data_8YNQ
# 
_entry.id   8YNQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8YNQ         pdb_00008ynq 10.2210/pdb8ynq/pdb 
WWPDB D_1300046006 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-19 ? 
2 'Structure model' 1 1 2025-02-26 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'              
2  2 'Structure model' '_citation.journal_abbrev'       
3  2 'Structure model' '_citation.journal_id_CSD'       
4  2 'Structure model' '_citation.journal_id_ISSN'      
5  2 'Structure model' '_citation.journal_volume'       
6  2 'Structure model' '_citation.page_first'           
7  2 'Structure model' '_citation.page_last'            
8  2 'Structure model' '_citation.pdbx_database_id_DOI' 
9  2 'Structure model' '_citation.title'                
10 2 'Structure model' '_citation.year'                 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YNQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yanyaqian@sjtu.edu.cn 
_pdbx_contact_author.name_first         yaqian 
_pdbx_contact_author.name_last          yan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0008-0232-1517 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, M.J.'  1 ? 
'Yan, Y.Q.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                2550 
_citation.page_last                 2560 
_citation.title                     
;Structural Insights into the Substrate Recognition Mechanism of an ATP-Grasp Peptide-Ligase Producing Diverse Dipeptides Containing Unnatural Amino Acids
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c07750 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yan, Y.Q.'   1  ? 
primary 'Li, S.Y.'    2  ? 
primary 'Wu, X.N.'    3  ? 
primary 'Zhou, T.'    4  ? 
primary 'Li, J.X.'    5  ? 
primary 'Huang, S.X.' 6  ? 
primary 'Zheng, J.T.' 7  ? 
primary 'Xu, J.'      8  ? 
primary 'Da, L.T.'    9  ? 
primary 'Xu, M.J.'    10 ? 
# 
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 'ATP-grasp peptide ligase'                    49193.633 4   ? ? ? 'SRA: SRR28004724' 
2 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' 506.196   2   ? ? ? ?                  
3 non-polymer syn GLYCEROL                                      92.094    6   ? ? ? ?                  
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                       106.120   9   ? ? ? ?                  
5 non-polymer nat 'ADENOSINE MONOPHOSPHATE'                     347.221   1   ? ? ? ?                  
6 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"                    427.201   1   ? ? ? ?                  
7 non-polymer syn 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL      122.143   1   ? ? ? ?                  
8 water       nat water                                         18.015    325 ? ? ? ?                  
# 
_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       
;MPKIILPNFRADYSEQVRDWLGISDATASSTDTTARFLWHAEDGDVLVIPDTVDPDFPGYVADTLGIDGTSVHVERTQTP
LSEAVLQDPEFIDRLAAHTGTGAGWSLFPCVSTRAAAQLTRKLNVAALDGYEFAMQNGIDLLNMKSTFRRLAAGLGTPLT
DGVVARGPAEVRSAIQELIAETGMVIAKQDRSGGGHGNIGISTSPESSFPGTREVLAYANDQLDTLADTLWSQLTDTQNQ
FITVETYHRADQRFFFEYHLDGDRARFLHSSILKYEQLPEGSGGSAKWIGLDSPSRSEFEATLKPAEEFIEMIRTIGYRG
YVNIDGIVLDDGRVFFHEINARWSGGLIYHTVAERLLGHDYARNNFFSSILNVVPAGLADLLRSLERAGVRYDKDSGEGA
VVLGCNSDLGPGAELLVFSKDWDRLTAMKDEIATTAGTLSLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPKIILPNFRADYSEQVRDWLGISDATASSTDTTARFLWHAEDGDVLVIPDTVDPDFPGYVADTLGIDGTSVHVERTQTP
LSEAVLQDPEFIDRLAAHTGTGAGWSLFPCVSTRAAAQLTRKLNVAALDGYEFAMQNGIDLLNMKSTFRRLAAGLGTPLT
DGVVARGPAEVRSAIQELIAETGMVIAKQDRSGGGHGNIGISTSPESSFPGTREVLAYANDQLDTLADTLWSQLTDTQNQ
FITVETYHRADQRFFFEYHLDGDRARFLHSSILKYEQLPEGSGGSAKWIGLDSPSRSEFEATLKPAEEFIEMIRTIGYRG
YVNIDGIVLDDGRVFFHEINARWSGGLIYHTVAERLLGHDYARNNFFSSILNVVPAGLADLLRSLERAGVRYDKDSGEGA
VVLGCNSDLGPGAELLVFSKDWDRLTAMKDEIATTAGTLSLEHHHHHH
;
_entity_poly.pdbx_strand_id                 C,D,A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ANP 
3 GLYCEROL                                      GOL 
4 'DI(HYDROXYETHYL)ETHER'                       PEG 
5 'ADENOSINE MONOPHOSPHATE'                     AMP 
6 "ADENOSINE-5'-DIPHOSPHATE"                    ADP 
7 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL      TRS 
8 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   PRO n 
1 3   LYS n 
1 4   ILE n 
1 5   ILE n 
1 6   LEU n 
1 7   PRO n 
1 8   ASN n 
1 9   PHE n 
1 10  ARG n 
1 11  ALA n 
1 12  ASP n 
1 13  TYR n 
1 14  SER n 
1 15  GLU n 
1 16  GLN n 
1 17  VAL n 
1 18  ARG n 
1 19  ASP n 
1 20  TRP n 
1 21  LEU n 
1 22  GLY n 
1 23  ILE n 
1 24  SER n 
1 25  ASP n 
1 26  ALA n 
1 27  THR n 
1 28  ALA n 
1 29  SER n 
1 30  SER n 
1 31  THR n 
1 32  ASP n 
1 33  THR n 
1 34  THR n 
1 35  ALA n 
1 36  ARG n 
1 37  PHE n 
1 38  LEU n 
1 39  TRP n 
1 40  HIS n 
1 41  ALA n 
1 42  GLU n 
1 43  ASP n 
1 44  GLY n 
1 45  ASP n 
1 46  VAL n 
1 47  LEU n 
1 48  VAL n 
1 49  ILE n 
1 50  PRO n 
1 51  ASP n 
1 52  THR n 
1 53  VAL n 
1 54  ASP n 
1 55  PRO n 
1 56  ASP n 
1 57  PHE n 
1 58  PRO n 
1 59  GLY n 
1 60  TYR n 
1 61  VAL n 
1 62  ALA n 
1 63  ASP n 
1 64  THR n 
1 65  LEU n 
1 66  GLY n 
1 67  ILE n 
1 68  ASP n 
1 69  GLY n 
1 70  THR n 
1 71  SER n 
1 72  VAL n 
1 73  HIS n 
1 74  VAL n 
1 75  GLU n 
1 76  ARG n 
1 77  THR n 
1 78  GLN n 
1 79  THR n 
1 80  PRO n 
1 81  LEU n 
1 82  SER n 
1 83  GLU n 
1 84  ALA n 
1 85  VAL n 
1 86  LEU n 
1 87  GLN n 
1 88  ASP n 
1 89  PRO n 
1 90  GLU n 
1 91  PHE n 
1 92  ILE n 
1 93  ASP n 
1 94  ARG n 
1 95  LEU n 
1 96  ALA n 
1 97  ALA n 
1 98  HIS n 
1 99  THR n 
1 100 GLY n 
1 101 THR n 
1 102 GLY n 
1 103 ALA n 
1 104 GLY n 
1 105 TRP n 
1 106 SER n 
1 107 LEU n 
1 108 PHE n 
1 109 PRO n 
1 110 CYS n 
1 111 VAL n 
1 112 SER n 
1 113 THR n 
1 114 ARG n 
1 115 ALA n 
1 116 ALA n 
1 117 ALA n 
1 118 GLN n 
1 119 LEU n 
1 120 THR n 
1 121 ARG n 
1 122 LYS n 
1 123 LEU n 
1 124 ASN n 
1 125 VAL n 
1 126 ALA n 
1 127 ALA n 
1 128 LEU n 
1 129 ASP n 
1 130 GLY n 
1 131 TYR n 
1 132 GLU n 
1 133 PHE n 
1 134 ALA n 
1 135 MET n 
1 136 GLN n 
1 137 ASN n 
1 138 GLY n 
1 139 ILE n 
1 140 ASP n 
1 141 LEU n 
1 142 LEU n 
1 143 ASN n 
1 144 MET n 
1 145 LYS n 
1 146 SER n 
1 147 THR n 
1 148 PHE n 
1 149 ARG n 
1 150 ARG n 
1 151 LEU n 
1 152 ALA n 
1 153 ALA n 
1 154 GLY n 
1 155 LEU n 
1 156 GLY n 
1 157 THR n 
1 158 PRO n 
1 159 LEU n 
1 160 THR n 
1 161 ASP n 
1 162 GLY n 
1 163 VAL n 
1 164 VAL n 
1 165 ALA n 
1 166 ARG n 
1 167 GLY n 
1 168 PRO n 
1 169 ALA n 
1 170 GLU n 
1 171 VAL n 
1 172 ARG n 
1 173 SER n 
1 174 ALA n 
1 175 ILE n 
1 176 GLN n 
1 177 GLU n 
1 178 LEU n 
1 179 ILE n 
1 180 ALA n 
1 181 GLU n 
1 182 THR n 
1 183 GLY n 
1 184 MET n 
1 185 VAL n 
1 186 ILE n 
1 187 ALA n 
1 188 LYS n 
1 189 GLN n 
1 190 ASP n 
1 191 ARG n 
1 192 SER n 
1 193 GLY n 
1 194 GLY n 
1 195 GLY n 
1 196 HIS n 
1 197 GLY n 
1 198 ASN n 
1 199 ILE n 
1 200 GLY n 
1 201 ILE n 
1 202 SER n 
1 203 THR n 
1 204 SER n 
1 205 PRO n 
1 206 GLU n 
1 207 SER n 
1 208 SER n 
1 209 PHE n 
1 210 PRO n 
1 211 GLY n 
1 212 THR n 
1 213 ARG n 
1 214 GLU n 
1 215 VAL n 
1 216 LEU n 
1 217 ALA n 
1 218 TYR n 
1 219 ALA n 
1 220 ASN n 
1 221 ASP n 
1 222 GLN n 
1 223 LEU n 
1 224 ASP n 
1 225 THR n 
1 226 LEU n 
1 227 ALA n 
1 228 ASP n 
1 229 THR n 
1 230 LEU n 
1 231 TRP n 
1 232 SER n 
1 233 GLN n 
1 234 LEU n 
1 235 THR n 
1 236 ASP n 
1 237 THR n 
1 238 GLN n 
1 239 ASN n 
1 240 GLN n 
1 241 PHE n 
1 242 ILE n 
1 243 THR n 
1 244 VAL n 
1 245 GLU n 
1 246 THR n 
1 247 TYR n 
1 248 HIS n 
1 249 ARG n 
1 250 ALA n 
1 251 ASP n 
1 252 GLN n 
1 253 ARG n 
1 254 PHE n 
1 255 PHE n 
1 256 PHE n 
1 257 GLU n 
1 258 TYR n 
1 259 HIS n 
1 260 LEU n 
1 261 ASP n 
1 262 GLY n 
1 263 ASP n 
1 264 ARG n 
1 265 ALA n 
1 266 ARG n 
1 267 PHE n 
1 268 LEU n 
1 269 HIS n 
1 270 SER n 
1 271 SER n 
1 272 ILE n 
1 273 LEU n 
1 274 LYS n 
1 275 TYR n 
1 276 GLU n 
1 277 GLN n 
1 278 LEU n 
1 279 PRO n 
1 280 GLU n 
1 281 GLY n 
1 282 SER n 
1 283 GLY n 
1 284 GLY n 
1 285 SER n 
1 286 ALA n 
1 287 LYS n 
1 288 TRP n 
1 289 ILE n 
1 290 GLY n 
1 291 LEU n 
1 292 ASP n 
1 293 SER n 
1 294 PRO n 
1 295 SER n 
1 296 ARG n 
1 297 SER n 
1 298 GLU n 
1 299 PHE n 
1 300 GLU n 
1 301 ALA n 
1 302 THR n 
1 303 LEU n 
1 304 LYS n 
1 305 PRO n 
1 306 ALA n 
1 307 GLU n 
1 308 GLU n 
1 309 PHE n 
1 310 ILE n 
1 311 GLU n 
1 312 MET n 
1 313 ILE n 
1 314 ARG n 
1 315 THR n 
1 316 ILE n 
1 317 GLY n 
1 318 TYR n 
1 319 ARG n 
1 320 GLY n 
1 321 TYR n 
1 322 VAL n 
1 323 ASN n 
1 324 ILE n 
1 325 ASP n 
1 326 GLY n 
1 327 ILE n 
1 328 VAL n 
1 329 LEU n 
1 330 ASP n 
1 331 ASP n 
1 332 GLY n 
1 333 ARG n 
1 334 VAL n 
1 335 PHE n 
1 336 PHE n 
1 337 HIS n 
1 338 GLU n 
1 339 ILE n 
1 340 ASN n 
1 341 ALA n 
1 342 ARG n 
1 343 TRP n 
1 344 SER n 
1 345 GLY n 
1 346 GLY n 
1 347 LEU n 
1 348 ILE n 
1 349 TYR n 
1 350 HIS n 
1 351 THR n 
1 352 VAL n 
1 353 ALA n 
1 354 GLU n 
1 355 ARG n 
1 356 LEU n 
1 357 LEU n 
1 358 GLY n 
1 359 HIS n 
1 360 ASP n 
1 361 TYR n 
1 362 ALA n 
1 363 ARG n 
1 364 ASN n 
1 365 ASN n 
1 366 PHE n 
1 367 PHE n 
1 368 SER n 
1 369 SER n 
1 370 ILE n 
1 371 LEU n 
1 372 ASN n 
1 373 VAL n 
1 374 VAL n 
1 375 PRO n 
1 376 ALA n 
1 377 GLY n 
1 378 LEU n 
1 379 ALA n 
1 380 ASP n 
1 381 LEU n 
1 382 LEU n 
1 383 ARG n 
1 384 SER n 
1 385 LEU n 
1 386 GLU n 
1 387 ARG n 
1 388 ALA n 
1 389 GLY n 
1 390 VAL n 
1 391 ARG n 
1 392 TYR n 
1 393 ASP n 
1 394 LYS n 
1 395 ASP n 
1 396 SER n 
1 397 GLY n 
1 398 GLU n 
1 399 GLY n 
1 400 ALA n 
1 401 VAL n 
1 402 VAL n 
1 403 LEU n 
1 404 GLY n 
1 405 CYS n 
1 406 ASN n 
1 407 SER n 
1 408 ASP n 
1 409 LEU n 
1 410 GLY n 
1 411 PRO n 
1 412 GLY n 
1 413 ALA n 
1 414 GLU n 
1 415 LEU n 
1 416 LEU n 
1 417 VAL n 
1 418 PHE n 
1 419 SER n 
1 420 LYS n 
1 421 ASP n 
1 422 TRP n 
1 423 ASP n 
1 424 ARG n 
1 425 LEU n 
1 426 THR n 
1 427 ALA n 
1 428 MET n 
1 429 LYS n 
1 430 ASP n 
1 431 GLU n 
1 432 ILE n 
1 433 ALA n 
1 434 THR n 
1 435 THR n 
1 436 ALA n 
1 437 GLY n 
1 438 THR n 
1 439 LEU n 
1 440 SER n 
1 441 LEU n 
1 442 GLU n 
1 443 HIS n 
1 444 HIS n 
1 445 HIS n 
1 446 HIS n 
1 447 HIS n 
1 448 HIS 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                   448 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Alb28 
_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      'Streptomyces albogriseolus 1-36' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1093098 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"                    ?                               'C10 H15 N5 O10 P2' 
427.201 
ALA 'L-peptide linking' y ALANINE                                       ?                               'C3 H7 N O2'        89.093 
AMP non-polymer         . 'ADENOSINE MONOPHOSPHATE'                     ?                               'C10 H14 N5 O7 P'   
347.221 
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ?                               'C10 H17 N6 O12 P3' 
506.196 
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 
GOL non-polymer         . GLYCEROL                                      'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094 
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                       ?                               'C4 H10 O3'         
106.120 
PHE 'L-peptide linking' y PHENYLALANINE                                 ?                               'C9 H11 N O2'       
165.189 
PRO 'L-peptide linking' y PROLINE                                       ?                               'C5 H9 N O2'        
115.130 
SER 'L-peptide linking' y SERINE                                        ?                               'C3 H7 N O3'        
105.093 
THR 'L-peptide linking' y THREONINE                                     ?                               'C4 H9 N O3'        
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                    ?                               'C11 H12 N2 O2'     
204.225 
TRS non-polymer         . 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL      'TRIS BUFFER'                   'C4 H12 N O3 1'     
122.143 
TYR 'L-peptide linking' y TYROSINE                                      ?                               'C9 H11 N O3'       
181.189 
VAL 'L-peptide linking' y VALINE                                        ?                               'C5 H11 N O2'       
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   C . n 
A 1 2   PRO 2   2   ?   ?   ?   C . n 
A 1 3   LYS 3   3   ?   ?   ?   C . n 
A 1 4   ILE 4   4   ?   ?   ?   C . n 
A 1 5   ILE 5   5   ?   ?   ?   C . n 
A 1 6   LEU 6   6   ?   ?   ?   C . n 
A 1 7   PRO 7   7   ?   ?   ?   C . n 
A 1 8   ASN 8   8   ?   ?   ?   C . n 
A 1 9   PHE 9   9   ?   ?   ?   C . n 
A 1 10  ARG 10  10  ?   ?   ?   C . n 
A 1 11  ALA 11  11  ?   ?   ?   C . n 
A 1 12  ASP 12  12  ?   ?   ?   C . n 
A 1 13  TYR 13  13  ?   ?   ?   C . n 
A 1 14  SER 14  14  ?   ?   ?   C . n 
A 1 15  GLU 15  15  ?   ?   ?   C . n 
A 1 16  GLN 16  16  ?   ?   ?   C . n 
A 1 17  VAL 17  17  ?   ?   ?   C . n 
A 1 18  ARG 18  18  ?   ?   ?   C . n 
A 1 19  ASP 19  19  ?   ?   ?   C . n 
A 1 20  TRP 20  20  ?   ?   ?   C . n 
A 1 21  LEU 21  21  ?   ?   ?   C . n 
A 1 22  GLY 22  22  ?   ?   ?   C . n 
A 1 23  ILE 23  23  ?   ?   ?   C . n 
A 1 24  SER 24  24  ?   ?   ?   C . n 
A 1 25  ASP 25  25  ?   ?   ?   C . n 
A 1 26  ALA 26  26  ?   ?   ?   C . n 
A 1 27  THR 27  27  ?   ?   ?   C . n 
A 1 28  ALA 28  28  ?   ?   ?   C . n 
A 1 29  SER 29  29  29  SER SER C . n 
A 1 30  SER 30  30  30  SER SER C . n 
A 1 31  THR 31  31  31  THR THR C . n 
A 1 32  ASP 32  32  32  ASP ASP C . n 
A 1 33  THR 33  33  33  THR THR C . n 
A 1 34  THR 34  34  34  THR THR C . n 
A 1 35  ALA 35  35  35  ALA ALA C . n 
A 1 36  ARG 36  36  36  ARG ARG C . n 
A 1 37  PHE 37  37  37  PHE PHE C . n 
A 1 38  LEU 38  38  38  LEU LEU C . n 
A 1 39  TRP 39  39  39  TRP TRP C . n 
A 1 40  HIS 40  40  40  HIS HIS C . n 
A 1 41  ALA 41  41  41  ALA ALA C . n 
A 1 42  GLU 42  42  42  GLU GLU C . n 
A 1 43  ASP 43  43  43  ASP ASP C . n 
A 1 44  GLY 44  44  44  GLY GLY C . n 
A 1 45  ASP 45  45  45  ASP ASP C . n 
A 1 46  VAL 46  46  46  VAL VAL C . n 
A 1 47  LEU 47  47  47  LEU LEU C . n 
A 1 48  VAL 48  48  48  VAL VAL C . n 
A 1 49  ILE 49  49  49  ILE ILE C . n 
A 1 50  PRO 50  50  50  PRO PRO C . n 
A 1 51  ASP 51  51  51  ASP ASP C . n 
A 1 52  THR 52  52  52  THR THR C . n 
A 1 53  VAL 53  53  53  VAL VAL C . n 
A 1 54  ASP 54  54  54  ASP ASP C . n 
A 1 55  PRO 55  55  55  PRO PRO C . n 
A 1 56  ASP 56  56  56  ASP ASP C . n 
A 1 57  PHE 57  57  57  PHE PHE C . n 
A 1 58  PRO 58  58  58  PRO PRO C . n 
A 1 59  GLY 59  59  59  GLY GLY C . n 
A 1 60  TYR 60  60  60  TYR TYR C . n 
A 1 61  VAL 61  61  61  VAL VAL C . n 
A 1 62  ALA 62  62  62  ALA ALA C . n 
A 1 63  ASP 63  63  63  ASP ASP C . n 
A 1 64  THR 64  64  64  THR THR C . n 
A 1 65  LEU 65  65  65  LEU LEU C . n 
A 1 66  GLY 66  66  66  GLY GLY C . n 
A 1 67  ILE 67  67  67  ILE ILE C . n 
A 1 68  ASP 68  68  68  ASP ASP C . n 
A 1 69  GLY 69  69  69  GLY GLY C . n 
A 1 70  THR 70  70  70  THR THR C . n 
A 1 71  SER 71  71  71  SER SER C . n 
A 1 72  VAL 72  72  72  VAL VAL C . n 
A 1 73  HIS 73  73  73  HIS HIS C . n 
A 1 74  VAL 74  74  74  VAL VAL C . n 
A 1 75  GLU 75  75  75  GLU GLU C . n 
A 1 76  ARG 76  76  76  ARG ARG C . n 
A 1 77  THR 77  77  77  THR THR C . n 
A 1 78  GLN 78  78  78  GLN GLN C . n 
A 1 79  THR 79  79  79  THR THR C . n 
A 1 80  PRO 80  80  80  PRO PRO C . n 
A 1 81  LEU 81  81  81  LEU LEU C . n 
A 1 82  SER 82  82  82  SER SER C . n 
A 1 83  GLU 83  83  83  GLU GLU C . n 
A 1 84  ALA 84  84  84  ALA ALA C . n 
A 1 85  VAL 85  85  85  VAL VAL C . n 
A 1 86  LEU 86  86  86  LEU LEU C . n 
A 1 87  GLN 87  87  87  GLN GLN C . n 
A 1 88  ASP 88  88  88  ASP ASP C . n 
A 1 89  PRO 89  89  89  PRO PRO C . n 
A 1 90  GLU 90  90  90  GLU GLU C . n 
A 1 91  PHE 91  91  91  PHE PHE C . n 
A 1 92  ILE 92  92  92  ILE ILE C . n 
A 1 93  ASP 93  93  93  ASP ASP C . n 
A 1 94  ARG 94  94  94  ARG ARG C . n 
A 1 95  LEU 95  95  95  LEU LEU C . n 
A 1 96  ALA 96  96  96  ALA ALA C . n 
A 1 97  ALA 97  97  97  ALA ALA C . n 
A 1 98  HIS 98  98  98  HIS HIS C . n 
A 1 99  THR 99  99  99  THR THR C . n 
A 1 100 GLY 100 100 100 GLY GLY C . n 
A 1 101 THR 101 101 101 THR THR C . n 
A 1 102 GLY 102 102 102 GLY GLY C . n 
A 1 103 ALA 103 103 103 ALA ALA C . n 
A 1 104 GLY 104 104 104 GLY GLY C . n 
A 1 105 TRP 105 105 105 TRP TRP C . n 
A 1 106 SER 106 106 106 SER SER C . n 
A 1 107 LEU 107 107 107 LEU LEU C . n 
A 1 108 PHE 108 108 108 PHE PHE C . n 
A 1 109 PRO 109 109 109 PRO PRO C . n 
A 1 110 CYS 110 110 110 CYS CYS C . n 
A 1 111 VAL 111 111 111 VAL VAL C . n 
A 1 112 SER 112 112 112 SER SER C . n 
A 1 113 THR 113 113 113 THR THR C . n 
A 1 114 ARG 114 114 114 ARG ARG C . n 
A 1 115 ALA 115 115 115 ALA ALA C . n 
A 1 116 ALA 116 116 116 ALA ALA C . n 
A 1 117 ALA 117 117 117 ALA ALA C . n 
A 1 118 GLN 118 118 118 GLN GLN C . n 
A 1 119 LEU 119 119 119 LEU LEU C . n 
A 1 120 THR 120 120 120 THR THR C . n 
A 1 121 ARG 121 121 121 ARG ARG C . n 
A 1 122 LYS 122 122 122 LYS LYS C . n 
A 1 123 LEU 123 123 123 LEU LEU C . n 
A 1 124 ASN 124 124 124 ASN ASN C . n 
A 1 125 VAL 125 125 125 VAL VAL C . n 
A 1 126 ALA 126 126 126 ALA ALA C . n 
A 1 127 ALA 127 127 127 ALA ALA C . n 
A 1 128 LEU 128 128 128 LEU LEU C . n 
A 1 129 ASP 129 129 129 ASP ASP C . n 
A 1 130 GLY 130 130 130 GLY GLY C . n 
A 1 131 TYR 131 131 131 TYR TYR C . n 
A 1 132 GLU 132 132 132 GLU GLU C . n 
A 1 133 PHE 133 133 133 PHE PHE C . n 
A 1 134 ALA 134 134 134 ALA ALA C . n 
A 1 135 MET 135 135 135 MET MET C . n 
A 1 136 GLN 136 136 136 GLN GLN C . n 
A 1 137 ASN 137 137 137 ASN ASN C . n 
A 1 138 GLY 138 138 138 GLY GLY C . n 
A 1 139 ILE 139 139 139 ILE ILE C . n 
A 1 140 ASP 140 140 140 ASP ASP C . n 
A 1 141 LEU 141 141 141 LEU LEU C . n 
A 1 142 LEU 142 142 142 LEU LEU C . n 
A 1 143 ASN 143 143 143 ASN ASN C . n 
A 1 144 MET 144 144 144 MET MET C . n 
A 1 145 LYS 145 145 145 LYS LYS C . n 
A 1 146 SER 146 146 146 SER SER C . n 
A 1 147 THR 147 147 147 THR THR C . n 
A 1 148 PHE 148 148 148 PHE PHE C . n 
A 1 149 ARG 149 149 149 ARG ARG C . n 
A 1 150 ARG 150 150 150 ARG ARG C . n 
A 1 151 LEU 151 151 151 LEU LEU C . n 
A 1 152 ALA 152 152 152 ALA ALA C . n 
A 1 153 ALA 153 153 153 ALA ALA C . n 
A 1 154 GLY 154 154 154 GLY GLY C . n 
A 1 155 LEU 155 155 155 LEU LEU C . n 
A 1 156 GLY 156 156 156 GLY GLY C . n 
A 1 157 THR 157 157 157 THR THR C . n 
A 1 158 PRO 158 158 158 PRO PRO C . n 
A 1 159 LEU 159 159 159 LEU LEU C . n 
A 1 160 THR 160 160 160 THR THR C . n 
A 1 161 ASP 161 161 161 ASP ASP C . n 
A 1 162 GLY 162 162 162 GLY GLY C . n 
A 1 163 VAL 163 163 163 VAL VAL C . n 
A 1 164 VAL 164 164 164 VAL VAL C . n 
A 1 165 ALA 165 165 165 ALA ALA C . n 
A 1 166 ARG 166 166 166 ARG ARG C . n 
A 1 167 GLY 167 167 167 GLY GLY C . n 
A 1 168 PRO 168 168 168 PRO PRO C . n 
A 1 169 ALA 169 169 169 ALA ALA C . n 
A 1 170 GLU 170 170 170 GLU GLU C . n 
A 1 171 VAL 171 171 171 VAL VAL C . n 
A 1 172 ARG 172 172 172 ARG ARG C . n 
A 1 173 SER 173 173 173 SER SER C . n 
A 1 174 ALA 174 174 174 ALA ALA C . n 
A 1 175 ILE 175 175 175 ILE ILE C . n 
A 1 176 GLN 176 176 176 GLN GLN C . n 
A 1 177 GLU 177 177 177 GLU GLU C . n 
A 1 178 LEU 178 178 178 LEU LEU C . n 
A 1 179 ILE 179 179 179 ILE ILE C . n 
A 1 180 ALA 180 180 180 ALA ALA C . n 
A 1 181 GLU 181 181 181 GLU GLU C . n 
A 1 182 THR 182 182 182 THR THR C . n 
A 1 183 GLY 183 183 183 GLY GLY C . n 
A 1 184 MET 184 184 184 MET MET C . n 
A 1 185 VAL 185 185 185 VAL VAL C . n 
A 1 186 ILE 186 186 186 ILE ILE C . n 
A 1 187 ALA 187 187 187 ALA ALA C . n 
A 1 188 LYS 188 188 188 LYS LYS C . n 
A 1 189 GLN 189 189 189 GLN GLN C . n 
A 1 190 ASP 190 190 190 ASP ASP C . n 
A 1 191 ARG 191 191 191 ARG ARG C . n 
A 1 192 SER 192 192 192 SER SER C . n 
A 1 193 GLY 193 193 193 GLY GLY C . n 
A 1 194 GLY 194 194 194 GLY GLY C . n 
A 1 195 GLY 195 195 195 GLY GLY C . n 
A 1 196 HIS 196 196 196 HIS HIS C . n 
A 1 197 GLY 197 197 197 GLY GLY C . n 
A 1 198 ASN 198 198 198 ASN ASN C . n 
A 1 199 ILE 199 199 199 ILE ILE C . n 
A 1 200 GLY 200 200 200 GLY GLY C . n 
A 1 201 ILE 201 201 201 ILE ILE C . n 
A 1 202 SER 202 202 202 SER SER C . n 
A 1 203 THR 203 203 203 THR THR C . n 
A 1 204 SER 204 204 204 SER SER C . n 
A 1 205 PRO 205 205 205 PRO PRO C . n 
A 1 206 GLU 206 206 206 GLU GLU C . n 
A 1 207 SER 207 207 207 SER SER C . n 
A 1 208 SER 208 208 208 SER SER C . n 
A 1 209 PHE 209 209 209 PHE PHE C . n 
A 1 210 PRO 210 210 210 PRO PRO C . n 
A 1 211 GLY 211 211 211 GLY GLY C . n 
A 1 212 THR 212 212 212 THR THR C . n 
A 1 213 ARG 213 213 213 ARG ARG C . n 
A 1 214 GLU 214 214 214 GLU GLU C . n 
A 1 215 VAL 215 215 215 VAL VAL C . n 
A 1 216 LEU 216 216 216 LEU LEU C . n 
A 1 217 ALA 217 217 217 ALA ALA C . n 
A 1 218 TYR 218 218 218 TYR TYR C . n 
A 1 219 ALA 219 219 219 ALA ALA C . n 
A 1 220 ASN 220 220 220 ASN ASN C . n 
A 1 221 ASP 221 221 221 ASP ASP C . n 
A 1 222 GLN 222 222 222 GLN GLN C . n 
A 1 223 LEU 223 223 223 LEU LEU C . n 
A 1 224 ASP 224 224 224 ASP ASP C . n 
A 1 225 THR 225 225 225 THR THR C . n 
A 1 226 LEU 226 226 226 LEU LEU C . n 
A 1 227 ALA 227 227 227 ALA ALA C . n 
A 1 228 ASP 228 228 228 ASP ASP C . n 
A 1 229 THR 229 229 229 THR THR C . n 
A 1 230 LEU 230 230 230 LEU LEU C . n 
A 1 231 TRP 231 231 231 TRP TRP C . n 
A 1 232 SER 232 232 232 SER SER C . n 
A 1 233 GLN 233 233 233 GLN GLN C . n 
A 1 234 LEU 234 234 234 LEU LEU C . n 
A 1 235 THR 235 235 235 THR THR C . n 
A 1 236 ASP 236 236 236 ASP ASP C . n 
A 1 237 THR 237 237 237 THR THR C . n 
A 1 238 GLN 238 238 238 GLN GLN C . n 
A 1 239 ASN 239 239 239 ASN ASN C . n 
A 1 240 GLN 240 240 240 GLN GLN C . n 
A 1 241 PHE 241 241 241 PHE PHE C . n 
A 1 242 ILE 242 242 242 ILE ILE C . n 
A 1 243 THR 243 243 243 THR THR C . n 
A 1 244 VAL 244 244 244 VAL VAL C . n 
A 1 245 GLU 245 245 245 GLU GLU C . n 
A 1 246 THR 246 246 246 THR THR C . n 
A 1 247 TYR 247 247 247 TYR TYR C . n 
A 1 248 HIS 248 248 248 HIS HIS C . n 
A 1 249 ARG 249 249 249 ARG ARG C . n 
A 1 250 ALA 250 250 250 ALA ALA C . n 
A 1 251 ASP 251 251 251 ASP ASP C . n 
A 1 252 GLN 252 252 252 GLN GLN C . n 
A 1 253 ARG 253 253 253 ARG ARG C . n 
A 1 254 PHE 254 254 254 PHE PHE C . n 
A 1 255 PHE 255 255 255 PHE PHE C . n 
A 1 256 PHE 256 256 256 PHE PHE C . n 
A 1 257 GLU 257 257 257 GLU GLU C . n 
A 1 258 TYR 258 258 258 TYR TYR C . n 
A 1 259 HIS 259 259 259 HIS HIS C . n 
A 1 260 LEU 260 260 260 LEU LEU C . n 
A 1 261 ASP 261 261 261 ASP ASP C . n 
A 1 262 GLY 262 262 262 GLY GLY C . n 
A 1 263 ASP 263 263 263 ASP ASP C . n 
A 1 264 ARG 264 264 264 ARG ARG C . n 
A 1 265 ALA 265 265 265 ALA ALA C . n 
A 1 266 ARG 266 266 266 ARG ARG C . n 
A 1 267 PHE 267 267 267 PHE PHE C . n 
A 1 268 LEU 268 268 268 LEU LEU C . n 
A 1 269 HIS 269 269 269 HIS HIS C . n 
A 1 270 SER 270 270 270 SER SER C . n 
A 1 271 SER 271 271 271 SER SER C . n 
A 1 272 ILE 272 272 272 ILE ILE C . n 
A 1 273 LEU 273 273 273 LEU LEU C . n 
A 1 274 LYS 274 274 274 LYS LYS C . n 
A 1 275 TYR 275 275 275 TYR TYR C . n 
A 1 276 GLU 276 276 276 GLU GLU C . n 
A 1 277 GLN 277 277 277 GLN GLN C . n 
A 1 278 LEU 278 278 278 LEU LEU C . n 
A 1 279 PRO 279 279 279 PRO PRO C . n 
A 1 280 GLU 280 280 280 GLU GLU C . n 
A 1 281 GLY 281 281 281 GLY GLY C . n 
A 1 282 SER 282 282 282 SER SER C . n 
A 1 283 GLY 283 283 283 GLY GLY C . n 
A 1 284 GLY 284 284 284 GLY GLY C . n 
A 1 285 SER 285 285 285 SER SER C . n 
A 1 286 ALA 286 286 286 ALA ALA C . n 
A 1 287 LYS 287 287 287 LYS LYS C . n 
A 1 288 TRP 288 288 288 TRP TRP C . n 
A 1 289 ILE 289 289 289 ILE ILE C . n 
A 1 290 GLY 290 290 290 GLY GLY C . n 
A 1 291 LEU 291 291 291 LEU LEU C . n 
A 1 292 ASP 292 292 292 ASP ASP C . n 
A 1 293 SER 293 293 293 SER SER C . n 
A 1 294 PRO 294 294 294 PRO PRO C . n 
A 1 295 SER 295 295 295 SER SER C . n 
A 1 296 ARG 296 296 296 ARG ARG C . n 
A 1 297 SER 297 297 297 SER SER C . n 
A 1 298 GLU 298 298 298 GLU GLU C . n 
A 1 299 PHE 299 299 299 PHE PHE C . n 
A 1 300 GLU 300 300 300 GLU GLU C . n 
A 1 301 ALA 301 301 301 ALA ALA C . n 
A 1 302 THR 302 302 302 THR THR C . n 
A 1 303 LEU 303 303 303 LEU LEU C . n 
A 1 304 LYS 304 304 304 LYS LYS C . n 
A 1 305 PRO 305 305 305 PRO PRO C . n 
A 1 306 ALA 306 306 306 ALA ALA C . n 
A 1 307 GLU 307 307 307 GLU GLU C . n 
A 1 308 GLU 308 308 308 GLU GLU C . n 
A 1 309 PHE 309 309 309 PHE PHE C . n 
A 1 310 ILE 310 310 310 ILE ILE C . n 
A 1 311 GLU 311 311 311 GLU GLU C . n 
A 1 312 MET 312 312 312 MET MET C . n 
A 1 313 ILE 313 313 313 ILE ILE C . n 
A 1 314 ARG 314 314 314 ARG ARG C . n 
A 1 315 THR 315 315 315 THR THR C . n 
A 1 316 ILE 316 316 316 ILE ILE C . n 
A 1 317 GLY 317 317 317 GLY GLY C . n 
A 1 318 TYR 318 318 318 TYR TYR C . n 
A 1 319 ARG 319 319 319 ARG ARG C . n 
A 1 320 GLY 320 320 320 GLY GLY C . n 
A 1 321 TYR 321 321 321 TYR TYR C . n 
A 1 322 VAL 322 322 322 VAL VAL C . n 
A 1 323 ASN 323 323 323 ASN ASN C . n 
A 1 324 ILE 324 324 324 ILE ILE C . n 
A 1 325 ASP 325 325 325 ASP ASP C . n 
A 1 326 GLY 326 326 326 GLY GLY C . n 
A 1 327 ILE 327 327 327 ILE ILE C . n 
A 1 328 VAL 328 328 328 VAL VAL C . n 
A 1 329 LEU 329 329 329 LEU LEU C . n 
A 1 330 ASP 330 330 330 ASP ASP C . n 
A 1 331 ASP 331 331 331 ASP ASP C . n 
A 1 332 GLY 332 332 332 GLY GLY C . n 
A 1 333 ARG 333 333 333 ARG ARG C . n 
A 1 334 VAL 334 334 334 VAL VAL C . n 
A 1 335 PHE 335 335 335 PHE PHE C . n 
A 1 336 PHE 336 336 336 PHE PHE C . n 
A 1 337 HIS 337 337 337 HIS HIS C . n 
A 1 338 GLU 338 338 338 GLU GLU C . n 
A 1 339 ILE 339 339 339 ILE ILE C . n 
A 1 340 ASN 340 340 340 ASN ASN C . n 
A 1 341 ALA 341 341 341 ALA ALA C . n 
A 1 342 ARG 342 342 342 ARG ARG C . n 
A 1 343 TRP 343 343 343 TRP TRP C . n 
A 1 344 SER 344 344 344 SER SER C . n 
A 1 345 GLY 345 345 345 GLY GLY C . n 
A 1 346 GLY 346 346 346 GLY GLY C . n 
A 1 347 LEU 347 347 347 LEU LEU C . n 
A 1 348 ILE 348 348 348 ILE ILE C . n 
A 1 349 TYR 349 349 349 TYR TYR C . n 
A 1 350 HIS 350 350 350 HIS HIS C . n 
A 1 351 THR 351 351 351 THR THR C . n 
A 1 352 VAL 352 352 352 VAL VAL C . n 
A 1 353 ALA 353 353 353 ALA ALA C . n 
A 1 354 GLU 354 354 354 GLU GLU C . n 
A 1 355 ARG 355 355 355 ARG ARG C . n 
A 1 356 LEU 356 356 356 LEU LEU C . n 
A 1 357 LEU 357 357 357 LEU LEU C . n 
A 1 358 GLY 358 358 358 GLY GLY C . n 
A 1 359 HIS 359 359 359 HIS HIS C . n 
A 1 360 ASP 360 360 360 ASP ASP C . n 
A 1 361 TYR 361 361 361 TYR TYR C . n 
A 1 362 ALA 362 362 362 ALA ALA C . n 
A 1 363 ARG 363 363 363 ARG ARG C . n 
A 1 364 ASN 364 364 364 ASN ASN C . n 
A 1 365 ASN 365 365 365 ASN ASN C . n 
A 1 366 PHE 366 366 366 PHE PHE C . n 
A 1 367 PHE 367 367 367 PHE PHE C . n 
A 1 368 SER 368 368 368 SER SER C . n 
A 1 369 SER 369 369 369 SER SER C . n 
A 1 370 ILE 370 370 370 ILE ILE C . n 
A 1 371 LEU 371 371 371 LEU LEU C . n 
A 1 372 ASN 372 372 372 ASN ASN C . n 
A 1 373 VAL 373 373 373 VAL VAL C . n 
A 1 374 VAL 374 374 374 VAL VAL C . n 
A 1 375 PRO 375 375 375 PRO PRO C . n 
A 1 376 ALA 376 376 376 ALA ALA C . n 
A 1 377 GLY 377 377 377 GLY GLY C . n 
A 1 378 LEU 378 378 378 LEU LEU C . n 
A 1 379 ALA 379 379 379 ALA ALA C . n 
A 1 380 ASP 380 380 380 ASP ASP C . n 
A 1 381 LEU 381 381 381 LEU LEU C . n 
A 1 382 LEU 382 382 382 LEU LEU C . n 
A 1 383 ARG 383 383 383 ARG ARG C . n 
A 1 384 SER 384 384 384 SER SER C . n 
A 1 385 LEU 385 385 385 LEU LEU C . n 
A 1 386 GLU 386 386 386 GLU GLU C . n 
A 1 387 ARG 387 387 387 ARG ARG C . n 
A 1 388 ALA 388 388 388 ALA ALA C . n 
A 1 389 GLY 389 389 389 GLY GLY C . n 
A 1 390 VAL 390 390 390 VAL VAL C . n 
A 1 391 ARG 391 391 391 ARG ARG C . n 
A 1 392 TYR 392 392 392 TYR TYR C . n 
A 1 393 ASP 393 393 393 ASP ASP C . n 
A 1 394 LYS 394 394 394 LYS LYS C . n 
A 1 395 ASP 395 395 395 ASP ASP C . n 
A 1 396 SER 396 396 396 SER SER C . n 
A 1 397 GLY 397 397 397 GLY GLY C . n 
A 1 398 GLU 398 398 398 GLU GLU C . n 
A 1 399 GLY 399 399 399 GLY GLY C . n 
A 1 400 ALA 400 400 400 ALA ALA C . n 
A 1 401 VAL 401 401 401 VAL VAL C . n 
A 1 402 VAL 402 402 402 VAL VAL C . n 
A 1 403 LEU 403 403 403 LEU LEU C . n 
A 1 404 GLY 404 404 404 GLY GLY C . n 
A 1 405 CYS 405 405 405 CYS CYS C . n 
A 1 406 ASN 406 406 406 ASN ASN C . n 
A 1 407 SER 407 407 407 SER SER C . n 
A 1 408 ASP 408 408 408 ASP ASP C . n 
A 1 409 LEU 409 409 409 LEU LEU C . n 
A 1 410 GLY 410 410 410 GLY GLY C . n 
A 1 411 PRO 411 411 411 PRO PRO C . n 
A 1 412 GLY 412 412 412 GLY GLY C . n 
A 1 413 ALA 413 413 413 ALA ALA C . n 
A 1 414 GLU 414 414 414 GLU GLU C . n 
A 1 415 LEU 415 415 415 LEU LEU C . n 
A 1 416 LEU 416 416 416 LEU LEU C . n 
A 1 417 VAL 417 417 417 VAL VAL C . n 
A 1 418 PHE 418 418 418 PHE PHE C . n 
A 1 419 SER 419 419 419 SER SER C . n 
A 1 420 LYS 420 420 420 LYS LYS C . n 
A 1 421 ASP 421 421 421 ASP ASP C . n 
A 1 422 TRP 422 422 422 TRP TRP C . n 
A 1 423 ASP 423 423 423 ASP ASP C . n 
A 1 424 ARG 424 424 424 ARG ARG C . n 
A 1 425 LEU 425 425 425 LEU LEU C . n 
A 1 426 THR 426 426 426 THR THR C . n 
A 1 427 ALA 427 427 427 ALA ALA C . n 
A 1 428 MET 428 428 428 MET MET C . n 
A 1 429 LYS 429 429 429 LYS LYS C . n 
A 1 430 ASP 430 430 430 ASP ASP C . n 
A 1 431 GLU 431 431 431 GLU GLU C . n 
A 1 432 ILE 432 432 432 ILE ILE C . n 
A 1 433 ALA 433 433 433 ALA ALA C . n 
A 1 434 THR 434 434 434 THR THR C . n 
A 1 435 THR 435 435 435 THR THR C . n 
A 1 436 ALA 436 436 436 ALA ALA C . n 
A 1 437 GLY 437 437 437 GLY GLY C . n 
A 1 438 THR 438 438 438 THR THR C . n 
A 1 439 LEU 439 439 439 LEU LEU C . n 
A 1 440 SER 440 440 440 SER SER C . n 
A 1 441 LEU 441 441 ?   ?   ?   C . n 
A 1 442 GLU 442 442 ?   ?   ?   C . n 
A 1 443 HIS 443 443 ?   ?   ?   C . n 
A 1 444 HIS 444 444 ?   ?   ?   C . n 
A 1 445 HIS 445 445 ?   ?   ?   C . n 
A 1 446 HIS 446 446 ?   ?   ?   C . n 
A 1 447 HIS 447 447 ?   ?   ?   C . n 
A 1 448 HIS 448 448 ?   ?   ?   C . n 
B 1 1   MET 1   1   ?   ?   ?   D . n 
B 1 2   PRO 2   2   ?   ?   ?   D . n 
B 1 3   LYS 3   3   ?   ?   ?   D . n 
B 1 4   ILE 4   4   ?   ?   ?   D . n 
B 1 5   ILE 5   5   ?   ?   ?   D . n 
B 1 6   LEU 6   6   ?   ?   ?   D . n 
B 1 7   PRO 7   7   ?   ?   ?   D . n 
B 1 8   ASN 8   8   ?   ?   ?   D . n 
B 1 9   PHE 9   9   ?   ?   ?   D . n 
B 1 10  ARG 10  10  ?   ?   ?   D . n 
B 1 11  ALA 11  11  ?   ?   ?   D . n 
B 1 12  ASP 12  12  ?   ?   ?   D . n 
B 1 13  TYR 13  13  ?   ?   ?   D . n 
B 1 14  SER 14  14  ?   ?   ?   D . n 
B 1 15  GLU 15  15  ?   ?   ?   D . n 
B 1 16  GLN 16  16  ?   ?   ?   D . n 
B 1 17  VAL 17  17  ?   ?   ?   D . n 
B 1 18  ARG 18  18  ?   ?   ?   D . n 
B 1 19  ASP 19  19  ?   ?   ?   D . n 
B 1 20  TRP 20  20  ?   ?   ?   D . n 
B 1 21  LEU 21  21  ?   ?   ?   D . n 
B 1 22  GLY 22  22  ?   ?   ?   D . n 
B 1 23  ILE 23  23  ?   ?   ?   D . n 
B 1 24  SER 24  24  ?   ?   ?   D . n 
B 1 25  ASP 25  25  ?   ?   ?   D . n 
B 1 26  ALA 26  26  ?   ?   ?   D . n 
B 1 27  THR 27  27  ?   ?   ?   D . n 
B 1 28  ALA 28  28  ?   ?   ?   D . n 
B 1 29  SER 29  29  ?   ?   ?   D . n 
B 1 30  SER 30  30  30  SER SER D . n 
B 1 31  THR 31  31  31  THR THR D . n 
B 1 32  ASP 32  32  32  ASP ASP D . n 
B 1 33  THR 33  33  33  THR THR D . n 
B 1 34  THR 34  34  34  THR THR D . n 
B 1 35  ALA 35  35  35  ALA ALA D . n 
B 1 36  ARG 36  36  36  ARG ARG D . n 
B 1 37  PHE 37  37  37  PHE PHE D . n 
B 1 38  LEU 38  38  38  LEU LEU D . n 
B 1 39  TRP 39  39  39  TRP TRP D . n 
B 1 40  HIS 40  40  40  HIS HIS D . n 
B 1 41  ALA 41  41  41  ALA ALA D . n 
B 1 42  GLU 42  42  42  GLU GLU D . n 
B 1 43  ASP 43  43  43  ASP ASP D . n 
B 1 44  GLY 44  44  44  GLY GLY D . n 
B 1 45  ASP 45  45  45  ASP ASP D . n 
B 1 46  VAL 46  46  46  VAL VAL D . n 
B 1 47  LEU 47  47  47  LEU LEU D . n 
B 1 48  VAL 48  48  48  VAL VAL D . n 
B 1 49  ILE 49  49  49  ILE ILE D . n 
B 1 50  PRO 50  50  50  PRO PRO D . n 
B 1 51  ASP 51  51  51  ASP ASP D . n 
B 1 52  THR 52  52  52  THR THR D . n 
B 1 53  VAL 53  53  53  VAL VAL D . n 
B 1 54  ASP 54  54  54  ASP ASP D . n 
B 1 55  PRO 55  55  55  PRO PRO D . n 
B 1 56  ASP 56  56  56  ASP ASP D . n 
B 1 57  PHE 57  57  57  PHE PHE D . n 
B 1 58  PRO 58  58  58  PRO PRO D . n 
B 1 59  GLY 59  59  59  GLY GLY D . n 
B 1 60  TYR 60  60  60  TYR TYR D . n 
B 1 61  VAL 61  61  61  VAL VAL D . n 
B 1 62  ALA 62  62  62  ALA ALA D . n 
B 1 63  ASP 63  63  63  ASP ASP D . n 
B 1 64  THR 64  64  64  THR THR D . n 
B 1 65  LEU 65  65  65  LEU LEU D . n 
B 1 66  GLY 66  66  66  GLY GLY D . n 
B 1 67  ILE 67  67  67  ILE ILE D . n 
B 1 68  ASP 68  68  68  ASP ASP D . n 
B 1 69  GLY 69  69  69  GLY GLY D . n 
B 1 70  THR 70  70  70  THR THR D . n 
B 1 71  SER 71  71  71  SER SER D . n 
B 1 72  VAL 72  72  72  VAL VAL D . n 
B 1 73  HIS 73  73  73  HIS HIS D . n 
B 1 74  VAL 74  74  74  VAL VAL D . n 
B 1 75  GLU 75  75  75  GLU GLU D . n 
B 1 76  ARG 76  76  76  ARG ARG D . n 
B 1 77  THR 77  77  77  THR THR D . n 
B 1 78  GLN 78  78  78  GLN GLN D . n 
B 1 79  THR 79  79  79  THR THR D . n 
B 1 80  PRO 80  80  80  PRO PRO D . n 
B 1 81  LEU 81  81  81  LEU LEU D . n 
B 1 82  SER 82  82  82  SER SER D . n 
B 1 83  GLU 83  83  83  GLU GLU D . n 
B 1 84  ALA 84  84  84  ALA ALA D . n 
B 1 85  VAL 85  85  85  VAL VAL D . n 
B 1 86  LEU 86  86  86  LEU LEU D . n 
B 1 87  GLN 87  87  87  GLN GLN D . n 
B 1 88  ASP 88  88  88  ASP ASP D . n 
B 1 89  PRO 89  89  89  PRO PRO D . n 
B 1 90  GLU 90  90  90  GLU GLU D . n 
B 1 91  PHE 91  91  91  PHE PHE D . n 
B 1 92  ILE 92  92  92  ILE ILE D . n 
B 1 93  ASP 93  93  93  ASP ASP D . n 
B 1 94  ARG 94  94  94  ARG ARG D . n 
B 1 95  LEU 95  95  95  LEU LEU D . n 
B 1 96  ALA 96  96  96  ALA ALA D . n 
B 1 97  ALA 97  97  97  ALA ALA D . n 
B 1 98  HIS 98  98  98  HIS HIS D . n 
B 1 99  THR 99  99  99  THR THR D . n 
B 1 100 GLY 100 100 100 GLY GLY D . n 
B 1 101 THR 101 101 101 THR THR D . n 
B 1 102 GLY 102 102 102 GLY GLY D . n 
B 1 103 ALA 103 103 103 ALA ALA D . n 
B 1 104 GLY 104 104 104 GLY GLY D . n 
B 1 105 TRP 105 105 105 TRP TRP D . n 
B 1 106 SER 106 106 106 SER SER D . n 
B 1 107 LEU 107 107 107 LEU LEU D . n 
B 1 108 PHE 108 108 108 PHE PHE D . n 
B 1 109 PRO 109 109 109 PRO PRO D . n 
B 1 110 CYS 110 110 110 CYS CYS D . n 
B 1 111 VAL 111 111 111 VAL VAL D . n 
B 1 112 SER 112 112 112 SER SER D . n 
B 1 113 THR 113 113 113 THR THR D . n 
B 1 114 ARG 114 114 114 ARG ARG D . n 
B 1 115 ALA 115 115 115 ALA ALA D . n 
B 1 116 ALA 116 116 116 ALA ALA D . n 
B 1 117 ALA 117 117 117 ALA ALA D . n 
B 1 118 GLN 118 118 118 GLN GLN D . n 
B 1 119 LEU 119 119 119 LEU LEU D . n 
B 1 120 THR 120 120 120 THR THR D . n 
B 1 121 ARG 121 121 121 ARG ARG D . n 
B 1 122 LYS 122 122 122 LYS LYS D . n 
B 1 123 LEU 123 123 123 LEU LEU D . n 
B 1 124 ASN 124 124 124 ASN ASN D . n 
B 1 125 VAL 125 125 125 VAL VAL D . n 
B 1 126 ALA 126 126 126 ALA ALA D . n 
B 1 127 ALA 127 127 127 ALA ALA D . n 
B 1 128 LEU 128 128 128 LEU LEU D . n 
B 1 129 ASP 129 129 129 ASP ASP D . n 
B 1 130 GLY 130 130 130 GLY GLY D . n 
B 1 131 TYR 131 131 131 TYR TYR D . n 
B 1 132 GLU 132 132 132 GLU GLU D . n 
B 1 133 PHE 133 133 133 PHE PHE D . n 
B 1 134 ALA 134 134 134 ALA ALA D . n 
B 1 135 MET 135 135 135 MET MET D . n 
B 1 136 GLN 136 136 136 GLN GLN D . n 
B 1 137 ASN 137 137 137 ASN ASN D . n 
B 1 138 GLY 138 138 138 GLY GLY D . n 
B 1 139 ILE 139 139 139 ILE ILE D . n 
B 1 140 ASP 140 140 140 ASP ASP D . n 
B 1 141 LEU 141 141 141 LEU LEU D . n 
B 1 142 LEU 142 142 142 LEU LEU D . n 
B 1 143 ASN 143 143 143 ASN ASN D . n 
B 1 144 MET 144 144 144 MET MET D . n 
B 1 145 LYS 145 145 145 LYS LYS D . n 
B 1 146 SER 146 146 146 SER SER D . n 
B 1 147 THR 147 147 147 THR THR D . n 
B 1 148 PHE 148 148 148 PHE PHE D . n 
B 1 149 ARG 149 149 149 ARG ARG D . n 
B 1 150 ARG 150 150 150 ARG ARG D . n 
B 1 151 LEU 151 151 151 LEU LEU D . n 
B 1 152 ALA 152 152 152 ALA ALA D . n 
B 1 153 ALA 153 153 153 ALA ALA D . n 
B 1 154 GLY 154 154 154 GLY GLY D . n 
B 1 155 LEU 155 155 155 LEU LEU D . n 
B 1 156 GLY 156 156 156 GLY GLY D . n 
B 1 157 THR 157 157 157 THR THR D . n 
B 1 158 PRO 158 158 158 PRO PRO D . n 
B 1 159 LEU 159 159 159 LEU LEU D . n 
B 1 160 THR 160 160 160 THR THR D . n 
B 1 161 ASP 161 161 161 ASP ASP D . n 
B 1 162 GLY 162 162 162 GLY GLY D . n 
B 1 163 VAL 163 163 163 VAL VAL D . n 
B 1 164 VAL 164 164 164 VAL VAL D . n 
B 1 165 ALA 165 165 165 ALA ALA D . n 
B 1 166 ARG 166 166 166 ARG ARG D . n 
B 1 167 GLY 167 167 167 GLY GLY D . n 
B 1 168 PRO 168 168 168 PRO PRO D . n 
B 1 169 ALA 169 169 169 ALA ALA D . n 
B 1 170 GLU 170 170 170 GLU GLU D . n 
B 1 171 VAL 171 171 171 VAL VAL D . n 
B 1 172 ARG 172 172 172 ARG ARG D . n 
B 1 173 SER 173 173 173 SER SER D . n 
B 1 174 ALA 174 174 174 ALA ALA D . n 
B 1 175 ILE 175 175 175 ILE ILE D . n 
B 1 176 GLN 176 176 176 GLN GLN D . n 
B 1 177 GLU 177 177 177 GLU GLU D . n 
B 1 178 LEU 178 178 178 LEU LEU D . n 
B 1 179 ILE 179 179 179 ILE ILE D . n 
B 1 180 ALA 180 180 180 ALA ALA D . n 
B 1 181 GLU 181 181 181 GLU GLU D . n 
B 1 182 THR 182 182 182 THR THR D . n 
B 1 183 GLY 183 183 183 GLY GLY D . n 
B 1 184 MET 184 184 184 MET MET D . n 
B 1 185 VAL 185 185 185 VAL VAL D . n 
B 1 186 ILE 186 186 186 ILE ILE D . n 
B 1 187 ALA 187 187 187 ALA ALA D . n 
B 1 188 LYS 188 188 188 LYS LYS D . n 
B 1 189 GLN 189 189 189 GLN GLN D . n 
B 1 190 ASP 190 190 190 ASP ASP D . n 
B 1 191 ARG 191 191 191 ARG ARG D . n 
B 1 192 SER 192 192 192 SER SER D . n 
B 1 193 GLY 193 193 193 GLY GLY D . n 
B 1 194 GLY 194 194 194 GLY GLY D . n 
B 1 195 GLY 195 195 195 GLY GLY D . n 
B 1 196 HIS 196 196 196 HIS HIS D . n 
B 1 197 GLY 197 197 197 GLY GLY D . n 
B 1 198 ASN 198 198 198 ASN ASN D . n 
B 1 199 ILE 199 199 199 ILE ILE D . n 
B 1 200 GLY 200 200 200 GLY GLY D . n 
B 1 201 ILE 201 201 201 ILE ILE D . n 
B 1 202 SER 202 202 202 SER SER D . n 
B 1 203 THR 203 203 203 THR THR D . n 
B 1 204 SER 204 204 204 SER SER D . n 
B 1 205 PRO 205 205 205 PRO PRO D . n 
B 1 206 GLU 206 206 206 GLU GLU D . n 
B 1 207 SER 207 207 207 SER SER D . n 
B 1 208 SER 208 208 208 SER SER D . n 
B 1 209 PHE 209 209 209 PHE PHE D . n 
B 1 210 PRO 210 210 210 PRO PRO D . n 
B 1 211 GLY 211 211 211 GLY GLY D . n 
B 1 212 THR 212 212 212 THR THR D . n 
B 1 213 ARG 213 213 213 ARG ARG D . n 
B 1 214 GLU 214 214 214 GLU GLU D . n 
B 1 215 VAL 215 215 215 VAL VAL D . n 
B 1 216 LEU 216 216 216 LEU LEU D . n 
B 1 217 ALA 217 217 217 ALA ALA D . n 
B 1 218 TYR 218 218 218 TYR TYR D . n 
B 1 219 ALA 219 219 219 ALA ALA D . n 
B 1 220 ASN 220 220 220 ASN ASN D . n 
B 1 221 ASP 221 221 221 ASP ASP D . n 
B 1 222 GLN 222 222 222 GLN GLN D . n 
B 1 223 LEU 223 223 223 LEU LEU D . n 
B 1 224 ASP 224 224 224 ASP ASP D . n 
B 1 225 THR 225 225 225 THR THR D . n 
B 1 226 LEU 226 226 226 LEU LEU D . n 
B 1 227 ALA 227 227 227 ALA ALA D . n 
B 1 228 ASP 228 228 228 ASP ASP D . n 
B 1 229 THR 229 229 229 THR THR D . n 
B 1 230 LEU 230 230 230 LEU LEU D . n 
B 1 231 TRP 231 231 231 TRP TRP D . n 
B 1 232 SER 232 232 232 SER SER D . n 
B 1 233 GLN 233 233 233 GLN GLN D . n 
B 1 234 LEU 234 234 234 LEU LEU D . n 
B 1 235 THR 235 235 235 THR THR D . n 
B 1 236 ASP 236 236 236 ASP ASP D . n 
B 1 237 THR 237 237 237 THR THR D . n 
B 1 238 GLN 238 238 238 GLN GLN D . n 
B 1 239 ASN 239 239 239 ASN ASN D . n 
B 1 240 GLN 240 240 240 GLN GLN D . n 
B 1 241 PHE 241 241 241 PHE PHE D . n 
B 1 242 ILE 242 242 242 ILE ILE D . n 
B 1 243 THR 243 243 243 THR THR D . n 
B 1 244 VAL 244 244 244 VAL VAL D . n 
B 1 245 GLU 245 245 245 GLU GLU D . n 
B 1 246 THR 246 246 246 THR THR D . n 
B 1 247 TYR 247 247 247 TYR TYR D . n 
B 1 248 HIS 248 248 248 HIS HIS D . n 
B 1 249 ARG 249 249 249 ARG ARG D . n 
B 1 250 ALA 250 250 250 ALA ALA D . n 
B 1 251 ASP 251 251 251 ASP ASP D . n 
B 1 252 GLN 252 252 252 GLN GLN D . n 
B 1 253 ARG 253 253 253 ARG ARG D . n 
B 1 254 PHE 254 254 254 PHE PHE D . n 
B 1 255 PHE 255 255 255 PHE PHE D . n 
B 1 256 PHE 256 256 256 PHE PHE D . n 
B 1 257 GLU 257 257 257 GLU GLU D . n 
B 1 258 TYR 258 258 258 TYR TYR D . n 
B 1 259 HIS 259 259 259 HIS HIS D . n 
B 1 260 LEU 260 260 260 LEU LEU D . n 
B 1 261 ASP 261 261 261 ASP ASP D . n 
B 1 262 GLY 262 262 262 GLY GLY D . n 
B 1 263 ASP 263 263 263 ASP ASP D . n 
B 1 264 ARG 264 264 264 ARG ARG D . n 
B 1 265 ALA 265 265 265 ALA ALA D . n 
B 1 266 ARG 266 266 266 ARG ARG D . n 
B 1 267 PHE 267 267 267 PHE PHE D . n 
B 1 268 LEU 268 268 268 LEU LEU D . n 
B 1 269 HIS 269 269 269 HIS HIS D . n 
B 1 270 SER 270 270 270 SER SER D . n 
B 1 271 SER 271 271 271 SER SER D . n 
B 1 272 ILE 272 272 272 ILE ILE D . n 
B 1 273 LEU 273 273 273 LEU LEU D . n 
B 1 274 LYS 274 274 274 LYS LYS D . n 
B 1 275 TYR 275 275 275 TYR TYR D . n 
B 1 276 GLU 276 276 276 GLU GLU D . n 
B 1 277 GLN 277 277 277 GLN GLN D . n 
B 1 278 LEU 278 278 278 LEU LEU D . n 
B 1 279 PRO 279 279 279 PRO PRO D . n 
B 1 280 GLU 280 280 280 GLU GLU D . n 
B 1 281 GLY 281 281 ?   ?   ?   D . n 
B 1 282 SER 282 282 ?   ?   ?   D . n 
B 1 283 GLY 283 283 ?   ?   ?   D . n 
B 1 284 GLY 284 284 ?   ?   ?   D . n 
B 1 285 SER 285 285 285 SER SER D . n 
B 1 286 ALA 286 286 286 ALA ALA D . n 
B 1 287 LYS 287 287 287 LYS LYS D . n 
B 1 288 TRP 288 288 288 TRP TRP D . n 
B 1 289 ILE 289 289 289 ILE ILE D . n 
B 1 290 GLY 290 290 290 GLY GLY D . n 
B 1 291 LEU 291 291 291 LEU LEU D . n 
B 1 292 ASP 292 292 292 ASP ASP D . n 
B 1 293 SER 293 293 293 SER SER D . n 
B 1 294 PRO 294 294 294 PRO PRO D . n 
B 1 295 SER 295 295 295 SER SER D . n 
B 1 296 ARG 296 296 296 ARG ARG D . n 
B 1 297 SER 297 297 297 SER SER D . n 
B 1 298 GLU 298 298 298 GLU GLU D . n 
B 1 299 PHE 299 299 299 PHE PHE D . n 
B 1 300 GLU 300 300 300 GLU GLU D . n 
B 1 301 ALA 301 301 301 ALA ALA D . n 
B 1 302 THR 302 302 302 THR THR D . n 
B 1 303 LEU 303 303 303 LEU LEU D . n 
B 1 304 LYS 304 304 304 LYS LYS D . n 
B 1 305 PRO 305 305 305 PRO PRO D . n 
B 1 306 ALA 306 306 306 ALA ALA D . n 
B 1 307 GLU 307 307 307 GLU GLU D . n 
B 1 308 GLU 308 308 308 GLU GLU D . n 
B 1 309 PHE 309 309 309 PHE PHE D . n 
B 1 310 ILE 310 310 310 ILE ILE D . n 
B 1 311 GLU 311 311 311 GLU GLU D . n 
B 1 312 MET 312 312 312 MET MET D . n 
B 1 313 ILE 313 313 313 ILE ILE D . n 
B 1 314 ARG 314 314 314 ARG ARG D . n 
B 1 315 THR 315 315 315 THR THR D . n 
B 1 316 ILE 316 316 316 ILE ILE D . n 
B 1 317 GLY 317 317 317 GLY GLY D . n 
B 1 318 TYR 318 318 318 TYR TYR D . n 
B 1 319 ARG 319 319 319 ARG ARG D . n 
B 1 320 GLY 320 320 320 GLY GLY D . n 
B 1 321 TYR 321 321 321 TYR TYR D . n 
B 1 322 VAL 322 322 322 VAL VAL D . n 
B 1 323 ASN 323 323 323 ASN ASN D . n 
B 1 324 ILE 324 324 324 ILE ILE D . n 
B 1 325 ASP 325 325 325 ASP ASP D . n 
B 1 326 GLY 326 326 326 GLY GLY D . n 
B 1 327 ILE 327 327 327 ILE ILE D . n 
B 1 328 VAL 328 328 328 VAL VAL D . n 
B 1 329 LEU 329 329 329 LEU LEU D . n 
B 1 330 ASP 330 330 330 ASP ASP D . n 
B 1 331 ASP 331 331 331 ASP ASP D . n 
B 1 332 GLY 332 332 332 GLY GLY D . n 
B 1 333 ARG 333 333 333 ARG ARG D . n 
B 1 334 VAL 334 334 334 VAL VAL D . n 
B 1 335 PHE 335 335 335 PHE PHE D . n 
B 1 336 PHE 336 336 336 PHE PHE D . n 
B 1 337 HIS 337 337 337 HIS HIS D . n 
B 1 338 GLU 338 338 338 GLU GLU D . n 
B 1 339 ILE 339 339 339 ILE ILE D . n 
B 1 340 ASN 340 340 340 ASN ASN D . n 
B 1 341 ALA 341 341 341 ALA ALA D . n 
B 1 342 ARG 342 342 342 ARG ARG D . n 
B 1 343 TRP 343 343 343 TRP TRP D . n 
B 1 344 SER 344 344 344 SER SER D . n 
B 1 345 GLY 345 345 345 GLY GLY D . n 
B 1 346 GLY 346 346 346 GLY GLY D . n 
B 1 347 LEU 347 347 347 LEU LEU D . n 
B 1 348 ILE 348 348 348 ILE ILE D . n 
B 1 349 TYR 349 349 349 TYR TYR D . n 
B 1 350 HIS 350 350 350 HIS HIS D . n 
B 1 351 THR 351 351 351 THR THR D . n 
B 1 352 VAL 352 352 352 VAL VAL D . n 
B 1 353 ALA 353 353 353 ALA ALA D . n 
B 1 354 GLU 354 354 354 GLU GLU D . n 
B 1 355 ARG 355 355 355 ARG ARG D . n 
B 1 356 LEU 356 356 356 LEU LEU D . n 
B 1 357 LEU 357 357 357 LEU LEU D . n 
B 1 358 GLY 358 358 358 GLY GLY D . n 
B 1 359 HIS 359 359 359 HIS HIS D . n 
B 1 360 ASP 360 360 360 ASP ASP D . n 
B 1 361 TYR 361 361 361 TYR TYR D . n 
B 1 362 ALA 362 362 362 ALA ALA D . n 
B 1 363 ARG 363 363 363 ARG ARG D . n 
B 1 364 ASN 364 364 364 ASN ASN D . n 
B 1 365 ASN 365 365 365 ASN ASN D . n 
B 1 366 PHE 366 366 366 PHE PHE D . n 
B 1 367 PHE 367 367 367 PHE PHE D . n 
B 1 368 SER 368 368 368 SER SER D . n 
B 1 369 SER 369 369 369 SER SER D . n 
B 1 370 ILE 370 370 370 ILE ILE D . n 
B 1 371 LEU 371 371 371 LEU LEU D . n 
B 1 372 ASN 372 372 372 ASN ASN D . n 
B 1 373 VAL 373 373 373 VAL VAL D . n 
B 1 374 VAL 374 374 374 VAL VAL D . n 
B 1 375 PRO 375 375 375 PRO PRO D . n 
B 1 376 ALA 376 376 376 ALA ALA D . n 
B 1 377 GLY 377 377 377 GLY GLY D . n 
B 1 378 LEU 378 378 378 LEU LEU D . n 
B 1 379 ALA 379 379 379 ALA ALA D . n 
B 1 380 ASP 380 380 380 ASP ASP D . n 
B 1 381 LEU 381 381 381 LEU LEU D . n 
B 1 382 LEU 382 382 382 LEU LEU D . n 
B 1 383 ARG 383 383 383 ARG ARG D . n 
B 1 384 SER 384 384 384 SER SER D . n 
B 1 385 LEU 385 385 385 LEU LEU D . n 
B 1 386 GLU 386 386 386 GLU GLU D . n 
B 1 387 ARG 387 387 387 ARG ARG D . n 
B 1 388 ALA 388 388 388 ALA ALA D . n 
B 1 389 GLY 389 389 389 GLY GLY D . n 
B 1 390 VAL 390 390 390 VAL VAL D . n 
B 1 391 ARG 391 391 391 ARG ARG D . n 
B 1 392 TYR 392 392 392 TYR TYR D . n 
B 1 393 ASP 393 393 393 ASP ASP D . n 
B 1 394 LYS 394 394 394 LYS LYS D . n 
B 1 395 ASP 395 395 395 ASP ASP D . n 
B 1 396 SER 396 396 396 SER SER D . n 
B 1 397 GLY 397 397 397 GLY GLY D . n 
B 1 398 GLU 398 398 398 GLU GLU D . n 
B 1 399 GLY 399 399 399 GLY GLY D . n 
B 1 400 ALA 400 400 400 ALA ALA D . n 
B 1 401 VAL 401 401 401 VAL VAL D . n 
B 1 402 VAL 402 402 402 VAL VAL D . n 
B 1 403 LEU 403 403 403 LEU LEU D . n 
B 1 404 GLY 404 404 404 GLY GLY D . n 
B 1 405 CYS 405 405 405 CYS CYS D . n 
B 1 406 ASN 406 406 406 ASN ASN D . n 
B 1 407 SER 407 407 407 SER SER D . n 
B 1 408 ASP 408 408 408 ASP ASP D . n 
B 1 409 LEU 409 409 409 LEU LEU D . n 
B 1 410 GLY 410 410 410 GLY GLY D . n 
B 1 411 PRO 411 411 411 PRO PRO D . n 
B 1 412 GLY 412 412 412 GLY GLY D . n 
B 1 413 ALA 413 413 413 ALA ALA D . n 
B 1 414 GLU 414 414 414 GLU GLU D . n 
B 1 415 LEU 415 415 415 LEU LEU D . n 
B 1 416 LEU 416 416 416 LEU LEU D . n 
B 1 417 VAL 417 417 417 VAL VAL D . n 
B 1 418 PHE 418 418 418 PHE PHE D . n 
B 1 419 SER 419 419 419 SER SER D . n 
B 1 420 LYS 420 420 420 LYS LYS D . n 
B 1 421 ASP 421 421 421 ASP ASP D . n 
B 1 422 TRP 422 422 422 TRP TRP D . n 
B 1 423 ASP 423 423 423 ASP ASP D . n 
B 1 424 ARG 424 424 424 ARG ARG D . n 
B 1 425 LEU 425 425 425 LEU LEU D . n 
B 1 426 THR 426 426 426 THR THR D . n 
B 1 427 ALA 427 427 427 ALA ALA D . n 
B 1 428 MET 428 428 428 MET MET D . n 
B 1 429 LYS 429 429 429 LYS LYS D . n 
B 1 430 ASP 430 430 430 ASP ASP D . n 
B 1 431 GLU 431 431 431 GLU GLU D . n 
B 1 432 ILE 432 432 432 ILE ILE D . n 
B 1 433 ALA 433 433 433 ALA ALA D . n 
B 1 434 THR 434 434 434 THR THR D . n 
B 1 435 THR 435 435 435 THR THR D . n 
B 1 436 ALA 436 436 436 ALA ALA D . n 
B 1 437 GLY 437 437 437 GLY GLY D . n 
B 1 438 THR 438 438 438 THR THR D . n 
B 1 439 LEU 439 439 439 LEU LEU D . n 
B 1 440 SER 440 440 440 SER SER D . n 
B 1 441 LEU 441 441 ?   ?   ?   D . n 
B 1 442 GLU 442 442 ?   ?   ?   D . n 
B 1 443 HIS 443 443 ?   ?   ?   D . n 
B 1 444 HIS 444 444 ?   ?   ?   D . n 
B 1 445 HIS 445 445 ?   ?   ?   D . n 
B 1 446 HIS 446 446 ?   ?   ?   D . n 
B 1 447 HIS 447 447 ?   ?   ?   D . n 
B 1 448 HIS 448 448 ?   ?   ?   D . n 
C 1 1   MET 1   1   ?   ?   ?   A . n 
C 1 2   PRO 2   2   ?   ?   ?   A . n 
C 1 3   LYS 3   3   ?   ?   ?   A . n 
C 1 4   ILE 4   4   ?   ?   ?   A . n 
C 1 5   ILE 5   5   ?   ?   ?   A . n 
C 1 6   LEU 6   6   ?   ?   ?   A . n 
C 1 7   PRO 7   7   ?   ?   ?   A . n 
C 1 8   ASN 8   8   ?   ?   ?   A . n 
C 1 9   PHE 9   9   ?   ?   ?   A . n 
C 1 10  ARG 10  10  ?   ?   ?   A . n 
C 1 11  ALA 11  11  ?   ?   ?   A . n 
C 1 12  ASP 12  12  ?   ?   ?   A . n 
C 1 13  TYR 13  13  ?   ?   ?   A . n 
C 1 14  SER 14  14  ?   ?   ?   A . n 
C 1 15  GLU 15  15  ?   ?   ?   A . n 
C 1 16  GLN 16  16  ?   ?   ?   A . n 
C 1 17  VAL 17  17  ?   ?   ?   A . n 
C 1 18  ARG 18  18  ?   ?   ?   A . n 
C 1 19  ASP 19  19  ?   ?   ?   A . n 
C 1 20  TRP 20  20  ?   ?   ?   A . n 
C 1 21  LEU 21  21  ?   ?   ?   A . n 
C 1 22  GLY 22  22  ?   ?   ?   A . n 
C 1 23  ILE 23  23  ?   ?   ?   A . n 
C 1 24  SER 24  24  ?   ?   ?   A . n 
C 1 25  ASP 25  25  ?   ?   ?   A . n 
C 1 26  ALA 26  26  ?   ?   ?   A . n 
C 1 27  THR 27  27  ?   ?   ?   A . n 
C 1 28  ALA 28  28  ?   ?   ?   A . n 
C 1 29  SER 29  29  ?   ?   ?   A . n 
C 1 30  SER 30  30  30  SER SER A . n 
C 1 31  THR 31  31  31  THR THR A . n 
C 1 32  ASP 32  32  32  ASP ASP A . n 
C 1 33  THR 33  33  33  THR THR A . n 
C 1 34  THR 34  34  34  THR THR A . n 
C 1 35  ALA 35  35  35  ALA ALA A . n 
C 1 36  ARG 36  36  36  ARG ARG A . n 
C 1 37  PHE 37  37  37  PHE PHE A . n 
C 1 38  LEU 38  38  38  LEU LEU A . n 
C 1 39  TRP 39  39  39  TRP TRP A . n 
C 1 40  HIS 40  40  40  HIS HIS A . n 
C 1 41  ALA 41  41  41  ALA ALA A . n 
C 1 42  GLU 42  42  42  GLU GLU A . n 
C 1 43  ASP 43  43  43  ASP ASP A . n 
C 1 44  GLY 44  44  44  GLY GLY A . n 
C 1 45  ASP 45  45  45  ASP ASP A . n 
C 1 46  VAL 46  46  46  VAL VAL A . n 
C 1 47  LEU 47  47  47  LEU LEU A . n 
C 1 48  VAL 48  48  48  VAL VAL A . n 
C 1 49  ILE 49  49  49  ILE ILE A . n 
C 1 50  PRO 50  50  50  PRO PRO A . n 
C 1 51  ASP 51  51  51  ASP ASP A . n 
C 1 52  THR 52  52  52  THR THR A . n 
C 1 53  VAL 53  53  53  VAL VAL A . n 
C 1 54  ASP 54  54  54  ASP ASP A . n 
C 1 55  PRO 55  55  55  PRO PRO A . n 
C 1 56  ASP 56  56  56  ASP ASP A . n 
C 1 57  PHE 57  57  57  PHE PHE A . n 
C 1 58  PRO 58  58  58  PRO PRO A . n 
C 1 59  GLY 59  59  59  GLY GLY A . n 
C 1 60  TYR 60  60  60  TYR TYR A . n 
C 1 61  VAL 61  61  61  VAL VAL A . n 
C 1 62  ALA 62  62  62  ALA ALA A . n 
C 1 63  ASP 63  63  63  ASP ASP A . n 
C 1 64  THR 64  64  64  THR THR A . n 
C 1 65  LEU 65  65  65  LEU LEU A . n 
C 1 66  GLY 66  66  66  GLY GLY A . n 
C 1 67  ILE 67  67  67  ILE ILE A . n 
C 1 68  ASP 68  68  68  ASP ASP A . n 
C 1 69  GLY 69  69  69  GLY GLY A . n 
C 1 70  THR 70  70  70  THR THR A . n 
C 1 71  SER 71  71  71  SER SER A . n 
C 1 72  VAL 72  72  72  VAL VAL A . n 
C 1 73  HIS 73  73  73  HIS HIS A . n 
C 1 74  VAL 74  74  74  VAL VAL A . n 
C 1 75  GLU 75  75  75  GLU GLU A . n 
C 1 76  ARG 76  76  76  ARG ARG A . n 
C 1 77  THR 77  77  77  THR THR A . n 
C 1 78  GLN 78  78  78  GLN GLN A . n 
C 1 79  THR 79  79  79  THR THR A . n 
C 1 80  PRO 80  80  80  PRO PRO A . n 
C 1 81  LEU 81  81  81  LEU LEU A . n 
C 1 82  SER 82  82  82  SER SER A . n 
C 1 83  GLU 83  83  83  GLU GLU A . n 
C 1 84  ALA 84  84  84  ALA ALA A . n 
C 1 85  VAL 85  85  85  VAL VAL A . n 
C 1 86  LEU 86  86  86  LEU LEU A . n 
C 1 87  GLN 87  87  87  GLN GLN A . n 
C 1 88  ASP 88  88  88  ASP ASP A . n 
C 1 89  PRO 89  89  89  PRO PRO A . n 
C 1 90  GLU 90  90  90  GLU GLU A . n 
C 1 91  PHE 91  91  91  PHE PHE A . n 
C 1 92  ILE 92  92  92  ILE ILE A . n 
C 1 93  ASP 93  93  93  ASP ASP A . n 
C 1 94  ARG 94  94  94  ARG ARG A . n 
C 1 95  LEU 95  95  95  LEU LEU A . n 
C 1 96  ALA 96  96  96  ALA ALA A . n 
C 1 97  ALA 97  97  97  ALA ALA A . n 
C 1 98  HIS 98  98  98  HIS HIS A . n 
C 1 99  THR 99  99  99  THR THR A . n 
C 1 100 GLY 100 100 100 GLY GLY A . n 
C 1 101 THR 101 101 101 THR THR A . n 
C 1 102 GLY 102 102 102 GLY GLY A . n 
C 1 103 ALA 103 103 103 ALA ALA A . n 
C 1 104 GLY 104 104 104 GLY GLY A . n 
C 1 105 TRP 105 105 105 TRP TRP A . n 
C 1 106 SER 106 106 106 SER SER A . n 
C 1 107 LEU 107 107 107 LEU LEU A . n 
C 1 108 PHE 108 108 108 PHE PHE A . n 
C 1 109 PRO 109 109 109 PRO PRO A . n 
C 1 110 CYS 110 110 110 CYS CYS A . n 
C 1 111 VAL 111 111 111 VAL VAL A . n 
C 1 112 SER 112 112 112 SER SER A . n 
C 1 113 THR 113 113 113 THR THR A . n 
C 1 114 ARG 114 114 114 ARG ARG A . n 
C 1 115 ALA 115 115 115 ALA ALA A . n 
C 1 116 ALA 116 116 116 ALA ALA A . n 
C 1 117 ALA 117 117 117 ALA ALA A . n 
C 1 118 GLN 118 118 118 GLN GLN A . n 
C 1 119 LEU 119 119 119 LEU LEU A . n 
C 1 120 THR 120 120 120 THR THR A . n 
C 1 121 ARG 121 121 121 ARG ARG A . n 
C 1 122 LYS 122 122 122 LYS LYS A . n 
C 1 123 LEU 123 123 123 LEU LEU A . n 
C 1 124 ASN 124 124 124 ASN ASN A . n 
C 1 125 VAL 125 125 125 VAL VAL A . n 
C 1 126 ALA 126 126 126 ALA ALA A . n 
C 1 127 ALA 127 127 127 ALA ALA A . n 
C 1 128 LEU 128 128 128 LEU LEU A . n 
C 1 129 ASP 129 129 129 ASP ASP A . n 
C 1 130 GLY 130 130 130 GLY GLY A . n 
C 1 131 TYR 131 131 131 TYR TYR A . n 
C 1 132 GLU 132 132 132 GLU GLU A . n 
C 1 133 PHE 133 133 133 PHE PHE A . n 
C 1 134 ALA 134 134 134 ALA ALA A . n 
C 1 135 MET 135 135 135 MET MET A . n 
C 1 136 GLN 136 136 136 GLN GLN A . n 
C 1 137 ASN 137 137 137 ASN ASN A . n 
C 1 138 GLY 138 138 138 GLY GLY A . n 
C 1 139 ILE 139 139 139 ILE ILE A . n 
C 1 140 ASP 140 140 140 ASP ASP A . n 
C 1 141 LEU 141 141 141 LEU LEU A . n 
C 1 142 LEU 142 142 142 LEU LEU A . n 
C 1 143 ASN 143 143 143 ASN ASN A . n 
C 1 144 MET 144 144 144 MET MET A . n 
C 1 145 LYS 145 145 145 LYS LYS A . n 
C 1 146 SER 146 146 146 SER SER A . n 
C 1 147 THR 147 147 147 THR THR A . n 
C 1 148 PHE 148 148 148 PHE PHE A . n 
C 1 149 ARG 149 149 149 ARG ARG A . n 
C 1 150 ARG 150 150 150 ARG ARG A . n 
C 1 151 LEU 151 151 151 LEU LEU A . n 
C 1 152 ALA 152 152 152 ALA ALA A . n 
C 1 153 ALA 153 153 153 ALA ALA A . n 
C 1 154 GLY 154 154 154 GLY GLY A . n 
C 1 155 LEU 155 155 155 LEU LEU A . n 
C 1 156 GLY 156 156 156 GLY GLY A . n 
C 1 157 THR 157 157 157 THR THR A . n 
C 1 158 PRO 158 158 158 PRO PRO A . n 
C 1 159 LEU 159 159 159 LEU LEU A . n 
C 1 160 THR 160 160 160 THR THR A . n 
C 1 161 ASP 161 161 161 ASP ASP A . n 
C 1 162 GLY 162 162 162 GLY GLY A . n 
C 1 163 VAL 163 163 163 VAL VAL A . n 
C 1 164 VAL 164 164 164 VAL VAL A . n 
C 1 165 ALA 165 165 165 ALA ALA A . n 
C 1 166 ARG 166 166 166 ARG ARG A . n 
C 1 167 GLY 167 167 167 GLY GLY A . n 
C 1 168 PRO 168 168 168 PRO PRO A . n 
C 1 169 ALA 169 169 169 ALA ALA A . n 
C 1 170 GLU 170 170 170 GLU GLU A . n 
C 1 171 VAL 171 171 171 VAL VAL A . n 
C 1 172 ARG 172 172 172 ARG ARG A . n 
C 1 173 SER 173 173 173 SER SER A . n 
C 1 174 ALA 174 174 174 ALA ALA A . n 
C 1 175 ILE 175 175 175 ILE ILE A . n 
C 1 176 GLN 176 176 176 GLN GLN A . n 
C 1 177 GLU 177 177 177 GLU GLU A . n 
C 1 178 LEU 178 178 178 LEU LEU A . n 
C 1 179 ILE 179 179 179 ILE ILE A . n 
C 1 180 ALA 180 180 180 ALA ALA A . n 
C 1 181 GLU 181 181 181 GLU GLU A . n 
C 1 182 THR 182 182 182 THR THR A . n 
C 1 183 GLY 183 183 183 GLY GLY A . n 
C 1 184 MET 184 184 184 MET MET A . n 
C 1 185 VAL 185 185 185 VAL VAL A . n 
C 1 186 ILE 186 186 186 ILE ILE A . n 
C 1 187 ALA 187 187 187 ALA ALA A . n 
C 1 188 LYS 188 188 188 LYS LYS A . n 
C 1 189 GLN 189 189 189 GLN GLN A . n 
C 1 190 ASP 190 190 190 ASP ASP A . n 
C 1 191 ARG 191 191 191 ARG ARG A . n 
C 1 192 SER 192 192 192 SER SER A . n 
C 1 193 GLY 193 193 193 GLY GLY A . n 
C 1 194 GLY 194 194 194 GLY GLY A . n 
C 1 195 GLY 195 195 195 GLY GLY A . n 
C 1 196 HIS 196 196 196 HIS HIS A . n 
C 1 197 GLY 197 197 197 GLY GLY A . n 
C 1 198 ASN 198 198 198 ASN ASN A . n 
C 1 199 ILE 199 199 199 ILE ILE A . n 
C 1 200 GLY 200 200 200 GLY GLY A . n 
C 1 201 ILE 201 201 201 ILE ILE A . n 
C 1 202 SER 202 202 202 SER SER A . n 
C 1 203 THR 203 203 203 THR THR A . n 
C 1 204 SER 204 204 204 SER SER A . n 
C 1 205 PRO 205 205 205 PRO PRO A . n 
C 1 206 GLU 206 206 206 GLU GLU A . n 
C 1 207 SER 207 207 207 SER SER A . n 
C 1 208 SER 208 208 208 SER SER A . n 
C 1 209 PHE 209 209 209 PHE PHE A . n 
C 1 210 PRO 210 210 210 PRO PRO A . n 
C 1 211 GLY 211 211 211 GLY GLY A . n 
C 1 212 THR 212 212 212 THR THR A . n 
C 1 213 ARG 213 213 213 ARG ARG A . n 
C 1 214 GLU 214 214 214 GLU GLU A . n 
C 1 215 VAL 215 215 215 VAL VAL A . n 
C 1 216 LEU 216 216 216 LEU LEU A . n 
C 1 217 ALA 217 217 217 ALA ALA A . n 
C 1 218 TYR 218 218 218 TYR TYR A . n 
C 1 219 ALA 219 219 219 ALA ALA A . n 
C 1 220 ASN 220 220 220 ASN ASN A . n 
C 1 221 ASP 221 221 221 ASP ASP A . n 
C 1 222 GLN 222 222 222 GLN GLN A . n 
C 1 223 LEU 223 223 223 LEU LEU A . n 
C 1 224 ASP 224 224 224 ASP ASP A . n 
C 1 225 THR 225 225 225 THR THR A . n 
C 1 226 LEU 226 226 226 LEU LEU A . n 
C 1 227 ALA 227 227 227 ALA ALA A . n 
C 1 228 ASP 228 228 228 ASP ASP A . n 
C 1 229 THR 229 229 229 THR THR A . n 
C 1 230 LEU 230 230 230 LEU LEU A . n 
C 1 231 TRP 231 231 231 TRP TRP A . n 
C 1 232 SER 232 232 232 SER SER A . n 
C 1 233 GLN 233 233 233 GLN GLN A . n 
C 1 234 LEU 234 234 234 LEU LEU A . n 
C 1 235 THR 235 235 235 THR THR A . n 
C 1 236 ASP 236 236 236 ASP ASP A . n 
C 1 237 THR 237 237 237 THR THR A . n 
C 1 238 GLN 238 238 238 GLN GLN A . n 
C 1 239 ASN 239 239 239 ASN ASN A . n 
C 1 240 GLN 240 240 240 GLN GLN A . n 
C 1 241 PHE 241 241 241 PHE PHE A . n 
C 1 242 ILE 242 242 242 ILE ILE A . n 
C 1 243 THR 243 243 243 THR THR A . n 
C 1 244 VAL 244 244 244 VAL VAL A . n 
C 1 245 GLU 245 245 245 GLU GLU A . n 
C 1 246 THR 246 246 246 THR THR A . n 
C 1 247 TYR 247 247 247 TYR TYR A . n 
C 1 248 HIS 248 248 248 HIS HIS A . n 
C 1 249 ARG 249 249 249 ARG ARG A . n 
C 1 250 ALA 250 250 250 ALA ALA A . n 
C 1 251 ASP 251 251 251 ASP ASP A . n 
C 1 252 GLN 252 252 252 GLN GLN A . n 
C 1 253 ARG 253 253 253 ARG ARG A . n 
C 1 254 PHE 254 254 254 PHE PHE A . n 
C 1 255 PHE 255 255 255 PHE PHE A . n 
C 1 256 PHE 256 256 256 PHE PHE A . n 
C 1 257 GLU 257 257 257 GLU GLU A . n 
C 1 258 TYR 258 258 258 TYR TYR A . n 
C 1 259 HIS 259 259 259 HIS HIS A . n 
C 1 260 LEU 260 260 260 LEU LEU A . n 
C 1 261 ASP 261 261 261 ASP ASP A . n 
C 1 262 GLY 262 262 262 GLY GLY A . n 
C 1 263 ASP 263 263 263 ASP ASP A . n 
C 1 264 ARG 264 264 264 ARG ARG A . n 
C 1 265 ALA 265 265 265 ALA ALA A . n 
C 1 266 ARG 266 266 266 ARG ARG A . n 
C 1 267 PHE 267 267 267 PHE PHE A . n 
C 1 268 LEU 268 268 268 LEU LEU A . n 
C 1 269 HIS 269 269 269 HIS HIS A . n 
C 1 270 SER 270 270 270 SER SER A . n 
C 1 271 SER 271 271 271 SER SER A . n 
C 1 272 ILE 272 272 272 ILE ILE A . n 
C 1 273 LEU 273 273 273 LEU LEU A . n 
C 1 274 LYS 274 274 274 LYS LYS A . n 
C 1 275 TYR 275 275 275 TYR TYR A . n 
C 1 276 GLU 276 276 276 GLU GLU A . n 
C 1 277 GLN 277 277 277 GLN GLN A . n 
C 1 278 LEU 278 278 278 LEU LEU A . n 
C 1 279 PRO 279 279 279 PRO PRO A . n 
C 1 280 GLU 280 280 280 GLU GLU A . n 
C 1 281 GLY 281 281 ?   ?   ?   A . n 
C 1 282 SER 282 282 282 SER SER A . n 
C 1 283 GLY 283 283 283 GLY GLY A . n 
C 1 284 GLY 284 284 284 GLY GLY A . n 
C 1 285 SER 285 285 285 SER SER A . n 
C 1 286 ALA 286 286 286 ALA ALA A . n 
C 1 287 LYS 287 287 287 LYS LYS A . n 
C 1 288 TRP 288 288 288 TRP TRP A . n 
C 1 289 ILE 289 289 289 ILE ILE A . n 
C 1 290 GLY 290 290 290 GLY GLY A . n 
C 1 291 LEU 291 291 291 LEU LEU A . n 
C 1 292 ASP 292 292 292 ASP ASP A . n 
C 1 293 SER 293 293 293 SER SER A . n 
C 1 294 PRO 294 294 294 PRO PRO A . n 
C 1 295 SER 295 295 295 SER SER A . n 
C 1 296 ARG 296 296 296 ARG ARG A . n 
C 1 297 SER 297 297 297 SER SER A . n 
C 1 298 GLU 298 298 298 GLU GLU A . n 
C 1 299 PHE 299 299 299 PHE PHE A . n 
C 1 300 GLU 300 300 300 GLU GLU A . n 
C 1 301 ALA 301 301 301 ALA ALA A . n 
C 1 302 THR 302 302 302 THR THR A . n 
C 1 303 LEU 303 303 303 LEU LEU A . n 
C 1 304 LYS 304 304 304 LYS LYS A . n 
C 1 305 PRO 305 305 305 PRO PRO A . n 
C 1 306 ALA 306 306 306 ALA ALA A . n 
C 1 307 GLU 307 307 307 GLU GLU A . n 
C 1 308 GLU 308 308 308 GLU GLU A . n 
C 1 309 PHE 309 309 309 PHE PHE A . n 
C 1 310 ILE 310 310 310 ILE ILE A . n 
C 1 311 GLU 311 311 311 GLU GLU A . n 
C 1 312 MET 312 312 312 MET MET A . n 
C 1 313 ILE 313 313 313 ILE ILE A . n 
C 1 314 ARG 314 314 314 ARG ARG A . n 
C 1 315 THR 315 315 315 THR THR A . n 
C 1 316 ILE 316 316 316 ILE ILE A . n 
C 1 317 GLY 317 317 317 GLY GLY A . n 
C 1 318 TYR 318 318 318 TYR TYR A . n 
C 1 319 ARG 319 319 319 ARG ARG A . n 
C 1 320 GLY 320 320 320 GLY GLY A . n 
C 1 321 TYR 321 321 321 TYR TYR A . n 
C 1 322 VAL 322 322 322 VAL VAL A . n 
C 1 323 ASN 323 323 323 ASN ASN A . n 
C 1 324 ILE 324 324 324 ILE ILE A . n 
C 1 325 ASP 325 325 325 ASP ASP A . n 
C 1 326 GLY 326 326 326 GLY GLY A . n 
C 1 327 ILE 327 327 327 ILE ILE A . n 
C 1 328 VAL 328 328 328 VAL VAL A . n 
C 1 329 LEU 329 329 329 LEU LEU A . n 
C 1 330 ASP 330 330 330 ASP ASP A . n 
C 1 331 ASP 331 331 331 ASP ASP A . n 
C 1 332 GLY 332 332 332 GLY GLY A . n 
C 1 333 ARG 333 333 333 ARG ARG A . n 
C 1 334 VAL 334 334 334 VAL VAL A . n 
C 1 335 PHE 335 335 335 PHE PHE A . n 
C 1 336 PHE 336 336 336 PHE PHE A . n 
C 1 337 HIS 337 337 337 HIS HIS A . n 
C 1 338 GLU 338 338 338 GLU GLU A . n 
C 1 339 ILE 339 339 339 ILE ILE A . n 
C 1 340 ASN 340 340 340 ASN ASN A . n 
C 1 341 ALA 341 341 341 ALA ALA A . n 
C 1 342 ARG 342 342 342 ARG ARG A . n 
C 1 343 TRP 343 343 343 TRP TRP A . n 
C 1 344 SER 344 344 344 SER SER A . n 
C 1 345 GLY 345 345 345 GLY GLY A . n 
C 1 346 GLY 346 346 346 GLY GLY A . n 
C 1 347 LEU 347 347 347 LEU LEU A . n 
C 1 348 ILE 348 348 348 ILE ILE A . n 
C 1 349 TYR 349 349 349 TYR TYR A . n 
C 1 350 HIS 350 350 350 HIS HIS A . n 
C 1 351 THR 351 351 351 THR THR A . n 
C 1 352 VAL 352 352 352 VAL VAL A . n 
C 1 353 ALA 353 353 353 ALA ALA A . n 
C 1 354 GLU 354 354 354 GLU GLU A . n 
C 1 355 ARG 355 355 355 ARG ARG A . n 
C 1 356 LEU 356 356 356 LEU LEU A . n 
C 1 357 LEU 357 357 357 LEU LEU A . n 
C 1 358 GLY 358 358 358 GLY GLY A . n 
C 1 359 HIS 359 359 359 HIS HIS A . n 
C 1 360 ASP 360 360 360 ASP ASP A . n 
C 1 361 TYR 361 361 361 TYR TYR A . n 
C 1 362 ALA 362 362 362 ALA ALA A . n 
C 1 363 ARG 363 363 363 ARG ARG A . n 
C 1 364 ASN 364 364 364 ASN ASN A . n 
C 1 365 ASN 365 365 365 ASN ASN A . n 
C 1 366 PHE 366 366 366 PHE PHE A . n 
C 1 367 PHE 367 367 367 PHE PHE A . n 
C 1 368 SER 368 368 368 SER SER A . n 
C 1 369 SER 369 369 369 SER SER A . n 
C 1 370 ILE 370 370 370 ILE ILE A . n 
C 1 371 LEU 371 371 371 LEU LEU A . n 
C 1 372 ASN 372 372 372 ASN ASN A . n 
C 1 373 VAL 373 373 373 VAL VAL A . n 
C 1 374 VAL 374 374 374 VAL VAL A . n 
C 1 375 PRO 375 375 375 PRO PRO A . n 
C 1 376 ALA 376 376 376 ALA ALA A . n 
C 1 377 GLY 377 377 377 GLY GLY A . n 
C 1 378 LEU 378 378 378 LEU LEU A . n 
C 1 379 ALA 379 379 379 ALA ALA A . n 
C 1 380 ASP 380 380 380 ASP ASP A . n 
C 1 381 LEU 381 381 381 LEU LEU A . n 
C 1 382 LEU 382 382 382 LEU LEU A . n 
C 1 383 ARG 383 383 383 ARG ARG A . n 
C 1 384 SER 384 384 384 SER SER A . n 
C 1 385 LEU 385 385 385 LEU LEU A . n 
C 1 386 GLU 386 386 386 GLU GLU A . n 
C 1 387 ARG 387 387 387 ARG ARG A . n 
C 1 388 ALA 388 388 388 ALA ALA A . n 
C 1 389 GLY 389 389 389 GLY GLY A . n 
C 1 390 VAL 390 390 390 VAL VAL A . n 
C 1 391 ARG 391 391 391 ARG ARG A . n 
C 1 392 TYR 392 392 392 TYR TYR A . n 
C 1 393 ASP 393 393 393 ASP ASP A . n 
C 1 394 LYS 394 394 394 LYS LYS A . n 
C 1 395 ASP 395 395 395 ASP ASP A . n 
C 1 396 SER 396 396 396 SER SER A . n 
C 1 397 GLY 397 397 397 GLY GLY A . n 
C 1 398 GLU 398 398 398 GLU GLU A . n 
C 1 399 GLY 399 399 399 GLY GLY A . n 
C 1 400 ALA 400 400 400 ALA ALA A . n 
C 1 401 VAL 401 401 401 VAL VAL A . n 
C 1 402 VAL 402 402 402 VAL VAL A . n 
C 1 403 LEU 403 403 403 LEU LEU A . n 
C 1 404 GLY 404 404 404 GLY GLY A . n 
C 1 405 CYS 405 405 405 CYS CYS A . n 
C 1 406 ASN 406 406 406 ASN ASN A . n 
C 1 407 SER 407 407 407 SER SER A . n 
C 1 408 ASP 408 408 408 ASP ASP A . n 
C 1 409 LEU 409 409 409 LEU LEU A . n 
C 1 410 GLY 410 410 410 GLY GLY A . n 
C 1 411 PRO 411 411 411 PRO PRO A . n 
C 1 412 GLY 412 412 412 GLY GLY A . n 
C 1 413 ALA 413 413 413 ALA ALA A . n 
C 1 414 GLU 414 414 414 GLU GLU A . n 
C 1 415 LEU 415 415 415 LEU LEU A . n 
C 1 416 LEU 416 416 416 LEU LEU A . n 
C 1 417 VAL 417 417 417 VAL VAL A . n 
C 1 418 PHE 418 418 418 PHE PHE A . n 
C 1 419 SER 419 419 419 SER SER A . n 
C 1 420 LYS 420 420 420 LYS LYS A . n 
C 1 421 ASP 421 421 421 ASP ASP A . n 
C 1 422 TRP 422 422 422 TRP TRP A . n 
C 1 423 ASP 423 423 423 ASP ASP A . n 
C 1 424 ARG 424 424 424 ARG ARG A . n 
C 1 425 LEU 425 425 425 LEU LEU A . n 
C 1 426 THR 426 426 426 THR THR A . n 
C 1 427 ALA 427 427 427 ALA ALA A . n 
C 1 428 MET 428 428 428 MET MET A . n 
C 1 429 LYS 429 429 429 LYS LYS A . n 
C 1 430 ASP 430 430 430 ASP ASP A . n 
C 1 431 GLU 431 431 431 GLU GLU A . n 
C 1 432 ILE 432 432 432 ILE ILE A . n 
C 1 433 ALA 433 433 433 ALA ALA A . n 
C 1 434 THR 434 434 434 THR THR A . n 
C 1 435 THR 435 435 435 THR THR A . n 
C 1 436 ALA 436 436 436 ALA ALA A . n 
C 1 437 GLY 437 437 437 GLY GLY A . n 
C 1 438 THR 438 438 438 THR THR A . n 
C 1 439 LEU 439 439 439 LEU LEU A . n 
C 1 440 SER 440 440 440 SER SER A . n 
C 1 441 LEU 441 441 ?   ?   ?   A . n 
C 1 442 GLU 442 442 ?   ?   ?   A . n 
C 1 443 HIS 443 443 ?   ?   ?   A . n 
C 1 444 HIS 444 444 ?   ?   ?   A . n 
C 1 445 HIS 445 445 ?   ?   ?   A . n 
C 1 446 HIS 446 446 ?   ?   ?   A . n 
C 1 447 HIS 447 447 ?   ?   ?   A . n 
C 1 448 HIS 448 448 ?   ?   ?   A . n 
D 1 1   MET 1   1   ?   ?   ?   B . n 
D 1 2   PRO 2   2   ?   ?   ?   B . n 
D 1 3   LYS 3   3   ?   ?   ?   B . n 
D 1 4   ILE 4   4   ?   ?   ?   B . n 
D 1 5   ILE 5   5   ?   ?   ?   B . n 
D 1 6   LEU 6   6   ?   ?   ?   B . n 
D 1 7   PRO 7   7   ?   ?   ?   B . n 
D 1 8   ASN 8   8   ?   ?   ?   B . n 
D 1 9   PHE 9   9   ?   ?   ?   B . n 
D 1 10  ARG 10  10  ?   ?   ?   B . n 
D 1 11  ALA 11  11  ?   ?   ?   B . n 
D 1 12  ASP 12  12  ?   ?   ?   B . n 
D 1 13  TYR 13  13  ?   ?   ?   B . n 
D 1 14  SER 14  14  ?   ?   ?   B . n 
D 1 15  GLU 15  15  ?   ?   ?   B . n 
D 1 16  GLN 16  16  ?   ?   ?   B . n 
D 1 17  VAL 17  17  ?   ?   ?   B . n 
D 1 18  ARG 18  18  ?   ?   ?   B . n 
D 1 19  ASP 19  19  ?   ?   ?   B . n 
D 1 20  TRP 20  20  ?   ?   ?   B . n 
D 1 21  LEU 21  21  ?   ?   ?   B . n 
D 1 22  GLY 22  22  ?   ?   ?   B . n 
D 1 23  ILE 23  23  ?   ?   ?   B . n 
D 1 24  SER 24  24  ?   ?   ?   B . n 
D 1 25  ASP 25  25  ?   ?   ?   B . n 
D 1 26  ALA 26  26  ?   ?   ?   B . n 
D 1 27  THR 27  27  ?   ?   ?   B . n 
D 1 28  ALA 28  28  ?   ?   ?   B . n 
D 1 29  SER 29  29  ?   ?   ?   B . n 
D 1 30  SER 30  30  30  SER SER B . n 
D 1 31  THR 31  31  31  THR THR B . n 
D 1 32  ASP 32  32  32  ASP ASP B . n 
D 1 33  THR 33  33  33  THR THR B . n 
D 1 34  THR 34  34  34  THR THR B . n 
D 1 35  ALA 35  35  35  ALA ALA B . n 
D 1 36  ARG 36  36  36  ARG ARG B . n 
D 1 37  PHE 37  37  37  PHE PHE B . n 
D 1 38  LEU 38  38  38  LEU LEU B . n 
D 1 39  TRP 39  39  39  TRP TRP B . n 
D 1 40  HIS 40  40  40  HIS HIS B . n 
D 1 41  ALA 41  41  41  ALA ALA B . n 
D 1 42  GLU 42  42  42  GLU GLU B . n 
D 1 43  ASP 43  43  43  ASP ASP B . n 
D 1 44  GLY 44  44  44  GLY GLY B . n 
D 1 45  ASP 45  45  45  ASP ASP B . n 
D 1 46  VAL 46  46  46  VAL VAL B . n 
D 1 47  LEU 47  47  47  LEU LEU B . n 
D 1 48  VAL 48  48  48  VAL VAL B . n 
D 1 49  ILE 49  49  49  ILE ILE B . n 
D 1 50  PRO 50  50  50  PRO PRO B . n 
D 1 51  ASP 51  51  51  ASP ASP B . n 
D 1 52  THR 52  52  52  THR THR B . n 
D 1 53  VAL 53  53  53  VAL VAL B . n 
D 1 54  ASP 54  54  54  ASP ASP B . n 
D 1 55  PRO 55  55  55  PRO PRO B . n 
D 1 56  ASP 56  56  56  ASP ASP B . n 
D 1 57  PHE 57  57  57  PHE PHE B . n 
D 1 58  PRO 58  58  58  PRO PRO B . n 
D 1 59  GLY 59  59  59  GLY GLY B . n 
D 1 60  TYR 60  60  60  TYR TYR B . n 
D 1 61  VAL 61  61  61  VAL VAL B . n 
D 1 62  ALA 62  62  62  ALA ALA B . n 
D 1 63  ASP 63  63  63  ASP ASP B . n 
D 1 64  THR 64  64  64  THR THR B . n 
D 1 65  LEU 65  65  65  LEU LEU B . n 
D 1 66  GLY 66  66  66  GLY GLY B . n 
D 1 67  ILE 67  67  67  ILE ILE B . n 
D 1 68  ASP 68  68  68  ASP ASP B . n 
D 1 69  GLY 69  69  69  GLY GLY B . n 
D 1 70  THR 70  70  70  THR THR B . n 
D 1 71  SER 71  71  71  SER SER B . n 
D 1 72  VAL 72  72  72  VAL VAL B . n 
D 1 73  HIS 73  73  73  HIS HIS B . n 
D 1 74  VAL 74  74  74  VAL VAL B . n 
D 1 75  GLU 75  75  75  GLU GLU B . n 
D 1 76  ARG 76  76  76  ARG ARG B . n 
D 1 77  THR 77  77  77  THR THR B . n 
D 1 78  GLN 78  78  78  GLN GLN B . n 
D 1 79  THR 79  79  79  THR THR B . n 
D 1 80  PRO 80  80  80  PRO PRO B . n 
D 1 81  LEU 81  81  81  LEU LEU B . n 
D 1 82  SER 82  82  82  SER SER B . n 
D 1 83  GLU 83  83  83  GLU GLU B . n 
D 1 84  ALA 84  84  84  ALA ALA B . n 
D 1 85  VAL 85  85  85  VAL VAL B . n 
D 1 86  LEU 86  86  86  LEU LEU B . n 
D 1 87  GLN 87  87  87  GLN GLN B . n 
D 1 88  ASP 88  88  88  ASP ASP B . n 
D 1 89  PRO 89  89  89  PRO PRO B . n 
D 1 90  GLU 90  90  90  GLU GLU B . n 
D 1 91  PHE 91  91  91  PHE PHE B . n 
D 1 92  ILE 92  92  92  ILE ILE B . n 
D 1 93  ASP 93  93  93  ASP ASP B . n 
D 1 94  ARG 94  94  94  ARG ARG B . n 
D 1 95  LEU 95  95  95  LEU LEU B . n 
D 1 96  ALA 96  96  96  ALA ALA B . n 
D 1 97  ALA 97  97  97  ALA ALA B . n 
D 1 98  HIS 98  98  98  HIS HIS B . n 
D 1 99  THR 99  99  99  THR THR B . n 
D 1 100 GLY 100 100 100 GLY GLY B . n 
D 1 101 THR 101 101 101 THR THR B . n 
D 1 102 GLY 102 102 102 GLY GLY B . n 
D 1 103 ALA 103 103 103 ALA ALA B . n 
D 1 104 GLY 104 104 104 GLY GLY B . n 
D 1 105 TRP 105 105 105 TRP TRP B . n 
D 1 106 SER 106 106 106 SER SER B . n 
D 1 107 LEU 107 107 107 LEU LEU B . n 
D 1 108 PHE 108 108 108 PHE PHE B . n 
D 1 109 PRO 109 109 109 PRO PRO B . n 
D 1 110 CYS 110 110 110 CYS CYS B . n 
D 1 111 VAL 111 111 111 VAL VAL B . n 
D 1 112 SER 112 112 112 SER SER B . n 
D 1 113 THR 113 113 113 THR THR B . n 
D 1 114 ARG 114 114 114 ARG ARG B . n 
D 1 115 ALA 115 115 115 ALA ALA B . n 
D 1 116 ALA 116 116 116 ALA ALA B . n 
D 1 117 ALA 117 117 117 ALA ALA B . n 
D 1 118 GLN 118 118 118 GLN GLN B . n 
D 1 119 LEU 119 119 119 LEU LEU B . n 
D 1 120 THR 120 120 120 THR THR B . n 
D 1 121 ARG 121 121 121 ARG ARG B . n 
D 1 122 LYS 122 122 122 LYS LYS B . n 
D 1 123 LEU 123 123 123 LEU LEU B . n 
D 1 124 ASN 124 124 124 ASN ASN B . n 
D 1 125 VAL 125 125 125 VAL VAL B . n 
D 1 126 ALA 126 126 126 ALA ALA B . n 
D 1 127 ALA 127 127 127 ALA ALA B . n 
D 1 128 LEU 128 128 128 LEU LEU B . n 
D 1 129 ASP 129 129 129 ASP ASP B . n 
D 1 130 GLY 130 130 130 GLY GLY B . n 
D 1 131 TYR 131 131 131 TYR TYR B . n 
D 1 132 GLU 132 132 132 GLU GLU B . n 
D 1 133 PHE 133 133 133 PHE PHE B . n 
D 1 134 ALA 134 134 134 ALA ALA B . n 
D 1 135 MET 135 135 135 MET MET B . n 
D 1 136 GLN 136 136 136 GLN GLN B . n 
D 1 137 ASN 137 137 137 ASN ASN B . n 
D 1 138 GLY 138 138 138 GLY GLY B . n 
D 1 139 ILE 139 139 139 ILE ILE B . n 
D 1 140 ASP 140 140 140 ASP ASP B . n 
D 1 141 LEU 141 141 141 LEU LEU B . n 
D 1 142 LEU 142 142 142 LEU LEU B . n 
D 1 143 ASN 143 143 143 ASN ASN B . n 
D 1 144 MET 144 144 144 MET MET B . n 
D 1 145 LYS 145 145 145 LYS LYS B . n 
D 1 146 SER 146 146 146 SER SER B . n 
D 1 147 THR 147 147 147 THR THR B . n 
D 1 148 PHE 148 148 148 PHE PHE B . n 
D 1 149 ARG 149 149 149 ARG ARG B . n 
D 1 150 ARG 150 150 150 ARG ARG B . n 
D 1 151 LEU 151 151 151 LEU LEU B . n 
D 1 152 ALA 152 152 152 ALA ALA B . n 
D 1 153 ALA 153 153 153 ALA ALA B . n 
D 1 154 GLY 154 154 154 GLY GLY B . n 
D 1 155 LEU 155 155 155 LEU LEU B . n 
D 1 156 GLY 156 156 156 GLY GLY B . n 
D 1 157 THR 157 157 157 THR THR B . n 
D 1 158 PRO 158 158 158 PRO PRO B . n 
D 1 159 LEU 159 159 159 LEU LEU B . n 
D 1 160 THR 160 160 160 THR THR B . n 
D 1 161 ASP 161 161 161 ASP ASP B . n 
D 1 162 GLY 162 162 162 GLY GLY B . n 
D 1 163 VAL 163 163 163 VAL VAL B . n 
D 1 164 VAL 164 164 164 VAL VAL B . n 
D 1 165 ALA 165 165 165 ALA ALA B . n 
D 1 166 ARG 166 166 166 ARG ARG B . n 
D 1 167 GLY 167 167 167 GLY GLY B . n 
D 1 168 PRO 168 168 168 PRO PRO B . n 
D 1 169 ALA 169 169 169 ALA ALA B . n 
D 1 170 GLU 170 170 170 GLU GLU B . n 
D 1 171 VAL 171 171 171 VAL VAL B . n 
D 1 172 ARG 172 172 172 ARG ARG B . n 
D 1 173 SER 173 173 173 SER SER B . n 
D 1 174 ALA 174 174 174 ALA ALA B . n 
D 1 175 ILE 175 175 175 ILE ILE B . n 
D 1 176 GLN 176 176 176 GLN GLN B . n 
D 1 177 GLU 177 177 177 GLU GLU B . n 
D 1 178 LEU 178 178 178 LEU LEU B . n 
D 1 179 ILE 179 179 179 ILE ILE B . n 
D 1 180 ALA 180 180 180 ALA ALA B . n 
D 1 181 GLU 181 181 181 GLU GLU B . n 
D 1 182 THR 182 182 182 THR THR B . n 
D 1 183 GLY 183 183 183 GLY GLY B . n 
D 1 184 MET 184 184 184 MET MET B . n 
D 1 185 VAL 185 185 185 VAL VAL B . n 
D 1 186 ILE 186 186 186 ILE ILE B . n 
D 1 187 ALA 187 187 187 ALA ALA B . n 
D 1 188 LYS 188 188 188 LYS LYS B . n 
D 1 189 GLN 189 189 189 GLN GLN B . n 
D 1 190 ASP 190 190 190 ASP ASP B . n 
D 1 191 ARG 191 191 191 ARG ARG B . n 
D 1 192 SER 192 192 192 SER SER B . n 
D 1 193 GLY 193 193 193 GLY GLY B . n 
D 1 194 GLY 194 194 194 GLY GLY B . n 
D 1 195 GLY 195 195 195 GLY GLY B . n 
D 1 196 HIS 196 196 196 HIS HIS B . n 
D 1 197 GLY 197 197 197 GLY GLY B . n 
D 1 198 ASN 198 198 198 ASN ASN B . n 
D 1 199 ILE 199 199 199 ILE ILE B . n 
D 1 200 GLY 200 200 200 GLY GLY B . n 
D 1 201 ILE 201 201 201 ILE ILE B . n 
D 1 202 SER 202 202 202 SER SER B . n 
D 1 203 THR 203 203 203 THR THR B . n 
D 1 204 SER 204 204 204 SER SER B . n 
D 1 205 PRO 205 205 205 PRO PRO B . n 
D 1 206 GLU 206 206 206 GLU GLU B . n 
D 1 207 SER 207 207 207 SER SER B . n 
D 1 208 SER 208 208 208 SER SER B . n 
D 1 209 PHE 209 209 209 PHE PHE B . n 
D 1 210 PRO 210 210 210 PRO PRO B . n 
D 1 211 GLY 211 211 211 GLY GLY B . n 
D 1 212 THR 212 212 212 THR THR B . n 
D 1 213 ARG 213 213 213 ARG ARG B . n 
D 1 214 GLU 214 214 214 GLU GLU B . n 
D 1 215 VAL 215 215 215 VAL VAL B . n 
D 1 216 LEU 216 216 216 LEU LEU B . n 
D 1 217 ALA 217 217 217 ALA ALA B . n 
D 1 218 TYR 218 218 218 TYR TYR B . n 
D 1 219 ALA 219 219 219 ALA ALA B . n 
D 1 220 ASN 220 220 220 ASN ASN B . n 
D 1 221 ASP 221 221 221 ASP ASP B . n 
D 1 222 GLN 222 222 222 GLN GLN B . n 
D 1 223 LEU 223 223 223 LEU LEU B . n 
D 1 224 ASP 224 224 224 ASP ASP B . n 
D 1 225 THR 225 225 225 THR THR B . n 
D 1 226 LEU 226 226 226 LEU LEU B . n 
D 1 227 ALA 227 227 227 ALA ALA B . n 
D 1 228 ASP 228 228 228 ASP ASP B . n 
D 1 229 THR 229 229 229 THR THR B . n 
D 1 230 LEU 230 230 230 LEU LEU B . n 
D 1 231 TRP 231 231 231 TRP TRP B . n 
D 1 232 SER 232 232 232 SER SER B . n 
D 1 233 GLN 233 233 233 GLN GLN B . n 
D 1 234 LEU 234 234 234 LEU LEU B . n 
D 1 235 THR 235 235 235 THR THR B . n 
D 1 236 ASP 236 236 236 ASP ASP B . n 
D 1 237 THR 237 237 237 THR THR B . n 
D 1 238 GLN 238 238 238 GLN GLN B . n 
D 1 239 ASN 239 239 239 ASN ASN B . n 
D 1 240 GLN 240 240 240 GLN GLN B . n 
D 1 241 PHE 241 241 241 PHE PHE B . n 
D 1 242 ILE 242 242 242 ILE ILE B . n 
D 1 243 THR 243 243 243 THR THR B . n 
D 1 244 VAL 244 244 244 VAL VAL B . n 
D 1 245 GLU 245 245 245 GLU GLU B . n 
D 1 246 THR 246 246 246 THR THR B . n 
D 1 247 TYR 247 247 247 TYR TYR B . n 
D 1 248 HIS 248 248 248 HIS HIS B . n 
D 1 249 ARG 249 249 249 ARG ARG B . n 
D 1 250 ALA 250 250 250 ALA ALA B . n 
D 1 251 ASP 251 251 251 ASP ASP B . n 
D 1 252 GLN 252 252 252 GLN GLN B . n 
D 1 253 ARG 253 253 253 ARG ARG B . n 
D 1 254 PHE 254 254 254 PHE PHE B . n 
D 1 255 PHE 255 255 255 PHE PHE B . n 
D 1 256 PHE 256 256 256 PHE PHE B . n 
D 1 257 GLU 257 257 257 GLU GLU B . n 
D 1 258 TYR 258 258 258 TYR TYR B . n 
D 1 259 HIS 259 259 259 HIS HIS B . n 
D 1 260 LEU 260 260 260 LEU LEU B . n 
D 1 261 ASP 261 261 261 ASP ASP B . n 
D 1 262 GLY 262 262 262 GLY GLY B . n 
D 1 263 ASP 263 263 263 ASP ASP B . n 
D 1 264 ARG 264 264 264 ARG ARG B . n 
D 1 265 ALA 265 265 265 ALA ALA B . n 
D 1 266 ARG 266 266 266 ARG ARG B . n 
D 1 267 PHE 267 267 267 PHE PHE B . n 
D 1 268 LEU 268 268 268 LEU LEU B . n 
D 1 269 HIS 269 269 269 HIS HIS B . n 
D 1 270 SER 270 270 270 SER SER B . n 
D 1 271 SER 271 271 271 SER SER B . n 
D 1 272 ILE 272 272 272 ILE ILE B . n 
D 1 273 LEU 273 273 273 LEU LEU B . n 
D 1 274 LYS 274 274 274 LYS LYS B . n 
D 1 275 TYR 275 275 275 TYR TYR B . n 
D 1 276 GLU 276 276 276 GLU GLU B . n 
D 1 277 GLN 277 277 ?   ?   ?   B . n 
D 1 278 LEU 278 278 ?   ?   ?   B . n 
D 1 279 PRO 279 279 ?   ?   ?   B . n 
D 1 280 GLU 280 280 ?   ?   ?   B . n 
D 1 281 GLY 281 281 281 GLY GLY B . n 
D 1 282 SER 282 282 282 SER SER B . n 
D 1 283 GLY 283 283 ?   ?   ?   B . n 
D 1 284 GLY 284 284 284 GLY GLY B . n 
D 1 285 SER 285 285 285 SER SER B . n 
D 1 286 ALA 286 286 286 ALA ALA B . n 
D 1 287 LYS 287 287 287 LYS LYS B . n 
D 1 288 TRP 288 288 288 TRP TRP B . n 
D 1 289 ILE 289 289 289 ILE ILE B . n 
D 1 290 GLY 290 290 290 GLY GLY B . n 
D 1 291 LEU 291 291 291 LEU LEU B . n 
D 1 292 ASP 292 292 292 ASP ASP B . n 
D 1 293 SER 293 293 293 SER SER B . n 
D 1 294 PRO 294 294 294 PRO PRO B . n 
D 1 295 SER 295 295 295 SER SER B . n 
D 1 296 ARG 296 296 296 ARG ARG B . n 
D 1 297 SER 297 297 297 SER SER B . n 
D 1 298 GLU 298 298 298 GLU GLU B . n 
D 1 299 PHE 299 299 299 PHE PHE B . n 
D 1 300 GLU 300 300 300 GLU GLU B . n 
D 1 301 ALA 301 301 301 ALA ALA B . n 
D 1 302 THR 302 302 302 THR THR B . n 
D 1 303 LEU 303 303 303 LEU LEU B . n 
D 1 304 LYS 304 304 304 LYS LYS B . n 
D 1 305 PRO 305 305 305 PRO PRO B . n 
D 1 306 ALA 306 306 306 ALA ALA B . n 
D 1 307 GLU 307 307 307 GLU GLU B . n 
D 1 308 GLU 308 308 308 GLU GLU B . n 
D 1 309 PHE 309 309 309 PHE PHE B . n 
D 1 310 ILE 310 310 310 ILE ILE B . n 
D 1 311 GLU 311 311 311 GLU GLU B . n 
D 1 312 MET 312 312 312 MET MET B . n 
D 1 313 ILE 313 313 313 ILE ILE B . n 
D 1 314 ARG 314 314 314 ARG ARG B . n 
D 1 315 THR 315 315 315 THR THR B . n 
D 1 316 ILE 316 316 316 ILE ILE B . n 
D 1 317 GLY 317 317 317 GLY GLY B . n 
D 1 318 TYR 318 318 318 TYR TYR B . n 
D 1 319 ARG 319 319 319 ARG ARG B . n 
D 1 320 GLY 320 320 320 GLY GLY B . n 
D 1 321 TYR 321 321 321 TYR TYR B . n 
D 1 322 VAL 322 322 322 VAL VAL B . n 
D 1 323 ASN 323 323 323 ASN ASN B . n 
D 1 324 ILE 324 324 324 ILE ILE B . n 
D 1 325 ASP 325 325 325 ASP ASP B . n 
D 1 326 GLY 326 326 326 GLY GLY B . n 
D 1 327 ILE 327 327 327 ILE ILE B . n 
D 1 328 VAL 328 328 328 VAL VAL B . n 
D 1 329 LEU 329 329 329 LEU LEU B . n 
D 1 330 ASP 330 330 330 ASP ASP B . n 
D 1 331 ASP 331 331 331 ASP ASP B . n 
D 1 332 GLY 332 332 332 GLY GLY B . n 
D 1 333 ARG 333 333 333 ARG ARG B . n 
D 1 334 VAL 334 334 334 VAL VAL B . n 
D 1 335 PHE 335 335 335 PHE PHE B . n 
D 1 336 PHE 336 336 336 PHE PHE B . n 
D 1 337 HIS 337 337 337 HIS HIS B . n 
D 1 338 GLU 338 338 338 GLU GLU B . n 
D 1 339 ILE 339 339 339 ILE ILE B . n 
D 1 340 ASN 340 340 340 ASN ASN B . n 
D 1 341 ALA 341 341 341 ALA ALA B . n 
D 1 342 ARG 342 342 342 ARG ARG B . n 
D 1 343 TRP 343 343 343 TRP TRP B . n 
D 1 344 SER 344 344 344 SER SER B . n 
D 1 345 GLY 345 345 345 GLY GLY B . n 
D 1 346 GLY 346 346 346 GLY GLY B . n 
D 1 347 LEU 347 347 347 LEU LEU B . n 
D 1 348 ILE 348 348 348 ILE ILE B . n 
D 1 349 TYR 349 349 349 TYR TYR B . n 
D 1 350 HIS 350 350 350 HIS HIS B . n 
D 1 351 THR 351 351 351 THR THR B . n 
D 1 352 VAL 352 352 352 VAL VAL B . n 
D 1 353 ALA 353 353 353 ALA ALA B . n 
D 1 354 GLU 354 354 354 GLU GLU B . n 
D 1 355 ARG 355 355 355 ARG ARG B . n 
D 1 356 LEU 356 356 356 LEU LEU B . n 
D 1 357 LEU 357 357 357 LEU LEU B . n 
D 1 358 GLY 358 358 358 GLY GLY B . n 
D 1 359 HIS 359 359 359 HIS HIS B . n 
D 1 360 ASP 360 360 360 ASP ASP B . n 
D 1 361 TYR 361 361 361 TYR TYR B . n 
D 1 362 ALA 362 362 362 ALA ALA B . n 
D 1 363 ARG 363 363 363 ARG ARG B . n 
D 1 364 ASN 364 364 364 ASN ASN B . n 
D 1 365 ASN 365 365 365 ASN ASN B . n 
D 1 366 PHE 366 366 366 PHE PHE B . n 
D 1 367 PHE 367 367 367 PHE PHE B . n 
D 1 368 SER 368 368 368 SER SER B . n 
D 1 369 SER 369 369 369 SER SER B . n 
D 1 370 ILE 370 370 370 ILE ILE B . n 
D 1 371 LEU 371 371 371 LEU LEU B . n 
D 1 372 ASN 372 372 372 ASN ASN B . n 
D 1 373 VAL 373 373 373 VAL VAL B . n 
D 1 374 VAL 374 374 374 VAL VAL B . n 
D 1 375 PRO 375 375 375 PRO PRO B . n 
D 1 376 ALA 376 376 376 ALA ALA B . n 
D 1 377 GLY 377 377 377 GLY GLY B . n 
D 1 378 LEU 378 378 378 LEU LEU B . n 
D 1 379 ALA 379 379 379 ALA ALA B . n 
D 1 380 ASP 380 380 380 ASP ASP B . n 
D 1 381 LEU 381 381 381 LEU LEU B . n 
D 1 382 LEU 382 382 382 LEU LEU B . n 
D 1 383 ARG 383 383 383 ARG ARG B . n 
D 1 384 SER 384 384 384 SER SER B . n 
D 1 385 LEU 385 385 385 LEU LEU B . n 
D 1 386 GLU 386 386 386 GLU GLU B . n 
D 1 387 ARG 387 387 387 ARG ARG B . n 
D 1 388 ALA 388 388 388 ALA ALA B . n 
D 1 389 GLY 389 389 389 GLY GLY B . n 
D 1 390 VAL 390 390 390 VAL VAL B . n 
D 1 391 ARG 391 391 391 ARG ARG B . n 
D 1 392 TYR 392 392 392 TYR TYR B . n 
D 1 393 ASP 393 393 393 ASP ASP B . n 
D 1 394 LYS 394 394 394 LYS LYS B . n 
D 1 395 ASP 395 395 395 ASP ASP B . n 
D 1 396 SER 396 396 396 SER SER B . n 
D 1 397 GLY 397 397 397 GLY GLY B . n 
D 1 398 GLU 398 398 398 GLU GLU B . n 
D 1 399 GLY 399 399 399 GLY GLY B . n 
D 1 400 ALA 400 400 400 ALA ALA B . n 
D 1 401 VAL 401 401 401 VAL VAL B . n 
D 1 402 VAL 402 402 402 VAL VAL B . n 
D 1 403 LEU 403 403 403 LEU LEU B . n 
D 1 404 GLY 404 404 404 GLY GLY B . n 
D 1 405 CYS 405 405 405 CYS CYS B . n 
D 1 406 ASN 406 406 406 ASN ASN B . n 
D 1 407 SER 407 407 407 SER SER B . n 
D 1 408 ASP 408 408 408 ASP ASP B . n 
D 1 409 LEU 409 409 409 LEU LEU B . n 
D 1 410 GLY 410 410 410 GLY GLY B . n 
D 1 411 PRO 411 411 411 PRO PRO B . n 
D 1 412 GLY 412 412 412 GLY GLY B . n 
D 1 413 ALA 413 413 413 ALA ALA B . n 
D 1 414 GLU 414 414 414 GLU GLU B . n 
D 1 415 LEU 415 415 415 LEU LEU B . n 
D 1 416 LEU 416 416 416 LEU LEU B . n 
D 1 417 VAL 417 417 417 VAL VAL B . n 
D 1 418 PHE 418 418 418 PHE PHE B . n 
D 1 419 SER 419 419 419 SER SER B . n 
D 1 420 LYS 420 420 420 LYS LYS B . n 
D 1 421 ASP 421 421 421 ASP ASP B . n 
D 1 422 TRP 422 422 422 TRP TRP B . n 
D 1 423 ASP 423 423 423 ASP ASP B . n 
D 1 424 ARG 424 424 424 ARG ARG B . n 
D 1 425 LEU 425 425 425 LEU LEU B . n 
D 1 426 THR 426 426 426 THR THR B . n 
D 1 427 ALA 427 427 427 ALA ALA B . n 
D 1 428 MET 428 428 428 MET MET B . n 
D 1 429 LYS 429 429 429 LYS LYS B . n 
D 1 430 ASP 430 430 430 ASP ASP B . n 
D 1 431 GLU 431 431 431 GLU GLU B . n 
D 1 432 ILE 432 432 432 ILE ILE B . n 
D 1 433 ALA 433 433 433 ALA ALA B . n 
D 1 434 THR 434 434 434 THR THR B . n 
D 1 435 THR 435 435 435 THR THR B . n 
D 1 436 ALA 436 436 436 ALA ALA B . n 
D 1 437 GLY 437 437 437 GLY GLY B . n 
D 1 438 THR 438 438 438 THR THR B . n 
D 1 439 LEU 439 439 439 LEU LEU B . n 
D 1 440 SER 440 440 440 SER SER B . n 
D 1 441 LEU 441 441 ?   ?   ?   B . n 
D 1 442 GLU 442 442 ?   ?   ?   B . n 
D 1 443 HIS 443 443 ?   ?   ?   B . n 
D 1 444 HIS 444 444 ?   ?   ?   B . n 
D 1 445 HIS 445 445 ?   ?   ?   B . n 
D 1 446 HIS 446 446 ?   ?   ?   B . n 
D 1 447 HIS 447 447 ?   ?   ?   B . n 
D 1 448 HIS 448 448 ?   ?   ?   B . 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 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 AMP ? ? AMP ? ? 'SUBJECT OF INVESTIGATION' ? 
3 ANP ? ? ANP ? ? 'SUBJECT OF INVESTIGATION' ? 
4 GOL ? ? GOL ? ? 'SUBJECT OF INVESTIGATION' ? 
5 PEG ? ? PEG ? ? 'SUBJECT OF INVESTIGATION' ? 
6 TRS ? ? TRS ? ? '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 
E  2 ANP 1  501 501 ANP ANP C . 
F  3 GOL 1  502 504 GOL GOL C . 
G  3 GOL 1  503 506 GOL GOL C . 
H  4 PEG 1  504 507 PEG PEG C . 
I  2 ANP 1  505 508 ANP ANP C . 
J  3 GOL 1  501 503 GOL GOL D . 
K  3 GOL 1  502 504 GOL GOL D . 
L  4 PEG 1  503 505 PEG PEG D . 
M  5 AMP 1  504 506 AMP AMP D . 
N  4 PEG 1  505 507 PEG PEG D . 
O  6 ADP 1  501 501 ADP ADP A . 
P  4 PEG 1  502 502 PEG PEG A . 
Q  4 PEG 1  503 503 PEG PEG A . 
R  4 PEG 1  504 504 PEG PEG A . 
S  4 PEG 1  505 505 PEG PEG A . 
T  3 GOL 1  506 506 GOL GOL A . 
U  4 PEG 1  501 501 PEG PEG B . 
V  4 PEG 1  502 502 PEG PEG B . 
W  3 GOL 1  503 503 GOL GOL B . 
X  7 TRS 1  504 504 TRS TRS B . 
Y  8 HOH 1  601 99  HOH HOH C . 
Y  8 HOH 2  602 193 HOH HOH C . 
Y  8 HOH 3  603 195 HOH HOH C . 
Y  8 HOH 4  604 154 HOH HOH C . 
Y  8 HOH 5  605 4   HOH HOH C . 
Y  8 HOH 6  606 144 HOH HOH C . 
Y  8 HOH 7  607 76  HOH HOH C . 
Y  8 HOH 8  608 212 HOH HOH C . 
Y  8 HOH 9  609 78  HOH HOH C . 
Y  8 HOH 10 610 54  HOH HOH C . 
Y  8 HOH 11 611 72  HOH HOH C . 
Y  8 HOH 12 612 109 HOH HOH C . 
Y  8 HOH 13 613 319 HOH HOH C . 
Y  8 HOH 14 614 110 HOH HOH C . 
Y  8 HOH 15 615 143 HOH HOH C . 
Y  8 HOH 16 616 183 HOH HOH C . 
Y  8 HOH 17 617 131 HOH HOH C . 
Y  8 HOH 18 618 64  HOH HOH C . 
Y  8 HOH 19 619 177 HOH HOH C . 
Y  8 HOH 20 620 210 HOH HOH C . 
Y  8 HOH 21 621 50  HOH HOH C . 
Y  8 HOH 22 622 48  HOH HOH C . 
Y  8 HOH 23 623 250 HOH HOH C . 
Y  8 HOH 24 624 172 HOH HOH C . 
Y  8 HOH 25 625 105 HOH HOH C . 
Y  8 HOH 26 626 155 HOH HOH C . 
Y  8 HOH 27 627 65  HOH HOH C . 
Y  8 HOH 28 628 104 HOH HOH C . 
Y  8 HOH 29 629 59  HOH HOH C . 
Y  8 HOH 30 630 239 HOH HOH C . 
Y  8 HOH 31 631 182 HOH HOH C . 
Y  8 HOH 32 632 136 HOH HOH C . 
Y  8 HOH 33 633 7   HOH HOH C . 
Y  8 HOH 34 634 159 HOH HOH C . 
Y  8 HOH 35 635 27  HOH HOH C . 
Y  8 HOH 36 636 234 HOH HOH C . 
Y  8 HOH 37 637 280 HOH HOH C . 
Y  8 HOH 38 638 186 HOH HOH C . 
Y  8 HOH 39 639 200 HOH HOH C . 
Y  8 HOH 40 640 112 HOH HOH C . 
Y  8 HOH 41 641 123 HOH HOH C . 
Y  8 HOH 42 642 124 HOH HOH C . 
Y  8 HOH 43 643 149 HOH HOH C . 
Y  8 HOH 44 644 74  HOH HOH C . 
Y  8 HOH 45 645 300 HOH HOH C . 
Y  8 HOH 46 646 174 HOH HOH C . 
Y  8 HOH 47 647 294 HOH HOH C . 
Y  8 HOH 48 648 191 HOH HOH C . 
Y  8 HOH 49 649 87  HOH HOH C . 
Y  8 HOH 50 650 316 HOH HOH C . 
Y  8 HOH 51 651 263 HOH HOH C . 
Y  8 HOH 52 652 157 HOH HOH C . 
Y  8 HOH 53 653 108 HOH HOH C . 
Y  8 HOH 54 654 295 HOH HOH C . 
Y  8 HOH 55 655 150 HOH HOH C . 
Y  8 HOH 56 656 58  HOH HOH C . 
Y  8 HOH 57 657 127 HOH HOH C . 
Y  8 HOH 58 658 92  HOH HOH C . 
Y  8 HOH 59 659 94  HOH HOH C . 
Y  8 HOH 60 660 84  HOH HOH C . 
Y  8 HOH 61 661 315 HOH HOH C . 
Y  8 HOH 62 662 299 HOH HOH C . 
Y  8 HOH 63 663 314 HOH HOH C . 
Y  8 HOH 64 664 324 HOH HOH C . 
Y  8 HOH 65 665 147 HOH HOH C . 
Y  8 HOH 66 666 134 HOH HOH C . 
Y  8 HOH 67 667 111 HOH HOH C . 
Z  8 HOH 1  601 281 HOH HOH D . 
Z  8 HOH 2  602 230 HOH HOH D . 
Z  8 HOH 3  603 130 HOH HOH D . 
Z  8 HOH 4  604 229 HOH HOH D . 
Z  8 HOH 5  605 207 HOH HOH D . 
Z  8 HOH 6  606 197 HOH HOH D . 
Z  8 HOH 7  607 13  HOH HOH D . 
Z  8 HOH 8  608 132 HOH HOH D . 
Z  8 HOH 9  609 247 HOH HOH D . 
Z  8 HOH 10 610 75  HOH HOH D . 
Z  8 HOH 11 611 252 HOH HOH D . 
Z  8 HOH 12 612 126 HOH HOH D . 
Z  8 HOH 13 613 11  HOH HOH D . 
Z  8 HOH 14 614 9   HOH HOH D . 
Z  8 HOH 15 615 77  HOH HOH D . 
Z  8 HOH 16 616 83  HOH HOH D . 
Z  8 HOH 17 617 116 HOH HOH D . 
Z  8 HOH 18 618 73  HOH HOH D . 
Z  8 HOH 19 619 196 HOH HOH D . 
Z  8 HOH 20 620 142 HOH HOH D . 
Z  8 HOH 21 621 35  HOH HOH D . 
Z  8 HOH 22 622 39  HOH HOH D . 
Z  8 HOH 23 623 261 HOH HOH D . 
Z  8 HOH 24 624 201 HOH HOH D . 
Z  8 HOH 25 625 226 HOH HOH D . 
Z  8 HOH 26 626 14  HOH HOH D . 
Z  8 HOH 27 627 233 HOH HOH D . 
Z  8 HOH 28 628 176 HOH HOH D . 
Z  8 HOH 29 629 139 HOH HOH D . 
Z  8 HOH 30 630 198 HOH HOH D . 
Z  8 HOH 31 631 310 HOH HOH D . 
Z  8 HOH 32 632 227 HOH HOH D . 
Z  8 HOH 33 633 8   HOH HOH D . 
Z  8 HOH 34 634 308 HOH HOH D . 
Z  8 HOH 35 635 17  HOH HOH D . 
Z  8 HOH 36 636 214 HOH HOH D . 
Z  8 HOH 37 637 189 HOH HOH D . 
Z  8 HOH 38 638 25  HOH HOH D . 
Z  8 HOH 39 639 284 HOH HOH D . 
Z  8 HOH 40 640 228 HOH HOH D . 
Z  8 HOH 41 641 288 HOH HOH D . 
Z  8 HOH 42 642 32  HOH HOH D . 
Z  8 HOH 43 643 135 HOH HOH D . 
Z  8 HOH 44 644 30  HOH HOH D . 
Z  8 HOH 45 645 175 HOH HOH D . 
Z  8 HOH 46 646 82  HOH HOH D . 
Z  8 HOH 47 647 311 HOH HOH D . 
Z  8 HOH 48 648 122 HOH HOH D . 
Z  8 HOH 49 649 213 HOH HOH D . 
Z  8 HOH 50 650 190 HOH HOH D . 
Z  8 HOH 51 651 70  HOH HOH D . 
Z  8 HOH 52 652 194 HOH HOH D . 
Z  8 HOH 53 653 306 HOH HOH D . 
Z  8 HOH 54 654 101 HOH HOH D . 
Z  8 HOH 55 655 241 HOH HOH D . 
Z  8 HOH 56 656 43  HOH HOH D . 
Z  8 HOH 57 657 138 HOH HOH D . 
Z  8 HOH 58 658 248 HOH HOH D . 
Z  8 HOH 59 659 185 HOH HOH D . 
Z  8 HOH 60 660 20  HOH HOH D . 
Z  8 HOH 61 661 297 HOH HOH D . 
Z  8 HOH 62 662 141 HOH HOH D . 
Z  8 HOH 63 663 237 HOH HOH D . 
Z  8 HOH 64 664 264 HOH HOH D . 
Z  8 HOH 65 665 219 HOH HOH D . 
Z  8 HOH 66 666 283 HOH HOH D . 
Z  8 HOH 67 667 89  HOH HOH D . 
Z  8 HOH 68 668 85  HOH HOH D . 
Z  8 HOH 69 669 22  HOH HOH D . 
Z  8 HOH 70 670 96  HOH HOH D . 
Z  8 HOH 71 671 222 HOH HOH D . 
Z  8 HOH 72 672 179 HOH HOH D . 
Z  8 HOH 73 673 42  HOH HOH D . 
Z  8 HOH 74 674 267 HOH HOH D . 
Z  8 HOH 75 675 253 HOH HOH D . 
Z  8 HOH 76 676 259 HOH HOH D . 
Z  8 HOH 77 677 66  HOH HOH D . 
Z  8 HOH 78 678 307 HOH HOH D . 
Z  8 HOH 79 679 128 HOH HOH D . 
Z  8 HOH 80 680 313 HOH HOH D . 
Z  8 HOH 81 681 321 HOH HOH D . 
Z  8 HOH 82 682 309 HOH HOH D . 
Z  8 HOH 83 683 215 HOH HOH D . 
Z  8 HOH 84 684 282 HOH HOH D . 
Z  8 HOH 85 685 276 HOH HOH D . 
Z  8 HOH 86 686 246 HOH HOH D . 
Z  8 HOH 87 687 204 HOH HOH D . 
Z  8 HOH 88 688 249 HOH HOH D . 
Z  8 HOH 89 689 289 HOH HOH D . 
Z  8 HOH 90 690 318 HOH HOH D . 
AA 8 HOH 1  601 140 HOH HOH A . 
AA 8 HOH 2  602 152 HOH HOH A . 
AA 8 HOH 3  603 164 HOH HOH A . 
AA 8 HOH 4  604 118 HOH HOH A . 
AA 8 HOH 5  605 145 HOH HOH A . 
AA 8 HOH 6  606 80  HOH HOH A . 
AA 8 HOH 7  607 62  HOH HOH A . 
AA 8 HOH 8  608 21  HOH HOH A . 
AA 8 HOH 9  609 31  HOH HOH A . 
AA 8 HOH 10 610 292 HOH HOH A . 
AA 8 HOH 11 611 165 HOH HOH A . 
AA 8 HOH 12 612 325 HOH HOH A . 
AA 8 HOH 13 613 81  HOH HOH A . 
AA 8 HOH 14 614 24  HOH HOH A . 
AA 8 HOH 15 615 323 HOH HOH A . 
AA 8 HOH 16 616 169 HOH HOH A . 
AA 8 HOH 17 617 184 HOH HOH A . 
AA 8 HOH 18 618 10  HOH HOH A . 
AA 8 HOH 19 619 6   HOH HOH A . 
AA 8 HOH 20 620 63  HOH HOH A . 
AA 8 HOH 21 621 3   HOH HOH A . 
AA 8 HOH 22 622 51  HOH HOH A . 
AA 8 HOH 23 623 244 HOH HOH A . 
AA 8 HOH 24 624 242 HOH HOH A . 
AA 8 HOH 25 625 23  HOH HOH A . 
AA 8 HOH 26 626 61  HOH HOH A . 
AA 8 HOH 27 627 93  HOH HOH A . 
AA 8 HOH 28 628 217 HOH HOH A . 
AA 8 HOH 29 629 103 HOH HOH A . 
AA 8 HOH 30 630 262 HOH HOH A . 
AA 8 HOH 31 631 216 HOH HOH A . 
AA 8 HOH 32 632 254 HOH HOH A . 
AA 8 HOH 33 633 258 HOH HOH A . 
AA 8 HOH 34 634 67  HOH HOH A . 
AA 8 HOH 35 635 1   HOH HOH A . 
AA 8 HOH 36 636 173 HOH HOH A . 
AA 8 HOH 37 637 119 HOH HOH A . 
AA 8 HOH 38 638 19  HOH HOH A . 
AA 8 HOH 39 639 49  HOH HOH A . 
AA 8 HOH 40 640 33  HOH HOH A . 
AA 8 HOH 41 641 60  HOH HOH A . 
AA 8 HOH 42 642 55  HOH HOH A . 
AA 8 HOH 43 643 114 HOH HOH A . 
AA 8 HOH 44 644 265 HOH HOH A . 
AA 8 HOH 45 645 320 HOH HOH A . 
AA 8 HOH 46 646 37  HOH HOH A . 
AA 8 HOH 47 647 71  HOH HOH A . 
AA 8 HOH 48 648 317 HOH HOH A . 
AA 8 HOH 49 649 301 HOH HOH A . 
AA 8 HOH 50 650 187 HOH HOH A . 
AA 8 HOH 51 651 232 HOH HOH A . 
AA 8 HOH 52 652 57  HOH HOH A . 
AA 8 HOH 53 653 2   HOH HOH A . 
AA 8 HOH 54 654 47  HOH HOH A . 
AA 8 HOH 55 655 202 HOH HOH A . 
AA 8 HOH 56 656 312 HOH HOH A . 
AA 8 HOH 57 657 303 HOH HOH A . 
AA 8 HOH 58 658 240 HOH HOH A . 
AA 8 HOH 59 659 208 HOH HOH A . 
AA 8 HOH 60 660 163 HOH HOH A . 
AA 8 HOH 61 661 148 HOH HOH A . 
AA 8 HOH 62 662 235 HOH HOH A . 
AA 8 HOH 63 663 269 HOH HOH A . 
AA 8 HOH 64 664 162 HOH HOH A . 
AA 8 HOH 65 665 171 HOH HOH A . 
AA 8 HOH 66 666 220 HOH HOH A . 
AA 8 HOH 67 667 181 HOH HOH A . 
AA 8 HOH 68 668 161 HOH HOH A . 
AA 8 HOH 69 669 243 HOH HOH A . 
AA 8 HOH 70 670 156 HOH HOH A . 
AA 8 HOH 71 671 52  HOH HOH A . 
AA 8 HOH 72 672 158 HOH HOH A . 
AA 8 HOH 73 673 238 HOH HOH A . 
AA 8 HOH 74 674 285 HOH HOH A . 
AA 8 HOH 75 675 286 HOH HOH A . 
BA 8 HOH 1  601 278 HOH HOH B . 
BA 8 HOH 2  602 257 HOH HOH B . 
BA 8 HOH 3  603 298 HOH HOH B . 
BA 8 HOH 4  604 256 HOH HOH B . 
BA 8 HOH 5  605 106 HOH HOH B . 
BA 8 HOH 6  606 209 HOH HOH B . 
BA 8 HOH 7  607 203 HOH HOH B . 
BA 8 HOH 8  608 40  HOH HOH B . 
BA 8 HOH 9  609 272 HOH HOH B . 
BA 8 HOH 10 610 279 HOH HOH B . 
BA 8 HOH 11 611 29  HOH HOH B . 
BA 8 HOH 12 612 255 HOH HOH B . 
BA 8 HOH 13 613 178 HOH HOH B . 
BA 8 HOH 14 614 68  HOH HOH B . 
BA 8 HOH 15 615 225 HOH HOH B . 
BA 8 HOH 16 616 95  HOH HOH B . 
BA 8 HOH 17 617 102 HOH HOH B . 
BA 8 HOH 18 618 133 HOH HOH B . 
BA 8 HOH 19 619 69  HOH HOH B . 
BA 8 HOH 20 620 15  HOH HOH B . 
BA 8 HOH 21 621 205 HOH HOH B . 
BA 8 HOH 22 622 291 HOH HOH B . 
BA 8 HOH 23 623 245 HOH HOH B . 
BA 8 HOH 24 624 98  HOH HOH B . 
BA 8 HOH 25 625 34  HOH HOH B . 
BA 8 HOH 26 626 304 HOH HOH B . 
BA 8 HOH 27 627 192 HOH HOH B . 
BA 8 HOH 28 628 115 HOH HOH B . 
BA 8 HOH 29 629 231 HOH HOH B . 
BA 8 HOH 30 630 268 HOH HOH B . 
BA 8 HOH 31 631 160 HOH HOH B . 
BA 8 HOH 32 632 113 HOH HOH B . 
BA 8 HOH 33 633 153 HOH HOH B . 
BA 8 HOH 34 634 36  HOH HOH B . 
BA 8 HOH 35 635 100 HOH HOH B . 
BA 8 HOH 36 636 5   HOH HOH B . 
BA 8 HOH 37 637 28  HOH HOH B . 
BA 8 HOH 38 638 167 HOH HOH B . 
BA 8 HOH 39 639 26  HOH HOH B . 
BA 8 HOH 40 640 260 HOH HOH B . 
BA 8 HOH 41 641 199 HOH HOH B . 
BA 8 HOH 42 642 86  HOH HOH B . 
BA 8 HOH 43 643 44  HOH HOH B . 
BA 8 HOH 44 644 107 HOH HOH B . 
BA 8 HOH 45 645 45  HOH HOH B . 
BA 8 HOH 46 646 90  HOH HOH B . 
BA 8 HOH 47 647 18  HOH HOH B . 
BA 8 HOH 48 648 12  HOH HOH B . 
BA 8 HOH 49 649 274 HOH HOH B . 
BA 8 HOH 50 650 151 HOH HOH B . 
BA 8 HOH 51 651 79  HOH HOH B . 
BA 8 HOH 52 652 251 HOH HOH B . 
BA 8 HOH 53 653 166 HOH HOH B . 
BA 8 HOH 54 654 120 HOH HOH B . 
BA 8 HOH 55 655 137 HOH HOH B . 
BA 8 HOH 56 656 188 HOH HOH B . 
BA 8 HOH 57 657 97  HOH HOH B . 
BA 8 HOH 58 658 16  HOH HOH B . 
BA 8 HOH 59 659 221 HOH HOH B . 
BA 8 HOH 60 660 224 HOH HOH B . 
BA 8 HOH 61 661 91  HOH HOH B . 
BA 8 HOH 62 662 223 HOH HOH B . 
BA 8 HOH 63 663 236 HOH HOH B . 
BA 8 HOH 64 664 206 HOH HOH B . 
BA 8 HOH 65 665 146 HOH HOH B . 
BA 8 HOH 66 666 46  HOH HOH B . 
BA 8 HOH 67 667 273 HOH HOH B . 
BA 8 HOH 68 668 38  HOH HOH B . 
BA 8 HOH 69 669 125 HOH HOH B . 
BA 8 HOH 70 670 211 HOH HOH B . 
BA 8 HOH 71 671 88  HOH HOH B . 
BA 8 HOH 72 672 290 HOH HOH B . 
BA 8 HOH 73 673 266 HOH HOH B . 
BA 8 HOH 74 674 41  HOH HOH B . 
BA 8 HOH 75 675 270 HOH HOH B . 
BA 8 HOH 76 676 322 HOH HOH B . 
BA 8 HOH 77 677 293 HOH HOH B . 
BA 8 HOH 78 678 275 HOH HOH B . 
BA 8 HOH 79 679 53  HOH HOH B . 
BA 8 HOH 80 680 296 HOH HOH B . 
BA 8 HOH 81 681 305 HOH HOH B . 
BA 8 HOH 82 682 56  HOH HOH B . 
BA 8 HOH 83 683 287 HOH HOH B . 
BA 8 HOH 84 684 170 HOH HOH B . 
BA 8 HOH 85 685 168 HOH HOH B . 
BA 8 HOH 86 686 129 HOH HOH B . 
BA 8 HOH 87 687 302 HOH HOH B . 
BA 8 HOH 88 688 180 HOH HOH B . 
BA 8 HOH 89 689 121 HOH HOH B . 
BA 8 HOH 90 690 218 HOH HOH B . 
BA 8 HOH 91 691 117 HOH HOH B . 
BA 8 HOH 92 692 277 HOH HOH B . 
BA 8 HOH 93 693 271 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? .           1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.19.2-4158 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.09 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YNQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     95.856 
_cell.length_a_esd                 ? 
_cell.length_b                     97.518 
_cell.length_b_esd                 ? 
_cell.length_c                     101.514 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8YNQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8YNQ 
_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             2.41 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.99 
_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, SITTING 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    'MgCl2.6H2O, Tris, PEG smear High, Glycerol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_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                         'STFC Large Pixel Detector' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-11-22 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97915 
_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 BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97915 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YNQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.45 
_reflns.d_resolution_low                               50.00 
_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                                     68197 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.819 
_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                                0.184 
_reflns.pdbx_Rpim_I_all                                0.100 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       219848 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.941 
_reflns.pdbx_CC_star                                   0.985 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.154 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_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 
_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 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_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 
2.45 2.49  ? ? ? ? ? ? 3316 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.684 ? ? 0.600 0.336 ? 1  1 0.793 0.940 ? 97.8  ? 0.495 ? ? ? ? ? ? ? ? ? 
2.49 2.54  ? ? ? ? ? ? 3385 ? ? ? ? ? ? ? ? ? ? ? 2.9 0.646 ? ? 0.552 0.303 ? 2  1 0.813 0.947 ? 99.2  ? 0.459 ? ? ? ? ? ? ? ? ? 
2.54 2.59  ? ? ? ? ? ? 3387 ? ? ? ? ? ? ? ? ? ? ? 3.0 0.671 ? ? 0.539 0.293 ? 3  1 0.856 0.960 ? 99.4  ? 0.450 ? ? ? ? ? ? ? ? ? 
2.59 2.64  ? ? ? ? ? ? 3354 ? ? ? ? ? ? ? ? ? ? ? 3.1 0.681 ? ? 0.534 0.289 ? 4  1 0.830 0.952 ? 99.3  ? 0.446 ? ? ? ? ? ? ? ? ? 
2.64 2.70  ? ? ? ? ? ? 3398 ? ? ? ? ? ? ? ? ? ? ? 3.1 0.703 ? ? 0.492 0.268 ? 5  1 0.830 0.953 ? 99.7  ? 0.411 ? ? ? ? ? ? ? ? ? 
2.70 2.76  ? ? ? ? ? ? 3392 ? ? ? ? ? ? ? ? ? ? ? 3.1 0.739 ? ? 0.417 0.229 ? 6  1 0.900 0.973 ? 99.9  ? 0.346 ? ? ? ? ? ? ? ? ? 
2.76 2.83  ? ? ? ? ? ? 3426 ? ? ? ? ? ? ? ? ? ? ? 3.3 0.757 ? ? 0.378 0.203 ? 7  1 0.910 0.976 ? 99.8  ? 0.317 ? ? ? ? ? ? ? ? ? 
2.83 2.90  ? ? ? ? ? ? 3387 ? ? ? ? ? ? ? ? ? ? ? 3.2 0.803 ? ? 0.363 0.198 ? 8  1 0.887 0.970 ? 99.7  ? 0.303 ? ? ? ? ? ? ? ? ? 
2.90 2.99  ? ? ? ? ? ? 3423 ? ? ? ? ? ? ? ? ? ? ? 3.4 0.816 ? ? 0.321 0.172 ? 9  1 0.918 0.978 ? 99.9  ? 0.270 ? ? ? ? ? ? ? ? ? 
2.99 3.09  ? ? ? ? ? ? 3410 ? ? ? ? ? ? ? ? ? ? ? 3.4 0.846 ? ? 0.291 0.155 ? 10 1 0.910 0.976 ? 99.9  ? 0.245 ? ? ? ? ? ? ? ? ? 
3.09 3.20  ? ? ? ? ? ? 3409 ? ? ? ? ? ? ? ? ? ? ? 3.4 0.961 ? ? 0.264 0.141 ? 11 1 0.925 0.980 ? 99.7  ? 0.222 ? ? ? ? ? ? ? ? ? 
3.20 3.32  ? ? ? ? ? ? 3385 ? ? ? ? ? ? ? ? ? ? ? 3.3 0.998 ? ? 0.235 0.127 ? 12 1 0.927 0.981 ? 99.9  ? 0.196 ? ? ? ? ? ? ? ? ? 
3.32 3.48  ? ? ? ? ? ? 3421 ? ? ? ? ? ? ? ? ? ? ? 3.3 1.023 ? ? 0.214 0.116 ? 13 1 0.926 0.981 ? 100.0 ? 0.179 ? ? ? ? ? ? ? ? ? 
3.48 3.66  ? ? ? ? ? ? 3406 ? ? ? ? ? ? ? ? ? ? ? 3.2 1.091 ? ? 0.200 0.110 ? 14 1 0.927 0.981 ? 99.8  ? 0.167 ? ? ? ? ? ? ? ? ? 
3.66 3.89  ? ? ? ? ? ? 3439 ? ? ? ? ? ? ? ? ? ? ? 3.4 1.001 ? ? 0.178 0.095 ? 15 1 0.952 0.988 ? 99.9  ? 0.150 ? ? ? ? ? ? ? ? ? 
3.89 4.19  ? ? ? ? ? ? 3389 ? ? ? ? ? ? ? ? ? ? ? 3.4 0.971 ? ? 0.168 0.090 ? 16 1 0.944 0.986 ? 99.9  ? 0.141 ? ? ? ? ? ? ? ? ? 
4.19 4.61  ? ? ? ? ? ? 3461 ? ? ? ? ? ? ? ? ? ? ? 3.3 0.900 ? ? 0.159 0.086 ? 17 1 0.956 0.989 ? 99.8  ? 0.134 ? ? ? ? ? ? ? ? ? 
4.61 5.28  ? ? ? ? ? ? 3430 ? ? ? ? ? ? ? ? ? ? ? 3.3 0.777 ? ? 0.146 0.079 ? 18 1 0.956 0.989 ? 100.0 ? 0.123 ? ? ? ? ? ? ? ? ? 
5.28 6.65  ? ? ? ? ? ? 3455 ? ? ? ? ? ? ? ? ? ? ? 3.3 0.650 ? ? 0.135 0.073 ? 19 1 0.952 0.988 ? 99.9  ? 0.113 ? ? ? ? ? ? ? ? ? 
6.65 50.00 ? ? ? ? ? ? 3524 ? ? ? ? ? ? ? ? ? ? ? 3.2 0.539 ? ? 0.109 0.060 ? 20 1 0.970 0.992 ? 99.4  ? 0.091 ? ? ? ? ? ? ? ? ? 
# 
_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                                 8YNQ 
_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                            2.45 
_refine.ls_d_res_low                             47.93 
_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                     57209 
_refine.ls_number_reflns_R_free                  2728 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    83.14 
_refine.ls_percent_reflns_R_free                 4.77 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2378 
_refine.ls_R_factor_R_free                       0.3188 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2337 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.40 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      AlphaFold 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 37.90 
_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                            0.47 
_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.pdbx_number_atoms_protein        12595 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         219 
_refine_hist.number_atoms_solvent             325 
_refine_hist.number_atoms_total               13139 
_refine_hist.d_res_high                       2.45 
_refine_hist.d_res_low                        47.93 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  ? 13065 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.138  ? 17735 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.983 ? 1862  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.056  ? 1975  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 2308  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.45 2.49  . . 77  1018 30.00 . . . . 0.3320 . . . . . . . . . . . 0.4904 
'X-RAY DIFFRACTION' 2.49 2.54  . . 70  1446 43.00 . . . . 0.2967 . . . . . . . . . . . 0.4510 
'X-RAY DIFFRACTION' 2.54 2.59  . . 63  1641 48.00 . . . . 0.2795 . . . . . . . . . . . 0.3362 
'X-RAY DIFFRACTION' 2.59 2.65  . . 109 1957 57.00 . . . . 0.2951 . . . . . . . . . . . 0.3532 
'X-RAY DIFFRACTION' 2.65 2.71  . . 89  2268 66.00 . . . . 0.3114 . . . . . . . . . . . 0.3786 
'X-RAY DIFFRACTION' 2.71 2.78  . . 111 2668 77.00 . . . . 0.3108 . . . . . . . . . . . 0.4530 
'X-RAY DIFFRACTION' 2.78 2.86  . . 145 3008 88.00 . . . . 0.3077 . . . . . . . . . . . 0.3827 
'X-RAY DIFFRACTION' 2.86 2.94  . . 143 3205 93.00 . . . . 0.3085 . . . . . . . . . . . 0.3958 
'X-RAY DIFFRACTION' 2.94 3.03  . . 127 3420 98.00 . . . . 0.2731 . . . . . . . . . . . 0.3978 
'X-RAY DIFFRACTION' 3.03 3.14  . . 200 3336 98.00 . . . . 0.2685 . . . . . . . . . . . 0.3999 
'X-RAY DIFFRACTION' 3.14 3.27  . . 163 3418 98.00 . . . . 0.2598 . . . . . . . . . . . 0.3265 
'X-RAY DIFFRACTION' 3.27 3.42  . . 212 3325 98.00 . . . . 0.2406 . . . . . . . . . . . 0.3318 
'X-RAY DIFFRACTION' 3.42 3.60  . . 201 3357 98.00 . . . . 0.2322 . . . . . . . . . . . 0.3324 
'X-RAY DIFFRACTION' 3.60 3.82  . . 185 3340 98.00 . . . . 0.2165 . . . . . . . . . . . 0.3149 
'X-RAY DIFFRACTION' 3.82 4.12  . . 184 3385 98.00 . . . . 0.1966 . . . . . . . . . . . 0.2764 
'X-RAY DIFFRACTION' 4.12 4.53  . . 227 3344 98.00 . . . . 0.1915 . . . . . . . . . . . 0.2512 
'X-RAY DIFFRACTION' 4.53 5.19  . . 196 3387 98.00 . . . . 0.2003 . . . . . . . . . . . 0.2866 
'X-RAY DIFFRACTION' 5.19 6.53  . . 149 3475 99.00 . . . . 0.2303 . . . . . . . . . . . 0.2991 
'X-RAY DIFFRACTION' 6.53 47.93 . . 77  3483 95.00 . . . . 0.1974 . . . . . . . . . . . 0.2666 
# 
_struct.entry_id                     8YNQ 
_struct.title                        'ATP-grasp peptide ligase from Streptomyces' 
_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        8YNQ 
_struct_keywords.text            'ATP-grasp enzymes, peptide ligase, Amide synthase, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
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 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 3 ? 
H  N N 4 ? 
I  N N 2 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 4 ? 
M  N N 5 ? 
N  N N 4 ? 
O  N N 6 ? 
P  N N 4 ? 
Q  N N 4 ? 
R  N N 4 ? 
S  N N 4 ? 
T  N N 3 ? 
U  N N 4 ? 
V  N N 4 ? 
W  N N 3 ? 
X  N N 7 ? 
Y  N N 8 ? 
Z  N N 8 ? 
AA N N 8 ? 
BA N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8YNQ 
_struct_ref.pdbx_db_accession          8YNQ 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8YNQ C 1 ? 448 ? 8YNQ 1 ? 448 ? 1 448 
2 1 8YNQ D 1 ? 448 ? 8YNQ 1 ? 448 ? 1 448 
3 1 8YNQ A 1 ? 448 ? 8YNQ 1 ? 448 ? 1 448 
4 1 8YNQ B 1 ? 448 ? 8YNQ 1 ? 448 ? 1 448 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7280  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  33220 ? 
2 'ABSA (A^2)' 6500  ? 
2 MORE         12    ? 
2 'SSA (A^2)'  33260 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,J,K,L,M,N,Y,Z   
2 1 C,D,O,P,Q,R,S,T,U,V,W,X,AA,BA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 THR A 33  ? ALA A 41  ? THR C 33  ALA C 41  5 ? 9  
HELX_P HELX_P2  AA2 ASP A 56  ? GLY A 66  ? ASP C 56  GLY C 66  1 ? 11 
HELX_P HELX_P3  AA3 ASP A 68  ? VAL A 72  ? ASP C 68  VAL C 72  5 ? 5  
HELX_P HELX_P4  AA4 SER A 82  ? ASP A 88  ? SER C 82  ASP C 88  1 ? 7  
HELX_P HELX_P5  AA5 ASP A 88  ? GLY A 100 ? ASP C 88  GLY C 100 1 ? 13 
HELX_P HELX_P6  AA6 THR A 113 ? LEU A 123 ? THR C 113 LEU C 123 1 ? 11 
HELX_P HELX_P7  AA7 GLY A 130 ? GLN A 136 ? GLY C 130 GLN C 136 1 ? 7  
HELX_P HELX_P8  AA8 ASN A 137 ? LEU A 142 ? ASN C 137 LEU C 142 1 ? 6  
HELX_P HELX_P9  AA9 MET A 144 ? GLY A 156 ? MET C 144 GLY C 156 1 ? 13 
HELX_P HELX_P10 AB1 GLY A 167 ? ILE A 179 ? GLY C 167 ILE C 179 1 ? 13 
HELX_P HELX_P11 AB2 GLN A 222 ? LEU A 234 ? GLN C 222 LEU C 234 1 ? 13 
HELX_P HELX_P12 AB3 PHE A 299 ? GLY A 317 ? PHE C 299 GLY C 317 1 ? 19 
HELX_P HELX_P13 AB4 GLY A 346 ? GLY A 358 ? GLY C 346 GLY C 358 1 ? 13 
HELX_P HELX_P14 AB5 ASP A 360 ? ASN A 364 ? ASP C 360 ASN C 364 5 ? 5  
HELX_P HELX_P15 AB6 GLY A 377 ? GLY A 389 ? GLY C 377 GLY C 389 1 ? 13 
HELX_P HELX_P16 AB7 ASP A 421 ? GLY A 437 ? ASP C 421 GLY C 437 1 ? 17 
HELX_P HELX_P17 AB8 THR B 34  ? ALA B 41  ? THR D 34  ALA D 41  5 ? 8  
HELX_P HELX_P18 AB9 ASP B 56  ? LEU B 65  ? ASP D 56  LEU D 65  1 ? 10 
HELX_P HELX_P19 AC1 ASP B 68  ? VAL B 72  ? ASP D 68  VAL D 72  5 ? 5  
HELX_P HELX_P20 AC2 SER B 82  ? ASP B 88  ? SER D 82  ASP D 88  1 ? 7  
HELX_P HELX_P21 AC3 ASP B 88  ? GLY B 100 ? ASP D 88  GLY D 100 1 ? 13 
HELX_P HELX_P22 AC4 THR B 113 ? ASN B 124 ? THR D 113 ASN D 124 1 ? 12 
HELX_P HELX_P23 AC5 GLY B 130 ? GLN B 136 ? GLY D 130 GLN D 136 1 ? 7  
HELX_P HELX_P24 AC6 ASN B 137 ? LEU B 141 ? ASN D 137 LEU D 141 5 ? 5  
HELX_P HELX_P25 AC7 MET B 144 ? GLY B 156 ? MET D 144 GLY D 156 1 ? 13 
HELX_P HELX_P26 AC8 GLY B 167 ? ILE B 179 ? GLY D 167 ILE D 179 1 ? 13 
HELX_P HELX_P27 AC9 LEU B 223 ? THR B 235 ? LEU D 223 THR D 235 1 ? 13 
HELX_P HELX_P28 AD1 PHE B 299 ? GLY B 317 ? PHE D 299 GLY D 317 1 ? 19 
HELX_P HELX_P29 AD2 GLY B 346 ? LEU B 357 ? GLY D 346 LEU D 357 1 ? 12 
HELX_P HELX_P30 AD3 ASP B 360 ? ASN B 364 ? ASP D 360 ASN D 364 5 ? 5  
HELX_P HELX_P31 AD4 GLY B 377 ? GLY B 389 ? GLY D 377 GLY D 389 1 ? 13 
HELX_P HELX_P32 AD5 ASP B 421 ? GLY B 437 ? ASP D 421 GLY D 437 1 ? 17 
HELX_P HELX_P33 AD6 ASP C 32  ? ALA C 41  ? ASP A 32  ALA A 41  5 ? 10 
HELX_P HELX_P34 AD7 ASP C 56  ? GLY C 66  ? ASP A 56  GLY A 66  1 ? 11 
HELX_P HELX_P35 AD8 SER C 82  ? ASP C 88  ? SER A 82  ASP A 88  1 ? 7  
HELX_P HELX_P36 AD9 ASP C 88  ? THR C 99  ? ASP A 88  THR A 99  1 ? 12 
HELX_P HELX_P37 AE1 THR C 113 ? LEU C 123 ? THR A 113 LEU A 123 1 ? 11 
HELX_P HELX_P38 AE2 GLY C 130 ? MET C 135 ? GLY A 130 MET A 135 1 ? 6  
HELX_P HELX_P39 AE3 ASN C 137 ? LEU C 142 ? ASN A 137 LEU A 142 1 ? 6  
HELX_P HELX_P40 AE4 MET C 144 ? GLY C 156 ? MET A 144 GLY A 156 1 ? 13 
HELX_P HELX_P41 AE5 GLY C 167 ? ILE C 179 ? GLY A 167 ILE A 179 1 ? 13 
HELX_P HELX_P42 AE6 ALA C 219 ? ASP C 221 ? ALA A 219 ASP A 221 5 ? 3  
HELX_P HELX_P43 AE7 GLN C 222 ? LEU C 234 ? GLN A 222 LEU A 234 1 ? 13 
HELX_P HELX_P44 AE8 PHE C 299 ? GLY C 317 ? PHE A 299 GLY A 317 1 ? 19 
HELX_P HELX_P45 AE9 GLY C 346 ? GLY C 358 ? GLY A 346 GLY A 358 1 ? 13 
HELX_P HELX_P46 AF1 ASP C 360 ? ASN C 364 ? ASP A 360 ASN A 364 5 ? 5  
HELX_P HELX_P47 AF2 GLY C 377 ? GLY C 389 ? GLY A 377 GLY A 389 1 ? 13 
HELX_P HELX_P48 AF3 ASP C 421 ? ALA C 436 ? ASP A 421 ALA A 436 1 ? 16 
HELX_P HELX_P49 AF4 THR D 34  ? ALA D 41  ? THR B 34  ALA B 41  5 ? 8  
HELX_P HELX_P50 AF5 ASP D 56  ? GLY D 66  ? ASP B 56  GLY B 66  1 ? 11 
HELX_P HELX_P51 AF6 ASP D 68  ? VAL D 72  ? ASP B 68  VAL B 72  5 ? 5  
HELX_P HELX_P52 AF7 SER D 82  ? ASP D 88  ? SER B 82  ASP B 88  1 ? 7  
HELX_P HELX_P53 AF8 ASP D 88  ? GLY D 100 ? ASP B 88  GLY B 100 1 ? 13 
HELX_P HELX_P54 AF9 THR D 113 ? LYS D 122 ? THR B 113 LYS B 122 1 ? 10 
HELX_P HELX_P55 AG1 GLY D 130 ? GLN D 136 ? GLY B 130 GLN B 136 1 ? 7  
HELX_P HELX_P56 AG2 ASN D 137 ? LEU D 142 ? ASN B 137 LEU B 142 1 ? 6  
HELX_P HELX_P57 AG3 MET D 144 ? GLY D 156 ? MET B 144 GLY B 156 1 ? 13 
HELX_P HELX_P58 AG4 GLY D 167 ? ILE D 179 ? GLY B 167 ILE B 179 1 ? 13 
HELX_P HELX_P59 AG5 GLN D 222 ? THR D 235 ? GLN B 222 THR B 235 1 ? 14 
HELX_P HELX_P60 AG6 PHE D 299 ? GLY D 317 ? PHE B 299 GLY B 317 1 ? 19 
HELX_P HELX_P61 AG7 GLY D 346 ? GLY D 358 ? GLY B 346 GLY B 358 1 ? 13 
HELX_P HELX_P62 AG8 ASP D 360 ? ASN D 365 ? ASP B 360 ASN B 365 1 ? 6  
HELX_P HELX_P63 AG9 GLY D 377 ? GLY D 389 ? GLY B 377 GLY B 389 1 ? 13 
HELX_P HELX_P64 AH1 ASP D 421 ? GLY D 437 ? ASP B 421 GLY B 437 1 ? 17 
# 
_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 ? 2 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
AA8 ? 5 ? 
AA9 ? 3 ? 
AB1 ? 2 ? 
AB2 ? 5 ? 
AB3 ? 2 ? 
AB4 ? 5 ? 
AB5 ? 3 ? 
AB6 ? 2 ? 
AB7 ? 5 ? 
AB8 ? 5 ? 
AB9 ? 3 ? 
# 
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      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? parallel      
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? parallel      
AB3 1 2 ? parallel      
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB6 1 2 ? parallel      
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB7 4 5 ? parallel      
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 46  ? ILE A 49  ? VAL C 46  ILE C 49  
AA1 2 HIS A 73  ? ARG A 76  ? HIS C 73  ARG C 76  
AA2 1 GLY A 162 ? ALA A 165 ? GLY C 162 ALA C 165 
AA2 2 ILE A 242 ? THR A 246 ? ILE C 242 THR C 246 
AA2 3 MET A 184 ? GLN A 189 ? MET C 184 GLN C 189 
AA2 4 ASN A 198 ? SER A 202 ? ASN C 198 SER C 202 
AA2 5 GLU A 214 ? ALA A 217 ? GLU C 214 ALA C 217 
AA3 1 PHE A 209 ? PRO A 210 ? PHE C 209 PRO C 210 
AA3 2 SER A 285 ? ALA A 286 ? SER C 285 ALA C 286 
AA4 1 TRP A 288 ? ASP A 292 ? TRP C 288 ASP C 292 
AA4 2 ALA A 265 ? TYR A 275 ? ALA C 265 TYR C 275 
AA4 3 GLN A 252 ? LEU A 260 ? GLN C 252 LEU C 260 
AA4 4 GLY A 320 ? VAL A 328 ? GLY C 320 VAL C 328 
AA4 5 VAL A 334 ? ASN A 340 ? VAL C 334 ASN C 340 
AA5 1 PHE A 366 ? VAL A 373 ? PHE C 366 VAL C 373 
AA5 2 ALA A 413 ? SER A 419 ? ALA C 413 SER C 419 
AA5 3 GLY A 399 ? GLY A 404 ? GLY C 399 GLY C 404 
AA6 1 VAL B 46  ? ILE B 49  ? VAL D 46  ILE D 49  
AA6 2 HIS B 73  ? ARG B 76  ? HIS D 73  ARG D 76  
AA7 1 GLY B 162 ? ALA B 165 ? GLY D 162 ALA D 165 
AA7 2 ILE B 242 ? THR B 246 ? ILE D 242 THR D 246 
AA7 3 MET B 184 ? GLN B 189 ? MET D 184 GLN D 189 
AA7 4 ASN B 198 ? SER B 202 ? ASN D 198 SER D 202 
AA7 5 VAL B 215 ? ALA B 217 ? VAL D 215 ALA D 217 
AA8 1 TRP B 288 ? ASP B 292 ? TRP D 288 ASP D 292 
AA8 2 ALA B 265 ? TYR B 275 ? ALA D 265 TYR D 275 
AA8 3 GLN B 252 ? LEU B 260 ? GLN D 252 LEU D 260 
AA8 4 TYR B 321 ? VAL B 328 ? TYR D 321 VAL D 328 
AA8 5 VAL B 334 ? ASN B 340 ? VAL D 334 ASN D 340 
AA9 1 PHE B 366 ? VAL B 373 ? PHE D 366 VAL D 373 
AA9 2 ALA B 413 ? SER B 419 ? ALA D 413 SER D 419 
AA9 3 GLY B 399 ? VAL B 402 ? GLY D 399 VAL D 402 
AB1 1 VAL C 46  ? ILE C 49  ? VAL A 46  ILE A 49  
AB1 2 HIS C 73  ? ARG C 76  ? HIS A 73  ARG A 76  
AB2 1 GLY C 162 ? ALA C 165 ? GLY A 162 ALA A 165 
AB2 2 ILE C 242 ? THR C 246 ? ILE A 242 THR A 246 
AB2 3 MET C 184 ? GLN C 189 ? MET A 184 GLN A 189 
AB2 4 ASN C 198 ? SER C 202 ? ASN A 198 SER A 202 
AB2 5 GLU C 214 ? ALA C 217 ? GLU A 214 ALA A 217 
AB3 1 SER C 208 ? PRO C 210 ? SER A 208 PRO A 210 
AB3 2 GLY C 284 ? ALA C 286 ? GLY A 284 ALA A 286 
AB4 1 TRP C 288 ? ASP C 292 ? TRP A 288 ASP A 292 
AB4 2 ALA C 265 ? TYR C 275 ? ALA A 265 TYR A 275 
AB4 3 GLN C 252 ? LEU C 260 ? GLN A 252 LEU A 260 
AB4 4 GLY C 320 ? VAL C 328 ? GLY A 320 VAL A 328 
AB4 5 VAL C 334 ? ASN C 340 ? VAL A 334 ASN A 340 
AB5 1 PHE C 366 ? VAL C 373 ? PHE A 366 VAL A 373 
AB5 2 ALA C 413 ? SER C 419 ? ALA A 413 SER A 419 
AB5 3 GLY C 399 ? GLY C 404 ? GLY A 399 GLY A 404 
AB6 1 VAL D 46  ? ILE D 49  ? VAL B 46  ILE B 49  
AB6 2 HIS D 73  ? ARG D 76  ? HIS B 73  ARG B 76  
AB7 1 GLY D 162 ? ALA D 165 ? GLY B 162 ALA B 165 
AB7 2 ILE D 242 ? THR D 246 ? ILE B 242 THR B 246 
AB7 3 MET D 184 ? GLN D 189 ? MET B 184 GLN B 189 
AB7 4 ASN D 198 ? SER D 202 ? ASN B 198 SER B 202 
AB7 5 GLU D 214 ? ALA D 217 ? GLU B 214 ALA B 217 
AB8 1 LYS D 287 ? ASP D 292 ? LYS B 287 ASP B 292 
AB8 2 ALA D 265 ? GLU D 276 ? ALA B 265 GLU B 276 
AB8 3 GLN D 252 ? LEU D 260 ? GLN B 252 LEU B 260 
AB8 4 GLY D 320 ? VAL D 328 ? GLY B 320 VAL B 328 
AB8 5 VAL D 334 ? ASN D 340 ? VAL B 334 ASN B 340 
AB9 1 PHE D 366 ? VAL D 373 ? PHE B 366 VAL B 373 
AB9 2 GLY D 412 ? SER D 419 ? GLY B 412 SER B 419 
AB9 3 GLY D 399 ? SER D 407 ? GLY B 399 SER B 407 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 47  ? N LEU C 47  O GLU A 75  ? O GLU C 75  
AA2 1 2 N ALA A 165 ? N ALA C 165 O ILE A 242 ? O ILE C 242 
AA2 2 3 O GLU A 245 ? O GLU C 245 N ILE A 186 ? N ILE C 186 
AA2 3 4 N ALA A 187 ? N ALA C 187 O ILE A 199 ? O ILE C 199 
AA2 4 5 N GLY A 200 ? N GLY C 200 O GLU A 214 ? O GLU C 214 
AA3 1 2 N PHE A 209 ? N PHE C 209 O ALA A 286 ? O ALA C 286 
AA4 1 2 O ASP A 292 ? O ASP C 292 N ILE A 272 ? N ILE C 272 
AA4 2 3 O LEU A 273 ? O LEU C 273 N ARG A 253 ? N ARG C 253 
AA4 3 4 N PHE A 254 ? N PHE C 254 O GLY A 326 ? O GLY C 326 
AA4 4 5 N ILE A 327 ? N ILE C 327 O PHE A 335 ? O PHE C 335 
AA5 1 2 N SER A 368 ? N SER C 368 O VAL A 417 ? O VAL C 417 
AA5 2 3 O GLU A 414 ? O GLU C 414 N LEU A 403 ? N LEU C 403 
AA6 1 2 N LEU B 47  ? N LEU D 47  O GLU B 75  ? O GLU D 75  
AA7 1 2 N ALA B 165 ? N ALA D 165 O ILE B 242 ? O ILE D 242 
AA7 2 3 O GLU B 245 ? O GLU D 245 N ILE B 186 ? N ILE D 186 
AA7 3 4 N ALA B 187 ? N ALA D 187 O ILE B 199 ? O ILE D 199 
AA7 4 5 N GLY B 200 ? N GLY D 200 O LEU B 216 ? O LEU D 216 
AA8 1 2 O GLY B 290 ? O GLY D 290 N LYS B 274 ? N LYS D 274 
AA8 2 3 O LEU B 273 ? O LEU D 273 N ARG B 253 ? N ARG D 253 
AA8 3 4 N TYR B 258 ? N TYR D 258 O VAL B 322 ? O VAL D 322 
AA8 4 5 N ILE B 327 ? N ILE D 327 O PHE B 335 ? O PHE D 335 
AA9 1 2 N VAL B 373 ? N VAL D 373 O ALA B 413 ? O ALA D 413 
AA9 2 3 O PHE B 418 ? O PHE D 418 N GLY B 399 ? N GLY D 399 
AB1 1 2 N LEU C 47  ? N LEU A 47  O GLU C 75  ? O GLU A 75  
AB2 1 2 N ALA C 165 ? N ALA A 165 O ILE C 242 ? O ILE A 242 
AB2 2 3 O GLU C 245 ? O GLU A 245 N ILE C 186 ? N ILE A 186 
AB2 3 4 N ALA C 187 ? N ALA A 187 O ILE C 199 ? O ILE A 199 
AB2 4 5 N SER C 202 ? N SER A 202 O LEU C 216 ? O LEU A 216 
AB3 1 2 N PHE C 209 ? N PHE A 209 O GLY C 284 ? O GLY A 284 
AB4 1 2 O GLY C 290 ? O GLY A 290 N LYS C 274 ? N LYS A 274 
AB4 2 3 O LEU C 268 ? O LEU A 268 N GLU C 257 ? N GLU A 257 
AB4 3 4 N TYR C 258 ? N TYR A 258 O VAL C 322 ? O VAL A 322 
AB4 4 5 N ILE C 327 ? N ILE A 327 O PHE C 335 ? O PHE A 335 
AB5 1 2 N VAL C 373 ? N VAL A 373 O ALA C 413 ? O ALA A 413 
AB5 2 3 O PHE C 418 ? O PHE A 418 N GLY C 399 ? N GLY A 399 
AB6 1 2 N LEU D 47  ? N LEU B 47  O GLU D 75  ? O GLU B 75  
AB7 1 2 N ALA D 165 ? N ALA B 165 O ILE D 242 ? O ILE B 242 
AB7 2 3 O GLU D 245 ? O GLU B 245 N ILE D 186 ? N ILE B 186 
AB7 3 4 N VAL D 185 ? N VAL B 185 O ILE D 201 ? O ILE B 201 
AB7 4 5 N GLY D 200 ? N GLY B 200 O LEU D 216 ? O LEU B 216 
AB8 1 2 O ILE D 289 ? O ILE B 289 N LYS D 274 ? N LYS B 274 
AB8 2 3 O LEU D 273 ? O LEU B 273 N ARG D 253 ? N ARG B 253 
AB8 3 4 N TYR D 258 ? N TYR B 258 O VAL D 322 ? O VAL B 322 
AB8 4 5 N ILE D 327 ? N ILE B 327 O PHE D 335 ? O PHE B 335 
AB9 1 2 N VAL D 373 ? N VAL B 373 O ALA D 413 ? O ALA B 413 
AB9 2 3 O LEU D 416 ? O LEU B 416 N VAL D 401 ? N VAL B 401 
# 
_pdbx_entry_details.entry_id                   8YNQ 
_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 O   B VAL 125 ? ? O   B HOH 601 ? ? 1.93 
2  1 O   B LEU 260 ? ? O   B HOH 602 ? ? 1.95 
3  1 O   A ALA 433 ? ? O   A HOH 601 ? ? 1.95 
4  1 O   B LEU 151 ? ? O   B HOH 603 ? ? 1.96 
5  1 O   C HOH 624 ? ? O   C HOH 663 ? ? 1.96 
6  1 O   A VAL 215 ? ? O   A HOH 602 ? ? 1.96 
7  1 O   A THR 77  ? ? O   A HOH 603 ? ? 1.98 
8  1 O   D SER 344 ? ? O   D HOH 601 ? ? 1.98 
9  1 O   A GLU 132 ? ? O   A HOH 604 ? ? 2.00 
10 1 O   A HOH 612 ? ? O   A HOH 660 ? ? 2.01 
11 1 O   D HOH 645 ? ? O   D HOH 676 ? ? 2.02 
12 1 O   A HOH 671 ? ? O   B HOH 682 ? ? 2.02 
13 1 O   A LEU 409 ? ? O   A HOH 605 ? ? 2.03 
14 1 OE2 B GLU 338 ? ? O   B HOH 604 ? ? 2.03 
15 1 O   C HOH 616 ? ? O   D HOH 669 ? ? 2.05 
16 1 O   B ALA 400 ? ? O   B HOH 605 ? ? 2.05 
17 1 O   D HOH 657 ? ? O   D HOH 662 ? ? 2.05 
18 1 OD1 D ASN 198 ? ? O   D HOH 602 ? ? 2.06 
19 1 O   D HOH 640 ? ? O   D HOH 641 ? ? 2.07 
20 1 N   B LEU 155 ? ? O   B HOH 603 ? ? 2.07 
21 1 O   D HOH 664 ? ? O   D HOH 685 ? ? 2.08 
22 1 O   B ALA 362 ? ? O   B HOH 606 ? ? 2.09 
23 1 O   A ARG 166 ? ? O   A HOH 606 ? ? 2.09 
24 1 OG  B SER 440 ? ? O   B HOH 607 ? ? 2.09 
25 1 N   B SER 112 ? ? O   B HOH 608 ? ? 2.09 
26 1 O   B HOH 653 ? ? O   B HOH 656 ? ? 2.10 
27 1 N   B GLY 154 ? ? O   B HOH 603 ? ? 2.10 
28 1 O3  B GOL 503 ? ? O   B HOH 609 ? ? 2.10 
29 1 O   D HOH 603 ? ? O   D HOH 671 ? ? 2.11 
30 1 O   D GLU 206 ? ? O   D HOH 603 ? ? 2.11 
31 1 O   A HOH 623 ? ? O   A HOH 644 ? ? 2.12 
32 1 O   D GLY 410 ? ? O   D HOH 604 ? ? 2.12 
33 1 OD2 B ASP 56  ? ? O   B HOH 610 ? ? 2.13 
34 1 OG  C SER 293 ? ? O   C HOH 601 ? ? 2.13 
35 1 O   C HOH 609 ? ? O   C HOH 627 ? ? 2.14 
36 1 OD2 B ASP 325 ? ? O   B HOH 604 ? ? 2.14 
37 1 O   A THR 99  ? ? O   A HOH 607 ? ? 2.14 
38 1 NH2 C ARG 166 ? ? OE2 C GLU 170 ? ? 2.15 
39 1 O   B HOH 690 ? ? O   B HOH 692 ? ? 2.15 
40 1 O1  A PEG 502 ? ? O   A HOH 608 ? ? 2.15 
41 1 O   B GLY 262 ? ? O   B HOH 611 ? ? 2.15 
42 1 NE  D ARG 213 ? ? O   D HOH 605 ? ? 2.15 
43 1 N   A LYS 394 ? ? O   A HOH 609 ? ? 2.16 
44 1 O   C HIS 98  ? ? O   C HOH 602 ? ? 2.16 
45 1 OG  A SER 192 ? ? O   A HOH 610 ? ? 2.16 
46 1 OE1 C GLN 277 ? ? O   C HOH 603 ? ? 2.17 
47 1 O   D GLY 397 ? ? O   D HOH 606 ? ? 2.17 
48 1 O2  B GOL 503 ? ? O   B HOH 612 ? ? 2.17 
49 1 O4  B PEG 501 ? ? O   B HOH 613 ? ? 2.17 
50 1 O   A HOH 637 ? ? O   A HOH 643 ? ? 2.17 
51 1 OD1 A ASP 93  ? ? O   A HOH 611 ? ? 2.18 
52 1 O   B HOH 629 ? ? O   B HOH 645 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O C HOH 657 ? ? 1_555 O B HOH 669 ? ? 1_556 2.08 
2 1 O C HOH 602 ? ? 1_555 O A HOH 666 ? ? 2_445 2.15 
3 1 O C HOH 631 ? ? 1_555 O A HOH 660 ? ? 2_545 2.15 
# 
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 SER C 30  ? ? 177.02  -127.70 
2  1 ASP C 43  ? ? -36.33  126.46  
3  1 THR C 113 ? ? -68.90  -173.92 
4  1 TYR C 131 ? ? -26.64  -70.19  
5  1 LEU C 142 ? ? -49.26  171.47  
6  1 ASN C 143 ? ? 69.58   -8.09   
7  1 GLU C 206 ? ? 95.41   17.24   
8  1 PHE C 209 ? ? -113.56 74.05   
9  1 GLU C 280 ? ? 36.96   32.50   
10 1 SER C 293 ? ? -94.46  -76.86  
11 1 PRO C 294 ? ? -47.26  92.32   
12 1 ARG C 296 ? ? -107.12 41.57   
13 1 ARG C 342 ? ? -175.01 -175.90 
14 1 ASP C 360 ? ? -93.71  42.85   
15 1 ASN C 406 ? ? -160.89 73.35   
16 1 LEU C 409 ? ? -53.34  105.34  
17 1 PRO C 411 ? ? -88.54  -106.11 
18 1 ASP D 51  ? ? -95.78  -158.20 
19 1 SER D 192 ? ? 178.79  165.58  
20 1 ARG D 213 ? ? -107.51 -75.83  
21 1 ALA D 219 ? ? -162.03 101.17  
22 1 ASP D 236 ? ? -138.89 -148.24 
23 1 HIS D 269 ? ? -170.95 -177.25 
24 1 GLU D 276 ? ? -163.03 -132.54 
25 1 SER D 293 ? ? -66.54  -147.21 
26 1 ARG D 296 ? ? -82.74  44.81   
27 1 SER D 297 ? ? -161.30 87.34   
28 1 GLU D 298 ? ? -157.99 66.94   
29 1 ASN D 406 ? ? -163.51 82.71   
30 1 LYS D 420 ? ? -68.35  2.18    
31 1 PRO A 50  ? ? -70.64  -152.77 
32 1 ASP A 51  ? ? 34.44   -140.75 
33 1 PRO A 55  ? ? -39.47  -28.33  
34 1 ASP A 68  ? ? -65.46  98.54   
35 1 LEU A 81  ? ? -84.16  42.99   
36 1 THR A 101 ? ? 68.30   -14.32  
37 1 SER A 112 ? ? -62.02  73.14   
38 1 GLN A 136 ? ? 69.06   -7.12   
39 1 LEU A 159 ? ? -163.21 116.43  
40 1 THR A 182 ? ? -140.23 -23.21  
41 1 PHE A 209 ? ? -152.82 71.94   
42 1 ARG A 264 ? ? -171.33 147.73  
43 1 SER A 293 ? ? -80.66  -143.81 
44 1 ARG A 296 ? ? -97.44  36.00   
45 1 GLU A 298 ? ? -104.61 68.08   
46 1 ASP A 331 ? ? -57.96  -9.46   
47 1 ASN A 406 ? ? -170.49 70.91   
48 1 SER A 419 ? ? -173.79 142.81  
49 1 LEU A 439 ? ? -107.07 58.77   
50 1 THR B 34  ? ? 66.02   -6.44   
51 1 ASP B 51  ? ? -105.09 -157.24 
52 1 THR B 113 ? ? -57.68  171.53  
53 1 VAL B 125 ? ? -97.89  -79.66  
54 1 LEU B 142 ? ? -64.06  -172.92 
55 1 ASN B 143 ? ? 55.11   12.95   
56 1 ASP B 263 ? ? -99.42  -66.74  
57 1 TYR B 275 ? ? -127.19 -167.04 
58 1 SER B 293 ? ? -55.94  -172.32 
59 1 PRO B 294 ? ? -7.76   121.00  
60 1 ARG B 342 ? ? -170.40 -174.15 
61 1 SER B 368 ? ? -171.85 136.44  
62 1 ASN B 372 ? ? 63.63   -4.63   
63 1 ASN B 406 ? ? -152.94 75.38   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ASP 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    292 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   SER 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    293 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -148.96 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     149 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.089 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? D HOH 689 ? 5.82 .    
