data_9KSW
# 
_entry.id   9KSW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9KSW         pdb_00009ksw 10.2210/pdb9ksw/pdb 
WWPDB D_1300054219 ?            ?                   
# 
_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       2025-06-25 
_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                        9KSW 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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              yemin@bjmu.edu.cn 
_pdbx_contact_author.name_first         Ye 
_pdbx_contact_author.name_last          Min 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9952-2380 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wang, H.T.' 1 0000-0002-5684-8655 
'Wang, Z.L.' 2 0000-0002-7875-0704 
'Ye, M.'     3 0000-0002-9952-2380 
# 
_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            J.Am.Chem.Soc. 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Insights into the Mechanisms of Sugar Acceptor Selectivity of Plant Flavonoid Apiosyltransferases.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.5c03771 
_citation.pdbx_database_id_PubMed   40459876 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, H.T.' 1  ?                   
primary 'Wang, Z.L.' 2  0000-0002-7875-0704 
primary 'Chen, N.H.' 3  ?                   
primary 'Huang, W.'  4  0009-0005-4519-910X 
primary 'Zou, J.L.'  5  ?                   
primary 'Tian, Y.G.' 6  ?                   
primary 'Ye, G.'     7  ?                   
primary 'Huang, J.'  8  ?                   
primary 'Wu, R.'     9  ?                   
primary 'Ye, M.'     10 0000-0002-9952-2380 
# 
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 'UDP-glycosyltransferase 79B30-like' 51554.344 1   ? ? ? ? 
2 non-polymer syn "URIDINE-5'-MONOPHOSPHATE"           324.181   1   ? ? ? ? 
3 non-polymer nat RUTIN                                610.517   1   ? ? ? ? 
4 water       nat water                                18.015    240 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        UGT79B91 
# 
_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       
;MDSPSSLHIAMFPWFAMGHLIPYLHLSNKLAKRGHKISFFTPKKTQTKLEQFNLYPNLITFYPLNVPHVDGLPFGAETTS
DVAISLGPILMTAMDQTQNQIELLLTQLKPQIIFFDFVFWLPKITQRLGIKSFLYFIINPATISYTTSPPRMFEAENLTE
VDLMKPPKGYPTSFNLQSHEAKHLASTRKIEFGSGIPFSVRSYNCLSLTDAIGFKGCREIEGPYVDYLQEQFGKPVLLSG
PVLPEQSKTALDEKWGSWLGGFKDGSLVYCALGSELKLKQDQFHELLLGLELTGFPFLAILKPPVGFETIEDALPEGFKE
RVKEKGIVHSGWIQQQLILEHPSVGCFVTHCGAGSITEGLVNNCQMVLLPQLNGDYIINARIMGRHLKVGVEVKKGEEDG
LFTKESVYEAVKIVMDDENEIGREVRSNHTKVRNLLLRHDLESSCLDTFCEKLQELVS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDSPSSLHIAMFPWFAMGHLIPYLHLSNKLAKRGHKISFFTPKKTQTKLEQFNLYPNLITFYPLNVPHVDGLPFGAETTS
DVAISLGPILMTAMDQTQNQIELLLTQLKPQIIFFDFVFWLPKITQRLGIKSFLYFIINPATISYTTSPPRMFEAENLTE
VDLMKPPKGYPTSFNLQSHEAKHLASTRKIEFGSGIPFSVRSYNCLSLTDAIGFKGCREIEGPYVDYLQEQFGKPVLLSG
PVLPEQSKTALDEKWGSWLGGFKDGSLVYCALGSELKLKQDQFHELLLGLELTGFPFLAILKPPVGFETIEDALPEGFKE
RVKEKGIVHSGWIQQQLILEHPSVGCFVTHCGAGSITEGLVNNCQMVLLPQLNGDYIINARIMGRHLKVGVEVKKGEEDG
LFTKESVYEAVKIVMDDENEIGREVRSNHTKVRNLLLRHDLESSCLDTFCEKLQELVS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "URIDINE-5'-MONOPHOSPHATE" U5P 
3 RUTIN                      RUT 
4 water                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   SER n 
1 4   PRO n 
1 5   SER n 
1 6   SER n 
1 7   LEU n 
1 8   HIS n 
1 9   ILE n 
1 10  ALA n 
1 11  MET n 
1 12  PHE n 
1 13  PRO n 
1 14  TRP n 
1 15  PHE n 
1 16  ALA n 
1 17  MET n 
1 18  GLY n 
1 19  HIS n 
1 20  LEU n 
1 21  ILE n 
1 22  PRO n 
1 23  TYR n 
1 24  LEU n 
1 25  HIS n 
1 26  LEU n 
1 27  SER n 
1 28  ASN n 
1 29  LYS n 
1 30  LEU n 
1 31  ALA n 
1 32  LYS n 
1 33  ARG n 
1 34  GLY n 
1 35  HIS n 
1 36  LYS n 
1 37  ILE n 
1 38  SER n 
1 39  PHE n 
1 40  PHE n 
1 41  THR n 
1 42  PRO n 
1 43  LYS n 
1 44  LYS n 
1 45  THR n 
1 46  GLN n 
1 47  THR n 
1 48  LYS n 
1 49  LEU n 
1 50  GLU n 
1 51  GLN n 
1 52  PHE n 
1 53  ASN n 
1 54  LEU n 
1 55  TYR n 
1 56  PRO n 
1 57  ASN n 
1 58  LEU n 
1 59  ILE n 
1 60  THR n 
1 61  PHE n 
1 62  TYR n 
1 63  PRO n 
1 64  LEU n 
1 65  ASN n 
1 66  VAL n 
1 67  PRO n 
1 68  HIS n 
1 69  VAL n 
1 70  ASP n 
1 71  GLY n 
1 72  LEU n 
1 73  PRO n 
1 74  PHE n 
1 75  GLY n 
1 76  ALA n 
1 77  GLU n 
1 78  THR n 
1 79  THR n 
1 80  SER n 
1 81  ASP n 
1 82  VAL n 
1 83  ALA n 
1 84  ILE n 
1 85  SER n 
1 86  LEU n 
1 87  GLY n 
1 88  PRO n 
1 89  ILE n 
1 90  LEU n 
1 91  MET n 
1 92  THR n 
1 93  ALA n 
1 94  MET n 
1 95  ASP n 
1 96  GLN n 
1 97  THR n 
1 98  GLN n 
1 99  ASN n 
1 100 GLN n 
1 101 ILE n 
1 102 GLU n 
1 103 LEU n 
1 104 LEU n 
1 105 LEU n 
1 106 THR n 
1 107 GLN n 
1 108 LEU n 
1 109 LYS n 
1 110 PRO n 
1 111 GLN n 
1 112 ILE n 
1 113 ILE n 
1 114 PHE n 
1 115 PHE n 
1 116 ASP n 
1 117 PHE n 
1 118 VAL n 
1 119 PHE n 
1 120 TRP n 
1 121 LEU n 
1 122 PRO n 
1 123 LYS n 
1 124 ILE n 
1 125 THR n 
1 126 GLN n 
1 127 ARG n 
1 128 LEU n 
1 129 GLY n 
1 130 ILE n 
1 131 LYS n 
1 132 SER n 
1 133 PHE n 
1 134 LEU n 
1 135 TYR n 
1 136 PHE n 
1 137 ILE n 
1 138 ILE n 
1 139 ASN n 
1 140 PRO n 
1 141 ALA n 
1 142 THR n 
1 143 ILE n 
1 144 SER n 
1 145 TYR n 
1 146 THR n 
1 147 THR n 
1 148 SER n 
1 149 PRO n 
1 150 PRO n 
1 151 ARG n 
1 152 MET n 
1 153 PHE n 
1 154 GLU n 
1 155 ALA n 
1 156 GLU n 
1 157 ASN n 
1 158 LEU n 
1 159 THR n 
1 160 GLU n 
1 161 VAL n 
1 162 ASP n 
1 163 LEU n 
1 164 MET n 
1 165 LYS n 
1 166 PRO n 
1 167 PRO n 
1 168 LYS n 
1 169 GLY n 
1 170 TYR n 
1 171 PRO n 
1 172 THR n 
1 173 SER n 
1 174 PHE n 
1 175 ASN n 
1 176 LEU n 
1 177 GLN n 
1 178 SER n 
1 179 HIS n 
1 180 GLU n 
1 181 ALA n 
1 182 LYS n 
1 183 HIS n 
1 184 LEU n 
1 185 ALA n 
1 186 SER n 
1 187 THR n 
1 188 ARG n 
1 189 LYS n 
1 190 ILE n 
1 191 GLU n 
1 192 PHE n 
1 193 GLY n 
1 194 SER n 
1 195 GLY n 
1 196 ILE n 
1 197 PRO n 
1 198 PHE n 
1 199 SER n 
1 200 VAL n 
1 201 ARG n 
1 202 SER n 
1 203 TYR n 
1 204 ASN n 
1 205 CYS n 
1 206 LEU n 
1 207 SER n 
1 208 LEU n 
1 209 THR n 
1 210 ASP n 
1 211 ALA n 
1 212 ILE n 
1 213 GLY n 
1 214 PHE n 
1 215 LYS n 
1 216 GLY n 
1 217 CYS n 
1 218 ARG n 
1 219 GLU n 
1 220 ILE n 
1 221 GLU n 
1 222 GLY n 
1 223 PRO n 
1 224 TYR n 
1 225 VAL n 
1 226 ASP n 
1 227 TYR n 
1 228 LEU n 
1 229 GLN n 
1 230 GLU n 
1 231 GLN n 
1 232 PHE n 
1 233 GLY n 
1 234 LYS n 
1 235 PRO n 
1 236 VAL n 
1 237 LEU n 
1 238 LEU n 
1 239 SER n 
1 240 GLY n 
1 241 PRO n 
1 242 VAL n 
1 243 LEU n 
1 244 PRO n 
1 245 GLU n 
1 246 GLN n 
1 247 SER n 
1 248 LYS n 
1 249 THR n 
1 250 ALA n 
1 251 LEU n 
1 252 ASP n 
1 253 GLU n 
1 254 LYS n 
1 255 TRP n 
1 256 GLY n 
1 257 SER n 
1 258 TRP n 
1 259 LEU n 
1 260 GLY n 
1 261 GLY n 
1 262 PHE n 
1 263 LYS n 
1 264 ASP n 
1 265 GLY n 
1 266 SER n 
1 267 LEU n 
1 268 VAL n 
1 269 TYR n 
1 270 CYS n 
1 271 ALA n 
1 272 LEU n 
1 273 GLY n 
1 274 SER n 
1 275 GLU n 
1 276 LEU n 
1 277 LYS n 
1 278 LEU n 
1 279 LYS n 
1 280 GLN n 
1 281 ASP n 
1 282 GLN n 
1 283 PHE n 
1 284 HIS n 
1 285 GLU n 
1 286 LEU n 
1 287 LEU n 
1 288 LEU n 
1 289 GLY n 
1 290 LEU n 
1 291 GLU n 
1 292 LEU n 
1 293 THR n 
1 294 GLY n 
1 295 PHE n 
1 296 PRO n 
1 297 PHE n 
1 298 LEU n 
1 299 ALA n 
1 300 ILE n 
1 301 LEU n 
1 302 LYS n 
1 303 PRO n 
1 304 PRO n 
1 305 VAL n 
1 306 GLY n 
1 307 PHE n 
1 308 GLU n 
1 309 THR n 
1 310 ILE n 
1 311 GLU n 
1 312 ASP n 
1 313 ALA n 
1 314 LEU n 
1 315 PRO n 
1 316 GLU n 
1 317 GLY n 
1 318 PHE n 
1 319 LYS n 
1 320 GLU n 
1 321 ARG n 
1 322 VAL n 
1 323 LYS n 
1 324 GLU n 
1 325 LYS n 
1 326 GLY n 
1 327 ILE n 
1 328 VAL n 
1 329 HIS n 
1 330 SER n 
1 331 GLY n 
1 332 TRP n 
1 333 ILE n 
1 334 GLN n 
1 335 GLN n 
1 336 GLN n 
1 337 LEU n 
1 338 ILE n 
1 339 LEU n 
1 340 GLU n 
1 341 HIS n 
1 342 PRO n 
1 343 SER n 
1 344 VAL n 
1 345 GLY n 
1 346 CYS n 
1 347 PHE n 
1 348 VAL n 
1 349 THR n 
1 350 HIS n 
1 351 CYS n 
1 352 GLY n 
1 353 ALA n 
1 354 GLY n 
1 355 SER n 
1 356 ILE n 
1 357 THR n 
1 358 GLU n 
1 359 GLY n 
1 360 LEU n 
1 361 VAL n 
1 362 ASN n 
1 363 ASN n 
1 364 CYS n 
1 365 GLN n 
1 366 MET n 
1 367 VAL n 
1 368 LEU n 
1 369 LEU n 
1 370 PRO n 
1 371 GLN n 
1 372 LEU n 
1 373 ASN n 
1 374 GLY n 
1 375 ASP n 
1 376 TYR n 
1 377 ILE n 
1 378 ILE n 
1 379 ASN n 
1 380 ALA n 
1 381 ARG n 
1 382 ILE n 
1 383 MET n 
1 384 GLY n 
1 385 ARG n 
1 386 HIS n 
1 387 LEU n 
1 388 LYS n 
1 389 VAL n 
1 390 GLY n 
1 391 VAL n 
1 392 GLU n 
1 393 VAL n 
1 394 LYS n 
1 395 LYS n 
1 396 GLY n 
1 397 GLU n 
1 398 GLU n 
1 399 ASP n 
1 400 GLY n 
1 401 LEU n 
1 402 PHE n 
1 403 THR n 
1 404 LYS n 
1 405 GLU n 
1 406 SER n 
1 407 VAL n 
1 408 TYR n 
1 409 GLU n 
1 410 ALA n 
1 411 VAL n 
1 412 LYS n 
1 413 ILE n 
1 414 VAL n 
1 415 MET n 
1 416 ASP n 
1 417 ASP n 
1 418 GLU n 
1 419 ASN n 
1 420 GLU n 
1 421 ILE n 
1 422 GLY n 
1 423 ARG n 
1 424 GLU n 
1 425 VAL n 
1 426 ARG n 
1 427 SER n 
1 428 ASN n 
1 429 HIS n 
1 430 THR n 
1 431 LYS n 
1 432 VAL n 
1 433 ARG n 
1 434 ASN n 
1 435 LEU n 
1 436 LEU n 
1 437 LEU n 
1 438 ARG n 
1 439 HIS n 
1 440 ASP n 
1 441 LEU n 
1 442 GLU n 
1 443 SER n 
1 444 SER n 
1 445 CYS n 
1 446 LEU n 
1 447 ASP n 
1 448 THR n 
1 449 PHE n 
1 450 CYS n 
1 451 GLU n 
1 452 LYS n 
1 453 LEU n 
1 454 GLN n 
1 455 GLU n 
1 456 LEU n 
1 457 VAL n 
1 458 SER 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                   458 
_entity_src_gen.gene_src_common_name               chickpea 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 LOC101505166 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Cicer arietinum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3827 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                    ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                   ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                 ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'            ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                   ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                  ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'            ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                    ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                  ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                      ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                 ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                    ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                     ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                 ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE              ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                    ? 'C5 H9 N O2'     115.130 
RUT non-polymer         . RUTIN                      
'2-(3,4-DIHYDROXYPHENYL)-5,7-DIHYDROXY-4-OXO-4H-CHROMEN-3-YL 6-O-(6-DEOXY-ALPHA-L-MANNOPYRANOSYL)-BETA-D-GLUCOPYRANOSIDE' 
'C27 H30 O16'    610.517 
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 
U5P non-polymer         . "URIDINE-5'-MONOPHOSPHATE" ? 'C9 H13 N2 O9 P' 324.181 
VAL 'L-peptide linking' y VALINE                     ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ASP 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   ?   ?   ?   A . n 
A 1 4   PRO 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   SER 6   6   6   SER SER A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   HIS 8   8   8   HIS HIS A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  MET 11  11  11  MET MET A . n 
A 1 12  PHE 12  12  12  PHE PHE A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  TRP 14  14  14  TRP TRP A . n 
A 1 15  PHE 15  15  15  PHE PHE A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  HIS 19  19  19  HIS HIS A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  PRO 22  22  22  PRO PRO A . n 
A 1 23  TYR 23  23  23  TYR TYR A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  HIS 25  25  25  HIS HIS A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  LYS 32  32  32  LYS LYS A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  HIS 35  35  35  HIS HIS A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  GLN 46  46  46  GLN GLN A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  GLN 51  51  51  GLN GLN A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  PRO 56  56  56  PRO PRO A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  PHE 61  61  61  PHE PHE A . n 
A 1 62  TYR 62  62  62  TYR TYR A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  PRO 67  67  67  PRO PRO A . n 
A 1 68  HIS 68  68  68  HIS HIS A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  ASP 70  70  70  ASP ASP A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  THR 78  78  78  THR THR A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  PRO 88  88  88  PRO PRO A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  MET 91  91  91  MET MET A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  MET 94  94  94  MET MET A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  GLN 98  98  98  GLN GLN A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 GLN 100 100 100 GLN GLN A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 PRO 110 110 110 PRO PRO A . n 
A 1 111 GLN 111 111 111 GLN GLN A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 PHE 115 115 115 PHE PHE A . n 
A 1 116 ASP 116 116 116 ASP ASP A . n 
A 1 117 PHE 117 117 117 PHE PHE A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 TRP 120 120 120 TRP TRP A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 LYS 123 123 123 LYS LYS A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 GLN 126 126 126 GLN GLN A . n 
A 1 127 ARG 127 127 127 ARG ARG A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 LYS 131 131 131 LYS LYS A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 TYR 135 135 135 TYR TYR A . n 
A 1 136 PHE 136 136 136 PHE PHE A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 PRO 140 140 140 PRO PRO A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 TYR 145 145 145 TYR TYR A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 PRO 150 150 150 PRO PRO A . n 
A 1 151 ARG 151 151 151 ARG ARG A . n 
A 1 152 MET 152 152 152 MET MET A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 GLU 156 156 156 GLU GLU A . n 
A 1 157 ASN 157 157 157 ASN ASN A . n 
A 1 158 LEU 158 158 158 LEU LEU A . n 
A 1 159 THR 159 159 159 THR THR A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 MET 164 164 164 MET MET A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 PRO 167 167 167 PRO PRO A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 PRO 171 171 171 PRO PRO A . n 
A 1 172 THR 172 172 172 THR THR A . n 
A 1 173 SER 173 173 173 SER SER A . n 
A 1 174 PHE 174 174 174 PHE PHE A . n 
A 1 175 ASN 175 175 175 ASN ASN A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 GLN 177 177 177 GLN GLN A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 HIS 179 179 179 HIS HIS A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 ALA 181 181 181 ALA ALA A . n 
A 1 182 LYS 182 182 182 LYS LYS A . n 
A 1 183 HIS 183 183 183 HIS HIS A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 LYS 189 189 189 LYS LYS A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 PHE 192 192 192 PHE PHE A . n 
A 1 193 GLY 193 193 193 GLY GLY A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 PHE 198 198 198 PHE PHE A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 ARG 201 201 201 ARG ARG A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 TYR 203 203 203 TYR TYR A . n 
A 1 204 ASN 204 204 204 ASN ASN A . n 
A 1 205 CYS 205 205 205 CYS CYS A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 SER 207 207 207 SER SER A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 PHE 214 214 214 PHE PHE A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 GLY 216 216 216 GLY GLY A . n 
A 1 217 CYS 217 217 217 CYS CYS A . n 
A 1 218 ARG 218 218 218 ARG ARG A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 GLY 222 222 222 GLY GLY A . n 
A 1 223 PRO 223 223 223 PRO PRO A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 TYR 227 227 227 TYR TYR A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 GLU 230 230 230 GLU GLU A . n 
A 1 231 GLN 231 231 231 GLN GLN A . n 
A 1 232 PHE 232 232 232 PHE PHE A . n 
A 1 233 GLY 233 233 233 GLY GLY A . n 
A 1 234 LYS 234 234 234 LYS LYS A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 VAL 242 242 242 VAL VAL A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 PRO 244 244 244 PRO PRO A . n 
A 1 245 GLU 245 245 245 GLU GLU A . n 
A 1 246 GLN 246 246 246 GLN GLN A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 GLU 253 253 253 GLU GLU A . n 
A 1 254 LYS 254 254 254 LYS LYS A . n 
A 1 255 TRP 255 255 255 TRP TRP A . n 
A 1 256 GLY 256 256 256 GLY GLY A . n 
A 1 257 SER 257 257 257 SER SER A . n 
A 1 258 TRP 258 258 258 TRP TRP A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 GLY 260 260 260 GLY GLY A . n 
A 1 261 GLY 261 261 261 GLY GLY A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 LYS 263 263 263 LYS LYS A . n 
A 1 264 ASP 264 264 264 ASP ASP A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 SER 266 266 266 SER SER A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 TYR 269 269 269 TYR TYR A . n 
A 1 270 CYS 270 270 270 CYS CYS A . n 
A 1 271 ALA 271 271 271 ALA ALA A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 GLU 275 275 275 GLU GLU A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 LYS 279 279 279 LYS LYS A . n 
A 1 280 GLN 280 280 280 GLN GLN A . n 
A 1 281 ASP 281 281 281 ASP ASP A . n 
A 1 282 GLN 282 282 282 GLN GLN A . n 
A 1 283 PHE 283 283 283 PHE PHE A . n 
A 1 284 HIS 284 284 284 HIS HIS A . n 
A 1 285 GLU 285 285 285 GLU GLU A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 GLY 289 289 289 GLY GLY A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 GLU 291 291 291 GLU GLU A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 THR 293 293 293 THR THR A . n 
A 1 294 GLY 294 294 294 GLY GLY A . n 
A 1 295 PHE 295 295 295 PHE PHE A . n 
A 1 296 PRO 296 296 296 PRO PRO A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 ILE 300 300 300 ILE ILE A . n 
A 1 301 LEU 301 301 301 LEU LEU A . n 
A 1 302 LYS 302 302 302 LYS LYS A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 PRO 304 304 304 PRO PRO A . n 
A 1 305 VAL 305 305 305 VAL VAL A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 PHE 307 307 307 PHE PHE A . n 
A 1 308 GLU 308 308 308 GLU GLU A . n 
A 1 309 THR 309 309 309 THR THR A . n 
A 1 310 ILE 310 310 310 ILE ILE A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 ASP 312 312 312 ASP ASP A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 LEU 314 314 314 LEU LEU A . n 
A 1 315 PRO 315 315 315 PRO PRO A . n 
A 1 316 GLU 316 316 316 GLU GLU A . n 
A 1 317 GLY 317 317 317 GLY GLY A . n 
A 1 318 PHE 318 318 318 PHE PHE A . n 
A 1 319 LYS 319 319 319 LYS LYS A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 ARG 321 321 321 ARG ARG A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
A 1 323 LYS 323 323 323 LYS LYS A . n 
A 1 324 GLU 324 324 324 GLU GLU A . n 
A 1 325 LYS 325 325 325 LYS LYS A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 ILE 327 327 327 ILE ILE A . n 
A 1 328 VAL 328 328 328 VAL VAL A . n 
A 1 329 HIS 329 329 329 HIS HIS A . n 
A 1 330 SER 330 330 330 SER SER A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 TRP 332 332 332 TRP TRP A . n 
A 1 333 ILE 333 333 333 ILE ILE A . n 
A 1 334 GLN 334 334 334 GLN GLN A . n 
A 1 335 GLN 335 335 335 GLN GLN A . n 
A 1 336 GLN 336 336 336 GLN GLN A . n 
A 1 337 LEU 337 337 337 LEU LEU A . n 
A 1 338 ILE 338 338 338 ILE ILE A . n 
A 1 339 LEU 339 339 339 LEU LEU A . n 
A 1 340 GLU 340 340 340 GLU GLU A . n 
A 1 341 HIS 341 341 341 HIS HIS A . n 
A 1 342 PRO 342 342 342 PRO PRO A . n 
A 1 343 SER 343 343 343 SER SER A . n 
A 1 344 VAL 344 344 344 VAL VAL A . n 
A 1 345 GLY 345 345 345 GLY GLY A . n 
A 1 346 CYS 346 346 346 CYS CYS A . n 
A 1 347 PHE 347 347 347 PHE PHE A . n 
A 1 348 VAL 348 348 348 VAL VAL A . n 
A 1 349 THR 349 349 349 THR THR A . n 
A 1 350 HIS 350 350 350 HIS HIS A . n 
A 1 351 CYS 351 351 351 CYS CYS A . n 
A 1 352 GLY 352 352 352 GLY GLY A . n 
A 1 353 ALA 353 353 353 ALA ALA A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 SER 355 355 355 SER SER A . n 
A 1 356 ILE 356 356 356 ILE ILE A . n 
A 1 357 THR 357 357 357 THR THR A . n 
A 1 358 GLU 358 358 358 GLU GLU A . n 
A 1 359 GLY 359 359 359 GLY GLY A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 VAL 361 361 361 VAL VAL A . n 
A 1 362 ASN 362 362 362 ASN ASN A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 CYS 364 364 364 CYS CYS A . n 
A 1 365 GLN 365 365 365 GLN GLN A . n 
A 1 366 MET 366 366 366 MET MET A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 LEU 369 369 369 LEU LEU A . n 
A 1 370 PRO 370 370 370 PRO PRO A . n 
A 1 371 GLN 371 371 371 GLN GLN A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 ASN 373 373 373 ASN ASN A . n 
A 1 374 GLY 374 374 374 GLY GLY A . n 
A 1 375 ASP 375 375 375 ASP ASP A . n 
A 1 376 TYR 376 376 376 TYR TYR A . n 
A 1 377 ILE 377 377 377 ILE ILE A . n 
A 1 378 ILE 378 378 378 ILE ILE A . n 
A 1 379 ASN 379 379 379 ASN ASN A . n 
A 1 380 ALA 380 380 380 ALA ALA A . n 
A 1 381 ARG 381 381 381 ARG ARG A . n 
A 1 382 ILE 382 382 382 ILE ILE A . n 
A 1 383 MET 383 383 383 MET MET A . n 
A 1 384 GLY 384 384 384 GLY GLY A . n 
A 1 385 ARG 385 385 385 ARG ARG A . n 
A 1 386 HIS 386 386 386 HIS HIS A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 LYS 388 388 388 LYS LYS A . n 
A 1 389 VAL 389 389 389 VAL VAL A . n 
A 1 390 GLY 390 390 390 GLY GLY A . n 
A 1 391 VAL 391 391 391 VAL VAL A . n 
A 1 392 GLU 392 392 392 GLU GLU A . n 
A 1 393 VAL 393 393 393 VAL VAL A . n 
A 1 394 LYS 394 394 394 LYS LYS A . n 
A 1 395 LYS 395 395 395 LYS LYS A . n 
A 1 396 GLY 396 396 396 GLY GLY A . n 
A 1 397 GLU 397 397 397 GLU GLU A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 ASP 399 399 399 ASP ASP A . n 
A 1 400 GLY 400 400 400 GLY GLY A . n 
A 1 401 LEU 401 401 401 LEU LEU A . n 
A 1 402 PHE 402 402 402 PHE PHE A . n 
A 1 403 THR 403 403 403 THR THR A . n 
A 1 404 LYS 404 404 404 LYS LYS A . n 
A 1 405 GLU 405 405 405 GLU GLU A . n 
A 1 406 SER 406 406 406 SER SER A . n 
A 1 407 VAL 407 407 407 VAL VAL A . n 
A 1 408 TYR 408 408 408 TYR TYR A . n 
A 1 409 GLU 409 409 409 GLU GLU A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 VAL 411 411 411 VAL VAL A . n 
A 1 412 LYS 412 412 412 LYS LYS A . n 
A 1 413 ILE 413 413 413 ILE ILE A . n 
A 1 414 VAL 414 414 414 VAL VAL A . n 
A 1 415 MET 415 415 415 MET MET A . n 
A 1 416 ASP 416 416 416 ASP ASP A . n 
A 1 417 ASP 417 417 417 ASP ASP A . n 
A 1 418 GLU 418 418 418 GLU GLU A . n 
A 1 419 ASN 419 419 419 ASN ASN A . n 
A 1 420 GLU 420 420 420 GLU GLU A . n 
A 1 421 ILE 421 421 421 ILE ILE A . n 
A 1 422 GLY 422 422 422 GLY GLY A . n 
A 1 423 ARG 423 423 423 ARG ARG A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 VAL 425 425 425 VAL VAL A . n 
A 1 426 ARG 426 426 426 ARG ARG A . n 
A 1 427 SER 427 427 427 SER SER A . n 
A 1 428 ASN 428 428 428 ASN ASN A . n 
A 1 429 HIS 429 429 429 HIS HIS A . n 
A 1 430 THR 430 430 430 THR THR A . n 
A 1 431 LYS 431 431 431 LYS LYS A . n 
A 1 432 VAL 432 432 432 VAL VAL A . n 
A 1 433 ARG 433 433 433 ARG ARG A . n 
A 1 434 ASN 434 434 434 ASN ASN A . n 
A 1 435 LEU 435 435 435 LEU LEU A . n 
A 1 436 LEU 436 436 436 LEU LEU A . n 
A 1 437 LEU 437 437 437 LEU LEU A . n 
A 1 438 ARG 438 438 438 ARG ARG A . n 
A 1 439 HIS 439 439 439 HIS HIS A . n 
A 1 440 ASP 440 440 440 ASP ASP A . n 
A 1 441 LEU 441 441 441 LEU LEU A . n 
A 1 442 GLU 442 442 442 GLU GLU A . n 
A 1 443 SER 443 443 443 SER SER A . n 
A 1 444 SER 444 444 444 SER SER A . n 
A 1 445 CYS 445 445 445 CYS CYS A . n 
A 1 446 LEU 446 446 446 LEU LEU A . n 
A 1 447 ASP 447 447 447 ASP ASP A . n 
A 1 448 THR 448 448 448 THR THR A . n 
A 1 449 PHE 449 449 449 PHE PHE A . n 
A 1 450 CYS 450 450 450 CYS CYS A . n 
A 1 451 GLU 451 451 451 GLU GLU A . n 
A 1 452 LYS 452 452 452 LYS LYS A . n 
A 1 453 LEU 453 453 453 LEU LEU A . n 
A 1 454 GLN 454 454 454 GLN GLN A . n 
A 1 455 GLU 455 455 455 GLU GLU A . n 
A 1 456 LEU 456 456 456 LEU LEU A . n 
A 1 457 VAL 457 457 457 VAL VAL A . n 
A 1 458 SER 458 458 458 SER SER A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 U5P ? ? U5P ? ? 'SUBJECT OF INVESTIGATION' ? 
2 RUT ? ? RUT ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 U5P 1   501 504 U5P UMP A . 
C 3 RUT 1   502 505 RUT RUT A . 
D 4 HOH 1   601 26  HOH HOH A . 
D 4 HOH 2   602 33  HOH HOH A . 
D 4 HOH 3   603 83  HOH HOH A . 
D 4 HOH 4   604 239 HOH HOH A . 
D 4 HOH 5   605 228 HOH HOH A . 
D 4 HOH 6   606 34  HOH HOH A . 
D 4 HOH 7   607 6   HOH HOH A . 
D 4 HOH 8   608 56  HOH HOH A . 
D 4 HOH 9   609 135 HOH HOH A . 
D 4 HOH 10  610 105 HOH HOH A . 
D 4 HOH 11  611 65  HOH HOH A . 
D 4 HOH 12  612 186 HOH HOH A . 
D 4 HOH 13  613 132 HOH HOH A . 
D 4 HOH 14  614 49  HOH HOH A . 
D 4 HOH 15  615 100 HOH HOH A . 
D 4 HOH 16  616 188 HOH HOH A . 
D 4 HOH 17  617 75  HOH HOH A . 
D 4 HOH 18  618 111 HOH HOH A . 
D 4 HOH 19  619 175 HOH HOH A . 
D 4 HOH 20  620 231 HOH HOH A . 
D 4 HOH 21  621 90  HOH HOH A . 
D 4 HOH 22  622 224 HOH HOH A . 
D 4 HOH 23  623 106 HOH HOH A . 
D 4 HOH 24  624 16  HOH HOH A . 
D 4 HOH 25  625 196 HOH HOH A . 
D 4 HOH 26  626 119 HOH HOH A . 
D 4 HOH 27  627 81  HOH HOH A . 
D 4 HOH 28  628 84  HOH HOH A . 
D 4 HOH 29  629 36  HOH HOH A . 
D 4 HOH 30  630 150 HOH HOH A . 
D 4 HOH 31  631 94  HOH HOH A . 
D 4 HOH 32  632 46  HOH HOH A . 
D 4 HOH 33  633 128 HOH HOH A . 
D 4 HOH 34  634 131 HOH HOH A . 
D 4 HOH 35  635 88  HOH HOH A . 
D 4 HOH 36  636 113 HOH HOH A . 
D 4 HOH 37  637 169 HOH HOH A . 
D 4 HOH 38  638 7   HOH HOH A . 
D 4 HOH 39  639 197 HOH HOH A . 
D 4 HOH 40  640 86  HOH HOH A . 
D 4 HOH 41  641 160 HOH HOH A . 
D 4 HOH 42  642 50  HOH HOH A . 
D 4 HOH 43  643 2   HOH HOH A . 
D 4 HOH 44  644 15  HOH HOH A . 
D 4 HOH 45  645 32  HOH HOH A . 
D 4 HOH 46  646 54  HOH HOH A . 
D 4 HOH 47  647 31  HOH HOH A . 
D 4 HOH 48  648 104 HOH HOH A . 
D 4 HOH 49  649 25  HOH HOH A . 
D 4 HOH 50  650 4   HOH HOH A . 
D 4 HOH 51  651 210 HOH HOH A . 
D 4 HOH 52  652 237 HOH HOH A . 
D 4 HOH 53  653 13  HOH HOH A . 
D 4 HOH 54  654 120 HOH HOH A . 
D 4 HOH 55  655 110 HOH HOH A . 
D 4 HOH 56  656 126 HOH HOH A . 
D 4 HOH 57  657 199 HOH HOH A . 
D 4 HOH 58  658 67  HOH HOH A . 
D 4 HOH 59  659 35  HOH HOH A . 
D 4 HOH 60  660 41  HOH HOH A . 
D 4 HOH 61  661 45  HOH HOH A . 
D 4 HOH 62  662 125 HOH HOH A . 
D 4 HOH 63  663 43  HOH HOH A . 
D 4 HOH 64  664 28  HOH HOH A . 
D 4 HOH 65  665 79  HOH HOH A . 
D 4 HOH 66  666 139 HOH HOH A . 
D 4 HOH 67  667 153 HOH HOH A . 
D 4 HOH 68  668 138 HOH HOH A . 
D 4 HOH 69  669 198 HOH HOH A . 
D 4 HOH 70  670 240 HOH HOH A . 
D 4 HOH 71  671 66  HOH HOH A . 
D 4 HOH 72  672 70  HOH HOH A . 
D 4 HOH 73  673 60  HOH HOH A . 
D 4 HOH 74  674 78  HOH HOH A . 
D 4 HOH 75  675 96  HOH HOH A . 
D 4 HOH 76  676 80  HOH HOH A . 
D 4 HOH 77  677 194 HOH HOH A . 
D 4 HOH 78  678 68  HOH HOH A . 
D 4 HOH 79  679 115 HOH HOH A . 
D 4 HOH 80  680 92  HOH HOH A . 
D 4 HOH 81  681 129 HOH HOH A . 
D 4 HOH 82  682 21  HOH HOH A . 
D 4 HOH 83  683 144 HOH HOH A . 
D 4 HOH 84  684 215 HOH HOH A . 
D 4 HOH 85  685 10  HOH HOH A . 
D 4 HOH 86  686 38  HOH HOH A . 
D 4 HOH 87  687 12  HOH HOH A . 
D 4 HOH 88  688 134 HOH HOH A . 
D 4 HOH 89  689 40  HOH HOH A . 
D 4 HOH 90  690 19  HOH HOH A . 
D 4 HOH 91  691 191 HOH HOH A . 
D 4 HOH 92  692 95  HOH HOH A . 
D 4 HOH 93  693 234 HOH HOH A . 
D 4 HOH 94  694 151 HOH HOH A . 
D 4 HOH 95  695 1   HOH HOH A . 
D 4 HOH 96  696 123 HOH HOH A . 
D 4 HOH 97  697 3   HOH HOH A . 
D 4 HOH 98  698 112 HOH HOH A . 
D 4 HOH 99  699 14  HOH HOH A . 
D 4 HOH 100 700 168 HOH HOH A . 
D 4 HOH 101 701 17  HOH HOH A . 
D 4 HOH 102 702 39  HOH HOH A . 
D 4 HOH 103 703 62  HOH HOH A . 
D 4 HOH 104 704 29  HOH HOH A . 
D 4 HOH 105 705 37  HOH HOH A . 
D 4 HOH 106 706 5   HOH HOH A . 
D 4 HOH 107 707 241 HOH HOH A . 
D 4 HOH 108 708 117 HOH HOH A . 
D 4 HOH 109 709 47  HOH HOH A . 
D 4 HOH 110 710 143 HOH HOH A . 
D 4 HOH 111 711 163 HOH HOH A . 
D 4 HOH 112 712 233 HOH HOH A . 
D 4 HOH 113 713 61  HOH HOH A . 
D 4 HOH 114 714 147 HOH HOH A . 
D 4 HOH 115 715 18  HOH HOH A . 
D 4 HOH 116 716 137 HOH HOH A . 
D 4 HOH 117 717 181 HOH HOH A . 
D 4 HOH 118 718 57  HOH HOH A . 
D 4 HOH 119 719 63  HOH HOH A . 
D 4 HOH 120 720 185 HOH HOH A . 
D 4 HOH 121 721 118 HOH HOH A . 
D 4 HOH 122 722 42  HOH HOH A . 
D 4 HOH 123 723 76  HOH HOH A . 
D 4 HOH 124 724 192 HOH HOH A . 
D 4 HOH 125 725 8   HOH HOH A . 
D 4 HOH 126 726 72  HOH HOH A . 
D 4 HOH 127 727 232 HOH HOH A . 
D 4 HOH 128 728 189 HOH HOH A . 
D 4 HOH 129 729 204 HOH HOH A . 
D 4 HOH 130 730 220 HOH HOH A . 
D 4 HOH 131 731 184 HOH HOH A . 
D 4 HOH 132 732 53  HOH HOH A . 
D 4 HOH 133 733 170 HOH HOH A . 
D 4 HOH 134 734 167 HOH HOH A . 
D 4 HOH 135 735 207 HOH HOH A . 
D 4 HOH 136 736 9   HOH HOH A . 
D 4 HOH 137 737 158 HOH HOH A . 
D 4 HOH 138 738 101 HOH HOH A . 
D 4 HOH 139 739 22  HOH HOH A . 
D 4 HOH 140 740 107 HOH HOH A . 
D 4 HOH 141 741 64  HOH HOH A . 
D 4 HOH 142 742 20  HOH HOH A . 
D 4 HOH 143 743 203 HOH HOH A . 
D 4 HOH 144 744 74  HOH HOH A . 
D 4 HOH 145 745 122 HOH HOH A . 
D 4 HOH 146 746 30  HOH HOH A . 
D 4 HOH 147 747 200 HOH HOH A . 
D 4 HOH 148 748 219 HOH HOH A . 
D 4 HOH 149 749 73  HOH HOH A . 
D 4 HOH 150 750 24  HOH HOH A . 
D 4 HOH 151 751 161 HOH HOH A . 
D 4 HOH 152 752 130 HOH HOH A . 
D 4 HOH 153 753 58  HOH HOH A . 
D 4 HOH 154 754 236 HOH HOH A . 
D 4 HOH 155 755 190 HOH HOH A . 
D 4 HOH 156 756 27  HOH HOH A . 
D 4 HOH 157 757 230 HOH HOH A . 
D 4 HOH 158 758 141 HOH HOH A . 
D 4 HOH 159 759 48  HOH HOH A . 
D 4 HOH 160 760 59  HOH HOH A . 
D 4 HOH 161 761 82  HOH HOH A . 
D 4 HOH 162 762 99  HOH HOH A . 
D 4 HOH 163 763 69  HOH HOH A . 
D 4 HOH 164 764 225 HOH HOH A . 
D 4 HOH 165 765 114 HOH HOH A . 
D 4 HOH 166 766 87  HOH HOH A . 
D 4 HOH 167 767 213 HOH HOH A . 
D 4 HOH 168 768 202 HOH HOH A . 
D 4 HOH 169 769 98  HOH HOH A . 
D 4 HOH 170 770 11  HOH HOH A . 
D 4 HOH 171 771 89  HOH HOH A . 
D 4 HOH 172 772 140 HOH HOH A . 
D 4 HOH 173 773 149 HOH HOH A . 
D 4 HOH 174 774 124 HOH HOH A . 
D 4 HOH 175 775 116 HOH HOH A . 
D 4 HOH 176 776 51  HOH HOH A . 
D 4 HOH 177 777 180 HOH HOH A . 
D 4 HOH 178 778 55  HOH HOH A . 
D 4 HOH 179 779 166 HOH HOH A . 
D 4 HOH 180 780 177 HOH HOH A . 
D 4 HOH 181 781 146 HOH HOH A . 
D 4 HOH 182 782 23  HOH HOH A . 
D 4 HOH 183 783 97  HOH HOH A . 
D 4 HOH 184 784 178 HOH HOH A . 
D 4 HOH 185 785 187 HOH HOH A . 
D 4 HOH 186 786 218 HOH HOH A . 
D 4 HOH 187 787 155 HOH HOH A . 
D 4 HOH 188 788 136 HOH HOH A . 
D 4 HOH 189 789 44  HOH HOH A . 
D 4 HOH 190 790 156 HOH HOH A . 
D 4 HOH 191 791 52  HOH HOH A . 
D 4 HOH 192 792 145 HOH HOH A . 
D 4 HOH 193 793 71  HOH HOH A . 
D 4 HOH 194 794 109 HOH HOH A . 
D 4 HOH 195 795 195 HOH HOH A . 
D 4 HOH 196 796 93  HOH HOH A . 
D 4 HOH 197 797 133 HOH HOH A . 
D 4 HOH 198 798 223 HOH HOH A . 
D 4 HOH 199 799 211 HOH HOH A . 
D 4 HOH 200 800 214 HOH HOH A . 
D 4 HOH 201 801 242 HOH HOH A . 
D 4 HOH 202 802 206 HOH HOH A . 
D 4 HOH 203 803 212 HOH HOH A . 
D 4 HOH 204 804 193 HOH HOH A . 
D 4 HOH 205 805 121 HOH HOH A . 
D 4 HOH 206 806 226 HOH HOH A . 
D 4 HOH 207 807 108 HOH HOH A . 
D 4 HOH 208 808 208 HOH HOH A . 
D 4 HOH 209 809 209 HOH HOH A . 
D 4 HOH 210 810 182 HOH HOH A . 
D 4 HOH 211 811 127 HOH HOH A . 
D 4 HOH 212 812 205 HOH HOH A . 
D 4 HOH 213 813 103 HOH HOH A . 
D 4 HOH 214 814 159 HOH HOH A . 
D 4 HOH 215 815 183 HOH HOH A . 
D 4 HOH 216 816 235 HOH HOH A . 
D 4 HOH 217 817 172 HOH HOH A . 
D 4 HOH 218 818 179 HOH HOH A . 
D 4 HOH 219 819 171 HOH HOH A . 
D 4 HOH 220 820 173 HOH HOH A . 
D 4 HOH 221 821 229 HOH HOH A . 
D 4 HOH 222 822 102 HOH HOH A . 
D 4 HOH 223 823 85  HOH HOH A . 
D 4 HOH 224 824 217 HOH HOH A . 
D 4 HOH 225 825 165 HOH HOH A . 
D 4 HOH 226 826 77  HOH HOH A . 
D 4 HOH 227 827 222 HOH HOH A . 
D 4 HOH 228 828 201 HOH HOH A . 
D 4 HOH 229 829 221 HOH HOH A . 
D 4 HOH 230 830 152 HOH HOH A . 
D 4 HOH 231 831 142 HOH HOH A . 
D 4 HOH 232 832 157 HOH HOH A . 
D 4 HOH 233 833 154 HOH HOH A . 
D 4 HOH 234 834 238 HOH HOH A . 
D 4 HOH 235 835 174 HOH HOH A . 
D 4 HOH 236 836 227 HOH HOH A . 
D 4 HOH 237 837 148 HOH HOH A . 
D 4 HOH 238 838 176 HOH HOH A . 
D 4 HOH 239 839 91  HOH HOH A . 
D 4 HOH 240 840 216 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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' ? 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    ? 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                    ? 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KSW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     80.342 
_cell.length_a_esd                 ? 
_cell.length_b                     120.505 
_cell.length_b_esd                 ? 
_cell.length_c                     47.794 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9KSW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 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                   9KSW 
_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             2.24 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.18 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20% w/v polyethylene glycol 3350, 0.2 M Calcium acetate hydrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_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 S 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         2023-09-15 
_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                    Si111 
_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   0.97895 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97895 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KSW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.05 
_reflns.d_resolution_low                               66.85 
_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                                     29883 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.2 
_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                                   0.985 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.05 
_reflns_shell.d_res_low                                     2.16 
_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                             4303 
_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                                  0.525 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9KSW 
_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                            2.05 
_refine.ls_d_res_low                             47.79 
_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                     29760 
_refine.ls_number_reflns_R_free                  1999 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.76 
_refine.ls_percent_reflns_R_free                 6.72 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1838 
_refine.ls_R_factor_R_free                       0.2262 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1807 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.33 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.92 
_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                            0.28 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.05 
_refine_hist.d_res_low                        47.79 
_refine_hist.number_atoms_solvent             240 
_refine_hist.number_atoms_total               3904 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3600 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         64 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009 ? 3759 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.968 ? 5102 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 7.350 ? 528  ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.057 ? 572  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 642  ? f_plane_restr      ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 2.05 2.10  . . 138 1925 98.00  . . . . 0.2740 . . . . . . . . . . . . . . . 0.3579 
'X-RAY DIFFRACTION' 2.10 2.16  . . 140 1952 99.00  . . . . 0.2299 . . . . . . . . . . . . . . . 0.2842 
'X-RAY DIFFRACTION' 2.16 2.22  . . 140 1944 100.00 . . . . 0.2160 . . . . . . . . . . . . . . . 0.2730 
'X-RAY DIFFRACTION' 2.22 2.30  . . 141 1961 100.00 . . . . 0.2156 . . . . . . . . . . . . . . . 0.2665 
'X-RAY DIFFRACTION' 2.30 2.38  . . 140 1937 100.00 . . . . 0.2062 . . . . . . . . . . . . . . . 0.2755 
'X-RAY DIFFRACTION' 2.38 2.47  . . 140 1951 100.00 . . . . 0.2069 . . . . . . . . . . . . . . . 0.2734 
'X-RAY DIFFRACTION' 2.47 2.59  . . 144 1988 100.00 . . . . 0.2059 . . . . . . . . . . . . . . . 0.2721 
'X-RAY DIFFRACTION' 2.59 2.72  . . 140 1949 100.00 . . . . 0.2013 . . . . . . . . . . . . . . . 0.2945 
'X-RAY DIFFRACTION' 2.72 2.89  . . 144 1993 100.00 . . . . 0.1923 . . . . . . . . . . . . . . . 0.2587 
'X-RAY DIFFRACTION' 2.89 3.11  . . 142 1986 100.00 . . . . 0.1900 . . . . . . . . . . . . . . . 0.2405 
'X-RAY DIFFRACTION' 3.12 3.43  . . 144 1995 100.00 . . . . 0.1873 . . . . . . . . . . . . . . . 0.2367 
'X-RAY DIFFRACTION' 3.43 3.92  . . 144 2007 100.00 . . . . 0.1526 . . . . . . . . . . . . . . . 0.1897 
'X-RAY DIFFRACTION' 3.92 4.94  . . 148 2033 100.00 . . . . 0.1377 . . . . . . . . . . . . . . . 0.1511 
'X-RAY DIFFRACTION' 4.95 47.79 . . 154 2140 100.00 . . . . 0.1617 . . . . . . . . . . . . . . . 0.1925 
# 
_struct.entry_id                     9KSW 
_struct.title                        'Complex structure of CaApiGT/UMP/Rutin' 
_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        9KSW 
_struct_keywords.text            'glycosyltransferase, apiosyltransferase, plant protein' 
_struct_keywords.pdbx_keywords   'PLANT PROTEIN' 
# 
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                    A0A1S2XDD2_CICAR 
_struct_ref.pdbx_db_accession          A0A1S2XDD2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MDSPSSLHIAMFPWFAMGHLIPYLHLSNKLAKRGHKISFFTPKKTQTKLEQFNLYPNLITFYPLNVPHVDGLPFGAETTS
DVAISLGPILMTAMDQTQNQIELLLTQLKPQIIFFDFVFWLPKITQRLGIKSFLYFIINPATISYTTSPPRMFEAENLTE
VDLMKPPKGYPTSFNLQSHEAKHLASTRKIEFGSGIPFSVRSYNCLSLTDAIGFKGCREIEGPYVDYLQEQFGKPVLLSG
PVLPEQSKTALDEKWGSWLGGFKDGSLVYCALGSELKLKQDQFHELLLGLELTGFPFLAILKPPVGFETIEDALPEGFKE
RVKEKGIVHSGWIQQQLILEHPSVGCFVTHCGAGSITEGLVNNCQMVLLPQLNGDYIINARIMGRHLKVGVEVKKGEEDG
LFTKESVYEAVKIVMDDENEIGREVRSNHTKVRNLLLRHDLESSCLDTFCEKLQELVS
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9KSW 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 458 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A1S2XDD2 
_struct_ref_seq.db_align_beg                  1 
_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       1 
_struct_ref_seq.pdbx_auth_seq_align_end       458 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
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 ALA A 16  ? ARG A 33  ? ALA A 16  ARG A 33  1 ? 18 
HELX_P HELX_P2  AA2 THR A 45  ? GLU A 50  ? THR A 45  GLU A 50  1 ? 6  
HELX_P HELX_P3  AA3 GLN A 51  ? ASN A 53  ? GLN A 51  ASN A 53  5 ? 3  
HELX_P HELX_P4  AA4 ALA A 83  ? SER A 85  ? ALA A 83  SER A 85  5 ? 3  
HELX_P HELX_P5  AA5 LEU A 86  ? GLN A 96  ? LEU A 86  GLN A 96  1 ? 11 
HELX_P HELX_P6  AA6 THR A 97  ? LYS A 109 ? THR A 97  LYS A 109 1 ? 13 
HELX_P HELX_P7  AA7 TRP A 120 ? LEU A 128 ? TRP A 120 LEU A 128 1 ? 9  
HELX_P HELX_P8  AA8 ASN A 139 ? SER A 148 ? ASN A 139 SER A 148 1 ? 10 
HELX_P HELX_P9  AA9 SER A 148 ? ALA A 155 ? SER A 148 ALA A 155 1 ? 8  
HELX_P HELX_P10 AB1 GLU A 156 ? LEU A 158 ? GLU A 156 LEU A 158 5 ? 3  
HELX_P HELX_P11 AB2 VAL A 161 ? LYS A 165 ? VAL A 161 LYS A 165 5 ? 5  
HELX_P HELX_P12 AB3 GLN A 177 ? ARG A 188 ? GLN A 177 ARG A 188 1 ? 12 
HELX_P HELX_P13 AB4 SER A 199 ? THR A 209 ? SER A 199 THR A 209 1 ? 11 
HELX_P HELX_P14 AB5 CYS A 217 ? GLY A 233 ? CYS A 217 GLY A 233 1 ? 17 
HELX_P HELX_P15 AB6 ASP A 252 ? GLY A 261 ? ASP A 252 GLY A 261 1 ? 10 
HELX_P HELX_P16 AB7 LYS A 279 ? GLY A 294 ? LYS A 279 GLY A 294 1 ? 16 
HELX_P HELX_P17 AB8 THR A 309 ? LEU A 314 ? THR A 309 LEU A 314 1 ? 6  
HELX_P HELX_P18 AB9 GLY A 317 ? LYS A 323 ? GLY A 317 LYS A 323 1 ? 7  
HELX_P HELX_P19 AC1 GLN A 334 ? HIS A 341 ? GLN A 334 HIS A 341 1 ? 8  
HELX_P HELX_P20 AC2 GLY A 352 ? VAL A 361 ? GLY A 352 VAL A 361 1 ? 10 
HELX_P HELX_P21 AC3 ASN A 373 ? HIS A 386 ? ASN A 373 HIS A 386 1 ? 14 
HELX_P HELX_P22 AC4 THR A 403 ? ASP A 416 ? THR A 403 ASP A 416 1 ? 14 
HELX_P HELX_P23 AC5 ASN A 419 ? LEU A 437 ? ASN A 419 LEU A 437 1 ? 19 
HELX_P HELX_P24 AC6 ASP A 440 ? VAL A 457 ? ASP A 440 VAL A 457 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 6 ? 
# 
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 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? parallel 
AA2 5 6 ? 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 ILE A 59  ? LEU A 64  ? ILE A 59  LEU A 64  
AA1 2 LYS A 36  ? PRO A 42  ? LYS A 36  PRO A 42  
AA1 3 HIS A 8   ? PHE A 12  ? HIS A 8   PHE A 12  
AA1 4 ILE A 112 ? PHE A 115 ? ILE A 112 PHE A 115 
AA1 5 LYS A 131 ? PHE A 136 ? LYS A 131 PHE A 136 
AA1 6 ALA A 211 ? PHE A 214 ? ALA A 211 PHE A 214 
AA1 7 VAL A 236 ? LEU A 238 ? VAL A 236 LEU A 238 
AA2 1 GLY A 326 ? HIS A 329 ? GLY A 326 HIS A 329 
AA2 2 PHE A 297 ? ILE A 300 ? PHE A 297 ILE A 300 
AA2 3 LEU A 267 ? ALA A 271 ? LEU A 267 ALA A 271 
AA2 4 VAL A 344 ? THR A 349 ? VAL A 344 THR A 349 
AA2 5 GLN A 365 ? LEU A 368 ? GLN A 365 LEU A 368 
AA2 6 GLY A 390 ? GLU A 392 ? GLY A 390 GLU A 392 
# 
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 O THR A 60  ? O THR A 60  N PHE A 39  ? N PHE A 39  
AA1 2 3 O LYS A 36  ? O LYS A 36  N ILE A 9   ? N ILE A 9   
AA1 3 4 N ALA A 10  ? N ALA A 10  O PHE A 114 ? O PHE A 114 
AA1 4 5 N ILE A 113 ? N ILE A 113 O PHE A 133 ? O PHE A 133 
AA1 5 6 N PHE A 136 ? N PHE A 136 O GLY A 213 ? O GLY A 213 
AA1 6 7 N ILE A 212 ? N ILE A 212 O LEU A 237 ? O LEU A 237 
AA2 1 2 O ILE A 327 ? O ILE A 327 N ALA A 299 ? N ALA A 299 
AA2 2 3 O ILE A 300 ? O ILE A 300 N CYS A 270 ? N CYS A 270 
AA2 3 4 N TYR A 269 ? N TYR A 269 O CYS A 346 ? O CYS A 346 
AA2 4 5 N PHE A 347 ? N PHE A 347 O VAL A 367 ? O VAL A 367 
AA2 5 6 N LEU A 368 ? N LEU A 368 O VAL A 391 ? O VAL A 391 
# 
_pdbx_entry_details.entry_id                   9KSW 
_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   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE2 A GLU 154 ? ? O A HOH 601 ? ? 1.93 
2 1 O   A HOH 633 ? ? O A HOH 804 ? ? 2.08 
3 1 O   A LEU 158 ? ? O A HOH 602 ? ? 2.12 
4 1 O   A HOH 680 ? ? O A HOH 829 ? ? 2.13 
5 1 O   A HOH 617 ? ? O A HOH 631 ? ? 2.16 
6 1 O   A HOH 783 ? ? O A HOH 811 ? ? 2.19 
# 
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 PHE A 117 ? ? 67.64  -33.42  
2 1 ALA A 155 ? ? 59.63  -103.85 
3 1 SER A 202 ? ? 93.30  -62.99  
4 1 LYS A 323 ? ? 57.96  -127.90 
5 1 HIS A 386 ? ? -98.12 -62.33  
# 
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 MET 1 ? A MET 1 
2 1 Y 1 A ASP 2 ? A ASP 2 
3 1 Y 1 A SER 3 ? A SER 3 
4 1 Y 1 A PRO 4 ? A PRO 4 
# 
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 
PHE N      N N N 250 
PHE CA     C N S 251 
PHE C      C N N 252 
PHE O      O N N 253 
PHE CB     C N N 254 
PHE CG     C Y N 255 
PHE CD1    C Y N 256 
PHE CD2    C Y N 257 
PHE CE1    C Y N 258 
PHE CE2    C Y N 259 
PHE CZ     C Y N 260 
PHE OXT    O N N 261 
PHE H      H N N 262 
PHE H2     H N N 263 
PHE HA     H N N 264 
PHE HB2    H N N 265 
PHE HB3    H N N 266 
PHE HD1    H N N 267 
PHE HD2    H N N 268 
PHE HE1    H N N 269 
PHE HE2    H N N 270 
PHE HZ     H N N 271 
PHE HXT    H N N 272 
PRO N      N N N 273 
PRO CA     C N S 274 
PRO C      C N N 275 
PRO O      O N N 276 
PRO CB     C N N 277 
PRO CG     C N N 278 
PRO CD     C N N 279 
PRO OXT    O N N 280 
PRO H      H N N 281 
PRO HA     H N N 282 
PRO HB2    H N N 283 
PRO HB3    H N N 284 
PRO HG2    H N N 285 
PRO HG3    H N N 286 
PRO HD2    H N N 287 
PRO HD3    H N N 288 
PRO HXT    H N N 289 
RUT O1     O Y N 290 
RUT C1     C Y N 291 
RUT C2     C Y N 292 
RUT O2     O N N 293 
RUT C3     C Y N 294 
RUT O3     O N N 295 
RUT C4     C Y N 296 
RUT O4     O N N 297 
RUT C5     C Y N 298 
RUT C6     C Y N 299 
RUT O5     O N N 300 
RUT C7     C Y N 301 
RUT C8     C Y N 302 
RUT C9     C Y N 303 
RUT C10    C Y N 304 
RUT C11    C Y N 305 
RUT C12    C Y N 306 
RUT O6     O N N 307 
RUT C13    C Y N 308 
RUT O7     O N N 309 
RUT C14    C Y N 310 
RUT C15    C Y N 311 
RUT C16    C N S 312 
RUT C17    C N R 313 
RUT O8     O N N 314 
RUT C18    C N S 315 
RUT O9     O N N 316 
RUT C19    C N S 317 
RUT O10    O N N 318 
RUT C20    C N R 319 
RUT C21    C N N 320 
RUT O11    O N N 321 
RUT C22    C N R 322 
RUT O12    O N N 323 
RUT C23    C N R 324 
RUT O13    O N N 325 
RUT C24    C N R 326 
RUT O14    O N N 327 
RUT C25    C N R 328 
RUT O15    O N N 329 
RUT C26    C N S 330 
RUT C27    C N N 331 
RUT O16    O N N 332 
RUT HO4    H N N 333 
RUT H5     H N N 334 
RUT HO5    H N N 335 
RUT H7     H N N 336 
RUT H11    H N N 337 
RUT HO6    H N N 338 
RUT HO7    H N N 339 
RUT H2     H N N 340 
RUT H1     H N N 341 
RUT H16    H N N 342 
RUT H17    H N N 343 
RUT HO8    H N N 344 
RUT H18    H N N 345 
RUT HO9    H N N 346 
RUT H19    H N N 347 
RUT H10    H N N 348 
RUT H20    H N N 349 
RUT H211   H N N 350 
RUT H212   H N N 351 
RUT H22    H N N 352 
RUT H23    H N N 353 
RUT H13    H N N 354 
RUT H24    H N N 355 
RUT H14    H N N 356 
RUT H25    H N N 357 
RUT H15    H N N 358 
RUT H26    H N N 359 
RUT H271   H N N 360 
RUT H272   H N N 361 
RUT H273   H N N 362 
SER N      N N N 363 
SER CA     C N S 364 
SER C      C N N 365 
SER O      O N N 366 
SER CB     C N N 367 
SER OG     O N N 368 
SER OXT    O N N 369 
SER H      H N N 370 
SER H2     H N N 371 
SER HA     H N N 372 
SER HB2    H N N 373 
SER HB3    H N N 374 
SER HG     H N N 375 
SER HXT    H N N 376 
THR N      N N N 377 
THR CA     C N S 378 
THR C      C N N 379 
THR O      O N N 380 
THR CB     C N R 381 
THR OG1    O N N 382 
THR CG2    C N N 383 
THR OXT    O N N 384 
THR H      H N N 385 
THR H2     H N N 386 
THR HA     H N N 387 
THR HB     H N N 388 
THR HG1    H N N 389 
THR HG21   H N N 390 
THR HG22   H N N 391 
THR HG23   H N N 392 
THR HXT    H N N 393 
TRP N      N N N 394 
TRP CA     C N S 395 
TRP C      C N N 396 
TRP O      O N N 397 
TRP CB     C N N 398 
TRP CG     C Y N 399 
TRP CD1    C Y N 400 
TRP CD2    C Y N 401 
TRP NE1    N Y N 402 
TRP CE2    C Y N 403 
TRP CE3    C Y N 404 
TRP CZ2    C Y N 405 
TRP CZ3    C Y N 406 
TRP CH2    C Y N 407 
TRP OXT    O N N 408 
TRP H      H N N 409 
TRP H2     H N N 410 
TRP HA     H N N 411 
TRP HB2    H N N 412 
TRP HB3    H N N 413 
TRP HD1    H N N 414 
TRP HE1    H N N 415 
TRP HE3    H N N 416 
TRP HZ2    H N N 417 
TRP HZ3    H N N 418 
TRP HH2    H N N 419 
TRP HXT    H N N 420 
TYR N      N N N 421 
TYR CA     C N S 422 
TYR C      C N N 423 
TYR O      O N N 424 
TYR CB     C N N 425 
TYR CG     C Y N 426 
TYR CD1    C Y N 427 
TYR CD2    C Y N 428 
TYR CE1    C Y N 429 
TYR CE2    C Y N 430 
TYR CZ     C Y N 431 
TYR OH     O N N 432 
TYR OXT    O N N 433 
TYR H      H N N 434 
TYR H2     H N N 435 
TYR HA     H N N 436 
TYR HB2    H N N 437 
TYR HB3    H N N 438 
TYR HD1    H N N 439 
TYR HD2    H N N 440 
TYR HE1    H N N 441 
TYR HE2    H N N 442 
TYR HH     H N N 443 
TYR HXT    H N N 444 
U5P N1     N N N 445 
U5P C2     C N N 446 
U5P N3     N N N 447 
U5P C4     C N N 448 
U5P C5     C N N 449 
U5P C6     C N N 450 
U5P O2     O N N 451 
U5P O4     O N N 452 
U5P "C1'"  C N R 453 
U5P "C2'"  C N R 454 
U5P "O2'"  O N N 455 
U5P "C3'"  C N S 456 
U5P "C4'"  C N R 457 
U5P "O3'"  O N N 458 
U5P "O4'"  O N N 459 
U5P "C5'"  C N N 460 
U5P "O5'"  O N N 461 
U5P P      P N N 462 
U5P O1P    O N N 463 
U5P O2P    O N N 464 
U5P O3P    O N N 465 
U5P HN3    H N N 466 
U5P H5     H N N 467 
U5P H6     H N N 468 
U5P "H1'"  H N N 469 
U5P "H2'"  H N N 470 
U5P "HO2'" H N N 471 
U5P "H3'"  H N N 472 
U5P "H4'"  H N N 473 
U5P "HO3'" H N N 474 
U5P "H5'1" H N N 475 
U5P "H5'2" H N N 476 
U5P HOP2   H N N 477 
U5P HOP3   H N N 478 
VAL N      N N N 479 
VAL CA     C N S 480 
VAL C      C N N 481 
VAL O      O N N 482 
VAL CB     C N N 483 
VAL CG1    C N N 484 
VAL CG2    C N N 485 
VAL OXT    O N N 486 
VAL H      H N N 487 
VAL H2     H N N 488 
VAL HA     H N N 489 
VAL HB     H N N 490 
VAL HG11   H N N 491 
VAL HG12   H N N 492 
VAL HG13   H N N 493 
VAL HG21   H N N 494 
VAL HG22   H N N 495 
VAL HG23   H N N 496 
VAL HXT    H N N 497 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
LEU N     CA     sing N N 173 
LEU N     H      sing N N 174 
LEU N     H2     sing N N 175 
LEU CA    C      sing N N 176 
LEU CA    CB     sing N N 177 
LEU CA    HA     sing N N 178 
LEU C     O      doub N N 179 
LEU C     OXT    sing N N 180 
LEU CB    CG     sing N N 181 
LEU CB    HB2    sing N N 182 
LEU CB    HB3    sing N N 183 
LEU CG    CD1    sing N N 184 
LEU CG    CD2    sing N N 185 
LEU CG    HG     sing N N 186 
LEU CD1   HD11   sing N N 187 
LEU CD1   HD12   sing N N 188 
LEU CD1   HD13   sing N N 189 
LEU CD2   HD21   sing N N 190 
LEU CD2   HD22   sing N N 191 
LEU CD2   HD23   sing N N 192 
LEU OXT   HXT    sing N N 193 
LYS N     CA     sing N N 194 
LYS N     H      sing N N 195 
LYS N     H2     sing N N 196 
LYS CA    C      sing N N 197 
LYS CA    CB     sing N N 198 
LYS CA    HA     sing N N 199 
LYS C     O      doub N N 200 
LYS C     OXT    sing N N 201 
LYS CB    CG     sing N N 202 
LYS CB    HB2    sing N N 203 
LYS CB    HB3    sing N N 204 
LYS CG    CD     sing N N 205 
LYS CG    HG2    sing N N 206 
LYS CG    HG3    sing N N 207 
LYS CD    CE     sing N N 208 
LYS CD    HD2    sing N N 209 
LYS CD    HD3    sing N N 210 
LYS CE    NZ     sing N N 211 
LYS CE    HE2    sing N N 212 
LYS CE    HE3    sing N N 213 
LYS NZ    HZ1    sing N N 214 
LYS NZ    HZ2    sing N N 215 
LYS NZ    HZ3    sing N N 216 
LYS OXT   HXT    sing N N 217 
MET N     CA     sing N N 218 
MET N     H      sing N N 219 
MET N     H2     sing N N 220 
MET CA    C      sing N N 221 
MET CA    CB     sing N N 222 
MET CA    HA     sing N N 223 
MET C     O      doub N N 224 
MET C     OXT    sing N N 225 
MET CB    CG     sing N N 226 
MET CB    HB2    sing N N 227 
MET CB    HB3    sing N N 228 
MET CG    SD     sing N N 229 
MET CG    HG2    sing N N 230 
MET CG    HG3    sing N N 231 
MET SD    CE     sing N N 232 
MET CE    HE1    sing N N 233 
MET CE    HE2    sing N N 234 
MET CE    HE3    sing N N 235 
MET OXT   HXT    sing N N 236 
PHE N     CA     sing N N 237 
PHE N     H      sing N N 238 
PHE N     H2     sing N N 239 
PHE CA    C      sing N N 240 
PHE CA    CB     sing N N 241 
PHE CA    HA     sing N N 242 
PHE C     O      doub N N 243 
PHE C     OXT    sing N N 244 
PHE CB    CG     sing N N 245 
PHE CB    HB2    sing N N 246 
PHE CB    HB3    sing N N 247 
PHE CG    CD1    doub Y N 248 
PHE CG    CD2    sing Y N 249 
PHE CD1   CE1    sing Y N 250 
PHE CD1   HD1    sing N N 251 
PHE CD2   CE2    doub Y N 252 
PHE CD2   HD2    sing N N 253 
PHE CE1   CZ     doub Y N 254 
PHE CE1   HE1    sing N N 255 
PHE CE2   CZ     sing Y N 256 
PHE CE2   HE2    sing N N 257 
PHE CZ    HZ     sing N N 258 
PHE OXT   HXT    sing N N 259 
PRO N     CA     sing N N 260 
PRO N     CD     sing N N 261 
PRO N     H      sing N N 262 
PRO CA    C      sing N N 263 
PRO CA    CB     sing N N 264 
PRO CA    HA     sing N N 265 
PRO C     O      doub N N 266 
PRO C     OXT    sing N N 267 
PRO CB    CG     sing N N 268 
PRO CB    HB2    sing N N 269 
PRO CB    HB3    sing N N 270 
PRO CG    CD     sing N N 271 
PRO CG    HG2    sing N N 272 
PRO CG    HG3    sing N N 273 
PRO CD    HD2    sing N N 274 
PRO CD    HD3    sing N N 275 
PRO OXT   HXT    sing N N 276 
RUT O1    C1     sing Y N 277 
RUT O1    C8     sing Y N 278 
RUT C1    C2     doub Y N 279 
RUT C1    C10    sing Y N 280 
RUT C2    O2     sing N N 281 
RUT C2    C3     sing Y N 282 
RUT O2    C16    sing N N 283 
RUT C3    O3     doub N N 284 
RUT C3    C9     sing Y N 285 
RUT C4    O4     sing N N 286 
RUT C4    C5     doub Y N 287 
RUT C4    C9     sing Y N 288 
RUT O4    HO4    sing N N 289 
