data_4UTC
# 
_entry.id   4UTC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4UTC         
PDBE  EBI-61244    
WWPDB D_1290061244 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 4UTA unspecified 
;CRYSTAL STRUCTURE OF DENGUE 2 VIRUS ENVELOPE GLYCOPROTEIN IN COMPLEX WITH THE FAB FRAGMENT OF THE BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C8
;
PDB 4UTB unspecified 
;CRYSTAL STRUCTURE OF DENGUE 2 VIRUS ENVELOPE GLYCOPROTEIN IN COMPLEX WITH THE FAB FRAGMENT OF THE BROADLY NEUTRALIZING HUMAN ANTIBODY EDE2 A11
;
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4UTC 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2014-07-18 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Kikuti, C.'         1 
'Rouvinski, A.'      2 
'Guardado-Calvo, P.' 3 
'Barba-Spaeth, G.'   4 
'Duquerroy, S.'      5 
'Vaney, M.C.'        6 
'Rey, F.A.'          7 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 'Recognition Determinants of Broadly Neutralizing Human Antibodies Against Dengue Viruses.'                                
Nature       520 109 ? 2015 NATUAS UK 0028-0836 0006 ? 25581790 10.1038/NATURE14130 
1       'A New Class of Highly Potent, Broadly Neutralizing Antibodies Isolated from Viremic Patients Infected with Dengue Virus.' 
Nat.Immunol. 16  170 ? 2015 ?      UK 1529-2908 ?    ? 25501631 10.1038/NI.3058     
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Rouvinski, A.'          1  
primary 'Guardado-Calvo, P.'     2  
primary 'Barba-Spaeth, G.'       3  
primary 'Duquerroy, S.'          4  
primary 'Vaney, M.'              5  
primary 'Kikuti, C.M.'           6  
primary 'Sanchez, M.E.N.'        7  
primary 'Dejnirattisai, W.'      8  
primary 'Wongwiwat, W.'          9  
primary 'Haouz, A.'              10 
primary 'Girard-Blanc, C.'       11 
primary 'Petres, S.'             12 
primary 'Shepard, W.E.'          13 
primary 'Despres, P.'            14 
primary 'Arenzana-Seisdedos, F.' 15 
primary 'Dussart, P.'            16 
primary 'Mongkolsapaya, J.'      17 
primary 'Screaton, G.R.'         18 
primary 'Rey, F.A.'              19 
1       'Dejnirattisai, W.'      20 
1       'Wongwiwat, W.'          21 
1       'Supasa, S.'             22 
1       'Zhang, X.'              23 
1       'Dai, X.'                24 
1       'Rouvinsky, A.'          25 
1       'Jumnainsong, A.'        26 
1       'Edwards, C.'            27 
1       'Quyen, N.T.H.'          28 
1       'Duangchinda, T.'        29 
1       'Grimes, J.M.'           30 
1       'Tsai, W.'               31 
1       'Lai, C.'                32 
1       'Wang, W.'               33 
1       'Malasit, P.'            34 
1       'Farrar, J.'             35 
1       'Simmons, C.P.'          36 
1       'Zhou, Z.H.'             37 
1       'Rey, F.A.'              38 
1       'Mongkolsapaya, J.'      39 
1       'Screaton, G.R.'         40 
# 
_cell.entry_id           4UTC 
_cell.length_a           105.462 
_cell.length_b           105.462 
_cell.length_c           165.895 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         4UTC 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
# 
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 'ENVELOPE GLYCOPROTEIN E' 46816.547 2 ? ? 'SOLUBLE ECTODOMAIN, RESIDUES 281-671' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE    221.208   8 ? ? ?                                      ? 
3 non-polymer man ALPHA-L-FUCOSE            164.156   2 ? ? ?                                      ? 
4 non-polymer man BETA-D-MANNOSE            180.156   3 ? ? ?                                      ? 
5 water       nat water                     18.015    6 ? ? ?                                      ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'E PROTEIN' 
# 
_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       
;MRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEP
SLNEEQDKRFICKHSMVDRGWGNGCGLFGKGGIVTCAKFTCKKNMEGKIVQPENLEYTIVITPHSGEEHAVGNDTGKHGK
EIKITPQSSTTEAELTGYGTVTMECSPRTGLDFNEMVLLQMEDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTF
KNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKIVKEIAETQHGTI
VIRVQYEGDGSPCKIPFEITDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIVGVEPGQLKLNWLRPLESRGP
FEGKPIPNPLLGLDSTRTGHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEP
SLNEEQDKRFICKHSMVDRGWGNGCGLFGKGGIVTCAKFTCKKNMEGKIVQPENLEYTIVITPHSGEEHAVGNDTGKHGK
EIKITPQSSTTEAELTGYGTVTMECSPRTGLDFNEMVLLQMEDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTF
KNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKIVKEIAETQHGTI
VIRVQYEGDGSPCKIPFEITDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIVGVEPGQLKLNWLRPLESRGP
FEGKPIPNPLLGLDSTRTGHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
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   ARG n 
1 3   CYS n 
1 4   ILE n 
1 5   GLY n 
1 6   ILE n 
1 7   SER n 
1 8   ASN n 
1 9   ARG n 
1 10  ASP n 
1 11  PHE n 
1 12  VAL n 
1 13  GLU n 
1 14  GLY n 
1 15  VAL n 
1 16  SER n 
1 17  GLY n 
1 18  GLY n 
1 19  SER n 
1 20  TRP n 
1 21  VAL n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  LEU n 
1 26  GLU n 
1 27  HIS n 
1 28  GLY n 
1 29  SER n 
1 30  CYS n 
1 31  VAL n 
1 32  THR n 
1 33  THR n 
1 34  MET n 
1 35  ALA n 
1 36  LYS n 
1 37  ASN n 
1 38  LYS n 
1 39  PRO n 
1 40  THR n 
1 41  LEU n 
1 42  ASP n 
1 43  PHE n 
1 44  GLU n 
1 45  LEU n 
1 46  ILE n 
1 47  LYS n 
1 48  THR n 
1 49  GLU n 
1 50  ALA n 
1 51  LYS n 
1 52  GLN n 
1 53  PRO n 
1 54  ALA n 
1 55  THR n 
1 56  LEU n 
1 57  ARG n 
1 58  LYS n 
1 59  TYR n 
1 60  CYS n 
1 61  ILE n 
1 62  GLU n 
1 63  ALA n 
1 64  LYS n 
1 65  LEU n 
1 66  THR n 
1 67  ASN n 
1 68  THR n 
1 69  THR n 
1 70  THR n 
1 71  GLU n 
1 72  SER n 
1 73  ARG n 
1 74  CYS n 
1 75  PRO n 
1 76  THR n 
1 77  GLN n 
1 78  GLY n 
1 79  GLU n 
1 80  PRO n 
1 81  SER n 
1 82  LEU n 
1 83  ASN n 
1 84  GLU n 
1 85  GLU n 
1 86  GLN n 
1 87  ASP n 
1 88  LYS n 
1 89  ARG n 
1 90  PHE n 
1 91  ILE n 
1 92  CYS n 
1 93  LYS n 
1 94  HIS n 
1 95  SER n 
1 96  MET n 
1 97  VAL n 
1 98  ASP n 
1 99  ARG n 
1 100 GLY n 
1 101 TRP n 
1 102 GLY n 
1 103 ASN n 
1 104 GLY n 
1 105 CYS n 
1 106 GLY n 
1 107 LEU n 
1 108 PHE n 
1 109 GLY n 
1 110 LYS n 
1 111 GLY n 
1 112 GLY n 
1 113 ILE n 
1 114 VAL n 
1 115 THR n 
1 116 CYS n 
1 117 ALA n 
1 118 LYS n 
1 119 PHE n 
1 120 THR n 
1 121 CYS n 
1 122 LYS n 
1 123 LYS n 
1 124 ASN n 
1 125 MET n 
1 126 GLU n 
1 127 GLY n 
1 128 LYS n 
1 129 ILE n 
1 130 VAL n 
1 131 GLN n 
1 132 PRO n 
1 133 GLU n 
1 134 ASN n 
1 135 LEU n 
1 136 GLU n 
1 137 TYR n 
1 138 THR n 
1 139 ILE n 
1 140 VAL n 
1 141 ILE n 
1 142 THR n 
1 143 PRO n 
1 144 HIS n 
1 145 SER n 
1 146 GLY n 
1 147 GLU n 
1 148 GLU n 
1 149 HIS n 
1 150 ALA n 
1 151 VAL n 
1 152 GLY n 
1 153 ASN n 
1 154 ASP n 
1 155 THR n 
1 156 GLY n 
1 157 LYS n 
1 158 HIS n 
1 159 GLY n 
1 160 LYS n 
1 161 GLU n 
1 162 ILE n 
1 163 LYS n 
1 164 ILE n 
1 165 THR n 
1 166 PRO n 
1 167 GLN n 
1 168 SER n 
1 169 SER n 
1 170 THR n 
1 171 THR n 
1 172 GLU n 
1 173 ALA n 
1 174 GLU n 
1 175 LEU n 
1 176 THR n 
1 177 GLY n 
1 178 TYR n 
1 179 GLY n 
1 180 THR n 
1 181 VAL n 
1 182 THR n 
1 183 MET n 
1 184 GLU n 
1 185 CYS n 
1 186 SER n 
1 187 PRO n 
1 188 ARG n 
1 189 THR n 
1 190 GLY n 
1 191 LEU n 
1 192 ASP n 
1 193 PHE n 
1 194 ASN n 
1 195 GLU n 
1 196 MET n 
1 197 VAL n 
1 198 LEU n 
1 199 LEU n 
1 200 GLN n 
1 201 MET n 
1 202 GLU n 
1 203 ASP n 
1 204 LYS n 
1 205 ALA n 
1 206 TRP n 
1 207 LEU n 
1 208 VAL n 
1 209 HIS n 
1 210 ARG n 
1 211 GLN n 
1 212 TRP n 
1 213 PHE n 
1 214 LEU n 
1 215 ASP n 
1 216 LEU n 
1 217 PRO n 
1 218 LEU n 
1 219 PRO n 
1 220 TRP n 
1 221 LEU n 
1 222 PRO n 
1 223 GLY n 
1 224 ALA n 
1 225 ASP n 
1 226 THR n 
1 227 GLN n 
1 228 GLY n 
1 229 SER n 
1 230 ASN n 
1 231 TRP n 
1 232 ILE n 
1 233 GLN n 
1 234 LYS n 
1 235 GLU n 
1 236 THR n 
1 237 LEU n 
1 238 VAL n 
1 239 THR n 
1 240 PHE n 
1 241 LYS n 
1 242 ASN n 
1 243 PRO n 
1 244 HIS n 
1 245 ALA n 
1 246 LYS n 
1 247 LYS n 
1 248 GLN n 
1 249 ASP n 
1 250 VAL n 
1 251 VAL n 
1 252 VAL n 
1 253 LEU n 
1 254 GLY n 
1 255 SER n 
1 256 GLN n 
1 257 GLU n 
1 258 GLY n 
1 259 ALA n 
1 260 MET n 
1 261 HIS n 
1 262 THR n 
1 263 ALA n 
1 264 LEU n 
1 265 THR n 
1 266 GLY n 
1 267 ALA n 
1 268 THR n 
1 269 GLU n 
1 270 ILE n 
1 271 GLN n 
1 272 MET n 
1 273 SER n 
1 274 SER n 
1 275 GLY n 
1 276 ASN n 
1 277 LEU n 
1 278 LEU n 
1 279 PHE n 
1 280 THR n 
1 281 GLY n 
1 282 HIS n 
1 283 LEU n 
1 284 LYS n 
1 285 CYS n 
1 286 ARG n 
1 287 LEU n 
1 288 ARG n 
1 289 MET n 
1 290 ASP n 
1 291 LYS n 
1 292 LEU n 
1 293 GLN n 
1 294 LEU n 
1 295 LYS n 
1 296 GLY n 
1 297 MET n 
1 298 SER n 
1 299 TYR n 
1 300 SER n 
1 301 MET n 
1 302 CYS n 
1 303 THR n 
1 304 GLY n 
1 305 LYS n 
1 306 PHE n 
1 307 LYS n 
1 308 ILE n 
1 309 VAL n 
1 310 LYS n 
1 311 GLU n 
1 312 ILE n 
1 313 ALA n 
1 314 GLU n 
1 315 THR n 
1 316 GLN n 
1 317 HIS n 
1 318 GLY n 
1 319 THR n 
1 320 ILE n 
1 321 VAL n 
1 322 ILE n 
1 323 ARG n 
1 324 VAL n 
1 325 GLN n 
1 326 TYR n 
1 327 GLU n 
1 328 GLY n 
1 329 ASP n 
1 330 GLY n 
1 331 SER n 
1 332 PRO n 
1 333 CYS n 
1 334 LYS n 
1 335 ILE n 
1 336 PRO n 
1 337 PHE n 
1 338 GLU n 
1 339 ILE n 
1 340 THR n 
1 341 ASP n 
1 342 LEU n 
1 343 GLU n 
1 344 LYS n 
1 345 ARG n 
1 346 HIS n 
1 347 VAL n 
1 348 LEU n 
1 349 GLY n 
1 350 ARG n 
1 351 LEU n 
1 352 ILE n 
1 353 THR n 
1 354 VAL n 
1 355 ASN n 
1 356 PRO n 
1 357 ILE n 
1 358 VAL n 
1 359 THR n 
1 360 GLU n 
1 361 LYS n 
1 362 ASP n 
1 363 SER n 
1 364 PRO n 
1 365 VAL n 
1 366 ASN n 
1 367 ILE n 
1 368 GLU n 
1 369 ALA n 
1 370 GLU n 
1 371 PRO n 
1 372 PRO n 
1 373 PHE n 
1 374 GLY n 
1 375 ASP n 
1 376 SER n 
1 377 TYR n 
1 378 ILE n 
1 379 ILE n 
1 380 VAL n 
1 381 GLY n 
1 382 VAL n 
1 383 GLU n 
1 384 PRO n 
1 385 GLY n 
1 386 GLN n 
1 387 LEU n 
1 388 LYS n 
1 389 LEU n 
1 390 ASN n 
1 391 TRP n 
1 392 LEU n 
1 393 ARG n 
1 394 PRO n 
1 395 LEU n 
1 396 GLU n 
1 397 SER n 
1 398 ARG n 
1 399 GLY n 
1 400 PRO n 
1 401 PHE n 
1 402 GLU n 
1 403 GLY n 
1 404 LYS n 
1 405 PRO n 
1 406 ILE n 
1 407 PRO n 
1 408 ASN n 
1 409 PRO n 
1 410 LEU n 
1 411 LEU n 
1 412 GLY n 
1 413 LEU n 
1 414 ASP n 
1 415 SER n 
1 416 THR n 
1 417 ARG n 
1 418 THR n 
1 419 GLY n 
1 420 HIS n 
1 421 HIS n 
1 422 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    FGA-02 
_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      'DENGUE VIRUS 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     11060 
_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               'FRUIT FLY' 
_entity_src_gen.pdbx_host_org_scientific_name      'DROSOPHILA MELANOGASTER' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7227 
_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            'SCHNEIDER 2' 
_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                       PMT/BIP/V5-HIS 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q68Y26_9FLAV 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          Q68Y26 
_struct_ref.pdbx_db_isoform            ? 
# 
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 4UTC A 1 ? 391 ? Q68Y26 281 ? 671 ? 1 391 
2 1 4UTC B 1 ? 391 ? Q68Y26 281 ? 671 ? 1 391 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 4UTC LEU A 392 ? UNP Q68Y26 ?   ?   'expression tag' 392 1  
1 4UTC ARG A 393 ? UNP Q68Y26 ?   ?   'expression tag' 393 2  
1 4UTC PRO A 394 ? UNP Q68Y26 ?   ?   'expression tag' 394 3  
1 4UTC LEU A 395 ? UNP Q68Y26 ?   ?   'expression tag' 395 4  
1 4UTC GLU A 396 ? UNP Q68Y26 ?   ?   'expression tag' 396 5  
1 4UTC SER A 397 ? UNP Q68Y26 ?   ?   'expression tag' 397 6  
1 4UTC ARG A 398 ? UNP Q68Y26 ?   ?   'expression tag' 398 7  
1 4UTC GLY A 399 ? UNP Q68Y26 ?   ?   'expression tag' 399 8  
1 4UTC PRO A 400 ? UNP Q68Y26 ?   ?   'expression tag' 400 9  
1 4UTC PHE A 401 ? UNP Q68Y26 ?   ?   'expression tag' 401 10 
1 4UTC GLU A 402 ? UNP Q68Y26 ?   ?   'expression tag' 402 11 
1 4UTC GLY A 403 ? UNP Q68Y26 ?   ?   'expression tag' 403 12 
1 4UTC LYS A 404 ? UNP Q68Y26 ?   ?   'expression tag' 404 13 
1 4UTC PRO A 405 ? UNP Q68Y26 ?   ?   'expression tag' 405 14 
1 4UTC ILE A 406 ? UNP Q68Y26 ?   ?   'expression tag' 406 15 
1 4UTC PRO A 407 ? UNP Q68Y26 ?   ?   'expression tag' 407 16 
1 4UTC ASN A 408 ? UNP Q68Y26 ?   ?   'expression tag' 408 17 
1 4UTC PRO A 409 ? UNP Q68Y26 ?   ?   'expression tag' 409 18 
1 4UTC LEU A 410 ? UNP Q68Y26 ?   ?   'expression tag' 410 19 
1 4UTC LEU A 411 ? UNP Q68Y26 ?   ?   'expression tag' 411 20 
1 4UTC GLY A 412 ? UNP Q68Y26 ?   ?   'expression tag' 412 21 
1 4UTC LEU A 413 ? UNP Q68Y26 ?   ?   'expression tag' 413 22 
1 4UTC ASP A 414 ? UNP Q68Y26 ?   ?   'expression tag' 414 23 
1 4UTC SER A 415 ? UNP Q68Y26 ?   ?   'expression tag' 415 24 
1 4UTC THR A 416 ? UNP Q68Y26 ?   ?   'expression tag' 416 25 
1 4UTC ARG A 417 ? UNP Q68Y26 ?   ?   'expression tag' 417 26 
1 4UTC THR A 418 ? UNP Q68Y26 ?   ?   'expression tag' 418 27 
1 4UTC GLY A 419 ? UNP Q68Y26 ?   ?   'expression tag' 419 28 
1 4UTC HIS A 420 ? UNP Q68Y26 ?   ?   'expression tag' 420 29 
1 4UTC HIS A 421 ? UNP Q68Y26 ?   ?   'expression tag' 421 30 
1 4UTC HIS A 422 ? UNP Q68Y26 ?   ?   'expression tag' 422 31 
1 4UTC LYS A 118 ? UNP Q68Y26 MET 398 conflict         118 32 
2 4UTC LEU B 392 ? UNP Q68Y26 ?   ?   'expression tag' 392 33 
2 4UTC ARG B 393 ? UNP Q68Y26 ?   ?   'expression tag' 393 34 
2 4UTC PRO B 394 ? UNP Q68Y26 ?   ?   'expression tag' 394 35 
2 4UTC LEU B 395 ? UNP Q68Y26 ?   ?   'expression tag' 395 36 
2 4UTC GLU B 396 ? UNP Q68Y26 ?   ?   'expression tag' 396 37 
2 4UTC SER B 397 ? UNP Q68Y26 ?   ?   'expression tag' 397 38 
2 4UTC ARG B 398 ? UNP Q68Y26 ?   ?   'expression tag' 398 39 
2 4UTC GLY B 399 ? UNP Q68Y26 ?   ?   'expression tag' 399 40 
2 4UTC PRO B 400 ? UNP Q68Y26 ?   ?   'expression tag' 400 41 
2 4UTC PHE B 401 ? UNP Q68Y26 ?   ?   'expression tag' 401 42 
2 4UTC GLU B 402 ? UNP Q68Y26 ?   ?   'expression tag' 402 43 
2 4UTC GLY B 403 ? UNP Q68Y26 ?   ?   'expression tag' 403 44 
2 4UTC LYS B 404 ? UNP Q68Y26 ?   ?   'expression tag' 404 45 
2 4UTC PRO B 405 ? UNP Q68Y26 ?   ?   'expression tag' 405 46 
2 4UTC ILE B 406 ? UNP Q68Y26 ?   ?   'expression tag' 406 47 
2 4UTC PRO B 407 ? UNP Q68Y26 ?   ?   'expression tag' 407 48 
2 4UTC ASN B 408 ? UNP Q68Y26 ?   ?   'expression tag' 408 49 
2 4UTC PRO B 409 ? UNP Q68Y26 ?   ?   'expression tag' 409 50 
2 4UTC LEU B 410 ? UNP Q68Y26 ?   ?   'expression tag' 410 51 
2 4UTC LEU B 411 ? UNP Q68Y26 ?   ?   'expression tag' 411 52 
2 4UTC GLY B 412 ? UNP Q68Y26 ?   ?   'expression tag' 412 53 
2 4UTC LEU B 413 ? UNP Q68Y26 ?   ?   'expression tag' 413 54 
2 4UTC ASP B 414 ? UNP Q68Y26 ?   ?   'expression tag' 414 55 
2 4UTC SER B 415 ? UNP Q68Y26 ?   ?   'expression tag' 415 56 
2 4UTC THR B 416 ? UNP Q68Y26 ?   ?   'expression tag' 416 57 
2 4UTC ARG B 417 ? UNP Q68Y26 ?   ?   'expression tag' 417 58 
2 4UTC THR B 418 ? UNP Q68Y26 ?   ?   'expression tag' 418 59 
2 4UTC GLY B 419 ? UNP Q68Y26 ?   ?   'expression tag' 419 60 
2 4UTC HIS B 420 ? UNP Q68Y26 ?   ?   'expression tag' 420 61 
2 4UTC HIS B 421 ? UNP Q68Y26 ?   ?   'expression tag' 421 62 
2 4UTC HIS B 422 ? UNP Q68Y26 ?   ?   'expression tag' 422 63 
2 4UTC LYS B 118 ? UNP Q68Y26 MET 398 conflict         118 64 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
BMA D-saccharide        . BETA-D-MANNOSE         ? 'C6 H12 O6'      180.156 
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
FUC saccharide          . ALPHA-L-FUCOSE         ? 'C6 H12 O5'      164.156 
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                  ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE             ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE              ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          4UTC 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.45 
_exptl_crystal.density_percent_sol   49.8 
_exptl_crystal.description           NONE 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '100MM TRIS PH 8.0 86 MM NAFORMATE 16% PEG 3,350' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MARMOSAIC 225 mm CCD' 
_diffrn_detector.pdbx_collection_date   2008-09-27 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.872600 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID23-2' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID23-2 
_diffrn_source.pdbx_wavelength             0.872600 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4UTC 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.00 
_reflns.d_resolution_high            3.10 
_reflns.number_obs                   17615 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.3 
_reflns.pdbx_Rmerge_I_obs            0.10 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        23.90 
_reflns.B_iso_Wilson_estimate        95.31 
_reflns.pdbx_redundancy              17.1 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             3.10 
_reflns_shell.d_res_low              3.26 
_reflns_shell.percent_possible_all   96.0 
_reflns_shell.Rmerge_I_obs           0.61 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.50 
_reflns_shell.pdbx_redundancy        6.5 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4UTC 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     17453 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             20.00 
_refine.ls_d_res_high                            3.08 
_refine.ls_percent_reflns_obs                    97.54 
_refine.ls_R_factor_obs                          0.2140 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2106 
_refine.ls_R_factor_R_free                       0.2788 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_number_reflns_R_free                  882 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.9254 
_refine.correlation_coeff_Fo_to_Fc_free          0.8736 
_refine.B_iso_mean                               85.62 
_refine.aniso_B[1][1]                            0.7469 
_refine.aniso_B[2][2]                            0.7469 
_refine.aniso_B[3][3]                            -1.4938 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  
'IDEAL-DIST CONTACT TERM CONTACT SETUP. ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY' 
_refine.pdbx_starting_model                      'PDB ENTRY 1OAN' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.512 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        4UTC 
_refine_analyze.Luzzati_coordinate_error_obs    0.585 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6072 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         165 
_refine_hist.number_atoms_solvent             6 
_refine_hist.number_atoms_total               6243 
_refine_hist.d_res_high                       3.08 
_refine_hist.d_res_low                        20.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.010 ? 2.00  6383 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.33  ? 2.00  8659 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  2295 'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? 2.00  158  'X-RAY DIFFRACTION' HARMONIC     
t_gen_planes              ?     ? 5.00  891  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 20.00 6383 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           2.70  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           22.12 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  895  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  6819 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   9 
_refine_ls_shell.d_res_high                       3.08 
_refine_ls_shell.d_res_low                        3.27 
_refine_ls_shell.number_reflns_R_work             2275 
_refine_ls_shell.R_factor_R_work                  0.2540 
_refine_ls_shell.percent_reflns_obs               97.54 
_refine_ls_shell.R_factor_R_free                  0.3370 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.41 
_refine_ls_shell.number_reflns_R_free             130 
_refine_ls_shell.number_reflns_all                2405 
_refine_ls_shell.R_factor_all                     0.2588 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.details        ? 
_struct_ncs_oper.matrix[1][1]   -0.172000 
_struct_ncs_oper.matrix[1][2]   0.890000 
_struct_ncs_oper.matrix[1][3]   -0.422000 
_struct_ncs_oper.matrix[2][1]   0.897000 
_struct_ncs_oper.matrix[2][2]   -0.035000 
_struct_ncs_oper.matrix[2][3]   -0.440000 
_struct_ncs_oper.matrix[3][1]   -0.406000 
_struct_ncs_oper.matrix[3][2]   -0.454000 
_struct_ncs_oper.matrix[3][3]   -0.793000 
_struct_ncs_oper.vector[1]      -0.57200 
_struct_ncs_oper.vector[2]      -37.68400 
_struct_ncs_oper.vector[3]      -83.16500 
# 
_struct.entry_id                  4UTC 
_struct.title                     'Crystal structure of dengue 2 virus envelope glycoprotein' 
_struct.pdbx_descriptor           'ENVELOPE GLYCOPROTEIN E' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4UTC 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'VIRAL PROTEIN, MEMBRANE FUSION, CLASS 2 FUSION PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 2 ? 
K N N 4 ? 
L N N 4 ? 
M N N 4 ? 
N N N 2 ? 
O N N 2 ? 
P N N 5 ? 
Q N N 5 ? 
# 
_struct_biol.id   1 
# 
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  1  LEU A 82  ? GLN A 86  ? LEU A 82  GLN A 86  5 ? 5 
HELX_P HELX_P2  2  GLY A 100 ? GLY A 104 ? GLY A 100 GLY A 104 5 ? 5 
HELX_P HELX_P3  3  GLN A 131 ? GLU A 133 ? GLN A 131 GLU A 133 5 ? 3 
HELX_P HELX_P4  4  ARG A 210 ? ASP A 215 ? ARG A 210 ASP A 215 1 ? 6 
HELX_P HELX_P5  5  GLN A 233 ? THR A 236 ? GLN A 233 THR A 236 5 ? 4 
HELX_P HELX_P6  6  GLN A 256 ? LEU A 264 ? GLN A 256 LEU A 264 1 ? 9 
HELX_P HELX_P7  7  LEU B 82  ? ASP B 87  ? LEU B 82  ASP B 87  5 ? 6 
HELX_P HELX_P8  8  GLN B 131 ? GLU B 133 ? GLN B 131 GLU B 133 5 ? 3 
HELX_P HELX_P9  9  ARG B 210 ? ASP B 215 ? ARG B 210 ASP B 215 1 ? 6 
HELX_P HELX_P10 10 GLN B 233 ? THR B 236 ? GLN B 233 THR B 236 5 ? 4 
HELX_P HELX_P11 11 GLN B 256 ? LEU B 264 ? GLN B 256 LEU B 264 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 3   SG  ? ? ? 1_555 A CYS 30  SG ? ? A CYS 3   A CYS 30  1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf2  disulf ? ? A CYS 60  SG  ? ? ? 1_555 A CYS 121 SG ? ? A CYS 60  A CYS 121 1_555 ? ? ? ? ? ? ? 2.070 ? 
disulf3  disulf ? ? A CYS 74  SG  ? ? ? 1_555 A CYS 105 SG ? ? A CYS 74  A CYS 105 1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf4  disulf ? ? A CYS 92  SG  ? ? ? 1_555 A CYS 116 SG ? ? A CYS 92  A CYS 116 1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf5  disulf ? ? A CYS 185 SG  ? ? ? 1_555 A CYS 285 SG ? ? A CYS 185 A CYS 285 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf6  disulf ? ? A CYS 302 SG  ? ? ? 1_555 A CYS 333 SG ? ? A CYS 302 A CYS 333 1_555 ? ? ? ? ? ? ? 2.060 ? 
disulf7  disulf ? ? B CYS 3   SG  ? ? ? 1_555 B CYS 30  SG ? ? B CYS 3   B CYS 30  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf8  disulf ? ? B CYS 60  SG  ? ? ? 1_555 B CYS 121 SG ? ? B CYS 60  B CYS 121 1_555 ? ? ? ? ? ? ? 2.061 ? 
disulf9  disulf ? ? B CYS 74  SG  ? ? ? 1_555 B CYS 105 SG ? ? B CYS 74  B CYS 105 1_555 ? ? ? ? ? ? ? 2.020 ? 
disulf10 disulf ? ? B CYS 92  SG  ? ? ? 1_555 B CYS 116 SG ? ? B CYS 92  B CYS 116 1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf11 disulf ? ? B CYS 185 SG  ? ? ? 1_555 B CYS 285 SG ? ? B CYS 185 B CYS 285 1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf12 disulf ? ? B CYS 302 SG  ? ? ? 1_555 B CYS 333 SG ? ? B CYS 302 B CYS 333 1_555 ? ? ? ? ? ? ? 2.049 ? 
covale1  covale ? ? A ASN 67  ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 67  A NAG 567 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale2  covale ? ? A ASN 153 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 153 A NAG 501 1_555 ? ? ? ? ? ? ? 1.437 ? 
covale3  covale ? ? C NAG .   O6  ? ? ? 1_555 D FUC .   C1 ? ? A NAG 501 A FUC 502 1_555 ? ? ? ? ? ? ? 1.406 ? 
covale4  covale ? ? C NAG .   O4  ? ? ? 1_555 E NAG .   C1 ? ? A NAG 501 A NAG 503 1_555 ? ? ? ? ? ? ? 1.419 ? 
covale5  covale ? ? F NAG .   O4  ? ? ? 1_555 G NAG .   C1 ? ? A NAG 567 A NAG 569 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale6  covale ? ? B ASN 67  ND2 ? ? ? 1_555 N NAG .   C1 ? ? B ASN 67  B NAG 567 1_555 ? ? ? ? ? ? ? 1.431 ? 
covale7  covale ? ? B ASN 153 ND2 ? ? ? 1_555 H NAG .   C1 ? ? B ASN 153 B NAG 501 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale8  covale ? ? H NAG .   O4  ? ? ? 1_555 J NAG .   C1 ? ? B NAG 501 B NAG 503 1_555 ? ? ? ? ? ? ? 1.412 ? 
covale9  covale ? ? H NAG .   O6  ? ? ? 1_555 I FUC .   C1 ? ? B NAG 501 B FUC 502 1_555 ? ? ? ? ? ? ? 1.407 ? 
covale10 covale ? ? J NAG .   O4  ? ? ? 1_555 K BMA .   C1 ? ? B NAG 503 B BMA 504 1_555 ? ? ? ? ? ? ? 1.466 ? 
covale11 covale ? ? K BMA .   O6  ? ? ? 1_555 L BMA .   C1 ? ? B BMA 504 B BMA 505 1_555 ? ? ? ? ? ? ? 1.401 ? 
covale12 covale ? ? K BMA .   O3  ? ? ? 1_555 M BMA .   C1 ? ? B BMA 504 B BMA 506 1_555 ? ? ? ? ? ? ? 1.516 ? 
covale13 covale ? ? N NAG .   O4  ? ? ? 1_555 O NAG .   C1 ? ? B NAG 567 B NAG 569 1_555 ? ? ? ? ? ? ? 1.428 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 331 A . ? SER 331 A PRO 332 A ? PRO 332 A 1 3.49 
2 GLU 383 A . ? GLU 383 A PRO 384 A ? PRO 384 A 1 0.14 
3 SER 331 B . ? SER 331 B PRO 332 B ? PRO 332 B 1 2.94 
4 GLU 383 B . ? GLU 383 B PRO 384 B ? PRO 384 B 1 4.71 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 5 ? 
AB ? 4 ? 
AC ? 2 ? 
AD ? 7 ? 
AE ? 4 ? 
AF ? 2 ? 
AG ? 4 ? 
AH ? 2 ? 
AI ? 3 ? 
BA ? 5 ? 
BB ? 4 ? 
BC ? 4 ? 
BD ? 3 ? 
BE ? 2 ? 
BF ? 4 ? 
BG ? 2 ? 
BH ? 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 
AA 1 2 ? parallel      
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AB 3 4 ? anti-parallel 
AC 1 2 ? anti-parallel 
AD 1 2 ? anti-parallel 
AD 2 3 ? parallel      
AD 3 4 ? anti-parallel 
AD 4 5 ? anti-parallel 
AD 5 6 ? anti-parallel 
AD 6 7 ? anti-parallel 
AE 1 2 ? anti-parallel 
AE 2 3 ? parallel      
AE 3 4 ? anti-parallel 
AF 1 2 ? anti-parallel 
AG 1 2 ? anti-parallel 
AG 2 3 ? anti-parallel 
AG 3 4 ? anti-parallel 
AH 1 2 ? anti-parallel 
AI 1 2 ? anti-parallel 
AI 2 3 ? anti-parallel 
BA 1 2 ? parallel      
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BA 4 5 ? anti-parallel 
BB 1 2 ? anti-parallel 
BB 2 3 ? anti-parallel 
BB 3 4 ? anti-parallel 
BC 1 2 ? anti-parallel 
BC 2 3 ? anti-parallel 
BC 3 4 ? anti-parallel 
BD 1 2 ? anti-parallel 
BD 2 3 ? anti-parallel 
BE 1 2 ? anti-parallel 
BF 1 2 ? anti-parallel 
BF 2 3 ? anti-parallel 
BF 3 4 ? anti-parallel 
BG 1 2 ? anti-parallel 
BH 1 2 ? anti-parallel 
BH 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 
AA 1 ARG A 9   ? GLU A 13  ? ARG A 9   GLU A 13  
AA 2 CYS A 30  ? ALA A 35  ? CYS A 30  ALA A 35  
AA 3 LYS A 38  ? ALA A 50  ? LYS A 38  ALA A 50  
AA 4 LEU A 135 ? PRO A 143 ? LEU A 135 PRO A 143 
AA 5 LYS A 160 ? ILE A 164 ? LYS A 160 ILE A 164 
AB 1 TRP A 20  ? LEU A 25  ? TRP A 20  LEU A 25  
AB 2 LEU A 283 ? ARG A 288 ? LEU A 283 ARG A 288 
AB 3 GLY A 179 ? SER A 186 ? GLY A 179 SER A 186 
AB 4 THR A 170 ? LEU A 175 ? THR A 170 LEU A 175 
AC 1 PHE A 90  ? ARG A 99  ? PHE A 90  ARG A 99  
AC 2 GLY A 109 ? ILE A 129 ? GLY A 109 ILE A 129 
AD 1 TRP A 220 ? PRO A 222 ? TRP A 220 PRO A 222 
AD 2 ALA A 54  ? SER A 72  ? ALA A 54  SER A 72  
AD 3 GLY A 109 ? ILE A 129 ? GLY A 109 ILE A 129 
AD 4 MET A 196 ? GLN A 200 ? MET A 196 GLN A 200 
AD 5 LYS A 204 ? HIS A 209 ? LYS A 204 HIS A 209 
AD 6 THR A 268 ? SER A 273 ? THR A 268 SER A 273 
AD 7 ASN A 276 ? LEU A 277 ? ASN A 276 LEU A 277 
AE 1 TRP A 220 ? PRO A 222 ? TRP A 220 PRO A 222 
AE 2 ALA A 54  ? SER A 72  ? ALA A 54  SER A 72  
AE 3 GLY A 109 ? ILE A 129 ? GLY A 109 ILE A 129 
AE 4 PHE A 90  ? ARG A 99  ? PHE A 90  ARG A 99  
AF 1 VAL A 238 ? LYS A 241 ? VAL A 238 LYS A 241 
AF 2 ASP A 249 ? VAL A 252 ? ASP A 249 VAL A 252 
AG 1 PHE A 306 ? GLU A 314 ? PHE A 306 GLU A 314 
AG 2 ILE A 320 ? TYR A 326 ? ILE A 320 TYR A 326 
AG 3 VAL A 365 ? GLU A 370 ? VAL A 365 GLU A 370 
AG 4 ARG A 350 ? LEU A 351 ? ARG A 350 LEU A 351 
AH 1 CYS A 333 ? LYS A 334 ? CYS A 333 LYS A 334 
AH 2 ILE A 357 ? VAL A 358 ? ILE A 357 VAL A 358 
AI 1 PHE A 337 ? THR A 340 ? PHE A 337 THR A 340 
AI 2 GLY A 374 ? VAL A 380 ? GLY A 374 VAL A 380 
AI 3 LEU A 387 ? ARG A 393 ? LEU A 387 ARG A 393 
BA 1 ARG B 9   ? GLU B 13  ? ARG B 9   GLU B 13  
BA 2 CYS B 30  ? ALA B 35  ? CYS B 30  ALA B 35  
BA 3 LYS B 38  ? ALA B 50  ? LYS B 38  ALA B 50  
BA 4 LEU B 135 ? PRO B 143 ? LEU B 135 PRO B 143 
BA 5 LYS B 160 ? ILE B 164 ? LYS B 160 ILE B 164 
BB 1 VAL B 21  ? LEU B 25  ? VAL B 21  LEU B 25  
BB 2 HIS B 282 ? ARG B 288 ? HIS B 282 ARG B 288 
BB 3 GLY B 179 ? ARG B 188 ? GLY B 179 ARG B 188 
BB 4 THR B 170 ? LEU B 175 ? THR B 170 LEU B 175 
BC 1 PHE B 90  ? ARG B 99  ? PHE B 90  ARG B 99  
BC 2 GLY B 109 ? ILE B 129 ? GLY B 109 ILE B 129 
BC 3 ALA B 54  ? SER B 72  ? ALA B 54  SER B 72  
BC 4 TRP B 220 ? PRO B 222 ? TRP B 220 PRO B 222 
BD 1 MET B 196 ? GLN B 200 ? MET B 196 GLN B 200 
BD 2 ALA B 205 ? HIS B 209 ? ALA B 205 HIS B 209 
BD 3 THR B 268 ? ILE B 270 ? THR B 268 ILE B 270 
BE 1 VAL B 238 ? LYS B 241 ? VAL B 238 LYS B 241 
BE 2 ASP B 249 ? VAL B 252 ? ASP B 249 VAL B 252 
BF 1 PHE B 306 ? GLU B 314 ? PHE B 306 GLU B 314 
BF 2 ILE B 320 ? TYR B 326 ? ILE B 320 TYR B 326 
BF 3 VAL B 365 ? GLU B 370 ? VAL B 365 GLU B 370 
BF 4 ARG B 350 ? LEU B 351 ? ARG B 350 LEU B 351 
BG 1 CYS B 333 ? LYS B 334 ? CYS B 333 LYS B 334 
BG 2 ILE B 357 ? VAL B 358 ? ILE B 357 VAL B 358 
BH 1 PHE B 337 ? THR B 340 ? PHE B 337 THR B 340 
BH 2 GLY B 374 ? VAL B 380 ? GLY B 374 VAL B 380 
BH 3 LEU B 387 ? ARG B 393 ? LEU B 387 ARG B 393 
# 
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 
AA 1 2 N ASP A 10  ? N ASP A 10  O CYS A 30  ? O CYS A 30  
AA 2 3 N ALA A 35  ? N ALA A 35  O LYS A 38  ? O LYS A 38  
AA 3 4 N GLU A 49  ? N GLU A 49  O GLU A 136 ? O GLU A 136 
AA 4 5 N ILE A 141 ? N ILE A 141 O LYS A 160 ? O LYS A 160 
AB 1 2 N LEU A 25  ? N LEU A 25  O LEU A 283 ? O LEU A 283 
AB 2 3 N ARG A 288 ? N ARG A 288 O THR A 182 ? O THR A 182 
AB 3 4 N MET A 183 ? N MET A 183 O THR A 171 ? O THR A 171 
AC 1 2 N ARG A 99  ? N ARG A 99  O GLY A 109 ? O GLY A 109 
AD 1 2 N LEU A 221 ? N LEU A 221 O LYS A 58  ? O LYS A 58  
AD 2 3 N GLU A 71  ? N GLU A 71  O VAL A 114 ? O VAL A 114 
AD 3 4 N LYS A 128 ? N LYS A 128 O LEU A 198 ? O LEU A 198 
AD 4 5 N LEU A 199 ? N LEU A 199 O TRP A 206 ? O TRP A 206 
AD 5 6 N LEU A 207 ? N LEU A 207 O THR A 268 ? O THR A 268 
AD 6 7 N SER A 273 ? N SER A 273 O ASN A 276 ? O ASN A 276 
AE 1 2 N LEU A 221 ? N LEU A 221 O LYS A 58  ? O LYS A 58  
AE 2 3 N GLU A 71  ? N GLU A 71  O VAL A 114 ? O VAL A 114 
AE 3 4 N ALA A 117 ? N ALA A 117 O ILE A 91  ? O ILE A 91  
AF 1 2 N LYS A 241 ? N LYS A 241 O ASP A 249 ? O ASP A 249 
AG 1 2 N ALA A 313 ? N ALA A 313 O VAL A 321 ? O VAL A 321 
AG 2 3 N VAL A 324 ? N VAL A 324 O VAL A 365 ? O VAL A 365 
AG 3 4 N GLU A 370 ? N GLU A 370 O ARG A 350 ? O ARG A 350 
AH 1 2 N CYS A 333 ? N CYS A 333 O VAL A 358 ? O VAL A 358 
AI 1 2 N THR A 340 ? N THR A 340 O TYR A 377 ? O TYR A 377 
AI 2 3 N VAL A 380 ? N VAL A 380 O LEU A 387 ? O LEU A 387 
BA 1 2 N ASP B 10  ? N ASP B 10  O CYS B 30  ? O CYS B 30  
BA 2 3 N ALA B 35  ? N ALA B 35  O LYS B 38  ? O LYS B 38  
BA 3 4 N GLU B 49  ? N GLU B 49  O GLU B 136 ? O GLU B 136 
BA 4 5 N ILE B 141 ? N ILE B 141 O LYS B 160 ? O LYS B 160 
BB 1 2 N LEU B 25  ? N LEU B 25  O LEU B 283 ? O LEU B 283 
BB 2 3 N ARG B 288 ? N ARG B 288 O THR B 182 ? O THR B 182 
BB 3 4 N MET B 183 ? N MET B 183 O THR B 171 ? O THR B 171 
BC 1 2 N ARG B 99  ? N ARG B 99  O GLY B 109 ? O GLY B 109 
BC 2 3 N ILE B 129 ? N ILE B 129 O ALA B 54  ? O ALA B 54  
BC 3 4 N LYS B 58  ? N LYS B 58  O LEU B 221 ? O LEU B 221 
BD 1 2 N LEU B 199 ? N LEU B 199 O TRP B 206 ? O TRP B 206 
BD 2 3 N LEU B 207 ? N LEU B 207 O THR B 268 ? O THR B 268 
BE 1 2 N LYS B 241 ? N LYS B 241 O ASP B 249 ? O ASP B 249 
BF 1 2 N ALA B 313 ? N ALA B 313 O VAL B 321 ? O VAL B 321 
BF 2 3 N VAL B 324 ? N VAL B 324 O VAL B 365 ? O VAL B 365 
BF 3 4 N GLU B 370 ? N GLU B 370 O ARG B 350 ? O ARG B 350 
BG 1 2 N CYS B 333 ? N CYS B 333 O VAL B 358 ? O VAL B 358 
BH 1 2 O THR B 340 ? O THR B 340 N TYR B 377 ? N TYR B 377 
BH 2 3 N VAL B 380 ? N VAL B 380 O LEU B 387 ? O LEU B 387 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 3  'Binding site for Poly-Saccharide residues NAG A 567 through NAG A 569 bound to ASN A 67'  
AC2 Software ? ? ? ? 6  'Binding site for Poly-Saccharide residues NAG A 501 through NAG A 503 bound to ASN A 153' 
AC3 Software ? ? ? ? 2  'Binding site for Poly-Saccharide residues NAG B 567 through NAG B 569 bound to ASN B 67'  
AC4 Software ? ? ? ? 11 'Binding site for Poly-Saccharide residues NAG B 501 through BMA B 506 bound to ASN B 153' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 3  ASN A 67  ? ASN A 67  . ? 1_555 ? 
2  AC1 3  ARG A 89  ? ARG A 89  . ? 1_555 ? 
3  AC1 3  LYS A 118 ? LYS A 118 . ? 1_555 ? 
4  AC2 6  GLU A 147 ? GLU A 147 . ? 1_555 ? 
5  AC2 6  HIS A 149 ? HIS A 149 . ? 1_555 ? 
6  AC2 6  ASN A 153 ? ASN A 153 . ? 1_555 ? 
7  AC2 6  LYS A 157 ? LYS A 157 . ? 1_555 ? 
8  AC2 6  HIS A 158 ? HIS A 158 . ? 1_555 ? 
9  AC2 6  GLY B 102 ? GLY B 102 . ? 1_555 ? 
10 AC3 2  ASN B 67  ? ASN B 67  . ? 1_555 ? 
11 AC3 2  LYS B 118 ? LYS B 118 . ? 1_555 ? 
12 AC4 11 GLN A 77  ? GLN A 77  . ? 8_554 ? 
13 AC4 11 GLY A 102 ? GLY A 102 . ? 1_555 ? 
14 AC4 11 LYS B 88  ? LYS B 88  . ? 6_544 ? 
15 AC4 11 GLU B 147 ? GLU B 147 . ? 1_555 ? 
16 AC4 11 HIS B 149 ? HIS B 149 . ? 1_555 ? 
17 AC4 11 ASN B 153 ? ASN B 153 . ? 1_555 ? 
18 AC4 11 LYS B 157 ? LYS B 157 . ? 1_555 ? 
19 AC4 11 HIS B 158 ? HIS B 158 . ? 1_555 ? 
20 AC4 11 VAL B 309 ? VAL B 309 . ? 8_554 ? 
21 AC4 11 LYS B 310 ? LYS B 310 . ? 8_554 ? 
22 AC4 11 GLU B 311 ? GLU B 311 . ? 8_554 ? 
# 
_database_PDB_matrix.entry_id          4UTC 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    4UTC 
_atom_sites.fract_transf_matrix[1][1]   0.009482 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009482 
_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]   0.006028 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 1   ? -34.968 10.422  -32.476 1.00 71.58  ? 1    MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? -35.301 10.413  -33.901 1.00 71.29  ? 1    MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? -34.271 9.592   -34.661 1.00 74.68  ? 1    MET A C   1 
ATOM   4    O O   . MET A 1 1   ? -34.377 9.459   -35.894 1.00 74.72  ? 1    MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? -35.400 11.828  -34.472 1.00 74.22  ? 1    MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? -36.386 12.722  -33.745 1.00 79.52  ? 1    MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? -37.445 13.642  -34.891 1.00 85.53  ? 1    MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? -36.299 14.876  -35.473 1.00 82.40  ? 1    MET A CE  1 
ATOM   9    N N   . ARG A 1 2   ? -33.274 9.027   -33.910 1.00 69.53  ? 2    ARG A N   1 
ATOM   10   C CA  . ARG A 1 2   ? -32.199 8.162   -34.396 1.00 69.51  ? 2    ARG A CA  1 
ATOM   11   C C   . ARG A 1 2   ? -32.769 6.929   -35.091 1.00 73.39  ? 2    ARG A C   1 
ATOM   12   O O   . ARG A 1 2   ? -32.309 6.556   -36.173 1.00 73.49  ? 2    ARG A O   1 
ATOM   13   C CB  . ARG A 1 2   ? -31.321 7.692   -33.233 1.00 71.84  ? 2    ARG A CB  1 
ATOM   14   C CG  . ARG A 1 2   ? -30.364 8.742   -32.695 1.00 88.12  ? 2    ARG A CG  1 
ATOM   15   C CD  . ARG A 1 2   ? -29.538 8.195   -31.546 1.00 94.42  ? 2    ARG A CD  1 
ATOM   16   N NE  . ARG A 1 2   ? -28.132 8.581   -31.660 1.00 106.22 ? 2    ARG A NE  1 
ATOM   17   C CZ  . ARG A 1 2   ? -27.149 7.746   -31.989 1.00 121.78 ? 2    ARG A CZ  1 
ATOM   18   N NH1 . ARG A 1 2   ? -27.406 6.463   -32.213 1.00 108.61 ? 2    ARG A NH1 1 
ATOM   19   N NH2 . ARG A 1 2   ? -25.899 8.181   -32.069 1.00 104.17 ? 2    ARG A NH2 1 
ATOM   20   N N   . CYS A 1 3   ? -33.793 6.324   -34.472 1.00 69.93  ? 3    CYS A N   1 
ATOM   21   C CA  . CYS A 1 3   ? -34.484 5.120   -34.924 1.00 71.21  ? 3    CYS A CA  1 
ATOM   22   C C   . CYS A 1 3   ? -35.054 5.213   -36.318 1.00 71.59  ? 3    CYS A C   1 
ATOM   23   O O   . CYS A 1 3   ? -35.207 4.191   -36.984 1.00 70.22  ? 3    CYS A O   1 
ATOM   24   C CB  . CYS A 1 3   ? -35.561 4.727   -33.918 1.00 73.41  ? 3    CYS A CB  1 
ATOM   25   S SG  . CYS A 1 3   ? -34.952 4.467   -32.227 1.00 78.11  ? 3    CYS A SG  1 
ATOM   26   N N   . ILE A 1 4   ? -35.408 6.427   -36.744 1.00 67.30  ? 4    ILE A N   1 
ATOM   27   C CA  . ILE A 1 4   ? -35.959 6.662   -38.067 1.00 66.70  ? 4    ILE A CA  1 
ATOM   28   C C   . ILE A 1 4   ? -34.869 6.293   -39.091 1.00 70.05  ? 4    ILE A C   1 
ATOM   29   O O   . ILE A 1 4   ? -33.845 6.992   -39.202 1.00 70.40  ? 4    ILE A O   1 
ATOM   30   C CB  . ILE A 1 4   ? -36.472 8.126   -38.209 1.00 69.67  ? 4    ILE A CB  1 
ATOM   31   C CG1 . ILE A 1 4   ? -37.457 8.512   -37.084 1.00 70.48  ? 4    ILE A CG1 1 
ATOM   32   C CG2 . ILE A 1 4   ? -37.092 8.349   -39.567 1.00 70.01  ? 4    ILE A CG2 1 
ATOM   33   C CD1 . ILE A 1 4   ? -37.640 10.041  -36.886 1.00 78.21  ? 4    ILE A CD1 1 
ATOM   34   N N   . GLY A 1 5   ? -35.083 5.162   -39.765 1.00 64.30  ? 5    GLY A N   1 
ATOM   35   C CA  . GLY A 1 5   ? -34.170 4.656   -40.785 1.00 63.74  ? 5    GLY A CA  1 
ATOM   36   C C   . GLY A 1 5   ? -33.653 3.253   -40.518 1.00 64.95  ? 5    GLY A C   1 
ATOM   37   O O   . GLY A 1 5   ? -33.328 2.513   -41.464 1.00 64.63  ? 5    GLY A O   1 
ATOM   38   N N   . ILE A 1 6   ? -33.567 2.900   -39.209 1.00 57.17  ? 6    ILE A N   1 
ATOM   39   C CA  . ILE A 1 6   ? -33.139 1.607   -38.649 1.00 54.24  ? 6    ILE A CA  1 
ATOM   40   C C   . ILE A 1 6   ? -34.283 0.579   -38.788 1.00 52.97  ? 6    ILE A C   1 
ATOM   41   O O   . ILE A 1 6   ? -35.361 0.778   -38.246 1.00 49.79  ? 6    ILE A O   1 
ATOM   42   C CB  . ILE A 1 6   ? -32.653 1.787   -37.155 1.00 56.78  ? 6    ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 6   ? -31.334 2.561   -37.076 1.00 56.08  ? 6    ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 6   ? -32.543 0.453   -36.420 1.00 58.01  ? 6    ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 6   ? -30.977 3.132   -35.715 1.00 63.58  ? 6    ILE A CD1 1 
ATOM   46   N N   . SER A 1 7   ? -34.022 -0.526  -39.481 1.00 51.62  ? 7    SER A N   1 
ATOM   47   C CA  . SER A 1 7   ? -34.969 -1.618  -39.692 1.00 52.75  ? 7    SER A CA  1 
ATOM   48   C C   . SER A 1 7   ? -35.240 -2.408  -38.418 1.00 62.39  ? 7    SER A C   1 
ATOM   49   O O   . SER A 1 7   ? -36.396 -2.768  -38.190 1.00 63.26  ? 7    SER A O   1 
ATOM   50   C CB  . SER A 1 7   ? -34.499 -2.553  -40.795 1.00 54.99  ? 7    SER A CB  1 
ATOM   51   O OG  . SER A 1 7   ? -33.242 -3.104  -40.450 1.00 65.86  ? 7    SER A OG  1 
ATOM   52   N N   . ASN A 1 8   ? -34.209 -2.693  -37.578 1.00 60.97  ? 8    ASN A N   1 
ATOM   53   C CA  . ASN A 1 8   ? -34.480 -3.440  -36.343 1.00 61.08  ? 8    ASN A CA  1 
ATOM   54   C C   . ASN A 1 8   ? -34.912 -2.472  -35.236 1.00 63.24  ? 8    ASN A C   1 
ATOM   55   O O   . ASN A 1 8   ? -34.138 -2.133  -34.330 1.00 61.24  ? 8    ASN A O   1 
ATOM   56   C CB  . ASN A 1 8   ? -33.321 -4.353  -35.943 1.00 66.20  ? 8    ASN A CB  1 
ATOM   57   C CG  . ASN A 1 8   ? -33.650 -5.231  -34.755 1.00 106.50 ? 8    ASN A CG  1 
ATOM   58   O OD1 . ASN A 1 8   ? -34.806 -5.643  -34.548 1.00 97.09  ? 8    ASN A OD1 1 
ATOM   59   N ND2 . ASN A 1 8   ? -32.641 -5.518  -33.932 1.00 106.29 ? 8    ASN A ND2 1 
ATOM   60   N N   . ARG A 1 9   ? -36.173 -2.023  -35.337 1.00 59.73  ? 9    ARG A N   1 
ATOM   61   C CA  . ARG A 1 9   ? -36.758 -1.020  -34.451 1.00 59.14  ? 9    ARG A CA  1 
ATOM   62   C C   . ARG A 1 9   ? -38.069 -1.457  -33.832 1.00 61.62  ? 9    ARG A C   1 
ATOM   63   O O   . ARG A 1 9   ? -38.916 -2.013  -34.526 1.00 60.42  ? 9    ARG A O   1 
ATOM   64   C CB  . ARG A 1 9   ? -36.956 0.258   -35.261 1.00 59.85  ? 9    ARG A CB  1 
ATOM   65   C CG  . ARG A 1 9   ? -37.493 1.419   -34.484 1.00 65.86  ? 9    ARG A CG  1 
ATOM   66   C CD  . ARG A 1 9   ? -38.150 2.344   -35.450 1.00 64.62  ? 9    ARG A CD  1 
ATOM   67   N NE  . ARG A 1 9   ? -38.607 3.557   -34.793 1.00 60.80  ? 9    ARG A NE  1 
ATOM   68   C CZ  . ARG A 1 9   ? -38.982 4.642   -35.449 1.00 74.70  ? 9    ARG A CZ  1 
ATOM   69   N NH1 . ARG A 1 9   ? -38.977 4.658   -36.776 1.00 79.17  ? 9    ARG A NH1 1 
ATOM   70   N NH2 . ARG A 1 9   ? -39.390 5.710   -34.791 1.00 50.75  ? 9    ARG A NH2 1 
ATOM   71   N N   . ASP A 1 10  ? -38.242 -1.184  -32.532 1.00 59.90  ? 10   ASP A N   1 
ATOM   72   C CA  . ASP A 1 10  ? -39.459 -1.532  -31.796 1.00 60.84  ? 10   ASP A CA  1 
ATOM   73   C C   . ASP A 1 10  ? -40.178 -0.283  -31.317 1.00 64.52  ? 10   ASP A C   1 
ATOM   74   O O   . ASP A 1 10  ? -39.536 0.697   -30.936 1.00 63.95  ? 10   ASP A O   1 
ATOM   75   C CB  . ASP A 1 10  ? -39.151 -2.456  -30.603 1.00 63.99  ? 10   ASP A CB  1 
ATOM   76   C CG  . ASP A 1 10  ? -38.292 -3.680  -30.921 1.00 86.89  ? 10   ASP A CG  1 
ATOM   77   O OD1 . ASP A 1 10  ? -38.612 -4.394  -31.905 1.00 91.18  ? 10   ASP A OD1 1 
ATOM   78   O OD2 . ASP A 1 10  ? -37.326 -3.954  -30.153 1.00 92.36  ? 10   ASP A OD2 1 
ATOM   79   N N   . PHE A 1 11  ? -41.510 -0.320  -31.330 1.00 62.07  ? 11   PHE A N   1 
ATOM   80   C CA  . PHE A 1 11  ? -42.363 0.778   -30.885 1.00 62.10  ? 11   PHE A CA  1 
ATOM   81   C C   . PHE A 1 11  ? -43.041 0.356   -29.591 1.00 66.44  ? 11   PHE A C   1 
ATOM   82   O O   . PHE A 1 11  ? -44.111 -0.240  -29.614 1.00 65.85  ? 11   PHE A O   1 
ATOM   83   C CB  . PHE A 1 11  ? -43.394 1.118   -31.969 1.00 64.05  ? 11   PHE A CB  1 
ATOM   84   C CG  . PHE A 1 11  ? -42.804 1.617   -33.266 1.00 66.06  ? 11   PHE A CG  1 
ATOM   85   C CD1 . PHE A 1 11  ? -42.299 0.730   -34.206 1.00 69.26  ? 11   PHE A CD1 1 
ATOM   86   C CD2 . PHE A 1 11  ? -42.757 2.977   -33.552 1.00 68.99  ? 11   PHE A CD2 1 
ATOM   87   C CE1 . PHE A 1 11  ? -41.730 1.199   -35.401 1.00 71.87  ? 11   PHE A CE1 1 
ATOM   88   C CE2 . PHE A 1 11  ? -42.205 3.443   -34.752 1.00 69.91  ? 11   PHE A CE2 1 
ATOM   89   C CZ  . PHE A 1 11  ? -41.709 2.551   -35.673 1.00 69.34  ? 11   PHE A CZ  1 
ATOM   90   N N   . VAL A 1 12  ? -42.371 0.596   -28.467 1.00 64.70  ? 12   VAL A N   1 