2 1 O ? D HOH 690 ? .    6.12 
# 
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 C MET 1   ? A MET 1   
2   1 Y 1 C PRO 2   ? A PRO 2   
3   1 Y 1 C LYS 3   ? A LYS 3   
4   1 Y 1 C ILE 4   ? A ILE 4   
5   1 Y 1 C ILE 5   ? A ILE 5   
6   1 Y 1 C LEU 6   ? A LEU 6   
7   1 Y 1 C PRO 7   ? A PRO 7   
8   1 Y 1 C ASN 8   ? A ASN 8   
9   1 Y 1 C PHE 9   ? A PHE 9   
10  1 Y 1 C ARG 10  ? A ARG 10  
11  1 Y 1 C ALA 11  ? A ALA 11  
12  1 Y 1 C ASP 12  ? A ASP 12  
13  1 Y 1 C TYR 13  ? A TYR 13  
14  1 Y 1 C SER 14  ? A SER 14  
15  1 Y 1 C GLU 15  ? A GLU 15  
16  1 Y 1 C GLN 16  ? A GLN 16  
17  1 Y 1 C VAL 17  ? A VAL 17  
18  1 Y 1 C ARG 18  ? A ARG 18  
19  1 Y 1 C ASP 19  ? A ASP 19  
20  1 Y 1 C TRP 20  ? A TRP 20  
21  1 Y 1 C LEU 21  ? A LEU 21  
22  1 Y 1 C GLY 22  ? A GLY 22  
23  1 Y 1 C ILE 23  ? A ILE 23  
24  1 Y 1 C SER 24  ? A SER 24  
25  1 Y 1 C ASP 25  ? A ASP 25  
26  1 Y 1 C ALA 26  ? A ALA 26  
27  1 Y 1 C THR 27  ? A THR 27  
28  1 Y 1 C ALA 28  ? A ALA 28  
29  1 Y 1 C LEU 441 ? A LEU 441 
30  1 Y 1 C GLU 442 ? A GLU 442 
31  1 Y 1 C HIS 443 ? A HIS 443 
32  1 Y 1 C HIS 444 ? A HIS 444 
33  1 Y 1 C HIS 445 ? A HIS 445 
34  1 Y 1 C HIS 446 ? A HIS 446 
35  1 Y 1 C HIS 447 ? A HIS 447 
36  1 Y 1 C HIS 448 ? A HIS 448 
37  1 Y 1 D MET 1   ? B MET 1   
38  1 Y 1 D PRO 2   ? B PRO 2   
39  1 Y 1 D LYS 3   ? B LYS 3   
40  1 Y 1 D ILE 4   ? B ILE 4   
41  1 Y 1 D ILE 5   ? B ILE 5   
42  1 Y 1 D LEU 6   ? B LEU 6   
43  1 Y 1 D PRO 7   ? B PRO 7   
44  1 Y 1 D ASN 8   ? B ASN 8   
45  1 Y 1 D PHE 9   ? B PHE 9   
46  1 Y 1 D ARG 10  ? B ARG 10  
47  1 Y 1 D ALA 11  ? B ALA 11  
48  1 Y 1 D ASP 12  ? B ASP 12  
49  1 Y 1 D TYR 13  ? B TYR 13  
50  1 Y 1 D SER 14  ? B SER 14  
51  1 Y 1 D GLU 15  ? B GLU 15  
52  1 Y 1 D GLN 16  ? B GLN 16  
53  1 Y 1 D VAL 17  ? B VAL 17  
54  1 Y 1 D ARG 18  ? B ARG 18  
55  1 Y 1 D ASP 19  ? B ASP 19  
56  1 Y 1 D TRP 20  ? B TRP 20  
57  1 Y 1 D LEU 21  ? B LEU 21  
58  1 Y 1 D GLY 22  ? B GLY 22  
59  1 Y 1 D ILE 23  ? B ILE 23  
60  1 Y 1 D SER 24  ? B SER 24  
61  1 Y 1 D ASP 25  ? B ASP 25  
62  1 Y 1 D ALA 26  ? B ALA 26  
63  1 Y 1 D THR 27  ? B THR 27  
64  1 Y 1 D ALA 28  ? B ALA 28  
65  1 Y 1 D SER 29  ? B SER 29  
66  1 Y 1 D GLY 281 ? B GLY 281 
67  1 Y 1 D SER 282 ? B SER 282 
68  1 Y 1 D GLY 283 ? B GLY 283 
69  1 Y 1 D GLY 284 ? B GLY 284 
70  1 Y 1 D LEU 441 ? B LEU 441 
71  1 Y 1 D GLU 442 ? B GLU 442 
72  1 Y 1 D HIS 443 ? B HIS 443 
73  1 Y 1 D HIS 444 ? B HIS 444 
74  1 Y 1 D HIS 445 ? B HIS 445 
75  1 Y 1 D HIS 446 ? B HIS 446 
76  1 Y 1 D HIS 447 ? B HIS 447 
77  1 Y 1 D HIS 448 ? B HIS 448 
78  1 Y 1 A MET 1   ? C MET 1   
79  1 Y 1 A PRO 2   ? C PRO 2   
80  1 Y 1 A LYS 3   ? C LYS 3   
81  1 Y 1 A ILE 4   ? C ILE 4   
82  1 Y 1 A ILE 5   ? C ILE 5   
83  1 Y 1 A LEU 6   ? C LEU 6   
84  1 Y 1 A PRO 7   ? C PRO 7   
85  1 Y 1 A ASN 8   ? C ASN 8   
86  1 Y 1 A PHE 9   ? C PHE 9   
87  1 Y 1 A ARG 10  ? C ARG 10  
88  1 Y 1 A ALA 11  ? C ALA 11  
89  1 Y 1 A ASP 12  ? C ASP 12  
90  1 Y 1 A TYR 13  ? C TYR 13  
91  1 Y 1 A SER 14  ? C SER 14  
92  1 Y 1 A GLU 15  ? C GLU 15  
93  1 Y 1 A GLN 16  ? C GLN 16  
94  1 Y 1 A VAL 17  ? C VAL 17  
95  1 Y 1 A ARG 18  ? C ARG 18  
96  1 Y 1 A ASP 19  ? C ASP 19  
97  1 Y 1 A TRP 20  ? C TRP 20  
98  1 Y 1 A LEU 21  ? C LEU 21  
99  1 Y 1 A GLY 22  ? C GLY 22  
100 1 Y 1 A ILE 23  ? C ILE 23  
101 1 Y 1 A SER 24  ? C SER 24  
102 1 Y 1 A ASP 25  ? C ASP 25  
103 1 Y 1 A ALA 26  ? C ALA 26  
104 1 Y 1 A THR 27  ? C THR 27  
105 1 Y 1 A ALA 28  ? C ALA 28  
106 1 Y 1 A SER 29  ? C SER 29  
107 1 Y 1 A GLY 281 ? C GLY 281 
108 1 Y 1 A LEU 441 ? C LEU 441 
109 1 Y 1 A GLU 442 ? C GLU 442 
110 1 Y 1 A HIS 443 ? C HIS 443 
111 1 Y 1 A HIS 444 ? C HIS 444 
112 1 Y 1 A HIS 445 ? C HIS 445 
113 1 Y 1 A HIS 446 ? C HIS 446 
114 1 Y 1 A HIS 447 ? C HIS 447 
115 1 Y 1 A HIS 448 ? C HIS 448 
116 1 Y 1 B MET 1   ? D MET 1   
117 1 Y 1 B PRO 2   ? D PRO 2   
118 1 Y 1 B LYS 3   ? D LYS 3   
119 1 Y 1 B ILE 4   ? D ILE 4   
120 1 Y 1 B ILE 5   ? D ILE 5   
121 1 Y 1 B LEU 6   ? D LEU 6   
122 1 Y 1 B PRO 7   ? D PRO 7   
123 1 Y 1 B ASN 8   ? D ASN 8   
124 1 Y 1 B PHE 9   ? D PHE 9   
125 1 Y 1 B ARG 10  ? D ARG 10  
126 1 Y 1 B ALA 11  ? D ALA 11  
127 1 Y 1 B ASP 12  ? D ASP 12  
128 1 Y 1 B TYR 13  ? D TYR 13  
129 1 Y 1 B SER 14  ? D SER 14  
130 1 Y 1 B GLU 15  ? D GLU 15  
131 1 Y 1 B GLN 16  ? D GLN 16  
132 1 Y 1 B VAL 17  ? D VAL 17  
133 1 Y 1 B ARG 18  ? D ARG 18  
134 1 Y 1 B ASP 19  ? D ASP 19  
135 1 Y 1 B TRP 20  ? D TRP 20  
136 1 Y 1 B LEU 21  ? D LEU 21  
137 1 Y 1 B GLY 22  ? D GLY 22  
138 1 Y 1 B ILE 23  ? D ILE 23  
139 1 Y 1 B SER 24  ? D SER 24  
140 1 Y 1 B ASP 25  ? D ASP 25  
141 1 Y 1 B ALA 26  ? D ALA 26  
142 1 Y 1 B THR 27  ? D THR 27  
143 1 Y 1 B ALA 28  ? D ALA 28  
144 1 Y 1 B SER 29  ? D SER 29  
145 1 Y 1 B GLN 277 ? D GLN 277 
146 1 Y 1 B LEU 278 ? D LEU 278 
147 1 Y 1 B PRO 279 ? D PRO 279 
148 1 Y 1 B GLU 280 ? D GLU 280 
149 1 Y 1 B GLY 283 ? D GLY 283 
150 1 Y 1 B LEU 441 ? D LEU 441 
151 1 Y 1 B GLU 442 ? D GLU 442 
152 1 Y 1 B HIS 443 ? D HIS 443 
153 1 Y 1 B HIS 444 ? D HIS 444 
154 1 Y 1 B HIS 445 ? D HIS 445 
155 1 Y 1 B HIS 446 ? D HIS 446 
156 1 Y 1 B HIS 447 ? D HIS 447 
157 1 Y 1 B HIS 448 ? D HIS 448 
# 
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 
ADP PB     P N N 1   
ADP O1B    O N N 2   
ADP O2B    O N N 3   
ADP O3B    O N N 4   
ADP PA     P N S 5   
ADP O1A    O N N 6   
ADP O2A    O N N 7   
ADP O3A    O N N 8   
ADP "O5'"  O N N 9   
ADP "C5'"  C N N 10  
ADP "C4'"  C N R 11  
ADP "O4'"  O N N 12  
ADP "C3'"  C N S 13  
ADP "O3'"  O N N 14  
ADP "C2'"  C N R 15  
ADP "O2'"  O N N 16  
ADP "C1'"  C N R 17  
ADP N9     N Y N 18  
ADP C8     C Y N 19  
ADP N7     N Y N 20  
ADP C5     C Y N 21  
ADP C6     C Y N 22  
ADP N6     N N N 23  
ADP N1     N Y N 24  
ADP C2     C Y N 25  
ADP N3     N Y N 26  
ADP C4     C Y N 27  
ADP HOB2   H N N 28  
ADP HOB3   H N N 29  
ADP HOA2   H N N 30  
ADP "H5'1" H N N 31  
ADP "H5'2" H N N 32  
ADP "H4'"  H N N 33  
ADP "H3'"  H N N 34  
ADP "HO3'" H N N 35  
ADP "H2'"  H N N 36  
ADP "HO2'" H N N 37  
ADP "H1'"  H N N 38  
ADP H8     H N N 39  
ADP HN61   H N N 40  
ADP HN62   H N N 41  
ADP H2     H N N 42  
ALA N      N N N 43  
ALA CA     C N S 44  
ALA C      C N N 45  
ALA O      O N N 46  
ALA CB     C N N 47  
ALA OXT    O N N 48  
ALA H      H N N 49  
ALA H2     H N N 50  
ALA HA     H N N 51  
ALA HB1    H N N 52  
ALA HB2    H N N 53  
ALA HB3    H N N 54  
ALA HXT    H N N 55  
AMP P      P N N 56  
AMP O1P    O N N 57  
AMP O2P    O N N 58  
AMP O3P    O N N 59  
AMP "O5'"  O N N 60  
AMP "C5'"  C N N 61  
AMP "C4'"  C N R 62  
AMP "O4'"  O N N 63  
AMP "C3'"  C N S 64  
AMP "O3'"  O N N 65  
AMP "C2'"  C N R 66  
AMP "O2'"  O N N 67  
AMP "C1'"  C N R 68  
AMP N9     N Y N 69  
AMP C8     C Y N 70  
AMP N7     N Y N 71  
AMP C5     C Y N 72  
AMP C6     C Y N 73  
AMP N6     N N N 74  
AMP N1     N Y N 75  
AMP C2     C Y N 76  
AMP N3     N Y N 77  
AMP C4     C Y N 78  
AMP HOP2   H N N 79  
AMP HOP3   H N N 80  
AMP "H5'1" H N N 81  
AMP "H5'2" H N N 82  
AMP "H4'"  H N N 83  
AMP "H3'"  H N N 84  
AMP "HO3'" H N N 85  
AMP "H2'"  H N N 86  
AMP "HO2'" H N N 87  
AMP "H1'"  H N N 88  
AMP H8     H N N 89  
AMP HN61   H N N 90  
AMP HN62   H N N 91  
AMP H2     H N N 92  
ANP PG     P N N 93  
ANP O1G    O N N 94  
ANP O2G    O N N 95  
ANP O3G    O N N 96  
ANP PB     P N N 97  
ANP O1B    O N N 98  
ANP O2B    O N N 99  
ANP N3B    N N N 100 
ANP PA     P N N 101 
ANP O1A    O N N 102 
ANP O2A    O N N 103 
ANP O3A    O N N 104 
ANP "O5'"  O N N 105 
ANP "C5'"  C N N 106 
ANP "C4'"  C N R 107 
ANP "O4'"  O N N 108 
ANP "C3'"  C N S 109 
ANP "O3'"  O N N 110 
ANP "C2'"  C N R 111 
ANP "O2'"  O N N 112 
ANP "C1'"  C N R 113 
ANP N9     N Y N 114 
ANP C8     C Y N 115 
ANP N7     N Y N 116 
ANP C5     C Y N 117 
ANP C6     C Y N 118 
ANP N6     N N N 119 
ANP N1     N Y N 120 
ANP C2     C Y N 121 
ANP N3     N Y N 122 
ANP C4     C Y N 123 
ANP HOG2   H N N 124 
ANP HOG3   H N N 125 
ANP HOB2   H N N 126 
ANP HNB1   H N N 127 
ANP HOA2   H N N 128 
ANP "H5'1" H N N 129 
ANP "H5'2" H N N 130 
ANP "H4'"  H N N 131 
ANP "H3'"  H N N 132 
ANP "HO3'" H N N 133 
ANP "H2'"  H N N 134 
ANP "HO2'" H N N 135 
ANP "H1'"  H N N 136 
ANP H8     H N N 137 
ANP HN61   H N N 138 
ANP HN62   H N N 139 
ANP H2     H N N 140 
ARG N      N N N 141 
ARG CA     C N S 142 
ARG C      C N N 143 
ARG O      O N N 144 
ARG CB     C N N 145 
ARG CG     C N N 146 
ARG CD     C N N 147 
ARG NE     N N N 148 
ARG CZ     C N N 149 
ARG NH1    N N N 150 
ARG NH2    N N N 151 
ARG OXT    O N N 152 
ARG H      H N N 153 
ARG H2     H N N 154 
ARG HA     H N N 155 
ARG HB2    H N N 156 
ARG HB3    H N N 157 
ARG HG2    H N N 158 
ARG HG3    H N N 159 
ARG HD2    H N N 160 
ARG HD3    H N N 161 
ARG HE     H N N 162 
ARG HH11   H N N 163 
ARG HH12   H N N 164 
ARG HH21   H N N 165 
ARG HH22   H N N 166 
ARG HXT    H N N 167 
ASN N      N N N 168 
ASN CA     C N S 169 
ASN C      C N N 170 
ASN O      O N N 171 
ASN CB     C N N 172 
ASN CG     C N N 173 
ASN OD1    O N N 174 
ASN ND2    N N N 175 
ASN OXT    O N N 176 
ASN H      H N N 177 
ASN H2     H N N 178 
ASN HA     H N N 179 
ASN HB2    H N N 180 
ASN HB3    H N N 181 
ASN HD21   H N N 182 
ASN HD22   H N N 183 
ASN HXT    H N N 184 
ASP N      N N N 185 
ASP CA     C N S 186 
ASP C      C N N 187 
ASP O      O N N 188 
ASP CB     C N N 189 
ASP CG     C N N 190 
ASP OD1    O N N 191 
ASP OD2    O N N 192 
ASP OXT    O N N 193 
ASP H      H N N 194 
ASP H2     H N N 195 
ASP HA     H N N 196 
ASP HB2    H N N 197 
ASP HB3    H N N 198 
ASP HD2    H N N 199 
ASP HXT    H N N 200 
CYS N      N N N 201 
CYS CA     C N R 202 
CYS C      C N N 203 
CYS O      O N N 204 
CYS CB     C N N 205 
CYS SG     S N N 206 
CYS OXT    O N N 207 
CYS H      H N N 208 
CYS H2     H N N 209 
CYS HA     H N N 210 
CYS HB2    H N N 211 
CYS HB3    H N N 212 
CYS HG     H N N 213 
CYS HXT    H N N 214 
GLN N      N N N 215 
GLN CA     C N S 216 
GLN C      C N N 217 
GLN O      O N N 218 
GLN CB     C N N 219 
GLN CG     C N N 220 
GLN CD     C N N 221 
GLN OE1    O N N 222 
GLN NE2    N N N 223 
GLN OXT    O N N 224 
GLN H      H N N 225 
GLN H2     H N N 226 
GLN HA     H N N 227 
GLN HB2    H N N 228 
GLN HB3    H N N 229 
GLN HG2    H N N 230 
GLN HG3    H N N 231 
GLN HE21   H N N 232 
GLN HE22   H N N 233 
GLN HXT    H N N 234 
GLU N      N N N 235 
GLU CA     C N S 236 
GLU C      C N N 237 
GLU O      O N N 238 
GLU CB     C N N 239 
GLU CG     C N N 240 
GLU CD     C N N 241 
GLU OE1    O N N 242 
GLU OE2    O N N 243 
GLU OXT    O N N 244 
GLU H      H N N 245 
GLU H2     H N N 246 
GLU HA     H N N 247 
GLU HB2    H N N 248 
GLU HB3    H N N 249 
GLU HG2    H N N 250 
GLU HG3    H N N 251 
GLU HE2    H N N 252 
GLU HXT    H N N 253 
GLY N      N N N 254 
GLY CA     C N N 255 
GLY C      C N N 256 
GLY O      O N N 257 
GLY OXT    O N N 258 
GLY H      H N N 259 
GLY H2     H N N 260 
GLY HA2    H N N 261 
GLY HA3    H N N 262 
GLY HXT    H N N 263 
GOL C1     C N N 264 
GOL O1     O N N 265 
GOL C2     C N N 266 
GOL O2     O N N 267 
GOL C3     C N N 268 
GOL O3     O N N 269 
GOL H11    H N N 270 
GOL H12    H N N 271 
GOL HO1    H N N 272 
GOL H2     H N N 273 
GOL HO2    H N N 274 
GOL H31    H N N 275 
GOL H32    H N N 276 
GOL HO3    H N N 277 
HIS N      N N N 278 
HIS CA     C N S 279 
HIS C      C N N 280 
HIS O      O N N 281 
HIS CB     C N N 282 
HIS CG     C Y N 283 
HIS ND1    N Y N 284 
HIS CD2    C Y N 285 
HIS CE1    C Y N 286 
HIS NE2    N Y N 287 
HIS OXT    O N N 288 
HIS H      H N N 289 
HIS H2     H N N 290 
HIS HA     H N N 291 
HIS HB2    H N N 292 
HIS HB3    H N N 293 
HIS HD1    H N N 294 
HIS HD2    H N N 295 
HIS HE1    H N N 296 
HIS HE2    H N N 297 
HIS HXT    H N N 298 
HOH O      O N N 299 
HOH H1     H N N 300 
HOH H2     H N N 301 
ILE N      N N N 302 
ILE CA     C N S 303 
ILE C      C N N 304 
ILE O      O N N 305 
ILE CB     C N S 306 
ILE CG1    C N N 307 
ILE CG2    C N N 308 
ILE CD1    C N N 309 
ILE OXT    O N N 310 
ILE H      H N N 311 
ILE H2     H N N 312 
ILE HA     H N N 313 
ILE HB     H N N 314 
ILE HG12   H N N 315 
ILE HG13   H N N 316 
ILE HG21   H N N 317 
ILE HG22   H N N 318 
ILE HG23   H N N 319 
ILE HD11   H N N 320 
ILE HD12   H N N 321 
ILE HD13   H N N 322 
ILE HXT    H N N 323 
LEU N      N N N 324 
LEU CA     C N S 325 
LEU C      C N N 326 
LEU O      O N N 327 
LEU CB     C N N 328 
LEU CG     C N N 329 
LEU CD1    C N N 330 
LEU CD2    C N N 331 
LEU OXT    O N N 332 
LEU H      H N N 333 
LEU H2     H N N 334 
LEU HA     H N N 335 
LEU HB2    H N N 336 
LEU HB3    H N N 337 
LEU HG     H N N 338 
LEU HD11   H N N 339 
LEU HD12   H N N 340 
LEU HD13   H N N 341 
LEU HD21   H N N 342 
LEU HD22   H N N 343 
LEU HD23   H N N 344 
LEU HXT    H N N 345 
LYS N      N N N 346 
LYS CA     C N S 347 
LYS C      C N N 348 
LYS O      O N N 349 
LYS CB     C N N 350 
LYS CG     C N N 351 
LYS CD     C N N 352 
LYS CE     C N N 353 
LYS NZ     N N N 354 
LYS OXT    O N N 355 
LYS H      H N N 356 
LYS H2     H N N 357 
LYS HA     H N N 358 
LYS HB2    H N N 359 
LYS HB3    H N N 360 
LYS HG2    H N N 361 
LYS HG3    H N N 362 
LYS HD2    H N N 363 
LYS HD3    H N N 364 
LYS HE2    H N N 365 
LYS HE3    H N N 366 
LYS HZ1    H N N 367 
LYS HZ2    H N N 368 
LYS HZ3    H N N 369 
LYS HXT    H N N 370 
MET N      N N N 371 
MET CA     C N S 372 
MET C      C N N 373 
MET O      O N N 374 
MET CB     C N N 375 
MET CG     C N N 376 
MET SD     S N N 377 
MET CE     C N N 378 
MET OXT    O N N 379 
MET H      H N N 380 
MET H2     H N N 381 
MET HA     H N N 382 
MET HB2    H N N 383 
MET HB3    H N N 384 
MET HG2    H N N 385 
MET HG3    H N N 386 
MET HE1    H N N 387 
MET HE2    H N N 388 
MET HE3    H N N 389 
MET HXT    H N N 390 
PEG C1     C N N 391 
PEG O1     O N N 392 
PEG C2     C N N 393 
PEG O2     O N N 394 
PEG C3     C N N 395 
PEG C4     C N N 396 
PEG O4     O N N 397 
PEG H11    H N N 398 
PEG H12    H N N 399 
PEG HO1    H N N 400 
PEG H21    H N N 401 
PEG H22    H N N 402 
PEG H31    H N N 403 
PEG H32    H N N 404 
PEG H41    H N N 405 
PEG H42    H N N 406 
PEG HO4    H N N 407 
PHE N      N N N 408 
PHE CA     C N S 409 
PHE C      C N N 410 
PHE O      O N N 411 
PHE CB     C N N 412 
PHE CG     C Y N 413 
PHE CD1    C Y N 414 
PHE CD2    C Y N 415 
PHE CE1    C Y N 416 
PHE CE2    C Y N 417 
PHE CZ     C Y N 418 
PHE OXT    O N N 419 
PHE H      H N N 420 
PHE H2     H N N 421 
PHE HA     H N N 422 
PHE HB2    H N N 423 
PHE HB3    H N N 424 
PHE HD1    H N N 425 
PHE HD2    H N N 426 
PHE HE1    H N N 427 
PHE HE2    H N N 428 
PHE HZ     H N N 429 
PHE HXT    H N N 430 
PRO N      N N N 431 
PRO CA     C N S 432 
PRO C      C N N 433 
PRO O      O N N 434 
PRO CB     C N N 435 
PRO CG     C N N 436 
PRO CD     C N N 437 
PRO OXT    O N N 438 
PRO H      H N N 439 
PRO HA     H N N 440 
PRO HB2    H N N 441 
PRO HB3    H N N 442 
PRO HG2    H N N 443 
PRO HG3    H N N 444 
PRO HD2    H N N 445 
PRO HD3    H N N 446 
PRO HXT    H N N 447 
SER N      N N N 448 
SER CA     C N S 449 
SER C      C N N 450 
SER O      O N N 451 
SER CB     C N N 452 
SER OG     O N N 453 
SER OXT    O N N 454 
SER H      H N N 455 
SER H2     H N N 456 
SER HA     H N N 457 
SER HB2    H N N 458 
SER HB3    H N N 459 
SER HG     H N N 460 
SER HXT    H N N 461 
THR N      N N N 462 
THR CA     C N S 463 
THR C      C N N 464 
THR O      O N N 465 
THR CB     C N R 466 
THR OG1    O N N 467 
THR CG2    C N N 468 
THR OXT    O N N 469 
THR H      H N N 470 
THR H2     H N N 471 
THR HA     H N N 472 
THR HB     H N N 473 
THR HG1    H N N 474 
THR HG21   H N N 475 
THR HG22   H N N 476 
THR HG23   H N N 477 
THR HXT    H N N 478 
TRP N      N N N 479 
TRP CA     C N S 480 
TRP C      C N N 481 
TRP O      O N N 482 
TRP CB     C N N 483 
TRP CG     C Y N 484 
TRP CD1    C Y N 485 
TRP CD2    C Y N 486 
TRP NE1    N Y N 487 
TRP CE2    C Y N 488 
TRP CE3    C Y N 489 
TRP CZ2    C Y N 490 
TRP CZ3    C Y N 491 
TRP CH2    C Y N 492 
TRP OXT    O N N 493 
TRP H      H N N 494 
TRP H2     H N N 495 
TRP HA     H N N 496 
TRP HB2    H N N 497 
TRP HB3    H N N 498 
TRP HD1    H N N 499 
TRP HE1    H N N 500 
TRP HE3    H N N 501 
TRP HZ2    H N N 502 
TRP HZ3    H N N 503 
TRP HH2    H N N 504 
TRP HXT    H N N 505 
TRS C      C N N 506 
TRS C1     C N N 507 
TRS C2     C N N 508 
TRS C3     C N N 509 
TRS N      N N N 510 
TRS O1     O N N 511 
TRS O2     O N N 512 
TRS O3     O N N 513 
TRS H11    H N N 514 
TRS H12    H N N 515 
TRS H21    H N N 516 
TRS H22    H N N 517 
TRS H31    H N N 518 
TRS H32    H N N 519 
TRS HN1    H N N 520 
TRS HN2    H N N 521 
TRS HN3    H N N 522 
TRS HO1    H N N 523 
TRS HO2    H N N 524 
TRS HO3    H N N 525 
TYR N      N N N 526 
TYR CA     C N S 527 
TYR C      C N N 528 
TYR O      O N N 529 
TYR CB     C N N 530 
TYR CG     C Y N 531 
TYR CD1    C Y N 532 
TYR CD2    C Y N 533 
TYR CE1    C Y N 534 
TYR CE2    C Y N 535 
TYR CZ     C Y N 536 
TYR OH     O N N 537 
TYR OXT    O N N 538 
TYR H      H N N 539 
TYR H2     H N N 540 
TYR HA     H N N 541 
TYR HB2    H N N 542 
TYR HB3    H N N 543 
TYR HD1    H N N 544 
TYR HD2    H N N 545 
TYR HE1    H N N 546 
TYR HE2    H N N 547 
TYR HH     H N N 548 
TYR HXT    H N N 549 
VAL N      N N N 550 
VAL CA     C N S 551 
VAL C      C N N 552 
VAL O      O N N 553 
VAL CB     C N N 554 
VAL CG1    C N N 555 
VAL CG2    C N N 556 
VAL OXT    O N N 557 
VAL H      H N N 558 
VAL H2     H N N 559 
VAL HA     H N N 560 
VAL HB     H N N 561 
VAL HG11   H N N 562 
VAL HG12   H N N 563 
VAL HG13   H N N 564 
VAL HG21   H N N 565 
VAL HG22   H N N 566 
VAL HG23   H N N 567 
VAL HXT    H N N 568 
# 
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 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
AMP P     O1P    doub N N 57  
AMP P     O2P    sing N N 58  
AMP P     O3P    sing N N 59  
AMP P     "O5'"  sing N N 60  
AMP O2P   HOP2   sing N N 61  
AMP O3P   HOP3   sing N N 62  
AMP "O5'" "C5'"  sing N N 63  
AMP "C5'" "C4'"  sing N N 64  
AMP "C5'" "H5'1" sing N N 65  
AMP "C5'" "H5'2" sing N N 66  
AMP "C4'" "O4'"  sing N N 67  
AMP "C4'" "C3'"  sing N N 68  
AMP "C4'" "H4'"  sing N N 69  
AMP "O4'" "C1'"  sing N N 70  
AMP "C3'" "O3'"  sing N N 71  
AMP "C3'" "C2'"  sing N N 72  
AMP "C3'" "H3'"  sing N N 73  
AMP "O3'" "HO3'" sing N N 74  
AMP "C2'" "O2'"  sing N N 75  
AMP "C2'" "C1'"  sing N N 76  
AMP "C2'" "H2'"  sing N N 77  
AMP "O2'" "HO2'" sing N N 78  
AMP "C1'" N9     sing N N 79  
AMP "C1'" "H1'"  sing N N 80  
AMP N9    C8     sing Y N 81  
AMP N9    C4     sing Y N 82  
AMP C8    N7     doub Y N 83  
AMP C8    H8     sing N N 84  
AMP N7    C5     sing Y N 85  
AMP C5    C6     sing Y N 86  
AMP C5    C4     doub Y N 87  
AMP C6    N6     sing N N 88  
AMP C6    N1     doub Y N 89  
AMP N6    HN61   sing N N 90  
AMP N6    HN62   sing N N 91  
AMP N1    C2     sing Y N 92  
AMP C2    N3     doub Y N 93  
AMP C2    H2     sing N N 94  
AMP N3    C4     sing Y N 95  
ANP PG    O1G    doub N N 96  
ANP PG    O2G    sing N N 97  
ANP PG    O3G    sing N N 98  
ANP PG    N3B    sing N N 99  
ANP O2G   HOG2   sing N N 100 
ANP O3G   HOG3   sing N N 101 
ANP PB    O1B    doub N N 102 
ANP PB    O2B    sing N N 103 
ANP PB    N3B    sing N N 104 
ANP PB    O3A    sing N N 105 
ANP O2B   HOB2   sing N N 106 
ANP N3B   HNB1   sing N N 107 
ANP PA    O1A    doub N N 108 
ANP PA    O2A    sing N N 109 
ANP PA    O3A    sing N N 110 
ANP PA    "O5'"  sing N N 111 
ANP O2A   HOA2   sing N N 112 
ANP "O5'" "C5'"  sing N N 113 
ANP "C5'" "C4'"  sing N N 114 
ANP "C5'" "H5'1" sing N N 115 
ANP "C5'" "H5'2" sing N N 116 
ANP "C4'" "O4'"  sing N N 117 
ANP "C4'" "C3'"  sing N N 118 
ANP "C4'" "H4'"  sing N N 119 
ANP "O4'" "C1'"  sing N N 120 
ANP "C3'" "O3'"  sing N N 121 
ANP "C3'" "C2'"  sing N N 122 
ANP "C3'" "H3'"  sing N N 123 
ANP "O3'" "HO3'" sing N N 124 
ANP "C2'" "O2'"  sing N N 125 
ANP "C2'" "C1'"  sing N N 126 
ANP "C2'" "H2'"  sing N N 127 
ANP "O2'" "HO2'" sing N N 128 
ANP "C1'" N9     sing N N 129 
ANP "C1'" "H1'"  sing N N 130 
ANP N9    C8     sing Y N 131 
ANP N9    C4     sing Y N 132 
ANP C8    N7     doub Y N 133 
ANP C8    H8     sing N N 134 
ANP N7    C5     sing Y N 135 
ANP C5    C6     sing Y N 136 
ANP C5    C4     doub Y N 137 
ANP C6    N6     sing N N 138 
ANP C6    N1     doub Y N 139 
ANP N6    HN61   sing N N 140 
ANP N6    HN62   sing N N 141 
ANP N1    C2     sing Y N 142 
ANP C2    N3     doub Y N 143 
ANP C2    H2     sing N N 144 
ANP N3    C4     sing Y N 145 
ARG N     CA     sing N N 146 
ARG N     H      sing N N 147 
ARG N     H2     sing N N 148 
ARG CA    C      sing N N 149 
ARG CA    CB     sing N N 150 
ARG CA    HA     sing N N 151 
ARG C     O      doub N N 152 
ARG C     OXT    sing N N 153 
ARG CB    CG     sing N N 154 
ARG CB    HB2    sing N N 155 
ARG CB    HB3    sing N N 156 
ARG CG    CD     sing N N 157 
ARG CG    HG2    sing N N 158 
ARG CG    HG3    sing N N 159 
ARG CD    NE     sing N N 160 
ARG CD    HD2    sing N N 161 
ARG CD    HD3    sing N N 162 
ARG NE    CZ     sing N N 163 
ARG NE    HE     sing N N 164 
ARG CZ    NH1    sing N N 165 
ARG CZ    NH2    doub N N 166 
ARG NH1   HH11   sing N N 167 
ARG NH1   HH12   sing N N 168 
ARG NH2   HH21   sing N N 169 
ARG NH2   HH22   sing N N 170 
ARG OXT   HXT    sing N N 171 
ASN N     CA     sing N N 172 
ASN N     H      sing N N 173 
ASN N     H2     sing N N 174 
ASN CA    C      sing N N 175 
ASN CA    CB     sing N N 176 
ASN CA    HA     sing N N 177 
ASN C     O      doub N N 178 
ASN C     OXT    sing N N 179 
ASN CB    CG     sing N N 180 
ASN CB    HB2    sing N N 181 
ASN CB    HB3    sing N N 182 
ASN CG    OD1    doub N N 183 
ASN CG    ND2    sing N N 184 
ASN ND2   HD21   sing N N 185 
ASN ND2   HD22   sing N N 186 
ASN OXT   HXT    sing N N 187 
ASP N     CA     sing N N 188 
ASP N     H      sing N N 189 
ASP N     H2     sing N N 190 
ASP CA    C      sing N N 191 
ASP CA    CB     sing N N 192 
ASP CA    HA     sing N N 193 
ASP C     O      doub N N 194 
ASP C     OXT    sing N N 195 
ASP CB    CG     sing N N 196 
ASP CB    HB2    sing N N 197 
ASP CB    HB3    sing N N 198 
ASP CG    OD1    doub N N 199 
ASP CG    OD2    sing N N 200 
ASP OD2   HD2    sing N N 201 
ASP OXT   HXT    sing N N 202 
CYS N     CA     sing N N 203 
CYS N     H      sing N N 204 
CYS N     H2     sing N N 205 
CYS CA    C      sing N N 206 
CYS CA    CB     sing N N 207 
CYS CA    HA     sing N N 208 
CYS C     O      doub N N 209 
CYS C     OXT    sing N N 210 
CYS CB    SG     sing N N 211 
CYS CB    HB2    sing N N 212 
CYS CB    HB3    sing N N 213 
CYS SG    HG     sing N N 214 
CYS OXT   HXT    sing N N 215 
GLN N     CA     sing N N 216 
GLN N     H      sing N N 217 
GLN N     H2     sing N N 218 
GLN CA    C      sing N N 219 
GLN CA    CB     sing N N 220 
GLN CA    HA     sing N N 221 
GLN C     O      doub N N 222 
GLN C     OXT    sing N N 223 
GLN CB    CG     sing N N 224 
GLN CB    HB2    sing N N 225 
GLN CB    HB3    sing N N 226 
GLN CG    CD     sing N N 227 
GLN CG    HG2    sing N N 228 
GLN CG    HG3    sing N N 229 
GLN CD    OE1    doub N N 230 
GLN CD    NE2    sing N N 231 
GLN NE2   HE21   sing N N 232 
GLN NE2   HE22   sing N N 233 
GLN OXT   HXT    sing N N 234 
GLU N     CA     sing N N 235 
GLU N     H      sing N N 236 
GLU N     H2     sing N N 237 
GLU CA    C      sing N N 238 
GLU CA    CB     sing N N 239 
GLU CA    HA     sing N N 240 
GLU C     O      doub N N 241 
GLU C     OXT    sing N N 242 
GLU CB    CG     sing N N 243 
GLU CB    HB2    sing N N 244 
GLU CB    HB3    sing N N 245 
GLU CG    CD     sing N N 246 
GLU CG    HG2    sing N N 247 
GLU CG    HG3    sing N N 248 
GLU CD    OE1    doub N N 249 
GLU CD    OE2    sing N N 250 
GLU OE2   HE2    sing N N 251 
GLU OXT   HXT    sing N N 252 
GLY N     CA     sing N N 253 
GLY N     H      sing N N 254 
GLY N     H2     sing N N 255 
GLY CA    C      sing N N 256 
GLY CA    HA2    sing N N 257 
GLY CA    HA3    sing N N 258 
GLY C     O      doub N N 259 
GLY C     OXT    sing N N 260 
GLY OXT   HXT    sing N N 261 
GOL C1    O1     sing N N 262 
GOL C1    C2     sing N N 263 
GOL C1    H11    sing N N 264 
GOL C1    H12    sing N N 265 
GOL O1    HO1    sing N N 266 
GOL C2    O2     sing N N 267 
GOL C2    C3     sing N N 268 
GOL C2    H2     sing N N 269 
GOL O2    HO2    sing N N 270 
GOL C3    O3     sing N N 271 
GOL C3    H31    sing N N 272 
GOL C3    H32    sing N N 273 
GOL O3    HO3    sing N N 274 
HIS N     CA     sing N N 275 
HIS N     H      sing N N 276 
HIS N     H2     sing N N 277 
HIS CA    C      sing N N 278 
HIS CA    CB     sing N N 279 
HIS CA    HA     sing N N 280 
HIS C     O      doub N N 281 
HIS C     OXT    sing N N 282 
HIS CB    CG     sing N N 283 
HIS CB    HB2    sing N N 284 
HIS CB    HB3    sing N N 285 
HIS CG    ND1    sing Y N 286 
HIS CG    CD2    doub Y N 287 
HIS ND1   CE1    doub Y N 288 
HIS ND1   HD1    sing N N 289 
HIS CD2   NE2    sing Y N 290 
HIS CD2   HD2    sing N N 291 
HIS CE1   NE2    sing Y N 292 
HIS CE1   HE1    sing N N 293 
HIS NE2   HE2    sing N N 294 
HIS OXT   HXT    sing N N 295 
HOH O     H1     sing N N 296 
HOH O     H2     sing N N 297 
ILE N     CA     sing N N 298 
ILE N     H      sing N N 299 
ILE N     H2     sing N N 300 
ILE CA    C      sing N N 301 
ILE CA    CB     sing N N 302 
ILE CA    HA     sing N N 303 
ILE C     O      doub N N 304 
ILE C     OXT    sing N N 305 
ILE CB    CG1    sing N N 306 
ILE CB    CG2    sing N N 307 
ILE CB    HB     sing N N 308 
ILE CG1   CD1    sing N N 309 
ILE CG1   HG12   sing N N 310 
ILE CG1   HG13   sing N N 311 
ILE CG2   HG21   sing N N 312 
ILE CG2   HG22   sing N N 313 
ILE CG2   HG23   sing N N 314 
ILE CD1   HD11   sing N N 315 
ILE CD1   HD12   sing N N 316 
ILE CD1   HD13   sing N N 317 
ILE OXT   HXT    sing N N 318 
LEU N     CA     sing N N 319 
LEU N     H      sing N N 320 
LEU N     H2     sing N N 321 
LEU CA    C      sing N N 322 
LEU CA    CB     sing N N 323 
LEU CA    HA     sing N N 324 
LEU C     O      doub N N 325 
LEU C     OXT    sing N N 326 
LEU CB    CG     sing N N 327 
LEU CB    HB2    sing N N 328 
LEU CB    HB3    sing N N 329 
LEU CG    CD1    sing N N 330 
LEU CG    CD2    sing N N 331 
LEU CG    HG     sing N N 332 
LEU CD1   HD11   sing N N 333 
LEU CD1   HD12   sing N N 334 
LEU CD1   HD13   sing N N 335 
LEU CD2   HD21   sing N N 336 
LEU CD2   HD22   sing N N 337 
LEU CD2   HD23   sing N N 338 
LEU OXT   HXT    sing N N 339 
LYS N     CA     sing N N 340 
LYS N     H      sing N N 341 
LYS N     H2     sing N N 342 
LYS CA    C      sing N N 343 
LYS CA    CB     sing N N 344 
LYS CA    HA     sing N N 345 
LYS C     O      doub N N 346 
LYS C     OXT    sing N N 347 
LYS CB    CG     sing N N 348 
LYS CB    HB2    sing N N 349 
LYS CB    HB3    sing N N 350 
LYS CG    CD     sing N N 351 
LYS CG    HG2    sing N N 352 
LYS CG    HG3    sing N N 353 
LYS CD    CE     sing N N 354 
LYS CD    HD2    sing N N 355 
LYS CD    HD3    sing N N 356 
LYS CE    NZ     sing N N 357 
LYS CE    HE2    sing N N 358 
LYS CE    HE3    sing N N 359 
LYS NZ    HZ1    sing N N 360 
LYS NZ    HZ2    sing N N 361 
LYS NZ    HZ3    sing N N 362 
LYS OXT   HXT    sing N N 363 
MET N     CA     sing N N 364 
MET N     H      sing N N 365 
MET N     H2     sing N N 366 
MET CA    C      sing N N 367 
MET CA    CB     sing N N 368 
MET CA    HA     sing N N 369 
MET C     O      doub N N 370 
MET C     OXT    sing N N 371 
MET CB    CG     sing N N 372 
MET CB    HB2    sing N N 373 
MET CB    HB3    sing N N 374 
MET CG    SD     sing N N 375 
MET CG    HG2    sing N N 376 
MET CG    HG3    sing N N 377 
MET SD    CE     sing N N 378 
MET CE    HE1    sing N N 379 
MET CE    HE2    sing N N 380 
MET CE    HE3    sing N N 381 
MET OXT   HXT    sing N N 382 
PEG C1    O1     sing N N 383 
PEG C1    C2     sing N N 384 
PEG C1    H11    sing N N 385 
PEG C1    H12    sing N N 386 
PEG O1    HO1    sing N N 387 
PEG C2    O2     sing N N 388 
PEG C2    H21    sing N N 389 
PEG C2    H22    sing N N 390 
PEG O2    C3     sing N N 391 
PEG C3    C4     sing N N 392 
PEG C3    H31    sing N N 393 
PEG C3    H32    sing N N 394 
PEG C4    O4     sing N N 395 
PEG C4    H41    sing N N 396 
PEG C4    H42    sing N N 397 
PEG O4    HO4    sing N N 398 
PHE N     CA     sing N N 399 
PHE N     H      sing N N 400 
PHE N     H2     sing N N 401 
PHE CA    C      sing N N 402 
PHE CA    CB     sing N N 403 
PHE CA    HA     sing N N 404 
PHE C     O      doub N N 405 
PHE C     OXT    sing N N 406 
PHE CB    CG     sing N N 407 
PHE CB    HB2    sing N N 408 
PHE CB    HB3    sing N N 409 
PHE CG    CD1    doub Y N 410 
PHE CG    CD2    sing Y N 411 
PHE CD1   CE1    sing Y N 412 
PHE CD1   HD1    sing N N 413 
PHE CD2   CE2    doub Y N 414 
PHE CD2   HD2    sing N N 415 
PHE CE1   CZ     doub Y N 416 
PHE CE1   HE1    sing N N 417 
PHE CE2   CZ     sing Y N 418 
PHE CE2   HE2    sing N N 419 
PHE CZ    HZ     sing N N 420 
PHE OXT   HXT    sing N N 421 
PRO N     CA     sing N N 422 
PRO N     CD     sing N N 423 
PRO N     H      sing N N 424 
PRO CA    C      sing N N 425 
PRO CA    CB     sing N N 426 
PRO CA    HA     sing N N 427 
PRO C     O      doub N N 428 
PRO C     OXT    sing N N 429 
PRO CB    CG     sing N N 430 
PRO CB    HB2    sing N N 431 
PRO CB    HB3    sing N N 432 
PRO CG    CD     sing N N 433 
PRO CG    HG2    sing N N 434 
PRO CG    HG3    sing N N 435 
PRO CD    HD2    sing N N 436 
PRO CD    HD3    sing N N 437 
PRO OXT   HXT    sing N N 438 
SER N     CA     sing N N 439 
SER N     H      sing N N 440 
SER N     H2     sing N N 441 
SER CA    C      sing N N 442 
SER CA    CB     sing N N 443 
SER CA    HA     sing N N 444 
SER C     O      doub N N 445 
SER C     OXT    sing N N 446 
SER CB    OG     sing N N 447 
SER CB    HB2    sing N N 448 
SER CB    HB3    sing N N 449 
SER OG    HG     sing N N 450 
SER OXT   HXT    sing N N 451 
THR N     CA     sing N N 452 
THR N     H      sing N N 453 
THR N     H2     sing N N 454 
THR CA    C      sing N N 455 
THR CA    CB     sing N N 456 
THR CA    HA     sing N N 457 
THR C     O      doub N N 458 
THR C     OXT    sing N N 459 
THR CB    OG1    sing N N 460 
THR CB    CG2    sing N N 461 
THR CB    HB     sing N N 462 
THR OG1   HG1    sing N N 463 
THR CG2   HG21   sing N N 464 
THR CG2   HG22   sing N N 465 
THR CG2   HG23   sing N N 466 
THR OXT   HXT    sing N N 467 
TRP N     CA     sing N N 468 
TRP N     H      sing N N 469 
TRP N     H2     sing N N 470 
TRP CA    C      sing N N 471 
TRP CA    CB     sing N N 472 
TRP CA    HA     sing N N 473 
TRP C     O      doub N N 474 
TRP C     OXT    sing N N 475 
TRP CB    CG     sing N N 476 
TRP CB    HB2    sing N N 477 
TRP CB    HB3    sing N N 478 
TRP CG    CD1    doub Y N 479 
TRP CG    CD2    sing Y N 480 
TRP CD1   NE1    sing Y N 481 
TRP CD1   HD1    sing N N 482 
TRP CD2   CE2    doub Y N 483 
TRP CD2   CE3    sing Y N 484 
TRP NE1   CE2    sing Y N 485 
TRP NE1   HE1    sing N N 486 
TRP CE2   CZ2    sing Y N 487 
TRP CE3   CZ3    doub Y N 488 
TRP CE3   HE3    sing N N 489 
TRP CZ2   CH2    doub Y N 490 
TRP CZ2   HZ2    sing N N 491 
TRP CZ3   CH2    sing Y N 492 
TRP CZ3   HZ3    sing N N 493 
TRP CH2   HH2    sing N N 494 
TRP OXT   HXT    sing N N 495 
TRS C     C1     sing N N 496 
TRS C     C2     sing N N 497 
TRS C     C3     sing N N 498 
TRS C     N      sing N N 499 
TRS C1    O1     sing N N 500 
TRS C1    H11    sing N N 501 
TRS C1    H12    sing N N 502 
TRS C2    O2     sing N N 503 
TRS C2    H21    sing N N 504 
TRS C2    H22    sing N N 505 
TRS C3    O3     sing N N 506 
TRS C3    H31    sing N N 507 
TRS C3    H32    sing N N 508 
TRS N     HN1    sing N N 509 
TRS N     HN2    sing N N 510 
TRS N     HN3    sing N N 511 
TRS O1    HO1    sing N N 512 
TRS O2    HO2    sing N N 513 
TRS O3    HO3    sing N N 514 
TYR N     CA     sing N N 515 
TYR N     H      sing N N 516 
TYR N     H2     sing N N 517 
TYR CA    C      sing N N 518 
TYR CA    CB     sing N N 519 
TYR CA    HA     sing N N 520 
TYR C     O      doub N N 521 
TYR C     OXT    sing N N 522 
TYR CB    CG     sing N N 523 
TYR CB    HB2    sing N N 524 
TYR CB    HB3    sing N N 525 
TYR CG    CD1    doub Y N 526 
TYR CG    CD2    sing Y N 527 
TYR CD1   CE1    sing Y N 528 
TYR CD1   HD1    sing N N 529 
TYR CD2   CE2    doub Y N 530 
TYR CD2   HD2    sing N N 531 
TYR CE1   CZ     doub Y N 532 
TYR CE1   HE1    sing N N 533 
TYR CE2   CZ     sing Y N 534 
TYR CE2   HE2    sing N N 535 
TYR CZ    OH     sing N N 536 
TYR OH    HH     sing N N 537 
TYR OXT   HXT    sing N N 538 
VAL N     CA     sing N N 539 
VAL N     H      sing N N 540 
VAL N     H2     sing N N 541 
VAL CA    C      sing N N 542 
VAL CA    CB     sing N N 543 
VAL CA    HA     sing N N 544 
VAL C     O      doub N N 545 
VAL C     OXT    sing N N 546 
VAL CB    CG1    sing N N 547 
VAL CB    CG2    sing N N 548 
VAL CB    HB     sing N N 549 
VAL CG1   HG11   sing N N 550 
VAL CG1   HG12   sing N N 551 
VAL CG1   HG13   sing N N 552 
VAL CG2   HG21   sing N N 553 
VAL CG2   HG22   sing N N 554 
VAL CG2   HG23   sing N N 555 
VAL OXT   HXT    sing N N 556 
# 
_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                    8YNQ 
_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]   0.010432 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000017 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010255 
_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]   0.009851 
_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 29  ? -3.208  3.170   20.494  1.00 60.80 ? 29  SER C N     1 
ATOM   2     C CA    . SER A  1 29  ? -1.941  3.288   21.205  1.00 56.95 ? 29  SER C CA    1 
ATOM   3     C C     . SER A  1 29  ? -0.932  4.121   20.409  1.00 64.91 ? 29  SER C C     1 
ATOM   4     O O     . SER A  1 29  ? 0.159   3.642   20.068  1.00 63.81 ? 29  SER C O     1 
ATOM   5     C CB    . SER A  1 29  ? -1.368  1.902   21.517  1.00 53.85 ? 29  SER C CB    1 
ATOM   6     O OG    . SER A  1 29  ? -1.687  1.498   22.845  1.00 71.83 ? 29  SER C OG    1 
ATOM   7     N N     . SER A  1 30  ? -1.309  5.371   20.147  1.00 55.86 ? 30  SER C N     1 
ATOM   8     C CA    . SER A  1 30  ? -0.481  6.294   19.374  1.00 54.87 ? 30  SER C CA    1 
ATOM   9     C C     . SER A  1 30  ? -1.190  7.626   19.168  1.00 56.26 ? 30  SER C C     1 
ATOM   10    O O     . SER A  1 30  ? -1.684  8.242   20.121  1.00 54.50 ? 30  SER C O     1 
ATOM   11    C CB    . SER A  1 30  ? -0.112  5.682   18.016  1.00 62.90 ? 30  SER C CB    1 
ATOM   12    O OG    . SER A  1 30  ? -1.267  5.253   17.308  1.00 70.89 ? 30  SER C OG    1 
ATOM   13    N N     . THR A  1 31  ? -1.264  8.048   17.914  1.00 50.13 ? 31  THR C N     1 
ATOM   14    C CA    . THR A  1 31  ? -1.769  9.363   17.561  1.00 49.23 ? 31  THR C CA    1 
ATOM   15    C C     . THR A  1 31  ? -3.282  9.456   17.751  1.00 46.74 ? 31  THR C C     1 
ATOM   16    O O     . THR A  1 31  ? -4.021  8.481   17.544  1.00 49.96 ? 31  THR C O     1 
ATOM   17    C CB    . THR A  1 31  ? -1.373  9.662   16.110  1.00 54.45 ? 31  THR C CB    1 
ATOM   18    O OG1   . THR A  1 31  ? -1.984  10.879  15.668  1.00 52.27 ? 31  THR C OG1   1 
ATOM   19    C CG2   . THR A  1 31  ? -1.793  8.514   15.185  1.00 52.92 ? 31  THR C CG2   1 
ATOM   20    N N     . ASP A  1 32  ? -3.745  10.645  18.167  1.00 42.76 ? 32  ASP C N     1 
ATOM   21    C CA    . ASP A  1 32  ? -5.169  10.987  18.153  1.00 39.54 ? 32  ASP C CA    1 
ATOM   22    C C     . ASP A  1 32  ? -5.413  12.183  17.243  1.00 34.66 ? 32  ASP C C     1 
ATOM   23    O O     . ASP A  1 32  ? -6.184  13.094  17.554  1.00 40.41 ? 32  ASP C O     1 
ATOM   24    C CB    . ASP A  1 32  ? -5.722  11.262  19.558  1.00 30.64 ? 32  ASP C CB    1 
ATOM   25    C CG    . ASP A  1 32  ? -5.153  12.513  20.205  1.00 31.97 ? 32  ASP C CG    1 
ATOM   26    O OD1   . ASP A  1 32  ? -4.108  13.007  19.742  1.00 27.23 ? 32  ASP C OD1   1 
ATOM   27    O OD2   . ASP A  1 32  ? -5.763  12.995  21.198  1.00 36.78 ? 32  ASP C OD2   1 
ATOM   28    N N     . THR A  1 33  ? -4.732  12.204  16.101  1.00 36.63 ? 33  THR C N     1 
ATOM   29    C CA    . THR A  1 33  ? -4.875  13.351  15.213  1.00 35.65 ? 33  THR C CA    1 
ATOM   30    C C     . THR A  1 33  ? -6.269  13.387  14.603  1.00 33.49 ? 33  THR C C     1 
ATOM   31    O O     . THR A  1 33  ? -6.810  14.464  14.342  1.00 38.40 ? 33  THR C O     1 
ATOM   32    C CB    . THR A  1 33  ? -3.776  13.315  14.144  1.00 38.73 ? 33  THR C CB    1 
ATOM   33    O OG1   . THR A  1 33  ? -4.019  14.302  13.130  1.00 39.39 ? 33  THR C OG1   1 
ATOM   34    C CG2   . THR A  1 33  ? -3.721  11.954  13.509  1.00 38.37 ? 33  THR C CG2   1 
ATOM   35    N N     . THR A  1 34  ? -6.893  12.229  14.440  1.00 30.13 ? 34  THR C N     1 
ATOM   36    C CA    . THR A  1 34  ? -8.250  12.204  13.916  1.00 40.72 ? 34  THR C CA    1 
ATOM   37    C C     . THR A  1 34  ? -9.264  12.753  14.916  1.00 40.17 ? 34  THR C C     1 
ATOM   38    O O     . THR A  1 34  ? -10.309 13.276  14.507  1.00 40.64 ? 34  THR C O     1 
ATOM   39    C CB    . THR A  1 34  ? -8.627  10.777  13.522  1.00 45.96 ? 34  THR C CB    1 
ATOM   40    O OG1   . THR A  1 34  ? -7.506  10.158  12.886  1.00 42.85 ? 34  THR C OG1   1 
ATOM   41    C CG2   . THR A  1 34  ? -9.792  10.781  12.552  1.00 44.80 ? 34  THR C CG2   1 
ATOM   42    N N     . ALA A  1 35  ? -8.975  12.658  16.221  1.00 41.03 ? 35  ALA C N     1 
ATOM   43    C CA    . ALA A  1 35  ? -9.957  12.982  17.255  1.00 33.92 ? 35  ALA C CA    1 
ATOM   44    C C     . ALA A  1 35  ? -10.388 14.442  17.237  1.00 32.64 ? 35  ALA C C     1 
ATOM   45    O O     . ALA A  1 35  ? -11.410 14.779  17.847  1.00 26.16 ? 35  ALA C O     1 
ATOM   46    C CB    . ALA A  1 35  ? -9.402  12.630  18.632  1.00 31.49 ? 35  ALA C CB    1 
ATOM   47    N N     . ARG A  1 36  ? -9.647  15.312  16.554  1.00 29.57 ? 36  ARG C N     1 
ATOM   48    C CA    . ARG A  1 36  ? -10.036 16.715  16.520  1.00 35.64 ? 36  ARG C CA    1 
ATOM   49    C C     . ARG A  1 36  ? -11.431 16.892  15.934  1.00 37.13 ? 36  ARG C C     1 
ATOM   50    O O     . ARG A  1 36  ? -12.149 17.834  16.291  1.00 36.32 ? 36  ARG C O     1 
ATOM   51    C CB    . ARG A  1 36  ? -9.025  17.512  15.699  1.00 34.21 ? 36  ARG C CB    1 
ATOM   52    C CG    . ARG A  1 36  ? -8.901  17.012  14.278  1.00 32.08 ? 36  ARG C CG    1 
ATOM   53    C CD    . ARG A  1 36  ? -7.539  17.291  13.730  1.00 32.97 ? 36  ARG C CD    1 
ATOM   54    N NE    . ARG A  1 36  ? -7.090  18.636  14.055  1.00 33.41 ? 36  ARG C NE    1 
ATOM   55    C CZ    . ARG A  1 36  ? -7.154  19.645  13.204  1.00 32.02 ? 36  ARG C CZ    1 
ATOM   56    N NH1   . ARG A  1 36  ? -7.680  19.496  11.999  1.00 31.45 ? 36  ARG C NH1   1 
ATOM   57    N NH2   . ARG A  1 36  ? -6.696  20.838  13.575  1.00 32.09 ? 36  ARG C NH2   1 
ATOM   58    N N     . PHE A  1 37  ? -11.840 15.985  15.057  1.00 34.40 ? 37  PHE C N     1 
ATOM   59    C CA    . PHE A  1 37  ? -13.063 16.202  14.308  1.00 38.17 ? 37  PHE C CA    1 
ATOM   60    C C     . PHE A  1 37  ? -14.292 15.771  15.077  1.00 38.92 ? 37  PHE C C     1 
ATOM   61    O O     . PHE A  1 37  ? -15.413 15.877  14.552  1.00 38.56 ? 37  PHE C O     1 
ATOM   62    C CB    . PHE A  1 37  ? -12.948 15.500  12.960  1.00 39.76 ? 37  PHE C CB    1 
ATOM   63    C CG    . PHE A  1 37  ? -11.793 15.994  12.160  1.00 30.87 ? 37  PHE C CG    1 
ATOM   64    C CD1   . PHE A  1 37  ? -11.766 17.311  11.722  1.00 32.06 ? 37  PHE C CD1   1 
ATOM   65    C CD2   . PHE A  1 37  ? -10.711 15.168  11.890  1.00 37.10 ? 37  PHE C CD2   1 
ATOM   66    C CE1   . PHE A  1 37  ? -10.688 17.796  10.986  1.00 36.63 ? 37  PHE C CE1   1 
ATOM   67    C CE2   . PHE A  1 37  ? -9.621  15.635  11.159  1.00 31.73 ? 37  PHE C CE2   1 
ATOM   68    C CZ    . PHE A  1 37  ? -9.611  16.954  10.709  1.00 34.45 ? 37  PHE C CZ    1 
ATOM   69    N N     . LEU A  1 38  ? -14.106 15.311  16.312  1.00 32.76 ? 38  LEU C N     1 
ATOM   70    C CA    . LEU A  1 38  ? -15.242 15.154  17.192  1.00 30.43 ? 38  LEU C CA    1 
ATOM   71    C C     . LEU A  1 38  ? -15.962 16.482  17.389  1.00 35.85 ? 38  LEU C C     1 
ATOM   72    O O     . LEU A  1 38  ? -17.155 16.490  17.712  1.00 38.30 ? 38  LEU C O     1 
ATOM   73    C CB    . LEU A  1 38  ? -14.773 14.550  18.518  1.00 30.77 ? 38  LEU C CB    1 
ATOM   74    C CG    . LEU A  1 38  ? -15.762 13.661  19.272  1.00 32.05 ? 38  LEU C CG    1 
ATOM   75    C CD1   . LEU A  1 38  ? -16.431 12.685  18.349  1.00 35.64 ? 38  LEU C CD1   1 
ATOM   76    C CD2   . LEU A  1 38  ? -15.032 12.908  20.333  1.00 32.96 ? 38  LEU C CD2   1 
ATOM   77    N N     . TRP A  1 39  ? -15.292 17.610  17.149  1.00 28.79 ? 39  TRP C N     1 
ATOM   78    C CA    . TRP A  1 39  ? -15.980 18.871  17.393  1.00 29.66 ? 39  TRP C CA    1 
ATOM   79    C C     . TRP A  1 39  ? -16.979 19.241  16.296  1.00 38.68 ? 39  TRP C C     1 
ATOM   80    O O     . TRP A  1 39  ? -17.663 20.265  16.426  1.00 40.69 ? 39  TRP C O     1 
ATOM   81    C CB    . TRP A  1 39  ? -14.982 20.004  17.547  1.00 25.09 ? 39  TRP C CB    1 
ATOM   82    C CG    . TRP A  1 39  ? -14.075 19.899  18.705  1.00 34.21 ? 39  TRP C CG    1 
ATOM   83    C CD1   . TRP A  1 39  ? -12.856 19.284  18.736  1.00 30.72 ? 39  TRP C CD1   1 
ATOM   84    C CD2   . TRP A  1 39  ? -14.272 20.470  20.005  1.00 30.72 ? 39  TRP C CD2   1 
ATOM   85    N NE1   . TRP A  1 39  ? -12.283 19.434  19.972  1.00 29.26 ? 39  TRP C NE1   1 
ATOM   86    C CE2   . TRP A  1 39  ? -13.124 20.165  20.771  1.00 30.78 ? 39  TRP C CE2   1 
ATOM   87    C CE3   . TRP A  1 39  ? -15.299 21.218  20.593  1.00 31.08 ? 39  TRP C CE3   1 
ATOM   88    C CZ2   . TRP A  1 39  ? -12.982 20.561  22.114  1.00 31.32 ? 39  TRP C CZ2   1 
ATOM   89    C CZ3   . TRP A  1 39  ? -15.160 21.615  21.930  1.00 36.01 ? 39  TRP C CZ3   1 
ATOM   90    C CH2   . TRP A  1 39  ? -14.008 21.281  22.674  1.00 29.31 ? 39  TRP C CH2   1 
ATOM   91    N N     . HIS A  1 40  ? -17.048 18.484  15.195  1.00 33.62 ? 40  HIS C N     1 
ATOM   92    C CA    . HIS A  1 40  ? -18.154 18.665  14.266  1.00 32.90 ? 40  HIS C CA    1 
ATOM   93    C C     . HIS A  1 40  ? -19.413 18.055  14.812  1.00 33.00 ? 40  HIS C C     1 
ATOM   94    O O     . HIS A  1 40  ? -20.498 18.392  14.340  1.00 37.77 ? 40  HIS C O     1 
ATOM   95    C CB    . HIS A  1 40  ? -17.872 18.025  12.901  1.00 30.34 ? 40  HIS C CB    1 
ATOM   96    C CG    . HIS A  1 40  ? -16.939 18.819  12.057  1.00 30.64 ? 40  HIS C CG    1 
ATOM   97    N ND1   . HIS A  1 40  ? -17.235 20.091  11.619  1.00 35.65 ? 40  HIS C ND1   1 
ATOM   98    C CD2   . HIS A  1 40  ? -15.700 18.537  11.593  1.00 33.83 ? 40  HIS C CD2   1 
ATOM   99    C CE1   . HIS A  1 40  ? -16.220 20.556  10.914  1.00 34.14 ? 40  HIS C CE1   1 
ATOM   100   N NE2   . HIS A  1 40  ? -15.275 19.633  10.885  1.00 32.34 ? 40  HIS C NE2   1 
ATOM   101   N N     . ALA A  1 41  ? -19.276 17.167  15.790  1.00 33.58 ? 41  ALA C N     1 
ATOM   102   C CA    . ALA A  1 41  ? -20.376 16.312  16.199  1.00 38.10 ? 41  ALA C CA    1 
ATOM   103   C C     . ALA A  1 41  ? -21.528 17.125  16.771  1.00 36.23 ? 41  ALA C C     1 
ATOM   104   O O     . ALA A  1 41  ? -21.336 18.072  17.536  1.00 32.74 ? 41  ALA C O     1 
ATOM   105   C CB    . ALA A  1 41  ? -19.899 15.292  17.239  1.00 34.34 ? 41  ALA C CB    1 
ATOM   106   N N     . GLU A  1 42  ? -22.725 16.754  16.380  1.00 37.69 ? 42  GLU C N     1 
ATOM   107   C CA    . GLU A  1 42  ? -23.918 17.156  17.077  1.00 36.06 ? 42  GLU C CA    1 
ATOM   108   C C     . GLU A  1 42  ? -24.590 15.900  17.586  1.00 40.63 ? 42  GLU C C     1 
ATOM   109   O O     . GLU A  1 42  ? -24.145 14.777  17.322  1.00 37.31 ? 42  GLU C O     1 
ATOM   110   C CB    . GLU A  1 42  ? -24.863 17.930  16.166  1.00 39.76 ? 42  GLU C CB    1 
ATOM   111   C CG    . GLU A  1 42  ? -24.172 18.714  15.095  1.00 41.45 ? 42  GLU C CG    1 
ATOM   112   C CD    . GLU A  1 42  ? -25.070 18.948  13.897  1.00 53.71 ? 42  GLU C CD    1 
ATOM   113   O OE1   . GLU A  1 42  ? -26.311 18.909  14.084  1.00 56.01 ? 42  GLU C OE1   1 
ATOM   114   O OE2   . GLU A  1 42  ? -24.542 19.183  12.782  1.00 53.11 ? 42  GLU C OE2   1 
ATOM   115   N N     . ASP A  1 43  ? -25.683 16.117  18.301  1.00 37.65 ? 43  ASP C N     1 
ATOM   116   C CA    . ASP A  1 43  ? -26.509 15.043  18.815  1.00 37.22 ? 43  ASP C CA    1 
ATOM   117   C C     . ASP A  1 43  ? -26.606 13.866  17.869  1.00 36.54 ? 43  ASP C C     1 
ATOM   118   O O     . ASP A  1 43  ? -26.958 14.015  16.694  1.00 35.72 ? 43  ASP C O     1 
ATOM   119   C CB    . ASP A  1 43  ? -27.896 15.582  19.089  1.00 45.60 ? 43  ASP C CB    1 
ATOM   120   C CG    . ASP A  1 43  ? -28.058 15.953  20.506  1.00 47.74 ? 43  ASP C CG    1 
ATOM   121   O OD1   . ASP A  1 43  ? -27.050 15.788  21.234  1.00 49.86 ? 43  ASP C OD1   1 
ATOM   122   O OD2   . ASP A  1 43  ? -29.158 16.406  20.886  1.00 50.40 ? 43  ASP C OD2   1 
ATOM   123   N N     . GLY A  1 44  ? -26.289 12.695  18.398  1.00 37.73 ? 44  GLY C N     1 
ATOM   124   C CA    . GLY A  1 44  ? -26.446 11.460  17.667  1.00 39.77 ? 44  GLY C CA    1 
ATOM   125   C C     . GLY A  1 44  ? -25.459 11.217  16.552  1.00 38.83 ? 44  GLY C C     1 
ATOM   126   O O     . GLY A  1 44  ? -25.541 10.160  15.922  1.00 38.54 ? 44  GLY C O     1 
ATOM   127   N N     . ASP A  1 45  ? -24.534 12.145  16.286  1.00 40.23 ? 45  ASP C N     1 
ATOM   128   C CA    . ASP A  1 45  ? -23.561 11.964  15.214  1.00 39.20 ? 45  ASP C CA    1 
ATOM   129   C C     . ASP A  1 45  ? -22.664 10.768  15.473  1.00 36.67 ? 45  ASP C C     1 
ATOM   130   O O     . ASP A  1 45  ? -22.594 10.226  16.580  1.00 33.73 ? 45  ASP C O     1 
ATOM   131   C CB    . ASP A  1 45  ? -22.667 13.184  15.062  1.00 36.10 ? 45  ASP C CB    1 
ATOM   132   C CG    . ASP A  1 45  ? -23.391 14.331  14.469  1.00 36.29 ? 45  ASP C CG    1 
ATOM   133   O OD1   . ASP A  1 45  ? -24.474 14.086  13.917  1.00 38.92 ? 45  ASP C OD1   1 
ATOM   134   O OD2   . ASP A  1 45  ? -22.891 15.461  14.556  1.00 34.38 ? 45  ASP C OD2   1 
ATOM   135   N N     . VAL A  1 46  ? -21.979 10.352  14.414  1.00 40.03 ? 46  VAL C N     1 
ATOM   136   C CA    . VAL A  1 46  ? -20.925 9.351   14.494  1.00 40.20 ? 46  VAL C CA    1 
ATOM   137   C C     . VAL A  1 46  ? -19.712 9.861   13.747  1.00 40.67 ? 46  VAL C C     1 
ATOM   138   O O     . VAL A  1 46  ? -19.818 10.300  12.595  1.00 37.23 ? 46  VAL C O     1 
ATOM   139   C CB    . VAL A  1 46  ? -21.339 7.980   13.935  1.00 39.50 ? 46  VAL C CB    1 
ATOM   140   C CG1   . VAL A  1 46  ? -20.371 6.906   14.439  1.00 38.61 ? 46  VAL C CG1   1 
ATOM   141   C CG2   . VAL A  1 46  ? -22.757 7.649   14.359  1.00 40.02 ? 46  VAL C CG2   1 
ATOM   142   N N     . LEU A  1 47  ? -18.568 9.800   14.415  1.00 46.38 ? 47  LEU C N     1 
ATOM   143   C CA    . LEU A  1 47  ? -17.263 10.080  13.848  1.00 45.55 ? 47  LEU C CA    1 
ATOM   144   C C     . LEU A  1 47  ? -16.549 8.763   13.586  1.00 42.33 ? 47  LEU C C     1 
ATOM   145   O O     . LEU A  1 47  ? -16.577 7.850   14.421  1.00 40.99 ? 47  LEU C O     1 
ATOM   146   C CB    . LEU A  1 47  ? -16.444 10.946  14.808  1.00 42.80 ? 47  LEU C CB    1 
ATOM   147   C CG    . LEU A  1 47  ? -15.081 11.438  14.324  1.00 43.17 ? 47  LEU C CG    1 
ATOM   148   C CD1   . LEU A  1 47  ? -15.262 12.571  13.351  1.00 43.85 ? 47  LEU C CD1   1 
ATOM   149   C CD2   . LEU A  1 47  ? -14.260 11.890  15.510  1.00 37.20 ? 47  LEU C CD2   1 
ATOM   150   N N     . VAL A  1 48  ? -15.919 8.657   12.424  1.00 38.71 ? 48  VAL C N     1 
ATOM   151   C CA    . VAL A  1 48  ? -15.156 7.468   12.075  1.00 42.50 ? 48  VAL C CA    1 
ATOM   152   C C     . VAL A  1 48  ? -13.680 7.822   12.182  1.00 43.17 ? 48  VAL C C     1 
ATOM   153   O O     . VAL A  1 48  ? -13.215 8.768   11.530  1.00 44.74 ? 48  VAL C O     1 
ATOM   154   C CB    . VAL A  1 48  ? -15.523 6.957   10.676  1.00 46.87 ? 48  VAL C CB    1 
ATOM   155   C CG1   . VAL A  1 48  ? -14.657 5.753   10.290  1.00 42.91 ? 48  VAL C CG1   1 
ATOM   156   C CG2   . VAL A  1 48  ? -16.997 6.595   10.635  1.00 41.55 ? 48  VAL C CG2   1 
ATOM   157   N N     . ILE A  1 49  ? -12.951 7.091   13.028  1.00 38.01 ? 49  ILE C N     1 
ATOM   158   C CA    . ILE A  1 49  ? -11.510 7.319   13.166  1.00 41.33 ? 49  ILE C CA    1 
ATOM   159   C C     . ILE A  1 49  ? -10.722 6.020   13.038  1.00 41.81 ? 49  ILE C C     1 
ATOM   160   O O     . ILE A  1 49  ? -11.184 4.947   13.449  1.00 42.80 ? 49  ILE C O     1 
ATOM   161   C CB    . ILE A  1 49  ? -11.153 8.019   14.492  1.00 45.44 ? 49  ILE C CB    1 
ATOM   162   C CG1   . ILE A  1 49  ? -10.908 7.009   15.621  1.00 40.51 ? 49  ILE C CG1   1 
ATOM   163   C CG2   . ILE A  1 49  ? -12.201 9.055   14.877  1.00 44.86 ? 49  ILE C CG2   1 
ATOM   164   C CD1   . ILE A  1 49  ? -10.240 7.614   16.844  1.00 40.76 ? 49  ILE C CD1   1 
ATOM   165   N N     . PRO A  1 50  ? -9.540  6.074   12.432  1.00 37.69 ? 50  PRO C N     1 
ATOM   166   C CA    . PRO A  1 50  ? -8.600  4.948   12.481  1.00 44.94 ? 50  PRO C CA    1 
ATOM   167   C C     . PRO A  1 50  ? -7.675  4.996   13.680  1.00 37.23 ? 50  PRO C C     1 
ATOM   168   O O     . PRO A  1 50  ? -6.743  4.197   13.762  1.00 35.06 ? 50  PRO C O     1 
ATOM   169   C CB    . PRO A  1 50  ? -7.796  5.149   11.194  1.00 44.21 ? 50  PRO C CB    1 
ATOM   170   C CG    . PRO A  1 50  ? -7.738  6.653   11.063  1.00 40.04 ? 50  PRO C CG    1 
ATOM   171   C CD    . PRO A  1 50  ? -9.021  7.198   11.634  1.00 36.33 ? 50  PRO C CD    1 
ATOM   172   N N     . ASP A  1 51  ? -7.940  5.916   14.565  1.00 43.12 ? 51  ASP C N     1 
ATOM   173   C CA    . ASP A  1 51  ? -7.017  6.443   15.530  1.00 44.37 ? 51  ASP C CA    1 
ATOM   174   C C     . ASP A  1 51  ? -7.365  5.916   16.904  1.00 47.48 ? 51  ASP C C     1 
ATOM   175   O O     . ASP A  1 51  ? -8.250  5.068   17.069  1.00 46.64 ? 51  ASP C O     1 
ATOM   176   C CB    . ASP A  1 51  ? -7.058  7.972   15.510  1.00 42.37 ? 51  ASP C CB    1 
ATOM   177   C CG    . ASP A  1 51  ? -5.876  8.552   14.848  1.00 42.93 ? 51  ASP C CG    1 
ATOM   178   O OD1   . ASP A  1 51  ? -4.854  7.836   14.806  1.00 49.57 ? 51  ASP C OD1   1 
ATOM   179   O OD2   . ASP A  1 51  ? -5.943  9.718   14.411  1.00 41.85 ? 51  ASP C OD2   1 
ATOM   180   N N     . THR A  1 52  ? -6.676  6.457   17.899  1.00 49.46 ? 52  THR C N     1 
ATOM   181   C CA    . THR A  1 52  ? -6.963  6.200   19.296  1.00 46.91 ? 52  THR C CA    1 
ATOM   182   C C     . THR A  1 52  ? -7.370  7.517   19.916  1.00 42.97 ? 52  THR C C     1 
ATOM   183   O O     . THR A  1 52  ? -6.648  8.505   19.792  1.00 47.88 ? 52  THR C O     1 
ATOM   184   C CB    . THR A  1 52  ? -5.744  5.649   20.016  1.00 50.83 ? 52  THR C CB    1 
ATOM   185   O OG1   . THR A  1 52  ? -5.002  4.819   19.117  1.00 55.77 ? 52  THR C OG1   1 
ATOM   186   C CG2   . THR A  1 52  ? -6.184  4.824   21.206  1.00 55.62 ? 52  THR C CG2   1 
ATOM   187   N N     . VAL A  1 53  ? -8.509  7.542   20.545  1.00 46.01 ? 53  VAL C N     1 
ATOM   188   C CA    . VAL A  1 53  ? -8.961  8.723   21.263  1.00 40.02 ? 53  VAL C CA    1 
ATOM   189   C C     . VAL A  1 53  ? -8.685  8.502   22.742  1.00 32.78 ? 53  VAL C C     1 
ATOM   190   O O     . VAL A  1 53  ? -8.853  7.387   23.252  1.00 33.86 ? 53  VAL C O     1 
ATOM   191   C CB    . VAL A  1 53  ? -10.450 8.971   20.981  1.00 33.61 ? 53  VAL C CB    1 
ATOM   192   C CG1   . VAL A  1 53  ? -11.227 7.735   21.303  1.00 35.30 ? 53  VAL C CG1   1 
ATOM   193   C CG2   . VAL A  1 53  ? -10.966 10.148  21.767  1.00 38.44 ? 53  VAL C CG2   1 
ATOM   194   N N     . ASP A  1 54  ? -8.213  9.535   23.428  1.00 33.38 ? 54  ASP C N     1 
ATOM   195   C CA    . ASP A  1 54  ? -8.214  9.469   24.879  1.00 35.87 ? 54  ASP C CA    1 
ATOM   196   C C     . ASP A  1 54  ? -9.617  9.067   25.309  1.00 35.12 ? 54  ASP C C     1 
ATOM   197   O O     . ASP A  1 54  ? -10.594 9.648   24.819  1.00 32.43 ? 54  ASP C O     1 
ATOM   198   C CB    . ASP A  1 54  ? -7.825  10.811  25.516  1.00 41.75 ? 54  ASP C CB    1 
ATOM   199   C CG    . ASP A  1 54  ? -7.590  10.719  27.049  1.00 40.91 ? 54  ASP C CG    1 
ATOM   200   O OD1   . ASP A  1 54  ? -8.526  10.371  27.804  1.00 36.93 ? 54  ASP C OD1   1 
ATOM   201   O OD2   . ASP A  1 54  ? -6.459  11.029  27.505  1.00 38.10 ? 54  ASP C OD2   1 
ATOM   202   N N     . PRO A  1 55  ? -9.766  8.046   26.150  1.00 38.79 ? 55  PRO C N     1 
ATOM   203   C CA    . PRO A  1 55  ? -11.114 7.569   26.486  1.00 42.79 ? 55  PRO C CA    1 
ATOM   204   C C     . PRO A  1 55  ? -11.951 8.609   27.210  1.00 38.16 ? 55  PRO C C     1 
ATOM   205   O O     . PRO A  1 55  ? -13.163 8.421   27.319  1.00 36.14 ? 55  PRO C O     1 
ATOM   206   C CB    . PRO A  1 55  ? -10.853 6.339   27.369  1.00 38.47 ? 55  PRO C CB    1 
ATOM   207   C CG    . PRO A  1 55  ? -9.405  6.038   27.228  1.00 40.17 ? 55  PRO C CG    1 
ATOM   208   C CD    . PRO A  1 55  ? -8.728  7.326   26.897  1.00 40.24 ? 55  PRO C CD    1 
ATOM   209   N N     . ASP A  1 56  ? -11.353 9.709   27.663  1.00 35.66 ? 56  ASP C N     1 
ATOM   210   C CA    . ASP A  1 56  ? -12.096 10.805  28.268  1.00 35.30 ? 56  ASP C CA    1 
ATOM   211   C C     . ASP A  1 56  ? -12.420 11.911  27.281  1.00 33.81 ? 56  ASP C C     1 
ATOM   212   O O     . ASP A  1 56  ? -13.331 12.706  27.540  1.00 37.62 ? 56  ASP C O     1 
ATOM   213   C CB    . ASP A  1 56  ? -11.297 11.393  29.439  1.00 36.17 ? 56  ASP C CB    1 
ATOM   214   C CG    . ASP A  1 56  ? -10.762 10.326  30.375  1.00 40.66 ? 56  ASP C CG    1 
ATOM   215   O OD1   . ASP A  1 56  ? -9.777  9.630   30.013  1.00 45.16 ? 56  ASP C OD1   1 
ATOM   216   O OD2   . ASP A  1 56  ? -11.337 10.174  31.474  1.00 46.92 ? 56  ASP C OD2   1 
ATOM   217   N N     . PHE A  1 57  ? -11.704 11.956  26.159  1.00 37.03 ? 57  PHE C N     1 
ATOM   218   C CA    . PHE A  1 57  ? -11.798 13.069  25.218  1.00 35.40 ? 57  PHE C CA    1 
ATOM   219   C C     . PHE A  1 57  ? -13.194 13.305  24.643  1.00 36.28 ? 57  PHE C C     1 
ATOM   220   O O     . PHE A  1 57  ? -13.570 14.483  24.504  1.00 34.95 ? 57  PHE C O     1 
ATOM   221   C CB    . PHE A  1 57  ? -10.798 12.840  24.079  1.00 33.99 ? 57  PHE C CB    1 
ATOM   222   C CG    . PHE A  1 57  ? -10.772 13.934  23.093  1.00 31.39 ? 57  PHE C CG    1 
ATOM   223   C CD1   . PHE A  1 57  ? -10.183 15.146  23.414  1.00 27.75 ? 57  PHE C CD1   1 
ATOM   224   C CD2   . PHE A  1 57  ? -11.346 13.767  21.845  1.00 35.27 ? 57  PHE C CD2   1 
ATOM   225   C CE1   . PHE A  1 57  ? -10.145 16.179  22.513  1.00 28.80 ? 57  PHE C CE1   1 
ATOM   226   C CE2   . PHE A  1 57  ? -11.313 14.795  20.921  1.00 33.67 ? 57  PHE C CE2   1 
ATOM   227   C CZ    . PHE A  1 57  ? -10.709 16.012  21.260  1.00 32.09 ? 57  PHE C CZ    1 
ATOM   228   N N     . PRO A  1 58  ? -13.976 12.288  24.245  1.00 38.01 ? 58  PRO C N     1 
ATOM   229   C CA    . PRO A  1 58  ? -15.341 12.581  23.766  1.00 31.41 ? 58  PRO C CA    1 
ATOM   230   C C     . PRO A  1 58  ? -16.155 13.408  24.747  1.00 35.53 ? 58  PRO C C     1 
ATOM   231   O O     . PRO A  1 58  ? -16.608 14.517  24.416  1.00 34.97 ? 58  PRO C O     1 
ATOM   232   C CB    . PRO A  1 58  ? -15.952 11.184  23.566  1.00 23.47 ? 58  PRO C CB    1 
ATOM   233   C CG    . PRO A  1 58  ? -14.843 10.240  23.523  1.00 28.16 ? 58  PRO C CG    1 
ATOM   234   C CD    . PRO A  1 58  ? -13.626 10.859  24.127  1.00 33.32 ? 58  PRO C CD    1 
ATOM   235   N N     . GLY A  1 59  ? -16.310 12.898  25.979  1.00 40.56 ? 59  GLY C N     1 
ATOM   236   C CA    . GLY A  1 59  ? -17.101 13.574  26.991  1.00 30.46 ? 59  GLY C CA    1 
ATOM   237   C C     . GLY A  1 59  ? -16.655 14.988  27.265  1.00 33.51 ? 59  GLY C C     1 
ATOM   238   O O     . GLY A  1 59  ? -17.480 15.844  27.570  1.00 33.57 ? 59  GLY C O     1 
ATOM   239   N N     . TYR A  1 60  ? -15.349 15.255  27.172  1.00 32.89 ? 60  TYR C N     1 
ATOM   240   C CA    . TYR A  1 60  ? -14.870 16.622  27.313  1.00 29.58 ? 60  TYR C CA    1 
ATOM   241   C C     . TYR A  1 60  ? -15.449 17.517  26.230  1.00 40.16 ? 60  TYR C C     1 
ATOM   242   O O     . TYR A  1 60  ? -15.867 18.648  26.515  1.00 41.41 ? 60  TYR C O     1 
ATOM   243   C CB    . TYR A  1 60  ? -13.351 16.643  27.259  1.00 29.12 ? 60  TYR C CB    1 
ATOM   244   C CG    . TYR A  1 60  ? -12.724 17.995  26.980  1.00 36.82 ? 60  TYR C CG    1 
ATOM   245   C CD1   . TYR A  1 60  ? -13.049 19.124  27.737  1.00 32.98 ? 60  TYR C CD1   1 
ATOM   246   C CD2   . TYR A  1 60  ? -11.789 18.142  25.960  1.00 33.73 ? 60  TYR C CD2   1 
ATOM   247   C CE1   . TYR A  1 60  ? -12.454 20.350  27.465  1.00 28.29 ? 60  TYR C CE1   1 
ATOM   248   C CE2   . TYR A  1 60  ? -11.187 19.359  25.698  1.00 26.66 ? 60  TYR C CE2   1 
ATOM   249   C CZ    . TYR A  1 60  ? -11.519 20.447  26.445  1.00 25.78 ? 60  TYR C CZ    1 
ATOM   250   O OH    . TYR A  1 60  ? -10.911 21.640  26.162  1.00 23.12 ? 60  TYR C OH    1 
ATOM   251   N N     . VAL A  1 61  ? -15.485 17.027  24.983  1.00 32.35 ? 61  VAL C N     1 
ATOM   252   C CA    . VAL A  1 61  ? -15.911 17.860  23.864  1.00 36.56 ? 61  VAL C CA    1 
ATOM   253   C C     . VAL A  1 61  ? -17.399 18.146  23.964  1.00 39.04 ? 61  VAL C C     1 
ATOM   254   O O     . VAL A  1 61  ? -17.823 19.306  24.038  1.00 34.87 ? 61  VAL C O     1 
ATOM   255   C CB    . VAL A  1 61  ? -15.567 17.190  22.524  1.00 35.11 ? 61  VAL C CB    1 
ATOM   256   C CG1   . VAL A  1 61  ? -16.309 17.884  21.393  1.00 36.57 ? 61  VAL C CG1   1 
ATOM   257   C CG2   . VAL A  1 61  ? -14.070 17.228  22.286  1.00 31.79 ? 61  VAL C CG2   1 
ATOM   258   N N     . ALA A  1 62  ? -18.208 17.079  23.969  1.00 40.76 ? 62  ALA C N     1 
ATOM   259   C CA    . ALA A  1 62  ? -19.655 17.215  24.129  1.00 41.38 ? 62  ALA C CA    1 
ATOM   260   C C     . ALA A  1 62  ? -19.996 18.104  25.312  1.00 41.44 ? 62  ALA C C     1 
ATOM   261   O O     . ALA A  1 62  ? -20.916 18.928  25.240  1.00 40.94 ? 62  ALA C O     1 
ATOM   262   C CB    . ALA A  1 62  ? -20.293 15.838  24.310  1.00 41.78 ? 62  ALA C CB    1 
ATOM   263   N N     . ASP A  1 63  ? -19.252 17.953  26.406  1.00 41.20 ? 63  ASP C N     1 
ATOM   264   C CA    . ASP A  1 63  ? -19.398 18.780  27.591  1.00 35.49 ? 63  ASP C CA    1 
ATOM   265   C C     . ASP A  1 63  ? -19.227 20.234  27.203  1.00 39.80 ? 63  ASP C C     1 
ATOM   266   O O     . ASP A  1 63  ? -20.182 21.011  27.239  1.00 47.39 ? 63  ASP C O     1 
ATOM   267   C CB    . ASP A  1 63  ? -18.368 18.374  28.636  1.00 34.74 ? 63  ASP C CB    1 
ATOM   268   C CG    . ASP A  1 63  ? -18.577 19.047  29.937  1.00 40.90 ? 63  ASP C CG    1 
ATOM   269   O OD1   . ASP A  1 63  ? -19.664 19.638  30.161  1.00 48.60 ? 63  ASP C OD1   1 
ATOM   270   O OD2   . ASP A  1 63  ? -17.641 18.969  30.747  1.00 47.01 ? 63  ASP C OD2   1 
ATOM   271   N N     . THR A  1 64  ? -18.011 20.597  26.802  1.00 41.24 ? 64  THR C N     1 
ATOM   272   C CA    . THR A  1 64  ? -17.757 21.949  26.327  1.00 36.61 ? 64  THR C CA    1 
ATOM   273   C C     . THR A  1 64  ? -18.764 22.353  25.264  1.00 39.84 ? 64  THR C C     1 
ATOM   274   O O     . THR A  1 64  ? -19.221 23.501  25.234  1.00 42.22 ? 64  THR C O     1 
ATOM   275   C CB    . THR A  1 64  ? -16.331 22.035  25.791  1.00 42.61 ? 64  THR C CB    1 
ATOM   276   O OG1   . THR A  1 64  ? -15.408 21.727  26.858  1.00 44.66 ? 64  THR C OG1   1 
ATOM   277   C CG2   . THR A  1 64  ? -16.044 23.431  25.236  1.00 34.80 ? 64  THR C CG2   1 
ATOM   278   N N     . LEU A  1 65  ? -19.150 21.411  24.400  1.00 42.44 ? 65  LEU C N     1 
ATOM   279   C CA    . LEU A  1 65  ? -20.079 21.732  23.324  1.00 40.06 ? 65  LEU C CA    1 
ATOM   280   C C     . LEU A  1 65  ? -21.510 21.859  23.820  1.00 47.36 ? 65  LEU C C     1 
ATOM   281   O O     . LEU A  1 65  ? -22.263 22.701  23.318  1.00 52.30 ? 65  LEU C O     1 
ATOM   282   C CB    . LEU A  1 65  ? -20.013 20.676  22.229  1.00 37.25 ? 65  LEU C CB    1 
ATOM   283   C CG    . LEU A  1 65  ? -18.804 20.828  21.325  1.00 38.59 ? 65  LEU C CG    1 
ATOM   284   C CD1   . LEU A  1 65  ? -18.980 19.941  20.101  1.00 31.73 ? 65  LEU C CD1   1 
ATOM   285   C CD2   . LEU A  1 65  ? -18.659 22.293  20.948  1.00 34.53 ? 65  LEU C CD2   1 
ATOM   286   N N     . GLY A  1 66  ? -21.908 21.035  24.790  1.00 46.14 ? 66  GLY C N     1 
ATOM   287   C CA    . GLY A  1 66  ? -23.290 20.985  25.235  1.00 44.08 ? 66  GLY C CA    1 
ATOM   288   C C     . GLY A  1 66  ? -24.110 19.879  24.606  1.00 47.30 ? 66  GLY C C     1 
ATOM   289   O O     . GLY A  1 66  ? -25.304 19.756  24.909  1.00 47.80 ? 66  GLY C O     1 
ATOM   290   N N     . ILE A  1 67  ? -23.501 19.080  23.731  1.00 48.88 ? 67  ILE C N     1 
ATOM   291   C CA    . ILE A  1 67  ? -24.159 17.944  23.117  1.00 51.75 ? 67  ILE C CA    1 
ATOM   292   C C     . ILE A  1 67  ? -24.574 16.913  24.178  1.00 48.48 ? 67  ILE C C     1 
ATOM   293   O O     . ILE A  1 67  ? -24.075 16.911  25.310  1.00 46.77 ? 67  ILE C O     1 
ATOM   294   C CB    . ILE A  1 67  ? -23.166 17.373  22.089  1.00 48.18 ? 67  ILE C CB    1 
ATOM   295   C CG1   . ILE A  1 67  ? -23.163 18.245  20.849  1.00 44.03 ? 67  ILE C CG1   1 
ATOM   296   C CG2   . ILE A  1 67  ? -23.503 15.975  21.670  1.00 53.50 ? 67  ILE C CG2   1 
ATOM   297   C CD1   . ILE A  1 67  ? -24.555 18.725  20.464  1.00 48.34 ? 67  ILE C CD1   1 
ATOM   298   N N     . ASP A  1 68  ? -25.540 16.060  23.822  1.00 44.88 ? 68  ASP C N     1 
ATOM   299   C CA    . ASP A  1 68  ? -25.810 14.860  24.614  1.00 51.81 ? 68  ASP C CA    1 
ATOM   300   C C     . ASP A  1 68  ? -24.713 13.856  24.284  1.00 53.86 ? 68  ASP C C     1 
ATOM   301   O O     . ASP A  1 68  ? -24.755 13.198  23.242  1.00 55.02 ? 68  ASP C O     1 
ATOM   302   C CB    . ASP A  1 68  ? -27.191 14.282  24.321  1.00 49.71 ? 68  ASP C CB    1 
ATOM   303   C CG    . ASP A  1 68  ? -27.414 12.923  24.998  1.00 50.14 ? 68  ASP C CG    1 
ATOM   304   O OD1   . ASP A  1 68  ? -26.820 12.696  26.078  1.00 48.09 ? 68  ASP C OD1   1 
ATOM   305   O OD2   . ASP A  1 68  ? -28.177 12.087  24.455  1.00 48.33 ? 68  ASP C OD2   1 
ATOM   306   N N     . GLY A  1 69  ? -23.725 13.741  25.177  1.00 49.61 ? 69  GLY C N     1 
ATOM   307   C CA    . GLY A  1 69  ? -22.541 12.954  24.872  1.00 45.80 ? 69  GLY C CA    1 
ATOM   308   C C     . GLY A  1 69  ? -22.854 11.507  24.548  1.00 47.18 ? 69  GLY C C     1 
ATOM   309   O O     . GLY A  1 69  ? -22.367 10.956  23.557  1.00 50.23 ? 69  GLY C O     1 
ATOM   310   N N     . THR A  1 70  ? -23.694 10.875  25.364  1.00 45.99 ? 70  THR C N     1 
ATOM   311   C CA    . THR A  1 70  ? -24.007 9.473   25.138  1.00 53.43 ? 70  THR C CA    1 
ATOM   312   C C     . THR A  1 70  ? -24.720 9.241   23.801  1.00 47.50 ? 70  THR C C     1 
ATOM   313   O O     . THR A  1 70  ? -24.936 8.086   23.416  1.00 44.80 ? 70  THR C O     1 
ATOM   314   C CB    . THR A  1 70  ? -24.824 8.967   26.323  1.00 54.95 ? 70  THR C CB    1 
ATOM   315   O OG1   . THR A  1 70  ? -26.069 9.671   26.376  1.00 54.56 ? 70  THR C OG1   1 
ATOM   316   C CG2   . THR A  1 70  ? -24.061 9.245   27.617  1.00 50.89 ? 70  THR C CG2   1 
ATOM   317   N N     . SER A  1 71  ? -25.044 10.310  23.075  1.00 49.71 ? 71  SER C N     1 
ATOM   318   C CA    . SER A  1 71  ? -25.618 10.205  21.738  1.00 52.05 ? 71  SER C CA    1 
ATOM   319   C C     . SER A  1 71  ? -24.553 10.069  20.652  1.00 48.14 ? 71  SER C C     1 
ATOM   320   O O     . SER A  1 71  ? -24.791 9.417   19.628  1.00 48.47 ? 71  SER C O     1 
ATOM   321   C CB    . SER A  1 71  ? -26.493 11.432  21.452  1.00 49.71 ? 71  SER C CB    1 
ATOM   322   O OG    . SER A  1 71  ? -25.705 12.494  20.919  1.00 47.57 ? 71  SER C OG    1 
ATOM   323   N N     . VAL A  1 72  ? -23.396 10.690  20.829  1.00 41.50 ? 72  VAL C N     1 
ATOM   324   C CA    . VAL A  1 72  ? -22.384 10.688  19.785  1.00 43.42 ? 72  VAL C CA    1 
ATOM   325   C C     . VAL A  1 72  ? -21.453 9.506   19.997  1.00 43.00 ? 72  VAL C C     1 
ATOM   326   O O     . VAL A  1 72  ? -20.907 9.315   21.087  1.00 46.25 ? 72  VAL C O     1 
ATOM   327   C CB    . VAL A  1 72  ? -21.618 12.014  19.759  1.00 40.05 ? 72  VAL C CB    1 
ATOM   328   C CG1   . VAL A  1 72  ? -20.700 12.040  18.565  1.00 39.67 ? 72  VAL C CG1   1 
ATOM   329   C CG2   . VAL A  1 72  ? -22.604 13.166  19.688  1.00 39.50 ? 72  VAL C CG2   1 
ATOM   330   N N     . HIS A  1 73  ? -21.292 8.697   18.965  1.00 41.15 ? 73  HIS C N     1 
ATOM   331   C CA    . HIS A  1 73  ? -20.440 7.530   19.051  1.00 40.70 ? 73  HIS C CA    1 
ATOM   332   C C     . HIS A  1 73  ? -19.228 7.730   18.156  1.00 44.06 ? 73  HIS C C     1 
ATOM   333   O O     . HIS A  1 73  ? -19.182 8.616   17.298  1.00 40.45 ? 73  HIS C O     1 
ATOM   334   C CB    . HIS A  1 73  ? -21.202 6.251   18.663  1.00 42.23 ? 73  HIS C CB    1 
ATOM   335   C CG    . HIS A  1 73  ? -22.267 5.861   19.649  1.00 55.58 ? 73  HIS C CG    1 
ATOM   336   N ND1   . HIS A  1 73  ? -22.047 4.964   20.676  1.00 55.82 ? 73  HIS C ND1   1 
ATOM   337   C CD2   . HIS A  1 73  ? -23.554 6.267   19.777  1.00 49.98 ? 73  HIS C CD2   1 
ATOM   338   C CE1   . HIS A  1 73  ? -23.155 4.824   21.383  1.00 46.06 ? 73  HIS C CE1   1 
ATOM   339   N NE2   . HIS A  1 73  ? -24.083 5.604   20.862  1.00 49.17 ? 73  HIS C NE2   1 
ATOM   340   N N     . VAL A  1 74  ? -18.229 6.898   18.392  1.00 40.81 ? 74  VAL C N     1 
ATOM   341   C CA    . VAL A  1 74  ? -16.971 6.968   17.686  1.00 36.50 ? 74  VAL C CA    1 
ATOM   342   C C     . VAL A  1 74  ? -16.671 5.546   17.248  1.00 37.95 ? 74  VAL C C     1 
ATOM   343   O O     . VAL A  1 74  ? -16.632 4.638   18.079  1.00 37.02 ? 74  VAL C O     1 
ATOM   344   C CB    . VAL A  1 74  ? -15.860 7.536   18.583  1.00 35.52 ? 74  VAL C CB    1 
ATOM   345   C CG1   . VAL A  1 74  ? -15.970 9.035   18.669  1.00 32.41 ? 74  VAL C CG1   1 
ATOM   346   C CG2   . VAL A  1 74  ? -15.960 6.952   19.982  1.00 43.44 ? 74  VAL C CG2   1 
ATOM   347   N N     . GLU A  1 75  ? -16.531 5.330   15.958  1.00 38.97 ? 75  GLU C N     1 
ATOM   348   C CA    . GLU A  1 75  ? -16.372 3.970   15.457  1.00 44.18 ? 75  GLU C CA    1 
ATOM   349   C C     . GLU A  1 75  ? -14.918 3.810   15.017  1.00 44.15 ? 75  GLU C C     1 
ATOM   350   O O     . GLU A  1 75  ? -14.499 4.342   13.983  1.00 41.94 ? 75  GLU C O     1 
ATOM   351   C CB    . GLU A  1 75  ? -17.382 3.680   14.345  1.00 46.60 ? 75  GLU C CB    1 
ATOM   352   C CG    . GLU A  1 75  ? -17.864 2.216   14.257  1.00 44.50 ? 75  GLU C CG    1 
ATOM   353   C CD    . GLU A  1 75  ? -18.832 1.785   15.367  1.00 48.12 ? 75  GLU C CD    1 
ATOM   354   O OE1   . GLU A  1 75  ? -19.297 2.630   16.160  1.00 47.55 ? 75  GLU C OE1   1 
ATOM   355   O OE2   . GLU A  1 75  ? -19.136 0.573   15.440  1.00 50.81 ? 75  GLU C OE2   1 
ATOM   356   N N     . ARG A  1 76  ? -14.143 3.101   15.827  1.00 37.96 ? 76  ARG C N     1 
ATOM   357   C CA    . ARG A  1 76  ? -12.727 2.940   15.557  1.00 37.98 ? 76  ARG C CA    1 
ATOM   358   C C     . ARG A  1 76  ? -12.525 1.873   14.493  1.00 39.96 ? 76  ARG C C     1 
ATOM   359   O O     . ARG A  1 76  ? -13.036 0.756   14.625  1.00 39.65 ? 76  ARG C O     1 
ATOM   360   C CB    . ARG A  1 76  ? -11.969 2.566   16.837  1.00 44.23 ? 76  ARG C CB    1 
ATOM   361   C CG    . ARG A  1 76  ? -12.010 3.644   17.931  1.00 40.53 ? 76  ARG C CG    1 
ATOM   362   C CD    . ARG A  1 76  ? -11.519 3.159   19.307  1.00 46.41 ? 76  ARG C CD    1 
ATOM   363   N NE    . ARG A  1 76  ? -11.831 4.138   20.349  1.00 44.89 ? 76  ARG C NE    1 
ATOM   364   C CZ    . ARG A  1 76  ? -13.031 4.293   20.892  1.00 44.07 ? 76  ARG C CZ    1 
ATOM   365   N NH1   . ARG A  1 76  ? -14.042 3.492   20.582  1.00 37.96 ? 76  ARG C NH1   1 
ATOM   366   N NH2   . ARG A  1 76  ? -13.225 5.275   21.769  1.00 50.51 ? 76  ARG C NH2   1 
ATOM   367   N N     . THR A  1 77  ? -11.793 2.235   13.435  1.00 45.57 ? 77  THR C N     1 
ATOM   368   C CA    . THR A  1 77  ? -11.298 1.320   12.411  1.00 45.04 ? 77  THR C CA    1 
ATOM   369   C C     . THR A  1 77  ? -9.826  1.026   12.652  1.00 46.25 ? 77  THR C C     1 
ATOM   370   O O     . THR A  1 77  ? -9.054  1.923   12.995  1.00 50.18 ? 77  THR C O     1 
ATOM   371   C CB    . THR A  1 77  ? -11.444 1.935   11.026  1.00 44.76 ? 77  THR C CB    1 
ATOM   372   O OG1   . THR A  1 77  ? -11.371 3.358   11.160  1.00 47.19 ? 77  THR C OG1   1 
ATOM   373   C CG2   . THR A  1 77  ? -12.765 1.544   10.379  1.00 41.74 ? 77  THR C CG2   1 
ATOM   374   N N     . GLN A  1 78  ? -9.425  -0.215  12.436  1.00 51.47 ? 78  GLN C N     1 
ATOM   375   C CA    . GLN A  1 78  ? -8.036  -0.584  12.668  1.00 59.97 ? 78  GLN C CA    1 
ATOM   376   C C     . GLN A  1 78  ? -7.125  -0.286  11.478  1.00 57.06 ? 78  GLN C C     1 
ATOM   377   O O     . GLN A  1 78  ? -5.941  -0.635  11.530  1.00 56.52 ? 78  GLN C O     1 
ATOM   378   C CB    . GLN A  1 78  ? -7.939  -2.066  13.047  1.00 60.89 ? 78  GLN C CB    1 
ATOM   379   C CG    . GLN A  1 78  ? -8.675  -2.424  14.324  1.00 53.48 ? 78  GLN C CG    1 
ATOM   380   C CD    . GLN A  1 78  ? -8.442  -3.859  14.725  1.00 60.71 ? 78  GLN C CD    1 
ATOM   381   O OE1   . GLN A  1 78  ? -7.826  -4.629  13.984  1.00 61.97 ? 78  GLN C OE1   1 
ATOM   382   N NE2   . GLN A  1 78  ? -8.922  -4.230  15.909  1.00 61.02 ? 78  GLN C NE2   1 
ATOM   383   N N     . THR A  1 79  ? -7.642  0.336   10.419  1.00 59.16 ? 79  THR C N     1 
ATOM   384   C CA    . THR A  1 79  ? -6.891  0.674   9.218   1.00 53.67 ? 79  THR C CA    1 
ATOM   385   C C     . THR A  1 79  ? -7.188  2.110   8.813   1.00 52.62 ? 79  THR C C     1 
ATOM   386   O O     . THR A  1 79  ? -8.162  2.710   9.285   1.00 54.91 ? 79  THR C O     1 
ATOM   387   C CB    . THR A  1 79  ? -7.224  -0.246  8.025   1.00 60.21 ? 79  THR C CB    1 
ATOM   388   O OG1   . THR A  1 79  ? -8.561  0.002   7.558   1.00 58.16 ? 79  THR C OG1   1 
ATOM   389   C CG2   . THR A  1 79  ? -7.050  -1.731  8.380   1.00 60.55 ? 79  THR C CG2   1 
ATOM   390   N N     . PRO A  1 80  ? -6.360  2.695   7.946   1.00 48.18 ? 80  PRO C N     1 
ATOM   391   C CA    . PRO A  1 80  ? -6.690  4.001   7.367   1.00 47.47 ? 80  PRO C CA    1 
ATOM   392   C C     . PRO A  1 80  ? -7.992  3.977   6.580   1.00 44.93 ? 80  PRO C C     1 
ATOM   393   O O     . PRO A  1 80  ? -8.443  2.940   6.089   1.00 43.20 ? 80  PRO C O     1 
ATOM   394   C CB    . PRO A  1 80  ? -5.496  4.284   6.448   1.00 44.73 ? 80  PRO C CB    1 
ATOM   395   C CG    . PRO A  1 80  ? -4.376  3.604   7.127   1.00 44.82 ? 80  PRO C CG    1 
ATOM   396   C CD    . PRO A  1 80  ? -4.969  2.317   7.654   1.00 47.97 ? 80  PRO C CD    1 
ATOM   397   N N     . LEU A  1 81  ? -8.584  5.165   6.445   1.00 44.72 ? 81  LEU C N     1 
ATOM   398   C CA    . LEU A  1 81  ? -9.891  5.339   5.807   1.00 47.70 ? 81  LEU C CA    1 
ATOM   399   C C     . LEU A  1 81  ? -9.764  5.305   4.277   1.00 47.43 ? 81  LEU C C     1 
ATOM   400   O O     . LEU A  1 81  ? -10.106 6.257   3.573   1.00 46.53 ? 81  LEU C O     1 
ATOM   401   C CB    . LEU A  1 81  ? -10.531 6.639   6.296   1.00 42.45 ? 81  LEU C CB    1 
ATOM   402   C CG    . LEU A  1 81  ? -11.128 6.598   7.724   1.00 45.38 ? 81  LEU C CG    1 
ATOM   403   C CD1   . LEU A  1 81  ? -11.962 7.830   8.106   1.00 33.62 ? 81  LEU C CD1   1 
ATOM   404   C CD2   . LEU A  1 81  ? -11.953 5.325   7.914   1.00 48.32 ? 81  LEU C CD2   1 
ATOM   405   N N     . SER A  1 82  ? -9.280  4.163   3.770   1.00 46.00 ? 82  SER C N     1 
ATOM   406   C CA    . SER A  1 82  ? -8.988  3.937   2.354   1.00 40.53 ? 82  SER C CA    1 
ATOM   407   C C     . SER A  1 82  ? -10.264 3.660   1.563   1.00 39.49 ? 82  SER C C     1 
ATOM   408   O O     . SER A  1 82  ? -11.297 3.293   2.131   1.00 39.23 ? 82  SER C O     1 
ATOM   409   C CB    . SER A  1 82  ? -8.043  2.750   2.186   1.00 41.62 ? 82  SER C CB    1 
ATOM   410   O OG    . SER A  1 82  ? -8.776  1.572   1.879   1.00 41.55 ? 82  SER C OG    1 
ATOM   411   N N     . GLU A  1 83  ? -10.175 3.818   0.228   1.00 29.05 ? 83  GLU C N     1 
ATOM   412   C CA    . GLU A  1 83  ? -11.327 3.535   -0.631  1.00 29.70 ? 83  GLU C CA    1 
ATOM   413   C C     . GLU A  1 83  ? -11.798 2.105   -0.455  1.00 34.49 ? 83  GLU C C     1 
ATOM   414   O O     . GLU A  1 83  ? -12.999 1.826   -0.542  1.00 33.41 ? 83  GLU C O     1 
ATOM   415   C CB    . GLU A  1 83  ? -10.999 3.774   -2.107  1.00 26.87 ? 83  GLU C CB    1 
ATOM   416   C CG    . GLU A  1 83  ? -10.750 5.243   -2.512  1.00 25.87 ? 83  GLU C CG    1 
ATOM   417   C CD    . GLU A  1 83  ? -12.003 6.110   -2.511  1.00 27.52 ? 83  GLU C CD    1 
ATOM   418   O OE1   . GLU A  1 83  ? -12.318 6.683   -1.450  1.00 33.18 ? 83  GLU C OE1   1 
ATOM   419   O OE2   . GLU A  1 83  ? -12.670 6.242   -3.565  1.00 30.03 ? 83  GLU C OE2   1 
ATOM   420   N N     . ALA A  1 84  ? -10.872 1.187   -0.199  1.00 35.12 ? 84  ALA C N     1 
ATOM   421   C CA    . ALA A  1 84  ? -11.279 -0.194  -0.032  1.00 35.00 ? 84  ALA C CA    1 
ATOM   422   C C     . ALA A  1 84  ? -12.133 -0.370  1.222   1.00 37.82 ? 84  ALA C C     1 
ATOM   423   O O     . ALA A  1 84  ? -13.066 -1.186  1.226   1.00 39.96 ? 84  ALA C O     1 
ATOM   424   C CB    . ALA A  1 84  ? -10.041 -1.091  -0.010  1.00 32.07 ? 84  ALA C CB    1 
ATOM   425   N N     . VAL A  1 85  ? -11.861 0.405   2.280   1.00 35.57 ? 85  VAL C N     1 
ATOM   426   C CA    . VAL A  1 85  ? -12.654 0.265   3.503   1.00 36.05 ? 85  VAL C CA    1 
ATOM   427   C C     . VAL A  1 85  ? -14.064 0.831   3.305   1.00 34.64 ? 85  VAL C C     1 
ATOM   428   O O     . VAL A  1 85  ? -15.052 0.206   3.701   1.00 43.87 ? 85  VAL C O     1 
ATOM   429   C CB    . VAL A  1 85  ? -11.934 0.905   4.708   1.00 38.81 ? 85  VAL C CB    1 
ATOM   430   C CG1   . VAL A  1 85  ? -12.721 0.658   5.985   1.00 36.05 ? 85  VAL C CG1   1 
ATOM   431   C CG2   . VAL A  1 85  ? -10.529 0.328   4.868   1.00 33.92 ? 85  VAL C CG2   1 
ATOM   432   N N     . LEU A  1 86  ? -14.193 2.002   2.678   1.00 34.42 ? 86  LEU C N     1 
ATOM   433   C CA    . LEU A  1 86  ? -15.519 2.505   2.323   1.00 33.26 ? 86  LEU C CA    1 
ATOM   434   C C     . LEU A  1 86  ? -16.316 1.478   1.536   1.00 38.19 ? 86  LEU C C     1 
ATOM   435   O O     . LEU A  1 86  ? -17.549 1.532   1.521   1.00 35.74 ? 86  LEU C O     1 
ATOM   436   C CB    . LEU A  1 86  ? -15.415 3.791   1.490   1.00 28.12 ? 86  LEU C CB    1 
ATOM   437   C CG    . LEU A  1 86  ? -14.702 4.992   2.113   1.00 28.93 ? 86  LEU C CG    1 
ATOM   438   C CD1   . LEU A  1 86  ? -15.231 6.254   1.506   1.00 27.76 ? 86  LEU C CD1   1 
ATOM   439   C CD2   . LEU A  1 86  ? -14.892 5.021   3.609   1.00 29.68 ? 86  LEU C CD2   1 
ATOM   440   N N     . GLN A  1 87  ? -15.633 0.551   0.875   1.00 38.52 ? 87  GLN C N     1 
ATOM   441   C CA    . GLN A  1 87  ? -16.280 -0.484  0.102   1.00 35.09 ? 87  GLN C CA    1 
ATOM   442   C C     . GLN A  1 87  ? -16.315 -1.813  0.837   1.00 43.62 ? 87  GLN C C     1 
ATOM   443   O O     . GLN A  1 87  ? -16.998 -2.738  0.385   1.00 50.13 ? 87  GLN C O     1 
ATOM   444   C CB    . GLN A  1 87  ? -15.559 -0.641  -1.240  1.00 37.36 ? 87  GLN C CB    1 
ATOM   445   C CG    . GLN A  1 87  ? -15.477 0.659   -2.053  1.00 36.42 ? 87  GLN C CG    1 
ATOM   446   C CD    . GLN A  1 87  ? -14.531 0.535   -3.240  1.00 44.39 ? 87  GLN C CD    1 
ATOM   447   O OE1   . GLN A  1 87  ? -13.707 -0.385  -3.301  1.00 50.66 ? 87  GLN C OE1   1 
ATOM   448   N NE2   . GLN A  1 87  ? -14.662 1.444   -4.200  1.00 37.78 ? 87  GLN C NE2   1 
ATOM   449   N N     . ASP A  1 88  ? -15.595 -1.923  1.943   1.00 38.46 ? 88  ASP C N     1 
ATOM   450   C CA    . ASP A  1 88  ? -15.614 -3.114  2.771   1.00 41.37 ? 88  ASP C CA    1 
ATOM   451   C C     . ASP A  1 88  ? -17.026 -3.397  3.278   1.00 41.96 ? 88  ASP C C     1 
ATOM   452   O O     . ASP A  1 88  ? -17.598 -2.561  3.995   1.00 41.56 ? 88  ASP C O     1 
ATOM   453   C CB    . ASP A  1 88  ? -14.654 -2.927  3.938   1.00 39.44 ? 88  ASP C CB    1 
ATOM   454   C CG    . ASP A  1 88  ? -14.460 -4.187  4.740   1.00 51.38 ? 88  ASP C CG    1 
ATOM   455   O OD1   . ASP A  1 88  ? -15.166 -5.193  4.479   1.00 52.62 ? 88  ASP C OD1   1 
ATOM   456   O OD2   . ASP A  1 88  ? -13.582 -4.171  5.632   1.00 57.48 ? 88  ASP C OD2   1 
ATOM   457   N N     . PRO A  1 89  ? -17.614 -4.550  2.940   1.00 43.95 ? 89  PRO C N     1 
ATOM   458   C CA    . PRO A  1 89  ? -18.981 -4.849  3.399   1.00 46.76 ? 89  PRO C CA    1 
ATOM   459   C C     . PRO A  1 89  ? -19.165 -4.814  4.902   1.00 43.82 ? 89  PRO C C     1 
ATOM   460   O O     . PRO A  1 89  ? -20.241 -4.423  5.370   1.00 45.20 ? 89  PRO C O     1 
ATOM   461   C CB    . PRO A  1 89  ? -19.216 -6.255  2.837   1.00 43.27 ? 89  PRO C CB    1 
ATOM   462   C CG    . PRO A  1 89  ? -18.433 -6.243  1.572   1.00 36.93 ? 89  PRO C CG    1 
ATOM   463   C CD    . PRO A  1 89  ? -17.181 -5.492  1.896   1.00 47.25 ? 89  PRO C CD    1 
ATOM   464   N N     . GLU A  1 90  ? -18.158 -5.220  5.679   1.00 45.21 ? 90  GLU C N     1 
ATOM   465   C CA    . GLU A  1 90  ? -18.301 -5.165  7.133   1.00 45.08 ? 90  GLU C CA    1 
ATOM   466   C C     . GLU A  1 90  ? -18.267 -3.725  7.626   1.00 43.09 ? 90  GLU C C     1 
ATOM   467   O O     . GLU A  1 90  ? -18.991 -3.362  8.566   1.00 40.54 ? 90  GLU C O     1 
ATOM   468   C CB    . GLU A  1 90  ? -17.205 -5.992  7.809   1.00 42.77 ? 90  GLU C CB    1 
ATOM   469   C CG    . GLU A  1 90  ? -16.476 -6.934  6.862   1.00 48.87 ? 90  GLU C CG    1 
ATOM   470   C CD    . GLU A  1 90  ? -15.046 -7.211  7.297   1.00 56.79 ? 90  GLU C CD    1 
ATOM   471   O OE1   . GLU A  1 90  ? -14.637 -6.665  8.342   1.00 61.88 ? 90  GLU C OE1   1 
ATOM   472   O OE2   . GLU A  1 90  ? -14.328 -7.975  6.606   1.00 54.86 ? 90  GLU C OE2   1 
ATOM   473   N N     . PHE A  1 91  ? -17.431 -2.895  6.996   1.00 42.68 ? 91  PHE C N     1 
ATOM   474   C CA    . PHE A  1 91  ? -17.344 -1.493  7.377   1.00 38.92 ? 91  PHE C CA    1 
ATOM   475   C C     . PHE A  1 91  ? -18.672 -0.801  7.153   1.00 39.40 ? 91  PHE C C     1 
ATOM   476   O O     . PHE A  1 91  ? -19.143 -0.034  8.001   1.00 38.34 ? 91  PHE C O     1 
ATOM   477   C CB    . PHE A  1 91  ? -16.234 -0.801  6.581   1.00 34.27 ? 91  PHE C CB    1 
ATOM   478   C CG    . PHE A  1 91  ? -16.255 0.692   6.691   1.00 32.19 ? 91  PHE C CG    1 
ATOM   479   C CD1   . PHE A  1 91  ? -15.551 1.336   7.696   1.00 32.28 ? 91  PHE C CD1   1 
ATOM   480   C CD2   . PHE A  1 91  ? -16.989 1.458   5.805   1.00 35.08 ? 91  PHE C CD2   1 
ATOM   481   C CE1   . PHE A  1 91  ? -15.575 2.704   7.809   1.00 31.25 ? 91  PHE C CE1   1 
ATOM   482   C CE2   . PHE A  1 91  ? -17.018 2.833   5.922   1.00 35.30 ? 91  PHE C CE2   1 
ATOM   483   C CZ    . PHE A  1 91  ? -16.307 3.451   6.926   1.00 33.03 ? 91  PHE C CZ    1 
ATOM   484   N N     . ILE A  1 92  ? -19.306 -1.084  6.026   1.00 39.97 ? 92  ILE C N     1 
ATOM   485   C CA    . ILE A  1 92  ? -20.584 -0.461  5.725   1.00 40.19 ? 92  ILE C CA    1 
ATOM   486   C C     . ILE A  1 92  ? -21.674 -0.955  6.678   1.00 41.92 ? 92  ILE C C     1 
ATOM   487   O O     . ILE A  1 92  ? -22.472 -0.158  7.192   1.00 42.21 ? 92  ILE C O     1 
ATOM   488   C CB    . ILE A  1 92  ? -20.929 -0.718  4.253   1.00 39.86 ? 92  ILE C CB    1 
ATOM   489   C CG1   . ILE A  1 92  ? -19.661 -0.494  3.437   1.00 38.37 ? 92  ILE C CG1   1 
ATOM   490   C CG2   . ILE A  1 92  ? -22.010 0.218   3.789   1.00 37.59 ? 92  ILE C CG2   1 
ATOM   491   C CD1   . ILE A  1 92  ? -19.879 -0.478  1.981   1.00 40.07 ? 92  ILE C CD1   1 
ATOM   492   N N     . ASP A  1 93  ? -21.733 -2.273  6.927   1.00 38.86 ? 93  ASP C N     1 
ATOM   493   C CA    . ASP A  1 93  ? -22.740 -2.796  7.855   1.00 42.03 ? 93  ASP C CA    1 
ATOM   494   C C     . ASP A  1 93  ? -22.599 -2.136  9.222   1.00 46.28 ? 93  ASP C C     1 
ATOM   495   O O     . ASP A  1 93  ? -23.578 -1.611  9.772   1.00 44.61 ? 93  ASP C O     1 
ATOM   496   C CB    . ASP A  1 93  ? -22.639 -4.322  7.981   1.00 40.73 ? 93  ASP C CB    1 
ATOM   497   C CG    . ASP A  1 93  ? -23.363 -5.073  6.861   1.00 41.07 ? 93  ASP C CG    1 
ATOM   498   O OD1   . ASP A  1 93  ? -24.066 -4.430  6.063   1.00 52.27 ? 93  ASP C OD1   1 
ATOM   499   O OD2   . ASP A  1 93  ? -23.227 -6.320  6.772   1.00 41.41 ? 93  ASP C OD2   1 
ATOM   500   N N     . ARG A  1 94  ? -21.368 -2.122  9.771   1.00 42.97 ? 94  ARG C N     1 
ATOM   501   C CA    . ARG A  1 94  ? -21.106 -1.428  11.034  1.00 45.16 ? 94  ARG C CA    1 
ATOM   502   C C     . ARG A  1 94  ? -21.531 0.038   10.983  1.00 46.30 ? 94  ARG C C     1 
ATOM   503   O O     . ARG A  1 94  ? -21.776 0.641   12.036  1.00 42.40 ? 94  ARG C O     1 
ATOM   504   C CB    . ARG A  1 94  ? -19.618 -1.525  11.417  1.00 45.32 ? 94  ARG C CB    1 
ATOM   505   C CG    . ARG A  1 94  ? -19.191 -2.841  12.098  1.00 49.19 ? 94  ARG C CG    1 
ATOM   506   C CD    . ARG A  1 94  ? -18.762 -2.683  13.595  1.00 47.31 ? 94  ARG C CD    1 
ATOM   507   N NE    . ARG A  1 94  ? -17.954 -1.499  13.881  1.00 49.48 ? 94  ARG C NE    1 
ATOM   508   C CZ    . ARG A  1 94  ? -16.702 -1.316  13.470  1.00 54.60 ? 94  ARG C CZ    1 
ATOM   509   N NH1   . ARG A  1 94  ? -16.085 -2.202  12.706  1.00 57.49 ? 94  ARG C NH1   1 
ATOM   510   N NH2   . ARG A  1 94  ? -16.048 -0.215  13.836  1.00 48.73 ? 94  ARG C NH2   1 
ATOM   511   N N     . LEU A  1 95  ? -21.624 0.619   9.781   1.00 47.16 ? 95  LEU C N     1 
ATOM   512   C CA    . LEU A  1 95  ? -22.183 1.951   9.577   1.00 46.30 ? 95  LEU C CA    1 
ATOM   513   C C     . LEU A  1 95  ? -23.705 1.912   9.442   1.00 45.29 ? 95  LEU C C     1 
ATOM   514   O O     . LEU A  1 95  ? -24.393 2.800   9.951   1.00 40.23 ? 95  LEU C O     1 
ATOM   515   C CB    . LEU A  1 95  ? -21.559 2.592   8.331   1.00 41.00 ? 95  LEU C CB    1 
ATOM   516   C CG    . LEU A  1 95  ? -20.261 3.396   8.500   1.00 39.65 ? 95  LEU C CG    1 
ATOM   517   C CD1   . LEU A  1 95  ? -20.066 4.362   7.338   1.00 34.02 ? 95  LEU C CD1   1 
ATOM   518   C CD2   . LEU A  1 95  ? -20.225 4.149   9.857   1.00 47.62 ? 95  LEU C CD2   1 
ATOM   519   N N     . ALA A  1 96  ? -24.234 0.897   8.754   1.00 42.04 ? 96  ALA C N     1 
ATOM   520   C CA    . ALA A  1 96  ? -25.676 0.706   8.695   1.00 41.66 ? 96  ALA C CA    1 
ATOM   521   C C     . ALA A  1 96  ? -26.278 0.657   10.090  1.00 46.67 ? 96  ALA C C     1 
ATOM   522   O O     . ALA A  1 96  ? -27.282 1.329   10.363  1.00 43.39 ? 96  ALA C O     1 
ATOM   523   C CB    . ALA A  1 96  ? -26.001 -0.573  7.925   1.00 40.55 ? 96  ALA C CB    1 
ATOM   524   N N     . ALA A  1 97  ? -25.629 -0.065  11.010  1.00 40.90 ? 97  ALA C N     1 
ATOM   525   C CA    . ALA A  1 97  ? -26.203 -0.253  12.337  1.00 41.34 ? 97  ALA C CA    1 
ATOM   526   C C     . ALA A  1 97  ? -26.580 1.077   12.959  1.00 40.83 ? 97  ALA C C     1 
ATOM   527   O O     . ALA A  1 97  ? -27.578 1.180   13.679  1.00 48.65 ? 97  ALA C O     1 
ATOM   528   C CB    . ALA A  1 97  ? -25.223 -1.012  13.231  1.00 49.22 ? 97  ALA C CB    1 
ATOM   529   N N     . HIS A  1 98  ? -25.815 2.120   12.660  1.00 42.79 ? 98  HIS C N     1 
ATOM   530   C CA    . HIS A  1 98  ? -26.152 3.450   13.161  1.00 42.59 ? 98  HIS C CA    1 
ATOM   531   C C     . HIS A  1 98  ? -27.080 4.201   12.204  1.00 41.27 ? 98  HIS C C     1 
ATOM   532   O O     . HIS A  1 98  ? -28.003 4.902   12.635  1.00 40.83 ? 98  HIS C O     1 
ATOM   533   C CB    . HIS A  1 98  ? -24.882 4.266   13.392  1.00 37.38 ? 98  HIS C CB    1 
ATOM   534   C CG    . HIS A  1 98  ? -23.904 3.644   14.338  1.00 42.59 ? 98  HIS C CG    1 
ATOM   535   N ND1   . HIS A  1 98  ? -23.416 4.321   15.436  1.00 48.57 ? 98  HIS C ND1   1 
ATOM   536   C CD2   . HIS A  1 98  ? -23.294 2.432   14.344  1.00 51.50 ? 98  HIS C CD2   1 
ATOM   537   C CE1   . HIS A  1 98  ? -22.556 3.552   16.084  1.00 52.03 ? 98  HIS C CE1   1 
ATOM   538   N NE2   . HIS A  1 98  ? -22.459 2.400   15.441  1.00 53.13 ? 98  HIS C NE2   1 
ATOM   539   N N     . THR A  1 99  ? -26.854 4.077   10.906  1.00 39.44 ? 99  THR C N     1 
ATOM   540   C CA    . THR A  1 99  ? -27.609 4.891   9.979   1.00 41.71 ? 99  THR C CA    1 
ATOM   541   C C     . THR A  1 99  ? -29.064 4.465   9.900   1.00 46.28 ? 99  THR C C     1 
ATOM   542   O O     . THR A  1 99  ? -29.899 5.239   9.416   1.00 45.83 ? 99  THR C O     1 
ATOM   543   C CB    . THR A  1 99  ? -26.964 4.806   8.592   1.00 41.95 ? 99  THR C CB    1 
ATOM   544   O OG1   . THR A  1 99  ? -26.786 3.432   8.207   1.00 39.75 ? 99  THR C OG1   1 
ATOM   545   C CG2   . THR A  1 99  ? -25.606 5.456   8.627   1.00 41.98 ? 99  THR C CG2   1 
ATOM   546   N N     . GLY A  1 100 ? -29.386 3.254   10.342  1.00 43.48 ? 100 GLY C N     1 
ATOM   547   C CA    . GLY A  1 100 ? -30.742 2.780   10.158  1.00 41.02 ? 100 GLY C CA    1 
ATOM   548   C C     . GLY A  1 100 ? -31.091 2.740   8.685   1.00 46.57 ? 100 GLY C C     1 
ATOM   549   O O     . GLY A  1 100 ? -30.297 2.283   7.855   1.00 54.86 ? 100 GLY C O     1 
ATOM   550   N N     . THR A  1 101 ? -32.283 3.244   8.341   1.00 46.79 ? 101 THR C N     1 
ATOM   551   C CA    . THR A  1 101 ? -32.763 3.252   6.961   1.00 50.78 ? 101 THR C CA    1 
ATOM   552   C C     . THR A  1 101 ? -32.322 4.487   6.195   1.00 48.04 ? 101 THR C C     1 
ATOM   553   O O     . THR A  1 101 ? -32.929 4.812   5.168   1.00 49.45 ? 101 THR C O     1 
ATOM   554   C CB    . THR A  1 101 ? -34.294 3.128   6.897   1.00 55.29 ? 101 THR C CB    1 
ATOM   555   O OG1   . THR A  1 101 ? -34.703 2.921   5.535   1.00 52.26 ? 101 THR C OG1   1 
ATOM   556   C CG2   . THR A  1 101 ? -34.965 4.387   7.425   1.00 50.53 ? 101 THR C CG2   1 
ATOM   557   N N     . GLY A  1 102 ? -31.281 5.176   6.671   1.00 50.89 ? 102 GLY C N     1 
ATOM   558   C CA    . GLY A  1 102 ? -30.725 6.334   5.988   1.00 47.41 ? 102 GLY C CA    1 
ATOM   559   C C     . GLY A  1 102 ? -31.479 7.620   6.262   1.00 48.31 ? 102 GLY C C     1 
ATOM   560   O O     . GLY A  1 102 ? -30.888 8.707   6.270   1.00 46.43 ? 102 GLY C O     1 
ATOM   561   N N     . ALA A  1 103 ? -32.789 7.498   6.485   1.00 44.21 ? 103 ALA C N     1 
ATOM   562   C CA    . ALA A  1 103 ? -33.637 8.653   6.746   1.00 41.72 ? 103 ALA C CA    1 
ATOM   563   C C     . ALA A  1 103 ? -33.125 9.451   7.937   1.00 39.71 ? 103 ALA C C     1 
ATOM   564   O O     . ALA A  1 103 ? -32.989 8.919   9.038   1.00 47.73 ? 103 ALA C O     1 
ATOM   565   C CB    . ALA A  1 103 ? -35.066 8.189   7.002   1.00 45.47 ? 103 ALA C CB    1 
ATOM   566   N N     . GLY A  1 104 ? -32.876 10.733  7.724   1.00 43.67 ? 104 GLY C N     1 
ATOM   567   C CA    . GLY A  1 104 ? -32.353 11.623  8.736   1.00 40.22 ? 104 GLY C CA    1 
ATOM   568   C C     . GLY A  1 104 ? -30.874 11.897  8.590   1.00 47.46 ? 104 GLY C C     1 
ATOM   569   O O     . GLY A  1 104 ? -30.378 12.917  9.097   1.00 45.82 ? 104 GLY C O     1 
ATOM   570   N N     . TRP A  1 105 ? -30.174 11.044  7.856   1.00 45.46 ? 105 TRP C N     1 
ATOM   571   C CA    . TRP A  1 105 ? -28.732 10.938  7.943   1.00 45.74 ? 105 TRP C CA    1 
ATOM   572   C C     . TRP A  1 105 ? -28.060 11.498  6.692   1.00 41.89 ? 105 TRP C C     1 
ATOM   573   O O     . TRP A  1 105 ? -28.653 11.547  5.607   1.00 41.80 ? 105 TRP C O     1 
ATOM   574   C CB    . TRP A  1 105 ? -28.335 9.476   8.165   1.00 43.19 ? 105 TRP C CB    1 
ATOM   575   C CG    . TRP A  1 105 ? -28.462 8.979   9.589   1.00 41.47 ? 105 TRP C CG    1 
ATOM   576   C CD1   . TRP A  1 105 ? -29.588 8.501   10.206  1.00 44.24 ? 105 TRP C CD1   1 
ATOM   577   C CD2   . TRP A  1 105 ? -27.425 8.915   10.556  1.00 44.02 ? 105 TRP C CD2   1 
ATOM   578   N NE1   . TRP A  1 105 ? -29.305 8.123   11.492  1.00 42.01 ? 105 TRP C NE1   1 
ATOM   579   C CE2   . TRP A  1 105 ? -27.984 8.373   11.737  1.00 46.59 ? 105 TRP C CE2   1 
ATOM   580   C CE3   . TRP A  1 105 ? -26.070 9.261   10.545  1.00 42.09 ? 105 TRP C CE3   1 
ATOM   581   C CZ2   . TRP A  1 105 ? -27.239 8.182   12.890  1.00 42.65 ? 105 TRP C CZ2   1 
ATOM   582   C CZ3   . TRP A  1 105 ? -25.326 9.058   11.690  1.00 38.59 ? 105 TRP C CZ3   1 
ATOM   583   C CH2   . TRP A  1 105 ? -25.912 8.532   12.849  1.00 43.61 ? 105 TRP C CH2   1 
ATOM   584   N N     . SER A  1 106 ? -26.807 11.915  6.868   1.00 39.45 ? 106 SER C N     1 
ATOM   585   C CA    . SER A  1 106 ? -25.935 12.355  5.792   1.00 34.66 ? 106 SER C CA    1 
ATOM   586   C C     . SER A  1 106 ? -24.513 11.906  6.114   1.00 40.37 ? 106 SER C C     1 
ATOM   587   O O     . SER A  1 106 ? -24.185 11.608  7.264   1.00 43.06 ? 106 SER C O     1 
ATOM   588   C CB    . SER A  1 106 ? -25.998 13.863  5.615   1.00 36.08 ? 106 SER C CB    1 
ATOM   589   O OG    . SER A  1 106 ? -25.717 14.483  6.854   1.00 43.46 ? 106 SER C OG    1 
ATOM   590   N N     . LEU A  1 107 ? -23.674 11.839  5.083   1.00 43.14 ? 107 LEU C N     1 
ATOM   591   C CA    . LEU A  1 107 ? -22.242 11.617  5.255   1.00 36.79 ? 107 LEU C CA    1 
ATOM   592   C C     . LEU A  1 107 ? -21.522 12.960  5.331   1.00 31.96 ? 107 LEU C C     1 
ATOM   593   O O     . LEU A  1 107 ? -21.888 13.915  4.649   1.00 33.20 ? 107 LEU C O     1 
ATOM   594   C CB    . LEU A  1 107 ? -21.692 10.773  4.101   1.00 30.47 ? 107 LEU C CB    1 
ATOM   595   C CG    . LEU A  1 107 ? -20.179 10.624  3.999   1.00 30.24 ? 107 LEU C CG    1 
ATOM   596   C CD1   . LEU A  1 107 ? -19.635 9.953   5.240   1.00 39.30 ? 107 LEU C CD1   1 
ATOM   597   C CD2   . LEU A  1 107 ? -19.855 9.773   2.809   1.00 32.98 ? 107 LEU C CD2   1 
ATOM   598   N N     . PHE A  1 108 ? -20.501 13.040  6.171   1.00 34.27 ? 108 PHE C N     1 
ATOM   599   C CA    . PHE A  1 108 ? -19.727 14.265  6.359   1.00 37.81 ? 108 PHE C CA    1 
ATOM   600   C C     . PHE A  1 108 ? -18.268 13.966  6.032   1.00 37.91 ? 108 PHE C C     1 
ATOM   601   O O     . PHE A  1 108 ? -17.412 13.928  6.926   1.00 38.32 ? 108 PHE C O     1 
ATOM   602   C CB    . PHE A  1 108 ? -19.864 14.800  7.785   1.00 40.31 ? 108 PHE C CB    1 
ATOM   603   C CG    . PHE A  1 108 ? -19.288 16.192  7.987   1.00 35.47 ? 108 PHE C CG    1 
ATOM   604   C CD1   . PHE A  1 108 ? -19.831 17.291  7.338   1.00 30.62 ? 108 PHE C CD1   1 
ATOM   605   C CD2   . PHE A  1 108 ? -18.219 16.396  8.846   1.00 35.74 ? 108 PHE C CD2   1 
ATOM   606   C CE1   . PHE A  1 108 ? -19.313 18.567  7.531   1.00 32.33 ? 108 PHE C CE1   1 
ATOM   607   C CE2   . PHE A  1 108 ? -17.693 17.671  9.049   1.00 35.53 ? 108 PHE C CE2   1 
ATOM   608   C CZ    . PHE A  1 108 ? -18.234 18.756  8.395   1.00 34.80 ? 108 PHE C CZ    1 
ATOM   609   N N     . PRO A  1 109 ? -17.953 13.742  4.758   1.00 34.26 ? 109 PRO C N     1 
ATOM   610   C CA    . PRO A  1 109 ? -16.617 13.265  4.404   1.00 33.31 ? 109 PRO C CA    1 
ATOM   611   C C     . PRO A  1 109 ? -15.661 14.405  4.113   1.00 32.49 ? 109 PRO C C     1 
ATOM   612   O O     . PRO A  1 109 ? -16.004 15.405  3.482   1.00 32.63 ? 109 PRO C O     1 
ATOM   613   C CB    . PRO A  1 109 ? -16.890 12.452  3.137   1.00 35.69 ? 109 PRO C CB    1 
ATOM   614   C CG    . PRO A  1 109 ? -18.037 13.227  2.461   1.00 32.18 ? 109 PRO C CG    1 
ATOM   615   C CD    . PRO A  1 109 ? -18.809 13.916  3.567   1.00 34.77 ? 109 PRO C CD    1 
ATOM   616   N N     . CYS A  1 110 ? -14.431 14.240  4.585   1.00 31.93 ? 110 CYS C N     1 
ATOM   617   C CA    . CYS A  1 110 ? -13.377 15.177  4.218   1.00 36.36 ? 110 CYS C CA    1 
ATOM   618   C C     . CYS A  1 110 ? -13.209 15.262  2.705   1.00 34.73 ? 110 CYS C C     1 
ATOM   619   O O     . CYS A  1 110 ? -13.229 16.349  2.117   1.00 31.99 ? 110 CYS C O     1 
ATOM   620   C CB    . CYS A  1 110 ? -12.059 14.773  4.871   1.00 37.08 ? 110 CYS C CB    1 
ATOM   621   S SG    . CYS A  1 110 ? -10.817 16.043  4.629   1.00 38.55 ? 110 CYS C SG    1 
ATOM   622   N N     . VAL A  1 111 ? -13.012 14.128  2.054   1.00 32.80 ? 111 VAL C N     1 
ATOM   623   C CA    . VAL A  1 111 ? -12.799 14.109  0.615   1.00 31.18 ? 111 VAL C CA    1 
ATOM   624   C C     . VAL A  1 111 ? -13.959 13.366  -0.022  1.00 30.86 ? 111 VAL C C     1 
ATOM   625   O O     . VAL A  1 111 ? -14.221 12.201  0.291   1.00 34.10 ? 111 VAL C O     1 
ATOM   626   C CB    . VAL A  1 111 ? -11.450 13.474  0.243   1.00 32.81 ? 111 VAL C CB    1 
ATOM   627   C CG1   . VAL A  1 111 ? -11.100 13.803  -1.193  1.00 29.95 ? 111 VAL C CG1   1 
ATOM   628   C CG2   . VAL A  1 111 ? -10.352 13.986  1.169   1.00 36.89 ? 111 VAL C CG2   1 
ATOM   629   N N     . SER A  1 112 ? -14.647 14.035  -0.929  1.00 35.44 ? 112 SER C N     1 
ATOM   630   C CA    . SER A  1 112 ? -15.746 13.407  -1.640  1.00 30.15 ? 112 SER C CA    1 
ATOM   631   C C     . SER A  1 112 ? -15.172 12.540  -2.755  1.00 31.37 ? 112 SER C C     1 
ATOM   632   O O     . SER A  1 112 ? -15.265 12.855  -3.942  1.00 38.20 ? 112 SER C O     1 
ATOM   633   C CB    . SER A  1 112 ? -16.679 14.475  -2.183  1.00 28.93 ? 112 SER C CB    1 
ATOM   634   O OG    . SER A  1 112 ? -16.795 15.530  -1.248  1.00 38.73 ? 112 SER C OG    1 
ATOM   635   N N     . THR A  1 113 ? -14.576 11.423  -2.363  1.00 22.80 ? 113 THR C N     1 
ATOM   636   C CA    . THR A  1 113 ? -14.104 10.486  -3.372  1.00 25.07 ? 113 THR C CA    1 
ATOM   637   C C     . THR A  1 113 ? -15.285 9.836   -4.086  1.00 31.04 ? 113 THR C C     1 
ATOM   638   O O     . THR A  1 113 ? -16.452 10.169  -3.874  1.00 36.62 ? 113 THR C O     1 
ATOM   639   C CB    . THR A  1 113 ? -13.258 9.404   -2.752  1.00 23.45 ? 113 THR C CB    1 
ATOM   640   O OG1   . THR A  1 113 ? -14.093 8.639   -1.885  1.00 26.50 ? 113 THR C OG1   1 
ATOM   641   C CG2   . THR A  1 113 ? -12.196 10.008  -1.983  1.00 27.06 ? 113 THR C CG2   1 
ATOM   642   N N     . ARG A  1 114 ? -14.977 8.868   -4.943  1.00 32.77 ? 114 ARG C N     1 
ATOM   643   C CA    . ARG A  1 114 ? -16.010 8.006   -5.500  1.00 29.38 ? 114 ARG C CA    1 
ATOM   644   C C     . ARG A  1 114 ? -16.562 7.072   -4.429  1.00 32.00 ? 114 ARG C C     1 
ATOM   645   O O     . ARG A  1 114 ? -17.777 6.990   -4.231  1.00 27.55 ? 114 ARG C O     1 
ATOM   646   C CB    . ARG A  1 114 ? -15.441 7.209   -6.679  1.00 34.40 ? 114 ARG C CB    1 
ATOM   647   C CG    . ARG A  1 114 ? -16.382 6.157   -7.320  1.00 34.49 ? 114 ARG C CG    1 
ATOM   648   C CD    . ARG A  1 114 ? -15.703 5.394   -8.491  1.00 33.08 ? 114 ARG C CD    1 
ATOM   649   N NE    . ARG A  1 114 ? -16.481 4.270   -9.020  1.00 37.16 ? 114 ARG C NE    1 
ATOM   650   C CZ    . ARG A  1 114 ? -17.271 4.328   -10.090 1.00 36.83 ? 114 ARG C CZ    1 
ATOM   651   N NH1   . ARG A  1 114 ? -17.437 5.450   -10.769 1.00 37.62 ? 114 ARG C NH1   1 
ATOM   652   N NH2   . ARG A  1 114 ? -17.921 3.233   -10.484 1.00 37.66 ? 114 ARG C NH2   1 
ATOM   653   N N     . ALA A  1 115 ? -15.681 6.366   -3.714  1.00 35.66 ? 115 ALA C N     1 
ATOM   654   C CA    . ALA A  1 115 ? -16.169 5.471   -2.672  1.00 29.77 ? 115 ALA C CA    1 
ATOM   655   C C     . ALA A  1 115 ? -17.063 6.217   -1.691  1.00 31.35 ? 115 ALA C C     1 
ATOM   656   O O     . ALA A  1 115 ? -18.058 5.658   -1.215  1.00 32.51 ? 115 ALA C O     1 
ATOM   657   C CB    . ALA A  1 115 ? -14.998 4.794   -1.957  1.00 25.73 ? 115 ALA C CB    1 
ATOM   658   N N     . ALA A  1 116 ? -16.777 7.495   -1.430  1.00 27.83 ? 116 ALA C N     1 
ATOM   659   C CA    . ALA A  1 116 ? -17.673 8.272   -0.582  1.00 26.23 ? 116 ALA C CA    1 
ATOM   660   C C     . ALA A  1 116 ? -19.081 8.274   -1.162  1.00 32.47 ? 116 ALA C C     1 
ATOM   661   O O     . ALA A  1 116 ? -20.030 7.750   -0.563  1.00 33.54 ? 116 ALA C O     1 
ATOM   662   C CB    . ALA A  1 116 ? -17.158 9.699   -0.435  1.00 27.59 ? 116 ALA C CB    1 
ATOM   663   N N     . ALA A  1 117 ? -19.224 8.839   -2.354  1.00 32.75 ? 117 ALA C N     1 
ATOM   664   C CA    . ALA A  1 117 ? -20.535 8.936   -2.972  1.00 31.49 ? 117 ALA C CA    1 
ATOM   665   C C     . ALA A  1 117 ? -21.249 7.578   -2.974  1.00 35.06 ? 117 ALA C C     1 
ATOM   666   O O     . ALA A  1 117 ? -22.436 7.491   -2.641  1.00 38.37 ? 117 ALA C O     1 
ATOM   667   C CB    . ALA A  1 117 ? -20.373 9.505   -4.383  1.00 28.53 ? 117 ALA C CB    1 
ATOM   668   N N     . GLN A  1 118 ? -20.524 6.499   -3.280  1.00 29.21 ? 118 GLN C N     1 
ATOM   669   C CA    . GLN A  1 118 ? -21.135 5.174   -3.307  1.00 31.91 ? 118 GLN C CA    1 
ATOM   670   C C     . GLN A  1 118 ? -21.592 4.729   -1.917  1.00 37.85 ? 118 GLN C C     1 
ATOM   671   O O     . GLN A  1 118 ? -22.504 3.893   -1.795  1.00 37.73 ? 118 GLN C O     1 
ATOM   672   C CB    . GLN A  1 118 ? -20.145 4.161   -3.912  1.00 35.21 ? 118 GLN C CB    1 
ATOM   673   C CG    . GLN A  1 118 ? -19.485 4.662   -5.218  1.00 42.60 ? 118 GLN C CG    1 
ATOM   674   C CD    . GLN A  1 118 ? -18.681 3.606   -6.033  1.00 44.37 ? 118 GLN C CD    1 
ATOM   675   O OE1   . GLN A  1 118 ? -17.613 3.139   -5.608  1.00 41.25 ? 118 GLN C OE1   1 
ATOM   676   N NE2   . GLN A  1 118 ? -19.190 3.260   -7.220  1.00 41.33 ? 118 GLN C NE2   1 
ATOM   677   N N     . LEU A  1 119 ? -20.963 5.249   -0.859  1.00 32.04 ? 119 LEU C N     1 
ATOM   678   C CA    . LEU A  1 119 ? -21.420 4.882   0.472   1.00 35.93 ? 119 LEU C CA    1 
ATOM   679   C C     . LEU A  1 119 ? -22.834 5.392   0.703   1.00 32.91 ? 119 LEU C C     1 
ATOM   680   O O     . LEU A  1 119 ? -23.735 4.617   1.051   1.00 35.07 ? 119 LEU C O     1 
ATOM   681   C CB    . LEU A  1 119 ? -20.454 5.408   1.532   1.00 35.37 ? 119 LEU C CB    1 
ATOM   682   C CG    . LEU A  1 119 ? -20.491 4.726   2.907   1.00 28.98 ? 119 LEU C CG    1 
ATOM   683   C CD1   . LEU A  1 119 ? -20.342 3.231   2.761   1.00 34.67 ? 119 LEU C CD1   1 
ATOM   684   C CD2   . LEU A  1 119 ? -19.377 5.263   3.793   1.00 33.49 ? 119 LEU C CD2   1 
ATOM   685   N N     . THR A  1 120 ? -23.065 6.680   0.437   1.00 27.18 ? 120 THR C N     1 
ATOM   686   C CA    . THR A  1 120 ? -24.373 7.254   0.714   1.00 30.44 ? 120 THR C CA    1 
ATOM   687   C C     . THR A  1 120 ? -25.479 6.419   0.082   1.00 36.31 ? 120 THR C C     1 
ATOM   688   O O     . THR A  1 120 ? -26.533 6.226   0.695   1.00 41.86 ? 120 THR C O     1 
ATOM   689   C CB    . THR A  1 120 ? -24.414 8.716   0.246   1.00 29.21 ? 120 THR C CB    1 
ATOM   690   O OG1   . THR A  1 120 ? -24.443 8.786   -1.181  1.00 33.63 ? 120 THR C OG1   1 
ATOM   691   C CG2   . THR A  1 120 ? -23.187 9.457   0.713   1.00 23.64 ? 120 THR C CG2   1 
ATOM   692   N N     . ARG A  1 121 ? -25.209 5.821   -1.082  1.00 35.91 ? 121 ARG C N     1 
ATOM   693   C CA    . ARG A  1 121 ? -26.230 5.052   -1.782  1.00 34.51 ? 121 ARG C CA    1 
ATOM   694   C C     . ARG A  1 121 ? -26.521 3.738   -1.077  1.00 41.03 ? 121 ARG C C     1 
ATOM   695   O O     . ARG A  1 121 ? -27.681 3.421   -0.801  1.00 48.24 ? 121 ARG C O     1 
ATOM   696   C CB    . ARG A  1 121 ? -25.806 4.792   -3.226  1.00 46.26 ? 121 ARG C CB    1 
ATOM   697   C CG    . ARG A  1 121 ? -26.945 4.296   -4.119  1.00 56.44 ? 121 ARG C CG    1 
ATOM   698   C CD    . ARG A  1 121 ? -26.560 4.322   -5.602  1.00 60.22 ? 121 ARG C CD    1 
ATOM   699   N NE    . ARG A  1 121 ? -27.459 3.526   -6.431  1.00 67.26 ? 121 ARG C NE    1 
ATOM   700   C CZ    . ARG A  1 121 ? -28.716 3.854   -6.714  1.00 68.79 ? 121 ARG C CZ    1 
ATOM   701   N NH1   . ARG A  1 121 ? -29.265 4.967   -6.250  1.00 60.19 ? 121 ARG C NH1   1 
ATOM   702   N NH2   . ARG A  1 121 ? -29.441 3.043   -7.483  1.00 67.84 ? 121 ARG C NH2   1 
ATOM   703   N N     . LYS A  1 122 ? -25.490 2.949   -0.787  1.00 40.79 ? 122 LYS C N     1 
ATOM   704   C CA    . LYS A  1 122 ? -25.755 1.638   -0.203  1.00 39.25 ? 122 LYS C CA    1 
ATOM   705   C C     . LYS A  1 122 ? -26.211 1.712   1.250   1.00 43.92 ? 122 LYS C C     1 
ATOM   706   O O     . LYS A  1 122 ? -26.739 0.723   1.765   1.00 48.69 ? 122 LYS C O     1 
ATOM   707   C CB    . LYS A  1 122 ? -24.519 0.741   -0.330  1.00 44.31 ? 122 LYS C CB    1 
ATOM   708   C CG    . LYS A  1 122 ? -24.286 0.249   -1.776  1.00 55.80 ? 122 LYS C CG    1 
ATOM   709   C CD    . LYS A  1 122 ? -23.300 -0.921  -1.892  1.00 41.25 ? 122 LYS C CD    1 
ATOM   710   C CE    . LYS A  1 122 ? -21.875 -0.451  -1.615  1.00 45.04 ? 122 LYS C CE    1 
ATOM   711   N NZ    . LYS A  1 122 ? -20.837 -1.542  -1.672  1.00 48.03 ? 122 LYS C NZ    1 
ATOM   712   N N     . LEU A  1 123 ? -26.062 2.853   1.912   1.00 42.30 ? 123 LEU C N     1 
ATOM   713   C CA    . LEU A  1 123 ? -26.608 3.040   3.246   1.00 37.22 ? 123 LEU C CA    1 
ATOM   714   C C     . LEU A  1 123 ? -27.955 3.724   3.235   1.00 38.97 ? 123 LEU C C     1 
ATOM   715   O O     . LEU A  1 123 ? -28.541 3.921   4.302   1.00 42.29 ? 123 LEU C O     1 
ATOM   716   C CB    . LEU A  1 123 ? -25.636 3.848   4.097   1.00 37.45 ? 123 LEU C CB    1 
ATOM   717   C CG    . LEU A  1 123 ? -24.414 3.077   4.560   1.00 43.81 ? 123 LEU C CG    1 
ATOM   718   C CD1   . LEU A  1 123 ? -23.896 3.697   5.832   1.00 43.42 ? 123 LEU C CD1   1 
ATOM   719   C CD2   . LEU A  1 123 ? -24.847 1.646   4.808   1.00 48.30 ? 123 LEU C CD2   1 
ATOM   720   N N     . ASN A  1 124 ? -28.447 4.101   2.059   1.00 40.91 ? 124 ASN C N     1 
ATOM   721   C CA    . ASN A  1 124 ? -29.719 4.795   1.901   1.00 40.27 ? 124 ASN C CA    1 
ATOM   722   C C     . ASN A  1 124 ? -29.683 6.163   2.555   1.00 38.79 ? 124 ASN C C     1 
ATOM   723   O O     . ASN A  1 124 ? -30.719 6.776   2.806   1.00 44.71 ? 124 ASN C O     1 
ATOM   724   C CB    . ASN A  1 124 ? -30.877 3.951   2.447   1.00 38.99 ? 124 ASN C CB    1 
ATOM   725   C CG    . ASN A  1 124 ? -32.097 4.011   1.573   1.00 44.76 ? 124 ASN C CG    1 
ATOM   726   O OD1   . ASN A  1 124 ? -32.991 4.846   1.759   1.00 43.76 ? 124 ASN C OD1   1 
ATOM   727   N ND2   . ASN A  1 124 ? -32.109 3.162   0.552   1.00 48.07 ? 124 ASN C ND2   1 
ATOM   728   N N     . VAL A  1 125 ? -28.491 6.651   2.835   1.00 34.66 ? 125 VAL C N     1 
ATOM   729   C CA    . VAL A  1 125 ? -28.323 7.961   3.440   1.00 37.85 ? 125 VAL C CA    1 
ATOM   730   C C     . VAL A  1 125 ? -28.506 9.011   2.351   1.00 36.68 ? 125 VAL C C     1 
ATOM   731   O O     . VAL A  1 125 ? -28.485 8.679   1.162   1.00 39.29 ? 125 VAL C O     1 
ATOM   732   C CB    . VAL A  1 125 ? -26.941 8.039   4.107   1.00 43.04 ? 125 VAL C CB    1 
ATOM   733   C CG1   . VAL A  1 125 ? -26.857 9.218   4.929   1.00 41.10 ? 125 VAL C CG1   1 
ATOM   734   C CG2   . VAL A  1 125 ? -26.722 6.843   5.005   1.00 41.24 ? 125 VAL C CG2   1 
ATOM   735   N N     . ALA A  1 126 ? -28.694 10.274  2.738   1.00 34.37 ? 126 ALA C N     1 
ATOM   736   C CA    . ALA A  1 126 ? -28.843 11.361  1.771   1.00 27.64 ? 126 ALA C CA    1 
ATOM   737   C C     . ALA A  1 126 ? -27.705 11.364  0.763   1.00 32.88 ? 126 ALA C C     1 
ATOM   738   O O     . ALA A  1 126 ? -26.546 11.093  1.102   1.00 32.91 ? 126 ALA C O     1 
ATOM   739   C CB    . ALA A  1 126 ? -28.883 12.716  2.483   1.00 30.72 ? 126 ALA C CB    1 
ATOM   740   N N     . ALA A  1 127 ? -28.051 11.689  -0.483  1.00 33.87 ? 127 ALA C N     1 
ATOM   741   C CA    . ALA A  1 127 ? -27.082 11.688  -1.571  1.00 33.94 ? 127 ALA C CA    1 
ATOM   742   C C     . ALA A  1 127 ? -26.012 12.745  -1.352  1.00 33.40 ? 127 ALA C C     1 
ATOM   743   O O     . ALA A  1 127 ? -26.294 13.868  -0.916  1.00 33.65 ? 127 ALA C O     1 
ATOM   744   C CB    . ALA A  1 127 ? -27.789 11.944  -2.902  1.00 32.29 ? 127 ALA C CB    1 
ATOM   745   N N     . LEU A  1 128 ? -24.775 12.381  -1.657  1.00 30.82 ? 128 LEU C N     1 
ATOM   746   C CA    . LEU A  1 128 ? -23.697 13.354  -1.604  1.00 32.99 ? 128 LEU C CA    1 
ATOM   747   C C     . LEU A  1 128 ? -23.945 14.382  -2.685  1.00 37.36 ? 128 LEU C C     1 
ATOM   748   O O     . LEU A  1 128 ? -24.225 14.012  -3.827  1.00 40.24 ? 128 LEU C O     1 
ATOM   749   C CB    . LEU A  1 128 ? -22.364 12.658  -1.818  1.00 31.51 ? 128 LEU C CB    1 
ATOM   750   C CG    . LEU A  1 128 ? -21.156 13.252  -1.118  1.00 37.75 ? 128 LEU C CG    1 
ATOM   751   C CD1   . LEU A  1 128 ? -20.107 12.158  -0.920  1.00 40.54 ? 128 LEU C CD1   1 
ATOM   752   C CD2   . LEU A  1 128 ? -20.590 14.398  -1.958  1.00 45.06 ? 128 LEU C CD2   1 
ATOM   753   N N     . ASP A  1 129 ? -23.903 15.667  -2.334  1.00 34.84 ? 129 ASP C N     1 
ATOM   754   C CA    . ASP A  1 129 ? -24.105 16.672  -3.374  1.00 37.42 ? 129 ASP C CA    1 
ATOM   755   C C     . ASP A  1 129 ? -22.940 16.637  -4.356  1.00 33.24 ? 129 ASP C C     1 
ATOM   756   O O     . ASP A  1 129 ? -21.782 16.478  -3.963  1.00 35.18 ? 129 ASP C O     1 
ATOM   757   C CB    . ASP A  1 129 ? -24.253 18.073  -2.784  1.00 38.55 ? 129 ASP C CB    1 
ATOM   758   C CG    . ASP A  1 129 ? -25.064 19.004  -3.690  1.00 35.18 ? 129 ASP C CG    1 
ATOM   759   O OD1   . ASP A  1 129 ? -25.596 18.540  -4.718  1.00 39.43 ? 129 ASP C OD1   1 
ATOM   760   O OD2   . ASP A  1 129 ? -25.143 20.214  -3.392  1.00 40.89 ? 129 ASP C OD2   1 
ATOM   761   N N     . GLY A  1 130 ? -23.245 16.777  -5.638  1.00 32.04 ? 130 GLY C N     1 
ATOM   762   C CA    . GLY A  1 130 ? -22.212 16.631  -6.638  1.00 36.32 ? 130 GLY C CA    1 
ATOM   763   C C     . GLY A  1 130 ? -21.905 15.199  -6.992  1.00 39.25 ? 130 GLY C C     1 
ATOM   764   O O     . GLY A  1 130 ? -20.897 14.945  -7.669  1.00 36.67 ? 130 GLY C O     1 
ATOM   765   N N     . TYR A  1 131 ? -22.748 14.262  -6.543  1.00 35.99 ? 131 TYR C N     1 
ATOM   766   C CA    . TYR A  1 131 ? -22.609 12.830  -6.773  1.00 38.42 ? 131 TYR C CA    1 
ATOM   767   C C     . TYR A  1 131 ? -21.838 12.510  -8.053  1.00 38.41 ? 131 TYR C C     1 
ATOM   768   O O     . TYR A  1 131 ? -20.681 12.072  -8.007  1.00 36.77 ? 131 TYR C O     1 
ATOM   769   C CB    . TYR A  1 131 ? -24.002 12.187  -6.810  1.00 35.46 ? 131 TYR C CB    1 
ATOM   770   C CG    . TYR A  1 131 ? -23.947 10.686  -6.795  1.00 38.07 ? 131 TYR C CG    1 
ATOM   771   C CD1   . TYR A  1 131 ? -23.432 10.013  -5.699  1.00 39.89 ? 131 TYR C CD1   1 
ATOM   772   C CD2   . TYR A  1 131 ? -24.384 9.934   -7.874  1.00 40.45 ? 131 TYR C CD2   1 
ATOM   773   C CE1   . TYR A  1 131 ? -23.359 8.632   -5.669  1.00 37.51 ? 131 TYR C CE1   1 
ATOM   774   C CE2   . TYR A  1 131 ? -24.320 8.537   -7.845  1.00 40.99 ? 131 TYR C CE2   1 
ATOM   775   C CZ    . TYR A  1 131 ? -23.798 7.903   -6.736  1.00 37.53 ? 131 TYR C CZ    1 
ATOM   776   O OH    . TYR A  1 131 ? -23.723 6.535   -6.671  1.00 46.73 ? 131 TYR C OH    1 
ATOM   777   N N     . GLU A  1 132 ? -22.462 12.783  -9.197  1.00 38.92 ? 132 GLU C N     1 
ATOM   778   C CA    . GLU A  1 132 ? -21.880 12.398  -10.477 1.00 38.62 ? 132 GLU C CA    1 
ATOM   779   C C     . GLU A  1 132 ? -20.467 12.937  -10.648 1.00 39.02 ? 132 GLU C C     1 
ATOM   780   O O     . GLU A  1 132 ? -19.566 12.212  -11.099 1.00 37.16 ? 132 GLU C O     1 
ATOM   781   C CB    . GLU A  1 132 ? -22.790 12.873  -11.595 1.00 41.36 ? 132 GLU C CB    1 
ATOM   782   C CG    . GLU A  1 132 ? -24.192 12.353  -11.415 1.00 42.78 ? 132 GLU C CG    1 
ATOM   783   C CD    . GLU A  1 132 ? -24.315 10.889  -11.846 1.00 57.72 ? 132 GLU C CD    1 
ATOM   784   O OE1   . GLU A  1 132 ? -25.445 10.338  -11.792 1.00 58.11 ? 132 GLU C OE1   1 
ATOM   785   O OE2   . GLU A  1 132 ? -23.274 10.286  -12.230 1.00 61.68 ? 132 GLU C OE2   1 
ATOM   786   N N     . PHE A  1 133 ? -20.246 14.196  -10.272 1.00 34.22 ? 133 PHE C N     1 
ATOM   787   C CA    . PHE A  1 133 ? -18.891 14.727  -10.283 1.00 32.51 ? 133 PHE C CA    1 
ATOM   788   C C     . PHE A  1 133 ? -17.961 13.830  -9.479  1.00 32.08 ? 133 PHE C C     1 
ATOM   789   O O     . PHE A  1 133 ? -16.897 13.418  -9.956  1.00 30.58 ? 133 PHE C O     1 
ATOM   790   C CB    . PHE A  1 133 ? -18.903 16.138  -9.721  1.00 27.38 ? 133 PHE C CB    1 
ATOM   791   C CG    . PHE A  1 133 ? -17.657 16.869  -9.966  1.00 28.61 ? 133 PHE C CG    1 
ATOM   792   C CD1   . PHE A  1 133 ? -17.216 17.072  -11.266 1.00 32.69 ? 133 PHE C CD1   1 
ATOM   793   C CD2   . PHE A  1 133 ? -16.917 17.361  -8.918  1.00 26.98 ? 133 PHE C CD2   1 
ATOM   794   C CE1   . PHE A  1 133 ? -16.064 17.766  -11.519 1.00 27.39 ? 133 PHE C CE1   1 
ATOM   795   C CE2   . PHE A  1 133 ? -15.740 18.056  -9.154  1.00 28.61 ? 133 PHE C CE2   1 
ATOM   796   C CZ    . PHE A  1 133 ? -15.314 18.263  -10.455 1.00 31.29 ? 133 PHE C CZ    1 
ATOM   797   N N     . ALA A  1 134 ? -18.376 13.488  -8.261  1.00 30.36 ? 134 ALA C N     1 
ATOM   798   C CA    . ALA A  1 134 ? -17.587 12.588  -7.438  1.00 31.80 ? 134 ALA C CA    1 
ATOM   799   C C     . ALA A  1 134 ? -17.434 11.244  -8.119  1.00 36.26 ? 134 ALA C C     1 
ATOM   800   O O     . ALA A  1 134 ? -16.332 10.680  -8.169  1.00 40.01 ? 134 ALA C O     1 
ATOM   801   C CB    . ALA A  1 134 ? -18.239 12.415  -6.066  1.00 37.15 ? 134 ALA C CB    1 
ATOM   802   N N     . MET A  1 135 ? -18.540 10.716  -8.655  1.00 33.19 ? 135 MET C N     1 
ATOM   803   C CA    . MET A  1 135 ? -18.507 9.415   -9.315  1.00 37.91 ? 135 MET C CA    1 
ATOM   804   C C     . MET A  1 135 ? -17.397 9.330   -10.369 1.00 37.38 ? 135 MET C C     1 
ATOM   805   O O     . MET A  1 135 ? -16.908 8.233   -10.676 1.00 30.70 ? 135 MET C O     1 
ATOM   806   C CB    . MET A  1 135 ? -19.857 9.115   -9.969  1.00 33.43 ? 135 MET C CB    1 
ATOM   807   C CG    . MET A  1 135 ? -20.966 8.665   -9.039  1.00 38.04 ? 135 MET C CG    1 
ATOM   808   S SD    . MET A  1 135 ? -20.457 7.493   -7.772  1.00 38.36 ? 135 MET C SD    1 
ATOM   809   C CE    . MET A  1 135 ? -21.212 5.998   -8.402  1.00 35.00 ? 135 MET C CE    1 
ATOM   810   N N     . GLN A  1 136 ? -17.008 10.469  -10.947 1.00 35.12 ? 136 GLN C N     1 
ATOM   811   C CA    . GLN A  1 136 ? -15.932 10.531  -11.920 1.00 31.25 ? 136 GLN C CA    1 
ATOM   812   C C     . GLN A  1 136 ? -14.617 10.985  -11.298 1.00 28.95 ? 136 GLN C C     1 
ATOM   813   O O     . GLN A  1 136 ? -13.756 11.510  -12.005 1.00 32.57 ? 136 GLN C O     1 
ATOM   814   C CB    . GLN A  1 136 ? -16.326 11.463  -13.068 1.00 35.16 ? 136 GLN C CB    1 
ATOM   815   C CG    . GLN A  1 136 ? -17.673 11.147  -13.723 1.00 32.56 ? 136 GLN C CG    1 
ATOM   816   C CD    . GLN A  1 136 ? -17.731 9.736   -14.298 1.00 29.06 ? 136 GLN C CD    1 
ATOM   817   O OE1   . GLN A  1 136 ? -17.008 9.415   -15.226 1.00 31.22 ? 136 GLN C OE1   1 
ATOM   818   N NE2   . GLN A  1 136 ? -18.615 8.908   -13.772 1.00 28.39 ? 136 GLN C NE2   1 
ATOM   819   N N     . ASN A  1 137 ? -14.449 10.801  -9.998  1.00 27.22 ? 137 ASN C N     1 
ATOM   820   C CA    . ASN A  1 137 ? -13.276 11.295  -9.286  1.00 34.30 ? 137 ASN C CA    1 
ATOM   821   C C     . ASN A  1 137 ? -12.928 12.701  -9.743  1.00 31.23 ? 137 ASN C C     1 
ATOM   822   O O     . ASN A  1 137 ? -11.753 13.015  -9.965  1.00 30.80 ? 137 ASN C O     1 
ATOM   823   C CB    . ASN A  1 137 ? -12.082 10.365  -9.479  1.00 31.57 ? 137 ASN C CB    1 
ATOM   824   C CG    . ASN A  1 137 ? -12.364 8.946   -9.005  1.00 35.37 ? 137 ASN C CG    1 
ATOM   825   O OD1   . ASN A  1 137 ? -12.019 7.986   -9.695  1.00 35.72 ? 137 ASN C OD1   1 
ATOM   826   N ND2   . ASN A  1 137 ? -12.987 8.804   -7.827  1.00 27.07 ? 137 ASN C ND2   1 
ATOM   827   N N     . GLY A  1 138 ? -13.941 13.543  -9.926  1.00 27.46 ? 138 GLY C N     1 
ATOM   828   C CA    . GLY A  1 138 ? -13.656 14.929  -10.231 1.00 26.27 ? 138 GLY C CA    1 
ATOM   829   C C     . GLY A  1 138 ? -12.736 15.544  -9.203  1.00 27.32 ? 138 GLY C C     1 
ATOM   830   O O     . GLY A  1 138 ? -11.725 16.157  -9.548  1.00 28.20 ? 138 GLY C O     1 
ATOM   831   N N     . ILE A  1 139 ? -13.056 15.345  -7.920  1.00 27.12 ? 139 ILE C N     1 
ATOM   832   C CA    . ILE A  1 139 ? -12.244 15.782  -6.793  1.00 23.48 ? 139 ILE C CA    1 
ATOM   833   C C     . ILE A  1 139 ? -10.764 15.570  -7.048  1.00 25.43 ? 139 ILE C C     1 
ATOM   834   O O     . ILE A  1 139 ? -9.937  16.407  -6.689  1.00 25.84 ? 139 ILE C O     1 
ATOM   835   C CB    . ILE A  1 139 ? -12.686 15.048  -5.516  1.00 32.14 ? 139 ILE C CB    1 
ATOM   836   C CG1   . ILE A  1 139 ? -13.056 13.578  -5.812  1.00 40.20 ? 139 ILE C CG1   1 
ATOM   837   C CG2   . ILE A  1 139 ? -13.861 15.772  -4.888  1.00 26.62 ? 139 ILE C CG2   1 
ATOM   838   C CD1   . ILE A  1 139 ? -11.871 12.552  -6.043  1.00 31.32 ? 139 ILE C CD1   1 
ATOM   839   N N     . ASP A  1 140 ? -10.425 14.459  -7.690  1.00 26.15 ? 140 ASP C N     1 
ATOM   840   C CA    . ASP A  1 140 ? -9.024  14.167  -7.938  1.00 25.49 ? 140 ASP C CA    1 
ATOM   841   C C     . ASP A  1 140 ? -8.442  15.016  -9.059  1.00 29.64 ? 140 ASP C C     1 
ATOM   842   O O     . ASP A  1 140 ? -7.240  15.301  -9.031  1.00 29.66 ? 140 ASP C O     1 
ATOM   843   C CB    . ASP A  1 140 ? -8.848  12.679  -8.244  1.00 28.01 ? 140 ASP C CB    1 
ATOM   844   C CG    . ASP A  1 140 ? -7.424  12.338  -8.628  1.00 36.35 ? 140 ASP C CG    1 
ATOM   845   O OD1   . ASP A  1 140 ? -6.563  12.307  -7.727  1.00 41.76 ? 140 ASP C OD1   1 
ATOM   846   O OD2   . ASP A  1 140 ? -7.167  12.110  -9.836  1.00 38.19 ? 140 ASP C OD2   1 
ATOM   847   N N     . LEU A  1 141 ? -9.252  15.441  -10.042 1.00 27.41 ? 141 LEU C N     1 
ATOM   848   C CA    . LEU A  1 141 ? -8.742  16.312  -11.115 1.00 25.75 ? 141 LEU C CA    1 
ATOM   849   C C     . LEU A  1 141 ? -8.444  17.708  -10.594 1.00 26.25 ? 141 LEU C C     1 
ATOM   850   O O     . LEU A  1 141 ? -7.347  18.247  -10.788 1.00 26.49 ? 141 LEU C O     1 
ATOM   851   C CB    . LEU A  1 141 ? -9.746  16.404  -12.245 1.00 25.03 ? 141 LEU C CB    1 
ATOM   852   C CG    . LEU A  1 141 ? -9.424  17.597  -13.135 1.00 20.03 ? 141 LEU C CG    1 
ATOM   853   C CD1   . LEU A  1 141 ? -8.159  17.325  -13.941 1.00 25.57 ? 141 LEU C CD1   1 
ATOM   854   C CD2   . LEU A  1 141 ? -10.607 17.930  -14.037 1.00 23.26 ? 141 LEU C CD2   1 
ATOM   855   N N     . LEU A  1 142 ? -9.421  18.310  -9.929  1.00 26.64 ? 142 LEU C N     1 
ATOM   856   C CA    . LEU A  1 142 ? -9.137  19.302  -8.907  1.00 29.63 ? 142 LEU C CA    1 
ATOM   857   C C     . LEU A  1 142 ? -8.085  18.703  -7.975  1.00 32.77 ? 142 LEU C C     1 
ATOM   858   O O     . LEU A  1 142 ? -7.733  17.528  -8.100  1.00 33.78 ? 142 LEU C O     1 
ATOM   859   C CB    . LEU A  1 142 ? -10.430 19.656  -8.180  1.00 24.35 ? 142 LEU C CB    1 
ATOM   860   C CG    . LEU A  1 142 ? -11.513 19.931  -9.232  1.00 22.90 ? 142 LEU C CG    1 
ATOM   861   C CD1   . LEU A  1 142 ? -12.838 20.312  -8.611  1.00 25.62 ? 142 LEU C CD1   1 
ATOM   862   C CD2   . LEU A  1 142 ? -11.019 21.050  -10.153 1.00 23.05 ? 142 LEU C CD2   1 
ATOM   863   N N     . ASN A  1 143 ? -7.537  19.483  -7.061  1.00 34.87 ? 143 ASN C N     1 
ATOM   864   C CA    . ASN A  1 143 ? -6.538  18.936  -6.134  1.00 36.74 ? 143 ASN C CA    1 
ATOM   865   C C     . ASN A  1 143 ? -5.210  18.587  -6.804  1.00 33.50 ? 143 ASN C C     1 
ATOM   866   O O     . ASN A  1 143 ? -4.259  18.226  -6.107  1.00 40.13 ? 143 ASN C O     1 
ATOM   867   C CB    . ASN A  1 143 ? -7.032  17.673  -5.401  1.00 28.91 ? 143 ASN C CB    1 
ATOM   868   C CG    . ASN A  1 143 ? -8.115  17.964  -4.379  1.00 35.90 ? 143 ASN C CG    1 
ATOM   869   O OD1   . ASN A  1 143 ? -8.227  19.085  -3.874  1.00 36.20 ? 143 ASN C OD1   1 
ATOM   870   N ND2   . ASN A  1 143 ? -8.949  16.951  -4.093  1.00 34.55 ? 143 ASN C ND2   1 
ATOM   871   N N     . MET A  1 144 ? -5.110  18.638  -8.130  1.00 29.57 ? 144 MET C N     1 
ATOM   872   C CA    . MET A  1 144 ? -3.802  18.521  -8.751  1.00 28.42 ? 144 MET C CA    1 
ATOM   873   C C     . MET A  1 144 ? -3.245  19.914  -8.921  1.00 26.55 ? 144 MET C C     1 
ATOM   874   O O     . MET A  1 144 ? -3.952  20.814  -9.375  1.00 29.13 ? 144 MET C O     1 
ATOM   875   C CB    . MET A  1 144 ? -3.876  17.802  -10.084 1.00 29.17 ? 144 MET C CB    1 
ATOM   876   C CG    . MET A  1 144 ? -4.655  16.556  -9.962  1.00 27.93 ? 144 MET C CG    1 
ATOM   877   S SD    . MET A  1 144 ? -4.812  15.865  -11.577 1.00 33.51 ? 144 MET C SD    1 
ATOM   878   C CE    . MET A  1 144 ? -3.068  15.856  -12.020 1.00 30.20 ? 144 MET C CE    1 
ATOM   879   N N     . LYS A  1 145 ? -2.002  20.099  -8.490  1.00 28.20 ? 145 LYS C N     1 
ATOM   880   C CA    . LYS A  1 145 ? -1.361  21.395  -8.632  1.00 27.75 ? 145 LYS C CA    1 
ATOM   881   C C     . LYS A  1 145 ? -1.415  21.855  -10.080 1.00 28.12 ? 145 LYS C C     1 
ATOM   882   O O     . LYS A  1 145 ? -1.850  22.978  -10.369 1.00 30.60 ? 145 LYS C O     1 
ATOM   883   C CB    . LYS A  1 145 ? 0.088   21.319  -8.139  1.00 29.54 ? 145 LYS C CB    1 
ATOM   884   C CG    . LYS A  1 145 ? 0.226   21.157  -6.625  1.00 34.83 ? 145 LYS C CG    1 
ATOM   885   C CD    . LYS A  1 145 ? 0.595   22.461  -5.951  1.00 29.79 ? 145 LYS C CD    1 
ATOM   886   C CE    . LYS A  1 145 ? 0.051   22.505  -4.546  1.00 38.39 ? 145 LYS C CE    1 
ATOM   887   N NZ    . LYS A  1 145 ? 0.062   21.154  -3.900  1.00 42.75 ? 145 LYS C NZ    1 
ATOM   888   N N     . SER A  1 146 ? -1.007  20.975  -11.008 1.00 28.68 ? 146 SER C N     1 
ATOM   889   C CA    . SER A  1 146 ? -1.001  21.316  -12.433 1.00 32.96 ? 146 SER C CA    1 
ATOM   890   C C     . SER A  1 146 ? -2.352  21.850  -12.885 1.00 30.07 ? 146 SER C C     1 
ATOM   891   O O     . SER A  1 146 ? -2.432  22.857  -13.609 1.00 30.53 ? 146 SER C O     1 
ATOM   892   C CB    . SER A  1 146 ? -0.621  20.091  -13.272 1.00 28.17 ? 146 SER C CB    1 
ATOM   893   O OG    . SER A  1 146 ? -1.392  18.961  -12.896 1.00 26.25 ? 146 SER C OG    1 
ATOM   894   N N     . THR A  1 147 ? -3.427  21.183  -12.462 1.00 25.33 ? 147 THR C N     1 
ATOM   895   C CA    . THR A  1 147 ? -4.761  21.667  -12.762 1.00 23.69 ? 147 THR C CA    1 
ATOM   896   C C     . THR A  1 147 ? -4.902  23.121  -12.337 1.00 28.11 ? 147 THR C C     1 
ATOM   897   O O     . THR A  1 147 ? -5.300  23.978  -13.129 1.00 29.37 ? 147 THR C O     1 
ATOM   898   C CB    . THR A  1 147 ? -5.794  20.791  -12.071 1.00 23.94 ? 147 THR C CB    1 
ATOM   899   O OG1   . THR A  1 147 ? -5.673  19.438  -12.532 1.00 23.09 ? 147 THR C OG1   1 
ATOM   900   C CG2   . THR A  1 147 ? -7.181  21.301  -12.381 1.00 28.97 ? 147 THR C CG2   1 
ATOM   901   N N     . PHE A  1 148 ? -4.526  23.431  -11.098 1.00 29.57 ? 148 PHE C N     1 
ATOM   902   C CA    . PHE A  1 148 ? -4.712  24.800  -10.640 1.00 27.39 ? 148 PHE C CA    1 
ATOM   903   C C     . PHE A  1 148 ? -3.953  25.787  -11.508 1.00 29.09 ? 148 PHE C C     1 
ATOM   904   O O     . PHE A  1 148 ? -4.484  26.849  -11.856 1.00 33.50 ? 148 PHE C O     1 
ATOM   905   C CB    . PHE A  1 148 ? -4.279  24.997  -9.199  1.00 23.73 ? 148 PHE C CB    1 
ATOM   906   C CG    . PHE A  1 148 ? -4.450  26.418  -8.762  1.00 28.31 ? 148 PHE C CG    1 
ATOM   907   C CD1   . PHE A  1 148 ? -5.714  26.907  -8.470  1.00 28.37 ? 148 PHE C CD1   1 
ATOM   908   C CD2   . PHE A  1 148 ? -3.378  27.291  -8.732  1.00 29.14 ? 148 PHE C CD2   1 
ATOM   909   C CE1   . PHE A  1 148 ? -5.911  28.218  -8.102  1.00 28.99 ? 148 PHE C CE1   1 
ATOM   910   C CE2   . PHE A  1 148 ? -3.564  28.609  -8.365  1.00 34.10 ? 148 PHE C CE2   1 
ATOM   911   C CZ    . PHE A  1 148 ? -4.840  29.074  -8.044  1.00 35.23 ? 148 PHE C CZ    1 
ATOM   912   N N     . ARG A  1 149 ? -2.703  25.482  -11.841 1.00 29.52 ? 149 ARG C N     1 
ATOM   913   C CA    . ARG A  1 149 ? -1.969  26.409  -12.694 1.00 29.96 ? 149 ARG C CA    1 
ATOM   914   C C     . ARG A  1 149 ? -2.684  26.579  -14.010 1.00 26.96 ? 149 ARG C C     1 
ATOM   915   O O     . ARG A  1 149 ? -2.755  27.682  -14.555 1.00 28.61 ? 149 ARG C O     1 
ATOM   916   C CB    . ARG A  1 149 ? -0.543  25.924  -12.909 1.00 29.05 ? 149 ARG C CB    1 
ATOM   917   C CG    . ARG A  1 149 ? 0.339   26.313  -11.752 1.00 30.76 ? 149 ARG C CG    1 
ATOM   918   C CD    . ARG A  1 149 ? 1.782   26.444  -12.151 1.00 29.07 ? 149 ARG C CD    1 
ATOM   919   N NE    . ARG A  1 149 ? 2.065   27.569  -13.034 1.00 27.00 ? 149 ARG C NE    1 
ATOM   920   C CZ    . ARG A  1 149 ? 2.379   28.783  -12.604 1.00 31.20 ? 149 ARG C CZ    1 
ATOM   921   N NH1   . ARG A  1 149 ? 2.361   29.089  -11.311 1.00 32.66 ? 149 ARG C NH1   1 
ATOM   922   N NH2   . ARG A  1 149 ? 2.744   29.707  -13.487 1.00 31.20 ? 149 ARG C NH2   1 
ATOM   923   N N     . ARG A  1 150 ? -3.267  25.506  -14.511 1.00 28.78 ? 150 ARG C N     1 
ATOM   924   C CA    . ARG A  1 150 ? -3.925  25.595  -15.802 1.00 26.00 ? 150 ARG C CA    1 
ATOM   925   C C     . ARG A  1 150 ? -5.160  26.493  -15.714 1.00 29.59 ? 150 ARG C C     1 
ATOM   926   O O     . ARG A  1 150 ? -5.223  27.545  -16.362 1.00 29.67 ? 150 ARG C O     1 
ATOM   927   C CB    . ARG A  1 150 ? -4.220  24.170  -16.286 1.00 31.08 ? 150 ARG C CB    1 
ATOM   928   C CG    . ARG A  1 150 ? -2.908  23.451  -16.764 1.00 33.73 ? 150 ARG C CG    1 
ATOM   929   C CD    . ARG A  1 150 ? -2.819  21.930  -16.505 1.00 31.71 ? 150 ARG C CD    1 
ATOM   930   N NE    . ARG A  1 150 ? -2.149  21.240  -17.612 1.00 32.68 ? 150 ARG C NE    1 
ATOM   931   C CZ    . ARG A  1 150 ? -2.095  19.919  -17.807 1.00 33.47 ? 150 ARG C CZ    1 
ATOM   932   N NH1   . ARG A  1 150 ? -2.727  19.061  -17.022 1.00 24.95 ? 150 ARG C NH1   1 
ATOM   933   N NH2   . ARG A  1 150 ? -1.377  19.444  -18.822 1.00 29.89 ? 150 ARG C NH2   1 
ATOM   934   N N     . LEU A  1 151 ? -6.116  26.143  -14.844 1.00 33.18 ? 151 LEU C N     1 
ATOM   935   C CA    . LEU A  1 151 ? -7.376  26.885  -14.765 1.00 29.29 ? 151 LEU C CA    1 
ATOM   936   C C     . LEU A  1 151 ? -7.160  28.355  -14.439 1.00 28.04 ? 151 LEU C C     1 
ATOM   937   O O     . LEU A  1 151 ? -7.818  29.229  -15.015 1.00 25.73 ? 151 LEU C O     1 
ATOM   938   C CB    . LEU A  1 151 ? -8.262  26.276  -13.701 1.00 24.75 ? 151 LEU C CB    1 
ATOM   939   C CG    . LEU A  1 151 ? -8.554  24.828  -13.968 1.00 25.08 ? 151 LEU C CG    1 
ATOM   940   C CD1   . LEU A  1 151 ? -9.648  24.465  -13.022 1.00 24.19 ? 151 LEU C CD1   1 
ATOM   941   C CD2   . LEU A  1 151 ? -9.008  24.675  -15.383 1.00 25.94 ? 151 LEU C CD2   1 
ATOM   942   N N     . ALA A  1 152 ? -6.281  28.646  -13.483 1.00 24.57 ? 152 ALA C N     1 
ATOM   943   C CA    . ALA A  1 152 ? -6.075  30.038  -13.101 1.00 27.91 ? 152 ALA C CA    1 
ATOM   944   C C     . ALA A  1 152 ? -5.473  30.821  -14.248 1.00 32.43 ? 152 ALA C C     1 
ATOM   945   O O     . ALA A  1 152 ? -5.902  31.942  -14.546 1.00 30.68 ? 152 ALA C O     1 
ATOM   946   C CB    . ALA A  1 152 ? -5.165  30.126  -11.880 1.00 28.07 ? 152 ALA C CB    1 
ATOM   947   N N     . ALA A  1 153 ? -4.466  30.240  -14.897 1.00 27.59 ? 153 ALA C N     1 
ATOM   948   C CA    . ALA A  1 153 ? -3.848  30.885  -16.034 1.00 25.27 ? 153 ALA C CA    1 
ATOM   949   C C     . ALA A  1 153 ? -4.848  31.101  -17.161 1.00 32.41 ? 153 ALA C C     1 
ATOM   950   O O     . ALA A  1 153 ? -4.664  32.016  -17.969 1.00 36.10 ? 153 ALA C O     1 
ATOM   951   C CB    . ALA A  1 153 ? -2.663  30.045  -16.506 1.00 26.58 ? 153 ALA C CB    1 
ATOM   952   N N     . GLY A  1 154 ? -5.902  30.289  -17.231 1.00 30.26 ? 154 GLY C N     1 
ATOM   953   C CA    . GLY A  1 154 ? -6.906  30.477  -18.253 1.00 29.49 ? 154 GLY C CA    1 
ATOM   954   C C     . GLY A  1 154 ? -7.930  31.489  -17.796 1.00 38.84 ? 154 GLY C C     1 
ATOM   955   O O     . GLY A  1 154 ? -8.445  32.293  -18.585 1.00 38.37 ? 154 GLY C O     1 
ATOM   956   N N     . LEU A  1 155 ? -8.214  31.451  -16.493 1.00 37.78 ? 155 LEU C N     1 
ATOM   957   C CA    . LEU A  1 155 ? -9.205  32.332  -15.897 1.00 30.24 ? 155 LEU C CA    1 
ATOM   958   C C     . LEU A  1 155 ? -8.670  33.744  -15.735 1.00 32.10 ? 155 LEU C C     1 
ATOM   959   O O     . LEU A  1 155 ? -9.411  34.716  -15.895 1.00 39.65 ? 155 LEU C O     1 
ATOM   960   C CB    . LEU A  1 155 ? -9.620  31.771  -14.545 1.00 34.57 ? 155 LEU C CB    1 
ATOM   961   C CG    . LEU A  1 155 ? -10.605 32.593  -13.736 1.00 36.79 ? 155 LEU C CG    1 
ATOM   962   C CD1   . LEU A  1 155 ? -11.713 33.139  -14.605 1.00 29.82 ? 155 LEU C CD1   1 
ATOM   963   C CD2   . LEU A  1 155 ? -11.167 31.693  -12.667 1.00 36.40 ? 155 LEU C CD2   1 
ATOM   964   N N     . GLY A  1 156 ? -7.394  33.878  -15.421 1.00 31.58 ? 156 GLY C N     1 
ATOM   965   C CA    . GLY A  1 156 ? -6.811  35.161  -15.109 1.00 30.87 ? 156 GLY C CA    1 
ATOM   966   C C     . GLY A  1 156 ? -6.302  35.254  -13.696 1.00 32.01 ? 156 GLY C C     1 
ATOM   967   O O     . GLY A  1 156 ? -5.609  36.227  -13.364 1.00 33.62 ? 156 GLY C O     1 
ATOM   968   N N     . THR A  1 157 ? -6.595  34.270  -12.853 1.00 33.80 ? 157 THR C N     1 
ATOM   969   C CA    . THR A  1 157 ? -6.190  34.331  -11.456 1.00 31.40 ? 157 THR C CA    1 
ATOM   970   C C     . THR A  1 157 ? -4.686  34.560  -11.340 1.00 30.56 ? 157 THR C C     1 
ATOM   971   O O     . THR A  1 157 ? -3.896  33.817  -11.945 1.00 33.30 ? 157 THR C O     1 
ATOM   972   C CB    . THR A  1 157 ? -6.583  33.051  -10.725 1.00 30.04 ? 157 THR C CB    1 
ATOM   973   O OG1   . THR A  1 157 ? -7.928  32.706  -11.081 1.00 30.29 ? 157 THR C OG1   1 
ATOM   974   C CG2   . THR A  1 157 ? -6.453  33.224  -9.204  1.00 30.20 ? 157 THR C CG2   1 
ATOM   975   N N     . PRO A  1 158 ? -4.260  35.563  -10.590 1.00 27.33 ? 158 PRO C N     1 
ATOM   976   C CA    . PRO A  1 158 ? -2.828  35.840  -10.450 1.00 32.11 ? 158 PRO C CA    1 
ATOM   977   C C     . PRO A  1 158 ? -2.057  34.587  -10.066 1.00 35.38 ? 158 PRO C C     1 
ATOM   978   O O     . PRO A  1 158 ? -2.373  33.921  -9.072  1.00 33.97 ? 158 PRO C O     1 
ATOM   979   C CB    . PRO A  1 158 ? -2.767  36.895  -9.337  1.00 32.35 ? 158 PRO C CB    1 
ATOM   980   C CG    . PRO A  1 158 ? -4.175  37.323  -9.069  1.00 33.37 ? 158 PRO C CG    1 
ATOM   981   C CD    . PRO A  1 158 ? -5.123  36.404  -9.745  1.00 29.71 ? 158 PRO C CD    1 
ATOM   982   N N     . LEU A  1 159 ? -1.048  34.266  -10.877 1.00 36.88 ? 159 LEU C N     1 
ATOM   983   C CA    . LEU A  1 159 ? -0.125  33.164  -10.655 1.00 29.78 ? 159 LEU C CA    1 
ATOM   984   C C     . LEU A  1 159 ? 1.291   33.692  -10.571 1.00 33.53 ? 159 LEU C C     1 
ATOM   985   O O     . LEU A  1 159 ? 1.612   34.738  -11.131 1.00 36.34 ? 159 LEU C O     1 
ATOM   986   C CB    . LEU A  1 159 ? -0.159  32.160  -11.792 1.00 28.21 ? 159 LEU C CB    1 
ATOM   987   C CG    . LEU A  1 159 ? -1.308  31.195  -11.853 1.00 32.60 ? 159 LEU C CG    1 
ATOM   988   C CD1   . LEU A  1 159 ? -1.087  30.295  -13.055 1.00 26.45 ? 159 LEU C CD1   1 
ATOM   989   C CD2   . LEU A  1 159 ? -1.316  30.414  -10.554 1.00 28.47 ? 159 LEU C CD2   1 
ATOM   990   N N     . THR A  1 160 ? 2.144   32.940  -9.892  1.00 36.91 ? 160 THR C N     1 
ATOM   991   C CA    . THR A  1 160 ? 3.581   33.134  -10.001 1.00 28.49 ? 160 THR C CA    1 
ATOM   992   C C     . THR A  1 160 ? 4.086   32.493  -11.276 1.00 27.39 ? 160 THR C C     1 
ATOM   993   O O     . THR A  1 160 ? 3.581   31.448  -11.687 1.00 33.66 ? 160 THR C O     1 
ATOM   994   C CB    . THR A  1 160 ? 4.293   32.491  -8.819  1.00 33.59 ? 160 THR C CB    1 
ATOM   995   O OG1   . THR A  1 160 ? 4.156   31.065  -8.920  1.00 35.48 ? 160 THR C OG1   1 
ATOM   996   C CG2   . THR A  1 160 ? 3.686   32.971  -7.515  1.00 39.22 ? 160 THR C CG2   1 
ATOM   997   N N     . ASP A  1 161 ? 5.096   33.116  -11.895 1.00 29.71 ? 161 ASP C N     1 
ATOM   998   C CA    . ASP A  1 161 ? 5.733   32.522  -13.064 1.00 30.87 ? 161 ASP C CA    1 
ATOM   999   C C     . ASP A  1 161 ? 6.043   31.066  -12.786 1.00 30.98 ? 161 ASP C C     1 
ATOM   1000  O O     . ASP A  1 161 ? 6.424   30.703  -11.674 1.00 32.96 ? 161 ASP C O     1 
ATOM   1001  C CB    . ASP A  1 161 ? 7.020   33.253  -13.420 1.00 40.15 ? 161 ASP C CB    1 
ATOM   1002  C CG    . ASP A  1 161 ? 6.792   34.394  -14.388 1.00 54.95 ? 161 ASP C CG    1 
ATOM   1003  O OD1   . ASP A  1 161 ? 5.846   35.191  -14.157 1.00 48.83 ? 161 ASP C OD1   1 
ATOM   1004  O OD2   . ASP A  1 161 ? 7.550   34.476  -15.393 1.00 62.68 ? 161 ASP C OD2   1 
ATOM   1005  N N     . GLY A  1 162 ? 5.825   30.220  -13.777 1.00 31.23 ? 162 GLY C N     1 
ATOM   1006  C CA    . GLY A  1 162 ? 5.985   28.804  -13.525 1.00 27.47 ? 162 GLY C CA    1 
ATOM   1007  C C     . GLY A  1 162 ? 5.564   27.994  -14.722 1.00 30.25 ? 162 GLY C C     1 
ATOM   1008  O O     . GLY A  1 162 ? 5.169   28.535  -15.762 1.00 35.37 ? 162 GLY C O     1 
ATOM   1009  N N     . VAL A  1 163 ? 5.642   26.673  -14.559 1.00 28.09 ? 163 VAL C N     1 
ATOM   1010  C CA    . VAL A  1 163 ? 5.516   25.747  -15.682 1.00 28.54 ? 163 VAL C CA    1 
ATOM   1011  C C     . VAL A  1 163 ? 4.928   24.421  -15.196 1.00 34.57 ? 163 VAL C C     1 
ATOM   1012  O O     . VAL A  1 163 ? 5.316   23.892  -14.144 1.00 31.67 ? 163 VAL C O     1 
ATOM   1013  C CB    . VAL A  1 163 ? 6.892   25.522  -16.348 1.00 29.46 ? 163 VAL C CB    1 
ATOM   1014  C CG1   . VAL A  1 163 ? 6.921   24.189  -17.091 1.00 31.42 ? 163 VAL C CG1   1 
ATOM   1015  C CG2   . VAL A  1 163 ? 7.258   26.689  -17.270 1.00 26.96 ? 163 VAL C CG2   1 
ATOM   1016  N N     . VAL A  1 164 ? 4.014   23.856  -15.983 1.00 27.32 ? 164 VAL C N     1 
ATOM   1017  C CA    . VAL A  1 164 ? 3.674   22.448  -15.800 1.00 24.57 ? 164 VAL C CA    1 
ATOM   1018  C C     . VAL A  1 164 ? 4.739   21.633  -16.535 1.00 30.75 ? 164 VAL C C     1 
ATOM   1019  O O     . VAL A  1 164 ? 4.673   21.443  -17.751 1.00 23.93 ? 164 VAL C O     1 
ATOM   1020  C CB    . VAL A  1 164 ? 2.266   22.123  -16.295 1.00 27.03 ? 164 VAL C CB    1 
ATOM   1021  C CG1   . VAL A  1 164 ? 1.935   20.697  -15.951 1.00 25.89 ? 164 VAL C CG1   1 
ATOM   1022  C CG2   . VAL A  1 164 ? 1.241   23.062  -15.676 1.00 26.36 ? 164 VAL C CG2   1 
ATOM   1023  N N     . ALA A  1 165 ? 5.734   21.151  -15.784 1.00 35.27 ? 165 ALA C N     1 
ATOM   1024  C CA    . ALA A  1 165 ? 6.899   20.466  -16.340 1.00 34.91 ? 165 ALA C CA    1 
ATOM   1025  C C     . ALA A  1 165 ? 6.570   19.018  -16.673 1.00 29.64 ? 165 ALA C C     1 
ATOM   1026  O O     . ALA A  1 165 ? 6.248   18.228  -15.786 1.00 32.26 ? 165 ALA C O     1 
ATOM   1027  C CB    . ALA A  1 165 ? 8.067   20.514  -15.359 1.00 30.83 ? 165 ALA C CB    1 
ATOM   1028  N N     . ARG A  1 166 ? 6.698   18.664  -17.942 1.00 32.27 ? 166 ARG C N     1 
ATOM   1029  C CA    . ARG A  1 166 ? 6.399   17.316  -18.392 1.00 29.60 ? 166 ARG C CA    1 
ATOM   1030  C C     . ARG A  1 166 ? 7.580   16.363  -18.270 1.00 35.53 ? 166 ARG C C     1 
ATOM   1031  O O     . ARG A  1 166 ? 7.395   15.164  -18.513 1.00 30.48 ? 166 ARG C O     1 
ATOM   1032  C CB    . ARG A  1 166 ? 5.929   17.364  -19.840 1.00 33.08 ? 166 ARG C CB    1 
ATOM   1033  C CG    . ARG A  1 166 ? 4.706   18.216  -20.006 1.00 31.37 ? 166 ARG C CG    1 
ATOM   1034  C CD    . ARG A  1 166 ? 4.636   18.830  -21.358 1.00 28.61 ? 166 ARG C CD    1 
ATOM   1035  N NE    . ARG A  1 166 ? 5.577   19.921  -21.536 1.00 33.80 ? 166 ARG C NE    1 
ATOM   1036  C CZ    . ARG A  1 166 ? 5.685   20.587  -22.674 1.00 30.76 ? 166 ARG C CZ    1 
ATOM   1037  N NH1   . ARG A  1 166 ? 4.950   20.270  -23.720 1.00 36.63 ? 166 ARG C NH1   1 
ATOM   1038  N NH2   . ARG A  1 166 ? 6.541   21.598  -22.765 1.00 27.19 ? 166 ARG C NH2   1 
ATOM   1039  N N     . GLY A  1 167 ? 8.777   16.856  -17.893 1.00 37.08 ? 167 GLY C N     1 
ATOM   1040  C CA    . GLY A  1 167 ? 9.964   16.027  -17.780 1.00 32.06 ? 167 GLY C CA    1 
ATOM   1041  C C     . GLY A  1 167 ? 11.172  16.768  -17.229 1.00 35.94 ? 167 GLY C C     1 
ATOM   1042  O O     . GLY A  1 167 ? 11.163  18.002  -17.118 1.00 36.78 ? 167 GLY C O     1 
ATOM   1043  N N     . PRO A  1 168 ? 12.252  16.030  -16.907 1.00 31.61 ? 168 PRO C N     1 
ATOM   1044  C CA    . PRO A  1 168 ? 13.371  16.655  -16.165 1.00 32.12 ? 168 PRO C CA    1 
ATOM   1045  C C     . PRO A  1 168 ? 14.123  17.726  -16.950 1.00 33.58 ? 168 PRO C C     1 
ATOM   1046  O O     . PRO A  1 168 ? 14.533  18.744  -16.364 1.00 34.60 ? 168 PRO C O     1 
ATOM   1047  C CB    . PRO A  1 168 ? 14.270  15.457  -15.812 1.00 34.41 ? 168 PRO C CB    1 
ATOM   1048  C CG    . PRO A  1 168 ? 13.955  14.418  -16.861 1.00 31.30 ? 168 PRO C CG    1 
ATOM   1049  C CD    . PRO A  1 168 ? 12.490  14.597  -17.176 1.00 25.90 ? 168 PRO C CD    1 
ATOM   1050  N N     . ALA A  1 169 ? 14.330  17.533  -18.255 1.00 29.70 ? 169 ALA C N     1 
ATOM   1051  C CA    . ALA A  1 169 ? 14.901  18.610  -19.053 1.00 29.23 ? 169 ALA C CA    1 
ATOM   1052  C C     . ALA A  1 169 ? 14.060  19.863  -18.924 1.00 34.83 ? 169 ALA C C     1 
ATOM   1053  O O     . ALA A  1 169 ? 14.594  20.968  -18.760 1.00 35.69 ? 169 ALA C O     1 
ATOM   1054  C CB    . ALA A  1 169 ? 15.006  18.205  -20.518 1.00 33.16 ? 169 ALA C CB    1 
ATOM   1055  N N     . GLU A  1 170 ? 12.735  19.710  -18.987 1.00 38.01 ? 170 GLU C N     1 
ATOM   1056  C CA    . GLU A  1 170 ? 11.868  20.845  -18.709 1.00 36.12 ? 170 GLU C CA    1 
ATOM   1057  C C     . GLU A  1 170 ? 12.195  21.413  -17.338 1.00 35.39 ? 170 GLU C C     1 
ATOM   1058  O O     . GLU A  1 170 ? 12.411  22.624  -17.199 1.00 37.06 ? 170 GLU C O     1 
ATOM   1059  C CB    . GLU A  1 170 ? 10.392  20.442  -18.825 1.00 38.91 ? 170 GLU C CB    1 
ATOM   1060  C CG    . GLU A  1 170 ? 9.481   21.567  -19.355 1.00 39.66 ? 170 GLU C CG    1 
ATOM   1061  C CD    . GLU A  1 170 ? 8.266   21.098  -20.173 1.00 37.58 ? 170 GLU C CD    1 
ATOM   1062  O OE1   . GLU A  1 170 ? 7.630   20.060  -19.852 1.00 36.81 ? 170 GLU C OE1   1 
ATOM   1063  O OE2   . GLU A  1 170 ? 7.921   21.811  -21.136 1.00 38.20 ? 170 GLU C OE2   1 
ATOM   1064  N N     . VAL A  1 171 ? 12.339  20.536  -16.331 1.00 32.05 ? 171 VAL C N     1 
ATOM   1065  C CA    . VAL A  1 171 ? 12.672  20.993  -14.981 1.00 32.04 ? 171 VAL C CA    1 
ATOM   1066  C C     . VAL A  1 171 ? 13.954  21.815  -15.003 1.00 34.07 ? 171 VAL C C     1 
ATOM   1067  O O     . VAL A  1 171 ? 14.047  22.873  -14.364 1.00 28.37 ? 171 VAL C O     1 
ATOM   1068  C CB    . VAL A  1 171 ? 12.767  19.796  -14.018 1.00 29.46 ? 171 VAL C CB    1 
ATOM   1069  C CG1   . VAL A  1 171 ? 13.303  20.228  -12.679 1.00 28.05 ? 171 VAL C CG1   1 
ATOM   1070  C CG2   . VAL A  1 171 ? 11.400  19.166  -13.849 1.00 26.34 ? 171 VAL C CG2   1 
ATOM   1071  N N     . ARG A  1 172 ? 14.932  21.378  -15.802 1.00 34.87 ? 172 ARG C N     1 
ATOM   1072  C CA    . ARG A  1 172 ? 16.211  22.079  -15.893 1.00 40.50 ? 172 ARG C CA    1 
ATOM   1073  C C     . ARG A  1 172 ? 16.033  23.517  -16.359 1.00 37.70 ? 172 ARG C C     1 
ATOM   1074  O O     . ARG A  1 172 ? 16.508  24.455  -15.709 1.00 35.23 ? 172 ARG C O     1 
ATOM   1075  C CB    . ARG A  1 172 ? 17.156  21.339  -16.847 1.00 37.84 ? 172 ARG C CB    1 
ATOM   1076  C CG    . ARG A  1 172 ? 18.613  21.677  -16.618 1.00 39.67 ? 172 ARG C CG    1 
ATOM   1077  C CD    . ARG A  1 172 ? 19.495  21.277  -17.785 1.00 44.55 ? 172 ARG C CD    1 
ATOM   1078  N NE    . ARG A  1 172 ? 20.618  22.202  -17.911 1.00 55.91 ? 172 ARG C NE    1 
ATOM   1079  C CZ    . ARG A  1 172 ? 20.524  23.419  -18.436 1.00 58.24 ? 172 ARG C CZ    1 
ATOM   1080  N NH1   . ARG A  1 172 ? 19.369  23.894  -18.886 1.00 49.66 ? 172 ARG C NH1   1 
ATOM   1081  N NH2   . ARG A  1 172 ? 21.616  24.175  -18.526 1.00 56.96 ? 172 ARG C NH2   1 
ATOM   1082  N N     . SER A  1 173 ? 15.381  23.705  -17.509 1.00 33.97 ? 173 SER C N     1 
ATOM   1083  C CA    . SER A  1 173 ? 15.253  25.043  -18.077 1.00 35.36 ? 173 SER C CA    1 
ATOM   1084  C C     . SER A  1 173 ? 14.347  25.924  -17.237 1.00 38.47 ? 173 SER C C     1 
ATOM   1085  O O     . SER A  1 173 ? 14.479  27.156  -17.256 1.00 39.49 ? 173 SER C O     1 
ATOM   1086  C CB    . SER A  1 173 ? 14.702  24.948  -19.489 1.00 37.39 ? 173 SER C CB    1 
ATOM   1087  O OG    . SER A  1 173 ? 13.543  24.136  -19.488 1.00 34.28 ? 173 SER C OG    1 
ATOM   1088  N N     . ALA A  1 174 ? 13.408  25.306  -16.518 1.00 39.06 ? 174 ALA C N     1 
ATOM   1089  C CA    . ALA A  1 174 ? 12.543  26.054  -15.612 1.00 42.43 ? 174 ALA C CA    1 
ATOM   1090  C C     . ALA A  1 174 ? 13.341  26.620  -14.445 1.00 36.57 ? 174 ALA C C     1 
ATOM   1091  O O     . ALA A  1 174 ? 13.281  27.824  -14.162 1.00 31.39 ? 174 ALA C O     1 
ATOM   1092  C CB    . ALA A  1 174 ? 11.413  25.158  -15.103 1.00 34.46 ? 174 ALA C CB    1 
ATOM   1093  N N     . ILE A  1 175 ? 14.095  25.764  -13.752 1.00 35.21 ? 175 ILE C N     1 
ATOM   1094  C CA    . ILE A  1 175 ? 14.923  26.256  -12.659 1.00 33.84 ? 175 ILE C CA    1 
ATOM   1095  C C     . ILE A  1 175 ? 15.851  27.337  -13.171 1.00 40.25 ? 175 ILE C C     1 
ATOM   1096  O O     . ILE A  1 175 ? 16.087  28.346  -12.497 1.00 40.34 ? 175 ILE C O     1 
ATOM   1097  C CB    . ILE A  1 175 ? 15.715  25.110  -12.015 1.00 33.23 ? 175 ILE C CB    1 
ATOM   1098  C CG1   . ILE A  1 175 ? 14.786  24.028  -11.481 1.00 30.38 ? 175 ILE C CG1   1 
ATOM   1099  C CG2   . ILE A  1 175 ? 16.591  25.648  -10.913 1.00 33.68 ? 175 ILE C CG2   1 
ATOM   1100  C CD1   . ILE A  1 175 ? 15.534  22.796  -11.087 1.00 27.46 ? 175 ILE C CD1   1 
ATOM   1101  N N     . GLN A  1 176 ? 16.366  27.151  -14.393 1.00 45.03 ? 176 GLN C N     1 
ATOM   1102  C CA    . GLN A  1 176 ? 17.297  28.109  -14.981 1.00 41.21 ? 176 GLN C CA    1 
ATOM   1103  C C     . GLN A  1 176 ? 16.607  29.433  -15.274 1.00 36.20 ? 176 GLN C C     1 
ATOM   1104  O O     . GLN A  1 176 ? 17.189  30.502  -15.060 1.00 36.30 ? 176 GLN C O     1 
ATOM   1105  C CB    . GLN A  1 176 ? 17.913  27.513  -16.253 1.00 44.32 ? 176 GLN C CB    1 
ATOM   1106  C CG    . GLN A  1 176 ? 18.894  28.414  -17.019 1.00 45.02 ? 176 GLN C CG    1 
ATOM   1107  C CD    . GLN A  1 176 ? 18.815  28.191  -18.535 1.00 52.98 ? 176 GLN C CD    1 
ATOM   1108  O OE1   . GLN A  1 176 ? 17.826  27.636  -19.038 1.00 50.15 ? 176 GLN C OE1   1 
ATOM   1109  N NE2   . GLN A  1 176 ? 19.844  28.637  -19.265 1.00 43.88 ? 176 GLN C NE2   1 
ATOM   1110  N N     . GLU A  1 177 ? 15.372  29.396  -15.760 1.00 36.10 ? 177 GLU C N     1 
ATOM   1111  C CA    . GLU A  1 177 ? 14.725  30.671  -16.007 1.00 38.18 ? 177 GLU C CA    1 
ATOM   1112  C C     . GLU A  1 177 ? 14.054  31.242  -14.772 1.00 42.06 ? 177 GLU C C     1 
ATOM   1113  O O     . GLU A  1 177 ? 14.035  32.468  -14.598 1.00 46.06 ? 177 GLU C O     1 
ATOM   1114  C CB    . GLU A  1 177 ? 13.695  30.575  -17.124 1.00 34.51 ? 177 GLU C CB    1 
ATOM   1115  C CG    . GLU A  1 177 ? 13.222  31.959  -17.475 1.00 44.96 ? 177 GLU C CG    1 
ATOM   1116  C CD    . GLU A  1 177 ? 12.182  31.998  -18.555 1.00 60.59 ? 177 GLU C CD    1 
ATOM   1117  O OE1   . GLU A  1 177 ? 11.439  31.007  -18.709 1.00 66.72 ? 177 GLU C OE1   1 
ATOM   1118  O OE2   . GLU A  1 177 ? 12.112  33.034  -19.252 1.00 65.56 ? 177 GLU C OE2   1 
ATOM   1119  N N     . LEU A  1 178 ? 13.517  30.396  -13.900 1.00 39.92 ? 178 LEU C N     1 
ATOM   1120  C CA    . LEU A  1 178 ? 12.683  30.891  -12.816 1.00 38.42 ? 178 LEU C CA    1 
ATOM   1121  C C     . LEU A  1 178 ? 13.476  31.252  -11.556 1.00 41.94 ? 178 LEU C C     1 
ATOM   1122  O O     . LEU A  1 178 ? 12.896  31.832  -10.631 1.00 47.51 ? 178 LEU C O     1 
ATOM   1123  C CB    . LEU A  1 178 ? 11.572  29.859  -12.496 1.00 39.66 ? 178 LEU C CB    1 
ATOM   1124  C CG    . LEU A  1 178 ? 10.632  29.311  -13.612 1.00 37.02 ? 178 LEU C CG    1 
ATOM   1125  C CD1   . LEU A  1 178 ? 9.812   28.088  -13.132 1.00 30.72 ? 178 LEU C CD1   1 
ATOM   1126  C CD2   . LEU A  1 178 ? 9.693   30.382  -14.162 1.00 35.27 ? 178 LEU C CD2   1 
ATOM   1127  N N     . ILE A  1 179 ? 14.783  30.963  -11.496 1.00 40.47 ? 179 ILE C N     1 
ATOM   1128  C CA    . ILE A  1 179 ? 15.554  31.208  -10.270 1.00 38.78 ? 179 ILE C CA    1 
ATOM   1129  C C     . ILE A  1 179 ? 15.903  32.683  -10.050 1.00 40.27 ? 179 ILE C C     1 
ATOM   1130  O O     . ILE A  1 179 ? 16.168  33.075  -8.911  1.00 45.30 ? 179 ILE C O     1 
ATOM   1131  C CB    . ILE A  1 179 ? 16.839  30.346  -10.283 1.00 36.51 ? 179 ILE C CB    1 
ATOM   1132  C CG1   . ILE A  1 179 ? 17.620  30.404  -8.961  1.00 29.65 ? 179 ILE C CG1   1 
ATOM   1133  C CG2   . ILE A  1 179 ? 17.760  30.767  -11.421 1.00 37.59 ? 179 ILE C CG2   1 
ATOM   1134  C CD1   . ILE A  1 179 ? 16.873  29.930  -7.764  1.00 39.09 ? 179 ILE C CD1   1 
ATOM   1135  N N     . ALA A  1 180 ? 15.881  33.525  -11.088 1.00 37.27 ? 180 ALA C N     1 
ATOM   1136  C CA    . ALA A  1 180 ? 16.567  34.818  -11.013 1.00 41.54 ? 180 ALA C CA    1 
ATOM   1137  C C     . ALA A  1 180 ? 15.835  35.823  -10.126 1.00 45.43 ? 180 ALA C C     1 
ATOM   1138  O O     . ALA A  1 180 ? 16.456  36.458  -9.259  1.00 41.53 ? 180 ALA C O     1 
ATOM   1139  C CB    . ALA A  1 180 ? 16.757  35.402  -12.416 1.00 47.81 ? 180 ALA C CB    1 
ATOM   1140  N N     . GLU A  1 181 ? 14.522  36.005  -10.347 1.00 43.87 ? 181 GLU C N     1 
ATOM   1141  C CA    . GLU A  1 181 ? 13.798  37.139  -9.756  1.00 39.53 ? 181 GLU C CA    1 
ATOM   1142  C C     . GLU A  1 181 ? 14.029  37.262  -8.250  1.00 40.14 ? 181 GLU C C     1 
ATOM   1143  O O     . GLU A  1 181 ? 14.260  38.363  -7.738  1.00 46.81 ? 181 GLU C O     1 
ATOM   1144  C CB    . GLU A  1 181 ? 12.297  37.044  -10.056 1.00 41.63 ? 181 GLU C CB    1 
ATOM   1145  C CG    . GLU A  1 181 ? 11.480  38.165  -9.419  1.00 40.35 ? 181 GLU C CG    1 
ATOM   1146  C CD    . GLU A  1 181 ? 10.062  38.248  -9.959  1.00 51.69 ? 181 GLU C CD    1 
ATOM   1147  O OE1   . GLU A  1 181 ? 9.756   37.528  -10.934 1.00 50.88 ? 181 GLU C OE1   1 
ATOM   1148  O OE2   . GLU A  1 181 ? 9.252   39.047  -9.423  1.00 57.01 ? 181 GLU C OE2   1 
ATOM   1149  N N     . THR A  1 182 ? 13.952  36.151  -7.514  1.00 38.08 ? 182 THR C N     1 
ATOM   1150  C CA    . THR A  1 182 ? 14.136  36.192  -6.068  1.00 35.26 ? 182 THR C CA    1 
ATOM   1151  C C     . THR A  1 182 ? 15.245  35.294  -5.579  1.00 39.77 ? 182 THR C C     1 
ATOM   1152  O O     . THR A  1 182 ? 15.544  35.312  -4.380  1.00 49.41 ? 182 THR C O     1 
ATOM   1153  C CB    . THR A  1 182 ? 12.851  35.796  -5.329  1.00 34.39 ? 182 THR C CB    1 
ATOM   1154  O OG1   . THR A  1 182 ? 12.723  34.361  -5.326  1.00 39.71 ? 182 THR C OG1   1 
ATOM   1155  C CG2   . THR A  1 182 ? 11.628  36.420  -5.987  1.00 33.03 ? 182 THR C CG2   1 
ATOM   1156  N N     . GLY A  1 183 ? 15.847  34.497  -6.452  1.00 37.42 ? 183 GLY C N     1 
ATOM   1157  C CA    . GLY A  1 183 ? 16.818  33.535  -6.019  1.00 36.01 ? 183 GLY C CA    1 
ATOM   1158  C C     . GLY A  1 183 ? 16.231  32.302  -5.384  1.00 40.34 ? 183 GLY C C     1 
ATOM   1159  O O     . GLY A  1 183 ? 16.994  31.450  -4.906  1.00 45.64 ? 183 GLY C O     1 
ATOM   1160  N N     . MET A  1 184 ? 14.907  32.181  -5.346  1.00 38.04 ? 184 MET C N     1 
ATOM   1161  C CA    . MET A  1 184 ? 14.249  31.024  -4.753  1.00 37.89 ? 184 MET C CA    1 
ATOM   1162  C C     . MET A  1 184 ? 13.249  30.466  -5.746  1.00 35.47 ? 184 MET C C     1 
ATOM   1163  O O     . MET A  1 184 ? 12.363  31.193  -6.205  1.00 38.11 ? 184 MET C O     1 
ATOM   1164  C CB    . MET A  1 184 ? 13.558  31.403  -3.450  1.00 36.45 ? 184 MET C CB    1 
ATOM   1165  C CG    . MET A  1 184 ? 14.412  32.303  -2.595  1.00 37.15 ? 184 MET C CG    1 
ATOM   1166  S SD    . MET A  1 184 ? 13.576  32.913  -1.135  1.00 46.58 ? 184 MET C SD    1 
ATOM   1167  C CE    . MET A  1 184 ? 14.988  33.200  -0.047  1.00 47.65 ? 184 MET C CE    1 
ATOM   1168  N N     . VAL A  1 185 ? 13.401  29.191  -6.083  1.00 30.21 ? 185 VAL C N     1 
ATOM   1169  C CA    . VAL A  1 185 ? 12.419  28.447  -6.865  1.00 32.17 ? 185 VAL C CA    1 
ATOM   1170  C C     . VAL A  1 185 ? 11.812  27.374  -5.972  1.00 30.60 ? 185 VAL C C     1 
ATOM   1171  O O     . VAL A  1 185 ? 12.477  26.835  -5.081  1.00 27.96 ? 185 VAL C O     1 
ATOM   1172  C CB    . VAL A  1 185 ? 13.057  27.827  -8.132  1.00 35.40 ? 185 VAL C CB    1 
ATOM   1173  C CG1   . VAL A  1 185 ? 12.337  26.550  -8.570  1.00 31.29 ? 185 VAL C CG1   1 
ATOM   1174  C CG2   . VAL A  1 185 ? 13.065  28.825  -9.267  1.00 32.95 ? 185 VAL C CG2   1 
ATOM   1175  N N     . ILE A  1 186 ? 10.543  27.061  -6.199  1.00 32.88 ? 186 ILE C N     1 
ATOM   1176  C CA    . ILE A  1 186 ? 9.912   25.962  -5.481  1.00 36.96 ? 186 ILE C CA    1 
ATOM   1177  C C     . ILE A  1 186 ? 9.448   24.917  -6.481  1.00 29.77 ? 186 ILE C C     1 
ATOM   1178  O O     . ILE A  1 186 ? 9.100   25.233  -7.618  1.00 25.90 ? 186 ILE C O     1 
ATOM   1179  C CB    . ILE A  1 186 ? 8.744   26.450  -4.605  1.00 35.89 ? 186 ILE C CB    1 
ATOM   1180  C CG1   . ILE A  1 186 ? 8.332   25.356  -3.595  1.00 32.22 ? 186 ILE C CG1   1 
ATOM   1181  C CG2   . ILE A  1 186 ? 7.628   26.952  -5.494  1.00 31.80 ? 186 ILE C CG2   1 
ATOM   1182  C CD1   . ILE A  1 186 ? 7.413   25.847  -2.474  1.00 23.91 ? 186 ILE C CD1   1 
ATOM   1183  N N     . ALA A  1 187 ? 9.457   23.660  -6.047  1.00 36.20 ? 187 ALA C N     1 
ATOM   1184  C CA    . ALA A  1 187 ? 9.164   22.523  -6.912  1.00 31.53 ? 187 ALA C CA    1 
ATOM   1185  C C     . ALA A  1 187 ? 8.246   21.570  -6.169  1.00 31.83 ? 187 ALA C C     1 
ATOM   1186  O O     . ALA A  1 187 ? 8.571   21.143  -5.060  1.00 34.76 ? 187 ALA C O     1 
ATOM   1187  C CB    . ALA A  1 187 ? 10.451  21.800  -7.310  1.00 26.07 ? 187 ALA C CB    1 
ATOM   1188  N N     . LYS A  1 188 ? 7.121   21.215  -6.769  1.00 28.14 ? 188 LYS C N     1 
ATOM   1189  C CA    . LYS A  1 188 ? 6.110   20.481  -6.022  1.00 36.56 ? 188 LYS C CA    1 
ATOM   1190  C C     . LYS A  1 188 ? 5.602   19.244  -6.762  1.00 41.52 ? 188 LYS C C     1 
ATOM   1191  O O     . LYS A  1 188 ? 5.460   19.237  -7.993  1.00 34.24 ? 188 LYS C O     1 
ATOM   1192  C CB    . LYS A  1 188 ? 4.916   21.392  -5.687  1.00 36.13 ? 188 LYS C CB    1 
ATOM   1193  C CG    . LYS A  1 188 ? 5.257   22.852  -5.400  1.00 32.60 ? 188 LYS C CG    1 
ATOM   1194  C CD    . LYS A  1 188 ? 4.023   23.610  -4.905  1.00 29.01 ? 188 LYS C CD    1 
ATOM   1195  C CE    . LYS A  1 188 ? 4.165   25.115  -5.073  1.00 32.98 ? 188 LYS C CE    1 
ATOM   1196  N NZ    . LYS A  1 188 ? 2.852   25.831  -5.074  1.00 35.39 ? 188 LYS C NZ    1 
ATOM   1197  N N     . GLN A  1 189 ? 5.316   18.207  -5.975  1.00 43.90 ? 189 GLN C N     1 
ATOM   1198  C CA    . GLN A  1 189 ? 4.533   17.059  -6.415  1.00 39.22 ? 189 GLN C CA    1 
ATOM   1199  C C     . GLN A  1 189 ? 3.153   17.511  -6.889  1.00 42.57 ? 189 GLN C C     1 
ATOM   1200  O O     . GLN A  1 189 ? 2.510   18.338  -6.232  1.00 43.30 ? 189 GLN C O     1 
ATOM   1201  C CB    . GLN A  1 189 ? 4.387   16.113  -5.226  1.00 39.09 ? 189 GLN C CB    1 
ATOM   1202  C CG    . GLN A  1 189 ? 4.506   14.646  -5.492  1.00 42.34 ? 189 GLN C CG    1 
ATOM   1203  C CD    . GLN A  1 189 ? 4.670   13.895  -4.194  1.00 47.90 ? 189 GLN C CD    1 
ATOM   1204  O OE1   . GLN A  1 189 ? 4.541   14.482  -3.116  1.00 46.13 ? 189 GLN C OE1   1 
ATOM   1205  N NE2   . GLN A  1 189 ? 4.934   12.591  -4.279  1.00 48.83 ? 189 GLN C NE2   1 
ATOM   1206  N N     . ASP A  1 190 ? 2.678   16.941  -8.011  1.00 41.44 ? 190 ASP C N     1 
ATOM   1207  C CA    . ASP A  1 190 ? 1.399   17.374  -8.598  1.00 38.32 ? 190 ASP C CA    1 
ATOM   1208  C C     . ASP A  1 190 ? 0.217   17.127  -7.662  1.00 35.93 ? 190 ASP C C     1 
ATOM   1209  O O     . ASP A  1 190 ? -0.665  17.982  -7.532  1.00 30.26 ? 190 ASP C O     1 
ATOM   1210  C CB    . ASP A  1 190 ? 1.139   16.679  -9.940  1.00 35.44 ? 190 ASP C CB    1 
ATOM   1211  C CG    . ASP A  1 190 ? 0.140   17.446  -10.824 1.00 32.12 ? 190 ASP C CG    1 
ATOM   1212  O OD1   . ASP A  1 190 ? -0.388  18.496  -10.389 1.00 30.50 ? 190 ASP C OD1   1 
ATOM   1213  O OD2   . ASP A  1 190 ? -0.096  17.008  -11.977 1.00 33.04 ? 190 ASP C OD2   1 
ATOM   1214  N N     . ARG A  1 191 ? 0.154   15.952  -7.037  1.00 35.48 ? 191 ARG C N     1 
ATOM   1215  C CA    . ARG A  1 191 ? -0.933  15.601  -6.118  1.00 42.13 ? 191 ARG C CA    1 
ATOM   1216  C C     . ARG A  1 191 ? -0.340  15.305  -4.743  1.00 39.64 ? 191 ARG C C     1 
ATOM   1217  O O     . ARG A  1 191 ? 0.103   14.181  -4.485  1.00 42.91 ? 191 ARG C O     1 
ATOM   1218  C CB    . ARG A  1 191 ? -1.731  14.405  -6.643  1.00 32.15 ? 191 ARG C CB    1 
ATOM   1219  C CG    . ARG A  1 191 ? -2.555  14.737  -7.886  1.00 42.20 ? 191 ARG C CG    1 
ATOM   1220  C CD    . ARG A  1 191 ? -3.851  13.910  -8.009  1.00 43.57 ? 191 ARG C CD    1 
ATOM   1221  N NE    . ARG A  1 191 ? -3.605  12.477  -7.939  1.00 38.29 ? 191 ARG C NE    1 
ATOM   1222  C CZ    . ARG A  1 191 ? -3.213  11.728  -8.960  1.00 46.24 ? 191 ARG C CZ    1 
ATOM   1223  N NH1   . ARG A  1 191 ? -3.121  12.221  -10.188 1.00 39.84 ? 191 ARG C NH1   1 
ATOM   1224  N NH2   . ARG A  1 191 ? -2.911  10.447  -8.744  1.00 52.02 ? 191 ARG C NH2   1 
ATOM   1225  N N     . SER A  1 192 ? -0.322  16.307  -3.870  1.00 38.91 ? 192 SER C N     1 
ATOM   1226  C CA    . SER A  1 192 ? 0.212   16.143  -2.519  1.00 41.69 ? 192 SER C CA    1 
ATOM   1227  C C     . SER A  1 192 ? -0.348  17.254  -1.627  1.00 45.57 ? 192 SER C C     1 
ATOM   1228  O O     . SER A  1 192 ? -1.259  17.995  -2.014  1.00 45.54 ? 192 SER C O     1 
ATOM   1229  C CB    . SER A  1 192 ? 1.742   16.134  -2.550  1.00 42.62 ? 192 SER C CB    1 
ATOM   1230  O OG    . SER A  1 192 ? 2.257   15.412  -1.449  1.00 44.44 ? 192 SER C OG    1 
ATOM   1231  N N     . GLY A  1 193 ? 0.194   17.376  -0.422  1.00 49.84 ? 193 GLY C N     1 
ATOM   1232  C CA    . GLY A  1 193 ? -0.338  18.364  0.500   1.00 48.10 ? 193 GLY C CA    1 
ATOM   1233  C C     . GLY A  1 193 ? 0.539   18.521  1.723   1.00 53.68 ? 193 GLY C C     1 
ATOM   1234  O O     . GLY A  1 193 ? 1.553   17.832  1.887   1.00 54.31 ? 193 GLY C O     1 
ATOM   1235  N N     . GLY A  1 194 ? 0.132   19.458  2.582   1.00 48.71 ? 194 GLY C N     1 
ATOM   1236  C CA    . GLY A  1 194 ? 0.834   19.698  3.827   1.00 46.62 ? 194 GLY C CA    1 
ATOM   1237  C C     . GLY A  1 194 ? 2.273   20.127  3.671   1.00 52.33 ? 194 GLY C C     1 
ATOM   1238  O O     . GLY A  1 194 ? 3.038   20.032  4.635   1.00 46.57 ? 194 GLY C O     1 
ATOM   1239  N N     . GLY A  1 195 ? 2.664   20.615  2.489   1.00 47.47 ? 195 GLY C N     1 
ATOM   1240  C CA    . GLY A  1 195 ? 4.049   20.960  2.230   1.00 41.55 ? 195 GLY C CA    1 
ATOM   1241  C C     . GLY A  1 195 ? 4.997   19.790  2.217   1.00 44.69 ? 195 GLY C C     1 
ATOM   1242  O O     . GLY A  1 195 ? 6.194   19.979  2.445   1.00 45.33 ? 195 GLY C O     1 
ATOM   1243  N N     . HIS A  1 196 ? 4.497   18.577  1.973   1.00 45.24 ? 196 HIS C N     1 
ATOM   1244  C CA    . HIS A  1 196 ? 5.338   17.389  1.947   1.00 46.09 ? 196 HIS C CA    1 
ATOM   1245  C C     . HIS A  1 196 ? 5.932   17.103  0.584   1.00 38.57 ? 196 HIS C C     1 
ATOM   1246  O O     . HIS A  1 196 ? 6.874   16.312  0.490   1.00 40.97 ? 196 HIS C O     1 
ATOM   1247  C CB    . HIS A  1 196 ? 4.547   16.154  2.376   1.00 51.36 ? 196 HIS C CB    1 
ATOM   1248  C CG    . HIS A  1 196 ? 3.754   16.351  3.625   1.00 55.98 ? 196 HIS C CG    1 
ATOM   1249  N ND1   . HIS A  1 196 ? 2.418   16.692  3.610   1.00 54.17 ? 196 HIS C ND1   1 
ATOM   1250  C CD2   . HIS A  1 196 ? 4.102   16.243  4.928   1.00 54.58 ? 196 HIS C CD2   1 
ATOM   1251  C CE1   . HIS A  1 196 ? 1.977   16.791  4.851   1.00 52.44 ? 196 HIS C CE1   1 
ATOM   1252  N NE2   . HIS A  1 196 ? 2.980   16.525  5.671   1.00 58.40 ? 196 HIS C NE2   1 
ATOM   1253  N N     . GLY A  1 197 ? 5.386   17.686  -0.474  1.00 42.33 ? 197 GLY C N     1 
ATOM   1254  C CA    . GLY A  1 197 ? 5.862   17.375  -1.802  1.00 36.41 ? 197 GLY C CA    1 
ATOM   1255  C C     . GLY A  1 197 ? 6.660   18.507  -2.397  1.00 31.55 ? 197 GLY C C     1 
ATOM   1256  O O     . GLY A  1 197 ? 7.089   18.421  -3.545  1.00 39.34 ? 197 GLY C O     1 
ATOM   1257  N N     . ASN A  1 198 ? 6.847   19.581  -1.639  1.00 36.55 ? 198 ASN C N     1 
ATOM   1258  C CA    . ASN A  1 198 ? 7.472   20.792  -2.150  1.00 31.70 ? 198 ASN C CA    1 
ATOM   1259  C C     . ASN A  1 198 ? 8.932   20.813  -1.749  1.00 36.33 ? 198 ASN C C     1 
ATOM   1260  O O     . ASN A  1 198 ? 9.266   20.693  -0.564  1.00 40.38 ? 198 ASN C O     1 
ATOM   1261  C CB    . ASN A  1 198 ? 6.774   22.044  -1.636  1.00 30.13 ? 198 ASN C CB    1 
ATOM   1262  C CG    . ASN A  1 198 ? 5.270   21.913  -1.657  1.00 38.03 ? 198 ASN C CG    1 
ATOM   1263  O OD1   . ASN A  1 198 ? 4.698   21.195  -2.492  1.00 41.88 ? 198 ASN C OD1   1 
ATOM   1264  N ND2   . ASN A  1 198 ? 4.612   22.598  -0.729  1.00 39.26 ? 198 ASN C ND2   1 
ATOM   1265  N N     . ILE A  1 199 ? 9.795   20.947  -2.742  1.00 38.77 ? 199 ILE C N     1 
ATOM   1266  C CA    . ILE A  1 199 ? 11.230  20.978  -2.535  1.00 36.58 ? 199 ILE C CA    1 
ATOM   1267  C C     . ILE A  1 199 ? 11.707  22.354  -2.925  1.00 33.84 ? 199 ILE C C     1 
ATOM   1268  O O     . ILE A  1 199 ? 11.362  22.849  -4.004  1.00 44.02 ? 199 ILE C O     1 
ATOM   1269  C CB    . ILE A  1 199 ? 11.952  19.905  -3.362  1.00 36.33 ? 199 ILE C CB    1 
ATOM   1270  C CG1   . ILE A  1 199 ? 11.582  18.510  -2.848  1.00 33.56 ? 199 ILE C CG1   1 
ATOM   1271  C CG2   . ILE A  1 199 ? 13.438  20.155  -3.296  1.00 34.85 ? 199 ILE C CG2   1 
ATOM   1272  C CD1   . ILE A  1 199 ? 12.295  17.390  -3.563  1.00 34.03 ? 199 ILE C CD1   1 
ATOM   1273  N N     . GLY A  1 200 ? 12.478  22.972  -2.053  1.00 36.58 ? 200 GLY C N     1 
ATOM   1274  C CA    . GLY A  1 200 ? 12.992  24.295  -2.316  1.00 39.48 ? 200 GLY C CA    1 
ATOM   1275  C C     . GLY A  1 200 ? 14.331  24.260  -3.027  1.00 44.38 ? 200 GLY C C     1 
ATOM   1276  O O     . GLY A  1 200 ? 15.126  23.333  -2.859  1.00 51.77 ? 200 GLY C O     1 
ATOM   1277  N N     . ILE A  1 201 ? 14.562  25.284  -3.848  1.00 41.19 ? 201 ILE C N     1 
ATOM   1278  C CA    . ILE A  1 201 ? 15.846  25.524  -4.498  1.00 41.35 ? 201 ILE C CA    1 
ATOM   1279  C C     . ILE A  1 201 ? 16.283  26.946  -4.149  1.00 41.45 ? 201 ILE C C     1 
ATOM   1280  O O     . ILE A  1 201 ? 15.518  27.905  -4.317  1.00 40.15 ? 201 ILE C O     1 
ATOM   1281  C CB    . ILE A  1 201 ? 15.765  25.314  -6.023  1.00 39.55 ? 201 ILE C CB    1 
ATOM   1282  C CG1   . ILE A  1 201 ? 15.798  23.822  -6.358  1.00 37.22 ? 201 ILE C CG1   1 
ATOM   1283  C CG2   . ILE A  1 201 ? 16.910  26.026  -6.730  1.00 37.27 ? 201 ILE C CG2   1 
ATOM   1284  C CD1   . ILE A  1 201 ? 14.472  23.125  -6.199  1.00 37.11 ? 201 ILE C CD1   1 
ATOM   1285  N N     . SER A  1 202 ? 17.490  27.077  -3.633  1.00 41.26 ? 202 SER C N     1 
ATOM   1286  C CA    . SER A  1 202 ? 17.936  28.348  -3.104  1.00 44.49 ? 202 SER C CA    1 
ATOM   1287  C C     . SER A  1 202 ? 19.306  28.671  -3.661  1.00 46.21 ? 202 SER C C     1 
ATOM   1288  O O     . SER A  1 202 ? 20.154  27.786  -3.797  1.00 46.47 ? 202 SER C O     1 
ATOM   1289  C CB    . SER A  1 202 ? 18.002  28.323  -1.591  1.00 45.09 ? 202 SER C CB    1 
ATOM   1290  O OG    . SER A  1 202 ? 17.842  29.623  -1.070  1.00 48.48 ? 202 SER C OG    1 
ATOM   1291  N N     . THR A  1 203 ? 19.514  29.938  -3.984  1.00 42.36 ? 203 THR C N     1 
ATOM   1292  C CA    . THR A  1 203 ? 20.851  30.381  -4.320  1.00 45.97 ? 203 THR C CA    1 
ATOM   1293  C C     . THR A  1 203 ? 21.596  30.910  -3.104  1.00 48.43 ? 203 THR C C     1 
ATOM   1294  O O     . THR A  1 203 ? 22.787  31.218  -3.207  1.00 54.27 ? 203 THR C O     1 
ATOM   1295  C CB    . THR A  1 203 ? 20.803  31.450  -5.408  1.00 45.54 ? 203 THR C CB    1 
ATOM   1296  O OG1   . THR A  1 203 ? 19.707  31.178  -6.288  1.00 50.44 ? 203 THR C OG1   1 
ATOM   1297  C CG2   . THR A  1 203 ? 22.074  31.389  -6.217  1.00 51.92 ? 203 THR C CG2   1 
ATOM   1298  N N     . SER A  1 204 ? 20.934  30.990  -1.951  1.00 50.53 ? 204 SER C N     1 
ATOM   1299  C CA    . SER A  1 204 ? 21.567  31.419  -0.726  1.00 50.15 ? 204 SER C CA    1 
ATOM   1300  C C     . SER A  1 204 ? 21.023  30.628  0.456   1.00 51.97 ? 204 SER C C     1 
ATOM   1301  O O     . SER A  1 204 ? 19.795  30.513  0.603   1.00 55.41 ? 204 SER C O     1 
ATOM   1302  C CB    . SER A  1 204 ? 21.337  32.908  -0.493  1.00 49.80 ? 204 SER C CB    1 
ATOM   1303  O OG    . SER A  1 204 ? 21.854  33.273  0.768   1.00 54.69 ? 204 SER C OG    1 
ATOM   1304  N N     . PRO A  1 205 ? 21.880  30.083  1.315   1.00 59.32 ? 205 PRO C N     1 
ATOM   1305  C CA    . PRO A  1 205 ? 21.398  29.657  2.629   1.00 58.51 ? 205 PRO C CA    1 
ATOM   1306  C C     . PRO A  1 205 ? 21.053  30.916  3.395   1.00 60.35 ? 205 PRO C C     1 
ATOM   1307  O O     . PRO A  1 205 ? 21.615  31.975  3.111   1.00 68.62 ? 205 PRO C O     1 
ATOM   1308  C CB    . PRO A  1 205 ? 22.608  28.939  3.231   1.00 59.85 ? 205 PRO C CB    1 
ATOM   1309  C CG    . PRO A  1 205 ? 23.777  29.675  2.636   1.00 58.16 ? 205 PRO C CG    1 
ATOM   1310  C CD    . PRO A  1 205 ? 23.356  30.052  1.236   1.00 62.68 ? 205 PRO C CD    1 
ATOM   1311  N N     . GLU A  1 206 ? 20.126  30.795  4.356   1.00 57.85 ? 206 GLU C N     1 
ATOM   1312  C CA    . GLU A  1 206 ? 19.463  31.915  5.049   1.00 66.57 ? 206 GLU C CA    1 
ATOM   1313  C C     . GLU A  1 206 ? 18.135  32.189  4.340   1.00 65.52 ? 206 GLU C C     1 
ATOM   1314  O O     . GLU A  1 206 ? 17.525  33.255  4.496   1.00 66.66 ? 206 GLU C O     1 
ATOM   1315  C CB    . GLU A  1 206 ? 20.337  33.187  5.106   1.00 66.93 ? 206 GLU C CB    1 
ATOM   1316  C CG    . GLU A  1 206 ? 19.862  34.388  5.921   1.00 72.75 ? 206 GLU C CG    1 
ATOM   1317  C CD    . GLU A  1 206 ? 20.711  35.625  5.629   1.00 72.35 ? 206 GLU C CD    1 
ATOM   1318  O OE1   . GLU A  1 206 ? 21.861  35.460  5.167   1.00 67.38 ? 206 GLU C OE1   1 
ATOM   1319  O OE2   . GLU A  1 206 ? 20.222  36.759  5.824   1.00 75.22 ? 206 GLU C OE2   1 
ATOM   1320  N N     . SER A  1 207 ? 17.685  31.219  3.550   1.00 62.93 ? 207 SER C N     1 
ATOM   1321  C CA    . SER A  1 207 ? 16.378  31.261  2.906   1.00 54.78 ? 207 SER C CA    1 
ATOM   1322  C C     . SER A  1 207 ? 15.354  30.607  3.824   1.00 51.70 ? 207 SER C C     1 
ATOM   1323  O O     . SER A  1 207 ? 15.556  29.470  4.269   1.00 55.40 ? 207 SER C O     1 
ATOM   1324  C CB    . SER A  1 207 ? 16.431  30.532  1.565   1.00 56.85 ? 207 SER C CB    1 
ATOM   1325  O OG    . SER A  1 207 ? 17.043  29.250  1.695   1.00 56.93 ? 207 SER C OG    1 
ATOM   1326  N N     . SER A  1 208 ? 14.269  31.315  4.124   1.00 44.48 ? 208 SER C N     1 
ATOM   1327  C CA    . SER A  1 208 ? 13.177  30.714  4.879   1.00 43.15 ? 208 SER C CA    1 
ATOM   1328  C C     . SER A  1 208 ? 12.154  30.192  3.877   1.00 45.92 ? 208 SER C C     1 
ATOM   1329  O O     . SER A  1 208 ? 11.571  30.973  3.116   1.00 47.90 ? 208 SER C O     1 
ATOM   1330  C CB    . SER A  1 208 ? 12.545  31.707  5.859   1.00 45.24 ? 208 SER C CB    1 
ATOM   1331  O OG    . SER A  1 208 ? 11.799  32.744  5.220   1.00 50.89 ? 208 SER C OG    1 
ATOM   1332  N N     . PHE A  1 209 ? 11.950  28.875  3.863   1.00 40.30 ? 209 PHE C N     1 
ATOM   1333  C CA    . PHE A  1 209 ? 10.991  28.304  2.926   1.00 36.35 ? 209 PHE C CA    1 
ATOM   1334  C C     . PHE A  1 209 ? 9.775   27.693  3.616   1.00 38.85 ? 209 PHE C C     1 
ATOM   1335  O O     . PHE A  1 209 ? 9.668   26.464  3.677   1.00 39.69 ? 209 PHE C O     1 
ATOM   1336  C CB    . PHE A  1 209 ? 11.660  27.237  2.073   1.00 40.06 ? 209 PHE C CB    1 
ATOM   1337  C CG    . PHE A  1 209 ? 12.376  27.772  0.854   1.00 40.64 ? 209 PHE C CG    1 
ATOM   1338  C CD1   . PHE A  1 209 ? 11.709  27.907  -0.353  1.00 37.67 ? 209 PHE C CD1   1 
ATOM   1339  C CD2   . PHE A  1 209 ? 13.725  28.086  0.907   1.00 40.62 ? 209 PHE C CD2   1 
ATOM   1340  C CE1   . PHE A  1 209 ? 12.364  28.369  -1.478  1.00 40.37 ? 209 PHE C CE1   1 
ATOM   1341  C CE2   . PHE A  1 209 ? 14.387  28.548  -0.216  1.00 43.93 ? 209 PHE C CE2   1 
ATOM   1342  C CZ    . PHE A  1 209 ? 13.706  28.695  -1.408  1.00 41.38 ? 209 PHE C CZ    1 
ATOM   1343  N N     . PRO A  1 210 ? 8.843   28.489  4.139   1.00 33.99 ? 210 PRO C N     1 
ATOM   1344  C CA    . PRO A  1 210 ? 7.534   27.940  4.501   1.00 34.98 ? 210 PRO C CA    1 
ATOM   1345  C C     . PRO A  1 210 ? 6.933   27.101  3.384   1.00 37.20 ? 210 PRO C C     1 
ATOM   1346  O O     . PRO A  1 210 ? 7.027   27.438  2.202   1.00 36.69 ? 210 PRO C O     1 
ATOM   1347  C CB    . PRO A  1 210 ? 6.700   29.191  4.772   1.00 32.82 ? 210 PRO C CB    1 
ATOM   1348  C CG    . PRO A  1 210 ? 7.683   30.096  5.383   1.00 41.04 ? 210 PRO C CG    1 
ATOM   1349  C CD    . PRO A  1 210 ? 8.978   29.876  4.597   1.00 33.51 ? 210 PRO C CD    1 
ATOM   1350  N N     . GLY A  1 211 ? 6.324   25.987  3.777   1.00 36.90 ? 211 GLY C N     1 
ATOM   1351  C CA    . GLY A  1 211 ? 5.659   25.129  2.826   1.00 33.85 ? 211 GLY C CA    1 
ATOM   1352  C C     . GLY A  1 211 ? 6.552   24.219  2.016   1.00 36.49 ? 211 GLY C C     1 
ATOM   1353  O O     . GLY A  1 211 ? 6.224   23.920  0.869   1.00 37.80 ? 211 GLY C O     1 
ATOM   1354  N N     . THR A  1 212 ? 7.670   23.756  2.577   1.00 34.71 ? 212 THR C N     1 
ATOM   1355  C CA    . THR A  1 212 ? 8.558   22.819  1.896   1.00 36.15 ? 212 THR C CA    1 
ATOM   1356  C C     . THR A  1 212 ? 9.115   21.820  2.901   1.00 40.66 ? 212 THR C C     1 
ATOM   1357  O O     . THR A  1 212 ? 9.166   22.097  4.101   1.00 46.59 ? 212 THR C O     1 
ATOM   1358  C CB    . THR A  1 212 ? 9.734   23.535  1.230   1.00 36.95 ? 212 THR C CB    1 
ATOM   1359  O OG1   . THR A  1 212 ? 10.600  24.041  2.253   1.00 34.88 ? 212 THR C OG1   1 
ATOM   1360  C CG2   . THR A  1 212 ? 9.268   24.692  0.364   1.00 34.94 ? 212 THR C CG2   1 
ATOM   1361  N N     . ARG A  1 213 ? 9.586   20.666  2.400   1.00 43.33 ? 213 ARG C N     1 
ATOM   1362  C CA    . ARG A  1 213 ? 10.256  19.666  3.244   1.00 40.03 ? 213 ARG C CA    1 
ATOM   1363  C C     . ARG A  1 213 ? 11.773  19.861  3.344   1.00 43.49 ? 213 ARG C C     1 
ATOM   1364  O O     . ARG A  1 213 ? 12.316  19.891  4.453   1.00 49.04 ? 213 ARG C O     1 
ATOM   1365  C CB    . ARG A  1 213 ? 9.977   18.247  2.751   1.00 37.55 ? 213 ARG C CB    1 
ATOM   1366  C CG    . ARG A  1 213 ? 10.946  17.248  3.371   1.00 44.46 ? 213 ARG C CG    1 
ATOM   1367  C CD    . ARG A  1 213 ? 10.322  15.878  3.581   1.00 45.60 ? 213 ARG C CD    1 
ATOM   1368  N NE    . ARG A  1 213 ? 9.671   15.399  2.370   1.00 46.62 ? 213 ARG C NE    1 
ATOM   1369  C CZ    . ARG A  1 213 ? 9.486   14.118  2.082   1.00 46.79 ? 213 ARG C CZ    1 
ATOM   1370  N NH1   . ARG A  1 213 ? 9.892   13.161  2.898   1.00 43.11 ? 213 ARG C NH1   1 
ATOM   1371  N NH2   . ARG A  1 213 ? 8.895   13.789  0.938   1.00 49.81 ? 213 ARG C NH2   1 
ATOM   1372  N N     . GLU A  1 214 ? 12.486  19.953  2.218   1.00 39.77 ? 214 GLU C N     1 
ATOM   1373  C CA    . GLU A  1 214 ? 13.923  20.211  2.251   1.00 42.42 ? 214 GLU C CA    1 
ATOM   1374  C C     . GLU A  1 214 ? 14.279  21.299  1.247   1.00 42.66 ? 214 GLU C C     1 
ATOM   1375  O O     . GLU A  1 214 ? 13.546  21.561  0.291   1.00 42.06 ? 214 GLU C O     1 
ATOM   1376  C CB    . GLU A  1 214 ? 14.743  18.931  1.970   1.00 44.84 ? 214 GLU C CB    1 
ATOM   1377  C CG    . GLU A  1 214 ? 16.284  19.080  2.061   1.00 45.19 ? 214 GLU C CG    1 
ATOM   1378  C CD    . GLU A  1 214 ? 16.762  19.850  3.296   1.00 46.41 ? 214 GLU C CD    1 
ATOM   1379  O OE1   . GLU A  1 214 ? 16.205  19.628  4.394   1.00 54.23 ? 214 GLU C OE1   1 
ATOM   1380  O OE2   . GLU A  1 214 ? 17.703  20.672  3.175   1.00 46.15 ? 214 GLU C OE2   1 
ATOM   1381  N N     . VAL A  1 215 ? 15.416  21.945  1.481   1.00 41.10 ? 215 VAL C N     1 
ATOM   1382  C CA    . VAL A  1 215 ? 15.912  23.000  0.613   1.00 39.17 ? 215 VAL C CA    1 
ATOM   1383  C C     . VAL A  1 215 ? 17.286  22.597  0.110   1.00 40.78 ? 215 VAL C C     1 
ATOM   1384  O O     . VAL A  1 215 ? 18.142  22.155  0.888   1.00 41.72 ? 215 VAL C O     1 
ATOM   1385  C CB    . VAL A  1 215 ? 15.968  24.355  1.341   1.00 46.99 ? 215 VAL C CB    1 
ATOM   1386  C CG1   . VAL A  1 215 ? 17.025  24.317  2.468   1.00 53.98 ? 215 VAL C CG1   1 
ATOM   1387  C CG2   . VAL A  1 215 ? 16.233  25.482  0.348   1.00 38.63 ? 215 VAL C CG2   1 
ATOM   1388  N N     . LEU A  1 216 ? 17.490  22.748  -1.190  1.00 37.62 ? 216 LEU C N     1 
ATOM   1389  C CA    . LEU A  1 216 ? 18.730  22.379  -1.842  1.00 40.59 ? 216 LEU C CA    1 
ATOM   1390  C C     . LEU A  1 216 ? 19.347  23.609  -2.486  1.00 43.45 ? 216 LEU C C     1 
ATOM   1391  O O     . LEU A  1 216 ? 18.651  24.415  -3.106  1.00 44.55 ? 216 LEU C O     1 
ATOM   1392  C CB    . LEU A  1 216 ? 18.494  21.296  -2.895  1.00 35.25 ? 216 LEU C CB    1 
ATOM   1393  C CG    . LEU A  1 216 ? 17.800  20.054  -2.344  1.00 35.74 ? 216 LEU C CG    1 
ATOM   1394  C CD1   . LEU A  1 216 ? 17.363  19.156  -3.478  1.00 35.30 ? 216 LEU C CD1   1 
ATOM   1395  C CD2   . LEU A  1 216 ? 18.698  19.304  -1.374  1.00 32.57 ? 216 LEU C CD2   1 
ATOM   1396  N N     . ALA A  1 217 ? 20.657  23.744  -2.332  1.00 45.93 ? 217 ALA C N     1 
ATOM   1397  C CA    . ALA A  1 217 ? 21.377  24.850  -2.941  1.00 44.82 ? 217 ALA C CA    1 
ATOM   1398  C C     . ALA A  1 217 ? 21.498  24.643  -4.450  1.00 46.66 ? 217 ALA C C     1 
ATOM   1399  O O     . ALA A  1 217 ? 21.831  23.549  -4.927  1.00 46.66 ? 217 ALA C O     1 
ATOM   1400  C CB    . ALA A  1 217 ? 22.756  24.994  -2.296  1.00 38.92 ? 217 ALA C CB    1 
ATOM   1401  N N     . TYR A  1 218 ? 21.199  25.697  -5.201  1.00 45.31 ? 218 TYR C N     1 
ATOM   1402  C CA    . TYR A  1 218 ? 21.332  25.691  -6.651  1.00 41.72 ? 218 TYR C CA    1 
ATOM   1403  C C     . TYR A  1 218 ? 22.758  26.092  -6.991  1.00 39.14 ? 218 TYR C C     1 
ATOM   1404  O O     . TYR A  1 218 ? 23.160  27.238  -6.768  1.00 42.96 ? 218 TYR C O     1 
ATOM   1405  C CB    . TYR A  1 218 ? 20.306  26.645  -7.264  1.00 45.61 ? 218 TYR C CB    1 
ATOM   1406  C CG    . TYR A  1 218 ? 20.540  27.120  -8.687  1.00 36.70 ? 218 TYR C CG    1 
ATOM   1407  C CD1   . TYR A  1 218 ? 21.425  28.159  -8.961  1.00 39.81 ? 218 TYR C CD1   1 
ATOM   1408  C CD2   . TYR A  1 218 ? 19.839  26.565  -9.746  1.00 36.42 ? 218 TYR C CD2   1 
ATOM   1409  C CE1   . TYR A  1 218 ? 21.641  28.610  -10.251 1.00 40.51 ? 218 TYR C CE1   1 
ATOM   1410  C CE2   . TYR A  1 218 ? 20.041  27.019  -11.049 1.00 48.35 ? 218 TYR C CE2   1 
ATOM   1411  C CZ    . TYR A  1 218 ? 20.950  28.046  -11.287 1.00 43.96 ? 218 TYR C CZ    1 
ATOM   1412  O OH    . TYR A  1 218 ? 21.176  28.510  -12.557 1.00 48.66 ? 218 TYR C OH    1 
ATOM   1413  N N     . ALA A  1 219 ? 23.536  25.155  -7.492  1.00 34.85 ? 219 ALA C N     1 
ATOM   1414  C CA    . ALA A  1 219 ? 24.743  25.558  -8.188  1.00 44.15 ? 219 ALA C CA    1 
ATOM   1415  C C     . ALA A  1 219 ? 24.452  25.597  -9.675  1.00 46.76 ? 219 ALA C C     1 
ATOM   1416  O O     . ALA A  1 219 ? 23.487  25.000  -10.165 1.00 48.24 ? 219 ALA C O     1 
ATOM   1417  C CB    . ALA A  1 219 ? 25.919  24.618  -7.903  1.00 46.28 ? 219 ALA C CB    1 
ATOM   1418  N N     . ASN A  1 220 ? 25.290  26.318  -10.404 1.00 48.95 ? 220 ASN C N     1 
ATOM   1419  C CA    . ASN A  1 220 ? 25.158  26.230  -11.844 1.00 50.03 ? 220 ASN C CA    1 
ATOM   1420  C C     . ASN A  1 220 ? 25.677  24.891  -12.355 1.00 51.96 ? 220 ASN C C     1 
ATOM   1421  O O     . ASN A  1 220 ? 24.991  24.207  -13.126 1.00 49.62 ? 220 ASN C O     1 
ATOM   1422  C CB    . ASN A  1 220 ? 25.862  27.392  -12.515 1.00 53.64 ? 220 ASN C CB    1 
ATOM   1423  C CG    . ASN A  1 220 ? 25.398  27.559  -13.921 1.00 54.82 ? 220 ASN C CG    1 
ATOM   1424  O OD1   . ASN A  1 220 ? 25.163  26.568  -14.602 1.00 58.96 ? 220 ASN C OD1   1 
ATOM   1425  N ND2   . ASN A  1 220 ? 25.229  28.799  -14.368 1.00 56.75 ? 220 ASN C ND2   1 
ATOM   1426  N N     . ASP A  1 221 ? 26.866  24.473  -11.890 1.00 52.19 ? 221 ASP C N     1 
ATOM   1427  C CA    . ASP A  1 221 ? 27.524  23.269  -12.399 1.00 50.52 ? 221 ASP C CA    1 
ATOM   1428  C C     . ASP A  1 221 ? 26.872  21.969  -11.938 1.00 46.93 ? 221 ASP C C     1 
ATOM   1429  O O     . ASP A  1 221 ? 27.369  20.899  -12.304 1.00 49.20 ? 221 ASP C O     1 
ATOM   1430  C CB    . ASP A  1 221 ? 29.005  23.270  -12.008 1.00 50.86 ? 221 ASP C CB    1 
ATOM   1431  C CG    . ASP A  1 221 ? 29.226  23.594  -10.543 1.00 52.16 ? 221 ASP C CG    1 
ATOM   1432  O OD1   . ASP A  1 221 ? 28.793  24.668  -10.084 1.00 46.23 ? 221 ASP C OD1   1 
ATOM   1433  O OD2   . ASP A  1 221 ? 29.852  22.775  -9.850  1.00 56.51 ? 221 ASP C OD2   1 
ATOM   1434  N N     . GLN A  1 222 ? 25.792  22.017  -11.150 1.00 48.21 ? 222 GLN C N     1 
ATOM   1435  C CA    . GLN A  1 222 ? 25.002  20.825  -10.845 1.00 49.33 ? 222 GLN C CA    1 
ATOM   1436  C C     . GLN A  1 222 ? 23.504  21.079  -11.028 1.00 38.82 ? 222 GLN C C     1 
ATOM   1437  O O     . GLN A  1 222 ? 22.670  20.457  -10.374 1.00 40.37 ? 222 GLN C O     1 
ATOM   1438  C CB    . GLN A  1 222 ? 25.312  20.282  -9.443  1.00 43.58 ? 222 GLN C CB    1 
ATOM   1439  C CG    . GLN A  1 222 ? 25.240  21.260  -8.300  1.00 44.38 ? 222 GLN C CG    1 
ATOM   1440  C CD    . GLN A  1 222 ? 25.678  20.625  -6.986  1.00 51.76 ? 222 GLN C CD    1 
ATOM   1441  O OE1   . GLN A  1 222 ? 26.177  19.495  -6.974  1.00 50.48 ? 222 GLN C OE1   1 
ATOM   1442  N NE2   . GLN A  1 222 ? 25.485  21.341  -5.870  1.00 47.34 ? 222 GLN C NE2   1 
ATOM   1443  N N     . LEU A  1 223 ? 23.146  21.962  -11.948 1.00 40.11 ? 223 LEU C N     1 
ATOM   1444  C CA    . LEU A  1 223 ? 21.753  22.070  -12.356 1.00 40.48 ? 223 LEU C CA    1 
ATOM   1445  C C     . LEU A  1 223 ? 21.292  20.860  -13.163 1.00 40.56 ? 223 LEU C C     1 
ATOM   1446  O O     . LEU A  1 223 ? 20.084  20.632  -13.298 1.00 36.95 ? 223 LEU C O     1 
ATOM   1447  C CB    . LEU A  1 223 ? 21.581  23.360  -13.150 1.00 48.87 ? 223 LEU C CB    1 
ATOM   1448  C CG    . LEU A  1 223 ? 20.329  23.639  -13.970 1.00 47.99 ? 223 LEU C CG    1 
ATOM   1449  C CD1   . LEU A  1 223 ? 19.150  23.934  -13.053 1.00 39.81 ? 223 LEU C CD1   1 
ATOM   1450  C CD2   . LEU A  1 223 ? 20.611  24.815  -14.909 1.00 49.15 ? 223 LEU C CD2   1 
ATOM   1451  N N     . ASP A  1 224 ? 22.226  20.082  -13.703 1.00 44.06 ? 224 ASP C N     1 
ATOM   1452  C CA    . ASP A  1 224 ? 21.879  18.823  -14.345 1.00 42.23 ? 224 ASP C CA    1 
ATOM   1453  C C     . ASP A  1 224 ? 21.162  17.901  -13.369 1.00 37.94 ? 224 ASP C C     1 
ATOM   1454  O O     . ASP A  1 224 ? 19.987  17.584  -13.557 1.00 33.56 ? 224 ASP C O     1 
ATOM   1455  C CB    . ASP A  1 224 ? 23.128  18.141  -14.902 1.00 43.05 ? 224 ASP C CB    1 
ATOM   1456  C CG    . ASP A  1 224 ? 23.556  18.709  -16.240 1.00 54.14 ? 224 ASP C CG    1 
ATOM   1457  O OD1   . ASP A  1 224 ? 22.853  18.469  -17.247 1.00 60.07 ? 224 ASP C OD1   1 
ATOM   1458  O OD2   . ASP A  1 224 ? 24.590  19.410  -16.282 1.00 56.64 ? 224 ASP C OD2   1 
ATOM   1459  N N     . THR A  1 225 ? 21.853  17.459  -12.320 1.00 39.60 ? 225 THR C N     1 
ATOM   1460  C CA    . THR A  1 225 ? 21.269  16.392  -11.515 1.00 45.60 ? 225 THR C CA    1 
ATOM   1461  C C     . THR A  1 225 ? 20.180  16.920  -10.597 1.00 36.95 ? 225 THR C C     1 
ATOM   1462  O O     . THR A  1 225 ? 19.243  16.182  -10.274 1.00 38.03 ? 225 THR C O     1 
ATOM   1463  C CB    . THR A  1 225 ? 22.340  15.677  -10.693 1.00 48.62 ? 225 THR C CB    1 
ATOM   1464  O OG1   . THR A  1 225 ? 22.427  16.285  -9.396  1.00 43.87 ? 225 THR C OG1   1 
ATOM   1465  C CG2   . THR A  1 225 ? 23.704  15.749  -11.392 1.00 49.00 ? 225 THR C CG2   1 
ATOM   1466  N N     . LEU A  1 226 ? 20.301  18.178  -10.164 1.00 35.20 ? 226 LEU C N     1 
ATOM   1467  C CA    . LEU A  1 226 ? 19.186  18.888  -9.555  1.00 30.24 ? 226 LEU C CA    1 
ATOM   1468  C C     . LEU A  1 226 ? 17.889  18.519  -10.235 1.00 29.50 ? 226 LEU C C     1 
ATOM   1469  O O     . LEU A  1 226 ? 16.979  17.993  -9.599  1.00 33.51 ? 226 LEU C O     1 
ATOM   1470  C CB    . LEU A  1 226 ? 19.404  20.397  -9.654  1.00 30.86 ? 226 LEU C CB    1 
ATOM   1471  C CG    . LEU A  1 226 ? 20.149  21.049  -8.503  1.00 33.26 ? 226 LEU C CG    1 
ATOM   1472  C CD1   . LEU A  1 226 ? 19.804  22.524  -8.412  1.00 32.18 ? 226 LEU C CD1   1 
ATOM   1473  C CD2   . LEU A  1 226 ? 19.789  20.319  -7.228  1.00 34.57 ? 226 LEU C CD2   1 
ATOM   1474  N N     . ALA A  1 227 ? 17.814  18.735  -11.554 1.00 29.78 ? 227 ALA C N     1 
ATOM   1475  C CA    . ALA A  1 227 ? 16.541  18.625  -12.257 1.00 30.06 ? 227 ALA C CA    1 
ATOM   1476  C C     . ALA A  1 227 ? 16.019  17.192  -12.261 1.00 38.23 ? 227 ALA C C     1 
ATOM   1477  O O     . ALA A  1 227 ? 14.808  16.968  -12.088 1.00 39.46 ? 227 ALA C O     1 
ATOM   1478  C CB    . ALA A  1 227 ? 16.674  19.158  -13.683 1.00 32.05 ? 227 ALA C CB    1 
ATOM   1479  N N     . ASP A  1 228 ? 16.909  16.200  -12.439 1.00 37.24 ? 228 ASP C N     1 
ATOM   1480  C CA    . ASP A  1 228 ? 16.453  14.810  -12.428 1.00 37.72 ? 228 ASP C CA    1 
ATOM   1481  C C     . ASP A  1 228 ? 16.276  14.268  -11.012 1.00 35.63 ? 228 ASP C C     1 
ATOM   1482  O O     . ASP A  1 228 ? 15.477  13.346  -10.808 1.00 35.61 ? 228 ASP C O     1 
ATOM   1483  C CB    . ASP A  1 228 ? 17.406  13.924  -13.241 1.00 41.78 ? 228 ASP C CB    1 
ATOM   1484  C CG    . ASP A  1 228 ? 16.678  13.140  -14.367 1.00 53.66 ? 228 ASP C CG    1 
ATOM   1485  O OD1   . ASP A  1 228 ? 15.729  12.367  -14.058 1.00 50.40 ? 228 ASP C OD1   1 
ATOM   1486  O OD2   . ASP A  1 228 ? 17.055  13.293  -15.559 1.00 53.44 ? 228 ASP C OD2   1 
ATOM   1487  N N     . THR A  1 229 ? 16.974  14.841  -10.033 1.00 28.27 ? 229 THR C N     1 
ATOM   1488  C CA    . THR A  1 229 ? 16.672  14.549  -8.639  1.00 31.36 ? 229 THR C CA    1 
ATOM   1489  C C     . THR A  1 229 ? 15.232  14.921  -8.304  1.00 33.69 ? 229 THR C C     1 
ATOM   1490  O O     . THR A  1 229 ? 14.501  14.139  -7.684  1.00 35.99 ? 229 THR C O     1 
ATOM   1491  C CB    . THR A  1 229 ? 17.643  15.304  -7.736  1.00 28.90 ? 229 THR C CB    1 
ATOM   1492  O OG1   . THR A  1 229 ? 18.984  14.952  -8.089  1.00 33.05 ? 229 THR C OG1   1 
ATOM   1493  C CG2   . THR A  1 229 ? 17.406  14.957  -6.290  1.00 27.77 ? 229 THR C CG2   1 
ATOM   1494  N N     . LEU A  1 230 ? 14.812  16.127  -8.693  1.00 36.09 ? 230 LEU C N     1 
ATOM   1495  C CA    . LEU A  1 230 ? 13.446  16.567  -8.436  1.00 30.33 ? 230 LEU C CA    1 
ATOM   1496  C C     . LEU A  1 230 ? 12.463  15.738  -9.231  1.00 33.47 ? 230 LEU C C     1 
ATOM   1497  O O     . LEU A  1 230 ? 11.465  15.244  -8.689  1.00 33.72 ? 230 LEU C O     1 
ATOM   1498  C CB    . LEU A  1 230 ? 13.288  18.039  -8.797  1.00 27.96 ? 230 LEU C CB    1 
ATOM   1499  C CG    . LEU A  1 230 ? 14.260  18.997  -8.114  1.00 32.23 ? 230 LEU C CG    1 
ATOM   1500  C CD1   . LEU A  1 230 ? 14.081  20.396  -8.668  1.00 35.82 ? 230 LEU C CD1   1 
ATOM   1501  C CD2   . LEU A  1 230 ? 14.060  18.996  -6.601  1.00 39.62 ? 230 LEU C CD2   1 
ATOM   1502  N N     . TRP A  1 231 ? 12.733  15.571  -10.522 1.00 29.24 ? 231 TRP C N     1 
ATOM   1503  C CA    . TRP A  1 231 ? 11.828  14.790  -11.339 1.00 33.26 ? 231 TRP C CA    1 
ATOM   1504  C C     . TRP A  1 231 ? 11.583  13.420  -10.728 1.00 33.72 ? 231 TRP C C     1 
ATOM   1505  O O     . TRP A  1 231 ? 10.436  13.002  -10.553 1.00 35.18 ? 231 TRP C O     1 
ATOM   1506  C CB    . TRP A  1 231 ? 12.375  14.643  -12.748 1.00 33.67 ? 231 TRP C CB    1 
ATOM   1507  C CG    . TRP A  1 231 ? 11.541  13.690  -13.541 1.00 32.31 ? 231 TRP C CG    1 
ATOM   1508  C CD1   . TRP A  1 231 ? 11.792  12.367  -13.771 1.00 26.95 ? 231 TRP C CD1   1 
ATOM   1509  C CD2   . TRP A  1 231 ? 10.292  13.976  -14.168 1.00 31.28 ? 231 TRP C CD2   1 
ATOM   1510  N NE1   . TRP A  1 231 ? 10.794  11.826  -14.536 1.00 26.99 ? 231 TRP C NE1   1 
ATOM   1511  C CE2   . TRP A  1 231 ? 9.860   12.794  -14.795 1.00 27.22 ? 231 TRP C CE2   1 
ATOM   1512  C CE3   . TRP A  1 231 ? 9.507   15.127  -14.278 1.00 32.32 ? 231 TRP C CE3   1 
ATOM   1513  C CZ2   . TRP A  1 231 ? 8.681   12.726  -15.514 1.00 24.33 ? 231 TRP C CZ2   1 
ATOM   1514  C CZ3   . TRP A  1 231 ? 8.342   15.056  -14.996 1.00 27.33 ? 231 TRP C CZ3   1 
ATOM   1515  C CH2   . TRP A  1 231 ? 7.939   13.866  -15.604 1.00 26.39 ? 231 TRP C CH2   1 
ATOM   1516  N N     . SER A  1 232 ? 12.657  12.712  -10.388 1.00 32.28 ? 232 SER C N     1 
ATOM   1517  C CA    . SER A  1 232 ? 12.515  11.318  -10.002 1.00 36.44 ? 232 SER C CA    1 
ATOM   1518  C C     . SER A  1 232 ? 11.748  11.177  -8.704  1.00 37.05 ? 232 SER C C     1 
ATOM   1519  O O     . SER A  1 232 ? 11.077  10.167  -8.474  1.00 42.31 ? 232 SER C O     1 
ATOM   1520  C CB    . SER A  1 232 ? 13.885  10.671  -9.859  1.00 36.47 ? 232 SER C CB    1 
ATOM   1521  O OG    . SER A  1 232 ? 13.856  9.795   -8.745  1.00 45.93 ? 232 SER C OG    1 
ATOM   1522  N N     . GLN A  1 233 ? 11.831  12.174  -7.857  1.00 34.87 ? 233 GLN C N     1 
ATOM   1523  C CA    . GLN A  1 233 ? 11.285  12.067  -6.528  1.00 38.45 ? 233 GLN C CA    1 
ATOM   1524  C C     . GLN A  1 233 ? 9.927   12.712  -6.383  1.00 38.52 ? 233 GLN C C     1 
ATOM   1525  O O     . GLN A  1 233 ? 9.282   12.522  -5.350  1.00 37.90 ? 233 GLN C O     1 
ATOM   1526  C CB    . GLN A  1 233 ? 12.238  12.712  -5.547  1.00 37.97 ? 233 GLN C CB    1 
ATOM   1527  C CG    . GLN A  1 233 ? 13.573  12.107  -5.600  1.00 35.38 ? 233 GLN C CG    1 
ATOM   1528  C CD    . GLN A  1 233 ? 14.296  12.389  -4.349  1.00 35.41 ? 233 GLN C CD    1 
ATOM   1529  O OE1   . GLN A  1 233 ? 13.799  13.114  -3.488  1.00 34.53 ? 233 GLN C OE1   1 
ATOM   1530  N NE2   . GLN A  1 233 ? 15.466  11.802  -4.204  1.00 39.76 ? 233 GLN C NE2   1 
ATOM   1531  N N     . LEU A  1 234 ? 9.489   13.493  -7.359  1.00 36.00 ? 234 LEU C N     1 
ATOM   1532  C CA    . LEU A  1 234 ? 8.196   14.152  -7.246  1.00 37.18 ? 234 LEU C CA    1 
ATOM   1533  C C     . LEU A  1 234 ? 7.226   13.645  -8.299  1.00 36.85 ? 234 LEU C C     1 
ATOM   1534  O O     . LEU A  1 234 ? 6.235   14.323  -8.603  1.00 35.55 ? 234 LEU C O     1 
ATOM   1535  C CB    . LEU A  1 234 ? 8.352   15.669  -7.326  1.00 33.72 ? 234 LEU C CB    1 
ATOM   1536  C CG    . LEU A  1 234 ? 9.409   16.231  -6.377  1.00 35.21 ? 234 LEU C CG    1 
ATOM   1537  C CD1   . LEU A  1 234 ? 9.421   17.759  -6.381  1.00 32.50 ? 234 LEU C CD1   1 
ATOM   1538  C CD2   . LEU A  1 234 ? 9.157   15.715  -4.992  1.00 33.29 ? 234 LEU C CD2   1 
ATOM   1539  N N     . THR A  1 235 ? 7.512   12.467  -8.866  1.00 35.96 ? 235 THR C N     1 
ATOM   1540  C CA    . THR A  1 235 ? 6.653   11.789  -9.832  1.00 38.43 ? 235 THR C CA    1 
ATOM   1541  C C     . THR A  1 235 ? 6.595   10.303  -9.502  1.00 36.60 ? 235 THR C C     1 
ATOM   1542  O O     . THR A  1 235 ? 7.408   9.778   -8.731  1.00 41.05 ? 235 THR C O     1 
ATOM   1543  C CB    . THR A  1 235 ? 7.139   11.955  -11.290 1.00 38.32 ? 235 THR C CB    1 
ATOM   1544  O OG1   . THR A  1 235 ? 8.321   11.169  -11.507 1.00 38.37 ? 235 THR C OG1   1 
ATOM   1545  C CG2   . THR A  1 235 ? 7.421   13.408  -11.636 1.00 34.27 ? 235 THR C CG2   1 
ATOM   1546  N N     . ASP A  1 236 ? 5.629   9.628   -10.120 1.00 32.13 ? 236 ASP C N     1 
ATOM   1547  C CA    . ASP A  1 236 ? 5.422   8.186   -10.001 1.00 35.29 ? 236 ASP C CA    1 
ATOM   1548  C C     . ASP A  1 236 ? 4.514   7.764   -11.149 1.00 40.20 ? 236 ASP C C     1 
ATOM   1549  O O     . ASP A  1 236 ? 4.213   8.564   -12.041 1.00 42.54 ? 236 ASP C O     1 
ATOM   1550  C CB    . ASP A  1 236 ? 4.836   7.809   -8.637  1.00 30.43 ? 236 ASP C CB    1 
ATOM   1551  C CG    . ASP A  1 236 ? 3.704   8.728   -8.208  1.00 43.13 ? 236 ASP C CG    1 
ATOM   1552  O OD1   . ASP A  1 236 ? 2.804   8.999   -9.052  1.00 36.68 ? 236 ASP C OD1   1 
ATOM   1553  O OD2   . ASP A  1 236 ? 3.722   9.176   -7.023  1.00 41.61 ? 236 ASP C OD2   1 
ATOM   1554  N N     . THR A  1 237 ? 4.066   6.506   -11.129 1.00 41.72 ? 237 THR C N     1 
ATOM   1555  C CA    . THR A  1 237 ? 3.244   5.999   -12.226 1.00 38.05 ? 237 THR C CA    1 
ATOM   1556  C C     . THR A  1 237 ? 2.121   6.969   -12.556 1.00 38.54 ? 237 THR C C     1 
ATOM   1557  O O     . THR A  1 237 ? 1.970   7.408   -13.702 1.00 45.72 ? 237 THR C O     1 
ATOM   1558  C CB    . THR A  1 237 ? 2.666   4.626   -11.868 1.00 36.06 ? 237 THR C CB    1 
ATOM   1559  O OG1   . THR A  1 237 ? 3.704   3.640   -11.919 1.00 37.72 ? 237 THR C OG1   1 
ATOM   1560  C CG2   . THR A  1 237 ? 1.573   4.238   -12.851 1.00 35.83 ? 237 THR C CG2   1 
ATOM   1561  N N     . GLN A  1 238 ? 1.358   7.351   -11.546 1.00 33.86 ? 238 GLN C N     1 
ATOM   1562  C CA    . GLN A  1 238 ? 0.139   8.112   -11.750 1.00 35.25 ? 238 GLN C CA    1 
ATOM   1563  C C     . GLN A  1 238 ? 0.368   9.612   -11.880 1.00 33.64 ? 238 GLN C C     1 
ATOM   1564  O O     . GLN A  1 238 ? -0.611  10.349  -11.957 1.00 39.50 ? 238 GLN C O     1 
ATOM   1565  C CB    . GLN A  1 238 ? -0.834  7.845   -10.594 1.00 31.25 ? 238 GLN C CB    1 
ATOM   1566  C CG    . GLN A  1 238 ? -1.188  6.377   -10.416 1.00 36.49 ? 238 GLN C CG    1 
ATOM   1567  C CD    . GLN A  1 238 ? -0.115  5.579   -9.653  1.00 45.44 ? 238 GLN C CD    1 
ATOM   1568  O OE1   . GLN A  1 238 ? 0.680   6.141   -8.879  1.00 39.60 ? 238 GLN C OE1   1 
