244  C CB  . SER A 1 43  ? 18.080  -54.965 2.978   1.00 48.25 ?  55  SER A CB  1 
ATOM   245  O OG  . SER A 1 43  ? 18.345  -55.880 4.024   1.00 44.60 ?  55  SER A OG  1 
ATOM   246  N N   . ARG A 1 44  ? 18.142  -56.878 0.646   1.00 40.74 ?  56  ARG A N   1 
ATOM   247  C CA  . ARG A 1 44  ? 18.572  -58.142 0.073   1.00 38.28 ?  56  ARG A CA  1 
ATOM   248  C C   . ARG A 1 44  ? 19.814  -57.890 -0.755  1.00 45.93 ?  56  ARG A C   1 
ATOM   249  O O   . ARG A 1 44  ? 19.960  -56.824 -1.357  1.00 49.42 ?  56  ARG A O   1 
ATOM   250  C CB  . ARG A 1 44  ? 17.479  -58.783 -0.798  1.00 46.88 ?  56  ARG A CB  1 
ATOM   251  C CG  . ARG A 1 44  ? 16.761  -57.853 -1.774  1.00 50.66 ?  56  ARG A CG  1 
ATOM   252  C CD  . ARG A 1 44  ? 15.954  -58.660 -2.776  1.00 46.10 ?  56  ARG A CD  1 
ATOM   253  N NE  . ARG A 1 44  ? 15.019  -57.858 -3.555  1.00 52.84 ?  56  ARG A NE  1 
ATOM   254  C CZ  . ARG A 1 44  ? 14.479  -58.256 -4.702  1.00 53.94 ?  56  ARG A CZ  1 
ATOM   255  N NH1 . ARG A 1 44  ? 14.761  -59.437 -5.223  1.00 56.73 ?  56  ARG A NH1 1 
ATOM   256  N NH2 . ARG A 1 44  ? 13.645  -57.446 -5.347  1.00 49.95 ?  56  ARG A NH2 1 
ATOM   257  N N   . LYS A 1 45  ? 20.708  -58.871 -0.778  1.00 42.64 ?  57  LYS A N   1 
ATOM   258  C CA  . LYS A 1 45  ? 21.851  -58.745 -1.658  1.00 44.91 ?  57  LYS A CA  1 
ATOM   259  C C   . LYS A 1 45  ? 21.371  -58.764 -3.104  1.00 48.91 ?  57  LYS A C   1 
ATOM   260  O O   . LYS A 1 45  ? 20.310  -59.309 -3.428  1.00 46.77 ?  57  LYS A O   1 
ATOM   261  C CB  . LYS A 1 45  ? 22.879  -59.847 -1.397  1.00 44.22 ?  57  LYS A CB  1 
ATOM   262  C CG  . LYS A 1 45  ? 24.275  -59.482 -1.906  1.00 47.81 ?  57  LYS A CG  1 
ATOM   263  C CD  . LYS A 1 45  ? 25.355  -60.410 -1.359  1.00 58.73 ?  57  LYS A CD  1 
ATOM   264  C CE  . LYS A 1 45  ? 26.752  -59.817 -1.561  1.00 61.59 ?  57  LYS A CE  1 
ATOM   265  N NZ  . LYS A 1 45  ? 27.779  -60.382 -0.630  1.00 61.53 ?  57  LYS A NZ  1 
ATOM   266  N N   . ALA A 1 46  ? 22.134  -58.112 -3.963  1.00 44.39 ?  58  ALA A N   1 
ATOM   267  C CA  . ALA A 1 46  ? 21.703  -57.946 -5.339  1.00 49.93 ?  58  ALA A CA  1 
ATOM   268  C C   . ALA A 1 46  ? 22.902  -58.134 -6.245  1.00 48.54 ?  58  ALA A C   1 
ATOM   269  O O   . ALA A 1 46  ? 23.898  -57.412 -6.121  1.00 50.00 ?  58  ALA A O   1 
ATOM   270  C CB  . ALA A 1 46  ? 21.059  -56.575 -5.561  1.00 46.71 ?  58  ALA A CB  1 
ATOM   271  N N   . PRO A 1 47  ? 22.862  -59.113 -7.150  1.00 52.08 ?  59  PRO A N   1 
ATOM   272  C CA  . PRO A 1 47  ? 23.996  -59.335 -8.054  1.00 52.28 ?  59  PRO A CA  1 
ATOM   273  C C   . PRO A 1 47  ? 23.989  -58.262 -9.133  1.00 52.05 ?  59  PRO A C   1 
ATOM   274  O O   . PRO A 1 47  ? 23.041  -58.160 -9.918  1.00 51.56 ?  59  PRO A O   1 
ATOM   275  C CB  . PRO A 1 47  ? 23.722  -60.730 -8.633  1.00 50.54 ?  59  PRO A CB  1 
ATOM   276  C CG  . PRO A 1 47  ? 22.539  -61.272 -7.847  1.00 45.90 ?  59  PRO A CG  1 
ATOM   277  C CD  . PRO A 1 47  ? 21.775  -60.067 -7.411  1.00 50.67 ?  59  PRO A CD  1 
ATOM   278  N N   . THR A 1 48  ? 25.028  -57.438 -9.149  1.00 47.23 ?  60  THR A N   1 
ATOM   279  C CA  . THR A 1 48  ? 25.078  -56.302 -10.051 1.00 47.13 ?  60  THR A CA  1 
ATOM   280  C C   . THR A 1 48  ? 26.393  -56.350 -10.809 1.00 48.76 ?  60  THR A C   1 
ATOM   281  O O   . THR A 1 48  ? 27.411  -56.783 -10.260 1.00 45.13 ?  60  THR A O   1 
ATOM   282  C CB  . THR A 1 48  ? 24.914  -54.962 -9.283  1.00 48.09 ?  60  THR A CB  1 
ATOM   283  O OG1 . THR A 1 48  ? 25.967  -54.809 -8.315  1.00 48.69 ?  60  THR A OG1 1 
ATOM   284  C CG2 . THR A 1 48  ? 23.555  -54.897 -8.573  1.00 37.36 ?  60  THR A CG2 1 
ATOM   285  N N   . ASP A 1 49  ? 26.356  -55.955 -12.089 1.00 44.18 ?  61  ASP A N   1 
ATOM   286  C CA  . ASP A 1 49  ? 27.589  -55.892 -12.863 1.00 45.43 ?  61  ASP A CA  1 
ATOM   287  C C   . ASP A 1 49  ? 28.578  -54.921 -12.228 1.00 49.68 ?  61  ASP A C   1 
ATOM   288  O O   . ASP A 1 49  ? 29.779  -55.202 -12.155 1.00 52.74 ?  61  ASP A O   1 
ATOM   289  C CB  . ASP A 1 49  ? 27.297  -55.466 -14.300 1.00 51.98 ?  61  ASP A CB  1 
ATOM   290  C CG  . ASP A 1 49  ? 26.350  -56.407 -15.019 1.00 54.68 ?  61  ASP A CG  1 
ATOM   291  O OD1 . ASP A 1 49  ? 26.598  -57.628 -15.003 1.00 58.15 ?  61  ASP A OD1 1 
ATOM   292  O OD2 . ASP A 1 49  ? 25.366  -55.916 -15.615 1.00 49.94 ?  61  ASP A OD2 1 
ATOM   293  N N   . ILE A 1 50  ? 28.091  -53.768 -11.770 1.00 49.40 ?  62  ILE A N   1 
ATOM   294  C CA  . ILE A 1 50  ? 28.978  -52.757 -11.200 1.00 50.59 ?  62  ILE A CA  1 
ATOM   295  C C   . ILE A 1 50  ? 29.600  -53.277 -9.907  1.00 46.52 ?  62  ILE A C   1 
ATOM   296  O O   . ILE A 1 50  ? 30.826  -53.234 -9.726  1.00 40.08 ?  62  ILE A O   1 
ATOM   297  C CB  . ILE A 1 50  ? 28.201  -51.445 -10.981 1.00 46.56 ?  62  ILE A CB  1 
ATOM   298  C CG1 . ILE A 1 50  ? 28.103  -50.662 -12.285 1.00 38.21 ?  62  ILE A CG1 1 
ATOM   299  C CG2 . ILE A 1 50  ? 28.849  -50.585 -9.909  1.00 47.68 ?  62  ILE A CG2 1 
ATOM   300  C CD1 . ILE A 1 50  ? 26.917  -49.730 -12.305 1.00 36.15 ?  62  ILE A CD1 1 
ATOM   301  N N   . GLY A 1 51  ? 28.759  -53.814 -9.012  1.00 44.96 ?  63  GLY A N   1 
ATOM   302  C CA  . GLY A 1 51  ? 29.258  -54.389 -7.771  1.00 50.07 ?  63  GLY A CA  1 
ATOM   303  C C   . GLY A 1 51  ? 30.293  -55.476 -8.002  1.00 56.35 ?  63  GLY A C   1 
ATOM   304  O O   . GLY A 1 51  ? 31.263  -55.595 -7.244  1.00 52.10 ?  63  GLY A O   1 
ATOM   305  N N   . ASN A 1 52  ? 30.112  -56.266 -9.067  1.00 50.30 ?  64  ASN A N   1 
ATOM   306  C CA  . ASN A 1 52  ? 31.078  -57.303 -9.409  1.00 52.82 ?  64  ASN A CA  1 
ATOM   307  C C   . ASN A 1 52  ? 32.396  -56.702 -9.885  1.00 52.52 ?  64  ASN A C   1 
ATOM   308  O O   . ASN A 1 52  ? 33.469  -57.131 -9.449  1.00 57.14 ?  64  ASN A O   1 
ATOM   309  C CB  . ASN A 1 52  ? 30.503  -58.234 -10.482 1.00 57.40 ?  64  ASN A CB  1 
ATOM   310  C CG  . ASN A 1 52  ? 29.435  -59.187 -9.940  1.00 56.31 ?  64  ASN A CG  1 
ATOM   311  O OD1 . ASN A 1 52  ? 29.229  -59.309 -8.729  1.00 54.90 ?  64  ASN A OD1 1 
ATOM   312  N ND2 . ASN A 1 52  ? 28.751  -59.867 -10.850 1.00 59.11 ?  64  ASN A ND2 1 
ATOM   313  N N   . GLN A 1 53  ? 32.338  -55.718 -10.792 1.00 50.68 ?  65  GLN A N   1 
ATOM   314  C CA  . GLN A 1 53  ? 33.551  -55.161 -11.391 1.00 50.27 ?  65  GLN A CA  1 
ATOM   315  C C   . GLN A 1 53  ? 34.424  -54.423 -10.387 1.00 51.71 ?  65  GLN A C   1 
ATOM   316  O O   . GLN A 1 53  ? 35.607  -54.193 -10.665 1.00 49.98 ?  65  GLN A O   1 
ATOM   317  C CB  . GLN A 1 53  ? 33.204  -54.199 -12.537 1.00 54.10 ?  65  GLN A CB  1 
ATOM   318  C CG  . GLN A 1 53  ? 33.099  -54.845 -13.918 1.00 61.63 ?  65  GLN A CG  1 
ATOM   319  C CD  . GLN A 1 53  ? 31.655  -55.005 -14.390 1.00 67.35 ?  65  GLN A CD  1 
ATOM   320  O OE1 . GLN A 1 53  ? 30.965  -54.020 -14.683 1.00 69.47 ?  65  GLN A OE1 1 
ATOM   321  N NE2 . GLN A 1 53  ? 31.186  -56.251 -14.440 1.00 68.44 ?  65  GLN A NE2 1 
ATOM   322  N N   . ASN A 1 54  ? 33.868  -54.024 -9.245  1.00 50.76 ?  66  ASN A N   1 
ATOM   323  C CA  . ASN A 1 54  ? 34.610  -53.297 -8.224  1.00 55.21 ?  66  ASN A CA  1 
ATOM   324  C C   . ASN A 1 54  ? 34.815  -54.122 -6.963  1.00 52.71 ?  66  ASN A C   1 
ATOM   325  O O   . ASN A 1 54  ? 35.324  -53.597 -5.969  1.00 54.98 ?  66  ASN A O   1 
ATOM   326  C CB  . ASN A 1 54  ? 33.902  -51.975 -7.891  1.00 49.36 ?  66  ASN A CB  1 
ATOM   327  C CG  . ASN A 1 54  ? 33.813  -51.040 -9.100  1.00 52.65 ?  66  ASN A CG  1 
ATOM   328  O OD1 . ASN A 1 54  ? 34.826  -50.519 -9.580  1.00 51.58 ?  66  ASN A OD1 1 
ATOM   329  N ND2 . ASN A 1 54  ? 32.600  -50.852 -9.614  1.00 52.67 ?  66  ASN A ND2 1 
ATOM   330  N N   . GLY A 1 55  ? 34.457  -55.404 -6.987  1.00 54.82 ?  67  GLY A N   1 
ATOM   331  C CA  . GLY A 1 55  ? 34.562  -56.230 -5.798  1.00 50.91 ?  67  GLY A CA  1 
ATOM   332  C C   . GLY A 1 55  ? 33.798  -55.667 -4.626  1.00 53.19 ?  67  GLY A C   1 
ATOM   333  O O   . GLY A 1 55  ? 34.219  -55.831 -3.474  1.00 57.05 ?  67  GLY A O   1 
ATOM   334  N N   . ALA A 1 56  ? 32.686  -54.989 -4.892  1.00 48.76 ?  68  ALA A N   1 
ATOM   335  C CA  . ALA A 1 56  ? 31.916  -54.303 -3.866  1.00 50.75 ?  68  ALA A CA  1 
ATOM   336  C C   . ALA A 1 56  ? 30.565  -54.975 -3.715  1.00 52.42 ?  68  ALA A C   1 
ATOM   337  O O   . ALA A 1 56  ? 29.884  -55.250 -4.711  1.00 56.76 ?  68  ALA A O   1 
ATOM   338  C CB  . ALA A 1 56  ? 31.729  -52.821 -4.210  1.00 49.20 ?  68  ALA A CB  1 
ATOM   339  N N   . ASP A 1 57  ? 30.182  -55.242 -2.474  1.00 44.96 ?  69  ASP A N   1 
ATOM   340  C CA  . ASP A 1 57  ? 28.848  -55.760 -2.232  1.00 49.85 ?  69  ASP A CA  1 
ATOM   341  C C   . ASP A 1 57  ? 27.808  -54.781 -2.756  1.00 54.33 ?  69  ASP A C   1 
ATOM   342  O O   . ASP A 1 57  ? 28.002  -53.562 -2.735  1.00 53.22 ?  69  ASP A O   1 
ATOM   343  C CB  . ASP A 1 57  ? 28.637  -56.005 -0.737  1.00 55.44 ?  69  ASP A CB  1 
ATOM   344  C CG  . ASP A 1 57  ? 29.449  -57.180 -0.219  1.00 59.09 ?  69  ASP A CG  1 
ATOM   345  O OD1 . ASP A 1 57  ? 30.134  -57.854 -1.022  1.00 63.19 ?  69  ASP A OD1 1 
ATOM   346  O OD2 . ASP A 1 57  ? 29.413  -57.424 1.000   1.00 67.25 ?  69  ASP A OD2 1 
ATOM   347  N N   . SER A 1 58  ? 26.703  -55.325 -3.252  1.00 55.65 ?  70  SER A N   1 
ATOM   348  C CA  . SER A 1 58  ? 25.557  -54.522 -3.640  1.00 48.65 ?  70  SER A CA  1 
ATOM   349  C C   . SER A 1 58  ? 24.310  -55.115 -3.016  1.00 46.82 ?  70  SER A C   1 
ATOM   350  O O   . SER A 1 58  ? 24.236  -56.319 -2.768  1.00 51.05 ?  70  SER A O   1 
ATOM   351  C CB  . SER A 1 58  ? 25.408  -54.423 -5.160  1.00 47.41 ?  70  SER A CB  1 
ATOM   352  O OG  . SER A 1 58  ? 25.526  -55.691 -5.774  1.00 52.10 ?  70  SER A OG  1 
ATOM   353  N N   . PHE A 1 59  ? 23.354  -54.243 -2.721  1.00 39.41 ?  71  PHE A N   1 
ATOM   354  C CA  . PHE A 1 59  ? 22.110  -54.634 -2.083  1.00 46.32 ?  71  PHE A CA  1 
ATOM   355  C C   . PHE A 1 59  ? 20.979  -53.800 -2.663  1.00 51.99 ?  71  PHE A C   1 
ATOM   356  O O   . PHE A 1 59  ? 21.191  -52.711 -3.206  1.00 48.63 ?  71  PHE A O   1 
ATOM   357  C CB  . PHE A 1 59  ? 22.117  -54.433 -0.545  1.00 49.03 ?  71  PHE A CB  1 
ATOM   358  C CG  . PHE A 1 59  ? 23.226  -55.160 0.177   1.00 55.17 ?  71  PHE A CG  1 
ATOM   359  C CD1 . PHE A 1 59  ? 24.555  -54.745 0.064   1.00 51.62 ?  71  PHE A CD1 1 
ATOM   360  C CD2 . PHE A 1 59  ? 22.937  -56.271 0.962   1.00 51.20 ?  71  PHE A CD2 1 
ATOM   361  C CE1 . PHE A 1 59  ? 25.571  -55.423 0.716   1.00 53.31 ?  71  PHE A CE1 1 
ATOM   362  C CE2 . PHE A 1 59  ? 23.951  -56.955 1.619   1.00 52.63 ?  71  PHE A CE2 1 
ATOM   363  C CZ  . PHE A 1 59  ? 25.271  -56.527 1.496   1.00 56.67 ?  71  PHE A CZ  1 
ATOM   364  N N   . GLN A 1 60  ? 19.766  -54.310 -2.521  1.00 45.84 ?  72  GLN A N   1 
ATOM   365  C CA  . GLN A 1 60  ? 18.587  -53.506 -2.760  1.00 45.50 ?  72  GLN A CA  1 
ATOM   366  C C   . GLN A 1 60  ? 17.985  -53.179 -1.408  1.00 45.86 ?  72  GLN A C   1 
ATOM   367  O O   . GLN A 1 60  ? 18.081  -53.971 -0.469  1.00 50.42 ?  72  GLN A O   1 
ATOM   368  C CB  . GLN A 1 60  ? 17.576  -54.238 -3.656  1.00 50.21 ?  72  GLN A CB  1 
ATOM   369  C CG  . GLN A 1 60  ? 18.063  -54.362 -5.108  1.00 49.59 ?  72  GLN A CG  1 
ATOM   370  C CD  . GLN A 1 60  ? 17.012  -54.907 -6.056  1.00 48.96 ?  72  GLN A CD  1 
ATOM   371  O OE1 . GLN A 1 60  ? 15.915  -55.299 -5.635  1.00 43.97 ?  72  GLN A OE1 1 
ATOM   372  N NE2 . GLN A 1 60  ? 17.346  -54.941 -7.351  1.00 45.87 ?  72  GLN A NE2 1 
ATOM   373  N N   . LEU A 1 61  ? 17.406  -51.992 -1.301  1.00 39.63 ?  73  LEU A N   1 
ATOM   374  C CA  . LEU A 1 61  ? 16.757  -51.560 -0.080  1.00 39.25 ?  73  LEU A CA  1 
ATOM   375  C C   . LEU A 1 61  ? 15.326  -51.200 -0.403  1.00 38.57 ?  73  LEU A C   1 
ATOM   376  O O   . LEU A 1 61  ? 15.072  -50.377 -1.281  1.00 43.08 ?  73  LEU A O   1 
ATOM   377  C CB  . LEU A 1 61  ? 17.447  -50.347 0.552   1.00 41.55 ?  73  LEU A CB  1 
ATOM   378  C CG  . LEU A 1 61  ? 18.947  -50.242 0.850   1.00 43.89 ?  73  LEU A CG  1 
ATOM   379  C CD1 . LEU A 1 61  ? 19.122  -49.239 1.978   1.00 46.89 ?  73  LEU A CD1 1 
ATOM   380  C CD2 . LEU A 1 61  ? 19.624  -51.570 1.196   1.00 44.61 ?  73  LEU A CD2 1 
ATOM   381  N N   . SER A 1 62  ? 14.402  -51.807 0.302   1.00 42.86 ?  74  SER A N   1 
ATOM   382  C CA  . SER A 1 62  ? 13.034  -51.340 0.289   1.00 43.27 ?  74  SER A CA  1 
ATOM   383  C C   . SER A 1 62  ? 12.861  -50.397 1.473   1.00 43.78 ?  74  SER A C   1 
ATOM   384  O O   . SER A 1 62  ? 13.327  -50.692 2.577   1.00 48.77 ?  74  SER A O   1 
ATOM   385  C CB  . SER A 1 62  ? 12.070  -52.524 0.358   1.00 43.79 ?  74  SER A CB  1 
ATOM   386  O OG  . SER A 1 62  ? 10.733  -52.079 0.301   1.00 47.74 ?  74  SER A OG  1 
ATOM   387  N N   . TYR A 1 63  ? 12.226  -49.253 1.237   1.00 42.88 ?  75  TYR A N   1 
ATOM   388  C CA  . TYR A 1 63  ? 12.181  -48.200 2.238   1.00 40.84 ?  75  TYR A CA  1 
ATOM   389  C C   . TYR A 1 63  ? 10.996  -47.299 1.952   1.00 39.80 ?  75  TYR A C   1 
ATOM   390  O O   . TYR A 1 63  ? 10.541  -47.183 0.811   1.00 43.80 ?  75  TYR A O   1 
ATOM   391  C CB  . TYR A 1 63  ? 13.474  -47.373 2.258   1.00 41.38 ?  75  TYR A CB  1 
ATOM   392  C CG  . TYR A 1 63  ? 13.702  -46.578 0.989   1.00 42.85 ?  75  TYR A CG  1 
ATOM   393  C CD1 . TYR A 1 63  ? 14.337  -47.156 -0.101  1.00 34.55 ?  75  TYR A CD1 1 
ATOM   394  C CD2 . TYR A 1 63  ? 13.263  -45.249 0.878   1.00 38.21 ?  75  TYR A CD2 1 
ATOM   395  C CE1 . TYR A 1 63  ? 14.536  -46.439 -1.272  1.00 41.17 ?  75  TYR A CE1 1 
ATOM   396  C CE2 . TYR A 1 63  ? 13.457  -44.520 -0.291  1.00 37.30 ?  75  TYR A CE2 1 
ATOM   397  C CZ  . TYR A 1 63  ? 14.096  -45.120 -1.364  1.00 39.75 ?  75  TYR A CZ  1 
ATOM   398  O OH  . TYR A 1 63  ? 14.300  -44.421 -2.537  1.00 34.14 ?  75  TYR A OH  1 
ATOM   399  N N   . ARG A 1 64  ? 10.505  -46.663 3.005   1.00 41.21 ?  76  ARG A N   1 
ATOM   400  C CA  . ARG A 1 64  ? 9.346   -45.801 2.888   1.00 41.32 ?  76  ARG A CA  1 
ATOM   401  C C   . ARG A 1 64  ? 9.783   -44.427 2.381   1.00 45.63 ?  76  ARG A C   1 
ATOM   402  O O   . ARG A 1 64  ? 10.865  -43.934 2.726   1.00 39.43 ?  76  ARG A O   1 
ATOM   403  C CB  . ARG A 1 64  ? 8.624   -45.697 4.233   1.00 38.16 ?  76  ARG A CB  1 
ATOM   404  C CG  . ARG A 1 64  ? 7.355   -44.842 4.191   1.00 44.98 ?  76  ARG A CG  1 
ATOM   405  C CD  . ARG A 1 64  ? 7.662   -43.413 4.615   1.00 43.13 ?  76  ARG A CD  1 
ATOM   406  N NE  . ARG A 1 64  ? 6.521   -42.512 4.526   1.00 42.04 ?  76  ARG A NE  1 
ATOM   407  C CZ  . ARG A 1 64  ? 5.857   -42.036 5.569   1.00 50.65 ?  76  ARG A CZ  1 
ATOM   408  N NH1 . ARG A 1 64  ? 6.125   -42.440 6.806   1.00 52.01 ?  76  ARG A NH1 1 
ATOM   409  N NH2 . ARG A 1 64  ? 4.902   -41.127 5.370   1.00 48.83 ?  76  ARG A NH2 1 
ATOM   410  N N   . THR A 1 65  ? 8.944   -43.830 1.532   1.00 41.02 ?  77  THR A N   1 
ATOM   411  C CA  . THR A 1 65  ? 9.138   -42.473 1.048   1.00 41.02 ?  77  THR A CA  1 
ATOM   412  C C   . THR A 1 65  ? 7.760   -41.825 0.945   1.00 36.60 ?  77  THR A C   1 
ATOM   413  O O   . THR A 1 65  ? 6.753   -42.391 1.376   1.00 36.29 ?  77  THR A O   1 
ATOM   414  C CB  . THR A 1 65  ? 9.927   -42.458 -0.272  1.00 40.50 ?  77  THR A CB  1 
ATOM   415  O OG1 . THR A 1 65  ? 10.167  -41.100 -0.660  1.00 38.78 ?  77  THR A OG1 1 
ATOM   416  C CG2 . THR A 1 65  ? 9.170   -43.185 -1.392  1.00 35.87 ?  77  THR A CG2 1 
ATOM   417  N N   . THR A 1 66  ? 7.704   -40.618 0.395   1.00 39.09 ?  78  THR A N   1 
ATOM   418  C CA  . THR A 1 66  ? 6.451   -39.866 0.312   1.00 45.49 ?  78  THR A CA  1 
ATOM   419  C C   . THR A 1 66  ? 6.201   -39.483 -1.143  1.00 39.11 ?  78  THR A C   1 
ATOM   420  O O   . THR A 1 66  ? 7.121   -39.028 -1.827  1.00 42.74 ?  78  THR A O   1 
ATOM   421  C CB  . THR A 1 66  ? 6.501   -38.614 1.217   1.00 41.73 ?  78  THR A CB  1 
ATOM   422  O OG1 . THR A 1 66  ? 6.359   -39.003 2.593   1.00 46.73 ?  78  THR A OG1 1 
ATOM   423  C CG2 . THR A 1 66  ? 5.414   -37.622 0.860   1.00 37.96 ?  78  THR A CG2 1 
ATOM   424  N N   . ASN A 1 67  ? 4.976   -39.679 -1.625  1.00 38.05 ?  79  ASN A N   1 
ATOM   425  C CA  . ASN A 1 67  ? 4.689   -39.351 -3.013  1.00 40.89 ?  79  ASN A CA  1 
ATOM   426  C C   . ASN A 1 67  ? 4.262   -37.885 -3.120  1.00 38.15 ?  79  ASN A C   1 
ATOM   427  O O   . ASN A 1 67  ? 4.258   -37.138 -2.141  1.00 39.08 ?  79  ASN A O   1 
ATOM   428  C CB  . ASN A 1 67  ? 3.666   -40.335 -3.603  1.00 38.67 ?  79  ASN A CB  1 
ATOM   429  C CG  . ASN A 1 67  ? 2.203   -40.032 -3.212  1.00 41.86 ?  79  ASN A CG  1 
ATOM   430  O OD1 . ASN A 1 67  ? 1.855   -38.963 -2.694  1.00 38.36 ?  79  ASN A OD1 1 
ATOM   431  N ND2 . ASN A 1 67  ? 1.334   -40.997 -3.489  1.00 41.38 ?  79  ASN A ND2 1 
ATOM   432  N N   . THR A 1 68  ? 3.877   -37.471 -4.325  1.00 38.19 ?  80  THR A N   1 
ATOM   433  C CA  . THR A 1 68  ? 3.556   -36.063 -4.564  1.00 40.22 ?  80  THR A CA  1 
ATOM   434  C C   . THR A 1 68  ? 2.326   -35.611 -3.774  1.00 41.35 ?  80  THR A C   1 
ATOM   435  O O   . THR A 1 68  ? 2.206   -34.427 -3.435  1.00 41.02 ?  80  THR A O   1 
ATOM   436  C CB  . THR A 1 68  ? 3.373   -35.843 -6.072  1.00 34.23 ?  80  THR A CB  1 
ATOM   437  O OG1 . THR A 1 68  ? 4.594   -36.186 -6.745  1.00 32.95 ?  80  THR A OG1 1 
ATOM   438  C CG2 . THR A 1 68  ? 3.000   -34.404 -6.400  1.00 31.60 ?  80  THR A CG2 1 
ATOM   439  N N   . GLN A 1 69  ? 1.413   -36.524 -3.452  1.00 40.72 ?  81  GLN A N   1 
ATOM   440  C CA  . GLN A 1 69  ? 0.205   -36.162 -2.717  1.00 44.20 ?  81  GLN A CA  1 
ATOM   441  C C   . GLN A 1 69  ? 0.412   -36.229 -1.208  1.00 44.03 ?  81  GLN A C   1 
ATOM   442  O O   . GLN A 1 69  ? -0.553  -36.060 -0.454  1.00 45.19 ?  81  GLN A O   1 
ATOM   443  C CB  . GLN A 1 69  ? -0.967  -37.063 -3.132  1.00 44.19 ?  81  GLN A CB  1 
ATOM   444  C CG  . GLN A 1 69  ? -1.584  -36.705 -4.478  1.00 43.14 ?  81  GLN A CG  1 
ATOM   445  C CD  . GLN A 1 69  ? -0.632  -36.988 -5.636  1.00 42.51 ?  81  GLN A CD  1 
ATOM   446  O OE1 . GLN A 1 69  ? -0.169  -38.121 -5.816  1.00 37.20 ?  81  GLN A OE1 1 
ATOM   447  N NE2 . GLN A 1 69  ? -0.308  -35.948 -6.406  1.00 39.56 ?  81  GLN A NE2 1 
ATOM   448  N N   . LYS A 1 70  ? 1.654   -36.473 -0.773  1.00 43.37 ?  82  LYS A N   1 
ATOM   449  C CA  . LYS A 1 70  ? 2.046   -36.592 0.628   1.00 46.02 ?  82  LYS A CA  1 
ATOM   450  C C   . LYS A 1 70  ? 1.566   -37.903 1.250   1.00 47.45 ?  82  LYS A C   1 
ATOM   451  O O   . LYS A 1 70  ? 1.272   -37.963 2.443   1.00 47.93 ?  82  LYS A O   1 
ATOM   452  C CB  . LYS A 1 70  ? 1.580   -35.381 1.444   1.00 37.88 ?  82  LYS A CB  1 
ATOM   453  C CG  . LYS A 1 70  ? 2.424   -34.143 1.139   1.00 49.19 ?  82  LYS A CG  1 
ATOM   454  C CD  . LYS A 1 70  ? 1.621   -32.853 1.155   1.00 51.01 ?  82  LYS A CD  1 
ATOM   455  C CE  . LYS A 1 70  ? 2.546   -31.627 1.119   1.00 65.14 ?  82  LYS A CE  1 
ATOM   456  N NZ  . LYS A 1 70  ? 1.807   -30.309 1.111   1.00 62.30 ?  82  LYS A NZ  1 
ATOM   457  N N   . GLU A 1 71  ? 1.496   -38.970 0.461   1.00 43.92 ?  83  GLU A N   1 
ATOM   458  C CA  . GLU A 1 71  ? 1.073   -40.273 0.952   1.00 39.65 ?  83  GLU A CA  1 
ATOM   459  C C   . GLU A 1 71  ? 2.265   -41.202 0.999   1.00 39.80 ?  83  GLU A C   1 
ATOM   460  O O   . GLU A 1 71  ? 3.127   -41.157 0.117   1.00 42.43 ?  83  GLU A O   1 
ATOM   461  C CB  . GLU A 1 71  ? 0.004   -40.900 0.069   1.00 38.80 ?  83  GLU A CB  1 
ATOM   462  C CG  . GLU A 1 71  ? -1.164  -39.999 -0.260  1.00 43.05 ?  83  GLU A CG  1 
ATOM   463  C CD  . GLU A 1 71  ? -1.914  -40.499 -1.480  1.00 53.42 ?  83  GLU A CD  1 
ATOM   464  O OE1 . GLU A 1 71  ? -1.314  -41.251 -2.295  1.00 49.27 ?  83  GLU A OE1 1 
ATOM   465  O OE2 . GLU A 1 71  ? -3.105  -40.150 -1.618  1.00 63.91 ?  83  GLU A OE2 1 
ATOM   466  N N   . ALA A 1 72  ? 2.308   -42.036 2.033   1.00 42.08 ?  84  ALA A N   1 
ATOM   467  C CA  . ALA A 1 72  ? 3.399   -42.985 2.184   1.00 42.62 ?  84  ALA A CA  1 
ATOM   468  C C   . ALA A 1 72  ? 3.340   -44.011 1.071   1.00 38.14 ?  84  ALA A C   1 
ATOM   469  O O   . ALA A 1 72  ? 2.261   -44.407 0.636   1.00 40.86 ?  84  ALA A O   1 
ATOM   470  C CB  . ALA A 1 72  ? 3.322   -43.690 3.534   1.00 40.48 ?  84  ALA A CB  1 
ATOM   471  N N   . GLN A 1 73  ? 4.511   -44.436 0.618   1.00 38.15 ?  85  GLN A N   1 
ATOM   472  C CA  . GLN A 1 73  ? 4.650   -45.492 -0.367  1.00 40.57 ?  85  GLN A CA  1 
ATOM   473  C C   . GLN A 1 73  ? 6.040   -46.075 -0.191  1.00 37.50 ?  85  GLN A C   1 
ATOM   474  O O   . GLN A 1 73  ? 6.921   -45.441 0.394   1.00 39.25 ?  85  GLN A O   1 
ATOM   475  C CB  . GLN A 1 73  ? 4.422   -44.964 -1.801  1.00 43.35 ?  85  GLN A CB  1 
ATOM   476  C CG  . GLN A 1 73  ? 5.652   -44.354 -2.515  1.00 37.90 ?  85  GLN A CG  1 
ATOM   477  C CD  . GLN A 1 73  ? 5.267   -43.530 -3.755  1.00 46.14 ?  85  GLN A CD  1 
ATOM   478  O OE1 . GLN A 1 73  ? 4.097   -43.495 -4.162  1.00 48.74 ?  85  GLN A OE1 1 
ATOM   479  N NE2 . GLN A 1 73  ? 6.255   -42.868 -4.357  1.00 39.06 ?  85  GLN A NE2 1 
ATOM   480  N N   . ALA A 1 74  ? 6.227   -47.291 -0.691  1.00 35.84 ?  86  ALA A N   1 
ATOM   481  C CA  . ALA A 1 74  ? 7.495   -47.992 -0.565  1.00 35.28 ?  86  ALA A CA  1 
ATOM   482  C C   . ALA A 1 74  ? 8.292   -47.861 -1.855  1.00 39.73 ?  86  ALA A C   1 
ATOM   483  O O   . ALA A 1 74  ? 7.726   -47.779 -2.948  1.00 43.15 ?  86  ALA A O   1 
ATOM   484  C CB  . ALA A 1 74  ? 7.265   -49.470 -0.243  1.00 38.76 ?  86  ALA A CB  1 
ATOM   485  N N   . ASN A 1 75  ? 9.614   -47.869 -1.730  1.00 36.50 ?  87  ASN A N   1 
ATOM   486  C CA  . ASN A 1 75  ? 10.464  -47.690 -2.895  1.00 35.98 ?  87  ASN A CA  1 
ATOM   487  C C   . ASN A 1 75  ? 11.721  -48.529 -2.734  1.00 36.29 ?  87  ASN A C   1 
ATOM   488  O O   . ASN A 1 75  ? 12.058  -48.981 -1.637  1.00 38.67 ?  87  ASN A O   1 
ATOM   489  C CB  . ASN A 1 75  ? 10.813  -46.207 -3.106  1.00 41.36 ?  87  ASN A CB  1 
ATOM   490  C CG  . ASN A 1 75  ? 11.319  -45.920 -4.507  1.00 39.21 ?  87  ASN A CG  1 
ATOM   491  O OD1 . ASN A 1 75  ? 10.911  -46.570 -5.465  1.00 39.98 ?  87  ASN A OD1 1 
ATOM   492  N ND2 . ASN A 1 75  ? 12.216  -44.943 -4.630  1.00 35.27 ?  87  ASN A ND2 1 
ATOM   493  N N   . VAL A 1 76  ? 12.413  -48.741 -3.846  1.00 38.53 ?  88  VAL A N   1 
ATOM   494  C CA  . VAL A 1 76  ? 13.652  -49.507 -3.857  1.00 39.73 ?  88  VAL A CA  1 
ATOM   495  C C   . VAL A 1 76  ? 14.783  -48.579 -4.265  1.00 39.30 ?  88  VAL A C   1 
ATOM   496  O O   . VAL A 1 76  ? 14.594  -47.682 -5.099  1.00 37.08 ?  88  VAL A O   1 
ATOM   497  C CB  . VAL A 1 76  ? 13.555  -50.733 -4.793  1.00 35.53 ?  88  VAL A CB  1 
ATOM   498  C CG1 . VAL A 1 76  ? 14.920  -51.404 -5.033  1.00 27.42 ?  88  VAL A CG1 1 
ATOM   499  C CG2 . VAL A 1 76  ? 12.562  -51.711 -4.224  1.00 40.98 ?  88  VAL A CG2 1 
ATOM   500  N N   . ALA A 1 77  ? 15.938  -48.764 -3.626  1.00 37.60 ?  89  ALA A N   1 
ATOM   501  C CA  . ALA A 1 77  ? 17.193  -48.159 -4.041  1.00 37.75 ?  89  ALA A CA  1 
ATOM   502  C C   . ALA A 1 77  ? 18.263  -49.242 -4.073  1.00 37.72 ?  89  ALA A C   1 
ATOM   503  O O   . ALA A 1 77  ? 18.103  -50.315 -3.493  1.00 38.68 ?  89  ALA A O   1 
ATOM   504  C CB  . ALA A 1 77  ? 17.611  -47.019 -3.102  1.00 37.36 ?  89  ALA A CB  1 
ATOM   505  N N   . THR A 1 78  ? 19.361  -48.944 -4.760  1.00 36.94 ?  90  THR A N   1 
ATOM   506  C CA  . THR A 1 78  ? 20.502  -49.838 -4.880  1.00 37.13 ?  90  THR A CA  1 
ATOM   507  C C   . THR A 1 78  ? 21.722  -49.190 -4.236  1.00 44.52 ?  90  THR A C   1 
ATOM   508  O O   . THR A 1 78  ? 22.044  -48.033 -4.533  1.00 41.50 ?  90  THR A O   1 
ATOM   509  C CB  . THR A 1 78  ? 20.793  -50.151 -6.343  1.00 35.50 ?  90  THR A CB  1 
ATOM   510  O OG1 . THR A 1 78  ? 19.601  -50.656 -6.946  1.00 39.45 ?  90  THR A OG1 1 
ATOM   511  C CG2 . THR A 1 78  ? 21.919  -51.171 -6.471  1.00 32.66 ?  90  THR A CG2 1 
ATOM   512  N N   . VAL A 1 79  ? 22.398  -49.935 -3.362  1.00 46.10 ?  91  VAL A N   1 
ATOM   513  C CA  . VAL A 1 79  ? 23.568  -49.448 -2.645  1.00 39.44 ?  91  VAL A CA  1 
ATOM   514  C C   . VAL A 1 79  ? 24.764  -50.328 -2.987  1.00 42.95 ?  91  VAL A C   1 
ATOM   515  O O   . VAL A 1 79  ? 24.649  -51.555 -3.055  1.00 45.57 ?  91  VAL A O   1 
ATOM   516  C CB  . VAL A 1 79  ? 23.319  -49.394 -1.122  1.00 41.67 ?  91  VAL A CB  1 
ATOM   517  C CG1 . VAL A 1 79  ? 22.131  -48.472 -0.801  1.00 37.44 ?  91  VAL A CG1 1 
ATOM   518  C CG2 . VAL A 1 79  ? 23.101  -50.786 -0.527  1.00 42.79 ?  91  VAL A CG2 1 
ATOM   519  N N   . PHE A 1 80  ? 25.899  -49.690 -3.254  1.00 45.92 ?  92  PHE A N   1 
ATOM   520  C CA  . PHE A 1 80  ? 27.176  -50.365 -3.441  1.00 45.29 ?  92  PHE A CA  1 
ATOM   521  C C   . PHE A 1 80  ? 28.070  -49.991 -2.264  1.00 48.19 ?  92  PHE A C   1 
ATOM   522  O O   . PHE A 1 80  ? 28.051  -48.846 -1.804  1.00 47.17 ?  92  PHE A O   1 
ATOM   523  C CB  . PHE A 1 80  ? 27.827  -49.982 -4.774  1.00 40.00 ?  92  PHE A CB  1 
ATOM   524  C CG  . PHE A 1 80  ? 26.901  -50.126 -5.957  1.00 46.22 ?  92  PHE A CG  1 
ATOM   525  C CD1 . PHE A 1 80  ? 25.844  -49.239 -6.149  1.00 45.26 ?  92  PHE A CD1 1 
ATOM   526  C CD2 . PHE A 1 80  ? 27.065  -51.164 -6.863  1.00 50.09 ?  92  PHE A CD2 1 
ATOM   527  C CE1 . PHE A 1 80  ? 24.982  -49.377 -7.214  1.00 43.09 ?  92  PHE A CE1 1 
ATOM   528  C CE2 . PHE A 1 80  ? 26.203  -51.307 -7.945  1.00 45.04 ?  92  PHE A CE2 1 
ATOM   529  C CZ  . PHE A 1 80  ? 25.165  -50.411 -8.123  1.00 42.47 ?  92  PHE A CZ  1 
ATOM   530  N N   . ILE A 1 81  ? 28.799  -50.974 -1.740  1.00 50.47 ?  93  ILE A N   1 
ATOM   531  C CA  . ILE A 1 81  ? 29.606  -50.801 -0.534  1.00 47.12 ?  93  ILE A CA  1 
ATOM   532  C C   . ILE A 1 81  ? 31.081  -50.964 -0.873  1.00 46.58 ?  93  ILE A C   1 
ATOM   533  O O   . ILE A 1 81  ? 31.539  -52.098 -1.071  1.00 54.24 ?  93  ILE A O   1 
ATOM   534  C CB  . ILE A 1 81  ? 29.194  -51.800 0.552   1.00 50.72 ?  93  ILE A CB  1 
ATOM   535  C CG1 . ILE A 1 81  ? 27.705  -51.635 0.872   1.00 50.44 ?  93  ILE A CG1 1 
ATOM   536  C CG2 . ILE A 1 81  ? 30.098  -51.652 1.772   1.00 48.68 ?  93  ILE A CG2 1 
ATOM   537  C CD1 . ILE A 1 81  ? 27.381  -50.336 1.556   1.00 52.99 ?  93  ILE A CD1 1 
ATOM   538  N N   . PRO A 1 82  ? 31.864  -49.887 -0.923  1.00 46.33 ?  94  PRO A N   1 
ATOM   539  C CA  . PRO A 1 82  ? 33.261  -50.025 -1.352  1.00 45.78 ?  94  PRO A CA  1 
ATOM   540  C C   . PRO A 1 82  ? 34.027  -50.943 -0.406  1.00 49.50 ?  94  PRO A C   1 
ATOM   541  O O   . PRO A 1 82  ? 33.761  -50.984 0.798   1.00 51.73 ?  94  PRO A O   1 
ATOM   542  C CB  . PRO A 1 82  ? 33.788  -48.587 -1.309  1.00 47.18 ?  94  PRO A CB  1 
ATOM   543  C CG  . PRO A 1 82  ? 32.957  -47.920 -0.247  1.00 43.97 ?  94  PRO A CG  1 
ATOM   544  C CD  . PRO A 1 82  ? 31.594  -48.575 -0.299  1.00 42.55 ?  94  PRO A CD  1 
ATOM   545  N N   . SER A 1 83  ? 34.962  -51.713 -0.966  1.00 55.68 ?  95  SER A N   1 
ATOM   546  C CA  . SER A 1 83  ? 35.720  -52.643 -0.135  1.00 57.86 ?  95  SER A CA  1 
ATOM   547  C C   . SER A 1 83  ? 36.501  -51.890 0.939   1.00 59.73 ?  95  SER A C   1 
ATOM   548  O O   . SER A 1 83  ? 36.390  -52.199 2.133   1.00 60.26 ?  95  SER A O   1 
ATOM   549  C CB  . SER A 1 83  ? 36.646  -53.510 -1.001  1.00 51.39 ?  95  SER A CB  1 
ATOM   550  O OG  . SER A 1 83  ? 37.281  -52.758 -2.015  1.00 54.01 ?  95  SER A OG  1 
ATOM   551  N N   . LYS A 1 84  ? 37.261  -50.865 0.542   1.00 54.51 ?  96  LYS A N   1 
ATOM   552  C CA  . LYS A 1 84  ? 37.960  -50.018 1.505   1.00 55.69 ?  96  LYS A CA  1 
ATOM   553  C C   . LYS A 1 84  ? 37.345  -48.617 1.567   1.00 55.09 ?  96  LYS A C   1 
ATOM   554  O O   . LYS A 1 84  ? 37.708  -47.743 0.759   1.00 51.35 ?  96  LYS A O   1 
ATOM   555  C CB  . LYS A 1 84  ? 39.452  -49.941 1.164   1.00 60.68 ?  96  LYS A CB  1 
ATOM   556  C CG  . LYS A 1 84  ? 39.788  -49.710 -0.307  1.00 67.20 ?  96  LYS A CG  1 
ATOM   557  C CD  . LYS A 1 84  ? 41.257  -50.055 -0.603  1.00 72.03 ?  96  LYS A CD  1 
ATOM   558  C CE  . LYS A 1 84  ? 41.883  -49.058 -1.579  1.00 76.61 ?  96  LYS A CE  1 
ATOM   559  N NZ  . LYS A 1 84  ? 42.719  -49.718 -2.626  1.00 72.25 ?  96  LYS A NZ  1 
ATOM   560  N N   . PRO A 1 85  ? 36.422  -48.350 2.504   1.00 47.96 ?  97  PRO A N   1 
ATOM   561  C CA  . PRO A 1 85  ? 35.794  -47.022 2.570   1.00 46.71 ?  97  PRO A CA  1 
ATOM   562  C C   . PRO A 1 85  ? 36.804  -45.924 2.866   1.00 55.32 ?  97  PRO A C   1 
ATOM   563  O O   . PRO A 1 85  ? 37.812  -46.136 3.543   1.00 59.35 ?  97  PRO A O   1 
ATOM   564  C CB  . PRO A 1 85  ? 34.780  -47.156 3.717   1.00 45.34 ?  97  PRO A CB  1 
ATOM   565  C CG  . PRO A 1 85  ? 34.526  -48.611 3.852   1.00 45.54 ?  97  PRO A CG  1 
ATOM   566  C CD  . PRO A 1 85  ? 35.780  -49.316 3.411   1.00 47.28 ?  97  PRO A CD  1 
ATOM   567  N N   . ALA A 1 86  ? 36.517  -44.734 2.355   1.00 55.36 ?  98  ALA A N   1 
ATOM   568  C CA  . ALA A 1 86  ? 37.329  -43.571 2.669   1.00 52.79 ?  98  ALA A CA  1 
ATOM   569  C C   . ALA A 1 86  ? 36.964  -43.036 4.045   1.00 48.88 ?  98  ALA A C   1 
ATOM   570  O O   . ALA A 1 86  ? 35.829  -43.185 4.509   1.00 48.59 ?  98  ALA A O   1 
ATOM   571  C CB  . ALA A 1 86  ? 37.133  -42.478 1.617   1.00 49.93 ?  98  ALA A CB  1 
ATOM   572  N N   . SER A 1 87  ? 37.942  -42.408 4.699   1.00 57.87 ?  99  SER A N   1 
ATOM   573  C CA  . SER A 1 87  ? 37.736  -41.788 6.006   1.00 55.35 ?  99  SER A CA  1 
ATOM   574  C C   . SER A 1 87  ? 38.137  -40.317 5.982   1.00 55.20 ?  99  SER A C   1 
ATOM   575  O O   . SER A 1 87  ? 39.270  -39.993 5.591   1.00 51.16 ?  99  SER A O   1 
ATOM   576  C CB  . SER A 1 87  ? 38.525  -42.511 7.093   1.00 49.22 ?  99  SER A CB  1 
ATOM   577  O OG  . SER A 1 87  ? 37.817  -42.416 8.312   1.00 64.77 ?  99  SER A OG  1 
ATOM   578  N N   . PRO A 1 88  ? 37.248  -39.394 6.378   1.00 52.51 ?  100 PRO A N   1 
ATOM   579  C CA  . PRO A 1 88  ? 35.861  -39.630 6.803   1.00 54.48 ?  100 PRO A CA  1 
ATOM   580  C C   . PRO A 1 88  ? 34.968  -40.125 5.651   1.00 51.66 ?  100 PRO A C   1 
ATOM   581  O O   . PRO A 1 88  ? 35.297  -39.911 4.477   1.00 45.73 ?  100 PRO A O   1 
ATOM   582  C CB  . PRO A 1 88  ? 35.411  -38.252 7.298   1.00 49.62 ?  100 PRO A CB  1 
ATOM   583  C CG  . PRO A 1 88  ? 36.230  -37.297 6.514   1.00 51.95 ?  100 PRO A CG  1 
ATOM   584  C CD  . PRO A 1 88  ? 37.569  -37.959 6.319   1.00 50.76 ?  100 PRO A CD  1 
ATOM   585  N N   . PRO A 1 89  ? 33.875  -40.805 5.979   1.00 51.39 ?  101 PRO A N   1 
ATOM   586  C CA  . PRO A 1 89  ? 33.077  -41.449 4.937   1.00 52.26 ?  101 PRO A CA  1 
ATOM   587  C C   . PRO A 1 89  ? 32.167  -40.456 4.236   1.00 52.28 ?  101 PRO A C   1 
ATOM   588  O O   . PRO A 1 89  ? 31.719  -39.467 4.821   1.00 49.93 ?  101 PRO A O   1 
ATOM   589  C CB  . PRO A 1 89  ? 32.267  -42.489 5.715   1.00 46.44 ?  101 PRO A CB  1 
ATOM   590  C CG  . PRO A 1 89  ? 32.044  -41.816 7.048   1.00 45.03 ?  101 PRO A CG  1 
ATOM   591  C CD  . PRO A 1 89  ? 33.321  -41.052 7.323   1.00 45.15 ?  101 PRO A CD  1 
ATOM   592  N N   . LYS A 1 90  ? 31.889  -40.758 2.963   1.00 51.15 ?  102 LYS A N   1 
ATOM   593  C CA  . LYS A 1 90  ? 31.034  -39.961 2.097   1.00 46.54 ?  102 LYS A CA  1 
ATOM   594  C C   . LYS A 1 90  ? 30.038  -40.862 1.367   1.00 48.61 ?  102 LYS A C   1 
ATOM   595  O O   . LYS A 1 90  ? 30.333  -42.023 1.063   1.00 46.69 ?  102 LYS A O   1 
ATOM   596  C CB  . LYS A 1 90  ? 31.878  -39.186 1.067   1.00 47.88 ?  102 LYS A CB  1 
ATOM   597  C CG  . LYS A 1 90  ? 32.961  -38.283 1.665   1.00 42.44 ?  102 LYS A CG  1 
ATOM   598  C CD  . LYS A 1 90  ? 32.349  -37.204 2.532   1.00 39.60 ?  102 LYS A CD  1 
ATOM   599  C CE  . LYS A 1 90  ? 33.399  -36.236 3.013   1.00 35.73 ?  102 LYS A CE  1 
ATOM   600  N NZ  . LYS A 1 90  ? 32.795  -35.162 3.850   1.00 37.07 ?  102 LYS A NZ  1 
ATOM   601  N N   . ILE A 1 91  ? 28.859  -40.314 1.071   1.00 45.94 ?  103 ILE A N   1 
ATOM   602  C CA  . ILE A 1 91  ? 27.860  -40.964 0.228   1.00 39.44 ?  103 ILE A CA  1 
ATOM   603  C C   . ILE A 1 91  ? 27.791  -40.235 -1.111  1.00 43.43 ?  103 ILE A C   1 
ATOM   604  O O   . ILE A 1 91  ? 27.622  -39.010 -1.155  1.00 40.27 ?  103 ILE A O   1 
ATOM   605  C CB  . ILE A 1 91  ? 26.472  -40.987 0.882   1.00 39.90 ?  103 ILE A CB  1 
ATOM   606  C CG1 . ILE A 1 91  ? 26.428  -42.006 2.018   1.00 38.62 ?  103 ILE A CG1 1 
ATOM   607  C CG2 . ILE A 1 91  ? 25.396  -41.308 -0.196  1.00 34.86 ?  103 ILE A CG2 1 
ATOM   608  C CD1 . ILE A 1 91  ? 25.156  -41.935 2.851   1.00 31.40 ?  103 ILE A CD1 1 
ATOM   609  N N   . PHE A 1 92  ? 27.890  -40.998 -2.194  1.00 41.29 ?  104 PHE A N   1 
ATOM   610  C CA  . PHE A 1 92  ? 27.784  -40.521 -3.569  1.00 31.65 ?  104 PHE A CA  1 
ATOM   611  C C   . PHE A 1 92  ? 26.457  -41.066 -4.108  1.00 40.63 ?  104 PHE A C   1 
ATOM   612  O O   . PHE A 1 92  ? 26.289  -42.285 -4.229  1.00 36.64 ?  104 PHE A O   1 
ATOM   613  C CB  . PHE A 1 92  ? 28.998  -41.007 -4.359  1.00 34.29 ?  104 PHE A CB  1 
ATOM   614  C CG  . PHE A 1 92  ? 29.010  -40.643 -5.834  1.00 44.83 ?  104 PHE A CG  1 
ATOM   615  C CD1 . PHE A 1 92  ? 28.279  -41.379 -6.763  1.00 41.56 ?  104 PHE A CD1 1 
ATOM   616  C CD2 . PHE A 1 92  ? 29.833  -39.623 -6.303  1.00 43.17 ?  104 PHE A CD2 1 
ATOM   617  C CE1 . PHE A 1 92  ? 28.328  -41.060 -8.126  1.00 41.02 ?  104 PHE A CE1 1 
ATOM   618  C CE2 . PHE A 1 92  ? 29.887  -39.298 -7.656  1.00 45.71 ?  104 PHE A CE2 1 
ATOM   619  C CZ  . PHE A 1 92  ? 29.139  -40.020 -8.571  1.00 41.64 ?  104 PHE A CZ  1 
ATOM   620  N N   . SER A 1 93  ? 25.497  -40.163 -4.367  1.00 38.16 ?  105 SER A N   1 
ATOM   621  C CA  . SER A 1 93  ? 24.166  -40.502 -4.872  1.00 36.19 ?  105 SER A CA  1 
ATOM   622  C C   . SER A 1 93  ? 24.122  -40.251 -6.384  1.00 39.43 ?  105 SER A C   1 
ATOM   623  O O   . SER A 1 93  ? 24.116  -39.095 -6.830  1.00 34.83 ?  105 SER A O   1 
ATOM   624  C CB  . SER A 1 93  ? 23.105  -39.683 -4.145  1.00 31.50 ?  105 SER A CB  1 
ATOM   625  O OG  . SER A 1 93  ? 21.790  -40.129 -4.431  1.00 33.50 ?  105 SER A OG  1 
ATOM   626  N N   . TYR A 1 94  ? 24.111  -41.333 -7.173  1.00 39.86 ?  106 TYR A N   1 
ATOM   627  C CA  . TYR A 1 94  ? 24.094  -41.256 -8.637  1.00 35.29 ?  106 TYR A CA  1 
ATOM   628  C C   . TYR A 1 94  ? 22.660  -41.378 -9.150  1.00 34.03 ?  106 TYR A C   1 
ATOM   629  O O   . TYR A 1 94  ? 21.983  -42.371 -8.867  1.00 39.49 ?  106 TYR A O   1 
ATOM   630  C CB  . TYR A 1 94  ? 24.976  -42.345 -9.246  1.00 29.95 ?  106 TYR A CB  1 
ATOM   631  C CG  . TYR A 1 94  ? 24.966  -42.321 -10.745 1.00 33.44 ?  106 TYR A CG  1 
ATOM   632  C CD1 . TYR A 1 94  ? 25.773  -41.428 -11.440 1.00 37.65 ?  106 TYR A CD1 1 
ATOM   633  C CD2 . TYR A 1 94  ? 24.134  -43.176 -11.480 1.00 34.87 ?  106 TYR A CD2 1 
ATOM   634  C CE1 . TYR A 1 94  ? 25.765  -41.373 -12.832 1.00 35.13 ?  106 TYR A CE1 1 
ATOM   635  C CE2 . TYR A 1 94  ? 24.116  -43.128 -12.872 1.00 32.98 ?  106 TYR A CE2 1 
ATOM   636  C CZ  . TYR A 1 94  ? 24.932  -42.225 -13.533 1.00 32.18 ?  106 TYR A CZ  1 
ATOM   637  O OH  . TYR A 1 94  ? 24.938  -42.164 -14.886 1.00 31.50 ?  106 TYR A OH  1 
ATOM   638  N N   . GLN A 1 95  ? 22.200  -40.383 -9.910  1.00 34.07 ?  107 GLN A N   1 
ATOM   639  C CA  . GLN A 1 95  ? 20.840  -40.377 -10.450 1.00 33.29 ?  107 GLN A CA  1 
ATOM   640  C C   . GLN A 1 95  ? 20.844  -40.789 -11.923 1.00 35.51 ?  107 GLN A C   1 
ATOM   641  O O   . GLN A 1 95  ? 21.517  -40.156 -12.756 1.00 30.63 ?  107 GLN A O   1 
ATOM   642  C CB  . GLN A 1 95  ? 20.175  -39.010 -10.288 1.00 32.62 ?  107 GLN A CB  1 
ATOM   643  C CG  . GLN A 1 95  ? 19.698  -38.723 -8.887  1.00 29.90 ?  107 GLN A CG  1 
ATOM   644  C CD  . GLN A 1 95  ? 20.844  -38.800 -7.870  1.00 36.53 ?  107 GLN A CD  1 
ATOM   645  O OE1 . GLN A 1 95  ? 20.817  -39.621 -6.954  1.00 34.72 ?  107 GLN A OE1 1 
ATOM   646  N NE2 . GLN A 1 95  ? 21.865  -37.947 -8.046  1.00 33.35 ?  107 GLN A NE2 1 
ATOM   647  N N   . VAL A 1 96  ? 20.034  -41.835 -12.246 1.00 31.53 ?  108 VAL A N   1 
ATOM   648  C CA  . VAL A 1 96  ? 19.990  -42.475 -13.558 1.00 32.09 ?  108 VAL A CA  1 
ATOM   649  C C   . VAL A 1 96  ? 19.010  -41.730 -14.457 1.00 27.42 ?  108 VAL A C   1 
ATOM   650  O O   . VAL A 1 96  ? 17.965  -41.273 -13.995 1.00 29.54 ?  108 VAL A O   1 
ATOM   651  C CB  . VAL A 1 96  ? 19.587  -43.956 -13.389 1.00 39.36 ?  108 VAL A CB  1 
ATOM   652  C CG1 . VAL A 1 96  ? 19.317  -44.654 -14.734 1.00 28.58 ?  108 VAL A CG1 1 
ATOM   653  C CG2 . VAL A 1 96  ? 20.642  -44.690 -12.585 1.00 34.31 ?  108 VAL A CG2 1 
ATOM   654  N N   . TYR A 1 97  ? 19.317  -41.607 -15.750 1.00 27.19 ?  109 TYR A N   1 
ATOM   655  C CA  . TYR A 1 97  ? 18.318  -41.067 -16.683 1.00 29.14 ?  109 TYR A CA  1 
ATOM   656  C C   . TYR A 1 97  ? 17.404  -42.213 -17.162 1.00 28.36 ?  109 TYR A C   1 