ATOM   91   C CA  . VAL A 1 12  ? -42.836 0.232   -27.118 1.00 65.59  ? 12   VAL A CA  1 
ATOM   92   C C   . VAL A 1 12  ? -43.769 1.324   -26.575 1.00 72.87  ? 12   VAL A C   1 
ATOM   93   O O   . VAL A 1 12  ? -43.329 2.456   -26.377 1.00 72.03  ? 12   VAL A O   1 
ATOM   94   C CB  . VAL A 1 12  ? -41.646 -0.032  -26.140 1.00 68.24  ? 12   VAL A CB  1 
ATOM   95   C CG1 . VAL A 1 12  ? -42.130 -0.304  -24.718 1.00 67.48  ? 12   VAL A CG1 1 
ATOM   96   C CG2 . VAL A 1 12  ? -40.762 -1.163  -26.639 1.00 67.97  ? 12   VAL A CG2 1 
ATOM   97   N N   . GLU A 1 13  ? -45.041 0.980   -26.317 1.00 71.87  ? 13   GLU A N   1 
ATOM   98   C CA  . GLU A 1 13  ? -45.988 1.932   -25.753 1.00 73.01  ? 13   GLU A CA  1 
ATOM   99   C C   . GLU A 1 13  ? -46.380 1.503   -24.358 1.00 79.65  ? 13   GLU A C   1 
ATOM   100  O O   . GLU A 1 13  ? -46.798 0.364   -24.144 1.00 79.16  ? 13   GLU A O   1 
ATOM   101  C CB  . GLU A 1 13  ? -47.220 2.151   -26.650 1.00 74.73  ? 13   GLU A CB  1 
ATOM   102  C CG  . GLU A 1 13  ? -48.020 3.393   -26.268 1.00 89.02  ? 13   GLU A CG  1 
ATOM   103  C CD  . GLU A 1 13  ? -49.225 3.734   -27.125 1.00 115.76 ? 13   GLU A CD  1 
ATOM   104  O OE1 . GLU A 1 13  ? -49.809 2.808   -27.735 1.00 131.00 ? 13   GLU A OE1 1 
ATOM   105  O OE2 . GLU A 1 13  ? -49.599 4.930   -27.168 1.00 100.32 ? 13   GLU A OE2 1 
ATOM   106  N N   . GLY A 1 14  ? -46.197 2.418   -23.421 1.00 78.85  ? 14   GLY A N   1 
ATOM   107  C CA  . GLY A 1 14  ? -46.510 2.190   -22.027 1.00 80.63  ? 14   GLY A CA  1 
ATOM   108  C C   . GLY A 1 14  ? -47.959 2.488   -21.756 1.00 90.99  ? 14   GLY A C   1 
ATOM   109  O O   . GLY A 1 14  ? -48.510 3.460   -22.296 1.00 91.23  ? 14   GLY A O   1 
ATOM   110  N N   . VAL A 1 15  ? -48.585 1.635   -20.922 1.00 91.56  ? 15   VAL A N   1 
ATOM   111  C CA  . VAL A 1 15  ? -49.964 1.824   -20.494 1.00 92.68  ? 15   VAL A CA  1 
ATOM   112  C C   . VAL A 1 15  ? -49.960 3.110   -19.693 1.00 99.12  ? 15   VAL A C   1 
ATOM   113  O O   . VAL A 1 15  ? -49.368 3.201   -18.614 1.00 98.31  ? 15   VAL A O   1 
ATOM   114  C CB  . VAL A 1 15  ? -50.575 0.624   -19.739 1.00 96.47  ? 15   VAL A CB  1 
ATOM   115  C CG1 . VAL A 1 15  ? -51.998 0.937   -19.287 1.00 96.12  ? 15   VAL A CG1 1 
ATOM   116  C CG2 . VAL A 1 15  ? -50.555 -0.617  -20.621 1.00 96.31  ? 15   VAL A CG2 1 
ATOM   117  N N   . SER A 1 16  ? -50.492 4.131   -20.359 1.00 98.20  ? 16   SER A N   1 
ATOM   118  C CA  . SER A 1 16  ? -50.634 5.532   -19.985 1.00 98.81  ? 16   SER A CA  1 
ATOM   119  C C   . SER A 1 16  ? -51.121 5.720   -18.553 1.00 102.47 ? 16   SER A C   1 
ATOM   120  O O   . SER A 1 16  ? -52.080 5.076   -18.111 1.00 101.39 ? 16   SER A O   1 
ATOM   121  C CB  . SER A 1 16  ? -51.518 6.236   -21.005 1.00 103.47 ? 16   SER A CB  1 
ATOM   122  O OG  . SER A 1 16  ? -51.061 5.939   -22.322 1.00 111.83 ? 16   SER A OG  1 
ATOM   123  N N   . GLY A 1 17  ? -50.375 6.543   -17.830 1.00 99.93  ? 17   GLY A N   1 
ATOM   124  C CA  . GLY A 1 17  ? -50.545 6.778   -16.402 1.00 100.23 ? 17   GLY A CA  1 
ATOM   125  C C   . GLY A 1 17  ? -49.366 6.179   -15.655 1.00 104.93 ? 17   GLY A C   1 
ATOM   126  O O   . GLY A 1 17  ? -48.809 6.816   -14.754 1.00 104.73 ? 17   GLY A O   1 
ATOM   127  N N   . GLY A 1 18  ? -48.975 4.965   -16.074 1.00 101.87 ? 18   GLY A N   1 
ATOM   128  C CA  . GLY A 1 18  ? -47.857 4.194   -15.540 1.00 101.76 ? 18   GLY A CA  1 
ATOM   129  C C   . GLY A 1 18  ? -46.563 4.981   -15.522 1.00 106.58 ? 18   GLY A C   1 
ATOM   130  O O   . GLY A 1 18  ? -46.249 5.691   -16.487 1.00 106.80 ? 18   GLY A O   1 
ATOM   131  N N   . SER A 1 19  ? -45.827 4.883   -14.391 1.00 102.09 ? 19   SER A N   1 
ATOM   132  C CA  . SER A 1 19  ? -44.569 5.583   -14.148 1.00 100.65 ? 19   SER A CA  1 
ATOM   133  C C   . SER A 1 19  ? -43.332 4.819   -14.617 1.00 103.90 ? 19   SER A C   1 
ATOM   134  O O   . SER A 1 19  ? -42.218 5.284   -14.399 1.00 103.30 ? 19   SER A O   1 
ATOM   135  C CB  . SER A 1 19  ? -44.460 5.965   -12.679 1.00 102.37 ? 19   SER A CB  1 
ATOM   136  O OG  . SER A 1 19  ? -45.412 6.972   -12.386 1.00 108.69 ? 19   SER A OG  1 
ATOM   137  N N   . TRP A 1 20  ? -43.523 3.660   -15.271 1.00 100.68 ? 20   TRP A N   1 
ATOM   138  C CA  . TRP A 1 20  ? -42.428 2.836   -15.790 1.00 100.47 ? 20   TRP A CA  1 
ATOM   139  C C   . TRP A 1 20  ? -42.784 2.156   -17.079 1.00 99.41  ? 20   TRP A C   1 
ATOM   140  O O   . TRP A 1 20  ? -43.956 1.842   -17.309 1.00 98.52  ? 20   TRP A O   1 
ATOM   141  C CB  . TRP A 1 20  ? -42.031 1.716   -14.824 1.00 100.58 ? 20   TRP A CB  1 
ATOM   142  C CG  . TRP A 1 20  ? -42.262 1.982   -13.377 1.00 102.67 ? 20   TRP A CG  1 
ATOM   143  C CD1 . TRP A 1 20  ? -43.343 1.607   -12.629 1.00 105.79 ? 20   TRP A CD1 1 
ATOM   144  C CD2 . TRP A 1 20  ? -41.350 2.618   -12.482 1.00 103.03 ? 20   TRP A CD2 1 
ATOM   145  N NE1 . TRP A 1 20  ? -43.160 1.979   -11.317 1.00 105.55 ? 20   TRP A NE1 1 
ATOM   146  C CE2 . TRP A 1 20  ? -41.945 2.606   -11.198 1.00 107.30 ? 20   TRP A CE2 1 
ATOM   147  C CE3 . TRP A 1 20  ? -40.070 3.185   -12.635 1.00 104.52 ? 20   TRP A CE3 1 
ATOM   148  C CZ2 . TRP A 1 20  ? -41.317 3.164   -10.081 1.00 106.84 ? 20   TRP A CZ2 1 
ATOM   149  C CZ3 . TRP A 1 20  ? -39.454 3.749   -11.530 1.00 106.28 ? 20   TRP A CZ3 1 
ATOM   150  C CH2 . TRP A 1 20  ? -40.077 3.743   -10.274 1.00 107.04 ? 20   TRP A CH2 1 
ATOM   151  N N   . VAL A 1 21  ? -41.759 1.822   -17.872 1.00 93.02  ? 21   VAL A N   1 
ATOM   152  C CA  . VAL A 1 21  ? -41.941 1.032   -19.087 1.00 92.14  ? 21   VAL A CA  1 
ATOM   153  C C   . VAL A 1 21  ? -40.728 0.136   -19.275 1.00 93.31  ? 21   VAL A C   1 
ATOM   154  O O   . VAL A 1 21  ? -39.594 0.577   -19.032 1.00 92.84  ? 21   VAL A O   1 
ATOM   155  C CB  . VAL A 1 21  ? -42.360 1.819   -20.363 1.00 96.14  ? 21   VAL A CB  1 
ATOM   156  C CG1 . VAL A 1 21  ? -41.159 2.386   -21.120 1.00 95.99  ? 21   VAL A CG1 1 
ATOM   157  C CG2 . VAL A 1 21  ? -43.216 0.949   -21.277 1.00 95.90  ? 21   VAL A CG2 1 
ATOM   158  N N   . ASP A 1 22  ? -40.967 -1.133  -19.660 1.00 87.47  ? 22   ASP A N   1 
ATOM   159  C CA  . ASP A 1 22  ? -39.859 -2.064  -19.818 1.00 86.56  ? 22   ASP A CA  1 
ATOM   160  C C   . ASP A 1 22  ? -39.394 -2.222  -21.249 1.00 86.69  ? 22   ASP A C   1 
ATOM   161  O O   . ASP A 1 22  ? -40.190 -2.551  -22.128 1.00 86.33  ? 22   ASP A O   1 
ATOM   162  C CB  . ASP A 1 22  ? -40.169 -3.417  -19.184 1.00 89.02  ? 22   ASP A CB  1 
ATOM   163  C CG  . ASP A 1 22  ? -39.956 -3.427  -17.692 1.00 102.66 ? 22   ASP A CG  1 
ATOM   164  O OD1 . ASP A 1 22  ? -38.831 -3.069  -17.245 1.00 104.69 ? 22   ASP A OD1 1 
ATOM   165  O OD2 . ASP A 1 22  ? -40.899 -3.811  -16.965 1.00 106.94 ? 22   ASP A OD2 1 
ATOM   166  N N   . ILE A 1 23  ? -38.097 -1.964  -21.478 1.00 80.51  ? 23   ILE A N   1 
ATOM   167  C CA  . ILE A 1 23  ? -37.461 -2.061  -22.793 1.00 79.24  ? 23   ILE A CA  1 
ATOM   168  C C   . ILE A 1 23  ? -36.207 -2.947  -22.766 1.00 83.00  ? 23   ILE A C   1 
ATOM   169  O O   . ILE A 1 23  ? -35.567 -3.099  -21.730 1.00 83.31  ? 23   ILE A O   1 
ATOM   170  C CB  . ILE A 1 23  ? -37.181 -0.685  -23.465 1.00 80.98  ? 23   ILE A CB  1 
ATOM   171  C CG1 . ILE A 1 23  ? -36.230 0.186   -22.634 1.00 80.27  ? 23   ILE A CG1 1 
ATOM   172  C CG2 . ILE A 1 23  ? -38.478 0.032   -23.800 1.00 81.66  ? 23   ILE A CG2 1 
ATOM   173  C CD1 . ILE A 1 23  ? -35.445 1.198   -23.417 1.00 85.13  ? 23   ILE A CD1 1 
ATOM   174  N N   . VAL A 1 24  ? -35.866 -3.516  -23.928 1.00 78.15  ? 24   VAL A N   1 
ATOM   175  C CA  . VAL A 1 24  ? -34.706 -4.378  -24.147 1.00 76.71  ? 24   VAL A CA  1 
ATOM   176  C C   . VAL A 1 24  ? -33.793 -3.708  -25.161 1.00 79.37  ? 24   VAL A C   1 
ATOM   177  O O   . VAL A 1 24  ? -34.100 -3.676  -26.357 1.00 79.92  ? 24   VAL A O   1 
ATOM   178  C CB  . VAL A 1 24  ? -35.085 -5.809  -24.621 1.00 79.62  ? 24   VAL A CB  1 
ATOM   179  C CG1 . VAL A 1 24  ? -33.875 -6.725  -24.556 1.00 79.05  ? 24   VAL A CG1 1 
ATOM   180  C CG2 . VAL A 1 24  ? -36.242 -6.385  -23.819 1.00 79.48  ? 24   VAL A CG2 1 
ATOM   181  N N   . LEU A 1 25  ? -32.686 -3.174  -24.694 1.00 75.02  ? 25   LEU A N   1 
ATOM   182  C CA  . LEU A 1 25  ? -31.743 -2.562  -25.603 1.00 75.99  ? 25   LEU A CA  1 
ATOM   183  C C   . LEU A 1 25  ? -30.649 -3.555  -25.996 1.00 84.18  ? 25   LEU A C   1 
ATOM   184  O O   . LEU A 1 25  ? -30.165 -4.321  -25.150 1.00 86.52  ? 25   LEU A O   1 
ATOM   185  C CB  . LEU A 1 25  ? -31.141 -1.277  -25.017 1.00 75.90  ? 25   LEU A CB  1 
ATOM   186  C CG  . LEU A 1 25  ? -32.101 -0.119  -24.768 1.00 80.95  ? 25   LEU A CG  1 
ATOM   187  C CD1 . LEU A 1 25  ? -31.348 1.095   -24.291 1.00 81.31  ? 25   LEU A CD1 1 
ATOM   188  C CD2 . LEU A 1 25  ? -32.895 0.241   -26.027 1.00 84.05  ? 25   LEU A CD2 1 
ATOM   189  N N   . GLU A 1 26  ? -30.291 -3.572  -27.287 1.00 79.83  ? 26   GLU A N   1 
ATOM   190  C CA  . GLU A 1 26  ? -29.226 -4.422  -27.808 1.00 78.84  ? 26   GLU A CA  1 
ATOM   191  C C   . GLU A 1 26  ? -28.530 -3.728  -28.973 1.00 80.04  ? 26   GLU A C   1 
ATOM   192  O O   . GLU A 1 26  ? -28.959 -2.645  -29.385 1.00 78.96  ? 26   GLU A O   1 
ATOM   193  C CB  . GLU A 1 26  ? -29.687 -5.871  -28.112 1.00 79.96  ? 26   GLU A CB  1 
ATOM   194  C CG  . GLU A 1 26  ? -30.592 -6.051  -29.307 1.00 87.88  ? 26   GLU A CG  1 
ATOM   195  C CD  . GLU A 1 26  ? -31.016 -7.487  -29.544 1.00 117.73 ? 26   GLU A CD  1 
ATOM   196  O OE1 . GLU A 1 26  ? -30.132 -8.376  -29.606 1.00 113.10 ? 26   GLU A OE1 1 
ATOM   197  O OE2 . GLU A 1 26  ? -32.241 -7.725  -29.651 1.00 121.76 ? 26   GLU A OE2 1 
ATOM   198  N N   . HIS A 1 27  ? -27.409 -4.299  -29.437 1.00 75.28  ? 27   HIS A N   1 
ATOM   199  C CA  . HIS A 1 27  ? -26.620 -3.703  -30.502 1.00 74.32  ? 27   HIS A CA  1 
ATOM   200  C C   . HIS A 1 27  ? -27.274 -3.951  -31.829 1.00 76.33  ? 27   HIS A C   1 
ATOM   201  O O   . HIS A 1 27  ? -27.786 -5.048  -32.061 1.00 75.58  ? 27   HIS A O   1 
ATOM   202  C CB  . HIS A 1 27  ? -25.170 -4.203  -30.466 1.00 75.08  ? 27   HIS A CB  1 
ATOM   203  C CG  . HIS A 1 27  ? -24.324 -3.491  -29.458 1.00 78.42  ? 27   HIS A CG  1 
ATOM   204  N ND1 . HIS A 1 27  ? -23.541 -2.401  -29.816 1.00 80.21  ? 27   HIS A ND1 1 
ATOM   205  C CD2 . HIS A 1 27  ? -24.173 -3.724  -28.131 1.00 79.88  ? 27   HIS A CD2 1 
ATOM   206  C CE1 . HIS A 1 27  ? -22.937 -2.012  -28.700 1.00 79.40  ? 27   HIS A CE1 1 
ATOM   207  N NE2 . HIS A 1 27  ? -23.289 -2.775  -27.658 1.00 79.63  ? 27   HIS A NE2 1 
ATOM   208  N N   . GLY A 1 28  ? -27.319 -2.901  -32.646 1.00 72.71  ? 28   GLY A N   1 
ATOM   209  C CA  . GLY A 1 28  ? -27.928 -2.894  -33.976 1.00 72.72  ? 28   GLY A CA  1 
ATOM   210  C C   . GLY A 1 28  ? -29.433 -2.748  -33.953 1.00 76.70  ? 28   GLY A C   1 
ATOM   211  O O   . GLY A 1 28  ? -30.104 -2.948  -34.974 1.00 76.26  ? 28   GLY A O   1 
ATOM   212  N N   . SER A 1 29  ? -29.957 -2.406  -32.771 1.00 73.42  ? 29   SER A N   1 
ATOM   213  C CA  . SER A 1 29  ? -31.370 -2.264  -32.472 1.00 73.93  ? 29   SER A CA  1 
ATOM   214  C C   . SER A 1 29  ? -31.640 -0.893  -31.853 1.00 78.33  ? 29   SER A C   1 
ATOM   215  O O   . SER A 1 29  ? -30.880 -0.415  -31.002 1.00 77.98  ? 29   SER A O   1 
ATOM   216  C CB  . SER A 1 29  ? -31.831 -3.396  -31.543 1.00 78.82  ? 29   SER A CB  1 
ATOM   217  O OG  . SER A 1 29  ? -32.988 -3.137  -30.756 1.00 91.15  ? 29   SER A OG  1 
ATOM   218  N N   . CYS A 1 30  ? -32.760 -0.289  -32.272 1.00 74.73  ? 30   CYS A N   1 
ATOM   219  C CA  . CYS A 1 30  ? -33.255 0.992   -31.791 1.00 73.75  ? 30   CYS A CA  1 
ATOM   220  C C   . CYS A 1 30  ? -34.620 0.792   -31.138 1.00 76.20  ? 30   CYS A C   1 
ATOM   221  O O   . CYS A 1 30  ? -35.352 -0.122  -31.529 1.00 76.04  ? 30   CYS A O   1 
ATOM   222  C CB  . CYS A 1 30  ? -33.342 1.973   -32.949 1.00 74.14  ? 30   CYS A CB  1 
ATOM   223  S SG  . CYS A 1 30  ? -33.082 3.686   -32.457 1.00 78.31  ? 30   CYS A SG  1 
ATOM   224  N N   . VAL A 1 31  ? -34.973 1.627   -30.151 1.00 71.67  ? 31   VAL A N   1 
ATOM   225  C CA  . VAL A 1 31  ? -36.287 1.531   -29.494 1.00 70.98  ? 31   VAL A CA  1 
ATOM   226  C C   . VAL A 1 31  ? -37.015 2.895   -29.405 1.00 73.37  ? 31   VAL A C   1 
ATOM   227  O O   . VAL A 1 31  ? -36.413 3.886   -28.992 1.00 72.66  ? 31   VAL A O   1 
ATOM   228  C CB  . VAL A 1 31  ? -36.175 0.842   -28.129 1.00 74.89  ? 31   VAL A CB  1 
ATOM   229  C CG1 . VAL A 1 31  ? -37.436 1.049   -27.299 1.00 74.38  ? 31   VAL A CG1 1 
ATOM   230  C CG2 . VAL A 1 31  ? -35.876 -0.644  -28.293 1.00 74.93  ? 31   VAL A CG2 1 
ATOM   231  N N   . THR A 1 32  ? -38.303 2.934   -29.788 1.00 68.39  ? 32   THR A N   1 
ATOM   232  C CA  . THR A 1 32  ? -39.116 4.147   -29.720 1.00 67.63  ? 32   THR A CA  1 
ATOM   233  C C   . THR A 1 32  ? -40.192 3.950   -28.636 1.00 71.12  ? 32   THR A C   1 
ATOM   234  O O   . THR A 1 32  ? -41.004 3.023   -28.737 1.00 69.70  ? 32   THR A O   1 
ATOM   235  C CB  . THR A 1 32  ? -39.658 4.504   -31.110 1.00 74.86  ? 32   THR A CB  1 
ATOM   236  O OG1 . THR A 1 32  ? -38.562 4.766   -31.979 1.00 75.80  ? 32   THR A OG1 1 
ATOM   237  C CG2 . THR A 1 32  ? -40.560 5.713   -31.095 1.00 72.61  ? 32   THR A CG2 1 
ATOM   238  N N   . THR A 1 33  ? -40.176 4.809   -27.592 1.00 67.17  ? 33   THR A N   1 
ATOM   239  C CA  . THR A 1 33  ? -41.106 4.726   -26.464 1.00 66.45  ? 33   THR A CA  1 
ATOM   240  C C   . THR A 1 33  ? -42.082 5.873   -26.407 1.00 70.61  ? 33   THR A C   1 
ATOM   241  O O   . THR A 1 33  ? -41.688 7.036   -26.476 1.00 69.33  ? 33   THR A O   1 
ATOM   242  C CB  . THR A 1 33  ? -40.362 4.601   -25.148 1.00 76.80  ? 33   THR A CB  1 
ATOM   243  O OG1 . THR A 1 33  ? -39.530 5.745   -24.982 1.00 79.85  ? 33   THR A OG1 1 
ATOM   244  C CG2 . THR A 1 33  ? -39.530 3.344   -25.070 1.00 76.89  ? 33   THR A CG2 1 
ATOM   245  N N   . MET A 1 34  ? -43.363 5.534   -26.232 1.00 68.71  ? 34   MET A N   1 
ATOM   246  C CA  . MET A 1 34  ? -44.489 6.465   -26.174 1.00 68.39  ? 34   MET A CA  1 
ATOM   247  C C   . MET A 1 34  ? -45.373 6.191   -24.979 1.00 72.16  ? 34   MET A C   1 
ATOM   248  O O   . MET A 1 34  ? -45.512 5.048   -24.557 1.00 71.56  ? 34   MET A O   1 
ATOM   249  C CB  . MET A 1 34  ? -45.337 6.334   -27.438 1.00 70.83  ? 34   MET A CB  1 
ATOM   250  C CG  . MET A 1 34  ? -44.553 6.467   -28.723 1.00 75.07  ? 34   MET A CG  1 
ATOM   251  S SD  . MET A 1 34  ? -45.443 5.745   -30.123 1.00 80.31  ? 34   MET A SD  1 
ATOM   252  C CE  . MET A 1 34  ? -46.548 7.128   -30.514 1.00 77.61  ? 34   MET A CE  1 
ATOM   253  N N   . ALA A 1 35  ? -45.995 7.244   -24.448 1.00 69.87  ? 35   ALA A N   1 
ATOM   254  C CA  . ALA A 1 35  ? -46.947 7.204   -23.329 1.00 69.72  ? 35   ALA A CA  1 
ATOM   255  C C   . ALA A 1 35  ? -47.854 8.417   -23.450 1.00 74.29  ? 35   ALA A C   1 
ATOM   256  O O   . ALA A 1 35  ? -47.393 9.449   -23.960 1.00 74.08  ? 35   ALA A O   1 
ATOM   257  C CB  . ALA A 1 35  ? -46.204 7.240   -22.002 1.00 70.19  ? 35   ALA A CB  1 
ATOM   258  N N   . LYS A 1 36  ? -49.138 8.305   -23.014 1.00 71.04  ? 36   LYS A N   1 
ATOM   259  C CA  . LYS A 1 36  ? -50.074 9.440   -23.097 1.00 70.97  ? 36   LYS A CA  1 
ATOM   260  C C   . LYS A 1 36  ? -49.583 10.618  -22.275 1.00 75.90  ? 36   LYS A C   1 
ATOM   261  O O   . LYS A 1 36  ? -49.228 10.446  -21.104 1.00 75.46  ? 36   LYS A O   1 
ATOM   262  C CB  . LYS A 1 36  ? -51.515 9.072   -22.732 1.00 73.24  ? 36   LYS A CB  1 
ATOM   263  C CG  . LYS A 1 36  ? -52.522 10.155  -23.086 1.00 101.64 ? 36   LYS A CG  1 
ATOM   264  C CD  . LYS A 1 36  ? -53.967 9.771   -22.772 1.00 123.37 ? 36   LYS A CD  1 
ATOM   265  C CE  . LYS A 1 36  ? -54.925 10.931  -22.989 1.00 139.45 ? 36   LYS A CE  1 
ATOM   266  N NZ  . LYS A 1 36  ? -55.917 10.694  -24.091 1.00 146.90 ? 36   LYS A NZ  1 
ATOM   267  N N   . ASN A 1 37  ? -49.509 11.802  -22.937 1.00 72.96  ? 37   ASN A N   1 
ATOM   268  C CA  . ASN A 1 37  ? -49.063 13.106  -22.417 1.00 72.20  ? 37   ASN A CA  1 
ATOM   269  C C   . ASN A 1 37  ? -47.613 13.065  -21.906 1.00 74.54  ? 37   ASN A C   1 
ATOM   270  O O   . ASN A 1 37  ? -47.239 13.795  -20.991 1.00 74.99  ? 37   ASN A O   1 
ATOM   271  C CB  . ASN A 1 37  ? -50.048 13.702  -21.385 1.00 69.53  ? 37   ASN A CB  1 
ATOM   272  C CG  . ASN A 1 37  ? -51.406 13.943  -21.968 1.00 98.72  ? 37   ASN A CG  1 
ATOM   273  O OD1 . ASN A 1 37  ? -52.386 13.259  -21.633 1.00 100.63 ? 37   ASN A OD1 1 
ATOM   274  N ND2 . ASN A 1 37  ? -51.472 14.846  -22.932 1.00 89.90  ? 37   ASN A ND2 1 
ATOM   275  N N   . LYS A 1 38  ? -46.794 12.236  -22.545 1.00 69.27  ? 38   LYS A N   1 
ATOM   276  C CA  . LYS A 1 38  ? -45.373 12.100  -22.243 1.00 68.50  ? 38   LYS A CA  1 
ATOM   277  C C   . LYS A 1 38  ? -44.634 12.148  -23.580 1.00 70.33  ? 38   LYS A C   1 
ATOM   278  O O   . LYS A 1 38  ? -45.195 11.753  -24.615 1.00 69.70  ? 38   LYS A O   1 
ATOM   279  C CB  . LYS A 1 38  ? -45.054 10.800  -21.463 1.00 70.57  ? 38   LYS A CB  1 
ATOM   280  C CG  . LYS A 1 38  ? -45.717 10.673  -20.083 1.00 82.13  ? 38   LYS A CG  1 
ATOM   281  C CD  . LYS A 1 38  ? -45.069 11.525  -19.000 1.00 87.66  ? 38   LYS A CD  1 
ATOM   282  C CE  . LYS A 1 38  ? -45.751 11.323  -17.669 1.00 92.25  ? 38   LYS A CE  1 
ATOM   283  N NZ  . LYS A 1 38  ? -45.073 12.071  -16.575 1.00 96.78  ? 38   LYS A NZ  1 
ATOM   284  N N   . PRO A 1 39  ? -43.397 12.655  -23.598 1.00 65.67  ? 39   PRO A N   1 
ATOM   285  C CA  . PRO A 1 39  ? -42.691 12.760  -24.870 1.00 66.14  ? 39   PRO A CA  1 
ATOM   286  C C   . PRO A 1 39  ? -42.198 11.436  -25.421 1.00 69.35  ? 39   PRO A C   1 
ATOM   287  O O   . PRO A 1 39  ? -41.821 10.536  -24.660 1.00 70.19  ? 39   PRO A O   1 
ATOM   288  C CB  . PRO A 1 39  ? -41.519 13.689  -24.559 1.00 68.62  ? 39   PRO A CB  1 
ATOM   289  C CG  . PRO A 1 39  ? -41.693 14.124  -23.151 1.00 72.77  ? 39   PRO A CG  1 
ATOM   290  C CD  . PRO A 1 39  ? -42.582 13.172  -22.487 1.00 67.60  ? 39   PRO A CD  1 
ATOM   291  N N   . THR A 1 40  ? -42.189 11.329  -26.755 1.00 63.42  ? 40   THR A N   1 
ATOM   292  C CA  . THR A 1 40  ? -41.701 10.146  -27.442 1.00 61.97  ? 40   THR A CA  1 
ATOM   293  C C   . THR A 1 40  ? -40.167 10.150  -27.415 1.00 64.38  ? 40   THR A C   1 
ATOM   294  O O   . THR A 1 40  ? -39.545 11.160  -27.738 1.00 65.45  ? 40   THR A O   1 
ATOM   295  C CB  . THR A 1 40  ? -42.362 10.031  -28.806 1.00 65.76  ? 40   THR A CB  1 
ATOM   296  O OG1 . THR A 1 40  ? -43.767 9.834   -28.596 1.00 66.10  ? 40   THR A OG1 1 
ATOM   297  C CG2 . THR A 1 40  ? -41.806 8.893   -29.626 1.00 63.36  ? 40   THR A CG2 1 
ATOM   298  N N   . LEU A 1 41  ? -39.570 9.042   -26.957 1.00 58.63  ? 41   LEU A N   1 
ATOM   299  C CA  . LEU A 1 41  ? -38.113 8.905   -26.844 1.00 57.20  ? 41   LEU A CA  1 
ATOM   300  C C   . LEU A 1 41  ? -37.523 7.754   -27.659 1.00 59.81  ? 41   LEU A C   1 
ATOM   301  O O   . LEU A 1 41  ? -38.132 6.674   -27.788 1.00 55.57  ? 41   LEU A O   1 
ATOM   302  C CB  . LEU A 1 41  ? -37.685 8.733   -25.388 1.00 56.71  ? 41   LEU A CB  1 
ATOM   303  C CG  . LEU A 1 41  ? -37.973 9.833   -24.416 1.00 59.42  ? 41   LEU A CG  1 
ATOM   304  C CD1 . LEU A 1 41  ? -37.666 9.357   -23.046 1.00 59.89  ? 41   LEU A CD1 1 
ATOM   305  C CD2 . LEU A 1 41  ? -37.144 11.033  -24.689 1.00 58.38  ? 41   LEU A CD2 1 
ATOM   306  N N   . ASP A 1 42  ? -36.286 7.993   -28.150 1.00 58.74  ? 42   ASP A N   1 
ATOM   307  C CA  . ASP A 1 42  ? -35.504 7.053   -28.942 1.00 60.01  ? 42   ASP A CA  1 
ATOM   308  C C   . ASP A 1 42  ? -34.284 6.562   -28.177 1.00 65.00  ? 42   ASP A C   1 
ATOM   309  O O   . ASP A 1 42  ? -33.510 7.370   -27.692 1.00 63.97  ? 42   ASP A O   1 
ATOM   310  C CB  . ASP A 1 42  ? -35.118 7.683   -30.291 1.00 62.12  ? 42   ASP A CB  1 
ATOM   311  C CG  . ASP A 1 42  ? -36.170 7.548   -31.379 1.00 73.71  ? 42   ASP A CG  1 
ATOM   312  O OD1 . ASP A 1 42  ? -37.354 7.308   -31.043 1.00 75.41  ? 42   ASP A OD1 1 
ATOM   313  O OD2 . ASP A 1 42  ? -35.802 7.618   -32.563 1.00 78.25  ? 42   ASP A OD2 1 
ATOM   314  N N   . PHE A 1 43  ? -34.128 5.238   -28.053 1.00 63.99  ? 43   PHE A N   1 
ATOM   315  C CA  . PHE A 1 43  ? -33.017 4.632   -27.320 1.00 64.97  ? 43   PHE A CA  1 
ATOM   316  C C   . PHE A 1 43  ? -32.181 3.700   -28.179 1.00 69.74  ? 43   PHE A C   1 
ATOM   317  O O   . PHE A 1 43  ? -32.726 2.854   -28.908 1.00 69.22  ? 43   PHE A O   1 
ATOM   318  C CB  . PHE A 1 43  ? -33.550 3.826   -26.134 1.00 67.24  ? 43   PHE A CB  1 
ATOM   319  C CG  . PHE A 1 43  ? -34.351 4.595   -25.126 1.00 69.03  ? 43   PHE A CG  1 
ATOM   320  C CD1 . PHE A 1 43  ? -35.723 4.728   -25.264 1.00 72.06  ? 43   PHE A CD1 1 
ATOM   321  C CD2 . PHE A 1 43  ? -33.744 5.140   -24.009 1.00 72.50  ? 43   PHE A CD2 1 
ATOM   322  C CE1 . PHE A 1 43  ? -36.468 5.427   -24.318 1.00 75.63  ? 43   PHE A CE1 1 
ATOM   323  C CE2 . PHE A 1 43  ? -34.491 5.817   -23.054 1.00 73.77  ? 43   PHE A CE2 1 
ATOM   324  C CZ  . PHE A 1 43  ? -35.843 5.976   -23.223 1.00 73.81  ? 43   PHE A CZ  1 
ATOM   325  N N   . GLU A 1 44  ? -30.858 3.814   -28.033 1.00 68.09  ? 44   GLU A N   1 
ATOM   326  C CA  . GLU A 1 44  ? -29.878 2.958   -28.702 1.00 69.91  ? 44   GLU A CA  1 
ATOM   327  C C   . GLU A 1 44  ? -28.744 2.590   -27.732 1.00 79.38  ? 44   GLU A C   1 
ATOM   328  O O   . GLU A 1 44  ? -28.352 3.409   -26.889 1.00 78.90  ? 44   GLU A O   1 
ATOM   329  C CB  . GLU A 1 44  ? -29.279 3.649   -29.935 1.00 70.85  ? 44   GLU A CB  1 
ATOM   330  C CG  . GLU A 1 44  ? -28.733 2.665   -30.953 1.00 78.91  ? 44   GLU A CG  1 
ATOM   331  C CD  . GLU A 1 44  ? -28.182 3.236   -32.242 1.00 104.73 ? 44   GLU A CD  1 
ATOM   332  O OE1 . GLU A 1 44  ? -28.812 4.158   -32.807 1.00 105.39 ? 44   GLU A OE1 1 
ATOM   333  O OE2 . GLU A 1 44  ? -27.168 2.693   -32.738 1.00 102.08 ? 44   GLU A OE2 1 
ATOM   334  N N   . LEU A 1 45  ? -28.226 1.362   -27.857 1.00 78.32  ? 45   LEU A N   1 
ATOM   335  C CA  . LEU A 1 45  ? -27.068 0.926   -27.098 1.00 78.96  ? 45   LEU A CA  1 
ATOM   336  C C   . LEU A 1 45  ? -25.918 1.133   -28.055 1.00 85.71  ? 45   LEU A C   1 
ATOM   337  O O   . LEU A 1 45  ? -25.862 0.456   -29.078 1.00 86.39  ? 45   LEU A O   1 
ATOM   338  C CB  . LEU A 1 45  ? -27.214 -0.546  -26.718 1.00 78.98  ? 45   LEU A CB  1 
ATOM   339  C CG  . LEU A 1 45  ? -26.116 -1.164  -25.882 1.00 82.78  ? 45   LEU A CG  1 
ATOM   340  C CD1 . LEU A 1 45  ? -25.781 -0.311  -24.663 1.00 82.35  ? 45   LEU A CD1 1 
ATOM   341  C CD2 . LEU A 1 45  ? -26.512 -2.556  -25.471 1.00 84.83  ? 45   LEU A CD2 1 
ATOM   342  N N   . ILE A 1 46  ? -25.076 2.136   -27.787 1.00 84.38  ? 46   ILE A N   1 
ATOM   343  C CA  . ILE A 1 46  ? -23.954 2.539   -28.628 1.00 86.10  ? 46   ILE A CA  1 
ATOM   344  C C   . ILE A 1 46  ? -22.716 1.638   -28.444 1.00 93.59  ? 46   ILE A C   1 
ATOM   345  O O   . ILE A 1 46  ? -22.169 1.169   -29.451 1.00 93.06  ? 46   ILE A O   1 
ATOM   346  C CB  . ILE A 1 46  ? -23.661 4.055   -28.435 1.00 90.03  ? 46   ILE A CB  1 
ATOM   347  C CG1 . ILE A 1 46  ? -24.694 4.907   -29.180 1.00 90.35  ? 46   ILE A CG1 1 
ATOM   348  C CG2 . ILE A 1 46  ? -22.220 4.464   -28.827 1.00 93.01  ? 46   ILE A CG2 1 
ATOM   349  C CD1 . ILE A 1 46  ? -24.885 4.602   -30.729 1.00 101.87 ? 46   ILE A CD1 1 
ATOM   350  N N   . LYS A 1 47  ? -22.270 1.407   -27.183 1.00 93.03  ? 47   LYS A N   1 
ATOM   351  C CA  . LYS A 1 47  ? -21.120 0.538   -26.900 1.00 93.83  ? 47   LYS A CA  1 
ATOM   352  C C   . LYS A 1 47  ? -21.208 -0.184  -25.555 1.00 99.05  ? 47   LYS A C   1 
ATOM   353  O O   . LYS A 1 47  ? -21.813 0.308   -24.603 1.00 97.45  ? 47   LYS A O   1 
ATOM   354  C CB  . LYS A 1 47  ? -19.768 1.281   -27.047 1.00 96.62  ? 47   LYS A CB  1 
ATOM   355  C CG  . LYS A 1 47  ? -19.466 2.325   -25.984 1.00 112.62 ? 47   LYS A CG  1 
ATOM   356  C CD  . LYS A 1 47  ? -18.394 3.308   -26.446 1.00 121.92 ? 47   LYS A CD  1 
ATOM   357  C CE  . LYS A 1 47  ? -18.245 4.484   -25.507 1.00 128.87 ? 47   LYS A CE  1 
ATOM   358  N NZ  . LYS A 1 47  ? -17.268 4.197   -24.422 1.00 131.39 ? 47   LYS A NZ  1 
ATOM   359  N N   . THR A 1 48  ? -20.599 -1.373  -25.519 1.00 98.94  ? 48   THR A N   1 
ATOM   360  C CA  . THR A 1 48  ? -20.413 -2.261  -24.366 1.00 100.37 ? 48   THR A CA  1 
ATOM   361  C C   . THR A 1 48  ? -18.881 -2.340  -24.234 1.00 108.61 ? 48   THR A C   1 
ATOM   362  O O   . THR A 1 48  ? -18.191 -2.475  -25.255 1.00 108.14 ? 48   THR A O   1 
ATOM   363  C CB  . THR A 1 48  ? -21.079 -3.625  -24.620 1.00 107.46 ? 48   THR A CB  1 
ATOM   364  O OG1 . THR A 1 48  ? -22.429 -3.445  -25.058 1.00 104.90 ? 48   THR A OG1 1 
ATOM   365  C CG2 . THR A 1 48  ? -21.041 -4.530  -23.409 1.00 106.60 ? 48   THR A CG2 1 
ATOM   366  N N   . GLU A 1 49  ? -18.347 -2.173  -23.002 1.00 108.11 ? 49   GLU A N   1 
ATOM   367  C CA  . GLU A 1 49  ? -16.897 -2.105  -22.762 1.00 108.60 ? 49   GLU A CA  1 
ATOM   368  C C   . GLU A 1 49  ? -16.448 -2.714  -21.411 1.00 113.33 ? 49   GLU A C   1 
ATOM   369  O O   . GLU A 1 49  ? -17.172 -2.624  -20.413 1.00 112.15 ? 49   GLU A O   1 
ATOM   370  C CB  . GLU A 1 49  ? -16.460 -0.627  -22.861 1.00 109.91 ? 49   GLU A CB  1 
ATOM   371  C CG  . GLU A 1 49  ? -14.966 -0.374  -22.831 1.00 122.71 ? 49   GLU A CG  1 
ATOM   372  C CD  . GLU A 1 49  ? -14.532 0.602   -21.754 1.00 152.83 ? 49   GLU A CD  1 
ATOM   373  O OE1 . GLU A 1 49  ? -14.852 1.807   -21.876 1.00 145.99 ? 49   GLU A OE1 1 
ATOM   374  O OE2 . GLU A 1 49  ? -13.874 0.161   -20.784 1.00 161.11 ? 49   GLU A OE2 1 
ATOM   375  N N   . ALA A 1 50  ? -15.230 -3.313  -21.394 1.00 110.63 ? 50   ALA A N   1 
ATOM   376  C CA  . ALA A 1 50  ? -14.609 -3.884  -20.204 1.00 110.20 ? 50   ALA A CA  1 
ATOM   377  C C   . ALA A 1 50  ? -13.538 -2.914  -19.690 1.00 114.35 ? 50   ALA A C   1 
ATOM   378  O O   . ALA A 1 50  ? -12.622 -2.534  -20.431 1.00 112.72 ? 50   ALA A O   1 
ATOM   379  C CB  . ALA A 1 50  ? -14.015 -5.242  -20.526 1.00 110.73 ? 50   ALA A CB  1 
ATOM   380  N N   . LYS A 1 51  ? -13.712 -2.440  -18.445 1.00 112.93 ? 51   LYS A N   1 
ATOM   381  C CA  . LYS A 1 51  ? -12.777 -1.504  -17.810 1.00 113.74 ? 51   LYS A CA  1 
ATOM   382  C C   . LYS A 1 51  ? -11.603 -2.277  -17.147 1.00 119.58 ? 51   LYS A C   1 
ATOM   383  O O   . LYS A 1 51  ? -11.790 -2.922  -16.107 1.00 120.00 ? 51   LYS A O   1 
ATOM   384  C CB  . LYS A 1 51  ? -13.501 -0.568  -16.811 1.00 115.53 ? 51   LYS A CB  1 
ATOM   385  C CG  . LYS A 1 51  ? -14.106 0.684   -17.446 1.00 118.97 ? 51   LYS A CG  1 
ATOM   386  C CD  . LYS A 1 51  ? -13.890 1.958   -16.595 1.00 121.74 ? 51   LYS A CD  1 
ATOM   387  C CE  . LYS A 1 51  ? -14.449 3.208   -17.256 1.00 119.36 ? 51   LYS A CE  1 
ATOM   388  N NZ  . LYS A 1 51  ? -13.800 4.466   -16.774 1.00 117.04 ? 51   LYS A NZ  1 
ATOM   389  N N   . GLN A 1 52  ? -10.403 -2.233  -17.786 1.00 115.30 ? 52   GLN A N   1 
ATOM   390  C CA  . GLN A 1 52  ? -9.173  -2.899  -17.341 1.00 114.64 ? 52   GLN A CA  1 
ATOM   391  C C   . GLN A 1 52  ? -9.345  -4.456  -17.083 1.00 114.71 ? 52   GLN A C   1 
ATOM   392  O O   . GLN A 1 52  ? -9.389  -4.899  -15.921 1.00 113.50 ? 52   GLN A O   1 
ATOM   393  C CB  . GLN A 1 52  ? -8.556  -2.165  -16.121 1.00 116.41 ? 52   GLN A CB  1 
ATOM   394  C CG  . GLN A 1 52  ? -7.025  -2.027  -16.173 1.00 137.59 ? 52   GLN A CG  1 
ATOM   395  C CD  . GLN A 1 52  ? -6.463  -1.395  -14.923 1.00 158.15 ? 52   GLN A CD  1 
ATOM   396  O OE1 . GLN A 1 52  ? -6.603  -0.193  -14.703 1.00 155.43 ? 52   GLN A OE1 1 
ATOM   397  N NE2 . GLN A 1 52  ? -5.799  -2.188  -14.087 1.00 146.75 ? 52   GLN A NE2 1 
ATOM   398  N N   . PRO A 1 53  ? -9.423  -5.289  -18.161 1.00 108.14 ? 53   PRO A N   1 
ATOM   399  C CA  . PRO A 1 53  ? -9.534  -6.747  -17.946 1.00 106.02 ? 53   PRO A CA  1 
ATOM   400  C C   . PRO A 1 53  ? -8.158  -7.396  -17.820 1.00 105.43 ? 53   PRO A C   1 
ATOM   401  O O   . PRO A 1 53  ? -7.205  -7.011  -18.517 1.00 105.16 ? 53   PRO A O   1 
ATOM   402  C CB  . PRO A 1 53  ? -10.275 -7.238  -19.189 1.00 107.66 ? 53   PRO A CB  1 
ATOM   403  C CG  . PRO A 1 53  ? -10.035 -6.175  -20.247 1.00 112.64 ? 53   PRO A CG  1 
ATOM   404  C CD  . PRO A 1 53  ? -9.417  -4.956  -19.607 1.00 108.85 ? 53   PRO A CD  1 
ATOM   405  N N   . ALA A 1 54  ? -8.046  -8.383  -16.933 1.00 98.01  ? 54   ALA A N   1 
ATOM   406  C CA  . ALA A 1 54  ? -6.764  -9.056  -16.712 1.00 95.86  ? 54   ALA A CA  1 
ATOM   407  C C   . ALA A 1 54  ? -6.489  -10.114 -17.777 1.00 94.09  ? 54   ALA A C   1 
ATOM   408  O O   . ALA A 1 54  ? -7.265  -11.061 -17.860 1.00 93.70  ? 54   ALA A O   1 
ATOM   409  C CB  . ALA A 1 54  ? -6.736  -9.689  -15.321 1.00 96.63  ? 54   ALA A CB  1 
ATOM   410  N N   . THR A 1 55  ? -5.376  -9.997  -18.567 1.00 85.17  ? 55   THR A N   1 
ATOM   411  C CA  . THR A 1 55  ? -4.989  -11.026 -19.562 1.00 81.69  ? 55   THR A CA  1 
ATOM   412  C C   . THR A 1 55  ? -4.756  -12.344 -18.798 1.00 76.54  ? 55   THR A C   1 
ATOM   413  O O   . THR A 1 55  ? -3.799  -12.438 -18.036 1.00 76.67  ? 55   THR A O   1 
ATOM   414  C CB  . THR A 1 55  ? -3.743  -10.584 -20.358 1.00 91.61  ? 55   THR A CB  1 
ATOM   415  O OG1 . THR A 1 55  ? -4.084  -9.445  -21.142 1.00 96.81  ? 55   THR A OG1 1 
ATOM   416  C CG2 . THR A 1 55  ? -3.218  -11.672 -21.282 1.00 90.17  ? 55   THR A CG2 1 
ATOM   417  N N   . LEU A 1 56  ? -5.676  -13.310 -18.915 1.00 65.45  ? 56   LEU A N   1 
ATOM   418  C CA  . LEU A 1 56  ? -5.542  -14.557 -18.169 1.00 61.97  ? 56   LEU A CA  1 
ATOM   419  C C   . LEU A 1 56  ? -4.331  -15.320 -18.668 1.00 64.80  ? 56   LEU A C   1 
ATOM   420  O O   . LEU A 1 56  ? -3.374  -15.495 -17.925 1.00 64.55  ? 56   LEU A O   1 
ATOM   421  C CB  . LEU A 1 56  ? -6.840  -15.409 -18.265 1.00 60.47  ? 56   LEU A CB  1 
ATOM   422  C CG  . LEU A 1 56  ? -6.925  -16.756 -17.547 1.00 61.89  ? 56   LEU A CG  1 
ATOM   423  C CD1 . LEU A 1 56  ? -6.384  -16.684 -16.160 1.00 61.46  ? 56   LEU A CD1 1 
ATOM   424  C CD2 . LEU A 1 56  ? -8.344  -17.221 -17.464 1.00 60.92  ? 56   LEU A CD2 1 
ATOM   425  N N   . ARG A 1 57  ? -4.348  -15.691 -19.949 1.00 60.25  ? 57   ARG A N   1 
ATOM   426  C CA  . ARG A 1 57  ? -3.334  -16.505 -20.589 1.00 59.17  ? 57   ARG A CA  1 
ATOM   427  C C   . ARG A 1 57  ? -3.302  -16.166 -22.090 1.00 61.47  ? 57   ARG A C   1 
ATOM   428  O O   . ARG A 1 57  ? -4.307  -15.733 -22.634 1.00 63.10  ? 57   ARG A O   1 
ATOM   429  C CB  . ARG A 1 57  ? -3.730  -17.966 -20.336 1.00 59.31  ? 57   ARG A CB  1 
ATOM   430  C CG  . ARG A 1 57  ? -2.748  -19.028 -20.734 1.00 75.48  ? 57   ARG A CG  1 
ATOM   431  C CD  . ARG A 1 57  ? -3.335  -20.387 -20.406 1.00 86.17  ? 57   ARG A CD  1 
ATOM   432  N NE  . ARG A 1 57  ? -3.031  -20.816 -19.040 1.00 90.26  ? 57   ARG A NE  1 
ATOM   433  C CZ  . ARG A 1 57  ? -3.343  -22.011 -18.542 1.00 97.75  ? 57   ARG A CZ  1 
ATOM   434  N NH1 . ARG A 1 57  ? -4.009  -22.894 -19.279 1.00 79.37  ? 57   ARG A NH1 1 
ATOM   435  N NH2 . ARG A 1 57  ? -3.005  -22.328 -17.300 1.00 78.65  ? 57   ARG A NH2 1 
ATOM   436  N N   . LYS A 1 58  ? -2.141  -16.304 -22.730 1.00 54.47  ? 58   LYS A N   1 
ATOM   437  C CA  . LYS A 1 58  ? -1.902  -16.036 -24.139 1.00 52.68  ? 58   LYS A CA  1 
ATOM   438  C C   . LYS A 1 58  ? -1.410  -17.358 -24.746 1.00 60.01  ? 58   LYS A C   1 
ATOM   439  O O   . LYS A 1 58  ? -0.471  -17.948 -24.213 1.00 62.40  ? 58   LYS A O   1 
ATOM   440  C CB  . LYS A 1 58  ? -0.829  -14.940 -24.257 1.00 54.05  ? 58   LYS A CB  1 
ATOM   441  C CG  . LYS A 1 58  ? -0.433  -14.543 -25.687 1.00 67.82  ? 58   LYS A CG  1 
ATOM   442  C CD  . LYS A 1 58  ? 0.869   -13.745 -25.761 1.00 76.03  ? 58   LYS A CD  1 
ATOM   443  C CE  . LYS A 1 58  ? 0.732   -12.263 -25.424 1.00 98.91  ? 58   LYS A CE  1 
ATOM   444  N NZ  . LYS A 1 58  ? 2.053   -11.565 -25.316 1.00 112.75 ? 58   LYS A NZ  1 
ATOM   445  N N   . TYR A 1 59  ? -2.061  -17.855 -25.825 1.00 55.94  ? 59   TYR A N   1 
ATOM   446  C CA  . TYR A 1 59  ? -1.678  -19.120 -26.468 1.00 54.12  ? 59   TYR A CA  1 
ATOM   447  C C   . TYR A 1 59  ? -1.059  -18.944 -27.824 1.00 60.20  ? 59   TYR A C   1 
ATOM   448  O O   . TYR A 1 59  ? -1.454  -18.061 -28.566 1.00 59.77  ? 59   TYR A O   1 
ATOM   449  C CB  . TYR A 1 59  ? -2.879  -20.029 -26.669 1.00 53.46  ? 59   TYR A CB  1 
ATOM   450  C CG  . TYR A 1 59  ? -3.449  -20.642 -25.421 1.00 54.57  ? 59   TYR A CG  1 
ATOM   451  C CD1 . TYR A 1 59  ? -2.994  -21.873 -24.955 1.00 55.48  ? 59   TYR A CD1 1 
ATOM   452  C CD2 . TYR A 1 59  ? -4.560  -20.084 -24.802 1.00 55.74  ? 59   TYR A CD2 1 
ATOM   453  C CE1 . TYR A 1 59  ? -3.610  -22.506 -23.878 1.00 54.31  ? 59   TYR A CE1 1 
ATOM   454  C CE2 . TYR A 1 59  ? -5.192  -20.714 -23.733 1.00 55.92  ? 59   TYR A CE2 1 
ATOM   455  C CZ  . TYR A 1 59  ? -4.711  -21.915 -23.267 1.00 57.91  ? 59   TYR A CZ  1 
ATOM   456  O OH  . TYR A 1 59  ? -5.332  -22.454 -22.170 1.00 57.18  ? 59   TYR A OH  1 
ATOM   457  N N   . CYS A 1 60  ? -0.160  -19.852 -28.190 1.00 59.86  ? 60   CYS A N   1 
ATOM   458  C CA  . CYS A 1 60  ? 0.439   -19.867 -29.507 1.00 60.93  ? 60   CYS A CA  1 
ATOM   459  C C   . CYS A 1 60  ? -0.369  -20.794 -30.367 1.00 62.13  ? 60   CYS A C   1 
ATOM   460  O O   . CYS A 1 60  ? -0.629  -21.942 -29.983 1.00 61.01  ? 60   CYS A O   1 
ATOM   461  C CB  . CYS A 1 60  ? 1.898   -20.289 -29.471 1.00 63.37  ? 60   CYS A CB  1 
ATOM   462  S SG  . CYS A 1 60  ? 2.750   -19.996 -31.032 1.00 69.16  ? 60   CYS A SG  1 
ATOM   463  N N   . ILE A 1 61  ? -0.796  -20.276 -31.533 1.00 56.99  ? 61   ILE A N   1 
ATOM   464  C CA  . ILE A 1 61  ? -1.620  -20.994 -32.511 1.00 53.46  ? 61   ILE A CA  1 
ATOM   465  C C   . ILE A 1 61  ? -0.837  -21.288 -33.799 1.00 53.36  ? 61   ILE A C   1 
ATOM   466  O O   . ILE A 1 61  ? -1.201  -22.200 -34.513 1.00 50.53  ? 61   ILE A O   1 
ATOM   467  C CB  . ILE A 1 61  ? -2.988  -20.304 -32.750 1.00 54.34  ? 61   ILE A CB  1 
ATOM   468  C CG1 . ILE A 1 61  ? -2.857  -18.890 -33.267 1.00 53.09  ? 61   ILE A CG1 1 
ATOM   469  C CG2 . ILE A 1 61  ? -3.820  -20.338 -31.483 1.00 53.71  ? 61   ILE A CG2 1 
ATOM   470  C CD1 . ILE A 1 61  ? -3.604  -18.679 -34.410 1.00 48.26  ? 61   ILE A CD1 1 
ATOM   471  N N   . GLU A 1 62  ? 0.254   -20.571 -34.044 1.00 51.43  ? 62   GLU A N   1 
ATOM   472  C CA  . GLU A 1 62  ? 1.106   -20.804 -35.212 1.00 53.76  ? 62   GLU A CA  1 
ATOM   473  C C   . GLU A 1 62  ? 2.546   -20.601 -34.810 1.00 59.50  ? 62   GLU A C   1 
ATOM   474  O O   . GLU A 1 62  ? 2.880   -19.535 -34.302 1.00 61.01  ? 62   GLU A O   1 
ATOM   475  C CB  . GLU A 1 62  ? 0.737   -19.885 -36.400 1.00 55.51  ? 62   GLU A CB  1 
ATOM   476  C CG  . GLU A 1 62  ? 1.486   -20.213 -37.678 1.00 68.30  ? 62   GLU A CG  1 
ATOM   477  C CD  . GLU A 1 62  ? 1.042   -19.481 -38.933 1.00 100.70 ? 62   GLU A CD  1 
ATOM   478  O OE1 . GLU A 1 62  ? -0.079  -18.920 -38.948 1.00 89.08  ? 62   GLU A OE1 1 
ATOM   479  O OE2 . GLU A 1 62  ? 1.814   -19.500 -39.921 1.00 100.08 ? 62   GLU A OE2 1 
ATOM   480  N N   . ALA A 1 63  ? 3.397   -21.615 -35.033 1.00 53.92  ? 63   ALA A N   1 
ATOM   481  C CA  . ALA A 1 63  ? 4.786   -21.542 -34.639 1.00 52.97  ? 63   ALA A CA  1 
ATOM   482  C C   . ALA A 1 63  ? 5.761   -21.792 -35.769 1.00 60.28  ? 63   ALA A C   1 
ATOM   483  O O   . ALA A 1 63  ? 5.373   -22.200 -36.874 1.00 59.94  ? 63   ALA A O   1 
ATOM   484  C CB  . ALA A 1 63  ? 5.047   -22.488 -33.493 1.00 53.19  ? 63   ALA A CB  1 
ATOM   485  N N   . LYS A 1 64  ? 7.039   -21.508 -35.489 1.00 59.62  ? 64   LYS A N   1 
ATOM   486  C CA  . LYS A 1 64  ? 8.130   -21.657 -36.434 1.00 61.19  ? 64   LYS A CA  1 
ATOM   487  C C   . LYS A 1 64  ? 9.372   -22.235 -35.731 1.00 68.57  ? 64   LYS A C   1 
ATOM   488  O O   . LYS A 1 64  ? 9.799   -21.697 -34.698 1.00 68.76  ? 64   LYS A O   1 
ATOM   489  C CB  . LYS A 1 64  ? 8.467   -20.309 -37.091 1.00 62.50  ? 64   LYS A CB  1 
ATOM   490  C CG  . LYS A 1 64  ? 9.128   -20.476 -38.453 1.00 77.23  ? 64   LYS A CG  1 
ATOM   491  C CD  . LYS A 1 64  ? 9.332   -19.146 -39.175 1.00 96.02  ? 64   LYS A CD  1 
ATOM   492  C CE  . LYS A 1 64  ? 10.672  -18.457 -38.971 1.00 108.48 ? 64   LYS A CE  1 
ATOM   493  N NZ  . LYS A 1 64  ? 10.904  -18.015 -37.565 1.00 113.36 ? 64   LYS A NZ  1 
ATOM   494  N N   . LEU A 1 65  ? 9.943   -23.331 -36.291 1.00 64.68  ? 65   LEU A N   1 
ATOM   495  C CA  . LEU A 1 65  ? 11.143  -23.915 -35.736 1.00 64.65  ? 65   LEU A CA  1 
ATOM   496  C C   . LEU A 1 65  ? 12.290  -23.555 -36.621 1.00 73.94  ? 65   LEU A C   1 
ATOM   497  O O   . LEU A 1 65  ? 12.260  -23.834 -37.814 1.00 73.74  ? 65   LEU A O   1 
ATOM   498  C CB  . LEU A 1 65  ? 11.058  -25.428 -35.585 1.00 64.10  ? 65   LEU A CB  1 
ATOM   499  C CG  . LEU A 1 65  ? 10.139  -25.994 -34.502 1.00 68.23  ? 65   LEU A CG  1 
ATOM   500  C CD1 . LEU A 1 65  ? 9.988   -27.490 -34.668 1.00 67.77  ? 65   LEU A CD1 1 
ATOM   501  C CD2 . LEU A 1 65  ? 10.627  -25.641 -33.089 1.00 69.75  ? 65   LEU A CD2 1 
ATOM   502  N N   . THR A 1 66  ? 13.295  -22.902 -36.031 1.00 74.78  ? 66   THR A N   1 
ATOM   503  C CA  . THR A 1 66  ? 14.537  -22.438 -36.666 1.00 75.16  ? 66   THR A CA  1 
ATOM   504  C C   . THR A 1 66  ? 15.724  -22.960 -35.861 1.00 79.25  ? 66   THR A C   1 
ATOM   505  O O   . THR A 1 66  ? 15.538  -23.679 -34.872 1.00 79.56  ? 66   THR A O   1 
ATOM   506  C CB  . THR A 1 66  ? 14.562  -20.892 -36.680 1.00 87.26  ? 66   THR A CB  1 
ATOM   507  O OG1 . THR A 1 66  ? 14.305  -20.376 -35.361 1.00 91.16  ? 66   THR A OG1 1 
ATOM   508  C CG2 . THR A 1 66  ? 13.598  -20.306 -37.677 1.00 83.91  ? 66   THR A CG2 1 
ATOM   509  N N   . ASN A 1 67  ? 16.941  -22.596 -36.287 1.00 75.85  ? 67   ASN A N   1 
ATOM   510  C CA  . ASN A 1 67  ? 18.194  -22.912 -35.611 1.00 76.21  ? 67   ASN A CA  1 
ATOM   511  C C   . ASN A 1 67  ? 18.354  -24.388 -35.184 1.00 79.91  ? 67   ASN A C   1 
ATOM   512  O O   . ASN A 1 67  ? 18.911  -24.639 -34.112 1.00 80.94  ? 67   ASN A O   1 
ATOM   513  C CB  . ASN A 1 67  ? 18.369  -21.969 -34.403 1.00 78.42  ? 67   ASN A CB  1 
ATOM   514  C CG  . ASN A 1 67  ? 18.389  -20.513 -34.783 1.00 110.77 ? 67   ASN A CG  1 
ATOM   515  O OD1 . ASN A 1 67  ? 17.342  -19.894 -35.009 1.00 95.83  ? 67   ASN A OD1 1 
ATOM   516  N ND2 . ASN A 1 67  ? 19.617  -19.993 -34.839 1.00 117.97 ? 67   ASN A ND2 1 
ATOM   517  N N   . THR A 1 68  ? 17.873  -25.355 -35.997 1.00 74.04  ? 68   THR A N   1 
ATOM   518  C CA  . THR A 1 68  ? 17.986  -26.773 -35.655 1.00 73.03  ? 68   THR A CA  1 
ATOM   519  C C   . THR A 1 68  ? 19.445  -27.183 -35.595 1.00 75.82  ? 68   THR A C   1 
ATOM   520  O O   . THR A 1 68  ? 20.175  -27.040 -36.573 1.00 75.12  ? 68   THR A O   1 
ATOM   521  C CB  . THR A 1 68  ? 17.125  -27.642 -36.566 1.00 83.02  ? 68   THR A CB  1 
ATOM   522  O OG1 . THR A 1 68  ? 15.767  -27.302 -36.345 1.00 83.60  ? 68   THR A OG1 1 
ATOM   523  C CG2 . THR A 1 68  ? 17.302  -29.129 -36.301 1.00 80.64  ? 68   THR A CG2 1 
ATOM   524  N N   . THR A 1 69  ? 19.859  -27.653 -34.404 1.00 72.57  ? 69   THR A N   1 
ATOM   525  C CA  . THR A 1 69  ? 21.226  -28.066 -34.050 1.00 71.23  ? 69   THR A CA  1 
ATOM   526  C C   . THR A 1 69  ? 21.266  -29.456 -33.391 1.00 69.43  ? 69   THR A C   1 
ATOM   527  O O   . THR A 1 69  ? 20.490  -29.729 -32.479 1.00 68.37  ? 69   THR A O   1 
ATOM   528  C CB  . THR A 1 69  ? 21.878  -26.987 -33.153 1.00 81.80  ? 69   THR A CB  1 
ATOM   529  O OG1 . THR A 1 69  ? 21.054  -26.748 -32.006 1.00 73.70  ? 69   THR A OG1 1 
ATOM   530  C CG2 . THR A 1 69  ? 22.140  -25.673 -33.905 1.00 85.84  ? 69   THR A CG2 1 
ATOM   531  N N   . THR A 1 70  ? 22.169  -30.324 -33.855 1.00 63.69  ? 70   THR A N   1 
ATOM   532  C CA  . THR A 1 70  ? 22.331  -31.669 -33.309 1.00 63.01  ? 70   THR A CA  1 
ATOM   533  C C   . THR A 1 70  ? 23.769  -32.029 -32.861 1.00 67.53  ? 70   THR A C   1 
ATOM   534  O O   . THR A 1 70  ? 24.728  -31.862 -33.633 1.00 67.84  ? 70   THR A O   1 
ATOM   535  C CB  . THR A 1 70  ? 21.811  -32.683 -34.300 1.00 64.43  ? 70   THR A CB  1 
ATOM   536  O OG1 . THR A 1 70  ? 20.414  -32.476 -34.488 1.00 72.39  ? 70   THR A OG1 1 
ATOM   537  C CG2 . THR A 1 70  ? 22.072  -34.098 -33.867 1.00 54.22  ? 70   THR A CG2 1 
ATOM   538  N N   . GLU A 1 71  ? 23.897  -32.553 -31.627 1.00 62.91  ? 71   GLU A N   1 
ATOM   539  C CA  . GLU A 1 71  ? 25.156  -33.074 -31.119 1.00 62.66  ? 71   GLU A CA  1 
ATOM   540  C C   . GLU A 1 71  ? 25.021  -34.558 -30.873 1.00 67.25  ? 71   GLU A C   1 
ATOM   541  O O   . GLU A 1 71  ? 24.071  -35.016 -30.233 1.00 67.46  ? 71   GLU A O   1 
ATOM   542  C CB  . GLU A 1 71  ? 25.658  -32.357 -29.864 1.00 64.29  ? 71   GLU A CB  1 
ATOM   543  C CG  . GLU A 1 71  ? 27.124  -32.644 -29.563 1.00 78.74  ? 71   GLU A CG  1 
ATOM   544  C CD  . GLU A 1 71  ? 27.689  -31.942 -28.345 1.00 123.30 ? 71   GLU A CD  1 
ATOM   545  O OE1 . GLU A 1 71  ? 28.056  -30.751 -28.470 1.00 133.93 ? 71   GLU A OE1 1 
ATOM   546  O OE2 . GLU A 1 71  ? 27.791  -32.587 -27.274 1.00 124.26 ? 71   GLU A OE2 1 
ATOM   547  N N   . SER A 1 72  ? 25.973  -35.317 -31.400 1.00 64.52  ? 72   SER A N   1 
ATOM   548  C CA  . SER A 1 72  ? 26.012  -36.763 -31.233 1.00 64.50  ? 72   SER A CA  1 
ATOM   549  C C   . SER A 1 72  ? 27.285  -37.198 -30.490 1.00 66.80  ? 72   SER A C   1 
ATOM   550  O O   . SER A 1 72  ? 28.181  -36.381 -30.199 1.00 64.98  ? 72   SER A O   1 
ATOM   551  C CB  . SER A 1 72  ? 25.868  -37.465 -32.579 1.00 69.38  ? 72   SER A CB  1 
ATOM   552  O OG  . SER A 1 72  ? 26.717  -36.857 -33.538 1.00 86.93  ? 72   SER A OG  1 
ATOM   553  N N   . ARG A 1 73  ? 27.302  -38.478 -30.104 1.00 63.15  ? 73   ARG A N   1 
ATOM   554  C CA  . ARG A 1 73  ? 28.403  -39.137 -29.410 1.00 62.32  ? 73   ARG A CA  1 
ATOM   555  C C   . ARG A 1 73  ? 28.490  -40.530 -29.963 1.00 64.33  ? 73   ARG A C   1 
ATOM   556  O O   . ARG A 1 73  ? 27.475  -41.117 -30.356 1.00 60.26  ? 73   ARG A O   1 
ATOM   557  C CB  . ARG A 1 73  ? 28.181  -39.194 -27.878 1.00 61.87  ? 73   ARG A CB  1 
ATOM   558  C CG  . ARG A 1 73  ? 28.335  -37.863 -27.132 1.00 65.45  ? 73   ARG A CG  1 
ATOM   559  C CD  . ARG A 1 73  ? 29.754  -37.547 -26.710 1.00 77.47  ? 73   ARG A CD  1 
ATOM   560  N NE  . ARG A 1 73  ? 29.827  -36.402 -25.798 1.00 94.09  ? 73   ARG A NE  1 