ATOM   1569  N NE2   . GLN A  1 238 ? -0.079  4.262   -9.889  1.00 40.92 ? 238 GLN C NE2   1 
ATOM   1570  N N     . ASN A  1 239 ? 1.607   10.097  -11.909 1.00 35.25 ? 239 ASN C N     1 
ATOM   1571  C CA    . ASN A  1 239 ? 1.855   11.544  -11.908 1.00 37.69 ? 239 ASN C CA    1 
ATOM   1572  C C     . ASN A  1 239 ? 3.043   11.870  -12.805 1.00 36.32 ? 239 ASN C C     1 
ATOM   1573  O O     . ASN A  1 239 ? 4.190   11.704  -12.391 1.00 39.60 ? 239 ASN C O     1 
ATOM   1574  C CB    . ASN A  1 239 ? 2.113   12.051  -10.500 1.00 31.73 ? 239 ASN C CB    1 
ATOM   1575  C CG    . ASN A  1 239 ? 0.903   11.951  -9.636  1.00 40.70 ? 239 ASN C CG    1 
ATOM   1576  O OD1   . ASN A  1 239 ? 0.136   12.897  -9.530  1.00 40.72 ? 239 ASN C OD1   1 
ATOM   1577  N ND2   . ASN A  1 239 ? 0.706   10.789  -9.019  1.00 41.22 ? 239 ASN C ND2   1 
ATOM   1578  N N     . GLN A  1 240 ? 2.782   12.387  -13.995 1.00 32.27 ? 240 GLN C N     1 
ATOM   1579  C CA    . GLN A  1 240 ? 3.872   12.783  -14.869 1.00 30.12 ? 240 GLN C CA    1 
ATOM   1580  C C     . GLN A  1 240 ? 3.949   14.293  -15.031 1.00 34.70 ? 240 GLN C C     1 
ATOM   1581  O O     . GLN A  1 240 ? 4.346   14.791  -16.085 1.00 35.72 ? 240 GLN C O     1 
ATOM   1582  C CB    . GLN A  1 240 ? 3.737   12.093  -16.216 1.00 29.69 ? 240 GLN C CB    1 
ATOM   1583  C CG    . GLN A  1 240 ? 3.968   10.609  -16.100 1.00 37.09 ? 240 GLN C CG    1 
ATOM   1584  C CD    . GLN A  1 240 ? 5.266   10.284  -15.390 1.00 33.63 ? 240 GLN C CD    1 
ATOM   1585  O OE1   . GLN A  1 240 ? 5.258   9.885   -14.237 1.00 36.03 ? 240 GLN C OE1   1 
ATOM   1586  N NE2   . GLN A  1 240 ? 6.390   10.469  -16.075 1.00 32.60 ? 240 GLN C NE2   1 
ATOM   1587  N N     . PHE A  1 241 ? 3.567   15.031  -13.996 1.00 30.72 ? 241 PHE C N     1 
ATOM   1588  C CA    . PHE A  1 241 ? 3.725   16.474  -13.980 1.00 31.66 ? 241 PHE C CA    1 
ATOM   1589  C C     . PHE A  1 241 ? 4.442   16.885  -12.708 1.00 33.93 ? 241 PHE C C     1 
ATOM   1590  O O     . PHE A  1 241 ? 4.176   16.334  -11.630 1.00 34.02 ? 241 PHE C O     1 
ATOM   1591  C CB    . PHE A  1 241 ? 2.369   17.204  -14.047 1.00 32.63 ? 241 PHE C CB    1 
ATOM   1592  C CG    . PHE A  1 241 ? 1.597   16.950  -15.309 1.00 29.71 ? 241 PHE C CG    1 
ATOM   1593  C CD1   . PHE A  1 241 ? 2.199   17.069  -16.546 1.00 28.78 ? 241 PHE C CD1   1 
ATOM   1594  C CD2   . PHE A  1 241 ? 0.253   16.596  -15.258 1.00 31.41 ? 241 PHE C CD2   1 
ATOM   1595  C CE1   . PHE A  1 241 ? 1.465   16.826  -17.730 1.00 30.05 ? 241 PHE C CE1   1 
ATOM   1596  C CE2   . PHE A  1 241 ? -0.480  16.344  -16.434 1.00 31.18 ? 241 PHE C CE2   1 
ATOM   1597  C CZ    . PHE A  1 241 ? 0.122   16.461  -17.666 1.00 23.15 ? 241 PHE C CZ    1 
ATOM   1598  N N     . ILE A  1 242 ? 5.327   17.873  -12.831 1.00 32.30 ? 242 ILE C N     1 
ATOM   1599  C CA    . ILE A  1 242 ? 5.904   18.554  -11.675 1.00 36.94 ? 242 ILE C CA    1 
ATOM   1600  C C     . ILE A  1 242 ? 5.768   20.050  -11.871 1.00 35.38 ? 242 ILE C C     1 
ATOM   1601  O O     . ILE A  1 242 ? 6.076   20.574  -12.944 1.00 37.32 ? 242 ILE C O     1 
ATOM   1602  C CB    . ILE A  1 242 ? 7.383   18.201  -11.466 1.00 36.01 ? 242 ILE C CB    1 
ATOM   1603  C CG1   . ILE A  1 242 ? 7.513   16.907  -10.707 1.00 32.82 ? 242 ILE C CG1   1 
ATOM   1604  C CG2   . ILE A  1 242 ? 8.124   19.284  -10.688 1.00 32.01 ? 242 ILE C CG2   1 
ATOM   1605  C CD1   . ILE A  1 242 ? 8.948   16.487  -10.668 1.00 39.05 ? 242 ILE C CD1   1 
ATOM   1606  N N     . THR A  1 243 ? 5.348   20.741  -10.827 1.00 34.88 ? 243 THR C N     1 
ATOM   1607  C CA    . THR A  1 243 ? 5.161   22.181  -10.893 1.00 34.53 ? 243 THR C CA    1 
ATOM   1608  C C     . THR A  1 243 ? 6.442   22.898  -10.493 1.00 35.28 ? 243 THR C C     1 
ATOM   1609  O O     . THR A  1 243 ? 7.094   22.514  -9.516  1.00 34.21 ? 243 THR C O     1 
ATOM   1610  C CB    . THR A  1 243 ? 3.995   22.583  -9.992  1.00 32.13 ? 243 THR C CB    1 
ATOM   1611  O OG1   . THR A  1 243 ? 2.838   22.776  -10.812 1.00 34.37 ? 243 THR C OG1   1 
ATOM   1612  C CG2   . THR A  1 243 ? 4.300   23.838  -9.213  1.00 37.09 ? 243 THR C CG2   1 
ATOM   1613  N N     . VAL A  1 244 ? 6.833   23.907  -11.273 1.00 34.80 ? 244 VAL C N     1 
ATOM   1614  C CA    . VAL A  1 244 ? 8.033   24.676  -10.971 1.00 33.54 ? 244 VAL C CA    1 
ATOM   1615  C C     . VAL A  1 244 ? 7.711   26.158  -11.101 1.00 33.83 ? 244 VAL C C     1 
ATOM   1616  O O     . VAL A  1 244 ? 7.194   26.587  -12.137 1.00 36.87 ? 244 VAL C O     1 
ATOM   1617  C CB    . VAL A  1 244 ? 9.207   24.278  -11.879 1.00 36.83 ? 244 VAL C CB    1 
ATOM   1618  C CG1   . VAL A  1 244 ? 10.532  24.644  -11.197 1.00 35.12 ? 244 VAL C CG1   1 
ATOM   1619  C CG2   . VAL A  1 244 ? 9.151   22.781  -12.198 1.00 28.55 ? 244 VAL C CG2   1 
ATOM   1620  N N     . GLU A  1 245 ? 8.042   26.935  -10.058 1.00 32.60 ? 245 GLU C N     1 
ATOM   1621  C CA    . GLU A  1 245 ? 7.578   28.310  -9.864  1.00 33.69 ? 245 GLU C CA    1 
ATOM   1622  C C     . GLU A  1 245 ? 8.636   29.170  -9.176  1.00 33.94 ? 245 GLU C C     1 
ATOM   1623  O O     . GLU A  1 245 ? 9.469   28.681  -8.407  1.00 35.90 ? 245 GLU C O     1 
ATOM   1624  C CB    . GLU A  1 245 ? 6.312   28.394  -8.993  1.00 28.01 ? 245 GLU C CB    1 
ATOM   1625  C CG    . GLU A  1 245 ? 5.197   27.452  -9.327  1.00 33.14 ? 245 GLU C CG    1 
ATOM   1626  C CD    . GLU A  1 245 ? 4.007   27.633  -8.390  1.00 37.06 ? 245 GLU C CD    1 
ATOM   1627  O OE1   . GLU A  1 245 ? 4.238   27.485  -7.172  1.00 41.29 ? 245 GLU C OE1   1 
ATOM   1628  O OE2   . GLU A  1 245 ? 2.862   27.927  -8.859  1.00 35.03 ? 245 GLU C OE2   1 
ATOM   1629  N N     . THR A  1 246 ? 8.548   30.470  -9.419  1.00 32.59 ? 246 THR C N     1 
ATOM   1630  C CA    . THR A  1 246 ? 9.292   31.446  -8.637  1.00 30.04 ? 246 THR C CA    1 
ATOM   1631  C C     . THR A  1 246 ? 8.786   31.449  -7.201  1.00 29.56 ? 246 THR C C     1 
ATOM   1632  O O     . THR A  1 246 ? 7.591   31.609  -6.960  1.00 30.37 ? 246 THR C O     1 
ATOM   1633  C CB    . THR A  1 246 ? 9.116   32.835  -9.258  1.00 34.51 ? 246 THR C CB    1 
ATOM   1634  O OG1   . THR A  1 246 ? 9.581   32.819  -10.617 1.00 34.49 ? 246 THR C OG1   1 
ATOM   1635  C CG2   . THR A  1 246 ? 9.840   33.926  -8.449  1.00 30.00 ? 246 THR C CG2   1 
ATOM   1636  N N     . TYR A  1 247 ? 9.684   31.266  -6.244  1.00 32.66 ? 247 TYR C N     1 
ATOM   1637  C CA    . TYR A  1 247 ? 9.314   31.354  -4.838  1.00 33.15 ? 247 TYR C CA    1 
ATOM   1638  C C     . TYR A  1 247 ? 9.520   32.783  -4.358  1.00 35.06 ? 247 TYR C C     1 
ATOM   1639  O O     . TYR A  1 247 ? 10.616  33.338  -4.502  1.00 34.28 ? 247 TYR C O     1 
ATOM   1640  C CB    . TYR A  1 247 ? 10.140  30.386  -3.986  1.00 35.54 ? 247 TYR C CB    1 
ATOM   1641  C CG    . TYR A  1 247 ? 9.593   30.203  -2.569  1.00 36.87 ? 247 TYR C CG    1 
ATOM   1642  C CD1   . TYR A  1 247 ? 9.948   31.070  -1.545  1.00 33.75 ? 247 TYR C CD1   1 
ATOM   1643  C CD2   . TYR A  1 247 ? 8.692   29.178  -2.276  1.00 34.59 ? 247 TYR C CD2   1 
ATOM   1644  C CE1   . TYR A  1 247 ? 9.434   30.914  -0.265  1.00 35.98 ? 247 TYR C CE1   1 
ATOM   1645  C CE2   . TYR A  1 247 ? 8.189   29.013  -1.005  1.00 33.47 ? 247 TYR C CE2   1 
ATOM   1646  C CZ    . TYR A  1 247 ? 8.558   29.886  -0.002  1.00 34.49 ? 247 TYR C CZ    1 
ATOM   1647  O OH    . TYR A  1 247 ? 8.057   29.720  1.273   1.00 30.98 ? 247 TYR C OH    1 
ATOM   1648  N N     . HIS A  1 248 ? 8.476   33.365  -3.773  1.00 32.34 ? 248 HIS C N     1 
ATOM   1649  C CA    . HIS A  1 248 ? 8.524   34.717  -3.236  1.00 38.11 ? 248 HIS C CA    1 
ATOM   1650  C C     . HIS A  1 248 ? 8.563   34.719  -1.709  1.00 39.88 ? 248 HIS C C     1 
ATOM   1651  O O     . HIS A  1 248 ? 7.994   33.840  -1.059  1.00 42.20 ? 248 HIS C O     1 
ATOM   1652  C CB    . HIS A  1 248 ? 7.310   35.544  -3.677  1.00 36.07 ? 248 HIS C CB    1 
ATOM   1653  C CG    . HIS A  1 248 ? 7.253   35.817  -5.148  1.00 37.19 ? 248 HIS C CG    1 
ATOM   1654  N ND1   . HIS A  1 248 ? 8.041   36.767  -5.765  1.00 36.67 ? 248 HIS C ND1   1 
ATOM   1655  C CD2   . HIS A  1 248 ? 6.471   35.292  -6.119  1.00 31.95 ? 248 HIS C CD2   1 
ATOM   1656  C CE1   . HIS A  1 248 ? 7.758   36.804  -7.053  1.00 31.32 ? 248 HIS C CE1   1 
ATOM   1657  N NE2   . HIS A  1 248 ? 6.809   35.918  -7.294  1.00 35.79 ? 248 HIS C NE2   1 
ATOM   1658  N N     . ARG A  1 249 ? 9.237   35.729  -1.152  1.00 37.82 ? 249 ARG C N     1 
ATOM   1659  C CA    . ARG A  1 249 ? 9.059   36.139  0.239   1.00 43.69 ? 249 ARG C CA    1 
ATOM   1660  C C     . ARG A  1 249 ? 7.734   36.890  0.388   1.00 49.22 ? 249 ARG C C     1 
ATOM   1661  O O     . ARG A  1 249 ? 7.280   37.572  -0.536  1.00 49.78 ? 249 ARG C O     1 
ATOM   1662  C CB    . ARG A  1 249 ? 10.219  37.039  0.673   1.00 37.80 ? 249 ARG C CB    1 
ATOM   1663  C CG    . ARG A  1 249 ? 11.019  36.531  1.845   1.00 52.45 ? 249 ARG C CG    1 
ATOM   1664  C CD    . ARG A  1 249 ? 11.771  35.226  1.520   1.00 57.60 ? 249 ARG C CD    1 
ATOM   1665  N NE    . ARG A  1 249 ? 12.342  34.640  2.731   1.00 54.96 ? 249 ARG C NE    1 
ATOM   1666  C CZ    . ARG A  1 249 ? 13.606  34.762  3.109   1.00 53.93 ? 249 ARG C CZ    1 
ATOM   1667  N NH1   . ARG A  1 249 ? 14.507  35.338  2.330   1.00 53.92 ? 249 ARG C NH1   1 
ATOM   1668  N NH2   . ARG A  1 249 ? 13.971  34.304  4.306   1.00 47.68 ? 249 ARG C NH2   1 
ATOM   1669  N N     . ALA A  1 250 ? 7.104   36.777  1.559   1.00 43.39 ? 250 ALA C N     1 
ATOM   1670  C CA    . ALA A  1 250 ? 5.724   37.241  1.653   1.00 45.90 ? 250 ALA C CA    1 
ATOM   1671  C C     . ALA A  1 250 ? 5.410   37.924  2.975   1.00 42.33 ? 250 ALA C C     1 
ATOM   1672  O O     . ALA A  1 250 ? 5.790   37.447  4.049   1.00 38.76 ? 250 ALA C O     1 
ATOM   1673  C CB    . ALA A  1 250 ? 4.735   36.083  1.448   1.00 45.78 ? 250 ALA C CB    1 
ATOM   1674  N N     . ASP A  1 251 ? 4.663   39.026  2.870   1.00 43.74 ? 251 ASP C N     1 
ATOM   1675  C CA    . ASP A  1 251 ? 4.127   39.712  4.042   1.00 40.85 ? 251 ASP C CA    1 
ATOM   1676  C C     . ASP A  1 251 ? 3.121   38.857  4.799   1.00 41.97 ? 251 ASP C C     1 
ATOM   1677  O O     . ASP A  1 251 ? 2.995   38.980  6.021   1.00 48.57 ? 251 ASP C O     1 
ATOM   1678  C CB    . ASP A  1 251 ? 3.477   41.026  3.612   1.00 40.13 ? 251 ASP C CB    1 
ATOM   1679  C CG    . ASP A  1 251 ? 3.387   42.037  4.743   1.00 50.90 ? 251 ASP C CG    1 
ATOM   1680  O OD1   . ASP A  1 251 ? 3.658   41.673  5.913   1.00 48.49 ? 251 ASP C OD1   1 
ATOM   1681  O OD2   . ASP A  1 251 ? 3.065   43.211  4.452   1.00 56.24 ? 251 ASP C OD2   1 
ATOM   1682  N N     . GLN A  1 252 ? 2.392   37.997  4.103   1.00 40.49 ? 252 GLN C N     1 
ATOM   1683  C CA    . GLN A  1 252 ? 1.337   37.233  4.746   1.00 39.90 ? 252 GLN C CA    1 
ATOM   1684  C C     . GLN A  1 252 ? 1.095   35.947  3.958   1.00 38.78 ? 252 GLN C C     1 
ATOM   1685  O O     . GLN A  1 252 ? 1.162   35.950  2.727   1.00 44.78 ? 252 GLN C O     1 
ATOM   1686  C CB    . GLN A  1 252 ? 0.064   38.089  4.851   1.00 43.46 ? 252 GLN C CB    1 
ATOM   1687  C CG    . GLN A  1 252 ? -0.868  37.698  6.003   1.00 46.43 ? 252 GLN C CG    1 
ATOM   1688  C CD    . GLN A  1 252 ? -0.273  38.000  7.358   1.00 45.57 ? 252 GLN C CD    1 
ATOM   1689  O OE1   . GLN A  1 252 ? 0.580   37.257  7.843   1.00 47.92 ? 252 GLN C OE1   1 
ATOM   1690  N NE2   . GLN A  1 252 ? -0.733  39.078  7.990   1.00 41.17 ? 252 GLN C NE2   1 
ATOM   1691  N N     . ARG A  1 253 ? 0.841   34.845  4.665   1.00 33.75 ? 253 ARG C N     1 
ATOM   1692  C CA    . ARG A  1 253 ? 0.567   33.544  4.052   1.00 31.68 ? 253 ARG C CA    1 
ATOM   1693  C C     . ARG A  1 253 ? -0.824  33.119  4.512   1.00 36.34 ? 253 ARG C C     1 
ATOM   1694  O O     . ARG A  1 253 ? -1.012  32.676  5.648   1.00 35.35 ? 253 ARG C O     1 
ATOM   1695  C CB    . ARG A  1 253 ? 1.631   32.515  4.423   1.00 32.60 ? 253 ARG C CB    1 
ATOM   1696  C CG    . ARG A  1 253 ? 3.040   32.895  3.950   1.00 37.88 ? 253 ARG C CG    1 
ATOM   1697  C CD    . ARG A  1 253 ? 4.001   31.720  4.018   1.00 38.36 ? 253 ARG C CD    1 
ATOM   1698  N NE    . ARG A  1 253 ? 4.849   31.621  2.834   1.00 40.65 ? 253 ARG C NE    1 
ATOM   1699  C CZ    . ARG A  1 253 ? 5.894   32.404  2.616   1.00 39.39 ? 253 ARG C CZ    1 
ATOM   1700  N NH1   . ARG A  1 253 ? 6.244   33.340  3.482   1.00 48.32 ? 253 ARG C NH1   1 
ATOM   1701  N NH2   . ARG A  1 253 ? 6.586   32.267  1.491   1.00 38.39 ? 253 ARG C NH2   1 
ATOM   1702  N N     . PHE A  1 254 ? -1.795  33.254  3.620   1.00 38.36 ? 254 PHE C N     1 
ATOM   1703  C CA    . PHE A  1 254 ? -3.203  33.202  3.957   1.00 31.23 ? 254 PHE C CA    1 
ATOM   1704  C C     . PHE A  1 254 ? -3.911  32.143  3.124   1.00 34.93 ? 254 PHE C C     1 
ATOM   1705  O O     . PHE A  1 254 ? -3.382  31.642  2.124   1.00 35.60 ? 254 PHE C O     1 
ATOM   1706  C CB    . PHE A  1 254 ? -3.853  34.579  3.720   1.00 35.04 ? 254 PHE C CB    1 
ATOM   1707  C CG    . PHE A  1 254 ? -4.073  34.917  2.257   1.00 32.24 ? 254 PHE C CG    1 
ATOM   1708  C CD1   . PHE A  1 254 ? -5.192  34.450  1.572   1.00 32.12 ? 254 PHE C CD1   1 
ATOM   1709  C CD2   . PHE A  1 254 ? -3.172  35.727  1.581   1.00 30.77 ? 254 PHE C CD2   1 
ATOM   1710  C CE1   . PHE A  1 254 ? -5.376  34.749  0.241   1.00 33.68 ? 254 PHE C CE1   1 
ATOM   1711  C CE2   . PHE A  1 254 ? -3.353  36.035  0.248   1.00 27.81 ? 254 PHE C CE2   1 
ATOM   1712  C CZ    . PHE A  1 254 ? -4.448  35.550  -0.424  1.00 31.97 ? 254 PHE C CZ    1 
ATOM   1713  N N     . PHE A  1 255 ? -5.147  31.843  3.519   1.00 32.24 ? 255 PHE C N     1 
ATOM   1714  C CA    . PHE A  1 255 ? -6.066  31.170  2.620   1.00 31.38 ? 255 PHE C CA    1 
ATOM   1715  C C     . PHE A  1 255 ? -7.497  31.525  3.001   1.00 34.38 ? 255 PHE C C     1 
ATOM   1716  O O     . PHE A  1 255 ? -7.771  32.017  4.097   1.00 31.34 ? 255 PHE C O     1 
ATOM   1717  C CB    . PHE A  1 255 ? -5.844  29.655  2.616   1.00 36.70 ? 255 PHE C CB    1 
ATOM   1718  C CG    . PHE A  1 255 ? -6.355  28.954  3.834   1.00 36.22 ? 255 PHE C CG    1 
ATOM   1719  C CD1   . PHE A  1 255 ? -5.569  28.837  4.958   1.00 36.52 ? 255 PHE C CD1   1 
ATOM   1720  C CD2   . PHE A  1 255 ? -7.608  28.387  3.841   1.00 34.91 ? 255 PHE C CD2   1 
ATOM   1721  C CE1   . PHE A  1 255 ? -6.031  28.175  6.071   1.00 35.31 ? 255 PHE C CE1   1 
ATOM   1722  C CE2   . PHE A  1 255 ? -8.073  27.720  4.964   1.00 34.06 ? 255 PHE C CE2   1 
ATOM   1723  C CZ    . PHE A  1 255 ? -7.281  27.611  6.073   1.00 30.60 ? 255 PHE C CZ    1 
ATOM   1724  N N     . PHE A  1 256 ? -8.403  31.292  2.064   1.00 34.06 ? 256 PHE C N     1 
ATOM   1725  C CA    . PHE A  1 256 ? -9.822  31.549  2.247   1.00 30.65 ? 256 PHE C CA    1 
ATOM   1726  C C     . PHE A  1 256 ? -10.573 30.242  2.046   1.00 29.90 ? 256 PHE C C     1 
ATOM   1727  O O     . PHE A  1 256 ? -10.357 29.564  1.041   1.00 32.17 ? 256 PHE C O     1 
ATOM   1728  C CB    . PHE A  1 256 ? -10.307 32.583  1.235   1.00 28.08 ? 256 PHE C CB    1 
ATOM   1729  C CG    . PHE A  1 256 ? -9.581  33.911  1.296   1.00 30.02 ? 256 PHE C CG    1 
ATOM   1730  C CD1   . PHE A  1 256 ? -9.104  34.408  2.481   1.00 28.62 ? 256 PHE C CD1   1 
ATOM   1731  C CD2   . PHE A  1 256 ? -9.422  34.680  0.147   1.00 33.74 ? 256 PHE C CD2   1 
ATOM   1732  C CE1   . PHE A  1 256 ? -8.466  35.636  2.528   1.00 31.44 ? 256 PHE C CE1   1 
ATOM   1733  C CE2   . PHE A  1 256 ? -8.776  35.912  0.184   1.00 32.39 ? 256 PHE C CE2   1 
ATOM   1734  C CZ    . PHE A  1 256 ? -8.296  36.388  1.375   1.00 33.00 ? 256 PHE C CZ    1 
ATOM   1735  N N     . GLU A  1 257 ? -11.447 29.876  2.982   1.00 26.66 ? 257 GLU C N     1 
ATOM   1736  C CA    . GLU A  1 257 ? -12.247 28.661  2.835   1.00 25.76 ? 257 GLU C CA    1 
ATOM   1737  C C     . GLU A  1 257 ? -13.708 28.995  2.530   1.00 27.20 ? 257 GLU C C     1 
ATOM   1738  O O     . GLU A  1 257 ? -14.270 29.948  3.081   1.00 31.47 ? 257 GLU C O     1 
ATOM   1739  C CB    . GLU A  1 257 ? -12.164 27.775  4.078   1.00 31.80 ? 257 GLU C CB    1 
ATOM   1740  C CG    . GLU A  1 257 ? -12.886 26.423  3.931   1.00 30.00 ? 257 GLU C CG    1 
ATOM   1741  C CD    . GLU A  1 257 ? -12.226 25.303  4.738   1.00 32.18 ? 257 GLU C CD    1 
ATOM   1742  O OE1   . GLU A  1 257 ? -11.563 25.585  5.774   1.00 31.51 ? 257 GLU C OE1   1 
ATOM   1743  O OE2   . GLU A  1 257 ? -12.378 24.134  4.332   1.00 30.73 ? 257 GLU C OE2   1 
ATOM   1744  N N     . TYR A  1 258 ? -14.314 28.196  1.650   1.00 22.69 ? 258 TYR C N     1 
ATOM   1745  C CA    . TYR A  1 258 ? -15.669 28.385  1.165   1.00 23.12 ? 258 TYR C CA    1 
ATOM   1746  C C     . TYR A  1 258 ? -16.468 27.092  1.317   1.00 27.76 ? 258 TYR C C     1 
ATOM   1747  O O     . TYR A  1 258 ? -15.896 26.000  1.427   1.00 24.67 ? 258 TYR C O     1 
ATOM   1748  C CB    . TYR A  1 258 ? -15.674 28.769  -0.306  1.00 25.92 ? 258 TYR C CB    1 
ATOM   1749  C CG    . TYR A  1 258 ? -14.974 30.052  -0.672  1.00 26.80 ? 258 TYR C CG    1 
ATOM   1750  C CD1   . TYR A  1 258 ? -13.581 30.135  -0.748  1.00 23.68 ? 258 TYR C CD1   1 
ATOM   1751  C CD2   . TYR A  1 258 ? -15.712 31.175  -1.006  1.00 26.00 ? 258 TYR C CD2   1 
ATOM   1752  C CE1   . TYR A  1 258 ? -12.951 31.334  -1.115  1.00 21.40 ? 258 TYR C CE1   1 
ATOM   1753  C CE2   . TYR A  1 258 ? -15.101 32.348  -1.364  1.00 27.72 ? 258 TYR C CE2   1 
ATOM   1754  C CZ    . TYR A  1 258 ? -13.732 32.433  -1.423  1.00 26.90 ? 258 TYR C CZ    1 
ATOM   1755  O OH    . TYR A  1 258 ? -13.193 33.646  -1.803  1.00 33.68 ? 258 TYR C OH    1 
ATOM   1756  N N     . HIS A  1 259 ? -17.806 27.209  1.272   1.00 28.36 ? 259 HIS C N     1 
ATOM   1757  C CA    . HIS A  1 259 ? -18.671 26.038  1.127   1.00 29.62 ? 259 HIS C CA    1 
ATOM   1758  C C     . HIS A  1 259 ? -19.559 26.221  -0.092  1.00 28.97 ? 259 HIS C C     1 
ATOM   1759  O O     . HIS A  1 259 ? -20.079 27.314  -0.330  1.00 32.87 ? 259 HIS C O     1 
ATOM   1760  C CB    . HIS A  1 259 ? -19.567 25.769  2.362   1.00 25.36 ? 259 HIS C CB    1 
ATOM   1761  C CG    . HIS A  1 259 ? -20.509 24.610  2.179   1.00 24.77 ? 259 HIS C CG    1 
ATOM   1762  N ND1   . HIS A  1 259 ? -20.247 23.344  2.665   1.00 25.27 ? 259 HIS C ND1   1 
ATOM   1763  C CD2   . HIS A  1 259 ? -21.703 24.522  1.541   1.00 25.26 ? 259 HIS C CD2   1 
ATOM   1764  C CE1   . HIS A  1 259 ? -21.246 22.533  2.361   1.00 22.30 ? 259 HIS C CE1   1 
ATOM   1765  N NE2   . HIS A  1 259 ? -22.138 23.222  1.671   1.00 29.94 ? 259 HIS C NE2   1 
ATOM   1766  N N     . LEU A  1 260 ? -19.791 25.129  -0.820  1.00 27.61 ? 260 LEU C N     1 
ATOM   1767  C CA    . LEU A  1 260 ? -20.393 25.176  -2.148  1.00 29.68 ? 260 LEU C CA    1 
ATOM   1768  C C     . LEU A  1 260 ? -21.660 24.335  -2.230  1.00 31.25 ? 260 LEU C C     1 
ATOM   1769  O O     . LEU A  1 260 ? -21.670 23.167  -1.810  1.00 30.01 ? 260 LEU C O     1 
ATOM   1770  C CB    . LEU A  1 260 ? -19.394 24.684  -3.201  1.00 28.87 ? 260 LEU C CB    1 
ATOM   1771  C CG    . LEU A  1 260 ? -18.476 25.696  -3.903  1.00 26.68 ? 260 LEU C CG    1 
ATOM   1772  C CD1   . LEU A  1 260 ? -17.518 26.390  -2.933  1.00 26.55 ? 260 LEU C CD1   1 
ATOM   1773  C CD2   . LEU A  1 260 ? -17.685 24.954  -4.972  1.00 25.08 ? 260 LEU C CD2   1 
ATOM   1774  N N     . ASP A  1 261 ? -22.713 24.930  -2.804  1.00 32.38 ? 261 ASP C N     1 
ATOM   1775  C CA    . ASP A  1 261 ? -23.940 24.238  -3.185  1.00 40.75 ? 261 ASP C CA    1 
ATOM   1776  C C     . ASP A  1 261 ? -24.396 24.772  -4.537  1.00 39.29 ? 261 ASP C C     1 
ATOM   1777  O O     . ASP A  1 261 ? -23.831 25.738  -5.067  1.00 37.43 ? 261 ASP C O     1 
ATOM   1778  C CB    . ASP A  1 261 ? -25.043 24.409  -2.128  1.00 33.67 ? 261 ASP C CB    1 
ATOM   1779  C CG    . ASP A  1 261 ? -25.445 25.864  -1.916  1.00 39.07 ? 261 ASP C CG    1 
ATOM   1780  O OD1   . ASP A  1 261 ? -25.151 26.734  -2.766  1.00 42.57 ? 261 ASP C OD1   1 
ATOM   1781  O OD2   . ASP A  1 261 ? -26.054 26.154  -0.863  1.00 49.60 ? 261 ASP C OD2   1 
ATOM   1782  N N     . GLY A  1 262 ? -25.471 24.179  -5.063  1.00 35.30 ? 262 GLY C N     1 
ATOM   1783  C CA    . GLY A  1 262 ? -25.977 24.598  -6.360  1.00 37.36 ? 262 GLY C CA    1 
ATOM   1784  C C     . GLY A  1 262 ? -26.280 26.081  -6.450  1.00 42.41 ? 262 GLY C C     1 
ATOM   1785  O O     . GLY A  1 262 ? -26.189 26.669  -7.533  1.00 40.85 ? 262 GLY C O     1 
ATOM   1786  N N     . ASP A  1 263 ? -26.588 26.718  -5.317  1.00 42.27 ? 263 ASP C N     1 
ATOM   1787  C CA    . ASP A  1 263 ? -27.055 28.101  -5.295  1.00 38.97 ? 263 ASP C CA    1 
ATOM   1788  C C     . ASP A  1 263 ? -25.953 29.111  -5.086  1.00 38.98 ? 263 ASP C C     1 
ATOM   1789  O O     . ASP A  1 263 ? -26.009 30.202  -5.655  1.00 42.83 ? 263 ASP C O     1 
ATOM   1790  C CB    . ASP A  1 263 ? -28.087 28.316  -4.186  1.00 43.35 ? 263 ASP C CB    1 
ATOM   1791  C CG    . ASP A  1 263 ? -28.842 27.051  -3.825  1.00 54.79 ? 263 ASP C CG    1 
ATOM   1792  O OD1   . ASP A  1 263 ? -28.216 25.956  -3.789  1.00 53.72 ? 263 ASP C OD1   1 
ATOM   1793  O OD2   . ASP A  1 263 ? -30.066 27.162  -3.565  1.00 60.29 ? 263 ASP C OD2   1 
ATOM   1794  N N     . ARG A  1 264 ? -24.968 28.797  -4.250  1.00 37.54 ? 264 ARG C N     1 
ATOM   1795  C CA    . ARG A  1 264 ? -24.009 29.816  -3.858  1.00 34.21 ? 264 ARG C CA    1 
ATOM   1796  C C     . ARG A  1 264 ? -22.698 29.182  -3.450  1.00 36.66 ? 264 ARG C C     1 
ATOM   1797  O O     . ARG A  1 264 ? -22.669 28.089  -2.877  1.00 33.85 ? 264 ARG C O     1 
ATOM   1798  C CB    . ARG A  1 264 ? -24.552 30.670  -2.709  1.00 36.60 ? 264 ARG C CB    1 
ATOM   1799  C CG    . ARG A  1 264 ? -25.049 29.866  -1.535  1.00 41.83 ? 264 ARG C CG    1 
ATOM   1800  C CD    . ARG A  1 264 ? -24.061 29.913  -0.419  1.00 37.87 ? 264 ARG C CD    1 
ATOM   1801  N NE    . ARG A  1 264 ? -24.354 28.965  0.647   1.00 41.91 ? 264 ARG C NE    1 
ATOM   1802  C CZ    . ARG A  1 264 ? -23.854 27.737  0.708   1.00 41.56 ? 264 ARG C CZ    1 
ATOM   1803  N NH1   . ARG A  1 264 ? -23.166 27.218  -0.298  1.00 37.05 ? 264 ARG C NH1   1 
ATOM   1804  N NH2   . ARG A  1 264 ? -24.013 27.026  1.820   1.00 38.78 ? 264 ARG C NH2   1 
ATOM   1805  N N     . ALA A  1 265 ? -21.622 29.880  -3.797  1.00 37.56 ? 265 ALA C N     1 
ATOM   1806  C CA    . ALA A  1 265 ? -20.309 29.683  -3.205  1.00 31.41 ? 265 ALA C CA    1 
ATOM   1807  C C     . ALA A  1 265 ? -20.242 30.539  -1.948  1.00 37.18 ? 265 ALA C C     1 
ATOM   1808  O O     . ALA A  1 265 ? -20.409 31.759  -2.025  1.00 39.28 ? 265 ALA C O     1 
ATOM   1809  C CB    . ALA A  1 265 ? -19.214 30.082  -4.189  1.00 35.27 ? 265 ALA C CB    1 
ATOM   1810  N N     . ARG A  1 266 ? -19.988 29.908  -0.802  1.00 32.60 ? 266 ARG C N     1 
ATOM   1811  C CA    . ARG A  1 266 ? -20.187 30.520  0.505   1.00 33.55 ? 266 ARG C CA    1 
ATOM   1812  C C     . ARG A  1 266 ? -18.866 30.766  1.223   1.00 35.79 ? 266 ARG C C     1 
ATOM   1813  O O     . ARG A  1 266 ? -18.190 29.808  1.620   1.00 32.70 ? 266 ARG C O     1 
ATOM   1814  C CB    . ARG A  1 266 ? -21.070 29.632  1.371   1.00 38.16 ? 266 ARG C CB    1 
ATOM   1815  C CG    . ARG A  1 266 ? -21.545 30.372  2.559   1.00 37.90 ? 266 ARG C CG    1 
ATOM   1816  C CD    . ARG A  1 266 ? -22.394 29.508  3.401   1.00 50.45 ? 266 ARG C CD    1 
ATOM   1817  N NE    . ARG A  1 266 ? -21.896 28.167  3.701   1.00 48.50 ? 266 ARG C NE    1 
ATOM   1818  C CZ    . ARG A  1 266 ? -22.118 27.564  4.866   1.00 47.10 ? 266 ARG C CZ    1 
ATOM   1819  N NH1   . ARG A  1 266 ? -22.824 28.157  5.821   1.00 40.95 ? 266 ARG C NH1   1 
ATOM   1820  N NH2   . ARG A  1 266 ? -21.630 26.337  5.078   1.00 39.20 ? 266 ARG C NH2   1 
ATOM   1821  N N     . PHE A  1 267 ? -18.541 32.045  1.447   1.00 30.14 ? 267 PHE C N     1 
ATOM   1822  C CA    . PHE A  1 267 ? -17.362 32.407  2.218   1.00 26.94 ? 267 PHE C CA    1 
ATOM   1823  C C     . PHE A  1 267 ? -17.535 31.997  3.666   1.00 34.22 ? 267 PHE C C     1 
ATOM   1824  O O     . PHE A  1 267 ? -18.521 32.359  4.317   1.00 39.32 ? 267 PHE C O     1 
ATOM   1825  C CB    . PHE A  1 267 ? -17.111 33.902  2.170   1.00 26.55 ? 267 PHE C CB    1 
ATOM   1826  C CG    . PHE A  1 267 ? -15.768 34.313  2.733   1.00 32.08 ? 267 PHE C CG    1 
ATOM   1827  C CD1   . PHE A  1 267 ? -14.628 34.325  1.922   1.00 34.99 ? 267 PHE C CD1   1 
ATOM   1828  C CD2   . PHE A  1 267 ? -15.632 34.662  4.069   1.00 30.05 ? 267 PHE C CD2   1 
ATOM   1829  C CE1   . PHE A  1 267 ? -13.378 34.702  2.439   1.00 30.06 ? 267 PHE C CE1   1 
ATOM   1830  C CE2   . PHE A  1 267 ? -14.397 35.039  4.593   1.00 26.38 ? 267 PHE C CE2   1 
ATOM   1831  C CZ    . PHE A  1 267 ? -13.275 35.058  3.784   1.00 31.56 ? 267 PHE C CZ    1 
ATOM   1832  N N     . LEU A  1 268 ? -16.553 31.276  4.181   1.00 32.68 ? 268 LEU C N     1 
ATOM   1833  C CA    . LEU A  1 268 ? -16.587 30.762  5.536   1.00 30.45 ? 268 LEU C CA    1 
ATOM   1834  C C     . LEU A  1 268 ? -15.641 31.505  6.465   1.00 29.78 ? 268 LEU C C     1 
ATOM   1835  O O     . LEU A  1 268 ? -16.063 31.980  7.522   1.00 31.23 ? 268 LEU C O     1 
ATOM   1836  C CB    . LEU A  1 268 ? -16.244 29.265  5.516   1.00 28.45 ? 268 LEU C CB    1 
ATOM   1837  C CG    . LEU A  1 268 ? -17.217 28.388  4.739   1.00 27.25 ? 268 LEU C CG    1 
ATOM   1838  C CD1   . LEU A  1 268 ? -17.191 26.975  5.319   1.00 22.69 ? 268 LEU C CD1   1 
ATOM   1839  C CD2   . LEU A  1 268 ? -18.632 28.968  4.747   1.00 27.38 ? 268 LEU C CD2   1 
ATOM   1840  N N     . HIS A  1 269 ? -14.368 31.618  6.093   1.00 31.79 ? 269 HIS C N     1 
ATOM   1841  C CA    . HIS A  1 269 ? -13.352 32.219  6.952   1.00 29.90 ? 269 HIS C CA    1 
ATOM   1842  C C     . HIS A  1 269 ? -12.076 32.439  6.157   1.00 32.07 ? 269 HIS C C     1 
ATOM   1843  O O     . HIS A  1 269 ? -11.889 31.886  5.072   1.00 34.75 ? 269 HIS C O     1 
ATOM   1844  C CB    . HIS A  1 269 ? -13.056 31.351  8.175   1.00 30.87 ? 269 HIS C CB    1 
ATOM   1845  C CG    . HIS A  1 269 ? -12.250 30.130  7.872   1.00 29.30 ? 269 HIS C CG    1 
ATOM   1846  N ND1   . HIS A  1 269 ? -10.877 30.096  7.979   1.00 33.95 ? 269 HIS C ND1   1 
ATOM   1847  C CD2   . HIS A  1 269 ? -12.629 28.889  7.479   1.00 28.00 ? 269 HIS C CD2   1 
ATOM   1848  C CE1   . HIS A  1 269 ? -10.446 28.884  7.670   1.00 35.04 ? 269 HIS C CE1   1 
ATOM   1849  N NE2   . HIS A  1 269 ? -11.490 28.133  7.361   1.00 26.83 ? 269 HIS C NE2   1 
ATOM   1850  N N     . SER A  1 270 ? -11.216 33.276  6.712   1.00 34.98 ? 270 SER C N     1 
ATOM   1851  C CA    . SER A  1 270 ? -9.853  33.459  6.256   1.00 29.25 ? 270 SER C CA    1 
ATOM   1852  C C     . SER A  1 270 ? -8.957  33.217  7.460   1.00 32.21 ? 270 SER C C     1 
ATOM   1853  O O     . SER A  1 270 ? -9.410  33.317  8.601   1.00 26.92 ? 270 SER C O     1 
ATOM   1854  C CB    . SER A  1 270 ? -9.645  34.854  5.707   1.00 28.97 ? 270 SER C CB    1 
ATOM   1855  O OG    . SER A  1 270 ? -9.718  35.792  6.760   1.00 37.92 ? 270 SER C OG    1 
ATOM   1856  N N     . SER A  1 271 ? -7.689  32.889  7.195   1.00 35.81 ? 271 SER C N     1 
ATOM   1857  C CA    . SER A  1 271 ? -6.767  32.406  8.221   1.00 34.27 ? 271 SER C CA    1 
ATOM   1858  C C     . SER A  1 271 ? -5.309  32.624  7.803   1.00 34.88 ? 271 SER C C     1 
ATOM   1859  O O     . SER A  1 271 ? -4.962  32.499  6.619   1.00 31.03 ? 271 SER C O     1 
ATOM   1860  C CB    . SER A  1 271 ? -7.014  30.918  8.522   1.00 35.78 ? 271 SER C CB    1 
ATOM   1861  O OG    . SER A  1 271 ? -8.377  30.644  8.880   1.00 35.26 ? 271 SER C OG    1 
ATOM   1862  N N     . ILE A  1 272 ? -4.456  32.930  8.794   1.00 34.38 ? 272 ILE C N     1 
ATOM   1863  C CA    . ILE A  1 272 ? -3.022  33.137  8.583   1.00 30.85 ? 272 ILE C CA    1 
ATOM   1864  C C     . ILE A  1 272 ? -2.264  31.841  8.862   1.00 32.19 ? 272 ILE C C     1 
ATOM   1865  O O     . ILE A  1 272 ? -2.410  31.228  9.929   1.00 34.95 ? 272 ILE C O     1 
ATOM   1866  C CB    . ILE A  1 272 ? -2.497  34.282  9.459   1.00 33.18 ? 272 ILE C CB    1 
ATOM   1867  C CG1   . ILE A  1 272 ? -3.255  35.573  9.151   1.00 35.83 ? 272 ILE C CG1   1 
ATOM   1868  C CG2   . ILE A  1 272 ? -1.021  34.486  9.226   1.00 35.10 ? 272 ILE C CG2   1 
ATOM   1869  C CD1   . ILE A  1 272 ? -2.573  36.820  9.699   1.00 36.25 ? 272 ILE C CD1   1 
ATOM   1870  N N     . LEU A  1 273 ? -1.444  31.424  7.900   1.00 33.72 ? 273 LEU C N     1 
ATOM   1871  C CA    . LEU A  1 273 ? -0.665  30.198  8.015   1.00 35.11 ? 273 LEU C CA    1 
ATOM   1872  C C     . LEU A  1 273 ? 0.648   30.522  8.707   1.00 35.94 ? 273 LEU C C     1 
ATOM   1873  O O     . LEU A  1 273 ? 1.415   31.370  8.234   1.00 37.08 ? 273 LEU C O     1 
ATOM   1874  C CB    . LEU A  1 273 ? -0.395  29.586  6.639   1.00 35.54 ? 273 LEU C CB    1 
ATOM   1875  C CG    . LEU A  1 273 ? -1.504  29.348  5.600   1.00 37.71 ? 273 LEU C CG    1 
ATOM   1876  C CD1   . LEU A  1 273 ? -1.005  29.630  4.173   1.00 35.83 ? 273 LEU C CD1   1 
ATOM   1877  C CD2   . LEU A  1 273 ? -2.063  27.937  5.686   1.00 32.66 ? 273 LEU C CD2   1 
ATOM   1878  N N     . LYS A  1 274 ? 0.917   29.844  9.807   1.00 30.02 ? 274 LYS C N     1 
ATOM   1879  C CA    . LYS A  1 274 ? 2.065   30.166  10.637  1.00 35.20 ? 274 LYS C CA    1 
ATOM   1880  C C     . LYS A  1 274 ? 3.096   29.058  10.506  1.00 38.00 ? 274 LYS C C     1 
ATOM   1881  O O     . LYS A  1 274 ? 2.773   27.881  10.704  1.00 40.99 ? 274 LYS C O     1 
ATOM   1882  C CB    . LYS A  1 274 ? 1.638   30.346  12.093  1.00 36.15 ? 274 LYS C CB    1 
ATOM   1883  C CG    . LYS A  1 274 ? 0.270   31.006  12.234  1.00 36.77 ? 274 LYS C CG    1 
ATOM   1884  C CD    . LYS A  1 274 ? 0.323   32.419  11.742  1.00 31.03 ? 274 LYS C CD    1 
ATOM   1885  C CE    . LYS A  1 274 ? 1.445   33.150  12.443  1.00 34.85 ? 274 LYS C CE    1 
ATOM   1886  N NZ    . LYS A  1 274 ? 1.820   34.376  11.695  1.00 48.40 ? 274 LYS C NZ    1 
ATOM   1887  N N     . TYR A  1 275 ? 4.328   29.438  10.167  1.00 38.56 ? 275 TYR C N     1 
ATOM   1888  C CA    . TYR A  1 275 ? 5.428   28.506  9.960   1.00 39.80 ? 275 TYR C CA    1 
ATOM   1889  C C     . TYR A  1 275 ? 6.554   28.790  10.950  1.00 42.67 ? 275 TYR C C     1 
ATOM   1890  O O     . TYR A  1 275 ? 6.612   29.850  11.581  1.00 43.06 ? 275 TYR C O     1 
ATOM   1891  C CB    . TYR A  1 275 ? 5.964   28.577  8.525   1.00 36.74 ? 275 TYR C CB    1 
ATOM   1892  C CG    . TYR A  1 275 ? 4.912   28.360  7.475   1.00 36.44 ? 275 TYR C CG    1 
ATOM   1893  C CD1   . TYR A  1 275 ? 3.987   29.353  7.163   1.00 35.79 ? 275 TYR C CD1   1 
ATOM   1894  C CD2   . TYR A  1 275 ? 4.832   27.160  6.797   1.00 37.58 ? 275 TYR C CD2   1 
ATOM   1895  C CE1   . TYR A  1 275 ? 3.017   29.151  6.193   1.00 35.65 ? 275 TYR C CE1   1 
ATOM   1896  C CE2   . TYR A  1 275 ? 3.870   26.951  5.824   1.00 37.52 ? 275 TYR C CE2   1 
ATOM   1897  C CZ    . TYR A  1 275 ? 2.962   27.949  5.525   1.00 36.18 ? 275 TYR C CZ    1 
ATOM   1898  O OH    . TYR A  1 275 ? 1.993   27.739  4.556   1.00 40.67 ? 275 TYR C OH    1 
ATOM   1899  N N     . GLU A  1 276 ? 7.466   27.829  11.070  1.00 40.23 ? 276 GLU C N     1 
ATOM   1900  C CA    . GLU A  1 276 ? 8.490   27.920  12.097  1.00 41.70 ? 276 GLU C CA    1 
ATOM   1901  C C     . GLU A  1 276 ? 9.466   29.051  11.801  1.00 47.41 ? 276 GLU C C     1 
ATOM   1902  O O     . GLU A  1 276 ? 9.788   29.336  10.641  1.00 48.91 ? 276 GLU C O     1 
ATOM   1903  C CB    . GLU A  1 276 ? 9.239   26.596  12.218  1.00 43.83 ? 276 GLU C CB    1 
ATOM   1904  C CG    . GLU A  1 276 ? 10.206  26.336  11.101  1.00 47.28 ? 276 GLU C CG    1 
ATOM   1905  C CD    . GLU A  1 276 ? 10.899  25.000  11.236  1.00 49.36 ? 276 GLU C CD    1 
ATOM   1906  O OE1   . GLU A  1 276 ? 11.163  24.622  12.399  1.00 50.54 ? 276 GLU C OE1   1 
ATOM   1907  O OE2   . GLU A  1 276 ? 11.190  24.346  10.195  1.00 43.70 ? 276 GLU C OE2   1 
ATOM   1908  N N     . GLN A  1 277 ? 9.926   29.699  12.871  1.00 45.84 ? 277 GLN C N     1 
ATOM   1909  C CA    . GLN A  1 277 ? 10.925  30.760  12.784  1.00 53.91 ? 277 GLN C CA    1 
ATOM   1910  C C     . GLN A  1 277 ? 12.309  30.139  12.966  1.00 50.46 ? 277 GLN C C     1 
ATOM   1911  O O     . GLN A  1 277 ? 12.667  29.713  14.071  1.00 53.85 ? 277 GLN C O     1 
ATOM   1912  C CB    . GLN A  1 277 ? 10.655  31.844  13.828  1.00 51.72 ? 277 GLN C CB    1 
ATOM   1913  C CG    . GLN A  1 277 ? 9.627   32.893  13.402  1.00 44.80 ? 277 GLN C CG    1 
ATOM   1914  C CD    . GLN A  1 277 ? 9.177   33.783  14.551  1.00 57.23 ? 277 GLN C CD    1 
ATOM   1915  O OE1   . GLN A  1 277 ? 9.947   34.062  15.477  1.00 61.04 ? 277 GLN C OE1   1 
ATOM   1916  N NE2   . GLN A  1 277 ? 7.931   34.249  14.488  1.00 56.03 ? 277 GLN C NE2   1 
ATOM   1917  N N     . LEU A  1 278 ? 13.083  30.072  11.872  1.00 50.96 ? 278 LEU C N     1 
ATOM   1918  C CA    . LEU A  1 278 ? 14.433  29.525  11.925  1.00 54.79 ? 278 LEU C CA    1 
ATOM   1919  C C     . LEU A  1 278 ? 15.388  30.608  12.409  1.00 56.54 ? 278 LEU C C     1 
ATOM   1920  O O     . LEU A  1 278 ? 15.242  31.772  12.029  1.00 58.07 ? 278 LEU C O     1 
ATOM   1921  C CB    . LEU A  1 278 ? 14.878  29.017  10.547  1.00 46.53 ? 278 LEU C CB    1 
ATOM   1922  C CG    . LEU A  1 278 ? 13.856  28.257  9.704   1.00 42.01 ? 278 LEU C CG    1 
ATOM   1923  C CD1   . LEU A  1 278 ? 14.191  28.457  8.262   1.00 45.79 ? 278 LEU C CD1   1 
ATOM   1924  C CD2   . LEU A  1 278 ? 13.804  26.775  10.033  1.00 39.83 ? 278 LEU C CD2   1 
ATOM   1925  N N     . PRO A  1 279 ? 16.353  30.279  13.250  1.00 56.57 ? 279 PRO C N     1 
ATOM   1926  C CA    . PRO A  1 279 ? 17.301  31.312  13.702  1.00 62.68 ? 279 PRO C CA    1 
ATOM   1927  C C     . PRO A  1 279 ? 18.252  31.750  12.590  1.00 66.24 ? 279 PRO C C     1 
ATOM   1928  O O     . PRO A  1 279 ? 19.466  31.555  12.711  1.00 71.99 ? 279 PRO C O     1 
ATOM   1929  C CB    . PRO A  1 279 ? 18.029  30.614  14.852  1.00 61.20 ? 279 PRO C CB    1 
ATOM   1930  C CG    . PRO A  1 279 ? 18.000  29.180  14.471  1.00 53.80 ? 279 PRO C CG    1 
ATOM   1931  C CD    . PRO A  1 279 ? 16.669  28.958  13.812  1.00 51.99 ? 279 PRO C CD    1 
ATOM   1932  N N     . GLU A  1 280 ? 17.713  32.358  11.520  1.00 62.24 ? 280 GLU C N     1 
ATOM   1933  C CA    . GLU A  1 280 ? 18.413  32.683  10.270  1.00 63.74 ? 280 GLU C CA    1 
ATOM   1934  C C     . GLU A  1 280 ? 19.426  31.622  9.847   1.00 64.66 ? 280 GLU C C     1 
ATOM   1935  O O     . GLU A  1 280 ? 20.447  31.940  9.224   1.00 65.06 ? 280 GLU C O     1 
ATOM   1936  C CB    . GLU A  1 280 ? 19.108  34.044  10.364  1.00 63.62 ? 280 GLU C CB    1 
ATOM   1937  C CG    . GLU A  1 280 ? 20.285  34.117  11.317  1.00 61.47 ? 280 GLU C CG    1 
ATOM   1938  C CD    . GLU A  1 280 ? 19.855  34.618  12.668  1.00 68.71 ? 280 GLU C CD    1 
ATOM   1939  O OE1   . GLU A  1 280 ? 18.640  34.583  12.944  1.00 69.26 ? 280 GLU C OE1   1 
ATOM   1940  O OE2   . GLU A  1 280 ? 20.716  35.065  13.451  1.00 75.24 ? 280 GLU C OE2   1 
ATOM   1941  N N     . GLY A  1 281 ? 19.145  30.362  10.153  1.00 58.11 ? 281 GLY C N     1 
ATOM   1942  C CA    . GLY A  1 281 ? 20.119  29.324  9.926   1.00 57.38 ? 281 GLY C CA    1 
ATOM   1943  C C     . GLY A  1 281 ? 20.148  28.865  8.486   1.00 69.09 ? 281 GLY C C     1 
ATOM   1944  O O     . GLY A  1 281 ? 19.203  29.093  7.719   1.00 61.84 ? 281 GLY C O     1 
ATOM   1945  N N     . SER A  1 282 ? 21.257  28.197  8.129   1.00 75.15 ? 282 SER C N     1 
ATOM   1946  C CA    . SER A  1 282 ? 21.474  27.655  6.787   1.00 64.57 ? 282 SER C CA    1 
ATOM   1947  C C     . SER A  1 282 ? 20.487  26.549  6.432   1.00 66.08 ? 282 SER C C     1 
ATOM   1948  O O     . SER A  1 282 ? 20.494  26.071  5.284   1.00 60.68 ? 282 SER C O     1 
ATOM   1949  C CB    . SER A  1 282 ? 22.907  27.141  6.651   1.00 62.67 ? 282 SER C CB    1 
ATOM   1950  O OG    . SER A  1 282 ? 23.178  26.774  5.310   1.00 72.82 ? 282 SER C OG    1 
ATOM   1951  N N     . GLY A  1 283 ? 19.666  26.125  7.391   1.00 61.14 ? 283 GLY C N     1 
ATOM   1952  C CA    . GLY A  1 283 ? 18.446  25.421  7.058   1.00 54.44 ? 283 GLY C CA    1 
ATOM   1953  C C     . GLY A  1 283 ? 17.478  26.344  6.338   1.00 51.09 ? 283 GLY C C     1 
ATOM   1954  O O     . GLY A  1 283 ? 17.389  27.541  6.618   1.00 42.04 ? 283 GLY C O     1 
ATOM   1955  N N     . GLY A  1 284 ? 16.770  25.776  5.372   1.00 53.42 ? 284 GLY C N     1 
ATOM   1956  C CA    . GLY A  1 284 ? 15.790  26.534  4.627   1.00 45.86 ? 284 GLY C CA    1 
ATOM   1957  C C     . GLY A  1 284 ? 14.354  26.300  5.054   1.00 44.07 ? 284 GLY C C     1 
ATOM   1958  O O     . GLY A  1 284 ? 13.665  27.265  5.400   1.00 42.74 ? 284 GLY C O     1 
ATOM   1959  N N     . SER A  1 285 ? 13.902  25.042  5.059   1.00 41.56 ? 285 SER C N     1 
ATOM   1960  C CA    . SER A  1 285 ? 12.481  24.724  5.235   1.00 41.08 ? 285 SER C CA    1 
ATOM   1961  C C     . SER A  1 285 ? 11.949  25.148  6.599   1.00 39.59 ? 285 SER C C     1 
ATOM   1962  O O     . SER A  1 285 ? 12.520  24.808  7.641   1.00 39.59 ? 285 SER C O     1 
ATOM   1963  C CB    . SER A  1 285 ? 12.243  23.219  5.056   1.00 40.84 ? 285 SER C CB    1 
ATOM   1964  O OG    . SER A  1 285 ? 12.143  22.853  3.692   1.00 37.68 ? 285 SER C OG    1 
ATOM   1965  N N     . ALA A  1 286 ? 10.823  25.860  6.584   1.00 40.16 ? 286 ALA C N     1 
ATOM   1966  C CA    . ALA A  1 286 ? 10.108  26.240  7.795   1.00 38.83 ? 286 ALA C CA    1 
ATOM   1967  C C     . ALA A  1 286 ? 8.860   25.384  7.899   1.00 38.03 ? 286 ALA C C     1 
ATOM   1968  O O     . ALA A  1 286 ? 7.972   25.478  7.053   1.00 44.30 ? 286 ALA C O     1 
ATOM   1969  C CB    . ALA A  1 286 ? 9.742   27.724  7.799   1.00 37.73 ? 286 ALA C CB    1 
ATOM   1970  N N     . LYS A  1 287 ? 8.803   24.542  8.918   1.00 41.18 ? 287 LYS C N     1 
ATOM   1971  C CA    . LYS A  1 287 ? 7.649   23.682  9.117   1.00 40.55 ? 287 LYS C CA    1 
ATOM   1972  C C     . LYS A  1 287 ? 6.426   24.513  9.455   1.00 40.71 ? 287 LYS C C     1 
ATOM   1973  O O     . LYS A  1 287 ? 6.528   25.655  9.899   1.00 41.67 ? 287 LYS C O     1 
ATOM   1974  C CB    . LYS A  1 287 ? 7.902   22.690  10.248  1.00 44.39 ? 287 LYS C CB    1 
ATOM   1975  C CG    . LYS A  1 287 ? 7.189   21.357  10.083  1.00 53.70 ? 287 LYS C CG    1 
ATOM   1976  C CD    . LYS A  1 287 ? 7.967   20.225  10.768  1.00 57.96 ? 287 LYS C CD    1 
ATOM   1977  C CE    . LYS A  1 287 ? 7.178   18.906  10.788  1.00 63.97 ? 287 LYS C CE    1 
ATOM   1978  N NZ    . LYS A  1 287 ? 7.118   18.251  9.441   1.00 70.27 ? 287 LYS C NZ    1 
ATOM   1979  N N     . TRP A  1 288 ? 5.256   23.912  9.273   1.00 43.61 ? 288 TRP C N     1 
ATOM   1980  C CA    . TRP A  1 288 ? 4.000   24.599  9.534   1.00 41.64 ? 288 TRP C CA    1 
ATOM   1981  C C     . TRP A  1 288 ? 3.540   24.324  10.952  1.00 38.37 ? 288 TRP C C     1 
ATOM   1982  O O     . TRP A  1 288 ? 3.398   23.166  11.357  1.00 41.52 ? 288 TRP C O     1 
ATOM   1983  C CB    . TRP A  1 288 ? 2.908   24.174  8.564   1.00 41.82 ? 288 TRP C CB    1 
ATOM   1984  C CG    . TRP A  1 288 ? 1.563   24.627  9.028   1.00 34.84 ? 288 TRP C CG    1 
ATOM   1985  C CD1   . TRP A  1 288 ? 1.119   25.912  9.133   1.00 35.77 ? 288 TRP C CD1   1 
ATOM   1986  C CD2   . TRP A  1 288 ? 0.492   23.795  9.454   1.00 37.56 ? 288 TRP C CD2   1 
ATOM   1987  N NE1   . TRP A  1 288 ? -0.176  25.934  9.594   1.00 34.53 ? 288 TRP C NE1   1 
ATOM   1988  C CE2   . TRP A  1 288 ? -0.588  24.645  9.793   1.00 35.44 ? 288 TRP C CE2   1 
ATOM   1989  C CE3   . TRP A  1 288 ? 0.331   22.411  9.575   1.00 35.67 ? 288 TRP C CE3   1 
ATOM   1990  C CZ2   . TRP A  1 288 ? -1.806  24.155  10.247  1.00 36.08 ? 288 TRP C CZ2   1 
ATOM   1991  C CZ3   . TRP A  1 288 ? -0.879  21.927  10.027  1.00 37.23 ? 288 TRP C CZ3   1 
ATOM   1992  C CH2   . TRP A  1 288 ? -1.935  22.797  10.357  1.00 35.96 ? 288 TRP C CH2   1 
ATOM   1993  N N     . ILE A  1 289 ? 3.270   25.393  11.686  1.00 34.32 ? 289 ILE C N     1 
ATOM   1994  C CA    . ILE A  1 289 ? 3.136   25.299  13.127  1.00 34.73 ? 289 ILE C CA    1 
ATOM   1995  C C     . ILE A  1 289 ? 1.792   25.775  13.630  1.00 37.59 ? 289 ILE C C     1 
ATOM   1996  O O     . ILE A  1 289 ? 1.464   25.502  14.793  1.00 38.77 ? 289 ILE C O     1 
ATOM   1997  C CB    . ILE A  1 289 ? 4.257   26.084  13.826  1.00 34.47 ? 289 ILE C CB    1 
ATOM   1998  C CG1   . ILE A  1 289 ? 3.833   27.539  13.997  1.00 36.99 ? 289 ILE C CG1   1 
ATOM   1999  C CG2   . ILE A  1 289 ? 5.517   26.003  13.003  1.00 37.53 ? 289 ILE C CG2   1 
ATOM   2000  C CD1   . ILE A  1 289 ? 4.748   28.314  14.891  1.00 31.47 ? 289 ILE C CD1   1 
ATOM   2001  N N     . GLY A  1 290 ? 1.007   26.491  12.834  1.00 38.18 ? 290 GLY C N     1 
ATOM   2002  C CA    . GLY A  1 290 ? -0.280  26.922  13.324  1.00 33.65 ? 290 GLY C CA    1 
ATOM   2003  C C     . GLY A  1 290 ? -1.001  27.813  12.335  1.00 36.60 ? 290 GLY C C     1 
ATOM   2004  O O     . GLY A  1 290 ? -0.582  27.998  11.190  1.00 34.71 ? 290 GLY C O     1 
ATOM   2005  N N     . LEU A  1 291 ? -2.078  28.401  12.852  1.00 38.58 ? 291 LEU C N     1 
ATOM   2006  C CA    . LEU A  1 291 ? -3.155  28.980  12.067  1.00 32.23 ? 291 LEU C CA    1 
ATOM   2007  C C     . LEU A  1 291 ? -3.827  30.056  12.898  1.00 34.74 ? 291 LEU C C     1 
ATOM   2008  O O     . LEU A  1 291 ? -4.315  29.763  13.997  1.00 33.20 ? 291 LEU C O     1 
ATOM   2009  C CB    . LEU A  1 291 ? -4.161  27.902  11.702  1.00 29.98 ? 291 LEU C CB    1 
ATOM   2010  C CG    . LEU A  1 291 ? -4.675  28.017  10.285  1.00 30.78 ? 291 LEU C CG    1 
ATOM   2011  C CD1   . LEU A  1 291 ? -3.503  27.832  9.325   1.00 35.77 ? 291 LEU C CD1   1 
ATOM   2012  C CD2   . LEU A  1 291 ? -5.741  27.000  10.041  1.00 22.82 ? 291 LEU C CD2   1 
ATOM   2013  N N     . ASP A  1 292 ? -3.839  31.288  12.387  1.00 34.64 ? 292 ASP C N     1 
ATOM   2014  C CA    . ASP A  1 292 ? -4.506  32.429  13.020  1.00 37.05 ? 292 ASP C CA    1 
ATOM   2015  C C     . ASP A  1 292 ? -5.640  32.857  12.109  1.00 38.16 ? 292 ASP C C     1 
ATOM   2016  O O     . ASP A  1 292 ? -5.421  32.989  10.900  1.00 41.24 ? 292 ASP C O     1 
ATOM   2017  C CB    . ASP A  1 292 ? -3.542  33.599  13.224  1.00 39.17 ? 292 ASP C CB    1 
ATOM   2018  C CG    . ASP A  1 292 ? -2.366  33.252  14.136  1.00 38.95 ? 292 ASP C CG    1 
ATOM   2019  O OD1   . ASP A  1 292 ? -2.050  32.052  14.267  1.00 43.27 ? 292 ASP C OD1   1 
ATOM   2020  O OD2   . ASP A  1 292 ? -1.734  34.180  14.696  1.00 39.64 ? 292 ASP C OD2   1 
ATOM   2021  N N     . SER A  1 293 ? -6.859  33.059  12.663  1.00 38.20 ? 293 SER C N     1 
ATOM   2022  C CA    . SER A  1 293 ? -7.919  33.116  11.649  1.00 41.46 ? 293 SER C CA    1 
ATOM   2023  C C     . SER A  1 293 ? -8.294  34.493  11.163  1.00 45.52 ? 293 SER C C     1 
ATOM   2024  O O     . SER A  1 293 ? -7.931  34.825  10.030  1.00 50.53 ? 293 SER C O     1 
ATOM   2025  C CB    . SER A  1 293 ? -9.213  32.466  12.066  1.00 39.29 ? 293 SER C CB    1 
ATOM   2026  O OG    . SER A  1 293 ? -10.050 32.341  10.926  1.00 33.51 ? 293 SER C OG    1 
ATOM   2027  N N     . PRO A  1 294 ? -9.066  35.305  11.925  1.00 40.69 ? 294 PRO C N     1 
ATOM   2028  C CA    . PRO A  1 294 ? -9.527  36.573  11.332  1.00 38.46 ? 294 PRO C CA    1 
ATOM   2029  C C     . PRO A  1 294 ? -8.317  37.227  10.680  1.00 46.12 ? 294 PRO C C     1 
ATOM   2030  O O     . PRO A  1 294 ? -7.500  37.865  11.348  1.00 53.19 ? 294 PRO C O     1 
ATOM   2031  C CB    . PRO A  1 294 ? -10.055 37.382  12.522  1.00 39.40 ? 294 PRO C CB    1 
ATOM   2032  C CG    . PRO A  1 294 ? -9.864  36.500  13.745  1.00 44.68 ? 294 PRO C CG    1 
ATOM   2033  C CD    . PRO A  1 294 ? -8.908  35.410  13.387  1.00 37.89 ? 294 PRO C CD    1 
ATOM   2034  N N     . SER A  1 295 ? -8.136  36.941  9.396   1.00 39.30 ? 295 SER C N     1 
ATOM   2035  C CA    . SER A  1 295 ? -6.880  37.248  8.728   1.00 42.02 ? 295 SER C CA    1 
ATOM   2036  C C     . SER A  1 295 ? -6.818  38.716  8.364   1.00 42.04 ? 295 SER C C     1 
ATOM   2037  O O     . SER A  1 295 ? -7.835  39.419  8.313   1.00 42.77 ? 295 SER C O     1 
ATOM   2038  C CB    . SER A  1 295 ? -6.714  36.370  7.486   1.00 36.61 ? 295 SER C CB    1 
ATOM   2039  O OG    . SER A  1 295 ? -6.580  37.153  6.316   1.00 37.07 ? 295 SER C OG    1 
ATOM   2040  N N     . ARG A  1 296 ? -5.610  39.184  8.109   1.00 41.66 ? 296 ARG C N     1 
ATOM   2041  C CA    . ARG A  1 296 ? -5.417  40.573  7.724   1.00 41.44 ? 296 ARG C CA    1 
ATOM   2042  C C     . ARG A  1 296 ? -5.076  40.672  6.242   1.00 37.27 ? 296 ARG C C     1 
ATOM   2043  O O     . ARG A  1 296 ? -4.238  41.471  5.833   1.00 45.48 ? 296 ARG C O     1 
ATOM   2044  C CB    . ARG A  1 296 ? -4.359  41.231  8.607   1.00 42.31 ? 296 ARG C CB    1 
ATOM   2045  C CG    . ARG A  1 296 ? -4.957  42.024  9.771   1.00 48.81 ? 296 ARG C CG    1 
ATOM   2046  C CD    . ARG A  1 296 ? -6.036  41.229  10.515  1.00 50.71 ? 296 ARG C CD    1 
ATOM   2047  N NE    . ARG A  1 296 ? -5.480  40.155  11.330  1.00 54.51 ? 296 ARG C NE    1 
ATOM   2048  C CZ    . ARG A  1 296 ? -5.304  40.217  12.644  1.00 57.48 ? 296 ARG C CZ    1 
ATOM   2049  N NH1   . ARG A  1 296 ? -5.654  41.287  13.339  1.00 58.99 ? 296 ARG C NH1   1 
ATOM   2050  N NH2   . ARG A  1 296 ? -4.759  39.181  13.276  1.00 58.55 ? 296 ARG C NH2   1 
ATOM   2051  N N     . SER A  1 297 ? -5.768  39.878  5.415   1.00 32.18 ? 297 SER C N     1 
ATOM   2052  C CA    . SER A  1 297 ? -5.503  39.815  3.978   1.00 35.19 ? 297 SER C CA    1 
ATOM   2053  C C     . SER A  1 297 ? -6.797  39.815  3.132   1.00 40.11 ? 297 SER C C     1 
ATOM   2054  O O     . SER A  1 297 ? -6.825  39.265  2.022   1.00 35.57 ? 297 SER C O     1 
ATOM   2055  C CB    . SER A  1 297 ? -4.668  38.578  3.655   1.00 31.56 ? 297 SER C CB    1 
ATOM   2056  O OG    . SER A  1 297 ? -3.535  38.492  4.499   1.00 38.94 ? 297 SER C OG    1 
ATOM   2057  N N     . GLU A  1 298 ? -7.872  40.426  3.625   1.00 39.66 ? 298 GLU C N     1 
ATOM   2058  C CA    . GLU A  1 298 ? -9.171  40.391  2.955   1.00 32.35 ? 298 GLU C CA    1 
ATOM   2059  C C     . GLU A  1 298 ? -9.437  41.779  2.387   1.00 34.97 ? 298 GLU C C     1 
ATOM   2060  O O     . GLU A  1 298 ? -9.930  42.663  3.084   1.00 36.85 ? 298 GLU C O     1 
ATOM   2061  C CB    . GLU A  1 298 ? -10.291 39.965  3.918   1.00 35.05 ? 298 GLU C CB    1 
ATOM   2062  C CG    . GLU A  1 298 ? -10.363 38.461  4.226   1.00 34.05 ? 298 GLU C CG    1 
ATOM   2063  C CD    . GLU A  1 298 ? -11.432 38.106  5.271   1.00 39.48 ? 298 GLU C CD    1 
ATOM   2064  O OE1   . GLU A  1 298 ? -12.632 38.132  4.922   1.00 38.72 ? 298 GLU C OE1   1 
ATOM   2065  O OE2   . GLU A  1 298 ? -11.076 37.807  6.439   1.00 28.17 ? 298 GLU C OE2   1 
ATOM   2066  N N     . PHE A  1 299 ? -9.104  41.968  1.117   1.00 35.24 ? 299 PHE C N     1 
ATOM   2067  C CA    . PHE A  1 299 ? -9.424  43.196  0.411   1.00 32.77 ? 299 PHE C CA    1 
ATOM   2068  C C     . PHE A  1 299 ? -9.732  42.830  -1.033  1.00 34.46 ? 299 PHE C C     1 
ATOM   2069  O O     . PHE A  1 299 ? -9.905  41.652  -1.365  1.00 33.39 ? 299 PHE C O     1 
ATOM   2070  C CB    . PHE A  1 299 ? -8.279  44.208  0.520   1.00 31.52 ? 299 PHE C CB    1 
ATOM   2071  C CG    . PHE A  1 299 ? -6.926  43.577  0.557   1.00 39.79 ? 299 PHE C CG    1 
ATOM   2072  C CD1   . PHE A  1 299 ? -6.272  43.239  -0.626  1.00 40.37 ? 299 PHE C CD1   1 
ATOM   2073  C CD2   . PHE A  1 299 ? -6.301  43.310  1.770   1.00 41.28 ? 299 PHE C CD2   1 
ATOM   2074  C CE1   . PHE A  1 299 ? -5.018  42.657  -0.605  1.00 40.02 ? 299 PHE C CE1   1 
ATOM   2075  C CE2   . PHE A  1 299 ? -5.039  42.720  1.798   1.00 41.35 ? 299 PHE C CE2   1 
ATOM   2076  C CZ    . PHE A  1 299 ? -4.400  42.391  0.605   1.00 40.83 ? 299 PHE C CZ    1 
ATOM   2077  N N     . GLU A  1 300 ? -9.755  43.850  -1.897  1.00 36.70 ? 300 GLU C N     1 
ATOM   2078  C CA    . GLU A  1 300 ? -10.187 43.669  -3.282  1.00 38.94 ? 300 GLU C CA    1 
ATOM   2079  C C     . GLU A  1 300 ? -9.315  42.663  -4.016  1.00 36.40 ? 300 GLU C C     1 
ATOM   2080  O O     . GLU A  1 300 ? -9.828  41.764  -4.699  1.00 37.27 ? 300 GLU C O     1 
ATOM   2081  C CB    . GLU A  1 300 ? -10.171 45.016  -4.016  1.00 43.56 ? 300 GLU C CB    1 
ATOM   2082  C CG    . GLU A  1 300 ? -8.862  45.835  -3.901  1.00 45.20 ? 300 GLU C CG    1 
ATOM   2083  C CD    . GLU A  1 300 ? -8.231  46.182  -5.268  1.00 56.79 ? 300 GLU C CD    1 
ATOM   2084  O OE1   . GLU A  1 300 ? -8.555  45.515  -6.287  1.00 54.96 ? 300 GLU C OE1   1 
ATOM   2085  O OE2   . GLU A  1 300 ? -7.426  47.148  -5.327  1.00 54.10 ? 300 GLU C OE2   1 
ATOM   2086  N N     . ALA A  1 301 ? -7.996  42.800  -3.881  1.00 37.96 ? 301 ALA C N     1 
ATOM   2087  C CA    . ALA A  1 301 ? -7.038  42.057  -4.690  1.00 37.70 ? 301 ALA C CA    1 
ATOM   2088  C C     . ALA A  1 301 ? -6.930  40.592  -4.296  1.00 36.58 ? 301 ALA C C     1 
ATOM   2089  O O     . ALA A  1 301 ? -6.471  39.781  -5.107  1.00 34.64 ? 301 ALA C O     1 
ATOM   2090  C CB    . ALA A  1 301 ? -5.654  42.708  -4.595  1.00 38.24 ? 301 ALA C CB    1 
ATOM   2091  N N     . THR A  1 302 ? -7.311  40.232  -3.073  1.00 29.99 ? 302 THR C N     1 
ATOM   2092  C CA    . THR A  1 302 ? -7.321  38.824  -2.730  1.00 32.03 ? 302 THR C CA    1 
ATOM   2093  C C     . THR A  1 302 ? -8.717  38.234  -2.850  1.00 31.58 ? 302 THR C C     1 
ATOM   2094  O O     . THR A  1 302 ? -8.900  37.162  -3.432  1.00 32.55 ? 302 THR C O     1 
ATOM   2095  C CB    . THR A  1 302 ? -6.745  38.598  -1.319  1.00 36.25 ? 302 THR C CB    1 
ATOM   2096  O OG1   . THR A  1 302 ? -7.655  39.074  -0.312  1.00 35.90 ? 302 THR C OG1   1 
ATOM   2097  C CG2   . THR A  1 302 ? -5.423  39.319  -1.192  1.00 35.20 ? 302 THR C CG2   1 
ATOM   2098  N N     . LEU A  1 303 ? -9.715  38.932  -2.338  1.00 33.54 ? 303 LEU C N     1 
ATOM   2099  C CA    . LEU A  1 303 ? -11.060 38.386  -2.328  1.00 32.12 ? 303 LEU C CA    1 
ATOM   2100  C C     . LEU A  1 303 ? -11.557 38.198  -3.745  1.00 27.53 ? 303 LEU C C     1 
ATOM   2101  O O     . LEU A  1 303 ? -11.672 37.065  -4.203  1.00 34.72 ? 303 LEU C O     1 
ATOM   2102  C CB    . LEU A  1 303 ? -11.971 39.309  -1.531  1.00 31.97 ? 303 LEU C CB    1 
ATOM   2103  C CG    . LEU A  1 303 ? -11.584 39.340  -0.054  1.00 35.28 ? 303 LEU C CG    1 
ATOM   2104  C CD1   . LEU A  1 303 ? -12.242 40.518  0.646   1.00 33.91 ? 303 LEU C CD1   1 
ATOM   2105  C CD2   . LEU A  1 303 ? -11.970 38.009  0.623   1.00 28.35 ? 303 LEU C CD2   1 
ATOM   2106  N N     . LYS A  1 304 ? -11.784 39.293  -4.469  1.00 26.63 ? 304 LYS C N     1 
ATOM   2107  C CA    . LYS A  1 304 ? -12.499 39.202  -5.743  1.00 32.94 ? 304 LYS C CA    1 
ATOM   2108  C C     . LYS A  1 304 ? -11.891 38.220  -6.739  1.00 28.22 ? 304 LYS C C     1 
ATOM   2109  O O     . LYS A  1 304 ? -12.649 37.440  -7.340  1.00 29.69 ? 304 LYS C O     1 
ATOM   2110  C CB    . LYS A  1 304 ? -12.637 40.609  -6.341  1.00 35.75 ? 304 LYS C CB    1 
ATOM   2111  C CG    . LYS A  1 304 ? -13.687 41.469  -5.612  1.00 36.94 ? 304 LYS C CG    1 
ATOM   2112  C CD    . LYS A  1 304 ? -14.930 40.640  -5.223  1.00 36.98 ? 304 LYS C CD    1 
ATOM   2113  C CE    . LYS A  1 304 ? -16.116 41.516  -4.839  1.00 37.29 ? 304 LYS C CE    1 
ATOM   2114  N NZ    . LYS A  1 304 ? -16.021 42.832  -5.541  1.00 40.16 ? 304 LYS C NZ    1 
ATOM   2115  N N     . PRO A  1 305 ? -10.580 38.200  -6.986  1.00 27.55 ? 305 PRO C N     1 
ATOM   2116  C CA    . PRO A  1 305 ? -10.046 37.175  -7.892  1.00 26.20 ? 305 PRO C CA    1 
ATOM   2117  C C     . PRO A  1 305 ? -10.396 35.771  -7.424  1.00 32.60 ? 305 PRO C C     1 
ATOM   2118  O O     . PRO A  1 305 ? -11.001 34.984  -8.172  1.00 31.64 ? 305 PRO C O     1 
ATOM   2119  C CB    . PRO A  1 305 ? -8.534  37.406  -7.848  1.00 27.62 ? 305 PRO C CB    1 
ATOM   2120  C CG    . PRO A  1 305 ? -8.351  38.738  -7.293  1.00 29.89 ? 305 PRO C CG    1 
ATOM   2121  C CD    . PRO A  1 305 ? -9.521  39.078  -6.460  1.00 31.98 ? 305 PRO C CD    1 
ATOM   2122  N N     . ALA A  1 306 ? -10.009 35.465  -6.177  1.00 30.48 ? 306 ALA C N     1 
ATOM   2123  C CA    . ALA A  1 306 ? -10.387 34.206  -5.537  1.00 29.77 ? 306 ALA C CA    1 
ATOM   2124  C C     . ALA A  1 306 ? -11.865 33.906  -5.726  1.00 27.48 ? 306 ALA C C     1 
ATOM   2125  O O     . ALA A  1 306 ? -12.243 32.801  -6.134  1.00 26.73 ? 306 ALA C O     1 
ATOM   2126  C CB    . ALA A  1 306 ? -10.060 34.271  -4.051  1.00 30.39 ? 306 ALA C CB    1 
ATOM   2127  N N     . GLU A  1 307 ? -12.713 34.893  -5.432  1.00 25.83 ? 307 GLU C N     1 
ATOM   2128  C CA    . GLU A  1 307 ? -14.138 34.799  -5.722  1.00 33.94 ? 307 GLU C CA    1 
ATOM   2129  C C     . GLU A  1 307 ? -14.372 34.265  -7.125  1.00 25.60 ? 307 GLU C C     1 
ATOM   2130  O O     . GLU A  1 307 ? -14.977 33.204  -7.313  1.00 24.42 ? 307 GLU C O     1 
ATOM   2131  C CB    . GLU A  1 307 ? -14.795 36.174  -5.561  1.00 36.46 ? 307 GLU C CB    1 
ATOM   2132  C CG    . GLU A  1 307 ? -16.199 36.151  -4.981  1.00 40.69 ? 307 GLU C CG    1 
ATOM   2133  C CD    . GLU A  1 307 ? -16.649 37.518  -4.466  1.00 50.53 ? 307 GLU C CD    1 
ATOM   2134  O OE1   . GLU A  1 307 ? -17.050 38.353  -5.307  1.00 54.07 ? 307 GLU C OE1   1 
ATOM   2135  O OE2   . GLU A  1 307 ? -16.610 37.761  -3.231  1.00 46.81 ? 307 GLU C OE2   1 
ATOM   2136  N N     . GLU A  1 308 ? -13.862 34.976  -8.122  1.00 26.46 ? 308 GLU C N     1 
ATOM   2137  C CA    . GLU A  1 308 ? -14.067 34.562  -9.502  1.00 28.90 ? 308 GLU C CA    1 
ATOM   2138  C C     . GLU A  1 308 ? -13.614 33.117  -9.716  1.00 28.97 ? 308 GLU C C     1 
ATOM   2139  O O     . GLU A  1 308 ? -14.326 32.309  -10.324 1.00 21.99 ? 308 GLU C O     1 
ATOM   2140  C CB    . GLU A  1 308 ? -13.335 35.524  -10.437 1.00 28.30 ? 308 GLU C CB    1 
ATOM   2141  C CG    . GLU A  1 308 ? -14.104 35.837  -11.700 1.00 35.46 ? 308 GLU C CG    1 
ATOM   2142  C CD    . GLU A  1 308 ? -13.215 36.424  -12.760 1.00 37.39 ? 308 GLU C CD    1 
ATOM   2143  O OE1   . GLU A  1 308 ? -12.030 36.031  -12.789 1.00 35.97 ? 308 GLU C OE1   1 
ATOM   2144  O OE2   . GLU A  1 308 ? -13.691 37.258  -13.564 1.00 44.72 ? 308 GLU C OE2   1 
ATOM   2145  N N     . PHE A  1 309 ? -12.450 32.760  -9.166  1.00 27.75 ? 309 PHE C N     1 
ATOM   2146  C CA    . PHE A  1 309 ? -11.932 31.415  -9.391  1.00 28.69 ? 309 PHE C CA    1 
ATOM   2147  C C     . PHE A  1 309 ? -12.822 30.360  -8.763  1.00 27.90 ? 309 PHE C C     1 
ATOM   2148  O O     . PHE A  1 309 ? -13.013 29.281  -9.336  1.00 30.38 ? 309 PHE C O     1 
ATOM   2149  C CB    . PHE A  1 309 ? -10.512 31.295  -8.841  1.00 33.16 ? 309 PHE C CB    1 
ATOM   2150  C CG    . PHE A  1 309 ? -9.810  30.044  -9.270  1.00 34.45 ? 309 PHE C CG    1 
ATOM   2151  C CD1   . PHE A  1 309 ? -10.011 28.850  -8.593  1.00 35.02 ? 309 PHE C CD1   1 
ATOM   2152  C CD2   . PHE A  1 309 ? -8.959  30.054  -10.373 1.00 34.71 ? 309 PHE C CD2   1 
ATOM   2153  C CE1   . PHE A  1 309 ? -9.355  27.690  -9.002  1.00 33.69 ? 309 PHE C CE1   1 
ATOM   2154  C CE2   . PHE A  1 309 ? -8.303  28.901  -10.783 1.00 30.85 ? 309 PHE C CE2   1 
ATOM   2155  C CZ    . PHE A  1 309 ? -8.506  27.719  -10.100 1.00 33.67 ? 309 PHE C CZ    1 
ATOM   2156  N N     . ILE A  1 310 ? -13.371 30.658  -7.587  1.00 31.48 ? 310 ILE C N     1 
ATOM   2157  C CA    . ILE A  1 310 ? -14.140 29.676  -6.834  1.00 29.79 ? 310 ILE C CA    1 
ATOM   2158  C C     . ILE A  1 310 ? -15.497 29.432  -7.483  1.00 27.72 ? 310 ILE C C     1 
ATOM   2159  O O     . ILE A  1 310 ? -16.016 28.308  -7.495  1.00 23.54 ? 310 ILE C O     1 
ATOM   2160  C CB    . ILE A  1 310 ? -14.270 30.172  -5.384  1.00 30.85 ? 310 ILE C CB    1 
ATOM   2161  C CG1   . ILE A  1 310 ? -13.051 29.719  -4.586  1.00 27.33 ? 310 ILE C CG1   1 
ATOM   2162  C CG2   . ILE A  1 310 ? -15.565 29.715  -4.761  1.00 31.69 ? 310 ILE C CG2   1 
ATOM   2163  C CD1   . ILE A  1 310 ? -12.708 28.280  -4.815  1.00 27.12 ? 310 ILE C CD1   1 
ATOM   2164  N N     . GLU A  1 311 ? -16.084 30.482  -8.043  1.00 30.43 ? 311 GLU C N     1 
ATOM   2165  C CA    . GLU A  1 311 ? -17.358 30.349  -8.729  1.00 34.51 ? 311 GLU C CA    1 
ATOM   2166  C C     . GLU A  1 311 ? -17.247 29.403  -9.915  1.00 29.99 ? 311 GLU C C     1 
ATOM   2167  O O     . GLU A  1 311 ? -18.108 28.540  -10.131 1.00 30.16 ? 311 GLU C O     1 
ATOM   2168  C CB    . GLU A  1 311 ? -17.822 31.725  -9.191  1.00 38.75 ? 311 GLU C CB    1 
ATOM   2169  C CG    . GLU A  1 311 ? -19.254 31.746  -9.549  1.00 41.01 ? 311 GLU C CG    1 
ATOM   2170  C CD    . GLU A  1 311 ? -20.110 31.254  -8.414  1.00 44.51 ? 311 GLU C CD    1 
ATOM   2171  O OE1   . GLU A  1 311 ? -19.985 31.833  -7.308  1.00 36.50 ? 311 GLU C OE1   1 
ATOM   2172  O OE2   . GLU A  1 311 ? -20.898 30.301  -8.640  1.00 50.22 ? 311 GLU C OE2   1 
ATOM   2173  N N     . MET A  1 312 ? -16.197 29.564  -10.706 1.00 28.96 ? 312 MET C N     1 
ATOM   2174  C CA    . MET A  1 312 ? -16.016 28.680  -11.847 1.00 29.80 ? 312 MET C CA    1 
ATOM   2175  C C     . MET A  1 312 ? -15.899 27.235  -11.395 1.00 32.86 ? 312 MET C C     1 
ATOM   2176  O O     . MET A  1 312 ? -16.512 26.342  -11.986 1.00 35.76 ? 312 MET C O     1 
ATOM   2177  C CB    . MET A  1 312 ? -14.786 29.105  -12.648 1.00 27.67 ? 312 MET C CB    1 
ATOM   2178  C CG    . MET A  1 312 ? -14.112 27.994  -13.427 1.00 31.76 ? 312 MET C CG    1 
ATOM   2179  S SD    . MET A  1 312 ? -12.442 28.478  -13.922 1.00 56.49 ? 312 MET C SD    1 
ATOM   2180  C CE    . MET A  1 312 ? -11.468 27.965  -12.492 1.00 32.94 ? 312 MET C CE    1 
ATOM   2181  N N     . ILE A  1 313 ? -15.138 26.966  -10.333 1.00 32.01 ? 313 ILE C N     1 
ATOM   2182  C CA    . ILE A  1 313 ? -15.097 25.568  -9.932  1.00 32.96 ? 313 ILE C CA    1 
ATOM   2183  C C     . ILE A  1 313 ? -16.455 25.121  -9.368  1.00 34.43 ? 313 ILE C C     1 
ATOM   2184  O O     . ILE A  1 313 ? -16.735 23.911  -9.302  1.00 32.95 ? 313 ILE C O     1 
ATOM   2185  C CB    . ILE A  1 313 ? -13.911 25.301  -8.976  1.00 35.11 ? 313 ILE C CB    1 
ATOM   2186  C CG1   . ILE A  1 313 ? -14.222 25.745  -7.579  1.00 29.48 ? 313 ILE C CG1   1 
ATOM   2187  C CG2   . ILE A  1 313 ? -12.608 25.911  -9.476  1.00 33.01 ? 313 ILE C CG2   1 
ATOM   2188  C CD1   . ILE A  1 313 ? -14.673 24.588  -6.753  1.00 32.75 ? 313 ILE C CD1   1 
ATOM   2189  N N     . ARG A  1 314 ? -17.319 26.062  -8.961  1.00 33.79 ? 314 ARG C N     1 
ATOM   2190  C CA    . ARG A  1 314 ? -18.709 25.693  -8.699  1.00 31.91 ? 314 ARG C CA    1 
ATOM   2191  C C     . ARG A  1 314 ? -19.451 25.435  -10.009 1.00 34.98 ? 314 ARG C C     1 
ATOM   2192  O O     . ARG A  1 314 ? -20.265 24.505  -10.095 1.00 31.09 ? 314 ARG C O     1 
ATOM   2193  C CB    . ARG A  1 314 ? -19.421 26.774  -7.876  1.00 30.05 ? 314 ARG C CB    1 
ATOM   2194  C CG    . ARG A  1 314 ? -20.826 26.328  -7.393  1.00 35.71 ? 314 ARG C CG    1 
ATOM   2195  C CD    . ARG A  1 314 ? -21.549 27.330  -6.472  1.00 36.57 ? 314 ARG C CD    1 
ATOM   2196  N NE    . ARG A  1 314 ? -22.028 28.531  -7.153  1.00 40.17 ? 314 ARG C NE    1 
ATOM   2197  C CZ    . ARG A  1 314 ? -23.262 28.701  -7.616  1.00 38.87 ? 314 ARG C CZ    1 
ATOM   2198  N NH1   . ARG A  1 314 ? -24.180 27.755  -7.516  1.00 30.55 ? 314 ARG C NH1   1 
ATOM   2199  N NH2   . ARG A  1 314 ? -23.593 29.863  -8.179  1.00 38.42 ? 314 ARG C NH2   1 
ATOM   2200  N N     . THR A  1 315 ? -19.180 26.254  -11.034 1.00 30.24 ? 315 THR C N     1 
ATOM   2201  C CA    . THR A  1 315 ? -19.637 25.966  -12.394 1.00 27.06 ? 315 THR C CA    1 
ATOM   2202  C C     . THR A  1 315 ? -19.240 24.558  -12.820 1.00 28.78 ? 315 THR C C     1 
ATOM   2203  O O     . THR A  1 315 ? -20.095 23.773  -13.247 1.00 29.72 ? 315 THR C O     1 
ATOM   2204  C CB    . THR A  1 315 ? -19.056 26.976  -13.391 1.00 26.50 ? 315 THR C CB    1 
ATOM   2205  O OG1   . THR A  1 315 ? -19.209 28.315  -12.896 1.00 31.49 ? 315 THR C OG1   1 
ATOM   2206  C CG2   . THR A  1 315 ? -19.731 26.857  -14.734 1.00 33.59 ? 315 THR C CG2   1 
ATOM   2207  N N     . ILE A  1 316 ? -17.944 24.216  -12.725 1.00 26.12 ? 316 ILE C N     1 
ATOM   2208  C CA    . ILE A  1 316 ? -17.534 22.867  -13.118 1.00 26.19 ? 316 ILE C CA    1 
ATOM   2209  C C     . ILE A  1 316 ? -18.186 21.833  -12.207 1.00 30.18 ? 316 ILE C C     1 
ATOM   2210  O O     . ILE A  1 316 ? -18.481 20.717  -12.637 1.00 32.04 ? 316 ILE C O     1 
ATOM   2211  C CB    . ILE A  1 316 ? -15.997 22.714  -13.176 1.00 23.71 ? 316 ILE C CB    1 
ATOM   2212  C CG1   . ILE A  1 316 ? -15.419 22.511  -11.789 1.00 36.16 ? 316 ILE C CG1   1 
ATOM   2213  C CG2   . ILE A  1 316 ? -15.322 23.923  -13.822 1.00 24.52 ? 316 ILE C CG2   1 
ATOM   2214  C CD1   . ILE A  1 316 ? -13.915 22.722  -11.731 1.00 39.59 ? 316 ILE C CD1   1 
ATOM   2215  N N     . GLY A  1 317 ? -18.450 22.178  -10.955 1.00 30.95 ? 317 GLY C N     1 
ATOM   2216  C CA    . GLY A  1 317 ? -19.428 21.377  -10.255 1.00 29.85 ? 317 GLY C CA    1 
ATOM   2217  C C     . GLY A  1 317 ? -19.012 20.712  -8.965  1.00 28.22 ? 317 GLY C C     1 
ATOM   2218  O O     . GLY A  1 317 ? -19.754 19.867  -8.440  1.00 31.27 ? 317 GLY C O     1 
ATOM   2219  N N     . TYR A  1 318 ? -17.859 21.058  -8.425  1.00 27.41 ? 318 TYR C N     1 
ATOM   2220  C CA    . TYR A  1 318 ? -17.546 20.571  -7.094  1.00 26.15 ? 318 TYR C CA    1 
ATOM   2221  C C     . TYR A  1 318 ? -18.619 21.037  -6.107  1.00 32.01 ? 318 TYR C C     1 
ATOM   2222  O O     . TYR A  1 318 ? -19.207 22.113  -6.247  1.00 29.07 ? 318 TYR C O     1 
ATOM   2223  C CB    . TYR A  1 318 ? -16.168 21.046  -6.657  1.00 27.39 ? 318 TYR C CB    1 
ATOM   2224  C CG    . TYR A  1 318 ? -15.875 20.740  -5.207  1.00 27.36 ? 318 TYR C CG    1 
ATOM   2225  C CD1   . TYR A  1 318 ? -15.776 19.427  -4.757  1.00 30.23 ? 318 TYR C CD1   1 
ATOM   2226  C CD2   . TYR A  1 318 ? -15.730 21.756  -4.283  1.00 26.64 ? 318 TYR C CD2   1 
ATOM   2227  C CE1   . TYR A  1 318 ? -15.536 19.145  -3.423  1.00 23.11 ? 318 TYR C CE1   1 
ATOM   2228  C CE2   . TYR A  1 318 ? -15.480 21.477  -2.955  1.00 24.15 ? 318 TYR C CE2   1 
ATOM   2229  C CZ    . TYR A  1 318 ? -15.381 20.172  -2.541  1.00 21.35 ? 318 TYR C CZ    1 
ATOM   2230  O OH    . TYR A  1 318 ? -15.120 19.909  -1.220  1.00 23.50 ? 318 TYR C OH    1 
ATOM   2231  N N     . ARG A  1 319 ? -18.909 20.197  -5.119  1.00 29.20 ? 319 ARG C N     1 
ATOM   2232  C CA    . ARG A  1 319 ? -19.906 20.507  -4.112  1.00 27.69 ? 319 ARG C CA    1 
ATOM   2233  C C     . ARG A  1 319 ? -19.294 20.139  -2.779  1.00 25.94 ? 319 ARG C C     1 
ATOM   2234  O O     . ARG A  1 319 ? -18.694 19.068  -2.660  1.00 25.90 ? 319 ARG C O     1 
ATOM   2235  C CB    . ARG A  1 319 ? -21.199 19.720  -4.362  1.00 32.39 ? 319 ARG C CB    1 
ATOM   2236  C CG    . ARG A  1 319 ? -21.976 20.154  -5.596  1.00 30.19 ? 319 ARG C CG    1 
ATOM   2237  C CD    . ARG A  1 319 ? -22.467 21.583  -5.450  1.00 28.73 ? 319 ARG C CD    1 
ATOM   2238  N NE    . ARG A  1 319 ? -23.292 22.003  -6.574  1.00 29.40 ? 319 ARG C NE    1 
ATOM   2239  C CZ    . ARG A  1 319 ? -22.820 22.587  -7.667  1.00 34.41 ? 319 ARG C CZ    1 
ATOM   2240  N NH1   . ARG A  1 319 ? -21.525 22.820  -7.817  1.00 34.40 ? 319 ARG C NH1   1 
ATOM   2241  N NH2   . ARG A  1 319 ? -23.669 22.945  -8.635  1.00 34.89 ? 319 ARG C NH2   1 
ATOM   2242  N N     . GLY A  1 320 ? -19.398 21.030  -1.796  1.00 24.99 ? 320 GLY C N     1 
ATOM   2243  C CA    . GLY A  1 320 ? -18.740 20.817  -0.526  1.00 22.89 ? 320 GLY C CA    1 
ATOM   2244  C C     . GLY A  1 320 ? -17.714 21.901  -0.235  1.00 24.65 ? 320 GLY C C     1 
ATOM   2245  O O     . GLY A  1 320 ? -17.867 23.047  -0.677  1.00 23.53 ? 320 GLY C O     1 
ATOM   2246  N N     . TYR A  1 321 ? -16.680 21.523  0.538   1.00 23.87 ? 321 TYR C N     1 
ATOM   2247  C CA    . TYR A  1 321 ? -15.692 22.466  1.074   1.00 23.61 ? 321 TYR C CA    1 
ATOM   2248  C C     . TYR A  1 321 ? -14.461 22.559  0.184   1.00 25.67 ? 321 TYR C C     1 
ATOM   2249  O O     . TYR A  1 321 ? -13.945 21.544  -0.296  1.00 23.73 ? 321 TYR C O     1 
ATOM   2250  C CB    . TYR A  1 321 ? -15.247 22.048  2.483   1.00 26.62 ? 321 TYR C CB    1 
ATOM   2251  C CG    . TYR A  1 321 ? -16.393 22.048  3.477   1.00 29.93 ? 321 TYR C CG    1 
ATOM   2252  C CD1   . TYR A  1 321 ? -16.780 23.226  4.136   1.00 23.09 ? 321 TYR C CD1   1 
ATOM   2253  C CD2   . TYR A  1 321 ? -17.131 20.896  3.700   1.00 23.04 ? 321 TYR C CD2   1 
ATOM   2254  C CE1   . TYR A  1 321 ? -17.864 23.231  5.010   1.00 27.02 ? 321 TYR C CE1   1 
ATOM   2255  C CE2   . TYR A  1 321 ? -18.210 20.895  4.563   1.00 20.62 ? 321 TYR C CE2   1 
ATOM   2256  C CZ    . TYR A  1 321 ? -18.572 22.056  5.217   1.00 25.43 ? 321 TYR C CZ    1 
ATOM   2257  O OH    . TYR A  1 321 ? -19.644 22.035  6.076   1.00 29.21 ? 321 TYR C OH    1 
ATOM   2258  N N     . VAL A  1 322 ? -13.968 23.783  -0.005  1.00 23.43 ? 322 VAL C N     1 
ATOM   2259  C CA    . VAL A  1 322 ? -12.780 24.003  -0.819  1.00 27.22 ? 322 VAL C CA    1 
ATOM   2260  C C     . VAL A  1 322 ? -12.100 25.278  -0.353  1.00 24.75 ? 322 VAL C C     1 
ATOM   2261  O O     . VAL A  1 322 ? -12.738 26.189  0.176   1.00 22.88 ? 322 VAL C O     1 
ATOM   2262  C CB    . VAL A  1 322 ? -13.113 24.078  -2.325  1.00 25.25 ? 322 VAL C CB    1 
ATOM   2263  C CG1   . VAL A  1 322 ? -13.759 25.411  -2.648  1.00 22.88 ? 322 VAL C CG1   1 
ATOM   2264  C CG2   . VAL A  1 322 ? -11.853 23.885  -3.143  1.00 29.53 ? 322 VAL C CG2   1 
ATOM   2265  N N     . ASN A  1 323 ? -10.787 25.339  -0.532  1.00 25.82 ? 323 ASN C N     1 
ATOM   2266  C CA    . ASN A  1 323 ? -10.064 26.513  -0.078  1.00 29.86 ? 323 ASN C CA    1 
ATOM   2267  C C     . ASN A  1 323 ? -8.954  26.862  -1.056  1.00 28.48 ? 323 ASN C C     1 
ATOM   2268  O O     . ASN A  1 323 ? -8.443  26.009  -1.780  1.00 28.46 ? 323 ASN C O     1 
ATOM   2269  C CB    . ASN A  1 323 ? -9.498  26.298  1.322   1.00 29.93 ? 323 ASN C CB    1 
ATOM   2270  C CG    . ASN A  1 323 ? -8.313  25.398  1.313   1.00 29.76 ? 323 ASN C CG    1 
ATOM   2271  O OD1   . ASN A  1 323 ? -7.191  25.860  1.145   1.00 34.96 ? 323 ASN C OD1   1 
ATOM   2272  N ND2   . ASN A  1 323 ? -8.545  24.094  1.471   1.00 32.90 ? 323 ASN C ND2   1 
ATOM   2273  N N     . ILE A  1 324 ? -8.571  28.130  -1.052  1.00 30.09 ? 324 ILE C N     1 
ATOM   2274  C CA    . ILE A  1 324 ? -7.568  28.647  -1.970  1.00 31.74 ? 324 ILE C CA    1 
ATOM   2275  C C     . ILE A  1 324 ? -6.478  29.346  -1.154  1.00 30.18 ? 324 ILE C C     1 
ATOM   2276  O O     . ILE A  1 324 ? -6.777  30.193  -0.306  1.00 27.89 ? 324 ILE C O     1 
ATOM   2277  C CB    . ILE A  1 324 ? -8.233  29.573  -3.014  1.00 33.09 ? 324 ILE C CB    1 
ATOM   2278  C CG1   . ILE A  1 324 ? -7.270  29.939  -4.155  1.00 35.31 ? 324 ILE C CG1   1 
ATOM   2279  C CG2   . ILE A  1 324 ? -8.900  30.793  -2.349  1.00 25.90 ? 324 ILE C CG2   1 
ATOM   2280  C CD1   . ILE A  1 324 ? -7.959  30.524  -5.400  1.00 27.89 ? 324 ILE C CD1   1 
ATOM   2281  N N     . ASP A  1 325 ? -5.220  28.947  -1.376  1.00 34.73 ? 325 ASP C N     1 
ATOM   2282  C CA    . ASP A  1 325 ? -4.037  29.420  -0.657  1.00 33.51 ? 325 ASP C CA    1 
ATOM   2283  C C     . ASP A  1 325 ? -3.473  30.643  -1.366  1.00 34.13 ? 325 ASP C C     1 
ATOM   2284  O O     . ASP A  1 325 ? -3.627  30.782  -2.579  1.00 38.61 ? 325 ASP C O     1 
ATOM   2285  C CB    . ASP A  1 325 ? -2.959  28.324  -0.624  1.00 35.09 ? 325 ASP C CB    1 
ATOM   2286  C CG    . ASP A  1 325 ? -3.339  27.107  0.252   1.00 48.27 ? 325 ASP C CG    1 
ATOM   2287  O OD1   . ASP A  1 325 ? -4.500  27.021  0.729   1.00 47.57 ? 325 ASP C OD1   1 
ATOM   2288  O OD2   . ASP A  1 325 ? -2.477  26.204  0.445   1.00 47.99 ? 325 ASP C OD2   1 
ATOM   2289  N N     . GLY A  1 326 ? -2.779  31.512  -0.630  1.00 33.32 ? 326 GLY C N     1 
ATOM   2290  C CA    . GLY A  1 326 ? -2.190  32.663  -1.311  1.00 30.26 ? 326 GLY C CA    1 
ATOM   2291  C C     . GLY A  1 326 ? -1.232  33.471  -0.459  1.00 31.58 ? 326 GLY C C     1 
ATOM   2292  O O     . GLY A  1 326 ? -1.177  33.326  0.767   1.00 31.59 ? 326 GLY C O     1 
ATOM   2293  N N     . ILE A  1 327 ? -0.487  34.359  -1.136  1.00 28.71 ? 327 ILE C N     1 
ATOM   2294  C CA    . ILE A  1 327 ? 0.471   35.261  -0.498  1.00 31.46 ? 327 ILE C CA    1 
ATOM   2295  C C     . ILE A  1 327 ? 0.272   36.692  -0.983  1.00 33.79 ? 327 ILE C C     1 
ATOM   2296  O O     . ILE A  1 327 ? -0.184  36.936  -2.108  1.00 35.52 ? 327 ILE C O     1 
ATOM   2297  C CB    . ILE A  1 327 ? 1.936   34.853  -0.764  1.00 38.17 ? 327 ILE C CB    1 
ATOM   2298  C CG1   . ILE A  1 327 ? 2.177   34.715  -2.277  1.00 37.12 ? 327 ILE C CG1   1 
ATOM   2299  C CG2   . ILE A  1 327 ? 2.293   33.572  -0.001  1.00 37.94 ? 327 ILE C CG2   1 
ATOM   2300  C CD1   . ILE A  1 327 ? 3.475   35.331  -2.769  1.00 36.42 ? 327 ILE C CD1   1 
ATOM   2301  N N     . VAL A  1 328 ? 0.650   37.642  -0.130  1.00 31.37 ? 328 VAL C N     1 
ATOM   2302  C CA    . VAL A  1 328 ? 0.615   39.066  -0.448  1.00 36.60 ? 328 VAL C CA    1 
ATOM   2303  C C     . VAL A  1 328 ? 2.019   39.607  -0.256  1.00 39.66 ? 328 VAL C C     1 
ATOM   2304  O O     . VAL A  1 328 ? 2.637   39.369  0.787   1.00 43.61 ? 328 VAL C O     1 
ATOM   2305  C CB    . VAL A  1 328 ? -0.394  39.840  0.427   1.00 36.13 ? 328 VAL C CB    1 
ATOM   2306  C CG1   . VAL A  1 328 ? -0.929  41.069  -0.313  1.00 33.32 ? 328 VAL C CG1   1 
ATOM   2307  C CG2   . VAL A  1 328 ? -1.536  38.932  0.858   1.00 32.95 ? 328 VAL C CG2   1 
ATOM   2308  N N     . LEU A  1 329 ? 2.515   40.340  -1.248  1.00 41.05 ? 329 LEU C N     1 
ATOM   2309  C CA    . LEU A  1 329 ? 3.920   40.725  -1.301  1.00 45.94 ? 329 LEU C CA    1 
ATOM   2310  C C     . LEU A  1 329 ? 4.182   42.025  -0.534  1.00 47.67 ? 329 LEU C C     1 
ATOM   2311  O O     . LEU A  1 329 ? 3.290   42.852  -0.345  1.00 48.86 ? 329 LEU C O     1 
ATOM   2312  C CB    . LEU A  1 329 ? 4.366   40.860  -2.758  1.00 44.62 ? 329 LEU C CB    1 
ATOM   2313  C CG    . LEU A  1 329 ? 4.755   39.527  -3.403  1.00 43.11 ? 329 LEU C CG    1 
ATOM   2314  C CD1   . LEU A  1 329 ? 3.531   38.759  -3.777  1.00 42.77 ? 329 LEU C CD1   1 
ATOM   2315  C CD2   . LEU A  1 329 ? 5.577   39.755  -4.630  1.00 35.36 ? 329 LEU C CD2   1 
ATOM   2316  N N     . ASP A  1 330 ? 5.435   42.188  -0.081  1.00 45.45 ? 330 ASP C N     1 
ATOM   2317  C CA    . ASP A  1 330 ? 5.838   43.445  0.549   1.00 47.59 ? 330 ASP C CA    1 
ATOM   2318  C C     . ASP A  1 330 ? 5.475   44.639  -0.332  1.00 45.18 ? 330 ASP C C     1 
ATOM   2319  O O     . ASP A  1 330 ? 5.060   45.687  0.169   1.00 48.70 ? 330 ASP C O     1 
ATOM   2320  C CB    . ASP A  1 330 ? 7.347   43.446  0.853   1.00 51.42 ? 330 ASP C CB    1 
ATOM   2321  C CG    . ASP A  1 330 ? 7.736   42.473  1.970   1.00 54.82 ? 330 ASP C CG    1 
ATOM   2322  O OD1   . ASP A  1 330 ? 7.412   42.753  3.143   1.00 46.59 ? 330 ASP C OD1   1 
ATOM   2323  O OD2   . ASP A  1 330 ? 8.376   41.433  1.675   1.00 55.29 ? 330 ASP C OD2   1 
ATOM   2324  N N     . ASP A  1 331 ? 5.606   44.496  -1.650  1.00 44.77 ? 331 ASP C N     1 
ATOM   2325  C CA    . ASP A  1 331 ? 5.205   45.555  -2.568  1.00 42.41 ? 331 ASP C CA    1 
ATOM   2326  C C     . ASP A  1 331 ? 3.732   45.491  -2.952  1.00 45.59 ? 331 ASP C C     1 
ATOM   2327  O O     . ASP A  1 331 ? 3.298   46.289  -3.789  1.00 39.87 ? 331 ASP C O     1 
ATOM   2328  C CB    . ASP A  1 331 ? 6.053   45.525  -3.841  1.00 37.70 ? 331 ASP C CB    1 
ATOM   2329  C CG    . ASP A  1 331 ? 5.703   44.370  -4.769  1.00 41.92 ? 331 ASP C CG    1 
ATOM   2330  O OD1   . ASP A  1 331 ? 4.982   43.428  -4.373  1.00 44.05 ? 331 ASP C OD1   1 
ATOM   2331  O OD2   . ASP A  1 331 ? 6.164   44.409  -5.928  1.00 44.78 ? 331 ASP C OD2   1 
ATOM   2332  N N     . GLY A  1 332 ? 2.966   44.545  -2.393  1.00 44.97 ? 332 GLY C N     1 
ATOM   2333  C CA    . GLY A  1 332 ? 1.525   44.495  -2.560  1.00 40.83 ? 332 GLY C CA    1 
ATOM   2334  C C     . GLY A  1 332 ? 0.996   43.577  -3.649  1.00 47.28 ? 332 GLY C C     1 
ATOM   2335  O O     . GLY A  1 332 ? -0.230  43.533  -3.853  1.00 37.41 ? 332 GLY C O     1 
ATOM   2336  N N     . ARG A  1 333 ? 1.864   42.861  -4.366  1.00 41.20 ? 333 ARG C N     1 
ATOM   2337  C CA    . ARG A  1 333 ? 1.384   41.911  -5.358  1.00 45.71 ? 333 ARG C CA    1 
ATOM   2338  C C     . ARG A  1 333 ? 0.711   40.725  -4.655  1.00 46.48 ? 333 ARG C C     1 
ATOM   2339  O O     . ARG A  1 333 ? 1.035   40.389  -3.511  1.00 39.67 ? 333 ARG C O     1 
ATOM   2340  C CB    . ARG A  1 333 ? 2.541   41.437  -6.248  1.00 42.43 ? 333 ARG C CB    1 
ATOM   2341  C CG    . ARG A  1 333 ? 2.796   42.293  -7.483  1.00 42.59 ? 333 ARG C CG    1 
ATOM   2342  C CD    . ARG A  1 333 ? 4.177   42.000  -8.103  1.00 34.50 ? 333 ARG C CD    1 
ATOM   2343  N NE    . ARG A  1 333 ? 5.229   42.338  -7.153  1.00 36.05 ? 333 ARG C NE    1 
ATOM   2344  C CZ    . ARG A  1 333 ? 6.391   41.707  -7.041  1.00 34.53 ? 333 ARG C CZ    1 
ATOM   2345  N NH1   . ARG A  1 333 ? 6.724   40.712  -7.849  1.00 32.46 ? 333 ARG C NH1   1 
ATOM   2346  N NH2   . ARG A  1 333 ? 7.240   42.087  -6.091  1.00 30.47 ? 333 ARG C NH2   1 
ATOM   2347  N N     . VAL A  1 334 ? -0.254  40.102  -5.346  1.00 40.53 ? 334 VAL C N     1 
ATOM   2348  C CA    . VAL A  1 334 ? -0.965  38.934  -4.839  1.00 35.49 ? 334 VAL C CA    1 
ATOM   2349  C C     . VAL A  1 334 ? -0.718  37.775  -5.794  1.00 39.20 ? 334 VAL C C     1 
ATOM   2350  O O     . VAL A  1 334 ? -0.511  37.979  -6.992  1.00 41.57 ? 334 VAL C O     1 
ATOM   2351  C CB    . VAL A  1 334 ? -2.473  39.215  -4.686  1.00 38.73 ? 334 VAL C CB    1 
ATOM   2352  C CG1   . VAL A  1 334 ? -3.225  37.995  -4.144  1.00 34.85 ? 334 VAL C CG1   1 
ATOM   2353  C CG2   . VAL A  1 334 ? -2.690  40.420  -3.793  1.00 40.12 ? 334 VAL C CG2   1 
ATOM   2354  N N     . PHE A  1 335 ? -0.695  36.554  -5.246  1.00 39.48 ? 335 PHE C N     1 
ATOM   2355  C CA    . PHE A  1 335 ? -0.587  35.319  -6.018  1.00 30.63 ? 335 PHE C CA    1 
ATOM   2356  C C     . PHE A  1 335 ? -1.318  34.224  -5.264  1.00 36.05 ? 335 PHE C C     1 
ATOM   2357  O O     . PHE A  1 335 ? -1.269  34.176  -4.024  1.00 34.80 ? 335 PHE C O     1 
ATOM   2358  C CB    . PHE A  1 335 ? 0.859   34.877  -6.243  1.00 27.64 ? 335 PHE C CB    1 
ATOM   2359  C CG    . PHE A  1 335 ? 1.686   35.875  -6.978  1.00 32.99 ? 335 PHE C CG    1 
ATOM   2360  C CD1   . PHE A  1 335 ? 1.532   36.047  -8.334  1.00 33.54 ? 335 PHE C CD1   1 
ATOM   2361  C CD2   . PHE A  1 335 ? 2.619   36.651  -6.311  1.00 37.33 ? 335 PHE C CD2   1 
ATOM   2362  C CE1   . PHE A  1 335 ? 2.295   36.976  -9.014  1.00 35.20 ? 335 PHE C CE1   1 
ATOM   2363  C CE2   . PHE A  1 335 ? 3.397   37.590  -6.986  1.00 38.25 ? 335 PHE C CE2   1 
ATOM   2364  C CZ    . PHE A  1 335 ? 3.236   37.752  -8.332  1.00 34.02 ? 335 PHE C CZ    1 
ATOM   2365  N N     . PHE A  1 336 ? -1.985  33.347  -6.014  1.00 33.35 ? 336 PHE C N     1 
ATOM   2366  C CA    . PHE A  1 336 ? -2.654  32.180  -5.454  1.00 35.67 ? 336 PHE C CA    1 
ATOM   2367  C C     . PHE A  1 336 ? -1.919  30.911  -5.884  1.00 34.21 ? 336 PHE C C     1 
ATOM   2368  O O     . PHE A  1 336 ? -1.416  30.833  -7.015  1.00 27.65 ? 336 PHE C O     1 
ATOM   2369  C CB    . PHE A  1 336 ? -4.125  32.133  -5.888  1.00 31.56 ? 336 PHE C CB    1 
ATOM   2370  C CG    . PHE A  1 336 ? -4.954  33.288  -5.371  1.00 34.08 ? 336 PHE C CG    1 
ATOM   2371  C CD1   . PHE A  1 336 ? -5.597  33.206  -4.141  1.00 29.92 ? 336 PHE C CD1   1 
ATOM   2372  C CD2   . PHE A  1 336 ? -5.095  34.453  -6.116  1.00 34.07 ? 336 PHE C CD2   1 
ATOM   2373  C CE1   . PHE A  1 336 ? -6.368  34.268  -3.677  1.00 34.27 ? 336 PHE C CE1   1 
ATOM   2374  C CE2   . PHE A  1 336 ? -5.857  35.526  -5.643  1.00 35.02 ? 336 PHE C CE2   1 
ATOM   2375  C CZ    . PHE A  1 336 ? -6.499  35.430  -4.428  1.00 30.38 ? 336 PHE C CZ    1 
ATOM   2376  N N     . HIS A  1 337 ? -1.867  29.919  -4.977  1.00 28.66 ? 337 HIS C N     1 
ATOM   2377  C CA    . HIS A  1 337 ? -1.021  28.727  -5.101  1.00 29.02 ? 337 HIS C CA    1 
ATOM   2378  C C     . HIS A  1 337 ? -1.769  27.463  -5.476  1.00 32.56 ? 337 HIS C C     1 
ATOM   2379  O O     . HIS A  1 337 ? -1.271  26.697  -6.294  1.00 36.42 ? 337 HIS C O     1 
ATOM   2380  C CB    . HIS A  1 337 ? -0.257  28.458  -3.793  1.00 30.44 ? 337 HIS C CB    1 
ATOM   2381  C CG    . HIS A  1 337 ? 0.489   29.652  -3.288  1.00 30.77 ? 337 HIS C CG    1 
ATOM   2382  N ND1   . HIS A  1 337 ? 1.699   30.051  -3.811  1.00 33.23 ? 337 HIS C ND1   1 
ATOM   2383  C CD2   . HIS A  1 337 ? 0.159   30.578  -2.361  1.00 29.56 ? 337 HIS C CD2   1 
ATOM   2384  C CE1   . HIS A  1 337 ? 2.097   31.154  -3.207  1.00 31.49 ? 337 HIS C CE1   1 
ATOM   2385  N NE2   . HIS A  1 337 ? 1.177   31.497  -2.325  1.00 34.67 ? 337 HIS C NE2   1 
ATOM   2386  N N     . GLU A  1 338 ? -2.929  27.195  -4.881  1.00 38.09 ? 338 GLU C N     1 
ATOM   2387  C CA    . GLU A  1 338 ? -3.640  25.941  -5.108  1.00 31.82 ? 338 GLU C CA    1 
ATOM   2388  C C     . GLU A  1 338 ? -5.028  26.083  -4.509  1.00 31.42 ? 338 GLU C C     1 
ATOM   2389  O O     . GLU A  1 338 ? -5.292  26.994  -3.717  1.00 32.35 ? 338 GLU C O     1 
ATOM   2390  C CB    . GLU A  1 338 ? -2.904  24.747  -4.477  1.00 32.94 ? 338 GLU C CB    1 
ATOM   2391  C CG    . GLU A  1 338 ? -2.525  24.994  -3.025  1.00 36.35 ? 338 GLU C CG    1 
ATOM   2392  C CD    . GLU A  1 338 ? -2.513  23.739  -2.136  1.00 40.75 ? 338 GLU C CD    1 
ATOM   2393  O OE1   . GLU A  1 338 ? -2.391  22.608  -2.650  1.00 37.13 ? 338 GLU C OE1   1 
ATOM   2394  O OE2   . GLU A  1 338 ? -2.595  23.893  -0.897  1.00 44.02 ? 338 GLU C OE2   1 
ATOM   2395  N N     . ILE A  1 339 ? -5.915  25.154  -4.891  1.00 30.31 ? 339 ILE C N     1 
ATOM   2396  C CA    . ILE A  1 339 ? -7.125  24.871  -4.125  1.00 32.95 ? 339 ILE C CA    1 
ATOM   2397  C C     . ILE A  1 339 ? -7.073  23.420  -3.657  1.00 33.94 ? 339 ILE C C     1 
ATOM   2398  O O     . ILE A  1 339 ? -6.433  22.570  -4.287  1.00 31.51 ? 339 ILE C O     1 
ATOM   2399  C CB    . ILE A  1 339 ? -8.436  25.136  -4.899  1.00 25.89 ? 339 ILE C CB    1 
ATOM   2400  C CG1   . ILE A  1 339 ? -8.447  24.385  -6.217  1.00 27.58 ? 339 ILE C CG1   1 
ATOM   2401  C CG2   . ILE A  1 339 ? -8.639  26.608  -5.121  1.00 30.22 ? 339 ILE C CG2   1 
ATOM   2402  C CD1   . ILE A  1 339 ? -9.772  23.752  -6.530  1.00 24.26 ? 339 ILE C CD1   1 
ATOM   2403  N N     . ASN A  1 340 ? -7.740  23.142  -2.530  1.00 33.08 ? 340 ASN C N     1 
ATOM   2404  C CA    . ASN A  1 340 ? -7.921  21.780  -2.030  1.00 33.14 ? 340 ASN C CA    1 
ATOM   2405  C C     . ASN A  1 340 ? -9.423  21.572  -1.866  1.00 28.98 ? 340 ASN C C     1 
ATOM   2406  O O     . ASN A  1 340 ? -10.053 22.208  -1.010  1.00 27.93 ? 340 ASN C O     1 
ATOM   2407  C CB    . ASN A  1 340 ? -7.181  21.522  -0.700  1.00 36.80 ? 340 ASN C CB    1 
ATOM   2408  C CG    . ASN A  1 340 ? -5.863  22.281  -0.582  1.00 33.42 ? 340 ASN C CG    1 
ATOM   2409  O OD1   . ASN A  1 340 ? -5.867  23.506  -0.469  1.00 39.08 ? 340 ASN C OD1   1 
ATOM   2410  N ND2   . ASN A  1 340 ? -4.737  21.563  -0.605  1.00 36.36 ? 340 ASN C ND2   1 
ATOM   2411  N N     . ALA A  1 341 ? -9.999  20.707  -2.707  1.00 28.50 ? 341 ALA C N     1 
ATOM   2412  C CA    . ALA A  1 341 ? -11.377 20.253  -2.537  1.00 27.21 ? 341 ALA C CA    1 
ATOM   2413  C C     . ALA A  1 341 ? -11.352 19.208  -1.437  1.00 27.89 ? 341 ALA C C     1 
ATOM   2414  O O     . ALA A  1 341 ? -11.275 18.004  -1.682  1.00 31.11 ? 341 ALA C O     1 
ATOM   2415  C CB    . ALA A  1 341 ? -11.963 19.697  -3.829  1.00 25.27 ? 341 ALA C CB    1 
ATOM   2416  N N     . ARG A  1 342 ? -11.362 19.705  -0.197  1.00 27.97 ? 342 ARG C N     1 
ATOM   2417  C CA    . ARG A  1 342 ? -11.546 18.896  1.006   1.00 29.71 ? 342 ARG C CA    1 
ATOM   2418  C C     . ARG A  1 342 ? -11.625 19.806  2.224   1.00 27.99 ? 342 ARG C C     1 
ATOM   2419  O O     . ARG A  1 342 ? -11.619 21.034  2.101   1.00 29.44 ? 342 ARG C O     1 
ATOM   2420  C CB    . ARG A  1 342 ? -10.409 17.887  1.176   1.00 34.30 ? 342 ARG C CB    1 
ATOM   2421  C CG    . ARG A  1 342 ? -9.077  18.380  0.654   1.00 32.92 ? 342 ARG C CG    1 
ATOM   2422  C CD    . ARG A  1 342 ? -8.036  17.297  0.697   1.00 37.42 ? 342 ARG C CD    1 
ATOM   2423  N NE    . ARG A  1 342 ? -6.751  17.886  1.034   1.00 46.76 ? 342 ARG C NE    1 
ATOM   2424  C CZ    . ARG A  1 342 ? -5.829  18.214  0.139   1.00 46.51 ? 342 ARG C CZ    1 
ATOM   2425  N NH1   . ARG A  1 342 ? -5.996  17.959  -1.149  1.00 39.24 ? 342 ARG C NH1   1 
ATOM   2426  N NH2   . ARG A  1 342 ? -4.716  18.818  0.548   1.00 49.69 ? 342 ARG C NH2   1 
ATOM   2427  N N     . TRP A  1 343 ? -11.708 19.229  3.409   1.00 27.26 ? 343 TRP C N     1 
ATOM   2428  C CA    . TRP A  1 343 ? -11.571 20.062  4.585   1.00 30.27 ? 343 TRP C CA    1 
ATOM   2429  C C     . TRP A  1 343 ? -10.204 20.726  4.564   1.00 25.42 ? 343 TRP C C     1 
ATOM   2430  O O     . TRP A  1 343 ? -9.185  20.060  4.402   1.00 26.72 ? 343 TRP C O     1 
ATOM   2431  C CB    . TRP A  1 343 ? -11.742 19.235  5.857   1.00 30.99 ? 343 TRP C CB    1 
ATOM   2432  C CG    . TRP A  1 343 ? -13.045 18.503  5.936   1.00 30.62 ? 343 TRP C CG    1 
ATOM   2433  C CD1   . TRP A  1 343 ? -14.168 18.772  5.228   1.00 30.62 ? 343 TRP C CD1   1 
ATOM   2434  C CD2   . TRP A  1 343 ? -13.364 17.389  6.787   1.00 30.12 ? 343 TRP C CD2   1 
ATOM   2435  N NE1   . TRP A  1 343 ? -15.170 17.888  5.565   1.00 35.37 ? 343 TRP C NE1   1 
ATOM   2436  C CE2   . TRP A  1 343 ? -14.703 17.035  6.528   1.00 33.94 ? 343 TRP C CE2   1 
ATOM   2437  C CE3   . TRP A  1 343 ? -12.646 16.652  7.729   1.00 29.12 ? 343 TRP C CE3   1 
ATOM   2438  C CZ2   . TRP A  1 343 ? -15.337 15.982  7.171   1.00 31.93 ? 343 TRP C CZ2   1 
ATOM   2439  C CZ3   . TRP A  1 343 ? -13.292 15.609  8.385   1.00 38.31 ? 343 TRP C CZ3   1 
ATOM   2440  C CH2   . TRP A  1 343 ? -14.620 15.283  8.097   1.00 32.85 ? 343 TRP C CH2   1 
ATOM   2441  N N     . SER A  1 344 ? -10.177 22.041  4.685   1.00 23.16 ? 344 SER C N     1 
ATOM   2442  C CA    . SER A  1 344 ? -8.923  22.635  5.082   1.00 27.97 ? 344 SER C CA    1 
ATOM   2443  C C     . SER A  1 344 ? -8.602  22.210  6.515   1.00 35.01 ? 344 SER C C     1 
ATOM   2444  O O     . SER A  1 344 ? -9.409  21.565  7.195   1.00 37.18 ? 344 SER C O     1 
ATOM   2445  C CB    . SER A  1 344 ? -8.982  24.155  4.982   1.00 28.41 ? 344 SER C CB    1 
ATOM   2446  O OG    . SER A  1 344 ? -9.111  24.737  6.267   1.00 32.10 ? 344 SER C OG    1 
ATOM   2447  N N     . GLY A  1 345 ? -7.407  22.571  6.979   1.00 33.72 ? 345 GLY C N     1 
ATOM   2448  C CA    . GLY A  1 345 ? -7.092  22.384  8.380   1.00 20.93 ? 345 GLY C CA    1 
ATOM   2449  C C     . GLY A  1 345 ? -8.042  23.196  9.235   1.00 29.81 ? 345 GLY C C     1 
ATOM   2450  O O     . GLY A  1 345 ? -8.820  22.641  10.015  1.00 38.69 ? 345 GLY C O     1 
ATOM   2451  N N     . GLY A  1 346 ? -8.032  24.516  9.056   1.00 31.65 ? 346 GLY C N     1 
ATOM   2452  C CA    . GLY A  1 346 ? -8.721  25.414  9.965   1.00 22.62 ? 346 GLY C CA    1 
ATOM   2453  C C     . GLY A  1 346 ? -10.220 25.324  9.957   1.00 22.85 ? 346 GLY C C     1 
ATOM   2454  O O     . GLY A  1 346 ? -10.887 26.128  10.607  1.00 28.21 ? 346 GLY C O     1 
ATOM   2455  N N     . LEU A  1 347 ? -10.772 24.354  9.233   1.00 27.06 ? 347 LEU C N     1 
ATOM   2456  C CA    . LEU A  1 347 ? -12.223 24.224  9.203   1.00 26.21 ? 347 LEU C CA    1 
ATOM   2457  C C     . LEU A  1 347 ? -12.747 23.779  10.552  1.00 22.95 ? 347 LEU C C     1 
ATOM   2458  O O     . LEU A  1 347 ? -13.757 24.294  11.036  1.00 24.76 ? 347 LEU C O     1 
ATOM   2459  C CB    . LEU A  1 347 ? -12.661 23.248  8.113   1.00 22.86 ? 347 LEU C CB    1 
ATOM   2460  C CG    . LEU A  1 347 ? -14.174 22.995  8.101   1.00 23.60 ? 347 LEU C CG    1 
ATOM   2461  C CD1   . LEU A  1 347 ? -14.960 24.297  7.918   1.00 22.82 ? 347 LEU C CD1   1 
ATOM   2462  C CD2   . LEU A  1 347 ? -14.556 21.995  7.023   1.00 22.70 ? 347 LEU C CD2   1 
ATOM   2463  N N     . ILE A  1 348 ? -12.062 22.843  11.192  1.00 27.64 ? 348 ILE C N     1 
ATOM   2464  C CA    . ILE A  1 348 ? -12.449 22.516  12.558  1.00 32.48 ? 348 ILE C CA    1 
ATOM   2465  C C     . ILE A  1 348 ? -12.302 23.741  13.460  1.00 27.05 ? 348 ILE C C     1 
ATOM   2466  O O     . ILE A  1 348 ? -13.182 24.020  14.285  1.00 34.35 ? 348 ILE C O     1 
ATOM   2467  C CB    . ILE A  1 348 ? -11.665 21.291  13.078  1.00 31.46 ? 348 ILE C CB    1 
ATOM   2468  C CG1   . ILE A  1 348 ? -12.207 20.858  14.448  1.00 29.85 ? 348 ILE C CG1   1 
ATOM   2469  C CG2   . ILE A  1 348 ? -10.167 21.526  13.076  1.00 29.51 ? 348 ILE C CG2   1 
ATOM   2470  C CD1   . ILE A  1 348 ? -13.627 20.372  14.396  1.00 25.68 ? 348 ILE C CD1   1 
ATOM   2471  N N     . TYR A  1 349 ? -11.232 24.522  13.285  1.00 23.40 ? 349 TYR C N     1 
ATOM   2472  C CA    . TYR A  1 349 ? -11.112 25.770  14.037  1.00 28.92 ? 349 TYR C CA    1 
ATOM   2473  C C     . TYR A  1 349 ? -12.345 26.630  13.825  1.00 31.94 ? 349 TYR C C     1 
ATOM   2474  O O     . TYR A  1 349 ? -13.076 26.952  14.772  1.00 26.52 ? 349 TYR C O     1 
ATOM   2475  C CB    . TYR A  1 349 ? -9.859  26.559  13.631  1.00 26.42 ? 349 TYR C CB    1 
ATOM   2476  C CG    . TYR A  1 349 ? -8.541  25.821  13.782  1.00 31.02 ? 349 TYR C CG    1 
ATOM   2477  C CD1   . TYR A  1 349 ? -8.394  24.778  14.688  1.00 27.18 ? 349 TYR C CD1   1 
ATOM   2478  C CD2   . TYR A  1 349 ? -7.441  26.167  13.012  1.00 30.39 ? 349 TYR C CD2   1 
ATOM   2479  C CE1   . TYR A  1 349 ? -7.214  24.102  14.807  1.00 23.04 ? 349 TYR C CE1   1 
ATOM   2480  C CE2   . TYR A  1 349 ? -6.246  25.483  13.130  1.00 27.02 ? 349 TYR C CE2   1 
ATOM   2481  C CZ    . TYR A  1 349 ? -6.141  24.454  14.023  1.00 25.74 ? 349 TYR C CZ    1 
ATOM   2482  O OH    . TYR A  1 349 ? -4.943  23.787  14.142  1.00 24.21 ? 349 TYR C OH    1 
ATOM   2483  N N     . HIS A  1 350 ? -12.600 26.986  12.564  1.00 31.32 ? 350 HIS C N     1 
ATOM   2484  C CA    . HIS A  1 350 ? -13.765 27.798  12.247  1.00 27.28 ? 350 HIS C CA    1 
ATOM   2485  C C     . HIS A  1 350 ? -15.032 27.210  12.836  1.00 32.07 ? 350 HIS C C     1 
ATOM   2486  O O     . HIS A  1 350 ? -15.778 27.894  13.551  1.00 33.83 ? 350 HIS C O     1 
ATOM   2487  C CB    . HIS A  1 350 ? -13.934 27.918  10.758  1.00 27.38 ? 350 HIS C CB    1 
ATOM   2488  C CG    . HIS A  1 350 ? -15.178 28.644  10.383  1.00 31.68 ? 350 HIS C CG    1 
ATOM   2489  N ND1   . HIS A  1 350 ? -15.389 29.965  10.715  1.00 25.38 ? 350 HIS C ND1   1 
ATOM   2490  C CD2   . HIS A  1 350 ? -16.282 28.237  9.718   1.00 25.99 ? 350 HIS C CD2   1 
ATOM   2491  C CE1   . HIS A  1 350 ? -16.567 30.343  10.258  1.00 28.93 ? 350 HIS C CE1   1 
ATOM   2492  N NE2   . HIS A  1 350 ? -17.126 29.315  9.643   1.00 29.70 ? 350 HIS C NE2   1 
ATOM   2493  N N     . THR A  1 351 ? -15.306 25.948  12.517  1.00 28.54 ? 351 THR C N     1 
ATOM   2494  C CA    . THR A  1 351 ? -16.429 25.247  13.123  1.00 29.40 ? 351 THR C CA    1 
ATOM   2495  C C     . THR A  1 351 ? -16.517 25.558  14.603  1.00 33.74 ? 351 THR C C     1 
ATOM   2496  O O     . THR A  1 351 ? -17.448 26.248  15.029  1.00 35.25 ? 351 THR C O     1 
ATOM   2497  C CB    . THR A  1 351 ? -16.304 23.739  12.931  1.00 33.85 ? 351 THR C CB    1 
ATOM   2498  O OG1   . THR A  1 351 ? -15.888 23.456  11.588  1.00 34.22 ? 351 THR C OG1   1 
ATOM   2499  C CG2   . THR A  1 351 ? -17.640 23.043  13.199  1.00 33.75 ? 351 THR C CG2   1 
ATOM   2500  N N     . VAL A  1 352 ? -15.525 25.102  15.379  1.00 36.07 ? 352 VAL C N     1 
ATOM   2501  C CA    . VAL A  1 352 ? -15.580 25.268  16.833  1.00 32.07 ? 352 VAL C CA    1 
ATOM   2502  C C     . VAL A  1 352 ? -15.810 26.720  17.186  1.00 33.96 ? 352 VAL C C     1 
ATOM   2503  O O     . VAL A  1 352 ? -16.581 27.036  18.100  1.00 34.45 ? 352 VAL C O     1 
ATOM   2504  C CB    . VAL A  1 352 ? -14.304 24.731  17.498  1.00 31.03 ? 352 VAL C CB    1 
ATOM   2505  C CG1   . VAL A  1 352 ? -13.900 25.621  18.658  1.00 34.01 ? 352 VAL C CG1   1 
ATOM   2506  C CG2   . VAL A  1 352 ? -14.547 23.348  18.013  1.00 31.68 ? 352 VAL C CG2   1 
ATOM   2507  N N     . ALA A  1 353 ? -15.163 27.629  16.454  1.00 33.90 ? 353 ALA C N     1 
ATOM   2508  C CA    . ALA A  1 353 ? -15.396 29.049  16.682  1.00 32.25 ? 353 ALA C CA    1 
ATOM   2509  C C     . ALA A  1 353 ? -16.882 29.368  16.593  1.00 34.51 ? 353 ALA C C     1 
ATOM   2510  O O     . ALA A  1 353 ? -17.482 29.875  17.547  1.00 35.77 ? 353 ALA C O     1 
ATOM   2511  C CB    . ALA A  1 353 ? -14.593 29.876  15.681  1.00 26.26 ? 353 ALA C CB    1 
ATOM   2512  N N     . GLU A  1 354 ? -17.501 29.025  15.465  1.00 38.19 ? 354 GLU C N     1 
ATOM   2513  C CA    . GLU A  1 354 ? -18.933 29.224  15.295  1.00 33.16 ? 354 GLU C CA    1 
ATOM   2514  C C     . GLU A  1 354 ? -19.710 28.650  16.471  1.00 34.19 ? 354 GLU C C     1 
ATOM   2515  O O     . GLU A  1 354 ? -20.549 29.325  17.070  1.00 31.95 ? 354 GLU C O     1 
ATOM   2516  C CB    . GLU A  1 354 ? -19.364 28.564  13.993  1.00 35.40 ? 354 GLU C CB    1 
ATOM   2517  C CG    . GLU A  1 354 ? -19.792 29.515  12.915  1.00 40.10 ? 354 GLU C CG    1 
ATOM   2518  C CD    . GLU A  1 354 ? -20.426 28.780  11.757  1.00 49.28 ? 354 GLU C CD    1 
ATOM   2519  O OE1   . GLU A  1 354 ? -20.354 29.290  10.617  1.00 60.49 ? 354 GLU C OE1   1 
ATOM   2520  O OE2   . GLU A  1 354 ? -20.970 27.676  11.976  1.00 52.83 ? 354 GLU C OE2   1 
ATOM   2521  N N     . ARG A  1 355 ? -19.400 27.411  16.849  1.00 35.09 ? 355 ARG C N     1 
ATOM   2522  C CA    . ARG A  1 355 ? -20.227 26.729  17.830  1.00 33.47 ? 355 ARG C CA    1 
ATOM   2523  C C     . ARG A  1 355 ? -20.110 27.363  19.210  1.00 38.14 ? 355 ARG C C     1 
ATOM   2524  O O     . ARG A  1 355 ? -21.099 27.398  19.946  1.00 43.35 ? 355 ARG C O     1 
ATOM   2525  C CB    . ARG A  1 355 ? -19.865 25.246  17.883  1.00 32.44 ? 355 ARG C CB    1 
ATOM   2526  C CG    . ARG A  1 355 ? -19.960 24.532  16.532  1.00 29.53 ? 355 ARG C CG    1 
ATOM   2527  C CD    . ARG A  1 355 ? -19.803 23.027  16.681  1.00 31.51 ? 355 ARG C CD    1 
ATOM   2528  N NE    . ARG A  1 355 ? -20.995 22.431  17.282  1.00 35.21 ? 355 ARG C NE    1 
ATOM   2529  C CZ    . ARG A  1 355 ? -21.205 21.128  17.425  1.00 33.50 ? 355 ARG C CZ    1 
ATOM   2530  N NH1   . ARG A  1 355 ? -20.297 20.235  17.068  1.00 33.50 ? 355 ARG C NH1   1 
ATOM   2531  N NH2   . ARG A  1 355 ? -22.359 20.709  17.938  1.00 35.28 ? 355 ARG C NH2   1 
ATOM   2532  N N     . LEU A  1 356 ? -18.941 27.894  19.573  1.00 37.14 ? 356 LEU C N     1 
ATOM   2533  C CA    . LEU A  1 356 ? -18.767 28.412  20.930  1.00 34.40 ? 356 LEU C CA    1 
ATOM   2534  C C     . LEU A  1 356 ? -19.047 29.904  21.040  1.00 35.98 ? 356 LEU C C     1 
ATOM   2535  O O     . LEU A  1 356 ? -19.574 30.351  22.058  1.00 38.16 ? 356 LEU C O     1 
ATOM   2536  C CB    . LEU A  1 356 ? -17.355 28.128  21.450  1.00 33.45 ? 356 LEU C CB    1 
ATOM   2537  C CG    . LEU A  1 356 ? -17.008 26.647  21.579  1.00 32.08 ? 356 LEU C CG    1 
ATOM   2538  C CD1   . LEU A  1 356 ? -15.682 26.453  22.242  1.00 32.11 ? 356 LEU C CD1   1 
ATOM   2539  C CD2   . LEU A  1 356 ? -18.098 25.941  22.343  1.00 35.18 ? 356 LEU C CD2   1 
ATOM   2540  N N     . LEU A  1 357 ? -18.718 30.700  20.028  1.00 33.50 ? 357 LEU C N     1 
ATOM   2541  C CA    . LEU A  1 357 ? -18.949 32.132  20.122  1.00 32.15 ? 357 LEU C CA    1 
ATOM   2542  C C     . LEU A  1 357 ? -20.024 32.661  19.182  1.00 33.12 ? 357 LEU C C     1 
ATOM   2543  O O     . LEU A  1 357 ? -20.427 33.824  19.330  1.00 31.80 ? 357 LEU C O     1 
ATOM   2544  C CB    . LEU A  1 357 ? -17.652 32.893  19.862  1.00 36.20 ? 357 LEU C CB    1 
ATOM   2545  C CG    . LEU A  1 357 ? -16.419 32.367  20.579  1.00 42.32 ? 357 LEU C CG    1 
ATOM   2546  C CD1   . LEU A  1 357 ? -15.174 32.686  19.752  1.00 35.51 ? 357 LEU C CD1   1 
ATOM   2547  C CD2   . LEU A  1 357 ? -16.335 32.985  21.965  1.00 40.45 ? 357 LEU C CD2   1 
ATOM   2548  N N     . GLY A  1 358 ? -20.470 31.876  18.210  1.00 34.74 ? 358 GLY C N     1 
ATOM   2549  C CA    . GLY A  1 358 ? -21.514 32.299  17.298  1.00 35.97 ? 358 GLY C CA    1 
ATOM   2550  C C     . GLY A  1 358 ? -21.014 32.476  15.868  1.00 37.69 ? 358 GLY C C     1 
ATOM   2551  O O     . GLY A  1 358 ? -19.816 32.500  15.583  1.00 36.91 ? 358 GLY C O     1 
ATOM   2552  N N     . HIS A  1 359 ? -21.990 32.630  14.970  1.00 38.01 ? 359 HIS C N     1 
ATOM   2553  C CA    . HIS A  1 359 ? -21.718 32.653  13.538  1.00 46.89 ? 359 HIS C CA    1 
ATOM   2554  C C     . HIS A  1 359 ? -20.822 33.827  13.161  1.00 47.23 ? 359 HIS C C     1 
ATOM   2555  O O     . HIS A  1 359 ? -19.829 33.671  12.434  1.00 48.42 ? 359 HIS C O     1 
ATOM   2556  C CB    . HIS A  1 359 ? -23.038 32.714  12.764  1.00 43.40 ? 359 HIS C CB    1 
ATOM   2557  C CG    . HIS A  1 359 ? -22.875 32.579  11.274  1.00 63.27 ? 359 HIS C CG    1 
ATOM   2558  N ND1   . HIS A  1 359 ? -22.275 33.548  10.493  1.00 61.93 ? 359 HIS C ND1   1 
ATOM   2559  C CD2   . HIS A  1 359 ? -23.226 31.579  10.425  1.00 60.51 ? 359 HIS C CD2   1 
ATOM   2560  C CE1   . HIS A  1 359 ? -22.271 33.154  9.230   1.00 55.01 ? 359 HIS C CE1   1 
ATOM   2561  N NE2   . HIS A  1 359 ? -22.844 31.964  9.161   1.00 52.30 ? 359 HIS C NE2   1 
ATOM   2562  N N     . ASP A  1 360 ? -21.162 35.013  13.641  1.00 42.98 ? 360 ASP C N     1 
ATOM   2563  C CA    . ASP A  1 360 ? -20.465 36.230  13.249  1.00 44.33 ? 360 ASP C CA    1 
ATOM   2564  C C     . ASP A  1 360 ? -19.347 36.571  14.225  1.00 44.40 ? 360 ASP C C     1 
ATOM   2565  O O     . ASP A  1 360 ? -19.110 37.724  14.603  1.00 38.52 ? 360 ASP C O     1 
ATOM   2566  C CB    . ASP A  1 360 ? -21.497 37.339  13.116  1.00 49.71 ? 360 ASP C CB    1 
ATOM   2567  C CG    . ASP A  1 360 ? -22.748 36.859  12.352  1.00 57.10 ? 360 ASP C CG    1 
ATOM   2568  O OD1   . ASP A  1 360 ? -22.646 36.723  11.109  1.00 59.75 ? 360 ASP C OD1   1 
ATOM   2569  O OD2   . ASP A  1 360 ? -23.811 36.583  12.977  1.00 45.59 ? 360 ASP C OD2   1 
ATOM   2570  N N     . TYR A  1 361 ? -18.619 35.521  14.606  1.00 38.44 ? 361 TYR C N     1 
ATOM   2571  C CA    . TYR A  1 361 ? -17.601 35.616  15.636  1.00 34.49 ? 361 TYR C CA    1 
ATOM   2572  C C     . TYR A  1 361 ? -16.411 36.462  15.205  1.00 39.42 ? 361 TYR C C     1 
ATOM   2573  O O     . TYR A  1 361 ? -15.797 37.127  16.050  1.00 37.22 ? 361 TYR C O     1 
ATOM   2574  C CB    . TYR A  1 361 ? -17.146 34.210  16.006  1.00 37.22 ? 361 TYR C CB    1 
ATOM   2575  C CG    . TYR A  1 361 ? -16.409 33.458  14.911  1.00 37.35 ? 361 TYR C CG    1 
ATOM   2576  C CD1   . TYR A  1 361 ? -15.020 33.529  14.816  1.00 36.84 ? 361 TYR C CD1   1 
ATOM   2577  C CD2   . TYR A  1 361 ? -17.087 32.651  13.996  1.00 34.65 ? 361 TYR C CD2   1 
ATOM   2578  C CE1   . TYR A  1 361 ? -14.323 32.844  13.834  1.00 33.47 ? 361 TYR C CE1   1 
ATOM   2579  C CE2   . TYR A  1 361 ? -16.398 31.955  13.020  1.00 34.84 ? 361 TYR C CE2   1 
ATOM   2580  C CZ    . TYR A  1 361 ? -15.003 32.061  12.939  1.00 35.17 ? 361 TYR C CZ    1 
ATOM   2581  O OH    . TYR A  1 361 ? -14.264 31.388  11.972  1.00 35.50 ? 361 TYR C OH    1 
ATOM   2582  N N     . ALA A  1 362 ? -16.068 36.446  13.909  1.00 36.30 ? 362 ALA C N     1 
ATOM   2583  C CA    . ALA A  1 362 ? -14.853 37.106  13.443  1.00 32.96 ? 362 ALA C CA    1 
ATOM   2584  C C     . ALA A  1 362 ? -14.887 38.610  13.660  1.00 36.97 ? 362 ALA C C     1 
ATOM   2585  O O     . ALA A  1 362 ? -13.825 39.252  13.661  1.00 37.03 ? 362 ALA C O     1 
ATOM   2586  C CB    . ALA A  1 362 ? -14.626 36.809  11.965  1.00 31.63 ? 362 ALA C CB    1 
ATOM   2587  N N     . ARG A  1 363 ? -16.081 39.179  13.848  1.00 36.42 ? 363 ARG C N     1 
ATOM   2588  C CA    . ARG A  1 363 ? -16.198 40.607  14.113  1.00 39.77 ? 363 ARG C CA    1 
ATOM   2589  C C     . ARG A  1 363 ? -15.371 41.019  15.334  1.00 41.17 ? 363 ARG C C     1 
ATOM   2590  O O     . ARG A  1 363 ? -14.526 41.922  15.252  1.00 40.46 ? 363 ARG C O     1 
ATOM   2591  C CB    . ARG A  1 363 ? -17.673 40.977  14.295  1.00 42.26 ? 363 ARG C CB    1 
ATOM   2592  C CG    . ARG A  1 363 ? -18.020 42.422  13.961  1.00 43.30 ? 363 ARG C CG    1 
ATOM   2593  C CD    . ARG A  1 363 ? -19.437 42.544  13.408  1.00 49.34 ? 363 ARG C CD    1 
ATOM   2594  N NE    . ARG A  1 363 ? -19.473 42.435  11.949  1.00 63.02 ? 363 ARG C NE    1 
ATOM   2595  C CZ    . ARG A  1 363 ? -19.821 41.337  11.284  1.00 60.34 ? 363 ARG C CZ    1 
ATOM   2596  N NH1   . ARG A  1 363 ? -20.183 40.229  11.913  1.00 58.25 ? 363 ARG C NH1   1 
ATOM   2597  N NH2   . ARG A  1 363 ? -19.786 41.344  9.953   1.00 55.87 ? 363 ARG C NH2   1 
ATOM   2598  N N     . ASN A  1 364 ? -15.574 40.346  16.469  1.00 39.40 ? 364 ASN C N     1 
ATOM   2599  C CA    . ASN A  1 364 ? -15.018 40.783  17.746  1.00 38.57 ? 364 ASN C CA    1 
ATOM   2600  C C     . ASN A  1 364 ? -14.084 39.771  18.382  1.00 39.11 ? 364 ASN C C     1 
ATOM   2601  O O     . ASN A  1 364 ? -13.740 39.922  19.562  1.00 36.39 ? 364 ASN C O     1 
ATOM   2602  C CB    . ASN A  1 364 ? -16.136 41.095  18.733  1.00 31.75 ? 364 ASN C CB    1 
ATOM   2603  C CG    . ASN A  1 364 ? -16.733 42.439  18.494  1.00 43.59 ? 364 ASN C CG    1 
ATOM   2604  O OD1   . ASN A  1 364 ? -16.015 43.428  18.311  1.00 45.84 ? 364 ASN C OD1   1 
ATOM   2605  N ND2   . ASN A  1 364 ? -18.061 42.496  18.465  1.00 47.08 ? 364 ASN C ND2   1 
ATOM   2606  N N     . ASN A  1 365 ? -13.676 38.739  17.656  1.00 37.63 ? 365 ASN C N     1 
ATOM   2607  C CA    . ASN A  1 365 ? -12.939 37.655  18.279  1.00 36.41 ? 365 ASN C CA    1 
ATOM   2608  C C     . ASN A  1 365 ? -11.760 37.278  17.401  1.00 41.35 ? 365 ASN C C     1 
ATOM   2609  O O     . ASN A  1 365 ? -11.653 37.682  16.237  1.00 46.70 ? 365 ASN C O     1 
ATOM   2610  C CB    . ASN A  1 365 ? -13.837 36.433  18.535  1.00 40.15 ? 365 ASN C CB    1 
ATOM   2611  C CG    . ASN A  1 365 ? -14.967 36.712  19.555  1.00 40.95 ? 365 ASN C CG    1 
ATOM   2612  O OD1   . ASN A  1 365 ? -14.938 36.226  20.691  1.00 42.08 ? 365 ASN C OD1   1 
ATOM   2613  N ND2   . ASN A  1 365 ? -15.966 37.478  19.135  1.00 35.15 ? 365 ASN C ND2   1 
ATOM   2614  N N     . PHE A  1 366 ? -10.852 36.523  17.995  1.00 39.50 ? 366 PHE C N     1 
ATOM   2615  C CA    . PHE A  1 366 ? -9.670  36.036  17.318  1.00 35.61 ? 366 PHE C CA    1 
ATOM   2616  C C     . PHE A  1 366 ? -9.435  34.622  17.812  1.00 38.80 ? 366 PHE C C     1 
ATOM   2617  O O     . PHE A  1 366 ? -9.787  34.295  18.948  1.00 39.32 ? 366 PHE C O     1 
ATOM   2618  C CB    . PHE A  1 366 ? -8.414  36.873  17.620  1.00 36.03 ? 366 PHE C CB    1 
ATOM   2619  C CG    . PHE A  1 366 ? -8.565  38.348  17.395  1.00 37.85 ? 366 PHE C CG    1 
ATOM   2620  C CD1   . PHE A  1 366 ? -9.387  39.122  18.192  1.00 38.11 ? 366 PHE C CD1   1 
ATOM   2621  C CD2   . PHE A  1 366 ? -7.840  38.969  16.391  1.00 39.67 ? 366 PHE C CD2   1 
ATOM   2622  C CE1   . PHE A  1 366 ? -9.511  40.479  17.962  1.00 44.53 ? 366 PHE C CE1   1 
ATOM   2623  C CE2   . PHE A  1 366 ? -7.949  40.323  16.165  1.00 36.25 ? 366 PHE C CE2   1 
ATOM   2624  C CZ    . PHE A  1 366 ? -8.785  41.081  16.948  1.00 43.99 ? 366 PHE C CZ    1 
ATOM   2625  N N     . PHE A  1 367 ? -8.836  33.778  16.975  1.00 32.43 ? 367 PHE C N     1 
ATOM   2626  C CA    . PHE A  1 367 ? -8.411  32.494  17.498  1.00 34.48 ? 367 PHE C CA    1 
ATOM   2627  C C     . PHE A  1 367 ? -7.050  32.127  16.931  1.00 36.43 ? 367 PHE C C     1 
ATOM   2628  O O     . PHE A  1 367 ? -6.584  32.703  15.947  1.00 41.24 ? 367 PHE C O     1 
ATOM   2629  C CB    . PHE A  1 367 ? -9.483  31.400  17.280  1.00 35.91 ? 367 PHE C CB    1 
ATOM   2630  C CG    . PHE A  1 367 ? -9.655  30.902  15.859  1.00 32.91 ? 367 PHE C CG    1 
ATOM   2631  C CD1   . PHE A  1 367 ? -8.676  30.154  15.219  1.00 33.54 ? 367 PHE C CD1   1 
ATOM   2632  C CD2   . PHE A  1 367 ? -10.861 31.084  15.210  1.00 34.52 ? 367 PHE C CD2   1 
ATOM   2633  C CE1   . PHE A  1 367 ? -8.875  29.665  13.950  1.00 31.03 ? 367 PHE C CE1   1 
ATOM   2634  C CE2   . PHE A  1 367 ? -11.071 30.574  13.931  1.00 35.44 ? 367 PHE C CE2   1 
ATOM   2635  C CZ    . PHE A  1 367 ? -10.082 29.854  13.314  1.00 29.98 ? 367 PHE C CZ    1 
ATOM   2636  N N     . SER A  1 368 ? -6.397  31.179  17.602  1.00 34.27 ? 368 SER C N     1 
ATOM   2637  C CA    . SER A  1 368 ? -5.048  30.772  17.242  1.00 34.72 ? 368 SER C CA    1 
ATOM   2638  C C     . SER A  1 368 ? -4.783  29.397  17.819  1.00 37.77 ? 368 SER C C     1 
ATOM   2639  O O     . SER A  1 368 ? -5.027  29.170  19.013  1.00 34.81 ? 368 SER C O     1 
ATOM   2640  C CB    . SER A  1 368 ? -4.005  31.757  17.760  1.00 37.56 ? 368 SER C CB    1 
ATOM   2641  O OG    . SER A  1 368 ? -2.704  31.198  17.682  1.00 41.00 ? 368 SER C OG    1 
ATOM   2642  N N     . SER A  1 369 ? -4.287  28.496  16.969  1.00 37.89 ? 369 SER C N     1 
ATOM   2643  C CA    . SER A  1 369 ? -3.993  27.121  17.340  1.00 34.45 ? 369 SER C CA    1 
ATOM   2644  C C     . SER A  1 369 ? -2.524  26.968  17.691  1.00 30.98 ? 369 SER C C     1 
ATOM   2645  O O     . SER A  1 369 ? -1.710  27.867  17.488  1.00 31.70 ? 369 SER C O     1 
ATOM   2646  C CB    . SER A  1 369 ? -4.377  26.136  16.220  1.00 31.49 ? 369 SER C CB    1 
ATOM   2647  O OG    . SER A  1 369 ? -3.756  26.435  14.978  1.00 28.91 ? 369 SER C OG    1 
ATOM   2648  N N     . ILE A  1 370 ? -2.211  25.798  18.239  1.00 31.94 ? 370 ILE C N     1 
ATOM   2649  C CA    . ILE A  1 370 ? -0.875  25.399  18.665  1.00 34.39 ? 370 ILE C CA    1 
ATOM   2650  C C     . ILE A  1 370 ? -0.701  23.938  18.305  1.00 33.69 ? 370 ILE C C     1 
ATOM   2651  O O     . ILE A  1 370 ? -1.586  23.120  18.584  1.00 35.44 ? 370 ILE C O     1 
ATOM   2652  C CB    . ILE A  1 370 ? -0.668  25.556  20.189  1.00 42.79 ? 370 ILE C CB    1 
ATOM   2653  C CG1   . ILE A  1 370 ? -1.047  26.965  20.676  1.00 45.54 ? 370 ILE C CG1   1 
ATOM   2654  C CG2   . ILE A  1 370 ? 0.746   25.147  20.576  1.00 31.92 ? 370 ILE C CG2   1 
ATOM   2655  C CD1   . ILE A  1 370 ? -1.832  26.966  22.005  1.00 35.49 ? 370 ILE C CD1   1 
ATOM   2656  N N     . LEU A  1 371 ? 0.443   23.595  17.735  1.00 30.12 ? 371 LEU C N     1 
ATOM   2657  C CA    . LEU A  1 371 ? 0.652   22.224  17.318  1.00 30.07 ? 371 LEU C CA    1 
ATOM   2658  C C     . LEU A  1 371 ? 1.693   21.482  18.145  1.00 36.65 ? 371 LEU C C     1 
ATOM   2659  O O     . LEU A  1 371 ? 1.628   20.254  18.222  1.00 37.80 ? 371 LEU C O     1 
ATOM   2660  C CB    . LEU A  1 371 ? 1.048   22.204  15.839  1.00 43.07 ? 371 LEU C CB    1 
ATOM   2661  C CG    . LEU A  1 371 ? -0.005  21.976  14.751  1.00 43.91 ? 371 LEU C CG    1 
ATOM   2662  C CD1   . LEU A  1 371 ? -1.301  22.692  15.078  1.00 38.88 ? 371 LEU C CD1   1 
ATOM   2663  C CD2   . LEU A  1 371 ? 0.527   22.450  13.400  1.00 40.67 ? 371 LEU C CD2   1 
ATOM   2664  N N     . ASN A  1 372 ? 2.606   22.185  18.816  1.00 37.92 ? 372 ASN C N     1 
ATOM   2665  C CA    . ASN A  1 372 ? 3.784   21.550  19.388  1.00 35.59 ? 372 ASN C CA    1 
ATOM   2666  C C     . ASN A  1 372 ? 3.775   21.487  20.912  1.00 39.07 ? 372 ASN C C     1 
ATOM   2667  O O     . ASN A  1 372 ? 4.843   21.382  21.518  1.00 43.56 ? 372 ASN C O     1 
ATOM   2668  C CB    . ASN A  1 372 ? 5.047   22.263  18.901  1.00 37.28 ? 372 ASN C CB    1 
ATOM   2669  C CG    . ASN A  1 372 ? 4.983   23.760  19.087  1.00 38.65 ? 372 ASN C CG    1 
ATOM   2670  O OD1   . ASN A  1 372 ? 4.301   24.252  19.971  1.00 41.37 ? 372 ASN C OD1   1 
ATOM   2671  N ND2   . ASN A  1 372 ? 5.700   24.492  18.251  1.00 45.36 ? 372 ASN C ND2   1 
ATOM   2672  N N     . VAL A  1 373 ? 2.610   21.540  21.558  1.00 36.79 ? 373 VAL C N     1 
ATOM   2673  C CA    . VAL A  1 373 ? 2.607   21.321  22.999  1.00 40.83 ? 373 VAL C CA    1 
ATOM   2674  C C     . VAL A  1 373 ? 3.100   19.909  23.269  1.00 37.54 ? 373 VAL C C     1 
ATOM   2675  O O     . VAL A  1 373 ? 2.865   18.980  22.483  1.00 33.34 ? 373 VAL C O     1 
ATOM   2676  C CB    . VAL A  1 373 ? 1.217   21.569  23.615  1.00 38.27 ? 373 VAL C CB    1 
ATOM   2677  C CG1   . VAL A  1 373 ? 1.116   20.975  25.016  1.00 33.54 ? 373 VAL C CG1   1 
ATOM   2678  C CG2   . VAL A  1 373 ? 0.962   23.043  23.712  1.00 32.15 ? 373 VAL C CG2   1 
ATOM   2679  N N     . VAL A  1 374 ? 3.849   19.759  24.352  1.00 33.73 ? 374 VAL C N     1 
ATOM   2680  C CA    . VAL A  1 374 ? 4.241   18.439  24.807  1.00 37.59 ? 374 VAL C CA    1 
ATOM   2681  C C     . VAL A  1 374 ? 2.964   17.615  24.908  1.00 37.23 ? 374 VAL C C     1 
ATOM   2682  O O     . VAL A  1 374 ? 2.018   18.023  25.598  1.00 38.29 ? 374 VAL C O     1 
ATOM   2683  C CB    . VAL A  1 374 ? 4.996   18.523  26.141  1.00 40.49 ? 374 VAL C CB    1 
ATOM   2684  C CG1   . VAL A  1 374 ? 5.514   17.149  26.568  1.00 39.38 ? 374 VAL C CG1   1 
ATOM   2685  C CG2   . VAL A  1 374 ? 6.138   19.521  26.020  1.00 39.91 ? 374 VAL C CG2   1 
ATOM   2686  N N     . PRO A  1 375 ? 2.866   16.496  24.194  1.00 36.60 ? 375 PRO C N     1 
ATOM   2687  C CA    . PRO A  1 375 ? 1.672   15.657  24.289  1.00 37.24 ? 375 PRO C CA    1 
ATOM   2688  C C     . PRO A  1 375 ? 1.461   15.232  25.721  1.00 41.61 ? 375 PRO C C     1 
ATOM   2689  O O     . PRO A  1 375 ? 2.403   15.158  26.512  1.00 45.82 ? 375 PRO C O     1 
ATOM   2690  C CB    . PRO A  1 375 ? 2.003   14.453  23.402  1.00 37.16 ? 375 PRO C CB    1 
ATOM   2691  C CG    . PRO A  1 375 ? 3.050   14.936  22.489  1.00 36.75 ? 375 PRO C CG    1 
ATOM   2692  C CD    . PRO A  1 375 ? 3.861   15.929  23.273  1.00 41.84 ? 375 PRO C CD    1 
ATOM   2693  N N     . ALA A  1 376 ? 0.209   14.950  26.060  1.00 38.33 ? 376 ALA C N     1 
ATOM   2694  C CA    . ALA A  1 376 ? -0.049  14.589  27.447  1.00 42.90 ? 376 ALA C CA    1 
ATOM   2695  C C     . ALA A  1 376 ? -1.398  13.915  27.573  1.00 42.83 ? 376 ALA C C     1 
ATOM   2696  O O     . ALA A  1 376 ? -2.279  14.079  26.726  1.00 46.02 ? 376 ALA C O     1 
ATOM   2697  C CB    . ALA A  1 376 ? 0.006   15.809  28.360  1.00 45.49 ? 376 ALA C CB    1 
ATOM   2698  N N     . GLY A  1 377 ? -1.539  13.131  28.638  1.00 35.62 ? 377 GLY C N     1 
ATOM   2699  C CA    . GLY A  1 377 ? -2.858  12.682  29.012  1.00 41.25 ? 377 GLY C CA    1 
ATOM   2700  C C     . GLY A  1 377 ? -3.798  13.865  29.146  1.00 46.09 ? 377 GLY C C     1 
ATOM   2701  O O     . GLY A  1 377 ? -3.377  14.993  29.433  1.00 47.14 ? 377 GLY C O     1 
ATOM   2702  N N     . LEU A  1 378 ? -5.082  13.625  28.865  1.00 43.50 ? 378 LEU C N     1 
ATOM   2703  C CA    . LEU A  1 378 ? -6.016  14.739  28.857  1.00 43.24 ? 378 LEU C CA    1 
ATOM   2704  C C     . LEU A  1 378 ? -6.040  15.426  30.212  1.00 33.73 ? 378 LEU C C     1 
ATOM   2705  O O     . LEU A  1 378 ? -5.892  16.649  30.296  1.00 35.03 ? 378 LEU C O     1 
ATOM   2706  C CB    . LEU A  1 378 ? -7.419  14.283  28.449  1.00 44.94 ? 378 LEU C CB    1 
ATOM   2707  C CG    . LEU A  1 378 ? -8.334  15.494  28.139  1.00 40.03 ? 378 LEU C CG    1 
ATOM   2708  C CD1   . LEU A  1 378 ? -7.584  16.554  27.319  1.00 36.09 ? 378 LEU C CD1   1 
ATOM   2709  C CD2   . LEU A  1 378 ? -9.631  15.103  27.437  1.00 34.74 ? 378 LEU C CD2   1 
ATOM   2710  N N     . ALA A  1 379 ? -6.178  14.653  31.289  1.00 39.46 ? 379 ALA C N     1 
ATOM   2711  C CA    . ALA A  1 379 ? -6.228  15.265  32.614  1.00 34.71 ? 379 ALA C CA    1 
ATOM   2712  C C     . ALA A  1 379 ? -5.043  16.187  32.837  1.00 37.03 ? 379 ALA C C     1 
ATOM   2713  O O     . ALA A  1 379 ? -5.209  17.335  33.262  1.00 41.27 ? 379 ALA C O     1 
ATOM   2714  C CB    . ALA A  1 379 ? -6.280  14.194  33.690  1.00 37.46 ? 379 ALA C CB    1 
ATOM   2715  N N     . ASP A  1 380 ? -3.843  15.731  32.498  1.00 36.77 ? 380 ASP C N     1 
ATOM   2716  C CA    . ASP A  1 380 ? -2.672  16.576  32.701  1.00 42.17 ? 380 ASP C CA    1 
ATOM   2717  C C     . ASP A  1 380 ? -2.735  17.821  31.822  1.00 40.23 ? 380 ASP C C     1 
ATOM   2718  O O     . ASP A  1 380 ? -2.497  18.942  32.292  1.00 38.62 ? 380 ASP C O     1 
ATOM   2719  C CB    . ASP A  1 380 ? -1.409  15.759  32.441  1.00 37.89 ? 380 ASP C CB    1 
ATOM   2720  C CG    . ASP A  1 380 ? -1.328  14.552  33.351  1.00 47.76 ? 380 ASP C CG    1 
ATOM   2721  O OD1   . ASP A  1 380 ? -1.152  14.748  34.577  1.00 51.89 ? 380 ASP C OD1   1 
ATOM   2722  O OD2   . ASP A  1 380 ? -1.497  13.411  32.860  1.00 51.92 ? 380 ASP C OD2   1 
ATOM   2723  N N     . LEU A  1 381 ? -3.080  17.647  30.548  1.00 36.81 ? 381 LEU C N     1 
ATOM   2724  C CA    . LEU A  1 381 ? -3.143  18.797  29.655  1.00 39.65 ? 381 LEU C CA    1 
ATOM   2725  C C     . LEU A  1 381 ? -4.129  19.824  30.182  1.00 37.78 ? 381 LEU C C     1 
ATOM   2726  O O     . LEU A  1 381 ? -3.863  21.032  30.151  1.00 37.36 ? 381 LEU C O     1 
ATOM   2727  C CB    . LEU A  1 381 ? -3.527  18.350  28.243  1.00 38.36 ? 381 LEU C CB    1 
ATOM   2728  C CG    . LEU A  1 381 ? -2.323  18.046  27.358  1.00 40.47 ? 381 LEU C CG    1 
ATOM   2729  C CD1   . LEU A  1 381 ? -2.762  17.462  26.030  1.00 39.24 ? 381 LEU C CD1   1 
ATOM   2730  C CD2   . LEU A  1 381 ? -1.435  19.292  27.167  1.00 43.07 ? 381 LEU C CD2   1 
ATOM   2731  N N     . LEU A  1 382 ? -5.266  19.360  30.695  1.00 38.06 ? 382 LEU C N     1 
ATOM   2732  C CA    . LEU A  1 382 ? -6.219  20.276  31.308  1.00 44.19 ? 382 LEU C CA    1 
ATOM   2733  C C     . LEU A  1 382 ? -5.666  20.895  32.595  1.00 43.05 ? 382 LEU C C     1 
ATOM   2734  O O     . LEU A  1 382 ? -5.979  22.051  32.895  1.00 39.90 ? 382 LEU C O     1 
ATOM   2735  C CB    . LEU A  1 382 ? -7.545  19.552  31.569  1.00 39.05 ? 382 LEU C CB    1 
ATOM   2736  C CG    . LEU A  1 382 ? -8.548  19.430  30.396  1.00 40.94 ? 382 LEU C CG    1 
ATOM   2737  C CD1   . LEU A  1 382 ? -9.672  18.434  30.685  1.00 25.25 ? 382 LEU C CD1   1 
ATOM   2738  C CD2   . LEU A  1 382 ? -9.150  20.775  29.958  1.00 36.50 ? 382 LEU C CD2   1 
ATOM   2739  N N     . ARG A  1 383 ? -4.842  20.170  33.361  1.00 35.19 ? 383 ARG C N     1 
ATOM   2740  C CA    . ARG A  1 383 ? -4.220  20.793  34.525  1.00 36.14 ? 383 ARG C CA    1 
ATOM   2741  C C     . ARG A  1 383 ? -3.405  21.997  34.104  1.00 36.71 ? 383 ARG C C     1 
ATOM   2742  O O     . ARG A  1 383 ? -3.532  23.091  34.675  1.00 35.15 ? 383 ARG C O     1 
ATOM   2743  C CB    . ARG A  1 383 ? -3.327  19.793  35.258  1.00 40.29 ? 383 ARG C CB    1 
ATOM   2744  C CG    . ARG A  1 383 ? -3.947  19.190  36.506  1.00 44.46 ? 383 ARG C CG    1 
ATOM   2745  C CD    . ARG A  1 383 ? -3.808  20.041  37.761  1.00 34.54 ? 383 ARG C CD    1 
ATOM   2746  N NE    . ARG A  1 383 ? -4.960  20.908  37.974  1.00 28.68 ? 383 ARG C NE    1 
ATOM   2747  C CZ    . ARG A  1 383 ? -4.857  22.211  38.189  1.00 33.94 ? 383 ARG C CZ    1 
ATOM   2748  N NH1   . ARG A  1 383 ? -3.674  22.807  38.229  1.00 29.35 ? 383 ARG C NH1   1 
ATOM   2749  N NH2   . ARG A  1 383 ? -5.964  22.935  38.363  1.00 34.63 ? 383 ARG C NH2   1 
ATOM   2750  N N     . SER A  1 384 ? -2.568  21.801  33.084  1.00 32.96 ? 384 SER C N     1 
ATOM   2751  C CA    . SER A  1 384 ? -1.637  22.830  32.638  1.00 37.14 ? 384 SER C CA    1 
ATOM   2752  C C     . SER A  1 384 ? -2.351  24.139  32.319  1.00 34.32 ? 384 SER C C     1 
ATOM   2753  O O     . SER A  1 384 ? -1.973  25.206  32.808  1.00 35.02 ? 384 SER C O     1 
ATOM   2754  C CB    . SER A  1 384 ? -0.880  22.321  31.414  1.00 38.35 ? 384 SER C CB    1 
ATOM   2755  O OG    . SER A  1 384 ? -0.447  20.989  31.613  1.00 41.80 ? 384 SER C OG    1 
ATOM   2756  N N     . LEU A  1 385 ? -3.393  24.075  31.495  1.00 34.59 ? 385 LEU C N     1 
ATOM   2757  C CA    . LEU A  1 385 ? -4.135  25.284  31.162  1.00 37.89 ? 385 LEU C CA    1 
ATOM   2758  C C     . LEU A  1 385 ? -4.589  25.998  32.431  1.00 38.91 ? 385 LEU C C     1 
ATOM   2759  O O     . LEU A  1 385 ? -4.282  27.177  32.639  1.00 40.48 ? 385 LEU C O     1 
ATOM   2760  C CB    . LEU A  1 385 ? -5.326  24.941  30.260  1.00 36.61 ? 385 LEU C CB    1 
ATOM   2761  C CG    . LEU A  1 385 ? -5.071  24.272  28.895  1.00 43.57 ? 385 LEU C CG    1 
ATOM   2762  C CD1   . LEU A  1 385 ? -6.378  23.844  28.237  1.00 32.75 ? 385 LEU C CD1   1 
ATOM   2763  C CD2   . LEU A  1 385 ? -4.271  25.170  27.937  1.00 36.55 ? 385 LEU C CD2   1 
ATOM   2764  N N     . GLU A  1 386 ? -5.298  25.278  33.306  1.00 37.91 ? 386 GLU C N     1 
ATOM   2765  C CA    . GLU A  1 386 ? -5.622  25.795  34.636  1.00 43.72 ? 386 GLU C CA    1 
ATOM   2766  C C     . GLU A  1 386 ? -4.391  26.387  35.305  1.00 38.32 ? 386 GLU C C     1 
ATOM   2767  O O     . GLU A  1 386 ? -4.419  27.513  35.812  1.00 32.97 ? 386 GLU C O     1 
ATOM   2768  C CB    . GLU A  1 386 ? -6.222  24.679  35.511  1.00 41.17 ? 386 GLU C CB    1 
ATOM   2769  C CG    . GLU A  1 386 ? -7.752  24.578  35.426  1.00 43.63 ? 386 GLU C CG    1 
ATOM   2770  C CD    . GLU A  1 386 ? -8.334  23.330  36.083  1.00 40.86 ? 386 GLU C CD    1 
ATOM   2771  O OE1   . GLU A  1 386 ? -8.274  22.262  35.449  1.00 37.29 ? 386 GLU C OE1   1 
ATOM   2772  O OE2   . GLU A  1 386 ? -8.881  23.420  37.211  1.00 43.68 ? 386 GLU C OE2   1 
ATOM   2773  N N     . ARG A  1 387 ? -3.292  25.643  35.305  1.00 34.45 ? 387 ARG C N     1 
ATOM   2774  C CA    . ARG A  1 387 ? -2.091  26.179  35.921  1.00 41.21 ? 387 ARG C CA    1 
ATOM   2775  C C     . ARG A  1 387 ? -1.675  27.481  35.249  1.00 36.50 ? 387 ARG C C     1 
ATOM   2776  O O     . ARG A  1 387 ? -1.309  28.444  35.923  1.00 38.21 ? 387 ARG C O     1 
ATOM   2777  C CB    . ARG A  1 387 ? -0.981  25.141  35.844  1.00 41.81 ? 387 ARG C CB    1 
ATOM   2778  C CG    . ARG A  1 387 ? 0.155   25.381  36.793  1.00 33.56 ? 387 ARG C CG    1 
ATOM   2779  C CD    . ARG A  1 387 ? 0.728   24.055  37.230  1.00 37.48 ? 387 ARG C CD    1 
ATOM   2780  N NE    . ARG A  1 387 ? 0.857   23.122  36.112  1.00 39.48 ? 387 ARG C NE    1 
ATOM   2781  C CZ    . ARG A  1 387 ? 0.071   22.064  35.922  1.00 40.97 ? 387 ARG C CZ    1 
ATOM   2782  N NH1   . ARG A  1 387 ? -0.982  21.839  36.684  1.00 45.06 ? 387 ARG C NH1   1 
ATOM   2783  N NH2   . ARG A  1 387 ? 0.338   21.215  34.933  1.00 46.94 ? 387 ARG C NH2   1 
ATOM   2784  N N     . ALA A  1 388 ? -1.754  27.534  33.918  1.00 39.50 ? 388 ALA C N     1 
ATOM   2785  C CA    . ALA A  1 388 ? -1.454  28.741  33.157  1.00 41.45 ? 388 ALA C CA    1 
ATOM   2786  C C     . ALA A  1 388 ? -2.536  29.809  33.266  1.00 38.50 ? 388 ALA C C     1 
ATOM   2787  O O     . ALA A  1 388 ? -2.319  30.928  32.792  1.00 41.87 ? 388 ALA C O     1 
ATOM   2788  C CB    . ALA A  1 388 ? -1.240  28.391  31.680  1.00 40.97 ? 388 ALA C CB    1 
ATOM   2789  N N     . GLY A  1 389 ? -3.693  29.489  33.845  1.00 37.57 ? 389 GLY C N     1 
ATOM   2790  C CA    . GLY A  1 389 ? -4.786  30.445  33.984  1.00 33.77 ? 389 GLY C CA    1 
ATOM   2791  C C     . GLY A  1 389 ? -5.583  30.729  32.727  1.00 36.47 ? 389 GLY C C     1 
ATOM   2792  O O     . GLY A  1 389 ? -6.204  31.794  32.625  1.00 36.00 ? 389 GLY C O     1 
ATOM   2793  N N     . VAL A  1 390 ? -5.600  29.801  31.765  1.00 40.01 ? 390 VAL C N     1 
ATOM   2794  C CA    . VAL A  1 390 ? -6.179  30.044  30.446  1.00 35.72 ? 390 VAL C CA    1 
ATOM   2795  C C     . VAL A  1 390 ? -7.001  28.870  29.915  1.00 34.15 ? 390 VAL C C     1 
ATOM   2796  O O     . VAL A  1 390 ? -7.172  28.746  28.698  1.00 34.41 ? 390 VAL C O     1 
ATOM   2797  C CB    . VAL A  1 390 ? -5.079  30.396  29.424  1.00 37.23 ? 390 VAL C CB    1 
ATOM   2798  C CG1   . VAL A  1 390 ? -4.268  31.612  29.859  1.00 40.38 ? 390 VAL C CG1   1 
ATOM   2799  C CG2   . VAL A  1 390 ? -4.149  29.204  29.231  1.00 43.56 ? 390 VAL C CG2   1 
ATOM   2800  N N     . ARG A  1 391 ? -7.535  28.004  30.780  1.00 30.91 ? 391 ARG C N     1 
ATOM   2801  C CA    . ARG A  1 391 ? -8.454  26.998  30.258  1.00 30.01 ? 391 ARG C CA    1 
ATOM   2802  C C     . ARG A  1 391 ? -9.744  27.680  29.843  1.00 36.73 ? 391 ARG C C     1 
ATOM   2803  O O     . ARG A  1 391 ? -10.265 28.535  30.570  1.00 31.43 ? 391 ARG C O     1 
ATOM   2804  C CB    . ARG A  1 391 ? -8.768  25.897  31.270  1.00 27.34 ? 391 ARG C CB    1 
ATOM   2805  C CG    . ARG A  1 391 ? -10.002 25.088  30.843  1.00 21.40 ? 391 ARG C CG    1 
ATOM   2806  C CD    . ARG A  1 391 ? -10.365 23.961  31.788  1.00 24.54 ? 391 ARG C CD    1 
ATOM   2807  N NE    . ARG A  1 391 ? -11.399 23.091  31.231  1.00 30.11 ? 391 ARG C NE    1 
ATOM   2808  C CZ    . ARG A  1 391 ? -11.872 22.000  31.827  1.00 38.24 ? 391 ARG C CZ    1 
ATOM   2809  N NH1   . ARG A  1 391 ? -11.408 21.591  33.002  1.00 33.33 ? 391 ARG C NH1   1 
ATOM   2810  N NH2   . ARG A  1 391 ? -12.839 21.303  31.234  1.00 35.67 ? 391 ARG C NH2   1 
ATOM   2811  N N     . TYR A  1 392 ? -10.242 27.313  28.659  1.00 36.65 ? 392 TYR C N     1 
ATOM   2812  C CA    . TYR A  1 392 ? -11.384 27.982  28.059  1.00 36.37 ? 392 TYR C CA    1 
ATOM   2813  C C     . TYR A  1 392 ? -12.465 28.251  29.081  1.00 38.48 ? 392 TYR C C     1 
ATOM   2814  O O     . TYR A  1 392 ? -13.026 27.319  29.664  1.00 38.95 ? 392 TYR C O     1 
ATOM   2815  C CB    . TYR A  1 392 ? -11.979 27.158  26.937  1.00 37.98 ? 392 TYR C CB    1 
ATOM   2816  C CG    . TYR A  1 392 ? -13.089 27.941  26.295  1.00 38.85 ? 392 TYR C CG    1 
ATOM   2817  C CD1   . TYR A  1 392 ? -12.803 29.089  25.556  1.00 38.77 ? 392 TYR C CD1   1 
ATOM   2818  C CD2   . TYR A  1 392 ? -14.408 27.583  26.467  1.00 34.83 ? 392 TYR C CD2   1 
ATOM   2819  C CE1   . TYR A  1 392 ? -13.804 29.830  24.973  1.00 39.68 ? 392 TYR C CE1   1 
ATOM   2820  C CE2   . TYR A  1 392 ? -15.422 28.320  25.881  1.00 39.34 ? 392 TYR C CE2   1 
ATOM   2821  C CZ    . TYR A  1 392 ? -15.115 29.448  25.141  1.00 40.14 ? 392 TYR C CZ    1 
ATOM   2822  O OH    . TYR A  1 392 ? -16.122 30.192  24.564  1.00 38.99 ? 392 TYR C OH    1 
ATOM   2823  N N     . ASP A  1 393 ? -12.759 29.529  29.296  1.00 41.92 ? 393 ASP C N     1 
ATOM   2824  C CA    . ASP A  1 393 ? -13.742 29.947  30.285  1.00 39.75 ? 393 ASP C CA    1 
ATOM   2825  C C     . ASP A  1 393 ? -15.050 30.170  29.554  1.00 39.87 ? 393 ASP C C     1 
ATOM   2826  O O     . ASP A  1 393 ? -15.200 31.153  28.820  1.00 41.96 ? 393 ASP C O     1 
ATOM   2827  C CB    . ASP A  1 393 ? -13.297 31.207  31.020  1.00 44.86 ? 393 ASP C CB    1 
ATOM   2828  C CG    . ASP A  1 393 ? -14.305 31.667  32.069  1.00 48.27 ? 393 ASP C CG    1 
ATOM   2829  O OD1   . ASP A  1 393 ? -15.396 31.059  32.211  1.00 39.56 ? 393 ASP C OD1   1 
ATOM   2830  O OD2   . ASP A  1 393 ? -13.993 32.658  32.762  1.00 54.89 ? 393 ASP C OD2   1 
ATOM   2831  N N     . LYS A  1 394 ? -15.989 29.249  29.761  1.00 39.67 ? 394 LYS C N     1 
ATOM   2832  C CA    . LYS A  1 394 ? -17.298 29.367  29.135  1.00 44.32 ? 394 LYS C CA    1 
ATOM   2833  C C     . LYS A  1 394 ? -17.930 30.718  29.435  1.00 46.93 ? 394 LYS C C     1 
ATOM   2834  O O     . LYS A  1 394 ? -18.574 31.319  28.566  1.00 42.39 ? 394 LYS C O     1 
ATOM   2835  C CB    . LYS A  1 394 ? -18.199 28.230  29.614  1.00 39.15 ? 394 LYS C CB    1 
ATOM   2836  C CG    . LYS A  1 394 ? -19.561 28.197  28.952  1.00 42.10 ? 394 LYS C CG    1 
ATOM   2837  C CD    . LYS A  1 394 ? -19.490 28.552  27.453  1.00 53.68 ? 394 LYS C CD    1 
ATOM   2838  C CE    . LYS A  1 394 ? -18.710 27.529  26.606  1.00 44.64 ? 394 LYS C CE    1 
ATOM   2839  N NZ    . LYS A  1 394 ? -19.309 26.161  26.589  1.00 36.53 ? 394 LYS C NZ    1 
ATOM   2840  N N     . ASP A  1 395 ? -17.728 31.224  30.655  1.00 47.36 ? 395 ASP C N     1 
ATOM   2841  C CA    . ASP A  1 395 ? -18.355 32.475  31.056  1.00 45.13 ? 395 ASP C CA    1 
ATOM   2842  C C     . ASP A  1 395 ? -17.878 33.632  30.182  1.00 42.99 ? 395 ASP C C     1 
ATOM   2843  O O     . ASP A  1 395 ? -18.690 34.434  29.710  1.00 52.37 ? 395 ASP C O     1 
ATOM   2844  C CB    . ASP A  1 395 ? -18.078 32.748  32.547  1.00 48.71 ? 395 ASP C CB    1 
ATOM   2845  C CG    . ASP A  1 395 ? -18.892 31.833  33.490  1.00 51.34 ? 395 ASP C CG    1 
ATOM   2846  O OD1   . ASP A  1 395 ? -20.139 31.784  33.360  1.00 45.51 ? 395 ASP C OD1   1 
ATOM   2847  O OD2   . ASP A  1 395 ? -18.278 31.168  34.365  1.00 51.19 ? 395 ASP C OD2   1 
ATOM   2848  N N     . SER A  1 396 ? -16.569 33.723  29.936  1.00 41.91 ? 396 SER C N     1 
ATOM   2849  C CA    . SER A  1 396 ? -15.988 34.828  29.184  1.00 38.03 ? 396 SER C CA    1 
ATOM   2850  C C     . SER A  1 396 ? -15.622 34.468  27.753  1.00 43.33 ? 396 SER C C     1 
ATOM   2851  O O     . SER A  1 396 ? -15.094 35.324  27.038  1.00 43.09 ? 396 SER C O     1 
ATOM   2852  C CB    . SER A  1 396 ? -14.737 35.352  29.886  1.00 40.08 ? 396 SER C CB    1 
ATOM   2853  O OG    . SER A  1 396 ? -13.637 34.496  29.632  1.00 44.03 ? 396 SER C OG    1 
ATOM   2854  N N     . GLY A  1 397 ? -15.864 33.232  27.316  1.00 48.18 ? 397 GLY C N     1 
ATOM   2855  C CA    . GLY A  1 397 ? -15.507 32.845  25.956  1.00 44.41 ? 397 GLY C CA    1 
ATOM   2856  C C     . GLY A  1 397 ? -14.037 32.981  25.616  1.00 39.80 ? 397 GLY C C     1 
ATOM   2857  O O     . GLY A  1 397 ? -13.688 33.109  24.438  1.00 37.37 ? 397 GLY C O     1 
ATOM   2858  N N     . GLU A  1 398 ? -13.165 32.952  26.623  1.00 41.92 ? 398 GLU C N     1 
ATOM   2859  C CA    . GLU A  1 398 ? -11.728 33.106  26.472  1.00 36.35 ? 398 GLU C CA    1 
ATOM   2860  C C     . GLU A  1 398 ? -11.036 31.833  26.949  1.00 37.75 ? 398 GLU C C     1 
ATOM   2861  O O     . GLU A  1 398 ? -11.567 31.116  27.805  1.00 39.93 ? 398 GLU C O     1 
ATOM   2862  C CB    . GLU A  1 398 ? -11.241 34.322  27.272  1.00 36.13 ? 398 GLU C CB    1 
ATOM   2863  C CG    . GLU A  1 398 ? -11.939 35.621  26.896  1.00 33.53 ? 398 GLU C CG    1 
ATOM   2864  C CD    . GLU A  1 398 ? -10.971 36.779  26.719  1.00 42.57 ? 398 GLU C CD    1 
ATOM   2865  O OE1   . GLU A  1 398 ? -10.099 36.988  27.598  1.00 46.30 ? 398 GLU C OE1   1 
ATOM   2866  O OE2   . GLU A  1 398 ? -11.071 37.475  25.688  1.00 39.78 ? 398 GLU C OE2   1 
ATOM   2867  N N     . GLY A  1 399 ? -9.866  31.535  26.380  1.00 32.01 ? 399 GLY C N     1 
ATOM   2868  C CA    . GLY A  1 399 ? -9.068  30.406  26.820  1.00 30.02 ? 399 GLY C CA    1 
ATOM   2869  C C     . GLY A  1 399 ? -8.962  29.318  25.765  1.00 31.16 ? 399 GLY C C     1 
ATOM   2870  O O     . GLY A  1 399 ? -9.474  29.429  24.651  1.00 38.61 ? 399 GLY C O     1 
ATOM   2871  N N     . ALA A  1 400 ? -8.288  28.237  26.153  1.00 31.52 ? 400 ALA C N     1 
ATOM   2872  C CA    . ALA A  1 400 ? -7.854  27.194  25.235  1.00 25.92 ? 400 ALA C CA    1 
ATOM   2873  C C     . ALA A  1 400 ? -8.593  25.881  25.466  1.00 28.19 ? 400 ALA C C     1 
ATOM   2874  O O     . ALA A  1 400 ? -9.072  25.600  26.566  1.00 33.02 ? 400 ALA C O     1 
ATOM   2875  C CB    . ALA A  1 400 ? -6.361  26.949  25.381  1.00 30.93 ? 400 ALA C CB    1 
ATOM   2876  N N     . VAL A  1 401 ? -8.662  25.072  24.407  1.00 33.08 ? 401 VAL C N     1 
ATOM   2877  C CA    . VAL A  1 401 ? -9.396  23.806  24.383  1.00 27.21 ? 401 VAL C CA    1 
ATOM   2878  C C     . VAL A  1 401 ? -8.556  22.780  23.638  1.00 29.49 ? 401 VAL C C     1 
ATOM   2879  O O     . VAL A  1 401 ? -7.900  23.112  22.647  1.00 36.23 ? 401 VAL C O     1 
ATOM   2880  C CB    . VAL A  1 401 ? -10.786 23.941  23.714  1.00 30.69 ? 401 VAL C CB    1 
ATOM   2881  C CG1   . VAL A  1 401 ? -11.625 24.987  24.426  1.00 33.24 ? 401 VAL C CG1   1 
ATOM   2882  C CG2   . VAL A  1 401 ? -10.669 24.296  22.217  1.00 22.86 ? 401 VAL C CG2   1 
ATOM   2883  N N     . VAL A  1 402 ? -8.585  21.532  24.099  1.00 27.14 ? 402 VAL C N     1 
ATOM   2884  C CA    . VAL A  1 402 ? -7.741  20.496  23.518  1.00 27.53 ? 402 VAL C CA    1 
ATOM   2885  C C     . VAL A  1 402 ? -8.377  20.003  22.231  1.00 26.80 ? 402 VAL C C     1 
ATOM   2886  O O     . VAL A  1 402 ? -9.581  19.723  22.189  1.00 26.72 ? 402 VAL C O     1 
ATOM   2887  C CB    . VAL A  1 402 ? -7.534  19.337  24.504  1.00 29.33 ? 402 VAL C CB    1 
ATOM   2888  C CG1   . VAL A  1 402 ? -6.720  18.214  23.853  1.00 30.10 ? 402 VAL C CG1   1 
ATOM   2889  C CG2   . VAL A  1 402 ? -6.858  19.823  25.775  1.00 30.75 ? 402 VAL C CG2   1 
ATOM   2890  N N     . LEU A  1 403 ? -7.573  19.905  21.172  1.00 27.43 ? 403 LEU C N     1 
ATOM   2891  C CA    . LEU A  1 403 ? -8.037  19.261  19.948  1.00 30.43 ? 403 LEU C CA    1 
ATOM   2892  C C     . LEU A  1 403 ? -7.461  17.860  19.760  1.00 30.60 ? 403 LEU C C     1 
ATOM   2893  O O     . LEU A  1 403 ? -8.012  17.074  18.984  1.00 26.89 ? 403 LEU C O     1 
ATOM   2894  C CB    . LEU A  1 403 ? -7.713  20.118  18.720  1.00 28.59 ? 403 LEU C CB    1 
ATOM   2895  C CG    . LEU A  1 403 ? -8.393  21.472  18.470  1.00 34.37 ? 403 LEU C CG    1 
ATOM   2896  C CD1   . LEU A  1 403 ? -8.561  21.651  16.978  1.00 33.67 ? 403 LEU C CD1   1 
ATOM   2897  C CD2   . LEU A  1 403 ? -9.739  21.648  19.182  1.00 30.91 ? 403 LEU C CD2   1 
ATOM   2898  N N     . GLY A  1 404 ? -6.398  17.520  20.471  1.00 30.67 ? 404 GLY C N     1 
ATOM   2899  C CA    . GLY A  1 404 ? -5.853  16.184  20.412  1.00 28.71 ? 404 GLY C CA    1 
ATOM   2900  C C     . GLY A  1 404 ? -4.739  16.120  21.421  1.00 31.57 ? 404 GLY C C     1 
ATOM   2901  O O     . GLY A  1 404 ? -4.037  17.111  21.634  1.00 34.16 ? 404 GLY C O     1 
ATOM   2902  N N     . CYS A  1 405 ? -4.577  14.990  22.079  1.00 34.84 ? 405 CYS C N     1 
ATOM   2903  C CA    . CYS A  1 405 ? -3.600  14.933  23.156  1.00 40.14 ? 405 CYS C CA    1 
ATOM   2904  C C     . CYS A  1 405 ? -2.235  14.467  22.691  1.00 40.74 ? 405 CYS C C     1 
ATOM   2905  O O     . CYS A  1 405 ? -1.242  14.670  23.405  1.00 41.95 ? 405 CYS C O     1 
ATOM   2906  C CB    . CYS A  1 405 ? -4.101  14.011  24.262  1.00 41.33 ? 405 CYS C CB    1 
ATOM   2907  S SG    . CYS A  1 405 ? -5.681  14.504  24.887  1.00 38.69 ? 405 CYS C SG    1 
ATOM   2908  N N     . ASN A  1 406 ? -2.168  13.855  21.513  1.00 39.75 ? 406 ASN C N     1 
ATOM   2909  C CA    . ASN A  1 406 ? -0.915  13.346  20.982  1.00 39.08 ? 406 ASN C CA    1 
ATOM   2910  C C     . ASN A  1 406 ? -1.101  13.160  19.481  1.00 42.16 ? 406 ASN C C     1 
ATOM   2911  O O     . ASN A  1 406 ? -1.261  12.036  18.984  1.00 41.88 ? 406 ASN C O     1 
ATOM   2912  C CB    . ASN A  1 406 ? -0.538  12.051  21.693  1.00 34.29 ? 406 ASN C CB    1 
ATOM   2913  C CG    . ASN A  1 406 ? 0.565   11.325  21.006  1.00 35.99 ? 406 ASN C CG    1 
ATOM   2914  O OD1   . ASN A  1 406 ? 0.586   10.095  20.951  1.00 37.69 ? 406 ASN C OD1   1 
ATOM   2915  N ND2   . ASN A  1 406 ? 1.488   12.080  20.446  1.00 46.34 ? 406 ASN C ND2   1 
ATOM   2916  N N     . SER A  1 407 ? -1.134  14.268  18.759  1.00 34.82 ? 407 SER C N     1 
ATOM   2917  C CA    . SER A  1 407 ? -1.405  14.243  17.334  1.00 34.34 ? 407 SER C CA    1 
ATOM   2918  C C     . SER A  1 407 ? -0.090  14.395  16.572  1.00 39.53 ? 407 SER C C     1 
ATOM   2919  O O     . SER A  1 407 ? 0.841   15.051  17.044  1.00 38.87 ? 407 SER C O     1 
ATOM   2920  C CB    . SER A  1 407 ? -2.391  15.359  16.979  1.00 35.99 ? 407 SER C CB    1 
ATOM   2921  O OG    . SER A  1 407 ? -2.229  15.789  15.636  1.00 39.66 ? 407 SER C OG    1 
ATOM   2922  N N     . ASP A  1 408 ? 0.007   13.752  15.411  1.00 42.59 ? 408 ASP C N     1 
ATOM   2923  C CA    . ASP A  1 408 ? 1.184   13.954  14.574  1.00 42.23 ? 408 ASP C CA    1 
ATOM   2924  C C     . ASP A  1 408 ? 0.991   15.102  13.600  1.00 38.65 ? 408 ASP C C     1 
ATOM   2925  O O     . ASP A  1 408 ? 1.865   15.348  12.773  1.00 45.84 ? 408 ASP C O     1 
ATOM   2926  C CB    . ASP A  1 408 ? 1.582   12.666  13.829  1.00 38.14 ? 408 ASP C CB    1 
ATOM   2927  C CG    . ASP A  1 408 ? 0.437   11.686  13.678  1.00 51.94 ? 408 ASP C CG    1 
ATOM   2928  O OD1   . ASP A  1 408 ? -0.725  12.155  13.649  1.00 56.84 ? 408 ASP C OD1   1 
ATOM   2929  O OD2   . ASP A  1 408 ? 0.692   10.452  13.604  1.00 44.24 ? 408 ASP C OD2   1 
ATOM   2930  N N     . LEU A  1 409 ? -0.121  15.824  13.708  1.00 39.83 ? 409 LEU C N     1 
ATOM   2931  C CA    . LEU A  1 409 ? -0.304  17.080  12.997  1.00 37.26 ? 409 LEU C CA    1 
ATOM   2932  C C     . LEU A  1 409 ? 0.870   17.989  13.301  1.00 45.41 ? 409 LEU C C     1 
ATOM   2933  O O     . LEU A  1 409 ? 0.951   18.551  14.400  1.00 51.69 ? 409 LEU C O     1 
ATOM   2934  C CB    . LEU A  1 409 ? -1.602  17.752  13.422  1.00 35.36 ? 409 LEU C CB    1 
ATOM   2935  C CG    . LEU A  1 409 ? -2.777  17.652  12.476  1.00 35.82 ? 409 LEU C CG    1 
ATOM   2936  C CD1   . LEU A  1 409 ? -3.710  18.798  12.765  1.00 36.44 ? 409 LEU C CD1   1 
ATOM   2937  C CD2   . LEU A  1 409 ? -2.292  17.684  11.038  1.00 43.91 ? 409 LEU C CD2   1 
ATOM   2938  N N     . GLY A  1 410 ? 1.776   18.146  12.340  1.00 46.83 ? 410 GLY C N     1 
ATOM   2939  C CA    . GLY A  1 410 ? 3.083   18.697  12.620  1.00 55.95 ? 410 GLY C CA    1 
ATOM   2940  C C     . GLY A  1 410 ? 3.735   18.018  13.811  1.00 57.41 ? 410 GLY C C     1 
ATOM   2941  O O     . GLY A  1 410 ? 4.255   16.900  13.737  1.00 56.87 ? 410 GLY C O     1 
ATOM   2942  N N     . PRO A  1 411 ? 3.707   18.672  14.937  1.00 48.01 ? 411 PRO C N     1 
ATOM   2943  C CA    . PRO A  1 411 ? 4.379   18.118  16.117  1.00 52.82 ? 411 PRO C CA    1 
ATOM   2944  C C     . PRO A  1 411 ? 3.508   17.202  16.943  1.00 47.92 ? 411 PRO C C     1 
ATOM   2945  O O     . PRO A  1 411 ? 3.279   16.064  16.536  1.00 49.10 ? 411 PRO C O     1 
ATOM   2946  C CB    . PRO A  1 411 ? 4.758   19.377  16.914  1.00 59.00 ? 411 PRO C CB    1 
ATOM   2947  C CG    . PRO A  1 411 ? 4.574   20.564  15.933  1.00 61.31 ? 411 PRO C CG    1 
ATOM   2948  C CD    . PRO A  1 411 ? 3.513   20.123  15.000  1.00 54.18 ? 411 PRO C CD    1 
ATOM   2949  N N     . GLY A  1 412 ? 3.056   17.687  18.111  1.00 42.10 ? 412 GLY C N     1 
ATOM   2950  C CA    . GLY A  1 412 ? 2.341   16.900  19.112  1.00 44.62 ? 412 GLY C CA    1 
ATOM   2951  C C     . GLY A  1 412 ? 0.913   17.350  19.411  1.00 44.55 ? 412 GLY C C     1 
ATOM   2952  O O     . GLY A  1 412 ? 0.074   17.382  18.498  1.00 45.57 ? 412 GLY C O     1 
ATOM   2953  N N     . ALA A  1 413 ? 0.617   17.695  20.671  1.00 38.15 ? 413 ALA C N     1 
ATOM   2954  C CA    . ALA A  1 413 ? -0.756  18.010  21.069  1.00 34.50 ? 413 ALA C CA    1 
ATOM   2955  C C     . ALA A  1 413 ? -1.218  19.330  20.462  1.00 31.69 ? 413 ALA C C     1 
ATOM   2956  O O     . ALA A  1 413 ? -0.450  20.284  20.349  1.00 36.11 ? 413 ALA C O     1 
ATOM   2957  C CB    . ALA A  1 413 ? -0.886  18.070  22.593  1.00 37.09 ? 413 ALA C CB    1 
ATOM   2958  N N     . GLU A  1 414 ? -2.486  19.385  20.074  1.00 32.97 ? 414 GLU C N     1 
ATOM   2959  C CA    . GLU A  1 414 ? -3.042  20.526  19.367  1.00 28.58 ? 414 GLU C CA    1 
ATOM   2960  C C     . GLU A  1 414 ? -4.060  21.203  20.267  1.00 27.70 ? 414 GLU C C     1 
ATOM   2961  O O     . GLU A  1 414 ? -4.954  20.542  20.805  1.00 26.95 ? 414 GLU C O     1 
ATOM   2962  C CB    . GLU A  1 414 ? -3.693  20.095  18.045  1.00 23.12 ? 414 GLU C CB    1 
ATOM   2963  C CG    . GLU A  1 414 ? -4.418  21.239  17.347  1.00 32.86 ? 414 GLU C CG    1 
ATOM   2964  C CD    . GLU A  1 414 ? -5.271  20.854  16.127  1.00 32.19 ? 414 GLU C CD    1 
ATOM   2965  O OE1   . GLU A  1 414 ? -5.710  19.688  15.956  1.00 30.08 ? 414 GLU C OE1   1 
ATOM   2966  O OE2   . GLU A  1 414 ? -5.530  21.770  15.329  1.00 25.78 ? 414 GLU C OE2   1 
ATOM   2967  N N     . LEU A  1 415 ? -3.922  22.512  20.435  1.00 27.43 ? 415 LEU C N     1 
ATOM   2968  C CA    . LEU A  1 415 ? -4.867  23.289  21.224  1.00 29.26 ? 415 LEU C CA    1 
ATOM   2969  C C     . LEU A  1 415 ? -5.327  24.476  20.397  1.00 31.32 ? 415 LEU C C     1 
ATOM   2970  O O     . LEU A  1 415 ? -4.666  24.870  19.436  1.00 35.63 ? 415 LEU C O     1 
ATOM   2971  C CB    . LEU A  1 415 ? -4.253  23.822  22.530  1.00 29.30 ? 415 LEU C CB    1 
ATOM   2972  C CG    . LEU A  1 415 ? -3.612  22.919  23.580  1.00 29.07 ? 415 LEU C CG    1 
ATOM   2973  C CD1   . LEU A  1 415 ? -2.769  23.761  24.496  1.00 24.79 ? 415 LEU C CD1   1 
ATOM   2974  C CD2   . LEU A  1 415 ? -4.653  22.205  24.401  1.00 30.27 ? 415 LEU C CD2   1 
ATOM   2975  N N     . LEU A  1 416 ? -6.425  25.096  20.821  1.00 30.29 ? 416 LEU C N     1 
ATOM   2976  C CA    . LEU A  1 416 ? -7.020  26.199  20.080  1.00 31.82 ? 416 LEU C CA    1 
ATOM   2977  C C     . LEU A  1 416 ? -7.458  27.272  21.060  1.00 28.73 ? 416 LEU C C     1 
ATOM   2978  O O     . LEU A  1 416 ? -8.314  27.008  21.907  1.00 31.48 ? 416 LEU C O     1 
ATOM   2979  C CB    . LEU A  1 416 ? -8.211  25.702  19.263  1.00 30.28 ? 416 LEU C CB    1 
ATOM   2980  C CG    . LEU A  1 416 ? -9.003  26.808  18.583  1.00 29.93 ? 416 LEU C CG    1 
ATOM   2981  C CD1   . LEU A  1 416 ? -8.112  27.446  17.543  1.00 32.88 ? 416 LEU C CD1   1 
ATOM   2982  C CD2   . LEU A  1 416 ? -10.274 26.262  17.956  1.00 27.71 ? 416 LEU C CD2   1 
ATOM   2983  N N     . VAL A  1 417 ? -6.896  28.478  20.944  1.00 28.22 ? 417 VAL C N     1 
ATOM   2984  C CA    . VAL A  1 417 ? -7.075  29.520  21.955  1.00 34.80 ? 417 VAL C CA    1 
ATOM   2985  C C     . VAL A  1 417 ? -7.947  30.649  21.426  1.00 32.22 ? 417 VAL C C     1 
ATOM   2986  O O     . VAL A  1 417 ? -7.761  31.119  20.301  1.00 32.20 ? 417 VAL C O     1 
ATOM   2987  C CB    . VAL A  1 417 ? -5.736  30.093  22.445  1.00 35.55 ? 417 VAL C CB    1 
ATOM   2988  C CG1   . VAL A  1 417 ? -5.962  30.882  23.714  1.00 35.52 ? 417 VAL C CG1   1 
ATOM   2989  C CG2   . VAL A  1 417 ? -4.736  28.986  22.690  1.00 32.56 ? 417 VAL C CG2   1 
ATOM   2990  N N     . PHE A  1 418 ? -8.857  31.123  22.270  1.00 29.95 ? 418 PHE C N     1 
ATOM   2991  C CA    . PHE A  1 418 ? -9.767  32.195  21.914  1.00 31.16 ? 418 PHE C CA    1 
ATOM   2992  C C     . PHE A  1 418 ? -9.536  33.417  22.777  1.00 35.52 ? 418 PHE C C     1 
ATOM   2993  O O     . PHE A  1 418 ? -9.079  33.318  23.916  1.00 33.07 ? 418 PHE C O     1 
ATOM   2994  C CB    . PHE A  1 418 ? -11.200 31.769  22.067  1.00 28.87 ? 418 PHE C CB    1 
ATOM   2995  C CG    . PHE A  1 418 ? -11.546 30.601  21.234  1.00 34.20 ? 418 PHE C CG    1 
ATOM   2996  C CD1   . PHE A  1 418 ? -11.844 30.764  19.889  1.00 36.26 ? 418 PHE C CD1   1 
ATOM   2997  C CD2   . PHE A  1 418 ? -11.565 29.328  21.775  1.00 36.11 ? 418 PHE C CD2   1 
ATOM   2998  C CE1   . PHE A  1 418 ? -12.174 29.681  19.097  1.00 26.63 ? 418 PHE C CE1   1 
ATOM   2999  C CE2   . PHE A  1 418 ? -11.895 28.235  20.980  1.00 34.18 ? 418 PHE C CE2   1 
ATOM   3000  C CZ    . PHE A  1 418 ? -12.203 28.423  19.646  1.00 30.21 ? 418 PHE C CZ    1 
ATOM   3001  N N     . SER A  1 419 ? -9.868  34.571  22.212  1.00 36.60 ? 419 SER C N     1 
ATOM   3002  C CA    . SER A  1 419 ? -9.851  35.821  22.948  1.00 40.85 ? 419 SER C CA    1 
ATOM   3003  C C     . SER A  1 419 ? -10.496 36.883  22.081  1.00 40.02 ? 419 SER C C     1 
ATOM   3004  O O     . SER A  1 419 ? -10.483 36.794  20.849  1.00 38.72 ? 419 SER C O     1 
ATOM   3005  C CB    . SER A  1 419 ? -8.438  36.259  23.324  1.00 42.14 ? 419 SER C CB    1 
ATOM   3006  O OG    . SER A  1 419 ? -8.385  37.682  23.392  1.00 41.07 ? 419 SER C OG    1 
ATOM   3007  N N     . LYS A  1 420 ? -11.044 37.898  22.748  1.00 37.47 ? 420 LYS C N     1 
ATOM   3008  C CA    . LYS A  1 420 ? -11.585 39.087  22.109  1.00 39.35 ? 420 LYS C CA    1 
ATOM   3009  C C     . LYS A  1 420 ? -10.522 40.128  21.866  1.00 43.60 ? 420 LYS C C     1 
ATOM   3010  O O     . LYS A  1 420 ? -10.857 41.262  21.515  1.00 45.51 ? 420 LYS C O     1 
ATOM   3011  C CB    . LYS A  1 420 ? -12.690 39.708  22.969  1.00 41.64 ? 420 LYS C CB    1 
ATOM   3012  C CG    . LYS A  1 420 ? -14.091 39.233  22.639  1.00 45.61 ? 420 LYS C CG    1 
ATOM   3013  C CD    . LYS A  1 420 ? -14.868 38.878  23.896  1.00 44.46 ? 420 LYS C CD    1 
ATOM   3014  C CE    . LYS A  1 420 ? -16.236 38.341  23.562  1.00 42.49 ? 420 LYS C CE    1 
ATOM   3015  N NZ    . LYS A  1 420 ? -16.242 36.860  23.698  1.00 44.80 ? 420 LYS C NZ    1 
ATOM   3016  N N     . ASP A  1 421 ? -9.257  39.784  22.076  1.00 42.63 ? 421 ASP C N     1 
ATOM   3017  C CA    . ASP A  1 421 ? -8.192  40.773  22.059  1.00 42.91 ? 421 ASP C CA    1 
ATOM   3018  C C     . ASP A  1 421 ? -6.915  40.086  21.602  1.00 43.48 ? 421 ASP C C     1 
ATOM   3019  O O     . ASP A  1 421 ? -6.572  39.020  22.117  1.00 44.20 ? 421 ASP C O     1 
ATOM   3020  C CB    . ASP A  1 421 ? -8.029  41.397  23.448  1.00 44.70 ? 421 ASP C CB    1 
ATOM   3021  C CG    . ASP A  1 421 ? -7.204  42.691  23.420  1.00 50.32 ? 421 ASP C CG    1 
ATOM   3022  O OD1   . ASP A  1 421 ? -7.763  43.763  23.068  1.00 42.97 ? 421 ASP C OD1   1 
ATOM   3023  O OD2   . ASP A  1 421 ? -6.004  42.621  23.754  1.00 46.61 ? 421 ASP C OD2   1 
ATOM   3024  N N     . TRP A  1 422 ? -6.213  40.694  20.642  1.00 46.28 ? 422 TRP C N     1 
ATOM   3025  C CA    . TRP A  1 422 ? -5.116  39.989  19.985  1.00 40.29 ? 422 TRP C CA    1 
ATOM   3026  C C     . TRP A  1 422 ? -3.940  39.800  20.929  1.00 39.20 ? 422 TRP C C     1 
ATOM   3027  O O     . TRP A  1 422 ? -3.358  38.712  21.012  1.00 37.06 ? 422 TRP C O     1 
ATOM   3028  C CB    . TRP A  1 422 ? -4.695  40.749  18.725  1.00 48.53 ? 422 TRP C CB    1 
ATOM   3029  C CG    . TRP A  1 422 ? -3.494  40.166  18.017  1.00 49.56 ? 422 TRP C CG    1 
ATOM   3030  C CD1   . TRP A  1 422 ? -2.323  40.805  17.721  1.00 52.39 ? 422 TRP C CD1   1 
ATOM   3031  C CD2   . TRP A  1 422 ? -3.360  38.832  17.513  1.00 50.43 ? 422 TRP C CD2   1 
ATOM   3032  N NE1   . TRP A  1 422 ? -1.467  39.947  17.067  1.00 57.84 ? 422 TRP C NE1   1 
ATOM   3033  C CE2   . TRP A  1 422 ? -2.081  38.730  16.933  1.00 49.84 ? 422 TRP C CE2   1 
ATOM   3034  C CE3   . TRP A  1 422 ? -4.193  37.713  17.506  1.00 48.90 ? 422 TRP C CE3   1 
ATOM   3035  C CZ2   . TRP A  1 422 ? -1.618  37.556  16.360  1.00 51.61 ? 422 TRP C CZ2   1 
ATOM   3036  C CZ3   . TRP A  1 422 ? -3.729  36.551  16.939  1.00 48.11 ? 422 TRP C CZ3   1 
ATOM   3037  C CH2   . TRP A  1 422 ? -2.455  36.481  16.372  1.00 48.09 ? 422 TRP C CH2   1 
ATOM   3038  N N     . ASP A  1 423 ? -3.573  40.850  21.650  1.00 39.13 ? 423 ASP C N     1 
ATOM   3039  C CA    . ASP A  1 423 ? -2.428  40.743  22.538  1.00 41.76 ? 423 ASP C CA    1 
ATOM   3040  C C     . ASP A  1 423 ? -2.710  39.800  23.698  1.00 41.68 ? 423 ASP C C     1 
ATOM   3041  O O     . ASP A  1 423 ? -1.824  39.059  24.130  1.00 44.55 ? 423 ASP C O     1 
ATOM   3042  C CB    . ASP A  1 423 ? -2.043  42.124  23.050  1.00 45.29 ? 423 ASP C CB    1 
ATOM   3043  C CG    . ASP A  1 423 ? -1.530  43.024  21.955  1.00 47.99 ? 423 ASP C CG    1 
ATOM   3044  O OD1   . ASP A  1 423 ? -1.082  42.505  20.904  1.00 43.92 ? 423 ASP C OD1   1 
ATOM   3045  O OD2   . ASP A  1 423 ? -1.562  44.259  22.154  1.00 53.91 ? 423 ASP C OD2   1 
ATOM   3046  N N     . ARG A  1 424 ? -3.927  39.825  24.235  1.00 41.50 ? 424 ARG C N     1 
ATOM   3047  C CA    . ARG A  1 424 ? -4.233  38.910  25.325  1.00 42.66 ? 424 ARG C CA    1 
ATOM   3048  C C     . ARG A  1 424 ? -4.056  37.465  24.871  1.00 42.85 ? 424 ARG C C     1 
ATOM   3049  O O     . ARG A  1 424 ? -3.434  36.664  25.577  1.00 42.52 ? 424 ARG C O     1 
ATOM   3050  C CB    . ARG A  1 424 ? -5.650  39.163  25.850  1.00 43.25 ? 424 ARG C CB    1 
ATOM   3051  C CG    . ARG A  1 424 ? -6.089  38.238  26.979  1.00 46.29 ? 424 ARG C CG    1 
ATOM   3052  C CD    . ARG A  1 424 ? -7.047  38.930  27.946  1.00 41.68 ? 424 ARG C CD    1 
ATOM   3053  N NE    . ARG A  1 424 ? -8.333  39.229  27.323  1.00 44.33 ? 424 ARG C NE    1 
ATOM   3054  C CZ    . ARG A  1 424 ? -8.655  40.407  26.798  1.00 45.80 ? 424 ARG C CZ    1 
ATOM   3055  N NH1   . ARG A  1 424 ? -7.799  41.417  26.783  1.00 44.44 ? 424 ARG C NH1   1 
ATOM   3056  N NH2   . ARG A  1 424 ? -9.870  40.581  26.288  1.00 40.62 ? 424 ARG C NH2   1 
ATOM   3057  N N     . LEU A  1 425 ? -4.541  37.138  23.663  1.00 41.63 ? 425 LEU C N     1 
ATOM   3058  C CA    . LEU A  1 425 ? -4.482  35.765  23.159  1.00 39.40 ? 425 LEU C CA    1 
ATOM   3059  C C     . LEU A  1 425 ? -3.044  35.273  23.051  1.00 45.37 ? 425 LEU C C     1 
ATOM   3060  O O     . LEU A  1 425 ? -2.714  34.170  23.511  1.00 45.54 ? 425 LEU C O     1 
ATOM   3061  C CB    . LEU A  1 425 ? -5.176  35.666  21.801  1.00 35.00 ? 425 LEU C CB    1 
ATOM   3062  C CG    . LEU A  1 425 ? -5.127  34.273  21.152  1.00 38.78 ? 425 LEU C CG    1 
ATOM   3063  C CD1   . LEU A  1 425 ? -6.443  33.897  20.456  1.00 38.48 ? 425 LEU C CD1   1 
ATOM   3064  C CD2   . LEU A  1 425 ? -3.967  34.171  20.170  1.00 37.68 ? 425 LEU C CD2   1 
ATOM   3065  N N     . THR A  1 426 ? -2.182  36.056  22.397  1.00 44.88 ? 426 THR C N     1 
ATOM   3066  C CA    . THR A  1 426 ? -0.756  35.754  22.399  1.00 43.48 ? 426 THR C CA    1 
ATOM   3067  C C     . THR A  1 426 ? -0.260  35.518  23.826  1.00 44.54 ? 426 THR C C     1 
ATOM   3068  O O     . THR A  1 426 ? 0.273   34.448  24.145  1.00 48.59 ? 426 THR C O     1 
ATOM   3069  C CB    . THR A  1 426 ? 0.016   36.891  21.721  1.00 43.03 ? 426 THR C CB    1 
ATOM   3070  O OG1   . THR A  1 426 ? -0.676  37.288  20.530  1.00 50.32 ? 426 THR C OG1   1 
ATOM   3071  C CG2   . THR A  1 426 ? 1.412   36.446  21.335  1.00 40.37 ? 426 THR C CG2   1 
ATOM   3072  N N     . ALA A  1 427 ? -0.481  36.492  24.715  1.00 41.76 ? 427 ALA C N     1 
ATOM   3073  C CA    . ALA A  1 427 ? -0.061  36.339  26.108  1.00 47.41 ? 427 ALA C CA    1 
ATOM   3074  C C     . ALA A  1 427 ? -0.542  35.018  26.704  1.00 43.53 ? 427 ALA C C     1 
ATOM   3075  O O     . ALA A  1 427 ? 0.180   34.386  27.487  1.00 38.44 ? 427 ALA C O     1 
ATOM   3076  C CB    . ALA A  1 427 ? -0.562  37.518  26.942  1.00 43.37 ? 427 ALA C CB    1 
ATOM   3077  N N     . MET A  1 428 ? -1.756  34.574  26.335  1.00 44.24 ? 428 MET C N     1 
ATOM   3078  C CA    . MET A  1 428 ? -2.210  33.256  26.776  1.00 42.76 ? 428 MET C CA    1 
ATOM   3079  C C     . MET A  1 428 ? -1.346  32.159  26.193  1.00 45.32 ? 428 MET C C     1 
ATOM   3080  O O     . MET A  1 428 ? -1.123  31.126  26.844  1.00 40.52 ? 428 MET C O     1 
ATOM   3081  C CB    . MET A  1 428 ? -3.662  32.990  26.384  1.00 36.86 ? 428 MET C CB    1 
ATOM   3082  C CG    . MET A  1 428 ? -4.611  34.115  26.562  1.00 40.65 ? 428 MET C CG    1 
ATOM   3083  S SD    . MET A  1 428 ? -6.263  33.579  26.073  1.00 50.73 ? 428 MET C SD    1 
ATOM   3084  C CE    . MET A  1 428 ? -7.244  35.003  26.565  1.00 42.65 ? 428 MET C CE    1 
ATOM   3085  N N     . LYS A  1 429 ? -0.842  32.367  24.975  1.00 39.93 ? 429 LYS C N     1 
ATOM   3086  C CA    . LYS A  1 429 ? -0.159  31.291  24.271  1.00 39.64 ? 429 LYS C CA    1 
ATOM   3087  C C     . LYS A  1 429 ? 1.151   30.920  24.959  1.00 42.02 ? 429 LYS C C     1 
ATOM   3088  O O     . LYS A  1 429 ? 1.377   29.751  25.294  1.00 43.44 ? 429 LYS C O     1 
ATOM   3089  C CB    . LYS A  1 429 ? 0.069   31.692  22.813  1.00 44.07 ? 429 LYS C CB    1 
ATOM   3090  C CG    . LYS A  1 429 ? -1.216  31.865  22.008  1.00 40.51 ? 429 LYS C CG    1 
ATOM   3091  C CD    . LYS A  1 429 ? -0.934  32.228  20.551  1.00 38.93 ? 429 LYS C CD    1 
ATOM   3092  C CE    . LYS A  1 429 ? -0.279  31.081  19.802  1.00 39.71 ? 429 LYS C CE    1 
ATOM   3093  N NZ    . LYS A  1 429 ? -0.001  31.504  18.417  1.00 36.25 ? 429 LYS C NZ    1 
ATOM   3094  N N     . ASP A  1 430 ? 2.028   31.899  25.186  1.00 41.95 ? 430 ASP C N     1 
ATOM   3095  C CA    . ASP A  1 430 ? 3.309   31.568  25.805  1.00 44.66 ? 430 ASP C CA    1 
ATOM   3096  C C     . ASP A  1 430 ? 3.124   31.115  27.240  1.00 42.23 ? 430 ASP C C     1 
ATOM   3097  O O     . ASP A  1 430 ? 3.926   30.323  27.745  1.00 39.13 ? 430 ASP C O     1 
ATOM   3098  C CB    . ASP A  1 430 ? 4.260   32.761  25.746  1.00 48.64 ? 430 ASP C CB    1 
ATOM   3099  C CG    . ASP A  1 430 ? 3.544   34.074  25.931  1.00 53.40 ? 430 ASP C CG    1 
ATOM   3100  O OD1   . ASP A  1 430 ? 2.293   34.034  26.049  1.00 51.64 ? 430 ASP C OD1   1 
ATOM   3101  O OD2   . ASP A  1 430 ? 4.227   35.129  25.960  1.00 51.20 ? 430 ASP C OD2   1 
ATOM   3102  N N     . GLU A  1 431 ? 2.088   31.629  27.909  1.00 41.18 ? 431 GLU C N     1 
ATOM   3103  C CA    . GLU A  1 431 ? 1.657   31.057  29.174  1.00 43.89 ? 431 GLU C CA    1 
ATOM   3104  C C     . GLU A  1 431 ? 1.560   29.544  29.056  1.00 44.49 ? 431 GLU C C     1 
ATOM   3105  O O     . GLU A  1 431 ? 2.119   28.800  29.869  1.00 42.43 ? 431 GLU C O     1 
ATOM   3106  C CB    . GLU A  1 431 ? 0.314   31.663  29.575  1.00 38.91 ? 431 GLU C CB    1 
ATOM   3107  C CG    . GLU A  1 431 ? 0.426   32.658  30.675  1.00 40.08 ? 431 GLU C CG    1 
ATOM   3108  C CD    . GLU A  1 431 ? 1.277   32.117  31.828  1.00 53.79 ? 431 GLU C CD    1 
ATOM   3109  O OE1   . GLU A  1 431 ? 0.897   31.061  32.385  1.00 54.08 ? 431 GLU C OE1   1 
ATOM   3110  O OE2   . GLU A  1 431 ? 2.306   32.746  32.155  1.00 52.45 ? 431 GLU C OE2   1 
ATOM   3111  N N     . ILE A  1 432 ? 0.898   29.078  27.999  1.00 39.81 ? 432 ILE C N     1 
ATOM   3112  C CA    . ILE A  1 432 ? 0.760   27.645  27.768  1.00 43.31 ? 432 ILE C CA    1 
ATOM   3113  C C     . ILE A  1 432 ? 2.114   27.012  27.477  1.00 45.97 ? 432 ILE C C     1 
ATOM   3114  O O     . ILE A  1 432 ? 2.421   25.920  27.965  1.00 46.32 ? 432 ILE C O     1 
ATOM   3115  C CB    . ILE A  1 432 ? -0.234  27.402  26.620  1.00 45.54 ? 432 ILE C CB    1 
ATOM   3116  C CG1   . ILE A  1 432 ? -1.667  27.524  27.148  1.00 43.21 ? 432 ILE C CG1   1 
ATOM   3117  C CG2   . ILE A  1 432 ? 0.030   26.055  25.972  1.00 38.54 ? 432 ILE C CG2   1 
ATOM   3118  C CD1   . ILE A  1 432 ? -2.697  27.734  26.082  1.00 43.98 ? 432 ILE C CD1   1 
ATOM   3119  N N     . ALA A  1 433 ? 2.937   27.675  26.660  1.00 50.05 ? 433 ALA C N     1 
ATOM   3120  C CA    . ALA A  1 433 ? 4.254   27.132  26.345  1.00 46.93 ? 433 ALA C CA    1 
ATOM   3121  C C     . ALA A  1 433 ? 5.123   27.043  27.592  1.00 47.60 ? 433 ALA C C     1 
ATOM   3122  O O     . ALA A  1 433 ? 5.931   26.117  27.739  1.00 50.87 ? 433 ALA C O     1 
ATOM   3123  C CB    . ALA A  1 433 ? 4.929   27.995  25.282  1.00 52.53 ? 433 ALA C CB    1 
ATOM   3124  N N     . THR A  1 434 ? 4.988   28.021  28.485  1.00 50.12 ? 434 THR C N     1 
ATOM   3125  C CA    . THR A  1 434 ? 5.674   27.965  29.769  1.00 46.62 ? 434 THR C CA    1 
ATOM   3126  C C     . THR A  1 434 ? 5.110   26.845  30.624  1.00 46.77 ? 434 THR C C     1 
ATOM   3127  O O     . THR A  1 434 ? 5.853   26.089  31.258  1.00 50.81 ? 434 THR C O     1 
ATOM   3128  C CB    . THR A  1 434 ? 5.522   29.315  30.481  1.00 48.35 ? 434 THR C CB    1 
ATOM   3129  O OG1   . THR A  1 434 ? 6.347   30.293  29.837  1.00 59.84 ? 434 THR C OG1   1 
ATOM   3130  C CG2   . THR A  1 434 ? 5.904   29.231  31.945  1.00 46.31 ? 434 THR C CG2   1 
ATOM   3131  N N     . THR A  1 435 ? 3.796   26.699  30.608  1.00 44.38 ? 435 THR C N     1 
ATOM   3132  C CA    . THR A  1 435 ? 3.116   25.855  31.575  1.00 44.35 ? 435 THR C CA    1 
ATOM   3133  C C     . THR A  1 435 ? 3.115   24.388  31.156  1.00 43.83 ? 435 THR C C     1 
ATOM   3134  O O     . THR A  1 435 ? 3.345   23.502  31.988  1.00 41.08 ? 435 THR C O     1 
ATOM   3135  C CB    . THR A  1 435 ? 1.693   26.373  31.753  1.00 40.98 ? 435 THR C CB    1 
ATOM   3136  O OG1   . THR A  1 435 ? 1.647   27.356  32.805  1.00 40.65 ? 435 THR C OG1   1 
ATOM   3137  C CG2   . THR A  1 435 ? 0.789   25.259  32.055  1.00 37.45 ? 435 THR C CG2   1 
ATOM   3138  N N     . ALA A  1 436 ? 2.863   24.105  29.881  1.00 43.10 ? 436 ALA C N     1 
ATOM   3139  C CA    . ALA A  1 436 ? 2.787   22.735  29.402  1.00 43.26 ? 436 ALA C CA    1 
ATOM   3140  C C     . ALA A  1 436 ? 3.941   22.385  28.483  1.00 39.06 ? 436 ALA C C     1 
ATOM   3141  O O     . ALA A  1 436 ? 3.955   21.290  27.912  1.00 39.05 ? 436 ALA C O     1 
ATOM   3142  C CB    . ALA A  1 436 ? 1.452   22.495  28.683  1.00 40.42 ? 436 ALA C CB    1 
ATOM   3143  N N     . GLY A  1 437 ? 4.900   23.284  28.319  1.00 41.81 ? 437 GLY C N     1 
ATOM   3144  C CA    . GLY A  1 437 ? 6.046   22.996  27.497  1.00 38.89 ? 437 GLY C CA    1 
ATOM   3145  C C     . GLY A  1 437 ? 5.682   22.898  26.039  1.00 38.87 ? 437 GLY C C     1 
ATOM   3146  O O     . GLY A  1 437 ? 4.508   22.764  25.690  1.00 39.89 ? 437 GLY C O     1 
ATOM   3147  N N     . THR A  1 438 ? 6.687   22.988  25.175  1.00 48.93 ? 438 THR C N     1 
ATOM   3148  C CA    . THR A  1 438 ? 6.506   22.749  23.751  1.00 45.90 ? 438 THR C CA    1 
ATOM   3149  C C     . THR A  1 438 ? 7.679   21.922  23.240  1.00 44.05 ? 438 THR C C     1 
ATOM   3150  O O     . THR A  1 438 ? 8.750   21.877  23.855  1.00 45.17 ? 438 THR C O     1 
ATOM   3151  C CB    . THR A  1 438 ? 6.383   24.054  22.948  1.00 45.83 ? 438 THR C CB    1 
ATOM   3152  O OG1   . THR A  1 438 ? 7.587   24.817  23.081  1.00 49.51 ? 438 THR C OG1   1 
ATOM   3153  C CG2   . THR A  1 438 ? 5.203   24.880  23.446  1.00 41.60 ? 438 THR C CG2   1 
ATOM   3154  N N     . LEU A  1 439 ? 7.447   21.257  22.106  1.00 45.86 ? 439 LEU C N     1 
ATOM   3155  C CA    . LEU A  1 439 ? 8.444   20.466  21.374  1.00 44.00 ? 439 LEU C CA    1 
ATOM   3156  C C     . LEU A  1 439 ? 8.986   21.309  20.218  1.00 48.23 ? 439 LEU C C     1 
ATOM   3157  O O     . LEU A  1 439 ? 8.509   21.218  19.085  1.00 52.03 ? 439 LEU C O     1 
ATOM   3158  C CB    . LEU A  1 439 ? 7.817   19.182  20.842  1.00 38.60 ? 439 LEU C CB    1 
ATOM   3159  C CG    . LEU A  1 439 ? 7.559   18.027  21.802  1.00 41.75 ? 439 LEU C CG    1 
ATOM   3160  C CD1   . LEU A  1 439 ? 6.603   17.051  21.122  1.00 30.64 ? 439 LEU C CD1   1 
ATOM   3161  C CD2   . LEU A  1 439 ? 8.881   17.347  22.246  1.00 41.92 ? 439 LEU C CD2   1 
ATOM   3162  N N     . SER A  1 440 ? 10.007  22.116  20.485  1.00 46.96 ? 440 SER C N     1 
ATOM   3163  C CA    . SER A  1 440 ? 10.563  22.958  19.418  1.00 51.67 ? 440 SER C CA    1 
ATOM   3164  C C     . SER A  1 440 ? 11.941  22.465  18.890  1.00 54.12 ? 440 SER C C     1 
ATOM   3165  O O     . SER A  1 440 ? 12.628  21.695  19.562  1.00 55.76 ? 440 SER C O     1 
ATOM   3166  C CB    . SER A  1 440 ? 10.652  24.397  19.917  1.00 43.69 ? 440 SER C CB    1 
ATOM   3167  O OG    . SER A  1 440 ? 9.413   24.806  20.469  1.00 43.61 ? 440 SER C OG    1 
ATOM   3168  N N     . SER B  1 30  ? 5.433   11.030  -51.203 1.00 43.11 ? 30  SER D N     1 
ATOM   3169  C CA    . SER B  1 30  ? 4.276   10.264  -51.650 1.00 44.93 ? 30  SER D CA    1 
ATOM   3170  C C     . SER B  1 30  ? 2.966   10.941  -51.324 1.00 45.94 ? 30  SER D C     1 
ATOM   3171  O O     . SER B  1 30  ? 2.334   11.561  -52.176 1.00 47.92 ? 30  SER D O     1 
ATOM   3172  C CB    . SER B  1 30  ? 4.267   8.870   -51.026 1.00 42.64 ? 30  SER D CB    1 
ATOM   3173  O OG    . SER B  1 30  ? 4.813   7.928   -51.926 1.00 48.03 ? 30  SER D OG    1 
ATOM   3174  N N     . THR B  1 31  ? 2.561   10.807  -50.069 1.00 50.40 ? 31  THR D N     1 
ATOM   3175  C CA    . THR B  1 31  ? 1.220   11.168  -49.648 1.00 44.59 ? 31  THR D CA    1 
ATOM   3176  C C     . THR B  1 31  ? 1.110   12.675  -49.427 1.00 42.24 ? 31  THR D C     1 
ATOM   3177  O O     . THR B  1 31  ? 2.113   13.379  -49.288 1.00 41.55 ? 31  THR D O     1 
ATOM   3178  C CB    . THR B  1 31  ? 0.863   10.394  -48.384 1.00 43.96 ? 31  THR D CB    1 
ATOM   3179  O OG1   . THR B  1 31  ? 2.047   10.235  -47.591 1.00 47.69 ? 31  THR D OG1   1 
ATOM   3180  C CG2   . THR B  1 31  ? 0.343   9.015   -48.757 1.00 36.67 ? 31  THR D CG2   1 
ATOM   3181  N N     . ASP B  1 32  ? -0.137  13.178  -49.418 1.00 42.89 ? 32  ASP D N     1 
ATOM   3182  C CA    . ASP B  1 32  ? -0.376  14.613  -49.284 1.00 40.94 ? 32  ASP D CA    1 
ATOM   3183  C C     . ASP B  1 32  ? -1.501  14.912  -48.297 1.00 37.65 ? 32  ASP D C     1 
ATOM   3184  O O     . ASP B  1 32  ? -2.181  15.932  -48.423 1.00 36.40 ? 32  ASP D O     1 
ATOM   3185  C CB    . ASP B  1 32  ? -0.696  15.245  -50.638 1.00 35.06 ? 32  ASP D CB    1 
ATOM   3186  C CG    . ASP B  1 32  ? -1.923  14.658  -51.269 1.00 40.76 ? 32  ASP D CG    1 
ATOM   3187  O OD1   . ASP B  1 32  ? -2.350  13.603  -50.765 1.00 40.59 ? 32  ASP D OD1   1 
ATOM   3188  O OD2   . ASP B  1 32  ? -2.451  15.229  -52.263 1.00 42.34 ? 32  ASP D OD2   1 
ATOM   3189  N N     . THR B  1 33  ? -1.697  14.034  -47.308 1.00 41.09 ? 33  THR D N     1 
ATOM   3190  C CA    . THR B  1 33  ? -2.768  14.168  -46.326 1.00 39.24 ? 33  THR D CA    1 
ATOM   3191  C C     . THR B  1 33  ? -2.829  15.544  -45.682 1.00 30.80 ? 33  THR D C     1 
ATOM   3192  O O     . THR B  1 33  ? -3.851  15.889  -45.090 1.00 30.63 ? 33  THR D O     1 
ATOM   3193  C CB    . THR B  1 33  ? -2.604  13.129  -45.204 1.00 44.67 ? 33  THR D CB    1 
ATOM   3194  O OG1   . THR B  1 33  ? -2.064  11.913  -45.737 1.00 50.69 ? 33  THR D OG1   1 
ATOM   3195  C CG2   . THR B  1 33  ? -3.956  12.832  -44.573 1.00 45.61 ? 33  THR D CG2   1 
ATOM   3196  N N     . THR B  1 34  ? -1.762  16.331  -45.767 1.00 36.24 ? 34  THR D N     1 
ATOM   3197  C CA    . THR B  1 34  ? -1.728  17.665  -45.185 1.00 36.13 ? 34  THR D CA    1 
ATOM   3198  C C     . THR B  1 34  ? -2.094  18.747  -46.185 1.00 34.88 ? 34  THR D C     1 
ATOM   3199  O O     . THR B  1 34  ? -2.712  19.746  -45.803 1.00 37.36 ? 34  THR D O     1 
ATOM   3200  C CB    . THR B  1 34  ? -0.340  17.951  -44.591 1.00 39.66 ? 34  THR D CB    1 
ATOM   3201  O OG1   . THR B  1 34  ? -0.119  17.086  -43.472 1.00 39.74 ? 34  THR D OG1   1 
ATOM   3202  C CG2   . THR B  1 34  ? -0.229  19.389  -44.096 1.00 40.81 ? 34  THR D CG2   1 
ATOM   3203  N N     . ALA B  1 35  ? -1.775  18.545  -47.465 1.00 39.87 ? 35  ALA D N     1 
ATOM   3204  C CA    . ALA B  1 35  ? -2.140  19.476  -48.533 1.00 36.14 ? 35  ALA D CA    1 
ATOM   3205  C C     . ALA B  1 35  ? -3.555  20.034  -48.393 1.00 31.74 ? 35  ALA D C     1 
ATOM   3206  O O     . ALA B  1 35  ? -3.811  21.167  -48.804 1.00 34.47 ? 35  ALA D O     1 
ATOM   3207  C CB    . ALA B  1 35  ? -1.982  18.794  -49.896 1.00 34.20 ? 35  ALA D CB    1 
ATOM   3208  N N     . ARG B  1 36  ? -4.471  19.268  -47.797 1.00 34.30 ? 36  ARG D N     1 
ATOM   3209  C CA    . ARG B  1 36  ? -5.848  19.736  -47.670 1.00 32.54 ? 36  ARG D CA    1 
ATOM   3210  C C     . ARG B  1 36  ? -5.914  21.101  -46.998 1.00 34.33 ? 36  ARG D C     1 
ATOM   3211  O O     . ARG B  1 36  ? -6.677  21.973  -47.433 1.00 33.36 ? 36  ARG D O     1 
ATOM   3212  C CB    . ARG B  1 36  ? -6.682  18.720  -46.897 1.00 31.44 ? 36  ARG D CB    1 
ATOM   3213  C CG    . ARG B  1 36  ? -6.105  18.369  -45.524 1.00 29.26 ? 36  ARG D CG    1 
ATOM   3214  C CD    . ARG B  1 36  ? -6.627  17.015  -45.030 1.00 30.69 ? 36  ARG D CD    1 
ATOM   3215  N NE    . ARG B  1 36  ? -8.072  16.864  -45.153 1.00 25.82 ? 36  ARG D NE    1 
ATOM   3216  C CZ    . ARG B  1 36  ? -8.938  17.198  -44.211 1.00 26.04 ? 36  ARG D CZ    1 
ATOM   3217  N NH1   . ARG B  1 36  ? -8.544  17.753  -43.079 1.00 36.62 ? 36  ARG D NH1   1 
ATOM   3218  N NH2   . ARG B  1 36  ? -10.232 16.961  -44.404 1.00 26.62 ? 36  ARG D NH2   1 
ATOM   3219  N N     . PHE B  1 37  ? -5.100  21.322  -45.955 1.00 31.12 ? 37  PHE D N     1 
ATOM   3220  C CA    . PHE B  1 37  ? -5.170  22.587  -45.227 1.00 25.74 ? 37  PHE D CA    1 
ATOM   3221  C C     . PHE B  1 37  ? -4.723  23.760  -46.077 1.00 31.16 ? 37  PHE D C     1 
ATOM   3222  O O     . PHE B  1 37  ? -4.841  24.909  -45.637 1.00 32.39 ? 37  PHE D O     1 
ATOM   3223  C CB    . PHE B  1 37  ? -4.355  22.475  -43.938 1.00 28.77 ? 37  PHE D CB    1 
ATOM   3224  C CG    . PHE B  1 37  ? -4.735  21.268  -43.122 1.00 31.91 ? 37  PHE D CG    1 
ATOM   3225  C CD1   . PHE B  1 37  ? -5.985  21.188  -42.525 1.00 28.72 ? 37  PHE D CD1   1 
ATOM   3226  C CD2   . PHE B  1 37  ? -3.877  20.193  -43.001 1.00 30.02 ? 37  PHE D CD2   1 
ATOM   3227  C CE1   . PHE B  1 37  ? -6.356  20.077  -41.812 1.00 29.27 ? 37  PHE D CE1   1 
ATOM   3228  C CE2   . PHE B  1 37  ? -4.242  19.084  -42.283 1.00 31.73 ? 37  PHE D CE2   1 
ATOM   3229  C CZ    . PHE B  1 37  ? -5.489  19.022  -41.683 1.00 26.73 ? 37  PHE D CZ    1 
ATOM   3230  N N     . LEU B  1 38  ? -4.276  23.503  -47.304 1.00 32.12 ? 38  LEU D N     1 
ATOM   3231  C CA    . LEU B  1 38  ? -4.051  24.589  -48.243 1.00 31.72 ? 38  LEU D CA    1 
ATOM   3232  C C     . LEU B  1 38  ? -5.333  25.358  -48.515 1.00 32.31 ? 38  LEU D C     1 
ATOM   3233  O O     . LEU B  1 38  ? -5.274  26.532  -48.886 1.00 31.05 ? 38  LEU D O     1 
ATOM   3234  C CB    . LEU B  1 38  ? -3.475  24.047  -49.549 1.00 34.36 ? 38  LEU D CB    1 
ATOM   3235  C CG    . LEU B  1 38  ? -2.469  24.891  -50.336 1.00 33.28 ? 38  LEU D CG    1 
ATOM   3236  C CD1   . LEU B  1 38  ? -1.879  24.023  -51.440 1.00 41.78 ? 38  LEU D CD1   1 
ATOM   3237  C CD2   . LEU B  1 38  ? -3.069  26.146  -50.927 1.00 27.25 ? 38  LEU D CD2   1 
ATOM   3238  N N     . TRP B  1 39  ? -6.497  24.734  -48.338 1.00 29.65 ? 39  TRP D N     1 
ATOM   3239  C CA    . TRP B  1 39  ? -7.682  25.532  -48.630 1.00 32.37 ? 39  TRP D CA    1 
ATOM   3240  C C     . TRP B  1 39  ? -7.939  26.611  -47.590 1.00 30.84 ? 39  TRP D C     1 
ATOM   3241  O O     . TRP B  1 39  ? -8.828  27.436  -47.805 1.00 31.47 ? 39  TRP D O     1 
ATOM   3242  C CB    . TRP B  1 39  ? -8.912  24.639  -48.783 1.00 31.42 ? 39  TRP D CB    1 
ATOM   3243  C CG    . TRP B  1 39  ? -8.872  23.773  -50.015 1.00 32.51 ? 39  TRP D CG    1 
ATOM   3244  C CD1   . TRP B  1 39  ? -8.195  22.597  -50.170 1.00 33.79 ? 39  TRP D CD1   1 
ATOM   3245  C CD2   . TRP B  1 39  ? -9.533  24.017  -51.263 1.00 33.81 ? 39  TRP D CD2   1 
ATOM   3246  N NE1   . TRP B  1 39  ? -8.403  22.089  -51.432 1.00 29.19 ? 39  TRP D NE1   1 
ATOM   3247  C CE2   . TRP B  1 39  ? -9.219  22.943  -52.121 1.00 29.50 ? 39  TRP D CE2   1 
ATOM   3248  C CE3   . TRP B  1 39  ? -10.365 25.035  -51.734 1.00 34.75 ? 39  TRP D CE3   1 
ATOM   3249  C CZ2   . TRP B  1 39  ? -9.700  22.864  -53.416 1.00 29.71 ? 39  TRP D CZ2   1 
ATOM   3250  C CZ3   . TRP B  1 39  ? -10.846 24.950  -53.024 1.00 29.53 ? 39  TRP D CZ3   1 
ATOM   3251  C CH2   . TRP B  1 39  ? -10.514 23.873  -53.846 1.00 29.51 ? 39  TRP D CH2   1 
ATOM   3252  N N     . HIS B  1 40  ? -7.173  26.658  -46.499 1.00 31.47 ? 40  HIS D N     1 
ATOM   3253  C CA    . HIS B  1 40  ? -7.317  27.730  -45.521 1.00 34.19 ? 40  HIS D CA    1 
ATOM   3254  C C     . HIS B  1 40  ? -6.642  29.020  -45.959 1.00 34.19 ? 40  HIS D C     1 
ATOM   3255  O O     . HIS B  1 40  ? -6.591  29.974  -45.173 1.00 36.32 ? 40  HIS D O     1 
ATOM   3256  C CB    . HIS B  1 40  ? -6.710  27.320  -44.177 1.00 32.08 ? 40  HIS D CB    1 
ATOM   3257  C CG    . HIS B  1 40  ? -7.688  26.735  -43.220 1.00 30.60 ? 40  HIS D CG    1 
ATOM   3258  N ND1   . HIS B  1 40  ? -7.509  25.493  -42.651 1.00 30.93 ? 40  HIS D ND1   1 
ATOM   3259  C CD2   . HIS B  1 40  ? -8.843  27.223  -42.712 1.00 34.18 ? 40  HIS D CD2   1 
ATOM   3260  C CE1   . HIS B  1 40  ? -8.516  25.237  -41.837 1.00 30.56 ? 40  HIS D CE1   1 
ATOM   3261  N NE2   . HIS B  1 40  ? -9.341  26.269  -41.860 1.00 36.67 ? 40  HIS D NE2   1 
ATOM   3262  N N     . ALA B  1 41  ? -6.111  29.064  -47.172 1.00 33.84 ? 41  ALA D N     1 
ATOM   3263  C CA    . ALA B  1 41  ? -5.045  29.988  -47.517 1.00 35.22 ? 41  ALA D CA    1 
ATOM   3264  C C     . ALA B  1 41  ? -5.565  31.243  -48.197 1.00 38.63 ? 41  ALA D C     1 
ATOM   3265  O O     . ALA B  1 41  ? -6.510  31.208  -48.992 1.00 38.37 ? 41  ALA D O     1 
ATOM   3266  C CB    . ALA B  1 41  ? -4.008  29.315  -48.424 1.00 35.40 ? 41  ALA D CB    1 
ATOM   3267  N N     . GLU B  1 42  ? -4.890  32.348  -47.891 1.00 39.92 ? 42  GLU D N     1 
ATOM   3268  C CA    . GLU B  1 42  ? -5.114  33.646  -48.494 1.00 39.74 ? 42  GLU D CA    1 
ATOM   3269  C C     . GLU B  1 42  ? -3.760  34.213  -48.902 1.00 42.75 ? 42  GLU D C     1 
ATOM   3270  O O     . GLU B  1 42  ? -2.715  33.663  -48.554 1.00 41.40 ? 42  GLU D O     1 
ATOM   3271  C CB    . GLU B  1 42  ? -5.860  34.575  -47.527 1.00 40.79 ? 42  GLU D CB    1 
ATOM   3272  C CG    . GLU B  1 42  ? -7.114  33.956  -46.922 1.00 35.95 ? 42  GLU D CG    1 
ATOM   3273  C CD    . GLU B  1 42  ? -8.393  34.618  -47.391 1.00 44.12 ? 42  GLU D CD    1 
ATOM   3274  O OE1   . GLU B  1 42  ? -8.370  35.827  -47.713 1.00 45.71 ? 42  GLU D OE1   1 
ATOM   3275  O OE2   . GLU B  1 42  ? -9.433  33.926  -47.438 1.00 46.00 ? 42  GLU D OE2   1 
ATOM   3276  N N     . ASP B  1 43  ? -3.784  35.310  -49.666 1.00 43.73 ? 43  ASP D N     1 
ATOM   3277  C CA    . ASP B  1 43  ? -2.555  35.883  -50.204 1.00 46.69 ? 43  ASP D CA    1 
ATOM   3278  C C     . ASP B  1 43  ? -1.565  36.213  -49.101 1.00 50.78 ? 43  ASP D C     1 
ATOM   3279  O O     . ASP B  1 43  ? -1.924  36.777  -48.063 1.00 53.69 ? 43  ASP D O     1 
ATOM   3280  C CB    . ASP B  1 43  ? -2.852  37.147  -51.000 1.00 48.49 ? 43  ASP D CB    1 
ATOM   3281  C CG    . ASP B  1 43  ? -3.876  36.915  -52.076 1.00 56.85 ? 43  ASP D CG    1 
ATOM   3282  O OD1   . ASP B  1 43  ? -4.039  35.747  -52.493 1.00 60.70 ? 43  ASP D OD1   1 
ATOM   3283  O OD2   . ASP B  1 43  ? -4.521  37.901  -52.497 1.00 67.25 ? 43  ASP D OD2   1 
ATOM   3284  N N     . GLY B  1 44  ? -0.305  35.873  -49.345 1.00 46.20 ? 44  GLY D N     1 
ATOM   3285  C CA    . GLY B  1 44  ? 0.737   36.100  -48.373 1.00 47.35 ? 44  GLY D CA    1 
ATOM   3286  C C     . GLY B  1 44  ? 0.960   34.962  -47.405 1.00 45.14 ? 44  GLY D C     1 
ATOM   3287  O O     . GLY B  1 44  ? 1.925   35.016  -46.631 1.00 46.51 ? 44  GLY D O     1 
ATOM   3288  N N     . ASP B  1 45  ? 0.133   33.920  -47.445 1.00 42.99 ? 45  ASP D N     1 
ATOM   3289  C CA    . ASP B  1 45  ? 0.148   32.936  -46.374 1.00 41.75 ? 45  ASP D CA    1 
ATOM   3290  C C     . ASP B  1 45  ? 1.240   31.894  -46.568 1.00 34.69 ? 45  ASP D C     1 
ATOM   3291  O O     . ASP B  1 45  ? 1.798   31.708  -47.651 1.00 38.34 ? 45  ASP D O     1 
ATOM   3292  C CB    . ASP B  1 45  ? -1.193  32.217  -46.263 1.00 37.94 ? 45  ASP D CB    1 
ATOM   3293  C CG    . ASP B  1 45  ? -2.221  33.030  -45.550 1.00 35.70 ? 45  ASP D CG    1 
ATOM   3294  O OD1   . ASP B  1 45  ? -1.917  34.168  -45.150 1.00 39.28 ? 45  ASP D OD1   1 
ATOM   3295  O OD2   . ASP B  1 45  ? -3.344  32.532  -45.391 1.00 38.05 ? 45  ASP D OD2   1 
ATOM   3296  N N     . VAL B  1 46  ? 1.516   31.193  -45.480 1.00 41.67 ? 46  VAL D N     1 
ATOM   3297  C CA    . VAL B  1 46  ? 2.411   30.053  -45.459 1.00 34.22 ? 46  VAL D CA    1 
ATOM   3298  C C     . VAL B  1 46  ? 1.615   28.844  -45.016 1.00 37.97 ? 46  VAL D C     1 
ATOM   3299  O O     . VAL B  1 46  ? 0.811   28.917  -44.079 1.00 40.44 ? 46  VAL D O     1 
ATOM   3300  C CB    . VAL B  1 46  ? 3.594   30.281  -44.507 1.00 32.94 ? 46  VAL D CB    1 
ATOM   3301  C CG1   . VAL B  1 46  ? 4.599   29.172  -44.671 1.00 38.44 ? 46  VAL D CG1   1 
ATOM   3302  C CG2   . VAL B  1 46  ? 4.213   31.641  -44.764 1.00 45.34 ? 46  VAL D CG2   1 
ATOM   3303  N N     . LEU B  1 47  ? 1.825   27.741  -45.699 1.00 37.03 ? 47  LEU D N     1 
ATOM   3304  C CA    . LEU B  1 47  ? 1.431   26.456  -45.170 1.00 35.97 ? 47  LEU D CA    1 
ATOM   3305  C C     . LEU B  1 47  ? 2.696   25.716  -44.785 1.00 38.51 ? 47  LEU D C     1 
ATOM   3306  O O     . LEU B  1 47  ? 3.754   25.911  -45.388 1.00 40.06 ? 47  LEU D O     1 
ATOM   3307  C CB    . LEU B  1 47  ? 0.628   25.639  -46.181 1.00 35.92 ? 47  LEU D CB    1 
ATOM   3308  C CG    . LEU B  1 47  ? 0.207   24.237  -45.728 1.00 41.52 ? 47  LEU D CG    1 
ATOM   3309  C CD1   . LEU B  1 47  ? -0.697  24.293  -44.451 1.00 37.51 ? 47  LEU D CD1   1 
ATOM   3310  C CD2   . LEU B  1 47  ? -0.464  23.487  -46.877 1.00 30.88 ? 47  LEU D CD2   1 
ATOM   3311  N N     . VAL B  1 48  ? 2.589   24.902  -43.746 1.00 42.11 ? 48  VAL D N     1 
ATOM   3312  C CA    . VAL B  1 48  ? 3.638   23.967  -43.374 1.00 39.47 ? 48  VAL D CA    1 
ATOM   3313  C C     . VAL B  1 48  ? 3.084   22.564  -43.549 1.00 42.12 ? 48  VAL D C     1 
ATOM   3314  O O     . VAL B  1 48  ? 1.962   22.276  -43.107 1.00 46.86 ? 48  VAL D O     1 
ATOM   3315  C CB    . VAL B  1 48  ? 4.118   24.185  -41.933 1.00 37.54 ? 48  VAL D CB    1 
ATOM   3316  C CG1   . VAL B  1 48  ? 5.150   23.163  -41.603 1.00 44.07 ? 48  VAL D CG1   1 
ATOM   3317  C CG2   . VAL B  1 48  ? 4.674   25.584  -41.766 1.00 26.88 ? 48  VAL D CG2   1 
ATOM   3318  N N     . ILE B  1 49  ? 3.842   21.712  -44.234 1.00 41.64 ? 49  ILE D N     1 
ATOM   3319  C CA    . ILE B  1 49  ? 3.433   20.328  -44.450 1.00 42.30 ? 49  ILE D CA    1 
ATOM   3320  C C     . ILE B  1 49  ? 4.612   19.418  -44.149 1.00 42.56 ? 49  ILE D C     1 
ATOM   3321  O O     . ILE B  1 49  ? 5.771   19.783  -44.403 1.00 47.55 ? 49  ILE D O     1 
ATOM   3322  C CB    . ILE B  1 49  ? 2.919   20.092  -45.882 1.00 45.59 ? 49  ILE D CB    1 
ATOM   3323  C CG1   . ILE B  1 49  ? 4.034   19.563  -46.801 1.00 44.45 ? 49  ILE D CG1   1 
ATOM   3324  C CG2   . ILE B  1 49  ? 2.312   21.361  -46.452 1.00 39.42 ? 49  ILE D CG2   1 
ATOM   3325  C CD1   . ILE B  1 49  ? 3.727   19.707  -48.295 1.00 38.98 ? 49  ILE D CD1   1 
ATOM   3326  N N     . PRO B  1 50  ? 4.366   18.247  -43.570 1.00 42.33 ? 50  PRO D N     1 
ATOM   3327  C CA    . PRO B  1 50  ? 5.375   17.185  -43.553 1.00 45.07 ? 50  PRO D CA    1 
ATOM   3328  C C     . PRO B  1 50  ? 5.282   16.251  -44.749 1.00 52.53 ? 50  PRO D C     1 
ATOM   3329  O O     . PRO B  1 50  ? 6.121   15.349  -44.868 1.00 60.01 ? 50  PRO D O     1 
ATOM   3330  C CB    . PRO B  1 50  ? 5.033   16.443  -42.257 1.00 45.63 ? 50  PRO D CB    1 
ATOM   3331  C CG    . PRO B  1 50  ? 3.530   16.530  -42.196 1.00 44.24 ? 50  PRO D CG    1 
ATOM   3332  C CD    . PRO B  1 50  ? 3.137   17.848  -42.864 1.00 43.60 ? 50  PRO D CD    1 
ATOM   3333  N N     . ASP B  1 51  ? 4.291   16.463  -45.624 1.00 54.60 ? 51  ASP D N     1 
ATOM   3334  C CA    . ASP B  1 51  ? 3.928   15.632  -46.764 1.00 46.05 ? 51  ASP D CA    1 
ATOM   3335  C C     . ASP B  1 51  ? 4.588   16.180  -48.036 1.00 48.06 ? 51  ASP D C     1 
ATOM   3336  O O     . ASP B  1 51  ? 5.598   16.892  -47.969 1.00 46.97 ? 51  ASP D O     1 
ATOM   3337  C CB    . ASP B  1 51  ? 2.390   15.586  -46.890 1.00 42.89 ? 51  ASP D CB    1 
ATOM   3338  C CG    . ASP B  1 51  ? 1.710   14.853  -45.726 1.00 48.78 ? 51  ASP D CG    1 
ATOM   3339  O OD1   . ASP B  1 51  ? 2.263   14.867  -44.605 1.00 55.82 ? 51  ASP D OD1   1 
ATOM   3340  O OD2   . ASP B  1 51  ? 0.615   14.263  -45.921 1.00 43.96 ? 51  ASP D OD2   1 
ATOM   3341  N N     . THR B  1 52  ? 4.024   15.834  -49.200 1.00 49.53 ? 52  THR D N     1 
ATOM   3342  C CA    . THR B  1 52  ? 4.316   16.442  -50.491 1.00 42.21 ? 52  THR D CA    1 
ATOM   3343  C C     . THR B  1 52  ? 3.035   16.983  -51.092 1.00 44.38 ? 52  THR D C     1 
ATOM   3344  O O     . THR B  1 52  ? 1.937   16.525  -50.781 1.00 41.20 ? 52  THR D O     1 
ATOM   3345  C CB    . THR B  1 52  ? 4.875   15.456  -51.504 1.00 41.10 ? 52  THR D CB    1 
ATOM   3346  O OG1   . THR B  1 52  ? 5.288   14.262  -50.839 1.00 46.87 ? 52  THR D OG1   1 
ATOM   3347  C CG2   . THR B  1 52  ? 6.015   16.091  -52.298 1.00 39.64 ? 52  THR D CG2   1 
ATOM   3348  N N     . VAL B  1 53  ? 3.190   17.915  -52.020 1.00 42.31 ? 53  VAL D N     1 
ATOM   3349  C CA    . VAL B  1 53  ? 2.064   18.458  -52.760 1.00 42.86 ? 53  VAL D CA    1 
ATOM   3350  C C     . VAL B  1 53  ? 2.159   17.981  -54.201 1.00 41.03 ? 53  VAL D C     1 
ATOM   3351  O O     . VAL B  1 53  ? 3.225   18.068  -54.826 1.00 42.76 ? 53  VAL D O     1 
ATOM   3352  C CB    . VAL B  1 53  ? 2.037   19.993  -52.689 1.00 46.72 ? 53  VAL D CB    1 
ATOM   3353  C CG1   . VAL B  1 53  ? 3.415   20.573  -53.035 1.00 47.41 ? 53  VAL D CG1   1 
ATOM   3354  C CG2   . VAL B  1 53  ? 0.973   20.532  -53.594 1.00 41.28 ? 53  VAL D CG2   1 
ATOM   3355  N N     . ASP B  1 54  ? 1.060   17.444  -54.711 1.00 39.93 ? 54  ASP D N     1 
ATOM   3356  C CA    . ASP B  1 54  ? 0.925   17.270  -56.144 1.00 38.89 ? 54  ASP D CA    1 
ATOM   3357  C C     . ASP B  1 54  ? 1.266   18.600  -56.809 1.00 43.10 ? 54  ASP D C     1 
ATOM   3358  O O     . ASP B  1 54  ? 0.597   19.607  -56.531 1.00 46.05 ? 54  ASP D O     1 
ATOM   3359  C CB    . ASP B  1 54  ? -0.498  16.834  -56.502 1.00 40.42 ? 54  ASP D CB    1 
ATOM   3360  C CG    . ASP B  1 54  ? -0.677  16.567  -57.995 1.00 39.54 ? 54  ASP D CG    1 
ATOM   3361  O OD1   . ASP B  1 54  ? -0.426  17.479  -58.804 1.00 36.07 ? 54  ASP D OD1   1 
ATOM   3362  O OD2   . ASP B  1 54  ? -1.066  15.439  -58.366 1.00 41.06 ? 54  ASP D OD2   1 
ATOM   3363  N N     . PRO B  1 55  ? 2.291   18.651  -57.675 1.00 36.57 ? 55  PRO D N     1 
ATOM   3364  C CA    . PRO B  1 55  ? 2.825   19.944  -58.147 1.00 32.77 ? 55  PRO D CA    1 
ATOM   3365  C C     . PRO B  1 55  ? 1.770   20.952  -58.577 1.00 36.04 ? 55  PRO D C     1 
ATOM   3366  O O     . PRO B  1 55  ? 1.965   22.176  -58.459 1.00 33.74 ? 55  PRO D O     1 
ATOM   3367  C CB    . PRO B  1 55  ? 3.709   19.534  -59.325 1.00 35.32 ? 55  PRO D CB    1 
ATOM   3368  C CG    . PRO B  1 55  ? 4.145   18.137  -58.993 1.00 38.43 ? 55  PRO D CG    1 
ATOM   3369  C CD    . PRO B  1 55  ? 3.039   17.500  -58.208 1.00 35.27 ? 55  PRO D CD    1 
ATOM   3370  N N     . ASP B  1 56  ? 0.637   20.434  -59.049 1.00 34.42 ? 56  ASP D N     1 
ATOM   3371  C CA    . ASP B  1 56  ? -0.462  21.225  -59.586 1.00 30.99 ? 56  ASP D CA    1 
ATOM   3372  C C     . ASP B  1 56  ? -1.432  21.729  -58.525 1.00 39.66 ? 56  ASP D C     1 
ATOM   3373  O O     . ASP B  1 56  ? -2.060  22.778  -58.727 1.00 40.05 ? 56  ASP D O     1 
ATOM   3374  C CB    . ASP B  1 56  ? -1.234  20.380  -60.593 1.00 38.14 ? 56  ASP D CB    1 
ATOM   3375  C CG    . ASP B  1 56  ? -0.731  20.567  -62.012 1.00 44.80 ? 56  ASP D CG    1 
ATOM   3376  O OD1   . ASP B  1 56  ? -1.118  21.573  -62.655 1.00 41.88 ? 56  ASP D OD1   1 
ATOM   3377  O OD2   . ASP B  1 56  ? 0.060   19.715  -62.482 1.00 43.89 ? 56  ASP D OD2   1 
ATOM   3378  N N     . PHE B  1 57  ? -1.576  20.990  -57.410 1.00 37.16 ? 57  PHE D N     1 
ATOM   3379  C CA    . PHE B  1 57  ? -2.547  21.189  -56.336 1.00 35.23 ? 57  PHE D CA    1 
ATOM   3380  C C     . PHE B  1 57  ? -2.653  22.610  -55.785 1.00 32.62 ? 57  PHE D C     1 
ATOM   3381  O O     . PHE B  1 57  ? -3.744  23.007  -55.369 1.00 30.08 ? 57  PHE D O     1 
ATOM   3382  C CB    . PHE B  1 57  ? -2.217  20.232  -55.198 1.00 35.78 ? 57  PHE D CB    1 
ATOM   3383  C CG    . PHE B  1 57  ? -3.296  20.110  -54.169 1.00 39.73 ? 57  PHE D CG    1 
ATOM   3384  C CD1   . PHE B  1 57  ? -3.358  20.985  -53.095 1.00 43.21 ? 57  PHE D CD1   1 
ATOM   3385  C CD2   . PHE B  1 57  ? -4.220  19.092  -54.246 1.00 36.07 ? 57  PHE D CD2   1 
ATOM   3386  C CE1   . PHE B  1 57  ? -4.339  20.852  -52.130 1.00 38.87 ? 57  PHE D CE1   1 
ATOM   3387  C CE2   . PHE B  1 57  ? -5.198  18.958  -53.294 1.00 38.37 ? 57  PHE D CE2   1 
ATOM   3388  C CZ    . PHE B  1 57  ? -5.265  19.843  -52.234 1.00 38.90 ? 57  PHE D CZ    1 
ATOM   3389  N N     . PRO B  1 58  ? -1.569  23.389  -55.702 1.00 32.37 ? 58  PRO D N     1 
ATOM   3390  C CA    . PRO B  1 58  ? -1.709  24.767  -55.211 1.00 27.37 ? 58  PRO D CA    1 
ATOM   3391  C C     . PRO B  1 58  ? -2.354  25.703  -56.198 1.00 31.10 ? 58  PRO D C     1 
ATOM   3392  O O     . PRO B  1 58  ? -3.285  26.427  -55.837 1.00 37.98 ? 58  PRO D O     1 
ATOM   3393  C CB    . PRO B  1 58  ? -0.267  25.192  -54.942 1.00 27.84 ? 58  PRO D CB    1 
ATOM   3394  C CG    . PRO B  1 58  ? 0.415   23.905  -54.632 1.00 35.57 ? 58  PRO D CG    1 
ATOM   3395  C CD    . PRO B  1 58  ? -0.166  22.955  -55.632 1.00 32.74 ? 58  PRO D CD    1 
ATOM   3396  N N     . GLY B  1 59  ? -1.847  25.741  -57.430 1.00 30.96 ? 59  GLY D N     1 
ATOM   3397  C CA    . GLY B  1 59  ? -2.488  26.568  -58.439 1.00 22.49 ? 59  GLY D CA    1 
ATOM   3398  C C     . GLY B  1 59  ? -3.956  26.236  -58.577 1.00 31.16 ? 59  GLY D C     1 
ATOM   3399  O O     . GLY B  1 59  ? -4.819  27.116  -58.518 1.00 31.55 ? 59  GLY D O     1 
ATOM   3400  N N     . TYR B  1 60  ? -4.262  24.946  -58.718 1.00 28.97 ? 60  TYR D N     1 
ATOM   3401  C CA    . TYR B  1 60  ? -5.647  24.508  -58.793 1.00 27.00 ? 60  TYR D CA    1 
ATOM   3402  C C     . TYR B  1 60  ? -6.460  25.021  -57.602 1.00 35.73 ? 60  TYR D C     1 
ATOM   3403  O O     . TYR B  1 60  ? -7.494  25.680  -57.775 1.00 32.30 ? 60  TYR D O     1 
ATOM   3404  C CB    . TYR B  1 60  ? -5.680  22.990  -58.870 1.00 29.96 ? 60  TYR D CB    1 
ATOM   3405  C CG    . TYR B  1 60  ? -6.980  22.399  -58.398 1.00 36.87 ? 60  TYR D CG    1 
ATOM   3406  C CD1   . TYR B  1 60  ? -8.143  22.570  -59.140 1.00 38.75 ? 60  TYR D CD1   1 
ATOM   3407  C CD2   . TYR B  1 60  ? -7.060  21.684  -57.201 1.00 34.34 ? 60  TYR D CD2   1 
ATOM   3408  C CE1   . TYR B  1 60  ? -9.354  22.030  -58.723 1.00 35.56 ? 60  TYR D CE1   1 
ATOM   3409  C CE2   . TYR B  1 60  ? -8.267  21.145  -56.773 1.00 36.41 ? 60  TYR D CE2   1 
ATOM   3410  C CZ    . TYR B  1 60  ? -9.416  21.324  -57.548 1.00 37.04 ? 60  TYR D CZ    1 
ATOM   3411  O OH    . TYR B  1 60  ? -10.641 20.814  -57.162 1.00 37.47 ? 60  TYR D OH    1 
ATOM   3412  N N     . VAL B  1 61  ? -5.991  24.744  -56.374 1.00 35.42 ? 61  VAL D N     1 
ATOM   3413  C CA    . VAL B  1 61  ? -6.698  25.210  -55.179 1.00 33.96 ? 61  VAL D CA    1 
ATOM   3414  C C     . VAL B  1 61  ? -6.828  26.727  -55.197 1.00 29.46 ? 61  VAL D C     1 
ATOM   3415  O O     . VAL B  1 61  ? -7.904  27.274  -54.936 1.00 31.85 ? 61  VAL D O     1 
ATOM   3416  C CB    . VAL B  1 61  ? -5.997  24.705  -53.896 1.00 29.54 ? 61  VAL D CB    1 
ATOM   3417  C CG1   . VAL B  1 61  ? -6.514  25.429  -52.671 1.00 27.65 ? 61  VAL D CG1   1 
ATOM   3418  C CG2   . VAL B  1 61  ? -6.221  23.204  -53.713 1.00 29.35 ? 61  VAL D CG2   1 
ATOM   3419  N N     . ALA B  1 62  ? -5.749  27.429  -55.537 1.00 25.87 ? 62  ALA D N     1 
ATOM   3420  C CA    . ALA B  1 62  ? -5.776  28.885  -55.517 1.00 31.27 ? 62  ALA D CA    1 
ATOM   3421  C C     . ALA B  1 62  ? -6.518  29.480  -56.702 1.00 38.91 ? 62  ALA D C     1 
ATOM   3422  O O     . ALA B  1 62  ? -6.914  30.649  -56.637 1.00 37.29 ? 62  ALA D O     1 
ATOM   3423  C CB    . ALA B  1 62  ? -4.357  29.442  -55.499 1.00 37.69 ? 62  ALA D CB    1 
ATOM   3424  N N     . ASP B  1 63  ? -6.673  28.728  -57.798 1.00 37.78 ? 63  ASP D N     1 
ATOM   3425  C CA    . ASP B  1 63  ? -7.529  29.194  -58.885 1.00 38.86 ? 63  ASP D CA    1 
ATOM   3426  C C     . ASP B  1 63  ? -8.983  29.092  -58.471 1.00 38.21 ? 63  ASP D C     1 
ATOM   3427  O O     . ASP B  1 63  ? -9.741  30.066  -58.581 1.00 37.67 ? 63  ASP D O     1 
ATOM   3428  C CB    . ASP B  1 63  ? -7.275  28.386  -60.160 1.00 37.55 ? 63  ASP D CB    1 
ATOM   3429  C CG    . ASP B  1 63  ? -6.206  29.001  -61.027 1.00 40.98 ? 63  ASP D CG    1 
ATOM   3430  O OD1   . ASP B  1 63  ? -5.989  30.232  -60.924 1.00 48.16 ? 63  ASP D OD1   1 
ATOM   3431  O OD2   . ASP B  1 63  ? -5.582  28.256  -61.808 1.00 39.61 ? 63  ASP D OD2   1 
ATOM   3432  N N     . THR B  1 64  ? -9.368  27.919  -57.945 1.00 35.60 ? 64  THR D N     1 
ATOM   3433  C CA    . THR B  1 64  ? -10.692 27.726  -57.362 1.00 36.43 ? 64  THR D CA    1 
ATOM   3434  C C     . THR B  1 64  ? -10.976 28.761  -56.279 1.00 34.75 ? 64  THR D C     1 
ATOM   3435  O O     . THR B  1 64  ? -12.001 29.451  -56.321 1.00 38.38 ? 64  THR D O     1 
ATOM   3436  C CB    . THR B  1 64  ? -10.797 26.317  -56.781 1.00 37.55 ? 64  THR D CB    1 
ATOM   3437  O OG1   . THR B  1 64  ? -9.805  25.478  -57.393 1.00 39.43 ? 64  THR D OG1   1 
ATOM   3438  C CG2   . THR B  1 64  ? -12.182 25.731  -57.017 1.00 26.09 ? 64  THR D CG2   1 
ATOM   3439  N N     . LEU B  1 65  ? -10.079 28.888  -55.296 1.00 35.36 ? 65  LEU D N     1 
ATOM   3440  C CA    . LEU B  1 65  ? -10.305 29.881  -54.255 1.00 34.40 ? 65  LEU D CA    1 
ATOM   3441  C C     . LEU B  1 65  ? -10.210 31.301  -54.778 1.00 34.11 ? 65  LEU D C     1 
ATOM   3442  O O     . LEU B  1 65  ? -10.441 32.239  -54.014 1.00 32.37 ? 65  LEU D O     1 
ATOM   3443  C CB    . LEU B  1 65  ? -9.311  29.687  -53.115 1.00 36.48 ? 65  LEU D CB    1 
ATOM   3444  C CG    . LEU B  1 65  ? -9.656  28.614  -52.081 1.00 35.64 ? 65  LEU D CG    1 
ATOM   3445  C CD1   . LEU B  1 65  ? -8.396  28.265  -51.312 1.00 32.22 ? 65  LEU D CD1   1 
ATOM   3446  C CD2   . LEU B  1 65  ? -10.774 29.057  -51.131 1.00 26.89 ? 65  LEU D CD2   1 
ATOM   3447  N N     . GLY B  1 66  ? -9.863  31.478  -56.051 1.00 38.76 ? 66  GLY D N     1 
ATOM   3448  C CA    . GLY B  1 66  ? -9.753  32.794  -56.643 1.00 41.24 ? 66  GLY D CA    1 
ATOM   3449  C C     . GLY B  1 66  ? -8.743  33.683  -55.951 1.00 37.64 ? 66  GLY D C     1 
ATOM   3450  O O     . GLY B  1 66  ? -9.064  34.816  -55.587 1.00 45.76 ? 66  GLY D O     1 
ATOM   3451  N N     . ILE B  1 67  ? -7.520  33.193  -55.758 1.00 33.82 ? 67  ILE D N     1 
ATOM   3452  C CA    . ILE B  1 67  ? -6.477  33.958  -55.091 1.00 37.37 ? 67  ILE D CA    1 
ATOM   3453  C C     . ILE B  1 67  ? -5.157  33.743  -55.829 1.00 45.59 ? 67  ILE D C     1 
ATOM   3454  O O     . ILE B  1 67  ? -4.992  32.784  -56.589 1.00 48.38 ? 67  ILE D O     1 
ATOM   3455  C CB    . ILE B  1 67  ? -6.350  33.571  -53.595 1.00 46.04 ? 67  ILE D CB    1 
ATOM   3456  C CG1   . ILE B  1 67  ? -5.928  32.106  -53.445 1.00 44.44 ? 67  ILE D CG1   1 
ATOM   3457  C CG2   . ILE B  1 67  ? -7.674  33.813  -52.830 1.00 41.28 ? 67  ILE D CG2   1 
ATOM   3458  C CD1   . ILE B  1 67  ? -5.379  31.750  -52.036 1.00 42.06 ? 67  ILE D CD1   1 
ATOM   3459  N N     . ASP B  1 68  ? -4.207  34.654  -55.587 1.00 45.58 ? 68  ASP D N     1 
ATOM   3460  C CA    . ASP B  1 68  ? -2.958  34.751  -56.354 1.00 42.76 ? 68  ASP D CA    1 
ATOM   3461  C C     . ASP B  1 68  ? -2.026  33.628  -55.942 1.00 42.02 ? 68  ASP D C     1 
ATOM   3462  O O     . ASP B  1 68  ? -1.240  33.763  -55.008 1.00 45.12 ? 68  ASP D O     1 
ATOM   3463  C CB    . ASP B  1 68  ? -2.297  36.109  -56.131 1.00 46.12 ? 68  ASP D CB    1 
ATOM   3464  C CG    . ASP B  1 68  ? -0.897  36.187  -56.709 1.00 46.13 ? 68  ASP D CG    1 
ATOM   3465  O OD1   . ASP B  1 68  ? -0.559  35.364  -57.584 1.00 47.59 ? 68  ASP D OD1   1 
ATOM   3466  O OD2   . ASP B  1 68  ? -0.137  37.088  -56.291 1.00 46.27 ? 68  ASP D OD2   1 
ATOM   3467  N N     . GLY B  1 69  ? -2.095  32.519  -56.675 1.00 43.90 ? 69  GLY D N     1 
ATOM   3468  C CA    . GLY B  1 69  ? -1.296  31.349  -56.380 1.00 43.18 ? 69  GLY D CA    1 
ATOM   3469  C C     . GLY B  1 69  ? 0.117   31.708  -56.017 1.00 44.64 ? 69  GLY D C     1 
ATOM   3470  O O     . GLY B  1 69  ? 0.657   31.223  -55.012 1.00 41.64 ? 69  GLY D O     1 
ATOM   3471  N N     . THR B  1 70  ? 0.699   32.622  -56.799 1.00 43.77 ? 70  THR D N     1 
ATOM   3472  C CA    . THR B  1 70  ? 2.079   33.041  -56.583 1.00 47.03 ? 70  THR D CA    1 
ATOM   3473  C C     . THR B  1 70  ? 2.271   33.825  -55.287 1.00 49.21 ? 70  THR D C     1 
ATOM   3474  O O     . THR B  1 70  ? 3.416   34.119  -54.920 1.00 46.41 ? 70  THR D O     1 
ATOM   3475  C CB    . THR B  1 70  ? 2.562   33.873  -57.767 1.00 38.41 ? 70  THR D CB    1 
ATOM   3476  O OG1   . THR B  1 70  ? 2.063   35.210  -57.644 1.00 38.70 ? 70  THR D OG1   1 
ATOM   3477  C CG2   . THR B  1 70  ? 2.049   33.264  -59.041 1.00 40.55 ? 70  THR D CG2   1 
ATOM   3478  N N     . SER B  1 71  ? 1.189   34.190  -54.601 1.00 47.26 ? 71  SER D N     1 
ATOM   3479  C CA    . SER B  1 71  ? 1.247   34.888  -53.326 1.00 45.55 ? 71  SER D CA    1 
ATOM   3480  C C     . SER B  1 71  ? 1.036   33.946  -52.155 1.00 47.37 ? 71  SER D C     1 
ATOM   3481  O O     . SER B  1 71  ? 0.678   34.400  -51.065 1.00 48.90 ? 71  SER D O     1 
ATOM   3482  C CB    . SER B  1 71  ? 0.193   35.988  -53.279 1.00 47.91 ? 71  SER D CB    1 
ATOM   3483  O OG    . SER B  1 71  ? -1.087  35.400  -53.100 1.00 43.17 ? 71  SER D OG    1 
ATOM   3484  N N     . VAL B  1 72  ? 1.229   32.646  -52.362 1.00 48.95 ? 72  VAL D N     1 
ATOM   3485  C CA    . VAL B  1 72  ? 0.899   31.620  -51.381 1.00 44.55 ? 72  VAL D CA    1 
ATOM   3486  C C     . VAL B  1 72  ? 2.064   30.634  -51.295 1.00 49.64 ? 72  VAL D C     1 
ATOM   3487  O O     . VAL B  1 72  ? 2.566   30.174  -52.326 1.00 44.75 ? 72  VAL D O     1 
ATOM   3488  C CB    . VAL B  1 72  ? -0.410  30.912  -51.763 1.00 36.97 ? 72  VAL D CB    1 
ATOM   3489  C CG1   . VAL B  1 72  ? -0.520  29.582  -51.060 1.00 39.98 ? 72  VAL D CG1   1 
ATOM   3490  C CG2   . VAL B  1 72  ? -1.571  31.807  -51.419 1.00 41.45 ? 72  VAL D CG2   1 
ATOM   3491  N N     . HIS B  1 73  ? 2.503   30.317  -50.071 1.00 45.86 ? 73  HIS D N     1 
ATOM   3492  C CA    . HIS B  1 73  ? 3.731   29.561  -49.884 1.00 42.64 ? 73  HIS D CA    1 
ATOM   3493  C C     . HIS B  1 73  ? 3.474   28.207  -49.228 1.00 41.66 ? 73  HIS D C     1 
ATOM   3494  O O     . HIS B  1 73  ? 2.472   27.996  -48.539 1.00 44.20 ? 73  HIS D O     1 
ATOM   3495  C CB    . HIS B  1 73  ? 4.742   30.355  -49.058 1.00 42.53 ? 73  HIS D CB    1 
ATOM   3496  C CG    . HIS B  1 73  ? 5.672   31.182  -49.888 1.00 52.36 ? 73  HIS D CG    1 