ATOM   657  O O   . TYR A 1 97  ? 17.454  -42.670 -18.300 1.00 26.24 ?  109 TYR A O   1 
ATOM   658  C CB  . TYR A 1 97  ? 19.000  -40.327 -17.837 1.00 27.21 ?  109 TYR A CB  1 
ATOM   659  C CG  . TYR A 1 97  ? 20.240  -41.024 -18.376 1.00 29.40 ?  109 TYR A CG  1 
ATOM   660  C CD1 . TYR A 1 97  ? 20.138  -42.023 -19.346 1.00 27.99 ?  109 TYR A CD1 1 
ATOM   661  C CD2 . TYR A 1 97  ? 21.507  -40.699 -17.910 1.00 30.39 ?  109 TYR A CD2 1 
ATOM   662  C CE1 . TYR A 1 97  ? 21.255  -42.679 -19.828 1.00 28.09 ?  109 TYR A CE1 1 
ATOM   663  C CE2 . TYR A 1 97  ? 22.632  -41.352 -18.388 1.00 31.22 ?  109 TYR A CE2 1 
ATOM   664  C CZ  . TYR A 1 97  ? 22.501  -42.342 -19.346 1.00 34.23 ?  109 TYR A CZ  1 
ATOM   665  O OH  . TYR A 1 97  ? 23.618  -42.992 -19.822 1.00 31.24 ?  109 TYR A OH  1 
ATOM   666  N N   . GLU A 1 98  ? 16.552  -42.686 -16.242 1.00 28.62 ?  110 GLU A N   1 
ATOM   667  C CA  . GLU A 1 98  ? 15.653  -43.798 -16.552 1.00 35.97 ?  110 GLU A CA  1 
ATOM   668  C C   . GLU A 1 98  ? 14.769  -43.479 -17.755 1.00 34.90 ?  110 GLU A C   1 
ATOM   669  O O   . GLU A 1 98  ? 14.674  -44.275 -18.700 1.00 33.73 ?  110 GLU A O   1 
ATOM   670  C CB  . GLU A 1 98  ? 14.786  -44.147 -15.342 1.00 32.67 ?  110 GLU A CB  1 
ATOM   671  C CG  . GLU A 1 98  ? 13.673  -45.107 -15.694 1.00 34.21 ?  110 GLU A CG  1 
ATOM   672  C CD  . GLU A 1 98  ? 12.805  -45.495 -14.495 1.00 40.59 ?  110 GLU A CD  1 
ATOM   673  O OE1 . GLU A 1 98  ? 13.014  -44.943 -13.393 1.00 38.80 ?  110 GLU A OE1 1 
ATOM   674  O OE2 . GLU A 1 98  ? 11.922  -46.366 -14.652 1.00 38.34 ?  110 GLU A OE2 1 
ATOM   675  N N   . ASP A 1 99  ? 14.106  -42.318 -17.730 1.00 32.50 ?  111 ASP A N   1 
ATOM   676  C CA  . ASP A 1 99  ? 13.400  -41.781 -18.895 1.00 32.09 ?  111 ASP A CA  1 
ATOM   677  C C   . ASP A 1 99  ? 12.303  -42.732 -19.392 1.00 35.40 ?  111 ASP A C   1 
ATOM   678  O O   . ASP A 1 99  ? 12.066  -42.854 -20.596 1.00 35.18 ?  111 ASP A O   1 
ATOM   679  C CB  . ASP A 1 99  ? 14.383  -41.459 -20.030 1.00 31.61 ?  111 ASP A CB  1 
ATOM   680  C CG  . ASP A 1 99  ? 15.354  -40.295 -19.697 1.00 35.38 ?  111 ASP A CG  1 
ATOM   681  O OD1 . ASP A 1 99  ? 15.390  -39.780 -18.543 1.00 28.62 ?  111 ASP A OD1 1 
ATOM   682  O OD2 . ASP A 1 99  ? 16.103  -39.905 -20.629 1.00 31.88 ?  111 ASP A OD2 1 
ATOM   683  N N   . SER A 1 100 ? 11.618  -43.405 -18.467 1.00 32.82 ?  112 SER A N   1 
ATOM   684  C CA  . SER A 1 100 ? 10.582  -44.370 -18.813 1.00 35.07 ?  112 SER A CA  1 
ATOM   685  C C   . SER A 1 100 ? 9.427   -44.243 -17.834 1.00 35.26 ?  112 SER A C   1 
ATOM   686  O O   . SER A 1 100 ? 9.598   -43.758 -16.722 1.00 37.96 ?  112 SER A O   1 
ATOM   687  C CB  . SER A 1 100 ? 11.096  -45.811 -18.780 1.00 35.67 ?  112 SER A CB  1 
ATOM   688  O OG  . SER A 1 100 ? 12.295  -45.977 -19.507 1.00 32.61 ?  112 SER A OG  1 
ATOM   689  N N   . THR A 1 101 ? 8.234   -44.671 -18.256 1.00 35.33 ?  113 THR A N   1 
ATOM   690  C CA  . THR A 1 101 ? 7.124   -44.718 -17.307 1.00 37.60 ?  113 THR A CA  1 
ATOM   691  C C   . THR A 1 101 ? 6.621   -46.148 -17.206 1.00 34.99 ?  113 THR A C   1 
ATOM   692  O O   . THR A 1 101 ? 5.419   -46.410 -17.325 1.00 36.96 ?  113 THR A O   1 
ATOM   693  C CB  . THR A 1 101 ? 6.000   -43.745 -17.680 1.00 34.68 ?  113 THR A CB  1 
ATOM   694  O OG1 . THR A 1 101 ? 5.394   -44.123 -18.925 1.00 32.98 ?  113 THR A OG1 1 
ATOM   695  C CG2 . THR A 1 101 ? 6.560   -42.344 -17.814 1.00 36.11 ?  113 THR A CG2 1 
ATOM   696  N N   . GLN A 1 102 ? 7.549   -47.073 -16.968 1.00 34.60 ?  114 GLN A N   1 
ATOM   697  C CA  . GLN A 1 102 ? 7.249   -48.486 -16.791 1.00 35.15 ?  114 GLN A CA  1 
ATOM   698  C C   . GLN A 1 102 ? 8.179   -49.055 -15.730 1.00 35.47 ?  114 GLN A C   1 
ATOM   699  O O   . GLN A 1 102 ? 9.395   -48.842 -15.796 1.00 39.77 ?  114 GLN A O   1 
ATOM   700  C CB  . GLN A 1 102 ? 7.414   -49.245 -18.117 1.00 30.94 ?  114 GLN A CB  1 
ATOM   701  C CG  . GLN A 1 102 ? 7.716   -50.732 -17.986 1.00 32.94 ?  114 GLN A CG  1 
ATOM   702  C CD  . GLN A 1 102 ? 6.665   -51.492 -17.183 1.00 36.19 ?  114 GLN A CD  1 
ATOM   703  O OE1 . GLN A 1 102 ? 6.998   -52.350 -16.368 1.00 34.63 ?  114 GLN A OE1 1 
ATOM   704  N NE2 . GLN A 1 102 ? 5.394   -51.168 -17.405 1.00 36.20 ?  114 GLN A NE2 1 
ATOM   705  N N   . LEU A 1 103 ? 7.611   -49.824 -14.795 1.00 33.48 ?  115 LEU A N   1 
ATOM   706  C CA  . LEU A 1 103 ? 8.351   -50.252 -13.610 1.00 34.44 ?  115 LEU A CA  1 
ATOM   707  C C   . LEU A 1 103 ? 9.555   -51.136 -13.938 1.00 34.07 ?  115 LEU A C   1 
ATOM   708  O O   . LEU A 1 103 ? 10.573  -51.070 -13.240 1.00 33.32 ?  115 LEU A O   1 
ATOM   709  C CB  . LEU A 1 103 ? 7.406   -50.968 -12.635 1.00 36.85 ?  115 LEU A CB  1 
ATOM   710  C CG  . LEU A 1 103 ? 8.001   -51.190 -11.241 1.00 36.63 ?  115 LEU A CG  1 
ATOM   711  C CD1 . LEU A 1 103 ? 7.989   -49.882 -10.421 1.00 34.09 ?  115 LEU A CD1 1 
ATOM   712  C CD2 . LEU A 1 103 ? 7.279   -52.321 -10.516 1.00 39.00 ?  115 LEU A CD2 1 
ATOM   713  N N   . ASN A 1 104 ? 9.494   -51.964 -14.979 1.00 37.64 ?  116 ASN A N   1 
ATOM   714  C CA  . ASN A 1 104 ? 10.677  -52.788 -15.206 1.00 36.14 ?  116 ASN A CA  1 
ATOM   715  C C   . ASN A 1 104 ? 11.788  -52.028 -15.935 1.00 35.96 ?  116 ASN A C   1 
ATOM   716  O O   . ASN A 1 104 ? 12.804  -52.628 -16.314 1.00 36.55 ?  116 ASN A O   1 
ATOM   717  C CB  . ASN A 1 104 ? 10.316  -54.112 -15.912 1.00 37.77 ?  116 ASN A CB  1 
ATOM   718  C CG  . ASN A 1 104 ? 9.696   -53.936 -17.307 1.00 44.22 ?  116 ASN A CG  1 
ATOM   719  O OD1 . ASN A 1 104 ? 9.910   -52.941 -17.998 1.00 40.50 ?  116 ASN A OD1 1 
ATOM   720  N ND2 . ASN A 1 104 ? 8.945   -54.951 -17.736 1.00 44.88 ?  116 ASN A ND2 1 
ATOM   721  N N   . CYS A 1 105 ? 11.640  -50.713 -16.100 1.00 37.98 ?  117 CYS A N   1 
ATOM   722  C CA  . CYS A 1 105 ? 12.741  -49.858 -16.541 1.00 39.73 ?  117 CYS A CA  1 
ATOM   723  C C   . CYS A 1 105 ? 13.558  -49.274 -15.378 1.00 42.17 ?  117 CYS A C   1 
ATOM   724  O O   . CYS A 1 105 ? 14.551  -48.574 -15.624 1.00 41.73 ?  117 CYS A O   1 
ATOM   725  C CB  . CYS A 1 105 ? 12.201  -48.715 -17.404 1.00 39.77 ?  117 CYS A CB  1 
ATOM   726  S SG  . CYS A 1 105 ? 10.996  -49.198 -18.684 1.00 33.83 ?  117 CYS A SG  1 
ATOM   727  N N   . ALA A 1 106 ? 13.177  -49.564 -14.130 1.00 39.19 ?  118 ALA A N   1 
ATOM   728  C CA  . ALA A 1 106 ? 13.751  -48.900 -12.963 1.00 38.58 ?  118 ALA A CA  1 
ATOM   729  C C   . ALA A 1 106 ? 15.263  -49.125 -12.863 1.00 35.56 ?  118 ALA A C   1 
ATOM   730  O O   . ALA A 1 106 ? 15.792  -50.137 -13.335 1.00 36.34 ?  118 ALA A O   1 
ATOM   731  C CB  . ALA A 1 106 ? 13.067  -49.389 -11.680 1.00 35.35 ?  118 ALA A CB  1 
ATOM   732  N N   . PRO A 1 107 ? 15.983  -48.182 -12.250 1.00 36.82 ?  119 PRO A N   1 
ATOM   733  C CA  . PRO A 1 107 ? 17.437  -48.364 -12.079 1.00 33.04 ?  119 PRO A CA  1 
ATOM   734  C C   . PRO A 1 107 ? 17.824  -49.656 -11.356 1.00 35.19 ?  119 PRO A C   1 
ATOM   735  O O   . PRO A 1 107 ? 18.754  -50.354 -11.798 1.00 31.03 ?  119 PRO A O   1 
ATOM   736  C CB  . PRO A 1 107 ? 17.847  -47.113 -11.282 1.00 36.02 ?  119 PRO A CB  1 
ATOM   737  C CG  . PRO A 1 107 ? 16.807  -46.067 -11.616 1.00 32.88 ?  119 PRO A CG  1 
ATOM   738  C CD  . PRO A 1 107 ? 15.533  -46.806 -11.937 1.00 40.01 ?  119 PRO A CD  1 
ATOM   739  N N   . SER A 1 108 ? 17.141  -49.989 -10.253 1.00 32.47 ?  120 SER A N   1 
ATOM   740  C CA  . SER A 1 108 ? 17.485  -51.191 -9.491  1.00 37.79 ?  120 SER A CA  1 
ATOM   741  C C   . SER A 1 108 ? 17.528  -52.413 -10.392 1.00 36.87 ?  120 SER A C   1 
ATOM   742  O O   . SER A 1 108 ? 18.560  -53.086 -10.506 1.00 40.57 ?  120 SER A O   1 
ATOM   743  C CB  . SER A 1 108 ? 16.495  -51.411 -8.342  1.00 34.50 ?  120 SER A CB  1 
ATOM   744  O OG  . SER A 1 108 ? 15.158  -51.269 -8.763  1.00 30.88 ?  120 SER A OG  1 
ATOM   745  N N   . TYR A 1 109 ? 16.414  -52.690 -11.069 1.00 40.03 ?  121 TYR A N   1 
ATOM   746  C CA  . TYR A 1 109 ? 16.368  -53.815 -12.000 1.00 39.63 ?  121 TYR A CA  1 
ATOM   747  C C   . TYR A 1 109 ? 17.480  -53.712 -13.049 1.00 38.72 ?  121 TYR A C   1 
ATOM   748  O O   . TYR A 1 109 ? 18.166  -54.703 -13.335 1.00 35.70 ?  121 TYR A O   1 
ATOM   749  C CB  . TYR A 1 109 ? 14.979  -53.879 -12.649 1.00 40.26 ?  121 TYR A CB  1 
ATOM   750  C CG  . TYR A 1 109 ? 14.645  -55.192 -13.324 1.00 46.01 ?  121 TYR A CG  1 
ATOM   751  C CD1 . TYR A 1 109 ? 14.959  -56.413 -12.723 1.00 46.00 ?  121 TYR A CD1 1 
ATOM   752  C CD2 . TYR A 1 109 ? 14.062  -55.208 -14.595 1.00 44.14 ?  121 TYR A CD2 1 
ATOM   753  C CE1 . TYR A 1 109 ? 14.671  -57.617 -13.353 1.00 48.40 ?  121 TYR A CE1 1 
ATOM   754  C CE2 . TYR A 1 109 ? 13.774  -56.402 -15.239 1.00 46.19 ?  121 TYR A CE2 1 
ATOM   755  C CZ  . TYR A 1 109 ? 14.079  -57.600 -14.616 1.00 50.62 ?  121 TYR A CZ  1 
ATOM   756  O OH  . TYR A 1 109 ? 13.792  -58.775 -15.253 1.00 52.95 ?  121 TYR A OH  1 
ATOM   757  N N   . SER A 1 110 ? 17.712  -52.508 -13.597 1.00 36.47 ?  122 SER A N   1 
ATOM   758  C CA  . SER A 1 110 ? 18.710  -52.385 -14.660 1.00 35.79 ?  122 SER A CA  1 
ATOM   759  C C   . SER A 1 110 ? 20.140  -52.536 -14.155 1.00 34.45 ?  122 SER A C   1 
ATOM   760  O O   . SER A 1 110 ? 21.038  -52.780 -14.970 1.00 32.80 ?  122 SER A O   1 
ATOM   761  C CB  . SER A 1 110 ? 18.571  -51.052 -15.418 1.00 33.48 ?  122 SER A CB  1 
ATOM   762  O OG  . SER A 1 110 ? 17.233  -50.576 -15.448 1.00 34.16 ?  122 SER A OG  1 
ATOM   763  N N   . TYR A 1 111 ? 20.381  -52.401 -12.844 1.00 32.63 ?  123 TYR A N   1 
ATOM   764  C CA  . TYR A 1 111 ? 21.725  -52.647 -12.316 1.00 36.17 ?  123 TYR A CA  1 
ATOM   765  C C   . TYR A 1 111 ? 22.061  -54.133 -12.211 1.00 43.17 ?  123 TYR A C   1 
ATOM   766  O O   . TYR A 1 111 ? 23.251  -54.484 -12.221 1.00 48.42 ?  123 TYR A O   1 
ATOM   767  C CB  . TYR A 1 111 ? 21.906  -52.018 -10.925 1.00 37.66 ?  123 TYR A CB  1 
ATOM   768  C CG  . TYR A 1 111 ? 22.106  -50.510 -10.914 1.00 36.59 ?  123 TYR A CG  1 
ATOM   769  C CD1 . TYR A 1 111 ? 23.219  -49.916 -11.524 1.00 32.72 ?  123 TYR A CD1 1 
ATOM   770  C CD2 . TYR A 1 111 ? 21.177  -49.687 -10.297 1.00 33.18 ?  123 TYR A CD2 1 
ATOM   771  C CE1 . TYR A 1 111 ? 23.389  -48.544 -11.517 1.00 32.44 ?  123 TYR A CE1 1 
ATOM   772  C CE2 . TYR A 1 111 ? 21.329  -48.316 -10.294 1.00 34.50 ?  123 TYR A CE2 1 
ATOM   773  C CZ  . TYR A 1 111 ? 22.439  -47.745 -10.894 1.00 35.80 ?  123 TYR A CZ  1 
ATOM   774  O OH  . TYR A 1 111 ? 22.581  -46.368 -10.859 1.00 33.42 ?  123 TYR A OH  1 
ATOM   775  N N   . LEU A 1 112 ? 21.057  -55.008 -12.112 1.00 42.72 ?  124 LEU A N   1 
ATOM   776  C CA  . LEU A 1 112 ? 21.302  -56.446 -11.983 1.00 44.91 ?  124 LEU A CA  1 
ATOM   777  C C   . LEU A 1 112 ? 22.140  -56.982 -13.142 1.00 42.41 ?  124 LEU A C   1 
ATOM   778  O O   . LEU A 1 112 ? 22.191  -56.413 -14.237 1.00 43.31 ?  124 LEU A O   1 
ATOM   779  C CB  . LEU A 1 112 ? 19.986  -57.225 -11.916 1.00 38.20 ?  124 LEU A CB  1 
ATOM   780  C CG  . LEU A 1 112 ? 18.998  -56.746 -10.849 1.00 45.53 ?  124 LEU A CG  1 
ATOM   781  C CD1 . LEU A 1 112 ? 17.659  -57.500 -10.924 1.00 44.47 ?  124 LEU A CD1 1 
ATOM   782  C CD2 . LEU A 1 112 ? 19.629  -56.835 -9.443  1.00 39.01 ?  124 LEU A CD2 1 
ATOM   783  N N   . THR A 1 113 ? 22.814  -58.096 -12.880 1.00 51.98 ?  125 THR A N   1 
ATOM   784  C CA  . THR A 1 113 ? 23.498  -58.827 -13.936 1.00 49.33 ?  125 THR A CA  1 
ATOM   785  C C   . THR A 1 113 ? 22.488  -59.349 -14.957 1.00 43.89 ?  125 THR A C   1 
ATOM   786  O O   . THR A 1 113 ? 21.276  -59.392 -14.720 1.00 35.88 ?  125 THR A O   1 
ATOM   787  C CB  . THR A 1 113 ? 24.279  -59.994 -13.350 1.00 50.30 ?  125 THR A CB  1 
ATOM   788  O OG1 . THR A 1 113 ? 23.418  -60.716 -12.455 1.00 47.83 ?  125 THR A OG1 1 
ATOM   789  C CG2 . THR A 1 113 ? 25.495  -59.479 -12.585 1.00 51.06 ?  125 THR A CG2 1 
ATOM   790  N N   . GLY A 1 114 ? 23.002  -59.743 -16.110 1.00 44.85 ?  126 GLY A N   1 
ATOM   791  C CA  . GLY A 1 114 ? 22.173  -60.308 -17.152 1.00 52.08 ?  126 GLY A CA  1 
ATOM   792  C C   . GLY A 1 114 ? 22.188  -59.457 -18.401 1.00 53.00 ?  126 GLY A C   1 
ATOM   793  O O   . GLY A 1 114 ? 22.935  -58.483 -18.519 1.00 61.04 ?  126 GLY A O   1 
ATOM   794  N N   . PHE A 1 115 ? 21.345  -59.839 -19.356 1.00 51.25 ?  127 PHE A N   1 
ATOM   795  C CA  . PHE A 1 115 ? 21.335  -59.193 -20.664 1.00 53.76 ?  127 PHE A CA  1 
ATOM   796  C C   . PHE A 1 115 ? 19.973  -58.670 -21.091 1.00 48.53 ?  127 PHE A C   1 
ATOM   797  O O   . PHE A 1 115 ? 19.923  -57.788 -21.953 1.00 53.26 ?  127 PHE A O   1 
ATOM   798  C CB  . PHE A 1 115 ? 21.858  -60.153 -21.748 1.00 50.27 ?  127 PHE A CB  1 
ATOM   799  C CG  . PHE A 1 115 ? 20.874  -61.238 -22.127 1.00 59.74 ?  127 PHE A CG  1 
ATOM   800  C CD1 . PHE A 1 115 ? 20.959  -62.501 -21.549 1.00 57.57 ?  127 PHE A CD1 1 
ATOM   801  C CD2 . PHE A 1 115 ? 19.869  -61.006 -23.066 1.00 56.74 ?  127 PHE A CD2 1 
ATOM   802  C CE1 . PHE A 1 115 ? 20.057  -63.504 -21.888 1.00 60.88 ?  127 PHE A CE1 1 
ATOM   803  C CE2 . PHE A 1 115 ? 18.963  -62.007 -23.407 1.00 57.01 ?  127 PHE A CE2 1 
ATOM   804  C CZ  . PHE A 1 115 ? 19.055  -63.255 -22.818 1.00 52.80 ?  127 PHE A CZ  1 
ATOM   805  N N   . ASP A 1 116 ? 18.878  -59.163 -20.526 1.00 48.49 ?  128 ASP A N   1 
ATOM   806  C CA  . ASP A 1 116 ? 17.550  -58.855 -21.036 1.00 51.92 ?  128 ASP A CA  1 
ATOM   807  C C   . ASP A 1 116 ? 16.833  -57.742 -20.279 1.00 44.67 ?  128 ASP A C   1 
ATOM   808  O O   . ASP A 1 116 ? 15.708  -57.394 -20.657 1.00 43.69 ?  128 ASP A O   1 
ATOM   809  C CB  . ASP A 1 116 ? 16.679  -60.118 -21.027 1.00 49.36 ?  128 ASP A CB  1 
ATOM   810  C CG  . ASP A 1 116 ? 16.531  -60.704 -19.646 1.00 52.08 ?  128 ASP A CG  1 
ATOM   811  O OD1 . ASP A 1 116 ? 17.454  -60.520 -18.833 1.00 51.92 ?  128 ASP A OD1 1 
ATOM   812  O OD2 . ASP A 1 116 ? 15.501  -61.352 -19.373 1.00 58.23 ?  128 ASP A OD2 1 
ATOM   813  N N   . GLU A 1 117 ? 17.425  -57.190 -19.224 1.00 44.53 ?  129 GLU A N   1 
ATOM   814  C CA  . GLU A 1 117 ? 16.774  -56.087 -18.527 1.00 43.04 ?  129 GLU A CA  1 
ATOM   815  C C   . GLU A 1 117 ? 16.499  -54.975 -19.533 1.00 39.50 ?  129 GLU A C   1 
ATOM   816  O O   . GLU A 1 117 ? 17.411  -54.579 -20.277 1.00 38.21 ?  129 GLU A O   1 
ATOM   817  C CB  . GLU A 1 117 ? 17.632  -55.575 -17.370 1.00 41.24 ?  129 GLU A CB  1 
ATOM   818  C CG  . GLU A 1 117 ? 17.566  -56.449 -16.137 1.00 41.78 ?  129 GLU A CG  1 
ATOM   819  C CD  . GLU A 1 117 ? 18.723  -57.436 -16.039 1.00 41.92 ?  129 GLU A CD  1 
ATOM   820  O OE1 . GLU A 1 117 ? 19.462  -57.637 -17.033 1.00 46.69 ?  129 GLU A OE1 1 
ATOM   821  O OE2 . GLU A 1 117 ? 18.903  -58.003 -14.948 1.00 43.77 ?  129 GLU A OE2 1 
ATOM   822  N N   . PRO A 1 118 ? 15.255  -54.495 -19.635 1.00 37.67 ?  130 PRO A N   1 
ATOM   823  C CA  . PRO A 1 118 ? 14.894  -53.652 -20.786 1.00 43.05 ?  130 PRO A CA  1 
ATOM   824  C C   . PRO A 1 118 ? 15.528  -52.260 -20.779 1.00 44.48 ?  130 PRO A C   1 
ATOM   825  O O   . PRO A 1 118 ? 15.730  -51.698 -21.862 1.00 36.28 ?  130 PRO A O   1 
ATOM   826  C CB  . PRO A 1 118 ? 13.363  -53.582 -20.698 1.00 38.51 ?  130 PRO A CB  1 
ATOM   827  C CG  . PRO A 1 118 ? 13.046  -53.866 -19.262 1.00 37.61 ?  130 PRO A CG  1 
ATOM   828  C CD  . PRO A 1 118 ? 14.089  -54.833 -18.800 1.00 35.82 ?  130 PRO A CD  1 
ATOM   829  N N   . ASN A 1 119 ? 15.854  -51.684 -19.613 1.00 39.22 ?  131 ASN A N   1 
ATOM   830  C CA  . ASN A 1 119 ? 16.496  -50.372 -19.563 1.00 35.99 ?  131 ASN A CA  1 
ATOM   831  C C   . ASN A 1 119 ? 17.991  -50.464 -19.248 1.00 37.67 ?  131 ASN A C   1 
ATOM   832  O O   . ASN A 1 119 ? 18.587  -49.506 -18.750 1.00 38.86 ?  131 ASN A O   1 
ATOM   833  C CB  . ASN A 1 119 ? 15.781  -49.469 -18.557 1.00 34.62 ?  131 ASN A CB  1 
ATOM   834  C CG  . ASN A 1 119 ? 15.636  -48.050 -19.071 1.00 34.86 ?  131 ASN A CG  1 
ATOM   835  O OD1 . ASN A 1 119 ? 15.967  -47.783 -20.222 1.00 34.91 ?  131 ASN A OD1 1 
ATOM   836  N ND2 . ASN A 1 119 ? 15.153  -47.138 -18.230 1.00 29.01 ?  131 ASN A ND2 1 
ATOM   837  N N   . LYS A 1 120 ? 18.615  -51.601 -19.540 1.00 39.27 ?  132 LYS A N   1 
ATOM   838  C CA  . LYS A 1 120 ? 20.025  -51.797 -19.221 1.00 41.62 ?  132 LYS A CA  1 
ATOM   839  C C   . LYS A 1 120 ? 20.928  -50.718 -19.829 1.00 36.91 ?  132 LYS A C   1 
ATOM   840  O O   . LYS A 1 120 ? 22.055  -50.528 -19.369 1.00 34.15 ?  132 LYS A O   1 
ATOM   841  C CB  . LYS A 1 120 ? 20.439  -53.197 -19.698 1.00 38.06 ?  132 LYS A CB  1 
ATOM   842  C CG  . LYS A 1 120 ? 21.752  -53.689 -19.173 1.00 42.02 ?  132 LYS A CG  1 
ATOM   843  C CD  . LYS A 1 120 ? 21.574  -54.605 -17.980 1.00 46.54 ?  132 LYS A CD  1 
ATOM   844  C CE  . LYS A 1 120 ? 22.839  -55.433 -17.777 1.00 41.54 ?  132 LYS A CE  1 
ATOM   845  N NZ  . LYS A 1 120 ? 22.702  -56.245 -16.564 1.00 45.05 ?  132 LYS A NZ  1 
ATOM   846  N N   . VAL A 1 121 ? 20.469  -50.020 -20.865 1.00 40.91 ?  133 VAL A N   1 
ATOM   847  C CA  . VAL A 1 121 ? 21.294  -48.980 -21.476 1.00 40.24 ?  133 VAL A CA  1 
ATOM   848  C C   . VAL A 1 121 ? 21.589  -47.852 -20.482 1.00 39.85 ?  133 VAL A C   1 
ATOM   849  O O   . VAL A 1 121 ? 22.621  -47.179 -20.588 1.00 37.17 ?  133 VAL A O   1 
ATOM   850  C CB  . VAL A 1 121 ? 20.605  -48.459 -22.759 1.00 34.58 ?  133 VAL A CB  1 
ATOM   851  C CG1 . VAL A 1 121 ? 19.478  -47.498 -22.422 1.00 33.80 ?  133 VAL A CG1 1 
ATOM   852  C CG2 . VAL A 1 121 ? 21.599  -47.810 -23.672 1.00 34.49 ?  133 VAL A CG2 1 
ATOM   853  N N   . THR A 1 122 ? 20.707  -47.638 -19.496 1.00 37.96 ?  134 THR A N   1 
ATOM   854  C CA  . THR A 1 122 ? 20.857  -46.565 -18.523 1.00 36.04 ?  134 THR A CA  1 
ATOM   855  C C   . THR A 1 122 ? 21.843  -46.901 -17.393 1.00 39.31 ?  134 THR A C   1 
ATOM   856  O O   . THR A 1 122 ? 21.979  -46.094 -16.462 1.00 38.94 ?  134 THR A O   1 
ATOM   857  C CB  . THR A 1 122 ? 19.495  -46.195 -17.908 1.00 35.95 ?  134 THR A CB  1 
ATOM   858  O OG1 . THR A 1 122 ? 18.922  -47.329 -17.234 1.00 31.99 ?  134 THR A OG1 1 
ATOM   859  C CG2 . THR A 1 122 ? 18.521  -45.665 -18.962 1.00 33.71 ?  134 THR A CG2 1 
ATOM   860  N N   . THR A 1 123 ? 22.529  -48.056 -17.438 1.00 39.63 ?  135 THR A N   1 
ATOM   861  C CA  . THR A 1 123 ? 23.405  -48.462 -16.341 1.00 33.17 ?  135 THR A CA  1 
ATOM   862  C C   . THR A 1 123 ? 24.716  -49.092 -16.799 1.00 32.98 ?  135 THR A C   1 
ATOM   863  O O   . THR A 1 123 ? 25.480  -49.558 -15.951 1.00 38.19 ?  135 THR A O   1 
ATOM   864  C CB  . THR A 1 123 ? 22.715  -49.463 -15.405 1.00 38.25 ?  135 THR A CB  1 
ATOM   865  O OG1 . THR A 1 123 ? 22.372  -50.641 -16.148 1.00 37.44 ?  135 THR A OG1 1 
ATOM   866  C CG2 . THR A 1 123 ? 21.453  -48.862 -14.721 1.00 32.55 ?  135 THR A CG2 1 
ATOM   867  N N   . VAL A 1 124 ? 25.019  -49.126 -18.097 1.00 34.87 ?  136 VAL A N   1 
ATOM   868  C CA  . VAL A 1 124 ? 26.214  -49.803 -18.589 1.00 32.89 ?  136 VAL A CA  1 
ATOM   869  C C   . VAL A 1 124 ? 27.075  -48.921 -19.476 1.00 35.95 ?  136 VAL A C   1 
ATOM   870  O O   . VAL A 1 124 ? 28.107  -49.379 -19.961 1.00 40.09 ?  136 VAL A O   1 
ATOM   871  C CB  . VAL A 1 124 ? 25.855  -51.106 -19.338 1.00 36.24 ?  136 VAL A CB  1 
ATOM   872  C CG1 . VAL A 1 124 ? 25.084  -52.070 -18.426 1.00 31.45 ?  136 VAL A CG1 1 
ATOM   873  C CG2 . VAL A 1 124 ? 25.066  -50.786 -20.614 1.00 32.73 ?  136 VAL A CG2 1 
ATOM   874  N N   . LEU A 1 125 ? 26.690  -47.669 -19.719 1.00 37.96 ?  137 LEU A N   1 
ATOM   875  C CA  . LEU A 1 125 ? 27.506  -46.810 -20.577 1.00 40.43 ?  137 LEU A CA  1 
ATOM   876  C C   . LEU A 1 125 ? 28.447  -45.918 -19.753 1.00 45.64 ?  137 LEU A C   1 
ATOM   877  O O   . LEU A 1 125 ? 29.591  -46.301 -19.471 1.00 40.19 ?  137 LEU A O   1 
ATOM   878  C CB  . LEU A 1 125 ? 26.598  -45.975 -21.490 1.00 39.98 ?  137 LEU A CB  1 
ATOM   879  C CG  . LEU A 1 125 ? 25.720  -46.807 -22.439 1.00 41.44 ?  137 LEU A CG  1 
ATOM   880  C CD1 . LEU A 1 125 ? 24.868  -45.924 -23.361 1.00 35.86 ?  137 LEU A CD1 1 
ATOM   881  C CD2 . LEU A 1 125 ? 26.592  -47.776 -23.236 1.00 30.37 ?  137 LEU A CD2 1 
ATOM   882  N N   . ASP A 1 126 ? 27.991  -44.722 -19.364 1.00 39.01 ?  138 ASP A N   1 
ATOM   883  C CA  . ASP A 1 126 ? 28.816  -43.901 -18.492 1.00 40.04 ?  138 ASP A CA  1 
ATOM   884  C C   . ASP A 1 126 ? 28.539  -44.191 -17.029 1.00 37.40 ?  138 ASP A C   1 
ATOM   885  O O   . ASP A 1 126 ? 29.446  -44.051 -16.208 1.00 35.31 ?  138 ASP A O   1 
ATOM   886  C CB  . ASP A 1 126 ? 28.613  -42.407 -18.794 1.00 37.37 ?  138 ASP A CB  1 
ATOM   887  C CG  . ASP A 1 126 ? 27.151  -42.009 -18.821 1.00 37.57 ?  138 ASP A CG  1 
ATOM   888  O OD1 . ASP A 1 126 ? 26.283  -42.903 -18.792 1.00 33.96 ?  138 ASP A OD1 1 
ATOM   889  O OD2 . ASP A 1 126 ? 26.875  -40.800 -18.856 1.00 32.82 ?  138 ASP A OD2 1 
ATOM   890  N N   . THR A 1 127 ? 27.321  -44.635 -16.705 1.00 34.51 ?  139 THR A N   1 
ATOM   891  C CA  . THR A 1 127 ? 26.960  -45.032 -15.344 1.00 35.29 ?  139 THR A CA  1 
ATOM   892  C C   . THR A 1 127 ? 27.974  -45.929 -14.642 1.00 38.99 ?  139 THR A C   1 
ATOM   893  O O   . THR A 1 127 ? 28.279  -45.666 -13.469 1.00 41.78 ?  139 THR A O   1 
ATOM   894  C CB  . THR A 1 127 ? 25.596  -45.730 -15.357 1.00 30.68 ?  139 THR A CB  1 
ATOM   895  O OG1 . THR A 1 127 ? 24.607  -44.826 -15.842 1.00 32.90 ?  139 THR A OG1 1 
ATOM   896  C CG2 . THR A 1 127 ? 25.219  -46.168 -13.958 1.00 30.96 ?  139 THR A CG2 1 
ATOM   897  N N   . PRO A 1 128 ? 28.493  -47.006 -15.245 1.00 38.50 ?  140 PRO A N   1 
ATOM   898  C CA  . PRO A 1 128 ? 29.459  -47.823 -14.490 1.00 36.15 ?  140 PRO A CA  1 
ATOM   899  C C   . PRO A 1 128 ? 30.788  -47.118 -14.276 1.00 35.58 ?  140 PRO A C   1 
ATOM   900  O O   . PRO A 1 128 ? 31.393  -47.284 -13.212 1.00 36.68 ?  140 PRO A O   1 
ATOM   901  C CB  . PRO A 1 128 ? 29.613  -49.080 -15.359 1.00 34.75 ?  140 PRO A CB  1 
ATOM   902  C CG  . PRO A 1 128 ? 29.358  -48.576 -16.787 1.00 34.77 ?  140 PRO A CG  1 
ATOM   903  C CD  . PRO A 1 128 ? 28.272  -47.531 -16.615 1.00 37.14 ?  140 PRO A CD  1 
ATOM   904  N N   . ILE A 1 129 ? 31.266  -46.335 -15.254 1.00 35.33 ?  141 ILE A N   1 
ATOM   905  C CA  . ILE A 1 129 ? 32.506  -45.579 -15.064 1.00 37.03 ?  141 ILE A CA  1 
ATOM   906  C C   . ILE A 1 129 ? 32.348  -44.577 -13.926 1.00 39.13 ?  141 ILE A C   1 
ATOM   907  O O   . ILE A 1 129 ? 33.255  -44.391 -13.104 1.00 42.67 ?  141 ILE A O   1 
ATOM   908  C CB  . ILE A 1 129 ? 32.922  -44.885 -16.371 1.00 39.84 ?  141 ILE A CB  1 
ATOM   909  C CG1 . ILE A 1 129 ? 33.192  -45.921 -17.467 1.00 37.95 ?  141 ILE A CG1 1 
ATOM   910  C CG2 . ILE A 1 129 ? 34.157  -44.009 -16.143 1.00 36.67 ?  141 ILE A CG2 1 
ATOM   911  C CD1 . ILE A 1 129 ? 33.329  -45.315 -18.836 1.00 38.49 ?  141 ILE A CD1 1 
ATOM   912  N N   . ILE A 1 130 ? 31.174  -43.958 -13.830 1.00 36.14 ?  142 ILE A N   1 
ATOM   913  C CA  . ILE A 1 130 ? 30.929  -42.965 -12.794 1.00 37.83 ?  142 ILE A CA  1 
ATOM   914  C C   . ILE A 1 130 ? 30.812  -43.629 -11.425 1.00 41.04 ?  142 ILE A C   1 
ATOM   915  O O   . ILE A 1 130 ? 31.437  -43.188 -10.451 1.00 41.04 ?  142 ILE A O   1 
ATOM   916  C CB  . ILE A 1 130 ? 29.685  -42.131 -13.149 1.00 33.82 ?  142 ILE A CB  1 
ATOM   917  C CG1 . ILE A 1 130 ? 29.988  -41.320 -14.409 1.00 34.06 ?  142 ILE A CG1 1 
ATOM   918  C CG2 . ILE A 1 130 ? 29.254  -41.251 -11.967 1.00 30.83 ?  142 ILE A CG2 1 
ATOM   919  C CD1 . ILE A 1 130 ? 28.797  -40.700 -15.061 1.00 35.82 ?  142 ILE A CD1 1 
ATOM   920  N N   . ILE A 1 131 ? 30.030  -44.705 -11.324 1.00 37.25 ?  143 ILE A N   1 
ATOM   921  C CA  . ILE A 1 131 ? 29.893  -45.333 -10.011 1.00 40.86 ?  143 ILE A CA  1 
ATOM   922  C C   . ILE A 1 131 ? 31.178  -46.055 -9.615  1.00 40.02 ?  143 ILE A C   1 
ATOM   923  O O   . ILE A 1 131 ? 31.489  -46.165 -8.425  1.00 40.29 ?  143 ILE A O   1 
ATOM   924  C CB  . ILE A 1 131 ? 28.677  -46.274 -9.973  1.00 41.03 ?  143 ILE A CB  1 
ATOM   925  C CG1 . ILE A 1 131 ? 27.392  -45.472 -10.198 1.00 37.23 ?  143 ILE A CG1 1 
ATOM   926  C CG2 . ILE A 1 131 ? 28.626  -47.036 -8.640  1.00 34.01 ?  143 ILE A CG2 1 
ATOM   927  C CD1 . ILE A 1 131 ? 26.091  -46.262 -9.992  1.00 35.84 ?  143 ILE A CD1 1 
ATOM   928  N N   . SER A 1 132 ? 31.953  -46.539 -10.586 1.00 41.34 ?  144 SER A N   1 
ATOM   929  C CA  . SER A 1 132 ? 33.225  -47.167 -10.250 1.00 42.46 ?  144 SER A CA  1 
ATOM   930  C C   . SER A 1 132 ? 34.172  -46.160 -9.616  1.00 45.69 ?  144 SER A C   1 
ATOM   931  O O   . SER A 1 132 ? 34.774  -46.430 -8.566  1.00 43.78 ?  144 SER A O   1 
ATOM   932  C CB  . SER A 1 132 ? 33.861  -47.782 -11.495 1.00 41.18 ?  144 SER A CB  1 
ATOM   933  O OG  . SER A 1 132 ? 33.373  -49.093 -11.707 1.00 47.02 ?  144 SER A OG  1 
ATOM   934  N N   . TRP A 1 133 ? 34.320  -44.990 -10.252 1.00 46.81 ?  145 TRP A N   1 
ATOM   935  C CA  . TRP A 1 133 ? 35.172  -43.929 -9.718  1.00 40.64 ?  145 TRP A CA  1 
ATOM   936  C C   . TRP A 1 133 ? 34.863  -43.667 -8.248  1.00 37.95 ?  145 TRP A C   1 
ATOM   937  O O   . TRP A 1 133 ? 35.757  -43.729 -7.399  1.00 42.82 ?  145 TRP A O   1 
ATOM   938  C CB  . TRP A 1 133 ? 35.003  -42.657 -10.554 1.00 37.41 ?  145 TRP A CB  1 
ATOM   939  C CG  . TRP A 1 133 ? 35.674  -41.438 -9.962  1.00 40.10 ?  145 TRP A CG  1 
ATOM   940  C CD1 . TRP A 1 133 ? 36.968  -41.041 -10.155 1.00 42.26 ?  145 TRP A CD1 1 
ATOM   941  C CD2 . TRP A 1 133 ? 35.080  -40.456 -9.098  1.00 35.47 ?  145 TRP A CD2 1 
ATOM   942  N NE1 . TRP A 1 133 ? 37.220  -39.890 -9.452  1.00 43.13 ?  145 TRP A NE1 1 
ATOM   943  C CE2 . TRP A 1 133 ? 36.080  -39.502 -8.802  1.00 37.71 ?  145 TRP A CE2 1 
ATOM   944  C CE3 . TRP A 1 133 ? 33.796  -40.283 -8.555  1.00 39.37 ?  145 TRP A CE3 1 
ATOM   945  C CZ2 . TRP A 1 133 ? 35.843  -38.389 -7.984  1.00 36.58 ?  145 TRP A CZ2 1 
ATOM   946  C CZ3 . TRP A 1 133 ? 33.561  -39.175 -7.726  1.00 40.12 ?  145 TRP A CZ3 1 
ATOM   947  C CH2 . TRP A 1 133 ? 34.585  -38.247 -7.451  1.00 31.43 ?  145 TRP A CH2 1 
ATOM   948  N N   . ALA A 1 134 ? 33.586  -43.427 -7.927  1.00 34.16 ?  146 ALA A N   1 
ATOM   949  C CA  . ALA A 1 134 ? 33.188  -43.171 -6.546  1.00 39.67 ?  146 ALA A CA  1 
ATOM   950  C C   . ALA A 1 134 ? 33.575  -44.318 -5.617  1.00 44.07 ?  146 ALA A C   1 
ATOM   951  O O   . ALA A 1 134 ? 33.956  -44.088 -4.464  1.00 44.00 ?  146 ALA A O   1 
ATOM   952  C CB  . ALA A 1 134 ? 31.683  -42.922 -6.471  1.00 35.80 ?  146 ALA A CB  1 
ATOM   953  N N   . LEU A 1 135 ? 33.454  -45.562 -6.085  1.00 41.46 ?  147 LEU A N   1 
ATOM   954  C CA  . LEU A 1 135 ? 33.803  -46.693 -5.231  1.00 44.18 ?  147 LEU A CA  1 
ATOM   955  C C   . LEU A 1 135 ? 35.313  -46.795 -5.054  1.00 45.20 ?  147 LEU A C   1 
ATOM   956  O O   . LEU A 1 135 ? 35.797  -47.116 -3.963  1.00 45.21 ?  147 LEU A O   1 
ATOM   957  C CB  . LEU A 1 135 ? 33.234  -47.990 -5.815  1.00 38.30 ?  147 LEU A CB  1 
ATOM   958  C CG  . LEU A 1 135 ? 31.749  -48.240 -5.556  1.00 40.81 ?  147 LEU A CG  1 
ATOM   959  C CD1 . LEU A 1 135 ? 31.217  -49.310 -6.491  1.00 40.96 ?  147 LEU A CD1 1 
ATOM   960  C CD2 . LEU A 1 135 ? 31.472  -48.614 -4.084  1.00 39.60 ?  147 LEU A CD2 1 
ATOM   961  N N   . GLN A 1 136 ? 36.072  -46.523 -6.118  1.00 46.23 ?  148 GLN A N   1 
ATOM   962  C CA  . GLN A 1 136 ? 37.523  -46.567 -6.037  1.00 45.68 ?  148 GLN A CA  1 
ATOM   963  C C   . GLN A 1 136 ? 38.093  -45.452 -5.174  1.00 50.01 ?  148 GLN A C   1 
ATOM   964  O O   . GLN A 1 136 ? 39.261  -45.532 -4.780  1.00 55.44 ?  148 GLN A O   1 
ATOM   965  C CB  . GLN A 1 136 ? 38.132  -46.498 -7.440  1.00 45.94 ?  148 GLN A CB  1 
ATOM   966  C CG  . GLN A 1 136 ? 38.417  -47.859 -8.036  1.00 49.15 ?  148 GLN A CG  1 
ATOM   967  C CD  . GLN A 1 136 ? 38.615  -47.801 -9.540  1.00 61.53 ?  148 GLN A CD  1 
ATOM   968  O OE1 . GLN A 1 136 ? 39.346  -46.948 -10.051 1.00 66.03 ?  148 GLN A OE1 1 
ATOM   969  N NE2 . GLN A 1 136 ? 37.958  -48.710 -10.260 1.00 60.82 ?  148 GLN A NE2 1 
ATOM   970  N N   . GLN A 1 137 ? 37.314  -44.411 -4.891  1.00 48.12 ?  149 GLN A N   1 
ATOM   971  C CA  . GLN A 1 137 ? 37.702  -43.389 -3.927  1.00 45.81 ?  149 GLN A CA  1 
ATOM   972  C C   . GLN A 1 137 ? 37.213  -43.706 -2.521  1.00 46.92 ?  149 GLN A C   1 
ATOM   973  O O   . GLN A 1 137 ? 37.409  -42.898 -1.611  1.00 54.71 ?  149 GLN A O   1 
ATOM   974  C CB  . GLN A 1 137 ? 37.167  -42.015 -4.361  1.00 42.18 ?  149 GLN A CB  1 
ATOM   975  C CG  . GLN A 1 137 ? 37.458  -41.662 -5.810  1.00 42.96 ?  149 GLN A CG  1 
ATOM   976  C CD  . GLN A 1 137 ? 38.774  -40.940 -5.981  1.00 50.04 ?  149 GLN A CD  1 
ATOM   977  O OE1 . GLN A 1 137 ? 38.978  -39.857 -5.419  1.00 54.06 ?  149 GLN A OE1 1 
ATOM   978  N NE2 . GLN A 1 137 ? 39.681  -41.529 -6.765  1.00 53.05 ?  149 GLN A NE2 1 
ATOM   979  N N   . GLY A 1 138 ? 36.571  -44.844 -2.315  1.00 43.94 ?  150 GLY A N   1 
ATOM   980  C CA  . GLY A 1 138 ? 36.058  -45.168 -1.005  1.00 45.30 ?  150 GLY A CA  1 
ATOM   981  C C   . GLY A 1 138 ? 34.681  -44.635 -0.676  1.00 45.59 ?  150 GLY A C   1 
ATOM   982  O O   . GLY A 1 138 ? 34.250  -44.759 0.477   1.00 46.92 ?  150 GLY A O   1 
ATOM   983  N N   . TYR A 1 139 ? 33.963  -44.064 -1.635  1.00 41.40 ?  151 TYR A N   1 
ATOM   984  C CA  . TYR A 1 139 ? 32.654  -43.521 -1.307  1.00 45.43 ?  151 TYR A CA  1 
ATOM   985  C C   . TYR A 1 139 ? 31.599  -44.621 -1.265  1.00 42.37 ?  151 TYR A C   1 
ATOM   986  O O   . TYR A 1 139 ? 31.650  -45.596 -2.016  1.00 43.42 ?  151 TYR A O   1 
ATOM   987  C CB  . TYR A 1 139 ? 32.235  -42.432 -2.305  1.00 44.78 ?  151 TYR A CB  1 
ATOM   988  C CG  . TYR A 1 139 ? 33.274  -41.339 -2.514  1.00 48.79 ?  151 TYR A CG  1 
ATOM   989  C CD1 . TYR A 1 139 ? 33.422  -40.725 -3.752  1.00 44.21 ?  151 TYR A CD1 1 
ATOM   990  C CD2 . TYR A 1 139 ? 34.117  -40.934 -1.471  1.00 51.70 ?  151 TYR A CD2 1 
ATOM   991  C CE1 . TYR A 1 139 ? 34.360  -39.727 -3.955  1.00 48.83 ?  151 TYR A CE1 1 
ATOM   992  C CE2 . TYR A 1 139 ? 35.071  -39.931 -1.672  1.00 51.45 ?  151 TYR A CE2 1 
ATOM   993  C CZ  . TYR A 1 139 ? 35.183  -39.333 -2.916  1.00 49.43 ?  151 TYR A CZ  1 
ATOM   994  O OH  . TYR A 1 139 ? 36.122  -38.349 -3.128  1.00 46.41 ?  151 TYR A OH  1 
ATOM   995  N N   . TYR A 1 140 ? 30.650  -44.461 -0.355  1.00 38.82 ?  152 TYR A N   1 
ATOM   996  C CA  . TYR A 1 140 ? 29.444  -45.269 -0.350  1.00 43.30 ?  152 TYR A CA  1 
ATOM   997  C C   . TYR A 1 140 ? 28.505  -44.764 -1.439  1.00 44.47 ?  152 TYR A C   1 
ATOM   998  O O   . TYR A 1 140 ? 28.264  -43.557 -1.539  1.00 43.40 ?  152 TYR A O   1 
ATOM   999  C CB  . TYR A 1 140 ? 28.764  -45.178 1.018   1.00 44.90 ?  152 TYR A CB  1 
ATOM   1000 C CG  . TYR A 1 140 ? 29.527  -45.855 2.130   1.00 50.64 ?  152 TYR A CG  1 
ATOM   1001 C CD1 . TYR A 1 140 ? 29.386  -47.222 2.358   1.00 51.65 ?  152 TYR A CD1 1 
ATOM   1002 C CD2 . TYR A 1 140 ? 30.392  -45.130 2.956   1.00 52.74 ?  152 TYR A CD2 1 
ATOM   1003 C CE1 . TYR A 1 140 ? 30.079  -47.850 3.377   1.00 55.86 ?  152 TYR A CE1 1 
ATOM   1004 C CE2 . TYR A 1 140 ? 31.097  -45.754 3.975   1.00 53.04 ?  152 TYR A CE2 1 
ATOM   1005 C CZ  . TYR A 1 140 ? 30.933  -47.116 4.183   1.00 56.09 ?  152 TYR A CZ  1 
ATOM   1006 O OH  . TYR A 1 140 ? 31.621  -47.762 5.187   1.00 57.68 ?  152 TYR A OH  1 
ATOM   1007 N N   . VAL A 1 141 ? 27.958  -45.676 -2.243  1.00 44.03 ?  153 VAL A N   1 
ATOM   1008 C CA  . VAL A 1 141 ? 27.157  -45.310 -3.408  1.00 36.23 ?  153 VAL A CA  1 
ATOM   1009 C C   . VAL A 1 141 ? 25.714  -45.762 -3.216  1.00 39.46 ?  153 VAL A C   1 
ATOM   1010 O O   . VAL A 1 141 ? 25.448  -46.937 -2.943  1.00 38.88 ?  153 VAL A O   1 
ATOM   1011 C CB  . VAL A 1 141 ? 27.744  -45.896 -4.700  1.00 40.96 ?  153 VAL A CB  1 
ATOM   1012 C CG1 . VAL A 1 141 ? 26.986  -45.340 -5.885  1.00 40.04 ?  153 VAL A CG1 1 
ATOM   1013 C CG2 . VAL A 1 141 ? 29.231  -45.574 -4.810  1.00 35.37 ?  153 VAL A CG2 1 
ATOM   1014 N N   . VAL A 1 142 ? 24.784  -44.822 -3.353  1.00 36.03 ?  154 VAL A N   1 
ATOM   1015 C CA  . VAL A 1 142 ? 23.368  -45.112 -3.491  1.00 33.19 ?  154 VAL A CA  1 
ATOM   1016 C C   . VAL A 1 142 ? 22.908  -44.596 -4.851  1.00 40.98 ?  154 VAL A C   1 
ATOM   1017 O O   . VAL A 1 142 ? 23.401  -43.583 -5.362  1.00 39.42 ?  154 VAL A O   1 
ATOM   1018 C CB  . VAL A 1 142 ? 22.519  -44.491 -2.362  1.00 40.05 ?  154 VAL A CB  1 
ATOM   1019 C CG1 . VAL A 1 142 ? 22.730  -42.973 -2.299  1.00 37.55 ?  154 VAL A CG1 1 
ATOM   1020 C CG2 . VAL A 1 142 ? 21.033  -44.822 -2.562  1.00 37.52 ?  154 VAL A CG2 1 
ATOM   1021 N N   . SER A 1 143 ? 21.978  -45.326 -5.457  1.00 40.37 ?  155 SER A N   1 
ATOM   1022 C CA  . SER A 1 143 ? 21.256  -44.851 -6.633  1.00 36.69 ?  155 SER A CA  1 
ATOM   1023 C C   . SER A 1 143 ? 19.815  -45.303 -6.465  1.00 37.22 ?  155 SER A C   1 
ATOM   1024 O O   . SER A 1 143 ? 19.523  -46.499 -6.536  1.00 39.22 ?  155 SER A O   1 
ATOM   1025 C CB  . SER A 1 143 ? 21.869  -45.385 -7.920  1.00 34.83 ?  155 SER A CB  1 
ATOM   1026 O OG  . SER A 1 143 ? 21.041  -45.079 -9.026  1.00 36.60 ?  155 SER A OG  1 
ATOM   1027 N N   . SER A 1 144 ? 18.930  -44.361 -6.183  1.00 33.91 ?  156 SER A N   1 
ATOM   1028 C CA  . SER A 1 144 ? 17.554  -44.706 -5.895  1.00 33.45 ?  156 SER A CA  1 
ATOM   1029 C C   . SER A 1 144 ? 16.783  -44.965 -7.187  1.00 36.13 ?  156 SER A C   1 
ATOM   1030 O O   . SER A 1 144 ? 17.184  -44.557 -8.278  1.00 32.50 ?  156 SER A O   1 
ATOM   1031 C CB  . SER A 1 144 ? 16.876  -43.583 -5.107  1.00 37.94 ?  156 SER A CB  1 
ATOM   1032 O OG  . SER A 1 144 ? 17.380  -43.468 -3.782  1.00 39.64 ?  156 SER A OG  1 
ATOM   1033 N N   . ASP A 1 145 ? 15.651  -45.651 -7.052  1.00 35.90 ?  157 ASP A N   1 
ATOM   1034 C CA  . ASP A 1 145 ? 14.646  -45.641 -8.112  1.00 34.25 ?  157 ASP A CA  1 
ATOM   1035 C C   . ASP A 1 145 ? 13.891  -44.322 -7.970  1.00 33.68 ?  157 ASP A C   1 
ATOM   1036 O O   . ASP A 1 145 ? 12.778  -44.248 -7.434  1.00 31.75 ?  157 ASP A O   1 
ATOM   1037 C CB  . ASP A 1 145 ? 13.730  -46.861 -8.028  1.00 33.62 ?  157 ASP A CB  1 
ATOM   1038 C CG  . ASP A 1 145 ? 14.454  -48.169 -8.406  1.00 35.55 ?  157 ASP A CG  1 
ATOM   1039 O OD1 . ASP A 1 145 ? 15.625  -48.101 -8.853  1.00 33.32 ?  157 ASP A OD1 1 
ATOM   1040 O OD2 . ASP A 1 145 ? 13.855  -49.265 -8.245  1.00 37.35 ?  157 ASP A OD2 1 
ATOM   1041 N N   . HIS A 1 146 ? 14.528  -43.252 -8.472  1.00 31.77 ?  158 HIS A N   1 
ATOM   1042 C CA  . HIS A 1 146 ? 14.023  -41.900 -8.237  1.00 30.20 ?  158 HIS A CA  1 
ATOM   1043 C C   . HIS A 1 146 ? 12.615  -41.702 -8.781  1.00 31.13 ?  158 HIS A C   1 
ATOM   1044 O O   . HIS A 1 146 ? 11.878  -40.847 -8.279  1.00 31.71 ?  158 HIS A O   1 
ATOM   1045 C CB  . HIS A 1 146 ? 14.951  -40.885 -8.871  1.00 30.85 ?  158 HIS A CB  1 
ATOM   1046 C CG  . HIS A 1 146 ? 15.213  -41.162 -10.310 1.00 30.34 ?  158 HIS A CG  1 
ATOM   1047 N ND1 . HIS A 1 146 ? 16.091  -42.144 -10.726 1.00 33.15 ?  158 HIS A ND1 1 
ATOM   1048 C CD2 . HIS A 1 146 ? 14.686  -40.620 -11.434 1.00 29.77 ?  158 HIS A CD2 1 
ATOM   1049 C CE1 . HIS A 1 146 ? 16.102  -42.182 -12.049 1.00 33.27 ?  158 HIS A CE1 1 
ATOM   1050 N NE2 . HIS A 1 146 ? 15.271  -41.258 -12.503 1.00 30.54 ?  158 HIS A NE2 1 
ATOM   1051 N N   . GLU A 1 147 ? 12.210  -42.479 -9.793  1.00 35.16 ?  159 GLU A N   1 
ATOM   1052 C CA  . GLU A 1 147 ? 10.843  -42.335 -10.286 1.00 32.24 ?  159 GLU A CA  1 
ATOM   1053 C C   . GLU A 1 147 ? 9.807   -42.946 -9.341  1.00 32.63 ?  159 GLU A C   1 
ATOM   1054 O O   . GLU A 1 147 ? 8.614   -42.640 -9.464  1.00 31.68 ?  159 GLU A O   1 
ATOM   1055 C CB  . GLU A 1 147 ? 10.740  -42.931 -11.690 1.00 35.93 ?  159 GLU A CB  1 
ATOM   1056 C CG  . GLU A 1 147 ? 11.479  -42.113 -12.751 1.00 31.70 ?  159 GLU A CG  1 
ATOM   1057 C CD  . GLU A 1 147 ? 11.198  -42.627 -14.153 1.00 39.53 ?  159 GLU A CD  1 
ATOM   1058 O OE1 . GLU A 1 147 ? 10.251  -43.431 -14.267 1.00 39.17 ?  159 GLU A OE1 1 
ATOM   1059 O OE2 . GLU A 1 147 ? 11.912  -42.254 -15.125 1.00 34.45 ?  159 GLU A OE2 1 
ATOM   1060 N N   . GLY A 1 148 ? 10.231  -43.755 -8.371  1.00 34.00 ?  160 GLY A N   1 
ATOM   1061 C CA  . GLY A 1 148 ? 9.314   -44.308 -7.408  1.00 37.03 ?  160 GLY A CA  1 
ATOM   1062 C C   . GLY A 1 148 ? 8.468   -45.435 -7.972  1.00 38.26 ?  160 GLY A C   1 
ATOM   1063 O O   . GLY A 1 148 ? 8.554   -45.791 -9.157  1.00 34.08 ?  160 GLY A O   1 
ATOM   1064 N N   . PRO A 1 149 ? 7.624   -46.021 -7.120  1.00 38.11 ?  161 PRO A N   1 
ATOM   1065 C CA  . PRO A 1 149 ? 6.800   -47.154 -7.587  1.00 41.45 ?  161 PRO A CA  1 
ATOM   1066 C C   . PRO A 1 149 ? 5.809   -46.773 -8.681  1.00 34.70 ?  161 PRO A C   1 
ATOM   1067 O O   . PRO A 1 149 ? 5.473   -47.635 -9.500  1.00 34.95 ?  161 PRO A O   1 
ATOM   1068 C CB  . PRO A 1 149 ? 6.088   -47.628 -6.309  1.00 34.71 ?  161 PRO A CB  1 