RUT C5    C6     sing Y N 290 
RUT C5    H5     sing N N 291 
RUT C6    O5     sing N N 292 
RUT C6    C7     doub Y N 293 
RUT O5    HO5    sing N N 294 
RUT C7    C8     sing Y N 295 
RUT C7    H7     sing N N 296 
RUT C8    C9     doub Y N 297 
RUT C10   C11    doub Y N 298 
RUT C10   C15    sing Y N 299 
RUT C11   C12    sing Y N 300 
RUT C11   H11    sing N N 301 
RUT C12   O6     sing N N 302 
RUT C12   C13    doub Y N 303 
RUT O6    HO6    sing N N 304 
RUT C13   O7     sing N N 305 
RUT C13   C14    sing Y N 306 
RUT O7    HO7    sing N N 307 
RUT C14   C15    doub Y N 308 
RUT C14   H2     sing N N 309 
RUT C15   H1     sing N N 310 
RUT C16   C17    sing N N 311 
RUT C16   O11    sing N N 312 
RUT C16   H16    sing N N 313 
RUT C17   O8     sing N N 314 
RUT C17   C18    sing N N 315 
RUT C17   H17    sing N N 316 
RUT O8    HO8    sing N N 317 
RUT C18   O9     sing N N 318 
RUT C18   C19    sing N N 319 
RUT C18   H18    sing N N 320 
RUT O9    HO9    sing N N 321 
RUT C19   O10    sing N N 322 
RUT C19   C20    sing N N 323 
RUT C19   H19    sing N N 324 
RUT O10   H10    sing N N 325 
RUT C20   C21    sing N N 326 
RUT C20   O11    sing N N 327 
RUT C20   H20    sing N N 328 
RUT C21   O12    sing N N 329 
RUT C21   H211   sing N N 330 
RUT C21   H212   sing N N 331 
RUT C22   O12    sing N N 332 
RUT C22   C23    sing N N 333 
RUT C22   O16    sing N N 334 
RUT C22   H22    sing N N 335 
RUT C23   O13    sing N N 336 
RUT C23   C24    sing N N 337 
RUT C23   H23    sing N N 338 
RUT O13   H13    sing N N 339 
RUT C24   O14    sing N N 340 
RUT C24   C25    sing N N 341 
RUT C24   H24    sing N N 342 
RUT O14   H14    sing N N 343 
RUT C25   O15    sing N N 344 
RUT C25   C26    sing N N 345 
RUT C25   H25    sing N N 346 
RUT O15   H15    sing N N 347 
RUT C26   C27    sing N N 348 
RUT C26   O16    sing N N 349 
RUT C26   H26    sing N N 350 
RUT C27   H271   sing N N 351 
RUT C27   H272   sing N N 352 
RUT C27   H273   sing N N 353 
SER N     CA     sing N N 354 
SER N     H      sing N N 355 
SER N     H2     sing N N 356 
SER CA    C      sing N N 357 
SER CA    CB     sing N N 358 
SER CA    HA     sing N N 359 
SER C     O      doub N N 360 
SER C     OXT    sing N N 361 
SER CB    OG     sing N N 362 
SER CB    HB2    sing N N 363 
SER CB    HB3    sing N N 364 
SER OG    HG     sing N N 365 
SER OXT   HXT    sing N N 366 
THR N     CA     sing N N 367 
THR N     H      sing N N 368 
THR N     H2     sing N N 369 
THR CA    C      sing N N 370 
THR CA    CB     sing N N 371 
THR CA    HA     sing N N 372 
THR C     O      doub N N 373 
THR C     OXT    sing N N 374 
THR CB    OG1    sing N N 375 
THR CB    CG2    sing N N 376 
THR CB    HB     sing N N 377 
THR OG1   HG1    sing N N 378 
THR CG2   HG21   sing N N 379 
THR CG2   HG22   sing N N 380 
THR CG2   HG23   sing N N 381 
THR OXT   HXT    sing N N 382 
TRP N     CA     sing N N 383 
TRP N     H      sing N N 384 
TRP N     H2     sing N N 385 
TRP CA    C      sing N N 386 
TRP CA    CB     sing N N 387 
TRP CA    HA     sing N N 388 
TRP C     O      doub N N 389 
TRP C     OXT    sing N N 390 
TRP CB    CG     sing N N 391 
TRP CB    HB2    sing N N 392 
TRP CB    HB3    sing N N 393 
TRP CG    CD1    doub Y N 394 
TRP CG    CD2    sing Y N 395 
TRP CD1   NE1    sing Y N 396 
TRP CD1   HD1    sing N N 397 
TRP CD2   CE2    doub Y N 398 
TRP CD2   CE3    sing Y N 399 
TRP NE1   CE2    sing Y N 400 
TRP NE1   HE1    sing N N 401 
TRP CE2   CZ2    sing Y N 402 
TRP CE3   CZ3    doub Y N 403 
TRP CE3   HE3    sing N N 404 
TRP CZ2   CH2    doub Y N 405 
TRP CZ2   HZ2    sing N N 406 
TRP CZ3   CH2    sing Y N 407 
TRP CZ3   HZ3    sing N N 408 
TRP CH2   HH2    sing N N 409 
TRP OXT   HXT    sing N N 410 
TYR N     CA     sing N N 411 
TYR N     H      sing N N 412 
TYR N     H2     sing N N 413 
TYR CA    C      sing N N 414 
TYR CA    CB     sing N N 415 
TYR CA    HA     sing N N 416 
TYR C     O      doub N N 417 
TYR C     OXT    sing N N 418 
TYR CB    CG     sing N N 419 
TYR CB    HB2    sing N N 420 
TYR CB    HB3    sing N N 421 
TYR CG    CD1    doub Y N 422 
TYR CG    CD2    sing Y N 423 
TYR CD1   CE1    sing Y N 424 
TYR CD1   HD1    sing N N 425 
TYR CD2   CE2    doub Y N 426 
TYR CD2   HD2    sing N N 427 
TYR CE1   CZ     doub Y N 428 
TYR CE1   HE1    sing N N 429 
TYR CE2   CZ     sing Y N 430 
TYR CE2   HE2    sing N N 431 
TYR CZ    OH     sing N N 432 
TYR OH    HH     sing N N 433 
TYR OXT   HXT    sing N N 434 
U5P N1    C2     sing N N 435 
U5P N1    C6     sing N N 436 
U5P N1    "C1'"  sing N N 437 
U5P C2    N3     sing N N 438 
U5P C2    O2     doub N N 439 
U5P N3    C4     sing N N 440 
U5P N3    HN3    sing N N 441 
U5P C4    C5     sing N N 442 
U5P C4    O4     doub N N 443 
U5P C5    C6     doub N N 444 
U5P C5    H5     sing N N 445 
U5P C6    H6     sing N N 446 
U5P "C1'" "C2'"  sing N N 447 
U5P "C1'" "O4'"  sing N N 448 
U5P "C1'" "H1'"  sing N N 449 
U5P "C2'" "O2'"  sing N N 450 
U5P "C2'" "C3'"  sing N N 451 
U5P "C2'" "H2'"  sing N N 452 
U5P "O2'" "HO2'" sing N N 453 
U5P "C3'" "C4'"  sing N N 454 
U5P "C3'" "O3'"  sing N N 455 
U5P "C3'" "H3'"  sing N N 456 
U5P "C4'" "O4'"  sing N N 457 
U5P "C4'" "C5'"  sing N N 458 
U5P "C4'" "H4'"  sing N N 459 
U5P "O3'" "HO3'" sing N N 460 
U5P "C5'" "O5'"  sing N N 461 
U5P "C5'" "H5'1" sing N N 462 
U5P "C5'" "H5'2" sing N N 463 
U5P "O5'" P      sing N N 464 
U5P P     O1P    doub N N 465 
U5P P     O2P    sing N N 466 
U5P P     O3P    sing N N 467 
U5P O2P   HOP2   sing N N 468 
U5P O3P   HOP3   sing N N 469 
VAL N     CA     sing N N 470 
VAL N     H      sing N N 471 
VAL N     H2     sing N N 472 
VAL CA    C      sing N N 473 
VAL CA    CB     sing N N 474 
VAL CA    HA     sing N N 475 
VAL C     O      doub N N 476 
VAL C     OXT    sing N N 477 
VAL CB    CG1    sing N N 478 
VAL CB    CG2    sing N N 479 
VAL CB    HB     sing N N 480 
VAL CG1   HG11   sing N N 481 
VAL CG1   HG12   sing N N 482 
VAL CG1   HG13   sing N N 483 
VAL CG2   HG21   sing N N 484 
VAL CG2   HG22   sing N N 485 
VAL CG2   HG23   sing N N 486 
VAL OXT   HXT    sing N N 487 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             '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                    9KSW 
_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]   0.012447 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.008298 
_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]   0.020923 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
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     . SER A 1 5   ? -35.150 1.614  5.660   1.00 42.81 ?  5   SER A N     1 
ATOM   2    C CA    . SER A 1 5   ? -35.451 1.804  7.078   1.00 50.67 ?  5   SER A CA    1 
ATOM   3    C C     . SER A 1 5   ? -34.512 2.844  7.693   1.00 51.77 ?  5   SER A C     1 
ATOM   4    O O     . SER A 1 5   ? -33.362 2.988  7.265   1.00 48.18 ?  5   SER A O     1 
ATOM   5    C CB    . SER A 1 5   ? -35.343 0.483  7.836   1.00 53.10 ?  5   SER A CB    1 
ATOM   6    O OG    . SER A 1 5   ? -35.777 -0.602 7.029   1.00 63.36 ?  5   SER A OG    1 
ATOM   7    N N     . SER A 1 6   ? -34.994 3.571  8.696   1.00 43.37 ?  6   SER A N     1 
ATOM   8    C CA    . SER A 1 6   ? -34.194 4.634  9.276   1.00 39.59 ?  6   SER A CA    1 
ATOM   9    C C     . SER A 1 6   ? -33.184 4.048  10.258  1.00 41.55 ?  6   SER A C     1 
ATOM   10   O O     . SER A 1 6   ? -33.477 3.083  10.972  1.00 37.41 ?  6   SER A O     1 
ATOM   11   C CB    . SER A 1 6   ? -35.082 5.659  9.974   1.00 34.94 ?  6   SER A CB    1 
ATOM   12   O OG    . SER A 1 6   ? -35.563 5.137  11.193  1.00 46.46 ?  6   SER A OG    1 
ATOM   13   N N     . LEU A 1 7   ? -31.983 4.632  10.279  1.00 36.40 ?  7   LEU A N     1 
ATOM   14   C CA    . LEU A 1 7   ? -30.904 4.172  11.136  1.00 30.45 ?  7   LEU A CA    1 
ATOM   15   C C     . LEU A 1 7   ? -30.911 4.911  12.467  1.00 29.56 ?  7   LEU A C     1 
ATOM   16   O O     . LEU A 1 7   ? -31.473 5.999  12.603  1.00 30.07 ?  7   LEU A O     1 
ATOM   17   C CB    . LEU A 1 7   ? -29.544 4.372  10.465  1.00 34.06 ?  7   LEU A CB    1 
ATOM   18   C CG    . LEU A 1 7   ? -29.341 3.905  9.033   1.00 36.42 ?  7   LEU A CG    1 
ATOM   19   C CD1   . LEU A 1 7   ? -28.267 4.745  8.362   1.00 30.94 ?  7   LEU A CD1   1 
ATOM   20   C CD2   . LEU A 1 7   ? -28.969 2.440  9.028   1.00 36.91 ?  7   LEU A CD2   1 
ATOM   21   N N     . HIS A 1 8   ? -30.242 4.314  13.448  1.00 27.66 ?  8   HIS A N     1 
ATOM   22   C CA    . HIS A 1 8   ? -29.962 4.966  14.722  1.00 30.03 ?  8   HIS A CA    1 
ATOM   23   C C     . HIS A 1 8   ? -28.446 5.176  14.806  1.00 26.64 ?  8   HIS A C     1 
ATOM   24   O O     . HIS A 1 8   ? -27.675 4.210  14.871  1.00 26.28 ?  8   HIS A O     1 
ATOM   25   C CB    . HIS A 1 8   ? -30.489 4.131  15.886  1.00 27.82 ?  8   HIS A CB    1 
ATOM   26   C CG    . HIS A 1 8   ? -30.221 4.728  17.233  1.00 30.78 ?  8   HIS A CG    1 
ATOM   27   N ND1   . HIS A 1 8   ? -30.330 4.005  18.399  1.00 26.02 ?  8   HIS A ND1   1 
ATOM   28   C CD2   . HIS A 1 8   ? -29.849 5.978  17.600  1.00 32.53 ?  8   HIS A CD2   1 
ATOM   29   C CE1   . HIS A 1 8   ? -30.034 4.779  19.426  1.00 30.20 ?  8   HIS A CE1   1 
ATOM   30   N NE2   . HIS A 1 8   ? -29.736 5.981  18.970  1.00 31.95 ?  8   HIS A NE2   1 
ATOM   31   N N     . ILE A 1 9   ? -28.022 6.433  14.788  1.00 28.15 ?  9   ILE A N     1 
ATOM   32   C CA    . ILE A 1 9   ? -26.607 6.784  14.733  1.00 26.76 ?  9   ILE A CA    1 
ATOM   33   C C     . ILE A 1 9   ? -26.224 7.527  16.005  1.00 22.05 ?  9   ILE A C     1 
ATOM   34   O O     . ILE A 1 9   ? -26.908 8.468  16.411  1.00 22.63 ?  9   ILE A O     1 
ATOM   35   C CB    . ILE A 1 9   ? -26.283 7.639  13.495  1.00 24.03 ?  9   ILE A CB    1 
ATOM   36   C CG1   . ILE A 1 9   ? -26.755 6.936  12.229  1.00 22.14 ?  9   ILE A CG1   1 
ATOM   37   C CG2   . ILE A 1 9   ? -24.777 7.913  13.434  1.00 23.91 ?  9   ILE A CG2   1 
ATOM   38   C CD1   . ILE A 1 9   ? -26.892 7.848  11.011  1.00 23.85 ?  9   ILE A CD1   1 
ATOM   39   N N     . ALA A 1 10  ? -25.130 7.117  16.622  1.00 21.94 ?  10  ALA A N     1 
ATOM   40   C CA    . ALA A 1 10  ? -24.541 7.871  17.716  1.00 21.68 ?  10  ALA A CA    1 
ATOM   41   C C     . ALA A 1 10  ? -23.383 8.713  17.193  1.00 18.95 ?  10  ALA A C     1 
ATOM   42   O O     . ALA A 1 10  ? -22.648 8.288  16.294  1.00 21.64 ?  10  ALA A O     1 
ATOM   43   C CB    . ALA A 1 10  ? -24.052 6.946  18.834  1.00 21.95 ?  10  ALA A CB    1 
ATOM   44   N N     . MET A 1 11  ? -23.224 9.906  17.765  1.00 20.94 ?  11  MET A N     1 
ATOM   45   C CA    . MET A 1 11  ? -22.200 10.865 17.360  1.00 20.71 ?  11  MET A CA    1 
ATOM   46   C C     . MET A 1 11  ? -21.284 11.140 18.541  1.00 22.11 ?  11  MET A C     1 
ATOM   47   O O     . MET A 1 11  ? -21.756 11.533 19.613  1.00 23.99 ?  11  MET A O     1 
ATOM   48   C CB    . MET A 1 11  ? -22.822 12.182 16.887  1.00 20.25 ?  11  MET A CB    1 
ATOM   49   C CG    . MET A 1 11  ? -23.809 12.039 15.751  1.00 26.22 ?  11  MET A CG    1 
ATOM   50   S SD    . MET A 1 11  ? -22.931 11.852 14.186  1.00 29.11 ?  11  MET A SD    1 
ATOM   51   C CE    . MET A 1 11  ? -24.182 12.259 12.972  1.00 27.04 ?  11  MET A CE    1 
ATOM   52   N N     . PHE A 1 12  ? -19.979 10.962 18.335  1.00 20.76 ?  12  PHE A N     1 
ATOM   53   C CA    . PHE A 1 12  ? -18.966 11.130 19.375  1.00 20.39 ?  12  PHE A CA    1 
ATOM   54   C C     . PHE A 1 12  ? -17.832 12.001 18.831  1.00 19.08 ?  12  PHE A C     1 
ATOM   55   O O     . PHE A 1 12  ? -16.706 11.520 18.632  1.00 17.89 ?  12  PHE A O     1 
ATOM   56   C CB    . PHE A 1 12  ? -18.447 9.767  19.845  1.00 20.09 ?  12  PHE A CB    1 
ATOM   57   C CG    . PHE A 1 12  ? -17.582 9.830  21.081  1.00 22.32 ?  12  PHE A CG    1 
ATOM   58   C CD1   . PHE A 1 12  ? -17.636 10.923 21.930  1.00 21.76 ?  12  PHE A CD1   1 
ATOM   59   C CD2   . PHE A 1 12  ? -16.728 8.787  21.396  1.00 22.50 ?  12  PHE A CD2   1 
ATOM   60   C CE1   . PHE A 1 12  ? -16.844 10.983 23.063  1.00 26.69 ?  12  PHE A CE1   1 
ATOM   61   C CE2   . PHE A 1 12  ? -15.934 8.834  22.530  1.00 25.94 ?  12  PHE A CE2   1 
ATOM   62   C CZ    . PHE A 1 12  ? -15.989 9.938  23.366  1.00 29.61 ?  12  PHE A CZ    1 
ATOM   63   N N     . PRO A 1 13  ? -18.088 13.295 18.615  1.00 18.23 ?  13  PRO A N     1 
ATOM   64   C CA    . PRO A 1 13  ? -17.042 14.190 18.095  1.00 16.09 ?  13  PRO A CA    1 
ATOM   65   C C     . PRO A 1 13  ? -16.003 14.620 19.130  1.00 18.34 ?  13  PRO A C     1 
ATOM   66   O O     . PRO A 1 13  ? -16.225 14.604 20.341  1.00 17.68 ?  13  PRO A O     1 
ATOM   67   C CB    . PRO A 1 13  ? -17.832 15.408 17.605  1.00 17.53 ?  13  PRO A CB    1 
ATOM   68   C CG    . PRO A 1 13  ? -19.066 15.435 18.438  1.00 18.61 ?  13  PRO A CG    1 
ATOM   69   C CD    . PRO A 1 13  ? -19.393 13.973 18.724  1.00 17.50 ?  13  PRO A CD    1 
ATOM   70   N N     . TRP A 1 14  ? -14.849 15.036 18.612  1.00 19.02 ?  14  TRP A N     1 
ATOM   71   C CA    . TRP A 1 14  ? -13.797 15.627 19.436  1.00 21.08 ?  14  TRP A CA    1 
ATOM   72   C C     . TRP A 1 14  ? -14.324 16.859 20.166  1.00 18.70 ?  14  TRP A C     1 
ATOM   73   O O     . TRP A 1 14  ? -15.216 17.565 19.678  1.00 17.10 ?  14  TRP A O     1 
ATOM   74   C CB    . TRP A 1 14  ? -12.602 15.974 18.531  1.00 18.01 ?  14  TRP A CB    1 
ATOM   75   C CG    . TRP A 1 14  ? -11.533 16.912 18.997  1.00 17.75 ?  14  TRP A CG    1 
ATOM   76   C CD1   . TRP A 1 14  ? -11.067 18.008 18.307  1.00 19.79 ?  14  TRP A CD1   1 
ATOM   77   C CD2   . TRP A 1 14  ? -10.701 16.809 20.183  1.00 19.86 ?  14  TRP A CD2   1 
ATOM   78   N NE1   . TRP A 1 14  ? -10.018 18.601 18.996  1.00 18.60 ?  14  TRP A NE1   1 
ATOM   79   C CE2   . TRP A 1 14  ? -9.782  17.900 20.149  1.00 19.26 ?  14  TRP A CE2   1 
ATOM   80   C CE3   . TRP A 1 14  ? -10.659 15.926 21.276  1.00 19.27 ?  14  TRP A CE3   1 
ATOM   81   C CZ2   . TRP A 1 14  ? -8.829  18.129 21.174  1.00 21.65 ?  14  TRP A CZ2   1 
ATOM   82   C CZ3   . TRP A 1 14  ? -9.707  16.154 22.297  1.00 21.81 ?  14  TRP A CZ3   1 
ATOM   83   C CH2   . TRP A 1 14  ? -8.811  17.247 22.234  1.00 20.57 ?  14  TRP A CH2   1 
ATOM   84   N N     . PHE A 1 15  ? -13.761 17.113 21.351  1.00 17.44 ?  15  PHE A N     1 
ATOM   85   C CA    . PHE A 1 15  ? -14.222 18.180 22.250  1.00 18.84 ?  15  PHE A CA    1 
ATOM   86   C C     . PHE A 1 15  ? -13.748 19.549 21.750  1.00 21.76 ?  15  PHE A C     1 
ATOM   87   O O     . PHE A 1 15  ? -12.876 20.196 22.338  1.00 21.10 ?  15  PHE A O     1 
ATOM   88   C CB    . PHE A 1 15  ? -13.722 17.941 23.672  1.00 24.05 ?  15  PHE A CB    1 
ATOM   89   C CG    . PHE A 1 15  ? -14.203 16.649 24.304  1.00 23.17 ?  15  PHE A CG    1 
ATOM   90   C CD1   . PHE A 1 15  ? -15.358 16.015 23.860  1.00 20.96 ?  15  PHE A CD1   1 
ATOM   91   C CD2   . PHE A 1 15  ? -13.489 16.077 25.357  1.00 25.80 ?  15  PHE A CD2   1 
ATOM   92   C CE1   . PHE A 1 15  ? -15.787 14.822 24.451  1.00 25.36 ?  15  PHE A CE1   1 
ATOM   93   C CE2   . PHE A 1 15  ? -13.914 14.896 25.967  1.00 28.21 ?  15  PHE A CE2   1 
ATOM   94   C CZ    . PHE A 1 15  ? -15.054 14.264 25.516  1.00 25.75 ?  15  PHE A CZ    1 
ATOM   95   N N     . ALA A 1 16  ? -14.343 19.992 20.643  1.00 21.38 ?  16  ALA A N     1 
ATOM   96   C CA    . ALA A 1 16  ? -13.967 21.269 20.040  1.00 22.32 ?  16  ALA A CA    1 
ATOM   97   C C     . ALA A 1 16  ? -15.152 21.814 19.265  1.00 18.54 ?  16  ALA A C     1 
ATOM   98   O O     . ALA A 1 16  ? -15.901 21.047 18.650  1.00 19.33 ?  16  ALA A O     1 
ATOM   99   C CB    . ALA A 1 16  ? -12.753 21.138 19.102  1.00 17.30 ?  16  ALA A CB    1 
ATOM   100  N N     . MET A 1 17  ? -15.317 23.136 19.304  1.00 18.17 ?  17  MET A N     1 
ATOM   101  C CA    . MET A 1 17  ? -16.401 23.775 18.563  1.00 21.14 ?  17  MET A CA    1 
ATOM   102  C C     . MET A 1 17  ? -16.291 23.483 17.070  1.00 19.48 ?  17  MET A C     1 
ATOM   103  O O     . MET A 1 17  ? -17.304 23.293 16.389  1.00 16.59 ?  17  MET A O     1 
ATOM   104  C CB    . MET A 1 17  ? -16.394 25.285 18.824  1.00 20.42 ?  17  MET A CB    1 
ATOM   105  C CG    . MET A 1 17  ? -16.924 25.748 20.199  1.00 27.47 ?  17  MET A CG    1 
ATOM   106  S SD    . MET A 1 17  ? -18.287 24.785 20.893  1.00 28.74 ?  17  MET A SD    1 
ATOM   107  C CE    . MET A 1 17  ? -19.681 25.635 20.141  1.00 27.84 ?  17  MET A CE    1 
ATOM   108  N N     . GLY A 1 18  ? -15.066 23.418 16.549  1.00 19.02 ?  18  GLY A N     1 
ATOM   109  C CA    . GLY A 1 18  ? -14.866 23.111 15.140  1.00 19.30 ?  18  GLY A CA    1 
ATOM   110  C C     . GLY A 1 18  ? -15.341 21.734 14.718  1.00 19.18 ?  18  GLY A C     1 
ATOM   111  O O     . GLY A 1 18  ? -15.515 21.492 13.522  1.00 18.33 ?  18  GLY A O     1 
ATOM   112  N N     . HIS A 1 19  ? -15.549 20.824 15.665  1.00 16.23 ?  19  HIS A N     1 
ATOM   113  C CA    . HIS A 1 19  ? -16.122 19.513 15.376  1.00 17.47 ?  19  HIS A CA    1 
ATOM   114  C C     . HIS A 1 19  ? -17.582 19.385 15.803  1.00 18.98 ?  19  HIS A C     1 
ATOM   115  O O     . HIS A 1 19  ? -18.378 18.761 15.087  1.00 17.46 ?  19  HIS A O     1 
ATOM   116  C CB    . HIS A 1 19  ? -15.290 18.411 16.046  1.00 14.89 ?  19  HIS A CB    1 
ATOM   117  C CG    . HIS A 1 19  ? -13.891 18.322 15.513  1.00 18.20 ?  19  HIS A CG    1 
ATOM   118  N ND1   . HIS A 1 19  ? -13.360 17.160 14.987  1.00 18.46 ?  19  HIS A ND1   1 
ATOM   119  C CD2   . HIS A 1 19  ? -12.924 19.266 15.394  1.00 16.78 ?  19  HIS A CD2   1 
ATOM   120  C CE1   . HIS A 1 19  ? -12.122 17.389 14.581  1.00 18.15 ?  19  HIS A CE1   1 
ATOM   121  N NE2   . HIS A 1 19  ? -11.833 18.658 14.817  1.00 17.79 ?  19  HIS A NE2   1 
ATOM   122  N N     . LEU A 1 20  ? -17.948 19.970 16.949  1.00 19.10 ?  20  LEU A N     1 
ATOM   123  C CA    . LEU A 1 20  ? -19.333 19.920 17.428  1.00 18.54 ?  20  LEU A CA    1 
ATOM   124  C C     . LEU A 1 20  ? -20.304 20.562 16.440  1.00 18.94 ?  20  LEU A C     1 
ATOM   125  O O     . LEU A 1 20  ? -21.381 20.018 16.182  1.00 18.56 ?  20  LEU A O     1 
ATOM   126  C CB    . LEU A 1 20  ? -19.437 20.612 18.783  1.00 20.85 ?  20  LEU A CB    1 
ATOM   127  C CG    . LEU A 1 20  ? -18.669 19.919 19.911  1.00 21.63 ?  20  LEU A CG    1 
ATOM   128  C CD1   . LEU A 1 20  ? -18.399 20.910 21.030  1.00 21.74 ?  20  LEU A CD1   1 
ATOM   129  C CD2   . LEU A 1 20  ? -19.439 18.693 20.403  1.00 22.88 ?  20  LEU A CD2   1 
ATOM   130  N N     . ILE A 1 21  ? -19.945 21.717 15.888  1.00 16.93 ?  21  ILE A N     1 
ATOM   131  C CA    . ILE A 1 21  ? -20.816 22.463 14.980  1.00 21.30 ?  21  ILE A CA    1 
ATOM   132  C C     . ILE A 1 21  ? -21.079 21.677 13.689  1.00 19.89 ?  21  ILE A C     1 
ATOM   133  O O     . ILE A 1 21  ? -22.256 21.421 13.380  1.00 19.36 ?  21  ILE A O     1 
ATOM   134  C CB    . ILE A 1 21  ? -20.246 23.868 14.707  1.00 21.02 ?  21  ILE A CB    1 
ATOM   135  C CG1   . ILE A 1 21  ? -20.502 24.788 15.903  1.00 22.60 ?  21  ILE A CG1   1 
ATOM   136  C CG2   . ILE A 1 21  ? -20.788 24.458 13.383  1.00 20.04 ?  21  ILE A CG2   1 
ATOM   137  C CD1   . ILE A 1 21  ? -19.673 26.060 15.867  1.00 21.81 ?  21  ILE A CD1   1 
ATOM   138  N N     . PRO A 1 22  ? -20.062 21.239 12.924  1.00 19.57 ?  22  PRO A N     1 
ATOM   139  C CA    . PRO A 1 22  ? -20.388 20.462 11.706  1.00 16.70 ?  22  PRO A CA    1 
ATOM   140  C C     . PRO A 1 22  ? -21.055 19.128 11.983  1.00 20.11 ?  22  PRO A C     1 
ATOM   141  O O     . PRO A 1 22  ? -21.948 18.748 11.216  1.00 19.12 ?  22  PRO A O     1 
ATOM   142  C CB    . PRO A 1 22  ? -19.040 20.294 10.990  1.00 17.60 ?  22  PRO A CB    1 
ATOM   143  C CG    . PRO A 1 22  ? -17.998 20.685 11.932  1.00 17.34 ?  22  PRO A CG    1 
ATOM   144  C CD    . PRO A 1 22  ? -18.620 21.567 12.998  1.00 18.35 ?  22  PRO A CD    1 
ATOM   145  N N     . TYR A 1 23  ? -20.665 18.401 13.050  1.00 17.55 ?  23  TYR A N     1 
ATOM   146  C CA    . TYR A 1 23  ? -21.367 17.164 13.401  1.00 17.93 ?  23  TYR A CA    1 
ATOM   147  C C     . TYR A 1 23  ? -22.859 17.418 13.632  1.00 19.05 ?  23  TYR A C     1 
ATOM   148  O O     . TYR A 1 23  ? -23.700 16.562 13.334  1.00 18.67 ?  23  TYR A O     1 
ATOM   149  C CB    . TYR A 1 23  ? -20.759 16.544 14.665  1.00 17.07 ?  23  TYR A CB    1 
ATOM   150  C CG    . TYR A 1 23  ? -19.687 15.496 14.461  1.00 18.02 ?  23  TYR A CG    1 
ATOM   151  C CD1   . TYR A 1 23  ? -18.470 15.818 13.853  1.00 12.75 ?  23  TYR A CD1   1 
ATOM   152  C CD2   . TYR A 1 23  ? -19.873 14.197 14.933  1.00 16.76 ?  23  TYR A CD2   1 
ATOM   153  C CE1   . TYR A 1 23  ? -17.475 14.852 13.677  1.00 15.49 ?  23  TYR A CE1   1 
ATOM   154  C CE2   . TYR A 1 23  ? -18.902 13.231 14.771  1.00 16.79 ?  23  TYR A CE2   1 
ATOM   155  C CZ    . TYR A 1 23  ? -17.705 13.554 14.142  1.00 18.52 ?  23  TYR A CZ    1 
ATOM   156  O OH    . TYR A 1 23  ? -16.752 12.577 14.008  1.00 16.52 ?  23  TYR A OH    1 
ATOM   157  N N     . LEU A 1 24  ? -23.189 18.592 14.176  1.00 21.21 ?  24  LEU A N     1 
ATOM   158  C CA    . LEU A 1 24  ? -24.566 19.003 14.402  1.00 21.34 ?  24  LEU A CA    1 
ATOM   159  C C     . LEU A 1 24  ? -25.256 19.436 13.111  1.00 22.40 ?  24  LEU A C     1 
ATOM   160  O O     . LEU A 1 24  ? -26.426 19.099 12.909  1.00 22.73 ?  24  LEU A O     1 
ATOM   161  C CB    . LEU A 1 24  ? -24.604 20.129 15.437  1.00 21.05 ?  24  LEU A CB    1 
ATOM   162  C CG    . LEU A 1 24  ? -25.289 19.734 16.742  1.00 30.23 ?  24  LEU A CG    1 
ATOM   163  C CD1   . LEU A 1 24  ? -25.582 20.962 17.615  1.00 37.35 ?  24  LEU A CD1   1 
ATOM   164  C CD2   . LEU A 1 24  ? -26.563 18.947 16.471  1.00 25.05 ?  24  LEU A CD2   1 
ATOM   165  N N     . HIS A 1 25  ? -24.572 20.189 12.233  1.00 22.74 ?  25  HIS A N     1 
ATOM   166  C CA    . HIS A 1 25  ? -25.142 20.465 10.912  1.00 22.19 ?  25  HIS A CA    1 
ATOM   167  C C     . HIS A 1 25  ? -25.545 19.165 10.222  1.00 24.13 ?  25  HIS A C     1 
ATOM   168  O O     . HIS A 1 25  ? -26.626 19.076 9.629   1.00 23.65 ?  25  HIS A O     1 
ATOM   169  C CB    . HIS A 1 25  ? -24.158 21.212 9.996   1.00 18.77 ?  25  HIS A CB    1 
ATOM   170  C CG    . HIS A 1 25  ? -23.837 22.624 10.401  1.00 26.08 ?  25  HIS A CG    1 
ATOM   171  N ND1   . HIS A 1 25  ? -24.742 23.466 11.010  1.00 22.51 ?  25  HIS A ND1   1 
ATOM   172  C CD2   . HIS A 1 25  ? -22.696 23.349 10.247  1.00 26.00 ?  25  HIS A CD2   1 
ATOM   173  C CE1   . HIS A 1 25  ? -24.171 24.640 11.230  1.00 23.17 ?  25  HIS A CE1   1 
ATOM   174  N NE2   . HIS A 1 25  ? -22.932 24.597 10.769  1.00 22.69 ?  25  HIS A NE2   1 
ATOM   175  N N     . LEU A 1 26  ? -24.672 18.148 10.277  1.00 19.76 ?  26  LEU A N     1 
ATOM   176  C CA    . LEU A 1 26  ? -24.935 16.886 9.584   1.00 22.67 ?  26  LEU A CA    1 
ATOM   177  C C     . LEU A 1 26  ? -26.058 16.090 10.249  1.00 18.93 ?  26  LEU A C     1 
ATOM   178  O O     . LEU A 1 26  ? -26.854 15.446 9.557   1.00 19.63 ?  26  LEU A O     1 
ATOM   179  C CB    . LEU A 1 26  ? -23.656 16.046 9.521   1.00 19.33 ?  26  LEU A CB    1 
ATOM   180  C CG    . LEU A 1 26  ? -23.732 14.712 8.778   1.00 19.64 ?  26  LEU A CG    1 
ATOM   181  C CD1   . LEU A 1 26  ? -24.110 14.891 7.283   1.00 17.14 ?  26  LEU A CD1   1 
ATOM   182  C CD2   . LEU A 1 26  ? -22.390 13.990 8.933   1.00 18.65 ?  26  LEU A CD2   1 
ATOM   183  N N     . SER A 1 27  ? -26.108 16.092 11.587  1.00 19.36 ?  27  SER A N     1 
ATOM   184  C CA    . SER A 1 27  ? -27.200 15.443 12.316  1.00 21.16 ?  27  SER A CA    1 
ATOM   185  C C     . SER A 1 27  ? -28.561 15.982 11.891  1.00 24.24 ?  27  SER A C     1 
ATOM   186  O O     . SER A 1 27  ? -29.511 15.212 11.717  1.00 23.54 ?  27  SER A O     1 
ATOM   187  C CB    . SER A 1 27  ? -27.022 15.631 13.823  1.00 23.84 ?  27  SER A CB    1 
ATOM   188  O OG    . SER A 1 27  ? -25.787 15.103 14.276  1.00 26.38 ?  27  SER A OG    1 
ATOM   189  N N     . ASN A 1 28  ? -28.678 17.305 11.735  1.00 22.22 ?  28  ASN A N     1 
ATOM   190  C CA    . ASN A 1 28  ? -29.924 17.890 11.251  1.00 25.73 ?  28  ASN A CA    1 
ATOM   191  C C     . ASN A 1 28  ? -30.271 17.369 9.856   1.00 27.45 ?  28  ASN A C     1 
ATOM   192  O O     . ASN A 1 28  ? -31.439 17.081 9.564   1.00 25.84 ?  28  ASN A O     1 
ATOM   193  C CB    . ASN A 1 28  ? -29.815 19.418 11.246  1.00 24.10 ?  28  ASN A CB    1 
ATOM   194  C CG    . ASN A 1 28  ? -29.861 20.023 12.641  1.00 28.66 ?  28  ASN A CG    1 
ATOM   195  O OD1   . ASN A 1 28  ? -30.668 19.619 13.470  1.00 28.38 ?  28  ASN A OD1   1 
ATOM   196  N ND2   . ASN A 1 28  ? -29.002 21.013 12.900  1.00 30.89 ?  28  ASN A ND2   1 
ATOM   197  N N     . LYS A 1 29  ? -29.269 17.233 8.981   1.00 22.97 ?  29  LYS A N     1 
ATOM   198  C CA    . LYS A 1 29  ? -29.524 16.691 7.645   1.00 24.37 ?  29  LYS A CA    1 
ATOM   199  C C     . LYS A 1 29  ? -29.958 15.230 7.695   1.00 26.89 ?  29  LYS A C     1 
ATOM   200  O O     . LYS A 1 29  ? -30.791 14.805 6.884   1.00 29.43 ?  29  LYS A O     1 
ATOM   201  C CB    . LYS A 1 29  ? -28.279 16.850 6.766   1.00 22.95 ?  29  LYS A CB    1 
ATOM   202  C CG    . LYS A 1 29  ? -27.792 18.307 6.672   1.00 22.76 ?  29  LYS A CG    1 
ATOM   203  C CD    . LYS A 1 29  ? -26.546 18.467 5.787   1.00 22.88 ?  29  LYS A CD    1 
ATOM   204  C CE    . LYS A 1 29  ? -25.920 19.860 5.936   1.00 24.26 ?  29  LYS A CE    1 
ATOM   205  N NZ    . LYS A 1 29  ? -26.782 20.959 5.386   1.00 23.78 ?  29  LYS A NZ    1 
ATOM   206  N N     . LEU A 1 30  ? -29.410 14.452 8.629   1.00 20.48 ?  30  LEU A N     1 
ATOM   207  C CA    . LEU A 1 30  ? -29.775 13.047 8.741   1.00 21.60 ?  30  LEU A CA    1 
ATOM   208  C C     . LEU A 1 30  ? -31.158 12.884 9.371   1.00 24.70 ?  30  LEU A C     1 
ATOM   209  O O     . LEU A 1 30  ? -31.951 12.034 8.940   1.00 24.07 ?  30  LEU A O     1 
ATOM   210  C CB    . LEU A 1 30  ? -28.708 12.304 9.549   1.00 19.32 ?  30  LEU A CB    1 
ATOM   211  C CG    . LEU A 1 30  ? -27.308 12.251 8.906   1.00 20.04 ?  30  LEU A CG    1 
ATOM   212  C CD1   . LEU A 1 30  ? -26.301 11.563 9.829   1.00 21.39 ?  30  LEU A CD1   1 
ATOM   213  C CD2   . LEU A 1 30  ? -27.336 11.553 7.545   1.00 19.78 ?  30  LEU A CD2   1 
ATOM   214  N N     . ALA A 1 31  ? -31.467 13.701 10.377  1.00 24.14 ?  31  ALA A N     1 
ATOM   215  C CA    . ALA A 1 31  ? -32.764 13.629 11.039  1.00 26.70 ?  31  ALA A CA    1 
ATOM   216  C C     . ALA A 1 31  ? -33.892 14.094 10.123  1.00 31.32 ?  31  ALA A C     1 
ATOM   217  O O     . ALA A 1 31  ? -35.016 13.586 10.225  1.00 28.86 ?  31  ALA A O     1 
ATOM   218  C CB    . ALA A 1 31  ? -32.733 14.451 12.328  1.00 26.25 ?  31  ALA A CB    1 
ATOM   219  N N     . LYS A 1 32  ? -33.618 15.054 9.229   1.00 29.53 ?  32  LYS A N     1 
ATOM   220  C CA    . LYS A 1 32  ? -34.594 15.423 8.211   1.00 29.26 ?  32  LYS A CA    1 
ATOM   221  C C     . LYS A 1 32  ? -35.009 14.218 7.375   1.00 31.79 ?  32  LYS A C     1 
ATOM   222  O O     . LYS A 1 32  ? -36.170 14.120 6.964   1.00 34.08 ?  32  LYS A O     1 
ATOM   223  C CB    . LYS A 1 32  ? -34.037 16.527 7.308   1.00 28.88 ?  32  LYS A CB    1 
ATOM   224  C CG    . LYS A 1 32  ? -35.096 17.236 6.483   1.00 29.38 ?  32  LYS A CG    1 
ATOM   225  C CD    . LYS A 1 32  ? -34.505 18.141 5.437   1.00 33.53 ?  32  LYS A CD    1 
ATOM   226  C CE    . LYS A 1 32  ? -35.605 18.735 4.576   1.00 38.19 ?  32  LYS A CE    1 
ATOM   227  N NZ    . LYS A 1 32  ? -35.627 18.146 3.206   1.00 48.98 ?  32  LYS A NZ    1 
ATOM   228  N N     . ARG A 1 33  ? -34.091 13.284 7.132   1.00 29.25 ?  33  ARG A N     1 
ATOM   229  C CA    . ARG A 1 33  ? -34.390 12.068 6.383   1.00 29.24 ?  33  ARG A CA    1 
ATOM   230  C C     . ARG A 1 33  ? -34.932 10.931 7.264   1.00 29.04 ?  33  ARG A C     1 
ATOM   231  O O     . ARG A 1 33  ? -35.042 9.789  6.797   1.00 28.96 ?  33  ARG A O     1 
ATOM   232  C CB    . ARG A 1 33  ? -33.139 11.615 5.632   1.00 26.76 ?  33  ARG A CB    1 
ATOM   233  C CG    . ARG A 1 33  ? -32.846 12.452 4.404   1.00 27.71 ?  33  ARG A CG    1 
ATOM   234  C CD    . ARG A 1 33  ? -31.357 12.575 4.123   1.00 29.36 ?  33  ARG A CD    1 
ATOM   235  N NE    . ARG A 1 33  ? -31.102 13.412 2.954   1.00 33.50 ?  33  ARG A NE    1 
ATOM   236  C CZ    . ARG A 1 33  ? -30.873 12.942 1.735   1.00 31.59 ?  33  ARG A CZ    1 
ATOM   237  N NH1   . ARG A 1 33  ? -30.824 11.637 1.493   1.00 30.37 ?  33  ARG A NH1   1 
ATOM   238  N NH2   . ARG A 1 33  ? -30.680 13.798 0.735   1.00 27.36 ?  33  ARG A NH2   1 
ATOM   239  N N     . GLY A 1 34  ? -35.231 11.206 8.526   1.00 26.29 ?  34  GLY A N     1 
ATOM   240  C CA    . GLY A 1 34  ? -35.856 10.240 9.404   1.00 31.22 ?  34  GLY A CA    1 
ATOM   241  C C     . GLY A 1 34  ? -34.934 9.455  10.314  1.00 29.72 ?  34  GLY A C     1 
ATOM   242  O O     . GLY A 1 34  ? -35.420 8.600  11.058  1.00 28.10 ?  34  GLY A O     1 
ATOM   243  N N     . HIS A 1 35  ? -33.630 9.721  10.307  1.00 26.64 ?  35  HIS A N     1 
ATOM   244  C CA    . HIS A 1 35  ? -32.738 8.957  11.167  1.00 26.84 ?  35  HIS A CA    1 
ATOM   245  C C     . HIS A 1 35  ? -32.696 9.555  12.567  1.00 26.78 ?  35  HIS A C     1 
ATOM   246  O O     . HIS A 1 35  ? -32.756 10.779 12.748  1.00 27.51 ?  35  HIS A O     1 
ATOM   247  C CB    . HIS A 1 35  ? -31.331 8.890  10.571  1.00 31.23 ?  35  HIS A CB    1 
ATOM   248  C CG    . HIS A 1 35  ? -31.307 8.382  9.162   1.00 30.33 ?  35  HIS A CG    1 
ATOM   249  N ND1   . HIS A 1 35  ? -31.486 7.054  8.848   1.00 29.91 ?  35  HIS A ND1   1 
ATOM   250  C CD2   . HIS A 1 35  ? -31.147 9.028  7.983   1.00 27.28 ?  35  HIS A CD2   1 
ATOM   251  C CE1   . HIS A 1 35  ? -31.427 6.900  7.539   1.00 27.93 ?  35  HIS A CE1   1 
ATOM   252  N NE2   . HIS A 1 35  ? -31.216 8.082  6.989   1.00 24.22 ?  35  HIS A NE2   1 
ATOM   253  N N     . LYS A 1 36  ? -32.611 8.670  13.554  1.00 24.85 ?  36  LYS A N     1 
ATOM   254  C CA    . LYS A 1 36  ? -32.503 9.039  14.954  1.00 25.23 ?  36  LYS A CA    1 
ATOM   255  C C     . LYS A 1 36  ? -31.031 9.193  15.319  1.00 23.04 ?  36  LYS A C     1 
ATOM   256  O O     . LYS A 1 36  ? -30.212 8.346  14.957  1.00 24.13 ?  36  LYS A O     1 
ATOM   257  C CB    . LYS A 1 36  ? -33.152 7.968  15.834  1.00 25.55 ?  36  LYS A CB    1 
ATOM   258  C CG    . LYS A 1 36  ? -33.173 8.308  17.291  1.00 26.20 ?  36  LYS A CG    1 
ATOM   259  C CD    . LYS A 1 36  ? -32.983 7.057  18.155  1.00 37.25 ?  36  LYS A CD    1 
ATOM   260  C CE    . LYS A 1 36  ? -34.087 6.026  17.968  1.00 34.05 ?  36  LYS A CE    1 
ATOM   261  N NZ    . LYS A 1 36  ? -35.115 6.090  19.060  1.00 49.25 ?  36  LYS A NZ    1 
ATOM   262  N N     . ILE A 1 37  ? -30.711 10.265 16.046  1.00 23.82 ?  37  ILE A N     1 
ATOM   263  C CA    . ILE A 1 37  ? -29.340 10.666 16.349  1.00 24.77 ?  37  ILE A CA    1 
ATOM   264  C C     . ILE A 1 37  ? -29.184 10.775 17.867  1.00 26.01 ?  37  ILE A C     1 
ATOM   265  O O     . ILE A 1 37  ? -29.902 11.540 18.521  1.00 24.19 ?  37  ILE A O     1 
ATOM   266  C CB    . ILE A 1 37  ? -28.972 12.000 15.668  1.00 27.57 ?  37  ILE A CB    1 
ATOM   267  C CG1   . ILE A 1 37  ? -29.222 11.965 14.147  1.00 23.73 ?  37  ILE A CG1   1 
ATOM   268  C CG2   . ILE A 1 37  ? -27.536 12.429 16.003  1.00 23.53 ?  37  ILE A CG2   1 
ATOM   269  C CD1   . ILE A 1 37  ? -28.418 10.933 13.388  1.00 24.01 ?  37  ILE A CD1   1 
ATOM   270  N N     . SER A 1 38  ? -28.243 10.015 18.420  1.00 25.18 ?  38  SER A N     1 
ATOM   271  C CA    . SER A 1 38  ? -27.840 10.123 19.817  1.00 27.70 ?  38  SER A CA    1 
ATOM   272  C C     . SER A 1 38  ? -26.521 10.891 19.875  1.00 25.39 ?  38  SER A C     1 
ATOM   273  O O     . SER A 1 38  ? -25.473 10.338 19.538  1.00 26.78 ?  38  SER A O     1 
ATOM   274  C CB    . SER A 1 38  ? -27.690 8.733  20.433  1.00 28.67 ?  38  SER A CB    1 
ATOM   275  O OG    . SER A 1 38  ? -28.930 8.039  20.495  1.00 31.86 ?  38  SER A OG    1 
ATOM   276  N N     . PHE A 1 39  ? -26.563 12.150 20.339  1.00 25.98 ?  39  PHE A N     1 
ATOM   277  C CA    . PHE A 1 39  ? -25.432 13.079 20.235  1.00 27.26 ?  39  PHE A CA    1 
ATOM   278  C C     . PHE A 1 39  ? -24.699 13.221 21.574  1.00 27.55 ?  39  PHE A C     1 
ATOM   279  O O     . PHE A 1 39  ? -25.177 13.929 22.468  1.00 26.12 ?  39  PHE A O     1 
ATOM   280  C CB    . PHE A 1 39  ? -25.920 14.448 19.750  1.00 23.38 ?  39  PHE A CB    1 
ATOM   281  C CG    . PHE A 1 39  ? -24.826 15.316 19.170  1.00 25.21 ?  39  PHE A CG    1 
ATOM   282  C CD1   . PHE A 1 39  ? -23.868 15.913 20.000  1.00 27.96 ?  39  PHE A CD1   1 
ATOM   283  C CD2   . PHE A 1 39  ? -24.749 15.541 17.794  1.00 24.79 ?  39  PHE A CD2   1 
ATOM   284  C CE1   . PHE A 1 39  ? -22.839 16.707 19.460  1.00 23.43 ?  39  PHE A CE1   1 
ATOM   285  C CE2   . PHE A 1 39  ? -23.725 16.342 17.251  1.00 22.87 ?  39  PHE A CE2   1 
ATOM   286  C CZ    . PHE A 1 39  ? -22.775 16.923 18.090  1.00 19.76 ?  39  PHE A CZ    1 
ATOM   287  N N     . PHE A 1 40  ? -23.503 12.616 21.689  1.00 23.43 ?  40  PHE A N     1 
ATOM   288  C CA    . PHE A 1 40  ? -22.718 12.692 22.925  1.00 24.76 ?  40  PHE A CA    1 
ATOM   289  C C     . PHE A 1 40  ? -21.918 13.991 22.970  1.00 28.59 ?  40  PHE A C     1 
ATOM   290  O O     . PHE A 1 40  ? -21.077 14.236 22.095  1.00 27.96 ?  40  PHE A O     1 
ATOM   291  C CB    . PHE A 1 40  ? -21.749 11.516 23.067  1.00 24.60 ?  40  PHE A CB    1 
ATOM   292  C CG    . PHE A 1 40  ? -22.382 10.150 22.929  1.00 25.30 ?  40  PHE A CG    1 
ATOM   293  C CD1   . PHE A 1 40  ? -23.730 9.946  23.172  1.00 26.24 ?  40  PHE A CD1   1 
ATOM   294  C CD2   . PHE A 1 40  ? -21.600 9.065  22.575  1.00 25.31 ?  40  PHE A CD2   1 
ATOM   295  C CE1   . PHE A 1 40  ? -24.291 8.674  23.047  1.00 26.03 ?  40  PHE A CE1   1 
ATOM   296  C CE2   . PHE A 1 40  ? -22.141 7.803  22.456  1.00 28.87 ?  40  PHE A CE2   1 
ATOM   297  C CZ    . PHE A 1 40  ? -23.500 7.607  22.686  1.00 27.32 ?  40  PHE A CZ    1 
ATOM   298  N N     . THR A 1 41  ? -22.130 14.792 24.012  1.00 24.40 ?  41  THR A N     1 
ATOM   299  C CA    . THR A 1 41  ? -21.485 16.089 24.157  1.00 27.00 ?  41  THR A CA    1 
ATOM   300  C C     . THR A 1 41  ? -21.048 16.308 25.598  1.00 31.17 ?  41  THR A C     1 
ATOM   301  O O     . THR A 1 41  ? -21.665 15.773 26.525  1.00 28.14 ?  41  THR A O     1 
ATOM   302  C CB    . THR A 1 41  ? -22.422 17.237 23.759  1.00 29.85 ?  41  THR A CB    1 
ATOM   303  O OG1   . THR A 1 41  ? -21.831 18.488 24.137  1.00 31.22 ?  41  THR A OG1   1 
ATOM   304  C CG2   . THR A 1 41  ? -23.772 17.089 24.472  1.00 29.29 ?  41  THR A CG2   1 
ATOM   305  N N     . PRO A 1 42  ? -19.990 17.089 25.814  1.00 32.72 ?  42  PRO A N     1 
ATOM   306  C CA    . PRO A 1 42  ? -19.652 17.503 27.179  1.00 32.00 ?  42  PRO A CA    1 
ATOM   307  C C     . PRO A 1 42  ? -20.804 18.251 27.840  1.00 27.90 ?  42  PRO A C     1 
ATOM   308  O O     . PRO A 1 42  ? -21.543 18.998 27.197  1.00 26.34 ?  42  PRO A O     1 
ATOM   309  C CB    . PRO A 1 42  ? -18.430 18.402 26.977  1.00 31.70 ?  42  PRO A CB    1 
ATOM   310  C CG    . PRO A 1 42  ? -17.767 17.813 25.761  1.00 27.84 ?  42  PRO A CG    1 
ATOM   311  C CD    . PRO A 1 42  ? -18.898 17.380 24.864  1.00 29.03 ?  42  PRO A CD    1 
ATOM   312  N N     . LYS A 1 43  ? -20.918 18.050 29.157  1.00 33.46 ?  43  LYS A N     1 
ATOM   313  C CA    . LYS A 1 43  ? -22.123 18.402 29.907  1.00 29.64 ?  43  LYS A CA    1 
ATOM   314  C C     . LYS A 1 43  ? -22.438 19.889 29.801  1.00 29.47 ?  43  LYS A C     1 
ATOM   315  O O     . LYS A 1 43  ? -23.527 20.270 29.362  1.00 27.51 ?  43  LYS A O     1 
ATOM   316  C CB    . LYS A 1 43  ? -21.956 17.977 31.367  1.00 32.83 ?  43  LYS A CB    1 
ATOM   317  C CG    . LYS A 1 43  ? -23.034 18.488 32.326  1.00 36.89 ?  43  LYS A CG    1 
ATOM   318  C CD    . LYS A 1 43  ? -23.344 17.445 33.411  1.00 36.72 ?  43  LYS A CD    1 
ATOM   319  C CE    . LYS A 1 43  ? -24.068 18.058 34.609  1.00 34.70 ?  43  LYS A CE    1 
ATOM   320  N NZ    . LYS A 1 43  ? -25.493 18.421 34.341  1.00 31.90 ?  43  LYS A NZ    1 
ATOM   321  N N     . LYS A 1 44  ? -21.489 20.754 30.184  1.00 28.00 ?  44  LYS A N     1 
ATOM   322  C CA    . LYS A 1 44  ? -21.787 22.188 30.187  1.00 29.28 ?  44  LYS A CA    1 
ATOM   323  C C     . LYS A 1 44  ? -21.934 22.740 28.767  1.00 31.60 ?  44  LYS A C     1 
ATOM   324  O O     . LYS A 1 44  ? -22.724 23.668 28.532  1.00 29.76 ?  44  LYS A O     1 
ATOM   325  C CB    . LYS A 1 44  ? -20.709 22.950 30.968  1.00 30.45 ?  44  LYS A CB    1 
ATOM   326  C CG    . LYS A 1 44  ? -20.718 22.639 32.483  1.00 36.84 ?  44  LYS A CG    1 
ATOM   327  C CD    . LYS A 1 44  ? -19.678 23.457 33.257  1.00 40.54 ?  44  LYS A CD    1 
ATOM   328  C CE    . LYS A 1 44  ? -18.246 23.140 32.829  1.00 34.93 ?  44  LYS A CE    1 
ATOM   329  N NZ    . LYS A 1 44  ? -17.788 21.796 33.273  1.00 36.55 ?  44  LYS A NZ    1 
ATOM   330  N N     . THR A 1 45  ? -21.224 22.153 27.807  1.00 32.33 ?  45  THR A N     1 
ATOM   331  C CA    . THR A 1 45  ? -21.282 22.619 26.423  1.00 28.67 ?  45  THR A CA    1 
ATOM   332  C C     . THR A 1 45  ? -22.672 22.465 25.810  1.00 34.42 ?  45  THR A C     1 
ATOM   333  O O     . THR A 1 45  ? -23.035 23.226 24.900  1.00 33.39 ?  45  THR A O     1 
ATOM   334  C CB    . THR A 1 45  ? -20.229 21.859 25.613  1.00 32.31 ?  45  THR A CB    1 
ATOM   335  O OG1   . THR A 1 45  ? -18.961 21.993 26.276  1.00 29.47 ?  45  THR A OG1   1 
ATOM   336  C CG2   . THR A 1 45  ? -20.123 22.378 24.181  1.00 26.85 ?  45  THR A CG2   1 
ATOM   337  N N     . GLN A 1 46  ? -23.477 21.517 26.302  1.00 29.13 ?  46  GLN A N     1 
ATOM   338  C CA    . GLN A 1 46  ? -24.780 21.282 25.687  1.00 28.75 ?  46  GLN A CA    1 
ATOM   339  C C     . GLN A 1 46  ? -25.611 22.564 25.584  1.00 35.26 ?  46  GLN A C     1 
ATOM   340  O O     . GLN A 1 46  ? -26.313 22.769 24.586  1.00 31.24 ?  46  GLN A O     1 
ATOM   341  C CB    . GLN A 1 46  ? -25.552 20.208 26.461  1.00 36.03 ?  46  GLN A CB    1 
ATOM   342  C CG    . GLN A 1 46  ? -26.936 19.956 25.881  1.00 31.30 ?  46  GLN A CG    1 
ATOM   343  C CD    . GLN A 1 46  ? -27.694 18.862 26.596  1.00 34.26 ?  46  GLN A CD    1 
ATOM   344  O OE1   . GLN A 1 46  ? -27.115 17.866 27.045  1.00 32.81 ?  46  GLN A OE1   1 
ATOM   345  N NE2   . GLN A 1 46  ? -29.006 19.047 26.716  1.00 35.46 ?  46  GLN A NE2   1 
ATOM   346  N N     . THR A 1 47  ? -25.522 23.450 26.590  1.00 32.12 ?  47  THR A N     1 
ATOM   347  C CA    . THR A 1 47  ? -26.264 24.712 26.553  1.00 35.83 ?  47  THR A CA    1 
ATOM   348  C C     . THR A 1 47  ? -25.986 25.492 25.285  1.00 33.34 ?  47  THR A C     1 
ATOM   349  O O     . THR A 1 47  ? -26.895 26.100 24.708  1.00 33.15 ?  47  THR A O     1 
ATOM   350  C CB    . THR A 1 47  ? -25.905 25.615 27.741  1.00 38.88 ?  47  THR A CB    1 
ATOM   351  O OG1   . THR A 1 47  ? -25.632 24.830 28.903  1.00 48.95 ?  47  THR A OG1   1 
ATOM   352  C CG2   . THR A 1 47  ? -27.054 26.595 28.025  1.00 37.15 ?  47  THR A CG2   1 
ATOM   353  N N     . LYS A 1 48  ? -24.717 25.529 24.866  1.00 36.34 ?  48  LYS A N     1 
ATOM   354  C CA    . LYS A 1 48  ? -24.337 26.260 23.666  1.00 34.99 ?  48  LYS A CA    1 
ATOM   355  C C     . LYS A 1 48  ? -24.787 25.549 22.396  1.00 32.45 ?  48  LYS A C     1 
ATOM   356  O O     . LYS A 1 48  ? -24.792 26.164 21.326  1.00 34.87 ?  48  LYS A O     1 
ATOM   357  C CB    . LYS A 1 48  ? -22.815 26.474 23.638  1.00 34.15 ?  48  LYS A CB    1 
ATOM   358  C CG    . LYS A 1 48  ? -22.239 27.201 24.863  1.00 46.61 ?  48  LYS A CG    1 
ATOM   359  C CD    . LYS A 1 48  ? -20.731 26.928 25.029  1.00 52.29 ?  48  LYS A CD    1 
ATOM   360  C CE    . LYS A 1 48  ? -20.011 28.055 25.780  1.00 62.24 ?  48  LYS A CE    1 
ATOM   361  N NZ    . LYS A 1 48  ? -19.273 27.583 27.003  1.00 58.29 ?  48  LYS A NZ    1 
ATOM   362  N N     . LEU A 1 49  ? -25.166 24.276 22.481  1.00 31.12 ?  49  LEU A N     1 
ATOM   363  C CA    . LEU A 1 49  ? -25.514 23.523 21.282  1.00 29.86 ?  49  LEU A CA    1 
ATOM   364  C C     . LEU A 1 49  ? -27.007 23.500 20.979  1.00 32.48 ?  49  LEU A C     1 
ATOM   365  O O     . LEU A 1 49  ? -27.375 23.177 19.845  1.00 33.40 ?  49  LEU A O     1 
ATOM   366  C CB    . LEU A 1 49  ? -25.000 22.086 21.394  1.00 28.84 ?  49  LEU A CB    1 
ATOM   367  C CG    . LEU A 1 49  ? -23.484 21.955 21.597  1.00 31.40 ?  49  LEU A CG    1 
ATOM   368  C CD1   . LEU A 1 49  ? -23.034 20.502 21.611  1.00 23.71 ?  49  LEU A CD1   1 
ATOM   369  C CD2   . LEU A 1 49  ? -22.723 22.759 20.549  1.00 29.67 ?  49  LEU A CD2   1 
ATOM   370  N N     . GLU A 1 50  ? -27.870 23.858 21.941  1.00 33.96 ?  50  GLU A N     1 
ATOM   371  C CA    . GLU A 1 50  ? -29.316 23.695 21.753  1.00 32.54 ?  50  GLU A CA    1 
ATOM   372  C C     . GLU A 1 50  ? -29.831 24.502 20.567  1.00 29.96 ?  50  GLU A C     1 
ATOM   373  O O     . GLU A 1 50  ? -30.727 24.051 19.844  1.00 28.32 ?  50  GLU A O     1 
ATOM   374  C CB    . GLU A 1 50  ? -30.072 24.104 23.024  1.00 36.74 ?  50  GLU A CB    1 
ATOM   375  C CG    . GLU A 1 50  ? -29.703 23.339 24.296  1.00 34.05 ?  50  GLU A CG    1 
ATOM   376  C CD    . GLU A 1 50  ? -30.350 21.963 24.370  1.00 40.89 ?  50  GLU A CD    1 
ATOM   377  O OE1   . GLU A 1 50  ? -31.209 21.666 23.516  1.00 42.65 ?  50  GLU A OE1   1 
ATOM   378  O OE2   . GLU A 1 50  ? -29.998 21.170 25.279  1.00 40.49 -1 50  GLU A OE2   1 
ATOM   379  N N     . GLN A 1 51  ? -29.278 25.700 20.353  1.00 32.36 ?  51  GLN A N     1 
ATOM   380  C CA    . GLN A 1 51  ? -29.731 26.584 19.280  1.00 35.06 ?  51  GLN A CA    1 
ATOM   381  C C     . GLN A 1 51  ? -29.594 25.955 17.895  1.00 35.27 ?  51  GLN A C     1 
ATOM   382  O O     . GLN A 1 51  ? -30.238 26.419 16.945  1.00 36.63 ?  51  GLN A O     1 
ATOM   383  C CB    . GLN A 1 51  ? -28.937 27.895 19.321  1.00 37.84 ?  51  GLN A CB    1 
ATOM   384  C CG    . GLN A 1 51  ? -27.428 27.676 19.251  1.00 36.62 ?  51  GLN A CG    1 
ATOM   385  C CD    . GLN A 1 51  ? -26.623 28.946 19.437  1.00 43.89 ?  51  GLN A CD    1 
ATOM   386  O OE1   . GLN A 1 51  ? -26.974 30.010 18.916  1.00 46.51 ?  51  GLN A OE1   1 
ATOM   387  N NE2   . GLN A 1 51  ? -25.527 28.839 20.184  1.00 41.27 ?  51  GLN A NE2   1 
ATOM   388  N N     . PHE A 1 52  ? -28.770 24.915 17.758  1.00 32.72 ?  52  PHE A N     1 
ATOM   389  C CA    . PHE A 1 52  ? -28.528 24.267 16.480  1.00 31.48 ?  52  PHE A CA    1 
ATOM   390  C C     . PHE A 1 52  ? -29.345 22.994 16.278  1.00 32.82 ?  52  PHE A C     1 
ATOM   391  O O     . PHE A 1 52  ? -29.363 22.462 15.162  1.00 33.44 ?  52  PHE A O     1 
ATOM   392  C CB    . PHE A 1 52  ? -27.032 23.948 16.340  1.00 30.74 ?  52  PHE A CB    1 
ATOM   393  C CG    . PHE A 1 52  ? -26.135 25.135 16.562  1.00 33.17 ?  52  PHE A CG    1 
ATOM   394  C CD1   . PHE A 1 52  ? -26.354 26.318 15.890  1.00 37.91 ?  52  PHE A CD1   1 
ATOM   395  C CD2   . PHE A 1 52  ? -25.059 25.058 17.434  1.00 38.42 ?  52  PHE A CD2   1 
ATOM   396  C CE1   . PHE A 1 52  ? -25.526 27.402 16.084  1.00 39.78 ?  52  PHE A CE1   1 
ATOM   397  C CE2   . PHE A 1 52  ? -24.223 26.142 17.630  1.00 38.46 ?  52  PHE A CE2   1 
ATOM   398  C CZ    . PHE A 1 52  ? -24.462 27.316 16.957  1.00 39.73 ?  52  PHE A CZ    1 
ATOM   399  N N     . ASN A 1 53  ? -30.007 22.487 17.320  1.00 35.74 ?  53  ASN A N     1 
ATOM   400  C CA    . ASN A 1 53  ? -30.842 21.293 17.203  1.00 30.07 ?  53  ASN A CA    1 
ATOM   401  C C     . ASN A 1 53  ? -32.165 21.680 16.558  1.00 31.51 ?  53  ASN A C     1 
ATOM   402  O O     . ASN A 1 53  ? -33.021 22.295 17.200  1.00 33.34 ?  53  ASN A O     1 
ATOM   403  C CB    . ASN A 1 53  ? -31.076 20.653 18.566  1.00 29.67 ?  53  ASN A CB    1 
ATOM   404  C CG    . ASN A 1 53  ? -31.783 19.300 18.463  1.00 31.77 ?  53  ASN A CG    1 
ATOM   405  O OD1   . ASN A 1 53  ? -32.336 18.942 17.416  1.00 31.31 ?  53  ASN A OD1   1 
ATOM   406  N ND2   . ASN A 1 53  ? -31.768 18.548 19.547  1.00 31.25 ?  53  ASN A ND2   1 
ATOM   407  N N     . LEU A 1 54  ? -32.343 21.318 15.296  1.00 28.39 ?  54  LEU A N     1 
ATOM   408  C CA    . LEU A 1 54  ? -33.565 21.642 14.577  1.00 31.31 ?  54  LEU A CA    1 
ATOM   409  C C     . LEU A 1 54  ? -34.563 20.489 14.567  1.00 32.63 ?  54  LEU A C     1 
ATOM   410  O O     . LEU A 1 54  ? -35.636 20.628 13.968  1.00 29.22 ?  54  LEU A O     1 
ATOM   411  C CB    . LEU A 1 54  ? -33.238 22.067 13.135  1.00 25.16 ?  54  LEU A CB    1 
ATOM   412  C CG    . LEU A 1 54  ? -32.110 23.083 12.924  1.00 29.77 ?  54  LEU A CG    1 
ATOM   413  C CD1   . LEU A 1 54  ? -31.829 23.367 11.442  1.00 26.49 ?  54  LEU A CD1   1 
ATOM   414  C CD2   . LEU A 1 54  ? -32.432 24.373 13.649  1.00 28.72 ?  54  LEU A CD2   1 
ATOM   415  N N     . TYR A 1 55  ? -34.234 19.353 15.192  1.00 30.78 ?  55  TYR A N     1 
ATOM   416  C CA    . TYR A 1 55  ? -35.116 18.178 15.231  1.00 30.97 ?  55  TYR A CA    1 
ATOM   417  C C     . TYR A 1 55  ? -35.031 17.513 16.601  1.00 29.09 ?  55  TYR A C     1 
ATOM   418  O O     . TYR A 1 55  ? -34.612 16.356 16.732  1.00 26.56 ?  55  TYR A O     1 
ATOM   419  C CB    . TYR A 1 55  ? -34.762 17.192 14.116  1.00 28.61 ?  55  TYR A CB    1 
ATOM   420  C CG    . TYR A 1 55  ? -34.914 17.801 12.747  1.00 31.45 ?  55  TYR A CG    1 
ATOM   421  C CD1   . TYR A 1 55  ? -33.867 18.488 12.153  1.00 26.48 ?  55  TYR A CD1   1 
ATOM   422  C CD2   . TYR A 1 55  ? -36.123 17.708 12.055  1.00 35.64 ?  55  TYR A CD2   1 
ATOM   423  C CE1   . TYR A 1 55  ? -34.007 19.065 10.922  1.00 26.95 ?  55  TYR A CE1   1 
ATOM   424  C CE2   . TYR A 1 55  ? -36.275 18.275 10.814  1.00 30.46 ?  55  TYR A CE2   1 
ATOM   425  C CZ    . TYR A 1 55  ? -35.209 18.953 10.249  1.00 36.52 ?  55  TYR A CZ    1 
ATOM   426  O OH    . TYR A 1 55  ? -35.345 19.521 9.007   1.00 34.80 ?  55  TYR A OH    1 
ATOM   427  N N     . PRO A 1 56  ? -35.483 18.211 17.649  1.00 34.32 ?  56  PRO A N     1 
ATOM   428  C CA    . PRO A 1 56  ? -35.308 17.699 19.020  1.00 30.08 ?  56  PRO A CA    1 
ATOM   429  C C     . PRO A 1 56  ? -36.064 16.417 19.308  1.00 34.92 ?  56  PRO A C     1 
ATOM   430  O O     . PRO A 1 56  ? -35.736 15.746 20.299  1.00 35.99 ?  56  PRO A O     1 
ATOM   431  C CB    . PRO A 1 56  ? -35.834 18.841 19.898  1.00 35.59 ?  56  PRO A CB    1 
ATOM   432  C CG    . PRO A 1 56  ? -36.244 19.940 18.952  1.00 33.97 ?  56  PRO A CG    1 
ATOM   433  C CD    . PRO A 1 56  ? -36.393 19.361 17.601  1.00 32.41 ?  56  PRO A CD    1 
ATOM   434  N N     . ASN A 1 57  ? -37.066 16.060 18.494  1.00 33.13 ?  57  ASN A N     1 
ATOM   435  C CA    . ASN A 1 57  ? -37.734 14.774 18.654  1.00 37.30 ?  57  ASN A CA    1 
ATOM   436  C C     . ASN A 1 57  ? -36.936 13.623 18.053  1.00 35.86 ?  57  ASN A C     1 
ATOM   437  O O     . ASN A 1 57  ? -37.251 12.461 18.337  1.00 31.43 ?  57  ASN A O     1 
ATOM   438  C CB    . ASN A 1 57  ? -39.139 14.822 18.032  1.00 37.64 ?  57  ASN A CB    1 
ATOM   439  C CG    . ASN A 1 57  ? -40.085 13.740 18.597  1.00 43.56 ?  57  ASN A CG    1 
ATOM   440  O OD1   . ASN A 1 57  ? -39.879 13.200 19.696  1.00 35.44 ?  57  ASN A OD1   1 
ATOM   441  N ND2   . ASN A 1 57  ? -41.132 13.428 17.835  1.00 42.36 ?  57  ASN A ND2   1 
ATOM   442  N N     . LEU A 1 58  ? -35.915 13.917 17.235  1.00 29.20 ?  58  LEU A N     1 
ATOM   443  C CA    . LEU A 1 58  ? -35.054 12.904 16.643  1.00 27.53 ?  58  LEU A CA    1 
ATOM   444  C C     . LEU A 1 58  ? -33.596 13.009 17.086  1.00 27.36 ?  58  LEU A C     1 
ATOM   445  O O     . LEU A 1 58  ? -32.904 11.986 17.131  1.00 25.32 ?  58  LEU A O     1 
ATOM   446  C CB    . LEU A 1 58  ? -35.152 12.968 15.104  1.00 27.09 ?  58  LEU A CB    1 
ATOM   447  C CG    . LEU A 1 58  ? -36.338 12.181 14.508  1.00 29.28 ?  58  LEU A CG    1 
ATOM   448  C CD1   . LEU A 1 58  ? -36.571 12.502 13.017  1.00 31.00 ?  58  LEU A CD1   1 
ATOM   449  C CD2   . LEU A 1 58  ? -36.150 10.673 14.703  1.00 26.21 ?  58  LEU A CD2   1 
ATOM   450  N N     . ILE A 1 59  ? -33.132 14.191 17.482  1.00 25.33 ?  59  ILE A N     1 
ATOM   451  C CA    . ILE A 1 59  ? -31.757 14.403 17.933  1.00 25.15 ?  59  ILE A CA    1 
ATOM   452  C C     . ILE A 1 59  ? -31.777 14.581 19.450  1.00 26.18 ?  59  ILE A C     1 
ATOM   453  O O     . ILE A 1 59  ? -32.318 15.572 19.957  1.00 28.15 ?  59  ILE A O     1 
ATOM   454  C CB    . ILE A 1 59  ? -31.118 15.622 17.243  1.00 23.39 ?  59  ILE A CB    1 
ATOM   455  C CG1   . ILE A 1 59  ? -31.231 15.517 15.725  1.00 23.81 ?  59  ILE A CG1   1 
ATOM   456  C CG2   . ILE A 1 59  ? -29.669 15.776 17.675  1.00 26.42 ?  59  ILE A CG2   1 
ATOM   457  C CD1   . ILE A 1 59  ? -30.672 16.694 14.983  1.00 27.12 ?  59  ILE A CD1   1 
ATOM   458  N N     . THR A 1 60  ? -31.180 13.643 20.185  1.00 27.45 ?  60  THR A N     1 
ATOM   459  C CA    . THR A 1 60  ? -31.126 13.711 21.644  1.00 28.60 ?  60  THR A CA    1 
ATOM   460  C C     . THR A 1 60  ? -29.681 13.841 22.109  1.00 30.60 ?  60  THR A C     1 
ATOM   461  O O     . THR A 1 60  ? -28.841 13.005 21.763  1.00 28.70 ?  60  THR A O     1 
ATOM   462  C CB    . THR A 1 60  ? -31.754 12.469 22.305  1.00 30.26 ?  60  THR A CB    1 
ATOM   463  O OG1   . THR A 1 60  ? -33.077 12.264 21.800  1.00 27.43 ?  60  THR A OG1   1 
ATOM   464  C CG2   . THR A 1 60  ? -31.824 12.655 23.824  1.00 27.65 ?  60  THR A CG2   1 
ATOM   465  N N     . PHE A 1 61  ? -29.404 14.876 22.909  1.00 29.91 ?  61  PHE A N     1 
ATOM   466  C CA    . PHE A 1 61  ? -28.095 15.043 23.541  1.00 28.03 ?  61  PHE A CA    1 
ATOM   467  C C     . PHE A 1 61  ? -27.954 14.120 24.755  1.00 32.15 ?  61  PHE A C     1 
ATOM   468  O O     . PHE A 1 61  ? -28.863 14.039 25.588  1.00 32.45 ?  61  PHE A O     1 
ATOM   469  C CB    . PHE A 1 61  ? -27.903 16.493 23.986  1.00 25.03 ?  61  PHE A CB    1 
ATOM   470  C CG    . PHE A 1 61  ? -27.784 17.488 22.856  1.00 32.19 ?  61  PHE A CG    1 
ATOM   471  C CD1   . PHE A 1 61  ? -26.662 17.493 22.013  1.00 27.38 ?  61  PHE A CD1   1 
ATOM   472  C CD2   . PHE A 1 61  ? -28.781 18.445 22.648  1.00 30.71 ?  61  PHE A CD2   1 
ATOM   473  C CE1   . PHE A 1 61  ? -26.551 18.436 20.984  1.00 26.53 ?  61  PHE A CE1   1 
ATOM   474  C CE2   . PHE A 1 61  ? -28.679 19.383 21.620  1.00 31.00 ?  61  PHE A CE2   1 
ATOM   475  C CZ    . PHE A 1 61  ? -27.562 19.380 20.786  1.00 26.53 ?  61  PHE A CZ    1 
ATOM   476  N N     . TYR A 1 62  ? -26.812 13.437 24.861  1.00 26.61 ?  62  TYR A N     1 
ATOM   477  C CA    . TYR A 1 62  ? -26.425 12.711 26.067  1.00 29.01 ?  62  TYR A CA    1 
ATOM   478  C C     . TYR A 1 62  ? -25.145 13.318 26.638  1.00 33.88 ?  62  TYR A C     1 
ATOM   479  O O     . TYR A 1 62  ? -24.092 13.280 25.979  1.00 29.50 ?  62  TYR A O     1 
ATOM   480  C CB    . TYR A 1 62  ? -26.261 11.211 25.770  1.00 28.61 ?  62  TYR A CB    1 
ATOM   481  C CG    . TYR A 1 62  ? -27.586 10.631 25.332  1.00 34.36 ?  62  TYR A CG    1 
ATOM   482  C CD1   . TYR A 1 62  ? -28.019 10.772 24.017  1.00 32.60 ?  62  TYR A CD1   1 
ATOM   483  C CD2   . TYR A 1 62  ? -28.445 10.009 26.244  1.00 31.04 ?  62  TYR A CD2   1 
ATOM   484  C CE1   . TYR A 1 62  ? -29.238 10.270 23.604  1.00 33.80 ?  62  TYR A CE1   1 
ATOM   485  C CE2   . TYR A 1 62  ? -29.670 9.504  25.838  1.00 28.53 ?  62  TYR A CE2   1 
ATOM   486  C CZ    . TYR A 1 62  ? -30.067 9.640  24.514  1.00 36.81 ?  62  TYR A CZ    1 
ATOM   487  O OH    . TYR A 1 62  ? -31.292 9.156  24.077  1.00 31.44 ?  62  TYR A OH    1 
ATOM   488  N N     . PRO A 1 63  ? -25.182 13.895 27.834  1.00 34.09 ?  63  PRO A N     1 
ATOM   489  C CA    . PRO A 1 63  ? -24.002 14.591 28.352  1.00 31.95 ?  63  PRO A CA    1 
ATOM   490  C C     . PRO A 1 63  ? -22.912 13.633 28.806  1.00 36.20 ?  63  PRO A C     1 
ATOM   491  O O     . PRO A 1 63  ? -23.167 12.490 29.193  1.00 36.34 ?  63  PRO A O     1 
ATOM   492  C CB    . PRO A 1 63  ? -24.562 15.398 29.528  1.00 35.09 ?  63  PRO A CB    1 
ATOM   493  C CG    . PRO A 1 63  ? -25.767 14.619 29.968  1.00 35.33 ?  63  PRO A CG    1 
ATOM   494  C CD    . PRO A 1 63  ? -26.343 14.008 28.738  1.00 34.59 ?  63  PRO A CD    1 
ATOM   495  N N     . LEU A 1 64  ? -21.669 14.115 28.721  1.00 33.55 ?  64  LEU A N     1 
ATOM   496  C CA    . LEU A 1 64  ? -20.491 13.418 29.209  1.00 29.91 ?  64  LEU A CA    1 