ATOM   3497  N ND1   . HIS B  1 73  ? 5.508   32.540  -50.061 1.00 57.42 ? 73  HIS D ND1   1 
ATOM   3498  C CD2   . HIS B  1 73  ? 6.770   30.841  -50.609 1.00 56.98 ? 73  HIS D CD2   1 
ATOM   3499  C CE1   . HIS B  1 73  ? 6.470   33.001  -50.845 1.00 60.55 ? 73  HIS D CE1   1 
ATOM   3500  N NE2   . HIS B  1 73  ? 7.248   31.991  -51.191 1.00 51.67 ? 73  HIS D NE2   1 
ATOM   3501  N N     . VAL B  1 74  ? 4.405   27.286  -49.466 1.00 34.84 ? 74  VAL D N     1 
ATOM   3502  C CA    . VAL B  1 74  ? 4.404   25.961  -48.866 1.00 33.89 ? 74  VAL D CA    1 
ATOM   3503  C C     . VAL B  1 74  ? 5.807   25.674  -48.368 1.00 38.43 ? 74  VAL D C     1 
ATOM   3504  O O     . VAL B  1 74  ? 6.753   25.606  -49.163 1.00 38.65 ? 74  VAL D O     1 
ATOM   3505  C CB    . VAL B  1 74  ? 3.983   24.871  -49.856 1.00 35.37 ? 74  VAL D CB    1 
ATOM   3506  C CG1   . VAL B  1 74  ? 4.387   23.529  -49.295 1.00 35.93 ? 74  VAL D CG1   1 
ATOM   3507  C CG2   . VAL B  1 74  ? 2.509   24.941  -50.119 1.00 35.04 ? 74  VAL D CG2   1 
ATOM   3508  N N     . GLU B  1 75  ? 5.942   25.482  -47.072 1.00 45.30 ? 75  GLU D N     1 
ATOM   3509  C CA    . GLU B  1 75  ? 7.223   25.203  -46.448 1.00 41.61 ? 75  GLU D CA    1 
ATOM   3510  C C     . GLU B  1 75  ? 7.181   23.764  -45.950 1.00 40.30 ? 75  GLU D C     1 
ATOM   3511  O O     . GLU B  1 75  ? 6.464   23.447  -44.998 1.00 42.34 ? 75  GLU D O     1 
ATOM   3512  C CB    . GLU B  1 75  ? 7.480   26.200  -45.323 1.00 47.33 ? 75  GLU D CB    1 
ATOM   3513  C CG    . GLU B  1 75  ? 8.939   26.555  -45.101 1.00 46.10 ? 75  GLU D CG    1 
ATOM   3514  C CD    . GLU B  1 75  ? 9.446   27.616  -46.039 1.00 49.22 ? 75  GLU D CD    1 
ATOM   3515  O OE1   . GLU B  1 75  ? 8.609   28.319  -46.634 1.00 46.19 ? 75  GLU D OE1   1 
ATOM   3516  O OE2   . GLU B  1 75  ? 10.682  27.753  -46.174 1.00 52.47 ? 75  GLU D OE2   1 
ATOM   3517  N N     . ARG B  1 76  ? 7.924   22.891  -46.607 1.00 45.30 ? 76  ARG D N     1 
ATOM   3518  C CA    . ARG B  1 76  ? 7.904   21.473  -46.279 1.00 51.10 ? 76  ARG D CA    1 
ATOM   3519  C C     . ARG B  1 76  ? 8.958   21.156  -45.227 1.00 51.37 ? 76  ARG D C     1 
ATOM   3520  O O     . ARG B  1 76  ? 10.074  21.677  -45.279 1.00 49.51 ? 76  ARG D O     1 
ATOM   3521  C CB    . ARG B  1 76  ? 8.154   20.634  -47.536 1.00 46.18 ? 76  ARG D CB    1 
ATOM   3522  C CG    . ARG B  1 76  ? 8.541   19.186  -47.277 1.00 50.37 ? 76  ARG D CG    1 
ATOM   3523  C CD    . ARG B  1 76  ? 9.915   18.907  -47.872 1.00 59.30 ? 76  ARG D CD    1 
ATOM   3524  N NE    . ARG B  1 76  ? 10.211  17.484  -48.003 1.00 59.71 ? 76  ARG D NE    1 
ATOM   3525  C CZ    . ARG B  1 76  ? 11.293  17.005  -48.601 1.00 60.33 ? 76  ARG D CZ    1 
ATOM   3526  N NH1   . ARG B  1 76  ? 12.206  17.808  -49.125 1.00 56.48 ? 76  ARG D NH1   1 
ATOM   3527  N NH2   . ARG B  1 76  ? 11.474  15.688  -48.659 1.00 67.10 ? 76  ARG D NH2   1 
ATOM   3528  N N     . THR B  1 77  ? 8.587   20.328  -44.255 1.00 48.92 ? 77  THR D N     1 
ATOM   3529  C CA    . THR B  1 77  ? 9.551   19.586  -43.456 1.00 50.24 ? 77  THR D CA    1 
ATOM   3530  C C     . THR B  1 77  ? 9.599   18.158  -43.973 1.00 48.40 ? 77  THR D C     1 
ATOM   3531  O O     . THR B  1 77  ? 8.664   17.679  -44.611 1.00 54.90 ? 77  THR D O     1 
ATOM   3532  C CB    . THR B  1 77  ? 9.189   19.586  -41.963 1.00 50.25 ? 77  THR D CB    1 
ATOM   3533  O OG1   . THR B  1 77  ? 7.832   19.155  -41.782 1.00 45.27 ? 77  THR D OG1   1 
ATOM   3534  C CG2   . THR B  1 77  ? 9.372   20.966  -41.362 1.00 43.04 ? 77  THR D CG2   1 
ATOM   3535  N N     . GLN B  1 78  ? 10.701  17.477  -43.703 1.00 50.59 ? 78  GLN D N     1 
ATOM   3536  C CA    . GLN B  1 78  ? 10.802  16.067  -44.045 1.00 56.36 ? 78  GLN D CA    1 
ATOM   3537  C C     . GLN B  1 78  ? 10.606  15.180  -42.825 1.00 49.40 ? 78  GLN D C     1 
ATOM   3538  O O     . GLN B  1 78  ? 10.815  13.968  -42.903 1.00 53.72 ? 78  GLN D O     1 
ATOM   3539  C CB    . GLN B  1 78  ? 12.147  15.783  -44.716 1.00 58.43 ? 78  GLN D CB    1 
ATOM   3540  C CG    . GLN B  1 78  ? 12.638  16.915  -45.616 1.00 58.08 ? 78  GLN D CG    1 
ATOM   3541  C CD    . GLN B  1 78  ? 13.681  16.466  -46.646 1.00 70.10 ? 78  GLN D CD    1 
ATOM   3542  O OE1   . GLN B  1 78  ? 13.620  15.348  -47.170 1.00 67.90 ? 78  GLN D OE1   1 
ATOM   3543  N NE2   . GLN B  1 78  ? 14.630  17.352  -46.955 1.00 64.19 ? 78  GLN D NE2   1 
ATOM   3544  N N     . THR B  1 79  ? 10.211  15.763  -41.707 1.00 49.72 ? 79  THR D N     1 
ATOM   3545  C CA    . THR B  1 79  ? 9.960   15.075  -40.455 1.00 45.52 ? 79  THR D CA    1 
ATOM   3546  C C     . THR B  1 79  ? 8.686   15.657  -39.876 1.00 48.98 ? 79  THR D C     1 
ATOM   3547  O O     . THR B  1 79  ? 8.334   16.803  -40.178 1.00 47.76 ? 79  THR D O     1 
ATOM   3548  C CB    . THR B  1 79  ? 11.105  15.287  -39.466 1.00 49.83 ? 79  THR D CB    1 
ATOM   3549  O OG1   . THR B  1 79  ? 11.219  16.693  -39.215 1.00 56.28 ? 79  THR D OG1   1 
ATOM   3550  C CG2   . THR B  1 79  ? 12.416  14.751  -40.036 1.00 55.57 ? 79  THR D CG2   1 
ATOM   3551  N N     . PRO B  1 80  ? 7.985   14.908  -39.023 1.00 47.76 ? 80  PRO D N     1 
ATOM   3552  C CA    . PRO B  1 80  ? 6.649   15.340  -38.602 1.00 38.00 ? 80  PRO D CA    1 
ATOM   3553  C C     . PRO B  1 80  ? 6.699   16.659  -37.847 1.00 44.10 ? 80  PRO D C     1 
ATOM   3554  O O     . PRO B  1 80  ? 7.734   17.069  -37.318 1.00 42.00 ? 80  PRO D O     1 
ATOM   3555  C CB    . PRO B  1 80  ? 6.163   14.195  -37.709 1.00 41.64 ? 80  PRO D CB    1 
ATOM   3556  C CG    . PRO B  1 80  ? 7.108   13.062  -37.944 1.00 41.76 ? 80  PRO D CG    1 
ATOM   3557  C CD    . PRO B  1 80  ? 8.401   13.671  -38.348 1.00 42.83 ? 80  PRO D CD    1 
ATOM   3558  N N     . LEU B  1 81  ? 5.551   17.339  -37.828 1.00 46.05 ? 81  LEU D N     1 
ATOM   3559  C CA    . LEU B  1 81  ? 5.407   18.688  -37.272 1.00 43.96 ? 81  LEU D CA    1 
ATOM   3560  C C     . LEU B  1 81  ? 5.173   18.591  -35.776 1.00 44.82 ? 81  LEU D C     1 
ATOM   3561  O O     . LEU B  1 81  ? 4.035   18.639  -35.316 1.00 47.98 ? 81  LEU D O     1 
ATOM   3562  C CB    . LEU B  1 81  ? 4.243   19.414  -37.932 1.00 39.49 ? 81  LEU D CB    1 
ATOM   3563  C CG    . LEU B  1 81  ? 4.489   19.857  -39.361 1.00 54.04 ? 81  LEU D CG    1 
ATOM   3564  C CD1   . LEU B  1 81  ? 3.330   20.717  -39.865 1.00 49.08 ? 81  LEU D CD1   1 
ATOM   3565  C CD2   . LEU B  1 81  ? 5.831   20.600  -39.418 1.00 52.95 ? 81  LEU D CD2   1 
ATOM   3566  N N     . SER B  1 82  ? 6.247   18.489  -34.997 1.00 43.51 ? 82  SER D N     1 
ATOM   3567  C CA    . SER B  1 82  ? 6.118   18.180  -33.576 1.00 38.26 ? 82  SER D CA    1 
ATOM   3568  C C     . SER B  1 82  ? 6.623   19.336  -32.722 1.00 38.13 ? 82  SER D C     1 
ATOM   3569  O O     . SER B  1 82  ? 7.100   20.360  -33.227 1.00 41.91 ? 82  SER D O     1 
ATOM   3570  C CB    . SER B  1 82  ? 6.880   16.910  -33.221 1.00 35.49 ? 82  SER D CB    1 
ATOM   3571  O OG    . SER B  1 82  ? 8.239   17.233  -33.055 1.00 38.88 ? 82  SER D OG    1 
ATOM   3572  N N     . GLU B  1 83  ? 6.514   19.153  -31.405 1.00 27.73 ? 83  GLU D N     1 
ATOM   3573  C CA    . GLU B  1 83  ? 7.017   20.165  -30.487 1.00 31.56 ? 83  GLU D CA    1 
ATOM   3574  C C     . GLU B  1 83  ? 8.490   20.463  -30.753 1.00 34.45 ? 83  GLU D C     1 
ATOM   3575  O O     . GLU B  1 83  ? 8.900   21.632  -30.772 1.00 34.04 ? 83  GLU D O     1 
ATOM   3576  C CB    . GLU B  1 83  ? 6.810   19.705  -29.041 1.00 39.64 ? 83  GLU D CB    1 
ATOM   3577  C CG    . GLU B  1 83  ? 5.386   19.291  -28.701 1.00 30.65 ? 83  GLU D CG    1 
ATOM   3578  C CD    . GLU B  1 83  ? 4.704   20.343  -27.903 1.00 37.81 ? 83  GLU D CD    1 
ATOM   3579  O OE1   . GLU B  1 83  ? 4.929   21.524  -28.218 1.00 33.72 ? 83  GLU D OE1   1 
ATOM   3580  O OE2   . GLU B  1 83  ? 3.943   20.017  -26.955 1.00 51.42 ? 83  GLU D OE2   1 
ATOM   3581  N N     . ALA B  1 84  ? 9.295   19.414  -30.986 1.00 32.91 ? 84  ALA D N     1 
ATOM   3582  C CA    . ALA B  1 84  ? 10.731  19.593  -31.196 1.00 33.27 ? 84  ALA D CA    1 
ATOM   3583  C C     . ALA B  1 84  ? 10.995  20.522  -32.372 1.00 39.15 ? 84  ALA D C     1 
ATOM   3584  O O     . ALA B  1 84  ? 11.801  21.456  -32.270 1.00 39.39 ? 84  ALA D O     1 
ATOM   3585  C CB    . ALA B  1 84  ? 11.404  18.240  -31.420 1.00 27.69 ? 84  ALA D CB    1 
ATOM   3586  N N     . VAL B  1 85  ? 10.307  20.275  -33.497 1.00 36.00 ? 85  VAL D N     1 
ATOM   3587  C CA    . VAL B  1 85  ? 10.334  21.172  -34.654 1.00 40.39 ? 85  VAL D CA    1 
ATOM   3588  C C     . VAL B  1 85  ? 10.043  22.603  -34.225 1.00 41.24 ? 85  VAL D C     1 
ATOM   3589  O O     . VAL B  1 85  ? 10.836  23.523  -34.461 1.00 40.89 ? 85  VAL D O     1 
ATOM   3590  C CB    . VAL B  1 85  ? 9.312   20.719  -35.712 1.00 43.05 ? 85  VAL D CB    1 
ATOM   3591  C CG1   . VAL B  1 85  ? 9.127   21.812  -36.747 1.00 44.30 ? 85  VAL D CG1   1 
ATOM   3592  C CG2   . VAL B  1 85  ? 9.729   19.421  -36.368 1.00 40.02 ? 85  VAL D CG2   1 
ATOM   3593  N N     . LEU B  1 86  ? 8.879   22.804  -33.606 1.00 38.88 ? 86  LEU D N     1 
ATOM   3594  C CA    . LEU B  1 86  ? 8.426   24.148  -33.291 1.00 37.11 ? 86  LEU D CA    1 
ATOM   3595  C C     . LEU B  1 86  ? 9.454   24.899  -32.477 1.00 36.37 ? 86  LEU D C     1 
ATOM   3596  O O     . LEU B  1 86  ? 9.590   26.117  -32.632 1.00 30.24 ? 86  LEU D O     1 
ATOM   3597  C CB    . LEU B  1 86  ? 7.102   24.080  -32.539 1.00 41.94 ? 86  LEU D CB    1 
ATOM   3598  C CG    . LEU B  1 86  ? 5.898   23.467  -33.268 1.00 36.64 ? 86  LEU D CG    1 
ATOM   3599  C CD1   . LEU B  1 86  ? 4.620   23.943  -32.578 1.00 35.36 ? 86  LEU D CD1   1 
ATOM   3600  C CD2   . LEU B  1 86  ? 5.879   23.808  -34.770 1.00 38.76 ? 86  LEU D CD2   1 
ATOM   3601  N N     . GLN B  1 87  ? 10.182  24.187  -31.609 1.00 41.55 ? 87  GLN D N     1 
ATOM   3602  C CA    . GLN B  1 87  ? 11.263  24.777  -30.827 1.00 43.45 ? 87  GLN D CA    1 
ATOM   3603  C C     . GLN B  1 87  ? 12.536  24.946  -31.647 1.00 38.17 ? 87  GLN D C     1 
ATOM   3604  O O     . GLN B  1 87  ? 13.315  25.864  -31.378 1.00 43.52 ? 87  GLN D O     1 
ATOM   3605  C CB    . GLN B  1 87  ? 11.547  23.914  -29.587 1.00 46.89 ? 87  GLN D CB    1 
ATOM   3606  C CG    . GLN B  1 87  ? 10.780  24.282  -28.295 1.00 44.05 ? 87  GLN D CG    1 
ATOM   3607  C CD    . GLN B  1 87  ? 10.139  23.069  -27.575 1.00 47.66 ? 87  GLN D CD    1 
ATOM   3608  O OE1   . GLN B  1 87  ? 10.687  21.962  -27.570 1.00 49.70 ? 87  GLN D OE1   1 
ATOM   3609  N NE2   . GLN B  1 87  ? 8.987   23.295  -26.942 1.00 41.37 ? 87  GLN D NE2   1 
ATOM   3610  N N     . ASP B  1 88  ? 12.754  24.077  -32.631 1.00 41.09 ? 88  ASP D N     1 
ATOM   3611  C CA    . ASP B  1 88  ? 13.952  24.058  -33.471 1.00 42.37 ? 88  ASP D CA    1 
ATOM   3612  C C     . ASP B  1 88  ? 14.169  25.390  -34.186 1.00 41.44 ? 88  ASP D C     1 
ATOM   3613  O O     . ASP B  1 88  ? 13.325  25.791  -34.999 1.00 40.97 ? 88  ASP D O     1 
ATOM   3614  C CB    . ASP B  1 88  ? 13.837  22.926  -34.499 1.00 43.05 ? 88  ASP D CB    1 
ATOM   3615  C CG    . ASP B  1 88  ? 15.035  22.852  -35.440 1.00 51.70 ? 88  ASP D CG    1 
ATOM   3616  O OD1   . ASP B  1 88  ? 16.104  23.414  -35.096 1.00 48.06 ? 88  ASP D OD1   1 
ATOM   3617  O OD2   . ASP B  1 88  ? 14.907  22.213  -36.520 1.00 52.51 ? 88  ASP D OD2   1 
ATOM   3618  N N     . PRO B  1 89  ? 15.293  26.076  -33.950 1.00 44.60 ? 89  PRO D N     1 
ATOM   3619  C CA    . PRO B  1 89  ? 15.460  27.421  -34.519 1.00 42.48 ? 89  PRO D CA    1 
ATOM   3620  C C     . PRO B  1 89  ? 15.745  27.415  -36.005 1.00 46.18 ? 89  PRO D C     1 
ATOM   3621  O O     . PRO B  1 89  ? 15.445  28.404  -36.684 1.00 44.07 ? 89  PRO D O     1 
ATOM   3622  C CB    . PRO B  1 89  ? 16.635  27.996  -33.720 1.00 42.28 ? 89  PRO D CB    1 
ATOM   3623  C CG    . PRO B  1 89  ? 17.418  26.800  -33.298 1.00 42.66 ? 89  PRO D CG    1 
ATOM   3624  C CD    . PRO B  1 89  ? 16.445  25.666  -33.128 1.00 47.56 ? 89  PRO D CD    1 
ATOM   3625  N N     . GLU B  1 90  ? 16.337  26.337  -36.526 1.00 48.20 ? 90  GLU D N     1 
ATOM   3626  C CA    . GLU B  1 90  ? 16.414  26.152  -37.970 1.00 49.63 ? 90  GLU D CA    1 
ATOM   3627  C C     . GLU B  1 90  ? 15.024  26.241  -38.570 1.00 46.10 ? 90  GLU D C     1 
ATOM   3628  O O     . GLU B  1 90  ? 14.723  27.117  -39.390 1.00 43.98 ? 90  GLU D O     1 
ATOM   3629  C CB    . GLU B  1 90  ? 17.057  24.800  -38.298 1.00 45.61 ? 90  GLU D CB    1 
ATOM   3630  C CG    . GLU B  1 90  ? 18.505  24.653  -37.837 1.00 52.25 ? 90  GLU D CG    1 
ATOM   3631  C CD    . GLU B  1 90  ? 19.421  25.762  -38.359 1.00 67.15 ? 90  GLU D CD    1 
ATOM   3632  O OE1   . GLU B  1 90  ? 20.335  25.453  -39.166 1.00 63.25 ? 90  GLU D OE1   1 
ATOM   3633  O OE2   . GLU B  1 90  ? 19.245  26.941  -37.961 1.00 65.98 ? 90  GLU D OE2   1 
ATOM   3634  N N     . PHE B  1 91  ? 14.158  25.331  -38.140 1.00 43.66 ? 91  PHE D N     1 
ATOM   3635  C CA    . PHE B  1 91  ? 12.738  25.501  -38.366 1.00 43.60 ? 91  PHE D CA    1 
ATOM   3636  C C     . PHE B  1 91  ? 12.289  26.930  -38.073 1.00 42.02 ? 91  PHE D C     1 
ATOM   3637  O O     . PHE B  1 91  ? 11.558  27.533  -38.864 1.00 46.59 ? 91  PHE D O     1 
ATOM   3638  C CB    . PHE B  1 91  ? 11.951  24.523  -37.511 1.00 35.22 ? 91  PHE D CB    1 
ATOM   3639  C CG    . PHE B  1 91  ? 10.492  24.736  -37.604 1.00 43.10 ? 91  PHE D CG    1 
ATOM   3640  C CD1   . PHE B  1 91  ? 9.828   24.449  -38.779 1.00 42.74 ? 91  PHE D CD1   1 
ATOM   3641  C CD2   . PHE B  1 91  ? 9.778   25.275  -36.549 1.00 49.16 ? 91  PHE D CD2   1 
ATOM   3642  C CE1   . PHE B  1 91  ? 8.474   24.661  -38.894 1.00 40.91 ? 91  PHE D CE1   1 
ATOM   3643  C CE2   . PHE B  1 91  ? 8.409   25.483  -36.657 1.00 44.70 ? 91  PHE D CE2   1 
ATOM   3644  C CZ    . PHE B  1 91  ? 7.764   25.176  -37.834 1.00 40.05 ? 91  PHE D CZ    1 
ATOM   3645  N N     . ILE B  1 92  ? 12.721  27.503  -36.954 1.00 36.82 ? 92  ILE D N     1 
ATOM   3646  C CA    . ILE B  1 92  ? 12.164  28.797  -36.572 1.00 41.91 ? 92  ILE D CA    1 
ATOM   3647  C C     . ILE B  1 92  ? 12.594  29.893  -37.544 1.00 45.31 ? 92  ILE D C     1 
ATOM   3648  O O     . ILE B  1 92  ? 11.761  30.666  -38.035 1.00 44.13 ? 92  ILE D O     1 
ATOM   3649  C CB    . ILE B  1 92  ? 12.522  29.144  -35.122 1.00 39.74 ? 92  ILE D CB    1 
ATOM   3650  C CG1   . ILE B  1 92  ? 11.784  28.186  -34.187 1.00 38.46 ? 92  ILE D CG1   1 
ATOM   3651  C CG2   . ILE B  1 92  ? 12.178  30.598  -34.835 1.00 37.17 ? 92  ILE D CG2   1 
ATOM   3652  C CD1   . ILE B  1 92  ? 11.420  28.767  -32.882 1.00 35.06 ? 92  ILE D CD1   1 
ATOM   3653  N N     . ASP B  1 93  ? 13.886  29.971  -37.857 1.00 47.73 ? 93  ASP D N     1 
ATOM   3654  C CA    . ASP B  1 93  ? 14.325  30.995  -38.801 1.00 47.63 ? 93  ASP D CA    1 
ATOM   3655  C C     . ASP B  1 93  ? 13.727  30.792  -40.189 1.00 47.33 ? 93  ASP D C     1 
ATOM   3656  O O     . ASP B  1 93  ? 13.490  31.776  -40.901 1.00 44.93 ? 93  ASP D O     1 
ATOM   3657  C CB    . ASP B  1 93  ? 15.845  31.026  -38.874 1.00 48.79 ? 93  ASP D CB    1 
ATOM   3658  C CG    . ASP B  1 93  ? 16.465  31.429  -37.572 1.00 56.23 ? 93  ASP D CG    1 
ATOM   3659  O OD1   . ASP B  1 93  ? 16.364  32.622  -37.196 1.00 62.35 ? 93  ASP D OD1   1 
ATOM   3660  O OD2   . ASP B  1 93  ? 17.022  30.536  -36.906 1.00 54.63 ? 93  ASP D OD2   1 
ATOM   3661  N N     . ARG B  1 94  ? 13.487  29.541  -40.596 1.00 44.27 ? 94  ARG D N     1 
ATOM   3662  C CA    . ARG B  1 94  ? 12.750  29.295  -41.835 1.00 45.74 ? 94  ARG D CA    1 
ATOM   3663  C C     . ARG B  1 94  ? 11.517  30.189  -41.922 1.00 46.97 ? 94  ARG D C     1 
ATOM   3664  O O     . ARG B  1 94  ? 11.307  30.890  -42.918 1.00 48.75 ? 94  ARG D O     1 
ATOM   3665  C CB    . ARG B  1 94  ? 12.348  27.824  -41.925 1.00 44.34 ? 94  ARG D CB    1 
ATOM   3666  C CG    . ARG B  1 94  ? 13.417  26.933  -42.520 1.00 40.93 ? 94  ARG D CG    1 
ATOM   3667  C CD    . ARG B  1 94  ? 13.005  26.400  -43.895 1.00 50.41 ? 94  ARG D CD    1 
ATOM   3668  N NE    . ARG B  1 94  ? 12.016  25.326  -43.843 1.00 51.05 ? 94  ARG D NE    1 
ATOM   3669  C CZ    . ARG B  1 94  ? 11.452  24.767  -44.910 1.00 49.59 ? 94  ARG D CZ    1 
ATOM   3670  N NH1   . ARG B  1 94  ? 11.688  25.213  -46.135 1.00 49.57 ? 94  ARG D NH1   1 
ATOM   3671  N NH2   . ARG B  1 94  ? 10.612  23.750  -44.744 1.00 47.43 ? 94  ARG D NH2   1 
ATOM   3672  N N     . LEU B  1 95  ? 10.708  30.203  -40.859 1.00 49.88 ? 95  LEU D N     1 
ATOM   3673  C CA    . LEU B  1 95  ? 9.501   31.031  -40.839 1.00 50.36 ? 95  LEU D CA    1 
ATOM   3674  C C     . LEU B  1 95  ? 9.835   32.514  -40.706 1.00 51.09 ? 95  LEU D C     1 
ATOM   3675  O O     . LEU B  1 95  ? 9.167   33.370  -41.310 1.00 46.35 ? 95  LEU D O     1 
ATOM   3676  C CB    . LEU B  1 95  ? 8.582   30.588  -39.695 1.00 44.17 ? 95  LEU D CB    1 
ATOM   3677  C CG    . LEU B  1 95  ? 8.085   29.141  -39.762 1.00 38.43 ? 95  LEU D CG    1 
ATOM   3678  C CD1   . LEU B  1 95  ? 7.156   28.823  -38.622 1.00 31.69 ? 95  LEU D CD1   1 
ATOM   3679  C CD2   . LEU B  1 95  ? 7.392   28.891  -41.074 1.00 34.21 ? 95  LEU D CD2   1 
ATOM   3680  N N     . ALA B  1 96  ? 10.860  32.835  -39.912 1.00 50.12 ? 96  ALA D N     1 
ATOM   3681  C CA    . ALA B  1 96  ? 11.281  34.217  -39.749 1.00 52.23 ? 96  ALA D CA    1 
ATOM   3682  C C     . ALA B  1 96  ? 11.678  34.857  -41.068 1.00 46.59 ? 96  ALA D C     1 
ATOM   3683  O O     . ALA B  1 96  ? 11.649  36.087  -41.178 1.00 48.25 ? 96  ALA D O     1 
ATOM   3684  C CB    . ALA B  1 96  ? 12.444  34.296  -38.755 1.00 57.62 ? 96  ALA D CB    1 
ATOM   3685  N N     . ALA B  1 97  ? 12.051  34.055  -42.069 1.00 53.00 ? 97  ALA D N     1 
ATOM   3686  C CA    . ALA B  1 97  ? 12.322  34.613  -43.392 1.00 50.41 ? 97  ALA D CA    1 
ATOM   3687  C C     . ALA B  1 97  ? 11.090  35.297  -43.949 1.00 48.14 ? 97  ALA D C     1 
ATOM   3688  O O     . ALA B  1 97  ? 11.176  36.399  -44.502 1.00 43.35 ? 97  ALA D O     1 
ATOM   3689  C CB    . ALA B  1 97  ? 12.800  33.522  -44.348 1.00 41.91 ? 97  ALA D CB    1 
ATOM   3690  N N     . HIS B  1 98  ? 9.924   34.669  -43.785 1.00 48.15 ? 98  HIS D N     1 
ATOM   3691  C CA    . HIS B  1 98  ? 8.688   35.301  -44.227 1.00 49.84 ? 98  HIS D CA    1 
ATOM   3692  C C     . HIS B  1 98  ? 8.266   36.408  -43.275 1.00 50.35 ? 98  HIS D C     1 
ATOM   3693  O O     . HIS B  1 98  ? 7.986   37.531  -43.703 1.00 51.46 ? 98  HIS D O     1 
ATOM   3694  C CB    . HIS B  1 98  ? 7.590   34.262  -44.345 1.00 44.17 ? 98  HIS D CB    1 
ATOM   3695  C CG    . HIS B  1 98  ? 7.925   33.149  -45.278 1.00 49.83 ? 98  HIS D CG    1 
ATOM   3696  N ND1   . HIS B  1 98  ? 8.781   32.124  -44.932 1.00 52.65 ? 98  HIS D ND1   1 
ATOM   3697  C CD2   . HIS B  1 98  ? 7.519   32.892  -46.544 1.00 50.80 ? 98  HIS D CD2   1 
ATOM   3698  C CE1   . HIS B  1 98  ? 8.884   31.279  -45.945 1.00 48.38 ? 98  HIS D CE1   1 
ATOM   3699  N NE2   . HIS B  1 98  ? 8.125   31.720  -46.933 1.00 51.45 ? 98  HIS D NE2   1 
ATOM   3700  N N     . THR B  1 99  ? 8.229   36.114  -41.975 1.00 55.05 ? 99  THR D N     1 
ATOM   3701  C CA    . THR B  1 99  ? 7.641   37.065  -41.042 1.00 49.25 ? 99  THR D CA    1 
ATOM   3702  C C     . THR B  1 99  ? 8.540   38.269  -40.806 1.00 44.48 ? 99  THR D C     1 
ATOM   3703  O O     . THR B  1 99  ? 8.038   39.342  -40.459 1.00 45.84 ? 99  THR D O     1 
ATOM   3704  C CB    . THR B  1 99  ? 7.311   36.366  -39.723 1.00 48.62 ? 99  THR D CB    1 
ATOM   3705  O OG1   . THR B  1 99  ? 6.308   37.120  -39.039 1.00 52.62 ? 99  THR D OG1   1 
ATOM   3706  C CG2   . THR B  1 99  ? 8.542   36.235  -38.833 1.00 46.48 ? 99  THR D CG2   1 
ATOM   3707  N N     . GLY B  1 100 ? 9.850   38.122  -41.016 1.00 44.12 ? 100 GLY D N     1 
ATOM   3708  C CA    . GLY B  1 100 ? 10.800  39.203  -40.820 1.00 52.14 ? 100 GLY D CA    1 
ATOM   3709  C C     . GLY B  1 100 ? 10.644  39.952  -39.512 1.00 51.03 ? 100 GLY D C     1 
ATOM   3710  O O     . GLY B  1 100 ? 11.191  39.540  -38.484 1.00 52.21 ? 100 GLY D O     1 
ATOM   3711  N N     . THR B  1 101 ? 9.895   41.054  -39.530 1.00 44.11 ? 101 THR D N     1 
ATOM   3712  C CA    . THR B  1 101 ? 9.647   41.760  -38.280 1.00 52.83 ? 101 THR D CA    1 
ATOM   3713  C C     . THR B  1 101 ? 8.514   41.143  -37.469 1.00 49.91 ? 101 THR D C     1 
ATOM   3714  O O     . THR B  1 101 ? 8.433   41.387  -36.259 1.00 52.42 ? 101 THR D O     1 
ATOM   3715  C CB    . THR B  1 101 ? 9.284   43.211  -38.535 1.00 54.34 ? 101 THR D CB    1 
ATOM   3716  O OG1   . THR B  1 101 ? 7.865   43.293  -38.716 1.00 53.04 ? 101 THR D OG1   1 
ATOM   3717  C CG2   . THR B  1 101 ? 9.981   43.709  -39.794 1.00 61.02 ? 101 THR D CG2   1 
ATOM   3718  N N     . GLY B  1 102 ? 7.634   40.369  -38.105 1.00 45.64 ? 102 GLY D N     1 
ATOM   3719  C CA    . GLY B  1 102 ? 6.455   39.845  -37.454 1.00 46.92 ? 102 GLY D CA    1 
ATOM   3720  C C     . GLY B  1 102 ? 5.229   40.729  -37.546 1.00 49.77 ? 102 GLY D C     1 
ATOM   3721  O O     . GLY B  1 102 ? 4.116   40.252  -37.283 1.00 50.80 ? 102 GLY D O     1 
ATOM   3722  N N     . ALA B  1 103 ? 5.400   42.001  -37.917 1.00 54.46 ? 103 ALA D N     1 
ATOM   3723  C CA    . ALA B  1 103 ? 4.279   42.931  -37.986 1.00 50.13 ? 103 ALA D CA    1 
ATOM   3724  C C     . ALA B  1 103 ? 3.245   42.440  -38.982 1.00 51.84 ? 103 ALA D C     1 
ATOM   3725  O O     . ALA B  1 103 ? 3.588   42.028  -40.095 1.00 52.48 ? 103 ALA D O     1 
ATOM   3726  C CB    . ALA B  1 103 ? 4.764   44.321  -38.383 1.00 43.67 ? 103 ALA D CB    1 
ATOM   3727  N N     . GLY B  1 104 ? 1.977   42.477  -38.575 1.00 52.88 ? 104 GLY D N     1 
ATOM   3728  C CA    . GLY B  1 104 ? 0.914   42.023  -39.444 1.00 46.57 ? 104 GLY D CA    1 
ATOM   3729  C C     . GLY B  1 104 ? 0.946   40.546  -39.754 1.00 53.42 ? 104 GLY D C     1 
ATOM   3730  O O     . GLY B  1 104 ? 0.263   40.105  -40.685 1.00 54.08 ? 104 GLY D O     1 
ATOM   3731  N N     . TRP B  1 105 ? 1.722   39.764  -39.005 1.00 55.50 ? 105 TRP D N     1 
ATOM   3732  C CA    . TRP B  1 105 ? 1.734   38.314  -39.135 1.00 48.89 ? 105 TRP D CA    1 
ATOM   3733  C C     . TRP B  1 105 ? 1.103   37.661  -37.906 1.00 49.30 ? 105 TRP D C     1 
ATOM   3734  O O     . TRP B  1 105 ? 1.184   38.181  -36.784 1.00 44.24 ? 105 TRP D O     1 
ATOM   3735  C CB    . TRP B  1 105 ? 3.153   37.778  -39.314 1.00 48.72 ? 105 TRP D CB    1 
ATOM   3736  C CG    . TRP B  1 105 ? 3.722   37.898  -40.684 1.00 55.58 ? 105 TRP D CG    1 
ATOM   3737  C CD1   . TRP B  1 105 ? 4.447   38.943  -41.174 1.00 57.30 ? 105 TRP D CD1   1 
ATOM   3738  C CD2   . TRP B  1 105 ? 3.657   36.922  -41.740 1.00 53.79 ? 105 TRP D CD2   1 
ATOM   3739  N NE1   . TRP B  1 105 ? 4.820   38.690  -42.473 1.00 59.96 ? 105 TRP D NE1   1 
ATOM   3740  C CE2   . TRP B  1 105 ? 4.347   37.458  -42.844 1.00 53.33 ? 105 TRP D CE2   1 
ATOM   3741  C CE3   . TRP B  1 105 ? 3.072   35.658  -41.862 1.00 47.32 ? 105 TRP D CE3   1 
ATOM   3742  C CZ2   . TRP B  1 105 ? 4.478   36.768  -44.051 1.00 49.34 ? 105 TRP D CZ2   1 
ATOM   3743  C CZ3   . TRP B  1 105 ? 3.198   34.980  -43.063 1.00 49.24 ? 105 TRP D CZ3   1 
ATOM   3744  C CH2   . TRP B  1 105 ? 3.897   35.533  -44.139 1.00 46.24 ? 105 TRP D CH2   1 
ATOM   3745  N N     . SER B  1 106 ? 0.480   36.504  -38.139 1.00 44.29 ? 106 SER D N     1 
ATOM   3746  C CA    . SER B  1 106 ? -0.166  35.710  -37.103 1.00 43.18 ? 106 SER D CA    1 
ATOM   3747  C C     . SER B  1 106 ? 0.086   34.236  -37.399 1.00 37.51 ? 106 SER D C     1 
ATOM   3748  O O     . SER B  1 106 ? 0.477   33.872  -38.505 1.00 38.77 ? 106 SER D O     1 
ATOM   3749  C CB    . SER B  1 106 ? -1.672  36.017  -37.029 1.00 35.34 ? 106 SER D CB    1 
ATOM   3750  O OG    . SER B  1 106 ? -2.437  34.848  -37.206 1.00 31.23 ? 106 SER D OG    1 
ATOM   3751  N N     . LEU B  1 107 ? -0.110  33.387  -36.398 1.00 37.82 ? 107 LEU D N     1 
ATOM   3752  C CA    . LEU B  1 107 ? 0.096   31.949  -36.535 1.00 37.39 ? 107 LEU D CA    1 
ATOM   3753  C C     . LEU B  1 107 ? -1.254  31.241  -36.437 1.00 39.03 ? 107 LEU D C     1 
ATOM   3754  O O     . LEU B  1 107 ? -2.134  31.677  -35.687 1.00 36.91 ? 107 LEU D O     1 
ATOM   3755  C CB    . LEU B  1 107 ? 1.066   31.447  -35.458 1.00 37.42 ? 107 LEU D CB    1 
ATOM   3756  C CG    . LEU B  1 107 ? 1.376   29.964  -35.249 1.00 37.60 ? 107 LEU D CG    1 
ATOM   3757  C CD1   . LEU B  1 107 ? 2.215   29.355  -36.385 1.00 27.44 ? 107 LEU D CD1   1 
ATOM   3758  C CD2   . LEU B  1 107 ? 2.090   29.830  -33.919 1.00 31.43 ? 107 LEU D CD2   1 
ATOM   3759  N N     . PHE B  1 108 ? -1.431  30.167  -37.210 1.00 33.48 ? 108 PHE D N     1 
ATOM   3760  C CA    . PHE B  1 108 ? -2.732  29.505  -37.356 1.00 41.76 ? 108 PHE D CA    1 
ATOM   3761  C C     . PHE B  1 108 ? -2.598  28.032  -37.006 1.00 39.64 ? 108 PHE D C     1 
ATOM   3762  O O     . PHE B  1 108 ? -2.698  27.160  -37.877 1.00 43.04 ? 108 PHE D O     1 
ATOM   3763  C CB    . PHE B  1 108 ? -3.275  29.679  -38.780 1.00 44.12 ? 108 PHE D CB    1 
ATOM   3764  C CG    . PHE B  1 108 ? -4.693  29.157  -38.985 1.00 37.46 ? 108 PHE D CG    1 
ATOM   3765  C CD1   . PHE B  1 108 ? -5.769  29.743  -38.345 1.00 34.23 ? 108 PHE D CD1   1 
ATOM   3766  C CD2   . PHE B  1 108 ? -4.941  28.098  -39.843 1.00 35.96 ? 108 PHE D CD2   1 
ATOM   3767  C CE1   . PHE B  1 108 ? -7.065  29.275  -38.553 1.00 38.25 ? 108 PHE D CE1   1 
ATOM   3768  C CE2   . PHE B  1 108 ? -6.235  27.629  -40.060 1.00 36.46 ? 108 PHE D CE2   1 
ATOM   3769  C CZ    . PHE B  1 108 ? -7.293  28.214  -39.408 1.00 40.99 ? 108 PHE D CZ    1 
ATOM   3770  N N     . PRO B  1 109 ? -2.401  27.714  -35.737 1.00 31.83 ? 109 PRO D N     1 
ATOM   3771  C CA    . PRO B  1 109 ? -2.044  26.341  -35.371 1.00 33.74 ? 109 PRO D CA    1 
ATOM   3772  C C     . PRO B  1 109 ? -3.257  25.433  -35.262 1.00 32.01 ? 109 PRO D C     1 
ATOM   3773  O O     . PRO B  1 109 ? -4.371  25.865  -34.973 1.00 37.83 ? 109 PRO D O     1 
ATOM   3774  C CB    . PRO B  1 109 ? -1.363  26.522  -34.012 1.00 34.41 ? 109 PRO D CB    1 
ATOM   3775  C CG    . PRO B  1 109 ? -2.072  27.695  -33.435 1.00 39.73 ? 109 PRO D CG    1 
ATOM   3776  C CD    . PRO B  1 109 ? -2.385  28.616  -34.580 1.00 32.43 ? 109 PRO D CD    1 
ATOM   3777  N N     . CYS B  1 110 ? -3.027  24.151  -35.517 1.00 35.89 ? 110 CYS D N     1 
ATOM   3778  C CA    . CYS B  1 110 ? -4.100  23.177  -35.392 1.00 33.46 ? 110 CYS D CA    1 
ATOM   3779  C C     . CYS B  1 110 ? -4.378  22.849  -33.940 1.00 36.43 ? 110 CYS D C     1 
ATOM   3780  O O     . CYS B  1 110 ? -5.531  22.614  -33.568 1.00 35.50 ? 110 CYS D O     1 
ATOM   3781  C CB    . CYS B  1 110 ? -3.758  21.896  -36.150 1.00 36.67 ? 110 CYS D CB    1 
ATOM   3782  S SG    . CYS B  1 110 ? -4.793  20.460  -35.749 1.00 33.16 ? 110 CYS D SG    1 
ATOM   3783  N N     . VAL B  1 111 ? -3.334  22.807  -33.117 1.00 33.22 ? 111 VAL D N     1 
ATOM   3784  C CA    . VAL B  1 111 ? -3.432  22.442  -31.711 1.00 32.63 ? 111 VAL D CA    1 
ATOM   3785  C C     . VAL B  1 111 ? -2.699  23.529  -30.942 1.00 33.17 ? 111 VAL D C     1 
ATOM   3786  O O     . VAL B  1 111 ? -1.472  23.643  -31.044 1.00 32.21 ? 111 VAL D O     1 
ATOM   3787  C CB    . VAL B  1 111 ? -2.824  21.059  -31.422 1.00 34.16 ? 111 VAL D CB    1 
ATOM   3788  C CG1   . VAL B  1 111 ? -3.404  20.476  -30.150 1.00 26.29 ? 111 VAL D CG1   1 
ATOM   3789  C CG2   . VAL B  1 111 ? -3.058  20.102  -32.580 1.00 30.78 ? 111 VAL D CG2   1 
ATOM   3790  N N     . SER B  1 112 ? -3.431  24.339  -30.185 1.00 31.71 ? 112 SER D N     1 
ATOM   3791  C CA    . SER B  1 112 ? -2.773  25.519  -29.632 1.00 33.03 ? 112 SER D CA    1 
ATOM   3792  C C     . SER B  1 112 ? -1.858  25.149  -28.460 1.00 33.40 ? 112 SER D C     1 
ATOM   3793  O O     . SER B  1 112 ? -2.139  25.477  -27.303 1.00 33.67 ? 112 SER D O     1 
ATOM   3794  C CB    . SER B  1 112 ? -3.823  26.571  -29.256 1.00 37.05 ? 112 SER D CB    1 
ATOM   3795  O OG    . SER B  1 112 ? -4.496  27.051  -30.428 1.00 38.61 ? 112 SER D OG    1 
ATOM   3796  N N     . THR B  1 113 ? -0.736  24.497  -28.785 1.00 31.70 ? 113 THR D N     1 
ATOM   3797  C CA    . THR B  1 113 ? 0.230   23.913  -27.871 1.00 27.68 ? 113 THR D CA    1 
ATOM   3798  C C     . THR B  1 113 ? 1.125   24.966  -27.223 1.00 35.07 ? 113 THR D C     1 
ATOM   3799  O O     . THR B  1 113 ? 1.213   26.116  -27.657 1.00 39.18 ? 113 THR D O     1 
ATOM   3800  C CB    . THR B  1 113 ? 1.150   22.942  -28.604 1.00 34.02 ? 113 THR D CB    1 
ATOM   3801  O OG1   . THR B  1 113 ? 1.886   23.660  -29.612 1.00 32.91 ? 113 THR D OG1   1 
ATOM   3802  C CG2   . THR B  1 113 ? 0.352   21.849  -29.242 1.00 36.22 ? 113 THR D CG2   1 
ATOM   3803  N N     . ARG B  1 114 ? 1.858   24.522  -26.201 1.00 32.31 ? 114 ARG D N     1 
ATOM   3804  C CA    . ARG B  1 114 ? 2.817   25.395  -25.542 1.00 33.00 ? 114 ARG D CA    1 
ATOM   3805  C C     . ARG B  1 114 ? 3.900   25.858  -26.511 1.00 36.43 ? 114 ARG D C     1 
ATOM   3806  O O     . ARG B  1 114 ? 4.310   27.025  -26.477 1.00 36.13 ? 114 ARG D O     1 
ATOM   3807  C CB    . ARG B  1 114 ? 3.436   24.673  -24.347 1.00 35.26 ? 114 ARG D CB    1 
ATOM   3808  C CG    . ARG B  1 114 ? 4.605   25.429  -23.700 1.00 36.76 ? 114 ARG D CG    1 
ATOM   3809  C CD    . ARG B  1 114 ? 5.132   24.671  -22.505 1.00 30.92 ? 114 ARG D CD    1 
ATOM   3810  N NE    . ARG B  1 114 ? 6.431   25.161  -22.090 1.00 32.97 ? 114 ARG D NE    1 
ATOM   3811  C CZ    . ARG B  1 114 ? 6.585   26.142  -21.217 1.00 36.07 ? 114 ARG D CZ    1 
ATOM   3812  N NH1   . ARG B  1 114 ? 5.538   26.771  -20.705 1.00 38.85 ? 114 ARG D NH1   1 
ATOM   3813  N NH2   . ARG B  1 114 ? 7.816   26.495  -20.840 1.00 30.95 ? 114 ARG D NH2   1 
ATOM   3814  N N     . ALA B  1 115 ? 4.381   24.963  -27.385 1.00 36.56 ? 115 ALA D N     1 
ATOM   3815  C CA    . ALA B  1 115 ? 5.395   25.381  -28.351 1.00 35.67 ? 115 ALA D CA    1 
ATOM   3816  C C     . ALA B  1 115 ? 4.824   26.383  -29.341 1.00 31.47 ? 115 ALA D C     1 
ATOM   3817  O O     . ALA B  1 115 ? 5.527   27.301  -29.777 1.00 32.86 ? 115 ALA D O     1 
ATOM   3818  C CB    . ALA B  1 115 ? 5.982   24.177  -29.094 1.00 32.01 ? 115 ALA D CB    1 
ATOM   3819  N N     . ALA B  1 116 ? 3.545   26.232  -29.689 1.00 34.59 ? 116 ALA D N     1 
ATOM   3820  C CA    . ALA B  1 116 ? 2.911   27.140  -30.640 1.00 34.00 ? 116 ALA D CA    1 
ATOM   3821  C C     . ALA B  1 116 ? 2.798   28.548  -30.075 1.00 35.35 ? 116 ALA D C     1 
ATOM   3822  O O     . ALA B  1 116 ? 2.947   29.534  -30.807 1.00 37.03 ? 116 ALA D O     1 
ATOM   3823  C CB    . ALA B  1 116 ? 1.533   26.611  -31.018 1.00 35.08 ? 116 ALA D CB    1 
ATOM   3824  N N     . ALA B  1 117 ? 2.522   28.667  -28.773 1.00 35.42 ? 117 ALA D N     1 
ATOM   3825  C CA    . ALA B  1 117 ? 2.527   29.985  -28.151 1.00 35.98 ? 117 ALA D CA    1 
ATOM   3826  C C     . ALA B  1 117 ? 3.923   30.588  -28.207 1.00 38.95 ? 117 ALA D C     1 
ATOM   3827  O O     . ALA B  1 117 ? 4.117   31.681  -28.752 1.00 41.92 ? 117 ALA D O     1 
ATOM   3828  C CB    . ALA B  1 117 ? 2.022   29.891  -26.714 1.00 32.60 ? 117 ALA D CB    1 
ATOM   3829  N N     . GLN B  1 118 ? 4.914   29.865  -27.670 1.00 34.05 ? 118 GLN D N     1 
ATOM   3830  C CA    . GLN B  1 118 ? 6.304   30.297  -27.711 1.00 31.94 ? 118 GLN D CA    1 
ATOM   3831  C C     . GLN B  1 118 ? 6.761   30.654  -29.118 1.00 34.33 ? 118 GLN D C     1 
ATOM   3832  O O     . GLN B  1 118 ? 7.569   31.577  -29.296 1.00 31.67 ? 118 GLN D O     1 
ATOM   3833  C CB    . GLN B  1 118 ? 7.185   29.190  -27.135 1.00 34.24 ? 118 GLN D CB    1 
ATOM   3834  C CG    . GLN B  1 118 ? 6.950   28.907  -25.659 1.00 32.80 ? 118 GLN D CG    1 
ATOM   3835  C CD    . GLN B  1 118 ? 7.872   27.831  -25.092 1.00 34.94 ? 118 GLN D CD    1 
ATOM   3836  O OE1   . GLN B  1 118 ? 7.948   26.711  -25.611 1.00 37.21 ? 118 GLN D OE1   1 
ATOM   3837  N NE2   . GLN B  1 118 ? 8.575   28.169  -24.015 1.00 31.53 ? 118 GLN D NE2   1 
ATOM   3838  N N     . LEU B  1 119 ? 6.266   29.930  -30.127 1.00 34.37 ? 119 LEU D N     1 
ATOM   3839  C CA    . LEU B  1 119 ? 6.543   30.286  -31.518 1.00 32.25 ? 119 LEU D CA    1 
ATOM   3840  C C     . LEU B  1 119 ? 5.976   31.668  -31.870 1.00 39.37 ? 119 LEU D C     1 
ATOM   3841  O O     . LEU B  1 119 ? 6.617   32.432  -32.593 1.00 39.96 ? 119 LEU D O     1 
ATOM   3842  C CB    . LEU B  1 119 ? 5.990   29.203  -32.466 1.00 33.15 ? 119 LEU D CB    1 
ATOM   3843  C CG    . LEU B  1 119 ? 6.393   29.162  -33.961 1.00 30.44 ? 119 LEU D CG    1 
ATOM   3844  C CD1   . LEU B  1 119 ? 7.755   28.516  -34.172 1.00 31.95 ? 119 LEU D CD1   1 
ATOM   3845  C CD2   . LEU B  1 119 ? 5.360   28.449  -34.828 1.00 28.59 ? 119 LEU D CD2   1 
ATOM   3846  N N     . THR B  1 120 ? 4.779   32.019  -31.376 1.00 35.87 ? 120 THR D N     1 
ATOM   3847  C CA    . THR B  1 120 ? 4.323   33.402  -31.558 1.00 37.47 ? 120 THR D CA    1 
ATOM   3848  C C     . THR B  1 120 ? 5.187   34.384  -30.771 1.00 40.70 ? 120 THR D C     1 
ATOM   3849  O O     . THR B  1 120 ? 5.405   35.518  -31.212 1.00 44.73 ? 120 THR D O     1 
ATOM   3850  C CB    . THR B  1 120 ? 2.852   33.566  -31.143 1.00 39.76 ? 120 THR D CB    1 
ATOM   3851  O OG1   . THR B  1 120 ? 2.725   33.538  -29.711 1.00 40.78 ? 120 THR D OG1   1 
ATOM   3852  C CG2   . THR B  1 120 ? 2.004   32.477  -31.729 1.00 39.91 ? 120 THR D CG2   1 
ATOM   3853  N N     . ARG B  1 121 ? 5.645   33.979  -29.589 1.00 39.92 ? 121 ARG D N     1 
ATOM   3854  C CA    . ARG B  1 121 ? 6.558   34.801  -28.815 1.00 40.06 ? 121 ARG D CA    1 
ATOM   3855  C C     . ARG B  1 121 ? 7.842   35.032  -29.591 1.00 40.37 ? 121 ARG D C     1 
ATOM   3856  O O     . ARG B  1 121 ? 8.296   36.171  -29.755 1.00 40.69 ? 121 ARG D O     1 
ATOM   3857  C CB    . ARG B  1 121 ? 6.830   34.106  -27.475 1.00 40.79 ? 121 ARG D CB    1 
ATOM   3858  C CG    . ARG B  1 121 ? 8.096   34.537  -26.727 1.00 47.77 ? 121 ARG D CG    1 
ATOM   3859  C CD    . ARG B  1 121 ? 7.955   35.938  -26.202 1.00 46.11 ? 121 ARG D CD    1 
ATOM   3860  N NE    . ARG B  1 121 ? 6.592   36.180  -25.760 1.00 45.24 ? 121 ARG D NE    1 
ATOM   3861  C CZ    . ARG B  1 121 ? 6.173   37.326  -25.245 1.00 57.22 ? 121 ARG D CZ    1 
ATOM   3862  N NH1   . ARG B  1 121 ? 7.001   38.345  -25.062 1.00 54.07 ? 121 ARG D NH1   1 
ATOM   3863  N NH2   . ARG B  1 121 ? 4.888   37.459  -24.919 1.00 54.42 ? 121 ARG D NH2   1 
ATOM   3864  N N     . LYS B  1 122 ? 8.423   33.953  -30.109 1.00 39.18 ? 122 LYS D N     1 
ATOM   3865  C CA    . LYS B  1 122 ? 9.750   34.033  -30.693 1.00 37.30 ? 122 LYS D CA    1 
ATOM   3866  C C     . LYS B  1 122 ? 9.742   34.780  -32.020 1.00 47.00 ? 122 LYS D C     1 
ATOM   3867  O O     . LYS B  1 122 ? 10.736  35.425  -32.366 1.00 54.73 ? 122 LYS D O     1 
ATOM   3868  C CB    . LYS B  1 122 ? 10.318  32.623  -30.874 1.00 41.73 ? 122 LYS D CB    1 
ATOM   3869  C CG    . LYS B  1 122 ? 11.080  32.056  -29.660 1.00 39.37 ? 122 LYS D CG    1 
ATOM   3870  C CD    . LYS B  1 122 ? 12.124  31.002  -30.095 1.00 40.26 ? 122 LYS D CD    1 
ATOM   3871  C CE    . LYS B  1 122 ? 11.819  29.591  -29.544 1.00 42.11 ? 122 LYS D CE    1 
ATOM   3872  N NZ    . LYS B  1 122 ? 12.949  28.612  -29.799 1.00 37.90 ? 122 LYS D NZ    1 
ATOM   3873  N N     . LEU B  1 123 ? 8.643   34.707  -32.779 1.00 48.45 ? 123 LEU D N     1 
ATOM   3874  C CA    . LEU B  1 123 ? 8.558   35.354  -34.083 1.00 39.39 ? 123 LEU D CA    1 
ATOM   3875  C C     . LEU B  1 123 ? 8.152   36.821  -33.999 1.00 47.01 ? 123 LEU D C     1 
ATOM   3876  O O     . LEU B  1 123 ? 8.160   37.499  -35.033 1.00 51.55 ? 123 LEU D O     1 
ATOM   3877  C CB    . LEU B  1 123 ? 7.559   34.613  -34.971 1.00 39.52 ? 123 LEU D CB    1 
ATOM   3878  C CG    . LEU B  1 123 ? 7.812   33.122  -35.239 1.00 42.07 ? 123 LEU D CG    1 
ATOM   3879  C CD1   . LEU B  1 123 ? 6.984   32.622  -36.414 1.00 41.59 ? 123 LEU D CD1   1 
ATOM   3880  C CD2   . LEU B  1 123 ? 9.286   32.821  -35.455 1.00 48.47 ? 123 LEU D CD2   1 
ATOM   3881  N N     . ASN B  1 124 ? 7.805   37.321  -32.806 1.00 44.93 ? 124 ASN D N     1 
ATOM   3882  C CA    . ASN B  1 124 ? 7.244   38.658  -32.592 1.00 43.23 ? 124 ASN D CA    1 
ATOM   3883  C C     . ASN B  1 124 ? 5.899   38.813  -33.274 1.00 46.35 ? 124 ASN D C     1 
ATOM   3884  O O     . ASN B  1 124 ? 5.410   39.934  -33.469 1.00 47.06 ? 124 ASN D O     1 
ATOM   3885  C CB    . ASN B  1 124 ? 8.201   39.760  -33.049 1.00 43.22 ? 124 ASN D CB    1 
ATOM   3886  C CG    . ASN B  1 124 ? 7.844   41.115  -32.462 1.00 55.65 ? 124 ASN D CG    1 
ATOM   3887  O OD1   . ASN B  1 124 ? 7.387   41.207  -31.306 1.00 48.53 ? 124 ASN D OD1   1 
ATOM   3888  N ND2   . ASN B  1 124 ? 8.048   42.181  -33.255 1.00 46.68 ? 124 ASN D ND2   1 
ATOM   3889  N N     . VAL B  1 125 ? 5.305   37.674  -33.612 1.00 47.32 ? 125 VAL D N     1 
ATOM   3890  C CA    . VAL B  1 125 ? 4.075   37.549  -34.376 1.00 41.93 ? 125 VAL D CA    1 
ATOM   3891  C C     . VAL B  1 125 ? 2.884   37.883  -33.474 1.00 48.43 ? 125 VAL D C     1 
ATOM   3892  O O     . VAL B  1 125 ? 3.068   38.155  -32.277 1.00 49.09 ? 125 VAL D O     1 
ATOM   3893  C CB    . VAL B  1 125 ? 4.041   36.128  -34.968 1.00 43.21 ? 125 VAL D CB    1 
ATOM   3894  C CG1   . VAL B  1 125 ? 2.941   35.260  -34.386 1.00 40.55 ? 125 VAL D CG1   1 
ATOM   3895  C CG2   . VAL B  1 125 ? 4.008   36.190  -36.473 1.00 45.38 ? 125 VAL D CG2   1 
ATOM   3896  N N     . ALA B  1 126 ? 1.669   37.934  -34.035 1.00 42.92 ? 126 ALA D N     1 
ATOM   3897  C CA    . ALA B  1 126 ? 0.491   38.132  -33.195 1.00 46.71 ? 126 ALA D CA    1 
ATOM   3898  C C     . ALA B  1 126 ? 0.540   37.184  -31.999 1.00 47.28 ? 126 ALA D C     1 
ATOM   3899  O O     . ALA B  1 126 ? 0.757   35.977  -32.156 1.00 45.13 ? 126 ALA D O     1 
ATOM   3900  C CB    . ALA B  1 126 ? -0.797  37.915  -33.997 1.00 34.95 ? 126 ALA D CB    1 
ATOM   3901  N N     . ALA B  1 127 ? 0.413   37.741  -30.799 1.00 46.31 ? 127 ALA D N     1 
ATOM   3902  C CA    . ALA B  1 127 ? 0.292   36.898  -29.623 1.00 41.40 ? 127 ALA D CA    1 
ATOM   3903  C C     . ALA B  1 127 ? -0.861  35.917  -29.806 1.00 42.28 ? 127 ALA D C     1 
ATOM   3904  O O     . ALA B  1 127 ? -1.962  36.300  -30.221 1.00 45.89 ? 127 ALA D O     1 
ATOM   3905  C CB    . ALA B  1 127 ? 0.059   37.761  -28.390 1.00 33.98 ? 127 ALA D CB    1 
ATOM   3906  N N     . LEU B  1 128 ? -0.586  34.641  -29.555 1.00 35.52 ? 128 LEU D N     1 
ATOM   3907  C CA    . LEU B  1 128 ? -1.656  33.660  -29.482 1.00 36.83 ? 128 LEU D CA    1 
ATOM   3908  C C     . LEU B  1 128 ? -2.700  34.089  -28.454 1.00 35.33 ? 128 LEU D C     1 
ATOM   3909  O O     . LEU B  1 128 ? -2.369  34.580  -27.371 1.00 32.08 ? 128 LEU D O     1 
ATOM   3910  C CB    . LEU B  1 128 ? -1.074  32.304  -29.103 1.00 38.00 ? 128 LEU D CB    1 
ATOM   3911  C CG    . LEU B  1 128 ? -1.731  31.024  -29.566 1.00 34.44 ? 128 LEU D CG    1 
ATOM   3912  C CD1   . LEU B  1 128 ? -1.559  30.881  -31.063 1.00 36.24 ? 128 LEU D CD1   1 
ATOM   3913  C CD2   . LEU B  1 128 ? -1.021  29.914  -28.848 1.00 36.12 ? 128 LEU D CD2   1 
ATOM   3914  N N     . ASP B  1 129 ? -3.973  33.941  -28.811 1.00 35.96 ? 129 ASP D N     1 
ATOM   3915  C CA    . ASP B  1 129 ? -5.029  34.168  -27.835 1.00 36.02 ? 129 ASP D CA    1 
ATOM   3916  C C     . ASP B  1 129 ? -5.033  33.031  -26.826 1.00 34.45 ? 129 ASP D C     1 
ATOM   3917  O O     . ASP B  1 129 ? -4.750  31.884  -27.169 1.00 38.94 ? 129 ASP D O     1 
ATOM   3918  C CB    . ASP B  1 129 ? -6.391  34.274  -28.525 1.00 37.53 ? 129 ASP D CB    1 
ATOM   3919  C CG    . ASP B  1 129 ? -7.414  35.045  -27.693 1.00 37.69 ? 129 ASP D CG    1 
ATOM   3920  O OD1   . ASP B  1 129 ? -7.108  35.376  -26.522 1.00 32.98 ? 129 ASP D OD1   1 
ATOM   3921  O OD2   . ASP B  1 129 ? -8.527  35.308  -28.209 1.00 39.11 ? 129 ASP D OD2   1 
ATOM   3922  N N     . GLY B  1 130 ? -5.359  33.346  -25.577 1.00 36.82 ? 130 GLY D N     1 
ATOM   3923  C CA    . GLY B  1 130 ? -5.217  32.355  -24.527 1.00 34.87 ? 130 GLY D CA    1 
ATOM   3924  C C     . GLY B  1 130 ? -3.788  31.923  -24.293 1.00 30.25 ? 130 GLY D C     1 
ATOM   3925  O O     . GLY B  1 130 ? -3.549  30.787  -23.872 1.00 29.19 ? 130 GLY D O     1 
ATOM   3926  N N     . TYR B  1 131 ? -2.827  32.813  -24.544 1.00 26.90 ? 131 TYR D N     1 
ATOM   3927  C CA    . TYR B  1 131 ? -1.422  32.437  -24.488 1.00 30.77 ? 131 TYR D CA    1 
ATOM   3928  C C     . TYR B  1 131 ? -1.088  31.710  -23.185 1.00 35.25 ? 131 TYR D C     1 
ATOM   3929  O O     . TYR B  1 131 ? -0.429  30.661  -23.202 1.00 34.31 ? 131 TYR D O     1 
ATOM   3930  C CB    . TYR B  1 131 ? -0.571  33.695  -24.682 1.00 30.06 ? 131 TYR D CB    1 
ATOM   3931  C CG    . TYR B  1 131 ? 0.924   33.546  -24.435 1.00 34.92 ? 131 TYR D CG    1 
ATOM   3932  C CD1   . TYR B  1 131 ? 1.795   33.188  -25.460 1.00 38.60 ? 131 TYR D CD1   1 
ATOM   3933  C CD2   . TYR B  1 131 ? 1.475   33.821  -23.181 1.00 35.75 ? 131 TYR D CD2   1 
ATOM   3934  C CE1   . TYR B  1 131 ? 3.169   33.070  -25.226 1.00 34.12 ? 131 TYR D CE1   1 
ATOM   3935  C CE2   . TYR B  1 131 ? 2.828   33.710  -22.946 1.00 32.86 ? 131 TYR D CE2   1 
ATOM   3936  C CZ    . TYR B  1 131 ? 3.669   33.333  -23.964 1.00 37.23 ? 131 TYR D CZ    1 
ATOM   3937  O OH    . TYR B  1 131 ? 5.015   33.228  -23.710 1.00 47.77 ? 131 TYR D OH    1 
ATOM   3938  N N     . GLU B  1 132 ? -1.585  32.217  -22.051 1.00 33.84 ? 132 GLU D N     1 
ATOM   3939  C CA    . GLU B  1 132 ? -1.189  31.667  -20.757 1.00 31.30 ? 132 GLU D CA    1 
ATOM   3940  C C     . GLU B  1 132 ? -1.768  30.280  -20.538 1.00 29.47 ? 132 GLU D C     1 
ATOM   3941  O O     . GLU B  1 132 ? -1.074  29.380  -20.060 1.00 33.45 ? 132 GLU D O     1 
ATOM   3942  C CB    . GLU B  1 132 ? -1.609  32.600  -19.624 1.00 26.95 ? 132 GLU D CB    1 
ATOM   3943  C CG    . GLU B  1 132 ? -1.397  34.097  -19.886 1.00 32.70 ? 132 GLU D CG    1 
ATOM   3944  C CD    . GLU B  1 132 ? 0.075   34.504  -20.065 1.00 42.93 ? 132 GLU D CD    1 
ATOM   3945  O OE1   . GLU B  1 132 ? 0.977   33.652  -19.905 1.00 43.30 ? 132 GLU D OE1   1 
ATOM   3946  O OE2   . GLU B  1 132 ? 0.333   35.697  -20.365 1.00 46.36 ? 132 GLU D OE2   1 
ATOM   3947  N N     . PHE B  1 133 ? -3.043  30.085  -20.850 1.00 26.69 ? 133 PHE D N     1 
ATOM   3948  C CA    . PHE B  1 133 ? -3.578  28.732  -20.784 1.00 32.68 ? 133 PHE D CA    1 
ATOM   3949  C C     . PHE B  1 133 ? -2.657  27.766  -21.517 1.00 34.00 ? 133 PHE D C     1 
ATOM   3950  O O     . PHE B  1 133 ? -2.277  26.717  -20.983 1.00 32.58 ? 133 PHE D O     1 
ATOM   3951  C CB    . PHE B  1 133 ? -4.981  28.698  -21.386 1.00 34.57 ? 133 PHE D CB    1 
ATOM   3952  C CG    . PHE B  1 133 ? -5.789  27.469  -21.020 1.00 34.77 ? 133 PHE D CG    1 
ATOM   3953  C CD1   . PHE B  1 133 ? -6.038  27.149  -19.693 1.00 30.29 ? 133 PHE D CD1   1 
ATOM   3954  C CD2   . PHE B  1 133 ? -6.346  26.668  -22.011 1.00 31.75 ? 133 PHE D CD2   1 
ATOM   3955  C CE1   . PHE B  1 133 ? -6.791  26.046  -19.364 1.00 26.91 ? 133 PHE D CE1   1 
ATOM   3956  C CE2   . PHE B  1 133 ? -7.110  25.562  -21.681 1.00 33.52 ? 133 PHE D CE2   1 
ATOM   3957  C CZ    . PHE B  1 133 ? -7.329  25.252  -20.359 1.00 34.64 ? 133 PHE D CZ    1 
ATOM   3958  N N     . ALA B  1 134 ? -2.250  28.138  -22.732 1.00 32.59 ? 134 ALA D N     1 
ATOM   3959  C CA    . ALA B  1 134 ? -1.426  27.258  -23.546 1.00 35.11 ? 134 ALA D CA    1 
ATOM   3960  C C     . ALA B  1 134 ? -0.052  27.039  -22.916 1.00 34.88 ? 134 ALA D C     1 
ATOM   3961  O O     . ALA B  1 134 ? 0.478   25.918  -22.929 1.00 31.65 ? 134 ALA D O     1 
ATOM   3962  C CB    . ALA B  1 134 ? -1.289  27.848  -24.946 1.00 31.58 ? 134 ALA D CB    1 
ATOM   3963  N N     . MET B  1 135 ? 0.542   28.099  -22.364 1.00 32.35 ? 135 MET D N     1 
ATOM   3964  C CA    . MET B  1 135 ? 1.875   27.976  -21.780 1.00 34.21 ? 135 MET D CA    1 
ATOM   3965  C C     . MET B  1 135 ? 1.878   27.006  -20.609 1.00 33.85 ? 135 MET D C     1 
ATOM   3966  O O     . MET B  1 135 ? 2.917   26.418  -20.292 1.00 37.96 ? 135 MET D O     1 
ATOM   3967  C CB    . MET B  1 135 ? 2.389   29.350  -21.336 1.00 29.48 ? 135 MET D CB    1 
ATOM   3968  C CG    . MET B  1 135 ? 2.712   30.283  -22.500 1.00 40.86 ? 135 MET D CG    1 
ATOM   3969  S SD    . MET B  1 135 ? 4.273   29.893  -23.358 1.00 34.74 ? 135 MET D SD    1 
ATOM   3970  C CE    . MET B  1 135 ? 5.396   29.941  -21.948 1.00 39.56 ? 135 MET D CE    1 
ATOM   3971  N N     . GLN B  1 136 ? 0.735   26.830  -19.949 1.00 33.06 ? 136 GLN D N     1 
ATOM   3972  C CA    . GLN B  1 136 ? 0.617   25.841  -18.895 1.00 33.06 ? 136 GLN D CA    1 
ATOM   3973  C C     . GLN B  1 136 ? 0.114   24.511  -19.426 1.00 33.80 ? 136 GLN D C     1 
ATOM   3974  O O     . GLN B  1 136 ? -0.356  23.681  -18.643 1.00 35.80 ? 136 GLN D O     1 
ATOM   3975  C CB    . GLN B  1 136 ? -0.286  26.366  -17.784 1.00 30.66 ? 136 GLN D CB    1 
ATOM   3976  C CG    . GLN B  1 136 ? 0.287   27.587  -17.105 1.00 27.17 ? 136 GLN D CG    1 
ATOM   3977  C CD    . GLN B  1 136 ? 1.596   27.276  -16.455 1.00 25.30 ? 136 GLN D CD    1 
ATOM   3978  O OE1   . GLN B  1 136 ? 1.738   26.245  -15.818 1.00 29.25 ? 136 GLN D OE1   1 
ATOM   3979  N NE2   . GLN B  1 136 ? 2.570   28.156  -16.614 1.00 27.45 ? 136 GLN D NE2   1 
ATOM   3980  N N     . ASN B  1 137 ? 0.243   24.284  -20.737 1.00 31.25 ? 137 ASN D N     1 
ATOM   3981  C CA    . ASN B  1 137 ? -0.209  23.060  -21.390 1.00 30.37 ? 137 ASN D CA    1 
ATOM   3982  C C     . ASN B  1 137 ? -1.681  22.813  -21.112 1.00 30.64 ? 137 ASN D C     1 
ATOM   3983  O O     . ASN B  1 137 ? -2.138  21.668  -21.020 1.00 28.21 ? 137 ASN D O     1 
ATOM   3984  C CB    . ASN B  1 137 ? 0.636   21.863  -20.976 1.00 28.55 ? 137 ASN D CB    1 
ATOM   3985  C CG    . ASN B  1 137 ? 2.092   22.016  -21.391 1.00 37.57 ? 137 ASN D CG    1 
ATOM   3986  O OD1   . ASN B  1 137 ? 2.410   22.042  -22.588 1.00 40.23 ? 137 ASN D OD1   1 
ATOM   3987  N ND2   . ASN B  1 137 ? 2.988   22.124  -20.403 1.00 34.80 ? 137 ASN D ND2   1 
ATOM   3988  N N     . GLY B  1 138 ? -2.423  23.913  -20.995 1.00 31.03 ? 138 GLY D N     1 
ATOM   3989  C CA    . GLY B  1 138 ? -3.813  23.822  -20.610 1.00 32.27 ? 138 GLY D CA    1 
ATOM   3990  C C     . GLY B  1 138 ? -4.650  23.070  -21.617 1.00 32.16 ? 138 GLY D C     1 
ATOM   3991  O O     . GLY B  1 138 ? -5.625  22.407  -21.255 1.00 32.14 ? 138 GLY D O     1 
ATOM   3992  N N     . ILE B  1 139 ? -4.294  23.158  -22.900 1.00 32.77 ? 139 ILE D N     1 
ATOM   3993  C CA    . ILE B  1 139 ? -5.169  22.553  -23.895 1.00 32.56 ? 139 ILE D CA    1 
ATOM   3994  C C     . ILE B  1 139 ? -5.039  21.041  -23.890 1.00 32.27 ? 139 ILE D C     1 
ATOM   3995  O O     . ILE B  1 139 ? -5.823  20.360  -24.563 1.00 34.54 ? 139 ILE D O     1 
ATOM   3996  C CB    . ILE B  1 139 ? -4.926  23.235  -25.258 1.00 30.11 ? 139 ILE D CB    1 
ATOM   3997  C CG1   . ILE B  1 139 ? -4.168  22.329  -26.202 1.00 28.35 ? 139 ILE D CG1   1 
ATOM   3998  C CG2   . ILE B  1 139 ? -4.212  24.577  -25.061 1.00 31.51 ? 139 ILE D CG2   1 
ATOM   3999  C CD1   . ILE B  1 139 ? -5.025  21.728  -27.216 1.00 29.94 ? 139 ILE D CD1   1 
ATOM   4000  N N     . ASP B  1 140 ? -4.138  20.491  -23.065 1.00 37.54 ? 140 ASP D N     1 
ATOM   4001  C CA    . ASP B  1 140 ? -3.988  19.049  -22.917 1.00 32.08 ? 140 ASP D CA    1 
ATOM   4002  C C     . ASP B  1 140 ? -4.817  18.437  -21.786 1.00 33.91 ? 140 ASP D C     1 
ATOM   4003  O O     . ASP B  1 140 ? -5.025  17.221  -21.796 1.00 36.08 ? 140 ASP D O     1 
ATOM   4004  C CB    . ASP B  1 140 ? -2.528  18.681  -22.691 1.00 38.05 ? 140 ASP D CB    1 
ATOM   4005  C CG    . ASP B  1 140 ? -2.319  17.197  -22.661 1.00 39.33 ? 140 ASP D CG    1 
ATOM   4006  O OD1   . ASP B  1 140 ? -2.865  16.529  -23.561 1.00 45.53 ? 140 ASP D OD1   1 
ATOM   4007  O OD2   . ASP B  1 140 ? -1.653  16.695  -21.728 1.00 34.93 ? 140 ASP D OD2   1 
ATOM   4008  N N     . LEU B  1 141 ? -5.311  19.213  -20.810 1.00 34.97 ? 141 LEU D N     1 
ATOM   4009  C CA    . LEU B  1 141 ? -6.309  18.643  -19.900 1.00 35.68 ? 141 LEU D CA    1 
ATOM   4010  C C     . LEU B  1 141 ? -7.564  18.334  -20.665 1.00 38.80 ? 141 LEU D C     1 
ATOM   4011  O O     . LEU B  1 141 ? -8.042  17.197  -20.681 1.00 44.42 ? 141 LEU D O     1 
ATOM   4012  C CB    . LEU B  1 141 ? -6.692  19.568  -18.752 1.00 33.81 ? 141 LEU D CB    1 
ATOM   4013  C CG    . LEU B  1 141 ? -5.706  20.192  -17.812 1.00 45.97 ? 141 LEU D CG    1 
ATOM   4014  C CD1   . LEU B  1 141 ? -5.167  21.354  -18.567 1.00 42.29 ? 141 LEU D CD1   1 
ATOM   4015  C CD2   . LEU B  1 141 ? -6.492  20.645  -16.585 1.00 36.12 ? 141 LEU D CD2   1 
ATOM   4016  N N     . LEU B  1 142 ? -8.138  19.364  -21.266 1.00 35.82 ? 142 LEU D N     1 
ATOM   4017  C CA    . LEU B  1 142 ? -9.051  19.173  -22.367 1.00 33.57 ? 142 LEU D CA    1 
ATOM   4018  C C     . LEU B  1 142 ? -8.321  18.308  -23.378 1.00 37.22 ? 142 LEU D C     1 
ATOM   4019  O O     . LEU B  1 142 ? -7.094  18.234  -23.375 1.00 42.74 ? 142 LEU D O     1 
ATOM   4020  C CB    . LEU B  1 142 ? -9.421  20.536  -22.952 1.00 37.63 ? 142 LEU D CB    1 
ATOM   4021  C CG    . LEU B  1 142 ? -9.354  21.695  -21.923 1.00 37.00 ? 142 LEU D CG    1 
ATOM   4022  C CD1   . LEU B  1 142 ? -9.781  23.033  -22.513 1.00 28.01 ? 142 LEU D CD1   1 
ATOM   4023  C CD2   . LEU B  1 142 ? -10.147 21.462  -20.619 1.00 32.06 ? 142 LEU D CD2   1 
ATOM   4024  N N     . ASN B  1 143 ? -9.062  17.635  -24.234 1.00 35.23 ? 143 ASN D N     1 
ATOM   4025  C CA    . ASN B  1 143 ? -8.490  16.618  -25.112 1.00 35.06 ? 143 ASN D CA    1 
ATOM   4026  C C     . ASN B  1 143 ? -8.039  15.408  -24.333 1.00 32.24 ? 143 ASN D C     1 
ATOM   4027  O O     . ASN B  1 143 ? -7.177  14.652  -24.798 1.00 36.80 ? 143 ASN D O     1 
ATOM   4028  C CB    . ASN B  1 143 ? -7.307  17.130  -25.936 1.00 32.25 ? 143 ASN D CB    1 
ATOM   4029  C CG    . ASN B  1 143 ? -7.694  18.242  -26.835 1.00 33.30 ? 143 ASN D CG    1 
ATOM   4030  O OD1   . ASN B  1 143 ? -8.877  18.506  -27.028 1.00 33.47 ? 143 ASN D OD1   1 
ATOM   4031  N ND2   . ASN B  1 143 ? -6.692  18.970  -27.346 1.00 27.01 ? 143 ASN D ND2   1 
ATOM   4032  N N     . MET B  1 144 ? -8.563  15.253  -23.129 1.00 33.51 ? 144 MET D N     1 
ATOM   4033  C CA    . MET B  1 144 ? -8.576  13.972  -22.450 1.00 31.98 ? 144 MET D CA    1 
ATOM   4034  C C     . MET B  1 144 ? -10.013 13.522  -22.352 1.00 28.67 ? 144 MET D C     1 
ATOM   4035  O O     . MET B  1 144 ? -10.899 14.322  -22.048 1.00 27.14 ? 144 MET D O     1 
ATOM   4036  C CB    . MET B  1 144 ? -7.996  14.039  -21.048 1.00 30.72 ? 144 MET D CB    1 
ATOM   4037  C CG    . MET B  1 144 ? -6.626  14.616  -20.937 1.00 32.41 ? 144 MET D CG    1 
ATOM   4038  S SD    . MET B  1 144 ? -6.241  14.562  -19.204 1.00 33.13 ? 144 MET D SD    1 
ATOM   4039  C CE    . MET B  1 144 ? -4.666  15.414  -19.107 1.00 33.80 ? 144 MET D CE    1 
ATOM   4040  N N     . LYS B  1 145 ? -10.251 12.243  -22.590 1.00 27.11 ? 145 LYS D N     1 
ATOM   4041  C CA    . LYS B  1 145 ? -11.601 11.768  -22.361 1.00 29.24 ? 145 LYS D CA    1 
ATOM   4042  C C     . LYS B  1 145 ? -11.945 11.748  -20.866 1.00 33.72 ? 145 LYS D C     1 
ATOM   4043  O O     . LYS B  1 145 ? -13.106 11.982  -20.495 1.00 33.18 ? 145 LYS D O     1 
ATOM   4044  C CB    . LYS B  1 145 ? -11.778 10.416  -23.039 1.00 30.39 ? 145 LYS D CB    1 
ATOM   4045  C CG    . LYS B  1 145 ? -12.041 10.590  -24.551 1.00 36.22 ? 145 LYS D CG    1 
ATOM   4046  C CD    . LYS B  1 145 ? -11.650 9.372   -25.367 1.00 38.45 ? 145 LYS D CD    1 
ATOM   4047  C CE    . LYS B  1 145 ? -11.420 9.707   -26.846 1.00 34.03 ? 145 LYS D CE    1 
ATOM   4048  N NZ    . LYS B  1 145 ? -10.163 10.470  -27.109 1.00 32.60 ? 145 LYS D NZ    1 
ATOM   4049  N N     . SER B  1 146 ? -10.955 11.537  -19.992 1.00 31.67 ? 146 SER D N     1 
ATOM   4050  C CA    . SER B  1 146 ? -11.219 11.601  -18.555 1.00 26.55 ? 146 SER D CA    1 
ATOM   4051  C C     . SER B  1 146 ? -11.719 12.984  -18.149 1.00 31.59 ? 146 SER D C     1 
ATOM   4052  O O     . SER B  1 146 ? -12.777 13.111  -17.517 1.00 30.18 ? 146 SER D O     1 
ATOM   4053  C CB    . SER B  1 146 ? -9.965  11.247  -17.775 1.00 28.09 ? 146 SER D CB    1 
ATOM   4054  O OG    . SER B  1 146 ? -8.881  12.030  -18.239 1.00 36.10 ? 146 SER D OG    1 
ATOM   4055  N N     . THR B  1 147 ? -10.972 14.036  -18.514 1.00 27.41 ? 147 THR D N     1 
ATOM   4056  C CA    . THR B  1 147 ? -11.392 15.402  -18.216 1.00 25.39 ? 147 THR D CA    1 
ATOM   4057  C C     . THR B  1 147 ? -12.816 15.675  -18.689 1.00 29.57 ? 147 THR D C     1 
ATOM   4058  O O     . THR B  1 147 ? -13.595 16.363  -18.008 1.00 29.31 ? 147 THR D O     1 
ATOM   4059  C CB    . THR B  1 147 ? -10.430 16.396  -18.859 1.00 26.56 ? 147 THR D CB    1 
ATOM   4060  O OG1   . THR B  1 147 ? -9.116  16.188  -18.334 1.00 30.79 ? 147 THR D OG1   1 
ATOM   4061  C CG2   . THR B  1 147 ? -10.856 17.832  -18.568 1.00 27.88 ? 147 THR D CG2   1 
ATOM   4062  N N     . PHE B  1 148 ? -13.182 15.138  -19.851 1.00 28.46 ? 148 PHE D N     1 
ATOM   4063  C CA    . PHE B  1 148 ? -14.494 15.449  -20.390 1.00 25.66 ? 148 PHE D CA    1 
ATOM   4064  C C     . PHE B  1 148 ? -15.580 14.976  -19.443 1.00 25.43 ? 148 PHE D C     1 
ATOM   4065  O O     . PHE B  1 148 ? -16.361 15.784  -18.934 1.00 27.95 ? 148 PHE D O     1 
ATOM   4066  C CB    . PHE B  1 148 ? -14.680 14.849  -21.779 1.00 25.94 ? 148 PHE D CB    1 
ATOM   4067  C CG    . PHE B  1 148 ? -16.015 15.157  -22.354 1.00 26.89 ? 148 PHE D CG    1 
ATOM   4068  C CD1   . PHE B  1 148 ? -16.298 16.425  -22.825 1.00 26.84 ? 148 PHE D CD1   1 
ATOM   4069  C CD2   . PHE B  1 148 ? -17.025 14.206  -22.335 1.00 28.01 ? 148 PHE D CD2   1 
ATOM   4070  C CE1   . PHE B  1 148 ? -17.543 16.716  -23.301 1.00 32.26 ? 148 PHE D CE1   1 
ATOM   4071  C CE2   . PHE B  1 148 ? -18.281 14.484  -22.816 1.00 22.50 ? 148 PHE D CE2   1 
ATOM   4072  C CZ    . PHE B  1 148 ? -18.547 15.737  -23.293 1.00 31.27 ? 148 PHE D CZ    1 
ATOM   4073  N N     . ARG B  1 149 ? -15.611 13.670  -19.157 1.00 26.69 ? 149 ARG D N     1 
ATOM   4074  C CA    . ARG B  1 149 ? -16.658 13.121  -18.293 1.00 27.08 ? 149 ARG D CA    1 
ATOM   4075  C C     . ARG B  1 149 ? -16.695 13.849  -16.956 1.00 30.07 ? 149 ARG D C     1 
ATOM   4076  O O     . ARG B  1 149 ? -17.764 14.248  -16.477 1.00 33.27 ? 149 ARG D O     1 
ATOM   4077  C CB    . ARG B  1 149 ? -16.447 11.623  -18.071 1.00 29.02 ? 149 ARG D CB    1 
ATOM   4078  C CG    . ARG B  1 149 ? -16.050 10.817  -19.300 1.00 31.63 ? 149 ARG D CG    1 
ATOM   4079  C CD    . ARG B  1 149 ? -16.374 9.347   -19.095 1.00 29.52 ? 149 ARG D CD    1 
ATOM   4080  N NE    . ARG B  1 149 ? -17.538 9.189   -18.229 1.00 32.33 ? 149 ARG D NE    1 
ATOM   4081  C CZ    . ARG B  1 149 ? -18.771 8.937   -18.649 1.00 35.45 ? 149 ARG D CZ    1 
ATOM   4082  N NH1   . ARG B  1 149 ? -19.049 8.797   -19.933 1.00 36.99 ? 149 ARG D NH1   1 
ATOM   4083  N NH2   . ARG B  1 149 ? -19.748 8.823   -17.757 1.00 33.78 ? 149 ARG D NH2   1 
ATOM   4084  N N     . ARG B  1 150 ? -15.528 14.034  -16.344 1.00 26.26 ? 150 ARG D N     1 
ATOM   4085  C CA    . ARG B  1 150 ? -15.459 14.790  -15.105 1.00 27.92 ? 150 ARG D CA    1 
ATOM   4086  C C     . ARG B  1 150 ? -16.182 16.112  -15.263 1.00 29.13 ? 150 ARG D C     1 
ATOM   4087  O O     . ARG B  1 150 ? -17.080 16.440  -14.479 1.00 31.77 ? 150 ARG D O     1 
ATOM   4088  C CB    . ARG B  1 150 ? -13.997 15.006  -14.695 1.00 27.76 ? 150 ARG D CB    1 
ATOM   4089  C CG    . ARG B  1 150 ? -13.245 13.698  -14.387 1.00 31.52 ? 150 ARG D CG    1 
ATOM   4090  C CD    . ARG B  1 150 ? -11.724 13.883  -14.108 1.00 31.21 ? 150 ARG D CD    1 
ATOM   4091  N NE    . ARG B  1 150 ? -11.217 12.863  -13.189 1.00 29.12 ? 150 ARG D NE    1 
ATOM   4092  C CZ    . ARG B  1 150 ? -9.936  12.661  -12.907 1.00 32.42 ? 150 ARG D CZ    1 
ATOM   4093  N NH1   . ARG B  1 150 ? -8.978  13.329  -13.528 1.00 33.06 ? 150 ARG D NH1   1 
ATOM   4094  N NH2   . ARG B  1 150 ? -9.608  11.784  -11.957 1.00 35.94 ? 150 ARG D NH2   1 
ATOM   4095  N N     . LEU B  1 151 ? -15.847 16.854  -16.314 1.00 28.91 ? 151 LEU D N     1 
ATOM   4096  C CA    . LEU B  1 151 ? -16.432 18.173  -16.481 1.00 29.80 ? 151 LEU D CA    1 
ATOM   4097  C C     . LEU B  1 151 ? -17.923 18.089  -16.737 1.00 32.63 ? 151 LEU D C     1 
ATOM   4098  O O     . LEU B  1 151 ? -18.682 18.988  -16.342 1.00 29.04 ? 151 LEU D O     1 
ATOM   4099  C CB    . LEU B  1 151 ? -15.758 18.891  -17.630 1.00 27.63 ? 151 LEU D CB    1 
ATOM   4100  C CG    . LEU B  1 151 ? -14.370 19.380  -17.305 1.00 28.48 ? 151 LEU D CG    1 
ATOM   4101  C CD1   . LEU B  1 151 ? -13.919 20.148  -18.516 1.00 24.76 ? 151 LEU D CD1   1 
ATOM   4102  C CD2   . LEU B  1 151 ? -14.393 20.256  -16.066 1.00 22.38 ? 151 LEU D CD2   1 
ATOM   4103  N N     . ALA B  1 152 ? -18.355 17.027  -17.396 1.00 28.96 ? 152 ALA D N     1 
ATOM   4104  C CA    . ALA B  1 152 ? -19.743 16.951  -17.801 1.00 32.58 ? 152 ALA D CA    1 
ATOM   4105  C C     . ALA B  1 152 ? -20.621 16.347  -16.723 1.00 29.61 ? 152 ALA D C     1 
ATOM   4106  O O     . ALA B  1 152 ? -21.818 16.637  -16.668 1.00 32.16 ? 152 ALA D O     1 
ATOM   4107  C CB    . ALA B  1 152 ? -19.860 16.149  -19.097 1.00 32.31 ? 152 ALA D CB    1 
ATOM   4108  N N     . ALA B  1 153 ? -20.065 15.496  -15.874 1.00 29.86 ? 153 ALA D N     1 
ATOM   4109  C CA    . ALA B  1 153 ? -20.803 15.099  -14.690 1.00 32.90 ? 153 ALA D CA    1 
ATOM   4110  C C     . ALA B  1 153 ? -21.109 16.322  -13.828 1.00 33.45 ? 153 ALA D C     1 
ATOM   4111  O O     . ALA B  1 153 ? -22.270 16.634  -13.548 1.00 37.50 ? 153 ALA D O     1 
ATOM   4112  C CB    . ALA B  1 153 ? -20.002 14.055  -13.913 1.00 36.42 ? 153 ALA D CB    1 
ATOM   4113  N N     . GLY B  1 154 ? -20.068 17.047  -13.424 1.00 31.77 ? 154 GLY D N     1 
ATOM   4114  C CA    . GLY B  1 154 ? -20.270 18.156  -12.519 1.00 31.78 ? 154 GLY D CA    1 
ATOM   4115  C C     . GLY B  1 154 ? -21.227 19.185  -13.074 1.00 32.70 ? 154 GLY D C     1 
ATOM   4116  O O     . GLY B  1 154 ? -22.049 19.743  -12.343 1.00 36.77 ? 154 GLY D O     1 
ATOM   4117  N N     . LEU B  1 155 ? -21.154 19.429  -14.375 1.00 27.55 ? 155 LEU D N     1 
ATOM   4118  C CA    . LEU B  1 155 ? -21.990 20.463  -14.964 1.00 28.25 ? 155 LEU D CA    1 
ATOM   4119  C C     . LEU B  1 155 ? -23.390 19.967  -15.238 1.00 28.60 ? 155 LEU D C     1 
ATOM   4120  O O     . LEU B  1 155 ? -24.333 20.764  -15.249 1.00 30.07 ? 155 LEU D O     1 
ATOM   4121  C CB    . LEU B  1 155 ? -21.378 20.978  -16.257 1.00 26.33 ? 155 LEU D CB    1 
ATOM   4122  C CG    . LEU B  1 155 ? -22.198 21.982  -17.070 1.00 32.91 ? 155 LEU D CG    1 
ATOM   4123  C CD1   . LEU B  1 155 ? -22.703 23.131  -16.218 1.00 33.67 ? 155 LEU D CD1   1 
ATOM   4124  C CD2   . LEU B  1 155 ? -21.389 22.521  -18.276 1.00 39.37 ? 155 LEU D CD2   1 
ATOM   4125  N N     . GLY B  1 156 ? -23.550 18.666  -15.434 1.00 28.82 ? 156 GLY D N     1 
ATOM   4126  C CA    . GLY B  1 156 ? -24.825 18.116  -15.817 1.00 32.33 ? 156 GLY D CA    1 
ATOM   4127  C C     . GLY B  1 156 ? -24.953 17.815  -17.291 1.00 35.80 ? 156 GLY D C     1 
ATOM   4128  O O     . GLY B  1 156 ? -26.020 17.345  -17.722 1.00 38.06 ? 156 GLY D O     1 
ATOM   4129  N N     . THR B  1 157 ? -23.904 18.066  -18.074 1.00 33.31 ? 157 THR D N     1 
ATOM   4130  C CA    . THR B  1 157 ? -23.934 17.722  -19.485 1.00 28.44 ? 157 THR D CA    1 
ATOM   4131  C C     . THR B  1 157 ? -24.114 16.217  -19.657 1.00 27.79 ? 157 THR D C     1 
ATOM   4132  O O     . THR B  1 157 ? -23.460 15.435  -18.959 1.00 29.35 ? 157 THR D O     1 
ATOM   4133  C CB    . THR B  1 157 ? -22.659 18.183  -20.157 1.00 29.86 ? 157 THR D CB    1 
ATOM   4134  O OG1   . THR B  1 157 ? -22.453 19.559  -19.822 1.00 34.01 ? 157 THR D OG1   1 
ATOM   4135  C CG2   . THR B  1 157 ? -22.778 18.042  -21.666 1.00 27.26 ? 157 THR D CG2   1 
ATOM   4136  N N     . PRO B  1 158 ? -24.983 15.786  -20.582 1.00 31.10 ? 158 PRO D N     1 
ATOM   4137  C CA    . PRO B  1 158 ? -25.370 14.366  -20.657 1.00 31.77 ? 158 PRO D CA    1 
ATOM   4138  C C     . PRO B  1 158 ? -24.281 13.428  -21.169 1.00 36.46 ? 158 PRO D C     1 
ATOM   4139  O O     . PRO B  1 158 ? -23.526 13.753  -22.093 1.00 34.35 ? 158 PRO D O     1 
ATOM   4140  C CB    . PRO B  1 158 ? -26.566 14.377  -21.615 1.00 28.53 ? 158 PRO D CB    1 
ATOM   4141  C CG    . PRO B  1 158 ? -26.551 15.704  -22.254 1.00 28.88 ? 158 PRO D CG    1 
ATOM   4142  C CD    . PRO B  1 158 ? -25.948 16.645  -21.284 1.00 28.88 ? 158 PRO D CD    1 
ATOM   4143  N N     . LEU B  1 159 ? -24.252 12.231  -20.575 1.00 34.75 ? 159 LEU D N     1 
ATOM   4144  C CA    . LEU B  1 159 ? -23.218 11.230  -20.796 1.00 40.30 ? 159 LEU D CA    1 
ATOM   4145  C C     . LEU B  1 159 ? -23.808 9.832   -20.715 1.00 39.67 ? 159 LEU D C     1 
ATOM   4146  O O     . LEU B  1 159 ? -24.620 9.551   -19.834 1.00 40.28 ? 159 LEU D O     1 
ATOM   4147  C CB    . LEU B  1 159 ? -22.111 11.309  -19.741 1.00 40.13 ? 159 LEU D CB    1 
ATOM   4148  C CG    . LEU B  1 159 ? -21.552 12.665  -19.373 1.00 31.77 ? 159 LEU D CG    1 
ATOM   4149  C CD1   . LEU B  1 159 ? -21.070 12.633  -17.930 1.00 31.65 ? 159 LEU D CD1   1 
ATOM   4150  C CD2   . LEU B  1 159 ? -20.430 12.903  -20.344 1.00 39.69 ? 159 LEU D CD2   1 
ATOM   4151  N N     . THR B  1 160 ? -23.366 8.947   -21.605 1.00 41.95 ? 160 THR D N     1 
ATOM   4152  C CA    . THR B  1 160 ? -23.565 7.527   -21.363 1.00 41.32 ? 160 THR D CA    1 
ATOM   4153  C C     . THR B  1 160 ? -23.001 7.172   -19.994 1.00 40.62 ? 160 THR D C     1 
ATOM   4154  O O     . THR B  1 160 ? -22.003 7.746   -19.544 1.00 43.14 ? 160 THR D O     1 
ATOM   4155  C CB    . THR B  1 160 ? -22.854 6.678   -22.421 1.00 44.98 ? 160 THR D CB    1 
ATOM   4156  O OG1   . THR B  1 160 ? -21.486 7.106   -22.542 1.00 42.06 ? 160 THR D OG1   1 
ATOM   4157  C CG2   . THR B  1 160 ? -23.545 6.780   -23.766 1.00 41.76 ? 160 THR D CG2   1 
ATOM   4158  N N     . ASP B  1 161 ? -23.640 6.220   -19.325 1.00 37.41 ? 161 ASP D N     1 
ATOM   4159  C CA    . ASP B  1 161 ? -23.052 5.702   -18.097 1.00 43.50 ? 161 ASP D CA    1 
ATOM   4160  C C     . ASP B  1 161 ? -21.611 5.288   -18.337 1.00 38.45 ? 161 ASP D C     1 
ATOM   4161  O O     . ASP B  1 161 ? -21.317 4.480   -19.232 1.00 38.21 ? 161 ASP D O     1 
ATOM   4162  C CB    . ASP B  1 161 ? -23.865 4.526   -17.555 1.00 40.54 ? 161 ASP D CB    1 
ATOM   4163  C CG    . ASP B  1 161 ? -24.479 4.820   -16.210 1.00 53.19 ? 161 ASP D CG    1 
ATOM   4164  O OD1   . ASP B  1 161 ? -24.408 5.986   -15.747 1.00 54.74 ? 161 ASP D OD1   1 
ATOM   4165  O OD2   . ASP B  1 161 ? -25.014 3.870   -15.600 1.00 63.24 ? 161 ASP D OD2   1 
ATOM   4166  N N     . GLY B  1 162 ? -20.704 5.871   -17.564 1.00 29.38 ? 162 GLY D N     1 
ATOM   4167  C CA    . GLY B  1 162 ? -19.299 5.644   -17.790 1.00 34.98 ? 162 GLY D CA    1 
ATOM   4168  C C     . GLY B  1 162 ? -18.530 5.553   -16.493 1.00 31.71 ? 162 GLY D C     1 
ATOM   4169  O O     . GLY B  1 162 ? -18.978 6.014   -15.438 1.00 31.34 ? 162 GLY D O     1 
ATOM   4170  N N     . VAL B  1 163 ? -17.363 4.927   -16.595 1.00 29.95 ? 163 VAL D N     1 
ATOM   4171  C CA    . VAL B  1 163 ? -16.372 4.907   -15.530 1.00 36.61 ? 163 VAL D CA    1 
ATOM   4172  C C     . VAL B  1 163 ? -15.045 5.397   -16.108 1.00 43.56 ? 163 VAL D C     1 
ATOM   4173  O O     . VAL B  1 163 ? -14.643 4.987   -17.207 1.00 37.15 ? 163 VAL D O     1 
ATOM   4174  C CB    . VAL B  1 163 ? -16.220 3.508   -14.891 1.00 35.05 ? 163 VAL D CB    1 
ATOM   4175  C CG1   . VAL B  1 163 ? -15.180 3.524   -13.775 1.00 35.63 ? 163 VAL D CG1   1 
ATOM   4176  C CG2   . VAL B  1 163 ? -17.542 3.023   -14.321 1.00 35.32 ? 163 VAL D CG2   1 
ATOM   4177  N N     . VAL B  1 164 ? -14.397 6.316   -15.386 1.00 39.27 ? 164 VAL D N     1 
ATOM   4178  C CA    . VAL B  1 164 ? -13.010 6.688   -15.637 1.00 40.96 ? 164 VAL D CA    1 
ATOM   4179  C C     . VAL B  1 164 ? -12.154 5.647   -14.926 1.00 38.95 ? 164 VAL D C     1 
ATOM   4180  O O     . VAL B  1 164 ? -11.887 5.766   -13.723 1.00 39.31 ? 164 VAL D O     1 
ATOM   4181  C CB    . VAL B  1 164 ? -12.712 8.126   -15.156 1.00 36.12 ? 164 VAL D CB    1 
ATOM   4182  C CG1   . VAL B  1 164 ? -11.261 8.530   -15.448 1.00 33.41 ? 164 VAL D CG1   1 
ATOM   4183  C CG2   . VAL B  1 164 ? -13.688 9.121   -15.792 1.00 33.25 ? 164 VAL D CG2   1 
ATOM   4184  N N     . ALA B  1 165 ? -11.755 4.602   -15.654 1.00 36.32 ? 165 ALA D N     1 
ATOM   4185  C CA    . ALA B  1 165 ? -11.049 3.485   -15.042 1.00 39.12 ? 165 ALA D CA    1 
ATOM   4186  C C     . ALA B  1 165 ? -9.655  3.911   -14.596 1.00 39.68 ? 165 ALA D C     1 
ATOM   4187  O O     . ALA B  1 165 ? -8.968  4.678   -15.277 1.00 37.26 ? 165 ALA D O     1 
ATOM   4188  C CB    . ALA B  1 165 ? -10.967 2.315   -16.018 1.00 35.56 ? 165 ALA D CB    1 
ATOM   4189  N N     . ARG B  1 166 ? -9.240  3.419   -13.434 1.00 37.04 ? 166 ARG D N     1 
ATOM   4190  C CA    . ARG B  1 166 ? -7.932  3.758   -12.903 1.00 33.80 ? 166 ARG D CA    1 
ATOM   4191  C C     . ARG B  1 166 ? -6.986  2.569   -12.857 1.00 33.93 ? 166 ARG D C     1 
ATOM   4192  O O     . ARG B  1 166 ? -5.885  2.698   -12.312 1.00 41.77 ? 166 ARG D O     1 
ATOM   4193  C CB    . ARG B  1 166 ? -8.063  4.364   -11.507 1.00 36.94 ? 166 ARG D CB    1 
ATOM   4194  C CG    . ARG B  1 166 ? -8.769  5.689   -11.453 1.00 34.41 ? 166 ARG D CG    1 
ATOM   4195  C CD    . ARG B  1 166 ? -9.055  6.052   -10.010 1.00 28.64 ? 166 ARG D CD    1 
ATOM   4196  N NE    . ARG B  1 166 ? -10.077 5.196   -9.425  1.00 30.20 ? 166 ARG D NE    1 
ATOM   4197  C CZ    . ARG B  1 166 ? -10.753 5.515   -8.333  1.00 35.50 ? 166 ARG D CZ    1 
ATOM   4198  N NH1   . ARG B  1 166 ? -10.536 6.658   -7.704  1.00 38.14 ? 166 ARG D NH1   1 
ATOM   4199  N NH2   . ARG B  1 166 ? -11.679 4.676   -7.868  1.00 31.52 ? 166 ARG D NH2   1 
ATOM   4200  N N     . GLY B  1 167 ? -7.374  1.419   -13.408 1.00 33.02 ? 167 GLY D N     1 
ATOM   4201  C CA    . GLY B  1 167 ? -6.528  0.248   -13.377 1.00 33.26 ? 167 GLY D CA    1 
ATOM   4202  C C     . GLY B  1 167 ? -7.279  -0.990  -13.804 1.00 39.02 ? 167 GLY D C     1 
ATOM   4203  O O     . GLY B  1 167 ? -8.512  -0.967  -13.920 1.00 38.34 ? 167 GLY D O     1 
ATOM   4204  N N     . PRO B  1 168 ? -6.560  -2.106  -14.037 1.00 38.46 ? 168 PRO D N     1 
ATOM   4205  C CA    . PRO B  1 168 ? -7.237  -3.289  -14.586 1.00 33.52 ? 168 PRO D CA    1 
ATOM   4206  C C     . PRO B  1 168 ? -8.348  -3.778  -13.690 1.00 37.68 ? 168 PRO D C     1 
ATOM   4207  O O     . PRO B  1 168 ? -9.400  -4.208  -14.187 1.00 38.75 ? 168 PRO D O     1 
ATOM   4208  C CB    . PRO B  1 168 ? -6.105  -4.316  -14.717 1.00 35.05 ? 168 PRO D CB    1 
ATOM   4209  C CG    . PRO B  1 168 ? -4.856  -3.528  -14.701 1.00 37.37 ? 168 PRO D CG    1 
ATOM   4210  C CD    . PRO B  1 168 ? -5.136  -2.378  -13.783 1.00 37.59 ? 168 PRO D CD    1 
ATOM   4211  N N     . ALA B  1 169 ? -8.161  -3.700  -12.373 1.00 34.68 ? 169 ALA D N     1 
ATOM   4212  C CA    . ALA B  1 169 ? -9.246  -4.081  -11.486 1.00 35.94 ? 169 ALA D CA    1 
ATOM   4213  C C     . ALA B  1 169 ? -10.501 -3.280  -11.811 1.00 39.67 ? 169 ALA D C     1 
ATOM   4214  O O     . ALA B  1 169 ? -11.578 -3.849  -12.034 1.00 41.88 ? 169 ALA D O     1 
ATOM   4215  C CB    . ALA B  1 169 ? -8.829  -3.892  -10.029 1.00 35.68 ? 169 ALA D CB    1 
ATOM   4216  N N     . GLU B  1 170 ? -10.369 -1.951  -11.890 1.00 43.76 ? 170 GLU D N     1 
ATOM   4217  C CA    . GLU B  1 170 ? -11.534 -1.094  -12.105 1.00 37.09 ? 170 GLU D CA    1 
ATOM   4218  C C     . GLU B  1 170 ? -12.089 -1.245  -13.512 1.00 38.29 ? 170 GLU D C     1 
ATOM   4219  O O     . GLU B  1 170 ? -13.288 -1.025  -13.740 1.00 42.24 ? 170 GLU D O     1 
ATOM   4220  C CB    . GLU B  1 170 ? -11.169 0.361   -11.812 1.00 37.02 ? 170 GLU D CB    1 
ATOM   4221  C CG    . GLU B  1 170 ? -12.329 1.317   -11.867 1.00 39.53 ? 170 GLU D CG    1 
ATOM   4222  C CD    . GLU B  1 170 ? -11.894 2.761   -11.647 1.00 45.67 ? 170 GLU D CD    1 
ATOM   4223  O OE1   . GLU B  1 170 ? -10.841 2.986   -10.995 1.00 41.44 ? 170 GLU D OE1   1 
ATOM   4224  O OE2   . GLU B  1 170 ? -12.607 3.675   -12.127 1.00 45.23 ? 170 GLU D OE2   1 
ATOM   4225  N N     . VAL B  1 171 ? -11.236 -1.612  -14.466 1.00 35.74 ? 171 VAL D N     1 
ATOM   4226  C CA    . VAL B  1 171 ? -11.721 -1.943  -15.796 1.00 36.17 ? 171 VAL D CA    1 
ATOM   4227  C C     . VAL B  1 171 ? -12.581 -3.196  -15.772 1.00 38.29 ? 171 VAL D C     1 
ATOM   4228  O O     . VAL B  1 171 ? -13.555 -3.301  -16.526 1.00 40.31 ? 171 VAL D O     1 
ATOM   4229  C CB    . VAL B  1 171 ? -10.533 -2.106  -16.751 1.00 42.33 ? 171 VAL D CB    1 
ATOM   4230  C CG1   . VAL B  1 171 ? -11.021 -2.480  -18.147 1.00 39.65 ? 171 VAL D CG1   1 
ATOM   4231  C CG2   . VAL B  1 171 ? -9.713  -0.828  -16.763 1.00 37.49 ? 171 VAL D CG2   1 
ATOM   4232  N N     . ARG B  1 172 ? -12.258 -4.157  -14.905 1.00 38.99 ? 172 ARG D N     1 
ATOM   4233  C CA    . ARG B  1 172 ? -13.019 -5.404  -14.875 1.00 47.85 ? 172 ARG D CA    1 
ATOM   4234  C C     . ARG B  1 172 ? -14.436 -5.185  -14.349 1.00 47.71 ? 172 ARG D C     1 
ATOM   4235  O O     . ARG B  1 172 ? -15.406 -5.717  -14.906 1.00 47.32 ? 172 ARG D O     1 
ATOM   4236  C CB    . ARG B  1 172 ? -12.280 -6.447  -14.032 1.00 50.52 ? 172 ARG D CB    1 
ATOM   4237  C CG    . ARG B  1 172 ? -12.452 -7.898  -14.514 1.00 60.20 ? 172 ARG D CG    1 
ATOM   4238  C CD    . ARG B  1 172 ? -12.718 -8.841  -13.337 1.00 68.24 ? 172 ARG D CD    1 
ATOM   4239  N NE    . ARG B  1 172 ? -13.248 -10.145 -13.721 1.00 68.27 ? 172 ARG D NE    1 
ATOM   4240  C CZ    . ARG B  1 172 ? -14.540 -10.428 -13.824 1.00 67.53 ? 172 ARG D CZ    1 
ATOM   4241  N NH1   . ARG B  1 172 ? -15.465 -9.496  -13.664 1.00 62.29 ? 172 ARG D NH1   1 
ATOM   4242  N NH2   . ARG B  1 172 ? -14.910 -11.671 -14.126 1.00 70.50 ? 172 ARG D NH2   1 
ATOM   4243  N N     . SER B  1 173 ? -14.576 -4.411  -13.277 1.00 46.63 ? 173 SER D N     1 
ATOM   4244  C CA    . SER B  1 173 ? -15.900 -4.165  -12.724 1.00 43.04 ? 173 SER D CA    1 
ATOM   4245  C C     . SER B  1 173 ? -16.761 -3.406  -13.714 1.00 39.90 ? 173 SER D C     1 
ATOM   4246  O O     . SER B  1 173 ? -17.923 -3.755  -13.948 1.00 43.26 ? 173 SER D O     1 
ATOM   4247  C CB    . SER B  1 173 ? -15.775 -3.383  -11.418 1.00 44.33 ? 173 SER D CB    1 
ATOM   4248  O OG    . SER B  1 173 ? -15.351 -2.056  -11.691 1.00 47.90 ? 173 SER D OG    1 
ATOM   4249  N N     . ALA B  1 174 ? -16.201 -2.358  -14.312 1.00 40.36 ? 174 ALA D N     1 
ATOM   4250  C CA    . ALA B  1 174 ? -17.016 -1.459  -15.116 1.00 44.13 ? 174 ALA D CA    1 
ATOM   4251  C C     . ALA B  1 174 ? -17.689 -2.198  -16.270 1.00 43.92 ? 174 ALA D C     1 
ATOM   4252  O O     . ALA B  1 174 ? -18.843 -1.911  -16.617 1.00 41.35 ? 174 ALA D O     1 
ATOM   4253  C CB    . ALA B  1 174 ? -16.159 -0.297  -15.620 1.00 39.97 ? 174 ALA D CB    1 
ATOM   4254  N N     . ILE B  1 175 ? -16.996 -3.163  -16.868 1.00 42.80 ? 175 ILE D N     1 
ATOM   4255  C CA    . ILE B  1 175 ? -17.646 -3.929  -17.922 1.00 44.42 ? 175 ILE D CA    1 
ATOM   4256  C C     . ILE B  1 175 ? -18.678 -4.891  -17.328 1.00 45.61 ? 175 ILE D C     1 
ATOM   4257  O O     . ILE B  1 175 ? -19.694 -5.182  -17.970 1.00 44.57 ? 175 ILE D O     1 
ATOM   4258  C CB    . ILE B  1 175 ? -16.590 -4.647  -18.792 1.00 47.45 ? 175 ILE D CB    1 
ATOM   4259  C CG1   . ILE B  1 175 ? -15.938 -3.668  -19.776 1.00 44.26 ? 175 ILE D CG1   1 
ATOM   4260  C CG2   . ILE B  1 175 ? -17.188 -5.784  -19.584 1.00 44.53 ? 175 ILE D CG2   1 
ATOM   4261  C CD1   . ILE B  1 175 ? -14.417 -3.770  -19.839 1.00 41.23 ? 175 ILE D CD1   1 
ATOM   4262  N N     . GLN B  1 176 ? -18.476 -5.365  -16.091 1.00 44.47 ? 176 GLN D N     1 
ATOM   4263  C CA    . GLN B  1 176 ? -19.456 -6.272  -15.500 1.00 47.27 ? 176 GLN D CA    1 
ATOM   4264  C C     . GLN B  1 176 ? -20.799 -5.594  -15.290 1.00 41.68 ? 176 GLN D C     1 
ATOM   4265  O O     . GLN B  1 176 ? -21.815 -6.282  -15.172 1.00 49.39 ? 176 GLN D O     1 
ATOM   4266  C CB    . GLN B  1 176 ? -18.936 -6.835  -14.174 1.00 51.70 ? 176 GLN D CB    1 
ATOM   4267  C CG    . GLN B  1 176 ? -19.829 -7.908  -13.546 1.00 54.83 ? 176 GLN D CG    1 
ATOM   4268  C CD    . GLN B  1 176 ? -19.040 -9.117  -13.044 1.00 70.81 ? 176 GLN D CD    1 
ATOM   4269  O OE1   . GLN B  1 176 ? -17.936 -9.391  -13.521 1.00 67.66 ? 176 GLN D OE1   1 
ATOM   4270  N NE2   . GLN B  1 176 ? -19.610 -9.851  -12.085 1.00 70.85 ? 176 GLN D NE2   1 
ATOM   4271  N N     . GLU B  1 177 ? -20.833 -4.263  -15.282 1.00 41.14 ? 177 GLU D N     1 
ATOM   4272  C CA    . GLU B  1 177 ? -22.053 -3.495  -15.051 1.00 41.83 ? 177 GLU D CA    1 
ATOM   4273  C C     . GLU B  1 177 ? -22.589 -2.787  -16.290 1.00 43.54 ? 177 GLU D C     1 
ATOM   4274  O O     . GLU B  1 177 ? -23.786 -2.874  -16.574 1.00 45.06 ? 177 GLU D O     1 
ATOM   4275  C CB    . GLU B  1 177 ? -21.808 -2.468  -13.941 1.00 46.07 ? 177 GLU D CB    1 
ATOM   4276  C CG    . GLU B  1 177 ? -23.005 -1.633  -13.614 1.00 52.85 ? 177 GLU D CG    1 
ATOM   4277  C CD    . GLU B  1 177 ? -22.691 -0.547  -12.604 1.00 63.57 ? 177 GLU D CD    1 
ATOM   4278  O OE1   . GLU B  1 177 ? -22.094 0.482   -12.999 1.00 60.78 ? 177 GLU D OE1   1 
ATOM   4279  O OE2   . GLU B  1 177 ? -23.043 -0.728  -11.415 1.00 64.35 ? 177 GLU D OE2   1 
ATOM   4280  N N     . LEU B  1 178 ? -21.744 -2.074  -17.047 1.00 43.87 ? 178 LEU D N     1 
ATOM   4281  C CA    . LEU B  1 178 ? -22.212 -1.291  -18.196 1.00 41.13 ? 178 LEU D CA    1 
ATOM   4282  C C     . LEU B  1 178 ? -22.578 -2.151  -19.407 1.00 38.49 ? 178 LEU D C     1 
ATOM   4283  O O     . LEU B  1 178 ? -23.147 -1.640  -20.383 1.00 36.03 ? 178 LEU D O     1 
ATOM   4284  C CB    . LEU B  1 178 ? -21.141 -0.264  -18.581 1.00 38.54 ? 178 LEU D CB    1 
ATOM   4285  C CG    . LEU B  1 178 ? -20.706 0.653   -17.422 1.00 39.26 ? 178 LEU D CG    1 
ATOM   4286  C CD1   . LEU B  1 178 ? -19.350 1.319   -17.662 1.00 33.48 ? 178 LEU D CD1   1 
ATOM   4287  C CD2   . LEU B  1 178 ? -21.776 1.696   -17.142 1.00 36.28 ? 178 LEU D CD2   1 
ATOM   4288  N N     . ILE B  1 179 ? -22.248 -3.439  -19.369 1.00 38.32 ? 179 ILE D N     1 
ATOM   4289  C CA    . ILE B  1 179 ? -22.578 -4.343  -20.458 1.00 38.64 ? 179 ILE D CA    1 
ATOM   4290  C C     . ILE B  1 179 ? -24.075 -4.601  -20.557 1.00 37.78 ? 179 ILE D C     1 
ATOM   4291  O O     . ILE B  1 179 ? -24.565 -5.041  -21.601 1.00 37.07 ? 179 ILE D O     1 
ATOM   4292  C CB    . ILE B  1 179 ? -21.739 -5.610  -20.200 1.00 38.92 ? 179 ILE D CB    1 
ATOM   4293  C CG1   . ILE B  1 179 ? -21.503 -6.405  -21.477 1.00 42.92 ? 179 ILE D CG1   1 
ATOM   4294  C CG2   . ILE B  1 179 ? -22.335 -6.448  -19.075 1.00 39.84 ? 179 ILE D CG2   1 
ATOM   4295  C CD1   . ILE B  1 179 ? -20.874 -5.585  -22.521 1.00 42.37 ? 179 ILE D CD1   1 
ATOM   4296  N N     . ALA B  1 180 ? -24.826 -4.338  -19.502 1.00 39.72 ? 180 ALA D N     1 
ATOM   4297  C CA    . ALA B  1 180 ? -26.139 -4.949  -19.389 1.00 36.95 ? 180 ALA D CA    1 
ATOM   4298  C C     . ALA B  1 180 ? -27.213 -4.188  -20.160 1.00 42.35 ? 180 ALA D C     1 
ATOM   4299  O O     . ALA B  1 180 ? -28.098 -4.816  -20.750 1.00 51.17 ? 180 ALA D O     1 
ATOM   4300  C CB    . ALA B  1 180 ? -26.508 -5.083  -17.918 1.00 39.47 ? 180 ALA D CB    1 
ATOM   4301  N N     . GLU B  1 181 ? -27.175 -2.850  -20.172 1.00 38.34 ? 181 GLU D N     1 
ATOM   4302  C CA    . GLU B  1 181 ? -28.248 -2.103  -20.831 1.00 44.66 ? 181 GLU D CA    1 
ATOM   4303  C C     . GLU B  1 181 ? -28.382 -2.491  -22.298 1.00 43.41 ? 181 GLU D C     1 
ATOM   4304  O O     . GLU B  1 181 ? -29.494 -2.651  -22.824 1.00 42.09 ? 181 GLU D O     1 
ATOM   4305  C CB    . GLU B  1 181 ? -28.001 -0.598  -20.728 1.00 44.20 ? 181 GLU D CB    1 
ATOM   4306  C CG    . GLU B  1 181 ? -29.116 0.224   -21.373 1.00 45.09 ? 181 GLU D CG    1 
ATOM   4307  C CD    . GLU B  1 181 ? -29.041 1.711   -21.044 1.00 53.74 ? 181 GLU D CD    1 
ATOM   4308  O OE1   . GLU B  1 181 ? -27.914 2.227   -20.898 1.00 55.81 ? 181 GLU D OE1   1 
ATOM   4309  O OE2   . GLU B  1 181 ? -30.101 2.372   -20.939 1.00 52.58 ? 181 GLU D OE2   1 
ATOM   4310  N N     . THR B  1 182 ? -27.257 -2.637  -22.971 1.00 40.31 ? 182 THR D N     1 
ATOM   4311  C CA    . THR B  1 182 ? -27.229 -2.795  -24.399 1.00 37.45 ? 182 THR D CA    1 
ATOM   4312  C C     . THR B  1 182 ? -26.494 -4.034  -24.833 1.00 39.10 ? 182 THR D C     1 
ATOM   4313  O O     . THR B  1 182 ? -26.559 -4.384  -26.012 1.00 43.51 ? 182 THR D O     1 
ATOM   4314  C CB    . THR B  1 182 ? -26.544 -1.587  -25.045 1.00 43.61 ? 182 THR D CB    1 
ATOM   4315  O OG1   . THR B  1 182 ? -25.126 -1.674  -24.811 1.00 40.78 ? 182 THR D OG1   1 
ATOM   4316  C CG2   . THR B  1 182 ? -27.084 -0.295  -24.438 1.00 40.86 ? 182 THR D CG2   1 
ATOM   4317  N N     . GLY B  1 183 ? -25.776 -4.693  -23.944 1.00 39.59 ? 183 GLY D N     1 
ATOM   4318  C CA    . GLY B  1 183 ? -24.829 -5.647  -24.452 1.00 38.22 ? 183 GLY D CA    1 
ATOM   4319  C C     . GLY B  1 183 ? -23.653 -5.032  -25.159 1.00 37.16 ? 183 GLY D C     1 
ATOM   4320  O O     . GLY B  1 183 ? -22.915 -5.748  -25.841 1.00 43.62 ? 183 GLY D O     1 
ATOM   4321  N N     . MET B  1 184 ? -23.436 -3.730  -25.018 1.00 35.78 ? 184 MET D N     1 
ATOM   4322  C CA    . MET B  1 184 ? -22.359 -3.089  -25.756 1.00 45.09 ? 184 MET D CA    1 
ATOM   4323  C C     . MET B  1 184 ? -21.598 -2.091  -24.900 1.00 38.97 ? 184 MET D C     1 
ATOM   4324  O O     . MET B  1 184 ? -22.203 -1.254  -24.224 1.00 35.62 ? 184 MET D O     1 
ATOM   4325  C CB    . MET B  1 184 ? -22.908 -2.392  -26.993 1.00 40.34 ? 184 MET D CB    1 
ATOM   4326  C CG    . MET B  1 184 ? -23.272 -3.367  -28.060 1.00 40.73 ? 184 MET D CG    1 
ATOM   4327  S SD    . MET B  1 184 ? -23.807 -2.505  -29.519 1.00 43.04 ? 184 MET D SD    1 
ATOM   4328  C CE    . MET B  1 184 ? -25.143 -1.504  -28.854 1.00 42.92 ? 184 MET D CE    1 
ATOM   4329  N N     . VAL B  1 185 ? -20.271 -2.143  -24.986 1.00 36.48 ? 185 VAL D N     1 
ATOM   4330  C CA    . VAL B  1 185 ? -19.412 -1.320  -24.149 1.00 38.25 ? 185 VAL D CA    1 
ATOM   4331  C C     . VAL B  1 185 ? -18.187 -0.879  -24.944 1.00 41.80 ? 185 VAL D C     1 
ATOM   4332  O O     . VAL B  1 185 ? -17.746 -1.569  -25.870 1.00 41.22 ? 185 VAL D O     1 
ATOM   4333  C CB    . VAL B  1 185 ? -19.032 -2.100  -22.877 1.00 39.33 ? 185 VAL D CB    1 
ATOM   4334  C CG1   . VAL B  1 185 ? -17.701 -1.661  -22.325 1.00 40.99 ? 185 VAL D CG1   1 
ATOM   4335  C CG2   . VAL B  1 185 ? -20.129 -1.959  -21.816 1.00 36.45 ? 185 VAL D CG2   1 
ATOM   4336  N N     . ILE B  1 186 ? -17.649 0.295   -24.582 1.00 40.46 ? 186 ILE D N     1 
ATOM   4337  C CA    . ILE B  1 186 ? -16.501 0.907   -25.246 1.00 39.83 ? 186 ILE D CA    1 
ATOM   4338  C C     . ILE B  1 186 ? -15.411 1.203   -24.225 1.00 37.01 ? 186 ILE D C     1 
ATOM   4339  O O     . ILE B  1 186 ? -15.686 1.483   -23.058 1.00 37.27 ? 186 ILE D O     1 
ATOM   4340  C CB    . ILE B  1 186 ? -16.909 2.204   -25.991 1.00 37.03 ? 186 ILE D CB    1 
ATOM   4341  C CG1   . ILE B  1 186 ? -15.947 2.506   -27.147 1.00 36.64 ? 186 ILE D CG1   1 
ATOM   4342  C CG2   . ILE B  1 186 ? -17.036 3.370   -25.024 1.00 33.14 ? 186 ILE D CG2   1 
ATOM   4343  C CD1   . ILE B  1 186 ? -16.514 3.485   -28.185 1.00 30.36 ? 186 ILE D CD1   1 
ATOM   4344  N N     . ALA B  1 187 ? -14.164 1.155   -24.672 1.00 36.85 ? 187 ALA D N     1 
ATOM   4345  C CA    . ALA B  1 187 ? -13.026 1.465   -23.815 1.00 31.76 ? 187 ALA D CA    1 
ATOM   4346  C C     . ALA B  1 187 ? -12.091 2.365   -24.604 1.00 37.54 ? 187 ALA D C     1 
ATOM   4347  O O     . ALA B  1 187 ? -11.527 1.949   -25.625 1.00 35.17 ? 187 ALA D O     1 
ATOM   4348  C CB    . ALA B  1 187 ? -12.313 0.198   -23.357 1.00 39.37 ? 187 ALA D CB    1 
ATOM   4349  N N     . LYS B  1 188 ? -11.933 3.595   -24.141 1.00 33.33 ? 188 LYS D N     1 
ATOM   4350  C CA    . LYS B  1 188 ? -11.237 4.627   -24.885 1.00 30.44 ? 188 LYS D CA    1 
ATOM   4351  C C     . LYS B  1 188 ? -9.936  4.950   -24.179 1.00 35.53 ? 188 LYS D C     1 
ATOM   4352  O O     . LYS B  1 188 ? -9.936  5.193   -22.972 1.00 38.75 ? 188 LYS D O     1 
ATOM   4353  C CB    . LYS B  1 188 ? -12.091 5.892   -24.979 1.00 32.74 ? 188 LYS D CB    1 
ATOM   4354  C CG    . LYS B  1 188 ? -13.588 5.642   -25.069 1.00 35.34 ? 188 LYS D CG    1 
ATOM   4355  C CD    . LYS B  1 188 ? -14.333 6.902   -25.535 1.00 35.49 ? 188 LYS D CD    1 
ATOM   4356  C CE    . LYS B  1 188 ? -15.791 6.591   -25.894 1.00 40.06 ? 188 LYS D CE    1 
ATOM   4357  N NZ    . LYS B  1 188 ? -16.711 7.773   -25.794 1.00 37.01 ? 188 LYS D NZ    1 
ATOM   4358  N N     . GLN B  1 189 ? -8.837  4.970   -24.924 1.00 38.16 ? 189 GLN D N     1 
ATOM   4359  C CA    . GLN B  1 189 ? -7.600  5.546   -24.405 1.00 41.28 ? 189 GLN D CA    1 
ATOM   4360  C C     . GLN B  1 189 ? -7.772  7.053   -24.177 1.00 37.60 ? 189 GLN D C     1 
ATOM   4361  O O     . GLN B  1 189 ? -8.452  7.736   -24.949 1.00 37.02 ? 189 GLN D O     1 
ATOM   4362  C CB    . GLN B  1 189 ? -6.438  5.262   -25.374 1.00 38.61 ? 189 GLN D CB    1 
ATOM   4363  C CG    . GLN B  1 189 ? -5.318  6.305   -25.347 1.00 37.96 ? 189 GLN D CG    1 
ATOM   4364  C CD    . GLN B  1 189 ? -3.979  5.761   -25.799 1.00 48.53 ? 189 GLN D CD    1 
ATOM   4365  O OE1   . GLN B  1 189 ? -2.951  5.968   -25.132 1.00 51.38 ? 189 GLN D OE1   1 
ATOM   4366  N NE2   . GLN B  1 189 ? -3.973  5.067   -26.941 1.00 45.57 ? 189 GLN D NE2   1 
ATOM   4367  N N     . ASP B  1 190 ? -7.135  7.578   -23.120 1.00 34.08 ? 190 ASP D N     1 
ATOM   4368  C CA    . ASP B  1 190 ? -7.499  8.899   -22.599 1.00 35.56 ? 190 ASP D CA    1 
ATOM   4369  C C     . ASP B  1 190 ? -7.127  10.015  -23.566 1.00 40.87 ? 190 ASP D C     1 
ATOM   4370  O O     . ASP B  1 190 ? -7.926  10.932  -23.796 1.00 40.35 ? 190 ASP D O     1 
ATOM   4371  C CB    . ASP B  1 190 ? -6.839  9.143   -21.234 1.00 40.01 ? 190 ASP D CB    1 
ATOM   4372  C CG    . ASP B  1 190 ? -7.657  10.083  -20.338 1.00 38.66 ? 190 ASP D CG    1 
ATOM   4373  O OD1   . ASP B  1 190 ? -8.845  10.357  -20.646 1.00 36.58 ? 190 ASP D OD1   1 
ATOM   4374  O OD2   . ASP B  1 190 ? -7.104  10.566  -19.328 1.00 38.26 ? 190 ASP D OD2   1 
ATOM   4375  N N     . ARG B  1 191 ? -5.919  9.959   -24.135 1.00 41.64 ? 191 ARG D N     1 
ATOM   4376  C CA    . ARG B  1 191 ? -5.487  10.871  -25.194 1.00 37.19 ? 191 ARG D CA    1 
ATOM   4377  C C     . ARG B  1 191 ? -5.482  10.111  -26.512 1.00 44.25 ? 191 ARG D C     1 
ATOM   4378  O O     . ARG B  1 191 ? -4.739  9.132   -26.653 1.00 49.30 ? 191 ARG D O     1 
ATOM   4379  C CB    . ARG B  1 191 ? -4.091  11.425  -24.912 1.00 31.54 ? 191 ARG D CB    1 
ATOM   4380  C CG    . ARG B  1 191 ? -4.010  12.382  -23.736 1.00 33.53 ? 191 ARG D CG    1 
ATOM   4381  C CD    . ARG B  1 191 ? -2.584  12.516  -23.288 1.00 28.58 ? 191 ARG D CD    1 
ATOM   4382  N NE    . ARG B  1 191 ? -2.351  13.687  -22.458 1.00 35.12 ? 191 ARG D NE    1 
ATOM   4383  C CZ    . ARG B  1 191 ? -2.285  13.676  -21.133 1.00 38.68 ? 191 ARG D CZ    1 
ATOM   4384  N NH1   . ARG B  1 191 ? -2.496  12.571  -20.433 1.00 38.87 ? 191 ARG D NH1   1 
ATOM   4385  N NH2   . ARG B  1 191 ? -1.994  14.802  -20.492 1.00 37.26 ? 191 ARG D NH2   1 
ATOM   4386  N N     . SER B  1 192 ? -6.303  10.549  -27.471 1.00 43.62 ? 192 SER D N     1 
ATOM   4387  C CA    . SER B  1 192 ? -6.422  9.860   -28.756 1.00 40.31 ? 192 SER D CA    1 
ATOM   4388  C C     . SER B  1 192 ? -7.452  10.594  -29.596 1.00 41.01 ? 192 SER D C     1 
ATOM   4389  O O     . SER B  1 192 ? -8.236  11.401  -29.085 1.00 50.68 ? 192 SER D O     1 
ATOM   4390  C CB    . SER B  1 192 ? -6.828  8.391   -28.606 1.00 41.97 ? 192 SER D CB    1 
ATOM   4391  O OG    . SER B  1 192 ? -7.665  7.982   -29.675 1.00 50.71 ? 192 SER D OG    1 
ATOM   4392  N N     . GLY B  1 193 ? -7.463  10.280  -30.893 1.00 35.71 ? 193 GLY D N     1 
ATOM   4393  C CA    . GLY B  1 193 ? -8.410  10.892  -31.799 1.00 46.56 ? 193 GLY D CA    1 
ATOM   4394  C C     . GLY B  1 193 ? -8.931  9.915   -32.836 1.00 49.91 ? 193 GLY D C     1 
ATOM   4395  O O     . GLY B  1 193 ? -8.427  8.797   -32.983 1.00 49.38 ? 193 GLY D O     1 
ATOM   4396  N N     . GLY B  1 194 ? -9.979  10.361  -33.538 1.00 51.84 ? 194 GLY D N     1 
ATOM   4397  C CA    . GLY B  1 194 ? -10.503 9.727   -34.734 1.00 48.52 ? 194 GLY D CA    1 
ATOM   4398  C C     . GLY B  1 194 ? -11.187 8.392   -34.546 1.00 50.67 ? 194 GLY D C     1 
ATOM   4399  O O     . GLY B  1 194 ? -11.612 7.790   -35.540 1.00 48.48 ? 194 GLY D O     1 
ATOM   4400  N N     . GLY B  1 195 ? -11.318 7.909   -33.317 1.00 52.11 ? 195 GLY D N     1 
ATOM   4401  C CA    . GLY B  1 195 ? -11.755 6.546   -33.091 1.00 46.76 ? 195 GLY D CA    1 
ATOM   4402  C C     . GLY B  1 195 ? -10.636 5.532   -33.022 1.00 45.85 ? 195 GLY D C     1 
ATOM   4403  O O     . GLY B  1 195 ? -10.902 4.335   -33.173 1.00 43.70 ? 195 GLY D O     1 
ATOM   4404  N N     . HIS B  1 196 ? -9.394  5.973   -32.773 1.00 53.02 ? 196 HIS D N     1 
ATOM   4405  C CA    . HIS B  1 196 ? -8.200  5.143   -32.886 1.00 46.75 ? 196 HIS D CA    1 
ATOM   4406  C C     . HIS B  1 196 ? -7.799  4.466   -31.579 1.00 43.94 ? 196 HIS D C     1 
ATOM   4407  O O     . HIS B  1 196 ? -7.102  3.448   -31.619 1.00 42.72 ? 196 HIS D O     1 
ATOM   4408  C CB    . HIS B  1 196 ? -7.026  5.997   -33.388 1.00 48.20 ? 196 HIS D CB    1 
ATOM   4409  C CG    . HIS B  1 196 ? -7.103  6.370   -34.844 1.00 54.18 ? 196 HIS D CG    1 
ATOM   4410  N ND1   . HIS B  1 196 ? -7.080  5.438   -35.861 1.00 56.07 ? 196 HIS D ND1   1 
ATOM   4411  C CD2   . HIS B  1 196 ? -7.196  7.580   -35.452 1.00 54.10 ? 196 HIS D CD2   1 
ATOM   4412  C CE1   . HIS B  1 196 ? -7.153  6.055   -37.028 1.00 53.67 ? 196 HIS D CE1   1 
ATOM   4413  N NE2   . HIS B  1 196 ? -7.226  7.355   -36.809 1.00 54.57 ? 196 HIS D NE2   1 
ATOM   4414  N N     . GLY B  1 197 ? -8.200  5.007   -30.429 1.00 44.66 ? 197 GLY D N     1 
ATOM   4415  C CA    . GLY B  1 197 ? -7.814  4.438   -29.148 1.00 42.18 ? 197 GLY D CA    1 
ATOM   4416  C C     . GLY B  1 197 ? -8.979  3.744   -28.474 1.00 39.65 ? 197 GLY D C     1 
ATOM   4417  O O     . GLY B  1 197 ? -9.010  3.559   -27.246 1.00 41.10 ? 197 GLY D O     1 
ATOM   4418  N N     . ASN B  1 198 ? -9.942  3.346   -29.299 1.00 35.68 ? 198 ASN D N     1 
ATOM   4419  C CA    . ASN B  1 198 ? -11.207 2.795   -28.845 1.00 36.85 ? 198 ASN D CA    1 
ATOM   4420  C C     . ASN B  1 198 ? -11.284 1.320   -29.218 1.00 37.35 ? 198 ASN D C     1 
ATOM   4421  O O     . ASN B  1 198 ? -11.053 0.952   -30.374 1.00 42.89 ? 198 ASN D O     1 
ATOM   4422  C CB    . ASN B  1 198 ? -12.390 3.567   -29.453 1.00 33.68 ? 198 ASN D CB    1 
ATOM   4423  C CG    . ASN B  1 198 ? -12.377 5.053   -29.082 1.00 32.80 ? 198 ASN D CG    1 
ATOM   4424  O OD1   . ASN B  1 198 ? -11.497 5.504   -28.345 1.00 34.68 ? 198 ASN D OD1   1 
ATOM   4425  N ND2   . ASN B  1 198 ? -13.354 5.811   -29.579 1.00 24.90 ? 198 ASN D ND2   1 
ATOM   4426  N N     . ILE B  1 199 ? -11.575 0.481   -28.230 1.00 37.61 ? 199 ILE D N     1 
ATOM   4427  C CA    . ILE B  1 199 ? -11.964 -0.906  -28.434 1.00 32.66 ? 199 ILE D CA    1 
ATOM   4428  C C     . ILE B  1 199 ? -13.381 -1.071  -27.905 1.00 35.47 ? 199 ILE D C     1 
ATOM   4429  O O     . ILE B  1 199 ? -13.744 -0.470  -26.888 1.00 36.91 ? 199 ILE D O     1 
ATOM   4430  C CB    . ILE B  1 199 ? -11.009 -1.873  -27.713 1.00 40.37 ? 199 ILE D CB    1 
ATOM   4431  C CG1   . ILE B  1 199 ? -9.543  -1.511  -27.999 1.00 35.60 ? 199 ILE D CG1   1 
ATOM   4432  C CG2   . ILE B  1 199 ? -11.354 -3.319  -28.075 1.00 43.48 ? 199 ILE D CG2   1 
ATOM   4433  C CD1   . ILE B  1 199 ? -8.621  -1.813  -26.854 1.00 34.08 ? 199 ILE D CD1   1 
ATOM   4434  N N     . GLY B  1 200 ? -14.185 -1.865  -28.604 1.00 34.59 ? 200 GLY D N     1 
ATOM   4435  C CA    . GLY B  1 200 ? -15.527 -2.174  -28.173 1.00 35.51 ? 200 GLY D CA    1 
ATOM   4436  C C     . GLY B  1 200 ? -15.592 -3.530  -27.496 1.00 42.58 ? 200 GLY D C     1 
ATOM   4437  O O     . GLY B  1 200 ? -14.652 -4.316  -27.519 1.00 41.66 ? 200 GLY D O     1 
ATOM   4438  N N     . ILE B  1 201 ? -16.730 -3.785  -26.861 1.00 45.97 ? 201 ILE D N     1 
ATOM   4439  C CA    . ILE B  1 201 ? -16.995 -5.056  -26.195 1.00 45.81 ? 201 ILE D CA    1 
ATOM   4440  C C     . ILE B  1 201 ? -18.416 -5.472  -26.549 1.00 46.91 ? 201 ILE D C     1 
ATOM   4441  O O     . ILE B  1 201 ? -19.372 -4.706  -26.335 1.00 45.70 ? 201 ILE D O     1 
ATOM   4442  C CB    . ILE B  1 201 ? -16.798 -4.973  -24.667 1.00 46.00 ? 201 ILE D CB    1 
ATOM   4443  C CG1   . ILE B  1 201 ? -15.359 -4.572  -24.337 1.00 42.15 ? 201 ILE D CG1   1 
ATOM   4444  C CG2   . ILE B  1 201 ? -17.112 -6.317  -23.995 1.00 46.49 ? 201 ILE D CG2   1 
ATOM   4445  C CD1   . ILE B  1 201 ? -15.139 -3.068  -24.225 1.00 44.39 ? 201 ILE D CD1   1 
ATOM   4446  N N     . SER B  1 202 ? -18.552 -6.671  -27.104 1.00 45.58 ? 202 SER D N     1 
ATOM   4447  C CA    . SER B  1 202 ? -19.804 -7.127  -27.681 1.00 47.60 ? 202 SER D CA    1 
ATOM   4448  C C     . SER B  1 202 ? -20.313 -8.355  -26.950 1.00 53.35 ? 202 SER D C     1 
ATOM   4449  O O     . SER B  1 202 ? -19.540 -9.192  -26.479 1.00 61.25 ? 202 SER D O     1 
ATOM   4450  C CB    . SER B  1 202 ? -19.639 -7.460  -29.176 1.00 52.34 ? 202 SER D CB    1 
ATOM   4451  O OG    . SER B  1 202 ? -20.455 -8.561  -29.566 1.00 57.63 ? 202 SER D OG    1 
ATOM   4452  N N     . THR B  1 203 ? -21.630 -8.455  -26.866 1.00 53.06 ? 203 THR D N     1 
ATOM   4453  C CA    . THR B  1 203 ? -22.282 -9.715  -26.567 1.00 52.87 ? 203 THR D CA    1 
ATOM   4454  C C     . THR B  1 203 ? -22.963 -10.298 -27.801 1.00 55.68 ? 203 THR D C     1 
ATOM   4455  O O     . THR B  1 203 ? -23.730 -11.258 -27.681 1.00 63.21 ? 203 THR D O     1 
ATOM   4456  C CB    . THR B  1 203 ? -23.276 -9.519  -25.420 1.00 56.01 ? 203 THR D CB    1 
ATOM   4457  O OG1   . THR B  1 203 ? -23.956 -8.269  -25.579 1.00 50.88 ? 203 THR D OG1   1 
ATOM   4458  C CG2   . THR B  1 203 ? -22.551 -9.490  -24.100 1.00 53.94 ? 203 THR D CG2   1 
ATOM   4459  N N     . SER B  1 204 ? -22.704 -9.735  -28.993 1.00 55.58 ? 204 SER D N     1 
ATOM   4460  C CA    . SER B  1 204 ? -23.307 -10.227 -30.229 1.00 59.74 ? 204 SER D CA    1 
ATOM   4461  C C     . SER B  1 204 ? -22.476 -9.866  -31.454 1.00 56.06 ? 204 SER D C     1 
ATOM   4462  O O     . SER B  1 204 ? -22.364 -8.689  -31.818 1.00 53.06 ? 204 SER D O     1 
ATOM   4463  C CB    . SER B  1 204 ? -24.728 -9.686  -30.412 1.00 62.78 ? 204 SER D CB    1 
ATOM   4464  O OG    . SER B  1 204 ? -25.260 -10.099 -31.668 1.00 61.87 ? 204 SER D OG    1 
ATOM   4465  N N     . PRO B  1 205 ? -21.936 -10.868 -32.148 1.00 60.74 ? 205 PRO D N     1 
ATOM   4466  C CA    . PRO B  1 205 ? -21.068 -10.589 -33.305 1.00 58.44 ? 205 PRO D CA    1 
ATOM   4467  C C     . PRO B  1 205 ? -21.741 -9.791  -34.415 1.00 64.40 ? 205 PRO D C     1 
ATOM   4468  O O     . PRO B  1 205 ? -21.036 -9.274  -35.294 1.00 69.15 ? 205 PRO D O     1 
ATOM   4469  C CB    . PRO B  1 205 ? -20.668 -11.990 -33.794 1.00 61.31 ? 205 PRO D CB    1 
ATOM   4470  C CG    . PRO B  1 205 ? -21.024 -12.930 -32.663 1.00 58.41 ? 205 PRO D CG    1 
ATOM   4471  C CD    . PRO B  1 205 ? -22.166 -12.307 -31.943 1.00 58.55 ? 205 PRO D CD    1 
ATOM   4472  N N     . GLU B  1 206 ? -23.071 -9.683  -34.428 1.00 62.97 ? 206 GLU D N     1 
ATOM   4473  C CA    . GLU B  1 206 ? -23.741 -8.835  -35.403 1.00 60.16 ? 206 GLU D CA    1 
ATOM   4474  C C     . GLU B  1 206 ? -24.061 -7.466  -34.830 1.00 58.54 ? 206 GLU D C     1 
ATOM   4475  O O     . GLU B  1 206 ? -25.015 -6.814  -35.269 1.00 63.54 ? 206 GLU D O     1 
ATOM   4476  C CB    . GLU B  1 206 ? -25.005 -9.502  -35.947 1.00 56.89 ? 206 GLU D CB    1 
ATOM   4477  C CG    . GLU B  1 206 ? -24.740 -10.439 -37.140 1.00 65.83 ? 206 GLU D CG    1 
ATOM   4478  C CD    . GLU B  1 206 ? -24.248 -9.723  -38.415 1.00 68.25 ? 206 GLU D CD    1 
ATOM   4479  O OE1   . GLU B  1 206 ? -24.241 -8.468  -38.456 1.00 67.18 ? 206 GLU D OE1   1 
ATOM   4480  O OE2   . GLU B  1 206 ? -23.854 -10.431 -39.379 1.00 56.80 ? 206 GLU D OE2   1 
ATOM   4481  N N     . SER B  1 207 ? -23.284 -7.025  -33.848 1.00 52.25 ? 207 SER D N     1 
ATOM   4482  C CA    . SER B  1 207 ? -23.327 -5.648  -33.380 1.00 53.56 ? 207 SER D CA    1 
ATOM   4483  C C     . SER B  1 207 ? -22.123 -4.904  -33.943 1.00 52.16 ? 207 SER D C     1 
ATOM   4484  O O     . SER B  1 207 ? -20.994 -5.412  -33.912 1.00 44.87 ? 207 SER D O     1 
ATOM   4485  C CB    . SER B  1 207 ? -23.341 -5.581  -31.854 1.00 51.25 ? 207 SER D CB    1 
ATOM   4486  O OG    . SER B  1 207 ? -23.970 -6.717  -31.294 1.00 49.42 ? 207 SER D OG    1 
ATOM   4487  N N     . SER B  1 208 ? -22.370 -3.710  -34.471 1.00 49.61 ? 208 SER D N     1 
ATOM   4488  C CA    . SER B  1 208 ? -21.352 -2.925  -35.158 1.00 49.92 ? 208 SER D CA    1 
ATOM   4489  C C     . SER B  1 208 ? -21.006 -1.681  -34.351 1.00 48.56 ? 208 SER D C     1 
ATOM   4490  O O     . SER B  1 208 ? -21.890 -1.045  -33.763 1.00 45.99 ? 208 SER D O     1 
ATOM   4491  C CB    . SER B  1 208 ? -21.830 -2.532  -36.554 1.00 54.39 ? 208 SER D CB    1 
ATOM   4492  O OG    . SER B  1 208 ? -22.657 -1.381  -36.485 1.00 62.23 ? 208 SER D OG    1 
ATOM   4493  N N     . PHE B  1 209 ? -19.714 -1.329  -34.329 1.00 39.70 ? 209 PHE D N     1 
ATOM   4494  C CA    . PHE B  1 209 ? -19.181 -0.330  -33.405 1.00 40.63 ? 209 PHE D CA    1 
ATOM   4495  C C     . PHE B  1 209 ? -18.475 0.776   -34.181 1.00 40.60 ? 209 PHE D C     1 
ATOM   4496  O O     . PHE B  1 209 ? -17.241 0.766   -34.315 1.00 42.42 ? 209 PHE D O     1 
ATOM   4497  C CB    . PHE B  1 209 ? -18.230 -0.967  -32.392 1.00 38.14 ? 209 PHE D CB    1 
ATOM   4498  C CG    . PHE B  1 209 ? -18.908 -1.878  -31.419 1.00 44.03 ? 209 PHE D CG    1 
ATOM   4499  C CD1   . PHE B  1 209 ? -19.396 -3.117  -31.824 1.00 45.29 ? 209 PHE D CD1   1 
ATOM   4500  C CD2   . PHE B  1 209 ? -19.063 -1.503  -30.092 1.00 45.25 ? 209 PHE D CD2   1 
ATOM   4501  C CE1   . PHE B  1 209 ? -20.029 -3.974  -30.923 1.00 46.74 ? 209 PHE D CE1   1 
ATOM   4502  C CE2   . PHE B  1 209 ? -19.694 -2.353  -29.178 1.00 48.20 ? 209 PHE D CE2   1 
ATOM   4503  C CZ    . PHE B  1 209 ? -20.177 -3.592  -29.598 1.00 49.74 ? 209 PHE D CZ    1 
ATOM   4504  N N     . PRO B  1 210 ? -19.221 1.747   -34.699 1.00 39.78 ? 210 PRO D N     1 
ATOM   4505  C CA    . PRO B  1 210 ? -18.584 2.970   -35.199 1.00 37.40 ? 210 PRO D CA    1 
ATOM   4506  C C     . PRO B  1 210 ? -17.750 3.617   -34.110 1.00 37.06 ? 210 PRO D C     1 
ATOM   4507  O O     . PRO B  1 210 ? -18.189 3.767   -32.969 1.00 37.07 ? 210 PRO D O     1 
ATOM   4508  C CB    . PRO B  1 210 ? -19.766 3.856   -35.601 1.00 37.21 ? 210 PRO D CB    1 
ATOM   4509  C CG    . PRO B  1 210 ? -20.874 2.916   -35.869 1.00 36.50 ? 210 PRO D CG    1 
ATOM   4510  C CD    . PRO B  1 210 ? -20.663 1.709   -34.994 1.00 40.34 ? 210 PRO D CD    1 
ATOM   4511  N N     . GLY B  1 211 ? -16.543 4.018   -34.477 1.00 34.11 ? 211 GLY D N     1 
ATOM   4512  C CA    . GLY B  1 211 ? -15.707 4.719   -33.535 1.00 37.92 ? 211 GLY D CA    1 
ATOM   4513  C C     . GLY B  1 211 ? -14.888 3.812   -32.666 1.00 39.87 ? 211 GLY D C     1 
ATOM   4514  O O     . GLY B  1 211 ? -14.373 4.265   -31.644 1.00 38.87 ? 211 GLY D O     1 
ATOM   4515  N N     . THR B  1 212 ? -14.751 2.543   -33.044 1.00 42.16 ? 212 THR D N     1 
ATOM   4516  C CA    . THR B  1 212 ? -13.862 1.592   -32.398 1.00 39.50 ? 212 THR D CA    1 
ATOM   4517  C C     . THR B  1 212 ? -12.789 1.132   -33.385 1.00 45.41 ? 212 THR D C     1 
ATOM   4518  O O     . THR B  1 212 ? -12.837 1.430   -34.582 1.00 36.22 ? 212 THR D O     1 
ATOM   4519  C CB    . THR B  1 212 ? -14.650 0.391   -31.859 1.00 38.60 ? 212 THR D CB    1 
ATOM   4520  O OG1   . THR B  1 212 ? -15.331 -0.267  -32.938 1.00 40.65 ? 212 THR D OG1   1 
ATOM   4521  C CG2   . THR B  1 212 ? -15.676 0.855   -30.827 1.00 39.93 ? 212 THR D CG2   1 
ATOM   4522  N N     . ARG B  1 213 ? -11.800 0.395   -32.878 1.00 46.41 ? 213 ARG D N     1 
ATOM   4523  C CA    . ARG B  1 213 ? -10.790 -0.217  -33.737 1.00 45.06 ? 213 ARG D CA    1 
ATOM   4524  C C     . ARG B  1 213 ? -11.009 -1.726  -33.814 1.00 49.33 ? 213 ARG D C     1 
ATOM   4525  O O     . ARG B  1 213 ? -11.520 -2.218  -34.821 1.00 52.87 ? 213 ARG D O     1 
ATOM   4526  C CB    . ARG B  1 213 ? -9.369  0.177   -33.285 1.00 39.77 ? 213 ARG D CB    1 
ATOM   4527  C CG    . ARG B  1 213 ? -8.781  -0.446  -32.020 1.00 40.46 ? 213 ARG D CG    1 
ATOM   4528  C CD    . ARG B  1 213 ? -7.382  0.087   -31.693 1.00 41.55 ? 213 ARG D CD    1 
ATOM   4529  N NE    . ARG B  1 213 ? -6.658  -0.806  -30.791 1.00 42.70 ? 213 ARG D NE    1 
ATOM   4530  C CZ    . ARG B  1 213 ? -5.748  -0.412  -29.910 1.00 35.42 ? 213 ARG D CZ    1 
ATOM   4531  N NH1   . ARG B  1 213 ? -5.425  0.866   -29.770 1.00 34.69 ? 213 ARG D NH1   1 
ATOM   4532  N NH2   . ARG B  1 213 ? -5.147  -1.322  -29.152 1.00 33.51 ? 213 ARG D NH2   1 
ATOM   4533  N N     . GLU B  1 214 ? -10.655 -2.486  -32.783 1.00 45.77 ? 214 GLU D N     1 
ATOM   4534  C CA    . GLU B  1 214 ? -11.091 -3.865  -32.677 1.00 43.86 ? 214 GLU D CA    1 
ATOM   4535  C C     . GLU B  1 214 ? -12.470 -3.879  -32.027 1.00 45.92 ? 214 GLU D C     1 
ATOM   4536  O O     . GLU B  1 214 ? -13.006 -2.837  -31.647 1.00 41.97 ? 214 GLU D O     1 
ATOM   4537  C CB    . GLU B  1 214 ? -10.088 -4.698  -31.879 1.00 45.78 ? 214 GLU D CB    1 
ATOM   4538  C CG    . GLU B  1 214 ? -8.854  -5.121  -32.642 1.00 43.26 ? 214 GLU D CG    1 
ATOM   4539  C CD    . GLU B  1 214 ? -8.584  -6.602  -32.480 1.00 54.51 ? 214 GLU D CD    1 
ATOM   4540  O OE1   . GLU B  1 214 ? -9.375  -7.256  -31.765 1.00 55.55 ? 214 GLU D OE1   1 
ATOM   4541  O OE2   . GLU B  1 214 ? -7.599  -7.118  -33.063 1.00 56.34 ? 214 GLU D OE2   1 
ATOM   4542  N N     . VAL B  1 215 ? -13.068 -5.069  -31.933 1.00 52.15 ? 215 VAL D N     1 
ATOM   4543  C CA    . VAL B  1 215 ? -14.180 -5.338  -31.023 1.00 45.55 ? 215 VAL D CA    1 
ATOM   4544  C C     . VAL B  1 215 ? -13.960 -6.733  -30.451 1.00 51.58 ? 215 VAL D C     1 
ATOM   4545  O O     . VAL B  1 215 ? -13.805 -7.697  -31.209 1.00 53.13 ? 215 VAL D O     1 
ATOM   4546  C CB    . VAL B  1 215 ? -15.567 -5.245  -31.688 1.00 43.04 ? 215 VAL D CB    1 
ATOM   4547  C CG1   . VAL B  1 215 ? -16.636 -5.713  -30.695 1.00 41.53 ? 215 VAL D CG1   1 
ATOM   4548  C CG2   . VAL B  1 215 ? -15.867 -3.816  -32.125 1.00 41.86 ? 215 VAL D CG2   1 
ATOM   4549  N N     . LEU B  1 216 ? -13.926 -6.837  -29.123 1.00 55.92 ? 216 LEU D N     1 
ATOM   4550  C CA    . LEU B  1 216 ? -13.695 -8.091  -28.413 1.00 51.89 ? 216 LEU D CA    1 
ATOM   4551  C C     . LEU B  1 216 ? -14.992 -8.573  -27.771 1.00 52.66 ? 216 LEU D C     1 
ATOM   4552  O O     . LEU B  1 216 ? -15.792 -7.767  -27.284 1.00 55.40 ? 216 LEU D O     1 
ATOM   4553  C CB    . LEU B  1 216 ? -12.606 -7.913  -27.349 1.00 51.00 ? 216 LEU D CB    1 
ATOM   4554  C CG    . LEU B  1 216 ? -11.186 -8.314  -27.774 1.00 56.44 ? 216 LEU D CG    1 
ATOM   4555  C CD1   . LEU B  1 216 ? -10.630 -7.363  -28.832 1.00 45.96 ? 216 LEU D CD1   1 
ATOM   4556  C CD2   . LEU B  1 216 ? -10.249 -8.409  -26.561 1.00 60.87 ? 216 LEU D CD2   1 
ATOM   4557  N N     . ALA B  1 217 ? -15.204 -9.886  -27.770 1.00 52.11 ? 217 ALA D N     1 
ATOM   4558  C CA    . ALA B  1 217 ? -16.465 -10.435 -27.289 1.00 54.10 ? 217 ALA D CA    1 
ATOM   4559  C C     . ALA B  1 217 ? -16.475 -10.581 -25.768 1.00 54.16 ? 217 ALA D C     1 
ATOM   4560  O O     . ALA B  1 217 ? -15.475 -10.967 -25.158 1.00 47.61 ? 217 ALA D O     1 
ATOM   4561  C CB    . ALA B  1 217 ? -16.733 -11.786 -27.944 1.00 59.39 ? 217 ALA D CB    1 
ATOM   4562  N N     . TYR B  1 218 ? -17.620 -10.263 -25.160 1.00 59.03 ? 218 TYR D N     1 
ATOM   4563  C CA    . TYR B  1 218 ? -17.775 -10.428 -23.719 1.00 64.37 ? 218 TYR D CA    1 
ATOM   4564  C C     . TYR B  1 218 ? -17.619 -11.897 -23.341 1.00 64.66 ? 218 TYR D C     1 
ATOM   4565  O O     . TYR B  1 218 ? -17.931 -12.799 -24.122 1.00 66.78 ? 218 TYR D O     1 
ATOM   4566  C CB    . TYR B  1 218 ? -19.139 -9.910  -23.240 1.00 61.26 ? 218 TYR D CB    1 
ATOM   4567  C CG    . TYR B  1 218 ? -19.304 -10.027 -21.733 1.00 66.67 ? 218 TYR D CG    1 
ATOM   4568  C CD1   . TYR B  1 218 ? -18.626 -9.173  -20.872 1.00 65.53 ? 218 TYR D CD1   1 
ATOM   4569  C CD2   . TYR B  1 218 ? -20.117 -11.010 -21.170 1.00 67.80 ? 218 TYR D CD2   1 
ATOM   4570  C CE1   . TYR B  1 218 ? -18.757 -9.283  -19.487 1.00 66.94 ? 218 TYR D CE1   1 
ATOM   4571  C CE2   . TYR B  1 218 ? -20.249 -11.133 -19.779 1.00 72.32 ? 218 TYR D CE2   1 
ATOM   4572  C CZ    . TYR B  1 218 ? -19.564 -10.262 -18.941 1.00 71.95 ? 218 TYR D CZ    1 
ATOM   4573  O OH    . TYR B  1 218 ? -19.676 -10.356 -17.562 1.00 66.28 ? 218 TYR D OH    1 
ATOM   4574  N N     . ALA B  1 219 ? -17.119 -12.138 -22.128 1.00 67.06 ? 219 ALA D N     1 
ATOM   4575  C CA    . ALA B  1 219 ? -16.823 -13.503 -21.708 1.00 69.80 ? 219 ALA D CA    1 
ATOM   4576  C C     . ALA B  1 219 ? -16.708 -13.507 -20.184 1.00 73.32 ? 219 ALA D C     1 
ATOM   4577  O O     . ALA B  1 219 ? -15.666 -13.134 -19.636 1.00 76.08 ? 219 ALA D O     1 
ATOM   4578  C CB    . ALA B  1 219 ? -15.556 -14.018 -22.369 1.00 70.70 ? 219 ALA D CB    1 
ATOM   4579  N N     . ASN B  1 220 ? -17.778 -13.962 -19.526 1.00 77.02 ? 220 ASN D N     1 
ATOM   4580  C CA    . ASN B  1 220 ? -17.861 -13.928 -18.068 1.00 73.20 ? 220 ASN D CA    1 
ATOM   4581  C C     . ASN B  1 220 ? -16.685 -14.646 -17.421 1.00 70.06 ? 220 ASN D C     1 
ATOM   4582  O O     . ASN B  1 220 ? -16.082 -14.150 -16.462 1.00 67.90 ? 220 ASN D O     1 
ATOM   4583  C CB    . ASN B  1 220 ? -19.172 -14.564 -17.631 1.00 70.09 ? 220 ASN D CB    1 
ATOM   4584  C CG    . ASN B  1 220 ? -19.508 -14.232 -16.222 1.00 74.40 ? 220 ASN D CG    1 
ATOM   4585  O OD1   . ASN B  1 220 ? -18.732 -13.566 -15.537 1.00 75.51 ? 220 ASN D OD1   1 
ATOM   4586  N ND2   . ASN B  1 220 ? -20.662 -14.687 -15.762 1.00 72.02 ? 220 ASN D ND2   1 
ATOM   4587  N N     . ASP B  1 221 ? -16.372 -15.836 -17.924 1.00 69.89 ? 221 ASP D N     1 
ATOM   4588  C CA    . ASP B  1 221 ? -15.310 -16.690 -17.417 1.00 71.12 ? 221 ASP D CA    1 
ATOM   4589  C C     . ASP B  1 221 ? -13.923 -16.104 -17.616 1.00 68.08 ? 221 ASP D C     1 
ATOM   4590  O O     . ASP B  1 221 ? -12.958 -16.617 -17.035 1.00 67.83 ? 221 ASP D O     1 
ATOM   4591  C CB    . ASP B  1 221 ? -15.434 -18.037 -18.127 1.00 79.55 ? 221 ASP D CB    1 
ATOM   4592  C CG    . ASP B  1 221 ? -16.334 -17.952 -19.367 1.00 85.83 ? 221 ASP D CG    1 
ATOM   4593  O OD1   . ASP B  1 221 ? -16.342 -16.880 -20.015 1.00 86.54 ? 221 ASP D OD1   1 
ATOM   4594  O OD2   . ASP B  1 221 ? -17.041 -18.937 -19.690 1.00 84.62 ? 221 ASP D OD2   1 
ATOM   4595  N N     . GLN B  1 222 ? -13.793 -15.061 -18.430 1.00 66.48 ? 222 GLN D N     1 
ATOM   4596  C CA    . GLN B  1 222 ? -12.498 -14.433 -18.702 1.00 71.28 ? 222 GLN D CA    1 
ATOM   4597  C C     . GLN B  1 222 ? -12.734 -12.930 -18.808 1.00 64.15 ? 222 GLN D C     1 
ATOM   4598  O O     . GLN B  1 222 ? -12.969 -12.395 -19.899 1.00 70.77 ? 222 GLN D O     1 
ATOM   4599  C CB    . GLN B  1 222 ? -11.845 -14.985 -19.967 1.00 77.12 ? 222 GLN D CB    1 
ATOM   4600  C CG    . GLN B  1 222 ? -12.819 -15.496 -21.012 1.00 73.12 ? 222 GLN D CG    1 
ATOM   4601  C CD    . GLN B  1 222 ? -12.153 -15.821 -22.332 1.00 69.89 ? 222 GLN D CD    1 
ATOM   4602  O OE1   . GLN B  1 222 ? -11.072 -16.415 -22.372 1.00 71.83 ? 222 GLN D OE1   1 
ATOM   4603  N NE2   . GLN B  1 222 ? -12.798 -15.424 -23.427 1.00 67.91 ? 222 GLN D NE2   1 
ATOM   4604  N N     . LEU B  1 223 ? -12.681 -12.253 -17.674 1.00 61.96 ? 223 LEU D N     1 
ATOM   4605  C CA    . LEU B  1 223 ? -12.718 -10.801 -17.668 1.00 65.27 ? 223 LEU D CA    1 
ATOM   4606  C C     . LEU B  1 223 ? -11.502 -10.179 -17.006 1.00 62.43 ? 223 LEU D C     1 
ATOM   4607  O O     . LEU B  1 223 ? -11.066 -9.114  -17.445 1.00 58.96 ? 223 LEU D O     1 
ATOM   4608  C CB    . LEU B  1 223 ? -13.993 -10.300 -16.970 1.00 67.85 ? 223 LEU D CB    1 
ATOM   4609  C CG    . LEU B  1 223 ? -15.280 -10.361 -17.793 1.00 72.78 ? 223 LEU D CG    1 
ATOM   4610  C CD1   . LEU B  1 223 ? -16.461 -9.679  -17.067 1.00 65.01 ? 223 LEU D CD1   1 
ATOM   4611  C CD2   . LEU B  1 223 ? -15.062 -9.794  -19.215 1.00 69.80 ? 223 LEU D CD2   1 
ATOM   4612  N N     . ASP B  1 224 ? -10.928 -10.830 -15.982 1.00 65.37 ? 224 ASP D N     1 
ATOM   4613  C CA    . ASP B  1 224 ? -9.602  -10.448 -15.514 1.00 59.88 ? 224 ASP D CA    1 
ATOM   4614  C C     . ASP B  1 224 ? -8.622  -10.431 -16.671 1.00 62.95 ? 224 ASP D C     1 
ATOM   4615  O O     . ASP B  1 224 ? -7.788  -9.524  -16.787 1.00 64.34 ? 224 ASP D O     1 
ATOM   4616  C CB    . ASP B  1 224 ? -9.117  -11.410 -14.425 1.00 61.07 ? 224 ASP D CB    1 
ATOM   4617  C CG    . ASP B  1 224 ? -9.394  -10.891 -13.019 1.00 67.08 ? 224 ASP D CG    1 
ATOM   4618  O OD1   . ASP B  1 224 ? -9.021  -9.729  -12.717 1.00 74.41 ? 224 ASP D OD1   1 
ATOM   4619  O OD2   . ASP B  1 224 ? -9.967  -11.643 -12.205 1.00 63.32 ? 224 ASP D OD2   1 
ATOM   4620  N N     . THR B  1 225 ? -8.701  -11.434 -17.543 1.00 61.15 ? 225 THR D N     1 
ATOM   4621  C CA    . THR B  1 225 ? -7.840  -11.418 -18.717 1.00 59.75 ? 225 THR D CA    1 
ATOM   4622  C C     . THR B  1 225 ? -8.316  -10.374 -19.717 1.00 57.59 ? 225 THR D C     1 
ATOM   4623  O O     . THR B  1 225 ? -7.500  -9.734  -20.388 1.00 60.85 ? 225 THR D O     1 
ATOM   4624  C CB    . THR B  1 225 ? -7.782  -12.809 -19.356 1.00 58.59 ? 225 THR D CB    1 
ATOM   4625  O OG1   . THR B  1 225 ? -8.902  -13.584 -18.907 1.00 61.13 ? 225 THR D OG1   1 
ATOM   4626  C CG2   . THR B  1 225 ? -6.480  -13.525 -18.973 1.00 50.54 ? 225 THR D CG2   1 
ATOM   4627  N N     . LEU B  1 226 ? -9.628  -10.159 -19.790 1.00 58.50 ? 226 LEU D N     1 
ATOM   4628  C CA    . LEU B  1 226 ? -10.187 -9.265  -20.795 1.00 54.51 ? 226 LEU D CA    1 
ATOM   4629  C C     . LEU B  1 226 ? -9.909  -7.800  -20.486 1.00 54.88 ? 226 LEU D C     1 
ATOM   4630  O O     . LEU B  1 226 ? -9.757  -6.993  -21.411 1.00 47.86 ? 226 LEU D O     1 
ATOM   4631  C CB    . LEU B  1 226 ? -11.685 -9.496  -20.901 1.00 55.50 ? 226 LEU D CB    1 
ATOM   4632  C CG    . LEU B  1 226 ? -12.234 -8.984  -22.211 1.00 53.95 ? 226 LEU D CG    1 
ATOM   4633  C CD1   . LEU B  1 226 ? -13.147 -10.034 -22.819 1.00 54.71 ? 226 LEU D CD1   1 
ATOM   4634  C CD2   . LEU B  1 226 ? -12.937 -7.675  -21.941 1.00 46.75 ? 226 LEU D CD2   1 
ATOM   4635  N N     . ALA B  1 227 ? -9.871  -7.430  -19.203 1.00 54.56 ? 227 ALA D N     1 
ATOM   4636  C CA    . ALA B  1 227 ? -9.476  -6.077  -18.827 1.00 52.64 ? 227 ALA D CA    1 
ATOM   4637  C C     . ALA B  1 227 ? -7.967  -5.878  -18.916 1.00 51.92 ? 227 ALA D C     1 
ATOM   4638  O O     . ALA B  1 227 ? -7.508  -4.749  -19.122 1.00 46.02 ? 227 ALA D O     1 
ATOM   4639  C CB    . ALA B  1 227 ? -9.963  -5.759  -17.413 1.00 52.82 ? 227 ALA D CB    1 
ATOM   4640  N N     . ASP B  1 228 ? -7.193  -6.955  -18.748 1.00 56.70 ? 228 ASP D N     1 
ATOM   4641  C CA    . ASP B  1 228 ? -5.750  -6.904  -18.963 1.00 53.30 ? 228 ASP D CA    1 
ATOM   4642  C C     . ASP B  1 228 ? -5.424  -6.396  -20.359 1.00 50.48 ? 228 ASP D C     1 
ATOM   4643  O O     . ASP B  1 228 ? -4.768  -5.361  -20.531 1.00 47.91 ? 228 ASP D O     1 
ATOM   4644  C CB    . ASP B  1 228 ? -5.147  -8.294  -18.762 1.00 61.46 ? 228 ASP D CB    1 
ATOM   4645  C CG    . ASP B  1 228 ? -4.437  -8.435  -17.446 1.00 66.42 ? 228 ASP D CG    1 
ATOM   4646  O OD1   . ASP B  1 228 ? -4.615  -7.552  -16.575 1.00 61.16 ? 228 ASP D OD1   1 
ATOM   4647  O OD2   . ASP B  1 228 ? -3.688  -9.425  -17.296 1.00 74.21 ? 228 ASP D OD2   1 
ATOM   4648  N N     . THR B  1 229 ? -5.872  -7.129  -21.378 1.00 51.33 ? 229 THR D N     1 
ATOM   4649  C CA    . THR B  1 229 ? -5.650  -6.682  -22.742 1.00 50.11 ? 229 THR D CA    1 
ATOM   4650  C C     . THR B  1 229 ? -6.230  -5.293  -22.959 1.00 48.58 ? 229 THR D C     1 
ATOM   4651  O O     . THR B  1 229 ? -5.685  -4.509  -23.744 1.00 47.32 ? 229 THR D O     1 
ATOM   4652  C CB    . THR B  1 229 ? -6.239  -7.700  -23.718 1.00 52.32 ? 229 THR D CB    1 
ATOM   4653  O OG1   . THR B  1 229 ? -6.062  -7.247  -25.066 1.00 55.11 ? 229 THR D OG1   1 
ATOM   4654  C CG2   . THR B  1 229 ? -7.703  -7.932  -23.432 1.00 52.36 ? 229 THR D CG2   1 
ATOM   4655  N N     . LEU B  1 230 ? -7.302  -4.950  -22.239 1.00 51.13 ? 230 LEU D N     1 
ATOM   4656  C CA    . LEU B  1 230 ? -7.840  -3.597  -22.333 1.00 47.82 ? 230 LEU D CA    1 
ATOM   4657  C C     . LEU B  1 230 ? -6.911  -2.594  -21.655 1.00 50.74 ? 230 LEU D C     1 
ATOM   4658  O O     . LEU B  1 230 ? -6.656  -1.508  -22.197 1.00 48.32 ? 230 LEU D O     1 
ATOM   4659  C CB    . LEU B  1 230 ? -9.243  -3.550  -21.732 1.00 48.38 ? 230 LEU D CB    1 
ATOM   4660  C CG    . LEU B  1 230 ? -10.372 -3.731  -22.757 1.00 47.60 ? 230 LEU D CG    1 
ATOM   4661  C CD1   . LEU B  1 230 ? -11.744 -3.772  -22.099 1.00 42.64 ? 230 LEU D CD1   1 
ATOM   4662  C CD2   . LEU B  1 230 ? -10.315 -2.636  -23.808 1.00 42.90 ? 230 LEU D CD2   1 
ATOM   4663  N N     . TRP B  1 231 ? -6.363  -2.954  -20.491 1.00 47.13 ? 231 TRP D N     1 
ATOM   4664  C CA    . TRP B  1 231 ? -5.411  -2.068  -19.828 1.00 43.95 ? 231 TRP D CA    1 
ATOM   4665  C C     . TRP B  1 231 ? -4.171  -1.884  -20.686 1.00 44.93 ? 231 TRP D C     1 
ATOM   4666  O O     . TRP B  1 231 ? -3.887  -0.779  -21.163 1.00 46.30 ? 231 TRP D O     1 
ATOM   4667  C CB    . TRP B  1 231 ? -5.047  -2.609  -18.438 1.00 41.32 ? 231 TRP D CB    1 
ATOM   4668  C CG    . TRP B  1 231 ? -4.242  -1.675  -17.572 1.00 34.16 ? 231 TRP D CG    1 
ATOM   4669  C CD1   . TRP B  1 231 ? -2.966  -1.860  -17.149 1.00 40.44 ? 231 TRP D CD1   1 
ATOM   4670  C CD2   . TRP B  1 231 ? -4.671  -0.431  -17.012 1.00 39.01 ? 231 TRP D CD2   1 
ATOM   4671  N NE1   . TRP B  1 231 ? -2.561  -0.807  -16.371 1.00 43.79 ? 231 TRP D NE1   1 
ATOM   4672  C CE2   . TRP B  1 231 ? -3.592  0.085   -16.265 1.00 40.33 ? 231 TRP D CE2   1 
ATOM   4673  C CE3   . TRP B  1 231 ? -5.862  0.301   -17.069 1.00 42.10 ? 231 TRP D CE3   1 
ATOM   4674  C CZ2   . TRP B  1 231 ? -3.665  1.301   -15.584 1.00 40.97 ? 231 TRP D CZ2   1 
ATOM   4675  C CZ3   . TRP B  1 231 ? -5.935  1.516   -16.399 1.00 40.11 ? 231 TRP D CZ3   1 
ATOM   4676  C CH2   . TRP B  1 231 ? -4.842  2.003   -15.664 1.00 40.93 ? 231 TRP D CH2   1 
ATOM   4677  N N     . SER B  1 232 ? -3.449  -2.974  -20.941 1.00 43.74 ? 232 SER D N     1 
ATOM   4678  C CA    . SER B  1 232 ? -2.139  -2.844  -21.560 1.00 42.68 ? 232 SER D CA    1 
ATOM   4679  C C     . SER B  1 232 ? -2.219  -2.134  -22.906 1.00 44.86 ? 232 SER D C     1 
ATOM   4680  O O     . SER B  1 232 ? -1.300  -1.390  -23.271 1.00 44.34 ? 232 SER D O     1 
ATOM   4681  C CB    . SER B  1 232 ? -1.501  -4.226  -21.702 1.00 49.91 ? 232 SER D CB    1 
ATOM   4682  O OG    . SER B  1 232 ? -0.701  -4.528  -20.562 1.00 51.51 ? 232 SER D OG    1 
ATOM   4683  N N     . GLN B  1 233 ? -3.319  -2.308  -23.640 1.00 45.47 ? 233 GLN D N     1 
ATOM   4684  C CA    . GLN B  1 233 ? -3.351  -1.746  -24.983 1.00 45.44 ? 233 GLN D CA    1 
ATOM   4685  C C     . GLN B  1 233 ? -3.710  -0.263  -24.991 1.00 45.01 ? 233 GLN D C     1 
ATOM   4686  O O     . GLN B  1 233 ? -3.306  0.458   -25.914 1.00 43.49 ? 233 GLN D O     1 
ATOM   4687  C CB    . GLN B  1 233 ? -4.305  -2.545  -25.872 1.00 42.21 ? 233 GLN D CB    1 
ATOM   4688  C CG    . GLN B  1 233 ? -3.727  -3.884  -26.296 1.00 48.73 ? 233 GLN D CG    1 
ATOM   4689  C CD    . GLN B  1 233 ? -4.274  -4.374  -27.637 1.00 59.73 ? 233 GLN D CD    1 
ATOM   4690  O OE1   . GLN B  1 233 ? -4.523  -3.581  -28.552 1.00 50.61 ? 233 GLN D OE1   1 
ATOM   4691  N NE2   . GLN B  1 233 ? -4.482  -5.689  -27.748 1.00 61.44 ? 233 GLN D NE2   1 
ATOM   4692  N N     . LEU B  1 234 ? -4.417  0.230   -23.970 1.00 41.81 ? 234 LEU D N     1 
ATOM   4693  C CA    . LEU B  1 234 ? -4.845  1.627   -23.977 1.00 41.12 ? 234 LEU D CA    1 
ATOM   4694  C C     . LEU B  1 234 ? -4.233  2.467   -22.845 1.00 42.78 ? 234 LEU D C     1 
ATOM   4695  O O     . LEU B  1 234 ? -4.716  3.572   -22.579 1.00 41.03 ? 234 LEU D O     1 
ATOM   4696  C CB    . LEU B  1 234 ? -6.373  1.708   -23.951 1.00 37.13 ? 234 LEU D CB    1 
ATOM   4697  C CG    . LEU B  1 234 ? -7.136  0.862   -24.981 1.00 35.75 ? 234 LEU D CG    1 
ATOM   4698  C CD1   . LEU B  1 234 ? -8.632  1.041   -24.792 1.00 34.30 ? 234 LEU D CD1   1 
ATOM   4699  C CD2   . LEU B  1 234 ? -6.728  1.174   -26.431 1.00 32.70 ? 234 LEU D CD2   1 
ATOM   4700  N N     . THR B  1 235 ? -3.164  1.993   -22.185 1.00 42.40 ? 235 THR D N     1 
ATOM   4701  C CA    . THR B  1 235 ? -2.443  2.789   -21.191 1.00 35.42 ? 235 THR D CA    1 
ATOM   4702  C C     . THR B  1 235 ? -0.955  2.812   -21.499 1.00 34.34 ? 235 THR D C     1 
ATOM   4703  O O     . THR B  1 235 ? -0.383  1.828   -21.971 1.00 35.18 ? 235 THR D O     1 
ATOM   4704  C CB    . THR B  1 235 ? -2.587  2.255   -19.757 1.00 37.61 ? 235 THR D CB    1 
ATOM   4705  O OG1   . THR B  1 235 ? -1.844  1.040   -19.621 1.00 33.71 ? 235 THR D OG1   1 
ATOM   4706  C CG2   . THR B  1 235 ? -4.037  2.010   -19.409 1.00 37.75 ? 235 THR D CG2   1 
ATOM   4707  N N     . ASP B  1 236 ? -0.319  3.936   -21.183 1.00 38.68 ? 236 ASP D N     1 
ATOM   4708  C CA    . ASP B  1 236 ? 1.135   4.019   -21.250 1.00 33.68 ? 236 ASP D CA    1 
ATOM   4709  C C     . ASP B  1 236 ? 1.652   4.793   -20.044 1.00 37.51 ? 236 ASP D C     1 
ATOM   4710  O O     . ASP B  1 236 ? 1.063   4.741   -18.961 1.00 39.80 ? 236 ASP D O     1 
ATOM   4711  C CB    . ASP B  1 236 ? 1.567   4.651   -22.568 1.00 32.08 ? 236 ASP D CB    1 
ATOM   4712  C CG    . ASP B  1 236 ? 0.850   5.947   -22.851 1.00 40.60 ? 236 ASP D CG    1 
ATOM   4713  O OD1   . ASP B  1 236 ? 1.107   6.921   -22.123 1.00 45.72 ? 236 ASP D OD1   1 
ATOM   4714  O OD2   . ASP B  1 236 ? 0.009   5.999   -23.778 1.00 40.40 ? 236 ASP D OD2   1 
ATOM   4715  N N     . THR B  1 237 ? 2.754   5.514   -20.209 1.00 37.97 ? 237 THR D N     1 
ATOM   4716  C CA    . THR B  1 237 ? 3.359   6.163   -19.054 1.00 36.12 ? 237 THR D CA    1 
ATOM   4717  C C     . THR B  1 237 ? 2.665   7.466   -18.704 1.00 38.72 ? 237 THR D C     1 
ATOM   4718  O O     . THR B  1 237 ? 2.548   7.809   -17.522 1.00 42.90 ? 237 THR D O     1 
ATOM   4719  C CB    . THR B  1 237 ? 4.839   6.415   -19.319 1.00 38.29 ? 237 THR D CB    1 
ATOM   4720  O OG1   . THR B  1 237 ? 5.522   5.154   -19.412 1.00 43.67 ? 237 THR D OG1   1 
ATOM   4721  C CG2   . THR B  1 237 ? 5.452   7.272   -18.211 1.00 36.11 ? 237 THR D CG2   1 
ATOM   4722  N N     . GLN B  1 238 ? 2.193   8.189   -19.709 1.00 40.67 ? 238 GLN D N     1 
ATOM   4723  C CA    . GLN B  1 238 ? 1.509   9.461   -19.515 1.00 45.29 ? 238 GLN D CA    1 
ATOM   4724  C C     . GLN B  1 238 ? 0.003   9.309   -19.361 1.00 41.84 ? 238 GLN D C     1 
ATOM   4725  O O     . GLN B  1 238 ? -0.642  10.204  -18.804 1.00 42.18 ? 238 GLN D O     1 
ATOM   4726  C CB    . GLN B  1 238 ? 1.796   10.393  -20.701 1.00 36.60 ? 238 GLN D CB    1 
ATOM   4727  C CG    . GLN B  1 238 ? 3.281   10.578  -21.001 1.00 40.65 ? 238 GLN D CG    1 
ATOM   4728  C CD    . GLN B  1 238 ? 3.901   9.395   -21.757 1.00 43.54 ? 238 GLN D CD    1 
ATOM   4729  O OE1   . GLN B  1 238 ? 3.239   8.700   -22.553 1.00 40.68 ? 238 GLN D OE1   1 
ATOM   4730  N NE2   . GLN B  1 238 ? 5.176   9.146   -21.482 1.00 42.91 ? 238 GLN D NE2   1 
ATOM   4731  N N     . ASN B  1 239 ? -0.557  8.211   -19.848 1.00 37.99 ? 239 ASN D N     1 
ATOM   4732  C CA    . ASN B  1 239 ? -1.989  7.965   -19.862 1.00 38.97 ? 239 ASN D CA    1 
ATOM   4733  C C     . ASN B  1 239 ? -2.294  6.784   -18.946 1.00 39.86 ? 239 ASN D C     1 
ATOM   4734  O O     . ASN B  1 239 ? -2.133  5.632   -19.356 1.00 40.65 ? 239 ASN D O     1 
ATOM   4735  C CB    . ASN B  1 239 ? -2.457  7.668   -21.276 1.00 43.97 ? 239 ASN D CB    1 
ATOM   4736  C CG    . ASN B  1 239 ? -2.235  8.820   -22.221 1.00 43.80 ? 239 ASN D CG    1 
ATOM   4737  O OD1   . ASN B  1 239 ? -3.074  9.711   -22.328 1.00 43.52 ? 239 ASN D OD1   1 
ATOM   4738  N ND2   . ASN B  1 239 ? -1.105  8.807   -22.924 1.00 43.68 ? 239 ASN D ND2   1 
ATOM   4739  N N     . GLN B  1 240 ? -2.768  7.070   -17.724 1.00 37.62 ? 240 GLN D N     1 
ATOM   4740  C CA    . GLN B  1 240 ? -3.123  6.051   -16.735 1.00 37.41 ? 240 GLN D CA    1 
ATOM   4741  C C     . GLN B  1 240 ? -4.615  6.084   -16.385 1.00 40.71 ? 240 GLN D C     1 
ATOM   4742  O O     . GLN B  1 240 ? -5.024  5.554   -15.338 1.00 38.70 ? 240 GLN D O     1 
ATOM   4743  C CB    . GLN B  1 240 ? -2.271  6.209   -15.460 1.00 30.48 ? 240 GLN D CB    1 
ATOM   4744  C CG    . GLN B  1 240 ? -1.976  4.916   -14.687 1.00 40.19 ? 240 GLN D CG    1 
ATOM   4745  C CD    . GLN B  1 240 ? -0.891  4.054   -15.346 1.00 43.65 ? 240 GLN D CD    1 
ATOM   4746  O OE1   . GLN B  1 240 ? -0.986  2.816   -15.377 1.00 39.70 ? 240 GLN D OE1   1 
ATOM   4747  N NE2   . GLN B  1 240 ? 0.138   4.709   -15.880 1.00 36.31 ? 240 GLN D NE2   1 
ATOM   4748  N N     . PHE B  1 241 ? -5.434  6.715   -17.225 1.00 37.53 ? 241 PHE D N     1 
ATOM   4749  C CA    . PHE B  1 241 ? -6.889  6.721   -17.079 1.00 42.56 ? 241 PHE D CA    1 
ATOM   4750  C C     . PHE B  1 241 ? -7.511  6.043   -18.298 1.00 44.44 ? 241 PHE D C     1 
ATOM   4751  O O     . PHE B  1 241 ? -7.127  6.331   -19.442 1.00 38.11 ? 241 PHE D O     1 
ATOM   4752  C CB    . PHE B  1 241 ? -7.445  8.148   -16.955 1.00 36.96 ? 241 PHE D CB    1 
ATOM   4753  C CG    . PHE B  1 241 ? -7.321  8.746   -15.592 1.00 42.22 ? 241 PHE D CG    1 
ATOM   4754  C CD1   . PHE B  1 241 ? -7.815  8.081   -14.475 1.00 45.51 ? 241 PHE D CD1   1 
ATOM   4755  C CD2   . PHE B  1 241 ? -6.724  9.987   -15.423 1.00 35.61 ? 241 PHE D CD2   1 
ATOM   4756  C CE1   . PHE B  1 241 ? -7.705  8.641   -13.204 1.00 37.01 ? 241 PHE D CE1   1 
ATOM   4757  C CE2   . PHE B  1 241 ? -6.606  10.550  -14.159 1.00 33.83 ? 241 PHE D CE2   1 
ATOM   4758  C CZ    . PHE B  1 241 ? -7.101  9.883   -13.049 1.00 37.08 ? 241 PHE D CZ    1 
ATOM   4759  N N     . ILE B  1 242 ? -8.475  5.157   -18.070 1.00 35.14 ? 242 ILE D N     1 
ATOM   4760  C CA    . ILE B  1 242 ? -9.250  4.598   -19.167 1.00 38.17 ? 242 ILE D CA    1 
ATOM   4761  C C     . ILE B  1 242 ? -10.707 4.914   -18.917 1.00 37.06 ? 242 ILE D C     1 
ATOM   4762  O O     . ILE B  1 242 ? -11.158 4.922   -17.769 1.00 42.29 ? 242 ILE D O     1 
ATOM   4763  C CB    . ILE B  1 242 ? -9.035  3.083   -19.342 1.00 38.90 ? 242 ILE D CB    1 
ATOM   4764  C CG1   . ILE B  1 242 ? -7.868  2.843   -20.278 1.00 40.73 ? 242 ILE D CG1   1 
ATOM   4765  C CG2   . ILE B  1 242 ? -10.252 2.405   -19.939 1.00 37.56 ? 242 ILE D CG2   1 
ATOM   4766  C CD1   . ILE B  1 242 ? -7.597  1.375   -20.508 1.00 47.12 ? 242 ILE D CD1   1 
ATOM   4767  N N     . THR B  1 243 ? -11.429 5.215   -19.984 1.00 32.07 ? 243 THR D N     1 
ATOM   4768  C CA    . THR B  1 243 ? -12.862 5.397   -19.914 1.00 31.78 ? 243 THR D CA    1 
ATOM   4769  C C     . THR B  1 243 ? -13.520 4.145   -20.452 1.00 33.28 ? 243 THR D C     1 
ATOM   4770  O O     . THR B  1 243 ? -13.044 3.561   -21.429 1.00 39.66 ? 243 THR D O     1 
ATOM   4771  C CB    . THR B  1 243 ? -13.297 6.597   -20.740 1.00 35.89 ? 243 THR D CB    1 
ATOM   4772  O OG1   . THR B  1 243 ? -12.566 6.591   -21.978 1.00 41.33 ? 243 THR D OG1   1 
ATOM   4773  C CG2   . THR B  1 243 ? -13.017 7.881   -19.987 1.00 28.13 ? 243 THR D CG2   1 
ATOM   4774  N N     . VAL B  1 244 ? -14.611 3.736   -19.817 1.00 31.89 ? 244 VAL D N     1 
ATOM   4775  C CA    . VAL B  1 244 ? -15.397 2.602   -20.285 1.00 35.73 ? 244 VAL D CA    1 
ATOM   4776  C C     . VAL B  1 244 ? -16.878 2.969   -20.207 1.00 35.49 ? 244 VAL D C     1 
ATOM   4777  O O     . VAL B  1 244 ? -17.389 3.271   -19.124 1.00 36.29 ? 244 VAL D O     1 
ATOM   4778  C CB    . VAL B  1 244 ? -15.087 1.322   -19.487 1.00 39.63 ? 244 VAL D CB    1 
ATOM   4779  C CG1   . VAL B  1 244 ? -16.075 0.223   -19.825 1.00 39.26 ? 244 VAL D CG1   1 
ATOM   4780  C CG2   . VAL B  1 244 ? -13.660 0.848   -19.776 1.00 38.61 ? 244 VAL D CG2   1 
ATOM   4781  N N     . GLU B  1 245 ? -17.563 2.955   -21.357 1.00 40.28 ? 245 GLU D N     1 
ATOM   4782  C CA    . GLU B  1 245 ? -18.930 3.451   -21.460 1.00 42.07 ? 245 GLU D CA    1 
ATOM   4783  C C     . GLU B  1 245 ? -19.863 2.403   -22.034 1.00 38.91 ? 245 GLU D C     1 
ATOM   4784  O O     . GLU B  1 245 ? -19.455 1.521   -22.796 1.00 35.92 ? 245 GLU D O     1 
ATOM   4785  C CB    . GLU B  1 245 ? -19.038 4.691   -22.355 1.00 35.96 ? 245 GLU D CB    1 
ATOM   4786  C CG    . GLU B  1 245 ? -18.205 5.834   -21.906 1.00 34.27 ? 245 GLU D CG    1 
ATOM   4787  C CD    . GLU B  1 245 ? -18.167 6.933   -22.922 1.00 38.88 ? 245 GLU D CD    1 
ATOM   4788  O OE1   . GLU B  1 245 ? -19.049 6.961   -23.816 1.00 42.57 ? 245 GLU D OE1   1 
ATOM   4789  O OE2   . GLU B  1 245 ? -17.249 7.773   -22.822 1.00 42.86 ? 245 GLU D OE2   1 
ATOM   4790  N N     . THR B  1 246 ? -21.127 2.540   -21.671 1.00 32.43 ? 246 THR D N     1 
ATOM   4791  C CA    . THR B  1 246 ? -22.171 1.872   -22.411 1.00 37.25 ? 246 THR D CA    1 
ATOM   4792  C C     . THR B  1 246 ? -22.184 2.394   -23.833 1.00 43.56 ? 246 THR D C     1 
ATOM   4793  O O     . THR B  1 246 ? -22.431 3.585   -24.067 1.00 41.92 ? 246 THR D O     1 
ATOM   4794  C CB    . THR B  1 246 ? -23.517 2.119   -21.755 1.00 39.35 ? 246 THR D CB    1 
ATOM   4795  O OG1   . THR B  1 246 ? -23.388 1.918   -20.347 1.00 40.72 ? 246 THR D OG1   1 
ATOM   4796  C CG2   . THR B  1 246 ? -24.550 1.168   -22.330 1.00 40.80 ? 246 THR D CG2   1 
ATOM   4797  N N     . TYR B  1 247 ? -21.904 1.509   -24.778 1.00 37.34 ? 247 TYR D N     1 
ATOM   4798  C CA    . TYR B  1 247 ? -22.107 1.841   -26.173 1.00 40.29 ? 247 TYR D CA    1 
ATOM   4799  C C     . TYR B  1 247 ? -23.587 1.755   -26.508 1.00 41.49 ? 247 TYR D C     1 
ATOM   4800  O O     . TYR B  1 247 ? -24.254 0.763   -26.197 1.00 43.33 ? 247 TYR D O     1 
ATOM   4801  C CB    . TYR B  1 247 ? -21.307 0.904   -27.072 1.00 39.18 ? 247 TYR D CB    1 
ATOM   4802  C CG    . TYR B  1 247 ? -21.028 1.506   -28.413 1.00 38.46 ? 247 TYR D CG    1 
ATOM   4803  C CD1   . TYR B  1 247 ? -20.375 2.727   -28.521 1.00 42.17 ? 247 TYR D CD1   1 
ATOM   4804  C CD2   . TYR B  1 247 ? -21.434 0.869   -29.580 1.00 42.09 ? 247 TYR D CD2   1 
ATOM   4805  C CE1   . TYR B  1 247 ? -20.117 3.297   -29.765 1.00 45.29 ? 247 TYR D CE1   1 
ATOM   4806  C CE2   . TYR B  1 247 ? -21.180 1.428   -30.826 1.00 43.37 ? 247 TYR D CE2   1 
ATOM   4807  C CZ    . TYR B  1 247 ? -20.523 2.638   -30.910 1.00 41.27 ? 247 TYR D CZ    1 
ATOM   4808  O OH    . TYR B  1 247 ? -20.281 3.200   -32.141 1.00 41.25 ? 247 TYR D OH    1 
ATOM   4809  N N     . HIS B  1 248 ? -24.096 2.799   -27.142 1.00 49.47 ? 248 HIS D N     1 
ATOM   4810  C CA    . HIS B  1 248 ? -25.473 2.848   -27.611 1.00 49.95 ? 248 HIS D CA    1 
ATOM   4811  C C     . HIS B  1 248 ? -25.503 2.891   -29.132 1.00 45.22 ? 248 HIS D C     1 
ATOM   4812  O O     . HIS B  1 248 ? -24.720 3.618   -29.752 1.00 45.56 ? 248 HIS D O     1 
ATOM   4813  C CB    . HIS B  1 248 ? -26.189 4.077   -27.057 1.00 46.42 ? 248 HIS D CB    1 
ATOM   4814  C CG    . HIS B  1 248 ? -26.402 4.041   -25.577 1.00 49.04 ? 248 HIS D CG    1 
ATOM   4815  N ND1   . HIS B  1 248 ? -25.431 4.419   -24.672 1.00 54.20 ? 248 HIS D ND1   1 
ATOM   4816  C CD2   . HIS B  1 248 ? -27.484 3.689   -24.841 1.00 50.49 ? 248 HIS D CD2   1 
ATOM   4817  C CE1   . HIS B  1 248 ? -25.903 4.296   -23.442 1.00 47.35 ? 248 HIS D CE1   1 
ATOM   4818  N NE2   . HIS B  1 248 ? -27.147 3.856   -23.518 1.00 45.69 ? 248 HIS D NE2   1 
ATOM   4819  N N     . ARG B  1 249 ? -26.398 2.105   -29.731 1.00 49.76 ? 249 ARG D N     1 
ATOM   4820  C CA    . ARG B  1 249 ? -26.683 2.246   -31.156 1.00 47.66 ? 249 ARG D CA    1 
ATOM   4821  C C     . ARG B  1 249 ? -27.418 3.563   -31.379 1.00 50.00 ? 249 ARG D C     1 
ATOM   4822  O O     . ARG B  1 249 ? -28.481 3.792   -30.795 1.00 52.77 ? 249 ARG D O     1 
ATOM   4823  C CB    . ARG B  1 249 ? -27.516 1.063   -31.650 1.00 43.67 ? 249 ARG D CB    1 
ATOM   4824  C CG    . ARG B  1 249 ? -27.699 0.974   -33.174 1.00 56.00 ? 249 ARG D CG    1 
ATOM   4825  C CD    . ARG B  1 249 ? -28.890 1.810   -33.697 1.00 54.43 ? 249 ARG D CD    1 
ATOM   4826  N NE    . ARG B  1 249 ? -30.189 1.202   -33.408 1.00 56.62 ? 249 ARG D NE    1 
ATOM   4827  C CZ    . ARG B  1 249 ? -31.268 1.875   -33.021 1.00 58.22 ? 249 ARG D CZ    1 
ATOM   4828  N NH1   . ARG B  1 249 ? -31.260 3.195   -32.907 1.00 58.44 ? 249 ARG D NH1   1 
ATOM   4829  N NH2   . ARG B  1 249 ? -32.388 1.208   -32.746 1.00 51.84 ? 249 ARG D NH2   1 
ATOM   4830  N N     . ALA B  1 250 ? -26.858 4.433   -32.207 1.00 47.14 ? 250 ALA D N     1 
ATOM   4831  C CA    . ALA B  1 250 ? -27.386 5.777   -32.378 1.00 47.26 ? 250 ALA D CA    1 
ATOM   4832  C C     . ALA B  1 250 ? -28.070 5.916   -33.728 1.00 51.87 ? 250 ALA D C     1 
ATOM   4833  O O     . ALA B  1 250 ? -27.662 5.297   -34.718 1.00 44.57 ? 250 ALA D O     1 
ATOM   4834  C CB    . ALA B  1 250 ? -26.278 6.828   -32.259 1.00 47.14 ? 250 ALA D CB    1 
ATOM   4835  N N     . ASP B  1 251 ? -29.121 6.742   -33.755 1.00 50.02 ? 251 ASP D N     1 
ATOM   4836  C CA    . ASP B  1 251 ? -29.756 7.120   -35.011 1.00 51.92 ? 251 ASP D CA    1 
ATOM   4837  C C     . ASP B  1 251 ? -29.082 8.312   -35.673 1.00 52.81 ? 251 ASP D C     1 
ATOM   4838  O O     . ASP B  1 251 ? -29.263 8.526   -36.880 1.00 50.12 ? 251 ASP D O     1 
ATOM   4839  C CB    . ASP B  1 251 ? -31.237 7.443   -34.791 1.00 50.27 ? 251 ASP D CB    1 
ATOM   4840  C CG    . ASP B  1 251 ? -31.947 7.839   -36.082 1.00 54.87 ? 251 ASP D CG    1 
ATOM   4841  O OD1   . ASP B  1 251 ? -32.153 6.954   -36.948 1.00 51.25 ? 251 ASP D OD1   1 
ATOM   4842  O OD2   . ASP B  1 251 ? -32.284 9.036   -36.230 1.00 54.97 ? 251 ASP D OD2   1 
ATOM   4843  N N     . GLN B  1 252 ? -28.316 9.090   -34.914 1.00 50.46 ? 252 GLN D N     1 
ATOM   4844  C CA    . GLN B  1 252 ? -27.620 10.249  -35.445 1.00 43.86 ? 252 GLN D CA    1 
ATOM   4845  C C     . GLN B  1 252 ? -26.276 10.322  -34.754 1.00 43.11 ? 252 GLN D C     1 
ATOM   4846  O O     . GLN B  1 252 ? -26.214 10.382  -33.525 1.00 43.93 ? 252 GLN D O     1 
ATOM   4847  C CB    . GLN B  1 252 ? -28.427 11.530  -35.222 1.00 46.78 ? 252 GLN D CB    1 
ATOM   4848  C CG    . GLN B  1 252 ? -29.478 11.773  -36.301 1.00 54.72 ? 252 GLN D CG    1 
ATOM   4849  C CD    . GLN B  1 252 ? -28.896 11.763  -37.724 1.00 55.71 ? 252 GLN D CD    1 
ATOM   4850  O OE1   . GLN B  1 252 ? -27.876 12.401  -38.005 1.00 49.03 ? 252 GLN D OE1   1 
ATOM   4851  N NE2   . GLN B  1 252 ? -29.551 11.031  -38.622 1.00 56.42 ? 252 GLN D NE2   1 
ATOM   4852  N N     . ARG B  1 253 ? -25.214 10.277  -35.529 1.00 41.09 ? 253 ARG D N     1 
ATOM   4853  C CA    . ARG B  1 253 ? -23.866 10.411  -35.012 1.00 35.53 ? 253 ARG D CA    1 
ATOM   4854  C C     . ARG B  1 253 ? -23.358 11.735  -35.552 1.00 36.02 ? 253 ARG D C     1 
ATOM   4855  O O     . ARG B  1 253 ? -23.058 11.851  -36.743 1.00 38.84 ? 253 ARG D O     1 
ATOM   4856  C CB    . ARG B  1 253 ? -23.018 9.236   -35.450 1.00 33.25 ? 253 ARG D CB    1 
ATOM   4857  C CG    . ARG B  1 253 ? -23.643 7.919   -35.061 1.00 35.03 ? 253 ARG D CG    1 
ATOM   4858  C CD    . ARG B  1 253 ? -22.557 6.850   -34.805 1.00 42.09 ? 253 ARG D CD    1 
ATOM   4859  N NE    . ARG B  1 253 ? -22.974 5.825   -33.848 1.00 43.44 ? 253 ARG D NE    1 
ATOM   4860  C CZ    . ARG B  1 253 ? -22.204 5.309   -32.899 1.00 41.66 ? 253 ARG D CZ    1 
ATOM   4861  N NH1   . ARG B  1 253 ? -20.952 5.712   -32.723 1.00 39.56 ? 253 ARG D NH1   1 
ATOM   4862  N NH2   . ARG B  1 253 ? -22.699 4.359   -32.112 1.00 40.45 ? 253 ARG D NH2   1 
ATOM   4863  N N     . PHE B  1 254 ? -23.290 12.737  -34.678 1.00 33.23 ? 254 PHE D N     1 
ATOM   4864  C CA    . PHE B  1 254 ? -23.038 14.115  -35.080 1.00 35.83 ? 254 PHE D CA    1 
ATOM   4865  C C     . PHE B  1 254 ? -22.001 14.759  -34.167 1.00 36.48 ? 254 PHE D C     1 
ATOM   4866  O O     . PHE B  1 254 ? -21.538 14.162  -33.189 1.00 34.77 ? 254 PHE D O     1 
ATOM   4867  C CB    . PHE B  1 254 ? -24.320 14.942  -35.028 1.00 35.65 ? 254 PHE D CB    1 
ATOM   4868  C CG    . PHE B  1 254 ? -24.710 15.334  -33.631 1.00 39.37 ? 254 PHE D CG    1 
ATOM   4869  C CD1   . PHE B  1 254 ? -25.194 14.381  -32.749 1.00 36.52 ? 254 PHE D CD1   1 
ATOM   4870  C CD2   . PHE B  1 254 ? -24.574 16.640  -33.195 1.00 37.11 ? 254 PHE D CD2   1 
ATOM   4871  C CE1   . PHE B  1 254 ? -25.535 14.718  -31.479 1.00 36.24 ? 254 PHE D CE1   1 
ATOM   4872  C CE2   . PHE B  1 254 ? -24.923 16.986  -31.910 1.00 37.48 ? 254 PHE D CE2   1 
ATOM   4873  C CZ    . PHE B  1 254 ? -25.396 16.028  -31.053 1.00 40.76 ? 254 PHE D CZ    1 
ATOM   4874  N N     . PHE B  1 255 ? -21.658 16.008  -34.493 1.00 34.96 ? 255 PHE D N     1 
ATOM   4875  C CA    . PHE B  1 255 ? -20.817 16.855  -33.659 1.00 31.90 ? 255 PHE D CA    1 
ATOM   4876  C C     . PHE B  1 255 ? -21.001 18.291  -34.114 1.00 31.45 ? 255 PHE D C     1 
ATOM   4877  O O     . PHE B  1 255 ? -21.530 18.551  -35.190 1.00 32.07 ? 255 PHE D O     1 
ATOM   4878  C CB    . PHE B  1 255 ? -19.345 16.436  -33.706 1.00 32.30 ? 255 PHE D CB    1 
ATOM   4879  C CG    . PHE B  1 255 ? -18.552 17.060  -34.818 1.00 37.08 ? 255 PHE D CG    1 
ATOM   4880  C CD1   . PHE B  1 255 ? -18.016 18.335  -34.690 1.00 35.29 ? 255 PHE D CD1   1 
ATOM   4881  C CD2   . PHE B  1 255 ? -18.294 16.350  -35.973 1.00 36.72 ? 255 PHE D CD2   1 
ATOM   4882  C CE1   . PHE B  1 255 ? -17.286 18.897  -35.698 1.00 33.89 ? 255 PHE D CE1   1 
ATOM   4883  C CE2   . PHE B  1 255 ? -17.540 16.906  -36.991 1.00 39.25 ? 255 PHE D CE2   1 
ATOM   4884  C CZ    . PHE B  1 255 ? -17.039 18.179  -36.857 1.00 40.51 ? 255 PHE D CZ    1 
ATOM   4885  N N     . PHE B  1 256 ? -20.571 19.218  -33.264 1.00 35.71 ? 256 PHE D N     1 
ATOM   4886  C CA    . PHE B  1 256 ? -20.706 20.658  -33.470 1.00 34.73 ? 256 PHE D CA    1 
ATOM   4887  C C     . PHE B  1 256 ? -19.326 21.277  -33.324 1.00 34.52 ? 256 PHE D C     1 
ATOM   4888  O O     . PHE B  1 256 ? -18.620 20.980  -32.360 1.00 33.34 ? 256 PHE D O     1 
ATOM   4889  C CB    . PHE B  1 256 ? -21.647 21.324  -32.408 1.00 32.74 ? 256 PHE D CB    1 
ATOM   4890  C CG    . PHE B  1 256 ? -23.088 20.840  -32.422 1.00 35.54 ? 256 PHE D CG    1 
ATOM   4891  C CD1   . PHE B  1 256 ? -23.665 20.295  -33.565 1.00 38.52 ? 256 PHE D CD1   1 
ATOM   4892  C CD2   . PHE B  1 256 ? -23.879 20.976  -31.290 1.00 35.24 ? 256 PHE D CD2   1 
ATOM   4893  C CE1   . PHE B  1 256 ? -24.994 19.882  -33.574 1.00 33.77 ? 256 PHE D CE1   1 
ATOM   4894  C CE2   . PHE B  1 256 ? -25.214 20.552  -31.285 1.00 36.97 ? 256 PHE D CE2   1 
ATOM   4895  C CZ    . PHE B  1 256 ? -25.768 20.012  -32.431 1.00 37.27 ? 256 PHE D CZ    1 
ATOM   4896  N N     . GLU B  1 257 ? -18.937 22.158  -34.232 1.00 31.80 ? 257 GLU D N     1 
ATOM   4897  C CA    . GLU B  1 257 ? -17.646 22.825  -34.100 1.00 32.60 ? 257 GLU D CA    1 
ATOM   4898  C C     . GLU B  1 257 ? -17.849 24.310  -33.836 1.00 28.86 ? 257 GLU D C     1 
ATOM   4899  O O     . GLU B  1 257 ? -18.730 24.940  -34.428 1.00 29.91 ? 257 GLU D O     1 
ATOM   4900  C CB    . GLU B  1 257 ? -16.765 22.623  -35.344 1.00 32.89 ? 257 GLU D CB    1 
ATOM   4901  C CG    . GLU B  1 257 ? -15.386 23.236  -35.204 1.00 30.96 ? 257 GLU D CG    1 
ATOM   4902  C CD    . GLU B  1 257 ? -14.338 22.586  -36.083 1.00 29.01 ? 257 GLU D CD    1 
ATOM   4903  O OE1   . GLU B  1 257 ? -14.691 22.143  -37.194 1.00 23.81 ? 257 GLU D OE1   1 
ATOM   4904  O OE2   . GLU B  1 257 ? -13.158 22.517  -35.663 1.00 31.92 ? 257 GLU D OE2   1 
ATOM   4905  N N     . TYR B  1 258 ? -17.007 24.858  -32.967 1.00 26.70 ? 258 TYR D N     1 
ATOM   4906  C CA    . TYR B  1 258 ? -17.146 26.209  -32.451 1.00 29.43 ? 258 TYR D CA    1 
ATOM   4907  C C     . TYR B  1 258 ? -15.860 26.983  -32.680 1.00 32.26 ? 258 TYR D C     1 
ATOM   4908  O O     . TYR B  1 258 ? -14.798 26.402  -32.926 1.00 31.38 ? 258 TYR D O     1 
ATOM   4909  C CB    . TYR B  1 258 ? -17.470 26.206  -30.945 1.00 30.25 ? 258 TYR D CB    1 
ATOM   4910  C CG    . TYR B  1 258 ? -18.824 25.602  -30.614 1.00 31.19 ? 258 TYR D CG    1 
ATOM   4911  C CD1   . TYR B  1 258 ? -18.972 24.238  -30.421 1.00 29.19 ? 258 TYR D CD1   1 
ATOM   4912  C CD2   . TYR B  1 258 ? -19.952 26.398  -30.509 1.00 32.81 ? 258 TYR D CD2   1 
ATOM   4913  C CE1   . TYR B  1 258 ? -20.201 23.689  -30.136 1.00 33.37 ? 258 TYR D CE1   1 
ATOM   4914  C CE2   . TYR B  1 258 ? -21.183 25.856  -30.221 1.00 32.98 ? 258 TYR D CE2   1 
ATOM   4915  C CZ    . TYR B  1 258 ? -21.308 24.498  -30.035 1.00 34.04 ? 258 TYR D CZ    1 
ATOM   4916  O OH    . TYR B  1 258 ? -22.549 23.950  -29.739 1.00 35.72 ? 258 TYR D OH    1 
ATOM   4917  N N     . HIS B  1 259 ? -15.961 28.308  -32.590 1.00 34.02 ? 259 HIS D N     1 
ATOM   4918  C CA    . HIS B  1 259 ? -14.788 29.158  -32.453 1.00 35.54 ? 259 HIS D CA    1 
ATOM   4919  C C     . HIS B  1 259 ? -14.920 30.034  -31.216 1.00 31.95 ? 259 HIS D C     1 
ATOM   4920  O O     . HIS B  1 259 ? -15.986 30.600  -30.970 1.00 32.91 ? 259 HIS D O     1 
ATOM   4921  C CB    . HIS B  1 259 ? -14.560 30.055  -33.655 1.00 30.96 ? 259 HIS D CB    1 
ATOM   4922  C CG    . HIS B  1 259 ? -13.347 30.916  -33.502 1.00 33.71 ? 259 HIS D CG    1 
ATOM   4923  N ND1   . HIS B  1 259 ? -13.400 32.194  -32.987 1.00 38.24 ? 259 HIS D ND1   1 
ATOM   4924  C CD2   . HIS B  1 259 ? -12.037 30.655  -33.724 1.00 35.15 ? 259 HIS D CD2   1 
ATOM   4925  C CE1   . HIS B  1 259 ? -12.180 32.698  -32.933 1.00 33.42 ? 259 HIS D CE1   1 
ATOM   4926  N NE2   . HIS B  1 259 ? -11.335 31.785  -33.377 1.00 34.30 ? 259 HIS D NE2   1 
ATOM   4927  N N     . LEU B  1 260 ? -13.812 30.187  -30.475 1.00 32.06 ? 260 LEU D N     1 
ATOM   4928  C CA    . LEU B  1 260 ? -13.801 30.857  -29.176 1.00 35.40 ? 260 LEU D CA    1 
ATOM   4929  C C     . LEU B  1 260 ? -12.782 31.997  -29.121 1.00 34.84 ? 260 LEU D C     1 
ATOM   4930  O O     . LEU B  1 260 ? -11.653 31.863  -29.609 1.00 34.01 ? 260 LEU D O     1 
ATOM   4931  C CB    . LEU B  1 260 ? -13.498 29.858  -28.048 1.00 29.66 ? 260 LEU D CB    1 
ATOM   4932  C CG    . LEU B  1 260 ? -14.665 29.107  -27.401 1.00 32.09 ? 260 LEU D CG    1 
ATOM   4933  C CD1   . LEU B  1 260 ? -15.339 28.162  -28.382 1.00 31.82 ? 260 LEU D CD1   1 
ATOM   4934  C CD2   . LEU B  1 260 ? -14.186 28.351  -26.183 1.00 30.60 ? 260 LEU D CD2   1 
ATOM   4935  N N     . ASP B  1 261 ? -13.200 33.117  -28.515 1.00 36.66 ? 261 ASP D N     1 
ATOM   4936  C CA    . ASP B  1 261 ? -12.346 34.271  -28.208 1.00 37.79 ? 261 ASP D CA    1 
ATOM   4937  C C     . ASP B  1 261 ? -12.780 34.852  -26.861 1.00 38.36 ? 261 ASP D C     1 
ATOM   4938  O O     . ASP B  1 261 ? -13.615 34.282  -26.147 1.00 38.35 ? 261 ASP D O     1 
ATOM   4939  C CB    . ASP B  1 261 ? -12.390 35.343  -29.317 1.00 42.13 ? 261 ASP D CB    1 
ATOM   4940  C CG    . ASP B  1 261 ? -13.804 35.946  -29.535 1.00 45.56 ? 261 ASP D CG    1 
ATOM   4941  O OD1   . ASP B  1 261 ? -14.695 35.817  -28.648 1.00 43.69 ? 261 ASP D OD1   1 
ATOM   4942  O OD2   . ASP B  1 261 ? -14.012 36.573  -30.611 1.00 46.41 ? 261 ASP D OD2   1 
ATOM   4943  N N     . GLY B  1 262 ? -12.225 36.018  -26.522 1.00 39.46 ? 262 GLY D N     1 
ATOM   4944  C CA    . GLY B  1 262 ? -12.520 36.634  -25.237 1.00 41.44 ? 262 GLY D CA    1 
ATOM   4945  C C     . GLY B  1 262 ? -13.928 37.156  -25.080 1.00 40.44 ? 262 GLY D C     1 
ATOM   4946  O O     . GLY B  1 262 ? -14.318 37.586  -23.988 1.00 42.86 ? 262 GLY D O     1 
ATOM   4947  N N     . ASP B  1 263 ? -14.717 37.131  -26.138 1.00 38.84 ? 263 ASP D N     1 
ATOM   4948  C CA    . ASP B  1 263 ? -16.064 37.652  -26.047 1.00 42.63 ? 263 ASP D CA    1 
ATOM   4949  C C     . ASP B  1 263 ? -17.117 36.559  -26.095 1.00 38.38 ? 263 ASP D C     1 
ATOM   4950  O O     . ASP B  1 263 ? -18.013 36.537  -25.250 1.00 37.68 ? 263 ASP D O     1 
ATOM   4951  C CB    . ASP B  1 263 ? -16.282 38.675  -27.167 1.00 44.00 ? 263 ASP D CB    1 
ATOM   4952  C CG    . ASP B  1 263 ? -15.438 39.915  -26.972 1.00 46.18 ? 263 ASP D CG    1 
ATOM   4953  O OD1   . ASP B  1 263 ? -15.093 40.223  -25.803 1.00 45.56 ? 263 ASP D OD1   1 
ATOM   4954  O OD2   . ASP B  1 263 ? -15.104 40.567  -27.983 1.00 48.00 ? 263 ASP D OD2   1 
ATOM   4955  N N     . ARG B  1 264 ? -17.013 35.629  -27.038 1.00 40.18 ? 264 ARG D N     1 
ATOM   4956  C CA    . ARG B  1 264 ? -18.125 34.741  -27.323 1.00 42.71 ? 264 ARG D CA    1 
ATOM   4957  C C     . ARG B  1 264 ? -17.606 33.429  -27.875 1.00 37.70 ? 264 ARG D C     1 
ATOM   4958  O O     . ARG B  1 264 ? -16.420 33.266  -28.161 1.00 33.76 ? 264 ARG D O     1 
ATOM   4959  C CB    . ARG B  1 264 ? -19.104 35.372  -28.323 1.00 43.27 ? 264 ARG D CB    1 
ATOM   4960  C CG    . ARG B  1 264 ? -18.514 35.570  -29.716 1.00 47.14 ? 264 ARG D CG    1 
ATOM   4961  C CD    . ARG B  1 264 ? -19.481 36.315  -30.652 1.00 57.04 ? 264 ARG D CD    1 
ATOM   4962  N NE    . ARG B  1 264 ? -19.458 37.765  -30.474 1.00 53.28 ? 264 ARG D NE    1 
ATOM   4963  C CZ    . ARG B  1 264 ? -20.541 38.532  -30.397 1.00 50.59 ? 264 ARG D CZ    1 
ATOM   4964  N NH1   . ARG B  1 264 ? -21.761 38.028  -30.529 1.00 52.20 ? 264 ARG D NH1   1 
ATOM   4965  N NH2   . ARG B  1 264 ? -20.398 39.838  -30.176 1.00 46.17 ? 264 ARG D NH2   1 
ATOM   4966  N N     . ALA B  1 265 ? -18.530 32.497  -28.030 1.00 38.16 ? 265 ALA D N     1 
ATOM   4967  C CA    . ALA B  1 265 ? -18.301 31.259  -28.755 1.00 36.42 ? 265 ALA D CA    1 
ATOM   4968  C C     . ALA B  1 265 ? -19.246 31.289  -29.949 1.00 39.76 ? 265 ALA D C     1 
ATOM   4969  O O     . ALA B  1 265 ? -20.452 31.093  -29.787 1.00 39.83 ? 265 ALA D O     1 
ATOM   4970  C CB    . ALA B  1 265 ? -18.561 30.052  -27.865 1.00 35.07 ? 265 ALA D CB    1 
ATOM   4971  N N     . ARG B  1 266 ? -18.718 31.572  -31.138 1.00 39.15 ? 266 ARG D N     1 
ATOM   4972  C CA    . ARG B  1 266 ? -19.536 31.542  -32.339 1.00 35.89 ? 266 ARG D CA    1 
ATOM   4973  C C     . ARG B  1 266 ? -19.699 30.092  -32.785 1.00 36.26 ? 266 ARG D C     1 
ATOM   4974  O O     . ARG B  1 266 ? -18.709 29.395  -33.021 1.00 40.39 ? 266 ARG D O     1 
ATOM   4975  C CB    . ARG B  1 266 ? -18.910 32.397  -33.440 1.00 40.85 ? 266 ARG D CB    1 
ATOM   4976  C CG    . ARG B  1 266 ? -19.081 33.910  -33.242 1.00 54.05 ? 266 ARG D CG    1 
ATOM   4977  C CD    . ARG B  1 266 ? -17.958 34.728  -33.925 1.00 56.46 ? 266 ARG D CD    1 
ATOM   4978  N NE    . ARG B  1 266 ? -18.302 36.141  -34.070 1.00 57.36 ? 266 ARG D NE    1 
ATOM   4979  C CZ    . ARG B  1 266 ? -17.492 37.079  -34.550 1.00 58.13 ? 266 ARG D CZ    1 
ATOM   4980  N NH1   . ARG B  1 266 ? -16.259 36.796  -34.949 1.00 54.67 ? 266 ARG D NH1   1 
ATOM   4981  N NH2   . ARG B  1 266 ? -17.931 38.333  -34.636 1.00 53.26 ? 266 ARG D NH2   1 
ATOM   4982  N N     . PHE B  1 267 ? -20.940 29.628  -32.862 1.00 36.94 ? 267 PHE D N     1 
ATOM   4983  C CA    . PHE B  1 267 ? -21.241 28.335  -33.470 1.00 32.40 ? 267 PHE D CA    1 
ATOM   4984  C C     . PHE B  1 267 ? -20.800 28.344  -34.930 1.00 36.52 ? 267 PHE D C     1 
ATOM   4985  O O     . PHE B  1 267 ? -21.274 29.157  -35.732 1.00 35.99 ? 267 PHE D O     1 
ATOM   4986  C CB    . PHE B  1 267 ? -22.748 28.053  -33.344 1.00 35.51 ? 267 PHE D CB    1 
ATOM   4987  C CG    . PHE B  1 267 ? -23.226 26.781  -34.035 1.00 39.91 ? 267 PHE D CG    1 
ATOM   4988  C CD1   . PHE B  1 267 ? -23.179 25.547  -33.383 1.00 40.09 ? 267 PHE D CD1   1 
ATOM   4989  C CD2   . PHE B  1 267 ? -23.765 26.827  -35.311 1.00 34.42 ? 267 PHE D CD2   1 
ATOM   4990  C CE1   . PHE B  1 267 ? -23.630 24.380  -34.013 1.00 38.56 ? 267 PHE D CE1   1 
ATOM   4991  C CE2   . PHE B  1 267 ? -24.217 25.663  -35.939 1.00 37.25 ? 267 PHE D CE2   1 
ATOM   4992  C CZ    . PHE B  1 267 ? -24.154 24.446  -35.293 1.00 35.82 ? 267 PHE D CZ    1 
ATOM   4993  N N     . LEU B  1 268 ? -19.879 27.452  -35.280 1.00 32.78 ? 268 LEU D N     1 
ATOM   4994  C CA    . LEU B  1 268 ? -19.421 27.439  -36.661 1.00 33.71 ? 268 LEU D CA    1 
ATOM   4995  C C     . LEU B  1 268 ? -20.292 26.563  -37.561 1.00 36.52 ? 268 LEU D C     1 
ATOM   4996  O O     . LEU B  1 268 ? -20.739 27.016  -38.615 1.00 35.39 ? 268 LEU D O     1 
ATOM   4997  C CB    . LEU B  1 268 ? -17.973 26.986  -36.711 1.00 32.09 ? 268 LEU D CB    1 
ATOM   4998  C CG    . LEU B  1 268 ? -17.076 27.968  -35.988 1.00 32.38 ? 268 LEU D CG    1 
ATOM   4999  C CD1   . LEU B  1 268 ? -15.630 27.610  -36.261 1.00 33.18 ? 268 LEU D CD1   1 
ATOM   5000  C CD2   . LEU B  1 268 ? -17.388 29.367  -36.447 1.00 28.59 ? 268 LEU D CD2   1 
ATOM   5001  N N     . HIS B  1 269 ? -20.554 25.319  -37.170 1.00 37.45 ? 269 HIS D N     1 
ATOM   5002  C CA    . HIS B  1 269 ? -21.373 24.437  -37.992 1.00 32.55 ? 269 HIS D CA    1 
ATOM   5003  C C     . HIS B  1 269 ? -21.692 23.168  -37.203 1.00 31.89 ? 269 HIS D C     1 
ATOM   5004  O O     . HIS B  1 269 ? -21.336 23.026  -36.030 1.00 38.51 ? 269 HIS D O     1 
ATOM   5005  C CB    . HIS B  1 269 ? -20.666 24.112  -39.310 1.00 33.77 ? 269 HIS D CB    1 
ATOM   5006  C CG    . HIS B  1 269 ? -19.491 23.198  -39.160 1.00 30.01 ? 269 HIS D CG    1 
ATOM   5007  N ND1   . HIS B  1 269 ? -19.593 21.827  -39.272 1.00 27.68 ? 269 HIS D ND1   1 
ATOM   5008  C CD2   . HIS B  1 269 ? -18.188 23.456  -38.899 1.00 29.17 ? 269 HIS D CD2   1 
ATOM   5009  C CE1   . HIS B  1 269 ? -18.403 21.282  -39.097 1.00 29.76 ? 269 HIS D CE1   1 
ATOM   5010  N NE2   . HIS B  1 269 ? -17.535 22.248  -38.859 1.00 30.89 ? 269 HIS D NE2   1 
ATOM   5011  N N     . SER B  1 270 ? -22.391 22.251  -37.868 1.00 35.99 ? 270 SER D N     1 
ATOM   5012  C CA    . SER B  1 270 ? -22.611 20.887  -37.416 1.00 33.83 ? 270 SER D CA    1 
ATOM   5013  C C     . SER B  1 270 ? -22.506 19.963  -38.623 1.00 39.01 ? 270 SER D C     1 
ATOM   5014  O O     . SER B  1 270 ? -22.774 20.372  -39.758 1.00 39.85 ? 270 SER D O     1 
ATOM   5015  C CB    . SER B  1 270 ? -23.973 20.722  -36.741 1.00 34.60 ? 270 SER D CB    1 
ATOM   5016  O OG    . SER B  1 270 ? -24.991 20.413  -37.673 1.00 36.80 ? 270 SER D OG    1 
ATOM   5017  N N     . SER B  1 271 ? -22.098 18.713  -38.378 1.00 44.12 ? 271 SER D N     1 
ATOM   5018  C CA    . SER B  1 271 ? -21.927 17.738  -39.453 1.00 38.10 ? 271 SER D CA    1 
ATOM   5019  C C     . SER B  1 271 ? -22.245 16.349  -38.923 1.00 38.17 ? 271 SER D C     1 
ATOM   5020  O O     . SER B  1 271 ? -22.517 16.165  -37.734 1.00 42.28 ? 271 SER D O     1 
ATOM   5021  C CB    . SER B  1 271 ? -20.519 17.815  -40.026 1.00 33.04 ? 271 SER D CB    1 
ATOM   5022  O OG    . SER B  1 271 ? -20.238 19.165  -40.336 1.00 36.38 ? 271 SER D OG    1 
ATOM   5023  N N     . ILE B  1 272 ? -22.216 15.364  -39.814 1.00 35.38 ? 272 ILE D N     1 
ATOM   5024  C CA    . ILE B  1 272 ? -22.546 13.987  -39.470 1.00 35.99 ? 272 ILE D CA    1 
ATOM   5025  C C     . ILE B  1 272 ? -21.309 13.123  -39.648 1.00 38.16 ? 272 ILE D C     1 
ATOM   5026  O O     . ILE B  1 272 ? -20.684 13.129  -40.714 1.00 40.92 ? 272 ILE D O     1 
ATOM   5027  C CB    . ILE B  1 272 ? -23.701 13.450  -40.322 1.00 35.46 ? 272 ILE D CB    1 
ATOM   5028  C CG1   . ILE B  1 272 ? -25.010 14.005  -39.788 1.00 40.81 ? 272 ILE D CG1   1 
ATOM   5029  C CG2   . ILE B  1 272 ? -23.679 11.927  -40.333 1.00 35.71 ? 272 ILE D CG2   1 
ATOM   5030  C CD1   . ILE B  1 272 ? -26.218 13.492  -40.489 1.00 45.50 ? 272 ILE D CD1   1 
ATOM   5031  N N     . LEU B  1 273 ? -20.953 12.391  -38.606 1.00 39.37 ? 273 LEU D N     1 
ATOM   5032  C CA    . LEU B  1 273 ? -19.919 11.377  -38.728 1.00 41.68 ? 273 LEU D CA    1 
ATOM   5033  C C     . LEU B  1 273 ? -20.513 10.184  -39.465 1.00 43.68 ? 273 LEU D C     1 
ATOM   5034  O O     . LEU B  1 273 ? -21.388 9.485   -38.940 1.00 41.30 ? 273 LEU D O     1 
ATOM   5035  C CB    . LEU B  1 273 ? -19.404 10.992  -37.343 1.00 36.53 ? 273 LEU D CB    1 
ATOM   5036  C CG    . LEU B  1 273 ? -18.787 12.121  -36.517 1.00 40.08 ? 273 LEU D CG    1 
ATOM   5037  C CD1   . LEU B  1 273 ? -19.394 12.210  -35.105 1.00 35.77 ? 273 LEU D CD1   1 
ATOM   5038  C CD2   . LEU B  1 273 ? -17.272 11.960  -36.441 1.00 47.98 ? 273 LEU D CD2   1 
ATOM   5039  N N     . LYS B  1 274 ? -20.063 9.961   -40.692 1.00 43.28 ? 274 LYS D N     1 
ATOM   5040  C CA    . LYS B  1 274 ? -20.597 8.892   -41.528 1.00 44.18 ? 274 LYS D CA    1 
ATOM   5041  C C     . LYS B  1 274 ? -19.689 7.674   -41.413 1.00 44.62 ? 274 LYS D C     1 
ATOM   5042  O O     . LYS B  1 274 ? -18.471 7.795   -41.556 1.00 42.99 ? 274 LYS D O     1 
ATOM   5043  C CB    . LYS B  1 274 ? -20.720 9.357   -42.981 1.00 42.56 ? 274 LYS D CB    1 
ATOM   5044  C CG    . LYS B  1 274 ? -22.129 9.768   -43.384 1.00 41.48 ? 274 LYS D CG    1 
ATOM   5045  C CD    . LYS B  1 274 ? -22.890 8.535   -43.886 1.00 48.18 ? 274 LYS D CD    1 
ATOM   5046  C CE    . LYS B  1 274 ? -24.389 8.563   -43.525 1.00 55.46 ? 274 LYS D CE    1 
ATOM   5047  N NZ    . LYS B  1 274 ? -25.165 7.327   -43.925 1.00 51.20 ? 274 LYS D NZ    1 
ATOM   5048  N N     . TYR B  1 275 ? -20.278 6.508   -41.145 1.00 48.58 ? 275 TYR D N     1 
ATOM   5049  C CA    . TYR B  1 275 ? -19.538 5.259   -40.970 1.00 44.11 ? 275 TYR D CA    1 
ATOM   5050  C C     . TYR B  1 275 ? -20.041 4.199   -41.956 1.00 50.36 ? 275 TYR D C     1 
ATOM   5051  O O     . TYR B  1 275 ? -20.965 4.433   -42.749 1.00 45.19 ? 275 TYR D O     1 
ATOM   5052  C CB    . TYR B  1 275 ? -19.640 4.778   -39.520 1.00 43.41 ? 275 TYR D CB    1 
ATOM   5053  C CG    . TYR B  1 275 ? -19.122 5.803   -38.534 1.00 42.23 ? 275 TYR D CG    1 
ATOM   5054  C CD1   . TYR B  1 275 ? -17.781 5.847   -38.183 1.00 38.09 ? 275 TYR D CD1   1 
ATOM   5055  C CD2   . TYR B  1 275 ? -19.972 6.739   -37.968 1.00 41.20 ? 275 TYR D CD2   1 
ATOM   5056  C CE1   . TYR B  1 275 ? -17.303 6.787   -37.297 1.00 33.57 ? 275 TYR D CE1   1 
ATOM   5057  C CE2   . TYR B  1 275 ? -19.496 7.680   -37.074 1.00 40.95 ? 275 TYR D CE2   1 
ATOM   5058  C CZ    . TYR B  1 275 ? -18.162 7.699   -36.750 1.00 36.00 ? 275 TYR D CZ    1 
ATOM   5059  O OH    . TYR B  1 275 ? -17.682 8.628   -35.862 1.00 46.97 ? 275 TYR D OH    1 
ATOM   5060  N N     . GLU B  1 276 ? -19.382 3.034   -41.932 1.00 52.78 ? 276 GLU D N     1 
ATOM   5061  C CA    . GLU B  1 276 ? -19.848 1.865   -42.673 1.00 60.84 ? 276 GLU D CA    1 
ATOM   5062  C C     . GLU B  1 276 ? -19.173 0.600   -42.147 1.00 67.12 ? 276 GLU D C     1 
ATOM   5063  O O     . GLU B  1 276 ? -19.159 0.377   -40.937 1.00 67.74 ? 276 GLU D O     1 
ATOM   5064  C CB    . GLU B  1 276 ? -19.626 2.042   -44.182 1.00 64.34 ? 276 GLU D CB    1 
ATOM   5065  C CG    . GLU B  1 276 ? -20.545 1.161   -45.050 1.00 67.58 ? 276 GLU D CG    1 
ATOM   5066  C CD    . GLU B  1 276 ? -21.842 0.758   -44.332 1.00 64.99 ? 276 GLU D CD    1 
ATOM   5067  O OE1   . GLU B  1 276 ? -22.711 1.625   -44.111 1.00 63.12 ? 276 GLU D OE1   1 
ATOM   5068  O OE2   . GLU B  1 276 ? -21.992 -0.439  -43.982 1.00 61.04 ? 276 GLU D OE2   1 
ATOM   5069  N N     . GLN B  1 277 ? -18.652 -0.251  -43.034 1.00 72.73 ? 277 GLN D N     1 
ATOM   5070  C CA    . GLN B  1 277 ? -18.049 -1.541  -42.665 1.00 68.45 ? 277 GLN D CA    1 
ATOM   5071  C C     . GLN B  1 277 ? -18.991 -2.429  -41.825 1.00 66.90 ? 277 GLN D C     1 
ATOM   5072  O O     . GLN B  1 277 ? -18.588 -3.014  -40.812 1.00 66.19 ? 277 GLN D O     1 
ATOM   5073  C CB    . GLN B  1 277 ? -16.710 -1.322  -41.951 1.00 58.42 ? 277 GLN D CB    1 
ATOM   5074  C CG    . GLN B  1 277 ? -15.577 -2.247  -42.405 1.00 62.84 ? 277 GLN D CG    1 
ATOM   5075  C CD    . GLN B  1 277 ? -15.284 -2.169  -43.896 1.00 63.70 ? 277 GLN D CD    1 
ATOM   5076  O OE1   . GLN B  1 277 ? -16.120 -2.516  -44.730 1.00 59.66 ? 277 GLN D OE1   1 
ATOM   5077  N NE2   . GLN B  1 277 ? -14.081 -1.712  -44.236 1.00 71.86 ? 277 GLN D NE2   1 
ATOM   5078  N N     . LEU B  1 278 ? -20.269 -2.558  -42.267 1.00 63.86 ? 278 LEU D N     1 
ATOM   5079  C CA    . LEU B  1 278 ? -21.212 -3.474  -41.607 1.00 62.76 ? 278 LEU D CA    1 
ATOM   5080  C C     . LEU B  1 278 ? -22.215 -4.073  -42.596 1.00 62.94 ? 278 LEU D C     1 
ATOM   5081  O O     . LEU B  1 278 ? -23.060 -3.353  -43.147 1.00 64.78 ? 278 LEU D O     1 
ATOM   5082  C CB    . LEU B  1 278 ? -21.929 -2.769  -40.437 1.00 63.89 ? 278 LEU D CB    1 
ATOM   5083  C CG    . LEU B  1 278 ? -22.986 -1.654  -40.576 1.00 62.73 ? 278 LEU D CG    1 
ATOM   5084  C CD1   . LEU B  1 278 ? -24.430 -2.150  -40.370 1.00 56.62 ? 278 LEU D CD1   1 
ATOM   5085  C CD2   . LEU B  1 278 ? -22.691 -0.515  -39.616 1.00 55.55 ? 278 LEU D CD2   1 
ATOM   5086  N N     . PRO B  1 279 ? -22.157 -5.398  -42.856 1.00 59.28 ? 279 PRO D N     1 
ATOM   5087  C CA    . PRO B  1 279 ? -22.966 -5.961  -43.943 1.00 55.01 ? 279 PRO D CA    1 
ATOM   5088  C C     . PRO B  1 279 ? -24.109 -6.868  -43.506 1.00 59.66 ? 279 PRO D C     1 
ATOM   5089  O O     . PRO B  1 279 ? -25.042 -7.089  -44.286 1.00 56.31 ? 279 PRO D O     1 
ATOM   5090  C CB    . PRO B  1 279 ? -21.925 -6.746  -44.741 1.00 60.37 ? 279 PRO D CB    1 
ATOM   5091  C CG    . PRO B  1 279 ? -20.990 -7.269  -43.667 1.00 63.13 ? 279 PRO D CG    1 
ATOM   5092  C CD    . PRO B  1 279 ? -21.072 -6.315  -42.472 1.00 62.49 ? 279 PRO D CD    1 
ATOM   5093  N N     . GLU B  1 280 ? -24.044 -7.380  -42.275 1.00 65.60 ? 280 GLU D N     1 
ATOM   5094  C CA    . GLU B  1 280 ? -24.964 -8.406  -41.761 1.00 64.51 ? 280 GLU D CA    1 
ATOM   5095  C C     . GLU B  1 280 ? -24.764 -9.723  -42.503 1.00 61.45 ? 280 GLU D C     1 
ATOM   5096  O O     . GLU B  1 280 ? -25.466 -10.700 -42.243 1.00 62.66 ? 280 GLU D O     1 
ATOM   5097  C CB    . GLU B  1 280 ? -26.428 -7.971  -41.871 1.00 60.25 ? 280 GLU D CB    1 
ATOM   5098  C CG    . GLU B  1 280 ? -26.812 -6.822  -40.973 1.00 70.36 ? 280 GLU D CG    1 
ATOM   5099  C CD    . GLU B  1 280 ? -27.982 -6.021  -41.530 1.00 78.47 ? 280 GLU D CD    1 
ATOM   5100  O OE1   . GLU B  1 280 ? -28.170 -6.009  -42.771 1.00 74.25 ? 280 GLU D OE1   1 
ATOM   5101  O OE2   . GLU B  1 280 ? -28.716 -5.408  -40.725 1.00 76.75 ? 280 GLU D OE2   1 
ATOM   5102  N N     . SER B  1 285 ? -14.971 -3.763  -37.891 1.00 55.59 ? 285 SER D N     1 
ATOM   5103  C CA    . SER B  1 285 ? -15.942 -2.860  -37.295 1.00 42.00 ? 285 SER D CA    1 
ATOM   5104  C C     . SER B  1 285 ? -15.986 -1.544  -38.013 1.00 45.88 ? 285 SER D C     1 
ATOM   5105  O O     . SER B  1 285 ? -15.147 -1.258  -38.854 1.00 55.42 ? 285 SER D O     1 
ATOM   5106  C CB    . SER B  1 285 ? -15.639 -2.643  -35.826 1.00 42.93 ? 285 SER D CB    1 
ATOM   5107  O OG    . SER B  1 285 ? -16.290 -3.662  -35.106 1.00 42.27 ? 285 SER D OG    1 
ATOM   5108  N N     . ALA B  1 286 ? -16.970 -0.729  -37.656 1.00 45.41 ? 286 ALA D N     1 
ATOM   5109  C CA    . ALA B  1 286 ? -17.415 0.356   -38.517 1.00 43.72 ? 286 ALA D CA    1 
ATOM   5110  C C     . ALA B  1 286 ? -16.350 1.433   -38.645 1.00 42.51 ? 286 ALA D C     1 
ATOM   5111  O O     . ALA B  1 286 ? -16.157 2.235   -37.728 1.00 45.61 ? 286 ALA D O     1 
ATOM   5112  C CB    . ALA B  1 286 ? -18.711 0.945   -37.973 1.00 47.42 ? 286 ALA D CB    1 
ATOM   5113  N N     . LYS B  1 287 ? -15.676 1.472   -39.789 1.00 41.85 ? 287 LYS D N     1 
ATOM   5114  C CA    . LYS B  1 287 ? -14.653 2.475   -40.021 1.00 34.52 ? 287 LYS D CA    1 
ATOM   5115  C C     . LYS B  1 287 ? -15.276 3.784   -40.489 1.00 41.77 ? 287 LYS D C     1 
ATOM   5116  O O     . LYS B  1 287 ? -16.323 3.803   -41.140 1.00 46.95 ? 287 LYS D O     1 
ATOM   5117  C CB    . LYS B  1 287 ? -13.651 1.980   -41.062 1.00 46.67 ? 287 LYS D CB    1 
ATOM   5118  C CG    . LYS B  1 287 ? -14.132 2.107   -42.503 1.00 44.65 ? 287 LYS D CG    1 
ATOM   5119  C CD    . LYS B  1 287 ? -13.035 1.717   -43.517 1.00 49.81 ? 287 LYS D CD    1 
ATOM   5120  C CE    . LYS B  1 287 ? -12.050 2.857   -43.771 1.00 39.47 ? 287 LYS D CE    1 
ATOM   5121  N NZ    . LYS B  1 287 ? -10.805 2.443   -44.475 1.00 28.24 ? 287 LYS D NZ    1 
ATOM   5122  N N     . TRP B  1 288 ? -14.627 4.888   -40.122 1.00 43.69 ? 288 TRP D N     1 
ATOM   5123  C CA    . TRP B  1 288 ? -15.003 6.213   -40.602 1.00 41.86 ? 288 TRP D CA    1 
ATOM   5124  C C     . TRP B  1 288 ? -14.779 6.311   -42.110 1.00 45.50 ? 288 TRP D C     1 
ATOM   5125  O O     . TRP B  1 288 ? -13.830 5.726   -42.632 1.00 50.53 ? 288 TRP D O     1 
ATOM   5126  C CB    . TRP B  1 288 ? -14.160 7.249   -39.869 1.00 39.96 ? 288 TRP D CB    1 
ATOM   5127  C CG    . TRP B  1 288 ? -14.499 8.644   -40.197 1.00 40.79 ? 288 TRP D CG    1 
ATOM   5128  C CD1   . TRP B  1 288 ? -15.731 9.215   -40.170 1.00 42.47 ? 288 TRP D CD1   1 
ATOM   5129  C CD2   . TRP B  1 288 ? -13.593 9.659   -40.628 1.00 40.70 ? 288 TRP D CD2   1 
ATOM   5130  N NE1   . TRP B  1 288 ? -15.653 10.535  -40.544 1.00 44.78 ? 288 TRP D NE1   1 
ATOM   5131  C CE2   . TRP B  1 288 ? -14.348 10.831  -40.840 1.00 46.46 ? 288 TRP D CE2   1 
ATOM   5132  C CE3   . TRP B  1 288 ? -12.216 9.692   -40.859 1.00 40.03 ? 288 TRP D CE3   1 
ATOM   5133  C CZ2   . TRP B  1 288 ? -13.771 12.028  -41.283 1.00 43.55 ? 288 TRP D CZ2   1 
ATOM   5134  C CZ3   . TRP B  1 288 ? -11.640 10.882  -41.298 1.00 42.64 ? 288 TRP D CZ3   1 
ATOM   5135  C CH2   . TRP B  1 288 ? -12.419 12.032  -41.503 1.00 42.17 ? 288 TRP D CH2   1 
ATOM   5136  N N     . ILE B  1 289 ? -15.664 7.032   -42.826 1.00 48.43 ? 289 ILE D N     1 
ATOM   5137  C CA    . ILE B  1 289 ? -15.612 7.097   -44.300 1.00 47.35 ? 289 ILE D CA    1 
ATOM   5138  C C     . ILE B  1 289 ? -15.856 8.490   -44.879 1.00 44.08 ? 289 ILE D C     1 
ATOM   5139  O O     . ILE B  1 289 ? -15.659 8.699   -46.083 1.00 47.29 ? 289 ILE D O     1 
ATOM   5140  C CB    . ILE B  1 289 ? -16.617 6.126   -44.965 1.00 42.82 ? 289 ILE D CB    1 
ATOM   5141  C CG1   . ILE B  1 289 ? -18.031 6.724   -44.991 1.00 41.56 ? 289 ILE D CG1   1 
ATOM   5142  C CG2   . ILE B  1 289 ? -16.596 4.761   -44.300 1.00 49.60 ? 289 ILE D CG2   1 
ATOM   5143  C CD1   . ILE B  1 289 ? -19.118 5.719   -45.311 1.00 41.61 ? 289 ILE D CD1   1 
ATOM   5144  N N     . GLY B  1 290 ? -16.328 9.432   -44.070 1.00 36.47 ? 290 GLY D N     1 
ATOM   5145  C CA    . GLY B  1 290 ? -16.652 10.742  -44.611 1.00 37.75 ? 290 GLY D CA    1 
ATOM   5146  C C     . GLY B  1 290 ? -17.461 11.562  -43.638 1.00 39.69 ? 290 GLY D C     1 
ATOM   5147  O O     . GLY B  1 290 ? -17.872 11.102  -42.568 1.00 43.30 ? 290 GLY D O     1 
ATOM   5148  N N     . LEU B  1 291 ? -17.677 12.803  -44.019 1.00 33.47 ? 291 LEU D N     1 
ATOM   5149  C CA    . LEU B  1 291 ? -18.511 13.695  -43.238 1.00 35.94 ? 291 LEU D CA    1 
ATOM   5150  C C     . LEU B  1 291 ? -19.598 14.257  -44.138 1.00 42.57 ? 291 LEU D C     1 
ATOM   5151  O O     . LEU B  1 291 ? -19.429 14.357  -45.360 1.00 37.27 ? 291 LEU D O     1 
ATOM   5152  C CB    . LEU B  1 291 ? -17.706 14.848  -42.628 1.00 37.33 ? 291 LEU D CB    1 
ATOM   5153  C CG    . LEU B  1 291 ? -16.879 14.629  -41.362 1.00 31.52 ? 291 LEU D CG    1 
ATOM   5154  C CD1   . LEU B  1 291 ? -16.356 15.949  -40.885 1.00 23.39 ? 291 LEU D CD1   1 
ATOM   5155  C CD2   . LEU B  1 291 ? -17.706 13.958  -40.297 1.00 36.44 ? 291 LEU D CD2   1 
ATOM   5156  N N     . ASP B  1 292 ? -20.714 14.625  -43.522 1.00 39.74 ? 292 ASP D N     1 
ATOM   5157  C CA    . ASP B  1 292 ? -21.838 15.185  -44.243 1.00 38.99 ? 292 ASP D CA    1 
ATOM   5158  C C     . ASP B  1 292 ? -22.212 16.515  -43.611 1.00 38.51 ? 292 ASP D C     1 
ATOM   5159  O O     . ASP B  1 292 ? -22.059 16.694  -42.406 1.00 41.37 ? 292 ASP D O     1 
ATOM   5160  C CB    . ASP B  1 292 ? -23.018 14.223  -44.223 1.00 42.85 ? 292 ASP D CB    1 
ATOM   5161  C CG    . ASP B  1 292 ? -22.769 12.966  -45.057 1.00 44.05 ? 292 ASP D CG    1 
ATOM   5162  O OD1   . ASP B  1 292 ? -21.601 12.661  -45.412 1.00 40.44 ? 292 ASP D OD1   1 
ATOM   5163  O OD2   . ASP B  1 292 ? -23.762 12.278  -45.362 1.00 44.83 ? 292 ASP D OD2   1 
ATOM   5164  N N     . SER B  1 293 ? -22.719 17.429  -44.439 1.00 37.33 ? 293 SER D N     1 
ATOM   5165  C CA    . SER B  1 293 ? -22.989 18.854  -44.247 1.00 37.16 ? 293 SER D CA    1 
ATOM   5166  C C     . SER B  1 293 ? -24.098 19.046  -43.221 1.00 42.40 ? 293 SER D C     1 
ATOM   5167  O O     . SER B  1 293 ? -24.145 18.216  -42.315 1.00 49.96 ? 293 SER D O     1 
ATOM   5168  C CB    . SER B  1 293 ? -23.326 19.426  -45.607 1.00 47.93 ? 293 SER D CB    1 
ATOM   5169  O OG    . SER B  1 293 ? -24.465 18.751  -46.113 1.00 47.62 ? 293 SER D OG    1 
ATOM   5170  N N     . PRO B  1 294 ? -25.047 20.118  -43.262 1.00 44.89 ? 294 PRO D N     1 
ATOM   5171  C CA    . PRO B  1 294 ? -25.843 20.342  -42.040 1.00 41.29 ? 294 PRO D CA    1 
ATOM   5172  C C     . PRO B  1 294 ? -26.333 19.037  -41.455 1.00 48.38 ? 294 PRO D C     1 
ATOM   5173  O O     . PRO B  1 294 ? -27.039 18.294  -42.138 1.00 56.31 ? 294 PRO D O     1 
ATOM   5174  C CB    . PRO B  1 294 ? -27.047 21.181  -42.497 1.00 39.67 ? 294 PRO D CB    1 
ATOM   5175  C CG    . PRO B  1 294 ? -26.745 21.705  -43.769 1.00 43.95 ? 294 PRO D CG    1 
ATOM   5176  C CD    . PRO B  1 294 ? -25.580 20.958  -44.365 1.00 43.77 ? 294 PRO D CD    1 
ATOM   5177  N N     . SER B  1 295 ? -25.900 18.705  -40.248 1.00 48.65 ? 295 SER D N     1 
ATOM   5178  C CA    . SER B  1 295 ? -26.419 17.513  -39.601 1.00 44.55 ? 295 SER D CA    1 
ATOM   5179  C C     . SER B  1 295 ? -27.936 17.584  -39.524 1.00 44.95 ? 295 SER D C     1 
ATOM   5180  O O     . SER B  1 295 ? -28.527 18.667  -39.449 1.00 46.40 ? 295 SER D O     1 
ATOM   5181  C CB    . SER B  1 295 ? -25.833 17.355  -38.199 1.00 46.11 ? 295 SER D CB    1 
ATOM   5182  O OG    . SER B  1 295 ? -26.325 18.339  -37.305 1.00 45.21 ? 295 SER D OG    1 
ATOM   5183  N N     . ARG B  1 296 ? -28.564 16.414  -39.587 1.00 51.93 ? 296 ARG D N     1 
ATOM   5184  C CA    . ARG B  1 296 ? -29.997 16.277  -39.338 1.00 51.55 ? 296 ARG D CA    1 
ATOM   5185  C C     . ARG B  1 296 ? -30.255 16.193  -37.849 1.00 46.31 ? 296 ARG D C     1 
ATOM   5186  O O     . ARG B  1 296 ? -31.001 15.344  -37.358 1.00 56.35 ? 296 ARG D O     1 
ATOM   5187  C CB    . ARG B  1 296 ? -30.566 15.062  -40.065 1.00 54.69 ? 296 ARG D CB    1 
ATOM   5188  C CG    . ARG B  1 296 ? -30.041 14.884  -41.488 1.00 54.17 ? 296 ARG D CG    1 
ATOM   5189  C CD    . ARG B  1 296 ? -30.748 13.778  -42.228 1.00 59.46 ? 296 ARG D CD    1 
ATOM   5190  N NE    . ARG B  1 296 ? -31.910 14.267  -42.962 1.00 74.03 ? 296 ARG D NE    1 
ATOM   5191  C CZ    . ARG B  1 296 ? -31.993 14.345  -44.287 1.00 78.31 ? 296 ARG D CZ    1 
ATOM   5192  N NH1   . ARG B  1 296 ? -31.002 13.941  -45.070 1.00 72.36 ? 296 ARG D NH1   1 
ATOM   5193  N NH2   . ARG B  1 296 ? -33.103 14.832  -44.843 1.00 74.04 ? 296 ARG D NH2   1 
ATOM   5194  N N     . SER B  1 297 ? -29.594 17.068  -37.102 1.00 45.04 ? 297 SER D N     1 
ATOM   5195  C CA    . SER B  1 297 ? -29.552 16.971  -35.648 1.00 43.99 ? 297 SER D CA    1 
ATOM   5196  C C     . SER B  1 297 ? -29.131 18.368  -35.195 1.00 40.03 ? 297 SER D C     1 
ATOM   5197  O O     . SER B  1 297 ? -27.941 18.638  -35.047 1.00 47.10 ? 297 SER D O     1 
ATOM   5198  C CB    . SER B  1 297 ? -28.570 15.929  -35.155 1.00 46.79 ? 297 SER D CB    1 
ATOM   5199  O OG    . SER B  1 297 ? -28.680 14.698  -35.853 1.00 52.63 ? 297 SER D OG    1 
ATOM   5200  N N     . GLU B  1 298 ? -30.098 19.244  -35.019 1.00 41.68 ? 298 GLU D N     1 
ATOM   5201  C CA    . GLU B  1 298 ? -29.772 20.572  -34.532 1.00 40.72 ? 298 GLU D CA    1 
ATOM   5202  C C     . GLU B  1 298 ? -31.016 21.183  -33.906 1.00 40.48 ? 298 GLU D C     1 
ATOM   5203  O O     . GLU B  1 298 ? -31.598 22.136  -34.419 1.00 44.75 ? 298 GLU D O     1 
ATOM   5204  C CB    . GLU B  1 298 ? -29.213 21.438  -35.666 1.00 33.11 ? 298 GLU D CB    1 
ATOM   5205  C CG    . GLU B  1 298 ? -28.816 22.803  -35.233 1.00 37.29 ? 298 GLU D CG    1 
ATOM   5206  C CD    . GLU B  1 298 ? -28.076 23.550  -36.290 1.00 46.33 ? 298 GLU D CD    1 
ATOM   5207  O OE1   . GLU B  1 298 ? -27.555 22.897  -37.215 1.00 47.67 ? 298 GLU D OE1   1 
ATOM   5208  O OE2   . GLU B  1 298 ? -28.020 24.796  -36.197 1.00 50.39 ? 298 GLU D OE2   1 
ATOM   5209  N N     . PHE B  1 299 ? -31.446 20.592  -32.788 1.00 41.47 ? 299 PHE D N     1 
ATOM   5210  C CA    . PHE B  1 299 ? -32.561 21.083  -32.007 1.00 42.92 ? 299 PHE D CA    1 
ATOM   5211  C C     . PHE B  1 299 ? -32.049 21.594  -30.671 1.00 41.88 ? 299 PHE D C     1 
ATOM   5212  O O     . PHE B  1 299 ? -30.854 21.550  -30.381 1.00 40.63 ? 299 PHE D O     1 
ATOM   5213  C CB    . PHE B  1 299 ? -33.604 19.984  -31.803 1.00 45.39 ? 299 PHE D CB    1 
ATOM   5214  C CG    . PHE B  1 299 ? -33.234 18.695  -32.454 1.00 45.52 ? 299 PHE D CG    1 
ATOM   5215  C CD1   . PHE B  1 299 ? -33.501 18.481  -33.803 1.00 45.52 ? 299 PHE D CD1   1 
ATOM   5216  C CD2   . PHE B  1 299 ? -32.610 17.691  -31.722 1.00 44.63 ? 299 PHE D CD2   1 
ATOM   5217  C CE1   . PHE B  1 299 ? -33.147 17.281  -34.428 1.00 43.08 ? 299 PHE D CE1   1 
ATOM   5218  C CE2   . PHE B  1 299 ? -32.254 16.488  -32.334 1.00 47.59 ? 299 PHE D CE2   1 
ATOM   5219  C CZ    . PHE B  1 299 ? -32.524 16.284  -33.697 1.00 46.78 ? 299 PHE D CZ    1 
ATOM   5220  N N     . GLU B  1 300 ? -32.979 22.049  -29.834 1.00 39.68 ? 300 GLU D N     1 
ATOM   5221  C CA    . GLU B  1 300 ? -32.580 22.660  -28.574 1.00 45.97 ? 300 GLU D CA    1 
ATOM   5222  C C     . GLU B  1 300 ? -31.910 21.635  -27.655 1.00 43.15 ? 300 GLU D C     1 
ATOM   5223  O O     . GLU B  1 300 ? -30.837 21.890  -27.089 1.00 39.27 ? 300 GLU D O     1 
ATOM   5224  C CB    . GLU B  1 300 ? -33.809 23.307  -27.911 1.00 47.99 ? 300 GLU D CB    1 
ATOM   5225  C CG    . GLU B  1 300 ? -33.528 24.509  -26.996 1.00 47.33 ? 300 GLU D CG    1 
ATOM   5226  C CD    . GLU B  1 300 ? -33.184 25.806  -27.750 1.00 53.45 ? 300 GLU D CD    1 
ATOM   5227  O OE1   . GLU B  1 300 ? -32.218 25.825  -28.566 1.00 49.92 ? 300 GLU D OE1   1 
ATOM   5228  O OE2   . GLU B  1 300 ? -33.877 26.823  -27.499 1.00 52.88 ? 300 GLU D OE2   1 
ATOM   5229  N N     . ALA B  1 301 ? -32.514 20.452  -27.526 1.00 40.92 ? 301 ALA D N     1 
ATOM   5230  C CA    . ALA B  1 301 ? -31.977 19.406  -26.660 1.00 46.47 ? 301 ALA D CA    1 
ATOM   5231  C C     . ALA B  1 301 ? -30.556 18.990  -27.023 1.00 46.40 ? 301 ALA D C     1 
ATOM   5232  O O     . ALA B  1 301 ? -29.921 18.261  -26.251 1.00 48.18 ? 301 ALA D O     1 
ATOM   5233  C CB    . ALA B  1 301 ? -32.882 18.170  -26.695 1.00 48.08 ? 301 ALA D CB    1 
ATOM   5234  N N     . THR B  1 302 ? -30.048 19.412  -28.172 1.00 39.78 ? 302 THR D N     1 
ATOM   5235  C CA    . THR B  1 302 ? -28.650 19.207  -28.509 1.00 42.39 ? 302 THR D CA    1 
ATOM   5236  C C     . THR B  1 302 ? -27.853 20.502  -28.435 1.00 38.94 ? 302 THR D C     1 
ATOM   5237  O O     . THR B  1 302 ? -26.784 20.549  -27.812 1.00 39.80 ? 302 THR D O     1 
ATOM   5238  C CB    . THR B  1 302 ? -28.544 18.570  -29.910 1.00 38.67 ? 302 THR D CB    1 
ATOM   5239  O OG1   . THR B  1 302 ? -29.048 19.463  -30.915 1.00 38.29 ? 302 THR D OG1   1 
ATOM   5240  C CG2   . THR B  1 302 ? -29.362 17.294  -29.975 1.00 34.57 ? 302 THR D CG2   1 
ATOM   5241  N N     . LEU B  1 303 ? -28.385 21.574  -29.018 1.00 38.36 ? 303 LEU D N     1 
ATOM   5242  C CA    . LEU B  1 303 ? -27.673 22.842  -29.049 1.00 35.24 ? 303 LEU D CA    1 
ATOM   5243  C C     . LEU B  1 303 ? -27.445 23.381  -27.644 1.00 41.89 ? 303 LEU D C     1 
ATOM   5244  O O     . LEU B  1 303 ? -26.313 23.718  -27.273 1.00 38.28 ? 303 LEU D O     1 
ATOM   5245  C CB    . LEU B  1 303 ? -28.459 23.839  -29.894 1.00 41.56 ? 303 LEU D CB    1 
ATOM   5246  C CG    . LEU B  1 303 ? -28.719 23.357  -31.321 1.00 42.15 ? 303 LEU D CG    1 
ATOM   5247  C CD1   . LEU B  1 303 ? -29.630 24.346  -32.020 1.00 44.70 ? 303 LEU D CD1   1 
ATOM   5248  C CD2   . LEU B  1 303 ? -27.401 23.135  -32.087 1.00 32.65 ? 303 LEU D CD2   1 
ATOM   5249  N N     . LYS B  1 304 ? -28.515 23.450  -26.837 1.00 44.29 ? 304 LYS D N     1 
ATOM   5250  C CA    . LYS B  1 304 ? -28.431 24.118  -25.538 1.00 35.59 ? 304 LYS D CA    1 
ATOM   5251  C C     . LYS B  1 304 ? -27.460 23.444  -24.583 1.00 34.52 ? 304 LYS D C     1 
ATOM   5252  O O     . LYS B  1 304 ? -26.641 24.158  -23.980 1.00 33.07 ? 304 LYS D O     1 
ATOM   5253  C CB    . LYS B  1 304 ? -29.825 24.238  -24.920 1.00 40.50 ? 304 LYS D CB    1 
ATOM   5254  C CG    . LYS B  1 304 ? -30.486 25.583  -25.195 1.00 45.66 ? 304 LYS D CG    1 
ATOM   5255  C CD    . LYS B  1 304 ? -31.648 25.885  -24.233 1.00 45.32 ? 304 LYS D CD    1 
ATOM   5256  C CE    . LYS B  1 304 ? -31.609 27.335  -23.741 1.00 45.19 ? 304 LYS D CE    1 
ATOM   5257  N NZ    . LYS B  1 304 ? -32.023 27.490  -22.317 1.00 46.60 ? 304 LYS D NZ    1 
ATOM   5258  N N     . PRO B  1 305 ? -27.487 22.119  -24.377 1.00 33.67 ? 305 PRO D N     1 
ATOM   5259  C CA    . PRO B  1 305 ? -26.512 21.534  -23.438 1.00 33.53 ? 305 PRO D CA    1 
ATOM   5260  C C     . PRO B  1 305 ? -25.073 21.642  -23.934 1.00 35.74 ? 305 PRO D C     1 
ATOM   5261  O O     . PRO B  1 305 ? -24.152 21.921  -23.147 1.00 33.20 ? 305 PRO D O     1 
ATOM   5262  C CB    . PRO B  1 305 ? -26.964 20.072  -23.324 1.00 32.34 ? 305 PRO D CB    1 
ATOM   5263  C CG    . PRO B  1 305 ? -28.268 19.988  -24.047 1.00 33.50 ? 305 PRO D CG    1 
ATOM   5264  C CD    . PRO B  1 305 ? -28.303 21.080  -25.026 1.00 33.41 ? 305 PRO D CD    1 
ATOM   5265  N N     . ALA B  1 306 ? -24.858 21.432  -25.233 1.00 36.49 ? 306 ALA D N     1 
ATOM   5266  C CA    . ALA B  1 306 ? -23.523 21.561  -25.804 1.00 32.98 ? 306 ALA D CA    1 
ATOM   5267  C C     . ALA B  1 306 ? -23.023 22.991  -25.727 1.00 31.79 ? 306 ALA D C     1 
ATOM   5268  O O     . ALA B  1 306 ? -21.839 23.227  -25.477 1.00 36.45 ? 306 ALA D O     1 
ATOM   5269  C CB    . ALA B  1 306 ? -23.535 21.090  -27.257 1.00 35.92 ? 306 ALA D CB    1 
ATOM   5270  N N     . GLU B  1 307 ? -23.906 23.957  -25.971 1.00 35.94 ? 307 GLU D N     1 
ATOM   5271  C CA    . GLU B  1 307 ? -23.515 25.361  -25.900 1.00 34.54 ? 307 GLU D CA    1 
ATOM   5272  C C     . GLU B  1 307 ? -23.125 25.761  -24.483 1.00 33.82 ? 307 GLU D C     1 
ATOM   5273  O O     . GLU B  1 307 ? -22.161 26.510  -24.290 1.00 35.11 ? 307 GLU D O     1 
ATOM   5274  C CB    . GLU B  1 307 ? -24.656 26.238  -26.410 1.00 36.50 ? 307 GLU D CB    1 
ATOM   5275  C CG    . GLU B  1 307 ? -24.465 27.718  -26.164 1.00 41.20 ? 307 GLU D CG    1 
ATOM   5276  C CD    . GLU B  1 307 ? -25.767 28.434  -25.842 1.00 46.16 ? 307 GLU D CD    1 
ATOM   5277  O OE1   . GLU B  1 307 ? -26.655 27.824  -25.201 1.00 50.36 ? 307 GLU D OE1   1 
ATOM   5278  O OE2   . GLU B  1 307 ? -25.907 29.609  -26.241 1.00 50.79 ? 307 GLU D OE2   1 
ATOM   5279  N N     . GLU B  1 308 ? -23.855 25.269  -23.483 1.00 28.29 ? 308 GLU D N     1 
ATOM   5280  C CA    . GLU B  1 308 ? -23.533 25.603  -22.104 1.00 30.88 ? 308 GLU D CA    1 
ATOM   5281  C C     . GLU B  1 308 ? -22.165 25.056  -21.714 1.00 34.30 ? 308 GLU D C     1 
ATOM   5282  O O     . GLU B  1 308 ? -21.314 25.791  -21.188 1.00 30.07 ? 308 GLU D O     1 
ATOM   5283  C CB    . GLU B  1 308 ? -24.617 25.067  -21.174 1.00 29.30 ? 308 GLU D CB    1 
ATOM   5284  C CG    . GLU B  1 308 ? -24.162 24.972  -19.745 1.00 32.63 ? 308 GLU D CG    1 
ATOM   5285  C CD    . GLU B  1 308 ? -25.299 24.645  -18.820 1.00 36.47 ? 308 GLU D CD    1 
ATOM   5286  O OE1   . GLU B  1 308 ? -25.914 23.566  -19.005 1.00 31.81 ? 308 GLU D OE1   1 
ATOM   5287  O OE2   . GLU B  1 308 ? -25.575 25.466  -17.915 1.00 32.21 ? 308 GLU D OE2   1 
ATOM   5288  N N     . PHE B  1 309 ? -21.933 23.759  -21.970 1.00 35.60 ? 309 PHE D N     1 
ATOM   5289  C CA    . PHE B  1 309 ? -20.620 23.162  -21.717 1.00 31.79 ? 309 PHE D CA    1 
ATOM   5290  C C     . PHE B  1 309 ? -19.519 23.958  -22.389 1.00 31.03 ? 309 PHE D C     1 
ATOM   5291  O O     . PHE B  1 309 ? -18.518 24.299  -21.754 1.00 29.31 ? 309 PHE D O     1 
ATOM   5292  C CB    . PHE B  1 309 ? -20.583 21.708  -22.202 1.00 33.02 ? 309 PHE D CB    1 
ATOM   5293  C CG    . PHE B  1 309 ? -19.247 21.020  -21.986 1.00 38.92 ? 309 PHE D CG    1 
ATOM   5294  C CD1   . PHE B  1 309 ? -18.205 21.130  -22.915 1.00 30.32 ? 309 PHE D CD1   1 
ATOM   5295  C CD2   . PHE B  1 309 ? -19.019 20.286  -20.820 1.00 33.43 ? 309 PHE D CD2   1 
ATOM   5296  C CE1   . PHE B  1 309 ? -16.987 20.509  -22.687 1.00 27.31 ? 309 PHE D CE1   1 
ATOM   5297  C CE2   . PHE B  1 309 ? -17.787 19.671  -20.588 1.00 29.94 ? 309 PHE D CE2   1 
ATOM   5298  C CZ    . PHE B  1 309 ? -16.779 19.779  -21.514 1.00 29.71 ? 309 PHE D CZ    1 
ATOM   5299  N N     . ILE B  1 310 ? -19.708 24.276  -23.676 1.00 28.55 ? 310 ILE D N     1 
ATOM   5300  C CA    . ILE B  1 310 ? -18.697 24.983  -24.453 1.00 30.27 ? 310 ILE D CA    1 
ATOM   5301  C C     . ILE B  1 310 ? -18.274 26.260  -23.730 1.00 34.04 ? 310 ILE D C     1 
ATOM   5302  O O     . ILE B  1 310 ? -17.079 26.520  -23.518 1.00 31.64 ? 310 ILE D O     1 
ATOM   5303  C CB    . ILE B  1 310 ? -19.232 25.273  -25.871 1.00 31.28 ? 310 ILE D CB    1 
ATOM   5304  C CG1   . ILE B  1 310 ? -19.207 24.015  -26.748 1.00 27.18 ? 310 ILE D CG1   1 
ATOM   5305  C CG2   . ILE B  1 310 ? -18.446 26.384  -26.528 1.00 30.35 ? 310 ILE D CG2   1 
ATOM   5306  C CD1   . ILE B  1 310 ? -17.853 23.349  -26.885 1.00 29.59 ? 310 ILE D CD1   1 
ATOM   5307  N N     . GLU B  1 311 ? -19.258 27.055  -23.299 1.00 33.60 ? 311 GLU D N     1 
ATOM   5308  C CA    . GLU B  1 311 ? -18.947 28.320  -22.636 1.00 36.49 ? 311 GLU D CA    1 
ATOM   5309  C C     . GLU B  1 311 ? -18.166 28.103  -21.341 1.00 36.79 ? 311 GLU D C     1 
ATOM   5310  O O     . GLU B  1 311 ? -17.233 28.862  -21.038 1.00 31.66 ? 311 GLU D O     1 
ATOM   5311  C CB    . GLU B  1 311 ? -20.229 29.106  -22.360 1.00 34.04 ? 311 GLU D CB    1 
ATOM   5312  C CG    . GLU B  1 311 ? -20.078 30.589  -22.648 1.00 36.16 ? 311 GLU D CG    1 
ATOM   5313  C CD    . GLU B  1 311 ? -19.127 31.269  -21.677 1.00 44.24 ? 311 GLU D CD    1 
ATOM   5314  O OE1   . GLU B  1 311 ? -19.032 30.806  -20.517 1.00 53.91 ? 311 GLU D OE1   1 
ATOM   5315  O OE2   . GLU B  1 311 ? -18.464 32.257  -22.065 1.00 43.97 ? 311 GLU D OE2   1 
ATOM   5316  N N     . MET B  1 312 ? -18.539 27.086  -20.550 1.00 35.99 ? 312 MET D N     1 
ATOM   5317  C CA    . MET B  1 312 ? -17.746 26.805  -19.361 1.00 32.69 ? 312 MET D CA    1 
ATOM   5318  C C     . MET B  1 312 ? -16.298 26.597  -19.749 1.00 29.33 ? 312 MET D C     1 
ATOM   5319  O O     . MET B  1 312 ? -15.393 27.120  -19.091 1.00 33.25 ? 312 MET D O     1 
ATOM   5320  C CB    . MET B  1 312 ? -18.246 25.577  -18.604 1.00 33.30 ? 312 MET D CB    1 
ATOM   5321  C CG    . MET B  1 312 ? -17.087 24.840  -17.926 1.00 34.94 ? 312 MET D CG    1 
ATOM   5322  S SD    . MET B  1 312 ? -17.478 23.244  -17.215 1.00 37.32 ? 312 MET D SD    1 
ATOM   5323  C CE    . MET B  1 312 ? -18.699 23.764  -16.061 1.00 38.08 ? 312 MET D CE    1 
ATOM   5324  N N     . ILE B  1 313 ? -16.054 25.891  -20.854 1.00 25.74 ? 313 ILE D N     1 
ATOM   5325  C CA    . ILE B  1 313 ? -14.676 25.802  -21.318 1.00 32.87 ? 313 ILE D CA    1 
ATOM   5326  C C     . ILE B  1 313 ? -14.179 27.170  -21.776 1.00 29.18 ? 313 ILE D C     1 
ATOM   5327  O O     . ILE B  1 313 ? -13.038 27.550  -21.485 1.00 30.47 ? 313 ILE D O     1 
ATOM   5328  C CB    . ILE B  1 313 ? -14.492 24.713  -22.399 1.00 29.99 ? 313 ILE D CB    1 
ATOM   5329  C CG1   . ILE B  1 313 ? -14.072 25.306  -23.730 1.00 29.25 ? 313 ILE D CG1   1 
ATOM   5330  C CG2   . ILE B  1 313 ? -15.674 23.783  -22.505 1.00 30.14 ? 313 ILE D CG2   1 
ATOM   5331  C CD1   . ILE B  1 313 ? -12.807 24.670  -24.254 1.00 33.01 ? 313 ILE D CD1   1 
ATOM   5332  N N     . ARG B  1 314 ? -15.029 27.959  -22.443 1.00 27.28 ? 314 ARG D N     1 
ATOM   5333  C CA    . ARG B  1 314 ? -14.625 29.336  -22.712 1.00 33.26 ? 314 ARG D CA    1 
ATOM   5334  C C     . ARG B  1 314 ? -14.191 30.032  -21.429 1.00 32.41 ? 314 ARG D C     1 
ATOM   5335  O O     . ARG B  1 314 ? -13.162 30.716  -21.400 1.00 29.81 ? 314 ARG D O     1 
ATOM   5336  C CB    . ARG B  1 314 ? -15.750 30.123  -23.386 1.00 34.93 ? 314 ARG D CB    1 
ATOM   5337  C CG    . ARG B  1 314 ? -15.201 31.167  -24.362 1.00 35.94 ? 314 ARG D CG    1 
ATOM   5338  C CD    . ARG B  1 314 ? -15.392 32.589  -23.888 1.00 31.15 ? 314 ARG D CD    1 
ATOM   5339  N NE    . ARG B  1 314 ? -16.683 33.094  -24.319 1.00 35.53 ? 314 ARG D NE    1 
ATOM   5340  C CZ    . ARG B  1 314 ? -17.291 34.139  -23.777 1.00 40.07 ? 314 ARG D CZ    1 
ATOM   5341  N NH1   . ARG B  1 314 ? -16.743 34.813  -22.780 1.00 39.86 ? 314 ARG D NH1   1 
ATOM   5342  N NH2   . ARG B  1 314 ? -18.482 34.514  -24.243 1.00 35.99 ? 314 ARG D NH2   1 
ATOM   5343  N N     . THR B  1 315 ? -14.947 29.823  -20.347 1.00 32.36 ? 315 THR D N     1 
ATOM   5344  C CA    . THR B  1 315 ? -14.636 30.443  -19.065 1.00 29.73 ? 315 THR D CA    1 
ATOM   5345  C C     . THR B  1 315 ? -13.292 29.974  -18.514 1.00 35.96 ? 315 THR D C     1 
ATOM   5346  O O     . THR B  1 315 ? -12.522 30.784  -17.978 1.00 39.22 ? 315 THR D O     1 
ATOM   5347  C CB    . THR B  1 315 ? -15.754 30.144  -18.067 1.00 32.07 ? 315 THR D CB    1 
ATOM   5348  O OG1   . THR B  1 315 ? -16.973 30.727  -18.532 1.00 32.96 ? 315 THR D OG1   1 
ATOM   5349  C CG2   . THR B  1 315 ? -15.432 30.702  -16.684 1.00 27.29 ? 315 THR D CG2   1 
ATOM   5350  N N     . ILE B  1 316 ? -12.975 28.680  -18.622 1.00 33.75 ? 316 ILE D N     1 
ATOM   5351  C CA    . ILE B  1 316 ? -11.714 28.243  -18.030 1.00 37.41 ? 316 ILE D CA    1 
ATOM   5352  C C     . ILE B  1 316 ? -10.501 28.676  -18.844 1.00 38.34 ? 316 ILE D C     1 
ATOM   5353  O O     . ILE B  1 316 ? -9.373  28.604  -18.329 1.00 40.30 ? 316 ILE D O     1 
ATOM   5354  C CB    . ILE B  1 316 ? -11.626 26.722  -17.818 1.00 32.40 ? 316 ILE D CB    1 
ATOM   5355  C CG1   . ILE B  1 316 ? -11.111 26.059  -19.072 1.00 35.51 ? 316 ILE D CG1   1 
ATOM   5356  C CG2   . ILE B  1 316 ? -12.969 26.132  -17.429 1.00 31.38 ? 316 ILE D CG2   1 
ATOM   5357  C CD1   . ILE B  1 316 ? -10.539 24.706  -18.803 1.00 47.57 ? 316 ILE D CD1   1 
ATOM   5358  N N     . GLY B  1 317 ? -10.684 29.113  -20.098 1.00 32.63 ? 317 GLY D N     1 
ATOM   5359  C CA    . GLY B  1 317 ? -9.606  29.838  -20.764 1.00 34.60 ? 317 GLY D CA    1 
ATOM   5360  C C     . GLY B  1 317 ? -9.291  29.548  -22.222 1.00 34.21 ? 317 GLY D C     1 
ATOM   5361  O O     . GLY B  1 317 ? -8.650  30.365  -22.896 1.00 32.86 ? 317 GLY D O     1 
ATOM   5362  N N     . TYR B  1 318 ? -9.742  28.410  -22.731 1.00 31.79 ? 318 TYR D N     1 
ATOM   5363  C CA    . TYR B  1 318 ? -9.369  28.002  -24.075 1.00 30.08 ? 318 TYR D CA    1 
ATOM   5364  C C     . TYR B  1 318 ? -9.771  29.046  -25.105 1.00 35.72 ? 318 TYR D C     1 
ATOM   5365  O O     . TYR B  1 318 ? -10.950 29.397  -25.228 1.00 33.29 ? 318 TYR D O     1 
ATOM   5366  C CB    . TYR B  1 318 ? -10.031 26.683  -24.412 1.00 26.74 ? 318 TYR D CB    1 
ATOM   5367  C CG    . TYR B  1 318 ? -9.747  26.252  -25.814 1.00 29.23 ? 318 TYR D CG    1 
ATOM   5368  C CD1   . TYR B  1 318 ? -8.444  26.023  -26.229 1.00 30.33 ? 318 TYR D CD1   1 
ATOM   5369  C CD2   . TYR B  1 318 ? -10.776 26.080  -26.732 1.00 29.27 ? 318 TYR D CD2   1 
ATOM   5370  C CE1   . TYR B  1 318 ? -8.166  25.619  -27.518 1.00 30.78 ? 318 TYR D CE1   1 
ATOM   5371  C CE2   . TYR B  1 318 ? -10.516 25.688  -28.025 1.00 29.28 ? 318 TYR D CE2   1 
ATOM   5372  C CZ    . TYR B  1 318 ? -9.203  25.463  -28.417 1.00 32.15 ? 318 TYR D CZ    1 
ATOM   5373  O OH    . TYR B  1 318 ? -8.918  25.074  -29.706 1.00 25.93 ? 318 TYR D OH    1 
ATOM   5374  N N     . ARG B  1 319 ? -8.797  29.522  -25.865 1.00 34.61 ? 319 ARG D N     1 
ATOM   5375  C CA    . ARG B  1 319 ? -9.046  30.435  -26.971 1.00 32.54 ? 319 ARG D CA    1 
ATOM   5376  C C     . ARG B  1 319 ? -8.781  29.699  -28.280 1.00 32.82 ? 319 ARG D C     1 
ATOM   5377  O O     . ARG B  1 319 ? -7.624  29.460  -28.634 1.00 37.99 ? 319 ARG D O     1 
ATOM   5378  C CB    . ARG B  1 319 ? -8.173  31.673  -26.840 1.00 31.56 ? 319 ARG D CB    1 
ATOM   5379  C CG    . ARG B  1 319 ? -8.668  32.615  -25.774 1.00 38.65 ? 319 ARG D CG    1 
ATOM   5380  C CD    . ARG B  1 319 ? -10.205 32.628  -25.725 1.00 33.80 ? 319 ARG D CD    1 
ATOM   5381  N NE    . ARG B  1 319 ? -10.672 33.335  -24.538 1.00 36.65 ? 319 ARG D NE    1 
ATOM   5382  C CZ    . ARG B  1 319 ? -11.064 32.751  -23.408 1.00 39.08 ? 319 ARG D CZ    1 
ATOM   5383  N NH1   . ARG B  1 319 ? -11.136 31.432  -23.293 1.00 29.35 ? 319 ARG D NH1   1 
ATOM   5384  N NH2   . ARG B  1 319 ? -11.393 33.510  -22.365 1.00 33.66 ? 319 ARG D NH2   1 
ATOM   5385  N N     . GLY B  1 320 ? -9.847  29.341  -28.991 1.00 34.94 ? 320 GLY D N     1 
ATOM   5386  C CA    . GLY B  1 320 ? -9.703  28.866  -30.359 1.00 32.26 ? 320 GLY D CA    1 
ATOM   5387  C C     . GLY B  1 320 ? -10.881 27.993  -30.780 1.00 30.35 ? 320 GLY D C     1 
ATOM   5388  O O     . GLY B  1 320 ? -11.970 28.077  -30.211 1.00 28.32 ? 320 GLY D O     1 
ATOM   5389  N N     . TYR B  1 321 ? -10.618 27.168  -31.800 1.00 27.11 ? 321 TYR D N     1 
ATOM   5390  C CA    . TYR B  1 321 ? -11.584 26.203  -32.310 1.00 28.91 ? 321 TYR D CA    1 
ATOM   5391  C C     . TYR B  1 321 ? -11.690 25.000  -31.391 1.00 26.35 ? 321 TYR D C     1 
ATOM   5392  O O     . TYR B  1 321 ? -10.678 24.395  -31.023 1.00 27.38 ? 321 TYR D O     1 
ATOM   5393  C CB    . TYR B  1 321 ? -11.169 25.698  -33.692 1.00 30.05 ? 321 TYR D CB    1 
ATOM   5394  C CG    . TYR B  1 321 ? -11.154 26.721  -34.794 1.00 39.08 ? 321 TYR D CG    1 
ATOM   5395  C CD1   . TYR B  1 321 ? -12.328 27.065  -35.466 1.00 40.64 ? 321 TYR D CD1   1 
ATOM   5396  C CD2   . TYR B  1 321 ? -9.962  27.325  -35.191 1.00 36.43 ? 321 TYR D CD2   1 
ATOM   5397  C CE1   . TYR B  1 321 ? -12.316 27.985  -36.486 1.00 38.46 ? 321 TYR D CE1   1 
ATOM   5398  C CE2   . TYR B  1 321 ? -9.939  28.248  -36.212 1.00 33.52 ? 321 TYR D CE2   1 
ATOM   5399  C CZ    . TYR B  1 321 ? -11.121 28.577  -36.853 1.00 39.65 ? 321 TYR D CZ    1 
ATOM   5400  O OH    . TYR B  1 321 ? -11.122 29.504  -37.867 1.00 49.10 ? 321 TYR D OH    1 
ATOM   5401  N N     . VAL B  1 322 ? -12.922 24.600  -31.093 1.00 28.42 ? 322 VAL D N     1 
ATOM   5402  C CA    . VAL B  1 322 ? -13.205 23.388  -30.337 1.00 24.65 ? 322 VAL D CA    1 
ATOM   5403  C C     . VAL B  1 322 ? -14.497 22.783  -30.868 1.00 24.78 ? 322 VAL D C     1 
ATOM   5404  O O     . VAL B  1 322 ? -15.389 23.502  -31.335 1.00 27.59 ? 322 VAL D O     1 
ATOM   5405  C CB    . VAL B  1 322 ? -13.316 23.686  -28.839 1.00 23.69 ? 322 VAL D CB    1 
ATOM   5406  C CG1   . VAL B  1 322 ? -14.607 24.474  -28.550 1.00 23.27 ? 322 VAL D CG1   1 
ATOM   5407  C CG2   . VAL B  1 322 ? -13.260 22.389  -28.058 1.00 27.29 ? 322 VAL D CG2   1 
ATOM   5408  N N     . ASN B  1 323 ? -14.592 21.451  -30.816 1.00 23.35 ? 323 ASN D N     1 
ATOM   5409  C CA    . ASN B  1 323 ? -15.783 20.738  -31.271 1.00 30.20 ? 323 ASN D CA    1 
ATOM   5410  C C     . ASN B  1 323 ? -16.207 19.698  -30.245 1.00 33.27 ? 323 ASN D C     1 
ATOM   5411  O O     . ASN B  1 323 ? -15.379 19.173  -29.506 1.00 39.61 ? 323 ASN D O     1 
ATOM   5412  C CB    . ASN B  1 323 ? -15.559 20.042  -32.615 1.00 27.78 ? 323 ASN D CB    1 
ATOM   5413  C CG    . ASN B  1 323 ? -14.328 19.195  -32.617 1.00 33.61 ? 323 ASN D CG    1 
ATOM   5414  O OD1   . ASN B  1 323 ? -13.248 19.640  -33.055 1.00 34.31 ? 323 ASN D OD1   1 
ATOM   5415  N ND2   . ASN B  1 323 ? -14.461 17.964  -32.123 1.00 30.78 ? 323 ASN D ND2   1 
ATOM   5416  N N     . ILE B  1 324 ? -17.499 19.385  -30.215 1.00 28.16 ? 324 ILE D N     1 
ATOM   5417  C CA    . ILE B  1 324 ? -18.060 18.448  -29.253 1.00 29.58 ? 324 ILE D CA    1 
ATOM   5418  C C     . ILE B  1 324 ? -18.754 17.313  -30.021 1.00 34.53 ? 324 ILE D C     1 
ATOM   5419  O O     . ILE B  1 324 ? -19.648 17.561  -30.842 1.00 33.78 ? 324 ILE D O     1 
ATOM   5420  C CB    . ILE B  1 324 ? -18.997 19.176  -28.262 1.00 35.00 ? 324 ILE D CB    1 
ATOM   5421  C CG1   . ILE B  1 324 ? -19.189 18.402  -26.962 1.00 34.74 ? 324 ILE D CG1   1 
ATOM   5422  C CG2   . ILE B  1 324 ? -20.349 19.615  -28.858 1.00 34.85 ? 324 ILE D CG2   1 
ATOM   5423  C CD1   . ILE B  1 324 ? -19.309 19.315  -25.795 1.00 34.70 ? 324 ILE D CD1   1 
ATOM   5424  N N     . ASP B  1 325 ? -18.288 16.077  -29.815 1.00 31.34 ? 325 ASP D N     1 