ATOM   1069 C CG  . PRO A 1 149 ? 6.049   -46.385 -5.422  1.00 37.84 ?  161 PRO A CG  1 
ATOM   1070 C CD  . PRO A 1 149 ? 7.347   -45.659 -5.717  1.00 37.79 ?  161 PRO A CD  1 
ATOM   1071 N N   . ARG A 1 150 ? 5.341   -45.517 -8.739  1.00 31.24 ?  162 ARG A N   1 
ATOM   1072 C CA  . ARG A 1 150 ? 4.421   -45.092 -9.795  1.00 33.64 ?  162 ARG A CA  1 
ATOM   1073 C C   . ARG A 1 150 ? 5.116   -44.744 -11.119 1.00 33.97 ?  162 ARG A C   1 
ATOM   1074 O O   . ARG A 1 150 ? 4.444   -44.215 -12.019 1.00 34.46 ?  162 ARG A O   1 
ATOM   1075 C CB  . ARG A 1 150 ? 3.596   -43.888 -9.348  1.00 30.85 ?  162 ARG A CB  1 
ATOM   1076 C CG  . ARG A 1 150 ? 3.022   -43.995 -7.968  1.00 33.15 ?  162 ARG A CG  1 
ATOM   1077 C CD  . ARG A 1 150 ? 1.866   -43.032 -7.812  1.00 30.87 ?  162 ARG A CD  1 
ATOM   1078 N NE  . ARG A 1 150 ? 2.348   -41.755 -7.302  1.00 32.75 ?  162 ARG A NE  1 
ATOM   1079 C CZ  . ARG A 1 150 ? 1.573   -40.709 -7.063  1.00 37.44 ?  162 ARG A CZ  1 
ATOM   1080 N NH1 . ARG A 1 150 ? 0.263   -40.783 -7.184  1.00 36.32 ?  162 ARG A NH1 1 
ATOM   1081 N NH2 . ARG A 1 150 ? 2.127   -39.563 -6.678  1.00 42.32 ?  162 ARG A NH2 1 
ATOM   1082 N N   . SER A 1 151 ? 6.417   -45.016 -11.235 1.00 28.75 ?  163 SER A N   1 
ATOM   1083 C CA  . SER A 1 151 ? 7.241   -44.731 -12.417 1.00 35.30 ?  163 SER A CA  1 
ATOM   1084 C C   . SER A 1 151 ? 7.000   -43.333 -13.004 1.00 37.20 ?  163 SER A C   1 
ATOM   1085 O O   . SER A 1 151 ? 6.856   -43.158 -14.220 1.00 33.16 ?  163 SER A O   1 
ATOM   1086 C CB  . SER A 1 151 ? 7.031   -45.803 -13.477 1.00 33.87 ?  163 SER A CB  1 
ATOM   1087 O OG  . SER A 1 151 ? 7.875   -46.900 -13.211 1.00 37.74 ?  163 SER A OG  1 
ATOM   1088 N N   . ALA A 1 152 ? 7.037   -42.317 -12.133 1.00 32.54 ?  164 ALA A N   1 
ATOM   1089 C CA  . ALA A 1 152 ? 6.594   -40.964 -12.492 1.00 33.11 ?  164 ALA A CA  1 
ATOM   1090 C C   . ALA A 1 152 ? 7.762   -40.099 -12.996 1.00 32.61 ?  164 ALA A C   1 
ATOM   1091 O O   . ALA A 1 152 ? 8.199   -39.136 -12.362 1.00 32.31 ?  164 ALA A O   1 
ATOM   1092 C CB  . ALA A 1 152 ? 5.882   -40.319 -11.309 1.00 30.49 ?  164 ALA A CB  1 
ATOM   1093 N N   . PHE A 1 153 ? 8.220   -40.431 -14.203 1.00 38.56 ?  165 PHE A N   1 
ATOM   1094 C CA  . PHE A 1 153 ? 9.258   -39.669 -14.905 1.00 37.40 ?  165 PHE A CA  1 
ATOM   1095 C C   . PHE A 1 153 ? 8.970   -38.158 -14.916 1.00 38.03 ?  165 PHE A C   1 
ATOM   1096 O O   . PHE A 1 153 ? 7.834   -37.724 -15.147 1.00 34.40 ?  165 PHE A O   1 
ATOM   1097 C CB  . PHE A 1 153 ? 9.377   -40.234 -16.335 1.00 35.92 ?  165 PHE A CB  1 
ATOM   1098 C CG  . PHE A 1 153 ? 10.283  -39.453 -17.246 1.00 35.68 ?  165 PHE A CG  1 
ATOM   1099 C CD1 . PHE A 1 153 ? 11.553  -39.085 -16.840 1.00 30.43 ?  165 PHE A CD1 1 
ATOM   1100 C CD2 . PHE A 1 153 ? 9.865   -39.115 -18.533 1.00 29.89 ?  165 PHE A CD2 1 
ATOM   1101 C CE1 . PHE A 1 153 ? 12.381  -38.362 -17.687 1.00 34.05 ?  165 PHE A CE1 1 
ATOM   1102 C CE2 . PHE A 1 153 ? 10.684  -38.406 -19.380 1.00 30.42 ?  165 PHE A CE2 1 
ATOM   1103 C CZ  . PHE A 1 153 ? 11.953  -38.023 -18.956 1.00 33.58 ?  165 PHE A CZ  1 
ATOM   1104 N N   . ILE A 1 154 ? 10.043  -37.370 -14.682 1.00 35.09 ?  166 ILE A N   1 
ATOM   1105 C CA  . ILE A 1 154 ? 10.159  -35.918 -14.439 1.00 30.61 ?  166 ILE A CA  1 
ATOM   1106 C C   . ILE A 1 154 ? 9.122   -35.314 -13.496 1.00 31.57 ?  166 ILE A C   1 
ATOM   1107 O O   . ILE A 1 154 ? 8.863   -34.105 -13.543 1.00 31.66 ?  166 ILE A O   1 
ATOM   1108 C CB  . ILE A 1 154 ? 10.196  -35.074 -15.736 1.00 30.46 ?  166 ILE A CB  1 
ATOM   1109 C CG1 . ILE A 1 154 ? 9.059   -35.414 -16.657 1.00 30.00 ?  166 ILE A CG1 1 
ATOM   1110 C CG2 . ILE A 1 154 ? 11.602  -35.058 -16.428 1.00 29.82 ?  166 ILE A CG2 1 
ATOM   1111 C CD1 . ILE A 1 154 ? 7.950   -34.501 -16.506 1.00 34.62 ?  166 ILE A CD1 1 
ATOM   1112 N N   . ALA A 1 155 ? 8.576   -36.104 -12.584 1.00 34.67 ?  167 ALA A N   1 
ATOM   1113 C CA  . ALA A 1 155 ? 7.752   -35.553 -11.510 1.00 35.66 ?  167 ALA A CA  1 
ATOM   1114 C C   . ALA A 1 155 ? 8.685   -35.156 -10.366 1.00 34.08 ?  167 ALA A C   1 
ATOM   1115 O O   . ALA A 1 155 ? 9.183   -36.020 -9.635  1.00 31.48 ?  167 ALA A O   1 
ATOM   1116 C CB  . ALA A 1 155 ? 6.705   -36.563 -11.057 1.00 34.81 ?  167 ALA A CB  1 
ATOM   1117 N N   . GLY A 1 156 ? 8.909   -33.847 -10.210 1.00 31.47 ?  168 GLY A N   1 
ATOM   1118 C CA  . GLY A 1 156 ? 10.032  -33.377 -9.402  1.00 33.22 ?  168 GLY A CA  1 
ATOM   1119 C C   . GLY A 1 156 ? 9.924   -33.713 -7.920  1.00 31.84 ?  168 GLY A C   1 
ATOM   1120 O O   . GLY A 1 156 ? 10.898  -34.151 -7.300  1.00 33.67 ?  168 GLY A O   1 
ATOM   1121 N N   . TYR A 1 157 ? 8.752   -33.486 -7.322  1.00 33.13 ?  169 TYR A N   1 
ATOM   1122 C CA  . TYR A 1 157 ? 8.579   -33.817 -5.906  1.00 31.65 ?  169 TYR A CA  1 
ATOM   1123 C C   . TYR A 1 157 ? 8.746   -35.310 -5.683  1.00 31.85 ?  169 TYR A C   1 
ATOM   1124 O O   . TYR A 1 157 ? 9.458   -35.735 -4.763  1.00 35.37 ?  169 TYR A O   1 
ATOM   1125 C CB  . TYR A 1 157 ? 7.217   -33.320 -5.413  1.00 27.43 ?  169 TYR A CB  1 
ATOM   1126 C CG  . TYR A 1 157 ? 7.080   -31.853 -5.669  1.00 34.51 ?  169 TYR A CG  1 
ATOM   1127 C CD1 . TYR A 1 157 ? 7.523   -30.922 -4.730  1.00 34.22 ?  169 TYR A CD1 1 
ATOM   1128 C CD2 . TYR A 1 157 ? 6.590   -31.381 -6.883  1.00 35.42 ?  169 TYR A CD2 1 
ATOM   1129 C CE1 . TYR A 1 157 ? 7.447   -29.564 -4.975  1.00 30.48 ?  169 TYR A CE1 1 
ATOM   1130 C CE2 . TYR A 1 157 ? 6.510   -30.015 -7.140  1.00 35.15 ?  169 TYR A CE2 1 
ATOM   1131 C CZ  . TYR A 1 157 ? 6.943   -29.115 -6.183  1.00 36.72 ?  169 TYR A CZ  1 
ATOM   1132 O OH  . TYR A 1 157 ? 6.877   -27.760 -6.429  1.00 40.48 ?  169 TYR A OH  1 
ATOM   1133 N N   . GLU A 1 158 ? 8.141   -36.118 -6.559  1.00 35.63 ?  170 GLU A N   1 
ATOM   1134 C CA  . GLU A 1 158 ? 8.274   -37.570 -6.491  1.00 32.12 ?  170 GLU A CA  1 
ATOM   1135 C C   . GLU A 1 158 ? 9.740   -37.997 -6.550  1.00 33.22 ?  170 GLU A C   1 
ATOM   1136 O O   . GLU A 1 158 ? 10.207  -38.767 -5.704  1.00 33.58 ?  170 GLU A O   1 
ATOM   1137 C CB  . GLU A 1 158 ? 7.458   -38.202 -7.626  1.00 30.98 ?  170 GLU A CB  1 
ATOM   1138 C CG  . GLU A 1 158 ? 7.013   -39.631 -7.385  1.00 30.99 ?  170 GLU A CG  1 
ATOM   1139 C CD  . GLU A 1 158 ? 5.583   -39.733 -6.885  1.00 35.12 ?  170 GLU A CD  1 
ATOM   1140 O OE1 . GLU A 1 158 ? 4.889   -38.693 -6.750  1.00 35.43 ?  170 GLU A OE1 1 
ATOM   1141 O OE2 . GLU A 1 158 ? 5.154   -40.872 -6.630  1.00 37.40 ?  170 GLU A OE2 1 
ATOM   1142 N N   . GLU A 1 159 ? 10.491  -37.486 -7.531  1.00 33.89 ?  171 GLU A N   1 
ATOM   1143 C CA  . GLU A 1 159 ? 11.915  -37.815 -7.630  1.00 33.26 ?  171 GLU A CA  1 
ATOM   1144 C C   . GLU A 1 159 ? 12.717  -37.276 -6.438  1.00 32.41 ?  171 GLU A C   1 
ATOM   1145 O O   . GLU A 1 159 ? 13.569  -37.976 -5.880  1.00 34.28 ?  171 GLU A O   1 
ATOM   1146 C CB  . GLU A 1 159 ? 12.476  -37.280 -8.953  1.00 32.34 ?  171 GLU A CB  1 
ATOM   1147 C CG  . GLU A 1 159 ? 11.918  -37.993 -10.185 1.00 34.56 ?  171 GLU A CG  1 
ATOM   1148 C CD  . GLU A 1 159 ? 12.350  -37.359 -11.492 1.00 32.13 ?  171 GLU A CD  1 
ATOM   1149 O OE1 . GLU A 1 159 ? 13.022  -36.311 -11.461 1.00 31.34 ?  171 GLU A OE1 1 
ATOM   1150 O OE2 . GLU A 1 159 ? 12.035  -37.924 -12.559 1.00 34.78 ?  171 GLU A OE2 1 
ATOM   1151 N N   . GLY A 1 160 ? 12.491  -36.022 -6.054  1.00 32.40 ?  172 GLY A N   1 
ATOM   1152 C CA  . GLY A 1 160 ? 13.240  -35.450 -4.950  1.00 34.39 ?  172 GLY A CA  1 
ATOM   1153 C C   . GLY A 1 160 ? 13.124  -36.231 -3.653  1.00 32.76 ?  172 GLY A C   1 
ATOM   1154 O O   . GLY A 1 160 ? 14.136  -36.677 -3.095  1.00 31.30 ?  172 GLY A O   1 
ATOM   1155 N N   . MET A 1 161 ? 11.890  -36.407 -3.173  1.00 29.63 ?  173 MET A N   1 
ATOM   1156 C CA  . MET A 1 161 ? 11.675  -37.094 -1.902  1.00 30.38 ?  173 MET A CA  1 
ATOM   1157 C C   . MET A 1 161 ? 12.212  -38.519 -1.957  1.00 38.33 ?  173 MET A C   1 
ATOM   1158 O O   . MET A 1 161 ? 12.803  -39.013 -0.986  1.00 36.80 ?  173 MET A O   1 
ATOM   1159 C CB  . MET A 1 161 ? 10.183  -37.080 -1.564  1.00 31.01 ?  173 MET A CB  1 
ATOM   1160 C CG  . MET A 1 161 ? 9.712   -35.675 -1.215  1.00 32.71 ?  173 MET A CG  1 
ATOM   1161 S SD  . MET A 1 161 ? 8.025   -35.521 -0.655  1.00 36.14 ?  173 MET A SD  1 
ATOM   1162 C CE  . MET A 1 161 ? 7.155   -35.674 -2.243  1.00 35.24 ?  173 MET A CE  1 
ATOM   1163 N N   . ALA A 1 162 ? 12.049  -39.181 -3.105  1.00 35.88 ?  174 ALA A N   1 
ATOM   1164 C CA  . ALA A 1 162 ? 12.525  -40.547 -3.250  1.00 31.60 ?  174 ALA A CA  1 
ATOM   1165 C C   . ALA A 1 162 ? 14.046  -40.619 -3.162  1.00 34.14 ?  174 ALA A C   1 
ATOM   1166 O O   . ALA A 1 162 ? 14.597  -41.532 -2.535  1.00 34.26 ?  174 ALA A O   1 
ATOM   1167 C CB  . ALA A 1 162 ? 12.018  -41.126 -4.576  1.00 28.59 ?  174 ALA A CB  1 
ATOM   1168 N N   . ILE A 1 163 ? 14.749  -39.676 -3.798  1.00 35.56 ?  175 ILE A N   1 
ATOM   1169 C CA  . ILE A 1 163 ? 16.211  -39.685 -3.732  1.00 39.80 ?  175 ILE A CA  1 
ATOM   1170 C C   . ILE A 1 163 ? 16.686  -39.416 -2.303  1.00 34.02 ?  175 ILE A C   1 
ATOM   1171 O O   . ILE A 1 163 ? 17.564  -40.115 -1.788  1.00 35.57 ?  175 ILE A O   1 
ATOM   1172 C CB  . ILE A 1 163 ? 16.808  -38.675 -4.729  1.00 37.10 ?  175 ILE A CB  1 
ATOM   1173 C CG1 . ILE A 1 163 ? 16.540  -39.135 -6.160  1.00 32.61 ?  175 ILE A CG1 1 
ATOM   1174 C CG2 . ILE A 1 163 ? 18.311  -38.525 -4.522  1.00 30.64 ?  175 ILE A CG2 1 
ATOM   1175 C CD1 . ILE A 1 163 ? 16.767  -38.071 -7.179  1.00 29.64 ?  175 ILE A CD1 1 
ATOM   1176 N N   . LEU A 1 164 ? 16.112  -38.410 -1.638  1.00 31.87 ?  176 LEU A N   1 
ATOM   1177 C CA  . LEU A 1 164 ? 16.582  -38.077 -0.291  1.00 37.75 ?  176 LEU A CA  1 
ATOM   1178 C C   . LEU A 1 164 ? 16.265  -39.196 0.704   1.00 40.29 ?  176 LEU A C   1 
ATOM   1179 O O   . LEU A 1 164 ? 17.128  -39.576 1.511   1.00 35.70 ?  176 LEU A O   1 
ATOM   1180 C CB  . LEU A 1 164 ? 15.979  -36.749 0.171   1.00 33.48 ?  176 LEU A CB  1 
ATOM   1181 C CG  . LEU A 1 164 ? 16.209  -35.572 -0.786  1.00 34.68 ?  176 LEU A CG  1 
ATOM   1182 C CD1 . LEU A 1 164 ? 15.082  -34.533 -0.655  1.00 31.40 ?  176 LEU A CD1 1 
ATOM   1183 C CD2 . LEU A 1 164 ? 17.597  -34.957 -0.570  1.00 28.17 ?  176 LEU A CD2 1 
ATOM   1184 N N   . ASP A 1 165 ? 15.038  -39.746 0.643   1.00 34.36 ?  177 ASP A N   1 
ATOM   1185 C CA  . ASP A 1 165 ? 14.680  -40.866 1.499   1.00 36.49 ?  177 ASP A CA  1 
ATOM   1186 C C   . ASP A 1 165 ? 15.490  -42.099 1.148   1.00 36.53 ?  177 ASP A C   1 
ATOM   1187 O O   . ASP A 1 165 ? 15.729  -42.948 2.013   1.00 36.51 ?  177 ASP A O   1 
ATOM   1188 C CB  . ASP A 1 165 ? 13.184  -41.158 1.404   1.00 34.90 ?  177 ASP A CB  1 
ATOM   1189 C CG  . ASP A 1 165 ? 12.361  -40.189 2.217   1.00 37.11 ?  177 ASP A CG  1 
ATOM   1190 O OD1 . ASP A 1 165 ? 12.853  -39.792 3.291   1.00 41.52 ?  177 ASP A OD1 1 
ATOM   1191 O OD2 . ASP A 1 165 ? 11.244  -39.808 1.796   1.00 36.13 ?  177 ASP A OD2 1 
ATOM   1192 N N   . GLY A 1 166 ? 15.943  -42.203 -0.099  1.00 35.51 ?  178 GLY A N   1 
ATOM   1193 C CA  . GLY A 1 166 ? 16.893  -43.249 -0.432  1.00 33.11 ?  178 GLY A CA  1 
ATOM   1194 C C   . GLY A 1 166 ? 18.203  -43.090 0.314   1.00 37.30 ?  178 GLY A C   1 
ATOM   1195 O O   . GLY A 1 166 ? 18.837  -44.078 0.700   1.00 39.76 ?  178 GLY A O   1 
ATOM   1196 N N   . ILE A 1 167 ? 18.624  -41.841 0.535   1.00 37.71 ?  179 ILE A N   1 
ATOM   1197 C CA  . ILE A 1 167 ? 19.872  -41.602 1.253   1.00 37.36 ?  179 ILE A CA  1 
ATOM   1198 C C   . ILE A 1 167 ? 19.695  -41.905 2.732   1.00 36.67 ?  179 ILE A C   1 
ATOM   1199 O O   . ILE A 1 167 ? 20.542  -42.567 3.344   1.00 37.36 ?  179 ILE A O   1 
ATOM   1200 C CB  . ILE A 1 167 ? 20.368  -40.164 1.012   1.00 41.31 ?  179 ILE A CB  1 
ATOM   1201 C CG1 . ILE A 1 167 ? 20.892  -40.013 -0.433  1.00 34.51 ?  179 ILE A CG1 1 
ATOM   1202 C CG2 . ILE A 1 167 ? 21.459  -39.779 2.031   1.00 28.46 ?  179 ILE A CG2 1 
ATOM   1203 C CD1 . ILE A 1 167 ? 20.709  -38.621 -1.000  1.00 31.75 ?  179 ILE A CD1 1 
ATOM   1204 N N   . ARG A 1 168 ? 18.578  -41.460 3.320   1.00 35.73 ?  180 ARG A N   1 
ATOM   1205 C CA  . ARG A 1 168 ? 18.263  -41.841 4.694   1.00 39.68 ?  180 ARG A CA  1 
ATOM   1206 C C   . ARG A 1 168 ? 18.289  -43.361 4.865   1.00 45.51 ?  180 ARG A C   1 
ATOM   1207 O O   . ARG A 1 168 ? 18.880  -43.878 5.825   1.00 46.47 ?  180 ARG A O   1 
ATOM   1208 C CB  . ARG A 1 168 ? 16.901  -41.270 5.100   1.00 35.08 ?  180 ARG A CB  1 
ATOM   1209 C CG  . ARG A 1 168 ? 16.798  -39.755 4.966   1.00 35.94 ?  180 ARG A CG  1 
ATOM   1210 C CD  . ARG A 1 168 ? 15.367  -39.267 5.229   1.00 35.30 ?  180 ARG A CD  1 
ATOM   1211 N NE  . ARG A 1 168 ? 15.325  -37.924 5.796   1.00 34.26 ?  180 ARG A NE  1 
ATOM   1212 C CZ  . ARG A 1 168 ? 14.254  -37.140 5.806   1.00 38.76 ?  180 ARG A CZ  1 
ATOM   1213 N NH1 . ARG A 1 168 ? 13.121  -37.510 5.232   1.00 37.96 ?  180 ARG A NH1 1 
ATOM   1214 N NH2 . ARG A 1 168 ? 14.317  -35.960 6.418   1.00 35.28 ?  180 ARG A NH2 1 
ATOM   1215 N N   . ALA A 1 169 ? 17.684  -44.095 3.922   1.00 42.25 ?  181 ALA A N   1 
ATOM   1216 C CA  . ALA A 1 169 ? 17.703  -45.555 3.978   1.00 45.21 ?  181 ALA A CA  1 
ATOM   1217 C C   . ALA A 1 169 ? 19.128  -46.103 3.893   1.00 39.85 ?  181 ALA A C   1 
ATOM   1218 O O   . ALA A 1 169 ? 19.483  -47.030 4.625   1.00 42.80 ?  181 ALA A O   1 
ATOM   1219 C CB  . ALA A 1 169 ? 16.824  -46.133 2.863   1.00 40.63 ?  181 ALA A CB  1 
ATOM   1220 N N   . PHE A 1 170 ? 19.962  -45.550 3.010   1.00 41.47 ?  182 PHE A N   1 
ATOM   1221 C CA  . PHE A 1 170 ? 21.360  -45.978 2.972   1.00 41.17 ?  182 PHE A CA  1 
ATOM   1222 C C   . PHE A 1 170 ? 22.037  -45.744 4.319   1.00 47.58 ?  182 PHE A C   1 
ATOM   1223 O O   . PHE A 1 170 ? 22.784  -46.604 4.811   1.00 45.28 ?  182 PHE A O   1 
ATOM   1224 C CB  . PHE A 1 170 ? 22.115  -45.236 1.871   1.00 42.00 ?  182 PHE A CB  1 
ATOM   1225 C CG  . PHE A 1 170 ? 23.408  -45.900 1.455   1.00 38.97 ?  182 PHE A CG  1 
ATOM   1226 C CD1 . PHE A 1 170 ? 23.744  -47.167 1.920   1.00 39.79 ?  182 PHE A CD1 1 
ATOM   1227 C CD2 . PHE A 1 170 ? 24.277  -45.260 0.586   1.00 36.78 ?  182 PHE A CD2 1 
ATOM   1228 C CE1 . PHE A 1 170 ? 24.924  -47.781 1.520   1.00 39.61 ?  182 PHE A CE1 1 
ATOM   1229 C CE2 . PHE A 1 170 ? 25.450  -45.869 0.171   1.00 38.83 ?  182 PHE A CE2 1 
ATOM   1230 C CZ  . PHE A 1 170 ? 25.776  -47.131 0.640   1.00 38.55 ?  182 PHE A CZ  1 
ATOM   1231 N N   . LYS A 1 171 ? 21.773  -44.585 4.934   1.00 45.78 ?  183 LYS A N   1 
ATOM   1232 C CA  . LYS A 1 171 ? 22.384  -44.270 6.221   1.00 49.68 ?  183 LYS A CA  1 
ATOM   1233 C C   . LYS A 1 171 ? 21.850  -45.182 7.323   1.00 46.69 ?  183 LYS A C   1 
ATOM   1234 O O   . LYS A 1 171 ? 22.629  -45.710 8.124   1.00 45.21 ?  183 LYS A O   1 
ATOM   1235 C CB  . LYS A 1 171 ? 22.160  -42.794 6.558   1.00 38.47 ?  183 LYS A CB  1 
ATOM   1236 C CG  . LYS A 1 171 ? 23.097  -41.851 5.787   1.00 43.39 ?  183 LYS A CG  1 
ATOM   1237 C CD  . LYS A 1 171 ? 22.560  -40.422 5.745   1.00 42.48 ?  183 LYS A CD  1 
ATOM   1238 C CE  . LYS A 1 171 ? 22.733  -39.704 7.095   1.00 47.64 ?  183 LYS A CE  1 
ATOM   1239 N NZ  . LYS A 1 171 ? 21.738  -38.602 7.299   1.00 43.50 ?  183 LYS A NZ  1 
ATOM   1240 N N   . ASN A 1 172 ? 20.530  -45.388 7.367   1.00 45.53 ?  184 ASN A N   1 
ATOM   1241 C CA  . ASN A 1 172 ? 19.943  -46.309 8.334   1.00 41.19 ?  184 ASN A CA  1 
ATOM   1242 C C   . ASN A 1 172 ? 20.509  -47.712 8.181   1.00 48.79 ?  184 ASN A C   1 
ATOM   1243 O O   . ASN A 1 172 ? 20.845  -48.367 9.176   1.00 50.67 ?  184 ASN A O   1 
ATOM   1244 C CB  . ASN A 1 172 ? 18.429  -46.338 8.167   1.00 38.77 ?  184 ASN A CB  1 
ATOM   1245 C CG  . ASN A 1 172 ? 17.775  -45.092 8.683   1.00 45.00 ?  184 ASN A CG  1 
ATOM   1246 O OD1 . ASN A 1 172 ? 18.328  -44.413 9.547   1.00 47.13 ?  184 ASN A OD1 1 
ATOM   1247 N ND2 . ASN A 1 172 ? 16.600  -44.762 8.147   1.00 44.02 ?  184 ASN A ND2 1 
ATOM   1248 N N   . PHE A 1 173 ? 20.640  -48.179 6.937   1.00 50.40 ?  185 PHE A N   1 
ATOM   1249 C CA  . PHE A 1 173 ? 20.982  -49.574 6.680   1.00 49.42 ?  185 PHE A CA  1 
ATOM   1250 C C   . PHE A 1 173 ? 22.427  -49.879 7.070   1.00 49.95 ?  185 PHE A C   1 
ATOM   1251 O O   . PHE A 1 173 ? 22.699  -50.906 7.701   1.00 52.94 ?  185 PHE A O   1 
ATOM   1252 C CB  . PHE A 1 173 ? 20.708  -49.895 5.203   1.00 48.17 ?  185 PHE A CB  1 
ATOM   1253 C CG  . PHE A 1 173 ? 21.269  -51.220 4.720   1.00 50.01 ?  185 PHE A CG  1 
ATOM   1254 C CD1 . PHE A 1 173 ? 20.654  -52.427 5.055   1.00 45.28 ?  185 PHE A CD1 1 
ATOM   1255 C CD2 . PHE A 1 173 ? 22.393  -51.252 3.890   1.00 46.11 ?  185 PHE A CD2 1 
ATOM   1256 C CE1 . PHE A 1 173 ? 21.171  -53.636 4.587   1.00 44.83 ?  185 PHE A CE1 1 
ATOM   1257 C CE2 . PHE A 1 173 ? 22.911  -52.459 3.418   1.00 46.41 ?  185 PHE A CE2 1 
ATOM   1258 C CZ  . PHE A 1 173 ? 22.300  -53.652 3.767   1.00 45.77 ?  185 PHE A CZ  1 
ATOM   1259 N N   . LYS A 1 174 ? 23.377  -49.014 6.699   1.00 48.34 ?  186 LYS A N   1 
ATOM   1260 C CA  . LYS A 1 174 ? 24.780  -49.245 7.041   1.00 51.49 ?  186 LYS A CA  1 
ATOM   1261 C C   . LYS A 1 174 ? 25.213  -48.471 8.281   1.00 48.44 ?  186 LYS A C   1 
ATOM   1262 O O   . LYS A 1 174 ? 26.414  -48.279 8.495   1.00 50.17 ?  186 LYS A O   1 
ATOM   1263 C CB  . LYS A 1 174 ? 25.702  -48.902 5.869   1.00 45.82 ?  186 LYS A CB  1 
ATOM   1264 C CG  . LYS A 1 174 ? 25.920  -50.047 4.883   1.00 49.07 ?  186 LYS A CG  1 
ATOM   1265 C CD  . LYS A 1 174 ? 26.280  -51.337 5.591   1.00 57.35 ?  186 LYS A CD  1 
ATOM   1266 C CE  . LYS A 1 174 ? 27.748  -51.394 5.986   1.00 55.05 ?  186 LYS A CE  1 
ATOM   1267 N NZ  . LYS A 1 174 ? 27.989  -52.543 6.917   1.00 60.70 ?  186 LYS A NZ  1 
ATOM   1268 N N   . ASN A 1 175 ? 24.255  -48.035 9.095   1.00 50.75 ?  187 ASN A N   1 
ATOM   1269 C CA  . ASN A 1 175 ? 24.475  -47.247 10.302  1.00 59.04 ?  187 ASN A CA  1 
ATOM   1270 C C   . ASN A 1 175 ? 25.636  -46.278 10.168  1.00 59.83 ?  187 ASN A C   1 
ATOM   1271 O O   . ASN A 1 175 ? 26.658  -46.418 10.847  1.00 63.08 ?  187 ASN A O   1 
ATOM   1272 C CB  . ASN A 1 175 ? 24.677  -48.166 11.498  1.00 61.84 ?  187 ASN A CB  1 
ATOM   1273 C CG  . ASN A 1 175 ? 23.425  -48.288 12.315  1.00 69.89 ?  187 ASN A CG  1 
ATOM   1274 O OD1 . ASN A 1 175 ? 22.861  -49.377 12.452  1.00 77.77 ?  187 ASN A OD1 1 
ATOM   1275 N ND2 . ASN A 1 175 ? 22.956  -47.154 12.851  1.00 66.48 ?  187 ASN A ND2 1 
ATOM   1276 N N   . LEU A 1 176 ? 25.484  -45.319 9.282   1.00 56.95 ?  188 LEU A N   1 
ATOM   1277 C CA  . LEU A 1 176 ? 26.488  -44.323 8.965   1.00 52.87 ?  188 LEU A CA  1 
ATOM   1278 C C   . LEU A 1 176 ? 26.262  -43.088 9.825   1.00 47.52 ?  188 LEU A C   1 
ATOM   1279 O O   . LEU A 1 176 ? 25.150  -42.859 10.314  1.00 42.63 ?  188 LEU A O   1 
ATOM   1280 C CB  . LEU A 1 176 ? 26.423  -43.978 7.471   1.00 49.53 ?  188 LEU A CB  1 
ATOM   1281 C CG  . LEU A 1 176 ? 26.801  -45.101 6.496   1.00 48.09 ?  188 LEU A CG  1 
ATOM   1282 C CD1 . LEU A 1 176 ? 26.211  -44.867 5.102   1.00 44.55 ?  188 LEU A CD1 1 
ATOM   1283 C CD2 . LEU A 1 176 ? 28.316  -45.285 6.414   1.00 47.13 ?  188 LEU A CD2 1 
ATOM   1284 N N   . PRO A 1 177 ? 27.303  -42.279 10.045  1.00 48.12 ?  189 PRO A N   1 
ATOM   1285 C CA  . PRO A 1 177 ? 27.153  -41.107 10.924  1.00 45.68 ?  189 PRO A CA  1 
ATOM   1286 C C   . PRO A 1 177 ? 26.122  -40.142 10.368  1.00 43.50 ?  189 PRO A C   1 
ATOM   1287 O O   . PRO A 1 177 ? 26.100  -39.865 9.171   1.00 50.11 ?  189 PRO A O   1 
ATOM   1288 C CB  . PRO A 1 177 ? 28.553  -40.484 10.934  1.00 42.42 ?  189 PRO A CB  1 
ATOM   1289 C CG  . PRO A 1 177 ? 29.476  -41.542 10.413  1.00 39.18 ?  189 PRO A CG  1 
ATOM   1290 C CD  . PRO A 1 177 ? 28.659  -42.381 9.478   1.00 43.59 ?  189 PRO A CD  1 
ATOM   1291 N N   . GLU A 1 178 ? 25.267  -39.629 11.254  1.00 43.35 ?  190 GLU A N   1 
ATOM   1292 C CA  . GLU A 1 178 ? 24.139  -38.800 10.836  1.00 42.69 ?  190 GLU A CA  1 
ATOM   1293 C C   . GLU A 1 178 ? 24.569  -37.582 10.017  1.00 50.99 ?  190 GLU A C   1 
ATOM   1294 O O   . GLU A 1 178 ? 23.735  -36.963 9.345   1.00 48.44 ?  190 GLU A O   1 
ATOM   1295 C CB  . GLU A 1 178 ? 23.352  -38.361 12.074  1.00 45.86 ?  190 GLU A CB  1 
ATOM   1296 C CG  . GLU A 1 178 ? 21.984  -37.671 11.857  1.00 50.26 ?  190 GLU A CG  1 
ATOM   1297 C CD  . GLU A 1 178 ? 20.989  -38.421 10.959  1.00 61.39 ?  190 GLU A CD  1 
ATOM   1298 O OE1 . GLU A 1 178 ? 21.363  -39.006 9.909   1.00 57.71 ?  190 GLU A OE1 1 
ATOM   1299 O OE2 . GLU A 1 178 ? 19.793  -38.421 11.329  1.00 64.49 ?  190 GLU A OE2 1 
ATOM   1300 N N   . ASP A 1 179 ? 25.853  -37.242 10.037  1.00 48.89 ?  191 ASP A N   1 
ATOM   1301 C CA  . ASP A 1 179 ? 26.383  -36.051 9.389   1.00 49.56 ?  191 ASP A CA  1 
ATOM   1302 C C   . ASP A 1 179 ? 27.346  -36.405 8.263   1.00 46.34 ?  191 ASP A C   1 
ATOM   1303 O O   . ASP A 1 179 ? 28.188  -35.583 7.884   1.00 46.31 ?  191 ASP A O   1 
ATOM   1304 C CB  . ASP A 1 179 ? 27.100  -35.191 10.424  1.00 56.51 ?  191 ASP A CB  1 
ATOM   1305 C CG  . ASP A 1 179 ? 28.219  -35.959 11.107  1.00 59.75 ?  191 ASP A CG  1 
ATOM   1306 O OD1 . ASP A 1 179 ? 27.930  -37.025 11.708  1.00 64.54 ?  191 ASP A OD1 1 
ATOM   1307 O OD2 . ASP A 1 179 ? 29.389  -35.527 11.004  1.00 61.18 ?  191 ASP A OD2 1 
ATOM   1308 N N   . ILE A 1 180 ? 27.288  -37.646 7.780   1.00 45.52 ?  192 ILE A N   1 
ATOM   1309 C CA  . ILE A 1 180 ? 28.073  -38.036 6.623   1.00 43.94 ?  192 ILE A CA  1 
ATOM   1310 C C   . ILE A 1 180 ? 27.793  -37.061 5.485   1.00 41.12 ?  192 ILE A C   1 
ATOM   1311 O O   . ILE A 1 180 ? 26.648  -36.665 5.244   1.00 36.32 ?  192 ILE A O   1 
ATOM   1312 C CB  . ILE A 1 180 ? 27.740  -39.491 6.241   1.00 45.97 ?  192 ILE A CB  1 
ATOM   1313 C CG1 . ILE A 1 180 ? 28.702  -40.017 5.179   1.00 40.23 ?  192 ILE A CG1 1 
ATOM   1314 C CG2 . ILE A 1 180 ? 26.273  -39.626 5.793   1.00 38.10 ?  192 ILE A CG2 1 
ATOM   1315 C CD1 . ILE A 1 180 ? 28.584  -41.507 4.960   1.00 43.76 ?  192 ILE A CD1 1 
ATOM   1316 N N   . GLY A 1 181 ? 28.856  -36.623 4.817   1.00 38.30 ?  193 GLY A N   1 
ATOM   1317 C CA  . GLY A 1 181 ? 28.697  -35.704 3.707   1.00 41.38 ?  193 GLY A CA  1 
ATOM   1318 C C   . GLY A 1 181 ? 28.234  -36.443 2.467   1.00 44.31 ?  193 GLY A C   1 
ATOM   1319 O O   . GLY A 1 181 ? 28.819  -37.464 2.082   1.00 39.27 ?  193 GLY A O   1 
ATOM   1320 N N   . VAL A 1 182 ? 27.190  -35.909 1.826   1.00 39.79 ?  194 VAL A N   1 
ATOM   1321 C CA  . VAL A 1 182 ? 26.599  -36.473 0.614   1.00 38.47 ?  194 VAL A CA  1 
ATOM   1322 C C   . VAL A 1 182 ? 26.986  -35.635 -0.599  1.00 37.29 ?  194 VAL A C   1 
ATOM   1323 O O   . VAL A 1 182 ? 27.039  -34.400 -0.521  1.00 41.13 ?  194 VAL A O   1 
ATOM   1324 C CB  . VAL A 1 182 ? 25.069  -36.541 0.766   1.00 39.35 ?  194 VAL A CB  1 
ATOM   1325 C CG1 . VAL A 1 182 ? 24.454  -37.362 -0.347  1.00 38.32 ?  194 VAL A CG1 1 
ATOM   1326 C CG2 . VAL A 1 182 ? 24.722  -37.109 2.141   1.00 40.55 ?  194 VAL A CG2 1 
ATOM   1327 N N   . GLY A 1 183 ? 27.246  -36.309 -1.715  1.00 38.86 ?  195 GLY A N   1 
ATOM   1328 C CA  . GLY A 1 183 ? 27.422  -35.640 -2.999  1.00 35.00 ?  195 GLY A CA  1 
ATOM   1329 C C   . GLY A 1 183 ? 26.575  -36.278 -4.082  1.00 37.41 ?  195 GLY A C   1 
ATOM   1330 O O   . GLY A 1 183 ? 26.383  -37.491 -4.098  1.00 39.26 ?  195 GLY A O   1 
ATOM   1331 N N   . PHE A 1 184 ? 26.066  -35.444 -4.995  1.00 34.15 ?  196 PHE A N   1 
ATOM   1332 C CA  . PHE A 1 184 ? 25.121  -35.862 -6.030  1.00 32.52 ?  196 PHE A CA  1 
ATOM   1333 C C   . PHE A 1 184 ? 25.735  -35.720 -7.420  1.00 33.71 ?  196 PHE A C   1 
ATOM   1334 O O   . PHE A 1 184 ? 26.432  -34.737 -7.706  1.00 34.15 ?  196 PHE A O   1 
ATOM   1335 C CB  . PHE A 1 184 ? 23.831  -35.032 -6.005  1.00 30.50 ?  196 PHE A CB  1 
ATOM   1336 C CG  . PHE A 1 184 ? 23.040  -35.109 -4.722  1.00 30.22 ?  196 PHE A CG  1 
ATOM   1337 C CD1 . PHE A 1 184 ? 23.479  -34.492 -3.565  1.00 30.94 ?  196 PHE A CD1 1 
ATOM   1338 C CD2 . PHE A 1 184 ? 21.809  -35.755 -4.693  1.00 34.44 ?  196 PHE A CD2 1 
ATOM   1339 C CE1 . PHE A 1 184 ? 22.715  -34.544 -2.396  1.00 30.96 ?  196 PHE A CE1 1 
ATOM   1340 C CE2 . PHE A 1 184 ? 21.050  -35.819 -3.533  1.00 27.88 ?  196 PHE A CE2 1 
ATOM   1341 C CZ  . PHE A 1 184 ? 21.500  -35.212 -2.390  1.00 31.36 ?  196 PHE A CZ  1 
ATOM   1342 N N   . TYR A 1 185 ? 25.461  -36.698 -8.286  1.00 32.05 ?  197 TYR A N   1 
ATOM   1343 C CA  . TYR A 1 185 ? 25.758  -36.621 -9.714  1.00 30.18 ?  197 TYR A CA  1 
ATOM   1344 C C   . TYR A 1 185 ? 24.540  -37.061 -10.514 1.00 33.48 ?  197 TYR A C   1 
ATOM   1345 O O   . TYR A 1 185 ? 23.809  -37.968 -10.100 1.00 36.17 ?  197 TYR A O   1 
ATOM   1346 C CB  . TYR A 1 185 ? 26.942  -37.486 -10.102 1.00 27.50 ?  197 TYR A CB  1 
ATOM   1347 C CG  . TYR A 1 185 ? 27.414  -37.307 -11.535 1.00 31.38 ?  197 TYR A CG  1 
ATOM   1348 C CD1 . TYR A 1 185 ? 26.747  -37.919 -12.609 1.00 33.12 ?  197 TYR A CD1 1 
ATOM   1349 C CD2 . TYR A 1 185 ? 28.534  -36.543 -11.822 1.00 32.32 ?  197 TYR A CD2 1 
ATOM   1350 C CE1 . TYR A 1 185 ? 27.179  -37.756 -13.927 1.00 30.85 ?  197 TYR A CE1 1 
ATOM   1351 C CE2 . TYR A 1 185 ? 28.983  -36.381 -13.135 1.00 31.31 ?  197 TYR A CE2 1 
ATOM   1352 C CZ  . TYR A 1 185 ? 28.303  -36.990 -14.182 1.00 33.76 ?  197 TYR A CZ  1 
ATOM   1353 O OH  . TYR A 1 185 ? 28.748  -36.825 -15.476 1.00 34.42 ?  197 TYR A OH  1 
ATOM   1354 N N   . GLY A 1 186 ? 24.322  -36.409 -11.655 1.00 33.69 ?  198 GLY A N   1 
ATOM   1355 C CA  . GLY A 1 186 ? 23.300  -36.816 -12.603 1.00 32.55 ?  198 GLY A CA  1 
ATOM   1356 C C   . GLY A 1 186 ? 23.352  -36.027 -13.902 1.00 33.09 ?  198 GLY A C   1 
ATOM   1357 O O   . GLY A 1 186 ? 23.659  -34.828 -13.892 1.00 29.59 ?  198 GLY A O   1 
ATOM   1358 N N   . TYR A 1 187 ? 23.067  -36.685 -15.026 1.00 29.47 ?  199 TYR A N   1 
ATOM   1359 C CA  . TYR A 1 187 ? 22.929  -36.017 -16.314 1.00 29.77 ?  199 TYR A CA  1 
ATOM   1360 C C   . TYR A 1 187 ? 21.547  -36.280 -16.903 1.00 30.18 ?  199 TYR A C   1 
ATOM   1361 O O   . TYR A 1 187 ? 20.930  -37.327 -16.658 1.00 28.06 ?  199 TYR A O   1 
ATOM   1362 C CB  . TYR A 1 187 ? 24.002  -36.474 -17.317 1.00 27.30 ?  199 TYR A CB  1 
ATOM   1363 C CG  . TYR A 1 187 ? 24.065  -35.596 -18.543 1.00 28.63 ?  199 TYR A CG  1 
ATOM   1364 C CD1 . TYR A 1 187 ? 24.716  -34.363 -18.508 1.00 29.28 ?  199 TYR A CD1 1 
ATOM   1365 C CD2 . TYR A 1 187 ? 23.466  -35.989 -19.739 1.00 26.13 ?  199 TYR A CD2 1 
ATOM   1366 C CE1 . TYR A 1 187 ? 24.769  -33.547 -19.640 1.00 29.03 ?  199 TYR A CE1 1 
ATOM   1367 C CE2 . TYR A 1 187 ? 23.506  -35.178 -20.874 1.00 27.41 ?  199 TYR A CE2 1 
ATOM   1368 C CZ  . TYR A 1 187 ? 24.164  -33.961 -20.815 1.00 31.13 ?  199 TYR A CZ  1 
ATOM   1369 O OH  . TYR A 1 187 ? 24.209  -33.152 -21.920 1.00 31.92 ?  199 TYR A OH  1 
ATOM   1370 N N   . ALA A 1 188 ? 21.072  -35.317 -17.691 1.00 28.54 ?  200 ALA A N   1 
ATOM   1371 C CA  . ALA A 1 188 ? 19.862  -35.465 -18.514 1.00 28.17 ?  200 ALA A CA  1 
ATOM   1372 C C   . ALA A 1 188 ? 18.694  -35.756 -17.573 1.00 28.32 ?  200 ALA A C   1 
ATOM   1373 O O   . ALA A 1 188 ? 18.479  -34.984 -16.624 1.00 24.83 ?  200 ALA A O   1 
ATOM   1374 C CB  . ALA A 1 188 ? 20.109  -36.509 -19.608 1.00 26.04 ?  200 ALA A CB  1 
ATOM   1375 N N   . GLY A 1 189 ? 17.910  -36.818 -17.798 1.00 25.24 ?  201 GLY A N   1 
ATOM   1376 C CA  . GLY A 1 189 ? 16.859  -37.158 -16.855 1.00 23.55 ?  201 GLY A CA  1 
ATOM   1377 C C   . GLY A 1 189 ? 17.389  -37.390 -15.459 1.00 25.11 ?  201 GLY A C   1 
ATOM   1378 O O   . GLY A 1 189 ? 16.689  -37.120 -14.481 1.00 26.03 ?  201 GLY A O   1 
ATOM   1379 N N   . GLY A 1 190 ? 18.637  -37.873 -15.344 1.00 22.77 ?  202 GLY A N   1 
ATOM   1380 C CA  . GLY A 1 190 ? 19.279  -37.931 -14.039 1.00 24.88 ?  202 GLY A CA  1 
ATOM   1381 C C   . GLY A 1 190 ? 19.518  -36.550 -13.446 1.00 29.62 ?  202 GLY A C   1 
ATOM   1382 O O   . GLY A 1 190 ? 19.412  -36.354 -12.232 1.00 30.60 ?  202 GLY A O   1 
ATOM   1383 N N   . ALA A 1 191 ? 19.804  -35.562 -14.296 1.00 27.80 ?  203 ALA A N   1 
ATOM   1384 C CA  . ALA A 1 191 ? 19.992  -34.204 -13.790 1.00 27.18 ?  203 ALA A CA  1 
ATOM   1385 C C   . ALA A 1 191 ? 18.686  -33.596 -13.282 1.00 27.23 ?  203 ALA A C   1 
ATOM   1386 O O   . ALA A 1 191 ? 18.698  -32.852 -12.297 1.00 27.78 ?  203 ALA A O   1 
ATOM   1387 C CB  . ALA A 1 191 ? 20.612  -33.328 -14.869 1.00 27.65 ?  203 ALA A CB  1 
ATOM   1388 N N   . HIS A 1 192 ? 17.548  -33.905 -13.922 1.00 28.27 ?  204 HIS A N   1 
ATOM   1389 C CA  . HIS A 1 192 ? 16.270  -33.400 -13.420 1.00 27.25 ?  204 HIS A CA  1 
ATOM   1390 C C   . HIS A 1 192 ? 15.994  -33.921 -12.010 1.00 30.65 ?  204 HIS A C   1 
ATOM   1391 O O   . HIS A 1 192 ? 15.621  -33.153 -11.115 1.00 26.53 ?  204 HIS A O   1 
ATOM   1392 C CB  . HIS A 1 192 ? 15.106  -33.776 -14.359 1.00 26.48 ?  204 HIS A CB  1 
ATOM   1393 C CG  . HIS A 1 192 ? 13.754  -33.341 -13.850 1.00 25.10 ?  204 HIS A CG  1 
ATOM   1394 N ND1 . HIS A 1 192 ? 12.992  -34.107 -12.994 1.00 31.56 ?  204 HIS A ND1 1 
ATOM   1395 C CD2 . HIS A 1 192 ? 13.049  -32.200 -14.047 1.00 25.94 ?  204 HIS A CD2 1 
ATOM   1396 C CE1 . HIS A 1 192 ? 11.873  -33.467 -12.696 1.00 30.62 ?  204 HIS A CE1 1 
ATOM   1397 N NE2 . HIS A 1 192 ? 11.891  -32.299 -13.312 1.00 29.45 ?  204 HIS A NE2 1 
ATOM   1398 N N   . ALA A 1 193 ? 16.140  -35.236 -11.807 1.00 28.98 ?  205 ALA A N   1 
ATOM   1399 C CA  . ALA A 1 193 ? 15.923  -35.810 -10.484 1.00 31.78 ?  205 ALA A CA  1 
ATOM   1400 C C   . ALA A 1 193 ? 16.928  -35.265 -9.471  1.00 29.65 ?  205 ALA A C   1 
ATOM   1401 O O   . ALA A 1 193 ? 16.560  -34.938 -8.337  1.00 28.10 ?  205 ALA A O   1 
ATOM   1402 C CB  . ALA A 1 193 ? 16.007  -37.335 -10.554 1.00 25.35 ?  205 ALA A CB  1 
ATOM   1403 N N   . THR A 1 194 ? 18.205  -35.176 -9.863  1.00 28.58 ?  206 THR A N   1 
ATOM   1404 C CA  . THR A 1 194 ? 19.204  -34.532 -9.014  1.00 31.32 ?  206 THR A CA  1 
ATOM   1405 C C   . THR A 1 194 ? 18.791  -33.108 -8.653  1.00 30.57 ?  206 THR A C   1 
ATOM   1406 O O   . THR A 1 194 ? 18.792  -32.729 -7.476  1.00 29.83 ?  206 THR A O   1 
ATOM   1407 C CB  . THR A 1 194 ? 20.553  -34.522 -9.718  1.00 30.88 ?  206 THR A CB  1 
ATOM   1408 O OG1 . THR A 1 194 ? 20.996  -35.869 -9.896  1.00 32.43 ?  206 THR A OG1 1 
ATOM   1409 C CG2 . THR A 1 194 ? 21.578  -33.750 -8.868  1.00 35.06 ?  206 THR A CG2 1 
ATOM   1410 N N   . ALA A 1 195 ? 18.426  -32.307 -9.657  1.00 28.20 ?  207 ALA A N   1 
ATOM   1411 C CA  . ALA A 1 195 ? 18.085  -30.909 -9.402  1.00 28.44 ?  207 ALA A CA  1 
ATOM   1412 C C   . ALA A 1 195 ? 16.962  -30.793 -8.387  1.00 29.74 ?  207 ALA A C   1 
ATOM   1413 O O   . ALA A 1 195 ? 16.967  -29.884 -7.547  1.00 30.40 ?  207 ALA A O   1 
ATOM   1414 C CB  . ALA A 1 195 ? 17.680  -30.205 -10.698 1.00 22.99 ?  207 ALA A CB  1 
ATOM   1415 N N   . TRP A 1 196 ? 15.981  -31.696 -8.455  1.00 26.52 ?  208 TRP A N   1 
ATOM   1416 C CA  . TRP A 1 196 ? 14.861  -31.622 -7.530  1.00 28.96 ?  208 TRP A CA  1 
ATOM   1417 C C   . TRP A 1 196 ? 15.232  -32.145 -6.149  1.00 30.58 ?  208 TRP A C   1 
ATOM   1418 O O   . TRP A 1 196 ? 14.726  -31.628 -5.152  1.00 34.51 ?  208 TRP A O   1 
ATOM   1419 C CB  . TRP A 1 196 ? 13.654  -32.382 -8.083  1.00 30.29 ?  208 TRP A CB  1 
ATOM   1420 C CG  . TRP A 1 196 ? 12.837  -31.512 -8.959  1.00 32.26 ?  208 TRP A CG  1 
ATOM   1421 C CD1 . TRP A 1 196 ? 12.970  -31.363 -10.305 1.00 27.08 ?  208 TRP A CD1 1 
ATOM   1422 C CD2 . TRP A 1 196 ? 11.781  -30.624 -8.552  1.00 28.57 ?  208 TRP A CD2 1 
ATOM   1423 N NE1 . TRP A 1 196 ? 12.057  -30.446 -10.765 1.00 30.48 ?  208 TRP A NE1 1 
ATOM   1424 C CE2 . TRP A 1 196 ? 11.312  -29.979 -9.718  1.00 28.11 ?  208 TRP A CE2 1 
ATOM   1425 C CE3 . TRP A 1 196 ? 11.188  -30.318 -7.318  1.00 27.63 ?  208 TRP A CE3 1 
ATOM   1426 C CZ2 . TRP A 1 196 ? 10.278  -29.037 -9.697  1.00 30.15 ?  208 TRP A CZ2 1 
ATOM   1427 C CZ3 . TRP A 1 196 ? 10.158  -29.391 -7.287  1.00 31.03 ?  208 TRP A CZ3 1 
ATOM   1428 C CH2 . TRP A 1 196 ? 9.708   -28.755 -8.476  1.00 32.49 ?  208 TRP A CH2 1 
ATOM   1429 N N   . ALA A 1 197 ? 16.098  -33.158 -6.071  1.00 25.18 ?  209 ALA A N   1 
ATOM   1430 C CA  . ALA A 1 197 ? 16.534  -33.644 -4.769  1.00 32.73 ?  209 ALA A CA  1 
ATOM   1431 C C   . ALA A 1 197 ? 17.240  -32.538 -3.976  1.00 36.14 ?  209 ALA A C   1 
ATOM   1432 O O   . ALA A 1 197 ? 16.927  -32.316 -2.800  1.00 31.47 ?  209 ALA A O   1 
ATOM   1433 C CB  . ALA A 1 197 ? 17.439  -34.865 -4.935  1.00 26.23 ?  209 ALA A CB  1 
ATOM   1434 N N   . VAL A 1 198 ? 18.193  -31.828 -4.601  1.00 30.79 ?  210 VAL A N   1 
ATOM   1435 C CA  . VAL A 1 198 ? 18.918  -30.804 -3.848  1.00 31.70 ?  210 VAL A CA  1 
ATOM   1436 C C   . VAL A 1 198 ? 18.002  -29.627 -3.555  1.00 33.49 ?  210 VAL A C   1 
ATOM   1437 O O   . VAL A 1 198 ? 18.130  -28.976 -2.514  1.00 36.47 ?  210 VAL A O   1 
ATOM   1438 C CB  . VAL A 1 198 ? 20.203  -30.329 -4.563  1.00 31.31 ?  210 VAL A CB  1 
ATOM   1439 C CG1 . VAL A 1 198 ? 21.190  -31.454 -4.767  1.00 34.26 ?  210 VAL A CG1 1 
ATOM   1440 C CG2 . VAL A 1 198 ? 19.903  -29.645 -5.858  1.00 30.25 ?  210 VAL A CG2 1 
ATOM   1441 N N   . SER A 1 199 ? 17.054  -29.346 -4.448  1.00 33.34 ?  211 SER A N   1 
ATOM   1442 C CA  . SER A 1 199 ? 16.110  -28.266 -4.201  1.00 29.93 ?  211 SER A CA  1 
ATOM   1443 C C   . SER A 1 199 ? 15.282  -28.556 -2.958  1.00 37.27 ?  211 SER A C   1 
ATOM   1444 O O   . SER A 1 199 ? 15.059  -27.666 -2.123  1.00 34.64 ?  211 SER A O   1 
ATOM   1445 C CB  . SER A 1 199 ? 15.218  -28.071 -5.427  1.00 26.91 ?  211 SER A CB  1 
ATOM   1446 O OG  . SER A 1 199 ? 14.365  -26.944 -5.307  1.00 32.45 ?  211 SER A OG  1 
ATOM   1447 N N   . LEU A 1 200 ? 14.850  -29.811 -2.797  1.00 35.66 ?  212 LEU A N   1 
ATOM   1448 C CA  . LEU A 1 200 ? 13.957  -30.171 -1.698  1.00 41.71 ?  212 LEU A CA  1 
ATOM   1449 C C   . LEU A 1 200 ? 14.697  -30.497 -0.402  1.00 36.77 ?  212 LEU A C   1 
ATOM   1450 O O   . LEU A 1 200 ? 14.051  -30.606 0.647   1.00 37.42 ?  212 LEU A O   1 
ATOM   1451 C CB  . LEU A 1 200 ? 13.087  -31.360 -2.112  1.00 29.93 ?  212 LEU A CB  1 
ATOM   1452 C CG  . LEU A 1 200 ? 12.113  -31.004 -3.231  1.00 36.23 ?  212 LEU A CG  1 
ATOM   1453 C CD1 . LEU A 1 200 ? 11.286  -32.235 -3.619  1.00 31.71 ?  212 LEU A CD1 1 
ATOM   1454 C CD2 . LEU A 1 200 ? 11.214  -29.807 -2.847  1.00 28.27 ?  212 LEU A CD2 1 
ATOM   1455 N N   . ALA A 1 201 ? 16.026  -30.613 -0.456  1.00 32.88 ?  213 ALA A N   1 
ATOM   1456 C CA  . ALA A 1 201 ? 16.799  -31.190 0.640   1.00 37.57 ?  213 ALA A CA  1 
ATOM   1457 C C   . ALA A 1 201 ? 16.580  -30.431 1.951   1.00 40.81 ?  213 ALA A C   1 
ATOM   1458 O O   . ALA A 1 201 ? 16.191  -31.017 2.964   1.00 37.96 ?  213 ALA A O   1 
ATOM   1459 C CB  . ALA A 1 201 ? 18.279  -31.214 0.248   1.00 34.16 ?  213 ALA A CB  1 
ATOM   1460 N N   . GLU A 1 202 ? 16.817  -29.116 1.943   1.00 38.36 ?  214 GLU A N   1 
ATOM   1461 C CA  . GLU A 1 202 ? 16.650  -28.305 3.146   1.00 43.74 ?  214 GLU A CA  1 
ATOM   1462 C C   . GLU A 1 202 ? 15.274  -28.490 3.770   1.00 41.09 ?  214 GLU A C   1 
ATOM   1463 O O   . GLU A 1 202 ? 15.147  -28.709 4.982   1.00 35.24 ?  214 GLU A O   1 
ATOM   1464 C CB  . GLU A 1 202 ? 16.872  -26.822 2.816   1.00 48.19 ?  214 GLU A CB  1 
ATOM   1465 C CG  . GLU A 1 202 ? 17.086  -25.916 4.041   1.00 46.54 ?  214 GLU A CG  1 
ATOM   1466 C CD  . GLU A 1 202 ? 17.616  -26.682 5.239   1.00 56.15 ?  214 GLU A CD  1 
ATOM   1467 O OE1 . GLU A 1 202 ? 16.969  -26.634 6.317   1.00 66.86 ?  214 GLU A OE1 1 
ATOM   1468 O OE2 . GLU A 1 202 ? 18.696  -27.315 5.116   1.00 61.52 ?  214 GLU A OE2 1 
ATOM   1469 N N   . GLY A 1 203 ? 14.228  -28.376 2.953   1.00 37.30 ?  215 GLY A N   1 
ATOM   1470 C CA  . GLY A 1 203 ? 12.876  -28.408 3.478   1.00 34.20 ?  215 GLY A CA  1 
ATOM   1471 C C   . GLY A 1 203 ? 12.426  -29.784 3.918   1.00 40.66 ?  215 GLY A C   1 
ATOM   1472 O O   . GLY A 1 203 ? 11.607  -29.905 4.830   1.00 44.19 ?  215 GLY A O   1 
ATOM   1473 N N   . TYR A 1 204 ? 12.953  -30.835 3.298   1.00 39.09 ?  216 TYR A N   1 
ATOM   1474 C CA  . TYR A 1 204 ? 12.443  -32.186 3.497   1.00 38.65 ?  216 TYR A CA  1 
ATOM   1475 C C   . TYR A 1 204 ? 13.403  -33.075 4.263   1.00 36.56 ?  216 TYR A C   1 
ATOM   1476 O O   . TYR A 1 204 ? 12.965  -33.898 5.060   1.00 37.34 ?  216 TYR A O   1 
ATOM   1477 C CB  . TYR A 1 204 ? 12.120  -32.828 2.135   1.00 36.87 ?  216 TYR A CB  1 
ATOM   1478 C CG  . TYR A 1 204 ? 11.521  -34.229 2.173   1.00 35.42 ?  216 TYR A CG  1 
ATOM   1479 C CD1 . TYR A 1 204 ? 10.143  -34.422 2.340   1.00 30.76 ?  216 TYR A CD1 1 
ATOM   1480 C CD2 . TYR A 1 204 ? 12.327  -35.356 2.003   1.00 36.79 ?  216 TYR A CD2 1 
ATOM   1481 C CE1 . TYR A 1 204 ? 9.591   -35.698 2.360   1.00 32.04 ?  216 TYR A CE1 1 