ATOM   497  C C     . LEU A 1 64  ? -19.815 14.282 30.266  1.00 32.80 ?  64  LEU A C     1 
ATOM   498  O O     . LEU A 1 64  ? -19.763 15.506 30.132  1.00 29.77 ?  64  LEU A O     1 
ATOM   499  C CB    . LEU A 1 64  ? -19.499 13.133 28.078  1.00 30.47 ?  64  LEU A CB    1 
ATOM   500  C CG    . LEU A 1 64  ? -19.935 12.236 26.919  1.00 34.35 ?  64  LEU A CG    1 
ATOM   501  C CD1   . LEU A 1 64  ? -18.813 12.143 25.904  1.00 29.76 ?  64  LEU A CD1   1 
ATOM   502  C CD2   . LEU A 1 64  ? -20.331 10.850 27.416  1.00 31.89 ?  64  LEU A CD2   1 
ATOM   503  N N     . ASN A 1 65  ? -19.293 13.654 31.315  1.00 33.70 ?  65  ASN A N     1 
ATOM   504  C CA    . ASN A 1 65  ? -18.475 14.366 32.294  1.00 34.90 ?  65  ASN A CA    1 
ATOM   505  C C     . ASN A 1 65  ? -17.019 14.270 31.860  1.00 31.00 ?  65  ASN A C     1 
ATOM   506  O O     . ASN A 1 65  ? -16.445 13.178 31.836  1.00 35.35 ?  65  ASN A O     1 
ATOM   507  C CB    . ASN A 1 65  ? -18.660 13.789 33.691  1.00 32.74 ?  65  ASN A CB    1 
ATOM   508  C CG    . ASN A 1 65  ? -20.078 13.877 34.161  1.00 35.25 ?  65  ASN A CG    1 
ATOM   509  O OD1   . ASN A 1 65  ? -20.681 14.952 34.172  1.00 35.26 ?  65  ASN A OD1   1 
ATOM   510  N ND2   . ASN A 1 65  ? -20.636 12.737 34.539  1.00 40.41 ?  65  ASN A ND2   1 
ATOM   511  N N     . VAL A 1 66  ? -16.426 15.408 31.511  1.00 32.04 ?  66  VAL A N     1 
ATOM   512  C CA    . VAL A 1 66  ? -15.036 15.425 31.061  1.00 31.92 ?  66  VAL A CA    1 
ATOM   513  C C     . VAL A 1 66  ? -14.144 15.208 32.279  1.00 34.13 ?  66  VAL A C     1 
ATOM   514  O O     . VAL A 1 66  ? -13.980 16.118 33.102  1.00 30.76 ?  66  VAL A O     1 
ATOM   515  C CB    . VAL A 1 66  ? -14.698 16.725 30.313  1.00 34.80 ?  66  VAL A CB    1 
ATOM   516  C CG1   . VAL A 1 66  ? -13.212 16.785 29.987  1.00 29.03 ?  66  VAL A CG1   1 
ATOM   517  C CG2   . VAL A 1 66  ? -15.536 16.830 29.018  1.00 30.65 ?  66  VAL A CG2   1 
ATOM   518  N N     . PRO A 1 67  ? -13.548 14.027 32.420  1.00 33.25 ?  67  PRO A N     1 
ATOM   519  C CA    . PRO A 1 67  ? -12.830 13.701 33.656  1.00 38.03 ?  67  PRO A CA    1 
ATOM   520  C C     . PRO A 1 67  ? -11.590 14.555 33.848  1.00 41.46 ?  67  PRO A C     1 
ATOM   521  O O     . PRO A 1 67  ? -10.922 14.960 32.892  1.00 37.27 ?  67  PRO A O     1 
ATOM   522  C CB    . PRO A 1 67  ? -12.446 12.226 33.480  1.00 36.44 ?  67  PRO A CB    1 
ATOM   523  C CG    . PRO A 1 67  ? -12.843 11.841 32.099  1.00 38.48 ?  67  PRO A CG    1 
ATOM   524  C CD    . PRO A 1 67  ? -13.335 13.035 31.357  1.00 34.42 ?  67  PRO A CD    1 
ATOM   525  N N     . HIS A 1 68  ? -11.277 14.799 35.114  1.00 38.34 ?  68  HIS A N     1 
ATOM   526  C CA    . HIS A 1 68  ? -10.044 15.482 35.460  1.00 37.53 ?  68  HIS A CA    1 
ATOM   527  C C     . HIS A 1 68  ? -8.834  14.681 34.992  1.00 37.93 ?  68  HIS A C     1 
ATOM   528  O O     . HIS A 1 68  ? -8.779  13.456 35.130  1.00 37.37 ?  68  HIS A O     1 
ATOM   529  C CB    . HIS A 1 68  ? -9.970  15.702 36.969  1.00 39.42 ?  68  HIS A CB    1 
ATOM   530  C CG    . HIS A 1 68  ? -8.578  15.910 37.476  1.00 40.68 ?  68  HIS A CG    1 
ATOM   531  N ND1   . HIS A 1 68  ? -7.915  17.115 37.357  1.00 43.28 ?  68  HIS A ND1   1 
ATOM   532  C CD2   . HIS A 1 68  ? -7.708  15.060 38.075  1.00 40.79 ?  68  HIS A CD2   1 
ATOM   533  C CE1   . HIS A 1 68  ? -6.704  17.002 37.877  1.00 42.62 ?  68  HIS A CE1   1 
ATOM   534  N NE2   . HIS A 1 68  ? -6.554  15.766 38.321  1.00 39.68 ?  68  HIS A NE2   1 
ATOM   535  N N     . VAL A 1 69  ? -7.871  15.387 34.417  1.00 35.19 ?  69  VAL A N     1 
ATOM   536  C CA    . VAL A 1 69  ? -6.544  14.865 34.129  1.00 35.18 ?  69  VAL A CA    1 
ATOM   537  C C     . VAL A 1 69  ? -5.559  15.889 34.671  1.00 35.65 ?  69  VAL A C     1 
ATOM   538  O O     . VAL A 1 69  ? -5.807  17.095 34.576  1.00 34.99 ?  69  VAL A O     1 
ATOM   539  C CB    . VAL A 1 69  ? -6.343  14.617 32.612  1.00 35.64 ?  69  VAL A CB    1 
ATOM   540  C CG1   . VAL A 1 69  ? -4.929  14.184 32.313  1.00 28.02 ?  69  VAL A CG1   1 
ATOM   541  C CG2   . VAL A 1 69  ? -7.342  13.559 32.094  1.00 34.36 ?  69  VAL A CG2   1 
ATOM   542  N N     . ASP A 1 70  ? -4.484  15.416 35.303  1.00 32.82 ?  70  ASP A N     1 
ATOM   543  C CA    . ASP A 1 70  ? -3.534  16.333 35.925  1.00 39.95 ?  70  ASP A CA    1 
ATOM   544  C C     . ASP A 1 70  ? -3.022  17.321 34.894  1.00 39.15 ?  70  ASP A C     1 
ATOM   545  O O     . ASP A 1 70  ? -2.499  16.928 33.848  1.00 37.67 ?  70  ASP A O     1 
ATOM   546  C CB    . ASP A 1 70  ? -2.356  15.572 36.546  1.00 41.35 ?  70  ASP A CB    1 
ATOM   547  C CG    . ASP A 1 70  ? -1.436  16.475 37.379  1.00 37.43 ?  70  ASP A CG    1 
ATOM   548  O OD1   . ASP A 1 70  ? -1.869  17.564 37.831  1.00 41.44 ?  70  ASP A OD1   1 
ATOM   549  O OD2   . ASP A 1 70  ? -0.271  16.083 37.607  1.00 42.08 -1 70  ASP A OD2   1 
ATOM   550  N N     . GLY A 1 71  ? -3.169  18.606 35.195  1.00 33.74 ?  71  GLY A N     1 
ATOM   551  C CA    . GLY A 1 71  ? -2.754  19.654 34.297  1.00 33.70 ?  71  GLY A CA    1 
ATOM   552  C C     . GLY A 1 71  ? -3.888  20.299 33.540  1.00 35.00 ?  71  GLY A C     1 
ATOM   553  O O     . GLY A 1 71  ? -3.684  21.353 32.931  1.00 33.54 ?  71  GLY A O     1 
ATOM   554  N N     . LEU A 1 72  ? -5.065  19.710 33.569  1.00 32.56 ?  72  LEU A N     1 
ATOM   555  C CA    . LEU A 1 72  ? -6.217  20.230 32.852  1.00 30.90 ?  72  LEU A CA    1 
ATOM   556  C C     . LEU A 1 72  ? -6.949  21.242 33.722  1.00 36.94 ?  72  LEU A C     1 
ATOM   557  O O     . LEU A 1 72  ? -7.279  20.929 34.875  1.00 37.29 ?  72  LEU A O     1 
ATOM   558  C CB    . LEU A 1 72  ? -7.162  19.094 32.466  1.00 34.09 ?  72  LEU A CB    1 
ATOM   559  C CG    . LEU A 1 72  ? -8.402  19.482 31.663  1.00 33.53 ?  72  LEU A CG    1 
ATOM   560  C CD1   . LEU A 1 72  ? -8.023  19.616 30.208  1.00 30.58 ?  72  LEU A CD1   1 
ATOM   561  C CD2   . LEU A 1 72  ? -9.549  18.459 31.851  1.00 40.13 ?  72  LEU A CD2   1 
ATOM   562  N N     . PRO A 1 73  ? -7.209  22.453 33.222  1.00 34.63 ?  73  PRO A N     1 
ATOM   563  C CA    . PRO A 1 73  ? -7.916  23.446 34.042  1.00 37.55 ?  73  PRO A CA    1 
ATOM   564  C C     . PRO A 1 73  ? -9.263  22.923 34.518  1.00 40.32 ?  73  PRO A C     1 
ATOM   565  O O     . PRO A 1 73  ? -9.935  22.146 33.833  1.00 39.08 ?  73  PRO A O     1 
ATOM   566  C CB    . PRO A 1 73  ? -8.084  24.654 33.106  1.00 34.27 ?  73  PRO A CB    1 
ATOM   567  C CG    . PRO A 1 73  ? -7.272  24.366 31.883  1.00 34.24 ?  73  PRO A CG    1 
ATOM   568  C CD    . PRO A 1 73  ? -6.587  23.041 32.023  1.00 35.17 ?  73  PRO A CD    1 
ATOM   569  N N     . PHE A 1 74  ? -9.646  23.361 35.718  1.00 36.11 ?  74  PHE A N     1 
ATOM   570  C CA    . PHE A 1 74  ? -10.888 22.914 36.328  1.00 30.94 ?  74  PHE A CA    1 
ATOM   571  C C     . PHE A 1 74  ? -12.081 23.276 35.452  1.00 33.58 ?  74  PHE A C     1 
ATOM   572  O O     . PHE A 1 74  ? -12.225 24.423 35.019  1.00 32.10 ?  74  PHE A O     1 
ATOM   573  C CB    . PHE A 1 74  ? -11.047 23.538 37.722  1.00 32.84 ?  74  PHE A CB    1 
ATOM   574  C CG    . PHE A 1 74  ? -12.432 23.363 38.307  1.00 33.26 ?  74  PHE A CG    1 
ATOM   575  C CD1   . PHE A 1 74  ? -12.762 22.217 39.014  1.00 36.62 ?  74  PHE A CD1   1 
ATOM   576  C CD2   . PHE A 1 74  ? -13.402 24.327 38.125  1.00 28.17 ?  74  PHE A CD2   1 
ATOM   577  C CE1   . PHE A 1 74  ? -14.039 22.043 39.547  1.00 31.05 ?  74  PHE A CE1   1 
ATOM   578  C CE2   . PHE A 1 74  ? -14.694 24.155 38.635  1.00 38.22 ?  74  PHE A CE2   1 
ATOM   579  C CZ    . PHE A 1 74  ? -15.006 23.012 39.353  1.00 33.46 ?  74  PHE A CZ    1 
ATOM   580  N N     . GLY A 1 75  ? -12.953 22.292 35.219  1.00 34.74 ?  75  GLY A N     1 
ATOM   581  C CA    . GLY A 1 75  ? -14.165 22.476 34.451  1.00 30.90 ?  75  GLY A CA    1 
ATOM   582  C C     . GLY A 1 75  ? -13.991 22.536 32.946  1.00 27.44 ?  75  GLY A C     1 
ATOM   583  O O     . GLY A 1 75  ? -14.984 22.719 32.239  1.00 29.68 ?  75  GLY A O     1 
ATOM   584  N N     . ALA A 1 76  ? -12.770 22.378 32.434  1.00 33.31 ?  76  ALA A N     1 
ATOM   585  C CA    . ALA A 1 76  ? -12.518 22.567 31.009  1.00 31.10 ?  76  ALA A CA    1 
ATOM   586  C C     . ALA A 1 76  ? -13.159 21.444 30.210  1.00 28.81 ?  76  ALA A C     1 
ATOM   587  O O     . ALA A 1 76  ? -13.053 20.267 30.574  1.00 28.37 ?  76  ALA A O     1 
ATOM   588  C CB    . ALA A 1 76  ? -11.018 22.622 30.735  1.00 30.29 ?  76  ALA A CB    1 
ATOM   589  N N     . GLU A 1 77  ? -13.841 21.806 29.128  1.00 30.78 ?  77  GLU A N     1 
ATOM   590  C CA    . GLU A 1 77  ? -14.549 20.802 28.333  1.00 29.18 ?  77  GLU A CA    1 
ATOM   591  C C     . GLU A 1 77  ? -14.092 20.740 26.886  1.00 27.20 ?  77  GLU A C     1 
ATOM   592  O O     . GLU A 1 77  ? -13.997 19.644 26.340  1.00 29.32 ?  77  GLU A O     1 
ATOM   593  C CB    . GLU A 1 77  ? -16.066 21.047 28.403  1.00 26.22 ?  77  GLU A CB    1 
ATOM   594  C CG    . GLU A 1 77  ? -16.640 20.692 29.792  1.00 31.19 ?  77  GLU A CG    1 
ATOM   595  C CD    . GLU A 1 77  ? -18.166 20.600 29.844  1.00 32.82 ?  77  GLU A CD    1 
ATOM   596  O OE1   . GLU A 1 77  ? -18.847 20.994 28.870  1.00 31.65 ?  77  GLU A OE1   1 
ATOM   597  O OE2   . GLU A 1 77  ? -18.681 20.135 30.885  1.00 35.69 -1 77  GLU A OE2   1 
ATOM   598  N N     . THR A 1 78  ? -13.762 21.873 26.259  1.00 25.57 ?  78  THR A N     1 
ATOM   599  C CA    . THR A 1 78  ? -13.406 21.903 24.844  1.00 28.57 ?  78  THR A CA    1 
ATOM   600  C C     . THR A 1 78  ? -12.126 22.703 24.632  1.00 26.10 ?  78  THR A C     1 
ATOM   601  O O     . THR A 1 78  ? -11.648 23.398 25.531  1.00 21.18 ?  78  THR A O     1 
ATOM   602  C CB    . THR A 1 78  ? -14.517 22.514 23.984  1.00 24.75 ?  78  THR A CB    1 
ATOM   603  O OG1   . THR A 1 78  ? -14.492 23.931 24.150  1.00 26.87 ?  78  THR A OG1   1 
ATOM   604  C CG2   . THR A 1 78  ? -15.899 21.964 24.358  1.00 24.11 ?  78  THR A CG2   1 
ATOM   605  N N     . THR A 1 79  ? -11.587 22.630 23.407  1.00 22.47 ?  79  THR A N     1 
ATOM   606  C CA    . THR A 1 79  ? -10.378 23.390 23.102  1.00 22.36 ?  79  THR A CA    1 
ATOM   607  C C     . THR A 1 79  ? -10.592 24.892 23.199  1.00 26.90 ?  79  THR A C     1 
ATOM   608  O O     . THR A 1 79  ? -9.612  25.638 23.119  1.00 28.42 ?  79  THR A O     1 
ATOM   609  C CB    . THR A 1 79  ? -9.840  23.082 21.692  1.00 23.73 ?  79  THR A CB    1 
ATOM   610  O OG1   . THR A 1 79  ? -10.876 23.318 20.722  1.00 23.71 ?  79  THR A OG1   1 
ATOM   611  C CG2   . THR A 1 79  ? -9.312  21.641 21.582  1.00 21.93 ?  79  THR A CG2   1 
ATOM   612  N N     . SER A 1 80  ? -11.832 25.364 23.311  1.00 25.32 ?  80  SER A N     1 
ATOM   613  C CA    . SER A 1 80  ? -12.029 26.787 23.567  1.00 31.18 ?  80  SER A CA    1 
ATOM   614  C C     . SER A 1 80  ? -11.731 27.152 25.017  1.00 34.28 ?  80  SER A C     1 
ATOM   615  O O     . SER A 1 80  ? -11.589 28.342 25.318  1.00 33.24 ?  80  SER A O     1 
ATOM   616  C CB    . SER A 1 80  ? -13.463 27.213 23.215  1.00 30.26 ?  80  SER A CB    1 
ATOM   617  O OG    . SER A 1 80  ? -13.743 27.044 21.834  1.00 32.20 ?  80  SER A OG    1 
ATOM   618  N N     . ASP A 1 81  ? -11.613 26.157 25.905  1.00 34.33 ?  81  ASP A N     1 
ATOM   619  C CA    . ASP A 1 81  ? -11.379 26.361 27.330  1.00 31.52 ?  81  ASP A CA    1 
ATOM   620  C C     . ASP A 1 81  ? -9.919  26.216 27.740  1.00 35.06 ?  81  ASP A C     1 
ATOM   621  O O     . ASP A 1 81  ? -9.611  26.390 28.921  1.00 33.96 ?  81  ASP A O     1 
ATOM   622  C CB    . ASP A 1 81  ? -12.187 25.355 28.156  1.00 30.31 ?  81  ASP A CB    1 
ATOM   623  C CG    . ASP A 1 81  ? -13.693 25.448 27.917  1.00 35.81 ?  81  ASP A CG    1 
ATOM   624  O OD1   . ASP A 1 81  ? -14.171 26.504 27.450  1.00 33.56 ?  81  ASP A OD1   1 
ATOM   625  O OD2   . ASP A 1 81  ? -14.395 24.446 28.203  1.00 32.61 -1 81  ASP A OD2   1 
ATOM   626  N N     . VAL A 1 82  ? -9.029  25.825 26.834  1.00 32.50 ?  82  VAL A N     1 
ATOM   627  C CA    . VAL A 1 82  ? -7.632  25.587 27.180  1.00 31.10 ?  82  VAL A CA    1 
ATOM   628  C C     . VAL A 1 82  ? -6.761  26.072 26.035  1.00 35.81 ?  82  VAL A C     1 
ATOM   629  O O     . VAL A 1 82  ? -7.193  26.110 24.875  1.00 32.08 ?  82  VAL A O     1 
ATOM   630  C CB    . VAL A 1 82  ? -7.318  24.097 27.483  1.00 33.17 ?  82  VAL A CB    1 
ATOM   631  C CG1   . VAL A 1 82  ? -8.235  23.557 28.573  1.00 32.62 ?  82  VAL A CG1   1 
ATOM   632  C CG2   . VAL A 1 82  ? -7.414  23.245 26.217  1.00 26.12 ?  82  VAL A CG2   1 
ATOM   633  N N     . ALA A 1 83  ? -5.531  26.458 26.379  1.00 30.61 ?  83  ALA A N     1 
ATOM   634  C CA    . ALA A 1 83  ? -4.542  26.851 25.393  1.00 27.02 ?  83  ALA A CA    1 
ATOM   635  C C     . ALA A 1 83  ? -4.159  25.653 24.535  1.00 31.34 ?  83  ALA A C     1 
ATOM   636  O O     . ALA A 1 83  ? -4.362  24.495 24.915  1.00 26.13 ?  83  ALA A O     1 
ATOM   637  C CB    . ALA A 1 83  ? -3.296  27.425 26.073  1.00 33.86 ?  83  ALA A CB    1 
ATOM   638  N N     . ILE A 1 84  ? -3.585  25.949 23.364  1.00 27.41 ?  84  ILE A N     1 
ATOM   639  C CA    . ILE A 1 84  ? -3.329  24.914 22.365  1.00 28.15 ?  84  ILE A CA    1 
ATOM   640  C C     . ILE A 1 84  ? -2.305  23.915 22.878  1.00 32.03 ?  84  ILE A C     1 
ATOM   641  O O     . ILE A 1 84  ? -2.348  22.728 22.521  1.00 31.60 ?  84  ILE A O     1 
ATOM   642  C CB    . ILE A 1 84  ? -2.899  25.566 21.027  1.00 28.79 ?  84  ILE A CB    1 
ATOM   643  C CG1   . ILE A 1 84  ? -2.464  24.530 19.983  1.00 23.16 ?  84  ILE A CG1   1 
ATOM   644  C CG2   . ILE A 1 84  ? -1.799  26.600 21.247  1.00 36.57 ?  84  ILE A CG2   1 
ATOM   645  C CD1   . ILE A 1 84  ? -3.620  23.733 19.353  1.00 34.78 ?  84  ILE A CD1   1 
ATOM   646  N N     . SER A 1 85  ? -1.376  24.363 23.731  1.00 27.39 ?  85  SER A N     1 
ATOM   647  C CA    . SER A 1 85  ? -0.426  23.431 24.331  1.00 28.84 ?  85  SER A CA    1 
ATOM   648  C C     . SER A 1 85  ? -1.089  22.415 25.269  1.00 25.57 ?  85  SER A C     1 
ATOM   649  O O     . SER A 1 85  ? -0.478  21.389 25.577  1.00 30.56 ?  85  SER A O     1 
ATOM   650  C CB    . SER A 1 85  ? 0.656   24.201 25.091  1.00 29.18 ?  85  SER A CB    1 
ATOM   651  O OG    . SER A 1 85  ? 0.071   24.889 26.177  1.00 28.11 ?  85  SER A OG    1 
ATOM   652  N N     . LEU A 1 86  ? -2.310  22.661 25.724  1.00 22.95 ?  86  LEU A N     1 
ATOM   653  C CA    . LEU A 1 86  ? -2.994  21.732 26.616  1.00 26.74 ?  86  LEU A CA    1 
ATOM   654  C C     . LEU A 1 86  ? -3.933  20.766 25.887  1.00 28.33 ?  86  LEU A C     1 
ATOM   655  O O     . LEU A 1 86  ? -4.546  19.911 26.537  1.00 27.28 ?  86  LEU A O     1 
ATOM   656  C CB    . LEU A 1 86  ? -3.755  22.511 27.697  1.00 23.77 ?  86  LEU A CB    1 
ATOM   657  C CG    . LEU A 1 86  ? -2.843  23.362 28.615  1.00 31.87 ?  86  LEU A CG    1 
ATOM   658  C CD1   . LEU A 1 86  ? -3.609  24.010 29.762  1.00 27.76 ?  86  LEU A CD1   1 
ATOM   659  C CD2   . LEU A 1 86  ? -1.650  22.558 29.154  1.00 27.90 ?  86  LEU A CD2   1 
ATOM   660  N N     . GLY A 1 87  ? -4.049  20.863 24.555  1.00 28.64 ?  87  GLY A N     1 
ATOM   661  C CA    . GLY A 1 87  ? -4.830  19.910 23.797  1.00 26.12 ?  87  GLY A CA    1 
ATOM   662  C C     . GLY A 1 87  ? -4.544  18.442 24.075  1.00 25.88 ?  87  GLY A C     1 
ATOM   663  O O     . GLY A 1 87  ? -5.484  17.650 24.180  1.00 24.06 ?  87  GLY A O     1 
ATOM   664  N N     . PRO A 1 88  ? -3.274  18.036 24.174  1.00 24.37 ?  88  PRO A N     1 
ATOM   665  C CA    . PRO A 1 88  ? -3.011  16.617 24.481  1.00 27.86 ?  88  PRO A CA    1 
ATOM   666  C C     . PRO A 1 88  ? -3.605  16.152 25.811  1.00 29.47 ?  88  PRO A C     1 
ATOM   667  O O     . PRO A 1 88  ? -3.991  14.981 25.928  1.00 29.95 ?  88  PRO A O     1 
ATOM   668  C CB    . PRO A 1 88  ? -1.477  16.528 24.476  1.00 27.10 ?  88  PRO A CB    1 
ATOM   669  C CG    . PRO A 1 88  ? -0.986  17.752 23.763  1.00 28.42 ?  88  PRO A CG    1 
ATOM   670  C CD    . PRO A 1 88  ? -2.118  18.696 23.535  1.00 28.50 ?  88  PRO A CD    1 
ATOM   671  N N     . ILE A 1 89  ? -3.706  17.031 26.808  1.00 23.78 ?  89  ILE A N     1 
ATOM   672  C CA    . ILE A 1 89  ? -4.275  16.629 28.085  1.00 23.95 ?  89  ILE A CA    1 
ATOM   673  C C     . ILE A 1 89  ? -5.785  16.457 27.962  1.00 27.39 ?  89  ILE A C     1 
ATOM   674  O O     . ILE A 1 89  ? -6.364  15.495 28.485  1.00 23.56 ?  89  ILE A O     1 
ATOM   675  C CB    . ILE A 1 89  ? -3.889  17.648 29.169  1.00 26.99 ?  89  ILE A CB    1 
ATOM   676  C CG1   . ILE A 1 89  ? -2.394  17.575 29.445  1.00 28.85 ?  89  ILE A CG1   1 
ATOM   677  C CG2   . ILE A 1 89  ? -4.644  17.385 30.465  1.00 31.63 ?  89  ILE A CG2   1 
ATOM   678  C CD1   . ILE A 1 89  ? -1.972  18.489 30.582  1.00 34.46 ?  89  ILE A CD1   1 
ATOM   679  N N     . LEU A 1 90  ? -6.442  17.375 27.253  1.00 23.44 ?  90  LEU A N     1 
ATOM   680  C CA    . LEU A 1 90  ? -7.864  17.217 26.971  1.00 24.19 ?  90  LEU A CA    1 
ATOM   681  C C     . LEU A 1 90  ? -8.130  15.914 26.211  1.00 25.34 ?  90  LEU A C     1 
ATOM   682  O O     . LEU A 1 90  ? -9.144  15.244 26.452  1.00 25.30 ?  90  LEU A O     1 
ATOM   683  C CB    . LEU A 1 90  ? -8.371  18.439 26.199  1.00 27.62 ?  90  LEU A CB    1 
ATOM   684  C CG    . LEU A 1 90  ? -9.863  18.589 25.929  1.00 24.78 ?  90  LEU A CG    1 
ATOM   685  C CD1   . LEU A 1 90  ? -10.647 18.845 27.231  1.00 25.78 ?  90  LEU A CD1   1 
ATOM   686  C CD2   . LEU A 1 90  ? -10.042 19.699 24.907  1.00 22.15 ?  90  LEU A CD2   1 
ATOM   687  N N     . MET A 1 91  ? -7.210  15.515 25.322  1.00 21.52 ?  91  MET A N     1 
ATOM   688  C CA    . MET A 1 91  ? -7.343  14.226 24.644  1.00 24.80 ?  91  MET A CA    1 
ATOM   689  C C     . MET A 1 91  ? -7.266  13.073 25.644  1.00 26.20 ?  91  MET A C     1 
ATOM   690  O O     . MET A 1 91  ? -8.074  12.140 25.587  1.00 26.99 ?  91  MET A O     1 
ATOM   691  C CB    . MET A 1 91  ? -6.276  14.071 23.553  1.00 21.33 ?  91  MET A CB    1 
ATOM   692  C CG    . MET A 1 91  ? -6.446  12.826 22.662  1.00 22.27 ?  91  MET A CG    1 
ATOM   693  S SD    . MET A 1 91  ? -8.048  12.722 21.798  1.00 24.56 ?  91  MET A SD    1 
ATOM   694  C CE    . MET A 1 91  ? -8.623  11.080 22.282  1.00 22.98 ?  91  MET A CE    1 
ATOM   695  N N     . THR A 1 92  ? -6.304  13.125 26.581  1.00 26.08 ?  92  THR A N     1 
ATOM   696  C CA    . THR A 1 92  ? -6.267  12.117 27.643  1.00 26.59 ?  92  THR A CA    1 
ATOM   697  C C     . THR A 1 92  ? -7.616  12.049 28.356  1.00 27.70 ?  92  THR A C     1 
ATOM   698  O O     . THR A 1 92  ? -8.145  10.959 28.596  1.00 27.31 ?  92  THR A O     1 
ATOM   699  C CB    . THR A 1 92  ? -5.140  12.408 28.642  1.00 29.87 ?  92  THR A CB    1 
ATOM   700  O OG1   . THR A 1 92  ? -3.872  12.380 27.977  1.00 26.26 ?  92  THR A OG1   1 
ATOM   701  C CG2   . THR A 1 92  ? -5.129  11.372 29.760  1.00 27.76 ?  92  THR A CG2   1 
ATOM   702  N N     . ALA A 1 93  ? -8.214  13.211 28.637  1.00 24.17 ?  93  ALA A N     1 
ATOM   703  C CA    . ALA A 1 93  ? -9.559  13.246 29.206  1.00 25.97 ?  93  ALA A CA    1 
ATOM   704  C C     . ALA A 1 93  ? -10.579 12.550 28.306  1.00 30.30 ?  93  ALA A C     1 
ATOM   705  O O     . ALA A 1 93  ? -11.442 11.809 28.794  1.00 29.32 ?  93  ALA A O     1 
ATOM   706  C CB    . ALA A 1 93  ? -9.983  14.688 29.470  1.00 25.51 ?  93  ALA A CB    1 
ATOM   707  N N     . MET A 1 94  ? -10.523 12.785 26.995  1.00 26.68 ?  94  MET A N     1 
ATOM   708  C CA    . MET A 1 94  ? -11.522 12.150 26.149  1.00 28.92 ?  94  MET A CA    1 
ATOM   709  C C     . MET A 1 94  ? -11.312 10.638 26.107  1.00 28.45 ?  94  MET A C     1 
ATOM   710  O O     . MET A 1 94  ? -12.284 9.871  26.110  1.00 32.10 ?  94  MET A O     1 
ATOM   711  C CB    . MET A 1 94  ? -11.528 12.780 24.747  1.00 26.74 ?  94  MET A CB    1 
ATOM   712  C CG    . MET A 1 94  ? -12.449 12.081 23.751  1.00 23.83 ?  94  MET A CG    1 
ATOM   713  S SD    . MET A 1 94  ? -12.301 12.666 22.041  1.00 25.50 ?  94  MET A SD    1 
ATOM   714  C CE    . MET A 1 94  ? -13.971 12.278 21.430  1.00 20.68 ?  94  MET A CE    1 
ATOM   715  N N     . ASP A 1 95  ? -10.063 10.184 26.111  1.00 25.34 ?  95  ASP A N     1 
ATOM   716  C CA    . ASP A 1 95  ? -9.815  8.754  26.285  1.00 31.32 ?  95  ASP A CA    1 
ATOM   717  C C     . ASP A 1 95  ? -10.496 8.227  27.552  1.00 33.09 ?  95  ASP A C     1 
ATOM   718  O O     . ASP A 1 95  ? -11.070 7.132  27.552  1.00 32.34 ?  95  ASP A O     1 
ATOM   719  C CB    . ASP A 1 95  ? -8.316  8.484  26.331  1.00 25.30 ?  95  ASP A CB    1 
ATOM   720  C CG    . ASP A 1 95  ? -7.693  8.363  24.949  1.00 31.49 ?  95  ASP A CG    1 
ATOM   721  O OD1   . ASP A 1 95  ? -8.420  8.139  23.954  1.00 33.06 ?  95  ASP A OD1   1 
ATOM   722  O OD2   . ASP A 1 95  ? -6.459  8.485  24.856  1.00 29.46 -1 95  ASP A OD2   1 
ATOM   723  N N     . GLN A 1 96  ? -10.487 9.017  28.621  1.00 27.74 ?  96  GLN A N     1 
ATOM   724  C CA    . GLN A 1 96  ? -11.004 8.599  29.920  1.00 31.32 ?  96  GLN A CA    1 
ATOM   725  C C     . GLN A 1 96  ? -12.531 8.582  30.007  1.00 37.55 ?  96  GLN A C     1 
ATOM   726  O O     . GLN A 1 96  ? -13.071 8.174  31.044  1.00 34.45 ?  96  GLN A O     1 
ATOM   727  C CB    . GLN A 1 96  ? -10.442 9.508  31.010  1.00 31.68 ?  96  GLN A CB    1 
ATOM   728  C CG    . GLN A 1 96  ? -8.992  9.225  31.332  1.00 29.47 ?  96  GLN A CG    1 
ATOM   729  C CD    . GLN A 1 96  ? -8.795  7.786  31.762  1.00 44.96 ?  96  GLN A CD    1 
ATOM   730  O OE1   . GLN A 1 96  ? -7.969  7.064  31.190  1.00 43.60 ?  96  GLN A OE1   1 
ATOM   731  N NE2   . GLN A 1 96  ? -9.597  7.337  32.731  1.00 42.42 ?  96  GLN A NE2   1 
ATOM   732  N N     . THR A 1 97  ? -13.243 9.026  28.974  1.00 31.35 ?  97  THR A N     1 
ATOM   733  C CA    . THR A 1 97  ? -14.685 8.850  28.939  1.00 30.11 ?  97  THR A CA    1 
ATOM   734  C C     . THR A 1 97  ? -15.079 7.447  28.514  1.00 31.49 ?  97  THR A C     1 
ATOM   735  O O     . THR A 1 97  ? -16.271 7.183  28.342  1.00 29.27 ?  97  THR A O     1 
ATOM   736  C CB    . THR A 1 97  ? -15.333 9.862  27.989  1.00 32.24 ?  97  THR A CB    1 
ATOM   737  O OG1   . THR A 1 97  ? -14.905 9.575  26.659  1.00 30.11 ?  97  THR A OG1   1 
ATOM   738  C CG2   . THR A 1 97  ? -14.944 11.306 28.351  1.00 28.21 ?  97  THR A CG2   1 
ATOM   739  N N     . GLN A 1 98  ? -14.112 6.549  28.327  1.00 30.14 ?  98  GLN A N     1 
ATOM   740  C CA    . GLN A 1 98  ? -14.435 5.225  27.807  1.00 37.83 ?  98  GLN A CA    1 
ATOM   741  C C     . GLN A 1 98  ? -15.542 4.553  28.620  1.00 39.26 ?  98  GLN A C     1 
ATOM   742  O O     . GLN A 1 98  ? -16.502 4.027  28.052  1.00 38.13 ?  98  GLN A O     1 
ATOM   743  C CB    . GLN A 1 98  ? -13.186 4.349  27.763  1.00 32.90 ?  98  GLN A CB    1 
ATOM   744  C CG    . GLN A 1 98  ? -13.410 3.087  26.951  1.00 35.37 ?  98  GLN A CG    1 
ATOM   745  C CD    . GLN A 1 98  ? -12.236 2.146  26.976  1.00 38.35 ?  98  GLN A CD    1 
ATOM   746  O OE1   . GLN A 1 98  ? -11.089 2.558  26.815  1.00 40.13 ?  98  GLN A OE1   1 
ATOM   747  N NE2   . GLN A 1 98  ? -12.516 0.864  27.135  1.00 46.47 ?  98  GLN A NE2   1 
ATOM   748  N N     . ASN A 1 99  ? -15.457 4.617  29.953  1.00 40.89 ?  99  ASN A N     1 
ATOM   749  C CA    . ASN A 1 99  ? -16.444 3.946  30.798  1.00 40.61 ?  99  ASN A CA    1 
ATOM   750  C C     . ASN A 1 99  ? -17.845 4.499  30.578  1.00 38.91 ?  99  ASN A C     1 
ATOM   751  O O     . ASN A 1 99  ? -18.808 3.736  30.458  1.00 40.59 ?  99  ASN A O     1 
ATOM   752  C CB    . ASN A 1 99  ? -16.050 4.056  32.273  1.00 42.57 ?  99  ASN A CB    1 
ATOM   753  C CG    . ASN A 1 99  ? -14.960 3.073  32.659  1.00 47.94 ?  99  ASN A CG    1 
ATOM   754  O OD1   . ASN A 1 99  ? -14.808 2.021  32.035  1.00 54.91 ?  99  ASN A OD1   1 
ATOM   755  N ND2   . ASN A 1 99  ? -14.184 3.418  33.683  1.00 48.87 ?  99  ASN A ND2   1 
ATOM   756  N N     . GLN A 1 100 ? -18.001 5.825  30.545  1.00 37.96 ?  100 GLN A N     1 
ATOM   757  C CA    . GLN A 1 100 ? -19.345 6.311  30.267  1.00 35.13 ?  100 GLN A CA    1 
ATOM   758  C C     . GLN A 1 100 ? -19.754 6.092  28.810  1.00 34.05 ?  100 GLN A C     1 
ATOM   759  O O     . GLN A 1 100 ? -20.957 6.066  28.517  1.00 34.02 ?  100 GLN A O     1 
ATOM   760  C CB    . GLN A 1 100 ? -19.512 7.784  30.666  1.00 35.23 ?  100 GLN A CB    1 
ATOM   761  C CG    . GLN A 1 100 ? -18.290 8.630  30.675  1.00 39.19 ?  100 GLN A CG    1 
ATOM   762  C CD    . GLN A 1 100 ? -18.497 9.964  31.396  1.00 35.96 ?  100 GLN A CD    1 
ATOM   763  O OE1   . GLN A 1 100 ? -19.616 10.461 31.514  1.00 36.13 ?  100 GLN A OE1   1 
ATOM   764  N NE2   . GLN A 1 100 ? -17.406 10.547 31.873  1.00 37.28 ?  100 GLN A NE2   1 
ATOM   765  N N     . ILE A 1 101 ? -18.801 5.887  27.900  1.00 31.81 ?  101 ILE A N     1 
ATOM   766  C CA    . ILE A 1 101 ? -19.162 5.618  26.509  1.00 34.52 ?  101 ILE A CA    1 
ATOM   767  C C     . ILE A 1 101 ? -19.701 4.195  26.359  1.00 37.67 ?  101 ILE A C     1 
ATOM   768  O O     . ILE A 1 101 ? -20.717 3.973  25.686  1.00 33.57 ?  101 ILE A O     1 
ATOM   769  C CB    . ILE A 1 101 ? -17.965 5.866  25.565  1.00 33.87 ?  101 ILE A CB    1 
ATOM   770  C CG1   . ILE A 1 101 ? -17.680 7.371  25.383  1.00 30.05 ?  101 ILE A CG1   1 
ATOM   771  C CG2   . ILE A 1 101 ? -18.219 5.205  24.209  1.00 28.16 ?  101 ILE A CG2   1 
ATOM   772  C CD1   . ILE A 1 101 ? -18.874 8.203  24.937  1.00 28.81 ?  101 ILE A CD1   1 
ATOM   773  N N     . GLU A 1 102 ? -19.025 3.204  26.972  1.00 38.35 ?  102 GLU A N     1 
ATOM   774  C CA    . GLU A 1 102 ? -19.542 1.834  26.954  1.00 36.53 ?  102 GLU A CA    1 
ATOM   775  C C     . GLU A 1 102 ? -20.942 1.763  27.562  1.00 34.50 ?  102 GLU A C     1 
ATOM   776  O O     . GLU A 1 102 ? -21.814 1.056  27.048  1.00 34.91 ?  102 GLU A O     1 
ATOM   777  C CB    . GLU A 1 102 ? -18.593 0.867  27.680  1.00 39.14 ?  102 GLU A CB    1 
ATOM   778  C CG    . GLU A 1 102 ? -17.109 1.225  27.600  1.00 45.48 ?  102 GLU A CG    1 
ATOM   779  C CD    . GLU A 1 102 ? -16.151 0.147  28.168  1.00 55.93 ?  102 GLU A CD    1 
ATOM   780  O OE1   . GLU A 1 102 ? -16.027 0.067  29.415  1.00 51.99 ?  102 GLU A OE1   1 
ATOM   781  O OE2   . GLU A 1 102 ? -15.484 -0.578 27.378  1.00 54.08 -1 102 GLU A OE2   1 
ATOM   782  N N     . LEU A 1 103 ? -21.183 2.498  28.646  1.00 36.95 ?  103 LEU A N     1 
ATOM   783  C CA    . LEU A 1 103 ? -22.513 2.479  29.246  1.00 34.79 ?  103 LEU A CA    1 
ATOM   784  C C     . LEU A 1 103 ? -23.547 3.027  28.280  1.00 41.46 ?  103 LEU A C     1 
ATOM   785  O O     . LEU A 1 103 ? -24.638 2.460  28.134  1.00 43.15 ?  103 LEU A O     1 
ATOM   786  C CB    . LEU A 1 103 ? -22.526 3.287  30.542  1.00 36.44 ?  103 LEU A CB    1 
ATOM   787  C CG    . LEU A 1 103 ? -22.439 2.440  31.806  1.00 42.52 ?  103 LEU A CG    1 
ATOM   788  C CD1   . LEU A 1 103 ? -22.063 3.295  33.005  1.00 45.58 ?  103 LEU A CD1   1 
ATOM   789  C CD2   . LEU A 1 103 ? -23.752 1.719  32.045  1.00 49.86 ?  103 LEU A CD2   1 
ATOM   790  N N     . LEU A 1 104 ? -23.214 4.123  27.596  1.00 38.08 ?  104 LEU A N     1 
ATOM   791  C CA    . LEU A 1 104 ? -24.168 4.744  26.688  1.00 33.61 ?  104 LEU A CA    1 
ATOM   792  C C     . LEU A 1 104 ? -24.473 3.830  25.509  1.00 33.75 ?  104 LEU A C     1 
ATOM   793  O O     . LEU A 1 104 ? -25.638 3.684  25.116  1.00 34.20 ?  104 LEU A O     1 
ATOM   794  C CB    . LEU A 1 104 ? -23.630 6.098  26.223  1.00 34.06 ?  104 LEU A CB    1 
ATOM   795  C CG    . LEU A 1 104 ? -23.963 7.268  27.156  1.00 32.62 ?  104 LEU A CG    1 
ATOM   796  C CD1   . LEU A 1 104 ? -23.178 8.528  26.783  1.00 28.62 ?  104 LEU A CD1   1 
ATOM   797  C CD2   . LEU A 1 104 ? -25.452 7.554  27.161  1.00 27.68 ?  104 LEU A CD2   1 
ATOM   798  N N     . LEU A 1 105 ? -23.447 3.182  24.948  1.00 29.39 ?  105 LEU A N     1 
ATOM   799  C CA    . LEU A 1 105 ? -23.686 2.281  23.827  1.00 31.36 ?  105 LEU A CA    1 
ATOM   800  C C     . LEU A 1 105 ? -24.543 1.102  24.258  1.00 40.62 ?  105 LEU A C     1 
ATOM   801  O O     . LEU A 1 105 ? -25.415 0.647  23.504  1.00 37.83 ?  105 LEU A O     1 
ATOM   802  C CB    . LEU A 1 105 ? -22.373 1.791  23.233  1.00 28.17 ?  105 LEU A CB    1 
ATOM   803  C CG    . LEU A 1 105 ? -21.587 2.865  22.478  1.00 34.23 ?  105 LEU A CG    1 
ATOM   804  C CD1   . LEU A 1 105 ? -20.335 2.281  21.841  1.00 32.87 ?  105 LEU A CD1   1 
ATOM   805  C CD2   . LEU A 1 105 ? -22.469 3.537  21.439  1.00 29.30 ?  105 LEU A CD2   1 
ATOM   806  N N     . THR A 1 106 ? -24.323 0.607  25.479  1.00 39.49 ?  106 THR A N     1 
ATOM   807  C CA    . THR A 1 106 ? -25.089 -0.537 25.953  1.00 41.08 ?  106 THR A CA    1 
ATOM   808  C C     . THR A 1 106 ? -26.559 -0.180 26.108  1.00 37.42 ?  106 THR A C     1 
ATOM   809  O O     . THR A 1 106 ? -27.439 -0.945 25.694  1.00 44.03 ?  106 THR A O     1 
ATOM   810  C CB    . THR A 1 106 ? -24.497 -1.041 27.266  1.00 40.29 ?  106 THR A CB    1 
ATOM   811  O OG1   . THR A 1 106 ? -23.344 -1.836 26.973  1.00 41.35 ?  106 THR A OG1   1 
ATOM   812  C CG2   . THR A 1 106 ? -25.497 -1.895 28.002  1.00 44.11 ?  106 THR A CG2   1 
ATOM   813  N N     . GLN A 1 107 ? -26.851 0.996  26.655  1.00 36.72 ?  107 GLN A N     1 
ATOM   814  C CA    . GLN A 1 107 ? -28.247 1.341  26.868  1.00 42.00 ?  107 GLN A CA    1 
ATOM   815  C C     . GLN A 1 107 ? -28.927 1.782  25.576  1.00 45.67 ?  107 GLN A C     1 
ATOM   816  O O     . GLN A 1 107 ? -30.079 1.412  25.329  1.00 41.85 ?  107 GLN A O     1 
ATOM   817  C CB    . GLN A 1 107 ? -28.357 2.417  27.944  1.00 44.86 ?  107 GLN A CB    1 
ATOM   818  C CG    . GLN A 1 107 ? -28.775 3.786  27.461  1.00 45.27 ?  107 GLN A CG    1 
ATOM   819  C CD    . GLN A 1 107 ? -28.987 4.729  28.617  1.00 49.89 ?  107 GLN A CD    1 
ATOM   820  O OE1   . GLN A 1 107 ? -28.476 4.490  29.717  1.00 52.57 ?  107 GLN A OE1   1 
ATOM   821  N NE2   . GLN A 1 107 ? -29.719 5.817  28.379  1.00 47.48 ?  107 GLN A NE2   1 
ATOM   822  N N     . LEU A 1 108 ? -28.233 2.539  24.720  1.00 39.55 ?  108 LEU A N     1 
ATOM   823  C CA    . LEU A 1 108 ? -28.893 3.140  23.565  1.00 37.70 ?  108 LEU A CA    1 
ATOM   824  C C     . LEU A 1 108 ? -28.885 2.233  22.336  1.00 34.57 ?  108 LEU A C     1 
ATOM   825  O O     . LEU A 1 108 ? -29.769 2.355  21.482  1.00 35.16 ?  108 LEU A O     1 
ATOM   826  C CB    . LEU A 1 108 ? -28.236 4.490  23.238  1.00 37.46 ?  108 LEU A CB    1 
ATOM   827  C CG    . LEU A 1 108 ? -28.649 5.646  24.158  1.00 37.55 ?  108 LEU A CG    1 
ATOM   828  C CD1   . LEU A 1 108 ? -27.725 6.862  24.039  1.00 33.97 ?  108 LEU A CD1   1 
ATOM   829  C CD2   . LEU A 1 108 ? -30.081 6.049  23.864  1.00 39.97 ?  108 LEU A CD2   1 
ATOM   830  N N     . LYS A 1 109 ? -27.903 1.342  22.233  1.00 32.42 ?  109 LYS A N     1 
ATOM   831  C CA    . LYS A 1 109 ? -27.671 0.407  21.135  1.00 33.58 ?  109 LYS A CA    1 
ATOM   832  C C     . LYS A 1 109 ? -27.882 0.980  19.732  1.00 31.74 ?  109 LYS A C     1 
ATOM   833  O O     . LYS A 1 109 ? -28.790 0.544  19.013  1.00 32.49 ?  109 LYS A O     1 
ATOM   834  C CB    . LYS A 1 109 ? -28.549 -0.829 21.339  1.00 40.33 ?  109 LYS A CB    1 
ATOM   835  C CG    . LYS A 1 109 ? -28.619 -1.273 22.787  1.00 40.02 ?  109 LYS A CG    1 
ATOM   836  C CD    . LYS A 1 109 ? -28.843 -2.765 22.887  1.00 47.05 ?  109 LYS A CD    1 
ATOM   837  C CE    . LYS A 1 109 ? -29.953 -3.062 23.861  1.00 42.70 ?  109 LYS A CE    1 
ATOM   838  N NZ    . LYS A 1 109 ? -31.265 -2.632 23.286  1.00 47.35 ?  109 LYS A NZ    1 
ATOM   839  N N     . PRO A 1 110 ? -27.047 1.917  19.288  1.00 35.34 ?  110 PRO A N     1 
ATOM   840  C CA    . PRO A 1 110 ? -27.131 2.392  17.903  1.00 29.76 ?  110 PRO A CA    1 
ATOM   841  C C     . PRO A 1 110 ? -26.543 1.371  16.941  1.00 26.92 ?  110 PRO A C     1 
ATOM   842  O O     . PRO A 1 110 ? -25.808 0.461  17.329  1.00 30.32 ?  110 PRO A O     1 
ATOM   843  C CB    . PRO A 1 110 ? -26.282 3.667  17.921  1.00 28.22 ?  110 PRO A CB    1 
ATOM   844  C CG    . PRO A 1 110 ? -25.190 3.327  18.923  1.00 26.28 ?  110 PRO A CG    1 
ATOM   845  C CD    . PRO A 1 110 ? -25.914 2.532  20.008  1.00 31.54 ?  110 PRO A CD    1 
ATOM   846  N N     . GLN A 1 111 ? -26.863 1.545  15.660  1.00 24.12 ?  111 GLN A N     1 
ATOM   847  C CA    . GLN A 1 111 ? -26.269 0.673  14.656  1.00 22.70 ?  111 GLN A CA    1 
ATOM   848  C C     . GLN A 1 111 ? -24.892 1.155  14.199  1.00 30.58 ?  111 GLN A C     1 
ATOM   849  O O     . GLN A 1 111 ? -24.089 0.351  13.698  1.00 29.20 ?  111 GLN A O     1 
ATOM   850  C CB    . GLN A 1 111 ? -27.193 0.572  13.460  1.00 27.48 ?  111 GLN A CB    1 
ATOM   851  C CG    . GLN A 1 111 ? -28.574 0.053  13.816  1.00 31.85 ?  111 GLN A CG    1 
ATOM   852  C CD    . GLN A 1 111 ? -29.561 0.376  12.739  1.00 33.49 ?  111 GLN A CD    1 
ATOM   853  O OE1   . GLN A 1 111 ? -30.197 1.431  12.761  1.00 33.62 ?  111 GLN A OE1   1 
ATOM   854  N NE2   . GLN A 1 111 ? -29.660 -0.502 11.751  1.00 36.59 ?  111 GLN A NE2   1 
ATOM   855  N N     . ILE A 1 112 ? -24.621 2.455  14.333  1.00 21.50 ?  112 ILE A N     1 
ATOM   856  C CA    . ILE A 1 112 ? -23.375 3.083  13.905  1.00 24.76 ?  112 ILE A CA    1 
ATOM   857  C C     . ILE A 1 112 ? -23.032 4.145  14.934  1.00 23.63 ?  112 ILE A C     1 
ATOM   858  O O     . ILE A 1 112 ? -23.926 4.775  15.511  1.00 24.52 ?  112 ILE A O     1 
ATOM   859  C CB    . ILE A 1 112 ? -23.481 3.740  12.498  1.00 25.07 ?  112 ILE A CB    1 
ATOM   860  C CG1   . ILE A 1 112 ? -24.408 2.948  11.577  1.00 30.00 ?  112 ILE A CG1   1 
ATOM   861  C CG2   . ILE A 1 112 ? -22.093 3.958  11.859  1.00 25.38 ?  112 ILE A CG2   1 
ATOM   862  C CD1   . ILE A 1 112 ? -24.476 3.467  10.152  1.00 31.76 ?  112 ILE A CD1   1 
ATOM   863  N N     . ILE A 1 113 ? -21.732 4.360  15.154  1.00 22.72 ?  113 ILE A N     1 
ATOM   864  C CA    . ILE A 1 113 ? -21.260 5.524  15.902  1.00 21.80 ?  113 ILE A CA    1 
ATOM   865  C C     . ILE A 1 113 ? -20.209 6.258  15.057  1.00 22.66 ?  113 ILE A C     1 
ATOM   866  O O     . ILE A 1 113 ? -19.235 5.647  14.598  1.00 19.72 ?  113 ILE A O     1 
ATOM   867  C CB    . ILE A 1 113 ? -20.715 5.144  17.298  1.00 26.34 ?  113 ILE A CB    1 
ATOM   868  C CG1   . ILE A 1 113 ? -20.146 6.372  18.032  1.00 22.44 ?  113 ILE A CG1   1 
ATOM   869  C CG2   . ILE A 1 113 ? -19.713 3.980  17.233  1.00 23.62 ?  113 ILE A CG2   1 
ATOM   870  C CD1   . ILE A 1 113 ? -20.247 6.271  19.546  1.00 25.43 ?  113 ILE A CD1   1 
ATOM   871  N N     . PHE A 1 114 ? -20.459 7.548  14.786  1.00 22.65 ?  114 PHE A N     1 
ATOM   872  C CA    . PHE A 1 114 ? -19.468 8.440  14.178  1.00 20.23 ?  114 PHE A CA    1 
ATOM   873  C C     . PHE A 1 114 ? -18.524 8.922  15.275  1.00 19.76 ?  114 PHE A C     1 
ATOM   874  O O     . PHE A 1 114 ? -18.998 9.373  16.325  1.00 23.85 ?  114 PHE A O     1 
ATOM   875  C CB    . PHE A 1 114 ? -20.130 9.677  13.550  1.00 19.56 ?  114 PHE A CB    1 
ATOM   876  C CG    . PHE A 1 114 ? -20.948 9.436  12.283  1.00 22.40 ?  114 PHE A CG    1 
ATOM   877  C CD1   . PHE A 1 114 ? -21.573 8.223  12.019  1.00 20.57 ?  114 PHE A CD1   1 
ATOM   878  C CD2   . PHE A 1 114 ? -21.122 10.482 11.373  1.00 18.04 ?  114 PHE A CD2   1 
ATOM   879  C CE1   . PHE A 1 114 ? -22.325 8.037  10.850  1.00 22.51 ?  114 PHE A CE1   1 
ATOM   880  C CE2   . PHE A 1 114 ? -21.878 10.315 10.201  1.00 21.87 ?  114 PHE A CE2   1 
ATOM   881  C CZ    . PHE A 1 114 ? -22.488 9.083  9.938   1.00 22.25 ?  114 PHE A CZ    1 
ATOM   882  N N     . PHE A 1 115 ? -17.206 8.897  15.039  1.00 20.67 ?  115 PHE A N     1 
ATOM   883  C CA    . PHE A 1 115 ? -16.293 9.342  16.100  1.00 18.92 ?  115 PHE A CA    1 
ATOM   884  C C     . PHE A 1 115 ? -15.046 10.034 15.536  1.00 18.47 ?  115 PHE A C     1 
ATOM   885  O O     . PHE A 1 115 ? -14.712 9.894  14.358  1.00 17.08 ?  115 PHE A O     1 
ATOM   886  C CB    . PHE A 1 115 ? -15.869 8.163  16.998  1.00 18.74 ?  115 PHE A CB    1 
ATOM   887  C CG    . PHE A 1 115 ? -14.930 7.198  16.326  1.00 20.94 ?  115 PHE A CG    1 
ATOM   888  C CD1   . PHE A 1 115 ? -15.401 6.290  15.377  1.00 19.59 ?  115 PHE A CD1   1 
ATOM   889  C CD2   . PHE A 1 115 ? -13.570 7.206  16.624  1.00 18.73 ?  115 PHE A CD2   1 
ATOM   890  C CE1   . PHE A 1 115 ? -14.525 5.418  14.740  1.00 19.51 ?  115 PHE A CE1   1 
ATOM   891  C CE2   . PHE A 1 115 ? -12.698 6.332  16.008  1.00 19.48 ?  115 PHE A CE2   1 
ATOM   892  C CZ    . PHE A 1 115 ? -13.178 5.427  15.062  1.00 20.76 ?  115 PHE A CZ    1 
ATOM   893  N N     . ASP A 1 116 ? -14.355 10.771 16.423  1.00 21.17 ?  116 ASP A N     1 
ATOM   894  C CA    . ASP A 1 116 ? -12.990 11.275 16.240  1.00 21.48 ?  116 ASP A CA    1 
ATOM   895  C C     . ASP A 1 116 ? -12.013 10.614 17.207  1.00 20.69 ?  116 ASP A C     1 
ATOM   896  O O     . ASP A 1 116 ? -12.355 10.361 18.367  1.00 21.89 ?  116 ASP A O     1 
ATOM   897  C CB    . ASP A 1 116 ? -12.890 12.781 16.535  1.00 20.02 ?  116 ASP A CB    1 
ATOM   898  C CG    . ASP A 1 116 ? -13.448 13.657 15.430  1.00 21.63 ?  116 ASP A CG    1 
ATOM   899  O OD1   . ASP A 1 116 ? -13.154 13.415 14.239  1.00 22.75 ?  116 ASP A OD1   1 
ATOM   900  O OD2   . ASP A 1 116 ? -14.173 14.610 15.786  1.00 21.70 -1 116 ASP A OD2   1 
ATOM   901  N N     . PHE A 1 117 ? -10.775 10.398 16.744  1.00 17.15 ?  117 PHE A N     1 
ATOM   902  C CA    . PHE A 1 117 ? -9.603  10.252 17.612  1.00 20.85 ?  117 PHE A CA    1 
ATOM   903  C C     . PHE A 1 117 ? -9.525  9.008  18.507  1.00 24.17 ?  117 PHE A C     1 
ATOM   904  O O     . PHE A 1 117 ? -8.418  8.539  18.781  1.00 21.14 ?  117 PHE A O     1 
ATOM   905  C CB    . PHE A 1 117 ? -9.473  11.488 18.516  1.00 16.15 ?  117 PHE A CB    1 
ATOM   906  C CG    . PHE A 1 117 ? -8.803  12.664 17.853  1.00 20.17 ?  117 PHE A CG    1 
ATOM   907  C CD1   . PHE A 1 117 ? -7.630  12.503 17.132  1.00 20.08 ?  117 PHE A CD1   1 
ATOM   908  C CD2   . PHE A 1 117 ? -9.348  13.931 17.959  1.00 19.88 ?  117 PHE A CD2   1 
ATOM   909  C CE1   . PHE A 1 117 ? -7.003  13.588 16.529  1.00 19.28 ?  117 PHE A CE1   1 
ATOM   910  C CE2   . PHE A 1 117 ? -8.734  15.023 17.337  1.00 21.25 ?  117 PHE A CE2   1 
ATOM   911  C CZ    . PHE A 1 117 ? -7.563  14.845 16.627  1.00 19.37 ?  117 PHE A CZ    1 
ATOM   912  N N     . VAL A 1 118 ? -10.641 8.477  19.010  1.00 21.04 ?  118 VAL A N     1 
ATOM   913  C CA    . VAL A 1 118 ? -10.580 7.466  20.083  1.00 21.20 ?  118 VAL A CA    1 
ATOM   914  C C     . VAL A 1 118 ? -10.442 6.096  19.418  1.00 25.66 ?  118 VAL A C     1 
ATOM   915  O O     . VAL A 1 118 ? -11.426 5.411  19.115  1.00 23.47 ?  118 VAL A O     1 
ATOM   916  C CB    . VAL A 1 118 ? -11.777 7.555  21.038  1.00 24.12 ?  118 VAL A CB    1 
ATOM   917  C CG1   . VAL A 1 118 ? -11.674 8.826  21.874  1.00 22.67 ?  118 VAL A CG1   1 
ATOM   918  C CG2   . VAL A 1 118 ? -13.136 7.517  20.304  1.00 21.32 ?  118 VAL A CG2   1 
ATOM   919  N N     . PHE A 1 119 ? -9.191  5.668  19.216  1.00 22.99 ?  119 PHE A N     1 
ATOM   920  C CA    . PHE A 1 119 ? -8.960  4.413  18.504  1.00 26.72 ?  119 PHE A CA    1 
ATOM   921  C C     . PHE A 1 119 ? -9.274  3.184  19.351  1.00 28.41 ?  119 PHE A C     1 
ATOM   922  O O     . PHE A 1 119 ? -9.277  2.071  18.820  1.00 27.63 ?  119 PHE A O     1 
ATOM   923  C CB    . PHE A 1 119 ? -7.520  4.339  17.982  1.00 22.86 ?  119 PHE A CB    1 
ATOM   924  C CG    . PHE A 1 119 ? -6.470  4.364  19.061  1.00 29.20 ?  119 PHE A CG    1 
ATOM   925  C CD1   . PHE A 1 119 ? -6.055  3.187  19.680  1.00 29.95 ?  119 PHE A CD1   1 
ATOM   926  C CD2   . PHE A 1 119 ? -5.886  5.569  19.449  1.00 29.72 ?  119 PHE A CD2   1 
ATOM   927  C CE1   . PHE A 1 119 ? -5.071  3.213  20.680  1.00 37.13 ?  119 PHE A CE1   1 
ATOM   928  C CE2   . PHE A 1 119 ? -4.897  5.611  20.440  1.00 34.86 ?  119 PHE A CE2   1 
ATOM   929  C CZ    . PHE A 1 119 ? -4.486  4.427  21.062  1.00 34.32 ?  119 PHE A CZ    1 
ATOM   930  N N     . TRP A 1 120 ? -9.546  3.349  20.638  1.00 28.60 ?  120 TRP A N     1 
ATOM   931  C CA    . TRP A 1 120 ? -10.022 2.222  21.427  1.00 30.76 ?  120 TRP A CA    1 
ATOM   932  C C     . TRP A 1 120 ? -11.485 1.884  21.154  1.00 34.61 ?  120 TRP A C     1 
ATOM   933  O O     . TRP A 1 120 ? -11.962 0.849  21.631  1.00 36.41 ?  120 TRP A O     1 
ATOM   934  C CB    . TRP A 1 120 ? -9.810  2.510  22.921  1.00 29.92 ?  120 TRP A CB    1 
ATOM   935  C CG    . TRP A 1 120 ? -10.250 3.881  23.365  1.00 28.65 ?  120 TRP A CG    1 
ATOM   936  C CD1   . TRP A 1 120 ? -9.450  4.961  23.620  1.00 33.11 ?  120 TRP A CD1   1 
ATOM   937  C CD2   . TRP A 1 120 ? -11.592 4.309  23.631  1.00 29.24 ?  120 TRP A CD2   1 
ATOM   938  N NE1   . TRP A 1 120 ? -10.214 6.032  24.011  1.00 29.01 ?  120 TRP A NE1   1 
ATOM   939  C CE2   . TRP A 1 120 ? -11.528 5.655  24.038  1.00 24.78 ?  120 TRP A CE2   1 
ATOM   940  C CE3   . TRP A 1 120 ? -12.840 3.683  23.564  1.00 30.14 ?  120 TRP A CE3   1 
ATOM   941  C CZ2   . TRP A 1 120 ? -12.665 6.388  24.370  1.00 27.97 ?  120 TRP A CZ2   1 
ATOM   942  C CZ3   . TRP A 1 120 ? -13.969 4.416  23.891  1.00 27.60 ?  120 TRP A CZ3   1 
ATOM   943  C CH2   . TRP A 1 120 ? -13.872 5.753  24.283  1.00 27.34 ?  120 TRP A CH2   1 
ATOM   944  N N     . LEU A 1 121 ? -12.205 2.716  20.387  1.00 30.56 ?  121 LEU A N     1 
ATOM   945  C CA    . LEU A 1 121 ? -13.642 2.504  20.242  1.00 29.71 ?  121 LEU A CA    1 
ATOM   946  C C     . LEU A 1 121 ? -13.972 1.301  19.369  1.00 32.15 ?  121 LEU A C     1 
ATOM   947  O O     . LEU A 1 121 ? -14.844 0.510  19.765  1.00 34.02 ?  121 LEU A O     1 
ATOM   948  C CB    . LEU A 1 121 ? -14.314 3.783  19.732  1.00 31.74 ?  121 LEU A CB    1 
ATOM   949  C CG    . LEU A 1 121 ? -15.845 3.781  19.663  1.00 25.81 ?  121 LEU A CG    1 
ATOM   950  C CD1   . LEU A 1 121 ? -16.447 3.483  21.027  1.00 31.18 ?  121 LEU A CD1   1 
ATOM   951  C CD2   . LEU A 1 121 ? -16.377 5.113  19.113  1.00 25.45 ?  121 LEU A CD2   1 
ATOM   952  N N     . PRO A 1 122 ? -13.354 1.098  18.194  1.00 29.93 ?  122 PRO A N     1 
ATOM   953  C CA    . PRO A 1 122 ? -13.754 -0.052 17.362  1.00 30.84 ?  122 PRO A CA    1 
ATOM   954  C C     . PRO A 1 122 ? -13.742 -1.392 18.097  1.00 39.12 ?  122 PRO A C     1 
ATOM   955  O O     . PRO A 1 122 ? -14.588 -2.251 17.809  1.00 35.71 ?  122 PRO A O     1 
ATOM   956  C CB    . PRO A 1 122 ? -12.733 -0.018 16.215  1.00 32.42 ?  122 PRO A CB    1 
ATOM   957  C CG    . PRO A 1 122 ? -12.390 1.439  16.074  1.00 30.69 ?  122 PRO A CG    1 
ATOM   958  C CD    . PRO A 1 122 ? -12.346 1.936  17.506  1.00 30.42 ?  122 PRO A CD    1 
ATOM   959  N N     . LYS A 1 123 ? -12.830 -1.592 19.055  1.00 41.02 ?  123 LYS A N     1 
ATOM   960  C CA    . LYS A 1 123 ? -12.848 -2.832 19.822  1.00 41.29 ?  123 LYS A CA    1 
ATOM   961  C C     . LYS A 1 123 ? -14.150 -2.973 20.596  1.00 36.37 ?  123 LYS A C     1 
ATOM   962  O O     . LYS A 1 123 ? -14.760 -4.047 20.603  1.00 40.71 ?  123 LYS A O     1 
ATOM   963  C CB    . LYS A 1 123 ? -11.655 -2.891 20.773  1.00 41.32 ?  123 LYS A CB    1 
ATOM   964  C CG    . LYS A 1 123 ? -11.363 -4.286 21.278  1.00 40.98 ?  123 LYS A CG    1 
ATOM   965  C CD    . LYS A 1 123 ? -10.291 -4.284 22.356  1.00 46.79 ?  123 LYS A CD    1 
ATOM   966  C CE    . LYS A 1 123 ? -10.522 -5.424 23.348  1.00 52.41 ?  123 LYS A CE    1 
ATOM   967  N NZ    . LYS A 1 123 ? -9.471  -5.487 24.409  1.00 52.79 ?  123 LYS A NZ    1 
ATOM   968  N N     . ILE A 1 124 ? -14.601 -1.892 21.235  1.00 33.16 ?  124 ILE A N     1 
ATOM   969  C CA    . ILE A 1 124 ? -15.848 -1.928 21.996  1.00 40.09 ?  124 ILE A CA    1 
ATOM   970  C C     . ILE A 1 124 ? -17.041 -2.178 21.083  1.00 42.23 ?  124 ILE A C     1 
ATOM   971  O O     . ILE A 1 124 ? -17.945 -2.953 21.415  1.00 43.37 ?  124 ILE A O     1 
ATOM   972  C CB    . ILE A 1 124 ? -16.038 -0.621 22.779  1.00 38.61 ?  124 ILE A CB    1 
ATOM   973  C CG1   . ILE A 1 124 ? -14.837 -0.343 23.671  1.00 35.01 ?  124 ILE A CG1   1 
ATOM   974  C CG2   . ILE A 1 124 ? -17.338 -0.660 23.577  1.00 39.74 ?  124 ILE A CG2   1 
ATOM   975  C CD1   . ILE A 1 124 ? -14.989 0.965  24.391  1.00 35.01 ?  124 ILE A CD1   1 
ATOM   976  N N     . THR A 1 125 ? -17.091 -1.487 19.940  1.00 37.78 ?  125 THR A N     1 
ATOM   977  C CA    . THR A 1 125 ? -18.317 -1.507 19.148  1.00 36.49 ?  125 THR A CA    1 
ATOM   978  C C     . THR A 1 125 ? -18.529 -2.868 18.502  1.00 40.47 ?  125 THR A C     1 
ATOM   979  O O     . THR A 1 125 ? -19.667 -3.347 18.402  1.00 38.16 ?  125 THR A O     1 
ATOM   980  C CB    . THR A 1 125 ? -18.290 -0.416 18.078  1.00 33.00 ?  125 THR A CB    1 
ATOM   981  O OG1   . THR A 1 125 ? -17.090 -0.535 17.303  1.00 33.30 ?  125 THR A OG1   1 
ATOM   982  C CG2   . THR A 1 125 ? -18.362 0.962  18.720  1.00 32.77 ?  125 THR A CG2   1 
ATOM   983  N N     . GLN A 1 126 ? -17.451 -3.504 18.050  1.00 36.30 ?  126 GLN A N     1 
ATOM   984  C CA    . GLN A 1 126 ? -17.624 -4.790 17.398  1.00 41.90 ?  126 GLN A CA    1 
ATOM   985  C C     . GLN A 1 126 ? -18.070 -5.853 18.390  1.00 44.19 ?  126 GLN A C     1 
ATOM   986  O O     . GLN A 1 126 ? -18.821 -6.765 18.025  1.00 45.74 ?  126 GLN A O     1 
ATOM   987  C CB    . GLN A 1 126 ? -16.336 -5.207 16.720  1.00 41.05 ?  126 GLN A CB    1 
ATOM   988  C CG    . GLN A 1 126 ? -15.545 -6.109 17.575  1.00 47.36 ?  126 GLN A CG    1 
ATOM   989  C CD    . GLN A 1 126 ? -14.685 -7.007 16.780  1.00 53.21 ?  126 GLN A CD    1 
ATOM   990  O OE1   . GLN A 1 126 ? -15.113 -7.544 15.759  1.00 56.37 ?  126 GLN A OE1   1 
ATOM   991  N NE2   . GLN A 1 126 ? -13.469 -7.220 17.255  1.00 63.59 ?  126 GLN A NE2   1 
ATOM   992  N N     . ARG A 1 127 ? -17.634 -5.740 19.646  1.00 41.71 ?  127 ARG A N     1 
ATOM   993  C CA    . ARG A 1 127 ? -18.129 -6.633 20.683  1.00 46.11 ?  127 ARG A CA    1 
ATOM   994  C C     . ARG A 1 127 ? -19.623 -6.427 20.920  1.00 46.40 ?  127 ARG A C     1 
ATOM   995  O O     . ARG A 1 127 ? -20.335 -7.380 21.256  1.00 48.13 ?  127 ARG A O     1 
ATOM   996  C CB    . ARG A 1 127 ? -17.314 -6.424 21.963  1.00 43.21 ?  127 ARG A CB    1 
ATOM   997  C CG    . ARG A 1 127 ? -17.923 -7.018 23.210  1.00 47.34 ?  127 ARG A CG    1 
ATOM   998  C CD    . ARG A 1 127 ? -16.917 -7.073 24.352  1.00 52.02 ?  127 ARG A CD    1 
ATOM   999  N NE    . ARG A 1 127 ? -16.437 -5.761 24.782  1.00 49.74 ?  127 ARG A NE    1 
ATOM   1000 C CZ    . ARG A 1 127 ? -17.158 -4.879 25.465  1.00 50.94 ?  127 ARG A CZ    1 
ATOM   1001 N NH1   . ARG A 1 127 ? -18.425 -5.108 25.777  1.00 55.30 ?  127 ARG A NH1   1 
ATOM   1002 N NH2   . ARG A 1 127 ? -16.591 -3.738 25.847  1.00 49.69 ?  127 ARG A NH2   1 
ATOM   1003 N N     . LEU A 1 128 ? -20.127 -5.212 20.710  1.00 42.07 ?  128 LEU A N     1 
ATOM   1004 C CA    . LEU A 1 128 ? -21.551 -4.950 20.861  1.00 40.00 ?  128 LEU A CA    1 
ATOM   1005 C C     . LEU A 1 128 ? -22.325 -5.078 19.556  1.00 40.18 ?  128 LEU A C     1 
ATOM   1006 O O     . LEU A 1 128 ? -23.536 -4.826 19.543  1.00 35.98 ?  128 LEU A O     1 
ATOM   1007 C CB    . LEU A 1 128 ? -21.780 -3.557 21.451  1.00 38.97 ?  128 LEU A CB    1 
ATOM   1008 C CG    . LEU A 1 128 ? -21.083 -3.258 22.772  1.00 42.07 ?  128 LEU A CG    1 
ATOM   1009 C CD1   . LEU A 1 128 ? -21.593 -1.937 23.374  1.00 34.13 ?  128 LEU A CD1   1 
ATOM   1010 C CD2   . LEU A 1 128 ? -21.261 -4.426 23.737  1.00 46.71 ?  128 LEU A CD2   1 
ATOM   1011 N N     . GLY A 1 129 ? -21.672 -5.474 18.469  1.00 36.21 ?  129 GLY A N     1 
ATOM   1012 C CA    . GLY A 1 129 ? -22.356 -5.518 17.192  1.00 36.52 ?  129 GLY A CA    1 
ATOM   1013 C C     . GLY A 1 129 ? -22.687 -4.156 16.614  1.00 37.31 ?  129 GLY A C     1 
ATOM   1014 O O     . GLY A 1 129 ? -23.670 -4.033 15.886  1.00 35.88 ?  129 GLY A O     1 
ATOM   1015 N N     . ILE A 1 130 ? -21.885 -3.123 16.926  1.00 35.77 ?  130 ILE A N     1 
ATOM   1016 C CA    . ILE A 1 130 ? -22.036 -1.773 16.382  1.00 32.47 ?  130 ILE A CA    1 
ATOM   1017 C C     . ILE A 1 130 ? -20.955 -1.535 15.334  1.00 34.95 ?  130 ILE A C     1 
ATOM   1018 O O     . ILE A 1 130 ? -19.828 -2.037 15.444  1.00 32.83 ?  130 ILE A O     1 
ATOM   1019 C CB    . ILE A 1 130 ? -21.966 -0.717 17.512  1.00 32.73 ?  130 ILE A CB    1 
ATOM   1020 C CG1   . ILE A 1 130 ? -22.845 -1.148 18.688  1.00 30.37 ?  130 ILE A CG1   1 
ATOM   1021 C CG2   . ILE A 1 130 ? -22.349 0.667  17.001  1.00 30.13 ?  130 ILE A CG2   1 
ATOM   1022 C CD1   . ILE A 1 130 ? -22.768 -0.255 19.919  1.00 27.02 ?  130 ILE A CD1   1 
ATOM   1023 N N     . LYS A 1 131 ? -21.287 -0.772 14.298  1.00 33.25 ?  131 LYS A N     1 
ATOM   1024 C CA    . LYS A 1 131 ? -20.295 -0.427 13.285  1.00 32.30 ?  131 LYS A CA    1 
ATOM   1025 C C     . LYS A 1 131 ? -19.610 0.880  13.671  1.00 27.99 ?  131 LYS A C     1 
ATOM   1026 O O     . LYS A 1 131 ? -20.256 1.818  14.146  1.00 27.47 ?  131 LYS A O     1 
ATOM   1027 C CB    . LYS A 1 131 ? -20.933 -0.299 11.899  1.00 34.43 ?  131 LYS A CB    1 
ATOM   1028 C CG    . LYS A 1 131 ? -21.799 -1.491 11.444  1.00 34.55 ?  131 LYS A CG    1 
ATOM   1029 C CD    . LYS A 1 131 ? -21.022 -2.814 11.409  1.00 37.93 ?  131 LYS A CD    1 
ATOM   1030 C CE    . LYS A 1 131 ? -20.109 -2.905 10.194  1.00 40.78 ?  131 LYS A CE    1 
ATOM   1031 N NZ    . LYS A 1 131 ? -19.453 -4.248 10.036  1.00 49.41 ?  131 LYS A NZ    1 
ATOM   1032 N N     . SER A 1 132 ? -18.299 0.937  13.474  1.00 28.33 ?  132 SER A N     1 
ATOM   1033 C CA    . SER A 1 132 ? -17.518 2.117  13.829  1.00 23.74 ?  132 SER A CA    1 
ATOM   1034 C C     . SER A 1 132 ? -17.247 2.940  12.571  1.00 20.58 ?  132 SER A C     1 
ATOM   1035 O O     . SER A 1 132 ? -16.843 2.391  11.543  1.00 24.08 ?  132 SER A O     1 
ATOM   1036 C CB    . SER A 1 132 ? -16.216 1.704  14.532  1.00 26.65 ?  132 SER A CB    1 
ATOM   1037 O OG    . SER A 1 132 ? -15.410 0.856  13.719  1.00 28.67 ?  132 SER A OG    1 
ATOM   1038 N N     . PHE A 1 133 ? -17.504 4.247  12.639  1.00 20.45 ?  133 PHE A N     1 
ATOM   1039 C CA    . PHE A 1 133 ? -17.367 5.136  11.485  1.00 18.70 ?  133 PHE A CA    1 
ATOM   1040 C C     . PHE A 1 133 ? -16.506 6.339  11.866  1.00 19.27 ?  133 PHE A C     1 
ATOM   1041 O O     . PHE A 1 133 ? -16.968 7.247  12.568  1.00 19.40 ?  133 PHE A O     1 
ATOM   1042 C CB    . PHE A 1 133 ? -18.743 5.596  10.985  1.00 21.35 ?  133 PHE A CB    1 
ATOM   1043 C CG    . PHE A 1 133 ? -18.716 6.241  9.634   1.00 22.19 ?  133 PHE A CG    1 
ATOM   1044 C CD1   . PHE A 1 133 ? -18.339 5.516  8.517   1.00 21.79 ?  133 PHE A CD1   1 
ATOM   1045 C CD2   . PHE A 1 133 ? -19.058 7.580  9.476   1.00 19.92 ?  133 PHE A CD2   1 
ATOM   1046 C CE1   . PHE A 1 133 ? -18.326 6.109  7.258   1.00 25.46 ?  133 PHE A CE1   1 
ATOM   1047 C CE2   . PHE A 1 133 ? -19.033 8.169  8.230   1.00 21.99 ?  133 PHE A CE2   1 
ATOM   1048 C CZ    . PHE A 1 133 ? -18.671 7.430  7.115   1.00 19.08 ?  133 PHE A CZ    1 
ATOM   1049 N N     . LEU A 1 134 ? -15.258 6.356  11.409  1.00 19.86 ?  134 LEU A N     1 
ATOM   1050 C CA    . LEU A 1 134 ? -14.363 7.471  11.704  1.00 16.01 ?  134 LEU A CA    1 
ATOM   1051 C C     . LEU A 1 134 ? -14.726 8.624  10.771  1.00 18.86 ?  134 LEU A C     1 
ATOM   1052 O O     . LEU A 1 134 ? -14.507 8.533  9.551   1.00 20.13 ?  134 LEU A O     1 
ATOM   1053 C CB    . LEU A 1 134 ? -12.918 7.024  11.519  1.00 17.25 ?  134 LEU A CB    1 
ATOM   1054 C CG    . LEU A 1 134 ? -11.777 8.030  11.720  1.00 16.76 ?  134 LEU A CG    1 
ATOM   1055 C CD1   . LEU A 1 134 ? -11.660 8.455  13.164  1.00 18.83 ?  134 LEU A CD1   1 
ATOM   1056 C CD2   . LEU A 1 134 ? -10.470 7.426  11.225  1.00 13.92 ?  134 LEU A CD2   1 
ATOM   1057 N N     . TYR A 1 135 ? -15.308 9.698  11.316  1.00 13.28 ?  135 TYR A N     1 
ATOM   1058 C CA    . TYR A 1 135 ? -15.872 10.767 10.481  1.00 16.54 ?  135 TYR A CA    1 
ATOM   1059 C C     . TYR A 1 135 ? -15.083 12.067 10.660  1.00 16.15 ?  135 TYR A C     1 
ATOM   1060 O O     . TYR A 1 135 ? -15.249 12.762 11.669  1.00 15.47 ?  135 TYR A O     1 
ATOM   1061 C CB    . TYR A 1 135 ? -17.355 11.005 10.777  1.00 15.28 ?  135 TYR A CB    1 
ATOM   1062 C CG    . TYR A 1 135 ? -17.914 12.128 9.921   1.00 16.77 ?  135 TYR A CG    1 
ATOM   1063 C CD1   . TYR A 1 135 ? -17.907 12.032 8.530   1.00 15.88 ?  135 TYR A CD1   1 
ATOM   1064 C CD2   . TYR A 1 135 ? -18.399 13.305 10.496  1.00 14.36 ?  135 TYR A CD2   1 