ATOM   5425  C CA    . ASP B  1 325 ? -18.946 14.925  -30.425 1.00 33.84 ? 325 ASP D CA    1 
ATOM   5426  C C     . ASP B  1 325 ? -20.208 14.578  -29.626 1.00 40.61 ? 325 ASP D C     1 
ATOM   5427  O O     . ASP B  1 325 ? -20.316 14.895  -28.430 1.00 34.84 ? 325 ASP D O     1 
ATOM   5428  C CB    . ASP B  1 325 ? -18.016 13.688  -30.484 1.00 30.67 ? 325 ASP D CB    1 
ATOM   5429  C CG    . ASP B  1 325 ? -16.645 13.969  -31.114 1.00 41.85 ? 325 ASP D CG    1 
ATOM   5430  O OD1   . ASP B  1 325 ? -16.392 15.125  -31.532 1.00 43.03 ? 325 ASP D OD1   1 
ATOM   5431  O OD2   . ASP B  1 325 ? -15.808 13.015  -31.193 1.00 43.72 ? 325 ASP D OD2   1 
ATOM   5432  N N     . GLY B  1 326 ? -21.157 13.895  -30.290 1.00 39.53 ? 326 GLY D N     1 
ATOM   5433  C CA    . GLY B  1 326 ? -22.380 13.430  -29.636 1.00 32.91 ? 326 GLY D CA    1 
ATOM   5434  C C     . GLY B  1 326 ? -23.252 12.560  -30.527 1.00 40.83 ? 326 GLY D C     1 
ATOM   5435  O O     . GLY B  1 326 ? -23.064 12.484  -31.748 1.00 38.23 ? 326 GLY D O     1 
ATOM   5436  N N     . ILE B  1 327 ? -24.233 11.903  -29.893 1.00 35.12 ? 327 ILE D N     1 
ATOM   5437  C CA    . ILE B  1 327 ? -25.205 11.078  -30.601 1.00 38.73 ? 327 ILE D CA    1 
ATOM   5438  C C     . ILE B  1 327 ? -26.628 11.533  -30.286 1.00 42.42 ? 327 ILE D C     1 
ATOM   5439  O O     . ILE B  1 327 ? -26.875 12.294  -29.351 1.00 43.05 ? 327 ILE D O     1 
ATOM   5440  C CB    . ILE B  1 327 ? -25.071 9.587   -30.265 1.00 38.91 ? 327 ILE D CB    1 
ATOM   5441  C CG1   . ILE B  1 327 ? -25.432 9.360   -28.811 1.00 36.47 ? 327 ILE D CG1   1 
ATOM   5442  C CG2   . ILE B  1 327 ? -23.686 9.094   -30.566 1.00 41.33 ? 327 ILE D CG2   1 
ATOM   5443  C CD1   . ILE B  1 327 ? -25.227 7.948   -28.389 1.00 37.34 ? 327 ILE D CD1   1 
ATOM   5444  N N     . VAL B  1 328 ? -27.573 11.023  -31.088 1.00 46.32 ? 328 VAL D N     1 
ATOM   5445  C CA    . VAL B  1 328 ? -29.014 11.107  -30.842 1.00 42.44 ? 328 VAL D CA    1 
ATOM   5446  C C     . VAL B  1 328 ? -29.626 9.739   -31.115 1.00 46.45 ? 328 VAL D C     1 
ATOM   5447  O O     . VAL B  1 328 ? -29.293 9.087   -32.114 1.00 51.87 ? 328 VAL D O     1 
ATOM   5448  C CB    . VAL B  1 328 ? -29.700 12.185  -31.710 1.00 44.82 ? 328 VAL D CB    1 
ATOM   5449  C CG1   . VAL B  1 328 ? -31.192 12.179  -31.496 1.00 43.29 ? 328 VAL D CG1   1 
ATOM   5450  C CG2   . VAL B  1 328 ? -29.142 13.563  -31.393 1.00 46.21 ? 328 VAL D CG2   1 
ATOM   5451  N N     . LEU B  1 329 ? -30.522 9.306   -30.234 1.00 47.40 ? 329 LEU D N     1 
ATOM   5452  C CA    . LEU B  1 329 ? -31.070 7.956   -30.251 1.00 45.26 ? 329 LEU D CA    1 
ATOM   5453  C C     . LEU B  1 329 ? -32.450 7.932   -30.901 1.00 50.25 ? 329 LEU D C     1 
ATOM   5454  O O     . LEU B  1 329 ? -33.113 8.963   -31.069 1.00 51.01 ? 329 LEU D O     1 
ATOM   5455  C CB    . LEU B  1 329 ? -31.159 7.397   -28.827 1.00 49.61 ? 329 LEU D CB    1 
ATOM   5456  C CG    . LEU B  1 329 ? -29.931 6.924   -28.032 1.00 46.95 ? 329 LEU D CG    1 
ATOM   5457  C CD1   . LEU B  1 329 ? -29.552 5.506   -28.404 1.00 47.80 ? 329 LEU D CD1   1 
ATOM   5458  C CD2   . LEU B  1 329 ? -28.734 7.852   -28.176 1.00 44.97 ? 329 LEU D CD2   1 
ATOM   5459  N N     . ASP B  1 330 ? -32.884 6.727   -31.273 1.00 54.54 ? 330 ASP D N     1 
ATOM   5460  C CA    . ASP B  1 330 ? -34.212 6.590   -31.867 1.00 51.78 ? 330 ASP D CA    1 
ATOM   5461  C C     . ASP B  1 330 ? -35.291 7.098   -30.914 1.00 53.30 ? 330 ASP D C     1 
ATOM   5462  O O     . ASP B  1 330 ? -36.114 7.949   -31.281 1.00 58.81 ? 330 ASP D O     1 
ATOM   5463  C CB    . ASP B  1 330 ? -34.453 5.138   -32.307 1.00 54.97 ? 330 ASP D CB    1 
ATOM   5464  C CG    . ASP B  1 330 ? -34.604 4.148   -31.136 1.00 66.77 ? 330 ASP D CG    1 
ATOM   5465  O OD1   . ASP B  1 330 ? -34.524 4.560   -29.951 1.00 65.35 ? 330 ASP D OD1   1 
ATOM   5466  O OD2   . ASP B  1 330 ? -34.801 2.941   -31.421 1.00 67.28 ? 330 ASP D OD2   1 
ATOM   5467  N N     . ASP B  1 331 ? -35.264 6.626   -29.665 1.00 52.88 ? 331 ASP D N     1 
ATOM   5468  C CA    . ASP B  1 331 ? -36.226 7.100   -28.683 1.00 48.69 ? 331 ASP D CA    1 
ATOM   5469  C C     . ASP B  1 331 ? -36.116 8.608   -28.502 1.00 52.28 ? 331 ASP D C     1 
ATOM   5470  O O     . ASP B  1 331 ? -37.128 9.319   -28.510 1.00 59.01 ? 331 ASP D O     1 
ATOM   5471  C CB    . ASP B  1 331 ? -36.043 6.360   -27.353 1.00 54.04 ? 331 ASP D CB    1 
ATOM   5472  C CG    . ASP B  1 331 ? -34.654 6.557   -26.720 1.00 55.74 ? 331 ASP D CG    1 
ATOM   5473  O OD1   . ASP B  1 331 ? -34.095 7.680   -26.757 1.00 53.40 ? 331 ASP D OD1   1 
ATOM   5474  O OD2   . ASP B  1 331 ? -34.137 5.582   -26.130 1.00 46.04 ? 331 ASP D OD2   1 
ATOM   5475  N N     . GLY B  1 332 ? -34.886 9.116   -28.359 1.00 49.65 ? 332 GLY D N     1 
ATOM   5476  C CA    . GLY B  1 332 ? -34.638 10.548  -28.346 1.00 51.55 ? 332 GLY D CA    1 
ATOM   5477  C C     . GLY B  1 332 ? -33.513 11.055  -27.456 1.00 49.05 ? 332 GLY D C     1 
ATOM   5478  O O     . GLY B  1 332 ? -33.134 12.228  -27.560 1.00 39.54 ? 332 GLY D O     1 
ATOM   5479  N N     . ARG B  1 333 ? -32.971 10.200  -26.583 1.00 47.30 ? 333 ARG D N     1 
ATOM   5480  C CA    . ARG B  1 333 ? -31.989 10.659  -25.605 1.00 42.85 ? 333 ARG D CA    1 
ATOM   5481  C C     . ARG B  1 333 ? -30.733 11.163  -26.298 1.00 42.69 ? 333 ARG D C     1 
ATOM   5482  O O     . ARG B  1 333 ? -30.243 10.559  -27.256 1.00 44.06 ? 333 ARG D O     1 
ATOM   5483  C CB    . ARG B  1 333 ? -31.626 9.542   -24.629 1.00 39.95 ? 333 ARG D CB    1 
ATOM   5484  C CG    . ARG B  1 333 ? -32.522 9.460   -23.396 1.00 32.88 ? 333 ARG D CG    1 
ATOM   5485  C CD    . ARG B  1 333 ? -32.160 8.241   -22.571 1.00 31.12 ? 333 ARG D CD    1 
ATOM   5486  N NE    . ARG B  1 333 ? -32.051 7.065   -23.425 1.00 41.48 ? 333 ARG D NE    1 
ATOM   5487  C CZ    . ARG B  1 333 ? -31.444 5.935   -23.092 1.00 42.28 ? 333 ARG D CZ    1 
ATOM   5488  N NH1   . ARG B  1 333 ? -30.851 5.785   -21.921 1.00 46.87 ? 333 ARG D NH1   1 
ATOM   5489  N NH2   . ARG B  1 333 ? -31.423 4.933   -23.962 1.00 44.30 ? 333 ARG D NH2   1 
ATOM   5490  N N     . VAL B  1 334 ? -30.225 12.281  -25.812 1.00 34.16 ? 334 VAL D N     1 
ATOM   5491  C CA    . VAL B  1 334 ? -29.060 12.930  -26.385 1.00 34.93 ? 334 VAL D CA    1 
ATOM   5492  C C     . VAL B  1 334 ? -27.862 12.629  -25.501 1.00 39.32 ? 334 VAL D C     1 
ATOM   5493  O O     . VAL B  1 334 ? -27.994 12.528  -24.275 1.00 43.19 ? 334 VAL D O     1 
ATOM   5494  C CB    . VAL B  1 334 ? -29.311 14.442  -26.530 1.00 37.63 ? 334 VAL D CB    1 
ATOM   5495  C CG1   . VAL B  1 334 ? -28.006 15.227  -26.624 1.00 34.70 ? 334 VAL D CG1   1 
ATOM   5496  C CG2   . VAL B  1 334 ? -30.176 14.690  -27.758 1.00 37.24 ? 334 VAL D CG2   1 
ATOM   5497  N N     . PHE B  1 335 ? -26.693 12.460  -26.120 1.00 42.08 ? 335 PHE D N     1 
ATOM   5498  C CA    . PHE B  1 335 ? -25.474 12.131  -25.391 1.00 41.27 ? 335 PHE D CA    1 
ATOM   5499  C C     . PHE B  1 335 ? -24.292 12.809  -26.062 1.00 38.34 ? 335 PHE D C     1 
ATOM   5500  O O     . PHE B  1 335 ? -24.281 12.966  -27.286 1.00 38.59 ? 335 PHE D O     1 
ATOM   5501  C CB    . PHE B  1 335 ? -25.225 10.619  -25.358 1.00 40.53 ? 335 PHE D CB    1 
ATOM   5502  C CG    . PHE B  1 335 ? -26.132 9.866   -24.436 1.00 40.94 ? 335 PHE D CG    1 
ATOM   5503  C CD1   . PHE B  1 335 ? -26.366 10.314  -23.150 1.00 43.03 ? 335 PHE D CD1   1 
ATOM   5504  C CD2   . PHE B  1 335 ? -26.731 8.686   -24.854 1.00 45.41 ? 335 PHE D CD2   1 
ATOM   5505  C CE1   . PHE B  1 335 ? -27.196 9.603   -22.306 1.00 44.97 ? 335 PHE D CE1   1 
ATOM   5506  C CE2   . PHE B  1 335 ? -27.561 7.970   -24.018 1.00 41.62 ? 335 PHE D CE2   1 
ATOM   5507  C CZ    . PHE B  1 335 ? -27.795 8.430   -22.746 1.00 44.88 ? 335 PHE D CZ    1 
ATOM   5508  N N     . PHE B  1 336 ? -23.282 13.179  -25.257 1.00 32.16 ? 336 PHE D N     1 
ATOM   5509  C CA    . PHE B  1 336 ? -22.036 13.743  -25.762 1.00 26.68 ? 336 PHE D CA    1 
ATOM   5510  C C     . PHE B  1 336 ? -20.862 12.866  -25.348 1.00 30.14 ? 336 PHE D C     1 
ATOM   5511  O O     . PHE B  1 336 ? -20.910 12.199  -24.307 1.00 30.70 ? 336 PHE D O     1 
ATOM   5512  C CB    . PHE B  1 336 ? -21.855 15.170  -25.263 1.00 29.28 ? 336 PHE D CB    1 
ATOM   5513  C CG    . PHE B  1 336 ? -22.949 16.092  -25.718 1.00 35.74 ? 336 PHE D CG    1 
ATOM   5514  C CD1   . PHE B  1 336 ? -23.031 16.483  -27.046 1.00 35.55 ? 336 PHE D CD1   1 
ATOM   5515  C CD2   . PHE B  1 336 ? -23.933 16.519  -24.839 1.00 34.32 ? 336 PHE D CD2   1 
ATOM   5516  C CE1   . PHE B  1 336 ? -24.060 17.312  -27.483 1.00 35.25 ? 336 PHE D CE1   1 
ATOM   5517  C CE2   . PHE B  1 336 ? -24.961 17.346  -25.274 1.00 34.86 ? 336 PHE D CE2   1 
ATOM   5518  C CZ    . PHE B  1 336 ? -25.023 17.743  -26.600 1.00 31.10 ? 336 PHE D CZ    1 
ATOM   5519  N N     . HIS B  1 337 ? -19.809 12.854  -26.177 1.00 27.66 ? 337 HIS D N     1 
ATOM   5520  C CA    . HIS B  1 337 ? -18.634 12.023  -25.920 1.00 27.88 ? 337 HIS D CA    1 
ATOM   5521  C C     . HIS B  1 337 ? -17.396 12.807  -25.501 1.00 30.65 ? 337 HIS D C     1 
ATOM   5522  O O     . HIS B  1 337 ? -16.737 12.448  -24.522 1.00 31.87 ? 337 HIS D O     1 
ATOM   5523  C CB    . HIS B  1 337 ? -18.266 11.187  -27.147 1.00 28.71 ? 337 HIS D CB    1 
ATOM   5524  C CG    . HIS B  1 337 ? -19.437 10.613  -27.873 1.00 31.05 ? 337 HIS D CG    1 
ATOM   5525  N ND1   . HIS B  1 337 ? -20.299 9.709   -27.295 1.00 32.44 ? 337 HIS D ND1   1 
ATOM   5526  C CD2   . HIS B  1 337 ? -19.872 10.793  -29.144 1.00 35.72 ? 337 HIS D CD2   1 
ATOM   5527  C CE1   . HIS B  1 337 ? -21.222 9.362   -28.172 1.00 35.56 ? 337 HIS D CE1   1 
ATOM   5528  N NE2   . HIS B  1 337 ? -20.985 10.005  -29.303 1.00 38.19 ? 337 HIS D NE2   1 
ATOM   5529  N N     . GLU B  1 338 ? -17.009 13.830  -26.253 1.00 32.90 ? 338 GLU D N     1 
ATOM   5530  C CA    . GLU B  1 338 ? -15.746 14.498  -25.987 1.00 32.77 ? 338 GLU D CA    1 
ATOM   5531  C C     . GLU B  1 338 ? -15.828 15.901  -26.560 1.00 27.12 ? 338 GLU D C     1 
ATOM   5532  O O     . GLU B  1 338 ? -16.733 16.222  -27.321 1.00 32.35 ? 338 GLU D O     1 
ATOM   5533  C CB    . GLU B  1 338 ? -14.551 13.719  -26.582 1.00 27.30 ? 338 GLU D CB    1 
ATOM   5534  C CG    . GLU B  1 338 ? -14.605 13.550  -28.094 1.00 31.72 ? 338 GLU D CG    1 
ATOM   5535  C CD    . GLU B  1 338 ? -13.359 12.898  -28.674 1.00 34.92 ? 338 GLU D CD    1 
ATOM   5536  O OE1   . GLU B  1 338 ? -12.710 12.135  -27.954 1.00 39.59 ? 338 GLU D OE1   1 
ATOM   5537  O OE2   . GLU B  1 338 ? -13.025 13.126  -29.851 1.00 30.93 ? 338 GLU D OE2   1 
ATOM   5538  N N     . ILE B  1 339 ? -14.913 16.749  -26.120 1.00 30.17 ? 339 ILE D N     1 
ATOM   5539  C CA    . ILE B  1 339 ? -14.463 17.899  -26.889 1.00 30.00 ? 339 ILE D CA    1 
ATOM   5540  C C     . ILE B  1 339 ? -13.030 17.612  -27.295 1.00 28.24 ? 339 ILE D C     1 
ATOM   5541  O O     . ILE B  1 339 ? -12.247 17.068  -26.510 1.00 31.37 ? 339 ILE D O     1 
ATOM   5542  C CB    . ILE B  1 339 ? -14.519 19.240  -26.125 1.00 31.35 ? 339 ILE D CB    1 
ATOM   5543  C CG1   . ILE B  1 339 ? -13.895 19.108  -24.742 1.00 25.29 ? 339 ILE D CG1   1 
ATOM   5544  C CG2   . ILE B  1 339 ? -15.929 19.761  -26.036 1.00 36.31 ? 339 ILE D CG2   1 
ATOM   5545  C CD1   . ILE B  1 339 ? -13.039 20.297  -24.383 1.00 25.67 ? 339 ILE D CD1   1 
ATOM   5546  N N     . ASN B  1 340 ? -12.696 17.964  -28.521 1.00 31.56 ? 340 ASN D N     1 
ATOM   5547  C CA    . ASN B  1 340 ? -11.317 18.058  -28.967 1.00 31.10 ? 340 ASN D CA    1 
ATOM   5548  C C     . ASN B  1 340 ? -11.069 19.547  -29.181 1.00 26.71 ? 340 ASN D C     1 
ATOM   5549  O O     . ASN B  1 340 ? -11.826 20.204  -29.904 1.00 29.16 ? 340 ASN D O     1 
ATOM   5550  C CB    . ASN B  1 340 ? -11.087 17.214  -30.232 1.00 30.51 ? 340 ASN D CB    1 
ATOM   5551  C CG    . ASN B  1 340 ? -11.818 15.838  -30.183 1.00 31.72 ? 340 ASN D CG    1 
ATOM   5552  O OD1   . ASN B  1 340 ? -12.985 15.744  -30.547 1.00 37.84 ? 340 ASN D OD1   1 
ATOM   5553  N ND2   . ASN B  1 340 ? -11.125 14.780  -29.743 1.00 32.25 ? 340 ASN D ND2   1 
ATOM   5554  N N     . ALA B  1 341 ? -10.089 20.103  -28.467 1.00 29.73 ? 341 ALA D N     1 
ATOM   5555  C CA    . ALA B  1 341 ? -9.709  21.515  -28.622 1.00 30.99 ? 341 ALA D CA    1 
ATOM   5556  C C     . ALA B  1 341 ? -8.667  21.607  -29.728 1.00 29.81 ? 341 ALA D C     1 
ATOM   5557  O O     . ALA B  1 341 ? -7.468  21.776  -29.487 1.00 27.56 ? 341 ALA D O     1 
ATOM   5558  C CB    . ALA B  1 341 ? -9.183  22.100  -27.314 1.00 28.76 ? 341 ALA D CB    1 
ATOM   5559  N N     . ARG B  1 342 ? -9.151  21.470  -30.961 1.00 29.45 ? 342 ARG D N     1 
ATOM   5560  C CA    . ARG B  1 342 ? -8.334  21.451  -32.170 1.00 28.55 ? 342 ARG D CA    1 
ATOM   5561  C C     . ARG B  1 342 ? -9.302  21.528  -33.352 1.00 35.16 ? 342 ARG D C     1 
ATOM   5562  O O     . ARG B  1 342 ? -10.525 21.555  -33.163 1.00 36.10 ? 342 ARG D O     1 
ATOM   5563  C CB    . ARG B  1 342 ? -7.424  20.215  -32.198 1.00 29.48 ? 342 ARG D CB    1 
ATOM   5564  C CG    . ARG B  1 342 ? -8.134  18.860  -32.046 1.00 33.79 ? 342 ARG D CG    1 
ATOM   5565  C CD    . ARG B  1 342 ? -8.405  18.219  -33.434 1.00 48.11 ? 342 ARG D CD    1 
ATOM   5566  N NE    . ARG B  1 342 ? -8.820  16.808  -33.471 1.00 54.08 ? 342 ARG D NE    1 
ATOM   5567  C CZ    . ARG B  1 342 ? -10.064 16.369  -33.677 1.00 45.54 ? 342 ARG D CZ    1 
ATOM   5568  N NH1   . ARG B  1 342 ? -11.093 17.201  -33.759 1.00 41.73 ? 342 ARG D NH1   1 
ATOM   5569  N NH2   . ARG B  1 342 ? -10.281 15.058  -33.797 1.00 43.55 ? 342 ARG D NH2   1 
ATOM   5570  N N     . TRP B  1 343 ? -8.753  21.603  -34.572 1.00 36.19 ? 343 TRP D N     1 
ATOM   5571  C CA    . TRP B  1 343 ? -9.594  21.594  -35.771 1.00 28.65 ? 343 TRP D CA    1 
ATOM   5572  C C     . TRP B  1 343 ? -10.356 20.286  -35.819 1.00 31.50 ? 343 TRP D C     1 
ATOM   5573  O O     . TRP B  1 343 ? -9.755  19.214  -35.752 1.00 35.38 ? 343 TRP D O     1 
ATOM   5574  C CB    . TRP B  1 343 ? -8.750  21.731  -37.042 1.00 25.48 ? 343 TRP D CB    1 
ATOM   5575  C CG    . TRP B  1 343 ? -7.873  22.966  -37.136 1.00 32.61 ? 343 TRP D CG    1 
ATOM   5576  C CD1   . TRP B  1 343 ? -8.064  24.175  -36.509 1.00 34.02 ? 343 TRP D CD1   1 
ATOM   5577  C CD2   . TRP B  1 343 ? -6.684  23.116  -37.929 1.00 31.04 ? 343 TRP D CD2   1 
ATOM   5578  N NE1   . TRP B  1 343 ? -7.062  25.055  -36.862 1.00 37.95 ? 343 TRP D NE1   1 
ATOM   5579  C CE2   . TRP B  1 343 ? -6.208  24.430  -37.733 1.00 34.53 ? 343 TRP D CE2   1 
ATOM   5580  C CE3   . TRP B  1 343 ? -5.972  22.264  -38.774 1.00 31.85 ? 343 TRP D CE3   1 
ATOM   5581  C CZ2   . TRP B  1 343 ? -5.051  24.904  -38.351 1.00 38.05 ? 343 TRP D CZ2   1 
ATOM   5582  C CZ3   . TRP B  1 343 ? -4.830  22.746  -39.396 1.00 34.84 ? 343 TRP D CZ3   1 
ATOM   5583  C CH2   . TRP B  1 343 ? -4.381  24.046  -39.180 1.00 30.48 ? 343 TRP D CH2   1 
ATOM   5584  N N     . SER B  1 344 ? -11.679 20.359  -35.937 1.00 31.10 ? 344 SER D N     1 
ATOM   5585  C CA    . SER B  1 344 ? -12.450 19.123  -35.926 1.00 28.50 ? 344 SER D CA    1 
ATOM   5586  C C     . SER B  1 344 ? -11.949 18.098  -36.924 1.00 31.55 ? 344 SER D C     1 
ATOM   5587  O O     . SER B  1 344 ? -12.130 16.900  -36.697 1.00 38.33 ? 344 SER D O     1 
ATOM   5588  C CB    . SER B  1 344 ? -13.900 19.403  -36.209 1.00 26.79 ? 344 SER D CB    1 
ATOM   5589  O OG    . SER B  1 344 ? -14.023 20.025  -37.463 1.00 29.81 ? 344 SER D OG    1 
ATOM   5590  N N     . GLY B  1 345 ? -11.279 18.517  -37.991 1.00 27.03 ? 345 GLY D N     1 
ATOM   5591  C CA    . GLY B  1 345 ? -10.999 17.631  -39.096 1.00 33.50 ? 345 GLY D CA    1 
ATOM   5592  C C     . GLY B  1 345 ? -11.976 17.762  -40.246 1.00 33.15 ? 345 GLY D C     1 
ATOM   5593  O O     . GLY B  1 345 ? -11.642 17.404  -41.378 1.00 33.86 ? 345 GLY D O     1 
ATOM   5594  N N     . GLY B  1 346 ? -13.182 18.250  -39.978 1.00 32.51 ? 346 GLY D N     1 
ATOM   5595  C CA    . GLY B  1 346 ? -14.054 18.773  -41.003 1.00 34.95 ? 346 GLY D CA    1 
ATOM   5596  C C     . GLY B  1 346 ? -14.133 20.283  -40.998 1.00 33.43 ? 346 GLY D C     1 
ATOM   5597  O O     . GLY B  1 346 ? -14.951 20.849  -41.736 1.00 37.16 ? 346 GLY D O     1 
ATOM   5598  N N     . LEU B  1 347 ? -13.333 20.963  -40.176 1.00 29.60 ? 347 LEU D N     1 
ATOM   5599  C CA    . LEU B  1 347 ? -13.231 22.412  -40.281 1.00 28.95 ? 347 LEU D CA    1 
ATOM   5600  C C     . LEU B  1 347 ? -12.875 22.808  -41.702 1.00 35.54 ? 347 LEU D C     1 
ATOM   5601  O O     . LEU B  1 347 ? -13.441 23.762  -42.256 1.00 36.85 ? 347 LEU D O     1 
ATOM   5602  C CB    . LEU B  1 347 ? -12.192 22.942  -39.283 1.00 26.33 ? 347 LEU D CB    1 
ATOM   5603  C CG    . LEU B  1 347 ? -12.008 24.456  -39.134 1.00 31.31 ? 347 LEU D CG    1 
ATOM   5604  C CD1   . LEU B  1 347 ? -13.190 25.112  -38.433 1.00 29.68 ? 347 LEU D CD1   1 
ATOM   5605  C CD2   . LEU B  1 347 ? -10.760 24.750  -38.350 1.00 35.75 ? 347 LEU D CD2   1 
ATOM   5606  N N     . ILE B  1 348 ? -11.965 22.052  -42.325 1.00 32.56 ? 348 ILE D N     1 
ATOM   5607  C CA    . ILE B  1 348 ? -11.545 22.375  -43.681 1.00 32.51 ? 348 ILE D CA    1 
ATOM   5608  C C     . ILE B  1 348 ? -12.733 22.312  -44.626 1.00 31.24 ? 348 ILE D C     1 
ATOM   5609  O O     . ILE B  1 348 ? -12.918 23.196  -45.475 1.00 34.45 ? 348 ILE D O     1 
ATOM   5610  C CB    . ILE B  1 348 ? -10.392 21.447  -44.117 1.00 34.82 ? 348 ILE D CB    1 
ATOM   5611  C CG1   . ILE B  1 348 ? -9.721  21.973  -45.393 1.00 32.06 ? 348 ILE D CG1   1 
ATOM   5612  C CG2   . ILE B  1 348 ? -10.877 20.012  -44.253 1.00 29.55 ? 348 ILE D CG2   1 
ATOM   5613  C CD1   . ILE B  1 348 ? -9.301  23.422  -45.286 1.00 31.77 ? 348 ILE D CD1   1 
ATOM   5614  N N     . TYR B  1 349 ? -13.584 21.297  -44.462 1.00 30.96 ? 349 TYR D N     1 
ATOM   5615  C CA    . TYR B  1 349 ? -14.788 21.186  -45.277 1.00 35.50 ? 349 TYR D CA    1 
ATOM   5616  C C     . TYR B  1 349 ? -15.618 22.453  -45.171 1.00 34.62 ? 349 TYR D C     1 
ATOM   5617  O O     . TYR B  1 349 ? -16.026 23.042  -46.176 1.00 30.30 ? 349 TYR D O     1 
ATOM   5618  C CB    . TYR B  1 349 ? -15.610 19.980  -44.828 1.00 31.99 ? 349 TYR D CB    1 
ATOM   5619  C CG    . TYR B  1 349 ? -14.948 18.643  -45.065 1.00 32.37 ? 349 TYR D CG    1 
ATOM   5620  C CD1   . TYR B  1 349 ? -13.819 18.527  -45.874 1.00 34.08 ? 349 TYR D CD1   1 
ATOM   5621  C CD2   . TYR B  1 349 ? -15.470 17.488  -44.495 1.00 29.17 ? 349 TYR D CD2   1 
ATOM   5622  C CE1   . TYR B  1 349 ? -13.223 17.293  -46.099 1.00 32.12 ? 349 TYR D CE1   1 
ATOM   5623  C CE2   . TYR B  1 349 ? -14.893 16.265  -44.708 1.00 28.79 ? 349 TYR D CE2   1 
ATOM   5624  C CZ    . TYR B  1 349 ? -13.767 16.164  -45.505 1.00 35.61 ? 349 TYR D CZ    1 
ATOM   5625  O OH    . TYR B  1 349 ? -13.201 14.923  -45.701 1.00 38.01 ? 349 TYR D OH    1 
ATOM   5626  N N     . HIS B  1 350 ? -15.831 22.901  -43.941 1.00 30.88 ? 350 HIS D N     1 
ATOM   5627  C CA    . HIS B  1 350 ? -16.633 24.088  -43.680 1.00 33.01 ? 350 HIS D CA    1 
ATOM   5628  C C     . HIS B  1 350 ? -15.988 25.329  -44.276 1.00 34.28 ? 350 HIS D C     1 
ATOM   5629  O O     . HIS B  1 350 ? -16.661 26.136  -44.932 1.00 35.19 ? 350 HIS D O     1 
ATOM   5630  C CB    . HIS B  1 350 ? -16.808 24.221  -42.175 1.00 33.30 ? 350 HIS D CB    1 
ATOM   5631  C CG    . HIS B  1 350 ? -17.289 25.557  -41.725 1.00 36.14 ? 350 HIS D CG    1 
ATOM   5632  N ND1   . HIS B  1 350 ? -18.606 25.948  -41.837 1.00 36.16 ? 350 HIS D ND1   1 
ATOM   5633  C CD2   . HIS B  1 350 ? -16.639 26.578  -41.114 1.00 35.75 ? 350 HIS D CD2   1 
ATOM   5634  C CE1   . HIS B  1 350 ? -18.742 27.164  -41.336 1.00 36.25 ? 350 HIS D CE1   1 
ATOM   5635  N NE2   . HIS B  1 350 ? -17.565 27.566  -40.885 1.00 38.48 ? 350 HIS D NE2   1 
ATOM   5636  N N     . THR B  1 351 ? -14.678 25.503  -44.060 1.00 33.08 ? 351 THR D N     1 
ATOM   5637  C CA    . THR B  1 351 ? -13.999 26.651  -44.654 1.00 36.51 ? 351 THR D CA    1 
ATOM   5638  C C     . THR B  1 351 ? -14.256 26.678  -46.141 1.00 35.82 ? 351 THR D C     1 
ATOM   5639  O O     . THR B  1 351 ? -14.677 27.703  -46.695 1.00 35.44 ? 351 THR D O     1 
ATOM   5640  C CB    . THR B  1 351 ? -12.487 26.620  -44.400 1.00 38.64 ? 351 THR D CB    1 
ATOM   5641  O OG1   . THR B  1 351 ? -12.184 27.080  -43.072 1.00 30.63 ? 351 THR D OG1   1 
ATOM   5642  C CG2   . THR B  1 351 ? -11.773 27.515  -45.416 1.00 30.73 ? 351 THR D CG2   1 
ATOM   5643  N N     . VAL B  1 352 ? -14.053 25.528  -46.789 1.00 33.75 ? 352 VAL D N     1 
ATOM   5644  C CA    . VAL B  1 352 ? -14.199 25.453  -48.239 1.00 33.32 ? 352 VAL D CA    1 
ATOM   5645  C C     . VAL B  1 352 ? -15.577 25.946  -48.640 1.00 36.99 ? 352 VAL D C     1 
ATOM   5646  O O     . VAL B  1 352 ? -15.723 26.864  -49.462 1.00 40.50 ? 352 VAL D O     1 
ATOM   5647  C CB    . VAL B  1 352 ? -13.941 24.018  -48.735 1.00 32.73 ? 352 VAL D CB    1 
ATOM   5648  C CG1   . VAL B  1 352 ? -14.114 23.945  -50.239 1.00 30.95 ? 352 VAL D CG1   1 
ATOM   5649  C CG2   . VAL B  1 352 ? -12.533 23.584  -48.390 1.00 30.99 ? 352 VAL D CG2   1 
ATOM   5650  N N     . ALA B  1 353 ? -16.606 25.375  -48.015 1.00 35.45 ? 353 ALA D N     1 
ATOM   5651  C CA    . ALA B  1 353 ? -17.979 25.726  -48.340 1.00 32.51 ? 353 ALA D CA    1 
ATOM   5652  C C     . ALA B  1 353 ? -18.189 27.232  -48.263 1.00 35.64 ? 353 ALA D C     1 
ATOM   5653  O O     . ALA B  1 353 ? -18.693 27.846  -49.207 1.00 37.21 ? 353 ALA D O     1 
ATOM   5654  C CB    . ALA B  1 353 ? -18.928 24.982  -47.399 1.00 34.79 ? 353 ALA D CB    1 
ATOM   5655  N N     . GLU B  1 354 ? -17.766 27.851  -47.158 1.00 40.44 ? 354 GLU D N     1 
ATOM   5656  C CA    . GLU B  1 354 ? -17.982 29.282  -46.967 1.00 38.85 ? 354 GLU D CA    1 
ATOM   5657  C C     . GLU B  1 354 ? -17.212 30.115  -47.984 1.00 35.75 ? 354 GLU D C     1 
ATOM   5658  O O     . GLU B  1 354 ? -17.690 31.177  -48.406 1.00 37.04 ? 354 GLU D O     1 
ATOM   5659  C CB    . GLU B  1 354 ? -17.579 29.688  -45.545 1.00 40.72 ? 354 GLU D CB    1 
ATOM   5660  C CG    . GLU B  1 354 ? -18.726 29.666  -44.538 1.00 41.41 ? 354 GLU D CG    1 
ATOM   5661  C CD    . GLU B  1 354 ? -18.357 30.198  -43.137 1.00 49.56 ? 354 GLU D CD    1 
ATOM   5662  O OE1   . GLU B  1 354 ? -17.182 30.578  -42.890 1.00 45.75 ? 354 GLU D OE1   1 
ATOM   5663  O OE2   . GLU B  1 354 ? -19.269 30.227  -42.273 1.00 49.93 ? 354 GLU D OE2   1 
ATOM   5664  N N     . ARG B  1 355 ? -16.026 29.665  -48.387 1.00 32.55 ? 355 ARG D N     1 
ATOM   5665  C CA    . ARG B  1 355 ? -15.231 30.454  -49.316 1.00 30.29 ? 355 ARG D CA    1 
ATOM   5666  C C     . ARG B  1 355 ? -15.707 30.296  -50.752 1.00 33.36 ? 355 ARG D C     1 
ATOM   5667  O O     . ARG B  1 355 ? -15.374 31.128  -51.606 1.00 34.17 ? 355 ARG D O     1 
ATOM   5668  C CB    . ARG B  1 355 ? -13.760 30.065  -49.191 1.00 29.01 ? 355 ARG D CB    1 
ATOM   5669  C CG    . ARG B  1 355 ? -13.157 30.399  -47.828 1.00 33.37 ? 355 ARG D CG    1 
ATOM   5670  C CD    . ARG B  1 355 ? -11.643 30.267  -47.852 1.00 31.75 ? 355 ARG D CD    1 
ATOM   5671  N NE    . ARG B  1 355 ? -11.027 31.293  -48.681 1.00 29.79 ? 355 ARG D NE    1 
ATOM   5672  C CZ    . ARG B  1 355 ? -9.741  31.321  -49.004 1.00 34.99 ? 355 ARG D CZ    1 
ATOM   5673  N NH1   . ARG B  1 355 ? -8.897  30.409  -48.555 1.00 36.21 ? 355 ARG D NH1   1 
ATOM   5674  N NH2   . ARG B  1 355 ? -9.294  32.280  -49.811 1.00 42.16 ? 355 ARG D NH2   1 
ATOM   5675  N N     . LEU B  1 356 ? -16.473 29.248  -51.032 1.00 28.99 ? 356 LEU D N     1 
ATOM   5676  C CA    . LEU B  1 356 ? -17.029 29.004  -52.348 1.00 33.21 ? 356 LEU D CA    1 
ATOM   5677  C C     . LEU B  1 356 ? -18.469 29.463  -52.451 1.00 35.81 ? 356 LEU D C     1 
ATOM   5678  O O     . LEU B  1 356 ? -18.843 30.101  -53.442 1.00 38.09 ? 356 LEU D O     1 
ATOM   5679  C CB    . LEU B  1 356 ? -16.952 27.511  -52.683 1.00 32.51 ? 356 LEU D CB    1 
ATOM   5680  C CG    . LEU B  1 356 ? -15.549 26.955  -52.933 1.00 30.42 ? 356 LEU D CG    1 
ATOM   5681  C CD1   . LEU B  1 356 ? -15.614 25.539  -53.466 1.00 30.13 ? 356 LEU D CD1   1 
ATOM   5682  C CD2   . LEU B  1 356 ? -14.788 27.839  -53.889 1.00 29.31 ? 356 LEU D CD2   1 
ATOM   5683  N N     . LEU B  1 357 ? -19.266 29.185  -51.420 1.00 36.13 ? 357 LEU D N     1 
ATOM   5684  C CA    . LEU B  1 357 ? -20.710 29.349  -51.454 1.00 36.29 ? 357 LEU D CA    1 
ATOM   5685  C C     . LEU B  1 357 ? -21.213 30.523  -50.639 1.00 38.63 ? 357 LEU D C     1 
ATOM   5686  O O     . LEU B  1 357 ? -22.141 31.203  -51.074 1.00 48.83 ? 357 LEU D O     1 
ATOM   5687  C CB    . LEU B  1 357 ? -21.391 28.067  -50.970 1.00 33.21 ? 357 LEU D CB    1 
ATOM   5688  C CG    . LEU B  1 357 ? -20.991 26.859  -51.807 1.00 33.79 ? 357 LEU D CG    1 
ATOM   5689  C CD1   . LEU B  1 357 ? -21.826 25.648  -51.446 1.00 32.72 ? 357 LEU D CD1   1 
ATOM   5690  C CD2   . LEU B  1 357 ? -21.097 27.184  -53.290 1.00 37.79 ? 357 LEU D CD2   1 
ATOM   5691  N N     . GLY B  1 358 ? -20.635 30.798  -49.482 1.00 38.36 ? 358 GLY D N     1 
ATOM   5692  C CA    . GLY B  1 358 ? -21.072 31.935  -48.694 1.00 38.29 ? 358 GLY D CA    1 
ATOM   5693  C C     . GLY B  1 358 ? -21.267 31.606  -47.235 1.00 44.29 ? 358 GLY D C     1 
ATOM   5694  O O     . GLY B  1 358 ? -21.670 30.496  -46.873 1.00 42.38 ? 358 GLY D O     1 
ATOM   5695  N N     . HIS B  1 359 ? -20.970 32.593  -46.378 1.00 44.77 ? 359 HIS D N     1 
ATOM   5696  C CA    . HIS B  1 359 ? -21.136 32.508  -44.928 1.00 42.96 ? 359 HIS D CA    1 
ATOM   5697  C C     . HIS B  1 359 ? -22.327 31.662  -44.524 1.00 38.53 ? 359 HIS D C     1 
ATOM   5698  O O     . HIS B  1 359 ? -22.213 30.791  -43.659 1.00 46.92 ? 359 HIS D O     1 
ATOM   5699  C CB    . HIS B  1 359 ? -21.294 33.902  -44.331 1.00 45.32 ? 359 HIS D CB    1 
ATOM   5700  C CG    . HIS B  1 359 ? -20.003 34.528  -43.898 1.00 54.48 ? 359 HIS D CG    1 
ATOM   5701  N ND1   . HIS B  1 359 ? -19.770 35.889  -43.961 1.00 58.34 ? 359 HIS D ND1   1 
ATOM   5702  C CD2   . HIS B  1 359 ? -18.879 33.980  -43.376 1.00 59.75 ? 359 HIS D CD2   1 
ATOM   5703  C CE1   . HIS B  1 359 ? -18.558 36.149  -43.500 1.00 64.32 ? 359 HIS D CE1   1 
ATOM   5704  N NE2   . HIS B  1 359 ? -17.997 35.008  -43.139 1.00 69.21 ? 359 HIS D NE2   1 
ATOM   5705  N N     . ASP B  1 360 ? -23.466 31.899  -45.166 1.00 38.22 ? 360 ASP D N     1 
ATOM   5706  C CA    . ASP B  1 360 ? -24.712 31.215  -44.856 1.00 43.21 ? 360 ASP D CA    1 
ATOM   5707  C C     . ASP B  1 360 ? -24.917 29.958  -45.695 1.00 39.77 ? 360 ASP D C     1 
ATOM   5708  O O     . ASP B  1 360 ? -26.047 29.472  -45.793 1.00 39.16 ? 360 ASP D O     1 
ATOM   5709  C CB    . ASP B  1 360 ? -25.897 32.169  -45.059 1.00 46.82 ? 360 ASP D CB    1 
ATOM   5710  C CG    . ASP B  1 360 ? -27.187 31.657  -44.413 1.00 57.24 ? 360 ASP D CG    1 
ATOM   5711  O OD1   . ASP B  1 360 ? -27.112 30.937  -43.388 1.00 57.92 ? 360 ASP D OD1   1 
ATOM   5712  O OD2   . ASP B  1 360 ? -28.278 31.950  -44.956 1.00 54.53 ? 360 ASP D OD2   1 
ATOM   5713  N N     . TYR B  1 361 ? -23.856 29.410  -46.282 1.00 38.36 ? 361 TYR D N     1 
ATOM   5714  C CA    . TYR B  1 361 ? -24.026 28.343  -47.265 1.00 42.10 ? 361 TYR D CA    1 
ATOM   5715  C C     . TYR B  1 361 ? -24.958 27.232  -46.800 1.00 41.17 ? 361 TYR D C     1 
ATOM   5716  O O     . TYR B  1 361 ? -25.694 26.669  -47.616 1.00 43.78 ? 361 TYR D O     1 
ATOM   5717  C CB    . TYR B  1 361 ? -22.675 27.742  -47.607 1.00 39.98 ? 361 TYR D CB    1 
ATOM   5718  C CG    . TYR B  1 361 ? -22.076 26.980  -46.451 1.00 38.86 ? 361 TYR D CG    1 
ATOM   5719  C CD1   . TYR B  1 361 ? -21.283 27.616  -45.521 1.00 37.50 ? 361 TYR D CD1   1 
ATOM   5720  C CD2   . TYR B  1 361 ? -22.295 25.620  -46.303 1.00 38.96 ? 361 TYR D CD2   1 
ATOM   5721  C CE1   . TYR B  1 361 ? -20.728 26.920  -44.479 1.00 39.80 ? 361 TYR D CE1   1 
ATOM   5722  C CE2   . TYR B  1 361 ? -21.743 24.919  -45.263 1.00 38.50 ? 361 TYR D CE2   1 
ATOM   5723  C CZ    . TYR B  1 361 ? -20.959 25.569  -44.358 1.00 38.88 ? 361 TYR D CZ    1 
ATOM   5724  O OH    . TYR B  1 361 ? -20.415 24.858  -43.315 1.00 40.55 ? 361 TYR D OH    1 
ATOM   5725  N N     . ALA B  1 362 ? -24.951 26.902  -45.507 1.00 37.63 ? 362 ALA D N     1 
ATOM   5726  C CA    . ALA B  1 362 ? -25.697 25.736  -45.038 1.00 44.24 ? 362 ALA D CA    1 
ATOM   5727  C C     . ALA B  1 362 ? -27.192 25.833  -45.321 1.00 40.44 ? 362 ALA D C     1 
ATOM   5728  O O     . ALA B  1 362 ? -27.864 24.801  -45.415 1.00 35.09 ? 362 ALA D O     1 
ATOM   5729  C CB    . ALA B  1 362 ? -25.470 25.531  -43.537 1.00 45.01 ? 362 ALA D CB    1 
ATOM   5730  N N     . ARG B  1 363 ? -27.724 27.044  -45.460 1.00 42.60 ? 363 ARG D N     1 
ATOM   5731  C CA    . ARG B  1 363 ? -29.154 27.205  -45.684 1.00 44.50 ? 363 ARG D CA    1 
ATOM   5732  C C     . ARG B  1 363 ? -29.636 26.381  -46.887 1.00 48.27 ? 363 ARG D C     1 
ATOM   5733  O O     . ARG B  1 363 ? -30.584 25.597  -46.767 1.00 51.41 ? 363 ARG D O     1 
ATOM   5734  C CB    . ARG B  1 363 ? -29.464 28.692  -45.849 1.00 44.51 ? 363 ARG D CB    1 
ATOM   5735  C CG    . ARG B  1 363 ? -30.918 29.020  -46.082 1.00 55.60 ? 363 ARG D CG    1 
ATOM   5736  C CD    . ARG B  1 363 ? -31.348 30.236  -45.256 1.00 56.54 ? 363 ARG D CD    1 
ATOM   5737  N NE    . ARG B  1 363 ? -32.057 29.876  -44.033 1.00 55.35 ? 363 ARG D NE    1 
ATOM   5738  C CZ    . ARG B  1 363 ? -33.378 29.913  -43.914 1.00 59.61 ? 363 ARG D CZ    1 
ATOM   5739  N NH1   . ARG B  1 363 ? -34.150 30.279  -44.925 1.00 60.14 ? 363 ARG D NH1   1 
ATOM   5740  N NH2   . ARG B  1 363 ? -33.940 29.571  -42.756 1.00 56.29 ? 363 ARG D NH2   1 
ATOM   5741  N N     . ASN B  1 364 ? -28.958 26.487  -48.039 1.00 44.36 ? 364 ASN D N     1 
ATOM   5742  C CA    . ASN B  1 364 ? -29.423 25.831  -49.267 1.00 46.62 ? 364 ASN D CA    1 
ATOM   5743  C C     . ASN B  1 364 ? -28.437 24.837  -49.874 1.00 47.23 ? 364 ASN D C     1 
ATOM   5744  O O     . ASN B  1 364 ? -28.663 24.369  -51.001 1.00 48.35 ? 364 ASN D O     1 
ATOM   5745  C CB    . ASN B  1 364 ? -29.766 26.873  -50.332 1.00 50.82 ? 364 ASN D CB    1 
ATOM   5746  C CG    . ASN B  1 364 ? -30.256 28.162  -49.731 1.00 52.62 ? 364 ASN D CG    1 
ATOM   5747  O OD1   . ASN B  1 364 ? -29.496 29.126  -49.603 1.00 46.72 ? 364 ASN D OD1   1 
ATOM   5748  N ND2   . ASN B  1 364 ? -31.537 28.192  -49.354 1.00 48.31 ? 364 ASN D ND2   1 
ATOM   5749  N N     . ASN B  1 365 ? -27.357 24.500  -49.178 1.00 45.90 ? 365 ASN D N     1 
ATOM   5750  C CA    . ASN B  1 365 ? -26.319 23.667  -49.749 1.00 43.05 ? 365 ASN D CA    1 
ATOM   5751  C C     . ASN B  1 365 ? -26.045 22.461  -48.876 1.00 46.60 ? 365 ASN D C     1 
ATOM   5752  O O     . ASN B  1 365 ? -26.411 22.413  -47.699 1.00 43.47 ? 365 ASN D O     1 
ATOM   5753  C CB    . ASN B  1 365 ? -25.027 24.437  -49.925 1.00 42.24 ? 365 ASN D CB    1 
ATOM   5754  C CG    . ASN B  1 365 ? -25.152 25.506  -50.953 1.00 46.50 ? 365 ASN D CG    1 
ATOM   5755  O OD1   . ASN B  1 365 ? -24.926 25.266  -52.144 1.00 52.83 ? 365 ASN D OD1   1 
ATOM   5756  N ND2   . ASN B  1 365 ? -25.524 26.705  -50.513 1.00 45.76 ? 365 ASN D ND2   1 
ATOM   5757  N N     . PHE B  1 366 ? -25.371 21.492  -49.485 1.00 46.47 ? 366 PHE D N     1 
ATOM   5758  C CA    . PHE B  1 366 ? -24.941 20.280  -48.813 1.00 44.38 ? 366 PHE D CA    1 
ATOM   5759  C C     . PHE B  1 366 ? -23.561 19.916  -49.337 1.00 44.35 ? 366 PHE D C     1 
ATOM   5760  O O     . PHE B  1 366 ? -23.312 19.977  -50.547 1.00 41.40 ? 366 PHE D O     1 
ATOM   5761  C CB    . PHE B  1 366 ? -25.908 19.106  -49.057 1.00 45.16 ? 366 PHE D CB    1 
ATOM   5762  C CG    . PHE B  1 366 ? -27.358 19.412  -48.757 1.00 46.42 ? 366 PHE D CG    1 
ATOM   5763  C CD1   . PHE B  1 366 ? -28.145 20.129  -49.652 1.00 48.44 ? 366 PHE D CD1   1 
ATOM   5764  C CD2   . PHE B  1 366 ? -27.944 18.944  -47.588 1.00 48.70 ? 366 PHE D CD2   1 
ATOM   5765  C CE1   . PHE B  1 366 ? -29.483 20.394  -49.368 1.00 48.04 ? 366 PHE D CE1   1 
ATOM   5766  C CE2   . PHE B  1 366 ? -29.274 19.205  -47.298 1.00 39.21 ? 366 PHE D CE2   1 
ATOM   5767  C CZ    . PHE B  1 366 ? -30.042 19.931  -48.186 1.00 46.62 ? 366 PHE D CZ    1 
ATOM   5768  N N     . PHE B  1 367 ? -22.661 19.550  -48.434 1.00 44.84 ? 367 PHE D N     1 
ATOM   5769  C CA    . PHE B  1 367 ? -21.380 19.003  -48.831 1.00 42.00 ? 367 PHE D CA    1 
ATOM   5770  C C     . PHE B  1 367 ? -21.191 17.622  -48.234 1.00 41.28 ? 367 PHE D C     1 
ATOM   5771  O O     . PHE B  1 367 ? -21.791 17.270  -47.215 1.00 39.68 ? 367 PHE D O     1 
ATOM   5772  C CB    . PHE B  1 367 ? -20.190 19.939  -48.475 1.00 40.93 ? 367 PHE D CB    1 
ATOM   5773  C CG    . PHE B  1 367 ? -19.987 20.212  -46.997 1.00 39.39 ? 367 PHE D CG    1 
ATOM   5774  C CD1   . PHE B  1 367 ? -19.473 19.245  -46.146 1.00 39.49 ? 367 PHE D CD1   1 
ATOM   5775  C CD2   . PHE B  1 367 ? -20.234 21.480  -46.481 1.00 42.00 ? 367 PHE D CD2   1 
ATOM   5776  C CE1   . PHE B  1 367 ? -19.266 19.523  -44.794 1.00 39.93 ? 367 PHE D CE1   1 
ATOM   5777  C CE2   . PHE B  1 367 ? -20.027 21.764  -45.138 1.00 36.12 ? 367 PHE D CE2   1 
ATOM   5778  C CZ    . PHE B  1 367 ? -19.546 20.783  -44.294 1.00 37.80 ? 367 PHE D CZ    1 
ATOM   5779  N N     . SER B  1 368 ? -20.360 16.839  -48.905 1.00 40.94 ? 368 SER D N     1 
ATOM   5780  C CA    . SER B  1 368 ? -20.076 15.486  -48.476 1.00 39.49 ? 368 SER D CA    1 
ATOM   5781  C C     . SER B  1 368 ? -18.711 15.082  -49.016 1.00 42.09 ? 368 SER D C     1 
ATOM   5782  O O     . SER B  1 368 ? -18.243 15.601  -50.037 1.00 37.17 ? 368 SER D O     1 
ATOM   5783  C CB    . SER B  1 368 ? -21.157 14.518  -48.944 1.00 33.85 ? 368 SER D CB    1 
ATOM   5784  O OG    . SER B  1 368 ? -20.866 13.220  -48.459 1.00 41.82 ? 368 SER D OG    1 
ATOM   5785  N N     . SER B  1 369 ? -18.080 14.147  -48.323 1.00 37.86 ? 369 SER D N     1 
ATOM   5786  C CA    . SER B  1 369 ? -16.683 13.849  -48.568 1.00 34.93 ? 369 SER D CA    1 
ATOM   5787  C C     . SER B  1 369 ? -16.517 12.367  -48.860 1.00 37.07 ? 369 SER D C     1 
ATOM   5788  O O     . SER B  1 369 ? -17.120 11.517  -48.199 1.00 36.53 ? 369 SER D O     1 
ATOM   5789  C CB    . SER B  1 369 ? -15.818 14.270  -47.372 1.00 40.81 ? 369 SER D CB    1 
ATOM   5790  O OG    . SER B  1 369 ? -16.030 13.461  -46.222 1.00 38.35 ? 369 SER D OG    1 
ATOM   5791  N N     . ILE B  1 370 ? -15.713 12.076  -49.874 1.00 38.20 ? 370 ILE D N     1 
ATOM   5792  C CA    . ILE B  1 370 ? -15.345 10.717  -50.247 1.00 42.39 ? 370 ILE D CA    1 
ATOM   5793  C C     . ILE B  1 370 ? -13.883 10.531  -49.894 1.00 41.30 ? 370 ILE D C     1 
ATOM   5794  O O     . ILE B  1 370 ? -13.069 11.440  -50.088 1.00 42.37 ? 370 ILE D O     1 
ATOM   5795  C CB    . ILE B  1 370 ? -15.546 10.425  -51.753 1.00 41.40 ? 370 ILE D CB    1 
ATOM   5796  C CG1   . ILE B  1 370 ? -16.830 11.029  -52.304 1.00 36.94 ? 370 ILE D CG1   1 
ATOM   5797  C CG2   . ILE B  1 370 ? -15.537 8.935   -52.029 1.00 40.87 ? 370 ILE D CG2   1 
ATOM   5798  C CD1   . ILE B  1 370 ? -16.819 11.044  -53.833 1.00 40.55 ? 370 ILE D CD1   1 
ATOM   5799  N N     . LEU B  1 371 ? -13.548 9.354   -49.389 1.00 43.53 ? 371 LEU D N     1 
ATOM   5800  C CA    . LEU B  1 371 ? -12.170 8.904   -49.309 1.00 47.26 ? 371 LEU D CA    1 
ATOM   5801  C C     . LEU B  1 371 ? -12.120 7.491   -49.892 1.00 50.03 ? 371 LEU D C     1 
ATOM   5802  O O     . LEU B  1 371 ? -13.154 6.918   -50.262 1.00 57.68 ? 371 LEU D O     1 
ATOM   5803  C CB    . LEU B  1 371 ? -11.671 8.985   -47.865 1.00 46.83 ? 371 LEU D CB    1 
ATOM   5804  C CG    . LEU B  1 371 ? -12.016 10.358  -47.277 1.00 43.19 ? 371 LEU D CG    1 
ATOM   5805  C CD1   . LEU B  1 371 ? -13.060 10.271  -46.171 1.00 40.19 ? 371 LEU D CD1   1 
ATOM   5806  C CD2   . LEU B  1 371 ? -10.787 11.020  -46.778 1.00 45.69 ? 371 LEU D CD2   1 
ATOM   5807  N N     . ASN B  1 372 ? -10.923 6.924   -49.989 1.00 48.33 ? 372 ASN D N     1 
ATOM   5808  C CA    . ASN B  1 372 ? -10.683 5.677   -50.718 1.00 58.48 ? 372 ASN D CA    1 
ATOM   5809  C C     . ASN B  1 372 ? -11.005 5.798   -52.220 1.00 55.90 ? 372 ASN D C     1 
ATOM   5810  O O     . ASN B  1 372 ? -11.101 4.772   -52.914 1.00 60.61 ? 372 ASN D O     1 
ATOM   5811  C CB    . ASN B  1 372 ? -11.450 4.481   -50.091 1.00 59.68 ? 372 ASN D CB    1 
ATOM   5812  C CG    . ASN B  1 372 ? -10.548 3.224   -49.813 1.00 64.37 ? 372 ASN D CG    1 
ATOM   5813  O OD1   . ASN B  1 372 ? -9.359  3.181   -50.156 1.00 57.81 ? 372 ASN D OD1   1 
ATOM   5814  N ND2   . ASN B  1 372 ? -11.146 2.199   -49.192 1.00 57.66 ? 372 ASN D ND2   1 
ATOM   5815  N N     . VAL B  1 373 ? -11.174 7.020   -52.751 1.00 48.21 ? 373 VAL D N     1 
ATOM   5816  C CA    . VAL B  1 373 ? -11.176 7.189   -54.203 1.00 45.64 ? 373 VAL D CA    1 
ATOM   5817  C C     . VAL B  1 373 ? -9.827  6.748   -54.729 1.00 43.36 ? 373 VAL D C     1 
ATOM   5818  O O     . VAL B  1 373 ? -8.784  7.106   -54.166 1.00 41.38 ? 373 VAL D O     1 
ATOM   5819  C CB    . VAL B  1 373 ? -11.462 8.643   -54.611 1.00 43.13 ? 373 VAL D CB    1 
ATOM   5820  C CG1   . VAL B  1 373 ? -10.843 8.938   -55.960 1.00 43.64 ? 373 VAL D CG1   1 
ATOM   5821  C CG2   . VAL B  1 373 ? -12.941 8.901   -54.683 1.00 41.12 ? 373 VAL D CG2   1 
ATOM   5822  N N     . VAL B  1 374 ? -9.845  5.944   -55.788 1.00 46.63 ? 374 VAL D N     1 
ATOM   5823  C CA    . VAL B  1 374 ? -8.624  5.456   -56.416 1.00 42.09 ? 374 VAL D CA    1 
ATOM   5824  C C     . VAL B  1 374 ? -7.734  6.663   -56.689 1.00 43.87 ? 374 VAL D C     1 
ATOM   5825  O O     . VAL B  1 374 ? -8.090  7.516   -57.514 1.00 52.96 ? 374 VAL D O     1 
ATOM   5826  C CB    . VAL B  1 374 ? -8.947  4.652   -57.684 1.00 46.31 ? 374 VAL D CB    1 
ATOM   5827  C CG1   . VAL B  1 374 ? -7.693  4.443   -58.540 1.00 43.75 ? 374 VAL D CG1   1 
ATOM   5828  C CG2   . VAL B  1 374 ? -9.583  3.321   -57.307 1.00 42.64 ? 374 VAL D CG2   1 
ATOM   5829  N N     . PRO B  1 375 ? -6.610  6.807   -55.983 1.00 45.18 ? 375 PRO D N     1 
ATOM   5830  C CA    . PRO B  1 375 ? -5.795  8.020   -56.117 1.00 35.83 ? 375 PRO D CA    1 
ATOM   5831  C C     . PRO B  1 375 ? -5.190  8.149   -57.505 1.00 44.50 ? 375 PRO D C     1 
ATOM   5832  O O     . PRO B  1 375 ? -5.017  7.173   -58.240 1.00 47.69 ? 375 PRO D O     1 
ATOM   5833  C CB    . PRO B  1 375 ? -4.697  7.830   -55.058 1.00 43.48 ? 375 PRO D CB    1 
ATOM   5834  C CG    . PRO B  1 375 ? -5.212  6.775   -54.135 1.00 40.97 ? 375 PRO D CG    1 
ATOM   5835  C CD    . PRO B  1 375 ? -6.063  5.882   -54.972 1.00 44.68 ? 375 PRO D CD    1 
ATOM   5836  N N     . ALA B  1 376 ? -4.841  9.378   -57.855 1.00 42.82 ? 376 ALA D N     1 
ATOM   5837  C CA    . ALA B  1 376 ? -4.180  9.620   -59.127 1.00 36.65 ? 376 ALA D CA    1 
ATOM   5838  C C     . ALA B  1 376 ? -3.659  11.048  -59.120 1.00 37.35 ? 376 ALA D C     1 
ATOM   5839  O O     . ALA B  1 376 ? -3.882  11.806  -58.172 1.00 36.79 ? 376 ALA D O     1 
ATOM   5840  C CB    . ALA B  1 376 ? -5.120  9.386   -60.304 1.00 35.04 ? 376 ALA D CB    1 
ATOM   5841  N N     . GLY B  1 377 ? -2.939  11.391  -60.185 1.00 35.89 ? 377 GLY D N     1 
ATOM   5842  C CA    . GLY B  1 377 ? -2.542  12.769  -60.390 1.00 35.55 ? 377 GLY D CA    1 
ATOM   5843  C C     . GLY B  1 377 ? -3.742  13.693  -60.335 1.00 40.95 ? 377 GLY D C     1 
ATOM   5844  O O     . GLY B  1 377 ? -4.887  13.276  -60.552 1.00 41.71 ? 377 GLY D O     1 
ATOM   5845  N N     . LEU B  1 378 ? -3.485  14.958  -60.000 1.00 38.05 ? 378 LEU D N     1 
ATOM   5846  C CA    . LEU B  1 378 ? -4.571  15.931  -59.977 1.00 38.23 ? 378 LEU D CA    1 
ATOM   5847  C C     . LEU B  1 378 ? -5.231  16.050  -61.351 1.00 40.95 ? 378 LEU D C     1 
ATOM   5848  O O     . LEU B  1 378 ? -6.464  16.065  -61.461 1.00 38.91 ? 378 LEU D O     1 
ATOM   5849  C CB    . LEU B  1 378 ? -4.039  17.278  -59.480 1.00 37.56 ? 378 LEU D CB    1 
ATOM   5850  C CG    . LEU B  1 378 ? -5.132  18.312  -59.234 1.00 37.15 ? 378 LEU D CG    1 
ATOM   5851  C CD1   . LEU B  1 378 ? -5.468  18.352  -57.783 1.00 41.34 ? 378 LEU D CD1   1 
ATOM   5852  C CD2   . LEU B  1 378 ? -4.650  19.669  -59.689 1.00 37.28 ? 378 LEU D CD2   1 
ATOM   5853  N N     . ALA B  1 379 ? -4.418  16.104  -62.409 1.00 44.69 ? 379 ALA D N     1 
ATOM   5854  C CA    . ALA B  1 379 ? -4.906  16.029  -63.784 1.00 37.99 ? 379 ALA D CA    1 
ATOM   5855  C C     . ALA B  1 379 ? -5.821  14.827  -64.001 1.00 41.69 ? 379 ALA D C     1 
ATOM   5856  O O     . ALA B  1 379 ? -6.963  14.959  -64.459 1.00 47.36 ? 379 ALA D O     1 
ATOM   5857  C CB    . ALA B  1 379 ? -3.714  15.948  -64.735 1.00 42.91 ? 379 ALA D CB    1 
ATOM   5858  N N     . ASP B  1 380 ? -5.314  13.631  -63.713 1.00 40.46 ? 380 ASP D N     1 
ATOM   5859  C CA    . ASP B  1 380 ? -6.140  12.446  -63.878 1.00 42.27 ? 380 ASP D CA    1 
ATOM   5860  C C     . ASP B  1 380 ? -7.359  12.512  -62.976 1.00 39.93 ? 380 ASP D C     1 
ATOM   5861  O O     . ASP B  1 380 ? -8.403  11.947  -63.307 1.00 44.24 ? 380 ASP D O     1 
ATOM   5862  C CB    . ASP B  1 380 ? -5.321  11.175  -63.608 1.00 45.53 ? 380 ASP D CB    1 
ATOM   5863  C CG    . ASP B  1 380 ? -4.042  11.095  -64.469 1.00 52.23 ? 380 ASP D CG    1 
ATOM   5864  O OD1   . ASP B  1 380 ? -3.116  11.913  -64.248 1.00 48.05 ? 380 ASP D OD1   1 
ATOM   5865  O OD2   . ASP B  1 380 ? -3.958  10.212  -65.359 1.00 52.18 ? 380 ASP D OD2   1 
ATOM   5866  N N     . LEU B  1 381 ? -7.262  13.208  -61.843 1.00 40.64 ? 381 LEU D N     1 
ATOM   5867  C CA    . LEU B  1 381 ? -8.442  13.357  -60.992 1.00 38.80 ? 381 LEU D CA    1 
ATOM   5868  C C     . LEU B  1 381 ? -9.452  14.300  -61.627 1.00 37.85 ? 381 LEU D C     1 
ATOM   5869  O O     . LEU B  1 381 ? -10.633 13.963  -61.756 1.00 39.39 ? 381 LEU D O     1 
ATOM   5870  C CB    . LEU B  1 381 ? -8.047  13.851  -59.604 1.00 32.27 ? 381 LEU D CB    1 
ATOM   5871  C CG    . LEU B  1 381 ? -7.706  12.704  -58.669 1.00 30.49 ? 381 LEU D CG    1 
ATOM   5872  C CD1   . LEU B  1 381 ? -7.238  13.220  -57.326 1.00 33.48 ? 381 LEU D CD1   1 
ATOM   5873  C CD2   . LEU B  1 381 ? -8.897  11.777  -58.523 1.00 28.28 ? 381 LEU D CD2   1 
ATOM   5874  N N     . LEU B  1 382 ? -8.997  15.478  -62.064 1.00 40.69 ? 382 LEU D N     1 
ATOM   5875  C CA    . LEU B  1 382 ? -9.926  16.445  -62.637 1.00 41.10 ? 382 LEU D CA    1 
ATOM   5876  C C     . LEU B  1 382 ? -10.663 15.863  -63.835 1.00 38.94 ? 382 LEU D C     1 
ATOM   5877  O O     . LEU B  1 382 ? -11.860 16.118  -64.002 1.00 41.01 ? 382 LEU D O     1 
ATOM   5878  C CB    . LEU B  1 382 ? -9.194  17.735  -63.008 1.00 35.39 ? 382 LEU D CB    1 
ATOM   5879  C CG    . LEU B  1 382 ? -8.646  18.489  -61.778 1.00 38.16 ? 382 LEU D CG    1 
ATOM   5880  C CD1   . LEU B  1 382 ? -8.152  19.900  -62.101 1.00 36.23 ? 382 LEU D CD1   1 
ATOM   5881  C CD2   . LEU B  1 382 ? -9.662  18.539  -60.638 1.00 34.94 ? 382 LEU D CD2   1 
ATOM   5882  N N     . ARG B  1 383 ? -9.994  15.025  -64.638 1.00 37.31 ? 383 ARG D N     1 
ATOM   5883  C CA    . ARG B  1 383 ? -10.639 14.504  -65.845 1.00 39.15 ? 383 ARG D CA    1 
ATOM   5884  C C     . ARG B  1 383 ? -11.818 13.594  -65.503 1.00 38.63 ? 383 ARG D C     1 
ATOM   5885  O O     . ARG B  1 383 ? -12.890 13.711  -66.103 1.00 39.46 ? 383 ARG D O     1 
ATOM   5886  C CB    . ARG B  1 383 ? -9.623  13.784  -66.747 1.00 41.14 ? 383 ARG D CB    1 
ATOM   5887  C CG    . ARG B  1 383 ? -9.117  12.434  -66.241 1.00 46.78 ? 383 ARG D CG    1 
ATOM   5888  C CD    . ARG B  1 383 ? -8.501  11.569  -67.346 1.00 51.05 ? 383 ARG D CD    1 
ATOM   5889  N NE    . ARG B  1 383 ? -7.766  10.439  -66.788 1.00 49.73 ? 383 ARG D NE    1 
ATOM   5890  C CZ    . ARG B  1 383 ? -6.444  10.315  -66.824 1.00 50.52 ? 383 ARG D CZ    1 
ATOM   5891  N NH1   . ARG B  1 383 ? -5.680  11.236  -67.380 1.00 49.33 ? 383 ARG D NH1   1 
ATOM   5892  N NH2   . ARG B  1 383 ? -5.870  9.240   -66.283 1.00 56.46 ? 383 ARG D NH2   1 
ATOM   5893  N N     . SER B  1 384 ? -11.652 12.693  -64.532 1.00 37.21 ? 384 SER D N     1 
ATOM   5894  C CA    . SER B  1 384 ? -12.763 11.819  -64.173 1.00 36.95 ? 384 SER D CA    1 
ATOM   5895  C C     . SER B  1 384 ? -13.915 12.621  -63.604 1.00 38.77 ? 384 SER D C     1 
ATOM   5896  O O     . SER B  1 384 ? -15.087 12.329  -63.886 1.00 37.16 ? 384 SER D O     1 
ATOM   5897  C CB    . SER B  1 384 ? -12.320 10.760  -63.169 1.00 43.20 ? 384 SER D CB    1 
ATOM   5898  O OG    . SER B  1 384 ? -11.984 9.550   -63.831 1.00 49.74 ? 384 SER D OG    1 
ATOM   5899  N N     . LEU B  1 385 ? -13.604 13.639  -62.803 1.00 39.10 ? 385 LEU D N     1 
ATOM   5900  C CA    . LEU B  1 385 ? -14.672 14.505  -62.331 1.00 39.60 ? 385 LEU D CA    1 
ATOM   5901  C C     . LEU B  1 385 ? -15.373 15.142  -63.501 1.00 35.52 ? 385 LEU D C     1 
ATOM   5902  O O     . LEU B  1 385 ? -16.607 15.194  -63.534 1.00 37.93 ? 385 LEU D O     1 
ATOM   5903  C CB    . LEU B  1 385 ? -14.151 15.569  -61.369 1.00 36.13 ? 385 LEU D CB    1 
ATOM   5904  C CG    . LEU B  1 385 ? -14.018 14.964  -59.971 1.00 40.28 ? 385 LEU D CG    1 
ATOM   5905  C CD1   . LEU B  1 385 ? -12.572 14.688  -59.636 1.00 40.15 ? 385 LEU D CD1   1 
ATOM   5906  C CD2   . LEU B  1 385 ? -14.640 15.846  -58.930 1.00 37.31 ? 385 LEU D CD2   1 
ATOM   5907  N N     . GLU B  1 386 ? -14.605 15.590  -64.491 1.00 34.53 ? 386 GLU D N     1 
ATOM   5908  C CA    . GLU B  1 386 ? -15.212 16.064  -65.728 1.00 33.38 ? 386 GLU D CA    1 
ATOM   5909  C C     . GLU B  1 386 ? -15.933 14.930  -66.448 1.00 38.93 ? 386 GLU D C     1 
ATOM   5910  O O     . GLU B  1 386 ? -17.112 15.061  -66.803 1.00 40.76 ? 386 GLU D O     1 
ATOM   5911  C CB    . GLU B  1 386 ? -14.157 16.702  -66.620 1.00 29.47 ? 386 GLU D CB    1 
ATOM   5912  C CG    . GLU B  1 386 ? -13.995 18.166  -66.328 1.00 30.54 ? 386 GLU D CG    1 
ATOM   5913  C CD    . GLU B  1 386 ? -13.013 18.853  -67.231 1.00 32.22 ? 386 GLU D CD    1 
ATOM   5914  O OE1   . GLU B  1 386 ? -13.298 18.998  -68.442 1.00 43.78 ? 386 GLU D OE1   1 
ATOM   5915  O OE2   . GLU B  1 386 ? -11.951 19.258  -66.723 1.00 30.77 ? 386 GLU D OE2   1 
ATOM   5916  N N     . ARG B  1 387 ? -15.253 13.792  -66.640 1.00 39.43 ? 387 ARG D N     1 
ATOM   5917  C CA    . ARG B  1 387 ? -15.889 12.648  -67.295 1.00 37.18 ? 387 ARG D CA    1 
ATOM   5918  C C     . ARG B  1 387 ? -17.183 12.260  -66.603 1.00 40.48 ? 387 ARG D C     1 
ATOM   5919  O O     . ARG B  1 387 ? -18.111 11.788  -67.265 1.00 42.44 ? 387 ARG D O     1 
ATOM   5920  C CB    . ARG B  1 387 ? -14.934 11.454  -67.332 1.00 41.11 ? 387 ARG D CB    1 
ATOM   5921  C CG    . ARG B  1 387 ? -15.470 10.235  -68.058 1.00 43.26 ? 387 ARG D CG    1 
ATOM   5922  C CD    . ARG B  1 387 ? -14.496 9.063   -67.944 1.00 40.48 ? 387 ARG D CD    1 
ATOM   5923  N NE    . ARG B  1 387 ? -13.133 9.533   -67.734 1.00 41.33 ? 387 ARG D NE    1 
ATOM   5924  C CZ    . ARG B  1 387 ? -12.352 9.148   -66.732 1.00 48.24 ? 387 ARG D CZ    1 
ATOM   5925  N NH1   . ARG B  1 387 ? -12.756 8.249   -65.843 1.00 43.23 ? 387 ARG D NH1   1 
ATOM   5926  N NH2   . ARG B  1 387 ? -11.135 9.679   -66.617 1.00 43.54 ? 387 ARG D NH2   1 
ATOM   5927  N N     . ALA B  1 388 ? -17.280 12.486  -65.281 1.00 41.19 ? 388 ALA D N     1 
ATOM   5928  C CA    . ALA B  1 388 ? -18.518 12.229  -64.541 1.00 40.41 ? 388 ALA D CA    1 
ATOM   5929  C C     . ALA B  1 388 ? -19.527 13.367  -64.622 1.00 34.25 ? 388 ALA D C     1 
ATOM   5930  O O     . ALA B  1 388 ? -20.704 13.151  -64.315 1.00 34.38 ? 388 ALA D O     1 
ATOM   5931  C CB    . ALA B  1 388 ? -18.220 11.962  -63.067 1.00 39.12 ? 388 ALA D CB    1 
ATOM   5932  N N     . GLY B  1 389 ? -19.097 14.569  -64.988 1.00 31.43 ? 389 GLY D N     1 
ATOM   5933  C CA    . GLY B  1 389 ? -19.997 15.702  -65.042 1.00 32.87 ? 389 GLY D CA    1 
ATOM   5934  C C     . GLY B  1 389 ? -20.200 16.425  -63.731 1.00 35.50 ? 389 GLY D C     1 
ATOM   5935  O O     . GLY B  1 389 ? -21.160 17.198  -63.608 1.00 25.99 ? 389 GLY D O     1 
ATOM   5936  N N     . VAL B  1 390 ? -19.316 16.220  -62.752 1.00 36.58 ? 390 VAL D N     1 
ATOM   5937  C CA    . VAL B  1 390 ? -19.541 16.730  -61.405 1.00 36.36 ? 390 VAL D CA    1 
ATOM   5938  C C     . VAL B  1 390 ? -18.342 17.499  -60.857 1.00 32.77 ? 390 VAL D C     1 
ATOM   5939  O O     . VAL B  1 390 ? -18.189 17.626  -59.645 1.00 36.72 ? 390 VAL D O     1 
ATOM   5940  C CB    . VAL B  1 390 ? -19.914 15.579  -60.452 1.00 40.38 ? 390 VAL D CB    1 
ATOM   5941  C CG1   . VAL B  1 390 ? -21.052 14.727  -61.040 1.00 33.35 ? 390 VAL D CG1   1 
ATOM   5942  C CG2   . VAL B  1 390 ? -18.686 14.723  -60.168 1.00 40.57 ? 390 VAL D CG2   1 
ATOM   5943  N N     . ARG B  1 391 ? -17.491 18.045  -61.713 1.00 35.14 ? 391 ARG D N     1 
ATOM   5944  C CA    . ARG B  1 391 ? -16.454 18.918  -61.180 1.00 35.15 ? 391 ARG D CA    1 
ATOM   5945  C C     . ARG B  1 391 ? -17.099 20.180  -60.602 1.00 38.48 ? 391 ARG D C     1 
ATOM   5946  O O     . ARG B  1 391 ? -18.157 20.623  -61.065 1.00 41.36 ? 391 ARG D O     1 
ATOM   5947  C CB    . ARG B  1 391 ? -15.451 19.278  -62.274 1.00 31.89 ? 391 ARG D CB    1 
ATOM   5948  C CG    . ARG B  1 391 ? -14.221 20.000  -61.764 1.00 31.64 ? 391 ARG D CG    1 
ATOM   5949  C CD    . ARG B  1 391 ? -13.194 20.264  -62.851 1.00 29.89 ? 391 ARG D CD    1 
ATOM   5950  N NE    . ARG B  1 391 ? -12.516 21.533  -62.630 1.00 32.93 ? 391 ARG D NE    1 
ATOM   5951  C CZ    . ARG B  1 391 ? -11.315 21.830  -63.100 1.00 37.84 ? 391 ARG D CZ    1 
ATOM   5952  N NH1   . ARG B  1 391 ? -10.619 20.958  -63.806 1.00 36.98 ? 391 ARG D NH1   1 
ATOM   5953  N NH2   . ARG B  1 391 ? -10.811 23.043  -62.878 1.00 41.25 ? 391 ARG D NH2   1 
ATOM   5954  N N     . TYR B  1 392 ? -16.482 20.750  -59.559 1.00 35.06 ? 392 TYR D N     1 
ATOM   5955  C CA    . TYR B  1 392 ? -17.035 21.984  -59.012 1.00 34.88 ? 392 TYR D CA    1 
ATOM   5956  C C     . TYR B  1 392 ? -17.116 23.034  -60.101 1.00 35.18 ? 392 TYR D C     1 
ATOM   5957  O O     . TYR B  1 392 ? -16.194 23.193  -60.907 1.00 32.19 ? 392 TYR D O     1 
ATOM   5958  C CB    . TYR B  1 392 ? -16.219 22.547  -57.851 1.00 34.29 ? 392 TYR D CB    1 
ATOM   5959  C CG    . TYR B  1 392 ? -16.916 23.745  -57.180 1.00 32.96 ? 392 TYR D CG    1 
ATOM   5960  C CD1   . TYR B  1 392 ? -18.063 23.561  -56.399 1.00 37.25 ? 392 TYR D CD1   1 
ATOM   5961  C CD2   . TYR B  1 392 ? -16.444 25.042  -57.335 1.00 25.78 ? 392 TYR D CD2   1 
ATOM   5962  C CE1   . TYR B  1 392 ? -18.708 24.627  -55.782 1.00 32.75 ? 392 TYR D CE1   1 
ATOM   5963  C CE2   . TYR B  1 392 ? -17.088 26.119  -56.722 1.00 29.49 ? 392 TYR D CE2   1 
ATOM   5964  C CZ    . TYR B  1 392 ? -18.216 25.900  -55.949 1.00 32.26 ? 392 TYR D CZ    1 
ATOM   5965  O OH    . TYR B  1 392 ? -18.865 26.954  -55.346 1.00 33.87 ? 392 TYR D OH    1 
ATOM   5966  N N     . ASP B  1 393 ? -18.236 23.755  -60.103 1.00 39.91 ? 393 ASP D N     1 
ATOM   5967  C CA    . ASP B  1 393 ? -18.602 24.671  -61.181 1.00 39.21 ? 393 ASP D CA    1 
ATOM   5968  C C     . ASP B  1 393 ? -19.189 25.922  -60.539 1.00 38.27 ? 393 ASP D C     1 
ATOM   5969  O O     . ASP B  1 393 ? -20.349 25.901  -60.125 1.00 41.61 ? 393 ASP D O     1 
ATOM   5970  C CB    . ASP B  1 393 ? -19.596 23.990  -62.108 1.00 36.59 ? 393 ASP D CB    1 
ATOM   5971  C CG    . ASP B  1 393 ? -20.332 24.963  -63.003 1.00 48.14 ? 393 ASP D CG    1 
ATOM   5972  O OD1   . ASP B  1 393 ? -19.873 26.113  -63.182 1.00 45.68 ? 393 ASP D OD1   1 
ATOM   5973  O OD2   . ASP B  1 393 ? -21.379 24.552  -63.549 1.00 53.36 ? 393 ASP D OD2   1 
ATOM   5974  N N     . LYS B  1 394 ? -18.401 27.009  -60.493 1.00 37.48 ? 394 LYS D N     1 
ATOM   5975  C CA    . LYS B  1 394 ? -18.785 28.187  -59.711 1.00 41.71 ? 394 LYS D CA    1 
ATOM   5976  C C     . LYS B  1 394 ? -20.183 28.687  -60.048 1.00 50.56 ? 394 LYS D C     1 
ATOM   5977  O O     . LYS B  1 394 ? -20.869 29.242  -59.178 1.00 52.69 ? 394 LYS D O     1 
ATOM   5978  C CB    . LYS B  1 394 ? -17.795 29.341  -59.916 1.00 45.99 ? 394 LYS D CB    1 
ATOM   5979  C CG    . LYS B  1 394 ? -17.739 30.352  -58.717 1.00 55.44 ? 394 LYS D CG    1 
ATOM   5980  C CD    . LYS B  1 394 ? -18.511 31.693  -58.934 1.00 56.24 ? 394 LYS D CD    1 
ATOM   5981  C CE    . LYS B  1 394 ? -18.900 32.374  -57.592 1.00 55.88 ? 394 LYS D CE    1 
ATOM   5982  N NZ    . LYS B  1 394 ? -19.459 33.764  -57.713 1.00 47.14 ? 394 LYS D NZ    1 
ATOM   5983  N N     . ASP B  1 395 ? -20.616 28.509  -61.297 1.00 50.54 ? 395 ASP D N     1 
ATOM   5984  C CA    . ASP B  1 395 ? -21.917 29.015  -61.727 1.00 48.83 ? 395 ASP D CA    1 
ATOM   5985  C C     . ASP B  1 395 ? -23.042 28.369  -60.935 1.00 47.93 ? 395 ASP D C     1 
ATOM   5986  O O     . ASP B  1 395 ? -23.856 29.058  -60.308 1.00 57.92 ? 395 ASP D O     1 
ATOM   5987  C CB    . ASP B  1 395 ? -22.103 28.767  -63.225 1.00 54.08 ? 395 ASP D CB    1 
ATOM   5988  C CG    . ASP B  1 395 ? -21.372 29.789  -64.090 1.00 57.08 ? 395 ASP D CG    1 
ATOM   5989  O OD1   . ASP B  1 395 ? -20.919 30.820  -63.531 1.00 55.35 ? 395 ASP D OD1   1 
ATOM   5990  O OD2   . ASP B  1 395 ? -21.258 29.554  -65.325 1.00 57.65 ? 395 ASP D OD2   1 
ATOM   5991  N N     . SER B  1 396 ? -23.105 27.038  -60.954 1.00 45.56 ? 396 SER D N     1 
ATOM   5992  C CA    . SER B  1 396 ? -24.149 26.331  -60.228 1.00 42.19 ? 396 SER D CA    1 
ATOM   5993  C C     . SER B  1 396 ? -23.875 26.243  -58.735 1.00 42.15 ? 396 SER D C     1 
ATOM   5994  O O     . SER B  1 396 ? -24.821 26.125  -57.953 1.00 45.55 ? 396 SER D O     1 
ATOM   5995  C CB    . SER B  1 396 ? -24.307 24.920  -60.778 1.00 46.04 ? 396 SER D CB    1 
ATOM   5996  O OG    . SER B  1 396 ? -23.110 24.185  -60.579 1.00 45.22 ? 396 SER D OG    1 
ATOM   5997  N N     . GLY B  1 397 ? -22.614 26.304  -58.322 1.00 44.62 ? 397 GLY D N     1 
ATOM   5998  C CA    . GLY B  1 397 ? -22.278 25.991  -56.952 1.00 42.32 ? 397 GLY D CA    1 
ATOM   5999  C C     . GLY B  1 397 ? -22.309 24.513  -56.684 1.00 43.58 ? 397 GLY D C     1 
ATOM   6000  O O     . GLY B  1 397 ? -22.360 24.097  -55.519 1.00 39.88 ? 397 GLY D O     1 
ATOM   6001  N N     . GLU B  1 398 ? -22.288 23.706  -57.743 1.00 39.77 ? 398 GLU D N     1 
ATOM   6002  C CA    . GLU B  1 398 ? -22.421 22.262  -57.663 1.00 42.02 ? 398 GLU D CA    1 
ATOM   6003  C C     . GLU B  1 398 ? -21.110 21.589  -58.039 1.00 41.80 ? 398 GLU D C     1 
ATOM   6004  O O     . GLU B  1 398 ? -20.331 22.107  -58.852 1.00 43.25 ? 398 GLU D O     1 
ATOM   6005  C CB    . GLU B  1 398 ? -23.514 21.752  -58.605 1.00 45.14 ? 398 GLU D CB    1 
ATOM   6006  C CG    . GLU B  1 398 ? -24.885 22.252  -58.294 1.00 45.48 ? 398 GLU D CG    1 
ATOM   6007  C CD    . GLU B  1 398 ? -25.704 21.209  -57.599 1.00 48.11 ? 398 GLU D CD    1 
ATOM   6008  O OE1   . GLU B  1 398 ? -25.262 20.036  -57.607 1.00 51.19 ? 398 GLU D OE1   1 
ATOM   6009  O OE2   . GLU B  1 398 ? -26.777 21.556  -57.049 1.00 45.65 ? 398 GLU D OE2   1 
ATOM   6010  N N     . GLY B  1 399 ? -20.899 20.414  -57.475 1.00 36.22 ? 399 GLY D N     1 
ATOM   6011  C CA    . GLY B  1 399 ? -19.795 19.597  -57.867 1.00 36.82 ? 399 GLY D CA    1 
ATOM   6012  C C     . GLY B  1 399 ? -18.782 19.442  -56.762 1.00 37.60 ? 399 GLY D C     1 
ATOM   6013  O O     . GLY B  1 399 ? -19.055 19.666  -55.584 1.00 40.90 ? 399 GLY D O     1 
ATOM   6014  N N     . ALA B  1 400 ? -17.574 19.059  -57.170 1.00 36.81 ? 400 ALA D N     1 
ATOM   6015  C CA    . ALA B  1 400 ? -16.610 18.477  -56.261 1.00 36.40 ? 400 ALA D CA    1 
ATOM   6016  C C     . ALA B  1 400 ? -15.231 19.077  -56.470 1.00 33.49 ? 400 ALA D C     1 
ATOM   6017  O O     . ALA B  1 400 ? -14.883 19.534  -57.557 1.00 31.06 ? 400 ALA D O     1 
ATOM   6018  C CB    . ALA B  1 400 ? -16.552 16.956  -56.406 1.00 31.29 ? 400 ALA D CB    1 
ATOM   6019  N N     . VAL B  1 401 ? -14.469 19.112  -55.380 1.00 38.10 ? 401 VAL D N     1 
ATOM   6020  C CA    . VAL B  1 401 ? -13.115 19.637  -55.376 1.00 37.61 ? 401 VAL D CA    1 
ATOM   6021  C C     . VAL B  1 401 ? -12.221 18.626  -54.683 1.00 36.06 ? 401 VAL D C     1 
ATOM   6022  O O     . VAL B  1 401 ? -12.678 17.751  -53.942 1.00 30.80 ? 401 VAL D O     1 
ATOM   6023  C CB    . VAL B  1 401 ? -13.003 21.003  -54.673 1.00 35.13 ? 401 VAL D CB    1 
ATOM   6024  C CG1   . VAL B  1 401 ? -13.887 22.029  -55.369 1.00 29.54 ? 401 VAL D CG1   1 
ATOM   6025  C CG2   . VAL B  1 401 ? -13.346 20.849  -53.207 1.00 29.97 ? 401 VAL D CG2   1 
ATOM   6026  N N     . VAL B  1 402 ? -10.923 18.790  -54.923 1.00 36.79 ? 402 VAL D N     1 
ATOM   6027  C CA    . VAL B  1 402 ? -9.889  17.868  -54.477 1.00 38.44 ? 402 VAL D CA    1 
ATOM   6028  C C     . VAL B  1 402 ? -9.192  18.448  -53.261 1.00 38.35 ? 402 VAL D C     1 
ATOM   6029  O O     . VAL B  1 402 ? -8.685  19.580  -53.302 1.00 33.45 ? 402 VAL D O     1 
ATOM   6030  C CB    . VAL B  1 402 ? -8.877  17.606  -55.596 1.00 33.80 ? 402 VAL D CB    1 
ATOM   6031  C CG1   . VAL B  1 402 ? -8.011  16.401  -55.251 1.00 31.14 ? 402 VAL D CG1   1 
ATOM   6032  C CG2   . VAL B  1 402 ? -9.611  17.408  -56.900 1.00 34.36 ? 402 VAL D CG2   1 
ATOM   6033  N N     . LEU B  1 403 ? -9.146  17.664  -52.186 1.00 37.50 ? 403 LEU D N     1 
ATOM   6034  C CA    . LEU B  1 403 ? -8.394  18.027  -50.998 1.00 32.81 ? 403 LEU D CA    1 
ATOM   6035  C C     . LEU B  1 403 ? -7.149  17.165  -50.818 1.00 33.74 ? 403 LEU D C     1 
ATOM   6036  O O     . LEU B  1 403 ? -6.515  17.200  -49.758 1.00 40.15 ? 403 LEU D O     1 
ATOM   6037  C CB    . LEU B  1 403 ? -9.302  17.944  -49.777 1.00 31.84 ? 403 LEU D CB    1 
ATOM   6038  C CG    . LEU B  1 403 ? -10.084 19.234  -49.502 1.00 33.93 ? 403 LEU D CG    1 
ATOM   6039  C CD1   . LEU B  1 403 ? -10.801 19.801  -50.719 1.00 33.24 ? 403 LEU D CD1   1 
ATOM   6040  C CD2   . LEU B  1 403 ? -11.081 18.999  -48.372 1.00 40.30 ? 403 LEU D CD2   1 
ATOM   6041  N N     . GLY B  1 404 ? -6.766  16.404  -51.832 1.00 36.56 ? 404 GLY D N     1 
ATOM   6042  C CA    . GLY B  1 404 ? -5.598  15.566  -51.693 1.00 38.51 ? 404 GLY D CA    1 
ATOM   6043  C C     . GLY B  1 404 ? -5.618  14.415  -52.671 1.00 36.58 ? 404 GLY D C     1 
ATOM   6044  O O     . GLY B  1 404 ? -6.587  13.659  -52.748 1.00 31.51 ? 404 GLY D O     1 
ATOM   6045  N N     . CYS B  1 405 ? -4.551  14.277  -53.440 1.00 40.92 ? 405 CYS D N     1 
ATOM   6046  C CA    . CYS B  1 405 ? -4.560  13.213  -54.427 1.00 39.56 ? 405 CYS D CA    1 
ATOM   6047  C C     . CYS B  1 405 ? -4.172  11.879  -53.834 1.00 41.73 ? 405 CYS D C     1 
ATOM   6048  O O     . CYS B  1 405 ? -4.390  10.845  -54.475 1.00 40.64 ? 405 CYS D O     1 
ATOM   6049  C CB    . CYS B  1 405 ? -3.614  13.542  -55.567 1.00 39.88 ? 405 CYS D CB    1 
ATOM   6050  S SG    . CYS B  1 405 ? -3.960  15.095  -56.321 1.00 40.05 ? 405 CYS D SG    1 
ATOM   6051  N N     . ASN B  1 406 ? -3.617  11.875  -52.626 1.00 40.50 ? 406 ASN D N     1 
ATOM   6052  C CA    . ASN B  1 406 ? -3.007  10.662  -52.110 1.00 40.24 ? 406 ASN D CA    1 
ATOM   6053  C C     . ASN B  1 406 ? -2.820  10.785  -50.606 1.00 43.23 ? 406 ASN D C     1 
ATOM   6054  O O     . ASN B  1 406 ? -1.738  11.155  -50.136 1.00 42.61 ? 406 ASN D O     1 
ATOM   6055  C CB    . ASN B  1 406 ? -1.670  10.430  -52.814 1.00 44.80 ? 406 ASN D CB    1 
ATOM   6056  C CG    . ASN B  1 406 ? -1.215  8.995   -52.728 1.00 47.19 ? 406 ASN D CG    1 
ATOM   6057  O OD1   . ASN B  1 406 ? -2.027  8.079   -52.552 1.00 48.16 ? 406 ASN D OD1   1 
ATOM   6058  N ND2   . ASN B  1 406 ? 0.092   8.789   -52.839 1.00 46.20 ? 406 ASN D ND2   1 
ATOM   6059  N N     . SER B  1 407 ? -3.862  10.511  -49.837 1.00 42.01 ? 407 SER D N     1 
ATOM   6060  C CA    . SER B  1 407 ? -3.784  10.758  -48.408 1.00 45.39 ? 407 SER D CA    1 
ATOM   6061  C C     . SER B  1 407 ? -4.045  9.485   -47.619 1.00 46.02 ? 407 SER D C     1 
ATOM   6062  O O     . SER B  1 407 ? -4.616  8.506   -48.119 1.00 41.04 ? 407 SER D O     1 
ATOM   6063  C CB    . SER B  1 407 ? -4.761  11.855  -47.983 1.00 44.82 ? 407 SER D CB    1 
ATOM   6064  O OG    . SER B  1 407 ? -5.979  11.737  -48.693 1.00 47.58 ? 407 SER D OG    1 
ATOM   6065  N N     . ASP B  1 408 ? -3.609  9.521   -46.368 1.00 48.50 ? 408 ASP D N     1 
ATOM   6066  C CA    . ASP B  1 408 ? -3.687  8.371   -45.484 1.00 48.82 ? 408 ASP D CA    1 
ATOM   6067  C C     . ASP B  1 408 ? -4.946  8.338   -44.651 1.00 48.33 ? 408 ASP D C     1 
ATOM   6068  O O     . ASP B  1 408 ? -5.238  7.294   -44.054 1.00 47.15 ? 408 ASP D O     1 
ATOM   6069  C CB    . ASP B  1 408 ? -2.487  8.347   -44.546 1.00 48.62 ? 408 ASP D CB    1 
ATOM   6070  C CG    . ASP B  1 408 ? -1.218  7.982   -45.255 1.00 55.61 ? 408 ASP D CG    1 
ATOM   6071  O OD1   . ASP B  1 408 ? -1.291  7.579   -46.450 1.00 51.60 ? 408 ASP D OD1   1 
ATOM   6072  O OD2   . ASP B  1 408 ? -0.153  8.096   -44.611 1.00 55.32 ? 408 ASP D OD2   1 
ATOM   6073  N N     . LEU B  1 409 ? -5.689  9.450   -44.597 1.00 50.94 ? 409 LEU D N     1 
ATOM   6074  C CA    . LEU B  1 409 ? -6.791  9.575   -43.638 1.00 55.30 ? 409 LEU D CA    1 
ATOM   6075  C C     . LEU B  1 409 ? -7.945  8.648   -44.006 1.00 55.27 ? 409 LEU D C     1 
ATOM   6076  O O     . LEU B  1 409 ? -8.417  7.861   -43.174 1.00 54.48 ? 409 LEU D O     1 
ATOM   6077  C CB    . LEU B  1 409 ? -7.243  11.043  -43.529 1.00 50.23 ? 409 LEU D CB    1 
ATOM   6078  C CG    . LEU B  1 409 ? -8.078  11.757  -44.591 1.00 44.38 ? 409 LEU D CG    1 
ATOM   6079  C CD1   . LEU B  1 409 ? -8.385  13.231  -44.246 1.00 36.26 ? 409 LEU D CD1   1 
ATOM   6080  C CD2   . LEU B  1 409 ? -7.382  11.659  -45.932 1.00 55.54 ? 409 LEU D CD2   1 
ATOM   6081  N N     . GLY B  1 410 ? -8.404  8.717   -45.247 1.00 51.87 ? 410 GLY D N     1 
ATOM   6082  C CA    . GLY B  1 410 ? -9.228  7.677   -45.804 1.00 48.91 ? 410 GLY D CA    1 
ATOM   6083  C C     . GLY B  1 410 ? -8.510  7.200   -47.037 1.00 54.18 ? 410 GLY D C     1 
ATOM   6084  O O     . GLY B  1 410 ? -8.780  7.669   -48.159 1.00 51.08 ? 410 GLY D O     1 
ATOM   6085  N N     . PRO B  1 411 ? -7.567  6.218   -46.843 1.00 52.61 ? 411 PRO D N     1 
ATOM   6086  C CA    . PRO B  1 411 ? -6.468  6.041   -47.807 1.00 39.38 ? 411 PRO D CA    1 
ATOM   6087  C C     . PRO B  1 411 ? -7.021  6.112   -49.205 1.00 45.68 ? 411 PRO D C     1 
ATOM   6088  O O     . PRO B  1 411 ? -7.873  5.303   -49.562 1.00 49.34 ? 411 PRO D O     1 
ATOM   6089  C CB    . PRO B  1 411 ? -5.901  4.649   -47.491 1.00 34.48 ? 411 PRO D CB    1 
ATOM   6090  C CG    . PRO B  1 411 ? -6.630  4.151   -46.316 1.00 43.18 ? 411 PRO D CG    1 
ATOM   6091  C CD    . PRO B  1 411 ? -7.869  4.976   -46.110 1.00 45.89 ? 411 PRO D CD    1 
ATOM   6092  N N     . GLY B  1 412 ? -6.637  7.127   -49.950 1.00 45.20 ? 412 GLY D N     1 
ATOM   6093  C CA    . GLY B  1 412 ? -7.198  7.355   -51.260 1.00 42.41 ? 412 GLY D CA    1 
ATOM   6094  C C     . GLY B  1 412 ? -7.117  8.827   -51.576 1.00 40.58 ? 412 GLY D C     1 
ATOM   6095  O O     . GLY B  1 412 ? -6.459  9.588   -50.876 1.00 42.82 ? 412 GLY D O     1 
ATOM   6096  N N     . ALA B  1 413 ? -7.778  9.210   -52.660 1.00 39.00 ? 413 ALA D N     1 
ATOM   6097  C CA    . ALA B  1 413 ? -7.979  10.623  -52.925 1.00 40.08 ? 413 ALA D CA    1 
ATOM   6098  C C     . ALA B  1 413 ? -9.132  11.115  -52.068 1.00 36.66 ? 413 ALA D C     1 
ATOM   6099  O O     . ALA B  1 413 ? -10.140 10.420  -51.916 1.00 38.81 ? 413 ALA D O     1 
ATOM   6100  C CB    . ALA B  1 413 ? -8.267  10.868  -54.409 1.00 29.29 ? 413 ALA D CB    1 
ATOM   6101  N N     . GLU B  1 414 ? -8.974  12.300  -51.480 1.00 34.93 ? 414 GLU D N     1 
ATOM   6102  C CA    . GLU B  1 414 ? -10.015 12.896  -50.645 1.00 36.15 ? 414 GLU D CA    1 
ATOM   6103  C C     . GLU B  1 414 ? -10.717 14.024  -51.396 1.00 37.05 ? 414 GLU D C     1 
ATOM   6104  O O     . GLU B  1 414 ? -10.099 15.055  -51.701 1.00 34.83 ? 414 GLU D O     1 
ATOM   6105  C CB    . GLU B  1 414 ? -9.448  13.415  -49.327 1.00 35.66 ? 414 GLU D CB    1 
ATOM   6106  C CG    . GLU B  1 414 ? -10.525 13.982  -48.392 1.00 37.89 ? 414 GLU D CG    1 
ATOM   6107  C CD    . GLU B  1 414 ? -9.975  14.908  -47.313 1.00 37.84 ? 414 GLU D CD    1 
ATOM   6108  O OE1   . GLU B  1 414 ? -8.730  15.121  -47.277 1.00 34.29 ? 414 GLU D OE1   1 
ATOM   6109  O OE2   . GLU B  1 414 ? -10.802 15.429  -46.522 1.00 29.30 ? 414 GLU D OE2   1 
ATOM   6110  N N     . LEU B  1 415 ? -12.013 13.839  -51.656 1.00 38.88 ? 415 LEU D N     1 
ATOM   6111  C CA    . LEU B  1 415 ? -12.851 14.794  -52.373 1.00 38.41 ? 415 LEU D CA    1 
ATOM   6112  C C     . LEU B  1 415 ? -13.867 15.445  -51.442 1.00 37.31 ? 415 LEU D C     1 
ATOM   6113  O O     . LEU B  1 415 ? -14.244 14.894  -50.404 1.00 38.78 ? 415 LEU D O     1 
ATOM   6114  C CB    . LEU B  1 415 ? -13.604 14.119  -53.530 1.00 32.08 ? 415 LEU D CB    1 
ATOM   6115  C CG    . LEU B  1 415 ? -12.798 13.524  -54.687 1.00 33.29 ? 415 LEU D CG    1 
ATOM   6116  C CD1   . LEU B  1 415 ? -13.587 13.638  -56.024 1.00 37.60 ? 415 LEU D CD1   1 
ATOM   6117  C CD2   . LEU B  1 415 ? -11.419 14.179  -54.781 1.00 25.36 ? 415 LEU D CD2   1 
ATOM   6118  N N     . LEU B  1 416 ? -14.321 16.629  -51.845 1.00 34.81 ? 416 LEU D N     1 
ATOM   6119  C CA    . LEU B  1 416 ? -15.413 17.339  -51.193 1.00 31.61 ? 416 LEU D CA    1 
ATOM   6120  C C     . LEU B  1 416 ? -16.401 17.726  -52.281 1.00 40.16 ? 416 LEU D C     1 
ATOM   6121  O O     . LEU B  1 416 ? -15.987 18.242  -53.324 1.00 39.09 ? 416 LEU D O     1 
ATOM   6122  C CB    . LEU B  1 416 ? -14.901 18.576  -50.475 1.00 29.26 ? 416 LEU D CB    1 
ATOM   6123  C CG    . LEU B  1 416 ? -15.879 19.246  -49.529 1.00 31.57 ? 416 LEU D CG    1 
ATOM   6124  C CD1   . LEU B  1 416 ? -16.378 18.213  -48.560 1.00 36.67 ? 416 LEU D CD1   1 
ATOM   6125  C CD2   . LEU B  1 416 ? -15.208 20.397  -48.792 1.00 28.20 ? 416 LEU D CD2   1 
ATOM   6126  N N     . VAL B  1 417 ? -17.699 17.483  -52.052 1.00 40.89 ? 417 VAL D N     1 
ATOM   6127  C CA    . VAL B  1 417 ? -18.717 17.606  -53.101 1.00 42.02 ? 417 VAL D CA    1 
ATOM   6128  C C     . VAL B  1 417 ? -19.901 18.463  -52.639 1.00 43.18 ? 417 VAL D C     1 
ATOM   6129  O O     . VAL B  1 417 ? -20.434 18.258  -51.545 1.00 40.67 ? 417 VAL D O     1 
ATOM   6130  C CB    . VAL B  1 417 ? -19.214 16.216  -53.539 1.00 41.68 ? 417 VAL D CB    1 
ATOM   6131  C CG1   . VAL B  1 417 ? -19.929 16.317  -54.892 1.00 51.52 ? 417 VAL D CG1   1 
ATOM   6132  C CG2   . VAL B  1 417 ? -18.065 15.230  -53.602 1.00 36.00 ? 417 VAL D CG2   1 
ATOM   6133  N N     . PHE B  1 418 ? -20.362 19.369  -53.508 1.00 37.09 ? 418 PHE D N     1 
ATOM   6134  C CA    . PHE B  1 418 ? -21.378 20.356  -53.172 1.00 35.46 ? 418 PHE D CA    1 
ATOM   6135  C C     . PHE B  1 418 ? -22.651 20.139  -53.963 1.00 39.63 ? 418 PHE D C     1 
ATOM   6136  O O     . PHE B  1 418 ? -22.600 19.742  -55.124 1.00 43.64 ? 418 PHE D O     1 
ATOM   6137  C CB    . PHE B  1 418 ? -20.885 21.748  -53.482 1.00 37.94 ? 418 PHE D CB    1 
ATOM   6138  C CG    . PHE B  1 418 ? -19.833 22.201  -52.567 1.00 36.31 ? 418 PHE D CG    1 
ATOM   6139  C CD1   . PHE B  1 418 ? -20.104 22.343  -51.218 1.00 36.74 ? 418 PHE D CD1   1 
ATOM   6140  C CD2   . PHE B  1 418 ? -18.571 22.447  -53.030 1.00 34.60 ? 418 PHE D CD2   1 
ATOM   6141  C CE1   . PHE B  1 418 ? -19.132 22.729  -50.344 1.00 35.50 ? 418 PHE D CE1   1 
ATOM   6142  C CE2   . PHE B  1 418 ? -17.581 22.851  -52.170 1.00 35.68 ? 418 PHE D CE2   1 
ATOM   6143  C CZ    . PHE B  1 418 ? -17.863 22.991  -50.816 1.00 44.17 ? 418 PHE D CZ    1 
ATOM   6144  N N     . SER B  1 419 ? -23.792 20.471  -53.357 1.00 41.45 ? 419 SER D N     1 
ATOM   6145  C CA    . SER B  1 419 ? -25.060 20.381  -54.077 1.00 40.48 ? 419 SER D CA    1 
ATOM   6146  C C     . SER B  1 419 ? -26.185 21.075  -53.314 1.00 49.62 ? 419 SER D C     1 
ATOM   6147  O O     . SER B  1 419 ? -26.325 20.904  -52.096 1.00 48.17 ? 419 SER D O     1 
ATOM   6148  C CB    . SER B  1 419 ? -25.450 18.921  -54.332 1.00 42.13 ? 419 SER D CB    1 
ATOM   6149  O OG    . SER B  1 419 ? -26.615 18.841  -55.128 1.00 44.70 ? 419 SER D OG    1 
ATOM   6150  N N     . LYS B  1 420 ? -27.013 21.824  -54.048 1.00 48.16 ? 420 LYS D N     1 
ATOM   6151  C CA    . LYS B  1 420 ? -28.225 22.395  -53.478 1.00 43.39 ? 420 LYS D CA    1 
ATOM   6152  C C     . LYS B  1 420 ? -29.260 21.341  -53.135 1.00 48.92 ? 420 LYS D C     1 
ATOM   6153  O O     . LYS B  1 420 ? -30.351 21.699  -52.681 1.00 51.89 ? 420 LYS D O     1 
ATOM   6154  C CB    . LYS B  1 420 ? -28.847 23.395  -54.446 1.00 43.37 ? 420 LYS D CB    1 
ATOM   6155  C CG    . LYS B  1 420 ? -27.860 24.313  -55.136 1.00 50.64 ? 420 LYS D CG    1 
ATOM   6156  C CD    . LYS B  1 420 ? -27.175 25.245  -54.141 1.00 50.22 ? 420 LYS D CD    1 
ATOM   6157  C CE    . LYS B  1 420 ? -27.639 26.684  -54.325 1.00 52.38 ? 420 LYS D CE    1 
ATOM   6158  N NZ    . LYS B  1 420 ? -26.602 27.661  -53.923 1.00 51.66 ? 420 LYS D NZ    1 
ATOM   6159  N N     . ASP B  1 421 ? -28.960 20.061  -53.334 1.00 44.50 ? 421 ASP D N     1 
ATOM   6160  C CA    . ASP B  1 421 ? -29.969 19.015  -53.224 1.00 46.49 ? 421 ASP D CA    1 
ATOM   6161  C C     . ASP B  1 421 ? -29.285 17.741  -52.760 1.00 46.38 ? 421 ASP D C     1 
ATOM   6162  O O     . ASP B  1 421 ? -28.343 17.280  -53.409 1.00 51.29 ? 421 ASP D O     1 
ATOM   6163  C CB    . ASP B  1 421 ? -30.660 18.808  -54.574 1.00 49.12 ? 421 ASP D CB    1 
ATOM   6164  C CG    . ASP B  1 421 ? -31.654 17.664  -54.561 1.00 51.97 ? 421 ASP D CG    1 
ATOM   6165  O OD1   . ASP B  1 421 ? -31.222 16.481  -54.642 1.00 44.46 ? 421 ASP D OD1   1 
ATOM   6166  O OD2   . ASP B  1 421 ? -32.871 17.965  -54.491 1.00 47.30 ? 421 ASP D OD2   1 
ATOM   6167  N N     . TRP B  1 422 ? -29.745 17.173  -51.648 1.00 45.41 ? 422 TRP D N     1 
ATOM   6168  C CA    . TRP B  1 422 ? -29.110 15.964  -51.134 1.00 47.37 ? 422 TRP D CA    1 
ATOM   6169  C C     . TRP B  1 422 ? -29.137 14.850  -52.172 1.00 50.29 ? 422 TRP D C     1 
ATOM   6170  O O     . TRP B  1 422 ? -28.111 14.213  -52.435 1.00 49.92 ? 422 TRP D O     1 
ATOM   6171  C CB    . TRP B  1 422 ? -29.786 15.523  -49.829 1.00 50.73 ? 422 TRP D CB    1 
ATOM   6172  C CG    . TRP B  1 422 ? -29.756 14.030  -49.562 1.00 55.57 ? 422 TRP D CG    1 
ATOM   6173  C CD1   . TRP B  1 422 ? -30.825 13.170  -49.584 1.00 60.12 ? 422 TRP D CD1   1 
ATOM   6174  C CD2   . TRP B  1 422 ? -28.617 13.233  -49.217 1.00 57.38 ? 422 TRP D CD2   1 
ATOM   6175  N NE1   . TRP B  1 422 ? -30.418 11.890  -49.284 1.00 60.15 ? 422 TRP D NE1   1 
ATOM   6176  C CE2   . TRP B  1 422 ? -29.069 11.899  -49.056 1.00 64.79 ? 422 TRP D CE2   1 
ATOM   6177  C CE3   . TRP B  1 422 ? -27.257 13.509  -49.044 1.00 59.76 ? 422 TRP D CE3   1 
ATOM   6178  C CZ2   . TRP B  1 422 ? -28.207 10.846  -48.725 1.00 67.93 ? 422 TRP D CZ2   1 
ATOM   6179  C CZ3   . TRP B  1 422 ? -26.398 12.459  -48.717 1.00 65.70 ? 422 TRP D CZ3   1 
ATOM   6180  C CH2   . TRP B  1 422 ? -26.879 11.144  -48.560 1.00 63.66 ? 422 TRP D CH2   1 
ATOM   6181  N N     . ASP B  1 423 ? -30.297 14.628  -52.804 1.00 53.14 ? 423 ASP D N     1 
ATOM   6182  C CA    . ASP B  1 423 ? -30.436 13.507  -53.735 1.00 52.76 ? 423 ASP D CA    1 
ATOM   6183  C C     . ASP B  1 423 ? -29.492 13.650  -54.924 1.00 50.32 ? 423 ASP D C     1 
ATOM   6184  O O     . ASP B  1 423 ? -28.895 12.666  -55.376 1.00 50.14 ? 423 ASP D O     1 
ATOM   6185  C CB    . ASP B  1 423 ? -31.885 13.392  -54.215 1.00 52.62 ? 423 ASP D CB    1 
ATOM   6186  C CG    . ASP B  1 423 ? -32.880 13.464  -53.076 1.00 55.05 ? 423 ASP D CG    1 
ATOM   6187  O OD1   . ASP B  1 423 ? -32.803 12.617  -52.157 1.00 54.02 ? 423 ASP D OD1   1 
ATOM   6188  O OD2   . ASP B  1 423 ? -33.728 14.384  -53.097 1.00 55.64 ? 423 ASP D OD2   1 
ATOM   6189  N N     . ARG B  1 424 ? -29.351 14.865  -55.455 1.00 50.70 ? 424 ARG D N     1 
ATOM   6190  C CA    . ARG B  1 424 ? -28.358 15.081  -56.499 1.00 47.75 ? 424 ARG D CA    1 
ATOM   6191  C C     . ARG B  1 424 ? -26.965 14.717  -55.996 1.00 46.42 ? 424 ARG D C     1 
ATOM   6192  O O     . ARG B  1 424 ? -26.229 13.978  -56.663 1.00 42.35 ? 424 ARG D O     1 
ATOM   6193  C CB    . ARG B  1 424 ? -28.405 16.533  -56.983 1.00 51.77 ? 424 ARG D CB    1 
ATOM   6194  C CG    . ARG B  1 424 ? -29.354 16.768  -58.155 1.00 53.68 ? 424 ARG D CG    1 
ATOM   6195  C CD    . ARG B  1 424 ? -30.180 18.035  -57.934 1.00 57.17 ? 424 ARG D CD    1 
ATOM   6196  N NE    . ARG B  1 424 ? -30.501 18.734  -59.174 1.00 61.91 ? 424 ARG D NE    1 
ATOM   6197  C CZ    . ARG B  1 424 ? -31.519 18.439  -59.976 1.00 66.93 ? 424 ARG D CZ    1 
ATOM   6198  N NH1   . ARG B  1 424 ? -32.372 17.467  -59.690 1.00 64.07 ? 424 ARG D NH1   1 
ATOM   6199  N NH2   . ARG B  1 424 ? -31.685 19.137  -61.098 1.00 67.93 ? 424 ARG D NH2   1 
ATOM   6200  N N     . LEU B  1 425 ? -26.602 15.209  -54.800 1.00 44.20 ? 425 LEU D N     1 
ATOM   6201  C CA    . LEU B  1 425 ? -25.297 14.911  -54.204 1.00 45.10 ? 425 LEU D CA    1 
ATOM   6202  C C     . LEU B  1 425 ? -25.031 13.413  -54.158 1.00 42.39 ? 425 LEU D C     1 
ATOM   6203  O O     . LEU B  1 425 ? -23.907 12.964  -54.414 1.00 35.93 ? 425 LEU D O     1 
ATOM   6204  C CB    . LEU B  1 425 ? -25.223 15.503  -52.792 1.00 45.70 ? 425 LEU D CB    1 
ATOM   6205  C CG    . LEU B  1 425 ? -23.871 15.795  -52.126 1.00 39.59 ? 425 LEU D CG    1 
ATOM   6206  C CD1   . LEU B  1 425 ? -22.973 16.650  -53.018 1.00 38.60 ? 425 LEU D CD1   1 
ATOM   6207  C CD2   . LEU B  1 425 ? -24.061 16.474  -50.769 1.00 34.88 ? 425 LEU D CD2   1 
ATOM   6208  N N     . THR B  1 426 ? -26.070 12.626  -53.845 1.00 46.43 ? 426 THR D N     1 
ATOM   6209  C CA    . THR B  1 426 ? -25.946 11.174  -53.764 1.00 42.94 ? 426 THR D CA    1 
ATOM   6210  C C     . THR B  1 426 ? -25.698 10.562  -55.134 1.00 44.91 ? 426 THR D C     1 
ATOM   6211  O O     . THR B  1 426 ? -24.960 9.578   -55.259 1.00 45.28 ? 426 THR D O     1 
ATOM   6212  C CB    . THR B  1 426 ? -27.208 10.581  -53.140 1.00 48.64 ? 426 THR D CB    1 
ATOM   6213  O OG1   . THR B  1 426 ? -27.489 11.252  -51.903 1.00 54.74 ? 426 THR D OG1   1 
ATOM   6214  C CG2   . THR B  1 426 ? -27.023 9.096   -52.859 1.00 49.32 ? 426 THR D CG2   1 
ATOM   6215  N N     . ALA B  1 427 ? -26.319 11.112  -56.173 1.00 44.14 ? 427 ALA D N     1 
ATOM   6216  C CA    . ALA B  1 427 ? -26.025 10.635  -57.517 1.00 42.88 ? 427 ALA D CA    1 
ATOM   6217  C C     . ALA B  1 427 ? -24.605 11.016  -57.920 1.00 38.54 ? 427 ALA D C     1 
ATOM   6218  O O     . ALA B  1 427 ? -23.830 10.171  -58.386 1.00 41.43 ? 427 ALA D O     1 
ATOM   6219  C CB    . ALA B  1 427 ? -27.053 11.189  -58.505 1.00 42.89 ? 427 ALA D CB    1 
ATOM   6220  N N     . MET B  1 428 ? -24.239 12.282  -57.713 1.00 40.08 ? 428 MET D N     1 
ATOM   6221  C CA    . MET B  1 428 ? -22.897 12.742  -58.058 1.00 39.61 ? 428 MET D CA    1 
ATOM   6222  C C     . MET B  1 428 ? -21.826 11.848  -57.437 1.00 41.93 ? 428 MET D C     1 
ATOM   6223  O O     . MET B  1 428 ? -20.835 11.499  -58.088 1.00 42.89 ? 428 MET D O     1 
ATOM   6224  C CB    . MET B  1 428 ? -22.700 14.185  -57.589 1.00 38.95 ? 428 MET D CB    1 
ATOM   6225  C CG    . MET B  1 428 ? -23.296 15.282  -58.453 1.00 36.20 ? 428 MET D CG    1 
ATOM   6226  S SD    . MET B  1 428 ? -23.520 16.789  -57.473 1.00 43.91 ? 428 MET D SD    1 
ATOM   6227  C CE    . MET B  1 428 ? -23.084 18.031  -58.687 1.00 44.87 ? 428 MET D CE    1 
ATOM   6228  N N     . LYS B  1 429 ? -22.003 11.469  -56.171 1.00 44.54 ? 429 LYS D N     1 
ATOM   6229  C CA    . LYS B  1 429 ? -21.016 10.614  -55.524 1.00 38.05 ? 429 LYS D CA    1 
ATOM   6230  C C     . LYS B  1 429 ? -20.936 9.261   -56.220 1.00 38.88 ? 429 LYS D C     1 
ATOM   6231  O O     . LYS B  1 429 ? -19.844 8.782   -56.550 1.00 42.47 ? 429 LYS D O     1 
ATOM   6232  C CB    . LYS B  1 429 ? -21.361 10.471  -54.044 1.00 38.21 ? 429 LYS D CB    1 
ATOM   6233  C CG    . LYS B  1 429 ? -20.918 11.669  -53.235 1.00 37.26 ? 429 LYS D CG    1 
ATOM   6234  C CD    . LYS B  1 429 ? -21.888 12.027  -52.086 1.00 47.57 ? 429 LYS D CD    1 
ATOM   6235  C CE    . LYS B  1 429 ? -21.892 10.991  -50.945 1.00 49.78 ? 429 LYS D CE    1 
ATOM   6236  N NZ    . LYS B  1 429 ? -23.282 10.664  -50.458 1.00 56.63 ? 429 LYS D NZ    1 
ATOM   6237  N N     . ASP B  1 430 ? -22.093 8.647   -56.485 1.00 40.64 ? 430 ASP D N     1 
ATOM   6238  C CA    . ASP B  1 430 ? -22.121 7.345   -57.142 1.00 41.32 ? 430 ASP D CA    1 
ATOM   6239  C C     . ASP B  1 430 ? -21.479 7.405   -58.519 1.00 43.29 ? 430 ASP D C     1 
ATOM   6240  O O     . ASP B  1 430 ? -20.918 6.409   -58.991 1.00 43.13 ? 430 ASP D O     1 
ATOM   6241  C CB    . ASP B  1 430 ? -23.562 6.850   -57.252 1.00 42.86 ? 430 ASP D CB    1 
ATOM   6242  C CG    . ASP B  1 430 ? -24.061 6.195   -55.968 1.00 52.67 ? 430 ASP D CG    1 
ATOM   6243  O OD1   . ASP B  1 430 ? -23.224 5.679   -55.181 1.00 48.98 ? 430 ASP D OD1   1 
ATOM   6244  O OD2   . ASP B  1 430 ? -25.300 6.204   -55.746 1.00 52.72 ? 430 ASP D OD2   1 
ATOM   6245  N N     . GLU B  1 431 ? -21.556 8.563   -59.176 1.00 44.50 ? 431 GLU D N     1 
ATOM   6246  C CA    . GLU B  1 431 ? -20.818 8.764   -60.419 1.00 48.52 ? 431 GLU D CA    1 
ATOM   6247  C C     . GLU B  1 431 ? -19.317 8.752   -60.169 1.00 44.76 ? 431 GLU D C     1 
ATOM   6248  O O     . GLU B  1 431 ? -18.568 8.056   -60.866 1.00 46.17 ? 431 GLU D O     1 
ATOM   6249  C CB    . GLU B  1 431 ? -21.234 10.081  -61.082 1.00 42.16 ? 431 GLU D CB    1 
ATOM   6250  C CG    . GLU B  1 431 ? -22.640 10.082  -61.655 1.00 40.25 ? 431 GLU D CG    1 
ATOM   6251  C CD    . GLU B  1 431 ? -22.932 8.848   -62.487 1.00 48.48 ? 431 GLU D CD    1 
ATOM   6252  O OE1   . GLU B  1 431 ? -21.991 8.288   -63.096 1.00 55.06 ? 431 GLU D OE1   1 
ATOM   6253  O OE2   . GLU B  1 431 ? -24.113 8.434   -62.537 1.00 58.47 ? 431 GLU D OE2   1 
ATOM   6254  N N     . ILE B  1 432 ? -18.861 9.529   -59.183 1.00 40.20 ? 432 ILE D N     1 
ATOM   6255  C CA    . ILE B  1 432 ? -17.436 9.565   -58.873 1.00 42.64 ? 432 ILE D CA    1 
ATOM   6256  C C     . ILE B  1 432 ? -16.939 8.169   -58.546 1.00 45.74 ? 432 ILE D C     1 
ATOM   6257  O O     . ILE B  1 432 ? -15.823 7.783   -58.922 1.00 44.40 ? 432 ILE D O     1 
ATOM   6258  C CB    . ILE B  1 432 ? -17.170 10.561  -57.735 1.00 40.11 ? 432 ILE D CB    1 
ATOM   6259  C CG1   . ILE B  1 432 ? -17.514 11.965  -58.219 1.00 42.54 ? 432 ILE D CG1   1 
ATOM   6260  C CG2   . ILE B  1 432 ? -15.722 10.498  -57.283 1.00 38.59 ? 432 ILE D CG2   1 
ATOM   6261  C CD1   . ILE B  1 432 ? -18.201 12.805  -57.199 1.00 33.37 ? 432 ILE D CD1   1 
ATOM   6262  N N     . ALA B  1 433 ? -17.774 7.375   -57.874 1.00 44.44 ? 433 ALA D N     1 
ATOM   6263  C CA    . ALA B  1 433 ? -17.532 5.941   -57.814 1.00 42.54 ? 433 ALA D CA    1 
ATOM   6264  C C     . ALA B  1 433 ? -17.332 5.376   -59.220 1.00 41.17 ? 433 ALA D C     1 
ATOM   6265  O O     . ALA B  1 433 ? -16.252 4.880   -59.557 1.00 36.69 ? 433 ALA D O     1 
ATOM   6266  C CB    . ALA B  1 433 ? -18.690 5.253   -57.093 1.00 42.40 ? 433 ALA D CB    1 
ATOM   6267  N N     . THR B  1 434 ? -18.360 5.505   -60.069 1.00 43.42 ? 434 THR D N     1 
ATOM   6268  C CA    . THR B  1 434 ? -18.341 4.903   -61.407 1.00 44.73 ? 434 THR D CA    1 
ATOM   6269  C C     . THR B  1 434 ? -17.128 5.340   -62.216 1.00 41.88 ? 434 THR D C     1 
ATOM   6270  O O     . THR B  1 434 ? -16.417 4.512   -62.797 1.00 45.36 ? 434 THR D O     1 
ATOM   6271  C CB    . THR B  1 434 ? -19.611 5.279   -62.171 1.00 45.91 ? 434 THR D CB    1 
ATOM   6272  O OG1   . THR B  1 434 ? -20.759 4.716   -61.525 1.00 44.51 ? 434 THR D OG1   1 
ATOM   6273  C CG2   . THR B  1 434 ? -19.531 4.794   -63.624 1.00 44.38 ? 434 THR D CG2   1 
ATOM   6274  N N     . THR B  1 435 ? -16.887 6.643   -62.273 1.00 43.66 ? 435 THR D N     1 
ATOM   6275  C CA    . THR B  1 435 ? -15.979 7.235   -63.244 1.00 40.28 ? 435 THR D CA    1 
ATOM   6276  C C     . THR B  1 435 ? -14.546 7.319   -62.756 1.00 41.87 ? 435 THR D C     1 
ATOM   6277  O O     . THR B  1 435 ? -13.616 7.194   -63.561 1.00 46.43 ? 435 THR D O     1 
ATOM   6278  C CB    . THR B  1 435 ? -16.470 8.637   -63.593 1.00 43.98 ? 435 THR D CB    1 
ATOM   6279  O OG1   . THR B  1 435 ? -17.772 8.555   -64.201 1.00 42.70 ? 435 THR D OG1   1 
ATOM   6280  C CG2   . THR B  1 435 ? -15.487 9.349   -64.506 1.00 43.94 ? 435 THR D CG2   1 
ATOM   6281  N N     . ALA B  1 436 ? -14.350 7.524   -61.455 1.00 46.62 ? 436 ALA D N     1 
ATOM   6282  C CA    . ALA B  1 436 ? -13.032 7.743   -60.876 1.00 47.01 ? 436 ALA D CA    1 
ATOM   6283  C C     . ALA B  1 436 ? -12.510 6.552   -60.101 1.00 41.92 ? 436 ALA D C     1 
ATOM   6284  O O     . ALA B  1 436 ? -11.300 6.336   -60.057 1.00 39.55 ? 436 ALA D O     1 
ATOM   6285  C CB    . ALA B  1 436 ? -13.061 8.960   -59.948 1.00 46.10 ? 436 ALA D CB    1 
ATOM   6286  N N     . GLY B  1 437 ? -13.391 5.785   -59.484 1.00 43.70 ? 437 GLY D N     1 
ATOM   6287  C CA    . GLY B  1 437 ? -12.953 4.560   -58.869 1.00 47.04 ? 437 GLY D CA    1 
ATOM   6288  C C     . GLY B  1 437 ? -12.707 4.694   -57.386 1.00 49.19 ? 437 GLY D C     1 
ATOM   6289  O O     . GLY B  1 437 ? -11.964 5.570   -56.929 1.00 52.39 ? 437 GLY D O     1 
ATOM   6290  N N     . THR B  1 438 ? -13.333 3.809   -56.631 1.00 46.36 ? 438 THR D N     1 
ATOM   6291  C CA    . THR B  1 438 ? -13.088 3.662   -55.210 1.00 55.08 ? 438 THR D CA    1 
ATOM   6292  C C     . THR B  1 438 ? -12.311 2.374   -54.963 1.00 59.73 ? 438 THR D C     1 
ATOM   6293  O O     . THR B  1 438 ? -12.134 1.530   -55.849 1.00 59.75 ? 438 THR D O     1 
ATOM   6294  C CB    . THR B  1 438 ? -14.411 3.671   -54.423 1.00 56.62 ? 438 THR D CB    1 
ATOM   6295  O OG1   . THR B  1 438 ? -14.965 2.343   -54.351 1.00 54.57 ? 438 THR D OG1   1 
ATOM   6296  C CG2   . THR B  1 438 ? -15.419 4.605   -55.109 1.00 44.93 ? 438 THR D CG2   1 
ATOM   6297  N N     . LEU B  1 439 ? -11.820 2.244   -53.744 1.00 59.21 ? 439 LEU D N     1 
ATOM   6298  C CA    . LEU B  1 439 ? -11.240 1.002   -53.275 1.00 57.46 ? 439 LEU D CA    1 
ATOM   6299  C C     . LEU B  1 439 ? -12.100 0.487   -52.135 1.00 62.04 ? 439 LEU D C     1 
ATOM   6300  O O     . LEU B  1 439 ? -12.584 1.267   -51.308 1.00 63.92 ? 439 LEU D O     1 
ATOM   6301  C CB    . LEU B  1 439 ? -9.797  1.216   -52.853 1.00 55.79 ? 439 LEU D CB    1 
ATOM   6302  C CG    . LEU B  1 439 ? -8.934  1.472   -54.093 1.00 62.32 ? 439 LEU D CG    1 
ATOM   6303  C CD1   . LEU B  1 439 ? -7.773  2.447   -53.817 1.00 51.42 ? 439 LEU D CD1   1 
ATOM   6304  C CD2   . LEU B  1 439 ? -8.435  0.137   -54.686 1.00 58.63 ? 439 LEU D CD2   1 
ATOM   6305  N N     . SER B  1 440 ? -12.328 -0.818  -52.122 1.00 62.06 ? 440 SER D N     1 
ATOM   6306  C CA    . SER B  1 440 ? -13.198 -1.415  -51.116 1.00 65.51 ? 440 SER D CA    1 
ATOM   6307  C C     . SER B  1 440 ? -12.474 -1.678  -49.780 1.00 68.39 ? 440 SER D C     1 
ATOM   6308  O O     . SER B  1 440 ? -11.258 -1.904  -49.710 1.00 63.01 ? 440 SER D O     1 
ATOM   6309  C CB    . SER B  1 440 ? -13.799 -2.711  -51.656 1.00 68.83 ? 440 SER D CB    1 
ATOM   6310  O OG    . SER B  1 440 ? -13.038 -3.834  -51.247 1.00 72.45 ? 440 SER D OG    1 
ATOM   6311  N N     . SER C  1 30  ? -45.963 61.447  11.342  1.00 50.57 ? 30  SER A N     1 
ATOM   6312  C CA    . SER C  1 30  ? -46.930 60.581  12.017  1.00 46.79 ? 30  SER A CA    1 
ATOM   6313  C C     . SER C  1 30  ? -46.581 59.102  11.861  1.00 49.58 ? 30  SER A C     1 
ATOM   6314  O O     . SER C  1 30  ? -46.612 58.348  12.839  1.00 53.96 ? 30  SER A O     1 
ATOM   6315  C CB    . SER C  1 30  ? -48.346 60.826  11.485  1.00 49.94 ? 30  SER A CB    1 
ATOM   6316  O OG    . SER C  1 30  ? -48.889 62.045  11.968  1.00 67.86 ? 30  SER A OG    1 
ATOM   6317  N N     . THR C  1 31  ? -46.263 58.693  10.634  1.00 41.77 ? 31  THR A N     1 
ATOM   6318  C CA    . THR C  1 31  ? -45.952 57.302  10.343  1.00 40.81 ? 31  THR A CA    1 
ATOM   6319  C C     . THR C  1 31  ? -44.460 57.031  10.535  1.00 38.27 ? 31  THR A C     1 
ATOM   6320  O O     . THR C  1 31  ? -43.626 57.939  10.512  1.00 38.64 ? 31  THR A O     1 
ATOM   6321  C CB    . THR C  1 31  ? -46.383 56.932  8.916   1.00 39.71 ? 31  THR A CB    1 
ATOM   6322  O OG1   . THR C  1 31  ? -45.269 56.400  8.187   1.00 38.62 ? 31  THR A OG1   1 
ATOM   6323  C CG2   . THR C  1 31  ? -46.942 58.144  8.175   1.00 43.83 ? 31  THR A CG2   1 
ATOM   6324  N N     . ASP C  1 32  ? -44.132 55.766  10.748  1.00 35.43 ? 32  ASP A N     1 
ATOM   6325  C CA    . ASP C  1 32  ? -42.740 55.332  10.762  1.00 36.73 ? 32  ASP A CA    1 
ATOM   6326  C C     . ASP C  1 32  ? -42.558 54.158  9.807   1.00 32.95 ? 32  ASP A C     1 
ATOM   6327  O O     . ASP C  1 32  ? -41.828 53.197  10.074  1.00 35.47 ? 32  ASP A O     1 
ATOM   6328  C CB    . ASP C  1 32  ? -42.278 55.006  12.181  1.00 30.36 ? 32  ASP A CB    1 
ATOM   6329  C CG    . ASP C  1 32  ? -42.884 53.728  12.729  1.00 30.80 ? 32  ASP A CG    1 
ATOM   6330  O OD1   . ASP C  1 32  ? -43.848 53.181  12.142  1.00 29.14 ? 32  ASP A OD1   1 
ATOM   6331  O OD2   . ASP C  1 32  ? -42.383 53.261  13.771  1.00 38.81 ? 32  ASP A OD2   1 
ATOM   6332  N N     . THR C  1 33  ? -43.234 54.235  8.667   1.00 33.02 ? 33  THR A N     1 
ATOM   6333  C CA    . THR C  1 33  ? -43.233 53.121  7.734   1.00 33.39 ? 33  THR A CA    1 
ATOM   6334  C C     . THR C  1 33  ? -41.814 52.801  7.269   1.00 35.61 ? 33  THR A C     1 
ATOM   6335  O O     . THR C  1 33  ? -41.362 51.654  7.367   1.00 40.96 ? 33  THR A O     1 
ATOM   6336  C CB    . THR C  1 33  ? -44.162 53.447  6.565   1.00 35.78 ? 33  THR A CB    1 
ATOM   6337  O OG1   . THR C  1 33  ? -45.311 54.159  7.051   1.00 34.86 ? 33  THR A OG1   1 
ATOM   6338  C CG2   . THR C  1 33  ? -44.630 52.167  5.885   1.00 40.01 ? 33  THR A CG2   1 
ATOM   6339  N N     . THR C  1 34  ? -41.075 53.818  6.821   1.00 34.57 ? 34  THR A N     1 
ATOM   6340  C CA    . THR C  1 34  ? -39.704 53.628  6.365   1.00 32.14 ? 34  THR A CA    1 
ATOM   6341  C C     . THR C  1 34  ? -38.738 53.244  7.484   1.00 38.50 ? 34  THR A C     1 
ATOM   6342  O O     . THR C  1 34  ? -37.561 53.010  7.184   1.00 36.65 ? 34  THR A O     1 
ATOM   6343  C CB    . THR C  1 34  ? -39.167 54.902  5.729   1.00 29.18 ? 34  THR A CB    1 
ATOM   6344  O OG1   . THR C  1 34  ? -39.019 55.889  6.756   1.00 38.00 ? 34  THR A OG1   1 
ATOM   6345  C CG2   . THR C  1 34  ? -40.106 55.422  4.694   1.00 29.26 ? 34  THR A CG2   1 
ATOM   6346  N N     . ALA C  1 35  ? -39.165 53.224  8.753   1.00 34.79 ? 35  ALA A N     1 
ATOM   6347  C CA    . ALA C  1 35  ? -38.236 52.876  9.825   1.00 32.84 ? 35  ALA A CA    1 
ATOM   6348  C C     . ALA C  1 35  ? -37.769 51.437  9.709   1.00 33.35 ? 35  ALA A C     1 
ATOM   6349  O O     . ALA C  1 35  ? -36.698 51.096  10.226  1.00 32.15 ? 35  ALA A O     1 
ATOM   6350  C CB    . ALA C  1 35  ? -38.879 53.103  11.205  1.00 35.54 ? 35  ALA A CB    1 
ATOM   6351  N N     . ARG C  1 36  ? -38.555 50.589  9.041   1.00 31.32 ? 36  ARG A N     1 
ATOM   6352  C CA    . ARG C  1 36  ? -38.164 49.199  8.869   1.00 32.82 ? 36  ARG A CA    1 
ATOM   6353  C C     . ARG C  1 36  ? -36.811 49.067  8.185   1.00 31.06 ? 36  ARG A C     1 
ATOM   6354  O O     . ARG C  1 36  ? -36.155 48.026  8.319   1.00 26.55 ? 36  ARG A O     1 
ATOM   6355  C CB    . ARG C  1 36  ? -39.222 48.471  8.060   1.00 32.46 ? 36  ARG A CB    1 
ATOM   6356  C CG    . ARG C  1 36  ? -39.440 49.089  6.689   1.00 31.90 ? 36  ARG A CG    1 
ATOM   6357  C CD    . ARG C  1 36  ? -40.787 48.646  6.170   1.00 32.91 ? 36  ARG A CD    1 
ATOM   6358  N NE    . ARG C  1 36  ? -41.037 47.234  6.441   1.00 34.40 ? 36  ARG A NE    1 
ATOM   6359  C CZ    . ARG C  1 36  ? -40.951 46.275  5.533   1.00 31.46 ? 36  ARG A CZ    1 
ATOM   6360  N NH1   . ARG C  1 36  ? -40.598 46.537  4.286   1.00 28.74 ? 36  ARG A NH1   1 
ATOM   6361  N NH2   . ARG C  1 36  ? -41.188 45.018  5.891   1.00 37.26 ? 36  ARG A NH2   1 
ATOM   6362  N N     . PHE C  1 37  ? -36.371 50.104  7.480   1.00 30.47 ? 37  PHE A N     1 
ATOM   6363  C CA    . PHE C  1 37  ? -35.167 50.033  6.676   1.00 27.11 ? 37  PHE A CA    1 
ATOM   6364  C C     . PHE C  1 37  ? -33.930 50.426  7.453   1.00 31.99 ? 37  PHE A C     1 
ATOM   6365  O O     . PHE C  1 37  ? -32.822 50.326  6.910   1.00 32.61 ? 37  PHE A O     1 
ATOM   6366  C CB    . PHE C  1 37  ? -35.309 50.911  5.436   1.00 27.91 ? 37  PHE A CB    1 
ATOM   6367  C CG    . PHE C  1 37  ? -36.383 50.447  4.493   1.00 31.35 ? 37  PHE A CG    1 
ATOM   6368  C CD1   . PHE C  1 37  ? -36.281 49.223  3.857   1.00 26.54 ? 37  PHE A CD1   1 
ATOM   6369  C CD2   . PHE C  1 37  ? -37.507 51.238  4.248   1.00 30.46 ? 37  PHE A CD2   1 
ATOM   6370  C CE1   . PHE C  1 37  ? -37.284 48.794  2.990   1.00 26.67 ? 37  PHE A CE1   1 
ATOM   6371  C CE2   . PHE C  1 37  ? -38.513 50.818  3.375   1.00 20.44 ? 37  PHE A CE2   1 
ATOM   6372  C CZ    . PHE C  1 37  ? -38.405 49.595  2.757   1.00 26.01 ? 37  PHE A CZ    1 
ATOM   6373  N N     . LEU C  1 38  ? -34.079 50.846  8.716   1.00 32.93 ? 38  LEU A N     1 
ATOM   6374  C CA    . LEU C  1 38  ? -32.897 51.051  9.545   1.00 25.06 ? 38  LEU A CA    1 
ATOM   6375  C C     . LEU C  1 38  ? -32.131 49.752  9.761   1.00 22.48 ? 38  LEU A C     1 
ATOM   6376  O O     . LEU C  1 38  ? -30.905 49.785  9.897   1.00 27.49 ? 38  LEU A O     1 
ATOM   6377  C CB    . LEU C  1 38  ? -33.297 51.687  10.877  1.00 27.12 ? 38  LEU A CB    1 
ATOM   6378  C CG    . LEU C  1 38  ? -32.145 52.288  11.681  1.00 32.72 ? 38  LEU A CG    1 
ATOM   6379  C CD1   . LEU C  1 38  ? -31.243 53.137  10.797  1.00 32.26 ? 38  LEU A CD1   1 
ATOM   6380  C CD2   . LEU C  1 38  ? -32.686 53.105  12.833  1.00 30.53 ? 38  LEU A CD2   1 
ATOM   6381  N N     . TRP C  1 39  ? -32.813 48.602  9.720   1.00 22.70 ? 39  TRP A N     1 
ATOM   6382  C CA    . TRP C  1 39  ? -32.182 47.295  9.944   1.00 28.55 ? 39  TRP A CA    1 
ATOM   6383  C C     . TRP C  1 39  ? -31.147 46.908  8.852   1.00 29.34 ? 39  TRP A C     1 
ATOM   6384  O O     . TRP C  1 39  ? -30.529 45.849  8.974   1.00 29.59 ? 39  TRP A O     1 
ATOM   6385  C CB    . TRP C  1 39  ? -33.265 46.190  10.067  1.00 28.96 ? 39  TRP A CB    1 
ATOM   6386  C CG    . TRP C  1 39  ? -34.099 46.163  11.396  1.00 28.73 ? 39  TRP A CG    1 
ATOM   6387  C CD1   . TRP C  1 39  ? -35.285 46.793  11.616  1.00 26.17 ? 39  TRP A CD1   1 
ATOM   6388  C CD2   . TRP C  1 39  ? -33.805 45.441  12.621  1.00 25.61 ? 39  TRP A CD2   1 
ATOM   6389  N NE1   . TRP C  1 39  ? -35.745 46.520  12.888  1.00 26.03 ? 39  TRP A NE1   1 
ATOM   6390  C CE2   . TRP C  1 39  ? -34.855 45.700  13.523  1.00 25.37 ? 39  TRP A CE2   1 
ATOM   6391  C CE3   . TRP C  1 39  ? -32.762 44.609  13.035  1.00 24.77 ? 39  TRP A CE3   1 
ATOM   6392  C CZ2   . TRP C  1 39  ? -34.879 45.178  14.834  1.00 26.08 ? 39  TRP A CZ2   1 
ATOM   6393  C CZ3   . TRP C  1 39  ? -32.795 44.083  14.350  1.00 24.71 ? 39  TRP A CZ3   1 
ATOM   6394  C CH2   . TRP C  1 39  ? -33.849 44.366  15.221  1.00 19.77 ? 39  TRP A CH2   1 
ATOM   6395  N N     . HIS C  1 40  ? -30.958 47.693  7.789   1.00 27.80 ? 40  HIS A N     1 
ATOM   6396  C CA    . HIS C  1 40  ? -29.846 47.440  6.870   1.00 33.45 ? 40  HIS A CA    1 
ATOM   6397  C C     . HIS C  1 40  ? -28.546 48.028  7.392   1.00 35.48 ? 40  HIS A C     1 
ATOM   6398  O O     . HIS C  1 40  ? -27.472 47.684  6.885   1.00 37.68 ? 40  HIS A O     1 
ATOM   6399  C CB    . HIS C  1 40  ? -30.112 48.045  5.477   1.00 28.36 ? 40  HIS A CB    1 
ATOM   6400  C CG    . HIS C  1 40  ? -31.022 47.237  4.606   1.00 27.96 ? 40  HIS A CG    1 
ATOM   6401  N ND1   . HIS C  1 40  ? -30.719 45.961  4.180   1.00 34.63 ? 40  HIS A ND1   1 
ATOM   6402  C CD2   . HIS C  1 40  ? -32.231 47.532  4.075   1.00 26.30 ? 40  HIS A CD2   1 
ATOM   6403  C CE1   . HIS C  1 40  ? -31.706 45.504  3.428   1.00 30.27 ? 40  HIS A CE1   1 
ATOM   6404  N NE2   . HIS C  1 40  ? -32.635 46.438  3.349   1.00 28.96 ? 40  HIS A NE2   1 
ATOM   6405  N N     . ALA C  1 41  ? -28.624 48.900  8.388   1.00 28.76 ? 41  ALA A N     1 
ATOM   6406  C CA    . ALA C  1 41  ? -27.526 49.811  8.644   1.00 29.61 ? 41  ALA A CA    1 
ATOM   6407  C C     . ALA C  1 41  ? -26.332 49.072  9.235   1.00 36.01 ? 41  ALA A C     1 
ATOM   6408  O O     . ALA C  1 41  ? -26.492 48.190  10.082  1.00 34.78 ? 41  ALA A O     1 
ATOM   6409  C CB    . ALA C  1 41  ? -27.999 50.917  9.576   1.00 24.62 ? 41  ALA A CB    1 
ATOM   6410  N N     . GLU C  1 42  ? -25.133 49.406  8.750   1.00 37.09 ? 42  GLU A N     1 
ATOM   6411  C CA    . GLU C  1 42  ? -23.881 49.062  9.413   1.00 33.92 ? 42  GLU A CA    1 
ATOM   6412  C C     . GLU C  1 42  ? -23.300 50.307  10.052  1.00 34.50 ? 42  GLU A C     1 
ATOM   6413  O O     . GLU C  1 42  ? -23.754 51.424  9.791   1.00 34.05 ? 42  GLU A O     1 
ATOM   6414  C CB    . GLU C  1 42  ? -22.833 48.510  8.451   1.00 34.00 ? 42  GLU A CB    1 
ATOM   6415  C CG    . GLU C  1 42  ? -23.237 47.386  7.560   1.00 40.54 ? 42  GLU A CG    1 
ATOM   6416  C CD    . GLU C  1 42  ? -22.310 47.324  6.339   1.00 61.29 ? 42  GLU A CD    1 
ATOM   6417  O OE1   . GLU C  1 42  ? -22.769 47.648  5.209   1.00 47.97 ? 42  GLU A OE1   1 
ATOM   6418  O OE2   . GLU C  1 42  ? -21.110 46.976  6.528   1.00 63.18 ? 42  GLU A OE2   1 
ATOM   6419  N N     . ASP C  1 43  ? -22.253 50.100  10.857  1.00 39.50 ? 43  ASP A N     1 
ATOM   6420  C CA    . ASP C  1 43  ? -21.526 51.212  11.462  1.00 36.11 ? 43  ASP A CA    1 
ATOM   6421  C C     . ASP C  1 43  ? -21.213 52.248  10.409  1.00 37.58 ? 43  ASP A C     1 
ATOM   6422  O O     . ASP C  1 43  ? -20.546 51.953  9.410   1.00 37.76 ? 43  ASP A O     1 
ATOM   6423  C CB    . ASP C  1 43  ? -20.230 50.731  12.112  1.00 36.36 ? 43  ASP A CB    1 
ATOM   6424  C CG    . ASP C  1 43  ? -20.434 50.280  13.522  1.00 46.43 ? 43  ASP A CG    1 
ATOM   6425  O OD1   . ASP C  1 43  ? -21.607 50.034  13.881  1.00 44.72 ? 43  ASP A OD1   1 
ATOM   6426  O OD2   . ASP C  1 43  ? -19.433 50.162  14.264  1.00 51.81 ? 43  ASP A OD2   1 
ATOM   6427  N N     . GLY C  1 44  ? -21.737 53.452  10.607  1.00 40.49 ? 44  GLY A N     1 
ATOM   6428  C CA    . GLY C  1 44  ? -21.504 54.549  9.704   1.00 35.52 ? 44  GLY A CA    1 
ATOM   6429  C C     . GLY C  1 44  ? -22.672 54.891  8.816   1.00 32.05 ? 44  GLY A C     1 
ATOM   6430  O O     . GLY C  1 44  ? -22.775 56.038  8.390   1.00 33.68 ? 44  GLY A O     1 
ATOM   6431  N N     . ASP C  1 45  ? -23.572 53.945  8.549   1.00 35.69 ? 45  ASP A N     1 
ATOM   6432  C CA    . ASP C  1 45  ? -24.577 54.143  7.511   1.00 37.31 ? 45  ASP A CA    1 
ATOM   6433  C C     . ASP C  1 45  ? -25.464 55.349  7.802   1.00 38.85 ? 45  ASP A C     1 
ATOM   6434  O O     . ASP C  1 45  ? -25.665 55.745  8.956   1.00 40.16 ? 45  ASP A O     1 
ATOM   6435  C CB    . ASP C  1 45  ? -25.435 52.896  7.379   1.00 33.45 ? 45  ASP A CB    1 
ATOM   6436  C CG    . ASP C  1 45  ? -24.713 51.800  6.704   1.00 30.15 ? 45  ASP A CG    1 
ATOM   6437  O OD1   . ASP C  1 45  ? -23.686 52.111  6.086   1.00 33.71 ? 45  ASP A OD1   1 
ATOM   6438  O OD2   . ASP C  1 45  ? -25.152 50.638  6.793   1.00 34.10 ? 45  ASP A OD2   1 
ATOM   6439  N N     . VAL C  1 46  ? -26.004 55.930  6.734   1.00 38.50 ? 46  VAL A N     1 
ATOM   6440  C CA    . VAL C  1 46  ? -26.966 57.021  6.828   1.00 31.99 ? 46  VAL A CA    1 
ATOM   6441  C C     . VAL C  1 46  ? -28.271 56.536  6.249   1.00 33.44 ? 46  VAL A C     1 
ATOM   6442  O O     . VAL C  1 46  ? -28.309 56.148  5.072   1.00 30.71 ? 46  VAL A O     1 
ATOM   6443  C CB    . VAL C  1 46  ? -26.494 58.268  6.081   1.00 28.76 ? 46  VAL A CB    1 
ATOM   6444  C CG1   . VAL C  1 46  ? -27.590 59.315  6.095   1.00 23.27 ? 46  VAL A CG1   1 
ATOM   6445  C CG2   . VAL C  1 46  ? -25.226 58.771  6.736   1.00 36.76 ? 46  VAL A CG2   1 
ATOM   6446  N N     . LEU C  1 47  ? -29.335 56.562  7.068   1.00 26.33 ? 47  LEU A N     1 
ATOM   6447  C CA    . LEU C  1 47  ? -30.691 56.267  6.624   1.00 28.92 ? 47  LEU A CA    1 
ATOM   6448  C C     . LEU C  1 47  ? -31.445 57.563  6.345   1.00 33.67 ? 47  LEU A C     1 
ATOM   6449  O O     . LEU C  1 47  ? -31.485 58.461  7.198   1.00 30.24 ? 47  LEU A O     1 
ATOM   6450  C CB    . LEU C  1 47  ? -31.454 55.432  7.653   1.00 28.32 ? 47  LEU A CB    1 
ATOM   6451  C CG    . LEU C  1 47  ? -32.904 55.090  7.244   1.00 28.88 ? 47  LEU A CG    1 
ATOM   6452  C CD1   . LEU C  1 47  ? -33.001 54.331  5.914   1.00 29.08 ? 47  LEU A CD1   1 
ATOM   6453  C CD2   . LEU C  1 47  ? -33.614 54.307  8.323   1.00 34.05 ? 47  LEU A CD2   1 
ATOM   6454  N N     . VAL C  1 48  ? -32.055 57.646  5.161   1.00 32.44 ? 48  VAL A N     1 
ATOM   6455  C CA    . VAL C  1 48  ? -32.789 58.827  4.712   1.00 33.76 ? 48  VAL A CA    1 
ATOM   6456  C C     . VAL C  1 48  ? -34.269 58.458  4.675   1.00 33.17 ? 48  VAL A C     1 
ATOM   6457  O O     . VAL C  1 48  ? -34.737 57.830  3.720   1.00 33.76 ? 48  VAL A O     1 
ATOM   6458  C CB    . VAL C  1 48  ? -32.308 59.313  3.340   1.00 38.35 ? 48  VAL A CB    1 
ATOM   6459  C CG1   . VAL C  1 48  ? -33.180 60.489  2.846   1.00 36.27 ? 48  VAL A CG1   1 
ATOM   6460  C CG2   . VAL C  1 48  ? -30.830 59.686  3.389   1.00 31.56 ? 48  VAL A CG2   1 
ATOM   6461  N N     . ILE C  1 49  ? -35.009 58.886  5.696   1.00 33.89 ? 49  ILE A N     1 
ATOM   6462  C CA    . ILE C  1 49  ? -36.444 58.637  5.819   1.00 35.19 ? 49  ILE A CA    1 
ATOM   6463  C C     . ILE C  1 49  ? -37.259 59.912  5.629   1.00 36.56 ? 49  ILE A C     1 
ATOM   6464  O O     . ILE C  1 49  ? -36.907 60.977  6.159   1.00 38.09 ? 49  ILE A O     1 
ATOM   6465  C CB    . ILE C  1 49  ? -36.800 58.018  7.182   1.00 30.00 ? 49  ILE A CB    1 
ATOM   6466  C CG1   . ILE C  1 49  ? -36.640 59.038  8.302   1.00 40.08 ? 49  ILE A CG1   1 
ATOM   6467  C CG2   . ILE C  1 49  ? -35.949 56.826  7.488   1.00 31.01 ? 49  ILE A CG2   1 
ATOM   6468  C CD1   . ILE C  1 49  ? -37.694 58.909  9.410   1.00 40.87 ? 49  ILE A CD1   1 
ATOM   6469  N N     . PRO C  1 50  ? -38.382 59.840  4.918   1.00 33.21 ? 50  PRO A N     1 
ATOM   6470  C CA    . PRO C  1 50  ? -39.427 60.858  5.092   1.00 37.63 ? 50  PRO A CA    1 
ATOM   6471  C C     . PRO C  1 50  ? -40.043 60.623  6.463   1.00 41.77 ? 50  PRO A C     1 
ATOM   6472  O O     . PRO C  1 50  ? -39.357 60.064  7.313   1.00 48.88 ? 50  PRO A O     1 
ATOM   6473  C CB    . PRO C  1 50  ? -40.396 60.557  3.949   1.00 35.42 ? 50  PRO A CB    1 
ATOM   6474  C CG    . PRO C  1 50  ? -40.261 59.055  3.798   1.00 35.91 ? 50  PRO A CG    1 
ATOM   6475  C CD    . PRO C  1 50  ? -38.827 58.725  4.059   1.00 30.24 ? 50  PRO A CD    1 
ATOM   6476  N N     . ASP C  1 51  ? -41.300 60.981  6.699   1.00 38.35 ? 51  ASP A N     1 
ATOM   6477  C CA    . ASP C  1 51  ? -41.998 60.638  7.949   1.00 41.71 ? 51  ASP A CA    1 
ATOM   6478  C C     . ASP C  1 51  ? -41.069 60.634  9.178   1.00 39.33 ? 51  ASP A C     1 
ATOM   6479  O O     . ASP C  1 51  ? -40.218 61.519  9.286   1.00 40.50 ? 51  ASP A O     1 
ATOM   6480  C CB    . ASP C  1 51  ? -42.792 59.317  7.767   1.00 40.70 ? 51  ASP A CB    1 
ATOM   6481  C CG    . ASP C  1 51  ? -41.924 58.088  7.432   1.00 39.06 ? 51  ASP A CG    1 
ATOM   6482  O OD1   . ASP C  1 51  ? -40.808 57.958  7.967   1.00 42.81 ? 51  ASP A OD1   1 
ATOM   6483  O OD2   . ASP C  1 51  ? -42.409 57.204  6.676   1.00 31.02 ? 51  ASP A OD2   1 
ATOM   6484  N N     . THR C  1 52  ? -41.205 59.701  10.126  1.00 37.30 ? 52  THR A N     1 
ATOM   6485  C CA    . THR C  1 52  ? -40.462 59.847  11.382  1.00 43.31 ? 52  THR A CA    1 
ATOM   6486  C C     . THR C  1 52  ? -39.977 58.505  11.915  1.00 41.07 ? 52  THR A C     1 
ATOM   6487  O O     . THR C  1 52  ? -40.162 57.446  11.305  1.00 43.48 ? 52  THR A O     1 
ATOM   6488  C CB    . THR C  1 52  ? -41.309 60.546  12.447  1.00 48.71 ? 52  THR A CB    1 
ATOM   6489  O OG1   . THR C  1 52  ? -42.448 61.153  11.816  1.00 50.79 ? 52  THR A OG1   1 
ATOM   6490  C CG2   . THR C  1 52  ? -40.467 61.604  13.217  1.00 39.56 ? 52  THR A CG2   1 
ATOM   6491  N N     . VAL C  1 53  ? -39.329 58.560  13.072  1.00 36.65 ? 53  VAL A N     1 
ATOM   6492  C CA    . VAL C  1 53  ? -38.886 57.354  13.758  1.00 40.00 ? 53  VAL A CA    1 
ATOM   6493  C C     . VAL C  1 53  ? -39.145 57.541  15.241  1.00 36.58 ? 53  VAL A C     1 
ATOM   6494  O O     . VAL C  1 53  ? -38.891 58.614  15.795  1.00 38.58 ? 53  VAL A O     1 
ATOM   6495  C CB    . VAL C  1 53  ? -37.400 57.041  13.486  1.00 39.22 ? 53  VAL A CB    1 
ATOM   6496  C CG1   . VAL C  1 53  ? -36.492 58.020  14.209  1.00 37.14 ? 53  VAL A CG1   1 
ATOM   6497  C CG2   . VAL C  1 53  ? -37.082 55.650  13.908  1.00 35.91 ? 53  VAL A CG2   1 
ATOM   6498  N N     . ASP C  1 54  ? -39.686 56.511  15.867  1.00 35.51 ? 54  ASP A N     1 
ATOM   6499  C CA    . ASP C  1 54  ? -39.857 56.498  17.307  1.00 36.14 ? 54  ASP A CA    1 
ATOM   6500  C C     . ASP C  1 54  ? -38.537 56.858  17.981  1.00 44.44 ? 54  ASP A C     1 
ATOM   6501  O O     . ASP C  1 54  ? -37.544 56.131  17.804  1.00 41.01 ? 54  ASP A O     1 
ATOM   6502  C CB    . ASP C  1 54  ? -40.326 55.122  17.764  1.00 39.84 ? 54  ASP A CB    1 
ATOM   6503  C CG    . ASP C  1 54  ? -40.922 55.148  19.153  1.00 45.67 ? 54  ASP A CG    1 
ATOM   6504  O OD1   . ASP C  1 54  ? -40.141 55.402  20.113  1.00 47.23 ? 54  ASP A OD1   1 
ATOM   6505  O OD2   . ASP C  1 54  ? -42.152 54.929  19.280  1.00 40.79 ? 54  ASP A OD2   1 
ATOM   6506  N N     . PRO C  1 55  ? -38.487 57.950  18.778  1.00 46.38 ? 55  PRO A N     1 
ATOM   6507  C CA    . PRO C  1 55  ? -37.216 58.427  19.357  1.00 44.03 ? 55  PRO A CA    1 
ATOM   6508  C C     . PRO C  1 55  ? -36.279 57.327  19.831  1.00 40.63 ? 55  PRO A C     1 
ATOM   6509  O O     . PRO C  1 55  ? -35.056 57.494  19.818  1.00 41.24 ? 55  PRO A O     1 
ATOM   6510  C CB    . PRO C  1 55  ? -37.684 59.288  20.536  1.00 41.16 ? 55  PRO A CB    1 
ATOM   6511  C CG    . PRO C  1 55  ? -39.008 59.827  20.079  1.00 43.68 ? 55  PRO A CG    1 
ATOM   6512  C CD    . PRO C  1 55  ? -39.646 58.706  19.282  1.00 36.24 ? 55  PRO A CD    1 
ATOM   6513  N N     . ASP C  1 56  ? -36.852 56.192  20.225  1.00 40.50 ? 56  ASP A N     1 
ATOM   6514  C CA    . ASP C  1 56  ? -36.106 55.065  20.769  1.00 39.56 ? 56  ASP A CA    1 
ATOM   6515  C C     . ASP C  1 56  ? -35.741 54.013  19.735  1.00 38.57 ? 56  ASP A C     1 
ATOM   6516  O O     . ASP C  1 56  ? -34.839 53.204  19.982  1.00 32.76 ? 56  ASP A O     1 
ATOM   6517  C CB    . ASP C  1 56  ? -36.938 54.400  21.858  1.00 40.97 ? 56  ASP A CB    1 
ATOM   6518  C CG    . ASP C  1 56  ? -37.411 55.388  22.896  1.00 44.57 ? 56  ASP A CG    1 
ATOM   6519  O OD1   . ASP C  1 56  ? -38.499 56.001  22.693  1.00 45.64 ? 56  ASP A OD1   1 
ATOM   6520  O OD2   . ASP C  1 56  ? -36.679 55.545  23.903  1.00 36.60 ? 56  ASP A OD2   1 
ATOM   6521  N N     . PHE C  1 57  ? -36.440 53.982  18.614  1.00 36.63 ? 57  PHE A N     1 
ATOM   6522  C CA    . PHE C  1 57  ? -36.159 52.983  17.591  1.00 33.75 ? 57  PHE A CA    1 
ATOM   6523  C C     . PHE C  1 57  ? -34.692 52.844  17.234  1.00 29.66 ? 57  PHE A C     1 
ATOM   6524  O O     . PHE C  1 57  ? -34.201 51.709  17.217  1.00 29.28 ? 57  PHE A O     1 
ATOM   6525  C CB    . PHE C  1 57  ? -36.971 53.331  16.345  1.00 35.05 ? 57  PHE A CB    1 
ATOM   6526  C CG    . PHE C  1 57  ? -37.004 52.256  15.354  1.00 33.04 ? 57  PHE A CG    1 
ATOM   6527  C CD1   . PHE C  1 57  ? -37.710 51.096  15.610  1.00 34.36 ? 57  PHE A CD1   1 
ATOM   6528  C CD2   . PHE C  1 57  ? -36.334 52.390  14.149  1.00 38.32 ? 57  PHE A CD2   1 
ATOM   6529  C CE1   . PHE C  1 57  ? -37.759 50.072  14.662  1.00 35.47 ? 57  PHE A CE1   1 
ATOM   6530  C CE2   . PHE C  1 57  ? -36.381 51.388  13.188  1.00 36.83 ? 57  PHE A CE2   1 
ATOM   6531  C CZ    . PHE C  1 57  ? -37.086 50.226  13.438  1.00 37.07 ? 57  PHE A CZ    1 
ATOM   6532  N N     . PRO C  1 58  ? -33.946 53.909  16.928  1.00 30.33 ? 58  PRO A N     1 
ATOM   6533  C CA    . PRO C  1 58  ? -32.580 53.712  16.422  1.00 29.41 ? 58  PRO A CA    1 
ATOM   6534  C C     . PRO C  1 58  ? -31.754 52.839  17.335  1.00 32.67 ? 58  PRO A C     1 
ATOM   6535  O O     . PRO C  1 58  ? -31.441 51.694  16.990  1.00 35.21 ? 58  PRO A O     1 
ATOM   6536  C CB    . PRO C  1 58  ? -32.017 55.135  16.357  1.00 31.79 ? 58  PRO A CB    1 
ATOM   6537  C CG    . PRO C  1 58  ? -33.223 55.967  16.128  1.00 34.38 ? 58  PRO A CG    1 
ATOM   6538  C CD    . PRO C  1 58  ? -34.299 55.336  16.973  1.00 32.39 ? 58  PRO A CD    1 
ATOM   6539  N N     . GLY C  1 59  ? -31.437 53.365  18.518  1.00 36.45 ? 59  GLY A N     1 
ATOM   6540  C CA    . GLY C  1 59  ? -30.676 52.595  19.476  1.00 25.01 ? 59  GLY A CA    1 
ATOM   6541  C C     . GLY C  1 59  ? -31.234 51.206  19.656  1.00 29.11 ? 59  GLY A C     1 
ATOM   6542  O O     . GLY C  1 59  ? -30.480 50.242  19.802  1.00 36.41 ? 59  GLY A O     1 
ATOM   6543  N N     . TYR C  1 60  ? -32.556 51.080  19.615  1.00 29.31 ? 60  TYR A N     1 
ATOM   6544  C CA    . TYR C  1 60  ? -33.190 49.777  19.754  1.00 27.69 ? 60  TYR A CA    1 
ATOM   6545  C C     . TYR C  1 60  ? -32.688 48.816  18.688  1.00 33.08 ? 60  TYR A C     1 
ATOM   6546  O O     . TYR C  1 60  ? -32.233 47.700  18.985  1.00 31.20 ? 60  TYR A O     1 
ATOM   6547  C CB    . TYR C  1 60  ? -34.698 49.933  19.652  1.00 24.53 ? 60  TYR A CB    1 
ATOM   6548  C CG    . TYR C  1 60  ? -35.366 48.642  19.317  1.00 28.18 ? 60  TYR A CG    1 
ATOM   6549  C CD1   . TYR C  1 60  ? -35.469 47.638  20.266  1.00 26.86 ? 60  TYR A CD1   1 
ATOM   6550  C CD2   . TYR C  1 60  ? -35.869 48.406  18.057  1.00 22.75 ? 60  TYR A CD2   1 
ATOM   6551  C CE1   . TYR C  1 60  ? -36.077 46.449  19.972  1.00 29.22 ? 60  TYR A CE1   1 
ATOM   6552  C CE2   . TYR C  1 60  ? -36.473 47.217  17.752  1.00 21.36 ? 60  TYR A CE2   1 
ATOM   6553  C CZ    . TYR C  1 60  ? -36.585 46.237  18.705  1.00 26.91 ? 60  TYR A CZ    1 
ATOM   6554  O OH    . TYR C  1 60  ? -37.208 45.036  18.412  1.00 21.88 ? 60  TYR A OH    1 
ATOM   6555  N N     . VAL C  1 61  ? -32.784 49.233  17.430  1.00 28.74 ? 61  VAL A N     1 
ATOM   6556  C CA    . VAL C  1 61  ? -32.196 48.456  16.357  1.00 30.21 ? 61  VAL A CA    1 
ATOM   6557  C C     . VAL C  1 61  ? -30.714 48.245  16.621  1.00 30.61 ? 61  VAL A C     1 
ATOM   6558  O O     . VAL C  1 61  ? -30.183 47.147  16.418  1.00 31.73 ? 61  VAL A O     1 
ATOM   6559  C CB    . VAL C  1 61  ? -32.463 49.150  15.008  1.00 32.68 ? 61  VAL A CB    1 
ATOM   6560  C CG1   . VAL C  1 61  ? -32.009 48.268  13.854  1.00 30.00 ? 61  VAL A CG1   1 
ATOM   6561  C CG2   . VAL C  1 61  ? -33.973 49.487  14.868  1.00 27.11 ? 61  VAL A CG2   1 
ATOM   6562  N N     . ALA C  1 62  ? -30.038 49.272  17.143  1.00 32.92 ? 62  ALA A N     1 
ATOM   6563  C CA    . ALA C  1 62  ? -28.591 49.189  17.348  1.00 40.16 ? 62  ALA A CA    1 
ATOM   6564  C C     . ALA C  1 62  ? -28.213 48.080  18.333  1.00 39.86 ? 62  ALA A C     1 
ATOM   6565  O O     . ALA C  1 62  ? -27.331 47.257  18.046  1.00 38.02 ? 62  ALA A O     1 
ATOM   6566  C CB    . ALA C  1 62  ? -28.049 50.536  17.829  1.00 39.54 ? 62  ALA A CB    1 
ATOM   6567  N N     . ASP C  1 63  ? -28.857 48.055  19.509  1.00 39.13 ? 63  ASP A N     1 
ATOM   6568  C CA    . ASP C  1 63  ? -28.509 47.078  20.542  1.00 37.95 ? 63  ASP A CA    1 
ATOM   6569  C C     . ASP C  1 63  ? -28.685 45.658  20.032  1.00 39.48 ? 63  ASP A C     1 
ATOM   6570  O O     . ASP C  1 63  ? -27.784 44.821  20.157  1.00 45.21 ? 63  ASP A O     1 
ATOM   6571  C CB    . ASP C  1 63  ? -29.366 47.310  21.783  1.00 31.40 ? 63  ASP A CB    1 
ATOM   6572  C CG    . ASP C  1 63  ? -29.034 48.605  22.461  1.00 41.39 ? 63  ASP A CG    1 
ATOM   6573  O OD1   . ASP C  1 63  ? -27.923 49.106  22.196  1.00 38.81 ? 63  ASP A OD1   1 
ATOM   6574  O OD2   . ASP C  1 63  ? -29.867 49.135  23.239  1.00 50.53 ? 63  ASP A OD2   1 
ATOM   6575  N N     . THR C  1 64  ? -29.850 45.384  19.444  1.00 38.76 ? 64  THR A N     1 
ATOM   6576  C CA    . THR C  1 64  ? -30.182 44.069  18.902  1.00 41.92 ? 64  THR A CA    1 
ATOM   6577  C C     . THR C  1 64  ? -29.171 43.614  17.859  1.00 39.42 ? 64  THR A C     1 
ATOM   6578  O O     . THR C  1 64  ? -28.710 42.467  17.878  1.00 40.40 ? 64  THR A O     1 
ATOM   6579  C CB    . THR C  1 64  ? -31.567 44.142  18.276  1.00 39.23 ? 64  THR A CB    1 
ATOM   6580  O OG1   . THR C  1 64  ? -31.541 45.213  17.324  1.00 42.74 ? 64  THR A OG1   1 
ATOM   6581  C CG2   . THR C  1 64  ? -32.623 44.449  19.340  1.00 31.20 ? 64  THR A CG2   1 
ATOM   6582  N N     . LEU C  1 65  ? -28.839 44.487  16.919  1.00 38.89 ? 65  LEU A N     1 
ATOM   6583  C CA    . LEU C  1 65  ? -27.906 44.097  15.874  1.00 37.21 ? 65  LEU A CA    1 
ATOM   6584  C C     . LEU C  1 65  ? -26.462 44.044  16.357  1.00 43.53 ? 65  LEU A C     1 
ATOM   6585  O O     . LEU C  1 65  ? -25.638 43.384  15.711  1.00 42.82 ? 65  LEU A O     1 
ATOM   6586  C CB    . LEU C  1 65  ? -28.016 45.061  14.698  1.00 32.52 ? 65  LEU A CB    1 
ATOM   6587  C CG    . LEU C  1 65  ? -29.269 44.873  13.842  1.00 36.37 ? 65  LEU A CG    1 
ATOM   6588  C CD1   . LEU C  1 65  ? -29.427 46.027  12.861  1.00 33.64 ? 65  LEU A CD1   1 
ATOM   6589  C CD2   . LEU C  1 65  ? -29.291 43.504  13.106  1.00 32.01 ? 65  LEU A CD2   1 
ATOM   6590  N N     . GLY C  1 66  ? -26.137 44.720  17.464  1.00 43.70 ? 66  GLY A N     1 
ATOM   6591  C CA    . GLY C  1 66  ? -24.769 44.775  17.949  1.00 40.79 ? 66  GLY A CA    1 
ATOM   6592  C C     . GLY C  1 66  ? -23.919 45.859  17.333  1.00 36.03 ? 66  GLY A C     1 
ATOM   6593  O O     . GLY C  1 66  ? -22.697 45.706  17.247  1.00 42.60 ? 66  GLY A O     1 
ATOM   6594  N N     . ILE C  1 67  ? -24.512 46.955  16.916  1.00 38.86 ? 67  ILE A N     1 
ATOM   6595  C CA    . ILE C  1 67  ? -23.792 47.973  16.167  1.00 40.44 ? 67  ILE A CA    1 
ATOM   6596  C C     . ILE C  1 67  ? -23.662 49.225  17.028  1.00 40.25 ? 67  ILE A C     1 
ATOM   6597  O O     . ILE C  1 67  ? -24.505 49.507  17.891  1.00 42.01 ? 67  ILE A O     1 
ATOM   6598  C CB    . ILE C  1 67  ? -24.526 48.239  14.830  1.00 45.31 ? 67  ILE A CB    1 
ATOM   6599  C CG1   . ILE C  1 67  ? -23.877 47.465  13.675  1.00 39.30 ? 67  ILE A CG1   1 
ATOM   6600  C CG2   . ILE C  1 67  ? -24.651 49.722  14.526  1.00 45.69 ? 67  ILE A CG2   1 
ATOM   6601  C CD1   . ILE C  1 67  ? -23.874 45.962  13.843  1.00 43.57 ? 67  ILE A CD1   1 
ATOM   6602  N N     . ASP C  1 68  ? -22.574 49.960  16.814  1.00 40.47 ? 68  ASP A N     1 
ATOM   6603  C CA    . ASP C  1 68  ? -22.367 51.248  17.471  1.00 41.23 ? 68  ASP A CA    1 
ATOM   6604  C C     . ASP C  1 68  ? -23.433 52.221  16.972  1.00 45.36 ? 68  ASP A C     1 
ATOM   6605  O O     . ASP C  1 68  ? -23.304 52.804  15.897  1.00 44.52 ? 68  ASP A O     1 
ATOM   6606  C CB    . ASP C  1 68  ? -20.958 51.772  17.195  1.00 38.94 ? 68  ASP A CB    1 
ATOM   6607  C CG    . ASP C  1 68  ? -20.736 53.189  17.744  1.00 45.39 ? 68  ASP A CG    1 
ATOM   6608  O OD1   . ASP C  1 68  ? -21.387 53.558  18.747  1.00 44.96 ? 68  ASP A OD1   1 
ATOM   6609  O OD2   . ASP C  1 68  ? -19.905 53.945  17.184  1.00 44.02 ? 68  ASP A OD2   1 
ATOM   6610  N N     . GLY C  1 69  ? -24.498 52.397  17.757  1.00 43.63 ? 69  GLY A N     1 
ATOM   6611  C CA    . GLY C  1 69  ? -25.559 53.310  17.393  1.00 39.87 ? 69  GLY A CA    1 
ATOM   6612  C C     . GLY C  1 69  ? -25.100 54.731  17.173  1.00 39.31 ? 69  GLY A C     1 
ATOM   6613  O O     . GLY C  1 69  ? -25.745 55.471  16.433  1.00 46.26 ? 69  GLY A O     1 
ATOM   6614  N N     . THR C  1 70  ? -24.004 55.139  17.796  1.00 38.82 ? 70  THR A N     1 
ATOM   6615  C CA    . THR C  1 70  ? -23.510 56.487  17.559  1.00 44.48 ? 70  THR A CA    1 
ATOM   6616  C C     . THR C  1 70  ? -23.071 56.656  16.116  1.00 47.75 ? 70  THR A C     1 
ATOM   6617  O O     . THR C  1 70  ? -23.263 57.726  15.525  1.00 49.10 ? 70  THR A O     1 
ATOM   6618  C CB    . THR C  1 70  ? -22.351 56.795  18.496  1.00 43.21 ? 70  THR A CB    1 
ATOM   6619  O OG1   . THR C  1 70  ? -21.228 55.975  18.137  1.00 44.66 ? 70  THR A OG1   1 
ATOM   6620  C CG2   . THR C  1 70  ? -22.765 56.526  19.926  1.00 42.15 ? 70  THR A CG2   1 
ATOM   6621  N N     . SER C  1 71  ? -22.472 55.611  15.534  1.00 43.08 ? 71  SER A N     1 
ATOM   6622  C CA    . SER C  1 71  ? -22.023 55.691  14.146  1.00 45.76 ? 71  SER A CA    1 
ATOM   6623  C C     . SER C  1 71  ? -23.183 55.896  13.182  1.00 46.67 ? 71  SER A C     1 
ATOM   6624  O O     . SER C  1 71  ? -23.027 56.583  12.163  1.00 44.47 ? 71  SER A O     1 
ATOM   6625  C CB    . SER C  1 71  ? -21.247 54.430  13.778  1.00 42.89 ? 71  SER A CB    1 
ATOM   6626  O OG    . SER C  1 71  ? -22.069 53.301  14.002  1.00 45.54 ? 71  SER A OG    1 
ATOM   6627  N N     . VAL C  1 72  ? -24.353 55.331  13.481  1.00 40.65 ? 72  VAL A N     1 
ATOM   6628  C CA    . VAL C  1 72  ? -25.471 55.364  12.541  1.00 43.69 ? 72  VAL A CA    1 
ATOM   6629  C C     . VAL C  1 72  ? -26.309 56.616  12.792  1.00 46.18 ? 72  VAL A C     1 
ATOM   6630  O O     . VAL C  1 72  ? -26.590 56.963  13.947  1.00 51.87 ? 72  VAL A O     1 
ATOM   6631  C CB    . VAL C  1 72  ? -26.308 54.076  12.649  1.00 40.15 ? 72  VAL A CB    1 
ATOM   6632  C CG1   . VAL C  1 72  ? -26.643 53.757  14.107  1.00 46.47 ? 72  VAL A CG1   1 
ATOM   6633  C CG2   . VAL C  1 72  ? -27.571 54.171  11.790  1.00 36.35 ? 72  VAL A CG2   1 
ATOM   6634  N N     . HIS C  1 73  ? -26.667 57.318  11.712  1.00 41.34 ? 73  HIS A N     1 
ATOM   6635  C CA    . HIS C  1 73  ? -27.472 58.536  11.763  1.00 42.03 ? 73  HIS A CA    1 
ATOM   6636  C C     . HIS C  1 73  ? -28.695 58.372  10.870  1.00 41.30 ? 73  HIS A C     1 
ATOM   6637  O O     . HIS C  1 73  ? -28.688 57.592  9.911   1.00 37.04 ? 73  HIS A O     1 
ATOM   6638  C CB    . HIS C  1 73  ? -26.680 59.782  11.292  1.00 45.90 ? 73  HIS A CB    1 
ATOM   6639  C CG    . HIS C  1 73  ? -25.465 60.089  12.120  1.00 55.09 ? 73  HIS A CG    1 
ATOM   6640  N ND1   . HIS C  1 73  ? -25.463 61.031  13.129  1.00 60.26 ? 73  HIS A ND1   1 
ATOM   6641  C CD2   . HIS C  1 73  ? -24.217 59.561  12.101  1.00 54.26 ? 73  HIS A CD2   1 
ATOM   6642  C CE1   . HIS C  1 73  ? -24.266 61.073  13.690  1.00 55.05 ? 73  HIS A CE1   1 
ATOM   6643  N NE2   . HIS C  1 73  ? -23.491 60.192  13.083  1.00 57.27 ? 73  HIS A NE2   1 
ATOM   6644  N N     . VAL C  1 74  ? -29.755 59.100  11.191  1.00 39.24 ? 74  VAL A N     1 
ATOM   6645  C CA    . VAL C  1 74  ? -30.942 59.131  10.353  1.00 33.20 ? 74  VAL A CA    1 
ATOM   6646  C C     . VAL C  1 74  ? -31.195 60.581  9.972   1.00 32.37 ? 74  VAL A C     1 
ATOM   6647  O O     . VAL C  1 74  ? -30.960 61.493  10.767  1.00 31.86 ? 74  VAL A O     1 
ATOM   6648  C CB    . VAL C  1 74  ? -32.173 58.484  11.032  1.00 36.05 ? 74  VAL A CB    1 
ATOM   6649  C CG1   . VAL C  1 74  ? -31.737 57.480  12.098  1.00 34.38 ? 74  VAL A CG1   1 
ATOM   6650  C CG2   . VAL C  1 74  ? -33.108 59.531  11.610  1.00 37.74 ? 74  VAL A CG2   1 
ATOM   6651  N N     . GLU C  1 75  ? -31.608 60.789  8.728   1.00 34.48 ? 75  GLU A N     1 
ATOM   6652  C CA    . GLU C  1 75  ? -31.667 62.111  8.110   1.00 39.10 ? 75  GLU A CA    1 
ATOM   6653  C C     . GLU C  1 75  ? -33.080 62.288  7.553   1.00 36.68 ? 75  GLU A C     1 
ATOM   6654  O O     . GLU C  1 75  ? -33.416 61.736  6.500   1.00 37.24 ? 75  GLU A O     1 
ATOM   6655  C CB    . GLU C  1 75  ? -30.591 62.236  7.020   1.00 41.72 ? 75  GLU A CB    1 
ATOM   6656  C CG    . GLU C  1 75  ? -30.025 63.643  6.826   1.00 40.04 ? 75  GLU A CG    1 
ATOM   6657  C CD    . GLU C  1 75  ? -29.552 64.290  8.118   1.00 43.70 ? 75  GLU A CD    1 
ATOM   6658  O OE1   . GLU C  1 75  ? -28.862 63.615  8.914   1.00 40.98 ? 75  GLU A OE1   1 
ATOM   6659  O OE2   . GLU C  1 75  ? -29.861 65.485  8.329   1.00 50.67 ? 75  GLU A OE2   1 
ATOM   6660  N N     . ARG C  1 76  ? -33.917 63.032  8.264   1.00 34.23 ? 76  ARG A N     1 
ATOM   6661  C CA    . ARG C  1 76  ? -35.326 63.161  7.913   1.00 39.33 ? 76  ARG A CA    1 
ATOM   6662  C C     . ARG C  1 76  ? -35.475 64.263  6.881   1.00 33.70 ? 76  ARG A C     1 
ATOM   6663  O O     . ARG C  1 76  ? -35.263 65.438  7.188   1.00 36.78 ? 76  ARG A O     1 
ATOM   6664  C CB    . ARG C  1 76  ? -36.158 63.471  9.154   1.00 39.88 ? 76  ARG A CB    1 
ATOM   6665  C CG    . ARG C  1 76  ? -35.933 62.524  10.315  1.00 41.58 ? 76  ARG A CG    1 
ATOM   6666  C CD    . ARG C  1 76  ? -35.053 63.180  11.403  1.00 51.22 ? 76  ARG A CD    1 
ATOM   6667  N NE    . ARG C  1 76  ? -34.629 62.270  12.465  1.00 45.49 ? 76  ARG A NE    1 
ATOM   6668  C CZ    . ARG C  1 76  ? -35.434 61.765  13.392  1.00 49.41 ? 76  ARG A CZ    1 
ATOM   6669  N NH1   . ARG C  1 76  ? -36.749 61.948  13.345  1.00 51.53 ? 76  ARG A NH1   1 
ATOM   6670  N NH2   . ARG C  1 76  ? -34.906 61.074  14.401  1.00 49.55 ? 76  ARG A NH2   1 
ATOM   6671  N N     . THR C  1 77  ? -35.820 63.887  5.656   1.00 38.10 ? 77  THR A N     1 
ATOM   6672  C CA    . THR C  1 77  ? -36.373 64.880  4.756   1.00 42.71 ? 77  THR A CA    1 
ATOM   6673  C C     . THR C  1 77  ? -37.787 65.198  5.231   1.00 47.03 ? 77  THR A C     1 
ATOM   6674  O O     . THR C  1 77  ? -38.298 64.594  6.175   1.00 49.19 ? 77  THR A O     1 
ATOM   6675  C CB    . THR C  1 77  ? -36.340 64.390  3.306   1.00 41.08 ? 77  THR A CB    1 
ATOM   6676  O OG1   . THR C  1 77  ? -37.480 63.569  3.034   1.00 42.61 ? 77  THR A OG1   1 
ATOM   6677  C CG2   . THR C  1 77  ? -35.066 63.606  3.008   1.00 42.14 ? 77  THR A CG2   1 
ATOM   6678  N N     . GLN C  1 78  ? -38.442 66.168  4.608   1.00 48.95 ? 78  GLN A N     1 
ATOM   6679  C CA    . GLN C  1 78  ? -39.787 66.494  5.054   1.00 50.11 ? 78  GLN A CA    1 
ATOM   6680  C C     . GLN C  1 78  ? -40.845 66.103  4.039   1.00 44.40 ? 78  GLN A C     1 
ATOM   6681  O O     . GLN C  1 78  ? -42.042 66.265  4.302   1.00 41.40 ? 78  GLN A O     1 
ATOM   6682  C CB    . GLN C  1 78  ? -39.876 67.984  5.400   1.00 58.34 ? 78  GLN A CB    1 
ATOM   6683  C CG    . GLN C  1 78  ? -38.880 68.430  6.485   1.00 54.66 ? 78  GLN A CG    1 
ATOM   6684  C CD    . GLN C  1 78  ? -39.229 67.940  7.884   1.00 53.21 ? 78  GLN A CD    1 
ATOM   6685  O OE1   . GLN C  1 78  ? -39.969 66.967  8.064   1.00 52.11 ? 78  GLN A OE1   1 
ATOM   6686  N NE2   . GLN C  1 78  ? -38.721 68.647  8.889   1.00 56.83 ? 78  GLN A NE2   1 
ATOM   6687  N N     . THR C  1 79  ? -40.437 65.582  2.895   1.00 49.50 ? 79  THR A N     1 
ATOM   6688  C CA    . THR C  1 79  ? -41.336 65.179  1.825   1.00 49.13 ? 79  THR A CA    1 
ATOM   6689  C C     . THR C  1 79  ? -40.981 63.768  1.394   1.00 42.40 ? 79  THR A C     1 
ATOM   6690  O O     . THR C  1 79  ? -40.026 63.168  1.901   1.00 37.44 ? 79  THR A O     1 
ATOM   6691  C CB    . THR C  1 79  ? -41.240 66.140  0.631   1.00 48.63 ? 79  THR A CB    1 
ATOM   6692  O OG1   . THR C  1 79  ? -40.204 65.703  -0.265  1.00 52.99 ? 79  THR A OG1   1 
ATOM   6693  C CG2   . THR C  1 79  ? -40.942 67.555  1.104   1.00 50.48 ? 79  THR A CG2   1 
ATOM   6694  N N     . PRO C  1 80  ? -41.756 63.190  0.478   1.00 39.24 ? 80  PRO A N     1 
ATOM   6695  C CA    . PRO C  1 80  ? -41.349 61.927  -0.137  1.00 37.87 ? 80  PRO A CA    1 
ATOM   6696  C C     . PRO C  1 80  ? -40.038 62.050  -0.913  1.00 38.24 ? 80  PRO A C     1 
ATOM   6697  O O     . PRO C  1 80  ? -39.595 63.139  -1.301  1.00 35.23 ? 80  PRO A O     1 
ATOM   6698  C CB    . PRO C  1 80  ? -42.532 61.608  -1.053  1.00 42.11 ? 80  PRO A CB    1 
ATOM   6699  C CG    . PRO C  1 80  ? -43.702 62.154  -0.283  1.00 41.55 ? 80  PRO A CG    1 
ATOM   6700  C CD    . PRO C  1 80  ? -43.190 63.460  0.257   1.00 41.54 ? 80  PRO A CD    1 
ATOM   6701  N N     . LEU C  1 81  ? -39.413 60.891  -1.140  1.00 30.58 ? 81  LEU A N     1 
ATOM   6702  C CA    . LEU C  1 81  ? -38.043 60.850  -1.625  1.00 27.83 ? 81  LEU A CA    1 
ATOM   6703  C C     . LEU C  1 81  ? -37.999 60.985  -3.128  1.00 28.22 ? 81  LEU A C     1 
ATOM   6704  O O     . LEU C  1 81  ? -37.231 60.288  -3.792  1.00 35.24 ? 81  LEU A O     1 
ATOM   6705  C CB    . LEU C  1 81  ? -37.344 59.554  -1.200  1.00 31.48 ? 81  LEU A CB    1 
ATOM   6706  C CG    . LEU C  1 81  ? -36.604 59.627  0.144   1.00 29.10 ? 81  LEU A CG    1 
ATOM   6707  C CD1   . LEU C  1 81  ? -35.760 58.373  0.400   1.00 26.92 ? 81  LEU A CD1   1 
ATOM   6708  C CD2   . LEU C  1 81  ? -35.750 60.906  0.233   1.00 28.04 ? 81  LEU A CD2   1 
ATOM   6709  N N     . SER C  1 82  ? -38.800 61.900  -3.658  1.00 32.24 ? 82  SER A N     1 
ATOM   6710  C CA    . SER C  1 82  ? -39.036 62.037  -5.086  1.00 26.28 ? 82  SER A CA    1 
ATOM   6711  C C     . SER C  1 82  ? -37.768 62.467  -5.801  1.00 29.99 ? 82  SER A C     1 
ATOM   6712  O O     . SER C  1 82  ? -36.817 62.955  -5.186  1.00 37.98 ? 82  SER A O     1 
ATOM   6713  C CB    . SER C  1 82  ? -40.053 63.121  -5.346  1.00 26.49 ? 82  SER A CB    1 
ATOM   6714  O OG    . SER C  1 82  ? -39.322 64.336  -5.371  1.00 27.00 ? 82  SER A OG    1 
ATOM   6715  N N     . GLU C  1 83  ? -37.804 62.378  -7.134  1.00 28.62 ? 83  GLU A N     1 
ATOM   6716  C CA    . GLU C  1 83  ? -36.657 62.783  -7.951  1.00 33.24 ? 83  GLU A CA    1 
ATOM   6717  C C     . GLU C  1 83  ? -36.255 64.224  -7.663  1.00 32.03 ? 83  GLU A C     1 
ATOM   6718  O O     . GLU C  1 83  ? -35.061 64.547  -7.625  1.00 33.02 ? 83  GLU A O     1 
ATOM   6719  C CB    . GLU C  1 83  ? -36.971 62.613  -9.449  1.00 33.36 ? 83  GLU A CB    1 
ATOM   6720  C CG    . GLU C  1 83  ? -37.197 61.143  -9.942  1.00 29.36 ? 83  GLU A CG    1 
ATOM   6721  C CD    . GLU C  1 83  ? -35.902 60.309  -9.973  1.00 33.81 ? 83  GLU A CD    1 
ATOM   6722  O OE1   . GLU C  1 83  ? -35.520 59.750  -8.903  1.00 37.36 ? 83  GLU A OE1   1 
ATOM   6723  O OE2   . GLU C  1 83  ? -35.266 60.216  -11.053 1.00 30.16 ? 83  GLU A OE2   1 
ATOM   6724  N N     . ALA C  1 84  ? -37.241 65.106  -7.464  1.00 27.76 ? 84  ALA A N     1 
ATOM   6725  C CA    . ALA C  1 84  ? -36.927 66.500  -7.188  1.00 27.84 ? 84  ALA A CA    1 
ATOM   6726  C C     . ALA C  1 84  ? -36.057 66.620  -5.948  1.00 29.80 ? 84  ALA A C     1 
ATOM   6727  O O     . ALA C  1 84  ? -35.052 67.344  -5.945  1.00 33.17 ? 84  ALA A O     1 
ATOM   6728  C CB    . ALA C  1 84  ? -38.216 67.304  -7.022  1.00 29.60 ? 84  ALA A CB    1 
ATOM   6729  N N     . VAL C  1 85  ? -36.429 65.904  -4.886  1.00 26.28 ? 85  VAL A N     1 
ATOM   6730  C CA    . VAL C  1 85  ? -35.617 65.905  -3.680  1.00 28.45 ? 85  VAL A CA    1 
ATOM   6731  C C     . VAL C  1 85  ? -34.202 65.460  -4.012  1.00 29.35 ? 85  VAL A C     1 
ATOM   6732  O O     . VAL C  1 85  ? -33.231 66.146  -3.683  1.00 31.46 ? 85  VAL A O     1 
ATOM   6733  C CB    . VAL C  1 85  ? -36.254 65.021  -2.590  1.00 28.37 ? 85  VAL A CB    1 
ATOM   6734  C CG1   . VAL C  1 85  ? -35.258 64.739  -1.481  1.00 28.71 ? 85  VAL A CG1   1 
ATOM   6735  C CG2   . VAL C  1 85  ? -37.466 65.701  -1.994  1.00 29.10 ? 85  VAL A CG2   1 
ATOM   6736  N N     . LEU C  1 86  ? -34.057 64.329  -4.707  1.00 29.79 ? 86  LEU A N     1 
ATOM   6737  C CA    . LEU C  1 86  ? -32.703 63.862  -5.017  1.00 29.62 ? 86  LEU A CA    1 
ATOM   6738  C C     . LEU C  1 86  ? -31.928 64.851  -5.871  1.00 30.11 ? 86  LEU A C     1 
ATOM   6739  O O     . LEU C  1 86  ? -30.696 64.813  -5.854  1.00 33.59 ? 86  LEU A O     1 
ATOM   6740  C CB    . LEU C  1 86  ? -32.703 62.511  -5.731  1.00 26.17 ? 86  LEU A CB    1 
ATOM   6741  C CG    . LEU C  1 86  ? -33.613 61.389  -5.225  1.00 29.34 ? 86  LEU A CG    1 
ATOM   6742  C CD1   . LEU C  1 86  ? -33.243 60.087  -5.923  1.00 28.69 ? 86  LEU A CD1   1 
ATOM   6743  C CD2   . LEU C  1 86  ? -33.563 61.246  -3.703  1.00 29.92 ? 86  LEU A CD2   1 
ATOM   6744  N N     . GLN C  1 87  ? -32.603 65.741  -6.607  1.00 30.08 ? 87  GLN A N     1 
ATOM   6745  C CA    . GLN C  1 87  ? -31.902 66.785  -7.349  1.00 33.81 ? 87  GLN A CA    1 
ATOM   6746  C C     . GLN C  1 87  ? -31.824 68.097  -6.578  1.00 35.20 ? 87  GLN A C     1 
ATOM   6747  O O     . GLN C  1 87  ? -31.149 69.026  -7.030  1.00 39.84 ? 87  GLN A O     1 
ATOM   6748  C CB    . GLN C  1 87  ? -32.545 66.993  -8.727  1.00 29.94 ? 87  GLN A CB    1 
ATOM   6749  C CG    . GLN C  1 87  ? -32.570 65.697  -9.524  1.00 26.88 ? 87  GLN A CG    1 
ATOM   6750  C CD    . GLN C  1 87  ? -32.924 65.854  -11.001 1.00 36.24 ? 87  GLN A CD    1 
ATOM   6751  O OE1   . GLN C  1 87  ? -34.030 65.541  -11.416 1.00 35.33 ? 87  GLN A OE1   1 
ATOM   6752  N NE2   . GLN C  1 87  ? -31.964 66.301  -11.807 1.00 42.23 ? 87  GLN A NE2   1 
ATOM   6753  N N     . ASP C  1 88  ? -32.468 68.182  -5.423  1.00 30.55 ? 88  ASP A N     1 
ATOM   6754  C CA    . ASP C  1 88  ? -32.388 69.366  -4.587  1.00 32.92 ? 88  ASP A CA    1 
ATOM   6755  C C     . ASP C  1 88  ? -30.957 69.628  -4.139  1.00 34.34 ? 88  ASP A C     1 
ATOM   6756  O O     . ASP C  1 88  ? -30.350 68.758  -3.492  1.00 35.17 ? 88  ASP A O     1 
ATOM   6757  C CB    . ASP C  1 88  ? -33.277 69.210  -3.364  1.00 30.28 ? 88  ASP A CB    1 
ATOM   6758  C CG    . ASP C  1 88  ? -33.709 70.537  -2.799  1.00 44.43 ? 88  ASP A CG    1 
ATOM   6759  O OD1   . ASP C  1 88  ? -32.904 71.495  -2.892  1.00 45.19 ? 88  ASP A OD1   1 
ATOM   6760  O OD2   . ASP C  1 88  ? -34.851 70.633  -2.273  1.00 44.27 ? 88  ASP A OD2   1 
ATOM   6761  N N     . PRO C  1 89  ? -30.387 70.798  -4.443  1.00 35.83 ? 89  PRO A N     1 
ATOM   6762  C CA    . PRO C  1 89  ? -29.076 71.160  -3.863  1.00 38.47 ? 89  PRO A CA    1 
ATOM   6763  C C     . PRO C  1 89  ? -29.052 71.215  -2.343  1.00 33.39 ? 89  PRO A C     1 
ATOM   6764  O O     . PRO C  1 89  ? -28.028 70.856  -1.743  1.00 32.59 ? 89  PRO A O     1 
ATOM   6765  C CB    . PRO C  1 89  ? -28.804 72.534  -4.485  1.00 30.30 ? 89  PRO A CB    1 
ATOM   6766  C CG    . PRO C  1 89  ? -29.457 72.441  -5.810  1.00 29.64 ? 89  PRO A CG    1 
ATOM   6767  C CD    . PRO C  1 89  ? -30.727 71.661  -5.583  1.00 36.72 ? 89  PRO A CD    1 
ATOM   6768  N N     . GLU C  1 90  ? -30.129 71.686  -1.708  1.00 37.34 ? 90  GLU A N     1 
ATOM   6769  C CA    . GLU C  1 90  ? -30.287 71.544  -0.263  1.00 39.11 ? 90  GLU A CA    1 
ATOM   6770  C C     . GLU C  1 90  ? -29.941 70.128  0.177   1.00 35.37 ? 90  GLU A C     1 
ATOM   6771  O O     . GLU C  1 90  ? -29.065 69.903  1.019   1.00 30.08 ? 90  GLU A O     1 
ATOM   6772  C CB    . GLU C  1 90  ? -31.739 71.838  0.146   1.00 41.99 ? 90  GLU A CB    1 
ATOM   6773  C CG    . GLU C  1 90  ? -32.230 73.283  0.107   1.00 52.37 ? 90  GLU A CG    1 
ATOM   6774  C CD    . GLU C  1 90  ? -33.652 73.440  0.688   1.00 59.45 ? 90  GLU A CD    1 
ATOM   6775  O OE1   . GLU C  1 90  ? -34.114 72.546  1.445   1.00 55.48 ? 90  GLU A OE1   1 
ATOM   6776  O OE2   . GLU C  1 90  ? -34.307 74.459  0.379   1.00 55.97 ? 90  GLU A OE2   1 
ATOM   6777  N N     . PHE C  1 91  ? -30.654 69.163  -0.413  1.00 35.43 ? 91  PHE A N     1 
ATOM   6778  C CA    . PHE C  1 91  ? -30.691 67.793  0.076   1.00 31.47 ? 91  PHE A CA    1 
ATOM   6779  C C     . PHE C  1 91  ? -29.394 67.082  -0.238  1.00 33.58 ? 91  PHE A C     1 
ATOM   6780  O O     . PHE C  1 91  ? -28.833 66.378  0.618   1.00 31.33 ? 91  PHE A O     1 
ATOM   6781  C CB    . PHE C  1 91  ? -31.891 67.078  -0.557  1.00 32.30 ? 91  PHE A CB    1 
ATOM   6782  C CG    . PHE C  1 91  ? -31.810 65.579  -0.534  1.00 32.10 ? 91  PHE A CG    1 
ATOM   6783  C CD1   . PHE C  1 91  ? -31.171 64.884  -1.546  1.00 30.91 ? 91  PHE A CD1   1 
ATOM   6784  C CD2   . PHE C  1 91  ? -32.417 64.861  0.479   1.00 35.20 ? 91  PHE A CD2   1 
ATOM   6785  C CE1   . PHE C  1 91  ? -31.110 63.506  -1.527  1.00 30.81 ? 91  PHE A CE1   1 
ATOM   6786  C CE2   . PHE C  1 91  ? -32.362 63.489  0.498   1.00 30.99 ? 91  PHE A CE2   1 
ATOM   6787  C CZ    . PHE C  1 91  ? -31.709 62.812  -0.507  1.00 26.67 ? 91  PHE A CZ    1 
ATOM   6788  N N     . ILE C  1 92  ? -28.910 67.260  -1.468  1.00 29.89 ? 92  ILE A N     1 
ATOM   6789  C CA    . ILE C  1 92  ? -27.589 66.766  -1.841  1.00 32.64 ? 92  ILE A CA    1 
ATOM   6790  C C     . ILE C  1 92  ? -26.542 67.213  -0.823  1.00 33.15 ? 92  ILE A C     1 
ATOM   6791  O O     . ILE C  1 92  ? -25.827 66.394  -0.230  1.00 34.44 ? 92  ILE A O     1 
ATOM   6792  C CB    . ILE C  1 92  ? -27.219 67.248  -3.252  1.00 33.70 ? 92  ILE A CB    1 
ATOM   6793  C CG1   . ILE C  1 92  ? -28.226 66.737  -4.281  1.00 32.90 ? 92  ILE A CG1   1 
ATOM   6794  C CG2   . ILE C  1 92  ? -25.765 66.857  -3.592  1.00 30.76 ? 92  ILE A CG2   1 
ATOM   6795  C CD1   . ILE C  1 92  ? -27.793 67.012  -5.700  1.00 35.68 ? 92  ILE A CD1   1 
ATOM   6796  N N     . ASP C  1 93  ? -26.427 68.527  -0.623  1.00 28.62 ? 93  ASP A N     1 
ATOM   6797  C CA    . ASP C  1 93  ? -25.410 69.037  0.284   1.00 35.17 ? 93  ASP A CA    1 
ATOM   6798  C C     . ASP C  1 93  ? -25.518 68.349  1.631   1.00 33.96 ? 93  ASP A C     1 
ATOM   6799  O O     . ASP C  1 93  ? -24.538 67.782  2.127   1.00 34.66 ? 93  ASP A O     1 
ATOM   6800  C CB    . ASP C  1 93  ? -25.543 70.549  0.435   1.00 34.48 ? 93  ASP A CB    1 
ATOM   6801  C CG    . ASP C  1 93  ? -24.935 71.289  -0.711  1.00 34.14 ? 93  ASP A CG    1 
ATOM   6802  O OD1   . ASP C  1 93  ? -24.303 70.637  -1.568  1.00 42.27 ? 93  ASP A OD1   1 
ATOM   6803  O OD2   . ASP C  1 93  ? -25.074 72.525  -0.755  1.00 39.62 ? 93  ASP A OD2   1 
ATOM   6804  N N     . ARG C  1 94  ? -26.723 68.345  2.211   1.00 32.85 ? 94  ARG A N     1 
ATOM   6805  C CA    . ARG C  1 94  ? -26.952 67.597  3.442   1.00 36.36 ? 94  ARG A CA    1 
ATOM   6806  C C     . ARG C  1 94  ? -26.386 66.193  3.348   1.00 35.08 ? 94  ARG A C     1 
ATOM   6807  O O     . ARG C  1 94  ? -25.755 65.707  4.293   1.00 37.90 ? 94  ARG A O     1 
ATOM   6808  C CB    . ARG C  1 94  ? -28.440 67.545  3.760   1.00 40.35 ? 94  ARG A CB    1 
ATOM   6809  C CG    . ARG C  1 94  ? -28.940 68.806  4.403   1.00 45.66 ? 94  ARG A CG    1 
ATOM   6810  C CD    . ARG C  1 94  ? -30.065 68.516  5.390   1.00 49.86 ? 94  ARG A CD    1 
ATOM   6811  N NE    . ARG C  1 94  ? -29.611 68.169  6.735   1.00 55.73 ? 94  ARG A NE    1 
ATOM   6812  C CZ    . ARG C  1 94  ? -29.238 69.054  7.650   1.00 52.29 ? 94  ARG A CZ    1 
ATOM   6813  N NH1   . ARG C  1 94  ? -29.203 70.353  7.386   1.00 55.19 ? 94  ARG A NH1   1 
ATOM   6814  N NH2   . ARG C  1 94  ? -28.899 68.628  8.863   1.00 51.70 ? 94  ARG A NH2   1 
ATOM   6815  N N     . LEU C  1 95  ? -26.578 65.532  2.206   1.00 34.34 ? 95  LEU A N     1 
ATOM   6816  C CA    . LEU C  1 95  ? -25.985 64.217  2.029   1.00 30.49 ? 95  LEU A CA    1 
ATOM   6817  C C     . LEU C  1 95  ? -24.470 64.299  1.995   1.00 30.72 ? 95  LEU A C     1 
ATOM   6818  O O     . LEU C  1 95  ? -23.788 63.386  2.468   1.00 31.79 ? 95  LEU A O     1 
ATOM   6819  C CB    . LEU C  1 95  ? -26.511 63.566  0.751   1.00 30.61 ? 95  LEU A CB    1 
ATOM   6820  C CG    . LEU C  1 95  ? -27.817 62.795  0.901   1.00 29.33 ? 95  LEU A CG    1 
ATOM   6821  C CD1   . LEU C  1 95  ? -27.830 61.693  -0.110  1.00 27.60 ? 95  LEU A CD1   1 
ATOM   6822  C CD2   . LEU C  1 95  ? -27.987 62.230  2.324   1.00 33.73 ? 95  LEU A CD2   1 
ATOM   6823  N N     . ALA C  1 96  ? -23.923 65.384  1.460   1.00 33.35 ? 96  ALA A N     1 
ATOM   6824  C CA    . ALA C  1 96  ? -22.474 65.474  1.328   1.00 37.13 ? 96  ALA A CA    1 
ATOM   6825  C C     . ALA C  1 96  ? -21.789 65.837  2.634   1.00 33.62 ? 96  ALA A C     1 
ATOM   6826  O O     . ALA C  1 96  ? -20.560 65.771  2.708   1.00 32.87 ? 96  ALA A O     1 
ATOM   6827  C CB    . ALA C  1 96  ? -22.096 66.489  0.248   1.00 34.27 ? 96  ALA A CB    1 
ATOM   6828  N N     . ALA C  1 97  ? -22.550 66.212  3.657   1.00 32.43 ? 97  ALA A N     1 
ATOM   6829  C CA    . ALA C  1 97  ? -21.950 66.420  4.969   1.00 34.67 ? 97  ALA A CA    1 
ATOM   6830  C C     . ALA C  1 97  ? -21.453 65.112  5.545   1.00 34.16 ? 97  ALA A C     1 
ATOM   6831  O O     . ALA C  1 97  ? -20.427 65.082  6.230   1.00 36.24 ? 97  ALA A O     1 
ATOM   6832  C CB    . ALA C  1 97  ? -22.955 67.057  5.924   1.00 37.79 ? 97  ALA A CB    1 
ATOM   6833  N N     . HIS C  1 98  ? -22.187 64.024  5.301   1.00 39.14 ? 98  HIS A N     1 
ATOM   6834  C CA    . HIS C  1 98  ? -21.708 62.698  5.667   1.00 36.71 ? 98  HIS A CA    1 
ATOM   6835  C C     . HIS C  1 98  ? -20.715 62.180  4.642   1.00 33.25 ? 98  HIS A C     1 
ATOM   6836  O O     . HIS C  1 98  ? -19.630 61.706  4.998   1.00 32.04 ? 98  HIS A O     1 
ATOM   6837  C CB    . HIS C  1 98  ? -22.876 61.725  5.786   1.00 32.98 ? 98  HIS A CB    1 
ATOM   6838  C CG    . HIS C  1 98  ? -23.914 62.153  6.764   1.00 35.88 ? 98  HIS A CG    1 
ATOM   6839  N ND1   . HIS C  1 98  ? -23.909 61.739  8.079   1.00 41.99 ? 98  HIS A ND1   1 
ATOM   6840  C CD2   . HIS C  1 98  ? -24.999 62.948  6.621   1.00 39.36 ? 98  HIS A CD2   1 
ATOM   6841  C CE1   . HIS C  1 98  ? -24.940 62.276  8.710   1.00 42.82 ? 98  HIS A CE1   1 
ATOM   6842  N NE2   . HIS C  1 98  ? -25.620 63.011  7.846   1.00 40.31 ? 98  HIS A NE2   1 
ATOM   6843  N N     . THR C  1 99  ? -21.077 62.281  3.363   1.00 37.29 ? 99  THR A N     1 
ATOM   6844  C CA    . THR C  1 99  ? -20.278 61.760  2.252   1.00 38.07 ? 99  THR A CA    1 
ATOM   6845  C C     . THR C  1 99  ? -19.369 62.854  1.735   1.00 37.33 ? 99  THR A C     1 
ATOM   6846  O O     . THR C  1 99  ? -19.637 63.513  0.732   1.00 46.91 ? 99  THR A O     1 
ATOM   6847  C CB    . THR C  1 99  ? -21.193 61.302  1.119   1.00 33.66 ? 99  THR A CB    1 
ATOM   6848  O OG1   . THR C  1 99  ? -21.867 62.451  0.604   1.00 33.75 ? 99  THR A OG1   1 
ATOM   6849  C CG2   . THR C  1 99  ? -22.208 60.331  1.618   1.00 28.95 ? 99  THR A CG2   1 
ATOM   6850  N N     . GLY C  1 100 ? -18.249 63.060  2.418   1.00 34.70 ? 100 GLY A N     1 
ATOM   6851  C CA    . GLY C  1 100 ? -17.289 64.057  1.973   1.00 35.75 ? 100 GLY A CA    1 
ATOM   6852  C C     . GLY C  1 100 ? -16.123 63.381  1.281   1.00 41.05 ? 100 GLY A C     1 
ATOM   6853  O O     . GLY C  1 100 ? -15.555 62.422  1.796   1.00 51.13 ? 100 GLY A O     1 
ATOM   6854  N N     . THR C  1 101 ? -15.778 63.905  0.107   1.00 42.46 ? 101 THR A N     1 
ATOM   6855  C CA    . THR C  1 101 ? -14.834 63.290  -0.833  1.00 39.69 ? 101 THR A CA    1 
ATOM   6856  C C     . THR C  1 101 ? -15.430 62.024  -1.416  1.00 38.19 ? 101 THR A C     1 
ATOM   6857  O O     . THR C  1 101 ? -14.902 61.514  -2.394  1.00 39.13 ? 101 THR A O     1 
ATOM   6858  C CB    . THR C  1 101 ? -13.475 62.933  -0.219  1.00 39.08 ? 101 THR A CB    1 
ATOM   6859  O OG1   . THR C  1 101 ? -13.569 61.672  0.457   1.00 35.77 ? 101 THR A OG1   1 
ATOM   6860  C CG2   . THR C  1 101 ? -12.985 63.990  0.737   1.00 39.98 ? 101 THR A CG2   1 
ATOM   6861  N N     . GLY C  1 102 ? -16.512 61.507  -0.815  1.00 38.29 ? 102 GLY A N     1 
ATOM   6862  C CA    . GLY C  1 102 ? -17.226 60.353  -1.327  1.00 35.90 ? 102 GLY A CA    1 
ATOM   6863  C C     . GLY C  1 102 ? -16.523 59.022  -1.143  1.00 38.24 ? 102 GLY A C     1 
ATOM   6864  O O     . GLY C  1 102 ? -17.151 57.962  -1.346  1.00 34.66 ? 102 GLY A O     1 
ATOM   6865  N N     . ALA C  1 103 ? -15.249 59.034  -0.760  1.00 38.75 ? 103 ALA A N     1 
ATOM   6866  C CA    . ALA C  1 103 ? -14.481 57.801  -0.679  1.00 38.51 ? 103 ALA A CA    1 
ATOM   6867  C C     . ALA C  1 103 ? -15.044 56.889  0.403   1.00 37.46 ? 103 ALA A C     1 
ATOM   6868  O O     . ALA C  1 103 ? -15.418 57.336  1.490   1.00 40.30 ? 103 ALA A O     1 
ATOM   6869  C CB    . ALA C  1 103 ? -13.008 58.106  -0.403  1.00 35.75 ? 103 ALA A CB    1 
ATOM   6870  N N     . GLY C  1 104 ? -15.108 55.601  0.101   1.00 37.91 ? 104 GLY A N     1 
ATOM   6871  C CA    . GLY C  1 104 ? -15.636 54.637  1.038   1.00 33.57 ? 104 GLY A CA    1 
ATOM   6872  C C     . GLY C  1 104 ? -17.143 54.597  1.137   1.00 35.94 ? 104 GLY A C     1 
ATOM   6873  O O     . GLY C  1 104 ? -17.663 53.833  1.955   1.00 39.52 ? 104 GLY A O     1 
ATOM   6874  N N     . TRP C  1 105 ? -17.859 55.373  0.318   1.00 38.72 ? 105 TRP A N     1 
ATOM   6875  C CA    . TRP C  1 105 ? -19.303 55.560  0.437   1.00 34.50 ? 105 TRP A CA    1 
ATOM   6876  C C     . TRP C  1 105 ? -19.997 55.088  -0.831  1.00 32.60 ? 105 TRP A C     1 
ATOM   6877  O O     . TRP C  1 105 ? -19.595 55.456  -1.944  1.00 36.95 ? 105 TRP A O     1 
ATOM   6878  C CB    . TRP C  1 105 ? -19.671 57.034  0.684   1.00 37.41 ? 105 TRP A CB    1 
ATOM   6879  C CG    . TRP C  1 105 ? -19.676 57.509  2.134   1.00 36.95 ? 105 TRP A CG    1 
ATOM   6880  C CD1   . TRP C  1 105 ? -18.709 58.246  2.751   1.00 38.21 ? 105 TRP A CD1   1 
ATOM   6881  C CD2   . TRP C  1 105 ? -20.710 57.324  3.107   1.00 37.25 ? 105 TRP A CD2   1 
ATOM   6882  N NE1   . TRP C  1 105 ? -19.062 58.512  4.048   1.00 38.33 ? 105 TRP A NE1   1 
ATOM   6883  C CE2   . TRP C  1 105 ? -20.286 57.954  4.293   1.00 38.36 ? 105 TRP A CE2   1 
ATOM   6884  C CE3   . TRP C  1 105 ? -21.949 56.686  3.093   1.00 39.96 ? 105 TRP A CE3   1 
ATOM   6885  C CZ2   . TRP C  1 105 ? -21.049 57.958  5.449   1.00 33.34 ? 105 TRP A CZ2   1 
ATOM   6886  C CZ3   . TRP C  1 105 ? -22.706 56.685  4.254   1.00 41.79 ? 105 TRP A CZ3   1 
ATOM   6887  C CH2   . TRP C  1 105 ? -22.253 57.323  5.410   1.00 39.18 ? 105 TRP A CH2   1 
ATOM   6888  N N     . SER C  1 106 ? -21.043 54.294  -0.653  1.00 25.60 ? 106 SER A N     1 
ATOM   6889  C CA    . SER C  1 106 ? -21.932 53.880  -1.714  1.00 30.06 ? 106 SER A CA    1 
ATOM   6890  C C     . SER C  1 106 ? -23.333 54.397  -1.426  1.00 34.31 ? 106 SER A C     1 
ATOM   6891  O O     . SER C  1 106 ? -23.653 54.831  -0.312  1.00 34.18 ? 106 SER A O     1 
ATOM   6892  C CB    . SER C  1 106 ? -21.951 52.356  -1.847  1.00 33.05 ? 106 SER A CB    1 
ATOM   6893  O OG    . SER C  1 106 ? -21.944 51.772  -0.556  1.00 39.10 ? 106 SER A OG    1 
ATOM   6894  N N     . LEU C  1 107 ? -24.177 54.337  -2.451  1.00 30.26 ? 107 LEU A N     1 
ATOM   6895  C CA    . LEU C  1 107 ? -25.599 54.589  -2.305  1.00 28.60 ? 107 LEU A CA    1 
ATOM   6896  C C     . LEU C  1 107 ? -26.338 53.260  -2.409  1.00 29.23 ? 107 LEU A C     1 
ATOM   6897  O O     . LEU C  1 107 ? -26.015 52.425  -3.258  1.00 34.39 ? 107 LEU A O     1 
ATOM   6898  C CB    . LEU C  1 107 ? -26.089 55.573  -3.361  1.00 26.14 ? 107 LEU A CB    1 
ATOM   6899  C CG    . LEU C  1 107 ? -27.596 55.754  -3.481  1.00 25.74 ? 107 LEU A CG    1 
ATOM   6900  C CD1   . LEU C  1 107 ? -28.180 56.509  -2.273  1.00 23.55 ? 107 LEU A CD1   1 
ATOM   6901  C CD2   . LEU C  1 107 ? -27.910 56.488  -4.782  1.00 30.81 ? 107 LEU A CD2   1 
ATOM   6902  N N     . PHE C  1 108 ? -27.314 53.065  -1.524  1.00 26.29 ? 108 PHE A N     1 
ATOM   6903  C CA    . PHE C  1 108 ? -28.055 51.814  -1.376  1.00 27.37 ? 108 PHE A CA    1 
ATOM   6904  C C     . PHE C  1 108 ? -29.531 52.129  -1.619  1.00 30.62 ? 108 PHE A C     1 
ATOM   6905  O O     . PHE C  1 108 ? -30.324 52.194  -0.665  1.00 25.59 ? 108 PHE A O     1 
ATOM   6906  C CB    . PHE C  1 108 ? -27.810 51.219  0.016   1.00 30.03 ? 108 PHE A CB    1 
ATOM   6907  C CG    . PHE C  1 108 ? -28.518 49.904  0.287   1.00 25.77 ? 108 PHE A CG    1 
ATOM   6908  C CD1   . PHE C  1 108 ? -28.102 48.726  -0.313  1.00 26.26 ? 108 PHE A CD1   1 
ATOM   6909  C CD2   . PHE C  1 108 ? -29.581 49.845  1.192   1.00 30.37 ? 108 PHE A CD2   1 
ATOM   6910  C CE1   . PHE C  1 108 ? -28.758 47.505  -0.055  1.00 26.94 ? 108 PHE A CE1   1 
ATOM   6911  C CE2   . PHE C  1 108 ? -30.245 48.636  1.453   1.00 29.81 ? 108 PHE A CE2   1 
ATOM   6912  C CZ    . PHE C  1 108 ? -29.836 47.466  0.824   1.00 28.79 ? 108 PHE A CZ    1 
ATOM   6913  N N     . PRO C  1 109 ? -29.925 52.360  -2.884  1.00 26.47 ? 109 PRO A N     1 
ATOM   6914  C CA    . PRO C  1 109 ? -31.283 52.835  -3.188  1.00 25.15 ? 109 PRO A CA    1 
ATOM   6915  C C     . PRO C  1 109 ? -32.317 51.742  -3.414  1.00 31.49 ? 109 PRO A C     1 
ATOM   6916  O O     . PRO C  1 109 ? -32.057 50.678  -3.984  1.00 32.59 ? 109 PRO A O     1 
ATOM   6917  C CB    . PRO C  1 109 ? -31.080 53.617  -4.490  1.00 26.02 ? 109 PRO A CB    1 
ATOM   6918  C CG    . PRO C  1 109 ? -29.990 52.880  -5.167  1.00 25.60 ? 109 PRO A CG    1 
ATOM   6919  C CD    . PRO C  1 109 ? -29.071 52.374  -4.089  1.00 25.01 ? 109 PRO A CD    1 
ATOM   6920  N N     . CYS C  1 110 ? -33.534 52.042  -2.981  1.00 26.89 ? 110 CYS A N     1 
ATOM   6921  C CA    . CYS C  1 110 ? -34.616 51.109  -3.228  1.00 28.36 ? 110 CYS A CA    1 
ATOM   6922  C C     . CYS C  1 110 ? -34.894 51.007  -4.712  1.00 30.20 ? 110 CYS A C     1 
ATOM   6923  O O     . CYS C  1 110 ? -34.970 49.906  -5.284  1.00 28.10 ? 110 CYS A O     1 
ATOM   6924  C CB    . CYS C  1 110 ? -35.858 51.558  -2.484  1.00 29.48 ? 110 CYS A CB    1 
ATOM   6925  S SG    . CYS C  1 110 ? -37.146 50.350  -2.602  1.00 38.89 ? 110 CYS A SG    1 
ATOM   6926  N N     . VAL C  1 111 ? -35.030 52.156  -5.352  1.00 32.60 ? 111 VAL A N     1 
ATOM   6927  C CA    . VAL C  1 111 ? -35.328 52.243  -6.765  1.00 20.01 ? 111 VAL A CA    1 
ATOM   6928  C C     . VAL C  1 111 ? -34.196 52.990  -7.422  1.00 21.22 ? 111 VAL A C     1 
ATOM   6929  O O     . VAL C  1 111 ? -34.101 54.221  -7.323  1.00 22.82 ? 111 VAL A O     1 
ATOM   6930  C CB    . VAL C  1 111 ? -36.654 52.944  -7.014  1.00 25.39 ? 111 VAL A CB    1 
ATOM   6931  C CG1   . VAL C  1 111 ? -36.975 52.845  -8.486  1.00 29.12 ? 111 VAL A CG1   1 
ATOM   6932  C CG2   . VAL C  1 111 ? -37.719 52.283  -6.185  1.00 25.06 ? 111 VAL A CG2   1 
ATOM   6933  N N     . SER C  1 112 ? -33.353 52.252  -8.112  1.00 26.03 ? 112 SER A N     1 
ATOM   6934  C CA    . SER C  1 112 ? -32.246 52.815  -8.873  1.00 24.61 ? 112 SER A CA    1 
ATOM   6935  C C     . SER C  1 112 ? -32.729 53.740  -9.984  1.00 26.24 ? 112 SER A C     1 
ATOM   6936  O O     . SER C  1 112 ? -32.634 53.400  -11.162 1.00 31.93 ? 112 SER A O     1 
ATOM   6937  C CB    . SER C  1 112 ? -31.423 51.674  -9.478  1.00 18.08 ? 112 SER A CB    1 
ATOM   6938  O OG    . SER C  1 112 ? -31.025 50.751  -8.473  1.00 22.03 ? 112 SER A OG    1 
ATOM   6939  N N     . THR C  1 113 ? -33.206 54.931  -9.638  1.00 25.56 ? 113 THR A N     1 
ATOM   6940  C CA    . THR C  1 113 ? -33.669 55.823  -10.689 1.00 24.13 ? 113 THR A CA    1 
ATOM   6941  C C     . THR C  1 113 ? -32.510 56.576  -11.326 1.00 28.01 ? 113 THR A C     1 
ATOM   6942  O O     . THR C  1 113 ? -31.352 56.524  -10.877 1.00 26.05 ? 113 THR A O     1 
ATOM   6943  C CB    . THR C  1 113 ? -34.667 56.832  -10.137 1.00 25.85 ? 113 THR A CB    1 
ATOM   6944  O OG1   . THR C  1 113 ? -34.060 57.542  -9.058  1.00 27.66 ? 113 THR A OG1   1 
ATOM   6945  C CG2   . THR C  1 113 ? -35.904 56.156  -9.648  1.00 21.44 ? 113 THR A CG2   1 
ATOM   6946  N N     . ARG C  1 114 ? -32.859 57.324  -12.380 1.00 29.10 ? 114 ARG A N     1 
ATOM   6947  C CA    . ARG C  1 114 ? -31.896 58.216  -13.026 1.00 30.49 ? 114 ARG A CA    1 
ATOM   6948  C C     . ARG C  1 114 ? -31.355 59.246  -12.045 1.00 25.25 ? 114 ARG A C     1 
ATOM   6949  O O     . ARG C  1 114 ? -30.180 59.618  -12.129 1.00 26.90 ? 114 ARG A O     1 
ATOM   6950  C CB    . ARG C  1 114 ? -32.541 58.887  -14.249 1.00 32.07 ? 114 ARG A CB    1 
ATOM   6951  C CG    . ARG C  1 114 ? -31.889 60.190  -14.720 1.00 28.59 ? 114 ARG A CG    1 
ATOM   6952  C CD    . ARG C  1 114 ? -32.607 60.750  -15.953 1.00 28.35 ? 114 ARG A CD    1 
ATOM   6953  N NE    . ARG C  1 114 ? -31.929 61.909  -16.536 1.00 32.23 ? 114 ARG A NE    1 
ATOM   6954  C CZ    . ARG C  1 114 ? -30.920 61.841  -17.399 1.00 27.08 ? 114 ARG A CZ    1 
ATOM   6955  N NH1   . ARG C  1 114 ? -30.413 60.678  -17.778 1.00 29.96 ? 114 ARG A NH1   1 
ATOM   6956  N NH2   . ARG C  1 114 ? -30.413 62.965  -17.903 1.00 19.97 ? 114 ARG A NH2   1 
ATOM   6957  N N     . ALA C  1 115 ? -32.171 59.678  -11.075 1.00 26.23 ? 115 ALA A N     1 
ATOM   6958  C CA    . ALA C  1 115 ? -31.675 60.649  -10.097 1.00 29.90 ? 115 ALA A CA    1 
ATOM   6959  C C     . ALA C  1 115 ? -30.797 60.004  -9.046  1.00 29.16 ? 115 ALA A C     1 
ATOM   6960  O O     . ALA C  1 115 ? -29.916 60.671  -8.484  1.00 29.31 ? 115 ALA A O     1 
ATOM   6961  C CB    . ALA C  1 115 ? -32.824 61.378  -9.400  1.00 31.84 ? 115 ALA A CB    1 
ATOM   6962  N N     . ALA C  1 116 ? -31.026 58.726  -8.739  1.00 29.80 ? 116 ALA A N     1 
ATOM   6963  C CA    . ALA C  1 116 ? -30.078 58.025  -7.875  1.00 31.18 ? 116 ALA A CA    1 
ATOM   6964  C C     . ALA C  1 116 ? -28.710 58.004  -8.541  1.00 31.27 ? 116 ALA A C     1 
ATOM   6965  O O     . ALA C  1 116 ? -27.745 58.579  -8.027  1.00 34.65 ? 116 ALA A O     1 
ATOM   6966  C CB    . ALA C  1 116 ? -30.571 56.608  -7.557  1.00 23.95 ? 116 ALA A CB    1 
ATOM   6967  N N     . ALA C  1 117 ? -28.641 57.415  -9.740  1.00 29.54 ? 117 ALA A N     1 
ATOM   6968  C CA    . ALA C  1 117 ? -27.412 57.404  -10.520 1.00 28.59 ? 117 ALA A CA    1 
ATOM   6969  C C     . ALA C  1 117 ? -26.778 58.786  -10.583 1.00 30.58 ? 117 ALA A C     1 
ATOM   6970  O O     . ALA C  1 117 ? -25.583 58.953  -10.312 1.00 32.18 ? 117 ALA A O     1 
ATOM   6971  C CB    . ALA C  1 117 ? -27.723 56.894  -11.921 1.00 27.43 ? 117 ALA A CB    1 
ATOM   6972  N N     . GLN C  1 118 ? -27.578 59.799  -10.915 1.00 30.43 ? 118 GLN A N     1 
ATOM   6973  C CA    . GLN C  1 118 ? -27.076 61.167  -10.908 1.00 32.11 ? 118 GLN A CA    1 
ATOM   6974  C C     . GLN C  1 118 ? -26.577 61.566  -9.526  1.00 33.62 ? 118 GLN A C     1 
ATOM   6975  O O     . GLN C  1 118 ? -25.545 62.243  -9.396  1.00 33.62 ? 118 GLN A O     1 
ATOM   6976  C CB    . GLN C  1 118 ? -28.168 62.128  -11.377 1.00 32.91 ? 118 GLN A CB    1 
ATOM   6977  C CG    . GLN C  1 118 ? -28.452 62.081  -12.897 1.00 29.21 ? 118 GLN A CG    1 
ATOM   6978  C CD    . GLN C  1 118 ? -29.795 62.693  -13.275 1.00 28.69 ? 118 GLN A CD    1 
ATOM   6979  O OE1   . GLN C  1 118 ? -30.712 62.730  -12.467 1.00 33.21 ? 118 GLN A OE1   1 
ATOM   6980  N NE2   . GLN C  1 118 ? -29.916 63.168  -14.515 1.00 30.56 ? 118 GLN A NE2   1 
ATOM   6981  N N     . LEU C  1 119 ? -27.295 61.164  -8.476  1.00 27.41 ? 119 LEU A N     1 
ATOM   6982  C CA    . LEU C  1 119 ? -26.867 61.575  -7.150  1.00 29.41 ? 119 LEU A CA    1 
ATOM   6983  C C     . LEU C  1 119 ? -25.491 61.018  -6.830  1.00 31.96 ? 119 LEU A C     1 
ATOM   6984  O O     . LEU C  1 119 ? -24.646 61.722  -6.269  1.00 34.56 ? 119 LEU A O     1 
ATOM   6985  C CB    . LEU C  1 119 ? -27.875 61.140  -6.099  1.00 32.59 ? 119 LEU A CB    1 
ATOM   6986  C CG    . LEU C  1 119 ? -27.463 61.538  -4.681  1.00 25.30 ? 119 LEU A CG    1 
ATOM   6987  C CD1   . LEU C  1 119 ? -27.346 63.057  -4.516  1.00 27.66 ? 119 LEU A CD1   1 
ATOM   6988  C CD2   . LEU C  1 119 ? -28.462 60.995  -3.702  1.00 22.22 ? 119 LEU A CD2   1 
ATOM   6989  N N     . THR C  1 120 ? -25.237 59.764  -7.207  1.00 31.03 ? 120 THR A N     1 
ATOM   6990  C CA    . THR C  1 120 ? -23.933 59.171  -6.939  1.00 31.51 ? 120 THR A CA    1 
ATOM   6991  C C     . THR C  1 120 ? -22.820 60.023  -7.532  1.00 36.92 ? 120 THR A C     1 
ATOM   6992  O O     . THR C  1 120 ? -21.758 60.183  -6.921  1.00 40.02 ? 120 THR A O     1 
ATOM   6993  C CB    . THR C  1 120 ? -23.860 57.746  -7.499  1.00 32.96 ? 120 THR A CB    1 
ATOM   6994  O OG1   . THR C  1 120 ? -23.948 57.781  -8.932  1.00 39.75 ? 120 THR A OG1   1 
ATOM   6995  C CG2   . THR C  1 120 ? -24.991 56.902  -6.965  1.00 32.64 ? 120 THR A CG2   1 
ATOM   6996  N N     . ARG C  1 121 ? -23.059 60.604  -8.712  1.00 37.59 ? 121 ARG A N     1 
ATOM   6997  C CA    . ARG C  1 121 ? -22.069 61.476  -9.332  1.00 36.88 ? 121 ARG A CA    1 
ATOM   6998  C C     . ARG C  1 121 ? -21.918 62.773  -8.549  1.00 35.69 ? 121 ARG A C     1 
ATOM   6999  O O     . ARG C  1 121 ? -20.798 63.190  -8.235  1.00 35.88 ? 121 ARG A O     1 
ATOM   7000  C CB    . ARG C  1 121 ? -22.469 61.758  -10.781 1.00 37.34 ? 121 ARG A CB    1 
ATOM   7001  C CG    . ARG C  1 121 ? -21.320 62.130  -11.678 1.00 41.52 ? 121 ARG A CG    1 
ATOM   7002  C CD    . ARG C  1 121 ? -21.732 62.041  -13.125 1.00 46.91 ? 121 ARG A CD    1 
ATOM   7003  N NE    . ARG C  1 121 ? -21.111 60.898  -13.782 1.00 52.97 ? 121 ARG A NE    1 
ATOM   7004  C CZ    . ARG C  1 121 ? -21.222 60.615  -15.075 1.00 50.12 ? 121 ARG A CZ    1 
ATOM   7005  N NH1   . ARG C  1 121 ? -21.954 61.363  -15.889 1.00 52.11 ? 121 ARG A NH1   1 
ATOM   7006  N NH2   . ARG C  1 121 ? -20.579 59.557  -15.563 1.00 47.47 ? 121 ARG A NH2   1 
ATOM   7007  N N     . LYS C  1 122 ? -23.038 63.422  -8.221  1.00 36.40 ? 122 LYS A N     1 
ATOM   7008  C CA    . LYS C  1 122 ? -22.993 64.636  -7.405  1.00 35.14 ? 122 LYS A CA    1 
ATOM   7009  C C     . LYS C  1 122 ? -22.183 64.435  -6.126  1.00 38.24 ? 122 LYS A C     1 
ATOM   7010  O O     . LYS C  1 122 ? -21.305 65.242  -5.799  1.00 38.37 ? 122 LYS A O     1 
ATOM   7011  C CB    . LYS C  1 122 ? -24.415 65.084  -7.066  1.00 38.36 ? 122 LYS A CB    1 
ATOM   7012  C CG    . LYS C  1 122 ? -25.185 65.624  -8.259  1.00 39.29 ? 122 LYS A CG    1 
ATOM   7013  C CD    . LYS C  1 122 ? -24.695 67.010  -8.621  1.00 38.50 ? 122 LYS A CD    1 
ATOM   7014  C CE    . LYS C  1 122 ? -25.615 67.693  -9.606  1.00 35.94 ? 122 LYS A CE    1 
ATOM   7015  N NZ    . LYS C  1 122 ? -25.046 69.021  -9.958  1.00 38.48 ? 122 LYS A NZ    1 
ATOM   7016  N N     . LEU C  1 123 ? -22.461 63.358  -5.387  1.00 37.70 ? 123 LEU A N     1 
ATOM   7017  C CA    . LEU C  1 123 ? -21.760 63.079  -4.134  1.00 37.66 ? 123 LEU A CA    1 
ATOM   7018  C C     . LEU C  1 123 ? -20.405 62.409  -4.336  1.00 36.18 ? 123 LEU A C     1 
ATOM   7019  O O     . LEU C  1 123 ? -19.711 62.138  -3.346  1.00 32.06 ? 123 LEU A O     1 
ATOM   7020  C CB    . LEU C  1 123 ? -22.639 62.201  -3.238  1.00 32.44 ? 123 LEU A CB    1 
ATOM   7021  C CG    . LEU C  1 123 ? -23.984 62.795  -2.801  1.00 38.49 ? 123 LEU A CG    1 
ATOM   7022  C CD1   . LEU C  1 123 ? -24.911 61.695  -2.305  1.00 35.16 ? 123 LEU A CD1   1 
ATOM   7023  C CD2   . LEU C  1 123 ? -23.807 63.881  -1.710  1.00 34.80 ? 123 LEU A CD2   1 
ATOM   7024  N N     . ASN C  1 124 ? -20.037 62.134  -5.588  1.00 36.84 ? 124 ASN A N     1 
ATOM   7025  C CA    . ASN C  1 124 ? -18.839 61.385  -5.953  1.00 35.56 ? 124 ASN A CA    1 
ATOM   7026  C C     . ASN C  1 124 ? -18.617 60.201  -5.024  1.00 33.51 ? 124 ASN A C     1 
ATOM   7027  O O     . ASN C  1 124 ? -17.554 60.020  -4.434  1.00 36.04 ? 124 ASN A O     1 
ATOM   7028  C CB    . ASN C  1 124 ? -17.622 62.299  -5.998  1.00 39.68 ? 124 ASN A CB    1 
ATOM   7029  C CG    . ASN C  1 124 ? -17.132 62.510  -7.423  1.00 51.74 ? 124 ASN A CG    1 
ATOM   7030  O OD1   . ASN C  1 124 ? -16.981 61.548  -8.188  1.00 48.53 ? 124 ASN A OD1   1 
ATOM   7031  N ND2   . ASN C  1 124 ? -16.951 63.777  -7.811  1.00 49.88 ? 124 ASN A ND2   1 
ATOM   7032  N N     . VAL C  1 125 ? -19.657 59.402  -4.868  1.00 29.95 ? 125 VAL A N     1 
ATOM   7033  C CA    . VAL C  1 125 ? -19.535 58.148  -4.146  1.00 33.82 ? 125 VAL A CA    1 
ATOM   7034  C C     . VAL C  1 125 ? -19.360 57.086  -5.221  1.00 32.26 ? 125 VAL A C     1 
ATOM   7035  O O     . VAL C  1 125 ? -19.345 57.417  -6.412  1.00 36.54 ? 125 VAL A O     1 
ATOM   7036  C CB    . VAL C  1 125 ? -20.767 57.908  -3.253  1.00 35.30 ? 125 VAL A CB    1 
ATOM   7037  C CG1   . VAL C  1 125 ? -20.730 58.840  -2.067  1.00 31.58 ? 125 VAL A CG1   1 
ATOM   7038  C CG2   . VAL C  1 125 ? -22.053 58.128  -4.052  1.00 30.70 ? 125 VAL A CG2   1 
ATOM   7039  N N     . ALA C  1 126 ? -19.216 55.820  -4.829  1.00 31.88 ? 126 ALA A N     1 
ATOM   7040  C CA    . ALA C  1 126 ? -19.105 54.749  -5.818  1.00 26.17 ? 126 ALA A CA    1 
ATOM   7041  C C     . ALA C  1 126 ? -20.287 54.789  -6.781  1.00 27.93 ? 126 ALA A C     1 
ATOM   7042  O O     . ALA C  1 126 ? -21.440 54.901  -6.356  1.00 32.51 ? 126 ALA A O     1 
ATOM   7043  C CB    . ALA C  1 126 ? -19.048 53.392  -5.124  1.00 26.10 ? 126 ALA A CB    1 
ATOM   7044  N N     . ALA C  1 127 ? -20.000 54.720  -8.080  1.00 28.57 ? 127 ALA A N     1 
ATOM   7045  C CA    . ALA C  1 127 ? -21.049 54.820  -9.093  1.00 32.73 ? 127 ALA A CA    1 
ATOM   7046  C C     . ALA C  1 127 ? -22.085 53.718  -8.934  1.00 33.83 ? 127 ALA A C     1 
ATOM   7047  O O     . ALA C  1 127 ? -21.753 52.568  -8.626  1.00 33.01 ? 127 ALA A O     1 
ATOM   7048  C CB    . ALA C  1 127 ? -20.456 54.746  -10.494 1.00 30.90 ? 127 ALA A CB    1 
ATOM   7049  N N     . LEU C  1 128 ? -23.350 54.088  -9.139  1.00 32.22 ? 128 LEU A N     1 
ATOM   7050  C CA    . LEU C  1 128 ? -24.449 53.138  -9.038  1.00 34.21 ? 128 LEU A CA    1 
ATOM   7051  C C     . LEU C  1 128 ? -24.263 52.041  -10.071 1.00 36.44 ? 128 LEU A C     1 
ATOM   7052  O O     . LEU C  1 128 ? -24.096 52.328  -11.257 1.00 38.27 ? 128 LEU A O     1 
ATOM   7053  C CB    . LEU C  1 128 ? -25.777 53.855  -9.266  1.00 38.00 ? 128 LEU A CB    1 
ATOM   7054  C CG    . LEU C  1 128 ? -27.074 53.086  -9.032  1.00 37.89 ? 128 LEU A CG    1 
ATOM   7055  C CD1   . LEU C  1 128 ? -26.912 52.082  -7.885  1.00 41.99 ? 128 LEU A CD1   1 
ATOM   7056  C CD2   . LEU C  1 128 ? -28.196 54.066  -8.741  1.00 31.98 ? 128 LEU A CD2   1 
ATOM   7057  N N     . ASP C  1 129 ? -24.267 50.784  -9.627  1.00 34.98 ? 129 ASP A N     1 
ATOM   7058  C CA    . ASP C  1 129 ? -23.999 49.698  -10.564 1.00 33.41 ? 129 ASP A CA    1 
ATOM   7059  C C     . ASP C  1 129 ? -25.107 49.622  -11.605 1.00 32.00 ? 129 ASP A C     1 
ATOM   7060  O O     . ASP C  1 129 ? -26.292 49.640  -11.266 1.00 38.26 ? 129 ASP A O     1 
ATOM   7061  C CB    . ASP C  1 129 ? -23.860 48.367  -9.841  1.00 31.21 ? 129 ASP A CB    1 
ATOM   7062  C CG    . ASP C  1 129 ? -23.266 47.304  -10.729 1.00 35.23 ? 129 ASP A CG    1 
ATOM   7063  O OD1   . ASP C  1 129 ? -22.994 47.606  -11.912 1.00 32.93 ? 129 ASP A OD1   1 
ATOM   7064  O OD2   . ASP C  1 129 ? -23.069 46.168  -10.253 1.00 39.05 ? 129 ASP A OD2   1 
ATOM   7065  N N     . GLY C  1 130 ? -24.724 49.539  -12.873 1.00 36.09 ? 130 GLY A N     1 
ATOM   7066  C CA    . GLY C  1 130 ? -25.692 49.693  -13.946 1.00 35.43 ? 130 GLY A CA    1 
ATOM   7067  C C     . GLY C  1 130 ? -26.070 51.134  -14.199 1.00 34.60 ? 130 GLY A C     1 
ATOM   7068  O O     . GLY C  1 130 ? -27.197 51.407  -14.659 1.00 30.94 ? 130 GLY A O     1 
ATOM   7069  N N     . TYR C  1 131 ? -25.144 52.059  -13.904 1.00 31.07 ? 131 TYR A N     1 
ATOM   7070  C CA    . TYR C  1 131 ? -25.361 53.498  -13.997 1.00 31.46 ? 131 TYR A CA    1 
ATOM   7071  C C     . TYR C  1 131 ? -26.072 53.873  -15.295 1.00 38.16 ? 131 TYR A C     1 
ATOM   7072  O O     . TYR C  1 131 ? -27.114 54.541  -15.278 1.00 39.09 ? 131 TYR A O     1 
ATOM   7073  C CB    . TYR C  1 131 ? -23.994 54.186  -13.871 1.00 28.07 ? 131 TYR A CB    1 
ATOM   7074  C CG    . TYR C  1 131 ? -23.979 55.691  -13.923 1.00 31.51 ? 131 TYR A CG    1 
ATOM   7075  C CD1   . TYR C  1 131 ? -24.523 56.448  -12.910 1.00 36.62 ? 131 TYR A CD1   1 
ATOM   7076  C CD2   . TYR C  1 131 ? -23.378 56.354  -14.964 1.00 36.68 ? 131 TYR A CD2   1 
ATOM   7077  C CE1   . TYR C  1 131 ? -24.500 57.828  -12.958 1.00 32.68 ? 131 TYR A CE1   1 
ATOM   7078  C CE2   . TYR C  1 131 ? -23.342 57.727  -15.013 1.00 40.15 ? 131 TYR A CE2   1 
ATOM   7079  C CZ    . TYR C  1 131 ? -23.904 58.459  -14.011 1.00 37.24 ? 131 TYR A CZ    1 
ATOM   7080  O OH    . TYR C  1 131 ? -23.866 59.840  -14.076 1.00 47.81 ? 131 TYR A OH    1 
ATOM   7081  N N     . GLU C  1 132 ? -25.548 53.377  -16.427 1.00 35.28 ? 132 GLU A N     1 
ATOM   7082  C CA    . GLU C  1 132 ? -26.056 53.731  -17.755 1.00 31.41 ? 132 GLU A CA    1 
ATOM   7083  C C     . GLU C  1 132 ? -27.492 53.279  -17.980 1.00 32.30 ? 132 GLU A C     1 
ATOM   7084  O O     . GLU C  1 132 ? -28.279 53.984  -18.621 1.00 30.22 ? 132 GLU A O     1 
ATOM   7085  C CB    . GLU C  1 132 ? -25.156 53.112  -18.817 1.00 36.47 ? 132 GLU A CB    1 
ATOM   7086  C CG    . GLU C  1 132 ? -23.709 53.424  -18.600 1.00 35.54 ? 132 GLU A CG    1 
ATOM   7087  C CD    . GLU C  1 132 ? -23.450 54.893  -18.893 1.00 44.00 ? 132 GLU A CD    1 
ATOM   7088  O OE1   . GLU C  1 132 ? -24.053 55.402  -19.864 1.00 52.07 ? 132 GLU A OE1   1 
ATOM   7089  O OE2   . GLU C  1 132 ? -22.680 55.551  -18.154 1.00 46.14 ? 132 GLU A OE2   1 
ATOM   7090  N N     . PHE C  1 133 ? -27.822 52.071  -17.531 1.00 33.59 ? 133 PHE A N     1 
ATOM   7091  C CA    . PHE C  1 133 ? -29.185 51.584  -17.635 1.00 27.67 ? 133 PHE A CA    1 
ATOM   7092  C C     . PHE C  1 133 ? -30.139 52.490  -16.876 1.00 33.19 ? 133 PHE A C     1 
ATOM   7093  O O     . PHE C  1 133 ? -31.259 52.751  -17.338 1.00 29.58 ? 133 PHE A O     1 
ATOM   7094  C CB    . PHE C  1 133 ? -29.240 50.166  -17.095 1.00 25.23 ? 133 PHE A CB    1 
ATOM   7095  C CG    . PHE C  1 133 ? -30.516 49.469  -17.380 1.00 29.07 ? 133 PHE A CG    1 
ATOM   7096  C CD1   . PHE C  1 133 ? -30.927 49.268  -18.687 1.00 25.80 ? 133 PHE A CD1   1 
ATOM   7097  C CD2   . PHE C  1 133 ? -31.300 48.983  -16.340 1.00 23.00 ? 133 PHE A CD2   1 
ATOM   7098  C CE1   . PHE C  1 133 ? -32.096 48.619  -18.936 1.00 27.05 ? 133 PHE A CE1   1 
ATOM   7099  C CE2   . PHE C  1 133 ? -32.468 48.324  -16.596 1.00 22.89 ? 133 PHE A CE2   1 
ATOM   7100  C CZ    . PHE C  1 133 ? -32.867 48.137  -17.881 1.00 24.45 ? 133 PHE A CZ    1 
ATOM   7101  N N     . ALA C  1 134 ? -29.695 53.002  -15.715 1.00 28.47 ? 134 ALA A N     1 
ATOM   7102  C CA    . ALA C  1 134 ? -30.570 53.779  -14.840 1.00 30.31 ? 134 ALA A CA    1 
ATOM   7103  C C     . ALA C  1 134 ? -30.858 55.155  -15.425 1.00 32.84 ? 134 ALA A C     1 
ATOM   7104  O O     . ALA C  1 134 ? -32.018 55.571  -15.498 1.00 34.67 ? 134 ALA A O     1 
ATOM   7105  C CB    . ALA C  1 134 ? -29.947 53.898  -13.449 1.00 34.40 ? 134 ALA A CB    1 
ATOM   7106  N N     . MET C  1 135 ? -29.814 55.898  -15.806 1.00 32.84 ? 135 MET A N     1 
ATOM   7107  C CA    . MET C  1 135 ? -29.967 56.868  -16.883 1.00 36.57 ? 135 MET A CA    1 
ATOM   7108  C C     . MET C  1 135 ? -30.660 56.186  -18.051 1.00 32.82 ? 135 MET A C     1 
ATOM   7109  O O     . MET C  1 135 ? -30.530 54.980  -18.235 1.00 39.82 ? 135 MET A O     1 
ATOM   7110  C CB    . MET C  1 135 ? -28.599 57.380  -17.313 1.00 32.74 ? 135 MET A CB    1 
ATOM   7111  C CG    . MET C  1 135 ? -27.686 57.533  -16.141 1.00 32.94 ? 135 MET A CG    1 
ATOM   7112  S SD    . MET C  1 135 ? -28.157 58.977  -15.163 1.00 39.91 ? 135 MET A SD    1 
ATOM   7113  C CE    . MET C  1 135 ? -26.899 60.133  -15.655 1.00 37.42 ? 135 MET A CE    1 
ATOM   7114  N N     . GLN C  1 136 ? -31.419 56.937  -18.833 1.00 29.72 ? 136 GLN A N     1 
ATOM   7115  C CA    . GLN C  1 136 ? -32.299 56.328  -19.842 1.00 33.35 ? 136 GLN A CA    1 
ATOM   7116  C C     . GLN C  1 136 ? -33.445 55.581  -19.174 1.00 35.74 ? 136 GLN A C     1 
ATOM   7117  O O     . GLN C  1 136 ? -34.345 55.094  -19.865 1.00 38.25 ? 136 GLN A O     1 
ATOM   7118  C CB    . GLN C  1 136 ? -31.593 55.339  -20.796 1.00 34.23 ? 136 GLN A CB    1 
ATOM   7119  C CG    . GLN C  1 136 ? -30.212 55.707  -21.316 1.00 29.27 ? 136 GLN A CG    1 
ATOM   7120  C CD    . GLN C  1 136 ? -30.213 57.043  -22.033 1.00 32.40 ? 136 GLN A CD    1 
ATOM   7121  O OE1   . GLN C  1 136 ? -31.123 57.360  -22.807 1.00 29.84 ? 136 GLN A OE1   1 
ATOM   7122  N NE2   . GLN C  1 136 ? -29.189 57.841  -21.774 1.00 32.46 ? 136 GLN A NE2   1 
ATOM   7123  N N     . ASN C  1 137 ? -33.408 55.460  -17.845 1.00 29.18 ? 137 ASN A N     1 
ATOM   7124  C CA    . ASN C  1 137 ? -34.547 54.998  -17.052 1.00 29.12 ? 137 ASN A CA    1 
ATOM   7125  C C     . ASN C  1 137 ? -34.911 53.562  -17.379 1.00 28.03 ? 137 ASN A C     1 
ATOM   7126  O O     . ASN C  1 137 ? -36.081 53.218  -17.570 1.00 28.20 ? 137 ASN A O     1 
ATOM   7127  C CB    . ASN C  1 137 ? -35.733 55.939  -17.215 1.00 25.56 ? 137 ASN A CB    1 
ATOM   7128  C CG    . ASN C  1 137 ? -35.279 57.373  -17.233 1.00 30.09 ? 137 ASN A CG    1 
ATOM   7129  O OD1   . ASN C  1 137 ? -34.173 57.676  -16.779 1.00 36.13 ? 137 ASN A OD1   1 
ATOM   7130  N ND2   . ASN C  1 137 ? -36.097 58.257  -17.756 1.00 35.87 ? 137 ASN A ND2   1 
ATOM   7131  N N     . GLY C  1 138 ? -33.879 52.719  -17.403 1.00 26.89 ? 138 GLY A N     1 
ATOM   7132  C CA    . GLY C  1 138 ? -34.019 51.286  -17.509 1.00 23.38 ? 138 GLY A CA    1 
ATOM   7133  C C     . GLY C  1 138 ? -35.048 50.716  -16.572 1.00 27.42 ? 138 GLY A C     1 
ATOM   7134  O O     . GLY C  1 138 ? -36.057 50.174  -17.033 1.00 27.70 ? 138 GLY A O     1 
ATOM   7135  N N     . ILE C  1 139 ? -34.845 50.872  -15.260 1.00 29.90 ? 139 ILE A N     1 
ATOM   7136  C CA    . ILE C  1 139 ? -35.690 50.172  -14.295 1.00 28.95 ? 139 ILE A CA    1 
ATOM   7137  C C     . ILE C  1 139 ? -37.148 50.537  -14.499 1.00 28.88 ? 139 ILE A C     1 
ATOM   7138  O O     . ILE C  1 139 ? -38.045 49.754  -14.161 1.00 30.32 ? 139 ILE A O     1 
ATOM   7139  C CB    . ILE C  1 139 ? -35.225 50.429  -12.841 1.00 29.14 ? 139 ILE A CB    1 
ATOM   7140  C CG1   . ILE C  1 139 ? -35.643 51.803  -12.348 1.00 31.43 ? 139 ILE A CG1   1 
ATOM   7141  C CG2   . ILE C  1 139 ? -33.712 50.326  -12.748 1.00 26.52 ? 139 ILE A CG2   1 
ATOM   7142  C CD1   . ILE C  1 139 ? -37.038 51.850  -11.752 1.00 35.86 ? 139 ILE A CD1   1 
ATOM   7143  N N     . ASP C  1 140 ? -37.423 51.729  -15.029 1.00 28.55 ? 140 ASP A N     1 
ATOM   7144  C CA    . ASP C  1 140 ? -38.796 52.071  -15.362 1.00 27.60 ? 140 ASP A CA    1 
ATOM   7145  C C     . ASP C  1 140 ? -39.365 51.153  -16.428 1.00 31.62 ? 140 ASP A C     1 
ATOM   7146  O O     . ASP C  1 140 ? -40.575 50.892  -16.447 1.00 35.55 ? 140 ASP A O     1 
ATOM   7147  C CB    . ASP C  1 140 ? -38.870 53.504  -15.862 1.00 33.79 ? 140 ASP A CB    1 
ATOM   7148  C CG    . ASP C  1 140 ? -40.290 54.012  -15.947 1.00 36.25 ? 140 ASP A CG    1 
ATOM   7149  O OD1   . ASP C  1 140 ? -40.884 54.257  -14.870 1.00 52.02 ? 140 ASP A OD1   1 
ATOM   7150  O OD2   . ASP C  1 140 ? -40.828 54.128  -17.080 1.00 28.88 ? 140 ASP A OD2   1 
ATOM   7151  N N     . LEU C  1 141 ? -38.525 50.655  -17.326 1.00 30.62 ? 141 LEU A N     1 
ATOM   7152  C CA    . LEU C  1 141 ? -39.037 49.873  -18.443 1.00 28.96 ? 141 LEU A CA    1 
ATOM   7153  C C     . LEU C  1 141 ? -39.493 48.510  -17.966 1.00 30.81 ? 141 LEU A C     1 
ATOM   7154  O O     . LEU C  1 141 ? -40.610 48.074  -18.268 1.00 36.88 ? 141 LEU A O     1 
ATOM   7155  C CB    . LEU C  1 141 ? -37.964 49.766  -19.514 1.00 28.98 ? 141 LEU A CB    1 
ATOM   7156  C CG    . LEU C  1 141 ? -38.375 48.859  -20.650 1.00 30.84 ? 141 LEU A CG    1 
ATOM   7157  C CD1   . LEU C  1 141 ? -39.614 49.425  -21.329 1.00 31.07 ? 141 LEU A CD1   1 
ATOM   7158  C CD2   . LEU C  1 141 ? -37.209 48.764  -21.612 1.00 35.22 ? 141 LEU A CD2   1 
ATOM   7159  N N     . LEU C  1 142 ? -38.632 47.819  -17.222 1.00 27.18 ? 142 LEU A N     1 
ATOM   7160  C CA    . LEU C  1 142 ? -39.080 46.782  -16.313 1.00 31.36 ? 142 LEU A CA    1 
ATOM   7161  C C     . LEU C  1 142 ? -39.929 47.494  -15.265 1.00 36.04 ? 142 LEU A C     1 
ATOM   7162  O O     . LEU C  1 142 ? -40.043 48.718  -15.269 1.00 42.25 ? 142 LEU A O     1 
ATOM   7163  C CB    . LEU C  1 142 ? -37.884 46.071  -15.688 1.00 36.40 ? 142 LEU A CB    1 
ATOM   7164  C CG    . LEU C  1 142 ? -36.636 46.020  -16.581 1.00 37.76 ? 142 LEU A CG    1 
ATOM   7165  C CD1   . LEU C  1 142 ? -35.411 45.749  -15.722 1.00 32.18 ? 142 LEU A CD1   1 
ATOM   7166  C CD2   . LEU C  1 142 ? -36.744 44.999  -17.728 1.00 34.37 ? 142 LEU A CD2   1 
ATOM   7167  N N     . ASN C  1 143 ? -40.518 46.765  -14.338 1.00 33.83 ? 143 ASN A N     1 
ATOM   7168  C CA    . ASN C  1 143 ? -41.491 47.398  -13.423 1.00 36.60 ? 143 ASN A CA    1 
ATOM   7169  C C     . ASN C  1 143 ? -42.641 47.982  -14.232 1.00 32.30 ? 143 ASN A C     1 
ATOM   7170  O O     . ASN C  1 143 ? -43.177 49.045  -13.932 1.00 30.40 ? 143 ASN A O     1 
ATOM   7171  C CB    . ASN C  1 143 ? -40.859 48.493  -12.549 1.00 24.93 ? 143 ASN A CB    1 
ATOM   7172  C CG    . ASN C  1 143 ? -39.775 47.967  -11.675 1.00 28.91 ? 143 ASN A CG    1 
ATOM   7173  O OD1   . ASN C  1 143 ? -39.587 46.769  -11.565 1.00 32.93 ? 143 ASN A OD1   1 
ATOM   7174  N ND2   . ASN C  1 143 ? -38.973 48.878  -11.116 1.00 31.54 ? 143 ASN A ND2   1 
ATOM   7175  N N     . MET C  1 144 ? -42.927 47.324  -15.339 1.00 35.46 ? 144 MET A N     1 
ATOM   7176  C CA    . MET C  1 144 ? -44.100 47.592  -16.140 1.00 29.60 ? 144 MET A CA    1 
ATOM   7177  C C     . MET C  1 144 ? -44.702 46.239  -16.430 1.00 30.87 ? 144 MET A C     1 
ATOM   7178  O O     . MET C  1 144 ? -44.014 45.354  -16.946 1.00 33.39 ? 144 MET A O     1 
ATOM   7179  C CB    . MET C  1 144 ? -43.767 48.291  -17.447 1.00 34.74 ? 144 MET A CB    1 
ATOM   7180  C CG    . MET C  1 144 ? -43.726 49.774  -17.413 1.00 31.85 ? 144 MET A CG    1 
ATOM   7181  S SD    . MET C  1 144 ? -43.204 50.291  -19.054 1.00 32.00 ? 144 MET A SD    1 
ATOM   7182  C CE    . MET C  1 144 ? -44.660 49.953  -20.027 1.00 30.29 ? 144 MET A CE    1 
ATOM   7183  N N     . LYS C  1 145 ? -45.962 46.057  -16.078 1.00 30.02 ? 145 LYS A N     1 
ATOM   7184  C CA    . LYS C  1 145 ? -46.525 44.733  -16.273 1.00 30.46 ? 145 LYS A CA    1 
ATOM   7185  C C     . LYS C  1 145 ? -46.555 44.373  -17.750 1.00 29.60 ? 145 LYS A C     1 
ATOM   7186  O O     . LYS C  1 145 ? -46.211 43.242  -18.121 1.00 33.26 ? 145 LYS A O     1 
ATOM   7187  C CB    . LYS C  1 145 ? -47.902 44.652  -15.609 1.00 39.78 ? 145 LYS A CB    1 
ATOM   7188  C CG    . LYS C  1 145 ? -47.778 44.836  -14.082 1.00 41.82 ? 145 LYS A CG    1 
ATOM   7189  C CD    . LYS C  1 145 ? -48.841 44.151  -13.244 1.00 34.65 ? 145 LYS A CD    1 
ATOM   7190  C CE    . LYS C  1 145 ? -48.421 44.081  -11.754 1.00 41.13 ? 145 LYS A CE    1 
ATOM   7191  N NZ    . LYS C  1 145 ? -48.113 45.404  -11.115 1.00 41.34 ? 145 LYS A NZ    1 
ATOM   7192  N N     . SER C  1 146 ? -46.891 45.336  -18.610 1.00 28.68 ? 146 SER A N     1 
ATOM   7193  C CA    . SER C  1 146 ? -46.867 45.085  -20.050 1.00 28.77 ? 146 SER A CA    1 
ATOM   7194  C C     . SER C  1 146 ? -45.493 44.610  -20.507 1.00 30.81 ? 146 SER A C     1 
ATOM   7195  O O     . SER C  1 146 ? -45.386 43.732  -21.372 1.00 27.33 ? 146 SER A O     1 
ATOM   7196  C CB    . SER C  1 146 ? -47.262 46.351  -20.795 1.00 25.33 ? 146 SER A CB    1 
ATOM   7197  O OG    . SER C  1 146 ? -46.259 47.331  -20.604 1.00 28.98 ? 146 SER A OG    1 
ATOM   7198  N N     . THR C  1 147 ? -44.423 45.165  -19.924 1.00 28.87 ? 147 THR A N     1 
ATOM   7199  C CA    . THR C  1 147 ? -43.093 44.684  -20.280 1.00 27.29 ? 147 THR A CA    1 
ATOM   7200  C C     . THR C  1 147 ? -42.924 43.236  -19.864 1.00 31.45 ? 147 THR A C     1 
ATOM   7201  O O     . THR C  1 147 ? -42.411 42.418  -20.636 1.00 34.64 ? 147 THR A O     1 
ATOM   7202  C CB    . THR C  1 147 ? -42.001 45.526  -19.640 1.00 29.38 ? 147 THR A CB    1 
ATOM   7203  O OG1   . THR C  1 147 ? -42.159 46.900  -20.007 1.00 32.51 ? 147 THR A OG1   1 
ATOM   7204  C CG2   . THR C  1 147 ? -40.647 45.034  -20.148 1.00 23.55 ? 147 THR A CG2   1 
ATOM   7205  N N     . PHE C  1 148 ? -43.361 42.893  -18.654 1.00 25.81 ? 148 PHE A N     1 
ATOM   7206  C CA    . PHE C  1 148 ? -43.221 41.515  -18.215 1.00 25.56 ? 148 PHE A CA    1 
ATOM   7207  C C     . PHE C  1 148 ? -43.971 40.570  -19.139 1.00 30.71 ? 148 PHE A C     1 
ATOM   7208  O O     . PHE C  1 148 ? -43.380 39.641  -19.703 1.00 34.68 ? 148 PHE A O     1 
ATOM   7209  C CB    . PHE C  1 148 ? -43.711 41.335  -16.787 1.00 27.32 ? 148 PHE A CB    1 
ATOM   7210  C CG    . PHE C  1 148 ? -43.714 39.896  -16.344 1.00 26.67 ? 148 PHE A CG    1 
ATOM   7211  C CD1   . PHE C  1 148 ? -42.561 39.308  -15.864 1.00 26.30 ? 148 PHE A CD1   1 
ATOM   7212  C CD2   . PHE C  1 148 ? -44.864 39.115  -16.453 1.00 29.21 ? 148 PHE A CD2   1 
ATOM   7213  C CE1   . PHE C  1 148 ? -42.562 37.969  -15.476 1.00 29.58 ? 148 PHE A CE1   1 
ATOM   7214  C CE2   . PHE C  1 148 ? -44.871 37.784  -16.068 1.00 24.58 ? 148 PHE A CE2   1 
ATOM   7215  C CZ    . PHE C  1 148 ? -43.728 37.207  -15.587 1.00 30.33 ? 148 PHE A CZ    1 
ATOM   7216  N N     . ARG C  1 149 ? -45.282 40.783  -19.304 1.00 27.72 ? 149 ARG A N     1 
ATOM   7217  C CA    . ARG C  1 149 ? -46.055 39.888  -20.160 1.00 29.68 ? 149 ARG A CA    1 
ATOM   7218  C C     . ARG C  1 149 ? -45.383 39.714  -21.502 1.00 30.07 ? 149 ARG A C     1 
ATOM   7219  O O     . ARG C  1 149 ? -45.441 38.627  -22.089 1.00 31.66 ? 149 ARG A O     1 
ATOM   7220  C CB    . ARG C  1 149 ? -47.476 40.417  -20.374 1.00 33.62 ? 149 ARG A CB    1 
ATOM   7221  C CG    . ARG C  1 149 ? -48.345 40.377  -19.129 1.00 33.29 ? 149 ARG A CG    1 
ATOM   7222  C CD    . ARG C  1 149 ? -49.816 40.169  -19.432 1.00 28.69 ? 149 ARG A CD    1 
ATOM   7223  N NE    . ARG C  1 149 ? -50.068 39.119  -20.407 1.00 31.19 ? 149 ARG A NE    1 
ATOM   7224  C CZ    . ARG C  1 149 ? -50.462 37.889  -20.106 1.00 34.58 ? 149 ARG A CZ    1 
ATOM   7225  N NH1   . ARG C  1 149 ? -50.588 37.489  -18.850 1.00 33.52 ? 149 ARG A NH1   1 
ATOM   7226  N NH2   . ARG C  1 149 ? -50.737 37.038  -21.091 1.00 34.89 ? 149 ARG A NH2   1 
ATOM   7227  N N     . ARG C  1 150 ? -44.722 40.766  -21.992 1.00 24.13 ? 150 ARG A N     1 
ATOM   7228  C CA    . ARG C  1 150 ? -44.085 40.688  -23.300 1.00 26.41 ? 150 ARG A CA    1 
ATOM   7229  C C     . ARG C  1 150 ? -42.833 39.820  -23.236 1.00 27.45 ? 150 ARG A C     1 
ATOM   7230  O O     . ARG C  1 150 ? -42.704 38.830  -23.968 1.00 25.01 ? 150 ARG A O     1 
ATOM   7231  C CB    . ARG C  1 150 ? -43.758 42.095  -23.813 1.00 25.61 ? 150 ARG A CB    1 
ATOM   7232  C CG    . ARG C  1 150 ? -44.935 42.804  -24.487 1.00 26.97 ? 150 ARG A CG    1 
ATOM   7233  C CD    . ARG C  1 150 ? -44.820 44.338  -24.499 1.00 28.79 ? 150 ARG A CD    1 
ATOM   7234  N NE    . ARG C  1 150 ? -45.837 44.975  -25.339 1.00 30.91 ? 150 ARG A NE    1 
ATOM   7235  C CZ    . ARG C  1 150 ? -45.896 46.275  -25.613 1.00 32.72 ? 150 ARG A CZ    1 
ATOM   7236  N NH1   . ARG C  1 150 ? -44.997 47.125  -25.144 1.00 30.76 ? 150 ARG A NH1   1 
ATOM   7237  N NH2   . ARG C  1 150 ? -46.875 46.735  -26.390 1.00 30.39 ? 150 ARG A NH2   1 
ATOM   7238  N N     . LEU C  1 151 ? -41.910 40.153  -22.343 1.00 27.63 ? 151 LEU A N     1 
ATOM   7239  C CA    . LEU C  1 151 ? -40.690 39.373  -22.269 1.00 24.67 ? 151 LEU A CA    1 
ATOM   7240  C C     . LEU C  1 151 ? -41.006 37.914  -21.985 1.00 28.12 ? 151 LEU A C     1 
ATOM   7241  O O     . LEU C  1 151 ? -40.502 37.017  -22.667 1.00 29.70 ? 151 LEU A O     1 
ATOM   7242  C CB    . LEU C  1 151 ? -39.768 39.947  -21.207 1.00 26.40 ? 151 LEU A CB    1 
ATOM   7243  C CG    . LEU C  1 151 ? -39.430 41.433  -21.267 1.00 25.12 ? 151 LEU A CG    1 
ATOM   7244  C CD1   . LEU C  1 151 ? -38.445 41.744  -20.185 1.00 27.70 ? 151 LEU A CD1   1 
ATOM   7245  C CD2   . LEU C  1 151 ? -38.831 41.807  -22.553 1.00 21.92 ? 151 LEU A CD2   1 
ATOM   7246  N N     . ALA C  1 152 ? -41.873 37.658  -21.007 1.00 23.97 ? 152 ALA A N     1 
ATOM   7247  C CA    . ALA C  1 152 ? -42.118 36.280  -20.599 1.00 27.79 ? 152 ALA A CA    1 
ATOM   7248  C C     . ALA C  1 152 ? -42.743 35.485  -21.725 1.00 32.35 ? 152 ALA A C     1 
ATOM   7249  O O     . ALA C  1 152 ? -42.398 34.314  -21.945 1.00 32.89 ? 152 ALA A O     1 
ATOM   7250  C CB    . ALA C  1 152 ? -43.023 36.236  -19.370 1.00 34.35 ? 152 ALA A CB    1 
ATOM   7251  N N     . ALA C  1 153 ? -43.678 36.097  -22.447 1.00 30.98 ? 153 ALA A N     1 
ATOM   7252  C CA    . ALA C  1 153 ? -44.157 35.465  -23.664 1.00 25.15 ? 153 ALA A CA    1 
ATOM   7253  C C     . ALA C  1 153 ? -43.010 35.251  -24.649 1.00 25.96 ? 153 ALA A C     1 
ATOM   7254  O O     . ALA C  1 153 ? -42.949 34.225  -25.326 1.00 30.47 ? 153 ALA A O     1 
ATOM   7255  C CB    . ALA C  1 153 ? -45.269 36.307  -24.286 1.00 25.52 ? 153 ALA A CB    1 
ATOM   7256  N N     . GLY C  1 154 ? -42.087 36.199  -24.748 1.00 23.37 ? 154 GLY A N     1 
ATOM   7257  C CA    . GLY C  1 154 ? -40.998 36.006  -25.687 1.00 28.33 ? 154 GLY A CA    1 
ATOM   7258  C C     . GLY C  1 154 ? -40.146 34.807  -25.322 1.00 31.91 ? 154 GLY A C     1 
ATOM   7259  O O     . GLY C  1 154 ? -39.954 33.891  -26.131 1.00 33.78 ? 154 GLY A O     1 
ATOM   7260  N N     . LEU C  1 155 ? -39.654 34.786  -24.077 1.00 28.33 ? 155 LEU A N     1 
ATOM   7261  C CA    . LEU C  1 155 ? -38.760 33.728  -23.629 1.00 30.40 ? 155 LEU A CA    1 
ATOM   7262  C C     . LEU C  1 155 ? -39.439 32.363  -23.635 1.00 33.34 ? 155 LEU A C     1 
ATOM   7263  O O     . LEU C  1 155 ? -38.789 31.347  -23.901 1.00 37.67 ? 155 LEU A O     1 
ATOM   7264  C CB    . LEU C  1 155 ? -38.243 34.055  -22.224 1.00 30.33 ? 155 LEU A CB    1 
ATOM   7265  C CG    . LEU C  1 155 ? -37.148 33.112  -21.718 1.00 31.01 ? 155 LEU A CG    1 
ATOM   7266  C CD1   . LEU C  1 155 ? -36.124 32.926  -22.788 1.00 27.75 ? 155 LEU A CD1   1 
ATOM   7267  C CD2   . LEU C  1 155 ? -36.488 33.602  -20.458 1.00 32.93 ? 155 LEU A CD2   1 
ATOM   7268  N N     . GLY C  1 156 ? -40.734 32.319  -23.363 1.00 31.44 ? 156 GLY A N     1 
ATOM   7269  C CA    . GLY C  1 156 ? -41.380 31.100  -22.943 1.00 28.46 ? 156 GLY A CA    1 
ATOM   7270  C C     . GLY C  1 156 ? -41.553 30.971  -21.446 1.00 34.63 ? 156 GLY A C     1 
ATOM   7271  O O     . GLY C  1 156 ? -41.833 29.865  -20.968 1.00 37.30 ? 156 GLY A O     1 
ATOM   7272  N N     . THR C  1 157 ? -41.376 32.046  -20.689 1.00 29.07 ? 157 THR A N     1 
ATOM   7273  C CA    . THR C  1 157 ? -41.665 31.989  -19.263 1.00 33.12 ? 157 THR A CA    1 
ATOM   7274  C C     . THR C  1 157 ? -43.165 31.875  -19.025 1.00 34.42 ? 157 THR A C     1 
ATOM   7275  O O     . THR C  1 157 ? -43.913 32.768  -19.438 1.00 38.85 ? 157 THR A O     1 
ATOM   7276  C CB    . THR C  1 157 ? -41.147 33.211  -18.558 1.00 32.00 ? 157 THR A CB    1 
ATOM   7277  O OG1   . THR C  1 157 ? -39.905 33.603  -19.148 1.00 37.89 ? 157 THR A OG1   1 
ATOM   7278  C CG2   . THR C  1 157 ? -40.917 32.869  -17.115 1.00 28.64 ? 157 THR A CG2   1 
ATOM   7279  N N     . PRO C  1 158 ? -43.637 30.829  -18.343 1.00 31.41 ? 158 PRO A N     1 
ATOM   7280  C CA    . PRO C  1 158 ? -45.085 30.568  -18.249 1.00 34.12 ? 158 PRO A CA    1 
ATOM   7281  C C     . PRO C  1 158 ? -45.897 31.727  -17.677 1.00 37.35 ? 158 PRO A C     1 
ATOM   7282  O O     . PRO C  1 158 ? -45.464 32.445  -16.768 1.00 28.94 ? 158 PRO A O     1 
ATOM   7283  C CB    . PRO C  1 158 ? -45.165 29.346  -17.326 1.00 34.33 ? 158 PRO A CB    1 
ATOM   7284  C CG    . PRO C  1 158 ? -43.783 29.178  -16.744 1.00 29.92 ? 158 PRO A CG    1 
ATOM   7285  C CD    . PRO C  1 158 ? -42.834 29.764  -17.731 1.00 32.34 ? 158 PRO A CD    1 
ATOM   7286  N N     . LEU C  1 159 ? -47.133 31.831  -18.171 1.00 40.37 ? 159 LEU A N     1 
ATOM   7287  C CA    . LEU C  1 159 ? -47.916 33.064  -18.138 1.00 36.51 ? 159 LEU A CA    1 
ATOM   7288  C C     . LEU C  1 159 ? -49.380 32.716  -18.392 1.00 37.50 ? 159 LEU A C     1 
ATOM   7289  O O     . LEU C  1 159 ? -49.720 32.227  -19.479 1.00 39.42 ? 159 LEU A O     1 
ATOM   7290  C CB    . LEU C  1 159 ? -47.387 34.017  -19.214 1.00 36.01 ? 159 LEU A CB    1 
ATOM   7291  C CG    . LEU C  1 159 ? -47.511 35.532  -19.214 1.00 33.42 ? 159 LEU A CG    1 
ATOM   7292  C CD1   . LEU C  1 159 ? -46.949 36.052  -17.946 1.00 31.71 ? 159 LEU A CD1   1 
ATOM   7293  C CD2   . LEU C  1 159 ? -46.727 36.068  -20.416 1.00 31.33 ? 159 LEU A CD2   1 
ATOM   7294  N N     . THR C  1 160 ? -50.239 32.966  -17.403 1.00 32.73 ? 160 THR A N     1 
ATOM   7295  C CA    . THR C  1 160 ? -51.686 32.857  -17.573 1.00 32.65 ? 160 THR A CA    1 
ATOM   7296  C C     . THR C  1 160 ? -52.152 33.548  -18.849 1.00 37.47 ? 160 THR A C     1 
ATOM   7297  O O     . THR C  1 160 ? -51.567 34.544  -19.285 1.00 40.96 ? 160 THR A O     1 
ATOM   7298  C CB    . THR C  1 160 ? -52.401 33.500  -16.389 1.00 35.00 ? 160 THR A CB    1 
ATOM   7299  O OG1   . THR C  1 160 ? -52.560 34.896  -16.664 1.00 30.79 ? 160 THR A OG1   1 
ATOM   7300  C CG2   . THR C  1 160 ? -51.570 33.355  -15.123 1.00 42.73 ? 160 THR A CG2   1 
ATOM   7301  N N     . ASP C  1 161 ? -53.235 33.026  -19.434 1.00 35.01 ? 161 ASP A N     1 
ATOM   7302  C CA    . ASP C  1 161 ? -53.844 33.661  -20.594 1.00 34.28 ? 161 ASP A CA    1 
ATOM   7303  C C     . ASP C  1 161 ? -54.109 35.124  -20.291 1.00 31.14 ? 161 ASP A C     1 
ATOM   7304  O O     . ASP C  1 161 ? -54.617 35.466  -19.221 1.00 29.49 ? 161 ASP A O     1 
ATOM   7305  C CB    . ASP C  1 161 ? -55.150 32.959  -20.964 1.00 31.84 ? 161 ASP A CB    1 
ATOM   7306  C CG    . ASP C  1 161 ? -54.928 31.708  -21.768 1.00 42.68 ? 161 ASP A CG    1 
ATOM   7307  O OD1   . ASP C  1 161 ? -53.757 31.294  -21.928 1.00 43.85 ? 161 ASP A OD1   1 
ATOM   7308  O OD2   . ASP C  1 161 ? -55.928 31.127  -22.248 1.00 53.10 ? 161 ASP A OD2   1 
ATOM   7309  N N     . GLY C  1 162 ? -53.729 35.986  -21.220 1.00 28.31 ? 162 GLY A N     1 
ATOM   7310  C CA    . GLY C  1 162 ? -53.999 37.400  -21.061 1.00 31.04 ? 162 GLY A CA    1 
ATOM   7311  C C     . GLY C  1 162 ? -53.575 38.146  -22.303 1.00 34.26 ? 162 GLY A C     1 
ATOM   7312  O O     . GLY C  1 162 ? -52.870 37.611  -23.166 1.00 36.54 ? 162 GLY A O     1 
ATOM   7313  N N     . VAL C  1 163 ? -54.023 39.404  -22.385 1.00 34.72 ? 163 VAL A N     1 
ATOM   7314  C CA    . VAL C  1 163 ? -53.647 40.310  -23.465 1.00 40.13 ? 163 VAL A CA    1 
ATOM   7315  C C     . VAL C  1 163 ? -52.908 41.510  -22.865 1.00 38.21 ? 163 VAL A C     1 
ATOM   7316  O O     . VAL C  1 163 ? -52.924 41.733  -21.656 1.00 39.02 ? 163 VAL A O     1 
ATOM   7317  C CB    . VAL C  1 163 ? -54.860 40.777  -24.309 1.00 35.15 ? 163 VAL A CB    1 
ATOM   7318  C CG1   . VAL C  1 163 ? -55.964 39.740  -24.300 1.00 27.41 ? 163 VAL A CG1   1 
ATOM   7319  C CG2   . VAL C  1 163 ? -55.384 42.117  -23.827 1.00 34.97 ? 163 VAL A CG2   1 
ATOM   7320  N N     . VAL C  1 164 ? -52.226 42.259  -23.732 1.00 34.08 ? 164 VAL A N     1 
ATOM   7321  C CA    . VAL C  1 164 ? -51.727 43.592  -23.413 1.00 32.41 ? 164 VAL A CA    1 
ATOM   7322  C C     . VAL C  1 164 ? -52.663 44.580  -24.100 1.00 36.73 ? 164 VAL A C     1 
ATOM   7323  O O     . VAL C  1 164 ? -52.542 44.846  -25.308 1.00 32.92 ? 164 VAL A O     1 
ATOM   7324  C CB    . VAL C  1 164 ? -50.279 43.784  -23.855 1.00 32.62 ? 164 VAL A CB    1 
ATOM   7325  C CG1   . VAL C  1 164 ? -49.882 45.253  -23.694 1.00 25.35 ? 164 VAL A CG1   1 
ATOM   7326  C CG2   . VAL C  1 164 ? -49.370 42.856  -23.072 1.00 28.75 ? 164 VAL A CG2   1 
ATOM   7327  N N     . ALA C  1 165 ? -53.606 45.117  -23.323 1.00 32.08 ? 165 ALA A N     1 
ATOM   7328  C CA    . ALA C  1 165 ? -54.764 45.815  -23.861 1.00 32.56 ? 165 ALA A CA    1 
ATOM   7329  C C     . ALA C  1 165 ? -54.447 47.276  -24.107 1.00 29.92 ? 165 ALA A C     1 
ATOM   7330  O O     . ALA C  1 165 ? -53.897 47.956  -23.242 1.00 28.13 ? 165 ALA A O     1 
ATOM   7331  C CB    . ALA C  1 165 ? -55.953 45.696  -22.916 1.00 34.00 ? 165 ALA A CB    1 
ATOM   7332  N N     . ARG C  1 166 ? -54.826 47.759  -25.280 1.00 33.89 ? 166 ARG A N     1 
ATOM   7333  C CA    . ARG C  1 166 ? -54.444 49.094  -25.694 1.00 34.76 ? 166 ARG A CA    1 
ATOM   7334  C C     . ARG C  1 166 ? -55.612 50.065  -25.733 1.00 37.41 ? 166 ARG A C     1 
ATOM   7335  O O     . ARG C  1 166 ? -55.402 51.250  -26.014 1.00 33.70 ? 166 ARG A O     1 
ATOM   7336  C CB    . ARG C  1 166 ? -53.736 49.023  -27.043 1.00 32.81 ? 166 ARG A CB    1 
ATOM   7337  C CG    . ARG C  1 166 ? -52.563 48.074  -27.003 1.00 34.65 ? 166 ARG A CG    1 
ATOM   7338  C CD    . ARG C  1 166 ? -52.300 47.495  -28.341 1.00 31.09 ? 166 ARG A CD    1 
ATOM   7339  N NE    . ARG C  1 166 ? -53.351 46.575  -28.745 1.00 35.41 ? 166 ARG A NE    1 
ATOM   7340  C CZ    . ARG C  1 166 ? -53.323 45.895  -29.882 1.00 36.24 ? 166 ARG A CZ    1 
ATOM   7341  N NH1   . ARG C  1 166 ? -52.310 46.007  -30.722 1.00 29.50 ? 166 ARG A NH1   1 
ATOM   7342  N NH2   . ARG C  1 166 ? -54.340 45.090  -30.187 1.00 39.48 ? 166 ARG A NH2   1 
ATOM   7343  N N     . GLY C  1 167 ? -56.825 49.607  -25.416 1.00 38.99 ? 167 GLY A N     1 
ATOM   7344  C CA    . GLY C  1 167 ? -57.975 50.471  -25.288 1.00 35.54 ? 167 GLY A CA    1 
ATOM   7345  C C     . GLY C  1 167 ? -59.147 49.741  -24.666 1.00 35.27 ? 167 GLY A C     1 
ATOM   7346  O O     . GLY C  1 167 ? -59.084 48.536  -24.387 1.00 36.88 ? 167 GLY A O     1 
ATOM   7347  N N     . PRO C  1 168 ? -60.254 50.457  -24.455 1.00 34.45 ? 168 PRO A N     1 
ATOM   7348  C CA    . PRO C  1 168 ? -61.466 49.791  -23.938 1.00 36.43 ? 168 PRO A CA    1 
ATOM   7349  C C     . PRO C  1 168 ? -61.940 48.603  -24.778 1.00 40.38 ? 168 PRO A C     1 
ATOM   7350  O O     . PRO C  1 168 ? -62.295 47.560  -24.207 1.00 39.96 ? 168 PRO A O     1 
ATOM   7351  C CB    . PRO C  1 168 ? -62.497 50.927  -23.919 1.00 35.20 ? 168 PRO A CB    1 
ATOM   7352  C CG    . PRO C  1 168 ? -61.979 51.916  -24.898 1.00 38.55 ? 168 PRO A CG    1 