ATOM   1482 C CE2 . TYR A 1 204 ? 11.786  -36.646 2.015   1.00 35.36 ?  216 TYR A CE2 1 
ATOM   1483 C CZ  . TYR A 1 204 ? 10.414  -36.808 2.200   1.00 37.40 ?  216 TYR A CZ  1 
ATOM   1484 O OH  . TYR A 1 204 ? 9.870   -38.076 2.215   1.00 34.77 ?  216 TYR A OH  1 
ATOM   1485 N N   . ALA A 1 205 ? 14.702  -32.940 4.029   1.00 37.33 ?  217 ALA A N   1 
ATOM   1486 C CA  . ALA A 1 205 ? 15.720  -33.734 4.714   1.00 36.33 ?  217 ALA A CA  1 
ATOM   1487 C C   . ALA A 1 205 ? 16.830  -32.824 5.230   1.00 42.78 ?  217 ALA A C   1 
ATOM   1488 O O   . ALA A 1 205 ? 17.986  -32.933 4.805   1.00 41.17 ?  217 ALA A O   1 
ATOM   1489 C CB  . ALA A 1 205 ? 16.278  -34.807 3.786   1.00 34.51 ?  217 ALA A CB  1 
ATOM   1490 N N   . PRO A 1 206 ? 16.507  -31.909 6.159   1.00 43.96 ?  218 PRO A N   1 
ATOM   1491 C CA  . PRO A 1 206 ? 17.541  -30.997 6.690   1.00 41.19 ?  218 PRO A CA  1 
ATOM   1492 C C   . PRO A 1 206 ? 18.693  -31.705 7.361   1.00 38.43 ?  218 PRO A C   1 
ATOM   1493 O O   . PRO A 1 206 ? 19.770  -31.113 7.497   1.00 38.84 ?  218 PRO A O   1 
ATOM   1494 C CB  . PRO A 1 206 ? 16.775  -30.130 7.697   1.00 41.93 ?  218 PRO A CB  1 
ATOM   1495 C CG  . PRO A 1 206 ? 15.549  -30.950 8.061   1.00 44.21 ?  218 PRO A CG  1 
ATOM   1496 C CD  . PRO A 1 206 ? 15.199  -31.721 6.818   1.00 36.07 ?  218 PRO A CD  1 
ATOM   1497 N N   . GLU A 1 207 ? 18.512  -32.951 7.788   1.00 39.06 ?  219 GLU A N   1 
ATOM   1498 C CA  . GLU A 1 207 ? 19.588  -33.654 8.468   1.00 39.82 ?  219 GLU A CA  1 
ATOM   1499 C C   . GLU A 1 207 ? 20.606  -34.246 7.506   1.00 37.74 ?  219 GLU A C   1 
ATOM   1500 O O   . GLU A 1 207 ? 21.600  -34.823 7.957   1.00 42.25 ?  219 GLU A O   1 
ATOM   1501 C CB  . GLU A 1 207 ? 19.014  -34.743 9.377   1.00 36.44 ?  219 GLU A CB  1 
ATOM   1502 C CG  . GLU A 1 207 ? 18.831  -36.091 8.706   1.00 42.17 ?  219 GLU A CG  1 
ATOM   1503 C CD  . GLU A 1 207 ? 17.622  -36.124 7.774   1.00 38.11 ?  219 GLU A CD  1 
ATOM   1504 O OE1 . GLU A 1 207 ? 16.785  -35.190 7.820   1.00 36.21 ?  219 GLU A OE1 1 
ATOM   1505 O OE2 . GLU A 1 207 ? 17.518  -37.097 6.994   1.00 38.88 ?  219 GLU A OE2 1 
ATOM   1506 N N   . ILE A 1 208 ? 20.408  -34.104 6.205   1.00 36.43 ?  220 ILE A N   1 
ATOM   1507 C CA  . ILE A 1 208 ? 21.375  -34.600 5.233   1.00 38.28 ?  220 ILE A CA  1 
ATOM   1508 C C   . ILE A 1 208 ? 22.412  -33.516 4.978   1.00 33.37 ?  220 ILE A C   1 
ATOM   1509 O O   . ILE A 1 208 ? 22.062  -32.390 4.612   1.00 38.60 ?  220 ILE A O   1 
ATOM   1510 C CB  . ILE A 1 208 ? 20.679  -35.019 3.925   1.00 33.09 ?  220 ILE A CB  1 
ATOM   1511 C CG1 . ILE A 1 208 ? 19.586  -36.043 4.221   1.00 37.63 ?  220 ILE A CG1 1 
ATOM   1512 C CG2 . ILE A 1 208 ? 21.693  -35.595 2.960   1.00 30.58 ?  220 ILE A CG2 1 
ATOM   1513 C CD1 . ILE A 1 208 ? 19.039  -36.739 2.991   1.00 33.08 ?  220 ILE A CD1 1 
ATOM   1514 N N   . LYS A 1 209 ? 23.686  -33.860 5.137   1.00 35.90 ?  221 LYS A N   1 
ATOM   1515 C CA  . LYS A 1 209 ? 24.789  -32.913 4.964   1.00 39.59 ?  221 LYS A CA  1 
ATOM   1516 C C   . LYS A 1 209 ? 25.337  -33.041 3.549   1.00 42.24 ?  221 LYS A C   1 
ATOM   1517 O O   . LYS A 1 209 ? 25.958  -34.056 3.200   1.00 40.70 ?  221 LYS A O   1 
ATOM   1518 C CB  . LYS A 1 209 ? 25.896  -33.166 5.988   1.00 42.77 ?  221 LYS A CB  1 
ATOM   1519 C CG  . LYS A 1 209 ? 25.438  -33.087 7.438   1.00 43.72 ?  221 LYS A CG  1 
ATOM   1520 C CD  . LYS A 1 209 ? 24.880  -31.706 7.771   1.00 47.29 ?  221 LYS A CD  1 
ATOM   1521 C CE  . LYS A 1 209 ? 24.971  -31.418 9.272   1.00 49.47 ?  221 LYS A CE  1 
ATOM   1522 N NZ  . LYS A 1 209 ? 25.343  -30.002 9.530   1.00 54.60 ?  221 LYS A NZ  1 
ATOM   1523 N N   . ILE A 1 210 ? 25.145  -32.004 2.744   1.00 38.50 ?  222 ILE A N   1 
ATOM   1524 C CA  . ILE A 1 210 ? 25.494  -32.053 1.331   1.00 39.58 ?  222 ILE A CA  1 
ATOM   1525 C C   . ILE A 1 210 ? 26.789  -31.276 1.107   1.00 35.63 ?  222 ILE A C   1 
ATOM   1526 O O   . ILE A 1 210 ? 26.820  -30.050 1.248   1.00 37.29 ?  222 ILE A O   1 
ATOM   1527 C CB  . ILE A 1 210 ? 24.356  -31.507 0.458   1.00 35.63 ?  222 ILE A CB  1 
ATOM   1528 C CG1 . ILE A 1 210 ? 23.073  -32.317 0.710   1.00 35.63 ?  222 ILE A CG1 1 
ATOM   1529 C CG2 . ILE A 1 210 ? 24.791  -31.520 -1.014  1.00 32.48 ?  222 ILE A CG2 1 
ATOM   1530 C CD1 . ILE A 1 210 ? 21.816  -31.760 0.054   1.00 34.25 ?  222 ILE A CD1 1 
ATOM   1531 N N   . ASP A 1 211 ? 27.845  -31.984 0.697   1.00 34.31 ?  223 ASP A N   1 
ATOM   1532 C CA  . ASP A 1 211 ? 29.095  -31.329 0.327   1.00 31.79 ?  223 ASP A CA  1 
ATOM   1533 C C   . ASP A 1 211 ? 29.072  -30.740 -1.088  1.00 37.04 ?  223 ASP A C   1 
ATOM   1534 O O   . ASP A 1 211 ? 29.840  -29.807 -1.368  1.00 35.04 ?  223 ASP A O   1 
ATOM   1535 C CB  . ASP A 1 211 ? 30.267  -32.309 0.412   1.00 36.23 ?  223 ASP A CB  1 
ATOM   1536 C CG  . ASP A 1 211 ? 30.538  -32.812 1.827   1.00 37.60 ?  223 ASP A CG  1 
ATOM   1537 O OD1 . ASP A 1 211 ? 30.027  -32.223 2.802   1.00 37.86 ?  223 ASP A OD1 1 
ATOM   1538 O OD2 . ASP A 1 211 ? 31.263  -33.830 1.946   1.00 38.18 ?  223 ASP A OD2 1 
ATOM   1539 N N   . GLY A 1 212 ? 28.264  -31.281 -2.003  1.00 35.25 ?  224 GLY A N   1 
ATOM   1540 C CA  . GLY A 1 212 ? 28.322  -30.825 -3.391  1.00 32.58 ?  224 GLY A CA  1 
ATOM   1541 C C   . GLY A 1 212 ? 27.367  -31.582 -4.294  1.00 39.29 ?  224 GLY A C   1 
ATOM   1542 O O   . GLY A 1 212 ? 26.828  -32.637 -3.940  1.00 38.66 ?  224 GLY A O   1 
ATOM   1543 N N   . ALA A 1 213 ? 27.164  -31.018 -5.481  1.00 35.42 ?  225 ALA A N   1 
ATOM   1544 C CA  . ALA A 1 213 ? 26.334  -31.631 -6.505  1.00 32.59 ?  225 ALA A CA  1 
ATOM   1545 C C   . ALA A 1 213 ? 26.840  -31.175 -7.860  1.00 33.84 ?  225 ALA A C   1 
ATOM   1546 O O   . ALA A 1 213 ? 27.150  -29.995 -8.054  1.00 33.38 ?  225 ALA A O   1 
ATOM   1547 C CB  . ALA A 1 213 ? 24.853  -31.267 -6.352  1.00 29.35 ?  225 ALA A CB  1 
ATOM   1548 N N   . ALA A 1 214 ? 26.926  -32.122 -8.786  1.00 29.66 ?  226 ALA A N   1 
ATOM   1549 C CA  . ALA A 1 214 ? 27.315  -31.860 -10.162 1.00 29.30 ?  226 ALA A CA  1 
ATOM   1550 C C   . ALA A 1 214 ? 26.216  -32.411 -11.059 1.00 31.91 ?  226 ALA A C   1 
ATOM   1551 O O   . ALA A 1 214 ? 25.875  -33.595 -10.953 1.00 32.40 ?  226 ALA A O   1 
ATOM   1552 C CB  . ALA A 1 214 ? 28.664  -32.512 -10.481 1.00 28.84 ?  226 ALA A CB  1 
ATOM   1553 N N   . TYR A 1 215 ? 25.630  -31.562 -11.907 1.00 27.15 ?  227 TYR A N   1 
ATOM   1554 C CA  . TYR A 1 215 ? 24.595  -32.060 -12.805 1.00 28.46 ?  227 TYR A CA  1 
ATOM   1555 C C   . TYR A 1 215 ? 24.541  -31.238 -14.088 1.00 33.07 ?  227 TYR A C   1 
ATOM   1556 O O   . TYR A 1 215 ? 24.864  -30.043 -14.100 1.00 29.98 ?  227 TYR A O   1 
ATOM   1557 C CB  . TYR A 1 215 ? 23.209  -32.126 -12.133 1.00 24.32 ?  227 TYR A CB  1 
ATOM   1558 C CG  . TYR A 1 215 ? 22.729  -30.977 -11.259 1.00 28.80 ?  227 TYR A CG  1 
ATOM   1559 C CD1 . TYR A 1 215 ? 23.298  -30.722 -10.005 1.00 31.17 ?  227 TYR A CD1 1 
ATOM   1560 C CD2 . TYR A 1 215 ? 21.638  -30.192 -11.648 1.00 29.94 ?  227 TYR A CD2 1 
ATOM   1561 C CE1 . TYR A 1 215 ? 22.824  -29.699 -9.191  1.00 24.59 ?  227 TYR A CE1 1 
ATOM   1562 C CE2 . TYR A 1 215 ? 21.164  -29.155 -10.836 1.00 25.45 ?  227 TYR A CE2 1 
ATOM   1563 C CZ  . TYR A 1 215 ? 21.762  -28.919 -9.614  1.00 28.42 ?  227 TYR A CZ  1 
ATOM   1564 O OH  . TYR A 1 215 ? 21.284  -27.916 -8.795  1.00 26.26 ?  227 TYR A OH  1 
ATOM   1565 N N   . GLY A 1 216 ? 24.156  -31.904 -15.182 1.00 29.24 ?  228 GLY A N   1 
ATOM   1566 C CA  . GLY A 1 216 ? 24.160  -31.270 -16.489 1.00 28.73 ?  228 GLY A CA  1 
ATOM   1567 C C   . GLY A 1 216 ? 23.039  -31.758 -17.384 1.00 28.04 ?  228 GLY A C   1 
ATOM   1568 O O   . GLY A 1 216 ? 22.429  -32.798 -17.135 1.00 32.60 ?  228 GLY A O   1 
ATOM   1569 N N   . GLY A 1 217 ? 22.804  -31.011 -18.460 1.00 29.41 ?  229 GLY A N   1 
ATOM   1570 C CA  . GLY A 1 217 ? 21.654  -31.255 -19.329 1.00 30.52 ?  229 GLY A CA  1 
ATOM   1571 C C   . GLY A 1 217 ? 20.334  -31.143 -18.595 1.00 30.85 ?  229 GLY A C   1 
ATOM   1572 O O   . GLY A 1 217 ? 19.395  -31.906 -18.868 1.00 33.53 ?  229 GLY A O   1 
ATOM   1573 N N   . THR A 1 218 ? 20.237  -30.193 -17.686 1.00 27.30 ?  230 THR A N   1 
ATOM   1574 C CA  . THR A 1 218 ? 19.166  -30.174 -16.702 1.00 28.32 ?  230 THR A CA  1 
ATOM   1575 C C   . THR A 1 218 ? 17.851  -29.710 -17.307 1.00 30.81 ?  230 THR A C   1 
ATOM   1576 O O   . THR A 1 218 ? 17.776  -28.582 -17.808 1.00 27.50 ?  230 THR A O   1 
ATOM   1577 C CB  . THR A 1 218 ? 19.526  -29.250 -15.561 1.00 26.80 ?  230 THR A CB  1 
ATOM   1578 O OG1 . THR A 1 218 ? 20.851  -29.562 -15.121 1.00 30.19 ?  230 THR A OG1 1 
ATOM   1579 C CG2 . THR A 1 218 ? 18.519  -29.399 -14.421 1.00 26.91 ?  230 THR A CG2 1 
ATOM   1580 N N   . PRO A 1 219 ? 16.784  -30.521 -17.245 1.00 31.70 ?  231 PRO A N   1 
ATOM   1581 C CA  . PRO A 1 219 ? 15.447  -29.991 -17.533 1.00 29.25 ?  231 PRO A CA  1 
ATOM   1582 C C   . PRO A 1 219 ? 14.949  -29.159 -16.360 1.00 33.58 ?  231 PRO A C   1 
ATOM   1583 O O   . PRO A 1 219 ? 14.467  -29.720 -15.370 1.00 28.99 ?  231 PRO A O   1 
ATOM   1584 C CB  . PRO A 1 219 ? 14.602  -31.255 -17.748 1.00 28.64 ?  231 PRO A CB  1 
ATOM   1585 C CG  . PRO A 1 219 ? 15.596  -32.369 -17.966 1.00 26.36 ?  231 PRO A CG  1 
ATOM   1586 C CD  . PRO A 1 219 ? 16.781  -31.988 -17.128 1.00 29.30 ?  231 PRO A CD  1 
ATOM   1587 N N   . ALA A 1 220 ? 15.063  -27.828 -16.451 1.00 30.12 ?  232 ALA A N   1 
ATOM   1588 C CA  . ALA A 1 220 ? 14.650  -26.977 -15.338 1.00 31.73 ?  232 ALA A CA  1 
ATOM   1589 C C   . ALA A 1 220 ? 13.135  -26.848 -15.250 1.00 33.55 ?  232 ALA A C   1 
ATOM   1590 O O   . ALA A 1 220 ? 12.573  -26.884 -14.148 1.00 30.78 ?  232 ALA A O   1 
ATOM   1591 C CB  . ALA A 1 220 ? 15.280  -25.585 -15.458 1.00 30.25 ?  232 ALA A CB  1 
ATOM   1592 N N   . SER A 1 221 ? 12.462  -26.676 -16.387 1.00 29.94 ?  233 SER A N   1 
ATOM   1593 C CA  . SER A 1 221 ? 11.021  -26.468 -16.429 1.00 30.68 ?  233 SER A CA  1 
ATOM   1594 C C   . SER A 1 221 ? 10.372  -27.606 -17.203 1.00 31.09 ?  233 SER A C   1 
ATOM   1595 O O   . SER A 1 221 ? 10.765  -27.896 -18.335 1.00 28.97 ?  233 SER A O   1 
ATOM   1596 C CB  . SER A 1 221 ? 10.680  -25.110 -17.064 1.00 35.98 ?  233 SER A CB  1 
ATOM   1597 O OG  . SER A 1 221 ? 9.371   -25.083 -17.630 1.00 36.19 ?  233 SER A OG  1 
ATOM   1598 N N   . ALA A 1 222 ? 9.392   -28.260 -16.580 1.00 32.08 ?  234 ALA A N   1 
ATOM   1599 C CA  . ALA A 1 222 ? 8.641   -29.287 -17.285 1.00 29.57 ?  234 ALA A CA  1 
ATOM   1600 C C   . ALA A 1 222 ? 7.946   -28.703 -18.500 1.00 31.07 ?  234 ALA A C   1 
ATOM   1601 O O   . ALA A 1 222 ? 7.976   -29.291 -19.587 1.00 34.00 ?  234 ALA A O   1 
ATOM   1602 C CB  . ALA A 1 222 ? 7.620   -29.937 -16.352 1.00 29.82 ?  234 ALA A CB  1 
ATOM   1603 N N   . LYS A 1 223 ? 7.327   -27.535 -18.339 1.00 32.65 ?  235 LYS A N   1 
ATOM   1604 C CA  . LYS A 1 223 ? 6.588   -26.934 -19.439 1.00 33.69 ?  235 LYS A CA  1 
ATOM   1605 C C   . LYS A 1 223 ? 7.519   -26.591 -20.609 1.00 38.03 ?  235 LYS A C   1 
ATOM   1606 O O   . LYS A 1 223 ? 7.265   -26.981 -21.755 1.00 34.96 ?  235 LYS A O   1 
ATOM   1607 C CB  . LYS A 1 223 ? 5.841   -25.701 -18.931 1.00 35.21 ?  235 LYS A CB  1 
ATOM   1608 C CG  . LYS A 1 223 ? 4.794   -25.149 -19.880 1.00 38.84 ?  235 LYS A CG  1 
ATOM   1609 C CD  . LYS A 1 223 ? 4.634   -23.661 -19.676 1.00 42.96 ?  235 LYS A CD  1 
ATOM   1610 C CE  . LYS A 1 223 ? 3.398   -23.135 -20.367 1.00 46.51 ?  235 LYS A CE  1 
ATOM   1611 N NZ  . LYS A 1 223 ? 3.381   -21.647 -20.260 1.00 54.38 ?  235 LYS A NZ  1 
ATOM   1612 N N   . ASP A 1 224 ? 8.622   -25.884 -20.335 1.00 33.62 ?  236 ASP A N   1 
ATOM   1613 C CA  . ASP A 1 224 ? 9.499   -25.473 -21.425 1.00 33.47 ?  236 ASP A CA  1 
ATOM   1614 C C   . ASP A 1 224 ? 10.139  -26.667 -22.103 1.00 34.07 ?  236 ASP A C   1 
ATOM   1615 O O   . ASP A 1 224 ? 10.438  -26.613 -23.304 1.00 33.60 ?  236 ASP A O   1 
ATOM   1616 C CB  . ASP A 1 224 ? 10.600  -24.532 -20.926 1.00 34.23 ?  236 ASP A CB  1 
ATOM   1617 C CG  . ASP A 1 224 ? 10.057  -23.266 -20.298 1.00 36.87 ?  236 ASP A CG  1 
ATOM   1618 O OD1 . ASP A 1 224 ? 8.919   -22.847 -20.602 1.00 41.20 ?  236 ASP A OD1 1 
ATOM   1619 O OD2 . ASP A 1 224 ? 10.786  -22.690 -19.483 1.00 34.14 ?  236 ASP A OD2 1 
ATOM   1620 N N   . THR A 1 225 ? 10.395  -27.744 -21.358 1.00 32.02 ?  237 THR A N   1 
ATOM   1621 C CA  . THR A 1 225 ? 10.984  -28.902 -22.015 1.00 34.64 ?  237 THR A CA  1 
ATOM   1622 C C   . THR A 1 225 ? 9.968   -29.569 -22.928 1.00 32.63 ?  237 THR A C   1 
ATOM   1623 O O   . THR A 1 225 ? 10.320  -30.046 -24.015 1.00 36.62 ?  237 THR A O   1 
ATOM   1624 C CB  . THR A 1 225 ? 11.537  -29.890 -20.995 1.00 31.93 ?  237 THR A CB  1 
ATOM   1625 O OG1 . THR A 1 225 ? 12.360  -29.190 -20.069 1.00 32.02 ?  237 THR A OG1 1 
ATOM   1626 C CG2 . THR A 1 225 ? 12.388  -30.934 -21.691 1.00 31.74 ?  237 THR A CG2 1 
ATOM   1627 N N   . PHE A 1 226 ? 8.697   -29.576 -22.523 1.00 37.00 ?  238 PHE A N   1 
ATOM   1628 C CA  . PHE A 1 226 ? 7.660   -30.130 -23.387 1.00 36.29 ?  238 PHE A CA  1 
ATOM   1629 C C   . PHE A 1 226 ? 7.576   -29.354 -24.697 1.00 34.45 ?  238 PHE A C   1 
ATOM   1630 O O   . PHE A 1 226 ? 7.587   -29.950 -25.784 1.00 37.89 ?  238 PHE A O   1 
ATOM   1631 C CB  . PHE A 1 226 ? 6.300   -30.134 -22.679 1.00 34.12 ?  238 PHE A CB  1 
ATOM   1632 C CG  . PHE A 1 226 ? 5.156   -30.388 -23.612 1.00 34.57 ?  238 PHE A CG  1 
ATOM   1633 C CD1 . PHE A 1 226 ? 4.796   -31.695 -23.944 1.00 35.52 ?  238 PHE A CD1 1 
ATOM   1634 C CD2 . PHE A 1 226 ? 4.467   -29.325 -24.203 1.00 29.51 ?  238 PHE A CD2 1 
ATOM   1635 C CE1 . PHE A 1 226 ? 3.744   -31.946 -24.818 1.00 34.91 ?  238 PHE A CE1 1 
ATOM   1636 C CE2 . PHE A 1 226 ? 3.423   -29.557 -25.093 1.00 34.73 ?  238 PHE A CE2 1 
ATOM   1637 C CZ  . PHE A 1 226 ? 3.056   -30.873 -25.400 1.00 39.94 ?  238 PHE A CZ  1 
ATOM   1638 N N   . THR A 1 227 ? 7.473   -28.020 -24.611 1.00 33.74 ?  239 THR A N   1 
ATOM   1639 C CA  . THR A 1 227 ? 7.349   -27.197 -25.817 1.00 36.87 ?  239 THR A CA  1 
ATOM   1640 C C   . THR A 1 227 ? 8.557   -27.364 -26.728 1.00 36.22 ?  239 THR A C   1 
ATOM   1641 O O   . THR A 1 227 ? 8.420   -27.410 -27.954 1.00 40.25 ?  239 THR A O   1 
ATOM   1642 C CB  . THR A 1 227 ? 7.194   -25.723 -25.438 1.00 41.51 ?  239 THR A CB  1 
ATOM   1643 O OG1 . THR A 1 227 ? 6.397   -25.617 -24.259 1.00 39.68 ?  239 THR A OG1 1 
ATOM   1644 C CG2 . THR A 1 227 ? 6.554   -24.920 -26.579 1.00 36.08 ?  239 THR A CG2 1 
ATOM   1645 N N   . PHE A 1 228 ? 9.750   -27.446 -26.133 1.00 33.17 ?  240 PHE A N   1 
ATOM   1646 C CA  . PHE A 1 228 ? 10.983  -27.604 -26.888 1.00 32.82 ?  240 PHE A CA  1 
ATOM   1647 C C   . PHE A 1 228 ? 11.018  -28.921 -27.632 1.00 31.56 ?  240 PHE A C   1 
ATOM   1648 O O   . PHE A 1 228 ? 11.654  -29.025 -28.683 1.00 32.42 ?  240 PHE A O   1 
ATOM   1649 C CB  . PHE A 1 228 ? 12.165  -27.521 -25.920 1.00 33.06 ?  240 PHE A CB  1 
ATOM   1650 C CG  . PHE A 1 228 ? 13.505  -27.386 -26.584 1.00 32.68 ?  240 PHE A CG  1 
ATOM   1651 C CD1 . PHE A 1 228 ? 13.834  -26.226 -27.283 1.00 28.95 ?  240 PHE A CD1 1 
ATOM   1652 C CD2 . PHE A 1 228 ? 14.462  -28.395 -26.456 1.00 29.98 ?  240 PHE A CD2 1 
ATOM   1653 C CE1 . PHE A 1 228 ? 15.082  -26.091 -27.878 1.00 30.24 ?  240 PHE A CE1 1 
ATOM   1654 C CE2 . PHE A 1 228 ? 15.717  -28.267 -27.037 1.00 29.96 ?  240 PHE A CE2 1 
ATOM   1655 C CZ  . PHE A 1 228 ? 16.027  -27.115 -27.760 1.00 28.42 ?  240 PHE A CZ  1 
ATOM   1656 N N   . LEU A 1 229 ? 10.369  -29.944 -27.084 1.00 37.97 ?  241 LEU A N   1 
ATOM   1657 C CA  . LEU A 1 229 ? 10.456  -31.306 -27.597 1.00 34.52 ?  241 LEU A CA  1 
ATOM   1658 C C   . LEU A 1 229 ? 9.327   -31.667 -28.546 1.00 37.31 ?  241 LEU A C   1 
ATOM   1659 O O   . LEU A 1 229 ? 9.538   -32.484 -29.454 1.00 36.24 ?  241 LEU A O   1 
ATOM   1660 C CB  . LEU A 1 229 ? 10.440  -32.298 -26.438 1.00 33.02 ?  241 LEU A CB  1 
ATOM   1661 C CG  . LEU A 1 229 ? 11.758  -32.491 -25.714 1.00 35.22 ?  241 LEU A CG  1 
ATOM   1662 C CD1 . LEU A 1 229 ? 11.506  -33.335 -24.471 1.00 35.12 ?  241 LEU A CD1 1 
ATOM   1663 C CD2 . LEU A 1 229 ? 12.747  -33.156 -26.648 1.00 31.45 ?  241 LEU A CD2 1 
ATOM   1664 N N   . ASN A 1 230 ? 8.145   -31.073 -28.346 1.00 33.07 ?  242 ASN A N   1 
ATOM   1665 C CA  . ASN A 1 230 ? 6.938   -31.470 -29.068 1.00 35.58 ?  242 ASN A CA  1 
ATOM   1666 C C   . ASN A 1 230 ? 7.080   -31.197 -30.565 1.00 31.53 ?  242 ASN A C   1 
ATOM   1667 O O   . ASN A 1 230 ? 7.508   -30.114 -30.972 1.00 36.49 ?  242 ASN A O   1 
ATOM   1668 C CB  . ASN A 1 230 ? 5.741   -30.709 -28.488 1.00 38.43 ?  242 ASN A CB  1 
ATOM   1669 C CG  . ASN A 1 230 ? 4.411   -31.263 -28.941 1.00 39.02 ?  242 ASN A CG  1 
ATOM   1670 O OD1 . ASN A 1 230 ? 4.258   -32.475 -29.131 1.00 35.68 ?  242 ASN A OD1 1 
ATOM   1671 N ND2 . ASN A 1 230 ? 3.429   -30.376 -29.105 1.00 31.86 ?  242 ASN A ND2 1 
ATOM   1672 N N   . LYS A 1 231 ? 6.744   -32.193 -31.379 1.00 34.28 ?  243 LYS A N   1 
ATOM   1673 C CA  . LYS A 1 231 ? 6.771   -32.199 -32.849 1.00 35.20 ?  243 LYS A CA  1 
ATOM   1674 C C   . LYS A 1 231 ? 8.177   -32.411 -33.376 1.00 36.27 ?  243 LYS A C   1 
ATOM   1675 O O   . LYS A 1 231 ? 8.349   -32.477 -34.595 1.00 33.09 ?  243 LYS A O   1 
ATOM   1676 C CB  . LYS A 1 231 ? 6.206   -30.921 -33.496 1.00 35.18 ?  243 LYS A CB  1 
ATOM   1677 C CG  . LYS A 1 231 ? 4.818   -30.512 -33.005 1.00 41.76 ?  243 LYS A CG  1 
ATOM   1678 C CD  . LYS A 1 231 ? 4.698   -29.004 -32.877 1.00 46.97 ?  243 LYS A CD  1 
ATOM   1679 C CE  . LYS A 1 231 ? 4.069   -28.421 -34.118 1.00 51.74 ?  243 LYS A CE  1 
ATOM   1680 N NZ  . LYS A 1 231 ? 2.764   -29.090 -34.325 1.00 53.38 ?  243 LYS A NZ  1 
ATOM   1681 N N   . GLY A 1 232 ? 9.193   -32.491 -32.510 1.00 35.59 ?  244 GLY A N   1 
ATOM   1682 C CA  . GLY A 1 232 ? 10.541  -32.778 -32.946 1.00 29.77 ?  244 GLY A CA  1 
ATOM   1683 C C   . GLY A 1 232 ? 10.829  -34.275 -32.930 1.00 34.38 ?  244 GLY A C   1 
ATOM   1684 O O   . GLY A 1 232 ? 10.021  -35.096 -32.492 1.00 32.20 ?  244 GLY A O   1 
ATOM   1685 N N   . PHE A 1 233 ? 12.024  -34.617 -33.423 1.00 33.22 ?  245 PHE A N   1 
ATOM   1686 C CA  . PHE A 1 233 ? 12.434  -36.013 -33.492 1.00 28.89 ?  245 PHE A CA  1 
ATOM   1687 C C   . PHE A 1 233 ? 12.294  -36.701 -32.147 1.00 32.94 ?  245 PHE A C   1 
ATOM   1688 O O   . PHE A 1 233 ? 11.884  -37.865 -32.077 1.00 33.97 ?  245 PHE A O   1 
ATOM   1689 C CB  . PHE A 1 233 ? 13.871  -36.103 -33.966 1.00 30.93 ?  245 PHE A CB  1 
ATOM   1690 C CG  . PHE A 1 233 ? 14.391  -37.503 -34.050 1.00 33.23 ?  245 PHE A CG  1 
ATOM   1691 C CD1 . PHE A 1 233 ? 14.145  -38.284 -35.181 1.00 33.97 ?  245 PHE A CD1 1 
ATOM   1692 C CD2 . PHE A 1 233 ? 15.159  -38.032 -33.025 1.00 31.78 ?  245 PHE A CD2 1 
ATOM   1693 C CE1 . PHE A 1 233 ? 14.647  -39.583 -35.274 1.00 35.90 ?  245 PHE A CE1 1 
ATOM   1694 C CE2 . PHE A 1 233 ? 15.664  -39.334 -33.100 1.00 33.90 ?  245 PHE A CE2 1 
ATOM   1695 C CZ  . PHE A 1 233 ? 15.410  -40.110 -34.231 1.00 36.89 ?  245 PHE A CZ  1 
ATOM   1696 N N   . PHE A 1 234 ? 12.621  -35.997 -31.063 1.00 33.12 ?  246 PHE A N   1 
ATOM   1697 C CA  . PHE A 1 234 ? 12.576  -36.577 -29.728 1.00 29.27 ?  246 PHE A CA  1 
ATOM   1698 C C   . PHE A 1 234 ? 11.251  -36.294 -29.010 1.00 30.97 ?  246 PHE A C   1 
ATOM   1699 O O   . PHE A 1 234 ? 11.197  -36.346 -27.775 1.00 30.21 ?  246 PHE A O   1 
ATOM   1700 C CB  . PHE A 1 234 ? 13.769  -36.078 -28.905 1.00 33.18 ?  246 PHE A CB  1 
ATOM   1701 C CG  . PHE A 1 234 ? 15.117  -36.610 -29.376 1.00 29.63 ?  246 PHE A CG  1 
ATOM   1702 C CD1 . PHE A 1 234 ? 15.550  -37.877 -29.006 1.00 26.36 ?  246 PHE A CD1 1 
ATOM   1703 C CD2 . PHE A 1 234 ? 15.953  -35.824 -30.163 1.00 29.34 ?  246 PHE A CD2 1 
ATOM   1704 C CE1 . PHE A 1 234 ? 16.782  -38.366 -29.435 1.00 28.53 ?  246 PHE A CE1 1 
ATOM   1705 C CE2 . PHE A 1 234 ? 17.192  -36.296 -30.594 1.00 28.72 ?  246 PHE A CE2 1 
ATOM   1706 C CZ  . PHE A 1 234 ? 17.608  -37.570 -30.240 1.00 25.56 ?  246 PHE A CZ  1 
ATOM   1707 N N   . ALA A 1 235 ? 10.181  -36.017 -29.764 1.00 28.68 ?  247 ALA A N   1 
ATOM   1708 C CA  . ALA A 1 235 ? 8.852   -35.848 -29.185 1.00 30.26 ?  247 ALA A CA  1 
ATOM   1709 C C   . ALA A 1 235 ? 8.444   -37.021 -28.296 1.00 29.00 ?  247 ALA A C   1 
ATOM   1710 O O   . ALA A 1 235 ? 7.619   -36.851 -27.393 1.00 30.29 ?  247 ALA A O   1 
ATOM   1711 C CB  . ALA A 1 235 ? 7.820   -35.649 -30.310 1.00 31.42 ?  247 ALA A CB  1 
ATOM   1712 N N   . GLY A 1 236 ? 9.010   -38.214 -28.525 1.00 27.35 ?  248 GLY A N   1 
ATOM   1713 C CA  . GLY A 1 236 ? 8.698   -39.350 -27.671 1.00 27.73 ?  248 GLY A CA  1 
ATOM   1714 C C   . GLY A 1 236 ? 8.965   -39.101 -26.195 1.00 31.81 ?  248 GLY A C   1 
ATOM   1715 O O   . GLY A 1 236 ? 8.316   -39.700 -25.334 1.00 33.30 ?  248 GLY A O   1 
ATOM   1716 N N   . PHE A 1 237 ? 9.925   -38.223 -25.886 1.00 33.99 ?  249 PHE A N   1 
ATOM   1717 C CA  . PHE A 1 237 ? 10.176  -37.814 -24.508 1.00 28.55 ?  249 PHE A CA  1 
ATOM   1718 C C   . PHE A 1 237 ? 9.040   -36.951 -23.981 1.00 32.21 ?  249 PHE A C   1 
ATOM   1719 O O   . PHE A 1 237 ? 8.685   -37.031 -22.797 1.00 33.21 ?  249 PHE A O   1 
ATOM   1720 C CB  . PHE A 1 237 ? 11.496  -37.036 -24.433 1.00 28.09 ?  249 PHE A CB  1 
ATOM   1721 C CG  . PHE A 1 237 ? 12.720  -37.898 -24.361 1.00 31.45 ?  249 PHE A CG  1 
ATOM   1722 C CD1 . PHE A 1 237 ? 12.837  -38.889 -23.389 1.00 30.84 ?  249 PHE A CD1 1 
ATOM   1723 C CD2 . PHE A 1 237 ? 13.764  -37.714 -25.252 1.00 29.20 ?  249 PHE A CD2 1 
ATOM   1724 C CE1 . PHE A 1 237 ? 13.982  -39.684 -23.312 1.00 30.43 ?  249 PHE A CE1 1 
ATOM   1725 C CE2 . PHE A 1 237 ? 14.902  -38.513 -25.181 1.00 34.58 ?  249 PHE A CE2 1 
ATOM   1726 C CZ  . PHE A 1 237 ? 15.014  -39.496 -24.202 1.00 29.98 ?  249 PHE A CZ  1 
ATOM   1727 N N   . ALA A 1 238 ? 8.495   -36.079 -24.836 1.00 29.95 ?  250 ALA A N   1 
ATOM   1728 C CA  . ALA A 1 238 ? 7.323   -35.297 -24.449 1.00 32.77 ?  250 ALA A CA  1 
ATOM   1729 C C   . ALA A 1 238 ? 6.151   -36.208 -24.087 1.00 33.07 ?  250 ALA A C   1 
ATOM   1730 O O   . ALA A 1 238 ? 5.446   -35.958 -23.103 1.00 31.94 ?  250 ALA A O   1 
ATOM   1731 C CB  . ALA A 1 238 ? 6.927   -34.330 -25.577 1.00 28.04 ?  250 ALA A CB  1 
ATOM   1732 N N   . VAL A 1 239 ? 5.918   -37.263 -24.879 1.00 31.48 ?  251 VAL A N   1 
ATOM   1733 C CA  . VAL A 1 239 ? 4.917   -38.263 -24.500 1.00 33.49 ?  251 VAL A CA  1 
ATOM   1734 C C   . VAL A 1 239 ? 5.276   -38.869 -23.155 1.00 32.28 ?  251 VAL A C   1 
ATOM   1735 O O   . VAL A 1 239 ? 4.436   -38.972 -22.253 1.00 32.82 ?  251 VAL A O   1 
ATOM   1736 C CB  . VAL A 1 239 ? 4.791   -39.369 -25.571 1.00 32.00 ?  251 VAL A CB  1 
ATOM   1737 C CG1 . VAL A 1 239 ? 3.685   -40.334 -25.173 1.00 32.09 ?  251 VAL A CG1 1 
ATOM   1738 C CG2 . VAL A 1 239 ? 4.523   -38.797 -26.936 1.00 31.51 ?  251 VAL A CG2 1 
ATOM   1739 N N   . ALA A 1 240 ? 6.534   -39.295 -23.009 1.00 32.34 ?  252 ALA A N   1 
ATOM   1740 C CA  . ALA A 1 240 ? 6.977   -39.909 -21.759 1.00 32.53 ?  252 ALA A CA  1 
ATOM   1741 C C   . ALA A 1 240 ? 6.768   -38.973 -20.573 1.00 34.08 ?  252 ALA A C   1 
ATOM   1742 O O   . ALA A 1 240 ? 6.246   -39.388 -19.529 1.00 31.81 ?  252 ALA A O   1 
ATOM   1743 C CB  . ALA A 1 240 ? 8.439   -40.334 -21.876 1.00 26.90 ?  252 ALA A CB  1 
ATOM   1744 N N   . GLY A 1 241 ? 7.120   -37.696 -20.734 1.00 34.98 ?  253 GLY A N   1 
ATOM   1745 C CA  . GLY A 1 241 ? 6.968   -36.756 -19.637 1.00 33.03 ?  253 GLY A CA  1 
ATOM   1746 C C   . GLY A 1 241 ? 5.520   -36.492 -19.284 1.00 36.09 ?  253 GLY A C   1 
ATOM   1747 O O   . GLY A 1 241 ? 5.181   -36.300 -18.105 1.00 33.62 ?  253 GLY A O   1 
ATOM   1748 N N   . VAL A 1 242 ? 4.646   -36.450 -20.294 1.00 35.95 ?  254 VAL A N   1 
ATOM   1749 C CA  . VAL A 1 242 ? 3.222   -36.306 -20.007 1.00 36.40 ?  254 VAL A CA  1 
ATOM   1750 C C   . VAL A 1 242 ? 2.744   -37.502 -19.203 1.00 33.08 ?  254 VAL A C   1 
ATOM   1751 O O   . VAL A 1 242 ? 2.024   -37.356 -18.209 1.00 33.06 ?  254 VAL A O   1 
ATOM   1752 C CB  . VAL A 1 242 ? 2.411   -36.131 -21.310 1.00 38.19 ?  254 VAL A CB  1 
ATOM   1753 C CG1 . VAL A 1 242 ? 0.901   -36.271 -21.042 1.00 30.12 ?  254 VAL A CG1 1 
ATOM   1754 C CG2 . VAL A 1 242 ? 2.703   -34.777 -21.942 1.00 38.99 ?  254 VAL A CG2 1 
ATOM   1755 N N   . SER A 1 243 ? 3.159   -38.703 -19.617 1.00 34.53 ?  255 SER A N   1 
ATOM   1756 C CA  . SER A 1 243 ? 2.794   -39.925 -18.912 1.00 31.65 ?  255 SER A CA  1 
ATOM   1757 C C   . SER A 1 243 ? 3.297   -39.894 -17.475 1.00 34.80 ?  255 SER A C   1 
ATOM   1758 O O   . SER A 1 243 ? 2.581   -40.291 -16.549 1.00 33.92 ?  255 SER A O   1 
ATOM   1759 C CB  . SER A 1 243 ? 3.364   -41.128 -19.679 1.00 33.01 ?  255 SER A CB  1 
ATOM   1760 O OG  . SER A 1 243 ? 3.296   -42.341 -18.944 1.00 32.08 ?  255 SER A OG  1 
ATOM   1761 N N   . GLY A 1 244 ? 4.521   -39.396 -17.273 1.00 34.66 ?  256 GLY A N   1 
ATOM   1762 C CA  . GLY A 1 244 ? 5.116   -39.408 -15.944 1.00 33.63 ?  256 GLY A CA  1 
ATOM   1763 C C   . GLY A 1 244 ? 4.442   -38.438 -14.994 1.00 35.44 ?  256 GLY A C   1 
ATOM   1764 O O   . GLY A 1 244 ? 4.119   -38.792 -13.856 1.00 37.39 ?  256 GLY A O   1 
ATOM   1765 N N   . LEU A 1 245 ? 4.211   -37.203 -15.443 1.00 33.30 ?  257 LEU A N   1 
ATOM   1766 C CA  . LEU A 1 245 ? 3.502   -36.261 -14.582 1.00 33.75 ?  257 LEU A CA  1 
ATOM   1767 C C   . LEU A 1 245 ? 2.113   -36.779 -14.226 1.00 38.61 ?  257 LEU A C   1 
ATOM   1768 O O   . LEU A 1 245 ? 1.681   -36.687 -13.066 1.00 36.73 ?  257 LEU A O   1 
ATOM   1769 C CB  . LEU A 1 245 ? 3.415   -34.891 -15.249 1.00 30.48 ?  257 LEU A CB  1 
ATOM   1770 C CG  . LEU A 1 245 ? 4.772   -34.175 -15.315 1.00 31.41 ?  257 LEU A CG  1 
ATOM   1771 C CD1 . LEU A 1 245 ? 4.641   -32.814 -15.963 1.00 37.21 ?  257 LEU A CD1 1 
ATOM   1772 C CD2 . LEU A 1 245 ? 5.363   -34.028 -13.952 1.00 28.65 ?  257 LEU A CD2 1 
ATOM   1773 N N   . ALA A 1 246 ? 1.402   -37.339 -15.206 1.00 37.36 ?  258 ALA A N   1 
ATOM   1774 C CA  . ALA A 1 246 ? 0.060   -37.842 -14.932 1.00 38.98 ?  258 ALA A CA  1 
ATOM   1775 C C   . ALA A 1 246 ? 0.082   -38.963 -13.896 1.00 36.96 ?  258 ALA A C   1 
ATOM   1776 O O   . ALA A 1 246 ? -0.865  -39.101 -13.123 1.00 42.70 ?  258 ALA A O   1 
ATOM   1777 C CB  . ALA A 1 246 ? -0.604  -38.318 -16.225 1.00 35.24 ?  258 ALA A CB  1 
ATOM   1778 N N   . LEU A 1 247 ? 1.146   -39.760 -13.858 1.00 31.81 ?  259 LEU A N   1 
ATOM   1779 C CA  . LEU A 1 247 ? 1.256   -40.833 -12.881 1.00 35.01 ?  259 LEU A CA  1 
ATOM   1780 C C   . LEU A 1 247 ? 1.533   -40.306 -11.474 1.00 41.21 ?  259 LEU A C   1 
ATOM   1781 O O   . LEU A 1 247 ? 1.218   -40.991 -10.490 1.00 38.71 ?  259 LEU A O   1 
ATOM   1782 C CB  . LEU A 1 247 ? 2.355   -41.813 -13.307 1.00 35.11 ?  259 LEU A CB  1 
ATOM   1783 C CG  . LEU A 1 247 ? 2.067   -42.649 -14.558 1.00 34.23 ?  259 LEU A CG  1 
ATOM   1784 C CD1 . LEU A 1 247 ? 3.302   -43.404 -15.034 1.00 33.56 ?  259 LEU A CD1 1 
ATOM   1785 C CD2 . LEU A 1 247 ? 0.945   -43.619 -14.277 1.00 33.93 ?  259 LEU A CD2 1 
ATOM   1786 N N   . ALA A 1 248 ? 2.105   -39.109 -11.355 1.00 37.78 ?  260 ALA A N   1 
ATOM   1787 C CA  . ALA A 1 248 ? 2.314   -38.477 -10.062 1.00 37.33 ?  260 ALA A CA  1 
ATOM   1788 C C   . ALA A 1 248 ? 1.274   -37.407 -9.756  1.00 39.85 ?  260 ALA A C   1 
ATOM   1789 O O   . ALA A 1 248 ? 1.323   -36.806 -8.678  1.00 38.53 ?  260 ALA A O   1 
ATOM   1790 C CB  . ALA A 1 248 ? 3.715   -37.868 -9.992  1.00 35.88 ?  260 ALA A CB  1 
ATOM   1791 N N   . HIS A 1 249 ? 0.342   -37.149 -10.675 1.00 36.39 ?  261 HIS A N   1 
ATOM   1792 C CA  . HIS A 1 249 ? -0.718  -36.163 -10.473 1.00 39.60 ?  261 HIS A CA  1 
ATOM   1793 C C   . HIS A 1 249 ? -2.033  -36.778 -10.920 1.00 41.64 ?  261 HIS A C   1 
ATOM   1794 O O   . HIS A 1 249 ? -2.454  -36.607 -12.074 1.00 40.52 ?  261 HIS A O   1 
ATOM   1795 C CB  . HIS A 1 249 ? -0.428  -34.875 -11.229 1.00 40.13 ?  261 HIS A CB  1 
ATOM   1796 C CG  . HIS A 1 249 ? 0.788   -34.161 -10.741 1.00 45.48 ?  261 HIS A CG  1 
ATOM   1797 N ND1 . HIS A 1 249 ? 0.742   -33.222 -9.732  1.00 40.83 ?  261 HIS A ND1 1 
ATOM   1798 C CD2 . HIS A 1 249 ? 2.085   -34.252 -11.119 1.00 38.44 ?  261 HIS A CD2 1 
ATOM   1799 C CE1 . HIS A 1 249 ? 1.959   -32.756 -9.519  1.00 40.25 ?  261 HIS A CE1 1 
ATOM   1800 N NE2 . HIS A 1 249 ? 2.791   -33.363 -10.348 1.00 37.83 ?  261 HIS A NE2 1 
ATOM   1801 N N   . PRO A 1 250 ? -2.694  -37.533 -10.041 1.00 44.39 ?  262 PRO A N   1 
ATOM   1802 C CA  . PRO A 1 250 ? -3.908  -38.247 -10.464 1.00 39.80 ?  262 PRO A CA  1 
ATOM   1803 C C   . PRO A 1 250 ? -5.004  -37.332 -10.966 1.00 39.17 ?  262 PRO A C   1 
ATOM   1804 O O   . PRO A 1 250 ? -5.803  -37.760 -11.807 1.00 42.95 ?  262 PRO A O   1 
ATOM   1805 C CB  . PRO A 1 250 ? -4.323  -39.005 -9.194  1.00 41.35 ?  262 PRO A CB  1 
ATOM   1806 C CG  . PRO A 1 250 ? -3.023  -39.225 -8.464  1.00 42.54 ?  262 PRO A CG  1 
ATOM   1807 C CD  . PRO A 1 250 ? -2.220  -37.974 -8.712  1.00 38.32 ?  262 PRO A CD  1 
ATOM   1808 N N   . ASP A 1 251 ? -5.070  -36.083 -10.494 1.00 36.60 ?  263 ASP A N   1 
ATOM   1809 C CA  . ASP A 1 251 ? -6.063  -35.167 -11.042 1.00 38.19 ?  263 ASP A CA  1 
ATOM   1810 C C   . ASP A 1 251 ? -5.775  -34.846 -12.504 1.00 47.49 ?  263 ASP A C   1 
ATOM   1811 O O   . ASP A 1 251 ? -6.713  -34.635 -13.287 1.00 48.55 ?  263 ASP A O   1 
ATOM   1812 C CB  . ASP A 1 251 ? -6.169  -33.888 -10.200 1.00 36.85 ?  263 ASP A CB  1 
ATOM   1813 C CG  . ASP A 1 251 ? -4.858  -33.120 -10.067 1.00 43.32 ?  263 ASP A CG  1 
ATOM   1814 O OD1 . ASP A 1 251 ? -3.779  -33.646 -10.403 1.00 46.17 ?  263 ASP A OD1 1 
ATOM   1815 O OD2 . ASP A 1 251 ? -4.914  -31.964 -9.594  1.00 46.53 ?  263 ASP A OD2 1 
ATOM   1816 N N   . MET A 1 252 ? -4.498  -34.850 -12.902 1.00 43.64 ?  264 MET A N   1 
ATOM   1817 C CA  . MET A 1 252 ? -4.168  -34.697 -14.309 1.00 41.91 ?  264 MET A CA  1 
ATOM   1818 C C   . MET A 1 252 ? -4.406  -35.996 -15.071 1.00 40.52 ?  264 MET A C   1 
ATOM   1819 O O   . MET A 1 252 ? -4.846  -35.968 -16.225 1.00 40.52 ?  264 MET A O   1 
ATOM   1820 C CB  . MET A 1 252 ? -2.724  -34.187 -14.452 1.00 42.59 ?  264 MET A CB  1 
ATOM   1821 C CG  . MET A 1 252 ? -1.950  -34.621 -15.715 1.00 43.94 ?  264 MET A CG  1 
ATOM   1822 S SD  . MET A 1 252 ? -0.261  -33.933 -15.774 1.00 43.57 ?  264 MET A SD  1 
ATOM   1823 C CE  . MET A 1 252 ? 0.046   -33.850 -17.536 1.00 39.41 ?  264 MET A CE  1 
ATOM   1824 N N   . GLU A 1 253 ? -4.164  -37.147 -14.448 1.00 42.03 ?  265 GLU A N   1 
ATOM   1825 C CA  . GLU A 1 253 ? -4.592  -38.391 -15.085 1.00 43.53 ?  265 GLU A CA  1 
ATOM   1826 C C   . GLU A 1 253 ? -6.104  -38.398 -15.320 1.00 45.36 ?  265 GLU A C   1 
ATOM   1827 O O   . GLU A 1 253 ? -6.568  -38.755 -16.406 1.00 42.19 ?  265 GLU A O   1 
ATOM   1828 C CB  . GLU A 1 253 ? -4.174  -39.591 -14.243 1.00 40.86 ?  265 GLU A CB  1 
ATOM   1829 C CG  . GLU A 1 253 ? -4.564  -40.914 -14.883 1.00 44.10 ?  265 GLU A CG  1 
ATOM   1830 C CD  . GLU A 1 253 ? -3.569  -41.382 -15.934 1.00 43.93 ?  265 GLU A CD  1 
ATOM   1831 O OE1 . GLU A 1 253 ? -2.474  -40.797 -16.045 1.00 46.86 ?  265 GLU A OE1 1 
ATOM   1832 O OE2 . GLU A 1 253 ? -3.869  -42.351 -16.646 1.00 47.64 ?  265 GLU A OE2 1 
ATOM   1833 N N   . ALA A 1 254 ? -6.888  -37.975 -14.323 1.00 40.54 ?  266 ALA A N   1 
ATOM   1834 C CA  . ALA A 1 254 ? -8.336  -37.967 -14.492 1.00 49.20 ?  266 ALA A CA  1 
ATOM   1835 C C   . ALA A 1 254 ? -8.761  -36.994 -15.574 1.00 45.77 ?  266 ALA A C   1 
ATOM   1836 O O   . ALA A 1 254 ? -9.767  -37.227 -16.252 1.00 42.48 ?  266 ALA A O   1 
ATOM   1837 C CB  . ALA A 1 254 ? -9.040  -37.618 -13.176 1.00 44.17 ?  266 ALA A CB  1 
ATOM   1838 N N   . PHE A 1 255 ? -8.024  -35.895 -15.736 1.00 47.24 ?  267 PHE A N   1 
ATOM   1839 C CA  . PHE A 1 255 ? -8.351  -34.921 -16.774 1.00 44.49 ?  267 PHE A CA  1 
ATOM   1840 C C   . PHE A 1 255 ? -7.961  -35.430 -18.156 1.00 45.08 ?  267 PHE A C   1 
ATOM   1841 O O   . PHE A 1 255 ? -8.638  -35.129 -19.148 1.00 47.04 ?  267 PHE A O   1 
ATOM   1842 C CB  . PHE A 1 255 ? -7.653  -33.600 -16.460 1.00 43.50 ?  267 PHE A CB  1 
ATOM   1843 C CG  . PHE A 1 255 ? -8.085  -32.439 -17.318 1.00 46.40 ?  267 PHE A CG  1 
ATOM   1844 C CD1 . PHE A 1 255 ? -7.445  -32.165 -18.519 1.00 46.61 ?  267 PHE A CD1 1 
ATOM   1845 C CD2 . PHE A 1 255 ? -9.096  -31.595 -16.903 1.00 45.11 ?  267 PHE A CD2 1 
ATOM   1846 C CE1 . PHE A 1 255 ? -7.819  -31.080 -19.290 1.00 44.17 ?  267 PHE A CE1 1 
ATOM   1847 C CE2 . PHE A 1 255 ? -9.472  -30.511 -17.671 1.00 43.71 ?  267 PHE A CE2 1 
ATOM   1848 C CZ  . PHE A 1 255 ? -8.827  -30.252 -18.864 1.00 43.16 ?  267 PHE A CZ  1 
ATOM   1849 N N   . LEU A 1 256 ? -6.894  -36.223 -18.236 1.00 44.55 ?  268 LEU A N   1 
ATOM   1850 C CA  . LEU A 1 256 ? -6.359  -36.607 -19.536 1.00 45.63 ?  268 LEU A CA  1 
ATOM   1851 C C   . LEU A 1 256 ? -7.126  -37.768 -20.142 1.00 45.22 ?  268 LEU A C   1 
ATOM   1852 O O   . LEU A 1 256 ? -7.503  -37.706 -21.314 1.00 45.68 ?  268 LEU A O   1 
ATOM   1853 C CB  . LEU A 1 256 ? -4.875  -36.949 -19.417 1.00 42.61 ?  268 LEU A CB  1 
ATOM   1854 C CG  . LEU A 1 256 ? -3.952  -35.735 -19.451 1.00 50.06 ?  268 LEU A CG  1 
ATOM   1855 C CD1 . LEU A 1 256 ? -2.543  -36.188 -19.779 1.00 51.25 ?  268 LEU A CD1 1 
ATOM   1856 C CD2 . LEU A 1 256 ? -4.439  -34.701 -20.470 1.00 49.39 ?  268 LEU A CD2 1 
ATOM   1857 N N   . GLU A 1 257 ? -7.368  -38.827 -19.356 1.00 46.22 ?  269 GLU A N   1 
ATOM   1858 C CA  . GLU A 1 257 ? -7.940  -40.073 -19.875 1.00 51.04 ?  269 GLU A CA  1 
ATOM   1859 C C   . GLU A 1 257 ? -9.195  -39.877 -20.718 1.00 52.41 ?  269 GLU A C   1 
ATOM   1860 O O   . GLU A 1 257 ? -9.252  -40.432 -21.829 1.00 47.68 ?  269 GLU A O   1 
ATOM   1861 C CB  . GLU A 1 257 ? -8.226  -41.034 -18.716 1.00 48.98 ?  269 GLU A CB  1 
ATOM   1862 C CG  . GLU A 1 257 ? -7.183  -42.122 -18.520 1.00 53.93 ?  269 GLU A CG  1 
ATOM   1863 C CD  . GLU A 1 257 ? -7.386  -42.852 -17.191 1.00 68.01 ?  269 GLU A CD  1 
ATOM   1864 O OE1 . GLU A 1 257 ? -8.548  -43.206 -16.886 1.00 77.42 ?  269 GLU A OE1 1 
ATOM   1865 O OE2 . GLU A 1 257 ? -6.403  -43.058 -16.437 1.00 60.53 ?  269 GLU A OE2 1 
ATOM   1866 N N   . PRO A 1 258 ? -10.213 -39.123 -20.280 1.00 51.45 ?  270 PRO A N   1 
ATOM   1867 C CA  . PRO A 1 258 ? -11.374 -38.883 -21.150 1.00 52.37 ?  270 PRO A CA  1 
ATOM   1868 C C   . PRO A 1 258 ? -11.080 -38.006 -22.357 1.00 49.92 ?  270 PRO A C   1 
ATOM   1869 O O   . PRO A 1 258 ? -11.968 -37.848 -23.205 1.00 52.59 ?  270 PRO A O   1 
ATOM   1870 C CB  . PRO A 1 258 ? -12.378 -38.196 -20.212 1.00 50.34 ?  270 PRO A CB  1 
ATOM   1871 C CG  . PRO A 1 258 ? -11.541 -37.560 -19.181 1.00 48.76 ?  270 PRO A CG  1 
ATOM   1872 C CD  . PRO A 1 258 ? -10.424 -38.534 -18.947 1.00 50.28 ?  270 PRO A CD  1 
ATOM   1873 N N   . ARG A 1 259 ? -9.894  -37.411 -22.455 1.00 47.03 ?  271 ARG A N   1 
ATOM   1874 C CA  . ARG A 1 259 ? -9.548  -36.596 -23.611 1.00 44.43 ?  271 ARG A CA  1 
ATOM   1875 C C   . ARG A 1 259 ? -8.694  -37.343 -24.626 1.00 44.22 ?  271 ARG A C   1 
ATOM   1876 O O   . ARG A 1 259 ? -8.558  -36.876 -25.762 1.00 42.87 ?  271 ARG A O   1 
ATOM   1877 C CB  . ARG A 1 259 ? -8.832  -35.323 -23.163 1.00 42.77 ?  271 ARG A CB  1 
ATOM   1878 C CG  . ARG A 1 259 ? -9.730  -34.403 -22.387 1.00 45.84 ?  271 ARG A CG  1 
ATOM   1879 C CD  . ARG A 1 259 ? -9.013  -33.143 -21.929 1.00 46.75 ?  271 ARG A CD  1 
ATOM   1880 N NE  . ARG A 1 259 ? -9.954  -32.082 -21.606 1.00 44.88 ?  271 ARG A NE  1 
ATOM   1881 C CZ  . ARG A 1 259 ? -10.846 -32.143 -20.623 1.00 44.85 ?  271 ARG A CZ  1 
ATOM   1882 N NH1 . ARG A 1 259 ? -10.937 -33.204 -19.837 1.00 41.61 ?  271 ARG A NH1 1 
ATOM   1883 N NH2 . ARG A 1 259 ? -11.669 -31.114 -20.427 1.00 42.83 ?  271 ARG A NH2 1 
ATOM   1884 N N   . LEU A 1 260 ? -8.147  -38.494 -24.249 1.00 41.11 ?  272 LEU A N   1 
ATOM   1885 C CA  . LEU A 1 260 ? -7.365  -39.298 -25.171 1.00 44.87 ?  272 LEU A CA  1 
ATOM   1886 C C   . LEU A 1 260 ? -8.248  -39.816 -26.297 1.00 45.82 ?  272 LEU A C   1 
ATOM   1887 O O   . LEU A 1 260 ? -9.283  -40.441 -26.039 1.00 47.26 ?  272 LEU A O   1 
ATOM   1888 C CB  . LEU A 1 260 ? -6.732  -40.469 -24.427 1.00 44.65 ?  272 LEU A CB  1 
ATOM   1889 C CG  . LEU A 1 260 ? -5.667  -40.084 -23.403 1.00 45.86 ?  272 LEU A CG  1 
ATOM   1890 C CD1 . LEU A 1 260 ? -5.219  -41.341 -22.673 1.00 35.61 ?  272 LEU A CD1 1 
ATOM   1891 C CD2 . LEU A 1 260 ? -4.492  -39.352 -24.084 1.00 38.57 ?  272 LEU A CD2 1 
ATOM   1892 N N   . ASN A 1 261 ? -7.840  -39.575 -27.545 1.00 42.48 ?  273 ASN A N   1 
ATOM   1893 C CA  . ASN A 1 261 ? -8.585  -40.139 -28.659 1.00 39.81 ?  273 ASN A CA  1 
ATOM   1894 C C   . ASN A 1 261 ? -8.131  -41.572 -28.909 1.00 47.91 ?  273 ASN A C   1 