ATOM   561  C CZ  . ARG A 1 73  ? 29.975  -35.134 -26.184 1.00 120.06 ? 73   ARG A CZ  1 
ATOM   562  N NH1 . ARG A 1 73  ? 30.062  -34.828 -27.477 1.00 108.13 ? 73   ARG A NH1 1 
ATOM   563  N NH2 . ARG A 1 73  ? 30.025  -34.161 -25.281 1.00 111.17 ? 73   ARG A NH2 1 
ATOM   564  N N   . CYS A 1 74  ? 29.714  -41.049 -30.038 1.00 64.94  ? 74   CYS A N   1 
ATOM   565  C CA  . CYS A 1 74  ? 29.916  -42.402 -30.514 1.00 66.37  ? 74   CYS A CA  1 
ATOM   566  C C   . CYS A 1 74  ? 29.554  -43.345 -29.379 1.00 67.84  ? 74   CYS A C   1 
ATOM   567  O O   . CYS A 1 74  ? 29.496  -42.874 -28.236 1.00 69.26  ? 74   CYS A O   1 
ATOM   568  C CB  . CYS A 1 74  ? 31.350  -42.597 -30.978 1.00 68.10  ? 74   CYS A CB  1 
ATOM   569  S SG  . CYS A 1 74  ? 31.585  -42.229 -32.723 1.00 73.36  ? 74   CYS A SG  1 
ATOM   570  N N   . PRO A 1 75  ? 29.259  -44.651 -29.616 1.00 58.17  ? 75   PRO A N   1 
ATOM   571  C CA  . PRO A 1 75  ? 28.959  -45.519 -28.487 1.00 57.01  ? 75   PRO A CA  1 
ATOM   572  C C   . PRO A 1 75  ? 30.122  -45.472 -27.481 1.00 63.19  ? 75   PRO A C   1 
ATOM   573  O O   . PRO A 1 75  ? 31.283  -45.293 -27.888 1.00 63.79  ? 75   PRO A O   1 
ATOM   574  C CB  . PRO A 1 75  ? 28.827  -46.881 -29.142 1.00 57.76  ? 75   PRO A CB  1 
ATOM   575  C CG  . PRO A 1 75  ? 28.489  -46.597 -30.521 1.00 61.02  ? 75   PRO A CG  1 
ATOM   576  C CD  . PRO A 1 75  ? 29.272  -45.418 -30.869 1.00 57.04  ? 75   PRO A CD  1 
ATOM   577  N N   . THR A 1 76  ? 29.802  -45.557 -26.163 1.00 59.33  ? 76   THR A N   1 
ATOM   578  C CA  . THR A 1 76  ? 30.764  -45.553 -25.040 1.00 58.44  ? 76   THR A CA  1 
ATOM   579  C C   . THR A 1 76  ? 31.410  -44.184 -24.801 1.00 64.88  ? 76   THR A C   1 
ATOM   580  O O   . THR A 1 76  ? 32.211  -44.073 -23.873 1.00 64.34  ? 76   THR A O   1 
ATOM   581  C CB  . THR A 1 76  ? 31.864  -46.681 -25.146 1.00 51.86  ? 76   THR A CB  1 
ATOM   582  O OG1 . THR A 1 76  ? 32.996  -46.214 -25.856 1.00 37.91  ? 76   THR A OG1 1 
ATOM   583  C CG2 . THR A 1 76  ? 31.371  -48.008 -25.771 1.00 50.02  ? 76   THR A CG2 1 
ATOM   584  N N   . GLN A 1 77  ? 31.104  -43.162 -25.633 1.00 63.55  ? 77   GLN A N   1 
ATOM   585  C CA  . GLN A 1 77  ? 31.708  -41.824 -25.497 1.00 64.49  ? 77   GLN A CA  1 
ATOM   586  C C   . GLN A 1 77  ? 30.909  -40.860 -24.604 1.00 70.10  ? 77   GLN A C   1 
ATOM   587  O O   . GLN A 1 77  ? 31.233  -39.672 -24.539 1.00 70.93  ? 77   GLN A O   1 
ATOM   588  C CB  . GLN A 1 77  ? 31.982  -41.172 -26.878 1.00 66.13  ? 77   GLN A CB  1 
ATOM   589  C CG  . GLN A 1 77  ? 32.747  -42.038 -27.866 1.00 93.03  ? 77   GLN A CG  1 
ATOM   590  C CD  . GLN A 1 77  ? 34.238  -42.117 -27.623 1.00 116.16 ? 77   GLN A CD  1 
ATOM   591  O OE1 . GLN A 1 77  ? 34.908  -41.129 -27.281 1.00 109.76 ? 77   GLN A OE1 1 
ATOM   592  N NE2 . GLN A 1 77  ? 34.802  -43.299 -27.860 1.00 109.90 ? 77   GLN A NE2 1 
ATOM   593  N N   . GLY A 1 78  ? 29.871  -41.355 -23.950 1.00 67.38  ? 78   GLY A N   1 
ATOM   594  C CA  . GLY A 1 78  ? 29.034  -40.514 -23.097 1.00 67.61  ? 78   GLY A CA  1 
ATOM   595  C C   . GLY A 1 78  ? 27.751  -40.010 -23.739 1.00 70.42  ? 78   GLY A C   1 
ATOM   596  O O   . GLY A 1 78  ? 27.391  -40.448 -24.840 1.00 69.91  ? 78   GLY A O   1 
ATOM   597  N N   . GLU A 1 79  ? 27.039  -39.108 -23.017 1.00 65.82  ? 79   GLU A N   1 
ATOM   598  C CA  . GLU A 1 79  ? 25.778  -38.475 -23.424 1.00 65.48  ? 79   GLU A CA  1 
ATOM   599  C C   . GLU A 1 79  ? 26.100  -37.077 -24.002 1.00 68.56  ? 79   GLU A C   1 
ATOM   600  O O   . GLU A 1 79  ? 26.931  -36.356 -23.425 1.00 68.99  ? 79   GLU A O   1 
ATOM   601  C CB  . GLU A 1 79  ? 24.837  -38.345 -22.215 1.00 67.32  ? 79   GLU A CB  1 
ATOM   602  C CG  . GLU A 1 79  ? 23.358  -38.583 -22.504 1.00 81.85  ? 79   GLU A CG  1 
ATOM   603  C CD  . GLU A 1 79  ? 22.402  -38.231 -21.372 1.00 100.21 ? 79   GLU A CD  1 
ATOM   604  O OE1 . GLU A 1 79  ? 22.657  -37.236 -20.652 1.00 84.61  ? 79   GLU A OE1 1 
ATOM   605  O OE2 . GLU A 1 79  ? 21.377  -38.937 -21.225 1.00 101.33 ? 79   GLU A OE2 1 
ATOM   606  N N   . PRO A 1 80  ? 25.512  -36.683 -25.154 1.00 63.00  ? 80   PRO A N   1 
ATOM   607  C CA  . PRO A 1 80  ? 25.846  -35.365 -25.713 1.00 62.27  ? 80   PRO A CA  1 
ATOM   608  C C   . PRO A 1 80  ? 25.073  -34.239 -25.054 1.00 67.95  ? 80   PRO A C   1 
ATOM   609  O O   . PRO A 1 80  ? 24.065  -34.478 -24.380 1.00 67.30  ? 80   PRO A O   1 
ATOM   610  C CB  . PRO A 1 80  ? 25.532  -35.510 -27.194 1.00 64.12  ? 80   PRO A CB  1 
ATOM   611  C CG  . PRO A 1 80  ? 24.584  -36.665 -27.288 1.00 69.30  ? 80   PRO A CG  1 
ATOM   612  C CD  . PRO A 1 80  ? 24.509  -37.385 -25.974 1.00 64.73  ? 80   PRO A CD  1 
ATOM   613  N N   . SER A 1 81  ? 25.571  -33.006 -25.209 1.00 66.48  ? 81   SER A N   1 
ATOM   614  C CA  . SER A 1 81  ? 24.948  -31.839 -24.579 1.00 66.52  ? 81   SER A CA  1 
ATOM   615  C C   . SER A 1 81  ? 25.109  -30.550 -25.377 1.00 73.36  ? 81   SER A C   1 
ATOM   616  O O   . SER A 1 81  ? 26.178  -30.308 -25.954 1.00 74.64  ? 81   SER A O   1 
ATOM   617  C CB  . SER A 1 81  ? 25.519  -31.625 -23.182 1.00 65.83  ? 81   SER A CB  1 
ATOM   618  O OG  . SER A 1 81  ? 26.757  -30.935 -23.246 1.00 61.45  ? 81   SER A OG  1 
ATOM   619  N N   . LEU A 1 82  ? 24.060  -29.709 -25.361 1.00 68.90  ? 82   LEU A N   1 
ATOM   620  C CA  . LEU A 1 82  ? 24.060  -28.398 -25.991 1.00 68.48  ? 82   LEU A CA  1 
ATOM   621  C C   . LEU A 1 82  ? 23.686  -27.407 -24.907 1.00 72.62  ? 82   LEU A C   1 
ATOM   622  O O   . LEU A 1 82  ? 23.095  -27.805 -23.902 1.00 72.25  ? 82   LEU A O   1 
ATOM   623  C CB  . LEU A 1 82  ? 23.052  -28.341 -27.166 1.00 68.65  ? 82   LEU A CB  1 
ATOM   624  C CG  . LEU A 1 82  ? 23.246  -29.325 -28.339 1.00 72.88  ? 82   LEU A CG  1 
ATOM   625  C CD1 . LEU A 1 82  ? 22.058  -29.301 -29.291 1.00 72.89  ? 82   LEU A CD1 1 
ATOM   626  C CD2 . LEU A 1 82  ? 24.489  -29.023 -29.108 1.00 73.79  ? 82   LEU A CD2 1 
ATOM   627  N N   . ASN A 1 83  ? 24.054  -26.130 -25.078 1.00 70.40  ? 83   ASN A N   1 
ATOM   628  C CA  . ASN A 1 83  ? 23.713  -25.064 -24.115 1.00 70.90  ? 83   ASN A CA  1 
ATOM   629  C C   . ASN A 1 83  ? 22.198  -24.837 -24.146 1.00 73.53  ? 83   ASN A C   1 
ATOM   630  O O   . ASN A 1 83  ? 21.594  -24.612 -23.108 1.00 70.73  ? 83   ASN A O   1 
ATOM   631  C CB  . ASN A 1 83  ? 24.452  -23.756 -24.446 1.00 74.45  ? 83   ASN A CB  1 
ATOM   632  C CG  . ASN A 1 83  ? 25.927  -23.969 -24.681 1.00 106.30 ? 83   ASN A CG  1 
ATOM   633  O OD1 . ASN A 1 83  ? 26.726  -23.974 -23.733 1.00 99.64  ? 83   ASN A OD1 1 
ATOM   634  N ND2 . ASN A 1 83  ? 26.301  -24.242 -25.942 1.00 96.32  ? 83   ASN A ND2 1 
ATOM   635  N N   . GLU A 1 84  ? 21.593  -24.980 -25.350 1.00 70.73  ? 84   GLU A N   1 
ATOM   636  C CA  . GLU A 1 84  ? 20.171  -24.842 -25.691 1.00 70.67  ? 84   GLU A CA  1 
ATOM   637  C C   . GLU A 1 84  ? 19.273  -25.582 -24.736 1.00 75.45  ? 84   GLU A C   1 
ATOM   638  O O   . GLU A 1 84  ? 18.104  -25.216 -24.579 1.00 75.59  ? 84   GLU A O   1 
ATOM   639  C CB  . GLU A 1 84  ? 19.922  -25.315 -27.131 1.00 71.92  ? 84   GLU A CB  1 
ATOM   640  C CG  . GLU A 1 84  ? 20.446  -24.372 -28.201 1.00 81.31  ? 84   GLU A CG  1 
ATOM   641  C CD  . GLU A 1 84  ? 21.949  -24.185 -28.210 1.00 97.71  ? 84   GLU A CD  1 
ATOM   642  O OE1 . GLU A 1 84  ? 22.446  -23.344 -27.428 1.00 83.40  ? 84   GLU A OE1 1 
ATOM   643  O OE2 . GLU A 1 84  ? 22.637  -24.947 -28.926 1.00 96.81  ? 84   GLU A OE2 1 
ATOM   644  N N   . GLU A 1 85  ? 19.823  -26.621 -24.093 1.00 71.62  ? 85   GLU A N   1 
ATOM   645  C CA  . GLU A 1 85  ? 19.135  -27.395 -23.076 1.00 71.21  ? 85   GLU A CA  1 
ATOM   646  C C   . GLU A 1 85  ? 18.785  -26.463 -21.912 1.00 77.49  ? 85   GLU A C   1 
ATOM   647  O O   . GLU A 1 85  ? 17.635  -26.476 -21.486 1.00 76.64  ? 85   GLU A O   1 
ATOM   648  C CB  . GLU A 1 85  ? 19.985  -28.582 -22.645 1.00 72.05  ? 85   GLU A CB  1 
ATOM   649  C CG  . GLU A 1 85  ? 20.262  -29.543 -23.785 1.00 77.81  ? 85   GLU A CG  1 
ATOM   650  C CD  . GLU A 1 85  ? 21.033  -30.775 -23.363 1.00 91.56  ? 85   GLU A CD  1 
ATOM   651  O OE1 . GLU A 1 85  ? 22.263  -30.665 -23.156 1.00 80.58  ? 85   GLU A OE1 1 
ATOM   652  O OE2 . GLU A 1 85  ? 20.396  -31.836 -23.177 1.00 78.11  ? 85   GLU A OE2 1 
ATOM   653  N N   . GLN A 1 86  ? 19.737  -25.563 -21.506 1.00 77.49  ? 86   GLN A N   1 
ATOM   654  C CA  . GLN A 1 86  ? 19.602  -24.487 -20.472 1.00 78.67  ? 86   GLN A CA  1 
ATOM   655  C C   . GLN A 1 86  ? 18.707  -23.329 -20.998 1.00 83.50  ? 86   GLN A C   1 
ATOM   656  O O   . GLN A 1 86  ? 17.785  -22.915 -20.283 1.00 82.96  ? 86   GLN A O   1 
ATOM   657  C CB  . GLN A 1 86  ? 20.976  -23.894 -20.014 1.00 79.81  ? 86   GLN A CB  1 
ATOM   658  C CG  . GLN A 1 86  ? 22.135  -24.889 -19.846 1.00 91.32  ? 86   GLN A CG  1 
ATOM   659  C CD  . GLN A 1 86  ? 21.793  -26.020 -18.910 1.00 107.68 ? 86   GLN A CD  1 
ATOM   660  O OE1 . GLN A 1 86  ? 21.454  -25.796 -17.743 1.00 105.91 ? 86   GLN A OE1 1 
ATOM   661  N NE2 . GLN A 1 86  ? 21.821  -27.254 -19.419 1.00 93.81  ? 86   GLN A NE2 1 
ATOM   662  N N   . ASP A 1 87  ? 18.993  -22.818 -22.252 1.00 78.68  ? 87   ASP A N   1 
ATOM   663  C CA  . ASP A 1 87  ? 18.252  -21.762 -22.965 1.00 77.18  ? 87   ASP A CA  1 
ATOM   664  C C   . ASP A 1 87  ? 16.773  -22.214 -23.082 1.00 80.19  ? 87   ASP A C   1 
ATOM   665  O O   . ASP A 1 87  ? 16.479  -23.347 -23.494 1.00 79.93  ? 87   ASP A O   1 
ATOM   666  C CB  . ASP A 1 87  ? 18.890  -21.531 -24.352 1.00 78.48  ? 87   ASP A CB  1 
ATOM   667  C CG  . ASP A 1 87  ? 18.768  -20.155 -25.010 1.00 79.76  ? 87   ASP A CG  1 
ATOM   668  O OD1 . ASP A 1 87  ? 17.708  -19.491 -24.826 1.00 76.17  ? 87   ASP A OD1 1 
ATOM   669  O OD2 . ASP A 1 87  ? 19.690  -19.790 -25.807 1.00 82.66  ? 87   ASP A OD2 1 
ATOM   670  N N   . LYS A 1 88  ? 15.860  -21.357 -22.618 1.00 75.45  ? 88   LYS A N   1 
ATOM   671  C CA  . LYS A 1 88  ? 14.436  -21.672 -22.563 1.00 74.60  ? 88   LYS A CA  1 
ATOM   672  C C   . LYS A 1 88  ? 13.669  -21.478 -23.901 1.00 77.61  ? 88   LYS A C   1 
ATOM   673  O O   . LYS A 1 88  ? 12.561  -22.010 -24.050 1.00 77.34  ? 88   LYS A O   1 
ATOM   674  C CB  . LYS A 1 88  ? 13.775  -20.884 -21.416 1.00 76.30  ? 88   LYS A CB  1 
ATOM   675  C CG  . LYS A 1 88  ? 13.472  -21.699 -20.147 1.00 74.81  ? 88   LYS A CG  1 
ATOM   676  C CD  . LYS A 1 88  ? 12.327  -22.722 -20.335 1.00 83.03  ? 88   LYS A CD  1 
ATOM   677  C CE  . LYS A 1 88  ? 10.948  -22.104 -20.437 1.00 94.03  ? 88   LYS A CE  1 
ATOM   678  N NZ  . LYS A 1 88  ? 10.097  -22.790 -21.448 1.00 101.31 ? 88   LYS A NZ  1 
ATOM   679  N N   . ARG A 1 89  ? 14.273  -20.765 -24.876 1.00 72.64  ? 89   ARG A N   1 
ATOM   680  C CA  . ARG A 1 89  ? 13.657  -20.503 -26.184 1.00 71.16  ? 89   ARG A CA  1 
ATOM   681  C C   . ARG A 1 89  ? 13.709  -21.740 -27.065 1.00 74.98  ? 89   ARG A C   1 
ATOM   682  O O   . ARG A 1 89  ? 12.995  -21.806 -28.081 1.00 74.71  ? 89   ARG A O   1 
ATOM   683  C CB  . ARG A 1 89  ? 14.332  -19.318 -26.894 1.00 66.78  ? 89   ARG A CB  1 
ATOM   684  C CG  . ARG A 1 89  ? 14.284  -18.022 -26.095 1.00 69.05  ? 89   ARG A CG  1 
ATOM   685  C CD  . ARG A 1 89  ? 15.172  -16.939 -26.690 1.00 68.85  ? 89   ARG A CD  1 
ATOM   686  N NE  . ARG A 1 89  ? 16.604  -17.222 -26.571 1.00 68.02  ? 89   ARG A NE  1 
ATOM   687  C CZ  . ARG A 1 89  ? 17.537  -16.612 -27.292 1.00 85.75  ? 89   ARG A CZ  1 
ATOM   688  N NH1 . ARG A 1 89  ? 17.199  -15.681 -28.177 1.00 76.01  ? 89   ARG A NH1 1 
ATOM   689  N NH2 . ARG A 1 89  ? 18.819  -16.927 -27.135 1.00 74.69  ? 89   ARG A NH2 1 
ATOM   690  N N   . PHE A 1 90  ? 14.559  -22.720 -26.681 1.00 70.08  ? 90   PHE A N   1 
ATOM   691  C CA  . PHE A 1 90  ? 14.740  -23.938 -27.452 1.00 69.25  ? 90   PHE A CA  1 
ATOM   692  C C   . PHE A 1 90  ? 14.011  -25.115 -26.861 1.00 71.75  ? 90   PHE A C   1 
ATOM   693  O O   . PHE A 1 90  ? 13.811  -25.159 -25.649 1.00 71.47  ? 90   PHE A O   1 
ATOM   694  C CB  . PHE A 1 90  ? 16.227  -24.269 -27.600 1.00 71.12  ? 90   PHE A CB  1 
ATOM   695  C CG  . PHE A 1 90  ? 17.024  -23.239 -28.360 1.00 72.93  ? 90   PHE A CG  1 
ATOM   696  C CD1 . PHE A 1 90  ? 17.584  -22.148 -27.706 1.00 75.64  ? 90   PHE A CD1 1 
ATOM   697  C CD2 . PHE A 1 90  ? 17.240  -23.373 -29.724 1.00 76.03  ? 90   PHE A CD2 1 
ATOM   698  C CE1 . PHE A 1 90  ? 18.325  -21.194 -28.410 1.00 76.42  ? 90   PHE A CE1 1 
ATOM   699  C CE2 . PHE A 1 90  ? 17.980  -22.414 -30.432 1.00 78.55  ? 90   PHE A CE2 1 
ATOM   700  C CZ  . PHE A 1 90  ? 18.506  -21.326 -29.769 1.00 76.12  ? 90   PHE A CZ  1 
ATOM   701  N N   . ILE A 1 91  ? 13.593  -26.059 -27.731 1.00 66.76  ? 91   ILE A N   1 
ATOM   702  C CA  . ILE A 1 91  ? 12.977  -27.323 -27.351 1.00 65.83  ? 91   ILE A CA  1 
ATOM   703  C C   . ILE A 1 91  ? 13.920  -28.448 -27.806 1.00 68.92  ? 91   ILE A C   1 
ATOM   704  O O   . ILE A 1 91  ? 14.293  -28.544 -28.986 1.00 65.84  ? 91   ILE A O   1 
ATOM   705  C CB  . ILE A 1 91  ? 11.492  -27.509 -27.755 1.00 69.16  ? 91   ILE A CB  1 
ATOM   706  C CG1 . ILE A 1 91  ? 10.900  -28.815 -27.137 1.00 69.18  ? 91   ILE A CG1 1 
ATOM   707  C CG2 . ILE A 1 91  ? 11.297  -27.436 -29.285 1.00 71.25  ? 91   ILE A CG2 1 
ATOM   708  C CD1 . ILE A 1 91  ? 9.338   -28.964 -27.075 1.00 71.63  ? 91   ILE A CD1 1 
ATOM   709  N N   . CYS A 1 92  ? 14.354  -29.254 -26.817 1.00 66.92  ? 92   CYS A N   1 
ATOM   710  C CA  . CYS A 1 92  ? 15.315  -30.343 -26.991 1.00 65.71  ? 92   CYS A CA  1 
ATOM   711  C C   . CYS A 1 92  ? 14.751  -31.729 -26.725 1.00 63.89  ? 92   CYS A C   1 
ATOM   712  O O   . CYS A 1 92  ? 13.749  -31.903 -26.011 1.00 62.63  ? 92   CYS A O   1 
ATOM   713  C CB  . CYS A 1 92  ? 16.558  -30.091 -26.152 1.00 66.64  ? 92   CYS A CB  1 
ATOM   714  S SG  . CYS A 1 92  ? 17.283  -28.466 -26.423 1.00 71.87  ? 92   CYS A SG  1 
ATOM   715  N N   . LYS A 1 93  ? 15.432  -32.718 -27.307 1.00 56.15  ? 93   LYS A N   1 
ATOM   716  C CA  . LYS A 1 93  ? 15.142  -34.122 -27.148 1.00 54.38  ? 93   LYS A CA  1 
ATOM   717  C C   . LYS A 1 93  ? 16.413  -34.934 -27.342 1.00 58.28  ? 93   LYS A C   1 
ATOM   718  O O   . LYS A 1 93  ? 17.155  -34.711 -28.307 1.00 57.88  ? 93   LYS A O   1 
ATOM   719  C CB  . LYS A 1 93  ? 14.038  -34.565 -28.125 1.00 55.05  ? 93   LYS A CB  1 
ATOM   720  C CG  . LYS A 1 93  ? 13.806  -36.079 -28.237 1.00 51.41  ? 93   LYS A CG  1 
ATOM   721  C CD  . LYS A 1 93  ? 12.746  -36.620 -27.291 1.00 47.26  ? 93   LYS A CD  1 
ATOM   722  C CE  . LYS A 1 93  ? 12.299  -38.021 -27.648 1.00 57.88  ? 93   LYS A CE  1 
ATOM   723  N NZ  . LYS A 1 93  ? 11.576  -38.089 -28.958 1.00 62.21  ? 93   LYS A NZ  1 
ATOM   724  N N   . HIS A 1 94  ? 16.638  -35.891 -26.421 1.00 53.75  ? 94   HIS A N   1 
ATOM   725  C CA  . HIS A 1 94  ? 17.698  -36.884 -26.489 1.00 52.07  ? 94   HIS A CA  1 
ATOM   726  C C   . HIS A 1 94  ? 17.144  -38.148 -27.124 1.00 56.06  ? 94   HIS A C   1 
ATOM   727  O O   . HIS A 1 94  ? 16.002  -38.530 -26.855 1.00 55.35  ? 94   HIS A O   1 
ATOM   728  C CB  . HIS A 1 94  ? 18.185  -37.238 -25.111 1.00 52.17  ? 94   HIS A CB  1 
ATOM   729  C CG  . HIS A 1 94  ? 19.157  -36.263 -24.567 1.00 56.00  ? 94   HIS A CG  1 
ATOM   730  N ND1 . HIS A 1 94  ? 20.521  -36.493 -24.635 1.00 58.34  ? 94   HIS A ND1 1 
ATOM   731  C CD2 . HIS A 1 94  ? 18.938  -35.082 -23.947 1.00 57.92  ? 94   HIS A CD2 1 
ATOM   732  C CE1 . HIS A 1 94  ? 21.086  -35.450 -24.047 1.00 57.71  ? 94   HIS A CE1 1 
ATOM   733  N NE2 . HIS A 1 94  ? 20.169  -34.581 -23.606 1.00 57.78  ? 94   HIS A NE2 1 
ATOM   734  N N   . SER A 1 95  ? 17.960  -38.805 -27.955 1.00 53.47  ? 95   SER A N   1 
ATOM   735  C CA  . SER A 1 95  ? 17.612  -40.067 -28.578 1.00 54.06  ? 95   SER A CA  1 
ATOM   736  C C   . SER A 1 95  ? 18.871  -40.922 -28.786 1.00 61.26  ? 95   SER A C   1 
ATOM   737  O O   . SER A 1 95  ? 19.933  -40.587 -28.268 1.00 61.39  ? 95   SER A O   1 
ATOM   738  C CB  . SER A 1 95  ? 16.851  -39.831 -29.873 1.00 58.32  ? 95   SER A CB  1 
ATOM   739  O OG  . SER A 1 95  ? 15.741  -40.707 -29.959 1.00 74.87  ? 95   SER A OG  1 
ATOM   740  N N   . MET A 1 96  ? 18.747  -42.027 -29.530 1.00 60.09  ? 96   MET A N   1 
ATOM   741  C CA  . MET A 1 96  ? 19.812  -43.000 -29.804 1.00 60.35  ? 96   MET A CA  1 
ATOM   742  C C   . MET A 1 96  ? 19.824  -43.289 -31.281 1.00 60.49  ? 96   MET A C   1 
ATOM   743  O O   . MET A 1 96  ? 18.781  -43.616 -31.847 1.00 58.97  ? 96   MET A O   1 
ATOM   744  C CB  . MET A 1 96  ? 19.505  -44.354 -29.096 1.00 63.97  ? 96   MET A CB  1 
ATOM   745  C CG  . MET A 1 96  ? 19.404  -44.289 -27.606 1.00 69.11  ? 96   MET A CG  1 
ATOM   746  S SD  . MET A 1 96  ? 20.994  -44.721 -26.945 1.00 75.24  ? 96   MET A SD  1 
ATOM   747  C CE  . MET A 1 96  ? 21.370  -43.246 -25.870 1.00 71.52  ? 96   MET A CE  1 
ATOM   748  N N   . VAL A 1 97  ? 20.999  -43.251 -31.895 1.00 56.51  ? 97   VAL A N   1 
ATOM   749  C CA  . VAL A 1 97  ? 21.165  -43.611 -33.306 1.00 55.87  ? 97   VAL A CA  1 
ATOM   750  C C   . VAL A 1 97  ? 22.144  -44.781 -33.445 1.00 58.27  ? 97   VAL A C   1 
ATOM   751  O O   . VAL A 1 97  ? 22.920  -45.060 -32.528 1.00 57.12  ? 97   VAL A O   1 
ATOM   752  C CB  . VAL A 1 97  ? 21.552  -42.434 -34.236 1.00 59.72  ? 97   VAL A CB  1 
ATOM   753  C CG1 . VAL A 1 97  ? 20.454  -41.374 -34.286 1.00 59.41  ? 97   VAL A CG1 1 
ATOM   754  C CG2 . VAL A 1 97  ? 22.903  -41.834 -33.844 1.00 59.67  ? 97   VAL A CG2 1 
ATOM   755  N N   . ASP A 1 98  ? 22.107  -45.459 -34.599 1.00 53.81  ? 98   ASP A N   1 
ATOM   756  C CA  . ASP A 1 98  ? 23.030  -46.543 -34.890 1.00 52.76  ? 98   ASP A CA  1 
ATOM   757  C C   . ASP A 1 98  ? 24.352  -45.921 -35.284 1.00 59.90  ? 98   ASP A C   1 
ATOM   758  O O   . ASP A 1 98  ? 24.427  -45.085 -36.184 1.00 61.03  ? 98   ASP A O   1 
ATOM   759  C CB  . ASP A 1 98  ? 22.518  -47.425 -36.024 1.00 53.53  ? 98   ASP A CB  1 
ATOM   760  C CG  . ASP A 1 98  ? 21.365  -48.322 -35.662 1.00 63.54  ? 98   ASP A CG  1 
ATOM   761  O OD1 . ASP A 1 98  ? 21.243  -48.674 -34.482 1.00 60.68  ? 98   ASP A OD1 1 
ATOM   762  O OD2 . ASP A 1 98  ? 20.608  -48.721 -36.582 1.00 78.38  ? 98   ASP A OD2 1 
ATOM   763  N N   . ARG A 1 99  ? 25.373  -46.278 -34.559 1.00 57.62  ? 99   ARG A N   1 
ATOM   764  C CA  . ARG A 1 99  ? 26.720  -45.833 -34.804 1.00 58.39  ? 99   ARG A CA  1 
ATOM   765  C C   . ARG A 1 99  ? 27.588  -47.048 -35.133 1.00 65.53  ? 99   ARG A C   1 
ATOM   766  O O   . ARG A 1 99  ? 27.156  -48.187 -34.949 1.00 64.80  ? 99   ARG A O   1 
ATOM   767  C CB  . ARG A 1 99  ? 27.273  -45.009 -33.627 1.00 56.65  ? 99   ARG A CB  1 
ATOM   768  C CG  . ARG A 1 99  ? 26.633  -43.633 -33.396 1.00 61.19  ? 99   ARG A CG  1 
ATOM   769  C CD  . ARG A 1 99  ? 26.573  -42.693 -34.603 1.00 52.06  ? 99   ARG A CD  1 
ATOM   770  N NE  . ARG A 1 99  ? 27.874  -42.158 -35.045 1.00 31.98  ? 99   ARG A NE  1 
ATOM   771  C CZ  . ARG A 1 99  ? 28.449  -41.059 -34.548 1.00 54.87  ? 99   ARG A CZ  1 
ATOM   772  N NH1 . ARG A 1 99  ? 27.900  -40.416 -33.528 1.00 59.60  ? 99   ARG A NH1 1 
ATOM   773  N NH2 . ARG A 1 99  ? 29.604  -40.630 -35.030 1.00 36.57  ? 99   ARG A NH2 1 
ATOM   774  N N   . GLY A 1 100 ? 28.776  -46.772 -35.666 1.00 65.03  ? 100  GLY A N   1 
ATOM   775  C CA  . GLY A 1 100 ? 29.749  -47.758 -36.099 1.00 65.83  ? 100  GLY A CA  1 
ATOM   776  C C   . GLY A 1 100 ? 30.711  -47.197 -37.121 1.00 72.15  ? 100  GLY A C   1 
ATOM   777  O O   . GLY A 1 100 ? 30.721  -45.985 -37.370 1.00 71.28  ? 100  GLY A O   1 
ATOM   778  N N   . TRP A 1 101 ? 31.516  -48.092 -37.727 1.00 70.78  ? 101  TRP A N   1 
ATOM   779  C CA  . TRP A 1 101 ? 32.565  -47.763 -38.690 1.00 71.46  ? 101  TRP A CA  1 
ATOM   780  C C   . TRP A 1 101 ? 32.173  -46.844 -39.839 1.00 70.28  ? 101  TRP A C   1 
ATOM   781  O O   . TRP A 1 101 ? 32.895  -45.867 -40.021 1.00 67.75  ? 101  TRP A O   1 
ATOM   782  C CB  . TRP A 1 101 ? 33.264  -49.008 -39.231 1.00 72.40  ? 101  TRP A CB  1 
ATOM   783  C CG  . TRP A 1 101 ? 34.034  -49.818 -38.224 1.00 75.54  ? 101  TRP A CG  1 
ATOM   784  C CD1 . TRP A 1 101 ? 34.069  -49.651 -36.865 1.00 78.92  ? 101  TRP A CD1 1 
ATOM   785  C CD2 . TRP A 1 101 ? 34.803  -50.995 -38.501 1.00 76.33  ? 101  TRP A CD2 1 
ATOM   786  N NE1 . TRP A 1 101 ? 34.815  -50.648 -36.282 1.00 79.10  ? 101  TRP A NE1 1 
ATOM   787  C CE2 . TRP A 1 101 ? 35.282  -51.486 -37.262 1.00 81.09  ? 101  TRP A CE2 1 
ATOM   788  C CE3 . TRP A 1 101 ? 35.159  -51.672 -39.684 1.00 78.05  ? 101  TRP A CE3 1 
ATOM   789  C CZ2 . TRP A 1 101 ? 36.122  -52.606 -37.176 1.00 80.83  ? 101  TRP A CZ2 1 
ATOM   790  C CZ3 . TRP A 1 101 ? 35.983  -52.782 -39.595 1.00 80.03  ? 101  TRP A CZ3 1 
ATOM   791  C CH2 . TRP A 1 101 ? 36.453  -53.242 -38.354 1.00 80.91  ? 101  TRP A CH2 1 
ATOM   792  N N   . GLY A 1 102 ? 31.085  -47.129 -40.571 1.00 65.74  ? 102  GLY A N   1 
ATOM   793  C CA  . GLY A 1 102 ? 30.626  -46.383 -41.744 1.00 64.85  ? 102  GLY A CA  1 
ATOM   794  C C   . GLY A 1 102 ? 29.948  -45.052 -41.482 1.00 65.75  ? 102  GLY A C   1 
ATOM   795  O O   . GLY A 1 102 ? 29.360  -44.466 -42.398 1.00 65.49  ? 102  GLY A O   1 
ATOM   796  N N   . ASN A 1 103 ? 30.020  -44.577 -40.217 1.00 59.27  ? 103  ASN A N   1 
ATOM   797  C CA  . ASN A 1 103 ? 29.471  -43.321 -39.749 1.00 57.41  ? 103  ASN A CA  1 
ATOM   798  C C   . ASN A 1 103 ? 30.330  -42.726 -38.623 1.00 62.66  ? 103  ASN A C   1 
ATOM   799  O O   . ASN A 1 103 ? 29.845  -41.947 -37.790 1.00 63.22  ? 103  ASN A O   1 
ATOM   800  C CB  . ASN A 1 103 ? 27.971  -43.414 -39.410 1.00 53.83  ? 103  ASN A CB  1 
ATOM   801  C CG  . ASN A 1 103 ? 27.617  -44.327 -38.279 1.00 76.62  ? 103  ASN A CG  1 
ATOM   802  O OD1 . ASN A 1 103 ? 27.777  -43.972 -37.117 1.00 66.98  ? 103  ASN A OD1 1 
ATOM   803  N ND2 . ASN A 1 103 ? 27.068  -45.502 -38.593 1.00 68.53  ? 103  ASN A ND2 1 
ATOM   804  N N   . GLY A 1 104 ? 31.615  -43.057 -38.655 1.00 61.25  ? 104  GLY A N   1 
ATOM   805  C CA  . GLY A 1 104 ? 32.643  -42.470 -37.797 1.00 63.12  ? 104  GLY A CA  1 
ATOM   806  C C   . GLY A 1 104 ? 33.039  -43.072 -36.462 1.00 71.87  ? 104  GLY A C   1 
ATOM   807  O O   . GLY A 1 104 ? 33.883  -42.478 -35.776 1.00 73.47  ? 104  GLY A O   1 
ATOM   808  N N   . CYS A 1 105 ? 32.467  -44.228 -36.066 1.00 69.69  ? 105  CYS A N   1 
ATOM   809  C CA  . CYS A 1 105 ? 32.794  -44.806 -34.749 1.00 70.89  ? 105  CYS A CA  1 
ATOM   810  C C   . CYS A 1 105 ? 33.661  -46.039 -34.826 1.00 78.07  ? 105  CYS A C   1 
ATOM   811  O O   . CYS A 1 105 ? 33.386  -46.925 -35.637 1.00 77.98  ? 105  CYS A O   1 
ATOM   812  C CB  . CYS A 1 105 ? 31.528  -45.082 -33.933 1.00 70.92  ? 105  CYS A CB  1 
ATOM   813  S SG  . CYS A 1 105 ? 30.457  -43.638 -33.678 1.00 74.01  ? 105  CYS A SG  1 
ATOM   814  N N   . GLY A 1 106 ? 34.640  -46.134 -33.924 1.00 75.97  ? 106  GLY A N   1 
ATOM   815  C CA  . GLY A 1 106 ? 35.504  -47.310 -33.834 1.00 76.58  ? 106  GLY A CA  1 
ATOM   816  C C   . GLY A 1 106 ? 34.758  -48.555 -33.366 1.00 81.84  ? 106  GLY A C   1 
ATOM   817  O O   . GLY A 1 106 ? 35.118  -49.684 -33.725 1.00 81.65  ? 106  GLY A O   1 
ATOM   818  N N   . LEU A 1 107 ? 33.690  -48.341 -32.559 1.00 78.00  ? 107  LEU A N   1 
ATOM   819  C CA  . LEU A 1 107 ? 32.813  -49.376 -32.003 1.00 76.70  ? 107  LEU A CA  1 
ATOM   820  C C   . LEU A 1 107 ? 31.445  -49.297 -32.671 1.00 77.49  ? 107  LEU A C   1 
ATOM   821  O O   . LEU A 1 107 ? 31.068  -48.233 -33.146 1.00 75.92  ? 107  LEU A O   1 
ATOM   822  C CB  . LEU A 1 107 ? 32.630  -49.175 -30.495 1.00 76.54  ? 107  LEU A CB  1 
ATOM   823  C CG  . LEU A 1 107 ? 33.869  -49.173 -29.606 1.00 80.33  ? 107  LEU A CG  1 
ATOM   824  C CD1 . LEU A 1 107 ? 34.346  -47.742 -29.335 1.00 80.64  ? 107  LEU A CD1 1 
ATOM   825  C CD2 . LEU A 1 107 ? 33.552  -49.810 -28.287 1.00 82.54  ? 107  LEU A CD2 1 
ATOM   826  N N   . PHE A 1 108 ? 30.709  -50.412 -32.690 1.00 73.73  ? 108  PHE A N   1 
ATOM   827  C CA  . PHE A 1 108 ? 29.373  -50.500 -33.258 1.00 74.55  ? 108  PHE A CA  1 
ATOM   828  C C   . PHE A 1 108 ? 28.322  -50.551 -32.143 1.00 80.02  ? 108  PHE A C   1 
ATOM   829  O O   . PHE A 1 108 ? 28.324  -51.476 -31.329 1.00 83.33  ? 108  PHE A O   1 
ATOM   830  C CB  . PHE A 1 108 ? 29.239  -51.770 -34.090 1.00 77.35  ? 108  PHE A CB  1 
ATOM   831  C CG  . PHE A 1 108 ? 30.059  -51.838 -35.347 1.00 80.99  ? 108  PHE A CG  1 
ATOM   832  C CD1 . PHE A 1 108 ? 29.551  -51.363 -36.554 1.00 85.69  ? 108  PHE A CD1 1 
ATOM   833  C CD2 . PHE A 1 108 ? 31.291  -52.480 -35.357 1.00 85.08  ? 108  PHE A CD2 1 
ATOM   834  C CE1 . PHE A 1 108 ? 30.284  -51.482 -37.739 1.00 87.32  ? 108  PHE A CE1 1 
ATOM   835  C CE2 . PHE A 1 108 ? 32.022  -52.609 -36.544 1.00 88.64  ? 108  PHE A CE2 1 
ATOM   836  C CZ  . PHE A 1 108 ? 31.511  -52.110 -37.727 1.00 87.04  ? 108  PHE A CZ  1 
ATOM   837  N N   . GLY A 1 109 ? 27.405  -49.601 -32.138 1.00 73.56  ? 109  GLY A N   1 
ATOM   838  C CA  . GLY A 1 109 ? 26.344  -49.574 -31.144 1.00 72.59  ? 109  GLY A CA  1 
ATOM   839  C C   . GLY A 1 109 ? 25.407  -48.391 -31.229 1.00 75.64  ? 109  GLY A C   1 
ATOM   840  O O   . GLY A 1 109 ? 25.341  -47.722 -32.255 1.00 76.76  ? 109  GLY A O   1 
ATOM   841  N N   . LYS A 1 110 ? 24.685  -48.119 -30.137 1.00 70.08  ? 110  LYS A N   1 
ATOM   842  C CA  . LYS A 1 110 ? 23.714  -47.030 -30.083 1.00 68.81  ? 110  LYS A CA  1 
ATOM   843  C C   . LYS A 1 110 ? 24.334  -45.760 -29.527 1.00 73.35  ? 110  LYS A C   1 
ATOM   844  O O   . LYS A 1 110 ? 24.523  -45.631 -28.316 1.00 74.59  ? 110  LYS A O   1 
ATOM   845  C CB  . LYS A 1 110 ? 22.428  -47.449 -29.334 1.00 69.30  ? 110  LYS A CB  1 
ATOM   846  C CG  . LYS A 1 110 ? 21.679  -48.646 -29.963 1.00 59.31  ? 110  LYS A CG  1 
ATOM   847  C CD  . LYS A 1 110 ? 20.826  -48.228 -31.139 1.00 59.06  ? 110  LYS A CD  1 
ATOM   848  C CE  . LYS A 1 110 ? 19.830  -49.307 -31.492 1.00 66.33  ? 110  LYS A CE  1 
ATOM   849  N NZ  . LYS A 1 110 ? 19.099  -49.016 -32.768 1.00 65.50  ? 110  LYS A NZ  1 
ATOM   850  N N   . GLY A 1 111 ? 24.694  -44.862 -30.431 1.00 68.71  ? 111  GLY A N   1 
ATOM   851  C CA  . GLY A 1 111 ? 25.286  -43.580 -30.086 1.00 68.33  ? 111  GLY A CA  1 
ATOM   852  C C   . GLY A 1 111 ? 24.219  -42.565 -29.746 1.00 72.37  ? 111  GLY A C   1 
ATOM   853  O O   . GLY A 1 111 ? 23.257  -42.388 -30.494 1.00 72.57  ? 111  GLY A O   1 
ATOM   854  N N   . GLY A 1 112 ? 24.381  -41.923 -28.598 1.00 68.65  ? 112  GLY A N   1 
ATOM   855  C CA  . GLY A 1 112 ? 23.460  -40.910 -28.099 1.00 67.67  ? 112  GLY A CA  1 
ATOM   856  C C   . GLY A 1 112 ? 23.444  -39.655 -28.938 1.00 69.92  ? 112  GLY A C   1 
ATOM   857  O O   . GLY A 1 112 ? 24.498  -39.157 -29.339 1.00 69.10  ? 112  GLY A O   1 
ATOM   858  N N   . ILE A 1 113 ? 22.236  -39.159 -29.221 1.00 66.47  ? 113  ILE A N   1 
ATOM   859  C CA  . ILE A 1 113 ? 21.998  -37.959 -30.017 1.00 66.12  ? 113  ILE A CA  1 
ATOM   860  C C   . ILE A 1 113 ? 21.172  -36.969 -29.200 1.00 68.68  ? 113  ILE A C   1 
ATOM   861  O O   . ILE A 1 113 ? 20.492  -37.371 -28.253 1.00 69.14  ? 113  ILE A O   1 
ATOM   862  C CB  . ILE A 1 113 ? 21.312  -38.349 -31.358 1.00 69.54  ? 113  ILE A CB  1 
ATOM   863  C CG1 . ILE A 1 113 ? 21.661  -37.374 -32.469 1.00 71.18  ? 113  ILE A CG1 1 
ATOM   864  C CG2 . ILE A 1 113 ? 19.802  -38.541 -31.221 1.00 69.68  ? 113  ILE A CG2 1 
ATOM   865  C CD1 . ILE A 1 113 ? 20.844  -37.539 -33.845 1.00 87.92  ? 113  ILE A CD1 1 
ATOM   866  N N   . VAL A 1 114 ? 21.245  -35.689 -29.557 1.00 63.62  ? 114  VAL A N   1 
ATOM   867  C CA  . VAL A 1 114 ? 20.466  -34.610 -28.957 1.00 62.99  ? 114  VAL A CA  1 
ATOM   868  C C   . VAL A 1 114 ? 20.162  -33.547 -30.033 1.00 67.99  ? 114  VAL A C   1 
ATOM   869  O O   . VAL A 1 114 ? 21.060  -33.119 -30.756 1.00 69.14  ? 114  VAL A O   1 
ATOM   870  C CB  . VAL A 1 114 ? 21.048  -34.037 -27.628 1.00 66.08  ? 114  VAL A CB  1 
ATOM   871  C CG1 . VAL A 1 114 ? 22.420  -33.396 -27.809 1.00 65.56  ? 114  VAL A CG1 1 
ATOM   872  C CG2 . VAL A 1 114 ? 20.081  -33.063 -26.970 1.00 65.82  ? 114  VAL A CG2 1 
ATOM   873  N N   . THR A 1 115 ? 18.883  -33.183 -30.175 1.00 63.19  ? 115  THR A N   1 
ATOM   874  C CA  . THR A 1 115 ? 18.434  -32.189 -31.142 1.00 61.92  ? 115  THR A CA  1 
ATOM   875  C C   . THR A 1 115 ? 17.695  -31.051 -30.417 1.00 65.79  ? 115  THR A C   1 
ATOM   876  O O   . THR A 1 115 ? 16.808  -31.324 -29.596 1.00 64.20  ? 115  THR A O   1 
ATOM   877  C CB  . THR A 1 115 ? 17.559  -32.859 -32.225 1.00 65.07  ? 115  THR A CB  1 
ATOM   878  O OG1 . THR A 1 115 ? 18.128  -34.099 -32.645 1.00 55.46  ? 115  THR A OG1 1 
ATOM   879  C CG2 . THR A 1 115 ? 17.311  -31.963 -33.420 1.00 66.46  ? 115  THR A CG2 1 
ATOM   880  N N   . CYS A 1 116 ? 18.067  -29.779 -30.734 1.00 64.24  ? 116  CYS A N   1 
ATOM   881  C CA  . CYS A 1 116 ? 17.451  -28.543 -30.215 1.00 65.47  ? 116  CYS A CA  1 
ATOM   882  C C   . CYS A 1 116 ? 17.070  -27.642 -31.349 1.00 68.09  ? 116  CYS A C   1 
ATOM   883  O O   . CYS A 1 116 ? 17.807  -27.553 -32.329 1.00 66.90  ? 116  CYS A O   1 
ATOM   884  C CB  . CYS A 1 116 ? 18.360  -27.815 -29.236 1.00 67.24  ? 116  CYS A CB  1 
ATOM   885  S SG  . CYS A 1 116 ? 18.792  -28.777 -27.763 1.00 72.20  ? 116  CYS A SG  1 
ATOM   886  N N   . ALA A 1 117 ? 15.930  -26.950 -31.210 1.00 65.42  ? 117  ALA A N   1 
ATOM   887  C CA  . ALA A 1 117 ? 15.428  -26.012 -32.223 1.00 65.52  ? 117  ALA A CA  1 
ATOM   888  C C   . ALA A 1 117 ? 14.758  -24.842 -31.537 1.00 68.94  ? 117  ALA A C   1 
ATOM   889  O O   . ALA A 1 117 ? 14.255  -25.004 -30.411 1.00 67.57  ? 117  ALA A O   1 
ATOM   890  C CB  . ALA A 1 117 ? 14.455  -26.705 -33.163 1.00 66.28  ? 117  ALA A CB  1 
ATOM   891  N N   . LYS A 1 118 ? 14.797  -23.649 -32.197 1.00 65.08  ? 118  LYS A N   1 
ATOM   892  C CA  . LYS A 1 118 ? 14.245  -22.413 -31.641 1.00 63.78  ? 118  LYS A CA  1 
ATOM   893  C C   . LYS A 1 118 ? 12.786  -22.239 -31.964 1.00 64.75  ? 118  LYS A C   1 
ATOM   894  O O   . LYS A 1 118 ? 12.427  -22.070 -33.142 1.00 63.12  ? 118  LYS A O   1 
ATOM   895  C CB  . LYS A 1 118 ? 15.066  -21.180 -32.042 1.00 65.21  ? 118  LYS A CB  1 
ATOM   896  C CG  . LYS A 1 118 ? 15.073  -20.114 -30.954 1.00 74.32  ? 118  LYS A CG  1 
ATOM   897  C CD  . LYS A 1 118 ? 15.535  -18.771 -31.481 1.00 83.82  ? 118  LYS A CD  1 
ATOM   898  C CE  . LYS A 1 118 ? 15.270  -17.678 -30.478 1.00 99.25  ? 118  LYS A CE  1 
ATOM   899  N NZ  . LYS A 1 118 ? 15.744  -16.358 -30.974 1.00 117.99 ? 118  LYS A NZ  1 
ATOM   900  N N   . PHE A 1 119 ? 11.945  -22.267 -30.893 1.00 60.04  ? 119  PHE A N   1 
ATOM   901  C CA  . PHE A 1 119 ? 10.486  -22.100 -30.959 1.00 59.40  ? 119  PHE A CA  1 
ATOM   902  C C   . PHE A 1 119 ? 10.132  -20.630 -31.003 1.00 63.58  ? 119  PHE A C   1 
ATOM   903  O O   . PHE A 1 119 ? 10.305  -19.910 -30.010 1.00 62.19  ? 119  PHE A O   1 
ATOM   904  C CB  . PHE A 1 119 ? 9.778   -22.791 -29.792 1.00 60.73  ? 119  PHE A CB  1 
ATOM   905  C CG  . PHE A 1 119 ? 8.267   -22.778 -29.863 1.00 61.81  ? 119  PHE A CG  1 
ATOM   906  C CD1 . PHE A 1 119 ? 7.541   -21.700 -29.378 1.00 63.91  ? 119  PHE A CD1 1 
ATOM   907  C CD2 . PHE A 1 119 ? 7.566   -23.878 -30.346 1.00 64.69  ? 119  PHE A CD2 1 
ATOM   908  C CE1 . PHE A 1 119 ? 6.145   -21.704 -29.411 1.00 64.87  ? 119  PHE A CE1 1 
ATOM   909  C CE2 . PHE A 1 119 ? 6.167   -23.888 -30.364 1.00 67.20  ? 119  PHE A CE2 1 
ATOM   910  C CZ  . PHE A 1 119 ? 5.469   -22.799 -29.897 1.00 64.71  ? 119  PHE A CZ  1 
ATOM   911  N N   . THR A 1 120 ? 9.621   -20.198 -32.168 1.00 62.16  ? 120  THR A N   1 
ATOM   912  C CA  . THR A 1 120 ? 9.240   -18.821 -32.475 1.00 62.33  ? 120  THR A CA  1 
ATOM   913  C C   . THR A 1 120 ? 7.749   -18.782 -32.744 1.00 67.32  ? 120  THR A C   1 
ATOM   914  O O   . THR A 1 120 ? 7.287   -19.453 -33.676 1.00 67.25  ? 120  THR A O   1 
ATOM   915  C CB  . THR A 1 120 ? 10.028  -18.302 -33.707 1.00 67.90  ? 120  THR A CB  1 
ATOM   916  O OG1 . THR A 1 120 ? 11.310  -18.932 -33.822 1.00 63.99  ? 120  THR A OG1 1 
ATOM   917  C CG2 . THR A 1 120 ? 10.177  -16.804 -33.702 1.00 66.66  ? 120  THR A CG2 1 
ATOM   918  N N   . CYS A 1 121 ? 6.988   -18.019 -31.931 1.00 64.15  ? 121  CYS A N   1 
ATOM   919  C CA  . CYS A 1 121 ? 5.554   -17.918 -32.172 1.00 64.07  ? 121  CYS A CA  1 
ATOM   920  C C   . CYS A 1 121 ? 5.229   -16.877 -33.220 1.00 66.39  ? 121  CYS A C   1 
ATOM   921  O O   . CYS A 1 121 ? 5.738   -15.754 -33.167 1.00 66.55  ? 121  CYS A O   1 
ATOM   922  C CB  . CYS A 1 121 ? 4.781   -17.669 -30.899 1.00 65.19  ? 121  CYS A CB  1 
ATOM   923  S SG  . CYS A 1 121 ? 3.006   -17.943 -31.089 1.00 69.78  ? 121  CYS A SG  1 
ATOM   924  N N   . LYS A 1 122 ? 4.387   -17.258 -34.175 1.00 61.12  ? 122  LYS A N   1 
ATOM   925  C CA  . LYS A 1 122 ? 3.970   -16.436 -35.305 1.00 60.29  ? 122  LYS A CA  1 
ATOM   926  C C   . LYS A 1 122 ? 2.565   -15.787 -35.158 1.00 61.30  ? 122  LYS A C   1 
ATOM   927  O O   . LYS A 1 122 ? 2.335   -14.707 -35.683 1.00 60.33  ? 122  LYS A O   1 
ATOM   928  C CB  . LYS A 1 122 ? 4.042   -17.273 -36.575 1.00 63.58  ? 122  LYS A CB  1 
ATOM   929  C CG  . LYS A 1 122 ? 5.460   -17.488 -37.110 1.00 79.22  ? 122  LYS A CG  1 
ATOM   930  C CD  . LYS A 1 122 ? 5.490   -18.584 -38.187 1.00 94.23  ? 122  LYS A CD  1 
ATOM   931  C CE  . LYS A 1 122 ? 5.037   -18.173 -39.581 1.00 104.70 ? 122  LYS A CE  1 
ATOM   932  N NZ  . LYS A 1 122 ? 5.061   -19.329 -40.531 1.00 116.31 ? 122  LYS A NZ  1 
ATOM   933  N N   . LYS A 1 123 ? 1.639   -16.445 -34.487 1.00 56.71  ? 123  LYS A N   1 
ATOM   934  C CA  . LYS A 1 123 ? 0.276   -15.962 -34.245 1.00 56.22  ? 123  LYS A CA  1 
ATOM   935  C C   . LYS A 1 123 ? -0.122  -16.536 -32.888 1.00 59.16  ? 123  LYS A C   1 
ATOM   936  O O   . LYS A 1 123 ? 0.153   -17.702 -32.573 1.00 56.60  ? 123  LYS A O   1 
ATOM   937  C CB  . LYS A 1 123 ? -0.727  -16.424 -35.341 1.00 58.60  ? 123  LYS A CB  1 
ATOM   938  C CG  . LYS A 1 123 ? -0.910  -15.479 -36.508 1.00 67.55  ? 123  LYS A CG  1 
ATOM   939  C CD  . LYS A 1 123 ? -1.602  -16.165 -37.697 1.00 78.72  ? 123  LYS A CD  1 
ATOM   940  C CE  . LYS A 1 123 ? -1.317  -15.428 -39.003 1.00 91.09  ? 123  LYS A CE  1 
ATOM   941  N NZ  . LYS A 1 123 ? -2.058  -15.972 -40.179 1.00 93.31  ? 123  LYS A NZ  1 
ATOM   942  N N   . ASN A 1 124 ? -0.759  -15.704 -32.089 1.00 57.02  ? 124  ASN A N   1 
ATOM   943  C CA  . ASN A 1 124 ? -1.107  -16.038 -30.724 1.00 57.19  ? 124  ASN A CA  1 
ATOM   944  C C   . ASN A 1 124 ? -2.453  -15.424 -30.382 1.00 58.71  ? 124  ASN A C   1 
ATOM   945  O O   . ASN A 1 124 ? -2.969  -14.621 -31.166 1.00 56.66  ? 124  ASN A O   1 
ATOM   946  C CB  . ASN A 1 124 ? 0.024   -15.559 -29.760 1.00 61.26  ? 124  ASN A CB  1 
ATOM   947  C CG  . ASN A 1 124 ? 0.227   -14.053 -29.746 1.00 90.62  ? 124  ASN A CG  1 
ATOM   948  O OD1 . ASN A 1 124 ? -0.556  -13.309 -29.132 1.00 86.86  ? 124  ASN A OD1 1 
ATOM   949  N ND2 . ASN A 1 124 ? 1.258   -13.570 -30.459 1.00 78.60  ? 124  ASN A ND2 1 
ATOM   950  N N   . MET A 1 125 ? -3.024  -15.800 -29.228 1.00 54.61  ? 125  MET A N   1 
ATOM   951  C CA  . MET A 1 125 ? -4.338  -15.306 -28.864 1.00 54.31  ? 125  MET A CA  1 
ATOM   952  C C   . MET A 1 125 ? -4.504  -15.135 -27.358 1.00 62.20  ? 125  MET A C   1 
ATOM   953  O O   . MET A 1 125 ? -4.376  -16.088 -26.597 1.00 61.73  ? 125  MET A O   1 
ATOM   954  C CB  . MET A 1 125 ? -5.462  -16.158 -29.485 1.00 55.38  ? 125  MET A CB  1 
ATOM   955  C CG  . MET A 1 125 ? -5.158  -17.610 -29.531 1.00 58.73  ? 125  MET A CG  1 
ATOM   956  S SD  . MET A 1 125 ? -6.678  -18.577 -29.531 1.00 64.03  ? 125  MET A SD  1 
ATOM   957  C CE  . MET A 1 125 ? -6.201  -19.940 -28.596 1.00 60.85  ? 125  MET A CE  1 
ATOM   958  N N   . GLU A 1 126 ? -4.791  -13.895 -26.944 1.00 61.48  ? 126  GLU A N   1 
ATOM   959  C CA  . GLU A 1 126 ? -4.994  -13.489 -25.562 1.00 62.53  ? 126  GLU A CA  1 
ATOM   960  C C   . GLU A 1 126 ? -6.427  -13.750 -25.191 1.00 67.85  ? 126  GLU A C   1 
ATOM   961  O O   . GLU A 1 126 ? -7.312  -13.594 -26.021 1.00 67.24  ? 126  GLU A O   1 
ATOM   962  C CB  . GLU A 1 126 ? -4.720  -11.978 -25.391 1.00 64.61  ? 126  GLU A CB  1 
ATOM   963  C CG  . GLU A 1 126 ? -3.327  -11.491 -25.779 1.00 84.72  ? 126  GLU A CG  1 
ATOM   964  C CD  . GLU A 1 126 ? -3.092  -11.098 -27.233 1.00 132.11 ? 126  GLU A CD  1 
ATOM   965  O OE1 . GLU A 1 126 ? -4.064  -10.739 -27.942 1.00 145.19 ? 126  GLU A OE1 1 
ATOM   966  O OE2 . GLU A 1 126 ? -1.912  -11.115 -27.652 1.00 133.06 ? 126  GLU A OE2 1 
ATOM   967  N N   . GLY A 1 127 ? -6.644  -14.087 -23.937 1.00 67.07  ? 127  GLY A N   1 
ATOM   968  C CA  . GLY A 1 127 ? -7.966  -14.300 -23.372 1.00 68.81  ? 127  GLY A CA  1 
ATOM   969  C C   . GLY A 1 127 ? -8.057  -13.454 -22.120 1.00 78.09  ? 127  GLY A C   1 
ATOM   970  O O   . GLY A 1 127 ? -7.444  -13.798 -21.102 1.00 78.07  ? 127  GLY A O   1 
ATOM   971  N N   . LYS A 1 128 ? -8.764  -12.308 -22.197 1.00 77.51  ? 128  LYS A N   1 
ATOM   972  C CA  . LYS A 1 128 ? -8.855  -11.373 -21.075 1.00 78.13  ? 128  LYS A CA  1 
ATOM   973  C C   . LYS A 1 128 ? -9.974  -11.711 -20.079 1.00 87.67  ? 128  LYS A C   1 
ATOM   974  O O   . LYS A 1 128 ? -11.081 -12.038 -20.498 1.00 86.57  ? 128  LYS A O   1 
ATOM   975  C CB  . LYS A 1 128 ? -8.957  -9.938  -21.594 1.00 78.57  ? 128  LYS A CB  1 
ATOM   976  C CG  . LYS A 1 128 ? -7.604  -9.340  -21.975 1.00 80.79  ? 128  LYS A CG  1 
ATOM   977  C CD  . LYS A 1 128 ? -7.212  -9.613  -23.425 1.00 87.83  ? 128  LYS A CD  1 
ATOM   978  C CE  . LYS A 1 128 ? -5.956  -8.881  -23.838 1.00 96.04  ? 128  LYS A CE  1 
ATOM   979  N NZ  . LYS A 1 128 ? -6.249  -7.612  -24.559 1.00 103.35 ? 128  LYS A NZ  1 
ATOM   980  N N   . ILE A 1 129 ? -9.657  -11.674 -18.758 1.00 90.17  ? 129  ILE A N   1 
ATOM   981  C CA  . ILE A 1 129 ? -10.566 -11.947 -17.631 1.00 93.19  ? 129  ILE A CA  1 
ATOM   982  C C   . ILE A 1 129 ? -11.629 -10.861 -17.539 1.00 104.65 ? 129  ILE A C   1 
ATOM   983  O O   . ILE A 1 129 ? -11.315 -9.669  -17.375 1.00 104.44 ? 129  ILE A O   1 
ATOM   984  C CB  . ILE A 1 129 ? -9.850  -12.124 -16.240 1.00 96.33  ? 129  ILE A CB  1 
ATOM   985  C CG1 . ILE A 1 129 ? -8.991  -13.401 -16.169 1.00 97.25  ? 129  ILE A CG1 1 
ATOM   986  C CG2 . ILE A 1 129 ? -10.853 -12.097 -15.065 1.00 96.37  ? 129  ILE A CG2 1 
ATOM   987  C CD1 . ILE A 1 129 ? -8.000  -13.508 -14.857 1.00 105.85 ? 129  ILE A CD1 1 
ATOM   988  N N   . VAL A 1 130 ? -12.892 -11.292 -17.585 1.00 106.21 ? 130  VAL A N   1 
ATOM   989  C CA  . VAL A 1 130 ? -13.994 -10.375 -17.422 1.00 108.19 ? 130  VAL A CA  1 
ATOM   990  C C   . VAL A 1 130 ? -14.714 -10.673 -16.106 1.00 116.05 ? 130  VAL A C   1 
ATOM   991  O O   . VAL A 1 130 ? -14.865 -11.837 -15.701 1.00 114.99 ? 130  VAL A O   1 
ATOM   992  C CB  . VAL A 1 130 ? -14.923 -10.282 -18.671 1.00 112.58 ? 130  VAL A CB  1 
ATOM   993  C CG1 . VAL A 1 130 ? -16.163 -11.177 -18.566 1.00 112.33 ? 130  VAL A CG1 1 
ATOM   994  C CG2 . VAL A 1 130 ? -15.313 -8.832  -18.953 1.00 112.50 ? 130  VAL A CG2 1 
ATOM   995  N N   . GLN A 1 131 ? -15.055 -9.588  -15.406 1.00 116.48 ? 131  GLN A N   1 
ATOM   996  C CA  . GLN A 1 131 ? -15.836 -9.567  -14.169 1.00 117.73 ? 131  GLN A CA  1 
ATOM   997  C C   . GLN A 1 131 ? -17.078 -8.721  -14.509 1.00 123.64 ? 131  GLN A C   1 
ATOM   998  O O   . GLN A 1 131 ? -16.922 -7.675  -15.155 1.00 122.82 ? 131  GLN A O   1 
ATOM   999  C CB  . GLN A 1 131 ? -15.058 -8.921  -12.993 1.00 119.11 ? 131  GLN A CB  1 
ATOM   1000 C CG  . GLN A 1 131 ? -13.772 -9.644  -12.571 1.00 132.05 ? 131  GLN A CG  1 
ATOM   1001 C CD  . GLN A 1 131 ? -12.500 -8.841  -12.800 1.00 149.35 ? 131  GLN A CD  1 
ATOM   1002 O OE1 . GLN A 1 131 ? -12.508 -7.694  -13.278 1.00 146.61 ? 131  GLN A OE1 1 
ATOM   1003 N NE2 . GLN A 1 131 ? -11.366 -9.439  -12.455 1.00 135.59 ? 131  GLN A NE2 1 
ATOM   1004 N N   . PRO A 1 132 ? -18.315 -9.133  -14.131 1.00 121.82 ? 132  PRO A N   1 
ATOM   1005 C CA  . PRO A 1 132 ? -19.489 -8.291  -14.457 1.00 122.15 ? 132  PRO A CA  1 
ATOM   1006 C C   . PRO A 1 132 ? -19.382 -6.867  -13.896 1.00 127.27 ? 132  PRO A C   1 
ATOM   1007 O O   . PRO A 1 132 ? -19.911 -5.944  -14.510 1.00 128.09 ? 132  PRO A O   1 
ATOM   1008 C CB  . PRO A 1 132 ? -20.670 -9.053  -13.843 1.00 123.61 ? 132  PRO A CB  1 
ATOM   1009 C CG  . PRO A 1 132 ? -20.179 -10.441 -13.634 1.00 127.91 ? 132  PRO A CG  1 
ATOM   1010 C CD  . PRO A 1 132 ? -18.707 -10.344 -13.379 1.00 123.35 ? 132  PRO A CD  1 
ATOM   1011 N N   . GLU A 1 133 ? -18.631 -6.690  -12.789 1.00 122.74 ? 133  GLU A N   1 
ATOM   1012 C CA  . GLU A 1 133 ? -18.389 -5.427  -12.094 1.00 122.02 ? 133  GLU A CA  1 
ATOM   1013 C C   . GLU A 1 133 ? -17.785 -4.344  -12.983 1.00 124.14 ? 133  GLU A C   1 
ATOM   1014 O O   . GLU A 1 133 ? -18.332 -3.246  -13.036 1.00 123.93 ? 133  GLU A O   1 
ATOM   1015 C CB  . GLU A 1 133 ? -17.511 -5.650  -10.845 1.00 123.59 ? 133  GLU A CB  1 
ATOM   1016 C CG  . GLU A 1 133 ? -18.191 -6.421  -9.718  1.00 136.03 ? 133  GLU A CG  1 
ATOM   1017 C CD  . GLU A 1 133 ? -18.301 -7.934  -9.850  1.00 156.78 ? 133  GLU A CD  1 
ATOM   1018 O OE1 . GLU A 1 133 ? -17.632 -8.519  -10.734 1.00 149.66 ? 133  GLU A OE1 1 
ATOM   1019 O OE2 . GLU A 1 133 ? -19.053 -8.537  -9.049  1.00 148.25 ? 133  GLU A OE2 1 
ATOM   1020 N N   . ASN A 1 134 ? -16.684 -4.644  -13.691 1.00 119.59 ? 134  ASN A N   1 
ATOM   1021 C CA  . ASN A 1 134 ? -16.011 -3.657  -14.537 1.00 119.36 ? 134  ASN A CA  1 
ATOM   1022 C C   . ASN A 1 134 ? -16.577 -3.560  -15.988 1.00 122.84 ? 134  ASN A C   1 
ATOM   1023 O O   . ASN A 1 134 ? -15.899 -3.002  -16.860 1.00 122.31 ? 134  ASN A O   1 
ATOM   1024 C CB  . ASN A 1 134 ? -14.480 -3.883  -14.530 1.00 121.42 ? 134  ASN A CB  1 
ATOM   1025 C CG  . ASN A 1 134 ? -13.982 -5.278  -14.890 1.00 141.31 ? 134  ASN A CG  1 
ATOM   1026 O OD1 . ASN A 1 134 ? -14.693 -6.274  -14.788 1.00 132.35 ? 134  ASN A OD1 1 
ATOM   1027 N ND2 . ASN A 1 134 ? -12.712 -5.390  -15.262 1.00 131.37 ? 134  ASN A ND2 1 
ATOM   1028 N N   . LEU A 1 135 ? -17.844 -4.032  -16.221 1.00 118.65 ? 135  LEU A N   1 
ATOM   1029 C CA  . LEU A 1 135 ? -18.543 -4.017  -17.525 1.00 117.67 ? 135  LEU A CA  1 
ATOM   1030 C C   . LEU A 1 135 ? -19.440 -2.756  -17.661 1.00 121.36 ? 135  LEU A C   1 