ATOM   7353  C CD    . PRO C  1 168 ? -60.495 51.866  -24.790 1.00 34.41 ? 168 PRO A CD    1 
ATOM   7354  N N     . ALA C  1 169 ? -61.943 48.714  -26.114 1.00 30.31 ? 169 ALA A N     1 
ATOM   7355  C CA    . ALA C  1 169 ? -62.454 47.614  -26.927 1.00 31.51 ? 169 ALA A CA    1 
ATOM   7356  C C     . ALA C  1 169 ? -61.608 46.361  -26.760 1.00 34.89 ? 169 ALA A C     1 
ATOM   7357  O O     . ALA C  1 169 ? -62.145 45.243  -26.708 1.00 30.98 ? 169 ALA A O     1 
ATOM   7358  C CB    . ALA C  1 169 ? -62.526 48.019  -28.399 1.00 35.92 ? 169 ALA A CB    1 
ATOM   7359  N N     . GLU C  1 170 ? -60.277 46.521  -26.692 1.00 36.65 ? 170 GLU A N     1 
ATOM   7360  C CA    . GLU C  1 170 ? -59.433 45.385  -26.327 1.00 33.79 ? 170 GLU A CA    1 
ATOM   7361  C C     . GLU C  1 170 ? -59.776 44.883  -24.930 1.00 32.13 ? 170 GLU A C     1 
ATOM   7362  O O     . GLU C  1 170 ? -59.835 43.668  -24.704 1.00 31.45 ? 170 GLU A O     1 
ATOM   7363  C CB    . GLU C  1 170 ? -57.941 45.740  -26.427 1.00 35.67 ? 170 GLU A CB    1 
ATOM   7364  C CG    . GLU C  1 170 ? -57.036 44.506  -26.764 1.00 41.12 ? 170 GLU A CG    1 
ATOM   7365  C CD    . GLU C  1 170 ? -55.560 44.845  -27.112 1.00 45.16 ? 170 GLU A CD    1 
ATOM   7366  O OE1   . GLU C  1 170 ? -55.186 46.053  -27.130 1.00 41.17 ? 170 GLU A OE1   1 
ATOM   7367  O OE2   . GLU C  1 170 ? -54.768 43.890  -27.371 1.00 43.31 ? 170 GLU A OE2   1 
ATOM   7368  N N     . VAL C  1 171 ? -60.054 45.797  -23.990 1.00 29.88 ? 171 VAL A N     1 
ATOM   7369  C CA    . VAL C  1 171 ? -60.434 45.374  -22.641 1.00 31.55 ? 171 VAL A CA    1 
ATOM   7370  C C     . VAL C  1 171 ? -61.698 44.515  -22.681 1.00 38.00 ? 171 VAL A C     1 
ATOM   7371  O O     . VAL C  1 171 ? -61.771 43.447  -22.049 1.00 35.82 ? 171 VAL A O     1 
ATOM   7372  C CB    . VAL C  1 171 ? -60.617 46.589  -21.712 1.00 34.16 ? 171 VAL A CB    1 
ATOM   7373  C CG1   . VAL C  1 171 ? -61.130 46.129  -20.349 1.00 28.12 ? 171 VAL A CG1   1 
ATOM   7374  C CG2   . VAL C  1 171 ? -59.307 47.361  -21.529 1.00 31.93 ? 171 VAL A CG2   1 
ATOM   7375  N N     . ARG C  1 172 ? -62.715 44.963  -23.422 1.00 33.01 ? 172 ARG A N     1 
ATOM   7376  C CA    . ARG C  1 172 ? -63.988 44.247  -23.431 1.00 37.80 ? 172 ARG A CA    1 
ATOM   7377  C C     . ARG C  1 172 ? -63.814 42.818  -23.917 1.00 38.16 ? 172 ARG A C     1 
ATOM   7378  O O     . ARG C  1 172 ? -64.105 41.857  -23.192 1.00 36.08 ? 172 ARG A O     1 
ATOM   7379  C CB    . ARG C  1 172 ? -65.000 44.966  -24.315 1.00 45.03 ? 172 ARG A CB    1 
ATOM   7380  C CG    . ARG C  1 172 ? -66.400 44.363  -24.243 1.00 44.31 ? 172 ARG A CG    1 
ATOM   7381  C CD    . ARG C  1 172 ? -67.291 45.010  -25.279 1.00 45.79 ? 172 ARG A CD    1 
ATOM   7382  N NE    . ARG C  1 172 ? -68.600 44.380  -25.387 1.00 52.50 ? 172 ARG A NE    1 
ATOM   7383  C CZ    . ARG C  1 172 ? -68.818 43.162  -25.870 1.00 56.69 ? 172 ARG A CZ    1 
ATOM   7384  N NH1   . ARG C  1 172 ? -67.819 42.368  -26.232 1.00 46.63 ? 172 ARG A NH1   1 
ATOM   7385  N NH2   . ARG C  1 172 ? -70.072 42.730  -25.994 1.00 60.33 ? 172 ARG A NH2   1 
ATOM   7386  N N     . SER C  1 173 ? -63.371 42.670  -25.167 1.00 37.22 ? 173 SER A N     1 
ATOM   7387  C CA    . SER C  1 173 ? -63.080 41.350  -25.713 1.00 35.49 ? 173 SER A CA    1 
ATOM   7388  C C     . SER C  1 173 ? -62.167 40.573  -24.785 1.00 35.46 ? 173 SER A C     1 
ATOM   7389  O O     . SER C  1 173 ? -62.381 39.380  -24.546 1.00 36.99 ? 173 SER A O     1 
ATOM   7390  C CB    . SER C  1 173 ? -62.441 41.493  -27.091 1.00 29.82 ? 173 SER A CB    1 
ATOM   7391  O OG    . SER C  1 173 ? -61.462 42.521  -27.059 1.00 35.82 ? 173 SER A OG    1 
ATOM   7392  N N     . ALA C  1 174 ? -61.148 41.242  -24.240 1.00 32.63 ? 174 ALA A N     1 
ATOM   7393  C CA    . ALA C  1 174 ? -60.279 40.597  -23.268 1.00 31.67 ? 174 ALA A CA    1 
ATOM   7394  C C     . ALA C  1 174 ? -61.092 39.984  -22.139 1.00 37.23 ? 174 ALA A C     1 
ATOM   7395  O O     . ALA C  1 174 ? -60.930 38.799  -21.817 1.00 37.64 ? 174 ALA A O     1 
ATOM   7396  C CB    . ALA C  1 174 ? -59.272 41.601  -22.724 1.00 30.75 ? 174 ALA A CB    1 
ATOM   7397  N N     . ILE C  1 175 ? -61.990 40.772  -21.532 1.00 37.78 ? 175 ILE A N     1 
ATOM   7398  C CA    . ILE C  1 175 ? -62.826 40.229  -20.458 1.00 43.44 ? 175 ILE A CA    1 
ATOM   7399  C C     . ILE C  1 175 ? -63.706 39.110  -21.001 1.00 44.43 ? 175 ILE A C     1 
ATOM   7400  O O     . ILE C  1 175 ? -63.730 37.991  -20.469 1.00 45.81 ? 175 ILE A O     1 
ATOM   7401  C CB    . ILE C  1 175 ? -63.681 41.330  -19.799 1.00 38.53 ? 175 ILE A CB    1 
ATOM   7402  C CG1   . ILE C  1 175 ? -62.826 42.475  -19.267 1.00 40.96 ? 175 ILE A CG1   1 
ATOM   7403  C CG2   . ILE C  1 175 ? -64.464 40.768  -18.626 1.00 40.25 ? 175 ILE A CG2   1 
ATOM   7404  C CD1   . ILE C  1 175 ? -63.657 43.524  -18.564 1.00 30.85 ? 175 ILE A CD1   1 
ATOM   7405  N N     . GLN C  1 176 ? -64.429 39.399  -22.086 1.00 40.33 ? 176 GLN A N     1 
ATOM   7406  C CA    . GLN C  1 176 ? -65.367 38.430  -22.636 1.00 44.11 ? 176 GLN A CA    1 
ATOM   7407  C C     . GLN C  1 176 ? -64.692 37.100  -22.928 1.00 47.39 ? 176 GLN A C     1 
ATOM   7408  O O     . GLN C  1 176 ? -65.323 36.041  -22.822 1.00 52.34 ? 176 GLN A O     1 
ATOM   7409  C CB    . GLN C  1 176 ? -65.998 38.996  -23.906 1.00 47.97 ? 176 GLN A CB    1 
ATOM   7410  C CG    . GLN C  1 176 ? -67.200 38.220  -24.382 1.00 52.80 ? 176 GLN A CG    1 
ATOM   7411  C CD    . GLN C  1 176 ? -67.143 37.906  -25.859 1.00 61.58 ? 176 GLN A CD    1 
ATOM   7412  O OE1   . GLN C  1 176 ? -66.125 38.135  -26.527 1.00 60.10 ? 176 GLN A OE1   1 
ATOM   7413  N NE2   . GLN C  1 176 ? -68.243 37.377  -26.385 1.00 62.60 ? 176 GLN A NE2   1 
ATOM   7414  N N     . GLU C  1 177 ? -63.410 37.136  -23.272 1.00 43.54 ? 177 GLU A N     1 
ATOM   7415  C CA    . GLU C  1 177 ? -62.697 35.947  -23.703 1.00 47.49 ? 177 GLU A CA    1 
ATOM   7416  C C     . GLU C  1 177 ? -62.010 35.233  -22.552 1.00 41.71 ? 177 GLU A C     1 
ATOM   7417  O O     . GLU C  1 177 ? -61.979 33.997  -22.536 1.00 38.23 ? 177 GLU A O     1 
ATOM   7418  C CB    . GLU C  1 177 ? -61.682 36.332  -24.786 1.00 50.80 ? 177 GLU A CB    1 
ATOM   7419  C CG    . GLU C  1 177 ? -60.484 35.414  -24.920 1.00 51.47 ? 177 GLU A CG    1 
ATOM   7420  C CD    . GLU C  1 177 ? -59.294 36.097  -25.591 1.00 55.84 ? 177 GLU A CD    1 
ATOM   7421  O OE1   . GLU C  1 177 ? -59.432 37.260  -26.053 1.00 47.75 ? 177 GLU A OE1   1 
ATOM   7422  O OE2   . GLU C  1 177 ? -58.218 35.458  -25.653 1.00 53.76 ? 177 GLU A OE2   1 
ATOM   7423  N N     . LEU C  1 178 ? -61.490 35.988  -21.575 1.00 40.48 ? 178 LEU A N     1 
ATOM   7424  C CA    . LEU C  1 178 ? -60.678 35.429  -20.495 1.00 44.11 ? 178 LEU A CA    1 
ATOM   7425  C C     . LEU C  1 178 ? -61.478 34.993  -19.267 1.00 42.29 ? 178 LEU A C     1 
ATOM   7426  O O     . LEU C  1 178 ? -60.977 34.161  -18.495 1.00 44.31 ? 178 LEU A O     1 
ATOM   7427  C CB    . LEU C  1 178 ? -59.612 36.440  -20.055 1.00 40.25 ? 178 LEU A CB    1 
ATOM   7428  C CG    . LEU C  1 178 ? -58.540 36.729  -21.094 1.00 34.18 ? 178 LEU A CG    1 
ATOM   7429  C CD1   . LEU C  1 178 ? -57.748 37.972  -20.726 1.00 31.00 ? 178 LEU A CD1   1 
ATOM   7430  C CD2   . LEU C  1 178 ? -57.640 35.527  -21.188 1.00 38.04 ? 178 LEU A CD2   1 
ATOM   7431  N N     . ILE C  1 179 ? -62.687 35.536  -19.064 1.00 38.34 ? 179 ILE A N     1 
ATOM   7432  C CA    . ILE C  1 179 ? -63.492 35.241  -17.877 1.00 36.47 ? 179 ILE A CA    1 
ATOM   7433  C C     . ILE C  1 179 ? -63.876 33.769  -17.798 1.00 39.98 ? 179 ILE A C     1 
ATOM   7434  O O     . ILE C  1 179 ? -64.055 33.221  -16.703 1.00 42.49 ? 179 ILE A O     1 
ATOM   7435  C CB    . ILE C  1 179 ? -64.750 36.129  -17.870 1.00 44.63 ? 179 ILE A CB    1 
ATOM   7436  C CG1   . ILE C  1 179 ? -65.530 35.929  -16.575 1.00 41.00 ? 179 ILE A CG1   1 
ATOM   7437  C CG2   . ILE C  1 179 ? -65.658 35.802  -19.065 1.00 39.61 ? 179 ILE A CG2   1 
ATOM   7438  C CD1   . ILE C  1 179 ? -64.846 36.526  -15.390 1.00 43.50 ? 179 ILE A CD1   1 
ATOM   7439  N N     . ALA C  1 180 ? -63.996 33.102  -18.941 1.00 37.68 ? 180 ALA A N     1 
ATOM   7440  C CA    . ALA C  1 180 ? -64.692 31.818  -18.964 1.00 44.17 ? 180 ALA A CA    1 
ATOM   7441  C C     . ALA C  1 180 ? -63.930 30.725  -18.221 1.00 42.02 ? 180 ALA A C     1 
ATOM   7442  O O     . ALA C  1 180 ? -64.529 29.979  -17.442 1.00 45.31 ? 180 ALA A O     1 
ATOM   7443  C CB    . ALA C  1 180 ? -64.952 31.390  -20.408 1.00 48.61 ? 180 ALA A CB    1 
ATOM   7444  N N     . GLU C  1 181 ? -62.615 30.607  -18.454 1.00 39.94 ? 181 GLU A N     1 
ATOM   7445  C CA    . GLU C  1 181 ? -61.881 29.412  -18.033 1.00 38.90 ? 181 GLU A CA    1 
ATOM   7446  C C     . GLU C  1 181 ? -62.032 29.142  -16.541 1.00 43.29 ? 181 GLU A C     1 
ATOM   7447  O O     . GLU C  1 181 ? -61.945 27.990  -16.103 1.00 49.24 ? 181 GLU A O     1 
ATOM   7448  C CB    . GLU C  1 181 ? -60.395 29.551  -18.404 1.00 46.88 ? 181 GLU A CB    1 
ATOM   7449  C CG    . GLU C  1 181 ? -59.588 28.225  -18.443 1.00 49.42 ? 181 GLU A CG    1 
ATOM   7450  C CD    . GLU C  1 181 ? -58.050 28.415  -18.330 1.00 56.17 ? 181 GLU A CD    1 
ATOM   7451  O OE1   . GLU C  1 181 ? -57.535 29.512  -18.667 1.00 60.46 ? 181 GLU A OE1   1 
ATOM   7452  O OE2   . GLU C  1 181 ? -57.349 27.458  -17.911 1.00 47.64 ? 181 GLU A OE2   1 
ATOM   7453  N N     . THR C  1 182 ? -62.261 30.184  -15.745 1.00 48.29 ? 182 THR A N     1 
ATOM   7454  C CA    . THR C  1 182 ? -62.254 30.078  -14.288 1.00 37.74 ? 182 THR A CA    1 
ATOM   7455  C C     . THR C  1 182 ? -63.335 30.885  -13.596 1.00 39.66 ? 182 THR A C     1 
ATOM   7456  O O     . THR C  1 182 ? -63.663 30.574  -12.446 1.00 41.50 ? 182 THR A O     1 
ATOM   7457  C CB    . THR C  1 182 ? -60.914 30.556  -13.744 1.00 41.81 ? 182 THR A CB    1 
ATOM   7458  O OG1   . THR C  1 182 ? -60.795 31.962  -14.016 1.00 44.33 ? 182 THR A OG1   1 
ATOM   7459  C CG2   . THR C  1 182 ? -59.775 29.812  -14.416 1.00 43.64 ? 182 THR A CG2   1 
ATOM   7460  N N     . GLY C  1 183 ? -63.868 31.929  -14.214 1.00 38.67 ? 183 GLY A N     1 
ATOM   7461  C CA    . GLY C  1 183 ? -64.819 32.780  -13.557 1.00 36.52 ? 183 GLY A CA    1 
ATOM   7462  C C     . GLY C  1 183 ? -64.215 33.996  -12.915 1.00 43.12 ? 183 GLY A C     1 
ATOM   7463  O O     . GLY C  1 183 ? -64.928 34.717  -12.207 1.00 45.69 ? 183 GLY A O     1 
ATOM   7464  N N     . MET C  1 184 ? -62.930 34.251  -13.135 1.00 41.06 ? 184 MET A N     1 
ATOM   7465  C CA    . MET C  1 184 ? -62.251 35.396  -12.543 1.00 38.50 ? 184 MET A CA    1 
ATOM   7466  C C     . MET C  1 184 ? -61.257 35.971  -13.533 1.00 38.52 ? 184 MET A C     1 
ATOM   7467  O O     . MET C  1 184 ? -60.355 35.263  -13.996 1.00 41.63 ? 184 MET A O     1 
ATOM   7468  C CB    . MET C  1 184 ? -61.528 35.015  -11.247 1.00 37.00 ? 184 MET A CB    1 
ATOM   7469  C CG    . MET C  1 184 ? -62.437 34.753  -10.053 1.00 39.36 ? 184 MET A CG    1 
ATOM   7470  S SD    . MET C  1 184 ? -62.463 33.086  -9.430  1.00 48.89 ? 184 MET A SD    1 
ATOM   7471  C CE    . MET C  1 184 ? -61.088 33.138  -8.303  1.00 45.43 ? 184 MET A CE    1 
ATOM   7472  N N     . VAL C  1 185 ? -61.412 37.251  -13.832 1.00 33.16 ? 185 VAL A N     1 
ATOM   7473  C CA    . VAL C  1 185 ? -60.410 38.019  -14.548 1.00 38.18 ? 185 VAL A CA    1 
ATOM   7474  C C     . VAL C  1 185 ? -59.778 38.991  -13.561 1.00 36.60 ? 185 VAL A C     1 
ATOM   7475  O O     . VAL C  1 185 ? -60.388 39.369  -12.552 1.00 34.89 ? 185 VAL A O     1 
ATOM   7476  C CB    . VAL C  1 185 ? -61.025 38.740  -15.777 1.00 38.40 ? 185 VAL A CB    1 
ATOM   7477  C CG1   . VAL C  1 185 ? -60.149 39.903  -16.261 1.00 31.65 ? 185 VAL A CG1   1 
ATOM   7478  C CG2   . VAL C  1 185 ? -61.228 37.759  -16.911 1.00 36.93 ? 185 VAL A CG2   1 
ATOM   7479  N N     . ILE C  1 186 ? -58.523 39.351  -13.832 1.00 35.59 ? 186 ILE A N     1 
ATOM   7480  C CA    . ILE C  1 186 ? -57.796 40.376  -13.096 1.00 35.45 ? 186 ILE A CA    1 
ATOM   7481  C C     . ILE C  1 186 ? -57.267 41.398  -14.092 1.00 39.10 ? 186 ILE A C     1 
ATOM   7482  O O     . ILE C  1 186 ? -56.851 41.050  -15.205 1.00 39.63 ? 186 ILE A O     1 
ATOM   7483  C CB    . ILE C  1 186 ? -56.646 39.783  -12.254 1.00 38.82 ? 186 ILE A CB    1 
ATOM   7484  C CG1   . ILE C  1 186 ? -56.075 40.842  -11.302 1.00 35.71 ? 186 ILE A CG1   1 
ATOM   7485  C CG2   . ILE C  1 186 ? -55.576 39.192  -13.139 1.00 34.68 ? 186 ILE A CG2   1 
ATOM   7486  C CD1   . ILE C  1 186 ? -55.314 40.256  -10.114 1.00 30.06 ? 186 ILE A CD1   1 
ATOM   7487  N N     . ALA C  1 187 ? -57.307 42.667  -13.698 1.00 38.40 ? 187 ALA A N     1 
ATOM   7488  C CA    . ALA C  1 187 ? -56.988 43.770  -14.590 1.00 31.89 ? 187 ALA A CA    1 
ATOM   7489  C C     . ALA C  1 187 ? -56.151 44.774  -13.812 1.00 37.36 ? 187 ALA A C     1 
ATOM   7490  O O     . ALA C  1 187 ? -56.584 45.270  -12.764 1.00 34.85 ? 187 ALA A O     1 
ATOM   7491  C CB    . ALA C  1 187 ? -58.261 44.413  -15.145 1.00 32.53 ? 187 ALA A CB    1 
ATOM   7492  N N     . LYS C  1 188 ? -54.955 45.067  -14.334 1.00 34.76 ? 188 LYS A N     1 
ATOM   7493  C CA    . LYS C  1 188 ? -53.884 45.699  -13.579 1.00 33.91 ? 188 LYS A CA    1 
ATOM   7494  C C     . LYS C  1 188 ? -53.404 46.943  -14.305 1.00 38.37 ? 188 LYS A C     1 
ATOM   7495  O O     . LYS C  1 188 ? -53.193 46.913  -15.522 1.00 38.08 ? 188 LYS A O     1 
ATOM   7496  C CB    . LYS C  1 188 ? -52.703 44.730  -13.371 1.00 34.49 ? 188 LYS A CB    1 
ATOM   7497  C CG    . LYS C  1 188 ? -53.112 43.297  -12.991 1.00 37.33 ? 188 LYS A CG    1 
ATOM   7498  C CD    . LYS C  1 188 ? -51.941 42.440  -12.473 1.00 34.07 ? 188 LYS A CD    1 
ATOM   7499  C CE    . LYS C  1 188 ? -52.069 40.986  -12.926 1.00 38.63 ? 188 LYS A CE    1 
ATOM   7500  N NZ    . LYS C  1 188 ? -51.021 40.087  -12.347 1.00 39.71 ? 188 LYS A NZ    1 
ATOM   7501  N N     . GLN C  1 189 ? -53.254 48.036  -13.560 1.00 39.79 ? 189 GLN A N     1 
ATOM   7502  C CA    . GLN C  1 189 ? -52.568 49.205  -14.080 1.00 35.57 ? 189 GLN A CA    1 
ATOM   7503  C C     . GLN C  1 189 ? -51.130 48.835  -14.415 1.00 36.50 ? 189 GLN A C     1 
ATOM   7504  O O     . GLN C  1 189 ? -50.507 48.051  -13.700 1.00 38.15 ? 189 GLN A O     1 
ATOM   7505  C CB    . GLN C  1 189 ? -52.622 50.337  -13.049 1.00 40.32 ? 189 GLN A CB    1 
ATOM   7506  C CG    . GLN C  1 189 ? -51.777 51.552  -13.430 1.00 51.21 ? 189 GLN A CG    1 
ATOM   7507  C CD    . GLN C  1 189 ? -51.737 52.592  -12.346 1.00 47.93 ? 189 GLN A CD    1 
ATOM   7508  O OE1   . GLN C  1 189 ? -52.419 52.462  -11.339 1.00 42.42 ? 189 GLN A OE1   1 
ATOM   7509  N NE2   . GLN C  1 189 ? -50.923 53.629  -12.540 1.00 51.68 ? 189 GLN A NE2   1 
ATOM   7510  N N     . ASP C  1 190 ? -50.596 49.395  -15.511 1.00 41.04 ? 190 ASP A N     1 
ATOM   7511  C CA    . ASP C  1 190 ? -49.295 48.931  -15.996 1.00 31.91 ? 190 ASP A CA    1 
ATOM   7512  C C     . ASP C  1 190 ? -48.141 49.371  -15.098 1.00 36.87 ? 190 ASP A C     1 
ATOM   7513  O O     . ASP C  1 190 ? -47.131 48.661  -15.022 1.00 34.82 ? 190 ASP A O     1 
ATOM   7514  C CB    . ASP C  1 190 ? -49.048 49.399  -17.425 1.00 33.15 ? 190 ASP A CB    1 
ATOM   7515  C CG    . ASP C  1 190 ? -48.039 48.508  -18.185 1.00 32.59 ? 190 ASP A CG    1 
ATOM   7516  O OD1   . ASP C  1 190 ? -47.868 47.309  -17.869 1.00 31.89 ? 190 ASP A OD1   1 
ATOM   7517  O OD2   . ASP C  1 190 ? -47.398 49.019  -19.117 1.00 32.95 ? 190 ASP A OD2   1 
ATOM   7518  N N     . ARG C  1 191 ? -48.255 50.503  -14.392 1.00 41.85 ? 191 ARG A N     1 
ATOM   7519  C CA    . ARG C  1 191 ? -47.111 50.997  -13.617 1.00 41.26 ? 191 ARG A CA    1 
ATOM   7520  C C     . ARG C  1 191 ? -47.232 50.781  -12.113 1.00 45.40 ? 191 ARG A C     1 
ATOM   7521  O O     . ARG C  1 191 ? -46.270 50.329  -11.482 1.00 57.14 ? 191 ARG A O     1 
ATOM   7522  C CB    . ARG C  1 191 ? -46.875 52.481  -13.884 1.00 37.95 ? 191 ARG A CB    1 
ATOM   7523  C CG    . ARG C  1 191 ? -45.852 52.704  -14.948 1.00 36.68 ? 191 ARG A CG    1 
ATOM   7524  C CD    . ARG C  1 191 ? -45.203 54.047  -14.843 1.00 35.62 ? 191 ARG A CD    1 
ATOM   7525  N NE    . ARG C  1 191 ? -44.202 54.211  -15.887 1.00 42.25 ? 191 ARG A NE    1 
ATOM   7526  C CZ    . ARG C  1 191 ? -44.471 54.326  -17.180 1.00 42.59 ? 191 ARG A CZ    1 
ATOM   7527  N NH1   . ARG C  1 191 ? -45.720 54.309  -17.633 1.00 36.47 ? 191 ARG A NH1   1 
ATOM   7528  N NH2   . ARG C  1 191 ? -43.462 54.467  -18.041 1.00 38.89 ? 191 ARG A NH2   1 
ATOM   7529  N N     . SER C  1 192 ? -48.374 51.125  -11.525 1.00 41.61 ? 192 SER A N     1 
ATOM   7530  C CA    . SER C  1 192 ? -48.576 51.010  -10.082 1.00 48.72 ? 192 SER A CA    1 
ATOM   7531  C C     . SER C  1 192 ? -48.201 49.627  -9.562  1.00 47.13 ? 192 SER A C     1 
ATOM   7532  O O     . SER C  1 192 ? -48.739 48.613  -10.012 1.00 51.14 ? 192 SER A O     1 
ATOM   7533  C CB    . SER C  1 192 ? -50.044 51.308  -9.750  1.00 50.83 ? 192 SER A CB    1 
ATOM   7534  O OG    . SER C  1 192 ? -50.193 51.928  -8.478  1.00 56.27 ? 192 SER A OG    1 
ATOM   7535  N N     . GLY C  1 193 ? -47.272 49.584  -8.613  1.00 51.28 ? 193 GLY A N     1 
ATOM   7536  C CA    . GLY C  1 193 ? -46.999 48.378  -7.866  1.00 47.27 ? 193 GLY A CA    1 
ATOM   7537  C C     . GLY C  1 193 ? -47.754 48.356  -6.541  1.00 48.44 ? 193 GLY A C     1 
ATOM   7538  O O     . GLY C  1 193 ? -48.456 49.295  -6.171  1.00 53.58 ? 193 GLY A O     1 
ATOM   7539  N N     . GLY C  1 194 ? -47.607 47.238  -5.832  1.00 49.21 ? 194 GLY A N     1 
ATOM   7540  C CA    . GLY C  1 194 ? -48.158 47.072  -4.499  1.00 52.50 ? 194 GLY A CA    1 
ATOM   7541  C C     . GLY C  1 194 ? -49.466 46.307  -4.392  1.00 51.96 ? 194 GLY A C     1 
ATOM   7542  O O     . GLY C  1 194 ? -49.927 46.069  -3.269  1.00 48.30 ? 194 GLY A O     1 
ATOM   7543  N N     . GLY C  1 195 ? -50.062 45.886  -5.510  1.00 50.12 ? 195 GLY A N     1 
ATOM   7544  C CA    . GLY C  1 195 ? -51.432 45.400  -5.501  1.00 47.06 ? 195 GLY A CA    1 
ATOM   7545  C C     . GLY C  1 195 ? -52.488 46.490  -5.520  1.00 47.47 ? 195 GLY A C     1 
ATOM   7546  O O     . GLY C  1 195 ? -53.673 46.186  -5.344  1.00 43.04 ? 195 GLY A O     1 
ATOM   7547  N N     . HIS C  1 196 ? -52.091 47.745  -5.767  1.00 45.21 ? 196 HIS A N     1 
ATOM   7548  C CA    . HIS C  1 196 ? -52.923 48.929  -5.585  1.00 43.10 ? 196 HIS A CA    1 
ATOM   7549  C C     . HIS C  1 196 ? -53.672 49.371  -6.839  1.00 45.45 ? 196 HIS A C     1 
ATOM   7550  O O     . HIS C  1 196 ? -54.687 50.067  -6.722  1.00 47.97 ? 196 HIS A O     1 
ATOM   7551  C CB    . HIS C  1 196 ? -52.055 50.102  -5.115  1.00 55.35 ? 196 HIS A CB    1 
ATOM   7552  C CG    . HIS C  1 196 ? -51.708 50.065  -3.657  1.00 51.28 ? 196 HIS A CG    1 
ATOM   7553  N ND1   . HIS C  1 196 ? -52.628 49.761  -2.676  1.00 50.53 ? 196 HIS A ND1   1 
ATOM   7554  C CD2   . HIS C  1 196 ? -50.542 50.315  -3.015  1.00 53.63 ? 196 HIS A CD2   1 
ATOM   7555  C CE1   . HIS C  1 196 ? -52.040 49.821  -1.493  1.00 56.85 ? 196 HIS A CE1   1 
ATOM   7556  N NE2   . HIS C  1 196 ? -50.774 50.153  -1.672  1.00 58.55 ? 196 HIS A NE2   1 
ATOM   7557  N N     . GLY C  1 197 ? -53.184 49.034  -8.028  1.00 50.96 ? 197 GLY A N     1 
ATOM   7558  C CA    . GLY C  1 197 ? -53.861 49.414  -9.253  1.00 39.67 ? 197 GLY A CA    1 
ATOM   7559  C C     . GLY C  1 197 ? -54.483 48.239  -9.976  1.00 33.79 ? 197 GLY A C     1 
ATOM   7560  O O     . GLY C  1 197 ? -54.537 48.219  -11.206 1.00 42.10 ? 197 GLY A O     1 
ATOM   7561  N N     . ASN C  1 198 ? -54.952 47.254  -9.223  1.00 32.49 ? 198 ASN A N     1 
ATOM   7562  C CA    . ASN C  1 198 ? -55.566 46.057  -9.769  1.00 35.32 ? 198 ASN A CA    1 
ATOM   7563  C C     . ASN C  1 198 ? -57.065 46.082  -9.508  1.00 46.27 ? 198 ASN A C     1 
ATOM   7564  O O     . ASN C  1 198 ? -57.531 46.667  -8.523  1.00 47.78 ? 198 ASN A O     1 
ATOM   7565  C CB    . ASN C  1 198 ? -54.972 44.788  -9.148  1.00 36.45 ? 198 ASN A CB    1 
ATOM   7566  C CG    . ASN C  1 198 ? -53.476 44.653  -9.403  1.00 37.04 ? 198 ASN A CG    1 
ATOM   7567  O OD1   . ASN C  1 198 ? -52.887 45.456  -10.137 1.00 36.93 ? 198 ASN A OD1   1 
ATOM   7568  N ND2   . ASN C  1 198 ? -52.856 43.631  -8.805  1.00 30.80 ? 198 ASN A ND2   1 
ATOM   7569  N N     . ILE C  1 199 ? -57.820 45.437  -10.395 1.00 40.75 ? 199 ILE A N     1 
ATOM   7570  C CA    . ILE C  1 199 ? -59.249 45.248  -10.200 1.00 34.44 ? 199 ILE A CA    1 
ATOM   7571  C C     . ILE C  1 199 ? -59.577 43.813  -10.574 1.00 32.79 ? 199 ILE A C     1 
ATOM   7572  O O     . ILE C  1 199 ? -58.902 43.193  -11.402 1.00 35.83 ? 199 ILE A O     1 
ATOM   7573  C CB    . ILE C  1 199 ? -60.084 46.262  -11.022 1.00 38.42 ? 199 ILE A CB    1 
ATOM   7574  C CG1   . ILE C  1 199 ? -59.774 47.682  -10.558 1.00 35.73 ? 199 ILE A CG1   1 
ATOM   7575  C CG2   . ILE C  1 199 ? -61.589 45.996  -10.904 1.00 39.23 ? 199 ILE A CG2   1 
ATOM   7576  C CD1   . ILE C  1 199 ? -60.762 48.697  -11.031 1.00 38.00 ? 199 ILE A CD1   1 
ATOM   7577  N N     . GLY C  1 200 ? -60.608 43.274  -9.934  1.00 35.46 ? 200 GLY A N     1 
ATOM   7578  C CA    . GLY C  1 200 ? -61.085 41.943  -10.213 1.00 41.63 ? 200 GLY A CA    1 
ATOM   7579  C C     . GLY C  1 200 ? -62.430 41.983  -10.920 1.00 43.39 ? 200 GLY A C     1 
ATOM   7580  O O     . GLY C  1 200 ? -63.107 43.007  -10.988 1.00 49.86 ? 200 GLY A O     1 
ATOM   7581  N N     . ILE C  1 201 ? -62.794 40.831  -11.475 1.00 39.42 ? 201 ILE A N     1 
ATOM   7582  C CA    . ILE C  1 201 ? -64.035 40.647  -12.217 1.00 39.28 ? 201 ILE A CA    1 
ATOM   7583  C C     . ILE C  1 201 ? -64.531 39.253  -11.849 1.00 38.80 ? 201 ILE A C     1 
ATOM   7584  O O     . ILE C  1 201 ? -63.919 38.256  -12.239 1.00 38.79 ? 201 ILE A O     1 
ATOM   7585  C CB    . ILE C  1 201 ? -63.833 40.776  -13.737 1.00 41.92 ? 201 ILE A CB    1 
ATOM   7586  C CG1   . ILE C  1 201 ? -63.115 42.090  -14.093 1.00 40.54 ? 201 ILE A CG1   1 
ATOM   7587  C CG2   . ILE C  1 201 ? -65.160 40.702  -14.464 1.00 38.19 ? 201 ILE A CG2   1 
ATOM   7588  C CD1   . ILE C  1 201 ? -63.982 43.325  -14.083 1.00 39.64 ? 201 ILE A CD1   1 
ATOM   7589  N N     . SER C  1 202 ? -65.613 39.175  -11.088 1.00 43.94 ? 202 SER A N     1 
ATOM   7590  C CA    . SER C  1 202 ? -65.999 37.936  -10.433 1.00 48.92 ? 202 SER A CA    1 
ATOM   7591  C C     . SER C  1 202 ? -67.324 37.427  -10.990 1.00 46.57 ? 202 SER A C     1 
ATOM   7592  O O     . SER C  1 202 ? -68.212 38.213  -11.322 1.00 45.99 ? 202 SER A O     1 
ATOM   7593  C CB    . SER C  1 202 ? -66.084 38.165  -8.911  1.00 52.52 ? 202 SER A CB    1 
ATOM   7594  O OG    . SER C  1 202 ? -65.836 36.977  -8.192  1.00 61.71 ? 202 SER A OG    1 
ATOM   7595  N N     . THR C  1 203 ? -67.450 36.112  -11.045 1.00 45.70 ? 203 THR A N     1 
ATOM   7596  C CA    . THR C  1 203 ? -68.689 35.449  -11.391 1.00 50.62 ? 203 THR A CA    1 
ATOM   7597  C C     . THR C  1 203 ? -69.562 35.178  -10.160 1.00 54.74 ? 203 THR A C     1 
ATOM   7598  O O     . THR C  1 203 ? -70.778 35.386  -10.206 1.00 50.54 ? 203 THR A O     1 
ATOM   7599  C CB    . THR C  1 203 ? -68.370 34.137  -12.104 1.00 51.65 ? 203 THR A CB    1 
ATOM   7600  O OG1   . THR C  1 203 ? -67.193 33.549  -11.517 1.00 54.40 ? 203 THR A OG1   1 
ATOM   7601  C CG2   . THR C  1 203 ? -68.131 34.401  -13.560 1.00 53.19 ? 203 THR A CG2   1 
ATOM   7602  N N     . SER C  1 204 ? -68.975 34.660  -9.084  1.00 51.32 ? 204 SER A N     1 
ATOM   7603  C CA    . SER C  1 204 ? -69.663 34.452  -7.838  1.00 52.38 ? 204 SER A CA    1 
ATOM   7604  C C     . SER C  1 204 ? -69.051 35.356  -6.781  1.00 54.82 ? 204 SER A C     1 
ATOM   7605  O O     . SER C  1 204 ? -67.819 35.450  -6.707  1.00 55.25 ? 204 SER A O     1 
ATOM   7606  C CB    . SER C  1 204 ? -69.548 32.995  -7.397  1.00 55.77 ? 204 SER A CB    1 
ATOM   7607  O OG    . SER C  1 204 ? -69.503 32.907  -5.986  1.00 61.53 ? 204 SER A OG    1 
ATOM   7608  N N     . PRO C  1 205 ? -69.847 36.050  -5.966  1.00 54.10 ? 205 PRO A N     1 
ATOM   7609  C CA    . PRO C  1 205 ? -69.257 36.817  -4.860  1.00 50.71 ? 205 PRO A CA    1 
ATOM   7610  C C     . PRO C  1 205 ? -68.515 35.956  -3.850  1.00 50.46 ? 205 PRO A C     1 
ATOM   7611  O O     . PRO C  1 205 ? -67.889 36.497  -2.936  1.00 55.83 ? 205 PRO A O     1 
ATOM   7612  C CB    . PRO C  1 205 ? -70.467 37.514  -4.237  1.00 46.98 ? 205 PRO A CB    1 
ATOM   7613  C CG    . PRO C  1 205 ? -71.374 37.758  -5.423  1.00 52.72 ? 205 PRO A CG    1 
ATOM   7614  C CD    . PRO C  1 205 ? -71.171 36.572  -6.352  1.00 55.65 ? 205 PRO A CD    1 
ATOM   7615  N N     . GLU C  1 206 ? -68.547 34.631  -3.991  1.00 49.98 ? 206 GLU A N     1 
ATOM   7616  C CA    . GLU C  1 206 ? -67.716 33.812  -3.112  1.00 61.83 ? 206 GLU A CA    1 
ATOM   7617  C C     . GLU C  1 206 ? -66.235 33.891  -3.486  1.00 67.36 ? 206 GLU A C     1 
ATOM   7618  O O     . GLU C  1 206 ? -65.376 33.603  -2.639  1.00 66.48 ? 206 GLU A O     1 
ATOM   7619  C CB    . GLU C  1 206 ? -68.179 32.347  -3.123  1.00 57.47 ? 206 GLU A CB    1 
ATOM   7620  C CG    . GLU C  1 206 ? -69.630 32.122  -2.696  1.00 58.37 ? 206 GLU A CG    1 
ATOM   7621  C CD    . GLU C  1 206 ? -69.781 31.631  -1.261  1.00 62.04 ? 206 GLU A CD    1 
ATOM   7622  O OE1   . GLU C  1 206 ? -69.679 30.401  -1.028  1.00 62.71 ? 206 GLU A OE1   1 
ATOM   7623  O OE2   . GLU C  1 206 ? -70.030 32.473  -0.368  1.00 63.23 ? 206 GLU A OE2   1 
ATOM   7624  N N     . SER C  1 207 ? -65.922 34.285  -4.725  1.00 60.74 ? 207 SER A N     1 
ATOM   7625  C CA    . SER C  1 207 ? -64.542 34.317  -5.205  1.00 58.98 ? 207 SER A CA    1 
ATOM   7626  C C     . SER C  1 207 ? -63.736 35.394  -4.481  1.00 54.29 ? 207 SER A C     1 
ATOM   7627  O O     . SER C  1 207 ? -64.082 36.581  -4.527  1.00 49.36 ? 207 SER A O     1 
ATOM   7628  C CB    . SER C  1 207 ? -64.511 34.565  -6.718  1.00 61.78 ? 207 SER A CB    1 
ATOM   7629  O OG    . SER C  1 207 ? -65.378 33.701  -7.446  1.00 56.59 ? 207 SER A OG    1 
ATOM   7630  N N     . SER C  1 208 ? -62.652 34.979  -3.824  1.00 58.69 ? 208 SER A N     1 
ATOM   7631  C CA    . SER C  1 208 ? -61.696 35.903  -3.227  1.00 58.26 ? 208 SER A CA    1 
ATOM   7632  C C     . SER C  1 208 ? -60.655 36.294  -4.268  1.00 52.36 ? 208 SER A C     1 
ATOM   7633  O O     . SER C  1 208 ? -60.538 35.669  -5.322  1.00 50.03 ? 208 SER A O     1 
ATOM   7634  C CB    . SER C  1 208 ? -61.003 35.289  -2.015  1.00 49.80 ? 208 SER A CB    1 
ATOM   7635  O OG    . SER C  1 208 ? -60.091 34.279  -2.395  1.00 51.67 ? 208 SER A OG    1 
ATOM   7636  N N     . PHE C  1 209 ? -59.874 37.330  -3.953  1.00 44.60 ? 209 PHE A N     1 
ATOM   7637  C CA    . PHE C  1 209 ? -58.969 37.943  -4.926  1.00 41.68 ? 209 PHE A CA    1 
ATOM   7638  C C     . PHE C  1 209 ? -57.786 38.581  -4.207  1.00 41.24 ? 209 PHE A C     1 
ATOM   7639  O O     . PHE C  1 209 ? -57.666 39.809  -4.137  1.00 39.00 ? 209 PHE A O     1 
ATOM   7640  C CB    . PHE C  1 209 ? -59.709 38.990  -5.759  1.00 45.64 ? 209 PHE A CB    1 
ATOM   7641  C CG    . PHE C  1 209 ? -60.434 38.459  -6.969  1.00 34.96 ? 209 PHE A CG    1 
ATOM   7642  C CD1   . PHE C  1 209 ? -61.715 37.956  -6.865  1.00 43.76 ? 209 PHE A CD1   1 
ATOM   7643  C CD2   . PHE C  1 209 ? -59.870 38.569  -8.227  1.00 36.00 ? 209 PHE A CD2   1 
ATOM   7644  C CE1   . PHE C  1 209 ? -62.399 37.511  -8.001  1.00 47.23 ? 209 PHE A CE1   1 
ATOM   7645  C CE2   . PHE C  1 209 ? -60.545 38.137  -9.360  1.00 40.38 ? 209 PHE A CE2   1 
ATOM   7646  C CZ    . PHE C  1 209 ? -61.813 37.627  -9.242  1.00 42.14 ? 209 PHE A CZ    1 
ATOM   7647  N N     . PRO C  1 210 ? -56.874 37.772  -3.672  1.00 37.38 ? 210 PRO A N     1 
ATOM   7648  C CA    . PRO C  1 210 ? -55.626 38.340  -3.154  1.00 38.04 ? 210 PRO A CA    1 
ATOM   7649  C C     . PRO C  1 210 ? -54.872 39.062  -4.264  1.00 39.08 ? 210 PRO A C     1 
ATOM   7650  O O     . PRO C  1 210 ? -54.724 38.546  -5.372  1.00 38.61 ? 210 PRO A O     1 
ATOM   7651  C CB    . PRO C  1 210 ? -54.862 37.111  -2.648  1.00 41.07 ? 210 PRO A CB    1 
ATOM   7652  C CG    . PRO C  1 210 ? -55.918 36.101  -2.385  1.00 40.95 ? 210 PRO A CG    1 
ATOM   7653  C CD    . PRO C  1 210 ? -56.945 36.321  -3.452  1.00 38.48 ? 210 PRO A CD    1 
ATOM   7654  N N     . GLY C  1 211 ? -54.415 40.274  -3.967  1.00 35.11 ? 211 GLY A N     1 
ATOM   7655  C CA    . GLY C  1 211 ? -53.664 41.064  -4.916  1.00 31.06 ? 211 GLY A CA    1 
ATOM   7656  C C     . GLY C  1 211 ? -54.441 42.155  -5.618  1.00 40.79 ? 211 GLY A C     1 
ATOM   7657  O O     . GLY C  1 211 ? -53.900 42.769  -6.550  1.00 38.45 ? 211 GLY A O     1 
ATOM   7658  N N     . THR C  1 212 ? -55.678 42.433  -5.191  1.00 43.30 ? 212 THR A N     1 
ATOM   7659  C CA    . THR C  1 212 ? -56.575 43.385  -5.842  1.00 43.38 ? 212 THR A CA    1 
ATOM   7660  C C     . THR C  1 212 ? -56.997 44.472  -4.854  1.00 47.26 ? 212 THR A C     1 
ATOM   7661  O O     . THR C  1 212 ? -56.757 44.362  -3.651  1.00 47.44 ? 212 THR A O     1 
ATOM   7662  C CB    . THR C  1 212 ? -57.824 42.683  -6.412  1.00 46.75 ? 212 THR A CB    1 
ATOM   7663  O OG1   . THR C  1 212 ? -58.451 41.895  -5.393  1.00 47.27 ? 212 THR A OG1   1 
ATOM   7664  C CG2   . THR C  1 212 ? -57.468 41.771  -7.599  1.00 40.90 ? 212 THR A CG2   1 
ATOM   7665  N N     . ARG C  1 213 ? -57.632 45.534  -5.388  1.00 53.85 ? 213 ARG A N     1 
ATOM   7666  C CA    . ARG C  1 213 ? -58.206 46.658  -4.632  1.00 49.68 ? 213 ARG A CA    1 
ATOM   7667  C C     . ARG C  1 213 ? -59.728 46.630  -4.562  1.00 51.12 ? 213 ARG A C     1 
ATOM   7668  O O     . ARG C  1 213 ? -60.299 46.866  -3.491  1.00 54.69 ? 213 ARG A O     1 
ATOM   7669  C CB    . ARG C  1 213 ? -57.773 48.011  -5.225  1.00 47.10 ? 213 ARG A CB    1 
ATOM   7670  C CG    . ARG C  1 213 ? -58.832 49.134  -5.057  1.00 57.08 ? 213 ARG A CG    1 
ATOM   7671  C CD    . ARG C  1 213 ? -58.247 50.553  -4.828  1.00 57.95 ? 213 ARG A CD    1 
ATOM   7672  N NE    . ARG C  1 213 ? -57.375 50.994  -5.910  1.00 59.38 ? 213 ARG A NE    1 
ATOM   7673  C CZ    . ARG C  1 213 ? -57.305 52.241  -6.360  1.00 58.25 ? 213 ARG A CZ    1 
ATOM   7674  N NH1   . ARG C  1 213 ? -58.041 53.207  -5.833  1.00 53.22 ? 213 ARG A NH1   1 
ATOM   7675  N NH2   . ARG C  1 213 ? -56.473 52.524  -7.361  1.00 58.50 ? 213 ARG A NH2   1 
ATOM   7676  N N     . GLU C  1 214 ? -60.412 46.381  -5.673  1.00 43.44 ? 214 GLU A N     1 
ATOM   7677  C CA    . GLU C  1 214 ? -61.845 46.136  -5.646  1.00 45.57 ? 214 GLU A CA    1 
ATOM   7678  C C     . GLU C  1 214 ? -62.123 44.925  -6.518  1.00 43.50 ? 214 GLU A C     1 
ATOM   7679  O O     . GLU C  1 214 ? -61.233 44.411  -7.194  1.00 45.60 ? 214 GLU A O     1 
ATOM   7680  C CB    . GLU C  1 214 ? -62.654 47.360  -6.114  1.00 48.76 ? 214 GLU A CB    1 
ATOM   7681  C CG    . GLU C  1 214 ? -62.578 48.561  -5.150  1.00 52.65 ? 214 GLU A CG    1 
ATOM   7682  C CD    . GLU C  1 214 ? -63.947 49.093  -4.704  1.00 55.07 ? 214 GLU A CD    1 
ATOM   7683  O OE1   . GLU C  1 214 ? -64.871 48.289  -4.419  1.00 51.86 ? 214 GLU A OE1   1 
ATOM   7684  O OE2   . GLU C  1 214 ? -64.090 50.332  -4.619  1.00 54.74 ? 214 GLU A OE2   1 
ATOM   7685  N N     . VAL C  1 215 ? -63.357 44.436  -6.462  1.00 47.03 ? 215 VAL A N     1 
ATOM   7686  C CA    . VAL C  1 215 ? -63.808 43.324  -7.296  1.00 45.79 ? 215 VAL A CA    1 
ATOM   7687  C C     . VAL C  1 215 ? -65.266 43.562  -7.667  1.00 44.61 ? 215 VAL A C     1 
ATOM   7688  O O     . VAL C  1 215 ? -66.122 43.731  -6.790  1.00 44.23 ? 215 VAL A O     1 
ATOM   7689  C CB    . VAL C  1 215 ? -63.660 41.954  -6.600  1.00 43.77 ? 215 VAL A CB    1 
ATOM   7690  C CG1   . VAL C  1 215 ? -64.152 40.862  -7.527  1.00 39.57 ? 215 VAL A CG1   1 
ATOM   7691  C CG2   . VAL C  1 215 ? -62.217 41.680  -6.183  1.00 43.13 ? 215 VAL A CG2   1 
ATOM   7692  N N     . LEU C  1 216 ? -65.550 43.558  -8.960  1.00 44.31 ? 216 LEU A N     1 
ATOM   7693  C CA    . LEU C  1 216 ? -66.897 43.769  -9.468  1.00 45.33 ? 216 LEU A CA    1 
ATOM   7694  C C     . LEU C  1 216 ? -67.436 42.483  -10.073 1.00 42.40 ? 216 LEU A C     1 
ATOM   7695  O O     . LEU C  1 216 ? -66.689 41.551  -10.376 1.00 49.49 ? 216 LEU A O     1 
ATOM   7696  C CB    . LEU C  1 216 ? -66.911 44.894  -10.503 1.00 45.43 ? 216 LEU A CB    1 
ATOM   7697  C CG    . LEU C  1 216 ? -66.018 46.054  -10.062 1.00 41.98 ? 216 LEU A CG    1 
ATOM   7698  C CD1   . LEU C  1 216 ? -65.953 47.125  -11.121 1.00 39.98 ? 216 LEU A CD1   1 
ATOM   7699  C CD2   . LEU C  1 216 ? -66.514 46.630  -8.743  1.00 45.90 ? 216 LEU A CD2   1 
ATOM   7700  N N     . ALA C  1 217 ? -68.746 42.432  -10.242 1.00 46.48 ? 217 ALA A N     1 
ATOM   7701  C CA    . ALA C  1 217 ? -69.381 41.260  -10.825 1.00 43.22 ? 217 ALA A CA    1 
ATOM   7702  C C     . ALA C  1 217 ? -69.382 41.372  -12.343 1.00 48.65 ? 217 ALA A C     1 
ATOM   7703  O O     . ALA C  1 217 ? -69.367 42.474  -12.902 1.00 55.19 ? 217 ALA A O     1 
ATOM   7704  C CB    . ALA C  1 217 ? -70.802 41.108  -10.292 1.00 36.64 ? 217 ALA A CB    1 
ATOM   7705  N N     . TYR C  1 218 ? -69.373 40.217  -13.009 1.00 48.34 ? 218 TYR A N     1 
ATOM   7706  C CA    . TYR C  1 218 ? -69.278 40.176  -14.470 1.00 51.33 ? 218 TYR A CA    1 
ATOM   7707  C C     . TYR C  1 218 ? -70.690 40.387  -15.007 1.00 54.99 ? 218 TYR A C     1 
ATOM   7708  O O     . TYR C  1 218 ? -71.476 39.444  -15.145 1.00 56.45 ? 218 TYR A O     1 
ATOM   7709  C CB    . TYR C  1 218 ? -68.652 38.866  -14.963 1.00 50.26 ? 218 TYR A CB    1 
ATOM   7710  C CG    . TYR C  1 218 ? -68.855 38.631  -16.459 1.00 44.97 ? 218 TYR A CG    1 
ATOM   7711  C CD1   . TYR C  1 218 ? -68.139 39.372  -17.388 1.00 43.58 ? 218 TYR A CD1   1 
ATOM   7712  C CD2   . TYR C  1 218 ? -69.756 37.672  -16.939 1.00 40.28 ? 218 TYR A CD2   1 
ATOM   7713  C CE1   . TYR C  1 218 ? -68.338 39.196  -18.768 1.00 44.36 ? 218 TYR A CE1   1 
ATOM   7714  C CE2   . TYR C  1 218 ? -69.956 37.482  -18.309 1.00 47.42 ? 218 TYR A CE2   1 
ATOM   7715  C CZ    . TYR C  1 218 ? -69.243 38.247  -19.220 1.00 43.26 ? 218 TYR A CZ    1 
ATOM   7716  O OH    . TYR C  1 218 ? -69.466 38.038  -20.564 1.00 46.85 ? 218 TYR A OH    1 
ATOM   7717  N N     . ALA C  1 219 ? -71.048 41.641  -15.267 1.00 55.03 ? 219 ALA A N     1 
ATOM   7718  C CA    . ALA C  1 219 ? -72.338 41.919  -15.899 1.00 62.33 ? 219 ALA A CA    1 
ATOM   7719  C C     . ALA C  1 219 ? -72.154 41.780  -17.403 1.00 56.47 ? 219 ALA A C     1 
ATOM   7720  O O     . ALA C  1 219 ? -71.691 42.701  -18.082 1.00 55.04 ? 219 ALA A O     1 
ATOM   7721  C CB    . ALA C  1 219 ? -72.872 43.297  -15.521 1.00 65.66 ? 219 ALA A CB    1 
ATOM   7722  N N     . ASN C  1 220 ? -72.484 40.586  -17.910 1.00 53.88 ? 220 ASN A N     1 
ATOM   7723  C CA    . ASN C  1 220 ? -72.564 40.350  -19.344 1.00 52.14 ? 220 ASN A CA    1 
ATOM   7724  C C     . ASN C  1 220 ? -73.268 41.509  -20.037 1.00 59.15 ? 220 ASN A C     1 
ATOM   7725  O O     . ASN C  1 220 ? -72.769 42.049  -21.028 1.00 62.33 ? 220 ASN A O     1 
ATOM   7726  C CB    . ASN C  1 220 ? -73.291 39.028  -19.601 1.00 51.79 ? 220 ASN A CB    1 
ATOM   7727  C CG    . ASN C  1 220 ? -73.406 38.688  -21.083 1.00 63.38 ? 220 ASN A CG    1 
ATOM   7728  O OD1   . ASN C  1 220 ? -72.915 39.409  -21.955 1.00 65.68 ? 220 ASN A OD1   1 
ATOM   7729  N ND2   . ASN C  1 220 ? -74.063 37.573  -21.370 1.00 68.59 ? 220 ASN A ND2   1 
ATOM   7730  N N     . ASP C  1 221 ? -74.415 41.929  -19.494 1.00 62.93 ? 221 ASP A N     1 
ATOM   7731  C CA    . ASP C  1 221 ? -75.138 43.082  -20.028 1.00 59.55 ? 221 ASP A CA    1 
ATOM   7732  C C     . ASP C  1 221 ? -74.319 44.366  -19.974 1.00 61.57 ? 221 ASP A C     1 
ATOM   7733  O O     . ASP C  1 221 ? -74.513 45.256  -20.812 1.00 61.18 ? 221 ASP A O     1 
ATOM   7734  C CB    . ASP C  1 221 ? -76.435 43.261  -19.249 1.00 62.31 ? 221 ASP A CB    1 
ATOM   7735  C CG    . ASP C  1 221 ? -76.250 43.010  -17.757 1.00 68.59 ? 221 ASP A CG    1 
ATOM   7736  O OD1   . ASP C  1 221 ? -76.191 41.822  -17.363 1.00 63.01 ? 221 ASP A OD1   1 
ATOM   7737  O OD2   . ASP C  1 221 ? -76.128 43.992  -16.984 1.00 70.59 ? 221 ASP A OD2   1 
ATOM   7738  N N     . GLN C  1 222 ? -73.420 44.496  -18.990 1.00 63.86 ? 222 GLN A N     1 
ATOM   7739  C CA    . GLN C  1 222 ? -72.600 45.695  -18.815 1.00 63.38 ? 222 GLN A CA    1 
ATOM   7740  C C     . GLN C  1 222 ? -71.153 45.473  -19.232 1.00 59.45 ? 222 GLN A C     1 
ATOM   7741  O O     . GLN C  1 222 ? -70.286 46.295  -18.927 1.00 57.15 ? 222 GLN A O     1 
ATOM   7742  C CB    . GLN C  1 222 ? -72.655 46.177  -17.370 1.00 58.55 ? 222 GLN A CB    1 
ATOM   7743  C CG    . GLN C  1 222 ? -73.958 46.840  -16.995 1.00 58.60 ? 222 GLN A CG    1 
ATOM   7744  C CD    . GLN C  1 222 ? -74.053 47.071  -15.508 1.00 58.02 ? 222 GLN A CD    1 
ATOM   7745  O OE1   . GLN C  1 222 ? -73.654 46.208  -14.707 1.00 51.16 ? 222 GLN A OE1   1 
ATOM   7746  N NE2   . GLN C  1 222 ? -74.560 48.244  -15.120 1.00 49.57 ? 222 GLN A NE2   1 
ATOM   7747  N N     . LEU C  1 223 ? -70.881 44.375  -19.936 1.00 58.68 ? 223 LEU A N     1 
ATOM   7748  C CA    . LEU C  1 223 ? -69.542 44.131  -20.455 1.00 57.86 ? 223 LEU A CA    1 
ATOM   7749  C C     . LEU C  1 223 ? -69.029 45.320  -21.254 1.00 49.91 ? 223 LEU A C     1 
ATOM   7750  O O     . LEU C  1 223 ? -67.822 45.558  -21.318 1.00 49.12 ? 223 LEU A O     1 
ATOM   7751  C CB    . LEU C  1 223 ? -69.556 42.865  -21.304 1.00 56.60 ? 223 LEU A CB    1 
ATOM   7752  C CG    . LEU C  1 223 ? -68.215 42.296  -21.740 1.00 55.50 ? 223 LEU A CG    1 
ATOM   7753  C CD1   . LEU C  1 223 ? -67.277 42.178  -20.562 1.00 48.08 ? 223 LEU A CD1   1 
ATOM   7754  C CD2   . LEU C  1 223 ? -68.461 40.936  -22.362 1.00 56.97 ? 223 LEU A CD2   1 
ATOM   7755  N N     . ASP C  1 224 ? -69.932 46.090  -21.852 1.00 50.22 ? 224 ASP A N     1 
ATOM   7756  C CA    . ASP C  1 224 ? -69.535 47.349  -22.464 1.00 52.21 ? 224 ASP A CA    1 
ATOM   7757  C C     . ASP C  1 224 ? -69.001 48.317  -21.412 1.00 49.30 ? 224 ASP A C     1 
ATOM   7758  O O     . ASP C  1 224 ? -67.919 48.891  -21.567 1.00 46.02 ? 224 ASP A O     1 
ATOM   7759  C CB    . ASP C  1 224 ? -70.729 47.939  -23.215 1.00 47.68 ? 224 ASP A CB    1 
ATOM   7760  C CG    . ASP C  1 224 ? -71.332 46.950  -24.215 1.00 53.13 ? 224 ASP A CG    1 
ATOM   7761  O OD1   . ASP C  1 224 ? -70.565 46.222  -24.883 1.00 54.18 ? 224 ASP A OD1   1 
ATOM   7762  O OD2   . ASP C  1 224 ? -72.576 46.892  -24.335 1.00 54.02 ? 224 ASP A OD2   1 
ATOM   7763  N N     . THR C  1 225 ? -69.734 48.501  -20.317 1.00 48.94 ? 225 THR A N     1 
ATOM   7764  C CA    . THR C  1 225 ? -69.333 49.558  -19.398 1.00 53.26 ? 225 THR A CA    1 
ATOM   7765  C C     . THR C  1 225 ? -68.314 49.103  -18.360 1.00 49.25 ? 225 THR A C     1 
ATOM   7766  O O     . THR C  1 225 ? -67.530 49.937  -17.895 1.00 49.51 ? 225 THR A O     1 
ATOM   7767  C CB    . THR C  1 225 ? -70.553 50.175  -18.705 1.00 58.94 ? 225 THR A CB    1 
ATOM   7768  O OG1   . THR C  1 225 ? -71.735 49.439  -19.054 1.00 56.34 ? 225 THR A OG1   1 
ATOM   7769  C CG2   . THR C  1 225 ? -70.712 51.655  -19.135 1.00 50.77 ? 225 THR A CG2   1 
ATOM   7770  N N     . LEU C  1 226 ? -68.269 47.817  -17.992 1.00 47.88 ? 226 LEU A N     1 
ATOM   7771  C CA    . LEU C  1 226 ? -67.137 47.371  -17.182 1.00 43.67 ? 226 LEU A CA    1 
ATOM   7772  C C     . LEU C  1 226 ? -65.820 47.691  -17.871 1.00 42.09 ? 226 LEU A C     1 
ATOM   7773  O O     . LEU C  1 226 ? -64.878 48.170  -17.235 1.00 44.23 ? 226 LEU A O     1 
ATOM   7774  C CB    . LEU C  1 226 ? -67.199 45.876  -16.877 1.00 41.68 ? 226 LEU A CB    1 
ATOM   7775  C CG    . LEU C  1 226 ? -68.407 45.220  -16.230 1.00 48.98 ? 226 LEU A CG    1 
ATOM   7776  C CD1   . LEU C  1 226 ? -68.898 43.988  -17.050 1.00 53.52 ? 226 LEU A CD1   1 
ATOM   7777  C CD2   . LEU C  1 226 ? -68.066 44.902  -14.744 1.00 41.24 ? 226 LEU A CD2   1 
ATOM   7778  N N     . ALA C  1 227 ? -65.746 47.472  -19.181 1.00 41.36 ? 227 ALA A N     1 
ATOM   7779  C CA    . ALA C  1 227 ? -64.502 47.728  -19.898 1.00 44.91 ? 227 ALA A CA    1 
ATOM   7780  C C     . ALA C  1 227 ? -64.128 49.199  -19.849 1.00 43.39 ? 227 ALA A C     1 
ATOM   7781  O O     . ALA C  1 227 ? -62.954 49.550  -19.673 1.00 38.51 ? 227 ALA A O     1 
ATOM   7782  C CB    . ALA C  1 227 ? -64.625 47.268  -21.352 1.00 46.30 ? 227 ALA A CB    1 
ATOM   7783  N N     . ASP C  1 228 ? -65.110 50.076  -20.044 1.00 49.94 ? 228 ASP A N     1 
ATOM   7784  C CA    . ASP C  1 228 ? -64.803 51.496  -20.064 1.00 49.78 ? 228 ASP A CA    1 
ATOM   7785  C C     . ASP C  1 228 ? -64.397 51.969  -18.679 1.00 45.65 ? 228 ASP A C     1 
ATOM   7786  O O     . ASP C  1 228 ? -63.481 52.785  -18.545 1.00 46.85 ? 228 ASP A O     1 
ATOM   7787  C CB    . ASP C  1 228 ? -65.997 52.290  -20.601 1.00 55.18 ? 228 ASP A CB    1 
ATOM   7788  C CG    . ASP C  1 228 ? -65.569 53.547  -21.355 1.00 60.24 ? 228 ASP A CG    1 
ATOM   7789  O OD1   . ASP C  1 228 ? -64.588 53.465  -22.129 1.00 56.40 ? 228 ASP A OD1   1 
ATOM   7790  O OD2   . ASP C  1 228 ? -66.200 54.616  -21.161 1.00 59.17 ? 228 ASP A OD2   1 
ATOM   7791  N N     . THR C  1 229 ? -65.044 51.442  -17.634 1.00 44.33 ? 229 THR A N     1 
ATOM   7792  C CA    . THR C  1 229 ? -64.656 51.794  -16.271 1.00 43.92 ? 229 THR A CA    1 
ATOM   7793  C C     . THR C  1 229 ? -63.209 51.392  -15.984 1.00 44.55 ? 229 THR A C     1 
ATOM   7794  O O     . THR C  1 229 ? -62.510 52.085  -15.233 1.00 46.01 ? 229 THR A O     1 
ATOM   7795  C CB    . THR C  1 229 ? -65.610 51.138  -15.257 1.00 43.86 ? 229 THR A CB    1 
ATOM   7796  O OG1   . THR C  1 229 ? -66.971 51.391  -15.628 1.00 39.98 ? 229 THR A OG1   1 
ATOM   7797  C CG2   . THR C  1 229 ? -65.392 51.693  -13.857 1.00 44.39 ? 229 THR A CG2   1 
ATOM   7798  N N     . LEU C  1 230 ? -62.732 50.296  -16.590 1.00 44.54 ? 230 LEU A N     1 
ATOM   7799  C CA    . LEU C  1 230 ? -61.383 49.791  -16.310 1.00 42.98 ? 230 LEU A CA    1 
ATOM   7800  C C     . LEU C  1 230 ? -60.318 50.565  -17.070 1.00 38.95 ? 230 LEU A C     1 
ATOM   7801  O O     . LEU C  1 230 ? -59.278 50.921  -16.508 1.00 39.69 ? 230 LEU A O     1 
ATOM   7802  C CB    . LEU C  1 230 ? -61.274 48.314  -16.676 1.00 42.91 ? 230 LEU A CB    1 
ATOM   7803  C CG    . LEU C  1 230 ? -62.194 47.303  -16.017 1.00 43.29 ? 230 LEU A CG    1 
ATOM   7804  C CD1   . LEU C  1 230 ? -62.311 46.134  -16.957 1.00 46.42 ? 230 LEU A CD1   1 
ATOM   7805  C CD2   . LEU C  1 230 ? -61.655 46.857  -14.678 1.00 43.85 ? 230 LEU A CD2   1 
ATOM   7806  N N     . TRP C  1 231 ? -60.531 50.787  -18.364 1.00 41.24 ? 231 TRP A N     1 
ATOM   7807  C CA    . TRP C  1 231 ? -59.620 51.661  -19.084 1.00 43.54 ? 231 TRP A CA    1 
ATOM   7808  C C     . TRP C  1 231 ? -59.562 53.029  -18.416 1.00 43.44 ? 231 TRP A C     1 
ATOM   7809  O O     . TRP C  1 231 ? -58.490 53.638  -18.303 1.00 41.73 ? 231 TRP A O     1 
ATOM   7810  C CB    . TRP C  1 231 ? -60.040 51.788  -20.548 1.00 36.23 ? 231 TRP A CB    1 
ATOM   7811  C CG    . TRP C  1 231 ? -59.059 52.595  -21.267 1.00 34.68 ? 231 TRP A CG    1 
ATOM   7812  C CD1   . TRP C  1 231 ? -59.106 53.934  -21.495 1.00 32.12 ? 231 TRP A CD1   1 
ATOM   7813  C CD2   . TRP C  1 231 ? -57.824 52.134  -21.801 1.00 36.14 ? 231 TRP A CD2   1 
ATOM   7814  N NE1   . TRP C  1 231 ? -57.984 54.336  -22.167 1.00 34.99 ? 231 TRP A NE1   1 
ATOM   7815  C CE2   . TRP C  1 231 ? -57.177 53.248  -22.366 1.00 32.24 ? 231 TRP A CE2   1 
ATOM   7816  C CE3   . TRP C  1 231 ? -57.204 50.884  -21.861 1.00 33.68 ? 231 TRP A CE3   1 
ATOM   7817  C CZ2   . TRP C  1 231 ? -55.945 53.155  -22.977 1.00 30.09 ? 231 TRP A CZ2   1 
ATOM   7818  C CZ3   . TRP C  1 231 ? -55.990 50.786  -22.473 1.00 32.24 ? 231 TRP A CZ3   1 
ATOM   7819  C CH2   . TRP C  1 231 ? -55.364 51.918  -23.024 1.00 34.51 ? 231 TRP A CH2   1 
ATOM   7820  N N     . SER C  1 232 ? -60.701 53.484  -17.897 1.00 47.46 ? 232 SER A N     1 
ATOM   7821  C CA    . SER C  1 232 ? -60.825 54.858  -17.440 1.00 43.60 ? 232 SER A CA    1 
ATOM   7822  C C     . SER C  1 232 ? -60.024 55.101  -16.176 1.00 40.12 ? 232 SER A C     1 
ATOM   7823  O O     . SER C  1 232 ? -59.364 56.140  -16.040 1.00 44.33 ? 232 SER A O     1 
ATOM   7824  C CB    . SER C  1 232 ? -62.293 55.182  -17.201 1.00 44.82 ? 232 SER A CB    1 
ATOM   7825  O OG    . SER C  1 232 ? -62.531 56.551  -17.455 1.00 56.92 ? 232 SER A OG    1 
ATOM   7826  N N     . GLN C  1 233 ? -60.072 54.158  -15.243 1.00 39.13 ? 233 GLN A N     1 
ATOM   7827  C CA    . GLN C  1 233 ? -59.523 54.374  -13.912 1.00 44.77 ? 233 GLN A CA    1 
ATOM   7828  C C     . GLN C  1 233 ? -58.130 53.790  -13.727 1.00 49.63 ? 233 GLN A C     1 
ATOM   7829  O O     . GLN C  1 233 ? -57.525 54.008  -12.669 1.00 46.21 ? 233 GLN A O     1 
ATOM   7830  C CB    . GLN C  1 233 ? -60.469 53.786  -12.858 1.00 41.62 ? 233 GLN A CB    1 
ATOM   7831  C CG    . GLN C  1 233 ? -61.751 54.590  -12.667 1.00 42.97 ? 233 GLN A CG    1 
ATOM   7832  C CD    . GLN C  1 233 ? -62.719 53.912  -11.731 1.00 44.14 ? 233 GLN A CD    1 
ATOM   7833  O OE1   . GLN C  1 233 ? -62.531 52.751  -11.384 1.00 44.94 ? 233 GLN A OE1   1 
ATOM   7834  N NE2   . GLN C  1 233 ? -63.754 54.632  -11.306 1.00 44.73 ? 233 GLN A NE2   1 
ATOM   7835  N N     . LEU C  1 234 ? -57.610 53.058  -14.728 1.00 47.75 ? 234 LEU A N     1 
ATOM   7836  C CA    . LEU C  1 234 ? -56.273 52.475  -14.670 1.00 45.22 ? 234 LEU A CA    1 
ATOM   7837  C C     . LEU C  1 234 ? -55.415 52.896  -15.861 1.00 45.86 ? 234 LEU A C     1 
ATOM   7838  O O     . LEU C  1 234 ? -54.460 52.191  -16.207 1.00 50.52 ? 234 LEU A O     1 
ATOM   7839  C CB    . LEU C  1 234 ? -56.338 50.944  -14.593 1.00 43.29 ? 234 LEU A CB    1 
ATOM   7840  C CG    . LEU C  1 234 ? -57.250 50.263  -13.573 1.00 37.46 ? 234 LEU A CG    1 
ATOM   7841  C CD1   . LEU C  1 234 ? -57.310 48.794  -13.891 1.00 36.79 ? 234 LEU A CD1   1 
ATOM   7842  C CD2   . LEU C  1 234 ? -56.792 50.468  -12.136 1.00 38.97 ? 234 LEU A CD2   1 
ATOM   7843  N N     . THR C  1 235 ? -55.743 54.014  -16.508 1.00 46.50 ? 235 THR A N     1 
ATOM   7844  C CA    . THR C  1 235 ? -54.892 54.616  -17.524 1.00 41.66 ? 235 THR A CA    1 
ATOM   7845  C C     . THR C  1 235 ? -54.676 56.076  -17.168 1.00 43.88 ? 235 THR A C     1 
ATOM   7846  O O     . THR C  1 235 ? -55.552 56.714  -16.576 1.00 46.47 ? 235 THR A O     1 
ATOM   7847  C CB    . THR C  1 235 ? -55.514 54.533  -18.919 1.00 37.10 ? 235 THR A CB    1 
ATOM   7848  O OG1   . THR C  1 235 ? -56.817 55.121  -18.886 1.00 40.47 ? 235 THR A OG1   1 
ATOM   7849  C CG2   . THR C  1 235 ? -55.647 53.096  -19.362 1.00 36.95 ? 235 THR A CG2   1 
ATOM   7850  N N     . ASP C  1 236 ? -53.503 56.595  -17.514 1.00 41.39 ? 236 ASP A N     1 
ATOM   7851  C CA    . ASP C  1 236 ? -53.257 58.036  -17.524 1.00 39.39 ? 236 ASP A CA    1 
ATOM   7852  C C     . ASP C  1 236 ? -52.482 58.336  -18.799 1.00 44.00 ? 236 ASP A C     1 
ATOM   7853  O O     . ASP C  1 236 ? -52.462 57.533  -19.738 1.00 40.01 ? 236 ASP A O     1 
ATOM   7854  C CB    . ASP C  1 236 ? -52.528 58.500  -16.258 1.00 32.58 ? 236 ASP A CB    1 
ATOM   7855  C CG    . ASP C  1 236 ? -51.473 57.529  -15.809 1.00 40.86 ? 236 ASP A CG    1 
ATOM   7856  O OD1   . ASP C  1 236 ? -51.152 56.610  -16.584 1.00 47.93 ? 236 ASP A OD1   1 
ATOM   7857  O OD2   . ASP C  1 236 ? -50.966 57.663  -14.679 1.00 38.61 ? 236 ASP A OD2   1 
ATOM   7858  N N     . THR C  1 237 ? -51.837 59.501  -18.847 1.00 46.17 ? 237 THR A N     1 
ATOM   7859  C CA    . THR C  1 237 ? -51.079 59.845  -20.044 1.00 42.97 ? 237 THR A CA    1 
ATOM   7860  C C     . THR C  1 237 ? -49.792 59.044  -20.133 1.00 45.05 ? 237 THR A C     1 
ATOM   7861  O O     . THR C  1 237 ? -49.324 58.737  -21.237 1.00 48.48 ? 237 THR A O     1 
ATOM   7862  C CB    . THR C  1 237 ? -50.761 61.337  -20.053 1.00 43.66 ? 237 THR A CB    1 
ATOM   7863  O OG1   . THR C  1 237 ? -50.788 61.829  -18.710 1.00 36.14 ? 237 THR A OG1   1 
ATOM   7864  C CG2   . THR C  1 237 ? -51.782 62.097  -20.915 1.00 43.52 ? 237 THR A CG2   1 
ATOM   7865  N N     . GLN C  1 238 ? -49.214 58.703  -18.984 1.00 43.06 ? 238 GLN A N     1 
ATOM   7866  C CA    . GLN C  1 238 ? -48.004 57.899  -18.974 1.00 40.94 ? 238 GLN A CA    1 
ATOM   7867  C C     . GLN C  1 238 ? -48.308 56.457  -19.350 1.00 42.35 ? 238 GLN A C     1 
ATOM   7868  O O     . GLN C  1 238 ? -47.555 55.827  -20.100 1.00 40.30 ? 238 GLN A O     1 
ATOM   7869  C CB    . GLN C  1 238 ? -47.360 57.975  -17.593 1.00 43.40 ? 238 GLN A CB    1 
ATOM   7870  C CG    . GLN C  1 238 ? -47.016 59.402  -17.160 1.00 48.53 ? 238 GLN A CG    1 
ATOM   7871  C CD    . GLN C  1 238 ? -48.179 60.112  -16.436 1.00 54.97 ? 238 GLN A CD    1 
ATOM   7872  O OE1   . GLN C  1 238 ? -48.875 59.519  -15.596 1.00 45.88 ? 238 GLN A OE1   1 
ATOM   7873  N NE2   . GLN C  1 238 ? -48.391 61.386  -16.772 1.00 51.99 ? 238 GLN A NE2   1 
ATOM   7874  N N     . ASN C  1 239 ? -49.418 55.925  -18.858 1.00 44.72 ? 239 ASN A N     1 
ATOM   7875  C CA    . ASN C  1 239 ? -49.778 54.524  -19.050 1.00 43.02 ? 239 ASN A CA    1 
ATOM   7876  C C     . ASN C  1 239 ? -50.913 54.440  -20.052 1.00 42.18 ? 239 ASN A C     1 
ATOM   7877  O O     . ASN C  1 239 ? -52.061 54.755  -19.723 1.00 49.15 ? 239 ASN A O     1 
ATOM   7878  C CB    . ASN C  1 239 ? -50.192 53.884  -17.734 1.00 42.71 ? 239 ASN A CB    1 
ATOM   7879  C CG    . ASN C  1 239 ? -49.081 53.879  -16.727 1.00 47.14 ? 239 ASN A CG    1 
ATOM   7880  O OD1   . ASN C  1 239 ? -48.074 54.588  -16.882 1.00 45.05 ? 239 ASN A OD1   1 
ATOM   7881  N ND2   . ASN C  1 239 ? -49.255 53.084  -15.670 1.00 46.99 ? 239 ASN A ND2   1 
ATOM   7882  N N     . GLN C  1 240 ? -50.600 54.003  -21.264 1.00 44.80 ? 240 GLN A N     1 
ATOM   7883  C CA    . GLN C  1 240 ? -51.617 53.722  -22.263 1.00 40.99 ? 240 GLN A CA    1 
ATOM   7884  C C     . GLN C  1 240 ? -51.764 52.225  -22.510 1.00 40.36 ? 240 GLN A C     1 
ATOM   7885  O O     . GLN C  1 240 ? -52.267 51.817  -23.564 1.00 37.49 ? 240 GLN A O     1 
ATOM   7886  C CB    . GLN C  1 240 ? -51.317 54.469  -23.565 1.00 41.67 ? 240 GLN A CB    1 
ATOM   7887  C CG    . GLN C  1 240 ? -51.712 55.939  -23.530 1.00 39.66 ? 240 GLN A CG    1 
ATOM   7888  C CD    . GLN C  1 240 ? -53.190 56.138  -23.241 1.00 41.21 ? 240 GLN A CD    1 
ATOM   7889  O OE1   . GLN C  1 240 ? -54.048 55.685  -23.999 1.00 43.17 ? 240 GLN A OE1   1 
ATOM   7890  N NE2   . GLN C  1 240 ? -53.495 56.806  -22.134 1.00 38.83 ? 240 GLN A NE2   1 
ATOM   7891  N N     . PHE C  1 241 ? -51.343 51.394  -21.558 1.00 33.35 ? 241 PHE A N     1 
ATOM   7892  C CA    . PHE C  1 241 ? -51.683 49.980  -21.591 1.00 34.30 ? 241 PHE A CA    1 
ATOM   7893  C C     . PHE C  1 241 ? -52.353 49.585  -20.283 1.00 32.50 ? 241 PHE A C     1 
ATOM   7894  O O     . PHE C  1 241 ? -52.094 50.166  -19.223 1.00 34.22 ? 241 PHE A O     1 
ATOM   7895  C CB    . PHE C  1 241 ? -50.456 49.059  -21.798 1.00 32.01 ? 241 PHE A CB    1 
ATOM   7896  C CG    . PHE C  1 241 ? -49.546 49.453  -22.937 1.00 33.26 ? 241 PHE A CG    1 
ATOM   7897  C CD1   . PHE C  1 241 ? -48.571 50.426  -22.761 1.00 36.72 ? 241 PHE A CD1   1 
ATOM   7898  C CD2   . PHE C  1 241 ? -49.611 48.799  -24.151 1.00 31.67 ? 241 PHE A CD2   1 
ATOM   7899  C CE1   . PHE C  1 241 ? -47.701 50.765  -23.789 1.00 34.12 ? 241 PHE A CE1   1 
ATOM   7900  C CE2   . PHE C  1 241 ? -48.740 49.131  -25.174 1.00 32.06 ? 241 PHE A CE2   1 
ATOM   7901  C CZ    . PHE C  1 241 ? -47.783 50.115  -24.989 1.00 27.34 ? 241 PHE A CZ    1 
ATOM   7902  N N     . ILE C  1 242 ? -53.209 48.574  -20.369 1.00 32.76 ? 242 ILE A N     1 
ATOM   7903  C CA    . ILE C  1 242 ? -53.727 47.856  -19.210 1.00 37.70 ? 242 ILE A CA    1 
ATOM   7904  C C     . ILE C  1 242 ? -53.536 46.375  -19.478 1.00 38.66 ? 242 ILE A C     1 
ATOM   7905  O O     . ILE C  1 242 ? -53.679 45.925  -20.620 1.00 37.54 ? 242 ILE A O     1 
ATOM   7906  C CB    . ILE C  1 242 ? -55.216 48.176  -18.953 1.00 37.91 ? 242 ILE A CB    1 
ATOM   7907  C CG1   . ILE C  1 242 ? -55.369 49.644  -18.570 1.00 40.22 ? 242 ILE A CG1   1 
ATOM   7908  C CG2   . ILE C  1 242 ? -55.839 47.243  -17.894 1.00 34.89 ? 242 ILE A CG2   1 
ATOM   7909  C CD1   . ILE C  1 242 ? -56.726 49.950  -18.041 1.00 41.75 ? 242 ILE A CD1   1 
ATOM   7910  N N     . THR C  1 243 ? -53.203 45.619  -18.444 1.00 34.75 ? 243 THR A N     1 
ATOM   7911  C CA    . THR C  1 243 ? -53.058 44.180  -18.580 1.00 33.27 ? 243 THR A CA    1 
ATOM   7912  C C     . THR C  1 243 ? -54.304 43.490  -18.059 1.00 36.42 ? 243 THR A C     1 
ATOM   7913  O O     . THR C  1 243 ? -54.935 43.967  -17.109 1.00 34.64 ? 243 THR A O     1 
ATOM   7914  C CB    . THR C  1 243 ? -51.810 43.696  -17.849 1.00 35.67 ? 243 THR A CB    1 
ATOM   7915  O OG1   . THR C  1 243 ? -50.677 43.886  -18.712 1.00 32.43 ? 243 THR A OG1   1 
ATOM   7916  C CG2   . THR C  1 243 ? -51.916 42.234  -17.474 1.00 35.55 ? 243 THR A CG2   1 
ATOM   7917  N N     . VAL C  1 244 ? -54.678 42.389  -18.721 1.00 34.69 ? 244 VAL A N     1 
ATOM   7918  C CA    . VAL C  1 244 ? -55.909 41.662  -18.438 1.00 31.48 ? 244 VAL A CA    1 
ATOM   7919  C C     . VAL C  1 244 ? -55.630 40.168  -18.506 1.00 34.58 ? 244 VAL A C     1 
ATOM   7920  O O     . VAL C  1 244 ? -55.307 39.647  -19.576 1.00 37.47 ? 244 VAL A O     1 
ATOM   7921  C CB    . VAL C  1 244 ? -57.022 42.023  -19.433 1.00 31.54 ? 244 VAL A CB    1 
ATOM   7922  C CG1   . VAL C  1 244 ? -58.334 41.364  -18.996 1.00 35.61 ? 244 VAL A CG1   1 
ATOM   7923  C CG2   . VAL C  1 244 ? -57.184 43.537  -19.564 1.00 27.41 ? 244 VAL A CG2   1 
ATOM   7924  N N     . GLU C  1 245 ? -55.810 39.460  -17.395 1.00 35.17 ? 245 GLU A N     1 
ATOM   7925  C CA    . GLU C  1 245 ? -55.520 38.036  -17.392 1.00 32.49 ? 245 GLU A CA    1 
ATOM   7926  C C     . GLU C  1 245 ? -56.647 37.234  -16.761 1.00 38.01 ? 245 GLU A C     1 
ATOM   7927  O O     . GLU C  1 245 ? -57.407 37.729  -15.927 1.00 38.59 ? 245 GLU A O     1 
ATOM   7928  C CB    . GLU C  1 245 ? -54.227 37.726  -16.641 1.00 34.35 ? 245 GLU A CB    1 
ATOM   7929  C CG    . GLU C  1 245 ? -53.152 38.785  -16.761 1.00 37.71 ? 245 GLU A CG    1 
ATOM   7930  C CD    . GLU C  1 245 ? -51.899 38.437  -15.972 1.00 43.52 ? 245 GLU A CD    1 
ATOM   7931  O OE1   . GLU C  1 245 ? -51.981 37.625  -15.018 1.00 45.25 ? 245 GLU A OE1   1 
ATOM   7932  O OE2   . GLU C  1 245 ? -50.821 38.974  -16.312 1.00 43.40 ? 245 GLU A OE2   1 
ATOM   7933  N N     . THR C  1 246 ? -56.739 35.978  -17.173 1.00 37.88 ? 246 THR A N     1 
ATOM   7934  C CA    . THR C  1 246 ? -57.461 34.986  -16.403 1.00 35.30 ? 246 THR A CA    1 
ATOM   7935  C C     . THR C  1 246 ? -56.820 34.862  -15.018 1.00 40.78 ? 246 THR A C     1 
ATOM   7936  O O     . THR C  1 246 ? -55.607 35.021  -14.867 1.00 36.23 ? 246 THR A O     1 
ATOM   7937  C CB    . THR C  1 246 ? -57.433 33.662  -17.167 1.00 41.27 ? 246 THR A CB    1 
ATOM   7938  O OG1   . THR C  1 246 ? -57.921 33.888  -18.498 1.00 46.71 ? 246 THR A OG1   1 
ATOM   7939  C CG2   . THR C  1 246 ? -58.309 32.617  -16.504 1.00 42.03 ? 246 THR A CG2   1 
ATOM   7940  N N     . TYR C  1 247 ? -57.646 34.608  -13.990 1.00 44.72 ? 247 TYR A N     1 
ATOM   7941  C CA    . TYR C  1 247 ? -57.215 34.573  -12.587 1.00 36.13 ? 247 TYR A CA    1 
ATOM   7942  C C     . TYR C  1 247 ? -57.446 33.186  -12.005 1.00 32.97 ? 247 TYR A C     1 
ATOM   7943  O O     . TYR C  1 247 ? -58.556 32.655  -12.082 1.00 35.79 ? 247 TYR A O     1 
ATOM   7944  C CB    . TYR C  1 247 ? -57.975 35.616  -11.756 1.00 38.58 ? 247 TYR A CB    1 
ATOM   7945  C CG    . TYR C  1 247 ? -57.452 35.865  -10.355 1.00 35.00 ? 247 TYR A CG    1 
ATOM   7946  C CD1   . TYR C  1 247 ? -57.830 35.050  -9.296  1.00 39.09 ? 247 TYR A CD1   1 
ATOM   7947  C CD2   . TYR C  1 247 ? -56.618 36.946  -10.084 1.00 31.40 ? 247 TYR A CD2   1 
ATOM   7948  C CE1   . TYR C  1 247 ? -57.365 35.285  -8.004  1.00 39.77 ? 247 TYR A CE1   1 
ATOM   7949  C CE2   . TYR C  1 247 ? -56.144 37.190  -8.802  1.00 35.71 ? 247 TYR A CE2   1 
ATOM   7950  C CZ    . TYR C  1 247 ? -56.520 36.360  -7.760  1.00 39.32 ? 247 TYR A CZ    1 
ATOM   7951  O OH    . TYR C  1 247 ? -56.059 36.600  -6.476  1.00 36.15 ? 247 TYR A OH    1 
ATOM   7952  N N     . HIS C  1 248 ? -56.408 32.607  -11.416 1.00 37.73 ? 248 HIS A N     1 
ATOM   7953  C CA    . HIS C  1 248 ? -56.442 31.224  -10.966 1.00 39.93 ? 248 HIS A CA    1 
ATOM   7954  C C     . HIS C  1 248 ? -56.387 31.130  -9.450  1.00 39.71 ? 248 HIS A C     1 
ATOM   7955  O O     . HIS C  1 248 ? -55.796 31.971  -8.765  1.00 38.17 ? 248 HIS A O     1 
ATOM   7956  C CB    . HIS C  1 248 ? -55.276 30.422  -11.537 1.00 37.97 ? 248 HIS A CB    1 
ATOM   7957  C CG    . HIS C  1 248 ? -55.211 30.433  -13.026 1.00 41.14 ? 248 HIS A CG    1 
ATOM   7958  N ND1   . HIS C  1 248 ? -55.623 29.367  -13.797 1.00 45.00 ? 248 HIS A ND1   1 
ATOM   7959  C CD2   . HIS C  1 248 ? -54.773 31.377  -13.892 1.00 42.41 ? 248 HIS A CD2   1 
ATOM   7960  C CE1   . HIS C  1 248 ? -55.442 29.654  -15.075 1.00 46.69 ? 248 HIS A CE1   1 
ATOM   7961  N NE2   . HIS C  1 248 ? -54.926 30.867  -15.160 1.00 42.85 ? 248 HIS A NE2   1 
ATOM   7962  N N     . ARG C  1 249 ? -56.998 30.070  -8.945  1.00 43.31 ? 249 ARG A N     1 
ATOM   7963  C CA    . ARG C  1 249 ? -56.932 29.741  -7.531  1.00 52.33 ? 249 ARG A CA    1 
ATOM   7964  C C     . ARG C  1 249 ? -55.570 29.103  -7.275  1.00 49.49 ? 249 ARG A C     1 
ATOM   7965  O O     . ARG C  1 249 ? -55.266 28.022  -7.793  1.00 52.81 ? 249 ARG A O     1 
ATOM   7966  C CB    . ARG C  1 249 ? -58.094 28.824  -7.155  1.00 51.24 ? 249 ARG A CB    1 
ATOM   7967  C CG    . ARG C  1 249 ? -58.167 28.435  -5.683  1.00 59.83 ? 249 ARG A CG    1 
ATOM   7968  C CD    . ARG C  1 249 ? -59.568 28.680  -5.097  1.00 65.85 ? 249 ARG A CD    1 
ATOM   7969  N NE    . ARG C  1 249 ? -59.891 27.750  -4.019  1.00 58.30 ? 249 ARG A NE    1 
ATOM   7970  C CZ    . ARG C  1 249 ? -59.515 27.887  -2.756  1.00 62.17 ? 249 ARG A CZ    1 
ATOM   7971  N NH1   . ARG C  1 249 ? -58.825 28.941  -2.349  1.00 52.87 ? 249 ARG A NH1   1 
ATOM   7972  N NH2   . ARG C  1 249 ? -59.832 26.934  -1.880  1.00 65.96 ? 249 ARG A NH2   1 
ATOM   7973  N N     . ALA C  1 250 ? -54.740 29.785  -6.501  1.00 43.49 ? 250 ALA A N     1 
ATOM   7974  C CA    . ALA C  1 250 ? -53.372 29.374  -6.266  1.00 44.46 ? 250 ALA A CA    1 
ATOM   7975  C C     . ALA C  1 250 ? -53.290 28.588  -4.962  1.00 50.10 ? 250 ALA A C     1 
ATOM   7976  O O     . ALA C  1 250 ? -53.681 29.097  -3.903  1.00 48.72 ? 250 ALA A O     1 
ATOM   7977  C CB    . ALA C  1 250 ? -52.462 30.602  -6.207  1.00 42.34 ? 250 ALA A CB    1 
ATOM   7978  N N     . ASP C  1 251 ? -52.763 27.360  -5.028  1.00 43.69 ? 251 ASP A N     1 
ATOM   7979  C CA    . ASP C  1 251 ? -52.379 26.698  -3.787  1.00 38.32 ? 251 ASP A CA    1 
ATOM   7980  C C     . ASP C  1 251 ? -51.378 27.554  -3.032  1.00 41.74 ? 251 ASP A C     1 
ATOM   7981  O O     . ASP C  1 251 ? -51.572 27.863  -1.852  1.00 44.18 ? 251 ASP A O     1 
ATOM   7982  C CB    . ASP C  1 251 ? -51.801 25.313  -4.064  1.00 37.80 ? 251 ASP A CB    1 
ATOM   7983  C CG    . ASP C  1 251 ? -51.237 24.651  -2.805  1.00 40.91 ? 251 ASP A CG    1 
ATOM   7984  O OD1   . ASP C  1 251 ? -51.979 24.512  -1.809  1.00 46.42 ? 251 ASP A OD1   1 
ATOM   7985  O OD2   . ASP C  1 251 ? -50.047 24.275  -2.805  1.00 45.46 ? 251 ASP A OD2   1 
ATOM   7986  N N     . GLN C  1 252 ? -50.318 27.986  -3.721  1.00 40.26 ? 252 GLN A N     1 
ATOM   7987  C CA    . GLN C  1 252 ? -49.230 28.742  -3.125  1.00 37.94 ? 252 GLN A CA    1 
ATOM   7988  C C     . GLN C  1 252 ? -49.057 30.062  -3.862  1.00 35.78 ? 252 GLN A C     1 
ATOM   7989  O O     . GLN C  1 252 ? -49.113 30.099  -5.094  1.00 40.37 ? 252 GLN A O     1 
ATOM   7990  C CB    . GLN C  1 252 ? -47.927 27.943  -3.174  1.00 39.62 ? 252 GLN A CB    1 
ATOM   7991  C CG    . GLN C  1 252 ? -47.103 28.072  -1.889  1.00 49.72 ? 252 GLN A CG    1 
ATOM   7992  C CD    . GLN C  1 252 ? -47.775 27.384  -0.703  1.00 52.01 ? 252 GLN A CD    1 
ATOM   7993  O OE1   . GLN C  1 252 ? -48.038 26.179  -0.746  1.00 53.51 ? 252 GLN A OE1   1 
ATOM   7994  N NE2   . GLN C  1 252 ? -48.066 28.148  0.354   1.00 46.51 ? 252 GLN A NE2   1 
ATOM   7995  N N     . ARG C  1 253 ? -48.872 31.144  -3.103  1.00 29.68 ? 253 ARG A N     1 
ATOM   7996  C CA    . ARG C  1 253 ? -48.506 32.451  -3.643  1.00 30.38 ? 253 ARG A CA    1 
ATOM   7997  C C     . ARG C  1 253 ? -47.122 32.794  -3.134  1.00 33.04 ? 253 ARG A C     1 
ATOM   7998  O O     . ARG C  1 253 ? -46.909 32.882  -1.919  1.00 33.80 ? 253 ARG A O     1 
ATOM   7999  C CB    . ARG C  1 253 ? -49.479 33.544  -3.223  1.00 27.97 ? 253 ARG A CB    1 
ATOM   8000  C CG    . ARG C  1 253 ? -50.917 33.199  -3.468  1.00 34.95 ? 253 ARG A CG    1 
ATOM   8001  C CD    . ARG C  1 253 ? -51.785 34.433  -3.372  1.00 37.94 ? 253 ARG A CD    1 
ATOM   8002  N NE    . ARG C  1 253 ? -52.522 34.696  -4.601  1.00 43.18 ? 253 ARG A NE    1 
ATOM   8003  C CZ    . ARG C  1 253 ? -53.580 33.999  -4.991  1.00 36.87 ? 253 ARG A CZ    1 
ATOM   8004  N NH1   . ARG C  1 253 ? -53.995 32.941  -4.316  1.00 41.03 ? 253 ARG A NH1   1 
ATOM   8005  N NH2   . ARG C  1 253 ? -54.232 34.367  -6.086  1.00 35.02 ? 253 ARG A NH2   1 
ATOM   8006  N N     . PHE C  1 254 ? -46.185 32.988  -4.051  1.00 29.24 ? 254 PHE A N     1 
ATOM   8007  C CA    . PHE C  1 254 ? -44.794 33.097  -3.661  1.00 30.81 ? 254 PHE A CA    1 
ATOM   8008  C C     . PHE C  1 254 ? -44.100 34.175  -4.492  1.00 27.49 ? 254 PHE A C     1 
ATOM   8009  O O     . PHE C  1 254 ? -44.685 34.773  -5.399  1.00 31.83 ? 254 PHE A O     1 
ATOM   8010  C CB    . PHE C  1 254 ? -44.115 31.730  -3.809  1.00 30.81 ? 254 PHE A CB    1 
ATOM   8011  C CG    . PHE C  1 254 ? -43.896 31.332  -5.237  1.00 34.61 ? 254 PHE A CG    1 
ATOM   8012  C CD1   . PHE C  1 254 ? -42.731 31.702  -5.907  1.00 33.91 ? 254 PHE A CD1   1 
ATOM   8013  C CD2   . PHE C  1 254 ? -44.865 30.621  -5.926  1.00 34.49 ? 254 PHE A CD2   1 
ATOM   8014  C CE1   . PHE C  1 254 ? -42.530 31.368  -7.239  1.00 31.99 ? 254 PHE A CE1   1 
ATOM   8015  C CE2   . PHE C  1 254 ? -44.672 30.264  -7.259  1.00 34.46 ? 254 PHE A CE2   1 
ATOM   8016  C CZ    . PHE C  1 254 ? -43.496 30.639  -7.921  1.00 33.42 ? 254 PHE A CZ    1 
ATOM   8017  N N     . PHE C  1 255 ? -42.832 34.416  -4.171  1.00 32.21 ? 255 PHE A N     1 
ATOM   8018  C CA    . PHE C  1 255 ? -41.912 35.135  -5.043  1.00 30.14 ? 255 PHE A CA    1 
ATOM   8019  C C     . PHE C  1 255 ? -40.482 34.756  -4.650  1.00 30.53 ? 255 PHE A C     1 
ATOM   8020  O O     . PHE C  1 255 ? -40.236 34.139  -3.603  1.00 25.98 ? 255 PHE A O     1 
ATOM   8021  C CB    . PHE C  1 255 ? -42.157 36.657  -5.007  1.00 29.39 ? 255 PHE A CB    1 
ATOM   8022  C CG    . PHE C  1 255 ? -41.940 37.296  -3.652  1.00 30.37 ? 255 PHE A CG    1 
ATOM   8023  C CD1   . PHE C  1 255 ? -42.978 37.405  -2.751  1.00 31.26 ? 255 PHE A CD1   1 
ATOM   8024  C CD2   . PHE C  1 255 ? -40.700 37.815  -3.295  1.00 32.67 ? 255 PHE A CD2   1 
ATOM   8025  C CE1   . PHE C  1 255 ? -42.778 37.994  -1.498  1.00 34.93 ? 255 PHE A CE1   1 
ATOM   8026  C CE2   . PHE C  1 255 ? -40.495 38.405  -2.047  1.00 29.65 ? 255 PHE A CE2   1 
ATOM   8027  C CZ    . PHE C  1 255 ? -41.535 38.492  -1.152  1.00 26.76 ? 255 PHE A CZ    1 
ATOM   8028  N N     . PHE C  1 256 ? -39.539 35.108  -5.535  1.00 31.50 ? 256 PHE A N     1 
ATOM   8029  C CA    . PHE C  1 256 ? -38.116 34.842  -5.368  1.00 26.35 ? 256 PHE A CA    1 
ATOM   8030  C C     . PHE C  1 256 ? -37.346 36.152  -5.486  1.00 25.23 ? 256 PHE A C     1 
ATOM   8031  O O     . PHE C  1 256 ? -37.600 36.941  -6.394  1.00 25.88 ? 256 PHE A O     1 
ATOM   8032  C CB    . PHE C  1 256 ? -37.580 33.857  -6.444  1.00 28.96 ? 256 PHE A CB    1 
ATOM   8033  C CG    . PHE C  1 256 ? -38.253 32.497  -6.464  1.00 26.96 ? 256 PHE A CG    1 
ATOM   8034  C CD1   . PHE C  1 256 ? -38.874 31.979  -5.351  1.00 31.52 ? 256 PHE A CD1   1 
ATOM   8035  C CD2   . PHE C  1 256 ? -38.230 31.723  -7.617  1.00 30.49 ? 256 PHE A CD2   1 
ATOM   8036  C CE1   . PHE C  1 256 ? -39.481 30.721  -5.398  1.00 32.88 ? 256 PHE A CE1   1 
ATOM   8037  C CE2   . PHE C  1 256 ? -38.835 30.459  -7.663  1.00 31.25 ? 256 PHE A CE2   1 
ATOM   8038  C CZ    . PHE C  1 256 ? -39.457 29.961  -6.553  1.00 27.67 ? 256 PHE A CZ    1 
ATOM   8039  N N     . GLU C  1 257 ? -36.384 36.377  -4.598  1.00 27.31 ? 257 GLU A N     1 
ATOM   8040  C CA    . GLU C  1 257 ? -35.588 37.598  -4.611  1.00 23.39 ? 257 GLU A CA    1 
ATOM   8041  C C     . GLU C  1 257 ? -34.179 37.295  -5.076  1.00 27.12 ? 257 GLU A C     1 
ATOM   8042  O O     . GLU C  1 257 ? -33.517 36.404  -4.535  1.00 28.28 ? 257 GLU A O     1 
ATOM   8043  C CB    . GLU C  1 257 ? -35.508 38.232  -3.236  1.00 22.96 ? 257 GLU A CB    1 
ATOM   8044  C CG    . GLU C  1 257 ? -34.993 39.659  -3.240  1.00 26.42 ? 257 GLU A CG    1 
ATOM   8045  C CD    . GLU C  1 257 ? -35.739 40.533  -2.245  1.00 29.12 ? 257 GLU A CD    1 
ATOM   8046  O OE1   . GLU C  1 257 ? -36.362 39.970  -1.302  1.00 28.80 ? 257 GLU A OE1   1 
ATOM   8047  O OE2   . GLU C  1 257 ? -35.704 41.774  -2.400  1.00 27.51 ? 257 GLU A OE2   1 
ATOM   8048  N N     . TYR C  1 258 ? -33.712 38.063  -6.042  1.00 28.29 ? 258 TYR A N     1 
ATOM   8049  C CA    . TYR C  1 258 ? -32.368 37.900  -6.558  1.00 32.07 ? 258 TYR A CA    1 
ATOM   8050  C C     . TYR C  1 258 ? -31.578 39.183  -6.351  1.00 31.95 ? 258 TYR A C     1 
ATOM   8051  O O     . TYR C  1 258 ? -32.131 40.261  -6.092  1.00 25.77 ? 258 TYR A O     1 
ATOM   8052  C CB    . TYR C  1 258 ? -32.383 37.521  -8.054  1.00 28.56 ? 258 TYR A CB    1 
ATOM   8053  C CG    . TYR C  1 258 ? -33.090 36.211  -8.318  1.00 23.47 ? 258 TYR A CG    1 
ATOM   8054  C CD1   . TYR C  1 258 ? -34.466 36.151  -8.444  1.00 23.91 ? 258 TYR A CD1   1 
ATOM   8055  C CD2   . TYR C  1 258 ? -32.377 35.037  -8.414  1.00 24.62 ? 258 TYR A CD2   1 
ATOM   8056  C CE1   . TYR C  1 258 ? -35.106 34.949  -8.665  1.00 24.21 ? 258 TYR A CE1   1 
ATOM   8057  C CE2   . TYR C  1 258 ? -33.004 33.841  -8.629  1.00 24.69 ? 258 TYR A CE2   1 
ATOM   8058  C CZ    . TYR C  1 258 ? -34.365 33.800  -8.752  1.00 24.18 ? 258 TYR A CZ    1 
ATOM   8059  O OH    . TYR C  1 258 ? -34.981 32.591  -8.969  1.00 29.98 ? 258 TYR A OH    1 
ATOM   8060  N N     . HIS C  1 259 ? -30.266 39.046  -6.459  1.00 32.91 ? 259 HIS A N     1 
ATOM   8061  C CA    . HIS C  1 259 ? -29.388 40.191  -6.591  1.00 32.31 ? 259 HIS A CA    1 
ATOM   8062  C C     . HIS C  1 259 ? -28.606 40.046  -7.880  1.00 29.57 ? 259 HIS A C     1 
ATOM   8063  O O     . HIS C  1 259 ? -28.231 38.933  -8.260  1.00 36.01 ? 259 HIS A O     1 
ATOM   8064  C CB    . HIS C  1 259 ? -28.428 40.336  -5.429  1.00 24.40 ? 259 HIS A CB    1 
ATOM   8065  C CG    . HIS C  1 259 ? -27.716 41.639  -5.443  1.00 22.15 ? 259 HIS A CG    1 
ATOM   8066  N ND1   . HIS C  1 259 ? -26.399 41.760  -5.821  1.00 23.85 ? 259 HIS A ND1   1 
ATOM   8067  C CD2   . HIS C  1 259 ? -28.156 42.894  -5.200  1.00 26.39 ? 259 HIS A CD2   1 
ATOM   8068  C CE1   . HIS C  1 259 ? -26.041 43.028  -5.757  1.00 21.09 ? 259 HIS A CE1   1 
ATOM   8069  N NE2   . HIS C  1 259 ? -27.090 43.740  -5.390  1.00 22.65 ? 259 HIS A NE2   1 
ATOM   8070  N N     . LEU C  1 260 ? -28.373 41.167  -8.556  1.00 26.52 ? 260 LEU A N     1 
ATOM   8071  C CA    . LEU C  1 260 ? -27.795 41.163  -9.895  1.00 29.63 ? 260 LEU A CA    1 
ATOM   8072  C C     . LEU C  1 260 ? -26.547 42.035  -9.907  1.00 31.02 ? 260 LEU A C     1 
ATOM   8073  O O     . LEU C  1 260 ? -26.633 43.243  -9.633  1.00 25.51 ? 260 LEU A O     1 
ATOM   8074  C CB    . LEU C  1 260 ? -28.820 41.666  -10.911 1.00 33.61 ? 260 LEU A CB    1 
ATOM   8075  C CG    . LEU C  1 260 ? -29.634 40.556  -11.579 1.00 34.55 ? 260 LEU A CG    1 
ATOM   8076  C CD1   . LEU C  1 260 ? -30.487 39.791  -10.566 1.00 26.80 ? 260 LEU A CD1   1 
ATOM   8077  C CD2   . LEU C  1 260 ? -30.473 41.141  -12.705 1.00 24.79 ? 260 LEU A CD2   1 
ATOM   8078  N N     . ASP C  1 261 ? -25.391 41.429  -10.256 1.00 34.17 ? 261 ASP A N     1 
ATOM   8079  C CA    . ASP C  1 261 ? -24.084 42.023  -9.990  1.00 33.71 ? 261 ASP A CA    1 
ATOM   8080  C C     . ASP C  1 261 ? -23.206 42.252  -11.204 1.00 43.69 ? 261 ASP A C     1 
ATOM   8081  O O     . ASP C  1 261 ? -22.171 42.927  -11.072 1.00 51.11 ? 261 ASP A O     1 
ATOM   8082  C CB    . ASP C  1 261 ? -23.279 41.148  -9.026  1.00 35.09 ? 261 ASP A CB    1 
ATOM   8083  C CG    . ASP C  1 261 ? -22.508 40.095  -9.744  1.00 37.02 ? 261 ASP A CG    1 
ATOM   8084  O OD1   . ASP C  1 261 ? -23.086 39.032  -9.994  1.00 43.43 ? 261 ASP A OD1   1 
ATOM   8085  O OD2   . ASP C  1 261 ? -21.341 40.323  -10.090 1.00 39.43 ? 261 ASP A OD2   1 
ATOM   8086  N N     . GLY C  1 262 ? -23.538 41.702  -12.360 1.00 35.24 ? 262 GLY A N     1 
ATOM   8087  C CA    . GLY C  1 262 ? -22.662 41.852  -13.497 1.00 33.82 ? 262 GLY A CA    1 
ATOM   8088  C C     . GLY C  1 262 ? -21.720 40.693  -13.691 1.00 42.10 ? 262 GLY A C     1 
ATOM   8089  O O     . GLY C  1 262 ? -21.031 40.637  -14.715 1.00 50.39 ? 262 GLY A O     1 
ATOM   8090  N N     . ASP C  1 263 ? -21.669 39.769  -12.736 1.00 42.54 ? 263 ASP A N     1 
ATOM   8091  C CA    . ASP C  1 263 ? -21.053 38.469  -12.946 1.00 40.16 ? 263 ASP A CA    1 
ATOM   8092  C C     . ASP C  1 263 ? -21.982 37.303  -12.627 1.00 39.16 ? 263 ASP A C     1 
ATOM   8093  O O     . ASP C  1 263 ? -21.623 36.165  -12.937 1.00 43.70 ? 263 ASP A O     1 
ATOM   8094  C CB    . ASP C  1 263 ? -19.771 38.330  -12.103 1.00 42.90 ? 263 ASP A CB    1 
ATOM   8095  C CG    . ASP C  1 263 ? -18.679 39.334  -12.510 1.00 59.62 ? 263 ASP A CG    1 
ATOM   8096  O OD1   . ASP C  1 263 ? -17.931 39.064  -13.484 1.00 65.40 ? 263 ASP A OD1   1 
ATOM   8097  O OD2   . ASP C  1 263 ? -18.562 40.398  -11.852 1.00 61.41 ? 263 ASP A OD2   1 
ATOM   8098  N N     . ARG C  1 264 ? -23.162 37.542  -12.050 1.00 36.97 ? 264 ARG A N     1 
ATOM   8099  C CA    . ARG C  1 264 ? -23.977 36.481  -11.469 1.00 37.74 ? 264 ARG A CA    1 
ATOM   8100  C C     . ARG C  1 264 ? -25.341 37.016  -11.084 1.00 38.13 ? 264 ARG A C     1 
ATOM   8101  O O     . ARG C  1 264 ? -25.475 38.166  -10.662 1.00 37.81 ? 264 ARG A O     1 
ATOM   8102  C CB    . ARG C  1 264 ? -23.324 35.891  -10.216 1.00 38.72 ? 264 ARG A CB    1 
ATOM   8103  C CG    . ARG C  1 264 ? -23.498 34.402  -10.101 1.00 42.28 ? 264 ARG A CG    1 
ATOM   8104  C CD    . ARG C  1 264 ? -22.244 33.798  -9.543  1.00 44.85 ? 264 ARG A CD    1 
ATOM   8105  N NE    . ARG C  1 264 ? -21.049 34.420  -10.109 1.00 50.58 ? 264 ARG A NE    1 
ATOM   8106  C CZ    . ARG C  1 264 ? -20.511 34.098  -11.283 1.00 55.00 ? 264 ARG A CZ    1 
ATOM   8107  N NH1   . ARG C  1 264 ? -21.056 33.176  -12.069 1.00 50.50 ? 264 ARG A NH1   1 
ATOM   8108  N NH2   . ARG C  1 264 ? -19.389 34.703  -11.672 1.00 47.41 ? 264 ARG A NH2   1 
ATOM   8109  N N     . ALA C  1 265 ? -26.341 36.150  -11.186 1.00 42.76 ? 265 ALA A N     1 
ATOM   8110  C CA    . ALA C  1 265 ? -27.653 36.376  -10.591 1.00 33.96 ? 265 ALA A CA    1 
ATOM   8111  C C     . ALA C  1 265 ? -27.782 35.393  -9.438  1.00 33.93 ? 265 ALA A C     1 
ATOM   8112  O O     . ALA C  1 265 ? -27.875 34.182  -9.670  1.00 33.66 ? 265 ALA A O     1 
ATOM   8113  C CB    . ALA C  1 265 ? -28.760 36.184  -11.616 1.00 37.16 ? 265 ALA A CB    1 
ATOM   8114  N N     . ARG C  1 266 ? -27.762 35.917  -8.208  1.00 32.27 ? 266 ARG A N     1 
ATOM   8115  C CA    . ARG C  1 266 ? -27.727 35.126  -6.980  1.00 36.26 ? 266 ARG A CA    1 
ATOM   8116  C C     . ARG C  1 266 ? -29.082 35.121  -6.274  1.00 36.51 ? 266 ARG A C     1 
ATOM   8117  O O     . ARG C  1 266 ? -29.634 36.182  -5.955  1.00 36.31 ? 266 ARG A O     1 
ATOM   8118  C CB    . ARG C  1 266 ? -26.664 35.657  -6.012  1.00 42.39 ? 266 ARG A CB    1 
ATOM   8119  C CG    . ARG C  1 266 ? -26.369 34.736  -4.815  1.00 49.31 ? 266 ARG A CG    1 
ATOM   8120  C CD    . ARG C  1 266 ? -25.718 35.511  -3.684  1.00 53.26 ? 266 ARG A CD    1 
ATOM   8121  N NE    . ARG C  1 266 ? -24.273 35.556  -3.875  1.00 70.77 ? 266 ARG A NE    1 
ATOM   8122  C CZ    . ARG C  1 266 ? -23.627 36.599  -4.387  1.00 74.03 ? 266 ARG A CZ    1 
ATOM   8123  N NH1   . ARG C  1 266 ? -24.265 37.715  -4.710  1.00 70.87 ? 266 ARG A NH1   1 
ATOM   8124  N NH2   . ARG C  1 266 ? -22.312 36.519  -4.588  1.00 52.44 ? 266 ARG A NH2   1 
ATOM   8125  N N     . PHE C  1 267 ? -29.578 33.917  -5.993  1.00 30.96 ? 267 PHE A N     1 
ATOM   8126  C CA    . PHE C  1 267 ? -30.813 33.711  -5.246  1.00 25.87 ? 267 PHE A CA    1 
ATOM   8127  C C     . PHE C  1 267 ? -30.635 34.118  -3.781  1.00 30.92 ? 267 PHE A C     1 
ATOM   8128  O O     . PHE C  1 267 ? -29.700 33.678  -3.097  1.00 35.18 ? 267 PHE A O     1 
ATOM   8129  C CB    . PHE C  1 267 ? -31.208 32.235  -5.359  1.00 27.22 ? 267 PHE A CB    1 
ATOM   8130  C CG    . PHE C  1 267 ? -32.620 31.916  -4.938  1.00 33.21 ? 267 PHE A CG    1 
ATOM   8131  C CD1   . PHE C  1 267 ? -32.968 31.839  -3.593  1.00 33.65 ? 267 PHE A CD1   1 
ATOM   8132  C CD2   . PHE C  1 267 ? -33.589 31.633  -5.891  1.00 31.37 ? 267 PHE A CD2   1 
ATOM   8133  C CE1   . PHE C  1 267 ? -34.260 31.523  -3.216  1.00 32.34 ? 267 PHE A CE1   1 
ATOM   8134  C CE2   . PHE C  1 267 ? -34.883 31.311  -5.515  1.00 30.96 ? 267 PHE A CE2   1 
ATOM   8135  C CZ    . PHE C  1 267 ? -35.221 31.265  -4.184  1.00 32.67 ? 267 PHE A CZ    1 
ATOM   8136  N N     . LEU C  1 268 ? -31.535 34.953  -3.288  1.00 25.71 ? 268 LEU A N     1 
ATOM   8137  C CA    . LEU C  1 268 ? -31.409 35.310  -1.890  1.00 29.71 ? 268 LEU A CA    1 
ATOM   8138  C C     . LEU C  1 268 ? -32.315 34.458  -1.019  1.00 25.66 ? 268 LEU A C     1 
ATOM   8139  O O     . LEU C  1 268 ? -31.871 33.928  -0.002  1.00 28.86 ? 268 LEU A O     1 
ATOM   8140  C CB    . LEU C  1 268 ? -31.695 36.795  -1.712  1.00 29.22 ? 268 LEU A CB    1 
ATOM   8141  C CG    . LEU C  1 268 ? -30.918 37.581  -2.760  1.00 27.04 ? 268 LEU A CG    1 
ATOM   8142  C CD1   . LEU C  1 268 ? -31.249 39.062  -2.694  1.00 26.28 ? 268 LEU A CD1   1 
ATOM   8143  C CD2   . LEU C  1 268 ? -29.419 37.334  -2.625  1.00 28.48 ? 268 LEU A CD2   1 
ATOM   8144  N N     . HIS C  1 269 ? -33.563 34.272  -1.433  1.00 27.81 ? 269 HIS A N     1 
ATOM   8145  C CA    . HIS C  1 269 ? -34.571 33.684  -0.568  1.00 29.69 ? 269 HIS A CA    1 
ATOM   8146  C C     . HIS C  1 269 ? -35.851 33.507  -1.368  1.00 26.58 ? 269 HIS A C     1 
ATOM   8147  O O     . HIS C  1 269 ? -36.081 34.217  -2.341  1.00 30.61 ? 269 HIS A O     1 
ATOM   8148  C CB    . HIS C  1 269 ? -34.828 34.584  0.646   1.00 25.18 ? 269 HIS A CB    1 
ATOM   8149  C CG    . HIS C  1 269 ? -35.612 35.819  0.319   1.00 25.81 ? 269 HIS A CG    1 
ATOM   8150  N ND1   . HIS C  1 269 ? -36.989 35.866  0.386   1.00 28.54 ? 269 HIS A ND1   1 
ATOM   8151  C CD2   . HIS C  1 269 ? -35.218 37.045  -0.100  1.00 29.91 ? 269 HIS A CD2   1 
ATOM   8152  C CE1   . HIS C  1 269 ? -37.409 37.071  0.038   1.00 26.35 ? 269 HIS A CE1   1 
ATOM   8153  N NE2   . HIS C  1 269 ? -36.355 37.809  -0.257  1.00 27.93 ? 269 HIS A NE2   1 
ATOM   8154  N N     . SER C  1 270 ? -36.680 32.559  -0.943  1.00 24.76 ? 270 SER A N     1 
ATOM   8155  C CA    . SER C  1 270 ? -38.061 32.443  -1.380  1.00 25.80 ? 270 SER A CA    1 
ATOM   8156  C C     . SER C  1 270 ? -38.988 32.789  -0.220  1.00 32.73 ? 270 SER A C     1 
ATOM   8157  O O     . SER C  1 270 ? -38.664 32.510  0.939   1.00 34.81 ? 270 SER A O     1 
ATOM   8158  C CB    . SER C  1 270 ? -38.352 31.020  -1.851  1.00 32.30 ? 270 SER A CB    1 
ATOM   8159  O OG    . SER C  1 270 ? -38.626 30.174  -0.742  1.00 30.37 ? 270 SER A OG    1 
ATOM   8160  N N     . SER C  1 271 ? -40.159 33.364  -0.528  1.00 31.21 ? 271 SER A N     1 
ATOM   8161  C CA    . SER C  1 271 ? -41.086 33.830  0.507   1.00 27.61 ? 271 SER A CA    1 
ATOM   8162  C C     . SER C  1 271 ? -42.537 33.657  0.075   1.00 33.05 ? 271 SER A C     1 
ATOM   8163  O O     . SER C  1 271 ? -42.841 33.553  -1.115  1.00 33.21 ? 271 SER A O     1 
ATOM   8164  C CB    . SER C  1 271 ? -40.855 35.299  0.843   1.00 25.65 ? 271 SER A CB    1 
ATOM   8165  O OG    . SER C  1 271 ? -39.662 35.426  1.593   1.00 35.31 ? 271 SER A OG    1 
ATOM   8166  N N     . ILE C  1 272 ? -43.448 33.677  1.054   1.00 31.46 ? 272 ILE A N     1 
ATOM   8167  C CA    . ILE C  1 272 ? -44.866 33.387  0.814   1.00 31.22 ? 272 ILE A CA    1 
ATOM   8168  C C     . ILE C  1 272 ? -45.701 34.638  1.049   1.00 26.65 ? 272 ILE A C     1 
ATOM   8169  O O     . ILE C  1 272 ? -45.676 35.210  2.139   1.00 24.63 ? 272 ILE A O     1 
ATOM   8170  C CB    . ILE C  1 272 ? -45.372 32.243  1.701   1.00 31.46 ? 272 ILE A CB    1 
ATOM   8171  C CG1   . ILE C  1 272 ? -44.425 31.047  1.636   1.00 32.55 ? 272 ILE A CG1   1 
ATOM   8172  C CG2   . ILE C  1 272 ? -46.768 31.845  1.287   1.00 39.09 ? 272 ILE A CG2   1 
ATOM   8173  C CD1   . ILE C  1 272 ? -45.035 29.731  2.168   1.00 38.16 ? 272 ILE A CD1   1 
ATOM   8174  N N     . LEU C  1 273 ? -46.471 35.040  0.048   1.00 28.48 ? 273 LEU A N     1 
ATOM   8175  C CA    . LEU C  1 273 ? -47.334 36.211  0.183   1.00 31.26 ? 273 LEU A CA    1 
ATOM   8176  C C     . LEU C  1 273 ? -48.593 35.823  0.948   1.00 33.57 ? 273 LEU A C     1 
ATOM   8177  O O     . LEU C  1 273 ? -49.476 35.150  0.406   1.00 38.47 ? 273 LEU A O     1 
ATOM   8178  C CB    . LEU C  1 273 ? -47.683 36.765  -1.186  1.00 28.38 ? 273 LEU A CB    1 
ATOM   8179  C CG    . LEU C  1 273 ? -46.468 37.213  -1.962  1.00 30.00 ? 273 LEU A CG    1 
ATOM   8180  C CD1   . LEU C  1 273 ? -46.516 36.550  -3.318  1.00 32.66 ? 273 LEU A CD1   1 
ATOM   8181  C CD2   . LEU C  1 273 ? -46.491 38.718  -2.075  1.00 33.73 ? 273 LEU A CD2   1 
ATOM   8182  N N     . LYS C  1 274 ? -48.690 36.243  2.199   1.00 27.80 ? 274 LYS A N     1 
ATOM   8183  C CA    . LYS C  1 274 ? -49.852 35.916  3.000   1.00 31.07 ? 274 LYS A CA    1 
ATOM   8184  C C     . LYS C  1 274 ? -50.881 37.026  2.852   1.00 38.44 ? 274 LYS A C     1 
ATOM   8185  O O     . LYS C  1 274 ? -50.535 38.218  2.807   1.00 33.68 ? 274 LYS A O     1 
ATOM   8186  C CB    . LYS C  1 274 ? -49.484 35.731  4.472   1.00 28.24 ? 274 LYS A CB    1 
ATOM   8187  C CG    . LYS C  1 274 ? -48.307 34.836  4.714   1.00 30.38 ? 274 LYS A CG    1 
ATOM   8188  C CD    . LYS C  1 274 ? -48.465 33.523  4.009   1.00 27.56 ? 274 LYS A CD    1 
ATOM   8189  C CE    . LYS C  1 274 ? -49.483 32.657  4.714   1.00 32.18 ? 274 LYS A CE    1 
ATOM   8190  N NZ    . LYS C  1 274 ? -49.610 31.336  4.050   1.00 31.67 ? 274 LYS A NZ    1 
ATOM   8191  N N     . TYR C  1 275 ? -52.151 36.619  2.796   1.00 39.55 ? 275 TYR A N     1 
ATOM   8192  C CA    . TYR C  1 275 ? -53.285 37.499  2.557   1.00 37.77 ? 275 TYR A CA    1 
ATOM   8193  C C     . TYR C  1 275 ? -54.362 37.247  3.620   1.00 43.01 ? 275 TYR A C     1 
ATOM   8194  O O     . TYR C  1 275 ? -54.203 36.397  4.502   1.00 44.89 ? 275 TYR A O     1 
ATOM   8195  C CB    . TYR C  1 275 ? -53.800 37.299  1.125   1.00 39.74 ? 275 TYR A CB    1 
ATOM   8196  C CG    . TYR C  1 275 ? -52.792 37.736  0.072   1.00 36.42 ? 275 TYR A CG    1 
ATOM   8197  C CD1   . TYR C  1 275 ? -52.698 39.076  -0.314  1.00 36.83 ? 275 TYR A CD1   1 
ATOM   8198  C CD2   . TYR C  1 275 ? -51.927 36.825  -0.521  1.00 34.72 ? 275 TYR A CD2   1 
ATOM   8199  C CE1   . TYR C  1 275 ? -51.781 39.495  -1.251  1.00 32.15 ? 275 TYR A CE1   1 
ATOM   8200  C CE2   . TYR C  1 275 ? -51.000 37.242  -1.477  1.00 34.15 ? 275 TYR A CE2   1 
ATOM   8201  C CZ    . TYR C  1 275 ? -50.936 38.577  -1.836  1.00 35.63 ? 275 TYR A CZ    1 
ATOM   8202  O OH    . TYR C  1 275 ? -50.021 38.997  -2.792  1.00 43.31 ? 275 TYR A OH    1 
ATOM   8203  N N     . GLU C  1 276 ? -55.448 38.028  3.558   1.00 45.08 ? 276 GLU A N     1 
ATOM   8204  C CA    . GLU C  1 276 ? -56.595 37.872  4.452   1.00 48.34 ? 276 GLU A CA    1 
ATOM   8205  C C     . GLU C  1 276 ? -57.467 36.689  4.018   1.00 53.35 ? 276 GLU A C     1 
ATOM   8206  O O     . GLU C  1 276 ? -57.817 36.572  2.840   1.00 50.24 ? 276 GLU A O     1 
ATOM   8207  C CB    . GLU C  1 276 ? -57.444 39.152  4.458   1.00 47.90 ? 276 GLU A CB    1 
ATOM   8208  C CG    . GLU C  1 276 ? -56.745 40.421  4.950   1.00 50.33 ? 276 GLU A CG    1 
ATOM   8209  C CD    . GLU C  1 276 ? -57.015 41.652  4.070   1.00 56.03 ? 276 GLU A CD    1 
ATOM   8210  O OE1   . GLU C  1 276 ? -57.799 41.546  3.098   1.00 55.78 ? 276 GLU A OE1   1 
ATOM   8211  O OE2   . GLU C  1 276 ? -56.422 42.727  4.330   1.00 55.93 ? 276 GLU A OE2   1 
ATOM   8212  N N     . GLN C  1 277 ? -57.842 35.824  4.968   1.00 49.77 ? 277 GLN A N     1 
ATOM   8213  C CA    . GLN C  1 277 ? -58.830 34.782  4.696   1.00 49.66 ? 277 GLN A CA    1 
ATOM   8214  C C     . GLN C  1 277 ? -60.218 35.316  5.012   1.00 49.61 ? 277 GLN A C     1 
ATOM   8215  O O     . GLN C  1 277 ? -60.519 35.626  6.166   1.00 54.27 ? 277 GLN A O     1 
ATOM   8216  C CB    . GLN C  1 277 ? -58.568 33.516  5.502   1.00 47.65 ? 277 GLN A CB    1 
ATOM   8217  C CG    . GLN C  1 277 ? -57.989 32.412  4.670   1.00 54.03 ? 277 GLN A CG    1 
ATOM   8218  C CD    . GLN C  1 277 ? -56.492 32.511  4.598   1.00 63.00 ? 277 GLN A CD    1 
ATOM   8219  O OE1   . GLN C  1 277 ? -55.803 32.296  5.598   1.00 66.26 ? 277 GLN A OE1   1 
ATOM   8220  N NE2   . GLN C  1 277 ? -55.974 32.885  3.428   1.00 59.70 ? 277 GLN A NE2   1 
ATOM   8221  N N     . LEU C  1 278 ? -61.055 35.370  4.021   1.00 51.03 ? 278 LEU A N     1 
ATOM   8222  C CA    . LEU C  1 278 ? -62.274 36.167  4.032   1.00 55.76 ? 278 LEU A CA    1 
ATOM   8223  C C     . LEU C  1 278 ? -63.478 35.355  4.504   1.00 59.09 ? 278 LEU A C     1 
ATOM   8224  O O     . LEU C  1 278 ? -63.493 34.123  4.393   1.00 59.02 ? 278 LEU A O     1 
ATOM   8225  C CB    . LEU C  1 278 ? -62.531 36.721  2.633   1.00 58.37 ? 278 LEU A CB    1 
ATOM   8226  C CG    . LEU C  1 278 ? -61.316 37.261  1.885   1.00 54.76 ? 278 LEU A CG    1 
ATOM   8227  C CD1   . LEU C  1 278 ? -60.561 36.148  1.155   1.00 50.14 ? 278 LEU A CD1   1 
ATOM   8228  C CD2   . LEU C  1 278 ? -61.806 38.306  0.924   1.00 49.47 ? 278 LEU A CD2   1 
ATOM   8229  N N     . PRO C  1 279 ? -64.519 36.025  5.022   1.00 59.49 ? 279 PRO A N     1 
ATOM   8230  C CA    . PRO C  1 279 ? -65.632 35.293  5.644   1.00 55.36 ? 279 PRO A CA    1 
ATOM   8231  C C     . PRO C  1 279 ? -66.287 34.304  4.689   1.00 60.42 ? 279 PRO A C     1 
ATOM   8232  O O     . PRO C  1 279 ? -66.562 34.621  3.529   1.00 59.58 ? 279 PRO A O     1 
ATOM   8233  C CB    . PRO C  1 279 ? -66.612 36.406  6.045   1.00 52.35 ? 279 PRO A CB    1 
ATOM   8234  C CG    . PRO C  1 279 ? -65.837 37.657  6.023   1.00 50.15 ? 279 PRO A CG    1 
ATOM   8235  C CD    . PRO C  1 279 ? -64.747 37.483  5.031   1.00 55.37 ? 279 PRO A CD    1 
ATOM   8236  N N     . GLU C  1 280 ? -66.547 33.099  5.200   1.00 60.55 ? 280 GLU A N     1 
ATOM   8237  C CA    . GLU C  1 280 ? -67.295 32.058  4.487   1.00 63.22 ? 280 GLU A CA    1 
ATOM   8238  C C     . GLU C  1 280 ? -66.802 31.815  3.056   1.00 67.62 ? 280 GLU A C     1 
ATOM   8239  O O     . GLU C  1 280 ? -67.561 31.961  2.090   1.00 68.03 ? 280 GLU A O     1 
ATOM   8240  C CB    . GLU C  1 280 ? -68.790 32.401  4.463   1.00 57.15 ? 280 GLU A CB    1 
ATOM   8241  C CG    . GLU C  1 280 ? -69.554 31.901  5.679   1.00 69.95 ? 280 GLU A CG    1 
ATOM   8242  C CD    . GLU C  1 280 ? -69.843 30.400  5.632   1.00 77.50 ? 280 GLU A CD    1 
ATOM   8243  O OE1   . GLU C  1 280 ? -68.907 29.617  5.339   1.00 72.97 ? 280 GLU A OE1   1 
ATOM   8244  O OE2   . GLU C  1 280 ? -71.003 30.004  5.913   1.00 72.91 ? 280 GLU A OE2   1 
ATOM   8245  N N     . SER C  1 282 ? -68.393 35.890  3.192   1.00 52.85 ? 282 SER A N     1 
ATOM   8246  C CA    . SER C  1 282 ? -68.164 36.973  2.248   1.00 57.84 ? 282 SER A CA    1 
ATOM   8247  C C     . SER C  1 282 ? -67.115 36.593  1.202   1.00 62.08 ? 282 SER A C     1 
ATOM   8248  O O     . SER C  1 282 ? -66.873 35.411  0.965   1.00 62.86 ? 282 SER A O     1 
ATOM   8249  C CB    . SER C  1 282 ? -67.738 38.247  2.984   1.00 59.57 ? 282 SER A CB    1 
ATOM   8250  O OG    . SER C  1 282 ? -67.643 39.341  2.085   1.00 62.20 ? 282 SER A OG    1 
ATOM   8251  N N     . GLY C  1 283 ? -66.501 37.599  0.584   1.00 53.04 ? 283 GLY A N     1 
ATOM   8252  C CA    . GLY C  1 283 ? -65.592 37.353  -0.519  1.00 52.98 ? 283 GLY A CA    1 
ATOM   8253  C C     . GLY C  1 283 ? -65.049 38.653  -1.077  1.00 54.56 ? 283 GLY A C     1 
ATOM   8254  O O     . GLY C  1 283 ? -65.197 39.719  -0.476  1.00 55.53 ? 283 GLY A O     1 
ATOM   8255  N N     . GLY C  1 284 ? -64.408 38.546  -2.243  1.00 52.04 ? 284 GLY A N     1 
ATOM   8256  C CA    . GLY C  1 284 ? -63.789 39.692  -2.890  1.00 48.86 ? 284 GLY A CA    1 
ATOM   8257  C C     . GLY C  1 284 ? -62.334 39.915  -2.505  1.00 52.27 ? 284 GLY A C     1 
ATOM   8258  O O     . GLY C  1 284 ? -61.587 38.955  -2.255  1.00 50.82 ? 284 GLY A O     1 
ATOM   8259  N N     . SER C  1 285 ? -61.920 41.182  -2.427  1.00 48.33 ? 285 SER A N     1 
ATOM   8260  C CA    . SER C  1 285 ? -60.514 41.496  -2.190  1.00 47.81 ? 285 SER A CA    1 
ATOM   8261  C C     . SER C  1 285 ? -60.052 41.019  -0.821  1.00 48.28 ? 285 SER A C     1 
ATOM   8262  O O     . SER C  1 285 ? -60.727 41.241  0.192   1.00 44.80 ? 285 SER A O     1 
ATOM   8263  C CB    . SER C  1 285 ? -60.274 42.998  -2.327  1.00 48.85 ? 285 SER A CB    1 
ATOM   8264  O OG    . SER C  1 285 ? -60.982 43.526  -3.441  1.00 61.11 ? 285 SER A OG    1 
ATOM   8265  N N     . ALA C  1 286 ? -58.878 40.383  -0.804  1.00 44.05 ? 286 ALA A N     1 
ATOM   8266  C CA    . ALA C  1 286 ? -58.208 39.914  0.406   1.00 45.49 ? 286 ALA A CA    1 
ATOM   8267  C C     . ALA C  1 286 ? -56.822 40.551  0.467   1.00 44.57 ? 286 ALA A C     1 
ATOM   8268  O O     . ALA C  1 286 ? -55.861 39.981  -0.052  1.00 50.77 ? 286 ALA A O     1 
ATOM   8269  C CB    . ALA C  1 286 ? -58.114 38.410  0.397   1.00 44.89 ? 286 ALA A CB    1 
ATOM   8270  N N     . LYS C  1 287 ? -56.700 41.707  1.118   1.00 44.03 ? 287 LYS A N     1 
ATOM   8271  C CA    . LYS C  1 287 ? -55.436 42.432  1.050   1.00 47.13 ? 287 LYS A CA    1 
ATOM   8272  C C     . LYS C  1 287 ? -54.354 41.752  1.894   1.00 42.08 ? 287 LYS A C     1 
ATOM   8273  O O     . LYS C  1 287 ? -54.592 40.789  2.624   1.00 41.50 ? 287 LYS A O     1 
ATOM   8274  C CB    . LYS C  1 287 ? -55.610 43.892  1.470   1.00 49.83 ? 287 LYS A CB    1 
ATOM   8275  C CG    . LYS C  1 287 ? -54.763 44.871  0.630   1.00 44.94 ? 287 LYS A CG    1 
ATOM   8276  C CD    . LYS C  1 287 ? -54.906 46.290  1.158   1.00 57.16 ? 287 LYS A CD    1 
ATOM   8277  C CE    . LYS C  1 287 ? -53.717 47.161  0.779   1.00 54.49 ? 287 LYS A CE    1 
ATOM   8278  N NZ    . LYS C  1 287 ? -53.687 48.425  1.582   1.00 50.63 ? 287 LYS A NZ    1 
ATOM   8279  N N     . TRP C  1 288 ? -53.145 42.300  1.783   1.00 44.77 ? 288 TRP A N     1 
ATOM   8280  C CA    . TRP C  1 288 ? -51.909 41.620  2.155   1.00 36.74 ? 288 TRP A CA    1 
ATOM   8281  C C     . TRP C  1 288 ? -51.644 41.763  3.646   1.00 34.82 ? 288 TRP A C     1 
ATOM   8282  O O     . TRP C  1 288 ? -51.712 42.871  4.188   1.00 34.41 ? 288 TRP A O     1 
ATOM   8283  C CB    . TRP C  1 288 ? -50.769 42.216  1.331   1.00 31.99 ? 288 TRP A CB    1 
ATOM   8284  C CG    . TRP C  1 288 ? -49.444 41.721  1.636   1.00 28.77 ? 288 TRP A CG    1 
ATOM   8285  C CD1   . TRP C  1 288 ? -49.040 40.423  1.701   1.00 28.80 ? 288 TRP A CD1   1 
ATOM   8286  C CD2   . TRP C  1 288 ? -48.302 42.519  1.915   1.00 27.83 ? 288 TRP A CD2   1 
ATOM   8287  N NE1   . TRP C  1 288 ? -47.701 40.362  2.012   1.00 28.02 ? 288 TRP A NE1   1 
ATOM   8288  C CE2   . TRP C  1 288 ? -47.226 41.639  2.149   1.00 27.49 ? 288 TRP A CE2   1 
ATOM   8289  C CE3   . TRP C  1 288 ? -48.086 43.893  2.005   1.00 21.64 ? 288 TRP A CE3   1 
ATOM   8290  C CZ2   . TRP C  1 288 ? -45.955 42.092  2.465   1.00 26.73 ? 288 TRP A CZ2   1 
ATOM   8291  C CZ3   . TRP C  1 288 ? -46.834 44.338  2.312   1.00 25.54 ? 288 TRP A CZ3   1 
ATOM   8292  C CH2   . TRP C  1 288 ? -45.774 43.445  2.529   1.00 26.82 ? 288 TRP A CH2   1 
ATOM   8293  N N     . ILE C  1 289 ? -51.370 40.642  4.317   1.00 33.76 ? 289 ILE A N     1 
ATOM   8294  C CA    . ILE C  1 289 ? -51.212 40.650  5.766   1.00 34.86 ? 289 ILE A CA    1 
ATOM   8295  C C     . ILE C  1 289 ? -49.778 40.427  6.198   1.00 31.79 ? 289 ILE A C     1 
ATOM   8296  O O     . ILE C  1 289 ? -49.457 40.708  7.364   1.00 30.35 ? 289 ILE A O     1 
ATOM   8297  C CB    . ILE C  1 289 ? -52.134 39.620  6.458   1.00 38.13 ? 289 ILE A CB    1 
ATOM   8298  C CG1   . ILE C  1 289 ? -51.637 38.190  6.226   1.00 42.15 ? 289 ILE A CG1   1 
ATOM   8299  C CG2   . ILE C  1 289 ? -53.536 39.758  5.956   1.00 38.65 ? 289 ILE A CG2   1 
ATOM   8300  C CD1   . ILE C  1 289 ? -52.001 37.228  7.355   1.00 37.87 ? 289 ILE A CD1   1 
ATOM   8301  N N     . GLY C  1 290 ? -48.918 39.921  5.319   1.00 31.66 ? 290 GLY A N     1 
ATOM   8302  C CA    . GLY C  1 290 ? -47.502 39.802  5.615   1.00 32.06 ? 290 GLY A CA    1 
ATOM   8303  C C     . GLY C  1 290 ? -46.828 38.770  4.713   1.00 34.62 ? 290 GLY A C     1 
ATOM   8304  O O     . GLY C  1 290 ? -47.291 38.482  3.608   1.00 32.25 ? 290 GLY A O     1 
ATOM   8305  N N     . LEU C  1 291 ? -45.727 38.224  5.226   1.00 30.73 ? 291 LEU A N     1 
ATOM   8306  C CA    . LEU C  1 291 ? -44.916 37.270  4.494   1.00 30.02 ? 291 LEU A CA    1 
ATOM   8307  C C     . LEU C  1 291 ? -44.437 36.191  5.459   1.00 28.30 ? 291 LEU A C     1 
ATOM   8308  O O     . LEU C  1 291 ? -44.331 36.422  6.669   1.00 27.80 ? 291 LEU A O     1 
ATOM   8309  C CB    . LEU C  1 291 ? -43.723 37.980  3.798   1.00 32.29 ? 291 LEU A CB    1 
ATOM   8310  C CG    . LEU C  1 291 ? -44.006 38.996  2.656   1.00 28.50 ? 291 LEU A CG    1 
ATOM   8311  C CD1   . LEU C  1 291 ? -42.738 39.610  2.054   1.00 20.42 ? 291 LEU A CD1   1 
ATOM   8312  C CD2   . LEU C  1 291 ? -44.891 38.433  1.549   1.00 30.43 ? 291 LEU A CD2   1 
ATOM   8313  N N     . ASP C  1 292 ? -44.145 35.007  4.903   1.00 28.66 ? 292 ASP A N     1 
ATOM   8314  C CA    . ASP C  1 292 ? -43.648 33.837  5.630   1.00 32.93 ? 292 ASP A CA    1 
ATOM   8315  C C     . ASP C  1 292 ? -42.340 33.365  5.006   1.00 33.28 ? 292 ASP A C     1 
ATOM   8316  O O     . ASP C  1 292 ? -41.951 33.825  3.922   1.00 36.64 ? 292 ASP A O     1 
ATOM   8317  C CB    . ASP C  1 292 ? -44.656 32.678  5.609   1.00 32.90 ? 292 ASP A CB    1 
ATOM   8318  C CG    . ASP C  1 292 ? -45.922 32.972  6.408   1.00 32.93 ? 292 ASP A CG    1 
ATOM   8319  O OD1   . ASP C  1 292 ? -45.996 34.044  7.073   1.00 31.87 ? 292 ASP A OD1   1 
ATOM   8320  O OD2   . ASP C  1 292 ? -46.863 32.140  6.342   1.00 34.31 ? 292 ASP A OD2   1 
ATOM   8321  N N     . SER C  1 293 ? -41.719 32.349  5.685   1.00 34.44 ? 293 SER A N     1 
ATOM   8322  C CA    . SER C  1 293 ? -40.289 32.069  5.794   1.00 34.43 ? 293 SER A CA    1 
ATOM   8323  C C     . SER C  1 293 ? -39.884 31.341  4.512   1.00 38.44 ? 293 SER A C     1 
ATOM   8324  O O     . SER C  1 293 ? -40.491 31.706  3.509   1.00 40.78 ? 293 SER A O     1 
ATOM   8325  C CB    . SER C  1 293 ? -40.130 31.315  7.088   1.00 39.90 ? 293 SER A CB    1 
ATOM   8326  O OG    . SER C  1 293 ? -38.769 31.316  7.431   1.00 43.21 ? 293 SER A OG    1 
ATOM   8327  N N     . PRO C  1 294 ? -38.925 30.292  4.412   1.00 38.62 ? 294 PRO A N     1 
ATOM   8328  C CA    . PRO C  1 294 ? -38.782 29.681  3.101   1.00 33.91 ? 294 PRO A CA    1 
ATOM   8329  C C     . PRO C  1 294 ? -40.138 29.304  2.558   1.00 38.20 ? 294 PRO A C     1 
ATOM   8330  O O     . PRO C  1 294 ? -40.941 28.679  3.259   1.00 41.19 ? 294 PRO A O     1 
ATOM   8331  C CB    . PRO C  1 294 ? -37.910 28.459  3.392   1.00 34.43 ? 294 PRO A CB    1 
ATOM   8332  C CG    . PRO C  1 294 ? -37.731 28.390  4.840   1.00 47.31 ? 294 PRO A CG    1 
ATOM   8333  C CD    . PRO C  1 294 ? -37.871 29.729  5.287   1.00 44.27 ? 294 PRO A CD    1 
ATOM   8334  N N     . SER C  1 295 ? -40.437 29.775  1.360   1.00 35.00 ? 295 SER A N     1 
ATOM   8335  C CA    . SER C  1 295 ? -41.637 29.279  0.734   1.00 34.36 ? 295 SER A CA    1 
ATOM   8336  C C     . SER C  1 295 ? -41.538 27.766  0.637   1.00 34.33 ? 295 SER A C     1 
ATOM   8337  O O     . SER C  1 295 ? -40.466 27.174  0.778   1.00 35.45 ? 295 SER A O     1 
ATOM   8338  C CB    . SER C  1 295 ? -41.818 29.921  -0.637  1.00 34.02 ? 295 SER A CB    1 
ATOM   8339  O OG    . SER C  1 295 ? -40.915 29.360  -1.550  1.00 36.62 ? 295 SER A OG    1 
ATOM   8340  N N     . ARG C  1 296 ? -42.690 27.136  0.466   1.00 37.82 ? 296 ARG A N     1 
ATOM   8341  C CA    . ARG C  1 296 ? -42.738 25.733  0.088   1.00 38.77 ? 296 ARG A CA    1 
ATOM   8342  C C     . ARG C  1 296 ? -42.940 25.576  -1.425  1.00 43.34 ? 296 ARG A C     1 
ATOM   8343  O O     . ARG C  1 296 ? -43.643 24.670  -1.892  1.00 45.88 ? 296 ARG A O     1 
ATOM   8344  C CB    . ARG C  1 296 ? -43.823 25.017  0.884   1.00 41.14 ? 296 ARG A CB    1 
ATOM   8345  C CG    . ARG C  1 296 ? -45.259 25.376  0.446   1.00 55.53 ? 296 ARG A CG    1 
ATOM   8346  C CD    . ARG C  1 296 ? -46.328 24.910  1.441   1.00 60.16 ? 296 ARG A CD    1 
ATOM   8347  N NE    . ARG C  1 296 ? -46.551 25.857  2.525   1.00 54.69 ? 296 ARG A NE    1 
ATOM   8348  C CZ    . ARG C  1 296 ? -45.887 25.851  3.671   1.00 54.44 ? 296 ARG A CZ    1 
ATOM   8349  N NH1   . ARG C  1 296 ? -44.940 24.961  3.912   1.00 54.84 ? 296 ARG A NH1   1 
ATOM   8350  N NH2   . ARG C  1 296 ? -46.185 26.760  4.599   1.00 48.00 ? 296 ARG A NH2   1 
ATOM   8351  N N     . SER C  1 297 ? -42.344 26.470  -2.224  1.00 41.60 ? 297 SER A N     1 
ATOM   8352  C CA    . SER C  1 297 ? -42.487 26.457  -3.688  1.00 40.26 ? 297 SER A CA    1 
ATOM   8353  C C     . SER C  1 297 ? -41.127 26.614  -4.391  1.00 41.55 ? 297 SER A C     1 
ATOM   8354  O O     . SER C  1 297 ? -40.994 27.297  -5.417  1.00 42.01 ? 297 SER A O     1 
ATOM   8355  C CB    . SER C  1 297 ? -43.471 27.530  -4.147  1.00 35.04 ? 297 SER A CB    1 
ATOM   8356  O OG    . SER C  1 297 ? -44.790 27.214  -3.729  1.00 38.24 ? 297 SER A OG    1 
ATOM   8357  N N     . GLU C  1 298 ? -40.096 25.965  -3.848  1.00 41.33 ? 298 GLU A N     1 
ATOM   8358  C CA    . GLU C  1 298 ? -38.748 25.973  -4.421  1.00 35.30 ? 298 GLU A CA    1 
ATOM   8359  C C     . GLU C  1 298 ? -38.475 24.635  -5.104  1.00 36.83 ? 298 GLU A C     1 
ATOM   8360  O O     . GLU C  1 298 ? -37.666 23.823  -4.645  1.00 42.39 ? 298 GLU A O     1 
ATOM   8361  C CB    . GLU C  1 298 ? -37.700 26.219  -3.339  1.00 35.87 ? 298 GLU A CB    1 
ATOM   8362  C CG    . GLU C  1 298 ? -37.659 27.585  -2.687  1.00 37.30 ? 298 GLU A CG    1 
ATOM   8363  C CD    . GLU C  1 298 ? -36.488 27.684  -1.734  1.00 40.05 ? 298 GLU A CD    1 
ATOM   8364  O OE1   . GLU C  1 298 ? -35.529 26.906  -1.938  1.00 40.79 ? 298 GLU A OE1   1 
ATOM   8365  O OE2   . GLU C  1 298 ? -36.515 28.514  -0.793  1.00 38.81 ? 298 GLU A OE2   1 
ATOM   8366  N N     . PHE C  1 299 ? -39.182 24.389  -6.194  1.00 35.27 ? 299 PHE A N     1 
ATOM   8367  C CA    . PHE C  1 299 ? -38.880 23.228  -7.016  1.00 37.28 ? 299 PHE A CA    1 
ATOM   8368  C C     . PHE C  1 299 ? -38.467 23.679  -8.423  1.00 42.41 ? 299 PHE A C     1 
ATOM   8369  O O     . PHE C  1 299 ? -38.356 24.876  -8.723  1.00 40.24 ? 299 PHE A O     1 
ATOM   8370  C CB    . PHE C  1 299 ? -40.047 22.229  -7.048  1.00 41.37 ? 299 PHE A CB    1 
ATOM   8371  C CG    . PHE C  1 299 ? -41.425 22.851  -7.149  1.00 36.87 ? 299 PHE A CG    1 
ATOM   8372  C CD1   . PHE C  1 299 ? -42.136 23.187  -6.015  1.00 36.94 ? 299 PHE A CD1   1 
ATOM   8373  C CD2   . PHE C  1 299 ? -42.033 23.028  -8.385  1.00 38.08 ? 299 PHE A CD2   1 
ATOM   8374  C CE1   . PHE C  1 299 ? -43.420 23.730  -6.110  1.00 38.67 ? 299 PHE A CE1   1 
ATOM   8375  C CE2   . PHE C  1 299 ? -43.319 23.568  -8.493  1.00 36.19 ? 299 PHE A CE2   1 
ATOM   8376  C CZ    . PHE C  1 299 ? -44.010 23.919  -7.359  1.00 38.64 ? 299 PHE A CZ    1 
ATOM   8377  N N     . GLU C  1 300 ? -38.205 22.700  -9.290  1.00 39.61 ? 300 GLU A N     1 
ATOM   8378  C CA    . GLU C  1 300 ? -37.533 23.024  -10.541 1.00 38.68 ? 300 GLU A CA    1 
ATOM   8379  C C     . GLU C  1 300 ? -38.473 23.667  -11.535 1.00 39.97 ? 300 GLU A C     1 
ATOM   8380  O O     . GLU C  1 300 ? -38.038 24.523  -12.318 1.00 38.29 ? 300 GLU A O     1 
ATOM   8381  C CB    . GLU C  1 300 ? -36.893 21.782  -11.153 1.00 44.37 ? 300 GLU A CB    1 
ATOM   8382  C CG    . GLU C  1 300 ? -35.672 21.337  -10.366 1.00 53.04 ? 300 GLU A CG    1 
ATOM   8383  C CD    . GLU C  1 300 ? -35.158 19.976  -10.778 1.00 67.15 ? 300 GLU A CD    1 
ATOM   8384  O OE1   . GLU C  1 300 ? -35.739 19.394  -11.725 1.00 68.26 ? 300 GLU A OE1   1 
ATOM   8385  O OE2   . GLU C  1 300 ? -34.166 19.506  -10.164 1.00 71.78 ? 300 GLU A OE2   1 
ATOM   8386  N N     . ALA C  1 301 ? -39.752 23.270  -11.513 1.00 40.39 ? 301 ALA A N     1 
ATOM   8387  C CA    . ALA C  1 301 ? -40.754 23.923  -12.350 1.00 38.12 ? 301 ALA A CA    1 
ATOM   8388  C C     . ALA C  1 301 ? -40.829 25.405  -12.033 1.00 35.65 ? 301 ALA A C     1 
ATOM   8389  O O     . ALA C  1 301 ? -41.010 26.233  -12.927 1.00 35.86 ? 301 ALA A O     1 
ATOM   8390  C CB    . ALA C  1 301 ? -42.127 23.269  -12.166 1.00 31.86 ? 301 ALA A CB    1 
ATOM   8391  N N     . THR C  1 302 ? -40.671 25.766  -10.771 1.00 32.38 ? 302 THR A N     1 
ATOM   8392  C CA    . THR C  1 302 ? -40.638 27.188  -10.507 1.00 33.67 ? 302 THR A CA    1 
ATOM   8393  C C     . THR C  1 302 ? -39.230 27.751  -10.660 1.00 34.84 ? 302 THR A C     1 
ATOM   8394  O O     . THR C  1 302 ? -39.047 28.796  -11.297 1.00 33.71 ? 302 THR A O     1 
ATOM   8395  C CB    . THR C  1 302 ? -41.195 27.469  -9.113  1.00 37.00 ? 302 THR A CB    1 
ATOM   8396  O OG1   . THR C  1 302 ? -40.386 26.820  -8.120  1.00 38.55 ? 302 THR A OG1   1 
ATOM   8397  C CG2   . THR C  1 302 ? -42.616 26.940  -9.012  1.00 34.46 ? 302 THR A CG2   1 
ATOM   8398  N N     . LEU C  1 303 ? -38.225 27.062  -10.118 1.00 34.07 ? 303 LEU A N     1 
ATOM   8399  C CA    . LEU C  1 303 ? -36.902 27.667  -10.009 1.00 33.76 ? 303 LEU A CA    1 
ATOM   8400  C C     . LEU C  1 303 ? -36.264 27.852  -11.376 1.00 32.66 ? 303 LEU A C     1 
ATOM   8401  O O     . LEU C  1 303 ? -35.750 28.930  -11.689 1.00 32.23 ? 303 LEU A O     1 
ATOM   8402  C CB    . LEU C  1 303 ? -36.014 26.819  -9.109  1.00 30.04 ? 303 LEU A CB    1 
ATOM   8403  C CG    . LEU C  1 303 ? -36.312 27.094  -7.650  1.00 29.76 ? 303 LEU A CG    1 
ATOM   8404  C CD1   . LEU C  1 303 ? -35.655 26.084  -6.724  1.00 28.00 ? 303 LEU A CD1   1 
ATOM   8405  C CD2   . LEU C  1 303 ? -35.841 28.491  -7.349  1.00 31.23 ? 303 LEU A CD2   1 
ATOM   8406  N N     . LYS C  1 304 ? -36.297 26.819  -12.209 1.00 28.03 ? 304 LYS A N     1 
ATOM   8407  C CA    . LYS C  1 304 ? -35.582 26.905  -13.480 1.00 33.26 ? 304 LYS A CA    1 
ATOM   8408  C C     . LYS C  1 304 ? -36.131 27.996  -14.395 1.00 31.22 ? 304 LYS A C     1 
ATOM   8409  O O     . LYS C  1 304 ? -35.336 28.830  -14.862 1.00 28.15 ? 304 LYS A O     1 
ATOM   8410  C CB    . LYS C  1 304 ? -35.555 25.528  -14.155 1.00 32.96 ? 304 LYS A CB    1 
ATOM   8411  C CG    . LYS C  1 304 ? -35.143 24.397  -13.213 1.00 36.08 ? 304 LYS A CG    1 
ATOM   8412  C CD    . LYS C  1 304 ? -33.632 24.225  -13.091 1.00 36.06 ? 304 LYS A CD    1 
ATOM   8413  C CE    . LYS C  1 304 ? -33.264 23.466  -11.807 1.00 49.07 ? 304 LYS A CE    1 
ATOM   8414  N NZ    . LYS C  1 304 ? -32.902 22.028  -12.067 1.00 47.50 ? 304 LYS A NZ    1 
ATOM   8415  N N     . PRO C  1 305 ? -37.437 28.080  -14.683 1.00 33.39 ? 305 PRO A N     1 
ATOM   8416  C CA    . PRO C  1 305 ? -37.903 29.210  -15.501 1.00 32.29 ? 305 PRO A CA    1 
ATOM   8417  C C     . PRO C  1 305 ? -37.637 30.560  -14.861 1.00 31.16 ? 305 PRO A C     1 
ATOM   8418  O O     . PRO C  1 305 ? -37.453 31.544  -15.585 1.00 34.35 ? 305 PRO A O     1 
ATOM   8419  C CB    . PRO C  1 305 ? -39.404 28.941  -15.666 1.00 23.92 ? 305 PRO A CB    1 
ATOM   8420  C CG    . PRO C  1 305 ? -39.569 27.519  -15.352 1.00 26.19 ? 305 PRO A CG    1 
ATOM   8421  C CD    . PRO C  1 305 ? -38.549 27.186  -14.331 1.00 29.57 ? 305 PRO A CD    1 
ATOM   8422  N N     . ALA C  1 306 ? -37.572 30.643  -13.528 1.00 32.82 ? 306 ALA A N     1 
ATOM   8423  C CA    . ALA C  1 306 ? -37.276 31.934  -12.908 1.00 33.24 ? 306 ALA A CA    1 
ATOM   8424  C C     . ALA C  1 306 ? -35.809 32.296  -13.081 1.00 30.38 ? 306 ALA A C     1 
ATOM   8425  O O     . ALA C  1 306 ? -35.478 33.462  -13.344 1.00 27.38 ? 306 ALA A O     1 
ATOM   8426  C CB    . ALA C  1 306 ? -37.663 31.923  -11.431 1.00 28.03 ? 306 ALA A CB    1 
ATOM   8427  N N     . GLU C  1 307 ? -34.919 31.304  -12.941 1.00 28.55 ? 307 GLU A N     1 
ATOM   8428  C CA    . GLU C  1 307 ? -33.513 31.513  -13.271 1.00 33.74 ? 307 GLU A CA    1 
ATOM   8429  C C     . GLU C  1 307 ? -33.365 31.994  -14.705 1.00 27.89 ? 307 GLU A C     1 
ATOM   8430  O O     . GLU C  1 307 ? -32.717 33.013  -14.964 1.00 28.55 ? 307 GLU A O     1 
ATOM   8431  C CB    . GLU C  1 307 ? -32.705 30.230  -13.040 1.00 35.40 ? 307 GLU A CB    1 
ATOM   8432  C CG    . GLU C  1 307 ? -32.344 30.060  -11.558 1.00 46.11 ? 307 GLU A CG    1 
ATOM   8433  C CD    . GLU C  1 307 ? -31.485 28.840  -11.242 1.00 54.96 ? 307 GLU A CD    1 
ATOM   8434  O OE1   . GLU C  1 307 ? -31.754 28.180  -10.199 1.00 41.40 ? 307 GLU A OE1   1 
ATOM   8435  O OE2   . GLU C  1 307 ? -30.539 28.560  -12.022 1.00 56.57 ? 307 GLU A OE2   1 
ATOM   8436  N N     . GLU C  1 308 ? -33.978 31.283  -15.647 1.00 30.10 ? 308 GLU A N     1 
ATOM   8437  C CA    . GLU C  1 308 ? -33.908 31.698  -17.041 1.00 33.89 ? 308 GLU A CA    1 
ATOM   8438  C C     . GLU C  1 308 ? -34.320 33.156  -17.178 1.00 33.71 ? 308 GLU A C     1 
ATOM   8439  O O     . GLU C  1 308 ? -33.588 33.963  -17.768 1.00 30.10 ? 308 GLU A O     1 
ATOM   8440  C CB    . GLU C  1 308 ? -34.786 30.797  -17.923 1.00 37.41 ? 308 GLU A CB    1 
ATOM   8441  C CG    . GLU C  1 308 ? -34.041 29.777  -18.783 1.00 35.91 ? 308 GLU A CG    1 
ATOM   8442  C CD    . GLU C  1 308 ? -34.758 29.495  -20.111 1.00 51.59 ? 308 GLU A CD    1 
ATOM   8443  O OE1   . GLU C  1 308 ? -34.142 28.893  -21.028 1.00 55.74 ? 308 GLU A OE1   1 
ATOM   8444  O OE2   . GLU C  1 308 ? -35.943 29.882  -20.242 1.00 51.38 ? 308 GLU A OE2   1 
ATOM   8445  N N     . PHE C  1 309 ? -35.465 33.529  -16.585 1.00 30.00 ? 309 PHE A N     1 
ATOM   8446  C CA    . PHE C  1 309 ? -35.959 34.889  -16.779 1.00 26.60 ? 309 PHE A CA    1 
ATOM   8447  C C     . PHE C  1 309 ? -35.053 35.922  -16.118 1.00 32.60 ? 309 PHE A C     1 
ATOM   8448  O O     . PHE C  1 309 ? -34.700 36.936  -16.738 1.00 30.92 ? 309 PHE A O     1 
ATOM   8449  C CB    . PHE C  1 309 ? -37.369 35.062  -16.244 1.00 27.10 ? 309 PHE A CB    1 
ATOM   8450  C CG    . PHE C  1 309 ? -37.978 36.349  -16.691 1.00 30.11 ? 309 PHE A CG    1 
ATOM   8451  C CD1   . PHE C  1 309 ? -37.690 37.537  -16.037 1.00 26.64 ? 309 PHE A CD1   1 
ATOM   8452  C CD2   . PHE C  1 309 ? -38.770 36.388  -17.829 1.00 31.29 ? 309 PHE A CD2   1 
ATOM   8453  C CE1   . PHE C  1 309 ? -38.205 38.727  -16.496 1.00 27.97 ? 309 PHE A CE1   1 
ATOM   8454  C CE2   . PHE C  1 309 ? -39.290 37.573  -18.279 1.00 26.28 ? 309 PHE A CE2   1 
ATOM   8455  C CZ    . PHE C  1 309 ? -38.997 38.748  -17.621 1.00 23.59 ? 309 PHE A CZ    1 
ATOM   8456  N N     . ILE C  1 310 ? -34.723 35.720  -14.837 1.00 30.44 ? 310 ILE A N     1 
ATOM   8457  C CA    . ILE C  1 310 ? -33.870 36.673  -14.139 1.00 27.13 ? 310 ILE A CA    1 
ATOM   8458  C C     . ILE C  1 310 ? -32.555 36.839  -14.880 1.00 25.52 ? 310 ILE A C     1 
ATOM   8459  O O     . ILE C  1 310 ? -32.029 37.948  -14.998 1.00 23.96 ? 310 ILE A O     1 
ATOM   8460  C CB    . ILE C  1 310 ? -33.675 36.224  -12.681 1.00 28.23 ? 310 ILE A CB    1 
ATOM   8461  C CG1   . ILE C  1 310 ? -34.974 36.456  -11.924 1.00 27.62 ? 310 ILE A CG1   1 
ATOM   8462  C CG2   . ILE C  1 310 ? -32.546 36.978  -12.017 1.00 26.56 ? 310 ILE A CG2   1 
ATOM   8463  C CD1   . ILE C  1 310 ? -35.593 37.773  -12.253 1.00 29.51 ? 310 ILE A CD1   1 
ATOM   8464  N N     . GLU C  1 311 ? -32.038 35.752  -15.450 1.00 29.98 ? 311 GLU A N     1 
ATOM   8465  C CA    . GLU C  1 311 ? -30.786 35.833  -16.195 1.00 33.89 ? 311 GLU A CA    1 
ATOM   8466  C C     . GLU C  1 311 ? -30.904 36.784  -17.386 1.00 33.66 ? 311 GLU A C     1 
ATOM   8467  O O     . GLU C  1 311 ? -29.995 37.582  -17.657 1.00 32.29 ? 311 GLU A O     1 
ATOM   8468  C CB    . GLU C  1 311 ? -30.364 34.438  -16.654 1.00 30.16 ? 311 GLU A CB    1 
ATOM   8469  C CG    . GLU C  1 311 ? -28.851 34.253  -16.771 1.00 34.02 ? 311 GLU A CG    1 
ATOM   8470  C CD    . GLU C  1 311 ? -28.064 34.799  -15.572 1.00 43.92 ? 311 GLU A CD    1 
ATOM   8471  O OE1   . GLU C  1 311 ? -28.288 34.355  -14.409 1.00 39.36 ? 311 GLU A OE1   1 
ATOM   8472  O OE2   . GLU C  1 311 ? -27.186 35.653  -15.822 1.00 42.60 ? 311 GLU A OE2   1 
ATOM   8473  N N     . MET C  1 312 ? -32.018 36.728  -18.103 1.00 27.23 ? 312 MET A N     1 
ATOM   8474  C CA    . MET C  1 312 ? -32.144 37.612  -19.250 1.00 30.72 ? 312 MET A CA    1 
ATOM   8475  C C     . MET C  1 312 ? -32.250 39.069  -18.819 1.00 32.44 ? 312 MET A C     1 
ATOM   8476  O O     . MET C  1 312 ? -31.741 39.948  -19.535 1.00 29.15 ? 312 MET A O     1 
ATOM   8477  C CB    . MET C  1 312 ? -33.342 37.207  -20.102 1.00 27.45 ? 312 MET A CB    1 
ATOM   8478  C CG    . MET C  1 312 ? -33.912 38.321  -20.920 1.00 29.29 ? 312 MET A CG    1 
ATOM   8479  S SD    . MET C  1 312 ? -35.328 37.732  -21.841 1.00 35.90 ? 312 MET A SD    1 
ATOM   8480  C CE    . MET C  1 312 ? -34.831 36.040  -22.063 1.00 37.71 ? 312 MET A CE    1 
ATOM   8481  N N     . ILE C  1 313 ? -32.860 39.350  -17.651 1.00 28.45 ? 313 ILE A N     1 
ATOM   8482  C CA    . ILE C  1 313 ? -32.876 40.746  -17.212 1.00 30.79 ? 313 ILE A CA    1 
ATOM   8483  C C     . ILE C  1 313 ? -31.497 41.169  -16.730 1.00 29.75 ? 313 ILE A C     1 
ATOM   8484  O O     . ILE C  1 313 ? -31.185 42.362  -16.754 1.00 34.37 ? 313 ILE A O     1 
ATOM   8485  C CB    . ILE C  1 313 ? -33.917 41.131  -16.120 1.00 27.80 ? 313 ILE A CB    1 
ATOM   8486  C CG1   . ILE C  1 313 ? -33.372 40.889  -14.725 1.00 32.23 ? 313 ILE A CG1   1 
ATOM   8487  C CG2   . ILE C  1 313 ? -35.307 40.532  -16.351 1.00 22.90 ? 313 ILE A CG2   1 
ATOM   8488  C CD1   . ILE C  1 313 ? -34.095 41.667  -13.649 1.00 39.60 ? 313 ILE A CD1   1 
ATOM   8489  N N     . ARG C  1 314 ? -30.647 40.238  -16.299 1.00 23.54 ? 314 ARG A N     1 
ATOM   8490  C CA    . ARG C  1 314 ? -29.260 40.636  -16.094 1.00 28.41 ? 314 ARG A CA    1 
ATOM   8491  C C     . ARG C  1 314 ? -28.600 41.001  -17.417 1.00 32.39 ? 314 ARG A C     1 
ATOM   8492  O O     . ARG C  1 314 ? -27.768 41.915  -17.464 1.00 31.94 ? 314 ARG A O     1 
ATOM   8493  C CB    . ARG C  1 314 ? -28.468 39.531  -15.397 1.00 31.21 ? 314 ARG A CB    1 
ATOM   8494  C CG    . ARG C  1 314 ? -27.167 40.036  -14.793 1.00 31.56 ? 314 ARG A CG    1 
ATOM   8495  C CD    . ARG C  1 314 ? -26.549 39.063  -13.809 1.00 34.96 ? 314 ARG A CD    1 
ATOM   8496  N NE    . ARG C  1 314 ? -25.812 37.964  -14.434 1.00 41.68 ? 314 ARG A NE    1 
ATOM   8497  C CZ    . ARG C  1 314 ? -24.585 38.045  -14.947 1.00 42.99 ? 314 ARG A CZ    1 
ATOM   8498  N NH1   . ARG C  1 314 ? -23.941 39.198  -15.035 1.00 38.75 ? 314 ARG A NH1   1 
ATOM   8499  N NH2   . ARG C  1 314 ? -23.982 36.932  -15.367 1.00 43.23 ? 314 ARG A NH2   1 
ATOM   8500  N N     . THR C  1 315 ? -28.974 40.304  -18.495 1.00 32.08 ? 315 THR A N     1 
ATOM   8501  C CA    . THR C  1 315 ? -28.448 40.588  -19.828 1.00 31.30 ? 315 THR A CA    1 
ATOM   8502  C C     . THR C  1 315 ? -28.917 41.944  -20.341 1.00 27.63 ? 315 THR A C     1 
ATOM   8503  O O     . THR C  1 315 ? -28.116 42.736  -20.847 1.00 31.38 ? 315 THR A O     1 
ATOM   8504  C CB    . THR C  1 315 ? -28.871 39.482  -20.786 1.00 29.38 ? 315 THR A CB    1 
ATOM   8505  O OG1   . THR C  1 315 ? -28.011 38.353  -20.599 1.00 25.38 ? 315 THR A OG1   1 
ATOM   8506  C CG2   . THR C  1 315 ? -28.799 39.957  -22.209 1.00 36.85 ? 315 THR A CG2   1 
ATOM   8507  N N     . ILE C  1 316 ? -30.213 42.237  -20.228 1.00 24.74 ? 316 ILE A N     1 
ATOM   8508  C CA    . ILE C  1 316 ? -30.647 43.557  -20.662 1.00 28.33 ? 316 ILE A CA    1 
ATOM   8509  C C     . ILE C  1 316 ? -30.053 44.646  -19.786 1.00 30.14 ? 316 ILE A C     1 
ATOM   8510  O O     . ILE C  1 316 ? -29.954 45.802  -20.212 1.00 29.77 ? 316 ILE A O     1 
ATOM   8511  C CB    . ILE C  1 316 ? -32.182 43.640  -20.734 1.00 28.52 ? 316 ILE A CB    1 
ATOM   8512  C CG1   . ILE C  1 316 ? -32.808 43.275  -19.416 1.00 40.20 ? 316 ILE A CG1   1 
ATOM   8513  C CG2   . ILE C  1 316 ? -32.753 42.687  -21.808 1.00 31.16 ? 316 ILE A CG2   1 
ATOM   8514  C CD1   . ILE C  1 316 ? -34.307 42.884  -19.584 1.00 44.08 ? 316 ILE A CD1   1 
ATOM   8515  N N     . GLY C  1 317 ? -29.623 44.301  -18.579 1.00 30.92 ? 317 GLY A N     1 
ATOM   8516  C CA    . GLY C  1 317 ? -28.657 45.128  -17.889 1.00 28.36 ? 317 GLY A CA    1 
ATOM   8517  C C     . GLY C  1 317 ? -28.986 45.625  -16.496 1.00 29.68 ? 317 GLY A C     1 
ATOM   8518  O O     . GLY C  1 317 ? -28.250 46.461  -15.955 1.00 25.92 ? 317 GLY A O     1 
ATOM   8519  N N     . TYR C  1 318 ? -30.060 45.134  -15.887 1.00 26.74 ? 318 TYR A N     1 
ATOM   8520  C CA    . TYR C  1 318 ? -30.386 45.618  -14.560 1.00 23.25 ? 318 TYR A CA    1 
ATOM   8521  C C     . TYR C  1 318 ? -29.376 45.088  -13.546 1.00 28.15 ? 318 TYR A C     1 
ATOM   8522  O O     . TYR C  1 318 ? -28.918 43.945  -13.645 1.00 28.63 ? 318 TYR A O     1 
ATOM   8523  C CB    . TYR C  1 318 ? -31.798 45.222  -14.174 1.00 23.60 ? 318 TYR A CB    1 
ATOM   8524  C CG    . TYR C  1 318 ? -32.081 45.597  -12.748 1.00 27.33 ? 318 TYR A CG    1 
ATOM   8525  C CD1   . TYR C  1 318 ? -32.116 46.927  -12.349 1.00 25.36 ? 318 TYR A CD1   1 
ATOM   8526  C CD2   . TYR C  1 318 ? -32.262 44.614  -11.777 1.00 25.23 ? 318 TYR A CD2   1 
ATOM   8527  C CE1   . TYR C  1 318 ? -32.360 47.256  -11.019 1.00 28.28 ? 318 TYR A CE1   1 
ATOM   8528  C CE2   . TYR C  1 318 ? -32.503 44.935  -10.466 1.00 23.69 ? 318 TYR A CE2   1 
ATOM   8529  C CZ    . TYR C  1 318 ? -32.554 46.249  -10.086 1.00 24.59 ? 318 TYR A CZ    1 
ATOM   8530  O OH    . TYR C  1 318 ? -32.789 46.547  -8.763  1.00 25.10 ? 318 TYR A OH    1 
ATOM   8531  N N     . ARG C  1 319 ? -29.021 45.944  -12.574 1.00 26.24 ? 319 ARG A N     1 
ATOM   8532  C CA    . ARG C  1 319 ? -28.013 45.674  -11.548 1.00 26.69 ? 319 ARG A CA    1 
ATOM   8533  C C     . ARG C  1 319 ? -28.588 46.084  -10.201 1.00 23.72 ? 319 ARG A C     1 
ATOM   8534  O O     . ARG C  1 319 ? -28.838 47.270  -9.965  1.00 26.06 ? 319 ARG A O     1 
ATOM   8535  C CB    . ARG C  1 319 ? -26.722 46.445  -11.826 1.00 31.45 ? 319 ARG A CB    1 
ATOM   8536  C CG    . ARG C  1 319 ? -26.053 46.139  -13.159 1.00 31.67 ? 319 ARG A CG    1 
ATOM   8537  C CD    . ARG C  1 319 ? -25.357 44.772  -13.171 1.00 29.91 ? 319 ARG A CD    1 
ATOM   8538  N NE    . ARG C  1 319 ? -24.662 44.521  -14.434 1.00 28.50 ? 319 ARG A NE    1 
ATOM   8539  C CZ    . ARG C  1 319 ? -25.179 43.880  -15.479 1.00 32.07 ? 319 ARG A CZ    1 
ATOM   8540  N NH1   . ARG C  1 319 ? -26.411 43.389  -15.455 1.00 28.60 ? 319 ARG A NH1   1 
ATOM   8541  N NH2   . ARG C  1 319 ? -24.436 43.720  -16.577 1.00 36.36 ? 319 ARG A NH2   1 
ATOM   8542  N N     . GLY C  1 320 ? -28.796 45.131  -9.325  1.00 21.79 ? 320 GLY A N     1 
ATOM   8543  C CA    . GLY C  1 320 ? -29.498 45.403  -8.093  1.00 19.40 ? 320 GLY A CA    1 
ATOM   8544  C C     . GLY C  1 320 ? -30.465 44.279  -7.763  1.00 25.68 ? 320 GLY A C     1 
ATOM   8545  O O     . GLY C  1 320 ? -30.400 43.183  -8.329  1.00 22.64 ? 320 GLY A O     1 
ATOM   8546  N N     . TYR C  1 321 ? -31.369 44.562  -6.817  1.00 30.22 ? 321 TYR A N     1 
ATOM   8547  C CA    . TYR C  1 321 ? -32.334 43.573  -6.336  1.00 24.84 ? 321 TYR A CA    1 
ATOM   8548  C C     . TYR C  1 321 ? -33.513 43.473  -7.283  1.00 24.32 ? 321 TYR A C     1 
ATOM   8549  O O     . TYR C  1 321 ? -33.994 44.479  -7.817  1.00 28.09 ? 321 TYR A O     1 
ATOM   8550  C CB    . TYR C  1 321 ? -32.852 43.933  -4.940  1.00 24.60 ? 321 TYR A CB    1 
ATOM   8551  C CG    . TYR C  1 321 ? -31.770 43.900  -3.920  1.00 24.91 ? 321 TYR A CG    1 
ATOM   8552  C CD1   . TYR C  1 321 ? -31.423 42.713  -3.287  1.00 25.13 ? 321 TYR A CD1   1 
ATOM   8553  C CD2   . TYR C  1 321 ? -31.051 45.049  -3.613  1.00 27.86 ? 321 TYR A CD2   1 
ATOM   8554  C CE1   . TYR C  1 321 ? -30.382 42.675  -2.357  1.00 26.77 ? 321 TYR A CE1   1 
ATOM   8555  C CE2   . TYR C  1 321 ? -30.015 45.027  -2.686  1.00 26.74 ? 321 TYR A CE2   1 
ATOM   8556  C CZ    . TYR C  1 321 ? -29.683 43.843  -2.060  1.00 27.28 ? 321 TYR A CZ    1 
ATOM   8557  O OH    . TYR C  1 321 ? -28.659 43.827  -1.137  1.00 32.60 ? 321 TYR A OH    1 
ATOM   8558  N N     . VAL C  1 322 ? -33.988 42.251  -7.473  1.00 23.51 ? 322 VAL A N     1 
ATOM   8559  C CA    . VAL C  1 322 ? -35.161 42.010  -8.290  1.00 23.91 ? 322 VAL A CA    1 
ATOM   8560  C C     . VAL C  1 322 ? -35.894 40.806  -7.724  1.00 27.64 ? 322 VAL A C     1 
ATOM   8561  O O     . VAL C  1 322 ? -35.311 39.948  -7.052  1.00 30.51 ? 322 VAL A O     1 
ATOM   8562  C CB    . VAL C  1 322 ? -34.786 41.803  -9.772  1.00 28.43 ? 322 VAL A CB    1 
ATOM   8563  C CG1   . VAL C  1 322 ? -34.204 40.411  -9.981  1.00 33.21 ? 322 VAL A CG1   1 
ATOM   8564  C CG2   . VAL C  1 322 ? -36.004 42.021  -10.674 1.00 28.82 ? 322 VAL A CG2   1 
ATOM   8565  N N     . ASN C  1 323 ? -37.187 40.743  -8.004  1.00 27.34 ? 323 ASN A N     1 
ATOM   8566  C CA    . ASN C  1 323 ? -37.972 39.579  -7.637  1.00 30.18 ? 323 ASN A CA    1 
ATOM   8567  C C     . ASN C  1 323 ? -39.015 39.289  -8.708  1.00 27.77 ? 323 ASN A C     1 
ATOM   8568  O O     . ASN C  1 323 ? -39.414 40.169  -9.473  1.00 24.04 ? 323 ASN A O     1 
ATOM   8569  C CB    . ASN C  1 323 ? -38.624 39.789  -6.272  1.00 30.53 ? 323 ASN A CB    1 
ATOM   8570  C CG    . ASN C  1 323 ? -39.164 41.167  -6.123  1.00 29.43 ? 323 ASN A CG    1 
ATOM   8571  O OD1   . ASN C  1 323 ? -40.329 41.425  -6.435  1.00 27.84 ? 323 ASN A OD1   1 
ATOM   8572  N ND2   . ASN C  1 323 ? -38.305 42.090  -5.674  1.00 29.48 ? 323 ASN A ND2   1 
ATOM   8573  N N     . ILE C  1 324 ? -39.441 38.035  -8.757  1.00 29.55 ? 324 ILE A N     1 
ATOM   8574  C CA    . ILE C  1 324 ? -40.435 37.567  -9.708  1.00 27.68 ? 324 ILE A CA    1 
ATOM   8575  C C     . ILE C  1 324 ? -41.551 36.924  -8.901  1.00 26.72 ? 324 ILE A C     1 
ATOM   8576  O O     . ILE C  1 324 ? -41.302 36.043  -8.073  1.00 25.12 ? 324 ILE A O     1 
ATOM   8577  C CB    . ILE C  1 324 ? -39.824 36.592  -10.736 1.00 25.52 ? 324 ILE A CB    1 
ATOM   8578  C CG1   . ILE C  1 324 ? -40.783 36.320  -11.873 1.00 29.06 ? 324 ILE A CG1   1 
ATOM   8579  C CG2   . ILE C  1 324 ? -39.397 35.249  -10.129 1.00 22.83 ? 324 ILE A CG2   1 
ATOM   8580  C CD1   . ILE C  1 324 ? -40.220 35.263  -12.820 1.00 32.48 ? 324 ILE A CD1   1 
ATOM   8581  N N     . ASP C  1 325 ? -42.769 37.396  -9.099  1.00 31.62 ? 325 ASP A N     1 
ATOM   8582  C CA    . ASP C  1 325 ? -43.913 36.851  -8.385  1.00 35.18 ? 325 ASP A CA    1 
ATOM   8583  C C     . ASP C  1 325 ? -44.488 35.655  -9.152  1.00 31.39 ? 325 ASP A C     1 
ATOM   8584  O O     . ASP C  1 325 ? -44.267 35.506  -10.350 1.00 29.35 ? 325 ASP A O     1 
ATOM   8585  C CB    . ASP C  1 325 ? -44.963 37.953  -8.188  1.00 37.42 ? 325 ASP A CB    1 
ATOM   8586  C CG    . ASP C  1 325 ? -44.381 39.227  -7.524  1.00 45.67 ? 325 ASP A CG    1 
ATOM   8587  O OD1   . ASP C  1 325 ? -43.173 39.229  -7.167  1.00 44.02 ? 325 ASP A OD1   1 
ATOM   8588  O OD2   . ASP C  1 325 ? -45.135 40.225  -7.353  1.00 45.58 ? 325 ASP A OD2   1 
ATOM   8589  N N     . GLY C  1 326 ? -45.229 34.798  -8.454  1.00 33.17 ? 326 GLY A N     1 
ATOM   8590  C CA    . GLY C  1 326 ? -45.837 33.673  -9.148  1.00 30.70 ? 326 GLY A CA    1 
ATOM   8591  C C     . GLY C  1 326 ? -46.666 32.779  -8.248  1.00 28.96 ? 326 GLY A C     1 
ATOM   8592  O O     . GLY C  1 326 ? -46.639 32.886  -7.019  1.00 32.64 ? 326 GLY A O     1 
ATOM   8593  N N     . ILE C  1 327 ? -47.382 31.858  -8.895  1.00 28.37 ? 327 ILE A N     1 
ATOM   8594  C CA    . ILE C  1 327 ? -48.323 30.947  -8.247  1.00 32.68 ? 327 ILE A CA    1 
ATOM   8595  C C     . ILE C  1 327 ? -48.052 29.506  -8.671  1.00 32.54 ? 327 ILE A C     1 
ATOM   8596  O O     . ILE C  1 327 ? -47.557 29.241  -9.773  1.00 31.37 ? 327 ILE A O     1 
ATOM   8597  C CB    . ILE C  1 327 ? -49.788 31.295  -8.590  1.00 36.31 ? 327 ILE A CB    1 
ATOM   8598  C CG1   . ILE C  1 327 ? -49.984 31.218  -10.119 1.00 35.95 ? 327 ILE A CG1   1 
ATOM   8599  C CG2   . ILE C  1 327 ? -50.170 32.647  -8.001  1.00 37.20 ? 327 ILE A CG2   1 
ATOM   8600  C CD1   . ILE C  1 327 ? -51.311 31.677  -10.618 1.00 31.77 ? 327 ILE A CD1   1 
ATOM   8601  N N     . VAL C  1 328 ? -48.422 28.571  -7.794  1.00 28.98 ? 328 VAL A N     1 
ATOM   8602  C CA    . VAL C  1 328 ? -48.420 27.140  -8.086  1.00 31.31 ? 328 VAL A CA    1 
ATOM   8603  C C     . VAL C  1 328 ? -49.860 26.643  -7.933  1.00 40.20 ? 328 VAL A C     1 
ATOM   8604  O O     . VAL C  1 328 ? -50.452 26.772  -6.851  1.00 45.98 ? 328 VAL A O     1 
ATOM   8605  C CB    . VAL C  1 328 ? -47.454 26.373  -7.159  1.00 29.79 ? 328 VAL A CB    1 
ATOM   8606  C CG1   . VAL C  1 328 ? -47.285 24.936  -7.587  1.00 28.35 ? 328 VAL A CG1   1 
ATOM   8607  C CG2   . VAL C  1 328 ? -46.089 27.058  -7.102  1.00 27.58 ? 328 VAL A CG2   1 
ATOM   8608  N N     . LEU C  1 329 ? -50.432 26.093  -9.013  1.00 40.06 ? 329 LEU A N     1 
ATOM   8609  C CA    . LEU C  1 329 ? -51.839 25.689  -9.040  1.00 41.11 ? 329 LEU A CA    1 
ATOM   8610  C C     . LEU C  1 329 ? -52.066 24.351  -8.324  1.00 44.65 ? 329 LEU A C     1 
ATOM   8611  O O     . LEU C  1 329 ? -51.139 23.744  -7.784  1.00 41.62 ? 329 LEU A O     1 
ATOM   8612  C CB    . LEU C  1 329 ? -52.329 25.593  -10.479 1.00 41.08 ? 329 LEU A CB    1 
ATOM   8613  C CG    . LEU C  1 329 ? -53.237 26.703  -10.988 1.00 34.87 ? 329 LEU A CG    1 
ATOM   8614  C CD1   . LEU C  1 329 ? -52.734 28.073  -10.592 1.00 40.26 ? 329 LEU A CD1   1 
ATOM   8615  C CD2   . LEU C  1 329 ? -53.277 26.574  -12.458 1.00 37.79 ? 329 LEU A CD2   1 
ATOM   8616  N N     . ASP C  1 330 ? -53.329 23.876  -8.330  1.00 48.13 ? 330 ASP A N     1 
ATOM   8617  C CA    . ASP C  1 330 ? -53.659 22.549  -7.794  1.00 49.56 ? 330 ASP A CA    1 
ATOM   8618  C C     . ASP C  1 330 ? -53.262 21.436  -8.741  1.00 46.75 ? 330 ASP A C     1 
ATOM   8619  O O     . ASP C  1 330 ? -52.666 20.437  -8.326  1.00 53.23 ? 330 ASP A O     1 
ATOM   8620  C CB    . ASP C  1 330 ? -55.149 22.397  -7.540  1.00 51.76 ? 330 ASP A CB    1 
ATOM   8621  C CG    . ASP C  1 330 ? -55.705 23.520  -6.795  1.00 54.57 ? 330 ASP A CG    1 
ATOM   8622  O OD1   . ASP C  1 330 ? -55.424 24.672  -7.215  1.00 56.66 ? 330 ASP A OD1   1 
ATOM   8623  O OD2   . ASP C  1 330 ? -56.400 23.238  -5.791  1.00 49.21 ? 330 ASP A OD2   1 
ATOM   8624  N N     . ASP C  1 331 ? -53.658 21.558  -10.001 1.00 46.25 ? 331 ASP A N     1 
ATOM   8625  C CA    . ASP C  1 331 ? -53.269 20.578  -10.997 1.00 45.26 ? 331 ASP A CA    1 
ATOM   8626  C C     . ASP C  1 331 ? -51.758 20.449  -11.116 1.00 42.80 ? 331 ASP A C     1 
ATOM   8627  O O     . ASP C  1 331 ? -51.278 19.532  -11.794 1.00 40.70 ? 331 ASP A O     1 
ATOM   8628  C CB    . ASP C  1 331 ? -53.889 20.980  -12.320 1.00 42.11 ? 331 ASP A CB    1 
ATOM   8629  C CG    . ASP C  1 331 ? -53.786 22.458  -12.558 1.00 44.66 ? 331 ASP A CG    1 
ATOM   8630  O OD1   . ASP C  1 331 ? -52.718 23.026  -12.240 1.00 45.00 ? 331 ASP A OD1   1 
ATOM   8631  O OD2   . ASP C  1 331 ? -54.767 23.060  -13.044 1.00 48.60 ? 331 ASP A OD2   1 
ATOM   8632  N N     . GLY C  1 332 ? -51.007 21.347  -10.472 1.00 42.26 ? 332 GLY A N     1 
ATOM   8633  C CA    . GLY C  1 332 ? -49.558 21.311  -10.417 1.00 42.67 ? 332 GLY A CA    1 
ATOM   8634  C C     . GLY C  1 332 ? -48.893 22.418  -11.197 1.00 42.99 ? 332 GLY A C     1 
ATOM   8635  O O     . GLY C  1 332 ? -47.656 22.536  -11.159 1.00 35.72 ? 332 GLY A O     1 
ATOM   8636  N N     . ARG C  1 333 ? -49.678 23.236  -11.890 1.00 41.97 ? 333 ARG A N     1 
ATOM   8637  C CA    . ARG C  1 333 ? -49.144 24.219  -12.809 1.00 39.81 ? 333 ARG A CA    1 
ATOM   8638  C C     . ARG C  1 333 ? -48.532 25.394  -12.058 1.00 40.44 ? 333 ARG A C     1 
ATOM   8639  O O     . ARG C  1 333 ? -48.732 25.588  -10.853 1.00 33.95 ? 333 ARG A O     1 
ATOM   8640  C CB    . ARG C  1 333 ? -50.232 24.696  -13.769 1.00 37.31 ? 333 ARG A CB    1 
ATOM   8641  C CG    . ARG C  1 333 ? -50.743 23.554  -14.640 1.00 42.90 ? 333 ARG A CG    1 
ATOM   8642  C CD    . ARG C  1 333 ? -51.788 23.999  -15.652 1.00 37.30 ? 333 ARG A CD    1 
ATOM   8643  N NE    . ARG C  1 333 ? -53.135 23.880  -15.117 1.00 39.55 ? 333 ARG A NE    1 
ATOM   8644  C CZ    . ARG C  1 333 ? -54.042 24.841  -15.168 1.00 40.13 ? 333 ARG A CZ    1 
ATOM   8645  N NH1   . ARG C  1 333 ? -53.778 26.007  -15.738 1.00 41.67 ? 333 ARG A NH1   1 
ATOM   8646  N NH2   . ARG C  1 333 ? -55.233 24.635  -14.611 1.00 31.04 ? 333 ARG A NH2   1 
ATOM   8647  N N     . VAL C  1 334 ? -47.762 26.174  -12.803 1.00 38.78 ? 334 VAL A N     1 
ATOM   8648  C CA    . VAL C  1 334 ? -47.005 27.295  -12.281 1.00 35.38 ? 334 VAL A CA    1 
ATOM   8649  C C     . VAL C  1 334 ? -47.269 28.492  -13.180 1.00 37.36 ? 334 VAL A C     1 
ATOM   8650  O O     . VAL C  1 334 ? -47.331 28.353  -14.406 1.00 40.16 ? 334 VAL A O     1 
ATOM   8651  C CB    . VAL C  1 334 ? -45.502 26.964  -12.240 1.00 35.09 ? 334 VAL A CB    1 
ATOM   8652  C CG1   . VAL C  1 334 ? -44.725 28.125  -11.654 1.00 36.45 ? 334 VAL A CG1   1 
ATOM   8653  C CG2   . VAL C  1 334 ? -45.256 25.653  -11.478 1.00 23.04 ? 334 VAL A CG2   1 
ATOM   8654  N N     . PHE C  1 335 ? -47.446 29.660  -12.581 1.00 30.27 ? 335 PHE A N     1 
ATOM   8655  C CA    . PHE C  1 335 ? -47.521 30.887  -13.352 1.00 27.36 ? 335 PHE A CA    1 
ATOM   8656  C C     . PHE C  1 335 ? -46.748 31.958  -12.604 1.00 32.91 ? 335 PHE A C     1 
ATOM   8657  O O     . PHE C  1 335 ? -46.798 32.005  -11.372 1.00 34.58 ? 335 PHE A O     1 
ATOM   8658  C CB    . PHE C  1 335 ? -48.960 31.360  -13.552 1.00 34.02 ? 335 PHE A CB    1 
ATOM   8659  C CG    . PHE C  1 335 ? -49.820 30.434  -14.365 1.00 35.47 ? 335 PHE A CG    1 
ATOM   8660  C CD1   . PHE C  1 335 ? -49.718 30.399  -15.748 1.00 36.71 ? 335 PHE A CD1   1 
ATOM   8661  C CD2   . PHE C  1 335 ? -50.773 29.631  -13.742 1.00 36.78 ? 335 PHE A CD2   1 
ATOM   8662  C CE1   . PHE C  1 335 ? -50.528 29.557  -16.502 1.00 32.55 ? 335 PHE A CE1   1 
ATOM   8663  C CE2   . PHE C  1 335 ? -51.589 28.792  -14.480 1.00 38.56 ? 335 PHE A CE2   1 
ATOM   8664  C CZ    . PHE C  1 335 ? -51.465 28.756  -15.870 1.00 39.39 ? 335 PHE A CZ    1 
ATOM   8665  N N     . PHE C  1 336 ? -46.037 32.806  -13.348 1.00 28.23 ? 336 PHE A N     1 
ATOM   8666  C CA    . PHE C  1 336 ? -45.384 33.990  -12.812 1.00 29.34 ? 336 PHE A CA    1 
ATOM   8667  C C     . PHE C  1 336 ? -46.093 35.232  -13.318 1.00 33.94 ? 336 PHE A C     1 
ATOM   8668  O O     . PHE C  1 336 ? -46.574 35.256  -14.456 1.00 36.63 ? 336 PHE A O     1 
ATOM   8669  C CB    . PHE C  1 336 ? -43.919 34.063  -13.227 1.00 30.85 ? 336 PHE A CB    1 
ATOM   8670  C CG    . PHE C  1 336 ? -43.085 32.993  -12.630 1.00 33.65 ? 336 PHE A CG    1 
ATOM   8671  C CD1   . PHE C  1 336 ? -42.800 33.001  -11.274 1.00 31.40 ? 336 PHE A CD1   1 
ATOM   8672  C CD2   . PHE C  1 336 ? -42.599 31.959  -13.412 1.00 34.59 ? 336 PHE A CD2   1 
ATOM   8673  C CE1   . PHE C  1 336 ? -42.030 32.001  -10.709 1.00 34.89 ? 336 PHE A CE1   1 
ATOM   8674  C CE2   . PHE C  1 336 ? -41.824 30.937  -12.849 1.00 35.93 ? 336 PHE A CE2   1 
ATOM   8675  C CZ    . PHE C  1 336 ? -41.533 30.962  -11.503 1.00 34.03 ? 336 PHE A CZ    1 
ATOM   8676  N N     . HIS C  1 337 ? -46.123 36.275  -12.484 1.00 31.38 ? 337 HIS A N     1 
ATOM   8677  C CA    . HIS C  1 337 ? -46.934 37.458  -12.753 1.00 31.00 ? 337 HIS A CA    1 
ATOM   8678  C C     . HIS C  1 337 ? -46.147 38.706  -13.107 1.00 29.38 ? 337 HIS A C     1 
ATOM   8679  O O     . HIS C  1 337 ? -46.540 39.428  -14.013 1.00 33.33 ? 337 HIS A O     1 
ATOM   8680  C CB    . HIS C  1 337 ? -47.801 37.797  -11.553 1.00 37.07 ? 337 HIS A CB    1 
ATOM   8681  C CG    . HIS C  1 337 ? -48.354 36.608  -10.847 1.00 35.22 ? 337 HIS A CG    1 
ATOM   8682  N ND1   . HIS C  1 337 ? -49.141 35.670  -11.476 1.00 35.79 ? 337 HIS A ND1   1 
ATOM   8683  C CD2   . HIS C  1 337 ? -48.244 36.211  -9.561  1.00 37.85 ? 337 HIS A CD2   1 
ATOM   8684  C CE1   . HIS C  1 337 ? -49.481 34.736  -10.607 1.00 36.72 ? 337 HIS A CE1   1 
ATOM   8685  N NE2   . HIS C  1 337 ? -48.959 35.046  -9.436  1.00 39.59 ? 337 HIS A NE2   1 
ATOM   8686  N N     . GLU C  1 338 ? -45.103 39.040  -12.359 1.00 38.17 ? 338 GLU A N     1 
ATOM   8687  C CA    . GLU C  1 338 ? -44.380 40.278  -12.613 1.00 33.71 ? 338 GLU A CA    1 
ATOM   8688  C C     . GLU C  1 338 ? -42.942 40.100  -12.161 1.00 29.15 ? 338 GLU A C     1 
ATOM   8689  O O     . GLU C  1 338 ? -42.588 39.125  -11.498 1.00 27.96 ? 338 GLU A O     1 
ATOM   8690  C CB    . GLU C  1 338 ? -45.021 41.487  -11.889 1.00 35.99 ? 338 GLU A CB    1 
ATOM   8691  C CG    . GLU C  1 338 ? -45.085 41.356  -10.341 1.00 38.15 ? 338 GLU A CG    1 
ATOM   8692  C CD    . GLU C  1 338 ? -45.372 42.667  -9.574  1.00 39.24 ? 338 GLU A CD    1 
ATOM   8693  O OE1   . GLU C  1 338 ? -45.800 43.666  -10.178 1.00 40.33 ? 338 GLU A OE1   1 
ATOM   8694  O OE2   . GLU C  1 338 ? -45.206 42.682  -8.334  1.00 44.71 ? 338 GLU A OE2   1 
ATOM   8695  N N     . ILE C  1 339 ? -42.111 41.043  -12.558 1.00 30.14 ? 339 ILE A N     1 
ATOM   8696  C CA    . ILE C  1 339 ? -40.878 41.310  -11.842 1.00 34.51 ? 339 ILE A CA    1 
ATOM   8697  C C     . ILE C  1 339 ? -41.016 42.701  -11.261 1.00 33.01 ? 339 ILE A C     1 
ATOM   8698  O O     . ILE C  1 339 ? -41.681 43.569  -11.839 1.00 30.18 ? 339 ILE A O     1 
ATOM   8699  C CB    . ILE C  1 339 ? -39.567 41.227  -12.679 1.00 33.03 ? 339 ILE A CB    1 
ATOM   8700  C CG1   . ILE C  1 339 ? -39.619 42.107  -13.916 1.00 27.24 ? 339 ILE A CG1   1 
ATOM   8701  C CG2   . ILE C  1 339 ? -39.127 39.776  -12.946 1.00 31.38 ? 339 ILE A CG2   1 
ATOM   8702  C CD1   . ILE C  1 339 ? -38.248 42.691  -14.267 1.00 26.36 ? 339 ILE A CD1   1 
ATOM   8703  N N     . ASN C  1 340 ? -40.377 42.907  -10.111 1.00 30.01 ? 340 ASN A N     1 
ATOM   8704  C CA    . ASN C  1 340 ? -40.245 44.221  -9.493  1.00 35.80 ? 340 ASN A CA    1 
ATOM   8705  C C     . ASN C  1 340 ? -38.754 44.543  -9.406  1.00 31.01 ? 340 ASN A C     1 
ATOM   8706  O O     . ASN C  1 340 ? -37.992 43.820  -8.753  1.00 33.92 ? 340 ASN A O     1 
ATOM   8707  C CB    . ASN C  1 340 ? -40.922 44.245  -8.113  1.00 33.18 ? 340 ASN A CB    1 
ATOM   8708  C CG    . ASN C  1 340 ? -42.394 43.801  -8.166  1.00 39.96 ? 340 ASN A CG    1 
ATOM   8709  O OD1   . ASN C  1 340 ? -43.314 44.627  -8.190  1.00 47.58 ? 340 ASN A OD1   1 
ATOM   8710  N ND2   . ASN C  1 340 ? -42.618 42.487  -8.156  1.00 43.87 ? 340 ASN A ND2   1 
ATOM   8711  N N     . ALA C  1 341 ? -38.333 45.616  -10.066 1.00 25.36 ? 341 ALA A N     1 
ATOM   8712  C CA    . ALA C  1 341 ? -36.911 45.968  -10.094 1.00 28.77 ? 341 ALA A CA    1 
ATOM   8713  C C     . ALA C  1 341 ? -36.612 46.980  -8.989  1.00 32.01 ? 341 ALA A C     1 
ATOM   8714  O O     . ALA C  1 341 ? -36.414 48.179  -9.221  1.00 26.20 ? 341 ALA A O     1 
ATOM   8715  C CB    . ALA C  1 341 ? -36.523 46.493  -11.472 1.00 31.84 ? 341 ALA A CB    1 
ATOM   8716  N N     . ARG C  1 342 ? -36.571 46.457  -7.759  1.00 30.84 ? 342 ARG A N     1 
ATOM   8717  C CA    . ARG C  1 342 ? -36.483 47.279  -6.551  1.00 29.86 ? 342 ARG A CA    1 
ATOM   8718  C C     . ARG C  1 342 ? -36.443 46.368  -5.335  1.00 29.50 ? 342 ARG A C     1 
ATOM   8719  O O     . ARG C  1 342 ? -36.551 45.148  -5.474  1.00 29.98 ? 342 ARG A O     1 
ATOM   8720  C CB    . ARG C  1 342 ? -37.670 48.243  -6.442  1.00 30.48 ? 342 ARG A CB    1 
ATOM   8721  C CG    . ARG C  1 342 ? -39.042 47.590  -6.636  1.00 35.43 ? 342 ARG A CG    1 
ATOM   8722  C CD    . ARG C  1 342 ? -40.222 48.566  -6.428  1.00 38.77 ? 342 ARG A CD    1 
ATOM   8723  N NE    . ARG C  1 342 ? -41.541 47.920  -6.399  1.00 48.21 ? 342 ARG A NE    1 
ATOM   8724  C CZ    . ARG C  1 342 ? -42.295 47.660  -7.463  1.00 47.69 ? 342 ARG A CZ    1 
ATOM   8725  N NH1   . ARG C  1 342 ? -41.875 47.920  -8.694  1.00 42.37 ? 342 ARG A NH1   1 
ATOM   8726  N NH2   . ARG C  1 342 ? -43.504 47.129  -7.288  1.00 50.19 ? 342 ARG A NH2   1 
ATOM   8727  N N     . TRP C  1 343 ? -36.254 46.939  -4.148  1.00 28.50 ? 343 TRP A N     1 
ATOM   8728  C CA    . TRP C  1 343 ? -36.336 46.140  -2.935  1.00 29.73 ? 343 TRP A CA    1 
ATOM   8729  C C     . TRP C  1 343 ? -37.652 45.397  -2.915  1.00 29.28 ? 343 TRP A C     1 
ATOM   8730  O O     . TRP C  1 343 ? -38.688 45.954  -3.285  1.00 33.87 ? 343 TRP A O     1 
ATOM   8731  C CB    . TRP C  1 343 ? -36.270 47.027  -1.707  1.00 32.03 ? 343 TRP A CB    1 
ATOM   8732  C CG    . TRP C  1 343 ? -35.036 47.736  -1.596  1.00 29.67 ? 343 TRP A CG    1 
ATOM   8733  C CD1   . TRP C  1 343 ? -33.888 47.474  -2.263  1.00 30.11 ? 343 TRP A CD1   1 
ATOM   8734  C CD2   . TRP C  1 343 ? -34.773 48.833  -0.732  1.00 28.41 ? 343 TRP A CD2   1 
ATOM   8735  N NE1   . TRP C  1 343 ? -32.910 48.366  -1.886  1.00 36.21 ? 343 TRP A NE1   1 
ATOM   8736  C CE2   . TRP C  1 343 ? -33.429 49.209  -0.938  1.00 33.36 ? 343 TRP A CE2   1 
ATOM   8737  C CE3   . TRP C  1 343 ? -35.541 49.540  0.191   1.00 24.60 ? 343 TRP A CE3   1 
ATOM   8738  C CZ2   . TRP C  1 343 ? -32.837 50.277  -0.264  1.00 30.87 ? 343 TRP A CZ2   1 
ATOM   8739  C CZ3   . TRP C  1 343 ? -34.952 50.607  0.865   1.00 29.83 ? 343 TRP A CZ3   1 
ATOM   8740  C CH2   . TRP C  1 343 ? -33.610 50.958  0.639   1.00 29.82 ? 343 TRP A CH2   1 
ATOM   8741  N N     . SER C  1 344 ? -37.619 44.144  -2.486  1.00 28.86 ? 344 SER A N     1 
ATOM   8742  C CA    . SER C  1 344 ? -38.894 43.517  -2.179  1.00 34.25 ? 344 SER A CA    1 
ATOM   8743  C C     . SER C  1 344 ? -39.349 43.969  -0.794  1.00 34.73 ? 344 SER A C     1 
ATOM   8744  O O     . SER C  1 344 ? -38.590 44.591  -0.039  1.00 30.74 ? 344 SER A O     1 
ATOM   8745  C CB    . SER C  1 344 ? -38.795 41.990  -2.256  1.00 31.34 ? 344 SER A CB    1 
ATOM   8746  O OG    . SER C  1 344 ? -38.260 41.438  -1.070  1.00 31.50 ? 344 SER A OG    1 
ATOM   8747  N N     . GLY C  1 345 ? -40.619 43.683  -0.477  1.00 38.06 ? 345 GLY A N     1 
ATOM   8748  C CA    . GLY C  1 345 ? -41.137 43.893  0.872   1.00 26.33 ? 345 GLY A CA    1 
ATOM   8749  C C     . GLY C  1 345 ? -40.485 43.012  1.930   1.00 33.21 ? 345 GLY A C     1 
ATOM   8750  O O     . GLY C  1 345 ? -40.556 43.326  3.127   1.00 29.93 ? 345 GLY A O     1 
ATOM   8751  N N     . GLY C  1 346 ? -39.836 41.923  1.520   1.00 30.16 ? 346 GLY A N     1 
ATOM   8752  C CA    . GLY C  1 346 ? -39.280 41.000  2.483   1.00 27.05 ? 346 GLY A CA    1 
ATOM   8753  C C     . GLY C  1 346 ? -37.779 41.005  2.455   1.00 27.61 ? 346 GLY A C     1 
ATOM   8754  O O     . GLY C  1 346 ? -37.123 40.246  3.181   1.00 31.43 ? 346 GLY A O     1 
ATOM   8755  N N     . LEU C  1 347 ? -37.223 41.855  1.599   1.00 28.45 ? 347 LEU A N     1 
ATOM   8756  C CA    . LEU C  1 347 ? -35.774 41.980  1.541   1.00 27.15 ? 347 LEU A CA    1 
ATOM   8757  C C     . LEU C  1 347 ? -35.210 42.260  2.924   1.00 29.00 ? 347 LEU A C     1 
ATOM   8758  O O     . LEU C  1 347 ? -34.293 41.570  3.392   1.00 30.82 ? 347 LEU A O     1 
ATOM   8759  C CB    . LEU C  1 347 ? -35.379 43.076  0.551   1.00 29.17 ? 347 LEU A CB    1 
ATOM   8760  C CG    . LEU C  1 347 ? -33.889 43.429  0.481   1.00 29.42 ? 347 LEU A CG    1 
ATOM   8761  C CD1   . LEU C  1 347 ? -33.020 42.179  0.378   1.00 27.18 ? 347 LEU A CD1   1 
ATOM   8762  C CD2   . LEU C  1 347 ? -33.622 44.379  -0.695  1.00 31.96 ? 347 LEU A CD2   1 
ATOM   8763  N N     . ILE C  1 348 ? -35.777 43.241  3.623   1.00 26.26 ? 348 ILE A N     1 
ATOM   8764  C CA    . ILE C  1 348 ? -35.319 43.433  4.986   1.00 26.25 ? 348 ILE A CA    1 
ATOM   8765  C C     . ILE C  1 348 ? -35.634 42.219  5.830   1.00 27.07 ? 348 ILE A C     1 
ATOM   8766  O O     . ILE C  1 348 ? -34.917 41.937  6.797   1.00 27.94 ? 348 ILE A O     1 
ATOM   8767  C CB    . ILE C  1 348 ? -35.910 44.700  5.617   1.00 33.10 ? 348 ILE A CB    1 
ATOM   8768  C CG1   . ILE C  1 348 ? -37.419 44.690  5.525   1.00 26.88 ? 348 ILE A CG1   1 
ATOM   8769  C CG2   . ILE C  1 348 ? -35.302 45.967  5.011   1.00 32.85 ? 348 ILE A CG2   1 
ATOM   8770  C CD1   . ILE C  1 348 ? -37.891 46.043  5.727   1.00 32.85 ? 348 ILE A CD1   1 
ATOM   8771  N N     . TYR C  1 349 ? -36.720 41.502  5.524   1.00 23.67 ? 349 TYR A N     1 
ATOM   8772  C CA    . TYR C  1 349 ? -36.986 40.295  6.293   1.00 26.99 ? 349 TYR A CA    1 
ATOM   8773  C C     . TYR C  1 349 ? -35.792 39.379  6.167   1.00 28.75 ? 349 TYR A C     1 
ATOM   8774  O O     . TYR C  1 349 ? -35.251 38.886  7.164   1.00 23.75 ? 349 TYR A O     1 
ATOM   8775  C CB    . TYR C  1 349 ? -38.279 39.607  5.817   1.00 27.29 ? 349 TYR A CB    1 
ATOM   8776  C CG    . TYR C  1 349 ? -39.567 40.380  6.086   1.00 27.40 ? 349 TYR A CG    1 
ATOM   8777  C CD1   . TYR C  1 349 ? -39.567 41.537  6.867   1.00 28.49 ? 349 TYR A CD1   1 
ATOM   8778  C CD2   . TYR C  1 349 ? -40.779 39.956  5.566   1.00 25.93 ? 349 TYR A CD2   1 
ATOM   8779  C CE1   . TYR C  1 349 ? -40.728 42.242  7.111   1.00 22.30 ? 349 TYR A CE1   1 
ATOM   8780  C CE2   . TYR C  1 349 ? -41.951 40.667  5.813   1.00 25.14 ? 349 TYR A CE2   1 
ATOM   8781  C CZ    . TYR C  1 349 ? -41.911 41.807  6.587   1.00 23.62 ? 349 TYR A CZ    1 
ATOM   8782  O OH    . TYR C  1 349 ? -43.060 42.515  6.852   1.00 29.25 ? 349 TYR A OH    1 
ATOM   8783  N N     . HIS C  1 350 ? -35.307 39.236  4.935   1.00 24.98 ? 350 HIS A N     1 
ATOM   8784  C CA    . HIS C  1 350 ? -34.147 38.406  4.663   1.00 28.33 ? 350 HIS A CA    1 
ATOM   8785  C C     . HIS C  1 350 ? -32.907 38.954  5.356   1.00 30.12 ? 350 HIS A C     1 
ATOM   8786  O O     . HIS C  1 350 ? -32.154 38.199  5.983   1.00 27.66 ? 350 HIS A O     1 
ATOM   8787  C CB    . HIS C  1 350 ? -33.961 38.337  3.150   1.00 28.47 ? 350 HIS A CB    1 
ATOM   8788  C CG    . HIS C  1 350 ? -32.776 37.546  2.702   1.00 27.65 ? 350 HIS A CG    1 
ATOM   8789  N ND1   . HIS C  1 350 ? -32.494 36.282  3.178   1.00 26.18 ? 350 HIS A ND1   1 
ATOM   8790  C CD2   . HIS C  1 350 ? -31.836 37.816  1.764   1.00 29.54 ? 350 HIS A CD2   1 
ATOM   8791  C CE1   . HIS C  1 350 ? -31.412 35.822  2.574   1.00 30.88 ? 350 HIS A CE1   1 
ATOM   8792  N NE2   . HIS C  1 350 ? -30.994 36.734  1.710   1.00 32.59 ? 350 HIS A NE2   1 
ATOM   8793  N N     . THR C  1 351 ? -32.698 40.274  5.282   1.00 28.39 ? 351 THR A N     1 
ATOM   8794  C CA    . THR C  1 351 ? -31.491 40.883  5.840   1.00 29.70 ? 351 THR A CA    1 
ATOM   8795  C C     . THR C  1 351 ? -31.411 40.699  7.362   1.00 30.67 ? 351 THR A C     1 
ATOM   8796  O O     . THR C  1 351 ? -30.392 40.241  7.885   1.00 33.04 ? 351 THR A O     1 
ATOM   8797  C CB    . THR C  1 351 ? -31.440 42.372  5.469   1.00 34.31 ? 351 THR A CB    1 
ATOM   8798  O OG1   . THR C  1 351 ? -31.431 42.520  4.041   1.00 34.31 ? 351 THR A OG1   1 
ATOM   8799  C CG2   . THR C  1 351 ? -30.187 43.074  6.086   1.00 28.42 ? 351 THR A CG2   1 
ATOM   8800  N N     . VAL C  1 352 ? -32.473 41.057  8.091   1.00 28.35 ? 352 VAL A N     1 
ATOM   8801  C CA    . VAL C  1 352 ? -32.488 40.861  9.544   1.00 23.41 ? 352 VAL A CA    1 
ATOM   8802  C C     . VAL C  1 352 ? -32.154 39.412  9.888   1.00 28.94 ? 352 VAL A C     1 
ATOM   8803  O O     . VAL C  1 352 ? -31.374 39.138  10.813  1.00 31.47 ? 352 VAL A O     1 
ATOM   8804  C CB    . VAL C  1 352 ? -33.854 41.298  10.120  1.00 24.95 ? 352 VAL A CB    1 
ATOM   8805  C CG1   . VAL C  1 352 ? -33.940 41.127  11.656  1.00 23.24 ? 352 VAL A CG1   1 
ATOM   8806  C CG2   . VAL C  1 352 ? -34.145 42.757  9.737   1.00 23.44 ? 352 VAL A CG2   1 
ATOM   8807  N N     . ALA C  1 353 ? -32.711 38.464  9.123   1.00 25.04 ? 353 ALA A N     1 
ATOM   8808  C CA    . ALA C  1 353 ? -32.460 37.039  9.346   1.00 25.19 ? 353 ALA A CA    1 
ATOM   8809  C C     . ALA C  1 353 ? -30.969 36.693  9.243   1.00 33.62 ? 353 ALA A C     1 
ATOM   8810  O O     . ALA C  1 353 ? -30.414 36.017  10.123  1.00 37.20 ? 353 ALA A O     1 
ATOM   8811  C CB    . ALA C  1 353 ? -33.270 36.223  8.343   1.00 26.40 ? 353 ALA A CB    1 
ATOM   8812  N N     . GLU C  1 354 ? -30.314 37.127  8.152   1.00 33.24 ? 354 GLU A N     1 
ATOM   8813  C CA    . GLU C  1 354 ? -28.873 36.919  7.974   1.00 31.96 ? 354 GLU A CA    1 
ATOM   8814  C C     . GLU C  1 354 ? -28.082 37.479  9.135   1.00 32.61 ? 354 GLU A C     1 
ATOM   8815  O O     . GLU C  1 354 ? -27.092 36.883  9.574   1.00 34.68 ? 354 GLU A O     1 
ATOM   8816  C CB    . GLU C  1 354 ? -28.386 37.605  6.709   1.00 25.36 ? 354 GLU A CB    1 
ATOM   8817  C CG    . GLU C  1 354 ? -29.010 37.118  5.441   1.00 33.87 ? 354 GLU A CG    1 
ATOM   8818  C CD    . GLU C  1 354 ? -27.994 37.057  4.332   1.00 37.13 ? 354 GLU A CD    1 
ATOM   8819  O OE1   . GLU C  1 354 ? -27.356 38.104  4.043   1.00 41.75 ? 354 GLU A OE1   1 
ATOM   8820  O OE2   . GLU C  1 354 ? -27.821 35.958  3.766   1.00 38.15 ? 354 GLU A OE2   1 
ATOM   8821  N N     . ARG C  1 355 ? -28.464 38.654  9.603   1.00 27.79 ? 355 ARG A N     1 
ATOM   8822  C CA    . ARG C  1 355 ? -27.660 39.310  10.607  1.00 34.55 ? 355 ARG A CA    1 
ATOM   8823  C C     . ARG C  1 355 ? -27.880 38.679  11.966  1.00 34.22 ? 355 ARG A C     1 
ATOM   8824  O O     . ARG C  1 355 ? -26.944 38.605  12.769  1.00 34.28 ? 355 ARG A O     1 
ATOM   8825  C CB    . ARG C  1 355 ? -27.979 40.807  10.622  1.00 34.18 ? 355 ARG A CB    1 
ATOM   8826  C CG    . ARG C  1 355 ? -27.363 41.571  9.461   1.00 26.87 ? 355 ARG A CG    1 
ATOM   8827  C CD    . ARG C  1 355 ? -27.764 43.040  9.484   1.00 32.80 ? 355 ARG A CD    1 
ATOM   8828  N NE    . ARG C  1 355 ? -26.680 43.892  9.961   1.00 36.11 ? 355 ARG A NE    1 
ATOM   8829  C CZ    . ARG C  1 355 ? -26.760 45.209  10.099  1.00 31.85 ? 355 ARG A CZ    1 
ATOM   8830  N NH1   . ARG C  1 355 ? -27.864 45.868  9.794   1.00 30.36 ? 355 ARG A NH1   1 
ATOM   8831  N NH2   . ARG C  1 355 ? -25.702 45.880  10.550  1.00 32.12 ? 355 ARG A NH2   1 
ATOM   8832  N N     . LEU C  1 356 ? -29.091 38.191  12.222  1.00 33.91 ? 356 LEU A N     1 
ATOM   8833  C CA    . LEU C  1 356 ? -29.403 37.595  13.511  1.00 31.07 ? 356 LEU A CA    1 
ATOM   8834  C C     . LEU C  1 356 ? -29.119 36.103  13.518  1.00 30.06 ? 356 LEU A C     1 
ATOM   8835  O O     . LEU C  1 356 ? -28.447 35.599  14.419  1.00 34.44 ? 356 LEU A O     1 
ATOM   8836  C CB    . LEU C  1 356 ? -30.865 37.852  13.854  1.00 29.68 ? 356 LEU A CB    1 
ATOM   8837  C CG    . LEU C  1 356 ? -31.214 39.086  14.662  1.00 25.63 ? 356 LEU A CG    1 
ATOM   8838  C CD1   . LEU C  1 356 ? -30.623 40.347  14.104  1.00 27.85 ? 356 LEU A CD1   1 
ATOM   8839  C CD2   . LEU C  1 356 ? -32.705 39.190  14.614  1.00 39.16 ? 356 LEU A CD2   1 
ATOM   8840  N N     . LEU C  1 357 ? -29.600 35.389  12.511  1.00 24.88 ? 357 LEU A N     1 
ATOM   8841  C CA    . LEU C  1 357 ? -29.522 33.942  12.519  1.00 28.93 ? 357 LEU A CA    1 
ATOM   8842  C C     . LEU C  1 357 ? -28.395 33.392  11.660  1.00 36.53 ? 357 LEU A C     1 
ATOM   8843  O O     . LEU C  1 357 ? -28.242 32.167  11.585  1.00 33.52 ? 357 LEU A O     1 
ATOM   8844  C CB    . LEU C  1 357 ? -30.853 33.365  12.068  1.00 30.72 ? 357 LEU A CB    1 
ATOM   8845  C CG    . LEU C  1 357 ? -31.967 33.760  13.038  1.00 30.06 ? 357 LEU A CG    1 
ATOM   8846  C CD1   . LEU C  1 357 ? -33.098 32.782  12.920  1.00 34.35 ? 357 LEU A CD1   1 
ATOM   8847  C CD2   . LEU C  1 357 ? -31.483 33.804  14.474  1.00 33.04 ? 357 LEU A CD2   1 
ATOM   8848  N N     . GLY C  1 358 ? -27.609 34.259  11.013  1.00 33.72 ? 358 GLY A N     1 
ATOM   8849  C CA    . GLY C  1 358 ? -26.500 33.841  10.181  1.00 37.86 ? 358 GLY A CA    1 
ATOM   8850  C C     . GLY C  1 358 ? -26.905 33.525  8.746   1.00 42.06 ? 358 GLY A C     1 
ATOM   8851  O O     . GLY C  1 358 ? -28.085 33.421  8.393   1.00 37.70 ? 358 GLY A O     1 
ATOM   8852  N N     . HIS C  1 359 ? -25.881 33.362  7.905   1.00 41.34 ? 359 HIS A N     1 
ATOM   8853  C CA    . HIS C  1 359 ? -26.088 33.003  6.507   1.00 40.33 ? 359 HIS A CA    1 
ATOM   8854  C C     . HIS C  1 359 ? -26.720 31.620  6.389   1.00 35.07 ? 359 HIS A C     1 
ATOM   8855  O O     . HIS C  1 359 ? -26.589 30.782  7.279   1.00 37.39 ? 359 HIS A O     1 
ATOM   8856  C CB    . HIS C  1 359 ? -24.761 33.053  5.749   1.00 34.46 ? 359 HIS A CB    1 
ATOM   8857  C CG    . HIS C  1 359 ? -24.286 34.448  5.480   1.00 37.86 ? 359 HIS A CG    1 
ATOM   8858  N ND1   . HIS C  1 359 ? -24.817 35.238  4.482   1.00 38.24 ? 359 HIS A ND1   1 
ATOM   8859  C CD2   . HIS C  1 359 ? -23.350 35.207  6.098   1.00 42.71 ? 359 HIS A CD2   1 
ATOM   8860  C CE1   . HIS C  1 359 ? -24.225 36.419  4.492   1.00 36.84 ? 359 HIS A CE1   1 
ATOM   8861  N NE2   . HIS C  1 359 ? -23.332 36.427  5.465   1.00 41.85 ? 359 HIS A NE2   1 
ATOM   8862  N N     . ASP C  1 360 ? -27.429 31.395  5.284   1.00 31.07 ? 360 ASP A N     1 
ATOM   8863  C CA    . ASP C  1 360 ? -28.149 30.143  5.071   1.00 32.97 ? 360 ASP A CA    1 
ATOM   8864  C C     . ASP C  1 360 ? -28.985 29.772  6.289   1.00 36.91 ? 360 ASP A C     1 
ATOM   8865  O O     . ASP C  1 360 ? -29.105 28.592  6.639   1.00 32.09 ? 360 ASP A O     1 
ATOM   8866  C CB    . ASP C  1 360 ? -27.188 29.013  4.734   1.00 32.82 ? 360 ASP A CB    1 
ATOM   8867  C CG    . ASP C  1 360 ? -25.961 29.497  4.011   1.00 39.63 ? 360 ASP A CG    1 
ATOM   8868  O OD1   . ASP C  1 360 ? -26.072 30.176  2.964   1.00 37.60 ? 360 ASP A OD1   1 
ATOM   8869  O OD2   . ASP C  1 360 ? -24.868 29.232  4.535   1.00 33.97 ? 360 ASP A OD2   1 
ATOM   8870  N N     . TYR C  1 361 ? -29.532 30.799  6.955   1.00 37.78 ? 361 TYR A N     1 
ATOM   8871  C CA    . TYR C  1 361 ? -30.400 30.596  8.114   1.00 33.60 ? 361 TYR A CA    1 
ATOM   8872  C C     . TYR C  1 361 ? -31.577 29.702  7.778   1.00 32.02 ? 361 TYR A C     1 
ATOM   8873  O O     . TYR C  1 361 ? -32.110 29.015  8.659   1.00 31.52 ? 361 TYR A O     1 
ATOM   8874  C CB    . TYR C  1 361 ? -30.907 31.946  8.612   1.00 32.06 ? 361 TYR A CB    1 
ATOM   8875  C CG    . TYR C  1 361 ? -31.622 32.716  7.519   1.00 32.77 ? 361 TYR A CG    1 
ATOM   8876  C CD1   . TYR C  1 361 ? -32.977 32.545  7.317   1.00 30.83 ? 361 TYR A CD1   1 
ATOM   8877  C CD2   . TYR C  1 361 ? -30.939 33.588  6.668   1.00 34.20 ? 361 TYR A CD2   1 
ATOM   8878  C CE1   . TYR C  1 361 ? -33.649 33.211  6.320   1.00 30.85 ? 361 TYR A CE1   1 
ATOM   8879  C CE2   . TYR C  1 361 ? -31.609 34.273  5.657   1.00 29.94 ? 361 TYR A CE2   1 
ATOM   8880  C CZ    . TYR C  1 361 ? -32.974 34.070  5.495   1.00 32.15 ? 361 TYR A CZ    1 
ATOM   8881  O OH    . TYR C  1 361 ? -33.693 34.713  4.517   1.00 31.90 ? 361 TYR A OH    1 
ATOM   8882  N N     . ALA C  1 362 ? -31.997 29.704  6.507   1.00 31.77 ? 362 ALA A N     1 
ATOM   8883  C CA    . ALA C  1 362 ? -33.179 28.965  6.081   1.00 36.62 ? 362 ALA A CA    1 
ATOM   8884  C C     . ALA C  1 362 ? -32.994 27.469  6.204   1.00 36.69 ? 362 ALA A C     1 
ATOM   8885  O O     . ALA C  1 362 ? -33.972 26.725  6.084   1.00 39.59 ? 362 ALA A O     1 
ATOM   8886  C CB    . ALA C  1 362 ? -33.550 29.323  4.644   1.00 37.03 ? 362 ALA A CB    1 
ATOM   8887  N N     . ARG C  1 363 ? -31.771 27.018  6.443   1.00 37.44 ? 363 ARG A N     1 
ATOM   8888  C CA    . ARG C  1 363 ? -31.550 25.649  6.862   1.00 39.47 ? 363 ARG A CA    1 
ATOM   8889  C C     . ARG C  1 363 ? -32.519 25.278  7.974   1.00 41.41 ? 363 ARG A C     1 
ATOM   8890  O O     . ARG C  1 363 ? -33.427 24.473  7.759   1.00 41.63 ? 363 ARG A O     1 
ATOM   8891  C CB    . ARG C  1 363 ? -30.111 25.475  7.315   1.00 45.95 ? 363 ARG A CB    1 
ATOM   8892  C CG    . ARG C  1 363 ? -29.257 24.793  6.270   1.00 51.11 ? 363 ARG A CG    1 
ATOM   8893  C CD    . ARG C  1 363 ? -28.100 24.072  6.929   1.00 55.92 ? 363 ARG A CD    1 
ATOM   8894  N NE    . ARG C  1 363 ? -28.527 22.794  7.484   1.00 59.52 ? 363 ARG A NE    1 
ATOM   8895  C CZ    . ARG C  1 363 ? -28.359 22.448  8.751   1.00 61.69 ? 363 ARG A CZ    1 
ATOM   8896  N NH1   . ARG C  1 363 ? -27.797 23.274  9.622   1.00 52.73 ? 363 ARG A NH1   1 
ATOM   8897  N NH2   . ARG C  1 363 ? -28.797 21.260  9.164   1.00 66.17 ? 363 ARG A NH2   1 
ATOM   8898  N N     . ASN C  1 364 ? -32.384 25.894  9.145   1.00 40.38 ? 364 ASN A N     1 
ATOM   8899  C CA    . ASN C  1 364 ? -33.142 25.418  10.295  1.00 45.41 ? 364 ASN A CA    1 
ATOM   8900  C C     . ASN C  1 364 ? -33.944 26.520  10.968  1.00 43.16 ? 364 ASN A C     1 
ATOM   8901  O O     . ASN C  1 364 ? -34.274 26.416  12.156  1.00 38.56 ? 364 ASN A O     1 
ATOM   8902  C CB    . ASN C  1 364 ? -32.207 24.752  11.292  1.00 49.65 ? 364 ASN A CB    1 
ATOM   8903  C CG    . ASN C  1 364 ? -31.438 23.631  10.666  1.00 53.26 ? 364 ASN A CG    1 
ATOM   8904  O OD1   . ASN C  1 364 ? -30.337 23.841  10.168  1.00 52.60 ? 364 ASN A OD1   1 
ATOM   8905  N ND2   . ASN C  1 364 ? -32.023 22.432  10.657  1.00 56.74 ? 364 ASN A ND2   1 
ATOM   8906  N N     . ASN C  1 365 ? -34.301 27.560  10.227  1.00 38.38 ? 365 ASN A N     1 
ATOM   8907  C CA    . ASN C  1 365 ? -35.016 28.670  10.824  1.00 38.77 ? 365 ASN A CA    1 
ATOM   8908  C C     . ASN C  1 365 ? -36.189 29.086  9.948   1.00 39.44 ? 365 ASN A C     1 
ATOM   8909  O O     . ASN C  1 365 ? -36.127 29.004  8.715   1.00 37.52 ? 365 ASN A O     1 
ATOM   8910  C CB    . ASN C  1 365 ? -34.070 29.867  11.063  1.00 41.92 ? 365 ASN A CB    1 
ATOM   8911  C CG    . ASN C  1 365 ? -32.953 29.548  12.057  1.00 41.27 ? 365 ASN A CG    1 
ATOM   8912  O OD1   . ASN C  1 365 ? -33.135 29.636  13.285  1.00 45.21 ? 365 ASN A OD1   1 
ATOM   8913  N ND2   . ASN C  1 365 ? -31.790 29.180  11.530  1.00 34.59 ? 365 ASN A ND2   1 
ATOM   8914  N N     . PHE C  1 366 ? -37.265 29.524  10.614  1.00 43.53 ? 366 PHE A N     1 
ATOM   8915  C CA    . PHE C  1 366 ? -38.429 30.128  9.976   1.00 37.69 ? 366 PHE A CA    1 
ATOM   8916  C C     . PHE C  1 366 ? -38.663 31.534  10.526  1.00 34.12 ? 366 PHE A C     1 
ATOM   8917  O O     . PHE C  1 366 ? -38.314 31.829  11.678  1.00 33.72 ? 366 PHE A O     1 
ATOM   8918  C CB    . PHE C  1 366 ? -39.734 29.316  10.181  1.00 38.46 ? 366 PHE A CB    1 
ATOM   8919  C CG    . PHE C  1 366 ? -39.687 27.902  9.664   1.00 39.40 ? 366 PHE A CG    1 
ATOM   8920  C CD1   . PHE C  1 366 ? -40.065 27.595  8.366   1.00 40.53 ? 366 PHE A CD1   1 
ATOM   8921  C CD2   . PHE C  1 366 ? -39.310 26.869  10.509  1.00 42.24 ? 366 PHE A CD2   1 
ATOM   8922  C CE1   . PHE C  1 366 ? -40.033 26.285  7.916   1.00 38.22 ? 366 PHE A CE1   1 
ATOM   8923  C CE2   . PHE C  1 366 ? -39.273 25.571  10.064  1.00 39.29 ? 366 PHE A CE2   1 
ATOM   8924  C CZ    . PHE C  1 366 ? -39.640 25.276  8.770   1.00 31.38 ? 366 PHE A CZ    1 
ATOM   8925  N N     . PHE C  1 367 ? -39.265 32.396  9.685   1.00 32.53 ? 367 PHE A N     1 
ATOM   8926  C CA    . PHE C  1 367 ? -39.779 33.703  10.085  1.00 34.31 ? 367 PHE A CA    1 
ATOM   8927  C C     . PHE C  1 367 ? -41.117 34.001  9.418   1.00 33.92 ? 367 PHE A C     1 
ATOM   8928  O O     . PHE C  1 367 ? -41.585 33.284  8.528   1.00 32.10 ? 367 PHE A O     1 
ATOM   8929  C CB    . PHE C  1 367 ? -38.799 34.841  9.786   1.00 33.34 ? 367 PHE A CB    1 
ATOM   8930  C CG    . PHE C  1 367 ? -38.686 35.208  8.332   1.00 32.07 ? 367 PHE A CG    1 
ATOM   8931  C CD1   . PHE C  1 367 ? -39.643 36.012  7.709   1.00 30.32 ? 367 PHE A CD1   1 
ATOM   8932  C CD2   . PHE C  1 367 ? -37.584 34.803  7.593   1.00 30.33 ? 367 PHE A CD2   1 
ATOM   8933  C CE1   . PHE C  1 367 ? -39.519 36.361  6.362   1.00 29.51 ? 367 PHE A CE1   1 
ATOM   8934  C CE2   . PHE C  1 367 ? -37.452 35.161  6.249   1.00 30.87 ? 367 PHE A CE2   1 
ATOM   8935  C CZ    . PHE C  1 367 ? -38.418 35.931  5.633   1.00 27.63 ? 367 PHE A CZ    1 
ATOM   8936  N N     . SER C  1 368 ? -41.721 35.098  9.865   1.00 32.56 ? 368 SER A N     1 
ATOM   8937  C CA    . SER C  1 368 ? -43.031 35.539  9.405   1.00 33.43 ? 368 SER A CA    1 
ATOM   8938  C C     . SER C  1 368 ? -43.328 36.899  10.022  1.00 33.32 ? 368 SER A C     1 
ATOM   8939  O O     . SER C  1 368 ? -42.761 37.267  11.059  1.00 33.74 ? 368 SER A O     1 
ATOM   8940  C CB    . SER C  1 368 ? -44.136 34.543  9.766   1.00 36.32 ? 368 SER A CB    1 
ATOM   8941  O OG    . SER C  1 368 ? -45.338 34.882  9.082   1.00 36.98 ? 368 SER A OG    1 
ATOM   8942  N N     . SER C  1 369 ? -44.245 37.631  9.383   1.00 34.44 ? 369 SER A N     1 
ATOM   8943  C CA    . SER C  1 369 ? -44.475 39.042  9.672   1.00 32.46 ? 369 SER A CA    1 
ATOM   8944  C C     . SER C  1 369 ? -45.933 39.306  10.010  1.00 31.60 ? 369 SER A C     1 
ATOM   8945  O O     . SER C  1 369 ? -46.845 38.758  9.380   1.00 39.23 ? 369 SER A O     1 
ATOM   8946  C CB    . SER C  1 369 ? -44.069 39.927  8.481   1.00 31.37 ? 369 SER A CB    1 
ATOM   8947  O OG    . SER C  1 369 ? -45.017 39.838  7.425   1.00 27.85 ? 369 SER A OG    1 
ATOM   8948  N N     . ILE C  1 370 ? -46.134 40.162  10.995  1.00 28.96 ? 370 ILE A N     1 
ATOM   8949  C CA    . ILE C  1 370 ? -47.438 40.715  11.319  1.00 34.00 ? 370 ILE A CA    1 
ATOM   8950  C C     . ILE C  1 370 ? -47.405 42.171  10.882  1.00 37.23 ? 370 ILE A C     1 
ATOM   8951  O O     . ILE C  1 370 ? -46.522 42.931  11.308  1.00 36.66 ? 370 ILE A O     1 
ATOM   8952  C CB    . ILE C  1 370 ? -47.758 40.602  12.822  1.00 35.28 ? 370 ILE A CB    1 
ATOM   8953  C CG1   . ILE C  1 370 ? -47.707 39.144  13.301  1.00 38.86 ? 370 ILE A CG1   1 
ATOM   8954  C CG2   . ILE C  1 370 ? -49.118 41.197  13.118  1.00 32.85 ? 370 ILE A CG2   1 
ATOM   8955  C CD1   . ILE C  1 370 ? -46.873 38.939  14.564  1.00 31.03 ? 370 ILE A CD1   1 
ATOM   8956  N N     . LEU C  1 371 ? -48.355 42.555  10.027  1.00 34.60 ? 371 LEU A N     1 
ATOM   8957  C CA    . LEU C  1 371 ? -48.522 43.944  9.619   1.00 35.63 ? 371 LEU A CA    1 
ATOM   8958  C C     . LEU C  1 371 ? -49.552 44.696  10.442  1.00 37.64 ? 371 LEU A C     1 
ATOM   8959  O O     . LEU C  1 371 ? -49.488 45.929  10.495  1.00 38.89 ? 371 LEU A O     1 
ATOM   8960  C CB    . LEU C  1 371 ? -48.961 44.033  8.156   1.00 39.16 ? 371 LEU A CB    1 
ATOM   8961  C CG    . LEU C  1 371 ? -48.040 43.468  7.090   1.00 34.99 ? 371 LEU A CG    1 
ATOM   8962  C CD1   . LEU C  1 371 ? -48.663 43.732  5.741   1.00 32.19 ? 371 LEU A CD1   1 
ATOM   8963  C CD2   . LEU C  1 371 ? -46.660 44.098  7.191   1.00 33.91 ? 371 LEU A CD2   1 
ATOM   8964  N N     . ASN C  1 372 ? -50.509 43.992  11.057  1.00 38.58 ? 372 ASN A N     1 
ATOM   8965  C CA    . ASN C  1 372 ? -51.662 44.627  11.683  1.00 37.06 ? 372 ASN A CA    1 
ATOM   8966  C C     . ASN C  1 372 ? -51.600 44.606  13.205  1.00 40.02 ? 372 ASN A C     1 
ATOM   8967  O O     . ASN C  1 372 ? -52.641 44.576  13.861  1.00 46.78 ? 372 ASN A O     1 
ATOM   8968  C CB    . ASN C  1 372 ? -52.982 43.997  11.211  1.00 40.15 ? 372 ASN A CB    1 
ATOM   8969  C CG    . ASN C  1 372 ? -53.025 42.473  11.327  1.00 43.27 ? 372 ASN A CG    1 
ATOM   8970  O OD1   . ASN C  1 372 ? -52.108 41.832  11.839  1.00 43.43 ? 372 ASN A OD1   1 
ATOM   8971  N ND2   . ASN C  1 372 ? -54.112 41.888  10.834  1.00 41.94 ? 372 ASN A ND2   1 
ATOM   8972  N N     . VAL C  1 373 ? -50.411 44.631  13.803  1.00 37.82 ? 373 VAL A N     1 
ATOM   8973  C CA    . VAL C  1 373 ? -50.392 44.803  15.249  1.00 38.07 ? 373 VAL A CA    1 
ATOM   8974  C C     . VAL C  1 373 ? -50.935 46.191  15.566  1.00 40.04 ? 373 VAL A C     1 
ATOM   8975  O O     . VAL C  1 373 ? -50.711 47.153  14.814  1.00 38.89 ? 373 VAL A O     1 
ATOM   8976  C CB    . VAL C  1 373 ? -48.985 44.589  15.838  1.00 36.40 ? 373 VAL A CB    1 
ATOM   8977  C CG1   . VAL C  1 373 ? -48.917 45.105  17.284  1.00 35.93 ? 373 VAL A CG1   1 
ATOM   8978  C CG2   . VAL C  1 373 ? -48.628 43.139  15.842  1.00 33.52 ? 373 VAL A CG2   1 
ATOM   8979  N N     . VAL C  1 374 ? -51.693 46.291  16.656  1.00 39.62 ? 374 VAL A N     1 
ATOM   8980  C CA    . VAL C  1 374 ? -52.202 47.579  17.115  1.00 38.16 ? 374 VAL A CA    1 
ATOM   8981  C C     . VAL C  1 374 ? -51.021 48.511  17.358  1.00 36.22 ? 374 VAL A C     1 
ATOM   8982  O O     . VAL C  1 374 ? -50.094 48.162  18.105  1.00 38.52 ? 374 VAL A O     1 
ATOM   8983  C CB    . VAL C  1 374 ? -53.073 47.438  18.369  1.00 30.76 ? 374 VAL A CB    1 
ATOM   8984  C CG1   . VAL C  1 374 ? -53.295 48.781  18.967  1.00 30.95 ? 374 VAL A CG1   1 
ATOM   8985  C CG2   . VAL C  1 374 ? -54.414 46.828  18.022  1.00 38.78 ? 374 VAL A CG2   1 
ATOM   8986  N N     . PRO C  1 375 ? -50.998 49.675  16.711  1.00 36.38 ? 375 PRO A N     1 
ATOM   8987  C CA    . PRO C  1 375 ? -49.867 50.589  16.864  1.00 38.60 ? 375 PRO A CA    1 
ATOM   8988  C C     . PRO C  1 375 ? -49.662 50.989  18.311  1.00 40.24 ? 375 PRO A C     1 
ATOM   8989  O O     . PRO C  1 375 ? -50.591 50.992  19.118  1.00 44.75 ? 375 PRO A O     1 
ATOM   8990  C CB    . PRO C  1 375 ? -50.271 51.794  16.008  1.00 38.71 ? 375 PRO A CB    1 
ATOM   8991  C CG    . PRO C  1 375 ? -51.174 51.228  14.961  1.00 37.19 ? 375 PRO A CG    1 
ATOM   8992  C CD    . PRO C  1 375 ? -51.875 50.057  15.591  1.00 38.36 ? 375 PRO A CD    1 
ATOM   8993  N N     . ALA C  1 376 ? -48.427 51.356  18.625  1.00 44.15 ? 376 ALA A N     1 
ATOM   8994  C CA    . ALA C  1 376 ? -48.077 51.718  19.985  1.00 41.15 ? 376 ALA A CA    1 
ATOM   8995  C C     . ALA C  1 376 ? -46.630 52.166  19.974  1.00 39.00 ? 376 ALA A C     1 
ATOM   8996  O O     . ALA C  1 376 ? -45.889 51.894  19.024  1.00 40.61 ? 376 ALA A O     1 
ATOM   8997  C CB    . ALA C  1 376 ? -48.257 50.549  20.955  1.00 46.06 ? 376 ALA A CB    1 
ATOM   8998  N N     . GLY C  1 377 ? -46.240 52.851  21.039  1.00 36.33 ? 377 GLY A N     1 
ATOM   8999  C CA    . GLY C  1 377 ? -44.860 53.237  21.197  1.00 36.17 ? 377 GLY A CA    1 
ATOM   9000  C C     . GLY C  1 377 ? -43.956 52.021  21.249  1.00 42.30 ? 377 GLY A C     1 
ATOM   9001  O O     . GLY C  1 377 ? -44.389 50.865  21.300  1.00 43.45 ? 377 GLY A O     1 
ATOM   9002  N N     . LEU C  1 378 ? -42.653 52.303  21.230  1.00 40.86 ? 378 LEU A N     1 
ATOM   9003  C CA    . LEU C  1 378 ? -41.673 51.229  21.304  1.00 43.19 ? 378 LEU A CA    1 
ATOM   9004  C C     . LEU C  1 378 ? -41.711 50.542  22.668  1.00 35.00 ? 378 LEU A C     1 
ATOM   9005  O O     . LEU C  1 378 ? -41.559 49.318  22.755  1.00 30.44 ? 378 LEU A O     1 
ATOM   9006  C CB    . LEU C  1 378 ? -40.279 51.782  20.984  1.00 40.76 ? 378 LEU A CB    1 
ATOM   9007  C CG    . LEU C  1 378 ? -39.156 50.761  20.822  1.00 32.93 ? 378 LEU A CG    1 
ATOM   9008  C CD1   . LEU C  1 378 ? -39.660 49.518  20.132  1.00 29.58 ? 378 LEU A CD1   1 
ATOM   9009  C CD2   . LEU C  1 378 ? -38.039 51.384  20.023  1.00 37.80 ? 378 LEU A CD2   1 
ATOM   9010  N N     . ALA C  1 379 ? -41.946 51.313  23.737  1.00 41.66 ? 379 ALA A N     1 
ATOM   9011  C CA    . ALA C  1 379 ? -42.036 50.751  25.087  1.00 32.61 ? 379 ALA A CA    1 
ATOM   9012  C C     . ALA C  1 379 ? -43.191 49.773  25.212  1.00 35.65 ? 379 ALA A C     1 
ATOM   9013  O O     . ALA C  1 379 ? -43.009 48.634  25.656  1.00 40.87 ? 379 ALA A O     1 
ATOM   9014  C CB    . ALA C  1 379 ? -42.209 51.872  26.103  1.00 40.03 ? 379 ALA A CB    1 
ATOM   9015  N N     . ASP C  1 380 ? -44.401 50.217  24.857  1.00 38.54 ? 380 ASP A N     1 
ATOM   9016  C CA    . ASP C  1 380 ? -45.585 49.374  25.000  1.00 37.62 ? 380 ASP A CA    1 
ATOM   9017  C C     . ASP C  1 380 ? -45.503 48.154  24.102  1.00 34.90 ? 380 ASP A C     1 
ATOM   9018  O O     . ASP C  1 380 ? -46.027 47.091  24.441  1.00 36.37 ? 380 ASP A O     1 
ATOM   9019  C CB    . ASP C  1 380 ? -46.828 50.194  24.673  1.00 32.62 ? 380 ASP A CB    1 
ATOM   9020  C CG    . ASP C  1 380 ? -46.803 51.550  25.339  1.00 40.99 ? 380 ASP A CG    1 
ATOM   9021  O OD1   . ASP C  1 380 ? -46.734 51.605  26.582  1.00 41.23 ? 380 ASP A OD1   1 
ATOM   9022  O OD2   . ASP C  1 380 ? -46.811 52.569  24.618  1.00 49.21 ? 380 ASP A OD2   1 
ATOM   9023  N N     . LEU C  1 381 ? -44.839 48.296  22.957  1.00 37.70 ? 381 LEU A N     1 
ATOM   9024  C CA    . LEU C  1 381 ? -44.716 47.194  22.016  1.00 34.36 ? 381 LEU A CA    1 
ATOM   9025  C C     . LEU C  1 381 ? -43.756 46.143  22.545  1.00 29.89 ? 381 LEU A C     1 
ATOM   9026  O O     . LEU C  1 381 ? -44.094 44.957  22.626  1.00 25.64 ? 381 LEU A O     1 
ATOM   9027  C CB    . LEU C  1 381 ? -44.246 47.728  20.664  1.00 28.84 ? 381 LEU A CB    1 
ATOM   9028  C CG    . LEU C  1 381 ? -45.423 48.030  19.759  1.00 30.70 ? 381 LEU A CG    1 
ATOM   9029  C CD1   . LEU C  1 381 ? -44.957 48.514  18.394  1.00 33.97 ? 381 LEU A CD1   1 
ATOM   9030  C CD2   . LEU C  1 381 ? -46.239 46.758  19.638  1.00 35.03 ? 381 LEU A CD2   1 
ATOM   9031  N N     . LEU C  1 382 ? -42.546 46.566  22.901  1.00 26.97 ? 382 LEU A N     1 
ATOM   9032  C CA    . LEU C  1 382 ? -41.600 45.642  23.494  1.00 30.08 ? 382 LEU A CA    1 
ATOM   9033  C C     . LEU C  1 382 ? -42.171 45.048  24.769  1.00 36.30 ? 382 LEU A C     1 
ATOM   9034  O O     . LEU C  1 382 ? -41.971 43.862  25.063  1.00 32.07 ? 382 LEU A O     1 
ATOM   9035  C CB    . LEU C  1 382 ? -40.284 46.359  23.781  1.00 29.18 ? 382 LEU A CB    1 
ATOM   9036  C CG    . LEU C  1 382 ? -39.491 46.681  22.513  1.00 34.71 ? 382 LEU A CG    1 
ATOM   9037  C CD1   . LEU C  1 382 ? -38.303 47.599  22.808  1.00 26.96 ? 382 LEU A CD1   1 
ATOM   9038  C CD2   . LEU C  1 382 ? -39.030 45.399  21.838  1.00 36.31 ? 382 LEU A CD2   1 
ATOM   9039  N N     . ARG C  1 383 ? -42.894 45.855  25.538  1.00 30.59 ? 383 ARG A N     1 
ATOM   9040  C CA    . ARG C  1 383 ? -43.406 45.345  26.794  1.00 32.90 ? 383 ARG A CA    1 
ATOM   9041  C C     . ARG C  1 383 ? -44.389 44.205  26.545  1.00 35.78 ? 383 ARG A C     1 
ATOM   9042  O O     . ARG C  1 383 ? -44.313 43.152  27.198  1.00 32.99 ? 383 ARG A O     1 
ATOM   9043  C CB    . ARG C  1 383 ? -44.037 46.489  27.575  1.00 38.28 ? 383 ARG A CB    1 
ATOM   9044  C CG    . ARG C  1 383 ? -44.730 46.080  28.843  1.00 38.59 ? 383 ARG A CG    1 
ATOM   9045  C CD    . ARG C  1 383 ? -43.853 46.312  30.057  1.00 36.80 ? 383 ARG A CD    1 
ATOM   9046  N NE    . ARG C  1 383 ? -42.950 45.194  30.327  1.00 39.10 ? 383 ARG A NE    1 
ATOM   9047  C CZ    . ARG C  1 383 ? -43.324 43.938  30.570  1.00 37.39 ? 383 ARG A CZ    1 
ATOM   9048  N NH1   . ARG C  1 383 ? -44.597 43.561  30.528  1.00 31.62 ? 383 ARG A NH1   1 
ATOM   9049  N NH2   . ARG C  1 383 ? -42.393 43.032  30.862  1.00 33.82 ? 383 ARG A NH2   1 
ATOM   9050  N N     . SER C  1 384 ? -45.279 44.377  25.556  1.00 33.51 ? 384 SER A N     1 
ATOM   9051  C CA    . SER C  1 384 ? -46.263 43.345  25.236  1.00 34.45 ? 384 SER A CA    1 
ATOM   9052  C C     . SER C  1 384 ? -45.593 42.066  24.759  1.00 37.24 ? 384 SER A C     1 
ATOM   9053  O O     . SER C  1 384 ? -46.016 40.961  25.120  1.00 37.44 ? 384 SER A O     1 
ATOM   9054  C CB    . SER C  1 384 ? -47.233 43.850  24.172  1.00 30.62 ? 384 SER A CB    1 
ATOM   9055  O OG    . SER C  1 384 ? -47.721 45.126  24.526  1.00 35.07 ? 384 SER A OG    1 
ATOM   9056  N N     . LEU C  1 385 ? -44.569 42.190  23.913  1.00 33.29 ? 385 LEU A N     1 
ATOM   9057  C CA    . LEU C  1 385 ? -43.800 41.012  23.540  1.00 35.25 ? 385 LEU A CA    1 
ATOM   9058  C C     . LEU C  1 385 ? -43.252 40.339  24.784  1.00 31.28 ? 385 LEU A C     1 
ATOM   9059  O O     . LEU C  1 385 ? -43.393 39.127  24.971  1.00 30.09 ? 385 LEU A O     1 
ATOM   9060  C CB    . LEU C  1 385 ? -42.664 41.398  22.593  1.00 31.27 ? 385 LEU A CB    1 
ATOM   9061  C CG    . LEU C  1 385 ? -43.051 42.057  21.276  1.00 25.51 ? 385 LEU A CG    1 
ATOM   9062  C CD1   . LEU C  1 385 ? -41.795 42.488  20.636  1.00 23.73 ? 385 LEU A CD1   1 
ATOM   9063  C CD2   . LEU C  1 385 ? -43.802 41.076  20.403  1.00 25.25 ? 385 LEU A CD2   1 
ATOM   9064  N N     . GLU C  1 386 ? -42.631 41.124  25.652  1.00 35.28 ? 386 GLU A N     1 
ATOM   9065  C CA    . GLU C  1 386 ? -42.213 40.599  26.938  1.00 37.41 ? 386 GLU A CA    1 
ATOM   9066  C C     . GLU C  1 386 ? -43.393 39.967  27.647  1.00 38.85 ? 386 GLU A C     1 
ATOM   9067  O O     . GLU C  1 386 ? -43.294 38.845  28.160  1.00 39.05 ? 386 GLU A O     1 
ATOM   9068  C CB    . GLU C  1 386 ? -41.595 41.722  27.764  1.00 29.60 ? 386 GLU A CB    1 
ATOM   9069  C CG    . GLU C  1 386 ? -40.323 42.213  27.130  1.00 34.72 ? 386 GLU A CG    1 
ATOM   9070  C CD    . GLU C  1 386 ? -39.386 42.862  28.108  1.00 38.99 ? 386 GLU A CD    1 
ATOM   9071  O OE1   . GLU C  1 386 ? -39.668 42.826  29.321  1.00 38.05 ? 386 GLU A OE1   1 
ATOM   9072  O OE2   . GLU C  1 386 ? -38.349 43.400  27.659  1.00 45.61 ? 386 GLU A OE2   1 
ATOM   9073  N N     . ARG C  1 387 ? -44.541 40.646  27.624  1.00 35.07 ? 387 ARG A N     1 
ATOM   9074  C CA    . ARG C  1 387 ? -45.734 40.078  28.234  1.00 38.32 ? 387 ARG A CA    1 
ATOM   9075  C C     . ARG C  1 387 ? -46.067 38.716  27.625  1.00 38.35 ? 387 ARG A C     1 
ATOM   9076  O O     . ARG C  1 387 ? -46.458 37.788  28.343  1.00 39.25 ? 387 ARG A O     1 
ATOM   9077  C CB    . ARG C  1 387 ? -46.904 41.056  28.091  1.00 38.95 ? 387 ARG A CB    1 
ATOM   9078  C CG    . ARG C  1 387 ? -48.186 40.581  28.752  1.00 42.51 ? 387 ARG A CG    1 
ATOM   9079  C CD    . ARG C  1 387 ? -49.288 41.624  28.650  1.00 42.74 ? 387 ARG A CD    1 
ATOM   9080  N NE    . ARG C  1 387 ? -48.729 42.965  28.665  1.00 41.06 ? 387 ARG A NE    1 
ATOM   9081  C CZ    . ARG C  1 387 ? -49.031 43.917  27.795  1.00 44.56 ? 387 ARG A CZ    1 
ATOM   9082  N NH1   . ARG C  1 387 ? -49.881 43.703  26.797  1.00 36.92 ? 387 ARG A NH1   1 
ATOM   9083  N NH2   . ARG C  1 387 ? -48.465 45.116  27.931  1.00 45.87 ? 387 ARG A NH2   1 
ATOM   9084  N N     . ALA C  1 388 ? -45.871 38.555  26.317  1.00 34.54 ? 388 ALA A N     1 
ATOM   9085  C CA    . ALA C  1 388 ? -46.279 37.321  25.662  1.00 36.57 ? 388 ALA A CA    1 
ATOM   9086  C C     . ALA C  1 388 ? -45.229 36.218  25.743  1.00 34.47 ? 388 ALA A C     1 
ATOM   9087  O O     . ALA C  1 388 ? -45.539 35.073  25.393  1.00 32.74 ? 388 ALA A O     1 
ATOM   9088  C CB    . ALA C  1 388 ? -46.630 37.590  24.190  1.00 37.87 ? 388 ALA A CB    1 
ATOM   9089  N N     . GLY C  1 389 ? -44.011 36.522  26.197  1.00 32.54 ? 389 GLY A N     1 
ATOM   9090  C CA    . GLY C  1 389 ? -42.941 35.537  26.179  1.00 33.70 ? 389 GLY A CA    1 
ATOM   9091  C C     . GLY C  1 389 ? -42.301 35.298  24.828  1.00 31.22 ? 389 GLY A C     1 
ATOM   9092  O O     . GLY C  1 389 ? -41.684 34.246  24.617  1.00 32.34 ? 389 GLY A O     1 
ATOM   9093  N N     . VAL C  1 390 ? -42.401 36.257  23.912  1.00 32.52 ? 390 VAL A N     1 
ATOM   9094  C CA    . VAL C  1 390 ? -41.985 36.061  22.530  1.00 30.92 ? 390 VAL A CA    1 
ATOM   9095  C C     . VAL C  1 390 ? -41.009 37.155  22.102  1.00 30.51 ? 390 VAL A C     1 
ATOM   9096  O O     . VAL C  1 390 ? -40.723 37.307  20.916  1.00 29.09 ? 390 VAL A O     1 
ATOM   9097  C CB    . VAL C  1 390 ? -43.215 36.002  21.595  1.00 31.75 ? 390 VAL A CB    1 
ATOM   9098  C CG1   . VAL C  1 390 ? -44.254 35.013  22.129  1.00 32.08 ? 390 VAL A CG1   1 
ATOM   9099  C CG2   . VAL C  1 390 ? -43.854 37.383  21.411  1.00 33.77 ? 390 VAL A CG2   1 
ATOM   9100  N N     . ARG C  1 391 ? -40.466 37.915  23.046  1.00 30.91 ? 391 ARG A N     1 
ATOM   9101  C CA    . ARG C  1 391 ? -39.466 38.909  22.675  1.00 29.55 ? 391 ARG A CA    1 
ATOM   9102  C C     . ARG C  1 391 ? -38.197 38.217  22.209  1.00 36.94 ? 391 ARG A C     1 
ATOM   9103  O O     . ARG C  1 391 ? -37.783 37.204  22.783  1.00 39.33 ? 391 ARG A O     1 
ATOM   9104  C CB    . ARG C  1 391 ? -39.144 39.821  23.843  1.00 28.64 ? 391 ARG A CB    1 
ATOM   9105  C CG    . ARG C  1 391 ? -37.857 40.565  23.658  1.00 29.16 ? 391 ARG A CG    1 
ATOM   9106  C CD    . ARG C  1 391 ? -37.933 41.937  24.260  1.00 32.49 ? 391 ARG A CD    1 
ATOM   9107  N NE    . ARG C  1 391 ? -36.863 42.779  23.749  1.00 32.95 ? 391 ARG A NE    1 
ATOM   9108  C CZ    . ARG C  1 391 ? -36.410 43.864  24.371  1.00 40.29 ? 391 ARG A CZ    1 
ATOM   9109  N NH1   . ARG C  1 391 ? -36.962 44.301  25.495  1.00 41.93 ? 391 ARG A NH1   1 
ATOM   9110  N NH2   . ARG C  1 391 ? -35.359 44.511  23.871  1.00 33.94 ? 391 ARG A NH2   1 
ATOM   9111  N N     . TYR C  1 392 ? -37.579 38.766  21.163  1.00 32.50 ? 392 TYR A N     1 
ATOM   9112  C CA    . TYR C  1 392 ? -36.449 38.098  20.542  1.00 31.38 ? 392 TYR A CA    1 
ATOM   9113  C C     . TYR C  1 392 ? -35.285 37.921  21.509  1.00 36.77 ? 392 TYR A C     1 
ATOM   9114  O O     . TYR C  1 392 ? -34.796 38.892  22.099  1.00 30.43 ? 392 TYR A O     1 
ATOM   9115  C CB    . TYR C  1 392 ? -35.973 38.886  19.343  1.00 31.27 ? 392 TYR A CB    1 
ATOM   9116  C CG    . TYR C  1 392 ? -34.766 38.244  18.735  1.00 32.56 ? 392 TYR A CG    1 
ATOM   9117  C CD1   . TYR C  1 392 ? -34.902 37.176  17.858  1.00 35.54 ? 392 TYR A CD1   1 
ATOM   9118  C CD2   . TYR C  1 392 ? -33.491 38.676  19.052  1.00 32.12 ? 392 TYR A CD2   1 
ATOM   9119  C CE1   . TYR C  1 392 ? -33.804 36.574  17.287  1.00 33.23 ? 392 TYR A CE1   1 
ATOM   9120  C CE2   . TYR C  1 392 ? -32.385 38.074  18.492  1.00 35.56 ? 392 TYR A CE2   1 
ATOM   9121  C CZ    . TYR C  1 392 ? -32.552 37.028  17.606  1.00 32.28 ? 392 TYR A CZ    1 
ATOM   9122  O OH    . TYR C  1 392 ? -31.462 36.425  17.049  1.00 37.87 ? 392 TYR A OH    1 
ATOM   9123  N N     . ASP C  1 393 ? -34.799 36.681  21.627  1.00 37.58 ? 393 ASP A N     1 
ATOM   9124  C CA    . ASP C  1 393 ? -33.640 36.379  22.459  1.00 36.24 ? 393 ASP A CA    1 
ATOM   9125  C C     . ASP C  1 393 ? -32.491 35.868  21.605  1.00 38.40 ? 393 ASP A C     1 
ATOM   9126  O O     . ASP C  1 393 ? -32.596 34.801  20.985  1.00 39.62 ? 393 ASP A O     1 
ATOM   9127  C CB    . ASP C  1 393 ? -33.949 35.352  23.545  1.00 32.29 ? 393 ASP A CB    1 
ATOM   9128  C CG    . ASP C  1 393 ? -32.858 35.319  24.609  1.00 45.02 ? 393 ASP A CG    1 
ATOM   9129  O OD1   . ASP C  1 393 ? -31.868 36.073  24.449  1.00 46.14 ? 393 ASP A OD1   1 
ATOM   9130  O OD2   . ASP C  1 393 ? -32.972 34.552  25.593  1.00 52.28 ? 393 ASP A OD2   1 
ATOM   9131  N N     . LYS C  1 394 ? -31.375 36.596  21.635  1.00 39.87 ? 394 LYS A N     1 
ATOM   9132  C CA    . LYS C  1 394 ? -30.170 36.146  20.946  1.00 38.79 ? 394 LYS A CA    1 
ATOM   9133  C C     . LYS C  1 394 ? -29.711 34.777  21.441  1.00 42.51 ? 394 LYS A C     1 
ATOM   9134  O O     . LYS C  1 394 ? -29.057 34.036  20.703  1.00 39.61 ? 394 LYS A O     1 
ATOM   9135  C CB    . LYS C  1 394 ? -29.060 37.180  21.132  1.00 37.84 ? 394 LYS A CB    1 
ATOM   9136  C CG    . LYS C  1 394 ? -28.293 37.510  19.834  1.00 55.63 ? 394 LYS A CG    1 
ATOM   9137  C CD    . LYS C  1 394 ? -26.969 36.725  19.701  1.00 57.05 ? 394 LYS A CD    1 
ATOM   9138  C CE    . LYS C  1 394 ? -26.432 36.734  18.266  1.00 57.49 ? 394 LYS A CE    1 
ATOM   9139  N NZ    . LYS C  1 394 ? -25.193 35.913  18.150  1.00 58.25 ? 394 LYS A NZ    1 
ATOM   9140  N N     . ASP C  1 395 ? -30.046 34.419  22.681  1.00 43.80 ? 395 ASP A N     1 
ATOM   9141  C CA    . ASP C  1 395 ? -29.594 33.148  23.228  1.00 40.71 ? 395 ASP A CA    1 
ATOM   9142  C C     . ASP C  1 395 ? -30.250 31.951  22.559  1.00 40.26 ? 395 ASP A C     1 
ATOM   9143  O O     . ASP C  1 395 ? -29.756 30.831  22.702  1.00 41.14 ? 395 ASP A O     1 
ATOM   9144  C CB    . ASP C  1 395 ? -29.856 33.101  24.735  1.00 45.27 ? 395 ASP A CB    1 
ATOM   9145  C CG    . ASP C  1 395 ? -28.934 34.021  25.525  1.00 44.86 ? 395 ASP A CG    1 
ATOM   9146  O OD1   . ASP C  1 395 ? -27.798 34.274  25.062  1.00 39.21 ? 395 ASP A OD1   1 
ATOM   9147  O OD2   . ASP C  1 395 ? -29.342 34.473  26.622  1.00 49.01 ? 395 ASP A OD2   1 
ATOM   9148  N N     . SER C  1 396 ? -31.350 32.145  21.846  1.00 39.95 ? 396 SER A N     1 
ATOM   9149  C CA    . SER C  1 396 ? -32.030 31.038  21.197  1.00 38.98 ? 396 SER A CA    1 
ATOM   9150  C C     . SER C  1 396 ? -32.316 31.295  19.732  1.00 46.12 ? 396 SER A C     1 
ATOM   9151  O O     . SER C  1 396 ? -32.634 30.341  19.005  1.00 46.81 ? 396 SER A O     1 
ATOM   9152  C CB    . SER C  1 396 ? -33.358 30.747  21.892  1.00 35.91 ? 396 SER A CB    1 
ATOM   9153  O OG    . SER C  1 396 ? -34.091 31.952  21.993  1.00 31.65 ? 396 SER A OG    1 
ATOM   9154  N N     . GLY C  1 397 ? -32.217 32.543  19.277  1.00 43.06 ? 397 GLY A N     1 
ATOM   9155  C CA    . GLY C  1 397 ? -32.612 32.879  17.923  1.00 44.81 ? 397 GLY A CA    1 
ATOM   9156  C C     . GLY C  1 397 ? -34.095 32.734  17.681  1.00 42.09 ? 397 GLY A C     1 
ATOM   9157  O O     . GLY C  1 397 ? -34.512 32.373  16.570  1.00 43.76 ? 397 GLY A O     1 
ATOM   9158  N N     . GLU C  1 398 ? -34.905 32.969  18.707  1.00 39.56 ? 398 GLU A N     1 
ATOM   9159  C CA    . GLU C  1 398 ? -36.347 32.839  18.607  1.00 37.64 ? 398 GLU A CA    1 
ATOM   9160  C C     . GLU C  1 398 ? -36.987 34.073  19.226  1.00 34.87 ? 398 GLU A C     1 
ATOM   9161  O O     . GLU C  1 398 ? -36.416 34.713  20.117  1.00 30.22 ? 398 GLU A O     1 
ATOM   9162  C CB    . GLU C  1 398 ? -36.837 31.536  19.263  1.00 35.38 ? 398 GLU A CB    1 
ATOM   9163  C CG    . GLU C  1 398 ? -36.194 30.283  18.624  1.00 36.67 ? 398 GLU A CG    1 
ATOM   9164  C CD    . GLU C  1 398 ? -37.146 29.091  18.502  1.00 41.55 ? 398 GLU A CD    1 
ATOM   9165  O OE1   . GLU C  1 398 ? -38.173 29.070  19.212  1.00 36.48 ? 398 GLU A OE1   1 
ATOM   9166  O OE2   . GLU C  1 398 ? -36.875 28.175  17.682  1.00 40.86 ? 398 GLU A OE2   1 
ATOM   9167  N N     . GLY C  1 399 ? -38.146 34.445  18.689  1.00 36.07 ? 399 GLY A N     1 
ATOM   9168  C CA    . GLY C  1 399 ? -38.794 35.667  19.114  1.00 35.19 ? 399 GLY A CA    1 
ATOM   9169  C C     . GLY C  1 399 ? -39.100 36.686  18.031  1.00 31.67 ? 399 GLY A C     1 
ATOM   9170  O O     . GLY C  1 399 ? -39.146 36.375  16.834  1.00 31.23 ? 399 GLY A O     1 
ATOM   9171  N N     . ALA C  1 400 ? -39.314 37.926  18.456  1.00 31.28 ? 400 ALA A N     1 
ATOM   9172  C CA    . ALA C  1 400 ? -39.813 38.957  17.567  1.00 25.54 ? 400 ALA A CA    1 
ATOM   9173  C C     . ALA C  1 400 ? -39.100 40.268  17.847  1.00 23.03 ? 400 ALA A C     1 
ATOM   9174  O O     . ALA C  1 400 ? -38.526 40.484  18.915  1.00 28.23 ? 400 ALA A O     1 
ATOM   9175  C CB    . ALA C  1 400 ? -41.325 39.143  17.691  1.00 19.96 ? 400 ALA A CB    1 
ATOM   9176  N N     . VAL C  1 401 ? -39.137 41.128  16.840  1.00 22.51 ? 401 VAL A N     1 
ATOM   9177  C CA    . VAL C  1 401 ? -38.483 42.423  16.838  1.00 17.90 ? 401 VAL A CA    1 
ATOM   9178  C C     . VAL C  1 401 ? -39.431 43.379  16.121  1.00 20.00 ? 401 VAL A C     1 
ATOM   9179  O O     . VAL C  1 401 ? -40.379 42.962  15.458  1.00 22.46 ? 401 VAL A O     1 
ATOM   9180  C CB    . VAL C  1 401 ? -37.123 42.340  16.127  1.00 21.94 ? 401 VAL A CB    1 
ATOM   9181  C CG1   . VAL C  1 401 ? -36.267 41.329  16.797  1.00 21.20 ? 401 VAL A CG1   1 
ATOM   9182  C CG2   . VAL C  1 401 ? -37.327 41.918  14.693  1.00 19.43 ? 401 VAL A CG2   1 
ATOM   9183  N N     . VAL C  1 402 ? -39.191 44.674  16.261  1.00 23.54 ? 402 VAL A N     1 
ATOM   9184  C CA    . VAL C  1 402 ? -40.121 45.681  15.766  1.00 25.67 ? 402 VAL A CA    1 
ATOM   9185  C C     . VAL C  1 402 ? -39.518 46.320  14.526  1.00 24.23 ? 402 VAL A C     1 
ATOM   9186  O O     . VAL C  1 402 ? -38.347 46.718  14.530  1.00 21.17 ? 402 VAL A O     1 
ATOM   9187  C CB    . VAL C  1 402 ? -40.458 46.729  16.848  1.00 27.59 ? 402 VAL A CB    1 
ATOM   9188  C CG1   . VAL C  1 402 ? -40.842 48.097  16.261  1.00 26.44 ? 402 VAL A CG1   1 
ATOM   9189  C CG2   . VAL C  1 402 ? -41.578 46.226  17.731  1.00 32.59 ? 402 VAL A CG2   1 
ATOM   9190  N N     . LEU C  1 403 ? -40.328 46.400  13.461  1.00 30.80 ? 403 LEU A N     1 
ATOM   9191  C CA    . LEU C  1 403 ? -39.996 47.083  12.215  1.00 29.46 ? 403 LEU A CA    1 
ATOM   9192  C C     . LEU C  1 403 ? -40.800 48.360  12.014  1.00 30.51 ? 403 LEU A C     1 
ATOM   9193  O O     . LEU C  1 403 ? -40.582 49.076  11.029  1.00 35.03 ? 403 LEU A O     1 
ATOM   9194  C CB    . LEU C  1 403 ? -40.210 46.145  11.023  1.00 31.25 ? 403 LEU A CB    1 
ATOM   9195  C CG    . LEU C  1 403 ? -39.621 44.741  11.239  1.00 38.04 ? 403 LEU A CG    1 
ATOM   9196  C CD1   . LEU C  1 403 ? -39.928 43.848  10.047  1.00 35.41 ? 403 LEU A CD1   1 
ATOM   9197  C CD2   . LEU C  1 403 ? -38.110 44.760  11.551  1.00 29.32 ? 403 LEU A CD2   1 
ATOM   9198  N N     . GLY C  1 404 ? -41.720 48.668  12.915  1.00 28.99 ? 404 GLY A N     1 
ATOM   9199  C CA    . GLY C  1 404 ? -42.509 49.867  12.761  1.00 31.19 ? 404 GLY A CA    1 
ATOM   9200  C C     . GLY C  1 404 ? -43.542 49.939  13.856  1.00 33.53 ? 404 GLY A C     1 
ATOM   9201  O O     . GLY C  1 404 ? -44.272 48.969  14.086  1.00 33.03 ? 404 GLY A O     1 
ATOM   9202  N N     . CYS C  1 405 ? -43.586 51.074  14.558  1.00 33.94 ? 405 CYS A N     1 
ATOM   9203  C CA    . CYS C  1 405 ? -44.492 51.239  15.687  1.00 36.21 ? 405 CYS A CA    1 
ATOM   9204  C C     . CYS C  1 405 ? -45.878 51.643  15.247  1.00 36.88 ? 405 CYS A C     1 
ATOM   9205  O O     . CYS C  1 405 ? -46.830 51.484  16.018  1.00 35.22 ? 405 CYS A O     1 
ATOM   9206  C CB    . CYS C  1 405 ? -43.958 52.295  16.649  1.00 36.20 ? 405 CYS A CB    1 
ATOM   9207  S SG    . CYS C  1 405 ? -42.420 51.862  17.456  1.00 37.23 ? 405 CYS A SG    1 
ATOM   9208  N N     . ASN C  1 406 ? -45.991 52.149  14.019  1.00 37.26 ? 406 ASN A N     1 
ATOM   9209  C CA    . ASN C  1 406 ? -47.168 52.826  13.493  1.00 34.67 ? 406 ASN A CA    1 
ATOM   9210  C C     . ASN C  1 406 ? -46.981 53.038  11.996  1.00 39.06 ? 406 ASN A C     1 
ATOM   9211  O O     . ASN C  1 406 ? -46.769 54.168  11.539  1.00 38.14 ? 406 ASN A O     1 
ATOM   9212  C CB    . ASN C  1 406 ? -47.366 54.162  14.195  1.00 34.67 ? 406 ASN A CB    1 
ATOM   9213  C CG    . ASN C  1 406 ? -48.518 54.937  13.636  1.00 35.98 ? 406 ASN A CG    1 
ATOM   9214  O OD1   . ASN C  1 406 ? -49.524 54.364  13.224  1.00 36.03 ? 406 ASN A OD1   1 
ATOM   9215  N ND2   . ASN C  1 406 ? -48.366 56.259  13.587  1.00 36.24 ? 406 ASN A ND2   1 
ATOM   9216  N N     . SER C  1 407 ? -47.041 51.963  11.229  1.00 33.22 ? 407 SER A N     1 
ATOM   9217  C CA    . SER C  1 407 ? -46.643 51.999  9.835   1.00 35.21 ? 407 SER A CA    1 
ATOM   9218  C C     . SER C  1 407 ? -47.844 51.926  8.887   1.00 35.11 ? 407 SER A C     1 
ATOM   9219  O O     . SER C  1 407 ? -48.904 51.369  9.203   1.00 34.67 ? 407 SER A O     1 
ATOM   9220  C CB    . SER C  1 407 ? -45.658 50.857  9.563   1.00 33.31 ? 407 SER A CB    1 
ATOM   9221  O OG    . SER C  1 407 ? -45.866 50.329  8.267   1.00 38.03 ? 407 SER A OG    1 
ATOM   9222  N N     . ASP C  1 408 ? -47.661 52.501  7.706   1.00 35.66 ? 408 ASP A N     1 
ATOM   9223  C CA    . ASP C  1 408 ? -48.691 52.425  6.679   1.00 35.32 ? 408 ASP A CA    1 
ATOM   9224  C C     . ASP C  1 408 ? -48.795 51.028  6.068   1.00 35.77 ? 408 ASP A C     1 
ATOM   9225  O O     . ASP C  1 408 ? -49.852 50.671  5.543   1.00 33.59 ? 408 ASP A O     1 
ATOM   9226  C CB    . ASP C  1 408 ? -48.428 53.492  5.603   1.00 30.59 ? 408 ASP A CB    1 
ATOM   9227  C CG    . ASP C  1 408 ? -48.584 54.924  6.139   1.00 40.54 ? 408 ASP A CG    1 
ATOM   9228  O OD1   . ASP C  1 408 ? -49.638 55.219  6.748   1.00 37.43 ? 408 ASP A OD1   1 
ATOM   9229  O OD2   . ASP C  1 408 ? -47.655 55.753  5.969   1.00 38.87 ? 408 ASP A OD2   1 
ATOM   9230  N N     . LEU C  1 409 ? -47.738 50.218  6.162   1.00 34.19 ? 409 LEU A N     1 
ATOM   9231  C CA    . LEU C  1 409 ? -47.772 48.839  5.687   1.00 32.63 ? 409 LEU A CA    1 
ATOM   9232  C C     . LEU C  1 409 ? -48.868 48.040  6.373   1.00 38.43 ? 409 LEU A C     1 
ATOM   9233  O O     . LEU C  1 409 ? -48.762 47.742  7.569   1.00 39.52 ? 409 LEU A O     1 
ATOM   9234  C CB    . LEU C  1 409 ? -46.428 48.172  5.942   1.00 35.14 ? 409 LEU A CB    1 
ATOM   9235  C CG    . LEU C  1 409 ? -45.441 48.094  4.789   1.00 34.06 ? 409 LEU A CG    1 
ATOM   9236  C CD1   . LEU C  1 409 ? -44.308 47.096  5.126   1.00 29.21 ? 409 LEU A CD1   1 
ATOM   9237  C CD2   . LEU C  1 409 ? -46.165 47.762  3.457   1.00 30.45 ? 409 LEU A CD2   1 
ATOM   9238  N N     . GLY C  1 410 ? -49.908 47.667  5.633   1.00 43.95 ? 410 GLY A N     1 
ATOM   9239  C CA    . GLY C  1 410 ? -51.096 47.116  6.251   1.00 42.62 ? 410 GLY A CA    1 
ATOM   9240  C C     . GLY C  1 410 ? -51.749 48.115  7.188   1.00 42.66 ? 410 GLY A C     1 
ATOM   9241  O O     . GLY C  1 410 ? -51.788 49.328  6.949   1.00 38.07 ? 410 GLY A O     1 
ATOM   9242  N N     . PRO C  1 411 ? -52.304 47.639  8.249   1.00 48.71 ? 411 PRO A N     1 
ATOM   9243  C CA    . PRO C  1 411 ? -52.801 48.594  9.233   1.00 43.65 ? 411 PRO A CA    1 
ATOM   9244  C C     . PRO C  1 411 ? -51.661 49.374  9.868   1.00 43.71 ? 411 PRO A C     1 
ATOM   9245  O O     . PRO C  1 411 ? -51.534 50.576  9.614   1.00 46.85 ? 411 PRO A O     1 
ATOM   9246  C CB    . PRO C  1 411 ? -53.511 47.703  10.261  1.00 40.29 ? 411 PRO A CB    1 
ATOM   9247  C CG    . PRO C  1 411 ? -54.077 46.570  9.440   1.00 45.68 ? 411 PRO A CG    1 
ATOM   9248  C CD    . PRO C  1 411 ? -53.089 46.395  8.249   1.00 54.02 ? 411 PRO A CD    1 
ATOM   9249  N N     . GLY C  1 412 ? -50.822 48.723  10.656  1.00 37.57 ? 412 GLY A N     1 
ATOM   9250  C CA    . GLY C  1 412 ? -50.141 49.517  11.664  1.00 40.72 ? 412 GLY A CA    1 
ATOM   9251  C C     . GLY C  1 412 ? -48.807 49.011  12.146  1.00 38.34 ? 412 GLY A C     1 
ATOM   9252  O O     . GLY C  1 412 ? -47.812 49.149  11.434  1.00 45.91 ? 412 GLY A O     1 
ATOM   9253  N N     . ALA C  1 413 ? -48.744 48.473  13.359  1.00 34.06 ? 413 ALA A N     1 
ATOM   9254  C CA    . ALA C  1 413 ? -47.456 48.040  13.883  1.00 38.08 ? 413 ALA A CA    1 
ATOM   9255  C C     . ALA C  1 413 ? -46.993 46.785  13.151  1.00 36.65 ? 413 ALA A C     1 
ATOM   9256  O O     . ALA C  1 413 ? -47.779 45.867  12.915  1.00 37.26 ? 413 ALA A O     1 
ATOM   9257  C CB    . ALA C  1 413 ? -47.536 47.797  15.391  1.00 37.99 ? 413 ALA A CB    1 
ATOM   9258  N N     . GLU C  1 414 ? -45.714 46.768  12.768  1.00 32.45 ? 414 GLU A N     1 
ATOM   9259  C CA    . GLU C  1 414 ? -45.117 45.709  11.961  1.00 34.50 ? 414 GLU A CA    1 
ATOM   9260  C C     . GLU C  1 414 ? -44.069 44.969  12.785  1.00 29.64 ? 414 GLU A C     1 
ATOM   9261  O O     . GLU C  1 414 ? -43.194 45.592  13.397  1.00 28.18 ? 414 GLU A O     1 
ATOM   9262  C CB    . GLU C  1 414 ? -44.476 46.284  10.677  1.00 30.79 ? 414 GLU A CB    1 
ATOM   9263  C CG    . GLU C  1 414 ? -43.915 45.207  9.699   1.00 31.89 ? 414 GLU A CG    1 
ATOM   9264  C CD    . GLU C  1 414 ? -42.914 45.746  8.640   1.00 33.73 ? 414 GLU A CD    1 
ATOM   9265  O OE1   . GLU C  1 414 ? -42.372 46.865  8.803   1.00 34.22 ? 414 GLU A OE1   1 
ATOM   9266  O OE2   . GLU C  1 414 ? -42.674 45.029  7.644   1.00 21.50 ? 414 GLU A OE2   1 
ATOM   9267  N N     . LEU C  1 415 ? -44.145 43.645  12.784  1.00 25.73 ? 415 LEU A N     1 
ATOM   9268  C CA    . LEU C  1 415 ? -43.219 42.843  13.568  1.00 25.98 ? 415 LEU A CA    1 
ATOM   9269  C C     . LEU C  1 415 ? -42.783 41.649  12.745  1.00 30.09 ? 415 LEU A C     1 
ATOM   9270  O O     . LEU C  1 415 ? -43.553 41.119  11.934  1.00 30.43 ? 415 LEU A O     1 
ATOM   9271  C CB    . LEU C  1 415 ? -43.844 42.300  14.868  1.00 28.15 ? 415 LEU A CB    1 
ATOM   9272  C CG    . LEU C  1 415 ? -44.787 43.067  15.786  1.00 25.60 ? 415 LEU A CG    1 
ATOM   9273  C CD1   . LEU C  1 415 ? -45.256 42.152  16.916  1.00 31.74 ? 415 LEU A CD1   1 
ATOM   9274  C CD2   . LEU C  1 415 ? -44.145 44.288  16.358  1.00 29.15 ? 415 LEU A CD2   1 
ATOM   9275  N N     . LEU C  1 416 ? -41.560 41.196  13.020  1.00 33.22 ? 416 LEU A N     1 
ATOM   9276  C CA    . LEU C  1 416 ? -40.959 39.997  12.438  1.00 30.17 ? 416 LEU A CA    1 
ATOM   9277  C C     . LEU C  1 416 ? -40.729 38.973  13.536  1.00 26.65 ? 416 LEU A C     1 
ATOM   9278  O O     . LEU C  1 416 ? -40.247 39.334  14.612  1.00 25.67 ? 416 LEU A O     1 
ATOM   9279  C CB    . LEU C  1 416 ? -39.628 40.341  11.792  1.00 26.87 ? 416 LEU A CB    1 