ATOM   1895 O O   . ASN A 1 261 ? -7.309  -42.133 -28.173 1.00 47.45 ?  273 ASN A O   1 
ATOM   1896 C CB  . ASN A 1 261 ? -8.461  -39.281 -29.914 1.00 40.08 ?  273 ASN A CB  1 
ATOM   1897 C CG  . ASN A 1 261 ? -7.024  -38.974 -30.291 1.00 41.56 ?  273 ASN A CG  1 
ATOM   1898 O OD1 . ASN A 1 261 ? -6.141  -39.848 -30.271 1.00 37.85 ?  273 ASN A OD1 1 
ATOM   1899 N ND2 . ASN A 1 261 ? -6.789  -37.723 -30.670 1.00 31.93 ?  273 ASN A ND2 1 
ATOM   1900 N N   . ALA A 1 262 ? -8.709  -42.179 -29.948 1.00 44.08 ?  274 ALA A N   1 
ATOM   1901 C CA  . ALA A 1 262 ? -8.429  -43.578 -30.253 1.00 47.59 ?  274 ALA A CA  1 
ATOM   1902 C C   . ALA A 1 262 ? -6.930  -43.834 -30.388 1.00 46.58 ?  274 ALA A C   1 
ATOM   1903 O O   . ALA A 1 262 ? -6.404  -44.820 -29.858 1.00 50.07 ?  274 ALA A O   1 
ATOM   1904 C CB  . ALA A 1 262 ? -9.167  -43.976 -31.533 1.00 43.27 ?  274 ALA A CB  1 
ATOM   1905 N N   . LYS A 1 263 ? -6.221  -42.945 -31.088 1.00 49.52 ?  275 LYS A N   1 
ATOM   1906 C CA  . LYS A 1 263 ? -4.775  -43.085 -31.213 1.00 51.03 ?  275 LYS A CA  1 
ATOM   1907 C C   . LYS A 1 263 ? -4.087  -42.840 -29.872 1.00 44.85 ?  275 LYS A C   1 
ATOM   1908 O O   . LYS A 1 263 ? -3.299  -43.673 -29.405 1.00 44.41 ?  275 LYS A O   1 
ATOM   1909 C CB  . LYS A 1 263 ? -4.254  -42.119 -32.281 1.00 49.13 ?  275 LYS A CB  1 
ATOM   1910 C CG  . LYS A 1 263 ? -2.745  -42.141 -32.455 1.00 43.47 ?  275 LYS A CG  1 
ATOM   1911 C CD  . LYS A 1 263 ? -2.340  -42.895 -33.712 1.00 52.95 ?  275 LYS A CD  1 
ATOM   1912 C CE  . LYS A 1 263 ? -2.839  -42.180 -34.986 1.00 54.96 ?  275 LYS A CE  1 
ATOM   1913 N NZ  . LYS A 1 263 ? -2.696  -43.021 -36.213 1.00 41.90 ?  275 LYS A NZ  1 
ATOM   1914 N N   . GLY A 1 264 ? -4.392  -41.700 -29.241 1.00 41.68 ?  276 GLY A N   1 
ATOM   1915 C CA  . GLY A 1 264 ? -3.790  -41.358 -27.958 1.00 41.90 ?  276 GLY A CA  1 
ATOM   1916 C C   . GLY A 1 264 ? -3.924  -42.444 -26.906 1.00 48.49 ?  276 GLY A C   1 
ATOM   1917 O O   . GLY A 1 264 ? -2.988  -42.700 -26.144 1.00 46.85 ?  276 GLY A O   1 
ATOM   1918 N N   . LYS A 1 265 ? -5.086  -43.103 -26.846 1.00 46.50 ?  277 LYS A N   1 
ATOM   1919 C CA  . LYS A 1 265 ? -5.253  -44.162 -25.856 1.00 44.79 ?  277 LYS A CA  1 
ATOM   1920 C C   . LYS A 1 265 ? -4.216  -45.256 -26.065 1.00 48.74 ?  277 LYS A C   1 
ATOM   1921 O O   . LYS A 1 265 ? -3.635  -45.771 -25.099 1.00 49.54 ?  277 LYS A O   1 
ATOM   1922 C CB  . LYS A 1 265 ? -6.673  -44.737 -25.921 1.00 47.79 ?  277 LYS A CB  1 
ATOM   1923 C CG  . LYS A 1 265 ? -7.716  -43.942 -25.134 1.00 46.38 ?  277 LYS A CG  1 
ATOM   1924 C CD  . LYS A 1 265 ? -9.053  -44.689 -25.037 1.00 58.92 ?  277 LYS A CD  1 
ATOM   1925 C CE  . LYS A 1 265 ? -10.254 -43.733 -25.130 1.00 57.30 ?  277 LYS A CE  1 
ATOM   1926 N NZ  . LYS A 1 265 ? -11.071 -43.913 -26.382 1.00 62.20 ?  277 LYS A NZ  1 
ATOM   1927 N N   . GLN A 1 266 ? -3.939  -45.599 -27.325 1.00 45.27 ?  278 GLN A N   1 
ATOM   1928 C CA  . GLN A 1 266 ? -2.967  -46.650 -27.597 1.00 48.01 ?  278 GLN A CA  1 
ATOM   1929 C C   . GLN A 1 266 ? -1.533  -46.170 -27.445 1.00 43.14 ?  278 GLN A C   1 
ATOM   1930 O O   . GLN A 1 266 ? -0.642  -46.990 -27.188 1.00 38.00 ?  278 GLN A O   1 
ATOM   1931 C CB  . GLN A 1 266 ? -3.157  -47.205 -29.006 1.00 52.71 ?  278 GLN A CB  1 
ATOM   1932 C CG  . GLN A 1 266 ? -4.066  -48.414 -29.089 1.00 51.13 ?  278 GLN A CG  1 
ATOM   1933 C CD  . GLN A 1 266 ? -4.593  -48.589 -30.491 1.00 59.92 ?  278 GLN A CD  1 
ATOM   1934 O OE1 . GLN A 1 266 ? -5.524  -47.892 -30.894 1.00 63.28 ?  278 GLN A OE1 1 
ATOM   1935 N NE2 . GLN A 1 266 ? -3.977  -49.486 -31.261 1.00 54.15 ?  278 GLN A NE2 1 
ATOM   1936 N N   . VAL A 1 267 ? -1.281  -44.871 -27.642 1.00 39.40 ?  279 VAL A N   1 
ATOM   1937 C CA  . VAL A 1 267 ? 0.079   -44.362 -27.483 1.00 43.25 ?  279 VAL A CA  1 
ATOM   1938 C C   . VAL A 1 267 ? 0.509   -44.432 -26.017 1.00 41.03 ?  279 VAL A C   1 
ATOM   1939 O O   . VAL A 1 267 ? 1.582   -44.950 -25.689 1.00 35.70 ?  279 VAL A O   1 
ATOM   1940 C CB  . VAL A 1 267 ? 0.197   -42.937 -28.050 1.00 40.01 ?  279 VAL A CB  1 
ATOM   1941 C CG1 . VAL A 1 267 ? 1.475   -42.249 -27.521 1.00 33.64 ?  279 VAL A CG1 1 
ATOM   1942 C CG2 . VAL A 1 267 ? 0.218   -42.998 -29.559 1.00 37.10 ?  279 VAL A CG2 1 
ATOM   1943 N N   . PHE A 1 268 ? -0.339  -43.952 -25.110 1.00 42.82 ?  280 PHE A N   1 
ATOM   1944 C CA  . PHE A 1 268 ? 0.026   -43.972 -23.698 1.00 40.45 ?  280 PHE A CA  1 
ATOM   1945 C C   . PHE A 1 268 ? 0.031   -45.381 -23.132 1.00 40.34 ?  280 PHE A C   1 
ATOM   1946 O O   . PHE A 1 268 ? 0.868   -45.699 -22.278 1.00 40.58 ?  280 PHE A O   1 
ATOM   1947 C CB  . PHE A 1 268 ? -0.904  -43.053 -22.923 1.00 38.70 ?  280 PHE A CB  1 
ATOM   1948 C CG  . PHE A 1 268 ? -0.524  -41.619 -23.060 1.00 37.98 ?  280 PHE A CG  1 
ATOM   1949 C CD1 . PHE A 1 268 ? 0.424   -41.054 -22.209 1.00 38.38 ?  280 PHE A CD1 1 
ATOM   1950 C CD2 . PHE A 1 268 ? -1.049  -40.850 -24.086 1.00 37.03 ?  280 PHE A CD2 1 
ATOM   1951 C CE1 . PHE A 1 268 ? 0.808   -39.722 -22.357 1.00 32.65 ?  280 PHE A CE1 1 
ATOM   1952 C CE2 . PHE A 1 268 ? -0.679  -39.523 -24.243 1.00 38.54 ?  280 PHE A CE2 1 
ATOM   1953 C CZ  . PHE A 1 268 ? 0.250   -38.958 -23.381 1.00 35.62 ?  280 PHE A CZ  1 
ATOM   1954 N N   . GLU A 1 269 ? -0.856  -46.250 -23.616 1.00 42.31 ?  281 GLU A N   1 
ATOM   1955 C CA  . GLU A 1 269 ? -0.780  -47.650 -23.223 1.00 39.24 ?  281 GLU A CA  1 
ATOM   1956 C C   . GLU A 1 269 ? 0.566   -48.262 -23.621 1.00 37.76 ?  281 GLU A C   1 
ATOM   1957 O O   . GLU A 1 269 ? 1.184   -49.009 -22.842 1.00 35.09 ?  281 GLU A O   1 
ATOM   1958 C CB  . GLU A 1 269 ? -1.947  -48.411 -23.841 1.00 41.04 ?  281 GLU A CB  1 
ATOM   1959 C CG  . GLU A 1 269 ? -1.780  -49.918 -23.870 1.00 49.76 ?  281 GLU A CG  1 
ATOM   1960 C CD  . GLU A 1 269 ? -3.108  -50.624 -24.090 1.00 66.88 ?  281 GLU A CD  1 
ATOM   1961 O OE1 . GLU A 1 269 ? -3.098  -51.812 -24.493 1.00 68.63 ?  281 GLU A OE1 1 
ATOM   1962 O OE2 . GLU A 1 269 ? -4.162  -49.979 -23.865 1.00 70.94 ?  281 GLU A OE2 1 
ATOM   1963 N N   . GLN A 1 270 ? 1.045   -47.946 -24.826 1.00 36.15 ?  282 GLN A N   1 
ATOM   1964 C CA  . GLN A 1 270 ? 2.346   -48.447 -25.259 1.00 41.11 ?  282 GLN A CA  1 
ATOM   1965 C C   . GLN A 1 270 ? 3.481   -47.899 -24.385 1.00 37.70 ?  282 GLN A C   1 
ATOM   1966 O O   . GLN A 1 270 ? 4.418   -48.630 -24.031 1.00 35.26 ?  282 GLN A O   1 
ATOM   1967 C CB  . GLN A 1 270 ? 2.566   -48.077 -26.719 1.00 38.63 ?  282 GLN A CB  1 
ATOM   1968 C CG  . GLN A 1 270 ? 3.899   -48.485 -27.284 1.00 31.06 ?  282 GLN A CG  1 
ATOM   1969 C CD  . GLN A 1 270 ? 4.074   -47.983 -28.704 1.00 38.16 ?  282 GLN A CD  1 
ATOM   1970 O OE1 . GLN A 1 270 ? 3.977   -46.777 -28.970 1.00 35.71 ?  282 GLN A OE1 1 
ATOM   1971 N NE2 . GLN A 1 270 ? 4.317   -48.905 -29.630 1.00 38.92 ?  282 GLN A NE2 1 
ATOM   1972 N N   . ILE A 1 271 ? 3.411   -46.615 -24.022 1.00 33.68 ?  283 ILE A N   1 
ATOM   1973 C CA  . ILE A 1 271 ? 4.502   -46.005 -23.263 1.00 42.01 ?  283 ILE A CA  1 
ATOM   1974 C C   . ILE A 1 271 ? 4.452   -46.364 -21.787 1.00 34.57 ?  283 ILE A C   1 
ATOM   1975 O O   . ILE A 1 271 ? 5.435   -46.129 -21.077 1.00 36.88 ?  283 ILE A O   1 
ATOM   1976 C CB  . ILE A 1 271 ? 4.524   -44.475 -23.476 1.00 34.81 ?  283 ILE A CB  1 
ATOM   1977 C CG1 . ILE A 1 271 ? 5.963   -43.947 -23.446 1.00 32.60 ?  283 ILE A CG1 1 
ATOM   1978 C CG2 . ILE A 1 271 ? 3.677   -43.767 -22.459 1.00 28.86 ?  283 ILE A CG2 1 
ATOM   1979 C CD1 . ILE A 1 271 ? 6.076   -42.515 -23.921 1.00 29.92 ?  283 ILE A CD1 1 
ATOM   1980 N N   . ARG A 1 272 ? 3.359   -46.969 -21.316 1.00 38.90 ?  284 ARG A N   1 
ATOM   1981 C CA  . ARG A 1 272 ? 3.287   -47.498 -19.957 1.00 34.41 ?  284 ARG A CA  1 
ATOM   1982 C C   . ARG A 1 272 ? 3.469   -49.008 -19.888 1.00 36.23 ?  284 ARG A C   1 
ATOM   1983 O O   . ARG A 1 272 ? 3.460   -49.564 -18.789 1.00 36.02 ?  284 ARG A O   1 
ATOM   1984 C CB  . ARG A 1 272 ? 1.965   -47.099 -19.309 1.00 30.88 ?  284 ARG A CB  1 
ATOM   1985 C CG  . ARG A 1 272 ? 1.975   -45.639 -18.855 1.00 32.79 ?  284 ARG A CG  1 
ATOM   1986 C CD  . ARG A 1 272 ? 0.600   -45.093 -18.680 1.00 32.86 ?  284 ARG A CD  1 
ATOM   1987 N NE  . ARG A 1 272 ? 0.608   -43.697 -18.259 1.00 34.30 ?  284 ARG A NE  1 
ATOM   1988 C CZ  . ARG A 1 272 ? -0.388  -43.125 -17.594 1.00 41.06 ?  284 ARG A CZ  1 
ATOM   1989 N NH1 . ARG A 1 272 ? -1.456  -43.817 -17.219 1.00 41.80 ?  284 ARG A NH1 1 
ATOM   1990 N NH2 . ARG A 1 272 ? -0.304  -41.838 -17.274 1.00 35.04 ?  284 ARG A NH2 1 
ATOM   1991 N N   . SER A 1 273 ? 3.708   -49.672 -21.015 1.00 41.16 ?  285 SER A N   1 
ATOM   1992 C CA  . SER A 1 273 ? 3.701   -51.129 -21.109 1.00 38.28 ?  285 SER A CA  1 
ATOM   1993 C C   . SER A 1 273 ? 5.068   -51.718 -20.775 1.00 37.99 ?  285 SER A C   1 
ATOM   1994 O O   . SER A 1 273 ? 6.103   -51.060 -20.903 1.00 39.15 ?  285 SER A O   1 
ATOM   1995 C CB  . SER A 1 273 ? 3.280   -51.564 -22.518 1.00 38.38 ?  285 SER A CB  1 
ATOM   1996 O OG  . SER A 1 273 ? 4.282   -51.253 -23.488 1.00 38.65 ?  285 SER A OG  1 
ATOM   1997 N N   . ARG A 1 274 ? 5.059   -52.992 -20.375 1.00 37.87 ?  286 ARG A N   1 
ATOM   1998 C CA  . ARG A 1 274 ? 6.284   -53.668 -19.956 1.00 39.89 ?  286 ARG A CA  1 
ATOM   1999 C C   . ARG A 1 274 ? 7.347   -53.622 -21.048 1.00 39.76 ?  286 ARG A C   1 
ATOM   2000 O O   . ARG A 1 274 ? 7.042   -53.717 -22.239 1.00 41.31 ?  286 ARG A O   1 
ATOM   2001 C CB  . ARG A 1 274 ? 5.991   -55.126 -19.583 1.00 43.11 ?  286 ARG A CB  1 
ATOM   2002 C CG  . ARG A 1 274 ? 5.422   -55.324 -18.184 1.00 40.45 ?  286 ARG A CG  1 
ATOM   2003 C CD  . ARG A 1 274 ? 5.554   -56.778 -17.767 1.00 43.62 ?  286 ARG A CD  1 
ATOM   2004 N NE  . ARG A 1 274 ? 4.655   -57.142 -16.675 1.00 45.05 ?  286 ARG A NE  1 
ATOM   2005 C CZ  . ARG A 1 274 ? 4.886   -58.125 -15.812 1.00 41.69 ?  286 ARG A CZ  1 
ATOM   2006 N NH1 . ARG A 1 274 ? 5.989   -58.853 -15.872 1.00 38.85 ?  286 ARG A NH1 1 
ATOM   2007 N NH2 . ARG A 1 274 ? 3.973   -58.399 -14.883 1.00 41.75 ?  286 ARG A NH2 1 
ATOM   2008 N N   . GLY A 1 275 ? 8.605   -53.469 -20.633 1.00 39.73 ?  287 GLY A N   1 
ATOM   2009 C CA  . GLY A 1 275 ? 9.726   -53.418 -21.553 1.00 38.00 ?  287 GLY A CA  1 
ATOM   2010 C C   . GLY A 1 275 ? 9.849   -52.163 -22.408 1.00 38.76 ?  287 GLY A C   1 
ATOM   2011 O O   . GLY A 1 275 ? 10.788  -52.086 -23.204 1.00 34.76 ?  287 GLY A O   1 
ATOM   2012 N N   . PHE A 1 276 ? 8.934   -51.187 -22.292 1.00 36.82 ?  288 PHE A N   1 
ATOM   2013 C CA  . PHE A 1 276 ? 9.006   -49.943 -23.072 1.00 35.88 ?  288 PHE A CA  1 
ATOM   2014 C C   . PHE A 1 276 ? 9.830   -48.947 -22.264 1.00 37.36 ?  288 PHE A C   1 
ATOM   2015 O O   . PHE A 1 276 ? 9.312   -48.190 -21.439 1.00 32.30 ?  288 PHE A O   1 
ATOM   2016 C CB  . PHE A 1 276 ? 7.618   -49.395 -23.390 1.00 33.06 ?  288 PHE A CB  1 
ATOM   2017 C CG  . PHE A 1 276 ? 7.577   -48.482 -24.600 1.00 37.49 ?  288 PHE A CG  1 
ATOM   2018 C CD1 . PHE A 1 276 ? 7.772   -47.108 -24.466 1.00 36.75 ?  288 PHE A CD1 1 
ATOM   2019 C CD2 . PHE A 1 276 ? 7.338   -48.996 -25.877 1.00 35.10 ?  288 PHE A CD2 1 
ATOM   2020 C CE1 . PHE A 1 276 ? 7.732   -46.262 -25.584 1.00 35.73 ?  288 PHE A CE1 1 
ATOM   2021 C CE2 . PHE A 1 276 ? 7.297   -48.155 -26.997 1.00 34.82 ?  288 PHE A CE2 1 
ATOM   2022 C CZ  . PHE A 1 276 ? 7.484   -46.788 -26.846 1.00 36.20 ?  288 PHE A CZ  1 
ATOM   2023 N N   . CYS A 1 277 ? 11.138  -48.957 -22.502 1.00 36.64 ?  289 CYS A N   1 
ATOM   2024 C CA  . CYS A 1 277 ? 12.042  -48.102 -21.752 1.00 36.07 ?  289 CYS A CA  1 
ATOM   2025 C C   . CYS A 1 277 ? 12.740  -47.107 -22.676 1.00 37.91 ?  289 CYS A C   1 
ATOM   2026 O O   . CYS A 1 277 ? 12.259  -46.852 -23.795 1.00 31.88 ?  289 CYS A O   1 
ATOM   2027 C CB  . CYS A 1 277 ? 13.027  -48.975 -20.989 1.00 35.65 ?  289 CYS A CB  1 
ATOM   2028 S SG  . CYS A 1 277 ? 12.149  -50.201 -19.983 1.00 32.26 ?  289 CYS A SG  1 
ATOM   2029 N N   . LEU A 1 278 ? 13.858  -46.534 -22.216 1.00 33.04 ?  290 LEU A N   1 
ATOM   2030 C CA  . LEU A 1 278 ? 14.509  -45.471 -22.979 1.00 30.31 ?  290 LEU A CA  1 
ATOM   2031 C C   . LEU A 1 278 ? 14.761  -45.856 -24.430 1.00 31.38 ?  290 LEU A C   1 
ATOM   2032 O O   . LEU A 1 278 ? 14.437  -45.053 -25.319 1.00 34.36 ?  290 LEU A O   1 
ATOM   2033 C CB  . LEU A 1 278 ? 15.816  -45.043 -22.298 1.00 30.24 ?  290 LEU A CB  1 
ATOM   2034 C CG  . LEU A 1 278 ? 16.603  -43.864 -22.914 1.00 32.47 ?  290 LEU A CG  1 
ATOM   2035 C CD1 . LEU A 1 278 ? 15.712  -42.754 -23.480 1.00 32.94 ?  290 LEU A CD1 1 
ATOM   2036 C CD2 . LEU A 1 278 ? 17.539  -43.271 -21.868 1.00 34.19 ?  290 LEU A CD2 1 
ATOM   2037 N N   . PRO A 1 279 ? 15.304  -47.030 -24.751 1.00 32.55 ?  291 PRO A N   1 
ATOM   2038 C CA  . PRO A 1 279 ? 15.535  -47.316 -26.180 1.00 31.10 ?  291 PRO A CA  1 
ATOM   2039 C C   . PRO A 1 279 ? 14.240  -47.301 -26.977 1.00 35.25 ?  291 PRO A C   1 
ATOM   2040 O O   . PRO A 1 279 ? 14.219  -46.808 -28.110 1.00 32.70 ?  291 PRO A O   1 
ATOM   2041 C CB  . PRO A 1 279 ? 16.206  -48.700 -26.161 1.00 31.36 ?  291 PRO A CB  1 
ATOM   2042 C CG  . PRO A 1 279 ? 16.801  -48.817 -24.745 1.00 30.82 ?  291 PRO A CG  1 
ATOM   2043 C CD  . PRO A 1 279 ? 15.776  -48.129 -23.879 1.00 29.78 ?  291 PRO A CD  1 
ATOM   2044 N N   . SER A 1 280 ? 13.136  -47.762 -26.382 1.00 30.46 ?  292 SER A N   1 
ATOM   2045 C CA  . SER A 1 280 ? 11.849  -47.667 -27.065 1.00 33.90 ?  292 SER A CA  1 
ATOM   2046 C C   . SER A 1 280 ? 11.377  -46.221 -27.161 1.00 33.74 ?  292 SER A C   1 
ATOM   2047 O O   . SER A 1 280 ? 10.876  -45.796 -28.206 1.00 36.33 ?  292 SER A O   1 
ATOM   2048 C CB  . SER A 1 280 ? 10.804  -48.515 -26.338 1.00 34.61 ?  292 SER A CB  1 
ATOM   2049 O OG  . SER A 1 280 ? 11.157  -49.883 -26.359 1.00 36.40 ?  292 SER A OG  1 
ATOM   2050 N N   . VAL A 1 281 ? 11.536  -45.450 -26.082 1.00 34.72 ?  293 VAL A N   1 
ATOM   2051 C CA  . VAL A 1 281 ? 10.992  -44.097 -26.028 1.00 31.08 ?  293 VAL A CA  1 
ATOM   2052 C C   . VAL A 1 281 ? 11.555  -43.230 -27.161 1.00 31.74 ?  293 VAL A C   1 
ATOM   2053 O O   . VAL A 1 281 ? 10.843  -42.395 -27.736 1.00 27.20 ?  293 VAL A O   1 
ATOM   2054 C CB  . VAL A 1 281 ? 11.257  -43.489 -24.633 1.00 35.10 ?  293 VAL A CB  1 
ATOM   2055 C CG1 . VAL A 1 281 ? 11.152  -41.957 -24.646 1.00 25.95 ?  293 VAL A CG1 1 
ATOM   2056 C CG2 . VAL A 1 281 ? 10.308  -44.095 -23.599 1.00 32.37 ?  293 VAL A CG2 1 
ATOM   2057 N N   . VAL A 1 282 ? 12.832  -43.416 -27.512 1.00 28.37 ?  294 VAL A N   1 
ATOM   2058 C CA  . VAL A 1 282 ? 13.412  -42.587 -28.566 1.00 33.75 ?  294 VAL A CA  1 
ATOM   2059 C C   . VAL A 1 282 ? 13.214  -43.175 -29.956 1.00 36.86 ?  294 VAL A C   1 
ATOM   2060 O O   . VAL A 1 282 ? 13.561  -42.514 -30.954 1.00 30.72 ?  294 VAL A O   1 
ATOM   2061 C CB  . VAL A 1 282 ? 14.918  -42.318 -28.338 1.00 33.50 ?  294 VAL A CB  1 
ATOM   2062 C CG1 . VAL A 1 282 ? 15.128  -41.631 -27.000 1.00 34.41 ?  294 VAL A CG1 1 
ATOM   2063 C CG2 . VAL A 1 282 ? 15.719  -43.590 -28.412 1.00 28.01 ?  294 VAL A CG2 1 
ATOM   2064 N N   . LEU A 1 283 ? 12.678  -44.393 -30.056 1.00 35.56 ?  295 LEU A N   1 
ATOM   2065 C CA  . LEU A 1 283 ? 12.351  -45.009 -31.333 1.00 38.04 ?  295 LEU A CA  1 
ATOM   2066 C C   . LEU A 1 283 ? 10.862  -44.923 -31.658 1.00 38.65 ?  295 LEU A C   1 
ATOM   2067 O O   . LEU A 1 283 ? 10.426  -45.505 -32.649 1.00 40.71 ?  295 LEU A O   1 
ATOM   2068 C CB  . LEU A 1 283 ? 12.814  -46.467 -31.348 1.00 34.65 ?  295 LEU A CB  1 
ATOM   2069 C CG  . LEU A 1 283 ? 14.331  -46.616 -31.405 1.00 38.38 ?  295 LEU A CG  1 
ATOM   2070 C CD1 . LEU A 1 283 ? 14.758  -48.026 -31.038 1.00 37.34 ?  295 LEU A CD1 1 
ATOM   2071 C CD2 . LEU A 1 283 ? 14.874  -46.229 -32.765 1.00 31.85 ?  295 LEU A CD2 1 
ATOM   2072 N N   . HIS A 1 284 ? 10.075  -44.207 -30.851 1.00 37.20 ?  296 HIS A N   1 
ATOM   2073 C CA  . HIS A 1 284 ? 8.644   -44.084 -31.075 1.00 34.76 ?  296 HIS A CA  1 
ATOM   2074 C C   . HIS A 1 284 ? 8.210   -42.638 -30.907 1.00 37.27 ?  296 HIS A C   1 
ATOM   2075 O O   . HIS A 1 284 ? 8.855   -41.851 -30.200 1.00 29.27 ?  296 HIS A O   1 
ATOM   2076 C CB  . HIS A 1 284 ? 7.832   -44.956 -30.116 1.00 33.03 ?  296 HIS A CB  1 
ATOM   2077 C CG  . HIS A 1 284 ? 7.988   -46.418 -30.362 1.00 37.42 ?  296 HIS A CG  1 
ATOM   2078 N ND1 . HIS A 1 284 ? 9.164   -47.091 -30.114 1.00 39.46 ?  296 HIS A ND1 1 
ATOM   2079 C CD2 . HIS A 1 284 ? 7.126   -47.335 -30.857 1.00 38.71 ?  296 HIS A CD2 1 
ATOM   2080 C CE1 . HIS A 1 284 ? 9.014   -48.366 -30.423 1.00 41.35 ?  296 HIS A CE1 1 
ATOM   2081 N NE2 . HIS A 1 284 ? 7.786   -48.541 -30.877 1.00 43.27 ?  296 HIS A NE2 1 
ATOM   2082 N N   . ASN A 1 285 ? 7.100   -42.307 -31.571 1.00 33.24 ?  297 ASN A N   1 
ATOM   2083 C CA  . ASN A 1 285 ? 6.465   -40.994 -31.493 1.00 33.35 ?  297 ASN A CA  1 
ATOM   2084 C C   . ASN A 1 285 ? 7.361   -39.881 -32.019 1.00 32.24 ?  297 ASN A C   1 
ATOM   2085 O O   . ASN A 1 285 ? 7.144   -38.698 -31.701 1.00 30.20 ?  297 ASN A O   1 
ATOM   2086 C CB  . ASN A 1 285 ? 6.001   -40.707 -30.057 1.00 35.10 ?  297 ASN A CB  1 
ATOM   2087 C CG  . ASN A 1 285 ? 5.143   -41.848 -29.491 1.00 36.91 ?  297 ASN A CG  1 
ATOM   2088 O OD1 . ASN A 1 285 ? 4.103   -42.209 -30.068 1.00 39.78 ?  297 ASN A OD1 1 
ATOM   2089 N ND2 . ASN A 1 285 ? 5.590   -42.439 -28.393 1.00 32.60 ?  297 ASN A ND2 1 
ATOM   2090 N N   . ASN A 1 286 ? 8.368   -40.252 -32.813 1.00 27.94 ?  298 ASN A N   1 
ATOM   2091 C CA  . ASN A 1 286 ? 9.194   -39.265 -33.485 1.00 29.89 ?  298 ASN A CA  1 
ATOM   2092 C C   . ASN A 1 286 ? 8.296   -38.349 -34.303 1.00 32.63 ?  298 ASN A C   1 
ATOM   2093 O O   . ASN A 1 286 ? 7.451   -38.825 -35.062 1.00 33.03 ?  298 ASN A O   1 
ATOM   2094 C CB  . ASN A 1 286 ? 10.237  -39.960 -34.370 1.00 27.69 ?  298 ASN A CB  1 
ATOM   2095 C CG  . ASN A 1 286 ? 11.110  -40.960 -33.585 1.00 34.11 ?  298 ASN A CG  1 
ATOM   2096 O OD1 . ASN A 1 286 ? 10.741  -42.114 -33.377 1.00 37.23 ?  298 ASN A OD1 1 
ATOM   2097 N ND2 . ASN A 1 286 ? 12.272  -40.504 -33.145 1.00 36.30 ?  298 ASN A ND2 1 
ATOM   2098 N N   . PHE A 1 287 ? 8.429   -37.035 -34.077 1.00 31.95 ?  299 PHE A N   1 
ATOM   2099 C CA  . PHE A 1 287 ? 7.734   -35.952 -34.772 1.00 32.48 ?  299 PHE A CA  1 
ATOM   2100 C C   . PHE A 1 287 ? 6.242   -35.883 -34.485 1.00 37.95 ?  299 PHE A C   1 
ATOM   2101 O O   . PHE A 1 287 ? 5.514   -35.153 -35.181 1.00 39.54 ?  299 PHE A O   1 
ATOM   2102 C CB  . PHE A 1 287 ? 7.943   -36.035 -36.284 1.00 34.86 ?  299 PHE A CB  1 
ATOM   2103 C CG  . PHE A 1 287 ? 9.371   -36.009 -36.667 1.00 31.36 ?  299 PHE A CG  1 
ATOM   2104 C CD1 . PHE A 1 287 ? 10.121  -34.861 -36.476 1.00 24.21 ?  299 PHE A CD1 1 
ATOM   2105 C CD2 . PHE A 1 287 ? 9.982   -37.147 -37.163 1.00 29.06 ?  299 PHE A CD2 1 
ATOM   2106 C CE1 . PHE A 1 287 ? 11.458  -34.837 -36.812 1.00 32.37 ?  299 PHE A CE1 1 
ATOM   2107 C CE2 . PHE A 1 287 ? 11.323  -37.135 -37.508 1.00 30.03 ?  299 PHE A CE2 1 
ATOM   2108 C CZ  . PHE A 1 287 ? 12.065  -35.980 -37.335 1.00 30.56 ?  299 PHE A CZ  1 
ATOM   2109 N N   . VAL A 1 288 ? 5.801   -36.608 -33.462 1.00 35.59 ?  300 VAL A N   1 
ATOM   2110 C CA  . VAL A 1 288 ? 4.352   -36.623 -33.120 1.00 32.07 ?  300 VAL A CA  1 
ATOM   2111 C C   . VAL A 1 288 ? 3.995   -35.328 -32.384 1.00 35.89 ?  300 VAL A C   1 
ATOM   2112 O O   . VAL A 1 288 ? 4.899   -34.688 -31.812 1.00 34.92 ?  300 VAL A O   1 
ATOM   2113 C CB  . VAL A 1 288 ? 3.959   -37.850 -32.274 1.00 33.04 ?  300 VAL A CB  1 
ATOM   2114 C CG1 . VAL A 1 288 ? 4.098   -37.594 -30.778 1.00 41.04 ?  300 VAL A CG1 1 
ATOM   2115 C CG2 . VAL A 1 288 ? 2.554   -38.342 -32.598 1.00 35.27 ?  300 VAL A CG2 1 
ATOM   2116 N N   . ASP A 1 289 ? 2.719   -34.959 -32.418 1.00 41.52 ?  301 ASP A N   1 
ATOM   2117 C CA  . ASP A 1 289 ? 2.263   -33.806 -31.607 1.00 38.68 ?  301 ASP A CA  1 
ATOM   2118 C C   . ASP A 1 289 ? 1.420   -34.427 -30.495 1.00 39.27 ?  301 ASP A C   1 
ATOM   2119 O O   . ASP A 1 289 ? 0.524   -35.225 -30.812 1.00 38.07 ?  301 ASP A O   1 
ATOM   2120 C CB  . ASP A 1 289 ? 1.526   -32.772 -32.442 1.00 34.49 ?  301 ASP A CB  1 
ATOM   2121 C CG  . ASP A 1 289 ? 1.153   -31.484 -31.722 1.00 42.29 ?  301 ASP A CG  1 
ATOM   2122 O OD1 . ASP A 1 289 ? 1.349   -31.415 -30.493 1.00 41.75 ?  301 ASP A OD1 1 
ATOM   2123 O OD2 . ASP A 1 289 ? 0.670   -30.556 -32.401 1.00 47.85 ?  301 ASP A OD2 1 
ATOM   2124 N N   . VAL A 1 290 ? 1.717   -34.085 -29.245 1.00 36.40 ?  302 VAL A N   1 
ATOM   2125 C CA  . VAL A 1 290 ? 0.962   -34.625 -28.076 1.00 39.88 ?  302 VAL A CA  1 
ATOM   2126 C C   . VAL A 1 290 ? -0.487  -34.143 -28.233 1.00 36.48 ?  302 VAL A C   1 
ATOM   2127 O O   . VAL A 1 290 ? -1.405  -34.914 -27.918 1.00 35.02 ?  302 VAL A O   1 
ATOM   2128 C CB  . VAL A 1 290 ? 1.613   -34.226 -26.739 1.00 34.41 ?  302 VAL A CB  1 
ATOM   2129 C CG1 . VAL A 1 290 ? 0.736   -34.578 -25.543 1.00 34.14 ?  302 VAL A CG1 1 
ATOM   2130 C CG2 . VAL A 1 290 ? 2.990   -34.862 -26.592 1.00 32.91 ?  302 VAL A CG2 1 
ATOM   2131 N N   . PHE A 1 291 ? -0.671  -32.926 -28.735 1.00 36.47 ?  303 PHE A N   1 
ATOM   2132 C CA  . PHE A 1 291 ? -2.020  -32.325 -28.922 1.00 42.23 ?  303 PHE A CA  1 
ATOM   2133 C C   . PHE A 1 291 ? -2.819  -33.211 -29.888 1.00 41.34 ?  303 PHE A C   1 
ATOM   2134 O O   . PHE A 1 291 ? -4.031  -33.309 -29.708 1.00 41.06 ?  303 PHE A O   1 
ATOM   2135 C CB  . PHE A 1 291 ? -1.829  -30.861 -29.325 1.00 41.07 ?  303 PHE A CB  1 
ATOM   2136 C CG  . PHE A 1 291 ? -1.385  -29.997 -28.154 1.00 44.60 ?  303 PHE A CG  1 
ATOM   2137 C CD1 . PHE A 1 291 ? -2.193  -29.855 -27.033 1.00 43.29 ?  303 PHE A CD1 1 
ATOM   2138 C CD2 . PHE A 1 291 ? -0.154  -29.352 -28.168 1.00 42.26 ?  303 PHE A CD2 1 
ATOM   2139 C CE1 . PHE A 1 291 ? -1.789  -29.076 -25.963 1.00 50.51 ?  303 PHE A CE1 1 
ATOM   2140 C CE2 . PHE A 1 291 ? 0.246   -28.575 -27.094 1.00 41.71 ?  303 PHE A CE2 1 
ATOM   2141 C CZ  . PHE A 1 291 ? -0.572  -28.439 -25.997 1.00 46.68 ?  303 PHE A CZ  1 
ATOM   2142 N N   . SER A 1 292 ? -2.171  -33.804 -30.889 1.00 38.77 ?  304 SER A N   1 
ATOM   2143 C CA  . SER A 1 292 ? -2.854  -34.715 -31.847 1.00 42.16 ?  304 SER A CA  1 
ATOM   2144 C C   . SER A 1 292 ? -3.445  -35.909 -31.080 1.00 42.12 ?  304 SER A C   1 
ATOM   2145 O O   . SER A 1 292 ? -4.524  -36.379 -31.481 1.00 36.54 ?  304 SER A O   1 
ATOM   2146 C CB  . SER A 1 292 ? -1.907  -35.174 -32.923 1.00 37.15 ?  304 SER A CB  1 
ATOM   2147 O OG  . SER A 1 292 ? -1.172  -36.313 -32.502 1.00 41.26 ?  304 SER A OG  1 
ATOM   2148 N N   . LEU A 1 293 ? -2.753  -36.409 -30.060 1.00 39.96 ?  305 LEU A N   1 
ATOM   2149 C CA  . LEU A 1 293 ? -3.224  -37.542 -29.214 1.00 35.34 ?  305 LEU A CA  1 
ATOM   2150 C C   . LEU A 1 293 ? -4.528  -37.179 -28.472 1.00 41.36 ?  305 LEU A C   1 
ATOM   2151 O O   . LEU A 1 293 ? -5.279  -38.113 -28.148 1.00 38.62 ?  305 LEU A O   1 
ATOM   2152 C CB  . LEU A 1 293 ? -2.111  -37.985 -28.266 1.00 38.03 ?  305 LEU A CB  1 
ATOM   2153 C CG  . LEU A 1 293 ? -0.744  -38.219 -28.916 1.00 37.34 ?  305 LEU A CG  1 
ATOM   2154 C CD1 . LEU A 1 293 ? 0.297   -38.596 -27.881 1.00 28.52 ?  305 LEU A CD1 1 
ATOM   2155 C CD2 . LEU A 1 293 ? -0.835  -39.281 -29.996 1.00 41.58 ?  305 LEU A CD2 1 
ATOM   2156 N N   . VAL A 1 294 ? -4.703  -35.929 -28.042 1.00 36.47 ?  306 VAL A N   1 
ATOM   2157 C CA  . VAL A 1 294 ? -5.889  -35.550 -27.210 1.00 39.93 ?  306 VAL A CA  1 
ATOM   2158 C C   . VAL A 1 294 ? -6.882  -34.662 -27.981 1.00 47.04 ?  306 VAL A C   1 
ATOM   2159 O O   . VAL A 1 294 ? -6.461  -33.960 -28.909 1.00 49.93 ?  306 VAL A O   1 
ATOM   2160 C CB  . VAL A 1 294 ? -5.416  -34.827 -25.939 1.00 40.97 ?  306 VAL A CB  1 
ATOM   2161 C CG1 . VAL A 1 294 ? -5.216  -35.793 -24.779 1.00 35.49 ?  306 VAL A CG1 1 
ATOM   2162 C CG2 . VAL A 1 294 ? -4.152  -34.021 -26.203 1.00 43.96 ?  306 VAL A CG2 1 
ATOM   2163 N N   . ASN A 1 295 ? -8.171  -34.740 -27.642 1.00 45.76 ?  307 ASN A N   1 
ATOM   2164 C CA  . ASN A 1 295 ? -9.202  -33.858 -28.267 1.00 46.46 ?  307 ASN A CA  1 
ATOM   2165 C C   . ASN A 1 295 ? -8.900  -32.392 -27.931 1.00 41.98 ?  307 ASN A C   1 
ATOM   2166 O O   . ASN A 1 295 ? -9.153  -31.534 -28.793 1.00 50.44 ?  307 ASN A O   1 
ATOM   2167 C CB  . ASN A 1 295 ? -10.624 -34.302 -27.917 1.00 48.39 ?  307 ASN A CB  1 
ATOM   2168 C CG  . ASN A 1 295 ? -11.109 -33.858 -26.555 1.00 52.43 ?  307 ASN A CG  1 
ATOM   2169 O OD1 . ASN A 1 295 ? -10.313 -33.723 -25.620 1.00 48.61 ?  307 ASN A OD1 1 
ATOM   2170 N ND2 . ASN A 1 295 ? -12.411 -33.640 -26.418 1.00 49.48 ?  307 ASN A ND2 1 
ATOM   2171 N N   . ASP A 1 296 ? -8.441  -32.103 -26.713 1.00 42.22 ?  308 ASP A N   1 
ATOM   2172 C CA  . ASP A 1 296 ? -8.240  -30.694 -26.278 1.00 48.41 ?  308 ASP A CA  1 
ATOM   2173 C C   . ASP A 1 296 ? -6.851  -30.167 -26.646 1.00 48.58 ?  308 ASP A C   1 
ATOM   2174 O O   . ASP A 1 296 ? -5.856  -30.819 -26.277 1.00 51.04 ?  308 ASP A O   1 
ATOM   2175 C CB  . ASP A 1 296 ? -8.404  -30.608 -24.772 1.00 44.74 ?  308 ASP A CB  1 
ATOM   2176 C CG  . ASP A 1 296 ? -8.959  -29.308 -24.219 1.00 47.91 ?  308 ASP A CG  1 
ATOM   2177 O OD1 . ASP A 1 296 ? -8.777  -28.265 -24.874 1.00 49.30 ?  308 ASP A OD1 1 
ATOM   2178 O OD2 . ASP A 1 296 ? -9.574  -29.367 -23.139 1.00 49.65 ?  308 ASP A OD2 1 
ATOM   2179 N N   . THR A 1 297 ? -6.786  -29.030 -27.345 1.00 50.21 ?  309 THR A N   1 
ATOM   2180 C CA  . THR A 1 297 ? -5.493  -28.376 -27.657 1.00 47.39 ?  309 THR A CA  1 
ATOM   2181 C C   . THR A 1 297 ? -5.214  -27.340 -26.593 1.00 43.61 ?  309 THR A C   1 
ATOM   2182 O O   . THR A 1 297 ? -4.170  -26.670 -26.691 1.00 50.80 ?  309 THR A O   1 
ATOM   2183 C CB  . THR A 1 297 ? -5.552  -27.759 -29.053 1.00 48.63 ?  309 THR A CB  1 
ATOM   2184 O OG1 . THR A 1 297 ? -6.459  -26.666 -28.946 1.00 49.23 ?  309 THR A OG1 1 
ATOM   2185 C CG2 . THR A 1 297 ? -6.037  -28.745 -30.099 1.00 45.76 ?  309 THR A CG2 1 
ATOM   2186 N N   . ASN A 1 298 ? -6.116  -27.193 -25.624 1.00 49.87 ?  310 ASN A N   1 
ATOM   2187 C CA  . ASN A 1 298 ? -6.010  -26.141 -24.572 1.00 53.45 ?  310 ASN A CA  1 
ATOM   2188 C C   . ASN A 1 298 ? -5.493  -26.729 -23.256 1.00 48.74 ?  310 ASN A C   1 
ATOM   2189 O O   . ASN A 1 298 ? -5.586  -26.024 -22.236 1.00 52.75 ?  310 ASN A O   1 
ATOM   2190 C CB  . ASN A 1 298 ? -7.324  -25.389 -24.404 1.00 54.55 ?  310 ASN A CB  1 
ATOM   2191 C CG  . ASN A 1 298 ? -7.502  -24.334 -25.465 1.00 61.52 ?  310 ASN A CG  1 
ATOM   2192 O OD1 . ASN A 1 298 ? -6.546  -23.630 -25.807 1.00 63.00 ?  310 ASN A OD1 1 
ATOM   2193 N ND2 . ASN A 1 298 ? -8.708  -24.211 -25.999 1.00 66.29 ?  310 ASN A ND2 1 
ATOM   2194 N N   . LEU A 1 299 ? -4.942  -27.943 -23.264 1.00 43.63 ?  311 LEU A N   1 
ATOM   2195 C CA  . LEU A 1 299 ? -4.597  -28.609 -21.982 1.00 47.23 ?  311 LEU A CA  1 
ATOM   2196 C C   . LEU A 1 299 ? -3.588  -27.778 -21.183 1.00 47.36 ?  311 LEU A C   1 
ATOM   2197 O O   . LEU A 1 299 ? -3.771  -27.689 -19.953 1.00 51.35 ?  311 LEU A O   1 
ATOM   2198 C CB  . LEU A 1 299 ? -3.972  -29.960 -22.311 1.00 47.48 ?  311 LEU A CB  1 
ATOM   2199 C CG  . LEU A 1 299 ? -4.852  -30.971 -23.044 1.00 46.20 ?  311 LEU A CG  1 
ATOM   2200 C CD1 . LEU A 1 299 ? -4.011  -32.209 -23.262 1.00 43.89 ?  311 LEU A CD1 1 
ATOM   2201 C CD2 . LEU A 1 299 ? -6.036  -31.297 -22.170 1.00 47.04 ?  311 LEU A CD2 1 
ATOM   2202 N N   . LEU A 1 300 ? -2.580  -27.188 -21.824 1.00 52.90 ?  312 LEU A N   1 
ATOM   2203 C CA  . LEU A 1 300 ? -1.574  -26.460 -21.015 1.00 52.27 ?  312 LEU A CA  1 
ATOM   2204 C C   . LEU A 1 300 ? -2.277  -25.302 -20.298 1.00 51.68 ?  312 LEU A C   1 
ATOM   2205 O O   . LEU A 1 300 ? -1.943  -25.058 -19.132 1.00 52.89 ?  312 LEU A O   1 
ATOM   2206 C CB  . LEU A 1 300 ? -0.470  -25.936 -21.929 1.00 49.56 ?  312 LEU A CB  1 
ATOM   2207 C CG  . LEU A 1 300 ? 0.341   -26.983 -22.697 1.00 52.77 ?  312 LEU A CG  1 
ATOM   2208 C CD1 . LEU A 1 300 ? 1.196   -26.290 -23.743 1.00 48.41 ?  312 LEU A CD1 1 
ATOM   2209 C CD2 . LEU A 1 300 ? 1.221   -27.751 -21.738 1.00 49.19 ?  312 LEU A CD2 1 
ATOM   2210 N N   . ILE A 1 301 ? -3.169  -24.595 -20.992 1.00 53.15 ?  313 ILE A N   1 
ATOM   2211 C CA  . ILE A 1 301 ? -3.947  -23.455 -20.410 1.00 52.71 ?  313 ILE A CA  1 
ATOM   2212 C C   . ILE A 1 301 ? -4.916  -23.895 -19.293 1.00 53.38 ?  313 ILE A C   1 
ATOM   2213 O O   . ILE A 1 301 ? -5.063  -23.121 -18.327 1.00 51.96 ?  313 ILE A O   1 
ATOM   2214 C CB  . ILE A 1 301 ? -4.643  -22.656 -21.533 1.00 53.69 ?  313 ILE A CB  1 
ATOM   2215 C CG1 . ILE A 1 301 ? -6.168  -22.767 -21.485 1.00 56.17 ?  313 ILE A CG1 1 
ATOM   2216 C CG2 . ILE A 1 301 ? -4.094  -23.052 -22.904 1.00 49.43 ?  313 ILE A CG2 1 
ATOM   2217 C CD1 . ILE A 1 301 ? -6.875  -22.026 -22.604 1.00 55.15 ?  313 ILE A CD1 1 
ATOM   2218 N N   . GLU A 1 302 ? -5.586  -25.044 -19.421 1.00 52.62 ?  314 GLU A N   1 
ATOM   2219 C CA  . GLU A 1 302 ? -6.665  -25.414 -18.460 1.00 48.20 ?  314 GLU A CA  1 
ATOM   2220 C C   . GLU A 1 302 ? -6.184  -26.061 -17.156 1.00 51.64 ?  314 GLU A C   1 
ATOM   2221 O O   . GLU A 1 302 ? -5.052  -26.587 -17.129 1.00 47.17 ?  314 GLU A O   1 
ATOM   2222 C CB  . GLU A 1 302 ? -7.583  -26.425 -19.138 1.00 43.61 ?  314 GLU A CB  1 
ATOM   2223 C CG  . GLU A 1 302 ? -8.386  -25.827 -20.286 1.00 49.39 ?  314 GLU A CG  1 
ATOM   2224 C CD  . GLU A 1 302 ? -8.668  -26.870 -21.345 1.00 50.05 ?  314 GLU A CD  1 
ATOM   2225 O OE1 . GLU A 1 302 ? -7.950  -27.891 -21.360 1.00 47.99 ?  314 GLU A OE1 1 
ATOM   2226 O OE2 . GLU A 1 302 ? -9.601  -26.661 -22.144 1.00 55.28 ?  314 GLU A OE2 1 
ATOM   2227 N N   . GLU A 1 303 ? -7.038  -26.038 -16.118 1.00 49.66 ?  315 GLU A N   1 
ATOM   2228 C CA  . GLU A 1 303 ? -6.684  -26.743 -14.900 1.00 45.64 ?  315 GLU A CA  1 
ATOM   2229 C C   . GLU A 1 303 ? -7.073  -28.217 -15.020 1.00 48.09 ?  315 GLU A C   1 
ATOM   2230 O O   . GLU A 1 303 ? -7.998  -28.564 -15.762 1.00 44.26 ?  315 GLU A O   1 
ATOM   2231 C CB  . GLU A 1 303 ? -7.363  -26.103 -13.698 1.00 45.38 ?  315 GLU A CB  1 
ATOM   2232 C CG  . GLU A 1 303 ? -6.902  -24.672 -13.436 1.00 45.30 ?  315 GLU A CG  1 
ATOM   2233 C CD  . GLU A 1 303 ? -5.402  -24.556 -13.172 1.00 46.04 ?  315 GLU A CD  1 
ATOM   2234 O OE1 . GLU A 1 303 ? -4.712  -25.592 -13.014 1.00 48.07 ?  315 GLU A OE1 1 
ATOM   2235 O OE2 . GLU A 1 303 ? -4.903  -23.412 -13.132 1.00 42.34 ?  315 GLU A OE2 1 
ATOM   2236 N N   . PRO A 1 304 ? -6.366  -29.115 -14.317 1.00 42.30 ?  316 PRO A N   1 
ATOM   2237 C CA  . PRO A 1 304 ? -5.302  -28.867 -13.338 1.00 46.67 ?  316 PRO A CA  1 
ATOM   2238 C C   . PRO A 1 304 ? -3.904  -28.715 -13.919 1.00 48.50 ?  316 PRO A C   1 
ATOM   2239 O O   . PRO A 1 304 ? -2.984  -28.405 -13.152 1.00 48.21 ?  316 PRO A O   1 
ATOM   2240 C CB  . PRO A 1 304 ? -5.338  -30.125 -12.484 1.00 41.74 ?  316 PRO A CB  1 
ATOM   2241 C CG  . PRO A 1 304 ? -5.687  -31.201 -13.490 1.00 41.23 ?  316 PRO A CG  1 
ATOM   2242 C CD  . PRO A 1 304 ? -6.601  -30.558 -14.502 1.00 39.93 ?  316 PRO A CD  1 
ATOM   2243 N N   . ILE A 1 305 ? -3.736  -28.951 -15.224 1.00 42.07 ?  317 ILE A N   1 
ATOM   2244 C CA  . ILE A 1 305 ? -2.388  -29.063 -15.778 1.00 42.64 ?  317 ILE A CA  1 
ATOM   2245 C C   . ILE A 1 305 ? -1.644  -27.736 -15.679 1.00 41.40 ?  317 ILE A C   1 
ATOM   2246 O O   . ILE A 1 305 ? -0.457  -27.704 -15.329 1.00 40.02 ?  317 ILE A O   1 
ATOM   2247 C CB  . ILE A 1 305 ? -2.452  -29.592 -17.220 1.00 43.71 ?  317 ILE A CB  1 
ATOM   2248 C CG1 . ILE A 1 305 ? -2.817  -31.079 -17.174 1.00 43.01 ?  317 ILE A CG1 1 
ATOM   2249 C CG2 . ILE A 1 305 ? -1.129  -29.365 -17.940 1.00 37.55 ?  317 ILE A CG2 1 
ATOM   2250 C CD1 . ILE A 1 305 ? -3.223  -31.644 -18.498 1.00 44.54 ?  317 ILE A CD1 1 
ATOM   2251 N N   . ALA A 1 306 ? -2.336  -26.624 -15.944 1.00 38.90 ?  318 ALA A N   1 
ATOM   2252 C CA  . ALA A 1 306 ? -1.714  -25.306 -15.856 1.00 42.66 ?  318 ALA A CA  1 
ATOM   2253 C C   . ALA A 1 306 ? -1.107  -25.058 -14.478 1.00 42.85 ?  318 ALA A C   1 
ATOM   2254 O O   . ALA A 1 306 ? 0.020   -24.562 -14.369 1.00 39.39 ?  318 ALA A O   1 
ATOM   2255 C CB  . ALA A 1 306 ? -2.740  -24.224 -16.202 1.00 44.80 ?  318 ALA A CB  1 
ATOM   2256 N N   . GLY A 1 307 ? -1.835  -25.404 -13.413 1.00 43.71 ?  319 GLY A N   1 
ATOM   2257 C CA  . GLY A 1 307 ? -1.281  -25.252 -12.077 1.00 39.62 ?  319 GLY A CA  1 
ATOM   2258 C C   . GLY A 1 307 ? -0.178  -26.252 -11.787 1.00 39.28 ?  319 GLY A C   1 
ATOM   2259 O O   . GLY A 1 307 ? 0.822   -25.918 -11.150 1.00 44.33 ?  319 GLY A O   1 
ATOM   2260 N N   . ILE A 1 308 ? -0.340  -27.489 -12.252 1.00 40.71 ?  320 ILE A N   1 
ATOM   2261 C CA  . ILE A 1 308 ? 0.683   -28.508 -12.025 1.00 41.13 ?  320 ILE A CA  1 
ATOM   2262 C C   . ILE A 1 308 ? 2.011   -28.090 -12.652 1.00 40.24 ?  320 ILE A C   1 
ATOM   2263 O O   . ILE A 1 308 ? 3.082   -28.213 -12.034 1.00 37.26 ?  320 ILE A O   1 
ATOM   2264 C CB  . ILE A 1 308 ? 0.198   -29.859 -12.573 1.00 41.80 ?  320 ILE A CB  1 
ATOM   2265 C CG1 . ILE A 1 308 ? -0.952  -30.384 -11.706 1.00 38.10 ?  320 ILE A CG1 1 
ATOM   2266 C CG2 . ILE A 1 308 ? 1.358   -30.854 -12.655 1.00 37.04 ?  320 ILE A CG2 1 
ATOM   2267 C CD1 . ILE A 1 308 ? -1.824  -31.388 -12.401 1.00 38.01 ?  320 ILE A CD1 1 
ATOM   2268 N N   . LEU A 1 309 ? 1.962   -27.587 -13.888 1.00 40.33 ?  321 LEU A N   1 
ATOM   2269 C CA  . LEU A 1 309 ? 3.174   -27.131 -14.551 1.00 37.32 ?  321 LEU A CA  1 
ATOM   2270 C C   . LEU A 1 309 ? 3.839   -26.000 -13.776 1.00 37.74 ?  321 LEU A C   1 
ATOM   2271 O O   . LEU A 1 309 ? 5.070   -25.906 -13.750 1.00 36.76 ?  321 LEU A O   1 
ATOM   2272 C CB  . LEU A 1 309 ? 2.837   -26.711 -15.981 1.00 37.07 ?  321 LEU A CB  1 
ATOM   2273 C CG  . LEU A 1 309 ? 2.522   -27.912 -16.892 1.00 39.47 ?  321 LEU A CG  1 
ATOM   2274 C CD1 . LEU A 1 309 ? 2.141   -27.456 -18.290 1.00 42.57 ?  321 LEU A CD1 1 
ATOM   2275 C CD2 . LEU A 1 309 ? 3.688   -28.911 -16.956 1.00 34.10 ?  321 LEU A CD2 1 
ATOM   2276 N N   . LYS A 1 310 ? 3.042   -25.153 -13.112 1.00 40.26 ?  322 LYS A N   1 
ATOM   2277 C CA  . LYS A 1 310 ? 3.586   -24.097 -12.265 1.00 40.11 ?  322 LYS A CA  1 
ATOM   2278 C C   . LYS A 1 310 ? 4.204   -24.655 -10.993 1.00 40.96 ?  322 LYS A C   1 
ATOM   2279 O O   . LYS A 1 310 ? 4.996   -23.966 -10.340 1.00 41.85 ?  322 LYS A O   1 
ATOM   2280 C CB  . LYS A 1 310 ? 2.499   -23.076 -11.918 1.00 41.61 ?  322 LYS A CB  1 
ATOM   2281 C CG  . LYS A 1 310 ? 2.446   -21.925 -12.901 1.00 42.34 ?  322 LYS A CG  1 
ATOM   2282 C CD  . LYS A 1 310 ? 1.065   -21.327 -13.022 1.00 42.54 ?  322 LYS A CD  1 
ATOM   2283 C CE  . LYS A 1 310 ? 1.077   -20.201 -14.044 1.00 48.63 ?  322 LYS A CE  1 
ATOM   2284 N NZ  . LYS A 1 310 ? 0.150   -20.434 -15.195 1.00 55.96 ?  322 LYS A NZ  1 
ATOM   2285 N N   . GLN A 1 311 ? 3.874   -25.891 -10.634 1.00 40.86 ?  323 GLN A N   1 
ATOM   2286 C CA  . GLN A 1 311 ? 4.567   -26.547 -9.541  1.00 40.62 ?  323 GLN A CA  1 
ATOM   2287 C C   . GLN A 1 311 ? 5.777   -27.318 -10.031 1.00 35.90 ?  323 GLN A C   1 
ATOM   2288 O O   . GLN A 1 311 ? 6.786   -27.394 -9.324  1.00 34.67 ?  323 GLN A O   1 
ATOM   2289 C CB  . GLN A 1 311 ? 3.607   -27.480 -8.799  1.00 40.31 ?  323 GLN A CB  1 
ATOM   2290 C CG  . GLN A 1 311 ? 2.412   -26.750 -8.231  1.00 39.69 ?  323 GLN A CG  1 
ATOM   2291 C CD  . GLN A 1 311 ? 1.440   -27.667 -7.522  1.00 51.11 ?  323 GLN A CD  1 
ATOM   2292 O OE1 . GLN A 1 311 ? 1.372   -28.868 -7.802  1.00 56.80 ?  323 GLN A OE1 1 
ATOM   2293 N NE2 . GLN A 1 311 ? 0.680   -27.103 -6.586  1.00 54.87 ?  323 GLN A NE2 1 
ATOM   2294 N N   . GLU A 1 312 ? 5.707   -27.855 -11.243 1.00 34.52 ?  324 GLU A N   1 
ATOM   2295 C CA  . GLU A 1 312 ? 6.751   -28.729 -11.770 1.00 34.98 ?  324 GLU A CA  1 
ATOM   2296 C C   . GLU A 1 312 ? 7.821   -27.946 -12.528 1.00 37.15 ?  324 GLU A C   1 
ATOM   2297 O O   . GLU A 1 312 ? 8.203   -28.293 -13.648 1.00 34.23 ?  324 GLU A O   1 
ATOM   2298 C CB  . GLU A 1 312 ? 6.113   -29.796 -12.650 1.00 32.21 ?  324 GLU A CB  1 
ATOM   2299 C CG  . GLU A 1 312 ? 5.164   -30.703 -11.889 1.00 32.65 ?  324 GLU A CG  1 
ATOM   2300 C CD  . GLU A 1 312 ? 5.892   -31.788 -11.091 1.00 32.97 ?  324 GLU A CD  1 
ATOM   2301 O OE1 . GLU A 1 312 ? 7.146   -31.841 -11.101 1.00 31.38 ?  324 GLU A OE1 1 
ATOM   2302 O OE2 . GLU A 1 312 ? 5.194   -32.607 -10.467 1.00 33.07 ?  324 GLU A OE2 1 
ATOM   2303 N N   . THR A 1 313 ? 8.313   -26.872 -11.907 1.00 35.92 ?  325 THR A N   1 
ATOM   2304 C CA  . THR A 1 313 ? 9.405   -26.088 -12.471 1.00 34.69 ?  325 THR A CA  1 
ATOM   2305 C C   . THR A 1 313 ? 10.272  -25.530 -11.352 1.00 33.41 ?  325 THR A C   1 
ATOM   2306 O O   . THR A 1 313 ? 9.801   -25.293 -10.239 1.00 37.43 ?  325 THR A O   1 