ATOM   1031 O O   . LEU A 1 135 ? -20.457 -2.651  -16.963 1.00 122.30 ? 135  LEU A O   1 
ATOM   1032 C CB  . LEU A 1 135 ? -19.430 -5.279  -17.645 1.00 117.13 ? 135  LEU A CB  1 
ATOM   1033 C CG  . LEU A 1 135 ? -19.507 -5.963  -18.996 1.00 121.23 ? 135  LEU A CG  1 
ATOM   1034 C CD1 . LEU A 1 135 ? -20.139 -7.328  -18.847 1.00 121.09 ? 135  LEU A CD1 1 
ATOM   1035 C CD2 . LEU A 1 135 ? -20.287 -5.137  -20.014 1.00 123.39 ? 135  LEU A CD2 1 
ATOM   1036 N N   . GLU A 1 136 ? -19.087 -1.828  -18.574 1.00 114.95 ? 136  GLU A N   1 
ATOM   1037 C CA  . GLU A 1 136 ? -19.831 -0.578  -18.778 1.00 113.31 ? 136  GLU A CA  1 
ATOM   1038 C C   . GLU A 1 136 ? -20.669 -0.550  -20.070 1.00 113.51 ? 136  GLU A C   1 
ATOM   1039 O O   . GLU A 1 136 ? -20.213 -1.002  -21.124 1.00 113.44 ? 136  GLU A O   1 
ATOM   1040 C CB  . GLU A 1 136 ? -18.860 0.619   -18.732 1.00 114.76 ? 136  GLU A CB  1 
ATOM   1041 C CG  . GLU A 1 136 ? -19.506 1.996   -18.746 1.00 126.70 ? 136  GLU A CG  1 
ATOM   1042 C CD  . GLU A 1 136 ? -18.532 3.133   -18.980 1.00 154.80 ? 136  GLU A CD  1 
ATOM   1043 O OE1 . GLU A 1 136 ? -18.250 3.445   -20.161 1.00 155.08 ? 136  GLU A OE1 1 
ATOM   1044 O OE2 . GLU A 1 136 ? -18.053 3.713   -17.981 1.00 149.37 ? 136  GLU A OE2 1 
ATOM   1045 N N   . TYR A 1 137 ? -21.883 0.030   -19.985 1.00 106.68 ? 137  TYR A N   1 
ATOM   1046 C CA  . TYR A 1 137 ? -22.787 0.191   -21.130 1.00 104.66 ? 137  TYR A CA  1 
ATOM   1047 C C   . TYR A 1 137 ? -22.970 1.674   -21.485 1.00 104.88 ? 137  TYR A C   1 
ATOM   1048 O O   . TYR A 1 137 ? -22.959 2.528   -20.593 1.00 104.85 ? 137  TYR A O   1 
ATOM   1049 C CB  . TYR A 1 137 ? -24.139 -0.486  -20.869 1.00 105.28 ? 137  TYR A CB  1 
ATOM   1050 C CG  . TYR A 1 137 ? -24.027 -1.928  -20.428 1.00 106.97 ? 137  TYR A CG  1 
ATOM   1051 C CD1 . TYR A 1 137 ? -23.871 -2.952  -21.356 1.00 107.38 ? 137  TYR A CD1 1 
ATOM   1052 C CD2 . TYR A 1 137 ? -24.075 -2.270  -19.080 1.00 109.17 ? 137  TYR A CD2 1 
ATOM   1053 C CE1 . TYR A 1 137 ? -23.769 -4.283  -20.952 1.00 108.06 ? 137  TYR A CE1 1 
ATOM   1054 C CE2 . TYR A 1 137 ? -23.982 -3.596  -18.665 1.00 109.37 ? 137  TYR A CE2 1 
ATOM   1055 C CZ  . TYR A 1 137 ? -23.829 -4.599  -19.606 1.00 115.17 ? 137  TYR A CZ  1 
ATOM   1056 O OH  . TYR A 1 137 ? -23.722 -5.907  -19.212 1.00 117.00 ? 137  TYR A OH  1 
ATOM   1057 N N   . THR A 1 138 ? -23.118 1.977   -22.783 1.00 97.58  ? 138  THR A N   1 
ATOM   1058 C CA  . THR A 1 138 ? -23.313 3.344   -23.274 1.00 95.62  ? 138  THR A CA  1 
ATOM   1059 C C   . THR A 1 138 ? -24.621 3.435   -24.058 1.00 95.02  ? 138  THR A C   1 
ATOM   1060 O O   . THR A 1 138 ? -24.710 2.927   -25.173 1.00 94.73  ? 138  THR A O   1 
ATOM   1061 C CB  . THR A 1 138 ? -22.079 3.813   -24.057 1.00 104.95 ? 138  THR A CB  1 
ATOM   1062 O OG1 . THR A 1 138 ? -20.934 3.748   -23.204 1.00 105.42 ? 138  THR A OG1 1 
ATOM   1063 C CG2 . THR A 1 138 ? -22.234 5.223   -24.643 1.00 103.20 ? 138  THR A CG2 1 
ATOM   1064 N N   . ILE A 1 139 ? -25.632 4.086   -23.451 1.00 88.34  ? 139  ILE A N   1 
ATOM   1065 C CA  . ILE A 1 139 ? -26.984 4.303   -23.988 1.00 85.63  ? 139  ILE A CA  1 
ATOM   1066 C C   . ILE A 1 139 ? -27.137 5.747   -24.432 1.00 86.64  ? 139  ILE A C   1 
ATOM   1067 O O   . ILE A 1 139 ? -26.666 6.647   -23.742 1.00 86.72  ? 139  ILE A O   1 
ATOM   1068 C CB  . ILE A 1 139 ? -28.051 3.901   -22.928 1.00 87.54  ? 139  ILE A CB  1 
ATOM   1069 C CG1 . ILE A 1 139 ? -28.011 2.375   -22.661 1.00 87.08  ? 139  ILE A CG1 1 
ATOM   1070 C CG2 . ILE A 1 139 ? -29.469 4.370   -23.328 1.00 87.40  ? 139  ILE A CG2 1 
ATOM   1071 C CD1 . ILE A 1 139 ? -28.654 1.899   -21.417 1.00 90.31  ? 139  ILE A CD1 1 
ATOM   1072 N N   . VAL A 1 140 ? -27.776 5.962   -25.589 1.00 81.94  ? 140  VAL A N   1 
ATOM   1073 C CA  . VAL A 1 140 ? -28.071 7.297   -26.122 1.00 81.21  ? 140  VAL A CA  1 
ATOM   1074 C C   . VAL A 1 140 ? -29.607 7.534   -26.168 1.00 84.25  ? 140  VAL A C   1 
ATOM   1075 O O   . VAL A 1 140 ? -30.330 6.804   -26.856 1.00 84.42  ? 140  VAL A O   1 
ATOM   1076 C CB  . VAL A 1 140 ? -27.377 7.572   -27.464 1.00 84.01  ? 140  VAL A CB  1 
ATOM   1077 C CG1 . VAL A 1 140 ? -27.878 8.875   -28.083 1.00 83.82  ? 140  VAL A CG1 1 
ATOM   1078 C CG2 . VAL A 1 140 ? -25.872 7.622   -27.278 1.00 83.60  ? 140  VAL A CG2 1 
ATOM   1079 N N   . ILE A 1 141 ? -30.094 8.533   -25.411 1.00 78.03  ? 141  ILE A N   1 
ATOM   1080 C CA  . ILE A 1 141 ? -31.521 8.831   -25.396 1.00 76.85  ? 141  ILE A CA  1 
ATOM   1081 C C   . ILE A 1 141 ? -31.788 10.063  -26.220 1.00 79.07  ? 141  ILE A C   1 
ATOM   1082 O O   . ILE A 1 141 ? -31.305 11.134  -25.885 1.00 79.81  ? 141  ILE A O   1 
ATOM   1083 C CB  . ILE A 1 141 ? -32.112 8.960   -23.979 1.00 79.94  ? 141  ILE A CB  1 
ATOM   1084 C CG1 . ILE A 1 141 ? -31.568 7.879   -23.035 1.00 80.64  ? 141  ILE A CG1 1 
ATOM   1085 C CG2 . ILE A 1 141 ? -33.645 8.973   -24.026 1.00 79.40  ? 141  ILE A CG2 1 
ATOM   1086 C CD1 . ILE A 1 141 ? -30.730 8.399   -21.997 1.00 91.04  ? 141  ILE A CD1 1 
ATOM   1087 N N   . THR A 1 142 ? -32.555 9.919   -27.291 1.00 73.74  ? 142  THR A N   1 
ATOM   1088 C CA  . THR A 1 142 ? -32.861 11.031  -28.174 1.00 72.41  ? 142  THR A CA  1 
ATOM   1089 C C   . THR A 1 142 ? -34.354 11.335  -28.181 1.00 76.56  ? 142  THR A C   1 
ATOM   1090 O O   . THR A 1 142 ? -35.128 10.550  -28.733 1.00 78.06  ? 142  THR A O   1 
ATOM   1091 C CB  . THR A 1 142 ? -32.313 10.773  -29.579 1.00 67.34  ? 142  THR A CB  1 
ATOM   1092 O OG1 . THR A 1 142 ? -30.946 10.398  -29.477 1.00 66.82  ? 142  THR A OG1 1 
ATOM   1093 C CG2 . THR A 1 142 ? -32.471 11.969  -30.493 1.00 59.62  ? 142  THR A CG2 1 
ATOM   1094 N N   . PRO A 1 143 ? -34.788 12.481  -27.626 1.00 70.69  ? 143  PRO A N   1 
ATOM   1095 C CA  . PRO A 1 143 ? -36.207 12.826  -27.707 1.00 69.22  ? 143  PRO A CA  1 
ATOM   1096 C C   . PRO A 1 143 ? -36.646 13.199  -29.124 1.00 69.87  ? 143  PRO A C   1 
ATOM   1097 O O   . PRO A 1 143 ? -35.822 13.605  -29.955 1.00 68.80  ? 143  PRO A O   1 
ATOM   1098 C CB  . PRO A 1 143 ? -36.342 14.001  -26.743 1.00 71.17  ? 143  PRO A CB  1 
ATOM   1099 C CG  . PRO A 1 143 ? -35.035 14.622  -26.728 1.00 76.81  ? 143  PRO A CG  1 
ATOM   1100 C CD  . PRO A 1 143 ? -34.024 13.531  -26.932 1.00 72.91  ? 143  PRO A CD  1 
ATOM   1101 N N   . HIS A 1 144 ? -37.951 12.989  -29.399 1.00 65.02  ? 144  HIS A N   1 
ATOM   1102 C CA  . HIS A 1 144 ? -38.619 13.304  -30.646 1.00 64.42  ? 144  HIS A CA  1 
ATOM   1103 C C   . HIS A 1 144 ? -39.050 14.775  -30.550 1.00 69.99  ? 144  HIS A C   1 
ATOM   1104 O O   . HIS A 1 144 ? -40.210 15.081  -30.241 1.00 67.93  ? 144  HIS A O   1 
ATOM   1105 C CB  . HIS A 1 144 ? -39.824 12.375  -30.846 1.00 64.88  ? 144  HIS A CB  1 
ATOM   1106 C CG  . HIS A 1 144 ? -39.540 11.160  -31.677 1.00 68.39  ? 144  HIS A CG  1 
ATOM   1107 N ND1 . HIS A 1 144 ? -39.972 11.064  -32.991 1.00 70.27  ? 144  HIS A ND1 1 
ATOM   1108 C CD2 . HIS A 1 144 ? -38.927 10.004  -31.341 1.00 70.16  ? 144  HIS A CD2 1 
ATOM   1109 C CE1 . HIS A 1 144 ? -39.595 9.866   -33.414 1.00 69.41  ? 144  HIS A CE1 1 
ATOM   1110 N NE2 . HIS A 1 144 ? -38.963 9.190   -32.459 1.00 69.74  ? 144  HIS A NE2 1 
ATOM   1111 N N   . SER A 1 145 ? -38.060 15.680  -30.747 1.00 70.12  ? 145  SER A N   1 
ATOM   1112 C CA  . SER A 1 145 ? -38.169 17.156  -30.708 1.00 71.63  ? 145  SER A CA  1 
ATOM   1113 C C   . SER A 1 145 ? -38.183 17.827  -32.071 1.00 80.61  ? 145  SER A C   1 
ATOM   1114 O O   . SER A 1 145 ? -37.987 19.053  -32.170 1.00 80.58  ? 145  SER A O   1 
ATOM   1115 C CB  . SER A 1 145 ? -37.028 17.761  -29.899 1.00 73.94  ? 145  SER A CB  1 
ATOM   1116 O OG  . SER A 1 145 ? -35.759 17.526  -30.487 1.00 80.61  ? 145  SER A OG  1 
ATOM   1117 N N   . GLY A 1 146 ? -38.459 17.061  -33.101 1.00 79.48  ? 146  GLY A N   1 
ATOM   1118 C CA  . GLY A 1 146 ? -38.510 17.566  -34.459 1.00 80.15  ? 146  GLY A CA  1 
ATOM   1119 C C   . GLY A 1 146 ? -37.253 18.225  -34.980 1.00 86.17  ? 146  GLY A C   1 
ATOM   1120 O O   . GLY A 1 146 ? -37.225 18.591  -36.150 1.00 85.54  ? 146  GLY A O   1 
ATOM   1121 N N   . GLU A 1 147 ? -36.204 18.363  -34.138 1.00 85.64  ? 147  GLU A N   1 
ATOM   1122 C CA  . GLU A 1 147 ? -34.936 18.995  -34.487 1.00 87.29  ? 147  GLU A CA  1 
ATOM   1123 C C   . GLU A 1 147 ? -34.497 18.617  -35.882 1.00 95.00  ? 147  GLU A C   1 
ATOM   1124 O O   . GLU A 1 147 ? -34.270 17.445  -36.184 1.00 94.42  ? 147  GLU A O   1 
ATOM   1125 C CB  . GLU A 1 147 ? -33.829 18.709  -33.455 1.00 88.87  ? 147  GLU A CB  1 
ATOM   1126 C CG  . GLU A 1 147 ? -32.735 19.776  -33.391 1.00 100.03 ? 147  GLU A CG  1 
ATOM   1127 C CD  . GLU A 1 147 ? -32.017 20.111  -34.688 1.00 120.92 ? 147  GLU A CD  1 
ATOM   1128 O OE1 . GLU A 1 147 ? -31.183 19.299  -35.145 1.00 116.43 ? 147  GLU A OE1 1 
ATOM   1129 O OE2 . GLU A 1 147 ? -32.372 21.142  -35.303 1.00 115.72 ? 147  GLU A OE2 1 
ATOM   1130 N N   . GLU A 1 148 ? -34.441 19.643  -36.738 1.00 95.11  ? 148  GLU A N   1 
ATOM   1131 C CA  . GLU A 1 148 ? -34.085 19.651  -38.152 1.00 96.90  ? 148  GLU A CA  1 
ATOM   1132 C C   . GLU A 1 148 ? -33.148 18.520  -38.594 1.00 104.30 ? 148  GLU A C   1 
ATOM   1133 O O   . GLU A 1 148 ? -33.431 17.880  -39.609 1.00 104.48 ? 148  GLU A O   1 
ATOM   1134 C CB  . GLU A 1 148 ? -33.501 21.028  -38.505 1.00 98.67  ? 148  GLU A CB  1 
ATOM   1135 C CG  . GLU A 1 148 ? -33.004 21.189  -39.931 1.00 110.98 ? 148  GLU A CG  1 
ATOM   1136 C CD  . GLU A 1 148 ? -32.246 22.478  -40.191 1.00 129.47 ? 148  GLU A CD  1 
ATOM   1137 O OE1 . GLU A 1 148 ? -31.667 23.047  -39.237 1.00 105.60 ? 148  GLU A OE1 1 
ATOM   1138 O OE2 . GLU A 1 148 ? -32.264 22.939  -41.354 1.00 130.13 ? 148  GLU A OE2 1 
ATOM   1139 N N   . HIS A 1 149 ? -32.077 18.245  -37.827 1.00 102.81 ? 149  HIS A N   1 
ATOM   1140 C CA  . HIS A 1 149 ? -31.092 17.228  -38.196 1.00 103.32 ? 149  HIS A CA  1 
ATOM   1141 C C   . HIS A 1 149 ? -31.316 15.848  -37.580 1.00 104.63 ? 149  HIS A C   1 
ATOM   1142 O O   . HIS A 1 149 ? -31.030 14.857  -38.252 1.00 103.70 ? 149  HIS A O   1 
ATOM   1143 C CB  . HIS A 1 149 ? -29.671 17.725  -37.893 1.00 104.98 ? 149  HIS A CB  1 
ATOM   1144 C CG  . HIS A 1 149 ? -29.342 19.006  -38.580 1.00 109.08 ? 149  HIS A CG  1 
ATOM   1145 N ND1 . HIS A 1 149 ? -29.474 20.225  -37.934 1.00 111.23 ? 149  HIS A ND1 1 
ATOM   1146 C CD2 . HIS A 1 149 ? -28.959 19.221  -39.862 1.00 111.68 ? 149  HIS A CD2 1 
ATOM   1147 C CE1 . HIS A 1 149 ? -29.143 21.139  -38.834 1.00 111.31 ? 149  HIS A CE1 1 
ATOM   1148 N NE2 . HIS A 1 149 ? -28.817 20.581  -40.009 1.00 111.73 ? 149  HIS A NE2 1 
ATOM   1149 N N   . ALA A 1 150 ? -31.830 15.787  -36.331 1.00 99.86  ? 150  ALA A N   1 
ATOM   1150 C CA  . ALA A 1 150 ? -32.076 14.587  -35.510 1.00 99.38  ? 150  ALA A CA  1 
ATOM   1151 C C   . ALA A 1 150 ? -32.418 13.256  -36.260 1.00 103.88 ? 150  ALA A C   1 
ATOM   1152 O O   . ALA A 1 150 ? -31.942 12.199  -35.829 1.00 103.14 ? 150  ALA A O   1 
ATOM   1153 C CB  . ALA A 1 150 ? -33.144 14.878  -34.476 1.00 99.84  ? 150  ALA A CB  1 
ATOM   1154 N N   . VAL A 1 151 ? -33.198 13.307  -37.370 1.00 101.38 ? 151  VAL A N   1 
ATOM   1155 C CA  . VAL A 1 151 ? -33.605 12.125  -38.162 1.00 101.47 ? 151  VAL A CA  1 
ATOM   1156 C C   . VAL A 1 151 ? -32.396 11.280  -38.589 1.00 108.09 ? 151  VAL A C   1 
ATOM   1157 O O   . VAL A 1 151 ? -31.561 11.733  -39.378 1.00 107.65 ? 151  VAL A O   1 
ATOM   1158 C CB  . VAL A 1 151 ? -34.540 12.474  -39.361 1.00 104.33 ? 151  VAL A CB  1 
ATOM   1159 C CG1 . VAL A 1 151 ? -34.841 11.243  -40.221 1.00 103.61 ? 151  VAL A CG1 1 
ATOM   1160 C CG2 . VAL A 1 151 ? -35.835 13.109  -38.876 1.00 103.93 ? 151  VAL A CG2 1 
ATOM   1161 N N   . GLY A 1 152 ? -32.321 10.075  -38.021 1.00 107.01 ? 152  GLY A N   1 
ATOM   1162 C CA  . GLY A 1 152 ? -31.256 9.101   -38.247 1.00 108.06 ? 152  GLY A CA  1 
ATOM   1163 C C   . GLY A 1 152 ? -29.851 9.639   -38.038 1.00 115.13 ? 152  GLY A C   1 
ATOM   1164 O O   . GLY A 1 152 ? -28.915 9.137   -38.667 1.00 114.96 ? 152  GLY A O   1 
ATOM   1165 N N   . ASN A 1 153 ? -29.700 10.692  -37.167 1.00 113.62 ? 153  ASN A N   1 
ATOM   1166 C CA  . ASN A 1 153 ? -28.412 11.329  -36.883 1.00 114.58 ? 153  ASN A CA  1 
ATOM   1167 C C   . ASN A 1 153 ? -27.528 10.417  -36.056 1.00 121.62 ? 153  ASN A C   1 
ATOM   1168 O O   . ASN A 1 153 ? -27.662 10.335  -34.828 1.00 120.78 ? 153  ASN A O   1 
ATOM   1169 C CB  . ASN A 1 153 ? -28.538 12.735  -36.275 1.00 115.60 ? 153  ASN A CB  1 
ATOM   1170 C CG  . ASN A 1 153 ? -27.264 13.536  -36.466 1.00 140.70 ? 153  ASN A CG  1 
ATOM   1171 O OD1 . ASN A 1 153 ? -26.272 13.318  -35.766 1.00 134.58 ? 153  ASN A OD1 1 
ATOM   1172 N ND2 . ASN A 1 153 ? -27.289 14.467  -37.431 1.00 135.50 ? 153  ASN A ND2 1 
ATOM   1173 N N   . ASP A 1 154 ? -26.632 9.710   -36.770 1.00 120.84 ? 154  ASP A N   1 
ATOM   1174 C CA  . ASP A 1 154 ? -25.692 8.701   -36.263 1.00 121.74 ? 154  ASP A CA  1 
ATOM   1175 C C   . ASP A 1 154 ? -24.651 9.260   -35.310 1.00 126.10 ? 154  ASP A C   1 
ATOM   1176 O O   . ASP A 1 154 ? -24.261 8.566   -34.372 1.00 124.80 ? 154  ASP A O   1 
ATOM   1177 C CB  . ASP A 1 154 ? -25.005 7.957   -37.430 1.00 124.36 ? 154  ASP A CB  1 
ATOM   1178 C CG  . ASP A 1 154 ? -24.588 8.818   -38.623 1.00 142.17 ? 154  ASP A CG  1 
ATOM   1179 O OD1 . ASP A 1 154 ? -24.461 10.054  -38.455 1.00 143.94 ? 154  ASP A OD1 1 
ATOM   1180 O OD2 . ASP A 1 154 ? -24.369 8.251   -39.719 1.00 150.23 ? 154  ASP A OD2 1 
ATOM   1181 N N   . THR A 1 155 ? -24.198 10.510  -35.577 1.00 123.87 ? 155  THR A N   1 
ATOM   1182 C CA  . THR A 1 155 ? -23.201 11.296  -34.836 1.00 123.94 ? 155  THR A CA  1 
ATOM   1183 C C   . THR A 1 155 ? -23.440 11.233  -33.317 1.00 127.63 ? 155  THR A C   1 
ATOM   1184 O O   . THR A 1 155 ? -22.537 10.843  -32.562 1.00 127.37 ? 155  THR A O   1 
ATOM   1185 C CB  . THR A 1 155 ? -23.186 12.729  -35.394 1.00 133.66 ? 155  THR A CB  1 
ATOM   1186 O OG1 . THR A 1 155 ? -22.905 12.679  -36.797 1.00 129.78 ? 155  THR A OG1 1 
ATOM   1187 C CG2 . THR A 1 155 ? -22.195 13.638  -34.685 1.00 134.05 ? 155  THR A CG2 1 
ATOM   1188 N N   . GLY A 1 156 ? -24.672 11.553  -32.915 1.00 123.79 ? 156  GLY A N   1 
ATOM   1189 C CA  . GLY A 1 156 ? -25.112 11.479  -31.529 1.00 123.41 ? 156  GLY A CA  1 
ATOM   1190 C C   . GLY A 1 156 ? -25.377 12.787  -30.821 1.00 125.54 ? 156  GLY A C   1 
ATOM   1191 O O   . GLY A 1 156 ? -26.149 12.814  -29.857 1.00 124.78 ? 156  GLY A O   1 
ATOM   1192 N N   . LYS A 1 157 ? -24.741 13.874  -31.290 1.00 121.47 ? 157  LYS A N   1 
ATOM   1193 C CA  . LYS A 1 157 ? -24.813 15.223  -30.717 1.00 121.03 ? 157  LYS A CA  1 
ATOM   1194 C C   . LYS A 1 157 ? -26.201 15.612  -30.144 1.00 124.31 ? 157  LYS A C   1 
ATOM   1195 O O   . LYS A 1 157 ? -26.272 16.228  -29.074 1.00 124.42 ? 157  LYS A O   1 
ATOM   1196 C CB  . LYS A 1 157 ? -24.331 16.256  -31.746 1.00 122.97 ? 157  LYS A CB  1 
ATOM   1197 C CG  . LYS A 1 157 ? -22.833 16.221  -31.997 1.00 131.44 ? 157  LYS A CG  1 
ATOM   1198 C CD  . LYS A 1 157 ? -22.448 16.973  -33.264 1.00 140.25 ? 157  LYS A CD  1 
ATOM   1199 C CE  . LYS A 1 157 ? -20.949 16.985  -33.487 1.00 142.76 ? 157  LYS A CE  1 
ATOM   1200 N NZ  . LYS A 1 157 ? -20.589 17.352  -34.885 1.00 140.43 ? 157  LYS A NZ  1 
ATOM   1201 N N   . HIS A 1 158 ? -27.287 15.212  -30.840 1.00 119.24 ? 158  HIS A N   1 
ATOM   1202 C CA  . HIS A 1 158 ? -28.690 15.473  -30.486 1.00 118.26 ? 158  HIS A CA  1 
ATOM   1203 C C   . HIS A 1 158 ? -29.187 14.811  -29.183 1.00 119.84 ? 158  HIS A C   1 
ATOM   1204 O O   . HIS A 1 158 ? -30.096 15.333  -28.529 1.00 119.26 ? 158  HIS A O   1 
ATOM   1205 C CB  . HIS A 1 158 ? -29.601 15.009  -31.628 1.00 119.00 ? 158  HIS A CB  1 
ATOM   1206 C CG  . HIS A 1 158 ? -29.424 15.754  -32.908 1.00 122.26 ? 158  HIS A CG  1 
ATOM   1207 N ND1 . HIS A 1 158 ? -28.578 15.289  -33.897 1.00 123.97 ? 158  HIS A ND1 1 
ATOM   1208 C CD2 . HIS A 1 158 ? -30.034 16.879  -33.344 1.00 123.71 ? 158  HIS A CD2 1 
ATOM   1209 C CE1 . HIS A 1 158 ? -28.687 16.152  -34.892 1.00 123.17 ? 158  HIS A CE1 1 
ATOM   1210 N NE2 . HIS A 1 158 ? -29.553 17.122  -34.605 1.00 123.46 ? 158  HIS A NE2 1 
ATOM   1211 N N   . GLY A 1 159 ? -28.646 13.645  -28.865 1.00 114.68 ? 159  GLY A N   1 
ATOM   1212 C CA  . GLY A 1 159 ? -29.079 12.890  -27.700 1.00 113.59 ? 159  GLY A CA  1 
ATOM   1213 C C   . GLY A 1 159 ? -28.155 12.957  -26.507 1.00 115.61 ? 159  GLY A C   1 
ATOM   1214 O O   . GLY A 1 159 ? -26.961 13.212  -26.649 1.00 114.96 ? 159  GLY A O   1 
ATOM   1215 N N   . LYS A 1 160 ? -28.707 12.708  -25.321 1.00 111.13 ? 160  LYS A N   1 
ATOM   1216 C CA  . LYS A 1 160 ? -27.959 12.677  -24.069 1.00 110.15 ? 160  LYS A CA  1 
ATOM   1217 C C   . LYS A 1 160 ? -27.366 11.276  -23.842 1.00 111.85 ? 160  LYS A C   1 
ATOM   1218 O O   . LYS A 1 160 ? -28.114 10.298  -23.675 1.00 109.94 ? 160  LYS A O   1 
ATOM   1219 C CB  . LYS A 1 160 ? -28.853 13.104  -22.872 1.00 112.23 ? 160  LYS A CB  1 
ATOM   1220 C CG  . LYS A 1 160 ? -28.130 13.168  -21.509 1.00 119.43 ? 160  LYS A CG  1 
ATOM   1221 C CD  . LYS A 1 160 ? -27.471 14.543  -21.256 1.00 122.36 ? 160  LYS A CD  1 
ATOM   1222 C CE  . LYS A 1 160 ? -26.521 14.569  -20.079 1.00 114.81 ? 160  LYS A CE  1 
ATOM   1223 N NZ  . LYS A 1 160 ? -25.101 14.382  -20.489 1.00 107.07 ? 160  LYS A NZ  1 
ATOM   1224 N N   . GLU A 1 161 ? -26.013 11.199  -23.845 1.00 107.62 ? 161  GLU A N   1 
ATOM   1225 C CA  . GLU A 1 161 ? -25.250 9.981   -23.585 1.00 107.01 ? 161  GLU A CA  1 
ATOM   1226 C C   . GLU A 1 161 ? -25.378 9.639   -22.105 1.00 110.18 ? 161  GLU A C   1 
ATOM   1227 O O   . GLU A 1 161 ? -25.389 10.548  -21.262 1.00 109.25 ? 161  GLU A O   1 
ATOM   1228 C CB  . GLU A 1 161 ? -23.769 10.188  -23.930 1.00 108.36 ? 161  GLU A CB  1 
ATOM   1229 C CG  . GLU A 1 161 ? -23.390 9.697   -25.312 1.00 120.81 ? 161  GLU A CG  1 
ATOM   1230 C CD  . GLU A 1 161 ? -21.934 9.312   -25.524 1.00 145.91 ? 161  GLU A CD  1 
ATOM   1231 O OE1 . GLU A 1 161 ? -21.311 8.759   -24.587 1.00 150.90 ? 161  GLU A OE1 1 
ATOM   1232 O OE2 . GLU A 1 161 ? -21.439 9.495   -26.661 1.00 135.26 ? 161  GLU A OE2 1 
ATOM   1233 N N   . ILE A 1 162 ? -25.498 8.334   -21.784 1.00 106.33 ? 162  ILE A N   1 
ATOM   1234 C CA  . ILE A 1 162 ? -25.604 7.874   -20.398 1.00 106.18 ? 162  ILE A CA  1 
ATOM   1235 C C   . ILE A 1 162 ? -24.851 6.557   -20.212 1.00 111.94 ? 162  ILE A C   1 
ATOM   1236 O O   . ILE A 1 162 ? -24.898 5.693   -21.100 1.00 111.56 ? 162  ILE A O   1 
ATOM   1237 C CB  . ILE A 1 162 ? -27.050 7.826   -19.830 1.00 108.89 ? 162  ILE A CB  1 
ATOM   1238 C CG1 . ILE A 1 162 ? -27.781 6.529   -20.276 1.00 108.51 ? 162  ILE A CG1 1 
ATOM   1239 C CG2 . ILE A 1 162 ? -27.855 9.099   -20.096 1.00 110.28 ? 162  ILE A CG2 1 
ATOM   1240 C CD1 . ILE A 1 162 ? -28.719 6.020   -19.354 1.00 108.78 ? 162  ILE A CD1 1 
ATOM   1241 N N   . LYS A 1 163 ? -24.191 6.404   -19.041 1.00 109.67 ? 163  LYS A N   1 
ATOM   1242 C CA  . LYS A 1 163 ? -23.383 5.234   -18.703 1.00 109.67 ? 163  LYS A CA  1 
ATOM   1243 C C   . LYS A 1 163 ? -24.028 4.401   -17.628 1.00 113.80 ? 163  LYS A C   1 
ATOM   1244 O O   . LYS A 1 163 ? -24.357 4.906   -16.553 1.00 114.03 ? 163  LYS A O   1 
ATOM   1245 C CB  . LYS A 1 163 ? -21.951 5.630   -18.294 1.00 111.93 ? 163  LYS A CB  1 
ATOM   1246 C CG  . LYS A 1 163 ? -21.297 6.705   -19.160 1.00 123.92 ? 163  LYS A CG  1 
ATOM   1247 C CD  . LYS A 1 163 ? -20.582 6.130   -20.373 1.00 135.89 ? 163  LYS A CD  1 
ATOM   1248 C CE  . LYS A 1 163 ? -20.026 7.220   -21.260 1.00 150.19 ? 163  LYS A CE  1 
ATOM   1249 N NZ  . LYS A 1 163 ? -19.266 6.666   -22.414 1.00 160.84 ? 163  LYS A NZ  1 
ATOM   1250 N N   . ILE A 1 164 ? -24.260 3.142   -17.939 1.00 110.56 ? 164  ILE A N   1 
ATOM   1251 C CA  . ILE A 1 164 ? -24.847 2.265   -16.957 1.00 111.39 ? 164  ILE A CA  1 
ATOM   1252 C C   . ILE A 1 164 ? -23.713 1.322   -16.482 1.00 120.00 ? 164  ILE A C   1 
ATOM   1253 O O   . ILE A 1 164 ? -23.047 0.654   -17.288 1.00 120.02 ? 164  ILE A O   1 
ATOM   1254 C CB  . ILE A 1 164 ? -26.201 1.641   -17.435 1.00 113.84 ? 164  ILE A CB  1 
ATOM   1255 C CG1 . ILE A 1 164 ? -27.362 2.157   -16.569 1.00 113.72 ? 164  ILE A CG1 1 
ATOM   1256 C CG2 . ILE A 1 164 ? -26.228 0.118   -17.541 1.00 114.14 ? 164  ILE A CG2 1 
ATOM   1257 C CD1 . ILE A 1 164 ? -28.359 2.969   -17.283 1.00 114.48 ? 164  ILE A CD1 1 
ATOM   1258 N N   . THR A 1 165 ? -23.401 1.437   -15.175 1.00 118.65 ? 165  THR A N   1 
ATOM   1259 C CA  . THR A 1 165 ? -22.348 0.722   -14.450 1.00 118.96 ? 165  THR A CA  1 
ATOM   1260 C C   . THR A 1 165 ? -23.027 -0.203  -13.420 1.00 125.14 ? 165  THR A C   1 
ATOM   1261 O O   . THR A 1 165 ? -23.967 0.253   -12.761 1.00 125.51 ? 165  THR A O   1 
ATOM   1262 C CB  . THR A 1 165 ? -21.447 1.767   -13.750 1.00 123.10 ? 165  THR A CB  1 
ATOM   1263 O OG1 . THR A 1 165 ? -20.916 2.657   -14.728 1.00 119.74 ? 165  THR A OG1 1 
ATOM   1264 C CG2 . THR A 1 165 ? -20.308 1.151   -12.945 1.00 121.97 ? 165  THR A CG2 1 
ATOM   1265 N N   . PRO A 1 166 ? -22.560 -1.466  -13.213 1.00 121.68 ? 166  PRO A N   1 
ATOM   1266 C CA  . PRO A 1 166 ? -23.198 -2.339  -12.200 1.00 121.25 ? 166  PRO A CA  1 
ATOM   1267 C C   . PRO A 1 166 ? -23.042 -1.828  -10.767 1.00 123.93 ? 166  PRO A C   1 
ATOM   1268 O O   . PRO A 1 166 ? -23.712 -2.322  -9.852  1.00 122.36 ? 166  PRO A O   1 
ATOM   1269 C CB  . PRO A 1 166 ? -22.512 -3.687  -12.416 1.00 123.12 ? 166  PRO A CB  1 
ATOM   1270 C CG  . PRO A 1 166 ? -21.927 -3.589  -13.804 1.00 127.69 ? 166  PRO A CG  1 
ATOM   1271 C CD  . PRO A 1 166 ? -21.475 -2.182  -13.904 1.00 123.13 ? 166  PRO A CD  1 
ATOM   1272 N N   . GLN A 1 167 ? -22.181 -0.797  -10.596 1.00 121.12 ? 167  GLN A N   1 
ATOM   1273 C CA  . GLN A 1 167 ? -21.929 -0.084  -9.343  1.00 121.00 ? 167  GLN A CA  1 
ATOM   1274 C C   . GLN A 1 167 ? -22.945 1.083   -9.196  1.00 126.15 ? 167  GLN A C   1 
ATOM   1275 O O   . GLN A 1 167 ? -23.334 1.404   -8.062  1.00 126.18 ? 167  GLN A O   1 
ATOM   1276 C CB  . GLN A 1 167 ? -20.480 0.433   -9.278  1.00 121.81 ? 167  GLN A CB  1 
ATOM   1277 C CG  . GLN A 1 167 ? -19.402 -0.586  -9.692  1.00 132.15 ? 167  GLN A CG  1 
ATOM   1278 C CD  . GLN A 1 167 ? -19.231 -1.814  -8.805  1.00 146.67 ? 167  GLN A CD  1 
ATOM   1279 O OE1 . GLN A 1 167 ? -18.871 -2.899  -9.276  1.00 141.24 ? 167  GLN A OE1 1 
ATOM   1280 N NE2 . GLN A 1 167 ? -19.406 -1.676  -7.500  1.00 135.60 ? 167  GLN A NE2 1 
ATOM   1281 N N   . SER A 1 168 ? -23.395 1.685   -10.352 1.00 122.02 ? 168  SER A N   1 
ATOM   1282 C CA  . SER A 1 168 ? -24.384 2.785   -10.432 1.00 121.03 ? 168  SER A CA  1 
ATOM   1283 C C   . SER A 1 168 ? -25.605 2.462   -11.359 1.00 122.82 ? 168  SER A C   1 
ATOM   1284 O O   . SER A 1 168 ? -26.016 3.318   -12.157 1.00 123.06 ? 168  SER A O   1 
ATOM   1285 C CB  . SER A 1 168 ? -23.705 4.094   -10.847 1.00 124.27 ? 168  SER A CB  1 
ATOM   1286 O OG  . SER A 1 168 ? -23.429 4.157   -12.238 1.00 132.68 ? 168  SER A OG  1 
ATOM   1287 N N   . SER A 1 169 ? -26.185 1.228   -11.228 1.00 116.26 ? 169  SER A N   1 
ATOM   1288 C CA  . SER A 1 169 ? -27.313 0.684   -12.020 1.00 114.06 ? 169  SER A CA  1 
ATOM   1289 C C   . SER A 1 169 ? -28.491 1.664   -12.275 1.00 115.23 ? 169  SER A C   1 
ATOM   1290 O O   . SER A 1 169 ? -29.088 1.613   -13.357 1.00 114.73 ? 169  SER A O   1 
ATOM   1291 C CB  . SER A 1 169 ? -27.833 -0.614  -11.409 1.00 114.87 ? 169  SER A CB  1 
ATOM   1292 O OG  . SER A 1 169 ? -27.186 -1.745  -11.969 1.00 116.42 ? 169  SER A OG  1 
ATOM   1293 N N   . THR A 1 170 ? -28.803 2.555   -11.298 1.00 109.23 ? 170  THR A N   1 
ATOM   1294 C CA  . THR A 1 170 ? -29.873 3.562   -11.393 1.00 107.30 ? 170  THR A CA  1 
ATOM   1295 C C   . THR A 1 170 ? -29.295 4.945   -11.756 1.00 108.95 ? 170  THR A C   1 
ATOM   1296 O O   . THR A 1 170 ? -28.578 5.553   -10.951 1.00 107.63 ? 170  THR A O   1 
ATOM   1297 C CB  . THR A 1 170 ? -30.742 3.547   -10.126 1.00 103.64 ? 170  THR A CB  1 
ATOM   1298 O OG1 . THR A 1 170 ? -31.368 2.274   -10.038 1.00 94.07  ? 170  THR A OG1 1 
ATOM   1299 C CG2 . THR A 1 170 ? -31.802 4.627   -10.121 1.00 101.49 ? 170  THR A CG2 1 
ATOM   1300 N N   . THR A 1 171 ? -29.625 5.427   -12.981 1.00 104.54 ? 171  THR A N   1 
ATOM   1301 C CA  . THR A 1 171 ? -29.170 6.720   -13.524 1.00 103.68 ? 171  THR A CA  1 
ATOM   1302 C C   . THR A 1 171 ? -30.344 7.595   -13.992 1.00 107.54 ? 171  THR A C   1 
ATOM   1303 O O   . THR A 1 171 ? -31.193 7.136   -14.754 1.00 106.97 ? 171  THR A O   1 
ATOM   1304 C CB  . THR A 1 171 ? -28.103 6.550   -14.605 1.00 107.11 ? 171  THR A CB  1 
ATOM   1305 O OG1 . THR A 1 171 ? -27.236 5.454   -14.288 1.00 108.00 ? 171  THR A OG1 1 
ATOM   1306 C CG2 . THR A 1 171 ? -27.261 7.803   -14.775 1.00 103.63 ? 171  THR A CG2 1 
ATOM   1307 N N   . GLU A 1 172 ? -30.350 8.872   -13.532 1.00 104.35 ? 172  GLU A N   1 
ATOM   1308 C CA  . GLU A 1 172 ? -31.357 9.930   -13.726 1.00 103.78 ? 172  GLU A CA  1 
ATOM   1309 C C   . GLU A 1 172 ? -30.804 11.019  -14.665 1.00 105.26 ? 172  GLU A C   1 
ATOM   1310 O O   . GLU A 1 172 ? -30.197 11.986  -14.197 1.00 105.15 ? 172  GLU A O   1 
ATOM   1311 C CB  . GLU A 1 172 ? -31.729 10.531  -12.328 1.00 105.51 ? 172  GLU A CB  1 
ATOM   1312 C CG  . GLU A 1 172 ? -32.898 11.522  -12.286 1.00 120.03 ? 172  GLU A CG  1 
ATOM   1313 C CD  . GLU A 1 172 ? -33.135 12.281  -10.985 1.00 138.15 ? 172  GLU A CD  1 
ATOM   1314 O OE1 . GLU A 1 172 ? -33.324 11.629  -9.931  1.00 119.10 ? 172  GLU A OE1 1 
ATOM   1315 O OE2 . GLU A 1 172 ? -33.199 13.533  -11.035 1.00 131.79 ? 172  GLU A OE2 1 
ATOM   1316 N N   . ALA A 1 173 ? -31.000 10.873  -15.980 1.00 99.67  ? 173  ALA A N   1 
ATOM   1317 C CA  . ALA A 1 173 ? -30.481 11.896  -16.884 1.00 98.69  ? 173  ALA A CA  1 
ATOM   1318 C C   . ALA A 1 173 ? -31.458 13.037  -17.109 1.00 99.90  ? 173  ALA A C   1 
ATOM   1319 O O   . ALA A 1 173 ? -32.644 12.805  -17.369 1.00 99.02  ? 173  ALA A O   1 
ATOM   1320 C CB  . ALA A 1 173 ? -30.080 11.282  -18.204 1.00 99.56  ? 173  ALA A CB  1 
ATOM   1321 N N   . GLU A 1 174 ? -30.959 14.271  -17.001 1.00 95.29  ? 174  GLU A N   1 
ATOM   1322 C CA  . GLU A 1 174 ? -31.786 15.452  -17.228 1.00 94.94  ? 174  GLU A CA  1 
ATOM   1323 C C   . GLU A 1 174 ? -31.794 15.832  -18.705 1.00 95.68  ? 174  GLU A C   1 
ATOM   1324 O O   . GLU A 1 174 ? -30.810 16.364  -19.248 1.00 95.07  ? 174  GLU A O   1 
ATOM   1325 C CB  . GLU A 1 174 ? -31.396 16.649  -16.333 1.00 96.76  ? 174  GLU A CB  1 
ATOM   1326 C CG  . GLU A 1 174 ? -32.537 17.636  -16.060 1.00 112.05 ? 174  GLU A CG  1 
ATOM   1327 C CD  . GLU A 1 174 ? -32.984 18.603  -17.150 1.00 137.20 ? 174  GLU A CD  1 
ATOM   1328 O OE1 . GLU A 1 174 ? -32.114 19.269  -17.760 1.00 133.43 ? 174  GLU A OE1 1 
ATOM   1329 O OE2 . GLU A 1 174 ? -34.215 18.756  -17.331 1.00 127.54 ? 174  GLU A OE2 1 
ATOM   1330 N N   . LEU A 1 175 ? -32.935 15.556  -19.344 1.00 88.97  ? 175  LEU A N   1 
ATOM   1331 C CA  . LEU A 1 175 ? -33.174 15.881  -20.738 1.00 86.83  ? 175  LEU A CA  1 
ATOM   1332 C C   . LEU A 1 175 ? -33.614 17.347  -20.835 1.00 89.15  ? 175  LEU A C   1 
ATOM   1333 O O   . LEU A 1 175 ? -34.628 17.751  -20.248 1.00 88.58  ? 175  LEU A O   1 
ATOM   1334 C CB  . LEU A 1 175 ? -34.212 14.925  -21.349 1.00 86.33  ? 175  LEU A CB  1 
ATOM   1335 C CG  . LEU A 1 175 ? -33.829 13.446  -21.423 1.00 90.16  ? 175  LEU A CG  1 
ATOM   1336 C CD1 . LEU A 1 175 ? -35.048 12.586  -21.599 1.00 90.07  ? 175  LEU A CD1 1 
ATOM   1337 C CD2 . LEU A 1 175 ? -32.855 13.176  -22.546 1.00 92.83  ? 175  LEU A CD2 1 
ATOM   1338 N N   . THR A 1 176 ? -32.794 18.144  -21.538 1.00 84.80  ? 176  THR A N   1 
ATOM   1339 C CA  . THR A 1 176 ? -32.956 19.582  -21.777 1.00 84.23  ? 176  THR A CA  1 
ATOM   1340 C C   . THR A 1 176 ? -34.331 19.928  -22.414 1.00 87.67  ? 176  THR A C   1 
ATOM   1341 O O   . THR A 1 176 ? -34.496 19.912  -23.646 1.00 87.03  ? 176  THR A O   1 
ATOM   1342 C CB  . THR A 1 176 ? -31.770 20.104  -22.635 1.00 87.50  ? 176  THR A CB  1 
ATOM   1343 O OG1 . THR A 1 176 ? -30.567 19.383  -22.338 1.00 84.40  ? 176  THR A OG1 1 
ATOM   1344 C CG2 . THR A 1 176 ? -31.574 21.612  -22.517 1.00 81.58  ? 176  THR A CG2 1 
ATOM   1345 N N   . GLY A 1 177 ? -35.289 20.240  -21.556 1.00 83.59  ? 177  GLY A N   1 
ATOM   1346 C CA  . GLY A 1 177 ? -36.628 20.631  -21.976 1.00 83.31  ? 177  GLY A CA  1 
ATOM   1347 C C   . GLY A 1 177 ? -37.734 19.629  -21.703 1.00 86.82  ? 177  GLY A C   1 
ATOM   1348 O O   . GLY A 1 177 ? -38.918 19.947  -21.887 1.00 86.05  ? 177  GLY A O   1 
ATOM   1349 N N   . TYR A 1 178 ? -37.364 18.418  -21.252 1.00 83.14  ? 178  TYR A N   1 
ATOM   1350 C CA  . TYR A 1 178 ? -38.347 17.364  -21.005 1.00 83.18  ? 178  TYR A CA  1 
ATOM   1351 C C   . TYR A 1 178 ? -38.351 16.842  -19.579 1.00 88.60  ? 178  TYR A C   1 
ATOM   1352 O O   . TYR A 1 178 ? -39.240 16.069  -19.218 1.00 87.84  ? 178  TYR A O   1 
ATOM   1353 C CB  . TYR A 1 178 ? -38.157 16.220  -22.016 1.00 83.86  ? 178  TYR A CB  1 
ATOM   1354 C CG  . TYR A 1 178 ? -38.248 16.686  -23.451 1.00 84.99  ? 178  TYR A CG  1 
ATOM   1355 C CD1 . TYR A 1 178 ? -39.477 16.782  -24.098 1.00 86.70  ? 178  TYR A CD1 1 
ATOM   1356 C CD2 . TYR A 1 178 ? -37.114 17.089  -24.145 1.00 85.42  ? 178  TYR A CD2 1 
ATOM   1357 C CE1 . TYR A 1 178 ? -39.569 17.226  -25.410 1.00 86.07  ? 178  TYR A CE1 1 
ATOM   1358 C CE2 . TYR A 1 178 ? -37.197 17.555  -25.450 1.00 86.05  ? 178  TYR A CE2 1 
ATOM   1359 C CZ  . TYR A 1 178 ? -38.428 17.624  -26.078 1.00 90.32  ? 178  TYR A CZ  1 
ATOM   1360 O OH  . TYR A 1 178 ? -38.524 18.085  -27.363 1.00 87.00  ? 178  TYR A OH  1 
ATOM   1361 N N   . GLY A 1 179 ? -37.374 17.279  -18.788 1.00 86.07  ? 179  GLY A N   1 
ATOM   1362 C CA  . GLY A 1 179 ? -37.221 16.851  -17.408 1.00 86.70  ? 179  GLY A CA  1 
ATOM   1363 C C   . GLY A 1 179 ? -36.269 15.686  -17.268 1.00 92.72  ? 179  GLY A C   1 
ATOM   1364 O O   . GLY A 1 179 ? -35.358 15.530  -18.079 1.00 92.13  ? 179  GLY A O   1 
ATOM   1365 N N   . THR A 1 180 ? -36.474 14.860  -16.245 1.00 91.40  ? 180  THR A N   1 
ATOM   1366 C CA  . THR A 1 180 ? -35.598 13.726  -15.993 1.00 92.37  ? 180  THR A CA  1 
ATOM   1367 C C   . THR A 1 180 ? -36.295 12.384  -16.299 1.00 96.80  ? 180  THR A C   1 
ATOM   1368 O O   . THR A 1 180 ? -37.530 12.261  -16.237 1.00 96.26  ? 180  THR A O   1 
ATOM   1369 C CB  . THR A 1 180 ? -34.973 13.789  -14.556 1.00 107.59 ? 180  THR A CB  1 
ATOM   1370 O OG1 . THR A 1 180 ? -35.970 13.708  -13.535 1.00 113.81 ? 180  THR A OG1 1 
ATOM   1371 C CG2 . THR A 1 180 ? -34.080 15.004  -14.323 1.00 104.28 ? 180  THR A CG2 1 
ATOM   1372 N N   . VAL A 1 181 ? -35.474 11.383  -16.635 1.00 93.69  ? 181  VAL A N   1 
ATOM   1373 C CA  . VAL A 1 181 ? -35.913 10.013  -16.886 1.00 94.11  ? 181  VAL A CA  1 
ATOM   1374 C C   . VAL A 1 181 ? -34.992 9.119   -16.063 1.00 97.98  ? 181  VAL A C   1 
ATOM   1375 O O   . VAL A 1 181 ? -33.765 9.167   -16.232 1.00 97.07  ? 181  VAL A O   1 
ATOM   1376 C CB  . VAL A 1 181 ? -35.978 9.624   -18.395 1.00 98.56  ? 181  VAL A CB  1 
ATOM   1377 C CG1 . VAL A 1 181 ? -34.610 9.712   -19.071 1.00 98.26  ? 181  VAL A CG1 1 
ATOM   1378 C CG2 . VAL A 1 181 ? -36.612 8.245   -18.602 1.00 98.35  ? 181  VAL A CG2 1 
ATOM   1379 N N   . THR A 1 182 ? -35.550 8.380   -15.108 1.00 95.24  ? 182  THR A N   1 
ATOM   1380 C CA  . THR A 1 182 ? -34.658 7.516   -14.364 1.00 95.62  ? 182  THR A CA  1 
ATOM   1381 C C   . THR A 1 182 ? -34.708 6.175   -15.059 1.00 99.67  ? 182  THR A C   1 
ATOM   1382 O O   . THR A 1 182 ? -35.771 5.669   -15.432 1.00 98.48  ? 182  THR A O   1 
ATOM   1383 C CB  . THR A 1 182 ? -34.846 7.561   -12.828 1.00 108.13 ? 182  THR A CB  1 
ATOM   1384 O OG1 . THR A 1 182 ? -33.549 7.612   -12.220 1.00 106.94 ? 182  THR A OG1 1 
ATOM   1385 C CG2 . THR A 1 182 ? -35.609 6.367   -12.260 1.00 108.14 ? 182  THR A CG2 1 
ATOM   1386 N N   . MET A 1 183 ? -33.523 5.661   -15.305 1.00 97.60  ? 183  MET A N   1 
ATOM   1387 C CA  . MET A 1 183 ? -33.285 4.416   -16.000 1.00 97.88  ? 183  MET A CA  1 
ATOM   1388 C C   . MET A 1 183 ? -32.700 3.377   -15.064 1.00 104.13 ? 183  MET A C   1 
ATOM   1389 O O   . MET A 1 183 ? -31.682 3.636   -14.409 1.00 104.11 ? 183  MET A O   1 
ATOM   1390 C CB  . MET A 1 183 ? -32.335 4.670   -17.159 1.00 99.90  ? 183  MET A CB  1 
ATOM   1391 C CG  . MET A 1 183 ? -32.639 3.787   -18.327 1.00 103.59 ? 183  MET A CG  1 
ATOM   1392 S SD  . MET A 1 183 ? -31.792 4.248   -19.804 1.00 107.76 ? 183  MET A SD  1 
ATOM   1393 C CE  . MET A 1 183 ? -32.505 5.839   -20.062 1.00 104.71 ? 183  MET A CE  1 
ATOM   1394 N N   . GLU A 1 184 ? -33.355 2.208   -15.000 1.00 102.03 ? 184  GLU A N   1 
ATOM   1395 C CA  . GLU A 1 184 ? -32.935 1.109   -14.153 1.00 103.30 ? 184  GLU A CA  1 
ATOM   1396 C C   . GLU A 1 184 ? -32.673 -0.124  -15.006 1.00 110.45 ? 184  GLU A C   1 
ATOM   1397 O O   . GLU A 1 184 ? -33.608 -0.832  -15.393 1.00 109.71 ? 184  GLU A O   1 
ATOM   1398 C CB  . GLU A 1 184 ? -33.963 0.868   -13.038 1.00 105.00 ? 184  GLU A CB  1 
ATOM   1399 C CG  . GLU A 1 184 ? -33.622 1.636   -11.769 1.00 117.12 ? 184  GLU A CG  1 
ATOM   1400 C CD  . GLU A 1 184 ? -34.765 2.265   -10.995 1.00 132.71 ? 184  GLU A CD  1 
ATOM   1401 O OE1 . GLU A 1 184 ? -35.556 1.515   -10.377 1.00 127.70 ? 184  GLU A OE1 1 
ATOM   1402 O OE2 . GLU A 1 184 ? -34.843 3.514   -10.972 1.00 114.33 ? 184  GLU A OE2 1 
ATOM   1403 N N   . CYS A 1 185 ? -31.383 -0.360  -15.317 1.00 110.04 ? 185  CYS A N   1 
ATOM   1404 C CA  . CYS A 1 185 ? -30.937 -1.444  -16.192 1.00 111.67 ? 185  CYS A CA  1 
ATOM   1405 C C   . CYS A 1 185 ? -30.365 -2.667  -15.469 1.00 120.15 ? 185  CYS A C   1 
ATOM   1406 O O   . CYS A 1 185 ? -29.698 -2.541  -14.440 1.00 119.24 ? 185  CYS A O   1 
ATOM   1407 C CB  . CYS A 1 185 ? -29.956 -0.905  -17.224 1.00 112.05 ? 185  CYS A CB  1 
ATOM   1408 S SG  . CYS A 1 185 ? -30.662 0.363   -18.307 1.00 116.02 ? 185  CYS A SG  1 
ATOM   1409 N N   . SER A 1 186 ? -30.615 -3.858  -16.049 1.00 120.99 ? 186  SER A N   1 
ATOM   1410 C CA  . SER A 1 186 ? -30.182 -5.163  -15.527 1.00 122.40 ? 186  SER A CA  1 
ATOM   1411 C C   . SER A 1 186 ? -29.275 -5.913  -16.543 1.00 128.32 ? 186  SER A C   1 
ATOM   1412 O O   . SER A 1 186 ? -29.682 -6.123  -17.696 1.00 127.60 ? 186  SER A O   1 
ATOM   1413 C CB  . SER A 1 186 ? -31.391 -6.020  -15.148 1.00 126.67 ? 186  SER A CB  1 
ATOM   1414 O OG  . SER A 1 186 ? -32.372 -5.300  -14.413 1.00 135.33 ? 186  SER A OG  1 
ATOM   1415 N N   . PRO A 1 187 ? -28.045 -6.321  -16.141 1.00 126.80 ? 187  PRO A N   1 
ATOM   1416 C CA  . PRO A 1 187 ? -27.161 -7.007  -17.103 1.00 127.10 ? 187  PRO A CA  1 
ATOM   1417 C C   . PRO A 1 187 ? -27.610 -8.419  -17.454 1.00 130.43 ? 187  PRO A C   1 
ATOM   1418 O O   . PRO A 1 187 ? -27.788 -9.258  -16.566 1.00 129.74 ? 187  PRO A O   1 
ATOM   1419 C CB  . PRO A 1 187 ? -25.775 -6.951  -16.441 1.00 129.01 ? 187  PRO A CB  1 
ATOM   1420 C CG  . PRO A 1 187 ? -26.050 -6.832  -14.990 1.00 133.31 ? 187  PRO A CG  1 
ATOM   1421 C CD  . PRO A 1 187 ? -27.385 -6.137  -14.829 1.00 128.75 ? 187  PRO A CD  1 
ATOM   1422 N N   . ARG A 1 188 ? -27.822 -8.656  -18.762 1.00 126.97 ? 188  ARG A N   1 
ATOM   1423 C CA  . ARG A 1 188 ? -28.281 -9.937  -19.298 1.00 127.20 ? 188  ARG A CA  1 
ATOM   1424 C C   . ARG A 1 188 ? -27.529 -10.372 -20.580 1.00 133.36 ? 188  ARG A C   1 
ATOM   1425 O O   . ARG A 1 188 ? -26.935 -9.524  -21.257 1.00 133.96 ? 188  ARG A O   1 
ATOM   1426 C CB  . ARG A 1 188 ? -29.805 -9.894  -19.543 1.00 126.12 ? 188  ARG A CB  1 
ATOM   1427 C CG  . ARG A 1 188 ? -30.656 -9.738  -18.280 1.00 132.83 ? 188  ARG A CG  1 
ATOM   1428 C CD  . ARG A 1 188 ? -30.597 -10.976 -17.406 1.00 138.75 ? 188  ARG A CD  1 
ATOM   1429 N NE  . ARG A 1 188 ? -30.737 -10.654 -15.988 1.00 144.62 ? 188  ARG A NE  1 
ATOM   1430 C CZ  . ARG A 1 188 ? -30.251 -11.399 -15.000 1.00 156.65 ? 188  ARG A CZ  1 
ATOM   1431 N NH1 . ARG A 1 188 ? -29.569 -12.507 -15.268 1.00 144.51 ? 188  ARG A NH1 1 
ATOM   1432 N NH2 . ARG A 1 188 ? -30.436 -11.039 -13.738 1.00 140.56 ? 188  ARG A NH2 1 
ATOM   1433 N N   . THR A 1 189 ? -27.545 -11.705 -20.883 1.00 129.92 ? 189  THR A N   1 
ATOM   1434 C CA  . THR A 1 189 ? -26.964 -12.398 -22.057 1.00 153.00 ? 189  THR A CA  1 
ATOM   1435 C C   . THR A 1 189 ? -27.524 -13.825 -22.111 1.00 156.60 ? 189  THR A C   1 
ATOM   1436 O O   . THR A 1 189 ? -28.732 -14.014 -22.232 1.00 109.01 ? 189  THR A O   1 
ATOM   1437 C CB  . THR A 1 189 ? -25.407 -12.363 -22.078 1.00 161.27 ? 189  THR A CB  1 
ATOM   1438 O OG1 . THR A 1 189 ? -24.975 -11.034 -22.374 1.00 161.99 ? 189  THR A OG1 1 
ATOM   1439 C CG2 . THR A 1 189 ? -24.797 -13.313 -23.125 1.00 158.44 ? 189  THR A CG2 1 
ATOM   1440 N N   . ASP A 1 192 ? -23.104 -15.129 -17.947 1.00 121.83 ? 192  ASP A N   1 
ATOM   1441 C CA  . ASP A 1 192 ? -22.974 -14.789 -16.529 1.00 121.62 ? 192  ASP A CA  1 
ATOM   1442 C C   . ASP A 1 192 ? -21.841 -13.791 -16.259 1.00 127.61 ? 192  ASP A C   1 
ATOM   1443 O O   . ASP A 1 192 ? -21.922 -13.041 -15.284 1.00 126.80 ? 192  ASP A O   1 
ATOM   1444 C CB  . ASP A 1 192 ? -22.848 -16.052 -15.644 1.00 122.63 ? 192  ASP A CB  1 
ATOM   1445 C CG  . ASP A 1 192 ? -21.575 -16.871 -15.823 1.00 125.21 ? 192  ASP A CG  1 
ATOM   1446 O OD1 . ASP A 1 192 ? -20.526 -16.462 -15.286 1.00 128.45 ? 192  ASP A OD1 1 
ATOM   1447 O OD2 . ASP A 1 192 ? -21.647 -17.954 -16.441 1.00 124.22 ? 192  ASP A OD2 1 
ATOM   1448 N N   . PHE A 1 193 ? -20.782 -13.804 -17.122 1.00 126.39 ? 193  PHE A N   1 
ATOM   1449 C CA  . PHE A 1 193 ? -19.556 -12.967 -17.130 1.00 127.07 ? 193  PHE A CA  1 
ATOM   1450 C C   . PHE A 1 193 ? -18.572 -13.205 -15.942 1.00 130.25 ? 193  PHE A C   1 
ATOM   1451 O O   . PHE A 1 193 ? -17.417 -12.782 -16.049 1.00 129.63 ? 193  PHE A O   1 
ATOM   1452 C CB  . PHE A 1 193 ? -19.857 -11.460 -17.268 1.00 129.41 ? 193  PHE A CB  1 
ATOM   1453 C CG  . PHE A 1 193 ? -20.795 -11.101 -18.394 1.00 131.66 ? 193  PHE A CG  1 
ATOM   1454 C CD1 . PHE A 1 193 ? -20.324 -10.953 -19.693 1.00 135.30 ? 193  PHE A CD1 1 
ATOM   1455 C CD2 . PHE A 1 193 ? -22.148 -10.886 -18.152 1.00 134.29 ? 193  PHE A CD2 1 
ATOM   1456 C CE1 . PHE A 1 193 ? -21.195 -10.614 -20.735 1.00 136.53 ? 193  PHE A CE1 1 
ATOM   1457 C CE2 . PHE A 1 193 ? -23.018 -10.546 -19.194 1.00 137.39 ? 193  PHE A CE2 1 
ATOM   1458 C CZ  . PHE A 1 193 ? -22.534 -10.405 -20.477 1.00 135.61 ? 193  PHE A CZ  1 
ATOM   1459 N N   . ASN A 1 194 ? -19.007 -13.866 -14.834 1.00 125.78 ? 194  ASN A N   1 
ATOM   1460 C CA  . ASN A 1 194 ? -18.118 -14.142 -13.695 1.00 124.79 ? 194  ASN A CA  1 
ATOM   1461 C C   . ASN A 1 194 ? -17.011 -15.054 -14.188 1.00 125.68 ? 194  ASN A C   1 
ATOM   1462 O O   . ASN A 1 194 ? -15.844 -14.642 -14.234 1.00 125.44 ? 194  ASN A O   1 
ATOM   1463 C CB  . ASN A 1 194 ? -18.833 -14.806 -12.473 1.00 125.77 ? 194  ASN A CB  1 
ATOM   1464 C CG  . ASN A 1 194 ? -20.335 -14.958 -12.519 1.00 137.41 ? 194  ASN A CG  1 
ATOM   1465 O OD1 . ASN A 1 194 ? -21.089 -13.978 -12.499 1.00 128.88 ? 194  ASN A OD1 1 
ATOM   1466 N ND2 . ASN A 1 194 ? -20.800 -16.201 -12.480 1.00 125.43 ? 194  ASN A ND2 1 
ATOM   1467 N N   . GLU A 1 195 ? -17.413 -16.271 -14.624 1.00 119.33 ? 195  GLU A N   1 
ATOM   1468 C CA  . GLU A 1 195 ? -16.549 -17.332 -15.145 1.00 117.30 ? 195  GLU A CA  1 
ATOM   1469 C C   . GLU A 1 195 ? -16.565 -17.343 -16.675 1.00 115.51 ? 195  GLU A C   1 
ATOM   1470 O O   . GLU A 1 195 ? -16.898 -18.359 -17.303 1.00 115.62 ? 195  GLU A O   1 
ATOM   1471 C CB  . GLU A 1 195 ? -16.923 -18.707 -14.538 1.00 118.68 ? 195  GLU A CB  1 
ATOM   1472 C CG  . GLU A 1 195 ? -16.993 -18.734 -13.017 1.00 130.85 ? 195  GLU A CG  1 
ATOM   1473 C CD  . GLU A 1 195 ? -15.845 -18.063 -12.283 1.00 154.23 ? 195  GLU A CD  1 
ATOM   1474 O OE1 . GLU A 1 195 ? -14.732 -18.638 -12.261 1.00 149.47 ? 195  GLU A OE1 1 
ATOM   1475 O OE2 . GLU A 1 195 ? -16.058 -16.951 -11.746 1.00 146.95 ? 195  GLU A OE2 1 
ATOM   1476 N N   . MET A 1 196 ? -16.221 -16.188 -17.267 1.00 106.74 ? 196  MET A N   1 
ATOM   1477 C CA  . MET A 1 196 ? -16.162 -16.019 -18.708 1.00 104.36 ? 196  MET A CA  1 
ATOM   1478 C C   . MET A 1 196 ? -14.921 -15.245 -19.111 1.00 100.28 ? 196  MET A C   1 
ATOM   1479 O O   . MET A 1 196 ? -14.599 -14.197 -18.535 1.00 99.29  ? 196  MET A O   1 
ATOM   1480 C CB  . MET A 1 196 ? -17.438 -15.358 -19.265 1.00 107.31 ? 196  MET A CB  1 
ATOM   1481 C CG  . MET A 1 196 ? -18.664 -16.270 -19.297 1.00 111.81 ? 196  MET A CG  1 
ATOM   1482 S SD  . MET A 1 196 ? -18.504 -17.766 -20.318 1.00 116.89 ? 196  MET A SD  1 
ATOM   1483 C CE  . MET A 1 196 ? -20.132 -18.514 -20.073 1.00 113.42 ? 196  MET A CE  1 
ATOM   1484 N N   . VAL A 1 197 ? -14.219 -15.804 -20.100 1.00 90.72  ? 197  VAL A N   1 
ATOM   1485 C CA  . VAL A 1 197 ? -13.001 -15.294 -20.710 1.00 87.48  ? 197  VAL A CA  1 
ATOM   1486 C C   . VAL A 1 197 ? -13.392 -14.724 -22.069 1.00 87.28  ? 197  VAL A C   1 
ATOM   1487 O O   . VAL A 1 197 ? -14.054 -15.392 -22.862 1.00 86.64  ? 197  VAL A O   1 
ATOM   1488 C CB  . VAL A 1 197 ? -11.938 -16.418 -20.862 1.00 90.22  ? 197  VAL A CB  1 
ATOM   1489 C CG1 . VAL A 1 197 ? -10.670 -15.899 -21.516 1.00 89.61  ? 197  VAL A CG1 1 
ATOM   1490 C CG2 . VAL A 1 197 ? -11.608 -17.059 -19.527 1.00 90.00  ? 197  VAL A CG2 1 
ATOM   1491 N N   . LEU A 1 198 ? -12.963 -13.501 -22.342 1.00 81.10  ? 198  LEU A N   1 
ATOM   1492 C CA  . LEU A 1 198 ? -13.203 -12.841 -23.611 1.00 79.63  ? 198  LEU A CA  1 
ATOM   1493 C C   . LEU A 1 198 ? -11.981 -13.129 -24.474 1.00 80.88  ? 198  LEU A C   1 
ATOM   1494 O O   . LEU A 1 198 ? -10.968 -12.415 -24.402 1.00 79.69  ? 198  LEU A O   1 
ATOM   1495 C CB  . LEU A 1 198 ? -13.432 -11.330 -23.373 1.00 79.71  ? 198  LEU A CB  1 
ATOM   1496 C CG  . LEU A 1 198 ? -13.473 -10.382 -24.574 1.00 83.66  ? 198  LEU A CG  1 
ATOM   1497 C CD1 . LEU A 1 198 ? -14.776 -10.479 -25.299 1.00 83.57  ? 198  LEU A CD1 1 
ATOM   1498 C CD2 . LEU A 1 198 ? -13.193 -8.960  -24.145 1.00 84.12  ? 198  LEU A CD2 1 
ATOM   1499 N N   . LEU A 1 199 ? -12.058 -14.223 -25.249 1.00 77.13  ? 199  LEU A N   1 
ATOM   1500 C CA  . LEU A 1 199 ? -10.948 -14.633 -26.103 1.00 77.31  ? 199  LEU A CA  1 