ATOM   1065 C CE1   . TYR A 1 135 ? -18.400 13.066 7.724   1.00 15.84 ?  135 TYR A CE1   1 
ATOM   1066 C CE2   . TYR A 1 135 ? -18.884 14.350 9.695   1.00 15.09 ?  135 TYR A CE2   1 
ATOM   1067 C CZ    . TYR A 1 135 ? -18.869 14.222 8.311   1.00 13.11 ?  135 TYR A CZ    1 
ATOM   1068 O OH    . TYR A 1 135 ? -19.320 15.258 7.517   1.00 14.26 ?  135 TYR A OH    1 
ATOM   1069 N N     . PHE A 1 136 ? -14.292 12.430 9.640   1.00 15.84 ?  136 PHE A N     1 
ATOM   1070 C CA    . PHE A 1 136 ? -13.474 13.648 9.655   1.00 15.22 ?  136 PHE A CA    1 
ATOM   1071 C C     . PHE A 1 136 ? -14.222 14.852 9.084   1.00 13.93 ?  136 PHE A C     1 
ATOM   1072 O O     . PHE A 1 136 ? -14.762 14.783 7.977   1.00 13.76 ?  136 PHE A O     1 
ATOM   1073 C CB    . PHE A 1 136 ? -12.206 13.482 8.807   1.00 14.58 ?  136 PHE A CB    1 
ATOM   1074 C CG    . PHE A 1 136 ? -11.293 12.401 9.252   1.00 17.96 ?  136 PHE A CG    1 
ATOM   1075 C CD1   . PHE A 1 136 ? -10.290 12.666 10.192  1.00 17.49 ?  136 PHE A CD1   1 
ATOM   1076 C CD2   . PHE A 1 136 ? -11.383 11.123 8.691   1.00 16.15 ?  136 PHE A CD2   1 
ATOM   1077 C CE1   . PHE A 1 136 ? -9.418  11.665 10.585  1.00 15.74 ?  136 PHE A CE1   1 
ATOM   1078 C CE2   . PHE A 1 136 ? -10.518 10.131 9.079   1.00 16.97 ?  136 PHE A CE2   1 
ATOM   1079 C CZ    . PHE A 1 136 ? -9.533  10.402 10.019  1.00 17.43 ?  136 PHE A CZ    1 
ATOM   1080 N N     . ILE A 1 137 ? -14.145 15.989 9.770   1.00 13.69 ?  137 ILE A N     1 
ATOM   1081 C CA    . ILE A 1 137 ? -14.621 17.236 9.182   1.00 12.79 ?  137 ILE A CA    1 
ATOM   1082 C C     . ILE A 1 137 ? -13.468 18.109 8.680   1.00 13.82 ?  137 ILE A C     1 
ATOM   1083 O O     . ILE A 1 137 ? -13.692 19.267 8.321   1.00 14.79 ?  137 ILE A O     1 
ATOM   1084 C CB    . ILE A 1 137 ? -15.540 17.993 10.164  1.00 15.41 ?  137 ILE A CB    1 
ATOM   1085 C CG1   . ILE A 1 137 ? -14.898 18.104 11.557  1.00 15.66 ?  137 ILE A CG1   1 
ATOM   1086 C CG2   . ILE A 1 137 ? -16.886 17.246 10.286  1.00 13.80 ?  137 ILE A CG2   1 
ATOM   1087 C CD1   . ILE A 1 137 ? -13.778 19.171 11.674  1.00 16.23 ?  137 ILE A CD1   1 
ATOM   1088 N N     . ILE A 1 138 ? -12.232 17.584 8.672   1.00 10.80 ?  138 ILE A N     1 
ATOM   1089 C CA    . ILE A 1 138 ? -11.085 18.253 8.070   1.00 17.15 ?  138 ILE A CA    1 
ATOM   1090 C C     . ILE A 1 138 ? -10.882 17.677 6.674   1.00 17.85 ?  138 ILE A C     1 
ATOM   1091 O O     . ILE A 1 138 ? -11.602 16.761 6.264   1.00 20.02 ?  138 ILE A O     1 
ATOM   1092 C CB    . ILE A 1 138 ? -9.799  18.091 8.916   1.00 18.30 ?  138 ILE A CB    1 
ATOM   1093 C CG1   . ILE A 1 138 ? -9.377  16.615 9.000   1.00 16.27 ?  138 ILE A CG1   1 
ATOM   1094 C CG2   . ILE A 1 138 ? -9.966  18.742 10.282  1.00 16.47 ?  138 ILE A CG2   1 
ATOM   1095 C CD1   . ILE A 1 138 ? -7.902  16.407 9.414   1.00 14.88 ?  138 ILE A CD1   1 
ATOM   1096 N N     . ASN A 1 139 ? -9.897  18.202 5.956   1.00 17.32 ?  139 ASN A N     1 
ATOM   1097 C CA    . ASN A 1 139 ? -9.696  17.886 4.540   1.00 16.32 ?  139 ASN A CA    1 
ATOM   1098 C C     . ASN A 1 139 ? -9.094  16.497 4.367   1.00 15.25 ?  139 ASN A C     1 
ATOM   1099 O O     . ASN A 1 139 ? -8.059  16.198 4.974   1.00 16.47 ?  139 ASN A O     1 
ATOM   1100 C CB    . ASN A 1 139 ? -8.749  18.928 3.938   1.00 19.84 ?  139 ASN A CB    1 
ATOM   1101 C CG    . ASN A 1 139 ? -8.831  19.009 2.426   1.00 22.34 ?  139 ASN A CG    1 
ATOM   1102 O OD1   . ASN A 1 139 ? -8.997  18.001 1.739   1.00 21.22 ?  139 ASN A OD1   1 
ATOM   1103 N ND2   . ASN A 1 139 ? -8.704  20.222 1.901   1.00 22.17 ?  139 ASN A ND2   1 
ATOM   1104 N N     . PRO A 1 140 ? -9.669  15.634 3.527   1.00 16.69 ?  140 PRO A N     1 
ATOM   1105 C CA    . PRO A 1 140 ? -8.987  14.359 3.242   1.00 16.69 ?  140 PRO A CA    1 
ATOM   1106 C C     . PRO A 1 140 ? -7.618  14.553 2.600   1.00 18.38 ?  140 PRO A C     1 
ATOM   1107 O O     . PRO A 1 140 ? -6.786  13.648 2.681   1.00 17.37 ?  140 PRO A O     1 
ATOM   1108 C CB    . PRO A 1 140 ? -9.956  13.624 2.301   1.00 17.60 ?  140 PRO A CB    1 
ATOM   1109 C CG    . PRO A 1 140 ? -10.877 14.685 1.768   1.00 19.82 ?  140 PRO A CG    1 
ATOM   1110 C CD    . PRO A 1 140 ? -10.975 15.733 2.862   1.00 18.88 ?  140 PRO A CD    1 
ATOM   1111 N N     . ALA A 1 141 ? -7.358  15.703 1.964   1.00 17.68 ?  141 ALA A N     1 
ATOM   1112 C CA    . ALA A 1 141 ? -6.019  15.962 1.446   1.00 17.04 ?  141 ALA A CA    1 
ATOM   1113 C C     . ALA A 1 141 ? -4.988  15.990 2.559   1.00 18.45 ?  141 ALA A C     1 
ATOM   1114 O O     . ALA A 1 141 ? -3.823  15.646 2.324   1.00 15.81 ?  141 ALA A O     1 
ATOM   1115 C CB    . ALA A 1 141 ? -5.984  17.279 0.672   1.00 19.60 ?  141 ALA A CB    1 
ATOM   1116 N N     . THR A 1 142 ? -5.403  16.390 3.773   1.00 18.31 ?  142 THR A N     1 
ATOM   1117 C CA    . THR A 1 142 ? -4.496  16.494 4.912   1.00 16.46 ?  142 THR A CA    1 
ATOM   1118 C C     . THR A 1 142 ? -4.134  15.115 5.455   1.00 22.18 ?  142 THR A C     1 
ATOM   1119 O O     . THR A 1 142 ? -2.944  14.782 5.593   1.00 19.83 ?  142 THR A O     1 
ATOM   1120 C CB    . THR A 1 142 ? -5.130  17.359 6.018   1.00 16.42 ?  142 THR A CB    1 
ATOM   1121 O OG1   . THR A 1 142 ? -5.351  18.670 5.520   1.00 15.15 ?  142 THR A OG1   1 
ATOM   1122 C CG2   . THR A 1 142 ? -4.204  17.479 7.236   1.00 15.56 ?  142 THR A CG2   1 
ATOM   1123 N N     . ILE A 1 143 ? -5.155  14.305 5.772   1.00 17.63 ?  143 ILE A N     1 
ATOM   1124 C CA    . ILE A 1 143 ? -4.934  12.921 6.196   1.00 19.88 ?  143 ILE A CA    1 
ATOM   1125 C C     . ILE A 1 143 ? -4.111  12.161 5.154   1.00 20.54 ?  143 ILE A C     1 
ATOM   1126 O O     . ILE A 1 143 ? -3.220  11.378 5.497   1.00 20.99 ?  143 ILE A O     1 
ATOM   1127 C CB    . ILE A 1 143 ? -6.281  12.221 6.459   1.00 18.22 ?  143 ILE A CB    1 
ATOM   1128 C CG1   . ILE A 1 143 ? -7.005  12.865 7.639   1.00 20.36 ?  143 ILE A CG1   1 
ATOM   1129 C CG2   . ILE A 1 143 ? -6.077  10.709 6.728   1.00 17.46 ?  143 ILE A CG2   1 
ATOM   1130 C CD1   . ILE A 1 143 ? -6.231  12.799 8.931   1.00 15.37 ?  143 ILE A CD1   1 
ATOM   1131 N N     . SER A 1 144 ? -4.410  12.371 3.871   1.00 18.60 ?  144 SER A N     1 
ATOM   1132 C CA    . SER A 1 144 ? -3.673  11.706 2.797   1.00 21.52 ?  144 SER A CA    1 
ATOM   1133 C C     . SER A 1 144 ? -2.186  12.059 2.826   1.00 22.77 ?  144 SER A C     1 
ATOM   1134 O O     . SER A 1 144 ? -1.326  11.201 2.597   1.00 26.32 ?  144 SER A O     1 
ATOM   1135 C CB    . SER A 1 144 ? -4.264  12.111 1.448   1.00 19.10 ?  144 SER A CB    1 
ATOM   1136 O OG    . SER A 1 144 ? -5.475  11.456 1.184   1.00 24.54 ?  144 SER A OG    1 
ATOM   1137 N N     . TYR A 1 145 ? -1.868  13.322 3.085   1.00 21.08 ?  145 TYR A N     1 
ATOM   1138 C CA    . TYR A 1 145 ? -0.494  13.807 2.989   1.00 20.49 ?  145 TYR A CA    1 
ATOM   1139 C C     . TYR A 1 145 ? 0.358   13.363 4.169   1.00 23.10 ?  145 TYR A C     1 
ATOM   1140 O O     . TYR A 1 145 ? 1.560   13.139 4.001   1.00 22.74 ?  145 TYR A O     1 
ATOM   1141 C CB    . TYR A 1 145 ? -0.479  15.345 2.883   1.00 16.56 ?  145 TYR A CB    1 
ATOM   1142 C CG    . TYR A 1 145 ? 0.870   15.958 2.468   1.00 21.04 ?  145 TYR A CG    1 
ATOM   1143 C CD1   . TYR A 1 145 ? 1.184   16.140 1.129   1.00 21.61 ?  145 TYR A CD1   1 
ATOM   1144 C CD2   . TYR A 1 145 ? 1.812   16.353 3.418   1.00 18.49 ?  145 TYR A CD2   1 
ATOM   1145 C CE1   . TYR A 1 145 ? 2.377   16.706 0.741   1.00 25.55 ?  145 TYR A CE1   1 
ATOM   1146 C CE2   . TYR A 1 145 ? 3.029   16.928 3.032   1.00 23.90 ?  145 TYR A CE2   1 
ATOM   1147 C CZ    . TYR A 1 145 ? 3.301   17.102 1.684   1.00 25.72 ?  145 TYR A CZ    1 
ATOM   1148 O OH    . TYR A 1 145 ? 4.508   17.649 1.257   1.00 27.70 ?  145 TYR A OH    1 
ATOM   1149 N N     . THR A 1 146 ? -0.236  13.215 5.355   1.00 22.58 ?  146 THR A N     1 
ATOM   1150 C CA    . THR A 1 146 ? 0.524   12.980 6.578   1.00 21.56 ?  146 THR A CA    1 
ATOM   1151 C C     . THR A 1 146 ? 0.384   11.581 7.174   1.00 23.55 ?  146 THR A C     1 
ATOM   1152 O O     . THR A 1 146 ? 1.267   11.164 7.931   1.00 22.41 ?  146 THR A O     1 
ATOM   1153 C CB    . THR A 1 146 ? 0.095   13.979 7.660   1.00 23.21 ?  146 THR A CB    1 
ATOM   1154 O OG1   . THR A 1 146 ? -1.307  13.817 7.905   1.00 18.56 ?  146 THR A OG1   1 
ATOM   1155 C CG2   . THR A 1 146 ? 0.364   15.411 7.227   1.00 18.95 ?  146 THR A CG2   1 
ATOM   1156 N N     . THR A 1 147 ? -0.699  10.859 6.877   1.00 21.59 ?  147 THR A N     1 
ATOM   1157 C CA    . THR A 1 147 ? -1.082  9.672  7.638   1.00 23.00 ?  147 THR A CA    1 
ATOM   1158 C C     . THR A 1 147 ? -1.405  8.469  6.743   1.00 24.20 ?  147 THR A C     1 
ATOM   1159 O O     . THR A 1 147 ? -1.976  7.483  7.226   1.00 24.37 ?  147 THR A O     1 
ATOM   1160 C CB    . THR A 1 147 ? -2.286  10.002 8.546   1.00 21.19 ?  147 THR A CB    1 
ATOM   1161 O OG1   . THR A 1 147 ? -2.142  11.326 9.070   1.00 25.11 ?  147 THR A OG1   1 
ATOM   1162 C CG2   . THR A 1 147 ? -2.429  9.019  9.712   1.00 24.85 ?  147 THR A CG2   1 
ATOM   1163 N N     . SER A 1 148 ? -1.078  8.524  5.456   1.00 21.67 ?  148 SER A N     1 
ATOM   1164 C CA    . SER A 1 148 ? -1.209  7.341  4.629   1.00 26.75 ?  148 SER A CA    1 
ATOM   1165 C C     . SER A 1 148 ? -0.092  6.346  4.977   1.00 29.18 ?  148 SER A C     1 
ATOM   1166 O O     . SER A 1 148 ? 0.944   6.726  5.545   1.00 23.49 ?  148 SER A O     1 
ATOM   1167 C CB    . SER A 1 148 ? -1.175  7.713  3.151   1.00 24.48 ?  148 SER A CB    1 
ATOM   1168 O OG    . SER A 1 148 ? 0.016   8.396  2.826   1.00 31.92 ?  148 SER A OG    1 
ATOM   1169 N N     . PRO A 1 149 ? -0.304  5.060  4.696   1.00 27.49 ?  149 PRO A N     1 
ATOM   1170 C CA    . PRO A 1 149 ? 0.657   4.032  5.142   1.00 29.96 ?  149 PRO A CA    1 
ATOM   1171 C C     . PRO A 1 149 ? 2.089   4.360  4.752   1.00 25.67 ?  149 PRO A C     1 
ATOM   1172 O O     . PRO A 1 149 ? 2.984   4.182  5.587   1.00 29.28 ?  149 PRO A O     1 
ATOM   1173 C CB    . PRO A 1 149 ? 0.150   2.746  4.462   1.00 28.02 ?  149 PRO A CB    1 
ATOM   1174 C CG    . PRO A 1 149 ? -1.350  2.950  4.412   1.00 26.34 ?  149 PRO A CG    1 
ATOM   1175 C CD    . PRO A 1 149 ? -1.523  4.451  4.127   1.00 25.73 ?  149 PRO A CD    1 
ATOM   1176 N N     . PRO A 1 150 ? 2.366   4.846  3.526   1.00 23.90 ?  150 PRO A N     1 
ATOM   1177 C CA    . PRO A 1 150 ? 3.769   5.184  3.195   1.00 30.89 ?  150 PRO A CA    1 
ATOM   1178 C C     . PRO A 1 150 ? 4.484   6.077  4.212   1.00 31.21 ?  150 PRO A C     1 
ATOM   1179 O O     . PRO A 1 150 ? 5.682   5.879  4.446   1.00 33.72 ?  150 PRO A O     1 
ATOM   1180 C CB    . PRO A 1 150 ? 3.659   5.871  1.823   1.00 31.48 ?  150 PRO A CB    1 
ATOM   1181 C CG    . PRO A 1 150 ? 2.219   5.799  1.409   1.00 33.16 ?  150 PRO A CG    1 
ATOM   1182 C CD    . PRO A 1 150 ? 1.543   4.814  2.305   1.00 26.82 ?  150 PRO A CD    1 
ATOM   1183 N N     . ARG A 1 151 ? 3.805   7.043  4.831   1.00 26.19 ?  151 ARG A N     1 
ATOM   1184 C CA    . ARG A 1 151 ? 4.472   7.858  5.843   1.00 26.41 ?  151 ARG A CA    1 
ATOM   1185 C C     . ARG A 1 151 ? 4.718   7.091  7.130   1.00 27.64 ?  151 ARG A C     1 
ATOM   1186 O O     . ARG A 1 151 ? 5.701   7.357  7.831   1.00 28.84 ?  151 ARG A O     1 
ATOM   1187 C CB    . ARG A 1 151 ? 3.632   9.088  6.171   1.00 28.54 ?  151 ARG A CB    1 
ATOM   1188 C CG    . ARG A 1 151 ? 3.371   9.951  4.994   1.00 27.96 ?  151 ARG A CG    1 
ATOM   1189 C CD    . ARG A 1 151 ? 4.560   10.844 4.761   1.00 26.11 ?  151 ARG A CD    1 
ATOM   1190 N NE    . ARG A 1 151 ? 4.110   12.052 4.099   1.00 25.59 ?  151 ARG A NE    1 
ATOM   1191 C CZ    . ARG A 1 151 ? 4.829   12.758 3.244   1.00 29.58 ?  151 ARG A CZ    1 
ATOM   1192 N NH1   . ARG A 1 151 ? 6.073   12.415 2.942   1.00 24.92 ?  151 ARG A NH1   1 
ATOM   1193 N NH2   . ARG A 1 151 ? 4.286   13.842 2.685   1.00 22.74 ?  151 ARG A NH2   1 
ATOM   1194 N N     . MET A 1 152 ? 3.814   6.175  7.477   1.00 28.30 ?  152 MET A N     1 
ATOM   1195 C CA    . MET A 1 152 ? 3.844   5.544  8.792   1.00 30.48 ?  152 MET A CA    1 
ATOM   1196 C C     . MET A 1 152 ? 4.980   4.533  8.913   1.00 30.45 ?  152 MET A C     1 
ATOM   1197 O O     . MET A 1 152 ? 5.472   4.273  10.016  1.00 30.10 ?  152 MET A O     1 
ATOM   1198 C CB    . MET A 1 152 ? 2.503   4.864  9.038   1.00 24.22 ?  152 MET A CB    1 
ATOM   1199 C CG    . MET A 1 152 ? 1.363   5.826  9.332   1.00 32.98 ?  152 MET A CG    1 
ATOM   1200 S SD    . MET A 1 152 ? 1.816   7.481  9.904   1.00 27.91 ?  152 MET A SD    1 
ATOM   1201 C CE    . MET A 1 152 ? 1.878   7.117  11.658  1.00 25.76 ?  152 MET A CE    1 
ATOM   1202 N N     . PHE A 1 153 ? 5.388   3.936  7.798   1.00 29.12 ?  153 PHE A N     1 
ATOM   1203 C CA    . PHE A 1 153 ? 6.348   2.845  7.841   1.00 32.70 ?  153 PHE A CA    1 
ATOM   1204 C C     . PHE A 1 153 ? 7.778   3.339  7.966   1.00 36.86 ?  153 PHE A C     1 
ATOM   1205 O O     . PHE A 1 153 ? 8.663   2.579  8.385   1.00 30.20 ?  153 PHE A O     1 
ATOM   1206 C CB    . PHE A 1 153 ? 6.186   1.997  6.592   1.00 30.25 ?  153 PHE A CB    1 
ATOM   1207 C CG    . PHE A 1 153 ? 4.871   1.296  6.509   1.00 27.18 ?  153 PHE A CG    1 
ATOM   1208 C CD1   . PHE A 1 153 ? 4.286   0.761  7.647   1.00 26.07 ?  153 PHE A CD1   1 
ATOM   1209 C CD2   . PHE A 1 153 ? 4.223   1.161  5.294   1.00 27.31 ?  153 PHE A CD2   1 
ATOM   1210 C CE1   . PHE A 1 153 ? 3.076   0.093  7.573   1.00 29.69 ?  153 PHE A CE1   1 
ATOM   1211 C CE2   . PHE A 1 153 ? 3.018   0.499  5.205   1.00 27.59 ?  153 PHE A CE2   1 
ATOM   1212 C CZ    . PHE A 1 153 ? 2.438   -0.041 6.360   1.00 31.44 ?  153 PHE A CZ    1 
ATOM   1213 N N     . GLU A 1 154 ? 8.027   4.598  7.618   1.00 40.43 ?  154 GLU A N     1 
ATOM   1214 C CA    . GLU A 1 154 ? 9.338   5.154  7.913   1.00 45.89 ?  154 GLU A CA    1 
ATOM   1215 C C     . GLU A 1 154 ? 9.489   5.376  9.409   1.00 43.64 ?  154 GLU A C     1 
ATOM   1216 O O     . GLU A 1 154 ? 10.607  5.339  9.935   1.00 48.70 ?  154 GLU A O     1 
ATOM   1217 C CB    . GLU A 1 154 ? 9.546   6.436  7.107   1.00 45.20 ?  154 GLU A CB    1 
ATOM   1218 C CG    . GLU A 1 154 ? 9.842   6.173  5.615   1.00 45.21 ?  154 GLU A CG    1 
ATOM   1219 C CD    . GLU A 1 154 ? 11.205  5.493  5.376   1.00 57.11 ?  154 GLU A CD    1 
ATOM   1220 O OE1   . GLU A 1 154 ? 12.218  5.989  5.929   1.00 56.95 ?  154 GLU A OE1   1 
ATOM   1221 O OE2   . GLU A 1 154 ? 11.271  4.482  4.616   1.00 46.93 -1 154 GLU A OE2   1 
ATOM   1222 N N     . ALA A 1 155 ? 8.361   5.531  10.108  1.00 51.95 ?  155 ALA A N     1 
ATOM   1223 C CA    . ALA A 1 155 ? 8.294   5.673  11.558  1.00 53.57 ?  155 ALA A CA    1 
ATOM   1224 C C     . ALA A 1 155 ? 9.087   6.897  12.008  1.00 57.23 ?  155 ALA A C     1 
ATOM   1225 O O     . ALA A 1 155 ? 8.631   8.033  11.835  1.00 57.78 ?  155 ALA A O     1 
ATOM   1226 C CB    . ALA A 1 155 ? 8.782   4.393  12.252  1.00 45.93 ?  155 ALA A CB    1 
ATOM   1227 N N     . GLU A 1 156 ? 10.276  6.685  12.564  1.00 58.30 ?  156 GLU A N     1 
ATOM   1228 C CA    . GLU A 1 156 ? 11.086  7.791  13.049  1.00 59.70 ?  156 GLU A CA    1 
ATOM   1229 C C     . GLU A 1 156 ? 12.073  8.319  12.020  1.00 55.30 ?  156 GLU A C     1 
ATOM   1230 O O     . GLU A 1 156 ? 12.784  9.278  12.320  1.00 59.57 ?  156 GLU A O     1 
ATOM   1231 C CB    . GLU A 1 156 ? 11.840  7.381  14.311  1.00 62.97 ?  156 GLU A CB    1 
ATOM   1232 C CG    . GLU A 1 156 ? 11.110  7.783  15.577  1.00 66.17 ?  156 GLU A CG    1 
ATOM   1233 C CD    . GLU A 1 156 ? 10.304  6.641  16.167  1.00 69.30 ?  156 GLU A CD    1 
ATOM   1234 O OE1   . GLU A 1 156 ? 9.692   5.881  15.376  1.00 65.84 ?  156 GLU A OE1   1 
ATOM   1235 O OE2   . GLU A 1 156 ? 10.304  6.494  17.416  1.00 68.46 -1 156 GLU A OE2   1 
ATOM   1236 N N     . ASN A 1 157 ? 12.142  7.727  10.826  1.00 57.13 ?  157 ASN A N     1 
ATOM   1237 C CA    . ASN A 1 157 ? 12.966  8.284  9.755   1.00 60.25 ?  157 ASN A CA    1 
ATOM   1238 C C     . ASN A 1 157 ? 12.302  9.448  9.031   1.00 55.74 ?  157 ASN A C     1 
ATOM   1239 O O     . ASN A 1 157 ? 12.948  10.060 8.169   1.00 60.71 ?  157 ASN A O     1 
ATOM   1240 C CB    . ASN A 1 157 ? 13.328  7.214  8.712   1.00 58.96 ?  157 ASN A CB    1 
ATOM   1241 C CG    . ASN A 1 157 ? 14.145  6.086  9.291   1.00 60.56 ?  157 ASN A CG    1 
ATOM   1242 O OD1   . ASN A 1 157 ? 14.457  6.086  10.483  1.00 64.59 ?  157 ASN A OD1   1 
ATOM   1243 N ND2   . ASN A 1 157 ? 14.502  5.118  8.452   1.00 52.24 ?  157 ASN A ND2   1 
ATOM   1244 N N     . LEU A 1 158 ? 11.044  9.764  9.347   1.00 51.64 ?  158 LEU A N     1 
ATOM   1245 C CA    . LEU A 1 158 ? 10.314  10.816 8.643   1.00 53.39 ?  158 LEU A CA    1 
ATOM   1246 C C     . LEU A 1 158 ? 10.804  12.184 9.115   1.00 49.11 ?  158 LEU A C     1 
ATOM   1247 O O     . LEU A 1 158 ? 10.747  12.493 10.310  1.00 52.26 ?  158 LEU A O     1 
ATOM   1248 C CB    . LEU A 1 158 ? 8.807   10.663 8.858   1.00 42.14 ?  158 LEU A CB    1 
ATOM   1249 C CG    . LEU A 1 158 ? 7.998   11.325 7.748   1.00 37.62 ?  158 LEU A CG    1 
ATOM   1250 C CD1   . LEU A 1 158 ? 8.199   10.562 6.466   1.00 42.20 ?  158 LEU A CD1   1 
ATOM   1251 C CD2   . LEU A 1 158 ? 6.527   11.386 8.087   1.00 32.79 ?  158 LEU A CD2   1 
ATOM   1252 N N     . THR A 1 159 ? 11.281  13.002 8.176   1.00 47.19 ?  159 THR A N     1 
ATOM   1253 C CA    . THR A 1 159 ? 11.965  14.252 8.483   1.00 44.80 ?  159 THR A CA    1 
ATOM   1254 C C     . THR A 1 159 ? 11.388  15.408 7.661   1.00 39.90 ?  159 THR A C     1 
ATOM   1255 O O     . THR A 1 159 ? 10.527  15.227 6.795   1.00 36.83 ?  159 THR A O     1 
ATOM   1256 C CB    . THR A 1 159 ? 13.470  14.113 8.222   1.00 49.60 ?  159 THR A CB    1 
ATOM   1257 O OG1   . THR A 1 159 ? 14.166  15.239 8.779   1.00 56.50 ?  159 THR A OG1   1 
ATOM   1258 C CG2   . THR A 1 159 ? 13.724  14.020 6.738   1.00 38.74 ?  159 THR A CG2   1 
ATOM   1259 N N     . GLU A 1 160 ? 11.904  16.609 7.926   1.00 38.00 ?  160 GLU A N     1 
ATOM   1260 C CA    . GLU A 1 160 ? 11.395  17.812 7.275   1.00 36.42 ?  160 GLU A CA    1 
ATOM   1261 C C     . GLU A 1 160 ? 11.506  17.736 5.755   1.00 37.37 ?  160 GLU A C     1 
ATOM   1262 O O     . GLU A 1 160 ? 10.593  18.172 5.041   1.00 30.94 ?  160 GLU A O     1 
ATOM   1263 C CB    . GLU A 1 160 ? 12.143  19.035 7.797   1.00 41.68 ?  160 GLU A CB    1 
ATOM   1264 C CG    . GLU A 1 160 ? 11.656  19.506 9.155   1.00 49.12 ?  160 GLU A CG    1 
ATOM   1265 C CD    . GLU A 1 160 ? 12.597  19.154 10.312  1.00 58.68 ?  160 GLU A CD    1 
ATOM   1266 O OE1   . GLU A 1 160 ? 13.805  19.474 10.212  1.00 62.97 ?  160 GLU A OE1   1 
ATOM   1267 O OE2   . GLU A 1 160 ? 12.123  18.588 11.334  1.00 57.84 -1 160 GLU A OE2   1 
ATOM   1268 N N     . VAL A 1 161 ? 12.617  17.211 5.230   1.00 30.36 ?  161 VAL A N     1 
ATOM   1269 C CA    . VAL A 1 161 ? 12.696  17.128 3.774   1.00 32.58 ?  161 VAL A CA    1 
ATOM   1270 C C     . VAL A 1 161 ? 11.713  16.092 3.267   1.00 29.18 ?  161 VAL A C     1 
ATOM   1271 O O     . VAL A 1 161 ? 11.161  16.241 2.172   1.00 29.98 ?  161 VAL A O     1 
ATOM   1272 C CB    . VAL A 1 161 ? 14.129  16.825 3.274   1.00 35.45 ?  161 VAL A CB    1 
ATOM   1273 C CG1   . VAL A 1 161 ? 15.062  17.989 3.572   1.00 35.33 ?  161 VAL A CG1   1 
ATOM   1274 C CG2   . VAL A 1 161 ? 14.652  15.554 3.863   1.00 37.61 ?  161 VAL A CG2   1 
ATOM   1275 N N     . ASP A 1 162 ? 11.473  15.032 4.048   1.00 29.19 ?  162 ASP A N     1 
ATOM   1276 C CA    . ASP A 1 162 ? 10.494  14.029 3.647   1.00 31.31 ?  162 ASP A CA    1 
ATOM   1277 C C     . ASP A 1 162 ? 9.097   14.629 3.522   1.00 28.75 ?  162 ASP A C     1 
ATOM   1278 O O     . ASP A 1 162 ? 8.330   14.237 2.639   1.00 32.15 ?  162 ASP A O     1 
ATOM   1279 C CB    . ASP A 1 162 ? 10.476  12.870 4.644   1.00 35.95 ?  162 ASP A CB    1 
ATOM   1280 C CG    . ASP A 1 162 ? 11.694  11.951 4.509   1.00 45.82 ?  162 ASP A CG    1 
ATOM   1281 O OD1   . ASP A 1 162 ? 12.098  11.634 3.363   1.00 45.63 -1 162 ASP A OD1   1 
ATOM   1282 O OD2   . ASP A 1 162 ? 12.235  11.535 5.560   1.00 43.77 ?  162 ASP A OD2   1 
ATOM   1283 N N     . LEU A 1 163 ? 8.758   15.594 4.371   1.00 27.11 ?  163 LEU A N     1 
ATOM   1284 C CA    . LEU A 1 163 ? 7.424   16.183 4.359   1.00 29.35 ?  163 LEU A CA    1 
ATOM   1285 C C     . LEU A 1 163 ? 7.284   17.362 3.394   1.00 33.32 ?  163 LEU A C     1 
ATOM   1286 O O     . LEU A 1 163 ? 6.179   17.907 3.268   1.00 29.66 ?  163 LEU A O     1 
ATOM   1287 C CB    . LEU A 1 163 ? 7.031   16.591 5.784   1.00 30.75 ?  163 LEU A CB    1 
ATOM   1288 C CG    . LEU A 1 163 ? 6.584   15.358 6.591   1.00 34.63 ?  163 LEU A CG    1 
ATOM   1289 C CD1   . LEU A 1 163 ? 6.931   15.461 8.054   1.00 31.61 ?  163 LEU A CD1   1 
ATOM   1290 C CD2   . LEU A 1 163 ? 5.079   15.101 6.423   1.00 22.45 ?  163 LEU A CD2   1 
ATOM   1291 N N     . MET A 1 164 ? 8.354   17.750 2.681   1.00 29.45 ?  164 MET A N     1 
ATOM   1292 C CA    . MET A 1 164 ? 8.216   18.657 1.540   1.00 33.58 ?  164 MET A CA    1 
ATOM   1293 C C     . MET A 1 164 ? 7.744   17.955 0.271   1.00 31.53 ?  164 MET A C     1 
ATOM   1294 O O     . MET A 1 164 ? 7.422   18.634 -0.709  1.00 31.65 ?  164 MET A O     1 
ATOM   1295 C CB    . MET A 1 164 ? 9.538   19.376 1.224   1.00 28.95 ?  164 MET A CB    1 
ATOM   1296 C CG    . MET A 1 164 ? 10.060  20.235 2.352   1.00 35.15 ?  164 MET A CG    1 
ATOM   1297 S SD    . MET A 1 164 ? 9.406   21.921 2.342   1.00 35.52 ?  164 MET A SD    1 
ATOM   1298 C CE    . MET A 1 164 ? 10.141  22.642 0.873   1.00 34.19 ?  164 MET A CE    1 
ATOM   1299 N N     . LYS A 1 165 ? 7.720   16.633 0.253   1.00 30.13 ?  165 LYS A N     1 
ATOM   1300 C CA    . LYS A 1 165 ? 7.208   15.883 -0.882  1.00 32.26 ?  165 LYS A CA    1 
ATOM   1301 C C     . LYS A 1 165 ? 5.964   15.106 -0.465  1.00 32.19 ?  165 LYS A C     1 
ATOM   1302 O O     . LYS A 1 165 ? 5.852   14.687 0.692   1.00 31.93 ?  165 LYS A O     1 
ATOM   1303 C CB    . LYS A 1 165 ? 8.262   14.902 -1.413  1.00 36.88 ?  165 LYS A CB    1 
ATOM   1304 C CG    . LYS A 1 165 ? 9.697   15.371 -1.184  1.00 40.67 ?  165 LYS A CG    1 
ATOM   1305 C CD    . LYS A 1 165 ? 10.684  14.644 -2.080  1.00 47.74 ?  165 LYS A CD    1 
ATOM   1306 C CE    . LYS A 1 165 ? 11.900  14.175 -1.296  1.00 44.44 ?  165 LYS A CE    1 
ATOM   1307 N NZ    . LYS A 1 165 ? 12.508  12.974 -1.926  1.00 41.93 ?  165 LYS A NZ    1 
ATOM   1308 N N     . PRO A 1 166 ? 5.014   14.893 -1.366  1.00 30.57 ?  166 PRO A N     1 
ATOM   1309 C CA    . PRO A 1 166 ? 3.831   14.104 -1.008  1.00 34.02 ?  166 PRO A CA    1 
ATOM   1310 C C     . PRO A 1 166 ? 4.219   12.649 -0.834  1.00 36.05 ?  166 PRO A C     1 
ATOM   1311 O O     . PRO A 1 166 ? 5.294   12.234 -1.289  1.00 35.12 ?  166 PRO A O     1 
ATOM   1312 C CB    . PRO A 1 166 ? 2.893   14.299 -2.208  1.00 26.57 ?  166 PRO A CB    1 
ATOM   1313 C CG    . PRO A 1 166 ? 3.829   14.556 -3.352  1.00 34.87 ?  166 PRO A CG    1 
ATOM   1314 C CD    . PRO A 1 166 ? 5.017   15.290 -2.785  1.00 32.50 ?  166 PRO A CD    1 
ATOM   1315 N N     . PRO A 1 167 ? 3.398   11.851 -0.161  1.00 33.34 ?  167 PRO A N     1 
ATOM   1316 C CA    . PRO A 1 167 ? 3.673   10.411 -0.092  1.00 29.53 ?  167 PRO A CA    1 
ATOM   1317 C C     . PRO A 1 167 ? 3.517   9.768  -1.461  1.00 36.66 ?  167 PRO A C     1 
ATOM   1318 O O     . PRO A 1 167 ? 2.982   10.358 -2.407  1.00 34.04 ?  167 PRO A O     1 
ATOM   1319 C CB    . PRO A 1 167 ? 2.625   9.880  0.891   1.00 31.50 ?  167 PRO A CB    1 
ATOM   1320 C CG    . PRO A 1 167 ? 1.555   10.930 0.923   1.00 27.30 ?  167 PRO A CG    1 
ATOM   1321 C CD    . PRO A 1 167 ? 2.230   12.240 0.648   1.00 25.01 ?  167 PRO A CD    1 
ATOM   1322 N N     . LYS A 1 168 ? 3.981   8.519  -1.548  1.00 33.55 ?  168 LYS A N     1 
ATOM   1323 C CA    . LYS A 1 168 ? 3.913   7.779  -2.803  1.00 34.58 ?  168 LYS A CA    1 
ATOM   1324 C C     . LYS A 1 168 ? 2.465   7.607  -3.248  1.00 32.28 ?  168 LYS A C     1 
ATOM   1325 O O     . LYS A 1 168 ? 1.610   7.169  -2.467  1.00 31.18 ?  168 LYS A O     1 
ATOM   1326 C CB    . LYS A 1 168 ? 4.587   6.413  -2.641  1.00 35.85 ?  168 LYS A CB    1 
ATOM   1327 C CG    . LYS A 1 168 ? 4.487   5.517  -3.875  1.00 38.69 ?  168 LYS A CG    1 
ATOM   1328 C CD    . LYS A 1 168 ? 5.790   5.497  -4.666  1.00 52.94 ?  168 LYS A CD    1 
ATOM   1329 C CE    . LYS A 1 168 ? 5.546   5.236  -6.154  1.00 54.38 ?  168 LYS A CE    1 
ATOM   1330 N NZ    . LYS A 1 168 ? 6.475   6.007  -7.036  1.00 54.27 ?  168 LYS A NZ    1 
ATOM   1331 N N     . GLY A 1 169 ? 2.191   7.964  -4.504  1.00 31.39 ?  169 GLY A N     1 
ATOM   1332 C CA    . GLY A 1 169 ? 0.864   7.822  -5.078  1.00 26.33 ?  169 GLY A CA    1 
ATOM   1333 C C     . GLY A 1 169 ? -0.101  8.954  -4.787  1.00 29.75 ?  169 GLY A C     1 
ATOM   1334 O O     . GLY A 1 169 ? -1.266  8.866  -5.196  1.00 28.31 ?  169 GLY A O     1 
ATOM   1335 N N     . TYR A 1 170 ? 0.333   9.999  -4.086  1.00 26.82 ?  170 TYR A N     1 
ATOM   1336 C CA    . TYR A 1 170 ? -0.543  11.120 -3.759  1.00 26.44 ?  170 TYR A CA    1 
ATOM   1337 C C     . TYR A 1 170 ? -1.078  11.759 -5.038  1.00 28.67 ?  170 TYR A C     1 
ATOM   1338 O O     . TYR A 1 170 ? -0.313  12.001 -5.974  1.00 29.39 ?  170 TYR A O     1 
ATOM   1339 C CB    . TYR A 1 170 ? 0.223   12.159 -2.936  1.00 26.54 ?  170 TYR A CB    1 
ATOM   1340 C CG    . TYR A 1 170 ? -0.608  13.229 -2.233  1.00 25.68 ?  170 TYR A CG    1 
ATOM   1341 C CD1   . TYR A 1 170 ? -1.202  12.979 -1.001  1.00 24.16 ?  170 TYR A CD1   1 
ATOM   1342 C CD2   . TYR A 1 170 ? -0.790  14.490 -2.802  1.00 23.75 ?  170 TYR A CD2   1 
ATOM   1343 C CE1   . TYR A 1 170 ? -1.953  13.959 -0.353  1.00 21.50 ?  170 TYR A CE1   1 
ATOM   1344 C CE2   . TYR A 1 170 ? -1.541  15.476 -2.158  1.00 22.43 ?  170 TYR A CE2   1 
ATOM   1345 C CZ    . TYR A 1 170 ? -2.101  15.210 -0.927  1.00 19.06 ?  170 TYR A CZ    1 
ATOM   1346 O OH    . TYR A 1 170 ? -2.852  16.183 -0.272  1.00 24.03 ?  170 TYR A OH    1 
ATOM   1347 N N     . PRO A 1 171 ? -2.373  12.082 -5.098  1.00 28.70 ?  171 PRO A N     1 
ATOM   1348 C CA    . PRO A 1 171 ? -2.991  12.406 -6.394  1.00 25.87 ?  171 PRO A CA    1 
ATOM   1349 C C     . PRO A 1 171 ? -2.773  13.821 -6.919  1.00 28.41 ?  171 PRO A C     1 
ATOM   1350 O O     . PRO A 1 171 ? -3.138  14.075 -8.077  1.00 30.17 ?  171 PRO A O     1 
ATOM   1351 C CB    . PRO A 1 171 ? -4.485  12.148 -6.143  1.00 25.29 ?  171 PRO A CB    1 
ATOM   1352 C CG    . PRO A 1 171 ? -4.659  12.281 -4.666  1.00 24.17 ?  171 PRO A CG    1 
ATOM   1353 C CD    . PRO A 1 171 ? -3.370  11.803 -4.047  1.00 24.92 ?  171 PRO A CD    1 
ATOM   1354 N N     . THR A 1 172 ? -2.220  14.760 -6.147  1.00 26.87 ?  172 THR A N     1 
ATOM   1355 C CA    . THR A 1 172 ? -2.050  16.121 -6.655  1.00 29.19 ?  172 THR A CA    1 
ATOM   1356 C C     . THR A 1 172 ? -0.713  16.672 -6.189  1.00 27.86 ?  172 THR A C     1 
ATOM   1357 O O     . THR A 1 172 ? 0.017   16.041 -5.425  1.00 29.05 ?  172 THR A O     1 
ATOM   1358 C CB    . THR A 1 172 ? -3.179  17.087 -6.227  1.00 26.62 ?  172 THR A CB    1 
ATOM   1359 O OG1   . THR A 1 172 ? -3.022  17.432 -4.846  1.00 26.10 ?  172 THR A OG1   1 
ATOM   1360 C CG2   . THR A 1 172 ? -4.577  16.490 -6.456  1.00 26.78 ?  172 THR A CG2   1 
ATOM   1361 N N     . SER A 1 173 ? -0.386  17.863 -6.673  1.00 31.23 ?  173 SER A N     1 
ATOM   1362 C CA    . SER A 1 173 ? 0.902   18.476 -6.383  1.00 30.45 ?  173 SER A CA    1 
ATOM   1363 C C     . SER A 1 173 ? 0.673   19.859 -5.809  1.00 30.74 ?  173 SER A C     1 
ATOM   1364 O O     . SER A 1 173 ? -0.063  20.657 -6.397  1.00 27.00 ?  173 SER A O     1 
ATOM   1365 C CB    . SER A 1 173 ? 1.779   18.585 -7.638  1.00 32.86 ?  173 SER A CB    1 
ATOM   1366 O OG    . SER A 1 173 ? 1.456   17.587 -8.585  1.00 36.20 ?  173 SER A OG    1 
ATOM   1367 N N     . PHE A 1 174 ? 1.291   20.130 -4.659  1.00 26.24 ?  174 PHE A N     1 
ATOM   1368 C CA    . PHE A 1 174 ? 1.445   21.491 -4.171  1.00 30.90 ?  174 PHE A CA    1 
ATOM   1369 C C     . PHE A 1 174 ? 2.746   21.571 -3.385  1.00 32.65 ?  174 PHE A C     1 
ATOM   1370 O O     . PHE A 1 174 ? 3.327   20.554 -2.995  1.00 31.42 ?  174 PHE A O     1 
ATOM   1371 C CB    . PHE A 1 174 ? 0.250   21.945 -3.312  1.00 34.59 ?  174 PHE A CB    1 
ATOM   1372 C CG    . PHE A 1 174 ? -0.161  20.952 -2.258  1.00 26.85 ?  174 PHE A CG    1 
ATOM   1373 C CD1   . PHE A 1 174 ? 0.549   20.846 -1.075  1.00 25.90 ?  174 PHE A CD1   1 
ATOM   1374 C CD2   . PHE A 1 174 ? -1.247  20.124 -2.458  1.00 28.13 ?  174 PHE A CD2   1 
ATOM   1375 C CE1   . PHE A 1 174 ? 0.177   19.941 -0.108  1.00 24.48 ?  174 PHE A CE1   1 
ATOM   1376 C CE2   . PHE A 1 174 ? -1.629  19.217 -1.488  1.00 31.74 ?  174 PHE A CE2   1 
ATOM   1377 C CZ    . PHE A 1 174 ? -0.907  19.126 -0.309  1.00 22.69 ?  174 PHE A CZ    1 
ATOM   1378 N N     . ASN A 1 175 ? 3.203   22.795 -3.160  1.00 30.41 ?  175 ASN A N     1 
ATOM   1379 C CA    . ASN A 1 175 ? 4.474   23.040 -2.502  1.00 29.87 ?  175 ASN A CA    1 
ATOM   1380 C C     . ASN A 1 175 ? 4.211   23.569 -1.107  1.00 28.24 ?  175 ASN A C     1 
ATOM   1381 O O     . ASN A 1 175 ? 3.349   24.432 -0.916  1.00 33.70 ?  175 ASN A O     1 
ATOM   1382 C CB    . ASN A 1 175 ? 5.326   24.040 -3.294  1.00 31.26 ?  175 ASN A CB    1 
ATOM   1383 C CG    . ASN A 1 175 ? 5.605   23.570 -4.716  1.00 36.57 ?  175 ASN A CG    1 
ATOM   1384 O OD1   . ASN A 1 175 ? 5.919   22.401 -4.946  1.00 37.39 ?  175 ASN A OD1   1 
ATOM   1385 N ND2   . ASN A 1 175 ? 5.476   24.475 -5.674  1.00 38.32 ?  175 ASN A ND2   1 
ATOM   1386 N N     . LEU A 1 176 ? 4.945   23.045 -0.143  1.00 27.57 ?  176 LEU A N     1 
ATOM   1387 C CA    . LEU A 1 176 ? 4.972   23.579 1.205   1.00 27.93 ?  176 LEU A CA    1 
ATOM   1388 C C     . LEU A 1 176 ? 6.217   24.436 1.384   1.00 28.16 ?  176 LEU A C     1 
ATOM   1389 O O     . LEU A 1 176 ? 7.261   24.178 0.780   1.00 25.47 ?  176 LEU A O     1 
ATOM   1390 C CB    . LEU A 1 176 ? 4.991   22.468 2.253   1.00 26.00 ?  176 LEU A CB    1 
ATOM   1391 C CG    . LEU A 1 176 ? 3.806   21.518 2.401   1.00 28.47 ?  176 LEU A CG    1 
ATOM   1392 C CD1   . LEU A 1 176 ? 3.959   20.778 3.721   1.00 26.41 ?  176 LEU A CD1   1 
ATOM   1393 C CD2   . LEU A 1 176 ? 2.481   22.267 2.346   1.00 23.27 ?  176 LEU A CD2   1 
ATOM   1394 N N     . GLN A 1 177 ? 6.104   25.445 2.240   1.00 26.05 ?  177 GLN A N     1 
ATOM   1395 C CA    . GLN A 1 177 ? 7.291   26.179 2.636   1.00 24.14 ?  177 GLN A CA    1 
ATOM   1396 C C     . GLN A 1 177 ? 8.059   25.407 3.703   1.00 26.52 ?  177 GLN A C     1 
ATOM   1397 O O     . GLN A 1 177 ? 7.503   24.603 4.456   1.00 24.11 ?  177 GLN A O     1 
ATOM   1398 C CB    . GLN A 1 177 ? 6.924   27.570 3.153   1.00 25.86 ?  177 GLN A CB    1 
ATOM   1399 C CG    . GLN A 1 177 ? 6.330   28.459 2.098   1.00 25.91 ?  177 GLN A CG    1 
ATOM   1400 C CD    . GLN A 1 177 ? 6.087   29.876 2.574   1.00 28.16 ?  177 GLN A CD    1 
ATOM   1401 O OE1   . GLN A 1 177 ? 5.089   30.160 3.244   1.00 29.97 ?  177 GLN A OE1   1 
ATOM   1402 N NE2   . GLN A 1 177 ? 6.982   30.783 2.202   1.00 29.29 ?  177 GLN A NE2   1 
ATOM   1403 N N     . SER A 1 178 ? 9.359   25.698 3.775   1.00 24.52 ?  178 SER A N     1 
ATOM   1404 C CA    . SER A 1 178 ? 10.251  25.042 4.724   1.00 23.47 ?  178 SER A CA    1 
ATOM   1405 C C     . SER A 1 178 ? 9.725   25.080 6.163   1.00 24.52 ?  178 SER A C     1 
ATOM   1406 O O     . SER A 1 178 ? 9.792   24.076 6.881   1.00 25.14 ?  178 SER A O     1 
ATOM   1407 C CB    . SER A 1 178 ? 11.641  25.694 4.638   1.00 27.43 ?  178 SER A CB    1 
ATOM   1408 O OG    . SER A 1 178 ? 12.312  25.592 5.876   1.00 32.45 ?  178 SER A OG    1 
ATOM   1409 N N     . HIS A 1 179 ? 9.236   26.238 6.623   1.00 22.74 ?  179 HIS A N     1 
ATOM   1410 C CA    . HIS A 1 179 ? 8.736   26.317 7.999   1.00 21.26 ?  179 HIS A CA    1 
ATOM   1411 C C     . HIS A 1 179 ? 7.469   25.479 8.193   1.00 23.70 ?  179 HIS A C     1 
ATOM   1412 O O     . HIS A 1 179 ? 7.188   25.040 9.313   1.00 21.48 ?  179 HIS A O     1 
ATOM   1413 C CB    . HIS A 1 179 ? 8.483   27.780 8.410   1.00 21.88 ?  179 HIS A CB    1 
ATOM   1414 C CG    . HIS A 1 179 ? 7.273   28.411 7.783   1.00 21.63 ?  179 HIS A CG    1 
ATOM   1415 N ND1   . HIS A 1 179 ? 7.307   29.045 6.558   1.00 22.93 ?  179 HIS A ND1   1 
ATOM   1416 C CD2   . HIS A 1 179 ? 5.998   28.526 8.226   1.00 23.46 ?  179 HIS A CD2   1 
ATOM   1417 C CE1   . HIS A 1 179 ? 6.104   29.513 6.269   1.00 23.42 ?  179 HIS A CE1   1 
ATOM   1418 N NE2   . HIS A 1 179 ? 5.291   29.209 7.265   1.00 23.98 ?  179 HIS A NE2   1 
ATOM   1419 N N     . GLU A 1 180 ? 6.703   25.245 7.119   1.00 22.61 ?  180 GLU A N     1 
ATOM   1420 C CA    . GLU A 1 180 ? 5.504   24.416 7.217   1.00 23.06 ?  180 GLU A CA    1 
ATOM   1421 C C     . GLU A 1 180 ? 5.865   22.943 7.331   1.00 25.43 ?  180 GLU A C     1 
ATOM   1422 O O     . GLU A 1 180 ? 5.290   22.210 8.152   1.00 23.33 ?  180 GLU A O     1 
ATOM   1423 C CB    . GLU A 1 180 ? 4.595   24.676 6.012   1.00 22.64 ?  180 GLU A CB    1 
ATOM   1424 C CG    . GLU A 1 180 ? 3.975   26.074 6.043   1.00 25.70 ?  180 GLU A CG    1 
ATOM   1425 C CD    . GLU A 1 180 ? 3.403   26.526 4.705   1.00 26.09 ?  180 GLU A CD    1 
ATOM   1426 O OE1   . GLU A 1 180 ? 3.781   25.964 3.660   1.00 26.51 ?  180 GLU A OE1   1 
ATOM   1427 O OE2   . GLU A 1 180 ? 2.561   27.458 4.700   1.00 31.12 -1 180 GLU A OE2   1 
ATOM   1428 N N     . ALA A 1 181 ? 6.829   22.490 6.527   1.00 22.42 ?  181 ALA A N     1 
ATOM   1429 C CA    . ALA A 1 181 ? 7.266   21.105 6.633   1.00 26.20 ?  181 ALA A CA    1 
ATOM   1430 C C     . ALA A 1 181 ? 7.920   20.836 7.981   1.00 27.85 ?  181 ALA A C     1 
ATOM   1431 O O     . ALA A 1 181 ? 7.777   19.735 8.524   1.00 29.10 ?  181 ALA A O     1 
ATOM   1432 C CB    . ALA A 1 181 ? 8.214   20.764 5.482   1.00 26.71 ?  181 ALA A CB    1 
ATOM   1433 N N     . LYS A 1 182 ? 8.598   21.840 8.550   1.00 26.94 ?  182 LYS A N     1 
ATOM   1434 C CA    . LYS A 1 182 ? 9.196   21.700 9.874   1.00 30.18 ?  182 LYS A CA    1 
ATOM   1435 C C     . LYS A 1 182 ? 8.136   21.563 10.955  1.00 26.02 ?  182 LYS A C     1 
ATOM   1436 O O     . LYS A 1 182 ? 8.297   20.772 11.892  1.00 24.68 ?  182 LYS A O     1 
ATOM   1437 C CB    . LYS A 1 182 ? 10.103  22.891 10.179  1.00 30.58 ?  182 LYS A CB    1 
ATOM   1438 C CG    . LYS A 1 182 ? 11.093  22.624 11.298  1.00 37.84 ?  182 LYS A CG    1 
ATOM   1439 C CD    . LYS A 1 182 ? 12.430  23.314 11.022  1.00 47.21 ?  182 LYS A CD    1 
ATOM   1440 C CE    . LYS A 1 182 ? 12.950  22.944 9.635   1.00 50.69 ?  182 LYS A CE    1 
ATOM   1441 N NZ    . LYS A 1 182 ? 14.431  23.088 9.496   1.00 55.01 ?  182 LYS A NZ    1 
ATOM   1442 N N     . HIS A 1 183 ? 7.064   22.352 10.855  1.00 23.83 ?  183 HIS A N     1 
ATOM   1443 C CA    . HIS A 1 183 ? 5.908   22.174 11.728  1.00 26.08 ?  183 HIS A CA    1 
ATOM   1444 C C     . HIS A 1 183 ? 5.355   20.750 11.648  1.00 21.70 ?  183 HIS A C     1 
ATOM   1445 O O     . HIS A 1 183 ? 5.177   20.086 12.673  1.00 25.86 ?  183 HIS A O     1 
ATOM   1446 C CB    . HIS A 1 183 ? 4.820   23.186 11.369  1.00 21.87 ?  183 HIS A CB    1 
ATOM   1447 C CG    . HIS A 1 183 ? 3.670   23.188 12.329  1.00 24.83 ?  183 HIS A CG    1 
ATOM   1448 N ND1   . HIS A 1 183 ? 3.798   23.602 13.639  1.00 23.39 ?  183 HIS A ND1   1 
ATOM   1449 C CD2   . HIS A 1 183 ? 2.378   22.807 12.179  1.00 25.71 ?  183 HIS A CD2   1 
ATOM   1450 C CE1   . HIS A 1 183 ? 2.631   23.493 14.251  1.00 24.35 ?  183 HIS A CE1   1 
ATOM   1451 N NE2   . HIS A 1 183 ? 1.753   23.006 13.389  1.00 23.41 ?  183 HIS A NE2   1 
ATOM   1452 N N     . LEU A 1 184 ? 5.082   20.263 10.437  1.00 22.62 ?  184 LEU A N     1 
ATOM   1453 C CA    . LEU A 1 184 ? 4.523   18.917 10.283  1.00 26.12 ?  184 LEU A CA    1 
ATOM   1454 C C     . LEU A 1 184 ? 5.445   17.844 10.862  1.00 26.17 ?  184 LEU A C     1 
ATOM   1455 O O     . LEU A 1 184 ? 4.977   16.864 11.451  1.00 28.28 ?  184 LEU A O     1 
ATOM   1456 C CB    . LEU A 1 184 ? 4.240   18.625 8.807   1.00 20.82 ?  184 LEU A CB    1 
ATOM   1457 C CG    . LEU A 1 184 ? 3.063   19.361 8.159   1.00 26.99 ?  184 LEU A CG    1 
ATOM   1458 C CD1   . LEU A 1 184 ? 2.936   18.962 6.683   1.00 19.92 ?  184 LEU A CD1   1 
ATOM   1459 C CD2   . LEU A 1 184 ? 1.772   19.064 8.915   1.00 23.50 ?  184 LEU A CD2   1 
ATOM   1460 N N     . ALA A 1 185 ? 6.756   17.992 10.677  1.00 26.41 ?  185 ALA A N     1 
ATOM   1461 C CA    . ALA A 1 185 ? 7.677   16.953 11.120  1.00 26.01 ?  185 ALA A CA    1 
ATOM   1462 C C     . ALA A 1 185 ? 7.773   16.894 12.637  1.00 27.07 ?  185 ALA A C     1 
ATOM   1463 O O     . ALA A 1 185 ? 7.861   15.805 13.211  1.00 29.49 ?  185 ALA A O     1 
ATOM   1464 C CB    . ALA A 1 185 ? 9.065   17.182 10.513  1.00 33.28 ?  185 ALA A CB    1 
ATOM   1465 N N     . SER A 1 186 ? 7.780   18.046 13.308  1.00 27.69 ?  186 SER A N     1 
ATOM   1466 C CA    . SER A 1 186 ? 7.894   17.995 14.762  1.00 31.79 ?  186 SER A CA    1 
ATOM   1467 C C     . SER A 1 186 ? 6.561   17.693 15.443  1.00 31.15 ?  186 SER A C     1 
ATOM   1468 O O     . SER A 1 186 ? 6.527   16.902 16.392  1.00 33.11 ?  186 SER A O     1 
ATOM   1469 C CB    . SER A 1 186 ? 8.482   19.295 15.307  1.00 26.73 ?  186 SER A CB    1 
ATOM   1470 O OG    . SER A 1 186 ? 7.835   20.430 14.779  1.00 35.64 ?  186 SER A OG    1 
ATOM   1471 N N     . THR A 1 187 ? 5.449   18.298 14.989  1.00 28.19 ?  187 THR A N     1 
ATOM   1472 C CA    . THR A 1 187 ? 4.188   18.103 15.711  1.00 25.73 ?  187 THR A CA    1 
ATOM   1473 C C     . THR A 1 187 ? 3.658   16.676 15.584  1.00 22.09 ?  187 THR A C     1 
ATOM   1474 O O     . THR A 1 187 ? 2.969   16.202 16.491  1.00 26.65 ?  187 THR A O     1 
ATOM   1475 C CB    . THR A 1 187 ? 3.123   19.105 15.247  1.00 25.84 ?  187 THR A CB    1 
ATOM   1476 O OG1   . THR A 1 187 ? 2.928   19.002 13.819  1.00 23.32 ?  187 THR A OG1   1 
ATOM   1477 C CG2   . THR A 1 187 ? 3.525   20.530 15.643  1.00 20.63 ?  187 THR A CG2   1 
ATOM   1478 N N     . ARG A 1 188 ? 3.963   15.975 14.488  1.00 24.65 ?  188 ARG A N     1 
ATOM   1479 C CA    . ARG A 1 188 ? 3.410   14.633 14.284  1.00 23.26 ?  188 ARG A CA    1 
ATOM   1480 C C     . ARG A 1 188 ? 3.889   13.637 15.325  1.00 29.31 ?  188 ARG A C     1 
ATOM   1481 O O     . ARG A 1 188 ? 3.201   12.638 15.574  1.00 27.03 ?  188 ARG A O     1 
ATOM   1482 C CB    . ARG A 1 188 ? 3.757   14.101 12.894  1.00 22.25 ?  188 ARG A CB    1 
ATOM   1483 C CG    . ARG A 1 188 ? 5.213   13.632 12.742  1.00 25.58 ?  188 ARG A CG    1 
ATOM   1484 C CD    . ARG A 1 188 ? 5.500   13.235 11.293  1.00 22.99 ?  188 ARG A CD    1 
ATOM   1485 N NE    . ARG A 1 188 ? 4.912   11.935 10.980  1.00 22.96 ?  188 ARG A NE    1 
ATOM   1486 C CZ    . ARG A 1 188 ? 3.920   11.737 10.120  1.00 24.69 ?  188 ARG A CZ    1 
ATOM   1487 N NH1   . ARG A 1 188 ? 3.354   12.742 9.476   1.00 23.77 ?  188 ARG A NH1   1 
ATOM   1488 N NH2   . ARG A 1 188 ? 3.501   10.494 9.884   1.00 23.02 ?  188 ARG A NH2   1 
ATOM   1489 N N     . LYS A 1 189 ? 5.050   13.875 15.937  1.00 25.57 ?  189 LYS A N     1 
ATOM   1490 C CA    . LYS A 1 189 ? 5.539   12.963 16.951  1.00 29.35 ?  189 LYS A CA    1 
ATOM   1491 C C     . LYS A 1 189 ? 5.208   13.423 18.368  1.00 29.63 ?  189 LYS A C     1 
ATOM   1492 O O     . LYS A 1 189 ? 5.412   12.651 19.307  1.00 30.61 ?  189 LYS A O     1 
ATOM   1493 C CB    . LYS A 1 189 ? 7.055   12.734 16.774  1.00 30.57 ?  189 LYS A CB    1 
ATOM   1494 C CG    . LYS A 1 189 ? 7.935   13.901 17.157  1.00 38.19 ?  189 LYS A CG    1 
ATOM   1495 C CD    . LYS A 1 189 ? 9.323   13.800 16.481  1.00 42.54 ?  189 LYS A CD    1 
ATOM   1496 C CE    . LYS A 1 189 ? 10.217  14.983 16.871  1.00 42.16 ?  189 LYS A CE    1 
ATOM   1497 N NZ    . LYS A 1 189 ? 9.393   16.160 17.320  1.00 42.46 ?  189 LYS A NZ    1 
ATOM   1498 N N     . ILE A 1 190 ? 4.637   14.620 18.543  1.00 27.27 ?  190 ILE A N     1 
ATOM   1499 C CA    . ILE A 1 190 ? 4.223   15.056 19.875  1.00 26.46 ?  190 ILE A CA    1 
ATOM   1500 C C     . ILE A 1 190 ? 3.081   14.183 20.372  1.00 28.28 ?  190 ILE A C     1 
ATOM   1501 O O     . ILE A 1 190 ? 2.139   13.871 19.630  1.00 26.52 ?  190 ILE A O     1 
ATOM   1502 C CB    . ILE A 1 190 ? 3.799   16.536 19.885  1.00 28.47 ?  190 ILE A CB    1 
ATOM   1503 C CG1   . ILE A 1 190 ? 4.935   17.465 19.447  1.00 34.05 ?  190 ILE A CG1   1 
ATOM   1504 C CG2   . ILE A 1 190 ? 3.285   16.933 21.254  1.00 26.74 ?  190 ILE A CG2   1 
ATOM   1505 C CD1   . ILE A 1 190 ? 6.344   17.043 19.863  1.00 36.57 ?  190 ILE A CD1   1 
ATOM   1506 N N     . GLU A 1 191 ? 3.145   13.810 21.647  1.00 25.52 ?  191 GLU A N     1 
ATOM   1507 C CA    . GLU A 1 191 ? 2.109   12.987 22.255  1.00 29.12 ?  191 GLU A CA    1 
ATOM   1508 C C     . GLU A 1 191 ? 0.786   13.752 22.351  1.00 31.59 ?  191 GLU A C     1 
ATOM   1509 O O     . GLU A 1 191 ? 0.737   14.887 22.838  1.00 32.60 ?  191 GLU A O     1 
ATOM   1510 C CB    . GLU A 1 191 ? 2.572   12.526 23.639  1.00 34.92 ?  191 GLU A CB    1 
ATOM   1511 C CG    . GLU A 1 191 ? 3.249   11.141 23.615  1.00 36.47 ?  191 GLU A CG    1 
ATOM   1512 C CD    . GLU A 1 191 ? 4.257   10.917 24.748  1.00 48.93 ?  191 GLU A CD    1 
ATOM   1513 O OE1   . GLU A 1 191 ? 3.884   11.120 25.934  1.00 49.40 ?  191 GLU A OE1   1 
ATOM   1514 O OE2   . GLU A 1 191 ? 5.395   10.476 24.460  1.00 48.54 -1 191 GLU A OE2   1 
ATOM   1515 N N     . PHE A 1 192 ? -0.292  13.141 21.868  1.00 27.02 ?  192 PHE A N     1 
ATOM   1516 C CA    . PHE A 1 192 ? -1.620  13.756 21.888  1.00 26.47 ?  192 PHE A CA    1 
ATOM   1517 C C     . PHE A 1 192 ? -2.543  12.805 22.642  1.00 26.87 ?  192 PHE A C     1 
ATOM   1518 O O     . PHE A 1 192 ? -3.267  12.011 22.038  1.00 26.01 ?  192 PHE A O     1 
ATOM   1519 C CB    . PHE A 1 192 ? -2.127  14.039 20.453  1.00 24.85 ?  192 PHE A CB    1 
ATOM   1520 C CG    . PHE A 1 192 ? -3.390  14.876 20.393  1.00 22.85 ?  192 PHE A CG    1 
ATOM   1521 C CD1   . PHE A 1 192 ? -3.366  16.230 20.722  1.00 25.71 ?  192 PHE A CD1   1 
ATOM   1522 C CD2   . PHE A 1 192 ? -4.594  14.315 19.971  1.00 27.77 ?  192 PHE A CD2   1 
ATOM   1523 C CE1   . PHE A 1 192 ? -4.512  17.009 20.656  1.00 22.39 ?  192 PHE A CE1   1 
ATOM   1524 C CE2   . PHE A 1 192 ? -5.764  15.084 19.892  1.00 21.44 ?  192 PHE A CE2   1 
ATOM   1525 C CZ    . PHE A 1 192 ? -5.718  16.441 20.246  1.00 23.31 ?  192 PHE A CZ    1 
ATOM   1526 N N     . GLY A 1 193 ? -2.492  12.868 23.969  1.00 27.59 ?  193 GLY A N     1 
ATOM   1527 C CA    . GLY A 1 193 ? -3.367  12.051 24.789  1.00 30.42 ?  193 GLY A CA    1 
ATOM   1528 C C     . GLY A 1 193 ? -2.820  10.676 25.130  1.00 30.58 ?  193 GLY A C     1 
ATOM   1529 O O     . GLY A 1 193 ? -2.449  9.900  24.240  1.00 27.44 ?  193 GLY A O     1 
ATOM   1530 N N     . SER A 1 194 ? -2.770  10.365 26.429  1.00 31.82 ?  194 SER A N     1 
ATOM   1531 C CA    . SER A 1 194 ? -2.426  9.021  26.903  1.00 33.00 ?  194 SER A CA    1 
ATOM   1532 C C     . SER A 1 194 ? -1.107  8.517  26.320  1.00 32.74 ?  194 SER A C     1 
ATOM   1533 O O     . SER A 1 194 ? -0.950  7.325  26.058  1.00 33.32 ?  194 SER A O     1 
ATOM   1534 C CB    . SER A 1 194 ? -3.558  8.039  26.592  1.00 27.48 ?  194 SER A CB    1 
ATOM   1535 O OG    . SER A 1 194 ? -4.722  8.431  27.272  1.00 28.38 ?  194 SER A OG    1 
ATOM   1536 N N     . GLY A 1 195 ? -0.162  9.425  26.078  1.00 31.20 ?  195 GLY A N     1 
ATOM   1537 C CA    . GLY A 1 195 ? 1.156   9.039  25.619  1.00 32.72 ?  195 GLY A CA    1 
ATOM   1538 C C     . GLY A 1 195 ? 1.264   8.606  24.174  1.00 36.66 ?  195 GLY A C     1 
ATOM   1539 O O     . GLY A 1 195 ? 2.328   8.118  23.774  1.00 34.74 ?  195 GLY A O     1 
ATOM   1540 N N     . ILE A 1 196 ? 0.230   8.804  23.364  1.00 30.84 ?  196 ILE A N     1 
ATOM   1541 C CA    . ILE A 1 196 ? 0.192   8.316  21.985  1.00 29.54 ?  196 ILE A CA    1 
ATOM   1542 C C     . ILE A 1 196 ? 0.617   9.445  21.049  1.00 29.63 ?  196 ILE A C     1 
ATOM   1543 O O     . ILE A 1 196 ? -0.035  10.498 21.038  1.00 29.44 ?  196 ILE A O     1 
ATOM   1544 C CB    . ILE A 1 196 ? -1.204  7.802  21.609  1.00 25.21 ?  196 ILE A CB    1 
ATOM   1545 C CG1   . ILE A 1 196 ? -1.751  6.898  22.718  1.00 31.73 ?  196 ILE A CG1   1 
ATOM   1546 C CG2   . ILE A 1 196 ? -1.161  7.110  20.245  1.00 26.41 ?  196 ILE A CG2   1 
ATOM   1547 C CD1   . ILE A 1 196 ? -1.200  5.493  22.697  1.00 32.37 ?  196 ILE A CD1   1 
ATOM   1548 N N     . PRO A 1 197 ? 1.655   9.261  20.232  1.00 30.11 ?  197 PRO A N     1 
ATOM   1549 C CA    . PRO A 1 197 ? 2.053   10.325 19.304  1.00 27.26 ?  197 PRO A CA    1 
ATOM   1550 C C     . PRO A 1 197 ? 0.925   10.660 18.328  1.00 26.94 ?  197 PRO A C     1 
ATOM   1551 O O     . PRO A 1 197 ? 0.147   9.792  17.921  1.00 19.86 ?  197 PRO A O     1 
ATOM   1552 C CB    . PRO A 1 197 ? 3.274   9.732  18.584  1.00 27.57 ?  197 PRO A CB    1 
ATOM   1553 C CG    . PRO A 1 197 ? 3.777   8.643  19.511  1.00 28.75 ?  197 PRO A CG    1 
ATOM   1554 C CD    . PRO A 1 197 ? 2.536   8.083  20.142  1.00 27.89 ?  197 PRO A CD    1 
ATOM   1555 N N     . PHE A 1 198 ? 0.864   11.939 17.937  1.00 27.99 ?  198 PHE A N     1 
ATOM   1556 C CA    . PHE A 1 198 ? -0.298  12.445 17.205  1.00 26.03 ?  198 PHE A CA    1 
ATOM   1557 C C     . PHE A 1 198 ? -0.580  11.639 15.939  1.00 24.16 ?  198 PHE A C     1 
ATOM   1558 O O     . PHE A 1 198 ? -1.710  11.209 15.720  1.00 21.26 ?  198 PHE A O     1 
ATOM   1559 C CB    . PHE A 1 198 ? -0.138  13.924 16.845  1.00 23.60 ?  198 PHE A CB    1 
ATOM   1560 C CG    . PHE A 1 198 ? -1.368  14.506 16.150  1.00 18.62 ?  198 PHE A CG    1 
ATOM   1561 C CD1   . PHE A 1 198 ? -2.519  14.803 16.871  1.00 21.85 ?  198 PHE A CD1   1 
ATOM   1562 C CD2   . PHE A 1 198 ? -1.366  14.745 14.779  1.00 23.52 ?  198 PHE A CD2   1 
ATOM   1563 C CE1   . PHE A 1 198 ? -3.672  15.341 16.237  1.00 18.43 ?  198 PHE A CE1   1 
ATOM   1564 C CE2   . PHE A 1 198 ? -2.516  15.275 14.137  1.00 25.88 ?  198 PHE A CE2   1 
ATOM   1565 C CZ    . PHE A 1 198 ? -3.664  15.569 14.878  1.00 19.91 ?  198 PHE A CZ    1 
ATOM   1566 N N     . SER A 1 199 ? 0.408   11.447 15.068  1.00 22.65 ?  199 SER A N     1 
ATOM   1567 C CA    . SER A 1 199 ? 0.052   10.764 13.827  1.00 25.96 ?  199 SER A CA    1 
ATOM   1568 C C     . SER A 1 199 ? -0.226  9.276  14.048  1.00 31.01 ?  199 SER A C     1 
ATOM   1569 O O     . SER A 1 199 ? -1.033  8.690  13.308  1.00 27.01 ?  199 SER A O     1 
ATOM   1570 C CB    . SER A 1 199 ? 1.125   10.986 12.769  1.00 29.07 ?  199 SER A CB    1 
ATOM   1571 O OG    . SER A 1 199 ? 0.998   12.311 12.263  1.00 27.66 ?  199 SER A OG    1 
ATOM   1572 N N     . VAL A 1 200 ? 0.370   8.664  15.085  1.00 29.00 ?  200 VAL A N     1 
ATOM   1573 C CA    . VAL A 1 200 ? 0.112   7.246  15.367  1.00 24.48 ?  200 VAL A CA    1 
ATOM   1574 C C     . VAL A 1 200 ? -1.345  7.033  15.779  1.00 21.91 ?  200 VAL A C     1 
ATOM   1575 O O     . VAL A 1 200 ? -2.023  6.151  15.244  1.00 23.74 ?  200 VAL A O     1 
ATOM   1576 C CB    . VAL A 1 200 ? 1.083   6.708  16.431  1.00 23.25 ?  200 VAL A CB    1 
ATOM   1577 C CG1   . VAL A 1 200 ? 0.599   5.335  16.931  1.00 24.62 ?  200 VAL A CG1   1 
ATOM   1578 C CG2   . VAL A 1 200 ? 2.510   6.597  15.859  1.00 23.50 ?  200 VAL A CG2   1 
ATOM   1579 N N     . ARG A 1 201 ? -1.831  7.791  16.770  1.00 19.52 ?  201 ARG A N     1 
ATOM   1580 C CA    . ARG A 1 201 ? -3.267  8.037  16.848  1.00 27.35 ?  201 ARG A CA    1 
ATOM   1581 C C     . ARG A 1 201 ? -3.679  8.654  15.519  1.00 29.57 ?  201 ARG A C     1 
ATOM   1582 O O     . ARG A 1 201 ? -2.901  9.368  14.905  1.00 41.27 ?  201 ARG A O     1 
ATOM   1583 C CB    . ARG A 1 201 ? -3.613  8.981  18.010  1.00 21.38 ?  201 ARG A CB    1 
ATOM   1584 C CG    . ARG A 1 201 ? -5.118  9.208  18.202  1.00 22.63 ?  201 ARG A CG    1 
ATOM   1585 C CD    . ARG A 1 201 ? -5.465  10.281 19.251  1.00 25.36 ?  201 ARG A CD    1 
ATOM   1586 N NE    . ARG A 1 201 ? -4.918  10.019 20.580  1.00 25.06 ?  201 ARG A NE    1 
ATOM   1587 C CZ    . ARG A 1 201 ? -5.515  9.279  21.510  1.00 30.13 ?  201 ARG A CZ    1 
ATOM   1588 N NH1   . ARG A 1 201 ? -6.626  8.613  21.252  1.00 27.38 ?  201 ARG A NH1   1 
ATOM   1589 N NH2   . ARG A 1 201 ? -4.980  9.201  22.732  1.00 23.72 ?  201 ARG A NH2   1 
ATOM   1590 N N     . SER A 1 202 ? -4.871  8.346  15.048  1.00 29.68 ?  202 SER A N     1 
ATOM   1591 C CA    . SER A 1 202 ? -5.304  8.698  13.687  1.00 28.63 ?  202 SER A CA    1 
ATOM   1592 C C     . SER A 1 202 ? -4.999  7.523  12.781  1.00 23.53 ?  202 SER A C     1 
ATOM   1593 O O     . SER A 1 202 ? -5.915  6.924  12.226  1.00 24.80 ?  202 SER A O     1 
ATOM   1594 C CB    . SER A 1 202 ? -4.663  9.964  13.076  1.00 27.57 ?  202 SER A CB    1 
ATOM   1595 O OG    . SER A 1 202 ? -5.256  11.162 13.553  1.00 29.85 ?  202 SER A OG    1 
ATOM   1596 N N     . TYR A 1 203 ? -3.716  7.183  12.637  1.00 27.88 ?  203 TYR A N     1 
ATOM   1597 C CA    . TYR A 1 203 ? -3.368  5.983  11.888  1.00 24.67 ?  203 TYR A CA    1 
ATOM   1598 C C     . TYR A 1 203 ? -4.004  4.750  12.523  1.00 25.49 ?  203 TYR A C     1 
ATOM   1599 O O     . TYR A 1 203 ? -4.612  3.934  11.817  1.00 23.37 ?  203 TYR A O     1 
ATOM   1600 C CB    . TYR A 1 203 ? -1.856  5.850  11.796  1.00 27.49 ?  203 TYR A CB    1 
ATOM   1601 C CG    . TYR A 1 203 ? -1.397  4.704  10.931  1.00 24.20 ?  203 TYR A CG    1 
ATOM   1602 C CD1   . TYR A 1 203 ? -1.673  4.672  9.578   1.00 26.54 ?  203 TYR A CD1   1 
ATOM   1603 C CD2   . TYR A 1 203 ? -0.692  3.642  11.482  1.00 32.05 ?  203 TYR A CD2   1 
ATOM   1604 C CE1   . TYR A 1 203 ? -1.242  3.614  8.779   1.00 28.95 ?  203 TYR A CE1   1 
ATOM   1605 C CE2   . TYR A 1 203 ? -0.270  2.577  10.706  1.00 29.95 ?  203 TYR A CE2   1 
ATOM   1606 C CZ    . TYR A 1 203 ? -0.543  2.569  9.357   1.00 31.24 ?  203 TYR A CZ    1 
ATOM   1607 O OH    . TYR A 1 203 ? -0.104  1.506  8.593   1.00 39.66 ?  203 TYR A OH    1 
ATOM   1608 N N     . ASN A 1 204 ? -3.936  4.640  13.864  1.00 23.75 ?  204 ASN A N     1 
ATOM   1609 C CA    . ASN A 1 204 ? -4.668  3.589  14.579  1.00 23.10 ?  204 ASN A CA    1 
ATOM   1610 C C     . ASN A 1 204 ? -6.167  3.662  14.294  1.00 27.29 ?  204 ASN A C     1 
ATOM   1611 O O     . ASN A 1 204 ? -6.821  2.635  14.077  1.00 26.02 ?  204 ASN A O     1 
ATOM   1612 C CB    . ASN A 1 204 ? -4.436  3.696  16.082  1.00 21.42 ?  204 ASN A CB    1 
ATOM   1613 C CG    . ASN A 1 204 ? -3.028  3.261  16.504  1.00 32.78 ?  204 ASN A CG    1 
ATOM   1614 O OD1   . ASN A 1 204 ? -2.304  2.607  15.749  1.00 29.08 ?  204 ASN A OD1   1 
ATOM   1615 N ND2   . ASN A 1 204 ? -2.642  3.634  17.718  1.00 25.13 ?  204 ASN A ND2   1 
ATOM   1616 N N     . CYS A 1 205 ? -6.735  4.873  14.331  1.00 24.20 ?  205 CYS A N     1 
ATOM   1617 C CA    . CYS A 1 205 ? -8.153  5.051  14.033  1.00 22.44 ?  205 CYS A CA    1 
ATOM   1618 C C     . CYS A 1 205 ? -8.468  4.602  12.618  1.00 24.35 ?  205 CYS A C     1 
ATOM   1619 O O     . CYS A 1 205 ? -9.459  3.896  12.380  1.00 23.81 ?  205 CYS A O     1 
ATOM   1620 C CB    . CYS A 1 205 ? -8.562  6.514  14.204  1.00 24.27 ?  205 CYS A CB    1 
ATOM   1621 S SG    . CYS A 1 205 ? -8.589  7.130  15.890  1.00 22.49 ?  205 CYS A SG    1 
ATOM   1622 N N     . LEU A 1 206 ? -7.652  5.033  11.656  1.00 18.68 ?  206 LEU A N     1 
ATOM   1623 C CA    . LEU A 1 206 ? -7.892  4.631  10.276  1.00 22.32 ?  206 LEU A CA    1 
ATOM   1624 C C     . LEU A 1 206 ? -7.755  3.115  10.108  1.00 24.10 ?  206 LEU A C     1 
ATOM   1625 O O     . LEU A 1 206 ? -8.530  2.492  9.368   1.00 23.51 ?  206 LEU A O     1 
ATOM   1626 C CB    . LEU A 1 206 ? -6.934  5.376  9.348   1.00 19.96 ?  206 LEU A CB    1 
ATOM   1627 C CG    . LEU A 1 206 ? -7.082  6.902  9.205   1.00 19.95 ?  206 LEU A CG    1 
ATOM   1628 C CD1   . LEU A 1 206 ? -5.753  7.530  8.748   1.00 20.13 ?  206 LEU A CD1   1 
ATOM   1629 C CD2   . LEU A 1 206 ? -8.193  7.250  8.195   1.00 17.29 ?  206 LEU A CD2   1 
ATOM   1630 N N     . SER A 1 207 ? -6.776  2.508  10.792  1.00 22.94 ?  207 SER A N     1 
ATOM   1631 C CA    . SER A 1 207 ? -6.504  1.077  10.626  1.00 28.11 ?  207 SER A CA    1 
ATOM   1632 C C     . SER A 1 207 ? -7.594  0.207  11.237  1.00 28.02 ?  207 SER A C     1 