ATOM   2307 C CB  . THR A 1 313 ? 8.892   -24.937 -13.341 1.00 34.88 ?  325 THR A CB  1 
ATOM   2308 O OG1 . THR A 1 313 ? 10.008  -24.220 -13.879 1.00 32.58 ?  325 THR A OG1 1 
ATOM   2309 C CG2 . THR A 1 313 ? 8.009   -23.990 -12.519 1.00 33.02 ?  325 THR A CG2 1 
ATOM   2310 N N   . LEU A 1 314 ? 11.548  -25.328 -11.664 1.00 33.16 ?  326 LEU A N   1 
ATOM   2311 C CA  . LEU A 1 314 ? 12.504  -24.695 -10.773 1.00 33.71 ?  326 LEU A CA  1 
ATOM   2312 C C   . LEU A 1 314 ? 12.829  -23.262 -11.176 1.00 34.96 ?  326 LEU A C   1 
ATOM   2313 O O   . LEU A 1 314 ? 13.610  -22.599 -10.478 1.00 33.61 ?  326 LEU A O   1 
ATOM   2314 C CB  . LEU A 1 314 ? 13.798  -25.518 -10.716 1.00 30.45 ?  326 LEU A CB  1 
ATOM   2315 C CG  . LEU A 1 314 ? 13.591  -26.934 -10.191 1.00 32.34 ?  326 LEU A CG  1 
ATOM   2316 C CD1 . LEU A 1 314 ? 14.845  -27.743 -10.375 1.00 25.46 ?  326 LEU A CD1 1 
ATOM   2317 C CD2 . LEU A 1 314 ? 13.171  -26.909 -8.703  1.00 34.39 ?  326 LEU A CD2 1 
ATOM   2318 N N   . VAL A 1 315 ? 12.269  -22.775 -12.283 1.00 33.51 ?  327 VAL A N   1 
ATOM   2319 C CA  . VAL A 1 315 ? 12.455  -21.390 -12.713 1.00 33.99 ?  327 VAL A CA  1 
ATOM   2320 C C   . VAL A 1 315 ? 11.471  -20.522 -11.935 1.00 35.14 ?  327 VAL A C   1 
ATOM   2321 O O   . VAL A 1 315 ? 10.250  -20.688 -12.061 1.00 35.52 ?  327 VAL A O   1 
ATOM   2322 C CB  . VAL A 1 315 ? 12.252  -21.251 -14.233 1.00 34.46 ?  327 VAL A CB  1 
ATOM   2323 C CG1 . VAL A 1 315 ? 12.572  -19.849 -14.703 1.00 30.02 ?  327 VAL A CG1 1 
ATOM   2324 C CG2 . VAL A 1 315 ? 13.120  -22.255 -14.982 1.00 32.13 ?  327 VAL A CG2 1 
ATOM   2325 N N   . GLN A 1 316 ? 12.001  -19.623 -11.096 1.00 35.12 ?  328 GLN A N   1 
ATOM   2326 C CA  . GLN A 1 316 ? 11.139  -18.810 -10.236 1.00 37.11 ?  328 GLN A CA  1 
ATOM   2327 C C   . GLN A 1 316 ? 10.191  -17.945 -11.054 1.00 39.65 ?  328 GLN A C   1 
ATOM   2328 O O   . GLN A 1 316 ? 9.075   -17.650 -10.613 1.00 39.46 ?  328 GLN A O   1 
ATOM   2329 C CB  . GLN A 1 316 ? 11.985  -17.933 -9.309  1.00 34.50 ?  328 GLN A CB  1 
ATOM   2330 C CG  . GLN A 1 316 ? 11.172  -17.094 -8.336  1.00 33.81 ?  328 GLN A CG  1 
ATOM   2331 C CD  . GLN A 1 316 ? 10.355  -17.944 -7.368  1.00 41.99 ?  328 GLN A CD  1 
ATOM   2332 O OE1 . GLN A 1 316 ? 10.856  -18.366 -6.316  1.00 39.63 ?  328 GLN A OE1 1 
ATOM   2333 N NE2 . GLN A 1 316 ? 9.091   -18.197 -7.716  1.00 37.18 ?  328 GLN A NE2 1 
ATOM   2334 N N   . ALA A 1 317 ? 10.609  -17.540 -12.250 1.00 36.43 ?  329 ALA A N   1 
ATOM   2335 C CA  . ALA A 1 317 ? 9.742   -16.722 -13.083 1.00 36.34 ?  329 ALA A CA  1 
ATOM   2336 C C   . ALA A 1 317 ? 8.484   -17.465 -13.508 1.00 40.42 ?  329 ALA A C   1 
ATOM   2337 O O   . ALA A 1 317 ? 7.491   -16.810 -13.838 1.00 43.06 ?  329 ALA A O   1 
ATOM   2338 C CB  . ALA A 1 317 ? 10.509  -16.220 -14.318 1.00 34.04 ?  329 ALA A CB  1 
ATOM   2339 N N   . GLU A 1 318 ? 8.494   -18.810 -13.518 1.00 36.30 ?  330 GLU A N   1 
ATOM   2340 C CA  . GLU A 1 318 ? 7.286   -19.575 -13.829 1.00 36.62 ?  330 GLU A CA  1 
ATOM   2341 C C   . GLU A 1 318 ? 6.617   -20.179 -12.610 1.00 40.40 ?  330 GLU A C   1 
ATOM   2342 O O   . GLU A 1 318 ? 5.457   -20.588 -12.711 1.00 42.88 ?  330 GLU A O   1 
ATOM   2343 C CB  . GLU A 1 318 ? 7.579   -20.738 -14.785 1.00 33.29 ?  330 GLU A CB  1 
ATOM   2344 C CG  . GLU A 1 318 ? 8.815   -20.544 -15.592 1.00 42.95 ?  330 GLU A CG  1 
ATOM   2345 C CD  . GLU A 1 318 ? 9.143   -21.748 -16.450 1.00 48.04 ?  330 GLU A CD  1 
ATOM   2346 O OE1 . GLU A 1 318 ? 8.575   -22.851 -16.177 1.00 40.25 ?  330 GLU A OE1 1 
ATOM   2347 O OE2 . GLU A 1 318 ? 9.964   -21.569 -17.388 1.00 36.92 ?  330 GLU A OE2 1 
ATOM   2348 N N   . ALA A 1 319 ? 7.322   -20.293 -11.489 1.00 34.37 ?  331 ALA A N   1 
ATOM   2349 C CA  . ALA A 1 319 ? 6.835   -21.095 -10.378 1.00 37.28 ?  331 ALA A CA  1 
ATOM   2350 C C   . ALA A 1 319 ? 5.713   -20.376 -9.638  1.00 44.96 ?  331 ALA A C   1 
ATOM   2351 O O   . ALA A 1 319 ? 5.708   -19.147 -9.534  1.00 46.47 ?  331 ALA A O   1 
ATOM   2352 C CB  . ALA A 1 319 ? 7.979   -21.412 -9.417  1.00 34.12 ?  331 ALA A CB  1 
ATOM   2353 N N   . SER A 1 320 ? 4.752   -21.152 -9.132  1.00 41.11 ?  332 SER A N   1 
ATOM   2354 C CA  . SER A 1 320 ? 3.698   -20.639 -8.271  1.00 37.60 ?  332 SER A CA  1 
ATOM   2355 C C   . SER A 1 320 ? 4.037   -20.821 -6.804  1.00 45.46 ?  332 SER A C   1 
ATOM   2356 O O   . SER A 1 320 ? 3.142   -20.782 -5.952  1.00 48.87 ?  332 SER A O   1 
ATOM   2357 C CB  . SER A 1 320 ? 2.372   -21.325 -8.593  1.00 37.33 ?  332 SER A CB  1 
ATOM   2358 O OG  . SER A 1 320 ? 2.459   -22.722 -8.351  1.00 45.73 ?  332 SER A OG  1 
ATOM   2359 N N   . TYR A 1 321 ? 5.307   -21.065 -6.501  1.00 42.47 ?  333 TYR A N   1 
ATOM   2360 C CA  . TYR A 1 321 ? 5.784   -21.229 -5.141  1.00 42.33 ?  333 TYR A CA  1 
ATOM   2361 C C   . TYR A 1 321 ? 7.147   -20.565 -5.073  1.00 40.72 ?  333 TYR A C   1 
ATOM   2362 O O   . TYR A 1 321 ? 7.755   -20.266 -6.100  1.00 38.66 ?  333 TYR A O   1 
ATOM   2363 C CB  . TYR A 1 321 ? 5.872   -22.718 -4.732  1.00 39.98 ?  333 TYR A CB  1 
ATOM   2364 C CG  . TYR A 1 321 ? 6.937   -23.489 -5.493  1.00 35.40 ?  333 TYR A CG  1 
ATOM   2365 C CD1 . TYR A 1 321 ? 6.742   -23.850 -6.825  1.00 37.59 ?  333 TYR A CD1 1 
ATOM   2366 C CD2 . TYR A 1 321 ? 8.143   -23.832 -4.893  1.00 35.27 ?  333 TYR A CD2 1 
ATOM   2367 C CE1 . TYR A 1 321 ? 7.711   -24.544 -7.542  1.00 35.79 ?  333 TYR A CE1 1 
ATOM   2368 C CE2 . TYR A 1 321 ? 9.132   -24.528 -5.608  1.00 37.59 ?  333 TYR A CE2 1 
ATOM   2369 C CZ  . TYR A 1 321 ? 8.900   -24.876 -6.935  1.00 35.00 ?  333 TYR A CZ  1 
ATOM   2370 O OH  . TYR A 1 321 ? 9.855   -25.551 -7.655  1.00 32.63 ?  333 TYR A OH  1 
ATOM   2371 N N   . THR A 1 322 ? 7.624   -20.325 -3.855  1.00 41.03 ?  334 THR A N   1 
ATOM   2372 C CA  . THR A 1 322 ? 8.960   -19.774 -3.672  1.00 37.88 ?  334 THR A CA  1 
ATOM   2373 C C   . THR A 1 322 ? 9.967   -20.899 -3.857  1.00 38.45 ?  334 THR A C   1 
ATOM   2374 O O   . THR A 1 322 ? 10.048  -21.813 -3.030  1.00 39.08 ?  334 THR A O   1 
ATOM   2375 C CB  . THR A 1 322 ? 9.107   -19.126 -2.297  1.00 39.53 ?  334 THR A CB  1 
ATOM   2376 O OG1 . THR A 1 322 ? 8.171   -18.049 -2.172  1.00 46.48 ?  334 THR A OG1 1 
ATOM   2377 C CG2 . THR A 1 322 ? 10.512  -18.569 -2.127  1.00 34.82 ?  334 THR A CG2 1 
ATOM   2378 N N   . VAL A 1 323 ? 10.746  -20.824 -4.928  1.00 38.03 ?  335 VAL A N   1 
ATOM   2379 C CA  . VAL A 1 323 ? 11.707  -21.888 -5.231  1.00 33.65 ?  335 VAL A CA  1 
ATOM   2380 C C   . VAL A 1 323 ? 12.835  -21.865 -4.208  1.00 34.08 ?  335 VAL A C   1 
ATOM   2381 O O   . VAL A 1 323 ? 13.419  -20.795 -3.958  1.00 36.78 ?  335 VAL A O   1 
ATOM   2382 C CB  . VAL A 1 323 ? 12.258  -21.721 -6.644  1.00 34.24 ?  335 VAL A CB  1 
ATOM   2383 C CG1 . VAL A 1 323 ? 13.253  -22.866 -6.950  1.00 32.37 ?  335 VAL A CG1 1 
ATOM   2384 C CG2 . VAL A 1 323 ? 11.121  -21.660 -7.642  1.00 34.49 ?  335 VAL A CG2 1 
ATOM   2385 N N   . PRO A 1 324 ? 13.198  -23.010 -3.631  1.00 33.94 ?  336 PRO A N   1 
ATOM   2386 C CA  . PRO A 1 324 ? 14.393  -23.079 -2.778  1.00 32.64 ?  336 PRO A CA  1 
ATOM   2387 C C   . PRO A 1 324 ? 15.673  -22.678 -3.506  1.00 38.09 ?  336 PRO A C   1 
ATOM   2388 O O   . PRO A 1 324 ? 15.805  -22.825 -4.727  1.00 33.57 ?  336 PRO A O   1 
ATOM   2389 C CB  . PRO A 1 324 ? 14.450  -24.553 -2.363  1.00 33.74 ?  336 PRO A CB  1 
ATOM   2390 C CG  . PRO A 1 324 ? 13.065  -25.069 -2.517  1.00 35.06 ?  336 PRO A CG  1 
ATOM   2391 C CD  . PRO A 1 324 ? 12.437  -24.271 -3.650  1.00 35.92 ?  336 PRO A CD  1 
ATOM   2392 N N   . VAL A 1 325 ? 16.639  -22.199 -2.723  1.00 31.92 ?  337 VAL A N   1 
ATOM   2393 C CA  . VAL A 1 325 ? 17.923  -21.761 -3.258  1.00 34.26 ?  337 VAL A CA  1 
ATOM   2394 C C   . VAL A 1 325 ? 19.047  -22.447 -2.487  1.00 36.55 ?  337 VAL A C   1 
ATOM   2395 O O   . VAL A 1 325 ? 19.547  -21.902 -1.491  1.00 35.35 ?  337 VAL A O   1 
ATOM   2396 C CB  . VAL A 1 325 ? 18.056  -20.227 -3.205  1.00 37.86 ?  337 VAL A CB  1 
ATOM   2397 C CG1 . VAL A 1 325 ? 19.388  -19.793 -3.799  1.00 32.39 ?  337 VAL A CG1 1 
ATOM   2398 C CG2 . VAL A 1 325 ? 16.875  -19.538 -3.929  1.00 29.58 ?  337 VAL A CG2 1 
ATOM   2399 N N   . PRO A 1 326 ? 19.457  -23.646 -2.892  1.00 36.07 ?  338 PRO A N   1 
ATOM   2400 C CA  . PRO A 1 326 ? 20.542  -24.336 -2.180  1.00 36.28 ?  338 PRO A CA  1 
ATOM   2401 C C   . PRO A 1 326 ? 21.840  -23.540 -2.240  1.00 36.33 ?  338 PRO A C   1 
ATOM   2402 O O   . PRO A 1 326 ? 22.142  -22.884 -3.242  1.00 36.96 ?  338 PRO A O   1 
ATOM   2403 C CB  . PRO A 1 326 ? 20.671  -25.671 -2.931  1.00 30.67 ?  338 PRO A CB  1 
ATOM   2404 C CG  . PRO A 1 326 ? 19.365  -25.854 -3.609  1.00 29.01 ?  338 PRO A CG  1 
ATOM   2405 C CD  . PRO A 1 326 ? 18.829  -24.492 -3.922  1.00 29.24 ?  338 PRO A CD  1 
ATOM   2406 N N   . LYS A 1 327 ? 22.639  -23.659 -1.167  1.00 33.42 ?  339 LYS A N   1 
ATOM   2407 C CA  . LYS A 1 327 ? 23.832  -22.847 -0.962  1.00 30.80 ?  339 LYS A CA  1 
ATOM   2408 C C   . LYS A 1 327 ? 25.149  -23.592 -1.097  1.00 33.25 ?  339 LYS A C   1 
ATOM   2409 O O   . LYS A 1 327 ? 26.180  -22.939 -1.261  1.00 32.85 ?  339 LYS A O   1 
ATOM   2410 C CB  . LYS A 1 327 ? 23.815  -22.211 0.438   1.00 29.09 ?  339 LYS A CB  1 
ATOM   2411 C CG  . LYS A 1 327 ? 22.528  -21.521 0.814   1.00 25.04 ?  339 LYS A CG  1 
ATOM   2412 C CD  . LYS A 1 327 ? 22.171  -20.369 -0.154  1.00 34.09 ?  339 LYS A CD  1 
ATOM   2413 C CE  . LYS A 1 327 ? 20.911  -19.689 0.370   1.00 34.13 ?  339 LYS A CE  1 
ATOM   2414 N NZ  . LYS A 1 327 ? 20.042  -19.143 -0.675  1.00 43.56 ?  339 LYS A NZ  1 
ATOM   2415 N N   . PHE A 1 328 ? 25.159  -24.918 -0.974  1.00 30.05 ?  340 PHE A N   1 
ATOM   2416 C CA  . PHE A 1 328 ? 26.409  -25.669 -0.995  1.00 31.31 ?  340 PHE A CA  1 
ATOM   2417 C C   . PHE A 1 328 ? 27.045  -25.600 -2.387  1.00 32.28 ?  340 PHE A C   1 
ATOM   2418 O O   . PHE A 1 328 ? 26.404  -25.194 -3.362  1.00 31.73 ?  340 PHE A O   1 
ATOM   2419 C CB  . PHE A 1 328 ? 26.158  -27.129 -0.594  1.00 33.44 ?  340 PHE A CB  1 
ATOM   2420 C CG  . PHE A 1 328 ? 25.118  -27.800 -1.427  1.00 34.98 ?  340 PHE A CG  1 
ATOM   2421 C CD1 . PHE A 1 328 ? 25.462  -28.411 -2.632  1.00 33.38 ?  340 PHE A CD1 1 
ATOM   2422 C CD2 . PHE A 1 328 ? 23.783  -27.771 -1.046  1.00 32.42 ?  340 PHE A CD2 1 
ATOM   2423 C CE1 . PHE A 1 328 ? 24.507  -29.012 -3.418  1.00 32.18 ?  340 PHE A CE1 1 
ATOM   2424 C CE2 . PHE A 1 328 ? 22.819  -28.369 -1.832  1.00 37.09 ?  340 PHE A CE2 1 
ATOM   2425 C CZ  . PHE A 1 328 ? 23.183  -28.990 -3.027  1.00 28.73 ?  340 PHE A CZ  1 
ATOM   2426 N N   . PRO A 1 329 ? 28.319  -25.961 -2.497  1.00 31.67 ?  341 PRO A N   1 
ATOM   2427 C CA  . PRO A 1 329 ? 28.990  -25.876 -3.803  1.00 28.33 ?  341 PRO A CA  1 
ATOM   2428 C C   . PRO A 1 329 ? 28.263  -26.710 -4.852  1.00 35.80 ?  341 PRO A C   1 
ATOM   2429 O O   . PRO A 1 329 ? 27.972  -27.891 -4.644  1.00 34.14 ?  341 PRO A O   1 
ATOM   2430 C CB  . PRO A 1 329 ? 30.398  -26.420 -3.523  1.00 34.24 ?  341 PRO A CB  1 
ATOM   2431 C CG  . PRO A 1 329 ? 30.569  -26.382 -1.970  1.00 28.63 ?  341 PRO A CG  1 
ATOM   2432 C CD  . PRO A 1 329 ? 29.239  -26.143 -1.354  1.00 28.15 ?  341 PRO A CD  1 
ATOM   2433 N N   . ARG A 1 330 ? 27.968  -26.086 -5.990  1.00 32.16 ?  342 ARG A N   1 
ATOM   2434 C CA  . ARG A 1 330 ? 27.309  -26.774 -7.082  1.00 29.40 ?  342 ARG A CA  1 
ATOM   2435 C C   . ARG A 1 330 ? 28.106  -26.568 -8.353  1.00 32.35 ?  342 ARG A C   1 
ATOM   2436 O O   . ARG A 1 330 ? 28.751  -25.530 -8.548  1.00 33.70 ?  342 ARG A O   1 
ATOM   2437 C CB  . ARG A 1 330 ? 25.858  -26.298 -7.294  1.00 25.77 ?  342 ARG A CB  1 
ATOM   2438 C CG  . ARG A 1 330 ? 24.878  -26.867 -6.270  1.00 28.46 ?  342 ARG A CG  1 
ATOM   2439 C CD  . ARG A 1 330 ? 23.441  -26.605 -6.691  1.00 27.15 ?  342 ARG A CD  1 
ATOM   2440 N NE  . ARG A 1 330 ? 22.996  -25.277 -6.299  1.00 30.61 ?  342 ARG A NE  1 
ATOM   2441 C CZ  . ARG A 1 330 ? 21.824  -24.743 -6.614  1.00 32.71 ?  342 ARG A CZ  1 
ATOM   2442 N NH1 . ARG A 1 330 ? 20.975  -25.367 -7.414  1.00 33.51 ?  342 ARG A NH1 1 
ATOM   2443 N NH2 . ARG A 1 330 ? 21.489  -23.555 -6.105  1.00 26.71 ?  342 ARG A NH2 1 
ATOM   2444 N N   . PHE A 1 331 ? 28.043  -27.580 -9.214  1.00 31.12 ?  343 PHE A N   1 
ATOM   2445 C CA  . PHE A 1 331 ? 28.693  -27.582 -10.517 1.00 30.64 ?  343 PHE A CA  1 
ATOM   2446 C C   . PHE A 1 331 ? 27.661  -28.013 -11.556 1.00 35.85 ?  343 PHE A C   1 
ATOM   2447 O O   . PHE A 1 331 ? 27.153  -29.139 -11.498 1.00 28.68 ?  343 PHE A O   1 
ATOM   2448 C CB  . PHE A 1 331 ? 29.895  -28.525 -10.504 1.00 27.75 ?  343 PHE A CB  1 
ATOM   2449 C CG  . PHE A 1 331 ? 30.638  -28.587 -11.807 1.00 33.06 ?  343 PHE A CG  1 
ATOM   2450 C CD1 . PHE A 1 331 ? 30.196  -29.415 -12.841 1.00 30.16 ?  343 PHE A CD1 1 
ATOM   2451 C CD2 . PHE A 1 331 ? 31.793  -27.830 -11.997 1.00 32.39 ?  343 PHE A CD2 1 
ATOM   2452 C CE1 . PHE A 1 331 ? 30.892  -29.478 -14.038 1.00 32.74 ?  343 PHE A CE1 1 
ATOM   2453 C CE2 . PHE A 1 331 ? 32.494  -27.876 -13.198 1.00 34.58 ?  343 PHE A CE2 1 
ATOM   2454 C CZ  . PHE A 1 331 ? 32.050  -28.707 -14.225 1.00 34.64 ?  343 PHE A CZ  1 
ATOM   2455 N N   . MET A 1 332 ? 27.340  -27.117 -12.493 1.00 31.72 ?  344 MET A N   1 
ATOM   2456 C CA  . MET A 1 332 ? 26.372  -27.402 -13.536 1.00 26.10 ?  344 MET A CA  1 
ATOM   2457 C C   . MET A 1 332 ? 26.934  -27.091 -14.914 1.00 32.61 ?  344 MET A C   1 
ATOM   2458 O O   . MET A 1 332 ? 27.740  -26.169 -15.102 1.00 28.33 ?  344 MET A O   1 
ATOM   2459 C CB  . MET A 1 332 ? 25.040  -26.660 -13.312 1.00 24.60 ?  344 MET A CB  1 
ATOM   2460 C CG  . MET A 1 332 ? 24.436  -26.930 -11.946 1.00 25.27 ?  344 MET A CG  1 
ATOM   2461 S SD  . MET A 1 332 ? 22.944  -25.981 -11.558 1.00 30.43 ?  344 MET A SD  1 
ATOM   2462 C CE  . MET A 1 332 ? 21.814  -26.354 -12.934 1.00 26.59 ?  344 MET A CE  1 
ATOM   2463 N N   . TRP A 1 333 ? 26.511  -27.907 -15.878 1.00 28.68 ?  345 TRP A N   1 
ATOM   2464 C CA  . TRP A 1 333 ? 26.937  -27.739 -17.246 1.00 25.92 ?  345 TRP A CA  1 
ATOM   2465 C C   . TRP A 1 333 ? 25.754  -28.021 -18.155 1.00 30.19 ?  345 TRP A C   1 
ATOM   2466 O O   . TRP A 1 333 ? 24.714  -28.527 -17.717 1.00 29.13 ?  345 TRP A O   1 
ATOM   2467 C CB  . TRP A 1 333 ? 28.165  -28.604 -17.568 1.00 27.72 ?  345 TRP A CB  1 
ATOM   2468 C CG  . TRP A 1 333 ? 27.978  -30.103 -17.704 1.00 32.66 ?  345 TRP A CG  1 
ATOM   2469 C CD1 . TRP A 1 333 ? 27.939  -30.824 -18.888 1.00 32.52 ?  345 TRP A CD1 1 
ATOM   2470 C CD2 . TRP A 1 333 ? 27.903  -31.078 -16.647 1.00 30.69 ?  345 TRP A CD2 1 
ATOM   2471 N NE1 . TRP A 1 333 ? 27.823  -32.163 -18.621 1.00 30.65 ?  345 TRP A NE1 1 
ATOM   2472 C CE2 . TRP A 1 333 ? 27.798  -32.351 -17.260 1.00 31.45 ?  345 TRP A CE2 1 
ATOM   2473 C CE3 . TRP A 1 333 ? 27.906  -31.000 -15.248 1.00 32.21 ?  345 TRP A CE3 1 
ATOM   2474 C CZ2 . TRP A 1 333 ? 27.691  -33.536 -16.518 1.00 31.83 ?  345 TRP A CZ2 1 
ATOM   2475 C CZ3 . TRP A 1 333 ? 27.798  -32.185 -14.510 1.00 34.72 ?  345 TRP A CZ3 1 
ATOM   2476 C CH2 . TRP A 1 333 ? 27.688  -33.434 -15.153 1.00 33.66 ?  345 TRP A CH2 1 
ATOM   2477 N N   . HIS A 1 334 ? 25.903  -27.615 -19.421 1.00 26.52 ?  346 HIS A N   1 
ATOM   2478 C CA  . HIS A 1 334 ? 24.842  -27.697 -20.410 1.00 25.40 ?  346 HIS A CA  1 
ATOM   2479 C C   . HIS A 1 334 ? 25.419  -27.389 -21.785 1.00 29.54 ?  346 HIS A C   1 
ATOM   2480 O O   . HIS A 1 334 ? 26.250  -26.484 -21.926 1.00 33.69 ?  346 HIS A O   1 
ATOM   2481 C CB  . HIS A 1 334 ? 23.707  -26.725 -20.086 1.00 23.52 ?  346 HIS A CB  1 
ATOM   2482 C CG  . HIS A 1 334 ? 22.358  -27.213 -20.510 1.00 31.32 ?  346 HIS A CG  1 
ATOM   2483 N ND1 . HIS A 1 334 ? 21.412  -27.662 -19.612 1.00 31.93 ?  346 HIS A ND1 1 
ATOM   2484 C CD2 . HIS A 1 334 ? 21.797  -27.328 -21.737 1.00 27.90 ?  346 HIS A CD2 1 
ATOM   2485 C CE1 . HIS A 1 334 ? 20.322  -28.016 -20.267 1.00 30.11 ?  346 HIS A CE1 1 
ATOM   2486 N NE2 . HIS A 1 334 ? 20.533  -27.834 -21.558 1.00 32.41 ?  346 HIS A NE2 1 
ATOM   2487 N N   . ALA A 1 335 ? 25.001  -28.163 -22.783 1.00 30.00 ?  347 ALA A N   1 
ATOM   2488 C CA  . ALA A 1 335 ? 25.311  -27.841 -24.175 1.00 29.92 ?  347 ALA A CA  1 
ATOM   2489 C C   . ALA A 1 335 ? 24.480  -26.643 -24.594 1.00 32.52 ?  347 ALA A C   1 
ATOM   2490 O O   . ALA A 1 335 ? 23.252  -26.663 -24.462 1.00 31.02 ?  347 ALA A O   1 
ATOM   2491 C CB  . ALA A 1 335 ? 25.011  -29.026 -25.089 1.00 24.72 ?  347 ALA A CB  1 
ATOM   2492 N N   . LEU A 1 336 ? 25.139  -25.585 -25.066 1.00 31.13 ?  348 LEU A N   1 
ATOM   2493 C CA  . LEU A 1 336 ? 24.366  -24.447 -25.552 1.00 29.83 ?  348 LEU A CA  1 
ATOM   2494 C C   . LEU A 1 336 ? 23.399  -24.867 -26.653 1.00 31.77 ?  348 LEU A C   1 
ATOM   2495 O O   . LEU A 1 336 ? 22.200  -24.556 -26.538 1.00 30.83 ?  348 LEU A O   1 
ATOM   2496 C CB  . LEU A 1 336 ? 25.311  -23.324 -26.001 1.00 27.26 ?  348 LEU A CB  1 
ATOM   2497 C CG  . LEU A 1 336 ? 24.618  -22.114 -26.616 1.00 26.06 ?  348 LEU A CG  1 
ATOM   2498 C CD1 . LEU A 1 336 ? 23.665  -21.477 -25.615 1.00 29.19 ?  348 LEU A CD1 1 
ATOM   2499 C CD2 . LEU A 1 336 ? 25.636  -21.091 -27.095 1.00 33.60 ?  348 LEU A CD2 1 
ATOM   2500 N N   . PRO A 1 337 ? 23.817  -25.603 -27.713 1.00 29.42 ?  349 PRO A N   1 
ATOM   2501 C CA  . PRO A 1 337 ? 22.838  -26.033 -28.720 1.00 31.19 ?  349 PRO A CA  1 
ATOM   2502 C C   . PRO A 1 337 ? 22.211  -27.381 -28.383 1.00 31.67 ?  349 PRO A C   1 
ATOM   2503 O O   . PRO A 1 337 ? 21.900  -28.160 -29.292 1.00 31.61 ?  349 PRO A O   1 
ATOM   2504 C CB  . PRO A 1 337 ? 23.669  -26.106 -30.022 1.00 29.76 ?  349 PRO A CB  1 
ATOM   2505 C CG  . PRO A 1 337 ? 25.094  -25.841 -29.640 1.00 29.98 ?  349 PRO A CG  1 
ATOM   2506 C CD  . PRO A 1 337 ? 25.175  -25.980 -28.126 1.00 28.26 ?  349 PRO A CD  1 
ATOM   2507 N N   . ASP A 1 338 ? 22.024  -27.678 -27.092 1.00 32.95 ?  350 ASP A N   1 
ATOM   2508 C CA  . ASP A 1 338 ? 21.330  -28.906 -26.713 1.00 29.74 ?  350 ASP A CA  1 
ATOM   2509 C C   . ASP A 1 338 ? 20.028  -29.025 -27.493 1.00 29.82 ?  350 ASP A C   1 
ATOM   2510 O O   . ASP A 1 338 ? 19.214  -28.098 -27.506 1.00 25.99 ?  350 ASP A O   1 
ATOM   2511 C CB  . ASP A 1 338 ? 21.041  -28.921 -25.216 1.00 26.13 ?  350 ASP A CB  1 
ATOM   2512 C CG  . ASP A 1 338 ? 20.694  -30.304 -24.708 1.00 28.53 ?  350 ASP A CG  1 
ATOM   2513 O OD1 . ASP A 1 338 ? 19.784  -30.962 -25.278 1.00 29.16 ?  350 ASP A OD1 1 
ATOM   2514 O OD2 . ASP A 1 338 ? 21.331  -30.737 -23.724 1.00 27.34 ?  350 ASP A OD2 1 
ATOM   2515 N N   . GLU A 1 339 ? 19.844  -30.167 -28.163 1.00 30.28 ?  351 GLU A N   1 
ATOM   2516 C CA  . GLU A 1 339 ? 18.678  -30.366 -29.025 1.00 35.96 ?  351 GLU A CA  1 
ATOM   2517 C C   . GLU A 1 339 ? 17.556  -31.146 -28.346 1.00 33.22 ?  351 GLU A C   1 
ATOM   2518 O O   . GLU A 1 339 ? 16.437  -31.166 -28.867 1.00 37.62 ?  351 GLU A O   1 
ATOM   2519 C CB  . GLU A 1 339 ? 19.091  -31.069 -30.341 1.00 29.48 ?  351 GLU A CB  1 
ATOM   2520 C CG  . GLU A 1 339 ? 19.205  -32.563 -30.222 1.00 33.89 ?  351 GLU A CG  1 
ATOM   2521 C CD  . GLU A 1 339 ? 20.478  -33.010 -29.513 1.00 32.86 ?  351 GLU A CD  1 
ATOM   2522 O OE1 . GLU A 1 339 ? 20.937  -32.312 -28.573 1.00 28.25 ?  351 GLU A OE1 1 
ATOM   2523 O OE2 . GLU A 1 339 ? 21.011  -34.075 -29.897 1.00 31.54 ?  351 GLU A OE2 1 
ATOM   2524 N N   . ILE A 1 340 ? 17.814  -31.751 -27.194 1.00 32.98 ?  352 ILE A N   1 
ATOM   2525 C CA  . ILE A 1 340 ? 16.805  -32.482 -26.434 1.00 27.92 ?  352 ILE A CA  1 
ATOM   2526 C C   . ILE A 1 340 ? 16.314  -31.679 -25.233 1.00 31.58 ?  352 ILE A C   1 
ATOM   2527 O O   . ILE A 1 340 ? 15.113  -31.598 -24.992 1.00 31.62 ?  352 ILE A O   1 
ATOM   2528 C CB  . ILE A 1 340 ? 17.355  -33.856 -25.985 1.00 28.45 ?  352 ILE A CB  1 
ATOM   2529 C CG1 . ILE A 1 340 ? 17.836  -34.684 -27.179 1.00 29.59 ?  352 ILE A CG1 1 
ATOM   2530 C CG2 . ILE A 1 340 ? 16.291  -34.603 -25.209 1.00 29.02 ?  352 ILE A CG2 1 
ATOM   2531 C CD1 . ILE A 1 340 ? 18.536  -35.957 -26.803 1.00 26.60 ?  352 ILE A CD1 1 
ATOM   2532 N N   . VAL A 1 341 ? 17.216  -31.106 -24.438 1.00 28.52 ?  353 VAL A N   1 
ATOM   2533 C CA  . VAL A 1 341 ? 16.819  -30.403 -23.223 1.00 28.36 ?  353 VAL A CA  1 
ATOM   2534 C C   . VAL A 1 341 ? 17.243  -28.943 -23.337 1.00 29.39 ?  353 VAL A C   1 
ATOM   2535 O O   . VAL A 1 341 ? 18.443  -28.644 -23.392 1.00 29.41 ?  353 VAL A O   1 
ATOM   2536 C CB  . VAL A 1 341 ? 17.396  -31.052 -21.954 1.00 28.89 ?  353 VAL A CB  1 
ATOM   2537 C CG1 . VAL A 1 341 ? 17.079  -30.186 -20.704 1.00 24.95 ?  353 VAL A CG1 1 
ATOM   2538 C CG2 . VAL A 1 341 ? 16.831  -32.465 -21.809 1.00 26.18 ?  353 VAL A CG2 1 
ATOM   2539 N N   . PRO A 1 342 ? 16.296  -27.999 -23.367 1.00 29.31 ?  354 PRO A N   1 
ATOM   2540 C CA  . PRO A 1 342 ? 16.620  -26.637 -23.818 1.00 30.75 ?  354 PRO A CA  1 
ATOM   2541 C C   . PRO A 1 342 ? 17.578  -25.929 -22.868 1.00 31.78 ?  354 PRO A C   1 
ATOM   2542 O O   . PRO A 1 342 ? 17.455  -26.005 -21.641 1.00 32.03 ?  354 PRO A O   1 
ATOM   2543 C CB  . PRO A 1 342 ? 15.250  -25.946 -23.848 1.00 28.99 ?  354 PRO A CB  1 
ATOM   2544 C CG  . PRO A 1 342 ? 14.478  -26.661 -22.775 1.00 27.78 ?  354 PRO A CG  1 
ATOM   2545 C CD  . PRO A 1 342 ? 14.892  -28.111 -22.946 1.00 28.43 ?  354 PRO A CD  1 
ATOM   2546 N N   . PHE A 1 343 ? 18.537  -25.223 -23.458 1.00 36.47 ?  355 PHE A N   1 
ATOM   2547 C CA  . PHE A 1 343 ? 19.558  -24.557 -22.658 1.00 30.21 ?  355 PHE A CA  1 
ATOM   2548 C C   . PHE A 1 343 ? 18.965  -23.441 -21.812 1.00 28.82 ?  355 PHE A C   1 
ATOM   2549 O O   . PHE A 1 343 ? 19.290  -23.317 -20.626 1.00 34.73 ?  355 PHE A O   1 
ATOM   2550 C CB  . PHE A 1 343 ? 20.655  -24.014 -23.578 1.00 30.36 ?  355 PHE A CB  1 
ATOM   2551 C CG  . PHE A 1 343 ? 21.564  -23.018 -22.926 1.00 28.95 ?  355 PHE A CG  1 
ATOM   2552 C CD1 . PHE A 1 343 ? 22.697  -23.442 -22.240 1.00 33.78 ?  355 PHE A CD1 1 
ATOM   2553 C CD2 . PHE A 1 343 ? 21.307  -21.659 -23.008 1.00 26.01 ?  355 PHE A CD2 1 
ATOM   2554 C CE1 . PHE A 1 343 ? 23.562  -22.523 -21.644 1.00 32.24 ?  355 PHE A CE1 1 
ATOM   2555 C CE2 . PHE A 1 343 ? 22.167  -20.740 -22.411 1.00 31.42 ?  355 PHE A CE2 1 
ATOM   2556 C CZ  . PHE A 1 343 ? 23.292  -21.172 -21.734 1.00 29.69 ?  355 PHE A CZ  1 
ATOM   2557 N N   . GLN A 1 344 ? 18.110  -22.613 -22.404 1.00 30.83 ?  356 GLN A N   1 
ATOM   2558 C CA  . GLN A 1 344 ? 17.753  -21.350 -21.766 1.00 28.84 ?  356 GLN A CA  1 
ATOM   2559 C C   . GLN A 1 344 ? 17.060  -21.496 -20.403 1.00 33.48 ?  356 GLN A C   1 
ATOM   2560 O O   . GLN A 1 344 ? 17.381  -20.704 -19.504 1.00 31.98 ?  356 GLN A O   1 
ATOM   2561 C CB  . GLN A 1 344 ? 16.913  -20.518 -22.748 1.00 30.60 ?  356 GLN A CB  1 
ATOM   2562 C CG  . GLN A 1 344 ? 16.734  -19.042 -22.357 1.00 33.93 ?  356 GLN A CG  1 
ATOM   2563 C CD  . GLN A 1 344 ? 18.070  -18.303 -22.226 1.00 40.70 ?  356 GLN A CD  1 
ATOM   2564 O OE1 . GLN A 1 344 ? 18.403  -17.773 -21.158 1.00 42.49 ?  356 GLN A OE1 1 
ATOM   2565 N NE2 . GLN A 1 344 ? 18.848  -18.281 -23.309 1.00 38.14 ?  356 GLN A NE2 1 
ATOM   2566 N N   . PRO A 1 345 ? 16.135  -22.436 -20.165 1.00 34.49 ?  357 PRO A N   1 
ATOM   2567 C CA  . PRO A 1 345 ? 15.581  -22.535 -18.802 1.00 30.10 ?  357 PRO A CA  1 
ATOM   2568 C C   . PRO A 1 345 ? 16.626  -22.896 -17.763 1.00 30.81 ?  357 PRO A C   1 
ATOM   2569 O O   . PRO A 1 345 ? 16.524  -22.461 -16.606 1.00 29.19 ?  357 PRO A O   1 
ATOM   2570 C CB  . PRO A 1 345 ? 14.499  -23.623 -18.936 1.00 27.59 ?  357 PRO A CB  1 
ATOM   2571 C CG  . PRO A 1 345 ? 14.076  -23.549 -20.355 1.00 31.75 ?  357 PRO A CG  1 
ATOM   2572 C CD  . PRO A 1 345 ? 15.379  -23.294 -21.103 1.00 34.33 ?  357 PRO A CD  1 
ATOM   2573 N N   . ALA A 1 346 ? 17.628  -23.692 -18.143 1.00 31.52 ?  358 ALA A N   1 
ATOM   2574 C CA  . ALA A 1 346 ? 18.713  -24.009 -17.226 1.00 27.97 ?  358 ALA A CA  1 
ATOM   2575 C C   . ALA A 1 346 ? 19.558  -22.778 -16.948 1.00 28.96 ?  358 ALA A C   1 
ATOM   2576 O O   . ALA A 1 346 ? 19.947  -22.533 -15.801 1.00 31.35 ?  358 ALA A O   1 
ATOM   2577 C CB  . ALA A 1 346 ? 19.572  -25.134 -17.792 1.00 28.58 ?  358 ALA A CB  1 
ATOM   2578 N N   . ALA A 1 347 ? 19.824  -21.980 -17.988 1.00 31.78 ?  359 ALA A N   1 
ATOM   2579 C CA  . ALA A 1 347 ? 20.536  -20.720 -17.805 1.00 32.27 ?  359 ALA A CA  1 
ATOM   2580 C C   . ALA A 1 347 ? 19.731  -19.754 -16.934 1.00 32.49 ?  359 ALA A C   1 
ATOM   2581 O O   . ALA A 1 347 ? 20.288  -19.102 -16.042 1.00 37.70 ?  359 ALA A O   1 
ATOM   2582 C CB  . ALA A 1 347 ? 20.860  -20.098 -19.170 1.00 26.66 ?  359 ALA A CB  1 
ATOM   2583 N N   . ASN A 1 348 ? 18.416  -19.676 -17.149 1.00 27.80 ?  360 ASN A N   1 
ATOM   2584 C CA  . ASN A 1 348 ? 17.591  -18.799 -16.329 1.00 28.86 ?  360 ASN A CA  1 
ATOM   2585 C C   . ASN A 1 348 ? 17.571  -19.262 -14.876 1.00 35.39 ?  360 ASN A C   1 
ATOM   2586 O O   . ASN A 1 348 ? 17.579  -18.435 -13.951 1.00 37.92 ?  360 ASN A O   1 
ATOM   2587 C CB  . ASN A 1 348 ? 16.161  -18.723 -16.882 1.00 27.07 ?  360 ASN A CB  1 
ATOM   2588 C CG  . ASN A 1 348 ? 16.070  -17.985 -18.220 1.00 34.60 ?  360 ASN A CG  1 
ATOM   2589 O OD1 . ASN A 1 348 ? 17.044  -17.411 -18.701 1.00 33.99 ?  360 ASN A OD1 1 
ATOM   2590 N ND2 . ASN A 1 348 ? 14.881  -17.993 -18.818 1.00 38.42 ?  360 ASN A ND2 1 
ATOM   2591 N N   . TYR A 1 349 ? 17.521  -20.579 -14.656 1.00 32.51 ?  361 TYR A N   1 
ATOM   2592 C CA  . TYR A 1 349 ? 17.568  -21.104 -13.295 1.00 31.37 ?  361 TYR A CA  1 
ATOM   2593 C C   . TYR A 1 349 ? 18.863  -20.699 -12.614 1.00 32.79 ?  361 TYR A C   1 
ATOM   2594 O O   . TYR A 1 349 ? 18.860  -20.206 -11.479 1.00 34.82 ?  361 TYR A O   1 
ATOM   2595 C CB  . TYR A 1 349 ? 17.429  -22.632 -13.315 1.00 27.38 ?  361 TYR A CB  1 
ATOM   2596 C CG  . TYR A 1 349 ? 17.620  -23.282 -11.964 1.00 25.07 ?  361 TYR A CG  1 
ATOM   2597 C CD1 . TYR A 1 349 ? 16.633  -23.208 -11.016 1.00 24.63 ?  361 TYR A CD1 1 
ATOM   2598 C CD2 . TYR A 1 349 ? 18.783  -23.986 -11.650 1.00 23.71 ?  361 TYR A CD2 1 
ATOM   2599 C CE1 . TYR A 1 349 ? 16.777  -23.796 -9.795  1.00 29.23 ?  361 TYR A CE1 1 
ATOM   2600 C CE2 . TYR A 1 349 ? 18.943  -24.598 -10.409 1.00 26.25 ?  361 TYR A CE2 1 
ATOM   2601 C CZ  . TYR A 1 349 ? 17.916  -24.489 -9.483  1.00 30.43 ?  361 TYR A CZ  1 
ATOM   2602 O OH  . TYR A 1 349 ? 17.989  -25.032 -8.224  1.00 31.27 ?  361 TYR A OH  1 
ATOM   2603 N N   . VAL A 1 350 ? 19.986  -20.896 -13.306 1.00 32.25 ?  362 VAL A N   1 
ATOM   2604 C CA  . VAL A 1 350 ? 21.288  -20.577 -12.731 1.00 35.27 ?  362 VAL A CA  1 
ATOM   2605 C C   . VAL A 1 350 ? 21.348  -19.104 -12.351 1.00 38.37 ?  362 VAL A C   1 
ATOM   2606 O O   . VAL A 1 350 ? 21.734  -18.747 -11.231 1.00 38.87 ?  362 VAL A O   1 
ATOM   2607 C CB  . VAL A 1 350 ? 22.403  -20.960 -13.718 1.00 35.33 ?  362 VAL A CB  1 
ATOM   2608 C CG1 . VAL A 1 350 ? 23.714  -20.315 -13.329 1.00 30.01 ?  362 VAL A CG1 1 
ATOM   2609 C CG2 . VAL A 1 350 ? 22.533  -22.467 -13.768 1.00 34.41 ?  362 VAL A CG2 1 
ATOM   2610 N N   . LYS A 1 351 ? 20.929  -18.231 -13.267 1.00 35.53 ?  363 LYS A N   1 
ATOM   2611 C CA  . LYS A 1 351 ? 20.935  -16.800 -12.992 1.00 38.40 ?  363 LYS A CA  1 
ATOM   2612 C C   . LYS A 1 351 ? 20.085  -16.465 -11.763 1.00 39.19 ?  363 LYS A C   1 
ATOM   2613 O O   . LYS A 1 351 ? 20.551  -15.779 -10.844 1.00 37.35 ?  363 LYS A O   1 
ATOM   2614 C CB  . LYS A 1 351 ? 20.454  -16.044 -14.232 1.00 39.86 ?  363 LYS A CB  1 
ATOM   2615 C CG  . LYS A 1 351 ? 20.489  -14.523 -14.103 1.00 44.83 ?  363 LYS A CG  1 
ATOM   2616 C CD  . LYS A 1 351 ? 19.153  -13.889 -14.509 1.00 57.08 ?  363 LYS A CD  1 
ATOM   2617 C CE  . LYS A 1 351 ? 17.956  -14.468 -13.724 1.00 53.23 ?  363 LYS A CE  1 
ATOM   2618 N NZ  . LYS A 1 351 ? 16.904  -13.438 -13.384 1.00 52.19 ?  363 LYS A NZ  1 
ATOM   2619 N N   . GLU A 1 352 ? 18.845  -16.966 -11.718 1.00 38.83 ?  364 GLU A N   1 
ATOM   2620 C CA  . GLU A 1 352 ? 17.964  -16.706 -10.577 1.00 37.99 ?  364 GLU A CA  1 
ATOM   2621 C C   . GLU A 1 352 ? 18.597  -17.156 -9.266  1.00 38.02 ?  364 GLU A C   1 
ATOM   2622 O O   . GLU A 1 352 ? 18.599  -16.413 -8.274  1.00 34.01 ?  364 GLU A O   1 
ATOM   2623 C CB  . GLU A 1 352 ? 16.634  -17.423 -10.772 1.00 33.99 ?  364 GLU A CB  1 
ATOM   2624 C CG  . GLU A 1 352 ? 15.721  -16.795 -11.792 1.00 35.51 ?  364 GLU A CG  1 
ATOM   2625 C CD  . GLU A 1 352 ? 14.455  -17.599 -11.957 1.00 33.08 ?  364 GLU A CD  1 
ATOM   2626 O OE1 . GLU A 1 352 ? 14.384  -18.687 -11.365 1.00 35.82 ?  364 GLU A OE1 1 
ATOM   2627 O OE2 . GLU A 1 352 ? 13.536  -17.155 -12.670 1.00 35.10 ?  364 GLU A OE2 1 
ATOM   2628 N N   . GLN A 1 353 ? 19.123  -18.391 -9.245  1.00 35.32 ?  365 GLN A N   1 
ATOM   2629 C CA  . GLN A 1 353 ? 19.740  -18.934 -8.037  1.00 35.73 ?  365 GLN A CA  1 
ATOM   2630 C C   . GLN A 1 353 ? 20.901  -18.068 -7.578  1.00 36.34 ?  365 GLN A C   1 
ATOM   2631 O O   . GLN A 1 353 ? 21.061  -17.805 -6.380  1.00 35.57 ?  365 GLN A O   1 
ATOM   2632 C CB  . GLN A 1 353 ? 20.222  -20.362 -8.293  1.00 31.38 ?  365 GLN A CB  1 
ATOM   2633 C CG  . GLN A 1 353 ? 19.089  -21.343 -8.625  1.00 35.99 ?  365 GLN A CG  1 
ATOM   2634 C CD  . GLN A 1 353 ? 18.291  -21.744 -7.387  1.00 32.75 ?  365 GLN A CD  1 
ATOM   2635 O OE1 . GLN A 1 353 ? 18.851  -22.237 -6.414  1.00 28.06 ?  365 GLN A OE1 1 
ATOM   2636 N NE2 . GLN A 1 353 ? 16.986  -21.524 -7.428  1.00 29.79 ?  365 GLN A NE2 1 
ATOM   2637 N N   . CYS A 1 354 ? 21.716  -17.620 -8.531  1.00 32.57 ?  366 CYS A N   1 
ATOM   2638 C CA  . CYS A 1 354 ? 22.876  -16.800 -8.234  1.00 36.62 ?  366 CYS A CA  1 
ATOM   2639 C C   . CYS A 1 354 ? 22.483  -15.456 -7.624  1.00 36.49 ?  366 CYS A C   1 
ATOM   2640 O O   . CYS A 1 354 ? 23.135  -14.990 -6.689  1.00 38.39 ?  366 CYS A O   1 
ATOM   2641 C CB  . CYS A 1 354 ? 23.685  -16.603 -9.509  1.00 33.58 ?  366 CYS A CB  1 
ATOM   2642 S SG  . CYS A 1 354 ? 24.593  -18.071 -9.990  1.00 36.49 ?  366 CYS A SG  1 
ATOM   2643 N N   . GLN A 1 355 ? 21.421  -14.821 -8.131  1.00 32.95 ?  367 GLN A N   1 
ATOM   2644 C CA  . GLN A 1 355 ? 20.952  -13.563 -7.554  1.00 35.09 ?  367 GLN A CA  1 
ATOM   2645 C C   . GLN A 1 355 ? 20.398  -13.727 -6.147  1.00 40.79 ?  367 GLN A C   1 
ATOM   2646 O O   . GLN A 1 355 ? 20.164  -12.717 -5.482  1.00 48.37 ?  367 GLN A O   1 
ATOM   2647 C CB  . GLN A 1 355 ? 19.866  -12.916 -8.428  1.00 38.09 ?  367 GLN A CB  1 
ATOM   2648 C CG  . GLN A 1 355 ? 20.302  -12.619 -9.856  1.00 47.14 ?  367 GLN A CG  1 
ATOM   2649 C CD  . GLN A 1 355 ? 19.146  -12.169 -10.760 1.00 57.00 ?  367 GLN A CD  1 
ATOM   2650 O OE1 . GLN A 1 355 ? 18.015  -12.650 -10.637 1.00 56.39 ?  367 GLN A OE1 1 
ATOM   2651 N NE2 . GLN A 1 355 ? 19.441  -11.265 -11.696 1.00 62.73 ?  367 GLN A NE2 1 
ATOM   2652 N N   . LYS A 1 356 ? 20.177  -14.956 -5.680  1.00 39.75 ?  368 LYS A N   1 
ATOM   2653 C CA  . LYS A 1 356 ? 19.695  -15.212 -4.328  1.00 31.65 ?  368 LYS A CA  1 
ATOM   2654 C C   . LYS A 1 356 ? 20.712  -15.972 -3.478  1.00 33.49 ?  368 LYS A C   1 
ATOM   2655 O O   . LYS A 1 356 ? 20.344  -16.529 -2.437  1.00 40.38 ?  368 LYS A O   1 
ATOM   2656 C CB  . LYS A 1 356 ? 18.369  -15.970 -4.375  1.00 35.58 ?  368 LYS A CB  1 
ATOM   2657 C CG  . LYS A 1 356 ? 17.196  -15.163 -4.905  1.00 36.37 ?  368 LYS A CG  1 
ATOM   2658 C CD  . LYS A 1 356 ? 15.897  -15.681 -4.299  1.00 46.23 ?  368 LYS A CD  1 
ATOM   2659 C CE  . LYS A 1 356 ? 14.672  -14.963 -4.850  1.00 57.02 ?  368 LYS A CE  1 
ATOM   2660 N NZ  . LYS A 1 356 ? 13.421  -15.366 -4.125  1.00 55.54 ?  368 LYS A NZ  1 
ATOM   2661 N N   . GLY A 1 357 ? 21.980  -16.024 -3.885  1.00 33.36 ?  369 GLY A N   1 
ATOM   2662 C CA  . GLY A 1 357 ? 23.037  -16.475 -2.994  1.00 35.40 ?  369 GLY A CA  1 
ATOM   2663 C C   . GLY A 1 357 ? 23.676  -17.829 -3.270  1.00 39.58 ?  369 GLY A C   1 
ATOM   2664 O O   . GLY A 1 357 ? 24.525  -18.261 -2.472  1.00 35.72 ?  369 GLY A O   1 
ATOM   2665 N N   . ALA A 1 358 ? 23.325  -18.492 -4.373  1.00 34.94 ?  370 ALA A N   1 
ATOM   2666 C CA  . ALA A 1 358 ? 23.859  -19.806 -4.713  1.00 36.33 ?  370 ALA A CA  1 
ATOM   2667 C C   . ALA A 1 358 ? 25.368  -19.754 -4.995  1.00 34.87 ?  370 ALA A C   1 
ATOM   2668 O O   . ALA A 1 358 ? 25.969  -18.697 -5.225  1.00 34.66 ?  370 ALA A O   1 
ATOM   2669 C CB  . ALA A 1 358 ? 23.123  -20.382 -5.927  1.00 30.46 ?  370 ALA A CB  1 
ATOM   2670 N N   . ASN A 1 359 ? 25.980  -20.935 -4.982  1.00 29.74 ?  371 ASN A N   1 
ATOM   2671 C CA  . ASN A 1 359 ? 27.375  -21.122 -5.361  1.00 29.27 ?  371 ASN A CA  1 
ATOM   2672 C C   . ASN A 1 359 ? 27.397  -22.124 -6.522  1.00 34.91 ?  371 ASN A C   1 
ATOM   2673 O O   . ASN A 1 359 ? 27.608  -23.330 -6.326  1.00 29.10 ?  371 ASN A O   1 
ATOM   2674 C CB  . ASN A 1 359 ? 28.214  -21.597 -4.181  1.00 28.01 ?  371 ASN A CB  1 
ATOM   2675 C CG  . ASN A 1 359 ? 29.678  -21.805 -4.561  1.00 30.43 ?  371 ASN A CG  1 
ATOM   2676 O OD1 . ASN A 1 359 ? 30.111  -21.372 -5.627  1.00 31.31 ?  371 ASN A OD1 1 
ATOM   2677 N ND2 . ASN A 1 359 ? 30.434  -22.473 -3.704  1.00 22.95 ?  371 ASN A ND2 1 
ATOM   2678 N N   . ILE A 1 360 ? 27.169  -21.621 -7.738  1.00 32.61 ?  372 ILE A N   1 
ATOM   2679 C CA  . ILE A 1 360 ? 27.037  -22.468 -8.925  1.00 31.35 ?  372 ILE A CA  1 
ATOM   2680 C C   . ILE A 1 360 ? 28.175  -22.163 -9.884  1.00 31.93 ?  372 ILE A C   1 
ATOM   2681 O O   . ILE A 1 360 ? 28.283  -21.048 -10.410 1.00 31.97 ?  372 ILE A O   1 
ATOM   2682 C CB  . ILE A 1 360 ? 25.692  -22.284 -9.635  1.00 31.26 ?  372 ILE A CB  1 
ATOM   2683 C CG1 . ILE A 1 360 ? 24.540  -22.595 -8.695  1.00 27.68 ?  372 ILE A CG1 1 
ATOM   2684 C CG2 . ILE A 1 360 ? 25.640  -23.192 -10.878 1.00 31.04 ?  372 ILE A CG2 1 
ATOM   2685 C CD1 . ILE A 1 360 ? 23.174  -22.402 -9.331  1.00 30.73 ?  372 ILE A CD1 1 
ATOM   2686 N N   . ASN A 1 361 ? 28.994  -23.177 -10.117 1.00 34.43 ?  373 ASN A N   1 
ATOM   2687 C CA  . ASN A 1 361 ? 30.086  -23.176 -11.080 1.00 30.75 ?  373 ASN A CA  1 
ATOM   2688 C C   . ASN A 1 361 ? 29.515  -23.649 -12.417 1.00 35.70 ?  373 ASN A C   1 
ATOM   2689 O O   . ASN A 1 361 ? 29.264  -24.848 -12.598 1.00 33.18 ?  373 ASN A O   1 
ATOM   2690 C CB  . ASN A 1 361 ? 31.167  -24.102 -10.530 1.00 33.44 ?  373 ASN A CB  1 
ATOM   2691 C CG  . ASN A 1 361 ? 32.396  -24.188 -11.388 1.00 35.09 ?  373 ASN A CG  1 
ATOM   2692 O OD1 . ASN A 1 361 ? 32.354  -23.989 -12.602 1.00 33.22 ?  373 ASN A OD1 1 
ATOM   2693 N ND2 . ASN A 1 361 ? 33.516  -24.537 -10.749 1.00 31.67 ?  373 ASN A ND2 1 
ATOM   2694 N N   . TRP A 1 362 ? 29.305  -22.704 -13.340 1.00 32.16 ?  374 TRP A N   1 
ATOM   2695 C CA  . TRP A 1 362 ? 28.444  -22.860 -14.511 1.00 33.96 ?  374 TRP A CA  1 
ATOM   2696 C C   . TRP A 1 362 ? 29.303  -23.016 -15.757 1.00 34.36 ?  374 TRP A C   1 
ATOM   2697 O O   . TRP A 1 362 ? 30.199  -22.203 -16.005 1.00 34.65 ?  374 TRP A O   1 
ATOM   2698 C CB  . TRP A 1 362 ? 27.498  -21.653 -14.641 1.00 31.09 ?  374 TRP A CB  1 
ATOM   2699 C CG  . TRP A 1 362 ? 26.451  -21.643 -15.807 1.00 35.96 ?  374 TRP A CG  1 
ATOM   2700 C CD1 . TRP A 1 362 ? 26.161  -20.574 -16.618 1.00 35.12 ?  374 TRP A CD1 1 
ATOM   2701 C CD2 . TRP A 1 362 ? 25.547  -22.702 -16.220 1.00 33.62 ?  374 TRP A CD2 1 
ATOM   2702 N NE1 . TRP A 1 362 ? 25.168  -20.897 -17.511 1.00 39.15 ?  374 TRP A NE1 1 
ATOM   2703 C CE2 . TRP A 1 362 ? 24.771  -22.192 -17.297 1.00 38.66 ?  374 TRP A CE2 1 
ATOM   2704 C CE3 . TRP A 1 362 ? 25.323  -24.023 -15.791 1.00 31.81 ?  374 TRP A CE3 1 
ATOM   2705 C CZ2 . TRP A 1 362 ? 23.784  -22.964 -17.959 1.00 30.60 ?  374 TRP A CZ2 1 
ATOM   2706 C CZ3 . TRP A 1 362 ? 24.357  -24.793 -16.451 1.00 29.65 ?  374 TRP A CZ3 1 
ATOM   2707 C CH2 . TRP A 1 362 ? 23.596  -24.255 -17.523 1.00 35.01 ?  374 TRP A CH2 1 
ATOM   2708 N N   . ASN A 1 363 ? 29.018  -24.051 -16.546 1.00 30.91 ?  375 ASN A N   1 
ATOM   2709 C CA  . ASN A 1 363 ? 29.891  -24.477 -17.634 1.00 26.67 ?  375 ASN A CA  1 
ATOM   2710 C C   . ASN A 1 363 ? 29.067  -24.667 -18.901 1.00 31.68 ?  375 ASN A C   1 
ATOM   2711 O O   . ASN A 1 363 ? 28.260  -25.600 -18.990 1.00 31.59 ?  375 ASN A O   1 
ATOM   2712 C CB  . ASN A 1 363 ? 30.610  -25.765 -17.261 1.00 28.35 ?  375 ASN A CB  1 
ATOM   2713 C CG  . ASN A 1 363 ? 31.580  -25.574 -16.132 1.00 30.87 ?  375 ASN A CG  1 
ATOM   2714 O OD1 . ASN A 1 363 ? 32.784  -25.417 -16.361 1.00 40.10 ?  375 ASN A OD1 1 
ATOM   2715 N ND2 . ASN A 1 363 ? 31.080  -25.605 -14.908 1.00 26.99 ?  375 ASN A ND2 1 
ATOM   2716 N N   . VAL A 1 364 ? 29.270  -23.793 -19.882 1.00 33.66 ?  376 VAL A N   1 
ATOM   2717 C CA  . VAL A 1 364 ? 28.458  -23.771 -21.092 1.00 28.61 ?  376 VAL A CA  1 
ATOM   2718 C C   . VAL A 1 364 ? 29.320  -24.236 -22.252 1.00 30.06 ?  376 VAL A C   1 
ATOM   2719 O O   . VAL A 1 364 ? 30.295  -23.570 -22.609 1.00 32.41 ?  376 VAL A O   1 