ATOM   1501 C C   . LEU A 1 199 ? -10.828 -13.752 -27.350 1.00 83.68  ? 199  LEU A C   1 
ATOM   1502 O O   . LEU A 1 199 ? -11.796 -13.642 -28.088 1.00 84.11  ? 199  LEU A O   1 
ATOM   1503 C CB  . LEU A 1 199 ? -11.030 -16.134 -26.449 1.00 76.81  ? 199  LEU A CB  1 
ATOM   1504 C CG  . LEU A 1 199 ? -10.011 -16.684 -27.470 1.00 81.04  ? 199  LEU A CG  1 
ATOM   1505 C CD1 . LEU A 1 199 ? -8.592  -16.609 -26.968 1.00 80.91  ? 199  LEU A CD1 1 
ATOM   1506 C CD2 . LEU A 1 199 ? -10.314 -18.100 -27.804 1.00 83.97  ? 199  LEU A CD2 1 
ATOM   1507 N N   . GLN A 1 200 ? -9.650  -13.128 -27.574 1.00 81.90  ? 200  GLN A N   1 
ATOM   1508 C CA  . GLN A 1 200 ? -9.389  -12.265 -28.732 1.00 83.44  ? 200  GLN A CA  1 
ATOM   1509 C C   . GLN A 1 200 ? -8.428  -12.931 -29.689 1.00 86.51  ? 200  GLN A C   1 
ATOM   1510 O O   . GLN A 1 200 ? -7.282  -13.198 -29.314 1.00 85.10  ? 200  GLN A O   1 
ATOM   1511 C CB  . GLN A 1 200 ? -8.794  -10.906 -28.326 1.00 86.15  ? 200  GLN A CB  1 
ATOM   1512 C CG  . GLN A 1 200 ? -9.723  -9.946  -27.594 1.00 112.61 ? 200  GLN A CG  1 
ATOM   1513 C CD  . GLN A 1 200 ? -9.046  -8.600  -27.467 1.00 132.80 ? 200  GLN A CD  1 
ATOM   1514 O OE1 . GLN A 1 200 ? -8.873  -7.872  -28.450 1.00 130.45 ? 200  GLN A OE1 1 
ATOM   1515 N NE2 . GLN A 1 200 ? -8.620  -8.239  -26.263 1.00 120.85 ? 200  GLN A NE2 1 
ATOM   1516 N N   . MET A 1 201 ? -8.868  -13.105 -30.943 1.00 83.84  ? 201  MET A N   1 
ATOM   1517 C CA  . MET A 1 201 ? -8.076  -13.743 -31.970 1.00 84.20  ? 201  MET A CA  1 
ATOM   1518 C C   . MET A 1 201 ? -7.264  -12.753 -32.771 1.00 91.50  ? 201  MET A C   1 
ATOM   1519 O O   . MET A 1 201 ? -6.105  -12.540 -32.431 1.00 91.95  ? 201  MET A O   1 
ATOM   1520 C CB  . MET A 1 201 ? -8.942  -14.646 -32.830 1.00 86.20  ? 201  MET A CB  1 
ATOM   1521 C CG  . MET A 1 201 ? -9.037  -16.048 -32.252 1.00 89.03  ? 201  MET A CG  1 
ATOM   1522 S SD  . MET A 1 201 ? -8.304  -17.322 -33.307 1.00 92.11  ? 201  MET A SD  1 
ATOM   1523 C CE  . MET A 1 201 ? -6.595  -16.642 -33.558 1.00 88.13  ? 201  MET A CE  1 
ATOM   1524 N N   . GLU A 1 202 ? -7.839  -12.147 -33.812 1.00 90.29  ? 202  GLU A N   1 
ATOM   1525 C CA  . GLU A 1 202 ? -7.160  -11.127 -34.613 1.00 91.23  ? 202  GLU A CA  1 
ATOM   1526 C C   . GLU A 1 202 ? -8.012  -9.862  -34.426 1.00 97.57  ? 202  GLU A C   1 
ATOM   1527 O O   . GLU A 1 202 ? -7.892  -9.167  -33.406 1.00 97.35  ? 202  GLU A O   1 
ATOM   1528 C CB  . GLU A 1 202 ? -7.094  -11.564 -36.093 1.00 92.70  ? 202  GLU A CB  1 
ATOM   1529 C CG  . GLU A 1 202 ? -5.734  -12.083 -36.534 1.00 107.04 ? 202  GLU A CG  1 
ATOM   1530 C CD  . GLU A 1 202 ? -4.677  -11.051 -36.898 1.00 128.45 ? 202  GLU A CD  1 
ATOM   1531 O OE1 . GLU A 1 202 ? -5.043  -9.929  -37.328 1.00 124.09 ? 202  GLU A OE1 1 
ATOM   1532 O OE2 . GLU A 1 202 ? -3.473  -11.387 -36.796 1.00 116.67 ? 202  GLU A OE2 1 
ATOM   1533 N N   . ASP A 1 203 ? -8.929  -9.636  -35.382 1.00 94.43  ? 203  ASP A N   1 
ATOM   1534 C CA  . ASP A 1 203 ? -9.960  -8.603  -35.441 1.00 93.86  ? 203  ASP A CA  1 
ATOM   1535 C C   . ASP A 1 203 ? -11.277 -9.303  -35.022 1.00 94.18  ? 203  ASP A C   1 
ATOM   1536 O O   . ASP A 1 203 ? -12.324 -8.667  -34.813 1.00 94.62  ? 203  ASP A O   1 
ATOM   1537 C CB  . ASP A 1 203 ? -10.061 -8.036  -36.871 1.00 96.79  ? 203  ASP A CB  1 
ATOM   1538 C CG  . ASP A 1 203 ? -9.851  -9.036  -38.014 1.00 117.06 ? 203  ASP A CG  1 
ATOM   1539 O OD1 . ASP A 1 203 ? -10.182 -10.243 -37.830 1.00 119.57 ? 203  ASP A OD1 1 
ATOM   1540 O OD2 . ASP A 1 203 ? -9.375  -8.611  -39.095 1.00 124.44 ? 203  ASP A OD2 1 
ATOM   1541 N N   . LYS A 1 204 ? -11.182 -10.639 -34.891 1.00 85.96  ? 204  LYS A N   1 
ATOM   1542 C CA  . LYS A 1 204 ? -12.243 -11.511 -34.428 1.00 83.67  ? 204  LYS A CA  1 
ATOM   1543 C C   . LYS A 1 204 ? -11.982 -11.712 -32.931 1.00 80.47  ? 204  LYS A C   1 
ATOM   1544 O O   . LYS A 1 204 ? -10.819 -11.658 -32.489 1.00 78.62  ? 204  LYS A O   1 
ATOM   1545 C CB  . LYS A 1 204 ? -12.222 -12.863 -35.186 1.00 87.06  ? 204  LYS A CB  1 
ATOM   1546 C CG  . LYS A 1 204 ? -12.697 -12.810 -36.659 1.00 102.99 ? 204  LYS A CG  1 
ATOM   1547 C CD  . LYS A 1 204 ? -13.004 -14.206 -37.292 1.00 110.21 ? 204  LYS A CD  1 
ATOM   1548 C CE  . LYS A 1 204 ? -14.313 -14.846 -36.842 1.00 113.36 ? 204  LYS A CE  1 
ATOM   1549 N NZ  . LYS A 1 204 ? -14.588 -16.147 -37.519 1.00 115.73 ? 204  LYS A NZ  1 
ATOM   1550 N N   . ALA A 1 205 ? -13.087 -11.881 -32.163 1.00 72.90  ? 205  ALA A N   1 
ATOM   1551 C CA  . ALA A 1 205 ? -13.157 -12.105 -30.714 1.00 70.95  ? 205  ALA A CA  1 
ATOM   1552 C C   . ALA A 1 205 ? -14.495 -12.749 -30.330 1.00 73.38  ? 205  ALA A C   1 
ATOM   1553 O O   . ALA A 1 205 ? -15.442 -12.740 -31.127 1.00 73.94  ? 205  ALA A O   1 
ATOM   1554 C CB  . ALA A 1 205 ? -12.951 -10.810 -29.947 1.00 71.46  ? 205  ALA A CB  1 
ATOM   1555 N N   . TRP A 1 206 ? -14.538 -13.401 -29.154 1.00 67.94  ? 206  TRP A N   1 
ATOM   1556 C CA  . TRP A 1 206 ? -15.719 -14.101 -28.641 1.00 66.92  ? 206  TRP A CA  1 
ATOM   1557 C C   . TRP A 1 206 ? -15.712 -14.074 -27.138 1.00 71.10  ? 206  TRP A C   1 
ATOM   1558 O O   . TRP A 1 206 ? -14.753 -13.618 -26.513 1.00 70.25  ? 206  TRP A O   1 
ATOM   1559 C CB  . TRP A 1 206 ? -15.702 -15.599 -28.980 1.00 65.42  ? 206  TRP A CB  1 
ATOM   1560 C CG  . TRP A 1 206 ? -15.641 -16.009 -30.410 1.00 66.04  ? 206  TRP A CG  1 
ATOM   1561 C CD1 . TRP A 1 206 ? -16.547 -16.791 -31.058 1.00 68.88  ? 206  TRP A CD1 1 
ATOM   1562 C CD2 . TRP A 1 206 ? -14.500 -15.917 -31.273 1.00 65.80  ? 206  TRP A CD2 1 
ATOM   1563 N NE1 . TRP A 1 206 ? -16.085 -17.102 -32.315 1.00 68.45  ? 206  TRP A NE1 1 
ATOM   1564 C CE2 . TRP A 1 206 ? -14.833 -16.569 -32.476 1.00 69.73  ? 206  TRP A CE2 1 
ATOM   1565 C CE3 . TRP A 1 206 ? -13.215 -15.365 -31.139 1.00 67.06  ? 206  TRP A CE3 1 
ATOM   1566 C CZ2 . TRP A 1 206 ? -13.961 -16.612 -33.567 1.00 69.29  ? 206  TRP A CZ2 1 
ATOM   1567 C CZ3 . TRP A 1 206 ? -12.380 -15.351 -32.235 1.00 68.75  ? 206  TRP A CZ3 1 
ATOM   1568 C CH2 . TRP A 1 206 ? -12.734 -16.008 -33.420 1.00 69.46  ? 206  TRP A CH2 1 
ATOM   1569 N N   . LEU A 1 207 ? -16.766 -14.653 -26.560 1.00 69.03  ? 207  LEU A N   1 
ATOM   1570 C CA  . LEU A 1 207 ? -16.882 -14.815 -25.134 1.00 69.53  ? 207  LEU A CA  1 
ATOM   1571 C C   . LEU A 1 207 ? -17.004 -16.264 -24.948 1.00 75.07  ? 207  LEU A C   1 
ATOM   1572 O O   . LEU A 1 207 ? -17.877 -16.901 -25.548 1.00 73.25  ? 207  LEU A O   1 
ATOM   1573 C CB  . LEU A 1 207 ? -18.074 -14.063 -24.523 1.00 69.88  ? 207  LEU A CB  1 
ATOM   1574 C CG  . LEU A 1 207 ? -17.770 -13.418 -23.162 1.00 74.70  ? 207  LEU A CG  1 
ATOM   1575 C CD1 . LEU A 1 207 ? -17.068 -12.080 -23.325 1.00 74.63  ? 207  LEU A CD1 1 
ATOM   1576 C CD2 . LEU A 1 207 ? -19.028 -13.237 -22.341 1.00 76.65  ? 207  LEU A CD2 1 
ATOM   1577 N N   . VAL A 1 208 ? -16.072 -16.802 -24.151 1.00 75.94  ? 208  VAL A N   1 
ATOM   1578 C CA  . VAL A 1 208 ? -15.944 -18.225 -23.891 1.00 76.91  ? 208  VAL A CA  1 
ATOM   1579 C C   . VAL A 1 208 ? -15.698 -18.586 -22.387 1.00 85.00  ? 208  VAL A C   1 
ATOM   1580 O O   . VAL A 1 208 ? -15.177 -17.789 -21.607 1.00 84.43  ? 208  VAL A O   1 
ATOM   1581 C CB  . VAL A 1 208 ? -14.861 -18.748 -24.856 1.00 79.74  ? 208  VAL A CB  1 
ATOM   1582 C CG1 . VAL A 1 208 ? -13.482 -18.861 -24.216 1.00 78.90  ? 208  VAL A CG1 1 
ATOM   1583 C CG2 . VAL A 1 208 ? -15.309 -20.031 -25.522 1.00 79.65  ? 208  VAL A CG2 1 
ATOM   1584 N N   . HIS A 1 209 ? -16.143 -19.790 -22.006 1.00 85.22  ? 209  HIS A N   1 
ATOM   1585 C CA  . HIS A 1 209 ? -16.053 -20.450 -20.682 1.00 86.76  ? 209  HIS A CA  1 
ATOM   1586 C C   . HIS A 1 209 ? -14.620 -20.405 -20.116 1.00 87.91  ? 209  HIS A C   1 
ATOM   1587 O O   . HIS A 1 209 ? -13.672 -20.558 -20.882 1.00 88.10  ? 209  HIS A O   1 
ATOM   1588 C CB  . HIS A 1 209 ? -16.517 -21.923 -20.828 1.00 89.42  ? 209  HIS A CB  1 
ATOM   1589 C CG  . HIS A 1 209 ? -17.307 -22.198 -22.095 1.00 94.45  ? 209  HIS A CG  1 
ATOM   1590 N ND1 . HIS A 1 209 ? -16.699 -22.195 -23.360 1.00 96.68  ? 209  HIS A ND1 1 
ATOM   1591 C CD2 . HIS A 1 209 ? -18.630 -22.443 -22.257 1.00 97.07  ? 209  HIS A CD2 1 
ATOM   1592 C CE1 . HIS A 1 209 ? -17.667 -22.437 -24.230 1.00 96.33  ? 209  HIS A CE1 1 
ATOM   1593 N NE2 . HIS A 1 209 ? -18.846 -22.588 -23.621 1.00 96.88  ? 209  HIS A NE2 1 
ATOM   1594 N N   . ARG A 1 210 ? -14.449 -20.184 -18.800 1.00 81.90  ? 210  ARG A N   1 
ATOM   1595 C CA  . ARG A 1 210 ? -13.105 -20.116 -18.178 1.00 80.08  ? 210  ARG A CA  1 
ATOM   1596 C C   . ARG A 1 210 ? -12.407 -21.466 -18.228 1.00 78.68  ? 210  ARG A C   1 
ATOM   1597 O O   . ARG A 1 210 ? -11.226 -21.544 -18.551 1.00 77.79  ? 210  ARG A O   1 
ATOM   1598 C CB  . ARG A 1 210 ? -13.179 -19.610 -16.726 1.00 80.69  ? 210  ARG A CB  1 
ATOM   1599 C CG  . ARG A 1 210 ? -11.844 -19.159 -16.120 1.00 89.71  ? 210  ARG A CG  1 
ATOM   1600 C CD  . ARG A 1 210 ? -11.992 -18.679 -14.673 1.00 103.08 ? 210  ARG A CD  1 
ATOM   1601 N NE  . ARG A 1 210 ? -12.775 -17.441 -14.560 1.00 115.58 ? 210  ARG A NE  1 
ATOM   1602 C CZ  . ARG A 1 210 ? -12.263 -16.240 -14.295 1.00 128.38 ? 210  ARG A CZ  1 
ATOM   1603 N NH1 . ARG A 1 210 ? -10.959 -16.099 -14.077 1.00 115.22 ? 210  ARG A NH1 1 
ATOM   1604 N NH2 . ARG A 1 210 ? -13.054 -15.172 -14.238 1.00 109.80 ? 210  ARG A NH2 1 
ATOM   1605 N N   . GLN A 1 211 ? -13.153 -22.521 -17.935 1.00 71.66  ? 211  GLN A N   1 
ATOM   1606 C CA  . GLN A 1 211 ? -12.647 -23.878 -17.959 1.00 69.82  ? 211  GLN A CA  1 
ATOM   1607 C C   . GLN A 1 211 ? -12.285 -24.344 -19.362 1.00 74.62  ? 211  GLN A C   1 
ATOM   1608 O O   . GLN A 1 211 ? -11.253 -24.978 -19.521 1.00 76.04  ? 211  GLN A O   1 
ATOM   1609 C CB  . GLN A 1 211 ? -13.640 -24.827 -17.297 1.00 69.77  ? 211  GLN A CB  1 
ATOM   1610 C CG  . GLN A 1 211 ? -13.735 -24.597 -15.807 1.00 55.77  ? 211  GLN A CG  1 
ATOM   1611 C CD  . GLN A 1 211 ? -15.034 -25.087 -15.247 1.00 85.60  ? 211  GLN A CD  1 
ATOM   1612 O OE1 . GLN A 1 211 ? -15.599 -26.099 -15.688 1.00 88.13  ? 211  GLN A OE1 1 
ATOM   1613 N NE2 . GLN A 1 211 ? -15.536 -24.380 -14.245 1.00 77.49  ? 211  GLN A NE2 1 
ATOM   1614 N N   . TRP A 1 212 ? -13.096 -24.022 -20.378 1.00 70.32  ? 212  TRP A N   1 
ATOM   1615 C CA  . TRP A 1 212 ? -12.809 -24.444 -21.751 1.00 70.14  ? 212  TRP A CA  1 
ATOM   1616 C C   . TRP A 1 212 ? -11.464 -23.863 -22.198 1.00 72.20  ? 212  TRP A C   1 
ATOM   1617 O O   . TRP A 1 212 ? -10.586 -24.599 -22.655 1.00 72.15  ? 212  TRP A O   1 
ATOM   1618 C CB  . TRP A 1 212 ? -13.959 -24.024 -22.696 1.00 69.16  ? 212  TRP A CB  1 
ATOM   1619 C CG  . TRP A 1 212 ? -13.781 -24.425 -24.132 1.00 70.19  ? 212  TRP A CG  1 
ATOM   1620 C CD1 . TRP A 1 212 ? -14.100 -25.627 -24.689 1.00 73.37  ? 212  TRP A CD1 1 
ATOM   1621 C CD2 . TRP A 1 212 ? -13.218 -23.627 -25.193 1.00 69.90  ? 212  TRP A CD2 1 
ATOM   1622 N NE1 . TRP A 1 212 ? -13.750 -25.640 -26.026 1.00 73.08  ? 212  TRP A NE1 1 
ATOM   1623 C CE2 . TRP A 1 212 ? -13.222 -24.421 -26.364 1.00 73.80  ? 212  TRP A CE2 1 
ATOM   1624 C CE3 . TRP A 1 212 ? -12.631 -22.348 -25.249 1.00 70.94  ? 212  TRP A CE3 1 
ATOM   1625 C CZ2 . TRP A 1 212 ? -12.750 -23.950 -27.594 1.00 72.76  ? 212  TRP A CZ2 1 
ATOM   1626 C CZ3 . TRP A 1 212 ? -12.162 -21.880 -26.470 1.00 72.11  ? 212  TRP A CZ3 1 
ATOM   1627 C CH2 . TRP A 1 212 ? -12.223 -22.678 -27.624 1.00 72.74  ? 212  TRP A CH2 1 
ATOM   1628 N N   . PHE A 1 213 ? -11.297 -22.554 -21.998 1.00 66.59  ? 213  PHE A N   1 
ATOM   1629 C CA  . PHE A 1 213 ? -10.101 -21.814 -22.358 1.00 65.16  ? 213  PHE A CA  1 
ATOM   1630 C C   . PHE A 1 213 ? -8.870  -22.428 -21.735 1.00 67.69  ? 213  PHE A C   1 
ATOM   1631 O O   . PHE A 1 213 ? -7.982  -22.876 -22.448 1.00 67.65  ? 213  PHE A O   1 
ATOM   1632 C CB  . PHE A 1 213 ? -10.250 -20.352 -21.917 1.00 66.30  ? 213  PHE A CB  1 
ATOM   1633 C CG  . PHE A 1 213 ? -9.032  -19.492 -22.108 1.00 66.72  ? 213  PHE A CG  1 
ATOM   1634 C CD1 . PHE A 1 213 ? -8.704  -18.992 -23.364 1.00 67.96  ? 213  PHE A CD1 1 
ATOM   1635 C CD2 . PHE A 1 213 ? -8.247  -19.129 -21.025 1.00 68.75  ? 213  PHE A CD2 1 
ATOM   1636 C CE1 . PHE A 1 213 ? -7.609  -18.156 -23.539 1.00 68.58  ? 213  PHE A CE1 1 
ATOM   1637 C CE2 . PHE A 1 213 ? -7.148  -18.286 -21.199 1.00 71.62  ? 213  PHE A CE2 1 
ATOM   1638 C CZ  . PHE A 1 213 ? -6.838  -17.806 -22.457 1.00 68.91  ? 213  PHE A CZ  1 
ATOM   1639 N N   . LEU A 1 214 ? -8.837  -22.467 -20.413 1.00 62.96  ? 214  LEU A N   1 
ATOM   1640 C CA  . LEU A 1 214 ? -7.696  -22.956 -19.642 1.00 62.63  ? 214  LEU A CA  1 
ATOM   1641 C C   . LEU A 1 214 ? -7.226  -24.413 -20.014 1.00 67.10  ? 214  LEU A C   1 
ATOM   1642 O O   . LEU A 1 214 ? -6.020  -24.712 -19.903 1.00 65.87  ? 214  LEU A O   1 
ATOM   1643 C CB  . LEU A 1 214 ? -7.973  -22.790 -18.135 1.00 61.68  ? 214  LEU A CB  1 
ATOM   1644 C CG  . LEU A 1 214 ? -8.004  -21.322 -17.672 1.00 64.15  ? 214  LEU A CG  1 
ATOM   1645 C CD1 . LEU A 1 214 ? -8.530  -21.190 -16.290 1.00 63.17  ? 214  LEU A CD1 1 
ATOM   1646 C CD2 . LEU A 1 214 ? -6.654  -20.673 -17.794 1.00 66.53  ? 214  LEU A CD2 1 
ATOM   1647 N N   . ASP A 1 215 ? -8.143  -25.254 -20.553 1.00 62.19  ? 215  ASP A N   1 
ATOM   1648 C CA  . ASP A 1 215 ? -7.790  -26.600 -20.959 1.00 60.49  ? 215  ASP A CA  1 
ATOM   1649 C C   . ASP A 1 215 ? -7.586  -26.730 -22.460 1.00 64.10  ? 215  ASP A C   1 
ATOM   1650 O O   . ASP A 1 215 ? -8.120  -27.643 -23.078 1.00 64.28  ? 215  ASP A O   1 
ATOM   1651 C CB  . ASP A 1 215 ? -8.782  -27.626 -20.418 1.00 61.72  ? 215  ASP A CB  1 
ATOM   1652 C CG  . ASP A 1 215 ? -8.092  -28.885 -19.954 1.00 72.70  ? 215  ASP A CG  1 
ATOM   1653 O OD1 . ASP A 1 215 ? -7.083  -28.773 -19.246 1.00 72.51  ? 215  ASP A OD1 1 
ATOM   1654 O OD2 . ASP A 1 215 ? -8.558  -29.991 -20.316 1.00 81.67  ? 215  ASP A OD2 1 
ATOM   1655 N N   . LEU A 1 216 ? -6.789  -25.840 -23.056 1.00 60.77  ? 216  LEU A N   1 
ATOM   1656 C CA  . LEU A 1 216 ? -6.492  -25.967 -24.489 1.00 60.63  ? 216  LEU A CA  1 
ATOM   1657 C C   . LEU A 1 216 ? -5.128  -26.603 -24.657 1.00 64.45  ? 216  LEU A C   1 
ATOM   1658 O O   . LEU A 1 216 ? -4.139  -26.144 -24.069 1.00 63.82  ? 216  LEU A O   1 
ATOM   1659 C CB  . LEU A 1 216 ? -6.511  -24.628 -25.290 1.00 60.50  ? 216  LEU A CB  1 
ATOM   1660 C CG  . LEU A 1 216 ? -7.736  -23.721 -25.236 1.00 63.33  ? 216  LEU A CG  1 
ATOM   1661 C CD1 . LEU A 1 216 ? -7.520  -22.483 -26.072 1.00 62.04  ? 216  LEU A CD1 1 
ATOM   1662 C CD2 . LEU A 1 216 ? -9.013  -24.460 -25.587 1.00 64.20  ? 216  LEU A CD2 1 
ATOM   1663 N N   . PRO A 1 217 ? -5.048  -27.614 -25.526 1.00 61.70  ? 217  PRO A N   1 
ATOM   1664 C CA  . PRO A 1 217 ? -3.750  -28.264 -25.798 1.00 61.90  ? 217  PRO A CA  1 
ATOM   1665 C C   . PRO A 1 217 ? -2.800  -27.419 -26.670 1.00 63.47  ? 217  PRO A C   1 
ATOM   1666 O O   . PRO A 1 217 ? -2.474  -27.832 -27.791 1.00 63.23  ? 217  PRO A O   1 
ATOM   1667 C CB  . PRO A 1 217 ? -4.177  -29.526 -26.543 1.00 64.05  ? 217  PRO A CB  1 
ATOM   1668 C CG  . PRO A 1 217 ? -5.408  -29.087 -27.298 1.00 68.17  ? 217  PRO A CG  1 
ATOM   1669 C CD  . PRO A 1 217 ? -6.137  -28.252 -26.289 1.00 63.39  ? 217  PRO A CD  1 
ATOM   1670 N N   . LEU A 1 218 ? -2.382  -26.234 -26.188 1.00 58.07  ? 218  LEU A N   1 
ATOM   1671 C CA  . LEU A 1 218 ? -1.501  -25.359 -26.971 1.00 57.57  ? 218  LEU A CA  1 
ATOM   1672 C C   . LEU A 1 218 ? -0.397  -24.712 -26.133 1.00 63.24  ? 218  LEU A C   1 
ATOM   1673 O O   . LEU A 1 218 ? -0.603  -24.575 -24.926 1.00 64.82  ? 218  LEU A O   1 
ATOM   1674 C CB  . LEU A 1 218 ? -2.312  -24.245 -27.674 1.00 56.74  ? 218  LEU A CB  1 
ATOM   1675 C CG  . LEU A 1 218 ? -3.384  -24.633 -28.691 1.00 58.67  ? 218  LEU A CG  1 
ATOM   1676 C CD1 . LEU A 1 218 ? -4.273  -23.445 -28.991 1.00 57.68  ? 218  LEU A CD1 1 
ATOM   1677 C CD2 . LEU A 1 218 ? -2.766  -25.204 -29.963 1.00 57.81  ? 218  LEU A CD2 1 
ATOM   1678 N N   . PRO A 1 219 ? 0.751   -24.259 -26.717 1.00 59.34  ? 219  PRO A N   1 
ATOM   1679 C CA  . PRO A 1 219 ? 1.765   -23.576 -25.890 1.00 59.20  ? 219  PRO A CA  1 
ATOM   1680 C C   . PRO A 1 219 ? 1.209   -22.267 -25.329 1.00 65.38  ? 219  PRO A C   1 
ATOM   1681 O O   . PRO A 1 219 ? 0.449   -21.614 -26.017 1.00 65.47  ? 219  PRO A O   1 
ATOM   1682 C CB  . PRO A 1 219 ? 2.946   -23.354 -26.858 1.00 60.62  ? 219  PRO A CB  1 
ATOM   1683 C CG  . PRO A 1 219 ? 2.677   -24.312 -28.024 1.00 65.45  ? 219  PRO A CG  1 
ATOM   1684 C CD  . PRO A 1 219 ? 1.184   -24.317 -28.130 1.00 61.19  ? 219  PRO A CD  1 
ATOM   1685 N N   . TRP A 1 220 ? 1.502   -21.931 -24.068 1.00 64.40  ? 220  TRP A N   1 
ATOM   1686 C CA  . TRP A 1 220 ? 0.960   -20.727 -23.454 1.00 65.90  ? 220  TRP A CA  1 
ATOM   1687 C C   . TRP A 1 220 ? 1.940   -19.960 -22.588 1.00 71.71  ? 220  TRP A C   1 
ATOM   1688 O O   . TRP A 1 220 ? 3.020   -20.438 -22.262 1.00 71.52  ? 220  TRP A O   1 
ATOM   1689 C CB  . TRP A 1 220 ? -0.308  -21.036 -22.663 1.00 65.41  ? 220  TRP A CB  1 
ATOM   1690 C CG  . TRP A 1 220 ? -0.075  -21.954 -21.507 1.00 67.28  ? 220  TRP A CG  1 
ATOM   1691 C CD1 . TRP A 1 220 ? 0.014   -23.310 -21.551 1.00 70.19  ? 220  TRP A CD1 1 
ATOM   1692 C CD2 . TRP A 1 220 ? 0.129   -21.581 -20.138 1.00 67.81  ? 220  TRP A CD2 1 
ATOM   1693 N NE1 . TRP A 1 220 ? 0.243   -23.810 -20.293 1.00 69.91  ? 220  TRP A NE1 1 
ATOM   1694 C CE2 . TRP A 1 220 ? 0.320   -22.771 -19.406 1.00 71.53  ? 220  TRP A CE2 1 
ATOM   1695 C CE3 . TRP A 1 220 ? 0.192   -20.349 -19.456 1.00 69.79  ? 220  TRP A CE3 1 
ATOM   1696 C CZ2 . TRP A 1 220 ? 0.527   -22.773 -18.023 1.00 71.31  ? 220  TRP A CZ2 1 
ATOM   1697 C CZ3 . TRP A 1 220 ? 0.347   -20.352 -18.079 1.00 71.46  ? 220  TRP A CZ3 1 
ATOM   1698 C CH2 . TRP A 1 220 ? 0.523   -21.553 -17.378 1.00 72.21  ? 220  TRP A CH2 1 
ATOM   1699 N N   . LEU A 1 221 ? 1.516   -18.778 -22.186 1.00 68.94  ? 221  LEU A N   1 
ATOM   1700 C CA  . LEU A 1 221 ? 2.275   -17.876 -21.367 1.00 69.07  ? 221  LEU A CA  1 
ATOM   1701 C C   . LEU A 1 221 ? 1.295   -17.268 -20.411 1.00 78.60  ? 221  LEU A C   1 
ATOM   1702 O O   . LEU A 1 221 ? 0.163   -16.984 -20.827 1.00 76.27  ? 221  LEU A O   1 
ATOM   1703 C CB  . LEU A 1 221 ? 2.897   -16.751 -22.225 1.00 68.13  ? 221  LEU A CB  1 
ATOM   1704 C CG  . LEU A 1 221 ? 4.183   -17.062 -22.965 1.00 71.02  ? 221  LEU A CG  1 
ATOM   1705 C CD1 . LEU A 1 221 ? 4.712   -15.829 -23.677 1.00 71.16  ? 221  LEU A CD1 1 
ATOM   1706 C CD2 . LEU A 1 221 ? 5.228   -17.610 -22.037 1.00 70.83  ? 221  LEU A CD2 1 
ATOM   1707 N N   . PRO A 1 222 ? 1.703   -17.023 -19.132 1.00 80.78  ? 222  PRO A N   1 
ATOM   1708 C CA  . PRO A 1 222 ? 0.767   -16.399 -18.185 1.00 81.53  ? 222  PRO A CA  1 
ATOM   1709 C C   . PRO A 1 222 ? 0.510   -14.934 -18.549 1.00 86.59  ? 222  PRO A C   1 
ATOM   1710 O O   . PRO A 1 222 ? 1.353   -14.290 -19.207 1.00 85.28  ? 222  PRO A O   1 
ATOM   1711 C CB  . PRO A 1 222 ? 1.479   -16.553 -16.835 1.00 83.13  ? 222  PRO A CB  1 
ATOM   1712 C CG  . PRO A 1 222 ? 2.554   -17.573 -17.062 1.00 86.91  ? 222  PRO A CG  1 
ATOM   1713 C CD  . PRO A 1 222 ? 2.984   -17.342 -18.466 1.00 82.29  ? 222  PRO A CD  1 
ATOM   1714 N N   . GLY A 1 223 ? -0.639  -14.425 -18.110 1.00 84.90  ? 223  GLY A N   1 
ATOM   1715 C CA  . GLY A 1 223 ? -1.033  -13.047 -18.370 1.00 85.84  ? 223  GLY A CA  1 
ATOM   1716 C C   . GLY A 1 223 ? 0.100   -12.085 -18.115 1.00 92.46  ? 223  GLY A C   1 
ATOM   1717 O O   . GLY A 1 223 ? 0.567   -11.407 -19.038 1.00 91.83  ? 223  GLY A O   1 
ATOM   1718 N N   . ALA A 1 224 ? 0.626   -12.151 -16.875 1.00 91.29  ? 224  ALA A N   1 
ATOM   1719 C CA  . ALA A 1 224 ? 1.739   -11.365 -16.337 1.00 91.59  ? 224  ALA A CA  1 
ATOM   1720 C C   . ALA A 1 224 ? 2.912   -11.182 -17.311 1.00 99.99  ? 224  ALA A C   1 
ATOM   1721 O O   . ALA A 1 224 ? 3.452   -10.075 -17.402 1.00 98.91  ? 224  ALA A O   1 
ATOM   1722 C CB  . ALA A 1 224 ? 2.226   -11.986 -15.034 1.00 91.72  ? 224  ALA A CB  1 
ATOM   1723 N N   . ASP A 1 225 ? 3.289   -12.249 -18.053 1.00 100.74 ? 225  ASP A N   1 
ATOM   1724 C CA  . ASP A 1 225 ? 4.420   -12.221 -18.976 1.00 101.92 ? 225  ASP A CA  1 
ATOM   1725 C C   . ASP A 1 225 ? 4.257   -11.261 -20.123 1.00 107.91 ? 225  ASP A C   1 
ATOM   1726 O O   . ASP A 1 225 ? 3.283   -11.340 -20.871 1.00 108.11 ? 225  ASP A O   1 
ATOM   1727 C CB  . ASP A 1 225 ? 4.776   -13.618 -19.504 1.00 104.16 ? 225  ASP A CB  1 
ATOM   1728 C CG  . ASP A 1 225 ? 6.072   -13.599 -20.298 1.00 118.19 ? 225  ASP A CG  1 
ATOM   1729 O OD1 . ASP A 1 225 ? 7.154   -13.647 -19.672 1.00 119.81 ? 225  ASP A OD1 1 
ATOM   1730 O OD2 . ASP A 1 225 ? 6.006   -13.450 -21.535 1.00 124.87 ? 225  ASP A OD2 1 
ATOM   1731 N N   . THR A 1 226 ? 5.247   -10.375 -20.267 1.00 105.95 ? 226  THR A N   1 
ATOM   1732 C CA  . THR A 1 226 ? 5.354   -9.396  -21.347 1.00 106.79 ? 226  THR A CA  1 
ATOM   1733 C C   . THR A 1 226 ? 6.750   -9.575  -22.004 1.00 111.94 ? 226  THR A C   1 
ATOM   1734 O O   . THR A 1 226 ? 7.125   -8.831  -22.914 1.00 111.76 ? 226  THR A O   1 
ATOM   1735 C CB  . THR A 1 226 ? 4.969   -7.962  -20.875 1.00 117.44 ? 226  THR A CB  1 
ATOM   1736 O OG1 . THR A 1 226 ? 3.900   -8.025  -19.918 1.00 118.94 ? 226  THR A OG1 1 
ATOM   1737 C CG2 . THR A 1 226 ? 4.546   -7.050  -22.036 1.00 114.77 ? 226  THR A CG2 1 
ATOM   1738 N N   . GLN A 1 227 ? 7.497   -10.607 -21.557 1.00 109.06 ? 227  GLN A N   1 
ATOM   1739 C CA  . GLN A 1 227 ? 8.800   -10.983 -22.117 1.00 109.09 ? 227  GLN A CA  1 
ATOM   1740 C C   . GLN A 1 227 ? 8.548   -11.548 -23.532 1.00 112.03 ? 227  GLN A C   1 
ATOM   1741 O O   . GLN A 1 227 ? 9.117   -11.044 -24.512 1.00 111.63 ? 227  GLN A O   1 
ATOM   1742 C CB  . GLN A 1 227 ? 9.528   -12.008 -21.185 1.00 110.56 ? 227  GLN A CB  1 
ATOM   1743 C CG  . GLN A 1 227 ? 10.622  -12.895 -21.818 1.00 123.18 ? 227  GLN A CG  1 
ATOM   1744 C CD  . GLN A 1 227 ? 11.778  -12.108 -22.399 1.00 143.97 ? 227  GLN A CD  1 
ATOM   1745 O OE1 . GLN A 1 227 ? 11.844  -11.851 -23.609 1.00 137.46 ? 227  GLN A OE1 1 
ATOM   1746 N NE2 . GLN A 1 227 ? 12.708  -11.699 -21.547 1.00 139.09 ? 227  GLN A NE2 1 
ATOM   1747 N N   . GLY A 1 228 ? 7.657   -12.549 -23.602 1.00 107.01 ? 228  GLY A N   1 
ATOM   1748 C CA  . GLY A 1 228 ? 7.263   -13.239 -24.825 1.00 105.80 ? 228  GLY A CA  1 
ATOM   1749 C C   . GLY A 1 228 ? 8.461   -13.811 -25.543 1.00 106.89 ? 228  GLY A C   1 
ATOM   1750 O O   . GLY A 1 228 ? 8.885   -13.262 -26.565 1.00 106.91 ? 228  GLY A O   1 
ATOM   1751 N N   . SER A 1 229 ? 9.066   -14.859 -24.963 1.00 100.42 ? 229  SER A N   1 
ATOM   1752 C CA  . SER A 1 229 ? 10.252  -15.487 -25.536 1.00 99.01  ? 229  SER A CA  1 
ATOM   1753 C C   . SER A 1 229 ? 10.185  -16.995 -25.388 1.00 99.81  ? 229  SER A C   1 
ATOM   1754 O O   . SER A 1 229 ? 10.433  -17.717 -26.370 1.00 100.82 ? 229  SER A O   1 
ATOM   1755 C CB  . SER A 1 229 ? 11.517  -14.954 -24.870 1.00 103.25 ? 229  SER A CB  1 
ATOM   1756 O OG  . SER A 1 229 ? 12.401  -14.359 -25.808 1.00 112.74 ? 229  SER A OG  1 
ATOM   1757 N N   . ASN A 1 230 ? 9.847   -17.473 -24.154 1.00 90.72  ? 230  ASN A N   1 
ATOM   1758 C CA  . ASN A 1 230 ? 9.777   -18.897 -23.810 1.00 86.92  ? 230  ASN A CA  1 
ATOM   1759 C C   . ASN A 1 230 ? 8.405   -19.310 -23.288 1.00 80.92  ? 230  ASN A C   1 
ATOM   1760 O O   . ASN A 1 230 ? 7.934   -18.853 -22.238 1.00 79.49  ? 230  ASN A O   1 
ATOM   1761 C CB  . ASN A 1 230 ? 10.897  -19.289 -22.862 1.00 89.18  ? 230  ASN A CB  1 
ATOM   1762 C CG  . ASN A 1 230 ? 10.909  -18.513 -21.570 1.00 115.58 ? 230  ASN A CG  1 
ATOM   1763 O OD1 . ASN A 1 230 ? 10.304  -18.927 -20.562 1.00 101.65 ? 230  ASN A OD1 1 
ATOM   1764 N ND2 . ASN A 1 230 ? 11.591  -17.365 -21.585 1.00 112.46 ? 230  ASN A ND2 1 
ATOM   1765 N N   . TRP A 1 231 ? 7.797   -20.228 -24.048 1.00 70.00  ? 231  TRP A N   1 
ATOM   1766 C CA  . TRP A 1 231 ? 6.443   -20.740 -23.925 1.00 65.61  ? 231  TRP A CA  1 
ATOM   1767 C C   . TRP A 1 231 ? 6.292   -22.032 -23.169 1.00 65.63  ? 231  TRP A C   1 
ATOM   1768 O O   . TRP A 1 231 ? 7.057   -22.963 -23.419 1.00 67.90  ? 231  TRP A O   1 
ATOM   1769 C CB  . TRP A 1 231 ? 5.956   -20.984 -25.338 1.00 63.18  ? 231  TRP A CB  1 
ATOM   1770 C CG  . TRP A 1 231 ? 5.746   -19.741 -26.156 1.00 63.30  ? 231  TRP A CG  1 
ATOM   1771 C CD1 . TRP A 1 231 ? 6.630   -19.152 -27.017 1.00 65.77  ? 231  TRP A CD1 1 
ATOM   1772 C CD2 . TRP A 1 231 ? 4.518   -19.012 -26.279 1.00 62.54  ? 231  TRP A CD2 1 
ATOM   1773 N NE1 . TRP A 1 231 ? 6.030   -18.093 -27.657 1.00 64.47  ? 231  TRP A NE1 1 
ATOM   1774 C CE2 . TRP A 1 231 ? 4.729   -17.992 -27.230 1.00 65.75  ? 231  TRP A CE2 1 
ATOM   1775 C CE3 . TRP A 1 231 ? 3.249   -19.146 -25.693 1.00 63.32  ? 231  TRP A CE3 1 
ATOM   1776 C CZ2 . TRP A 1 231 ? 3.723   -17.094 -27.590 1.00 65.00  ? 231  TRP A CZ2 1 
ATOM   1777 C CZ3 . TRP A 1 231 ? 2.264   -18.245 -26.030 1.00 64.86  ? 231  TRP A CZ3 1 
ATOM   1778 C CH2 . TRP A 1 231 ? 2.495   -17.247 -26.988 1.00 65.62  ? 231  TRP A CH2 1 
ATOM   1779 N N   . ILE A 1 232 ? 5.254   -22.141 -22.309 1.00 56.48  ? 232  ILE A N   1 
ATOM   1780 C CA  . ILE A 1 232 ? 4.959   -23.397 -21.588 1.00 53.15  ? 232  ILE A CA  1 
ATOM   1781 C C   . ILE A 1 232 ? 4.306   -24.349 -22.603 1.00 54.62  ? 232  ILE A C   1 
ATOM   1782 O O   . ILE A 1 232 ? 3.635   -23.862 -23.501 1.00 56.61  ? 232  ILE A O   1 
ATOM   1783 C CB  . ILE A 1 232 ? 4.036   -23.133 -20.371 1.00 55.13  ? 232  ILE A CB  1 
ATOM   1784 C CG1 . ILE A 1 232 ? 4.697   -22.213 -19.342 1.00 54.79  ? 232  ILE A CG1 1 
ATOM   1785 C CG2 . ILE A 1 232 ? 3.573   -24.433 -19.716 1.00 55.76  ? 232  ILE A CG2 1 
ATOM   1786 C CD1 . ILE A 1 232 ? 3.907   -21.044 -18.998 1.00 67.43  ? 232  ILE A CD1 1 
ATOM   1787 N N   . GLN A 1 233 ? 4.514   -25.672 -22.487 1.00 47.64  ? 233  GLN A N   1 
ATOM   1788 C CA  . GLN A 1 233 ? 3.914   -26.712 -23.348 1.00 46.54  ? 233  GLN A CA  1 
ATOM   1789 C C   . GLN A 1 233 ? 4.299   -26.680 -24.856 1.00 49.22  ? 233  GLN A C   1 
ATOM   1790 O O   . GLN A 1 233 ? 3.514   -27.194 -25.651 1.00 47.75  ? 233  GLN A O   1 
ATOM   1791 C CB  . GLN A 1 233 ? 2.366   -26.723 -23.227 1.00 47.20  ? 233  GLN A CB  1 
ATOM   1792 C CG  . GLN A 1 233 ? 1.820   -27.273 -21.921 1.00 68.49  ? 233  GLN A CG  1 
ATOM   1793 C CD  . GLN A 1 233 ? 0.398   -26.830 -21.618 1.00 97.47  ? 233  GLN A CD  1 
ATOM   1794 O OE1 . GLN A 1 233 ? 0.003   -26.719 -20.446 1.00 99.55  ? 233  GLN A OE1 1 
ATOM   1795 N NE2 . GLN A 1 233 ? -0.410  -26.549 -22.646 1.00 83.80  ? 233  GLN A NE2 1 
ATOM   1796 N N   . LYS A 1 234 ? 5.490   -26.163 -25.257 1.00 46.34  ? 234  LYS A N   1 
ATOM   1797 C CA  . LYS A 1 234 ? 5.883   -26.131 -26.696 1.00 47.37  ? 234  LYS A CA  1 
ATOM   1798 C C   . LYS A 1 234 ? 5.603   -27.469 -27.397 1.00 55.98  ? 234  LYS A C   1 
ATOM   1799 O O   . LYS A 1 234 ? 5.282   -27.500 -28.589 1.00 55.94  ? 234  LYS A O   1 
ATOM   1800 C CB  . LYS A 1 234 ? 7.366   -25.725 -26.905 1.00 48.38  ? 234  LYS A CB  1 
ATOM   1801 C CG  . LYS A 1 234 ? 7.667   -24.256 -26.638 1.00 51.76  ? 234  LYS A CG  1 
ATOM   1802 C CD  . LYS A 1 234 ? 9.152   -23.935 -26.510 1.00 47.04  ? 234  LYS A CD  1 
ATOM   1803 C CE  . LYS A 1 234 ? 9.570   -24.022 -25.054 1.00 64.55  ? 234  LYS A CE  1 
ATOM   1804 N NZ  . LYS A 1 234 ? 9.866   -22.678 -24.482 1.00 73.24  ? 234  LYS A NZ  1 
ATOM   1805 N N   . GLU A 1 235 ? 5.694   -28.567 -26.620 1.00 55.26  ? 235  GLU A N   1 
ATOM   1806 C CA  . GLU A 1 235 ? 5.469   -29.973 -26.971 1.00 56.27  ? 235  GLU A CA  1 
ATOM   1807 C C   . GLU A 1 235 ? 4.149   -30.195 -27.726 1.00 63.71  ? 235  GLU A C   1 
ATOM   1808 O O   . GLU A 1 235 ? 4.006   -31.183 -28.462 1.00 64.43  ? 235  GLU A O   1 
ATOM   1809 C CB  . GLU A 1 235 ? 5.445   -30.822 -25.682 1.00 57.46  ? 235  GLU A CB  1 
ATOM   1810 C CG  . GLU A 1 235 ? 6.732   -30.747 -24.880 1.00 73.21  ? 235  GLU A CG  1 
ATOM   1811 C CD  . GLU A 1 235 ? 6.833   -29.628 -23.861 1.00 101.96 ? 235  GLU A CD  1 
ATOM   1812 O OE1 . GLU A 1 235 ? 5.842   -29.399 -23.129 1.00 101.57 ? 235  GLU A OE1 1 
ATOM   1813 O OE2 . GLU A 1 235 ? 7.925   -29.019 -23.758 1.00 95.23  ? 235  GLU A OE2 1 
ATOM   1814 N N   . THR A 1 236 ? 3.171   -29.295 -27.518 1.00 60.05  ? 236  THR A N   1 
ATOM   1815 C CA  . THR A 1 236 ? 1.852   -29.399 -28.136 1.00 59.12  ? 236  THR A CA  1 
ATOM   1816 C C   . THR A 1 236 ? 1.906   -29.025 -29.620 1.00 63.42  ? 236  THR A C   1 
ATOM   1817 O O   . THR A 1 236 ? 0.993   -29.382 -30.348 1.00 62.46  ? 236  THR A O   1 
ATOM   1818 C CB  . THR A 1 236 ? 0.811   -28.621 -27.316 1.00 56.27  ? 236  THR A CB  1 
ATOM   1819 O OG1 . THR A 1 236 ? 1.179   -27.244 -27.331 1.00 56.92  ? 236  THR A OG1 1 
ATOM   1820 C CG2 . THR A 1 236 ? 0.713   -29.116 -25.876 1.00 43.08  ? 236  THR A CG2 1 
ATOM   1821 N N   . LEU A 1 237 ? 2.966   -28.343 -30.072 1.00 62.18  ? 237  LEU A N   1 
ATOM   1822 C CA  . LEU A 1 237 ? 3.111   -27.968 -31.477 1.00 64.12  ? 237  LEU A CA  1 
ATOM   1823 C C   . LEU A 1 237 ? 4.366   -28.567 -32.067 1.00 74.10  ? 237  LEU A C   1 
ATOM   1824 O O   . LEU A 1 237 ? 4.575   -28.472 -33.275 1.00 73.89  ? 237  LEU A O   1 
ATOM   1825 C CB  . LEU A 1 237 ? 3.126   -26.420 -31.673 1.00 64.04  ? 237  LEU A CB  1 
ATOM   1826 C CG  . LEU A 1 237 ? 1.810   -25.599 -31.558 1.00 66.95  ? 237  LEU A CG  1 
ATOM   1827 C CD1 . LEU A 1 237 ? 1.920   -24.318 -32.316 1.00 66.69  ? 237  LEU A CD1 1 
ATOM   1828 C CD2 . LEU A 1 237 ? 0.587   -26.362 -32.068 1.00 66.41  ? 237  LEU A CD2 1 
ATOM   1829 N N   . VAL A 1 238 ? 5.235   -29.141 -31.215 1.00 75.36  ? 238  VAL A N   1 
ATOM   1830 C CA  . VAL A 1 238 ? 6.527   -29.729 -31.629 1.00 76.25  ? 238  VAL A CA  1 
ATOM   1831 C C   . VAL A 1 238 ? 6.508   -31.255 -31.518 1.00 82.39  ? 238  VAL A C   1 
ATOM   1832 O O   . VAL A 1 238 ? 5.902   -31.808 -30.599 1.00 82.05  ? 238  VAL A O   1 
ATOM   1833 C CB  . VAL A 1 238 ? 7.738   -29.114 -30.878 1.00 80.33  ? 238  VAL A CB  1 
ATOM   1834 C CG1 . VAL A 1 238 ? 9.060   -29.480 -31.563 1.00 80.35  ? 238  VAL A CG1 1 
ATOM   1835 C CG2 . VAL A 1 238 ? 7.610   -27.595 -30.784 1.00 80.30  ? 238  VAL A CG2 1 
ATOM   1836 N N   . THR A 1 239 ? 7.137   -31.927 -32.495 1.00 80.49  ? 239  THR A N   1 
ATOM   1837 C CA  . THR A 1 239 ? 7.222   -33.394 -32.586 1.00 80.11  ? 239  THR A CA  1 
ATOM   1838 C C   . THR A 1 239 ? 8.632   -33.825 -33.043 1.00 81.64  ? 239  THR A C   1 
ATOM   1839 O O   . THR A 1 239 ? 9.161   -33.273 -34.011 1.00 81.82  ? 239  THR A O   1 
ATOM   1840 C CB  . THR A 1 239 ? 6.111   -33.913 -33.546 1.00 90.09  ? 239  THR A CB  1 
ATOM   1841 O OG1 . THR A 1 239 ? 4.826   -33.416 -33.144 1.00 96.85  ? 239  THR A OG1 1 
ATOM   1842 C CG2 . THR A 1 239 ? 6.106   -35.435 -33.700 1.00 83.95  ? 239  THR A CG2 1 
ATOM   1843 N N   . PHE A 1 240 ? 9.230   -34.802 -32.341 1.00 74.74  ? 240  PHE A N   1 
ATOM   1844 C CA  . PHE A 1 240 ? 10.531  -35.354 -32.710 1.00 73.09  ? 240  PHE A CA  1 
ATOM   1845 C C   . PHE A 1 240 ? 10.323  -36.748 -33.360 1.00 79.55  ? 240  PHE A C   1 
ATOM   1846 O O   . PHE A 1 240 ? 9.593   -37.580 -32.826 1.00 78.84  ? 240  PHE A O   1 
ATOM   1847 C CB  . PHE A 1 240 ? 11.478  -35.398 -31.502 1.00 73.59  ? 240  PHE A CB  1 
ATOM   1848 C CG  . PHE A 1 240 ? 11.933  -34.049 -31.010 1.00 73.80  ? 240  PHE A CG  1 
ATOM   1849 C CD1 . PHE A 1 240 ? 11.190  -33.351 -30.065 1.00 75.43  ? 240  PHE A CD1 1 
ATOM   1850 C CD2 . PHE A 1 240 ? 13.115  -33.476 -31.486 1.00 75.93  ? 240  PHE A CD2 1 
ATOM   1851 C CE1 . PHE A 1 240 ? 11.607  -32.097 -29.613 1.00 76.13  ? 240  PHE A CE1 1 
ATOM   1852 C CE2 . PHE A 1 240 ? 13.543  -32.226 -31.020 1.00 78.66  ? 240  PHE A CE2 1 
ATOM   1853 C CZ  . PHE A 1 240 ? 12.777  -31.542 -30.093 1.00 76.30  ? 240  PHE A CZ  1 
ATOM   1854 N N   . LYS A 1 241 ? 10.940  -36.987 -34.504 1.00 78.96  ? 241  LYS A N   1 
ATOM   1855 C CA  . LYS A 1 241 ? 10.828  -38.258 -35.216 1.00 80.09  ? 241  LYS A CA  1 
ATOM   1856 C C   . LYS A 1 241 ? 12.192  -38.980 -35.439 1.00 85.74  ? 241  LYS A C   1 
ATOM   1857 O O   . LYS A 1 241 ? 13.106  -38.432 -36.049 1.00 84.82  ? 241  LYS A O   1 
ATOM   1858 C CB  . LYS A 1 241 ? 10.035  -38.124 -36.553 1.00 82.94  ? 241  LYS A CB  1 
ATOM   1859 C CG  . LYS A 1 241 ? 9.882   -36.732 -37.208 1.00 95.50  ? 241  LYS A CG  1 
ATOM   1860 C CD  . LYS A 1 241 ? 9.214   -36.834 -38.598 1.00 105.50 ? 241  LYS A CD  1 
ATOM   1861 C CE  . LYS A 1 241 ? 10.021  -36.229 -39.758 1.00 107.13 ? 241  LYS A CE  1 
ATOM   1862 N NZ  . LYS A 1 241 ? 9.363   -36.368 -41.085 1.00 105.14 ? 241  LYS A NZ  1 
ATOM   1863 N N   . ASN A 1 242 ? 12.281  -40.224 -34.992 1.00 84.16  ? 242  ASN A N   1 
ATOM   1864 C CA  . ASN A 1 242 ? 13.455  -41.083 -35.201 1.00 84.40  ? 242  ASN A CA  1 
ATOM   1865 C C   . ASN A 1 242 ? 12.958  -42.525 -35.444 1.00 89.95  ? 242  ASN A C   1 
ATOM   1866 O O   . ASN A 1 242 ? 12.980  -43.357 -34.529 1.00 90.10  ? 242  ASN A O   1 
ATOM   1867 C CB  . ASN A 1 242 ? 14.425  -40.994 -34.020 1.00 81.55  ? 242  ASN A CB  1 
ATOM   1868 C CG  . ASN A 1 242 ? 15.736  -41.712 -34.213 1.00 81.52  ? 242  ASN A CG  1 
ATOM   1869 O OD1 . ASN A 1 242 ? 16.067  -42.199 -35.296 1.00 76.53  ? 242  ASN A OD1 1 
ATOM   1870 N ND2 . ASN A 1 242 ? 16.529  -41.751 -33.162 1.00 69.36  ? 242  ASN A ND2 1 
ATOM   1871 N N   . PRO A 1 243 ? 12.462  -42.829 -36.660 1.00 87.49  ? 243  PRO A N   1 
ATOM   1872 C CA  . PRO A 1 243 ? 11.878  -44.156 -36.894 1.00 88.16  ? 243  PRO A CA  1 
ATOM   1873 C C   . PRO A 1 243 ? 12.842  -45.297 -37.208 1.00 94.49  ? 243  PRO A C   1 
ATOM   1874 O O   . PRO A 1 243 ? 12.467  -46.458 -37.027 1.00 94.83  ? 243  PRO A O   1 
ATOM   1875 C CB  . PRO A 1 243 ? 10.919  -43.907 -38.066 1.00 89.87  ? 243  PRO A CB  1 
ATOM   1876 C CG  . PRO A 1 243 ? 11.513  -42.795 -38.817 1.00 93.78  ? 243  PRO A CG  1 
ATOM   1877 C CD  . PRO A 1 243 ? 12.319  -41.962 -37.847 1.00 89.25  ? 243  PRO A CD  1 
ATOM   1878 N N   . HIS A 1 244 ? 14.045  -44.989 -37.712 1.00 92.23  ? 244  HIS A N   1 
ATOM   1879 C CA  . HIS A 1 244 ? 14.973  -46.036 -38.121 1.00 92.72  ? 244  HIS A CA  1 
ATOM   1880 C C   . HIS A 1 244 ? 16.326  -45.992 -37.409 1.00 93.39  ? 244  HIS A C   1 
ATOM   1881 O O   . HIS A 1 244 ? 17.261  -46.697 -37.818 1.00 93.39  ? 244  HIS A O   1 
ATOM   1882 C CB  . HIS A 1 244 ? 15.140  -46.001 -39.656 1.00 94.77  ? 244  HIS A CB  1 
ATOM   1883 C CG  . HIS A 1 244 ? 13.840  -46.018 -40.417 1.00 99.13  ? 244  HIS A CG  1 
ATOM   1884 N ND1 . HIS A 1 244 ? 12.913  -47.049 -40.258 1.00 101.35 ? 244  HIS A ND1 1 
ATOM   1885 C CD2 . HIS A 1 244 ? 13.363  -45.142 -41.334 1.00 101.45 ? 244  HIS A CD2 1 
ATOM   1886 C CE1 . HIS A 1 244 ? 11.910  -46.760 -41.074 1.00 101.02 ? 244  HIS A CE1 1 
ATOM   1887 N NE2 . HIS A 1 244 ? 12.132  -45.625 -41.745 1.00 101.36 ? 244  HIS A NE2 1 
ATOM   1888 N N   . ALA A 1 245 ? 16.422  -45.190 -36.325 1.00 86.94  ? 245  ALA A N   1 
ATOM   1889 C CA  . ALA A 1 245 ? 17.655  -44.971 -35.547 1.00 85.36  ? 245  ALA A CA  1 
ATOM   1890 C C   . ALA A 1 245 ? 18.808  -44.454 -36.440 1.00 84.77  ? 245  ALA A C   1 
ATOM   1891 O O   . ALA A 1 245 ? 19.975  -44.712 -36.161 1.00 83.31  ? 245  ALA A O   1 
ATOM   1892 C CB  . ALA A 1 245 ? 18.059  -46.230 -34.781 1.00 86.22  ? 245  ALA A CB  1 
ATOM   1893 N N   . LYS A 1 246 ? 18.460  -43.709 -37.511 1.00 79.23  ? 246  LYS A N   1 
ATOM   1894 C CA  . LYS A 1 246 ? 19.414  -43.139 -38.463 1.00 78.18  ? 246  LYS A CA  1 
ATOM   1895 C C   . LYS A 1 246 ? 19.583  -41.629 -38.215 1.00 82.79  ? 246  LYS A C   1 
ATOM   1896 O O   . LYS A 1 246 ? 20.682  -41.079 -38.392 1.00 82.98  ? 246  LYS A O   1 
ATOM   1897 C CB  . LYS A 1 246 ? 18.974  -43.405 -39.917 1.00 79.86  ? 246  LYS A CB  1 
ATOM   1898 C CG  . LYS A 1 246 ? 18.741  -44.873 -40.268 1.00 94.40  ? 246  LYS A CG  1 
ATOM   1899 C CD  . LYS A 1 246 ? 18.337  -45.078 -41.736 1.00 109.45 ? 246  LYS A CD  1 
ATOM   1900 C CE  . LYS A 1 246 ? 18.178  -46.549 -42.092 1.00 123.96 ? 246  LYS A CE  1 
ATOM   1901 N NZ  . LYS A 1 246 ? 17.967  -46.774 -43.555 1.00 128.32 ? 246  LYS A NZ  1 
ATOM   1902 N N   . LYS A 1 247 ? 18.481  -40.959 -37.806 1.00 79.20  ? 247  LYS A N   1 
ATOM   1903 C CA  . LYS A 1 247 ? 18.447  -39.518 -37.537 1.00 78.97  ? 247  LYS A CA  1 
ATOM   1904 C C   . LYS A 1 247 ? 17.190  -39.115 -36.743 1.00 81.67  ? 247  LYS A C   1 
ATOM   1905 O O   . LYS A 1 247 ? 16.147  -39.788 -36.830 1.00 81.25  ? 247  LYS A O   1 
ATOM   1906 C CB  . LYS A 1 247 ? 18.517  -38.721 -38.860 1.00 81.66  ? 247  LYS A CB  1 
ATOM   1907 C CG  . LYS A 1 247 ? 19.102  -37.323 -38.718 1.00 102.82 ? 247  LYS A CG  1 
ATOM   1908 C CD  . LYS A 1 247 ? 18.404  -36.346 -39.668 1.00 114.38 ? 247  LYS A CD  1 
ATOM   1909 C CE  . LYS A 1 247 ? 18.525  -34.895 -39.244 1.00 113.12 ? 247  LYS A CE  1 
ATOM   1910 N NZ  . LYS A 1 247 ? 17.609  -34.020 -40.028 1.00 114.95 ? 247  LYS A NZ  1 
ATOM   1911 N N   . GLN A 1 248 ? 17.302  -37.983 -36.006 1.00 77.03  ? 248  GLN A N   1 
ATOM   1912 C CA  . GLN A 1 248 ? 16.209  -37.357 -35.241 1.00 76.14  ? 248  GLN A CA  1 
ATOM   1913 C C   . GLN A 1 248 ? 15.697  -36.047 -35.947 1.00 82.32  ? 248  GLN A C   1 
ATOM   1914 O O   . GLN A 1 248 ? 16.452  -35.068 -36.067 1.00 82.64  ? 248  GLN A O   1 
ATOM   1915 C CB  . GLN A 1 248 ? 16.632  -37.116 -33.787 1.00 75.61  ? 248  GLN A CB  1 
ATOM   1916 C CG  . GLN A 1 248 ? 15.650  -36.287 -33.021 1.00 41.49  ? 248  GLN A CG  1 
ATOM   1917 C CD  . GLN A 1 248 ? 15.551  -36.729 -31.598 1.00 65.37  ? 248  GLN A CD  1 
ATOM   1918 O OE1 . GLN A 1 248 ? 14.708  -37.598 -31.248 1.00 61.33  ? 248  GLN A OE1 1 
ATOM   1919 N NE2 . GLN A 1 248 ? 16.395  -36.116 -30.745 1.00 52.23  ? 248  GLN A NE2 1 
ATOM   1920 N N   . ASP A 1 249 ? 14.418  -36.057 -36.416 1.00 78.91  ? 249  ASP A N   1 
ATOM   1921 C CA  . ASP A 1 249 ? 13.779  -34.960 -37.137 1.00 78.65  ? 249  ASP A CA  1 
ATOM   1922 C C   . ASP A 1 249 ? 12.807  -34.186 -36.283 1.00 79.60  ? 249  ASP A C   1 
ATOM   1923 O O   . ASP A 1 249 ? 11.999  -34.776 -35.584 1.00 78.31  ? 249  ASP A O   1 
ATOM   1924 C CB  . ASP A 1 249 ? 13.120  -35.464 -38.430 1.00 81.50  ? 249  ASP A CB  1 
ATOM   1925 C CG  . ASP A 1 249 ? 14.126  -35.700 -39.545 1.00 105.56 ? 249  ASP A CG  1 
ATOM   1926 O OD1 . ASP A 1 249 ? 15.070  -36.490 -39.335 1.00 108.85 ? 249  ASP A OD1 1 
ATOM   1927 O OD2 . ASP A 1 249 ? 13.998  -35.059 -40.610 1.00 116.81 ? 249  ASP A OD2 1 
ATOM   1928 N N   . VAL A 1 250 ? 12.887  -32.859 -36.334 1.00 75.71  ? 250  VAL A N   1 
ATOM   1929 C CA  . VAL A 1 250 ? 12.014  -31.996 -35.545 1.00 75.71  ? 250  VAL A CA  1 
ATOM   1930 C C   . VAL A 1 250 ? 10.934  -31.327 -36.440 1.00 78.94  ? 250  VAL A C   1 
ATOM   1931 O O   . VAL A 1 250 ? 11.253  -30.614 -37.401 1.00 78.85  ? 250  VAL A O   1 
ATOM   1932 C CB  . VAL A 1 250 ? 12.840  -31.018 -34.670 1.00 80.09  ? 250  VAL A CB  1 
ATOM   1933 C CG1 . VAL A 1 250 ? 13.622  -29.998 -35.501 1.00 80.21  ? 250  VAL A CG1 1 
ATOM   1934 C CG2 . VAL A 1 250 ? 11.968  -30.346 -33.614 1.00 79.81  ? 250  VAL A CG2 1 
ATOM   1935 N N   . VAL A 1 251 ? 9.649   -31.593 -36.121 1.00 75.12  ? 251  VAL A N   1 
ATOM   1936 C CA  . VAL A 1 251 ? 8.513   -31.108 -36.912 1.00 75.39  ? 251  VAL A CA  1 
ATOM   1937 C C   . VAL A 1 251 ? 7.442   -30.234 -36.152 1.00 77.51  ? 251  VAL A C   1 
ATOM   1938 O O   . VAL A 1 251 ? 6.921   -30.613 -35.091 1.00 75.05  ? 251  VAL A O   1 
ATOM   1939 C CB  . VAL A 1 251 ? 7.825   -32.290 -37.650 1.00 79.86  ? 251  VAL A CB  1 
ATOM   1940 C CG1 . VAL A 1 251 ? 8.692   -32.842 -38.768 1.00 79.72  ? 251  VAL A CG1 1 
ATOM   1941 C CG2 . VAL A 1 251 ? 7.387   -33.397 -36.687 1.00 79.43  ? 251  VAL A CG2 1 
ATOM   1942 N N   . VAL A 1 252 ? 7.108   -29.069 -36.781 1.00 74.40  ? 252  VAL A N   1 
ATOM   1943 C CA  . VAL A 1 252 ? 6.078   -28.100 -36.360 1.00 74.37  ? 252  VAL A CA  1 
ATOM   1944 C C   . VAL A 1 252 ? 4.708   -28.714 -36.692 1.00 75.78  ? 252  VAL A C   1 
ATOM   1945 O O   . VAL A 1 252 ? 4.578   -29.425 -37.683 1.00 74.52  ? 252  VAL A O   1 
ATOM   1946 C CB  . VAL A 1 252 ? 6.217   -26.706 -37.036 1.00 79.40  ? 252  VAL A CB  1 
ATOM   1947 C CG1 . VAL A 1 252 ? 5.598   -25.614 -36.172 1.00 79.69  ? 252  VAL A CG1 1 
ATOM   1948 C CG2 . VAL A 1 252 ? 7.668   -26.367 -37.378 1.00 79.26  ? 252  VAL A CG2 1 
ATOM   1949 N N   . LEU A 1 253 ? 3.695   -28.453 -35.881 1.00 72.20  ? 253  LEU A N   1 
ATOM   1950 C CA  . LEU A 1 253 ? 2.408   -29.103 -36.074 1.00 72.74  ? 253  LEU A CA  1 
ATOM   1951 C C   . LEU A 1 253 ? 1.382   -28.348 -36.936 1.00 76.74  ? 253  LEU A C   1 
ATOM   1952 O O   . LEU A 1 253 ? 0.269   -28.851 -37.111 1.00 78.76  ? 253  LEU A O   1 
ATOM   1953 C CB  . LEU A 1 253 ? 1.791   -29.475 -34.725 1.00 73.60  ? 253  LEU A CB  1 
ATOM   1954 C CG  . LEU A 1 253 ? 1.505   -30.962 -34.507 1.00 80.19  ? 253  LEU A CG  1 
ATOM   1955 C CD1 . LEU A 1 253 ? 1.761   -31.354 -33.051 1.00 82.03  ? 253  LEU A CD1 1 
ATOM   1956 C CD2 . LEU A 1 253 ? 0.066   -31.328 -34.931 1.00 82.51  ? 253  LEU A CD2 1 
ATOM   1957 N N   . GLY A 1 254 ? 1.743   -27.200 -37.497 1.00 69.98  ? 254  GLY A N   1 
ATOM   1958 C CA  . GLY A 1 254 ? 0.841   -26.486 -38.398 1.00 67.83  ? 254  GLY A CA  1 
ATOM   1959 C C   . GLY A 1 254 ? -0.196  -25.619 -37.718 1.00 65.74  ? 254  GLY A C   1 
ATOM   1960 O O   . GLY A 1 254 ? -0.767  -26.007 -36.687 1.00 64.19  ? 254  GLY A O   1 
ATOM   1961 N N   . SER A 1 255 ? -0.475  -24.449 -38.348 1.00 57.20  ? 255  SER A N   1 
ATOM   1962 C CA  . SER A 1 255 ? -1.377  -23.436 -37.842 1.00 54.48  ? 255  SER A CA  1 
ATOM   1963 C C   . SER A 1 255 ? -2.686  -23.971 -37.365 1.00 57.54  ? 255  SER A C   1 
ATOM   1964 O O   . SER A 1 255 ? -3.316  -24.775 -38.032 1.00 57.66  ? 255  SER A O   1 
ATOM   1965 C CB  . SER A 1 255 ? -1.597  -22.319 -38.842 1.00 56.26  ? 255  SER A CB  1 
ATOM   1966 O OG  . SER A 1 255 ? -2.239  -21.233 -38.188 1.00 63.83  ? 255  SER A OG  1 
ATOM   1967 N N   . GLN A 1 256 ? -3.074  -23.523 -36.175 1.00 53.68  ? 256  GLN A N   1 
ATOM   1968 C CA  . GLN A 1 256 ? -4.293  -23.887 -35.456 1.00 51.89  ? 256  GLN A CA  1 
ATOM   1969 C C   . GLN A 1 256 ? -5.360  -22.773 -35.556 1.00 53.98  ? 256  GLN A C   1 
ATOM   1970 O O   . GLN A 1 256 ? -6.366  -22.814 -34.841 1.00 53.55  ? 256  GLN A O   1 