ATOM   1633 O O     . SER A 1 207 ? -7.926  -0.849 10.687  1.00 33.23 ?  207 SER A O     1 
ATOM   1634 C CB    . SER A 1 207 ? -5.160  0.709  11.256  1.00 26.02 ?  207 SER A CB    1 
ATOM   1635 O OG    . SER A 1 207 ? -4.119  1.466  10.672  1.00 30.50 ?  207 SER A OG    1 
ATOM   1636 N N     . LEU A 1 208 ? -8.148  0.614  12.373  1.00 24.69 ?  208 LEU A N     1 
ATOM   1637 C CA    . LEU A 1 208 ? -9.039  -0.249 13.145  1.00 30.23 ?  208 LEU A CA    1 
ATOM   1638 C C     . LEU A 1 208 ? -10.523 0.020  12.929  1.00 29.35 ?  208 LEU A C     1 
ATOM   1639 O O     . LEU A 1 208 ? -11.344 -0.741 13.438  1.00 29.38 ?  208 LEU A O     1 
ATOM   1640 C CB    . LEU A 1 208 ? -8.757  -0.103 14.640  1.00 26.26 ?  208 LEU A CB    1 
ATOM   1641 C CG    . LEU A 1 208 ? -7.420  -0.564 15.194  1.00 32.66 ?  208 LEU A CG    1 
ATOM   1642 C CD1   . LEU A 1 208 ? -7.238  0.021  16.569  1.00 26.83 ?  208 LEU A CD1   1 
ATOM   1643 C CD2   . LEU A 1 208 ? -7.393  -2.083 15.252  1.00 31.90 ?  208 LEU A CD2   1 
ATOM   1644 N N     . THR A 1 209 ? -10.899 1.088  12.240  1.00 25.95 ?  209 THR A N     1 
ATOM   1645 C CA    . THR A 1 209 ? -12.324 1.348  12.114  1.00 24.53 ?  209 THR A CA    1 
ATOM   1646 C C     . THR A 1 209 ? -12.944 0.492  10.998  1.00 25.27 ?  209 THR A C     1 
ATOM   1647 O O     . THR A 1 209 ? -12.259 0.012  10.088  1.00 26.33 ?  209 THR A O     1 
ATOM   1648 C CB    . THR A 1 209 ? -12.567 2.839  11.840  1.00 24.74 ?  209 THR A CB    1 
ATOM   1649 O OG1   . THR A 1 209 ? -13.969 3.127  11.880  1.00 23.83 ?  209 THR A OG1   1 
ATOM   1650 C CG2   . THR A 1 209 ? -12.028 3.209  10.454  1.00 26.15 ?  209 THR A CG2   1 
ATOM   1651 N N     . ASP A 1 210 ? -14.271 0.332  11.066  1.00 28.05 ?  210 ASP A N     1 
ATOM   1652 C CA    . ASP A 1 210 ? -15.000 -0.367 10.009  1.00 24.54 ?  210 ASP A CA    1 
ATOM   1653 C C     . ASP A 1 210 ? -15.033 0.446  8.719   1.00 24.93 ?  210 ASP A C     1 
ATOM   1654 O O     . ASP A 1 210 ? -14.760 -0.080 7.636   1.00 24.49 ?  210 ASP A O     1 
ATOM   1655 C CB    . ASP A 1 210 ? -16.416 -0.688 10.472  1.00 25.89 ?  210 ASP A CB    1 
ATOM   1656 C CG    . ASP A 1 210 ? -16.456 -1.835 11.482  1.00 36.69 ?  210 ASP A CG    1 
ATOM   1657 O OD1   . ASP A 1 210 ? -15.666 -2.798 11.324  1.00 47.47 -1 210 ASP A OD1   1 
ATOM   1658 O OD2   . ASP A 1 210 ? -17.272 -1.783 12.430  1.00 34.41 -1 210 ASP A OD2   1 
ATOM   1659 N N     . ALA A 1 211 ? -15.378 1.729  8.807   1.00 23.66 ?  211 ALA A N     1 
ATOM   1660 C CA    . ALA A 1 211 ? -15.413 2.588  7.629   1.00 26.72 ?  211 ALA A CA    1 
ATOM   1661 C C     . ALA A 1 211 ? -14.949 3.992  8.005   1.00 22.45 ?  211 ALA A C     1 
ATOM   1662 O O     . ALA A 1 211 ? -14.923 4.362  9.180   1.00 20.98 ?  211 ALA A O     1 
ATOM   1663 C CB    . ALA A 1 211 ? -16.818 2.641  7.006   1.00 21.72 ?  211 ALA A CB    1 
ATOM   1664 N N     . ILE A 1 212 ? -14.622 4.779  6.977   1.00 20.08 ?  212 ILE A N     1 
ATOM   1665 C CA    . ILE A 1 212 ? -14.099 6.138  7.101   1.00 21.43 ?  212 ILE A CA    1 
ATOM   1666 C C     . ILE A 1 212 ? -15.032 7.089  6.359   1.00 20.77 ?  212 ILE A C     1 
ATOM   1667 O O     . ILE A 1 212 ? -15.585 6.735  5.316   1.00 21.50 ?  212 ILE A O     1 
ATOM   1668 C CB    . ILE A 1 212 ? -12.672 6.252  6.520   1.00 17.68 ?  212 ILE A CB    1 
ATOM   1669 C CG1   . ILE A 1 212 ? -11.712 5.260  7.195   1.00 19.59 ?  212 ILE A CG1   1 
ATOM   1670 C CG2   . ILE A 1 212 ? -12.133 7.698  6.601   1.00 16.58 ?  212 ILE A CG2   1 
ATOM   1671 C CD1   . ILE A 1 212 ? -10.554 4.857  6.292   1.00 15.54 ?  212 ILE A CD1   1 
ATOM   1672 N N     . GLY A 1 213 ? -15.175 8.305  6.875   1.00 18.76 ?  213 GLY A N     1 
ATOM   1673 C CA    . GLY A 1 213 ? -15.973 9.320  6.210   1.00 18.42 ?  213 GLY A CA    1 
ATOM   1674 C C     . GLY A 1 213 ? -15.353 10.699 6.349   1.00 18.27 ?  213 GLY A C     1 
ATOM   1675 O O     . GLY A 1 213 ? -14.630 10.992 7.310   1.00 15.13 ?  213 GLY A O     1 
ATOM   1676 N N     . PHE A 1 214 ? -15.666 11.554 5.371   1.00 17.11 ?  214 PHE A N     1 
ATOM   1677 C CA    . PHE A 1 214 ? -15.178 12.924 5.284   1.00 14.69 ?  214 PHE A CA    1 
ATOM   1678 C C     . PHE A 1 214 ? -16.309 13.859 4.882   1.00 18.40 ?  214 PHE A C     1 
ATOM   1679 O O     . PHE A 1 214 ? -17.142 13.524 4.030   1.00 14.16 ?  214 PHE A O     1 
ATOM   1680 C CB    . PHE A 1 214 ? -14.050 13.068 4.251   1.00 16.06 ?  214 PHE A CB    1 
ATOM   1681 C CG    . PHE A 1 214 ? -12.724 12.541 4.719   1.00 16.25 ?  214 PHE A CG    1 
ATOM   1682 C CD1   . PHE A 1 214 ? -11.859 13.354 5.425   1.00 17.68 ?  214 PHE A CD1   1 
ATOM   1683 C CD2   . PHE A 1 214 ? -12.352 11.217 4.451   1.00 15.55 ?  214 PHE A CD2   1 
ATOM   1684 C CE1   . PHE A 1 214 ? -10.613 12.876 5.873   1.00 17.06 ?  214 PHE A CE1   1 
ATOM   1685 C CE2   . PHE A 1 214 ? -11.138 10.715 4.896   1.00 18.28 ?  214 PHE A CE2   1 
ATOM   1686 C CZ    . PHE A 1 214 ? -10.251 11.558 5.608   1.00 17.17 ?  214 PHE A CZ    1 
ATOM   1687 N N     . LYS A 1 215 ? -16.326 15.039 5.495   1.00 19.00 ?  215 LYS A N     1 
ATOM   1688 C CA    . LYS A 1 215 ? -16.991 16.184 4.880   1.00 17.39 ?  215 LYS A CA    1 
ATOM   1689 C C     . LYS A 1 215 ? -16.416 16.426 3.487   1.00 20.03 ?  215 LYS A C     1 
ATOM   1690 O O     . LYS A 1 215 ? -15.200 16.362 3.292   1.00 18.93 ?  215 LYS A O     1 
ATOM   1691 C CB    . LYS A 1 215 ? -16.776 17.411 5.758   1.00 19.68 ?  215 LYS A CB    1 
ATOM   1692 C CG    . LYS A 1 215 ? -17.297 18.718 5.217   1.00 19.70 ?  215 LYS A CG    1 
ATOM   1693 C CD    . LYS A 1 215 ? -17.232 19.777 6.325   1.00 18.64 ?  215 LYS A CD    1 
ATOM   1694 C CE    . LYS A 1 215 ? -16.593 21.085 5.849   1.00 19.67 ?  215 LYS A CE    1 
ATOM   1695 N NZ    . LYS A 1 215 ? -17.037 22.245 6.689   1.00 19.53 ?  215 LYS A NZ    1 
ATOM   1696 N N     . GLY A 1 216 ? -17.287 16.705 2.510   1.00 21.08 ?  216 GLY A N     1 
ATOM   1697 C CA    . GLY A 1 216 ? -16.811 16.972 1.158   1.00 18.37 ?  216 GLY A CA    1 
ATOM   1698 C C     . GLY A 1 216 ? -17.652 16.378 0.030   1.00 21.91 ?  216 GLY A C     1 
ATOM   1699 O O     . GLY A 1 216 ? -18.627 15.658 0.275   1.00 20.13 ?  216 GLY A O     1 
ATOM   1700 N N     . CYS A 1 217 ? -17.272 16.669 -1.215  1.00 19.26 ?  217 CYS A N     1 
ATOM   1701 C CA    . CYS A 1 217 ? -17.987 16.202 -2.395  1.00 22.70 ?  217 CYS A CA    1 
ATOM   1702 C C     . CYS A 1 217 ? -16.990 15.658 -3.411  1.00 22.06 ?  217 CYS A C     1 
ATOM   1703 O O     . CYS A 1 217 ? -15.796 15.961 -3.356  1.00 20.98 ?  217 CYS A O     1 
ATOM   1704 C CB    . CYS A 1 217 ? -18.840 17.333 -3.023  1.00 25.12 ?  217 CYS A CB    1 
ATOM   1705 S SG    . CYS A 1 217 ? -17.862 18.700 -3.702  1.00 31.48 ?  217 CYS A SG    1 
ATOM   1706 N N     . ARG A 1 218 ? -17.495 14.841 -4.349  1.00 25.24 ?  218 ARG A N     1 
ATOM   1707 C CA    . ARG A 1 218 ? -16.606 14.206 -5.326  1.00 24.92 ?  218 ARG A CA    1 
ATOM   1708 C C     . ARG A 1 218 ? -15.822 15.230 -6.122  1.00 21.89 ?  218 ARG A C     1 
ATOM   1709 O O     . ARG A 1 218 ? -14.658 14.988 -6.465  1.00 19.27 ?  218 ARG A O     1 
ATOM   1710 C CB    . ARG A 1 218 ? -17.383 13.306 -6.305  1.00 26.10 ?  218 ARG A CB    1 
ATOM   1711 C CG    . ARG A 1 218 ? -18.042 12.081 -5.674  1.00 35.23 ?  218 ARG A CG    1 
ATOM   1712 C CD    . ARG A 1 218 ? -17.102 10.876 -5.498  1.00 33.68 ?  218 ARG A CD    1 
ATOM   1713 N NE    . ARG A 1 218 ? -16.116 10.737 -6.564  1.00 33.47 ?  218 ARG A NE    1 
ATOM   1714 C CZ    . ARG A 1 218 ? -14.919 10.182 -6.404  1.00 40.47 ?  218 ARG A CZ    1 
ATOM   1715 N NH1   . ARG A 1 218 ? -14.562 9.626  -5.254  1.00 37.83 ?  218 ARG A NH1   1 
ATOM   1716 N NH2   . ARG A 1 218 ? -14.046 10.212 -7.414  1.00 32.07 ?  218 ARG A NH2   1 
ATOM   1717 N N     . GLU A 1 219 ? -16.433 16.377 -6.414  1.00 18.53 ?  219 GLU A N     1 
ATOM   1718 C CA    . GLU A 1 219 ? -15.834 17.330 -7.339  1.00 25.01 ?  219 GLU A CA    1 
ATOM   1719 C C     . GLU A 1 219 ? -14.596 18.013 -6.758  1.00 26.71 ?  219 GLU A C     1 
ATOM   1720 O O     . GLU A 1 219 ? -13.754 18.492 -7.528  1.00 30.50 ?  219 GLU A O     1 
ATOM   1721 C CB    . GLU A 1 219 ? -16.881 18.369 -7.763  1.00 23.47 ?  219 GLU A CB    1 
ATOM   1722 C CG    . GLU A 1 219 ? -17.975 17.807 -8.664  1.00 24.87 ?  219 GLU A CG    1 
ATOM   1723 C CD    . GLU A 1 219 ? -19.128 17.130 -7.897  1.00 34.85 ?  219 GLU A CD    1 
ATOM   1724 O OE1   . GLU A 1 219 ? -19.019 16.959 -6.666  1.00 28.48 ?  219 GLU A OE1   1 
ATOM   1725 O OE2   . GLU A 1 219 ? -20.151 16.767 -8.535  1.00 39.17 -1 219 GLU A OE2   1 
ATOM   1726 N N     . ILE A 1 220 ? -14.450 18.047 -5.429  1.00 22.66 ?  220 ILE A N     1 
ATOM   1727 C CA    . ILE A 1 220 ? -13.292 18.648 -4.769  1.00 20.79 ?  220 ILE A CA    1 
ATOM   1728 C C     . ILE A 1 220 ? -12.460 17.601 -4.031  1.00 19.76 ?  220 ILE A C     1 
ATOM   1729 O O     . ILE A 1 220 ? -11.243 17.517 -4.216  1.00 20.27 ?  220 ILE A O     1 
ATOM   1730 C CB    . ILE A 1 220 ? -13.717 19.785 -3.807  1.00 18.92 ?  220 ILE A CB    1 
ATOM   1731 C CG1   . ILE A 1 220 ? -14.428 20.904 -4.573  1.00 22.19 ?  220 ILE A CG1   1 
ATOM   1732 C CG2   . ILE A 1 220 ? -12.500 20.335 -2.977  1.00 18.82 ?  220 ILE A CG2   1 
ATOM   1733 C CD1   . ILE A 1 220 ? -15.592 21.513 -3.824  1.00 24.61 ?  220 ILE A CD1   1 
ATOM   1734 N N     . GLU A 1 221 ? -13.098 16.814 -3.166  1.00 18.03 ?  221 GLU A N     1 
ATOM   1735 C CA    . GLU A 1 221 ? -12.408 15.880 -2.284  1.00 16.61 ?  221 GLU A CA    1 
ATOM   1736 C C     . GLU A 1 221 ? -12.208 14.488 -2.886  1.00 20.20 ?  221 GLU A C     1 
ATOM   1737 O O     . GLU A 1 221 ? -11.404 13.712 -2.350  1.00 24.67 ?  221 GLU A O     1 
ATOM   1738 C CB    . GLU A 1 221 ? -13.171 15.754 -0.961  1.00 18.06 ?  221 GLU A CB    1 
ATOM   1739 C CG    . GLU A 1 221 ? -12.928 16.879 0.023   1.00 16.99 ?  221 GLU A CG    1 
ATOM   1740 C CD    . GLU A 1 221 ? -13.801 18.106 -0.227  1.00 25.93 ?  221 GLU A CD    1 
ATOM   1741 O OE1   . GLU A 1 221 ? -14.671 18.073 -1.138  1.00 24.44 ?  221 GLU A OE1   1 
ATOM   1742 O OE2   . GLU A 1 221 ? -13.629 19.105 0.512   1.00 29.17 -1 221 GLU A OE2   1 
ATOM   1743 N N     . GLY A 1 222 ? -12.893 14.158 -3.982  1.00 21.26 ?  222 GLY A N     1 
ATOM   1744 C CA    . GLY A 1 222 ? -12.826 12.845 -4.605  1.00 21.08 ?  222 GLY A CA    1 
ATOM   1745 C C     . GLY A 1 222 ? -11.451 12.212 -4.785  1.00 25.52 ?  222 GLY A C     1 
ATOM   1746 O O     . GLY A 1 222 ? -11.237 11.058 -4.400  1.00 24.74 ?  222 GLY A O     1 
ATOM   1747 N N     . PRO A 1 223 ? -10.498 12.926 -5.401  1.00 20.33 ?  223 PRO A N     1 
ATOM   1748 C CA    . PRO A 1 223 ? -9.172  12.313 -5.605  1.00 25.35 ?  223 PRO A CA    1 
ATOM   1749 C C     . PRO A 1 223 ? -8.527  11.817 -4.314  1.00 23.19 ?  223 PRO A C     1 
ATOM   1750 O O     . PRO A 1 223 ? -7.882  10.759 -4.317  1.00 20.99 ?  223 PRO A O     1 
ATOM   1751 C CB    . PRO A 1 223 ? -8.355  13.442 -6.266  1.00 25.37 ?  223 PRO A CB    1 
ATOM   1752 C CG    . PRO A 1 223 ? -9.375  14.357 -6.871  1.00 21.79 ?  223 PRO A CG    1 
ATOM   1753 C CD    . PRO A 1 223 ? -10.563 14.290 -5.948  1.00 19.40 ?  223 PRO A CD    1 
ATOM   1754 N N     . TYR A 1 224 ? -8.710  12.541 -3.203  1.00 19.52 ?  224 TYR A N     1 
ATOM   1755 C CA    . TYR A 1 224 ? -8.121  12.155 -1.925  1.00 17.73 ?  224 TYR A CA    1 
ATOM   1756 C C     . TYR A 1 224 ? -8.867  11.000 -1.278  1.00 20.83 ?  224 TYR A C     1 
ATOM   1757 O O     . TYR A 1 224 ? -8.242  10.090 -0.724  1.00 19.43 ?  224 TYR A O     1 
ATOM   1758 C CB    . TYR A 1 224 ? -8.077  13.361 -0.994  1.00 15.69 ?  224 TYR A CB    1 
ATOM   1759 C CG    . TYR A 1 224 ? -7.395  14.543 -1.652  1.00 17.44 ?  224 TYR A CG    1 
ATOM   1760 C CD1   . TYR A 1 224 ? -6.027  14.539 -1.877  1.00 19.74 ?  224 TYR A CD1   1 
ATOM   1761 C CD2   . TYR A 1 224 ? -8.129  15.631 -2.105  1.00 19.80 ?  224 TYR A CD2   1 
ATOM   1762 C CE1   . TYR A 1 224 ? -5.401  15.601 -2.497  1.00 16.82 ?  224 TYR A CE1   1 
ATOM   1763 C CE2   . TYR A 1 224 ? -7.511  16.698 -2.729  1.00 16.36 ?  224 TYR A CE2   1 
ATOM   1764 C CZ    . TYR A 1 224 ? -6.158  16.670 -2.922  1.00 19.23 ?  224 TYR A CZ    1 
ATOM   1765 O OH    . TYR A 1 224 ? -5.561  17.738 -3.534  1.00 25.67 ?  224 TYR A OH    1 
ATOM   1766 N N     . VAL A 1 225 ? -10.195 11.006 -1.354  1.00 20.17 ?  225 VAL A N     1 
ATOM   1767 C CA    . VAL A 1 225 ? -10.977 9.892  -0.823  1.00 21.94 ?  225 VAL A CA    1 
ATOM   1768 C C     . VAL A 1 225 ? -10.673 8.594  -1.593  1.00 22.67 ?  225 VAL A C     1 
ATOM   1769 O O     . VAL A 1 225 ? -10.611 7.503  -1.006  1.00 22.68 ?  225 VAL A O     1 
ATOM   1770 C CB    . VAL A 1 225 ? -12.473 10.275 -0.837  1.00 22.05 ?  225 VAL A CB    1 
ATOM   1771 C CG1   . VAL A 1 225 ? -13.338 9.096  -1.049  1.00 29.37 ?  225 VAL A CG1   1 
ATOM   1772 C CG2   . VAL A 1 225 ? -12.851 11.009 0.484   1.00 20.30 ?  225 VAL A CG2   1 
ATOM   1773 N N     . ASP A 1 226 ? -10.439 8.691  -2.905  1.00 20.80 ?  226 ASP A N     1 
ATOM   1774 C CA    . ASP A 1 226 ? -10.085 7.498  -3.692  1.00 24.25 ?  226 ASP A CA    1 
ATOM   1775 C C     . ASP A 1 226 ? -8.743  6.918  -3.245  1.00 27.57 ?  226 ASP A C     1 
ATOM   1776 O O     . ASP A 1 226 ? -8.596  5.699  -3.060  1.00 27.76 ?  226 ASP A O     1 
ATOM   1777 C CB    . ASP A 1 226 ? -9.997  7.838  -5.177  1.00 22.56 ?  226 ASP A CB    1 
ATOM   1778 C CG    . ASP A 1 226 ? -11.330 8.095  -5.823  1.00 30.52 ?  226 ASP A CG    1 
ATOM   1779 O OD1   . ASP A 1 226 ? -12.376 7.893  -5.188  1.00 31.65 ?  226 ASP A OD1   1 
ATOM   1780 O OD2   . ASP A 1 226 ? -11.324 8.502  -7.007  1.00 37.04 -1 226 ASP A OD2   1 
ATOM   1781 N N     . TYR A 1 227 ? -7.739  7.790  -3.107  1.00 24.06 ?  227 TYR A N     1 
ATOM   1782 C CA    . TYR A 1 227 ? -6.420  7.378  -2.633  1.00 26.82 ?  227 TYR A CA    1 
ATOM   1783 C C     . TYR A 1 227 ? -6.496  6.720  -1.268  1.00 27.73 ?  227 TYR A C     1 
ATOM   1784 O O     . TYR A 1 227 ? -5.881  5.676  -1.044  1.00 25.85 ?  227 TYR A O     1 
ATOM   1785 C CB    . TYR A 1 227 ? -5.510  8.589  -2.580  1.00 26.33 ?  227 TYR A CB    1 
ATOM   1786 C CG    . TYR A 1 227 ? -4.135  8.372  -2.014  1.00 28.88 ?  227 TYR A CG    1 
ATOM   1787 C CD1   . TYR A 1 227 ? -3.133  7.779  -2.785  1.00 30.47 ?  227 TYR A CD1   1 
ATOM   1788 C CD2   . TYR A 1 227 ? -3.807  8.831  -0.742  1.00 27.25 ?  227 TYR A CD2   1 
ATOM   1789 C CE1   . TYR A 1 227 ? -1.857  7.618  -2.299  1.00 27.95 ?  227 TYR A CE1   1 
ATOM   1790 C CE2   . TYR A 1 227 ? -2.518  8.676  -0.240  1.00 26.04 ?  227 TYR A CE2   1 
ATOM   1791 C CZ    . TYR A 1 227 ? -1.553  8.067  -1.026  1.00 28.01 ?  227 TYR A CZ    1 
ATOM   1792 O OH    . TYR A 1 227 ? -0.279  7.909  -0.546  1.00 27.14 ?  227 TYR A OH    1 
ATOM   1793 N N     . LEU A 1 228 ? -7.247  7.311  -0.338  1.00 22.91 ?  228 LEU A N     1 
ATOM   1794 C CA    . LEU A 1 228 ? -7.325  6.713  0.986   1.00 23.10 ?  228 LEU A CA    1 
ATOM   1795 C C     . LEU A 1 228 ? -8.037  5.360  0.928   1.00 25.05 ?  228 LEU A C     1 
ATOM   1796 O O     . LEU A 1 228 ? -7.646  4.408  1.619   1.00 21.20 ?  228 LEU A O     1 
ATOM   1797 C CB    . LEU A 1 228 ? -8.014  7.678  1.947   1.00 22.20 ?  228 LEU A CB    1 
ATOM   1798 C CG    . LEU A 1 228 ? -7.212  8.889  2.458   1.00 20.25 ?  228 LEU A CG    1 
ATOM   1799 C CD1   . LEU A 1 228 ? -8.101  9.817  3.282   1.00 17.73 ?  228 LEU A CD1   1 
ATOM   1800 C CD2   . LEU A 1 228 ? -6.057  8.418  3.295   1.00 21.06 ?  228 LEU A CD2   1 
ATOM   1801 N N     . GLN A 1 229 ? -9.055  5.237  0.074   1.00 26.32 ?  229 GLN A N     1 
ATOM   1802 C CA    . GLN A 1 229 ? -9.769  3.967  -0.008  1.00 27.41 ?  229 GLN A CA    1 
ATOM   1803 C C     . GLN A 1 229 ? -8.868  2.859  -0.551  1.00 26.55 ?  229 GLN A C     1 
ATOM   1804 O O     . GLN A 1 229 ? -8.914  1.724  -0.068  1.00 28.63 ?  229 GLN A O     1 
ATOM   1805 C CB    . GLN A 1 229 ? -11.030 4.112  -0.859  1.00 26.95 ?  229 GLN A CB    1 
ATOM   1806 C CG    . GLN A 1 229 ? -11.914 2.871  -0.770  1.00 27.49 ?  229 GLN A CG    1 
ATOM   1807 C CD    . GLN A 1 229 ? -13.262 3.060  -1.419  1.00 33.95 ?  229 GLN A CD    1 
ATOM   1808 O OE1   . GLN A 1 229 ? -14.122 3.796  -0.911  1.00 33.06 ?  229 GLN A OE1   1 
ATOM   1809 N NE2   . GLN A 1 229 ? -13.469 2.380  -2.543  1.00 41.05 ?  229 GLN A NE2   1 
ATOM   1810 N N     . GLU A 1 230 ? -8.015  3.170  -1.523  1.00 26.98 ?  230 GLU A N     1 
ATOM   1811 C CA    . GLU A 1 230 ? -7.120  2.141  -2.026  1.00 30.99 ?  230 GLU A CA    1 
ATOM   1812 C C     . GLU A 1 230 ? -6.016  1.831  -1.022  1.00 31.10 ?  230 GLU A C     1 
ATOM   1813 O O     . GLU A 1 230 ? -5.606  0.671  -0.904  1.00 28.71 ?  230 GLU A O     1 
ATOM   1814 C CB    . GLU A 1 230 ? -6.554  2.547  -3.394  1.00 31.31 ?  230 GLU A CB    1 
ATOM   1815 C CG    . GLU A 1 230 ? -5.934  3.907  -3.433  1.00 40.62 ?  230 GLU A CG    1 
ATOM   1816 C CD    . GLU A 1 230 ? -4.784  4.042  -4.427  1.00 51.72 ?  230 GLU A CD    1 
ATOM   1817 O OE1   . GLU A 1 230 ? -5.046  4.507  -5.568  1.00 55.51 ?  230 GLU A OE1   1 
ATOM   1818 O OE2   . GLU A 1 230 ? -3.623  3.706  -4.057  1.00 50.84 -1 230 GLU A OE2   1 
ATOM   1819 N N     . GLN A 1 231 ? -5.571  2.833  -0.253  1.00 29.21 ?  231 GLN A N     1 
ATOM   1820 C CA    . GLN A 1 231 ? -4.508  2.629  0.734   1.00 27.71 ?  231 GLN A CA    1 
ATOM   1821 C C     . GLN A 1 231 ? -4.974  1.765  1.902   1.00 28.00 ?  231 GLN A C     1 
ATOM   1822 O O     . GLN A 1 231 ? -4.245  0.873  2.350   1.00 30.24 ?  231 GLN A O     1 
ATOM   1823 C CB    . GLN A 1 231 ? -4.001  3.976  1.259   1.00 24.94 ?  231 GLN A CB    1 
ATOM   1824 C CG    . GLN A 1 231 ? -3.208  4.784  0.251   1.00 28.61 ?  231 GLN A CG    1 
ATOM   1825 C CD    . GLN A 1 231 ? -1.902  4.127  -0.092  1.00 31.64 ?  231 GLN A CD    1 
ATOM   1826 O OE1   . GLN A 1 231 ? -1.254  3.527  0.768   1.00 29.81 ?  231 GLN A OE1   1 
ATOM   1827 N NE2   . GLN A 1 231 ? -1.508  4.221  -1.354  1.00 30.42 ?  231 GLN A NE2   1 
ATOM   1828 N N     . PHE A 1 232 ? -6.170  2.035  2.438   1.00 23.60 ?  232 PHE A N     1 
ATOM   1829 C CA    . PHE A 1 232 ? -6.629  1.352  3.645   1.00 27.43 ?  232 PHE A CA    1 
ATOM   1830 C C     . PHE A 1 232 ? -7.620  0.226  3.367   1.00 24.39 ?  232 PHE A C     1 
ATOM   1831 O O     . PHE A 1 232 ? -7.970  -0.507 4.295   1.00 26.10 ?  232 PHE A O     1 
ATOM   1832 C CB    . PHE A 1 232 ? -7.254  2.359  4.640   1.00 24.60 ?  232 PHE A CB    1 
ATOM   1833 C CG    . PHE A 1 232 ? -6.236  3.241  5.341   1.00 23.24 ?  232 PHE A CG    1 
ATOM   1834 C CD1   . PHE A 1 232 ? -5.594  2.811  6.502   1.00 23.52 ?  232 PHE A CD1   1 
ATOM   1835 C CD2   . PHE A 1 232 ? -5.911  4.491  4.825   1.00 24.87 ?  232 PHE A CD2   1 
ATOM   1836 C CE1   . PHE A 1 232 ? -4.652  3.609  7.135   1.00 26.56 ?  232 PHE A CE1   1 
ATOM   1837 C CE2   . PHE A 1 232 ? -4.966  5.304  5.458   1.00 20.12 ?  232 PHE A CE2   1 
ATOM   1838 C CZ    . PHE A 1 232 ? -4.338  4.866  6.602   1.00 22.48 ?  232 PHE A CZ    1 
ATOM   1839 N N     . GLY A 1 233 ? -8.082  0.080  2.130   1.00 27.85 ?  233 GLY A N     1 
ATOM   1840 C CA    . GLY A 1 233 ? -8.859  -1.079 1.741   1.00 31.87 ?  233 GLY A CA    1 
ATOM   1841 C C     . GLY A 1 233 ? -10.254 -1.165 2.313   1.00 33.70 ?  233 GLY A C     1 
ATOM   1842 O O     . GLY A 1 233 ? -10.865 -2.231 2.258   1.00 33.91 ?  233 GLY A O     1 
ATOM   1843 N N     . LYS A 1 234 ? -10.781 -0.086 2.862   1.00 28.56 ?  234 LYS A N     1 
ATOM   1844 C CA    . LYS A 1 234 ? -12.119 -0.063 3.432   1.00 27.62 ?  234 LYS A CA    1 
ATOM   1845 C C     . LYS A 1 234 ? -12.875 1.129  2.861   1.00 28.66 ?  234 LYS A C     1 
ATOM   1846 O O     . LYS A 1 234 ? -12.276 2.000  2.222   1.00 26.72 ?  234 LYS A O     1 
ATOM   1847 C CB    . LYS A 1 234 ? -12.056 0.006  4.966   1.00 27.95 ?  234 LYS A CB    1 
ATOM   1848 C CG    . LYS A 1 234 ? -11.231 1.176  5.511   1.00 30.26 ?  234 LYS A CG    1 
ATOM   1849 C CD    . LYS A 1 234 ? -11.123 1.108  7.038   1.00 26.49 ?  234 LYS A CD    1 
ATOM   1850 C CE    . LYS A 1 234 ? -10.177 0.010  7.465   1.00 26.69 ?  234 LYS A CE    1 
ATOM   1851 N NZ    . LYS A 1 234 ? -9.901  0.040  8.922   1.00 23.97 ?  234 LYS A NZ    1 
ATOM   1852 N N     . PRO A 1 235 ? -14.199 1.172  3.015   1.00 29.22 ?  235 PRO A N     1 
ATOM   1853 C CA    . PRO A 1 235 ? -14.959 2.266  2.386   1.00 24.00 ?  235 PRO A CA    1 
ATOM   1854 C C     . PRO A 1 235 ? -14.583 3.613  2.986   1.00 22.74 ?  235 PRO A C     1 
ATOM   1855 O O     . PRO A 1 235 ? -14.474 3.752  4.204   1.00 21.70 ?  235 PRO A O     1 
ATOM   1856 C CB    . PRO A 1 235 ? -16.422 1.903  2.681   1.00 22.75 ?  235 PRO A CB    1 
ATOM   1857 C CG    . PRO A 1 235 ? -16.411 0.409  2.845   1.00 24.60 ?  235 PRO A CG    1 
ATOM   1858 C CD    . PRO A 1 235 ? -15.082 0.085  3.490   1.00 25.11 ?  235 PRO A CD    1 
ATOM   1859 N N     . VAL A 1 236 ? -14.380 4.608  2.116   1.00 21.05 ?  236 VAL A N     1 
ATOM   1860 C CA    . VAL A 1 236 ? -14.146 5.992  2.523   1.00 20.43 ?  236 VAL A CA    1 
ATOM   1861 C C     . VAL A 1 236 ? -15.280 6.806  1.912   1.00 23.26 ?  236 VAL A C     1 
ATOM   1862 O O     . VAL A 1 236 ? -15.337 6.984  0.687   1.00 20.66 ?  236 VAL A O     1 
ATOM   1863 C CB    . VAL A 1 236 ? -12.762 6.517  2.092   1.00 21.73 ?  236 VAL A CB    1 
ATOM   1864 C CG1   . VAL A 1 236 ? -12.548 7.942  2.579   1.00 22.14 ?  236 VAL A CG1   1 
ATOM   1865 C CG2   . VAL A 1 236 ? -11.633 5.651  2.671   1.00 20.71 ?  236 VAL A CG2   1 
ATOM   1866 N N     . LEU A 1 237 ? -16.204 7.265  2.751   1.00 19.19 ?  237 LEU A N     1 
ATOM   1867 C CA    . LEU A 1 237 ? -17.418 7.913  2.277   1.00 25.03 ?  237 LEU A CA    1 
ATOM   1868 C C     . LEU A 1 237 ? -17.262 9.437  2.270   1.00 25.80 ?  237 LEU A C     1 
ATOM   1869 O O     . LEU A 1 237 ? -16.352 10.002 2.883   1.00 18.60 ?  237 LEU A O     1 
ATOM   1870 C CB    . LEU A 1 237 ? -18.627 7.507  3.135   1.00 19.57 ?  237 LEU A CB    1 
ATOM   1871 C CG    . LEU A 1 237 ? -18.896 6.016  3.358   1.00 25.58 ?  237 LEU A CG    1 
ATOM   1872 C CD1   . LEU A 1 237 ? -20.266 5.789  4.008   1.00 23.33 ?  237 LEU A CD1   1 
ATOM   1873 C CD2   . LEU A 1 237 ? -18.768 5.235  2.077   1.00 25.24 ?  237 LEU A CD2   1 
ATOM   1874 N N     . LEU A 1 238 ? -18.164 10.094 1.545   1.00 22.46 ?  238 LEU A N     1 
ATOM   1875 C CA    . LEU A 1 238 ? -18.266 11.548 1.519   1.00 21.17 ?  238 LEU A CA    1 
ATOM   1876 C C     . LEU A 1 238 ? -19.667 11.919 1.982   1.00 21.69 ?  238 LEU A C     1 
ATOM   1877 O O     . LEU A 1 238 ? -20.652 11.409 1.438   1.00 21.46 ?  238 LEU A O     1 
ATOM   1878 C CB    . LEU A 1 238 ? -17.999 12.097 0.107   1.00 21.95 ?  238 LEU A CB    1 
ATOM   1879 C CG    . LEU A 1 238 ? -16.521 12.143 -0.301  1.00 23.60 ?  238 LEU A CG    1 
ATOM   1880 C CD1   . LEU A 1 238 ? -16.363 12.330 -1.798  1.00 24.70 ?  238 LEU A CD1   1 
ATOM   1881 C CD2   . LEU A 1 238 ? -15.843 13.271 0.458   1.00 21.77 ?  238 LEU A CD2   1 
ATOM   1882 N N     . SER A 1 239 ? -19.761 12.782 2.999   1.00 18.52 ?  239 SER A N     1 
ATOM   1883 C CA    . SER A 1 239 ? -21.070 13.188 3.510   1.00 22.41 ?  239 SER A CA    1 
ATOM   1884 C C     . SER A 1 239 ? -21.750 14.257 2.664   1.00 22.39 ?  239 SER A C     1 
ATOM   1885 O O     . SER A 1 239 ? -22.901 14.603 2.942   1.00 23.33 ?  239 SER A O     1 
ATOM   1886 C CB    . SER A 1 239 ? -20.939 13.730 4.939   1.00 18.36 ?  239 SER A CB    1 
ATOM   1887 O OG    . SER A 1 239 ? -20.099 14.879 4.951   1.00 21.18 ?  239 SER A OG    1 
ATOM   1888 N N     . GLY A 1 240 ? -21.063 14.823 1.686   1.00 18.73 ?  240 GLY A N     1 
ATOM   1889 C CA    . GLY A 1 240 ? -21.474 16.085 1.131   1.00 19.28 ?  240 GLY A CA    1 
ATOM   1890 C C     . GLY A 1 240 ? -20.807 17.195 1.907   1.00 19.44 ?  240 GLY A C     1 
ATOM   1891 O O     . GLY A 1 240 ? -20.195 16.951 2.953   1.00 19.73 ?  240 GLY A O     1 
ATOM   1892 N N     . PRO A 1 241 ? -20.912 18.435 1.420   1.00 21.10 ?  241 PRO A N     1 
ATOM   1893 C CA    . PRO A 1 241 ? -20.051 19.513 1.936   1.00 21.47 ?  241 PRO A CA    1 
ATOM   1894 C C     . PRO A 1 241 ? -20.497 20.097 3.265   1.00 24.43 ?  241 PRO A C     1 
ATOM   1895 O O     . PRO A 1 241 ? -19.867 21.062 3.717   1.00 22.69 ?  241 PRO A O     1 
ATOM   1896 C CB    . PRO A 1 241 ? -20.125 20.578 0.826   1.00 22.57 ?  241 PRO A CB    1 
ATOM   1897 C CG    . PRO A 1 241 ? -21.524 20.410 0.281   1.00 21.86 ?  241 PRO A CG    1 
ATOM   1898 C CD    . PRO A 1 241 ? -21.819 18.906 0.352   1.00 19.54 ?  241 PRO A CD    1 
ATOM   1899 N N     . VAL A 1 242 ? -21.563 19.554 3.876   1.00 21.62 ?  242 VAL A N     1 
ATOM   1900 C CA    . VAL A 1 242 ? -22.102 19.992 5.164   1.00 20.16 ?  242 VAL A CA    1 
ATOM   1901 C C     . VAL A 1 242 ? -22.326 21.500 5.128   1.00 24.15 ?  242 VAL A C     1 
ATOM   1902 O O     . VAL A 1 242 ? -21.598 22.268 5.772   1.00 18.44 ?  242 VAL A O     1 
ATOM   1903 C CB    . VAL A 1 242 ? -21.190 19.589 6.341   1.00 19.74 ?  242 VAL A CB    1 
ATOM   1904 C CG1   . VAL A 1 242 ? -21.838 19.967 7.676   1.00 19.57 ?  242 VAL A CG1   1 
ATOM   1905 C CG2   . VAL A 1 242 ? -20.893 18.079 6.313   1.00 22.42 ?  242 VAL A CG2   1 
ATOM   1906 N N     . LEU A 1 243 ? -23.304 21.933 4.330   1.00 25.25 ?  243 LEU A N     1 
ATOM   1907 C CA    . LEU A 1 243 ? -23.625 23.351 4.248   1.00 20.29 ?  243 LEU A CA    1 
ATOM   1908 C C     . LEU A 1 243 ? -24.236 23.819 5.570   1.00 20.10 ?  243 LEU A C     1 
ATOM   1909 O O     . LEU A 1 243 ? -25.087 23.136 6.144   1.00 22.87 ?  243 LEU A O     1 
ATOM   1910 C CB    . LEU A 1 243 ? -24.596 23.628 3.087   1.00 15.54 ?  243 LEU A CB    1 
ATOM   1911 C CG    . LEU A 1 243 ? -24.184 23.151 1.681   1.00 21.95 ?  243 LEU A CG    1 
ATOM   1912 C CD1   . LEU A 1 243 ? -25.282 23.398 0.624   1.00 21.11 ?  243 LEU A CD1   1 
ATOM   1913 C CD2   . LEU A 1 243 ? -22.875 23.792 1.247   1.00 18.01 ?  243 LEU A CD2   1 
ATOM   1914 N N     . PRO A 1 244 ? -23.820 24.968 6.080   1.00 22.11 ?  244 PRO A N     1 
ATOM   1915 C CA    . PRO A 1 244 ? -24.301 25.402 7.395   1.00 25.07 ?  244 PRO A CA    1 
ATOM   1916 C C     . PRO A 1 244 ? -25.818 25.546 7.402   1.00 24.19 ?  244 PRO A C     1 
ATOM   1917 O O     . PRO A 1 244 ? -26.416 26.027 6.443   1.00 22.70 ?  244 PRO A O     1 
ATOM   1918 C CB    . PRO A 1 244 ? -23.596 26.747 7.603   1.00 25.71 ?  244 PRO A CB    1 
ATOM   1919 C CG    . PRO A 1 244 ? -22.347 26.649 6.718   1.00 26.07 ?  244 PRO A CG    1 
ATOM   1920 C CD    . PRO A 1 244 ? -22.822 25.887 5.509   1.00 24.51 ?  244 PRO A CD    1 
ATOM   1921 N N     . GLU A 1 245 ? -26.438 25.070 8.475   1.00 29.76 ?  245 GLU A N     1 
ATOM   1922 C CA    . GLU A 1 245 ? -27.870 25.204 8.694   1.00 28.67 ?  245 GLU A CA    1 
ATOM   1923 C C     . GLU A 1 245 ? -28.145 26.473 9.492   1.00 31.96 ?  245 GLU A C     1 
ATOM   1924 O O     . GLU A 1 245 ? -27.249 27.033 10.130  1.00 35.63 ?  245 GLU A O     1 
ATOM   1925 C CB    . GLU A 1 245 ? -28.403 23.989 9.444   1.00 27.76 ?  245 GLU A CB    1 
ATOM   1926 C CG    . GLU A 1 245 ? -28.150 22.664 8.730   1.00 30.71 ?  245 GLU A CG    1 
ATOM   1927 C CD    . GLU A 1 245 ? -29.194 22.370 7.659   1.00 35.53 ?  245 GLU A CD    1 
ATOM   1928 O OE1   . GLU A 1 245 ? -30.304 22.964 7.715   1.00 36.13 ?  245 GLU A OE1   1 
ATOM   1929 O OE2   . GLU A 1 245 ? -28.900 21.544 6.760   1.00 36.68 -1 245 GLU A OE2   1 
ATOM   1930 N N     . GLN A 1 246 ? -29.398 26.916 9.467   1.00 34.42 ?  246 GLN A N     1 
ATOM   1931 C CA    . GLN A 1 246 ? -29.761 28.158 10.140  1.00 37.39 ?  246 GLN A CA    1 
ATOM   1932 C C     . GLN A 1 246 ? -29.965 27.932 11.631  1.00 36.27 ?  246 GLN A C     1 
ATOM   1933 O O     . GLN A 1 246 ? -30.756 27.072 12.034  1.00 33.33 ?  246 GLN A O     1 
ATOM   1934 C CB    . GLN A 1 246 ? -31.036 28.759 9.544   1.00 35.98 ?  246 GLN A CB    1 
ATOM   1935 C CG    . GLN A 1 246 ? -31.422 30.103 10.206  1.00 39.27 ?  246 GLN A CG    1 
ATOM   1936 C CD    . GLN A 1 246 ? -32.747 30.676 9.701   1.00 47.66 ?  246 GLN A CD    1 
ATOM   1937 O OE1   . GLN A 1 246 ? -33.576 29.959 9.136   1.00 49.89 ?  246 GLN A OE1   1 
ATOM   1938 N NE2   . GLN A 1 246 ? -32.946 31.977 9.908   1.00 50.86 ?  246 GLN A NE2   1 
ATOM   1939 N N     . SER A 1 247 ? -29.272 28.731 12.444  1.00 36.07 ?  247 SER A N     1 
ATOM   1940 C CA    . SER A 1 247 ? -29.477 28.745 13.888  1.00 37.07 ?  247 SER A CA    1 
ATOM   1941 C C     . SER A 1 247 ? -30.847 29.322 14.245  1.00 36.75 ?  247 SER A C     1 
ATOM   1942 O O     . SER A 1 247 ? -31.437 30.099 13.489  1.00 31.55 ?  247 SER A O     1 
ATOM   1943 C CB    . SER A 1 247 ? -28.385 29.574 14.565  1.00 37.23 ?  247 SER A CB    1 
ATOM   1944 O OG    . SER A 1 247 ? -28.641 29.751 15.948  1.00 40.07 ?  247 SER A OG    1 
ATOM   1945 N N     . LYS A 1 248 ? -31.344 28.943 15.425  1.00 33.21 ?  248 LYS A N     1 
ATOM   1946 C CA    . LYS A 1 248 ? -32.582 29.508 15.952  1.00 38.48 ?  248 LYS A CA    1 
ATOM   1947 C C     . LYS A 1 248 ? -32.350 30.811 16.721  1.00 40.59 ?  248 LYS A C     1 
ATOM   1948 O O     . LYS A 1 248 ? -33.240 31.268 17.447  1.00 36.90 ?  248 LYS A O     1 
ATOM   1949 C CB    . LYS A 1 248 ? -33.289 28.477 16.833  1.00 38.18 ?  248 LYS A CB    1 
ATOM   1950 C CG    . LYS A 1 248 ? -33.824 27.276 16.046  1.00 37.46 ?  248 LYS A CG    1 
ATOM   1951 C CD    . LYS A 1 248 ? -34.405 26.219 16.976  1.00 39.37 ?  248 LYS A CD    1 
ATOM   1952 C CE    . LYS A 1 248 ? -33.343 25.703 17.927  1.00 38.41 ?  248 LYS A CE    1 
ATOM   1953 N NZ    . LYS A 1 248 ? -33.781 24.505 18.691  1.00 38.06 ?  248 LYS A NZ    1 
ATOM   1954 N N     . THR A 1 249 ? -31.175 31.413 16.567  1.00 35.20 ?  249 THR A N     1 
ATOM   1955 C CA    . THR A 1 249 ? -30.789 32.643 17.244  1.00 35.00 ?  249 THR A CA    1 
ATOM   1956 C C     . THR A 1 249 ? -30.452 33.663 16.169  1.00 36.82 ?  249 THR A C     1 
ATOM   1957 O O     . THR A 1 249 ? -29.529 33.441 15.374  1.00 34.33 ?  249 THR A O     1 
ATOM   1958 C CB    . THR A 1 249 ? -29.577 32.397 18.151  1.00 38.67 ?  249 THR A CB    1 
ATOM   1959 O OG1   . THR A 1 249 ? -29.817 31.263 18.997  1.00 35.95 ?  249 THR A OG1   1 
ATOM   1960 C CG2   . THR A 1 249 ? -29.264 33.623 19.006  1.00 38.31 ?  249 THR A CG2   1 
ATOM   1961 N N     . ALA A 1 250 ? -31.192 34.768 16.125  1.00 29.50 ?  250 ALA A N     1 
ATOM   1962 C CA    . ALA A 1 250 ? -30.880 35.765 15.105  1.00 33.20 ?  250 ALA A CA    1 
ATOM   1963 C C     . ALA A 1 250 ? -29.572 36.494 15.443  1.00 31.13 ?  250 ALA A C     1 
ATOM   1964 O O     . ALA A 1 250 ? -28.999 36.338 16.524  1.00 33.90 ?  250 ALA A O     1 
ATOM   1965 C CB    . ALA A 1 250 ? -32.024 36.762 14.950  1.00 28.33 ?  250 ALA A CB    1 
ATOM   1966 N N     . LEU A 1 251 ? -29.109 37.315 14.505  1.00 30.00 ?  251 LEU A N     1 
ATOM   1967 C CA    . LEU A 1 251 ? -27.837 38.003 14.679  1.00 29.58 ?  251 LEU A CA    1 
ATOM   1968 C C     . LEU A 1 251 ? -27.952 39.068 15.760  1.00 33.20 ?  251 LEU A C     1 
ATOM   1969 O O     . LEU A 1 251 ? -28.860 39.904 15.724  1.00 30.08 ?  251 LEU A O     1 
ATOM   1970 C CB    . LEU A 1 251 ? -27.394 38.638 13.367  1.00 29.25 ?  251 LEU A CB    1 
ATOM   1971 C CG    . LEU A 1 251 ? -26.196 39.591 13.439  1.00 25.39 ?  251 LEU A CG    1 
ATOM   1972 C CD1   . LEU A 1 251 ? -24.941 38.858 13.893  1.00 27.61 ?  251 LEU A CD1   1 
ATOM   1973 C CD2   . LEU A 1 251 ? -25.984 40.235 12.098  1.00 29.09 ?  251 LEU A CD2   1 
ATOM   1974 N N     . ASP A 1 252 ? -27.015 39.042 16.707  1.00 33.76 ?  252 ASP A N     1 
ATOM   1975 C CA    . ASP A 1 252 ? -26.967 40.024 17.786  1.00 34.08 ?  252 ASP A CA    1 
ATOM   1976 C C     . ASP A 1 252 ? -27.140 41.441 17.248  1.00 36.46 ?  252 ASP A C     1 
ATOM   1977 O O     . ASP A 1 252 ? -26.459 41.856 16.301  1.00 29.91 ?  252 ASP A O     1 
ATOM   1978 C CB    . ASP A 1 252 ? -25.645 39.894 18.544  1.00 36.32 ?  252 ASP A CB    1 
ATOM   1979 C CG    . ASP A 1 252 ? -25.559 40.824 19.763  1.00 44.08 ?  252 ASP A CG    1 
ATOM   1980 O OD1   . ASP A 1 252 ? -24.613 40.651 20.575  1.00 42.42 -1 252 ASP A OD1   1 
ATOM   1981 O OD2   . ASP A 1 252 ? -26.417 41.733 19.900  1.00 44.30 -1 252 ASP A OD2   1 
ATOM   1982 N N     . GLU A 1 253 ? -28.087 42.174 17.850  1.00 39.52 ?  253 GLU A N     1 
ATOM   1983 C CA    . GLU A 1 253 ? -28.473 43.477 17.320  1.00 36.61 ?  253 GLU A CA    1 
ATOM   1984 C C     . GLU A 1 253 ? -27.338 44.487 17.417  1.00 38.14 ?  253 GLU A C     1 
ATOM   1985 O O     . GLU A 1 253 ? -27.255 45.402 16.590  1.00 37.58 ?  253 GLU A O     1 
ATOM   1986 C CB    . GLU A 1 253 ? -29.709 43.988 18.058  1.00 45.96 ?  253 GLU A CB    1 
ATOM   1987 C CG    . GLU A 1 253 ? -30.487 45.049 17.304  1.00 43.89 ?  253 GLU A CG    1 
ATOM   1988 C CD    . GLU A 1 253 ? -30.240 46.450 17.850  1.00 58.97 ?  253 GLU A CD    1 
ATOM   1989 O OE1   . GLU A 1 253 ? -29.428 46.594 18.798  1.00 59.38 ?  253 GLU A OE1   1 
ATOM   1990 O OE2   . GLU A 1 253 ? -30.856 47.406 17.327  1.00 61.65 -1 253 GLU A OE2   1 
ATOM   1991 N N     . LYS A 1 254 ? -26.464 44.340 18.419  1.00 36.75 ?  254 LYS A N     1 
ATOM   1992 C CA    . LYS A 1 254 ? -25.275 45.180 18.498  1.00 36.69 ?  254 LYS A CA    1 
ATOM   1993 C C     . LYS A 1 254 ? -24.446 45.073 17.218  1.00 37.05 ?  254 LYS A C     1 
ATOM   1994 O O     . LYS A 1 254 ? -23.969 46.086 16.687  1.00 37.80 ?  254 LYS A O     1 
ATOM   1995 C CB    . LYS A 1 254 ? -24.455 44.798 19.742  1.00 38.53 ?  254 LYS A CB    1 
ATOM   1996 C CG    . LYS A 1 254 ? -22.918 44.642 19.556  1.00 40.42 ?  254 LYS A CG    1 
ATOM   1997 C CD    . LYS A 1 254 ? -22.169 45.936 19.908  1.00 45.59 ?  254 LYS A CD    1 
ATOM   1998 C CE    . LYS A 1 254 ? -20.697 45.909 19.497  1.00 46.24 ?  254 LYS A CE    1 
ATOM   1999 N NZ    . LYS A 1 254 ? -20.107 47.303 19.428  1.00 46.74 ?  254 LYS A NZ    1 
ATOM   2000 N N     . TRP A 1 255 ? -24.290 43.860 16.683  1.00 33.72 ?  255 TRP A N     1 
ATOM   2001 C CA    . TRP A 1 255 ? -23.494 43.739 15.468  1.00 32.65 ?  255 TRP A CA    1 
ATOM   2002 C C     . TRP A 1 255 ? -24.310 44.110 14.242  1.00 26.28 ?  255 TRP A C     1 
ATOM   2003 O O     . TRP A 1 255 ? -23.800 44.780 13.340  1.00 29.35 ?  255 TRP A O     1 
ATOM   2004 C CB    . TRP A 1 255 ? -22.915 42.326 15.342  1.00 28.43 ?  255 TRP A CB    1 
ATOM   2005 C CG    . TRP A 1 255 ? -21.941 42.019 16.424  1.00 30.34 ?  255 TRP A CG    1 
ATOM   2006 C CD1   . TRP A 1 255 ? -22.077 41.079 17.398  1.00 31.69 ?  255 TRP A CD1   1 
ATOM   2007 C CD2   . TRP A 1 255 ? -20.689 42.671 16.668  1.00 28.70 ?  255 TRP A CD2   1 
ATOM   2008 N NE1   . TRP A 1 255 ? -20.992 41.100 18.232  1.00 31.82 ?  255 TRP A NE1   1 
ATOM   2009 C CE2   . TRP A 1 255 ? -20.119 42.065 17.803  1.00 34.04 ?  255 TRP A CE2   1 
ATOM   2010 C CE3   . TRP A 1 255 ? -19.994 43.703 16.035  1.00 30.27 ?  255 TRP A CE3   1 
ATOM   2011 C CZ2   . TRP A 1 255 ? -18.874 42.454 18.321  1.00 31.15 ?  255 TRP A CZ2   1 
ATOM   2012 C CZ3   . TRP A 1 255 ? -18.760 44.097 16.551  1.00 29.70 ?  255 TRP A CZ3   1 
ATOM   2013 C CH2   . TRP A 1 255 ? -18.215 43.467 17.685  1.00 30.94 ?  255 TRP A CH2   1 
ATOM   2014 N N     . GLY A 1 256 ? -25.579 43.698 14.204  1.00 32.85 ?  256 GLY A N     1 
ATOM   2015 C CA    . GLY A 1 256 ? -26.437 44.068 13.090  1.00 27.26 ?  256 GLY A CA    1 
ATOM   2016 C C     . GLY A 1 256 ? -26.512 45.566 12.891  1.00 31.77 ?  256 GLY A C     1 
ATOM   2017 O O     . GLY A 1 256 ? -26.422 46.061 11.764  1.00 28.27 ?  256 GLY A O     1 
ATOM   2018 N N     . SER A 1 257 ? -26.653 46.314 13.988  1.00 32.52 ?  257 SER A N     1 
ATOM   2019 C CA    . SER A 1 257 ? -26.713 47.769 13.890  1.00 34.88 ?  257 SER A CA    1 
ATOM   2020 C C     . SER A 1 257 ? -25.407 48.336 13.363  1.00 30.65 ?  257 SER A C     1 
ATOM   2021 O O     . SER A 1 257 ? -25.396 49.198 12.475  1.00 31.28 ?  257 SER A O     1 
ATOM   2022 C CB    . SER A 1 257 ? -27.034 48.364 15.258  1.00 35.67 ?  257 SER A CB    1 
ATOM   2023 O OG    . SER A 1 257 ? -28.409 48.182 15.539  1.00 47.55 ?  257 SER A OG    1 
ATOM   2024 N N     . TRP A 1 258 ? -24.289 47.862 13.906  1.00 30.18 ?  258 TRP A N     1 
ATOM   2025 C CA    . TRP A 1 258 ? -23.001 48.437 13.538  1.00 28.95 ?  258 TRP A CA    1 
ATOM   2026 C C     . TRP A 1 258 ? -22.621 48.056 12.111  1.00 25.88 ?  258 TRP A C     1 
ATOM   2027 O O     . TRP A 1 258 ? -22.178 48.905 11.330  1.00 32.61 ?  258 TRP A O     1 
ATOM   2028 C CB    . TRP A 1 258 ? -21.937 47.991 14.542  1.00 29.56 ?  258 TRP A CB    1 
ATOM   2029 C CG    . TRP A 1 258 ? -20.568 48.547 14.263  1.00 34.33 ?  258 TRP A CG    1 
ATOM   2030 C CD1   . TRP A 1 258 ? -20.091 49.797 14.582  1.00 30.30 ?  258 TRP A CD1   1 
ATOM   2031 C CD2   . TRP A 1 258 ? -19.499 47.868 13.604  1.00 32.65 ?  258 TRP A CD2   1 
ATOM   2032 N NE1   . TRP A 1 258 ? -18.783 49.924 14.163  1.00 29.92 ?  258 TRP A NE1   1 
ATOM   2033 C CE2   . TRP A 1 258 ? -18.398 48.756 13.560  1.00 28.97 ?  258 TRP A CE2   1 
ATOM   2034 C CE3   . TRP A 1 258 ? -19.359 46.588 13.052  1.00 30.66 ?  258 TRP A CE3   1 
ATOM   2035 C CZ2   . TRP A 1 258 ? -17.183 48.407 12.978  1.00 30.71 ?  258 TRP A CZ2   1 
ATOM   2036 C CZ3   . TRP A 1 258 ? -18.143 46.244 12.479  1.00 27.57 ?  258 TRP A CZ3   1 
ATOM   2037 C CH2   . TRP A 1 258 ? -17.077 47.149 12.445  1.00 30.48 ?  258 TRP A CH2   1 
ATOM   2038 N N     . LEU A 1 259 ? -22.802 46.790 11.746  1.00 29.35 ?  259 LEU A N     1 
ATOM   2039 C CA    . LEU A 1 259 ? -22.542 46.385 10.369  1.00 28.66 ?  259 LEU A CA    1 
ATOM   2040 C C     . LEU A 1 259 ? -23.412 47.157 9.394   1.00 28.85 ?  259 LEU A C     1 
ATOM   2041 O O     . LEU A 1 259 ? -22.937 47.578 8.331   1.00 29.67 ?  259 LEU A O     1 
ATOM   2042 C CB    . LEU A 1 259 ? -22.783 44.889 10.203  1.00 28.24 ?  259 LEU A CB    1 
ATOM   2043 C CG    . LEU A 1 259 ? -21.727 44.034 10.875  1.00 28.96 ?  259 LEU A CG    1 
ATOM   2044 C CD1   . LEU A 1 259 ? -22.202 42.578 10.905  1.00 23.49 ?  259 LEU A CD1   1 
ATOM   2045 C CD2   . LEU A 1 259 ? -20.403 44.217 10.130  1.00 24.71 ?  259 LEU A CD2   1 
ATOM   2046 N N     . GLY A 1 260 ? -24.693 47.345 9.737   1.00 28.95 ?  260 GLY A N     1 
ATOM   2047 C CA    . GLY A 1 260 ? -25.643 47.994 8.845   1.00 32.38 ?  260 GLY A CA    1 
ATOM   2048 C C     . GLY A 1 260 ? -25.299 49.420 8.461   1.00 31.00 ?  260 GLY A C     1 
ATOM   2049 O O     . GLY A 1 260 ? -25.855 49.939 7.490   1.00 31.87 ?  260 GLY A O     1 
ATOM   2050 N N     . GLY A 1 261 ? -24.384 50.061 9.185   1.00 33.79 ?  261 GLY A N     1 
ATOM   2051 C CA    . GLY A 1 261 ? -23.960 51.397 8.821   1.00 31.53 ?  261 GLY A CA    1 
ATOM   2052 C C     . GLY A 1 261 ? -22.967 51.482 7.678   1.00 38.02 ?  261 GLY A C     1 
ATOM   2053 O O     . GLY A 1 261 ? -22.684 52.585 7.198   1.00 37.58 ?  261 GLY A O     1 
ATOM   2054 N N     . PHE A 1 262 ? -22.428 50.361 7.216   1.00 27.86 ?  262 PHE A N     1 
ATOM   2055 C CA    . PHE A 1 262 ? -21.436 50.412 6.156   1.00 29.59 ?  262 PHE A CA    1 
ATOM   2056 C C     . PHE A 1 262 ? -22.067 50.109 4.800   1.00 27.06 ?  262 PHE A C     1 
ATOM   2057 O O     . PHE A 1 262 ? -23.041 49.359 4.697   1.00 29.24 ?  262 PHE A O     1 
ATOM   2058 C CB    . PHE A 1 262 ? -20.295 49.436 6.448   1.00 31.04 ?  262 PHE A CB    1 
ATOM   2059 C CG    . PHE A 1 262 ? -19.572 49.728 7.744   1.00 31.52 ?  262 PHE A CG    1 
ATOM   2060 C CD1   . PHE A 1 262 ? -18.639 50.759 7.814   1.00 30.50 ?  262 PHE A CD1   1 
ATOM   2061 C CD2   . PHE A 1 262 ? -19.838 48.983 8.888   1.00 27.92 ?  262 PHE A CD2   1 
ATOM   2062 C CE1   . PHE A 1 262 ? -17.978 51.037 8.999   1.00 31.78 ?  262 PHE A CE1   1 
ATOM   2063 C CE2   . PHE A 1 262 ? -19.180 49.249 10.072  1.00 30.30 ?  262 PHE A CE2   1 
ATOM   2064 C CZ    . PHE A 1 262 ? -18.247 50.276 10.130  1.00 29.99 ?  262 PHE A CZ    1 
ATOM   2065 N N     . LYS A 1 263 ? -21.484 50.684 3.754   1.00 29.82 ?  263 LYS A N     1 
ATOM   2066 C CA    . LYS A 1 263 ? -21.963 50.419 2.407   1.00 32.80 ?  263 LYS A CA    1 
ATOM   2067 C C     . LYS A 1 263 ? -21.675 48.973 2.013   1.00 35.86 ?  263 LYS A C     1 
ATOM   2068 O O     . LYS A 1 263 ? -20.650 48.392 2.404   1.00 30.38 ?  263 LYS A O     1 
ATOM   2069 C CB    . LYS A 1 263 ? -21.317 51.395 1.417   1.00 38.35 ?  263 LYS A CB    1 
ATOM   2070 C CG    . LYS A 1 263 ? -20.377 50.754 0.392   1.00 43.60 ?  263 LYS A CG    1 
ATOM   2071 C CD    . LYS A 1 263 ? -19.690 51.801 -0.492  1.00 43.27 ?  263 LYS A CD    1 
ATOM   2072 C CE    . LYS A 1 263 ? -19.336 51.240 -1.866  1.00 55.02 ?  263 LYS A CE    1 
ATOM   2073 N NZ    . LYS A 1 263 ? -18.350 52.128 -2.570  1.00 56.14 ?  263 LYS A NZ    1 
ATOM   2074 N N     . ASP A 1 264 ? -22.602 48.395 1.245   1.00 33.44 ?  264 ASP A N     1 
ATOM   2075 C CA    . ASP A 1 264 ? -22.512 47.005 0.816   1.00 29.69 ?  264 ASP A CA    1 
ATOM   2076 C C     . ASP A 1 264 ? -21.131 46.694 0.256   1.00 28.53 ?  264 ASP A C     1 
ATOM   2077 O O     . ASP A 1 264 ? -20.589 47.450 -0.554  1.00 27.11 ?  264 ASP A O     1 
ATOM   2078 C CB    . ASP A 1 264 ? -23.577 46.719 -0.251  1.00 32.07 ?  264 ASP A CB    1 
ATOM   2079 C CG    . ASP A 1 264 ? -25.005 46.721 0.305   1.00 38.41 ?  264 ASP A CG    1 
ATOM   2080 O OD1   . ASP A 1 264 ? -25.183 46.573 1.536   1.00 38.37 ?  264 ASP A OD1   1 
ATOM   2081 O OD2   . ASP A 1 264 ? -25.957 46.847 -0.505  1.00 43.64 -1 264 ASP A OD2   1 
ATOM   2082 N N     . GLY A 1 265 ? -20.559 45.575 0.702   1.00 27.20 ?  265 GLY A N     1 
ATOM   2083 C CA    . GLY A 1 265 ? -19.309 45.094 0.147   1.00 25.83 ?  265 GLY A CA    1 
ATOM   2084 C C     . GLY A 1 265 ? -18.042 45.810 0.572   1.00 27.83 ?  265 GLY A C     1 
ATOM   2085 O O     . GLY A 1 265 ? -16.981 45.540 -0.014  1.00 22.79 ?  265 GLY A O     1 
ATOM   2086 N N     . SER A 1 266 ? -18.093 46.680 1.593   1.00 23.55 ?  266 SER A N     1 
ATOM   2087 C CA    . SER A 1 266 ? -16.947 47.527 1.929   1.00 23.91 ?  266 SER A CA    1 
ATOM   2088 C C     . SER A 1 266 ? -16.128 47.051 3.132   1.00 22.86 ?  266 SER A C     1 
ATOM   2089 O O     . SER A 1 266 ? -15.013 47.553 3.334   1.00 23.77 ?  266 SER A O     1 
ATOM   2090 C CB    . SER A 1 266 ? -17.415 48.970 2.204   1.00 24.81 ?  266 SER A CB    1 
ATOM   2091 O OG    . SER A 1 266 ? -18.214 49.019 3.374   1.00 25.37 ?  266 SER A OG    1 
ATOM   2092 N N     . LEU A 1 267 ? -16.645 46.134 3.944   1.00 22.94 ?  267 LEU A N     1 
ATOM   2093 C CA    . LEU A 1 267 ? -16.031 45.793 5.219   1.00 21.69 ?  267 LEU A CA    1 
ATOM   2094 C C     . LEU A 1 267 ? -15.111 44.576 5.092   1.00 22.62 ?  267 LEU A C     1 
ATOM   2095 O O     . LEU A 1 267 ? -15.443 43.590 4.422   1.00 19.12 ?  267 LEU A O     1 
ATOM   2096 C CB    . LEU A 1 267 ? -17.104 45.530 6.276   1.00 20.73 ?  267 LEU A CB    1 
ATOM   2097 C CG    . LEU A 1 267 ? -16.604 45.310 7.703   1.00 23.82 ?  267 LEU A CG    1 
ATOM   2098 C CD1   . LEU A 1 267 ? -17.370 46.143 8.722   1.00 26.43 ?  267 LEU A CD1   1 
ATOM   2099 C CD2   . LEU A 1 267 ? -16.679 43.838 8.078   1.00 25.51 ?  267 LEU A CD2   1 
ATOM   2100 N N     . VAL A 1 268 ? -13.958 44.647 5.747   1.00 17.07 ?  268 VAL A N     1 
ATOM   2101 C CA    . VAL A 1 268 ? -13.057 43.499 5.856   1.00 20.15 ?  268 VAL A CA    1 
ATOM   2102 C C     . VAL A 1 268 ? -13.369 42.769 7.165   1.00 16.02 ?  268 VAL A C     1 
ATOM   2103 O O     . VAL A 1 268 ? -13.306 43.357 8.241   1.00 16.21 ?  268 VAL A O     1 
ATOM   2104 C CB    . VAL A 1 268 ? -11.584 43.944 5.791   1.00 19.90 ?  268 VAL A CB    1 
ATOM   2105 C CG1   . VAL A 1 268 ? -10.644 42.763 5.999   1.00 19.57 ?  268 VAL A CG1   1 
ATOM   2106 C CG2   . VAL A 1 268 ? -11.288 44.638 4.436   1.00 16.76 ?  268 VAL A CG2   1 
ATOM   2107 N N     . TYR A 1 269 ? -13.738 41.498 7.080   1.00 18.16 ?  269 TYR A N     1 
ATOM   2108 C CA    . TYR A 1 269 ? -13.920 40.668 8.266   1.00 17.18 ?  269 TYR A CA    1 
ATOM   2109 C C     . TYR A 1 269 ? -12.719 39.744 8.430   1.00 17.42 ?  269 TYR A C     1 
ATOM   2110 O O     . TYR A 1 269 ? -12.391 38.984 7.514   1.00 20.48 ?  269 TYR A O     1 
ATOM   2111 C CB    . TYR A 1 269 ? -15.205 39.841 8.160   1.00 16.58 ?  269 TYR A CB    1 
ATOM   2112 C CG    . TYR A 1 269 ? -15.401 38.841 9.284   1.00 18.08 ?  269 TYR A CG    1 
ATOM   2113 C CD1   . TYR A 1 269 ? -15.768 39.262 10.564  1.00 22.29 ?  269 TYR A CD1   1 
ATOM   2114 C CD2   . TYR A 1 269 ? -15.223 37.478 9.070   1.00 17.08 ?  269 TYR A CD2   1 
ATOM   2115 C CE1   . TYR A 1 269 ? -15.952 38.334 11.602  1.00 21.04 ?  269 TYR A CE1   1 
ATOM   2116 C CE2   . TYR A 1 269 ? -15.391 36.559 10.092  1.00 19.05 ?  269 TYR A CE2   1 
ATOM   2117 C CZ    . TYR A 1 269 ? -15.768 36.985 11.361  1.00 21.95 ?  269 TYR A CZ    1 
ATOM   2118 O OH    . TYR A 1 269 ? -15.947 36.059 12.389  1.00 20.70 ?  269 TYR A OH    1 
ATOM   2119 N N     . CYS A 1 270 ? -12.085 39.782 9.601   1.00 18.68 ?  270 CYS A N     1 
ATOM   2120 C CA    . CYS A 1 270 ? -10.906 38.962 9.887   1.00 19.56 ?  270 CYS A CA    1 
ATOM   2121 C C     . CYS A 1 270 ? -11.116 38.135 11.156  1.00 18.89 ?  270 CYS A C     1 
ATOM   2122 O O     . CYS A 1 270 ? -11.418 38.694 12.213  1.00 19.02 ?  270 CYS A O     1 
ATOM   2123 C CB    . CYS A 1 270 ? -9.659  39.850 10.039  1.00 18.97 ?  270 CYS A CB    1 
ATOM   2124 S SG    . CYS A 1 270 ? -8.186  38.975 10.668  1.00 22.77 ?  270 CYS A SG    1 
ATOM   2125 N N     . ALA A 1 271 ? -10.933 36.814 11.065  1.00 16.96 ?  271 ALA A N     1 
ATOM   2126 C CA    . ALA A 1 271 ? -11.069 35.942 12.233  1.00 17.21 ?  271 ALA A CA    1 
ATOM   2127 C C     . ALA A 1 271 ? -10.174 34.717 12.087  1.00 22.54 ?  271 ALA A C     1 
ATOM   2128 O O     . ALA A 1 271 ? -10.135 34.105 11.019  1.00 17.40 ?  271 ALA A O     1 
ATOM   2129 C CB    . ALA A 1 271 ? -12.523 35.489 12.425  1.00 16.96 ?  271 ALA A CB    1 
ATOM   2130 N N     . LEU A 1 272 ? -9.493  34.328 13.171  1.00 23.66 ?  272 LEU A N     1 
ATOM   2131 C CA    . LEU A 1 272 ? -8.568  33.196 13.135  1.00 23.91 ?  272 LEU A CA    1 
ATOM   2132 C C     . LEU A 1 272 ? -9.001  32.061 14.065  1.00 25.31 ?  272 LEU A C     1 
ATOM   2133 O O     . LEU A 1 272 ? -8.169  31.373 14.654  1.00 24.19 ?  272 LEU A O     1 
ATOM   2134 C CB    . LEU A 1 272 ? -7.144  33.643 13.463  1.00 24.07 ?  272 LEU A CB    1 
ATOM   2135 C CG    . LEU A 1 272 ? -6.659  34.895 12.720  1.00 21.83 ?  272 LEU A CG    1 
ATOM   2136 C CD1   . LEU A 1 272 ? -5.239  35.243 13.165  1.00 26.17 ?  272 LEU A CD1   1 
ATOM   2137 C CD2   . LEU A 1 272 ? -6.729  34.710 11.184  1.00 21.17 ?  272 LEU A CD2   1 
ATOM   2138 N N     . GLY A 1 273 ? -10.313 31.824 14.171  1.00 26.36 ?  273 GLY A N     1 
ATOM   2139 C CA    . GLY A 1 273 ? -10.848 30.732 14.973  1.00 32.25 ?  273 GLY A CA    1 
ATOM   2140 C C     . GLY A 1 273 ? -10.892 31.049 16.462  1.00 32.03 ?  273 GLY A C     1 
ATOM   2141 O O     . GLY A 1 273 ? -10.807 32.197 16.889  1.00 35.05 ?  273 GLY A O     1 
ATOM   2142 N N     . SER A 1 274 ? -11.014 29.989 17.264  1.00 36.01 ?  274 SER A N     1 
ATOM   2143 C CA    . SER A 1 274 ? -11.078 30.115 18.716  1.00 41.32 ?  274 SER A CA    1 
ATOM   2144 C C     . SER A 1 274 ? -10.027 29.254 19.418  1.00 45.00 ?  274 SER A C     1 
ATOM   2145 O O     . SER A 1 274 ? -10.172 28.951 20.612  1.00 44.43 ?  274 SER A O     1 
ATOM   2146 C CB    . SER A 1 274 ? -12.471 29.733 19.209  1.00 40.98 ?  274 SER A CB    1 
ATOM   2147 O OG    . SER A 1 274 ? -12.700 28.364 18.914  1.00 40.65 ?  274 SER A OG    1 
ATOM   2148 N N     . GLU A 1 275 ? -8.982  28.837 18.709  1.00 42.92 ?  275 GLU A N     1 
ATOM   2149 C CA    . GLU A 1 275 ? -8.000  27.910 19.259  1.00 47.09 ?  275 GLU A CA    1 
ATOM   2150 C C     . GLU A 1 275 ? -6.595  28.495 19.407  1.00 47.84 ?  275 GLU A C     1 
ATOM   2151 O O     . GLU A 1 275 ? -5.691  27.765 19.850  1.00 40.37 ?  275 GLU A O     1 
ATOM   2152 C CB    . GLU A 1 275 ? -7.917  26.633 18.390  1.00 43.34 ?  275 GLU A CB    1 
ATOM   2153 C CG    . GLU A 1 275 ? -9.093  25.648 18.532  1.00 36.22 ?  275 GLU A CG    1 
ATOM   2154 C CD    . GLU A 1 275 ? -8.708  24.209 18.180  1.00 41.52 ?  275 GLU A CD    1 
ATOM   2155 O OE1   . GLU A 1 275 ? -7.556  23.998 17.704  1.00 40.33 ?  275 GLU A OE1   1 
ATOM   2156 O OE2   . GLU A 1 275 ? -9.544  23.284 18.403  1.00 24.76 -1 275 GLU A OE2   1 
ATOM   2157 N N     . LEU A 1 276 ? -6.375  29.771 19.062  1.00 43.58 ?  276 LEU A N     1 
ATOM   2158 C CA    . LEU A 1 276 ? -5.008  30.254 18.908  1.00 41.46 ?  276 LEU A CA    1 
ATOM   2159 C C     . LEU A 1 276 ? -4.892  31.714 19.311  1.00 35.02 ?  276 LEU A C     1 
ATOM   2160 O O     . LEU A 1 276 ? -5.837  32.488 19.176  1.00 37.65 ?  276 LEU A O     1 
ATOM   2161 C CB    . LEU A 1 276 ? -4.516  30.062 17.464  1.00 40.33 ?  276 LEU A CB    1 
ATOM   2162 C CG    . LEU A 1 276 ? -5.113  30.944 16.352  1.00 41.03 ?  276 LEU A CG    1 
ATOM   2163 C CD1   . LEU A 1 276 ? -4.456  32.353 16.214  1.00 34.08 ?  276 LEU A CD1   1 
ATOM   2164 C CD2   . LEU A 1 276 ? -5.124  30.179 15.008  1.00 37.13 ?  276 LEU A CD2   1 
ATOM   2165 N N     . LYS A 1 277 ? -3.703  32.071 19.799  1.00 34.10 ?  277 LYS A N     1 
ATOM   2166 C CA    . LYS A 1 277 ? -3.313  33.435 20.131  1.00 29.85 ?  277 LYS A CA    1 
ATOM   2167 C C     . LYS A 1 277 ? -2.142  33.817 19.234  1.00 34.26 ?  277 LYS A C     1 
ATOM   2168 O O     . LYS A 1 277 ? -1.180  33.053 19.116  1.00 32.97 ?  277 LYS A O     1 
ATOM   2169 C CB    . LYS A 1 277 ? -2.908  33.544 21.617  1.00 30.29 ?  277 LYS A CB    1 
ATOM   2170 C CG    . LYS A 1 277 ? -4.082  33.773 22.578  1.00 36.93 ?  277 LYS A CG    1 
ATOM   2171 C CD    . LYS A 1 277 ? -3.933  33.072 23.935  1.00 36.45 ?  277 LYS A CD    1 
ATOM   2172 C CE    . LYS A 1 277 ? -3.002  33.813 24.875  1.00 37.66 ?  277 LYS A CE    1 
ATOM   2173 N NZ    . LYS A 1 277 ? -3.431  35.226 25.150  1.00 40.35 ?  277 LYS A NZ    1 
ATOM   2174 N N     . LEU A 1 278 ? -2.222  34.973 18.581  1.00 25.51 ?  278 LEU A N     1 
ATOM   2175 C CA    . LEU A 1 278 ? -1.058  35.441 17.837  1.00 27.46 ?  278 LEU A CA    1 
ATOM   2176 C C     . LEU A 1 278 ? 0.037   35.921 18.790  1.00 26.82 ?  278 LEU A C     1 
ATOM   2177 O O     . LEU A 1 278 ? -0.232  36.307 19.927  1.00 25.49 ?  278 LEU A O     1 
ATOM   2178 C CB    . LEU A 1 278 ? -1.443  36.581 16.896  1.00 22.22 ?  278 LEU A CB    1 
ATOM   2179 C CG    . LEU A 1 278 ? -2.370  36.186 15.751  1.00 24.04 ?  278 LEU A CG    1 
ATOM   2180 C CD1   . LEU A 1 278 ? -3.049  37.426 15.194  1.00 24.50 ?  278 LEU A CD1   1 
ATOM   2181 C CD2   . LEU A 1 278 ? -1.601  35.446 14.692  1.00 24.81 ?  278 LEU A CD2   1 
ATOM   2182 N N     . LYS A 1 279 ? 1.287   35.891 18.316  1.00 25.62 ?  279 LYS A N     1 
ATOM   2183 C CA    . LYS A 1 279 ? 2.352   36.634 18.977  1.00 23.91 ?  279 LYS A CA    1 
ATOM   2184 C C     . LYS A 1 279 ? 2.140   38.131 18.765  1.00 26.59 ?  279 LYS A C     1 
ATOM   2185 O O     . LYS A 1 279 ? 1.575   38.557 17.756  1.00 21.05 ?  279 LYS A O     1 
ATOM   2186 C CB    . LYS A 1 279 ? 3.724   36.211 18.442  1.00 30.94 ?  279 LYS A CB    1 
ATOM   2187 C CG    . LYS A 1 279 ? 3.847   34.706 18.297  1.00 38.71 ?  279 LYS A CG    1 
ATOM   2188 C CD    . LYS A 1 279 ? 4.646   34.272 17.052  1.00 48.83 ?  279 LYS A CD    1 
ATOM   2189 C CE    . LYS A 1 279 ? 3.855   34.542 15.759  1.00 37.22 ?  279 LYS A CE    1 
ATOM   2190 N NZ    . LYS A 1 279 ? 2.396   34.092 15.746  1.00 31.41 ?  279 LYS A NZ    1 
ATOM   2191 N N     . GLN A 1 280 ? 2.611   38.938 19.728  1.00 22.54 ?  280 GLN A N     1 
ATOM   2192 C CA    . GLN A 1 280 ? 2.267   40.360 19.715  1.00 25.17 ?  280 GLN A CA    1 
ATOM   2193 C C     . GLN A 1 280 ? 2.781   41.058 18.455  1.00 25.56 ?  280 GLN A C     1 
ATOM   2194 O O     . GLN A 1 280 ? 2.107   41.942 17.915  1.00 24.02 ?  280 GLN A O     1 
ATOM   2195 C CB    . GLN A 1 280 ? 2.793   41.077 20.964  1.00 24.82 ?  280 GLN A CB    1 
ATOM   2196 C CG    . GLN A 1 280 ? 2.355   42.541 20.966  1.00 31.15 ?  280 GLN A CG    1 
ATOM   2197 C CD    . GLN A 1 280 ? 2.965   43.406 22.067  1.00 40.35 ?  280 GLN A CD    1 
ATOM   2198 O OE1   . GLN A 1 280 ? 4.081   43.158 22.539  1.00 34.60 ?  280 GLN A OE1   1 
ATOM   2199 N NE2   . GLN A 1 280 ? 2.230   44.451 22.462  1.00 37.87 ?  280 GLN A NE2   1 
ATOM   2200 N N     . ASP A 1 281 ? 3.963   40.672 17.967  1.00 21.19 ?  281 ASP A N     1 