ATOM   2720 C CB  . VAL A 1 364 ? 27.880  -22.383 -21.350 1.00 30.40 ?  376 VAL A CB  1 
ATOM   2721 C CG1 . VAL A 1 364 ? 27.013  -22.395 -22.611 1.00 30.52 ?  376 VAL A CG1 1 
ATOM   2722 C CG2 . VAL A 1 364 ? 27.096  -21.920 -20.106 1.00 32.08 ?  376 VAL A CG2 1 
ATOM   2723 N N   . TYR A 1 365 ? 28.986  -25.395 -22.830 1.00 33.70 ?  377 TYR A N   1 
ATOM   2724 C CA  . TYR A 1 365 ? 29.765  -25.926 -23.949 1.00 28.91 ?  377 TYR A CA  1 
ATOM   2725 C C   . TYR A 1 365 ? 29.172  -25.403 -25.245 1.00 29.48 ?  377 TYR A C   1 
ATOM   2726 O O   . TYR A 1 365 ? 27.986  -25.651 -25.513 1.00 32.57 ?  377 TYR A O   1 
ATOM   2727 C CB  . TYR A 1 365 ? 29.785  -27.442 -23.940 1.00 27.77 ?  377 TYR A CB  1 
ATOM   2728 C CG  . TYR A 1 365 ? 30.570  -28.008 -22.767 1.00 33.19 ?  377 TYR A CG  1 
ATOM   2729 C CD1 . TYR A 1 365 ? 29.955  -28.213 -21.539 1.00 32.13 ?  377 TYR A CD1 1 
ATOM   2730 C CD2 . TYR A 1 365 ? 31.926  -28.325 -22.881 1.00 31.30 ?  377 TYR A CD2 1 
ATOM   2731 C CE1 . TYR A 1 365 ? 30.651  -28.718 -20.461 1.00 32.94 ?  377 TYR A CE1 1 
ATOM   2732 C CE2 . TYR A 1 365 ? 32.639  -28.832 -21.799 1.00 29.92 ?  377 TYR A CE2 1 
ATOM   2733 C CZ  . TYR A 1 365 ? 31.988  -29.025 -20.591 1.00 34.55 ?  377 TYR A CZ  1 
ATOM   2734 O OH  . TYR A 1 365 ? 32.654  -29.521 -19.489 1.00 38.40 ?  377 TYR A OH  1 
ATOM   2735 N N   . PRO A 1 366 ? 29.933  -24.640 -26.043 1.00 28.74 ?  378 PRO A N   1 
ATOM   2736 C CA  . PRO A 1 366 ? 29.358  -23.976 -27.221 1.00 33.33 ?  378 PRO A CA  1 
ATOM   2737 C C   . PRO A 1 366 ? 29.150  -24.915 -28.399 1.00 33.77 ?  378 PRO A C   1 
ATOM   2738 O O   . PRO A 1 366 ? 28.177  -24.738 -29.134 1.00 33.34 ?  378 PRO A O   1 
ATOM   2739 C CB  . PRO A 1 366 ? 30.399  -22.896 -27.553 1.00 31.39 ?  378 PRO A CB  1 
ATOM   2740 C CG  . PRO A 1 366 ? 31.706  -23.539 -27.116 1.00 33.28 ?  378 PRO A CG  1 
ATOM   2741 C CD  . PRO A 1 366 ? 31.359  -24.310 -25.859 1.00 32.58 ?  378 PRO A CD  1 
ATOM   2742 N N   . ILE A 1 367 ? 30.051  -25.887 -28.600 1.00 30.73 ?  379 ILE A N   1 
ATOM   2743 C CA  . ILE A 1 367 ? 29.959  -26.837 -29.711 1.00 30.58 ?  379 ILE A CA  1 
ATOM   2744 C C   . ILE A 1 367 ? 29.647  -28.207 -29.137 1.00 32.79 ?  379 ILE A C   1 
ATOM   2745 O O   . ILE A 1 367 ? 30.557  -29.007 -28.904 1.00 38.99 ?  379 ILE A O   1 
ATOM   2746 C CB  . ILE A 1 367 ? 31.259  -26.911 -30.539 1.00 37.37 ?  379 ILE A CB  1 
ATOM   2747 C CG1 . ILE A 1 367 ? 31.870  -25.514 -30.797 1.00 34.22 ?  379 ILE A CG1 1 
ATOM   2748 C CG2 . ILE A 1 367 ? 31.036  -27.738 -31.826 1.00 28.82 ?  379 ILE A CG2 1 
ATOM   2749 C CD1 . ILE A 1 367 ? 31.081  -24.651 -31.744 1.00 31.99 ?  379 ILE A CD1 1 
ATOM   2750 N N   . ALA A 1 368 ? 28.371  -28.489 -28.898 1.00 31.75 ?  380 ALA A N   1 
ATOM   2751 C CA  . ALA A 1 368 ? 27.992  -29.702 -28.184 1.00 34.32 ?  380 ALA A CA  1 
ATOM   2752 C C   . ALA A 1 368 ? 26.511  -29.941 -28.416 1.00 27.42 ?  380 ALA A C   1 
ATOM   2753 O O   . ALA A 1 368 ? 25.785  -29.047 -28.849 1.00 30.84 ?  380 ALA A O   1 
ATOM   2754 C CB  . ALA A 1 368 ? 28.292  -29.603 -26.677 1.00 27.21 ?  380 ALA A CB  1 
ATOM   2755 N N   . GLU A 1 369 ? 26.072  -31.157 -28.116 1.00 27.36 ?  381 GLU A N   1 
ATOM   2756 C CA  . GLU A 1 369 ? 24.660  -31.505 -28.128 1.00 29.26 ?  381 GLU A CA  1 
ATOM   2757 C C   . GLU A 1 369 ? 24.372  -32.251 -26.836 1.00 29.30 ?  381 GLU A C   1 
ATOM   2758 O O   . GLU A 1 369 ? 25.261  -32.421 -26.001 1.00 30.58 ?  381 GLU A O   1 
ATOM   2759 C CB  . GLU A 1 369 ? 24.295  -32.317 -29.389 1.00 28.93 ?  381 GLU A CB  1 
ATOM   2760 C CG  . GLU A 1 369 ? 24.059  -31.393 -30.599 1.00 34.69 ?  381 GLU A CG  1 
ATOM   2761 C CD  . GLU A 1 369 ? 23.685  -32.111 -31.896 1.00 39.31 ?  381 GLU A CD  1 
ATOM   2762 O OE1 . GLU A 1 369 ? 24.288  -33.157 -32.239 1.00 36.91 ?  381 GLU A OE1 1 
ATOM   2763 O OE2 . GLU A 1 369 ? 22.773  -31.604 -32.585 1.00 39.87 ?  381 GLU A OE2 1 
ATOM   2764 N N   . HIS A 1 370 ? 23.128  -32.709 -26.662 1.00 29.36 ?  382 HIS A N   1 
ATOM   2765 C CA  . HIS A 1 370 ? 22.779  -33.391 -25.418 1.00 29.48 ?  382 HIS A CA  1 
ATOM   2766 C C   . HIS A 1 370 ? 23.713  -34.563 -25.136 1.00 30.53 ?  382 HIS A C   1 
ATOM   2767 O O   . HIS A 1 370 ? 24.109  -34.789 -23.987 1.00 34.54 ?  382 HIS A O   1 
ATOM   2768 C CB  . HIS A 1 370 ? 21.339  -33.873 -25.472 1.00 26.83 ?  382 HIS A CB  1 
ATOM   2769 C CG  . HIS A 1 370 ? 20.727  -34.111 -24.127 1.00 27.50 ?  382 HIS A CG  1 
ATOM   2770 N ND1 . HIS A 1 370 ? 20.454  -33.093 -23.241 1.00 27.71 ?  382 HIS A ND1 1 
ATOM   2771 C CD2 . HIS A 1 370 ? 20.287  -35.247 -23.537 1.00 26.61 ?  382 HIS A CD2 1 
ATOM   2772 C CE1 . HIS A 1 370 ? 19.893  -33.591 -22.155 1.00 24.94 ?  382 HIS A CE1 1 
ATOM   2773 N NE2 . HIS A 1 370 ? 19.777  -34.898 -22.313 1.00 27.54 ?  382 HIS A NE2 1 
ATOM   2774 N N   . VAL A 1 371 ? 24.101  -35.308 -26.167 1.00 31.97 ?  383 VAL A N   1 
ATOM   2775 C CA  . VAL A 1 371 ? 24.863  -36.527 -25.919 1.00 29.68 ?  383 VAL A CA  1 
ATOM   2776 C C   . VAL A 1 371 ? 26.333  -36.213 -25.724 1.00 30.75 ?  383 VAL A C   1 
ATOM   2777 O O   . VAL A 1 371 ? 26.963  -36.738 -24.803 1.00 31.66 ?  383 VAL A O   1 
ATOM   2778 C CB  . VAL A 1 371 ? 24.662  -37.556 -27.050 1.00 31.93 ?  383 VAL A CB  1 
ATOM   2779 C CG1 . VAL A 1 371 ? 25.741  -38.665 -26.950 1.00 28.03 ?  383 VAL A CG1 1 
ATOM   2780 C CG2 . VAL A 1 371 ? 23.252  -38.155 -26.979 1.00 33.71 ?  383 VAL A CG2 1 
ATOM   2781 N N   . THR A 1 372 ? 26.912  -35.379 -26.598 1.00 30.25 ?  384 THR A N   1 
ATOM   2782 C CA  . THR A 1 372 ? 28.331  -35.054 -26.451 1.00 31.02 ?  384 THR A CA  1 
ATOM   2783 C C   . THR A 1 372 ? 28.605  -34.343 -25.123 1.00 34.91 ?  384 THR A C   1 
ATOM   2784 O O   . THR A 1 372 ? 29.593  -34.655 -24.442 1.00 34.75 ?  384 THR A O   1 
ATOM   2785 C CB  . THR A 1 372 ? 28.815  -34.222 -27.640 1.00 26.99 ?  384 THR A CB  1 
ATOM   2786 O OG1 . THR A 1 372 ? 27.841  -33.220 -27.972 1.00 31.82 ?  384 THR A OG1 1 
ATOM   2787 C CG2 . THR A 1 372 ? 29.014  -35.116 -28.835 1.00 26.12 ?  384 THR A CG2 1 
ATOM   2788 N N   . ALA A 1 373 ? 27.716  -33.421 -24.710 1.00 30.70 ?  385 ALA A N   1 
ATOM   2789 C CA  . ALA A 1 373 ? 27.882  -32.757 -23.416 1.00 35.40 ?  385 ALA A CA  1 
ATOM   2790 C C   . ALA A 1 373 ? 27.764  -33.729 -22.256 1.00 34.28 ?  385 ALA A C   1 
ATOM   2791 O O   . ALA A 1 373 ? 28.249  -33.420 -21.162 1.00 36.40 ?  385 ALA A O   1 
ATOM   2792 C CB  . ALA A 1 373 ? 26.861  -31.622 -23.223 1.00 27.85 ?  385 ALA A CB  1 
ATOM   2793 N N   . GLU A 1 374 ? 27.120  -34.879 -22.467 1.00 32.27 ?  386 GLU A N   1 
ATOM   2794 C CA  . GLU A 1 374 ? 27.022  -35.882 -21.406 1.00 33.21 ?  386 GLU A CA  1 
ATOM   2795 C C   . GLU A 1 374 ? 28.398  -36.381 -20.998 1.00 31.41 ?  386 GLU A C   1 
ATOM   2796 O O   . GLU A 1 374 ? 28.618  -36.699 -19.823 1.00 31.93 ?  386 GLU A O   1 
ATOM   2797 C CB  . GLU A 1 374 ? 26.143  -37.059 -21.854 1.00 25.07 ?  386 GLU A CB  1 
ATOM   2798 C CG  . GLU A 1 374 ? 26.140  -38.250 -20.900 1.00 28.58 ?  386 GLU A CG  1 
ATOM   2799 C CD  . GLU A 1 374 ? 25.171  -39.372 -21.346 1.00 35.69 ?  386 GLU A CD  1 
ATOM   2800 O OE1 . GLU A 1 374 ? 24.679  -39.340 -22.499 1.00 32.19 ?  386 GLU A OE1 1 
ATOM   2801 O OE2 . GLU A 1 374 ? 24.900  -40.289 -20.549 1.00 32.63 ?  386 GLU A OE2 1 
ATOM   2802 N N   . ILE A 1 375 ? 29.332  -36.453 -21.943 1.00 29.66 ?  387 ILE A N   1 
ATOM   2803 C CA  . ILE A 1 375 ? 30.709  -36.820 -21.615 1.00 34.68 ?  387 ILE A CA  1 
ATOM   2804 C C   . ILE A 1 375 ? 31.556  -35.584 -21.305 1.00 35.02 ?  387 ILE A C   1 
ATOM   2805 O O   . ILE A 1 375 ? 32.353  -35.606 -20.366 1.00 35.15 ?  387 ILE A O   1 
ATOM   2806 C CB  . ILE A 1 375 ? 31.339  -37.653 -22.761 1.00 30.76 ?  387 ILE A CB  1 
ATOM   2807 C CG1 . ILE A 1 375 ? 30.509  -38.912 -23.064 1.00 35.29 ?  387 ILE A CG1 1 
ATOM   2808 C CG2 . ILE A 1 375 ? 32.783  -38.027 -22.430 1.00 34.40 ?  387 ILE A CG2 1 
ATOM   2809 C CD1 . ILE A 1 375 ? 30.272  -39.816 -21.862 1.00 31.45 ?  387 ILE A CD1 1 
ATOM   2810 N N   . PHE A 1 376 ? 31.395  -34.503 -22.090 1.00 32.86 ?  388 PHE A N   1 
ATOM   2811 C CA  . PHE A 1 376 ? 32.275  -33.338 -21.978 1.00 36.13 ?  388 PHE A CA  1 
ATOM   2812 C C   . PHE A 1 376 ? 32.444  -32.907 -20.519 1.00 38.00 ?  388 PHE A C   1 
ATOM   2813 O O   . PHE A 1 376 ? 33.566  -32.718 -20.041 1.00 37.00 ?  388 PHE A O   1 
ATOM   2814 C CB  . PHE A 1 376 ? 31.732  -32.168 -22.806 1.00 31.79 ?  388 PHE A CB  1 
ATOM   2815 C CG  . PHE A 1 376 ? 31.938  -32.309 -24.303 1.00 37.81 ?  388 PHE A CG  1 
ATOM   2816 C CD1 . PHE A 1 376 ? 32.839  -33.224 -24.821 1.00 33.34 ?  388 PHE A CD1 1 
ATOM   2817 C CD2 . PHE A 1 376 ? 31.210  -31.517 -25.191 1.00 37.26 ?  388 PHE A CD2 1 
ATOM   2818 C CE1 . PHE A 1 376 ? 33.018  -33.347 -26.183 1.00 39.09 ?  388 PHE A CE1 1 
ATOM   2819 C CE2 . PHE A 1 376 ? 31.389  -31.641 -26.575 1.00 36.60 ?  388 PHE A CE2 1 
ATOM   2820 C CZ  . PHE A 1 376 ? 32.292  -32.567 -27.064 1.00 34.60 ?  388 PHE A CZ  1 
ATOM   2821 N N   . GLY A 1 377 ? 31.336  -32.774 -19.794 1.00 33.67 ?  389 GLY A N   1 
ATOM   2822 C CA  . GLY A 1 377 ? 31.349  -32.318 -18.425 1.00 34.50 ?  389 GLY A CA  1 
ATOM   2823 C C   . GLY A 1 377 ? 31.394  -33.411 -17.384 1.00 33.22 ?  389 GLY A C   1 
ATOM   2824 O O   . GLY A 1 377 ? 31.234  -33.113 -16.194 1.00 33.24 ?  389 GLY A O   1 
ATOM   2825 N N   . LEU A 1 378 ? 31.611  -34.660 -17.804 1.00 33.52 ?  390 LEU A N   1 
ATOM   2826 C CA  . LEU A 1 378 ? 31.654  -35.790 -16.877 1.00 35.18 ?  390 LEU A CA  1 
ATOM   2827 C C   . LEU A 1 378 ? 32.875  -35.714 -15.957 1.00 32.78 ?  390 LEU A C   1 
ATOM   2828 O O   . LEU A 1 378 ? 32.751  -35.802 -14.727 1.00 28.08 ?  390 LEU A O   1 
ATOM   2829 C CB  . LEU A 1 378 ? 31.657  -37.103 -17.673 1.00 32.26 ?  390 LEU A CB  1 
ATOM   2830 C CG  . LEU A 1 378 ? 31.552  -38.445 -16.936 1.00 35.18 ?  390 LEU A CG  1 
ATOM   2831 C CD1 . LEU A 1 378 ? 31.036  -39.511 -17.902 1.00 35.40 ?  390 LEU A CD1 1 
ATOM   2832 C CD2 . LEU A 1 378 ? 32.868  -38.895 -16.313 1.00 26.55 ?  390 LEU A CD2 1 
ATOM   2833 N N   . VAL A 1 379 ? 34.068  -35.612 -16.541 1.00 33.87 ?  391 VAL A N   1 
ATOM   2834 C CA  . VAL A 1 379 ? 35.314  -35.656 -15.772 1.00 34.85 ?  391 VAL A CA  1 
ATOM   2835 C C   . VAL A 1 379 ? 35.450  -34.389 -14.924 1.00 33.03 ?  391 VAL A C   1 
ATOM   2836 O O   . VAL A 1 379 ? 35.718  -34.499 -13.720 1.00 36.17 ?  391 VAL A O   1 
ATOM   2837 C CB  . VAL A 1 379 ? 36.533  -35.879 -16.690 1.00 38.13 ?  391 VAL A CB  1 
ATOM   2838 C CG1 . VAL A 1 379 ? 37.829  -35.596 -15.953 1.00 39.84 ?  391 VAL A CG1 1 
ATOM   2839 C CG2 . VAL A 1 379 ? 36.541  -37.297 -17.233 1.00 35.41 ?  391 VAL A CG2 1 
ATOM   2840 N N   . PRO A 1 380 ? 35.249  -33.182 -15.462 1.00 31.99 ?  392 PRO A N   1 
ATOM   2841 C CA  . PRO A 1 380 ? 35.257  -32.005 -14.575 1.00 30.50 ?  392 PRO A CA  1 
ATOM   2842 C C   . PRO A 1 380 ? 34.279  -32.100 -13.414 1.00 34.48 ?  392 PRO A C   1 
ATOM   2843 O O   . PRO A 1 380 ? 34.609  -31.695 -12.287 1.00 32.88 ?  392 PRO A O   1 
ATOM   2844 C CB  . PRO A 1 380 ? 34.898  -30.861 -15.530 1.00 35.72 ?  392 PRO A CB  1 
ATOM   2845 C CG  . PRO A 1 380 ? 35.421  -31.294 -16.843 1.00 34.74 ?  392 PRO A CG  1 
ATOM   2846 C CD  . PRO A 1 380 ? 35.188  -32.783 -16.886 1.00 34.83 ?  392 PRO A CD  1 
ATOM   2847 N N   . GLY A 1 381 ? 33.080  -32.634 -13.654 1.00 32.71 ?  393 GLY A N   1 
ATOM   2848 C CA  . GLY A 1 381 ? 32.095  -32.727 -12.584 1.00 28.96 ?  393 GLY A CA  1 
ATOM   2849 C C   . GLY A 1 381 ? 32.494  -33.688 -11.477 1.00 31.99 ?  393 GLY A C   1 
ATOM   2850 O O   . GLY A 1 381 ? 32.232  -33.434 -10.295 1.00 32.92 ?  393 GLY A O   1 
ATOM   2851 N N   . LEU A 1 382 ? 33.128  -34.802 -11.837 1.00 30.17 ?  394 LEU A N   1 
ATOM   2852 C CA  . LEU A 1 382 ? 33.595  -35.730 -10.813 1.00 33.32 ?  394 LEU A CA  1 
ATOM   2853 C C   . LEU A 1 382 ? 34.795  -35.152 -10.069 1.00 37.62 ?  394 LEU A C   1 
ATOM   2854 O O   . LEU A 1 382 ? 34.908  -35.310 -8.845  1.00 31.23 ?  394 LEU A O   1 
ATOM   2855 C CB  . LEU A 1 382 ? 33.947  -37.086 -11.439 1.00 34.02 ?  394 LEU A CB  1 
ATOM   2856 C CG  . LEU A 1 382 ? 32.830  -37.960 -12.056 1.00 35.80 ?  394 LEU A CG  1 
ATOM   2857 C CD1 . LEU A 1 382 ? 33.401  -39.302 -12.535 1.00 32.42 ?  394 LEU A CD1 1 
ATOM   2858 C CD2 . LEU A 1 382 ? 31.689  -38.178 -11.096 1.00 25.50 ?  394 LEU A CD2 1 
ATOM   2859 N N   . ASP A 1 383 ? 35.705  -34.494 -10.801 1.00 36.51 ?  395 ASP A N   1 
ATOM   2860 C CA  . ASP A 1 383 ? 36.798  -33.768 -10.167 1.00 36.54 ?  395 ASP A CA  1 
ATOM   2861 C C   . ASP A 1 383 ? 36.249  -32.776 -9.158  1.00 36.66 ?  395 ASP A C   1 
ATOM   2862 O O   . ASP A 1 383 ? 36.666  -32.752 -7.993  1.00 39.40 ?  395 ASP A O   1 
ATOM   2863 C CB  . ASP A 1 383 ? 37.630  -33.049 -11.224 1.00 34.53 ?  395 ASP A CB  1 
ATOM   2864 C CG  . ASP A 1 383 ? 38.758  -32.216 -10.621 1.00 41.78 ?  395 ASP A CG  1 
ATOM   2865 O OD1 . ASP A 1 383 ? 39.685  -32.790 -10.013 1.00 42.27 ?  395 ASP A OD1 1 
ATOM   2866 O OD2 . ASP A 1 383 ? 38.716  -30.978 -10.765 1.00 49.29 ?  395 ASP A OD2 1 
ATOM   2867 N N   . PHE A 1 384 ? 35.274  -31.975 -9.593  1.00 33.56 ?  396 PHE A N   1 
ATOM   2868 C CA  . PHE A 1 384 ? 34.614  -31.028 -8.708  1.00 32.24 ?  396 PHE A CA  1 
ATOM   2869 C C   . PHE A 1 384 ? 34.055  -31.714 -7.468  1.00 35.53 ?  396 PHE A C   1 
ATOM   2870 O O   . PHE A 1 384 ? 34.113  -31.159 -6.366  1.00 36.28 ?  396 PHE A O   1 
ATOM   2871 C CB  . PHE A 1 384 ? 33.500  -30.307 -9.472  1.00 28.84 ?  396 PHE A CB  1 
ATOM   2872 C CG  . PHE A 1 384 ? 32.631  -29.448 -8.606  1.00 31.53 ?  396 PHE A CG  1 
ATOM   2873 C CD1 . PHE A 1 384 ? 31.561  -29.987 -7.910  1.00 32.93 ?  396 PHE A CD1 1 
ATOM   2874 C CD2 . PHE A 1 384 ? 32.878  -28.084 -8.490  1.00 33.50 ?  396 PHE A CD2 1 
ATOM   2875 C CE1 . PHE A 1 384 ? 30.746  -29.185 -7.080  1.00 35.93 ?  396 PHE A CE1 1 
ATOM   2876 C CE2 . PHE A 1 384 ? 32.063  -27.276 -7.685  1.00 33.39 ?  396 PHE A CE2 1 
ATOM   2877 C CZ  . PHE A 1 384 ? 30.993  -27.829 -6.979  1.00 32.32 ?  396 PHE A CZ  1 
ATOM   2878 N N   . LEU A 1 385 ? 33.465  -32.903 -7.632  1.00 33.09 ?  397 LEU A N   1 
ATOM   2879 C CA  . LEU A 1 385 ? 32.871  -33.572 -6.484  1.00 34.31 ?  397 LEU A CA  1 
ATOM   2880 C C   . LEU A 1 385 ? 33.955  -34.108 -5.558  1.00 35.88 ?  397 LEU A C   1 
ATOM   2881 O O   . LEU A 1 385 ? 33.765  -34.148 -4.337  1.00 31.31 ?  397 LEU A O   1 
ATOM   2882 C CB  . LEU A 1 385 ? 31.935  -34.705 -6.936  1.00 36.22 ?  397 LEU A CB  1 
ATOM   2883 C CG  . LEU A 1 385 ? 30.511  -34.392 -7.445  1.00 39.52 ?  397 LEU A CG  1 
ATOM   2884 C CD1 . LEU A 1 385 ? 29.734  -35.683 -7.802  1.00 30.46 ?  397 LEU A CD1 1 
ATOM   2885 C CD2 . LEU A 1 385 ? 29.704  -33.514 -6.479  1.00 25.13 ?  397 LEU A CD2 1 
ATOM   2886 N N   . SER A 1 386 ? 35.097  -34.513 -6.116  1.00 33.87 ?  398 SER A N   1 
ATOM   2887 C CA  . SER A 1 386 ? 36.218  -34.892 -5.267  1.00 40.08 ?  398 SER A CA  1 
ATOM   2888 C C   . SER A 1 386 ? 36.665  -33.714 -4.414  1.00 36.68 ?  398 SER A C   1 
ATOM   2889 O O   . SER A 1 386 ? 36.914  -33.871 -3.216  1.00 41.67 ?  398 SER A O   1 
ATOM   2890 C CB  . SER A 1 386 ? 37.372  -35.418 -6.119  1.00 40.95 ?  398 SER A CB  1 
ATOM   2891 O OG  . SER A 1 386 ? 38.552  -35.571 -5.354  1.00 46.48 ?  398 SER A OG  1 
ATOM   2892 N N   . LYS A 1 387 ? 36.732  -32.519 -5.008  1.00 37.92 ?  399 LYS A N   1 
ATOM   2893 C CA  . LYS A 1 387 ? 37.107  -31.320 -4.258  1.00 37.05 ?  399 LYS A CA  1 
ATOM   2894 C C   . LYS A 1 387 ? 36.034  -30.947 -3.234  1.00 37.57 ?  399 LYS A C   1 
ATOM   2895 O O   . LYS A 1 387 ? 36.355  -30.560 -2.105  1.00 38.09 ?  399 LYS A O   1 
ATOM   2896 C CB  . LYS A 1 387 ? 37.381  -30.164 -5.229  1.00 32.72 ?  399 LYS A CB  1 
ATOM   2897 C CG  . LYS A 1 387 ? 38.792  -30.190 -5.827  1.00 34.95 ?  399 LYS A CG  1 
ATOM   2898 C CD  . LYS A 1 387 ? 38.846  -29.739 -7.273  1.00 42.89 ?  399 LYS A CD  1 
ATOM   2899 C CE  . LYS A 1 387 ? 40.199  -30.115 -7.913  1.00 51.55 ?  399 LYS A CE  1 
ATOM   2900 N NZ  . LYS A 1 387 ? 40.508  -29.447 -9.247  1.00 53.88 ?  399 LYS A NZ  1 
ATOM   2901 N N   . ALA A 1 388 ? 34.757  -31.089 -3.594  1.00 36.05 ?  400 ALA A N   1 
ATOM   2902 C CA  . ALA A 1 388 ? 33.681  -30.756 -2.664  1.00 36.72 ?  400 ALA A CA  1 
ATOM   2903 C C   . ALA A 1 388 ? 33.711  -31.644 -1.433  1.00 38.38 ?  400 ALA A C   1 
ATOM   2904 O O   . ALA A 1 388 ? 33.382  -31.189 -0.329  1.00 35.56 ?  400 ALA A O   1 
ATOM   2905 C CB  . ALA A 1 388 ? 32.324  -30.872 -3.362  1.00 33.63 ?  400 ALA A CB  1 
ATOM   2906 N N   . PHE A 1 389 ? 34.092  -32.913 -1.605  1.00 35.29 ?  401 PHE A N   1 
ATOM   2907 C CA  . PHE A 1 389 ? 34.202  -33.816 -0.474  1.00 40.79 ?  401 PHE A CA  1 
ATOM   2908 C C   . PHE A 1 389 ? 35.339  -33.419 0.456   1.00 41.03 ?  401 PHE A C   1 
ATOM   2909 O O   . PHE A 1 389 ? 35.309  -33.781 1.634   1.00 40.40 ?  401 PHE A O   1 
ATOM   2910 C CB  . PHE A 1 389 ? 34.388  -35.252 -0.968  1.00 40.95 ?  401 PHE A CB  1 
ATOM   2911 C CG  . PHE A 1 389 ? 33.117  -35.896 -1.420  1.00 36.04 ?  401 PHE A CG  1 
ATOM   2912 C CD1 . PHE A 1 389 ? 31.957  -35.756 -0.670  1.00 39.51 ?  401 PHE A CD1 1 
ATOM   2913 C CD2 . PHE A 1 389 ? 33.074  -36.628 -2.595  1.00 35.29 ?  401 PHE A CD2 1 
ATOM   2914 C CE1 . PHE A 1 389 ? 30.773  -36.340 -1.084  1.00 40.06 ?  401 PHE A CE1 1 
ATOM   2915 C CE2 . PHE A 1 389 ? 31.911  -37.208 -3.017  1.00 40.67 ?  401 PHE A CE2 1 
ATOM   2916 C CZ  . PHE A 1 389 ? 30.746  -37.065 -2.265  1.00 41.43 ?  401 PHE A CZ  1 
ATOM   2917 N N   . LYS A 1 390 ? 36.326  -32.681 -0.053  1.00 41.08 ?  402 LYS A N   1 
ATOM   2918 C CA  . LYS A 1 390 ? 37.435  -32.149 0.722   1.00 39.24 ?  402 LYS A CA  1 
ATOM   2919 C C   . LYS A 1 390 ? 37.225  -30.691 1.132   1.00 43.74 ?  402 LYS A C   1 
ATOM   2920 O O   . LYS A 1 390 ? 38.169  -30.055 1.609   1.00 43.62 ?  402 LYS A O   1 
ATOM   2921 C CB  . LYS A 1 390 ? 38.728  -32.265 -0.087  1.00 42.19 ?  402 LYS A CB  1 
ATOM   2922 C CG  . LYS A 1 390 ? 39.213  -33.668 -0.256  1.00 47.47 ?  402 LYS A CG  1 
ATOM   2923 C CD  . LYS A 1 390 ? 39.956  -33.873 -1.554  1.00 48.23 ?  402 LYS A CD  1 
ATOM   2924 C CE  . LYS A 1 390 ? 39.881  -35.360 -1.937  1.00 52.59 ?  402 LYS A CE  1 
ATOM   2925 N NZ  . LYS A 1 390 ? 40.840  -35.779 -3.025  1.00 47.97 ?  402 LYS A NZ  1 
ATOM   2926 N N   . GLY A 1 391 ? 36.026  -30.146 0.939   1.00 43.77 ?  403 GLY A N   1 
ATOM   2927 C CA  . GLY A 1 391 ? 35.817  -28.715 1.161   1.00 44.42 ?  403 GLY A CA  1 
ATOM   2928 C C   . GLY A 1 391 ? 36.767  -27.827 0.385   1.00 42.36 ?  403 GLY A C   1 
ATOM   2929 O O   . GLY A 1 391 ? 37.191  -26.784 0.891   1.00 47.28 ?  403 GLY A O   1 
ATOM   2930 N N   . GLN A 1 392 ? 37.100  -28.208 -0.849  1.00 38.17 ?  404 GLN A N   1 
ATOM   2931 C CA  . GLN A 1 392 ? 38.101  -27.496 -1.628  1.00 40.12 ?  404 GLN A CA  1 
ATOM   2932 C C   . GLN A 1 392 ? 37.613  -27.118 -3.028  1.00 39.61 ?  404 GLN A C   1 
ATOM   2933 O O   . GLN A 1 392 ? 38.425  -26.992 -3.952  1.00 39.67 ?  404 GLN A O   1 
ATOM   2934 C CB  . GLN A 1 392 ? 39.380  -28.322 -1.723  1.00 43.59 ?  404 GLN A CB  1 
ATOM   2935 C CG  . GLN A 1 392 ? 40.203  -28.256 -0.465  1.00 48.02 ?  404 GLN A CG  1 
ATOM   2936 C CD  . GLN A 1 392 ? 41.229  -29.346 -0.393  1.00 51.17 ?  404 GLN A CD  1 
ATOM   2937 O OE1 . GLN A 1 392 ? 41.542  -29.991 -1.394  1.00 55.00 ?  404 GLN A OE1 1 
ATOM   2938 N NE2 . GLN A 1 392 ? 41.765  -29.567 0.802   1.00 60.81 ?  404 GLN A NE2 1 
ATOM   2939 N N   . THR A 1 393 ? 36.309  -26.922 -3.215  1.00 36.92 ?  405 THR A N   1 
ATOM   2940 C CA  . THR A 1 393 ? 35.844  -26.452 -4.514  1.00 39.22 ?  405 THR A CA  1 
ATOM   2941 C C   . THR A 1 393 ? 36.415  -25.065 -4.770  1.00 41.38 ?  405 THR A C   1 
ATOM   2942 O O   . THR A 1 393 ? 36.530  -24.265 -3.834  1.00 45.35 ?  405 THR A O   1 
ATOM   2943 C CB  . THR A 1 393 ? 34.317  -26.384 -4.583  1.00 40.77 ?  405 THR A CB  1 
ATOM   2944 O OG1 . THR A 1 393 ? 33.819  -25.545 -3.530  1.00 32.63 ?  405 THR A OG1 1 
ATOM   2945 C CG2 . THR A 1 393 ? 33.704  -27.790 -4.495  1.00 35.77 ?  405 THR A CG2 1 
ATOM   2946 N N   . PRO A 1 394 ? 36.773  -24.738 -6.006  1.00 38.77 ?  406 PRO A N   1 
ATOM   2947 C CA  . PRO A 1 394 ? 37.342  -23.413 -6.266  1.00 34.62 ?  406 PRO A CA  1 
ATOM   2948 C C   . PRO A 1 394 ? 36.301  -22.320 -6.088  1.00 38.16 ?  406 PRO A C   1 
ATOM   2949 O O   . PRO A 1 394 ? 35.088  -22.547 -6.128  1.00 35.92 ?  406 PRO A O   1 
ATOM   2950 C CB  . PRO A 1 394 ? 37.816  -23.506 -7.721  1.00 35.03 ?  406 PRO A CB  1 
ATOM   2951 C CG  . PRO A 1 394 ? 36.872  -24.498 -8.337  1.00 38.89 ?  406 PRO A CG  1 
ATOM   2952 C CD  . PRO A 1 394 ? 36.584  -25.512 -7.249  1.00 37.62 ?  406 PRO A CD  1 
ATOM   2953 N N   . LYS A 1 395 ? 36.797  -21.106 -5.872  1.00 39.65 ?  407 LYS A N   1 
ATOM   2954 C CA  . LYS A 1 395 ? 35.904  -19.964 -5.802  1.00 42.35 ?  407 LYS A CA  1 
ATOM   2955 C C   . LYS A 1 395 ? 35.586  -19.494 -7.221  1.00 38.47 ?  407 LYS A C   1 
ATOM   2956 O O   . LYS A 1 395 ? 36.483  -19.368 -8.061  1.00 39.58 ?  407 LYS A O   1 
ATOM   2957 C CB  . LYS A 1 395 ? 36.524  -18.843 -4.963  1.00 38.98 ?  407 LYS A CB  1 
ATOM   2958 C CG  . LYS A 1 395 ? 35.533  -17.713 -4.633  1.00 51.74 ?  407 LYS A CG  1 
ATOM   2959 C CD  . LYS A 1 395 ? 34.978  -17.766 -3.181  1.00 56.02 ?  407 LYS A CD  1 
ATOM   2960 C CE  . LYS A 1 395 ? 33.801  -16.764 -2.948  1.00 52.87 ?  407 LYS A CE  1 
ATOM   2961 N NZ  . LYS A 1 395 ? 32.783  -16.725 -4.071  1.00 51.65 ?  407 LYS A NZ  1 
ATOM   2962 N N   . VAL A 1 396 ? 34.301  -19.283 -7.494  1.00 34.70 ?  408 VAL A N   1 
ATOM   2963 C CA  . VAL A 1 396 ? 33.832  -18.752 -8.768  1.00 35.57 ?  408 VAL A CA  1 
ATOM   2964 C C   . VAL A 1 396 ? 32.758  -17.726 -8.489  1.00 32.29 ?  408 VAL A C   1 
ATOM   2965 O O   . VAL A 1 396 ? 32.007  -17.833 -7.515  1.00 30.84 ?  408 VAL A O   1 
ATOM   2966 C CB  . VAL A 1 396 ? 33.228  -19.811 -9.720  1.00 33.76 ?  408 VAL A CB  1 
ATOM   2967 C CG1 . VAL A 1 396 ? 34.308  -20.667 -10.336 1.00 39.02 ?  408 VAL A CG1 1 
ATOM   2968 C CG2 . VAL A 1 396 ? 32.155  -20.644 -8.984  1.00 28.15 ?  408 VAL A CG2 1 
ATOM   2969 N N   . ALA A 1 397 ? 32.671  -16.747 -9.378  1.00 27.70 ?  409 ALA A N   1 
ATOM   2970 C CA  . ALA A 1 397 ? 31.474  -15.931 -9.451  1.00 32.41 ?  409 ALA A CA  1 
ATOM   2971 C C   . ALA A 1 397 ? 30.305  -16.808 -9.884  1.00 33.60 ?  409 ALA A C   1 
ATOM   2972 O O   . ALA A 1 397 ? 30.378  -17.502 -10.905 1.00 34.46 ?  409 ALA A O   1 
ATOM   2973 C CB  . ALA A 1 397 ? 31.674  -14.780 -10.438 1.00 31.67 ?  409 ALA A CB  1 
ATOM   2974 N N   . CYS A 1 398 ? 29.239  -16.778 -9.095  1.00 32.61 ?  410 CYS A N   1 
ATOM   2975 C CA  . CYS A 1 398 ? 28.092  -17.640 -9.320  1.00 33.30 ?  410 CYS A CA  1 
ATOM   2976 C C   . CYS A 1 398 ? 27.535  -17.429 -10.720 1.00 38.22 ?  410 CYS A C   1 
ATOM   2977 O O   . CYS A 1 398 ? 27.216  -16.306 -11.111 1.00 37.88 ?  410 CYS A O   1 
ATOM   2978 C CB  . CYS A 1 398 ? 27.014  -17.359 -8.275  1.00 33.09 ?  410 CYS A CB  1 
ATOM   2979 S SG  . CYS A 1 398 ? 25.636  -18.535 -8.322  1.00 32.94 ?  410 CYS A SG  1 
ATOM   2980 N N   . GLY A 1 399 ? 27.375  -18.523 -11.458 1.00 37.16 ?  411 GLY A N   1 
ATOM   2981 C CA  . GLY A 1 399 ? 26.918  -18.443 -12.824 1.00 36.56 ?  411 GLY A CA  1 
ATOM   2982 C C   . GLY A 1 399 ? 28.026  -18.321 -13.838 1.00 36.58 ?  411 GLY A C   1 
ATOM   2983 O O   . GLY A 1 399 ? 27.744  -18.074 -15.012 1.00 36.02 ?  411 GLY A O   1 
ATOM   2984 N N   . SER A 1 400 ? 29.276  -18.458 -13.418 1.00 33.93 ?  412 SER A N   1 
ATOM   2985 C CA  . SER A 1 400 ? 30.418  -18.469 -14.316 1.00 38.00 ?  412 SER A CA  1 
ATOM   2986 C C   . SER A 1 400 ? 31.274  -19.665 -13.953 1.00 31.39 ?  412 SER A C   1 
ATOM   2987 O O   . SER A 1 400 ? 30.991  -20.374 -12.985 1.00 35.50 ?  412 SER A O   1 
ATOM   2988 C CB  . SER A 1 400 ? 31.252  -17.177 -14.227 1.00 41.09 ?  412 SER A CB  1 
ATOM   2989 O OG  . SER A 1 400 ? 30.454  -16.009 -14.229 1.00 38.68 ?  412 SER A OG  1 
ATOM   2990 N N   . GLY A 1 401 ? 32.328  -19.883 -14.743 1.00 30.87 ?  413 GLY A N   1 
ATOM   2991 C CA  . GLY A 1 401 ? 33.366  -20.831 -14.408 1.00 31.10 ?  413 GLY A CA  1 
ATOM   2992 C C   . GLY A 1 401 ? 34.575  -20.099 -13.844 1.00 38.62 ?  413 GLY A C   1 
ATOM   2993 O O   . GLY A 1 401 ? 34.615  -18.874 -13.778 1.00 39.03 ?  413 GLY A O   1 
ATOM   2994 N N   . VAL A 1 402 ? 35.549  -20.882 -13.390 1.00 41.00 ?  414 VAL A N   1 
ATOM   2995 C CA  . VAL A 1 402 ? 36.821  -20.291 -12.963 1.00 40.66 ?  414 VAL A CA  1 
ATOM   2996 C C   . VAL A 1 402 ? 37.390  -19.474 -14.116 1.00 43.84 ?  414 VAL A C   1 
ATOM   2997 O O   . VAL A 1 402 ? 37.465  -19.981 -15.253 1.00 47.60 ?  414 VAL A O   1 
ATOM   2998 C CB  . VAL A 1 402 ? 37.812  -21.385 -12.531 1.00 39.46 ?  414 VAL A CB  1 
ATOM   2999 C CG1 . VAL A 1 402 ? 39.146  -20.777 -12.226 1.00 45.31 ?  414 VAL A CG1 1 
ATOM   3000 C CG2 . VAL A 1 402 ? 37.299  -22.150 -11.330 1.00 41.32 ?  414 VAL A CG2 1 
ATOM   3001 N N   . PRO A 1 403 ? 37.790  -18.216 -13.906 1.00 43.04 ?  415 PRO A N   1 
ATOM   3002 C CA  . PRO A 1 403 ? 38.355  -17.448 -15.021 1.00 39.89 ?  415 PRO A CA  1 
ATOM   3003 C C   . PRO A 1 403 ? 39.765  -17.903 -15.339 1.00 38.90 ?  415 PRO A C   1 
ATOM   3004 O O   . PRO A 1 403 ? 40.340  -18.738 -14.632 1.00 40.38 ?  415 PRO A O   1 
ATOM   3005 C CB  . PRO A 1 403 ? 38.340  -16.002 -14.506 1.00 41.56 ?  415 PRO A CB  1 
ATOM   3006 C CG  . PRO A 1 403 ? 38.204  -16.107 -13.001 1.00 40.64 ?  415 PRO A CG  1 
ATOM   3007 C CD  . PRO A 1 403 ? 38.028  -17.554 -12.613 1.00 38.63 ?  415 PRO A CD  1 
ATOM   3008 N N   . ALA A 1 404 ? 40.339  -17.330 -16.387 1.00 43.16 ?  416 ALA A N   1 
ATOM   3009 C CA  . ALA A 1 404 ? 41.643  -17.780 -16.856 1.00 47.96 ?  416 ALA A CA  1 
ATOM   3010 C C   . ALA A 1 404 ? 42.712  -17.423 -15.832 1.00 45.49 ?  416 ALA A C   1 
ATOM   3011 O O   . ALA A 1 404 ? 42.773  -16.283 -15.366 1.00 48.81 ?  416 ALA A O   1 
ATOM   3012 C CB  . ALA A 1 404 ? 41.953  -17.162 -18.220 1.00 37.36 ?  416 ALA A CB  1 
ATOM   3013 N N   . ILE A 1 405 ? 43.527  -18.409 -15.453 1.00 47.74 ?  417 ILE A N   1 
ATOM   3014 C CA  . ILE A 1 405 ? 44.570  -18.244 -14.438 1.00 49.11 ?  417 ILE A CA  1 
ATOM   3015 C C   . ILE A 1 405 ? 45.857  -18.919 -14.901 1.00 52.33 ?  417 ILE A C   1 
ATOM   3016 O O   . ILE A 1 405 ? 45.888  -20.149 -15.032 1.00 52.78 ?  417 ILE A O   1 
ATOM   3017 C CB  . ILE A 1 405 ? 44.136  -18.822 -13.085 1.00 51.17 ?  417 ILE A CB  1 
ATOM   3018 C CG1 . ILE A 1 405 ? 42.912  -18.091 -12.542 1.00 49.64 ?  417 ILE A CG1 1 
ATOM   3019 C CG2 . ILE A 1 405 ? 45.289  -18.769 -12.101 1.00 51.90 ?  417 ILE A CG2 1 
ATOM   3020 C CD1 . ILE A 1 405 ? 42.149  -18.912 -11.503 1.00 45.53 ?  417 ILE A CD1 1 
ATOM   3021 N N   . PRO A 1 406 ? 46.933  -18.169 -15.151 1.00 53.88 ?  418 PRO A N   1 
ATOM   3022 C CA  . PRO A 1 406 ? 48.176  -18.785 -15.636 1.00 50.33 ?  418 PRO A CA  1 
ATOM   3023 C C   . PRO A 1 406 ? 48.665  -19.888 -14.712 1.00 55.49 ?  418 PRO A C   1 
ATOM   3024 O O   . PRO A 1 406 ? 48.534  -19.801 -13.488 1.00 57.15 ?  418 PRO A O   1 
ATOM   3025 C CB  . PRO A 1 406 ? 49.154  -17.609 -15.682 1.00 46.37 ?  418 PRO A CB  1 
ATOM   3026 C CG  . PRO A 1 406 ? 48.268  -16.446 -15.986 1.00 45.60 ?  418 PRO A CG  1 
ATOM   3027 C CD  . PRO A 1 406 ? 46.993  -16.698 -15.216 1.00 45.78 ?  418 PRO A CD  1 
ATOM   3028 N N   . GLY A 1 407 ? 49.203  -20.949 -15.323 1.00 52.33 ?  419 GLY A N   1 
ATOM   3029 C CA  . GLY A 1 407 ? 49.662  -22.121 -14.603 1.00 52.98 ?  419 GLY A CA  1 
ATOM   3030 C C   . GLY A 1 407 ? 48.585  -23.021 -14.027 1.00 56.56 ?  419 GLY A C   1 
ATOM   3031 O O   . GLY A 1 407 ? 48.912  -24.111 -13.542 1.00 59.89 ?  419 GLY A O   1 
ATOM   3032 N N   . ILE A 1 408 ? 47.315  -22.624 -14.057 1.00 54.05 ?  420 ILE A N   1 
ATOM   3033 C CA  . ILE A 1 408 ? 46.245  -23.372 -13.406 1.00 60.07 ?  420 ILE A CA  1 
ATOM   3034 C C   . ILE A 1 408 ? 45.210  -23.872 -14.411 1.00 60.45 ?  420 ILE A C   1 
ATOM   3035 O O   . ILE A 1 408 ? 44.848  -25.053 -14.415 1.00 62.53 ?  420 ILE A O   1 
ATOM   3036 C CB  . ILE A 1 408 ? 45.576  -22.536 -12.289 1.00 65.28 ?  420 ILE A CB  1 
ATOM   3037 C CG1 . ILE A 1 408 ? 46.476  -22.545 -11.045 1.00 65.48 ?  420 ILE A CG1 1 
ATOM   3038 C CG2 . ILE A 1 408 ? 44.154  -23.045 -11.996 1.00 57.47 ?  420 ILE A CG2 1 
ATOM   3039 C CD1 . ILE A 1 408 ? 46.200  -21.434 -10.059 1.00 70.39 ?  420 ILE A CD1 1 
ATOM   3040 N N   . ASN A 1 409 ? 44.713  -22.984 -15.265 1.00 55.65 ?  421 ASN A N   1 
ATOM   3041 C CA  . ASN A 1 409 ? 43.790  -23.398 -16.312 1.00 52.55 ?  421 ASN A CA  1 
ATOM   3042 C C   . ASN A 1 409 ? 44.075  -22.655 -17.610 1.00 53.24 ?  421 ASN A C   1 
ATOM   3043 O O   . ASN A 1 409 ? 43.195  -22.564 -18.477 1.00 55.52 ?  421 ASN A O   1 
ATOM   3044 C CB  . ASN A 1 409 ? 42.324  -23.210 -15.854 1.00 62.27 ?  421 ASN A CB  1 
ATOM   3045 C CG  . ASN A 1 409 ? 41.896  -21.730 -15.703 1.00 57.86 ?  421 ASN A CG  1 
ATOM   3046 O OD1 . ASN A 1 409 ? 42.461  -20.808 -16.299 1.00 49.37 ?  421 ASN A OD1 1 
ATOM   3047 N ND2 . ASN A 1 409 ? 40.871  -21.520 -14.889 1.00 57.54 ?  421 ASN A ND2 1 
ATOM   3048 N N   . SER A 1 410 ? 45.267  -22.089 -17.742 1.00 48.37 ?  422 SER A N   1 
ATOM   3049 C CA  . SER A 1 410 ? 45.681  -21.425 -18.968 1.00 51.29 ?  422 SER A CA  1 
ATOM   3050 C C   . SER A 1 410 ? 47.204  -21.389 -18.969 1.00 46.40 ?  422 SER A C   1 
ATOM   3051 O O   . SER A 1 410 ? 47.836  -21.795 -17.982 1.00 48.32 ?  422 SER A O   1 
ATOM   3052 C CB  . SER A 1 410 ? 45.045  -20.019 -19.093 1.00 53.56 ?  422 SER A CB  1 
ATOM   3053 O OG  . SER A 1 410 ? 45.549  -19.091 -18.160 1.00 50.49 ?  422 SER A OG  1 
ATOM   3054 N N   . PRO A 1 411 ? 47.827  -21.000 -20.085 1.00 45.22 ?  423 PRO A N   1 
ATOM   3055 C CA  . PRO A 1 411 ? 49.289  -21.131 -20.174 1.00 45.74 ?  423 PRO A CA  1 
ATOM   3056 C C   . PRO A 1 411 ? 49.994  -20.345 -19.081 1.00 48.64 ?  423 PRO A C   1 
ATOM   3057 O O   . PRO A 1 411 ? 49.480  -19.351 -18.565 1.00 47.44 ?  423 PRO A O   1 
ATOM   3058 C CB  . PRO A 1 411 ? 49.619  -20.571 -21.561 1.00 39.81 ?  423 PRO A CB  1 
ATOM   3059 C CG  . PRO A 1 411 ? 48.379  -20.701 -22.332 1.00 45.02 ?  423 PRO A CG  1 
ATOM   3060 C CD  . PRO A 1 411 ? 47.238  -20.592 -21.375 1.00 40.58 ?  423 PRO A CD  1 
ATOM   3061 N N   . SER A 1 412 ? 51.195  -20.802 -18.741 1.00 48.10 ?  424 SER A N   1 
ATOM   3062 C CA  . SER A 1 412 ? 51.983  -20.149 -17.713 1.00 47.31 ?  424 SER A CA  1 
ATOM   3063 C C   . SER A 1 412 ? 52.448  -18.769 -18.176 1.00 44.67 ?  424 SER A C   1 
ATOM   3064 O O   . SER A 1 412 ? 52.519  -18.475 -19.376 1.00 47.62 ?  424 SER A O   1 
ATOM   3065 C CB  . SER A 1 412 ? 53.187  -21.008 -17.342 1.00 48.67 ?  424 SER A CB  1 
ATOM   3066 O OG  . SER A 1 412 ? 54.170  -20.956 -18.364 1.00 46.23 ?  424 SER A OG  1 
ATOM   3067 N N   . THR A 1 413 ? 52.725  -17.908 -17.187 1.00 46.44 ?  425 THR A N   1 
ATOM   3068 C CA  . THR A 1 413 ? 53.298  -16.588 -17.443 1.00 45.03 ?  425 THR A CA  1 
ATOM   3069 C C   . THR A 1 413 ? 54.581  -16.710 -18.253 1.00 47.52 ?  425 THR A C   1 
ATOM   3070 O O   . THR A 1 413 ? 54.804  -15.937 -19.200 1.00 40.75 ?  425 THR A O   1 
ATOM   3071 C CB  . THR A 1 413 ? 53.572  -15.869 -16.107 1.00 43.89 ?  425 THR A CB  1 
ATOM   3072 O OG1 . THR A 1 413 ? 52.404  -15.913 -15.278 1.00 47.57 ?  425 THR A OG1 1 
ATOM   3073 C CG2 . THR A 1 413 ? 53.969  -14.414 -16.311 1.00 43.46 ?  425 THR A CG2 1 
ATOM   3074 N N   . GLN A 1 414 ? 55.432  -17.687 -17.890 1.00 44.03 ?  426 GLN A N   1 
ATOM   3075 C CA  . GLN A 1 414 ? 56.652  -17.966 -18.651 1.00 49.93 ?  426 GLN A CA  1 
ATOM   3076 C C   . GLN A 1 414 ? 56.335  -18.339 -20.095 1.00 45.82 ?  426 GLN A C   1 
ATOM   3077 O O   . GLN A 1 414 ? 56.946  -17.806 -21.031 1.00 43.95 ?  426 GLN A O   1 
ATOM   3078 C CB  . GLN A 1 414 ? 57.449  -19.094 -17.995 1.00 48.56 ?  426 GLN A CB  1 
ATOM   3079 C CG  . GLN A 1 414 ? 57.966  -18.808 -16.595 1.00 60.40 ?  426 GLN A CG  1 
ATOM   3080 C CD  . GLN A 1 414 ? 59.412  -18.298 -16.590 1.00 73.27 ?  426 GLN A CD  1 
ATOM   3081 O OE1 . GLN A 1 414 ? 60.232  -18.713 -17.420 1.00 72.43 ?  426 GLN A OE1 1 
ATOM   3082 N NE2 . GLN A 1 414 ? 59.734  -17.414 -15.633 1.00 67.95 ?  426 GLN A NE2 1 
ATOM   3083 N N   . ASN A 1 415 ? 55.392  -19.273 -20.291 1.00 44.28 ?  427 ASN A N   1 
ATOM   3084 C CA  . ASN A 1 415 ? 55.016  -19.699 -21.639 1.00 47.04 ?  427 ASN A CA  1 
ATOM   3085 C C   . ASN A 1 415 ? 54.516  -18.527 -22.473 1.00 44.85 ?  427 ASN A C   1 
ATOM   3086 O O   . ASN A 1 415 ? 54.892  -18.387 -23.642 1.00 50.73 ?  427 ASN A O   1 
ATOM   3087 C CB  . ASN A 1 415 ? 53.940  -20.793 -21.581 1.00 51.66 ?  427 ASN A CB  1 
ATOM   3088 C CG  . ASN A 1 415 ? 54.497  -22.176 -21.200 1.00 51.85 ?  427 ASN A CG  1 
ATOM   3089 O OD1 . ASN A 1 415 ? 55.708  -22.389 -21.132 1.00 53.98 ?  427 ASN A OD1 1 
ATOM   3090 N ND2 . ASN A 1 415 ? 53.593  -23.120 -20.952 1.00 54.41 ?  427 ASN A ND2 1 
ATOM   3091 N N   . VAL A 1 416 ? 53.671  -17.669 -21.897 1.00 45.77 ?  428 VAL A N   1 
ATOM   3092 C CA  . VAL A 1 416 ? 53.122  -16.559 -22.677 1.00 44.13 ?  428 VAL A CA  1 
ATOM   3093 C C   . VAL A 1 416 ? 54.134  -15.420 -22.828 1.00 42.61 ?  428 VAL A C   1 
ATOM   3094 O O   . VAL A 1 416 ? 54.299  -14.853 -23.914 1.00 41.25 ?  428 VAL A O   1 
ATOM   3095 C CB  . VAL A 1 416 ? 51.810  -16.064 -22.042 1.00 42.84 ?  428 VAL A CB  1 
ATOM   3096 C CG1 . VAL A 1 416 ? 51.265  -14.867 -22.810 1.00 41.17 ?  428 VAL A CG1 1 
ATOM   3097 C CG2 . VAL A 1 416 ? 50.784  -17.176 -22.004 1.00 47.46 ?  428 VAL A CG2 1 
ATOM   3098 N N   . LEU A 1 417 ? 54.806  -15.040 -21.748 1.00 47.09 ?  429 LEU A N   1 
ATOM   3099 C CA  . LEU A 1 417 ? 55.618  -13.831 -21.771 1.00 48.51 ?  429 LEU A CA  1 
ATOM   3100 C C   . LEU A 1 417 ? 57.096  -14.096 -22.001 1.00 51.26 ?  429 LEU A C   1 
ATOM   3101 O O   . LEU A 1 417 ? 57.829  -13.160 -22.344 1.00 48.68 ?  429 LEU A O   1 
ATOM   3102 C CB  . LEU A 1 417 ? 55.452  -13.056 -20.457 1.00 46.39 ?  429 LEU A CB  1 
ATOM   3103 C CG  . LEU A 1 417 ? 54.061  -12.478 -20.211 1.00 42.75 ?  429 LEU A CG  1 
ATOM   3104 C CD1 . LEU A 1 417 ? 54.076  -11.635 -18.951 1.00 47.28 ?  429 LEU A CD1 1 
ATOM   3105 C CD2 . LEU A 1 417 ? 53.612  -11.658 -21.401 1.00 41.60 ?  429 LEU A CD2 1 
ATOM   3106 N N   . GLY A 1 418 ? 57.545  -15.337 -21.843 1.00 45.81 ?  430 GLY A N   1 
ATOM   3107 C CA  . GLY A 1 418 ? 58.959  -15.612 -21.774 1.00 47.39 ?  430 GLY A CA  1 
ATOM   3108 C C   . GLY A 1 418 ? 59.498  -15.269 -20.399 1.00 56.01 ?  430 GLY A C   1 
ATOM   3109 O O   . GLY A 1 418 ? 58.823  -14.675 -19.558 1.00 55.27 ?  430 GLY A O   1 
ATOM   3110 N N   . SER A 1 419 ? 60.760  -15.636 -20.179 1.00 56.53 ?  431 SER A N   1 
ATOM   3111 C CA  . SER A 1 419 ? 61.302  -15.630 -18.828 1.00 56.64 ?  431 SER A CA  1 
ATOM   3112 C C   . SER A 1 419 ? 61.516  -14.217 -18.303 1.00 52.94 ?  431 SER A C   1 
ATOM   3113 O O   . SER A 1 419 ? 61.227  -13.944 -17.134 1.00 54.28 ?  431 SER A O   1 
ATOM   3114 C CB  . SER A 1 419 ? 62.608  -16.413 -18.794 1.00 61.18 ?  431 SER A CB  1 
ATOM   3115 O OG  . SER A 1 419 ? 62.348  -17.793 -18.633 1.00 69.52 ?  431 SER A OG  1 
ATOM   3116 N N   . ASP A 1 420 ? 62.036  -13.309 -19.134 1.00 51.60 ?  432 ASP A N   1 
ATOM   3117 C CA  . ASP A 1 420 ? 62.347  -11.965 -18.644 1.00 57.65 ?  432 ASP A CA  1 
ATOM   3118 C C   . ASP A 1 420 ? 61.081  -11.225 -18.229 1.00 54.90 ?  432 ASP A C   1 
ATOM   3119 O O   . ASP A 1 420 ? 60.906  -10.885 -17.051 1.00 52.72 ?  432 ASP A O   1 
ATOM   3120 C CB  . ASP A 1 420 ? 63.111  -11.158 -19.700 1.00 59.94 ?  432 ASP A CB  1 
ATOM   3121 C CG  . ASP A 1 420 ? 64.593  -11.495 -19.738 1.00 68.12 ?  432 ASP A CG  1 
ATOM   3122 O OD1 . ASP A 1 420 ? 65.206  -11.649 -18.657 1.00 69.44 ?  432 ASP A OD1 1 
ATOM   3123 O OD2 . ASP A 1 420 ? 65.148  -11.603 -20.854 1.00 77.45 -1 432 ASP A OD2 1 
ATOM   3124 N N   . LEU A 1 421 ? 60.184  -10.972 -19.190 1.00 49.95 ?  433 LEU A N   1 
ATOM   3125 C CA  . LEU A 1 421 ? 58.957  -10.242 -18.894 1.00 45.50 ?  433 LEU A CA  1 
ATOM   3126 C C   . LEU A 1 421 ? 58.125  -10.944 -17.832 1.00 48.69 ?  433 LEU A C   1 
ATOM   3127 O O   . LEU A 1 421 ? 57.345  -10.290 -17.131 1.00 50.34 ?  433 LEU A O   1 
ATOM   3128 C CB  . LEU A 1 421 ? 58.135  -10.030 -20.169 1.00 42.33 ?  433 LEU A CB  1 
ATOM   3129 C CG  . LEU A 1 421 ? 58.802  -9.281  -21.332 1.00 47.16 ?  433 LEU A CG  1 
ATOM   3130 C CD1 . LEU A 1 421 ? 57.932  -9.290  -22.581 1.00 48.71 ?  433 LEU A CD1 1 
ATOM   3131 C CD2 . LEU A 1 421 ? 59.162  -7.838  -20.958 1.00 45.78 ?  433 LEU A CD2 1 