ATOM   1971 C CB  . GLN A 1 256 ? -3.923  -24.200 -33.981 1.00 51.84  ? 256  GLN A CB  1 
ATOM   1972 C CG  . GLN A 1 256 ? -3.066  -25.451 -33.817 1.00 60.35  ? 256  GLN A CG  1 
ATOM   1973 C CD  . GLN A 1 256 ? -3.689  -26.714 -34.403 1.00 80.54  ? 256  GLN A CD  1 
ATOM   1974 O OE1 . GLN A 1 256 ? -3.079  -27.375 -35.269 1.00 72.79  ? 256  GLN A OE1 1 
ATOM   1975 N NE2 . GLN A 1 256 ? -4.905  -27.085 -33.946 1.00 66.27  ? 256  GLN A NE2 1 
ATOM   1976 N N   . GLU A 1 257 ? -5.130  -21.778 -36.439 1.00 48.81  ? 257  GLU A N   1 
ATOM   1977 C CA  . GLU A 1 257 ? -6.018  -20.622 -36.587 1.00 48.85  ? 257  GLU A CA  1 
ATOM   1978 C C   . GLU A 1 257 ? -7.434  -21.004 -36.996 1.00 55.88  ? 257  GLU A C   1 
ATOM   1979 O O   . GLU A 1 257 ? -8.379  -20.691 -36.254 1.00 55.86  ? 257  GLU A O   1 
ATOM   1980 C CB  . GLU A 1 257 ? -5.415  -19.583 -37.529 1.00 49.52  ? 257  GLU A CB  1 
ATOM   1981 C CG  . GLU A 1 257 ? -6.173  -18.273 -37.569 1.00 51.10  ? 257  GLU A CG  1 
ATOM   1982 C CD  . GLU A 1 257 ? -5.570  -17.249 -38.510 1.00 78.56  ? 257  GLU A CD  1 
ATOM   1983 O OE1 . GLU A 1 257 ? -5.000  -17.658 -39.551 1.00 72.20  ? 257  GLU A OE1 1 
ATOM   1984 O OE2 . GLU A 1 257 ? -5.697  -16.033 -38.221 1.00 75.04  ? 257  GLU A OE2 1 
ATOM   1985 N N   . GLY A 1 258 ? -7.549  -21.692 -38.142 1.00 52.79  ? 258  GLY A N   1 
ATOM   1986 C CA  . GLY A 1 258 ? -8.818  -22.151 -38.691 1.00 52.82  ? 258  GLY A CA  1 
ATOM   1987 C C   . GLY A 1 258 ? -9.441  -23.224 -37.827 1.00 58.56  ? 258  GLY A C   1 
ATOM   1988 O O   . GLY A 1 258 ? -10.664 -23.280 -37.683 1.00 59.19  ? 258  GLY A O   1 
ATOM   1989 N N   . ALA A 1 259 ? -8.581  -24.064 -37.225 1.00 55.05  ? 259  ALA A N   1 
ATOM   1990 C CA  . ALA A 1 259 ? -8.953  -25.131 -36.315 1.00 54.81  ? 259  ALA A CA  1 
ATOM   1991 C C   . ALA A 1 259 ? -9.742  -24.512 -35.162 1.00 60.79  ? 259  ALA A C   1 
ATOM   1992 O O   . ALA A 1 259 ? -10.857 -24.969 -34.868 1.00 60.39  ? 259  ALA A O   1 
ATOM   1993 C CB  . ALA A 1 259 ? -7.687  -25.810 -35.797 1.00 55.52  ? 259  ALA A CB  1 
ATOM   1994 N N   . MET A 1 260 ? -9.169  -23.427 -34.559 1.00 59.33  ? 260  MET A N   1 
ATOM   1995 C CA  . MET A 1 260 ? -9.750  -22.637 -33.477 1.00 60.08  ? 260  MET A CA  1 
ATOM   1996 C C   . MET A 1 260 ? -11.083 -22.057 -33.885 1.00 63.86  ? 260  MET A C   1 
ATOM   1997 O O   . MET A 1 260 ? -12.026 -22.255 -33.137 1.00 62.89  ? 260  MET A O   1 
ATOM   1998 C CB  . MET A 1 260 ? -8.802  -21.525 -33.024 1.00 63.28  ? 260  MET A CB  1 
ATOM   1999 C CG  . MET A 1 260 ? -7.872  -21.930 -31.880 1.00 68.53  ? 260  MET A CG  1 
ATOM   2000 S SD  . MET A 1 260 ? -8.672  -22.694 -30.417 1.00 74.52  ? 260  MET A SD  1 
ATOM   2001 C CE  . MET A 1 260 ? -9.517  -21.306 -29.725 1.00 71.50  ? 260  MET A CE  1 
ATOM   2002 N N   . HIS A 1 261 ? -11.189 -21.395 -35.089 1.00 61.73  ? 261  HIS A N   1 
ATOM   2003 C CA  . HIS A 1 261 ? -12.448 -20.807 -35.596 1.00 61.79  ? 261  HIS A CA  1 
ATOM   2004 C C   . HIS A 1 261 ? -13.572 -21.848 -35.634 1.00 67.26  ? 261  HIS A C   1 
ATOM   2005 O O   . HIS A 1 261 ? -14.686 -21.558 -35.205 1.00 66.04  ? 261  HIS A O   1 
ATOM   2006 C CB  . HIS A 1 261 ? -12.294 -20.163 -36.984 1.00 62.29  ? 261  HIS A CB  1 
ATOM   2007 C CG  . HIS A 1 261 ? -11.343 -19.006 -37.068 1.00 65.87  ? 261  HIS A CG  1 
ATOM   2008 N ND1 . HIS A 1 261 ? -10.726 -18.671 -38.264 1.00 67.72  ? 261  HIS A ND1 1 
ATOM   2009 C CD2 . HIS A 1 261 ? -10.932 -18.134 -36.119 1.00 67.95  ? 261  HIS A CD2 1 
ATOM   2010 C CE1 . HIS A 1 261 ? -9.955  -17.628 -38.006 1.00 66.92  ? 261  HIS A CE1 1 
ATOM   2011 N NE2 . HIS A 1 261 ? -10.045 -17.263 -36.729 1.00 67.46  ? 261  HIS A NE2 1 
ATOM   2012 N N   . THR A 1 262 ? -13.263 -23.065 -36.096 1.00 66.53  ? 262  THR A N   1 
ATOM   2013 C CA  . THR A 1 262 ? -14.211 -24.182 -36.161 1.00 68.07  ? 262  THR A CA  1 
ATOM   2014 C C   . THR A 1 262 ? -14.646 -24.605 -34.763 1.00 78.42  ? 262  THR A C   1 
ATOM   2015 O O   . THR A 1 262 ? -15.824 -24.881 -34.555 1.00 78.60  ? 262  THR A O   1 
ATOM   2016 C CB  . THR A 1 262 ? -13.602 -25.338 -36.934 1.00 69.60  ? 262  THR A CB  1 
ATOM   2017 O OG1 . THR A 1 262 ? -13.243 -24.876 -38.241 1.00 68.60  ? 262  THR A OG1 1 
ATOM   2018 C CG2 . THR A 1 262 ? -14.526 -26.542 -37.025 1.00 64.24  ? 262  THR A CG2 1 
ATOM   2019 N N   . ALA A 1 263 ? -13.701 -24.652 -33.808 1.00 79.38  ? 263  ALA A N   1 
ATOM   2020 C CA  . ALA A 1 263 ? -13.974 -25.008 -32.404 1.00 80.40  ? 263  ALA A CA  1 
ATOM   2021 C C   . ALA A 1 263 ? -14.868 -23.964 -31.737 1.00 86.14  ? 263  ALA A C   1 
ATOM   2022 O O   . ALA A 1 263 ? -15.669 -24.299 -30.871 1.00 85.59  ? 263  ALA A O   1 
ATOM   2023 C CB  . ALA A 1 263 ? -12.672 -25.122 -31.632 1.00 80.99  ? 263  ALA A CB  1 
ATOM   2024 N N   . LEU A 1 264 ? -14.738 -22.706 -32.173 1.00 84.19  ? 264  LEU A N   1 
ATOM   2025 C CA  . LEU A 1 264 ? -15.450 -21.549 -31.658 1.00 84.31  ? 264  LEU A CA  1 
ATOM   2026 C C   . LEU A 1 264 ? -16.783 -21.327 -32.381 1.00 93.65  ? 264  LEU A C   1 
ATOM   2027 O O   . LEU A 1 264 ? -17.347 -20.232 -32.255 1.00 93.82  ? 264  LEU A O   1 
ATOM   2028 C CB  . LEU A 1 264 ? -14.558 -20.296 -31.829 1.00 83.26  ? 264  LEU A CB  1 
ATOM   2029 C CG  . LEU A 1 264 ? -13.272 -20.205 -31.010 1.00 85.84  ? 264  LEU A CG  1 
ATOM   2030 C CD1 . LEU A 1 264 ? -12.313 -19.214 -31.624 1.00 84.73  ? 264  LEU A CD1 1 
ATOM   2031 C CD2 . LEU A 1 264 ? -13.557 -19.877 -29.564 1.00 86.57  ? 264  LEU A CD2 1 
ATOM   2032 N N   . THR A 1 265 ? -17.299 -22.340 -33.131 1.00 93.06  ? 265  THR A N   1 
ATOM   2033 C CA  . THR A 1 265 ? -18.564 -22.182 -33.864 1.00 94.00  ? 265  THR A CA  1 
ATOM   2034 C C   . THR A 1 265 ? -19.745 -21.985 -32.917 1.00 101.72 ? 265  THR A C   1 
ATOM   2035 O O   . THR A 1 265 ? -20.409 -20.950 -33.015 1.00 101.83 ? 265  THR A O   1 
ATOM   2036 C CB  . THR A 1 265 ? -18.770 -23.294 -34.887 1.00 97.38  ? 265  THR A CB  1 
ATOM   2037 O OG1 . THR A 1 265 ? -17.903 -23.008 -35.969 1.00 97.22  ? 265  THR A OG1 1 
ATOM   2038 C CG2 . THR A 1 265 ? -20.185 -23.373 -35.412 1.00 94.11  ? 265  THR A CG2 1 
ATOM   2039 N N   . GLY A 1 266 ? -19.961 -22.914 -31.984 1.00 100.38 ? 266  GLY A N   1 
ATOM   2040 C CA  . GLY A 1 266 ? -21.062 -22.800 -31.025 1.00 101.53 ? 266  GLY A CA  1 
ATOM   2041 C C   . GLY A 1 266 ? -21.032 -21.590 -30.095 1.00 108.38 ? 266  GLY A C   1 
ATOM   2042 O O   . GLY A 1 266 ? -22.070 -21.187 -29.565 1.00 107.52 ? 266  GLY A O   1 
ATOM   2043 N N   . ALA A 1 267 ? -19.841 -20.995 -29.904 1.00 107.28 ? 267  ALA A N   1 
ATOM   2044 C CA  . ALA A 1 267 ? -19.559 -19.879 -29.004 1.00 107.80 ? 267  ALA A CA  1 
ATOM   2045 C C   . ALA A 1 267 ? -20.168 -18.530 -29.377 1.00 112.03 ? 267  ALA A C   1 
ATOM   2046 O O   . ALA A 1 267 ? -20.453 -18.254 -30.547 1.00 109.88 ? 267  ALA A O   1 
ATOM   2047 C CB  . ALA A 1 267 ? -18.060 -19.727 -28.839 1.00 108.76 ? 267  ALA A CB  1 
ATOM   2048 N N   . THR A 1 268 ? -20.289 -17.671 -28.345 1.00 110.97 ? 268  THR A N   1 
ATOM   2049 C CA  . THR A 1 268 ? -20.831 -16.321 -28.410 1.00 111.60 ? 268  THR A CA  1 
ATOM   2050 C C   . THR A 1 268 ? -19.853 -15.387 -29.097 1.00 116.00 ? 268  THR A C   1 
ATOM   2051 O O   . THR A 1 268 ? -18.929 -14.884 -28.459 1.00 115.27 ? 268  THR A O   1 
ATOM   2052 C CB  . THR A 1 268 ? -21.205 -15.831 -27.003 1.00 121.68 ? 268  THR A CB  1 
ATOM   2053 O OG1 . THR A 1 268 ? -22.048 -16.797 -26.373 1.00 122.68 ? 268  THR A OG1 1 
ATOM   2054 C CG2 . THR A 1 268 ? -21.877 -14.466 -27.017 1.00 119.25 ? 268  THR A CG2 1 
ATOM   2055 N N   . GLU A 1 269 ? -20.067 -15.145 -30.394 1.00 113.49 ? 269  GLU A N   1 
ATOM   2056 C CA  . GLU A 1 269 ? -19.214 -14.230 -31.141 1.00 113.88 ? 269  GLU A CA  1 
ATOM   2057 C C   . GLU A 1 269 ? -19.574 -12.779 -30.772 1.00 117.64 ? 269  GLU A C   1 
ATOM   2058 O O   . GLU A 1 269 ? -20.753 -12.478 -30.531 1.00 117.19 ? 269  GLU A O   1 
ATOM   2059 C CB  . GLU A 1 269 ? -19.336 -14.479 -32.655 1.00 115.43 ? 269  GLU A CB  1 
ATOM   2060 C CG  . GLU A 1 269 ? -18.173 -13.915 -33.465 1.00 127.91 ? 269  GLU A CG  1 
ATOM   2061 C CD  . GLU A 1 269 ? -18.187 -14.114 -34.973 1.00 155.83 ? 269  GLU A CD  1 
ATOM   2062 O OE1 . GLU A 1 269 ? -19.203 -14.608 -35.520 1.00 148.71 ? 269  GLU A OE1 1 
ATOM   2063 O OE2 . GLU A 1 269 ? -17.177 -13.742 -35.614 1.00 153.52 ? 269  GLU A OE2 1 
ATOM   2064 N N   . ILE A 1 270 ? -18.543 -11.909 -30.682 1.00 113.64 ? 270  ILE A N   1 
ATOM   2065 C CA  . ILE A 1 270 ? -18.679 -10.474 -30.396 1.00 113.45 ? 270  ILE A CA  1 
ATOM   2066 C C   . ILE A 1 270 ? -17.807 -9.655  -31.326 1.00 118.39 ? 270  ILE A C   1 
ATOM   2067 O O   . ILE A 1 270 ? -16.665 -10.028 -31.594 1.00 117.68 ? 270  ILE A O   1 
ATOM   2068 C CB  . ILE A 1 270 ? -18.492 -10.046 -28.907 1.00 116.27 ? 270  ILE A CB  1 
ATOM   2069 C CG1 . ILE A 1 270 ? -17.169 -10.526 -28.309 1.00 116.52 ? 270  ILE A CG1 1 
ATOM   2070 C CG2 . ILE A 1 270 ? -19.661 -10.447 -28.034 1.00 117.36 ? 270  ILE A CG2 1 
ATOM   2071 C CD1 . ILE A 1 270 ? -16.113 -9.515  -28.347 1.00 122.51 ? 270  ILE A CD1 1 
ATOM   2072 N N   . GLN A 1 271 ? -18.340 -8.532  -31.810 1.00 116.45 ? 271  GLN A N   1 
ATOM   2073 C CA  . GLN A 1 271 ? -17.586 -7.637  -32.678 1.00 116.99 ? 271  GLN A CA  1 
ATOM   2074 C C   . GLN A 1 271 ? -16.685 -6.822  -31.757 1.00 121.64 ? 271  GLN A C   1 
ATOM   2075 O O   . GLN A 1 271 ? -17.158 -6.322  -30.737 1.00 121.21 ? 271  GLN A O   1 
ATOM   2076 C CB  . GLN A 1 271 ? -18.535 -6.741  -33.507 1.00 118.44 ? 271  GLN A CB  1 
ATOM   2077 C CG  . GLN A 1 271 ? -17.878 -6.076  -34.720 1.00 136.31 ? 271  GLN A CG  1 
ATOM   2078 C CD  . GLN A 1 271 ? -17.710 -7.007  -35.906 1.00 157.02 ? 271  GLN A CD  1 
ATOM   2079 O OE1 . GLN A 1 271 ? -16.890 -7.943  -35.897 1.00 150.23 ? 271  GLN A OE1 1 
ATOM   2080 N NE2 . GLN A 1 271 ? -18.451 -6.733  -36.977 1.00 150.47 ? 271  GLN A NE2 1 
ATOM   2081 N N   . MET A 1 272 ? -15.387 -6.751  -32.061 1.00 118.55 ? 272  MET A N   1 
ATOM   2082 C CA  . MET A 1 272 ? -14.481 -6.024  -31.187 1.00 118.45 ? 272  MET A CA  1 
ATOM   2083 C C   . MET A 1 272 ? -13.620 -5.020  -31.893 1.00 121.49 ? 272  MET A C   1 
ATOM   2084 O O   . MET A 1 272 ? -13.208 -5.249  -33.031 1.00 121.63 ? 272  MET A O   1 
ATOM   2085 C CB  . MET A 1 272 ? -13.619 -6.985  -30.369 1.00 121.10 ? 272  MET A CB  1 
ATOM   2086 C CG  . MET A 1 272 ? -13.904 -6.895  -28.900 1.00 125.22 ? 272  MET A CG  1 
ATOM   2087 S SD  . MET A 1 272 ? -12.626 -7.637  -27.871 1.00 129.81 ? 272  MET A SD  1 
ATOM   2088 C CE  . MET A 1 272 ? -11.670 -6.192  -27.477 1.00 126.45 ? 272  MET A CE  1 
ATOM   2089 N N   . SER A 1 273 ? -13.332 -3.908  -31.200 1.00 117.22 ? 273  SER A N   1 
ATOM   2090 C CA  . SER A 1 273 ? -12.477 -2.828  -31.679 1.00 117.16 ? 273  SER A CA  1 
ATOM   2091 C C   . SER A 1 273 ? -11.955 -2.014  -30.500 1.00 121.17 ? 273  SER A C   1 
ATOM   2092 O O   . SER A 1 273 ? -12.746 -1.422  -29.759 1.00 120.68 ? 273  SER A O   1 
ATOM   2093 C CB  . SER A 1 273 ? -13.210 -1.941  -32.685 1.00 120.96 ? 273  SER A CB  1 
ATOM   2094 O OG  . SER A 1 273 ? -14.410 -1.416  -32.141 1.00 130.93 ? 273  SER A OG  1 
ATOM   2095 N N   . SER A 1 274 ? -10.618 -2.018  -30.320 1.00 118.17 ? 274  SER A N   1 
ATOM   2096 C CA  . SER A 1 274 ? -9.855  -1.305  -29.281 1.00 118.43 ? 274  SER A CA  1 
ATOM   2097 C C   . SER A 1 274 ? -10.491 -1.359  -27.836 1.00 121.98 ? 274  SER A C   1 
ATOM   2098 O O   . SER A 1 274 ? -10.682 -0.319  -27.183 1.00 122.01 ? 274  SER A O   1 
ATOM   2099 C CB  . SER A 1 274 ? -9.574  0.131   -29.720 1.00 122.05 ? 274  SER A CB  1 
ATOM   2100 O OG  . SER A 1 274 ? -10.778 0.854   -29.918 1.00 130.01 ? 274  SER A OG  1 
ATOM   2101 N N   . GLY A 1 275 ? -10.795 -2.579  -27.374 1.00 116.49 ? 275  GLY A N   1 
ATOM   2102 C CA  . GLY A 1 275 ? -11.356 -2.843  -26.047 1.00 115.00 ? 275  GLY A CA  1 
ATOM   2103 C C   . GLY A 1 275 ? -12.870 -2.867  -25.945 1.00 115.10 ? 275  GLY A C   1 
ATOM   2104 O O   . GLY A 1 275 ? -13.420 -3.407  -24.972 1.00 114.77 ? 275  GLY A O   1 
ATOM   2105 N N   . ASN A 1 276 ? -13.549 -2.275  -26.948 1.00 108.07 ? 276  ASN A N   1 
ATOM   2106 C CA  . ASN A 1 276 ? -15.002 -2.131  -27.002 1.00 106.05 ? 276  ASN A CA  1 
ATOM   2107 C C   . ASN A 1 276 ? -15.674 -3.236  -27.759 1.00 104.95 ? 276  ASN A C   1 
ATOM   2108 O O   . ASN A 1 276 ? -15.386 -3.433  -28.943 1.00 104.21 ? 276  ASN A O   1 
ATOM   2109 C CB  . ASN A 1 276 ? -15.378 -0.785  -27.589 1.00 108.14 ? 276  ASN A CB  1 
ATOM   2110 C CG  . ASN A 1 276 ? -14.963 0.351   -26.705 1.00 138.34 ? 276  ASN A CG  1 
ATOM   2111 O OD1 . ASN A 1 276 ? -15.677 0.723   -25.768 1.00 136.36 ? 276  ASN A OD1 1 
ATOM   2112 N ND2 . ASN A 1 276 ? -13.783 0.905   -26.965 1.00 129.94 ? 276  ASN A ND2 1 
ATOM   2113 N N   . LEU A 1 277 ? -16.591 -3.951  -27.072 1.00 98.28  ? 277  LEU A N   1 
ATOM   2114 C CA  . LEU A 1 277 ? -17.340 -5.077  -27.636 1.00 95.96  ? 277  LEU A CA  1 
ATOM   2115 C C   . LEU A 1 277 ? -18.744 -4.668  -28.090 1.00 96.51  ? 277  LEU A C   1 
ATOM   2116 O O   . LEU A 1 277 ? -19.683 -4.599  -27.297 1.00 96.27  ? 277  LEU A O   1 
ATOM   2117 C CB  . LEU A 1 277 ? -17.360 -6.352  -26.734 1.00 95.17  ? 277  LEU A CB  1 
ATOM   2118 C CG  . LEU A 1 277 ? -17.977 -6.292  -25.342 1.00 98.29  ? 277  LEU A CG  1 
ATOM   2119 C CD1 . LEU A 1 277 ? -18.678 -7.588  -25.012 1.00 97.30  ? 277  LEU A CD1 1 
ATOM   2120 C CD2 . LEU A 1 277 ? -16.931 -5.944  -24.288 1.00 101.09 ? 277  LEU A CD2 1 
ATOM   2121 N N   . LEU A 1 278 ? -18.875 -4.416  -29.395 1.00 89.83  ? 278  LEU A N   1 
ATOM   2122 C CA  . LEU A 1 278 ? -20.143 -4.068  -30.011 1.00 88.19  ? 278  LEU A CA  1 
ATOM   2123 C C   . LEU A 1 278 ? -20.967 -5.389  -30.197 1.00 91.36  ? 278  LEU A C   1 
ATOM   2124 O O   . LEU A 1 278 ? -21.297 -5.781  -31.321 1.00 90.83  ? 278  LEU A O   1 
ATOM   2125 C CB  . LEU A 1 278 ? -19.920 -3.251  -31.322 1.00 87.66  ? 278  LEU A CB  1 
ATOM   2126 C CG  . LEU A 1 278 ? -19.165 -1.866  -31.264 1.00 91.32  ? 278  LEU A CG  1 
ATOM   2127 C CD1 . LEU A 1 278 ? -19.515 -1.034  -30.036 1.00 92.95  ? 278  LEU A CD1 1 
ATOM   2128 C CD2 . LEU A 1 278 ? -17.674 -2.009  -31.393 1.00 91.11  ? 278  LEU A CD2 1 
ATOM   2129 N N   . PHE A 1 279 ? -21.244 -6.071  -29.037 1.00 87.20  ? 279  PHE A N   1 
ATOM   2130 C CA  . PHE A 1 279 ? -21.972 -7.312  -28.757 1.00 115.39 ? 279  PHE A CA  1 
ATOM   2131 C C   . PHE A 1 279 ? -22.726 -7.903  -29.930 1.00 136.25 ? 279  PHE A C   1 
ATOM   2132 O O   . PHE A 1 279 ? -22.144 -8.654  -30.706 1.00 100.77 ? 279  PHE A O   1 
ATOM   2133 C CB  . PHE A 1 279 ? -22.925 -7.065  -27.583 1.00 117.79 ? 279  PHE A CB  1 
ATOM   2134 C CG  . PHE A 1 279 ? -23.613 -8.253  -26.940 1.00 120.70 ? 279  PHE A CG  1 
ATOM   2135 C CD1 . PHE A 1 279 ? -22.892 -9.394  -26.589 1.00 124.98 ? 279  PHE A CD1 1 
ATOM   2136 C CD2 . PHE A 1 279 ? -24.952 -8.181  -26.565 1.00 123.83 ? 279  PHE A CD2 1 
ATOM   2137 C CE1 . PHE A 1 279 ? -23.516 -10.472 -25.933 1.00 126.07 ? 279  PHE A CE1 1 
ATOM   2138 C CE2 . PHE A 1 279 ? -25.574 -9.257  -25.907 1.00 127.00 ? 279  PHE A CE2 1 
ATOM   2139 C CZ  . PHE A 1 279 ? -24.854 -10.395 -25.600 1.00 125.14 ? 279  PHE A CZ  1 
ATOM   2140 N N   . HIS A 1 282 ? -28.296 -7.595  -24.938 1.00 111.44 ? 282  HIS A N   1 
ATOM   2141 C CA  . HIS A 1 282 ? -29.658 -7.927  -24.521 1.00 111.36 ? 282  HIS A CA  1 
ATOM   2142 C C   . HIS A 1 282 ? -29.981 -7.274  -23.172 1.00 113.01 ? 282  HIS A C   1 
ATOM   2143 O O   . HIS A 1 282 ? -30.760 -7.822  -22.380 1.00 113.32 ? 282  HIS A O   1 
ATOM   2144 C CB  . HIS A 1 282 ? -29.887 -9.456  -24.502 1.00 112.96 ? 282  HIS A CB  1 
ATOM   2145 C CG  . HIS A 1 282 ? -29.774 -10.102 -25.855 1.00 117.38 ? 282  HIS A CG  1 
ATOM   2146 N ND1 . HIS A 1 282 ? -30.896 -10.337 -26.645 1.00 119.64 ? 282  HIS A ND1 1 
ATOM   2147 C CD2 . HIS A 1 282 ? -28.673 -10.534 -26.523 1.00 119.49 ? 282  HIS A CD2 1 
ATOM   2148 C CE1 . HIS A 1 282 ? -30.440 -10.896 -27.760 1.00 119.18 ? 282  HIS A CE1 1 
ATOM   2149 N NE2 . HIS A 1 282 ? -29.108 -11.028 -27.737 1.00 119.38 ? 282  HIS A NE2 1 
ATOM   2150 N N   . LEU A 1 283 ? -29.394 -6.070  -22.943 1.00 106.39 ? 283  LEU A N   1 
ATOM   2151 C CA  . LEU A 1 283 ? -29.517 -5.238  -21.742 1.00 104.70 ? 283  LEU A CA  1 
ATOM   2152 C C   . LEU A 1 283 ? -30.964 -4.754  -21.473 1.00 107.96 ? 283  LEU A C   1 
ATOM   2153 O O   . LEU A 1 283 ? -31.419 -3.834  -22.144 1.00 107.30 ? 283  LEU A O   1 
ATOM   2154 C CB  . LEU A 1 283 ? -28.547 -4.057  -21.892 1.00 104.22 ? 283  LEU A CB  1 
ATOM   2155 C CG  . LEU A 1 283 ? -28.327 -3.189  -20.673 1.00 108.93 ? 283  LEU A CG  1 
ATOM   2156 C CD1 . LEU A 1 283 ? -27.437 -3.880  -19.660 1.00 109.58 ? 283  LEU A CD1 1 
ATOM   2157 C CD2 . LEU A 1 283 ? -27.705 -1.876  -21.058 1.00 110.73 ? 283  LEU A CD2 1 
ATOM   2158 N N   . LYS A 1 284 ? -31.678 -5.362  -20.488 1.00 105.29 ? 284  LYS A N   1 
ATOM   2159 C CA  . LYS A 1 284 ? -33.088 -5.028  -20.152 1.00 105.12 ? 284  LYS A CA  1 
ATOM   2160 C C   . LYS A 1 284 ? -33.244 -3.915  -19.102 1.00 109.74 ? 284  LYS A C   1 
ATOM   2161 O O   . LYS A 1 284 ? -32.724 -4.028  -17.990 1.00 108.60 ? 284  LYS A O   1 
ATOM   2162 C CB  . LYS A 1 284 ? -33.892 -6.274  -19.742 1.00 106.72 ? 284  LYS A CB  1 
ATOM   2163 C CG  . LYS A 1 284 ? -33.936 -7.343  -20.829 1.00 115.23 ? 284  LYS A CG  1 
ATOM   2164 C CD  . LYS A 1 284 ? -35.151 -8.264  -20.722 1.00 120.55 ? 284  LYS A CD  1 
ATOM   2165 C CE  . LYS A 1 284 ? -35.097 -9.376  -21.751 1.00 121.68 ? 284  LYS A CE  1 
ATOM   2166 N NZ  . LYS A 1 284 ? -36.362 -10.154 -21.809 1.00 122.65 ? 284  LYS A NZ  1 
ATOM   2167 N N   . CYS A 1 285 ? -33.975 -2.844  -19.466 1.00 108.07 ? 285  CYS A N   1 
ATOM   2168 C CA  . CYS A 1 285 ? -34.184 -1.678  -18.605 1.00 109.07 ? 285  CYS A CA  1 
ATOM   2169 C C   . CYS A 1 285 ? -35.638 -1.385  -18.279 1.00 110.25 ? 285  CYS A C   1 
ATOM   2170 O O   . CYS A 1 285 ? -36.565 -1.856  -18.946 1.00 109.58 ? 285  CYS A O   1 
ATOM   2171 C CB  . CYS A 1 285 ? -33.504 -0.438  -19.181 1.00 110.80 ? 285  CYS A CB  1 
ATOM   2172 S SG  . CYS A 1 285 ? -31.776 -0.688  -19.651 1.00 115.82 ? 285  CYS A SG  1 
ATOM   2173 N N   . ARG A 1 286 ? -35.810 -0.568  -17.229 1.00 104.38 ? 286  ARG A N   1 
ATOM   2174 C CA  . ARG A 1 286 ? -37.077 -0.030  -16.761 1.00 102.45 ? 286  ARG A CA  1 
ATOM   2175 C C   . ARG A 1 286 ? -36.915 1.479   -16.873 1.00 102.42 ? 286  ARG A C   1 
ATOM   2176 O O   . ARG A 1 286 ? -35.836 2.012   -16.558 1.00 101.91 ? 286  ARG A O   1 
ATOM   2177 C CB  . ARG A 1 286 ? -37.351 -0.429  -15.314 1.00 101.77 ? 286  ARG A CB  1 
ATOM   2178 C CG  . ARG A 1 286 ? -38.829 -0.520  -15.016 1.00 111.13 ? 286  ARG A CG  1 
ATOM   2179 C CD  . ARG A 1 286 ? -39.075 -1.352  -13.782 1.00 120.73 ? 286  ARG A CD  1 
ATOM   2180 N NE  . ARG A 1 286 ? -39.826 -2.572  -14.056 1.00 129.34 ? 286  ARG A NE  1 
ATOM   2181 C CZ  . ARG A 1 286 ? -41.151 -2.645  -14.048 1.00 146.75 ? 286  ARG A CZ  1 
ATOM   2182 N NH1 . ARG A 1 286 ? -41.882 -1.564  -13.804 1.00 129.61 ? 286  ARG A NH1 1 
ATOM   2183 N NH2 . ARG A 1 286 ? -41.757 -3.800  -14.302 1.00 138.33 ? 286  ARG A NH2 1 
ATOM   2184 N N   . LEU A 1 287 ? -37.956 2.164   -17.389 1.00 95.14  ? 287  LEU A N   1 
ATOM   2185 C CA  . LEU A 1 287 ? -37.951 3.612   -17.592 1.00 92.41  ? 287  LEU A CA  1 
ATOM   2186 C C   . LEU A 1 287 ? -38.952 4.327   -16.716 1.00 91.31  ? 287  LEU A C   1 
ATOM   2187 O O   . LEU A 1 287 ? -40.122 3.951   -16.693 1.00 90.09  ? 287  LEU A O   1 
ATOM   2188 C CB  . LEU A 1 287 ? -38.217 3.943   -19.057 1.00 92.12  ? 287  LEU A CB  1 
ATOM   2189 C CG  . LEU A 1 287 ? -37.052 3.722   -19.978 1.00 96.29  ? 287  LEU A CG  1 
ATOM   2190 C CD1 . LEU A 1 287 ? -37.530 3.434   -21.342 1.00 96.39  ? 287  LEU A CD1 1 
ATOM   2191 C CD2 . LEU A 1 287 ? -36.125 4.912   -19.970 1.00 98.38  ? 287  LEU A CD2 1 
ATOM   2192 N N   . ARG A 1 288 ? -38.485 5.355   -15.988 1.00 84.59  ? 288  ARG A N   1 
ATOM   2193 C CA  . ARG A 1 288 ? -39.329 6.144   -15.113 1.00 83.00  ? 288  ARG A CA  1 
ATOM   2194 C C   . ARG A 1 288 ? -39.692 7.376   -15.858 1.00 85.83  ? 288  ARG A C   1 
ATOM   2195 O O   . ARG A 1 288 ? -38.827 8.223   -16.131 1.00 84.77  ? 288  ARG A O   1 
ATOM   2196 C CB  . ARG A 1 288 ? -38.636 6.475   -13.795 1.00 83.12  ? 288  ARG A CB  1 
ATOM   2197 N N   . MET A 1 289 ? -40.973 7.459   -16.247 1.00 82.80  ? 289  MET A N   1 
ATOM   2198 C CA  . MET A 1 289 ? -41.432 8.599   -17.034 1.00 82.46  ? 289  MET A CA  1 
ATOM   2199 C C   . MET A 1 289 ? -42.285 9.594   -16.259 1.00 87.97  ? 289  MET A C   1 
ATOM   2200 O O   . MET A 1 289 ? -42.695 10.594  -16.831 1.00 87.99  ? 289  MET A O   1 
ATOM   2201 C CB  . MET A 1 289 ? -42.132 8.142   -18.313 1.00 84.34  ? 289  MET A CB  1 
ATOM   2202 C CG  . MET A 1 289 ? -41.184 7.482   -19.268 1.00 87.61  ? 289  MET A CG  1 
ATOM   2203 S SD  . MET A 1 289 ? -42.057 6.663   -20.583 1.00 91.39  ? 289  MET A SD  1 
ATOM   2204 C CE  . MET A 1 289 ? -41.180 7.416   -22.056 1.00 88.63  ? 289  MET A CE  1 
ATOM   2205 N N   . ASP A 1 290 ? -42.504 9.354   -14.956 1.00 85.88  ? 290  ASP A N   1 
ATOM   2206 C CA  . ASP A 1 290 ? -43.258 10.230  -14.057 1.00 85.77  ? 290  ASP A CA  1 
ATOM   2207 C C   . ASP A 1 290 ? -42.634 11.636  -14.027 1.00 88.87  ? 290  ASP A C   1 
ATOM   2208 O O   . ASP A 1 290 ? -43.368 12.621  -14.009 1.00 88.73  ? 290  ASP A O   1 
ATOM   2209 C CB  . ASP A 1 290 ? -43.310 9.622   -12.638 1.00 88.20  ? 290  ASP A CB  1 
ATOM   2210 C CG  . ASP A 1 290 ? -41.944 9.340   -11.989 1.00 103.03 ? 290  ASP A CG  1 
ATOM   2211 O OD1 . ASP A 1 290 ? -41.344 8.274   -12.288 1.00 101.84 ? 290  ASP A OD1 1 
ATOM   2212 O OD2 . ASP A 1 290 ? -41.487 10.175  -11.171 1.00 112.04 ? 290  ASP A OD2 1 
ATOM   2213 N N   . LYS A 1 291 ? -41.287 11.718  -14.085 1.00 84.65  ? 291  LYS A N   1 
ATOM   2214 C CA  . LYS A 1 291 ? -40.542 12.975  -14.042 1.00 84.49  ? 291  LYS A CA  1 
ATOM   2215 C C   . LYS A 1 291 ? -40.323 13.607  -15.442 1.00 85.47  ? 291  LYS A C   1 
ATOM   2216 O O   . LYS A 1 291 ? -39.760 14.702  -15.547 1.00 84.71  ? 291  LYS A O   1 
ATOM   2217 C CB  . LYS A 1 291 ? -39.222 12.801  -13.265 1.00 87.92  ? 291  LYS A CB  1 
ATOM   2218 C CG  . LYS A 1 291 ? -39.366 13.025  -11.757 1.00 98.60  ? 291  LYS A CG  1 
ATOM   2219 C CD  . LYS A 1 291 ? -38.043 12.705  -11.014 1.00 105.05 ? 291  LYS A CD  1 
ATOM   2220 C CE  . LYS A 1 291 ? -38.222 12.415  -9.532  1.00 105.09 ? 291  LYS A CE  1 
ATOM   2221 N NZ  . LYS A 1 291 ? -37.883 11.006  -9.145  1.00 100.99 ? 291  LYS A NZ  1 
ATOM   2222 N N   . LEU A 1 292 ? -40.796 12.930  -16.497 1.00 79.34  ? 292  LEU A N   1 
ATOM   2223 C CA  . LEU A 1 292 ? -40.745 13.427  -17.867 1.00 77.61  ? 292  LEU A CA  1 
ATOM   2224 C C   . LEU A 1 292 ? -41.992 14.245  -18.153 1.00 82.20  ? 292  LEU A C   1 
ATOM   2225 O O   . LEU A 1 292 ? -43.092 13.894  -17.717 1.00 82.72  ? 292  LEU A O   1 
ATOM   2226 C CB  . LEU A 1 292 ? -40.714 12.270  -18.865 1.00 77.10  ? 292  LEU A CB  1 
ATOM   2227 C CG  . LEU A 1 292 ? -39.367 11.766  -19.321 1.00 81.43  ? 292  LEU A CG  1 
ATOM   2228 C CD1 . LEU A 1 292 ? -39.566 10.733  -20.386 1.00 80.07  ? 292  LEU A CD1 1 
ATOM   2229 C CD2 . LEU A 1 292 ? -38.472 12.914  -19.843 1.00 86.05  ? 292  LEU A CD2 1 
ATOM   2230 N N   . GLN A 1 293 ? -41.838 15.297  -18.944 1.00 78.17  ? 293  GLN A N   1 
ATOM   2231 C CA  . GLN A 1 293 ? -42.938 16.188  -19.330 1.00 76.80  ? 293  GLN A CA  1 
ATOM   2232 C C   . GLN A 1 293 ? -42.786 16.662  -20.777 1.00 74.85  ? 293  GLN A C   1 
ATOM   2233 O O   . GLN A 1 293 ? -41.655 16.814  -21.267 1.00 72.61  ? 293  GLN A O   1 
ATOM   2234 C CB  . GLN A 1 293 ? -43.044 17.378  -18.353 1.00 78.23  ? 293  GLN A CB  1 
ATOM   2235 C CG  . GLN A 1 293 ? -41.721 18.129  -18.128 1.00 93.95  ? 293  GLN A CG  1 
ATOM   2236 C CD  . GLN A 1 293 ? -41.784 19.112  -16.989 1.00 119.52 ? 293  GLN A CD  1 
ATOM   2237 O OE1 . GLN A 1 293 ? -41.730 20.327  -17.198 1.00 117.45 ? 293  GLN A OE1 1 
ATOM   2238 N NE2 . GLN A 1 293 ? -41.883 18.612  -15.753 1.00 111.15 ? 293  GLN A NE2 1 
ATOM   2239 N N   . LEU A 1 294 ? -43.939 16.901  -21.442 1.00 67.31  ? 294  LEU A N   1 
ATOM   2240 C CA  . LEU A 1 294 ? -44.014 17.380  -22.820 1.00 64.99  ? 294  LEU A CA  1 
ATOM   2241 C C   . LEU A 1 294 ? -43.548 18.809  -22.925 1.00 66.51  ? 294  LEU A C   1 
ATOM   2242 O O   . LEU A 1 294 ? -44.047 19.668  -22.183 1.00 66.70  ? 294  LEU A O   1 
ATOM   2243 C CB  . LEU A 1 294 ? -45.449 17.307  -23.338 1.00 64.38  ? 294  LEU A CB  1 
ATOM   2244 C CG  . LEU A 1 294 ? -45.897 15.987  -23.857 1.00 68.19  ? 294  LEU A CG  1 
ATOM   2245 C CD1 . LEU A 1 294 ? -47.387 15.983  -24.039 1.00 67.64  ? 294  LEU A CD1 1 
ATOM   2246 C CD2 . LEU A 1 294 ? -45.222 15.676  -25.171 1.00 71.65  ? 294  LEU A CD2 1 
ATOM   2247 N N   . LYS A 1 295 ? -42.597 19.082  -23.839 1.00 60.40  ? 295  LYS A N   1 
ATOM   2248 C CA  . LYS A 1 295 ? -42.153 20.446  -24.028 1.00 60.09  ? 295  LYS A CA  1 
ATOM   2249 C C   . LYS A 1 295 ? -43.308 21.088  -24.823 1.00 65.95  ? 295  LYS A C   1 
ATOM   2250 O O   . LYS A 1 295 ? -43.764 20.496  -25.808 1.00 64.82  ? 295  LYS A O   1 
ATOM   2251 C CB  . LYS A 1 295 ? -40.873 20.511  -24.868 1.00 61.99  ? 295  LYS A CB  1 
ATOM   2252 C CG  . LYS A 1 295 ? -40.057 21.788  -24.655 1.00 68.51  ? 295  LYS A CG  1 
ATOM   2253 C CD  . LYS A 1 295 ? -39.164 22.140  -25.867 1.00 76.28  ? 295  LYS A CD  1 
ATOM   2254 C CE  . LYS A 1 295 ? -38.103 23.189  -25.584 1.00 83.87  ? 295  LYS A CE  1 
ATOM   2255 N NZ  . LYS A 1 295 ? -38.644 24.455  -24.995 1.00 90.48  ? 295  LYS A NZ  1 
ATOM   2256 N N   . GLY A 1 296 ? -43.866 22.189  -24.338 1.00 64.59  ? 296  GLY A N   1 
ATOM   2257 C CA  . GLY A 1 296 ? -44.929 22.896  -25.052 1.00 64.75  ? 296  GLY A CA  1 
ATOM   2258 C C   . GLY A 1 296 ? -46.392 22.525  -24.882 1.00 69.08  ? 296  GLY A C   1 
ATOM   2259 O O   . GLY A 1 296 ? -47.234 23.024  -25.637 1.00 68.55  ? 296  GLY A O   1 
ATOM   2260 N N   . MET A 1 297 ? -46.731 21.703  -23.877 1.00 65.91  ? 297  MET A N   1 
ATOM   2261 C CA  . MET A 1 297 ? -48.127 21.343  -23.628 1.00 66.06  ? 297  MET A CA  1 
ATOM   2262 C C   . MET A 1 297 ? -49.002 22.572  -23.234 1.00 69.35  ? 297  MET A C   1 
ATOM   2263 O O   . MET A 1 297 ? -50.230 22.522  -23.345 1.00 70.09  ? 297  MET A O   1 
ATOM   2264 C CB  . MET A 1 297 ? -48.226 20.182  -22.620 1.00 68.85  ? 297  MET A CB  1 
ATOM   2265 C CG  . MET A 1 297 ? -49.501 19.348  -22.771 1.00 74.91  ? 297  MET A CG  1 
ATOM   2266 S SD  . MET A 1 297 ? -50.070 18.988  -24.509 1.00 82.44  ? 297  MET A SD  1 
ATOM   2267 C CE  . MET A 1 297 ? -51.667 18.141  -24.197 1.00 79.22  ? 297  MET A CE  1 
ATOM   2268 N N   . SER A 1 298 ? -48.362 23.683  -22.843 1.00 63.95  ? 298  SER A N   1 
ATOM   2269 C CA  . SER A 1 298 ? -49.026 24.921  -22.474 1.00 63.19  ? 298  SER A CA  1 
ATOM   2270 C C   . SER A 1 298 ? -48.842 26.004  -23.536 1.00 67.18  ? 298  SER A C   1 
ATOM   2271 O O   . SER A 1 298 ? -49.427 27.076  -23.394 1.00 67.21  ? 298  SER A O   1 
ATOM   2272 C CB  . SER A 1 298 ? -48.535 25.398  -21.112 1.00 67.80  ? 298  SER A CB  1 
ATOM   2273 O OG  . SER A 1 298 ? -49.392 24.986  -20.059 1.00 77.40  ? 298  SER A OG  1 
ATOM   2274 N N   . TYR A 1 299 ? -48.052 25.734  -24.612 1.00 63.14  ? 299  TYR A N   1 
ATOM   2275 C CA  . TYR A 1 299 ? -47.870 26.703  -25.698 1.00 62.60  ? 299  TYR A CA  1 
ATOM   2276 C C   . TYR A 1 299 ? -49.159 26.777  -26.493 1.00 67.77  ? 299  TYR A C   1 
ATOM   2277 O O   . TYR A 1 299 ? -49.926 25.809  -26.557 1.00 66.61  ? 299  TYR A O   1 
ATOM   2278 C CB  . TYR A 1 299 ? -46.740 26.316  -26.681 1.00 63.47  ? 299  TYR A CB  1 
ATOM   2279 C CG  . TYR A 1 299 ? -45.318 26.229  -26.168 1.00 65.56  ? 299  TYR A CG  1 
ATOM   2280 C CD1 . TYR A 1 299 ? -44.978 26.697  -24.896 1.00 68.22  ? 299  TYR A CD1 1 
ATOM   2281 C CD2 . TYR A 1 299 ? -44.299 25.714  -26.970 1.00 65.88  ? 299  TYR A CD2 1 
ATOM   2282 C CE1 . TYR A 1 299 ? -43.679 26.595  -24.416 1.00 69.33  ? 299  TYR A CE1 1 
ATOM   2283 C CE2 . TYR A 1 299 ? -42.995 25.611  -26.504 1.00 66.87  ? 299  TYR A CE2 1 
ATOM   2284 C CZ  . TYR A 1 299 ? -42.693 26.052  -25.226 1.00 81.86  ? 299  TYR A CZ  1 
ATOM   2285 O OH  . TYR A 1 299 ? -41.416 25.935  -24.750 1.00 92.44  ? 299  TYR A OH  1 
ATOM   2286 N N   . SER A 1 300 ? -49.386 27.929  -27.124 1.00 66.04  ? 300  SER A N   1 
ATOM   2287 C CA  . SER A 1 300 ? -50.562 28.145  -27.945 1.00 65.40  ? 300  SER A CA  1 
ATOM   2288 C C   . SER A 1 300 ? -50.364 27.562  -29.337 1.00 70.21  ? 300  SER A C   1 
ATOM   2289 O O   . SER A 1 300 ? -49.238 27.205  -29.703 1.00 69.21  ? 300  SER A O   1 
ATOM   2290 C CB  . SER A 1 300 ? -50.933 29.621  -27.964 1.00 67.57  ? 300  SER A CB  1 
ATOM   2291 O OG  . SER A 1 300 ? -51.502 29.965  -26.707 1.00 71.81  ? 300  SER A OG  1 
ATOM   2292 N N   . MET A 1 301 ? -51.468 27.403  -30.088 1.00 68.13  ? 301  MET A N   1 
ATOM   2293 C CA  . MET A 1 301 ? -51.441 26.815  -31.425 1.00 68.88  ? 301  MET A CA  1 
ATOM   2294 C C   . MET A 1 301 ? -50.886 27.787  -32.445 1.00 71.99  ? 301  MET A C   1 
ATOM   2295 O O   . MET A 1 301 ? -51.247 28.961  -32.438 1.00 71.53  ? 301  MET A O   1 
ATOM   2296 C CB  . MET A 1 301 ? -52.852 26.376  -31.851 1.00 72.20  ? 301  MET A CB  1 
ATOM   2297 C CG  . MET A 1 301 ? -53.422 25.251  -31.014 1.00 77.04  ? 301  MET A CG  1 
ATOM   2298 S SD  . MET A 1 301 ? -52.551 23.694  -31.282 1.00 82.44  ? 301  MET A SD  1 
ATOM   2299 C CE  . MET A 1 301 ? -53.359 23.165  -32.755 1.00 79.95  ? 301  MET A CE  1 
ATOM   2300 N N   . CYS A 1 302 ? -50.019 27.304  -33.341 1.00 68.83  ? 302  CYS A N   1 
ATOM   2301 C CA  . CYS A 1 302 ? -49.467 28.131  -34.413 1.00 68.74  ? 302  CYS A CA  1 
ATOM   2302 C C   . CYS A 1 302 ? -50.642 28.590  -35.260 1.00 74.10  ? 302  CYS A C   1 
ATOM   2303 O O   . CYS A 1 302 ? -51.606 27.836  -35.430 1.00 73.34  ? 302  CYS A O   1 
ATOM   2304 C CB  . CYS A 1 302 ? -48.460 27.346  -35.257 1.00 68.88  ? 302  CYS A CB  1 
ATOM   2305 S SG  . CYS A 1 302 ? -46.938 26.854  -34.390 1.00 72.60  ? 302  CYS A SG  1 
ATOM   2306 N N   . THR A 1 303 ? -50.594 29.824  -35.762 1.00 73.12  ? 303  THR A N   1 
ATOM   2307 C CA  . THR A 1 303 ? -51.683 30.368  -36.603 1.00 73.28  ? 303  THR A CA  1 
ATOM   2308 C C   . THR A 1 303 ? -51.233 30.568  -38.053 1.00 77.85  ? 303  THR A C   1 
ATOM   2309 O O   . THR A 1 303 ? -52.064 30.539  -38.968 1.00 78.27  ? 303  THR A O   1 
ATOM   2310 C CB  . THR A 1 303 ? -52.317 31.642  -35.988 1.00 72.84  ? 303  THR A CB  1 
ATOM   2311 O OG1 . THR A 1 303 ? -51.320 32.669  -35.836 1.00 75.01  ? 303  THR A OG1 1 
ATOM   2312 C CG2 . THR A 1 303 ? -53.065 31.362  -34.664 1.00 61.63  ? 303  THR A CG2 1 
ATOM   2313 N N   . GLY A 1 304 ? -49.926 30.716  -38.239 1.00 74.48  ? 304  GLY A N   1 
ATOM   2314 C CA  . GLY A 1 304 ? -49.306 30.949  -39.531 1.00 74.97  ? 304  GLY A CA  1 
ATOM   2315 C C   . GLY A 1 304 ? -49.387 29.830  -40.545 1.00 80.46  ? 304  GLY A C   1 
ATOM   2316 O O   . GLY A 1 304 ? -50.126 28.842  -40.384 1.00 81.57  ? 304  GLY A O   1 
ATOM   2317 N N   . LYS A 1 305 ? -48.612 30.013  -41.621 1.00 75.82  ? 305  LYS A N   1 
ATOM   2318 C CA  . LYS A 1 305 ? -48.527 29.095  -42.750 1.00 74.69  ? 305  LYS A CA  1 
ATOM   2319 C C   . LYS A 1 305 ? -47.225 28.312  -42.691 1.00 74.22  ? 305  LYS A C   1 
ATOM   2320 O O   . LYS A 1 305 ? -46.232 28.799  -42.142 1.00 72.97  ? 305  LYS A O   1 
ATOM   2321 C CB  . LYS A 1 305 ? -48.682 29.855  -44.094 1.00 77.65  ? 305  LYS A CB  1 
ATOM   2322 C CG  . LYS A 1 305 ? -50.027 30.599  -44.256 1.00 84.88  ? 305  LYS A CG  1 
ATOM   2323 C CD  . LYS A 1 305 ? -50.171 31.168  -45.661 1.00 100.18 ? 305  LYS A CD  1 
ATOM   2324 C CE  . LYS A 1 305 ? -51.475 31.901  -45.874 1.00 114.27 ? 305  LYS A CE  1 
ATOM   2325 N NZ  . LYS A 1 305 ? -52.193 31.435  -47.095 1.00 119.42 ? 305  LYS A NZ  1 
ATOM   2326 N N   . PHE A 1 306 ? -47.242 27.088  -43.249 1.00 69.08  ? 306  PHE A N   1 
ATOM   2327 C CA  . PHE A 1 306 ? -46.090 26.177  -43.249 1.00 67.20  ? 306  PHE A CA  1 
ATOM   2328 C C   . PHE A 1 306 ? -45.618 25.810  -44.640 1.00 70.24  ? 306  PHE A C   1 
ATOM   2329 O O   . PHE A 1 306 ? -46.428 25.649  -45.537 1.00 70.45  ? 306  PHE A O   1 
ATOM   2330 C CB  . PHE A 1 306 ? -46.438 24.904  -42.467 1.00 67.63  ? 306  PHE A CB  1 
ATOM   2331 C CG  . PHE A 1 306 ? -46.660 25.122  -40.995 1.00 66.72  ? 306  PHE A CG  1 
ATOM   2332 C CD1 . PHE A 1 306 ? -45.595 25.140  -40.116 1.00 68.54  ? 306  PHE A CD1 1 
ATOM   2333 C CD2 . PHE A 1 306 ? -47.934 25.302  -40.491 1.00 67.19  ? 306  PHE A CD2 1 
ATOM   2334 C CE1 . PHE A 1 306 ? -45.804 25.311  -38.755 1.00 71.46  ? 306  PHE A CE1 1 
ATOM   2335 C CE2 . PHE A 1 306 ? -48.146 25.486  -39.132 1.00 67.60  ? 306  PHE A CE2 1 
ATOM   2336 C CZ  . PHE A 1 306 ? -47.081 25.505  -38.275 1.00 69.04  ? 306  PHE A CZ  1 
ATOM   2337 N N   . LYS A 1 307 ? -44.319 25.652  -44.806 1.00 67.10  ? 307  LYS A N   1 
ATOM   2338 C CA  . LYS A 1 307 ? -43.692 25.278  -46.073 1.00 68.32  ? 307  LYS A CA  1 
ATOM   2339 C C   . LYS A 1 307 ? -43.121 23.838  -45.958 1.00 77.76  ? 307  LYS A C   1 
ATOM   2340 O O   . LYS A 1 307 ? -42.768 23.403  -44.860 1.00 79.01  ? 307  LYS A O   1 
ATOM   2341 C CB  . LYS A 1 307 ? -42.579 26.283  -46.406 1.00 69.57  ? 307  LYS A CB  1 
ATOM   2342 C CG  . LYS A 1 307 ? -42.205 26.365  -47.868 1.00 84.11  ? 307  LYS A CG  1 
ATOM   2343 C CD  . LYS A 1 307 ? -41.057 27.355  -48.102 1.00 100.19 ? 307  LYS A CD  1 
ATOM   2344 C CE  . LYS A 1 307 ? -39.744 27.126  -47.347 1.00 106.01 ? 307  LYS A CE  1 
ATOM   2345 N NZ  . LYS A 1 307 ? -38.985 28.389  -47.131 1.00 103.80 ? 307  LYS A NZ  1 
ATOM   2346 N N   . ILE A 1 308 ? -43.023 23.114  -47.085 1.00 75.10  ? 308  ILE A N   1 
ATOM   2347 C CA  . ILE A 1 308 ? -42.572 21.718  -47.135 1.00 75.30  ? 308  ILE A CA  1 
ATOM   2348 C C   . ILE A 1 308 ? -41.108 21.577  -47.569 1.00 81.78  ? 308  ILE A C   1 
ATOM   2349 O O   . ILE A 1 308 ? -40.806 21.454  -48.755 1.00 81.60  ? 308  ILE A O   1 
ATOM   2350 C CB  . ILE A 1 308 ? -43.521 20.827  -47.978 1.00 78.48  ? 308  ILE A CB  1 
ATOM   2351 C CG1 . ILE A 1 308 ? -44.461 21.657  -48.939 1.00 80.84  ? 308  ILE A CG1 1 
ATOM   2352 C CG2 . ILE A 1 308 ? -44.335 19.968  -47.059 1.00 76.31  ? 308  ILE A CG2 1 
ATOM   2353 C CD1 . ILE A 1 308 ? -43.789 22.514  -50.238 1.00 90.46  ? 308  ILE A CD1 1 
ATOM   2354 N N   . VAL A 1 309 ? -40.211 21.570  -46.573 1.00 80.62  ? 309  VAL A N   1 
ATOM   2355 C CA  . VAL A 1 309 ? -38.746 21.462  -46.668 1.00 81.21  ? 309  VAL A CA  1 
ATOM   2356 C C   . VAL A 1 309 ? -38.308 20.110  -47.293 1.00 85.22  ? 309  VAL A C   1 
ATOM   2357 O O   . VAL A 1 309 ? -37.519 20.095  -48.247 1.00 84.90  ? 309  VAL A O   1 
ATOM   2358 C CB  . VAL A 1 309 ? -38.131 21.693  -45.253 1.00 85.81  ? 309  VAL A CB  1 
ATOM   2359 C CG1 . VAL A 1 309 ? -36.610 21.532  -45.253 1.00 85.85  ? 309  VAL A CG1 1 
ATOM   2360 C CG2 . VAL A 1 309 ? -38.544 23.056  -44.677 1.00 85.64  ? 309  VAL A CG2 1 
ATOM   2361 N N   . LYS A 1 310 ? -38.810 18.992  -46.740 1.00 81.27  ? 310  LYS A N   1 
ATOM   2362 C CA  . LYS A 1 310 ? -38.510 17.653  -47.238 1.00 80.49  ? 310  LYS A CA  1 
ATOM   2363 C C   . LYS A 1 310 ? -39.812 16.891  -47.422 1.00 83.19  ? 310  LYS A C   1 
ATOM   2364 O O   . LYS A 1 310 ? -40.625 16.778  -46.479 1.00 83.50  ? 310  LYS A O   1 
ATOM   2365 C CB  . LYS A 1 310 ? -37.548 16.913  -46.294 1.00 82.76  ? 310  LYS A CB  1 
ATOM   2366 C CG  . LYS A 1 310 ? -36.610 15.938  -47.003 1.00 94.98  ? 310  LYS A CG  1 
ATOM   2367 C CD  . LYS A 1 310 ? -35.363 15.638  -46.152 1.00 101.31 ? 310  LYS A CD  1 
ATOM   2368 C CE  . LYS A 1 310 ? -34.199 15.059  -46.931 1.00 103.37 ? 310  LYS A CE  1 
ATOM   2369 N NZ  . LYS A 1 310 ? -33.453 16.090  -47.705 1.00 107.98 ? 310  LYS A NZ  1 
ATOM   2370 N N   . GLU A 1 311 ? -40.007 16.386  -48.658 1.00 76.96  ? 311  GLU A N   1 
ATOM   2371 C CA  . GLU A 1 311 ? -41.164 15.603  -49.095 1.00 75.81  ? 311  GLU A CA  1 
ATOM   2372 C C   . GLU A 1 311 ? -41.459 14.420  -48.150 1.00 77.96  ? 311  GLU A C   1 
ATOM   2373 O O   . GLU A 1 311 ? -40.541 13.884  -47.530 1.00 76.47  ? 311  GLU A O   1 
ATOM   2374 C CB  . GLU A 1 311 ? -40.904 15.095  -50.518 1.00 77.13  ? 311  GLU A CB  1 
ATOM   2375 C CG  . GLU A 1 311 ? -42.095 14.397  -51.158 1.00 91.45  ? 311  GLU A CG  1 
ATOM   2376 C CD  . GLU A 1 311 ? -41.977 14.080  -52.637 1.00 121.82 ? 311  GLU A CD  1 
ATOM   2377 O OE1 . GLU A 1 311 ? -41.418 14.915  -53.384 1.00 127.88 ? 311  GLU A OE1 1 
ATOM   2378 O OE2 . GLU A 1 311 ? -42.512 13.029  -53.060 1.00 113.68 ? 311  GLU A OE2 1 
ATOM   2379 N N   . ILE A 1 312 ? -42.741 14.024  -48.042 1.00 74.43  ? 312  ILE A N   1 
ATOM   2380 C CA  . ILE A 1 312 ? -43.137 12.869  -47.233 1.00 73.61  ? 312  ILE A CA  1 
ATOM   2381 C C   . ILE A 1 312 ? -42.340 11.676  -47.730 1.00 78.46  ? 312  ILE A C   1 
ATOM   2382 O O   . ILE A 1 312 ? -42.293 11.421  -48.938 1.00 78.05  ? 312  ILE A O   1 
ATOM   2383 C CB  . ILE A 1 312 ? -44.667 12.543  -47.258 1.00 75.87  ? 312  ILE A CB  1 
ATOM   2384 C CG1 . ILE A 1 312 ? -45.544 13.772  -46.940 1.00 75.93  ? 312  ILE A CG1 1 
ATOM   2385 C CG2 . ILE A 1 312 ? -44.988 11.368  -46.326 1.00 75.04  ? 312  ILE A CG2 1 
ATOM   2386 C CD1 . ILE A 1 312 ? -47.076 13.518  -46.925 1.00 74.57  ? 312  ILE A CD1 1 
ATOM   2387 N N   . ALA A 1 313 ? -41.673 10.991  -46.792 1.00 75.67  ? 313  ALA A N   1 
ATOM   2388 C CA  . ALA A 1 313 ? -40.882 9.783   -47.016 1.00 74.92  ? 313  ALA A CA  1 
ATOM   2389 C C   . ALA A 1 313 ? -41.437 8.720   -46.083 1.00 76.15  ? 313  ALA A C   1 
ATOM   2390 O O   . ALA A 1 313 ? -41.730 9.022   -44.922 1.00 75.79  ? 313  ALA A O   1 
ATOM   2391 C CB  . ALA A 1 313 ? -39.410 10.047  -46.701 1.00 75.58  ? 313  ALA A CB  1 
ATOM   2392 N N   . GLU A 1 314 ? -41.628 7.497   -46.591 1.00 70.20  ? 314  GLU A N   1 
ATOM   2393 C CA  . GLU A 1 314 ? -42.139 6.399   -45.774 1.00 68.53  ? 314  GLU A CA  1 
ATOM   2394 C C   . GLU A 1 314 ? -40.978 5.553   -45.229 1.00 68.26  ? 314  GLU A C   1 
ATOM   2395 O O   . GLU A 1 314 ? -40.048 5.200   -45.965 1.00 68.66  ? 314  GLU A O   1 
ATOM   2396 C CB  . GLU A 1 314 ? -43.151 5.544   -46.560 1.00 69.89  ? 314  GLU A CB  1 
ATOM   2397 C CG  . GLU A 1 314 ? -43.913 4.537   -45.710 1.00 78.56  ? 314  GLU A CG  1 
ATOM   2398 C CD  . GLU A 1 314 ? -44.864 3.637   -46.472 1.00 97.70  ? 314  GLU A CD  1 
ATOM   2399 O OE1 . GLU A 1 314 ? -44.408 2.984   -47.439 1.00 89.04  ? 314  GLU A OE1 1 
ATOM   2400 O OE2 . GLU A 1 314 ? -46.053 3.553   -46.078 1.00 90.38  ? 314  GLU A OE2 1 
ATOM   2401 N N   . THR A 1 315 ? -41.032 5.248   -43.935 1.00 60.69  ? 315  THR A N   1 
ATOM   2402 C CA  . THR A 1 315 ? -40.019 4.416   -43.299 1.00 58.81  ? 315  THR A CA  1 
ATOM   2403 C C   . THR A 1 315 ? -40.347 2.948   -43.547 1.00 61.30  ? 315  THR A C   1 
ATOM   2404 O O   . THR A 1 315 ? -41.440 2.624   -44.023 1.00 60.36  ? 315  THR A O   1 
ATOM   2405 C CB  . THR A 1 315 ? -39.821 4.750   -41.807 1.00 55.25  ? 315  THR A CB  1 
ATOM   2406 O OG1 . THR A 1 315 ? -40.857 4.153   -41.008 1.00 62.45  ? 315  THR A OG1 1 
ATOM   2407 C CG2 . THR A 1 315 ? -39.671 6.226   -41.547 1.00 39.25  ? 315  THR A CG2 1 
ATOM   2408 N N   . GLN A 1 316 ? -39.414 2.066   -43.194 1.00 57.45  ? 316  GLN A N   1 
ATOM   2409 C CA  . GLN A 1 316 ? -39.583 0.645   -43.368 1.00 58.30  ? 316  GLN A CA  1 
ATOM   2410 C C   . GLN A 1 316 ? -40.756 0.060   -42.560 1.00 66.49  ? 316  GLN A C   1 
ATOM   2411 O O   . GLN A 1 316 ? -41.237 -1.024  -42.909 1.00 68.46  ? 316  GLN A O   1 
ATOM   2412 C CB  . GLN A 1 316 ? -38.259 -0.079  -43.089 1.00 59.66  ? 316  GLN A CB  1 
ATOM   2413 C CG  . GLN A 1 316 ? -37.318 -0.028  -44.319 1.00 69.38  ? 316  GLN A CG  1 
ATOM   2414 C CD  . GLN A 1 316 ? -35.930 -0.563  -44.077 1.00 67.98  ? 316  GLN A CD  1 
ATOM   2415 O OE1 . GLN A 1 316 ? -35.742 -1.739  -43.810 1.00 57.34  ? 316  GLN A OE1 1 
ATOM   2416 N NE2 . GLN A 1 316 ? -34.929 0.293   -44.185 1.00 59.90  ? 316  GLN A NE2 1 
ATOM   2417 N N   . HIS A 1 317 ? -41.277 0.800   -41.553 1.00 62.98  ? 317  HIS A N   1 
ATOM   2418 C CA  . HIS A 1 317 ? -42.377 0.298   -40.725 1.00 62.92  ? 317  HIS A CA  1 
ATOM   2419 C C   . HIS A 1 317 ? -43.712 0.934   -41.054 1.00 68.27  ? 317  HIS A C   1 
ATOM   2420 O O   . HIS A 1 317 ? -44.619 0.923   -40.216 1.00 71.13  ? 317  HIS A O   1 
ATOM   2421 C CB  . HIS A 1 317 ? -42.036 0.411   -39.229 1.00 63.54  ? 317  HIS A CB  1 
ATOM   2422 C CG  . HIS A 1 317 ? -40.642 -0.033  -38.949 1.00 67.10  ? 317  HIS A CG  1 
ATOM   2423 N ND1 . HIS A 1 317 ? -40.314 -1.382  -38.910 1.00 68.51  ? 317  HIS A ND1 1 
ATOM   2424 C CD2 . HIS A 1 317 ? -39.509 0.702   -38.833 1.00 68.53  ? 317  HIS A CD2 1 
ATOM   2425 C CE1 . HIS A 1 317 ? -39.010 -1.422  -38.720 1.00 67.55  ? 317  HIS A CE1 1 
ATOM   2426 N NE2 . HIS A 1 317 ? -38.480 -0.193  -38.665 1.00 67.95  ? 317  HIS A NE2 1 
ATOM   2427 N N   . GLY A 1 318 ? -43.849 1.442   -42.275 1.00 61.84  ? 318  GLY A N   1 
ATOM   2428 C CA  . GLY A 1 318 ? -45.087 2.080   -42.720 1.00 60.35  ? 318  GLY A CA  1 
ATOM   2429 C C   . GLY A 1 318 ? -45.294 3.523   -42.278 1.00 59.11  ? 318  GLY A C   1 
ATOM   2430 O O   . GLY A 1 318 ? -46.124 4.230   -42.861 1.00 58.70  ? 318  GLY A O   1 
ATOM   2431 N N   . THR A 1 319 ? -44.528 3.977   -41.267 1.00 51.83  ? 319  THR A N   1 
ATOM   2432 C CA  . THR A 1 319 ? -44.608 5.336   -40.737 1.00 50.58  ? 319  THR A CA  1 
ATOM   2433 C C   . THR A 1 319 ? -44.077 6.324   -41.754 1.00 50.78  ? 319  THR A C   1 
ATOM   2434 O O   . THR A 1 319 ? -43.337 5.948   -42.647 1.00 48.17  ? 319  THR A O   1 
ATOM   2435 C CB  . THR A 1 319 ? -43.895 5.483   -39.355 1.00 58.71  ? 319  THR A CB  1 
ATOM   2436 O OG1 . THR A 1 319 ? -42.506 5.708   -39.561 1.00 60.14  ? 319  THR A OG1 1 
ATOM   2437 C CG2 . THR A 1 319 ? -44.115 4.294   -38.408 1.00 52.59  ? 319  THR A CG2 1 
ATOM   2438 N N   . ILE A 1 320 ? -44.486 7.573   -41.640 1.00 49.22  ? 320  ILE A N   1 
ATOM   2439 C CA  . ILE A 1 320 ? -44.051 8.605   -42.562 1.00 51.30  ? 320  ILE A CA  1 
ATOM   2440 C C   . ILE A 1 320 ? -43.371 9.725   -41.839 1.00 60.56  ? 320  ILE A C   1 