ATOM   2201 C CA    . ASP A 1 281 ? 4.490   41.290 16.751  1.00 24.65 ?  281 ASP A CA    1 
ATOM   2202 C C     . ASP A 1 281 ? 3.566   41.037 15.564  1.00 22.40 ?  281 ASP A C     1 
ATOM   2203 O O     . ASP A 1 281 ? 3.264   41.951 14.786  1.00 20.90 ?  281 ASP A O     1 
ATOM   2204 C CB    . ASP A 1 281 ? 5.891   40.751 16.460  1.00 29.95 ?  281 ASP A CB    1 
ATOM   2205 C CG    . ASP A 1 281 ? 6.001   39.248 16.712  1.00 39.46 ?  281 ASP A CG    1 
ATOM   2206 O OD1   . ASP A 1 281 ? 6.546   38.539 15.829  1.00 48.08 ?  281 ASP A OD1   1 
ATOM   2207 O OD2   . ASP A 1 281 ? 5.543   38.775 17.791  1.00 42.64 -1 281 ASP A OD2   1 
ATOM   2208 N N     . GLN A 1 282 ? 3.108   39.793 15.412  1.00 21.38 ?  282 GLN A N     1 
ATOM   2209 C CA    . GLN A 1 282 ? 2.222   39.471 14.300  1.00 20.91 ?  282 GLN A CA    1 
ATOM   2210 C C     . GLN A 1 282 ? 0.820   40.029 14.523  1.00 20.65 ?  282 GLN A C     1 
ATOM   2211 O O     . GLN A 1 282 ? 0.126   40.367 13.551  1.00 16.37 ?  282 GLN A O     1 
ATOM   2212 C CB    . GLN A 1 282 ? 2.197   37.958 14.086  1.00 20.13 ?  282 GLN A CB    1 
ATOM   2213 C CG    . GLN A 1 282 ? 3.555   37.381 13.645  1.00 22.23 ?  282 GLN A CG    1 
ATOM   2214 C CD    . GLN A 1 282 ? 3.904   37.794 12.213  1.00 20.40 ?  282 GLN A CD    1 
ATOM   2215 O OE1   . GLN A 1 282 ? 3.562   37.104 11.256  1.00 18.33 ?  282 GLN A OE1   1 
ATOM   2216 N NE2   . GLN A 1 282 ? 4.546   38.944 12.068  1.00 19.90 ?  282 GLN A NE2   1 
ATOM   2217 N N     . PHE A 1 283 ? 0.392   40.135 15.790  1.00 21.87 ?  283 PHE A N     1 
ATOM   2218 C CA    . PHE A 1 283 ? -0.853  40.833 16.120  1.00 20.20 ?  283 PHE A CA    1 
ATOM   2219 C C     . PHE A 1 283 ? -0.814  42.286 15.627  1.00 20.97 ?  283 PHE A C     1 
ATOM   2220 O O     . PHE A 1 283 ? -1.770  42.772 15.004  1.00 15.93 ?  283 PHE A O     1 
ATOM   2221 C CB    . PHE A 1 283 ? -1.064  40.738 17.638  1.00 20.32 ?  283 PHE A CB    1 
ATOM   2222 C CG    . PHE A 1 283 ? -2.362  41.323 18.152  1.00 21.42 ?  283 PHE A CG    1 
ATOM   2223 C CD1   . PHE A 1 283 ? -3.546  40.592 18.104  1.00 23.17 ?  283 PHE A CD1   1 
ATOM   2224 C CD2   . PHE A 1 283 ? -2.385  42.568 18.763  1.00 19.40 ?  283 PHE A CD2   1 
ATOM   2225 C CE1   . PHE A 1 283 ? -4.723  41.107 18.612  1.00 18.44 ?  283 PHE A CE1   1 
ATOM   2226 C CE2   . PHE A 1 283 ? -3.571  43.087 19.267  1.00 20.67 ?  283 PHE A CE2   1 
ATOM   2227 C CZ    . PHE A 1 283 ? -4.730  42.361 19.188  1.00 21.09 ?  283 PHE A CZ    1 
ATOM   2228 N N     . HIS A 1 284 ? 0.314   42.974 15.842  1.00 20.68 ?  284 HIS A N     1 
ATOM   2229 C CA    . HIS A 1 284 ? 0.450   44.351 15.365  1.00 23.87 ?  284 HIS A CA    1 
ATOM   2230 C C     . HIS A 1 284 ? 0.505   44.428 13.843  1.00 19.20 ?  284 HIS A C     1 
ATOM   2231 O O     . HIS A 1 284 ? -0.154  45.281 13.237  1.00 21.11 ?  284 HIS A O     1 
ATOM   2232 C CB    . HIS A 1 284 ? 1.698   45.011 15.962  1.00 28.78 ?  284 HIS A CB    1 
ATOM   2233 C CG    . HIS A 1 284 ? 1.553   45.387 17.405  1.00 28.55 ?  284 HIS A CG    1 
ATOM   2234 N ND1   . HIS A 1 284 ? 2.430   46.238 18.041  1.00 34.63 ?  284 HIS A ND1   1 
ATOM   2235 C CD2   . HIS A 1 284 ? 0.642   45.019 18.338  1.00 29.59 ?  284 HIS A CD2   1 
ATOM   2236 C CE1   . HIS A 1 284 ? 2.064   46.382 19.304  1.00 37.56 ?  284 HIS A CE1   1 
ATOM   2237 N NE2   . HIS A 1 284 ? 0.982   45.652 19.510  1.00 34.64 ?  284 HIS A NE2   1 
ATOM   2238 N N     . GLU A 1 285 ? 1.324   43.588 13.204  1.00 21.18 ?  285 GLU A N     1 
ATOM   2239 C CA    . GLU A 1 285 ? 1.415   43.649 11.747  1.00 20.21 ?  285 GLU A CA    1 
ATOM   2240 C C     . GLU A 1 285 ? 0.043   43.425 11.115  1.00 19.84 ?  285 GLU A C     1 
ATOM   2241 O O     . GLU A 1 285 ? -0.345  44.148 10.192  1.00 21.07 ?  285 GLU A O     1 
ATOM   2242 C CB    . GLU A 1 285 ? 2.427   42.621 11.211  1.00 18.55 ?  285 GLU A CB    1 
ATOM   2243 C CG    . GLU A 1 285 ? 3.934   42.932 11.502  1.00 20.32 ?  285 GLU A CG    1 
ATOM   2244 C CD    . GLU A 1 285 ? 4.369   44.340 11.067  1.00 27.92 ?  285 GLU A CD    1 
ATOM   2245 O OE1   . GLU A 1 285 ? 4.727   44.533 9.880   1.00 26.56 ?  285 GLU A OE1   1 
ATOM   2246 O OE2   . GLU A 1 285 ? 4.344   45.267 11.912  1.00 33.51 -1 285 GLU A OE2   1 
ATOM   2247 N N     . LEU A 1 286 ? -0.712  42.435 11.601  1.00 19.38 ?  286 LEU A N     1 
ATOM   2248 C CA    . LEU A 1 286 ? -2.045  42.194 11.047  1.00 17.78 ?  286 LEU A CA    1 
ATOM   2249 C C     . LEU A 1 286 ? -2.921  43.437 11.152  1.00 17.34 ?  286 LEU A C     1 
ATOM   2250 O O     . LEU A 1 286 ? -3.564  43.841 10.172  1.00 17.65 ?  286 LEU A O     1 
ATOM   2251 C CB    . LEU A 1 286 ? -2.720  41.011 11.754  1.00 16.75 ?  286 LEU A CB    1 
ATOM   2252 C CG    . LEU A 1 286 ? -4.166  40.673 11.316  1.00 21.84 ?  286 LEU A CG    1 
ATOM   2253 C CD1   . LEU A 1 286 ? -4.211  40.316 9.840   1.00 16.94 ?  286 LEU A CD1   1 
ATOM   2254 C CD2   . LEU A 1 286 ? -4.812  39.570 12.167  1.00 20.14 ?  286 LEU A CD2   1 
ATOM   2255 N N     . LEU A 1 287 ? -2.977  44.048 12.341  1.00 21.82 ?  287 LEU A N     1 
ATOM   2256 C CA    . LEU A 1 287 ? -3.916  45.155 12.554  1.00 24.26 ?  287 LEU A CA    1 
ATOM   2257 C C     . LEU A 1 287 ? -3.474  46.408 11.805  1.00 20.34 ?  287 LEU A C     1 
ATOM   2258 O O     . LEU A 1 287 ? -4.302  47.103 11.200  1.00 20.41 ?  287 LEU A O     1 
ATOM   2259 C CB    . LEU A 1 287 ? -4.077  45.448 14.050  1.00 19.11 ?  287 LEU A CB    1 
ATOM   2260 C CG    . LEU A 1 287 ? -4.757  44.347 14.864  1.00 24.00 ?  287 LEU A CG    1 
ATOM   2261 C CD1   . LEU A 1 287 ? -4.904  44.800 16.316  1.00 24.79 ?  287 LEU A CD1   1 
ATOM   2262 C CD2   . LEU A 1 287 ? -6.105  43.972 14.278  1.00 19.29 ?  287 LEU A CD2   1 
ATOM   2263 N N     . LEU A 1 288 ? -2.175  46.705 11.822  1.00 18.72 ?  288 LEU A N     1 
ATOM   2264 C CA    . LEU A 1 288 ? -1.665  47.816 11.018  1.00 22.48 ?  288 LEU A CA    1 
ATOM   2265 C C     . LEU A 1 288 ? -1.891  47.569 9.529   1.00 19.94 ?  288 LEU A C     1 
ATOM   2266 O O     . LEU A 1 288 ? -2.240  48.493 8.792   1.00 21.43 ?  288 LEU A O     1 
ATOM   2267 C CB    . LEU A 1 288 ? -0.181  48.055 11.323  1.00 18.87 ?  288 LEU A CB    1 
ATOM   2268 C CG    . LEU A 1 288 ? 0.154   48.551 12.740  1.00 22.64 ?  288 LEU A CG    1 
ATOM   2269 C CD1   . LEU A 1 288 ? 1.674   48.466 13.069  1.00 18.77 ?  288 LEU A CD1   1 
ATOM   2270 C CD2   . LEU A 1 288 ? -0.320  49.977 12.926  1.00 22.34 ?  288 LEU A CD2   1 
ATOM   2271 N N     . GLY A 1 289 ? -1.742  46.323 9.071   1.00 19.31 ?  289 GLY A N     1 
ATOM   2272 C CA    . GLY A 1 289 ? -2.065  46.023 7.680   1.00 17.45 ?  289 GLY A CA    1 
ATOM   2273 C C     . GLY A 1 289 ? -3.522  46.294 7.330   1.00 18.44 ?  289 GLY A C     1 
ATOM   2274 O O     . GLY A 1 289 ? -3.824  46.861 6.282   1.00 18.44 ?  289 GLY A O     1 
ATOM   2275 N N     . LEU A 1 290 ? -4.451  45.886 8.197   1.00 19.29 ?  290 LEU A N     1 
ATOM   2276 C CA    . LEU A 1 290 ? -5.850  46.197 7.934   1.00 17.49 ?  290 LEU A CA    1 
ATOM   2277 C C     . LEU A 1 290 ? -6.067  47.703 7.893   1.00 22.41 ?  290 LEU A C     1 
ATOM   2278 O O     . LEU A 1 290 ? -6.752  48.215 6.999   1.00 22.41 ?  290 LEU A O     1 
ATOM   2279 C CB    . LEU A 1 290 ? -6.739  45.549 8.993   1.00 19.15 ?  290 LEU A CB    1 
ATOM   2280 C CG    . LEU A 1 290 ? -6.798  44.019 8.993   1.00 19.87 ?  290 LEU A CG    1 
ATOM   2281 C CD1   . LEU A 1 290 ? -7.672  43.532 10.129  1.00 15.32 ?  290 LEU A CD1   1 
ATOM   2282 C CD2   . LEU A 1 290 ? -7.287  43.460 7.660   1.00 17.58 ?  290 LEU A CD2   1 
ATOM   2283 N N     . GLU A 1 291 ? -5.466  48.427 8.843   1.00 22.72 ?  291 GLU A N     1 
ATOM   2284 C CA    . GLU A 1 291 ? -5.599  49.881 8.883   1.00 26.02 ?  291 GLU A CA    1 
ATOM   2285 C C     . GLU A 1 291 ? -5.089  50.528 7.601   1.00 25.33 ?  291 GLU A C     1 
ATOM   2286 O O     . GLU A 1 291 ? -5.679  51.501 7.117   1.00 25.90 ?  291 GLU A O     1 
ATOM   2287 C CB    . GLU A 1 291 ? -4.857  50.453 10.095  1.00 24.18 ?  291 GLU A CB    1 
ATOM   2288 C CG    . GLU A 1 291 ? -4.774  51.975 10.025  1.00 29.08 ?  291 GLU A CG    1 
ATOM   2289 C CD    . GLU A 1 291 ? -4.031  52.608 11.170  1.00 31.88 ?  291 GLU A CD    1 
ATOM   2290 O OE1   . GLU A 1 291 ? -3.118  51.964 11.741  1.00 30.58 ?  291 GLU A OE1   1 
ATOM   2291 O OE2   . GLU A 1 291 ? -4.343  53.781 11.473  1.00 39.56 -1 291 GLU A OE2   1 
ATOM   2292 N N     . LEU A 1 292 ? -3.997  49.998 7.033   1.00 22.28 ?  292 LEU A N     1 
ATOM   2293 C CA    . LEU A 1 292 ? -3.396  50.583 5.837   1.00 23.92 ?  292 LEU A CA    1 
ATOM   2294 C C     . LEU A 1 292 ? -4.316  50.528 4.625   1.00 26.95 ?  292 LEU A C     1 
ATOM   2295 O O     . LEU A 1 292 ? -4.159  51.336 3.701   1.00 26.33 ?  292 LEU A O     1 
ATOM   2296 C CB    . LEU A 1 292 ? -2.089  49.864 5.484   1.00 21.27 ?  292 LEU A CB    1 
ATOM   2297 C CG    . LEU A 1 292 ? -0.826  50.207 6.266   1.00 28.66 ?  292 LEU A CG    1 
ATOM   2298 C CD1   . LEU A 1 292 ? 0.148   49.027 6.208   1.00 25.94 ?  292 LEU A CD1   1 
ATOM   2299 C CD2   . LEU A 1 292 ? -0.180  51.438 5.687   1.00 23.96 ?  292 LEU A CD2   1 
ATOM   2300 N N     . THR A 1 293 ? -5.251  49.581 4.584   1.00 20.66 ?  293 THR A N     1 
ATOM   2301 C CA    . THR A 1 293 ? -6.134  49.499 3.427   1.00 24.59 ?  293 THR A CA    1 
ATOM   2302 C C     . THR A 1 293 ? -7.123  50.654 3.382   1.00 27.61 ?  293 THR A C     1 
ATOM   2303 O O     . THR A 1 293 ? -7.620  51.001 2.304   1.00 28.14 ?  293 THR A O     1 
ATOM   2304 C CB    . THR A 1 293 ? -6.893  48.179 3.440   1.00 24.15 ?  293 THR A CB    1 
ATOM   2305 O OG1   . THR A 1 293 ? -7.900  48.228 4.454   1.00 20.73 ?  293 THR A OG1   1 
ATOM   2306 C CG2   . THR A 1 293 ? -5.928  47.007 3.742   1.00 21.37 ?  293 THR A CG2   1 
ATOM   2307 N N     . GLY A 1 294 ? -7.447  51.241 4.531   1.00 24.10 ?  294 GLY A N     1 
ATOM   2308 C CA    . GLY A 1 294 ? -8.463  52.265 4.586   1.00 26.17 ?  294 GLY A CA    1 
ATOM   2309 C C     . GLY A 1 294 ? -9.888  51.759 4.628   1.00 32.28 ?  294 GLY A C     1 
ATOM   2310 O O     . GLY A 1 294 ? -10.812 52.572 4.789   1.00 27.63 ?  294 GLY A O     1 
ATOM   2311 N N     . PHE A 1 295 ? -10.107 50.445 4.471   1.00 24.88 ?  295 PHE A N     1 
ATOM   2312 C CA    . PHE A 1 295 ? -11.464 49.932 4.540   1.00 25.91 ?  295 PHE A CA    1 
ATOM   2313 C C     . PHE A 1 295 ? -11.883 49.741 5.995   1.00 26.79 ?  295 PHE A C     1 
ATOM   2314 O O     . PHE A 1 295 ? -11.034 49.544 6.872   1.00 25.30 ?  295 PHE A O     1 
ATOM   2315 C CB    . PHE A 1 295 ? -11.577 48.604 3.800   1.00 28.19 ?  295 PHE A CB    1 
ATOM   2316 C CG    . PHE A 1 295 ? -11.110 48.661 2.376   1.00 25.73 ?  295 PHE A CG    1 
ATOM   2317 C CD1   . PHE A 1 295 ? -11.707 49.521 1.473   1.00 36.12 ?  295 PHE A CD1   1 
ATOM   2318 C CD2   . PHE A 1 295 ? -10.089 47.843 1.938   1.00 25.33 ?  295 PHE A CD2   1 
ATOM   2319 C CE1   . PHE A 1 295 ? -11.275 49.576 0.149   1.00 37.47 ?  295 PHE A CE1   1 
ATOM   2320 C CE2   . PHE A 1 295 ? -9.645  47.892 0.620   1.00 33.18 ?  295 PHE A CE2   1 
ATOM   2321 C CZ    . PHE A 1 295 ? -10.236 48.765 -0.275  1.00 27.23 ?  295 PHE A CZ    1 
ATOM   2322 N N     . PRO A 1 296 ? -13.181 49.831 6.285   1.00 21.64 ?  296 PRO A N     1 
ATOM   2323 C CA    . PRO A 1 296 ? -13.653 49.415 7.608   1.00 23.56 ?  296 PRO A CA    1 
ATOM   2324 C C     . PRO A 1 296 ? -13.348 47.941 7.819   1.00 21.30 ?  296 PRO A C     1 
ATOM   2325 O O     . PRO A 1 296 ? -13.287 47.160 6.866   1.00 22.41 ?  296 PRO A O     1 
ATOM   2326 C CB    . PRO A 1 296 ? -15.169 49.685 7.562   1.00 27.51 ?  296 PRO A CB    1 
ATOM   2327 C CG    . PRO A 1 296 ? -15.520 49.877 6.128   1.00 23.55 ?  296 PRO A CG    1 
ATOM   2328 C CD    . PRO A 1 296 ? -14.265 50.343 5.428   1.00 24.20 ?  296 PRO A CD    1 
ATOM   2329 N N     . PHE A 1 297 ? -13.141 47.561 9.078   1.00 22.54 ?  297 PHE A N     1 
ATOM   2330 C CA    . PHE A 1 297 ? -12.801 46.174 9.375   1.00 20.91 ?  297 PHE A CA    1 
ATOM   2331 C C     . PHE A 1 297 ? -13.349 45.787 10.735  1.00 18.42 ?  297 PHE A C     1 
ATOM   2332 O O     . PHE A 1 297 ? -13.540 46.632 11.614  1.00 21.06 ?  297 PHE A O     1 
ATOM   2333 C CB    . PHE A 1 297 ? -11.278 45.925 9.339   1.00 17.52 ?  297 PHE A CB    1 
ATOM   2334 C CG    . PHE A 1 297 ? -10.510 46.738 10.341  1.00 18.30 ?  297 PHE A CG    1 
ATOM   2335 C CD1   . PHE A 1 297 ? -10.324 46.279 11.640  1.00 20.49 ?  297 PHE A CD1   1 
ATOM   2336 C CD2   . PHE A 1 297 ? -9.989  47.975 9.990   1.00 22.42 ?  297 PHE A CD2   1 
ATOM   2337 C CE1   . PHE A 1 297 ? -9.611  47.033 12.571  1.00 20.84 ?  297 PHE A CE1   1 
ATOM   2338 C CE2   . PHE A 1 297 ? -9.283  48.734 10.912  1.00 23.00 ?  297 PHE A CE2   1 
ATOM   2339 C CZ    . PHE A 1 297 ? -9.098  48.260 12.208  1.00 23.26 ?  297 PHE A CZ    1 
ATOM   2340 N N     . LEU A 1 298 ? -13.600 44.491 10.888  1.00 14.38 ?  298 LEU A N     1 
ATOM   2341 C CA    . LEU A 1 298 ? -13.953 43.871 12.156  1.00 18.12 ?  298 LEU A CA    1 
ATOM   2342 C C     . LEU A 1 298 ? -13.008 42.691 12.350  1.00 21.12 ?  298 LEU A C     1 
ATOM   2343 O O     . LEU A 1 298 ? -13.035 41.734 11.570  1.00 18.15 ?  298 LEU A O     1 
ATOM   2344 C CB    . LEU A 1 298 ? -15.416 43.413 12.154  1.00 17.27 ?  298 LEU A CB    1 
ATOM   2345 C CG    . LEU A 1 298 ? -15.886 42.595 13.351  1.00 20.54 ?  298 LEU A CG    1 
ATOM   2346 C CD1   . LEU A 1 298 ? -15.623 43.323 14.647  1.00 21.64 ?  298 LEU A CD1   1 
ATOM   2347 C CD2   . LEU A 1 298 ? -17.394 42.250 13.209  1.00 22.43 ?  298 LEU A CD2   1 
ATOM   2348 N N     . ALA A 1 299 ? -12.146 42.760 13.356  1.00 17.52 ?  299 ALA A N     1 
ATOM   2349 C CA    . ALA A 1 299 ? -11.181 41.696 13.592  1.00 18.76 ?  299 ALA A CA    1 
ATOM   2350 C C     . ALA A 1 299 ? -11.556 40.980 14.880  1.00 20.36 ?  299 ALA A C     1 
ATOM   2351 O O     . ALA A 1 299 ? -11.628 41.609 15.939  1.00 20.47 ?  299 ALA A O     1 
ATOM   2352 C CB    . ALA A 1 299 ? -9.757  42.254 13.650  1.00 18.94 ?  299 ALA A CB    1 
ATOM   2353 N N     . ILE A 1 300 ? -11.795 39.676 14.785  1.00 16.92 ?  300 ILE A N     1 
ATOM   2354 C CA    . ILE A 1 300 ? -12.160 38.850 15.932  1.00 18.63 ?  300 ILE A CA    1 
ATOM   2355 C C     . ILE A 1 300 ? -10.922 38.048 16.312  1.00 20.16 ?  300 ILE A C     1 
ATOM   2356 O O     . ILE A 1 300 ? -10.573 37.060 15.652  1.00 20.83 ?  300 ILE A O     1 
ATOM   2357 C CB    . ILE A 1 300 ? -13.357 37.948 15.626  1.00 21.80 ?  300 ILE A CB    1 
ATOM   2358 C CG1   . ILE A 1 300 ? -14.535 38.784 15.113  1.00 18.11 ?  300 ILE A CG1   1 
ATOM   2359 C CG2   . ILE A 1 300 ? -13.752 37.147 16.873  1.00 23.46 ?  300 ILE A CG2   1 
ATOM   2360 C CD1   . ILE A 1 300 ? -14.881 39.928 16.036  1.00 19.49 ?  300 ILE A CD1   1 
ATOM   2361 N N     . LEU A 1 301 ? -10.255 38.475 17.381  1.00 20.94 ?  301 LEU A N     1 
ATOM   2362 C CA    . LEU A 1 301 ? -8.925  37.989 17.732  1.00 21.49 ?  301 LEU A CA    1 
ATOM   2363 C C     . LEU A 1 301 ? -8.803  37.854 19.242  1.00 25.10 ?  301 LEU A C     1 
ATOM   2364 O O     . LEU A 1 301 ? -9.279  38.720 19.985  1.00 24.92 ?  301 LEU A O     1 
ATOM   2365 C CB    . LEU A 1 301 ? -7.835  38.959 17.248  1.00 24.12 ?  301 LEU A CB    1 
ATOM   2366 C CG    . LEU A 1 301 ? -7.587  39.128 15.753  1.00 23.41 ?  301 LEU A CG    1 
ATOM   2367 C CD1   . LEU A 1 301 ? -6.783  40.401 15.504  1.00 20.15 ?  301 LEU A CD1   1 
ATOM   2368 C CD2   . LEU A 1 301 ? -6.859  37.895 15.198  1.00 25.42 ?  301 LEU A CD2   1 
ATOM   2369 N N     . LYS A 1 302 ? -8.153  36.785 19.691  1.00 22.04 ?  302 LYS A N     1 
ATOM   2370 C CA    . LYS A 1 302 ? -7.744  36.720 21.088  1.00 28.00 ?  302 LYS A CA    1 
ATOM   2371 C C     . LYS A 1 302 ? -6.627  37.736 21.336  1.00 27.66 ?  302 LYS A C     1 
ATOM   2372 O O     . LYS A 1 302 ? -5.919  38.128 20.399  1.00 25.91 ?  302 LYS A O     1 
ATOM   2373 C CB    . LYS A 1 302 ? -7.267  35.315 21.451  1.00 26.60 ?  302 LYS A CB    1 
ATOM   2374 C CG    . LYS A 1 302 ? -8.423  34.322 21.726  1.00 33.41 ?  302 LYS A CG    1 
ATOM   2375 C CD    . LYS A 1 302 ? -7.923  33.003 22.348  1.00 37.95 ?  302 LYS A CD    1 
ATOM   2376 C CE    . LYS A 1 302 ? -9.049  31.972 22.534  1.00 38.68 ?  302 LYS A CE    1 
ATOM   2377 N NZ    . LYS A 1 302 ? -10.187 32.539 23.341  1.00 39.75 ?  302 LYS A NZ    1 
ATOM   2378 N N     . PRO A 1 303 ? -6.463  38.205 22.572  1.00 28.06 ?  303 PRO A N     1 
ATOM   2379 C CA    . PRO A 1 303 ? -5.299  39.028 22.880  1.00 25.78 ?  303 PRO A CA    1 
ATOM   2380 C C     . PRO A 1 303 ? -4.027  38.212 22.669  1.00 25.95 ?  303 PRO A C     1 
ATOM   2381 O O     . PRO A 1 303 ? -4.037  36.982 22.833  1.00 23.97 ?  303 PRO A O     1 
ATOM   2382 C CB    . PRO A 1 303 ? -5.499  39.399 24.356  1.00 30.14 ?  303 PRO A CB    1 
ATOM   2383 C CG    . PRO A 1 303 ? -6.948  39.184 24.627  1.00 31.84 ?  303 PRO A CG    1 
ATOM   2384 C CD    . PRO A 1 303 ? -7.339  38.031 23.746  1.00 30.59 ?  303 PRO A CD    1 
ATOM   2385 N N     . PRO A 1 304 ? -2.942  38.857 22.266  1.00 24.72 ?  304 PRO A N     1 
ATOM   2386 C CA    . PRO A 1 304 ? -1.727  38.097 21.944  1.00 24.25 ?  304 PRO A CA    1 
ATOM   2387 C C     . PRO A 1 304 ? -1.125  37.438 23.179  1.00 28.71 ?  304 PRO A C     1 
ATOM   2388 O O     . PRO A 1 304 ? -1.461  37.752 24.323  1.00 28.64 ?  304 PRO A O     1 
ATOM   2389 C CB    . PRO A 1 304 ? -0.781  39.149 21.354  1.00 25.73 ?  304 PRO A CB    1 
ATOM   2390 C CG    . PRO A 1 304 ? -1.349  40.450 21.712  1.00 26.60 ?  304 PRO A CG    1 
ATOM   2391 C CD    . PRO A 1 304 ? -2.814  40.280 21.942  1.00 21.90 ?  304 PRO A CD    1 
ATOM   2392 N N     . VAL A 1 305 ? -0.198  36.509 22.915  1.00 27.02 ?  305 VAL A N     1 
ATOM   2393 C CA    . VAL A 1 305 ? 0.495   35.784 23.971  1.00 30.99 ?  305 VAL A CA    1 
ATOM   2394 C C     . VAL A 1 305 ? 1.049   36.764 24.994  1.00 30.84 ?  305 VAL A C     1 
ATOM   2395 O O     . VAL A 1 305 ? 1.668   37.773 24.642  1.00 28.03 ?  305 VAL A O     1 
ATOM   2396 C CB    . VAL A 1 305 ? 1.618   34.914 23.373  1.00 32.16 ?  305 VAL A CB    1 
ATOM   2397 C CG1   . VAL A 1 305 ? 2.482   34.323 24.479  1.00 31.88 ?  305 VAL A CG1   1 
ATOM   2398 C CG2   . VAL A 1 305 ? 1.032   33.816 22.497  1.00 32.86 ?  305 VAL A CG2   1 
ATOM   2399 N N     . GLY A 1 306 ? 0.813   36.469 26.270  1.00 29.33 ?  306 GLY A N     1 
ATOM   2400 C CA    . GLY A 1 306 ? 1.286   37.301 27.344  1.00 33.80 ?  306 GLY A CA    1 
ATOM   2401 C C     . GLY A 1 306 ? 0.350   38.411 27.750  1.00 31.78 ?  306 GLY A C     1 
ATOM   2402 O O     . GLY A 1 306 ? 0.555   39.002 28.814  1.00 30.70 ?  306 GLY A O     1 
ATOM   2403 N N     . PHE A 1 307 ? -0.670  38.712 26.943  1.00 34.93 ?  307 PHE A N     1 
ATOM   2404 C CA    . PHE A 1 307 ? -1.586  39.821 27.186  1.00 30.07 ?  307 PHE A CA    1 
ATOM   2405 C C     . PHE A 1 307 ? -2.979  39.287 27.499  1.00 37.20 ?  307 PHE A C     1 
ATOM   2406 O O     . PHE A 1 307 ? -3.375  38.222 27.019  1.00 36.47 ?  307 PHE A O     1 
ATOM   2407 C CB    . PHE A 1 307 ? -1.658  40.757 25.975  1.00 30.26 ?  307 PHE A CB    1 
ATOM   2408 C CG    . PHE A 1 307 ? -0.419  41.578 25.762  1.00 32.36 ?  307 PHE A CG    1 
ATOM   2409 C CD1   . PHE A 1 307 ? 0.689   41.040 25.123  1.00 31.57 ?  307 PHE A CD1   1 
ATOM   2410 C CD2   . PHE A 1 307 ? -0.367  42.894 26.202  1.00 32.20 ?  307 PHE A CD2   1 
ATOM   2411 C CE1   . PHE A 1 307 ? 1.841   41.802 24.925  1.00 33.17 ?  307 PHE A CE1   1 
ATOM   2412 C CE2   . PHE A 1 307 ? 0.775   43.661 26.022  1.00 34.59 ?  307 PHE A CE2   1 
ATOM   2413 C CZ    . PHE A 1 307 ? 1.885   43.116 25.378  1.00 36.11 ?  307 PHE A CZ    1 
ATOM   2414 N N     . GLU A 1 308 ? -3.740  40.030 28.305  1.00 40.29 ?  308 GLU A N     1 
ATOM   2415 C CA    . GLU A 1 308 ? -5.063  39.546 28.674  1.00 42.94 ?  308 GLU A CA    1 
ATOM   2416 C C     . GLU A 1 308 ? -6.216  40.381 28.148  1.00 33.14 ?  308 GLU A C     1 
ATOM   2417 O O     . GLU A 1 308 ? -7.351  39.902 28.177  1.00 38.01 ?  308 GLU A O     1 
ATOM   2418 C CB    . GLU A 1 308 ? -5.192  39.413 30.199  1.00 45.79 ?  308 GLU A CB    1 
ATOM   2419 C CG    . GLU A 1 308 ? -6.009  38.201 30.612  1.00 51.62 ?  308 GLU A CG    1 
ATOM   2420 C CD    . GLU A 1 308 ? -5.557  36.911 29.917  1.00 60.53 ?  308 GLU A CD    1 
ATOM   2421 O OE1   . GLU A 1 308 ? -4.659  36.227 30.456  1.00 64.79 ?  308 GLU A OE1   1 
ATOM   2422 O OE2   . GLU A 1 308 ? -6.115  36.564 28.848  1.00 62.00 -1 308 GLU A OE2   1 
ATOM   2423 N N     . THR A 1 309 ? -5.974  41.601 27.675  1.00 31.21 ?  309 THR A N     1 
ATOM   2424 C CA    . THR A 1 309 ? -7.012  42.415 27.064  1.00 32.95 ?  309 THR A CA    1 
ATOM   2425 C C     . THR A 1 309 ? -6.529  42.934 25.716  1.00 31.98 ?  309 THR A C     1 
ATOM   2426 O O     . THR A 1 309 ? -5.335  43.187 25.518  1.00 33.27 ?  309 THR A O     1 
ATOM   2427 C CB    . THR A 1 309 ? -7.421  43.590 27.975  1.00 35.41 ?  309 THR A CB    1 
ATOM   2428 O OG1   . THR A 1 309 ? -6.734  44.782 27.588  1.00 36.81 ?  309 THR A OG1   1 
ATOM   2429 C CG2   . THR A 1 309 ? -7.046  43.293 29.393  1.00 38.39 ?  309 THR A CG2   1 
ATOM   2430 N N     . ILE A 1 310 ? -7.477  43.089 24.788  1.00 33.40 ?  310 ILE A N     1 
ATOM   2431 C CA    . ILE A 1 310 ? -7.165  43.630 23.467  1.00 31.60 ?  310 ILE A CA    1 
ATOM   2432 C C     . ILE A 1 310 ? -6.546  45.012 23.601  1.00 35.71 ?  310 ILE A C     1 
ATOM   2433 O O     . ILE A 1 310 ? -5.517  45.331 22.982  1.00 29.10 ?  310 ILE A O     1 
ATOM   2434 C CB    . ILE A 1 310 ? -8.437  43.677 22.598  1.00 30.31 ?  310 ILE A CB    1 
ATOM   2435 C CG1   . ILE A 1 310 ? -8.778  42.293 22.062  1.00 29.68 ?  310 ILE A CG1   1 
ATOM   2436 C CG2   . ILE A 1 310 ? -8.270  44.663 21.458  1.00 26.82 ?  310 ILE A CG2   1 
ATOM   2437 C CD1   . ILE A 1 310 ? -7.785  41.769 21.037  1.00 26.44 ?  310 ILE A CD1   1 
ATOM   2438 N N     . GLU A 1 311 ? -7.170  45.851 24.427  1.00 32.21 ?  311 GLU A N     1 
ATOM   2439 C CA    . GLU A 1 311 ? -6.763  47.246 24.520  1.00 36.10 ?  311 GLU A CA    1 
ATOM   2440 C C     . GLU A 1 311 ? -5.307  47.377 24.964  1.00 33.59 ?  311 GLU A C     1 
ATOM   2441 O O     . GLU A 1 311 ? -4.581  48.236 24.453  1.00 31.87 ?  311 GLU A O     1 
ATOM   2442 C CB    . GLU A 1 311 ? -7.712  47.996 25.459  1.00 39.46 ?  311 GLU A CB    1 
ATOM   2443 C CG    . GLU A 1 311 ? -9.197  48.090 24.956  1.00 49.78 ?  311 GLU A CG    1 
ATOM   2444 C CD    . GLU A 1 311 ? -9.942  46.734 24.827  1.00 48.84 ?  311 GLU A CD    1 
ATOM   2445 O OE1   . GLU A 1 311 ? -9.603  45.770 25.559  1.00 43.71 ?  311 GLU A OE1   1 
ATOM   2446 O OE2   . GLU A 1 311 ? -10.860 46.628 23.972  1.00 53.07 -1 311 GLU A OE2   1 
ATOM   2447 N N     . ASP A 1 312 ? -4.852  46.505 25.879  1.00 31.05 ?  312 ASP A N     1 
ATOM   2448 C CA    . ASP A 1 312 ? -3.454  46.527 26.329  1.00 30.70 ?  312 ASP A CA    1 
ATOM   2449 C C     . ASP A 1 312 ? -2.483  46.355 25.168  1.00 33.65 ?  312 ASP A C     1 
ATOM   2450 O O     . ASP A 1 312 ? -1.383  46.921 25.171  1.00 34.10 ?  312 ASP A O     1 
ATOM   2451 C CB    . ASP A 1 312 ? -3.189  45.409 27.348  1.00 33.87 ?  312 ASP A CB    1 
ATOM   2452 C CG    . ASP A 1 312 ? -3.802  45.683 28.718  1.00 38.59 ?  312 ASP A CG    1 
ATOM   2453 O OD1   . ASP A 1 312 ? -4.023  46.863 29.037  1.00 35.17 ?  312 ASP A OD1   1 
ATOM   2454 O OD2   . ASP A 1 312 ? -4.042  44.712 29.479  1.00 47.77 -1 312 ASP A OD2   1 
ATOM   2455 N N     . ALA A 1 313 ? -2.859  45.546 24.186  1.00 33.54 ?  313 ALA A N     1 
ATOM   2456 C CA    . ALA A 1 313 ? -1.950  45.070 23.161  1.00 31.25 ?  313 ALA A CA    1 
ATOM   2457 C C     . ALA A 1 313 ? -2.043  45.842 21.850  1.00 30.36 ?  313 ALA A C     1 
ATOM   2458 O O     . ALA A 1 313 ? -1.249  45.582 20.942  1.00 32.94 ?  313 ALA A O     1 
ATOM   2459 C CB    . ALA A 1 313 ? -2.217  43.590 22.910  1.00 28.45 ?  313 ALA A CB    1 
ATOM   2460 N N     . LEU A 1 314 ? -2.984  46.772 21.725  1.00 27.19 ?  314 LEU A N     1 
ATOM   2461 C CA    . LEU A 1 314 ? -3.155  47.496 20.476  1.00 26.72 ?  314 LEU A CA    1 
ATOM   2462 C C     . LEU A 1 314 ? -1.920  48.347 20.177  1.00 27.96 ?  314 LEU A C     1 
ATOM   2463 O O     . LEU A 1 314 ? -1.310  48.894 21.103  1.00 30.54 ?  314 LEU A O     1 
ATOM   2464 C CB    . LEU A 1 314 ? -4.389  48.389 20.567  1.00 25.81 ?  314 LEU A CB    1 
ATOM   2465 C CG    . LEU A 1 314 ? -5.761  47.727 20.474  1.00 30.74 ?  314 LEU A CG    1 
ATOM   2466 C CD1   . LEU A 1 314 ? -6.838  48.778 20.670  1.00 26.52 ?  314 LEU A CD1   1 
ATOM   2467 C CD2   . LEU A 1 314 ? -5.923  46.986 19.148  1.00 20.36 ?  314 LEU A CD2   1 
ATOM   2468 N N     . PRO A 1 315 ? -1.525  48.491 18.909  1.00 28.31 ?  315 PRO A N     1 
ATOM   2469 C CA    . PRO A 1 315 ? -0.408  49.397 18.589  1.00 30.29 ?  315 PRO A CA    1 
ATOM   2470 C C     . PRO A 1 315 ? -0.709  50.806 19.083  1.00 31.77 ?  315 PRO A C     1 
ATOM   2471 O O     . PRO A 1 315 ? -1.869  51.210 19.186  1.00 26.30 ?  315 PRO A O     1 
ATOM   2472 C CB    . PRO A 1 315 ? -0.327  49.347 17.056  1.00 28.73 ?  315 PRO A CB    1 
ATOM   2473 C CG    . PRO A 1 315 ? -1.061  48.126 16.660  1.00 27.72 ?  315 PRO A CG    1 
ATOM   2474 C CD    . PRO A 1 315 ? -2.111  47.880 17.700  1.00 25.70 ?  315 PRO A CD    1 
ATOM   2475 N N     . GLU A 1 316 ? 0.342   51.559 19.412  1.00 33.64 ?  316 GLU A N     1 
ATOM   2476 C CA    . GLU A 1 316 ? 0.131   52.866 20.038  1.00 32.18 ?  316 GLU A CA    1 
ATOM   2477 C C     . GLU A 1 316 ? -0.566  53.829 19.075  1.00 33.98 ?  316 GLU A C     1 
ATOM   2478 O O     . GLU A 1 316 ? -0.184  53.939 17.906  1.00 32.71 ?  316 GLU A O     1 
ATOM   2479 C CB    . GLU A 1 316 ? 1.455   53.459 20.517  1.00 41.51 ?  316 GLU A CB    1 
ATOM   2480 C CG    . GLU A 1 316 ? 1.251   54.676 21.427  1.00 47.91 ?  316 GLU A CG    1 
ATOM   2481 C CD    . GLU A 1 316 ? 2.548   55.240 21.992  1.00 61.13 ?  316 GLU A CD    1 
ATOM   2482 O OE1   . GLU A 1 316 ? 3.582   54.533 21.948  1.00 62.90 ?  316 GLU A OE1   1 
ATOM   2483 O OE2   . GLU A 1 316 ? 2.531   56.397 22.480  1.00 66.58 -1 316 GLU A OE2   1 
ATOM   2484 N N     . GLY A 1 317 ? -1.606  54.515 19.566  1.00 34.17 ?  317 GLY A N     1 
ATOM   2485 C CA    . GLY A 1 317 ? -2.402  55.412 18.751  1.00 36.45 ?  317 GLY A CA    1 
ATOM   2486 C C     . GLY A 1 317 ? -3.469  54.752 17.893  1.00 36.47 ?  317 GLY A C     1 
ATOM   2487 O O     . GLY A 1 317 ? -4.244  55.462 17.234  1.00 33.96 ?  317 GLY A O     1 
ATOM   2488 N N     . PHE A 1 318 ? -3.544  53.422 17.895  1.00 35.85 ?  318 PHE A N     1 
ATOM   2489 C CA    . PHE A 1 318 ? -4.370  52.704 16.929  1.00 31.88 ?  318 PHE A CA    1 
ATOM   2490 C C     . PHE A 1 318 ? -5.848  53.059 17.077  1.00 32.63 ?  318 PHE A C     1 
ATOM   2491 O O     . PHE A 1 318 ? -6.522  53.403 16.096  1.00 29.59 ?  318 PHE A O     1 
ATOM   2492 C CB    . PHE A 1 318 ? -4.150  51.200 17.109  1.00 30.14 ?  318 PHE A CB    1 
ATOM   2493 C CG    . PHE A 1 318 ? -4.867  50.359 16.109  1.00 26.28 ?  318 PHE A CG    1 
ATOM   2494 C CD1   . PHE A 1 318 ? -4.314  50.142 14.852  1.00 26.16 ?  318 PHE A CD1   1 
ATOM   2495 C CD2   . PHE A 1 318 ? -6.086  49.777 16.422  1.00 27.93 ?  318 PHE A CD2   1 
ATOM   2496 C CE1   . PHE A 1 318 ? -4.967  49.362 13.918  1.00 25.66 ?  318 PHE A CE1   1 
ATOM   2497 C CE2   . PHE A 1 318 ? -6.749  48.980 15.495  1.00 27.46 ?  318 PHE A CE2   1 
ATOM   2498 C CZ    . PHE A 1 318 ? -6.191  48.781 14.240  1.00 24.57 ?  318 PHE A CZ    1 
ATOM   2499 N N     . LYS A 1 319 ? -6.369  52.983 18.300  1.00 31.82 ?  319 LYS A N     1 
ATOM   2500 C CA    . LYS A 1 319 ? -7.791  53.241 18.500  1.00 38.34 ?  319 LYS A CA    1 
ATOM   2501 C C     . LYS A 1 319 ? -8.148  54.667 18.108  1.00 39.70 ?  319 LYS A C     1 
ATOM   2502 O O     . LYS A 1 319 ? -9.187  54.896 17.479  1.00 37.59 ?  319 LYS A O     1 
ATOM   2503 C CB    . LYS A 1 319 ? -8.188  52.960 19.948  1.00 42.28 ?  319 LYS A CB    1 
ATOM   2504 C CG    . LYS A 1 319 ? -9.691  52.728 20.126  1.00 50.54 ?  319 LYS A CG    1 
ATOM   2505 C CD    . LYS A 1 319 ? -10.031 52.017 21.433  1.00 52.16 ?  319 LYS A CD    1 
ATOM   2506 C CE    . LYS A 1 319 ? -9.676  52.859 22.644  1.00 47.20 ?  319 LYS A CE    1 
ATOM   2507 N NZ    . LYS A 1 319 ? -8.253  52.664 23.054  1.00 51.16 ?  319 LYS A NZ    1 
ATOM   2508 N N     . GLU A 1 320 ? -7.271  55.634 18.419  1.00 40.86 ?  320 GLU A N     1 
ATOM   2509 C CA    . GLU A 1 320 ? -7.546  57.032 18.077  1.00 41.74 ?  320 GLU A CA    1 
ATOM   2510 C C     . GLU A 1 320 ? -7.502  57.297 16.577  1.00 43.10 ?  320 GLU A C     1 
ATOM   2511 O O     . GLU A 1 320 ? -8.096  58.280 16.117  1.00 43.50 ?  320 GLU A O     1 
ATOM   2512 C CB    . GLU A 1 320 ? -6.563  57.976 18.783  1.00 42.77 ?  320 GLU A CB    1 
ATOM   2513 C CG    . GLU A 1 320 ? -6.325  57.670 20.238  1.00 42.48 ?  320 GLU A CG    1 
ATOM   2514 C CD    . GLU A 1 320 ? -5.002  56.961 20.442  1.00 56.85 ?  320 GLU A CD    1 
ATOM   2515 O OE1   . GLU A 1 320 ? -5.007  55.706 20.494  1.00 51.54 ?  320 GLU A OE1   1 
ATOM   2516 O OE2   . GLU A 1 320 ? -3.956  57.656 20.515  1.00 61.57 -1 320 GLU A OE2   1 
ATOM   2517 N N     . ARG A 1 321 ? -6.816  56.460 15.803  1.00 39.97 ?  321 ARG A N     1 
ATOM   2518 C CA    . ARG A 1 321 ? -6.770  56.659 14.360  1.00 32.56 ?  321 ARG A CA    1 
ATOM   2519 C C     . ARG A 1 321 ? -7.968  56.022 13.658  1.00 38.73 ?  321 ARG A C     1 
ATOM   2520 O O     . ARG A 1 321 ? -8.646  56.672 12.853  1.00 37.01 ?  321 ARG A O     1 
ATOM   2521 C CB    . ARG A 1 321 ? -5.468  56.089 13.799  1.00 32.86 ?  321 ARG A CB    1 
ATOM   2522 C CG    . ARG A 1 321 ? -4.205  56.804 14.274  1.00 36.83 ?  321 ARG A CG    1 
ATOM   2523 C CD    . ARG A 1 321 ? -3.006  56.448 13.402  1.00 27.20 ?  321 ARG A CD    1 
ATOM   2524 N NE    . ARG A 1 321 ? -2.698  55.020 13.429  1.00 31.92 ?  321 ARG A NE    1 
ATOM   2525 C CZ    . ARG A 1 321 ? -1.852  54.448 14.277  1.00 30.80 ?  321 ARG A CZ    1 
ATOM   2526 N NH1   . ARG A 1 321 ? -1.221  55.149 15.202  1.00 27.74 ?  321 ARG A NH1   1 
ATOM   2527 N NH2   . ARG A 1 321 ? -1.642  53.135 14.201  1.00 28.95 ?  321 ARG A NH2   1 
ATOM   2528 N N     . VAL A 1 322 ? -8.246  54.752 13.953  1.00 36.95 ?  322 VAL A N     1 
ATOM   2529 C CA    . VAL A 1 322 ? -9.261  54.044 13.184  1.00 37.05 ?  322 VAL A CA    1 
ATOM   2530 C C     . VAL A 1 322 ? -10.667 54.457 13.596  1.00 40.44 ?  322 VAL A C     1 
ATOM   2531 O O     . VAL A 1 322 ? -11.595 54.337 12.788  1.00 43.71 ?  322 VAL A O     1 
ATOM   2532 C CB    . VAL A 1 322 ? -9.054  52.524 13.294  1.00 34.07 ?  322 VAL A CB    1 
ATOM   2533 C CG1   . VAL A 1 322 ? -7.548  52.190 13.255  1.00 25.13 ?  322 VAL A CG1   1 
ATOM   2534 C CG2   . VAL A 1 322 ? -9.691  51.991 14.541  1.00 32.88 ?  322 VAL A CG2   1 
ATOM   2535 N N     . LYS A 1 323 ? -10.843 54.965 14.815  1.00 39.81 ?  323 LYS A N     1 
ATOM   2536 C CA    . LYS A 1 323 ? -12.094 55.609 15.251  1.00 40.28 ?  323 LYS A CA    1 
ATOM   2537 C C     . LYS A 1 323 ? -13.237 54.610 15.095  1.00 42.98 ?  323 LYS A C     1 
ATOM   2538 O O     . LYS A 1 323 ? -13.129 53.480 15.596  1.00 44.79 ?  323 LYS A O     1 
ATOM   2539 C CB    . LYS A 1 323 ? -12.284 56.913 14.493  1.00 42.75 ?  323 LYS A CB    1 
ATOM   2540 C CG    . LYS A 1 323 ? -11.181 57.916 14.665  1.00 43.76 ?  323 LYS A CG    1 
ATOM   2541 C CD    . LYS A 1 323 ? -11.236 58.911 13.526  1.00 48.02 ?  323 LYS A CD    1 
ATOM   2542 C CE    . LYS A 1 323 ? -11.106 60.321 14.048  1.00 46.68 ?  323 LYS A CE    1 
ATOM   2543 N NZ    . LYS A 1 323 ? -9.673  60.642 14.259  1.00 51.54 ?  323 LYS A NZ    1 
ATOM   2544 N N     . GLU A 1 324 ? -14.328 54.970 14.421  1.00 43.95 ?  324 GLU A N     1 
ATOM   2545 C CA    . GLU A 1 324 ? -15.492 54.110 14.279  1.00 44.35 ?  324 GLU A CA    1 
ATOM   2546 C C     . GLU A 1 324 ? -15.394 53.181 13.080  1.00 37.60 ?  324 GLU A C     1 
ATOM   2547 O O     . GLU A 1 324 ? -16.315 52.394 12.848  1.00 39.90 ?  324 GLU A O     1 
ATOM   2548 C CB    . GLU A 1 324 ? -16.771 54.954 14.152  1.00 51.19 ?  324 GLU A CB    1 
ATOM   2549 C CG    . GLU A 1 324 ? -16.958 56.087 15.181  1.00 58.43 ?  324 GLU A CG    1 
ATOM   2550 C CD    . GLU A 1 324 ? -16.368 55.789 16.567  1.00 65.08 ?  324 GLU A CD    1 
ATOM   2551 O OE1   . GLU A 1 324 ? -17.078 55.168 17.400  1.00 65.14 ?  324 GLU A OE1   1 
ATOM   2552 O OE2   . GLU A 1 324 ? -15.210 56.206 16.832  1.00 58.91 -1 324 GLU A OE2   1 
ATOM   2553 N N     . LYS A 1 325 ? -14.324 53.263 12.302  1.00 36.19 ?  325 LYS A N     1 
ATOM   2554 C CA    . LYS A 1 325 ? -14.241 52.445 11.103  1.00 37.10 ?  325 LYS A CA    1 
ATOM   2555 C C     . LYS A 1 325 ? -13.715 51.047 11.377  1.00 35.50 ?  325 LYS A C     1 
ATOM   2556 O O     . LYS A 1 325 ? -13.805 50.192 10.491  1.00 33.41 ?  325 LYS A O     1 
ATOM   2557 C CB    . LYS A 1 325 ? -13.370 53.136 10.057  1.00 44.66 ?  325 LYS A CB    1 
ATOM   2558 C CG    . LYS A 1 325 ? -13.938 54.484 9.615   1.00 47.39 ?  325 LYS A CG    1 
ATOM   2559 C CD    . LYS A 1 325 ? -13.981 54.575 8.110   1.00 44.76 ?  325 LYS A CD    1 
ATOM   2560 C CE    . LYS A 1 325 ? -12.656 54.122 7.509   1.00 48.61 ?  325 LYS A CE    1 
ATOM   2561 N NZ    . LYS A 1 325 ? -12.679 54.223 6.023   1.00 46.34 ?  325 LYS A NZ    1 
ATOM   2562 N N     . GLY A 1 326 ? -13.203 50.783 12.577  1.00 28.01 ?  326 GLY A N     1 
ATOM   2563 C CA    . GLY A 1 326 ? -12.634 49.481 12.861  1.00 28.21 ?  326 GLY A CA    1 
ATOM   2564 C C     . GLY A 1 326 ? -12.842 49.039 14.290  1.00 26.06 ?  326 GLY A C     1 
ATOM   2565 O O     . GLY A 1 326 ? -12.766 49.848 15.217  1.00 29.90 ?  326 GLY A O     1 
ATOM   2566 N N     . ILE A 1 327 ? -13.105 47.756 14.482  1.00 21.35 ?  327 ILE A N     1 
ATOM   2567 C CA    . ILE A 1 327 ? -13.258 47.178 15.806  1.00 22.76 ?  327 ILE A CA    1 
ATOM   2568 C C     . ILE A 1 327 ? -12.355 45.963 15.903  1.00 22.00 ?  327 ILE A C     1 
ATOM   2569 O O     . ILE A 1 327 ? -12.290 45.158 14.968  1.00 19.66 ?  327 ILE A O     1 
ATOM   2570 C CB    . ILE A 1 327 ? -14.717 46.778 16.089  1.00 20.84 ?  327 ILE A CB    1 
ATOM   2571 C CG1   . ILE A 1 327 ? -15.601 48.014 16.226  1.00 27.78 ?  327 ILE A CG1   1 
ATOM   2572 C CG2   . ILE A 1 327 ? -14.801 45.928 17.346  1.00 20.96 ?  327 ILE A CG2   1 
ATOM   2573 C CD1   . ILE A 1 327 ? -16.959 47.701 16.889  1.00 32.58 ?  327 ILE A CD1   1 
ATOM   2574 N N     . VAL A 1 328 ? -11.649 45.840 17.020  1.00 19.87 ?  328 VAL A N     1 
ATOM   2575 C CA    . VAL A 1 328 ? -10.920 44.632 17.372  1.00 18.34 ?  328 VAL A CA    1 
ATOM   2576 C C     . VAL A 1 328 ? -11.582 44.074 18.623  1.00 20.90 ?  328 VAL A C     1 
ATOM   2577 O O     . VAL A 1 328 ? -11.657 44.758 19.646  1.00 24.89 ?  328 VAL A O     1 
ATOM   2578 C CB    . VAL A 1 328 ? -9.426  44.910 17.612  1.00 19.59 ?  328 VAL A CB    1 
ATOM   2579 C CG1   . VAL A 1 328 ? -8.696  43.617 17.944  1.00 20.84 ?  328 VAL A CG1   1 
ATOM   2580 C CG2   . VAL A 1 328 ? -8.793  45.595 16.418  1.00 21.51 ?  328 VAL A CG2   1 
ATOM   2581 N N     . HIS A 1 329 ? -12.036 42.828 18.558  1.00 24.42 ?  329 HIS A N     1 
ATOM   2582 C CA    . HIS A 1 329 ? -12.939 42.277 19.555  1.00 23.82 ?  329 HIS A CA    1 
ATOM   2583 C C     . HIS A 1 329 ? -12.561 40.834 19.854  1.00 27.50 ?  329 HIS A C     1 
ATOM   2584 O O     . HIS A 1 329 ? -12.182 40.089 18.942  1.00 22.27 ?  329 HIS A O     1 
ATOM   2585 C CB    . HIS A 1 329 ? -14.390 42.367 19.056  1.00 26.89 ?  329 HIS A CB    1 
ATOM   2586 C CG    . HIS A 1 329 ? -15.362 41.589 19.886  1.00 29.91 ?  329 HIS A CG    1 
ATOM   2587 N ND1   . HIS A 1 329 ? -15.869 42.066 21.076  1.00 29.50 ?  329 HIS A ND1   1 
ATOM   2588 C CD2   . HIS A 1 329 ? -15.906 40.360 19.708  1.00 29.32 ?  329 HIS A CD2   1 
ATOM   2589 C CE1   . HIS A 1 329 ? -16.689 41.166 21.593  1.00 30.88 ?  329 HIS A CE1   1 
ATOM   2590 N NE2   . HIS A 1 329 ? -16.729 40.122 20.784  1.00 31.44 ?  329 HIS A NE2   1 
ATOM   2591 N N     . SER A 1 330 ? -12.700 40.435 21.130  1.00 25.21 ?  330 SER A N     1 
ATOM   2592 C CA    . SER A 1 330 ? -12.224 39.142 21.620  1.00 27.19 ?  330 SER A CA    1 
ATOM   2593 C C     . SER A 1 330 ? -13.300 38.076 21.860  1.00 24.16 ?  330 SER A C     1 
ATOM   2594 O O     . SER A 1 330 ? -12.959 36.896 21.938  1.00 35.03 ?  330 SER A O     1 
ATOM   2595 C CB    . SER A 1 330 ? -11.463 39.330 22.933  1.00 26.48 ?  330 SER A CB    1 
ATOM   2596 O OG    . SER A 1 330 ? -10.086 39.246 22.709  1.00 35.78 ?  330 SER A OG    1 
ATOM   2597 N N     . GLY A 1 331 ? -14.553 38.425 22.028  1.00 32.84 ?  331 GLY A N     1 
ATOM   2598 C CA    . GLY A 1 331 ? -15.543 37.407 22.338  1.00 27.30 ?  331 GLY A CA    1 
ATOM   2599 C C     . GLY A 1 331 ? -15.890 36.502 21.154  1.00 32.08 ?  331 GLY A C     1 
ATOM   2600 O O     . GLY A 1 331 ? -15.572 36.771 19.994  1.00 30.27 ?  331 GLY A O     1 
ATOM   2601 N N     . TRP A 1 332 ? -16.546 35.386 21.486  1.00 28.20 ?  332 TRP A N     1 
ATOM   2602 C CA    . TRP A 1 332 ? -17.201 34.525 20.503  1.00 27.29 ?  332 TRP A CA    1 
ATOM   2603 C C     . TRP A 1 332 ? -18.339 35.270 19.818  1.00 26.55 ?  332 TRP A C     1 
ATOM   2604 O O     . TRP A 1 332 ? -19.208 35.822 20.491  1.00 30.63 ?  332 TRP A O     1 
ATOM   2605 C CB    . TRP A 1 332 ? -17.747 33.277 21.204  1.00 25.02 ?  332 TRP A CB    1 
ATOM   2606 C CG    . TRP A 1 332 ? -18.465 32.280 20.304  1.00 30.18 ?  332 TRP A CG    1 
ATOM   2607 C CD1   . TRP A 1 332 ? -19.803 32.259 19.977  1.00 27.59 ?  332 TRP A CD1   1 
ATOM   2608 C CD2   . TRP A 1 332 ? -17.876 31.150 19.640  1.00 23.42 ?  332 TRP A CD2   1 
ATOM   2609 N NE1   . TRP A 1 332 ? -20.068 31.186 19.145  1.00 27.61 ?  332 TRP A NE1   1 
ATOM   2610 C CE2   . TRP A 1 332 ? -18.906 30.493 18.926  1.00 23.95 ?  332 TRP A CE2   1 
ATOM   2611 C CE3   . TRP A 1 332 ? -16.584 30.630 19.584  1.00 26.19 ?  332 TRP A CE3   1 
ATOM   2612 C CZ2   . TRP A 1 332 ? -18.673 29.346 18.168  1.00 25.45 ?  332 TRP A CZ2   1 
ATOM   2613 C CZ3   . TRP A 1 332 ? -16.356 29.486 18.815  1.00 27.24 ?  332 TRP A CZ3   1 
ATOM   2614 C CH2   . TRP A 1 332 ? -17.388 28.867 18.120  1.00 23.27 ?  332 TRP A CH2   1 
ATOM   2615 N N     . ILE A 1 333 ? -18.359 35.277 18.482  1.00 25.38 ?  333 ILE A N     1 
ATOM   2616 C CA    . ILE A 1 333 ? -19.448 35.943 17.772  1.00 22.67 ?  333 ILE A CA    1 
ATOM   2617 C C     . ILE A 1 333 ? -20.135 34.976 16.813  1.00 22.73 ?  333 ILE A C     1 
ATOM   2618 O O     . ILE A 1 333 ? -19.728 33.819 16.684  1.00 22.14 ?  333 ILE A O     1 
ATOM   2619 C CB    . ILE A 1 333 ? -18.953 37.219 17.055  1.00 26.20 ?  333 ILE A CB    1 
ATOM   2620 C CG1   . ILE A 1 333 ? -17.615 36.993 16.344  1.00 25.65 ?  333 ILE A CG1   1 
ATOM   2621 C CG2   . ILE A 1 333 ? -18.807 38.380 18.048  1.00 29.42 ?  333 ILE A CG2   1 
ATOM   2622 C CD1   . ILE A 1 333 ? -17.708 36.223 15.099  1.00 22.92 ?  333 ILE A CD1   1 
ATOM   2623 N N     . GLN A 1 334 ? -21.202 35.436 16.155  1.00 20.94 ?  334 GLN A N     1 
ATOM   2624 C CA    . GLN A 1 334 ? -21.991 34.606 15.239  1.00 20.75 ?  334 GLN A CA    1 
ATOM   2625 C C     . GLN A 1 334 ? -21.394 34.734 13.838  1.00 22.67 ?  334 GLN A C     1 
ATOM   2626 O O     . GLN A 1 334 ? -21.895 35.462 12.978  1.00 19.93 ?  334 GLN A O     1 
ATOM   2627 C CB    . GLN A 1 334 ? -23.455 35.024 15.273  1.00 19.58 ?  334 GLN A CB    1 
ATOM   2628 C CG    . GLN A 1 334 ? -24.135 34.812 16.612  1.00 21.14 ?  334 GLN A CG    1 
ATOM   2629 C CD    . GLN A 1 334 ? -25.435 35.609 16.712  1.00 32.87 ?  334 GLN A CD    1 
ATOM   2630 O OE1   . GLN A 1 334 ? -25.421 36.835 16.865  1.00 29.76 ?  334 GLN A OE1   1 
ATOM   2631 N NE2   . GLN A 1 334 ? -26.562 34.915 16.593  1.00 28.26 ?  334 GLN A NE2   1 
ATOM   2632 N N     . GLN A 1 335 ? -20.285 34.010 13.616  1.00 19.67 ?  335 GLN A N     1 
ATOM   2633 C CA    . GLN A 1 335 ? -19.491 34.237 12.409  1.00 18.66 ?  335 GLN A CA    1 
ATOM   2634 C C     . GLN A 1 335 ? -20.288 33.945 11.151  1.00 18.79 ?  335 GLN A C     1 
ATOM   2635 O O     . GLN A 1 335 ? -20.198 34.687 10.161  1.00 19.67 ?  335 GLN A O     1 
ATOM   2636 C CB    . GLN A 1 335 ? -18.223 33.382 12.425  1.00 21.41 ?  335 GLN A CB    1 
ATOM   2637 C CG    . GLN A 1 335 ? -17.517 33.308 11.077  1.00 16.98 ?  335 GLN A CG    1 
ATOM   2638 C CD    . GLN A 1 335 ? -16.101 32.779 11.207  1.00 22.41 ?  335 GLN A CD    1 
ATOM   2639 O OE1   . GLN A 1 335 ? -15.279 33.383 11.892  1.00 20.51 ?  335 GLN A OE1   1 
ATOM   2640 N NE2   . GLN A 1 335 ? -15.820 31.627 10.580  1.00 17.94 ?  335 GLN A NE2   1 
ATOM   2641 N N     . GLN A 1 336 ? -21.056 32.857 11.155  1.00 19.28 ?  336 GLN A N     1 
ATOM   2642 C CA    . GLN A 1 336 ? -21.828 32.521 9.966   1.00 20.79 ?  336 GLN A CA    1 
ATOM   2643 C C     . GLN A 1 336 ? -22.825 33.626 9.636   1.00 22.18 ?  336 GLN A C     1 
ATOM   2644 O O     . GLN A 1 336 ? -23.013 33.974 8.467   1.00 22.97 ?  336 GLN A O     1 
ATOM   2645 C CB    . GLN A 1 336 ? -22.533 31.176 10.152  1.00 23.84 ?  336 GLN A CB    1 
ATOM   2646 C CG    . GLN A 1 336 ? -23.411 30.804 8.967   1.00 26.51 ?  336 GLN A CG    1 
ATOM   2647 C CD    . GLN A 1 336 ? -24.472 29.780 9.314   1.00 29.83 ?  336 GLN A CD    1 
ATOM   2648 O OE1   . GLN A 1 336 ? -24.225 28.826 10.060  1.00 28.09 ?  336 GLN A OE1   1 
ATOM   2649 N NE2   . GLN A 1 336 ? -25.665 29.971 8.768   1.00 29.35 ?  336 GLN A NE2   1 
ATOM   2650 N N     . LEU A 1 337 ? -23.429 34.238 10.653  1.00 25.93 ?  337 LEU A N     1 
ATOM   2651 C CA    . LEU A 1 337 ? -24.370 35.324 10.373  1.00 22.31 ?  337 LEU A CA    1 
ATOM   2652 C C     . LEU A 1 337 ? -23.645 36.571 9.900   1.00 24.23 ?  337 LEU A C     1 
ATOM   2653 O O     . LEU A 1 337 ? -24.167 37.312 9.061   1.00 24.85 ?  337 LEU A O     1 
ATOM   2654 C CB    . LEU A 1 337 ? -25.224 35.612 11.605  1.00 22.78 ?  337 LEU A CB    1 
ATOM   2655 C CG    . LEU A 1 337 ? -26.295 34.524 11.809  1.00 27.79 ?  337 LEU A CG    1 
ATOM   2656 C CD1   . LEU A 1 337 ? -27.040 34.741 13.108  1.00 33.29 ?  337 LEU A CD1   1 
ATOM   2657 C CD2   . LEU A 1 337 ? -27.291 34.493 10.650  1.00 26.84 ?  337 LEU A CD2   1 
ATOM   2658 N N     . ILE A 1 338 ? -22.409 36.778 10.357  1.00 19.55 ?  338 ILE A N     1 
ATOM   2659 C CA    . ILE A 1 338 ? -21.660 37.946 9.905   1.00 23.20 ?  338 ILE A CA    1 
ATOM   2660 C C     . ILE A 1 338 ? -21.233 37.783 8.451   1.00 22.14 ?  338 ILE A C     1 
ATOM   2661 O O     . ILE A 1 338 ? -21.378 38.703 7.635   1.00 19.87 ?  338 ILE A O     1 
ATOM   2662 C CB    . ILE A 1 338 ? -20.464 38.186 10.839  1.00 21.90 ?  338 ILE A CB    1 
ATOM   2663 C CG1   . ILE A 1 338 ? -21.002 38.551 12.230  1.00 24.18 ?  338 ILE A CG1   1 
ATOM   2664 C CG2   . ILE A 1 338 ? -19.554 39.273 10.251  1.00 16.56 ?  338 ILE A CG2   1 
ATOM   2665 C CD1   . ILE A 1 338 ? -19.961 38.973 13.196  1.00 29.69 ?  338 ILE A CD1   1 
ATOM   2666 N N     . LEU A 1 339 ? -20.714 36.604 8.098   1.00 21.00 ?  339 LEU A N     1 
ATOM   2667 C CA    . LEU A 1 339 ? -20.311 36.360 6.718   1.00 22.95 ?  339 LEU A CA    1 
ATOM   2668 C C     . LEU A 1 339 ? -21.467 36.526 5.737   1.00 26.19 ?  339 LEU A C     1 
ATOM   2669 O O     . LEU A 1 339 ? -21.230 36.832 4.567   1.00 28.04 ?  339 LEU A O     1 
ATOM   2670 C CB    . LEU A 1 339 ? -19.684 34.960 6.594   1.00 17.97 ?  339 LEU A CB    1 
ATOM   2671 C CG    . LEU A 1 339 ? -18.277 34.897 7.241   1.00 19.17 ?  339 LEU A CG    1 
ATOM   2672 C CD1   . LEU A 1 339 ? -17.700 33.473 7.303   1.00 17.06 ?  339 LEU A CD1   1 
ATOM   2673 C CD2   . LEU A 1 339 ? -17.305 35.832 6.549   1.00 19.68 ?  339 LEU A CD2   1 
ATOM   2674 N N     . GLU A 1 340 ? -22.710 36.347 6.188   1.00 25.83 ?  340 GLU A N     1 
ATOM   2675 C CA    . GLU A 1 340 ? -23.881 36.551 5.343   1.00 26.70 ?  340 GLU A CA    1 
ATOM   2676 C C     . GLU A 1 340 ? -24.255 38.020 5.163   1.00 27.21 ?  340 GLU A C     1 
ATOM   2677 O O     . GLU A 1 340 ? -25.010 38.338 4.245   1.00 26.89 ?  340 GLU A O     1 
ATOM   2678 C CB    . GLU A 1 340 ? -25.069 35.788 5.930   1.00 24.32 ?  340 GLU A CB    1 
ATOM   2679 C CG    . GLU A 1 340 ? -24.848 34.312 5.939   1.00 29.96 ?  340 GLU A CG    1 
ATOM   2680 C CD    . GLU A 1 340 ? -26.035 33.551 6.487   1.00 37.84 ?  340 GLU A CD    1 
ATOM   2681 O OE1   . GLU A 1 340 ? -26.946 34.207 7.043   1.00 42.42 ?  340 GLU A OE1   1 
ATOM   2682 O OE2   . GLU A 1 340 ? -26.040 32.298 6.393   1.00 40.40 -1 340 GLU A OE2   1 
ATOM   2683 N N     . HIS A 1 341 ? -23.724 38.920 5.982   1.00 26.45 ?  341 HIS A N     1 
ATOM   2684 C CA    . HIS A 1 341 ? -24.178 40.298 5.946   1.00 22.63 ?  341 HIS A CA    1 
ATOM   2685 C C     . HIS A 1 341 ? -23.624 41.032 4.720   1.00 23.47 ?  341 HIS A C     1 
ATOM   2686 O O     . HIS A 1 341 ? -22.454 40.868 4.365   1.00 27.09 ?  341 HIS A O     1 
ATOM   2687 C CB    . HIS A 1 341 ? -23.776 41.014 7.236   1.00 25.07 ?  341 HIS A CB    1 
ATOM   2688 C CG    . HIS A 1 341 ? -24.433 42.348 7.409   1.00 27.65 ?  341 HIS A CG    1 
ATOM   2689 N ND1   . HIS A 1 341 ? -24.042 43.466 6.701   1.00 27.45 ?  341 HIS A ND1   1 
ATOM   2690 C CD2   . HIS A 1 341 ? -25.466 42.738 8.192   1.00 22.95 ?  341 HIS A CD2   1 
ATOM   2691 C CE1   . HIS A 1 341 ? -24.799 44.489 7.050   1.00 28.86 ?  341 HIS A CE1   1 
ATOM   2692 N NE2   . HIS A 1 341 ? -25.668 44.075 7.955   1.00 24.69 ?  341 HIS A NE2   1 
ATOM   2693 N N     . PRO A 1 342 ? -24.446 41.853 4.055   1.00 29.60 ?  342 PRO A N     1 
ATOM   2694 C CA    . PRO A 1 342 ? -24.007 42.484 2.797   1.00 24.65 ?  342 PRO A CA    1 
ATOM   2695 C C     . PRO A 1 342 ? -22.893 43.512 2.950   1.00 24.52 ?  342 PRO A C     1 
ATOM   2696 O O     . PRO A 1 342 ? -22.321 43.917 1.933   1.00 21.54 ?  342 PRO A O     1 
ATOM   2697 C CB    . PRO A 1 342 ? -25.297 43.138 2.260   1.00 27.77 ?  342 PRO A CB    1 
ATOM   2698 C CG    . PRO A 1 342 ? -26.178 43.306 3.446   1.00 28.46 ?  342 PRO A CG    1 
ATOM   2699 C CD    . PRO A 1 342 ? -25.864 42.128 4.351   1.00 28.49 ?  342 PRO A CD    1 
ATOM   2700 N N     . SER A 1 343 ? -22.556 43.951 4.166   1.00 24.97 ?  343 SER A N     1 
ATOM   2701 C CA    . SER A 1 343 ? -21.434 44.885 4.315   1.00 27.10 ?  343 SER A CA    1 
ATOM   2702 C C     . SER A 1 343 ? -20.081 44.215 4.059   1.00 25.45 ?  343 SER A C     1 
ATOM   2703 O O     . SER A 1 343 ? -19.121 44.887 3.650   1.00 24.22 ?  343 SER A O     1 
ATOM   2704 C CB    . SER A 1 343 ? -21.447 45.509 5.714   1.00 23.19 ?  343 SER A CB    1 
ATOM   2705 O OG    . SER A 1 343 ? -21.411 44.506 6.718   1.00 23.96 ?  343 SER A OG    1 
ATOM   2706 N N     . VAL A 1 344 ? -19.991 42.904 4.270   1.00 25.36 ?  344 VAL A N     1 
ATOM   2707 C CA    . VAL A 1 344 ? -18.715 42.189 4.267   1.00 26.03 ?  344 VAL A CA    1 
ATOM   2708 C C     . VAL A 1 344 ? -18.270 41.987 2.823   1.00 21.53 ?  344 VAL A C     1 
ATOM   2709 O O     . VAL A 1 344 ? -18.924 41.275 2.063   1.00 31.13 ?  344 VAL A O     1 
ATOM   2710 C CB    . VAL A 1 344 ? -18.833 40.848 5.004   1.00 26.16 ?  344 VAL A CB    1 
ATOM   2711 C CG1   . VAL A 1 344 ? -17.529 40.048 4.907   1.00 22.71 ?  344 VAL A CG1   1 
ATOM   2712 C CG2   . VAL A 1 344 ? -19.240 41.081 6.478   1.00 19.94 ?  344 VAL A CG2   1 
ATOM   2713 N N     . GLY A 1 345 ? -17.159 42.607 2.441   1.00 21.86 ?  345 GLY A N     1 
ATOM   2714 C CA    . GLY A 1 345 ? -16.609 42.418 1.104   1.00 22.43 ?  345 GLY A CA    1 
ATOM   2715 C C     . GLY A 1 345 ? -15.405 41.489 1.026   1.00 22.52 ?  345 GLY A C     1 
ATOM   2716 O O     . GLY A 1 345 ? -15.057 41.001 -0.063  1.00 18.54 ?  345 GLY A O     1 
ATOM   2717 N N     . CYS A 1 346 ? -14.776 41.225 2.173   1.00 19.02 ?  346 CYS A N     1 
ATOM   2718 C CA    . CYS A 1 346 ? -13.523 40.484 2.241   1.00 21.93 ?  346 CYS A CA    1 
ATOM   2719 C C     . CYS A 1 346 ? -13.449 39.697 3.552   1.00 19.10 ?  346 CYS A C     1 
ATOM   2720 O O     . CYS A 1 346 ? -13.829 40.221 4.600   1.00 17.44 ?  346 CYS A O     1 
ATOM   2721 C CB    . CYS A 1 346 ? -12.329 41.457 2.129   1.00 20.47 ?  346 CYS A CB    1 
ATOM   2722 S SG    . CYS A 1 346 ? -10.736 40.635 2.275   1.00 24.01 ?  346 CYS A SG    1 
ATOM   2723 N N     . PHE A 1 347 ? -12.941 38.451 3.488   1.00 14.81 ?  347 PHE A N     1 
ATOM   2724 C CA    . PHE A 1 347 ? -12.801 37.536 4.630   1.00 13.76 ?  347 PHE A CA    1 
ATOM   2725 C C     . PHE A 1 347 ? -11.330 37.134 4.739   1.00 15.17 ?  347 PHE A C     1 
ATOM   2726 O O     . PHE A 1 347 ? -10.817 36.422 3.870   1.00 16.06 ?  347 PHE A O     1 
ATOM   2727 C CB    . PHE A 1 347 ? -13.697 36.290 4.450   1.00 15.11 ?  347 PHE A CB    1 
ATOM   2728 C CG    . PHE A 1 347 ? -13.668 35.290 5.599   1.00 13.47 ?  347 PHE A CG    1 
ATOM   2729 C CD1   . PHE A 1 347 ? -13.237 35.643 6.867   1.00 13.87 ?  347 PHE A CD1   1 
ATOM   2730 C CD2   . PHE A 1 347 ? -14.124 33.984 5.399   1.00 15.83 ?  347 PHE A CD2   1 
ATOM   2731 C CE1   . PHE A 1 347 ? -13.217 34.725 7.922   1.00 14.00 ?  347 PHE A CE1   1 
ATOM   2732 C CE2   . PHE A 1 347 ? -14.144 33.058 6.464   1.00 18.72 ?  347 PHE A CE2   1 
ATOM   2733 C CZ    . PHE A 1 347 ? -13.677 33.429 7.723   1.00 17.12 ?  347 PHE A CZ    1 
ATOM   2734 N N     . VAL A 1 348 ? -10.653 37.595 5.791   1.00 15.35 ?  348 VAL A N     1 
ATOM   2735 C CA    . VAL A 1 348 ? -9.275  37.193 6.097   1.00 13.81 ?  348 VAL A CA    1 
ATOM   2736 C C     . VAL A 1 348 ? -9.381  36.024 7.067   1.00 14.66 ?  348 VAL A C     1 
ATOM   2737 O O     . VAL A 1 348 ? -9.845  36.197 8.194   1.00 15.16 ?  348 VAL A O     1 
ATOM   2738 C CB    . VAL A 1 348 ? -8.462  38.344 6.711   1.00 15.62 ?  348 VAL A CB    1 
ATOM   2739 C CG1   . VAL A 1 348 ? -7.027  37.881 7.000   1.00 15.04 ?  348 VAL A CG1   1 
ATOM   2740 C CG2   . VAL A 1 348 ? -8.491  39.597 5.826   1.00 13.41 ?  348 VAL A CG2   1 
ATOM   2741 N N     . THR A 1 349 ? -8.990  34.825 6.633   1.00 13.31 ?  349 THR A N     1 
ATOM   2742 C CA    . THR A 1 349 ? -9.317  33.628 7.388   1.00 13.38 ?  349 THR A CA    1 
ATOM   2743 C C     . THR A 1 349 ? -8.065  32.836 7.745   1.00 17.88 ?  349 THR A C     1 
ATOM   2744 O O     . THR A 1 349 ? -7.086  32.836 7.003   1.00 15.69 ?  349 THR A O     1 
ATOM   2745 C CB    . THR A 1 349 ? -10.295 32.713 6.613   1.00 14.54 ?  349 THR A CB    1 
ATOM   2746 O OG1   . THR A 1 349 ? -10.514 31.521 7.375   1.00 15.97 ?  349 THR A OG1   1 
ATOM   2747 C CG2   . THR A 1 349 ? -9.742  32.312 5.230   1.00 16.25 ?  349 THR A CG2   1 
ATOM   2748 N N     . HIS A 1 350 ? -8.110  32.145 8.889   1.00 15.55 ?  350 HIS A N     1 
ATOM   2749 C CA    . HIS A 1 350 ? -7.031  31.226 9.245   1.00 15.73 ?  350 HIS A CA    1 
ATOM   2750 C C     . HIS A 1 350 ? -7.093  29.906 8.468   1.00 17.00 ?  350 HIS A C     1 
ATOM   2751 O O     . HIS A 1 350 ? -6.189  29.070 8.626   1.00 16.40 ?  350 HIS A O     1 
ATOM   2752 C CB    . HIS A 1 350 ? -7.055  30.939 10.745  1.00 13.73 ?  350 HIS A CB    1 
ATOM   2753 C CG    . HIS A 1 350 ? -8.197  30.073 11.162  1.00 18.03 ?  350 HIS A CG    1 
ATOM   2754 N ND1   . HIS A 1 350 ? -9.510  30.379 10.858  1.00 21.88 ?  350 HIS A ND1   1 
ATOM   2755 C CD2   . HIS A 1 350 ? -8.230  28.909 11.853  1.00 16.73 ?  350 HIS A CD2   1 
ATOM   2756 C CE1   . HIS A 1 350 ? -10.299 29.434 11.335  1.00 20.98 ?  350 HIS A CE1   1 
ATOM   2757 N NE2   . HIS A 1 350 ? -9.549  28.531 11.944  1.00 17.03 ?  350 HIS A NE2   1 
ATOM   2758 N N     . CYS A 1 351 ? -8.125  29.706 7.634   1.00 14.06 ?  351 CYS A N     1 
ATOM   2759 C CA    . CYS A 1 351 ? -8.273  28.535 6.758   1.00 14.35 ?  351 CYS A CA    1 
ATOM   2760 C C     . CYS A 1 351 ? -8.635  27.250 7.508   1.00 16.82 ?  351 CYS A C     1 
ATOM   2761 O O     . CYS A 1 351 ? -8.374  26.146 7.007   1.00 14.21 ?  351 CYS A O     1 
ATOM   2762 C CB    . CYS A 1 351 ? -7.011  28.311 5.911   1.00 18.67 ?  351 CYS A CB    1 
ATOM   2763 S SG    . CYS A 1 351 ? -6.605  29.733 4.846   1.00 16.21 ?  351 CYS A SG    1 
ATOM   2764 N N     . GLY A 1 352 ? -9.243  27.360 8.693   1.00 14.56 ?  352 GLY A N     1 
ATOM   2765 C CA    . GLY A 1 352 ? -9.895  26.201 9.289   1.00 17.48 ?  352 GLY A CA    1 
ATOM   2766 C C     . GLY A 1 352 ? -10.986 25.646 8.387   1.00 14.97 ?  352 GLY A C     1 
ATOM   2767 O O     . GLY A 1 352 ? -11.575 26.362 7.573   1.00 13.71 ?  352 GLY A O     1 
ATOM   2768 N N     . ALA A 1 353 ? -11.249 24.344 8.532   1.00 15.63 ?  353 ALA A N     1 