ATOM   3132 N N   . ALA A 1 422 ? 58.282  -12.260 -17.676 1.00 45.98 ?  434 ALA A N   1 
ATOM   3133 C CA  . ALA A 1 422 ? 57.538  -12.931 -16.620 1.00 46.04 ?  434 ALA A CA  1 
ATOM   3134 C C   . ALA A 1 422 ? 58.121  -12.605 -15.258 1.00 47.54 ?  434 ALA A C   1 
ATOM   3135 O O   . ALA A 1 422 ? 57.400  -12.603 -14.253 1.00 47.17 ?  434 ALA A O   1 
ATOM   3136 C CB  . ALA A 1 422 ? 57.518  -14.439 -16.842 1.00 48.06 ?  434 ALA A CB  1 
ATOM   3137 N N   . ASN A 1 423 ? 59.417  -12.322 -15.205 1.00 51.21 ?  435 ASN A N   1 
ATOM   3138 C CA  . ASN A 1 423 ? 60.026  -11.927 -13.942 1.00 53.84 ?  435 ASN A CA  1 
ATOM   3139 C C   . ASN A 1 423 ? 59.707  -10.471 -13.614 1.00 47.55 ?  435 ASN A C   1 
ATOM   3140 O O   . ASN A 1 423 ? 59.386  -10.145 -12.462 1.00 44.90 ?  435 ASN A O   1 
ATOM   3141 C CB  . ASN A 1 423 ? 61.533  -12.175 -14.003 1.00 56.02 ?  435 ASN A CB  1 
ATOM   3142 C CG  . ASN A 1 423 ? 61.892  -13.623 -13.699 1.00 64.66 ?  435 ASN A CG  1 
ATOM   3143 O OD1 . ASN A 1 423 ? 61.259  -14.274 -12.856 1.00 70.93 ?  435 ASN A OD1 1 
ATOM   3144 N ND2 . ASN A 1 423 ? 62.893  -14.141 -14.401 1.00 64.93 ?  435 ASN A ND2 1 
ATOM   3145 N N   . GLN A 1 424 ? 59.746  -9.600  -14.625 1.00 38.84 ?  436 GLN A N   1 
ATOM   3146 C CA  . GLN A 1 424 ? 59.289  -8.229  -14.442 1.00 44.32 ?  436 GLN A CA  1 
ATOM   3147 C C   . GLN A 1 424 ? 57.865  -8.187  -13.901 1.00 46.21 ?  436 GLN A C   1 
ATOM   3148 O O   . GLN A 1 424 ? 57.577  -7.460  -12.942 1.00 49.16 ?  436 GLN A O   1 
ATOM   3149 C CB  . GLN A 1 424 ? 59.380  -7.460  -15.758 1.00 41.88 ?  436 GLN A CB  1 
ATOM   3150 C CG  . GLN A 1 424 ? 60.735  -7.532  -16.388 1.00 45.53 ?  436 GLN A CG  1 
ATOM   3151 C CD  . GLN A 1 424 ? 60.860  -6.590  -17.537 1.00 47.97 ?  436 GLN A CD  1 
ATOM   3152 O OE1 . GLN A 1 424 ? 60.210  -5.551  -17.553 1.00 55.65 ?  436 GLN A OE1 1 
ATOM   3153 N NE2 . GLN A 1 424 ? 61.694  -6.940  -18.517 1.00 49.61 ?  436 GLN A NE2 1 
ATOM   3154 N N   . LEU A 1 425 ? 56.957  -8.952  -14.514 1.00 47.46 ?  437 LEU A N   1 
ATOM   3155 C CA  . LEU A 1 425 ? 55.569  -8.955  -14.065 1.00 42.71 ?  437 LEU A CA  1 
ATOM   3156 C C   . LEU A 1 425 ? 55.466  -9.486  -12.644 1.00 45.61 ?  437 LEU A C   1 
ATOM   3157 O O   . LEU A 1 425 ? 54.810  -8.876  -11.791 1.00 41.34 ?  437 LEU A O   1 
ATOM   3158 C CB  . LEU A 1 425 ? 54.702  -9.777  -15.019 1.00 44.77 ?  437 LEU A CB  1 
ATOM   3159 C CG  . LEU A 1 425 ? 53.215  -9.864  -14.658 1.00 47.51 ?  437 LEU A CG  1 
ATOM   3160 C CD1 . LEU A 1 425 ? 52.578  -8.481  -14.764 1.00 44.65 ?  437 LEU A CD1 1 
ATOM   3161 C CD2 . LEU A 1 425 ? 52.469  -10.869 -15.547 1.00 44.18 ?  437 LEU A CD2 1 
ATOM   3162 N N   . ASN A 1 426 ? 56.123  -10.620 -12.371 1.00 43.64 ?  438 ASN A N   1 
ATOM   3163 C CA  . ASN A 1 426 ? 56.117  -11.192 -11.027 1.00 42.66 ?  438 ASN A CA  1 
ATOM   3164 C C   . ASN A 1 426 ? 56.607  -10.189 -9.992  1.00 47.07 ?  438 ASN A C   1 
ATOM   3165 O O   . ASN A 1 426 ? 56.105  -10.150 -8.862  1.00 47.48 ?  438 ASN A O   1 
ATOM   3166 C CB  . ASN A 1 426 ? 57.006  -12.431 -10.976 1.00 47.61 ?  438 ASN A CB  1 
ATOM   3167 C CG  . ASN A 1 426 ? 56.329  -13.656 -11.508 1.00 50.24 ?  438 ASN A CG  1 
ATOM   3168 O OD1 . ASN A 1 426 ? 55.112  -13.783 -11.440 1.00 53.19 ?  438 ASN A OD1 1 
ATOM   3169 N ND2 . ASN A 1 426 ? 57.121  -14.584 -12.036 1.00 55.25 ?  438 ASN A ND2 1 
ATOM   3170 N N   . SER A 1 427 ? 57.604  -9.384  -10.347 1.00 47.18 ?  439 SER A N   1 
ATOM   3171 C CA  . SER A 1 427 ? 58.184  -8.502  -9.349  1.00 49.88 ?  439 SER A CA  1 
ATOM   3172 C C   . SER A 1 427 ? 57.359  -7.241  -9.107  1.00 49.02 ?  439 SER A C   1 
ATOM   3173 O O   . SER A 1 427 ? 57.715  -6.472  -8.212  1.00 51.61 ?  439 SER A O   1 
ATOM   3174 C CB  . SER A 1 427 ? 59.622  -8.137  -9.732  1.00 48.00 ?  439 SER A CB  1 
ATOM   3175 O OG  . SER A 1 427 ? 59.653  -7.250  -10.827 1.00 47.46 ?  439 SER A OG  1 
ATOM   3176 N N   . LEU A 1 428 ? 56.265  -7.015  -9.851  1.00 47.43 ?  440 LEU A N   1 
ATOM   3177 C CA  . LEU A 1 428 ? 55.332  -5.952  -9.480  1.00 42.36 ?  440 LEU A CA  1 
ATOM   3178 C C   . LEU A 1 428 ? 54.564  -6.286  -8.209  1.00 45.20 ?  440 LEU A C   1 
ATOM   3179 O O   . LEU A 1 428 ? 53.983  -5.380  -7.593  1.00 42.27 ?  440 LEU A O   1 
ATOM   3180 C CB  . LEU A 1 428 ? 54.342  -5.675  -10.603 1.00 38.54 ?  440 LEU A CB  1 
ATOM   3181 C CG  . LEU A 1 428 ? 54.935  -5.070  -11.865 1.00 42.61 ?  440 LEU A CG  1 
ATOM   3182 C CD1 . LEU A 1 428 ? 53.913  -5.075  -12.988 1.00 39.64 ?  440 LEU A CD1 1 
ATOM   3183 C CD2 . LEU A 1 428 ? 55.422  -3.661  -11.600 1.00 43.77 ?  440 LEU A CD2 1 
ATOM   3184 N N   . LYS A 1 429 ? 54.546  -7.554  -7.800  1.00 39.19 ?  441 LYS A N   1 
ATOM   3185 C CA  . LYS A 1 429 ? 53.867  -7.916  -6.564  1.00 40.70 ?  441 LYS A CA  1 
ATOM   3186 C C   . LYS A 1 429 ? 54.358  -7.035  -5.427  1.00 44.76 ?  441 LYS A C   1 
ATOM   3187 O O   . LYS A 1 429 ? 55.562  -6.937  -5.182  1.00 45.95 ?  441 LYS A O   1 
ATOM   3188 C CB  . LYS A 1 429 ? 54.108  -9.388  -6.226  1.00 43.10 ?  441 LYS A CB  1 
ATOM   3189 C CG  . LYS A 1 429 ? 53.115  -9.961  -5.224  1.00 44.54 ?  441 LYS A CG  1 
ATOM   3190 C CD  . LYS A 1 429 ? 53.594  -11.278 -4.616  1.00 45.80 ?  441 LYS A CD  1 
ATOM   3191 C CE  . LYS A 1 429 ? 52.401  -12.051 -4.045  1.00 62.24 ?  441 LYS A CE  1 
ATOM   3192 N NZ  . LYS A 1 429 ? 52.754  -13.373 -3.455  1.00 66.18 ?  441 LYS A NZ  1 
ATOM   3193 N N   . GLY A 1 430 ? 53.415  -6.376  -4.745  1.00 47.40 ?  442 GLY A N   1 
ATOM   3194 C CA  . GLY A 1 430 ? 53.711  -5.575  -3.577  1.00 41.27 ?  442 GLY A CA  1 
ATOM   3195 C C   . GLY A 1 430 ? 54.059  -4.129  -3.857  1.00 43.38 ?  442 GLY A C   1 
ATOM   3196 O O   . GLY A 1 430 ? 54.098  -3.324  -2.910  1.00 39.23 ?  442 GLY A O   1 
ATOM   3197 N N   . GLN A 1 431 ? 54.308  -3.774  -5.118  1.00 34.92 ?  443 GLN A N   1 
ATOM   3198 C CA  . GLN A 1 431 ? 54.617  -2.406  -5.493  1.00 40.74 ?  443 GLN A CA  1 
ATOM   3199 C C   . GLN A 1 431 ? 53.345  -1.594  -5.694  1.00 43.03 ?  443 GLN A C   1 
ATOM   3200 O O   . GLN A 1 431 ? 52.290  -2.136  -6.036  1.00 42.94 ?  443 GLN A O   1 
ATOM   3201 C CB  . GLN A 1 431 ? 55.438  -2.372  -6.774  1.00 41.91 ?  443 GLN A CB  1 
ATOM   3202 C CG  . GLN A 1 431 ? 56.857  -2.842  -6.612  1.00 43.42 ?  443 GLN A CG  1 
ATOM   3203 C CD  . GLN A 1 431 ? 57.588  -2.797  -7.931  1.00 58.48 ?  443 GLN A CD  1 
ATOM   3204 O OE1 . GLN A 1 431 ? 58.005  -3.825  -8.461  1.00 64.62 ?  443 GLN A OE1 1 
ATOM   3205 N NE2 . GLN A 1 431 ? 57.707  -1.594  -8.501  1.00 59.73 ?  443 GLN A NE2 1 
ATOM   3206 N N   . GLN A 1 432 ? 53.455  -0.282  -5.477  1.00 41.59 ?  444 GLN A N   1 
ATOM   3207 C CA  . GLN A 1 432 ? 52.303  0.595   -5.648  1.00 44.30 ?  444 GLN A CA  1 
ATOM   3208 C C   . GLN A 1 432 ? 51.837  0.584   -7.102  1.00 40.55 ?  444 GLN A C   1 
ATOM   3209 O O   . GLN A 1 432 ? 52.635  0.758   -8.027  1.00 38.42 ?  444 GLN A O   1 
ATOM   3210 C CB  . GLN A 1 432 ? 52.641  2.034   -5.219  1.00 39.48 ?  444 GLN A CB  1 
ATOM   3211 C CG  . GLN A 1 432 ? 52.611  2.313   -3.696  1.00 48.60 ?  444 GLN A CG  1 
ATOM   3212 C CD  . GLN A 1 432 ? 51.390  1.725   -2.992  1.00 53.66 ?  444 GLN A CD  1 
ATOM   3213 O OE1 . GLN A 1 432 ? 50.281  1.692   -3.551  1.00 52.83 ?  444 GLN A OE1 1 
ATOM   3214 N NE2 . GLN A 1 432 ? 51.586  1.251   -1.757  1.00 53.59 ?  444 GLN A NE2 1 
ATOM   3215 N N   . SER A 1 433 ? 50.540  0.384   -7.304  1.00 36.41 ?  445 SER A N   1 
ATOM   3216 C CA  . SER A 1 433 ? 49.973  0.643   -8.621  1.00 35.78 ?  445 SER A CA  1 
ATOM   3217 C C   . SER A 1 433 ? 49.682  2.131   -8.803  1.00 35.57 ?  445 SER A C   1 
ATOM   3218 O O   . SER A 1 433 ? 49.742  2.935   -7.860  1.00 35.85 ?  445 SER A O   1 
ATOM   3219 C CB  . SER A 1 433 ? 48.691  -0.154  -8.823  1.00 32.41 ?  445 SER A CB  1 
ATOM   3220 O OG  . SER A 1 433 ? 47.674  0.299   -7.951  1.00 32.13 ?  445 SER A OG  1 
ATOM   3221 N N   . ALA A 1 434 ? 49.337  2.491   -10.043 1.00 30.60 ?  446 ALA A N   1 
ATOM   3222 C CA  . ALA A 1 434 ? 48.957  3.863   -10.346 1.00 30.29 ?  446 ALA A CA  1 
ATOM   3223 C C   . ALA A 1 434 ? 47.750  4.318   -9.535  1.00 37.92 ?  446 ALA A C   1 
ATOM   3224 O O   . ALA A 1 434 ? 47.509  5.526   -9.425  1.00 30.18 ?  446 ALA A O   1 
ATOM   3225 C CB  . ALA A 1 434 ? 48.668  4.017   -11.838 1.00 35.13 ?  446 ALA A CB  1 
ATOM   3226 N N   . PHE A 1 435 ? 47.006  3.383   -8.940  1.00 34.77 ?  447 PHE A N   1 
ATOM   3227 C CA  . PHE A 1 435 ? 45.836  3.719   -8.146  1.00 31.97 ?  447 PHE A CA  1 
ATOM   3228 C C   . PHE A 1 435 ? 46.149  3.782   -6.656  1.00 36.01 ?  447 PHE A C   1 
ATOM   3229 O O   . PHE A 1 435 ? 45.227  3.895   -5.838  1.00 39.16 ?  447 PHE A O   1 
ATOM   3230 C CB  . PHE A 1 435 ? 44.708  2.723   -8.444  1.00 26.59 ?  447 PHE A CB  1 
ATOM   3231 C CG  . PHE A 1 435 ? 44.353  2.648   -9.911  1.00 27.92 ?  447 PHE A CG  1 
ATOM   3232 C CD1 . PHE A 1 435 ? 45.085  1.831   -10.786 1.00 27.93 ?  447 PHE A CD1 1 
ATOM   3233 C CD2 . PHE A 1 435 ? 43.317  3.414   -10.427 1.00 27.53 ?  447 PHE A CD2 1 
ATOM   3234 C CE1 . PHE A 1 435 ? 44.771  1.782   -12.150 1.00 29.27 ?  447 PHE A CE1 1 
ATOM   3235 C CE2 . PHE A 1 435 ? 42.985  3.363   -11.782 1.00 30.70 ?  447 PHE A CE2 1 
ATOM   3236 C CZ  . PHE A 1 435 ? 43.712  2.547   -12.648 1.00 26.80 ?  447 PHE A CZ  1 
ATOM   3237 N N   . GLY A 1 436 ? 47.427  3.729   -6.283  1.00 36.42 ?  448 GLY A N   1 
ATOM   3238 C CA  . GLY A 1 436 ? 47.801  3.846   -4.892  1.00 37.56 ?  448 GLY A CA  1 
ATOM   3239 C C   . GLY A 1 436 ? 47.548  2.624   -4.043  1.00 44.03 ?  448 GLY A C   1 
ATOM   3240 O O   . GLY A 1 436 ? 47.805  2.669   -2.834  1.00 54.14 ?  448 GLY A O   1 
ATOM   3241 N N   . LYS A 1 437 ? 47.041  1.552   -4.615  1.00 37.21 ?  449 LYS A N   1 
ATOM   3242 C CA  . LYS A 1 437 ? 46.962  0.286   -3.914  1.00 38.39 ?  449 LYS A CA  1 
ATOM   3243 C C   . LYS A 1 437 ? 47.994  -0.680  -4.499  1.00 39.14 ?  449 LYS A C   1 
ATOM   3244 O O   . LYS A 1 437 ? 48.308  -0.614  -5.694  1.00 35.04 ?  449 LYS A O   1 
ATOM   3245 C CB  . LYS A 1 437 ? 45.554  -0.320  -4.012  1.00 35.11 ?  449 LYS A CB  1 
ATOM   3246 C CG  . LYS A 1 437 ? 44.540  0.272   -3.032  1.00 33.11 ?  449 LYS A CG  1 
ATOM   3247 C CD  . LYS A 1 437 ? 43.097  0.009   -3.444  1.00 31.75 ?  449 LYS A CD  1 
ATOM   3248 C CE  . LYS A 1 437 ? 42.392  -0.948  -2.479  1.00 38.50 ?  449 LYS A CE  1 
ATOM   3249 N NZ  . LYS A 1 437 ? 40.898  -0.759  -2.421  1.00 39.67 ?  449 LYS A NZ  1 
ATOM   3250 N N   . PRO A 1 438 ? 48.554  -1.572  -3.684  1.00 39.58 ?  450 PRO A N   1 
ATOM   3251 C CA  . PRO A 1 438 ? 49.646  -2.425  -4.171  1.00 40.29 ?  450 PRO A CA  1 
ATOM   3252 C C   . PRO A 1 438 ? 49.160  -3.476  -5.157  1.00 37.04 ?  450 PRO A C   1 
ATOM   3253 O O   . PRO A 1 438 ? 48.029  -3.963  -5.078  1.00 36.84 ?  450 PRO A O   1 
ATOM   3254 C CB  . PRO A 1 438 ? 50.182  -3.075  -2.891  1.00 33.95 ?  450 PRO A CB  1 
ATOM   3255 C CG  . PRO A 1 438 ? 48.986  -3.143  -2.001  1.00 37.46 ?  450 PRO A CG  1 
ATOM   3256 C CD  . PRO A 1 438 ? 48.182  -1.890  -2.294  1.00 34.36 ?  450 PRO A CD  1 
ATOM   3257 N N   . PHE A 1 439 ? 50.043  -3.823  -6.098  1.00 38.30 ?  451 PHE A N   1 
ATOM   3258 C CA  . PHE A 1 439 ? 49.790  -4.937  -7.006  1.00 36.29 ?  451 PHE A CA  1 
ATOM   3259 C C   . PHE A 1 439 ? 49.805  -6.266  -6.256  1.00 39.07 ?  451 PHE A C   1 
ATOM   3260 O O   . PHE A 1 439 ? 50.481  -6.428  -5.237  1.00 37.64 ?  451 PHE A O   1 
ATOM   3261 C CB  . PHE A 1 439 ? 50.851  -5.010  -8.104  1.00 36.76 ?  451 PHE A CB  1 
ATOM   3262 C CG  . PHE A 1 439 ? 50.725  -3.964  -9.158  1.00 34.07 ?  451 PHE A CG  1 
ATOM   3263 C CD1 . PHE A 1 439 ? 49.609  -3.896  -9.959  1.00 31.87 ?  451 PHE A CD1 1 
ATOM   3264 C CD2 . PHE A 1 439 ? 51.744  -3.045  -9.355  1.00 37.81 ?  451 PHE A CD2 1 
ATOM   3265 C CE1 . PHE A 1 439 ? 49.498  -2.933  -10.934 1.00 28.56 ?  451 PHE A CE1 1 
ATOM   3266 C CE2 . PHE A 1 439 ? 51.639  -2.078  -10.333 1.00 35.39 ?  451 PHE A CE2 1 
ATOM   3267 C CZ  . PHE A 1 439 ? 50.509  -2.026  -11.125 1.00 32.02 ?  451 PHE A CZ  1 
ATOM   3268 N N   . GLY A 1 440 ? 49.077  -7.235  -6.799  1.00 42.98 ?  452 GLY A N   1 
ATOM   3269 C CA  . GLY A 1 440 ? 49.128  -8.602  -6.335  1.00 44.20 ?  452 GLY A CA  1 
ATOM   3270 C C   . GLY A 1 440 ? 49.957  -9.494  -7.241  1.00 43.70 ?  452 GLY A C   1 
ATOM   3271 O O   . GLY A 1 440 ? 50.754  -9.033  -8.068  1.00 39.33 ?  452 GLY A O   1 
ATOM   3272 N N   . SER A 1 441 ? 49.760  -10.796 -7.087  1.00 43.24 ?  453 SER A N   1 
ATOM   3273 C CA  . SER A 1 441 ? 50.440  -11.755 -7.939  1.00 43.09 ?  453 SER A CA  1 
ATOM   3274 C C   . SER A 1 441 ? 49.601  -12.046 -9.185  1.00 45.38 ?  453 SER A C   1 
ATOM   3275 O O   . SER A 1 441 ? 48.431  -11.654 -9.293  1.00 39.06 ?  453 SER A O   1 
ATOM   3276 C CB  . SER A 1 441 ? 50.728  -13.036 -7.167  1.00 42.74 ?  453 SER A CB  1 
ATOM   3277 O OG  . SER A 1 441 ? 49.556  -13.816 -7.039  1.00 44.53 ?  453 SER A OG  1 
ATOM   3278 N N   . VAL A 1 442 ? 50.227  -12.738 -10.144 1.00 43.65 ?  454 VAL A N   1 
ATOM   3279 C CA  . VAL A 1 442 ? 49.519  -13.114 -11.363 1.00 44.18 ?  454 VAL A CA  1 
ATOM   3280 C C   . VAL A 1 442 ? 48.406  -14.109 -11.053 1.00 41.83 ?  454 VAL A C   1 
ATOM   3281 O O   . VAL A 1 442 ? 47.397  -14.155 -11.763 1.00 43.88 ?  454 VAL A O   1 
ATOM   3282 C CB  . VAL A 1 442 ? 50.506  -13.675 -12.404 1.00 41.06 ?  454 VAL A CB  1 
ATOM   3283 C CG1 . VAL A 1 442 ? 51.252  -14.873 -11.841 1.00 43.14 ?  454 VAL A CG1 1 
ATOM   3284 C CG2 . VAL A 1 442 ? 49.785  -14.032 -13.673 1.00 44.93 ?  454 VAL A CG2 1 
ATOM   3285 N N   . SER A 1 443 ? 48.545  -14.904 -9.950  1.00 39.49 ?  455 SER A N   1 
ATOM   3286 C CA  . SER A 1 443 ? 47.574  -15.928 -9.571  1.00 44.24 ?  455 SER A CA  1 
ATOM   3287 C C   . SER A 1 443 ? 46.639  -15.416 -8.486  1.00 48.89 ?  455 SER A C   1 
ATOM   3288 O O   . SER A 1 443 ? 47.109  -14.954 -7.433  1.00 45.47 ?  455 SER A O   1 
ATOM   3289 C CB  . SER A 1 443 ? 48.285  -17.185 -9.072  1.00 40.72 ?  455 SER A CB  1 
ATOM   3290 O OG  . SER A 1 443 ? 48.858  -17.895 -10.151 1.00 56.91 ?  455 SER A OG  1 
ATOM   3291 N N   . PRO A 1 444 ? 45.329  -15.520 -8.684  1.00 47.16 ?  456 PRO A N   1 
ATOM   3292 C CA  . PRO A 1 444 ? 44.373  -15.157 -7.625  1.00 45.48 ?  456 PRO A CA  1 
ATOM   3293 C C   . PRO A 1 444 ? 44.526  -16.071 -6.423  1.00 53.41 ?  456 PRO A C   1 
ATOM   3294 O O   . PRO A 1 444 ? 45.225  -17.096 -6.497  1.00 50.02 ?  456 PRO A O   1 
ATOM   3295 C CB  . PRO A 1 444 ? 42.998  -15.344 -8.298  1.00 45.62 ?  456 PRO A CB  1 
ATOM   3296 C CG  . PRO A 1 444 ? 43.268  -15.430 -9.749  1.00 46.75 ?  456 PRO A CG  1 
ATOM   3297 C CD  . PRO A 1 444 ? 44.656  -16.005 -9.898  1.00 46.26 ?  456 PRO A CD  1 
ATOM   3298 N N   . PRO A 1 445 ? 43.896  -15.732 -5.290  1.00 63.01 ?  457 PRO A N   1 
ATOM   3299 C CA  . PRO A 1 445 ? 44.067  -16.555 -4.085  1.00 63.74 ?  457 PRO A CA  1 
ATOM   3300 C C   . PRO A 1 445 ? 43.433  -17.931 -4.248  1.00 68.83 ?  457 PRO A C   1 
ATOM   3301 O O   . PRO A 1 445 ? 42.311  -18.070 -4.745  1.00 66.75 ?  457 PRO A O   1 
ATOM   3302 C CB  . PRO A 1 445 ? 43.363  -15.742 -2.991  1.00 55.22 ?  457 PRO A CB  1 
ATOM   3303 C CG  . PRO A 1 445 ? 42.400  -14.889 -3.713  1.00 52.96 ?  457 PRO A CG  1 
ATOM   3304 C CD  . PRO A 1 445 ? 43.029  -14.564 -5.036  1.00 53.16 ?  457 PRO A CD  1 
ATOM   3305 N N   . LEU A 1 446 ? 44.174  -18.951 -3.819  1.00 76.89 ?  458 LEU A N   1 
ATOM   3306 C CA  . LEU A 1 446 ? 43.719  -20.336 -3.891  1.00 83.44 ?  458 LEU A CA  1 
ATOM   3307 C C   . LEU A 1 446 ? 42.967  -20.723 -2.619  1.00 84.04 ?  458 LEU A C   1 
ATOM   3308 O O   . LEU A 1 446 ? 42.067  -19.994 -2.177  1.00 79.49 ?  458 LEU A O   1 
ATOM   3309 C CB  . LEU A 1 446 ? 44.908  -21.277 -4.131  1.00 83.08 ?  458 LEU A CB  1 
ATOM   3310 C CG  . LEU A 1 446 ? 45.571  -21.114 -5.505  1.00 89.56 ?  458 LEU A CG  1 
ATOM   3311 C CD1 . LEU A 1 446 ? 46.851  -21.937 -5.625  1.00 93.42 ?  458 LEU A CD1 1 
ATOM   3312 C CD2 . LEU A 1 446 ? 44.582  -21.477 -6.614  1.00 83.95 ?  458 LEU A CD2 1 
ATOM   3313 O OXT . LEU A 1 446 ? 43.238  -21.769 -2.019  1.00 83.60 -1 458 LEU A OXT 1 
HETATM 3314 C C1  . NAG B 2 .   ? -13.005 -33.223 -25.162 1.00 49.05 ?  1   NAG B C1  1 
HETATM 3315 C C2  . NAG B 2 .   ? -14.053 -32.107 -25.154 1.00 52.09 ?  1   NAG B C2  1 
HETATM 3316 C C3  . NAG B 2 .   ? -14.467 -31.722 -23.732 1.00 56.05 ?  1   NAG B C3  1 
HETATM 3317 C C4  . NAG B 2 .   ? -14.644 -32.932 -22.822 1.00 50.34 ?  1   NAG B C4  1 
HETATM 3318 C C5  . NAG B 2 .   ? -13.397 -33.803 -22.903 1.00 53.31 ?  1   NAG B C5  1 
HETATM 3319 C C6  . NAG B 2 .   ? -13.453 -35.022 -22.012 1.00 51.29 ?  1   NAG B C6  1 
HETATM 3320 C C7  . NAG B 2 .   ? -12.440 -30.275 -25.644 1.00 51.84 ?  1   NAG B C7  1 
HETATM 3321 C C8  . NAG B 2 .   ? -11.964 -29.412 -26.771 1.00 50.39 ?  1   NAG B C8  1 
HETATM 3322 N N2  . NAG B 2 .   ? -13.583 -30.935 -25.865 1.00 51.33 ?  1   NAG B N2  1 
HETATM 3323 O O3  . NAG B 2 .   ? -15.665 -30.961 -23.819 1.00 50.82 ?  1   NAG B O3  1 
HETATM 3324 O O4  . NAG B 2 .   ? -14.805 -32.522 -21.463 1.00 57.58 ?  1   NAG B O4  1 
HETATM 3325 O O5  . NAG B 2 .   ? -13.264 -34.279 -24.253 1.00 52.01 ?  1   NAG B O5  1 
HETATM 3326 O O6  . NAG B 2 .   ? -14.771 -35.267 -21.530 1.00 51.98 ?  1   NAG B O6  1 
HETATM 3327 O O7  . NAG B 2 .   ? -11.824 -30.349 -24.585 1.00 53.36 ?  1   NAG B O7  1 
HETATM 3328 C C1  . NAG B 2 .   ? -16.021 -32.171 -20.871 1.00 64.75 ?  2   NAG B C1  1 
HETATM 3329 C C2  . NAG B 2 .   ? -15.800 -32.126 -19.359 1.00 64.65 ?  2   NAG B C2  1 
HETATM 3330 C C3  . NAG B 2 .   ? -17.112 -31.794 -18.655 1.00 64.55 ?  2   NAG B C3  1 
HETATM 3331 C C4  . NAG B 2 .   ? -17.723 -30.523 -19.230 1.00 70.27 ?  2   NAG B C4  1 
HETATM 3332 C C5  . NAG B 2 .   ? -17.867 -30.667 -20.741 1.00 71.48 ?  2   NAG B C5  1 
HETATM 3333 C C6  . NAG B 2 .   ? -18.375 -29.410 -21.405 1.00 74.34 ?  2   NAG B C6  1 
HETATM 3334 C C7  . NAG B 2 .   ? -13.988 -33.487 -18.447 1.00 66.99 ?  2   NAG B C7  1 
HETATM 3335 C C8  . NAG B 2 .   ? -13.486 -32.393 -17.555 1.00 57.72 ?  2   NAG B C8  1 
HETATM 3336 N N2  . NAG B 2 .   ? -15.250 -33.369 -18.863 1.00 64.94 ?  2   NAG B N2  1 
HETATM 3337 O O3  . NAG B 2 .   ? -16.883 -31.660 -17.259 1.00 71.19 ?  2   NAG B O3  1 
HETATM 3338 O O4  . NAG B 2 .   ? -19.013 -30.321 -18.660 1.00 71.36 ?  2   NAG B O4  1 
HETATM 3339 O O5  . NAG B 2 .   ? -16.574 -30.942 -21.314 1.00 66.04 ?  2   NAG B O5  1 
HETATM 3340 O O6  . NAG B 2 .   ? -17.461 -28.331 -21.223 1.00 84.60 ?  2   NAG B O6  1 
HETATM 3341 O O7  . NAG B 2 .   ? -13.282 -34.434 -18.776 1.00 69.64 ?  2   NAG B O7  1 
HETATM 3342 C C1  . PLM C 3 .   ? 16.527  -36.551 -20.929 1.00 29.16 ?  500 PLM A C1  1 
HETATM 3343 O O1  . PLM C 3 .   ? 17.137  -35.696 -21.589 1.00 24.86 ?  500 PLM A O1  1 
HETATM 3344 O O2  . PLM C 3 .   ? 17.088  -37.359 -20.179 1.00 33.82 ?  500 PLM A O2  1 
HETATM 3345 C C2  . PLM C 3 .   ? 15.014  -36.618 -21.047 1.00 29.44 ?  500 PLM A C2  1 
HETATM 3346 C C3  . PLM C 3 .   ? 14.372  -35.392 -21.605 1.00 30.99 ?  500 PLM A C3  1 
HETATM 3347 C C4  . PLM C 3 .   ? 13.335  -34.805 -20.668 1.00 29.88 ?  500 PLM A C4  1 
HETATM 3348 C C5  . PLM C 3 .   ? 11.913  -35.032 -21.109 1.00 33.94 ?  500 PLM A C5  1 
HETATM 3349 C C6  . PLM C 3 .   ? 10.883  -34.304 -20.287 1.00 32.52 ?  500 PLM A C6  1 
HETATM 3350 C C7  . PLM C 3 .   ? 9.504   -34.317 -20.888 1.00 35.78 ?  500 PLM A C7  1 
HETATM 3351 C C8  . PLM C 3 .   ? 8.876   -32.957 -21.017 1.00 35.43 ?  500 PLM A C8  1 
HETATM 3352 C C9  . PLM C 3 .   ? 7.912   -32.624 -19.912 1.00 40.25 ?  500 PLM A C9  1 
HETATM 3353 C CA  . PLM C 3 .   ? 6.480   -32.966 -20.221 1.00 38.76 ?  500 PLM A CA  1 
HETATM 3354 C CB  . PLM C 3 .   ? 5.474   -32.159 -19.443 1.00 39.20 ?  500 PLM A CB  1 
HETATM 3355 C CC  . PLM C 3 .   ? 4.195   -31.877 -20.183 1.00 41.22 ?  500 PLM A CC  1 
HETATM 3356 C CD  . PLM C 3 .   ? 2.965   -31.882 -19.314 1.00 47.88 ?  500 PLM A CD  1 
HETATM 3357 C CE  . PLM C 3 .   ? 1.741   -31.304 -19.975 1.00 48.19 ?  500 PLM A CE  1 
HETATM 3358 C CF  . PLM C 3 .   ? 1.806   -31.272 -21.478 1.00 48.28 ?  500 PLM A CF  1 
HETATM 3359 C CG  . PLM C 3 .   ? 0.459   -31.403 -22.146 1.00 48.21 ?  500 PLM A CG  1 
HETATM 3360 O O   . HOH D 4 .   ? 5.129   -54.089 6.651   1.00 52.65 ?  601 HOH A O   1 
HETATM 3361 O O   . HOH D 4 .   ? 55.710  -22.554 -17.608 1.00 43.97 ?  602 HOH A O   1 
HETATM 3362 O O   . HOH D 4 .   ? 2.698   -56.158 -15.796 1.00 50.87 ?  603 HOH A O   1 
HETATM 3363 O O   . HOH D 4 .   ? 54.901  -18.773 -15.831 1.00 58.07 ?  604 HOH A O   1 
HETATM 3364 O O   . HOH D 4 .   ? 3.788   -44.480 -30.749 1.00 35.94 ?  605 HOH A O   1 
HETATM 3365 O O   . HOH D 4 .   ? 5.046   -47.996 -11.870 1.00 36.61 ?  606 HOH A O   1 
HETATM 3366 O O   . HOH D 4 .   ? 20.678  -25.977 4.610   1.00 49.13 ?  607 HOH A O   1 
HETATM 3367 O O   . HOH D 4 .   ? 33.154  -23.211 -3.995  1.00 33.22 ?  608 HOH A O   1 
HETATM 3368 O O   . HOH D 4 .   ? 1.387   -23.799 -16.293 1.00 44.02 ?  609 HOH A O   1 
HETATM 3369 O O   . HOH D 4 .   ? 22.694  -35.419 -28.666 1.00 28.46 ?  610 HOH A O   1 
HETATM 3370 O O   . HOH D 4 .   ? 59.596  -3.354  -10.321 1.00 49.59 ?  611 HOH A O   1 
HETATM 3371 O O   . HOH D 4 .   ? 8.169   -40.103 -3.845  1.00 38.39 ?  612 HOH A O   1 
HETATM 3372 O O   . HOH D 4 .   ? 0.630   -24.220 -9.277  1.00 37.54 ?  613 HOH A O   1 
HETATM 3373 O O   . HOH D 4 .   ? 28.809  -14.794 -12.722 1.00 42.35 ?  614 HOH A O   1 
HETATM 3374 O O   . HOH D 4 .   ? 12.936  -57.834 -9.162  1.00 48.13 ?  615 HOH A O   1 
HETATM 3375 O O   . HOH D 4 .   ? 18.524  -42.795 -10.289 1.00 34.89 ?  616 HOH A O   1 
HETATM 3376 O O   . HOH D 4 .   ? 3.777   -44.605 -26.998 1.00 38.06 ?  617 HOH A O   1 
HETATM 3377 O O   . HOH D 4 .   ? 13.211  -18.305 -5.266  1.00 38.91 ?  618 HOH A O   1 
HETATM 3378 O O   . HOH D 4 .   ? 35.112  -31.499 -21.710 1.00 44.10 ?  619 HOH A O   1 
HETATM 3379 O O   . HOH D 4 .   ? 9.483   -31.439 -12.933 1.00 32.48 ?  620 HOH A O   1 
HETATM 3380 O O   . HOH D 4 .   ? 0.299   -55.628 3.518   1.00 54.46 ?  621 HOH A O   1 
HETATM 3381 O O   . HOH D 4 .   ? 22.214  -28.090 -17.186 1.00 24.87 ?  622 HOH A O   1 
HETATM 3382 O O   . HOH D 4 .   ? 31.723  -21.474 -23.149 1.00 34.61 ?  623 HOH A O   1 
HETATM 3383 O O   . HOH D 4 .   ? 31.984  -29.058 0.156   1.00 39.83 ?  624 HOH A O   1 
HETATM 3384 O O   . HOH D 4 .   ? 27.226  -22.557 -30.210 1.00 31.26 ?  625 HOH A O   1 
HETATM 3385 O O   . HOH D 4 .   ? -2.735  -25.844 -24.667 1.00 46.20 ?  626 HOH A O   1 
HETATM 3386 O O   . HOH D 4 .   ? 33.419  -43.426 2.569   1.00 48.04 ?  627 HOH A O   1 
HETATM 3387 O O   . HOH D 4 .   ? 18.176  -51.175 -22.629 1.00 35.63 ?  628 HOH A O   1 
HETATM 3388 O O   . HOH D 4 .   ? 45.807  -3.759  -3.712  1.00 37.40 ?  629 HOH A O   1 
HETATM 3389 O O   . HOH D 4 .   ? -6.852  -40.156 -11.629 1.00 43.21 ?  630 HOH A O   1 
HETATM 3390 O O   . HOH D 4 .   ? 12.281  -33.505 -30.323 1.00 30.12 ?  631 HOH A O   1 
HETATM 3391 O O   . HOH D 4 .   ? 6.208   -42.997 -7.751  1.00 30.20 ?  632 HOH A O   1 
HETATM 3392 O O   . HOH D 4 .   ? 18.021  -48.642 -7.896  1.00 34.21 ?  633 HOH A O   1 
HETATM 3393 O O   . HOH D 4 .   ? 18.663  -27.854 -8.444  1.00 27.07 ?  634 HOH A O   1 
HETATM 3394 O O   . HOH D 4 .   ? 34.798  -34.989 -19.472 1.00 35.86 ?  635 HOH A O   1 
HETATM 3395 O O   . HOH D 4 .   ? 14.967  -20.335 -9.378  1.00 36.86 ?  636 HOH A O   1 
HETATM 3396 O O   . HOH D 4 .   ? 8.866   -62.366 -13.515 1.00 48.89 ?  637 HOH A O   1 
HETATM 3397 O O   . HOH D 4 .   ? 19.862  -31.573 3.376   1.00 36.24 ?  638 HOH A O   1 
HETATM 3398 O O   . HOH D 4 .   ? 10.793  -39.509 -30.003 1.00 31.44 ?  639 HOH A O   1 
HETATM 3399 O O   . HOH D 4 .   ? 16.398  -26.799 -19.209 1.00 31.72 ?  640 HOH A O   1 
HETATM 3400 O O   . HOH D 4 .   ? 8.213   -45.836 -20.863 1.00 32.67 ?  641 HOH A O   1 
HETATM 3401 O O   . HOH D 4 .   ? 11.358  -29.153 -13.472 1.00 27.80 ?  642 HOH A O   1 
HETATM 3402 O O   . HOH D 4 .   ? 6.808   -26.246 -16.062 1.00 35.20 ?  643 HOH A O   1 
HETATM 3403 O O   . HOH D 4 .   ? 25.746  -52.010 -14.914 1.00 44.54 ?  644 HOH A O   1 
HETATM 3404 O O   . HOH D 4 .   ? 8.434   -50.081 -4.117  1.00 39.01 ?  645 HOH A O   1 
HETATM 3405 O O   . HOH D 4 .   ? 25.571  -52.926 -12.100 1.00 37.79 ?  646 HOH A O   1 
HETATM 3406 O O   . HOH D 4 .   ? 11.711  -27.008 -5.669  1.00 29.09 ?  647 HOH A O   1 
HETATM 3407 O O   . HOH D 4 .   ? 25.877  -59.479 -16.813 1.00 44.88 ?  648 HOH A O   1 
HETATM 3408 O O   . HOH D 4 .   ? 8.830   -58.942 -18.240 1.00 45.94 ?  649 HOH A O   1 
HETATM 3409 O O   . HOH D 4 .   ? 21.900  -43.428 -16.049 1.00 37.31 ?  650 HOH A O   1 
HETATM 3410 O O   . HOH D 4 .   ? 15.639  -52.575 -17.073 1.00 39.23 ?  651 HOH A O   1 
HETATM 3411 O O   . HOH D 4 .   ? 17.069  -47.156 -15.277 1.00 28.81 ?  652 HOH A O   1 
HETATM 3412 O O   . HOH D 4 .   ? 18.914  -41.957 -7.429  1.00 33.39 ?  653 HOH A O   1 
HETATM 3413 O O   . HOH D 4 .   ? 24.585  -23.497 -4.442  1.00 26.13 ?  654 HOH A O   1 
HETATM 3414 O O   . HOH D 4 .   ? 15.937  -42.724 -32.266 1.00 37.76 ?  655 HOH A O   1 
HETATM 3415 O O   . HOH D 4 .   ? 52.415  -9.996  -9.999  1.00 36.91 ?  656 HOH A O   1 
HETATM 3416 O O   . HOH D 4 .   ? 28.903  -22.991 -1.176  1.00 27.74 ?  657 HOH A O   1 
HETATM 3417 O O   . HOH D 4 .   ? 23.493  -30.458 -22.087 1.00 25.67 ?  658 HOH A O   1 
HETATM 3418 O O   . HOH D 4 .   ? -0.243  -43.296 -10.517 1.00 36.51 ?  659 HOH A O   1 
HETATM 3419 O O   . HOH D 4 .   ? 19.655  -25.519 -26.304 1.00 27.73 ?  660 HOH A O   1 
HETATM 3420 O O   . HOH D 4 .   ? 13.592  -30.701 -29.653 1.00 40.63 ?  661 HOH A O   1 
HETATM 3421 O O   . HOH D 4 .   ? -1.455  -43.741 -3.431  1.00 53.71 ?  662 HOH A O   1 
HETATM 3422 O O   . HOH D 4 .   ? 15.306  -56.016 -9.074  1.00 42.40 ?  663 HOH A O   1 
HETATM 3423 O O   . HOH D 4 .   ? -1.683  -32.608 -8.610  1.00 38.74 ?  664 HOH A O   1 
HETATM 3424 O O   . HOH D 4 .   ? 29.438  -18.941 -6.702  1.00 27.89 ?  665 HOH A O   1 
HETATM 3425 O O   . HOH D 4 .   ? 12.959  -44.990 -10.616 1.00 33.83 ?  666 HOH A O   1 
HETATM 3426 O O   . HOH D 4 .   ? 13.581  -27.020 -18.904 1.00 31.17 ?  667 HOH A O   1 
HETATM 3427 O O   . HOH D 4 .   ? 47.689  -17.400 -19.302 1.00 39.76 ?  668 HOH A O   1 
HETATM 3428 O O   . HOH D 4 .   ? 6.086   -34.534 -8.375  1.00 34.34 ?  669 HOH A O   1 
HETATM 3429 O O   . HOH D 4 .   ? 4.435   -48.679 -32.382 1.00 40.09 ?  670 HOH A O   1 
HETATM 3430 O O   . HOH D 4 .   ? 23.124  -39.597 -14.937 1.00 28.42 ?  671 HOH A O   1 
HETATM 3431 O O   . HOH D 4 .   ? 1.300   -35.815 -34.637 1.00 41.85 ?  672 HOH A O   1 
HETATM 3432 O O   . HOH D 4 .   ? 29.552  -20.079 -17.668 1.00 41.73 ?  673 HOH A O   1 
HETATM 3433 O O   . HOH D 4 .   ? 33.415  -24.071 -7.733  1.00 29.45 ?  674 HOH A O   1 
HETATM 3434 O O   . HOH D 4 .   ? 44.064  -27.675 -13.902 1.00 50.58 ?  675 HOH A O   1 
HETATM 3435 O O   . HOH D 4 .   ? 19.669  -41.655 -3.466  1.00 27.91 ?  676 HOH A O   1 
HETATM 3436 O O   . HOH D 4 .   ? 2.962   -46.448 -12.791 1.00 37.28 ?  677 HOH A O   1 
HETATM 3437 O O   . HOH D 4 .   ? 8.123   -42.345 -27.114 1.00 28.08 ?  678 HOH A O   1 
HETATM 3438 O O   . HOH D 4 .   ? 9.523   -51.517 -2.160  1.00 41.32 ?  679 HOH A O   1 
HETATM 3439 O O   . HOH D 4 .   ? 44.880  4.499   -3.122  1.00 36.88 ?  680 HOH A O   1 
HETATM 3440 O O   . HOH D 4 .   ? 27.461  -38.082 -17.674 1.00 34.06 ?  681 HOH A O   1 
HETATM 3441 O O   . HOH D 4 .   ? 27.161  -28.590 7.919   1.00 54.87 ?  682 HOH A O   1 
HETATM 3442 O O   . HOH D 4 .   ? 21.662  -29.057 -31.944 1.00 35.13 ?  683 HOH A O   1 
HETATM 3443 O O   . HOH D 4 .   ? 14.979  -42.485 8.439   1.00 41.04 ?  684 HOH A O   1 
HETATM 3444 O O   . HOH D 4 .   ? 60.534  -12.488 -21.983 1.00 53.66 ?  685 HOH A O   1 
HETATM 3445 O O   . HOH D 4 .   ? 24.479  -45.863 -18.930 1.00 28.32 ?  686 HOH A O   1 
HETATM 3446 O O   . HOH D 4 .   ? -2.212  -41.312 -11.998 1.00 40.92 ?  687 HOH A O   1 
HETATM 3447 O O   . HOH D 4 .   ? 3.723   -27.568 -29.180 1.00 41.03 ?  688 HOH A O   1 
HETATM 3448 O O   . HOH D 4 .   ? 17.540  -27.327 -0.298  1.00 33.27 ?  689 HOH A O   1 
HETATM 3449 O O   . HOH D 4 .   ? 13.896  -16.136 -15.284 1.00 39.14 ?  690 HOH A O   1 
HETATM 3450 O O   . HOH D 4 .   ? -9.293  -24.381 -16.559 1.00 52.47 ?  691 HOH A O   1 
HETATM 3451 O O   . HOH D 4 .   ? 31.211  -33.027 5.248   1.00 34.10 ?  692 HOH A O   1 
HETATM 3452 O O   . HOH D 4 .   ? 14.114  -26.971 0.461   1.00 31.65 ?  693 HOH A O   1 
HETATM 3453 O O   . HOH D 4 .   ? 13.943  -37.903 -14.663 1.00 27.86 ?  694 HOH A O   1 
HETATM 3454 O O   . HOH D 4 .   ? 14.160  -40.516 -15.080 1.00 29.70 ?  695 HOH A O   1 
HETATM 3455 O O   . HOH D 4 .   ? 25.664  -15.869 -5.394  1.00 40.11 ?  696 HOH A O   1 
HETATM 3456 O O   . HOH D 4 .   ? 32.272  -54.615 0.091   1.00 51.04 ?  697 HOH A O   1 
HETATM 3457 O O   . HOH D 4 .   ? 34.053  -26.998 -1.068  1.00 36.15 ?  698 HOH A O   1 
HETATM 3458 O O   . HOH D 4 .   ? 27.033  -58.113 -7.197  1.00 52.41 ?  699 HOH A O   1 
HETATM 3459 O O   . HOH D 4 .   ? 12.581  -53.904 -24.561 1.00 45.94 ?  700 HOH A O   1 
HETATM 3460 O O   . HOH D 4 .   ? 19.874  -53.640 -7.893  1.00 35.73 ?  701 HOH A O   1 
HETATM 3461 O O   . HOH D 4 .   ? 30.671  -23.917 -7.082  1.00 31.14 ?  702 HOH A O   1 
HETATM 3462 O O   . HOH D 4 .   ? 47.045  -9.149  -8.778  1.00 33.60 ?  703 HOH A O   1 
HETATM 3463 O O   . HOH D 4 .   ? 8.999   -39.533 8.765   1.00 42.38 ?  704 HOH A O   1 
HETATM 3464 O O   . HOH D 4 .   ? -11.753 -38.957 -15.003 1.00 46.20 ?  705 HOH A O   1 
HETATM 3465 O O   . HOH D 4 .   ? 31.436  -48.548 -19.729 1.00 46.40 ?  706 HOH A O   1 
HETATM 3466 O O   . HOH D 4 .   ? 5.605   -44.364 -33.017 1.00 39.35 ?  707 HOH A O   1 
HETATM 3467 O O   . HOH D 4 .   ? 32.621  -19.941 -5.168  1.00 32.56 ?  708 HOH A O   1 
HETATM 3468 O O   . HOH D 4 .   ? 23.592  -29.740 3.765   1.00 47.45 ?  709 HOH A O   1 
HETATM 3469 O O   . HOH D 4 .   ? -2.503  -21.818 -12.600 1.00 48.93 ?  710 HOH A O   1 
HETATM 3470 O O   . HOH D 4 .   ? 2.582   -42.044 -32.569 1.00 43.82 ?  711 HOH A O   1 
HETATM 3471 O O   . HOH D 4 .   ? 49.498  6.994   -7.844  1.00 32.90 ?  712 HOH A O   1 
HETATM 3472 O O   . HOH D 4 .   ? 2.303   -21.435 -3.202  1.00 58.03 ?  713 HOH A O   1 
HETATM 3473 O O   . HOH D 4 .   ? 21.311  -24.986 1.112   1.00 39.20 ?  714 HOH A O   1 
HETATM 3474 O O   . HOH D 4 .   ? 22.967  -18.024 -16.684 1.00 36.95 ?  715 HOH A O   1 
HETATM 3475 O O   . HOH D 4 .   ? 4.946   -39.043 7.474   1.00 55.17 ?  716 HOH A O   1 
HETATM 3476 O O   . HOH D 4 .   ? 23.710  -42.245 -22.700 1.00 30.00 ?  717 HOH A O   1 
HETATM 3477 O O   . HOH D 4 .   ? 29.680  -33.005 7.864   1.00 54.23 ?  718 HOH A O   1 
HETATM 3478 O O   . HOH D 4 .   ? 24.634  -63.019 -10.998 1.00 42.75 ?  719 HOH A O   1 
HETATM 3479 O O   . HOH D 4 .   ? 16.464  -21.555 0.187   1.00 38.63 ?  720 HOH A O   1 
HETATM 3480 O O   . HOH D 4 .   ? 3.556   -48.189 -15.815 1.00 36.81 ?  721 HOH A O   1 
HETATM 3481 O O   . HOH D 4 .   ? 4.631   -49.831 -14.453 1.00 37.58 ?  722 HOH A O   1 
HETATM 3482 O O   . HOH D 4 .   ? 17.375  -22.844 -25.308 1.00 32.39 ?  723 HOH A O   1 
HETATM 3483 O O   . HOH D 4 .   ? 32.244  -18.616 -17.474 0.50 40.09 ?  724 HOH A O   1 
HETATM 3484 O O   . HOH D 4 .   ? 17.027  -46.430 -29.146 1.00 29.00 ?  725 HOH A O   1 
HETATM 3485 O O   . HOH D 4 .   ? 20.595  -22.295 -27.776 1.00 40.70 ?  726 HOH A O   1 
HETATM 3486 O O   . HOH D 4 .   ? 13.818  -32.274 -34.156 1.00 38.05 ?  727 HOH A O   1 
HETATM 3487 O O   . HOH D 4 .   ? 6.752   -22.928 -22.857 1.00 45.93 ?  728 HOH A O   1 
HETATM 3488 O O   . HOH D 4 .   ? 15.547  -48.301 9.288   1.00 44.24 ?  729 HOH A O   1 
HETATM 3489 O O   . HOH D 4 .   ? 12.479  -16.816 -17.297 1.00 41.91 ?  730 HOH A O   1 
HETATM 3490 O O   . HOH D 4 .   ? 14.107  -17.263 -1.800  1.00 58.63 ?  731 HOH A O   1 
HETATM 3491 O O   . HOH D 4 .   ? 7.363   -53.132 -25.248 1.00 50.93 ?  732 HOH A O   1 
HETATM 3492 O O   . HOH D 4 .   ? 22.947  -34.124 -34.858 1.00 38.08 ?  733 HOH A O   1 
HETATM 3493 O O   . HOH D 4 .   ? 19.962  -32.023 -33.823 1.00 39.65 ?  734 HOH A O   1 
HETATM 3494 O O   . HOH D 4 .   ? 6.440   -41.766 -35.202 1.00 42.26 ?  735 HOH A O   1 
HETATM 3495 O O   . HOH D 4 .   ? 34.974  -24.034 -14.284 1.00 40.96 ?  736 HOH A O   1 
HETATM 3496 O O   . HOH D 4 .   ? -14.302 -33.296 -28.878 1.00 48.37 ?  737 HOH A O   1 
HETATM 3497 O O   . HOH D 4 .   ? 55.671  1.489   -7.710  1.00 41.71 ?  738 HOH A O   1 
HETATM 3498 O O   . HOH D 4 .   ? 5.429   -36.592 4.393   1.00 48.27 ?  739 HOH A O   1 
HETATM 3499 O O   . HOH D 4 .   ? 8.916   -52.030 -26.917 1.00 40.55 ?  740 HOH A O   1 
HETATM 3500 O O   . HOH D 4 .   ? 26.153  -40.161 14.241  1.00 52.62 ?  741 HOH A O   1 
HETATM 3501 O O   . HOH D 4 .   ? 14.156  -16.845 -21.678 1.00 42.42 ?  742 HOH A O   1 
HETATM 3502 O O   . HOH D 4 .   ? 32.304  -27.122 -26.729 1.00 34.20 ?  743 HOH A O   1 
HETATM 3503 O O   . HOH D 4 .   ? 10.898  -61.252 -2.940  1.00 54.87 ?  744 HOH A O   1 
HETATM 3504 O O   . HOH D 4 .   ? 52.761  -19.134 -14.248 1.00 47.17 ?  745 HOH A O   1 
HETATM 3505 O O   . HOH D 4 .   ? -1.793  -26.123 -28.743 1.00 48.26 ?  746 HOH A O   1 
HETATM 3506 O O   . HOH D 4 .   ? 24.310  -16.687 0.296   1.00 45.24 ?  747 HOH A O   1 
HETATM 3507 O O   . HOH D 4 .   ? 25.533  -35.621 -29.498 1.00 32.88 ?  748 HOH A O   1 
HETATM 3508 O O   . HOH D 4 .   ? 18.840  -41.532 8.184   1.00 41.26 ?  749 HOH A O   1 
HETATM 3509 O O   . HOH D 4 .   ? 36.393  -25.482 -11.917 1.00 45.36 ?  750 HOH A O   1 
HETATM 3510 O O   . HOH D 4 .   ? -7.247  -35.161 -32.799 1.00 47.39 ?  751 HOH A O   1 
HETATM 3511 O O   . HOH D 4 .   ? 24.628  -18.194 -19.295 1.00 39.82 ?  752 HOH A O   1 
HETATM 3512 O O   . HOH D 4 .   ? 9.862   -50.691 13.280  1.00 53.27 ?  753 HOH A O   1 
HETATM 3513 O O   . HOH D 4 .   ? 24.776  -16.408 -15.118 1.00 42.90 ?  754 HOH A O   1 
HETATM 3514 O O   . HOH D 4 .   ? 20.678  -28.851 2.801   1.00 47.53 ?  755 HOH A O   1 
HETATM 3515 O O   . HOH D 4 .   ? -0.124  -50.392 -27.527 1.00 49.17 ?  756 HOH A O   1 
HETATM 3516 O O   . HOH D 4 .   ? 29.145  -17.651 -4.104  1.00 36.58 ?  757 HOH A O   1 
HETATM 3517 O O   . HOH D 4 .   ? 15.862  -32.782 -31.999 1.00 47.28 ?  758 HOH A O   1 
HETATM 3518 O O   . HOH D 4 .   ? -9.836  -35.996 -31.424 1.00 42.51 ?  759 HOH A O   1 
HETATM 3519 O O   . HOH D 4 .   ? 8.643   -22.082 -24.114 1.00 42.85 ?  760 HOH A O   1 
HETATM 3520 O O   . HOH D 4 .   ? 17.545  -24.547 0.058   1.00 39.46 ?  761 HOH A O   1 
HETATM 3521 O O   . HOH D 4 .   ? 8.423   -48.443 13.356  1.00 54.07 ?  762 HOH A O   1 
HETATM 3522 O O   . HOH D 4 .   ? 52.130  5.782   -7.846  1.00 42.19 ?  763 HOH A O   1 
HETATM 3523 O O   . HOH D 4 .   ? 39.699  -16.826 -7.079  1.00 47.02 ?  764 HOH A O   1 
HETATM 3524 O O   . HOH D 4 .   ? 11.711  -27.746 0.023   1.00 51.23 ?  765 HOH A O   1 
HETATM 3525 O O   . HOH D 4 .   ? 38.453  1.939   -1.489  1.00 36.64 ?  766 HOH A O   1 
HETATM 3526 O O   . HOH D 4 .   ? 1.288   -52.031 -25.715 1.00 49.67 ?  767 HOH A O   1 
HETATM 3527 O O   . HOH D 4 .   ? 15.069  -17.779 -7.340  1.00 39.01 ?  768 HOH A O   1 
HETATM 3528 O O   . HOH D 4 .   ? 20.461  -27.512 0.300   1.00 35.62 ?  769 HOH A O   1 
HETATM 3529 O O   . HOH D 4 .   ? 4.220   -22.178 -16.438 1.00 52.76 ?  770 HOH A O   1 
HETATM 3530 O O   . HOH D 4 .   ? 23.646  -25.697 2.640   1.00 43.10 ?  771 HOH A O   1 
HETATM 3531 O O   . HOH D 4 .   ? 44.314  -22.601 -22.354 1.00 51.90 ?  772 HOH A O   1 
HETATM 3532 O O   . HOH D 4 .   ? 1.433   -26.904 -30.795 1.00 49.11 ?  773 HOH A O   1 
HETATM 3533 O O   . HOH D 4 .   ? 14.628  -15.362 -8.270  1.00 43.67 ?  774 HOH A O   1 
HETATM 3534 O O   . HOH D 4 .   ? -5.110  -41.769 -11.172 1.00 39.16 ?  775 HOH A O   1 
HETATM 3535 O O   . HOH D 4 .   ? -1.320  -21.833 -9.943  1.00 51.23 ?  776 HOH A O   1 
HETATM 3536 O O   . HOH D 4 .   ? 12.614  -29.638 -32.880 1.00 42.39 ?  777 HOH A O   1 
HETATM 3537 O O   . HOH D 4 .   ? 14.027  -24.300 1.276   1.00 45.25 ?  778 HOH A O   1 
HETATM 3538 O O   . HOH D 4 .   ? 18.042  -23.488 -27.675 1.00 42.93 ?  779 HOH A O   1 
HETATM 3539 O O   . HOH D 4 .   ? -1.146  -23.513 -25.165 1.00 45.37 ?  780 HOH A O   1 
HETATM 3540 O O   . HOH D 4 .   ? 13.477  -22.560 -23.988 1.00 42.60 ?  781 HOH A O   1 
HETATM 3541 O O   . HOH D 4 .   ? 46.084  6.785   -0.679  1.00 40.89 ?  782 HOH A O   1 
HETATM 3542 O O   . HOH D 4 .   ? 14.548  -21.951 -26.040 1.00 42.47 ?  783 HOH A O   1 
HETATM 3543 O O   . HOH D 4 .   ? -13.019 -38.783 -12.292 1.00 52.54 ?  784 HOH A O   1 
HETATM 3544 O O   . HOH D 4 .   ? 12.864  -22.501 -28.524 1.00 50.40 ?  785 HOH A O   1 
# 