ATOM   2441 O O   . ILE A 1 320 ? -43.636 9.949   -40.648 1.00 62.11  ? 320  ILE A O   1 
ATOM   2442 C CB  . ILE A 1 320 ? -45.191 9.114   -43.469 1.00 55.11  ? 320  ILE A CB  1 
ATOM   2443 C CG1 . ILE A 1 320 ? -46.393 9.680   -42.668 1.00 55.84  ? 320  ILE A CG1 1 
ATOM   2444 C CG2 . ILE A 1 320 ? -45.619 8.043   -44.436 1.00 56.83  ? 320  ILE A CG2 1 
ATOM   2445 C CD1 . ILE A 1 320 ? -46.572 11.127  -42.838 1.00 64.06  ? 320  ILE A CD1 1 
ATOM   2446 N N   . VAL A 1 321 ? -42.491 10.437  -42.564 1.00 58.25  ? 321  VAL A N   1 
ATOM   2447 C CA  . VAL A 1 321 ? -41.726 11.568  -42.044 1.00 58.88  ? 321  VAL A CA  1 
ATOM   2448 C C   . VAL A 1 321 ? -41.892 12.793  -42.950 1.00 62.77  ? 321  VAL A C   1 
ATOM   2449 O O   . VAL A 1 321 ? -41.804 12.678  -44.167 1.00 62.86  ? 321  VAL A O   1 
ATOM   2450 C CB  . VAL A 1 321 ? -40.234 11.204  -41.765 1.00 62.59  ? 321  VAL A CB  1 
ATOM   2451 C CG1 . VAL A 1 321 ? -39.489 12.347  -41.084 1.00 61.95  ? 321  VAL A CG1 1 
ATOM   2452 C CG2 . VAL A 1 321 ? -40.142 9.953   -40.917 1.00 62.47  ? 321  VAL A CG2 1 
ATOM   2453 N N   . ILE A 1 322 ? -42.103 13.953  -42.341 1.00 59.52  ? 322  ILE A N   1 
ATOM   2454 C CA  . ILE A 1 322 ? -42.266 15.219  -43.028 1.00 60.58  ? 322  ILE A CA  1 
ATOM   2455 C C   . ILE A 1 322 ? -41.398 16.288  -42.397 1.00 67.99  ? 322  ILE A C   1 
ATOM   2456 O O   . ILE A 1 322 ? -41.388 16.412  -41.172 1.00 69.65  ? 322  ILE A O   1 
ATOM   2457 C CB  . ILE A 1 322 ? -43.787 15.607  -43.085 1.00 64.52  ? 322  ILE A CB  1 
ATOM   2458 C CG1 . ILE A 1 322 ? -44.040 16.928  -43.820 1.00 66.51  ? 322  ILE A CG1 1 
ATOM   2459 C CG2 . ILE A 1 322 ? -44.481 15.614  -41.730 1.00 65.13  ? 322  ILE A CG2 1 
ATOM   2460 C CD1 . ILE A 1 322 ? -43.962 16.796  -45.383 1.00 83.75  ? 322  ILE A CD1 1 
ATOM   2461 N N   . ARG A 1 323 ? -40.631 17.041  -43.204 1.00 66.00  ? 323  ARG A N   1 
ATOM   2462 C CA  . ARG A 1 323 ? -39.859 18.179  -42.670 1.00 66.30  ? 323  ARG A CA  1 
ATOM   2463 C C   . ARG A 1 323 ? -40.494 19.515  -43.151 1.00 69.16  ? 323  ARG A C   1 
ATOM   2464 O O   . ARG A 1 323 ? -40.644 19.717  -44.355 1.00 69.03  ? 323  ARG A O   1 
ATOM   2465 C CB  . ARG A 1 323 ? -38.354 18.091  -42.948 1.00 67.68  ? 323  ARG A CB  1 
ATOM   2466 C CG  . ARG A 1 323 ? -37.533 19.026  -42.036 1.00 85.80  ? 323  ARG A CG  1 
ATOM   2467 C CD  . ARG A 1 323 ? -36.041 19.104  -42.375 1.00 96.43  ? 323  ARG A CD  1 
ATOM   2468 N NE  . ARG A 1 323 ? -35.358 17.814  -42.243 1.00 98.51  ? 323  ARG A NE  1 
ATOM   2469 C CZ  . ARG A 1 323 ? -34.321 17.431  -42.985 1.00 107.90 ? 323  ARG A CZ  1 
ATOM   2470 N NH1 . ARG A 1 323 ? -33.830 18.236  -43.922 1.00 86.98  ? 323  ARG A NH1 1 
ATOM   2471 N NH2 . ARG A 1 323 ? -33.771 16.235  -42.799 1.00 94.84  ? 323  ARG A NH2 1 
ATOM   2472 N N   . VAL A 1 324 ? -40.948 20.361  -42.211 1.00 64.13  ? 324  VAL A N   1 
ATOM   2473 C CA  . VAL A 1 324 ? -41.643 21.624  -42.483 1.00 63.80  ? 324  VAL A CA  1 
ATOM   2474 C C   . VAL A 1 324 ? -41.047 22.851  -41.780 1.00 70.99  ? 324  VAL A C   1 
ATOM   2475 O O   . VAL A 1 324 ? -40.592 22.748  -40.646 1.00 70.33  ? 324  VAL A O   1 
ATOM   2476 C CB  . VAL A 1 324 ? -43.159 21.538  -42.181 1.00 66.91  ? 324  VAL A CB  1 
ATOM   2477 C CG1 . VAL A 1 324 ? -43.892 20.737  -43.247 1.00 67.08  ? 324  VAL A CG1 1 
ATOM   2478 C CG2 . VAL A 1 324 ? -43.430 20.982  -40.790 1.00 66.42  ? 324  VAL A CG2 1 
ATOM   2479 N N   . GLN A 1 325 ? -41.138 24.029  -42.425 1.00 69.87  ? 325  GLN A N   1 
ATOM   2480 C CA  . GLN A 1 325 ? -40.687 25.306  -41.864 1.00 70.27  ? 325  GLN A CA  1 
ATOM   2481 C C   . GLN A 1 325 ? -41.887 26.243  -41.613 1.00 72.17  ? 325  GLN A C   1 
ATOM   2482 O O   . GLN A 1 325 ? -42.751 26.374  -42.481 1.00 71.59  ? 325  GLN A O   1 
ATOM   2483 C CB  . GLN A 1 325 ? -39.682 25.974  -42.806 1.00 72.52  ? 325  GLN A CB  1 
ATOM   2484 C CG  . GLN A 1 325 ? -38.436 26.493  -42.095 1.00 94.10  ? 325  GLN A CG  1 
ATOM   2485 C CD  . GLN A 1 325 ? -37.625 27.456  -42.933 1.00 114.22 ? 325  GLN A CD  1 
ATOM   2486 O OE1 . GLN A 1 325 ? -37.753 27.531  -44.167 1.00 111.70 ? 325  GLN A OE1 1 
ATOM   2487 N NE2 . GLN A 1 325 ? -36.755 28.210  -42.277 1.00 105.79 ? 325  GLN A NE2 1 
ATOM   2488 N N   . TYR A 1 326 ? -41.954 26.868  -40.417 1.00 67.84  ? 326  TYR A N   1 
ATOM   2489 C CA  . TYR A 1 326 ? -43.046 27.792  -40.038 1.00 66.86  ? 326  TYR A CA  1 
ATOM   2490 C C   . TYR A 1 326 ? -42.763 29.172  -40.567 1.00 70.90  ? 326  TYR A C   1 
ATOM   2491 O O   . TYR A 1 326 ? -41.643 29.668  -40.420 1.00 72.90  ? 326  TYR A O   1 
ATOM   2492 C CB  . TYR A 1 326 ? -43.251 27.834  -38.504 1.00 66.46  ? 326  TYR A CB  1 
ATOM   2493 C CG  . TYR A 1 326 ? -44.367 28.726  -37.982 1.00 64.86  ? 326  TYR A CG  1 
ATOM   2494 C CD1 . TYR A 1 326 ? -45.672 28.598  -38.456 1.00 64.97  ? 326  TYR A CD1 1 
ATOM   2495 C CD2 . TYR A 1 326 ? -44.145 29.604  -36.923 1.00 65.37  ? 326  TYR A CD2 1 
ATOM   2496 C CE1 . TYR A 1 326 ? -46.718 29.352  -37.918 1.00 62.88  ? 326  TYR A CE1 1 
ATOM   2497 C CE2 . TYR A 1 326 ? -45.184 30.362  -36.375 1.00 65.89  ? 326  TYR A CE2 1 
ATOM   2498 C CZ  . TYR A 1 326 ? -46.469 30.234  -36.877 1.00 69.07  ? 326  TYR A CZ  1 
ATOM   2499 O OH  . TYR A 1 326 ? -47.476 31.008  -36.351 1.00 67.12  ? 326  TYR A OH  1 
ATOM   2500 N N   . GLU A 1 327 ? -43.771 29.790  -41.183 1.00 64.92  ? 327  GLU A N   1 
ATOM   2501 C CA  . GLU A 1 327 ? -43.632 31.112  -41.773 1.00 64.49  ? 327  GLU A CA  1 
ATOM   2502 C C   . GLU A 1 327 ? -44.459 32.188  -41.058 1.00 69.81  ? 327  GLU A C   1 
ATOM   2503 O O   . GLU A 1 327 ? -44.538 33.308  -41.547 1.00 70.06  ? 327  GLU A O   1 
ATOM   2504 C CB  . GLU A 1 327 ? -43.928 31.041  -43.273 1.00 65.55  ? 327  GLU A CB  1 
ATOM   2505 C CG  . GLU A 1 327 ? -42.874 30.242  -44.018 1.00 75.37  ? 327  GLU A CG  1 
ATOM   2506 C CD  . GLU A 1 327 ? -43.204 29.923  -45.461 1.00 113.47 ? 327  GLU A CD  1 
ATOM   2507 O OE1 . GLU A 1 327 ? -44.208 29.214  -45.701 1.00 118.11 ? 327  GLU A OE1 1 
ATOM   2508 O OE2 . GLU A 1 327 ? -42.466 30.395  -46.356 1.00 117.25 ? 327  GLU A OE2 1 
ATOM   2509 N N   . GLY A 1 328 ? -45.003 31.846  -39.889 1.00 67.97  ? 328  GLY A N   1 
ATOM   2510 C CA  . GLY A 1 328 ? -45.824 32.721  -39.055 1.00 69.03  ? 328  GLY A CA  1 
ATOM   2511 C C   . GLY A 1 328 ? -45.014 33.498  -38.036 1.00 76.20  ? 328  GLY A C   1 
ATOM   2512 O O   . GLY A 1 328 ? -43.820 33.718  -38.260 1.00 75.55  ? 328  GLY A O   1 
ATOM   2513 N N   . ASP A 1 329 ? -45.650 33.941  -36.916 1.00 75.25  ? 329  ASP A N   1 
ATOM   2514 C CA  . ASP A 1 329 ? -44.956 34.753  -35.899 1.00 76.11  ? 329  ASP A CA  1 
ATOM   2515 C C   . ASP A 1 329 ? -45.091 34.290  -34.425 1.00 80.91  ? 329  ASP A C   1 
ATOM   2516 O O   . ASP A 1 329 ? -44.242 34.665  -33.598 1.00 82.03  ? 329  ASP A O   1 
ATOM   2517 C CB  . ASP A 1 329 ? -45.370 36.236  -35.996 1.00 78.16  ? 329  ASP A CB  1 
ATOM   2518 C CG  . ASP A 1 329 ? -45.095 36.908  -37.333 1.00 93.40  ? 329  ASP A CG  1 
ATOM   2519 O OD1 . ASP A 1 329 ? -43.945 36.798  -37.842 1.00 92.30  ? 329  ASP A OD1 1 
ATOM   2520 O OD2 . ASP A 1 329 ? -45.992 37.604  -37.831 1.00 103.81 ? 329  ASP A OD2 1 
ATOM   2521 N N   . GLY A 1 330 ? -46.131 33.508  -34.116 1.00 74.58  ? 330  GLY A N   1 
ATOM   2522 C CA  . GLY A 1 330 ? -46.434 33.055  -32.761 1.00 73.12  ? 330  GLY A CA  1 
ATOM   2523 C C   . GLY A 1 330 ? -45.389 32.301  -31.957 1.00 74.89  ? 330  GLY A C   1 
ATOM   2524 O O   . GLY A 1 330 ? -45.517 32.220  -30.730 1.00 72.74  ? 330  GLY A O   1 
ATOM   2525 N N   . SER A 1 331 ? -44.347 31.756  -32.632 1.00 72.75  ? 331  SER A N   1 
ATOM   2526 C CA  . SER A 1 331 ? -43.279 30.896  -32.087 1.00 72.63  ? 331  SER A CA  1 
ATOM   2527 C C   . SER A 1 331 ? -42.672 31.398  -30.776 1.00 77.59  ? 331  SER A C   1 
ATOM   2528 O O   . SER A 1 331 ? -42.403 32.593  -30.642 1.00 77.39  ? 331  SER A O   1 
ATOM   2529 C CB  . SER A 1 331 ? -42.194 30.616  -33.122 1.00 76.37  ? 331  SER A CB  1 
ATOM   2530 O OG  . SER A 1 331 ? -41.249 31.666  -33.233 1.00 91.12  ? 331  SER A OG  1 
ATOM   2531 N N   . PRO A 1 332 ? -42.502 30.518  -29.764 1.00 75.10  ? 332  PRO A N   1 
ATOM   2532 C CA  . PRO A 1 332 ? -42.762 29.060  -29.746 1.00 74.32  ? 332  PRO A CA  1 
ATOM   2533 C C   . PRO A 1 332 ? -44.246 28.699  -29.719 1.00 76.31  ? 332  PRO A C   1 
ATOM   2534 O O   . PRO A 1 332 ? -45.017 29.248  -28.910 1.00 77.85  ? 332  PRO A O   1 
ATOM   2535 C CB  . PRO A 1 332 ? -41.986 28.587  -28.517 1.00 76.06  ? 332  PRO A CB  1 
ATOM   2536 C CG  . PRO A 1 332 ? -42.023 29.778  -27.588 1.00 80.90  ? 332  PRO A CG  1 
ATOM   2537 C CD  . PRO A 1 332 ? -41.958 30.988  -28.473 1.00 76.73  ? 332  PRO A CD  1 
ATOM   2538 N N   . CYS A 1 333 ? -44.658 27.817  -30.647 1.00 68.79  ? 333  CYS A N   1 
ATOM   2539 C CA  . CYS A 1 333 ? -46.055 27.399  -30.761 1.00 67.09  ? 333  CYS A CA  1 
ATOM   2540 C C   . CYS A 1 333 ? -46.211 25.918  -31.191 1.00 64.89  ? 333  CYS A C   1 
ATOM   2541 O O   . CYS A 1 333 ? -45.305 25.358  -31.824 1.00 63.43  ? 333  CYS A O   1 
ATOM   2542 C CB  . CYS A 1 333 ? -46.836 28.354  -31.671 1.00 67.73  ? 333  CYS A CB  1 
ATOM   2543 S SG  . CYS A 1 333 ? -46.192 28.478  -33.365 1.00 72.21  ? 333  CYS A SG  1 
ATOM   2544 N N   . LYS A 1 334 ? -47.373 25.304  -30.854 1.00 57.33  ? 334  LYS A N   1 
ATOM   2545 C CA  . LYS A 1 334 ? -47.709 23.930  -31.246 1.00 55.92  ? 334  LYS A CA  1 
ATOM   2546 C C   . LYS A 1 334 ? -48.097 23.909  -32.755 1.00 58.47  ? 334  LYS A C   1 
ATOM   2547 O O   . LYS A 1 334 ? -49.025 24.640  -33.162 1.00 58.72  ? 334  LYS A O   1 
ATOM   2548 C CB  . LYS A 1 334 ? -48.922 23.401  -30.437 1.00 56.83  ? 334  LYS A CB  1 
ATOM   2549 C CG  . LYS A 1 334 ? -48.751 23.136  -28.959 1.00 47.86  ? 334  LYS A CG  1 
ATOM   2550 C CD  . LYS A 1 334 ? -50.069 22.547  -28.416 1.00 56.67  ? 334  LYS A CD  1 
ATOM   2551 C CE  . LYS A 1 334 ? -50.137 22.421  -26.900 1.00 75.31  ? 334  LYS A CE  1 
ATOM   2552 N NZ  . LYS A 1 334 ? -51.261 21.562  -26.423 1.00 72.39  ? 334  LYS A NZ  1 
ATOM   2553 N N   . ILE A 1 335 ? -47.423 23.062  -33.572 1.00 51.15  ? 335  ILE A N   1 
ATOM   2554 C CA  . ILE A 1 335 ? -47.760 22.920  -34.996 1.00 49.26  ? 335  ILE A CA  1 
ATOM   2555 C C   . ILE A 1 335 ? -49.038 22.099  -35.043 1.00 57.77  ? 335  ILE A C   1 
ATOM   2556 O O   . ILE A 1 335 ? -49.056 21.004  -34.456 1.00 58.47  ? 335  ILE A O   1 
ATOM   2557 C CB  . ILE A 1 335 ? -46.700 22.174  -35.813 1.00 50.84  ? 335  ILE A CB  1 
ATOM   2558 C CG1 . ILE A 1 335 ? -45.290 22.676  -35.587 1.00 52.57  ? 335  ILE A CG1 1 
ATOM   2559 C CG2 . ILE A 1 335 ? -47.047 22.191  -37.255 1.00 49.01  ? 335  ILE A CG2 1 
ATOM   2560 C CD1 . ILE A 1 335 ? -44.205 21.578  -35.609 1.00 60.05  ? 335  ILE A CD1 1 
ATOM   2561 N N   . PRO A 1 336 ? -50.121 22.578  -35.718 1.00 56.20  ? 336  PRO A N   1 
ATOM   2562 C CA  . PRO A 1 336 ? -51.352 21.770  -35.792 1.00 55.27  ? 336  PRO A CA  1 
ATOM   2563 C C   . PRO A 1 336 ? -51.123 20.604  -36.751 1.00 55.74  ? 336  PRO A C   1 
ATOM   2564 O O   . PRO A 1 336 ? -50.565 20.785  -37.837 1.00 55.37  ? 336  PRO A O   1 
ATOM   2565 C CB  . PRO A 1 336 ? -52.415 22.765  -36.299 1.00 56.66  ? 336  PRO A CB  1 
ATOM   2566 C CG  . PRO A 1 336 ? -51.762 24.111  -36.267 1.00 61.13  ? 336  PRO A CG  1 
ATOM   2567 C CD  . PRO A 1 336 ? -50.298 23.851  -36.438 1.00 57.70  ? 336  PRO A CD  1 
ATOM   2568 N N   . PHE A 1 337 ? -51.488 19.403  -36.323 1.00 49.05  ? 337  PHE A N   1 
ATOM   2569 C CA  . PHE A 1 337 ? -51.289 18.228  -37.150 1.00 47.62  ? 337  PHE A CA  1 
ATOM   2570 C C   . PHE A 1 337 ? -52.453 17.286  -37.066 1.00 50.39  ? 337  PHE A C   1 
ATOM   2571 O O   . PHE A 1 337 ? -52.976 17.029  -35.972 1.00 46.91  ? 337  PHE A O   1 
ATOM   2572 C CB  . PHE A 1 337 ? -49.991 17.521  -36.759 1.00 48.93  ? 337  PHE A CB  1 
ATOM   2573 C CG  . PHE A 1 337 ? -49.488 16.515  -37.748 1.00 49.30  ? 337  PHE A CG  1 
ATOM   2574 C CD1 . PHE A 1 337 ? -48.681 16.908  -38.805 1.00 51.56  ? 337  PHE A CD1 1 
ATOM   2575 C CD2 . PHE A 1 337 ? -49.774 15.168  -37.591 1.00 51.78  ? 337  PHE A CD2 1 
ATOM   2576 C CE1 . PHE A 1 337 ? -48.191 15.973  -39.706 1.00 54.70  ? 337  PHE A CE1 1 
ATOM   2577 C CE2 . PHE A 1 337 ? -49.286 14.230  -38.486 1.00 53.23  ? 337  PHE A CE2 1 
ATOM   2578 C CZ  . PHE A 1 337 ? -48.482 14.638  -39.531 1.00 53.06  ? 337  PHE A CZ  1 
ATOM   2579 N N   . GLU A 1 338 ? -52.852 16.755  -38.236 1.00 49.59  ? 338  GLU A N   1 
ATOM   2580 C CA  . GLU A 1 338 ? -53.962 15.826  -38.345 1.00 50.34  ? 338  GLU A CA  1 
ATOM   2581 C C   . GLU A 1 338 ? -53.846 14.896  -39.526 1.00 55.25  ? 338  GLU A C   1 
ATOM   2582 O O   . GLU A 1 338 ? -53.328 15.274  -40.578 1.00 52.30  ? 338  GLU A O   1 
ATOM   2583 C CB  . GLU A 1 338 ? -55.309 16.562  -38.377 1.00 52.09  ? 338  GLU A CB  1 
ATOM   2584 C CG  . GLU A 1 338 ? -56.372 15.814  -37.593 1.00 72.90  ? 338  GLU A CG  1 
ATOM   2585 C CD  . GLU A 1 338 ? -57.293 16.665  -36.735 1.00 117.12 ? 338  GLU A CD  1 
ATOM   2586 O OE1 . GLU A 1 338 ? -56.972 16.867  -35.539 1.00 121.25 ? 338  GLU A OE1 1 
ATOM   2587 O OE2 . GLU A 1 338 ? -58.373 17.062  -37.235 1.00 115.97 ? 338  GLU A OE2 1 
ATOM   2588 N N   . ILE A 1 339 ? -54.360 13.668  -39.337 1.00 54.25  ? 339  ILE A N   1 
ATOM   2589 C CA  . ILE A 1 339 ? -54.440 12.632  -40.366 1.00 53.86  ? 339  ILE A CA  1 
ATOM   2590 C C   . ILE A 1 339 ? -55.917 12.287  -40.379 1.00 59.59  ? 339  ILE A C   1 
ATOM   2591 O O   . ILE A 1 339 ? -56.474 11.890  -39.343 1.00 59.25  ? 339  ILE A O   1 
ATOM   2592 C CB  . ILE A 1 339 ? -53.500 11.408  -40.077 1.00 56.19  ? 339  ILE A CB  1 
ATOM   2593 C CG1 . ILE A 1 339 ? -52.033 11.753  -40.353 1.00 55.66  ? 339  ILE A CG1 1 
ATOM   2594 C CG2 . ILE A 1 339 ? -53.886 10.207  -40.910 1.00 57.17  ? 339  ILE A CG2 1 
ATOM   2595 C CD1 . ILE A 1 339 ? -51.109 11.171  -39.430 1.00 59.63  ? 339  ILE A CD1 1 
ATOM   2596 N N   . THR A 1 340 ? -56.580 12.542  -41.509 1.00 57.18  ? 340  THR A N   1 
ATOM   2597 C CA  . THR A 1 340 ? -58.015 12.240  -41.605 1.00 57.07  ? 340  THR A CA  1 
ATOM   2598 C C   . THR A 1 340 ? -58.303 11.446  -42.833 1.00 61.34  ? 340  THR A C   1 
ATOM   2599 O O   . THR A 1 340 ? -57.457 11.372  -43.724 1.00 61.19  ? 340  THR A O   1 
ATOM   2600 C CB  . THR A 1 340 ? -58.879 13.493  -41.693 1.00 55.84  ? 340  THR A CB  1 
ATOM   2601 O OG1 . THR A 1 340 ? -58.417 14.268  -42.789 1.00 44.23  ? 340  THR A OG1 1 
ATOM   2602 C CG2 . THR A 1 340 ? -58.955 14.268  -40.385 1.00 53.79  ? 340  THR A CG2 1 
ATOM   2603 N N   . ASP A 1 341 ? -59.541 10.923  -42.912 1.00 57.61  ? 341  ASP A N   1 
ATOM   2604 C CA  . ASP A 1 341 ? -60.066 10.210  -44.072 1.00 57.25  ? 341  ASP A CA  1 
ATOM   2605 C C   . ASP A 1 341 ? -60.124 11.222  -45.225 1.00 58.94  ? 341  ASP A C   1 
ATOM   2606 O O   . ASP A 1 341 ? -59.924 12.419  -44.982 1.00 56.95  ? 341  ASP A O   1 
ATOM   2607 C CB  . ASP A 1 341 ? -61.470 9.619   -43.755 1.00 58.98  ? 341  ASP A CB  1 
ATOM   2608 C CG  . ASP A 1 341 ? -62.605 10.617  -43.527 1.00 67.40  ? 341  ASP A CG  1 
ATOM   2609 O OD1 . ASP A 1 341 ? -62.346 11.686  -42.949 1.00 72.29  ? 341  ASP A OD1 1 
ATOM   2610 O OD2 . ASP A 1 341 ? -63.756 10.313  -43.921 1.00 68.19  ? 341  ASP A OD2 1 
ATOM   2611 N N   . LEU A 1 342 ? -60.381 10.759  -46.460 1.00 55.26  ? 342  LEU A N   1 
ATOM   2612 C CA  . LEU A 1 342 ? -60.458 11.677  -47.606 1.00 55.01  ? 342  LEU A CA  1 
ATOM   2613 C C   . LEU A 1 342 ? -61.504 12.762  -47.471 1.00 56.97  ? 342  LEU A C   1 
ATOM   2614 O O   . LEU A 1 342 ? -61.246 13.877  -47.909 1.00 54.98  ? 342  LEU A O   1 
ATOM   2615 C CB  . LEU A 1 342 ? -60.648 10.943  -48.940 1.00 55.10  ? 342  LEU A CB  1 
ATOM   2616 C CG  . LEU A 1 342 ? -59.497 10.075  -49.421 1.00 59.08  ? 342  LEU A CG  1 
ATOM   2617 C CD1 . LEU A 1 342 ? -59.702 9.680   -50.867 1.00 58.80  ? 342  LEU A CD1 1 
ATOM   2618 C CD2 . LEU A 1 342 ? -58.150 10.757  -49.202 1.00 60.26  ? 342  LEU A CD2 1 
ATOM   2619 N N   . GLU A 1 343 ? -62.653 12.443  -46.823 1.00 54.77  ? 343  GLU A N   1 
ATOM   2620 C CA  . GLU A 1 343 ? -63.783 13.350  -46.606 1.00 55.09  ? 343  GLU A CA  1 
ATOM   2621 C C   . GLU A 1 343 ? -63.596 14.305  -45.426 1.00 57.07  ? 343  GLU A C   1 
ATOM   2622 O O   . GLU A 1 343 ? -64.523 15.048  -45.125 1.00 56.60  ? 343  GLU A O   1 
ATOM   2623 C CB  . GLU A 1 343 ? -65.112 12.576  -46.499 1.00 57.30  ? 343  GLU A CB  1 
ATOM   2624 C CG  . GLU A 1 343 ? -65.990 12.704  -47.752 1.00 74.01  ? 343  GLU A CG  1 
ATOM   2625 C CD  . GLU A 1 343 ? -67.440 13.100  -47.502 1.00 115.32 ? 343  GLU A CD  1 
ATOM   2626 O OE1 . GLU A 1 343 ? -67.709 14.307  -47.285 1.00 110.65 ? 343  GLU A OE1 1 
ATOM   2627 O OE2 . GLU A 1 343 ? -68.310 12.197  -47.499 1.00 124.80 ? 343  GLU A OE2 1 
ATOM   2628 N N   . LYS A 1 344 ? -62.374 14.341  -44.827 1.00 53.24  ? 344  LYS A N   1 
ATOM   2629 C CA  . LYS A 1 344 ? -61.902 15.186  -43.714 1.00 52.20  ? 344  LYS A CA  1 
ATOM   2630 C C   . LYS A 1 344 ? -62.947 15.271  -42.580 1.00 56.85  ? 344  LYS A C   1 
ATOM   2631 O O   . LYS A 1 344 ? -63.406 16.361  -42.224 1.00 57.90  ? 344  LYS A O   1 
ATOM   2632 C CB  . LYS A 1 344 ? -61.455 16.557  -44.263 1.00 54.09  ? 344  LYS A CB  1 
ATOM   2633 C CG  . LYS A 1 344 ? -60.612 17.401  -43.286 1.00 77.81  ? 344  LYS A CG  1 
ATOM   2634 C CD  . LYS A 1 344 ? -60.236 18.800  -43.851 1.00 88.98  ? 344  LYS A CD  1 
ATOM   2635 C CE  . LYS A 1 344 ? -60.333 19.929  -42.831 1.00 89.75  ? 344  LYS A CE  1 
ATOM   2636 N NZ  . LYS A 1 344 ? -59.792 21.224  -43.359 1.00 87.41  ? 344  LYS A NZ  1 
ATOM   2637 N N   . ARG A 1 345 ? -63.366 14.084  -42.069 1.00 52.54  ? 345  ARG A N   1 
ATOM   2638 C CA  . ARG A 1 345 ? -64.431 13.844  -41.067 1.00 51.71  ? 345  ARG A CA  1 
ATOM   2639 C C   . ARG A 1 345 ? -63.949 12.956  -39.909 1.00 56.01  ? 345  ARG A C   1 
ATOM   2640 O O   . ARG A 1 345 ? -64.283 13.215  -38.742 1.00 56.03  ? 345  ARG A O   1 
ATOM   2641 C CB  . ARG A 1 345 ? -65.659 13.200  -41.765 1.00 50.67  ? 345  ARG A CB  1 
ATOM   2642 C CG  . ARG A 1 345 ? -66.702 12.561  -40.840 1.00 59.57  ? 345  ARG A CG  1 
ATOM   2643 C CD  . ARG A 1 345 ? -67.825 11.846  -41.563 1.00 71.76  ? 345  ARG A CD  1 
ATOM   2644 N NE  . ARG A 1 345 ? -68.641 12.737  -42.391 1.00 87.48  ? 345  ARG A NE  1 
ATOM   2645 C CZ  . ARG A 1 345 ? -68.930 12.511  -43.670 1.00 107.85 ? 345  ARG A CZ  1 
ATOM   2646 N NH1 . ARG A 1 345 ? -68.466 11.425  -44.283 1.00 95.56  ? 345  ARG A NH1 1 
ATOM   2647 N NH2 . ARG A 1 345 ? -69.683 13.371  -44.349 1.00 96.30  ? 345  ARG A NH2 1 
ATOM   2648 N N   . HIS A 1 346 ? -63.170 11.911  -40.245 1.00 52.29  ? 346  HIS A N   1 
ATOM   2649 C CA  . HIS A 1 346 ? -62.613 10.967  -39.288 1.00 51.71  ? 346  HIS A CA  1 
ATOM   2650 C C   . HIS A 1 346 ? -61.162 11.179  -38.979 1.00 57.63  ? 346  HIS A C   1 
ATOM   2651 O O   . HIS A 1 346 ? -60.330 11.237  -39.886 1.00 57.14  ? 346  HIS A O   1 
ATOM   2652 C CB  . HIS A 1 346 ? -62.827 9.540   -39.764 1.00 51.74  ? 346  HIS A CB  1 
ATOM   2653 C CG  . HIS A 1 346 ? -64.244 9.131   -39.606 1.00 54.72  ? 346  HIS A CG  1 
ATOM   2654 N ND1 . HIS A 1 346 ? -65.195 9.432   -40.568 1.00 56.34  ? 346  HIS A ND1 1 
ATOM   2655 C CD2 . HIS A 1 346 ? -64.855 8.584   -38.543 1.00 55.49  ? 346  HIS A CD2 1 
ATOM   2656 C CE1 . HIS A 1 346 ? -66.333 8.973   -40.092 1.00 55.24  ? 346  HIS A CE1 1 
ATOM   2657 N NE2 . HIS A 1 346 ? -66.181 8.475   -38.872 1.00 55.48  ? 346  HIS A NE2 1 
ATOM   2658 N N   . VAL A 1 347 ? -60.844 11.260  -37.675 1.00 55.11  ? 347  VAL A N   1 
ATOM   2659 C CA  . VAL A 1 347 ? -59.449 11.359  -37.245 1.00 53.90  ? 347  VAL A CA  1 
ATOM   2660 C C   . VAL A 1 347 ? -58.894 9.943   -37.267 1.00 56.83  ? 347  VAL A C   1 
ATOM   2661 O O   . VAL A 1 347 ? -59.508 9.014   -36.714 1.00 56.28  ? 347  VAL A O   1 
ATOM   2662 C CB  . VAL A 1 347 ? -59.187 12.103  -35.921 1.00 56.11  ? 347  VAL A CB  1 
ATOM   2663 C CG1 . VAL A 1 347 ? -57.690 12.146  -35.633 1.00 56.15  ? 347  VAL A CG1 1 
ATOM   2664 C CG2 . VAL A 1 347 ? -59.727 13.516  -35.998 1.00 55.52  ? 347  VAL A CG2 1 
ATOM   2665 N N   . LEU A 1 348 ? -57.778 9.789   -37.990 1.00 51.14  ? 348  LEU A N   1 
ATOM   2666 C CA  . LEU A 1 348 ? -57.144 8.516   -38.218 1.00 50.31  ? 348  LEU A CA  1 
ATOM   2667 C C   . LEU A 1 348 ? -55.661 8.529   -37.895 1.00 57.26  ? 348  LEU A C   1 
ATOM   2668 O O   . LEU A 1 348 ? -55.052 9.606   -37.824 1.00 56.54  ? 348  LEU A O   1 
ATOM   2669 C CB  . LEU A 1 348 ? -57.364 8.130   -39.688 1.00 49.48  ? 348  LEU A CB  1 
ATOM   2670 C CG  . LEU A 1 348 ? -58.789 7.813   -40.158 1.00 50.89  ? 348  LEU A CG  1 
ATOM   2671 C CD1 . LEU A 1 348 ? -58.869 7.902   -41.662 1.00 49.44  ? 348  LEU A CD1 1 
ATOM   2672 C CD2 . LEU A 1 348 ? -59.239 6.441   -39.680 1.00 49.90  ? 348  LEU A CD2 1 
ATOM   2673 N N   . GLY A 1 349 ? -55.106 7.323   -37.696 1.00 56.92  ? 349  GLY A N   1 
ATOM   2674 C CA  . GLY A 1 349 ? -53.703 7.089   -37.378 1.00 58.52  ? 349  GLY A CA  1 
ATOM   2675 C C   . GLY A 1 349 ? -53.224 7.838   -36.142 1.00 67.53  ? 349  GLY A C   1 
ATOM   2676 O O   . GLY A 1 349 ? -54.000 8.540   -35.487 1.00 70.17  ? 349  GLY A O   1 
ATOM   2677 N N   . ARG A 1 350 ? -51.932 7.738   -35.825 1.00 62.52  ? 350  ARG A N   1 
ATOM   2678 C CA  . ARG A 1 350 ? -51.375 8.373   -34.631 1.00 60.13  ? 350  ARG A CA  1 
ATOM   2679 C C   . ARG A 1 350 ? -50.102 9.177   -34.915 1.00 58.81  ? 350  ARG A C   1 
ATOM   2680 O O   . ARG A 1 350 ? -49.525 9.051   -35.995 1.00 59.16  ? 350  ARG A O   1 
ATOM   2681 C CB  . ARG A 1 350 ? -51.168 7.324   -33.511 1.00 59.42  ? 350  ARG A CB  1 
ATOM   2682 C CG  . ARG A 1 350 ? -50.100 6.270   -33.752 1.00 65.61  ? 350  ARG A CG  1 
ATOM   2683 C CD  . ARG A 1 350 ? -49.759 5.578   -32.437 1.00 88.54  ? 350  ARG A CD  1 
ATOM   2684 N NE  . ARG A 1 350 ? -48.738 4.538   -32.608 1.00 113.00 ? 350  ARG A NE  1 
ATOM   2685 C CZ  . ARG A 1 350 ? -48.988 3.231   -32.693 1.00 131.08 ? 350  ARG A CZ  1 
ATOM   2686 N NH1 . ARG A 1 350 ? -50.231 2.778   -32.597 1.00 119.24 ? 350  ARG A NH1 1 
ATOM   2687 N NH2 . ARG A 1 350 ? -47.995 2.369   -32.860 1.00 115.88 ? 350  ARG A NH2 1 
ATOM   2688 N N   . LEU A 1 351 ? -49.670 9.998   -33.953 1.00 50.83  ? 351  LEU A N   1 
ATOM   2689 C CA  . LEU A 1 351 ? -48.483 10.826  -34.070 1.00 48.87  ? 351  LEU A CA  1 
ATOM   2690 C C   . LEU A 1 351 ? -47.299 10.238  -33.252 1.00 53.60  ? 351  LEU A C   1 
ATOM   2691 O O   . LEU A 1 351 ? -47.392 10.137  -32.032 1.00 55.19  ? 351  LEU A O   1 
ATOM   2692 C CB  . LEU A 1 351 ? -48.823 12.218  -33.541 1.00 48.04  ? 351  LEU A CB  1 
ATOM   2693 C CG  . LEU A 1 351 ? -48.639 13.377  -34.472 1.00 52.86  ? 351  LEU A CG  1 
ATOM   2694 C CD1 . LEU A 1 351 ? -48.750 14.646  -33.725 1.00 53.08  ? 351  LEU A CD1 1 
ATOM   2695 C CD2 . LEU A 1 351 ? -47.264 13.381  -35.134 1.00 57.03  ? 351  LEU A CD2 1 
ATOM   2696 N N   . ILE A 1 352 ? -46.183 9.882   -33.900 1.00 47.27  ? 352  ILE A N   1 
ATOM   2697 C CA  . ILE A 1 352 ? -45.029 9.374   -33.166 1.00 45.72  ? 352  ILE A CA  1 
ATOM   2698 C C   . ILE A 1 352 ? -44.350 10.570  -32.487 1.00 52.18  ? 352  ILE A C   1 
ATOM   2699 O O   . ILE A 1 352 ? -44.264 10.569  -31.259 1.00 53.43  ? 352  ILE A O   1 
ATOM   2700 C CB  . ILE A 1 352 ? -44.072 8.522   -34.026 1.00 47.03  ? 352  ILE A CB  1 
ATOM   2701 C CG1 . ILE A 1 352 ? -44.829 7.418   -34.844 1.00 45.38  ? 352  ILE A CG1 1 
ATOM   2702 C CG2 . ILE A 1 352 ? -42.923 7.950   -33.170 1.00 46.68  ? 352  ILE A CG2 1 
ATOM   2703 C CD1 . ILE A 1 352 ? -45.477 6.288   -34.104 1.00 35.54  ? 352  ILE A CD1 1 
ATOM   2704 N N   . THR A 1 353 ? -43.952 11.619  -33.268 1.00 47.04  ? 353  THR A N   1 
ATOM   2705 C CA  . THR A 1 353 ? -43.363 12.864  -32.748 1.00 45.55  ? 353  THR A CA  1 
ATOM   2706 C C   . THR A 1 353 ? -44.510 13.684  -32.101 1.00 49.11  ? 353  THR A C   1 
ATOM   2707 O O   . THR A 1 353 ? -44.955 14.691  -32.666 1.00 48.59  ? 353  THR A O   1 
ATOM   2708 C CB  . THR A 1 353 ? -42.647 13.650  -33.874 1.00 50.43  ? 353  THR A CB  1 
ATOM   2709 O OG1 . THR A 1 353 ? -41.946 12.752  -34.748 1.00 53.80  ? 353  THR A OG1 1 
ATOM   2710 C CG2 . THR A 1 353 ? -41.711 14.742  -33.340 1.00 45.14  ? 353  THR A CG2 1 
ATOM   2711 N N   . VAL A 1 354 ? -44.986 13.229  -30.913 1.00 45.52  ? 354  VAL A N   1 
ATOM   2712 C CA  . VAL A 1 354 ? -46.080 13.853  -30.150 1.00 44.71  ? 354  VAL A CA  1 
ATOM   2713 C C   . VAL A 1 354 ? -45.782 15.312  -29.815 1.00 48.45  ? 354  VAL A C   1 
ATOM   2714 O O   . VAL A 1 354 ? -44.608 15.654  -29.538 1.00 45.93  ? 354  VAL A O   1 
ATOM   2715 C CB  . VAL A 1 354 ? -46.559 13.080  -28.884 1.00 46.72  ? 354  VAL A CB  1 
ATOM   2716 C CG1 . VAL A 1 354 ? -46.932 11.645  -29.211 1.00 45.81  ? 354  VAL A CG1 1 
ATOM   2717 C CG2 . VAL A 1 354 ? -45.536 13.143  -27.755 1.00 46.75  ? 354  VAL A CG2 1 
ATOM   2718 N N   . ASN A 1 355 ? -46.881 16.147  -29.824 1.00 44.48  ? 355  ASN A N   1 
ATOM   2719 C CA  . ASN A 1 355 ? -46.919 17.582  -29.531 1.00 44.16  ? 355  ASN A CA  1 
ATOM   2720 C C   . ASN A 1 355 ? -45.870 18.338  -30.352 1.00 53.94  ? 355  ASN A C   1 
ATOM   2721 O O   . ASN A 1 355 ? -44.967 18.946  -29.754 1.00 54.79  ? 355  ASN A O   1 
ATOM   2722 C CB  . ASN A 1 355 ? -46.757 17.843  -28.026 1.00 39.16  ? 355  ASN A CB  1 
ATOM   2723 C CG  . ASN A 1 355 ? -47.257 19.202  -27.618 1.00 64.97  ? 355  ASN A CG  1 
ATOM   2724 O OD1 . ASN A 1 355 ? -48.466 19.466  -27.609 1.00 59.30  ? 355  ASN A OD1 1 
ATOM   2725 N ND2 . ASN A 1 355 ? -46.339 20.104  -27.284 1.00 57.89  ? 355  ASN A ND2 1 
ATOM   2726 N N   . PRO A 1 356 ? -45.915 18.266  -31.718 1.00 53.38  ? 356  PRO A N   1 
ATOM   2727 C CA  . PRO A 1 356 ? -44.866 18.937  -32.523 1.00 54.47  ? 356  PRO A CA  1 
ATOM   2728 C C   . PRO A 1 356 ? -44.883 20.431  -32.308 1.00 62.57  ? 356  PRO A C   1 
ATOM   2729 O O   . PRO A 1 356 ? -45.969 21.035  -32.333 1.00 64.21  ? 356  PRO A O   1 
ATOM   2730 C CB  . PRO A 1 356 ? -45.194 18.537  -33.963 1.00 55.96  ? 356  PRO A CB  1 
ATOM   2731 C CG  . PRO A 1 356 ? -46.627 18.162  -33.939 1.00 59.56  ? 356  PRO A CG  1 
ATOM   2732 C CD  . PRO A 1 356 ? -46.896 17.580  -32.582 1.00 54.81  ? 356  PRO A CD  1 
ATOM   2733 N N   . ILE A 1 357 ? -43.714 21.009  -31.991 1.00 59.47  ? 357  ILE A N   1 
ATOM   2734 C CA  . ILE A 1 357 ? -43.642 22.441  -31.694 1.00 59.61  ? 357  ILE A CA  1 
ATOM   2735 C C   . ILE A 1 357 ? -42.597 23.198  -32.544 1.00 66.39  ? 357  ILE A C   1 
ATOM   2736 O O   . ILE A 1 357 ? -41.650 22.601  -33.052 1.00 64.31  ? 357  ILE A O   1 
ATOM   2737 C CB  . ILE A 1 357 ? -43.444 22.703  -30.166 1.00 61.63  ? 357  ILE A CB  1 
ATOM   2738 C CG1 . ILE A 1 357 ? -42.086 22.210  -29.675 1.00 62.00  ? 357  ILE A CG1 1 
ATOM   2739 C CG2 . ILE A 1 357 ? -44.590 22.152  -29.317 1.00 60.90  ? 357  ILE A CG2 1 
ATOM   2740 C CD1 . ILE A 1 357 ? -41.395 23.218  -28.754 1.00 74.46  ? 357  ILE A CD1 1 
ATOM   2741 N N   . VAL A 1 358 ? -42.792 24.520  -32.693 1.00 67.48  ? 358  VAL A N   1 
ATOM   2742 C CA  . VAL A 1 358 ? -41.831 25.404  -33.349 1.00 69.26  ? 358  VAL A CA  1 
ATOM   2743 C C   . VAL A 1 358 ? -41.132 26.126  -32.189 1.00 76.52  ? 358  VAL A C   1 
ATOM   2744 O O   . VAL A 1 358 ? -41.772 26.475  -31.191 1.00 74.89  ? 358  VAL A O   1 
ATOM   2745 C CB  . VAL A 1 358 ? -42.437 26.414  -34.355 1.00 73.40  ? 358  VAL A CB  1 
ATOM   2746 C CG1 . VAL A 1 358 ? -41.333 27.130  -35.140 1.00 72.86  ? 358  VAL A CG1 1 
ATOM   2747 C CG2 . VAL A 1 358 ? -43.403 25.727  -35.315 1.00 73.56  ? 358  VAL A CG2 1 
ATOM   2748 N N   . THR A 1 359 ? -39.813 26.287  -32.297 1.00 76.59  ? 359  THR A N   1 
ATOM   2749 C CA  . THR A 1 359 ? -38.983 26.962  -31.303 1.00 77.26  ? 359  THR A CA  1 
ATOM   2750 C C   . THR A 1 359 ? -38.451 28.266  -31.931 1.00 83.32  ? 359  THR A C   1 
ATOM   2751 O O   . THR A 1 359 ? -38.481 29.317  -31.284 1.00 81.66  ? 359  THR A O   1 
ATOM   2752 C CB  . THR A 1 359 ? -37.946 25.955  -30.786 1.00 82.05  ? 359  THR A CB  1 
ATOM   2753 O OG1 . THR A 1 359 ? -38.611 25.130  -29.834 1.00 76.65  ? 359  THR A OG1 1 
ATOM   2754 C CG2 . THR A 1 359 ? -36.687 26.615  -30.175 1.00 81.40  ? 359  THR A CG2 1 
ATOM   2755 N N   . GLU A 1 360 ? -38.011 28.166  -33.219 1.00 82.80  ? 360  GLU A N   1 
ATOM   2756 C CA  . GLU A 1 360 ? -37.503 29.232  -34.082 1.00 84.01  ? 360  GLU A CA  1 
ATOM   2757 C C   . GLU A 1 360 ? -38.053 29.004  -35.493 1.00 89.72  ? 360  GLU A C   1 
ATOM   2758 O O   . GLU A 1 360 ? -38.051 27.859  -35.971 1.00 89.52  ? 360  GLU A O   1 
ATOM   2759 C CB  . GLU A 1 360 ? -35.967 29.209  -34.139 1.00 85.67  ? 360  GLU A CB  1 
ATOM   2760 C CG  . GLU A 1 360 ? -35.277 29.525  -32.827 1.00 99.06  ? 360  GLU A CG  1 
ATOM   2761 C CD  . GLU A 1 360 ? -33.986 28.757  -32.651 1.00 131.56 ? 360  GLU A CD  1 
ATOM   2762 O OE1 . GLU A 1 360 ? -33.095 28.881  -33.526 1.00 129.83 ? 360  GLU A OE1 1 
ATOM   2763 O OE2 . GLU A 1 360 ? -33.880 28.002  -31.656 1.00 133.59 ? 360  GLU A OE2 1 
ATOM   2764 N N   . LYS A 1 361 ? -38.493 30.094  -36.164 1.00 87.18  ? 361  LYS A N   1 
ATOM   2765 C CA  . LYS A 1 361 ? -39.030 30.066  -37.530 1.00 87.92  ? 361  LYS A CA  1 
ATOM   2766 C C   . LYS A 1 361 ? -37.980 29.540  -38.510 1.00 94.27  ? 361  LYS A C   1 
ATOM   2767 O O   . LYS A 1 361 ? -38.315 28.772  -39.419 1.00 94.17  ? 361  LYS A O   1 
ATOM   2768 C CB  . LYS A 1 361 ? -39.495 31.470  -37.964 1.00 90.58  ? 361  LYS A CB  1 
ATOM   2769 C CG  . LYS A 1 361 ? -40.991 31.739  -37.831 1.00 105.65 ? 361  LYS A CG  1 
ATOM   2770 C CD  . LYS A 1 361 ? -41.420 32.270  -36.441 1.00 119.25 ? 361  LYS A CD  1 
ATOM   2771 C CE  . LYS A 1 361 ? -41.203 33.753  -36.209 1.00 128.29 ? 361  LYS A CE  1 
ATOM   2772 N NZ  . LYS A 1 361 ? -41.735 34.200  -34.894 1.00 129.28 ? 361  LYS A NZ  1 
ATOM   2773 N N   . ASP A 1 362 ? -36.712 29.946  -38.300 1.00 92.72  ? 362  ASP A N   1 
ATOM   2774 C CA  . ASP A 1 362 ? -35.547 29.566  -39.105 1.00 94.07  ? 362  ASP A CA  1 
ATOM   2775 C C   . ASP A 1 362 ? -35.300 28.048  -39.148 1.00 97.88  ? 362  ASP A C   1 
ATOM   2776 O O   . ASP A 1 362 ? -34.996 27.500  -40.214 1.00 98.08  ? 362  ASP A O   1 
ATOM   2777 C CB  . ASP A 1 362 ? -34.283 30.292  -38.590 1.00 97.00  ? 362  ASP A CB  1 
ATOM   2778 C CG  . ASP A 1 362 ? -34.273 31.808  -38.794 1.00 116.98 ? 362  ASP A CG  1 
ATOM   2779 O OD1 . ASP A 1 362 ? -35.355 32.383  -39.127 1.00 118.72 ? 362  ASP A OD1 1 
ATOM   2780 O OD2 . ASP A 1 362 ? -33.184 32.423  -38.626 1.00 123.48 ? 362  ASP A OD2 1 
ATOM   2781 N N   . SER A 1 363 ? -35.431 27.383  -37.984 1.00 92.86  ? 363  SER A N   1 
ATOM   2782 C CA  . SER A 1 363 ? -35.200 25.952  -37.821 1.00 91.28  ? 363  SER A CA  1 
ATOM   2783 C C   . SER A 1 363 ? -36.418 25.098  -38.257 1.00 89.51  ? 363  SER A C   1 
ATOM   2784 O O   . SER A 1 363 ? -37.461 25.138  -37.573 1.00 90.12  ? 363  SER A O   1 
ATOM   2785 C CB  . SER A 1 363 ? -34.801 25.645  -36.374 1.00 96.43  ? 363  SER A CB  1 
ATOM   2786 O OG  . SER A 1 363 ? -34.591 24.256  -36.151 1.00 108.39 ? 363  SER A OG  1 
ATOM   2787 N N   . PRO A 1 364 ? -36.293 24.292  -39.359 1.00 79.09  ? 364  PRO A N   1 
ATOM   2788 C CA  . PRO A 1 364 ? -37.404 23.419  -39.766 1.00 76.54  ? 364  PRO A CA  1 
ATOM   2789 C C   . PRO A 1 364 ? -37.635 22.305  -38.754 1.00 73.51  ? 364  PRO A C   1 
ATOM   2790 O O   . PRO A 1 364 ? -36.811 22.088  -37.870 1.00 72.34  ? 364  PRO A O   1 
ATOM   2791 C CB  . PRO A 1 364 ? -36.968 22.868  -41.132 1.00 78.34  ? 364  PRO A CB  1 
ATOM   2792 C CG  . PRO A 1 364 ? -35.823 23.674  -41.534 1.00 83.41  ? 364  PRO A CG  1 
ATOM   2793 C CD  . PRO A 1 364 ? -35.159 24.138  -40.280 1.00 79.35  ? 364  PRO A CD  1 
ATOM   2794 N N   . VAL A 1 365 ? -38.784 21.642  -38.861 1.00 65.43  ? 365  VAL A N   1 
ATOM   2795 C CA  . VAL A 1 365 ? -39.203 20.595  -37.952 1.00 63.17  ? 365  VAL A CA  1 
ATOM   2796 C C   . VAL A 1 365 ? -39.445 19.284  -38.711 1.00 64.61  ? 365  VAL A C   1 
ATOM   2797 O O   . VAL A 1 365 ? -39.936 19.289  -39.836 1.00 63.63  ? 365  VAL A O   1 
ATOM   2798 C CB  . VAL A 1 365 ? -40.451 21.043  -37.115 1.00 65.96  ? 365  VAL A CB  1 
ATOM   2799 C CG1 . VAL A 1 365 ? -40.997 19.909  -36.234 1.00 65.30  ? 365  VAL A CG1 1 
ATOM   2800 C CG2 . VAL A 1 365 ? -40.168 22.293  -36.278 1.00 65.39  ? 365  VAL A CG2 1 
ATOM   2801 N N   . ASN A 1 366 ? -39.136 18.169  -38.052 1.00 59.43  ? 366  ASN A N   1 
ATOM   2802 C CA  . ASN A 1 366 ? -39.342 16.826  -38.547 1.00 58.64  ? 366  ASN A CA  1 
ATOM   2803 C C   . ASN A 1 366 ? -40.451 16.135  -37.749 1.00 61.91  ? 366  ASN A C   1 
ATOM   2804 O O   . ASN A 1 366 ? -40.386 16.061  -36.514 1.00 62.07  ? 366  ASN A O   1 
ATOM   2805 C CB  . ASN A 1 366 ? -38.063 16.037  -38.450 1.00 58.49  ? 366  ASN A CB  1 
ATOM   2806 C CG  . ASN A 1 366 ? -37.041 16.478  -39.432 1.00 75.24  ? 366  ASN A CG  1 
ATOM   2807 O OD1 . ASN A 1 366 ? -37.092 16.125  -40.615 1.00 72.33  ? 366  ASN A OD1 1 
ATOM   2808 N ND2 . ASN A 1 366 ? -36.100 17.255  -38.960 1.00 61.80  ? 366  ASN A ND2 1 
ATOM   2809 N N   . ILE A 1 367 ? -41.476 15.640  -38.449 1.00 55.36  ? 367  ILE A N   1 
ATOM   2810 C CA  . ILE A 1 367 ? -42.595 14.977  -37.802 1.00 52.75  ? 367  ILE A CA  1 
ATOM   2811 C C   . ILE A 1 367 ? -42.726 13.572  -38.339 1.00 54.56  ? 367  ILE A C   1 
ATOM   2812 O O   . ILE A 1 367 ? -42.729 13.365  -39.552 1.00 53.45  ? 367  ILE A O   1 
ATOM   2813 C CB  . ILE A 1 367 ? -43.924 15.781  -37.914 1.00 55.39  ? 367  ILE A CB  1 
ATOM   2814 C CG1 . ILE A 1 367 ? -43.788 17.212  -37.396 1.00 54.54  ? 367  ILE A CG1 1 
ATOM   2815 C CG2 . ILE A 1 367 ? -45.079 15.075  -37.180 1.00 58.65  ? 367  ILE A CG2 1 
ATOM   2816 C CD1 . ILE A 1 367 ? -43.967 18.197  -38.424 1.00 56.83  ? 367  ILE A CD1 1 
ATOM   2817 N N   . GLU A 1 368 ? -42.830 12.606  -37.417 1.00 50.51  ? 368  GLU A N   1 
ATOM   2818 C CA  . GLU A 1 368 ? -43.054 11.204  -37.737 1.00 49.89  ? 368  GLU A CA  1 
ATOM   2819 C C   . GLU A 1 368 ? -44.423 10.836  -37.238 1.00 49.85  ? 368  GLU A C   1 
ATOM   2820 O O   . GLU A 1 368 ? -44.738 11.050  -36.062 1.00 46.46  ? 368  GLU A O   1 
ATOM   2821 C CB  . GLU A 1 368 ? -41.996 10.279  -37.110 1.00 51.84  ? 368  GLU A CB  1 
ATOM   2822 C CG  . GLU A 1 368 ? -42.090 8.837   -37.613 1.00 64.72  ? 368  GLU A CG  1 
ATOM   2823 C CD  . GLU A 1 368 ? -41.137 7.801   -37.035 1.00 88.86  ? 368  GLU A CD  1 
ATOM   2824 O OE1 . GLU A 1 368 ? -40.849 7.847   -35.818 1.00 79.19  ? 368  GLU A OE1 1 
ATOM   2825 O OE2 . GLU A 1 368 ? -40.710 6.907   -37.797 1.00 90.18  ? 368  GLU A OE2 1 
ATOM   2826 N N   . ALA A 1 369 ? -45.233 10.265  -38.146 1.00 46.39  ? 369  ALA A N   1 
ATOM   2827 C CA  . ALA A 1 369 ? -46.596 9.807   -37.853 1.00 45.68  ? 369  ALA A CA  1 
ATOM   2828 C C   . ALA A 1 369 ? -46.890 8.494   -38.538 1.00 46.85  ? 369  ALA A C   1 
ATOM   2829 O O   . ALA A 1 369 ? -46.296 8.197   -39.575 1.00 44.67  ? 369  ALA A O   1 
ATOM   2830 C CB  . ALA A 1 369 ? -47.611 10.850  -38.291 1.00 46.61  ? 369  ALA A CB  1 
ATOM   2831 N N   . GLU A 1 370 ? -47.813 7.724   -37.957 1.00 45.13  ? 370  GLU A N   1 
ATOM   2832 C CA  . GLU A 1 370 ? -48.271 6.452   -38.502 1.00 47.44  ? 370  GLU A CA  1 
ATOM   2833 C C   . GLU A 1 370 ? -49.592 6.688   -39.285 1.00 54.94  ? 370  GLU A C   1 
ATOM   2834 O O   . GLU A 1 370 ? -50.656 6.844   -38.654 1.00 54.81  ? 370  GLU A O   1 
ATOM   2835 C CB  . GLU A 1 370 ? -48.468 5.383   -37.392 1.00 48.94  ? 370  GLU A CB  1 
ATOM   2836 C CG  . GLU A 1 370 ? -48.797 3.992   -37.920 1.00 55.13  ? 370  GLU A CG  1 
ATOM   2837 C CD  . GLU A 1 370 ? -48.223 2.856   -37.097 1.00 86.48  ? 370  GLU A CD  1 
ATOM   2838 O OE1 . GLU A 1 370 ? -48.226 2.950   -35.844 1.00 87.92  ? 370  GLU A OE1 1 
ATOM   2839 O OE2 . GLU A 1 370 ? -47.767 1.865   -37.713 1.00 82.71  ? 370  GLU A OE2 1 
ATOM   2840 N N   . PRO A 1 371 ? -49.548 6.716   -40.650 1.00 50.94  ? 371  PRO A N   1 
ATOM   2841 C CA  . PRO A 1 371 ? -50.790 6.897   -41.408 1.00 50.08  ? 371  PRO A CA  1 
ATOM   2842 C C   . PRO A 1 371 ? -51.666 5.639   -41.375 1.00 54.99  ? 371  PRO A C   1 
ATOM   2843 O O   . PRO A 1 371 ? -51.123 4.549   -41.187 1.00 54.12  ? 371  PRO A O   1 
ATOM   2844 C CB  . PRO A 1 371 ? -50.293 7.189   -42.823 1.00 51.29  ? 371  PRO A CB  1 
ATOM   2845 C CG  . PRO A 1 371 ? -48.999 6.510   -42.913 1.00 56.05  ? 371  PRO A CG  1 
ATOM   2846 C CD  . PRO A 1 371 ? -48.389 6.550   -41.551 1.00 51.95  ? 371  PRO A CD  1 
ATOM   2847 N N   . PRO A 1 372 ? -53.007 5.741   -41.573 1.00 53.32  ? 372  PRO A N   1 
ATOM   2848 C CA  . PRO A 1 372 ? -53.828 4.527   -41.643 1.00 53.59  ? 372  PRO A CA  1 
ATOM   2849 C C   . PRO A 1 372 ? -53.666 3.797   -42.978 1.00 60.51  ? 372  PRO A C   1 
ATOM   2850 O O   . PRO A 1 372 ? -53.235 4.394   -43.982 1.00 61.10  ? 372  PRO A O   1 
ATOM   2851 C CB  . PRO A 1 372 ? -55.245 5.073   -41.520 1.00 54.99  ? 372  PRO A CB  1 
ATOM   2852 C CG  . PRO A 1 372 ? -55.183 6.395   -42.150 1.00 59.11  ? 372  PRO A CG  1 
ATOM   2853 C CD  . PRO A 1 372 ? -53.837 6.945   -41.794 1.00 54.80  ? 372  PRO A CD  1 
ATOM   2854 N N   . PHE A 1 373 ? -54.030 2.504   -42.991 1.00 58.29  ? 373  PHE A N   1 
ATOM   2855 C CA  . PHE A 1 373 ? -53.978 1.686   -44.197 1.00 58.08  ? 373  PHE A CA  1 
ATOM   2856 C C   . PHE A 1 373 ? -54.959 2.209   -45.217 1.00 59.97  ? 373  PHE A C   1 
ATOM   2857 O O   . PHE A 1 373 ? -56.147 2.286   -44.952 1.00 60.17  ? 373  PHE A O   1 
ATOM   2858 C CB  . PHE A 1 373 ? -54.194 0.189   -43.895 1.00 60.31  ? 373  PHE A CB  1 
ATOM   2859 C CG  . PHE A 1 373 ? -52.903 -0.501  -43.512 1.00 62.37  ? 373  PHE A CG  1 
ATOM   2860 C CD1 . PHE A 1 373 ? -51.957 -0.828  -44.481 1.00 66.49  ? 373  PHE A CD1 1 
ATOM   2861 C CD2 . PHE A 1 373 ? -52.603 -0.767  -42.178 1.00 63.73  ? 373  PHE A CD2 1 
ATOM   2862 C CE1 . PHE A 1 373 ? -50.728 -1.389  -44.119 1.00 67.44  ? 373  PHE A CE1 1 
ATOM   2863 C CE2 . PHE A 1 373 ? -51.372 -1.318  -41.818 1.00 66.37  ? 373  PHE A CE2 1 
ATOM   2864 C CZ  . PHE A 1 373 ? -50.450 -1.639  -42.790 1.00 65.33  ? 373  PHE A CZ  1 
ATOM   2865 N N   . GLY A 1 374 ? -54.436 2.625   -46.348 1.00 55.13  ? 374  GLY A N   1 
ATOM   2866 C CA  . GLY A 1 374 ? -55.223 3.164   -47.437 1.00 54.27  ? 374  GLY A CA  1 
ATOM   2867 C C   . GLY A 1 374 ? -55.037 4.651   -47.573 1.00 56.37  ? 374  GLY A C   1 
ATOM   2868 O O   . GLY A 1 374 ? -53.998 5.206   -47.168 1.00 54.05  ? 374  GLY A O   1 
ATOM   2869 N N   . ASP A 1 375 ? -56.077 5.301   -48.127 1.00 52.83  ? 375  ASP A N   1 
ATOM   2870 C CA  . ASP A 1 375 ? -56.048 6.735   -48.353 1.00 52.26  ? 375  ASP A CA  1 
ATOM   2871 C C   . ASP A 1 375 ? -56.369 7.537   -47.099 1.00 55.79  ? 375  ASP A C   1 
ATOM   2872 O O   . ASP A 1 375 ? -57.252 7.169   -46.304 1.00 54.16  ? 375  ASP A O   1 
ATOM   2873 C CB  . ASP A 1 375 ? -56.921 7.168   -49.537 1.00 53.60  ? 375  ASP A CB  1 
ATOM   2874 C CG  . ASP A 1 375 ? -56.389 6.765   -50.895 1.00 66.16  ? 375  ASP A CG  1 
ATOM   2875 O OD1 . ASP A 1 375 ? -55.328 7.295   -51.307 1.00 68.72  ? 375  ASP A OD1 1 
ATOM   2876 O OD2 . ASP A 1 375 ? -57.061 5.965   -51.575 1.00 69.69  ? 375  ASP A OD2 1 
ATOM   2877 N N   . SER A 1 376 ? -55.582 8.621   -46.917 1.00 50.78  ? 376  SER A N   1 
ATOM   2878 C CA  . SER A 1 376 ? -55.708 9.582   -45.836 1.00 48.70  ? 376  SER A CA  1 
ATOM   2879 C C   . SER A 1 376 ? -55.224 10.941  -46.320 1.00 50.17  ? 376  SER A C   1 
ATOM   2880 O O   . SER A 1 376 ? -54.695 11.053  -47.429 1.00 48.24  ? 376  SER A O   1 
ATOM   2881 C CB  . SER A 1 376 ? -54.924 9.123   -44.611 1.00 49.68  ? 376  SER A CB  1 
ATOM   2882 O OG  . SER A 1 376 ? -53.600 8.722   -44.916 1.00 52.00  ? 376  SER A OG  1 
ATOM   2883 N N   . TYR A 1 377 ? -55.466 11.971  -45.507 1.00 46.92  ? 377  TYR A N   1 
ATOM   2884 C CA  . TYR A 1 377 ? -55.014 13.334  -45.723 1.00 47.01  ? 377  TYR A CA  1 
ATOM   2885 C C   . TYR A 1 377 ? -54.122 13.742  -44.561 1.00 50.07  ? 377  TYR A C   1 
ATOM   2886 O O   . TYR A 1 377 ? -54.531 13.675  -43.388 1.00 50.65  ? 377  TYR A O   1 
ATOM   2887 C CB  . TYR A 1 377 ? -56.176 14.330  -45.835 1.00 48.85  ? 377  TYR A CB  1 
ATOM   2888 C CG  . TYR A 1 377 ? -56.624 14.621  -47.250 1.00 54.22  ? 377  TYR A CG  1 
ATOM   2889 C CD1 . TYR A 1 377 ? -55.822 15.357  -48.125 1.00 55.74  ? 377  TYR A CD1 1 
ATOM   2890 C CD2 . TYR A 1 377 ? -57.870 14.201  -47.708 1.00 57.33  ? 377  TYR A CD2 1 
ATOM   2891 C CE1 . TYR A 1 377 ? -56.230 15.622  -49.433 1.00 56.56  ? 377  TYR A CE1 1 
ATOM   2892 C CE2 . TYR A 1 377 ? -58.301 14.488  -49.003 1.00 59.00  ? 377  TYR A CE2 1 
ATOM   2893 C CZ  . TYR A 1 377 ? -57.485 15.211  -49.856 1.00 66.68  ? 377  TYR A CZ  1 
ATOM   2894 O OH  . TYR A 1 377 ? -57.927 15.490  -51.128 1.00 72.71  ? 377  TYR A OH  1 
ATOM   2895 N N   . ILE A 1 378 ? -52.893 14.114  -44.874 1.00 43.60  ? 378  ILE A N   1 
ATOM   2896 C CA  . ILE A 1 378 ? -51.987 14.630  -43.868 1.00 42.47  ? 378  ILE A CA  1 
ATOM   2897 C C   . ILE A 1 378 ? -52.148 16.140  -43.901 1.00 48.85  ? 378  ILE A C   1 
ATOM   2898 O O   . ILE A 1 378 ? -51.784 16.802  -44.873 1.00 48.03  ? 378  ILE A O   1 
ATOM   2899 C CB  . ILE A 1 378 ? -50.541 14.141  -44.007 1.00 43.74  ? 378  ILE A CB  1 
ATOM   2900 C CG1 . ILE A 1 378 ? -50.490 12.648  -43.689 1.00 43.73  ? 378  ILE A CG1 1 
ATOM   2901 C CG2 . ILE A 1 378 ? -49.605 14.935  -43.070 1.00 41.03  ? 378  ILE A CG2 1 
ATOM   2902 C CD1 . ILE A 1 378 ? -49.568 11.907  -44.508 1.00 54.20  ? 378  ILE A CD1 1 
ATOM   2903 N N   . ILE A 1 379 ? -52.751 16.655  -42.845 1.00 47.04  ? 379  ILE A N   1 
ATOM   2904 C CA  . ILE A 1 379 ? -53.055 18.060  -42.678 1.00 47.83  ? 379  ILE A CA  1 
ATOM   2905 C C   . ILE A 1 379 ? -52.140 18.695  -41.600 1.00 54.66  ? 379  ILE A C   1 
ATOM   2906 O O   . ILE A 1 379 ? -52.256 18.464  -40.383 1.00 53.97  ? 379  ILE A O   1 
ATOM   2907 C CB  . ILE A 1 379 ? -54.592 18.263  -42.442 1.00 50.81  ? 379  ILE A CB  1 
ATOM   2908 C CG1 . ILE A 1 379 ? -55.428 17.771  -43.659 1.00 49.51  ? 379  ILE A CG1 1 
ATOM   2909 C CG2 . ILE A 1 379 ? -54.932 19.715  -42.079 1.00 52.66  ? 379  ILE A CG2 1 
ATOM   2910 C CD1 . ILE A 1 379 ? -56.702 17.052  -43.301 1.00 38.60  ? 379  ILE A CD1 1 