ATOM   2769 C CA    . ALA A 1 353 ? -12.152 23.656 7.614   1.00 12.64 ?  353 ALA A CA    1 
ATOM   2770 C C     . ALA A 1 353 ? -13.560 24.252 7.653   1.00 13.32 ?  353 ALA A C     1 
ATOM   2771 O O     . ALA A 1 353 ? -14.223 24.354 6.618   1.00 15.90 ?  353 ALA A O     1 
ATOM   2772 C CB    . ALA A 1 353 ? -12.193 22.160 7.934   1.00 12.35 ?  353 ALA A CB    1 
ATOM   2773 N N     . GLY A 1 354 ? -14.044 24.631 8.835   1.00 16.08 ?  354 GLY A N     1 
ATOM   2774 C CA    . GLY A 1 354 ? -15.388 25.186 8.916   1.00 17.12 ?  354 GLY A CA    1 
ATOM   2775 C C     . GLY A 1 354 ? -15.465 26.589 8.343   1.00 17.73 ?  354 GLY A C     1 
ATOM   2776 O O     . GLY A 1 354 ? -16.402 26.921 7.606   1.00 14.38 ?  354 GLY A O     1 
ATOM   2777 N N     . SER A 1 355 ? -14.465 27.425 8.654   1.00 14.88 ?  355 SER A N     1 
ATOM   2778 C CA    . SER A 1 355 ? -14.424 28.785 8.113   1.00 15.70 ?  355 SER A CA    1 
ATOM   2779 C C     . SER A 1 355 ? -14.289 28.769 6.595   1.00 15.83 ?  355 SER A C     1 
ATOM   2780 O O     . SER A 1 355 ? -14.851 29.632 5.907   1.00 16.38 ?  355 SER A O     1 
ATOM   2781 C CB    . SER A 1 355 ? -13.269 29.581 8.749   1.00 15.28 ?  355 SER A CB    1 
ATOM   2782 O OG    . SER A 1 355 ? -13.441 29.670 10.162  1.00 18.59 ?  355 SER A OG    1 
ATOM   2783 N N     . ILE A 1 356 ? -13.552 27.792 6.054   1.00 16.03 ?  356 ILE A N     1 
ATOM   2784 C CA    . ILE A 1 356 ? -13.415 27.677 4.600   1.00 15.44 ?  356 ILE A CA    1 
ATOM   2785 C C     . ILE A 1 356 ? -14.786 27.502 3.956   1.00 16.29 ?  356 ILE A C     1 
ATOM   2786 O O     . ILE A 1 356 ? -15.142 28.218 3.021   1.00 14.28 ?  356 ILE A O     1 
ATOM   2787 C CB    . ILE A 1 356 ? -12.487 26.510 4.215   1.00 14.23 ?  356 ILE A CB    1 
ATOM   2788 C CG1   . ILE A 1 356 ? -11.006 26.829 4.507   1.00 18.51 ?  356 ILE A CG1   1 
ATOM   2789 C CG2   . ILE A 1 356 ? -12.631 26.210 2.721   1.00 15.73 ?  356 ILE A CG2   1 
ATOM   2790 C CD1   . ILE A 1 356 ? -10.491 28.038 3.762   1.00 16.63 ?  356 ILE A CD1   1 
ATOM   2791 N N     . THR A 1 357 ? -15.568 26.536 4.448   1.00 15.70 ?  357 THR A N     1 
ATOM   2792 C CA    . THR A 1 357 ? -16.901 26.303 3.890   1.00 15.77 ?  357 THR A CA    1 
ATOM   2793 C C     . THR A 1 357 ? -17.776 27.534 4.033   1.00 16.95 ?  357 THR A C     1 
ATOM   2794 O O     . THR A 1 357 ? -18.441 27.946 3.080   1.00 17.02 ?  357 THR A O     1 
ATOM   2795 C CB    . THR A 1 357 ? -17.565 25.108 4.568   1.00 15.81 ?  357 THR A CB    1 
ATOM   2796 O OG1   . THR A 1 357 ? -16.767 23.949 4.334   1.00 20.56 ?  357 THR A OG1   1 
ATOM   2797 C CG2   . THR A 1 357 ? -18.986 24.880 3.995   1.00 19.02 ?  357 THR A CG2   1 
ATOM   2798 N N     . GLU A 1 358 ? -17.753 28.160 5.208   1.00 17.48 ?  358 GLU A N     1 
ATOM   2799 C CA    . GLU A 1 358 ? -18.592 29.331 5.439   1.00 16.39 ?  358 GLU A CA    1 
ATOM   2800 C C     . GLU A 1 358 ? -18.236 30.469 4.492   1.00 17.00 ?  358 GLU A C     1 
ATOM   2801 O O     . GLU A 1 358 ? -19.126 31.213 4.065   1.00 23.80 ?  358 GLU A O     1 
ATOM   2802 C CB    . GLU A 1 358 ? -18.479 29.767 6.906   1.00 15.55 ?  358 GLU A CB    1 
ATOM   2803 C CG    . GLU A 1 358 ? -19.342 28.911 7.830   1.00 20.52 ?  358 GLU A CG    1 
ATOM   2804 C CD    . GLU A 1 358 ? -18.822 28.851 9.275   1.00 25.73 ?  358 GLU A CD    1 
ATOM   2805 O OE1   . GLU A 1 358 ? -18.084 29.780 9.699   1.00 21.08 ?  358 GLU A OE1   1 
ATOM   2806 O OE2   . GLU A 1 358 ? -19.179 27.878 9.986   1.00 27.61 -1 358 GLU A OE2   1 
ATOM   2807 N N     . GLY A 1 359 ? -16.954 30.596 4.116   1.00 18.04 ?  359 GLY A N     1 
ATOM   2808 C CA    . GLY A 1 359 ? -16.538 31.599 3.142   1.00 16.48 ?  359 GLY A CA    1 
ATOM   2809 C C     . GLY A 1 359 ? -16.935 31.232 1.719   1.00 20.62 ?  359 GLY A C     1 
ATOM   2810 O O     . GLY A 1 359 ? -17.424 32.078 0.965   1.00 17.51 ?  359 GLY A O     1 
ATOM   2811 N N     . LEU A 1 360 ? -16.763 29.955 1.359   1.00 17.08 ?  360 LEU A N     1 
ATOM   2812 C CA    . LEU A 1 360 ? -17.069 29.507 -0.002  1.00 20.58 ?  360 LEU A CA    1 
ATOM   2813 C C     . LEU A 1 360 ? -18.534 29.735 -0.364  1.00 18.50 ?  360 LEU A C     1 
ATOM   2814 O O     . LEU A 1 360 ? -18.841 30.100 -1.501  1.00 20.19 ?  360 LEU A O     1 
ATOM   2815 C CB    . LEU A 1 360 ? -16.711 28.030 -0.168  1.00 17.82 ?  360 LEU A CB    1 
ATOM   2816 C CG    . LEU A 1 360 ? -15.193 27.781 -0.287  1.00 16.90 ?  360 LEU A CG    1 
ATOM   2817 C CD1   . LEU A 1 360 ? -14.884 26.291 -0.403  1.00 18.48 ?  360 LEU A CD1   1 
ATOM   2818 C CD2   . LEU A 1 360 ? -14.578 28.576 -1.431  1.00 22.20 ?  360 LEU A CD2   1 
ATOM   2819 N N     . VAL A 1 361 ? -19.459 29.524 0.581   1.00 17.20 ?  361 VAL A N     1 
ATOM   2820 C CA    . VAL A 1 361 ? -20.881 29.651 0.246   1.00 18.45 ?  361 VAL A CA    1 
ATOM   2821 C C     . VAL A 1 361 ? -21.373 31.087 0.320   1.00 19.66 ?  361 VAL A C     1 
ATOM   2822 O O     . VAL A 1 361 ? -22.566 31.330 0.090   1.00 20.86 ?  361 VAL A O     1 
ATOM   2823 C CB    . VAL A 1 361 ? -21.793 28.787 1.138   1.00 16.47 ?  361 VAL A CB    1 
ATOM   2824 C CG1   . VAL A 1 361 ? -21.405 27.321 1.066   1.00 17.51 ?  361 VAL A CG1   1 
ATOM   2825 C CG2   . VAL A 1 361 ? -21.791 29.300 2.583   1.00 19.84 ?  361 VAL A CG2   1 
ATOM   2826 N N     . ASN A 1 362 ? -20.497 32.049 0.597   1.00 18.83 ?  362 ASN A N     1 
ATOM   2827 C CA    . ASN A 1 362 ? -20.894 33.455 0.666   1.00 22.81 ?  362 ASN A CA    1 
ATOM   2828 C C     . ASN A 1 362 ? -20.179 34.256 -0.424  1.00 21.97 ?  362 ASN A C     1 
ATOM   2829 O O     . ASN A 1 362 ? -19.420 33.717 -1.233  1.00 21.04 ?  362 ASN A O     1 
ATOM   2830 C CB    . ASN A 1 362 ? -20.643 34.018 2.068   1.00 20.39 ?  362 ASN A CB    1 
ATOM   2831 C CG    . ASN A 1 362 ? -21.746 33.626 3.051   1.00 26.81 ?  362 ASN A CG    1 
ATOM   2832 O OD1   . ASN A 1 362 ? -22.873 34.106 2.947   1.00 26.46 ?  362 ASN A OD1   1 
ATOM   2833 N ND2   . ASN A 1 362 ? -21.434 32.723 3.979   1.00 20.89 ?  362 ASN A ND2   1 
ATOM   2834 N N     . ASN A 1 363 ? -20.448 35.558 -0.467  1.00 21.78 ?  363 ASN A N     1 
ATOM   2835 C CA    . ASN A 1 363 ? -19.963 36.375 -1.573  1.00 25.68 ?  363 ASN A CA    1 
ATOM   2836 C C     . ASN A 1 363 ? -18.603 37.012 -1.314  1.00 22.95 ?  363 ASN A C     1 
ATOM   2837 O O     . ASN A 1 363 ? -17.977 37.485 -2.267  1.00 27.24 ?  363 ASN A O     1 
ATOM   2838 C CB    . ASN A 1 363 ? -20.985 37.480 -1.915  1.00 27.43 ?  363 ASN A CB    1 
ATOM   2839 C CG    . ASN A 1 363 ? -22.255 36.927 -2.541  1.00 34.11 ?  363 ASN A CG    1 
ATOM   2840 O OD1   . ASN A 1 363 ? -22.212 35.996 -3.363  1.00 26.09 ?  363 ASN A OD1   1 
ATOM   2841 N ND2   . ASN A 1 363 ? -23.404 37.494 -2.150  1.00 31.72 ?  363 ASN A ND2   1 
ATOM   2842 N N     . CYS A 1 364 ? -18.123 37.003 -0.070  1.00 23.75 ?  364 CYS A N     1 
ATOM   2843 C CA    . CYS A 1 364 ? -16.898 37.719 0.288   1.00 23.36 ?  364 CYS A CA    1 
ATOM   2844 C C     . CYS A 1 364 ? -15.688 37.223 -0.500  1.00 20.79 ?  364 CYS A C     1 
ATOM   2845 O O     . CYS A 1 364 ? -15.540 36.021 -0.758  1.00 20.96 ?  364 CYS A O     1 
ATOM   2846 C CB    . CYS A 1 364 ? -16.632 37.538 1.780   1.00 20.65 ?  364 CYS A CB    1 
ATOM   2847 S SG    . CYS A 1 364 ? -16.755 35.775 2.274   1.00 24.74 ?  364 CYS A SG    1 
ATOM   2848 N N     . GLN A 1 365 ? -14.808 38.155 -0.863  1.00 18.68 ?  365 GLN A N     1 
ATOM   2849 C CA    . GLN A 1 365 ? -13.487 37.785 -1.352  1.00 18.48 ?  365 GLN A CA    1 
ATOM   2850 C C     . GLN A 1 365 ? -12.687 37.148 -0.216  1.00 19.68 ?  365 GLN A C     1 
ATOM   2851 O O     . GLN A 1 365 ? -12.790 37.575 0.937   1.00 22.38 ?  365 GLN A O     1 
ATOM   2852 C CB    . GLN A 1 365 ? -12.762 39.026 -1.882  1.00 20.62 ?  365 GLN A CB    1 
ATOM   2853 C CG    . GLN A 1 365 ? -13.407 39.671 -3.139  1.00 17.37 ?  365 GLN A CG    1 
ATOM   2854 C CD    . GLN A 1 365 ? -13.031 38.930 -4.416  1.00 23.22 ?  365 GLN A CD    1 
ATOM   2855 O OE1   . GLN A 1 365 ? -13.391 37.758 -4.600  1.00 17.61 ?  365 GLN A OE1   1 
ATOM   2856 N NE2   . GLN A 1 365 ? -12.271 39.604 -5.293  1.00 18.97 ?  365 GLN A NE2   1 
ATOM   2857 N N     . MET A 1 366 ? -11.881 36.132 -0.535  1.00 20.87 ?  366 MET A N     1 
ATOM   2858 C CA    . MET A 1 366 ? -11.144 35.361 0.474   1.00 21.24 ?  366 MET A CA    1 
ATOM   2859 C C     . MET A 1 366 ? -9.675  35.754 0.484   1.00 20.02 ?  366 MET A C     1 
ATOM   2860 O O     . MET A 1 366 ? -8.998  35.640 -0.540  1.00 18.52 ?  366 MET A O     1 
ATOM   2861 C CB    . MET A 1 366 ? -11.209 33.853 0.207   1.00 21.61 ?  366 MET A CB    1 
ATOM   2862 C CG    . MET A 1 366 ? -12.554 33.299 -0.105  1.00 29.90 ?  366 MET A CG    1 
ATOM   2863 S SD    . MET A 1 366 ? -13.344 32.961 1.444   1.00 38.77 ?  366 MET A SD    1 
ATOM   2864 C CE    . MET A 1 366 ? -13.032 31.200 1.464   1.00 26.61 ?  366 MET A CE    1 
ATOM   2865 N N     . VAL A 1 367 ? -9.166  36.128 1.654   1.00 19.21 ?  367 VAL A N     1 
ATOM   2866 C CA    . VAL A 1 367 ? -7.733  36.323 1.869   1.00 16.64 ?  367 VAL A CA    1 
ATOM   2867 C C     . VAL A 1 367 ? -7.267  35.240 2.831   1.00 14.86 ?  367 VAL A C     1 
ATOM   2868 O O     . VAL A 1 367 ? -7.804  35.109 3.936   1.00 15.24 ?  367 VAL A O     1 
ATOM   2869 C CB    . VAL A 1 367 ? -7.419  37.734 2.392   1.00 15.90 ?  367 VAL A CB    1 
ATOM   2870 C CG1   . VAL A 1 367 ? -5.913  37.866 2.829   1.00 11.55 ?  367 VAL A CG1   1 
ATOM   2871 C CG2   . VAL A 1 367 ? -7.752  38.769 1.300   1.00 17.23 ?  367 VAL A CG2   1 
ATOM   2872 N N     . LEU A 1 368 ? -6.311  34.426 2.397   1.00 15.56 ?  368 LEU A N     1 
ATOM   2873 C CA    . LEU A 1 368 ? -5.917  33.241 3.148   1.00 17.89 ?  368 LEU A CA    1 
ATOM   2874 C C     . LEU A 1 368 ? -4.699  33.549 4.009   1.00 16.84 ?  368 LEU A C     1 
ATOM   2875 O O     . LEU A 1 368 ? -3.620  33.863 3.489   1.00 18.23 ?  368 LEU A O     1 
ATOM   2876 C CB    . LEU A 1 368 ? -5.630  32.060 2.211   1.00 16.61 ?  368 LEU A CB    1 
ATOM   2877 C CG    . LEU A 1 368 ? -6.654  31.924 1.079   1.00 20.78 ?  368 LEU A CG    1 
ATOM   2878 C CD1   . LEU A 1 368 ? -6.111  31.057 -0.071  1.00 20.57 ?  368 LEU A CD1   1 
ATOM   2879 C CD2   . LEU A 1 368 ? -8.032  31.441 1.588   1.00 18.83 ?  368 LEU A CD2   1 
ATOM   2880 N N     . LEU A 1 369 ? -4.863  33.420 5.320   1.00 17.35 ?  369 LEU A N     1 
ATOM   2881 C CA    . LEU A 1 369 ? -3.798  33.667 6.289   1.00 15.71 ?  369 LEU A CA    1 
ATOM   2882 C C     . LEU A 1 369 ? -3.678  32.450 7.202   1.00 16.61 ?  369 LEU A C     1 
ATOM   2883 O O     . LEU A 1 369 ? -3.977  32.522 8.402   1.00 16.10 ?  369 LEU A O     1 
ATOM   2884 C CB    . LEU A 1 369 ? -4.094  34.938 7.086   1.00 18.72 ?  369 LEU A CB    1 
ATOM   2885 C CG    . LEU A 1 369 ? -3.007  35.414 8.058   1.00 22.27 ?  369 LEU A CG    1 
ATOM   2886 C CD1   . LEU A 1 369 ? -1.850  36.001 7.278   1.00 21.26 ?  369 LEU A CD1   1 
ATOM   2887 C CD2   . LEU A 1 369 ? -3.541  36.408 9.105   1.00 25.72 ?  369 LEU A CD2   1 
ATOM   2888 N N     . PRO A 1 370 ? -3.260  31.302 6.657   1.00 15.98 ?  370 PRO A N     1 
ATOM   2889 C CA    . PRO A 1 370 ? -3.280  30.067 7.453   1.00 16.17 ?  370 PRO A CA    1 
ATOM   2890 C C     . PRO A 1 370 ? -2.376  30.198 8.667   1.00 18.09 ?  370 PRO A C     1 
ATOM   2891 O O     . PRO A 1 370 ? -1.285  30.770 8.591   1.00 16.06 ?  370 PRO A O     1 
ATOM   2892 C CB    . PRO A 1 370 ? -2.764  28.990 6.482   1.00 15.49 ?  370 PRO A CB    1 
ATOM   2893 C CG    . PRO A 1 370 ? -1.997  29.759 5.415   1.00 15.87 ?  370 PRO A CG    1 
ATOM   2894 C CD    . PRO A 1 370 ? -2.677  31.105 5.313   1.00 15.05 ?  370 PRO A CD    1 
ATOM   2895 N N     . GLN A 1 371 ? -2.845  29.673 9.799   1.00 15.62 ?  371 GLN A N     1 
ATOM   2896 C CA    . GLN A 1 371 ? -2.001  29.597 10.982  1.00 19.17 ?  371 GLN A CA    1 
ATOM   2897 C C     . GLN A 1 371 ? -1.318  28.218 11.034  1.00 19.80 ?  371 GLN A C     1 
ATOM   2898 O O     . GLN A 1 371 ? -1.512  27.375 10.158  1.00 17.83 ?  371 GLN A O     1 
ATOM   2899 C CB    . GLN A 1 371 ? -2.832  29.920 12.225  1.00 12.61 ?  371 GLN A CB    1 
ATOM   2900 C CG    . GLN A 1 371 ? -3.343  31.375 12.256  1.00 17.13 ?  371 GLN A CG    1 
ATOM   2901 C CD    . GLN A 1 371 ? -2.234  32.398 12.016  1.00 23.47 ?  371 GLN A CD    1 
ATOM   2902 O OE1   . GLN A 1 371 ? -1.367  32.601 12.867  1.00 21.37 ?  371 GLN A OE1   1 
ATOM   2903 N NE2   . GLN A 1 371 ? -2.250  33.035 10.846  1.00 19.28 ?  371 GLN A NE2   1 
ATOM   2904 N N     . LEU A 1 372 ? -0.478  27.982 12.047  1.00 20.61 ?  372 LEU A N     1 
ATOM   2905 C CA    . LEU A 1 372 ? 0.392   26.804 12.036  1.00 19.77 ?  372 LEU A CA    1 
ATOM   2906 C C     . LEU A 1 372 ? -0.400  25.566 12.453  1.00 18.32 ?  372 LEU A C     1 
ATOM   2907 O O     . LEU A 1 372 ? -0.493  25.214 13.629  1.00 21.35 ?  372 LEU A O     1 
ATOM   2908 C CB    . LEU A 1 372 ? 1.604   27.017 12.941  1.00 26.94 ?  372 LEU A CB    1 
ATOM   2909 C CG    . LEU A 1 372 ? 2.901   27.603 12.341  1.00 28.12 ?  372 LEU A CG    1 
ATOM   2910 C CD1   . LEU A 1 372 ? 4.029   27.634 13.369  1.00 25.22 ?  372 LEU A CD1   1 
ATOM   2911 C CD2   . LEU A 1 372 ? 3.365   26.896 11.057  1.00 24.99 ?  372 LEU A CD2   1 
ATOM   2912 N N     . ASN A 1 373 ? -0.925  24.867 11.460  1.00 20.98 ?  373 ASN A N     1 
ATOM   2913 C CA    . ASN A 1 373 ? -1.722  23.661 11.643  1.00 18.24 ?  373 ASN A CA    1 
ATOM   2914 C C     . ASN A 1 373 ? -1.769  22.987 10.279  1.00 15.33 ?  373 ASN A C     1 
ATOM   2915 O O     . ASN A 1 373 ? -1.929  23.662 9.267   1.00 14.29 ?  373 ASN A O     1 
ATOM   2916 C CB    . ASN A 1 373 ? -3.134  24.005 12.186  1.00 18.30 ?  373 ASN A CB    1 
ATOM   2917 C CG    . ASN A 1 373 ? -4.133  22.846 12.068  1.00 19.87 ?  373 ASN A CG    1 
ATOM   2918 O OD1   . ASN A 1 373 ? -4.484  22.431 10.967  1.00 16.84 ?  373 ASN A OD1   1 
ATOM   2919 N ND2   . ASN A 1 373 ? -4.598  22.338 13.206  1.00 16.04 ?  373 ASN A ND2   1 
ATOM   2920 N N     . GLY A 1 374 ? -1.593  21.664 10.256  1.00 18.15 ?  374 GLY A N     1 
ATOM   2921 C CA    . GLY A 1 374 ? -1.485  20.964 8.983   1.00 13.64 ?  374 GLY A CA    1 
ATOM   2922 C C     . GLY A 1 374 ? -2.708  21.137 8.095   1.00 16.11 ?  374 GLY A C     1 
ATOM   2923 O O     . GLY A 1 374 ? -2.586  21.426 6.905   1.00 14.89 ?  374 GLY A O     1 
ATOM   2924 N N     . ASP A 1 375 ? -3.913  20.967 8.657   1.00 16.62 ?  375 ASP A N     1 
ATOM   2925 C CA    . ASP A 1 375 ? -5.108  21.162 7.841   1.00 12.80 ?  375 ASP A CA    1 
ATOM   2926 C C     . ASP A 1 375 ? -5.218  22.605 7.348   1.00 14.65 ?  375 ASP A C     1 
ATOM   2927 O O     . ASP A 1 375 ? -5.574  22.836 6.189   1.00 15.13 ?  375 ASP A O     1 
ATOM   2928 C CB    . ASP A 1 375 ? -6.380  20.772 8.608   1.00 16.72 ?  375 ASP A CB    1 
ATOM   2929 C CG    . ASP A 1 375 ? -7.586  20.530 7.657   1.00 15.85 ?  375 ASP A CG    1 
ATOM   2930 O OD1   . ASP A 1 375 ? -7.452  19.706 6.723   1.00 14.99 ?  375 ASP A OD1   1 
ATOM   2931 O OD2   . ASP A 1 375 ? -8.665  21.165 7.836   1.00 17.42 -1 375 ASP A OD2   1 
ATOM   2932 N N     . TYR A 1 376 ? -4.952  23.593 8.219   1.00 13.54 ?  376 TYR A N     1 
ATOM   2933 C CA    . TYR A 1 376 ? -5.031  24.987 7.781   1.00 15.08 ?  376 TYR A CA    1 
ATOM   2934 C C     . TYR A 1 376 ? -4.130  25.208 6.568   1.00 17.86 ?  376 TYR A C     1 
ATOM   2935 O O     . TYR A 1 376 ? -4.561  25.766 5.555   1.00 17.68 ?  376 TYR A O     1 
ATOM   2936 C CB    . TYR A 1 376 ? -4.616  25.959 8.900   1.00 13.13 ?  376 TYR A CB    1 
ATOM   2937 C CG    . TYR A 1 376 ? -5.353  25.939 10.234  1.00 18.03 ?  376 TYR A CG    1 
ATOM   2938 C CD1   . TYR A 1 376 ? -6.479  25.132 10.463  1.00 17.59 ?  376 TYR A CD1   1 
ATOM   2939 C CD2   . TYR A 1 376 ? -4.916  26.756 11.271  1.00 15.30 ?  376 TYR A CD2   1 
ATOM   2940 C CE1   . TYR A 1 376 ? -7.151  25.163 11.704  1.00 17.28 ?  376 TYR A CE1   1 
ATOM   2941 C CE2   . TYR A 1 376 ? -5.568  26.792 12.489  1.00 19.22 ?  376 TYR A CE2   1 
ATOM   2942 C CZ    . TYR A 1 376 ? -6.675  25.996 12.702  1.00 17.37 ?  376 TYR A CZ    1 
ATOM   2943 O OH    . TYR A 1 376 ? -7.291  26.053 13.915  1.00 24.93 ?  376 TYR A OH    1 
ATOM   2944 N N     . ILE A 1 377 ? -2.860  24.766 6.668   1.00 16.34 ?  377 ILE A N     1 
ATOM   2945 C CA    . ILE A 1 377 ? -1.871  25.009 5.616   1.00 14.47 ?  377 ILE A CA    1 
ATOM   2946 C C     . ILE A 1 377 ? -2.317  24.360 4.312   1.00 17.15 ?  377 ILE A C     1 
ATOM   2947 O O     . ILE A 1 377 ? -2.306  24.986 3.244   1.00 16.91 ?  377 ILE A O     1 
ATOM   2948 C CB    . ILE A 1 377 ? -0.479  24.497 6.060   1.00 18.25 ?  377 ILE A CB    1 
ATOM   2949 C CG1   . ILE A 1 377 ? 0.118   25.418 7.139   1.00 16.44 ?  377 ILE A CG1   1 
ATOM   2950 C CG2   . ILE A 1 377 ? 0.487   24.371 4.853   1.00 15.47 ?  377 ILE A CG2   1 
ATOM   2951 C CD1   . ILE A 1 377 ? 1.118   24.735 8.055   1.00 17.63 ?  377 ILE A CD1   1 
ATOM   2952 N N     . ILE A 1 378 ? -2.753  23.104 4.384   1.00 16.24 ?  378 ILE A N     1 
ATOM   2953 C CA    . ILE A 1 378 ? -3.116  22.396 3.161   1.00 16.78 ?  378 ILE A CA    1 
ATOM   2954 C C     . ILE A 1 378 ? -4.413  22.964 2.577   1.00 16.69 ?  378 ILE A C     1 
ATOM   2955 O O     . ILE A 1 378 ? -4.523  23.151 1.362   1.00 16.09 ?  378 ILE A O     1 
ATOM   2956 C CB    . ILE A 1 378 ? -3.178  20.883 3.435   1.00 17.01 ?  378 ILE A CB    1 
ATOM   2957 C CG1   . ILE A 1 378 ? -1.751  20.356 3.522   1.00 15.83 ?  378 ILE A CG1   1 
ATOM   2958 C CG2   . ILE A 1 378 ? -3.947  20.134 2.339   1.00 17.50 ?  378 ILE A CG2   1 
ATOM   2959 C CD1   . ILE A 1 378 ? -1.707  18.968 4.055   1.00 20.92 ?  378 ILE A CD1   1 
ATOM   2960 N N     . ASN A 1 379 ? -5.374  23.334 3.432   1.00 15.42 ?  379 ASN A N     1 
ATOM   2961 C CA    . ASN A 1 379 ? -6.524  24.093 2.949   1.00 16.15 ?  379 ASN A CA    1 
ATOM   2962 C C     . ASN A 1 379 ? -6.084  25.325 2.165   1.00 16.15 ?  379 ASN A C     1 
ATOM   2963 O O     . ASN A 1 379 ? -6.597  25.599 1.074   1.00 15.79 ?  379 ASN A O     1 
ATOM   2964 C CB    . ASN A 1 379 ? -7.424  24.514 4.122   1.00 16.55 ?  379 ASN A CB    1 
ATOM   2965 C CG    . ASN A 1 379 ? -8.310  23.373 4.632   1.00 18.33 ?  379 ASN A CG    1 
ATOM   2966 O OD1   . ASN A 1 379 ? -8.576  22.401 3.917   1.00 14.04 ?  379 ASN A OD1   1 
ATOM   2967 N ND2   . ASN A 1 379 ? -8.727  23.472 5.891   1.00 15.61 ?  379 ASN A ND2   1 
ATOM   2968 N N     . ALA A 1 380 ? -5.122  26.077 2.704   1.00 16.15 ?  380 ALA A N     1 
ATOM   2969 C CA    . ALA A 1 380 ? -4.729  27.327 2.057   1.00 15.13 ?  380 ALA A CA    1 
ATOM   2970 C C     . ALA A 1 380 ? -4.094  27.085 0.691   1.00 16.00 ?  380 ALA A C     1 
ATOM   2971 O O     . ALA A 1 380 ? -4.366  27.830 -0.262  1.00 15.09 ?  380 ALA A O     1 
ATOM   2972 C CB    . ALA A 1 380 ? -3.780  28.107 2.956   1.00 15.66 ?  380 ALA A CB    1 
ATOM   2973 N N     . ARG A 1 381 ? -3.253  26.051 0.571   1.00 18.78 ?  381 ARG A N     1 
ATOM   2974 C CA    . ARG A 1 381 ? -2.630  25.751 -0.719  1.00 18.12 ?  381 ARG A CA    1 
ATOM   2975 C C     . ARG A 1 381 ? -3.668  25.367 -1.756  1.00 17.90 ?  381 ARG A C     1 
ATOM   2976 O O     . ARG A 1 381 ? -3.641  25.850 -2.891  1.00 20.76 ?  381 ARG A O     1 
ATOM   2977 C CB    . ARG A 1 381 ? -1.622  24.609 -0.591  1.00 22.37 ?  381 ARG A CB    1 
ATOM   2978 C CG    . ARG A 1 381 ? -0.352  25.007 0.029   1.00 25.04 ?  381 ARG A CG    1 
ATOM   2979 C CD    . ARG A 1 381 ? 0.343   26.153 -0.744  1.00 30.43 ?  381 ARG A CD    1 
ATOM   2980 N NE    . ARG A 1 381 ? 0.638   27.190 0.239   1.00 25.17 ?  381 ARG A NE    1 
ATOM   2981 C CZ    . ARG A 1 381 ? 1.435   27.006 1.285   1.00 28.25 ?  381 ARG A CZ    1 
ATOM   2982 N NH1   . ARG A 1 381 ? 2.205   25.938 1.385   1.00 31.20 ?  381 ARG A NH1   1 
ATOM   2983 N NH2   . ARG A 1 381 ? 1.451   27.910 2.265   1.00 30.71 ?  381 ARG A NH2   1 
ATOM   2984 N N     . ILE A 1 382 ? -4.547  24.437 -1.395  1.00 17.11 ?  382 ILE A N     1 
ATOM   2985 C CA    . ILE A 1 382 ? -5.619  24.016 -2.287  1.00 19.67 ?  382 ILE A CA    1 
ATOM   2986 C C     . ILE A 1 382 ? -6.476  25.211 -2.700  1.00 20.12 ?  382 ILE A C     1 
ATOM   2987 O O     . ILE A 1 382 ? -6.713  25.445 -3.896  1.00 19.93 ?  382 ILE A O     1 
ATOM   2988 C CB    . ILE A 1 382 ? -6.440  22.906 -1.604  1.00 20.29 ?  382 ILE A CB    1 
ATOM   2989 C CG1   . ILE A 1 382 ? -5.621  21.597 -1.634  1.00 22.70 ?  382 ILE A CG1   1 
ATOM   2990 C CG2   . ILE A 1 382 ? -7.818  22.726 -2.243  1.00 18.07 ?  382 ILE A CG2   1 
ATOM   2991 C CD1   . ILE A 1 382 ? -6.176  20.509 -0.754  1.00 18.65 ?  382 ILE A CD1   1 
ATOM   2992 N N     . MET A 1 383 ? -6.922  26.005 -1.717  1.00 14.99 ?  383 MET A N     1 
ATOM   2993 C CA    . MET A 1 383 ? -7.761  27.169 -2.001  1.00 16.21 ?  383 MET A CA    1 
ATOM   2994 C C     . MET A 1 383 ? -7.025  28.177 -2.884  1.00 18.40 ?  383 MET A C     1 
ATOM   2995 O O     . MET A 1 383 ? -7.620  28.767 -3.796  1.00 19.67 ?  383 MET A O     1 
ATOM   2996 C CB    . MET A 1 383 ? -8.202  27.829 -0.681  1.00 16.22 ?  383 MET A CB    1 
ATOM   2997 C CG    . MET A 1 383 ? -9.285  27.048 0.095   1.00 18.80 ?  383 MET A CG    1 
ATOM   2998 S SD    . MET A 1 383 ? -10.686 26.455 -0.890  1.00 27.08 ?  383 MET A SD    1 
ATOM   2999 C CE    . MET A 1 383 ? -10.807 24.712 -0.417  1.00 23.47 ?  383 MET A CE    1 
ATOM   3000 N N     . GLY A 1 384 ? -5.728  28.372 -2.643  1.00 18.00 ?  384 GLY A N     1 
ATOM   3001 C CA    . GLY A 1 384 ? -4.984  29.419 -3.319  1.00 17.62 ?  384 GLY A CA    1 
ATOM   3002 C C     . GLY A 1 384 ? -4.451  28.981 -4.668  1.00 23.02 ?  384 GLY A C     1 
ATOM   3003 O O     . GLY A 1 384 ? -4.405  29.782 -5.608  1.00 19.84 ?  384 GLY A O     1 
ATOM   3004 N N     . ARG A 1 385 ? -4.076  27.706 -4.790  1.00 17.64 ?  385 ARG A N     1 
ATOM   3005 C CA    . ARG A 1 385 ? -3.322  27.249 -5.952  1.00 22.96 ?  385 ARG A CA    1 
ATOM   3006 C C     . ARG A 1 385 ? -4.082  26.284 -6.839  1.00 23.67 ?  385 ARG A C     1 
ATOM   3007 O O     . ARG A 1 385 ? -3.777  26.216 -8.024  1.00 23.84 ?  385 ARG A O     1 
ATOM   3008 C CB    . ARG A 1 385 ? -2.009  26.566 -5.532  1.00 23.67 ?  385 ARG A CB    1 
ATOM   3009 C CG    . ARG A 1 385 ? -0.904  27.437 -4.865  1.00 24.78 ?  385 ARG A CG    1 
ATOM   3010 C CD    . ARG A 1 385 ? -0.790  28.855 -5.433  1.00 34.82 ?  385 ARG A CD    1 
ATOM   3011 N NE    . ARG A 1 385 ? -0.624  28.896 -6.885  1.00 40.82 ?  385 ARG A NE    1 
ATOM   3012 C CZ    . ARG A 1 385 ? -0.993  29.914 -7.657  1.00 42.08 ?  385 ARG A CZ    1 
ATOM   3013 N NH1   . ARG A 1 385 ? -1.533  31.016 -7.147  1.00 39.82 ?  385 ARG A NH1   1 
ATOM   3014 N NH2   . ARG A 1 385 ? -0.831  29.821 -8.975  1.00 42.32 ?  385 ARG A NH2   1 
ATOM   3015 N N     . HIS A 1 386 ? -5.040  25.519 -6.299  1.00 20.93 ?  386 HIS A N     1 
ATOM   3016 C CA    . HIS A 1 386 ? -5.849  24.588 -7.089  1.00 24.97 ?  386 HIS A CA    1 
ATOM   3017 C C     . HIS A 1 386 ? -7.202  25.182 -7.464  1.00 21.31 ?  386 HIS A C     1 
ATOM   3018 O O     . HIS A 1 386 ? -7.507  25.342 -8.644  1.00 24.27 ?  386 HIS A O     1 
ATOM   3019 C CB    . HIS A 1 386 ? -6.063  23.268 -6.331  1.00 22.86 ?  386 HIS A CB    1 
ATOM   3020 C CG    . HIS A 1 386 ? -4.813  22.463 -6.151  1.00 24.25 ?  386 HIS A CG    1 
ATOM   3021 N ND1   . HIS A 1 386 ? -4.787  21.274 -5.450  1.00 26.40 ?  386 HIS A ND1   1 
ATOM   3022 C CD2   . HIS A 1 386 ? -3.543  22.678 -6.574  1.00 27.72 ?  386 HIS A CD2   1 
ATOM   3023 C CE1   . HIS A 1 386 ? -3.554  20.797 -5.439  1.00 28.11 ?  386 HIS A CE1   1 
ATOM   3024 N NE2   . HIS A 1 386 ? -2.779  21.632 -6.110  1.00 29.42 ?  386 HIS A NE2   1 
ATOM   3025 N N     . LEU A 1 387 ? -8.035  25.499 -6.476  1.00 23.83 ?  387 LEU A N     1 
ATOM   3026 C CA    . LEU A 1 387 ? -9.299  26.164 -6.770  1.00 21.26 ?  387 LEU A CA    1 
ATOM   3027 C C     . LEU A 1 387 ? -9.103  27.628 -7.145  1.00 19.39 ?  387 LEU A C     1 
ATOM   3028 O O     . LEU A 1 387 ? -9.945  28.191 -7.850  1.00 19.94 ?  387 LEU A O     1 
ATOM   3029 C CB    . LEU A 1 387 ? -10.251 26.059 -5.576  1.00 18.26 ?  387 LEU A CB    1 
ATOM   3030 C CG    . LEU A 1 387 ? -10.560 24.640 -5.103  1.00 26.78 ?  387 LEU A CG    1 
ATOM   3031 C CD1   . LEU A 1 387 ? -11.792 24.612 -4.177  1.00 23.92 ?  387 LEU A CD1   1 
ATOM   3032 C CD2   . LEU A 1 387 ? -10.739 23.706 -6.290  1.00 27.27 ?  387 LEU A CD2   1 
ATOM   3033 N N     . LYS A 1 388 ? -7.994  28.227 -6.725  1.00 18.80 ?  388 LYS A N     1 
ATOM   3034 C CA    . LYS A 1 388 ? -7.699  29.650 -6.943  1.00 21.09 ?  388 LYS A CA    1 
ATOM   3035 C C     . LYS A 1 388 ? -8.900  30.538 -6.611  1.00 18.19 ?  388 LYS A C     1 
ATOM   3036 O O     . LYS A 1 388 ? -9.329  31.379 -7.407  1.00 17.70 ?  388 LYS A O     1 
ATOM   3037 C CB    . LYS A 1 388 ? -7.198  29.888 -8.369  1.00 20.71 ?  388 LYS A CB    1 
ATOM   3038 C CG    . LYS A 1 388 ? -5.912  29.116 -8.677  1.00 23.19 ?  388 LYS A CG    1 
ATOM   3039 C CD    . LYS A 1 388 ? -5.450  29.313 -10.126 1.00 24.37 ?  388 LYS A CD    1 
ATOM   3040 C CE    . LYS A 1 388 ? -4.123  28.597 -10.403 1.00 34.11 ?  388 LYS A CE    1 
ATOM   3041 N NZ    . LYS A 1 388 ? -3.672  28.702 -11.835 1.00 41.42 ?  388 LYS A NZ    1 
ATOM   3042 N N     . VAL A 1 389 ? -9.433  30.355 -5.397  1.00 17.27 ?  389 VAL A N     1 
ATOM   3043 C CA    . VAL A 1 389 ? -10.568 31.137 -4.917  1.00 19.92 ?  389 VAL A CA    1 
ATOM   3044 C C     . VAL A 1 389 ? -10.161 32.232 -3.941  1.00 20.04 ?  389 VAL A C     1 
ATOM   3045 O O     . VAL A 1 389 ? -11.024 32.989 -3.478  1.00 16.91 ?  389 VAL A O     1 
ATOM   3046 C CB    . VAL A 1 389 ? -11.632 30.236 -4.255  1.00 21.09 ?  389 VAL A CB    1 
ATOM   3047 C CG1   . VAL A 1 389 ? -12.234 29.278 -5.282  1.00 18.78 ?  389 VAL A CG1   1 
ATOM   3048 C CG2   . VAL A 1 389 ? -11.021 29.494 -3.078  1.00 19.05 ?  389 VAL A CG2   1 
ATOM   3049 N N     . GLY A 1 390 ? -8.888  32.321 -3.584  1.00 19.57 ?  390 GLY A N     1 
ATOM   3050 C CA    . GLY A 1 390 ? -8.464  33.390 -2.696  1.00 20.26 ?  390 GLY A CA    1 
ATOM   3051 C C     . GLY A 1 390 ? -6.989  33.668 -2.872  1.00 17.42 ?  390 GLY A C     1 
ATOM   3052 O O     . GLY A 1 390 ? -6.290  32.960 -3.599  1.00 18.91 ?  390 GLY A O     1 
ATOM   3053 N N     . VAL A 1 391 ? -6.526  34.733 -2.214  1.00 18.01 ?  391 VAL A N     1 
ATOM   3054 C CA    . VAL A 1 391 ? -5.136  35.185 -2.301  1.00 18.59 ?  391 VAL A CA    1 
ATOM   3055 C C     . VAL A 1 391 ? -4.467  34.944 -0.955  1.00 19.07 ?  391 VAL A C     1 
ATOM   3056 O O     . VAL A 1 391 ? -4.969  35.410 0.078   1.00 18.27 ?  391 VAL A O     1 
ATOM   3057 C CB    . VAL A 1 391 ? -5.048  36.676 -2.680  1.00 19.55 ?  391 VAL A CB    1 
ATOM   3058 C CG1   . VAL A 1 391 ? -3.585  37.175 -2.621  1.00 14.93 ?  391 VAL A CG1   1 
ATOM   3059 C CG2   . VAL A 1 391 ? -5.661  36.929 -4.059  1.00 17.73 ?  391 VAL A CG2   1 
ATOM   3060 N N     . GLU A 1 392 ? -3.324  34.249 -0.961  1.00 14.21 ?  392 GLU A N     1 
ATOM   3061 C CA    . GLU A 1 392 ? -2.641  33.935 0.281   1.00 17.64 ?  392 GLU A CA    1 
ATOM   3062 C C     . GLU A 1 392 ? -1.668  35.050 0.636   1.00 20.17 ?  392 GLU A C     1 
ATOM   3063 O O     . GLU A 1 392 ? -1.017  35.618 -0.241  1.00 19.83 ?  392 GLU A O     1 
ATOM   3064 C CB    . GLU A 1 392 ? -1.895  32.592 0.203   1.00 18.43 ?  392 GLU A CB    1 
ATOM   3065 C CG    . GLU A 1 392 ? -1.411  32.140 1.604   1.00 21.17 ?  392 GLU A CG    1 
ATOM   3066 C CD    . GLU A 1 392 ? -0.727  30.757 1.669   1.00 25.66 ?  392 GLU A CD    1 
ATOM   3067 O OE1   . GLU A 1 392 ? -0.803  29.969 0.694   1.00 26.94 ?  392 GLU A OE1   1 
ATOM   3068 O OE2   . GLU A 1 392 ? -0.137  30.456 2.732   1.00 26.92 -1 392 GLU A OE2   1 
ATOM   3069 N N     . VAL A 1 393 ? -1.579  35.362 1.929   1.00 16.53 ?  393 VAL A N     1 
ATOM   3070 C CA    . VAL A 1 393 ? -0.660  36.389 2.417   1.00 15.18 ?  393 VAL A CA    1 
ATOM   3071 C C     . VAL A 1 393 ? 0.747   35.797 2.453   1.00 20.17 ?  393 VAL A C     1 
ATOM   3072 O O     . VAL A 1 393 ? 0.955   34.721 3.020   1.00 16.09 ?  393 VAL A O     1 
ATOM   3073 C CB    . VAL A 1 393 ? -1.096  36.885 3.811   1.00 18.48 ?  393 VAL A CB    1 
ATOM   3074 C CG1   . VAL A 1 393 ? 0.025   37.760 4.481   1.00 14.45 ?  393 VAL A CG1   1 
ATOM   3075 C CG2   . VAL A 1 393 ? -2.449  37.614 3.745   1.00 11.17 ?  393 VAL A CG2   1 
ATOM   3076 N N     . LYS A 1 394 ? 1.714   36.485 1.837   1.00 18.87 ?  394 LYS A N     1 
ATOM   3077 C CA    . LYS A 1 394 ? 3.101   36.002 1.819   1.00 21.23 ?  394 LYS A CA    1 
ATOM   3078 C C     . LYS A 1 394 ? 3.700   35.910 3.225   1.00 19.58 ?  394 LYS A C     1 
ATOM   3079 O O     . LYS A 1 394 ? 3.607   36.856 4.012   1.00 21.32 ?  394 LYS A O     1 
ATOM   3080 C CB    . LYS A 1 394 ? 3.973   36.936 0.966   1.00 26.86 ?  394 LYS A CB    1 
ATOM   3081 C CG    . LYS A 1 394 ? 3.470   37.132 -0.456  1.00 36.25 ?  394 LYS A CG    1 
ATOM   3082 C CD    . LYS A 1 394 ? 3.821   35.929 -1.345  1.00 46.72 ?  394 LYS A CD    1 
ATOM   3083 C CE    . LYS A 1 394 ? 3.323   36.131 -2.778  1.00 49.38 ?  394 LYS A CE    1 
ATOM   3084 N NZ    . LYS A 1 394 ? 3.272   37.574 -3.163  1.00 48.59 ?  394 LYS A NZ    1 
ATOM   3085 N N     . LYS A 1 395 ? 4.348   34.776 3.518   1.00 19.99 ?  395 LYS A N     1 
ATOM   3086 C CA    . LYS A 1 395 ? 5.071   34.506 4.756   1.00 16.69 ?  395 LYS A CA    1 
ATOM   3087 C C     . LYS A 1 395 ? 6.561   34.286 4.466   1.00 24.82 ?  395 LYS A C     1 
ATOM   3088 O O     . LYS A 1 395 ? 6.927   33.802 3.396   1.00 23.39 ?  395 LYS A O     1 
ATOM   3089 C CB    . LYS A 1 395 ? 4.514   33.244 5.466   1.00 22.53 ?  395 LYS A CB    1 
ATOM   3090 C CG    . LYS A 1 395 ? 3.089   33.368 6.082   1.00 29.36 ?  395 LYS A CG    1 
ATOM   3091 C CD    . LYS A 1 395 ? 2.698   32.109 6.892   1.00 24.85 ?  395 LYS A CD    1 
ATOM   3092 C CE    . LYS A 1 395 ? 2.600   30.860 5.977   1.00 30.59 ?  395 LYS A CE    1 
ATOM   3093 N NZ    . LYS A 1 395 ? 2.438   29.544 6.716   1.00 27.47 ?  395 LYS A NZ    1 
ATOM   3094 N N     . GLY A 1 396 ? 7.418   34.604 5.436   1.00 20.21 ?  396 GLY A N     1 
ATOM   3095 C CA    . GLY A 1 396 ? 8.825   34.245 5.314   1.00 21.06 ?  396 GLY A CA    1 
ATOM   3096 C C     . GLY A 1 396 ? 9.020   32.743 5.140   1.00 25.04 ?  396 GLY A C     1 
ATOM   3097 O O     . GLY A 1 396 ? 8.373   31.926 5.802   1.00 22.85 ?  396 GLY A O     1 
ATOM   3098 N N     . GLU A 1 397 ? 9.934   32.380 4.236   1.00 19.92 ?  397 GLU A N     1 
ATOM   3099 C CA    . GLU A 1 397 ? 10.153  30.974 3.897   1.00 23.24 ?  397 GLU A CA    1 
ATOM   3100 C C     . GLU A 1 397 ? 10.529  30.149 5.127   1.00 22.30 ?  397 GLU A C     1 
ATOM   3101 O O     . GLU A 1 397 ? 9.959   29.079 5.367   1.00 23.84 ?  397 GLU A O     1 
ATOM   3102 C CB    . GLU A 1 397 ? 11.246  30.868 2.830   1.00 24.36 ?  397 GLU A CB    1 
ATOM   3103 C CG    . GLU A 1 397 ? 11.622  29.440 2.438   1.00 27.30 ?  397 GLU A CG    1 
ATOM   3104 C CD    . GLU A 1 397 ? 10.482  28.724 1.719   1.00 36.74 ?  397 GLU A CD    1 
ATOM   3105 O OE1   . GLU A 1 397 ? 10.458  27.459 1.711   1.00 33.71 ?  397 GLU A OE1   1 
ATOM   3106 O OE2   . GLU A 1 397 ? 9.612   29.442 1.157   1.00 32.85 -1 397 GLU A OE2   1 
ATOM   3107 N N     . GLU A 1 398 ? 11.495  30.627 5.908   1.00 20.10 ?  398 GLU A N     1 
ATOM   3108 C CA    . GLU A 1 398 ? 12.013  29.953 7.095   1.00 21.44 ?  398 GLU A CA    1 
ATOM   3109 C C     . GLU A 1 398 ? 11.328  30.398 8.395   1.00 24.48 ?  398 GLU A C     1 
ATOM   3110 O O     . GLU A 1 398 ? 11.169  29.580 9.303   1.00 22.13 ?  398 GLU A O     1 
ATOM   3111 C CB    . GLU A 1 398 ? 13.533  30.195 7.232   1.00 25.03 ?  398 GLU A CB    1 
ATOM   3112 C CG    . GLU A 1 398 ? 14.402  29.879 5.988   1.00 28.19 ?  398 GLU A CG    1 
ATOM   3113 C CD    . GLU A 1 398 ? 14.618  28.382 5.711   1.00 36.92 ?  398 GLU A CD    1 
ATOM   3114 O OE1   . GLU A 1 398 ? 14.235  27.538 6.550   1.00 42.95 ?  398 GLU A OE1   1 
ATOM   3115 O OE2   . GLU A 1 398 ? 15.201  28.046 4.653   1.00 41.60 -1 398 GLU A OE2   1 
ATOM   3116 N N     . ASP A 1 399 ? 10.931  31.675 8.543   1.00 21.13 ?  399 ASP A N     1 
ATOM   3117 C CA    . ASP A 1 399 ? 10.413  32.104 9.847   1.00 20.73 ?  399 ASP A CA    1 
ATOM   3118 C C     . ASP A 1 399 ? 8.882   32.071 9.969   1.00 19.36 ?  399 ASP A C     1 
ATOM   3119 O O     . ASP A 1 399 ? 8.376   32.136 11.090  1.00 23.04 ?  399 ASP A O     1 
ATOM   3120 C CB    . ASP A 1 399 ? 10.944  33.497 10.228  1.00 20.52 ?  399 ASP A CB    1 
ATOM   3121 C CG    . ASP A 1 399 ? 10.531  34.621 9.262   1.00 21.24 ?  399 ASP A CG    1 
ATOM   3122 O OD1   . ASP A 1 399 ? 9.454   34.555 8.621   1.00 22.00 ?  399 ASP A OD1   1 
ATOM   3123 O OD2   . ASP A 1 399 ? 11.280  35.630 9.207   1.00 18.72 -1 399 ASP A OD2   1 
ATOM   3124 N N     . GLY A 1 400 ? 8.137   31.972 8.871   1.00 18.84 ?  400 GLY A N     1 
ATOM   3125 C CA    . GLY A 1 400 ? 6.686   31.853 8.976   1.00 20.60 ?  400 GLY A CA    1 
ATOM   3126 C C     . GLY A 1 400 ? 5.945   33.116 9.372   1.00 23.73 ?  400 GLY A C     1 
ATOM   3127 O O     . GLY A 1 400 ? 4.775   33.042 9.781   1.00 19.49 ?  400 GLY A O     1 
ATOM   3128 N N     . LEU A 1 401 ? 6.571   34.281 9.227   1.00 19.06 ?  401 LEU A N     1 
ATOM   3129 C CA    . LEU A 1 401 ? 6.000   35.546 9.658   1.00 18.80 ?  401 LEU A CA    1 
ATOM   3130 C C     . LEU A 1 401 ? 5.581   36.384 8.457   1.00 20.71 ?  401 LEU A C     1 
ATOM   3131 O O     . LEU A 1 401 ? 6.136   36.248 7.358   1.00 17.54 ?  401 LEU A O     1 
ATOM   3132 C CB    . LEU A 1 401 ? 7.011   36.322 10.510  1.00 20.60 ?  401 LEU A CB    1 
ATOM   3133 C CG    . LEU A 1 401 ? 7.605   35.627 11.736  1.00 21.27 ?  401 LEU A CG    1 
ATOM   3134 C CD1   . LEU A 1 401 ? 8.798   36.427 12.289  1.00 19.67 ?  401 LEU A CD1   1 
ATOM   3135 C CD2   . LEU A 1 401 ? 6.527   35.455 12.796  1.00 18.15 ?  401 LEU A CD2   1 
ATOM   3136 N N     . PHE A 1 402 ? 4.606   37.273 8.671   1.00 17.06 ?  402 PHE A N     1 
ATOM   3137 C CA    . PHE A 1 402 ? 4.185   38.192 7.625   1.00 17.18 ?  402 PHE A CA    1 
ATOM   3138 C C     . PHE A 1 402 ? 4.455   39.636 8.035   1.00 18.26 ?  402 PHE A C     1 
ATOM   3139 O O     . PHE A 1 402 ? 4.635   39.952 9.212   1.00 21.01 ?  402 PHE A O     1 
ATOM   3140 C CB    . PHE A 1 402 ? 2.691   38.020 7.271   1.00 17.86 ?  402 PHE A CB    1 
ATOM   3141 C CG    . PHE A 1 402 ? 1.764   38.069 8.457   1.00 15.30 ?  402 PHE A CG    1 
ATOM   3142 C CD1   . PHE A 1 402 ? 1.336   39.279 8.974   1.00 18.02 ?  402 PHE A CD1   1 
ATOM   3143 C CD2   . PHE A 1 402 ? 1.308   36.899 9.044   1.00 19.37 ?  402 PHE A CD2   1 
ATOM   3144 C CE1   . PHE A 1 402 ? 0.465   39.325 10.076  1.00 19.68 ?  402 PHE A CE1   1 
ATOM   3145 C CE2   . PHE A 1 402 ? 0.448   36.924 10.137  1.00 19.04 ?  402 PHE A CE2   1 
ATOM   3146 C CZ    . PHE A 1 402 ? 0.029   38.145 10.655  1.00 21.34 ?  402 PHE A CZ    1 
ATOM   3147 N N     . THR A 1 403 ? 4.478   40.512 7.046   1.00 17.98 ?  403 THR A N     1 
ATOM   3148 C CA    . THR A 1 403 ? 4.576   41.952 7.254   1.00 20.93 ?  403 THR A CA    1 
ATOM   3149 C C     . THR A 1 403 ? 3.196   42.580 7.128   1.00 20.04 ?  403 THR A C     1 
ATOM   3150 O O     . THR A 1 403 ? 2.291   42.027 6.497   1.00 18.44 ?  403 THR A O     1 
ATOM   3151 C CB    . THR A 1 403 ? 5.494   42.623 6.217   1.00 20.34 ?  403 THR A CB    1 
ATOM   3152 O OG1   . THR A 1 403 ? 4.908   42.470 4.914   1.00 19.00 ?  403 THR A OG1   1 
ATOM   3153 C CG2   . THR A 1 403 ? 6.910   42.047 6.228   1.00 18.86 ?  403 THR A CG2   1 
ATOM   3154 N N     . LYS A 1 404 ? 3.062   43.781 7.682   1.00 19.00 ?  404 LYS A N     1 
ATOM   3155 C CA    . LYS A 1 404 ? 1.814   44.494 7.507   1.00 20.48 ?  404 LYS A CA    1 
ATOM   3156 C C     . LYS A 1 404 ? 1.596   44.827 6.047   1.00 21.17 ?  404 LYS A C     1 
ATOM   3157 O O     . LYS A 1 404 ? 0.449   44.876 5.591   1.00 23.50 ?  404 LYS A O     1 
ATOM   3158 C CB    . LYS A 1 404 ? 1.776   45.751 8.382   1.00 20.92 ?  404 LYS A CB    1 
ATOM   3159 C CG    . LYS A 1 404 ? 2.751   46.884 8.003   1.00 23.01 ?  404 LYS A CG    1 
ATOM   3160 C CD    . LYS A 1 404 ? 2.741   47.965 9.112   1.00 23.21 ?  404 LYS A CD    1 
ATOM   3161 C CE    . LYS A 1 404 ? 3.562   49.205 8.756   1.00 26.40 ?  404 LYS A CE    1 
ATOM   3162 N NZ    . LYS A 1 404 ? 5.016   48.912 8.825   1.00 23.86 ?  404 LYS A NZ    1 
ATOM   3163 N N     . GLU A 1 405 ? 2.680   45.031 5.288   1.00 19.80 ?  405 GLU A N     1 
ATOM   3164 C CA    . GLU A 1 405 ? 2.522   45.332 3.869   1.00 21.70 ?  405 GLU A CA    1 
ATOM   3165 C C     . GLU A 1 405 ? 2.006   44.121 3.100   1.00 19.46 ?  405 GLU A C     1 
ATOM   3166 O O     . GLU A 1 405 ? 1.273   44.286 2.129   1.00 18.68 ?  405 GLU A O     1 
ATOM   3167 C CB    . GLU A 1 405 ? 3.841   45.829 3.263   1.00 20.30 ?  405 GLU A CB    1 
ATOM   3168 C CG    . GLU A 1 405 ? 4.318   47.210 3.804   1.00 23.20 ?  405 GLU A CG    1 
ATOM   3169 C CD    . GLU A 1 405 ? 5.013   47.127 5.187   1.00 27.26 ?  405 GLU A CD    1 
ATOM   3170 O OE1   . GLU A 1 405 ? 5.314   46.004 5.653   1.00 26.80 ?  405 GLU A OE1   1 
ATOM   3171 O OE2   . GLU A 1 405 ? 5.242   48.191 5.816   1.00 27.53 -1 405 GLU A OE2   1 
ATOM   3172 N N     . SER A 1 406 ? 2.336   42.900 3.532   1.00 20.25 ?  406 SER A N     1 
ATOM   3173 C CA    . SER A 1 406 ? 1.810   41.735 2.822   1.00 19.13 ?  406 SER A CA    1 
ATOM   3174 C C     . SER A 1 406 ? 0.314   41.552 3.077   1.00 18.55 ?  406 SER A C     1 
ATOM   3175 O O     . SER A 1 406 ? -0.436  41.181 2.161   1.00 17.59 ?  406 SER A O     1 
ATOM   3176 C CB    . SER A 1 406 ? 2.602   40.491 3.208   1.00 21.13 ?  406 SER A CB    1 
ATOM   3177 O OG    . SER A 1 406 ? 3.898   40.543 2.603   1.00 23.33 ?  406 SER A OG    1 
ATOM   3178 N N     . VAL A 1 407 ? -0.133  41.831 4.305   1.00 17.61 ?  407 VAL A N     1 
ATOM   3179 C CA    . VAL A 1 407 ? -1.561  41.841 4.634   1.00 15.02 ?  407 VAL A CA    1 
ATOM   3180 C C     . VAL A 1 407 ? -2.289  42.913 3.832   1.00 16.88 ?  407 VAL A C     1 
ATOM   3181 O O     . VAL A 1 407 ? -3.330  42.663 3.211   1.00 19.89 ?  407 VAL A O     1 
ATOM   3182 C CB    . VAL A 1 407 ? -1.755  42.078 6.141   1.00 15.13 ?  407 VAL A CB    1 
ATOM   3183 C CG1   . VAL A 1 407 ? -3.231  42.267 6.451   1.00 14.15 ?  407 VAL A CG1   1 
ATOM   3184 C CG2   . VAL A 1 407 ? -1.142  40.951 6.974   1.00 15.55 ?  407 VAL A CG2   1 
ATOM   3185 N N     . TYR A 1 408 ? -1.774  44.141 3.882   1.00 19.87 ?  408 TYR A N     1 
ATOM   3186 C CA    . TYR A 1 408 ? -2.343  45.239 3.109   1.00 20.24 ?  408 TYR A CA    1 
ATOM   3187 C C     . TYR A 1 408 ? -2.468  44.881 1.629   1.00 23.04 ?  408 TYR A C     1 
ATOM   3188 O O     . TYR A 1 408 ? -3.503  45.142 0.998   1.00 23.01 ?  408 TYR A O     1 
ATOM   3189 C CB    . TYR A 1 408 ? -1.472  46.486 3.288   1.00 22.25 ?  408 TYR A CB    1 
ATOM   3190 C CG    . TYR A 1 408 ? -1.683  47.539 2.233   1.00 26.37 ?  408 TYR A CG    1 
ATOM   3191 C CD1   . TYR A 1 408 ? -2.799  48.390 2.281   1.00 25.04 ?  408 TYR A CD1   1 
ATOM   3192 C CD2   . TYR A 1 408 ? -0.788  47.682 1.181   1.00 28.63 ?  408 TYR A CD2   1 
ATOM   3193 C CE1   . TYR A 1 408 ? -3.001  49.371 1.315   1.00 27.91 ?  408 TYR A CE1   1 
ATOM   3194 C CE2   . TYR A 1 408 ? -0.978  48.656 0.206   1.00 32.10 ?  408 TYR A CE2   1 
ATOM   3195 C CZ    . TYR A 1 408 ? -2.082  49.502 0.280   1.00 30.89 ?  408 TYR A CZ    1 
ATOM   3196 O OH    . TYR A 1 408 ? -2.277  50.467 -0.686  1.00 34.60 ?  408 TYR A OH    1 
ATOM   3197 N N     . GLU A 1 409 ? -1.412  44.294 1.060   1.00 21.23 ?  409 GLU A N     1 
ATOM   3198 C CA    . GLU A 1 409 ? -1.394  43.962 -0.361  1.00 21.28 ?  409 GLU A CA    1 
ATOM   3199 C C     . GLU A 1 409 ? -2.479  42.964 -0.722  1.00 18.79 ?  409 GLU A C     1 
ATOM   3200 O O     . GLU A 1 409 ? -3.139  43.110 -1.756  1.00 20.27 ?  409 GLU A O     1 
ATOM   3201 C CB    . GLU A 1 409 ? -0.040  43.370 -0.763  1.00 26.58 ?  409 GLU A CB    1 
ATOM   3202 C CG    . GLU A 1 409 ? 1.106   44.353 -0.960  1.00 40.73 ?  409 GLU A CG    1 
ATOM   3203 C CD    . GLU A 1 409 ? 0.820   45.398 -2.030  1.00 52.84 ?  409 GLU A CD    1 
ATOM   3204 O OE1   . GLU A 1 409 ? -0.035  45.134 -2.916  1.00 47.99 ?  409 GLU A OE1   1 
ATOM   3205 O OE2   . GLU A 1 409 ? 1.476   46.473 -1.993  1.00 63.02 -1 409 GLU A OE2   1 
ATOM   3206 N N     . ALA A 1 410 ? -2.640  41.916 0.088   1.00 16.71 ?  410 ALA A N     1 
ATOM   3207 C CA    . ALA A 1 410 ? -3.595  40.866 -0.255  1.00 20.59 ?  410 ALA A CA    1 
ATOM   3208 C C     . ALA A 1 410 ? -5.021  41.403 -0.237  1.00 19.30 ?  410 ALA A C     1 
ATOM   3209 O O     . ALA A 1 410 ? -5.826  41.087 -1.121  1.00 19.11 ?  410 ALA A O     1 
ATOM   3210 C CB    . ALA A 1 410 ? -3.440  39.672 0.699   1.00 16.03 ?  410 ALA A CB    1 
ATOM   3211 N N     . VAL A 1 411 ? -5.343  42.238 0.747   1.00 20.09 ?  411 VAL A N     1 
ATOM   3212 C CA    . VAL A 1 411 ? -6.694  42.778 0.839   1.00 21.59 ?  411 VAL A CA    1 
ATOM   3213 C C     . VAL A 1 411 ? -6.951  43.750 -0.309  1.00 21.96 ?  411 VAL A C     1 
ATOM   3214 O O     . VAL A 1 411 ? -8.016  43.728 -0.950  1.00 21.72 ?  411 VAL A O     1 
ATOM   3215 C CB    . VAL A 1 411 ? -6.897  43.440 2.217   1.00 20.28 ?  411 VAL A CB    1 
ATOM   3216 C CG1   . VAL A 1 411 ? -8.217  44.198 2.270   1.00 21.35 ?  411 VAL A CG1   1 
ATOM   3217 C CG2   . VAL A 1 411 ? -6.809  42.396 3.366   1.00 14.62 ?  411 VAL A CG2   1 
ATOM   3218 N N     . LYS A 1 412 ? -5.964  44.595 -0.600  1.00 20.08 ?  412 LYS A N     1 
ATOM   3219 C CA    . LYS A 1 412 ? -6.087  45.566 -1.680  1.00 25.58 ?  412 LYS A CA    1 
ATOM   3220 C C     . LYS A 1 412 ? -6.318  44.887 -3.027  1.00 22.35 ?  412 LYS A C     1 
ATOM   3221 O O     . LYS A 1 412 ? -7.081  45.385 -3.854  1.00 24.02 ?  412 LYS A O     1 
ATOM   3222 C CB    . LYS A 1 412 ? -4.827  46.431 -1.719  1.00 25.09 ?  412 LYS A CB    1 
ATOM   3223 C CG    . LYS A 1 412 ? -4.947  47.709 -2.535  1.00 37.04 ?  412 LYS A CG    1 
ATOM   3224 C CD    . LYS A 1 412 ? -3.702  47.942 -3.396  1.00 39.46 ?  412 LYS A CD    1 
ATOM   3225 C CE    . LYS A 1 412 ? -3.432  46.725 -4.309  1.00 42.72 ?  412 LYS A CE    1 
ATOM   3226 N NZ    . LYS A 1 412 ? -2.910  47.079 -5.682  1.00 41.56 ?  412 LYS A NZ    1 
ATOM   3227 N N     . ILE A 1 413 ? -5.657  43.756 -3.270  1.00 21.34 ?  413 ILE A N     1 
ATOM   3228 C CA    . ILE A 1 413 ? -5.774  43.077 -4.560  1.00 23.53 ?  413 ILE A CA    1 
ATOM   3229 C C     . ILE A 1 413 ? -7.194  42.564 -4.770  1.00 27.62 ?  413 ILE A C     1 
ATOM   3230 O O     . ILE A 1 413 ? -7.762  42.685 -5.871  1.00 24.68 ?  413 ILE A O     1 
ATOM   3231 C CB    . ILE A 1 413 ? -4.738  41.931 -4.647  1.00 27.33 ?  413 ILE A CB    1 
ATOM   3232 C CG1   . ILE A 1 413 ? -3.320  42.477 -4.791  1.00 24.95 ?  413 ILE A CG1   1 
ATOM   3233 C CG2   . ILE A 1 413 ? -5.042  40.962 -5.796  1.00 26.51 ?  413 ILE A CG2   1 
ATOM   3234 C CD1   . ILE A 1 413 ? -2.284  41.383 -4.887  1.00 25.87 ?  413 ILE A CD1   1 
ATOM   3235 N N     . VAL A 1 414 ? -7.798  41.989 -3.724  1.00 20.37 ?  414 VAL A N     1 
ATOM   3236 C CA    . VAL A 1 414 ? -9.133  41.407 -3.894  1.00 22.73 ?  414 VAL A CA    1 
ATOM   3237 C C     . VAL A 1 414 ? -10.242 42.450 -3.796  1.00 24.22 ?  414 VAL A C     1 
ATOM   3238 O O     . VAL A 1 414 ? -11.357 42.204 -4.277  1.00 27.32 ?  414 VAL A O     1 
ATOM   3239 C CB    . VAL A 1 414 ? -9.403  40.279 -2.879  1.00 21.58 ?  414 VAL A CB    1 
ATOM   3240 C CG1   . VAL A 1 414 ? -8.375  39.202 -2.999  1.00 19.16 ?  414 VAL A CG1   1 
ATOM   3241 C CG2   . VAL A 1 414 ? -9.487  40.821 -1.429  1.00 23.07 ?  414 VAL A CG2   1 
ATOM   3242 N N     . MET A 1 415 ? -9.984  43.597 -3.176  1.00 24.20 ?  415 MET A N     1 
ATOM   3243 C CA    . MET A 1 415 ? -11.005 44.629 -3.068  1.00 26.01 ?  415 MET A CA    1 
ATOM   3244 C C     . MET A 1 415 ? -11.014 45.568 -4.274  1.00 26.15 ?  415 MET A C     1 
ATOM   3245 O O     . MET A 1 415 ? -12.009 46.263 -4.499  1.00 26.97 ?  415 MET A O     1 
ATOM   3246 C CB    . MET A 1 415 ? -10.791 45.425 -1.780  1.00 24.71 ?  415 MET A CB    1 
ATOM   3247 C CG    . MET A 1 415 ? -11.110 44.633 -0.488  1.00 26.04 ?  415 MET A CG    1 
ATOM   3248 S SD    . MET A 1 415 ? -12.840 44.090 -0.431  1.00 31.46 ?  415 MET A SD    1 
ATOM   3249 C CE    . MET A 1 415 ? -13.429 45.171 0.871   1.00 26.99 ?  415 MET A CE    1 
ATOM   3250 N N     . ASP A 1 416 ? -9.954  45.567 -5.074  1.00 27.58 ?  416 ASP A N     1 
ATOM   3251 C CA    . ASP A 1 416 ? -9.831  46.435 -6.246  1.00 28.90 ?  416 ASP A CA    1 
ATOM   3252 C C     . ASP A 1 416 ? -10.619 45.833 -7.410  1.00 34.56 ?  416 ASP A C     1 
ATOM   3253 O O     . ASP A 1 416 ? -10.194 44.837 -8.005  1.00 33.85 ?  416 ASP A O     1 
ATOM   3254 C CB    . ASP A 1 416 ? -8.349  46.600 -6.585  1.00 32.67 ?  416 ASP A CB    1 
ATOM   3255 C CG    . ASP A 1 416 ? -8.090  47.549 -7.772  1.00 40.22 ?  416 ASP A CG    1 
ATOM   3256 O OD1   . ASP A 1 416 ? -9.051  47.966 -8.463  1.00 35.58 ?  416 ASP A OD1   1 
ATOM   3257 O OD2   . ASP A 1 416 ? -6.897  47.877 -7.996  1.00 39.75 -1 416 ASP A OD2   1 
ATOM   3258 N N     . ASP A 1 417 ? -11.764 46.444 -7.740  1.00 35.93 ?  417 ASP A N     1 
ATOM   3259 C CA    . ASP A 1 417 ? -12.578 46.006 -8.876  1.00 42.53 ?  417 ASP A CA    1 
ATOM   3260 C C     . ASP A 1 417 ? -11.783 45.884 -10.173 1.00 41.82 ?  417 ASP A C     1 
ATOM   3261 O O     . ASP A 1 417 ? -12.114 45.053 -11.027 1.00 46.27 ?  417 ASP A O     1 
ATOM   3262 C CB    . ASP A 1 417 ? -13.731 46.983 -9.108  1.00 41.92 ?  417 ASP A CB    1 
ATOM   3263 C CG    . ASP A 1 417 ? -14.998 46.557 -8.421  1.00 53.81 ?  417 ASP A CG    1 
ATOM   3264 O OD1   . ASP A 1 417 ? -15.211 45.333 -8.287  1.00 61.90 ?  417 ASP A OD1   1 
ATOM   3265 O OD2   . ASP A 1 417 ? -15.787 47.446 -8.026  1.00 62.03 -1 417 ASP A OD2   1 
ATOM   3266 N N     . GLU A 1 418 ? -10.761 46.715 -10.358 1.00 38.76 ?  418 GLU A N     1 
ATOM   3267 C CA    . GLU A 1 418 ? -10.007 46.735 -11.605 1.00 39.29 ?  418 GLU A CA    1 
ATOM   3268 C C     . GLU A 1 418 ? -8.787  45.826 -11.588 1.00 38.27 ?  418 GLU A C     1 
ATOM   3269 O O     . GLU A 1 418 ? -8.087  45.734 -12.602 1.00 37.42 ?  418 GLU A O     1 
ATOM   3270 C CB    . GLU A 1 418 ? -9.579  48.167 -11.944 1.00 44.71 ?  418 GLU A CB    1 
ATOM   3271 C CG    . GLU A 1 418 ? -10.741 49.165 -11.976 1.00 52.61 ?  418 GLU A CG    1 
ATOM   3272 C CD    . GLU A 1 418 ? -10.619 50.209 -13.079 1.00 58.74 ?  418 GLU A CD    1 
ATOM   3273 O OE1   . GLU A 1 418 ? -9.492  50.462 -13.561 1.00 63.07 ?  418 GLU A OE1   1 
ATOM   3274 O OE2   . GLU A 1 418 ? -11.658 50.789 -13.454 1.00 59.17 -1 418 GLU A OE2   1 
ATOM   3275 N N     . ASN A 1 419 ? -8.520  45.142 -10.483 1.00 36.50 ?  419 ASN A N     1 
ATOM   3276 C CA    . ASN A 1 419 ? -7.368  44.257 -10.411 1.00 33.93 ?  419 ASN A CA    1 
ATOM   3277 C C     . ASN A 1 419 ? -7.737  42.898 -10.989 1.00 30.81 ?  419 ASN A C     1 
ATOM   3278 O O     . ASN A 1 419 ? -8.744  42.300 -10.598 1.00 32.18 ?  419 ASN A O     1 
ATOM   3279 C CB    . ASN A 1 419 ? -6.888  44.123 -8.966  1.00 31.49 ?  419 ASN A CB    1 
ATOM   3280 C CG    . ASN A 1 419 ? -5.627  43.299 -8.851  1.00 29.77 ?  419 ASN A CG    1 
ATOM   3281 O OD1   . ASN A 1 419 ? -5.631  42.103 -9.136  1.00 31.70 ?  419 ASN A OD1   1 
ATOM   3282 N ND2   . ASN A 1 419 ? -4.540  43.929 -8.414  1.00 28.57 ?  419 ASN A ND2   1 
ATOM   3283 N N     . GLU A 1 420 ? -6.913  42.408 -11.913 1.00 30.18 ?  420 GLU A N     1 
ATOM   3284 C CA    . GLU A 1 420 ? -7.268  41.201 -12.660 1.00 35.34 ?  420 GLU A CA    1 
ATOM   3285 C C     . GLU A 1 420 ? -7.158  39.941 -11.809 1.00 30.02 ?  420 GLU A C     1 
ATOM   3286 O O     . GLU A 1 420 ? -7.847  38.950 -12.078 1.00 24.79 ?  420 GLU A O     1 
ATOM   3287 C CB    . GLU A 1 420 ? -6.385  41.064 -13.906 1.00 43.68 ?  420 GLU A CB    1 
ATOM   3288 C CG    . GLU A 1 420 ? -6.800  41.989 -15.050 1.00 44.66 ?  420 GLU A CG    1 
ATOM   3289 C CD    . GLU A 1 420 ? -8.275  41.812 -15.442 1.00 47.20 ?  420 GLU A CD    1 
ATOM   3290 O OE1   . GLU A 1 420 ? -8.685  40.672 -15.789 1.00 47.46 ?  420 GLU A OE1   1 
ATOM   3291 O OE2   . GLU A 1 420 ? -9.024  42.822 -15.397 1.00 42.54 -1 420 GLU A OE2   1 
ATOM   3292 N N     . ILE A 1 421 ? -6.277  39.939 -10.812 1.00 27.54 ?  421 ILE A N     1 
ATOM   3293 C CA    . ILE A 1 421 ? -6.210  38.793 -9.918  1.00 31.41 ?  421 ILE A CA    1 
ATOM   3294 C C     . ILE A 1 421 ? -7.423  38.781 -8.995  1.00 26.06 ?  421 ILE A C     1 
ATOM   3295 O O     . ILE A 1 421 ? -8.029  37.729 -8.757  1.00 23.37 ?  421 ILE A O     1 
ATOM   3296 C CB    . ILE A 1 421 ? -4.885  38.804 -9.144  1.00 25.65 ?  421 ILE A CB    1 
ATOM   3297 C CG1   . ILE A 1 421 ? -3.751  38.465 -10.105 1.00 31.94 ?  421 ILE A CG1   1 
ATOM   3298 C CG2   . ILE A 1 421 ? -4.930  37.821 -7.970  1.00 29.75 ?  421 ILE A CG2   1 
ATOM   3299 C CD1   . ILE A 1 421 ? -2.384  38.555 -9.490  1.00 29.53 ?  421 ILE A CD1   1 
ATOM   3300 N N     . GLY A 1 422 ? -7.800  39.951 -8.473  1.00 22.02 ?  422 GLY A N     1 
ATOM   3301 C CA    . GLY A 1 422 ? -9.040  40.048 -7.719  1.00 25.10 ?  422 GLY A CA    1 
ATOM   3302 C C     . GLY A 1 422 ? -10.243 39.586 -8.520  1.00 25.51 ?  422 GLY A C     1 
ATOM   3303 O O     . GLY A 1 422 ? -11.146 38.931 -7.985  1.00 22.18 ?  422 GLY A O     1 
ATOM   3304 N N     . ARG A 1 423 ? -10.269 39.909 -9.817  1.00 25.79 ?  423 ARG A N     1 
ATOM   3305 C CA    . ARG A 1 423 ? -11.392 39.500 -10.651 1.00 26.86 ?  423 ARG A CA    1 
ATOM   3306 C C     . ARG A 1 423 ? -11.379 37.997 -10.874 1.00 21.66 ?  423 ARG A C     1 
ATOM   3307 O O     . ARG A 1 423 ? -12.439 37.359 -10.911 1.00 23.20 ?  423 ARG A O     1 
ATOM   3308 C CB    . ARG A 1 423 ? -11.356 40.256 -11.988 1.00 33.16 ?  423 ARG A CB    1 
ATOM   3309 C CG    . ARG A 1 423 ? -11.546 41.770 -11.840 1.00 37.03 ?  423 ARG A CG    1 
ATOM   3310 C CD    . ARG A 1 423 ? -11.597 42.512 -13.179 1.00 42.87 ?  423 ARG A CD    1 
ATOM   3311 N NE    . ARG A 1 423 ? -12.554 41.940 -14.121 1.00 52.49 ?  423 ARG A NE    1 
ATOM   3312 C CZ    . ARG A 1 423 ? -13.871 41.867 -13.938 1.00 61.28 ?  423 ARG A CZ    1 
ATOM   3313 N NH1   . ARG A 1 423 ? -14.453 42.348 -12.848 1.00 58.17 ?  423 ARG A NH1   1 
ATOM   3314 N NH2   . ARG A 1 423 ? -14.625 41.299 -14.879 1.00 60.44 ?  423 ARG A NH2   1 
ATOM   3315 N N     . GLU A 1 424 ? -10.182 37.420 -11.017 1.00 22.49 ?  424 GLU A N     1 
ATOM   3316 C CA    . GLU A 1 424 ? -10.053 35.987 -11.259 1.00 27.84 ?  424 GLU A CA    1 
ATOM   3317 C C     . GLU A 1 424 ? -10.466 35.166 -10.041 1.00 24.73 ?  424 GLU A C     1 
ATOM   3318 O O     . GLU A 1 424 ? -11.157 34.149 -10.189 1.00 22.31 ?  424 GLU A O     1 
ATOM   3319 C CB    . GLU A 1 424 ? -8.614  35.651 -11.676 1.00 29.36 ?  424 GLU A CB    1 
ATOM   3320 C CG    . GLU A 1 424 ? -8.338  34.153 -11.920 1.00 31.65 ?  424 GLU A CG    1 
ATOM   3321 C CD    . GLU A 1 424 ? -6.854  33.777 -11.708 1.00 49.36 ?  424 GLU A CD    1 
ATOM   3322 O OE1   . GLU A 1 424 ? -6.058  34.655 -11.278 1.00 51.17 ?  424 GLU A OE1   1 
ATOM   3323 O OE2   . GLU A 1 424 ? -6.479  32.608 -11.977 1.00 48.50 -1 424 GLU A OE2   1 
ATOM   3324 N N     . VAL A 1 425 ? -10.035 35.559 -8.832  1.00 24.72 ?  425 VAL A N     1 
ATOM   3325 C CA    . VAL A 1 425 ? -10.464 34.791 -7.663  1.00 20.93 ?  425 VAL A CA    1 
ATOM   3326 C C     . VAL A 1 425 ? -11.967 34.978 -7.419  1.00 20.32 ?  425 VAL A C     1 
ATOM   3327 O O     . VAL A 1 425 ? -12.643 34.054 -6.955  1.00 19.61 ?  425 VAL A O     1 
ATOM   3328 C CB    . VAL A 1 425 ? -9.618  35.121 -6.407  1.00 18.51 ?  425 VAL A CB    1 
ATOM   3329 C CG1   . VAL A 1 425 ? -8.099  34.877 -6.667  1.00 17.59 ?  425 VAL A CG1   1 
ATOM   3330 C CG2   . VAL A 1 425 ? -9.873  36.520 -5.880  1.00 18.26 ?  425 VAL A CG2   1 
ATOM   3331 N N     . ARG A 1 426 ? -12.525 36.147 -7.741  1.00 17.80 ?  426 ARG A N     1 
ATOM   3332 C CA    . ARG A 1 426 ? -13.971 36.318 -7.605  1.00 19.61 ?  426 ARG A CA    1 
ATOM   3333 C C     . ARG A 1 426 ? -14.714 35.338 -8.503  1.00 20.13 ?  426 ARG A C     1 
ATOM   3334 O O     . ARG A 1 426 ? -15.594 34.596 -8.050  1.00 19.97 ?  426 ARG A O     1 
ATOM   3335 C CB    . ARG A 1 426 ? -14.380 37.756 -7.936  1.00 22.44 ?  426 ARG A CB    1 
ATOM   3336 C CG    . ARG A 1 426 ? -15.885 38.030 -7.652  1.00 23.03 ?  426 ARG A CG    1 