ATOM   9280  C CG    . LEU C  1 416 ? -39.119 39.315  10.781  1.00 39.28 ? 416 LEU A CG    1 
ATOM   9281  C CD1   . LEU C  1 416 ? -40.164 39.019  9.674   1.00 30.06 ? 416 LEU A CD1   1 
ATOM   9282  C CD2   . LEU C  1 416 ? -37.830 39.837  10.195  1.00 34.58 ? 416 LEU A CD2   1 
ATOM   9283  N N     . VAL C  1 417 ? -41.054 37.706  13.277  1.00 26.47 ? 417 VAL A N     1 
ATOM   9284  C CA    . VAL C  1 417 ? -40.941 36.657  14.290  1.00 31.35 ? 417 VAL A CA    1 
ATOM   9285  C C     . VAL C  1 417 ? -40.072 35.528  13.766  1.00 31.15 ? 417 VAL A C     1 
ATOM   9286  O O     . VAL C  1 417 ? -40.264 35.072  12.635  1.00 31.36 ? 417 VAL A O     1 
ATOM   9287  C CB    . VAL C  1 417 ? -42.313 36.096  14.714  1.00 35.44 ? 417 VAL A CB    1 
ATOM   9288  C CG1   . VAL C  1 417 ? -42.174 35.380  16.039  1.00 28.39 ? 417 VAL A CG1   1 
ATOM   9289  C CG2   . VAL C  1 417 ? -43.358 37.204  14.800  1.00 30.02 ? 417 VAL A CG2   1 
ATOM   9290  N N     . PHE C  1 418 ? -39.148 35.056  14.603  1.00 29.72 ? 418 PHE A N     1 
ATOM   9291  C CA    . PHE C  1 418 ? -38.238 33.971  14.266  1.00 32.32 ? 418 PHE A CA    1 
ATOM   9292  C C     . PHE C  1 418 ? -38.469 32.778  15.178  1.00 32.55 ? 418 PHE A C     1 
ATOM   9293  O O     . PHE C  1 418 ? -38.923 32.923  16.313  1.00 29.12 ? 418 PHE A O     1 
ATOM   9294  C CB    . PHE C  1 418 ? -36.775 34.403  14.395  1.00 34.20 ? 418 PHE A CB    1 
ATOM   9295  C CG    . PHE C  1 418 ? -36.431 35.583  13.561  1.00 27.70 ? 418 PHE A CG    1 
ATOM   9296  C CD1   . PHE C  1 418 ? -36.256 35.442  12.186  1.00 28.37 ? 418 PHE A CD1   1 
ATOM   9297  C CD2   . PHE C  1 418 ? -36.319 36.841  14.139  1.00 26.16 ? 418 PHE A CD2   1 
ATOM   9298  C CE1   . PHE C  1 418 ? -35.947 36.541  11.386  1.00 28.67 ? 418 PHE A CE1   1 
ATOM   9299  C CE2   . PHE C  1 418 ? -36.020 37.946  13.363  1.00 30.58 ? 418 PHE A CE2   1 
ATOM   9300  C CZ    . PHE C  1 418 ? -35.827 37.795  11.970  1.00 29.88 ? 418 PHE A CZ    1 
ATOM   9301  N N     . SER C  1 419 ? -38.108 31.601  14.675  1.00 38.34 ? 419 SER A N     1 
ATOM   9302  C CA    . SER C  1 419 ? -38.198 30.347  15.422  1.00 40.25 ? 419 SER A CA    1 
ATOM   9303  C C     . SER C  1 419 ? -37.573 29.181  14.649  1.00 39.10 ? 419 SER A C     1 
ATOM   9304  O O     . SER C  1 419 ? -37.691 29.114  13.424  1.00 37.02 ? 419 SER A O     1 
ATOM   9305  C CB    . SER C  1 419 ? -39.659 30.020  15.755  1.00 41.17 ? 419 SER A CB    1 
ATOM   9306  O OG    . SER C  1 419 ? -39.838 28.648  16.094  1.00 38.33 ? 419 SER A OG    1 
ATOM   9307  N N     . LYS C  1 420 ? -36.905 28.262  15.340  1.00 40.03 ? 420 LYS A N     1 
ATOM   9308  C CA    . LYS C  1 420 ? -36.411 27.062  14.680  1.00 40.21 ? 420 LYS A CA    1 
ATOM   9309  C C     . LYS C  1 420 ? -37.482 25.991  14.570  1.00 35.53 ? 420 LYS A C     1 
ATOM   9310  O O     . LYS C  1 420 ? -37.125 24.839  14.327  1.00 41.39 ? 420 LYS A O     1 
ATOM   9311  C CB    . LYS C  1 420 ? -35.180 26.510  15.414  1.00 39.34 ? 420 LYS A CB    1 
ATOM   9312  C CG    . LYS C  1 420 ? -34.189 27.575  15.868  1.00 38.19 ? 420 LYS A CG    1 
ATOM   9313  C CD    . LYS C  1 420 ? -32.741 27.113  15.755  1.00 37.72 ? 420 LYS A CD    1 
ATOM   9314  C CE    . LYS C  1 420 ? -31.763 28.086  16.458  1.00 51.56 ? 420 LYS A CE    1 
ATOM   9315  N NZ    . LYS C  1 420 ? -31.809 29.522  15.987  1.00 47.24 ? 420 LYS A NZ    1 
ATOM   9316  N N     . ASP C  1 421 ? -38.760 26.360  14.734  1.00 38.44 ? 421 ASP A N     1 
ATOM   9317  C CA    . ASP C  1 421 ? -39.898 25.438  14.690  1.00 40.00 ? 421 ASP A CA    1 
ATOM   9318  C C     . ASP C  1 421 ? -41.163 26.193  14.300  1.00 39.08 ? 421 ASP A C     1 
ATOM   9319  O O     . ASP C  1 421 ? -41.637 27.040  15.068  1.00 33.49 ? 421 ASP A O     1 
ATOM   9320  C CB    . ASP C  1 421 ? -40.112 24.755  16.036  1.00 44.67 ? 421 ASP A CB    1 
ATOM   9321  C CG    . ASP C  1 421 ? -41.477 24.096  16.134  1.00 46.44 ? 421 ASP A CG    1 
ATOM   9322  O OD1   . ASP C  1 421 ? -41.589 22.928  15.711  1.00 49.03 ? 421 ASP A OD1   1 
ATOM   9323  O OD2   . ASP C  1 421 ? -42.441 24.743  16.605  1.00 46.94 ? 421 ASP A OD2   1 
ATOM   9324  N N     . TRP C  1 422 ? -41.733 25.832  13.141  1.00 42.88 ? 422 TRP A N     1 
ATOM   9325  C CA    . TRP C  1 422 ? -42.804 26.612  12.521  1.00 39.51 ? 422 TRP A CA    1 
ATOM   9326  C C     . TRP C  1 422 ? -44.013 26.731  13.420  1.00 39.66 ? 422 TRP A C     1 
ATOM   9327  O O     . TRP C  1 422 ? -44.656 27.787  13.478  1.00 42.23 ? 422 TRP A O     1 
ATOM   9328  C CB    . TRP C  1 422 ? -43.224 25.963  11.213  1.00 41.69 ? 422 TRP A CB    1 
ATOM   9329  C CG    . TRP C  1 422 ? -44.347 26.663  10.493  1.00 45.20 ? 422 TRP A CG    1 
ATOM   9330  C CD1   . TRP C  1 422 ? -45.577 26.148  10.181  1.00 43.48 ? 422 TRP A CD1   1 
ATOM   9331  C CD2   . TRP C  1 422 ? -44.317 27.986  9.943   1.00 50.29 ? 422 TRP A CD2   1 
ATOM   9332  N NE1   . TRP C  1 422 ? -46.315 27.075  9.476   1.00 45.05 ? 422 TRP A NE1   1 
ATOM   9333  C CE2   . TRP C  1 422 ? -45.561 28.211  9.322   1.00 52.37 ? 422 TRP A CE2   1 
ATOM   9334  C CE3   . TRP C  1 422 ? -43.357 29.006  9.916   1.00 49.00 ? 422 TRP A CE3   1 
ATOM   9335  C CZ2   . TRP C  1 422 ? -45.868 29.417  8.695   1.00 53.41 ? 422 TRP A CZ2   1 
ATOM   9336  C CZ3   . TRP C  1 422 ? -43.667 30.203  9.290   1.00 42.55 ? 422 TRP A CZ3   1 
ATOM   9337  C CH2   . TRP C  1 422 ? -44.908 30.397  8.690   1.00 43.95 ? 422 TRP A CH2   1 
ATOM   9338  N N     . ASP C  1 423 ? -44.374 25.638  14.084  1.00 41.46 ? 423 ASP A N     1 
ATOM   9339  C CA    . ASP C  1 423 ? -45.529 25.669  14.965  1.00 39.42 ? 423 ASP A CA    1 
ATOM   9340  C C     . ASP C  1 423 ? -45.287 26.582  16.152  1.00 37.44 ? 423 ASP A C     1 
ATOM   9341  O O     . ASP C  1 423 ? -46.175 27.347  16.534  1.00 41.55 ? 423 ASP A O     1 
ATOM   9342  C CB    . ASP C  1 423 ? -45.871 24.258  15.419  1.00 45.79 ? 423 ASP A CB    1 
ATOM   9343  C CG    . ASP C  1 423 ? -46.338 23.379  14.271  1.00 51.39 ? 423 ASP A CG    1 
ATOM   9344  O OD1   . ASP C  1 423 ? -47.101 23.876  13.403  1.00 43.56 ? 423 ASP A OD1   1 
ATOM   9345  O OD2   . ASP C  1 423 ? -45.940 22.191  14.243  1.00 52.22 ? 423 ASP A OD2   1 
ATOM   9346  N N     . ARG C  1 424 ? -44.093 26.522  16.750  1.00 38.01 ? 424 ARG A N     1 
ATOM   9347  C CA    . ARG C  1 424 ? -43.748 27.509  17.764  1.00 34.70 ? 424 ARG A CA    1 
ATOM   9348  C C     . ARG C  1 424 ? -43.969 28.903  17.230  1.00 37.21 ? 424 ARG A C     1 
ATOM   9349  O O     . ARG C  1 424 ? -44.588 29.738  17.899  1.00 36.52 ? 424 ARG A O     1 
ATOM   9350  C CB    . ARG C  1 424 ? -42.304 27.350  18.206  1.00 39.40 ? 424 ARG A CB    1 
ATOM   9351  C CG    . ARG C  1 424 ? -42.109 26.324  19.288  1.00 45.64 ? 424 ARG A CG    1 
ATOM   9352  C CD    . ARG C  1 424 ? -40.699 25.771  19.209  1.00 48.70 ? 424 ARG A CD    1 
ATOM   9353  N NE    . ARG C  1 424 ? -39.791 26.373  20.179  1.00 53.57 ? 424 ARG A NE    1 
ATOM   9354  C CZ    . ARG C  1 424 ? -38.471 26.383  20.058  1.00 46.04 ? 424 ARG A CZ    1 
ATOM   9355  N NH1   . ARG C  1 424 ? -37.877 25.940  18.960  1.00 37.36 ? 424 ARG A NH1   1 
ATOM   9356  N NH2   . ARG C  1 424 ? -37.729 26.859  21.059  1.00 43.12 ? 424 ARG A NH2   1 
ATOM   9357  N N     . LEU C  1 425 ? -43.513 29.155  15.998  1.00 36.38 ? 425 LEU A N     1 
ATOM   9358  C CA    . LEU C  1 425 ? -43.730 30.453  15.381  1.00 34.54 ? 425 LEU A CA    1 
ATOM   9359  C C     . LEU C  1 425 ? -45.204 30.799  15.356  1.00 37.05 ? 425 LEU A C     1 
ATOM   9360  O O     . LEU C  1 425 ? -45.601 31.907  15.743  1.00 38.31 ? 425 LEU A O     1 
ATOM   9361  C CB    . LEU C  1 425 ? -43.162 30.476  13.975  1.00 32.55 ? 425 LEU A CB    1 
ATOM   9362  C CG    . LEU C  1 425 ? -42.613 31.855  13.627  1.00 39.11 ? 425 LEU A CG    1 
ATOM   9363  C CD1   . LEU C  1 425 ? -41.708 31.740  12.393  1.00 45.30 ? 425 LEU A CD1   1 
ATOM   9364  C CD2   . LEU C  1 425 ? -43.708 32.897  13.395  1.00 37.87 ? 425 LEU A CD2   1 
ATOM   9365  N N     . THR C  1 426 ? -46.024 29.861  14.883  1.00 37.80 ? 426 THR A N     1 
ATOM   9366  C CA    . THR C  1 426 ? -47.470 30.038  14.862  1.00 36.99 ? 426 THR A CA    1 
ATOM   9367  C C     . THR C  1 426 ? -48.009 30.431  16.232  1.00 37.37 ? 426 THR A C     1 
ATOM   9368  O O     . THR C  1 426 ? -48.707 31.441  16.375  1.00 39.87 ? 426 THR A O     1 
ATOM   9369  C CB    . THR C  1 426 ? -48.110 28.740  14.387  1.00 38.18 ? 426 THR A CB    1 
ATOM   9370  O OG1   . THR C  1 426 ? -47.859 28.581  12.986  1.00 36.36 ? 426 THR A OG1   1 
ATOM   9371  C CG2   . THR C  1 426 ? -49.601 28.737  14.669  1.00 40.63 ? 426 THR A CG2   1 
ATOM   9372  N N     . ALA C  1 427 ? -47.696 29.634  17.254  1.00 38.72 ? 427 ALA A N     1 
ATOM   9373  C CA    . ALA C  1 427 ? -48.178 29.931  18.599  1.00 40.54 ? 427 ALA A CA    1 
ATOM   9374  C C     . ALA C  1 427 ? -47.656 31.279  19.066  1.00 37.44 ? 427 ALA A C     1 
ATOM   9375  O O     . ALA C  1 427 ? -48.350 32.022  19.772  1.00 34.22 ? 427 ALA A O     1 
ATOM   9376  C CB    . ALA C  1 427 ? -47.754 28.822  19.573  1.00 32.77 ? 427 ALA A CB    1 
ATOM   9377  N N     . MET C  1 428 ? -46.421 31.601  18.691  1.00 34.32 ? 428 MET A N     1 
ATOM   9378  C CA    . MET C  1 428 ? -45.854 32.889  19.061  1.00 33.04 ? 428 MET A CA    1 
ATOM   9379  C C     . MET C  1 428 ? -46.679 34.014  18.457  1.00 38.34 ? 428 MET A C     1 
ATOM   9380  O O     . MET C  1 428 ? -47.106 34.944  19.161  1.00 31.49 ? 428 MET A O     1 
ATOM   9381  C CB    . MET C  1 428 ? -44.410 32.946  18.579  1.00 35.50 ? 428 MET A CB    1 
ATOM   9382  C CG    . MET C  1 428 ? -43.405 32.582  19.635  1.00 40.43 ? 428 MET A CG    1 
ATOM   9383  S SD    . MET C  1 428 ? -41.720 32.762  19.041  1.00 42.99 ? 428 MET A SD    1 
ATOM   9384  C CE    . MET C  1 428 ? -41.900 32.201  17.377  1.00 33.28 ? 428 MET A CE    1 
ATOM   9385  N N     . LYS C  1 429 ? -46.941 33.911  17.148  1.00 33.48 ? 429 LYS A N     1 
ATOM   9386  C CA    . LYS C  1 429 ? -47.706 34.927  16.452  1.00 36.42 ? 429 LYS A CA    1 
ATOM   9387  C C     . LYS C  1 429 ? -48.943 35.297  17.255  1.00 38.23 ? 429 LYS A C     1 
ATOM   9388  O O     . LYS C  1 429 ? -49.099 36.443  17.684  1.00 39.47 ? 429 LYS A O     1 
ATOM   9389  C CB    . LYS C  1 429 ? -48.066 34.442  15.042  1.00 38.62 ? 429 LYS A CB    1 
ATOM   9390  C CG    . LYS C  1 429 ? -47.306 35.177  13.924  1.00 40.56 ? 429 LYS A CG    1 
ATOM   9391  C CD    . LYS C  1 429 ? -47.410 34.501  12.536  1.00 39.93 ? 429 LYS A CD    1 
ATOM   9392  C CE    . LYS C  1 429 ? -48.817 34.612  11.876  1.00 42.12 ? 429 LYS A CE    1 
ATOM   9393  N NZ    . LYS C  1 429 ? -48.977 35.760  10.925  1.00 46.17 ? 429 LYS A NZ    1 
ATOM   9394  N N     . ASP C  1 430 ? -49.800 34.328  17.547  1.00 39.86 ? 430 ASP A N     1 
ATOM   9395  C CA    . ASP C  1 430 ? -51.040 34.766  18.178  1.00 43.46 ? 430 ASP A CA    1 
ATOM   9396  C C     . ASP C  1 430 ? -50.902 35.070  19.662  1.00 37.48 ? 430 ASP A C     1 
ATOM   9397  O O     . ASP C  1 430 ? -51.784 35.738  20.204  1.00 39.02 ? 430 ASP A O     1 
ATOM   9398  C CB    . ASP C  1 430 ? -52.185 33.768  17.952  1.00 43.77 ? 430 ASP A CB    1 
ATOM   9399  C CG    . ASP C  1 430 ? -51.755 32.344  18.036  1.00 45.55 ? 430 ASP A CG    1 
ATOM   9400  O OD1   . ASP C  1 430 ? -50.550 32.101  18.280  1.00 47.70 ? 430 ASP A OD1   1 
ATOM   9401  O OD2   . ASP C  1 430 ? -52.635 31.468  17.842  1.00 45.73 ? 430 ASP A OD2   1 
ATOM   9402  N N     . GLU C  1 431 ? -49.824 34.663  20.334  1.00 36.41 ? 431 GLU A N     1 
ATOM   9403  C CA    . GLU C  1 431 ? -49.608 35.273  21.640  1.00 39.96 ? 431 GLU A CA    1 
ATOM   9404  C C     . GLU C  1 431 ? -49.356 36.762  21.488  1.00 39.30 ? 431 GLU A C     1 
ATOM   9405  O O     . GLU C  1 431 ? -49.635 37.527  22.413  1.00 40.79 ? 431 GLU A O     1 
ATOM   9406  C CB    . GLU C  1 431 ? -48.459 34.604  22.402  1.00 37.32 ? 431 GLU A CB    1 
ATOM   9407  C CG    . GLU C  1 431 ? -48.858 33.345  23.205  1.00 39.84 ? 431 GLU A CG    1 
ATOM   9408  C CD    . GLU C  1 431 ? -50.085 33.539  24.102  1.00 49.34 ? 431 GLU A CD    1 
ATOM   9409  O OE1   . GLU C  1 431 ? -50.274 34.649  24.664  1.00 40.89 ? 431 GLU A OE1   1 
ATOM   9410  O OE2   . GLU C  1 431 ? -50.863 32.563  24.247  1.00 51.41 ? 431 GLU A OE2   1 
ATOM   9411  N N     . ILE C  1 432 ? -48.865 37.185  20.325  1.00 32.68 ? 432 ILE A N     1 
ATOM   9412  C CA    . ILE C  1 432 ? -48.779 38.607  20.029  1.00 36.20 ? 432 ILE A CA    1 
ATOM   9413  C C     . ILE C  1 432 ? -50.174 39.166  19.785  1.00 36.78 ? 432 ILE A C     1 
ATOM   9414  O O     . ILE C  1 432 ? -50.554 40.217  20.311  1.00 31.57 ? 432 ILE A O     1 
ATOM   9415  C CB    . ILE C  1 432 ? -47.855 38.831  18.816  1.00 33.88 ? 432 ILE A CB    1 
ATOM   9416  C CG1   . ILE C  1 432 ? -46.507 38.141  19.041  1.00 36.48 ? 432 ILE A CG1   1 
ATOM   9417  C CG2   . ILE C  1 432 ? -47.696 40.301  18.527  1.00 34.60 ? 432 ILE A CG2   1 
ATOM   9418  C CD1   . ILE C  1 432 ? -45.760 37.816  17.761  1.00 38.30 ? 432 ILE A CD1   1 
ATOM   9419  N N     . ALA C  1 433 ? -50.959 38.470  18.969  1.00 40.01 ? 433 ALA A N     1 
ATOM   9420  C CA    . ALA C  1 433 ? -52.360 38.837  18.822  1.00 40.84 ? 433 ALA A CA    1 
ATOM   9421  C C     . ALA C  1 433 ? -53.048 38.869  20.176  1.00 44.51 ? 433 ALA A C     1 
ATOM   9422  O O     . ALA C  1 433 ? -53.819 39.789  20.477  1.00 43.21 ? 433 ALA A O     1 
ATOM   9423  C CB    . ALA C  1 433 ? -53.065 37.847  17.900  1.00 36.53 ? 433 ALA A CB    1 
ATOM   9424  N N     . THR C  1 434 ? -52.775 37.867  21.011  1.00 44.00 ? 434 THR A N     1 
ATOM   9425  C CA    . THR C  1 434 ? -53.377 37.839  22.331  1.00 39.80 ? 434 THR A CA    1 
ATOM   9426  C C     . THR C  1 434 ? -52.957 39.058  23.117  1.00 41.38 ? 434 THR A C     1 
ATOM   9427  O O     . THR C  1 434 ? -53.788 39.728  23.732  1.00 48.41 ? 434 THR A O     1 
ATOM   9428  C CB    . THR C  1 434 ? -52.973 36.562  23.065  1.00 45.80 ? 434 THR A CB    1 
ATOM   9429  O OG1   . THR C  1 434 ? -53.710 35.456  22.523  1.00 53.24 ? 434 THR A OG1   1 
ATOM   9430  C CG2   . THR C  1 434 ? -53.198 36.674  24.588  1.00 39.97 ? 434 THR A CG2   1 
ATOM   9431  N N     . THR C  1 435 ? -51.684 39.395  23.061  1.00 37.84 ? 435 THR A N     1 
ATOM   9432  C CA    . THR C  1 435 ? -51.128 40.330  24.016  1.00 37.93 ? 435 THR A CA    1 
ATOM   9433  C C     . THR C  1 435 ? -50.917 41.718  23.426  1.00 41.75 ? 435 THR A C     1 
ATOM   9434  O O     . THR C  1 435 ? -51.126 42.722  24.112  1.00 44.68 ? 435 THR A O     1 
ATOM   9435  C CB    . THR C  1 435 ? -49.820 39.745  24.547  1.00 39.68 ? 435 THR A CB    1 
ATOM   9436  O OG1   . THR C  1 435 ? -50.108 38.578  25.344  1.00 36.19 ? 435 THR A OG1   1 
ATOM   9437  C CG2   . THR C  1 435 ? -49.066 40.751  25.338  1.00 39.23 ? 435 THR A CG2   1 
ATOM   9438  N N     . ALA C  1 436 ? -50.517 41.812  22.165  1.00 42.25 ? 436 ALA A N     1 
ATOM   9439  C CA    . ALA C  1 436 ? -50.402 43.118  21.536  1.00 42.72 ? 436 ALA A CA    1 
ATOM   9440  C C     . ALA C  1 436 ? -51.703 43.539  20.883  1.00 41.49 ? 436 ALA A C     1 
ATOM   9441  O O     . ALA C  1 436 ? -51.974 44.739  20.758  1.00 40.86 ? 436 ALA A O     1 
ATOM   9442  C CB    . ALA C  1 436 ? -49.277 43.116  20.497  1.00 37.89 ? 436 ALA A CB    1 
ATOM   9443  N N     . GLY C  1 437 ? -52.520 42.574  20.485  1.00 44.06 ? 437 GLY A N     1 
ATOM   9444  C CA    . GLY C  1 437 ? -53.781 42.883  19.849  1.00 45.18 ? 437 GLY A CA    1 
ATOM   9445  C C     . GLY C  1 437 ? -53.570 43.415  18.454  1.00 42.65 ? 437 GLY A C     1 
ATOM   9446  O O     . GLY C  1 437 ? -52.712 44.276  18.244  1.00 40.23 ? 437 GLY A O     1 
ATOM   9447  N N     . THR C  1 438 ? -54.342 42.912  17.499  1.00 43.95 ? 438 THR A N     1 
ATOM   9448  C CA    . THR C  1 438 ? -54.187 43.255  16.096  1.00 38.63 ? 438 THR A CA    1 
ATOM   9449  C C     . THR C  1 438 ? -55.251 44.265  15.669  1.00 45.50 ? 438 THR A C     1 
ATOM   9450  O O     . THR C  1 438 ? -56.194 44.563  16.404  1.00 43.73 ? 438 THR A O     1 
ATOM   9451  C CB    . THR C  1 438 ? -54.260 41.989  15.242  1.00 43.96 ? 438 THR A CB    1 
ATOM   9452  O OG1   . THR C  1 438 ? -55.587 41.839  14.721  1.00 46.18 ? 438 THR A OG1   1 
ATOM   9453  C CG2   . THR C  1 438 ? -53.921 40.784  16.082  1.00 39.03 ? 438 THR A CG2   1 
ATOM   9454  N N     . LEU C  1 439 ? -55.061 44.822  14.467  1.00 51.37 ? 439 LEU A N     1 
ATOM   9455  C CA    . LEU C  1 439 ? -55.982 45.794  13.882  1.00 49.10 ? 439 LEU A CA    1 
ATOM   9456  C C     . LEU C  1 439 ? -56.781 45.168  12.746  1.00 54.37 ? 439 LEU A C     1 
ATOM   9457  O O     . LEU C  1 439 ? -56.721 45.652  11.604  1.00 55.88 ? 439 LEU A O     1 
ATOM   9458  C CB    . LEU C  1 439 ? -55.252 47.018  13.355  1.00 40.95 ? 439 LEU A CB    1 
ATOM   9459  C CG    . LEU C  1 439 ? -55.128 48.172  14.339  1.00 42.05 ? 439 LEU A CG    1 
ATOM   9460  C CD1   . LEU C  1 439 ? -54.326 49.168  13.595  1.00 43.14 ? 439 LEU A CD1   1 
ATOM   9461  C CD2   . LEU C  1 439 ? -56.500 48.714  14.711  1.00 36.33 ? 439 LEU A CD2   1 
ATOM   9462  N N     . SER C  1 440 ? -57.526 44.101  13.040  1.00 53.60 ? 440 SER A N     1 
ATOM   9463  C CA    . SER C  1 440 ? -58.297 43.414  11.990  1.00 59.84 ? 440 SER A CA    1 
ATOM   9464  C C     . SER C  1 440 ? -59.563 44.182  11.691  1.00 67.96 ? 440 SER A C     1 
ATOM   9465  O O     . SER C  1 440 ? -59.723 45.353  12.102  1.00 65.34 ? 440 SER A O     1 
ATOM   9466  C CB    . SER C  1 440 ? -58.609 41.984  12.405  1.00 66.87 ? 440 SER A CB    1 
ATOM   9467  O OG    . SER C  1 440 ? -57.513 41.154  11.971  1.00 65.27 ? 440 SER A OG    1 
ATOM   9468  N N     . SER D  1 30  ? -52.689 56.962  -57.147 1.00 52.17 ? 30  SER B N     1 
ATOM   9469  C CA    . SER D  1 30  ? -52.267 56.396  -58.422 1.00 49.75 ? 30  SER B CA    1 
ATOM   9470  C C     . SER D  1 30  ? -50.862 55.862  -58.252 1.00 49.92 ? 30  SER B C     1 
ATOM   9471  O O     . SER D  1 30  ? -50.069 55.807  -59.187 1.00 53.19 ? 30  SER B O     1 
ATOM   9472  C CB    . SER D  1 30  ? -52.315 57.448  -59.522 1.00 47.28 ? 30  SER B CB    1 
ATOM   9473  O OG    . SER D  1 30  ? -51.820 58.684  -59.042 1.00 48.13 ? 30  SER B OG    1 
ATOM   9474  N N     . THR D  1 31  ? -50.564 55.467  -57.028 1.00 51.49 ? 31  THR B N     1 
ATOM   9475  C CA    . THR D  1 31  ? -49.209 55.146  -56.623 1.00 49.93 ? 31  THR B CA    1 
ATOM   9476  C C     . THR D  1 31  ? -49.005 53.636  -56.613 1.00 51.13 ? 31  THR B C     1 
ATOM   9477  O O     . THR D  1 31  ? -49.941 52.866  -56.373 1.00 49.78 ? 31  THR B O     1 
ATOM   9478  C CB    . THR D  1 31  ? -48.936 55.751  -55.246 1.00 46.02 ? 31  THR B CB    1 
ATOM   9479  O OG1   . THR D  1 31  ? -48.083 56.890  -55.405 1.00 43.94 ? 31  THR B OG1   1 
ATOM   9480  C CG2   . THR D  1 31  ? -48.290 54.746  -54.290 1.00 43.96 ? 31  THR B CG2   1 
ATOM   9481  N N     . ASP D  1 32  ? -47.771 53.216  -56.909 1.00 44.84 ? 32  ASP B N     1 
ATOM   9482  C CA    . ASP D  1 32  ? -47.423 51.801  -56.873 1.00 45.74 ? 32  ASP B CA    1 
ATOM   9483  C C     . ASP D  1 32  ? -46.213 51.537  -55.983 1.00 44.15 ? 32  ASP B C     1 
ATOM   9484  O O     . ASP D  1 32  ? -45.401 50.648  -56.273 1.00 41.96 ? 32  ASP B O     1 
ATOM   9485  C CB    . ASP D  1 32  ? -47.176 51.255  -58.278 1.00 43.32 ? 32  ASP B CB    1 
ATOM   9486  C CG    . ASP D  1 32  ? -45.881 51.738  -58.868 1.00 46.70 ? 32  ASP B CG    1 
ATOM   9487  O OD1   . ASP D  1 32  ? -45.335 52.743  -58.362 1.00 47.08 ? 32  ASP B OD1   1 
ATOM   9488  O OD2   . ASP D  1 32  ? -45.403 51.099  -59.834 1.00 52.38 ? 32  ASP B OD2   1 
ATOM   9489  N N     . THR D  1 33  ? -46.061 52.301  -54.906 1.00 45.80 ? 33  THR B N     1 
ATOM   9490  C CA    . THR D  1 33  ? -45.181 51.843  -53.853 1.00 38.48 ? 33  THR B CA    1 
ATOM   9491  C C     . THR D  1 33  ? -45.692 50.484  -53.388 1.00 36.73 ? 33  THR B C     1 
ATOM   9492  O O     . THR D  1 33  ? -46.815 50.089  -53.693 1.00 49.32 ? 33  THR B O     1 
ATOM   9493  C CB    . THR D  1 33  ? -45.137 52.863  -52.723 1.00 38.39 ? 33  THR B CB    1 
ATOM   9494  O OG1   . THR D  1 33  ? -45.267 54.179  -53.275 1.00 36.62 ? 33  THR B OG1   1 
ATOM   9495  C CG2   . THR D  1 33  ? -43.828 52.776  -51.985 1.00 35.72 ? 33  THR B CG2   1 
ATOM   9496  N N     . THR D  1 34  ? -44.847 49.733  -52.699 1.00 33.91 ? 34  THR B N     1 
ATOM   9497  C CA    . THR D  1 34  ? -45.207 48.376  -52.275 1.00 45.51 ? 34  THR B CA    1 
ATOM   9498  C C     . THR D  1 34  ? -45.387 47.414  -53.461 1.00 46.34 ? 34  THR B C     1 
ATOM   9499  O O     . THR D  1 34  ? -45.554 46.206  -53.250 1.00 44.01 ? 34  THR B O     1 
ATOM   9500  C CB    . THR D  1 34  ? -46.482 48.326  -51.379 1.00 37.42 ? 34  THR B CB    1 
ATOM   9501  O OG1   . THR D  1 34  ? -47.673 48.375  -52.168 1.00 41.14 ? 34  THR B OG1   1 
ATOM   9502  C CG2   . THR D  1 34  ? -46.531 49.457  -50.359 1.00 41.23 ? 34  THR B CG2   1 
ATOM   9503  N N     . ALA D  1 35  ? -45.338 47.900  -54.708 1.00 42.49 ? 35  ALA B N     1 
ATOM   9504  C CA    . ALA D  1 35  ? -45.214 46.960  -55.817 1.00 39.63 ? 35  ALA B CA    1 
ATOM   9505  C C     . ALA D  1 35  ? -43.825 46.338  -55.852 1.00 40.34 ? 35  ALA B C     1 
ATOM   9506  O O     . ALA D  1 35  ? -43.643 45.224  -56.358 1.00 36.49 ? 35  ALA B O     1 
ATOM   9507  C CB    . ALA D  1 35  ? -45.517 47.631  -57.150 1.00 39.45 ? 35  ALA B CB    1 
ATOM   9508  N N     . ARG D  1 36  ? -42.841 47.039  -55.306 1.00 38.68 ? 36  ARG B N     1 
ATOM   9509  C CA    . ARG D  1 36  ? -41.507 46.480  -55.199 1.00 36.80 ? 36  ARG B CA    1 
ATOM   9510  C C     . ARG D  1 36  ? -41.523 45.075  -54.614 1.00 39.01 ? 36  ARG B C     1 
ATOM   9511  O O     . ARG D  1 36  ? -40.674 44.250  -54.962 1.00 38.83 ? 36  ARG B O     1 
ATOM   9512  C CB    . ARG D  1 36  ? -40.651 47.402  -54.338 1.00 38.89 ? 36  ARG B CB    1 
ATOM   9513  C CG    . ARG D  1 36  ? -41.285 47.695  -52.984 1.00 37.58 ? 36  ARG B CG    1 
ATOM   9514  C CD    . ARG D  1 36  ? -40.995 49.127  -52.537 1.00 40.58 ? 36  ARG B CD    1 
ATOM   9515  N NE    . ARG D  1 36  ? -39.593 49.491  -52.725 1.00 33.48 ? 36  ARG B NE    1 
ATOM   9516  C CZ    . ARG D  1 36  ? -38.622 49.147  -51.890 1.00 34.87 ? 36  ARG B CZ    1 
ATOM   9517  N NH1   . ARG D  1 36  ? -38.869 48.457  -50.787 1.00 36.02 ? 36  ARG B NH1   1 
ATOM   9518  N NH2   . ARG D  1 36  ? -37.372 49.493  -52.172 1.00 37.88 ? 36  ARG B NH2   1 
ATOM   9519  N N     . PHE D  1 37  ? -42.474 44.767  -53.738 1.00 37.20 ? 37  PHE B N     1 
ATOM   9520  C CA    . PHE D  1 37  ? -42.383 43.491  -53.043 1.00 37.09 ? 37  PHE B CA    1 
ATOM   9521  C C     . PHE D  1 37  ? -42.828 42.310  -53.891 1.00 37.69 ? 37  PHE B C     1 
ATOM   9522  O O     . PHE D  1 37  ? -42.652 41.162  -53.463 1.00 36.49 ? 37  PHE B O     1 
ATOM   9523  C CB    . PHE D  1 37  ? -43.159 43.553  -51.733 1.00 35.63 ? 37  PHE B CB    1 
ATOM   9524  C CG    . PHE D  1 37  ? -42.763 44.708  -50.881 1.00 33.26 ? 37  PHE B CG    1 
ATOM   9525  C CD1   . PHE D  1 37  ? -41.578 44.684  -50.178 1.00 32.00 ? 37  PHE B CD1   1 
ATOM   9526  C CD2   . PHE D  1 37  ? -43.546 45.841  -50.827 1.00 32.92 ? 37  PHE B CD2   1 
ATOM   9527  C CE1   . PHE D  1 37  ? -41.199 45.757  -49.409 1.00 28.63 ? 37  PHE B CE1   1 
ATOM   9528  C CE2   . PHE D  1 37  ? -43.173 46.912  -50.054 1.00 33.52 ? 37  PHE B CE2   1 
ATOM   9529  C CZ    . PHE D  1 37  ? -41.995 46.871  -49.350 1.00 31.45 ? 37  PHE B CZ    1 
ATOM   9530  N N     . LEU D  1 38  ? -43.330 42.545  -55.102 1.00 37.00 ? 38  LEU B N     1 
ATOM   9531  C CA    . LEU D  1 38  ? -43.547 41.426  -56.007 1.00 36.73 ? 38  LEU B CA    1 
ATOM   9532  C C     . LEU D  1 38  ? -42.269 40.617  -56.204 1.00 36.12 ? 38  LEU B C     1 
ATOM   9533  O O     . LEU D  1 38  ? -42.338 39.416  -56.495 1.00 35.80 ? 38  LEU B O     1 
ATOM   9534  C CB    . LEU D  1 38  ? -44.085 41.935  -57.357 1.00 44.31 ? 38  LEU B CB    1 
ATOM   9535  C CG    . LEU D  1 38  ? -45.180 41.186  -58.149 1.00 36.55 ? 38  LEU B CG    1 
ATOM   9536  C CD1   . LEU D  1 38  ? -44.606 40.035  -58.933 1.00 36.64 ? 38  LEU B CD1   1 
ATOM   9537  C CD2   . LEU D  1 38  ? -46.299 40.670  -57.276 1.00 33.20 ? 38  LEU B CD2   1 
ATOM   9538  N N     . TRP D  1 39  ? -41.100 41.229  -56.008 1.00 38.17 ? 39  TRP B N     1 
ATOM   9539  C CA    . TRP D  1 39  ? -39.858 40.494  -56.232 1.00 38.55 ? 39  TRP B CA    1 
ATOM   9540  C C     . TRP D  1 39  ? -39.629 39.401  -55.206 1.00 36.10 ? 39  TRP B C     1 
ATOM   9541  O O     . TRP D  1 39  ? -38.632 38.670  -55.313 1.00 32.83 ? 39  TRP B O     1 
ATOM   9542  C CB    . TRP D  1 39  ? -38.682 41.468  -56.261 1.00 34.92 ? 39  TRP B CB    1 
ATOM   9543  C CG    . TRP D  1 39  ? -38.780 42.431  -57.419 1.00 40.80 ? 39  TRP B CG    1 
ATOM   9544  C CD1   . TRP D  1 39  ? -39.411 43.640  -57.432 1.00 41.28 ? 39  TRP B CD1   1 
ATOM   9545  C CD2   . TRP D  1 39  ? -38.268 42.238  -58.738 1.00 36.58 ? 39  TRP B CD2   1 
ATOM   9546  N NE1   . TRP D  1 39  ? -39.299 44.227  -58.664 1.00 36.15 ? 39  TRP B NE1   1 
ATOM   9547  C CE2   . TRP D  1 39  ? -38.604 43.383  -59.489 1.00 37.83 ? 39  TRP B CE2   1 
ATOM   9548  C CE3   . TRP D  1 39  ? -37.535 41.222  -59.352 1.00 41.28 ? 39  TRP B CE3   1 
ATOM   9549  C CZ2   . TRP D  1 39  ? -38.237 43.537  -60.830 1.00 39.41 ? 39  TRP B CZ2   1 
ATOM   9550  C CZ3   . TRP D  1 39  ? -37.168 41.377  -60.694 1.00 43.32 ? 39  TRP B CZ3   1 
ATOM   9551  C CH2   . TRP D  1 39  ? -37.519 42.528  -61.412 1.00 35.94 ? 39  TRP B CH2   1 
ATOM   9552  N N     . HIS D  1 40  ? -40.530 39.271  -54.231 1.00 34.03 ? 40  HIS B N     1 
ATOM   9553  C CA    . HIS D  1 40  ? -40.475 38.209  -53.241 1.00 31.40 ? 40  HIS B CA    1 
ATOM   9554  C C     . HIS D  1 40  ? -41.171 36.947  -53.707 1.00 32.57 ? 40  HIS B C     1 
ATOM   9555  O O     . HIS D  1 40  ? -40.940 35.869  -53.144 1.00 33.27 ? 40  HIS B O     1 
ATOM   9556  C CB    . HIS D  1 40  ? -41.126 38.683  -51.948 1.00 32.61 ? 40  HIS B CB    1 
ATOM   9557  C CG    . HIS D  1 40  ? -40.162 39.256  -50.973 1.00 37.49 ? 40  HIS B CG    1 
ATOM   9558  N ND1   . HIS D  1 40  ? -39.114 38.524  -50.450 1.00 38.91 ? 40  HIS B ND1   1 
ATOM   9559  C CD2   . HIS D  1 40  ? -40.087 40.487  -50.416 1.00 33.31 ? 40  HIS B CD2   1 
ATOM   9560  C CE1   . HIS D  1 40  ? -38.432 39.284  -49.613 1.00 36.75 ? 40  HIS B CE1   1 
ATOM   9561  N NE2   . HIS D  1 40  ? -39.001 40.478  -49.575 1.00 36.47 ? 40  HIS B NE2   1 
ATOM   9562  N N     . ALA D  1 41  ? -41.997 37.068  -54.735 1.00 30.62 ? 41  ALA B N     1 
ATOM   9563  C CA    . ALA D  1 41  ? -42.948 36.038  -55.095 1.00 33.72 ? 41  ALA B CA    1 
ATOM   9564  C C     . ALA D  1 41  ? -42.259 34.749  -55.515 1.00 35.49 ? 41  ALA B C     1 
ATOM   9565  O O     . ALA D  1 41  ? -41.081 34.717  -55.872 1.00 36.39 ? 41  ALA B O     1 
ATOM   9566  C CB    . ALA D  1 41  ? -43.852 36.521  -56.233 1.00 34.73 ? 41  ALA B CB    1 
ATOM   9567  N N     . GLU D  1 42  ? -43.034 33.673  -55.442 1.00 38.09 ? 42  GLU B N     1 
ATOM   9568  C CA    . GLU D  1 42  ? -42.719 32.380  -56.013 1.00 40.48 ? 42  GLU B CA    1 
ATOM   9569  C C     . GLU D  1 42  ? -44.013 31.836  -56.610 1.00 47.35 ? 42  GLU B C     1 
ATOM   9570  O O     . GLU D  1 42  ? -45.048 32.513  -56.607 1.00 46.52 ? 42  GLU B O     1 
ATOM   9571  C CB    . GLU D  1 42  ? -42.130 31.440  -54.958 1.00 40.17 ? 42  GLU B CB    1 
ATOM   9572  C CG    . GLU D  1 42  ? -41.041 32.066  -54.076 1.00 46.02 ? 42  GLU B CG    1 
ATOM   9573  C CD    . GLU D  1 42  ? -39.636 31.991  -54.686 1.00 51.52 ? 42  GLU B CD    1 
ATOM   9574  O OE1   . GLU D  1 42  ? -39.499 31.597  -55.881 1.00 46.61 ? 42  GLU B OE1   1 
ATOM   9575  O OE2   . GLU D  1 42  ? -38.671 32.337  -53.957 1.00 41.60 ? 42  GLU B OE2   1 
ATOM   9576  N N     . ASP D  1 43  ? -43.960 30.605  -57.120 1.00 49.86 ? 43  ASP B N     1 
ATOM   9577  C CA    . ASP D  1 43  ? -45.125 29.996  -57.761 1.00 48.10 ? 43  ASP B CA    1 
ATOM   9578  C C     . ASP D  1 43  ? -46.307 29.897  -56.800 1.00 45.32 ? 43  ASP B C     1 
ATOM   9579  O O     . ASP D  1 43  ? -46.204 29.286  -55.730 1.00 41.78 ? 43  ASP B O     1 
ATOM   9580  C CB    . ASP D  1 43  ? -44.760 28.610  -58.293 1.00 42.55 ? 43  ASP B CB    1 
ATOM   9581  C CG    . ASP D  1 43  ? -43.944 28.678  -59.563 1.00 45.54 ? 43  ASP B CG    1 
ATOM   9582  O OD1   . ASP D  1 43  ? -44.165 29.626  -60.345 1.00 45.18 ? 43  ASP B OD1   1 
ATOM   9583  O OD2   . ASP D  1 43  ? -43.090 27.788  -59.785 1.00 43.85 ? 43  ASP B OD2   1 
ATOM   9584  N N     . GLY D  1 44  ? -47.433 30.488  -57.188 1.00 44.48 ? 44  GLY B N     1 
ATOM   9585  C CA    . GLY D  1 44  ? -48.649 30.378  -56.413 1.00 48.28 ? 44  GLY B CA    1 
ATOM   9586  C C     . GLY D  1 44  ? -48.796 31.372  -55.279 1.00 52.39 ? 44  GLY B C     1 
ATOM   9587  O O     . GLY D  1 44  ? -49.836 31.360  -54.599 1.00 50.05 ? 44  GLY B O     1 
ATOM   9588  N N     . ASP D  1 45  ? -47.805 32.238  -55.058 1.00 47.72 ? 45  ASP B N     1 
ATOM   9589  C CA    . ASP D  1 45  ? -47.854 33.203  -53.969 1.00 43.14 ? 45  ASP B CA    1 
ATOM   9590  C C     . ASP D  1 45  ? -48.946 34.250  -54.210 1.00 42.02 ? 45  ASP B C     1 
ATOM   9591  O O     . ASP D  1 45  ? -49.524 34.367  -55.297 1.00 43.62 ? 45  ASP B O     1 
ATOM   9592  C CB    . ASP D  1 45  ? -46.497 33.897  -53.805 1.00 38.66 ? 45  ASP B CB    1 
ATOM   9593  C CG    . ASP D  1 45  ? -45.494 33.064  -53.008 1.00 38.88 ? 45  ASP B CG    1 
ATOM   9594  O OD1   . ASP D  1 45  ? -45.897 32.128  -52.280 1.00 43.00 ? 45  ASP B OD1   1 
ATOM   9595  O OD2   . ASP D  1 45  ? -44.288 33.355  -53.111 1.00 34.01 ? 45  ASP B OD2   1 
ATOM   9596  N N     . VAL D  1 46  ? -49.225 35.021  -53.162 1.00 41.00 ? 46  VAL B N     1 
ATOM   9597  C CA    . VAL D  1 46  ? -50.150 36.142  -53.219 1.00 40.35 ? 46  VAL B CA    1 
ATOM   9598  C C     . VAL D  1 46  ? -49.449 37.387  -52.698 1.00 42.59 ? 46  VAL B C     1 
ATOM   9599  O O     . VAL D  1 46  ? -48.716 37.329  -51.702 1.00 42.18 ? 46  VAL B O     1 
ATOM   9600  C CB    . VAL D  1 46  ? -51.426 35.884  -52.396 1.00 42.95 ? 46  VAL B CB    1 
ATOM   9601  C CG1   . VAL D  1 46  ? -52.590 36.742  -52.926 1.00 43.11 ? 46  VAL B CG1   1 
ATOM   9602  C CG2   . VAL D  1 46  ? -51.772 34.416  -52.397 1.00 41.60 ? 46  VAL B CG2   1 
ATOM   9603  N N     . LEU D  1 47  ? -49.691 38.517  -53.362 1.00 39.49 ? 47  LEU B N     1 
ATOM   9604  C CA    . LEU D  1 47  ? -49.264 39.823  -52.881 1.00 40.12 ? 47  LEU B CA    1 
ATOM   9605  C C     . LEU D  1 47  ? -50.489 40.671  -52.566 1.00 42.17 ? 47  LEU B C     1 
ATOM   9606  O O     . LEU D  1 47  ? -51.439 40.720  -53.357 1.00 41.12 ? 47  LEU B O     1 
ATOM   9607  C CB    . LEU D  1 47  ? -48.373 40.540  -53.898 1.00 34.08 ? 47  LEU B CB    1 
ATOM   9608  C CG    . LEU D  1 47  ? -48.130 42.016  -53.585 1.00 33.07 ? 47  LEU B CG    1 
ATOM   9609  C CD1   . LEU D  1 47  ? -47.472 42.185  -52.226 1.00 36.23 ? 47  LEU B CD1   1 
ATOM   9610  C CD2   . LEU D  1 47  ? -47.290 42.665  -54.645 1.00 30.50 ? 47  LEU B CD2   1 
ATOM   9611  N N     . VAL D  1 48  ? -50.472 41.322  -51.405 1.00 40.87 ? 48  VAL B N     1 
ATOM   9612  C CA    . VAL D  1 48  ? -51.474 42.314  -51.042 1.00 41.65 ? 48  VAL B CA    1 
ATOM   9613  C C     . VAL D  1 48  ? -50.833 43.688  -51.138 1.00 46.46 ? 48  VAL B C     1 
ATOM   9614  O O     . VAL D  1 48  ? -49.693 43.881  -50.687 1.00 48.04 ? 48  VAL B O     1 
ATOM   9615  C CB    . VAL D  1 48  ? -52.030 42.068  -49.632 1.00 45.12 ? 48  VAL B CB    1 
ATOM   9616  C CG1   . VAL D  1 48  ? -53.122 43.092  -49.311 1.00 45.88 ? 48  VAL B CG1   1 
ATOM   9617  C CG2   . VAL D  1 48  ? -52.566 40.657  -49.530 1.00 44.49 ? 48  VAL B CG2   1 
ATOM   9618  N N     . ILE D  1 49  ? -51.553 44.630  -51.745 1.00 37.20 ? 49  ILE B N     1 
ATOM   9619  C CA    . ILE D  1 49  ? -51.062 45.994  -51.908 1.00 41.41 ? 49  ILE B CA    1 
ATOM   9620  C C     . ILE D  1 49  ? -52.173 46.976  -51.584 1.00 43.47 ? 49  ILE B C     1 
ATOM   9621  O O     . ILE D  1 49  ? -53.319 46.796  -52.017 1.00 49.00 ? 49  ILE B O     1 
ATOM   9622  C CB    . ILE D  1 49  ? -50.535 46.261  -53.328 1.00 49.67 ? 49  ILE B CB    1 
ATOM   9623  C CG1   . ILE D  1 49  ? -51.678 46.286  -54.361 1.00 48.30 ? 49  ILE B CG1   1 
ATOM   9624  C CG2   . ILE D  1 49  ? -49.484 45.249  -53.694 1.00 47.11 ? 49  ILE B CG2   1 
ATOM   9625  C CD1   . ILE D  1 49  ? -51.321 46.956  -55.688 1.00 47.33 ? 49  ILE B CD1   1 
ATOM   9626  N N     . PRO D  1 50  ? -51.886 48.031  -50.831 1.00 45.42 ? 50  PRO B N     1 
ATOM   9627  C CA    . PRO D  1 50  ? -52.869 49.110  -50.707 1.00 47.46 ? 50  PRO B CA    1 
ATOM   9628  C C     . PRO D  1 50  ? -53.039 49.886  -51.994 1.00 53.07 ? 50  PRO B C     1 
ATOM   9629  O O     . PRO D  1 50  ? -54.010 50.648  -52.112 1.00 56.56 ? 50  PRO B O     1 
ATOM   9630  C CB    . PRO D  1 50  ? -52.281 49.987  -49.601 1.00 41.67 ? 50  PRO B CB    1 
ATOM   9631  C CG    . PRO D  1 50  ? -50.817 49.791  -49.744 1.00 46.58 ? 50  PRO B CG    1 
ATOM   9632  C CD    . PRO D  1 50  ? -50.617 48.351  -50.158 1.00 47.02 ? 50  PRO B CD    1 
ATOM   9633  N N     . ASP D  1 51  ? -52.163 49.670  -52.976 1.00 53.06 ? 51  ASP B N     1 
ATOM   9634  C CA    . ASP D  1 51  ? -51.881 50.599  -54.055 1.00 47.62 ? 51  ASP B CA    1 
ATOM   9635  C C     . ASP D  1 51  ? -52.509 50.149  -55.359 1.00 47.16 ? 51  ASP B C     1 
ATOM   9636  O O     . ASP D  1 51  ? -53.479 49.379  -55.368 1.00 48.57 ? 51  ASP B O     1 
ATOM   9637  C CB    . ASP D  1 51  ? -50.363 50.752  -54.209 1.00 49.89 ? 51  ASP B CB    1 
ATOM   9638  C CG    . ASP D  1 51  ? -49.732 51.493  -53.061 1.00 52.50 ? 51  ASP B CG    1 
ATOM   9639  O OD1   . ASP D  1 51  ? -50.457 51.779  -52.077 1.00 61.28 ? 51  ASP B OD1   1 
ATOM   9640  O OD2   . ASP D  1 51  ? -48.526 51.827  -53.158 1.00 46.84 ? 51  ASP B OD2   1 
ATOM   9641  N N     . THR D  1 52  ? -51.940 50.640  -56.456 1.00 47.03 ? 52  THR B N     1 
ATOM   9642  C CA    . THR D  1 52  ? -52.205 50.224  -57.820 1.00 47.73 ? 52  THR B CA    1 
ATOM   9643  C C     . THR D  1 52  ? -50.898 49.708  -58.419 1.00 52.48 ? 52  THR B C     1 
ATOM   9644  O O     . THR D  1 52  ? -49.808 50.061  -57.969 1.00 54.38 ? 52  THR B O     1 
ATOM   9645  C CB    . THR D  1 52  ? -52.748 51.397  -58.634 1.00 49.04 ? 52  THR B CB    1 
ATOM   9646  O OG1   . THR D  1 52  ? -51.650 52.193  -59.101 1.00 53.05 ? 52  THR B OG1   1 
ATOM   9647  C CG2   . THR D  1 52  ? -53.624 52.277  -57.752 1.00 52.26 ? 52  THR B CG2   1 
ATOM   9648  N N     . VAL D  1 53  ? -50.991 48.866  -59.439 1.00 41.08 ? 53  VAL B N     1 
ATOM   9649  C CA    . VAL D  1 53  ? -49.809 48.239  -60.009 1.00 38.99 ? 53  VAL B CA    1 
ATOM   9650  C C     . VAL D  1 53  ? -49.859 48.362  -61.525 1.00 44.53 ? 53  VAL B C     1 
ATOM   9651  O O     . VAL D  1 53  ? -50.880 48.034  -62.140 1.00 45.21 ? 53  VAL B O     1 
ATOM   9652  C CB    . VAL D  1 53  ? -49.705 46.768  -59.575 1.00 38.25 ? 53  VAL B CB    1 
ATOM   9653  C CG1   . VAL D  1 53  ? -49.122 45.921  -60.667 1.00 44.98 ? 53  VAL B CG1   1 
ATOM   9654  C CG2   . VAL D  1 53  ? -48.856 46.674  -58.331 1.00 46.95 ? 53  VAL B CG2   1 
ATOM   9655  N N     . ASP D  1 54  ? -48.766 48.847  -62.125 1.00 41.95 ? 54  ASP B N     1 
ATOM   9656  C CA    . ASP D  1 54  ? -48.701 48.986  -63.572 1.00 36.86 ? 54  ASP B CA    1 
ATOM   9657  C C     . ASP D  1 54  ? -49.110 47.668  -64.219 1.00 42.32 ? 54  ASP B C     1 
ATOM   9658  O O     . ASP D  1 54  ? -48.691 46.600  -63.750 1.00 42.38 ? 54  ASP B O     1 
ATOM   9659  C CB    . ASP D  1 54  ? -47.290 49.390  -64.013 1.00 42.95 ? 54  ASP B CB    1 
ATOM   9660  C CG    . ASP D  1 54  ? -47.228 49.889  -65.469 1.00 46.39 ? 54  ASP B CG    1 
ATOM   9661  O OD1   . ASP D  1 54  ? -47.276 49.037  -66.383 1.00 48.47 ? 54  ASP B OD1   1 
ATOM   9662  O OD2   . ASP D  1 54  ? -47.095 51.116  -65.710 1.00 41.46 ? 54  ASP B OD2   1 
ATOM   9663  N N     . PRO D  1 55  ? -49.955 47.693  -65.253 1.00 45.93 ? 55  PRO B N     1 
ATOM   9664  C CA    . PRO D  1 55  ? -50.562 46.439  -65.748 1.00 46.05 ? 55  PRO B CA    1 
ATOM   9665  C C     . PRO D  1 55  ? -49.568 45.390  -66.202 1.00 47.52 ? 55  PRO B C     1 
ATOM   9666  O O     . PRO D  1 55  ? -49.933 44.212  -66.306 1.00 47.10 ? 55  PRO B O     1 
ATOM   9667  C CB    . PRO D  1 55  ? -51.446 46.910  -66.917 1.00 48.61 ? 55  PRO B CB    1 
ATOM   9668  C CG    . PRO D  1 55  ? -51.026 48.342  -67.200 1.00 48.67 ? 55  PRO B CG    1 
ATOM   9669  C CD    . PRO D  1 55  ? -50.565 48.880  -65.873 1.00 44.82 ? 55  PRO B CD    1 
ATOM   9670  N N     . ASP D  1 56  ? -48.321 45.766  -66.462 1.00 44.33 ? 56  ASP B N     1 
ATOM   9671  C CA    . ASP D  1 56  ? -47.353 44.837  -67.016 1.00 43.53 ? 56  ASP B CA    1 
ATOM   9672  C C     . ASP D  1 56  ? -46.313 44.359  -66.003 1.00 44.79 ? 56  ASP B C     1 
ATOM   9673  O O     . ASP D  1 56  ? -45.668 43.332  -66.236 1.00 47.74 ? 56  ASP B O     1 
ATOM   9674  C CB    . ASP D  1 56  ? -46.669 45.498  -68.226 1.00 47.52 ? 56  ASP B CB    1 
ATOM   9675  C CG    . ASP D  1 56  ? -47.690 46.105  -69.237 1.00 52.43 ? 56  ASP B CG    1 
ATOM   9676  O OD1   . ASP D  1 56  ? -48.377 47.117  -68.916 1.00 53.12 ? 56  ASP B OD1   1 
ATOM   9677  O OD2   . ASP D  1 56  ? -47.807 45.561  -70.360 1.00 48.52 ? 56  ASP B OD2   1 
ATOM   9678  N N     . PHE D  1 57  ? -46.185 45.048  -64.867 1.00 43.90 ? 57  PHE B N     1 
ATOM   9679  C CA    . PHE D  1 57  ? -45.138 44.763  -63.886 1.00 40.02 ? 57  PHE B CA    1 
ATOM   9680  C C     . PHE D  1 57  ? -45.101 43.318  -63.391 1.00 37.61 ? 57  PHE B C     1 
ATOM   9681  O O     . PHE D  1 57  ? -43.993 42.788  -63.223 1.00 36.35 ? 57  PHE B O     1 
ATOM   9682  C CB    . PHE D  1 57  ? -45.325 45.763  -62.733 1.00 41.38 ? 57  PHE B CB    1 
ATOM   9683  C CG    . PHE D  1 57  ? -44.322 45.654  -61.622 1.00 40.93 ? 57  PHE B CG    1 
ATOM   9684  C CD1   . PHE D  1 57  ? -44.563 44.833  -60.534 1.00 40.69 ? 57  PHE B CD1   1 
ATOM   9685  C CD2   . PHE D  1 57  ? -43.183 46.438  -61.623 1.00 39.77 ? 57  PHE B CD2   1 
ATOM   9686  C CE1   . PHE D  1 57  ? -43.671 44.771  -59.496 1.00 35.99 ? 57  PHE B CE1   1 
ATOM   9687  C CE2   . PHE D  1 57  ? -42.286 46.376  -60.588 1.00 35.46 ? 57  PHE B CE2   1 
ATOM   9688  C CZ    . PHE D  1 57  ? -42.532 45.543  -59.526 1.00 37.97 ? 57  PHE B CZ    1 
ATOM   9689  N N     . PRO D  1 58  ? -46.222 42.647  -63.115 1.00 39.58 ? 58  PRO B N     1 
ATOM   9690  C CA    . PRO D  1 58  ? -46.135 41.239  -62.679 1.00 38.34 ? 58  PRO B CA    1 
ATOM   9691  C C     . PRO D  1 58  ? -45.554 40.322  -63.735 1.00 40.75 ? 58  PRO B C     1 
ATOM   9692  O O     . PRO D  1 58  ? -44.633 39.549  -63.450 1.00 40.47 ? 58  PRO B O     1 
ATOM   9693  C CB    . PRO D  1 58  ? -47.595 40.874  -62.387 1.00 40.65 ? 58  PRO B CB    1 
ATOM   9694  C CG    . PRO D  1 58  ? -48.271 42.174  -62.131 1.00 43.41 ? 58  PRO B CG    1 
ATOM   9695  C CD    . PRO D  1 58  ? -47.593 43.176  -63.001 1.00 43.08 ? 58  PRO B CD    1 
ATOM   9696  N N     . GLY D  1 59  ? -46.090 40.375  -64.951 1.00 37.61 ? 59  GLY B N     1 
ATOM   9697  C CA    . GLY D  1 59  ? -45.502 39.607  -66.033 1.00 38.61 ? 59  GLY B CA    1 
ATOM   9698  C C     . GLY D  1 59  ? -44.009 39.819  -66.140 1.00 35.16 ? 59  GLY B C     1 
ATOM   9699  O O     . GLY D  1 59  ? -43.227 38.869  -66.097 1.00 37.50 ? 59  GLY B O     1 
ATOM   9700  N N     . TYR D  1 60  ? -43.591 41.081  -66.222 1.00 35.16 ? 60  TYR B N     1 
ATOM   9701  C CA    . TYR D  1 60  ? -42.177 41.412  -66.344 1.00 33.61 ? 60  TYR B CA    1 
ATOM   9702  C C     . TYR D  1 60  ? -41.363 40.958  -65.141 1.00 43.13 ? 60  TYR B C     1 
ATOM   9703  O O     . TYR D  1 60  ? -40.212 40.521  -65.306 1.00 44.76 ? 60  TYR B O     1 
ATOM   9704  C CB    . TYR D  1 60  ? -42.003 42.918  -66.519 1.00 34.95 ? 60  TYR B CB    1 
ATOM   9705  C CG    . TYR D  1 60  ? -40.575 43.405  -66.307 1.00 44.41 ? 60  TYR B CG    1 
ATOM   9706  C CD1   . TYR D  1 60  ? -39.628 43.229  -67.300 1.00 47.14 ? 60  TYR B CD1   1 
ATOM   9707  C CD2   . TYR D  1 60  ? -40.168 44.040  -65.120 1.00 42.82 ? 60  TYR B CD2   1 
ATOM   9708  C CE1   . TYR D  1 60  ? -38.332 43.646  -67.137 1.00 45.09 ? 60  TYR B CE1   1 
ATOM   9709  C CE2   . TYR D  1 60  ? -38.839 44.475  -64.958 1.00 37.57 ? 60  TYR B CE2   1 
ATOM   9710  C CZ    . TYR D  1 60  ? -37.933 44.265  -65.983 1.00 44.91 ? 60  TYR B CZ    1 
ATOM   9711  O OH    . TYR D  1 60  ? -36.610 44.655  -65.920 1.00 58.76 ? 60  TYR B OH    1 
ATOM   9712  N N     . VAL D  1 61  ? -41.917 41.083  -63.928 1.00 39.82 ? 61  VAL B N     1 
ATOM   9713  C CA    . VAL D  1 61  ? -41.187 40.648  -62.740 1.00 41.68 ? 61  VAL B CA    1 
ATOM   9714  C C     . VAL D  1 61  ? -41.019 39.138  -62.753 1.00 37.40 ? 61  VAL B C     1 
ATOM   9715  O O     . VAL D  1 61  ? -39.975 38.611  -62.357 1.00 37.29 ? 61  VAL B O     1 
ATOM   9716  C CB    . VAL D  1 61  ? -41.896 41.130  -61.463 1.00 35.37 ? 61  VAL B CB    1 
ATOM   9717  C CG1   . VAL D  1 61  ? -41.425 40.322  -60.283 1.00 37.76 ? 61  VAL B CG1   1 
ATOM   9718  C CG2   . VAL D  1 61  ? -41.597 42.597  -61.231 1.00 36.97 ? 61  VAL B CG2   1 
ATOM   9719  N N     . ALA D  1 62  ? -42.042 38.426  -63.229 1.00 34.76 ? 62  ALA B N     1 
ATOM   9720  C CA    . ALA D  1 62  ? -41.968 36.973  -63.362 1.00 41.80 ? 62  ALA B CA    1 
ATOM   9721  C C     . ALA D  1 62  ? -40.860 36.542  -64.321 1.00 41.66 ? 62  ALA B C     1 
ATOM   9722  O O     . ALA D  1 62  ? -40.035 35.686  -63.977 1.00 43.96 ? 62  ALA B O     1 
ATOM   9723  C CB    . ALA D  1 62  ? -43.317 36.425  -63.831 1.00 43.62 ? 62  ALA B CB    1 
ATOM   9724  N N     . ASP D  1 63  ? -40.838 37.103  -65.539 1.00 42.94 ? 63  ASP B N     1 
ATOM   9725  C CA    . ASP D  1 63  ? -39.847 36.695  -66.538 1.00 40.41 ? 63  ASP B CA    1 
ATOM   9726  C C     . ASP D  1 63  ? -38.437 36.894  -66.017 1.00 45.29 ? 63  ASP B C     1 
ATOM   9727  O O     . ASP D  1 63  ? -37.655 35.940  -65.939 1.00 51.33 ? 63  ASP B O     1 
ATOM   9728  C CB    . ASP D  1 63  ? -40.024 37.483  -67.828 1.00 39.67 ? 63  ASP B CB    1 
ATOM   9729  C CG    . ASP D  1 63  ? -41.459 37.619  -68.214 1.00 50.37 ? 63  ASP B CG    1 
ATOM   9730  O OD1   . ASP D  1 63  ? -42.214 36.641  -68.019 1.00 54.75 ? 63  ASP B OD1   1 
ATOM   9731  O OD2   . ASP D  1 63  ? -41.843 38.719  -68.677 1.00 54.84 ? 63  ASP B OD2   1 
ATOM   9732  N N     . THR D  1 64  ? -38.098 38.138  -65.651 1.00 39.01 ? 64  THR B N     1 
ATOM   9733  C CA    . THR D  1 64  ? -36.786 38.416  -65.081 1.00 41.65 ? 64  THR B CA    1 
ATOM   9734  C C     . THR D  1 64  ? -36.435 37.396  -64.007 1.00 39.57 ? 64  THR B C     1 
ATOM   9735  O O     . THR D  1 64  ? -35.295 36.921  -63.935 1.00 40.98 ? 64  THR B O     1 
ATOM   9736  C CB    . THR D  1 64  ? -36.752 39.824  -64.483 1.00 46.23 ? 64  THR B CB    1 
ATOM   9737  O OG1   . THR D  1 64  ? -37.106 40.793  -65.484 1.00 44.23 ? 64  THR B OG1   1 
ATOM   9738  C CG2   . THR D  1 64  ? -35.362 40.128  -63.932 1.00 34.45 ? 64  THR B CG2   1 
ATOM   9739  N N     . LEU D  1 65  ? -37.429 37.012  -63.202 1.00 39.21 ? 65  LEU B N     1 
ATOM   9740  C CA    . LEU D  1 65  ? -37.206 36.191  -62.022 1.00 38.20 ? 65  LEU B CA    1 
ATOM   9741  C C     . LEU D  1 65  ? -37.131 34.714  -62.369 1.00 40.52 ? 65  LEU B C     1 
ATOM   9742  O O     . LEU D  1 65  ? -36.356 33.966  -61.754 1.00 39.72 ? 65  LEU B O     1 
ATOM   9743  C CB    . LEU D  1 65  ? -38.327 36.428  -61.014 1.00 42.69 ? 65  LEU B CB    1 
ATOM   9744  C CG    . LEU D  1 65  ? -37.904 37.186  -59.764 1.00 46.72 ? 65  LEU B CG    1 
ATOM   9745  C CD1   . LEU D  1 65  ? -39.112 37.547  -58.873 1.00 40.01 ? 65  LEU B CD1   1 
ATOM   9746  C CD2   . LEU D  1 65  ? -36.879 36.330  -59.055 1.00 41.18 ? 65  LEU B CD2   1 
ATOM   9747  N N     . GLY D  1 66  ? -37.948 34.282  -63.321 1.00 37.72 ? 66  GLY B N     1 
ATOM   9748  C CA    . GLY D  1 66  ? -37.939 32.930  -63.815 1.00 39.02 ? 66  GLY B CA    1 
ATOM   9749  C C     . GLY D  1 66  ? -39.119 32.059  -63.416 1.00 43.81 ? 66  GLY B C     1 
ATOM   9750  O O     . GLY D  1 66  ? -39.016 30.831  -63.530 1.00 53.20 ? 66  GLY B O     1 
ATOM   9751  N N     . ILE D  1 67  ? -40.233 32.644  -62.986 1.00 38.05 ? 67  ILE B N     1 
ATOM   9752  C CA    . ILE D  1 67  ? -41.286 31.901  -62.313 1.00 41.26 ? 67  ILE B CA    1 
ATOM   9753  C C     . ILE D  1 67  ? -42.598 32.013  -63.102 1.00 46.92 ? 67  ILE B C     1 
ATOM   9754  O O     . ILE D  1 67  ? -42.716 32.775  -64.063 1.00 46.58 ? 67  ILE B O     1 
ATOM   9755  C CB    . ILE D  1 67  ? -41.454 32.376  -60.860 1.00 46.22 ? 67  ILE B CB    1 
ATOM   9756  C CG1   . ILE D  1 67  ? -41.888 33.848  -60.814 1.00 44.69 ? 67  ILE B CG1   1 
ATOM   9757  C CG2   . ILE D  1 67  ? -40.136 32.202  -60.086 1.00 40.30 ? 67  ILE B CG2   1 
ATOM   9758  C CD1   . ILE D  1 67  ? -42.160 34.346  -59.385 1.00 41.58 ? 67  ILE B CD1   1 
ATOM   9759  N N     . ASP D  1 68  ? -43.593 31.235  -62.674 1.00 48.51 ? 68  ASP B N     1 
ATOM   9760  C CA    . ASP D  1 68  ? -44.845 31.062  -63.424 1.00 50.38 ? 68  ASP B CA    1 
ATOM   9761  C C     . ASP D  1 68  ? -45.811 32.180  -63.042 1.00 47.30 ? 68  ASP B C     1 
ATOM   9762  O O     . ASP D  1 68  ? -46.528 32.091  -62.039 1.00 50.76 ? 68  ASP B O     1 
ATOM   9763  C CB    . ASP D  1 68  ? -45.425 29.675  -63.147 1.00 54.66 ? 68  ASP B CB    1 
ATOM   9764  C CG    . ASP D  1 68  ? -46.778 29.440  -63.801 1.00 53.59 ? 68  ASP B CG    1 
ATOM   9765  O OD1   . ASP D  1 68  ? -47.107 30.131  -64.796 1.00 49.53 ? 68  ASP B OD1   1 
ATOM   9766  O OD2   . ASP D  1 68  ? -47.510 28.546  -63.302 1.00 49.46 ? 68  ASP B OD2   1 
ATOM   9767  N N     . GLY D  1 69  ? -45.831 33.237  -63.851 1.00 44.34 ? 69  GLY B N     1 
ATOM   9768  C CA    . GLY D  1 69  ? -46.666 34.384  -63.533 1.00 47.77 ? 69  GLY B CA    1 
ATOM   9769  C C     . GLY D  1 69  ? -48.133 34.033  -63.371 1.00 51.26 ? 69  GLY B C     1 
ATOM   9770  O O     . GLY D  1 69  ? -48.823 34.601  -62.521 1.00 53.23 ? 69  GLY B O     1 
ATOM   9771  N N     . THR D  1 70  ? -48.634 33.089  -64.175 1.00 47.62 ? 70  THR B N     1 
ATOM   9772  C CA    . THR D  1 70  ? -50.053 32.742  -64.103 1.00 50.48 ? 70  THR B CA    1 
ATOM   9773  C C     . THR D  1 70  ? -50.428 32.058  -62.788 1.00 53.42 ? 70  THR B C     1 
ATOM   9774  O O     . THR D  1 70  ? -51.625 31.935  -62.492 1.00 49.63 ? 70  THR B O     1 
ATOM   9775  C CB    . THR D  1 70  ? -50.450 31.858  -65.295 1.00 48.56 ? 70  THR B CB    1 
ATOM   9776  O OG1   . THR D  1 70  ? -49.790 30.584  -65.211 1.00 47.93 ? 70  THR B OG1   1 
ATOM   9777  C CG2   . THR D  1 70  ? -50.074 32.539  -66.609 1.00 45.82 ? 70  THR B CG2   1 
ATOM   9778  N N     . SER D  1 71  ? -49.441 31.625  -61.999 1.00 49.56 ? 71  SER B N     1 
ATOM   9779  C CA    . SER D  1 71  ? -49.677 31.029  -60.690 1.00 48.59 ? 71  SER B CA    1 
ATOM   9780  C C     . SER D  1 71  ? -49.777 32.063  -59.588 1.00 49.42 ? 71  SER B C     1 
ATOM   9781  O O     . SER D  1 71  ? -50.449 31.827  -58.580 1.00 50.57 ? 71  SER B O     1 
ATOM   9782  C CB    . SER D  1 71  ? -48.534 30.093  -60.321 1.00 50.19 ? 71  SER B CB    1 
ATOM   9783  O OG    . SER D  1 71  ? -47.533 30.854  -59.666 1.00 45.68 ? 71  SER B OG    1 
ATOM   9784  N N     . VAL D  1 72  ? -49.083 33.177  -59.745 1.00 47.18 ? 72  VAL B N     1 
ATOM   9785  C CA    . VAL D  1 72  ? -49.017 34.197  -58.714 1.00 46.07 ? 72  VAL B CA    1 
ATOM   9786  C C     . VAL D  1 72  ? -50.280 35.036  -58.784 1.00 45.92 ? 72  VAL B C     1 
ATOM   9787  O O     . VAL D  1 72  ? -50.674 35.474  -59.864 1.00 44.86 ? 72  VAL B O     1 
ATOM   9788  C CB    . VAL D  1 72  ? -47.765 35.060  -58.908 1.00 44.71 ? 72  VAL B CB    1 
ATOM   9789  C CG1   . VAL D  1 72  ? -47.667 36.113  -57.832 1.00 43.09 ? 72  VAL B CG1   1 
ATOM   9790  C CG2   . VAL D  1 72  ? -46.534 34.170  -58.936 1.00 45.27 ? 72  VAL B CG2   1 
ATOM   9791  N N     . HIS D  1 73  ? -50.918 35.263  -57.641 1.00 45.55 ? 73  HIS B N     1 
ATOM   9792  C CA    . HIS D  1 73  ? -52.109 36.096  -57.574 1.00 41.83 ? 73  HIS B CA    1 
ATOM   9793  C C     . HIS D  1 73  ? -51.814 37.366  -56.786 1.00 40.24 ? 73  HIS B C     1 
ATOM   9794  O O     . HIS D  1 73  ? -50.877 37.429  -55.990 1.00 45.67 ? 73  HIS B O     1 
ATOM   9795  C CB    . HIS D  1 73  ? -53.279 35.325  -56.947 1.00 44.56 ? 73  HIS B CB    1 
ATOM   9796  C CG    . HIS D  1 73  ? -53.579 34.027  -57.635 1.00 46.17 ? 73  HIS B CG    1 
ATOM   9797  N ND1   . HIS D  1 73  ? -52.717 32.951  -57.608 1.00 46.97 ? 73  HIS B ND1   1 
ATOM   9798  C CD2   . HIS D  1 73  ? -54.639 33.641  -58.384 1.00 46.60 ? 73  HIS B CD2   1 
ATOM   9799  C CE1   . HIS D  1 73  ? -53.235 31.956  -58.306 1.00 47.76 ? 73  HIS B CE1   1 
ATOM   9800  N NE2   . HIS D  1 73  ? -54.400 32.349  -58.789 1.00 55.24 ? 73  HIS B NE2   1 
ATOM   9801  N N     . VAL D  1 74  ? -52.614 38.398  -57.022 1.00 40.93 ? 74  VAL B N     1 
ATOM   9802  C CA    . VAL D  1 74  ? -52.442 39.665  -56.323 1.00 41.12 ? 74  VAL B CA    1 
ATOM   9803  C C     . VAL D  1 74  ? -53.813 40.247  -56.047 1.00 42.31 ? 74  VAL B C     1 
ATOM   9804  O O     . VAL D  1 74  ? -54.593 40.475  -56.979 1.00 43.34 ? 74  VAL B O     1 
ATOM   9805  C CB    . VAL D  1 74  ? -51.592 40.665  -57.116 1.00 36.40 ? 74  VAL B CB    1 
ATOM   9806  C CG1   . VAL D  1 74  ? -51.989 42.095  -56.763 1.00 37.30 ? 74  VAL B CG1   1 
ATOM   9807  C CG2   . VAL D  1 74  ? -50.147 40.429  -56.799 1.00 36.79 ? 74  VAL B CG2   1 
ATOM   9808  N N     . GLU D  1 75  ? -54.106 40.480  -54.778 1.00 46.59 ? 75  GLU B N     1 
ATOM   9809  C CA    . GLU D  1 75  ? -55.377 41.031  -54.337 1.00 44.53 ? 75  GLU B CA    1 
ATOM   9810  C C     . GLU D  1 75  ? -55.114 42.447  -53.848 1.00 43.53 ? 75  GLU B C     1 
ATOM   9811  O O     . GLU D  1 75  ? -54.423 42.643  -52.847 1.00 43.89 ? 75  GLU B O     1 
ATOM   9812  C CB    . GLU D  1 75  ? -55.975 40.161  -53.239 1.00 42.29 ? 75  GLU B CB    1 
ATOM   9813  C CG    . GLU D  1 75  ? -55.743 38.682  -53.448 1.00 47.91 ? 75  GLU B CG    1 
ATOM   9814  C CD    . GLU D  1 75  ? -56.920 38.005  -54.116 1.00 47.33 ? 75  GLU B CD    1 
ATOM   9815  O OE1   . GLU D  1 75  ? -57.707 38.727  -54.755 1.00 51.14 ? 75  GLU B OE1   1 
ATOM   9816  O OE2   . GLU D  1 75  ? -57.048 36.761  -54.020 1.00 42.81 ? 75  GLU B OE2   1 
ATOM   9817  N N     . ARG D  1 76  ? -55.635 43.432  -54.567 1.00 48.00 ? 76  ARG B N     1 
ATOM   9818  C CA    . ARG D  1 76  ? -55.516 44.811  -54.122 1.00 51.40 ? 76  ARG B CA    1 
ATOM   9819  C C     . ARG D  1 76  ? -56.589 45.117  -53.081 1.00 52.21 ? 76  ARG B C     1 
ATOM   9820  O O     . ARG D  1 76  ? -57.651 44.482  -53.041 1.00 47.13 ? 76  ARG B O     1 
ATOM   9821  C CB    . ARG D  1 76  ? -55.652 45.773  -55.307 1.00 49.26 ? 76  ARG B CB    1 
ATOM   9822  C CG    . ARG D  1 76  ? -57.099 45.965  -55.641 1.00 56.45 ? 76  ARG B CG    1 
ATOM   9823  C CD    . ARG D  1 76  ? -57.445 46.883  -56.804 1.00 63.18 ? 76  ARG B CD    1 
ATOM   9824  N NE    . ARG D  1 76  ? -58.898 46.957  -57.001 1.00 73.05 ? 76  ARG B NE    1 
ATOM   9825  C CZ    . ARG D  1 76  ? -59.760 45.938  -56.975 1.00 71.01 ? 76  ARG B CZ    1 
ATOM   9826  N NH1   . ARG D  1 76  ? -59.360 44.676  -56.905 1.00 58.54 ? 76  ARG B NH1   1 
ATOM   9827  N NH2   . ARG D  1 76  ? -61.067 46.194  -57.020 1.00 67.38 ? 76  ARG B NH2   1 
ATOM   9828  N N     . THR D  1 77  ? -56.288 46.089  -52.219 1.00 49.61 ? 77  THR B N     1 
ATOM   9829  C CA    . THR D  1 77  ? -57.266 46.715  -51.341 1.00 44.82 ? 77  THR B CA    1 
ATOM   9830  C C     . THR D  1 77  ? -57.219 48.219  -51.551 1.00 49.25 ? 77  THR B C     1 
ATOM   9831  O O     . THR D  1 77  ? -56.146 48.781  -51.782 1.00 56.07 ? 77  THR B O     1 
ATOM   9832  C CB    . THR D  1 77  ? -56.998 46.407  -49.879 1.00 46.81 ? 77  THR B CB    1 
ATOM   9833  O OG1   . THR D  1 77  ? -56.060 47.360  -49.381 1.00 55.27 ? 77  THR B OG1   1 
ATOM   9834  C CG2   . THR D  1 77  ? -56.415 45.017  -49.716 1.00 48.34 ? 77  THR B CG2   1 
ATOM   9835  N N     . GLN D  1 78  ? -58.378 48.879  -51.487 1.00 54.20 ? 78  GLN B N     1 
ATOM   9836  C CA    . GLN D  1 78  ? -58.391 50.328  -51.691 1.00 54.69 ? 78  GLN B CA    1 
ATOM   9837  C C     . GLN D  1 78  ? -57.912 51.078  -50.457 1.00 55.73 ? 78  GLN B C     1 
ATOM   9838  O O     . GLN D  1 78  ? -57.474 52.225  -50.583 1.00 63.10 ? 78  GLN B O     1 
ATOM   9839  C CB    . GLN D  1 78  ? -59.797 50.813  -52.096 1.00 63.10 ? 78  GLN B CB    1 
ATOM   9840  C CG    . GLN D  1 78  ? -59.895 52.309  -52.530 1.00 65.04 ? 78  GLN B CG    1 
ATOM   9841  C CD    . GLN D  1 78  ? -61.237 52.696  -53.205 1.00 67.54 ? 78  GLN B CD    1 
ATOM   9842  O OE1   . GLN D  1 78  ? -62.157 51.883  -53.304 1.00 61.19 ? 78  GLN B OE1   1 
ATOM   9843  N NE2   . GLN D  1 78  ? -61.338 53.947  -53.667 1.00 63.13 ? 78  GLN B NE2   1 
ATOM   9844  N N     . THR D  1 79  ? -57.955 50.449  -49.279 1.00 52.21 ? 79  THR B N     1 
ATOM   9845  C CA    . THR D  1 79  ? -57.515 51.076  -48.040 1.00 51.93 ? 79  THR B CA    1 
ATOM   9846  C C     . THR D  1 79  ? -56.167 50.518  -47.591 1.00 50.63 ? 79  THR B C     1 
ATOM   9847  O O     . THR D  1 79  ? -55.731 49.463  -48.063 1.00 47.77 ? 79  THR B O     1 
ATOM   9848  C CB    . THR D  1 79  ? -58.559 50.859  -46.945 1.00 48.32 ? 79  THR B CB    1 
ATOM   9849  O OG1   . THR D  1 79  ? -59.029 49.507  -47.006 1.00 56.15 ? 79  THR B OG1   1 
ATOM   9850  C CG2   . THR D  1 79  ? -59.731 51.813  -47.135 1.00 52.92 ? 79  THR B CG2   1 
ATOM   9851  N N     . PRO D  1 80  ? -55.460 51.221  -46.697 1.00 47.95 ? 80  PRO B N     1 
ATOM   9852  C CA    . PRO D  1 80  ? -54.189 50.696  -46.186 1.00 44.34 ? 80  PRO B CA    1 
ATOM   9853  C C     . PRO D  1 80  ? -54.374 49.434  -45.355 1.00 49.74 ? 80  PRO B C     1 
ATOM   9854  O O     . PRO D  1 80  ? -55.419 49.214  -44.734 1.00 48.71 ? 80  PRO B O     1 
ATOM   9855  C CB    . PRO D  1 80  ? -53.658 51.849  -45.332 1.00 40.00 ? 80  PRO B CB    1 
ATOM   9856  C CG    . PRO D  1 80  ? -54.241 53.064  -45.973 1.00 41.45 ? 80  PRO B CG    1 
ATOM   9857  C CD    . PRO D  1 80  ? -55.623 52.649  -46.371 1.00 47.09 ? 80  PRO B CD    1 
ATOM   9858  N N     . LEU D  1 81  ? -53.334 48.596  -45.353 1.00 41.98 ? 81  LEU B N     1 
ATOM   9859  C CA    . LEU D  1 81  ? -53.352 47.332  -44.616 1.00 39.36 ? 81  LEU B CA    1 
ATOM   9860  C C     . LEU D  1 81  ? -53.286 47.636  -43.124 1.00 48.68 ? 81  LEU B C     1 
ATOM   9861  O O     . LEU D  1 81  ? -52.219 47.614  -42.514 1.00 52.70 ? 81  LEU B O     1 
ATOM   9862  C CB    . LEU D  1 81  ? -52.181 46.440  -45.021 1.00 41.47 ? 81  LEU B CB    1 
ATOM   9863  C CG    . LEU D  1 81  ? -51.604 46.430  -46.446 1.00 53.09 ? 81  LEU B CG    1 
ATOM   9864  C CD1   . LEU D  1 81  ? -50.516 47.486  -46.610 1.00 51.52 ? 81  LEU B CD1   1 
ATOM   9865  C CD2   . LEU D  1 81  ? -51.056 45.057  -46.807 1.00 41.61 ? 81  LEU B CD2   1 
ATOM   9866  N N     . SER D  1 82  ? -54.446 47.908  -42.519 1.00 51.13 ? 82  SER B N     1 
ATOM   9867  C CA    . SER D  1 82  ? -54.523 48.176  -41.086 1.00 41.60 ? 82  SER B CA    1 
ATOM   9868  C C     . SER D  1 82  ? -54.877 46.920  -40.305 1.00 46.59 ? 82  SER B C     1 
ATOM   9869  O O     . SER D  1 82  ? -55.412 45.947  -40.845 1.00 40.22 ? 82  SER B O     1 
ATOM   9870  C CB    . SER D  1 82  ? -55.562 49.248  -40.773 1.00 42.43 ? 82  SER B CB    1 
ATOM   9871  O OG    . SER D  1 82  ? -55.059 50.516  -41.101 1.00 51.79 ? 82  SER B OG    1 
ATOM   9872  N N     . GLU D  1 83  ? -54.587 46.966  -39.001 1.00 42.09 ? 83  GLU B N     1 
ATOM   9873  C CA    . GLU D  1 83  ? -55.038 45.898  -38.124 1.00 37.83 ? 83  GLU B CA    1 
ATOM   9874  C C     . GLU D  1 83  ? -56.525 45.662  -38.311 1.00 39.86 ? 83  GLU B C     1 
ATOM   9875  O O     . GLU D  1 83  ? -56.982 44.514  -38.336 1.00 39.25 ? 83  GLU B O     1 
ATOM   9876  C CB    . GLU D  1 83  ? -54.722 46.227  -36.666 1.00 38.78 ? 83  GLU B CB    1 
ATOM   9877  C CG    . GLU D  1 83  ? -53.239 46.431  -36.358 1.00 33.02 ? 83  GLU B CG    1 
ATOM   9878  C CD    . GLU D  1 83  ? -52.453 45.142  -36.392 1.00 32.69 ? 83  GLU B CD    1 
ATOM   9879  O OE1   . GLU D  1 83  ? -52.045 44.745  -37.496 1.00 39.73 ? 83  GLU B OE1   1 
ATOM   9880  O OE2   . GLU D  1 83  ? -52.240 44.516  -35.328 1.00 32.60 ? 83  GLU B OE2   1 
ATOM   9881  N N     . ALA D  1 84  ? -57.293 46.742  -38.481 1.00 42.44 ? 84  ALA B N     1 
ATOM   9882  C CA    . ALA D  1 84  ? -58.700 46.597  -38.835 1.00 43.45 ? 84  ALA B CA    1 
ATOM   9883  C C     . ALA D  1 84  ? -58.850 45.739  -40.083 1.00 47.07 ? 84  ALA B C     1 
ATOM   9884  O O     . ALA D  1 84  ? -59.673 44.813  -40.132 1.00 49.29 ? 84  ALA B O     1 
ATOM   9885  C CB    . ALA D  1 84  ? -59.332 47.970  -39.062 1.00 33.04 ? 84  ALA B CB    1 
ATOM   9886  N N     . VAL D  1 85  ? -58.041 46.028  -41.100 1.00 42.92 ? 85  VAL B N     1 
ATOM   9887  C CA    . VAL D  1 85  ? -58.123 45.265  -42.339 1.00 43.46 ? 85  VAL B CA    1 
ATOM   9888  C C     . VAL D  1 85  ? -57.756 43.808  -42.074 1.00 48.16 ? 85  VAL B C     1 
ATOM   9889  O O     . VAL D  1 85  ? -58.430 42.884  -42.558 1.00 50.53 ? 85  VAL B O     1 
ATOM   9890  C CB    . VAL D  1 85  ? -57.230 45.911  -43.415 1.00 36.93 ? 85  VAL B CB    1 
ATOM   9891  C CG1   . VAL D  1 85  ? -56.421 44.867  -44.165 1.00 44.75 ? 85  VAL B CG1   1 
ATOM   9892  C CG2   . VAL D  1 85  ? -58.053 46.717  -44.352 1.00 42.06 ? 85  VAL B CG2   1 
ATOM   9893  N N     . LEU D  1 86  ? -56.710 43.575  -41.264 1.00 39.52 ? 86  LEU B N     1 
ATOM   9894  C CA    . LEU D  1 86  ? -56.350 42.200  -40.958 1.00 36.71 ? 86  LEU B CA    1 
ATOM   9895  C C     . LEU D  1 86  ? -57.354 41.530  -40.048 1.00 46.16 ? 86  LEU B C     1 
ATOM   9896  O O     . LEU D  1 86  ? -57.317 40.300  -39.913 1.00 41.67 ? 86  LEU B O     1 
ATOM   9897  C CB    . LEU D  1 86  ? -54.977 42.123  -40.318 1.00 38.50 ? 86  LEU B CB    1 
ATOM   9898  C CG    . LEU D  1 86  ? -53.834 42.646  -41.164 1.00 39.16 ? 86  LEU B CG    1 
ATOM   9899  C CD1   . LEU D  1 86  ? -53.324 43.948  -40.618 1.00 42.30 ? 86  LEU B CD1   1 
ATOM   9900  C CD2   . LEU D  1 86  ? -52.744 41.602  -41.193 1.00 39.10 ? 86  LEU B CD2   1 
ATOM   9901  N N     . GLN D  1 87  ? -58.232 42.309  -39.416 1.00 50.93 ? 87  GLN B N     1 
ATOM   9902  C CA    . GLN D  1 87  ? -59.300 41.762  -38.599 1.00 48.53 ? 87  GLN B CA    1 
ATOM   9903  C C     . GLN D  1 87  ? -60.644 41.742  -39.308 1.00 49.85 ? 87  GLN B C     1 
ATOM   9904  O O     . GLN D  1 87  ? -61.556 41.043  -38.844 1.00 57.13 ? 87  GLN B O     1 
ATOM   9905  C CB    . GLN D  1 87  ? -59.428 42.553  -37.297 1.00 46.89 ? 87  GLN B CB    1 
ATOM   9906  C CG    . GLN D  1 87  ? -58.195 42.497  -36.425 1.00 42.84 ? 87  GLN B CG    1 
ATOM   9907  C CD    . GLN D  1 87  ? -58.236 43.520  -35.317 1.00 44.94 ? 87  GLN B CD    1 
ATOM   9908  O OE1   . GLN D  1 87  ? -57.770 44.655  -35.477 1.00 45.12 ? 87  GLN B OE1   1 
ATOM   9909  N NE2   . GLN D  1 87  ? -58.799 43.130  -34.182 1.00 49.27 ? 87  GLN B NE2   1 
ATOM   9910  N N     . ASP D  1 88  ? -60.787 42.482  -40.406 1.00 45.26 ? 88  ASP B N     1 
ATOM   9911  C CA    . ASP D  1 88  ? -62.009 42.419  -41.198 1.00 49.85 ? 88  ASP B CA    1 
ATOM   9912  C C     . ASP D  1 88  ? -62.182 41.015  -41.770 1.00 49.48 ? 88  ASP B C     1 
ATOM   9913  O O     . ASP D  1 88  ? -61.345 40.570  -42.566 1.00 54.23 ? 88  ASP B O     1 
ATOM   9914  C CB    . ASP D  1 88  ? -61.988 43.441  -42.331 1.00 44.61 ? 88  ASP B CB    1 
ATOM   9915  C CG    . ASP D  1 88  ? -63.186 43.310  -43.253 1.00 53.91 ? 88  ASP B CG    1 
ATOM   9916  O OD1   . ASP D  1 88  ? -64.160 42.627  -42.867 1.00 55.16 ? 88  ASP B OD1   1 
ATOM   9917  O OD2   . ASP D  1 88  ? -63.159 43.874  -44.372 1.00 55.62 ? 88  ASP B OD2   1 
ATOM   9918  N N     . PRO D  1 89  ? -63.241 40.295  -41.409 1.00 44.67 ? 89  PRO B N     1 
ATOM   9919  C CA    . PRO D  1 89  ? -63.442 38.958  -41.981 1.00 49.24 ? 89  PRO B CA    1 
ATOM   9920  C C     . PRO D  1 89  ? -63.803 38.985  -43.457 1.00 49.64 ? 89  PRO B C     1 
ATOM   9921  O O     . PRO D  1 89  ? -63.602 37.974  -44.148 1.00 45.58 ? 89  PRO B O     1 
ATOM   9922  C CB    . PRO D  1 89  ? -64.580 38.381  -41.133 1.00 45.86 ? 89  PRO B CB    1 
ATOM   9923  C CG    . PRO D  1 89  ? -65.316 39.575  -40.647 1.00 45.77 ? 89  PRO B CG    1 
ATOM   9924  C CD    . PRO D  1 89  ? -64.331 40.693  -40.509 1.00 43.20 ? 89  PRO B CD    1 
ATOM   9925  N N     . GLU D  1 90  ? -64.346 40.100  -43.954 1.00 48.95 ? 90  GLU B N     1 
ATOM   9926  C CA    . GLU D  1 90  ? -64.474 40.274  -45.393 1.00 50.68 ? 90  GLU B CA    1 
ATOM   9927  C C     . GLU D  1 90  ? -63.112 40.170  -46.049 1.00 52.65 ? 90  GLU B C     1 
ATOM   9928  O O     . GLU D  1 90  ? -62.948 39.507  -47.082 1.00 49.84 ? 90  GLU B O     1 
ATOM   9929  C CB    . GLU D  1 90  ? -65.114 41.626  -45.705 1.00 56.59 ? 90  GLU B CB    1 
ATOM   9930  C CG    . GLU D  1 90  ? -65.841 41.689  -47.044 1.00 57.20 ? 90  GLU B CG    1 
ATOM   9931  C CD    . GLU D  1 90  ? -67.197 42.357  -46.915 1.00 65.14 ? 90  GLU B CD    1 
ATOM   9932  O OE1   . GLU D  1 90  ? -68.156 41.688  -46.462 1.00 60.56 ? 90  GLU B OE1   1 
ATOM   9933  O OE2   . GLU D  1 90  ? -67.300 43.558  -47.253 1.00 69.87 ? 90  GLU B OE2   1 
ATOM   9934  N N     . PHE D  1 91  ? -62.117 40.807  -45.441 1.00 52.58 ? 91  PHE B N     1 
ATOM   9935  C CA    . PHE D  1 91  ? -60.745 40.626  -45.884 1.00 49.27 ? 91  PHE B CA    1 
ATOM   9936  C C     . PHE D  1 91  ? -60.273 39.198  -45.628 1.00 52.22 ? 91  PHE B C     1 
ATOM   9937  O O     . PHE D  1 91  ? -59.740 38.538  -46.528 1.00 56.87 ? 91  PHE B O     1 
ATOM   9938  C CB    . PHE D  1 91  ? -59.842 41.630  -45.174 1.00 47.58 ? 91  PHE B CB    1 
ATOM   9939  C CG    . PHE D  1 91  ? -58.411 41.440  -45.489 1.00 49.01 ? 91  PHE B CG    1 
ATOM   9940  C CD1   . PHE D  1 91  ? -57.656 40.500  -44.810 1.00 51.57 ? 91  PHE B CD1   1 
ATOM   9941  C CD2   . PHE D  1 91  ? -57.816 42.173  -46.496 1.00 56.62 ? 91  PHE B CD2   1 
ATOM   9942  C CE1   . PHE D  1 91  ? -56.330 40.294  -45.121 1.00 51.09 ? 91  PHE B CE1   1 
ATOM   9943  C CE2   . PHE D  1 91  ? -56.483 41.977  -46.817 1.00 56.41 ? 91  PHE B CE2   1 
ATOM   9944  C CZ    . PHE D  1 91  ? -55.739 41.034  -46.120 1.00 56.23 ? 91  PHE B CZ    1 
ATOM   9945  N N     . ILE D  1 92  ? -60.438 38.715  -44.393 1.00 49.60 ? 92  ILE B N     1 
ATOM   9946  C CA    . ILE D  1 92  ? -59.921 37.405  -44.000 1.00 52.50 ? 92  ILE B CA    1 
ATOM   9947  C C     . ILE D  1 92  ? -60.468 36.300  -44.891 1.00 50.84 ? 92  ILE B C     1 
ATOM   9948  O O     . ILE D  1 92  ? -59.784 35.299  -45.149 1.00 52.92 ? 92  ILE B O     1 
ATOM   9949  C CB    . ILE D  1 92  ? -60.243 37.146  -42.518 1.00 49.50 ? 92  ILE B CB    1 
ATOM   9950  C CG1   . ILE D  1 92  ? -59.593 38.216  -41.653 1.00 46.91 ? 92  ILE B CG1   1 
ATOM   9951  C CG2   . ILE D  1 92  ? -59.787 35.766  -42.096 1.00 50.29 ? 92  ILE B CG2   1 
ATOM   9952  C CD1   . ILE D  1 92  ? -60.289 38.407  -40.336 1.00 53.33 ? 92  ILE B CD1   1 
ATOM   9953  N N     . ASP D  1 93  ? -61.687 36.456  -45.393 1.00 48.41 ? 93  ASP B N     1 
ATOM   9954  C CA    . ASP D  1 93  ? -62.186 35.432  -46.298 1.00 52.21 ? 93  ASP B CA    1 
ATOM   9955  C C     . ASP D  1 93  ? -61.497 35.484  -47.661 1.00 52.59 ? 93  ASP B C     1 
ATOM   9956  O O     . ASP D  1 93  ? -61.289 34.430  -48.272 1.00 57.02 ? 93  ASP B O     1 
ATOM   9957  C CB    . ASP D  1 93  ? -63.700 35.542  -46.428 1.00 50.47 ? 93  ASP B CB    1 
ATOM   9958  C CG    . ASP D  1 93  ? -64.418 34.528  -45.552 1.00 55.10 ? 93  ASP B CG    1 
ATOM   9959  O OD1   . ASP D  1 93  ? -63.915 34.252  -44.433 1.00 51.68 ? 93  ASP B OD1   1 
ATOM   9960  O OD2   . ASP D  1 93  ? -65.464 33.995  -45.981 1.00 52.26 ? 93  ASP B OD2   1 
ATOM   9961  N N     . ARG D  1 94  ? -61.105 36.671  -48.139 1.00 47.62 ? 94  ARG B N     1 
ATOM   9962  C CA    . ARG D  1 94  ? -60.383 36.764  -49.410 1.00 47.11 ? 94  ARG B CA    1 
ATOM   9963  C C     . ARG D  1 94  ? -59.167 35.855  -49.405 1.00 48.29 ? 94  ARG B C     1 
ATOM   9964  O O     . ARG D  1 94  ? -59.043 34.937  -50.222 1.00 49.08 ? 94  ARG B O     1 
ATOM   9965  C CB    . ARG D  1 94  ? -59.941 38.205  -49.680 1.00 45.52 ? 94  ARG B CB    1 
ATOM   9966  C CG    . ARG D  1 94  ? -61.004 39.106  -50.266 1.00 46.94 ? 94  ARG B CG    1 
ATOM   9967  C CD    . ARG D  1 94  ? -60.957 39.140  -51.791 1.00 47.28 ? 94  ARG B CD    1 
ATOM   9968  N NE    . ARG D  1 94  ? -59.840 39.894  -52.363 1.00 52.86 ? 94  ARG B NE    1 
ATOM   9969  C CZ    . ARG D  1 94  ? -59.634 41.199  -52.214 1.00 48.28 ? 94  ARG B CZ    1 
ATOM   9970  N NH1   . ARG D  1 94  ? -60.385 41.938  -51.407 1.00 49.58 ? 94  ARG B NH1   1 
ATOM   9971  N NH2   . ARG D  1 94  ? -58.656 41.784  -52.903 1.00 36.32 ? 94  ARG B NH2   1 
ATOM   9972  N N     . LEU D  1 95  ? -58.252 36.113  -48.480 1.00 48.07 ? 95  LEU B N     1 
ATOM   9973  C CA    . LEU D  1 95  ? -57.073 35.273  -48.346 1.00 53.64 ? 95  LEU B CA    1 
ATOM   9974  C C     . LEU D  1 95  ? -57.461 33.806  -48.234 1.00 52.43 ? 95  LEU B C     1 
ATOM   9975  O O     . LEU D  1 95  ? -56.929 32.949  -48.954 1.00 51.32 ? 95  LEU B O     1 
ATOM   9976  C CB    . LEU D  1 95  ? -56.276 35.718  -47.120 1.00 51.32 ? 95  LEU B CB    1 
ATOM   9977  C CG    . LEU D  1 95  ? -55.700 37.130  -47.237 1.00 50.31 ? 95  LEU B CG    1 
ATOM   9978  C CD1   . LEU D  1 95  ? -54.624 37.352  -46.200 1.00 49.94 ? 95  LEU B CD1   1 
ATOM   9979  C CD2   . LEU D  1 95  ? -55.146 37.380  -48.631 1.00 51.87 ? 95  LEU B CD2   1 
ATOM   9980  N N     . ALA D  1 96  ? -58.419 33.510  -47.346 1.00 53.49 ? 96  ALA B N     1 
ATOM   9981  C CA    . ALA D  1 96  ? -58.809 32.135  -47.069 1.00 51.61 ? 96  ALA B CA    1 
ATOM   9982  C C     . ALA D  1 96  ? -59.042 31.350  -48.349 1.00 53.92 ? 96  ALA B C     1 
ATOM   9983  O O     . ALA D  1 96  ? -58.855 30.126  -48.374 1.00 53.53 ? 96  ALA B O     1 
ATOM   9984  C CB    . ALA D  1 96  ? -60.061 32.132  -46.197 1.00 53.32 ? 96  ALA B CB    1 
ATOM   9985  N N     . ALA D  1 97  ? -59.399 32.047  -49.430 1.00 52.42 ? 97  ALA B N     1 
ATOM   9986  C CA    . ALA D  1 97  ? -59.705 31.390  -50.695 1.00 54.44 ? 97  ALA B CA    1 
ATOM   9987  C C     . ALA D  1 97  ? -58.529 30.553  -51.186 1.00 60.57 ? 97  ALA B C     1 
ATOM   9988  O O     . ALA D  1 97  ? -58.638 29.328  -51.335 1.00 64.43 ? 97  ALA B O     1 
ATOM   9989  C CB    . ALA D  1 97  ? -60.111 32.435  -51.737 1.00 51.43 ? 97  ALA B CB    1 
ATOM   9990  N N     . HIS D  1 98  ? -57.390 31.198  -51.447 1.00 55.57 ? 98  HIS B N     1 
ATOM   9991  C CA    . HIS D  1 98  ? -56.241 30.457  -51.949 1.00 52.90 ? 98  HIS B CA    1 
ATOM   9992  C C     . HIS D  1 98  ? -55.792 29.405  -50.946 1.00 52.60 ? 98  HIS B C     1 
ATOM   9993  O O     . HIS D  1 98  ? -55.454 28.277  -51.324 1.00 51.76 ? 98  HIS B O     1 
ATOM   9994  C CB    . HIS D  1 98  ? -55.099 31.416  -52.257 1.00 50.45 ? 98  HIS B CB    1 
ATOM   9995  C CG    . HIS D  1 98  ? -55.510 32.611  -53.061 1.00 53.96 ? 98  HIS B CG    1 
ATOM   9996  N ND1   . HIS D  1 98  ? -55.374 32.668  -54.433 1.00 53.56 ? 98  HIS B ND1   1 
ATOM   9997  C CD2   . HIS D  1 98  ? -56.042 33.799  -52.685 1.00 49.87 ? 98  HIS B CD2   1 
ATOM   9998  C CE1   . HIS D  1 98  ? -55.805 33.840  -54.866 1.00 53.33 ? 98  HIS B CE1   1 
ATOM   9999  N NE2   . HIS D  1 98  ? -56.211 34.547  -53.826 1.00 45.09 ? 98  HIS B NE2   1 
ATOM   10000 N N     . THR D  1 99  ? -55.813 29.747  -49.654 1.00 51.40 ? 99  THR B N     1 
ATOM   10001 C CA    . THR D  1 99  ? -55.178 28.890  -48.660 1.00 51.42 ? 99  THR B CA    1 
ATOM   10002 C C     . THR D  1 99  ? -55.916 27.570  -48.512 1.00 49.38 ? 99  THR B C     1 
ATOM   10003 O O     . THR D  1 99  ? -55.283 26.511  -48.429 1.00 50.07 ? 99  THR B O     1 
ATOM   10004 C CB    . THR D  1 99  ? -55.081 29.628  -47.328 1.00 54.54 ? 99  THR B CB    1 
ATOM   10005 O OG1   . THR D  1 99  ? -56.392 29.900  -46.824 1.00 58.30 ? 99  THR B OG1   1 
ATOM   10006 C CG2   . THR D  1 99  ? -54.358 30.935  -47.530 1.00 54.73 ? 99  THR B CG2   1 
ATOM   10007 N N     . GLY D  1 100 ? -57.246 27.609  -48.502 1.00 52.12 ? 100 GLY B N     1 
ATOM   10008 C CA    . GLY D  1 100 ? -58.037 26.396  -48.437 1.00 52.95 ? 100 GLY B CA    1 
ATOM   10009 C C     . GLY D  1 100 ? -58.018 25.798  -47.052 1.00 53.54 ? 100 GLY B C     1 
ATOM   10010 O O     . GLY D  1 100 ? -58.466 26.447  -46.102 1.00 56.04 ? 100 GLY B O     1 
ATOM   10011 N N     . THR D  1 101 ? -57.510 24.568  -46.913 1.00 51.25 ? 101 THR B N     1 
ATOM   10012 C CA    . THR D  1 101 ? -57.267 24.035  -45.574 1.00 51.43 ? 101 THR B CA    1 
ATOM   10013 C C     . THR D  1 101 ? -56.190 24.833  -44.863 1.00 56.88 ? 101 THR B C     1 
ATOM   10014 O O     . THR D  1 101 ? -56.197 24.929  -43.628 1.00 52.03 ? 101 THR B O     1 
ATOM   10015 C CB    . THR D  1 101 ? -56.849 22.561  -45.627 1.00 58.96 ? 101 THR B CB    1 
ATOM   10016 O OG1   . THR D  1 101 ? -56.277 22.178  -44.365 1.00 61.65 ? 101 THR B OG1   1 
ATOM   10017 C CG2   . THR D  1 101 ? -55.816 22.331  -46.721 1.00 57.64 ? 101 THR B CG2   1 
ATOM   10018 N N     . GLY D  1 102 ? -55.266 25.405  -45.628 1.00 56.42 ? 102 GLY B N     1 
ATOM   10019 C CA    . GLY D  1 102 ? -54.157 26.153  -45.090 1.00 52.68 ? 102 GLY B CA    1 
ATOM   10020 C C     . GLY D  1 102 ? -52.878 25.370  -44.917 1.00 57.01 ? 102 GLY B C     1 
ATOM   10021 O O     . GLY D  1 102 ? -52.007 25.815  -44.164 1.00 63.58 ? 102 GLY B O     1 
ATOM   10022 N N     . ALA D  1 103 ? -52.723 24.230  -45.595 1.00 56.66 ? 103 ALA B N     1 
ATOM   10023 C CA    . ALA D  1 103 ? -51.615 23.330  -45.283 1.00 55.04 ? 103 ALA B CA    1 
ATOM   10024 C C     . ALA D  1 103 ? -50.308 23.785  -45.928 1.00 56.33 ? 103 ALA B C     1 
ATOM   10025 O O     . ALA D  1 103 ? -49.291 23.958  -45.245 1.00 57.72 ? 103 ALA B O     1 
ATOM   10026 C CB    . ALA D  1 103 ? -51.965 21.905  -45.713 1.00 58.41 ? 103 ALA B CB    1 
ATOM   10027 N N     . GLY D  1 104 ? -50.313 23.989  -47.240 1.00 53.79 ? 104 GLY B N     1 
ATOM   10028 C CA    . GLY D  1 104 ? -49.081 24.354  -47.918 1.00 62.46 ? 104 GLY B CA    1 
ATOM   10029 C C     . GLY D  1 104 ? -48.868 25.850  -48.035 1.00 62.28 ? 104 GLY B C     1 
ATOM   10030 O O     . GLY D  1 104 ? -48.276 26.338  -49.009 1.00 63.86 ? 104 GLY B O     1 
ATOM   10031 N N     . TRP D  1 105 ? -49.343 26.590  -47.041 1.00 54.85 ? 105 TRP B N     1 
ATOM   10032 C CA    . TRP D  1 105 ? -49.335 28.039  -47.104 1.00 51.98 ? 105 TRP B CA    1 
ATOM   10033 C C     . TRP D  1 105 ? -48.690 28.613  -45.853 1.00 52.76 ? 105 TRP B C     1 
ATOM   10034 O O     . TRP D  1 105 ? -48.605 27.952  -44.815 1.00 52.74 ? 105 TRP B O     1 
ATOM   10035 C CB    . TRP D  1 105 ? -50.750 28.579  -47.247 1.00 47.78 ? 105 TRP B CB    1 
ATOM   10036 C CG    . TRP D  1 105 ? -51.312 28.380  -48.561 1.00 46.79 ? 105 TRP B CG    1 
ATOM   10037 C CD1   . TRP D  1 105 ? -51.967 27.283  -49.010 1.00 48.40 ? 105 TRP B CD1   1 
ATOM   10038 C CD2   . TRP D  1 105 ? -51.292 29.315  -49.630 1.00 46.89 ? 105 TRP B CD2   1 
ATOM   10039 N NE1   . TRP D  1 105 ? -52.365 27.476  -50.306 1.00 53.36 ? 105 TRP B NE1   1 
ATOM   10040 C CE2   . TRP D  1 105 ? -51.956 28.716  -50.716 1.00 49.38 ? 105 TRP B CE2   1 
ATOM   10041 C CE3   . TRP D  1 105 ? -50.771 30.607  -49.778 1.00 41.43 ? 105 TRP B CE3   1 
ATOM   10042 C CZ2   . TRP D  1 105 ? -52.121 29.361  -51.942 1.00 50.55 ? 105 TRP B CZ2   1 
ATOM   10043 C CZ3   . TRP D  1 105 ? -50.923 31.247  -50.986 1.00 43.93 ? 105 TRP B CZ3   1 
ATOM   10044 C CH2   . TRP D  1 105 ? -51.598 30.625  -52.060 1.00 50.82 ? 105 TRP B CH2   1 
ATOM   10045 N N     . SER D  1 106 ? -48.251 29.869  -45.963 1.00 46.90 ? 106 SER B N     1 
ATOM   10046 C CA    . SER D  1 106 ? -47.798 30.635  -44.810 1.00 44.03 ? 106 SER B CA    1 
ATOM   10047 C C     . SER D  1 106 ? -48.049 32.110  -45.091 1.00 39.42 ? 106 SER B C     1 
ATOM   10048 O O     . SER D  1 106 ? -48.485 32.489  -46.177 1.00 37.35 ? 106 SER B O     1 
ATOM   10049 C CB    . SER D  1 106 ? -46.321 30.345  -44.465 1.00 39.51 ? 106 SER B CB    1 
ATOM   10050 O OG    . SER D  1 106 ? -45.416 30.697  -45.496 1.00 43.95 ? 106 SER B OG    1 
ATOM   10051 N N     . LEU D  1 107 ? -47.808 32.942  -44.079 1.00 41.57 ? 107 LEU B N     1 
ATOM   10052 C CA    . LEU D  1 107 ? -47.946 34.388  -44.187 1.00 36.27 ? 107 LEU B CA    1 
ATOM   10053 C C     . LEU D  1 107 ? -46.568 35.025  -44.153 1.00 31.53 ? 107 LEU B C     1 
ATOM   10054 O O     . LEU D  1 107 ? -45.633 34.482  -43.564 1.00 35.69 ? 107 LEU B O     1 
ATOM   10055 C CB    . LEU D  1 107 ? -48.805 34.956  -43.052 1.00 38.42 ? 107 LEU B CB    1 
ATOM   10056 C CG    . LEU D  1 107 ? -48.863 36.485  -42.923 1.00 36.41 ? 107 LEU B CG    1 
ATOM   10057 C CD1   . LEU D  1 107 ? -49.576 37.096  -44.136 1.00 32.06 ? 107 LEU B CD1   1 
ATOM   10058 C CD2   . LEU D  1 107 ? -49.540 36.907  -41.622 1.00 34.07 ? 107 LEU B CD2   1 
ATOM   10059 N N     . PHE D  1 108 ? -46.441 36.179  -44.790 1.00 33.01 ? 108 PHE B N     1 
ATOM   10060 C CA    . PHE D  1 108 ? -45.143 36.817  -45.001 1.00 32.23 ? 108 PHE B CA    1 
ATOM   10061 C C     . PHE D  1 108 ? -45.320 38.309  -44.798 1.00 32.23 ? 108 PHE B C     1 
ATOM   10062 O O     . PHE D  1 108 ? -45.205 39.105  -45.737 1.00 32.61 ? 108 PHE B O     1 
ATOM   10063 C CB    . PHE D  1 108 ? -44.607 36.489  -46.401 1.00 40.41 ? 108 PHE B CB    1 
ATOM   10064 C CG    . PHE D  1 108 ? -43.183 36.923  -46.637 1.00 37.91 ? 108 PHE B CG    1 
ATOM   10065 C CD1   . PHE D  1 108 ? -42.153 36.433  -45.849 1.00 32.90 ? 108 PHE B CD1   1 
ATOM   10066 C CD2   . PHE D  1 108 ? -42.882 37.819  -47.651 1.00 32.68 ? 108 PHE B CD2   1 
ATOM   10067 C CE1   . PHE D  1 108 ? -40.860 36.835  -46.066 1.00 34.07 ? 108 PHE B CE1   1 
ATOM   10068 C CE2   . PHE D  1 108 ? -41.593 38.227  -47.871 1.00 31.14 ? 108 PHE B CE2   1 
ATOM   10069 C CZ    . PHE D  1 108 ? -40.580 37.743  -47.080 1.00 39.38 ? 108 PHE B CZ    1 
ATOM   10070 N N     . PRO D  1 109 ? -45.600 38.728  -43.570 1.00 28.97 ? 109 PRO B N     1 
ATOM   10071 C CA    . PRO D  1 109 ? -45.931 40.125  -43.312 1.00 29.59 ? 109 PRO B CA    1 
ATOM   10072 C C     . PRO D  1 109 ? -44.703 40.958  -43.023 1.00 29.43 ? 109 PRO B C     1 
ATOM   10073 O O     . PRO D  1 109 ? -43.693 40.485  -42.504 1.00 32.24 ? 109 PRO B O     1 
ATOM   10074 C CB    . PRO D  1 109 ? -46.803 40.030  -42.057 1.00 32.74 ? 109 PRO B CB    1 
ATOM   10075 C CG    . PRO D  1 109 ? -46.129 38.927  -41.285 1.00 35.85 ? 109 PRO B CG    1 
ATOM   10076 C CD    . PRO D  1 109 ? -45.553 37.955  -42.320 1.00 32.10 ? 109 PRO B CD    1 
ATOM   10077 N N     . CYS D  1 110 ? -44.819 42.233  -43.357 1.00 30.83 ? 110 CYS B N     1 
ATOM   10078 C CA    . CYS D  1 110 ? -43.733 43.155  -43.072 1.00 28.69 ? 110 CYS B CA    1 
ATOM   10079 C C     . CYS D  1 110 ? -43.566 43.367  -41.577 1.00 35.15 ? 110 CYS B C     1 
ATOM   10080 O O     . CYS D  1 110 ? -42.434 43.463  -41.074 1.00 32.24 ? 110 CYS B O     1 
ATOM   10081 C CB    . CYS D  1 110 ? -44.013 44.472  -43.767 1.00 31.95 ? 110 CYS B CB    1 
ATOM   10082 S SG    . CYS D  1 110 ? -42.879 45.712  -43.304 1.00 36.09 ? 110 CYS B SG    1 
ATOM   10083 N N     . VAL D  1 111 ? -44.684 43.449  -40.854 1.00 33.33 ? 111 VAL B N     1 
ATOM   10084 C CA    . VAL D  1 111 ? -44.689 43.725  -39.422 1.00 32.15 ? 111 VAL B CA    1 
ATOM   10085 C C     . VAL D  1 111 ? -45.537 42.660  -38.739 1.00 35.73 ? 111 VAL B C     1 
ATOM   10086 O O     . VAL D  1 111 ? -46.715 42.467  -39.091 1.00 31.34 ? 111 VAL B O     1 
ATOM   10087 C CB    . VAL D  1 111 ? -45.227 45.134  -39.106 1.00 36.51 ? 111 VAL B CB    1 
ATOM   10088 C CG1   . VAL D  1 111 ? -44.899 45.519  -37.650 1.00 32.37 ? 111 VAL B CG1   1 
ATOM   10089 C CG2   . VAL D  1 111 ? -44.674 46.157  -40.089 1.00 31.27 ? 111 VAL B CG2   1 
ATOM   10090 N N     . SER D  1 112 ? -44.946 41.987  -37.755 1.00 30.53 ? 112 SER B N     1 
ATOM   10091 C CA    . SER D  1 112 ? -45.588 40.842  -37.120 1.00 35.55 ? 112 SER B CA    1 
ATOM   10092 C C     . SER D  1 112 ? -46.502 41.269  -35.980 1.00 34.70 ? 112 SER B C     1 
ATOM   10093 O O     . SER D  1 112 ? -46.350 40.827  -34.845 1.00 36.25 ? 112 SER B O     1 
ATOM   10094 C CB    . SER D  1 112 ? -44.526 39.867  -36.648 1.00 34.71 ? 112 SER B CB    1 
ATOM   10095 O OG    . SER D  1 112 ? -44.025 39.138  -37.758 1.00 37.29 ? 112 SER B OG    1 
ATOM   10096 N N     . THR D  1 113 ? -47.450 42.145  -36.305 1.00 31.01 ? 113 THR B N     1 
ATOM   10097 C CA    . THR D  1 113 ? -48.394 42.665  -35.339 1.00 32.67 ? 113 THR B CA    1 
ATOM   10098 C C     . THR D  1 113 ? -49.185 41.554  -34.667 1.00 34.47 ? 113 THR B C     1 
ATOM   10099 O O     . THR D  1 113 ? -49.166 40.387  -35.076 1.00 35.97 ? 113 THR B O     1 
ATOM   10100 C CB    . THR D  1 113 ? -49.405 43.593  -35.997 1.00 32.72 ? 113 THR B CB    1 
ATOM   10101 O OG1   . THR D  1 113 ? -50.327 42.809  -36.752 1.00 35.21 ? 113 THR B OG1   1 
ATOM   10102 C CG2   . THR D  1 113 ? -48.722 44.591  -36.882 1.00 35.04 ? 113 THR B CG2   1 
ATOM   10103 N N     . ARG D  1 114 ? -49.941 41.958  -33.644 1.00 33.86 ? 114 ARG B N     1 
ATOM   10104 C CA    . ARG D  1 114 ? -50.861 41.039  -33.001 1.00 36.85 ? 114 ARG B CA    1 
ATOM   10105 C C     . ARG D  1 114 ? -51.914 40.565  -33.991 1.00 36.86 ? 114 ARG B C     1 
ATOM   10106 O O     . ARG D  1 114 ? -52.248 39.372  -34.032 1.00 36.85 ? 114 ARG B O     1 
ATOM   10107 C CB    . ARG D  1 114 ? -51.484 41.724  -31.779 1.00 40.78 ? 114 ARG B CB    1 
ATOM   10108 C CG    . ARG D  1 114 ? -52.644 40.966  -31.097 1.00 34.28 ? 114 ARG B CG    1 
ATOM   10109 C CD    . ARG D  1 114 ? -53.000 41.581  -29.734 1.00 37.30 ? 114 ARG B CD    1 
ATOM   10110 N NE    . ARG D  1 114 ? -54.303 41.150  -29.221 1.00 40.03 ? 114 ARG B NE    1 
ATOM   10111 C CZ    . ARG D  1 114 ? -54.509 40.110  -28.422 1.00 39.56 ? 114 ARG B CZ    1 
ATOM   10112 N NH1   . ARG D  1 114 ? -53.511 39.339  -28.017 1.00 36.59 ? 114 ARG B NH1   1 
ATOM   10113 N NH2   . ARG D  1 114 ? -55.749 39.836  -28.018 1.00 36.56 ? 114 ARG B NH2   1 
ATOM   10114 N N     . ALA D  1 115 ? -52.420 41.477  -34.828 1.00 33.97 ? 115 ALA B N     1 
ATOM   10115 C CA    . ALA D  1 115 ? -53.388 41.061  -35.842 1.00 37.52 ? 115 ALA B CA    1 
ATOM   10116 C C     . ALA D  1 115 ? -52.762 40.084  -36.825 1.00 36.73 ? 115 ALA B C     1 
ATOM   10117 O O     . ALA D  1 115 ? -53.435 39.173  -37.316 1.00 40.07 ? 115 ALA B O     1 
ATOM   10118 C CB    . ALA D  1 115 ? -53.957 42.267  -36.588 1.00 31.31 ? 115 ALA B CB    1 
ATOM   10119 N N     . ALA D  1 116 ? -51.469 40.245  -37.104 1.00 34.45 ? 116 ALA B N     1 
ATOM   10120 C CA    . ALA D  1 116 ? -50.785 39.332  -38.014 1.00 37.05 ? 116 ALA B CA    1 
ATOM   10121 C C     . ALA D  1 116 ? -50.744 37.913  -37.455 1.00 42.38 ? 116 ALA B C     1 
ATOM   10122 O O     . ALA D  1 116 ? -51.055 36.946  -38.163 1.00 44.12 ? 116 ALA B O     1 
ATOM   10123 C CB    . ALA D  1 116 ? -49.372 39.836  -38.300 1.00 34.30 ? 116 ALA B CB    1 
ATOM   10124 N N     . ALA D  1 117 ? -50.331 37.760  -36.194 1.00 40.61 ? 117 ALA B N     1 
ATOM   10125 C CA    . ALA D  1 117 ? -50.311 36.425  -35.606 1.00 39.83 ? 117 ALA B CA    1 
ATOM   10126 C C     . ALA D  1 117 ? -51.692 35.790  -35.688 1.00 42.94 ? 117 ALA B C     1 
ATOM   10127 O O     . ALA D  1 117 ? -51.837 34.649  -36.142 1.00 44.51 ? 117 ALA B O     1 
ATOM   10128 C CB    . ALA D  1 117 ? -49.812 36.492  -34.163 1.00 37.54 ? 117 ALA B CB    1 
ATOM   10129 N N     . GLN D  1 118 ? -52.729 36.544  -35.321 1.00 46.24 ? 118 GLN B N     1 
ATOM   10130 C CA    . GLN D  1 118 ? -54.080 35.995  -35.334 1.00 49.73 ? 118 GLN B CA    1 
ATOM   10131 C C     . GLN D  1 118 ? -54.544 35.670  -36.745 1.00 49.40 ? 118 GLN B C     1 
ATOM   10132 O O     . GLN D  1 118 ? -55.404 34.800  -36.931 1.00 48.78 ? 118 GLN B O     1 
ATOM   10133 C CB    . GLN D  1 118 ? -55.060 36.972  -34.691 1.00 42.79 ? 118 GLN B CB    1 
ATOM   10134 C CG    . GLN D  1 118 ? -54.776 37.320  -33.271 1.00 39.10 ? 118 GLN B CG    1 
ATOM   10135 C CD    . GLN D  1 118 ? -55.752 38.360  -32.739 1.00 40.93 ? 118 GLN B CD    1 
ATOM   10136 O OE1   . GLN D  1 118 ? -55.580 39.564  -32.954 1.00 42.18 ? 118 GLN B OE1   1 
ATOM   10137 N NE2   . GLN D  1 118 ? -56.782 37.898  -32.044 1.00 38.79 ? 118 GLN B NE2   1 
ATOM   10138 N N     . LEU D  1 119 ? -54.019 36.380  -37.743 1.00 45.04 ? 119 LEU B N     1 
ATOM   10139 C CA    . LEU D  1 119 ? -54.370 36.066  -39.119 1.00 41.34 ? 119 LEU B CA    1 
ATOM   10140 C C     . LEU D  1 119 ? -53.886 34.676  -39.496 1.00 47.20 ? 119 LEU B C     1 
ATOM   10141 O O     . LEU D  1 119 ? -54.591 33.929  -40.182 1.00 46.16 ? 119 LEU B O     1 
ATOM   10142 C CB    . LEU D  1 119 ? -53.777 37.108  -40.051 1.00 37.46 ? 119 LEU B CB    1 
ATOM   10143 C CG    . LEU D  1 119 ? -54.113 36.916  -41.518 1.00 40.26 ? 119 LEU B CG    1 
ATOM   10144 C CD1   . LEU D  1 119 ? -55.604 36.657  -41.749 1.00 31.01 ? 119 LEU B CD1   1 
ATOM   10145 C CD2   . LEU D  1 119 ? -53.648 38.155  -42.226 1.00 36.07 ? 119 LEU B CD2   1 
ATOM   10146 N N     . THR D  1 120 ? -52.684 34.311  -39.045 1.00 50.79 ? 120 THR B N     1 
ATOM   10147 C CA    . THR D  1 120 ? -52.185 32.964  -39.293 1.00 49.95 ? 120 THR B CA    1 
ATOM   10148 C C     . THR D  1 120 ? -53.174 31.922  -38.787 1.00 51.60 ? 120 THR B C     1 
ATOM   10149 O O     . THR D  1 120 ? -53.491 30.960  -39.496 1.00 53.28 ? 120 THR B O     1 
ATOM   10150 C CB    . THR D  1 120 ? -50.794 32.766  -38.651 1.00 51.63 ? 120 THR B CB    1 
ATOM   10151 O OG1   . THR D  1 120 ? -50.890 32.719  -37.212 1.00 50.39 ? 120 THR B OG1   1 
ATOM   10152 C CG2   . THR D  1 120 ? -49.815 33.884  -39.076 1.00 39.61 ? 120 THR B CG2   1 
ATOM   10153 N N     . ARG D  1 121 ? -53.711 32.129  -37.579 1.00 52.94 ? 121 ARG B N     1 
ATOM   10154 C CA    . ARG D  1 121 ? -54.565 31.127  -36.959 1.00 52.87 ? 121 ARG B CA    1 
ATOM   10155 C C     . ARG D  1 121 ? -55.960 31.118  -37.584 1.00 50.65 ? 121 ARG B C     1 
ATOM   10156 O O     . ARG D  1 121 ? -56.490 30.048  -37.900 1.00 56.77 ? 121 ARG B O     1 
ATOM   10157 C CB    . ARG D  1 121 ? -54.605 31.358  -35.441 1.00 51.96 ? 121 ARG B CB    1 
ATOM   10158 C CG    . ARG D  1 121 ? -55.021 30.145  -34.617 1.00 51.24 ? 121 ARG B CG    1 
ATOM   10159 C CD    . ARG D  1 121 ? -54.167 28.912  -34.915 1.00 61.82 ? 121 ARG B CD    1 
ATOM   10160 N NE    . ARG D  1 121 ? -54.986 27.711  -35.076 1.00 64.48 ? 121 ARG B NE    1 
ATOM   10161 C CZ    . ARG D  1 121 ? -54.518 26.502  -35.367 1.00 63.08 ? 121 ARG B CZ    1 
ATOM   10162 N NH1   . ARG D  1 121 ? -53.221 26.276  -35.510 1.00 61.54 ? 121 ARG B NH1   1 
ATOM   10163 N NH2   . ARG D  1 121 ? -55.372 25.492  -35.510 1.00 66.44 ? 121 ARG B NH2   1 
ATOM   10164 N N     . LYS D  1 122 ? -56.554 32.287  -37.831 1.00 52.31 ? 122 LYS B N     1 
ATOM   10165 C CA    . LYS D  1 122 ? -57.869 32.322  -38.484 1.00 52.23 ? 122 LYS B CA    1 
ATOM   10166 C C     . LYS D  1 122 ? -57.836 31.748  -39.902 1.00 49.30 ? 122 LYS B C     1 
ATOM   10167 O O     . LYS D  1 122 ? -58.889 31.692  -40.551 1.00 49.44 ? 122 LYS B O     1 
ATOM   10168 C CB    . LYS D  1 122 ? -58.427 33.756  -38.530 1.00 54.12 ? 122 LYS B CB    1 
ATOM   10169 C CG    . LYS D  1 122 ? -58.649 34.389  -37.141 1.00 56.00 ? 122 LYS B CG    1 
ATOM   10170 C CD    . LYS D  1 122 ? -59.171 35.846  -37.187 1.00 62.05 ? 122 LYS B CD    1 
ATOM   10171 C CE    . LYS D  1 122 ? -60.705 35.968  -37.395 1.00 70.02 ? 122 LYS B CE    1 
ATOM   10172 N NZ    . LYS D  1 122 ? -61.265 37.382  -37.332 1.00 53.06 ? 122 LYS B NZ    1 
ATOM   10173 N N     . LEU D  1 123 ? -56.672 31.339  -40.394 1.00 48.74 ? 123 LEU B N     1 
ATOM   10174 C CA    . LEU D  1 123 ? -56.563 30.673  -41.681 1.00 50.67 ? 123 LEU B CA    1 
ATOM   10175 C C     . LEU D  1 123 ? -56.081 29.244  -41.558 1.00 52.95 ? 123 LEU B C     1 
ATOM   10176 O O     . LEU D  1 123 ? -56.109 28.519  -42.557 1.00 56.37 ? 123 LEU B O     1 
ATOM   10177 C CB    . LEU D  1 123 ? -55.610 31.449  -42.601 1.00 44.92 ? 123 LEU B CB    1 
ATOM   10178 C CG    . LEU D  1 123 ? -56.154 32.599  -43.451 1.00 45.34 ? 123 LEU B CG    1 
ATOM   10179 C CD1   . LEU D  1 123 ? -57.198 33.423  -42.712 1.00 49.83 ? 123 LEU B CD1   1 
ATOM   10180 C CD2   . LEU D  1 123 ? -54.998 33.494  -43.898 1.00 40.60 ? 123 LEU B CD2   1 
ATOM   10181 N N     . ASN D  1 124 ? -55.671 28.820  -40.359 1.00 50.04 ? 124 ASN B N     1 
ATOM   10182 C CA    . ASN D  1 124 ? -55.023 27.535  -40.152 1.00 50.46 ? 124 ASN B CA    1 
ATOM   10183 C C     . ASN D  1 124 ? -53.894 27.355  -41.160 1.00 54.14 ? 124 ASN B C     1 
ATOM   10184 O O     . ASN D  1 124 ? -53.792 26.344  -41.860 1.00 56.61 ? 124 ASN B O     1 
ATOM   10185 C CB    . ASN D  1 124 ? -56.028 26.384  -40.231 1.00 53.49 ? 124 ASN B CB    1 
ATOM   10186 C CG    . ASN D  1 124 ? -55.415 25.059  -39.806 1.00 59.30 ? 124 ASN B CG    1 
ATOM   10187 O OD1   . ASN D  1 124 ? -54.813 24.967  -38.738 1.00 66.73 ? 124 ASN B OD1   1 
ATOM   10188 N ND2   . ASN D  1 124 ? -55.523 24.042  -40.659 1.00 54.98 ? 124 ASN B ND2   1 
ATOM   10189 N N     . VAL D  1 125 ? -53.037 28.363  -41.244 1.00 52.27 ? 125 VAL B N     1 
ATOM   10190 C CA    . VAL D  1 125 ? -52.081 28.393  -42.341 1.00 53.49 ? 125 VAL B CA    1 
ATOM   10191 C C     . VAL D  1 125 ? -50.718 27.848  -41.892 1.00 56.33 ? 125 VAL B C     1 
ATOM   10192 O O     . VAL D  1 125 ? -50.390 26.684  -42.160 1.00 59.63 ? 125 VAL B O     1 
ATOM   10193 C CB    . VAL D  1 125 ? -52.044 29.814  -42.952 1.00 52.71 ? 125 VAL B CB    1 
ATOM   10194 C CG1   . VAL D  1 125 ? -51.701 30.891  -41.939 1.00 43.60 ? 125 VAL B CG1   1 
ATOM   10195 C CG2   . VAL D  1 125 ? -51.149 29.876  -44.141 1.00 50.44 ? 125 VAL B CG2   1 
ATOM   10196 N N     . ALA D  1 126 ? -49.915 28.658  -41.204 1.00 52.32 ? 126 ALA B N     1 
ATOM   10197 C CA    . ALA D  1 126 ? -48.655 28.207  -40.616 1.00 42.74 ? 126 ALA B CA    1 
ATOM   10198 C C     . ALA D  1 126 ? -48.372 29.147  -39.464 1.00 42.31 ? 126 ALA B C     1 
ATOM   10199 O O     . ALA D  1 126 ? -48.549 30.365  -39.604 1.00 38.74 ? 126 ALA B O     1 
ATOM   10200 C CB    . ALA D  1 126 ? -47.502 28.214  -41.624 1.00 35.04 ? 126 ALA B CB    1 
ATOM   10201 N N     . ALA D  1 127 ? -47.989 28.587  -38.324 1.00 39.69 ? 127 ALA B N     1 
ATOM   10202 C CA    . ALA D  1 127 ? -47.893 29.392  -37.116 1.00 38.18 ? 127 ALA B CA    1 
ATOM   10203 C C     . ALA D  1 127 ? -46.752 30.378  -37.259 1.00 33.66 ? 127 ALA B C     1 
ATOM   10204 O O     . ALA D  1 127 ? -45.621 29.993  -37.563 1.00 31.19 ? 127 ALA B O     1 
ATOM   10205 C CB    . ALA D  1 127 ? -47.687 28.508  -35.886 1.00 41.35 ? 127 ALA B CB    1 
ATOM   10206 N N     . LEU D  1 128 ? -47.071 31.651  -37.080 1.00 37.34 ? 128 LEU B N     1 
ATOM   10207 C CA    . LEU D  1 128 ? -46.064 32.694  -37.062 1.00 33.03 ? 128 LEU B CA    1 
ATOM   10208 C C     . LEU D  1 128 ? -45.015 32.382  -35.999 1.00 40.51 ? 128 LEU B C     1 
ATOM   10209 O O     . LEU D  1 128 ? -45.354 32.117  -34.841 1.00 40.89 ? 128 LEU B O     1 
ATOM   10210 C CB    . LEU D  1 128 ? -46.735 34.023  -36.759 1.00 35.03 ? 128 LEU B CB    1 
ATOM   10211 C CG    . LEU D  1 128 ? -45.844 35.203  -37.053 1.00 35.97 ? 128 LEU B CG    1 
ATOM   10212 C CD1   . LEU D  1 128 ? -45.594 35.195  -38.548 1.00 36.85 ? 128 LEU B CD1   1 
ATOM   10213 C CD2   . LEU D  1 128 ? -46.486 36.487  -36.573 1.00 34.37 ? 128 LEU B CD2   1 
ATOM   10214 N N     . ASP D  1 129 ? -43.741 32.395  -36.399 1.00 42.43 ? 129 ASP B N     1 
ATOM   10215 C CA    . ASP D  1 129 ? -42.648 32.269  -35.445 1.00 36.93 ? 129 ASP B CA    1 
ATOM   10216 C C     . ASP D  1 129 ? -42.580 33.480  -34.535 1.00 38.72 ? 129 ASP B C     1 
ATOM   10217 O O     . ASP D  1 129 ? -42.644 34.626  -34.995 1.00 36.69 ? 129 ASP B O     1 
ATOM   10218 C CB    . ASP D  1 129 ? -41.312 32.090  -36.155 1.00 37.27 ? 129 ASP B CB    1 
ATOM   10219 C CG    . ASP D  1 129 ? -40.350 31.260  -35.343 1.00 44.49 ? 129 ASP B CG    1 
ATOM   10220 O OD1   . ASP D  1 129 ? -40.801 30.722  -34.288 1.00 36.11 ? 129 ASP B OD1   1 
ATOM   10221 O OD2   . ASP D  1 129 ? -39.171 31.130  -35.771 1.00 43.31 ? 129 ASP B OD2   1 
ATOM   10222 N N     . GLY D  1 130 ? -42.402 33.209  -33.239 1.00 37.11 ? 130 GLY B N     1 
ATOM   10223 C CA    . GLY D  1 130 ? -42.541 34.243  -32.232 1.00 37.78 ? 130 GLY B CA    1 
ATOM   10224 C C     . GLY D  1 130 ? -43.988 34.582  -31.942 1.00 36.39 ? 130 GLY B C     1 
ATOM   10225 O O     . GLY D  1 130 ? -44.302 35.729  -31.602 1.00 37.02 ? 130 GLY B O     1 
ATOM   10226 N N     . TYR D  1 131 ? -44.880 33.599  -32.075 1.00 30.50 ? 131 TYR B N     1 
ATOM   10227 C CA    . TYR D  1 131 ? -46.312 33.855  -31.982 1.00 38.75 ? 131 TYR B CA    1 
ATOM   10228 C C     . TYR D  1 131 ? -46.668 34.535  -30.666 1.00 39.07 ? 131 TYR B C     1 
ATOM   10229 O O     . TYR D  1 131 ? -47.300 35.598  -30.642 1.00 35.93 ? 131 TYR B O     1 
ATOM   10230 C CB    . TYR D  1 131 ? -47.070 32.537  -32.125 1.00 38.52 ? 131 TYR B CB    1 
ATOM   10231 C CG    . TYR D  1 131 ? -48.562 32.701  -32.145 1.00 37.72 ? 131 TYR B CG    1 
ATOM   10232 C CD1   . TYR D  1 131 ? -49.208 33.197  -33.269 1.00 45.48 ? 131 TYR B CD1   1 
ATOM   10233 C CD2   . TYR D  1 131 ? -49.333 32.361  -31.042 1.00 42.64 ? 131 TYR B CD2   1 
ATOM   10234 C CE1   . TYR D  1 131 ? -50.598 33.351  -33.298 1.00 47.91 ? 131 TYR B CE1   1 
ATOM   10235 C CE2   . TYR D  1 131 ? -50.720 32.514  -31.060 1.00 45.69 ? 131 TYR B CE2   1 
ATOM   10236 C CZ    . TYR D  1 131 ? -51.342 33.013  -32.191 1.00 46.30 ? 131 TYR B CZ    1 
ATOM   10237 O OH    . TYR D  1 131 ? -52.703 33.166  -32.220 1.00 46.70 ? 131 TYR B OH    1 
ATOM   10238 N N     . GLU D  1 132 ? -46.255 33.938  -29.558 1.00 40.16 ? 132 GLU B N     1 
ATOM   10239 C CA    . GLU D  1 132 ? -46.672 34.444  -28.263 1.00 35.27 ? 132 GLU B CA    1 
ATOM   10240 C C     . GLU D  1 132 ? -46.141 35.844  -28.015 1.00 34.26 ? 132 GLU B C     1 
ATOM   10241 O O     . GLU D  1 132 ? -46.877 36.721  -27.549 1.00 35.29 ? 132 GLU B O     1 
ATOM   10242 C CB    . GLU D  1 132 ? -46.216 33.483  -27.177 1.00 27.38 ? 132 GLU B CB    1 
ATOM   10243 C CG    . GLU D  1 132 ? -47.171 32.339  -27.078 1.00 34.66 ? 132 GLU B CG    1 
ATOM   10244 C CD    . GLU D  1 132 ? -48.635 32.799  -27.125 1.00 51.10 ? 132 GLU B CD    1 
ATOM   10245 O OE1   . GLU D  1 132 ? -48.978 33.881  -26.566 1.00 53.97 ? 132 GLU B OE1   1 
ATOM   10246 O OE2   . GLU D  1 132 ? -49.444 32.082  -27.764 1.00 49.41 ? 132 GLU B OE2   1 
ATOM   10247 N N     . PHE D  1 133 ? -44.868 36.068  -28.320 1.00 32.57 ? 133 PHE B N     1 
ATOM   10248 C CA    . PHE D  1 133 ? -44.307 37.401  -28.189 1.00 27.30 ? 133 PHE B CA    1 
ATOM   10249 C C     . PHE D  1 133 ? -45.141 38.399  -28.972 1.00 34.06 ? 133 PHE B C     1 
ATOM   10250 O O     . PHE D  1 133 ? -45.539 39.449  -28.450 1.00 35.37 ? 133 PHE B O     1 
ATOM   10251 C CB    . PHE D  1 133 ? -42.861 37.384  -28.681 1.00 26.41 ? 133 PHE B CB    1 
ATOM   10252 C CG    . PHE D  1 133 ? -42.185 38.708  -28.627 1.00 27.09 ? 133 PHE B CG    1 
ATOM   10253 C CD1   . PHE D  1 133 ? -42.125 39.418  -27.451 1.00 23.53 ? 133 PHE B CD1   1 
ATOM   10254 C CD2   . PHE D  1 133 ? -41.595 39.240  -29.755 1.00 26.45 ? 133 PHE B CD2   1 
ATOM   10255 C CE1   . PHE D  1 133 ? -41.488 40.620  -27.412 1.00 25.48 ? 133 PHE B CE1   1 
ATOM   10256 C CE2   . PHE D  1 133 ? -40.973 40.461  -29.719 1.00 23.90 ? 133 PHE B CE2   1 
ATOM   10257 C CZ    . PHE D  1 133 ? -40.910 41.149  -28.555 1.00 24.27 ? 133 PHE B CZ    1 
ATOM   10258 N N     . ALA D  1 134 ? -45.453 38.063  -30.224 1.00 32.21 ? 134 ALA B N     1 
ATOM   10259 C CA    . ALA D  1 134 ? -46.200 38.982  -31.062 1.00 30.96 ? 134 ALA B CA    1 
ATOM   10260 C C     . ALA D  1 134 ? -47.593 39.200  -30.509 1.00 35.86 ? 134 ALA B C     1 
ATOM   10261 O O     . ALA D  1 134 ? -48.142 40.302  -30.619 1.00 38.08 ? 134 ALA B O     1 
ATOM   10262 C CB    . ALA D  1 134 ? -46.270 38.449  -32.491 1.00 32.90 ? 134 ALA B CB    1 
ATOM   10263 N N     . MET D  1 135 ? -48.174 38.162  -29.907 1.00 34.78 ? 135 MET B N     1 
ATOM   10264 C CA    . MET D  1 135 ? -49.522 38.277  -29.367 1.00 32.84 ? 135 MET B CA    1 
ATOM   10265 C C     . MET D  1 135 ? -49.583 39.316  -28.257 1.00 32.00 ? 135 MET B C     1 
ATOM   10266 O O     . MET D  1 135 ? -50.598 39.999  -28.108 1.00 35.08 ? 135 MET B O     1 
ATOM   10267 C CB    . MET D  1 135 ? -49.996 36.913  -28.867 1.00 34.04 ? 135 MET B CB    1 
ATOM   10268 C CG    . MET D  1 135 ? -50.798 36.063  -29.897 1.00 43.13 ? 135 MET B CG    1 
ATOM   10269 S SD    . MET D  1 135 ? -51.966 36.887  -31.035 1.00 39.19 ? 135 MET B SD    1 
ATOM   10270 C CE    . MET D  1 135 ? -53.491 36.618  -30.133 1.00 33.90 ? 135 MET B CE    1 
ATOM   10271 N N     . GLN D  1 136 ? -48.505 39.475  -27.493 1.00 29.49 ? 136 GLN B N     1 
ATOM   10272 C CA    . GLN D  1 136 ? -48.454 40.459  -26.421 1.00 32.96 ? 136 GLN B CA    1 
ATOM   10273 C C     . GLN D  1 136 ? -48.012 41.845  -26.898 1.00 33.20 ? 136 GLN B C     1 
ATOM   10274 O O     . GLN D  1 136 ? -47.562 42.656  -26.079 1.00 25.69 ? 136 GLN B O     1 
ATOM   10275 C CB    . GLN D  1 136 ? -47.536 39.956  -25.310 1.00 29.99 ? 136 GLN B CB    1 
ATOM   10276 C CG    . GLN D  1 136 ? -48.058 38.686  -24.629 1.00 30.71 ? 136 GLN B CG    1 
ATOM   10277 C CD    . GLN D  1 136 ? -49.430 38.857  -23.967 1.00 26.47 ? 136 GLN B CD    1 
ATOM   10278 O OE1   . GLN D  1 136 ? -49.803 39.937  -23.524 1.00 31.07 ? 136 GLN B OE1   1 
ATOM   10279 N NE2   . GLN D  1 136 ? -50.167 37.777  -23.878 1.00 29.45 ? 136 GLN B NE2   1 
ATOM   10280 N N     . ASN D  1 137 ? -48.149 42.134  -28.195 1.00 30.06 ? 137 ASN B N     1 
ATOM   10281 C CA    . ASN D  1 137 ? -47.706 43.400  -28.778 1.00 32.70 ? 137 ASN B CA    1 
ATOM   10282 C C     . ASN D  1 137 ? -46.215 43.654  -28.511 1.00 34.20 ? 137 ASN B C     1 
ATOM   10283 O O     . ASN D  1 137 ? -45.804 44.776  -28.208 1.00 30.28 ? 137 ASN B O     1 
ATOM   10284 C CB    . ASN D  1 137 ? -48.563 44.563  -28.275 1.00 34.90 ? 137 ASN B CB    1 
ATOM   10285 C CG    . ASN D  1 137 ? -50.043 44.298  -28.442 1.00 35.04 ? 137 ASN B CG    1 
ATOM   10286 O OD1   . ASN D  1 137 ? -50.481 43.873  -29.511 1.00 39.80 ? 137 ASN B OD1   1 
ATOM   10287 N ND2   . ASN D  1 137 ? -50.822 44.551  -27.394 1.00 32.90 ? 137 ASN B ND2   1 
ATOM   10288 N N     . GLY D  1 138 ? -45.398 42.604  -28.681 1.00 31.22 ? 138 GLY B N     1 
ATOM   10289 C CA    . GLY D  1 138 ? -44.002 42.692  -28.314 1.00 28.71 ? 138 GLY B CA    1 
ATOM   10290 C C     . GLY D  1 138 ? -43.177 43.538  -29.261 1.00 33.64 ? 138 GLY B C     1 
ATOM   10291 O O     . GLY D  1 138 ? -42.242 44.237  -28.838 1.00 31.03 ? 138 GLY B O     1 
ATOM   10292 N N     . ILE D  1 139 ? -43.458 43.446  -30.560 1.00 37.09 ? 139 ILE B N     1 
ATOM   10293 C CA    . ILE D  1 139 ? -42.529 44.072  -31.491 1.00 36.42 ? 139 ILE B CA    1 
ATOM   10294 C C     . ILE D  1 139 ? -42.624 45.593  -31.444 1.00 37.80 ? 139 ILE B C     1 
ATOM   10295 O O     . ILE D  1 139 ? -41.682 46.284  -31.866 1.00 34.24 ? 139 ILE B O     1 
ATOM   10296 C CB    . ILE D  1 139 ? -42.746 43.596  -32.918 1.00 40.44 ? 139 ILE B CB    1 
ATOM   10297 C CG1   . ILE D  1 139 ? -44.156 43.933  -33.358 1.00 45.96 ? 139 ILE B CG1   1 
ATOM   10298 C CG2   . ILE D  1 139 ? -42.547 42.067  -32.980 1.00 38.09 ? 139 ILE B CG2   1 
ATOM   10299 C CD1   . ILE D  1 139 ? -44.507 43.255  -34.616 1.00 42.02 ? 139 ILE B CD1   1 
ATOM   10300 N N     . ASP D  1 140 ? -43.738 46.133  -30.929 1.00 39.71 ? 140 ASP B N     1 
ATOM   10301 C CA    . ASP D  1 140 ? -43.870 47.569  -30.702 1.00 36.95 ? 140 ASP B CA    1 
ATOM   10302 C C     . ASP D  1 140 ? -43.198 48.003  -29.417 1.00 36.71 ? 140 ASP B C     1 
ATOM   10303 O O     . ASP D  1 140 ? -42.871 49.189  -29.272 1.00 37.45 ? 140 ASP B O     1 
ATOM   10304 C CB    . ASP D  1 140 ? -45.339 47.953  -30.678 1.00 34.82 ? 140 ASP B CB    1 
ATOM   10305 C CG    . ASP D  1 140 ? -46.145 47.103  -31.638 1.00 53.30 ? 140 ASP B CG    1 
ATOM   10306 O OD1   . ASP D  1 140 ? -45.901 47.192  -32.874 1.00 55.79 ? 140 ASP B OD1   1 
ATOM   10307 O OD2   . ASP D  1 140 ? -46.969 46.290  -31.155 1.00 49.62 ? 140 ASP B OD2   1 
ATOM   10308 N N     . LEU D  1 141 ? -42.951 47.075  -28.493 1.00 31.86 ? 141 LEU B N     1 
ATOM   10309 C CA    . LEU D  1 141 ? -42.001 47.401  -27.441 1.00 34.59 ? 141 LEU B CA    1 
ATOM   10310 C C     . LEU D  1 141 ? -40.647 47.710  -28.064 1.00 32.91 ? 141 LEU B C     1 
ATOM   10311 O O     . LEU D  1 141 ? -40.061 48.765  -27.809 1.00 35.15 ? 141 LEU B O     1 
ATOM   10312 C CB    . LEU D  1 141 ? -41.905 46.277  -26.413 1.00 32.05 ? 141 LEU B CB    1 
ATOM   10313 C CG    . LEU D  1 141 ? -40.820 46.547  -25.356 1.00 30.35 ? 141 LEU B CG    1 
ATOM   10314 C CD1   . LEU D  1 141 ? -40.889 47.958  -24.777 1.00 22.95 ? 141 LEU B CD1   1 
ATOM   10315 C CD2   . LEU D  1 141 ? -40.885 45.526  -24.248 1.00 28.23 ? 141 LEU B CD2   1 
ATOM   10316 N N     . LEU D  1 142 ? -40.177 46.841  -28.949 1.00 37.50 ? 142 LEU B N     1 
ATOM   10317 C CA    . LEU D  1 142 ? -39.134 47.223  -29.889 1.00 36.75 ? 142 LEU B CA    1 
ATOM   10318 C C     . LEU D  1 142 ? -39.711 48.310  -30.793 1.00 35.05 ? 142 LEU B C     1 
ATOM   10319 O O     . LEU D  1 142 ? -40.808 48.832  -30.579 1.00 39.18 ? 142 LEU B O     1 
ATOM   10320 C CB    . LEU D  1 142 ? -38.656 45.997  -30.654 1.00 34.75 ? 142 LEU B CB    1 
ATOM   10321 C CG    . LEU D  1 142 ? -38.653 44.782  -29.726 1.00 31.57 ? 142 LEU B CG    1 
ATOM   10322 C CD1   . LEU D  1 142 ? -38.292 43.502  -30.447 1.00 34.13 ? 142 LEU B CD1   1 
ATOM   10323 C CD2   . LEU D  1 142 ? -37.670 45.033  -28.623 1.00 30.13 ? 142 LEU B CD2   1 
ATOM   10324 N N     . ASN D  1 143 ? -38.990 48.702  -31.806 1.00 31.29 ? 143 ASN B N     1 
ATOM   10325 C CA    . ASN D  1 143 ? -39.483 49.761  -32.679 1.00 37.80 ? 143 ASN B CA    1 
ATOM   10326 C C     . ASN D  1 143 ? -39.834 51.024  -31.901 1.00 32.62 ? 143 ASN B C     1 
ATOM   10327 O O     . ASN D  1 143 ? -40.527 51.891  -32.423 1.00 37.52 ? 143 ASN B O     1 
ATOM   10328 C CB    . ASN D  1 143 ? -40.696 49.305  -33.517 1.00 31.25 ? 143 ASN B CB    1 
ATOM   10329 C CG    . ASN D  1 143 ? -40.374 48.114  -34.439 1.00 35.61 ? 143 ASN B CG    1 
ATOM   10330 O OD1   . ASN D  1 143 ? -39.216 47.663  -34.541 1.00 33.58 ? 143 ASN B OD1   1 
ATOM   10331 N ND2   . ASN D  1 143 ? -41.409 47.568  -35.073 1.00 29.98 ? 143 ASN B ND2   1 
ATOM   10332 N N     . MET D  1 144 ? -39.422 51.118  -30.640 1.00 33.76 ? 144 MET B N     1 
ATOM   10333 C CA    . MET D  1 144 ? -39.369 52.378  -29.920 1.00 35.50 ? 144 MET B CA    1 
ATOM   10334 C C     . MET D  1 144 ? -37.908 52.733  -29.717 1.00 32.04 ? 144 MET B C     1 
ATOM   10335 O O     . MET D  1 144 ? -37.104 51.871  -29.336 1.00 31.21 ? 144 MET B O     1 
ATOM   10336 C CB    . MET D  1 144 ? -40.084 52.313  -28.561 1.00 32.28 ? 144 MET B CB    1 
ATOM   10337 C CG    . MET D  1 144 ? -41.549 51.937  -28.631 1.00 35.12 ? 144 MET B CG    1 
ATOM   10338 S SD    . MET D  1 144 ? -42.240 51.383  -27.052 1.00 37.54 ? 144 MET B SD    1 
ATOM   10339 C CE    . MET D  1 144 ? -42.486 52.927  -26.195 1.00 31.73 ? 144 MET B CE    1 
ATOM   10340 N N     . LYS D  1 145 ? -37.569 53.998  -29.972 1.00 32.07 ? 145 LYS B N     1 
ATOM   10341 C CA    . LYS D  1 145 ? -36.199 54.450  -29.758 1.00 28.87 ? 145 LYS B CA    1 
ATOM   10342 C C     . LYS D  1 145 ? -35.836 54.417  -28.278 1.00 31.69 ? 145 LYS B C     1 
ATOM   10343 O O     . LYS D  1 145 ? -34.700 54.083  -27.907 1.00 27.43 ? 145 LYS B O     1 
ATOM   10344 C CB    . LYS D  1 145 ? -36.030 55.850  -30.327 1.00 27.73 ? 145 LYS B CB    1 
ATOM   10345 C CG    . LYS D  1 145 ? -36.561 55.979  -31.742 1.00 35.80 ? 145 LYS B CG    1 
ATOM   10346 C CD    . LYS D  1 145 ? -35.524 55.517  -32.760 1.00 36.96 ? 145 LYS B CD    1 
ATOM   10347 C CE    . LYS D  1 145 ? -35.815 56.025  -34.155 1.00 33.46 ? 145 LYS B CE    1 
ATOM   10348 N NZ    . LYS D  1 145 ? -37.278 55.982  -34.460 1.00 34.56 ? 145 LYS B NZ    1 
ATOM   10349 N N     . SER D  1 146 ? -36.788 54.770  -27.414 1.00 29.10 ? 146 SER B N     1 
ATOM   10350 C CA    . SER D  1 146 ? -36.525 54.687  -25.987 1.00 27.56 ? 146 SER B CA    1 
ATOM   10351 C C     . SER D  1 146 ? -36.186 53.262  -25.594 1.00 28.42 ? 146 SER B C     1 
ATOM   10352 O O     . SER D  1 146 ? -35.300 53.027  -24.765 1.00 27.32 ? 146 SER B O     1 
ATOM   10353 C CB    . SER D  1 146 ? -37.729 55.185  -25.215 1.00 24.82 ? 146 SER B CB    1 
ATOM   10354 O OG    . SER D  1 146 ? -38.893 54.551  -25.702 1.00 31.65 ? 146 SER B OG    1 
ATOM   10355 N N     . THR D  1 147 ? -36.850 52.289  -26.208 1.00 24.74 ? 147 THR B N     1 
ATOM   10356 C CA    . THR D  1 147 ? -36.491 50.916  -25.906 1.00 27.18 ? 147 THR B CA    1 
ATOM   10357 C C     . THR D  1 147 ? -35.054 50.629  -26.293 1.00 28.17 ? 147 THR B C     1 
ATOM   10358 O O     . THR D  1 147 ? -34.316 49.979  -25.543 1.00 27.63 ? 147 THR B O     1 
ATOM   10359 C CB    . THR D  1 147 ? -37.428 49.957  -26.611 1.00 24.71 ? 147 THR B CB    1 
ATOM   10360 O OG1   . THR D  1 147 ? -38.756 50.167  -26.133 1.00 33.07 ? 147 THR B OG1   1 
ATOM   10361 C CG2   . THR D  1 147 ? -37.030 48.558  -26.294 1.00 25.81 ? 147 THR B CG2   1 
ATOM   10362 N N     . PHE D  1 148 ? -34.631 51.121  -27.452 1.00 28.01 ? 148 PHE B N     1 
ATOM   10363 C CA    . PHE D  1 148 ? -33.300 50.764  -27.929 1.00 29.45 ? 148 PHE B CA    1 
ATOM   10364 C C     . PHE D  1 148 ? -32.219 51.361  -27.050 1.00 26.74 ? 148 PHE B C     1 
ATOM   10365 O O     . PHE D  1 148 ? -31.249 50.681  -26.716 1.00 31.11 ? 148 PHE B O     1 
ATOM   10366 C CB    . PHE D  1 148 ? -33.097 51.201  -29.377 1.00 29.98 ? 148 PHE B CB    1 
ATOM   10367 C CG    . PHE D  1 148 ? -31.706 50.958  -29.855 1.00 29.78 ? 148 PHE B CG    1 
ATOM   10368 C CD1   . PHE D  1 148 ? -31.316 49.683  -30.245 1.00 29.26 ? 148 PHE B CD1   1 
ATOM   10369 C CD2   . PHE D  1 148 ? -30.774 51.983  -29.872 1.00 28.54 ? 148 PHE B CD2   1 
ATOM   10370 C CE1   . PHE D  1 148 ? -30.037 49.430  -30.660 1.00 30.92 ? 148 PHE B CE1   1 
ATOM   10371 C CE2   . PHE D  1 148 ? -29.475 51.745  -30.276 1.00 31.35 ? 148 PHE B CE2   1 
ATOM   10372 C CZ    . PHE D  1 148 ? -29.105 50.461  -30.676 1.00 34.68 ? 148 PHE B CZ    1 
ATOM   10373 N N     . ARG D  1 149 ? -32.370 52.627  -26.659 1.00 27.75 ? 149 ARG B N     1 
ATOM   10374 C CA    . ARG D  1 149 ? -31.382 53.253  -25.774 1.00 32.28 ? 149 ARG B CA    1 
ATOM   10375 C C     . ARG D  1 149 ? -31.319 52.575  -24.421 1.00 32.17 ? 149 ARG B C     1 
ATOM   10376 O O     . ARG D  1 149 ? -30.234 52.396  -23.862 1.00 36.85 ? 149 ARG B O     1 
ATOM   10377 C CB    . ARG D  1 149 ? -31.697 54.724  -25.584 1.00 31.00 ? 149 ARG B CB    1 
ATOM   10378 C CG    . ARG D  1 149 ? -31.649 55.413  -26.888 1.00 33.36 ? 149 ARG B CG    1 
ATOM   10379 C CD    . ARG D  1 149 ? -31.266 56.863  -26.759 1.00 35.58 ? 149 ARG B CD    1 
ATOM   10380 N NE    . ARG D  1 149 ? -30.103 56.944  -25.874 1.00 32.16 ? 149 ARG B NE    1 
ATOM   10381 C CZ    . ARG D  1 149 ? -28.976 57.600  -26.168 1.00 30.64 ? 149 ARG B CZ    1 
ATOM   10382 N NH1   . ARG D  1 149 ? -28.622 57.861  -27.431 1.00 32.40 ? 149 ARG B NH1   1 
ATOM   10383 N NH2   . ARG D  1 149 ? -28.114 57.901  -25.183 1.00 31.73 ? 149 ARG B NH2   1 
ATOM   10384 N N     . ARG D  1 150 ? -32.467 52.220  -23.869 1.00 30.98 ? 150 ARG B N     1 
ATOM   10385 C CA    . ARG D  1 150 ? -32.500 51.448  -22.640 1.00 25.93 ? 150 ARG B CA    1 
ATOM   10386 C C     . ARG D  1 150 ? -31.721 50.156  -22.817 1.00 25.03 ? 150 ARG B C     1 
ATOM   10387 O O     . ARG D  1 150 ? -30.642 49.993  -22.242 1.00 28.02 ? 150 ARG B O     1 
ATOM   10388 C CB    . ARG D  1 150 ? -33.950 51.184  -22.254 1.00 29.10 ? 150 ARG B CB    1 
ATOM   10389 C CG    . ARG D  1 150 ? -34.654 52.437  -21.797 1.00 30.22 ? 150 ARG B CG    1 
ATOM   10390 C CD    . ARG D  1 150 ? -36.159 52.302  -21.899 1.00 27.92 ? 150 ARG B CD    1 
ATOM   10391 N NE    . ARG D  1 150 ? -36.792 53.040  -20.819 1.00 30.48 ? 150 ARG B NE    1 
ATOM   10392 C CZ    . ARG D  1 150 ? -38.098 53.184  -20.653 1.00 25.91 ? 150 ARG B CZ    1 
ATOM   10393 N NH1   . ARG D  1 150 ? -38.967 52.680  -21.508 1.00 23.33 ? 150 ARG B NH1   1 
ATOM   10394 N NH2   . ARG D  1 150 ? -38.542 53.859  -19.598 1.00 26.08 ? 150 ARG B NH2   1 
ATOM   10395 N N     . LEU D  1 151 ? -32.238 49.257  -23.654 1.00 29.76 ? 151 LEU B N     1 
ATOM   10396 C CA    . LEU D  1 151 ? -31.581 47.975  -23.905 1.00 31.25 ? 151 LEU B CA    1 
ATOM   10397 C C     . LEU D  1 151 ? -30.133 48.104  -24.336 1.00 32.97 ? 151 LEU B C     1 
ATOM   10398 O O     . LEU D  1 151 ? -29.336 47.198  -24.066 1.00 33.30 ? 151 LEU B O     1 
ATOM   10399 C CB    . LEU D  1 151 ? -32.315 47.215  -24.989 1.00 21.69 ? 151 LEU B CB    1 
ATOM   10400 C CG    . LEU D  1 151 ? -33.718 46.807  -24.632 1.00 25.89 ? 151 LEU B CG    1 
ATOM   10401 C CD1   . LEU D  1 151 ? -34.388 46.334  -25.888 1.00 26.14 ? 151 LEU B CD1   1 
ATOM   10402 C CD2   . LEU D  1 151 ? -33.698 45.715  -23.576 1.00 24.87 ? 151 LEU B CD2   1 
ATOM   10403 N N     . ALA D  1 152 ? -29.757 49.200  -25.003 1.00 28.78 ? 152 ALA B N     1 
ATOM   10404 C CA    . ALA D  1 152 ? -28.372 49.290  -25.438 1.00 31.46 ? 152 ALA B CA    1 
ATOM   10405 C C     . ALA D  1 152 ? -27.476 49.845  -24.344 1.00 33.93 ? 152 ALA B C     1 
ATOM   10406 O O     . ALA D  1 152 ? -26.284 49.520  -24.299 1.00 33.02 ? 152 ALA B O     1 
ATOM   10407 C CB    . ALA D  1 152 ? -28.268 50.142  -26.706 1.00 33.29 ? 152 ALA B CB    1 
ATOM   10408 N N     . ALA D  1 153 ? -28.025 50.676  -23.459 1.00 31.76 ? 153 ALA B N     1 
ATOM   10409 C CA    . ALA D  1 153 ? -27.200 51.276  -22.426 1.00 29.77 ? 153 ALA B CA    1 
ATOM   10410 C C     . ALA D  1 153 ? -26.768 50.257  -21.382 1.00 32.40 ? 153 ALA B C     1 
ATOM   10411 O O     . ALA D  1 153 ? -25.689 50.402  -20.808 1.00 33.10 ? 153 ALA B O     1 
ATOM   10412 C CB    . ALA D  1 153 ? -27.952 52.420  -21.757 1.00 34.74 ? 153 ALA B CB    1 
ATOM   10413 N N     . GLY D  1 154 ? -27.577 49.229  -21.121 1.00 29.96 ? 154 GLY B N     1 
ATOM   10414 C CA    . GLY D  1 154 ? -27.249 48.275  -20.077 1.00 34.12 ? 154 GLY B CA    1 
ATOM   10415 C C     . GLY D  1 154 ? -26.514 47.057  -20.593 1.00 30.87 ? 154 GLY B C     1 
ATOM   10416 O O     . GLY D  1 154 ? -25.695 46.477  -19.883 1.00 34.10 ? 154 GLY B O     1 
ATOM   10417 N N     . LEU D  1 155 ? -26.817 46.649  -21.823 1.00 31.95 ? 155 LEU B N     1 
ATOM   10418 C CA    . LEU D  1 155 ? -26.016 45.624  -22.481 1.00 33.27 ? 155 LEU B CA    1 
ATOM   10419 C C     . LEU D  1 155 ? -24.621 46.134  -22.755 1.00 33.42 ? 155 LEU B C     1 
ATOM   10420 O O     . LEU D  1 155 ? -23.650 45.378  -22.675 1.00 36.87 ? 155 LEU B O     1 
ATOM   10421 C CB    . LEU D  1 155 ? -26.642 45.214  -23.808 1.00 35.53 ? 155 LEU B CB    1 
ATOM   10422 C CG    . LEU D  1 155 ? -25.880 44.074  -24.471 1.00 35.00 ? 155 LEU B CG    1 
ATOM   10423 C CD1   . LEU D  1 155 ? -25.880 42.884  -23.525 1.00 33.42 ? 155 LEU B CD1   1 
ATOM   10424 C CD2   . LEU D  1 155 ? -26.446 43.705  -25.843 1.00 34.93 ? 155 LEU B CD2   1 
ATOM   10425 N N     . GLY D  1 156 ? -24.510 47.409  -23.109 1.00 33.04 ? 156 GLY B N     1 
ATOM   10426 C CA    . GLY D  1 156 ? -23.240 48.045  -23.365 1.00 27.51 ? 156 GLY B CA    1 
ATOM   10427 C C     . GLY D  1 156 ? -23.061 48.498  -24.795 1.00 31.55 ? 156 GLY B C     1 
ATOM   10428 O O     . GLY D  1 156 ? -22.057 49.157  -25.100 1.00 36.64 ? 156 GLY B O     1 
ATOM   10429 N N     . THR D  1 157 ? -23.988 48.164  -25.679 1.00 31.91 ? 157 THR B N     1 
ATOM   10430 C CA    . THR D  1 157 ? -23.932 48.597  -27.071 1.00 34.95 ? 157 THR B CA    1 
ATOM   10431 C C     . THR D  1 157 ? -23.498 50.061  -27.123 1.00 31.71 ? 157 THR B C     1 
ATOM   10432 O O     . THR D  1 157 ? -23.973 50.867  -26.316 1.00 36.64 ? 157 THR B O     1 
ATOM   10433 C CB    . THR D  1 157 ? -25.294 48.362  -27.717 1.00 27.32 ? 157 THR B CB    1 
ATOM   10434 O OG1   . THR D  1 157 ? -25.689 47.012  -27.446 1.00 29.96 ? 157 THR B OG1   1 
ATOM   10435 C CG2   . THR D  1 157 ? -25.251 48.591  -29.231 1.00 29.68 ? 157 THR B CG2   1 
ATOM   10436 N N     . PRO D  1 158 ? -22.535 50.423  -27.969 1.00 28.68 ? 158 PRO B N     1 
ATOM   10437 C CA    . PRO D  1 158 ? -22.088 51.825  -28.020 1.00 34.53 ? 158 PRO B CA    1 
ATOM   10438 C C     . PRO D  1 158 ? -23.230 52.722  -28.447 1.00 32.74 ? 158 PRO B C     1 
ATOM   10439 O O     . PRO D  1 158 ? -23.876 52.476  -29.460 1.00 34.38 ? 158 PRO B O     1 
ATOM   10440 C CB    . PRO D  1 158 ? -20.964 51.817  -29.069 1.00 34.49 ? 158 PRO B CB    1 
ATOM   10441 C CG    . PRO D  1 158 ? -21.187 50.537  -29.873 1.00 34.97 ? 158 PRO B CG    1 
ATOM   10442 C CD    . PRO D  1 158 ? -21.772 49.554  -28.885 1.00 32.63 ? 158 PRO B CD    1 
ATOM   10443 N N     . LEU D  1 159 ? -23.499 53.755  -27.657 1.00 34.71 ? 159 LEU B N     1 
ATOM   10444 C CA    . LEU D  1 159 ? -24.596 54.667  -27.946 1.00 32.99 ? 159 LEU B CA    1 
ATOM   10445 C C     . LEU D  1 159 ? -24.064 56.084  -27.971 1.00 32.46 ? 159 LEU B C     1 
ATOM   10446 O O     . LEU D  1 159 ? -23.084 56.403  -27.299 1.00 37.45 ? 159 LEU B O     1 
ATOM   10447 C CB    . LEU D  1 159 ? -25.705 54.577  -26.904 1.00 38.63 ? 159 LEU B CB    1 
ATOM   10448 C CG    . LEU D  1 159 ? -27.013 53.814  -27.122 1.00 38.66 ? 159 LEU B CG    1 
ATOM   10449 C CD1   . LEU D  1 159 ? -27.875 54.053  -25.882 1.00 37.09 ? 159 LEU B CD1   1 
ATOM   10450 C CD2   . LEU D  1 159 ? -27.754 54.237  -28.383 1.00 35.09 ? 159 LEU B CD2   1 
ATOM   10451 N N     . THR D  1 160 ? -24.694 56.931  -28.769 1.00 37.16 ? 160 THR B N     1 
ATOM   10452 C CA    . THR D  1 160 ? -24.377 58.347  -28.680 1.00 37.47 ? 160 THR B CA    1 
ATOM   10453 C C     . THR D  1 160 ? -24.887 58.878  -27.355 1.00 36.35 ? 160 THR B C     1 
ATOM   10454 O O     . THR D  1 160 ? -25.786 58.301  -26.747 1.00 40.22 ? 160 THR B O     1 
ATOM   10455 C CB    . THR D  1 160 ? -25.030 59.131  -29.811 1.00 40.48 ? 160 THR B CB    1 
ATOM   10456 O OG1   . THR D  1 160 ? -26.340 59.531  -29.391 1.00 42.43 ? 160 THR B OG1   1 
ATOM   10457 C CG2   . THR D  1 160 ? -25.175 58.261  -31.051 1.00 45.21 ? 160 THR B CG2   1 
ATOM   10458 N N     . ASP D  1 161 ? -24.293 59.970  -26.888 1.00 43.88 ? 161 ASP B N     1 
ATOM   10459 C CA    . ASP D  1 161 ? -24.778 60.570  -25.655 1.00 33.14 ? 161 ASP B CA    1 
ATOM   10460 C C     . ASP D  1 161 ? -26.192 61.070  -25.889 1.00 36.94 ? 161 ASP B C     1 
ATOM   10461 O O     . ASP D  1 161 ? -26.518 61.552  -26.980 1.00 42.07 ? 161 ASP B O     1 
ATOM   10462 C CB    . ASP D  1 161 ? -23.852 61.699  -25.214 1.00 33.82 ? 161 ASP B CB    1 
ATOM   10463 C CG    . ASP D  1 161 ? -22.577 61.178  -24.522 1.00 48.60 ? 161 ASP B CG    1 
ATOM   10464 O OD1   . ASP D  1 161 ? -22.641 60.079  -23.924 1.00 46.13 ? 161 ASP B OD1   1 
ATOM   10465 O OD2   . ASP D  1 161 ? -21.520 61.865  -24.561 1.00 47.85 ? 161 ASP B OD2   1 
ATOM   10466 N N     . GLY D  1 162 ? -27.049 60.890  -24.887 1.00 28.74 ? 162 GLY B N     1 
ATOM   10467 C CA    . GLY D  1 162 ? -28.441 61.239  -25.062 1.00 29.60 ? 162 GLY B CA    1 
ATOM   10468 C C     . GLY D  1 162 ? -29.410 60.884  -23.947 1.00 31.84 ? 162 GLY B C     1 
ATOM   10469 O O     . GLY D  1 162 ? -29.214 59.927  -23.199 1.00 33.64 ? 162 GLY B O     1 
ATOM   10470 N N     . VAL D  1 163 ? -30.476 61.651  -23.839 1.00 26.90 ? 163 VAL B N     1 
ATOM   10471 C CA    . VAL D  1 163 ? -31.470 61.472  -22.802 1.00 24.47 ? 163 VAL B CA    1 
ATOM   10472 C C     . VAL D  1 163 ? -32.709 60.811  -23.398 1.00 35.09 ? 163 VAL B C     1 
ATOM   10473 O O     . VAL D  1 163 ? -33.124 61.131  -24.525 1.00 36.33 ? 163 VAL B O     1 
ATOM   10474 C CB    . VAL D  1 163 ? -31.812 62.836  -22.169 1.00 28.61 ? 163 VAL B CB    1 
ATOM   10475 C CG1   . VAL D  1 163 ? -33.042 62.719  -21.284 1.00 38.10 ? 163 VAL B CG1   1 
ATOM   10476 C CG2   . VAL D  1 163 ? -30.672 63.341  -21.343 1.00 24.13 ? 163 VAL B CG2   1 
ATOM   10477 N N     . VAL D  1 164 ? -33.304 59.879  -22.654 1.00 32.95 ? 164 VAL B N     1 
ATOM   10478 C CA    . VAL D  1 164 ? -34.683 59.478  -22.921 1.00 30.77 ? 164 VAL B CA    1 
ATOM   10479 C C     . VAL D  1 164 ? -35.573 60.478  -22.180 1.00 31.82 ? 164 VAL B C     1 
ATOM   10480 O O     . VAL D  1 164 ? -35.644 60.470  -20.949 1.00 29.82 ? 164 VAL B O     1 
ATOM   10481 C CB    . VAL D  1 164 ? -34.963 58.028  -22.493 1.00 27.77 ? 164 VAL B CB    1 
ATOM   10482 C CG1   . VAL D  1 164 ? -36.408 57.635  -22.782 1.00 26.68 ? 164 VAL B CG1   1 
ATOM   10483 C CG2   . VAL D  1 164 ? -34.052 57.065  -23.208 1.00 26.65 ? 164 VAL B CG2   1 
ATOM   10484 N N     . ALA D  1 165 ? -36.225 61.367  -22.932 1.00 34.26 ? 165 ALA B N     1 
ATOM   10485 C CA    . ALA D  1 165 ? -36.851 62.561  -22.377 1.00 32.52 ? 165 ALA B CA    1 
ATOM   10486 C C     . ALA D  1 165 ? -38.342 62.356  -22.179 1.00 29.30 ? 165 ALA B C     1 
ATOM   10487 O O     . ALA D  1 165 ? -39.014 61.715  -22.990 1.00 32.50 ? 165 ALA B O     1 
ATOM   10488 C CB    . ALA D  1 165 ? -36.618 63.786  -23.265 1.00 34.91 ? 165 ALA B CB    1 
ATOM   10489 N N     . ARG D  1 166 ? -38.854 62.932  -21.103 1.00 28.39 ? 166 ARG B N     1 
ATOM   10490 C CA    . ARG D  1 166 ? -40.190 62.625  -20.636 1.00 32.58 ? 166 ARG B CA    1 
ATOM   10491 C C     . ARG D  1 166 ? -41.104 63.836  -20.609 1.00 34.10 ? 166 ARG B C     1 
ATOM   10492 O O     . ARG D  1 166 ? -42.302 63.681  -20.332 1.00 36.16 ? 166 ARG B O     1 
ATOM   10493 C CB    . ARG D  1 166 ? -40.127 61.993  -19.240 1.00 32.63 ? 166 ARG B CB    1 
ATOM   10494 C CG    . ARG D  1 166 ? -39.200 60.780  -19.143 1.00 30.92 ? 166 ARG B CG    1 
ATOM   10495 C CD    . ARG D  1 166 ? -38.901 60.425  -17.685 1.00 28.08 ? 166 ARG B CD    1 
ATOM   10496 N NE    . ARG D  1 166 ? -37.808 61.227  -17.149 1.00 40.33 ? 166 ARG B NE    1 
ATOM   10497 C CZ    . ARG D  1 166 ? -37.196 60.989  -15.995 1.00 39.90 ? 166 ARG B CZ    1 
ATOM   10498 N NH1   . ARG D  1 166 ? -37.567 59.989  -15.215 1.00 38.07 ? 166 ARG B NH1   1 
ATOM   10499 N NH2   . ARG D  1 166 ? -36.182 61.770  -15.619 1.00 34.97 ? 166 ARG B NH2   1 
ATOM   10500 N N     . GLY D  1 167 ? -40.586 65.024  -20.905 1.00 31.80 ? 167 GLY B N     1 
ATOM   10501 C CA    . GLY D  1 167 ? -41.392 66.216  -20.922 1.00 33.24 ? 167 GLY B CA    1 
ATOM   10502 C C     . GLY D  1 167 ? -40.645 67.423  -21.441 1.00 36.52 ? 167 GLY B C     1 
ATOM   10503 O O     . GLY D  1 167 ? -39.446 67.375  -21.749 1.00 34.33 ? 167 GLY B O     1 
ATOM   10504 N N     . PRO D  1 168 ? -41.358 68.546  -21.525 1.00 35.35 ? 168 PRO B N     1 
ATOM   10505 C CA    . PRO D  1 168 ? -40.742 69.789  -22.026 1.00 34.38 ? 168 PRO B CA    1 
ATOM   10506 C C     . PRO D  1 168 ? -39.462 70.202  -21.307 1.00 36.79 ? 168 PRO B C     1 
ATOM   10507 O O     . PRO D  1 168 ? -38.466 70.531  -21.963 1.00 38.21 ? 168 PRO B O     1 
ATOM   10508 C CB    . PRO D  1 168 ? -41.860 70.818  -21.826 1.00 42.63 ? 168 PRO B CB    1 
ATOM   10509 C CG    . PRO D  1 168 ? -43.127 70.020  -21.803 1.00 41.81 ? 168 PRO B CG    1 
ATOM   10510 C CD    . PRO D  1 168 ? -42.783 68.701  -21.199 1.00 34.90 ? 168 PRO B CD    1 
ATOM   10511 N N     . ALA D  1 169 ? -39.458 70.212  -19.970 1.00 43.16 ? 169 ALA B N     1 
ATOM   10512 C CA    . ALA D  1 169 ? -38.278 70.687  -19.250 1.00 39.93 ? 169 ALA B CA    1 
ATOM   10513 C C     . ALA D  1 169 ? -37.111 69.728  -19.385 1.00 34.47 ? 169 ALA B C     1 
ATOM   10514 O O     . ALA D  1 169 ? -35.956 70.164  -19.449 1.00 38.17 ? 169 ALA B O     1 
ATOM   10515 C CB    . ALA D  1 169 ? -38.594 70.903  -17.777 1.00 40.17 ? 169 ALA B CB    1 
ATOM   10516 N N     . GLU D  1 170 ? -37.381 68.427  -19.406 1.00 34.22 ? 170 GLU B N     1 
ATOM   10517 C CA    . GLU D  1 170 ? -36.301 67.482  -19.639 1.00 34.10 ? 170 GLU B CA    1 
ATOM   10518 C C     . GLU D  1 170 ? -35.705 67.684  -21.019 1.00 39.45 ? 170 GLU B C     1 
ATOM   10519 O O     . GLU D  1 170 ? -34.480 67.624  -21.190 1.00 42.25 ? 170 GLU B O     1 
ATOM   10520 C CB    . GLU D  1 170 ? -36.806 66.059  -19.478 1.00 31.88 ? 170 GLU B CB    1 
ATOM   10521 C CG    . GLU D  1 170 ? -35.850 65.189  -18.750 1.00 34.18 ? 170 GLU B CG    1 
ATOM   10522 C CD    . GLU D  1 170 ? -36.453 63.861  -18.405 1.00 36.97 ? 170 GLU B CD    1 
ATOM   10523 O OE1   . GLU D  1 170 ? -37.397 63.455  -19.118 1.00 32.40 ? 170 GLU B OE1   1 
ATOM   10524 O OE2   . GLU D  1 170 ? -35.993 63.236  -17.416 1.00 43.12 ? 170 GLU B OE2   1 
ATOM   10525 N N     . VAL D  1 171 ? -36.560 67.945  -22.014 1.00 37.99 ? 171 VAL B N     1 
ATOM   10526 C CA    . VAL D  1 171 ? -36.074 68.304  -23.340 1.00 36.74 ? 171 VAL B CA    1 
ATOM   10527 C C     . VAL D  1 171 ? -35.307 69.617  -23.292 1.00 42.01 ? 171 VAL B C     1 
ATOM   10528 O O     . VAL D  1 171 ? -34.241 69.753  -23.909 1.00 40.89 ? 171 VAL B O     1 
ATOM   10529 C CB    . VAL D  1 171 ? -37.240 68.380  -24.331 1.00 34.36 ? 171 VAL B CB    1 
ATOM   10530 C CG1   . VAL D  1 171 ? -36.792 69.099  -25.588 1.00 33.43 ? 171 VAL B CG1   1 
ATOM   10531 C CG2   . VAL D  1 171 ? -37.711 67.000  -24.640 1.00 36.23 ? 171 VAL B CG2   1 
ATOM   10532 N N     . ARG D  1 172 ? -35.833 70.606  -22.563 1.00 39.51 ? 172 ARG B N     1 
ATOM   10533 C CA    . ARG D  1 172 ? -35.111 71.868  -22.430 1.00 43.43 ? 172 ARG B CA    1 
ATOM   10534 C C     . ARG D  1 172 ? -33.725 71.646  -21.842 1.00 43.13 ? 172 ARG B C     1 
ATOM   10535 O O     . ARG D  1 172 ? -32.744 72.234  -22.313 1.00 45.49 ? 172 ARG B O     1 
ATOM   10536 C CB    . ARG D  1 172 ? -35.902 72.857  -21.573 1.00 41.56 ? 172 ARG B CB    1 
ATOM   10537 C CG    . ARG D  1 172 ? -35.170 74.155  -21.348 1.00 41.96 ? 172 ARG B CG    1 
ATOM   10538 C CD    . ARG D  1 172 ? -36.107 75.326  -21.092 1.00 43.21 ? 172 ARG B CD    1 
ATOM   10539 N NE    . ARG D  1 172 ? -35.553 76.593  -21.573 1.00 54.59 ? 172 ARG B NE    1 
ATOM   10540 C CZ    . ARG D  1 172 ? -34.440 77.170  -21.124 1.00 55.61 ? 172 ARG B CZ    1 
ATOM   10541 N NH1   . ARG D  1 172 ? -33.705 76.620  -20.163 1.00 34.95 ? 172 ARG B NH1   1 
ATOM   10542 N NH2   . ARG D  1 172 ? -34.056 78.332  -21.651 1.00 56.34 ? 172 ARG B NH2   1 
ATOM   10543 N N     . SER D  1 173 ? -33.616 70.787  -20.828 1.00 39.89 ? 173 SER B N     1 
ATOM   10544 C CA    . SER D  1 173 ? -32.320 70.580  -20.198 1.00 45.22 ? 173 SER B CA    1 
ATOM   10545 C C     . SER D  1 173 ? -31.427 69.644  -20.990 1.00 42.97 ? 173 SER B C     1 
ATOM   10546 O O     . SER D  1 173 ? -30.199 69.744  -20.900 1.00 46.76 ? 173 SER B O     1 
ATOM   10547 C CB    . SER D  1 173 ? -32.510 70.040  -18.787 1.00 42.18 ? 173 SER B CB    1 
ATOM   10548 O OG    . SER D  1 173 ? -33.647 69.212  -18.771 1.00 44.15 ? 173 SER B OG    1 
ATOM   10549 N N     . ALA D  1 174 ? -32.008 68.732  -21.757 1.00 42.92 ? 174 ALA B N     1 
ATOM   10550 C CA    . ALA D  1 174 ? -31.184 67.803  -22.520 1.00 44.44 ? 174 ALA B CA    1 
ATOM   10551 C C     . ALA D  1 174 ? -30.352 68.539  -23.561 1.00 46.10 ? 174 ALA B C     1 
ATOM   10552 O O     . ALA D  1 174 ? -29.133 68.348  -23.638 1.00 46.78 ? 174 ALA B O     1 
ATOM   10553 C CB    . ALA D  1 174 ? -32.063 66.739  -23.176 1.00 45.74 ? 174 ALA B CB    1 
ATOM   10554 N N     . ILE D  1 175 ? -30.991 69.407  -24.356 1.00 50.08 ? 175 ILE B N     1 
ATOM   10555 C CA    . ILE D  1 175 ? -30.269 70.130  -25.407 1.00 50.70 ? 175 ILE B CA    1 
ATOM   10556 C C     . ILE D  1 175 ? -29.313 71.158  -24.803 1.00 51.05 ? 175 ILE B C     1 
ATOM   10557 O O     . ILE D  1 175 ? -28.224 71.401  -25.346 1.00 49.82 ? 175 ILE B O     1 
ATOM   10558 C CB    . ILE D  1 175 ? -31.254 70.784  -26.400 1.00 46.81 ? 175 ILE B CB    1 
ATOM   10559 C CG1   . ILE D  1 175 ? -32.323 69.786  -26.858 1.00 45.79 ? 175 ILE B CG1   1 
ATOM   10560 C CG2   . ILE D  1 175 ? -30.512 71.304  -27.624 1.00 51.20 ? 175 ILE B CG2   1 
ATOM   10561 C CD1   . ILE D  1 175 ? -33.689 70.415  -27.086 1.00 42.33 ? 175 ILE B CD1   1 
ATOM   10562 N N     . GLN D  1 176 ? -29.702 71.774  -23.685 1.00 50.80 ? 176 GLN B N     1 
ATOM   10563 C CA    . GLN D  1 176 ? -28.812 72.571  -22.850 1.00 49.64 ? 176 GLN B CA    1 
ATOM   10564 C C     . GLN D  1 176 ? -27.472 71.845  -22.736 1.00 50.37 ? 176 GLN B C     1 
ATOM   10565 O O     . GLN D  1 176 ? -26.400 72.450  -22.823 1.00 55.65 ? 176 GLN B O     1 
ATOM   10566 C CB    . GLN D  1 176 ? -29.486 72.777  -21.483 1.00 52.88 ? 176 GLN B CB    1 
ATOM   10567 C CG    . GLN D  1 176 ? -29.437 74.169  -20.878 1.00 53.99 ? 176 GLN B CG    1 
ATOM   10568 C CD    . GLN D  1 176 ? -28.089 74.489  -20.279 1.00 63.27 ? 176 GLN B CD    1 
ATOM   10569 O OE1   . GLN D  1 176 ? -27.146 73.708  -20.401 1.00 65.15 ? 176 GLN B OE1   1 
ATOM   10570 N NE2   . GLN D  1 176 ? -28.001 75.623  -19.588 1.00 70.30 ? 176 GLN B NE2   1 
ATOM   10571 N N     . GLU D  1 177 ? -27.534 70.523  -22.614 1.00 48.73 ? 177 GLU B N     1 
ATOM   10572 C CA    . GLU D  1 177 ? -26.369 69.683  -22.384 1.00 49.93 ? 177 GLU B CA    1 
ATOM   10573 C C     . GLU D  1 177 ? -25.691 69.245  -23.683 1.00 48.11 ? 177 GLU B C     1 
ATOM   10574 O O     . GLU D  1 177 ? -24.552 69.629  -23.957 1.00 48.27 ? 177 GLU B O     1 
ATOM   10575 C CB    . GLU D  1 177 ? -26.817 68.469  -21.569 1.00 51.08 ? 177 GLU B CB    1 
ATOM   10576 C CG    . GLU D  1 177 ? -25.712 67.694  -20.916 1.00 55.41 ? 177 GLU B CG    1 
ATOM   10577 C CD    . GLU D  1 177 ? -26.261 66.608  -20.014 1.00 57.43 ? 177 GLU B CD    1 
ATOM   10578 O OE1   . GLU D  1 177 ? -27.038 66.933  -19.081 1.00 62.75 ? 177 GLU B OE1   1 
ATOM   10579 O OE2   . GLU D  1 177 ? -25.928 65.428  -20.244 1.00 54.24 ? 177 GLU B OE2   1 
ATOM   10580 N N     . LEU D  1 178 ? -26.396 68.449  -24.491 1.00 42.36 ? 178 LEU B N     1 
ATOM   10581 C CA    . LEU D  1 178 ? -25.806 67.719  -25.611 1.00 44.19 ? 178 LEU B CA    1 
ATOM   10582 C C     . LEU D  1 178 ? -25.298 68.626  -26.722 1.00 45.43 ? 178 LEU B C     1 
ATOM   10583 O O     . LEU D  1 178 ? -24.479 68.191  -27.542 1.00 43.81 ? 178 LEU B O     1 
ATOM   10584 C CB    . LEU D  1 178 ? -26.842 66.758  -26.193 1.00 43.64 ? 178 LEU B CB    1 
ATOM   10585 C CG    . LEU D  1 178 ? -27.620 65.923  -25.179 1.00 41.06 ? 178 LEU B CG    1 
ATOM   10586 C CD1   . LEU D  1 178 ? -28.802 65.255  -25.845 1.00 38.63 ? 178 LEU B CD1   1 
ATOM   10587 C CD2   . LEU D  1 178 ? -26.701 64.898  -24.544 1.00 37.92 ? 178 LEU B CD2   1 
ATOM   10588 N N     . ILE D  1 179 ? -25.776 69.868  -26.783 1.00 44.70 ? 179 ILE B N     1 
ATOM   10589 C CA    . ILE D  1 179 ? -25.383 70.742  -27.870 1.00 46.59 ? 179 ILE B CA    1 
ATOM   10590 C C     . ILE D  1 179 ? -23.879 70.968  -27.887 1.00 48.87 ? 179 ILE B C     1 
ATOM   10591 O O     . ILE D  1 179 ? -23.311 71.276  -28.940 1.00 45.52 ? 179 ILE B O     1 
ATOM   10592 C CB    . ILE D  1 179 ? -26.148 72.073  -27.763 1.00 49.30 ? 179 ILE B CB    1 
ATOM   10593 C CG1   . ILE D  1 179 ? -25.844 72.962  -28.965 1.00 51.91 ? 179 ILE B CG1   1 
ATOM   10594 C CG2   . ILE D  1 179 ? -25.739 72.821  -26.504 1.00 49.71 ? 179 ILE B CG2   1 
ATOM   10595 C CD1   . ILE D  1 179 ? -26.439 72.462  -30.256 1.00 48.76 ? 179 ILE B CD1   1 
ATOM   10596 N N     . ALA D  1 180 ? -23.212 70.789  -26.747 1.00 44.05 ? 180 ALA B N     1 
ATOM   10597 C CA    . ALA D  1 180 ? -21.817 71.189  -26.644 1.00 44.12 ? 180 ALA B CA    1 
ATOM   10598 C C     . ALA D  1 180 ? -20.895 70.345  -27.508 1.00 45.52 ? 180 ALA B C     1 
ATOM   10599 O O     . ALA D  1 180 ? -19.923 70.880  -28.048 1.00 50.00 ? 180 ALA B O     1 
ATOM   10600 C CB    . ALA D  1 180 ? -21.362 71.130  -25.194 1.00 46.87 ? 180 ALA B CB    1 
ATOM   10601 N N     . GLU D  1 181 ? -21.158 69.048  -27.670 1.00 49.50 ? 181 GLU B N     1 
ATOM   10602 C CA    . GLU D  1 181 ? -20.125 68.206  -28.274 1.00 51.25 ? 181 GLU B CA    1 
ATOM   10603 C C     . GLU D  1 181 ? -19.900 68.551  -29.737 1.00 50.18 ? 181 GLU B C     1 
ATOM   10604 O O     . GLU D  1 181 ? -18.769 68.821  -30.153 1.00 57.71 ? 181 GLU B O     1 
ATOM   10605 C CB    . GLU D  1 181 ? -20.451 66.722  -28.159 1.00 50.85 ? 181 GLU B CB    1 
ATOM   10606 C CG    . GLU D  1 181 ? -19.283 65.919  -28.734 1.00 51.59 ? 181 GLU B CG    1 
ATOM   10607 C CD    . GLU D  1 181 ? -19.467 64.420  -28.682 1.00 56.51 ? 181 GLU B CD    1 
ATOM   10608 O OE1   . GLU D  1 181 ? -20.529 63.965  -28.183 1.00 63.09 ? 181 GLU B OE1   1 
ATOM   10609 O OE2   . GLU D  1 181 ? -18.521 63.707  -29.114 1.00 51.02 ? 181 GLU B OE2   1 
ATOM   10610 N N     . THR D  1 182 ? -20.967 68.499  -30.542 1.00 55.28 ? 182 THR B N     1 
ATOM   10611 C CA    . THR D  1 182 ? -20.912 68.756  -31.978 1.00 49.92 ? 182 THR B CA    1 
ATOM   10612 C C     . THR D  1 182 ? -21.612 70.043  -32.398 1.00 50.96 ? 182 THR B C     1 
ATOM   10613 O O     . THR D  1 182 ? -21.509 70.438  -33.562 1.00 49.86 ? 182 THR B O     1 
ATOM   10614 C CB    . THR D  1 182 ? -21.549 67.591  -32.757 1.00 45.92 ? 182 THR B CB    1 
ATOM   10615 O OG1   . THR D  1 182 ? -22.954 67.548  -32.483 1.00 45.45 ? 182 THR B OG1   1 
ATOM   10616 C CG2   . THR D  1 182 ? -20.920 66.262  -32.367 1.00 47.22 ? 182 THR B CG2   1 
ATOM   10617 N N     . GLY D  1 183 ? -22.328 70.703  -31.500 1.00 53.67 ? 183 GLY B N     1 
ATOM   10618 C CA    . GLY D  1 183 ? -23.221 71.726  -31.979 1.00 46.01 ? 183 GLY B CA    1 
ATOM   10619 C C     . GLY D  1 183 ? -24.336 71.165  -32.808 1.00 48.80 ? 183 GLY B C     1 
ATOM   10620 O O     . GLY D  1 183 ? -24.928 71.889  -33.614 1.00 54.39 ? 183 GLY B O     1 
ATOM   10621 N N     . MET D  1 184 ? -24.621 69.872  -32.655 1.00 49.25 ? 184 MET B N     1 
ATOM   10622 C CA    . MET D  1 184 ? -25.669 69.210  -33.423 1.00 51.31 ? 184 MET B CA    1 
ATOM   10623 C C     . MET D  1 184 ? -26.401 68.223  -32.530 1.00 47.33 ? 184 MET B C     1 
ATOM   10624 O O     . MET D  1 184 ? -25.790 67.308  -31.969 1.00 45.13 ? 184 MET B O     1 
ATOM   10625 C CB    . MET D  1 184 ? -25.090 68.508  -34.651 1.00 42.17 ? 184 MET B CB    1 
ATOM   10626 C CG    . MET D  1 184 ? -24.405 69.477  -35.561 1.00 44.08 ? 184 MET B CG    1 
ATOM   10627 S SD    . MET D  1 184 ? -24.057 68.783  -37.151 1.00 51.64 ? 184 MET B SD    1 
ATOM   10628 C CE    . MET D  1 184 ? -23.086 67.346  -36.689 1.00 45.72 ? 184 MET B CE    1 
ATOM   10629 N N     . VAL D  1 185 ? -27.706 68.407  -32.407 1.00 41.45 ? 185 VAL B N     1 
ATOM   10630 C CA    . VAL D  1 185 ? -28.536 67.523  -31.611 1.00 44.94 ? 185 VAL B CA    1 
ATOM   10631 C C     . VAL D  1 185 ? -29.655 67.009  -32.515 1.00 48.69 ? 185 VAL B C     1 
ATOM   10632 O O     . VAL D  1 185 ? -30.026 67.661  -33.500 1.00 45.90 ? 185 VAL B O     1 
ATOM   10633 C CB    . VAL D  1 185 ? -29.055 68.276  -30.357 1.00 44.38 ? 185 VAL B CB    1 
ATOM   10634 C CG1   . VAL D  1 185 ? -30.283 67.618  -29.743 1.00 40.47 ? 185 VAL B CG1   1 
ATOM   10635 C CG2   . VAL D  1 185 ? -27.937 68.429  -29.314 1.00 42.04 ? 185 VAL B CG2   1 
ATOM   10636 N N     . ILE D  1 186 ? -30.152 65.801  -32.218 1.00 45.99 ? 186 ILE B N     1 
ATOM   10637 C CA    . ILE D  1 186 ? -31.290 65.236  -32.931 1.00 43.28 ? 186 ILE B CA    1 
ATOM   10638 C C     . ILE D  1 186 ? -32.345 64.817  -31.919 1.00 38.94 ? 186 ILE B C     1 
ATOM   10639 O O     . ILE D  1 186 ? -32.029 64.311  -30.836 1.00 41.48 ? 186 ILE B O     1 
ATOM   10640 C CB    . ILE D  1 186 ? -30.885 64.061  -33.864 1.00 44.30 ? 186 ILE B CB    1 
ATOM   10641 C CG1   . ILE D  1 186 ? -32.032 63.700  -34.822 1.00 37.90 ? 186 ILE B CG1   1 
ATOM   10642 C CG2   . ILE D  1 186 ? -30.394 62.839  -33.092 1.00 36.89 ? 186 ILE B CG2   1 
ATOM   10643 C CD1   . ILE D  1 186 ? -31.600 62.814  -35.976 1.00 37.10 ? 186 ILE B CD1   1 
ATOM   10644 N N     . ALA D  1 187 ? -33.601 65.070  -32.263 1.00 41.16 ? 187 ALA B N     1 
ATOM   10645 C CA    . ALA D  1 187 ? -34.743 64.745  -31.429 1.00 40.49 ? 187 ALA B CA    1 
ATOM   10646 C C     . ALA D  1 187 ? -35.687 63.872  -32.231 1.00 38.15 ? 187 ALA B C     1 
ATOM   10647 O O     . ALA D  1 187 ? -35.977 64.173  -33.391 1.00 45.22 ? 187 ALA B O     1 
ATOM   10648 C CB    . ALA D  1 187 ? -35.467 66.007  -30.965 1.00 43.57 ? 187 ALA B CB    1 
ATOM   10649 N N     . LYS D  1 188 ? -36.187 62.811  -31.604 1.00 35.93 ? 188 LYS B N     1 
ATOM   10650 C CA    . LYS D  1 188 ? -36.723 61.667  -32.326 1.00 37.46 ? 188 LYS B CA    1 
ATOM   10651 C C     . LYS D  1 188 ? -38.103 61.275  -31.816 1.00 40.56 ? 188 LYS B C     1 
ATOM   10652 O O     . LYS D  1 188 ? -38.301 61.099  -30.609 1.00 37.39 ? 188 LYS B O     1 
ATOM   10653 C CB    . LYS D  1 188 ? -35.764 60.479  -32.193 1.00 37.04 ? 188 LYS B CB    1 
ATOM   10654 C CG    . LYS D  1 188 ? -34.317 60.745  -32.696 1.00 30.07 ? 188 LYS B CG    1 
ATOM   10655 C CD    . LYS D  1 188 ? -33.640 59.398  -32.967 1.00 35.59 ? 188 LYS B CD    1 
ATOM   10656 C CE    . LYS D  1 188 ? -32.318 59.481  -33.715 1.00 34.07 ? 188 LYS B CE    1 
ATOM   10657 N NZ    . LYS D  1 188 ? -31.965 58.139  -34.308 1.00 39.16 ? 188 LYS B NZ    1 
ATOM   10658 N N     . GLN D  1 189 ? -39.051 61.116  -32.733 1.00 38.93 ? 189 GLN B N     1 
ATOM   10659 C CA    . GLN D  1 189 ? -40.282 60.426  -32.368 1.00 45.35 ? 189 GLN B CA    1 
ATOM   10660 C C     . GLN D  1 189 ? -39.959 58.975  -31.998 1.00 44.55 ? 189 GLN B C     1 
ATOM   10661 O O     . GLN D  1 189 ? -39.270 58.267  -32.746 1.00 40.61 ? 189 GLN B O     1 
ATOM   10662 C CB    . GLN D  1 189 ? -41.303 60.495  -33.521 1.00 44.62 ? 189 GLN B CB    1 
ATOM   10663 C CG    . GLN D  1 189 ? -42.751 60.861  -33.085 1.00 49.98 ? 189 GLN B CG    1 
ATOM   10664 C CD    . GLN D  1 189 ? -43.669 61.230  -34.256 1.00 58.59 ? 189 GLN B CD    1 
ATOM   10665 O OE1   . GLN D  1 189 ? -43.387 60.889  -35.405 1.00 59.83 ? 189 GLN B OE1   1 
ATOM   10666 N NE2   . GLN D  1 189 ? -44.767 61.944  -33.963 1.00 53.68 ? 189 GLN B NE2   1 
ATOM   10667 N N     . ASP D  1 190 ? -40.456 58.543  -30.831 1.00 36.90 ? 190 ASP B N     1 
ATOM   10668 C CA    . ASP D  1 190 ? -40.145 57.210  -30.304 1.00 37.66 ? 190 ASP B CA    1 
ATOM   10669 C C     . ASP D  1 190 ? -40.588 56.099  -31.248 1.00 38.77 ? 190 ASP B C     1 
ATOM   10670 O O     . ASP D  1 190 ? -39.850 55.131  -31.468 1.00 39.77 ? 190 ASP B O     1 
ATOM   10671 C CB    . ASP D  1 190 ? -40.802 57.028  -28.934 1.00 41.64 ? 190 ASP B CB    1 
ATOM   10672 C CG    . ASP D  1 190 ? -40.118 55.968  -28.077 1.00 39.59 ? 190 ASP B CG    1 
ATOM   10673 O OD1   . ASP D  1 190 ? -38.919 55.663  -28.314 1.00 38.28 ? 190 ASP B OD1   1 
ATOM   10674 O OD2   . ASP D  1 190 ? -40.792 55.447  -27.149 1.00 37.35 ? 190 ASP B OD2   1 
ATOM   10675 N N     . ARG D  1 191 ? -41.793 56.205  -31.804 1.00 45.55 ? 191 ARG B N     1 
ATOM   10676 C CA    . ARG D  1 191 ? -42.275 55.278  -32.832 1.00 46.17 ? 191 ARG B CA    1 
ATOM   10677 C C     . ARG D  1 191 ? -42.337 56.042  -34.156 1.00 47.69 ? 191 ARG B C     1 
ATOM   10678 O O     . ARG D  1 191 ? -43.156 56.956  -34.307 1.00 51.77 ? 191 ARG B O     1 
ATOM   10679 C CB    . ARG D  1 191 ? -43.636 54.679  -32.448 1.00 38.23 ? 191 ARG B CB    1 
ATOM   10680 C CG    . ARG D  1 191 ? -43.628 53.852  -31.144 1.00 38.70 ? 191 ARG B CG    1 
ATOM   10681 C CD    . ARG D  1 191 ? -44.974 53.185  -30.853 1.00 33.74 ? 191 ARG B CD    1 
ATOM   10682 N NE    . ARG D  1 191 ? -44.958 52.400  -29.619 1.00 44.58 ? 191 ARG B NE    1 
ATOM   10683 C CZ    . ARG D  1 191 ? -45.476 52.789  -28.455 1.00 45.55 ? 191 ARG B CZ    1 
ATOM   10684 N NH1   . ARG D  1 191 ? -46.030 53.982  -28.303 1.00 40.01 ? 191 ARG B NH1   1 
ATOM   10685 N NH2   . ARG D  1 191 ? -45.429 51.960  -27.411 1.00 40.86 ? 191 ARG B NH2   1 
ATOM   10686 N N     . SER D  1 192 ? -41.448 55.685  -35.101 1.00 50.77 ? 192 SER B N     1 
ATOM   10687 C CA    . SER D  1 192 ? -41.394 56.289  -36.434 1.00 44.63 ? 192 SER B CA    1 
ATOM   10688 C C     . SER D  1 192 ? -40.330 55.612  -37.294 1.00 43.87 ? 192 SER B C     1 
ATOM   10689 O O     . SER D  1 192 ? -39.590 54.741  -36.822 1.00 43.06 ? 192 SER B O     1 
ATOM   10690 C CB    . SER D  1 192 ? -41.108 57.793  -36.349 1.00 46.74 ? 192 SER B CB    1 
ATOM   10691 O OG    . SER D  1 192 ? -41.887 58.514  -37.291 1.00 46.88 ? 192 SER B OG    1 
ATOM   10692 N N     . GLY D  1 193 ? -40.239 56.003  -38.561 1.00 43.96 ? 193 GLY B N     1 
ATOM   10693 C CA    . GLY D  1 193 ? -39.246 55.419  -39.439 1.00 36.91 ? 193 GLY B CA    1 
ATOM   10694 C C     . GLY D  1 193 ? -38.782 56.398  -40.493 1.00 41.82 ? 193 GLY B C     1 
ATOM   10695 O O     . GLY D  1 193 ? -39.481 57.354  -40.840 1.00 47.81 ? 193 GLY B O     1 
ATOM   10696 N N     . GLY D  1 194 ? -37.577 56.143  -40.995 1.00 48.98 ? 194 GLY B N     1 
ATOM   10697 C CA    . GLY D  1 194 ? -37.060 56.838  -42.164 1.00 50.35 ? 194 GLY B CA    1 
ATOM   10698 C C     . GLY D  1 194 ? -36.887 58.332  -42.007 1.00 51.38 ? 194 GLY B C     1 
ATOM   10699 O O     . GLY D  1 194 ? -37.026 59.066  -42.994 1.00 54.74 ? 194 GLY B O     1 
ATOM   10700 N N     . GLY D  1 195 ? -36.589 58.811  -40.796 1.00 44.43 ? 195 GLY B N     1 
ATOM   10701 C CA    . GLY D  1 195 ? -36.366 60.233  -40.587 1.00 43.75 ? 195 GLY B CA    1 
ATOM   10702 C C     . GLY D  1 195 ? -37.607 61.103  -40.551 1.00 44.66 ? 195 GLY B C     1 
ATOM   10703 O O     . GLY D  1 195 ? -37.487 62.331  -40.469 1.00 41.61 ? 195 GLY B O     1 
ATOM   10704 N N     . HIS D  1 196 ? -38.797 60.514  -40.586 1.00 46.87 ? 196 HIS B N     1 
ATOM   10705 C CA    . HIS D  1 196 ? -40.008 61.317  -40.648 1.00 47.41 ? 196 HIS B CA    1 
ATOM   10706 C C     . HIS D  1 196 ? -40.441 61.868  -39.292 1.00 48.85 ? 196 HIS B C     1 
ATOM   10707 O O     . HIS D  1 196 ? -41.376 62.672  -39.257 1.00 54.31 ? 196 HIS B O     1 
ATOM   10708 C CB    . HIS D  1 196 ? -41.136 60.491  -41.275 1.00 46.28 ? 196 HIS B CB    1 
ATOM   10709 C CG    . HIS D  1 196 ? -40.723 59.762  -42.523 1.00 51.72 ? 196 HIS B CG    1 
ATOM   10710 N ND1   . HIS D  1 196 ? -41.059 58.446  -42.769 1.00 52.55 ? 196 HIS B ND1   1 
ATOM   10711 C CD2   . HIS D  1 196 ? -39.988 60.165  -43.590 1.00 52.23 ? 196 HIS B CD2   1 
ATOM   10712 C CE1   . HIS D  1 196 ? -40.550 58.071  -43.932 1.00 53.10 ? 196 HIS B CE1   1 
ATOM   10713 N NE2   . HIS D  1 196 ? -39.894 59.094  -44.450 1.00 49.89 ? 196 HIS B NE2   1 
ATOM   10714 N N     . GLY D  1 197 ? -39.794 61.474  -38.189 1.00 45.96 ? 197 GLY B N     1 
ATOM   10715 C CA    . GLY D  1 197 ? -40.178 61.933  -36.859 1.00 41.19 ? 197 GLY B CA    1 
ATOM   10716 C C     . GLY D  1 197 ? -39.003 62.532  -36.112 1.00 40.74 ? 197 GLY B C     1 
ATOM   10717 O O     . GLY D  1 197 ? -39.009 62.651  -34.884 1.00 42.84 ? 197 GLY B O     1 
ATOM   10718 N N     . ASN D  1 198 ? -37.984 62.913  -36.873 1.00 40.16 ? 198 ASN B N     1 
ATOM   10719 C CA    . ASN D  1 198 ? -36.729 63.426  -36.358 1.00 33.74 ? 198 ASN B CA    1 
ATOM   10720 C C     . ASN D  1 198 ? -36.564 64.866  -36.788 1.00 36.64 ? 198 ASN B C     1 
ATOM   10721 O O     . ASN D  1 198 ? -36.746 65.196  -37.960 1.00 41.13 ? 198 ASN B O     1 
ATOM   10722 C CB    . ASN D  1 198 ? -35.552 62.607  -36.866 1.00 36.87 ? 198 ASN B CB    1 
ATOM   10723 C CG    . ASN D  1 198 ? -35.796 61.120  -36.751 1.00 40.60 ? 198 ASN B CG    1 
ATOM   10724 O OD1   . ASN D  1 198 ? -36.732 60.675  -36.072 1.00 37.09 ? 198 ASN B OD1   1 
ATOM   10725 N ND2   . ASN D  1 198 ? -34.949 60.335  -37.412 1.00 36.08 ? 198 ASN B ND2   1 
ATOM   10726 N N     . ILE D  1 199 ? -36.224 65.714  -35.839 1.00 43.48 ? 199 ILE B N     1 
ATOM   10727 C CA    . ILE D  1 199 ? -36.004 67.130  -36.072 1.00 42.50 ? 199 ILE B CA    1 
ATOM   10728 C C     . ILE D  1 199 ? -34.614 67.442  -35.556 1.00 42.83 ? 199 ILE B C     1 
ATOM   10729 O O     . ILE D  1 199 ? -34.226 66.958  -34.486 1.00 45.51 ? 199 ILE B O     1 
ATOM   10730 C CB    . ILE D  1 199 ? -37.076 67.986  -35.356 1.00 39.72 ? 199 ILE B CB    1 
ATOM   10731 C CG1   . ILE D  1 199 ? -38.486 67.586  -35.813 1.00 37.05 ? 199 ILE B CG1   1 
ATOM   10732 C CG2   . ILE D  1 199 ? -36.804 69.457  -35.561 1.00 44.60 ? 199 ILE B CG2   1 
ATOM   10733 C CD1   . ILE D  1 199 ? -39.612 68.419  -35.242 1.00 39.63 ? 199 ILE B CD1   1 
ATOM   10734 N N     . GLY D  1 200 ? -33.859 68.228  -36.315 1.00 42.76 ? 200 GLY B N     1 
ATOM   10735 C CA    . GLY D  1 200 ? -32.497 68.584  -35.946 1.00 45.02 ? 200 GLY B CA    1 
ATOM   10736 C C     . GLY D  1 200 ? -32.362 69.978  -35.354 1.00 46.77 ? 200 GLY B C     1 
ATOM   10737 O O     . GLY D  1 200 ? -33.095 70.901  -35.716 1.00 46.03 ? 200 GLY B O     1 
ATOM   10738 N N     . ILE D  1 201 ? -31.420 70.116  -34.421 1.00 43.42 ? 201 ILE B N     1 
ATOM   10739 C CA    . ILE D  1 201 ? -31.070 71.395  -33.810 1.00 46.36 ? 201 ILE B CA    1 
ATOM   10740 C C     . ILE D  1 201 ? -29.567 71.596  -33.965 1.00 51.15 ? 201 ILE B C     1 
ATOM   10741 O O     . ILE D  1 201 ? -28.781 70.699  -33.628 1.00 53.07 ? 201 ILE B O     1 
ATOM   10742 C CB    . ILE D  1 201 ? -31.484 71.459  -32.324 1.00 46.25 ? 201 ILE B CB    1 
ATOM   10743 C CG1   . ILE D  1 201 ? -32.996 71.645  -32.189 1.00 47.78 ? 201 ILE B CG1   1 
ATOM   10744 C CG2   . ILE D  1 201 ? -30.770 72.604  -31.597 1.00 43.40 ? 201 ILE B CG2   1 
ATOM   10745 C CD1   . ILE D  1 201 ? -33.789 70.359  -32.263 1.00 46.09 ? 201 ILE B CD1   1 
ATOM   10746 N N     . SER D  1 202 ? -29.167 72.762  -34.485 1.00 49.55 ? 202 SER B N     1 
ATOM   10747 C CA    . SER D  1 202 ? -27.765 73.013  -34.788 1.00 47.71 ? 202 SER B CA    1 
ATOM   10748 C C     . SER D  1 202 ? -27.384 74.437  -34.430 1.00 47.72 ? 202 SER B C     1 
ATOM   10749 O O     . SER D  1 202 ? -28.193 75.365  -34.494 1.00 50.63 ? 202 SER B O     1 
ATOM   10750 C CB    . SER D  1 202 ? -27.440 72.766  -36.268 1.00 51.32 ? 202 SER B CB    1 
ATOM   10751 O OG    . SER D  1 202 ? -26.047 72.875  -36.496 1.00 53.29 ? 202 SER B OG    1 
ATOM   10752 N N     . THR D  1 203 ? -26.121 74.590  -34.065 1.00 51.96 ? 203 THR B N     1 
ATOM   10753 C CA    . THR D  1 203 ? -25.518 75.867  -33.744 1.00 46.08 ? 203 THR B CA    1 
ATOM   10754 C C     . THR D  1 203 ? -24.953 76.562  -34.963 1.00 51.10 ? 203 THR B C     1 
ATOM   10755 O O     . THR D  1 203 ? -24.110 77.453  -34.826 1.00 54.85 ? 203 THR B O     1 
ATOM   10756 C CB    . THR D  1 203 ? -24.400 75.667  -32.733 1.00 51.30 ? 203 THR B CB    1 
ATOM   10757 O OG1   . THR D  1 203 ? -23.904 76.949  -32.344 1.00 74.75 ? 203 THR B OG1   1 
ATOM   10758 C CG2   . THR D  1 203 ? -23.262 74.876  -33.368 1.00 46.67 ? 203 THR B CG2   1 
ATOM   10759 N N     . SER D  1 204 ? -25.363 76.155  -36.157 1.00 53.35 ? 204 SER B N     1 
ATOM   10760 C CA    . SER D  1 204 ? -24.765 76.702  -37.358 1.00 56.47 ? 204 SER B CA    1 
ATOM   10761 C C     . SER D  1 204 ? -25.772 76.426  -38.450 1.00 56.89 ? 204 SER B C     1 
ATOM   10762 O O     . SER D  1 204 ? -26.327 75.321  -38.475 1.00 57.79 ? 204 SER B O     1 
ATOM   10763 C CB    . SER D  1 204 ? -23.415 76.049  -37.705 1.00 59.04 ? 204 SER B CB    1 
ATOM   10764 O OG    . SER D  1 204 ? -22.518 75.995  -36.595 1.00 51.60 ? 204 SER B OG    1 
ATOM   10765 N N     . PRO D  1 205 ? -26.066 77.385  -39.333 1.00 64.58 ? 205 PRO B N     1 
ATOM   10766 C CA    . PRO D  1 205 ? -26.887 77.079  -40.510 1.00 60.06 ? 205 PRO B CA    1 
ATOM   10767 C C     . PRO D  1 205 ? -26.125 76.354  -41.606 1.00 60.72 ? 205 PRO B C     1 
ATOM   10768 O O     . PRO D  1 205 ? -26.714 76.073  -42.657 1.00 61.10 ? 205 PRO B O     1 
ATOM   10769 C CB    . PRO D  1 205 ? -27.349 78.463  -40.993 1.00 59.51 ? 205 PRO B CB    1 
ATOM   10770 C CG    . PRO D  1 205 ? -26.318 79.413  -40.491 1.00 61.19 ? 205 PRO B CG    1 
ATOM   10771 C CD    . PRO D  1 205 ? -25.684 78.805  -39.259 1.00 64.43 ? 205 PRO B CD    1 
ATOM   10772 N N     . GLU D  1 206 ? -24.842 76.043  -41.389 1.00 59.65 ? 206 GLU B N     1 
ATOM   10773 C CA    . GLU D  1 206 ? -24.048 75.331  -42.383 1.00 63.58 ? 206 GLU B CA    1 
ATOM   10774 C C     . GLU D  1 206 ? -24.176 73.812  -42.262 1.00 62.18 ? 206 GLU B C     1 
ATOM   10775 O O     . GLU D  1 206 ? -24.205 73.116  -43.285 1.00 64.86 ? 206 GLU B O     1 
ATOM   10776 C CB    . GLU D  1 206 ? -22.573 75.739  -42.278 1.00 58.81 ? 206 GLU B CB    1 
ATOM   10777 C CG    . GLU D  1 206 ? -21.714 75.333  -43.487 1.00 65.37 ? 206 GLU B CG    1 
ATOM   10778 C CD    . GLU D  1 206 ? -21.444 73.824  -43.555 1.00 68.98 ? 206 GLU B CD    1 
ATOM   10779 O OE1   . GLU D  1 206 ? -21.234 73.206  -42.487 1.00 72.53 ? 206 GLU B OE1   1 
ATOM   10780 O OE2   . GLU D  1 206 ? -21.483 73.248  -44.666 1.00 63.74 ? 206 GLU B OE2   1 
ATOM   10781 N N     . SER D  1 207 ? -24.234 73.279  -41.043 1.00 57.95 ? 207 SER B N     1 
ATOM   10782 C CA    . SER D  1 207 ? -24.248 71.830  -40.859 1.00 56.40 ? 207 SER B CA    1 
ATOM   10783 C C     . SER D  1 207 ? -25.527 71.211  -41.419 1.00 49.47 ? 207 SER B C     1 
ATOM   10784 O O     . SER D  1 207 ? -26.610 71.796  -41.331 1.00 51.07 ? 207 SER B O     1 
ATOM   10785 C CB    . SER D  1 207 ? -24.098 71.495  -39.377 1.00 56.46 ? 207 SER B CB    1 
ATOM   10786 O OG    . SER D  1 207 ? -24.424 72.617  -38.564 1.00 56.97 ? 207 SER B OG    1 
ATOM   10787 N N     . SER D  1 208 ? -25.396 70.024  -42.011 1.00 45.30 ? 208 SER B N     1 
ATOM   10788 C CA    . SER D  1 208 ? -26.520 69.344  -42.648 1.00 53.29 ? 208 SER B CA    1 
ATOM   10789 C C     . SER D  1 208 ? -26.835 68.046  -41.906 1.00 47.87 ? 208 SER B C     1 
ATOM   10790 O O     . SER D  1 208 ? -25.978 67.478  -41.222 1.00 50.54 ? 208 SER B O     1 
ATOM   10791 C CB    . SER D  1 208 ? -26.239 69.092  -44.150 1.00 47.78 ? 208 SER B CB    1 
ATOM   10792 O OG    . SER D  1 208 ? -25.869 67.753  -44.422 1.00 50.77 ? 208 SER B OG    1 
ATOM   10793 N N     . PHE D  1 209 ? -28.090 67.588  -42.021 1.00 44.85 ? 209 PHE B N     1 
ATOM   10794 C CA    . PHE D  1 209 ? -28.660 66.576  -41.120 1.00 44.19 ? 209 PHE B CA    1 
ATOM   10795 C C     . PHE D  1 209 ? -29.398 65.485  -41.901 1.00 43.70 ? 209 PHE B C     1 
ATOM   10796 O O     . PHE D  1 209 ? -30.630 65.524  -42.037 1.00 44.37 ? 209 PHE B O     1 
ATOM   10797 C CB    . PHE D  1 209 ? -29.614 67.229  -40.107 1.00 47.41 ? 209 PHE B CB    1 
ATOM   10798 C CG    . PHE D  1 209 ? -28.927 67.924  -38.927 1.00 53.79 ? 209 PHE B CG    1 
ATOM   10799 C CD1   . PHE D  1 209 ? -27.961 68.913  -39.125 1.00 52.89 ? 209 PHE B CD1   1 
ATOM   10800 C CD2   . PHE D  1 209 ? -29.285 67.613  -37.615 1.00 49.73 ? 209 PHE B CD2   1 
ATOM   10801 C CE1   . PHE D  1 209 ? -27.345 69.553  -38.044 1.00 52.41 ? 209 PHE B CE1   1 
ATOM   10802 C CE2   . PHE D  1 209 ? -28.666 68.254  -36.533 1.00 48.70 ? 209 PHE B CE2   1 
ATOM   10803 C CZ    . PHE D  1 209 ? -27.702 69.225  -36.753 1.00 46.38 ? 209 PHE B CZ    1 
ATOM   10804 N N     . PRO D  1 210 ? -28.680 64.486  -42.419 1.00 43.79 ? 210 PRO B N     1 
ATOM   10805 C CA    . PRO D  1 210 ? -29.358 63.273  -42.906 1.00 43.86 ? 210 PRO B CA    1 
ATOM   10806 C C     . PRO D  1 210 ? -30.150 62.604  -41.791 1.00 45.22 ? 210 PRO B C     1 
ATOM   10807 O O     . PRO D  1 210 ? -29.769 62.641  -40.621 1.00 43.30 ? 210 PRO B O     1 
ATOM   10808 C CB    . PRO D  1 210 ? -28.206 62.376  -43.374 1.00 37.00 ? 210 PRO B CB    1 
ATOM   10809 C CG    . PRO D  1 210 ? -27.093 63.290  -43.639 1.00 37.82 ? 210 PRO B CG    1 
ATOM   10810 C CD    . PRO D  1 210 ? -27.234 64.459  -42.701 1.00 39.71 ? 210 PRO B CD    1 
ATOM   10811 N N     . GLY D  1 211 ? -31.256 61.964  -42.162 1.00 42.55 ? 211 GLY B N     1 
ATOM   10812 C CA    . GLY D  1 211 ? -32.072 61.308  -41.164 1.00 42.61 ? 211 GLY B CA    1 
ATOM   10813 C C     . GLY D  1 211 ? -32.994 62.228  -40.402 1.00 42.80 ? 211 GLY B C     1 
ATOM   10814 O O     . GLY D  1 211 ? -33.669 61.771  -39.476 1.00 39.26 ? 211 GLY B O     1 
ATOM   10815 N N     . THR D  1 212 ? -33.039 63.510  -40.758 1.00 47.64 ? 212 THR B N     1 
ATOM   10816 C CA    . THR D  1 212 ? -34.005 64.452  -40.218 1.00 46.89 ? 212 THR B CA    1 
ATOM   10817 C C     . THR D  1 212 ? -35.004 64.853  -41.287 1.00 45.00 ? 212 THR B C     1 
ATOM   10818 O O     . THR D  1 212 ? -34.703 64.826  -42.486 1.00 44.13 ? 212 THR B O     1 
ATOM   10819 C CB    . THR D  1 212 ? -33.334 65.724  -39.716 1.00 48.28 ? 212 THR B CB    1 
ATOM   10820 O OG1   . THR D  1 212 ? -32.616 66.315  -40.809 1.00 46.66 ? 212 THR B OG1   1 
ATOM   10821 C CG2   . THR D  1 212 ? -32.395 65.429  -38.547 1.00 47.36 ? 212 THR B CG2   1 
ATOM   10822 N N     . ARG D  1 213 ? -36.190 65.252  -40.834 1.00 42.73 ? 213 ARG B N     1 
ATOM   10823 C CA    . ARG D  1 213 ? -37.144 65.893  -41.727 1.00 48.26 ? 213 ARG B CA    1 
ATOM   10824 C C     . ARG D  1 213 ? -37.009 67.417  -41.717 1.00 50.02 ? 213 ARG B C     1 
ATOM   10825 O O     . ARG D  1 213 ? -37.294 68.059  -42.738 1.00 51.21 ? 213 ARG B O     1 
ATOM   10826 C CB    . ARG D  1 213 ? -38.579 65.465  -41.377 1.00 44.15 ? 213 ARG B CB    1 
ATOM   10827 C CG    . ARG D  1 213 ? -39.040 65.826  -39.979 1.00 45.89 ? 213 ARG B CG    1 
ATOM   10828 C CD    . ARG D  1 213 ? -40.554 65.729  -39.828 1.00 46.08 ? 213 ARG B CD    1 
ATOM   10829 N NE    . ARG D  1 213 ? -40.990 66.329  -38.570 1.00 49.94 ? 213 ARG B NE    1 
ATOM   10830 C CZ    . ARG D  1 213 ? -42.083 65.982  -37.899 1.00 51.44 ? 213 ARG B CZ    1 
ATOM   10831 N NH1   . ARG D  1 213 ? -42.909 65.052  -38.353 1.00 46.80 ? 213 ARG B NH1   1 
ATOM   10832 N NH2   . ARG D  1 213 ? -42.350 66.580  -36.738 1.00 47.31 ? 213 ARG B NH2   1 
ATOM   10833 N N     . GLU D  1 214 ? -36.557 68.011  -40.610 1.00 45.50 ? 214 GLU B N     1 
ATOM   10834 C CA    . GLU D  1 214 ? -36.270 69.441  -40.578 1.00 50.17 ? 214 GLU B CA    1 
ATOM   10835 C C     . GLU D  1 214 ? -35.194 69.746  -39.545 1.00 48.87 ? 214 GLU B C     1 
ATOM   10836 O O     . GLU D  1 214 ? -34.887 68.931  -38.668 1.00 46.46 ? 214 GLU B O     1 
ATOM   10837 C CB    . GLU D  1 214 ? -37.518 70.278  -40.274 1.00 53.22 ? 214 GLU B CB    1 
ATOM   10838 C CG    . GLU D  1 214 ? -38.153 70.056  -38.912 1.00 50.98 ? 214 GLU B CG    1 
ATOM   10839 C CD    . GLU D  1 214 ? -39.264 71.060  -38.631 1.00 57.41 ? 214 GLU B CD    1 
ATOM   10840 O OE1   . GLU D  1 214 ? -38.980 72.282  -38.550 1.00 56.61 ? 214 GLU B OE1   1 
ATOM   10841 O OE2   . GLU D  1 214 ? -40.433 70.619  -38.509 1.00 64.40 ? 214 GLU B OE2   1 
ATOM   10842 N N     . VAL D  1 215 ? -34.627 70.945  -39.654 1.00 44.16 ? 215 VAL B N     1 
ATOM   10843 C CA    . VAL D  1 215 ? -33.593 71.395  -38.734 1.00 45.36 ? 215 VAL B CA    1 
ATOM   10844 C C     . VAL D  1 215 ? -33.958 72.783  -38.234 1.00 45.31 ? 215 VAL B C     1 
ATOM   10845 O O     . VAL D  1 215 ? -34.061 73.727  -39.028 1.00 46.26 ? 215 VAL B O     1 
ATOM   10846 C CB    . VAL D  1 215 ? -32.196 71.416  -39.374 1.00 43.04 ? 215 VAL B CB    1 
ATOM   10847 C CG1   . VAL D  1 215 ? -31.177 71.918  -38.357 1.00 41.93 ? 215 VAL B CG1   1 
ATOM   10848 C CG2   . VAL D  1 215 ? -31.812 70.033  -39.863 1.00 44.89 ? 215 VAL B CG2   1 
ATOM   10849 N N     . LEU D  1 216 ? -34.126 72.913  -36.926 1.00 41.69 ? 216 LEU B N     1 
ATOM   10850 C CA    . LEU D  1 216 ? -34.274 74.214  -36.306 1.00 39.60 ? 216 LEU B CA    1 
ATOM   10851 C C     . LEU D  1 216 ? -32.913 74.743  -35.860 1.00 44.26 ? 216 LEU B C     1 
ATOM   10852 O O     . LEU D  1 216 ? -31.911 74.019  -35.821 1.00 40.39 ? 216 LEU B O     1 
ATOM   10853 C CB    . LEU D  1 216 ? -35.236 74.128  -35.126 1.00 41.32 ? 216 LEU B CB    1 
ATOM   10854 C CG    . LEU D  1 216 ? -36.671 73.783  -35.523 1.00 41.85 ? 216 LEU B CG    1 
ATOM   10855 C CD1   . LEU D  1 216 ? -37.352 73.026  -34.397 1.00 42.62 ? 216 LEU B CD1   1 
ATOM   10856 C CD2   . LEU D  1 216 ? -37.453 75.038  -35.895 1.00 48.16 ? 216 LEU B CD2   1 
ATOM   10857 N N     . ALA D  1 217 ? -32.884 76.035  -35.527 1.00 47.55 ? 217 ALA B N     1 
ATOM   10858 C CA    . ALA D  1 217 ? -31.680 76.706  -35.050 1.00 46.32 ? 217 ALA B CA    1 
ATOM   10859 C C     . ALA D  1 217 ? -31.698 76.806  -33.530 1.00 49.29 ? 217 ALA B C     1 
ATOM   10860 O O     . ALA D  1 217 ? -32.743 77.061  -32.926 1.00 44.27 ? 217 ALA B O     1 
ATOM   10861 C CB    . ALA D  1 217 ? -31.550 78.104  -35.661 1.00 41.19 ? 217 ALA B CB    1 
ATOM   10862 N N     . TYR D  1 218 ? -30.533 76.606  -32.914 1.00 52.93 ? 218 TYR B N     1 
ATOM   10863 C CA    . TYR D  1 218 ? -30.409 76.715  -31.466 1.00 55.44 ? 218 TYR B CA    1 
ATOM   10864 C C     . TYR D  1 218 ? -30.304 78.178  -31.050 1.00 51.18 ? 218 TYR B C     1 
ATOM   10865 O O     . TYR D  1 218 ? -29.606 78.965  -31.692 1.00 56.37 ? 218 TYR B O     1 
ATOM   10866 C CB    . TYR D  1 218 ? -29.181 75.940  -30.977 1.00 53.43 ? 218 TYR B CB    1 
ATOM   10867 C CG    . TYR D  1 218 ? -28.827 76.157  -29.515 1.00 50.79 ? 218 TYR B CG    1 
ATOM   10868 C CD1   . TYR D  1 218 ? -29.412 75.396  -28.515 1.00 50.89 ? 218 TYR B CD1   1 
ATOM   10869 C CD2   . TYR D  1 218 ? -27.899 77.120  -29.145 1.00 46.32 ? 218 TYR B CD2   1 
ATOM   10870 C CE1   . TYR D  1 218 ? -29.079 75.589  -27.189 1.00 55.49 ? 218 TYR B CE1   1 
ATOM   10871 C CE2   . TYR D  1 218 ? -27.565 77.325  -27.833 1.00 45.54 ? 218 TYR B CE2   1 
ATOM   10872 C CZ    . TYR D  1 218 ? -28.151 76.557  -26.851 1.00 58.54 ? 218 TYR B CZ    1 
ATOM   10873 O OH    . TYR D  1 218 ? -27.803 76.759  -25.524 1.00 59.40 ? 218 TYR B OH    1 
ATOM   10874 N N     . ALA D  1 219 ? -31.004 78.533  -29.971 1.00 50.88 ? 219 ALA B N     1 
ATOM   10875 C CA    . ALA D  1 219 ? -30.905 79.848  -29.343 1.00 49.82 ? 219 ALA B CA    1 
ATOM   10876 C C     . ALA D  1 219 ? -31.299 79.699  -27.883 1.00 57.40 ? 219 ALA B C     1 
ATOM   10877 O O     . ALA D  1 219 ? -32.355 79.124  -27.593 1.00 58.59 ? 219 ALA B O     1 
ATOM   10878 C CB    . ALA D  1 219 ? -31.810 80.880  -30.021 1.00 50.73 ? 219 ALA B CB    1 
ATOM   10879 N N     . ASN D  1 220 ? -30.455 80.203  -26.972 1.00 56.69 ? 220 ASN B N     1 
ATOM   10880 C CA    . ASN D  1 220 ? -30.776 80.119  -25.549 1.00 58.72 ? 220 ASN B CA    1 
ATOM   10881 C C     . ASN D  1 220 ? -32.068 80.856  -25.240 1.00 58.81 ? 220 ASN B C     1 
ATOM   10882 O O     . ASN D  1 220 ? -32.997 80.296  -24.644 1.00 61.48 ? 220 ASN B O     1 
ATOM   10883 C CB    . ASN D  1 220 ? -29.647 80.678  -24.693 1.00 60.31 ? 220 ASN B CB    1 
ATOM   10884 C CG    . ASN D  1 220 ? -29.939 80.533  -23.205 1.00 68.44 ? 220 ASN B CG    1 
ATOM   10885 O OD1   . ASN D  1 220 ? -30.549 81.413  -22.580 1.00 63.74 ? 220 ASN B OD1   1 
ATOM   10886 N ND2   . ASN D  1 220 ? -29.523 79.408  -22.633 1.00 70.81 ? 220 ASN B ND2   1 
ATOM   10887 N N     . ASP D  1 221 ? -32.129 82.131  -25.603 1.00 53.50 ? 221 ASP B N     1 
ATOM   10888 C CA    . ASP D  1 221 ? -33.422 82.774  -25.706 1.00 54.21 ? 221 ASP B CA    1 
ATOM   10889 C C     . ASP D  1 221 ? -34.342 81.827  -26.450 1.00 55.06 ? 221 ASP B C     1 
ATOM   10890 O O     . ASP D  1 221 ? -33.927 81.195  -27.423 1.00 58.66 ? 221 ASP B O     1 
ATOM   10891 C CB    . ASP D  1 221 ? -33.301 84.111  -26.442 1.00 60.31 ? 221 ASP B CB    1 
ATOM   10892 C CG    . ASP D  1 221 ? -32.513 83.998  -27.747 1.00 64.35 ? 221 ASP B CG    1 
ATOM   10893 O OD1   . ASP D  1 221 ? -31.264 84.134  -27.713 1.00 60.44 ? 221 ASP B OD1   1 
ATOM   10894 O OD2   . ASP D  1 221 ? -33.142 83.773  -28.807 1.00 65.90 ? 221 ASP B OD2   1 
ATOM   10895 N N     . GLN D  1 222 ? -35.557 81.668  -25.937 1.00 58.14 ? 222 GLN B N     1 
ATOM   10896 C CA    . GLN D  1 222 ? -36.593 80.792  -26.489 1.00 67.15 ? 222 GLN B CA    1 
ATOM   10897 C C     . GLN D  1 222 ? -36.188 79.310  -26.501 1.00 63.77 ? 222 GLN B C     1 
ATOM   10898 O O     . GLN D  1 222 ? -36.854 78.492  -27.152 1.00 63.42 ? 222 GLN B O     1 
ATOM   10899 C CB    . GLN D  1 222 ? -37.039 81.259  -27.897 1.00 62.88 ? 222 GLN B CB    1 
ATOM   10900 C CG    . GLN D  1 222 ? -36.240 80.722  -29.085 1.00 59.22 ? 222 GLN B CG    1 
ATOM   10901 C CD    . GLN D  1 222 ? -36.548 81.458  -30.363 1.00 66.24 ? 222 GLN B CD    1 
ATOM   10902 O OE1   . GLN D  1 222 ? -37.365 82.384  -30.380 1.00 67.15 ? 222 GLN B OE1   1 
ATOM   10903 N NE2   . GLN D  1 222 ? -35.886 81.061  -31.449 1.00 65.23 ? 222 GLN B NE2   1 
ATOM   10904 N N     . LEU D  1 223 ? -35.127 78.931  -25.781 1.00 57.89 ? 223 LEU B N     1 
ATOM   10905 C CA    . LEU D  1 223 ? -34.899 77.512  -25.524 1.00 56.21 ? 223 LEU B CA    1 
ATOM   10906 C C     . LEU D  1 223 ? -36.157 76.840  -24.998 1.00 52.39 ? 223 LEU B C     1 
ATOM   10907 O O     . LEU D  1 223 ? -36.345 75.637  -25.190 1.00 49.88 ? 223 LEU B O     1 
ATOM   10908 C CB    . LEU D  1 223 ? -33.760 77.325  -24.520 1.00 59.18 ? 223 LEU B CB    1 
ATOM   10909 C CG    . LEU D  1 223 ? -32.912 76.057  -24.611 1.00 65.07 ? 223 LEU B CG    1 
ATOM   10910 C CD1   . LEU D  1 223 ? -32.497 75.841  -26.067 1.00 70.75 ? 223 LEU B CD1   1 
ATOM   10911 C CD2   . LEU D  1 223 ? -31.687 76.083  -23.669 1.00 56.49 ? 223 LEU B CD2   1 
ATOM   10912 N N     . ASP D  1 224 ? -37.026 77.600  -24.327 1.00 52.72 ? 224 ASP B N     1 
ATOM   10913 C CA    . ASP D  1 224 ? -38.347 77.088  -23.981 1.00 54.73 ? 224 ASP B CA    1 
ATOM   10914 C C     . ASP D  1 224 ? -39.208 76.923  -25.229 1.00 55.34 ? 224 ASP B C     1 
ATOM   10915 O O     . ASP D  1 224 ? -40.022 75.995  -25.314 1.00 56.29 ? 224 ASP B O     1 
ATOM   10916 C CB    . ASP D  1 224 ? -39.043 78.019  -22.974 1.00 53.05 ? 224 ASP B CB    1 
ATOM   10917 C CG    . ASP D  1 224 ? -38.103 78.541  -21.893 1.00 56.19 ? 224 ASP B CG    1 
ATOM   10918 O OD1   . ASP D  1 224 ? -37.247 79.400  -22.210 1.00 55.55 ? 224 ASP B OD1   1 
ATOM   10919 O OD2   . ASP D  1 224 ? -38.234 78.100  -20.725 1.00 49.39 ? 224 ASP B OD2   1 
ATOM   10920 N N     . THR D  1 225 ? -39.052 77.820  -26.204 1.00 53.76 ? 225 THR B N     1 
ATOM   10921 C CA    . THR D  1 225 ? -39.864 77.725  -27.411 1.00 58.24 ? 225 THR B CA    1 
ATOM   10922 C C     . THR D  1 225 ? -39.574 76.428  -28.155 1.00 56.06 ? 225 THR B C     1 
ATOM   10923 O O     . THR D  1 225 ? -40.498 75.741  -28.607 1.00 58.85 ? 225 THR B O     1 
ATOM   10924 C CB    . THR D  1 225 ? -39.617 78.937  -28.318 1.00 65.37 ? 225 THR B CB    1 
ATOM   10925 O OG1   . THR D  1 225 ? -40.057 80.139  -27.663 1.00 66.40 ? 225 THR B OG1   1 
ATOM   10926 C CG2   . THR D  1 225 ? -40.351 78.777  -29.646 1.00 66.21 ? 225 THR B CG2   1 
ATOM   10927 N N     . LEU D  1 226 ? -38.296 76.068  -28.274 1.00 55.53 ? 226 LEU B N     1 
ATOM   10928 C CA    . LEU D  1 226 ? -37.934 74.834  -28.959 1.00 53.40 ? 226 LEU B CA    1 
ATOM   10929 C C     . LEU D  1 226 ? -38.447 73.627  -28.202 1.00 49.09 ? 226 LEU B C     1 
ATOM   10930 O O     . LEU D  1 226 ? -39.213 72.819  -28.735 1.00 50.64 ? 226 LEU B O     1 
ATOM   10931 C CB    . LEU D  1 226 ? -36.420 74.752  -29.126 1.00 49.78 ? 226 LEU B CB    1 
ATOM   10932 C CG    . LEU D  1 226 ? -35.944 75.550  -30.335 1.00 53.35 ? 226 LEU B CG    1 
ATOM   10933 C CD1   . LEU D  1 226 ? -34.604 76.186  -30.049 1.00 56.94 ? 226 LEU B CD1   1 
ATOM   10934 C CD2   . LEU D  1 226 ? -35.870 74.646  -31.550 1.00 51.45 ? 226 LEU B CD2   1 
ATOM   10935 N N     . ALA D  1 227 ? -38.036 73.495  -26.943 1.00 49.22 ? 227 ALA B N     1 
ATOM   10936 C CA    . ALA D  1 227 ? -38.494 72.381  -26.128 1.00 46.56 ? 227 ALA B CA    1 
ATOM   10937 C C     . ALA D  1 227 ? -40.007 72.297  -26.089 1.00 49.25 ? 227 ALA B C     1 
ATOM   10938 O O     . ALA D  1 227 ? -40.554 71.205  -25.895 1.00 49.87 ? 227 ALA B O     1 
ATOM   10939 C CB    . ALA D  1 227 ? -37.943 72.499  -24.712 1.00 46.93 ? 227 ALA B CB    1 
ATOM   10940 N N     . ASP D  1 228 ? -40.697 73.418  -26.284 1.00 51.42 ? 228 ASP B N     1 
ATOM   10941 C CA    . ASP D  1 228 ? -42.143 73.353  -26.425 1.00 53.12 ? 228 ASP B CA    1 
ATOM   10942 C C     . ASP D  1 228 ? -42.549 72.913  -27.827 1.00 51.15 ? 228 ASP B C     1 
ATOM   10943 O O     . ASP D  1 228 ? -43.475 72.105  -27.974 1.00 49.56 ? 228 ASP B O     1 
ATOM   10944 C CB    . ASP D  1 228 ? -42.770 74.703  -26.080 1.00 60.85 ? 228 ASP B CB    1 
ATOM   10945 C CG    . ASP D  1 228 ? -43.088 74.827  -24.599 1.00 64.84 ? 228 ASP B CG    1 
ATOM   10946 O OD1   . ASP D  1 228 ? -42.843 73.839  -23.868 1.00 57.81 ? 228 ASP B OD1   1 
ATOM   10947 O OD2   . ASP D  1 228 ? -43.581 75.900  -24.172 1.00 59.69 ? 228 ASP B OD2   1 
ATOM   10948 N N     . THR D  1 229 ? -41.862 73.424  -28.859 1.00 52.40 ? 229 THR B N     1 
ATOM   10949 C CA    . THR D  1 229 ? -42.194 73.076  -30.242 1.00 49.95 ? 229 THR B CA    1 
ATOM   10950 C C     . THR D  1 229 ? -41.946 71.600  -30.513 1.00 45.96 ? 229 THR B C     1 
ATOM   10951 O O     . THR D  1 229 ? -42.831 70.888  -31.001 1.00 45.08 ? 229 THR B O     1 
ATOM   10952 C CB    . THR D  1 229 ? -41.383 73.927  -31.217 1.00 49.88 ? 229 THR B CB    1 
ATOM   10953 O OG1   . THR D  1 229 ? -42.039 75.188  -31.399 1.00 58.51 ? 229 THR B OG1   1 
ATOM   10954 C CG2   . THR D  1 229 ? -41.258 73.221  -32.565 1.00 40.39 ? 229 THR B CG2   1 
ATOM   10955 N N     . LEU D  1 230 ? -40.728 71.135  -30.227 1.00 47.95 ? 230 LEU B N     1 
ATOM   10956 C CA    . LEU D  1 230 ? -40.408 69.712  -30.227 1.00 47.72 ? 230 LEU B CA    1 
ATOM   10957 C C     . LEU D  1 230 ? -41.502 68.886  -29.574 1.00 50.83 ? 230 LEU B C     1 
ATOM   10958 O O     . LEU D  1 230 ? -42.174 68.081  -30.231 1.00 50.80 ? 230 LEU B O     1 
ATOM   10959 C CB    . LEU D  1 230 ? -39.092 69.483  -29.481 1.00 43.39 ? 230 LEU B CB    1 
ATOM   10960 C CG    . LEU D  1 230 ? -37.893 70.145  -30.131 1.00 45.39 ? 230 LEU B CG    1 
ATOM   10961 C CD1   . LEU D  1 230 ? -36.617 69.619  -29.493 1.00 39.39 ? 230 LEU B CD1   1 
ATOM   10962 C CD2   . LEU D  1 230 ? -37.936 69.886  -31.620 1.00 36.16 ? 230 LEU B CD2   1 
ATOM   10963 N N     . TRP D  1 231 ? -41.690 69.111  -28.266 1.00 47.84 ? 231 TRP B N     1 
ATOM   10964 C CA    . TRP D  1 231 ? -42.580 68.282  -27.463 1.00 45.48 ? 231 TRP B CA    1 
ATOM   10965 C C     . TRP D  1 231 ? -43.978 68.234  -28.058 1.00 44.89 ? 231 TRP B C     1 
ATOM   10966 O O     . TRP D  1 231 ? -44.643 67.192  -28.020 1.00 47.44 ? 231 TRP B O     1 
ATOM   10967 C CB    . TRP D  1 231 ? -42.616 68.795  -26.017 1.00 42.42 ? 231 TRP B CB    1 
ATOM   10968 C CG    . TRP D  1 231 ? -43.409 67.916  -25.119 1.00 41.41 ? 231 TRP B CG    1 
ATOM   10969 C CD1   . TRP D  1 231 ? -44.674 68.133  -24.678 1.00 42.46 ? 231 TRP B CD1   1 
ATOM   10970 C CD2   . TRP D  1 231 ? -43.008 66.654  -24.582 1.00 41.02 ? 231 TRP B CD2   1 
ATOM   10971 N NE1   . TRP D  1 231 ? -45.084 67.098  -23.883 1.00 37.69 ? 231 TRP B NE1   1 
ATOM   10972 C CE2   . TRP D  1 231 ? -44.081 66.170  -23.813 1.00 41.64 ? 231 TRP B CE2   1 
ATOM   10973 C CE3   . TRP D  1 231 ? -41.845 65.891  -24.670 1.00 37.43 ? 231 TRP B CE3   1 
ATOM   10974 C CZ2   . TRP D  1 231 ? -44.030 64.950  -23.140 1.00 41.49 ? 231 TRP B CZ2   1 
ATOM   10975 C CZ3   . TRP D  1 231 ? -41.791 64.690  -24.002 1.00 37.40 ? 231 TRP B CZ3   1 
ATOM   10976 C CH2   . TRP D  1 231 ? -42.880 64.225  -23.252 1.00 40.68 ? 231 TRP B CH2   1 
ATOM   10977 N N     . SER D  1 232 ? -44.424 69.342  -28.648 1.00 48.28 ? 232 SER B N     1 
ATOM   10978 C CA    . SER D  1 232 ? -45.732 69.390  -29.294 1.00 48.57 ? 232 SER B CA    1 
ATOM   10979 C C     . SER D  1 232 ? -45.725 68.668  -30.633 1.00 51.25 ? 232 SER B C     1 
ATOM   10980 O O     . SER D  1 232 ? -46.717 68.027  -31.005 1.00 49.28 ? 232 SER B O     1 
ATOM   10981 C CB    . SER D  1 232 ? -46.147 70.842  -29.478 1.00 43.31 ? 232 SER B CB    1 
ATOM   10982 O OG    . SER D  1 232 ? -44.988 71.630  -29.692 1.00 49.17 ? 232 SER B OG    1 
ATOM   10983 N N     . GLN D  1 233 ? -44.611 68.762  -31.364 1.00 51.56 ? 233 GLN B N     1 
ATOM   10984 C CA    . GLN D  1 233 ? -44.531 68.128  -32.674 1.00 51.62 ? 233 GLN B CA    1 
ATOM   10985 C C     . GLN D  1 233 ? -44.368 66.618  -32.553 1.00 47.58 ? 233 GLN B C     1 
ATOM   10986 O O     . GLN D  1 233 ? -44.951 65.862  -33.336 1.00 45.15 ? 233 GLN B O     1 
ATOM   10987 C CB    . GLN D  1 233 ? -43.367 68.721  -33.467 1.00 50.93 ? 233 GLN B CB    1 
ATOM   10988 C CG    . GLN D  1 233 ? -43.565 70.160  -33.880 1.00 48.83 ? 233 GLN B CG    1 
ATOM   10989 C CD    . GLN D  1 233 ? -42.889 70.474  -35.195 1.00 52.82 ? 233 GLN B CD    1 
ATOM   10990 O OE1   . GLN D  1 233 ? -41.971 71.297  -35.256 1.00 55.87 ? 233 GLN B OE1   1 
ATOM   10991 N NE2   . GLN D  1 233 ? -43.332 69.810  -36.260 1.00 53.89 ? 233 GLN B NE2   1 
ATOM   10992 N N     . LEU D  1 234 ? -43.575 66.159  -31.579 1.00 45.42 ? 234 LEU B N     1 
ATOM   10993 C CA    . LEU D  1 234 ? -43.091 64.784  -31.581 1.00 46.74 ? 234 LEU B CA    1 
ATOM   10994 C C     . LEU D  1 234 ? -43.657 63.946  -30.444 1.00 49.48 ? 234 LEU B C     1 
ATOM   10995 O O     . LEU D  1 234 ? -43.114 62.877  -30.151 1.00 45.33 ? 234 LEU B O     1 
ATOM   10996 C CB    . LEU D  1 234 ? -41.561 64.748  -31.542 1.00 39.23 ? 234 LEU B CB    1 
ATOM   10997 C CG    . LEU D  1 234 ? -40.823 65.549  -32.623 1.00 43.92 ? 234 LEU B CG    1 
ATOM   10998 C CD1   . LEU D  1 234 ? -39.353 65.182  -32.660 1.00 44.68 ? 234 LEU B CD1   1 
ATOM   10999 C CD2   . LEU D  1 234 ? -41.446 65.372  -34.004 1.00 43.98 ? 234 LEU B CD2   1 
ATOM   11000 N N     . THR D  1 235 ? -44.734 64.394  -29.799 1.00 49.21 ? 235 THR B N     1 
ATOM   11001 C CA    . THR D  1 235 ? -45.404 63.591  -28.787 1.00 45.34 ? 235 THR B CA    1 
ATOM   11002 C C     . THR D  1 235 ? -46.891 63.507  -29.082 1.00 37.47 ? 235 THR B C     1 
ATOM   11003 O O     . THR D  1 235 ? -47.486 64.408  -29.675 1.00 38.31 ? 235 THR B O     1 
ATOM   11004 C CB    . THR D  1 235 ? -45.225 64.149  -27.376 1.00 38.29 ? 235 THR B CB    1 
ATOM   11005 O OG1   . THR D  1 235 ? -45.797 65.456  -27.317 1.00 43.64 ? 235 THR B OG1   1 
ATOM   11006 C CG2   . THR D  1 235 ? -43.769 64.220  -27.004 1.00 41.16 ? 235 THR B CG2   1 
ATOM   11007 N N     . ASP D  1 236 ? -47.484 62.410  -28.642 1.00 37.82 ? 236 ASP B N     1 
ATOM   11008 C CA    . ASP D  1 236 ? -48.912 62.212  -28.759 1.00 37.90 ? 236 ASP B CA    1 
ATOM   11009 C C     . ASP D  1 236 ? -49.333 61.281  -27.632 1.00 43.93 ? 236 ASP B C     1 
ATOM   11010 O O     . ASP D  1 236 ? -48.556 61.018  -26.706 1.00 43.39 ? 236 ASP B O     1 
ATOM   11011 C CB    . ASP D  1 236 ? -49.255 61.686  -30.153 1.00 40.62 ? 236 ASP B CB    1 
ATOM   11012 C CG    . ASP D  1 236 ? -48.687 60.315  -30.400 1.00 49.34 ? 236 ASP B CG    1 
ATOM   11013 O OD1   . ASP D  1 236 ? -47.669 59.978  -29.753 1.00 50.13 ? 236 ASP B OD1   1 
ATOM   11014 O OD2   . ASP D  1 236 ? -49.242 59.585  -31.249 1.00 52.37 ? 236 ASP B OD2   1 
ATOM   11015 N N     . THR D  1 237 ? -50.570 60.779  -27.709 1.00 46.62 ? 237 THR B N     1 
ATOM   11016 C CA    . THR D  1 237 ? -51.150 60.065  -26.570 1.00 49.25 ? 237 THR B CA    1 
ATOM   11017 C C     . THR D  1 237 ? -50.365 58.801  -26.244 1.00 45.25 ? 237 THR B C     1 
ATOM   11018 O O     . THR D  1 237 ? -49.923 58.597  -25.108 1.00 47.97 ? 237 THR B O     1 
ATOM   11019 C CB    . THR D  1 237 ? -52.607 59.711  -26.853 1.00 49.60 ? 237 THR B CB    1 
ATOM   11020 O OG1   . THR D  1 237 ? -53.357 60.908  -27.098 1.00 46.02 ? 237 THR B OG1   1 
ATOM   11021 C CG2   . THR D  1 237 ? -53.193 58.950  -25.655 1.00 45.12 ? 237 THR B CG2   1 
ATOM   11022 N N     . GLN D  1 238 ? -50.202 57.931  -27.235 1.00 47.80 ? 238 GLN B N     1 
ATOM   11023 C CA    . GLN D  1 238 ? -49.469 56.691  -27.029 1.00 49.04 ? 238 GLN B CA    1 
ATOM   11024 C C     . GLN D  1 238 ? -48.020 56.962  -26.645 1.00 45.97 ? 238 GLN B C     1 
ATOM   11025 O O     . GLN D  1 238 ? -47.458 56.270  -25.788 1.00 47.09 ? 238 GLN B O     1 
ATOM   11026 C CB    . GLN D  1 238 ? -49.549 55.842  -28.299 1.00 44.72 ? 238 GLN B CB    1 
ATOM   11027 C CG    . GLN D  1 238 ? -50.969 55.332  -28.632 1.00 49.70 ? 238 GLN B CG    1 
ATOM   11028 C CD    . GLN D  1 238 ? -51.925 56.440  -29.082 1.00 51.83 ? 238 GLN B CD    1 
ATOM   11029 O OE1   . GLN D  1 238 ? -51.493 57.552  -29.399 1.00 49.41 ? 238 GLN B OE1   1 
ATOM   11030 N NE2   . GLN D  1 238 ? -53.229 56.142  -29.096 1.00 47.52 ? 238 GLN B NE2   1 
ATOM   11031 N N     . ASN D  1 239 ? -47.412 57.984  -27.241 1.00 43.32 ? 239 ASN B N     1 
ATOM   11032 C CA    . ASN D  1 239 ? -45.969 58.183  -27.189 1.00 41.93 ? 239 ASN B CA    1 
ATOM   11033 C C     . ASN D  1 239 ? -45.650 59.423  -26.357 1.00 42.58 ? 239 ASN B C     1 
ATOM   11034 O O     . ASN D  1 239 ? -45.817 60.554  -26.824 1.00 41.14 ? 239 ASN B O     1 
ATOM   11035 C CB    . ASN D  1 239 ? -45.415 58.288  -28.603 1.00 40.58 ? 239 ASN B CB    1 
ATOM   11036 C CG    . ASN D  1 239 ? -45.568 56.998  -29.391 1.00 41.31 ? 239 ASN B CG    1 
ATOM   11037 O OD1   . ASN D  1 239 ? -45.184 55.926  -28.931 1.00 45.10 ? 239 ASN B OD1   1 
ATOM   11038 N ND2   . ASN D  1 239 ? -46.156 57.095  -30.574 1.00 38.03 ? 239 ASN B ND2   1 
ATOM   11039 N N     . GLN D  1 240 ? -45.165 59.198  -25.128 1.00 41.64 ? 240 GLN B N     1 
ATOM   11040 C CA    . GLN D  1 240 ? -44.816 60.258  -24.188 1.00 33.91 ? 240 GLN B CA    1 
ATOM   11041 C C     . GLN D  1 240 ? -43.318 60.285  -23.891 1.00 38.74 ? 240 GLN B C     1 
ATOM   11042 O O     . GLN D  1 240 ? -42.904 60.722  -22.811 1.00 38.12 ? 240 GLN B O     1 
ATOM   11043 C CB    . GLN D  1 240 ? -45.610 60.096  -22.892 1.00 30.91 ? 240 GLN B CB    1 
ATOM   11044 C CG    . GLN D  1 240 ? -47.106 60.361  -23.024 1.00 38.97 ? 240 GLN B CG    1 
ATOM   11045 C CD    . GLN D  1 240 ? -47.436 61.821  -23.403 1.00 46.79 ? 240 GLN B CD    1 
ATOM   11046 O OE1   . GLN D  1 240 ? -46.908 62.765  -22.808 1.00 37.99 ? 240 GLN B OE1   1 
ATOM   11047 N NE2   . GLN D  1 240 ? -48.308 62.002  -24.402 1.00 40.29 ? 240 GLN B NE2   1 
ATOM   11048 N N     . PHE D  1 241 ? -42.495 59.799  -24.832 1.00 34.76 ? 241 PHE B N     1 
ATOM   11049 C CA    . PHE D  1 241 ? -41.035 59.862  -24.737 1.00 38.77 ? 241 PHE B CA    1 
ATOM   11050 C C     . PHE D  1 241 ? -40.462 60.457  -26.016 1.00 40.25 ? 241 PHE B C     1 
ATOM   11051 O O     . PHE D  1 241 ? -40.743 59.964  -27.113 1.00 40.12 ? 241 PHE B O     1 
ATOM   11052 C CB    . PHE D  1 241 ? -40.364 58.472  -24.536 1.00 36.78 ? 241 PHE B CB    1 
ATOM   11053 C CG    . PHE D  1 241 ? -40.670 57.781  -23.220 1.00 34.38 ? 241 PHE B CG    1 
ATOM   11054 C CD1   . PHE D  1 241 ? -40.850 58.493  -22.048 1.00 32.58 ? 241 PHE B CD1   1 
ATOM   11055 C CD2   . PHE D  1 241 ? -40.761 56.390  -23.174 1.00 28.03 ? 241 PHE B CD2   1 
ATOM   11056 C CE1   . PHE D  1 241 ? -41.133 57.816  -20.869 1.00 32.04 ? 241 PHE B CE1   1 
ATOM   11057 C CE2   . PHE D  1 241 ? -41.032 55.721  -22.010 1.00 22.04 ? 241 PHE B CE2   1 
ATOM   11058 C CZ    . PHE D  1 241 ? -41.216 56.424  -20.856 1.00 24.66 ? 241 PHE B CZ    1 
ATOM   11059 N N     . ILE D  1 242 ? -39.618 61.472  -25.879 1.00 38.20 ? 242 ILE B N     1 
ATOM   11060 C CA    . ILE D  1 242 ? -38.734 61.908  -26.951 1.00 33.80 ? 242 ILE B CA    1 
ATOM   11061 C C     . ILE D  1 242 ? -37.325 61.461  -26.598 1.00 34.69 ? 242 ILE B C     1 
ATOM   11062 O O     . ILE D  1 242 ? -36.932 61.495  -25.432 1.00 38.60 ? 242 ILE B O     1 
ATOM   11063 C CB    . ILE D  1 242 ? -38.751 63.435  -27.140 1.00 39.21 ? 242 ILE B CB    1 
ATOM   11064 C CG1   . ILE D  1 242 ? -40.120 63.929  -27.565 1.00 39.28 ? 242 ILE B CG1   1 
ATOM   11065 C CG2   . ILE D  1 242 ? -37.666 63.870  -28.111 1.00 40.73 ? 242 ILE B CG2   1 
ATOM   11066 C CD1   . ILE D  1 242 ? -40.184 65.440  -27.602 1.00 47.43 ? 242 ILE B CD1   1 
ATOM   11067 N N     . THR D  1 243 ? -36.565 61.071  -27.597 1.00 34.65 ? 243 THR B N     1 
ATOM   11068 C CA    . THR D  1 243 ? -35.155 60.759  -27.431 1.00 32.92 ? 243 THR B CA    1 
ATOM   11069 C C     . THR D  1 243 ? -34.319 61.916  -27.978 1.00 37.57 ? 243 THR B C     1 
ATOM   11070 O O     . THR D  1 243 ? -34.425 62.263  -29.161 1.00 40.45 ? 243 THR B O     1 
ATOM   11071 C CB    . THR D  1 243 ? -34.828 59.455  -28.153 1.00 33.20 ? 243 THR B CB    1 
ATOM   11072 O OG1   . THR D  1 243 ? -35.514 58.379  -27.503 1.00 32.89 ? 243 THR B OG1   1 
ATOM   11073 C CG2   . THR D  1 243 ? -33.361 59.186  -28.112 1.00 33.36 ? 243 THR B CG2   1 
ATOM   11074 N N     . VAL D  1 244 ? -33.485 62.507  -27.125 1.00 39.25 ? 244 VAL B N     1 
ATOM   11075 C CA    . VAL D  1 244 ? -32.632 63.637  -27.497 1.00 41.47 ? 244 VAL B CA    1 
ATOM   11076 C C     . VAL D  1 244 ? -31.176 63.186  -27.409 1.00 40.57 ? 244 VAL B C     1 
ATOM   11077 O O     . VAL D  1 244 ? -30.744 62.688  -26.361 1.00 36.85 ? 244 VAL B O     1 
ATOM   11078 C CB    . VAL D  1 244 ? -32.904 64.855  -26.598 1.00 42.51 ? 244 VAL B CB    1 
ATOM   11079 C CG1   . VAL D  1 244 ? -32.086 66.064  -27.048 1.00 41.76 ? 244 VAL B CG1   1 
ATOM   11080 C CG2   . VAL D  1 244 ? -34.413 65.177  -26.573 1.00 37.65 ? 244 VAL B CG2   1 
ATOM   11081 N N     . GLU D  1 245 ? -30.419 63.355  -28.506 1.00 41.34 ? 245 GLU B N     1 
ATOM   11082 C CA    . GLU D  1 245 ? -29.072 62.780  -28.636 1.00 43.55 ? 245 GLU B CA    1 
ATOM   11083 C C     . GLU D  1 245 ? -28.062 63.793  -29.193 1.00 45.40 ? 245 GLU B C     1 
ATOM   11084 O O     . GLU D  1 245 ? -28.409 64.700  -29.962 1.00 38.66 ? 245 GLU B O     1 
ATOM   11085 C CB    . GLU D  1 245 ? -29.000 61.555  -29.579 1.00 40.94 ? 245 GLU B CB    1 
ATOM   11086 C CG    . GLU D  1 245 ? -30.040 60.557  -29.509 1.00 45.43 ? 245 GLU B CG    1 
ATOM   11087 C CD    . GLU D  1 245 ? -29.709 59.355  -30.367 1.00 45.32 ? 245 GLU B CD    1 
ATOM   11088 O OE1   . GLU D  1 245 ? -28.778 59.446  -31.253 1.00 50.41 ? 245 GLU B OE1   1 
ATOM   11089 O OE2   . GLU D  1 245 ? -30.353 58.283  -30.087 1.00 36.95 ? 245 GLU B OE2   1 
ATOM   11090 N N     . THR D  1 246 ? -26.780 63.605  -28.843 1.00 40.78 ? 246 THR B N     1 
ATOM   11091 C CA    . THR D  1 246 ? -25.707 64.297  -29.567 1.00 43.32 ? 246 THR B CA    1 
ATOM   11092 C C     . THR D  1 246 ? -25.633 63.823  -31.026 1.00 46.36 ? 246 THR B C     1 
ATOM   11093 O O     . THR D  1 246 ? -25.284 62.668  -31.299 1.00 42.66 ? 246 THR B O     1 
ATOM   11094 C CB    . THR D  1 246 ? -24.345 64.092  -28.885 1.00 44.47 ? 246 THR B CB    1 
ATOM   11095 O OG1   . THR D  1 246 ? -24.291 64.846  -27.672 1.00 42.29 ? 246 THR B OG1   1 
ATOM   11096 C CG2   . THR D  1 246 ? -23.220 64.586  -29.785 1.00 47.10 ? 246 THR B CG2   1 
ATOM   11097 N N     . TYR D  1 247 ? -25.965 64.699  -31.970 1.00 42.74 ? 247 TYR B N     1 
ATOM   11098 C CA    . TYR D  1 247 ? -25.859 64.347  -33.378 1.00 45.41 ? 247 TYR B CA    1 
ATOM   11099 C C     . TYR D  1 247 ? -24.405 64.389  -33.834 1.00 48.07 ? 247 TYR B C     1 
ATOM   11100 O O     . TYR D  1 247 ? -23.611 65.217  -33.375 1.00 45.64 ? 247 TYR B O     1 
ATOM   11101 C CB    . TYR D  1 247 ? -26.693 65.292  -34.233 1.00 45.56 ? 247 TYR B CB    1 
ATOM   11102 C CG    . TYR D  1 247 ? -26.857 64.801  -35.637 1.00 45.52 ? 247 TYR B CG    1 
ATOM   11103 C CD1   . TYR D  1 247 ? -27.832 63.866  -35.953 1.00 44.00 ? 247 TYR B CD1   1 
ATOM   11104 C CD2   . TYR D  1 247 ? -26.032 65.256  -36.641 1.00 44.12 ? 247 TYR B CD2   1 
ATOM   11105 C CE1   . TYR D  1 247 ? -27.981 63.414  -37.222 1.00 38.36 ? 247 TYR B CE1   1 
ATOM   11106 C CE2   . TYR D  1 247 ? -26.175 64.806  -37.910 1.00 41.68 ? 247 TYR B CE2   1 
ATOM   11107 C CZ    . TYR D  1 247 ? -27.144 63.888  -38.196 1.00 39.43 ? 247 TYR B CZ    1 
ATOM   11108 O OH    . TYR D  1 247 ? -27.274 63.448  -39.486 1.00 43.53 ? 247 TYR B OH    1 
ATOM   11109 N N     . HIS D  1 248 ? -24.060 63.485  -34.749 1.00 48.62 ? 248 HIS B N     1 
ATOM   11110 C CA    . HIS D  1 248 ? -22.681 63.321  -35.196 1.00 49.23 ? 248 HIS B CA    1 
ATOM   11111 C C     . HIS D  1 248 ? -22.596 63.312  -36.712 1.00 46.64 ? 248 HIS B C     1 
ATOM   11112 O O     . HIS D  1 248 ? -23.484 62.799  -37.399 1.00 51.97 ? 248 HIS B O     1 
ATOM   11113 C CB    . HIS D  1 248 ? -22.064 62.024  -34.681 1.00 42.23 ? 248 HIS B CB    1 
ATOM   11114 C CG    . HIS D  1 248 ? -21.810 62.020  -33.213 1.00 43.36 ? 248 HIS B CG    1 
ATOM   11115 N ND1   . HIS D  1 248 ? -20.561 62.238  -32.676 1.00 43.78 ? 248 HIS B ND1   1 
ATOM   11116 C CD2   . HIS D  1 248 ? -22.644 61.824  -32.166 1.00 44.97 ? 248 HIS B CD2   1 
ATOM   11117 C CE1   . HIS D  1 248 ? -20.637 62.179  -31.359 1.00 41.63 ? 248 HIS B CE1   1 
ATOM   11118 N NE2   . HIS D  1 248 ? -21.890 61.929  -31.025 1.00 44.26 ? 248 HIS B NE2   1 
ATOM   11119 N N     . ARG D  1 249 ? -21.502 63.866  -37.221 1.00 46.48 ? 249 ARG B N     1 
ATOM   11120 C CA    . ARG D  1 249 ? -21.154 63.776  -38.635 1.00 50.86 ? 249 ARG B CA    1 
ATOM   11121 C C     . ARG D  1 249 ? -20.185 62.615  -38.815 1.00 51.44 ? 249 ARG B C     1 
ATOM   11122 O O     . ARG D  1 249 ? -19.147 62.563  -38.150 1.00 56.52 ? 249 ARG B O     1 
ATOM   11123 C CB    . ARG D  1 249 ? -20.528 65.083  -39.125 1.00 50.30 ? 249 ARG B CB    1 
ATOM   11124 C CG    . ARG D  1 249 ? -19.960 65.032  -40.549 1.00 62.66 ? 249 ARG B CG    1 
ATOM   11125 C CD    . ARG D  1 249 ? -18.422 65.153  -40.578 1.00 66.99 ? 249 ARG B CD    1 
ATOM   11126 N NE    . ARG D  1 249 ? -17.764 64.019  -39.935 1.00 67.46 ? 249 ARG B NE    1 
ATOM   11127 C CZ    . ARG D  1 249 ? -17.361 62.918  -40.561 1.00 60.82 ? 249 ARG B CZ    1 
ATOM   11128 N NH1   . ARG D  1 249 ? -17.472 62.788  -41.875 1.00 58.67 ? 249 ARG B NH1   1 
ATOM   11129 N NH2   . ARG D  1 249 ? -16.843 61.919  -39.847 1.00 56.15 ? 249 ARG B NH2   1 
ATOM   11130 N N     . ALA D  1 250 ? -20.513 61.691  -39.705 1.00 47.58 ? 250 ALA B N     1 
ATOM   11131 C CA    . ALA D  1 250 ? -19.777 60.442  -39.775 1.00 45.15 ? 250 ALA B CA    1 
ATOM   11132 C C     . ALA D  1 250 ? -19.268 60.155  -41.181 1.00 53.07 ? 250 ALA B C     1 
ATOM   11133 O O     . ALA D  1 250 ? -19.866 60.551  -42.192 1.00 45.40 ? 250 ALA B O     1 
ATOM   11134 C CB    . ALA D  1 250 ? -20.634 59.271  -39.309 1.00 46.29 ? 250 ALA B CB    1 
ATOM   11135 N N     . ASP D  1 251 ? -18.140 59.443  -41.219 1.00 48.32 ? 251 ASP B N     1 
ATOM   11136 C CA    . ASP D  1 251 ? -17.652 58.902  -42.474 1.00 44.90 ? 251 ASP B CA    1 
ATOM   11137 C C     . ASP D  1 251 ? -18.704 58.021  -43.132 1.00 45.34 ? 251 ASP B C     1 
ATOM   11138 O O     . ASP D  1 251 ? -19.009 58.189  -44.317 1.00 52.59 ? 251 ASP B O     1 
ATOM   11139 C CB    . ASP D  1 251 ? -16.364 58.118  -42.241 1.00 45.27 ? 251 ASP B CB    1 
ATOM   11140 C CG    . ASP D  1 251 ? -15.743 57.643  -43.528 1.00 44.47 ? 251 ASP B CG    1 
ATOM   11141 O OD1   . ASP D  1 251 ? -15.978 58.287  -44.577 1.00 44.32 ? 251 ASP B OD1   1 
ATOM   11142 O OD2   . ASP D  1 251 ? -15.024 56.626  -43.491 1.00 52.19 ? 251 ASP B OD2   1 
ATOM   11143 N N     . GLN D  1 252 ? -19.291 57.091  -42.373 1.00 42.04 ? 252 GLN B N     1 
ATOM   11144 C CA    . GLN D  1 252 ? -20.141 56.048  -42.939 1.00 41.09 ? 252 GLN B CA    1 
ATOM   11145 C C     . GLN D  1 252 ? -21.459 55.909  -42.172 1.00 40.95 ? 252 GLN B C     1 
ATOM   11146 O O     . GLN D  1 252 ? -21.504 56.056  -40.945 1.00 33.49 ? 252 GLN B O     1 
ATOM   11147 C CB    . GLN D  1 252 ? -19.384 54.693  -42.969 1.00 48.78 ? 252 GLN B CB    1 
ATOM   11148 C CG    . GLN D  1 252 ? -17.873 54.773  -43.307 1.00 45.63 ? 252 GLN B CG    1 
ATOM   11149 C CD    . GLN D  1 252 ? -17.053 53.679  -42.621 1.00 48.28 ? 252 GLN B CD    1 
ATOM   11150 O OE1   . GLN D  1 252 ? -17.592 52.636  -42.228 1.00 43.41 ? 252 GLN B OE1   1 
ATOM   11151 N NE2   . GLN D  1 252 ? -15.743 53.914  -42.479 1.00 48.60 ? 252 GLN B NE2   1 
ATOM   11152 N N     . ARG D  1 253 ? -22.535 55.630  -42.912 1.00 38.73 ? 253 ARG B N     1 
ATOM   11153 C CA    . ARG D  1 253 ? -23.866 55.393  -42.354 1.00 38.48 ? 253 ARG B CA    1 
ATOM   11154 C C     . ARG D  1 253 ? -24.399 54.087  -42.931 1.00 40.51 ? 253 ARG B C     1 
ATOM   11155 O O     . ARG D  1 253 ? -24.595 53.982  -44.150 1.00 41.27 ? 253 ARG B O     1 
ATOM   11156 C CB    . ARG D  1 253 ? -24.837 56.543  -42.671 1.00 33.32 ? 253 ARG B CB    1 
ATOM   11157 C CG    . ARG D  1 253 ? -24.237 57.941  -42.566 1.00 37.68 ? 253 ARG B CG    1 
ATOM   11158 C CD    . ARG D  1 253 ? -25.296 59.064  -42.747 1.00 43.10 ? 253 ARG B CD    1 
ATOM   11159 N NE    . ARG D  1 253 ? -24.998 60.238  -41.930 1.00 41.08 ? 253 ARG B NE    1 
ATOM   11160 C CZ    . ARG D  1 253 ? -25.578 60.510  -40.769 1.00 40.52 ? 253 ARG B CZ    1 
ATOM   11161 N NH1   . ARG D  1 253 ? -26.565 59.755  -40.294 1.00 36.36 ? 253 ARG B NH1   1 
ATOM   11162 N NH2   . ARG D  1 253 ? -25.158 61.562  -40.066 1.00 35.17 ? 253 ARG B NH2   1 
ATOM   11163 N N     . PHE D  1 254 ? -24.657 53.099  -42.064 1.00 37.97 ? 254 PHE B N     1 
ATOM   11164 C CA    . PHE D  1 254 ? -24.937 51.738  -42.510 1.00 31.32 ? 254 PHE B CA    1 
ATOM   11165 C C     . PHE D  1 254 ? -26.091 51.155  -41.715 1.00 32.41 ? 254 PHE B C     1 
ATOM   11166 O O     . PHE D  1 254 ? -26.602 51.768  -40.771 1.00 26.78 ? 254 PHE B O     1 
ATOM   11167 C CB    . PHE D  1 254 ? -23.710 50.839  -42.344 1.00 31.87 ? 254 PHE B CB    1 
ATOM   11168 C CG    . PHE D  1 254 ? -23.247 50.730  -40.923 1.00 31.09 ? 254 PHE B CG    1 
ATOM   11169 C CD1   . PHE D  1 254 ? -22.448 51.716  -40.370 1.00 32.72 ? 254 PHE B CD1   1 
ATOM   11170 C CD2   . PHE D  1 254 ? -23.643 49.672  -40.139 1.00 28.25 ? 254 PHE B CD2   1 
ATOM   11171 C CE1   . PHE D  1 254 ? -22.038 51.640  -39.067 1.00 38.52 ? 254 PHE B CE1   1 
ATOM   11172 C CE2   . PHE D  1 254 ? -23.238 49.579  -38.842 1.00 30.23 ? 254 PHE B CE2   1 
ATOM   11173 C CZ    . PHE D  1 254 ? -22.435 50.566  -38.294 1.00 37.58 ? 254 PHE B CZ    1 
ATOM   11174 N N     . PHE D  1 255 ? -26.478 49.937  -42.097 1.00 34.88 ? 255 PHE B N     1 
ATOM   11175 C CA    . PHE D  1 255 ? -27.331 49.102  -41.263 1.00 34.00 ? 255 PHE B CA    1 
ATOM   11176 C C     . PHE D  1 255 ? -27.101 47.644  -41.615 1.00 31.62 ? 255 PHE B C     1 
ATOM   11177 O O     . PHE D  1 255 ? -26.981 47.297  -42.791 1.00 38.28 ? 255 PHE B O     1 
ATOM   11178 C CB    . PHE D  1 255 ? -28.819 49.465  -41.401 1.00 30.75 ? 255 PHE B CB    1 
ATOM   11179 C CG    . PHE D  1 255 ? -29.456 49.066  -42.713 1.00 35.58 ? 255 PHE B CG    1 
ATOM   11180 C CD1   . PHE D  1 255 ? -29.253 49.813  -43.855 1.00 36.63 ? 255 PHE B CD1   1 
ATOM   11181 C CD2   . PHE D  1 255 ? -30.330 47.986  -42.778 1.00 40.03 ? 255 PHE B CD2   1 
ATOM   11182 C CE1   . PHE D  1 255 ? -29.867 49.454  -45.045 1.00 37.16 ? 255 PHE B CE1   1 
ATOM   11183 C CE2   . PHE D  1 255 ? -30.947 47.634  -43.965 1.00 35.52 ? 255 PHE B CE2   1 
ATOM   11184 C CZ    . PHE D  1 255 ? -30.720 48.363  -45.086 1.00 34.80 ? 255 PHE B CZ    1 
ATOM   11185 N N     . PHE D  1 256 ? -27.026 46.804  -40.586 1.00 29.85 ? 256 PHE B N     1 
ATOM   11186 C CA    . PHE D  1 256 ? -26.993 45.358  -40.759 1.00 34.02 ? 256 PHE B CA    1 
ATOM   11187 C C     . PHE D  1 256 ? -28.407 44.790  -40.652 1.00 35.16 ? 256 PHE B C     1 
ATOM   11188 O O     . PHE D  1 256 ? -29.098 45.029  -39.656 1.00 38.89 ? 256 PHE B O     1 
ATOM   11189 C CB    . PHE D  1 256 ? -26.100 44.706  -39.701 1.00 31.68 ? 256 PHE B CB    1 
ATOM   11190 C CG    . PHE D  1 256 ? -24.705 45.201  -39.700 1.00 28.47 ? 256 PHE B CG    1 
ATOM   11191 C CD1   . PHE D  1 256 ? -24.111 45.617  -40.868 1.00 31.72 ? 256 PHE B CD1   1 
ATOM   11192 C CD2   . PHE D  1 256 ? -23.978 45.239  -38.537 1.00 28.22 ? 256 PHE B CD2   1 
ATOM   11193 C CE1   . PHE D  1 256 ? -22.817 46.073  -40.880 1.00 30.50 ? 256 PHE B CE1   1 
ATOM   11194 C CE2   . PHE D  1 256 ? -22.681 45.698  -38.547 1.00 32.34 ? 256 PHE B CE2   1 
ATOM   11195 C CZ    . PHE D  1 256 ? -22.105 46.112  -39.724 1.00 26.56 ? 256 PHE B CZ    1 
ATOM   11196 N N     . GLU D  1 257 ? -28.836 44.032  -41.663 1.00 32.09 ? 257 GLU B N     1 
ATOM   11197 C CA    . GLU D  1 257 ? -30.097 43.306  -41.581 1.00 29.02 ? 257 GLU B CA    1 
ATOM   11198 C C     . GLU D  1 257 ? -29.839 41.864  -41.165 1.00 29.26 ? 257 GLU B C     1 
ATOM   11199 O O     . GLU D  1 257 ? -28.807 41.282  -41.499 1.00 31.80 ? 257 GLU B O     1 
ATOM   11200 C CB    . GLU D  1 257 ? -30.849 43.338  -42.914 1.00 31.56 ? 257 GLU B CB    1 
ATOM   11201 C CG    . GLU D  1 257 ? -32.255 42.733  -42.866 1.00 30.90 ? 257 GLU B CG    1 
ATOM   11202 C CD    . GLU D  1 257 ? -33.249 43.515  -43.701 1.00 33.12 ? 257 GLU B CD    1 
ATOM   11203 O OE1   . GLU D  1 257 ? -32.798 44.216  -44.646 1.00 27.48 ? 257 GLU B OE1   1 
ATOM   11204 O OE2   . GLU D  1 257 ? -34.469 43.424  -43.407 1.00 32.23 ? 257 GLU B OE2   1 
ATOM   11205 N N     . TYR D  1 258 ? -30.783 41.289  -40.426 1.00 27.31 ? 258 TYR B N     1 
ATOM   11206 C CA    . TYR D  1 258 ? -30.669 39.908  -39.996 1.00 30.48 ? 258 TYR B CA    1 
ATOM   11207 C C     . TYR D  1 258 ? -32.044 39.263  -40.027 1.00 33.81 ? 258 TYR B C     1 
ATOM   11208 O O     . TYR D  1 258 ? -33.077 39.927  -40.170 1.00 27.74 ? 258 TYR B O     1 
ATOM   11209 C CB    . TYR D  1 258 ? -30.098 39.762  -38.567 1.00 36.55 ? 258 TYR B CB    1 
ATOM   11210 C CG    . TYR D  1 258 ? -28.757 40.429  -38.247 1.00 31.16 ? 258 TYR B CG    1 
ATOM   11211 C CD1   . TYR D  1 258 ? -28.669 41.794  -38.037 1.00 28.69 ? 258 TYR B CD1   1 
ATOM   11212 C CD2   . TYR D  1 258 ? -27.601 39.676  -38.081 1.00 28.09 ? 258 TYR B CD2   1 
ATOM   11213 C CE1   . TYR D  1 258 ? -27.461 42.386  -37.705 1.00 29.93 ? 258 TYR B CE1   1 
ATOM   11214 C CE2   . TYR D  1 258 ? -26.401 40.265  -37.758 1.00 25.25 ? 258 TYR B CE2   1 
ATOM   11215 C CZ    . TYR D  1 258 ? -26.338 41.614  -37.571 1.00 24.97 ? 258 TYR B CZ    1 
ATOM   11216 O OH    . TYR D  1 258 ? -25.147 42.209  -37.261 1.00 29.78 ? 258 TYR B OH    1 
ATOM   11217 N N     . HIS D  1 259 ? -32.039 37.947  -39.846 1.00 39.35 ? 259 HIS B N     1 
ATOM   11218 C CA    . HIS D  1 259 ? -33.243 37.143  -39.749 1.00 35.15 ? 259 HIS B CA    1 
ATOM   11219 C C     . HIS D  1 259 ? -33.043 36.154  -38.607 1.00 37.28 ? 259 HIS B C     1 
ATOM   11220 O O     . HIS D  1 259 ? -31.933 35.640  -38.410 1.00 33.84 ? 259 HIS B O     1 
ATOM   11221 C CB    . HIS D  1 259 ? -33.525 36.433  -41.068 1.00 31.75 ? 259 HIS B CB    1 
ATOM   11222 C CG    . HIS D  1 259 ? -34.665 35.478  -41.002 1.00 33.21 ? 259 HIS B CG    1 
ATOM   11223 N ND1   . HIS D  1 259 ? -34.516 34.181  -40.567 1.00 29.19 ? 259 HIS B ND1   1 
ATOM   11224 C CD2   . HIS D  1 259 ? -35.968 35.620  -41.336 1.00 34.16 ? 259 HIS B CD2   1 
ATOM   11225 C CE1   . HIS D  1 259 ? -35.679 33.562  -40.640 1.00 33.37 ? 259 HIS B CE1   1 
ATOM   11226 N NE2   . HIS D  1 259 ? -36.578 34.413  -41.099 1.00 30.36 ? 259 HIS B NE2   1 
ATOM   11227 N N     . LEU D  1 260 ? -34.107 35.931  -37.826 1.00 38.44 ? 260 LEU B N     1 
ATOM   11228 C CA    . LEU D  1 260 ? -34.004 35.272  -36.530 1.00 31.32 ? 260 LEU B CA    1 
ATOM   11229 C C     . LEU D  1 260 ? -34.997 34.131  -36.431 1.00 37.49 ? 260 LEU B C     1 
ATOM   11230 O O     . LEU D  1 260 ? -36.134 34.231  -36.919 1.00 35.32 ? 260 LEU B O     1 
ATOM   11231 C CB    . LEU D  1 260 ? -34.281 36.208  -35.371 1.00 32.02 ? 260 LEU B CB    1 
ATOM   11232 C CG    . LEU D  1 260 ? -33.224 37.173  -34.834 1.00 37.58 ? 260 LEU B CG    1 
ATOM   11233 C CD1   . LEU D  1 260 ? -32.373 37.792  -35.937 1.00 34.96 ? 260 LEU B CD1   1 
ATOM   11234 C CD2   . LEU D  1 260 ? -33.871 38.257  -33.966 1.00 30.88 ? 260 LEU B CD2   1 
ATOM   11235 N N     . ASP D  1 261 ? -34.558 33.057  -35.779 1.00 34.90 ? 261 ASP B N     1 
ATOM   11236 C CA    . ASP D  1 261 ? -35.435 31.939  -35.473 1.00 37.44 ? 261 ASP B CA    1 
ATOM   11237 C C     . ASP D  1 261 ? -34.933 31.312  -34.178 1.00 33.69 ? 261 ASP B C     1 
ATOM   11238 O O     . ASP D  1 261 ? -34.022 31.838  -33.533 1.00 30.50 ? 261 ASP B O     1 
ATOM   11239 C CB    . ASP D  1 261 ? -35.526 30.968  -36.665 1.00 31.59 ? 261 ASP B CB    1 
ATOM   11240 C CG    . ASP D  1 261 ? -34.201 30.281  -36.987 1.00 37.33 ? 261 ASP B CG    1 
ATOM   11241 O OD1   . ASP D  1 261 ? -33.347 30.108  -36.083 1.00 39.46 ? 261 ASP B OD1   1 
ATOM   11242 O OD2   . ASP D  1 261 ? -34.019 29.889  -38.164 1.00 40.64 ? 261 ASP B OD2   1 
ATOM   11243 N N     . GLY D  1 262 ? -35.521 30.174  -33.809 1.00 35.93 ? 262 GLY B N     1 
ATOM   11244 C CA    . GLY D  1 262 ? -35.310 29.560  -32.502 1.00 38.73 ? 262 GLY B CA    1 
ATOM   11245 C C     . GLY D  1 262 ? -33.896 29.086  -32.235 1.00 39.29 ? 262 GLY B C     1 
ATOM   11246 O O     . GLY D  1 262 ? -33.556 28.807  -31.080 1.00 38.02 ? 262 GLY B O     1 
ATOM   11247 N N     . ASP D  1 263 ? -33.072 28.989  -33.265 1.00 35.73 ? 263 ASP B N     1 
ATOM   11248 C CA    . ASP D  1 263 ? -31.688 28.610  -33.061 1.00 38.93 ? 263 ASP B CA    1 
ATOM   11249 C C     . ASP D  1 263 ? -30.784 29.836  -33.063 1.00 43.03 ? 263 ASP B C     1 
ATOM   11250 O O     . ASP D  1 263 ? -30.202 30.195  -32.034 1.00 35.97 ? 263 ASP B O     1 
ATOM   11251 C CB    . ASP D  1 263 ? -31.271 27.625  -34.139 1.00 40.98 ? 263 ASP B CB    1 
ATOM   11252 C CG    . ASP D  1 263 ? -32.135 26.396  -34.140 1.00 42.43 ? 263 ASP B CG    1 
ATOM   11253 O OD1   . ASP D  1 263 ? -32.757 26.121  -33.097 1.00 45.94 ? 263 ASP B OD1   1 
ATOM   11254 O OD2   . ASP D  1 263 ? -32.211 25.714  -35.182 1.00 44.03 ? 263 ASP B OD2   1 
ATOM   11255 N N     . ARG D  1 264 ? -30.669 30.494  -34.210 1.00 46.07 ? 264 ARG B N     1 
ATOM   11256 C CA    . ARG D  1 264 ? -29.675 31.538  -34.381 1.00 41.94 ? 264 ARG B CA    1 
ATOM   11257 C C     . ARG D  1 264 ? -30.308 32.794  -34.955 1.00 34.24 ? 264 ARG B C     1 
ATOM   11258 O O     . ARG D  1 264 ? -31.449 32.797  -35.425 1.00 33.13 ? 264 ARG B O     1 
ATOM   11259 C CB    . ARG D  1 264 ? -28.542 31.061  -35.293 1.00 42.69 ? 264 ARG B CB    1 
ATOM   11260 C CG    . ARG D  1 264 ? -29.025 30.285  -36.528 1.00 50.83 ? 264 ARG B CG    1 
ATOM   11261 C CD    . ARG D  1 264 ? -28.083 29.130  -36.885 1.00 53.50 ? 264 ARG B CD    1 
ATOM   11262 N NE    . ARG D  1 264 ? -28.035 28.092  -35.850 1.00 53.10 ? 264 ARG B NE    1 
ATOM   11263 C CZ    . ARG D  1 264 ? -27.083 27.962  -34.921 1.00 51.86 ? 264 ARG B CZ    1 
ATOM   11264 N NH1   . ARG D  1 264 ? -26.054 28.796  -34.845 1.00 49.96 ? 264 ARG B NH1   1 
ATOM   11265 N NH2   . ARG D  1 264 ? -27.146 26.948  -34.063 1.00 33.51 ? 264 ARG B NH2   1 
ATOM   11266 N N     . ALA D  1 265 ? -29.541 33.875  -34.869 1.00 38.85 ? 265 ALA B N     1 
ATOM   11267 C CA    . ALA D  1 265 ? -29.698 35.041  -35.721 1.00 35.20 ? 265 ALA B CA    1 
ATOM   11268 C C     . ALA D  1 265 ? -28.739 34.902  -36.891 1.00 35.05 ? 265 ALA B C     1 
ATOM   11269 O O     . ALA D  1 265 ? -27.597 34.461  -36.722 1.00 30.43 ? 265 ALA B O     1 
ATOM   11270 C CB    . ALA D  1 265 ? -29.400 36.329  -34.957 1.00 32.30 ? 265 ALA B CB    1 
ATOM   11271 N N     . ARG D  1 266 ? -29.202 35.268  -38.080 1.00 39.88 ? 266 ARG B N     1 
ATOM   11272 C CA    . ARG D  1 266 ? -28.423 35.054  -39.293 1.00 44.74 ? 266 ARG B CA    1 
ATOM   11273 C C     . ARG D  1 266 ? -28.159 36.379  -40.009 1.00 42.32 ? 266 ARG B C     1 
ATOM   11274 O O     . ARG D  1 266 ? -29.099 37.105  -40.358 1.00 40.37 ? 266 ARG B O     1 
ATOM   11275 C CB    . ARG D  1 266 ? -29.130 34.065  -40.222 1.00 43.78 ? 266 ARG B CB    1 
ATOM   11276 C CG    . ARG D  1 266 ? -28.790 32.610  -39.932 1.00 43.77 ? 266 ARG B CG    1 
ATOM   11277 C CD    . ARG D  1 266 ? -29.811 31.654  -40.552 1.00 47.95 ? 266 ARG B CD    1 
ATOM   11278 N NE    . ARG D  1 266 ? -30.446 32.184  -41.760 1.00 56.68 ? 266 ARG B NE    1 
ATOM   11279 C CZ    . ARG D  1 266 ? -31.757 32.351  -41.915 1.00 58.56 ? 266 ARG B CZ    1 
ATOM   11280 N NH1   . ARG D  1 266 ? -32.610 32.077  -40.932 1.00 51.25 ? 266 ARG B NH1   1 
ATOM   11281 N NH2   . ARG D  1 266 ? -32.222 32.807  -43.084 1.00 41.81 ? 266 ARG B NH2   1 
ATOM   11282 N N     . PHE D  1 267 ? -26.876 36.689  -40.212 1.00 41.63 ? 267 PHE B N     1 
ATOM   11283 C CA    . PHE D  1 267 ? -26.475 37.810  -41.051 1.00 37.69 ? 267 PHE B CA    1 
ATOM   11284 C C     . PHE D  1 267 ? -26.970 37.605  -42.478 1.00 35.49 ? 267 PHE B C     1 
ATOM   11285 O O     . PHE D  1 267 ? -26.774 36.542  -43.070 1.00 36.24 ? 267 PHE B O     1 
ATOM   11286 C CB    . PHE D  1 267 ? -24.949 37.941  -41.040 1.00 39.33 ? 267 PHE B CB    1 
ATOM   11287 C CG    . PHE D  1 267 ? -24.437 39.255  -41.575 1.00 41.88 ? 267 PHE B CG    1 
ATOM   11288 C CD1   . PHE D  1 267 ? -24.915 40.466  -41.080 1.00 39.96 ? 267 PHE B CD1   1 
ATOM   11289 C CD2   . PHE D  1 267 ? -23.473 39.276  -42.570 1.00 36.30 ? 267 PHE B CD2   1 
ATOM   11290 C CE1   . PHE D  1 267 ? -24.441 41.679  -41.562 1.00 34.94 ? 267 PHE B CE1   1 
ATOM   11291 C CE2   . PHE D  1 267 ? -22.991 40.478  -43.059 1.00 36.43 ? 267 PHE B CE2   1 
ATOM   11292 C CZ    . PHE D  1 267 ? -23.476 41.684  -42.553 1.00 39.27 ? 267 PHE B CZ    1 
ATOM   11293 N N     . LEU D  1 268 ? -27.615 38.620  -43.032 1.00 34.32 ? 268 LEU B N     1 
ATOM   11294 C CA    . LEU D  1 268 ? -27.996 38.588  -44.438 1.00 35.15 ? 268 LEU B CA    1 
ATOM   11295 C C     . LEU D  1 268 ? -27.230 39.588  -45.287 1.00 30.51 ? 268 LEU B C     1 
ATOM   11296 O O     . LEU D  1 268 ? -26.757 39.232  -46.364 1.00 36.89 ? 268 LEU B O     1 
ATOM   11297 C CB    . LEU D  1 268 ? -29.501 38.832  -44.599 1.00 33.72 ? 268 LEU B CB    1 
ATOM   11298 C CG    . LEU D  1 268 ? -30.439 37.988  -43.716 1.00 33.76 ? 268 LEU B CG    1 
ATOM   11299 C CD1   . LEU D  1 268 ? -31.856 38.495  -43.853 1.00 32.96 ? 268 LEU B CD1   1 
ATOM   11300 C CD2   . LEU D  1 268 ? -30.384 36.498  -44.011 1.00 30.54 ? 268 LEU B CD2   1 
ATOM   11301 N N     . HIS D  1 269 ? -27.054 40.820  -44.826 1.00 30.52 ? 269 HIS B N     1 
ATOM   11302 C CA    . HIS D  1 269 ? -26.310 41.795  -45.611 1.00 29.31 ? 269 HIS B CA    1 
ATOM   11303 C C     . HIS D  1 269 ? -26.080 43.041  -44.768 1.00 34.06 ? 269 HIS B C     1 
ATOM   11304 O O     . HIS D  1 269 ? -26.762 43.262  -43.758 1.00 31.10 ? 269 HIS B O     1 
ATOM   11305 C CB    . HIS D  1 269 ? -27.071 42.174  -46.881 1.00 25.82 ? 269 HIS B CB    1 
ATOM   11306 C CG    . HIS D  1 269 ? -28.229 43.078  -46.618 1.00 28.04 ? 269 HIS B CG    1 
ATOM   11307 N ND1   . HIS D  1 269 ? -28.144 44.450  -46.728 1.00 33.03 ? 269 HIS B ND1   1 
ATOM   11308 C CD2   . HIS D  1 269 ? -29.483 42.814  -46.183 1.00 31.25 ? 269 HIS B CD2   1 
ATOM   11309 C CE1   . HIS D  1 269 ? -29.303 44.989  -46.392 1.00 34.59 ? 269 HIS B CE1   1 
ATOM   11310 N NE2   . HIS D  1 269 ? -30.134 44.018  -46.060 1.00 33.66 ? 269 HIS B NE2   1 
ATOM   11311 N N     . SER D  1 270 ? -25.137 43.871  -45.224 1.00 30.58 ? 270 SER B N     1 
ATOM   11312 C CA    . SER D  1 270 ? -24.988 45.248  -44.775 1.00 27.78 ? 270 SER B CA    1 
ATOM   11313 C C     . SER D  1 270 ? -25.238 46.184  -45.946 1.00 30.59 ? 270 SER B C     1 
ATOM   11314 O O     . SER D  1 270 ? -24.998 45.822  -47.100 1.00 31.22 ? 270 SER B O     1 
ATOM   11315 C CB    . SER D  1 270 ? -23.598 45.502  -44.224 1.00 31.54 ? 270 SER B CB    1 
ATOM   11316 O OG    . SER D  1 270 ? -22.686 45.728  -45.286 1.00 36.80 ? 270 SER B OG    1 
ATOM   11317 N N     . SER D  1 271 ? -25.699 47.400  -45.654 1.00 30.51 ? 271 SER B N     1 
ATOM   11318 C CA    . SER D  1 271 ? -25.889 48.364  -46.731 1.00 33.53 ? 271 SER B CA    1 
ATOM   11319 C C     . SER D  1 271 ? -25.621 49.776  -46.237 1.00 30.30 ? 271 SER B C     1 
ATOM   11320 O O     . SER D  1 271 ? -25.656 50.046  -45.041 1.00 31.98 ? 271 SER B O     1 
ATOM   11321 C CB    . SER D  1 271 ? -27.290 48.252  -47.318 1.00 34.13 ? 271 SER B CB    1 
ATOM   11322 O OG    . SER D  1 271 ? -27.541 46.909  -47.720 1.00 35.05 ? 271 SER B OG    1 
ATOM   11323 N N     . ILE D  1 272 ? -25.352 50.680  -47.185 1.00 33.13 ? 272 ILE B N     1 
ATOM   11324 C CA    . ILE D  1 272 ? -25.005 52.071  -46.893 1.00 31.99 ? 272 ILE B CA    1 
ATOM   11325 C C     . ILE D  1 272 ? -26.226 52.949  -47.102 1.00 33.12 ? 272 ILE B C     1 
ATOM   11326 O O     . ILE D  1 272 ? -26.938 52.808  -48.099 1.00 34.17 ? 272 ILE B O     1 
ATOM   11327 C CB    . ILE D  1 272 ? -23.854 52.564  -47.790 1.00 31.52 ? 272 ILE B CB    1 
ATOM   11328 C CG1   . ILE D  1 272 ? -22.541 51.901  -47.425 1.00 30.92 ? 272 ILE B CG1   1 
ATOM   11329 C CG2   . ILE D  1 272 ? -23.691 54.067  -47.677 1.00 27.74 ? 272 ILE B CG2   1 
ATOM   11330 C CD1   . ILE D  1 272 ? -21.513 51.996  -48.514 1.00 32.77 ? 272 ILE B CD1   1 
ATOM   11331 N N     . LEU D  1 273 ? -26.459 53.882  -46.189 1.00 33.78 ? 273 LEU B N     1 
ATOM   11332 C CA    . LEU D  1 273 ? -27.516 54.869  -46.368 1.00 34.19 ? 273 LEU B CA    1 
ATOM   11333 C C     . LEU D  1 273 ? -26.960 56.120  -47.036 1.00 36.38 ? 273 LEU B C     1 
ATOM   11334 O O     . LEU D  1 273 ? -26.018 56.740  -46.529 1.00 35.19 ? 273 LEU B O     1 
ATOM   11335 C CB    . LEU D  1 273 ? -28.160 55.210  -45.031 1.00 33.60 ? 273 LEU B CB    1 
ATOM   11336 C CG    . LEU D  1 273 ? -29.078 54.071  -44.567 1.00 40.23 ? 273 LEU B CG    1 
ATOM   11337 C CD1   . LEU D  1 273 ? -28.723 53.582  -43.151 1.00 37.71 ? 273 LEU B CD1   1 
ATOM   11338 C CD2   . LEU D  1 273 ? -30.555 54.475  -44.640 1.00 34.77 ? 273 LEU B CD2   1 
ATOM   11339 N N     . LYS D  1 274 ? -27.570 56.517  -48.151 1.00 34.41 ? 274 LYS B N     1 
ATOM   11340 C CA    . LYS D  1 274 ? -27.087 57.650  -48.930 1.00 42.04 ? 274 LYS B CA    1 
ATOM   11341 C C     . LYS D  1 274 ? -28.128 58.773  -48.968 1.00 43.86 ? 274 LYS B C     1 
ATOM   11342 O O     . LYS D  1 274 ? -29.320 58.518  -49.192 1.00 36.63 ? 274 LYS B O     1 
ATOM   11343 C CB    . LYS D  1 274 ? -26.688 57.176  -50.330 1.00 35.88 ? 274 LYS B CB    1 
ATOM   11344 C CG    . LYS D  1 274 ? -25.351 56.444  -50.303 1.00 32.48 ? 274 LYS B CG    1 
ATOM   11345 C CD    . LYS D  1 274 ? -24.606 56.575  -51.596 1.00 38.68 ? 274 LYS B CD    1 
ATOM   11346 C CE    . LYS D  1 274 ? -23.981 57.938  -51.722 1.00 44.74 ? 274 LYS B CE    1 
ATOM   11347 N NZ    . LYS D  1 274 ? -24.942 58.903  -52.364 1.00 43.56 ? 274 LYS B NZ    1 
ATOM   11348 N N     . TYR D  1 275 ? -27.667 60.019  -48.760 1.00 45.07 ? 275 TYR B N     1 
ATOM   11349 C CA    . TYR D  1 275 ? -28.549 61.172  -48.542 1.00 45.93 ? 275 TYR B CA    1 
ATOM   11350 C C     . TYR D  1 275 ? -28.282 62.364  -49.465 1.00 49.43 ? 275 TYR B C     1 
ATOM   11351 O O     . TYR D  1 275 ? -27.559 62.246  -50.461 1.00 48.97 ? 275 TYR B O     1 
ATOM   11352 C CB    . TYR D  1 275 ? -28.432 61.660  -47.086 1.00 43.95 ? 275 TYR B CB    1 
ATOM   11353 C CG    . TYR D  1 275 ? -28.783 60.598  -46.078 1.00 39.61 ? 275 TYR B CG    1 
ATOM   11354 C CD1   . TYR D  1 275 ? -27.850 59.651  -45.695 1.00 39.47 ? 275 TYR B CD1   1 
ATOM   11355 C CD2   . TYR D  1 275 ? -30.048 60.533  -45.525 1.00 43.26 ? 275 TYR B CD2   1 
ATOM   11356 C CE1   . TYR D  1 275 ? -28.164 58.672  -44.797 1.00 44.34 ? 275 TYR B CE1   1 
ATOM   11357 C CE2   . TYR D  1 275 ? -30.372 59.559  -44.623 1.00 43.42 ? 275 TYR B CE2   1 
ATOM   11358 C CZ    . TYR D  1 275 ? -29.425 58.630  -44.259 1.00 44.97 ? 275 TYR B CZ    1 
ATOM   11359 O OH    . TYR D  1 275 ? -29.720 57.649  -43.342 1.00 43.64 ? 275 TYR B OH    1 
ATOM   11360 N N     . GLU D  1 276 ? -28.883 63.509  -49.107 1.00 50.95 ? 276 GLU B N     1 
ATOM   11361 C CA    . GLU D  1 276 ? -28.736 64.841  -49.723 1.00 50.71 ? 276 GLU B CA    1 
ATOM   11362 C C     . GLU D  1 276 ? -29.863 65.071  -50.721 1.00 50.94 ? 276 GLU B C     1 
ATOM   11363 O O     . GLU D  1 276 ? -30.872 65.704  -50.381 1.00 45.99 ? 276 GLU B O     1 
ATOM   11364 C CB    . GLU D  1 276 ? -27.359 65.054  -50.385 1.00 50.06 ? 276 GLU B CB    1 
ATOM   11365 C CG    . GLU D  1 276 ? -27.152 66.484  -50.929 1.00 54.70 ? 276 GLU B CG    1 
ATOM   11366 C CD    . GLU D  1 276 ? -25.701 66.942  -50.887 1.00 58.23 ? 276 GLU B CD    1 
ATOM   11367 O OE1   . GLU D  1 276 ? -24.800 66.099  -51.107 1.00 60.29 ? 276 GLU B OE1   1 
ATOM   11368 O OE2   . GLU D  1 276 ? -25.468 68.147  -50.620 1.00 50.01 ? 276 GLU B OE2   1 
ATOM   11369 N N     . GLY D  1 281 ? -32.536 74.894  -45.236 1.00 43.36 ? 281 GLY B N     1 
ATOM   11370 C CA    . GLY D  1 281 ? -32.988 76.240  -44.928 1.00 56.24 ? 281 GLY B CA    1 
ATOM   11371 C C     . GLY D  1 281 ? -34.491 76.329  -44.715 1.00 69.38 ? 281 GLY B C     1 
ATOM   11372 O O     . GLY D  1 281 ? -34.962 76.312  -43.569 1.00 68.64 ? 281 GLY B O     1 
ATOM   11373 N N     . SER D  1 282 ? -35.244 76.420  -45.815 1.00 65.62 ? 282 SER B N     1 
ATOM   11374 C CA    . SER D  1 282 ? -36.707 76.462  -45.758 1.00 64.73 ? 282 SER B CA    1 
ATOM   11375 C C     . SER D  1 282 ? -37.287 75.222  -45.077 1.00 63.30 ? 282 SER B C     1 
ATOM   11376 O O     . SER D  1 282 ? -38.042 75.327  -44.105 1.00 61.54 ? 282 SER B O     1 
ATOM   11377 C CB    . SER D  1 282 ? -37.301 76.599  -47.162 1.00 64.49 ? 282 SER B CB    1 
ATOM   11378 O OG    . SER D  1 282 ? -36.576 77.535  -47.936 1.00 66.36 ? 282 SER B OG    1 
ATOM   11379 N N     . GLY D  1 284 ? -35.495 71.432  -45.054 1.00 50.66 ? 284 GLY B N     1 
ATOM   11380 C CA    . GLY D  1 284 ? -34.791 71.163  -43.811 1.00 56.10 ? 284 GLY B CA    1 
ATOM   11381 C C     . GLY D  1 284 ? -33.360 70.676  -44.001 1.00 56.09 ? 284 GLY B C     1 
ATOM   11382 O O     . GLY D  1 284 ? -32.416 71.474  -43.964 1.00 55.57 ? 284 GLY B O     1 
ATOM   11383 N N     . SER D  1 285 ? -33.183 69.369  -44.190 1.00 51.50 ? 285 SER B N     1 
ATOM   11384 C CA    . SER D  1 285 ? -31.859 68.841  -44.475 1.00 46.34 ? 285 SER B CA    1 
ATOM   11385 C C     . SER D  1 285 ? -31.987 67.521  -45.216 1.00 43.19 ? 285 SER B C     1 
ATOM   11386 O O     . SER D  1 285 ? -33.089 67.040  -45.494 1.00 49.67 ? 285 SER B O     1 
ATOM   11387 C CB    . SER D  1 285 ? -31.042 68.690  -43.197 1.00 43.83 ? 285 SER B CB    1 
ATOM   11388 O OG    . SER D  1 285 ? -29.874 69.477  -43.295 1.00 37.83 ? 285 SER B OG    1 
ATOM   11389 N N     . ALA D  1 286 ? -30.830 66.937  -45.513 1.00 40.53 ? 286 ALA B N     1 
ATOM   11390 C CA    . ALA D  1 286 ? -30.676 65.785  -46.385 1.00 37.55 ? 286 ALA B CA    1 
ATOM   11391 C C     . ALA D  1 286 ? -31.708 64.696  -46.158 1.00 45.07 ? 286 ALA B C     1 
ATOM   11392 O O     . ALA D  1 286 ? -31.692 64.018  -45.125 1.00 48.13 ? 286 ALA B O     1 
ATOM   11393 C CB    . ALA D  1 286 ? -29.287 65.189  -46.204 1.00 39.19 ? 286 ALA B CB    1 
ATOM   11394 N N     . LYS D  1 287 ? -32.598 64.514  -47.125 1.00 39.79 ? 287 LYS B N     1 
ATOM   11395 C CA    . LYS D  1 287 ? -33.461 63.350  -47.141 1.00 44.26 ? 287 LYS B CA    1 
ATOM   11396 C C     . LYS D  1 287 ? -32.681 62.117  -47.610 1.00 46.59 ? 287 LYS B C     1 
ATOM   11397 O O     . LYS D  1 287 ? -31.473 62.165  -47.856 1.00 44.22 ? 287 LYS B O     1 
ATOM   11398 C CB    . LYS D  1 287 ? -34.687 63.626  -48.007 1.00 48.91 ? 287 LYS B CB    1 
ATOM   11399 C CG    . LYS D  1 287 ? -35.688 64.586  -47.329 1.00 57.09 ? 287 LYS B CG    1 
ATOM   11400 C CD    . LYS D  1 287 ? -35.884 64.267  -45.830 1.00 56.28 ? 287 LYS B CD    1 
ATOM   11401 C CE    . LYS D  1 287 ? -36.544 62.886  -45.610 1.00 50.11 ? 287 LYS B CE    1 
ATOM   11402 N NZ    . LYS D  1 287 ? -37.753 62.933  -44.716 1.00 51.92 ? 287 LYS B NZ    1 
ATOM   11403 N N     . TRP D  1 288 ? -33.379 60.987  -47.708 1.00 46.03 ? 288 TRP B N     1 
ATOM   11404 C CA    . TRP D  1 288 ? -32.780 59.703  -48.059 1.00 43.87 ? 288 TRP B CA    1 
ATOM   11405 C C     . TRP D  1 288 ? -33.045 59.424  -49.535 1.00 46.72 ? 288 TRP B C     1 
ATOM   11406 O O     . TRP D  1 288 ? -34.185 59.549  -49.993 1.00 47.60 ? 288 TRP B O     1 
ATOM   11407 C CB    . TRP D  1 288 ? -33.354 58.585  -47.176 1.00 42.74 ? 288 TRP B CB    1 
ATOM   11408 C CG    . TRP D  1 288 ? -33.269 57.176  -47.763 1.00 44.84 ? 288 TRP B CG    1 
ATOM   11409 C CD1   . TRP D  1 288 ? -32.145 56.395  -47.889 1.00 43.63 ? 288 TRP B CD1   1 
ATOM   11410 C CD2   . TRP D  1 288 ? -34.356 56.388  -48.280 1.00 43.59 ? 288 TRP B CD2   1 
ATOM   11411 N NE1   . TRP D  1 288 ? -32.465 55.179  -48.464 1.00 39.04 ? 288 TRP B NE1   1 
ATOM   11412 C CE2   . TRP D  1 288 ? -33.814 55.147  -48.710 1.00 42.78 ? 288 TRP B CE2   1 
ATOM   11413 C CE3   . TRP D  1 288 ? -35.729 56.610  -48.429 1.00 40.90 ? 288 TRP B CE3   1 
ATOM   11414 C CZ2   . TRP D  1 288 ? -34.605 54.138  -49.272 1.00 38.77 ? 288 TRP B CZ2   1 
ATOM   11415 C CZ3   . TRP D  1 288 ? -36.515 55.604  -48.986 1.00 37.79 ? 288 TRP B CZ3   1 
ATOM   11416 C CH2   . TRP D  1 288 ? -35.950 54.387  -49.404 1.00 44.70 ? 288 TRP B CH2   1 
ATOM   11417 N N     . ILE D  1 289 ? -31.998 59.065  -50.280 1.00 46.74 ? 289 ILE B N     1 
ATOM   11418 C CA    . ILE D  1 289 ? -32.115 58.868  -51.723 1.00 44.76 ? 289 ILE B CA    1 
ATOM   11419 C C     . ILE D  1 289 ? -31.838 57.439  -52.173 1.00 39.72 ? 289 ILE B C     1 
ATOM   11420 O O     . ILE D  1 289 ? -32.196 57.098  -53.312 1.00 36.87 ? 289 ILE B O     1 
ATOM   11421 C CB    . ILE D  1 289 ? -31.229 59.862  -52.511 1.00 43.05 ? 289 ILE B CB    1 
ATOM   11422 C CG1   . ILE D  1 289 ? -29.744 59.507  -52.421 1.00 41.41 ? 289 ILE B CG1   1 
ATOM   11423 C CG2   . ILE D  1 289 ? -31.450 61.268  -52.006 1.00 38.62 ? 289 ILE B CG2   1 
ATOM   11424 C CD1   . ILE D  1 289 ? -28.881 60.393  -53.302 1.00 38.04 ? 289 ILE B CD1   1 
ATOM   11425 N N     . GLY D  1 290 ? -31.244 56.588  -51.339 1.00 34.95 ? 290 GLY B N     1 
ATOM   11426 C CA    . GLY D  1 290 ? -31.203 55.172  -51.650 1.00 32.81 ? 290 GLY B CA    1 
ATOM   11427 C C     . GLY D  1 290 ? -30.116 54.431  -50.893 1.00 35.68 ? 290 GLY B C     1 
ATOM   11428 O O     . GLY D  1 290 ? -29.503 54.951  -49.965 1.00 42.27 ? 290 GLY B O     1 
ATOM   11429 N N     . LEU D  1 291 ? -29.883 53.199  -51.336 1.00 37.62 ? 291 LEU B N     1 
ATOM   11430 C CA    . LEU D  1 291 ? -29.032 52.249  -50.640 1.00 30.42 ? 291 LEU B CA    1 
ATOM   11431 C C     . LEU D  1 291 ? -27.987 51.680  -51.580 1.00 36.20 ? 291 LEU B C     1 
ATOM   11432 O O     . LEU D  1 291 ? -28.184 51.615  -52.796 1.00 41.17 ? 291 LEU B O     1 
ATOM   11433 C CB    . LEU D  1 291 ? -29.834 51.088  -50.072 1.00 28.47 ? 291 LEU B CB    1 
ATOM   11434 C CG    . LEU D  1 291 ? -30.783 51.504  -48.966 1.00 31.57 ? 291 LEU B CG    1 
ATOM   11435 C CD1   . LEU D  1 291 ? -31.382 50.273  -48.350 1.00 29.35 ? 291 LEU B CD1   1 
ATOM   11436 C CD2   . LEU D  1 291 ? -30.058 52.350  -47.949 1.00 33.12 ? 291 LEU B CD2   1 
ATOM   11437 N N     . ASP D  1 292 ? -26.888 51.211  -50.985 1.00 36.78 ? 292 ASP B N     1 
ATOM   11438 C CA    . ASP D  1 292 ? -25.765 50.633  -51.710 1.00 38.65 ? 292 ASP B CA    1 
ATOM   11439 C C     . ASP D  1 292 ? -25.343 49.320  -51.051 1.00 38.13 ? 292 ASP B C     1 
ATOM   11440 O O     . ASP D  1 292 ? -25.459 49.155  -49.830 1.00 40.04 ? 292 ASP B O     1 
ATOM   11441 C CB    . ASP D  1 292 ? -24.594 51.647  -51.764 1.00 42.10 ? 292 ASP B CB    1 
ATOM   11442 C CG    . ASP D  1 292 ? -24.847 52.833  -52.759 1.00 48.89 ? 292 ASP B CG    1 
ATOM   11443 O OD1   . ASP D  1 292 ? -25.894 52.869  -53.461 1.00 41.35 ? 292 ASP B OD1   1 
ATOM   11444 O OD2   . ASP D  1 292 ? -23.988 53.751  -52.823 1.00 47.12 ? 292 ASP B OD2   1 
ATOM   11445 N N     . SER D  1 293 ? -24.853 48.381  -51.880 1.00 34.55 ? 293 SER B N     1 
ATOM   11446 C CA    . SER D  1 293 ? -24.458 46.995  -51.584 1.00 35.17 ? 293 SER B CA    1 
ATOM   11447 C C     . SER D  1 293 ? -23.418 46.974  -50.474 1.00 42.48 ? 293 SER B C     1 
ATOM   11448 O O     . SER D  1 293 ? -23.152 48.029  -49.893 1.00 39.41 ? 293 SER B O     1 
ATOM   11449 C CB    . SER D  1 293 ? -23.903 46.362  -52.858 1.00 40.12 ? 293 SER B CB    1 
ATOM   11450 O OG    . SER D  1 293 ? -22.497 46.523  -52.932 1.00 45.30 ? 293 SER B OG    1 
ATOM   11451 N N     . PRO D  1 294 ? -22.776 45.777  -50.134 1.00 41.82 ? 294 PRO B N     1 
ATOM   11452 C CA    . PRO D  1 294 ? -21.647 45.769  -49.195 1.00 37.85 ? 294 PRO B CA    1 
ATOM   11453 C C     . PRO D  1 294 ? -21.129 47.134  -48.784 1.00 44.70 ? 294 PRO B C     1 
ATOM   11454 O O     . PRO D  1 294 ? -20.703 47.934  -49.621 1.00 45.72 ? 294 PRO B O     1 
ATOM   11455 C CB    . PRO D  1 294 ? -20.596 44.987  -49.995 1.00 42.04 ? 294 PRO B CB    1 
ATOM   11456 C CG    . PRO D  1 294 ? -21.443 44.021  -50.838 1.00 38.01 ? 294 PRO B CG    1 
ATOM   11457 C CD    . PRO D  1 294 ? -22.905 44.427  -50.664 1.00 42.47 ? 294 PRO B CD    1 
ATOM   11458 N N     . SER D  1 295 ? -21.167 47.387  -47.482 1.00 41.76 ? 295 SER B N     1 
ATOM   11459 C CA    . SER D  1 295 ? -21.280 48.753  -46.994 1.00 37.62 ? 295 SER B CA    1 
ATOM   11460 C C     . SER D  1 295 ? -19.953 49.427  -46.677 1.00 47.85 ? 295 SER B C     1 
ATOM   11461 O O     . SER D  1 295 ? -19.959 50.601  -46.293 1.00 55.77 ? 295 SER B O     1 
ATOM   11462 C CB    . SER D  1 295 ? -22.151 48.758  -45.740 1.00 40.46 ? 295 SER B CB    1 
ATOM   11463 O OG    . SER D  1 295 ? -21.550 47.966  -44.725 1.00 42.43 ? 295 SER B OG    1 
ATOM   11464 N N     . ARG D  1 296 ? -18.825 48.725  -46.786 1.00 51.60 ? 296 ARG B N     1 
ATOM   11465 C CA    . ARG D  1 296 ? -17.526 49.276  -46.392 1.00 56.03 ? 296 ARG B CA    1 
ATOM   11466 C C     . ARG D  1 296 ? -17.455 49.554  -44.887 1.00 43.16 ? 296 ARG B C     1 
ATOM   11467 O O     . ARG D  1 296 ? -16.591 50.296  -44.424 1.00 51.22 ? 296 ARG B O     1 
ATOM   11468 C CB    . ARG D  1 296 ? -17.204 50.532  -47.234 1.00 55.99 ? 296 ARG B CB    1 
ATOM   11469 C CG    . ARG D  1 296 ? -15.879 51.281  -47.011 1.00 61.34 ? 296 ARG B CG    1 
ATOM   11470 C CD    . ARG D  1 296 ? -14.661 50.468  -47.403 1.00 63.90 ? 296 ARG B CD    1 
ATOM   11471 N NE    . ARG D  1 296 ? -14.757 49.907  -48.745 1.00 66.20 ? 296 ARG B NE    1 
ATOM   11472 C CZ    . ARG D  1 296 ? -15.011 48.631  -49.003 1.00 68.05 ? 296 ARG B CZ    1 
ATOM   11473 N NH1   . ARG D  1 296 ? -15.238 47.761  -48.028 1.00 59.32 ? 296 ARG B NH1   1 
ATOM   11474 N NH2   . ARG D  1 296 ? -15.028 48.214  -50.268 1.00 66.56 ? 296 ARG B NH2   1 
ATOM   11475 N N     . SER D  1 297 ? -18.329 48.941  -44.090 1.00 41.19 ? 297 SER B N     1 
ATOM   11476 C CA    . SER D  1 297 ? -18.416 49.259  -42.671 1.00 43.15 ? 297 SER B CA    1 
ATOM   11477 C C     . SER D  1 297 ? -18.474 48.015  -41.795 1.00 39.22 ? 297 SER B C     1 
ATOM   11478 O O     . SER D  1 297 ? -18.700 48.129  -40.581 1.00 36.89 ? 297 SER B O     1 
ATOM   11479 C CB    . SER D  1 297 ? -19.631 50.155  -42.409 1.00 45.34 ? 297 SER B CB    1 
ATOM   11480 O OG    . SER D  1 297 ? -19.683 51.226  -43.349 1.00 44.68 ? 297 SER B OG    1 
ATOM   11481 N N     . GLU D  1 298 ? -18.268 46.841  -42.374 1.00 34.60 ? 298 GLU B N     1 
ATOM   11482 C CA    . GLU D  1 298 ? -18.175 45.617  -41.600 1.00 36.77 ? 298 GLU B CA    1 
ATOM   11483 C C     . GLU D  1 298 ? -16.763 45.488  -41.057 1.00 38.15 ? 298 GLU B C     1 
ATOM   11484 O O     . GLU D  1 298 ? -15.799 45.478  -41.827 1.00 47.84 ? 298 GLU B O     1 
ATOM   11485 C CB    . GLU D  1 298 ? -18.506 44.402  -42.461 1.00 34.93 ? 298 GLU B CB    1 
ATOM   11486 C CG    . GLU D  1 298 ? -19.909 44.355  -42.978 1.00 35.17 ? 298 GLU B CG    1 
ATOM   11487 C CD    . GLU D  1 298 ? -20.125 43.209  -43.955 1.00 40.21 ? 298 GLU B CD    1 
ATOM   11488 O OE1   . GLU D  1 298 ? -19.308 42.260  -44.002 1.00 36.79 ? 298 GLU B OE1   1 
ATOM   11489 O OE2   . GLU D  1 298 ? -21.125 43.261  -44.691 1.00 43.55 ? 298 GLU B OE2   1 
ATOM   11490 N N     . PHE D  1 299 ? -16.642 45.388  -39.746 1.00 40.57 ? 299 PHE B N     1 
ATOM   11491 C CA    . PHE D  1 299 ? -15.410 44.952  -39.106 1.00 39.78 ? 299 PHE B CA    1 
ATOM   11492 C C     . PHE D  1 299 ? -15.726 44.710  -37.632 1.00 40.45 ? 299 PHE B C     1 
ATOM   11493 O O     . PHE D  1 299 ? -16.879 44.823  -37.203 1.00 39.23 ? 299 PHE B O     1 
ATOM   11494 C CB    . PHE D  1 299 ? -14.270 45.948  -39.304 1.00 38.84 ? 299 PHE B CB    1 
ATOM   11495 C CG    . PHE D  1 299 ? -14.716 47.363  -39.362 1.00 43.21 ? 299 PHE B CG    1 
ATOM   11496 C CD1   . PHE D  1 299 ? -14.957 48.063  -38.189 1.00 42.78 ? 299 PHE B CD1   1 
ATOM   11497 C CD2   . PHE D  1 299 ? -14.881 48.008  -40.581 1.00 44.38 ? 299 PHE B CD2   1 
ATOM   11498 C CE1   . PHE D  1 299 ? -15.369 49.382  -38.226 1.00 46.51 ? 299 PHE B CE1   1 
ATOM   11499 C CE2   . PHE D  1 299 ? -15.297 49.331  -40.630 1.00 51.20 ? 299 PHE B CE2   1 
ATOM   11500 C CZ    . PHE D  1 299 ? -15.544 50.022  -39.448 1.00 47.22 ? 299 PHE B CZ    1 
ATOM   11501 N N     . GLU D  1 300 ? -14.686 44.366  -36.861 1.00 39.15 ? 300 GLU B N     1 
ATOM   11502 C CA    . GLU D  1 300 ? -14.907 43.777  -35.546 1.00 43.89 ? 300 GLU B CA    1 
ATOM   11503 C C     . GLU D  1 300 ? -15.571 44.762  -34.601 1.00 38.38 ? 300 GLU B C     1 
ATOM   11504 O O     . GLU D  1 300 ? -16.607 44.458  -34.002 1.00 38.42 ? 300 GLU B O     1 
ATOM   11505 C CB    . GLU D  1 300 ? -13.595 43.276  -34.963 1.00 42.41 ? 300 GLU B CB    1 
ATOM   11506 C CG    . GLU D  1 300 ? -13.817 42.065  -34.100 1.00 43.93 ? 300 GLU B CG    1 
ATOM   11507 C CD    . GLU D  1 300 ? -12.937 42.044  -32.884 1.00 51.53 ? 300 GLU B CD    1 
ATOM   11508 O OE1   . GLU D  1 300 ? -12.069 42.939  -32.749 1.00 47.92 ? 300 GLU B OE1   1 
ATOM   11509 O OE2   . GLU D  1 300 ? -13.126 41.129  -32.052 1.00 63.89 ? 300 GLU B OE2   1 
ATOM   11510 N N     . ALA D  1 301 ? -15.003 45.961  -34.468 1.00 40.15 ? 301 ALA B N     1 
ATOM   11511 C CA    . ALA D  1 301 ? -15.599 46.971  -33.592 1.00 48.41 ? 301 ALA B CA    1 
ATOM   11512 C C     . ALA D  1 301 ? -17.057 47.277  -33.943 1.00 47.13 ? 301 ALA B C     1 
ATOM   11513 O O     . ALA D  1 301 ? -17.741 47.952  -33.162 1.00 42.01 ? 301 ALA B O     1 
ATOM   11514 C CB    . ALA D  1 301 ? -14.781 48.268  -33.635 1.00 43.17 ? 301 ALA B CB    1 
ATOM   11515 N N     . THR D  1 302 ? -17.535 46.787  -35.088 1.00 44.11 ? 302 THR B N     1 
ATOM   11516 C CA    . THR D  1 302 ? -18.873 47.061  -35.587 1.00 39.09 ? 302 THR B CA    1 
ATOM   11517 C C     . THR D  1 302 ? -19.715 45.793  -35.652 1.00 35.44 ? 302 THR B C     1 
ATOM   11518 O O     . THR D  1 302 ? -20.765 45.727  -35.005 1.00 37.49 ? 302 THR B O     1 
ATOM   11519 C CB    . THR D  1 302 ? -18.753 47.751  -36.961 1.00 43.42 ? 302 THR B CB    1 
ATOM   11520 O OG1   . THR D  1 302 ? -18.227 49.075  -36.779 1.00 43.87 ? 302 THR B OG1   1 
ATOM   11521 C CG2   . THR D  1 302 ? -20.089 47.861  -37.665 1.00 35.93 ? 302 THR B CG2   1 
ATOM   11522 N N     . LEU D  1 303 ? -19.277 44.774  -36.390 1.00 39.86 ? 303 LEU B N     1 
ATOM   11523 C CA    . LEU D  1 303 ? -20.041 43.533  -36.488 1.00 31.76 ? 303 LEU B CA    1 
ATOM   11524 C C     . LEU D  1 303 ? -20.262 42.889  -35.123 1.00 37.54 ? 303 LEU B C     1 
ATOM   11525 O O     . LEU D  1 303 ? -21.275 42.209  -34.919 1.00 35.14 ? 303 LEU B O     1 
ATOM   11526 C CB    . LEU D  1 303 ? -19.324 42.560  -37.420 1.00 26.72 ? 303 LEU B CB    1 
ATOM   11527 C CG    . LEU D  1 303 ? -19.109 42.936  -38.902 1.00 37.67 ? 303 LEU B CG    1 
ATOM   11528 C CD1   . LEU D  1 303 ? -18.048 42.033  -39.553 1.00 34.10 ? 303 LEU B CD1   1 
ATOM   11529 C CD2   . LEU D  1 303 ? -20.417 42.896  -39.723 1.00 28.06 ? 303 LEU B CD2   1 
ATOM   11530 N N     . LYS D  1 304 ? -19.343 43.119  -34.167 1.00 41.30 ? 304 LYS B N     1 
ATOM   11531 C CA    . LYS D  1 304 ? -19.310 42.439  -32.874 1.00 39.50 ? 304 LYS B CA    1 
ATOM   11532 C C     . LYS D  1 304 ? -20.335 43.036  -31.905 1.00 36.76 ? 304 LYS B C     1 
ATOM   11533 O O     . LYS D  1 304 ? -21.257 42.318  -31.492 1.00 39.80 ? 304 LYS B O     1 
ATOM   11534 C CB    . LYS D  1 304 ? -17.875 42.463  -32.321 1.00 40.76 ? 304 LYS B CB    1 
ATOM   11535 C CG    . LYS D  1 304 ? -17.685 41.947  -30.933 1.00 46.16 ? 304 LYS B CG    1 
ATOM   11536 C CD    . LYS D  1 304 ? -17.664 43.085  -29.921 1.00 51.45 ? 304 LYS B CD    1 
ATOM   11537 C CE    . LYS D  1 304 ? -18.535 42.726  -28.713 1.00 49.19 ? 304 LYS B CE    1 
ATOM   11538 N NZ    . LYS D  1 304 ? -18.630 43.821  -27.724 1.00 41.87 ? 304 LYS B NZ    1 
ATOM   11539 N N     . PRO D  1 305 ? -20.262 44.323  -31.534 1.00 36.75 ? 305 PRO B N     1 
ATOM   11540 C CA    . PRO D  1 305 ? -21.268 44.835  -30.578 1.00 39.35 ? 305 PRO B CA    1 
ATOM   11541 C C     . PRO D  1 305 ? -22.705 44.709  -31.083 1.00 40.54 ? 305 PRO B C     1 
ATOM   11542 O O     . PRO D  1 305 ? -23.639 44.535  -30.281 1.00 39.26 ? 305 PRO B O     1 
ATOM   11543 C CB    . PRO D  1 305 ? -20.856 46.303  -30.384 1.00 35.28 ? 305 PRO B CB    1 
ATOM   11544 C CG    . PRO D  1 305 ? -19.420 46.366  -30.855 1.00 37.63 ? 305 PRO B CG    1 
ATOM   11545 C CD    . PRO D  1 305 ? -19.361 45.401  -31.986 1.00 37.52 ? 305 PRO B CD    1 
ATOM   11546 N N     . ALA D  1 306 ? -22.896 44.771  -32.403 1.00 39.01 ? 306 ALA B N     1 
ATOM   11547 C CA    . ALA D  1 306 ? -24.231 44.709  -32.984 1.00 32.90 ? 306 ALA B CA    1 
ATOM   11548 C C     . ALA D  1 306 ? -24.769 43.293  -32.949 1.00 34.61 ? 306 ALA B C     1 
ATOM   11549 O O     . ALA D  1 306 ? -25.909 43.062  -32.532 1.00 34.17 ? 306 ALA B O     1 
ATOM   11550 C CB    . ALA D  1 306 ? -24.197 45.213  -34.421 1.00 32.65 ? 306 ALA B CB    1 
ATOM   11551 N N     . GLU D  1 307 ? -23.967 42.334  -33.415 1.00 36.64 ? 307 GLU B N     1 
ATOM   11552 C CA    . GLU D  1 307 ? -24.337 40.932  -33.274 1.00 36.06 ? 307 GLU B CA    1 
ATOM   11553 C C     . GLU D  1 307 ? -24.597 40.587  -31.815 1.00 35.68 ? 307 GLU B C     1 
ATOM   11554 O O     . GLU D  1 307 ? -25.533 39.846  -31.502 1.00 31.04 ? 307 GLU B O     1 
ATOM   11555 C CB    . GLU D  1 307 ? -23.243 40.042  -33.861 1.00 37.21 ? 307 GLU B CB    1 
ATOM   11556 C CG    . GLU D  1 307 ? -23.393 38.565  -33.560 1.00 45.64 ? 307 GLU B CG    1 
ATOM   11557 C CD    . GLU D  1 307 ? -22.050 37.854  -33.418 1.00 55.87 ? 307 GLU B CD    1 
ATOM   11558 O OE1   . GLU D  1 307 ? -21.101 38.202  -34.164 1.00 51.74 ? 307 GLU B OE1   1 
ATOM   11559 O OE2   . GLU D  1 307 ? -21.945 36.951  -32.549 1.00 55.79 ? 307 GLU B OE2   1 
ATOM   11560 N N     . GLU D  1 308 ? -23.793 41.131  -30.902 1.00 36.32 ? 308 GLU B N     1 
ATOM   11561 C CA    . GLU D  1 308 ? -24.108 40.963  -29.493 1.00 35.30 ? 308 GLU B CA    1 
ATOM   11562 C C     . GLU D  1 308 ? -25.504 41.481  -29.200 1.00 33.75 ? 308 GLU B C     1 
ATOM   11563 O O     . GLU D  1 308 ? -26.370 40.744  -28.715 1.00 32.76 ? 308 GLU B O     1 
ATOM   11564 C CB    . GLU D  1 308 ? -23.085 41.685  -28.629 1.00 42.05 ? 308 GLU B CB    1 
ATOM   11565 C CG    . GLU D  1 308 ? -23.060 41.173  -27.195 1.00 39.38 ? 308 GLU B CG    1 
ATOM   11566 C CD    . GLU D  1 308 ? -22.398 42.143  -26.216 1.00 43.47 ? 308 GLU B CD    1 
ATOM   11567 O OE1   . GLU D  1 308 ? -21.795 43.150  -26.657 1.00 42.73 ? 308 GLU B OE1   1 
ATOM   11568 O OE2   . GLU D  1 308 ? -22.474 41.889  -24.990 1.00 46.28 ? 308 GLU B OE2   1 
ATOM   11569 N N     . PHE D  1 309 ? -25.752 42.747  -29.526 1.00 32.31 ? 309 PHE B N     1 
ATOM   11570 C CA    . PHE D  1 309 ? -27.067 43.314  -29.293 1.00 31.28 ? 309 PHE B CA    1 
ATOM   11571 C C     . PHE D  1 309 ? -28.162 42.398  -29.805 1.00 31.18 ? 309 PHE B C     1 
ATOM   11572 O O     . PHE D  1 309 ? -28.968 41.878  -29.027 1.00 31.43 ? 309 PHE B O     1 
ATOM   11573 C CB    . PHE D  1 309 ? -27.181 44.679  -29.952 1.00 32.12 ? 309 PHE B CB    1 
ATOM   11574 C CG    . PHE D  1 309 ? -28.488 45.343  -29.674 1.00 36.61 ? 309 PHE B CG    1 
ATOM   11575 C CD1   . PHE D  1 309 ? -28.662 46.072  -28.504 1.00 37.42 ? 309 PHE B CD1   1 
ATOM   11576 C CD2   . PHE D  1 309 ? -29.564 45.202  -30.549 1.00 37.02 ? 309 PHE B CD2   1 
ATOM   11577 C CE1   . PHE D  1 309 ? -29.876 46.670  -28.211 1.00 31.18 ? 309 PHE B CE1   1 
ATOM   11578 C CE2   . PHE D  1 309 ? -30.784 45.803  -30.268 1.00 33.13 ? 309 PHE B CE2   1 
ATOM   11579 C CZ    . PHE D  1 309 ? -30.935 46.534  -29.096 1.00 32.37 ? 309 PHE B CZ    1 
ATOM   11580 N N     . ILE D  1 310 ? -28.180 42.176  -31.123 1.00 32.67 ? 310 ILE B N     1 
ATOM   11581 C CA    . ILE D  1 310 ? -29.239 41.421  -31.804 1.00 33.11 ? 310 ILE B CA    1 
ATOM   11582 C C     . ILE D  1 310 ? -29.571 40.112  -31.095 1.00 32.26 ? 310 ILE B C     1 
ATOM   11583 O O     . ILE D  1 310 ? -30.736 39.687  -31.053 1.00 28.53 ? 310 ILE B O     1 
ATOM   11584 C CB    . ILE D  1 310 ? -28.819 41.155  -33.267 1.00 31.93 ? 310 ILE B CB    1 
ATOM   11585 C CG1   . ILE D  1 310 ? -28.641 42.465  -34.026 1.00 31.91 ? 310 ILE B CG1   1 
ATOM   11586 C CG2   . ILE D  1 310 ? -29.833 40.293  -33.971 1.00 29.30 ? 310 ILE B CG2   1 
ATOM   11587 C CD1   . ILE D  1 310 ? -29.928 42.984  -34.605 1.00 34.84 ? 310 ILE B CD1   1 
ATOM   11588 N N     . GLU D  1 311 ? -28.560 39.439  -30.544 1.00 35.08 ? 311 GLU B N     1 
ATOM   11589 C CA    . GLU D  1 311 ? -28.810 38.133  -29.949 1.00 31.76 ? 311 GLU B CA    1 
ATOM   11590 C C     . GLU D  1 311 ? -29.662 38.256  -28.696 1.00 28.07 ? 311 GLU B C     1 
ATOM   11591 O O     . GLU D  1 311 ? -30.534 37.419  -28.442 1.00 26.21 ? 311 GLU B O     1 
ATOM   11592 C CB    . GLU D  1 311 ? -27.484 37.432  -29.653 1.00 29.41 ? 311 GLU B CB    1 
ATOM   11593 C CG    . GLU D  1 311 ? -27.629 36.114  -28.869 1.00 36.07 ? 311 GLU B CG    1 
ATOM   11594 C CD    . GLU D  1 311 ? -28.419 35.032  -29.607 1.00 38.04 ? 311 GLU B CD    1 
ATOM   11595 O OE1   . GLU D  1 311 ? -28.353 34.966  -30.861 1.00 41.49 ? 311 GLU B OE1   1 
ATOM   11596 O OE2   . GLU D  1 311 ? -29.104 34.244  -28.914 1.00 38.24 ? 311 GLU B OE2   1 
ATOM   11597 N N     . MET D  1 312 ? -29.433 39.291  -27.896 1.00 28.80 ? 312 MET B N     1 
ATOM   11598 C CA    . MET D  1 312 ? -30.290 39.472  -26.734 1.00 34.09 ? 312 MET B CA    1 
ATOM   11599 C C     . MET D  1 312 ? -31.726 39.715  -27.156 1.00 32.04 ? 312 MET B C     1 
ATOM   11600 O O     . MET D  1 312 ? -32.664 39.269  -26.478 1.00 28.03 ? 312 MET B O     1 
ATOM   11601 C CB    . MET D  1 312 ? -29.784 40.623  -25.873 1.00 24.67 ? 312 MET B CB    1 
ATOM   11602 C CG    . MET D  1 312 ? -30.852 41.171  -25.008 1.00 29.63 ? 312 MET B CG    1 
ATOM   11603 S SD    . MET D  1 312 ? -30.586 42.930  -24.921 1.00 39.15 ? 312 MET B SD    1 
ATOM   11604 C CE    . MET D  1 312 ? -29.200 42.960  -23.813 1.00 32.52 ? 312 MET B CE    1 
ATOM   11605 N N     . ILE D  1 313 ? -31.919 40.403  -28.282 1.00 27.94 ? 313 ILE B N     1 
ATOM   11606 C CA    . ILE D  1 313 ? -33.280 40.604  -28.731 1.00 27.77 ? 313 ILE B CA    1 
ATOM   11607 C C     . ILE D  1 313 ? -33.817 39.299  -29.289 1.00 27.30 ? 313 ILE B C     1 
ATOM   11608 O O     . ILE D  1 313 ? -35.020 39.025  -29.198 1.00 28.07 ? 313 ILE B O     1 
ATOM   11609 C CB    . ILE D  1 313 ? -33.366 41.782  -29.727 1.00 31.91 ? 313 ILE B CB    1 
ATOM   11610 C CG1   . ILE D  1 313 ? -33.817 41.314  -31.096 1.00 24.24 ? 313 ILE B CG1   1 
ATOM   11611 C CG2   . ILE D  1 313 ? -32.076 42.565  -29.802 1.00 32.19 ? 313 ILE B CG2   1 
ATOM   11612 C CD1   . ILE D  1 313 ? -35.259 41.538  -31.269 1.00 28.88 ? 313 ILE B CD1   1 
ATOM   11613 N N     . ARG D  1 314 ? -32.939 38.452  -29.829 1.00 30.89 ? 314 ARG B N     1 
ATOM   11614 C CA    . ARG D  1 314 ? -33.324 37.066  -30.074 1.00 31.88 ? 314 ARG B CA    1 
ATOM   11615 C C     . ARG D  1 314 ? -33.835 36.430  -28.786 1.00 28.54 ? 314 ARG B C     1 
ATOM   11616 O O     . ARG D  1 314 ? -34.997 36.021  -28.707 1.00 23.86 ? 314 ARG B O     1 
ATOM   11617 C CB    . ARG D  1 314 ? -32.145 36.273  -30.648 1.00 30.06 ? 314 ARG B CB    1 
ATOM   11618 C CG    . ARG D  1 314 ? -32.514 35.119  -31.574 1.00 32.51 ? 314 ARG B CG    1 
ATOM   11619 C CD    . ARG D  1 314 ? -31.268 34.295  -31.973 1.00 35.83 ? 314 ARG B CD    1 
ATOM   11620 N NE    . ARG D  1 314 ? -30.875 33.382  -30.906 1.00 36.06 ? 314 ARG B NE    1 
ATOM   11621 C CZ    . ARG D  1 314 ? -31.585 32.321  -30.530 1.00 42.50 ? 314 ARG B CZ    1 
ATOM   11622 N NH1   . ARG D  1 314 ? -32.636 31.907  -31.221 1.00 40.95 ? 314 ARG B NH1   1 
ATOM   11623 N NH2   . ARG D  1 314 ? -31.231 31.654  -29.432 1.00 42.35 ? 314 ARG B NH2   1 
ATOM   11624 N N     . THR D  1 315 ? -32.980 36.381  -27.752 1.00 27.53 ? 315 THR B N     1 
ATOM   11625 C CA    . THR D  1 315 ? -33.354 35.793  -26.466 1.00 26.53 ? 315 THR B CA    1 
ATOM   11626 C C     . THR D  1 315 ? -34.683 36.348  -25.989 1.00 27.87 ? 315 THR B C     1 
ATOM   11627 O O     . THR D  1 315 ? -35.559 35.599  -25.539 1.00 23.35 ? 315 THR B O     1 
ATOM   11628 C CB    . THR D  1 315 ? -32.274 36.071  -25.418 1.00 29.31 ? 315 THR B CB    1 
ATOM   11629 O OG1   . THR D  1 315 ? -30.980 35.914  -26.000 1.00 30.81 ? 315 THR B OG1   1 
ATOM   11630 C CG2   . THR D  1 315 ? -32.396 35.121  -24.228 1.00 26.71 ? 315 THR B CG2   1 
ATOM   11631 N N     . ILE D  1 316 ? -34.868 37.660  -26.133 1.00 27.80 ? 316 ILE B N     1 
ATOM   11632 C CA    . ILE D  1 316 ? -36.091 38.301  -25.668 1.00 24.59 ? 316 ILE B CA    1 
ATOM   11633 C C     . ILE D  1 316 ? -37.322 37.683  -26.319 1.00 27.45 ? 316 ILE B C     1 
ATOM   11634 O O     . ILE D  1 316 ? -38.302 37.387  -25.633 1.00 32.91 ? 316 ILE B O     1 
ATOM   11635 C CB    . ILE D  1 316 ? -36.014 39.813  -25.901 1.00 23.61 ? 316 ILE B CB    1 
ATOM   11636 C CG1   . ILE D  1 316 ? -35.096 40.410  -24.852 1.00 26.45 ? 316 ILE B CG1   1 
ATOM   11637 C CG2   . ILE D  1 316 ? -37.364 40.423  -25.759 1.00 19.99 ? 316 ILE B CG2   1 
ATOM   11638 C CD1   . ILE D  1 316 ? -34.924 41.868  -24.981 1.00 26.63 ? 316 ILE B CD1   1 
ATOM   11639 N N     . GLY D  1 317 ? -37.309 37.478  -27.639 1.00 27.28 ? 317 GLY B N     1 
ATOM   11640 C CA    . GLY D  1 317 ? -38.370 36.663  -28.206 1.00 23.98 ? 317 GLY B CA    1 
ATOM   11641 C C     . GLY D  1 317 ? -38.782 36.915  -29.646 1.00 31.53 ? 317 GLY B C     1 
ATOM   11642 O O     . GLY D  1 317 ? -39.604 36.165  -30.184 1.00 32.96 ? 317 GLY B O     1 
ATOM   11643 N N     . TYR D  1 318 ? -38.245 37.951  -30.289 1.00 27.52 ? 318 TYR B N     1 
ATOM   11644 C CA    . TYR D  1 318 ? -38.635 38.222  -31.666 1.00 30.33 ? 318 TYR B CA    1 
ATOM   11645 C C     . TYR D  1 318 ? -38.117 37.128  -32.601 1.00 30.74 ? 318 TYR B C     1 
ATOM   11646 O O     . TYR D  1 318 ? -36.995 36.638  -32.461 1.00 31.46 ? 318 TYR B O     1 
ATOM   11647 C CB    . TYR D  1 318 ? -38.114 39.583  -32.121 1.00 24.75 ? 318 TYR B CB    1 
ATOM   11648 C CG    . TYR D  1 318 ? -38.438 39.876  -33.562 1.00 27.95 ? 318 TYR B CG    1 
ATOM   11649 C CD1   . TYR D  1 318 ? -39.655 40.431  -33.923 1.00 29.34 ? 318 TYR B CD1   1 
ATOM   11650 C CD2   . TYR D  1 318 ? -37.541 39.567  -34.565 1.00 34.51 ? 318 TYR B CD2   1 
ATOM   11651 C CE1   . TYR D  1 318 ? -39.969 40.687  -35.243 1.00 29.48 ? 318 TYR B CE1   1 
ATOM   11652 C CE2   . TYR D  1 318 ? -37.836 39.816  -35.886 1.00 35.49 ? 318 TYR B CE2   1 
ATOM   11653 C CZ    . TYR D  1 318 ? -39.056 40.375  -36.223 1.00 35.86 ? 318 TYR B CZ    1 
ATOM   11654 O OH    . TYR D  1 318 ? -39.352 40.622  -37.546 1.00 33.43 ? 318 TYR B OH    1 
ATOM   11655 N N     . ARG D  1 319 ? -38.936 36.740  -33.561 1.00 25.20 ? 319 ARG B N     1 
ATOM   11656 C CA    . ARG D  1 319 ? -38.490 35.854  -34.613 1.00 28.87 ? 319 ARG B CA    1 
ATOM   11657 C C     . ARG D  1 319 ? -38.823 36.550  -35.904 1.00 29.12 ? 319 ARG B C     1 
ATOM   11658 O O     . ARG D  1 319 ? -39.957 37.003  -36.077 1.00 34.26 ? 319 ARG B O     1 
ATOM   11659 C CB    . ARG D  1 319 ? -39.177 34.494  -34.542 1.00 31.22 ? 319 ARG B CB    1 
ATOM   11660 C CG    . ARG D  1 319 ? -39.077 33.846  -33.181 1.00 32.00 ? 319 ARG B CG    1 
ATOM   11661 C CD    . ARG D  1 319 ? -37.669 33.351  -32.942 1.00 29.89 ? 319 ARG B CD    1 
ATOM   11662 N NE    . ARG D  1 319 ? -37.566 32.580  -31.709 1.00 32.08 ? 319 ARG B NE    1 
ATOM   11663 C CZ    . ARG D  1 319 ? -37.092 33.049  -30.555 1.00 37.75 ? 319 ARG B CZ    1 
ATOM   11664 N NH1   . ARG D  1 319 ? -36.704 34.312  -30.420 1.00 28.50 ? 319 ARG B NH1   1 
ATOM   11665 N NH2   . ARG D  1 319 ? -36.982 32.224  -29.511 1.00 32.85 ? 319 ARG B NH2   1 
ATOM   11666 N N     . GLY D  1 320 ? -37.841 36.660  -36.792 1.00 30.73 ? 320 GLY B N     1 
ATOM   11667 C CA    . GLY D  1 320 ? -38.116 37.221  -38.099 1.00 33.42 ? 320 GLY B CA    1 
ATOM   11668 C C     . GLY D  1 320 ? -37.098 38.240  -38.566 1.00 31.41 ? 320 GLY B C     1 
ATOM   11669 O O     . GLY D  1 320 ? -35.961 38.229  -38.107 1.00 32.46 ? 320 GLY B O     1 
ATOM   11670 N N     . TYR D  1 321 ? -37.500 39.137  -39.456 1.00 31.73 ? 321 TYR B N     1 
ATOM   11671 C CA    . TYR D  1 321 ? -36.567 40.093  -40.033 1.00 33.30 ? 321 TYR B CA    1 
ATOM   11672 C C     . TYR D  1 321 ? -36.342 41.264  -39.085 1.00 29.14 ? 321 TYR B C     1 
ATOM   11673 O O     . TYR D  1 321 ? -37.293 41.921  -38.648 1.00 32.91 ? 321 TYR B O     1 
ATOM   11674 C CB    . TYR D  1 321 ? -37.085 40.579  -41.395 1.00 31.24 ? 321 TYR B CB    1 
ATOM   11675 C CG    . TYR D  1 321 ? -37.116 39.464  -42.420 1.00 36.35 ? 321 TYR B CG    1 
ATOM   11676 C CD1   . TYR D  1 321 ? -35.928 38.919  -42.925 1.00 36.49 ? 321 TYR B CD1   1 
ATOM   11677 C CD2   . TYR D  1 321 ? -38.318 38.924  -42.851 1.00 34.47 ? 321 TYR B CD2   1 
ATOM   11678 C CE1   . TYR D  1 321 ? -35.945 37.882  -43.839 1.00 32.75 ? 321 TYR B CE1   1 
ATOM   11679 C CE2   . TYR D  1 321 ? -38.345 37.884  -43.761 1.00 35.67 ? 321 TYR B CE2   1 
ATOM   11680 C CZ    . TYR D  1 321 ? -37.157 37.370  -44.258 1.00 38.61 ? 321 TYR B CZ    1 
ATOM   11681 O OH    . TYR D  1 321 ? -37.178 36.343  -45.176 1.00 48.11 ? 321 TYR B OH    1 
ATOM   11682 N N     . VAL D  1 322 ? -35.078 41.546  -38.793 1.00 27.48 ? 322 VAL B N     1 
ATOM   11683 C CA    . VAL D  1 322 ? -34.721 42.685  -37.957 1.00 31.73 ? 322 VAL B CA    1 
ATOM   11684 C C     . VAL D  1 322 ? -33.426 43.301  -38.476 1.00 30.48 ? 322 VAL B C     1 
ATOM   11685 O O     . VAL D  1 322 ? -32.595 42.619  -39.085 1.00 28.75 ? 322 VAL B O     1 
ATOM   11686 C CB    . VAL D  1 322 ? -34.608 42.276  -36.473 1.00 30.61 ? 322 VAL B CB    1 
ATOM   11687 C CG1   . VAL D  1 322 ? -33.485 41.293  -36.290 1.00 28.26 ? 322 VAL B CG1   1 
ATOM   11688 C CG2   . VAL D  1 322 ? -34.443 43.512  -35.579 1.00 30.97 ? 322 VAL B CG2   1 
ATOM   11689 N N     . ASN D  1 323 ? -33.289 44.620  -38.275 1.00 32.08 ? 323 ASN B N     1 
ATOM   11690 C CA    . ASN D  1 323 ? -32.111 45.375  -38.693 1.00 30.37 ? 323 ASN B CA    1 
ATOM   11691 C C     . ASN D  1 323 ? -31.755 46.403  -37.624 1.00 30.32 ? 323 ASN B C     1 
ATOM   11692 O O     . ASN D  1 323 ? -32.612 46.850  -36.864 1.00 33.94 ? 323 ASN B O     1 
ATOM   11693 C CB    . ASN D  1 323 ? -32.315 46.073  -40.051 1.00 33.12 ? 323 ASN B CB    1 
ATOM   11694 C CG    . ASN D  1 323 ? -33.377 47.150  -40.002 1.00 34.76 ? 323 ASN B CG    1 
ATOM   11695 O OD1   . ASN D  1 323 ? -33.188 48.201  -39.384 1.00 34.73 ? 323 ASN B OD1   1 
ATOM   11696 N ND2   . ASN D  1 323 ? -34.503 46.900  -40.665 1.00 34.21 ? 323 ASN B ND2   1 
ATOM   11697 N N     . ILE D  1 324 ? -30.472 46.790  -37.594 1.00 32.47 ? 324 ILE B N     1 
ATOM   11698 C CA    . ILE D  1 324 ? -29.916 47.767  -36.657 1.00 27.04 ? 324 ILE B CA    1 
ATOM   11699 C C     . ILE D  1 324 ? -29.000 48.732  -37.413 1.00 25.60 ? 324 ILE B C     1 
ATOM   11700 O O     . ILE D  1 324 ? -28.101 48.295  -38.135 1.00 28.61 ? 324 ILE B O     1 
ATOM   11701 C CB    . ILE D  1 324 ? -29.155 47.050  -35.516 1.00 28.53 ? 324 ILE B CB    1 
ATOM   11702 C CG1   . ILE D  1 324 ? -28.627 48.038  -34.483 1.00 29.91 ? 324 ILE B CG1   1 
ATOM   11703 C CG2   . ILE D  1 324 ? -28.030 46.178  -36.064 1.00 35.52 ? 324 ILE B CG2   1 
ATOM   11704 C CD1   . ILE D  1 324 ? -27.700 47.416  -33.524 1.00 32.85 ? 324 ILE B CD1   1 
ATOM   11705 N N     . ASP D  1 325 ? -29.221 50.043  -37.265 1.00 30.11 ? 325 ASP B N     1 
ATOM   11706 C CA    . ASP D  1 325 ? -28.392 51.030  -37.954 1.00 31.90 ? 325 ASP B CA    1 
ATOM   11707 C C     . ASP D  1 325 ? -27.349 51.643  -37.013 1.00 32.53 ? 325 ASP B C     1 
ATOM   11708 O O     . ASP D  1 325 ? -27.461 51.586  -35.786 1.00 30.34 ? 325 ASP B O     1 
ATOM   11709 C CB    . ASP D  1 325 ? -29.219 52.170  -38.593 1.00 26.75 ? 325 ASP B CB    1 
ATOM   11710 C CG    . ASP D  1 325 ? -30.747 51.985  -38.480 1.00 38.91 ? 325 ASP B CG    1 
ATOM   11711 O OD1   . ASP D  1 325 ? -31.265 50.839  -38.553 1.00 42.59 ? 325 ASP B OD1   1 
ATOM   11712 O OD2   . ASP D  1 325 ? -31.453 53.020  -38.344 1.00 38.20 ? 325 ASP B OD2   1 
ATOM   11713 N N     . GLY D  1 326 ? -26.334 52.251  -37.614 1.00 28.61 ? 326 GLY B N     1 
ATOM   11714 C CA    . GLY D  1 326 ? -25.348 52.977  -36.845 1.00 29.19 ? 326 GLY B CA    1 
ATOM   11715 C C     . GLY D  1 326 ? -24.436 53.778  -37.745 1.00 33.23 ? 326 GLY B C     1 
ATOM   11716 O O     . GLY D  1 326 ? -24.671 53.906  -38.950 1.00 35.91 ? 326 GLY B O     1 
ATOM   11717 N N     . ILE D  1 327 ? -23.370 54.317  -37.145 1.00 35.09 ? 327 ILE B N     1 
ATOM   11718 C CA    . ILE D  1 327 ? -22.412 55.159  -37.850 1.00 28.39 ? 327 ILE B CA    1 
ATOM   11719 C C     . ILE D  1 327 ? -20.998 54.813  -37.416 1.00 34.28 ? 327 ILE B C     1 
ATOM   11720 O O     . ILE D  1 327 ? -20.765 54.167  -36.390 1.00 33.50 ? 327 ILE B O     1 
ATOM   11721 C CB    . ILE D  1 327 ? -22.643 56.660  -37.617 1.00 28.17 ? 327 ILE B CB    1 
ATOM   11722 C CG1   . ILE D  1 327 ? -22.524 56.984  -36.129 1.00 30.59 ? 327 ILE B CG1   1 
ATOM   11723 C CG2   . ILE D  1 327 ? -23.972 57.092  -38.185 1.00 31.94 ? 327 ILE B CG2   1 
ATOM   11724 C CD1   . ILE D  1 327 ? -22.758 58.426  -35.800 1.00 31.25 ? 327 ILE B CD1   1 
ATOM   11725 N N     . VAL D  1 328 ? -20.050 55.311  -38.205 1.00 38.66 ? 328 VAL B N     1 
ATOM   11726 C CA    . VAL D  1 328 ? -18.619 55.215  -37.938 1.00 41.64 ? 328 VAL B CA    1 
ATOM   11727 C C     . VAL D  1 328 ? -18.042 56.609  -38.158 1.00 41.26 ? 328 VAL B C     1 
ATOM   11728 O O     . VAL D  1 328 ? -18.062 57.115  -39.285 1.00 50.57 ? 328 VAL B O     1 
ATOM   11729 C CB    . VAL D  1 328 ? -17.935 54.192  -38.858 1.00 39.94 ? 328 VAL B CB    1 
ATOM   11730 C CG1   . VAL D  1 328 ? -16.504 53.979  -38.448 1.00 42.94 ? 328 VAL B CG1   1 
ATOM   11731 C CG2   . VAL D  1 328 ? -18.711 52.877  -38.867 1.00 40.23 ? 328 VAL B CG2   1 
ATOM   11732 N N     . LEU D  1 329 ? -17.550 57.243  -37.101 1.00 39.82 ? 329 LEU B N     1 
ATOM   11733 C CA    . LEU D  1 329 ? -16.836 58.490  -37.339 1.00 44.69 ? 329 LEU B CA    1 
ATOM   11734 C C     . LEU D  1 329 ? -15.450 58.194  -37.902 1.00 47.37 ? 329 LEU B C     1 
ATOM   11735 O O     . LEU D  1 329 ? -14.938 57.076  -37.802 1.00 51.02 ? 329 LEU B O     1 
ATOM   11736 C CB    . LEU D  1 329 ? -16.701 59.318  -36.058 1.00 49.85 ? 329 LEU B CB    1 
ATOM   11737 C CG    . LEU D  1 329 ? -17.918 59.633  -35.176 1.00 54.35 ? 329 LEU B CG    1 
ATOM   11738 C CD1   . LEU D  1 329 ? -17.438 60.285  -33.882 1.00 51.57 ? 329 LEU B CD1   1 
ATOM   11739 C CD2   . LEU D  1 329 ? -18.977 60.505  -35.868 1.00 41.90 ? 329 LEU B CD2   1 
ATOM   11740 N N     . ASP D  1 330 ? -14.828 59.215  -38.495 1.00 49.42 ? 330 ASP B N     1 
ATOM   11741 C CA    . ASP D  1 330 ? -13.497 58.979  -39.038 1.00 50.42 ? 330 ASP B CA    1 
ATOM   11742 C C     . ASP D  1 330 ? -12.444 58.872  -37.952 1.00 49.49 ? 330 ASP B C     1 
ATOM   11743 O O     . ASP D  1 330 ? -11.327 58.435  -38.248 1.00 57.54 ? 330 ASP B O     1 
ATOM   11744 C CB    . ASP D  1 330 ? -13.111 60.063  -40.054 1.00 52.42 ? 330 ASP B CB    1 
ATOM   11745 C CG    . ASP D  1 330 ? -13.137 61.458  -39.468 1.00 59.38 ? 330 ASP B CG    1 
ATOM   11746 O OD1   . ASP D  1 330 ? -13.188 61.591  -38.221 1.00 62.95 ? 330 ASP B OD1   1 
ATOM   11747 O OD2   . ASP D  1 330 ? -13.107 62.426  -40.264 1.00 55.01 ? 330 ASP B OD2   1 
ATOM   11748 N N     . ASP D  1 331 ? -12.768 59.268  -36.718 1.00 50.08 ? 331 ASP B N     1 
ATOM   11749 C CA    . ASP D  1 331 ? -11.920 58.964  -35.571 1.00 48.35 ? 331 ASP B CA    1 
ATOM   11750 C C     . ASP D  1 331 ? -12.115 57.537  -35.071 1.00 49.29 ? 331 ASP B C     1 
ATOM   11751 O O     . ASP D  1 331 ? -11.459 57.139  -34.099 1.00 52.46 ? 331 ASP B O     1 
ATOM   11752 C CB    . ASP D  1 331 ? -12.151 59.984  -34.436 1.00 49.94 ? 331 ASP B CB    1 
ATOM   11753 C CG    . ASP D  1 331 ? -13.579 59.960  -33.857 1.00 52.10 ? 331 ASP B CG    1 
ATOM   11754 O OD1   . ASP D  1 331 ? -14.000 58.934  -33.285 1.00 50.35 ? 331 ASP B OD1   1 
ATOM   11755 O OD2   . ASP D  1 331 ? -14.278 60.999  -33.938 1.00 53.52 ? 331 ASP B OD2   1 
ATOM   11756 N N     . GLY D  1 332 ? -12.996 56.761  -35.720 1.00 47.71 ? 332 GLY B N     1 
ATOM   11757 C CA    . GLY D  1 332 ? -13.155 55.337  -35.497 1.00 45.54 ? 332 GLY B CA    1 
ATOM   11758 C C     . GLY D  1 332 ? -14.318 54.962  -34.599 1.00 45.57 ? 332 GLY B C     1 
ATOM   11759 O O     . GLY D  1 332 ? -14.820 53.832  -34.684 1.00 46.97 ? 332 GLY B O     1 
ATOM   11760 N N     . ARG D  1 333 ? -14.746 55.876  -33.735 1.00 40.88 ? 333 ARG B N     1 
ATOM   11761 C CA    . ARG D  1 333 ? -15.789 55.578  -32.770 1.00 37.55 ? 333 ARG B CA    1 
ATOM   11762 C C     . ARG D  1 333 ? -17.051 55.088  -33.462 1.00 42.75 ? 333 ARG B C     1 
ATOM   11763 O O     . ARG D  1 333 ? -17.518 55.687  -34.434 1.00 48.54 ? 333 ARG B O     1 
ATOM   11764 C CB    . ARG D  1 333 ? -16.084 56.820  -31.949 1.00 39.53 ? 333 ARG B CB    1 
ATOM   11765 C CG    . ARG D  1 333 ? -15.016 57.099  -30.946 1.00 34.44 ? 333 ARG B CG    1 
ATOM   11766 C CD    . ARG D  1 333 ? -15.403 58.239  -30.068 1.00 33.69 ? 333 ARG B CD    1 
ATOM   11767 N NE    . ARG D  1 333 ? -15.458 59.491  -30.803 1.00 36.86 ? 333 ARG B NE    1 
ATOM   11768 C CZ    . ARG D  1 333 ? -16.311 60.466  -30.525 1.00 42.90 ? 333 ARG B CZ    1 
ATOM   11769 N NH1   . ARG D  1 333 ? -17.227 60.333  -29.578 1.00 35.60 ? 333 ARG B NH1   1 
ATOM   11770 N NH2   . ARG D  1 333 ? -16.242 61.604  -31.211 1.00 41.97 ? 333 ARG B NH2   1 
ATOM   11771 N N     . VAL D  1 334 ? -17.591 53.986  -32.976 1.00 36.39 ? 334 VAL B N     1 
ATOM   11772 C CA    . VAL D  1 334 ? -18.828 53.435  -33.506 1.00 34.24 ? 334 VAL B CA    1 
ATOM   11773 C C     . VAL D  1 334 ? -19.966 53.803  -32.567 1.00 36.54 ? 334 VAL B C     1 
ATOM   11774 O O     . VAL D  1 334 ? -19.768 53.964  -31.358 1.00 36.93 ? 334 VAL B O     1 
ATOM   11775 C CB    . VAL D  1 334 ? -18.687 51.911  -33.687 1.00 33.68 ? 334 VAL B CB    1 
ATOM   11776 C CG1   . VAL D  1 334 ? -20.002 51.273  -34.027 1.00 29.24 ? 334 VAL B CG1   1 
ATOM   11777 C CG2   . VAL D  1 334 ? -17.650 51.628  -34.772 1.00 37.25 ? 334 VAL B CG2   1 
ATOM   11778 N N     . PHE D  1 335 ? -21.167 53.965  -33.131 1.00 36.55 ? 335 PHE B N     1 
ATOM   11779 C CA    . PHE D  1 335 ? -22.377 54.235  -32.361 1.00 33.24 ? 335 PHE B CA    1 
ATOM   11780 C C     . PHE D  1 335 ? -23.583 53.683  -33.117 1.00 30.54 ? 335 PHE B C     1 
ATOM   11781 O O     . PHE D  1 335 ? -23.614 53.767  -34.344 1.00 31.71 ? 335 PHE B O     1 
ATOM   11782 C CB    . PHE D  1 335 ? -22.546 55.742  -32.130 1.00 38.43 ? 335 PHE B CB    1 
ATOM   11783 C CG    . PHE D  1 335 ? -21.493 56.341  -31.244 1.00 43.85 ? 335 PHE B CG    1 
ATOM   11784 C CD1   . PHE D  1 335 ? -21.477 56.079  -29.883 1.00 39.70 ? 335 PHE B CD1   1 
ATOM   11785 C CD2   . PHE D  1 335 ? -20.512 57.170  -31.781 1.00 47.02 ? 335 PHE B CD2   1 
ATOM   11786 C CE1   . PHE D  1 335 ? -20.504 56.626  -29.072 1.00 37.50 ? 335 PHE B CE1   1 
ATOM   11787 C CE2   . PHE D  1 335 ? -19.536 57.719  -30.976 1.00 45.60 ? 335 PHE B CE2   1 
ATOM   11788 C CZ    . PHE D  1 335 ? -19.535 57.442  -29.614 1.00 42.50 ? 335 PHE B CZ    1 
ATOM   11789 N N     . PHE D  1 336 ? -24.587 53.158  -32.396 1.00 28.82 ? 336 PHE B N     1 
ATOM   11790 C CA    . PHE D  1 336 ? -25.804 52.623  -33.011 1.00 31.64 ? 336 PHE B CA    1 
ATOM   11791 C C     . PHE D  1 336 ? -27.051 53.457  -32.697 1.00 32.28 ? 336 PHE B C     1 
ATOM   11792 O O     . PHE D  1 336 ? -27.197 54.014  -31.604 1.00 34.43 ? 336 PHE B O     1 
ATOM   11793 C CB    . PHE D  1 336 ? -26.035 51.182  -32.578 1.00 28.10 ? 336 PHE B CB    1 
ATOM   11794 C CG    . PHE D  1 336 ? -25.031 50.232  -33.137 1.00 32.20 ? 336 PHE B CG    1 
ATOM   11795 C CD1   . PHE D  1 336 ? -23.840 49.980  -32.455 1.00 35.75 ? 336 PHE B CD1   1 
ATOM   11796 C CD2   . PHE D  1 336 ? -25.250 49.607  -34.354 1.00 30.46 ? 336 PHE B CD2   1 
ATOM   11797 C CE1   . PHE D  1 336 ? -22.889 49.100  -32.962 1.00 31.27 ? 336 PHE B CE1   1 
ATOM   11798 C CE2   . PHE D  1 336 ? -24.309 48.725  -34.869 1.00 32.74 ? 336 PHE B CE2   1 
ATOM   11799 C CZ    . PHE D  1 336 ? -23.123 48.472  -34.168 1.00 33.91 ? 336 PHE B CZ    1 
ATOM   11800 N N     . HIS D  1 337 ? -27.963 53.519  -33.676 1.00 30.46 ? 337 HIS B N     1 
ATOM   11801 C CA    . HIS D  1 337 ? -29.154 54.368  -33.627 1.00 31.17 ? 337 HIS B CA    1 
ATOM   11802 C C     . HIS D  1 337 ? -30.365 53.651  -33.056 1.00 30.81 ? 337 HIS B C     1 
ATOM   11803 O O     . HIS D  1 337 ? -31.020 54.173  -32.147 1.00 37.29 ? 337 HIS B O     1 
ATOM   11804 C CB    . HIS D  1 337 ? -29.533 54.875  -35.026 1.00 31.65 ? 337 HIS B CB    1 
ATOM   11805 C CG    . HIS D  1 337 ? -28.442 55.617  -35.728 1.00 35.56 ? 337 HIS B CG    1 
ATOM   11806 N ND1   . HIS D  1 337 ? -27.650 56.551  -35.095 1.00 34.31 ? 337 HIS B ND1   1 
ATOM   11807 C CD2   . HIS D  1 337 ? -28.014 55.571  -37.014 1.00 34.70 ? 337 HIS B CD2   1 
ATOM   11808 C CE1   . HIS D  1 337 ? -26.773 57.038  -35.957 1.00 33.10 ? 337 HIS B CE1   1 
ATOM   11809 N NE2   . HIS D  1 337 ? -26.977 56.464  -37.130 1.00 31.42 ? 337 HIS B NE2   1 
ATOM   11810 N N     . GLU D  1 338 ? -30.699 52.485  -33.601 1.00 30.12 ? 338 GLU B N     1 
ATOM   11811 C CA    . GLU D  1 338 ? -32.000 51.871  -33.353 1.00 32.04 ? 338 GLU B CA    1 
ATOM   11812 C C     . GLU D  1 338 ? -31.987 50.439  -33.872 1.00 33.62 ? 338 GLU B C     1 
ATOM   11813 O O     . GLU D  1 338 ? -31.014 49.984  -34.484 1.00 29.16 ? 338 GLU B O     1 
ATOM   11814 C CB    . GLU D  1 338 ? -33.120 52.663  -34.036 1.00 35.08 ? 338 GLU B CB    1 
ATOM   11815 C CG    . GLU D  1 338 ? -32.891 52.864  -35.531 1.00 32.94 ? 338 GLU B CG    1 
ATOM   11816 C CD    . GLU D  1 338 ? -34.180 52.938  -36.337 1.00 37.30 ? 338 GLU B CD    1 
ATOM   11817 O OE1   . GLU D  1 338 ? -35.260 53.109  -35.728 1.00 39.79 ? 338 GLU B OE1   1 
ATOM   11818 O OE2   . GLU D  1 338 ? -34.119 52.856  -37.584 1.00 31.51 ? 338 GLU B OE2   1 
ATOM   11819 N N     . ILE D  1 339 ? -33.094 49.728  -33.610 1.00 36.14 ? 339 ILE B N     1 
ATOM   11820 C CA    . ILE D  1 339 ? -33.501 48.543  -34.357 1.00 37.21 ? 339 ILE B CA    1 
ATOM   11821 C C     . ILE D  1 339 ? -34.837 48.843  -35.024 1.00 34.52 ? 339 ILE B C     1 
ATOM   11822 O O     . ILE D  1 339 ? -35.588 49.715  -34.590 1.00 38.96 ? 339 ILE B O     1 
ATOM   11823 C CB    . ILE D  1 339 ? -33.628 47.270  -33.481 1.00 37.56 ? 339 ILE B CB    1 
ATOM   11824 C CG1   . ILE D  1 339 ? -34.385 47.530  -32.167 1.00 34.59 ? 339 ILE B CG1   1 
ATOM   11825 C CG2   . ILE D  1 339 ? -32.264 46.625  -33.262 1.00 39.66 ? 339 ILE B CG2   1 
ATOM   11826 C CD1   . ILE D  1 339 ? -35.900 47.477  -32.277 1.00 31.43 ? 339 ILE B CD1   1 
ATOM   11827 N N     . ASN D  1 340 ? -35.142 48.093  -36.075 1.00 32.32 ? 340 ASN B N     1 
ATOM   11828 C CA    . ASN D  1 340 ? -36.503 48.015  -36.580 1.00 30.80 ? 340 ASN B CA    1 
ATOM   11829 C C     . ASN D  1 340 ? -36.777 46.546  -36.828 1.00 33.17 ? 340 ASN B C     1 
ATOM   11830 O O     . ASN D  1 340 ? -36.018 45.889  -37.544 1.00 34.35 ? 340 ASN B O     1 
ATOM   11831 C CB    . ASN D  1 340 ? -36.689 48.862  -37.844 1.00 35.72 ? 340 ASN B CB    1 
ATOM   11832 C CG    . ASN D  1 340 ? -35.836 50.138  -37.836 1.00 39.37 ? 340 ASN B CG    1 
ATOM   11833 O OD1   . ASN D  1 340 ? -34.606 50.073  -37.902 1.00 37.48 ? 340 ASN B OD1   1 
ATOM   11834 N ND2   . ASN D  1 340 ? -36.490 51.301  -37.711 1.00 34.77 ? 340 ASN B ND2   1 
ATOM   11835 N N     . ALA D  1 341 ? -37.814 46.011  -36.185 1.00 36.03 ? 341 ALA B N     1 
ATOM   11836 C CA    . ALA D  1 341 ? -38.116 44.586  -36.283 1.00 31.91 ? 341 ALA B CA    1 
ATOM   11837 C C     . ALA D  1 341 ? -39.237 44.439  -37.303 1.00 38.42 ? 341 ALA B C     1 
ATOM   11838 O O     . ALA D  1 341 ? -40.417 44.277  -36.981 1.00 40.32 ? 341 ALA B O     1 
ATOM   11839 C CB    . ALA D  1 341 ? -38.477 44.003  -34.926 1.00 35.10 ? 341 ALA B CB    1 
ATOM   11840 N N     . ARG D  1 342 ? -38.839 44.501  -38.555 1.00 31.62 ? 342 ARG B N     1 
ATOM   11841 C CA    . ARG D  1 342 ? -39.737 44.514  -39.697 1.00 36.61 ? 342 ARG B CA    1 
ATOM   11842 C C     . ARG D  1 342 ? -38.833 44.347  -40.903 1.00 35.50 ? 342 ARG B C     1 
ATOM   11843 O O     . ARG D  1 342 ? -37.621 44.144  -40.764 1.00 33.06 ? 342 ARG B O     1 
ATOM   11844 C CB    . ARG D  1 342 ? -40.559 45.808  -39.761 1.00 31.07 ? 342 ARG B CB    1 
ATOM   11845 C CG    . ARG D  1 342 ? -39.705 47.063  -39.551 1.00 33.11 ? 342 ARG B CG    1 
ATOM   11846 C CD    . ARG D  1 342 ? -40.189 48.241  -40.373 1.00 36.06 ? 342 ARG B CD    1 
ATOM   11847 N NE    . ARG D  1 342 ? -39.764 49.564  -39.896 1.00 47.30 ? 342 ARG B NE    1 
ATOM   11848 C CZ    . ARG D  1 342 ? -38.652 50.210  -40.252 1.00 43.24 ? 342 ARG B CZ    1 
ATOM   11849 N NH1   . ARG D  1 342 ? -37.714 49.632  -40.994 1.00 38.41 ? 342 ARG B NH1   1 
ATOM   11850 N NH2   . ARG D  1 342 ? -38.478 51.472  -39.851 1.00 32.13 ? 342 ARG B NH2   1 
ATOM   11851 N N     . TRP D  1 343 ? -39.397 44.445  -42.082 1.00 29.30 ? 343 TRP B N     1 
ATOM   11852 C CA    . TRP D  1 343 ? -38.525 44.569  -43.225 1.00 33.83 ? 343 TRP B CA    1 
ATOM   11853 C C     . TRP D  1 343 ? -37.794 45.896  -43.113 1.00 37.28 ? 343 TRP B C     1 
ATOM   11854 O O     . TRP D  1 343 ? -38.392 46.923  -42.768 1.00 33.58 ? 343 TRP B O     1 
ATOM   11855 C CB    . TRP D  1 343 ? -39.315 44.479  -44.528 1.00 31.88 ? 343 TRP B CB    1 
ATOM   11856 C CG    . TRP D  1 343 ? -40.092 43.201  -44.627 1.00 34.74 ? 343 TRP B CG    1 
ATOM   11857 C CD1   . TRP D  1 343 ? -39.904 42.069  -43.875 1.00 36.86 ? 343 TRP B CD1   1 
ATOM   11858 C CD2   . TRP D  1 343 ? -41.183 42.917  -45.515 1.00 28.25 ? 343 TRP B CD2   1 
ATOM   11859 N NE1   . TRP D  1 343 ? -40.807 41.101  -44.252 1.00 38.05 ? 343 TRP B NE1   1 
ATOM   11860 C CE2   . TRP D  1 343 ? -41.603 41.597  -45.251 1.00 31.19 ? 343 TRP B CE2   1 
ATOM   11861 C CE3   . TRP D  1 343 ? -41.835 43.644  -46.511 1.00 28.33 ? 343 TRP B CE3   1 
ATOM   11862 C CZ2   . TRP D  1 343 ? -42.650 40.995  -45.937 1.00 34.03 ? 343 TRP B CZ2   1 
ATOM   11863 C CZ3   . TRP D  1 343 ? -42.859 43.045  -47.196 1.00 32.79 ? 343 TRP B CZ3   1 
ATOM   11864 C CH2   . TRP D  1 343 ? -43.265 41.731  -46.904 1.00 31.19 ? 343 TRP B CH2   1 
ATOM   11865 N N     . SER D  1 344 ? -36.483 45.859  -43.329 1.00 31.16 ? 344 SER B N     1 
ATOM   11866 C CA    . SER D  1 344 ? -35.811 47.084  -43.683 1.00 35.46 ? 344 SER B CA    1 
ATOM   11867 C C     . SER D  1 344 ? -36.377 47.593  -45.003 1.00 40.80 ? 344 SER B C     1 
ATOM   11868 O O     . SER D  1 344 ? -37.129 46.903  -45.703 1.00 39.93 ? 344 SER B O     1 
ATOM   11869 C CB    . SER D  1 344 ? -34.319 46.855  -43.842 1.00 33.82 ? 344 SER B CB    1 
ATOM   11870 O OG    . SER D  1 344 ? -34.059 46.390  -45.151 1.00 35.58 ? 344 SER B OG    1 
ATOM   11871 N N     . GLY D  1 345 ? -35.996 48.813  -45.360 1.00 38.41 ? 345 GLY B N     1 
ATOM   11872 C CA    . GLY D  1 345 ? -36.258 49.252  -46.714 1.00 36.39 ? 345 GLY B CA    1 
ATOM   11873 C C     . GLY D  1 345 ? -35.553 48.374  -47.726 1.00 39.13 ? 345 GLY B C     1 
ATOM   11874 O O     . GLY D  1 345 ? -36.093 48.091  -48.797 1.00 39.34 ? 345 GLY B O     1 
ATOM   11875 N N     . GLY D  1 346 ? -34.354 47.894  -47.381 1.00 38.42 ? 346 GLY B N     1 
ATOM   11876 C CA    . GLY D  1 346 ? -33.444 47.302  -48.338 1.00 35.51 ? 346 GLY B CA    1 
ATOM   11877 C C     . GLY D  1 346 ? -33.474 45.805  -48.433 1.00 37.20 ? 346 GLY B C     1 
ATOM   11878 O O     . GLY D  1 346 ? -32.790 45.241  -49.298 1.00 34.80 ? 346 GLY B O     1 
ATOM   11879 N N     . LEU D  1 347 ? -34.236 45.146  -47.557 1.00 36.55 ? 347 LEU B N     1 
ATOM   11880 C CA    . LEU D  1 347 ? -34.395 43.700  -47.628 1.00 32.04 ? 347 LEU B CA    1 
ATOM   11881 C C     . LEU D  1 347 ? -34.711 43.242  -49.053 1.00 38.14 ? 347 LEU B C     1 
ATOM   11882 O O     . LEU D  1 347 ? -34.141 42.255  -49.542 1.00 35.87 ? 347 LEU B O     1 
ATOM   11883 C CB    . LEU D  1 347 ? -35.491 43.273  -46.649 1.00 28.62 ? 347 LEU B CB    1 
ATOM   11884 C CG    . LEU D  1 347 ? -36.084 41.861  -46.714 1.00 29.05 ? 347 LEU B CG    1 
ATOM   11885 C CD1   . LEU D  1 347 ? -35.018 40.783  -46.714 1.00 28.96 ? 347 LEU B CD1   1 
ATOM   11886 C CD2   . LEU D  1 347 ? -37.001 41.653  -45.542 1.00 30.79 ? 347 LEU B CD2   1 
ATOM   11887 N N     . ILE D  1 348 ? -35.581 43.970  -49.755 1.00 34.39 ? 348 ILE B N     1 
ATOM   11888 C CA    . ILE D  1 348 ? -36.027 43.481  -51.051 1.00 31.56 ? 348 ILE B CA    1 
ATOM   11889 C C     . ILE D  1 348 ? -34.893 43.544  -52.071 1.00 32.80 ? 348 ILE B C     1 
ATOM   11890 O O     . ILE D  1 348 ? -34.851 42.724  -52.997 1.00 32.34 ? 348 ILE B O     1 
ATOM   11891 C CB    . ILE D  1 348 ? -37.278 44.263  -51.498 1.00 34.09 ? 348 ILE B CB    1 
ATOM   11892 C CG1   . ILE D  1 348 ? -37.733 43.828  -52.890 1.00 33.82 ? 348 ILE B CG1   1 
ATOM   11893 C CG2   . ILE D  1 348 ? -37.055 45.766  -51.407 1.00 33.82 ? 348 ILE B CG2   1 
ATOM   11894 C CD1   . ILE D  1 348 ? -38.468 42.522  -52.866 1.00 37.06 ? 348 ILE B CD1   1 
ATOM   11895 N N     . TYR D  1 349 ? -33.947 44.489  -51.915 1.00 31.51 ? 349 TYR B N     1 
ATOM   11896 C CA    . TYR D  1 349 ? -32.773 44.519  -52.792 1.00 33.46 ? 349 TYR B CA    1 
ATOM   11897 C C     . TYR D  1 349 ? -31.879 43.322  -52.543 1.00 32.83 ? 349 TYR B C     1 
ATOM   11898 O O     . TYR D  1 349 ? -31.372 42.701  -53.484 1.00 36.38 ? 349 TYR B O     1 
ATOM   11899 C CB    . TYR D  1 349 ? -31.925 45.775  -52.583 1.00 35.63 ? 349 TYR B CB    1 
ATOM   11900 C CG    . TYR D  1 349 ? -32.623 47.096  -52.682 1.00 35.12 ? 349 TYR B CG    1 
ATOM   11901 C CD1   . TYR D  1 349 ? -33.867 47.217  -53.277 1.00 39.56 ? 349 TYR B CD1   1 
ATOM   11902 C CD2   . TYR D  1 349 ? -32.014 48.240  -52.198 1.00 35.63 ? 349 TYR B CD2   1 
ATOM   11903 C CE1   . TYR D  1 349 ? -34.494 48.446  -53.365 1.00 41.10 ? 349 TYR B CE1   1 
ATOM   11904 C CE2   . TYR D  1 349 ? -32.629 49.464  -52.274 1.00 33.88 ? 349 TYR B CE2   1 
ATOM   11905 C CZ    . TYR D  1 349 ? -33.866 49.563  -52.859 1.00 36.58 ? 349 TYR B CZ    1 
ATOM   11906 O OH    . TYR D  1 349 ? -34.471 50.788  -52.939 1.00 39.36 ? 349 TYR B OH    1 
ATOM   11907 N N     . HIS D  1 350 ? -31.602 43.037  -51.277 1.00 29.78 ? 350 HIS B N     1 
ATOM   11908 C CA    . HIS D  1 350 ? -30.910 41.807  -50.963 1.00 29.39 ? 350 HIS B CA    1 
ATOM   11909 C C     . HIS D  1 350 ? -31.574 40.652  -51.680 1.00 34.20 ? 350 HIS B C     1 
ATOM   11910 O O     . HIS D  1 350 ? -30.913 39.843  -52.341 1.00 37.49 ? 350 HIS B O     1 
ATOM   11911 C CB    . HIS D  1 350 ? -30.926 41.591  -49.463 1.00 32.05 ? 350 HIS B CB    1 
ATOM   11912 C CG    . HIS D  1 350 ? -30.319 40.297  -49.031 1.00 33.95 ? 350 HIS B CG    1 
ATOM   11913 N ND1   . HIS D  1 350 ? -28.959 40.085  -49.007 1.00 37.42 ? 350 HIS B ND1   1 
ATOM   11914 C CD2   . HIS D  1 350 ? -30.885 39.157  -48.579 1.00 32.95 ? 350 HIS B CD2   1 
ATOM   11915 C CE1   . HIS D  1 350 ? -28.713 38.870  -48.552 1.00 32.89 ? 350 HIS B CE1   1 
ATOM   11916 N NE2   . HIS D  1 350 ? -29.865 38.286  -48.286 1.00 35.75 ? 350 HIS B NE2   1 
ATOM   11917 N N     . THR D  1 351 ? -32.904 40.603  -51.604 1.00 39.36 ? 351 THR B N     1 
ATOM   11918 C CA    . THR D  1 351 ? -33.656 39.499  -52.192 1.00 40.55 ? 351 THR B CA    1 
ATOM   11919 C C     . THR D  1 351 ? -33.442 39.445  -53.702 1.00 37.90 ? 351 THR B C     1 
ATOM   11920 O O     . THR D  1 351 ? -33.120 38.390  -54.260 1.00 37.56 ? 351 THR B O     1 
ATOM   11921 C CB    . THR D  1 351 ? -35.147 39.639  -51.826 1.00 39.80 ? 351 THR B CB    1 
ATOM   11922 O OG1   . THR D  1 351 ? -35.273 40.119  -50.481 1.00 34.68 ? 351 THR B OG1   1 
ATOM   11923 C CG2   . THR D  1 351 ? -35.880 38.300  -51.903 1.00 41.42 ? 351 THR B CG2   1 
ATOM   11924 N N     . VAL D  1 352 ? -33.555 40.588  -54.371 1.00 36.67 ? 352 VAL B N     1 
ATOM   11925 C CA    . VAL D  1 352 ? -33.377 40.614  -55.822 1.00 40.35 ? 352 VAL B CA    1 
ATOM   11926 C C     . VAL D  1 352 ? -31.971 40.139  -56.204 1.00 39.24 ? 352 VAL B C     1 
ATOM   11927 O O     . VAL D  1 352 ? -31.806 39.275  -57.077 1.00 36.10 ? 352 VAL B O     1 
ATOM   11928 C CB    . VAL D  1 352 ? -33.686 42.022  -56.362 1.00 39.29 ? 352 VAL B CB    1 
ATOM   11929 C CG1   . VAL D  1 352 ? -33.118 42.194  -57.735 1.00 36.78 ? 352 VAL B CG1   1 
ATOM   11930 C CG2   . VAL D  1 352 ? -35.205 42.244  -56.388 1.00 37.98 ? 352 VAL B CG2   1 
ATOM   11931 N N     . ALA D  1 353 ? -30.941 40.678  -55.542 1.00 34.27 ? 353 ALA B N     1 
ATOM   11932 C CA    . ALA D  1 353 ? -29.570 40.259  -55.821 1.00 34.22 ? 353 ALA B CA    1 
ATOM   11933 C C     . ALA D  1 353 ? -29.406 38.750  -55.672 1.00 35.21 ? 353 ALA B C     1 
ATOM   11934 O O     . ALA D  1 353 ? -28.953 38.064  -56.589 1.00 35.40 ? 353 ALA B O     1 
ATOM   11935 C CB    . ALA D  1 353 ? -28.602 40.994  -54.899 1.00 34.04 ? 353 ALA B CB    1 
ATOM   11936 N N     . GLU D  1 354 ? -29.768 38.218  -54.510 1.00 36.96 ? 354 GLU B N     1 
ATOM   11937 C CA    . GLU D  1 354 ? -29.626 36.783  -54.294 1.00 40.04 ? 354 GLU B CA    1 
ATOM   11938 C C     . GLU D  1 354 ? -30.369 35.977  -55.353 1.00 40.24 ? 354 GLU B C     1 
ATOM   11939 O O     . GLU D  1 354 ? -29.853 34.970  -55.858 1.00 40.95 ? 354 GLU B O     1 
ATOM   11940 C CB    . GLU D  1 354 ? -30.135 36.405  -52.908 1.00 44.24 ? 354 GLU B CB    1 
ATOM   11941 C CG    . GLU D  1 354 ? -29.337 36.964  -51.764 1.00 43.55 ? 354 GLU B CG    1 
ATOM   11942 C CD    . GLU D  1 354 ? -29.102 35.923  -50.659 1.00 51.77 ? 354 GLU B CD    1 
ATOM   11943 O OE1   . GLU D  1 354 ? -30.083 35.229  -50.282 1.00 44.04 ? 354 GLU B OE1   1 
ATOM   11944 O OE2   . GLU D  1 354 ? -27.936 35.797  -50.186 1.00 51.83 ? 354 GLU B OE2   1 
ATOM   11945 N N     . ARG D  1 355 ? -31.587 36.395  -55.692 1.00 31.84 ? 355 ARG B N     1 
ATOM   11946 C CA    . ARG D  1 355 ? -32.358 35.638  -56.662 1.00 31.74 ? 355 ARG B CA    1 
ATOM   11947 C C     . ARG D  1 355 ? -31.759 35.763  -58.053 1.00 39.65 ? 355 ARG B C     1 
ATOM   11948 O O     . ARG D  1 355 ? -31.840 34.821  -58.852 1.00 39.58 ? 355 ARG B O     1 
ATOM   11949 C CB    . ARG D  1 355 ? -33.811 36.108  -56.664 1.00 31.83 ? 355 ARG B CB    1 
ATOM   11950 C CG    . ARG D  1 355 ? -34.628 35.639  -55.478 1.00 32.09 ? 355 ARG B CG    1 
ATOM   11951 C CD    . ARG D  1 355 ? -36.122 35.929  -55.654 1.00 34.87 ? 355 ARG B CD    1 
ATOM   11952 N NE    . ARG D  1 355 ? -36.853 34.797  -56.214 1.00 36.06 ? 355 ARG B NE    1 
ATOM   11953 C CZ    . ARG D  1 355 ? -38.157 34.793  -56.456 1.00 38.51 ? 355 ARG B CZ    1 
ATOM   11954 N NH1   . ARG D  1 355 ? -38.919 35.838  -56.167 1.00 36.70 ? 355 ARG B NH1   1 
ATOM   11955 N NH2   . ARG D  1 355 ? -38.710 33.719  -57.013 1.00 40.49 ? 355 ARG B NH2   1 
ATOM   11956 N N     . LEU D  1 356 ? -31.138 36.904  -58.349 1.00 37.45 ? 356 LEU B N     1 
ATOM   11957 C CA    . LEU D  1 356 ? -30.575 37.147  -59.666 1.00 35.69 ? 356 LEU B CA    1 
ATOM   11958 C C     . LEU D  1 356 ? -29.098 36.760  -59.753 1.00 36.79 ? 356 LEU B C     1 
ATOM   11959 O O     . LEU D  1 356 ? -28.649 36.250  -60.786 1.00 39.31 ? 356 LEU B O     1 
ATOM   11960 C CB    . LEU D  1 356 ? -30.771 38.618  -60.033 1.00 36.05 ? 356 LEU B CB    1 
ATOM   11961 C CG    . LEU D  1 356 ? -32.216 39.015  -60.358 1.00 36.88 ? 356 LEU B CG    1 
ATOM   11962 C CD1   . LEU D  1 356 ? -32.275 40.330  -61.110 1.00 31.92 ? 356 LEU B CD1   1 
ATOM   11963 C CD2   . LEU D  1 356 ? -32.910 37.940  -61.142 1.00 28.44 ? 356 LEU B CD2   1 
ATOM   11964 N N     . LEU D  1 357 ? -28.333 36.969  -58.684 1.00 37.38 ? 357 LEU B N     1 
ATOM   11965 C CA    . LEU D  1 357 ? -26.903 36.690  -58.705 1.00 34.81 ? 357 LEU B CA    1 
ATOM   11966 C C     . LEU D  1 357 ? -26.482 35.586  -57.742 1.00 41.20 ? 357 LEU B C     1 
ATOM   11967 O O     . LEU D  1 357 ? -25.280 35.455  -57.468 1.00 46.04 ? 357 LEU B O     1 
ATOM   11968 C CB    . LEU D  1 357 ? -26.115 37.955  -58.381 1.00 32.04 ? 357 LEU B CB    1 
ATOM   11969 C CG    . LEU D  1 357 ? -26.721 39.236  -58.921 1.00 34.18 ? 357 LEU B CG    1 
ATOM   11970 C CD1   . LEU D  1 357 ? -26.212 40.445  -58.122 1.00 30.23 ? 357 LEU B CD1   1 
ATOM   11971 C CD2   . LEU D  1 357 ? -26.365 39.333  -60.394 1.00 42.53 ? 357 LEU B CD2   1 
ATOM   11972 N N     . GLY D  1 358 ? -27.419 34.797  -57.212 1.00 38.33 ? 358 GLY B N     1 
ATOM   11973 C CA    . GLY D  1 358 ? -27.074 33.704  -56.331 1.00 32.95 ? 358 GLY B CA    1 
ATOM   11974 C C     . GLY D  1 358 ? -26.836 34.160  -54.911 1.00 40.43 ? 358 GLY B C     1 
ATOM   11975 O O     . GLY D  1 358 ? -26.825 35.347  -54.594 1.00 41.48 ? 358 GLY B O     1 
ATOM   11976 N N     . HIS D  1 359 ? -26.629 33.184  -54.035 1.00 45.81 ? 359 HIS B N     1 
ATOM   11977 C CA    . HIS D  1 359 ? -26.529 33.473  -52.610 1.00 48.74 ? 359 HIS B CA    1 
ATOM   11978 C C     . HIS D  1 359 ? -25.144 33.974  -52.182 1.00 45.99 ? 359 HIS B C     1 
ATOM   11979 O O     . HIS D  1 359 ? -24.831 34.006  -50.990 1.00 50.74 ? 359 HIS B O     1 
ATOM   11980 C CB    . HIS D  1 359 ? -26.933 32.235  -51.810 1.00 48.72 ? 359 HIS B CB    1 
ATOM   11981 C CG    . HIS D  1 359 ? -28.346 31.818  -52.057 1.00 52.24 ? 359 HIS B CG    1 
ATOM   11982 N ND1   . HIS D  1 359 ? -28.783 30.520  -51.909 1.00 50.29 ? 359 HIS B ND1   1 
ATOM   11983 C CD2   . HIS D  1 359 ? -29.419 32.536  -52.465 1.00 53.50 ? 359 HIS B CD2   1 
ATOM   11984 C CE1   . HIS D  1 359 ? -30.068 30.459  -52.212 1.00 56.92 ? 359 HIS B CE1   1 
ATOM   11985 N NE2   . HIS D  1 359 ? -30.479 31.670  -52.546 1.00 54.87 ? 359 HIS B NE2   1 
ATOM   11986 N N     . ASP D  1 360 ? -24.309 34.398  -53.109 1.00 39.31 ? 360 ASP B N     1 
ATOM   11987 C CA    . ASP D  1 360 ? -22.983 34.864  -52.744 1.00 40.78 ? 360 ASP B CA    1 
ATOM   11988 C C     . ASP D  1 360 ? -22.669 36.179  -53.435 1.00 41.48 ? 360 ASP B C     1 
ATOM   11989 O O     . ASP D  1 360 ? -21.511 36.610  -53.438 1.00 40.81 ? 360 ASP B O     1 
ATOM   11990 C CB    . ASP D  1 360 ? -21.940 33.801  -53.082 1.00 46.28 ? 360 ASP B CB    1 
ATOM   11991 C CG    . ASP D  1 360 ? -20.651 34.020  -52.355 1.00 49.43 ? 360 ASP B CG    1 
ATOM   11992 O OD1   . ASP D  1 360 ? -20.684 34.734  -51.332 1.00 53.86 ? 360 ASP B OD1   1 
ATOM   11993 O OD2   . ASP D  1 360 ? -19.611 33.498  -52.810 1.00 50.63 ? 360 ASP B OD2   1 
ATOM   11994 N N     . TYR D  1 361 ? -23.706 36.836  -53.976 1.00 42.77 ? 361 TYR B N     1 
ATOM   11995 C CA    . TYR D  1 361 ? -23.535 37.997  -54.848 1.00 42.64 ? 361 TYR B CA    1 
ATOM   11996 C C     . TYR D  1 361 ? -22.629 39.060  -54.248 1.00 41.19 ? 361 TYR B C     1 
ATOM   11997 O O     . TYR D  1 361 ? -22.011 39.843  -54.981 1.00 40.27 ? 361 TYR B O     1 
ATOM   11998 C CB    . TYR D  1 361 ? -24.896 38.618  -55.158 1.00 37.16 ? 361 TYR B CB    1 
ATOM   11999 C CG    . TYR D  1 361 ? -25.535 39.295  -53.969 1.00 38.20 ? 361 TYR B CG    1 
ATOM   12000 C CD1   . TYR D  1 361 ? -26.285 38.573  -53.070 1.00 38.26 ? 361 TYR B CD1   1 
ATOM   12001 C CD2   . TYR D  1 361 ? -25.394 40.660  -53.750 1.00 40.12 ? 361 TYR B CD2   1 
ATOM   12002 C CE1   . TYR D  1 361 ? -26.874 39.172  -51.992 1.00 38.54 ? 361 TYR B CE1   1 
ATOM   12003 C CE2   . TYR D  1 361 ? -25.996 41.274  -52.656 1.00 39.05 ? 361 TYR B CE2   1 
ATOM   12004 C CZ    . TYR D  1 361 ? -26.732 40.512  -51.779 1.00 36.84 ? 361 TYR B CZ    1 
ATOM   12005 O OH    . TYR D  1 361 ? -27.329 41.067  -50.671 1.00 29.70 ? 361 TYR B OH    1 
ATOM   12006 N N     . ALA D  1 362 ? -22.549 39.121  -52.924 1.00 39.91 ? 362 ALA B N     1 
ATOM   12007 C CA    . ALA D  1 362 ? -21.825 40.222  -52.309 1.00 43.73 ? 362 ALA B CA    1 
ATOM   12008 C C     . ALA D  1 362 ? -20.338 40.153  -52.618 1.00 43.18 ? 362 ALA B C     1 
ATOM   12009 O O     . ALA D  1 362 ? -19.696 41.200  -52.775 1.00 40.45 ? 362 ALA B O     1 
ATOM   12010 C CB    . ALA D  1 362 ? -22.072 40.244  -50.797 1.00 42.24 ? 362 ALA B CB    1 
ATOM   12011 N N     . ARG D  1 363 ? -19.779 38.943  -52.741 1.00 44.57 ? 363 ARG B N     1 
ATOM   12012 C CA    . ARG D  1 363 ? -18.357 38.838  -53.040 1.00 42.65 ? 363 ARG B CA    1 
ATOM   12013 C C     . ARG D  1 363 ? -18.003 39.588  -54.314 1.00 39.63 ? 363 ARG B C     1 
ATOM   12014 O O     . ARG D  1 363 ? -17.008 40.320  -54.355 1.00 40.46 ? 363 ARG B O     1 
ATOM   12015 C CB    . ARG D  1 363 ? -17.916 37.378  -53.156 1.00 48.92 ? 363 ARG B CB    1 
ATOM   12016 C CG    . ARG D  1 363 ? -16.377 37.284  -53.210 1.00 52.82 ? 363 ARG B CG    1 
ATOM   12017 C CD    . ARG D  1 363 ? -15.862 35.938  -52.793 1.00 46.39 ? 363 ARG B CD    1 
ATOM   12018 N NE    . ARG D  1 363 ? -15.613 35.086  -53.945 1.00 48.48 ? 363 ARG B NE    1 
ATOM   12019 C CZ    . ARG D  1 363 ? -16.455 34.153  -54.371 1.00 54.42 ? 363 ARG B CZ    1 
ATOM   12020 N NH1   . ARG D  1 363 ? -17.635 33.968  -53.799 1.00 50.48 ? 363 ARG B NH1   1 
ATOM   12021 N NH2   . ARG D  1 363 ? -16.106 33.389  -55.398 1.00 52.40 ? 363 ARG B NH2   1 
ATOM   12022 N N     . ASN D  1 364 ? -18.806 39.437  -55.358 1.00 41.57 ? 364 ASN B N     1 
ATOM   12023 C CA    . ASN D  1 364 ? -18.393 39.918  -56.664 1.00 43.26 ? 364 ASN B CA    1 
ATOM   12024 C C     . ASN D  1 364 ? -19.234 41.051  -57.195 1.00 36.17 ? 364 ASN B C     1 
ATOM   12025 O O     . ASN D  1 364 ? -18.903 41.605  -58.241 1.00 42.71 ? 364 ASN B O     1 
ATOM   12026 C CB    . ASN D  1 364 ? -18.410 38.767  -57.674 1.00 38.94 ? 364 ASN B CB    1 
ATOM   12027 C CG    . ASN D  1 364 ? -17.264 37.809  -57.460 1.00 47.53 ? 364 ASN B CG    1 
ATOM   12028 O OD1   . ASN D  1 364 ? -16.135 38.223  -57.175 1.00 52.83 ? 364 ASN B OD1   1 
ATOM   12029 N ND2   . ASN D  1 364 ? -17.551 36.519  -57.541 1.00 53.91 ? 364 ASN B ND2   1 
ATOM   12030 N N     . ASN D  1 365 ? -20.302 41.413  -56.522 1.00 38.54 ? 365 ASN B N     1 
ATOM   12031 C CA    . ASN D  1 365 ? -21.249 42.315  -57.129 1.00 39.89 ? 365 ASN B CA    1 
ATOM   12032 C C     . ASN D  1 365 ? -21.585 43.449  -56.184 1.00 41.78 ? 365 ASN B C     1 
ATOM   12033 O O     . ASN D  1 365 ? -21.447 43.345  -54.965 1.00 36.17 ? 365 ASN B O     1 
ATOM   12034 C CB    . ASN D  1 365 ? -22.516 41.582  -57.534 1.00 41.47 ? 365 ASN B CB    1 
ATOM   12035 C CG    . ASN D  1 365 ? -22.227 40.332  -58.312 1.00 41.21 ? 365 ASN B CG    1 
ATOM   12036 O OD1   . ASN D  1 365 ? -22.438 40.292  -59.525 1.00 41.53 ? 365 ASN B OD1   1 
ATOM   12037 N ND2   . ASN D  1 365 ? -21.744 39.292  -57.623 1.00 40.38 ? 365 ASN B ND2   1 
ATOM   12038 N N     . PHE D  1 366 ? -22.035 44.536  -56.798 1.00 44.91 ? 366 PHE B N     1 
ATOM   12039 C CA    . PHE D  1 366 ? -22.483 45.741  -56.129 1.00 43.09 ? 366 PHE B CA    1 
ATOM   12040 C C     . PHE D  1 366 ? -23.886 46.043  -56.636 1.00 43.21 ? 366 PHE B C     1 
ATOM   12041 O O     . PHE D  1 366 ? -24.213 45.718  -57.778 1.00 36.26 ? 366 PHE B O     1 
ATOM   12042 C CB    . PHE D  1 366 ? -21.521 46.913  -56.418 1.00 39.06 ? 366 PHE B CB    1 
ATOM   12043 C CG    . PHE D  1 366 ? -20.076 46.580  -56.174 1.00 44.87 ? 366 PHE B CG    1 
ATOM   12044 C CD1   . PHE D  1 366 ? -19.365 45.797  -57.067 1.00 40.42 ? 366 PHE B CD1   1 
ATOM   12045 C CD2   . PHE D  1 366 ? -19.430 47.034  -55.034 1.00 48.72 ? 366 PHE B CD2   1 
ATOM   12046 C CE1   . PHE D  1 366 ? -18.042 45.482  -56.835 1.00 40.60 ? 366 PHE B CE1   1 
ATOM   12047 C CE2   . PHE D  1 366 ? -18.098 46.723  -54.798 1.00 41.48 ? 366 PHE B CE2   1 
ATOM   12048 C CZ    . PHE D  1 366 ? -17.404 45.945  -55.705 1.00 37.49 ? 366 PHE B CZ    1 
ATOM   12049 N N     . PHE D  1 367 ? -24.737 46.617  -55.772 1.00 41.09 ? 367 PHE B N     1 
ATOM   12050 C CA    . PHE D  1 367 ? -26.019 47.171  -56.199 1.00 37.46 ? 367 PHE B CA    1 
ATOM   12051 C C     . PHE D  1 367 ? -26.219 48.535  -55.561 1.00 40.14 ? 367 PHE B C     1 
ATOM   12052 O O     . PHE D  1 367 ? -25.494 48.948  -54.654 1.00 38.18 ? 367 PHE B O     1 
ATOM   12053 C CB    . PHE D  1 367 ? -27.238 46.269  -55.886 1.00 32.82 ? 367 PHE B CB    1 
ATOM   12054 C CG    . PHE D  1 367 ? -27.543 46.113  -54.415 1.00 36.33 ? 367 PHE B CG    1 
ATOM   12055 C CD1   . PHE D  1 367 ? -28.403 46.985  -53.769 1.00 38.74 ? 367 PHE B CD1   1 
ATOM   12056 C CD2   . PHE D  1 367 ? -27.012 45.047  -53.690 1.00 44.14 ? 367 PHE B CD2   1 
ATOM   12057 C CE1   . PHE D  1 367 ? -28.684 46.822  -52.416 1.00 38.67 ? 367 PHE B CE1   1 
ATOM   12058 C CE2   . PHE D  1 367 ? -27.292 44.880  -52.332 1.00 37.24 ? 367 PHE B CE2   1 
ATOM   12059 C CZ    . PHE D  1 367 ? -28.124 45.767  -51.700 1.00 31.69 ? 367 PHE B CZ    1 
ATOM   12060 N N     . SER D  1 368 ? -27.235 49.223  -56.052 1.00 37.05 ? 368 SER B N     1 
ATOM   12061 C CA    . SER D  1 368 ? -27.499 50.596  -55.681 1.00 34.70 ? 368 SER B CA    1 
ATOM   12062 C C     . SER D  1 368 ? -28.838 50.971  -56.278 1.00 36.53 ? 368 SER B C     1 
ATOM   12063 O O     . SER D  1 368 ? -29.126 50.630  -57.429 1.00 36.69 ? 368 SER B O     1 
ATOM   12064 C CB    . SER D  1 368 ? -26.407 51.532  -56.199 1.00 38.29 ? 368 SER B CB    1 
ATOM   12065 O OG    . SER D  1 368 ? -26.777 52.879  -55.984 1.00 40.91 ? 368 SER B OG    1 
ATOM   12066 N N     . SER D  1 369 ? -29.648 51.644  -55.491 1.00 32.94 ? 369 SER B N     1 
ATOM   12067 C CA    . SER D  1 369 ? -31.006 51.948  -55.884 1.00 30.98 ? 369 SER B CA    1 
ATOM   12068 C C     . SER D  1 369 ? -31.099 53.397  -56.319 1.00 33.39 ? 369 SER B C     1 
ATOM   12069 O O     . SER D  1 369 ? -30.320 54.248  -55.887 1.00 34.77 ? 369 SER B O     1 
ATOM   12070 C CB    . SER D  1 369 ? -31.981 51.683  -54.739 1.00 35.00 ? 369 SER B CB    1 
ATOM   12071 O OG    . SER D  1 369 ? -31.986 52.749  -53.801 1.00 35.28 ? 369 SER B OG    1 
ATOM   12072 N N     . ILE D  1 370 ? -32.064 53.655  -57.199 1.00 35.09 ? 370 ILE B N     1 
ATOM   12073 C CA    . ILE D  1 370 ? -32.393 54.979  -57.708 1.00 39.60 ? 370 ILE B CA    1 
ATOM   12074 C C     . ILE D  1 370 ? -33.878 55.182  -57.466 1.00 41.13 ? 370 ILE B C     1 
ATOM   12075 O O     . ILE D  1 370 ? -34.710 54.542  -58.123 1.00 40.35 ? 370 ILE B O     1 
ATOM   12076 C CB    . ILE D  1 370 ? -32.092 55.140  -59.210 1.00 39.73 ? 370 ILE B CB    1 
ATOM   12077 C CG1   . ILE D  1 370 ? -30.688 54.703  -59.582 1.00 39.26 ? 370 ILE B CG1   1 
ATOM   12078 C CG2   . ILE D  1 370 ? -32.280 56.579  -59.650 1.00 38.16 ? 370 ILE B CG2   1 
ATOM   12079 C CD1   . ILE D  1 370 ? -30.409 54.929  -61.069 1.00 36.66 ? 370 ILE B CD1   1 
ATOM   12080 N N     . LEU D  1 371 ? -34.218 56.070  -56.557 1.00 40.94 ? 371 LEU B N     1 
ATOM   12081 C CA    . LEU D  1 371 ? -35.574 56.591  -56.528 1.00 42.77 ? 371 LEU B CA    1 
ATOM   12082 C C     . LEU D  1 371 ? -35.550 57.830  -57.437 1.00 49.50 ? 371 LEU B C     1 
ATOM   12083 O O     . LEU D  1 371 ? -34.600 58.016  -58.208 1.00 53.56 ? 371 LEU B O     1 
ATOM   12084 C CB    . LEU D  1 371 ? -35.977 56.831  -55.075 1.00 43.21 ? 371 LEU B CB    1 
ATOM   12085 C CG    . LEU D  1 371 ? -35.196 55.892  -54.134 1.00 38.43 ? 371 LEU B CG    1 
ATOM   12086 C CD1   . LEU D  1 371 ? -35.383 56.290  -52.672 1.00 38.40 ? 371 LEU B CD1   1 
ATOM   12087 C CD2   . LEU D  1 371 ? -35.519 54.403  -54.357 1.00 33.57 ? 371 LEU B CD2   1 
ATOM   12088 N N     . ASN D  1 372 ? -36.567 58.689  -57.405 1.00 44.06 ? 372 ASN B N     1 
ATOM   12089 C CA    . ASN D  1 372 ? -36.500 60.015  -58.034 1.00 42.69 ? 372 ASN B CA    1 
ATOM   12090 C C     . ASN D  1 372 ? -36.334 59.985  -59.552 1.00 46.96 ? 372 ASN B C     1 
ATOM   12091 O O     . ASN D  1 372 ? -36.324 61.058  -60.188 1.00 47.82 ? 372 ASN B O     1 
ATOM   12092 C CB    . ASN D  1 372 ? -35.383 60.881  -57.423 1.00 42.34 ? 372 ASN B CB    1 
ATOM   12093 C CG    . ASN D  1 372 ? -34.131 60.970  -58.293 1.00 49.20 ? 372 ASN B CG    1 
ATOM   12094 O OD1   . ASN D  1 372 ? -33.671 62.067  -58.621 1.00 58.45 ? 372 ASN B OD1   1 
ATOM   12095 N ND2   . ASN D  1 372 ? -33.576 59.822  -58.667 1.00 46.46 ? 372 ASN B ND2   1 
ATOM   12096 N N     . VAL D  1 373 ? -36.171 58.805  -60.158 1.00 44.44 ? 373 VAL B N     1 
ATOM   12097 C CA    . VAL D  1 373 ? -36.337 58.700  -61.601 1.00 43.27 ? 373 VAL B CA    1 
ATOM   12098 C C     . VAL D  1 373 ? -37.740 59.184  -61.944 1.00 42.88 ? 373 VAL B C     1 
ATOM   12099 O O     . VAL D  1 373 ? -38.685 59.014  -61.164 1.00 44.01 ? 373 VAL B O     1 
ATOM   12100 C CB    . VAL D  1 373 ? -36.106 57.258  -62.088 1.00 46.01 ? 373 VAL B CB    1 
ATOM   12101 C CG1   . VAL D  1 373 ? -36.649 57.030  -63.518 1.00 41.33 ? 373 VAL B CG1   1 
ATOM   12102 C CG2   . VAL D  1 373 ? -34.636 56.922  -62.038 1.00 44.80 ? 373 VAL B CG2   1 
ATOM   12103 N N     . VAL D  1 374 ? -37.868 59.823  -63.104 1.00 43.45 ? 374 VAL B N     1 
ATOM   12104 C CA    . VAL D  1 374 ? -39.143 60.292  -63.640 1.00 39.51 ? 374 VAL B CA    1 
ATOM   12105 C C     . VAL D  1 374 ? -40.087 59.107  -63.822 1.00 41.10 ? 374 VAL B C     1 
ATOM   12106 O O     . VAL D  1 374 ? -39.729 58.133  -64.503 1.00 41.03 ? 374 VAL B O     1 
ATOM   12107 C CB    . VAL D  1 374 ? -38.928 61.043  -64.966 1.00 39.55 ? 374 VAL B CB    1 
ATOM   12108 C CG1   . VAL D  1 374 ? -40.262 61.480  -65.579 1.00 35.63 ? 374 VAL B CG1   1 
ATOM   12109 C CG2   . VAL D  1 374 ? -37.999 62.239  -64.757 1.00 41.84 ? 374 VAL B CG2   1 
ATOM   12110 N N     . PRO D  1 375 ? -41.278 59.119  -63.219 1.00 39.46 ? 375 PRO B N     1 
ATOM   12111 C CA    . PRO D  1 375 ? -42.175 57.970  -63.362 1.00 35.57 ? 375 PRO B CA    1 
ATOM   12112 C C     . PRO D  1 375 ? -42.698 57.883  -64.779 1.00 38.46 ? 375 PRO B C     1 
ATOM   12113 O O     . PRO D  1 375 ? -43.041 58.891  -65.399 1.00 39.73 ? 375 PRO B O     1 
ATOM   12114 C CB    . PRO D  1 375 ? -43.299 58.259  -62.363 1.00 37.46 ? 375 PRO B CB    1 
ATOM   12115 C CG    . PRO D  1 375 ? -43.235 59.714  -62.114 1.00 39.04 ? 375 PRO B CG    1 
ATOM   12116 C CD    . PRO D  1 375 ? -41.809 60.133  -62.294 1.00 39.64 ? 375 PRO B CD    1 
ATOM   12117 N N     . ALA D  1 376 ? -42.726 56.668  -65.307 1.00 36.51 ? 376 ALA B N     1 
ATOM   12118 C CA    . ALA D  1 376 ? -43.292 56.453  -66.628 1.00 42.28 ? 376 ALA B CA    1 
ATOM   12119 C C     . ALA D  1 376 ? -43.884 55.063  -66.670 1.00 43.36 ? 376 ALA B C     1 
ATOM   12120 O O     . ALA D  1 376 ? -43.706 54.256  -65.749 1.00 43.94 ? 376 ALA B O     1 
ATOM   12121 C CB    . ALA D  1 376 ? -42.258 56.615  -67.748 1.00 39.99 ? 376 ALA B CB    1 
ATOM   12122 N N     . GLY D  1 377 ? -44.609 54.803  -67.748 1.00 39.10 ? 377 GLY B N     1 
ATOM   12123 C CA    . GLY D  1 377 ? -45.051 53.459  -68.025 1.00 42.51 ? 377 GLY B CA    1 
ATOM   12124 C C     . GLY D  1 377 ? -43.880 52.513  -67.924 1.00 39.53 ? 377 GLY B C     1 
ATOM   12125 O O     . GLY D  1 377 ? -42.738 52.862  -68.259 1.00 32.54 ? 377 GLY B O     1 
ATOM   12126 N N     . LEU D  1 378 ? -44.151 51.321  -67.396 1.00 40.42 ? 378 LEU B N     1 
ATOM   12127 C CA    . LEU D  1 378 ? -43.144 50.275  -67.420 1.00 37.60 ? 378 LEU B CA    1 
ATOM   12128 C C     . LEU D  1 378 ? -42.519 50.170  -68.803 1.00 35.47 ? 378 LEU B C     1 
ATOM   12129 O O     . LEU D  1 378 ? -41.304 50.314  -68.952 1.00 36.97 ? 378 LEU B O     1 
ATOM   12130 C CB    . LEU D  1 378 ? -43.751 48.944  -67.003 1.00 35.74 ? 378 LEU B CB    1 
ATOM   12131 C CG    . LEU D  1 378 ? -42.604 47.941  -66.964 1.00 39.20 ? 378 LEU B CG    1 
ATOM   12132 C CD1   . LEU D  1 378 ? -41.535 48.479  -66.027 1.00 35.68 ? 378 LEU B CD1   1 
ATOM   12133 C CD2   . LEU D  1 378 ? -43.073 46.553  -66.545 1.00 41.34 ? 378 LEU B CD2   1 
ATOM   12134 N N     . ALA D  1 379 ? -43.349 49.957  -69.832 1.00 34.48 ? 379 ALA B N     1 
ATOM   12135 C CA    . ALA D  1 379 ? -42.831 49.851  -71.197 1.00 35.92 ? 379 ALA B CA    1 
ATOM   12136 C C     . ALA D  1 379 ? -41.877 50.992  -71.510 1.00 36.14 ? 379 ALA B C     1 
ATOM   12137 O O     . ALA D  1 379 ? -40.704 50.767  -71.826 1.00 40.81 ? 379 ALA B O     1 
ATOM   12138 C CB    . ALA D  1 379 ? -43.978 49.827  -72.200 1.00 28.84 ? 379 ALA B CB    1 
ATOM   12139 N N     . ASP D  1 380 ? -42.346 52.230  -71.366 1.00 36.61 ? 380 ASP B N     1 
ATOM   12140 C CA    . ASP D  1 380 ? -41.499 53.388  -71.647 1.00 31.05 ? 380 ASP B CA    1 
ATOM   12141 C C     . ASP D  1 380 ? -40.272 53.409  -70.754 1.00 33.83 ? 380 ASP B C     1 
ATOM   12142 O O     . ASP D  1 380 ? -39.186 53.811  -71.188 1.00 37.21 ? 380 ASP B O     1 
ATOM   12143 C CB    . ASP D  1 380 ? -42.313 54.658  -71.491 1.00 31.31 ? 380 ASP B CB    1 
ATOM   12144 C CG    . ASP D  1 380 ? -43.248 54.862  -72.650 1.00 39.88 ? 380 ASP B CG    1 
ATOM   12145 O OD1   . ASP D  1 380 ? -42.867 54.471  -73.768 1.00 40.42 ? 380 ASP B OD1   1 
ATOM   12146 O OD2   . ASP D  1 380 ? -44.382 55.349  -72.445 1.00 47.31 ? 380 ASP B OD2   1 
ATOM   12147 N N     . LEU D  1 381 ? -40.419 52.980  -69.500 1.00 37.24 ? 381 LEU B N     1 
ATOM   12148 C CA    . LEU D  1 381 ? -39.245 52.822  -68.646 1.00 42.43 ? 381 LEU B CA    1 
ATOM   12149 C C     . LEU D  1 381 ? -38.231 51.887  -69.290 1.00 39.63 ? 381 LEU B C     1 
ATOM   12150 O O     . LEU D  1 381 ? -37.025 52.173  -69.332 1.00 37.68 ? 381 LEU B O     1 
ATOM   12151 C CB    . LEU D  1 381 ? -39.651 52.275  -67.272 1.00 37.45 ? 381 LEU B CB    1 
ATOM   12152 C CG    . LEU D  1 381 ? -39.476 53.216  -66.090 1.00 36.49 ? 381 LEU B CG    1 
ATOM   12153 C CD1   . LEU D  1 381 ? -38.340 54.196  -66.334 1.00 34.51 ? 381 LEU B CD1   1 
ATOM   12154 C CD2   . LEU D  1 381 ? -40.772 53.942  -65.820 1.00 42.58 ? 381 LEU B CD2   1 
ATOM   12155 N N     . LEU D  1 382 ? -38.711 50.750  -69.791 1.00 35.36 ? 382 LEU B N     1 
ATOM   12156 C CA    . LEU D  1 382 ? -37.814 49.741  -70.317 1.00 35.31 ? 382 LEU B CA    1 
ATOM   12157 C C     . LEU D  1 382 ? -37.126 50.210  -71.583 1.00 35.61 ? 382 LEU B C     1 
ATOM   12158 O O     . LEU D  1 382 ? -36.063 49.685  -71.923 1.00 34.38 ? 382 LEU B O     1 
ATOM   12159 C CB    . LEU D  1 382 ? -38.581 48.442  -70.552 1.00 33.76 ? 382 LEU B CB    1 
ATOM   12160 C CG    . LEU D  1 382 ? -38.627 47.445  -69.386 1.00 33.35 ? 382 LEU B CG    1 
ATOM   12161 C CD1   . LEU D  1 382 ? -38.667 48.125  -68.038 1.00 38.72 ? 382 LEU B CD1   1 
ATOM   12162 C CD2   . LEU D  1 382 ? -39.826 46.527  -69.514 1.00 35.05 ? 382 LEU B CD2   1 
ATOM   12163 N N     . ARG D  1 383 ? -37.688 51.196  -72.283 1.00 34.13 ? 383 ARG B N     1 
ATOM   12164 C CA    . ARG D  1 383 ? -36.938 51.782  -73.391 1.00 38.32 ? 383 ARG B CA    1 
ATOM   12165 C C     . ARG D  1 383 ? -35.794 52.624  -72.864 1.00 32.79 ? 383 ARG B C     1 
ATOM   12166 O O     . ARG D  1 383 ? -34.697 52.615  -73.429 1.00 37.74 ? 383 ARG B O     1 
ATOM   12167 C CB    . ARG D  1 383 ? -37.839 52.638  -74.287 1.00 35.60 ? 383 ARG B CB    1 
ATOM   12168 C CG    . ARG D  1 383 ? -38.748 51.873  -75.242 1.00 39.33 ? 383 ARG B CG    1 
ATOM   12169 C CD    . ARG D  1 383 ? -38.013 51.211  -76.423 1.00 37.19 ? 383 ARG B CD    1 
ATOM   12170 N NE    . ARG D  1 383 ? -36.787 51.923  -76.731 1.00 32.75 ? 383 ARG B NE    1 
ATOM   12171 C CZ    . ARG D  1 383 ? -35.649 51.337  -77.061 1.00 30.43 ? 383 ARG B CZ    1 
ATOM   12172 N NH1   . ARG D  1 383 ? -35.580 50.029  -77.272 1.00 26.16 ? 383 ARG B NH1   1 
ATOM   12173 N NH2   . ARG D  1 383 ? -34.552 52.079  -77.173 1.00 33.43 ? 383 ARG B NH2   1 
ATOM   12174 N N     . SER D  1 384 ? -36.034 53.357  -71.783 1.00 30.81 ? 384 SER B N     1 
ATOM   12175 C CA    . SER D  1 384 ? -35.000 54.245  -71.269 1.00 37.36 ? 384 SER B CA    1 
ATOM   12176 C C     . SER D  1 384 ? -33.750 53.464  -70.898 1.00 37.46 ? 384 SER B C     1 
ATOM   12177 O O     . SER D  1 384 ? -32.622 53.902  -71.179 1.00 34.92 ? 384 SER B O     1 
ATOM   12178 C CB    . SER D  1 384 ? -35.525 55.019  -70.054 1.00 41.69 ? 384 SER B CB    1 
ATOM   12179 O OG    . SER D  1 384 ? -36.423 56.056  -70.423 1.00 37.45 ? 384 SER B OG    1 
ATOM   12180 N N     . LEU D  1 385 ? -33.934 52.294  -70.272 1.00 36.97 ? 385 LEU B N     1 
ATOM   12181 C CA    . LEU D  1 385 ? -32.787 51.474  -69.909 1.00 34.49 ? 385 LEU B CA    1 
ATOM   12182 C C     . LEU D  1 385 ? -32.079 50.939  -71.151 1.00 30.67 ? 385 LEU B C     1 
ATOM   12183 O O     . LEU D  1 385 ? -30.863 51.097  -71.301 1.00 31.57 ? 385 LEU B O     1 
ATOM   12184 C CB    . LEU D  1 385 ? -33.224 50.341  -68.979 1.00 34.48 ? 385 LEU B CB    1 
ATOM   12185 C CG    . LEU D  1 385 ? -33.445 50.705  -67.491 1.00 36.12 ? 385 LEU B CG    1 
ATOM   12186 C CD1   . LEU D  1 385 ? -33.829 49.495  -66.641 1.00 35.95 ? 385 LEU B CD1   1 
ATOM   12187 C CD2   . LEU D  1 385 ? -32.248 51.396  -66.871 1.00 35.59 ? 385 LEU B CD2   1 
ATOM   12188 N N     . GLU D  1 386 ? -32.820 50.293  -72.050 1.00 32.70 ? 386 GLU B N     1 
ATOM   12189 C CA    . GLU D  1 386 ? -32.225 49.849  -73.302 1.00 30.26 ? 386 GLU B CA    1 
ATOM   12190 C C     . GLU D  1 386 ? -31.504 50.993  -73.985 1.00 26.80 ? 386 GLU B C     1 
ATOM   12191 O O     . GLU D  1 386 ? -30.372 50.836  -74.450 1.00 25.99 ? 386 GLU B O     1 
ATOM   12192 C CB    . GLU D  1 386 ? -33.306 49.266  -74.211 1.00 28.15 ? 386 GLU B CB    1 
ATOM   12193 C CG    . GLU D  1 386 ? -33.423 47.767  -74.101 1.00 27.19 ? 386 GLU B CG    1 
ATOM   12194 C CD    . GLU D  1 386 ? -34.733 47.217  -74.636 1.00 28.95 ? 386 GLU B CD    1 
ATOM   12195 O OE1   . GLU D  1 386 ? -35.028 47.361  -75.837 1.00 30.99 ? 386 GLU B OE1   1 
ATOM   12196 O OE2   . GLU D  1 386 ? -35.476 46.627  -73.842 1.00 31.30 ? 386 GLU B OE2   1 
ATOM   12197 N N     . ARG D  1 387 ? -32.126 52.167  -74.010 1.00 29.07 ? 387 ARG B N     1 
ATOM   12198 C CA    . ARG D  1 387 ? -31.519 53.309  -74.677 1.00 35.21 ? 387 ARG B CA    1 
ATOM   12199 C C     . ARG D  1 387 ? -30.178 53.694  -74.058 1.00 37.05 ? 387 ARG B C     1 
ATOM   12200 O O     . ARG D  1 387 ? -29.335 54.264  -74.756 1.00 41.89 ? 387 ARG B O     1 
ATOM   12201 C CB    . ARG D  1 387 ? -32.481 54.500  -74.654 1.00 35.55 ? 387 ARG B CB    1 
ATOM   12202 C CG    . ARG D  1 387 ? -32.216 55.550  -75.733 1.00 37.40 ? 387 ARG B CG    1 
ATOM   12203 C CD    . ARG D  1 387 ? -33.239 56.699  -75.716 1.00 34.88 ? 387 ARG B CD    1 
ATOM   12204 N NE    . ARG D  1 387 ? -34.562 56.258  -75.292 1.00 40.88 ? 387 ARG B NE    1 
ATOM   12205 C CZ    . ARG D  1 387 ? -35.274 56.834  -74.336 1.00 37.17 ? 387 ARG B CZ    1 
ATOM   12206 N NH1   . ARG D  1 387 ? -34.829 57.894  -73.695 1.00 40.48 ? 387 ARG B NH1   1 
ATOM   12207 N NH2   . ARG D  1 387 ? -36.470 56.339  -74.026 1.00 40.60 ? 387 ARG B NH2   1 
ATOM   12208 N N     . ALA D  1 388 ? -29.940 53.368  -72.785 1.00 36.69 ? 388 ALA B N     1 
ATOM   12209 C CA    . ALA D  1 388 ? -28.678 53.702  -72.128 1.00 31.53 ? 388 ALA B CA    1 
ATOM   12210 C C     . ALA D  1 388 ? -27.684 52.554  -72.070 1.00 28.84 ? 388 ALA B C     1 
ATOM   12211 O O     . ALA D  1 388 ? -26.534 52.782  -71.691 1.00 28.99 ? 388 ALA B O     1 
ATOM   12212 C CB    . ALA D  1 388 ? -28.926 54.186  -70.704 1.00 35.19 ? 388 ALA B CB    1 
ATOM   12213 N N     . GLY D  1 389 ? -28.091 51.334  -72.411 1.00 31.55 ? 389 GLY B N     1 
ATOM   12214 C CA    . GLY D  1 389 ? -27.211 50.175  -72.316 1.00 33.87 ? 389 GLY B CA    1 
ATOM   12215 C C     . GLY D  1 389 ? -27.132 49.481  -70.964 1.00 35.21 ? 389 GLY B C     1 
ATOM   12216 O O     . GLY D  1 389 ? -26.175 48.733  -70.723 1.00 29.54 ? 389 GLY B O     1 
ATOM   12217 N N     . VAL D  1 390 ? -28.107 49.680  -70.076 1.00 32.41 ? 390 VAL B N     1 
ATOM   12218 C CA    . VAL D  1 390 ? -27.934 49.259  -68.692 1.00 33.57 ? 390 VAL B CA    1 
ATOM   12219 C C     . VAL D  1 390 ? -29.171 48.524  -68.190 1.00 39.21 ? 390 VAL B C     1 
ATOM   12220 O O     . VAL D  1 390 ? -29.446 48.478  -66.984 1.00 42.85 ? 390 VAL B O     1 
ATOM   12221 C CB    . VAL D  1 390 ? -27.595 50.472  -67.805 1.00 34.51 ? 390 VAL B CB    1 
ATOM   12222 C CG1   . VAL D  1 390 ? -26.539 51.348  -68.477 1.00 34.73 ? 390 VAL B CG1   1 
ATOM   12223 C CG2   . VAL D  1 390 ? -28.827 51.304  -67.551 1.00 38.48 ? 390 VAL B CG2   1 
ATOM   12224 N N     . ARG D  1 391 ? -29.933 47.943  -69.103 1.00 33.24 ? 391 ARG B N     1 
ATOM   12225 C CA    . ARG D  1 391 ? -31.015 47.067  -68.689 1.00 32.62 ? 391 ARG B CA    1 
ATOM   12226 C C     . ARG D  1 391 ? -30.432 45.778  -68.124 1.00 37.72 ? 391 ARG B C     1 
ATOM   12227 O O     . ARG D  1 391 ? -29.369 45.320  -68.554 1.00 39.13 ? 391 ARG B O     1 
ATOM   12228 C CB    . ARG D  1 391 ? -31.932 46.772  -69.880 1.00 29.83 ? 391 ARG B CB    1 
ATOM   12229 C CG    . ARG D  1 391 ? -32.932 45.643  -69.648 1.00 36.32 ? 391 ARG B CG    1 
ATOM   12230 C CD    . ARG D  1 391 ? -34.259 45.869  -70.369 1.00 25.72 ? 391 ARG B CD    1 
ATOM   12231 N NE    . ARG D  1 391 ? -35.204 44.799  -70.076 1.00 29.55 ? 391 ARG B NE    1 
ATOM   12232 C CZ    . ARG D  1 391 ? -36.271 44.529  -70.817 1.00 34.66 ? 391 ARG B CZ    1 
ATOM   12233 N NH1   . ARG D  1 391 ? -36.534 45.222  -71.911 1.00 31.18 ? 391 ARG B NH1   1 
ATOM   12234 N NH2   . ARG D  1 391 ? -37.102 43.550  -70.443 1.00 28.72 ? 391 ARG B NH2   1 
ATOM   12235 N N     . TYR D  1 392 ? -31.120 45.195  -67.138 1.00 36.48 ? 392 TYR B N     1 
ATOM   12236 C CA    . TYR D  1 392 ? -30.614 43.937  -66.600 1.00 39.16 ? 392 TYR B CA    1 
ATOM   12237 C C     . TYR D  1 392 ? -30.397 42.896  -67.692 1.00 37.86 ? 392 TYR B C     1 
ATOM   12238 O O     . TYR D  1 392 ? -31.358 42.438  -68.315 1.00 43.55 ? 392 TYR B O     1 
ATOM   12239 C CB    . TYR D  1 392 ? -31.544 43.342  -65.546 1.00 32.68 ? 392 TYR B CB    1 
ATOM   12240 C CG    . TYR D  1 392 ? -30.883 42.166  -64.850 1.00 37.85 ? 392 TYR B CG    1 
ATOM   12241 C CD1   . TYR D  1 392 ? -29.730 42.346  -64.090 1.00 34.46 ? 392 TYR B CD1   1 
ATOM   12242 C CD2   . TYR D  1 392 ? -31.374 40.876  -64.988 1.00 38.84 ? 392 TYR B CD2   1 
ATOM   12243 C CE1   . TYR D  1 392 ? -29.100 41.280  -63.459 1.00 33.51 ? 392 TYR B CE1   1 
ATOM   12244 C CE2   . TYR D  1 392 ? -30.748 39.796  -64.359 1.00 41.66 ? 392 TYR B CE2   1 
ATOM   12245 C CZ    . TYR D  1 392 ? -29.610 40.007  -63.594 1.00 41.19 ? 392 TYR B CZ    1 
ATOM   12246 O OH    . TYR D  1 392 ? -28.980 38.943  -62.974 1.00 42.43 ? 392 TYR B OH    1 
ATOM   12247 N N     . ASP D  1 393 ? -29.141 42.516  -67.916 1.00 38.71 ? 393 ASP B N     1 
ATOM   12248 C CA    . ASP D  1 393 ? -28.767 41.403  -68.788 1.00 41.17 ? 393 ASP B CA    1 
ATOM   12249 C C     . ASP D  1 393 ? -28.234 40.254  -67.927 1.00 43.08 ? 393 ASP B C     1 
ATOM   12250 O O     . ASP D  1 393 ? -27.266 40.436  -67.176 1.00 46.55 ? 393 ASP B O     1 
ATOM   12251 C CB    . ASP D  1 393 ? -27.720 41.863  -69.808 1.00 45.72 ? 393 ASP B CB    1 
ATOM   12252 C CG    . ASP D  1 393 ? -26.903 40.706  -70.393 1.00 52.55 ? 393 ASP B CG    1 
ATOM   12253 O OD1   . ASP D  1 393 ? -27.336 40.134  -71.421 1.00 46.63 ? 393 ASP B OD1   1 
ATOM   12254 O OD2   . ASP D  1 393 ? -25.824 40.381  -69.827 1.00 52.32 ? 393 ASP B OD2   1 
ATOM   12255 N N     . LYS D  1 394 ? -28.855 39.072  -68.034 1.00 39.90 ? 394 LYS B N     1 
ATOM   12256 C CA    . LYS D  1 394 ? -28.493 37.975  -67.132 1.00 45.33 ? 394 LYS B CA    1 
ATOM   12257 C C     . LYS D  1 394 ? -27.119 37.389  -67.467 1.00 49.70 ? 394 LYS B C     1 
ATOM   12258 O O     . LYS D  1 394 ? -26.450 36.827  -66.587 1.00 50.81 ? 394 LYS B O     1 
ATOM   12259 C CB    . LYS D  1 394 ? -29.573 36.877  -67.159 1.00 45.04 ? 394 LYS B CB    1 
ATOM   12260 C CG    . LYS D  1 394 ? -29.454 35.777  -66.057 1.00 51.37 ? 394 LYS B CG    1 
ATOM   12261 C CD    . LYS D  1 394 ? -28.464 34.640  -66.424 1.00 47.96 ? 394 LYS B CD    1 
ATOM   12262 C CE    . LYS D  1 394 ? -28.491 33.477  -65.436 1.00 52.64 ? 394 LYS B CE    1 
ATOM   12263 N NZ    . LYS D  1 394 ? -29.539 32.478  -65.788 1.00 57.32 ? 394 LYS B NZ    1 
ATOM   12264 N N     . ASP D  1 395 ? -26.693 37.484  -68.726 1.00 47.88 ? 395 ASP B N     1 
ATOM   12265 C CA    . ASP D  1 395 ? -25.358 37.024  -69.086 1.00 46.22 ? 395 ASP B CA    1 
ATOM   12266 C C     . ASP D  1 395 ? -24.312 37.702  -68.211 1.00 47.29 ? 395 ASP B C     1 
ATOM   12267 O O     . ASP D  1 395 ? -23.624 37.048  -67.418 1.00 54.81 ? 395 ASP B O     1 
ATOM   12268 C CB    . ASP D  1 395 ? -25.092 37.298  -70.570 1.00 54.14 ? 395 ASP B CB    1 
ATOM   12269 C CG    . ASP D  1 395 ? -25.636 36.202  -71.483 1.00 56.84 ? 395 ASP B CG    1 
ATOM   12270 O OD1   . ASP D  1 395 ? -26.361 35.312  -70.986 1.00 47.65 ? 395 ASP B OD1   1 
ATOM   12271 O OD2   . ASP D  1 395 ? -25.339 36.233  -72.702 1.00 63.75 ? 395 ASP B OD2   1 
ATOM   12272 N N     . SER D  1 396 ? -24.216 39.033  -68.313 1.00 50.23 ? 396 SER B N     1 
ATOM   12273 C CA    . SER D  1 396 ? -23.294 39.803  -67.487 1.00 43.96 ? 396 SER B CA    1 
ATOM   12274 C C     . SER D  1 396 ? -23.725 39.867  -66.034 1.00 42.64 ? 396 SER B C     1 
ATOM   12275 O O     . SER D  1 396 ? -22.898 40.183  -65.172 1.00 42.52 ? 396 SER B O     1 
ATOM   12276 C CB    . SER D  1 396 ? -23.169 41.226  -68.020 1.00 41.91 ? 396 SER B CB    1 
ATOM   12277 O OG    . SER D  1 396 ? -24.443 41.790  -68.216 1.00 44.80 ? 396 SER B OG    1 
ATOM   12278 N N     . GLY D  1 397 ? -24.988 39.564  -65.743 1.00 45.90 ? 397 GLY B N     1 
ATOM   12279 C CA    . GLY D  1 397 ? -25.533 39.848  -64.429 1.00 43.10 ? 397 GLY B CA    1 
ATOM   12280 C C     . GLY D  1 397 ? -25.438 41.313  -64.080 1.00 44.57 ? 397 GLY B C     1 
ATOM   12281 O O     . GLY D  1 397 ? -25.287 41.654  -62.899 1.00 39.42 ? 397 GLY B O     1 
ATOM   12282 N N     . GLU D  1 398 ? -25.499 42.196  -65.087 1.00 39.22 ? 398 GLU B N     1 
ATOM   12283 C CA    . GLU D  1 398 ? -25.281 43.626  -64.902 1.00 39.96 ? 398 GLU B CA    1 
ATOM   12284 C C     . GLU D  1 398 ? -26.404 44.427  -65.545 1.00 41.70 ? 398 GLU B C     1 
ATOM   12285 O O     . GLU D  1 398 ? -26.769 44.178  -66.699 1.00 42.58 ? 398 GLU B O     1 
ATOM   12286 C CB    . GLU D  1 398 ? -23.944 44.059  -65.499 1.00 43.18 ? 398 GLU B CB    1 
ATOM   12287 C CG    . GLU D  1 398 ? -22.756 43.452  -64.815 1.00 44.13 ? 398 GLU B CG    1 
ATOM   12288 C CD    . GLU D  1 398 ? -21.478 44.143  -65.198 1.00 43.79 ? 398 GLU B CD    1 
ATOM   12289 O OE1   . GLU D  1 398 ? -21.457 44.853  -66.230 1.00 46.65 ? 398 GLU B OE1   1 
ATOM   12290 O OE2   . GLU D  1 398 ? -20.481 43.967  -64.470 1.00 43.13 ? 398 GLU B OE2   1 
ATOM   12291 N N     . GLY D  1 399 ? -26.922 45.414  -64.806 1.00 42.14 ? 399 GLY B N     1 
ATOM   12292 C CA    . GLY D  1 399 ? -27.974 46.281  -65.295 1.00 37.65 ? 399 GLY B CA    1 
ATOM   12293 C C     . GLY D  1 399 ? -29.033 46.612  -64.262 1.00 35.54 ? 399 GLY B C     1 
ATOM   12294 O O     . GLY D  1 399 ? -29.061 46.034  -63.170 1.00 36.24 ? 399 GLY B O     1 
ATOM   12295 N N     . ALA D  1 400 ? -29.923 47.535  -64.604 1.00 34.12 ? 400 ALA B N     1 
ATOM   12296 C CA    . ALA D  1 400 ? -30.960 47.998  -63.695 1.00 32.98 ? 400 ALA B CA    1 
ATOM   12297 C C     . ALA D  1 400 ? -32.274 47.266  -63.942 1.00 35.32 ? 400 ALA B C     1 
ATOM   12298 O O     . ALA D  1 400 ? -32.630 46.968  -65.087 1.00 37.08 ? 400 ALA B O     1 
ATOM   12299 C CB    . ALA D  1 400 ? -31.174 49.508  -63.837 1.00 33.64 ? 400 ALA B CB    1 
ATOM   12300 N N     . VAL D  1 401 ? -32.987 46.972  -62.855 1.00 37.08 ? 401 VAL B N     1 
ATOM   12301 C CA    . VAL D  1 401 ? -34.349 46.463  -62.914 1.00 37.30 ? 401 VAL B CA    1 
ATOM   12302 C C     . VAL D  1 401 ? -35.252 47.448  -62.192 1.00 39.12 ? 401 VAL B C     1 
ATOM   12303 O O     . VAL D  1 401 ? -34.807 48.276  -61.389 1.00 42.72 ? 401 VAL B O     1 
ATOM   12304 C CB    . VAL D  1 401 ? -34.509 45.064  -62.293 1.00 42.28 ? 401 VAL B CB    1 
ATOM   12305 C CG1   . VAL D  1 401 ? -33.571 44.073  -62.956 1.00 33.34 ? 401 VAL B CG1   1 
ATOM   12306 C CG2   . VAL D  1 401 ? -34.332 45.132  -60.764 1.00 33.56 ? 401 VAL B CG2   1 
ATOM   12307 N N     . VAL D  1 402 ? -36.544 47.315  -62.454 1.00 38.01 ? 402 VAL B N     1 
ATOM   12308 C CA    . VAL D  1 402 ? -37.539 48.256  -61.966 1.00 41.60 ? 402 VAL B CA    1 
ATOM   12309 C C     . VAL D  1 402 ? -38.304 47.616  -60.817 1.00 37.57 ? 402 VAL B C     1 
ATOM   12310 O O     . VAL D  1 402 ? -38.904 46.542  -60.963 1.00 37.03 ? 402 VAL B O     1 
ATOM   12311 C CB    . VAL D  1 402 ? -38.477 48.705  -63.095 1.00 41.01 ? 402 VAL B CB    1 
ATOM   12312 C CG1   . VAL D  1 402 ? -37.645 49.263  -64.241 1.00 39.76 ? 402 VAL B CG1   1 
ATOM   12313 C CG2   . VAL D  1 402 ? -39.302 47.549  -63.595 1.00 43.37 ? 402 VAL B CG2   1 
ATOM   12314 N N     . LEU D  1 403 ? -38.255 48.267  -59.662 1.00 36.56 ? 403 LEU B N     1 
ATOM   12315 C CA    . LEU D  1 403 ? -39.064 47.843  -58.535 1.00 34.53 ? 403 LEU B CA    1 
ATOM   12316 C C     . LEU D  1 403 ? -40.369 48.610  -58.449 1.00 31.17 ? 403 LEU B C     1 
ATOM   12317 O O     . LEU D  1 403 ? -41.361 48.064  -57.964 1.00 34.36 ? 403 LEU B O     1 
ATOM   12318 C CB    . LEU D  1 403 ? -38.269 47.983  -57.247 1.00 30.48 ? 403 LEU B CB    1 
ATOM   12319 C CG    . LEU D  1 403 ? -37.671 46.611  -56.973 1.00 37.57 ? 403 LEU B CG    1 
ATOM   12320 C CD1   . LEU D  1 403 ? -36.589 46.263  -57.993 1.00 33.50 ? 403 LEU B CD1   1 
ATOM   12321 C CD2   . LEU D  1 403 ? -37.155 46.538  -55.551 1.00 40.21 ? 403 LEU B CD2   1 
ATOM   12322 N N     . GLY D  1 404 ? -40.400 49.846  -58.937 1.00 34.75 ? 404 GLY B N     1 
ATOM   12323 C CA    . GLY D  1 404 ? -41.652 50.570  -59.043 1.00 39.11 ? 404 GLY B CA    1 
ATOM   12324 C C     . GLY D  1 404 ? -41.671 51.648  -60.110 1.00 40.56 ? 404 GLY B C     1 
ATOM   12325 O O     . GLY D  1 404 ? -40.690 52.374  -60.278 1.00 36.20 ? 404 GLY B O     1 
ATOM   12326 N N     . CYS D  1 405 ? -42.787 51.784  -60.827 1.00 41.73 ? 405 CYS B N     1 
ATOM   12327 C CA    . CYS D  1 405 ? -42.844 52.774  -61.894 1.00 37.34 ? 405 CYS B CA    1 
ATOM   12328 C C     . CYS D  1 405 ? -43.196 54.167  -61.397 1.00 47.41 ? 405 CYS B C     1 
ATOM   12329 O O     . CYS D  1 405 ? -42.837 55.150  -62.053 1.00 46.54 ? 405 CYS B O     1 
ATOM   12330 C CB    . CYS D  1 405 ? -43.857 52.365  -62.959 1.00 41.67 ? 405 CYS B CB    1 
ATOM   12331 S SG    . CYS D  1 405 ? -43.376 50.997  -63.992 1.00 49.66 ? 405 CYS B SG    1 
ATOM   12332 N N     . ASN D  1 406 ? -43.939 54.281  -60.273 1.00 47.86 ? 406 ASN B N     1 
ATOM   12333 C CA    . ASN D  1 406 ? -44.436 55.586  -59.796 1.00 43.96 ? 406 ASN B CA    1 
ATOM   12334 C C     . ASN D  1 406 ? -44.619 55.525  -58.277 1.00 43.68 ? 406 ASN B C     1 
ATOM   12335 O O     . ASN D  1 406 ? -45.734 55.438  -57.747 1.00 46.22 ? 406 ASN B O     1 
ATOM   12336 C CB    . ASN D  1 406 ? -45.748 55.980  -60.469 1.00 44.18 ? 406 ASN B CB    1 
ATOM   12337 C CG    . ASN D  1 406 ? -46.164 57.387  -60.129 1.00 48.21 ? 406 ASN B CG    1 
ATOM   12338 O OD1   . ASN D  1 406 ? -45.341 58.206  -59.694 1.00 44.65 ? 406 ASN B OD1   1 
ATOM   12339 N ND2   . ASN D  1 406 ? -47.450 57.683  -60.314 1.00 40.79 ? 406 ASN B ND2   1 
ATOM   12340 N N     . SER D  1 407 ? -43.509 55.577  -57.564 1.00 42.49 ? 407 SER B N     1 
ATOM   12341 C CA    . SER D  1 407 ? -43.506 55.296  -56.138 1.00 46.64 ? 407 SER B CA    1 
ATOM   12342 C C     . SER D  1 407 ? -43.426 56.586  -55.334 1.00 44.25 ? 407 SER B C     1 
ATOM   12343 O O     . SER D  1 407 ? -42.671 57.503  -55.677 1.00 42.02 ? 407 SER B O     1 
ATOM   12344 C CB    . SER D  1 407 ? -42.337 54.382  -55.772 1.00 41.76 ? 407 SER B CB    1 
ATOM   12345 O OG    . SER D  1 407 ? -42.179 54.349  -54.372 1.00 47.85 ? 407 SER B OG    1 
ATOM   12346 N N     . ASP D  1 408 ? -44.217 56.652  -54.261 1.00 43.06 ? 408 ASP B N     1 
ATOM   12347 C CA    . ASP D  1 408 ? -44.085 57.780  -53.346 1.00 47.74 ? 408 ASP B CA    1 
ATOM   12348 C C     . ASP D  1 408 ? -42.811 57.665  -52.537 1.00 43.28 ? 408 ASP B C     1 
ATOM   12349 O O     . ASP D  1 408 ? -42.216 58.686  -52.175 1.00 40.47 ? 408 ASP B O     1 
ATOM   12350 C CB    . ASP D  1 408 ? -45.299 57.878  -52.423 1.00 48.95 ? 408 ASP B CB    1 
ATOM   12351 C CG    . ASP D  1 408 ? -46.565 58.242  -53.167 1.00 53.72 ? 408 ASP B CG    1 
ATOM   12352 O OD1   . ASP D  1 408 ? -46.470 58.789  -54.290 1.00 47.90 ? 408 ASP B OD1   1 
ATOM   12353 O OD2   . ASP D  1 408 ? -47.660 57.970  -52.630 1.00 59.56 ? 408 ASP B OD2   1 
ATOM   12354 N N     . LEU D  1 409 ? -42.388 56.436  -52.254 1.00 38.63 ? 409 LEU B N     1 
ATOM   12355 C CA    . LEU D  1 409 ? -41.077 56.173  -51.677 1.00 44.05 ? 409 LEU B CA    1 
ATOM   12356 C C     . LEU D  1 409 ? -39.983 56.833  -52.491 1.00 44.80 ? 409 LEU B C     1 
ATOM   12357 O O     . LEU D  1 409 ? -39.852 56.545  -53.683 1.00 53.02 ? 409 LEU B O     1 
ATOM   12358 C CB    . LEU D  1 409 ? -40.849 54.669  -51.639 1.00 43.78 ? 409 LEU B CB    1 
ATOM   12359 C CG    . LEU D  1 409 ? -39.516 54.258  -51.061 1.00 41.13 ? 409 LEU B CG    1 
ATOM   12360 C CD1   . LEU D  1 409 ? -39.592 54.490  -49.565 1.00 52.75 ? 409 LEU B CD1   1 
ATOM   12361 C CD2   . LEU D  1 409 ? -39.283 52.803  -51.392 1.00 38.01 ? 409 LEU B CD2   1 
ATOM   12362 N N     . GLY D  1 410 ? -39.174 57.682  -51.845 1.00 44.81 ? 410 GLY B N     1 
ATOM   12363 C CA    . GLY D  1 410 ? -38.261 58.559  -52.552 1.00 44.80 ? 410 GLY B CA    1 
ATOM   12364 C C     . GLY D  1 410 ? -38.874 58.981  -53.863 1.00 46.93 ? 410 GLY B C     1 
ATOM   12365 O O     . GLY D  1 410 ? -38.599 58.392  -54.920 1.00 57.49 ? 410 GLY B O     1 
ATOM   12366 N N     . PRO D  1 411 ? -39.718 60.021  -53.838 1.00 45.96 ? 411 PRO B N     1 
ATOM   12367 C CA    . PRO D  1 411 ? -40.781 60.131  -54.862 1.00 40.49 ? 411 PRO B CA    1 
ATOM   12368 C C     . PRO D  1 411 ? -40.211 60.063  -56.266 1.00 39.55 ? 411 PRO B C     1 
ATOM   12369 O O     . PRO D  1 411 ? -39.325 60.845  -56.625 1.00 41.59 ? 411 PRO B O     1 
ATOM   12370 C CB    . PRO D  1 411 ? -41.426 61.495  -54.575 1.00 33.93 ? 411 PRO B CB    1 
ATOM   12371 C CG    . PRO D  1 411 ? -40.508 62.189  -53.628 1.00 42.00 ? 411 PRO B CG    1 
ATOM   12372 C CD    . PRO D  1 411 ? -39.356 61.313  -53.253 1.00 37.53 ? 411 PRO B CD    1 
ATOM   12373 N N     . GLY D  1 412 ? -40.656 59.081  -57.030 1.00 38.62 ? 412 GLY B N     1 
ATOM   12374 C CA    . GLY D  1 412 ? -40.125 58.846  -58.359 1.00 37.68 ? 412 GLY B CA    1 
ATOM   12375 C C     . GLY D  1 412 ? -40.272 57.388  -58.738 1.00 40.41 ? 412 GLY B C     1 
ATOM   12376 O O     . GLY D  1 412 ? -40.840 56.582  -58.002 1.00 39.14 ? 412 GLY B O     1 
ATOM   12377 N N     . ALA D  1 413 ? -39.758 57.068  -59.916 1.00 40.76 ? 413 ALA B N     1 
ATOM   12378 C CA    . ALA D  1 413 ? -39.679 55.681  -60.337 1.00 37.34 ? 413 ALA B CA    1 
ATOM   12379 C C     . ALA D  1 413 ? -38.464 55.033  -59.698 1.00 39.48 ? 413 ALA B C     1 
ATOM   12380 O O     . ALA D  1 413 ? -37.422 55.668  -59.527 1.00 45.32 ? 413 ALA B O     1 
ATOM   12381 C CB    . ALA D  1 413 ? -39.587 55.570  -61.857 1.00 36.22 ? 413 ALA B CB    1 
ATOM   12382 N N     . GLU D  1 414 ? -38.599 53.755  -59.349 1.00 38.93 ? 414 GLU B N     1 
ATOM   12383 C CA    . GLU D  1 414 ? -37.597 53.043  -58.562 1.00 38.43 ? 414 GLU B CA    1 
ATOM   12384 C C     . GLU D  1 414 ? -36.933 51.967  -59.411 1.00 35.50 ? 414 GLU B C     1 
ATOM   12385 O O     . GLU D  1 414 ? -37.581 50.985  -59.794 1.00 36.73 ? 414 GLU B O     1 
ATOM   12386 C CB    . GLU D  1 414 ? -38.220 52.419  -57.314 1.00 35.06 ? 414 GLU B CB    1 
ATOM   12387 C CG    . GLU D  1 414 ? -37.179 51.928  -56.324 1.00 36.80 ? 414 GLU B CG    1 
ATOM   12388 C CD    . GLU D  1 414 ? -37.783 51.217  -55.126 1.00 38.53 ? 414 GLU B CD    1 
ATOM   12389 O OE1   . GLU D  1 414 ? -38.689 50.382  -55.312 1.00 40.59 ? 414 GLU B OE1   1 
ATOM   12390 O OE2   . GLU D  1 414 ? -37.352 51.503  -53.995 1.00 31.88 ? 414 GLU B OE2   1 
ATOM   12391 N N     . LEU D  1 415 ? -35.641 52.143  -59.680 1.00 37.24 ? 415 LEU B N     1 
ATOM   12392 C CA    . LEU D  1 415 ? -34.806 51.124  -60.297 1.00 35.84 ? 415 LEU B CA    1 
ATOM   12393 C C     . LEU D  1 415 ? -33.799 50.612  -59.292 1.00 29.30 ? 415 LEU B C     1 
ATOM   12394 O O     . LEU D  1 415 ? -33.385 51.334  -58.387 1.00 34.54 ? 415 LEU B O     1 
ATOM   12395 C CB    . LEU D  1 415 ? -34.006 51.653  -61.474 1.00 35.47 ? 415 LEU B CB    1 
ATOM   12396 C CG    . LEU D  1 415 ? -34.658 52.751  -62.256 1.00 37.50 ? 415 LEU B CG    1 
ATOM   12397 C CD1   . LEU D  1 415 ? -33.577 53.348  -63.127 1.00 31.29 ? 415 LEU B CD1   1 
ATOM   12398 C CD2   . LEU D  1 415 ? -35.764 52.105  -63.059 1.00 41.98 ? 415 LEU B CD2   1 
ATOM   12399 N N     . LEU D  1 416 ? -33.367 49.382  -59.486 1.00 25.84 ? 416 LEU B N     1 
ATOM   12400 C CA    . LEU D  1 416 ? -32.239 48.844  -58.750 1.00 33.95 ? 416 LEU B CA    1 
ATOM   12401 C C     . LEU D  1 416 ? -31.218 48.396  -59.778 1.00 34.80 ? 416 LEU B C     1 
ATOM   12402 O O     . LEU D  1 416 ? -31.583 47.710  -60.735 1.00 36.60 ? 416 LEU B O     1 
ATOM   12403 C CB    . LEU D  1 416 ? -32.675 47.685  -57.849 1.00 30.91 ? 416 LEU B CB    1 
ATOM   12404 C CG    . LEU D  1 416 ? -31.624 46.994  -56.989 1.00 30.88 ? 416 LEU B CG    1 
ATOM   12405 C CD1   . LEU D  1 416 ? -31.213 47.868  -55.791 1.00 35.25 ? 416 LEU B CD1   1 
ATOM   12406 C CD2   . LEU D  1 416 ? -32.172 45.660  -56.521 1.00 29.12 ? 416 LEU B CD2   1 
ATOM   12407 N N     . VAL D  1 417 ? -29.956 48.787  -59.588 1.00 33.22 ? 417 VAL B N     1 
ATOM   12408 C CA    . VAL D  1 417 ? -28.897 48.608  -60.584 1.00 37.60 ? 417 VAL B CA    1 
ATOM   12409 C C     . VAL D  1 417 ? -27.792 47.693  -60.042 1.00 36.92 ? 417 VAL B C     1 
ATOM   12410 O O     . VAL D  1 417 ? -27.295 47.893  -58.928 1.00 35.70 ? 417 VAL B O     1 
ATOM   12411 C CB    . VAL D  1 417 ? -28.308 49.967  -60.997 1.00 36.75 ? 417 VAL B CB    1 
ATOM   12412 C CG1   . VAL D  1 417 ? -27.477 49.811  -62.233 1.00 37.26 ? 417 VAL B CG1   1 
ATOM   12413 C CG2   . VAL D  1 417 ? -29.423 50.990  -61.187 1.00 31.45 ? 417 VAL B CG2   1 
ATOM   12414 N N     . PHE D  1 418 ? -27.374 46.722  -60.845 1.00 36.08 ? 418 PHE B N     1 
ATOM   12415 C CA    . PHE D  1 418 ? -26.374 45.748  -60.430 1.00 29.92 ? 418 PHE B CA    1 
ATOM   12416 C C     . PHE D  1 418 ? -25.098 45.895  -61.252 1.00 36.56 ? 418 PHE B C     1 
ATOM   12417 O O     . PHE D  1 418 ? -25.154 46.199  -62.445 1.00 39.26 ? 418 PHE B O     1 
ATOM   12418 C CB    . PHE D  1 418 ? -26.922 44.339  -60.590 1.00 28.66 ? 418 PHE B CB    1 
ATOM   12419 C CG    . PHE D  1 418 ? -27.975 43.992  -59.595 1.00 34.20 ? 418 PHE B CG    1 
ATOM   12420 C CD1   . PHE D  1 418 ? -27.632 43.604  -58.313 1.00 33.74 ? 418 PHE B CD1   1 
ATOM   12421 C CD2   . PHE D  1 418 ? -29.303 44.064  -59.926 1.00 33.17 ? 418 PHE B CD2   1 
ATOM   12422 C CE1   . PHE D  1 418 ? -28.585 43.292  -57.397 1.00 29.70 ? 418 PHE B CE1   1 
ATOM   12423 C CE2   . PHE D  1 418 ? -30.268 43.734  -59.001 1.00 35.37 ? 418 PHE B CE2   1 
ATOM   12424 C CZ    . PHE D  1 418 ? -29.901 43.344  -57.734 1.00 34.28 ? 418 PHE B CZ    1 
ATOM   12425 N N     . SER D  1 419 ? -23.945 45.665  -60.621 1.00 39.28 ? 419 SER B N     1 
ATOM   12426 C CA    . SER D  1 419 ? -22.670 45.702  -61.329 1.00 38.26 ? 419 SER B CA    1 
ATOM   12427 C C     . SER D  1 419 ? -21.631 44.869  -60.599 1.00 40.23 ? 419 SER B C     1 
ATOM   12428 O O     . SER D  1 419 ? -21.671 44.720  -59.373 1.00 42.43 ? 419 SER B O     1 
ATOM   12429 C CB    . SER D  1 419 ? -22.131 47.126  -61.489 1.00 42.59 ? 419 SER B CB    1 
ATOM   12430 O OG    . SER D  1 419 ? -20.892 47.132  -62.191 1.00 39.84 ? 419 SER B OG    1 
ATOM   12431 N N     . LYS D  1 420 ? -20.692 44.336  -61.373 1.00 39.53 ? 420 LYS B N     1 
ATOM   12432 C CA    . LYS D  1 420 ? -19.524 43.664  -60.832 1.00 40.31 ? 420 LYS B CA    1 
ATOM   12433 C C     . LYS D  1 420 ? -18.398 44.627  -60.493 1.00 38.44 ? 420 LYS B C     1 
ATOM   12434 O O     . LYS D  1 420 ? -17.416 44.206  -59.875 1.00 43.11 ? 420 LYS B O     1 
ATOM   12435 C CB    . LYS D  1 420 ? -19.019 42.612  -61.824 1.00 36.76 ? 420 LYS B CB    1 
ATOM   12436 C CG    . LYS D  1 420 ? -20.092 41.638  -62.259 1.00 37.45 ? 420 LYS B CG    1 
ATOM   12437 C CD    . LYS D  1 420 ? -19.556 40.229  -62.388 1.00 37.17 ? 420 LYS B CD    1 
ATOM   12438 C CE    . LYS D  1 420 ? -20.618 39.197  -61.978 1.00 44.06 ? 420 LYS B CE    1 
ATOM   12439 N NZ    . LYS D  1 420 ? -22.037 39.682  -62.097 1.00 37.21 ? 420 LYS B NZ    1 
ATOM   12440 N N     . ASP D  1 421 ? -18.525 45.898  -60.870 1.00 39.09 ? 421 ASP B N     1 
ATOM   12441 C CA    . ASP D  1 421 ? -17.483 46.901  -60.677 1.00 42.27 ? 421 ASP B CA    1 
ATOM   12442 C C     . ASP D  1 421 ? -18.135 48.216  -60.277 1.00 49.39 ? 421 ASP B C     1 
ATOM   12443 O O     . ASP D  1 421 ? -18.946 48.767  -61.037 1.00 48.63 ? 421 ASP B O     1 
ATOM   12444 C CB    . ASP D  1 421 ? -16.653 47.091  -61.950 1.00 49.71 ? 421 ASP B CB    1 
ATOM   12445 C CG    . ASP D  1 421 ? -15.441 47.990  -61.733 1.00 52.86 ? 421 ASP B CG    1 
ATOM   12446 O OD1   . ASP D  1 421 ? -15.622 49.217  -61.512 1.00 45.09 ? 421 ASP B OD1   1 
ATOM   12447 O OD2   . ASP D  1 421 ? -14.308 47.453  -61.784 1.00 54.78 ? 421 ASP B OD2   1 
ATOM   12448 N N     . TRP D  1 422 ? -17.747 48.734  -59.104 1.00 45.74 ? 422 TRP B N     1 
ATOM   12449 C CA    . TRP D  1 422 ? -18.467 49.863  -58.525 1.00 47.17 ? 422 TRP B CA    1 
ATOM   12450 C C     . TRP D  1 422 ? -18.419 51.095  -59.421 1.00 49.12 ? 422 TRP B C     1 
ATOM   12451 O O     . TRP D  1 422 ? -19.376 51.881  -59.451 1.00 47.65 ? 422 TRP B O     1 
ATOM   12452 C CB    . TRP D  1 422 ? -17.922 50.203  -57.134 1.00 46.73 ? 422 TRP B CB    1 
ATOM   12453 C CG    . TRP D  1 422 ? -18.596 51.423  -56.593 1.00 51.57 ? 422 TRP B CG    1 
ATOM   12454 C CD1   . TRP D  1 422 ? -18.127 52.706  -56.633 1.00 48.19 ? 422 TRP B CD1   1 
ATOM   12455 C CD2   . TRP D  1 422 ? -19.905 51.493  -55.995 1.00 56.24 ? 422 TRP B CD2   1 
ATOM   12456 N NE1   . TRP D  1 422 ? -19.049 53.566  -56.074 1.00 54.78 ? 422 TRP B NE1   1 
ATOM   12457 C CE2   . TRP D  1 422 ? -20.146 52.848  -55.675 1.00 56.26 ? 422 TRP B CE2   1 
ATOM   12458 C CE3   . TRP D  1 422 ? -20.890 50.538  -55.689 1.00 54.39 ? 422 TRP B CE3   1 
ATOM   12459 C CZ2   . TRP D  1 422 ? -21.334 53.275  -55.061 1.00 59.77 ? 422 TRP B CZ2   1 
ATOM   12460 C CZ3   . TRP D  1 422 ? -22.071 50.962  -55.077 1.00 46.69 ? 422 TRP B CZ3   1 
ATOM   12461 C CH2   . TRP D  1 422 ? -22.282 52.319  -54.776 1.00 52.57 ? 422 TRP B CH2   1 
ATOM   12462 N N     . ASP D  1 423 ? -17.323 51.290  -60.155 1.00 50.63 ? 423 ASP B N     1 
ATOM   12463 C CA    . ASP D  1 423 ? -17.242 52.452  -61.033 1.00 47.61 ? 423 ASP B CA    1 
ATOM   12464 C C     . ASP D  1 423 ? -18.209 52.320  -62.202 1.00 43.90 ? 423 ASP B C     1 
ATOM   12465 O O     . ASP D  1 423 ? -18.850 53.299  -62.600 1.00 43.12 ? 423 ASP B O     1 
ATOM   12466 C CB    . ASP D  1 423 ? -15.804 52.640  -61.523 1.00 52.48 ? 423 ASP B CB    1 
ATOM   12467 C CG    . ASP D  1 423 ? -14.955 53.410  -60.529 1.00 45.49 ? 423 ASP B CG    1 
ATOM   12468 O OD1   . ASP D  1 423 ? -15.534 53.914  -59.540 1.00 39.94 ? 423 ASP B OD1   1 
ATOM   12469 O OD2   . ASP D  1 423 ? -13.722 53.512  -60.730 1.00 46.10 ? 423 ASP B OD2   1 
ATOM   12470 N N     . ARG D  1 424 ? -18.349 51.115  -62.749 1.00 44.63 ? 424 ARG B N     1 
ATOM   12471 C CA    . ARG D  1 424 ? -19.345 50.917  -63.791 1.00 47.36 ? 424 ARG B CA    1 
ATOM   12472 C C     . ARG D  1 424 ? -20.750 51.152  -63.253 1.00 49.16 ? 424 ARG B C     1 
ATOM   12473 O O     . ARG D  1 424 ? -21.633 51.611  -63.994 1.00 46.88 ? 424 ARG B O     1 
ATOM   12474 C CB    . ARG D  1 424 ? -19.207 49.515  -64.375 1.00 41.45 ? 424 ARG B CB    1 
ATOM   12475 C CG    . ARG D  1 424 ? -18.044 49.397  -65.325 1.00 48.36 ? 424 ARG B CG    1 
ATOM   12476 C CD    . ARG D  1 424 ? -18.434 48.626  -66.568 1.00 46.97 ? 424 ARG B CD    1 
ATOM   12477 N NE    . ARG D  1 424 ? -18.984 47.334  -66.188 1.00 47.81 ? 424 ARG B NE    1 
ATOM   12478 C CZ    . ARG D  1 424 ? -18.254 46.322  -65.744 1.00 46.52 ? 424 ARG B CZ    1 
ATOM   12479 N NH1   . ARG D  1 424 ? -16.940 46.415  -65.621 1.00 52.29 ? 424 ARG B NH1   1 
ATOM   12480 N NH2   . ARG D  1 424 ? -18.854 45.187  -65.419 1.00 40.75 ? 424 ARG B NH2   1 
ATOM   12481 N N     . LEU D  1 425 ? -20.972 50.853  -61.965 1.00 45.88 ? 425 LEU B N     1 
ATOM   12482 C CA    . LEU D  1 425 ? -22.270 51.123  -61.346 1.00 45.91 ? 425 LEU B CA    1 
ATOM   12483 C C     . LEU D  1 425 ? -22.670 52.581  -61.531 1.00 46.29 ? 425 LEU B C     1 
ATOM   12484 O O     . LEU D  1 425 ? -23.830 52.891  -61.828 1.00 46.64 ? 425 LEU B O     1 
ATOM   12485 C CB    . LEU D  1 425 ? -22.239 50.740  -59.858 1.00 42.73 ? 425 LEU B CB    1 
ATOM   12486 C CG    . LEU D  1 425 ? -23.551 50.542  -59.090 1.00 41.39 ? 425 LEU B CG    1 
ATOM   12487 C CD1   . LEU D  1 425 ? -24.606 50.001  -59.997 1.00 39.38 ? 425 LEU B CD1   1 
ATOM   12488 C CD2   . LEU D  1 425 ? -23.378 49.595  -57.931 1.00 37.52 ? 425 LEU B CD2   1 
ATOM   12489 N N     . THR D  1 426 ? -21.703 53.484  -61.428 1.00 45.48 ? 426 THR B N     1 
ATOM   12490 C CA    . THR D  1 426 ? -22.006 54.907  -61.402 1.00 48.25 ? 426 THR B CA    1 
ATOM   12491 C C     . THR D  1 426 ? -22.379 55.449  -62.778 1.00 45.90 ? 426 THR B C     1 
ATOM   12492 O O     . THR D  1 426 ? -23.392 56.145  -62.926 1.00 46.12 ? 426 THR B O     1 
ATOM   12493 C CB    . THR D  1 426 ? -20.810 55.657  -60.831 1.00 55.37 ? 426 THR B CB    1 
ATOM   12494 O OG1   . THR D  1 426 ? -20.291 54.927  -59.703 1.00 54.63 ? 426 THR B OG1   1 
ATOM   12495 C CG2   . THR D  1 426 ? -21.234 57.053  -60.406 1.00 59.04 ? 426 THR B CG2   1 
ATOM   12496 N N     . ALA D  1 427 ? -21.566 55.158  -63.792 1.00 45.30 ? 427 ALA B N     1 
ATOM   12497 C CA    . ALA D  1 427 ? -21.892 55.609  -65.139 1.00 43.86 ? 427 ALA B CA    1 
ATOM   12498 C C     . ALA D  1 427 ? -23.289 55.148  -65.536 1.00 42.28 ? 427 ALA B C     1 
ATOM   12499 O O     . ALA D  1 427 ? -24.113 55.946  -65.987 1.00 46.18 ? 427 ALA B O     1 
ATOM   12500 C CB    . ALA D  1 427 ? -20.843 55.094  -66.125 1.00 52.67 ? 427 ALA B CB    1 
ATOM   12501 N N     . MET D  1 428 ? -23.576 53.858  -65.333 1.00 39.62 ? 428 MET B N     1 
ATOM   12502 C CA    . MET D  1 428 ? -24.892 53.299  -65.642 1.00 38.87 ? 428 MET B CA    1 
ATOM   12503 C C     . MET D  1 428 ? -26.004 54.167  -65.062 1.00 40.77 ? 428 MET B C     1 
ATOM   12504 O O     . MET D  1 428 ? -26.914 54.599  -65.778 1.00 40.44 ? 428 MET B O     1 
ATOM   12505 C CB    . MET D  1 428 ? -24.976 51.875  -65.087 1.00 42.02 ? 428 MET B CB    1 
ATOM   12506 C CG    . MET D  1 428 ? -24.334 50.825  -65.976 1.00 43.43 ? 428 MET B CG    1 
ATOM   12507 S SD    . MET D  1 428 ? -24.377 49.134  -65.337 1.00 57.20 ? 428 MET B SD    1 
ATOM   12508 C CE    . MET D  1 428 ? -23.945 49.354  -63.634 1.00 43.61 ? 428 MET B CE    1 
ATOM   12509 N N     . LYS D  1 429 ? -25.925 54.450  -63.760 1.00 40.85 ? 429 LYS B N     1 
ATOM   12510 C CA    . LYS D  1 429 ? -26.863 55.373  -63.139 1.00 40.04 ? 429 LYS B CA    1 
ATOM   12511 C C     . LYS D  1 429 ? -26.810 56.729  -63.819 1.00 38.76 ? 429 LYS B C     1 
ATOM   12512 O O     . LYS D  1 429 ? -27.843 57.293  -64.188 1.00 41.11 ? 429 LYS B O     1 
ATOM   12513 C CB    . LYS D  1 429 ? -26.544 55.523  -61.649 1.00 43.90 ? 429 LYS B CB    1 
ATOM   12514 C CG    . LYS D  1 429 ? -26.816 54.299  -60.794 1.00 40.84 ? 429 LYS B CG    1 
ATOM   12515 C CD    . LYS D  1 429 ? -26.024 54.359  -59.492 1.00 36.68 ? 429 LYS B CD    1 
ATOM   12516 C CE    . LYS D  1 429 ? -26.859 54.877  -58.332 1.00 36.22 ? 429 LYS B CE    1 
ATOM   12517 N NZ    . LYS D  1 429 ? -26.625 56.336  -58.049 1.00 48.52 ? 429 LYS B NZ    1 
ATOM   12518 N N     . ASP D  1 430 ? -25.607 57.280  -63.967 1.00 36.71 ? 430 ASP B N     1 
ATOM   12519 C CA    . ASP D  1 430 ? -25.471 58.572  -64.618 1.00 42.05 ? 430 ASP B CA    1 
ATOM   12520 C C     . ASP D  1 430 ? -26.083 58.542  -66.013 1.00 42.87 ? 430 ASP B C     1 
ATOM   12521 O O     . ASP D  1 430 ? -26.684 59.529  -66.451 1.00 43.27 ? 430 ASP B O     1 
ATOM   12522 C CB    . ASP D  1 430 ? -23.993 58.969  -64.664 1.00 48.41 ? 430 ASP B CB    1 
ATOM   12523 C CG    . ASP D  1 430 ? -23.663 60.168  -63.763 1.00 55.46 ? 430 ASP B CG    1 
ATOM   12524 O OD1   . ASP D  1 430 ? -24.492 60.546  -62.900 1.00 47.10 ? 430 ASP B OD1   1 
ATOM   12525 O OD2   . ASP D  1 430 ? -22.565 60.746  -63.930 1.00 62.14 ? 430 ASP B OD2   1 
ATOM   12526 N N     . GLU D  1 431 ? -25.975 57.411  -66.708 1.00 43.79 ? 431 GLU B N     1 
ATOM   12527 C CA    . GLU D  1 431 ? -26.690 57.234  -67.965 1.00 43.79 ? 431 GLU B CA    1 
ATOM   12528 C C     . GLU D  1 431 ? -28.181 57.027  -67.736 1.00 47.59 ? 431 GLU B C     1 
ATOM   12529 O O     . GLU D  1 431 ? -28.992 57.360  -68.611 1.00 49.55 ? 431 GLU B O     1 
ATOM   12530 C CB    . GLU D  1 431 ? -26.115 56.046  -68.747 1.00 41.17 ? 431 GLU B CB    1 
ATOM   12531 C CG    . GLU D  1 431 ? -24.633 56.147  -69.104 1.00 43.06 ? 431 GLU B CG    1 
ATOM   12532 C CD    . GLU D  1 431 ? -24.332 57.267  -70.081 1.00 49.11 ? 431 GLU B CD    1 
ATOM   12533 O OE1   . GLU D  1 431 ? -25.216 57.598  -70.906 1.00 50.56 ? 431 GLU B OE1   1 
ATOM   12534 O OE2   . GLU D  1 431 ? -23.202 57.808  -70.024 1.00 51.53 ? 431 GLU B OE2   1 
ATOM   12535 N N     . ILE D  1 432 ? -28.558 56.473  -66.579 1.00 43.05 ? 432 ILE B N     1 
ATOM   12536 C CA    . ILE D  1 432 ? -29.973 56.323  -66.251 1.00 43.10 ? 432 ILE B CA    1 
ATOM   12537 C C     . ILE D  1 432 ? -30.639 57.693  -66.154 1.00 41.76 ? 432 ILE B C     1 
ATOM   12538 O O     . ILE D  1 432 ? -31.636 57.973  -66.832 1.00 39.12 ? 432 ILE B O     1 
ATOM   12539 C CB    . ILE D  1 432 ? -30.131 55.521  -64.947 1.00 41.49 ? 432 ILE B CB    1 
ATOM   12540 C CG1   . ILE D  1 432 ? -29.952 54.027  -65.211 1.00 41.24 ? 432 ILE B CG1   1 
ATOM   12541 C CG2   . ILE D  1 432 ? -31.472 55.803  -64.329 1.00 38.49 ? 432 ILE B CG2   1 
ATOM   12542 C CD1   . ILE D  1 432 ? -29.382 53.245  -64.035 1.00 36.92 ? 432 ILE B CD1   1 
ATOM   12543 N N     . ALA D  1 433 ? -30.084 58.577  -65.322 1.00 44.30 ? 433 ALA B N     1 
ATOM   12544 C CA    . ALA D  1 433 ? -30.646 59.921  -65.213 1.00 51.07 ? 433 ALA B CA    1 
ATOM   12545 C C     . ALA D  1 433 ? -30.559 60.678  -66.538 1.00 48.95 ? 433 ALA B C     1 
ATOM   12546 O O     . ALA D  1 433 ? -31.393 61.554  -66.807 1.00 49.14 ? 433 ALA B O     1 
ATOM   12547 C CB    . ALA D  1 433 ? -29.948 60.702  -64.095 1.00 45.64 ? 433 ALA B CB    1 
ATOM   12548 N N     . THR D  1 434 ? -29.572 60.355  -67.382 1.00 47.95 ? 434 THR B N     1 
ATOM   12549 C CA    . THR D  1 434 ? -29.464 61.014  -68.681 1.00 48.50 ? 434 THR B CA    1 
ATOM   12550 C C     . THR D  1 434 ? -30.627 60.631  -69.580 1.00 49.61 ? 434 THR B C     1 
ATOM   12551 O O     . THR D  1 434 ? -31.284 61.495  -70.175 1.00 53.39 ? 434 THR B O     1 
ATOM   12552 C CB    . THR D  1 434 ? -28.140 60.649  -69.349 1.00 48.95 ? 434 THR B CB    1 
ATOM   12553 O OG1   . THR D  1 434 ? -27.061 61.093  -68.521 1.00 46.77 ? 434 THR B OG1   1 
ATOM   12554 C CG2   . THR D  1 434 ? -28.040 61.294  -70.739 1.00 38.19 ? 434 THR B CG2   1 
ATOM   12555 N N     . THR D  1 435 ? -30.902 59.335  -69.673 1.00 44.67 ? 435 THR B N     1 
ATOM   12556 C CA    . THR D  1 435 ? -31.905 58.785  -70.567 1.00 44.82 ? 435 THR B CA    1 
ATOM   12557 C C     . THR D  1 435 ? -33.298 58.748  -69.941 1.00 47.37 ? 435 THR B C     1 
ATOM   12558 O O     . THR D  1 435 ? -34.293 59.046  -70.620 1.00 36.58 ? 435 THR B O     1 
ATOM   12559 C CB    . THR D  1 435 ? -31.468 57.384  -70.969 1.00 43.02 ? 435 THR B CB    1 
ATOM   12560 O OG1   . THR D  1 435 ? -30.199 57.471  -71.629 1.00 46.90 ? 435 THR B OG1   1 
ATOM   12561 C CG2   . THR D  1 435 ? -32.477 56.768  -71.893 1.00 43.21 ? 435 THR B CG2   1 
ATOM   12562 N N     . ALA D  1 436 ? -33.391 58.405  -68.650 1.00 43.80 ? 436 ALA B N     1 
ATOM   12563 C CA    . ALA D  1 436 ? -34.680 58.301  -67.984 1.00 38.26 ? 436 ALA B CA    1 
ATOM   12564 C C     . ALA D  1 436 ? -35.079 59.565  -67.247 1.00 43.89 ? 436 ALA B C     1 
ATOM   12565 O O     . ALA D  1 436 ? -36.270 59.750  -66.988 1.00 47.57 ? 436 ALA B O     1 
ATOM   12566 C CB    . ALA D  1 436 ? -34.686 57.133  -66.999 1.00 40.89 ? 436 ALA B CB    1 
ATOM   12567 N N     . GLY D  1 437 ? -34.127 60.430  -66.901 1.00 47.29 ? 437 GLY B N     1 
ATOM   12568 C CA    . GLY D  1 437 ? -34.441 61.680  -66.235 1.00 43.09 ? 437 GLY B CA    1 
ATOM   12569 C C     . GLY D  1 437 ? -34.755 61.534  -64.761 1.00 48.78 ? 437 GLY B C     1 
ATOM   12570 O O     . GLY D  1 437 ? -35.336 60.529  -64.336 1.00 50.10 ? 437 GLY B O     1 
ATOM   12571 N N     . THR D  1 438 ? -34.381 62.531  -63.966 1.00 49.61 ? 438 THR B N     1 
ATOM   12572 C CA    . THR D  1 438 ? -34.678 62.536  -62.545 1.00 51.73 ? 438 THR B CA    1 
ATOM   12573 C C     . THR D  1 438 ? -35.292 63.880  -62.171 1.00 55.62 ? 438 THR B C     1 
ATOM   12574 O O     . THR D  1 438 ? -35.248 64.846  -62.940 1.00 50.35 ? 438 THR B O     1 
ATOM   12575 C CB    . THR D  1 438 ? -33.424 62.251  -61.721 1.00 50.62 ? 438 THR B CB    1 
ATOM   12576 O OG1   . THR D  1 438 ? -32.394 63.167  -62.106 1.00 56.35 ? 438 THR B OG1   1 
ATOM   12577 C CG2   . THR D  1 438 ? -32.946 60.831  -61.974 1.00 46.98 ? 438 THR B CG2   1 
ATOM   12578 N N     . LEU D  1 439 ? -35.890 63.929  -60.978 1.00 55.81 ? 439 LEU B N     1 
ATOM   12579 C CA    . LEU D  1 439 ? -36.559 65.148  -60.539 1.00 49.88 ? 439 LEU B CA    1 
ATOM   12580 C C     . LEU D  1 439 ? -35.550 66.210  -60.127 1.00 59.80 ? 439 LEU B C     1 
ATOM   12581 O O     . LEU D  1 439 ? -35.429 67.250  -60.783 1.00 63.74 ? 439 LEU B O     1 
ATOM   12582 C CB    . LEU D  1 439 ? -37.497 64.857  -59.373 1.00 49.37 ? 439 LEU B CB    1 
ATOM   12583 C CG    . LEU D  1 439 ? -38.499 63.712  -59.452 1.00 47.08 ? 439 LEU B CG    1 
ATOM   12584 C CD1   . LEU D  1 439 ? -39.594 63.956  -58.432 1.00 49.48 ? 439 LEU B CD1   1 
ATOM   12585 C CD2   . LEU D  1 439 ? -39.076 63.560  -60.834 1.00 47.24 ? 439 LEU B CD2   1 
ATOM   12586 N N     . SER D  1 440 ? -34.808 65.938  -59.051 1.00 65.77 ? 440 SER B N     1 
ATOM   12587 C CA    . SER D  1 440 ? -33.970 66.898  -58.308 1.00 71.74 ? 440 SER B CA    1 
ATOM   12588 C C     . SER D  1 440 ? -34.840 67.882  -57.498 1.00 78.48 ? 440 SER B C     1 
ATOM   12589 O O     . SER D  1 440 ? -36.084 67.807  -57.514 1.00 75.33 ? 440 SER B O     1 
ATOM   12590 C CB    . SER D  1 440 ? -33.004 67.660  -59.237 1.00 66.60 ? 440 SER B CB    1 
ATOM   12591 O OG    . SER D  1 440 ? -31.729 67.039  -59.305 1.00 60.19 ? 440 SER B OG    1 
HETATM 12592 P PG    . ANP E  2 .   ? -26.158 12.983  11.038  1.00 63.92 ? 501 ANP C PG    1 
HETATM 12593 O O1G   . ANP E  2 .   ? -26.575 14.073  11.995  1.00 50.30 ? 501 ANP C O1G   1 
HETATM 12594 O O2G   . ANP E  2 .   ? -27.423 12.061  10.852  1.00 50.41 ? 501 ANP C O2G   1 
HETATM 12595 O O3G   . ANP E  2 .   ? -25.722 13.604  9.633   1.00 55.23 ? 501 ANP C O3G   1 
HETATM 12596 P PB    . ANP E  2 .   ? -23.473 11.926  10.758  1.00 55.75 ? 501 ANP C PB    1 
HETATM 12597 O O1B   . ANP E  2 .   ? -23.532 12.922  9.647   1.00 48.86 ? 501 ANP C O1B   1 
HETATM 12598 O O2B   . ANP E  2 .   ? -22.310 12.262  11.742  1.00 51.62 ? 501 ANP C O2B   1 
HETATM 12599 N N3B   . ANP E  2 .   ? -24.889 12.042  11.674  1.00 50.60 ? 501 ANP C N3B   1 
HETATM 12600 P PA    . ANP E  2 .   ? -21.986 10.131  9.164   1.00 51.98 ? 501 ANP C PA    1 
HETATM 12601 O O1A   . ANP E  2 .   ? -21.124 8.934   9.411   1.00 38.95 ? 501 ANP C O1A   1 
HETATM 12602 O O2A   . ANP E  2 .   ? -22.640 9.930   7.794   1.00 58.97 ? 501 ANP C O2A   1 
HETATM 12603 O O3A   . ANP E  2 .   ? -23.186 10.481  10.186  1.00 51.83 ? 501 ANP C O3A   1 
HETATM 12604 O "O5'" . ANP E  2 .   ? -21.100 11.406  9.149   1.00 45.38 ? 501 ANP C "O5'" 1 
HETATM 12605 C "C5'" . ANP E  2 .   ? -19.869 11.254  8.516   1.00 38.43 ? 501 ANP C "C5'" 1 
HETATM 12606 C "C4'" . ANP E  2 .   ? -18.921 11.106  9.649   1.00 43.73 ? 501 ANP C "C4'" 1 
HETATM 12607 O "O4'" . ANP E  2 .   ? -17.664 10.615  9.138   1.00 58.56 ? 501 ANP C "O4'" 1 
HETATM 12608 C "C3'" . ANP E  2 .   ? -18.630 12.422  10.367  1.00 41.24 ? 501 ANP C "C3'" 1 
HETATM 12609 O "O3'" . ANP E  2 .   ? -18.551 12.251  11.776  1.00 44.78 ? 501 ANP C "O3'" 1 
HETATM 12610 C "C2'" . ANP E  2 .   ? -17.259 12.814  9.827   1.00 45.44 ? 501 ANP C "C2'" 1 
HETATM 12611 O "O2'" . ANP E  2 .   ? -16.595 13.547  10.850  1.00 44.83 ? 501 ANP C "O2'" 1 
HETATM 12612 C "C1'" . ANP E  2 .   ? -16.629 11.442  9.611   1.00 45.04 ? 501 ANP C "C1'" 1 
HETATM 12613 N N9    . ANP E  2 .   ? -15.526 11.403  8.658   1.00 46.53 ? 501 ANP C N9    1 
HETATM 12614 C C8    . ANP E  2 .   ? -15.556 11.311  7.293   1.00 33.97 ? 501 ANP C C8    1 
HETATM 12615 N N7    . ANP E  2 .   ? -14.370 11.312  6.732   1.00 38.24 ? 501 ANP C N7    1 
HETATM 12616 C C5    . ANP E  2 .   ? -13.499 11.371  7.813   1.00 34.22 ? 501 ANP C C5    1 
HETATM 12617 C C6    . ANP E  2 .   ? -12.093 11.387  7.903   1.00 36.19 ? 501 ANP C C6    1 
HETATM 12618 N N6    . ANP E  2 .   ? -11.267 11.314  6.862   1.00 30.65 ? 501 ANP C N6    1 
HETATM 12619 N N1    . ANP E  2 .   ? -11.547 11.455  9.131   1.00 45.35 ? 501 ANP C N1    1 
HETATM 12620 C C2    . ANP E  2 .   ? -12.351 11.495  10.194  1.00 39.86 ? 501 ANP C C2    1 
HETATM 12621 N N3    . ANP E  2 .   ? -13.681 11.493  10.233  1.00 43.71 ? 501 ANP C N3    1 
HETATM 12622 C C4    . ANP E  2 .   ? -14.198 11.424  8.999   1.00 44.59 ? 501 ANP C C4    1 
HETATM 12623 C C1    . GOL F  3 .   ? -11.975 11.332  3.761   1.00 34.30 ? 502 GOL C C1    1 
HETATM 12624 O O1    . GOL F  3 .   ? -12.842 10.576  2.912   1.00 27.86 ? 502 GOL C O1    1 
HETATM 12625 C C2    . GOL F  3 .   ? -10.814 10.397  4.174   1.00 33.59 ? 502 GOL C C2    1 
HETATM 12626 O O2    . GOL F  3 .   ? -11.162 9.073   4.186   1.00 34.77 ? 502 GOL C O2    1 
HETATM 12627 C C3    . GOL F  3 .   ? -9.619  10.744  3.295   1.00 34.11 ? 502 GOL C C3    1 
HETATM 12628 O O3    . GOL F  3 .   ? -8.967  11.760  3.966   1.00 36.29 ? 502 GOL C O3    1 
HETATM 12629 C C1    . GOL G  3 .   ? -22.332 17.391  12.212  1.00 41.72 ? 503 GOL C C1    1 
HETATM 12630 O O1    . GOL G  3 .   ? -21.628 16.802  13.266  1.00 42.48 ? 503 GOL C O1    1 
HETATM 12631 C C2    . GOL G  3 .   ? -21.784 16.818  10.918  1.00 38.74 ? 503 GOL C C2    1 
HETATM 12632 O O2    . GOL G  3 .   ? -20.413 17.059  10.798  1.00 46.15 ? 503 GOL C O2    1 
HETATM 12633 C C3    . GOL G  3 .   ? -22.148 15.332  10.987  1.00 43.12 ? 503 GOL C C3    1 
HETATM 12634 O O3    . GOL G  3 .   ? -23.498 15.197  10.598  1.00 44.62 ? 503 GOL C O3    1 
HETATM 12635 C C1    . PEG H  4 .   ? 5.457   23.902  6.102   1.00 46.05 ? 504 PEG C C1    1 
HETATM 12636 O O1    . PEG H  4 .   ? 6.774   23.840  5.581   1.00 45.46 ? 504 PEG C O1    1 
HETATM 12637 C C2    . PEG H  4 .   ? 4.619   22.755  5.630   1.00 50.60 ? 504 PEG C C2    1 
HETATM 12638 O O2    . PEG H  4 .   ? 3.946   23.114  4.434   1.00 50.02 ? 504 PEG C O2    1 
HETATM 12639 C C3    . PEG H  4 .   ? 2.568   23.404  4.636   1.00 47.91 ? 504 PEG C C3    1 
HETATM 12640 C C4    . PEG H  4 .   ? 2.200   24.648  3.890   1.00 41.78 ? 504 PEG C C4    1 
HETATM 12641 O O4    . PEG H  4 .   ? 1.094   25.310  4.480   1.00 44.82 ? 504 PEG C O4    1 
HETATM 12642 P PG    . ANP I  2 .   ? -1.420  22.506  1.842   1.00 58.26 ? 505 ANP C PG    1 
HETATM 12643 O O1G   . ANP I  2 .   ? -0.595  22.259  3.080   1.00 47.56 ? 505 ANP C O1G   1 
HETATM 12644 O O2G   . ANP I  2 .   ? -1.887  21.158  1.173   1.00 45.40 ? 505 ANP C O2G   1 
HETATM 12645 O O3G   . ANP I  2 .   ? -2.696  23.387  2.208   1.00 64.15 ? 505 ANP C O3G   1 
HETATM 12646 P PB    . ANP I  2 .   ? 0.477   22.342  -0.225  1.00 44.50 ? 505 ANP C PB    1 
HETATM 12647 O O1B   . ANP I  2 .   ? -0.325  21.210  -0.796  1.00 45.92 ? 505 ANP C O1B   1 
HETATM 12648 O O2B   . ANP I  2 .   ? 1.613   21.823  0.692   1.00 46.30 ? 505 ANP C O2B   1 
HETATM 12649 N N3B   . ANP I  2 .   ? -0.517  23.352  0.693   1.00 53.47 ? 505 ANP C N3B   1 
HETATM 12650 P PA    . ANP I  2 .   ? 1.205   24.788  -1.259  1.00 40.63 ? 505 ANP C PA    1 
HETATM 12651 O O1A   . ANP I  2 .   ? -0.132  25.424  -1.350  1.00 37.75 ? 505 ANP C O1A   1 
HETATM 12652 O O2A   . ANP I  2 .   ? 2.264   25.276  -2.259  1.00 43.21 ? 505 ANP C O2A   1 
HETATM 12653 O O3A   . ANP I  2 .   ? 1.093   23.192  -1.390  1.00 45.18 ? 505 ANP C O3A   1 
HETATM 12654 O "O5'" . ANP I  2 .   ? 1.665   25.048  0.243   1.00 42.23 ? 505 ANP C "O5'" 1 
HETATM 12655 C "C5'" . ANP I  2 .   ? 3.001   25.368  0.563   1.00 40.37 ? 505 ANP C "C5'" 1 
HETATM 12656 C "C4'" . ANP I  2 .   ? 3.058   26.714  1.244   1.00 39.32 ? 505 ANP C "C4'" 1 
HETATM 12657 O "O4'" . ANP I  2 .   ? 4.339   27.311  0.953   1.00 40.78 ? 505 ANP C "O4'" 1 
HETATM 12658 C "C3'" . ANP I  2 .   ? 2.003   27.737  0.828   1.00 36.16 ? 505 ANP C "C3'" 1 
HETATM 12659 O "O3'" . ANP I  2 .   ? 0.947   27.767  1.781   1.00 36.76 ? 505 ANP C "O3'" 1 
HETATM 12660 C "C2'" . ANP I  2 .   ? 2.771   29.056  0.882   1.00 39.26 ? 505 ANP C "C2'" 1 
HETATM 12661 O "O2'" . ANP I  2 .   ? 2.888   29.505  2.227   1.00 34.86 ? 505 ANP C "O2'" 1 
HETATM 12662 C "C1'" . ANP I  2 .   ? 4.161   28.614  0.447   1.00 38.45 ? 505 ANP C "C1'" 1 
HETATM 12663 N N9    . ANP I  2 .   ? 4.391   28.591  -0.992  1.00 35.46 ? 505 ANP C N9    1 
HETATM 12664 C C8    . ANP I  2 .   ? 4.106   27.587  -1.879  1.00 32.20 ? 505 ANP C C8    1 
HETATM 12665 N N7    . ANP I  2 .   ? 4.452   27.859  -3.119  1.00 39.71 ? 505 ANP C N7    1 
HETATM 12666 C C5    . ANP I  2 .   ? 5.030   29.119  -3.030  1.00 36.88 ? 505 ANP C C5    1 
HETATM 12667 C C6    . ANP I  2 .   ? 5.611   29.978  -3.996  1.00 37.15 ? 505 ANP C C6    1 
HETATM 12668 N N6    . ANP I  2 .   ? 5.708   29.683  -5.297  1.00 32.05 ? 505 ANP C N6    1 
HETATM 12669 N N1    . ANP I  2 .   ? 6.087   31.171  -3.572  1.00 36.49 ? 505 ANP C N1    1 
HETATM 12670 C C2    . ANP I  2 .   ? 5.987   31.480  -2.276  1.00 38.27 ? 505 ANP C C2    1 
HETATM 12671 N N3    . ANP I  2 .   ? 5.472   30.756  -1.280  1.00 39.80 ? 505 ANP C N3    1 
HETATM 12672 C C4    . ANP I  2 .   ? 5.005   29.585  -1.726  1.00 38.20 ? 505 ANP C C4    1 
HETATM 12673 C C1    . GOL J  3 .   ? -17.814 9.092   -32.348 1.00 36.38 ? 501 GOL D C1    1 
HETATM 12674 O O1    . GOL J  3 .   ? -19.122 8.691   -32.618 1.00 35.28 ? 501 GOL D O1    1 
HETATM 12675 C C2    . GOL J  3 .   ? -17.211 7.796   -31.807 1.00 39.59 ? 501 GOL D C2    1 
HETATM 12676 O O2    . GOL J  3 .   ? -15.874 7.938   -31.366 1.00 38.98 ? 501 GOL D O2    1 
HETATM 12677 C C3    . GOL J  3 .   ? -18.207 7.421   -30.725 1.00 33.85 ? 501 GOL D C3    1 
HETATM 12678 O O3    . GOL J  3 .   ? -18.388 6.052   -30.713 1.00 36.53 ? 501 GOL D O3    1 
HETATM 12679 C C1    . GOL K  3 .   ? -0.565  32.754  -40.942 1.00 40.09 ? 502 GOL D C1    1 
HETATM 12680 O O1    . GOL K  3 .   ? 0.767   32.279  -40.868 1.00 32.80 ? 502 GOL D O1    1 
HETATM 12681 C C2    . GOL K  3 .   ? -0.878  33.082  -42.384 1.00 39.41 ? 502 GOL D C2    1 
HETATM 12682 O O2    . GOL K  3 .   ? -2.240  33.151  -42.560 1.00 37.66 ? 502 GOL D O2    1 
HETATM 12683 C C3    . GOL K  3 .   ? -0.181  34.453  -42.626 1.00 41.09 ? 502 GOL D C3    1 
HETATM 12684 O O3    . GOL K  3 .   ? -0.960  35.429  -42.040 1.00 29.46 ? 502 GOL D O3    1 
HETATM 12685 C C1    . PEG L  4 .   ? 0.129   29.417  -40.377 1.00 32.56 ? 503 PEG D C1    1 
HETATM 12686 O O1    . PEG L  4 .   ? 1.346   29.924  -40.910 1.00 29.14 ? 503 PEG D O1    1 
HETATM 12687 C C2    . PEG L  4 .   ? -0.655  28.647  -41.406 1.00 37.36 ? 503 PEG D C2    1 
HETATM 12688 O O2    . PEG L  4 .   ? -0.426  27.249  -41.245 1.00 41.87 ? 503 PEG D O2    1 
HETATM 12689 C C3    . PEG L  4 .   ? -0.515  26.837  -39.885 1.00 40.43 ? 503 PEG D C3    1 
HETATM 12690 C C4    . PEG L  4 .   ? 0.169   25.518  -39.684 1.00 45.33 ? 503 PEG D C4    1 
HETATM 12691 O O4    . PEG L  4 .   ? 0.630   25.346  -38.351 1.00 33.95 ? 503 PEG D O4    1 
HETATM 12692 P P     . AMP M  5 .   ? -0.299  22.344  -34.621 1.00 64.20 ? 504 AMP D P     1 
HETATM 12693 O O1P   . AMP M  5 .   ? -1.208  21.144  -34.785 1.00 59.25 ? 504 AMP D O1P   1 
HETATM 12694 O O2P   . AMP M  5 .   ? 0.966   22.000  -33.859 1.00 46.49 ? 504 AMP D O2P   1 
HETATM 12695 O O3P   . AMP M  5 .   ? -1.007  23.573  -34.094 1.00 48.17 ? 504 AMP D O3P   1 
HETATM 12696 O "O5'" . AMP M  5 .   ? 0.183   22.687  -36.117 1.00 56.27 ? 504 AMP D "O5'" 1 
HETATM 12697 C "C5'" . AMP M  5 .   ? -0.741  22.867  -37.205 1.00 52.59 ? 504 AMP D "C5'" 1 
HETATM 12698 C "C4'" . AMP M  5 .   ? -0.196  22.344  -38.517 1.00 53.26 ? 504 AMP D "C4'" 1 
HETATM 12699 O "O4'" . AMP M  5 .   ? 0.820   21.370  -38.234 1.00 65.80 ? 504 AMP D "O4'" 1 
HETATM 12700 C "C3'" . AMP M  5 .   ? -1.171  21.643  -39.443 1.00 47.18 ? 504 AMP D "C3'" 1 
HETATM 12701 O "O3'" . AMP M  5 .   ? -0.677  21.720  -40.779 1.00 47.47 ? 504 AMP D "O3'" 1 
HETATM 12702 C "C2'" . AMP M  5 .   ? -1.113  20.182  -38.967 1.00 49.39 ? 504 AMP D "C2'" 1 
HETATM 12703 O "O2'" . AMP M  5 .   ? -1.237  19.233  -40.009 1.00 50.94 ? 504 AMP D "O2'" 1 
HETATM 12704 C "C1'" . AMP M  5 .   ? 0.270   20.070  -38.305 1.00 47.83 ? 504 AMP D "C1'" 1 
HETATM 12705 N N9    . AMP M  5 .   ? 0.267   19.534  -36.937 1.00 55.55 ? 504 AMP D N9    1 
HETATM 12706 C C8    . AMP M  5 .   ? 1.144   19.955  -36.003 1.00 52.37 ? 504 AMP D C8    1 
HETATM 12707 N N7    . AMP M  5 .   ? 0.964   19.309  -34.816 1.00 53.09 ? 504 AMP D N7    1 
HETATM 12708 C C5    . AMP M  5 .   ? -0.028  18.418  -34.991 1.00 48.67 ? 504 AMP D C5    1 
HETATM 12709 C C6    . AMP M  5 .   ? -0.679  17.405  -34.148 1.00 52.40 ? 504 AMP D C6    1 
HETATM 12710 N N6    . AMP M  5 .   ? -0.281  17.230  -32.861 1.00 56.88 ? 504 AMP D N6    1 
HETATM 12711 N N1    . AMP M  5 .   ? -1.675  16.670  -34.694 1.00 51.17 ? 504 AMP D N1    1 
HETATM 12712 C C2    . AMP M  5 .   ? -2.067  16.835  -35.971 1.00 49.47 ? 504 AMP D C2    1 
HETATM 12713 N N3    . AMP M  5 .   ? -1.515  17.734  -36.802 1.00 56.39 ? 504 AMP D N3    1 
HETATM 12714 C C4    . AMP M  5 .   ? -0.493  18.550  -36.390 1.00 61.93 ? 504 AMP D C4    1 
HETATM 12715 C C1    . PEG N  4 .   ? -14.282 10.015  -29.700 1.00 29.17 ? 505 PEG D C1    1 
HETATM 12716 O O1    . PEG N  4 .   ? -15.196 8.999   -29.363 1.00 23.20 ? 505 PEG D O1    1 
HETATM 12717 C C2    . PEG N  4 .   ? -12.907 9.439   -29.879 1.00 34.17 ? 505 PEG D C2    1 
HETATM 12718 O O2    . PEG N  4 .   ? -12.143 10.290  -30.704 1.00 29.84 ? 505 PEG D O2    1 
HETATM 12719 C C3    . PEG N  4 .   ? -12.676 10.337  -32.023 1.00 38.67 ? 505 PEG D C3    1 
HETATM 12720 C C4    . PEG N  4 .   ? -13.084 11.724  -32.432 1.00 34.62 ? 505 PEG D C4    1 
HETATM 12721 O O4    . PEG N  4 .   ? -11.971 12.515  -32.800 1.00 34.50 ? 505 PEG D O4    1 
HETATM 12722 P PB    . ADP O  6 .   ? -46.550 43.777  -5.696  1.00 66.00 ? 501 ADP A PB    1 
HETATM 12723 O O1B   . ADP O  6 .   ? -45.636 44.792  -6.311  1.00 65.81 ? 501 ADP A O1B   1 
HETATM 12724 O O2B   . ADP O  6 .   ? -46.710 43.972  -4.216  1.00 39.77 ? 501 ADP A O2B   1 
HETATM 12725 O O3B   . ADP O  6 .   ? -46.184 42.365  -6.048  1.00 50.01 ? 501 ADP A O3B   1 
HETATM 12726 P PA    . ADP O  6 .   ? -48.496 44.213  -7.859  1.00 55.71 ? 501 ADP A PA    1 
HETATM 12727 O O1A   . ADP O  6 .   ? -47.393 44.875  -8.608  1.00 42.57 ? 501 ADP A O1A   1 
HETATM 12728 O O2A   . ADP O  6 .   ? -49.824 44.883  -7.885  1.00 43.43 ? 501 ADP A O2A   1 
HETATM 12729 O O3A   . ADP O  6 .   ? -48.004 44.027  -6.348  1.00 47.40 ? 501 ADP A O3A   1 
HETATM 12730 O "O5'" . ADP O  6 .   ? -48.665 42.698  -8.354  1.00 44.60 ? 501 ADP A "O5'" 1 
HETATM 12731 C "C5'" . ADP O  6 .   ? -49.992 42.112  -8.323  1.00 43.93 ? 501 ADP A "C5'" 1 
HETATM 12732 C "C4'" . ADP O  6 .   ? -49.952 40.840  -7.516  1.00 43.16 ? 501 ADP A "C4'" 1 
HETATM 12733 O "O4'" . ADP O  6 .   ? -51.278 40.259  -7.402  1.00 49.69 ? 501 ADP A "O4'" 1 
HETATM 12734 C "C3'" . ADP O  6 .   ? -49.115 39.705  -8.102  1.00 47.08 ? 501 ADP A "C3'" 1 
HETATM 12735 O "O3'" . ADP O  6 .   ? -47.726 39.952  -7.937  1.00 53.32 ? 501 ADP A "O3'" 1 
HETATM 12736 C "C2'" . ADP O  6 .   ? -49.707 38.523  -7.336  1.00 41.41 ? 501 ADP A "C2'" 1 
HETATM 12737 O "O2'" . ADP O  6 .   ? -49.314 38.510  -5.984  1.00 46.53 ? 501 ADP A "O2'" 1 
HETATM 12738 C "C1'" . ADP O  6 .   ? -51.191 38.850  -7.459  1.00 45.38 ? 501 ADP A "C1'" 1 
HETATM 12739 N N9    . ADP O  6 .   ? -51.767 38.408  -8.721  1.00 43.14 ? 501 ADP A N9    1 
HETATM 12740 C C8    . ADP O  6 .   ? -51.756 39.115  -9.893  1.00 38.30 ? 501 ADP A C8    1 
HETATM 12741 N N7    . ADP O  6 .   ? -52.331 38.488  -10.886 1.00 52.93 ? 501 ADP A N7    1 
HETATM 12742 C C5    . ADP O  6 .   ? -52.748 37.288  -10.338 1.00 45.99 ? 501 ADP A C5    1 
HETATM 12743 C C6    . ADP O  6 .   ? -53.425 36.188  -10.894 1.00 43.16 ? 501 ADP A C6    1 
HETATM 12744 N N6    . ADP O  6 .   ? -53.807 36.123  -12.164 1.00 46.72 ? 501 ADP A N6    1 
HETATM 12745 N N1    . ADP O  6 .   ? -53.692 35.144  -10.078 1.00 46.44 ? 501 ADP A N1    1 
HETATM 12746 C C2    . ADP O  6 .   ? -53.297 35.223  -8.802  1.00 49.27 ? 501 ADP A C2    1 
HETATM 12747 N N3    . ADP O  6 .   ? -52.656 36.203  -8.171  1.00 51.27 ? 501 ADP A N3    1 
HETATM 12748 C C4    . ADP O  6 .   ? -52.405 37.224  -9.003  1.00 46.38 ? 501 ADP A C4    1 
HETATM 12749 C C1    . PEG P  4 .   ? -31.370 54.637  0.881   1.00 25.95 ? 502 PEG A C1    1 
HETATM 12750 O O1    . PEG P  4 .   ? -31.486 54.911  2.289   1.00 27.87 ? 502 PEG A O1    1 
HETATM 12751 C C2    . PEG P  4 .   ? -32.084 55.644  0.023   1.00 18.63 ? 502 PEG A C2    1 
HETATM 12752 O O2    . PEG P  4 .   ? -33.241 55.012  -0.493  1.00 25.06 ? 502 PEG A O2    1 
HETATM 12753 C C3    . PEG P  4 .   ? -34.049 54.460  0.528   1.00 19.86 ? 502 PEG A C3    1 
HETATM 12754 C C4    . PEG P  4 .   ? -35.491 54.720  0.252   1.00 26.42 ? 502 PEG A C4    1 
HETATM 12755 O O4    . PEG P  4 .   ? -36.234 54.249  1.355   1.00 25.82 ? 502 PEG A O4    1 
HETATM 12756 C C1    . PEG Q  4 .   ? -29.653 52.928  4.043   1.00 30.18 ? 503 PEG A C1    1 
HETATM 12757 O O1    . PEG Q  4 .   ? -29.275 52.217  5.233   1.00 32.73 ? 503 PEG A O1    1 
HETATM 12758 C C2    . PEG Q  4 .   ? -28.489 53.706  3.510   1.00 30.18 ? 503 PEG A C2    1 
HETATM 12759 O O2    . PEG Q  4 .   ? -28.884 54.572  2.453   1.00 28.04 ? 503 PEG A O2    1 
HETATM 12760 C C3    . PEG Q  4 .   ? -27.953 54.561  1.369   1.00 26.45 ? 503 PEG A C3    1 
HETATM 12761 C C4    . PEG Q  4 .   ? -26.874 55.551  1.680   1.00 24.65 ? 503 PEG A C4    1 
HETATM 12762 O O4    . PEG Q  4 .   ? -27.448 56.842  1.836   1.00 20.66 ? 503 PEG A O4    1 
HETATM 12763 C C1    . PEG R  4 .   ? -18.977 53.803  5.009   1.00 37.52 ? 504 PEG A C1    1 
HETATM 12764 O O1    . PEG R  4 .   ? -18.812 52.443  4.639   1.00 36.87 ? 504 PEG A O1    1 
HETATM 12765 C C2    . PEG R  4 .   ? -20.406 54.098  5.303   1.00 36.96 ? 504 PEG A C2    1 
HETATM 12766 O O2    . PEG R  4 .   ? -21.222 53.116  4.670   1.00 40.76 ? 504 PEG A O2    1 
HETATM 12767 C C3    . PEG R  4 .   ? -21.437 53.346  3.273   1.00 33.00 ? 504 PEG A C3    1 
HETATM 12768 C C4    . PEG R  4 .   ? -22.755 52.763  2.826   1.00 36.90 ? 504 PEG A C4    1 
HETATM 12769 O O4    . PEG R  4 .   ? -23.888 53.580  3.150   1.00 35.70 ? 504 PEG A O4    1 
HETATM 12770 C C1    . PEG S  4 .   ? -35.489 55.395  -4.307  1.00 30.15 ? 505 PEG A C1    1 
HETATM 12771 O O1    . PEG S  4 .   ? -34.890 54.131  -4.045  1.00 29.43 ? 505 PEG A O1    1 
HETATM 12772 C C2    . PEG S  4 .   ? -36.067 55.968  -3.049  1.00 33.22 ? 505 PEG A C2    1 
HETATM 12773 O O2    . PEG S  4 .   ? -37.481 55.809  -3.051  1.00 38.85 ? 505 PEG A O2    1 
HETATM 12774 C C3    . PEG S  4 .   ? -37.939 54.557  -3.549  1.00 30.66 ? 505 PEG A C3    1 
HETATM 12775 C C4    . PEG S  4 .   ? -38.851 53.906  -2.546  1.00 40.03 ? 505 PEG A C4    1 
HETATM 12776 O O4    . PEG S  4 .   ? -40.180 53.759  -3.039  1.00 37.00 ? 505 PEG A O4    1 
HETATM 12777 C C1    . GOL T  3 .   ? -42.855 42.032  -4.274  1.00 40.19 ? 506 GOL A C1    1 
HETATM 12778 O O1    . GOL T  3 .   ? -43.185 40.895  -5.015  1.00 48.47 ? 506 GOL A O1    1 
HETATM 12779 C C2    . GOL T  3 .   ? -43.752 41.965  -3.032  1.00 47.71 ? 506 GOL A C2    1 
HETATM 12780 O O2    . GOL T  3 .   ? -43.473 40.861  -2.242  1.00 43.42 ? 506 GOL A O2    1 
HETATM 12781 C C3    . GOL T  3 .   ? -43.572 43.329  -2.304  1.00 47.99 ? 506 GOL A C3    1 
HETATM 12782 O O3    . GOL T  3 .   ? -42.200 43.499  -2.139  1.00 41.58 ? 506 GOL A O3    1 
HETATM 12783 C C1    . PEG U  4 .   ? -47.657 31.819  -49.587 1.00 36.86 ? 501 PEG B C1    1 
HETATM 12784 O O1    . PEG U  4 .   ? -46.992 30.585  -49.792 1.00 30.95 ? 501 PEG B O1    1 
HETATM 12785 C C2    . PEG U  4 .   ? -46.823 32.780  -48.804 1.00 32.81 ? 501 PEG B C2    1 
HETATM 12786 O O2    . PEG U  4 .   ? -47.344 34.085  -48.977 1.00 30.02 ? 501 PEG B O2    1 
HETATM 12787 C C3    . PEG U  4 .   ? -48.672 34.229  -48.518 1.00 27.41 ? 501 PEG B C3    1 
HETATM 12788 C C4    . PEG U  4 .   ? -49.067 35.667  -48.619 1.00 27.79 ? 501 PEG B C4    1 
HETATM 12789 O O4    . PEG U  4 .   ? -48.268 36.487  -47.784 1.00 24.17 ? 501 PEG B O4    1 
HETATM 12790 C C1    . PEG V  4 .   ? -46.976 44.872  -48.329 1.00 36.97 ? 502 PEG B C1    1 
HETATM 12791 O O1    . PEG V  4 .   ? -45.845 45.736  -48.364 1.00 37.14 ? 502 PEG B O1    1 
HETATM 12792 C C2    . PEG V  4 .   ? -47.074 44.152  -47.022 1.00 31.58 ? 502 PEG B C2    1 
HETATM 12793 O O2    . PEG V  4 .   ? -47.642 42.879  -47.265 1.00 31.93 ? 502 PEG B O2    1 
HETATM 12794 C C3    . PEG V  4 .   ? -47.417 41.956  -46.204 1.00 30.57 ? 502 PEG B C3    1 
HETATM 12795 C C4    . PEG V  4 .   ? -48.150 40.678  -46.498 1.00 26.33 ? 502 PEG B C4    1 
HETATM 12796 O O4    . PEG V  4 .   ? -47.943 40.242  -47.840 1.00 26.02 ? 502 PEG B O4    1 
HETATM 12797 C C1    . GOL W  3 .   ? -28.971 59.599  -35.216 1.00 33.24 ? 503 GOL B C1    1 
HETATM 12798 O O1    . GOL W  3 .   ? -28.109 60.463  -34.460 1.00 36.36 ? 503 GOL B O1    1 
HETATM 12799 C C2    . GOL W  3 .   ? -28.842 60.062  -36.678 1.00 36.82 ? 503 GOL B C2    1 
HETATM 12800 O O2    . GOL W  3 .   ? -27.515 60.339  -37.011 1.00 36.24 ? 503 GOL B O2    1 
HETATM 12801 C C3    . GOL W  3 .   ? -29.450 58.933  -37.516 1.00 35.84 ? 503 GOL B C3    1 
HETATM 12802 O O3    . GOL W  3 .   ? -29.246 59.296  -38.872 1.00 24.20 ? 503 GOL B O3    1 
HETATM 12803 C C     . TRS X  7 .   ? -34.916 56.028  -38.304 1.00 31.22 ? 504 TRS B C     1 
HETATM 12804 C C1    . TRS X  7 .   ? -34.874 55.746  -39.804 1.00 33.65 ? 504 TRS B C1    1 
HETATM 12805 C C2    . TRS X  7 .   ? -36.048 55.250  -37.652 1.00 32.94 ? 504 TRS B C2    1 
HETATM 12806 C C3    . TRS X  7 .   ? -33.524 55.861  -37.678 1.00 29.84 ? 504 TRS B C3    1 
HETATM 12807 N N     . TRS X  7 .   ? -35.302 57.412  -38.135 1.00 32.78 ? 504 TRS B N     1 
HETATM 12808 O O1    . TRS X  7 .   ? -35.322 54.438  -40.152 1.00 27.81 ? 504 TRS B O1    1 
HETATM 12809 O O2    . TRS X  7 .   ? -36.190 53.932  -38.157 1.00 35.90 ? 504 TRS B O2    1 
HETATM 12810 O O3    . TRS X  7 .   ? -33.122 56.961  -36.879 1.00 26.82 ? 504 TRS B O3    1 
HETATM 12811 O O     . HOH Y  8 .   ? -11.758 33.547  11.329  1.00 35.64 ? 601 HOH C O     1 
HETATM 12812 O O     . HOH Y  8 .   ? -28.747 5.447   14.592  1.00 40.06 ? 602 HOH C O     1 
HETATM 12813 O O     . HOH Y  8 .   ? 10.438  35.642  16.874  1.00 60.90 ? 603 HOH C O     1 
HETATM 12814 O O     . HOH Y  8 .   ? 2.718   19.021  -4.114  1.00 35.48 ? 604 HOH C O     1 
HETATM 12815 O O     . HOH Y  8 .   ? -17.972 34.776  11.819  1.00 35.66 ? 605 HOH C O     1 
HETATM 12816 O O     . HOH Y  8 .   ? -25.152 34.809  13.329  1.00 44.59 ? 606 HOH C O     1 
HETATM 12817 O O     . HOH Y  8 .   ? -17.682 14.671  12.470  1.00 42.02 ? 607 HOH C O     1 
HETATM 12818 O O     . HOH Y  8 .   ? 12.608  26.146  13.254  1.00 40.51 ? 608 HOH C O     1 
HETATM 12819 O O     . HOH Y  8 .   ? -29.184 12.811  12.090  1.00 41.73 ? 609 HOH C O     1 
HETATM 12820 O O     . HOH Y  8 .   ? 12.917  34.220  -13.645 1.00 29.18 ? 610 HOH C O     1 
HETATM 12821 O O     . HOH Y  8 .   ? -25.890 29.188  -8.137  1.00 38.05 ? 611 HOH C O     1 
HETATM 12822 O O     . HOH Y  8 .   ? -18.829 38.421  11.390  1.00 70.63 ? 612 HOH C O     1 
HETATM 12823 O O     . HOH Y  8 .   ? 13.142  33.088  -8.687  1.00 38.70 ? 613 HOH C O     1 
HETATM 12824 O O     . HOH Y  8 .   ? -14.338 -6.493  2.685   1.00 43.64 ? 614 HOH C O     1 
HETATM 12825 O O     . HOH Y  8 .   ? 2.660   29.529  -5.965  1.00 30.97 ? 615 HOH C O     1 
HETATM 12826 O O     . HOH Y  8 .   ? -12.669 4.709   -5.445  1.00 32.55 ? 616 HOH C O     1 
HETATM 12827 O O     . HOH Y  8 .   ? 8.392   34.488  3.544   1.00 35.93 ? 617 HOH C O     1 
HETATM 12828 O O     . HOH Y  8 .   ? 0.431   29.670  -8.194  1.00 29.99 ? 618 HOH C O     1 
HETATM 12829 O O     . HOH Y  8 .   ? -25.108 12.815  2.226   1.00 26.01 ? 619 HOH C O     1 
HETATM 12830 O O     . HOH Y  8 .   ? 6.583   10.945  -5.225  1.00 39.94 ? 620 HOH C O     1 
HETATM 12831 O O     . HOH Y  8 .   ? 3.080   13.394  18.970  1.00 32.89 ? 621 HOH C O     1 
HETATM 12832 O O     . HOH Y  8 .   ? -6.578  12.143  31.432  1.00 37.95 ? 622 HOH C O     1 
HETATM 12833 O O     . HOH Y  8 .   ? 6.196   10.839  -18.592 1.00 32.16 ? 623 HOH C O     1 
HETATM 12834 O O     . HOH Y  8 .   ? 12.204  19.235  18.972  1.00 40.13 ? 624 HOH C O     1 
HETATM 12835 O O     . HOH Y  8 .   ? 2.650   31.245  34.261  1.00 37.64 ? 625 HOH C O     1 
HETATM 12836 O O     . HOH Y  8 .   ? -10.422 20.565  9.930   1.00 25.64 ? 626 HOH C O     1 
HETATM 12837 O O     . HOH Y  8 .   ? -27.673 12.184  13.469  1.00 33.75 ? 627 HOH C O     1 
HETATM 12838 O O     . HOH Y  8 .   ? -5.428  44.493  21.995  1.00 46.79 ? 628 HOH C O     1 
HETATM 12839 O O     . HOH Y  8 .   ? -18.127 13.780  22.393  1.00 27.73 ? 629 HOH C O     1 
HETATM 12840 O O     . HOH Y  8 .   ? -4.774  17.205  16.023  1.00 34.31 ? 630 HOH C O     1 
HETATM 12841 O O     . HOH Y  8 .   ? 17.209  20.004  6.825   1.00 38.38 ? 631 HOH C O     1 
HETATM 12842 O O     . HOH Y  8 .   ? -6.466  -5.254  16.191  1.00 48.66 ? 632 HOH C O     1 
HETATM 12843 O O     . HOH Y  8 .   ? -4.129  18.498  -14.823 1.00 21.51 ? 633 HOH C O     1 
HETATM 12844 O O     . HOH Y  8 .   ? 24.600  22.035  -15.651 1.00 46.42 ? 634 HOH C O     1 
HETATM 12845 O O     . HOH Y  8 .   ? -12.495 24.147  28.961  1.00 31.01 ? 635 HOH C O     1 
HETATM 12846 O O     . HOH Y  8 .   ? -28.237 7.334   -7.175  1.00 52.57 ? 636 HOH C O     1 
HETATM 12847 O O     . HOH Y  8 .   ? -22.034 20.973  30.624  1.00 46.80 ? 637 HOH C O     1 
HETATM 12848 O O     . HOH Y  8 .   ? 5.094   9.417   -4.639  1.00 40.29 ? 638 HOH C O     1 
HETATM 12849 O O     . HOH Y  8 .   ? 18.661  27.316  2.827   1.00 45.42 ? 639 HOH C O     1 
HETATM 12850 O O     . HOH Y  8 .   ? 2.469   18.902  28.197  1.00 35.58 ? 640 HOH C O     1 
HETATM 12851 O O     . HOH Y  8 .   ? -5.339  22.516  -6.854  1.00 27.45 ? 641 HOH C O     1 
HETATM 12852 O O     . HOH Y  8 .   ? 21.090  26.760  -20.954 1.00 41.90 ? 642 HOH C O     1 
HETATM 12853 O O     . HOH Y  8 .   ? 9.228   22.239  16.497  1.00 44.00 ? 643 HOH C O     1 
HETATM 12854 O O     . HOH Y  8 .   ? -0.626  40.415  -8.607  1.00 37.31 ? 644 HOH C O     1 
HETATM 12855 O O     . HOH Y  8 .   ? -19.512 33.589  -4.998  1.00 39.26 ? 645 HOH C O     1 
HETATM 12856 O O     . HOH Y  8 .   ? -8.175  28.967  33.497  1.00 28.23 ? 646 HOH C O     1 
HETATM 12857 O O     . HOH Y  8 .   ? -28.277 16.257  15.278  1.00 38.69 ? 647 HOH C O     1 
HETATM 12858 O O     . HOH Y  8 .   ? -19.964 21.214  11.316  1.00 32.29 ? 648 HOH C O     1 
HETATM 12859 O O     . HOH Y  8 .   ? -32.182 1.822   -7.269  1.00 40.62 ? 649 HOH C O     1 
HETATM 12860 O O     . HOH Y  8 .   ? -16.253 33.268  -12.439 1.00 30.16 ? 650 HOH C O     1 
HETATM 12861 O O     . HOH Y  8 .   ? 0.444   34.708  16.723  1.00 34.86 ? 651 HOH C O     1 
HETATM 12862 O O     . HOH Y  8 .   ? -22.671 20.512  -0.699  1.00 41.37 ? 652 HOH C O     1 
HETATM 12863 O O     . HOH Y  8 .   ? -0.972  10.838  34.457  1.00 39.90 ? 653 HOH C O     1 
HETATM 12864 O O     . HOH Y  8 .   ? 16.718  9.799   -6.210  1.00 28.28 ? 654 HOH C O     1 
HETATM 12865 O O     . HOH Y  8 .   ? 3.089   5.029   -7.268  1.00 44.08 ? 655 HOH C O     1 
HETATM 12866 O O     . HOH Y  8 .   ? -2.237  44.724  -5.960  1.00 43.76 ? 656 HOH C O     1 
HETATM 12867 O O     . HOH Y  8 .   ? -22.487 33.504  34.656  1.00 38.35 ? 657 HOH C O     1 
HETATM 12868 O O     . HOH Y  8 .   ? 0.424   32.349  35.344  1.00 38.07 ? 658 HOH C O     1 
HETATM 12869 O O     . HOH Y  8 .   ? -19.185 33.055  7.638   1.00 30.48 ? 659 HOH C O     1 
HETATM 12870 O O     . HOH Y  8 .   ? 18.817  10.177  -16.779 1.00 32.81 ? 660 HOH C O     1 
HETATM 12871 O O     . HOH Y  8 .   ? -28.936 18.322  16.814  1.00 51.53 ? 661 HOH C O     1 
HETATM 12872 O O     . HOH Y  8 .   ? 20.526  25.324  1.490   1.00 45.77 ? 662 HOH C O     1 
HETATM 12873 O O     . HOH Y  8 .   ? 11.355  18.285  17.483  1.00 48.24 ? 663 HOH C O     1 
HETATM 12874 O O     . HOH Y  8 .   ? -26.945 -1.428  5.501   1.00 47.02 ? 664 HOH C O     1 
HETATM 12875 O O     . HOH Y  8 .   ? 8.284   22.022  14.323  1.00 39.26 ? 665 HOH C O     1 
HETATM 12876 O O     . HOH Y  8 .   ? -18.351 35.713  7.626   1.00 40.64 ? 666 HOH C O     1 
HETATM 12877 O O     . HOH Y  8 .   ? -12.357 -7.676  1.776   1.00 32.24 ? 667 HOH C O     1 
HETATM 12878 O O     . HOH Z  8 .   ? -12.636 15.271  -35.683 1.00 34.19 ? 601 HOH D O     1 
HETATM 12879 O O     . HOH Z  8 .   ? -10.317 6.968   -27.514 1.00 34.13 ? 602 HOH D O     1 
HETATM 12880 O O     . HOH Z  8 .   ? -24.903 -5.639  -37.022 1.00 53.02 ? 603 HOH D O     1 
HETATM 12881 O O     . HOH Z  8 .   ? -8.496  9.758   -48.424 1.00 39.36 ? 604 HOH D O     1 
HETATM 12882 O O     . HOH Z  8 .   ? -6.758  -2.943  -31.028 1.00 48.02 ? 605 HOH D O     1 
HETATM 12883 O O     . HOH Z  8 .   ? -24.121 23.639  -54.342 1.00 42.45 ? 606 HOH D O     1 
HETATM 12884 O O     . HOH Z  8 .   ? -14.027 23.047  -61.258 1.00 31.40 ? 607 HOH D O     1 
HETATM 12885 O O     . HOH Z  8 .   ? -18.449 -3.680  -35.530 1.00 42.46 ? 608 HOH D O     1 
HETATM 12886 O O     . HOH Z  8 .   ? -5.768  -7.167  -34.294 1.00 55.81 ? 609 HOH D O     1 
HETATM 12887 O O     . HOH Z  8 .   ? -3.902  32.168  -41.489 1.00 32.43 ? 610 HOH D O     1 
HETATM 12888 O O     . HOH Z  8 .   ? -31.862 26.387  -30.673 1.00 44.11 ? 611 HOH D O     1 
HETATM 12889 O O     . HOH Z  8 .   ? 3.146   37.146  -57.530 1.00 31.58 ? 612 HOH D O     1 
HETATM 12890 O O     . HOH Z  8 .   ? -13.870 5.539   -11.840 1.00 32.65 ? 613 HOH D O     1 
HETATM 12891 O O     . HOH Z  8 .   ? -2.031  17.090  -53.535 1.00 36.56 ? 614 HOH D O     1 
HETATM 12892 O O     . HOH Z  8 .   ? 3.601   22.457  -26.515 1.00 36.90 ? 615 HOH D O     1 
HETATM 12893 O O     . HOH Z  8 .   ? -1.001  5.869   -48.040 1.00 45.86 ? 616 HOH D O     1 
HETATM 12894 O O     . HOH Z  8 .   ? 4.270   22.648  -58.710 1.00 31.79 ? 617 HOH D O     1 
HETATM 12895 O O     . HOH Z  8 .   ? 1.319   17.446  -31.114 1.00 34.72 ? 618 HOH D O     1 
HETATM 12896 O O     . HOH Z  8 .   ? -18.139 29.175  -55.804 1.00 35.25 ? 619 HOH D O     1 
HETATM 12897 O O     . HOH Z  8 .   ? -6.892  13.076  -12.402 1.00 25.23 ? 620 HOH D O     1 
HETATM 12898 O O     . HOH Z  8 .   ? 7.303   23.836  -25.309 1.00 30.37 ? 621 HOH D O     1 
HETATM 12899 O O     . HOH Z  8 .   ? -12.127 15.590  -24.568 1.00 29.81 ? 622 HOH D O     1 
HETATM 12900 O O     . HOH Z  8 .   ? -15.450 9.546   -26.992 1.00 44.74 ? 623 HOH D O     1 
HETATM 12901 O O     . HOH Z  8 .   ? -5.827  12.958  -27.683 1.00 39.12 ? 624 HOH D O     1 
HETATM 12902 O O     . HOH Z  8 .   ? -14.055 -4.770  -49.204 1.00 55.93 ? 625 HOH D O     1 
HETATM 12903 O O     . HOH Z  8 .   ? -20.968 9.425   -23.204 1.00 37.18 ? 626 HOH D O     1 
HETATM 12904 O O     . HOH Z  8 .   ? 8.285   26.898  -30.682 1.00 33.39 ? 627 HOH D O     1 
HETATM 12905 O O     . HOH Z  8 .   ? -3.717  17.834  -37.978 1.00 35.95 ? 628 HOH D O     1 
HETATM 12906 O O     . HOH Z  8 .   ? -24.492 2.016   -42.309 1.00 36.85 ? 629 HOH D O     1 
HETATM 12907 O O     . HOH Z  8 .   ? 2.544   39.245  -30.003 1.00 43.73 ? 630 HOH D O     1 
HETATM 12908 O O     . HOH Z  8 .   ? -21.068 10.384  -32.458 1.00 32.29 ? 631 HOH D O     1 
HETATM 12909 O O     . HOH Z  8 .   ? -11.941 36.501  -32.163 1.00 30.14 ? 632 HOH D O     1 
HETATM 12910 O O     . HOH Z  8 .   ? -19.195 12.091  -46.653 1.00 34.38 ? 633 HOH D O     1 
HETATM 12911 O O     . HOH Z  8 .   ? -5.291  6.079   -21.299 1.00 40.65 ? 634 HOH D O     1 
HETATM 12912 O O     . HOH Z  8 .   ? -18.613 6.148   -28.087 1.00 25.89 ? 635 HOH D O     1 
HETATM 12913 O O     . HOH Z  8 .   ? 18.521  34.074  -37.647 1.00 49.98 ? 636 HOH D O     1 
HETATM 12914 O O     . HOH Z  8 .   ? -4.674  5.616   -12.723 1.00 35.39 ? 637 HOH D O     1 
HETATM 12915 O O     . HOH Z  8 .   ? -8.677  14.366  -15.950 1.00 30.72 ? 638 HOH D O     1 
HETATM 12916 O O     . HOH Z  8 .   ? -16.999 30.501  -40.237 1.00 34.32 ? 639 HOH D O     1 
HETATM 12917 O O     . HOH Z  8 .   ? 3.855   8.285   -47.097 1.00 36.03 ? 640 HOH D O     1 
HETATM 12918 O O     . HOH Z  8 .   ? 2.922   8.930   -45.368 1.00 43.48 ? 641 HOH D O     1 
HETATM 12919 O O     . HOH Z  8 .   ? -7.003  32.520  -59.823 1.00 41.23 ? 642 HOH D O     1 
HETATM 12920 O O     . HOH Z  8 .   ? -24.746 4.957   -42.626 1.00 31.93 ? 643 HOH D O     1 
HETATM 12921 O O     . HOH Z  8 .   ? -24.507 21.569  -20.240 1.00 30.06 ? 644 HOH D O     1 
HETATM 12922 O O     . HOH Z  8 .   ? -6.294  -2.343  -10.828 1.00 37.05 ? 645 HOH D O     1 
HETATM 12923 O O     . HOH Z  8 .   ? -4.614  32.978  -31.358 1.00 35.85 ? 646 HOH D O     1 
HETATM 12924 O O     . HOH Z  8 .   ? -4.600  9.358   -19.002 1.00 39.73 ? 647 HOH D O     1 
HETATM 12925 O O     . HOH Z  8 .   ? -9.685  33.694  -30.396 1.00 39.50 ? 648 HOH D O     1 
HETATM 12926 O O     . HOH Z  8 .   ? -30.691 4.610   -37.544 1.00 44.56 ? 649 HOH D O     1 
HETATM 12927 O O     . HOH Z  8 .   ? -22.492 8.074   -15.811 1.00 35.75 ? 650 HOH D O     1 
HETATM 12928 O O     . HOH Z  8 .   ? -25.289 30.273  -58.184 1.00 44.32 ? 651 HOH D O     1 
HETATM 12929 O O     . HOH Z  8 .   ? 3.504   31.528  -39.995 1.00 36.45 ? 652 HOH D O     1 
HETATM 12930 O O     . HOH Z  8 .   ? -7.074  -9.859  -32.315 1.00 43.01 ? 653 HOH D O     1 
HETATM 12931 O O     . HOH Z  8 .   ? -7.241  8.112   -63.987 1.00 41.75 ? 654 HOH D O     1 
HETATM 12932 O O     . HOH Z  8 .   ? -26.657 -11.060 -44.880 1.00 43.29 ? 655 HOH D O     1 
HETATM 12933 O O     . HOH Z  8 .   ? -14.912 7.929   -35.277 1.00 35.84 ? 656 HOH D O     1 
HETATM 12934 O O     . HOH Z  8 .   ? -21.731 -7.038  -37.991 1.00 50.21 ? 657 HOH D O     1 
HETATM 12935 O O     . HOH Z  8 .   ? -7.407  32.554  -21.400 1.00 31.12 ? 658 HOH D O     1 
HETATM 12936 O O     . HOH Z  8 .   ? -8.539  8.351   -40.276 1.00 35.51 ? 659 HOH D O     1 
HETATM 12937 O O     . HOH Z  8 .   ? -10.519 37.973  -27.922 1.00 33.35 ? 660 HOH D O     1 
HETATM 12938 O O     . HOH Z  8 .   ? 12.209  20.798  -48.956 1.00 30.00 ? 661 HOH D O     1 
HETATM 12939 O O     . HOH Z  8 .   ? -19.942 -7.048  -36.981 1.00 49.39 ? 662 HOH D O     1 
HETATM 12940 O O     . HOH Z  8 .   ? -15.932 0.921   -11.767 1.00 38.37 ? 663 HOH D O     1 
HETATM 12941 O O     . HOH Z  8 .   ? 2.096   35.202  -17.524 1.00 41.48 ? 664 HOH D O     1 
HETATM 12942 O O     . HOH Z  8 .   ? -40.181 9.200   -28.772 1.00 44.95 ? 665 HOH D O     1 
HETATM 12943 O O     . HOH Z  8 .   ? -21.169 30.694  -55.407 1.00 45.03 ? 666 HOH D O     1 
HETATM 12944 O O     . HOH Z  8 .   ? -10.228 36.371  -21.958 1.00 29.89 ? 667 HOH D O     1 
HETATM 12945 O O     . HOH Z  8 .   ? -8.635  35.876  -23.843 1.00 38.59 ? 668 HOH D O     1 
HETATM 12946 O O     . HOH Z  8 .   ? -11.288 3.226   -5.109  1.00 35.89 ? 669 HOH D O     1 
HETATM 12947 O O     . HOH Z  8 .   ? 3.471   42.337  -34.114 1.00 42.19 ? 670 HOH D O     1 
HETATM 12948 O O     . HOH Z  8 .   ? -24.609 -3.668  -37.721 1.00 63.06 ? 671 HOH D O     1 
HETATM 12949 O O     . HOH Z  8 .   ? -20.905 -9.142  -38.914 1.00 55.24 ? 672 HOH D O     1 
HETATM 12950 O O     . HOH Z  8 .   ? -11.758 40.630  -28.023 1.00 31.94 ? 673 HOH D O     1 
HETATM 12951 O O     . HOH Z  8 .   ? -13.971 30.946  -43.797 1.00 36.10 ? 674 HOH D O     1 
HETATM 12952 O O     . HOH Z  8 .   ? -35.709 22.324  -31.781 1.00 40.78 ? 675 HOH D O     1 
HETATM 12953 O O     . HOH Z  8 .   ? -7.585  -0.885  -10.281 1.00 37.77 ? 676 HOH D O     1 
HETATM 12954 O O     . HOH Z  8 .   ? -6.248  14.099  -15.519 1.00 27.29 ? 677 HOH D O     1 
HETATM 12955 O O     . HOH Z  8 .   ? -8.164  5.498   -39.913 1.00 48.91 ? 678 HOH D O     1 
HETATM 12956 O O     . HOH Z  8 .   ? -8.078  32.525  -31.589 1.00 32.97 ? 679 HOH D O     1 
HETATM 12957 O O     . HOH Z  8 .   ? 3.740   16.088  -26.870 1.00 42.03 ? 680 HOH D O     1 
HETATM 12958 O O     . HOH Z  8 .   ? 13.727  23.282  -48.966 1.00 44.85 ? 681 HOH D O     1 
HETATM 12959 O O     . HOH Z  8 .   ? -26.378 -2.366  -37.726 1.00 44.23 ? 682 HOH D O     1 
HETATM 12960 O O     . HOH Z  8 .   ? -13.668 32.778  -42.288 1.00 40.31 ? 683 HOH D O     1 
HETATM 12961 O O     . HOH Z  8 .   ? 4.475   25.498  -57.311 1.00 36.93 ? 684 HOH D O     1 
HETATM 12962 O O     . HOH Z  8 .   ? 1.067   35.993  -15.895 1.00 33.63 ? 685 HOH D O     1 
HETATM 12963 O O     . HOH Z  8 .   ? -7.018  5.510   -62.181 1.00 35.20 ? 686 HOH D O     1 
HETATM 12964 O O     . HOH Z  8 .   ? -12.909 32.981  -44.359 1.00 31.80 ? 687 HOH D O     1 
HETATM 12965 O O     . HOH Z  8 .   ? -37.210 19.834  -31.000 1.00 35.23 ? 688 HOH D O     1 
HETATM 12966 O O     . HOH Z  8 .   ? -7.237  4.078   -63.975 1.00 44.32 ? 689 HOH D O     1 
HETATM 12967 O O     . HOH Z  8 .   ? 1.896   14.075  -28.084 1.00 38.47 ? 690 HOH D O     1 
HETATM 12968 O O     . HOH AA 8 .   ? -55.294 40.384  19.350  1.00 39.33 ? 601 HOH A O     1 
HETATM 12969 O O     . HOH AA 8 .   ? -67.399 44.775  -5.725  1.00 43.50 ? 602 HOH A O     1 
HETATM 12970 O O     . HOH AA 8 .   ? -38.674 63.318  7.639   1.00 37.92 ? 603 HOH A O     1 
HETATM 12971 O O     . HOH AA 8 .   ? -27.527 55.463  -19.739 1.00 30.71 ? 604 HOH A O     1 
HETATM 12972 O O     . HOH AA 8 .   ? -48.175 47.617  9.504   1.00 45.51 ? 605 HOH A O     1 
HETATM 12973 O O     . HOH AA 8 .   ? -53.835 52.617  -26.216 1.00 34.92 ? 606 HOH A O     1 
HETATM 12974 O O     . HOH AA 8 .   ? -19.118 63.911  -1.308  1.00 36.16 ? 607 HOH A O     1 
HETATM 12975 O O     . HOH AA 8 .   ? -30.212 56.457  3.068   1.00 30.67 ? 608 HOH A O     1 
HETATM 12976 O O     . HOH AA 8 .   ? -31.258 37.882  23.365  1.00 34.83 ? 609 HOH A O     1 
HETATM 12977 O O     . HOH AA 8 .   ? -52.165 52.415  -7.730  1.00 61.69 ? 610 HOH A O     1 
HETATM 12978 O O     . HOH AA 8 .   ? -23.079 70.133  -3.297  1.00 37.53 ? 611 HOH A O     1 
HETATM 12979 O O     . HOH AA 8 .   ? -15.595 65.375  -8.508  1.00 53.73 ? 612 HOH A O     1 
HETATM 12980 O O     . HOH AA 8 .   ? -26.010 58.416  1.237   1.00 33.52 ? 613 HOH A O     1 
HETATM 12981 O O     . HOH AA 8 .   ? -50.614 47.678  -9.232  1.00 42.82 ? 614 HOH A O     1 
HETATM 12982 O O     . HOH AA 8 .   ? -49.310 28.426  2.192   1.00 49.63 ? 615 HOH A O     1 
HETATM 12983 O O     . HOH AA 8 .   ? -36.745 20.265  -13.527 1.00 42.64 ? 616 HOH A O     1 
HETATM 12984 O O     . HOH AA 8 .   ? -25.244 32.193  2.250   1.00 37.09 ? 617 HOH A O     1 
HETATM 12985 O O     . HOH AA 8 .   ? -34.038 30.495  -9.173  1.00 28.13 ? 618 HOH A O     1 
HETATM 12986 O O     . HOH AA 8 .   ? -28.558 45.247  3.742   1.00 22.26 ? 619 HOH A O     1 
HETATM 12987 O O     . HOH AA 8 .   ? -51.467 36.581  -5.596  1.00 37.68 ? 620 HOH A O     1 
HETATM 12988 O O     . HOH AA 8 .   ? -32.407 49.722  -6.833  1.00 21.60 ? 621 HOH A O     1 
HETATM 12989 O O     . HOH AA 8 .   ? -37.653 45.273  2.044   1.00 26.25 ? 622 HOH A O     1 
HETATM 12990 O O     . HOH AA 8 .   ? -24.889 69.043  -12.357 1.00 43.82 ? 623 HOH A O     1 
HETATM 12991 O O     . HOH AA 8 .   ? -23.054 53.582  -5.081  1.00 31.02 ? 624 HOH A O     1 
HETATM 12992 O O     . HOH AA 8 .   ? -29.497 63.692  -7.677  1.00 27.87 ? 625 HOH A O     1 
HETATM 12993 O O     . HOH AA 8 .   ? -17.478 60.841  1.687   1.00 31.15 ? 626 HOH A O     1 
HETATM 12994 O O     . HOH AA 8 .   ? -38.426 70.329  10.751  1.00 45.52 ? 627 HOH A O     1 
HETATM 12995 O O     . HOH AA 8 .   ? -17.253 50.461  4.376   1.00 49.80 ? 628 HOH A O     1 
HETATM 12996 O O     . HOH AA 8 .   ? -38.258 31.297  -17.993 1.00 30.69 ? 629 HOH A O     1 
HETATM 12997 O O     . HOH AA 8 .   ? -46.181 25.129  -4.275  1.00 34.89 ? 630 HOH A O     1 
HETATM 12998 O O     . HOH AA 8 .   ? -43.971 55.482  17.535  1.00 39.26 ? 631 HOH A O     1 
HETATM 12999 O O     . HOH AA 8 .   ? -69.793 35.678  5.358   1.00 46.94 ? 632 HOH A O     1 
HETATM 13000 O O     . HOH AA 8 .   ? -63.793 42.857  -3.060  1.00 42.89 ? 633 HOH A O     1 
HETATM 13001 O O     . HOH AA 8 .   ? -31.622 65.985  6.459   1.00 41.26 ? 634 HOH A O     1 
HETATM 13002 O O     . HOH AA 8 .   ? -43.414 49.236  8.373   1.00 28.26 ? 635 HOH A O     1 
HETATM 13003 O O     . HOH AA 8 .   ? -51.301 49.584  1.644   1.00 47.49 ? 636 HOH A O     1 
HETATM 13004 O O     . HOH AA 8 .   ? -37.131 42.468  20.010  1.00 19.79 ? 637 HOH A O     1 
HETATM 13005 O O     . HOH AA 8 .   ? -19.999 49.909  7.770   1.00 31.56 ? 638 HOH A O     1 
HETATM 13006 O O     . HOH AA 8 .   ? -54.270 47.092  -2.844  1.00 43.51 ? 639 HOH A O     1 
HETATM 13007 O O     . HOH AA 8 .   ? -18.862 56.626  16.904  1.00 34.25 ? 640 HOH A O     1 
HETATM 13008 O O     . HOH AA 8 .   ? -58.045 58.044  -17.562 1.00 44.05 ? 641 HOH A O     1 
HETATM 13009 O O     . HOH AA 8 .   ? -42.528 43.887  -14.471 1.00 33.40 ? 642 HOH A O     1 
HETATM 13010 O O     . HOH AA 8 .   ? -35.709 41.660  21.438  1.00 28.98 ? 643 HOH A O     1 
HETATM 13011 O O     . HOH AA 8 .   ? -26.977 69.162  -12.008 1.00 39.62 ? 644 HOH A O     1 
HETATM 13012 O O     . HOH AA 8 .   ? -43.287 57.277  -18.235 1.00 37.43 ? 645 HOH A O     1 
HETATM 13013 O O     . HOH AA 8 .   ? -52.798 44.248  6.404   1.00 32.90 ? 646 HOH A O     1 
HETATM 13014 O O     . HOH AA 8 .   ? -45.243 57.404  -20.546 1.00 31.26 ? 647 HOH A O     1 
HETATM 13015 O O     . HOH AA 8 .   ? -52.276 42.648  28.036  1.00 51.35 ? 648 HOH A O     1 
HETATM 13016 O O     . HOH AA 8 .   ? -14.825 56.709  4.257   1.00 31.77 ? 649 HOH A O     1 
HETATM 13017 O O     . HOH AA 8 .   ? -58.799 28.689  -10.748 1.00 40.22 ? 650 HOH A O     1 
HETATM 13018 O O     . HOH AA 8 .   ? -22.850 46.257  10.944  1.00 36.34 ? 651 HOH A O     1 
HETATM 13019 O O     . HOH AA 8 .   ? -32.651 31.597  1.605   1.00 23.26 ? 652 HOH A O     1 
HETATM 13020 O O     . HOH AA 8 .   ? -64.607 44.928  -28.307 1.00 24.61 ? 653 HOH A O     1 
HETATM 13021 O O     . HOH AA 8 .   ? -54.631 29.979  -18.238 1.00 36.20 ? 654 HOH A O     1 
HETATM 13022 O O     . HOH AA 8 .   ? -19.854 43.976  -9.520  1.00 44.26 ? 655 HOH A O     1 
HETATM 13023 O O     . HOH AA 8 .   ? -43.287 46.378  -10.912 1.00 33.34 ? 656 HOH A O     1 
HETATM 13024 O O     . HOH AA 8 .   ? -26.805 56.095  -22.668 1.00 37.08 ? 657 HOH A O     1 
HETATM 13025 O O     . HOH AA 8 .   ? -17.015 52.943  16.719  1.00 45.84 ? 658 HOH A O     1 
HETATM 13026 O O     . HOH AA 8 .   ? -36.944 27.944  23.855  1.00 41.34 ? 659 HOH A O     1 
HETATM 13027 O O     . HOH AA 8 .   ? -16.665 66.882  -7.723  1.00 34.77 ? 660 HOH A O     1 
HETATM 13028 O O     . HOH AA 8 .   ? -50.175 61.932  -14.044 1.00 42.09 ? 661 HOH A O     1 
HETATM 13029 O O     . HOH AA 8 .   ? -36.341 67.792  2.900   1.00 41.11 ? 662 HOH A O     1 
HETATM 13030 O O     . HOH AA 8 .   ? -75.650 47.587  -24.046 1.00 37.22 ? 663 HOH A O     1 
HETATM 13031 O O     . HOH AA 8 .   ? -32.318 31.575  -22.367 1.00 32.47 ? 664 HOH A O     1 
HETATM 13032 O O     . HOH AA 8 .   ? -31.820 33.024  -20.755 1.00 26.53 ? 665 HOH A O     1 
HETATM 13033 O O     . HOH AA 8 .   ? -67.856 54.798  -16.519 1.00 40.18 ? 666 HOH A O     1 
HETATM 13034 O O     . HOH AA 8 .   ? -30.015 35.363  -21.270 1.00 29.83 ? 667 HOH A O     1 
HETATM 13035 O O     . HOH AA 8 .   ? -33.701 42.540  26.511  1.00 31.97 ? 668 HOH A O     1 
HETATM 13036 O O     . HOH AA 8 .   ? -23.937 71.142  -12.860 1.00 55.32 ? 669 HOH A O     1 
HETATM 13037 O O     . HOH AA 8 .   ? -35.388 41.068  27.610  1.00 32.76 ? 670 HOH A O     1 
HETATM 13038 O O     . HOH AA 8 .   ? -40.694 30.474  -27.634 1.00 40.64 ? 671 HOH A O     1 
HETATM 13039 O O     . HOH AA 8 .   ? -32.332 42.051  24.832  1.00 32.15 ? 672 HOH A O     1 
HETATM 13040 O O     . HOH AA 8 .   ? -34.139 68.492  1.891   1.00 39.85 ? 673 HOH A O     1 
HETATM 13041 O O     . HOH AA 8 .   ? -56.091 30.245  15.303  1.00 35.68 ? 674 HOH A O     1 
HETATM 13042 O O     . HOH AA 8 .   ? -56.855 32.449  16.602  1.00 34.20 ? 675 HOH A O     1 
HETATM 13043 O O     . HOH BA 8 .   ? -51.541 25.186  -41.778 1.00 52.71 ? 601 HOH B O     1 
HETATM 13044 O O     . HOH BA 8 .   ? -37.571 33.019  -37.422 1.00 32.25 ? 602 HOH B O     1 
HETATM 13045 O O     . HOH BA 8 .   ? -28.188 47.953  -22.669 1.00 56.00 ? 603 HOH B O     1 
HETATM 13046 O O     . HOH BA 8 .   ? -33.300 53.380  -39.363 1.00 29.24 ? 604 HOH B O     1 
HETATM 13047 O O     . HOH BA 8 .   ? -34.194 45.807  -65.740 1.00 32.71 ? 605 HOH B O     1 
HETATM 13048 O O     . HOH BA 8 .   ? -18.899 43.104  -53.085 1.00 34.77 ? 606 HOH B O     1 
HETATM 13049 O O     . HOH BA 8 .   ? -31.342 66.459  -61.276 1.00 49.21 ? 607 HOH B O     1 
HETATM 13050 O O     . HOH BA 8 .   ? -42.936 42.377  -37.325 1.00 34.66 ? 608 HOH B O     1 
HETATM 13051 O O     . HOH BA 8 .   ? -28.245 58.036  -40.221 1.00 47.37 ? 609 HOH B O     1 
HETATM 13052 O O     . HOH BA 8 .   ? -48.814 43.718  -70.710 1.00 45.74 ? 610 HOH B O     1 
HETATM 13053 O O     . HOH BA 8 .   ? -32.804 28.493  -29.090 1.00 42.24 ? 611 HOH B O     1 
HETATM 13054 O O     . HOH BA 8 .   ? -26.208 61.253  -35.541 1.00 34.02 ? 612 HOH B O     1 
HETATM 13055 O O     . HOH BA 8 .   ? -47.009 38.063  -48.586 1.00 34.70 ? 613 HOH B O     1 
HETATM 13056 O O     . HOH BA 8 .   ? -24.159 52.087  -24.499 1.00 32.92 ? 614 HOH B O     1 
HETATM 13057 O O     . HOH BA 8 .   ? -16.818 34.564  -58.315 1.00 56.24 ? 615 HOH B O     1 
HETATM 13058 O O     . HOH BA 8 .   ? -16.902 48.294  -31.126 1.00 28.66 ? 616 HOH B O     1 
HETATM 13059 O O     . HOH BA 8 .   ? -55.419 41.827  -32.904 1.00 42.42 ? 617 HOH B O     1 
HETATM 13060 O O     . HOH BA 8 .   ? -59.892 47.633  -50.332 1.00 43.83 ? 618 HOH B O     1 
HETATM 13061 O O     . HOH BA 8 .   ? -32.363 58.066  -55.369 1.00 48.21 ? 619 HOH B O     1 
HETATM 13062 O O     . HOH BA 8 .   ? -44.741 50.051  -26.369 1.00 27.83 ? 620 HOH B O     1 
HETATM 13063 O O     . HOH BA 8 .   ? -34.262 73.662  -46.134 1.00 54.68 ? 621 HOH B O     1 
HETATM 13064 O O     . HOH BA 8 .   ? -47.740 52.877  -64.364 1.00 35.89 ? 622 HOH B O     1 
HETATM 13065 O O     . HOH BA 8 .   ? -35.908 81.062  -23.123 1.00 54.29 ? 623 HOH B O     1 
HETATM 13066 O O     . HOH BA 8 .   ? -51.594 29.890  -55.045 1.00 46.60 ? 624 HOH B O     1 
HETATM 13067 O O     . HOH BA 8 .   ? -25.388 59.973  -48.220 1.00 31.08 ? 625 HOH B O     1 
HETATM 13068 O O     . HOH BA 8 .   ? -31.637 64.785  -58.667 1.00 55.08 ? 626 HOH B O     1 
HETATM 13069 O O     . HOH BA 8 .   ? -34.226 67.723  -42.855 1.00 54.99 ? 627 HOH B O     1 
HETATM 13070 O O     . HOH BA 8 .   ? -23.752 68.947  -29.676 1.00 41.73 ? 628 HOH B O     1 
HETATM 13071 O O     . HOH BA 8 .   ? -47.395 28.230  -50.185 1.00 46.46 ? 629 HOH B O     1 
HETATM 13072 O O     . HOH BA 8 .   ? -43.532 48.547  -34.534 1.00 30.84 ? 630 HOH B O     1 
HETATM 13073 O O     . HOH BA 8 .   ? -45.258 56.110  -70.339 1.00 40.28 ? 631 HOH B O     1 
HETATM 13074 O O     . HOH BA 8 .   ? -23.057 42.225  -60.819 1.00 39.42 ? 632 HOH B O     1 
HETATM 13075 O O     . HOH BA 8 .   ? -35.132 44.562  -40.600 1.00 29.66 ? 633 HOH B O     1 
HETATM 13076 O O     . HOH BA 8 .   ? -39.446 52.144  -23.862 1.00 26.04 ? 634 HOH B O     1 
HETATM 13077 O O     . HOH BA 8 .   ? -41.374 70.193  -18.398 1.00 42.80 ? 635 HOH B O     1 
HETATM 13078 O O     . HOH BA 8 .   ? -38.353 59.493  -37.659 1.00 38.41 ? 636 HOH B O     1 
HETATM 13079 O O     . HOH BA 8 .   ? -40.194 33.992  -29.050 1.00 34.00 ? 637 HOH B O     1 
HETATM 13080 O O     . HOH BA 8 .   ? -58.578 46.023  -33.513 1.00 38.10 ? 638 HOH B O     1 
HETATM 13081 O O     . HOH BA 8 .   ? -48.357 43.625  -40.722 1.00 27.62 ? 639 HOH B O     1 
HETATM 13082 O O     . HOH BA 8 .   ? -38.737 56.547  -69.355 1.00 33.16 ? 640 HOH B O     1 
HETATM 13083 O O     . HOH BA 8 .   ? -36.375 68.954  -45.090 1.00 48.01 ? 641 HOH B O     1 
HETATM 13084 O O     . HOH BA 8 .   ? -36.940 58.845  -45.614 1.00 40.83 ? 642 HOH B O     1 
HETATM 13085 O O     . HOH BA 8 .   ? -23.147 71.149  -44.763 1.00 50.02 ? 643 HOH B O     1 
HETATM 13086 O O     . HOH BA 8 .   ? -9.459  43.521  -32.596 1.00 47.50 ? 644 HOH B O     1 
HETATM 13087 O O     . HOH BA 8 .   ? -47.772 29.333  -52.035 1.00 31.06 ? 645 HOH B O     1 
HETATM 13088 O O     . HOH BA 8 .   ? -28.623 64.782  -19.355 1.00 42.19 ? 646 HOH B O     1 
HETATM 13089 O O     . HOH BA 8 .   ? -40.132 39.041  -40.113 1.00 26.63 ? 647 HOH B O     1 
HETATM 13090 O O     . HOH BA 8 .   ? -30.256 56.992  -39.924 1.00 21.08 ? 648 HOH B O     1 
HETATM 13091 O O     . HOH BA 8 .   ? -26.666 69.503  -48.565 1.00 47.79 ? 649 HOH B O     1 
HETATM 13092 O O     . HOH BA 8 .   ? -52.620 25.850  -32.870 1.00 42.67 ? 650 HOH B O     1 
HETATM 13093 O O     . HOH BA 8 .   ? -32.125 31.730  -66.354 1.00 38.47 ? 651 HOH B O     1 
HETATM 13094 O O     . HOH BA 8 .   ? -44.951 56.121  -24.653 1.00 33.81 ? 652 HOH B O     1 
HETATM 13095 O O     . HOH BA 8 .   ? -57.654 47.443  -35.683 1.00 40.09 ? 653 HOH B O     1 
HETATM 13096 O O     . HOH BA 8 .   ? -34.400 50.840  -44.263 1.00 32.15 ? 654 HOH B O     1 
HETATM 13097 O O     . HOH BA 8 .   ? -63.030 41.703  -36.546 1.00 40.91 ? 655 HOH B O     1 
HETATM 13098 O O     . HOH BA 8 .   ? -56.461 46.745  -34.107 1.00 39.25 ? 656 HOH B O     1 
HETATM 13099 O O     . HOH BA 8 .   ? -12.287 46.097  -35.264 1.00 41.11 ? 657 HOH B O     1 
HETATM 13100 O O     . HOH BA 8 .   ? -41.221 52.912  -19.705 1.00 23.03 ? 658 HOH B O     1 
HETATM 13101 O O     . HOH BA 8 .   ? -25.273 70.987  -50.476 1.00 26.10 ? 659 HOH B O     1 
HETATM 13102 O O     . HOH BA 8 .   ? -53.876 21.750  -42.886 1.00 53.65 ? 660 HOH B O     1 
HETATM 13103 O O     . HOH BA 8 .   ? -55.508 30.755  -60.940 1.00 37.54 ? 661 HOH B O     1 
HETATM 13104 O O     . HOH BA 8 .   ? -50.561 46.409  -70.821 1.00 45.42 ? 662 HOH B O     1 
HETATM 13105 O O     . HOH BA 8 .   ? -31.978 58.279  -39.238 1.00 34.45 ? 663 HOH B O     1 
HETATM 13106 O O     . HOH BA 8 .   ? -38.107 28.395  -35.798 1.00 45.31 ? 664 HOH B O     1 
HETATM 13107 O O     . HOH BA 8 .   ? -46.297 49.824  -69.778 1.00 39.31 ? 665 HOH B O     1 
HETATM 13108 O O     . HOH BA 8 .   ? -35.396 50.583  -31.415 1.00 32.29 ? 666 HOH B O     1 
HETATM 13109 O O     . HOH BA 8 .   ? -43.209 64.675  -41.299 1.00 40.60 ? 667 HOH B O     1 
HETATM 13110 O O     . HOH BA 8 .   ? -54.069 25.761  -52.138 1.00 37.80 ? 668 HOH B O     1 
HETATM 13111 O O     . HOH BA 8 .   ? -23.760 34.557  -65.770 1.00 34.52 ? 669 HOH B O     1 
HETATM 13112 O O     . HOH BA 8 .   ? -43.090 29.009  -46.467 1.00 35.65 ? 670 HOH B O     1 
HETATM 13113 O O     . HOH BA 8 .   ? -39.045 57.498  -72.916 1.00 44.24 ? 671 HOH B O     1 
HETATM 13114 O O     . HOH BA 8 .   ? -61.908 45.692  -59.902 1.00 56.80 ? 672 HOH B O     1 
HETATM 13115 O O     . HOH BA 8 .   ? -43.494 56.600  -26.236 1.00 37.04 ? 673 HOH B O     1 
HETATM 13116 O O     . HOH BA 8 .   ? -42.547 34.044  -28.458 1.00 26.65 ? 674 HOH B O     1 
HETATM 13117 O O     . HOH BA 8 .   ? -26.238 35.675  -33.006 1.00 33.94 ? 675 HOH B O     1 
HETATM 13118 O O     . HOH BA 8 .   ? -38.457 35.463  -50.233 1.00 39.30 ? 676 HOH B O     1 
HETATM 13119 O O     . HOH BA 8 .   ? -32.172 76.243  -39.193 1.00 45.77 ? 677 HOH B O     1 
HETATM 13120 O O     . HOH BA 8 .   ? -32.291 64.456  -67.667 1.00 45.61 ? 678 HOH B O     1 
HETATM 13121 O O     . HOH BA 8 .   ? -34.519 42.590  -67.923 1.00 51.89 ? 679 HOH B O     1 
HETATM 13122 O O     . HOH BA 8 .   ? -16.977 53.446  -29.918 1.00 40.94 ? 680 HOH B O     1 
HETATM 13123 O O     . HOH BA 8 .   ? -35.881 32.276  -57.893 1.00 43.80 ? 681 HOH B O     1 
HETATM 13124 O O     . HOH BA 8 .   ? -38.739 30.037  -27.917 1.00 43.48 ? 682 HOH B O     1 
HETATM 13125 O O     . HOH BA 8 .   ? -40.882 31.431  -30.778 1.00 39.33 ? 683 HOH B O     1 
HETATM 13126 O O     . HOH BA 8 .   ? -39.072 57.863  -47.531 1.00 32.72 ? 684 HOH B O     1 
HETATM 13127 O O     . HOH BA 8 .   ? -37.523 59.222  -49.049 1.00 39.08 ? 685 HOH B O     1 
HETATM 13128 O O     . HOH BA 8 .   ? -8.149  57.438  -36.554 1.00 36.81 ? 686 HOH B O     1 
HETATM 13129 O O     . HOH BA 8 .   ? -45.056 26.635  -45.628 1.00 39.71 ? 687 HOH B O     1 
HETATM 13130 O O     . HOH BA 8 .   ? -7.461  58.141  -39.011 1.00 35.01 ? 688 HOH B O     1 
HETATM 13131 O O     . HOH BA 8 .   ? -43.517 48.635  -46.790 1.00 32.96 ? 689 HOH B O     1 
HETATM 13132 O O     . HOH BA 8 .   ? -24.173 73.019  -51.540 1.00 28.44 ? 690 HOH B O     1 
HETATM 13133 O O     . HOH BA 8 .   ? -45.088 49.391  -44.822 1.00 30.64 ? 691 HOH B O     1 
HETATM 13134 O O     . HOH BA 8 .   ? -25.468 73.546  -49.909 1.00 47.34 ? 692 HOH B O     1 
HETATM 13135 O O     . HOH BA 8 .   ? -27.104 74.499  -48.085 1.00 40.49 ? 693 HOH B O     1 
# 