ATOM   3337 C CD    . ARG A 1 426 ? -16.328 39.493 -7.888  1.00 24.37 ?  426 ARG A CD    1 
ATOM   3338 N NE    . ARG A 1 426 ? -15.692 40.466 -7.005  1.00 21.90 ?  426 ARG A NE    1 
ATOM   3339 C CZ    . ARG A 1 426 ? -16.030 40.675 -5.736  1.00 23.37 ?  426 ARG A CZ    1 
ATOM   3340 N NH1   . ARG A 1 426 ? -17.007 39.996 -5.159  1.00 20.69 ?  426 ARG A NH1   1 
ATOM   3341 N NH2   . ARG A 1 426 ? -15.375 41.596 -5.032  1.00 25.41 ?  426 ARG A NH2   1 
ATOM   3342 N N     . SER A 1 427 ? -14.337 35.306 -9.782  1.00 21.70 ?  427 SER A N     1 
ATOM   3343 C CA    . SER A 1 427 ? -14.933 34.384 -10.738 1.00 21.21 ?  427 SER A CA    1 
ATOM   3344 C C     . SER A 1 427 ? -14.759 32.928 -10.306 1.00 20.81 ?  427 SER A C     1 
ATOM   3345 O O     . SER A 1 427 ? -15.692 32.128 -10.421 1.00 17.97 ?  427 SER A O     1 
ATOM   3346 C CB    . SER A 1 427 ? -14.306 34.638 -12.112 1.00 25.96 ?  427 SER A CB    1 
ATOM   3347 O OG    . SER A 1 427 ? -14.687 33.659 -13.047 1.00 28.91 ?  427 SER A OG    1 
ATOM   3348 N N     . ASN A 1 428 ? -13.581 32.566 -9.784  1.00 20.20 ?  428 ASN A N     1 
ATOM   3349 C CA    . ASN A 1 428 ? -13.361 31.180 -9.362  1.00 18.95 ?  428 ASN A CA    1 
ATOM   3350 C C     . ASN A 1 428 ? -14.175 30.851 -8.112  1.00 20.82 ?  428 ASN A C     1 
ATOM   3351 O O     . ASN A 1 428 ? -14.700 29.740 -7.977  1.00 19.53 ?  428 ASN A O     1 
ATOM   3352 C CB    . ASN A 1 428 ? -11.872 30.922 -9.111  1.00 21.61 ?  428 ASN A CB    1 
ATOM   3353 C CG    . ASN A 1 428 ? -11.032 30.954 -10.395 1.00 26.41 ?  428 ASN A CG    1 
ATOM   3354 O OD1   . ASN A 1 428 ? -11.556 30.840 -11.511 1.00 24.95 ?  428 ASN A OD1   1 
ATOM   3355 N ND2   . ASN A 1 428 ? -9.721  31.098 -10.234 1.00 19.86 ?  428 ASN A ND2   1 
ATOM   3356 N N     . HIS A 1 429 ? -14.293 31.812 -7.192  1.00 18.26 ?  429 HIS A N     1 
ATOM   3357 C CA    . HIS A 1 429 ? -15.129 31.629 -6.010  1.00 20.50 ?  429 HIS A CA    1 
ATOM   3358 C C     . HIS A 1 429 ? -16.597 31.456 -6.410  1.00 17.04 ?  429 HIS A C     1 
ATOM   3359 O O     . HIS A 1 429 ? -17.286 30.567 -5.907  1.00 18.15 ?  429 HIS A O     1 
ATOM   3360 C CB    . HIS A 1 429 ? -14.915 32.825 -5.068  1.00 16.59 ?  429 HIS A CB    1 
ATOM   3361 C CG    . HIS A 1 429 ? -15.681 32.760 -3.781  1.00 18.86 ?  429 HIS A CG    1 
ATOM   3362 N ND1   . HIS A 1 429 ? -15.625 33.766 -2.837  1.00 18.45 ?  429 HIS A ND1   1 
ATOM   3363 C CD2   . HIS A 1 429 ? -16.510 31.819 -3.277  1.00 19.55 ?  429 HIS A CD2   1 
ATOM   3364 C CE1   . HIS A 1 429 ? -16.397 33.453 -1.814  1.00 21.82 ?  429 HIS A CE1   1 
ATOM   3365 N NE2   . HIS A 1 429 ? -16.943 32.274 -2.049  1.00 21.58 ?  429 HIS A NE2   1 
ATOM   3366 N N     . THR A 1 430 ? -17.073 32.259 -7.354  1.00 18.04 ?  430 THR A N     1 
ATOM   3367 C CA    . THR A 1 430 ? -18.446 32.094 -7.830  1.00 22.33 ?  430 THR A CA    1 
ATOM   3368 C C     . THR A 1 430 ? -18.682 30.701 -8.417  1.00 19.77 ?  430 THR A C     1 
ATOM   3369 O O     . THR A 1 430 ? -19.741 30.103 -8.201  1.00 19.20 ?  430 THR A O     1 
ATOM   3370 C CB    . THR A 1 430 ? -18.765 33.180 -8.855  1.00 23.59 ?  430 THR A CB    1 
ATOM   3371 O OG1   . THR A 1 430 ? -18.757 34.446 -8.190  1.00 24.70 ?  430 THR A OG1   1 
ATOM   3372 C CG2   . THR A 1 430 ? -20.143 32.944 -9.492  1.00 25.21 ?  430 THR A CG2   1 
ATOM   3373 N N     . LYS A 1 431 ? -17.709 30.169 -9.165  1.00 21.71 ?  431 LYS A N     1 
ATOM   3374 C CA    . LYS A 1 431 ? -17.861 28.830 -9.727  1.00 21.12 ?  431 LYS A CA    1 
ATOM   3375 C C     . LYS A 1 431 ? -17.965 27.786 -8.633  1.00 20.59 ?  431 LYS A C     1 
ATOM   3376 O O     . LYS A 1 431 ? -18.774 26.857 -8.732  1.00 18.47 ?  431 LYS A O     1 
ATOM   3377 C CB    . LYS A 1 431 ? -16.689 28.486 -10.638 1.00 21.77 ?  431 LYS A CB    1 
ATOM   3378 C CG    . LYS A 1 431 ? -16.774 29.093 -12.005 1.00 29.47 ?  431 LYS A CG    1 
ATOM   3379 C CD    . LYS A 1 431 ? -15.584 28.653 -12.869 1.00 28.85 ?  431 LYS A CD    1 
ATOM   3380 C CE    . LYS A 1 431 ? -15.202 29.734 -13.872 1.00 38.77 ?  431 LYS A CE    1 
ATOM   3381 N NZ    . LYS A 1 431 ? -13.732 29.706 -14.175 1.00 43.52 ?  431 LYS A NZ    1 
ATOM   3382 N N     . VAL A 1 432 ? -17.128 27.901 -7.596  1.00 19.94 ?  432 VAL A N     1 
ATOM   3383 C CA    . VAL A 1 432 ? -17.174 26.926 -6.513  1.00 18.40 ?  432 VAL A CA    1 
ATOM   3384 C C     . VAL A 1 432 ? -18.444 27.102 -5.689  1.00 16.95 ?  432 VAL A C     1 
ATOM   3385 O O     . VAL A 1 432 ? -19.076 26.123 -5.294  1.00 15.76 ?  432 VAL A O     1 
ATOM   3386 C CB    . VAL A 1 432 ? -15.916 27.028 -5.634  1.00 19.56 ?  432 VAL A CB    1 
ATOM   3387 C CG1   . VAL A 1 432 ? -16.029 26.076 -4.434  1.00 17.27 ?  432 VAL A CG1   1 
ATOM   3388 C CG2   . VAL A 1 432 ? -14.671 26.703 -6.456  1.00 19.77 ?  432 VAL A CG2   1 
ATOM   3389 N N     . ARG A 1 433 ? -18.835 28.348 -5.413  1.00 16.65 ?  433 ARG A N     1 
ATOM   3390 C CA    . ARG A 1 433 ? -20.107 28.573 -4.722  1.00 18.70 ?  433 ARG A CA    1 
ATOM   3391 C C     . ARG A 1 433 ? -21.279 27.980 -5.503  1.00 16.94 ?  433 ARG A C     1 
ATOM   3392 O O     . ARG A 1 433 ? -22.165 27.342 -4.920  1.00 17.48 ?  433 ARG A O     1 
ATOM   3393 C CB    . ARG A 1 433 ? -20.334 30.067 -4.494  1.00 15.71 ?  433 ARG A CB    1 
ATOM   3394 C CG    . ARG A 1 433 ? -21.634 30.369 -3.696  1.00 20.73 ?  433 ARG A CG    1 
ATOM   3395 C CD    . ARG A 1 433 ? -21.808 31.865 -3.376  1.00 20.53 ?  433 ARG A CD    1 
ATOM   3396 N NE    . ARG A 1 433 ? -21.837 32.705 -4.563  1.00 20.84 ?  433 ARG A NE    1 
ATOM   3397 C CZ    . ARG A 1 433 ? -20.819 33.445 -4.993  1.00 22.28 ?  433 ARG A CZ    1 
ATOM   3398 N NH1   . ARG A 1 433 ? -19.664 33.510 -4.331  1.00 21.56 ?  433 ARG A NH1   1 
ATOM   3399 N NH2   . ARG A 1 433 ? -20.955 34.132 -6.117  1.00 18.77 ?  433 ARG A NH2   1 
ATOM   3400 N N     . ASN A 1 434 ? -21.307 28.187 -6.826  1.00 18.29 ?  434 ASN A N     1 
ATOM   3401 C CA    . ASN A 1 434 ? -22.432 27.691 -7.624  1.00 20.25 ?  434 ASN A CA    1 
ATOM   3402 C C     . ASN A 1 434 ? -22.506 26.167 -7.601  1.00 22.17 ?  434 ASN A C     1 
ATOM   3403 O O     . ASN A 1 434 ? -23.610 25.591 -7.656  1.00 18.79 ?  434 ASN A O     1 
ATOM   3404 C CB    . ASN A 1 434 ? -22.330 28.218 -9.058  1.00 20.82 ?  434 ASN A CB    1 
ATOM   3405 C CG    . ASN A 1 434 ? -22.688 29.709 -9.159  1.00 27.09 ?  434 ASN A CG    1 
ATOM   3406 O OD1   . ASN A 1 434 ? -23.290 30.269 -8.250  1.00 24.23 ?  434 ASN A OD1   1 
ATOM   3407 N ND2   . ASN A 1 434 ? -22.308 30.346 -10.263 1.00 27.13 ?  434 ASN A ND2   1 
ATOM   3408 N N     . LEU A 1 435 ? -21.349 25.497 -7.480  1.00 17.49 ?  435 LEU A N     1 
ATOM   3409 C CA    . LEU A 1 435 ? -21.350 24.040 -7.366  1.00 21.84 ?  435 LEU A CA    1 
ATOM   3410 C C     . LEU A 1 435 ? -21.819 23.589 -5.984  1.00 16.11 ?  435 LEU A C     1 
ATOM   3411 O O     . LEU A 1 435 ? -22.668 22.704 -5.872  1.00 17.36 ?  435 LEU A O     1 
ATOM   3412 C CB    . LEU A 1 435 ? -19.958 23.485 -7.693  1.00 22.63 ?  435 LEU A CB    1 
ATOM   3413 C CG    . LEU A 1 435 ? -19.710 22.020 -7.330  1.00 23.55 ?  435 LEU A CG    1 
ATOM   3414 C CD1   . LEU A 1 435 ? -20.504 21.084 -8.227  1.00 20.63 ?  435 LEU A CD1   1 
ATOM   3415 C CD2   . LEU A 1 435 ? -18.208 21.715 -7.390  1.00 28.63 ?  435 LEU A CD2   1 
ATOM   3416 N N     . LEU A 1 436 ? -21.295 24.198 -4.916  1.00 16.68 ?  436 LEU A N     1 
ATOM   3417 C CA    . LEU A 1 436 ? -21.660 23.760 -3.568  1.00 16.52 ?  436 LEU A CA    1 
ATOM   3418 C C     . LEU A 1 436 ? -23.151 23.979 -3.272  1.00 16.96 ?  436 LEU A C     1 
ATOM   3419 O O     . LEU A 1 436 ? -23.756 23.206 -2.511  1.00 15.50 ?  436 LEU A O     1 
ATOM   3420 C CB    . LEU A 1 436 ? -20.802 24.495 -2.521  1.00 13.33 ?  436 LEU A CB    1 
ATOM   3421 C CG    . LEU A 1 436 ? -19.294 24.169 -2.473  1.00 17.43 ?  436 LEU A CG    1 
ATOM   3422 C CD1   . LEU A 1 436 ? -18.585 24.966 -1.382  1.00 15.39 ?  436 LEU A CD1   1 
ATOM   3423 C CD2   . LEU A 1 436 ? -19.070 22.667 -2.263  1.00 17.01 ?  436 LEU A CD2   1 
ATOM   3424 N N     . LEU A 1 437 ? -23.748 25.023 -3.849  1.00 16.99 ?  437 LEU A N     1 
ATOM   3425 C CA    . LEU A 1 437 ? -25.150 25.397 -3.640  1.00 16.62 ?  437 LEU A CA    1 
ATOM   3426 C C     . LEU A 1 437 ? -26.082 24.870 -4.740  1.00 16.88 ?  437 LEU A C     1 
ATOM   3427 O O     . LEU A 1 437 ? -27.299 25.103 -4.680  1.00 15.51 ?  437 LEU A O     1 
ATOM   3428 C CB    . LEU A 1 437 ? -25.262 26.934 -3.538  1.00 13.72 ?  437 LEU A CB    1 
ATOM   3429 C CG    . LEU A 1 437 ? -24.510 27.579 -2.358  1.00 19.96 ?  437 LEU A CG    1 
ATOM   3430 C CD1   . LEU A 1 437 ? -24.823 29.066 -2.208  1.00 18.76 ?  437 LEU A CD1   1 
ATOM   3431 C CD2   . LEU A 1 437 ? -24.845 26.849 -1.052  1.00 17.85 ?  437 LEU A CD2   1 
ATOM   3432 N N     . ARG A 1 438 ? -25.537 24.177 -5.740  1.00 19.62 ?  438 ARG A N     1 
ATOM   3433 C CA    . ARG A 1 438 ? -26.357 23.561 -6.780  1.00 20.81 ?  438 ARG A CA    1 
ATOM   3434 C C     . ARG A 1 438 ? -27.509 22.790 -6.149  1.00 20.65 ?  438 ARG A C     1 
ATOM   3435 O O     . ARG A 1 438 ? -27.321 22.049 -5.183  1.00 15.96 ?  438 ARG A O     1 
ATOM   3436 C CB    . ARG A 1 438 ? -25.514 22.613 -7.642  1.00 18.75 ?  438 ARG A CB    1 
ATOM   3437 C CG    . ARG A 1 438 ? -25.953 22.480 -9.102  1.00 28.55 ?  438 ARG A CG    1 
ATOM   3438 C CD    . ARG A 1 438 ? -25.020 21.541 -9.875  1.00 25.02 ?  438 ARG A CD    1 
ATOM   3439 N NE    . ARG A 1 438 ? -25.148 20.171 -9.389  1.00 26.49 ?  438 ARG A NE    1 
ATOM   3440 C CZ    . ARG A 1 438 ? -24.192 19.253 -9.470  1.00 27.78 ?  438 ARG A CZ    1 
ATOM   3441 N NH1   . ARG A 1 438 ? -23.016 19.521 -10.025 1.00 22.34 ?  438 ARG A NH1   1 
ATOM   3442 N NH2   . ARG A 1 438 ? -24.427 18.031 -9.002  1.00 24.04 ?  438 ARG A NH2   1 
ATOM   3443 N N     . HIS A 1 439 ? -28.701 22.953 -6.734  1.00 18.13 ?  439 HIS A N     1 
ATOM   3444 C CA    . HIS A 1 439 ? -29.927 22.421 -6.144  1.00 17.71 ?  439 HIS A CA    1 
ATOM   3445 C C     . HIS A 1 439 ? -29.840 20.926 -5.811  1.00 18.34 ?  439 HIS A C     1 
ATOM   3446 O O     . HIS A 1 439 ? -30.470 20.471 -4.851  1.00 17.15 ?  439 HIS A O     1 
ATOM   3447 C CB    . HIS A 1 439 ? -31.109 22.712 -7.092  1.00 17.86 ?  439 HIS A CB    1 
ATOM   3448 C CG    . HIS A 1 439 ? -31.165 21.811 -8.290  1.00 19.14 ?  439 HIS A CG    1 
ATOM   3449 N ND1   . HIS A 1 439 ? -30.261 21.900 -9.329  1.00 20.33 ?  439 HIS A ND1   1 
ATOM   3450 C CD2   . HIS A 1 439 ? -32.022 20.810 -8.622  1.00 20.97 ?  439 HIS A CD2   1 
ATOM   3451 C CE1   . HIS A 1 439 ? -30.543 20.978 -10.236 1.00 19.88 ?  439 HIS A CE1   1 
ATOM   3452 N NE2   . HIS A 1 439 ? -31.615 20.314 -9.841  1.00 21.25 ?  439 HIS A NE2   1 
ATOM   3453 N N     . ASP A 1 440 ? -29.060 20.141 -6.561  1.00 18.01 ?  440 ASP A N     1 
ATOM   3454 C CA    . ASP A 1 440 ? -28.992 18.708 -6.288  1.00 19.37 ?  440 ASP A CA    1 
ATOM   3455 C C     . ASP A 1 440 ? -27.638 18.224 -5.762  1.00 21.21 ?  440 ASP A C     1 
ATOM   3456 O O     . ASP A 1 440 ? -27.450 17.006 -5.633  1.00 18.99 ?  440 ASP A O     1 
ATOM   3457 C CB    . ASP A 1 440 ? -29.363 17.914 -7.540  1.00 22.95 ?  440 ASP A CB    1 
ATOM   3458 C CG    . ASP A 1 440 ? -28.432 18.206 -8.703  1.00 26.90 ?  440 ASP A CG    1 
ATOM   3459 O OD1   . ASP A 1 440 ? -27.819 19.298 -8.708  1.00 26.71 ?  440 ASP A OD1   1 
ATOM   3460 O OD2   . ASP A 1 440 ? -28.319 17.353 -9.606  1.00 31.12 -1 440 ASP A OD2   1 
ATOM   3461 N N     . LEU A 1 441 ? -26.694 19.118 -5.434  1.00 22.03 ?  441 LEU A N     1 
ATOM   3462 C CA    . LEU A 1 441 ? -25.362 18.631 -5.058  1.00 20.36 ?  441 LEU A CA    1 
ATOM   3463 C C     . LEU A 1 441 ? -25.370 17.976 -3.672  1.00 21.34 ?  441 LEU A C     1 
ATOM   3464 O O     . LEU A 1 441 ? -25.040 16.793 -3.531  1.00 22.82 ?  441 LEU A O     1 
ATOM   3465 C CB    . LEU A 1 441 ? -24.323 19.751 -5.096  1.00 20.97 ?  441 LEU A CB    1 
ATOM   3466 C CG    . LEU A 1 441 ? -23.038 19.013 -4.643  1.00 24.29 ?  441 LEU A CG    1 
ATOM   3467 C CD1   . LEU A 1 441 ? -22.070 18.723 -5.791  1.00 20.51 ?  441 LEU A CD1   1 
ATOM   3468 C CD2   . LEU A 1 441 ? -22.354 19.631 -3.443  1.00 19.71 ?  441 LEU A CD2   1 
ATOM   3469 N N     . GLU A 1 442 ? -25.730 18.729 -2.626  1.00 20.02 ?  442 GLU A N     1 
ATOM   3470 C CA    . GLU A 1 442 ? -25.698 18.150 -1.280  1.00 23.18 ?  442 GLU A CA    1 
ATOM   3471 C C     . GLU A 1 442 ? -26.700 17.004 -1.142  1.00 23.13 ?  442 GLU A C     1 
ATOM   3472 O O     . GLU A 1 442 ? -26.397 15.976 -0.517  1.00 17.58 ?  442 GLU A O     1 
ATOM   3473 C CB    . GLU A 1 442 ? -25.954 19.219 -0.203  1.00 20.38 ?  442 GLU A CB    1 
ATOM   3474 C CG    . GLU A 1 442 ? -26.033 18.617 1.221   1.00 27.32 ?  442 GLU A CG    1 
ATOM   3475 C CD    . GLU A 1 442 ? -25.867 19.628 2.357   1.00 23.55 ?  442 GLU A CD    1 
ATOM   3476 O OE1   . GLU A 1 442 ? -26.802 20.412 2.635   1.00 23.43 ?  442 GLU A OE1   1 
ATOM   3477 O OE2   . GLU A 1 442 ? -24.810 19.618 2.999   1.00 24.67 -1 442 GLU A OE2   1 
ATOM   3478 N N     . SER A 1 443 ? -27.889 17.144 -1.741  1.00 21.76 ?  443 SER A N     1 
ATOM   3479 C CA    . SER A 1 443 ? -28.892 16.088 -1.605  1.00 20.59 ?  443 SER A CA    1 
ATOM   3480 C C     . SER A 1 443 ? -28.407 14.773 -2.211  1.00 20.56 ?  443 SER A C     1 
ATOM   3481 O O     . SER A 1 443 ? -28.596 13.707 -1.618  1.00 23.14 ?  443 SER A O     1 
ATOM   3482 C CB    . SER A 1 443 ? -30.228 16.515 -2.233  1.00 21.04 ?  443 SER A CB    1 
ATOM   3483 O OG    . SER A 1 443 ? -30.061 16.877 -3.588  1.00 23.68 ?  443 SER A OG    1 
ATOM   3484 N N     . SER A 1 444 ? -27.784 14.815 -3.383  1.00 19.19 ?  444 SER A N     1 
ATOM   3485 C CA    . SER A 1 444 ? -27.326 13.556 -3.963  1.00 24.45 ?  444 SER A CA    1 
ATOM   3486 C C     . SER A 1 444 ? -26.051 13.033 -3.292  1.00 25.11 ?  444 SER A C     1 
ATOM   3487 O O     . SER A 1 444 ? -25.828 11.814 -3.281  1.00 22.66 ?  444 SER A O     1 
ATOM   3488 C CB    . SER A 1 444 ? -27.137 13.696 -5.478  1.00 26.28 ?  444 SER A CB    1 
ATOM   3489 O OG    . SER A 1 444 ? -26.029 14.509 -5.810  1.00 33.13 ?  444 SER A OG    1 
ATOM   3490 N N     . CYS A 1 445 ? -25.238 13.909 -2.687  1.00 21.42 ?  445 CYS A N     1 
ATOM   3491 C CA    . CYS A 1 445 ? -24.159 13.427 -1.824  1.00 21.43 ?  445 CYS A CA    1 
ATOM   3492 C C     . CYS A 1 445 ? -24.719 12.615 -0.664  1.00 22.58 ?  445 CYS A C     1 
ATOM   3493 O O     . CYS A 1 445 ? -24.223 11.525 -0.347  1.00 19.52 ?  445 CYS A O     1 
ATOM   3494 C CB    . CYS A 1 445 ? -23.350 14.602 -1.292  1.00 18.50 ?  445 CYS A CB    1 
ATOM   3495 S SG    . CYS A 1 445 ? -22.198 15.270 -2.487  1.00 25.20 ?  445 CYS A SG    1 
ATOM   3496 N N     . LEU A 1 446 ? -25.740 13.154 -0.002  1.00 19.67 ?  446 LEU A N     1 
ATOM   3497 C CA    . LEU A 1 446 ? -26.335 12.485 1.147   1.00 21.65 ?  446 LEU A CA    1 
ATOM   3498 C C     . LEU A 1 446 ? -27.091 11.234 0.738   1.00 24.59 ?  446 LEU A C     1 
ATOM   3499 O O     . LEU A 1 446 ? -27.166 10.286 1.524   1.00 23.61 ?  446 LEU A O     1 
ATOM   3500 C CB    . LEU A 1 446 ? -27.286 13.430 1.871   1.00 26.58 ?  446 LEU A CB    1 
ATOM   3501 C CG    . LEU A 1 446 ? -26.603 14.563 2.634   1.00 27.42 ?  446 LEU A CG    1 
ATOM   3502 C CD1   . LEU A 1 446 ? -27.622 15.658 2.953   1.00 25.01 ?  446 LEU A CD1   1 
ATOM   3503 C CD2   . LEU A 1 446 ? -25.984 13.974 3.907   1.00 20.94 ?  446 LEU A CD2   1 
ATOM   3504 N N     . ASP A 1 447 ? -27.683 11.229 -0.463  1.00 22.66 ?  447 ASP A N     1 
ATOM   3505 C CA    . ASP A 1 447 ? -28.345 10.026 -0.971  1.00 25.81 ?  447 ASP A CA    1 
ATOM   3506 C C     . ASP A 1 447 ? -27.361 8.865  -1.029  1.00 27.29 ?  447 ASP A C     1 
ATOM   3507 O O     . ASP A 1 447 ? -27.625 7.772  -0.517  1.00 26.99 ?  447 ASP A O     1 
ATOM   3508 C CB    . ASP A 1 447 ? -28.911 10.285 -2.372  1.00 27.13 ?  447 ASP A CB    1 
ATOM   3509 C CG    . ASP A 1 447 ? -30.206 11.119 -2.370  1.00 29.65 ?  447 ASP A CG    1 
ATOM   3510 O OD1   . ASP A 1 447 ? -30.829 11.305 -1.297  1.00 35.09 ?  447 ASP A OD1   1 
ATOM   3511 O OD2   . ASP A 1 447 ? -30.593 11.586 -3.475  1.00 30.76 -1 447 ASP A OD2   1 
ATOM   3512 N N     . THR A 1 448 ? -26.215 9.092  -1.667  1.00 22.09 ?  448 THR A N     1 
ATOM   3513 C CA    . THR A 1 448 ? -25.172 8.079  -1.726  1.00 26.70 ?  448 THR A CA    1 
ATOM   3514 C C     . THR A 1 448 ? -24.651 7.744  -0.327  1.00 26.12 ?  448 THR A C     1 
ATOM   3515 O O     . THR A 1 448 ? -24.469 6.569  0.020   1.00 24.07 ?  448 THR A O     1 
ATOM   3516 C CB    . THR A 1 448 ? -24.048 8.590  -2.623  1.00 27.00 ?  448 THR A CB    1 
ATOM   3517 O OG1   . THR A 1 448 ? -24.559 8.822  -3.945  1.00 29.13 ?  448 THR A OG1   1 
ATOM   3518 C CG2   . THR A 1 448 ? -22.867 7.611  -2.647  1.00 31.58 ?  448 THR A CG2   1 
ATOM   3519 N N     . PHE A 1 449 ? -24.406 8.779  0.486   1.00 23.85 ?  449 PHE A N     1 
ATOM   3520 C CA    . PHE A 1 449 ? -23.930 8.615  1.859   1.00 23.30 ?  449 PHE A CA    1 
ATOM   3521 C C     . PHE A 1 449 ? -24.801 7.638  2.641   1.00 24.17 ?  449 PHE A C     1 
ATOM   3522 O O     . PHE A 1 449 ? -24.297 6.688  3.257   1.00 24.86 ?  449 PHE A O     1 
ATOM   3523 C CB    . PHE A 1 449 ? -23.911 9.979  2.558   1.00 16.47 ?  449 PHE A CB    1 
ATOM   3524 C CG    . PHE A 1 449 ? -23.171 9.995  3.868   1.00 18.79 ?  449 PHE A CG    1 
ATOM   3525 C CD1   . PHE A 1 449 ? -21.854 9.586  3.940   1.00 22.06 ?  449 PHE A CD1   1 
ATOM   3526 C CD2   . PHE A 1 449 ? -23.783 10.463 5.022   1.00 19.71 ?  449 PHE A CD2   1 
ATOM   3527 C CE1   . PHE A 1 449 ? -21.164 9.618  5.149   1.00 20.29 ?  449 PHE A CE1   1 
ATOM   3528 C CE2   . PHE A 1 449 ? -23.108 10.496 6.216   1.00 19.19 ?  449 PHE A CE2   1 
ATOM   3529 C CZ    . PHE A 1 449 ? -21.792 10.073 6.280   1.00 17.59 ?  449 PHE A CZ    1 
ATOM   3530 N N     . CYS A 1 450 ? -26.117 7.870  2.628   1.00 22.78 ?  450 CYS A N     1 
ATOM   3531 C CA    . CYS A 1 450 ? -27.039 7.056  3.411   1.00 25.39 ?  450 CYS A CA    1 
ATOM   3532 C C     . CYS A 1 450 ? -27.149 5.636  2.854   1.00 23.72 ?  450 CYS A C     1 
ATOM   3533 O O     . CYS A 1 450 ? -27.194 4.668  3.625   1.00 25.44 ?  450 CYS A O     1 
ATOM   3534 C CB    . CYS A 1 450 ? -28.401 7.747  3.471   1.00 28.70 ?  450 CYS A CB    1 
ATOM   3535 S SG    . CYS A 1 450 ? -28.384 9.297  4.486   1.00 31.85 ?  450 CYS A SG    1 
ATOM   3536 N N     . GLU A 1 451 ? -27.185 5.488  1.525   1.00 25.07 ?  451 GLU A N     1 
ATOM   3537 C CA    . GLU A 1 451 ? -27.100 4.160  0.921   1.00 25.74 ?  451 GLU A CA    1 
ATOM   3538 C C     . GLU A 1 451 ? -25.876 3.401  1.418   1.00 28.72 ?  451 GLU A C     1 
ATOM   3539 O O     . GLU A 1 451 ? -25.966 2.217  1.762   1.00 27.56 ?  451 GLU A O     1 
ATOM   3540 C CB    . GLU A 1 451 ? -27.036 4.264  -0.599  1.00 31.58 ?  451 GLU A CB    1 
ATOM   3541 C CG    . GLU A 1 451 ? -28.342 4.542  -1.330  1.00 38.92 ?  451 GLU A CG    1 
ATOM   3542 C CD    . GLU A 1 451 ? -28.104 4.902  -2.810  1.00 45.82 ?  451 GLU A CD    1 
ATOM   3543 O OE1   . GLU A 1 451 ? -27.076 4.467  -3.386  1.00 46.33 ?  451 GLU A OE1   1 
ATOM   3544 O OE2   . GLU A 1 451 ? -28.939 5.626  -3.395  1.00 56.51 -1 451 GLU A OE2   1 
ATOM   3545 N N     . LYS A 1 452 ? -24.715 4.064  1.459   1.00 26.23 ?  452 LYS A N     1 
ATOM   3546 C CA    . LYS A 1 452 ? -23.494 3.356  1.837   1.00 28.33 ?  452 LYS A CA    1 
ATOM   3547 C C     . LYS A 1 452 ? -23.479 3.016  3.321   1.00 27.71 ?  452 LYS A C     1 
ATOM   3548 O O     . LYS A 1 452 ? -22.924 1.982  3.704   1.00 28.28 ?  452 LYS A O     1 
ATOM   3549 C CB    . LYS A 1 452 ? -22.262 4.169  1.443   1.00 22.58 ?  452 LYS A CB    1 
ATOM   3550 C CG    . LYS A 1 452 ? -22.172 4.337  -0.057  1.00 27.09 ?  452 LYS A CG    1 
ATOM   3551 C CD    . LYS A 1 452 ? -20.810 4.015  -0.632  1.00 33.06 ?  452 LYS A CD    1 
ATOM   3552 C CE    . LYS A 1 452 ? -20.941 3.545  -2.080  1.00 43.89 ?  452 LYS A CE    1 
ATOM   3553 N NZ    . LYS A 1 452 ? -19.854 4.056  -2.974  1.00 51.46 ?  452 LYS A NZ    1 
ATOM   3554 N N     . LEU A 1 453 ? -24.098 3.852  4.158   1.00 24.59 ?  453 LEU A N     1 
ATOM   3555 C CA    . LEU A 1 453 ? -24.246 3.507  5.566   1.00 24.94 ?  453 LEU A CA    1 
ATOM   3556 C C     . LEU A 1 453 ? -25.171 2.313  5.725   1.00 27.04 ?  453 LEU A C     1 
ATOM   3557 O O     . LEU A 1 453 ? -24.894 1.412  6.521   1.00 28.72 ?  453 LEU A O     1 
ATOM   3558 C CB    . LEU A 1 453 ? -24.788 4.697  6.356   1.00 19.56 ?  453 LEU A CB    1 
ATOM   3559 C CG    . LEU A 1 453 ? -23.918 5.957  6.486   1.00 28.61 ?  453 LEU A CG    1 
ATOM   3560 C CD1   . LEU A 1 453 ? -24.709 7.104  7.125   1.00 19.18 ?  453 LEU A CD1   1 
ATOM   3561 C CD2   . LEU A 1 453 ? -22.638 5.662  7.276   1.00 20.14 ?  453 LEU A CD2   1 
ATOM   3562 N N     . GLN A 1 454 ? -26.283 2.307  4.981   1.00 28.85 ?  454 GLN A N     1 
ATOM   3563 C CA    . GLN A 1 454 ? -27.194 1.169  4.972   1.00 31.55 ?  454 GLN A CA    1 
ATOM   3564 C C     . GLN A 1 454 ? -26.452 -0.127 4.656   1.00 31.86 ?  454 GLN A C     1 
ATOM   3565 O O     . GLN A 1 454 ? -26.617 -1.134 5.349   1.00 36.72 ?  454 GLN A O     1 
ATOM   3566 C CB    . GLN A 1 454 ? -28.314 1.413  3.957   1.00 31.38 ?  454 GLN A CB    1 
ATOM   3567 C CG    . GLN A 1 454 ? -29.380 2.411  4.419   1.00 28.64 ?  454 GLN A CG    1 
ATOM   3568 C CD    . GLN A 1 454 ? -30.182 1.890  5.584   1.00 34.74 ?  454 GLN A CD    1 
ATOM   3569 O OE1   . GLN A 1 454 ? -30.129 0.696  5.901   1.00 35.40 ?  454 GLN A OE1   1 
ATOM   3570 N NE2   . GLN A 1 454 ? -30.941 2.775  6.233   1.00 37.28 ?  454 GLN A NE2   1 
ATOM   3571 N N     . GLU A 1 455 ? -25.626 -0.115 3.607   1.00 31.26 ?  455 GLU A N     1 
ATOM   3572 C CA    . GLU A 1 455 ? -24.774 -1.267 3.313   1.00 30.81 ?  455 GLU A CA    1 
ATOM   3573 C C     . GLU A 1 455 ? -23.909 -1.642 4.510   1.00 39.07 ?  455 GLU A C     1 
ATOM   3574 O O     . GLU A 1 455 ? -23.668 -2.829 4.766   1.00 41.77 ?  455 GLU A O     1 
ATOM   3575 C CB    . GLU A 1 455 ? -23.868 -0.966 2.122   1.00 31.48 ?  455 GLU A CB    1 
ATOM   3576 C CG    . GLU A 1 455 ? -24.398 -1.268 0.749   1.00 43.00 ?  455 GLU A CG    1 
ATOM   3577 C CD    . GLU A 1 455 ? -23.500 -0.659 -0.311  1.00 50.97 ?  455 GLU A CD    1 
ATOM   3578 O OE1   . GLU A 1 455 ? -22.271 -0.890 -0.233  1.00 48.05 ?  455 GLU A OE1   1 
ATOM   3579 O OE2   . GLU A 1 455 ? -24.014 0.043  -1.211  1.00 49.25 -1 455 GLU A OE2   1 
ATOM   3580 N N     . LEU A 1 456 ? -23.403 -0.641 5.240   1.00 31.49 ?  456 LEU A N     1 
ATOM   3581 C CA    . LEU A 1 456 ? -22.445 -0.930 6.302   1.00 33.48 ?  456 LEU A CA    1 
ATOM   3582 C C     . LEU A 1 456 ? -23.098 -1.718 7.439   1.00 34.70 ?  456 LEU A C     1 
ATOM   3583 O O     . LEU A 1 456 ? -22.470 -2.604 8.026   1.00 35.04 ?  456 LEU A O     1 
ATOM   3584 C CB    . LEU A 1 456 ? -21.811 0.374  6.807   1.00 26.03 ?  456 LEU A CB    1 
ATOM   3585 C CG    . LEU A 1 456 ? -20.738 0.343  7.913   1.00 32.06 ?  456 LEU A CG    1 
ATOM   3586 C CD1   . LEU A 1 456 ? -19.422 -0.234 7.402   1.00 27.60 ?  456 LEU A CD1   1 
ATOM   3587 C CD2   . LEU A 1 456 ? -20.497 1.750  8.492   1.00 30.97 ?  456 LEU A CD2   1 
ATOM   3588 N N     . VAL A 1 457 ? -24.364 -1.443 7.741   1.00 33.45 ?  457 VAL A N     1 
ATOM   3589 C CA    . VAL A 1 457 ? -25.030 -2.125 8.849   1.00 38.44 ?  457 VAL A CA    1 
ATOM   3590 C C     . VAL A 1 457 ? -25.756 -3.366 8.351   1.00 41.36 ?  457 VAL A C     1 
ATOM   3591 O O     . VAL A 1 457 ? -26.506 -4.005 9.098   1.00 42.48 ?  457 VAL A O     1 
ATOM   3592 C CB    . VAL A 1 457 ? -25.998 -1.183 9.588   1.00 36.19 ?  457 VAL A CB    1 
ATOM   3593 C CG1   . VAL A 1 457 ? -25.232 -0.025 10.151  1.00 28.81 ?  457 VAL A CG1   1 
ATOM   3594 C CG2   . VAL A 1 457 ? -27.077 -0.694 8.655   1.00 35.07 ?  457 VAL A CG2   1 
ATOM   3595 N N     . SER A 1 458 ? -25.534 -3.718 7.093   1.00 43.02 ?  458 SER A N     1 
ATOM   3596 C CA    . SER A 1 458 ? -26.111 -4.923 6.518   1.00 45.93 ?  458 SER A CA    1 
ATOM   3597 C C     . SER A 1 458 ? -25.057 -6.017 6.368   1.00 48.60 ?  458 SER A C     1 
ATOM   3598 O O     . SER A 1 458 ? -25.341 -7.101 5.855   1.00 54.93 ?  458 SER A O     1 
ATOM   3599 C CB    . SER A 1 458 ? -26.742 -4.611 5.166   1.00 44.06 ?  458 SER A CB    1 
ATOM   3600 O OG    . SER A 1 458 ? -27.999 -3.977 5.349   1.00 55.53 ?  458 SER A OG    1 
HETATM 3601 N N1    . U5P B 2 .   ? -16.774 30.420 15.173  1.00 27.52 ?  501 U5P A N1    1 
HETATM 3602 C C2    . U5P B 2 .   ? -17.826 31.223 15.580  1.00 24.20 ?  501 U5P A C2    1 
HETATM 3603 N N3    . U5P B 2 .   ? -17.461 32.340 16.283  1.00 20.40 ?  501 U5P A N3    1 
HETATM 3604 C C4    . U5P B 2 .   ? -16.183 32.702 16.663  1.00 25.23 ?  501 U5P A C4    1 
HETATM 3605 C C5    . U5P B 2 .   ? -15.146 31.807 16.231  1.00 23.44 ?  501 U5P A C5    1 
HETATM 3606 C C6    . U5P B 2 .   ? -15.472 30.716 15.517  1.00 23.89 ?  501 U5P A C6    1 
HETATM 3607 O O2    . U5P B 2 .   ? -18.992 30.985 15.298  1.00 23.63 ?  501 U5P A O2    1 
HETATM 3608 O O4    . U5P B 2 .   ? -16.027 33.739 17.306  1.00 24.34 ?  501 U5P A O4    1 
HETATM 3609 C "C1'" . U5P B 2 .   ? -17.119 29.188 14.432  1.00 26.36 ?  501 U5P A "C1'" 1 
HETATM 3610 C "C2'" . U5P B 2 .   ? -16.832 29.226 12.930  1.00 28.32 ?  501 U5P A "C2'" 1 
HETATM 3611 O "O2'" . U5P B 2 .   ? -17.911 29.799 12.221  1.00 21.79 ?  501 U5P A "O2'" 1 
HETATM 3612 C "C3'" . U5P B 2 .   ? -16.683 27.727 12.633  1.00 29.03 ?  501 U5P A "C3'" 1 
HETATM 3613 C "C4'" . U5P B 2 .   ? -15.973 27.216 13.898  1.00 25.47 ?  501 U5P A "C4'" 1 
HETATM 3614 O "O3'" . U5P B 2 .   ? -17.952 27.104 12.476  1.00 28.11 ?  501 U5P A "O3'" 1 
HETATM 3615 O "O4'" . U5P B 2 .   ? -16.344 28.134 14.956  1.00 26.96 ?  501 U5P A "O4'" 1 
HETATM 3616 C "C5'" . U5P B 2 .   ? -14.471 27.179 13.808  1.00 31.70 ?  501 U5P A "C5'" 1 
HETATM 3617 O "O5'" . U5P B 2 .   ? -14.141 26.084 12.943  1.00 27.02 ?  501 U5P A "O5'" 1 
HETATM 3618 P P     . U5P B 2 .   ? -12.790 26.133 12.091  1.00 25.48 ?  501 U5P A P     1 
HETATM 3619 O O1P   . U5P B 2 .   ? -11.633 26.329 13.067  1.00 29.08 -1 501 U5P A O1P   1 
HETATM 3620 O O2P   . U5P B 2 .   ? -12.925 27.282 11.122  1.00 20.51 ?  501 U5P A O2P   1 
HETATM 3621 O O3P   . U5P B 2 .   ? -12.792 24.759 11.415  1.00 16.81 -1 501 U5P A O3P   1 
HETATM 3622 O O1    . RUT C 3 .   ? -5.729  15.445 12.028  1.00 18.04 ?  502 RUT A O1    1 
HETATM 3623 C C1    . RUT C 3 .   ? -6.773  16.080 12.658  1.00 17.97 ?  502 RUT A C1    1 
HETATM 3624 C C2    . RUT C 3 .   ? -6.765  17.477 12.821  1.00 17.26 ?  502 RUT A C2    1 
HETATM 3625 O O2    . RUT C 3 .   ? -7.812  18.104 13.486  1.00 19.63 ?  502 RUT A O2    1 
HETATM 3626 C C3    . RUT C 3 .   ? -5.676  18.212 12.334  1.00 18.15 ?  502 RUT A C3    1 
HETATM 3627 O O3    . RUT C 3 .   ? -5.645  19.467 12.433  1.00 17.52 ?  502 RUT A O3    1 
HETATM 3628 C C4    . RUT C 3 .   ? -3.417  18.162 11.183  1.00 18.90 ?  502 RUT A C4    1 
HETATM 3629 O O4    . RUT C 3 .   ? -3.301  19.507 11.283  1.00 15.92 ?  502 RUT A O4    1 
HETATM 3630 C C5    . RUT C 3 .   ? -2.409  17.435 10.591  1.00 17.70 ?  502 RUT A C5    1 
HETATM 3631 C C6    . RUT C 3 .   ? -2.526  16.038 10.502  1.00 22.26 ?  502 RUT A C6    1 
HETATM 3632 O O5    . RUT C 3 .   ? -1.530  15.338 9.920   1.00 20.37 ?  502 RUT A O5    1 
HETATM 3633 C C7    . RUT C 3 .   ? -3.648  15.363 10.973  1.00 18.49 ?  502 RUT A C7    1 
HETATM 3634 C C8    . RUT C 3 .   ? -4.641  16.124 11.560  1.00 21.15 ?  502 RUT A C8    1 
HETATM 3635 C C9    . RUT C 3 .   ? -4.572  17.514 11.687  1.00 19.76 ?  502 RUT A C9    1 
HETATM 3636 C C10   . RUT C 3 .   ? -7.820  15.143 13.085  1.00 18.49 ?  502 RUT A C10   1 
HETATM 3637 C C11   . RUT C 3 .   ? -7.478  13.802 13.314  1.00 17.52 ?  502 RUT A C11   1 
HETATM 3638 C C12   . RUT C 3 .   ? -8.426  12.877 13.704  1.00 22.40 ?  502 RUT A C12   1 
HETATM 3639 O O6    . RUT C 3 .   ? -8.092  11.573 13.956  1.00 19.54 ?  502 RUT A O6    1 
HETATM 3640 C C13   . RUT C 3 .   ? -9.755  13.277 13.856  1.00 19.51 ?  502 RUT A C13   1 
HETATM 3641 O O7    . RUT C 3 .   ? -10.644 12.325 14.239  1.00 19.86 ?  502 RUT A O7    1 
HETATM 3642 C C14   . RUT C 3 .   ? -10.115 14.593 13.630  1.00 15.87 ?  502 RUT A C14   1 
HETATM 3643 C C15   . RUT C 3 .   ? -9.159  15.520 13.232  1.00 18.01 ?  502 RUT A C15   1 
HETATM 3644 C C16   . RUT C 3 .   ? -7.460  19.108 14.441  1.00 18.35 ?  502 RUT A C16   1 
HETATM 3645 C C17   . RUT C 3 .   ? -8.659  19.506 15.297  1.00 17.12 ?  502 RUT A C17   1 
HETATM 3646 O O8    . RUT C 3 .   ? -9.647  20.129 14.481  1.00 17.84 ?  502 RUT A O8    1 
HETATM 3647 C C18   . RUT C 3 .   ? -8.211  20.515 16.359  1.00 18.31 ?  502 RUT A C18   1 
HETATM 3648 O O9    . RUT C 3 .   ? -9.280  20.819 17.248  1.00 19.40 ?  502 RUT A O9    1 
HETATM 3649 C C19   . RUT C 3 .   ? -6.990  20.038 17.135  1.00 19.22 ?  502 RUT A C19   1 
HETATM 3650 O O10   . RUT C 3 .   ? -6.550  21.077 18.002  1.00 20.32 ?  502 RUT A O10   1 
HETATM 3651 C C20   . RUT C 3 .   ? -5.893  19.682 16.134  1.00 20.01 ?  502 RUT A C20   1 
HETATM 3652 C C21   . RUT C 3 .   ? -4.595  19.197 16.740  1.00 21.17 ?  502 RUT A C21   1 
HETATM 3653 O O11   . RUT C 3 .   ? -6.385  18.652 15.241  1.00 19.60 ?  502 RUT A O11   1 
HETATM 3654 C C22   . RUT C 3 .   ? -2.347  18.716 16.013  1.00 21.87 ?  502 RUT A C22   1 
HETATM 3655 O O12   . RUT C 3 .   ? -3.634  19.152 15.674  1.00 22.64 ?  502 RUT A O12   1 
HETATM 3656 C C23   . RUT C 3 .   ? -1.500  18.740 14.741  1.00 24.66 ?  502 RUT A C23   1 
HETATM 3657 O O13   . RUT C 3 .   ? -0.224  18.141 14.962  1.00 26.55 ?  502 RUT A O13   1 
HETATM 3658 C C24   . RUT C 3 .   ? -1.312  20.178 14.267  1.00 25.68 ?  502 RUT A C24   1 
HETATM 3659 O O14   . RUT C 3 .   ? -0.498  20.238 13.092  1.00 26.45 ?  502 RUT A O14   1 
HETATM 3660 C C25   . RUT C 3 .   ? -0.710  21.015 15.376  1.00 24.14 ?  502 RUT A C25   1 
HETATM 3661 O O15   . RUT C 3 .   ? -0.623  22.374 14.946  1.00 27.60 ?  502 RUT A O15   1 
HETATM 3662 C C26   . RUT C 3 .   ? -1.593  20.924 16.616  1.00 26.13 ?  502 RUT A C26   1 
HETATM 3663 C C27   . RUT C 3 .   ? -1.013  21.641 17.811  1.00 26.50 ?  502 RUT A C27   1 
HETATM 3664 O O16   . RUT C 3 .   ? -1.783  19.544 17.008  1.00 23.11 ?  502 RUT A O16   1 
HETATM 3665 O O     . HOH D 4 .   ? 12.802  3.602  3.841   1.00 48.84 ?  601 HOH A O     1 
HETATM 3666 O O     . HOH D 4 .   ? 11.419  11.397 11.991  1.00 47.96 ?  602 HOH A O     1 
HETATM 3667 O O     . HOH D 4 .   ? -28.259 35.922 7.616   1.00 34.03 ?  603 HOH A O     1 
HETATM 3668 O O     . HOH D 4 .   ? -1.651  4.840  -3.652  1.00 51.25 ?  604 HOH A O     1 
HETATM 3669 O O     . HOH D 4 .   ? -34.360 15.884 22.183  1.00 37.80 ?  605 HOH A O     1 
HETATM 3670 O O     . HOH D 4 .   ? -0.189  48.785 25.971  1.00 33.75 ?  606 HOH A O     1 
HETATM 3671 O O     . HOH D 4 .   ? -6.793  19.426 -4.646  1.00 19.96 ?  607 HOH A O     1 
HETATM 3672 O O     . HOH D 4 .   ? -1.838  29.472 -1.380  1.00 26.42 ?  608 HOH A O     1 
HETATM 3673 O O     . HOH D 4 .   ? -24.854 31.181 0.819   1.00 33.08 ?  609 HOH A O     1 
HETATM 3674 O O     . HOH D 4 .   ? -29.491 -1.634 5.926   1.00 38.21 ?  610 HOH A O     1 
HETATM 3675 O O     . HOH D 4 .   ? -27.584 26.933 22.546  1.00 33.60 ?  611 HOH A O     1 
HETATM 3676 O O     . HOH D 4 .   ? -27.245 18.944 35.926  1.00 33.60 ?  612 HOH A O     1 
HETATM 3677 O O     . HOH D 4 .   ? -9.131  18.761 36.028  1.00 40.20 ?  613 HOH A O     1 
HETATM 3678 O O     . HOH D 4 .   ? -31.305 25.170 8.045   1.00 34.01 ?  614 HOH A O     1 
HETATM 3679 O O     . HOH D 4 .   ? -18.723 36.378 -9.765  1.00 29.02 ?  615 HOH A O     1 
HETATM 3680 O O     . HOH D 4 .   ? -16.404 44.541 -2.225  1.00 33.96 ?  616 HOH A O     1 
HETATM 3681 O O     . HOH D 4 .   ? -13.446 18.104 3.655   1.00 27.84 ?  617 HOH A O     1 
HETATM 3682 O O     . HOH D 4 .   ? -0.449  32.679 7.198   1.00 25.98 ?  618 HOH A O     1 
HETATM 3683 O O     . HOH D 4 .   ? -22.524 7.049  30.214  1.00 40.21 ?  619 HOH A O     1 
HETATM 3684 O O     . HOH D 4 .   ? -26.729 23.266 12.571  1.00 28.80 ?  620 HOH A O     1 
HETATM 3685 O O     . HOH D 4 .   ? -16.284 -1.611 15.135  1.00 35.13 ?  621 HOH A O     1 
HETATM 3686 O O     . HOH D 4 .   ? 7.266   4.175  3.391   1.00 37.00 ?  622 HOH A O     1 
HETATM 3687 O O     . HOH D 4 .   ? -20.925 17.800 -10.740 1.00 33.48 ?  623 HOH A O     1 
HETATM 3688 O O     . HOH D 4 .   ? -13.962 15.108 12.504  1.00 18.38 ?  624 HOH A O     1 
HETATM 3689 O O     . HOH D 4 .   ? -9.562  24.926 14.241  1.00 33.71 ?  625 HOH A O     1 
HETATM 3690 O O     . HOH D 4 .   ? -8.181  30.811 -12.642 1.00 33.01 ?  626 HOH A O     1 
HETATM 3691 O O     . HOH D 4 .   ? -12.539 31.941 -13.753 1.00 34.54 ?  627 HOH A O     1 
HETATM 3692 O O     . HOH D 4 .   ? 4.299   18.880 -1.289  1.00 30.64 ?  628 HOH A O     1 
HETATM 3693 O O     . HOH D 4 .   ? 9.513   32.479 13.383  1.00 22.07 ?  629 HOH A O     1 
HETATM 3694 O O     . HOH D 4 .   ? 9.341   2.781  4.864   1.00 39.64 ?  630 HOH A O     1 
HETATM 3695 O O     . HOH D 4 .   ? -12.000 19.236 2.520   1.00 29.39 ?  631 HOH A O     1 
HETATM 3696 O O     . HOH D 4 .   ? -15.559 23.196 2.171   1.00 26.88 ?  632 HOH A O     1 
HETATM 3697 O O     . HOH D 4 .   ? -5.441  55.496 9.868   1.00 41.21 ?  633 HOH A O     1 
HETATM 3698 O O     . HOH D 4 .   ? -19.389 -7.234 15.538  1.00 43.48 ?  634 HOH A O     1 
HETATM 3699 O O     . HOH D 4 .   ? -5.968  20.725 20.506  1.00 24.64 ?  635 HOH A O     1 
HETATM 3700 O O     . HOH D 4 .   ? -31.265 8.819  21.504  1.00 35.37 ?  636 HOH A O     1 
HETATM 3701 O O     . HOH D 4 .   ? 1.124   17.348 12.889  1.00 30.03 ?  637 HOH A O     1 
HETATM 3702 O O     . HOH D 4 .   ? -1.344  12.947 11.336  1.00 24.93 ?  638 HOH A O     1 
HETATM 3703 O O     . HOH D 4 .   ? -2.101  -0.136 11.039  1.00 34.98 ?  639 HOH A O     1 
HETATM 3704 O O     . HOH D 4 .   ? -19.861 37.545 2.463   1.00 27.89 ?  640 HOH A O     1 
HETATM 3705 O O     . HOH D 4 .   ? -27.931 48.919 6.280   1.00 40.30 ?  641 HOH A O     1 
HETATM 3706 O O     . HOH D 4 .   ? -25.939 26.636 -8.225  1.00 17.36 ?  642 HOH A O     1 
HETATM 3707 O O     . HOH D 4 .   ? -27.927 26.887 -6.504  1.00 17.54 ?  643 HOH A O     1 
HETATM 3708 O O     . HOH D 4 .   ? -21.753 10.682 -0.837  1.00 20.74 ?  644 HOH A O     1 
HETATM 3709 O O     . HOH D 4 .   ? -4.880  32.338 -6.026  1.00 28.40 ?  645 HOH A O     1 
HETATM 3710 O O     . HOH D 4 .   ? -13.095 24.977 20.335  1.00 31.06 ?  646 HOH A O     1 
HETATM 3711 O O     . HOH D 4 .   ? 0.206   32.641 4.457   1.00 24.41 ?  647 HOH A O     1 
HETATM 3712 O O     . HOH D 4 .   ? -7.153  25.314 22.200  1.00 34.28 ?  648 HOH A O     1 
HETATM 3713 O O     . HOH D 4 .   ? -6.828  9.545  -6.422  1.00 27.60 ?  649 HOH A O     1 
HETATM 3714 O O     . HOH D 4 .   ? -15.132 22.988 11.369  1.00 15.86 ?  650 HOH A O     1 
HETATM 3715 O O     . HOH D 4 .   ? -14.657 38.619 -11.629 1.00 35.22 ?  651 HOH A O     1 
HETATM 3716 O O     . HOH D 4 .   ? -4.632  12.853 35.987  1.00 44.35 ?  652 HOH A O     1 
HETATM 3717 O O     . HOH D 4 .   ? -11.505 32.168 9.816   1.00 18.39 ?  653 HOH A O     1 
HETATM 3718 O O     . HOH D 4 .   ? 15.316  25.945 3.023   1.00 42.29 ?  654 HOH A O     1 
HETATM 3719 O O     . HOH D 4 .   ? -30.302 37.104 12.135  1.00 28.90 ?  655 HOH A O     1 
HETATM 3720 O O     . HOH D 4 .   ? 1.698   24.858 -3.942  1.00 31.36 ?  656 HOH A O     1 
HETATM 3721 O O     . HOH D 4 .   ? -13.783 41.607 -8.488  1.00 30.69 ?  657 HOH A O     1 
HETATM 3722 O O     . HOH D 4 .   ? -23.817 48.576 17.651  1.00 36.10 ?  658 HOH A O     1 
HETATM 3723 O O     . HOH D 4 .   ? 5.142   38.987 4.533   1.00 21.98 ?  659 HOH A O     1 
HETATM 3724 O O     . HOH D 4 .   ? -19.576 22.895 7.412   1.00 18.86 ?  660 HOH A O     1 
HETATM 3725 O O     . HOH D 4 .   ? -31.166 15.914 4.474   1.00 28.12 ?  661 HOH A O     1 
HETATM 3726 O O     . HOH D 4 .   ? -2.706  12.069 -9.803  1.00 36.41 ?  662 HOH A O     1 
HETATM 3727 O O     . HOH D 4 .   ? 12.460  36.045 11.580  1.00 26.16 ?  663 HOH A O     1 
HETATM 3728 O O     . HOH D 4 .   ? -8.688  50.587 7.656   1.00 27.63 ?  664 HOH A O     1 
HETATM 3729 O O     . HOH D 4 .   ? 0.857   15.585 11.128  1.00 24.06 ?  665 HOH A O     1 
HETATM 3730 O O     . HOH D 4 .   ? -28.207 30.971 11.410  1.00 33.19 ?  666 HOH A O     1 
HETATM 3731 O O     . HOH D 4 .   ? 3.812   30.647 10.546  1.00 29.18 ?  667 HOH A O     1 
HETATM 3732 O O     . HOH D 4 .   ? -31.383 9.034  1.912   1.00 32.58 ?  668 HOH A O     1 
HETATM 3733 O O     . HOH D 4 .   ? -5.564  7.415  29.622  1.00 30.80 ?  669 HOH A O     1 
HETATM 3734 O O     . HOH D 4 .   ? -11.622 42.588 -7.590  1.00 36.25 ?  670 HOH A O     1 
HETATM 3735 O O     . HOH D 4 .   ? -30.077 32.314 12.772  1.00 33.22 ?  671 HOH A O     1 
HETATM 3736 O O     . HOH D 4 .   ? 2.139   16.129 24.778  1.00 33.30 ?  672 HOH A O     1 
HETATM 3737 O O     . HOH D 4 .   ? -17.682 17.716 32.120  1.00 35.40 ?  673 HOH A O     1 
HETATM 3738 O O     . HOH D 4 .   ? -9.246  52.868 1.220   1.00 33.18 ?  674 HOH A O     1 
HETATM 3739 O O     . HOH D 4 .   ? -38.198 15.598 7.972   1.00 39.90 ?  675 HOH A O     1 
HETATM 3740 O O     . HOH D 4 .   ? -16.169 19.636 33.492  1.00 33.60 ?  676 HOH A O     1 
HETATM 3741 O O     . HOH D 4 .   ? 0.340   11.924 26.996  1.00 40.49 ?  677 HOH A O     1 
HETATM 3742 O O     . HOH D 4 .   ? -16.030 42.115 -2.343  1.00 26.39 ?  678 HOH A O     1 
HETATM 3743 O O     . HOH D 4 .   ? -21.345 40.109 1.640   1.00 32.73 ?  679 HOH A O     1 
HETATM 3744 O O     . HOH D 4 .   ? -1.946  30.160 20.612  1.00 37.18 ?  680 HOH A O     1 
HETATM 3745 O O     . HOH D 4 .   ? 6.521   45.906 8.361   1.00 31.06 ?  681 HOH A O     1 
HETATM 3746 O O     . HOH D 4 .   ? -32.324 21.856 -3.407  1.00 19.99 ?  682 HOH A O     1 
HETATM 3747 O O     . HOH D 4 .   ? -1.988  13.782 29.365  1.00 39.52 ?  683 HOH A O     1 
HETATM 3748 O O     . HOH D 4 .   ? 2.743   50.290 19.137  1.00 39.08 ?  684 HOH A O     1 
HETATM 3749 O O     . HOH D 4 .   ? 3.047   15.441 9.760   1.00 18.24 ?  685 HOH A O     1 
HETATM 3750 O O     . HOH D 4 .   ? -18.402 14.778 22.204  1.00 22.72 ?  686 HOH A O     1 
HETATM 3751 O O     . HOH D 4 .   ? -28.872 25.973 -2.618  1.00 20.21 ?  687 HOH A O     1 
HETATM 3752 O O     . HOH D 4 .   ? -32.687 13.181 -2.033  1.00 32.96 ?  688 HOH A O     1 
HETATM 3753 O O     . HOH D 4 .   ? -32.694 10.681 19.594  1.00 27.69 ?  689 HOH A O     1 
HETATM 3754 O O     . HOH D 4 .   ? 2.784   34.474 11.181  1.00 18.97 ?  690 HOH A O     1 
HETATM 3755 O O     . HOH D 4 .   ? 2.316   40.051 -2.471  1.00 45.55 ?  691 HOH A O     1 
HETATM 3756 O O     . HOH D 4 .   ? -13.265 5.441  31.386  1.00 34.55 ?  692 HOH A O     1 
HETATM 3757 O O     . HOH D 4 .   ? -21.015 29.085 -12.345 1.00 36.07 ?  693 HOH A O     1 
HETATM 3758 O O     . HOH D 4 .   ? 3.501   37.920 22.130  1.00 33.54 ?  694 HOH A O     1 
HETATM 3759 O O     . HOH D 4 .   ? -9.319  22.731 10.009  1.00 15.42 ?  695 HOH A O     1 
HETATM 3760 O O     . HOH D 4 .   ? -20.512 14.901 -5.597  1.00 36.27 ?  696 HOH A O     1 
HETATM 3761 O O     . HOH D 4 .   ? -26.152 21.848 -2.681  1.00 16.54 ?  697 HOH A O     1 
HETATM 3762 O O     . HOH D 4 .   ? -13.359 18.992 33.004  1.00 33.64 ?  698 HOH A O     1 
HETATM 3763 O O     . HOH D 4 .   ? -11.749 22.517 12.644  1.00 21.62 ?  699 HOH A O     1 
HETATM 3764 O O     . HOH D 4 .   ? -16.426 20.139 -0.582  1.00 32.90 ?  700 HOH A O     1 
HETATM 3765 O O     . HOH D 4 .   ? -12.799 35.104 -3.276  1.00 19.97 ?  701 HOH A O     1 
HETATM 3766 O O     . HOH D 4 .   ? -21.751 27.166 10.725  1.00 29.56 ?  702 HOH A O     1 
HETATM 3767 O O     . HOH D 4 .   ? 0.637   52.373 15.774  1.00 31.79 ?  703 HOH A O     1 
HETATM 3768 O O     . HOH D 4 .   ? 1.066   33.892 13.200  1.00 26.85 ?  704 HOH A O     1 
HETATM 3769 O O     . HOH D 4 .   ? -4.520  36.530 18.549  1.00 24.17 ?  705 HOH A O     1 
HETATM 3770 O O     . HOH D 4 .   ? -23.369 17.250 3.637   1.00 23.54 ?  706 HOH A O     1 
HETATM 3771 O O     . HOH D 4 .   ? -37.768 13.938 10.335  1.00 37.06 ?  707 HOH A O     1 
HETATM 3772 O O     . HOH D 4 .   ? 3.558   9.917  15.092  1.00 30.75 ?  708 HOH A O     1 
HETATM 3773 O O     . HOH D 4 .   ? -13.582 -6.663 19.983  1.00 40.39 ?  709 HOH A O     1 
HETATM 3774 O O     . HOH D 4 .   ? -22.726 36.432 0.889   1.00 33.23 ?  710 HOH A O     1 
HETATM 3775 O O     . HOH D 4 .   ? 1.131   28.985 9.128   1.00 23.31 ?  711 HOH A O     1 
HETATM 3776 O O     . HOH D 4 .   ? -30.629 14.666 -5.210  1.00 32.63 ?  712 HOH A O     1 
HETATM 3777 O O     . HOH D 4 .   ? 16.856  27.130 7.449   1.00 32.72 ?  713 HOH A O     1 
HETATM 3778 O O     . HOH D 4 .   ? -10.022 -0.637 18.902  1.00 30.76 ?  714 HOH A O     1 
HETATM 3779 O O     . HOH D 4 .   ? -15.867 36.567 -3.996  1.00 20.36 ?  715 HOH A O     1 
HETATM 3780 O O     . HOH D 4 .   ? -12.736 44.889 22.244  1.00 40.98 ?  716 HOH A O     1 
HETATM 3781 O O     . HOH D 4 .   ? -27.850 45.005 9.578   1.00 31.82 ?  717 HOH A O     1 
HETATM 3782 O O     . HOH D 4 .   ? -12.513 24.506 17.036  1.00 26.30 ?  718 HOH A O     1 
HETATM 3783 O O     . HOH D 4 .   ? 6.618   42.892 2.711   1.00 24.95 ?  719 HOH A O     1 
HETATM 3784 O O     . HOH D 4 .   ? -15.701 7.862  32.016  1.00 41.29 ?  720 HOH A O     1 
HETATM 3785 O O     . HOH D 4 .   ? 6.237   7.981  0.075   1.00 37.51 ?  721 HOH A O     1 
HETATM 3786 O O     . HOH D 4 .   ? -1.527  51.244 9.509   1.00 24.37 ?  722 HOH A O     1 
HETATM 3787 O O     . HOH D 4 .   ? -21.662 51.645 11.843  1.00 33.68 ?  723 HOH A O     1 
HETATM 3788 O O     . HOH D 4 .   ? 7.342   45.257 3.818   1.00 33.96 ?  724 HOH A O     1 
HETATM 3789 O O     . HOH D 4 .   ? -29.040 19.668 -2.526  1.00 21.48 ?  725 HOH A O     1 
HETATM 3790 O O     . HOH D 4 .   ? -9.917  18.950 -0.781  1.00 23.97 ?  726 HOH A O     1 
HETATM 3791 O O     . HOH D 4 .   ? -30.266 6.941  0.151   1.00 28.73 ?  727 HOH A O     1 
HETATM 3792 O O     . HOH D 4 .   ? -29.214 10.931 -5.880  1.00 37.24 ?  728 HOH A O     1 
HETATM 3793 O O     . HOH D 4 .   ? -25.531 33.104 2.718   1.00 39.31 ?  729 HOH A O     1 
HETATM 3794 O O     . HOH D 4 .   ? -19.586 17.584 34.223  1.00 35.81 ?  730 HOH A O     1 
HETATM 3795 O O     . HOH D 4 .   ? -26.248 1.070  30.033  1.00 42.88 ?  731 HOH A O     1 
HETATM 3796 O O     . HOH D 4 .   ? -6.734  35.135 17.839  1.00 28.93 ?  732 HOH A O     1 
HETATM 3797 O O     . HOH D 4 .   ? -22.252 21.549 -11.890 1.00 26.33 ?  733 HOH A O     1 
HETATM 3798 O O     . HOH D 4 .   ? -5.323  24.305 15.943  1.00 32.02 ?  734 HOH A O     1 
HETATM 3799 O O     . HOH D 4 .   ? 11.178  3.672  14.321  1.00 46.32 ?  735 HOH A O     1 
HETATM 3800 O O     . HOH D 4 .   ? -15.316 21.548 8.933   1.00 16.54 ?  736 HOH A O     1 
HETATM 3801 O O     . HOH D 4 .   ? -11.755 27.586 15.884  1.00 35.08 ?  737 HOH A O     1 
HETATM 3802 O O     . HOH D 4 .   ? -24.373 46.824 4.523   1.00 30.83 ?  738 HOH A O     1 
HETATM 3803 O O     . HOH D 4 .   ? -22.706 37.681 17.246  1.00 25.55 ?  739 HOH A O     1 
HETATM 3804 O O     . HOH D 4 .   ? 8.863   13.227 12.443  1.00 38.62 ?  740 HOH A O     1 
HETATM 3805 O O     . HOH D 4 .   ? -3.057  20.630 20.693  1.00 27.63 ?  741 HOH A O     1 
HETATM 3806 O O     . HOH D 4 .   ? -12.941 31.858 12.594  1.00 24.23 ?  742 HOH A O     1 
HETATM 3807 O O     . HOH D 4 .   ? -22.755 15.638 -8.040  1.00 38.99 ?  743 HOH A O     1 
HETATM 3808 O O     . HOH D 4 .   ? 7.410   21.617 -0.616  1.00 31.59 ?  744 HOH A O     1 
HETATM 3809 O O     . HOH D 4 .   ? 0.508   1.251  1.038   1.00 31.88 ?  745 HOH A O     1 
HETATM 3810 O O     . HOH D 4 .   ? -17.676 24.458 11.340  1.00 19.38 ?  746 HOH A O     1 
HETATM 3811 O O     . HOH D 4 .   ? -20.007 40.474 -0.497  1.00 31.94 ?  747 HOH A O     1 
HETATM 3812 O O     . HOH D 4 .   ? 4.546   9.353  12.331  1.00 34.83 ?  748 HOH A O     1 
HETATM 3813 O O     . HOH D 4 .   ? -9.107  34.605 16.124  1.00 30.74 ?  749 HOH A O     1 
HETATM 3814 O O     . HOH D 4 .   ? 0.768   39.191 0.429   1.00 22.09 ?  750 HOH A O     1 
HETATM 3815 O O     . HOH D 4 .   ? -2.244  33.426 -3.533  1.00 28.26 ?  751 HOH A O     1 
HETATM 3816 O O     . HOH D 4 .   ? 5.260   14.410 23.553  1.00 29.08 ?  752 HOH A O     1 
HETATM 3817 O O     . HOH D 4 .   ? -9.362  22.665 13.083  1.00 28.35 ?  753 HOH A O     1 
HETATM 3818 O O     . HOH D 4 .   ? -36.014 4.382  5.400   1.00 53.90 ?  754 HOH A O     1 
HETATM 3819 O O     . HOH D 4 .   ? -5.747  5.662  24.760  1.00 33.09 ?  755 HOH A O     1 
HETATM 3820 O O     . HOH D 4 .   ? -26.927 38.091 8.542   1.00 27.29 ?  756 HOH A O     1 
HETATM 3821 O O     . HOH D 4 .   ? -0.941  37.188 30.544  1.00 46.13 ?  757 HOH A O     1 
HETATM 3822 O O     . HOH D 4 .   ? 7.473   10.651 12.455  1.00 38.11 ?  758 HOH A O     1 
HETATM 3823 O O     . HOH D 4 .   ? -11.869 48.305 18.589  1.00 25.71 ?  759 HOH A O     1 
HETATM 3824 O O     . HOH D 4 .   ? -19.774 25.328 -11.023 1.00 22.79 ?  760 HOH A O     1 
HETATM 3825 O O     . HOH D 4 .   ? -20.016 13.558 -3.557  1.00 32.22 ?  761 HOH A O     1 
HETATM 3826 O O     . HOH D 4 .   ? -33.668 27.449 11.924  1.00 37.94 ?  762 HOH A O     1 
HETATM 3827 O O     . HOH D 4 .   ? 0.725   17.649 17.721  1.00 25.95 ?  763 HOH A O     1 
HETATM 3828 O O     . HOH D 4 .   ? -31.705 16.526 23.754  1.00 34.42 ?  764 HOH A O     1 
HETATM 3829 O O     . HOH D 4 .   ? -12.547 42.319 23.408  1.00 28.98 ?  765 HOH A O     1 
HETATM 3830 O O     . HOH D 4 .   ? -3.131  23.847 15.522  1.00 26.27 ?  766 HOH A O     1 
HETATM 3831 O O     . HOH D 4 .   ? -13.870 18.519 -10.493 1.00 36.19 ?  767 HOH A O     1 
HETATM 3832 O O     . HOH D 4 .   ? 7.419   10.719 0.140   1.00 33.41 ?  768 HOH A O     1 
HETATM 3833 O O     . HOH D 4 .   ? -9.750  -4.944 1.728   1.00 37.76 ?  769 HOH A O     1 
HETATM 3834 O O     . HOH D 4 .   ? -17.622 35.340 -5.538  1.00 20.79 ?  770 HOH A O     1 
HETATM 3835 O O     . HOH D 4 .   ? -18.416 1.118  31.875  1.00 43.18 ?  771 HOH A O     1 
HETATM 3836 O O     . HOH D 4 .   ? 7.125   33.774 0.400   1.00 44.24 ?  772 HOH A O     1 
HETATM 3837 O O     . HOH D 4 .   ? -24.771 -2.554 13.352  1.00 35.36 ?  773 HOH A O     1 
HETATM 3838 O O     . HOH D 4 .   ? -13.741 22.788 4.095   1.00 25.11 ?  774 HOH A O     1 
HETATM 3839 O O     . HOH D 4 .   ? -10.372 42.388 25.224  1.00 31.86 ?  775 HOH A O     1 
HETATM 3840 O O     . HOH D 4 .   ? 0.475   30.035 14.032  1.00 22.49 ?  776 HOH A O     1 
HETATM 3841 O O     . HOH D 4 .   ? -0.186  25.607 16.601  1.00 31.86 ?  777 HOH A O     1 
HETATM 3842 O O     . HOH D 4 .   ? -25.839 27.941 12.639  1.00 32.37 ?  778 HOH A O     1 
HETATM 3843 O O     . HOH D 4 .   ? -13.646 19.887 5.350   1.00 25.76 ?  779 HOH A O     1 
HETATM 3844 O O     . HOH D 4 .   ? 1.222   47.767 22.353  1.00 37.83 ?  780 HOH A O     1 
HETATM 3845 O O     . HOH D 4 .   ? -1.142  18.953 19.924  1.00 35.22 ?  781 HOH A O     1 
HETATM 3846 O O     . HOH D 4 .   ? -11.377 22.491 15.782  1.00 21.66 ?  782 HOH A O     1 
HETATM 3847 O O     . HOH D 4 .   ? -8.471  10.696 33.836  1.00 46.05 ?  783 HOH A O     1 
HETATM 3848 O O     . HOH D 4 .   ? -12.005 19.392 35.571  1.00 38.94 ?  784 HOH A O     1 
HETATM 3849 O O     . HOH D 4 .   ? -23.291 33.229 -10.672 1.00 36.34 ?  785 HOH A O     1 
HETATM 3850 O O     . HOH D 4 .   ? -7.855  53.175 8.506   1.00 34.61 ?  786 HOH A O     1 
HETATM 3851 O O     . HOH D 4 .   ? -26.964 10.372 -5.754  1.00 37.61 ?  787 HOH A O     1 
HETATM 3852 O O     . HOH D 4 .   ? -0.526  13.772 26.163  1.00 35.27 ?  788 HOH A O     1 
HETATM 3853 O O     . HOH D 4 .   ? 0.614   33.350 9.753   1.00 23.02 ?  789 HOH A O     1 
HETATM 3854 O O     . HOH D 4 .   ? 3.640   40.694 -0.465  1.00 38.27 ?  790 HOH A O     1 
HETATM 3855 O O     . HOH D 4 .   ? -31.725 8.227  3.952   1.00 31.05 ?  791 HOH A O     1 
HETATM 3856 O O     . HOH D 4 .   ? -19.441 24.812 9.706   1.00 27.60 ?  792 HOH A O     1 
HETATM 3857 O O     . HOH D 4 .   ? -17.894 32.816 -12.496 1.00 32.75 ?  793 HOH A O     1 
HETATM 3858 O O     . HOH D 4 .   ? -20.427 8.476  0.150   1.00 21.35 ?  794 HOH A O     1 
HETATM 3859 O O     . HOH D 4 .   ? -3.638  28.884 22.317  1.00 36.72 ?  795 HOH A O     1 
HETATM 3860 O O     . HOH D 4 .   ? -26.379 31.897 15.837  1.00 36.70 ?  796 HOH A O     1 
HETATM 3861 O O     . HOH D 4 .   ? -9.108  19.775 -3.601  1.00 31.29 ?  797 HOH A O     1 
HETATM 3862 O O     . HOH D 4 .   ? -18.933 38.379 22.342  1.00 37.76 ?  798 HOH A O     1 
HETATM 3863 O O     . HOH D 4 .   ? 1.861   20.111 23.783  1.00 30.48 ?  799 HOH A O     1 
HETATM 3864 O O     . HOH D 4 .   ? 4.713   47.350 16.067  1.00 41.78 ?  800 HOH A O     1 
HETATM 3865 O O     . HOH D 4 .   ? -33.813 15.491 3.037   1.00 36.15 ?  801 HOH A O     1 
HETATM 3866 O O     . HOH D 4 .   ? -22.248 38.560 19.938  1.00 38.67 ?  802 HOH A O     1 
HETATM 3867 O O     . HOH D 4 .   ? -7.703  -1.638 -1.812  1.00 49.30 ?  803 HOH A O     1 
HETATM 3868 O O     . HOH D 4 .   ? -7.363  54.919 10.416  1.00 44.16 ?  804 HOH A O     1 
HETATM 3869 O O     . HOH D 4 .   ? -27.690 44.106 21.750  1.00 49.87 ?  805 HOH A O     1 
HETATM 3870 O O     . HOH D 4 .   ? 7.572   10.180 26.885  1.00 51.47 ?  806 HOH A O     1 
HETATM 3871 O O     . HOH D 4 .   ? 6.044   30.380 12.569  1.00 33.06 ?  807 HOH A O     1 
HETATM 3872 O O     . HOH D 4 .   ? -12.521 -3.487 12.037  1.00 47.45 ?  808 HOH A O     1 
HETATM 3873 O O     . HOH D 4 .   ? 2.644   31.442 13.666  1.00 33.71 ?  809 HOH A O     1 
HETATM 3874 O O     . HOH D 4 .   ? -15.091 22.146 0.178   1.00 33.31 ?  810 HOH A O     1 
HETATM 3875 O O     . HOH D 4 .   ? -6.507  10.936 34.783  1.00 39.44 ?  811 HOH A O     1 
HETATM 3876 O O     . HOH D 4 .   ? -17.941 23.971 35.996  1.00 40.78 ?  812 HOH A O     1 
HETATM 3877 O O     . HOH D 4 .   ? -19.714 20.127 35.705  1.00 37.68 ?  813 HOH A O     1 
HETATM 3878 O O     . HOH D 4 .   ? 10.112  2.685  16.827  1.00 42.27 ?  814 HOH A O     1 
HETATM 3879 O O     . HOH D 4 .   ? -5.964  22.853 22.225  1.00 31.62 ?  815 HOH A O     1 
HETATM 3880 O O     . HOH D 4 .   ? 3.469   49.419 16.781  1.00 38.67 ?  816 HOH A O     1 
HETATM 3881 O O     . HOH D 4 .   ? -16.478 21.120 1.695   1.00 30.99 ?  817 HOH A O     1 
HETATM 3882 O O     . HOH D 4 .   ? 1.617   30.821 10.947  1.00 31.21 ?  818 HOH A O     1 
HETATM 3883 O O     . HOH D 4 .   ? -31.072 34.755 11.497  1.00 33.19 ?  819 HOH A O     1 
HETATM 3884 O O     . HOH D 4 .   ? -34.125 9.841  1.056   1.00 42.58 ?  820 HOH A O     1 
HETATM 3885 O O     . HOH D 4 .   ? -3.233  -1.746 12.489  1.00 39.15 ?  821 HOH A O     1 
HETATM 3886 O O     . HOH D 4 .   ? 7.611   40.582 1.576   1.00 30.52 ?  822 HOH A O     1 
HETATM 3887 O O     . HOH D 4 .   ? -22.139 24.270 -11.064 1.00 31.73 ?  823 HOH A O     1 
HETATM 3888 O O     . HOH D 4 .   ? -34.040 25.997 10.105  1.00 45.69 ?  824 HOH A O     1 
HETATM 3889 O O     . HOH D 4 .   ? 9.641   36.495 2.353   1.00 27.22 ?  825 HOH A O     1 
HETATM 3890 O O     . HOH D 4 .   ? -28.331 22.159 -1.340  1.00 23.06 ?  826 HOH A O     1 
HETATM 3891 O O     . HOH D 4 .   ? -19.752 31.404 -13.129 1.00 35.95 ?  827 HOH A O     1 
HETATM 3892 O O     . HOH D 4 .   ? -24.481 24.719 -11.501 1.00 39.08 ?  828 HOH A O     1 
HETATM 3893 O O     . HOH D 4 .   ? -0.406  29.102 19.582  1.00 46.06 ?  829 HOH A O     1 
HETATM 3894 O O     . HOH D 4 .   ? -20.165 53.354 11.341  1.00 46.10 ?  830 HOH A O     1 
HETATM 3895 O O     . HOH D 4 .   ? -27.800 39.741 7.189   1.00 38.63 ?  831 HOH A O     1 
HETATM 3896 O O     . HOH D 4 .   ? -30.429 18.202 3.486   1.00 36.79 ?  832 HOH A O     1 
HETATM 3897 O O     . HOH D 4 .   ? -29.147 38.570 10.333  1.00 37.47 ?  833 HOH A O     1 
HETATM 3898 O O     . HOH D 4 .   ? -6.871  4.609  27.053  1.00 38.53 ?  834 HOH A O     1 
HETATM 3899 O O     . HOH D 4 .   ? 2.725   51.516 15.505  1.00 37.46 ?  835 HOH A O     1 
HETATM 3900 O O     . HOH D 4 .   ? -9.783  4.190  -7.608  1.00 44.32 ?  836 HOH A O     1 
HETATM 3901 O O     . HOH D 4 .   ? 12.099  34.244 13.538  1.00 34.61 ?  837 HOH A O     1 
HETATM 3902 O O     . HOH D 4 .   ? 1.141   16.586 27.289  1.00 36.61 ?  838 HOH A O     1 
HETATM 3903 O O     . HOH D 4 .   ? -1.373  30.182 23.675  1.00 35.16 ?  839 HOH A O     1 
HETATM 3904 O O     . HOH D 4 .   ? 11.517  33.885 -0.255  1.00 36.56 ?  840 HOH A O     1 
# 