ATOM   2911 N N   . VAL A 1 380 ? -51.214 19.491  -42.083 1.00 53.98  ? 380  VAL A N   1 
ATOM   2912 C CA  . VAL A 1 380 ? -50.295 20.200  -41.224 1.00 54.88  ? 380  VAL A CA  1 
ATOM   2913 C C   . VAL A 1 380 ? -50.554 21.702  -41.340 1.00 59.67  ? 380  VAL A C   1 
ATOM   2914 O O   . VAL A 1 380 ? -50.540 22.286  -42.422 1.00 56.46  ? 380  VAL A O   1 
ATOM   2915 C CB  . VAL A 1 380 ? -48.824 19.773  -41.397 1.00 59.51  ? 380  VAL A CB  1 
ATOM   2916 C CG1 . VAL A 1 380 ? -48.390 19.767  -42.857 1.00 59.61  ? 380  VAL A CG1 1 
ATOM   2917 C CG2 . VAL A 1 380 ? -47.889 20.616  -40.537 1.00 59.52  ? 380  VAL A CG2 1 
ATOM   2918 N N   . GLY A 1 381 ? -50.844 22.282  -40.195 1.00 60.20  ? 381  GLY A N   1 
ATOM   2919 C CA  . GLY A 1 381 ? -51.130 23.690  -40.068 1.00 61.70  ? 381  GLY A CA  1 
ATOM   2920 C C   . GLY A 1 381 ? -52.600 23.979  -40.021 1.00 69.84  ? 381  GLY A C   1 
ATOM   2921 O O   . GLY A 1 381 ? -53.427 23.058  -39.945 1.00 70.80  ? 381  GLY A O   1 
ATOM   2922 N N   . VAL A 1 382 ? -52.911 25.280  -40.047 1.00 67.94  ? 382  VAL A N   1 
ATOM   2923 C CA  . VAL A 1 382 ? -54.254 25.816  -39.989 1.00 68.53  ? 382  VAL A CA  1 
ATOM   2924 C C   . VAL A 1 382 ? -54.480 26.760  -41.167 1.00 77.58  ? 382  VAL A C   1 
ATOM   2925 O O   . VAL A 1 382 ? -53.509 27.341  -41.683 1.00 77.63  ? 382  VAL A O   1 
ATOM   2926 C CB  . VAL A 1 382 ? -54.523 26.412  -38.579 1.00 70.95  ? 382  VAL A CB  1 
ATOM   2927 C CG1 . VAL A 1 382 ? -55.094 27.826  -38.593 1.00 70.82  ? 382  VAL A CG1 1 
ATOM   2928 C CG2 . VAL A 1 382 ? -55.393 25.470  -37.779 1.00 70.20  ? 382  VAL A CG2 1 
ATOM   2929 N N   . GLU A 1 383 ? -55.767 26.838  -41.624 1.00 76.66  ? 383  GLU A N   1 
ATOM   2930 C CA  . GLU A 1 383 ? -56.269 27.658  -42.738 1.00 76.92  ? 383  GLU A CA  1 
ATOM   2931 C C   . GLU A 1 383 ? -56.136 29.167  -42.444 1.00 82.77  ? 383  GLU A C   1 
ATOM   2932 O O   . GLU A 1 383 ? -56.462 29.569  -41.321 1.00 83.12  ? 383  GLU A O   1 
ATOM   2933 C CB  . GLU A 1 383 ? -57.731 27.280  -43.082 1.00 77.69  ? 383  GLU A CB  1 
ATOM   2934 C CG  . GLU A 1 383 ? -57.858 26.264  -44.206 1.00 80.50  ? 383  GLU A CG  1 
ATOM   2935 C CD  . GLU A 1 383 ? -57.439 26.769  -45.575 1.00 102.38 ? 383  GLU A CD  1 
ATOM   2936 O OE1 . GLU A 1 383 ? -58.265 27.456  -46.215 1.00 118.19 ? 383  GLU A OE1 1 
ATOM   2937 O OE2 . GLU A 1 383 ? -56.289 26.507  -46.000 1.00 84.38  ? 383  GLU A OE2 1 
ATOM   2938 N N   . PRO A 1 384 ? -55.669 30.031  -43.395 1.00 79.06  ? 384  PRO A N   1 
ATOM   2939 C CA  . PRO A 1 384 ? -55.227 29.763  -44.789 1.00 78.29  ? 384  PRO A CA  1 
ATOM   2940 C C   . PRO A 1 384 ? -53.810 29.201  -44.842 1.00 80.18  ? 384  PRO A C   1 
ATOM   2941 O O   . PRO A 1 384 ? -53.109 29.237  -43.831 1.00 82.32  ? 384  PRO A O   1 
ATOM   2942 C CB  . PRO A 1 384 ? -55.263 31.156  -45.425 1.00 80.25  ? 384  PRO A CB  1 
ATOM   2943 C CG  . PRO A 1 384 ? -54.902 32.075  -44.296 1.00 84.75  ? 384  PRO A CG  1 
ATOM   2944 C CD  . PRO A 1 384 ? -55.537 31.466  -43.063 1.00 80.48  ? 384  PRO A CD  1 
ATOM   2945 N N   . GLY A 1 385 ? -53.378 28.739  -46.008 1.00 72.35  ? 385  GLY A N   1 
ATOM   2946 C CA  . GLY A 1 385 ? -52.044 28.163  -46.150 1.00 70.60  ? 385  GLY A CA  1 
ATOM   2947 C C   . GLY A 1 385 ? -51.888 26.813  -45.465 1.00 71.03  ? 385  GLY A C   1 
ATOM   2948 O O   . GLY A 1 385 ? -50.764 26.317  -45.310 1.00 72.56  ? 385  GLY A O   1 
ATOM   2949 N N   . GLN A 1 386 ? -53.036 26.210  -45.053 1.00 61.40  ? 386  GLN A N   1 
ATOM   2950 C CA  . GLN A 1 386 ? -53.145 24.897  -44.445 1.00 57.75  ? 386  GLN A CA  1 
ATOM   2951 C C   . GLN A 1 386 ? -52.625 23.952  -45.488 1.00 61.96  ? 386  GLN A C   1 
ATOM   2952 O O   . GLN A 1 386 ? -53.039 24.066  -46.648 1.00 62.54  ? 386  GLN A O   1 
ATOM   2953 C CB  . GLN A 1 386 ? -54.616 24.578  -44.191 1.00 56.92  ? 386  GLN A CB  1 
ATOM   2954 C CG  . GLN A 1 386 ? -54.849 23.472  -43.208 1.00 45.74  ? 386  GLN A CG  1 
ATOM   2955 C CD  . GLN A 1 386 ? -56.222 22.852  -43.321 1.00 65.61  ? 386  GLN A CD  1 
ATOM   2956 O OE1 . GLN A 1 386 ? -56.726 22.559  -44.405 1.00 66.60  ? 386  GLN A OE1 1 
ATOM   2957 N NE2 . GLN A 1 386 ? -56.842 22.559  -42.196 1.00 52.14  ? 386  GLN A NE2 1 
ATOM   2958 N N   . LEU A 1 387 ? -51.658 23.089  -45.110 1.00 58.16  ? 387  LEU A N   1 
ATOM   2959 C CA  . LEU A 1 387 ? -51.079 22.061  -45.980 1.00 57.36  ? 387  LEU A CA  1 
ATOM   2960 C C   . LEU A 1 387 ? -51.982 20.813  -45.906 1.00 64.20  ? 387  LEU A C   1 
ATOM   2961 O O   . LEU A 1 387 ? -52.315 20.341  -44.814 1.00 62.54  ? 387  LEU A O   1 
ATOM   2962 C CB  . LEU A 1 387 ? -49.622 21.739  -45.631 1.00 56.25  ? 387  LEU A CB  1 
ATOM   2963 C CG  . LEU A 1 387 ? -48.601 22.853  -45.829 1.00 60.39  ? 387  LEU A CG  1 
ATOM   2964 C CD1 . LEU A 1 387 ? -47.251 22.453  -45.263 1.00 61.13  ? 387  LEU A CD1 1 
ATOM   2965 C CD2 . LEU A 1 387 ? -48.406 23.163  -47.284 1.00 62.59  ? 387  LEU A CD2 1 
ATOM   2966 N N   . LYS A 1 388 ? -52.481 20.371  -47.072 1.00 63.46  ? 388  LYS A N   1 
ATOM   2967 C CA  . LYS A 1 388 ? -53.396 19.236  -47.163 1.00 63.78  ? 388  LYS A CA  1 
ATOM   2968 C C   . LYS A 1 388 ? -52.772 18.190  -48.106 1.00 69.31  ? 388  LYS A C   1 
ATOM   2969 O O   . LYS A 1 388 ? -53.072 18.143  -49.297 1.00 69.19  ? 388  LYS A O   1 
ATOM   2970 C CB  . LYS A 1 388 ? -54.803 19.682  -47.624 1.00 65.27  ? 388  LYS A CB  1 
ATOM   2971 C CG  . LYS A 1 388 ? -55.325 20.982  -46.997 1.00 79.21  ? 388  LYS A CG  1 
ATOM   2972 C CD  . LYS A 1 388 ? -56.394 21.655  -47.868 1.00 97.29  ? 388  LYS A CD  1 
ATOM   2973 C CE  . LYS A 1 388 ? -56.685 23.104  -47.531 1.00 116.49 ? 388  LYS A CE  1 
ATOM   2974 N NZ  . LYS A 1 388 ? -55.631 24.048  -48.003 1.00 130.12 ? 388  LYS A NZ  1 
ATOM   2975 N N   . LEU A 1 389 ? -51.856 17.391  -47.557 1.00 66.25  ? 389  LEU A N   1 
ATOM   2976 C CA  . LEU A 1 389 ? -51.131 16.336  -48.268 1.00 66.05  ? 389  LEU A CA  1 
ATOM   2977 C C   . LEU A 1 389 ? -51.933 15.044  -48.289 1.00 67.76  ? 389  LEU A C   1 
ATOM   2978 O O   . LEU A 1 389 ? -52.733 14.800  -47.399 1.00 66.51  ? 389  LEU A O   1 
ATOM   2979 C CB  . LEU A 1 389 ? -49.739 16.119  -47.650 1.00 66.24  ? 389  LEU A CB  1 
ATOM   2980 C CG  . LEU A 1 389 ? -48.841 17.373  -47.635 1.00 70.86  ? 389  LEU A CG  1 
ATOM   2981 C CD1 . LEU A 1 389 ? -47.827 17.337  -46.487 1.00 69.66  ? 389  LEU A CD1 1 
ATOM   2982 C CD2 . LEU A 1 389 ? -48.175 17.598  -48.997 1.00 73.57  ? 389  LEU A CD2 1 
ATOM   2983 N N   . ASN A 1 390 ? -51.738 14.236  -49.325 1.00 63.06  ? 390  ASN A N   1 
ATOM   2984 C CA  . ASN A 1 390 ? -52.467 12.991  -49.529 1.00 62.17  ? 390  ASN A CA  1 
ATOM   2985 C C   . ASN A 1 390 ? -51.542 11.807  -49.471 1.00 64.27  ? 390  ASN A C   1 
ATOM   2986 O O   . ASN A 1 390 ? -50.475 11.813  -50.095 1.00 64.68  ? 390  ASN A O   1 
ATOM   2987 C CB  . ASN A 1 390 ? -53.204 13.015  -50.857 1.00 64.41  ? 390  ASN A CB  1 
ATOM   2988 C CG  . ASN A 1 390 ? -52.548 13.845  -51.933 1.00 112.79 ? 390  ASN A CG  1 
ATOM   2989 O OD1 . ASN A 1 390 ? -51.309 13.948  -52.033 1.00 108.92 ? 390  ASN A OD1 1 
ATOM   2990 N ND2 . ASN A 1 390 ? -53.381 14.486  -52.745 1.00 113.52 ? 390  ASN A ND2 1 
ATOM   2991 N N   . TRP A 1 391 ? -51.963 10.778  -48.734 1.00 58.05  ? 391  TRP A N   1 
ATOM   2992 C CA  . TRP A 1 391 ? -51.168 9.589   -48.546 1.00 56.43  ? 391  TRP A CA  1 
ATOM   2993 C C   . TRP A 1 391 ? -51.908 8.303   -48.853 1.00 62.32  ? 391  TRP A C   1 
ATOM   2994 O O   . TRP A 1 391 ? -53.126 8.217   -48.671 1.00 63.37  ? 391  TRP A O   1 
ATOM   2995 C CB  . TRP A 1 391 ? -50.581 9.552   -47.111 1.00 53.77  ? 391  TRP A CB  1 
ATOM   2996 C CG  . TRP A 1 391 ? -49.424 8.602   -46.969 1.00 53.66  ? 391  TRP A CG  1 
ATOM   2997 C CD1 . TRP A 1 391 ? -49.414 7.399   -46.321 1.00 56.21  ? 391  TRP A CD1 1 
ATOM   2998 C CD2 . TRP A 1 391 ? -48.166 8.704   -47.642 1.00 52.91  ? 391  TRP A CD2 1 
ATOM   2999 N NE1 . TRP A 1 391 ? -48.201 6.775   -46.501 1.00 55.06  ? 391  TRP A NE1 1 
ATOM   3000 C CE2 . TRP A 1 391 ? -47.439 7.531   -47.353 1.00 56.34  ? 391  TRP A CE2 1 
ATOM   3001 C CE3 . TRP A 1 391 ? -47.598 9.663   -48.496 1.00 53.47  ? 391  TRP A CE3 1 
ATOM   3002 C CZ2 . TRP A 1 391 ? -46.172 7.304   -47.876 1.00 55.54  ? 391  TRP A CZ2 1 
ATOM   3003 C CZ3 . TRP A 1 391 ? -46.342 9.434   -49.008 1.00 54.46  ? 391  TRP A CZ3 1 
ATOM   3004 C CH2 . TRP A 1 391 ? -45.630 8.287   -48.671 1.00 55.13  ? 391  TRP A CH2 1 
ATOM   3005 N N   . LEU A 1 392 ? -51.136 7.302   -49.275 1.00 58.74  ? 392  LEU A N   1 
ATOM   3006 C CA  . LEU A 1 392 ? -51.627 5.970   -49.527 1.00 59.06  ? 392  LEU A CA  1 
ATOM   3007 C C   . LEU A 1 392 ? -50.762 4.943   -48.793 1.00 67.88  ? 392  LEU A C   1 
ATOM   3008 O O   . LEU A 1 392 ? -49.538 5.016   -48.867 1.00 68.56  ? 392  LEU A O   1 
ATOM   3009 C CB  . LEU A 1 392 ? -51.631 5.715   -51.019 1.00 58.08  ? 392  LEU A CB  1 
ATOM   3010 C CG  . LEU A 1 392 ? -52.167 4.397   -51.427 1.00 61.07  ? 392  LEU A CG  1 
ATOM   3011 C CD1 . LEU A 1 392 ? -53.662 4.333   -51.215 1.00 61.12  ? 392  LEU A CD1 1 
ATOM   3012 C CD2 . LEU A 1 392 ? -51.813 4.129   -52.823 1.00 62.25  ? 392  LEU A CD2 1 
ATOM   3013 N N   . ARG A 1 393 ? -51.385 4.019   -48.059 1.00 67.19  ? 393  ARG A N   1 
ATOM   3014 C CA  . ARG A 1 393 ? -50.638 2.983   -47.353 1.00 68.88  ? 393  ARG A CA  1 
ATOM   3015 C C   . ARG A 1 393 ? -51.281 1.676   -47.736 1.00 78.48  ? 393  ARG A C   1 
ATOM   3016 O O   . ARG A 1 393 ? -52.281 1.273   -47.149 1.00 79.16  ? 393  ARG A O   1 
ATOM   3017 C CB  . ARG A 1 393 ? -50.627 3.198   -45.827 1.00 68.64  ? 393  ARG A CB  1 
ATOM   3018 C CG  . ARG A 1 393 ? -49.741 2.211   -45.088 1.00 70.98  ? 393  ARG A CG  1 
ATOM   3019 C CD  . ARG A 1 393 ? -49.937 2.265   -43.590 1.00 77.67  ? 393  ARG A CD  1 
ATOM   3020 N NE  . ARG A 1 393 ? -48.972 1.382   -42.932 1.00 86.99  ? 393  ARG A NE  1 
ATOM   3021 C CZ  . ARG A 1 393 ? -48.918 1.130   -41.626 1.00 86.20  ? 393  ARG A CZ  1 
ATOM   3022 N NH1 . ARG A 1 393 ? -49.798 1.682   -40.798 1.00 72.68  ? 393  ARG A NH1 1 
ATOM   3023 N NH2 . ARG A 1 393 ? -48.002 0.301   -41.141 1.00 55.43  ? 393  ARG A NH2 1 
ATOM   3024 N N   . PRO A 1 394 ? -50.783 1.016   -48.784 1.00 78.53  ? 394  PRO A N   1 
ATOM   3025 C CA  . PRO A 1 394 ? -51.450 -0.231  -49.218 1.00 78.75  ? 394  PRO A CA  1 
ATOM   3026 C C   . PRO A 1 394 ? -51.336 -1.378  -48.218 1.00 83.77  ? 394  PRO A C   1 
ATOM   3027 O O   . PRO A 1 394 ? -50.434 -1.360  -47.368 1.00 84.03  ? 394  PRO A O   1 
ATOM   3028 C CB  . PRO A 1 394 ? -50.770 -0.552  -50.542 1.00 80.75  ? 394  PRO A CB  1 
ATOM   3029 C CG  . PRO A 1 394 ? -49.415 0.141   -50.454 1.00 85.67  ? 394  PRO A CG  1 
ATOM   3030 C CD  . PRO A 1 394 ? -49.620 1.368   -49.633 1.00 80.88  ? 394  PRO A CD  1 
ATOM   3031 N N   . LEU A 1 395 ? -52.242 -2.374  -48.324 1.00 80.32  ? 395  LEU A N   1 
ATOM   3032 C CA  . LEU A 1 395 ? -52.238 -3.543  -47.437 1.00 115.00 ? 395  LEU A CA  1 
ATOM   3033 C C   . LEU A 1 395 ? -51.299 -4.652  -47.950 1.00 151.66 ? 395  LEU A C   1 
ATOM   3034 O O   . LEU A 1 395 ? -50.125 -4.714  -47.568 1.00 112.85 ? 395  LEU A O   1 
ATOM   3035 C CB  . LEU A 1 395 ? -53.662 -4.079  -47.243 1.00 114.94 ? 395  LEU A CB  1 
ATOM   3036 N N   . MET B 1 1   ? 28.211  -55.170 -47.512 1.00 73.93  ? 1    MET B N   1 
ATOM   3037 C CA  . MET B 1 1   ? 28.972  -54.616 -46.394 1.00 74.66  ? 1    MET B CA  1 
ATOM   3038 C C   . MET B 1 1   ? 28.317  -53.359 -45.807 1.00 79.55  ? 1    MET B C   1 
ATOM   3039 O O   . MET B 1 1   ? 28.832  -52.793 -44.841 1.00 77.15  ? 1    MET B O   1 
ATOM   3040 C CB  . MET B 1 1   ? 30.420  -54.352 -46.802 1.00 77.60  ? 1    MET B CB  1 
ATOM   3041 C CG  . MET B 1 1   ? 31.056  -55.507 -47.593 1.00 82.31  ? 1    MET B CG  1 
ATOM   3042 S SD  . MET B 1 1   ? 32.242  -56.518 -46.667 1.00 86.96  ? 1    MET B SD  1 
ATOM   3043 C CE  . MET B 1 1   ? 33.584  -55.299 -46.397 1.00 82.61  ? 1    MET B CE  1 
ATOM   3044 N N   . ARG B 1 2   ? 27.164  -52.940 -46.403 1.00 78.99  ? 2    ARG B N   1 
ATOM   3045 C CA  . ARG B 1 2   ? 26.333  -51.799 -45.987 1.00 79.25  ? 2    ARG B CA  1 
ATOM   3046 C C   . ARG B 1 2   ? 25.656  -52.121 -44.662 1.00 80.76  ? 2    ARG B C   1 
ATOM   3047 O O   . ARG B 1 2   ? 25.654  -51.282 -43.771 1.00 78.69  ? 2    ARG B O   1 
ATOM   3048 C CB  . ARG B 1 2   ? 25.227  -51.520 -47.024 1.00 84.08  ? 2    ARG B CB  1 
ATOM   3049 C CG  . ARG B 1 2   ? 25.679  -50.828 -48.297 1.00 109.15 ? 2    ARG B CG  1 
ATOM   3050 C CD  . ARG B 1 2   ? 24.511  -50.612 -49.267 1.00 131.30 ? 2    ARG B CD  1 
ATOM   3051 N NE  . ARG B 1 2   ? 24.555  -49.266 -49.853 1.00 143.55 ? 2    ARG B NE  1 
ATOM   3052 C CZ  . ARG B 1 2   ? 23.711  -48.283 -49.550 1.00 152.11 ? 2    ARG B CZ  1 
ATOM   3053 N NH1 . ARG B 1 2   ? 22.716  -48.493 -48.697 1.00 140.21 ? 2    ARG B NH1 1 
ATOM   3054 N NH2 . ARG B 1 2   ? 23.851  -47.085 -50.106 1.00 131.82 ? 2    ARG B NH2 1 
ATOM   3055 N N   . CYS B 1 3   ? 25.085  -53.345 -44.549 1.00 77.72  ? 3    CYS B N   1 
ATOM   3056 C CA  . CYS B 1 3   ? 24.367  -53.875 -43.399 1.00 78.22  ? 3    CYS B CA  1 
ATOM   3057 C C   . CYS B 1 3   ? 25.150  -53.817 -42.103 1.00 78.87  ? 3    CYS B C   1 
ATOM   3058 O O   . CYS B 1 3   ? 24.534  -53.738 -41.036 1.00 79.53  ? 3    CYS B O   1 
ATOM   3059 C CB  . CYS B 1 3   ? 23.875  -55.288 -43.671 1.00 80.60  ? 3    CYS B CB  1 
ATOM   3060 S SG  . CYS B 1 3   ? 22.841  -55.452 -45.144 1.00 86.24  ? 3    CYS B SG  1 
ATOM   3061 N N   . ILE B 1 4   ? 26.488  -53.911 -42.177 1.00 70.90  ? 4    ILE B N   1 
ATOM   3062 C CA  . ILE B 1 4   ? 27.334  -53.857 -40.995 1.00 69.07  ? 4    ILE B CA  1 
ATOM   3063 C C   . ILE B 1 4   ? 27.172  -52.459 -40.353 1.00 73.77  ? 4    ILE B C   1 
ATOM   3064 O O   . ILE B 1 4   ? 27.627  -51.454 -40.912 1.00 72.71  ? 4    ILE B O   1 
ATOM   3065 C CB  . ILE B 1 4   ? 28.807  -54.202 -41.340 1.00 71.20  ? 4    ILE B CB  1 
ATOM   3066 C CG1 . ILE B 1 4   ? 28.920  -55.527 -42.111 1.00 70.75  ? 4    ILE B CG1 1 
ATOM   3067 C CG2 . ILE B 1 4   ? 29.692  -54.190 -40.085 1.00 70.62  ? 4    ILE B CG2 1 
ATOM   3068 C CD1 . ILE B 1 4   ? 30.254  -55.678 -42.890 1.00 77.76  ? 4    ILE B CD1 1 
ATOM   3069 N N   . GLY B 1 5   ? 26.478  -52.418 -39.217 1.00 71.94  ? 5    GLY B N   1 
ATOM   3070 C CA  . GLY B 1 5   ? 26.204  -51.181 -38.484 1.00 72.07  ? 5    GLY B CA  1 
ATOM   3071 C C   . GLY B 1 5   ? 24.726  -50.900 -38.278 1.00 75.99  ? 5    GLY B C   1 
ATOM   3072 O O   . GLY B 1 5   ? 24.361  -50.225 -37.309 1.00 76.67  ? 5    GLY B O   1 
ATOM   3073 N N   . ILE B 1 6   ? 23.877  -51.431 -39.201 1.00 70.76  ? 6    ILE B N   1 
ATOM   3074 C CA  . ILE B 1 6   ? 22.418  -51.331 -39.246 1.00 70.33  ? 6    ILE B CA  1 
ATOM   3075 C C   . ILE B 1 6   ? 21.820  -52.355 -38.272 1.00 78.44  ? 6    ILE B C   1 
ATOM   3076 O O   . ILE B 1 6   ? 22.044  -53.563 -38.425 1.00 80.46  ? 6    ILE B O   1 
ATOM   3077 C CB  . ILE B 1 6   ? 21.862  -51.497 -40.715 1.00 72.20  ? 6    ILE B CB  1 
ATOM   3078 C CG1 . ILE B 1 6   ? 22.209  -50.271 -41.588 1.00 71.90  ? 6    ILE B CG1 1 
ATOM   3079 C CG2 . ILE B 1 6   ? 20.344  -51.795 -40.765 1.00 71.83  ? 6    ILE B CG2 1 
ATOM   3080 C CD1 . ILE B 1 6   ? 22.062  -50.473 -43.092 1.00 75.61  ? 6    ILE B CD1 1 
ATOM   3081 N N   . SER B 1 7   ? 21.023  -51.862 -37.301 1.00 74.13  ? 7    SER B N   1 
ATOM   3082 C CA  . SER B 1 7   ? 20.357  -52.681 -36.298 1.00 72.68  ? 7    SER B CA  1 
ATOM   3083 C C   . SER B 1 7   ? 19.216  -53.516 -36.879 1.00 73.52  ? 7    SER B C   1 
ATOM   3084 O O   . SER B 1 7   ? 19.070  -54.664 -36.484 1.00 73.35  ? 7    SER B O   1 
ATOM   3085 C CB  . SER B 1 7   ? 19.872  -51.813 -35.148 1.00 76.14  ? 7    SER B CB  1 
ATOM   3086 O OG  . SER B 1 7   ? 19.014  -50.807 -35.653 1.00 85.92  ? 7    SER B OG  1 
ATOM   3087 N N   . ASN B 1 8   ? 18.408  -52.972 -37.797 1.00 69.18  ? 8    ASN B N   1 
ATOM   3088 C CA  . ASN B 1 8   ? 17.321  -53.780 -38.360 1.00 69.26  ? 8    ASN B CA  1 
ATOM   3089 C C   . ASN B 1 8   ? 17.829  -54.584 -39.545 1.00 73.84  ? 8    ASN B C   1 
ATOM   3090 O O   . ASN B 1 8   ? 17.571  -54.259 -40.701 1.00 73.18  ? 8    ASN B O   1 
ATOM   3091 C CB  . ASN B 1 8   ? 16.068  -52.953 -38.686 1.00 71.46  ? 8    ASN B CB  1 
ATOM   3092 C CG  . ASN B 1 8   ? 14.888  -53.806 -39.118 1.00 95.78  ? 8    ASN B CG  1 
ATOM   3093 O OD1 . ASN B 1 8   ? 14.722  -54.969 -38.694 1.00 95.46  ? 8    ASN B OD1 1 
ATOM   3094 N ND2 . ASN B 1 8   ? 14.052  -53.253 -39.987 1.00 80.86  ? 8    ASN B ND2 1 
ATOM   3095 N N   . ARG B 1 9   ? 18.571  -55.649 -39.236 1.00 72.00  ? 9    ARG B N   1 
ATOM   3096 C CA  . ARG B 1 9   ? 19.256  -56.499 -40.209 1.00 71.46  ? 9    ARG B CA  1 
ATOM   3097 C C   . ARG B 1 9   ? 18.925  -57.979 -40.066 1.00 74.90  ? 9    ARG B C   1 
ATOM   3098 O O   . ARG B 1 9   ? 18.900  -58.489 -38.948 1.00 75.58  ? 9    ARG B O   1 
ATOM   3099 C CB  . ARG B 1 9   ? 20.762  -56.266 -40.051 1.00 68.59  ? 9    ARG B CB  1 
ATOM   3100 C CG  . ARG B 1 9   ? 21.614  -57.014 -41.032 1.00 75.26  ? 9    ARG B CG  1 
ATOM   3101 C CD  . ARG B 1 9   ? 22.974  -57.158 -40.428 1.00 70.99  ? 9    ARG B CD  1 
ATOM   3102 N NE  . ARG B 1 9   ? 23.898  -57.773 -41.363 1.00 54.41  ? 9    ARG B NE  1 
ATOM   3103 C CZ  . ARG B 1 9   ? 25.203  -57.776 -41.190 1.00 65.85  ? 9    ARG B CZ  1 
ATOM   3104 N NH1 . ARG B 1 9   ? 25.731  -57.244 -40.097 1.00 48.12  ? 9    ARG B NH1 1 
ATOM   3105 N NH2 . ARG B 1 9   ? 25.994  -58.345 -42.088 1.00 68.27  ? 9    ARG B NH2 1 
ATOM   3106 N N   . ASP B 1 10  ? 18.710  -58.667 -41.190 1.00 70.73  ? 10   ASP B N   1 
ATOM   3107 C CA  . ASP B 1 10  ? 18.405  -60.092 -41.209 1.00 71.75  ? 10   ASP B CA  1 
ATOM   3108 C C   . ASP B 1 10  ? 19.504  -60.882 -41.918 1.00 78.42  ? 10   ASP B C   1 
ATOM   3109 O O   . ASP B 1 10  ? 20.074  -60.397 -42.904 1.00 79.78  ? 10   ASP B O   1 
ATOM   3110 C CB  . ASP B 1 10  ? 17.053  -60.355 -41.880 1.00 74.12  ? 10   ASP B CB  1 
ATOM   3111 C CG  . ASP B 1 10  ? 15.887  -59.531 -41.355 1.00 99.16  ? 10   ASP B CG  1 
ATOM   3112 O OD1 . ASP B 1 10  ? 15.724  -59.444 -40.112 1.00 101.91 ? 10   ASP B OD1 1 
ATOM   3113 O OD2 . ASP B 1 10  ? 15.098  -59.026 -42.183 1.00 113.20 ? 10   ASP B OD2 1 
ATOM   3114 N N   . PHE B 1 11  ? 19.785  -62.109 -41.421 1.00 73.31  ? 11   PHE B N   1 
ATOM   3115 C CA  . PHE B 1 11  ? 20.790  -63.000 -41.996 1.00 72.20  ? 11   PHE B CA  1 
ATOM   3116 C C   . PHE B 1 11  ? 20.070  -64.179 -42.615 1.00 79.99  ? 11   PHE B C   1 
ATOM   3117 O O   . PHE B 1 11  ? 19.833  -65.187 -41.953 1.00 79.83  ? 11   PHE B O   1 
ATOM   3118 C CB  . PHE B 1 11  ? 21.801  -63.455 -40.949 1.00 72.85  ? 11   PHE B CB  1 
ATOM   3119 C CG  . PHE B 1 11  ? 22.596  -62.344 -40.323 1.00 73.66  ? 11   PHE B CG  1 
ATOM   3120 C CD1 . PHE B 1 11  ? 22.044  -61.546 -39.320 1.00 75.12  ? 11   PHE B CD1 1 
ATOM   3121 C CD2 . PHE B 1 11  ? 23.905  -62.105 -40.714 1.00 76.23  ? 11   PHE B CD2 1 
ATOM   3122 C CE1 . PHE B 1 11  ? 22.778  -60.509 -38.739 1.00 77.95  ? 11   PHE B CE1 1 
ATOM   3123 C CE2 . PHE B 1 11  ? 24.646  -61.084 -40.122 1.00 77.32  ? 11   PHE B CE2 1 
ATOM   3124 C CZ  . PHE B 1 11  ? 24.079  -60.295 -39.129 1.00 76.46  ? 11   PHE B CZ  1 
ATOM   3125 N N   . VAL B 1 12  ? 19.690  -64.032 -43.889 1.00 79.52  ? 12   VAL B N   1 
ATOM   3126 C CA  . VAL B 1 12  ? 18.988  -65.055 -44.666 1.00 79.71  ? 12   VAL B CA  1 
ATOM   3127 C C   . VAL B 1 12  ? 19.989  -66.044 -45.302 1.00 82.15  ? 12   VAL B C   1 
ATOM   3128 O O   . VAL B 1 12  ? 20.806  -65.638 -46.120 1.00 79.92  ? 12   VAL B O   1 
ATOM   3129 C CB  . VAL B 1 12  ? 18.063  -64.406 -45.740 1.00 84.05  ? 12   VAL B CB  1 
ATOM   3130 C CG1 . VAL B 1 12  ? 17.356  -65.468 -46.576 1.00 83.74  ? 12   VAL B CG1 1 
ATOM   3131 C CG2 . VAL B 1 12  ? 17.049  -63.454 -45.112 1.00 83.81  ? 12   VAL B CG2 1 
ATOM   3132 N N   . GLU B 1 13  ? 19.901  -67.328 -44.941 1.00 80.67  ? 13   GLU B N   1 
ATOM   3133 C CA  . GLU B 1 13  ? 20.750  -68.353 -45.539 1.00 81.48  ? 13   GLU B CA  1 
ATOM   3134 C C   . GLU B 1 13  ? 19.911  -69.320 -46.371 1.00 85.95  ? 13   GLU B C   1 
ATOM   3135 O O   . GLU B 1 13  ? 18.909  -69.866 -45.900 1.00 84.83  ? 13   GLU B O   1 
ATOM   3136 C CB  . GLU B 1 13  ? 21.608  -69.089 -44.495 1.00 83.12  ? 13   GLU B CB  1 
ATOM   3137 C CG  . GLU B 1 13  ? 22.742  -69.899 -45.119 1.00 97.00  ? 13   GLU B CG  1 
ATOM   3138 C CD  . GLU B 1 13  ? 23.663  -70.667 -44.184 1.00 129.59 ? 13   GLU B CD  1 
ATOM   3139 O OE1 . GLU B 1 13  ? 23.200  -71.106 -43.104 1.00 127.57 ? 13   GLU B OE1 1 
ATOM   3140 O OE2 . GLU B 1 13  ? 24.839  -70.883 -44.564 1.00 124.43 ? 13   GLU B OE2 1 
ATOM   3141 N N   . GLY B 1 14  ? 20.320  -69.494 -47.613 1.00 83.65  ? 14   GLY B N   1 
ATOM   3142 C CA  . GLY B 1 14  ? 19.651  -70.408 -48.527 1.00 117.91 ? 14   GLY B CA  1 
ATOM   3143 C C   . GLY B 1 14  ? 20.189  -71.815 -48.384 1.00 132.13 ? 14   GLY B C   1 
ATOM   3144 O O   . GLY B 1 14  ? 21.399  -72.006 -48.243 1.00 90.86  ? 14   GLY B O   1 
ATOM   3145 N N   . TRP B 1 20  ? 17.467  -70.525 -55.266 1.00 127.34 ? 20   TRP B N   1 
ATOM   3146 C CA  . TRP B 1 20  ? 16.177  -69.919 -54.941 1.00 127.51 ? 20   TRP B CA  1 
ATOM   3147 C C   . TRP B 1 20  ? 16.019  -69.656 -53.416 1.00 126.05 ? 20   TRP B C   1 
ATOM   3148 O O   . TRP B 1 20  ? 15.744  -70.570 -52.633 1.00 124.53 ? 20   TRP B O   1 
ATOM   3149 C CB  . TRP B 1 20  ? 14.986  -70.701 -55.555 1.00 127.77 ? 20   TRP B CB  1 
ATOM   3150 C CG  . TRP B 1 20  ? 14.729  -72.075 -54.997 1.00 129.93 ? 20   TRP B CG  1 
ATOM   3151 C CD1 . TRP B 1 20  ? 13.645  -72.472 -54.267 1.00 132.99 ? 20   TRP B CD1 1 
ATOM   3152 C CD2 . TRP B 1 20  ? 15.566  -73.238 -55.140 1.00 130.32 ? 20   TRP B CD2 1 
ATOM   3153 N NE1 . TRP B 1 20  ? 13.755  -73.805 -53.939 1.00 132.82 ? 20   TRP B NE1 1 
ATOM   3154 C CE2 . TRP B 1 20  ? 14.929  -74.299 -54.455 1.00 134.61 ? 20   TRP B CE2 1 
ATOM   3155 C CE3 . TRP B 1 20  ? 16.800  -73.486 -55.777 1.00 131.81 ? 20   TRP B CE3 1 
ATOM   3156 C CZ2 . TRP B 1 20  ? 15.486  -75.587 -54.385 1.00 134.19 ? 20   TRP B CZ2 1 
ATOM   3157 C CZ3 . TRP B 1 20  ? 17.357  -74.756 -55.694 1.00 133.46 ? 20   TRP B CZ3 1 
ATOM   3158 C CH2 . TRP B 1 20  ? 16.701  -75.792 -55.013 1.00 134.18 ? 20   TRP B CH2 1 
ATOM   3159 N N   . VAL B 1 21  ? 16.244  -68.378 -53.014 1.00 119.69 ? 21   VAL B N   1 
ATOM   3160 C CA  . VAL B 1 21  ? 16.156  -67.870 -51.631 1.00 117.48 ? 21   VAL B CA  1 
ATOM   3161 C C   . VAL B 1 21  ? 15.181  -66.663 -51.559 1.00 118.06 ? 21   VAL B C   1 
ATOM   3162 O O   . VAL B 1 21  ? 15.261  -65.747 -52.384 1.00 118.33 ? 21   VAL B O   1 
ATOM   3163 C CB  . VAL B 1 21  ? 17.551  -67.597 -50.980 1.00 120.20 ? 21   VAL B CB  1 
ATOM   3164 C CG1 . VAL B 1 21  ? 18.274  -66.407 -51.607 1.00 119.51 ? 21   VAL B CG1 1 
ATOM   3165 C CG2 . VAL B 1 21  ? 17.440  -67.437 -49.474 1.00 119.86 ? 21   VAL B CG2 1 
ATOM   3166 N N   . ASP B 1 22  ? 14.247  -66.690 -50.597 1.00 110.48 ? 22   ASP B N   1 
ATOM   3167 C CA  . ASP B 1 22  ? 13.247  -65.643 -50.459 1.00 108.44 ? 22   ASP B CA  1 
ATOM   3168 C C   . ASP B 1 22  ? 13.601  -64.595 -49.435 1.00 106.74 ? 22   ASP B C   1 
ATOM   3169 O O   . ASP B 1 22  ? 13.829  -64.923 -48.267 1.00 105.66 ? 22   ASP B O   1 
ATOM   3170 C CB  . ASP B 1 22  ? 11.868  -66.247 -50.181 1.00 110.72 ? 22   ASP B CB  1 
ATOM   3171 C CG  . ASP B 1 22  ? 11.177  -66.755 -51.426 1.00 123.89 ? 22   ASP B CG  1 
ATOM   3172 O OD1 . ASP B 1 22  ? 10.965  -65.949 -52.358 1.00 123.94 ? 22   ASP B OD1 1 
ATOM   3173 O OD2 . ASP B 1 22  ? 10.812  -67.949 -51.455 1.00 133.63 ? 22   ASP B OD2 1 
ATOM   3174 N N   . ILE B 1 23  ? 13.642  -63.322 -49.878 1.00 99.97  ? 23   ILE B N   1 
ATOM   3175 C CA  . ILE B 1 23  ? 13.939  -62.179 -49.002 1.00 98.48  ? 23   ILE B CA  1 
ATOM   3176 C C   . ILE B 1 23  ? 12.858  -61.108 -49.065 1.00 100.71 ? 23   ILE B C   1 
ATOM   3177 O O   . ILE B 1 23  ? 12.173  -60.972 -50.081 1.00 100.03 ? 23   ILE B O   1 
ATOM   3178 C CB  . ILE B 1 23  ? 15.350  -61.565 -49.180 1.00 101.16 ? 23   ILE B CB  1 
ATOM   3179 C CG1 . ILE B 1 23  ? 15.570  -61.019 -50.608 1.00 101.26 ? 23   ILE B CG1 1 
ATOM   3180 C CG2 . ILE B 1 23  ? 16.429  -62.548 -48.759 1.00 101.76 ? 23   ILE B CG2 1 
ATOM   3181 C CD1 . ILE B 1 23  ? 16.586  -59.882 -50.696 1.00 104.93 ? 23   ILE B CD1 1 
ATOM   3182 N N   . VAL B 1 24  ? 12.718  -60.357 -47.958 1.00 96.83  ? 24   VAL B N   1 
ATOM   3183 C CA  . VAL B 1 24  ? 11.747  -59.281 -47.799 1.00 96.35  ? 24   VAL B CA  1 
ATOM   3184 C C   . VAL B 1 24  ? 12.505  -57.985 -47.567 1.00 98.36  ? 24   VAL B C   1 
ATOM   3185 O O   . VAL B 1 24  ? 13.069  -57.765 -46.489 1.00 97.47  ? 24   VAL B O   1 
ATOM   3186 C CB  . VAL B 1 24  ? 10.698  -59.548 -46.677 1.00 100.41 ? 24   VAL B CB  1 
ATOM   3187 C CG1 . VAL B 1 24  ? 9.604   -58.489 -46.680 1.00 100.14 ? 24   VAL B CG1 1 
ATOM   3188 C CG2 . VAL B 1 24  ? 10.074  -60.933 -46.816 1.00 100.39 ? 24   VAL B CG2 1 
ATOM   3189 N N   . LEU B 1 25  ? 12.519  -57.131 -48.583 1.00 93.18  ? 25   LEU B N   1 
ATOM   3190 C CA  . LEU B 1 25  ? 13.164  -55.844 -48.447 1.00 91.73  ? 25   LEU B CA  1 
ATOM   3191 C C   . LEU B 1 25  ? 12.147  -54.765 -48.057 1.00 92.68  ? 25   LEU B C   1 
ATOM   3192 O O   . LEU B 1 25  ? 11.025  -54.752 -48.560 1.00 91.59  ? 25   LEU B O   1 
ATOM   3193 C CB  . LEU B 1 25  ? 13.925  -55.471 -49.723 1.00 91.58  ? 25   LEU B CB  1 
ATOM   3194 C CG  . LEU B 1 25  ? 15.099  -56.374 -50.115 1.00 96.12  ? 25   LEU B CG  1 
ATOM   3195 C CD1 . LEU B 1 25  ? 15.798  -55.839 -51.339 1.00 96.58  ? 25   LEU B CD1 1 
ATOM   3196 C CD2 . LEU B 1 25  ? 16.109  -56.523 -48.984 1.00 98.11  ? 25   LEU B CD2 1 
ATOM   3197 N N   . GLU B 1 26  ? 12.532  -53.896 -47.121 1.00 87.71  ? 26   GLU B N   1 
ATOM   3198 C CA  . GLU B 1 26  ? 11.724  -52.766 -46.679 1.00 86.86  ? 26   GLU B CA  1 
ATOM   3199 C C   . GLU B 1 26  ? 12.632  -51.588 -46.291 1.00 91.36  ? 26   GLU B C   1 
ATOM   3200 O O   . GLU B 1 26  ? 13.863  -51.725 -46.298 1.00 91.01  ? 26   GLU B O   1 
ATOM   3201 C CB  . GLU B 1 26  ? 10.691  -53.152 -45.604 1.00 87.97  ? 26   GLU B CB  1 
ATOM   3202 C CG  . GLU B 1 26  ? 11.251  -53.474 -44.231 1.00 98.07  ? 26   GLU B CG  1 
ATOM   3203 C CD  . GLU B 1 26  ? 10.214  -53.850 -43.189 1.00 111.99 ? 26   GLU B CD  1 
ATOM   3204 O OE1 . GLU B 1 26  ? 9.289   -53.041 -42.945 1.00 104.01 ? 26   GLU B OE1 1 
ATOM   3205 O OE2 . GLU B 1 26  ? 10.346  -54.944 -42.593 1.00 96.63  ? 26   GLU B OE2 1 
ATOM   3206 N N   . HIS B 1 27  ? 12.029  -50.417 -46.048 1.00 88.19  ? 27   HIS B N   1 
ATOM   3207 C CA  . HIS B 1 27  ? 12.781  -49.214 -45.733 1.00 88.16  ? 27   HIS B CA  1 
ATOM   3208 C C   . HIS B 1 27  ? 13.263  -49.259 -44.314 1.00 92.28  ? 27   HIS B C   1 
ATOM   3209 O O   . HIS B 1 27  ? 12.524  -49.687 -43.435 1.00 92.57  ? 27   HIS B O   1 
ATOM   3210 C CB  . HIS B 1 27  ? 11.969  -47.942 -46.044 1.00 88.99  ? 27   HIS B CB  1 
ATOM   3211 C CG  . HIS B 1 27  ? 11.992  -47.552 -47.498 1.00 92.47  ? 27   HIS B CG  1 
ATOM   3212 N ND1 . HIS B 1 27  ? 12.907  -46.628 -47.990 1.00 94.22  ? 27   HIS B ND1 1 
ATOM   3213 C CD2 . HIS B 1 27  ? 11.229  -47.993 -48.527 1.00 94.20  ? 27   HIS B CD2 1 
ATOM   3214 C CE1 . HIS B 1 27  ? 12.663  -46.530 -49.290 1.00 93.55  ? 27   HIS B CE1 1 
ATOM   3215 N NE2 . HIS B 1 27  ? 11.665  -47.331 -49.660 1.00 93.95  ? 27   HIS B NE2 1 
ATOM   3216 N N   . GLY B 1 28  ? 14.522  -48.872 -44.119 1.00 88.58  ? 28   GLY B N   1 
ATOM   3217 C CA  . GLY B 1 28  ? 15.203  -48.852 -42.822 1.00 87.49  ? 28   GLY B CA  1 
ATOM   3218 C C   . GLY B 1 28  ? 15.723  -50.208 -42.390 1.00 87.86  ? 28   GLY B C   1 
ATOM   3219 O O   . GLY B 1 28  ? 16.154  -50.381 -41.248 1.00 86.50  ? 28   GLY B O   1 
ATOM   3220 N N   . SER B 1 29  ? 15.664  -51.173 -43.315 1.00 83.09  ? 29   SER B N   1 
ATOM   3221 C CA  . SER B 1 29  ? 16.046  -52.562 -43.140 1.00 82.50  ? 29   SER B CA  1 
ATOM   3222 C C   . SER B 1 29  ? 17.092  -52.983 -44.173 1.00 86.51  ? 29   SER B C   1 
ATOM   3223 O O   . SER B 1 29  ? 16.973  -52.644 -45.355 1.00 87.00  ? 29   SER B O   1 
ATOM   3224 C CB  . SER B 1 29  ? 14.803  -53.452 -43.227 1.00 84.59  ? 29   SER B CB  1 
ATOM   3225 O OG  . SER B 1 29  ? 15.030  -54.811 -43.580 1.00 88.21  ? 29   SER B OG  1 
ATOM   3226 N N   . CYS B 1 30  ? 18.092  -53.754 -43.711 1.00 81.68  ? 30   CYS B N   1 
ATOM   3227 C CA  . CYS B 1 30  ? 19.165  -54.325 -44.512 1.00 80.97  ? 30   CYS B CA  1 
ATOM   3228 C C   . CYS B 1 30  ? 19.066  -55.844 -44.487 1.00 80.33  ? 30   CYS B C   1 
ATOM   3229 O O   . CYS B 1 30  ? 18.587  -56.387 -43.499 1.00 80.53  ? 30   CYS B O   1 
ATOM   3230 C CB  . CYS B 1 30  ? 20.515  -53.849 -43.989 1.00 82.18  ? 30   CYS B CB  1 
ATOM   3231 S SG  . CYS B 1 30  ? 21.793  -53.708 -45.271 1.00 86.48  ? 30   CYS B SG  1 
ATOM   3232 N N   . VAL B 1 31  ? 19.510  -56.537 -45.549 1.00 73.62  ? 31   VAL B N   1 
ATOM   3233 C CA  . VAL B 1 31  ? 19.476  -58.010 -45.587 1.00 72.62  ? 31   VAL B CA  1 
ATOM   3234 C C   . VAL B 1 31  ? 20.831  -58.621 -46.023 1.00 78.17  ? 31   VAL B C   1 
ATOM   3235 O O   . VAL B 1 31  ? 21.406  -58.189 -47.017 1.00 77.89  ? 31   VAL B O   1 
ATOM   3236 C CB  . VAL B 1 31  ? 18.291  -58.538 -46.431 1.00 74.59  ? 31   VAL B CB  1 
ATOM   3237 C CG1 . VAL B 1 31  ? 18.450  -60.014 -46.772 1.00 73.99  ? 31   VAL B CG1 1 
ATOM   3238 C CG2 . VAL B 1 31  ? 16.976  -58.289 -45.721 1.00 74.04  ? 31   VAL B CG2 1 
ATOM   3239 N N   . THR B 1 32  ? 21.318  -59.636 -45.291 1.00 75.63  ? 32   THR B N   1 
ATOM   3240 C CA  . THR B 1 32  ? 22.562  -60.331 -45.619 1.00 76.34  ? 32   THR B CA  1 
ATOM   3241 C C   . THR B 1 32  ? 22.230  -61.768 -46.053 1.00 84.12  ? 32   THR B C   1 
ATOM   3242 O O   . THR B 1 32  ? 21.633  -62.520 -45.287 1.00 83.62  ? 32   THR B O   1 
ATOM   3243 C CB  . THR B 1 32  ? 23.567  -60.208 -44.463 1.00 78.62  ? 32   THR B CB  1 
ATOM   3244 O OG1 . THR B 1 32  ? 23.878  -58.829 -44.251 1.00 76.46  ? 32   THR B OG1 1 
ATOM   3245 C CG2 . THR B 1 32  ? 24.842  -60.964 -44.719 1.00 74.43  ? 32   THR B CG2 1 
ATOM   3246 N N   . THR B 1 33  ? 22.586  -62.128 -47.296 1.00 84.13  ? 33   THR B N   1 
ATOM   3247 C CA  . THR B 1 33  ? 22.294  -63.449 -47.869 1.00 85.39  ? 33   THR B CA  1 
ATOM   3248 C C   . THR B 1 33  ? 23.542  -64.279 -48.129 1.00 92.40  ? 33   THR B C   1 
ATOM   3249 O O   . THR B 1 33  ? 24.512  -63.803 -48.730 1.00 92.68  ? 33   THR B O   1 
ATOM   3250 C CB  . THR B 1 33  ? 21.480  -63.335 -49.141 1.00 94.26  ? 33   THR B CB  1 
ATOM   3251 O OG1 . THR B 1 33  ? 22.244  -62.587 -50.097 1.00 102.05 ? 33   THR B OG1 1 
ATOM   3252 C CG2 . THR B 1 33  ? 20.125  -62.711 -48.906 1.00 88.73  ? 33   THR B CG2 1 
ATOM   3253 N N   . MET B 1 34  ? 23.481  -65.543 -47.700 1.00 89.94  ? 34   MET B N   1 
ATOM   3254 C CA  . MET B 1 34  ? 24.557  -66.515 -47.798 1.00 90.23  ? 34   MET B CA  1 
ATOM   3255 C C   . MET B 1 34  ? 24.060  -67.833 -48.359 1.00 97.96  ? 34   MET B C   1 
ATOM   3256 O O   . MET B 1 34  ? 22.905  -68.216 -48.152 1.00 97.00  ? 34   MET B O   1 
ATOM   3257 C CB  . MET B 1 34  ? 25.149  -66.775 -46.411 1.00 92.34  ? 34   MET B CB  1 
ATOM   3258 C CG  . MET B 1 34  ? 25.590  -65.535 -45.703 1.00 96.23  ? 34   MET B CG  1 
ATOM   3259 S SD  . MET B 1 34  ? 25.743  -65.819 -43.940 1.00 100.90 ? 34   MET B SD  1 
ATOM   3260 C CE  . MET B 1 34  ? 27.383  -66.582 -43.885 1.00 97.75  ? 34   MET B CE  1 
ATOM   3261 N N   . ALA B 1 35  ? 24.961  -68.539 -49.055 1.00 98.55  ? 35   ALA B N   1 
ATOM   3262 C CA  . ALA B 1 35  ? 24.747  -69.871 -49.623 1.00 99.93  ? 35   ALA B CA  1 
ATOM   3263 C C   . ALA B 1 35  ? 26.116  -70.540 -49.752 1.00 105.39 ? 35   ALA B C   1 
ATOM   3264 O O   . ALA B 1 35  ? 27.111  -69.826 -49.958 1.00 105.26 ? 35   ALA B O   1 
ATOM   3265 C CB  . ALA B 1 35  ? 24.082  -69.766 -50.981 1.00 100.78 ? 35   ALA B CB  1 
ATOM   3266 N N   . LYS B 1 36  ? 26.178  -71.892 -49.609 1.00 101.81 ? 36   LYS B N   1 
ATOM   3267 C CA  . LYS B 1 36  ? 27.449  -72.618 -49.703 1.00 101.39 ? 36   LYS B CA  1 
ATOM   3268 C C   . LYS B 1 36  ? 28.091  -72.429 -51.070 1.00 103.77 ? 36   LYS B C   1 
ATOM   3269 O O   . LYS B 1 36  ? 27.428  -72.641 -52.091 1.00 102.87 ? 36   LYS B O   1 
ATOM   3270 C CB  . LYS B 1 36  ? 27.323  -74.116 -49.340 1.00 104.05 ? 36   LYS B CB  1 
ATOM   3271 C CG  . LYS B 1 36  ? 28.684  -74.790 -49.136 1.00 122.15 ? 36   LYS B CG  1 
ATOM   3272 C CD  . LYS B 1 36  ? 28.582  -76.249 -48.757 1.00 132.60 ? 36   LYS B CD  1 
ATOM   3273 C CE  . LYS B 1 36  ? 29.954  -76.880 -48.691 1.00 144.51 ? 36   LYS B CE  1 
ATOM   3274 N NZ  . LYS B 1 36  ? 29.878  -78.265 -48.175 1.00 152.19 ? 36   LYS B NZ  1 
ATOM   3275 N N   . ASN B 1 37  ? 29.377  -71.978 -51.062 1.00 99.59  ? 37   ASN B N   1 
ATOM   3276 C CA  . ASN B 1 37  ? 30.236  -71.707 -52.225 1.00 99.35  ? 37   ASN B CA  1 
ATOM   3277 C C   . ASN B 1 37  ? 29.648  -70.636 -53.176 1.00 101.00 ? 37   ASN B C   1 
ATOM   3278 O O   . ASN B 1 37  ? 29.863  -70.658 -54.393 1.00 99.97  ? 37   ASN B O   1 
ATOM   3279 C CB  . ASN B 1 37  ? 30.629  -72.999 -52.959 1.00 102.29 ? 37   ASN B CB  1 
ATOM   3280 C CG  . ASN B 1 37  ? 31.445  -73.906 -52.069 1.00 130.05 ? 37   ASN B CG  1 
ATOM   3281 O OD1 . ASN B 1 37  ? 30.989  -74.979 -51.661 1.00 121.41 ? 37   ASN B OD1 1 
ATOM   3282 N ND2 . ASN B 1 37  ? 32.639  -73.451 -51.679 1.00 124.26 ? 37   ASN B ND2 1 
ATOM   3283 N N   . LYS B 1 38  ? 28.927  -69.682 -52.586 1.00 96.20  ? 38   LYS B N   1 
ATOM   3284 C CA  . LYS B 1 38  ? 28.332  -68.548 -53.278 1.00 95.05  ? 38   LYS B CA  1 
ATOM   3285 C C   . LYS B 1 38  ? 28.695  -67.308 -52.476 1.00 96.82  ? 38   LYS B C   1 
ATOM   3286 O O   . LYS B 1 38  ? 28.873  -67.409 -51.256 1.00 97.03  ? 38   LYS B O   1 
ATOM   3287 C CB  . LYS B 1 38  ? 26.804  -68.692 -53.422 1.00 97.46  ? 38   LYS B CB  1 
ATOM   3288 C CG  . LYS B 1 38  ? 26.334  -69.896 -54.251 1.00 112.99 ? 38   LYS B CG  1 
ATOM   3289 C CD  . LYS B 1 38  ? 26.521  -69.733 -55.751 1.00 122.53 ? 38   LYS B CD  1 
ATOM   3290 C CE  . LYS B 1 38  ? 25.988  -70.937 -56.487 1.00 129.06 ? 38   LYS B CE  1 
ATOM   3291 N NZ  . LYS B 1 38  ? 26.057  -70.748 -57.956 1.00 133.89 ? 38   LYS B NZ  1 
ATOM   3292 N N   . PRO B 1 39  ? 28.852  -66.137 -53.124 1.00 90.45  ? 39   PRO B N   1 
ATOM   3293 C CA  . PRO B 1 39  ? 29.250  -64.939 -52.370 1.00 89.29  ? 39   PRO B CA  1 
ATOM   3294 C C   . PRO B 1 39  ? 28.156  -64.378 -51.469 1.00 93.19  ? 39   PRO B C   1 
ATOM   3295 O O   . PRO B 1 39  ? 26.960  -64.439 -51.793 1.00 92.96  ? 39   PRO B O   1 
ATOM   3296 C CB  . PRO B 1 39  ? 29.671  -63.943 -53.453 1.00 90.60  ? 39   PRO B CB  1 
ATOM   3297 C CG  . PRO B 1 39  ? 29.555  -64.671 -54.745 1.00 95.25  ? 39   PRO B CG  1 
ATOM   3298 C CD  . PRO B 1 39  ? 28.679  -65.838 -54.554 1.00 91.15  ? 39   PRO B CD  1 
ATOM   3299 N N   . THR B 1 40  ? 28.577  -63.831 -50.322 1.00 88.68  ? 40   THR B N   1 
ATOM   3300 C CA  . THR B 1 40  ? 27.664  -63.202 -49.376 1.00 87.59  ? 40   THR B CA  1 
ATOM   3301 C C   . THR B 1 40  ? 27.276  -61.814 -49.914 1.00 89.45  ? 40   THR B C   1 
ATOM   3302 O O   . THR B 1 40  ? 28.153  -61.029 -50.308 1.00 87.80  ? 40   THR B O   1 
ATOM   3303 C CB  . THR B 1 40  ? 28.248  -63.246 -47.969 1.00 86.47  ? 40   THR B CB  1 
ATOM   3304 O OG1 . THR B 1 40  ? 28.334  -64.624 -47.581 1.00 78.56  ? 40   THR B OG1 1 
ATOM   3305 C CG2 . THR B 1 40  ? 27.411  -62.478 -46.961 1.00 81.05  ? 40   THR B CG2 1 
ATOM   3306 N N   . LEU B 1 41  ? 25.951  -61.549 -49.983 1.00 83.86  ? 41   LEU B N   1 
ATOM   3307 C CA  . LEU B 1 41  ? 25.417  -60.291 -50.506 1.00 81.29  ? 41   LEU B CA  1 
ATOM   3308 C C   . LEU B 1 41  ? 24.585  -59.505 -49.511 1.00 81.48  ? 41   LEU B C   1 
ATOM   3309 O O   . LEU B 1 41  ? 23.846  -60.080 -48.707 1.00 79.73  ? 41   LEU B O   1 
ATOM   3310 C CB  . LEU B 1 41  ? 24.584  -60.528 -51.771 1.00 80.41  ? 41   LEU B CB  1 
ATOM   3311 C CG  . LEU B 1 41  ? 25.269  -61.121 -52.987 1.00 83.41  ? 41   LEU B CG  1 
ATOM   3312 C CD1 . LEU B 1 41  ? 24.252  -61.480 -54.005 1.00 82.99  ? 41   LEU B CD1 1 
ATOM   3313 C CD2 . LEU B 1 41  ? 26.250  -60.164 -53.597 1.00 83.70  ? 41   LEU B CD2 1 
ATOM   3314 N N   . ASP B 1 42  ? 24.673  -58.171 -49.634 1.00 77.15  ? 42   ASP B N   1 
ATOM   3315 C CA  . ASP B 1 42  ? 23.948  -57.184 -48.830 1.00 76.15  ? 42   ASP B CA  1 
ATOM   3316 C C   . ASP B 1 42  ? 22.901  -56.449 -49.670 1.00 77.85  ? 42   ASP B C   1 
ATOM   3317 O O   . ASP B 1 42  ? 23.231  -55.891 -50.707 1.00 77.85  ? 42   ASP B O   1 
ATOM   3318 C CB  . ASP B 1 42  ? 24.928  -56.208 -48.144 1.00 77.71  ? 42   ASP B CB  1 
ATOM   3319 C CG  . ASP B 1 42  ? 25.515  -56.719 -46.842 1.00 88.72  ? 42   ASP B CG  1 
ATOM   3320 O OD1 . ASP B 1 42  ? 25.468  -57.952 -46.605 1.00 90.96  ? 42   ASP B OD1 1 
ATOM   3321 O OD2 . ASP B 1 42  ? 25.966  -55.887 -46.035 1.00 92.56  ? 42   ASP B OD2 1 
ATOM   3322 N N   . PHE B 1 43  ? 21.648  -56.462 -49.228 1.00 73.31  ? 43   PHE B N   1 
ATOM   3323 C CA  . PHE B 1 43  ? 20.536  -55.813 -49.930 1.00 72.84  ? 43   PHE B CA  1 
ATOM   3324 C C   . PHE B 1 43  ? 19.838  -54.745 -49.084 1.00 75.88  ? 43   PHE B C   1 
ATOM   3325 O O   . PHE B 1 43  ? 19.546  -54.971 -47.901 1.00 76.03  ? 43   PHE B O   1 
ATOM   3326 C CB  . PHE B 1 43  ? 19.489  -56.840 -50.346 1.00 74.48  ? 43   PHE B CB  1 
ATOM   3327 C CG  . PHE B 1 43  ? 19.983  -57.934 -51.242 1.00 76.63  ? 43   PHE B CG  1 
ATOM   3328 C CD1 . PHE B 1 43  ? 20.519  -59.094 -50.714 1.00 80.30  ? 43   PHE B CD1 1 
ATOM   3329 C CD2 . PHE B 1 43  ? 19.839  -57.844 -52.619 1.00 80.23  ? 43   PHE B CD2 1 
ATOM   3330 C CE1 . PHE B 1 43  ? 20.952  -60.127 -51.552 1.00 83.70  ? 43   PHE B CE1 1 
ATOM   3331 C CE2 . PHE B 1 43  ? 20.248  -58.889 -53.454 1.00 81.57  ? 43   PHE B CE2 1 
ATOM   3332 C CZ  . PHE B 1 43  ? 20.827  -60.012 -52.918 1.00 81.43  ? 43   PHE B CZ  1 
ATOM   3333 N N   . GLU B 1 44  ? 19.535  -53.600 -49.715 1.00 70.09  ? 44   GLU B N   1 
ATOM   3334 C CA  . GLU B 1 44  ? 18.809  -52.478 -49.118 1.00 68.53  ? 44   GLU B CA  1 
ATOM   3335 C C   . GLU B 1 44  ? 17.820  -51.908 -50.128 1.00 76.92  ? 44   GLU B C   1 
ATOM   3336 O O   . GLU B 1 44  ? 18.111  -51.872 -51.328 1.00 78.43  ? 44   GLU B O   1 
ATOM   3337 C CB  . GLU B 1 44  ? 19.760  -51.374 -48.655 1.00 68.64  ? 44   GLU B CB  1 
ATOM   3338 C CG  . GLU B 1 44  ? 19.164  -50.514 -47.562 1.00 75.71  ? 44   GLU B CG  1 
ATOM   3339 C CD  . GLU B 1 44  ? 20.046  -49.438 -46.952 1.00 102.95 ? 44   GLU B CD  1 
ATOM   3340 O OE1 . GLU B 1 44  ? 21.244  -49.705 -46.678 1.00 75.27  ? 44   GLU B OE1 1 
ATOM   3341 O OE2 . GLU B 1 44  ? 19.497  -48.349 -46.653 1.00 107.11 ? 44   GLU B OE2 1 
ATOM   3342 N N   . LEU B 1 45  ? 16.643  -51.475 -49.648 1.00 74.22  ? 45   LEU B N   1 
ATOM   3343 C CA  . LEU B 1 45  ? 15.659  -50.783 -50.470 1.00 73.43  ? 45   LEU B CA  1 
ATOM   3344 C C   . LEU B 1 45  ? 15.936  -49.315 -50.199 1.00 79.73  ? 45   LEU B C   1 
ATOM   3345 O O   . LEU B 1 45  ? 15.724  -48.859 -49.077 1.00 80.02  ? 45   LEU B O   1 
ATOM   3346 C CB  . LEU B 1 45  ? 14.252  -51.163 -50.044 1.00 72.84  ? 45   LEU B CB  1 
ATOM   3347 C CG  . LEU B 1 45  ? 13.112  -50.562 -50.828 1.00 77.04  ? 45   LEU B CG  1 
ATOM   3348 C CD1 . LEU B 1 45  ? 13.298  -50.757 -52.335 1.00 77.33  ? 45   LEU B CD1 1 
ATOM   3349 C CD2 . LEU B 1 45  ? 11.809  -51.170 -50.380 1.00 80.05  ? 45   LEU B CD2 1 
ATOM   3350 N N   . ILE B 1 46  ? 16.519  -48.616 -51.182 1.00 78.54  ? 46   ILE B N   1 
ATOM   3351 C CA  . ILE B 1 46  ? 16.928  -47.216 -51.088 1.00 79.88  ? 46   ILE B CA  1 
ATOM   3352 C C   . ILE B 1 46  ? 15.751  -46.242 -51.277 1.00 85.87  ? 46   ILE B C   1 
ATOM   3353 O O   . ILE B 1 46  ? 15.593  -45.341 -50.452 1.00 84.33  ? 46   ILE B O   1 
ATOM   3354 C CB  . ILE B 1 46  ? 18.118  -46.950 -52.050 1.00 83.72  ? 46   ILE B CB  1 
ATOM   3355 C CG1 . ILE B 1 46  ? 19.425  -47.501 -51.438 1.00 84.89  ? 46   ILE B CG1 1 
ATOM   3356 C CG2 . ILE B 1 46  ? 18.278  -45.462 -52.452 1.00 84.99  ? 46   ILE B CG2 1 
ATOM   3357 C CD1 . ILE B 1 46  ? 19.829  -47.013 -49.964 1.00 95.71  ? 46   ILE B CD1 1 
ATOM   3358 N N   . LYS B 1 47  ? 14.944  -46.406 -52.356 1.00 85.00  ? 47   LYS B N   1 
ATOM   3359 C CA  . LYS B 1 47  ? 13.783  -45.545 -52.608 1.00 85.13  ? 47   LYS B CA  1 
ATOM   3360 C C   . LYS B 1 47  ? 12.637  -46.250 -53.331 1.00 89.08  ? 47   LYS B C   1 
ATOM   3361 O O   . LYS B 1 47  ? 12.841  -47.188 -54.103 1.00 87.43  ? 47   LYS B O   1 
ATOM   3362 C CB  . LYS B 1 47  ? 14.162  -44.227 -53.333 1.00 87.44  ? 47   LYS B CB  1 
ATOM   3363 C CG  . LYS B 1 47  ? 14.599  -44.368 -54.790 1.00 102.98 ? 47   LYS B CG  1 
ATOM   3364 C CD  . LYS B 1 47  ? 15.377  -43.158 -55.269 1.00 117.36 ? 47   LYS B CD  1 
ATOM   3365 C CE  . LYS B 1 47  ? 16.058  -43.379 -56.601 1.00 127.27 ? 47   LYS B CE  1 
ATOM   3366 N NZ  . LYS B 1 47  ? 17.468  -43.824 -56.436 1.00 131.99 ? 47   LYS B NZ  1 
ATOM   3367 N N   . THR B 1 48  ? 11.425  -45.768 -53.038 1.00 86.91  ? 48   THR B N   1 
ATOM   3368 C CA  . THR B 1 48  ? 10.144  -46.146 -53.629 1.00 86.78  ? 48   THR B CA  1 
ATOM   3369 C C   . THR B 1 48  ? 9.651   -44.819 -54.248 1.00 89.42  ? 48   THR B C   1 
ATOM   3370 O O   . THR B 1 48  ? 9.787   -43.778 -53.606 1.00 87.96  ? 48   THR B O   1 
ATOM   3371 C CB  . THR B 1 48  ? 9.196   -46.703 -52.533 1.00 95.58  ? 48   THR B CB  1 
ATOM   3372 O OG1 . THR B 1 48  ? 9.846   -47.741 -51.783 1.00 90.81  ? 48   THR B OG1 1 
ATOM   3373 C CG2 . THR B 1 48  ? 7.909   -47.231 -53.097 1.00 94.41  ? 48   THR B CG2 1 
ATOM   3374 N N   . GLU B 1 49  ? 9.173   -44.832 -55.513 1.00 86.91  ? 49   GLU B N   1 
ATOM   3375 C CA  . GLU B 1 49  ? 8.722   -43.613 -56.221 1.00 87.02  ? 49   GLU B CA  1 
ATOM   3376 C C   . GLU B 1 49  ? 7.599   -43.822 -57.265 1.00 91.17  ? 49   GLU B C   1 
ATOM   3377 O O   . GLU B 1 49  ? 7.537   -44.867 -57.931 1.00 90.21  ? 49   GLU B O   1 
ATOM   3378 C CB  . GLU B 1 49  ? 9.910   -42.877 -56.889 1.00 88.63  ? 49   GLU B CB  1 
ATOM   3379 C CG  . GLU B 1 49  ? 10.061  -41.427 -56.446 1.00 104.55 ? 49   GLU B CG  1 
ATOM   3380 C CD  . GLU B 1 49  ? 10.323  -40.358 -57.498 1.00 130.32 ? 49   GLU B CD  1 
ATOM   3381 O OE1 . GLU B 1 49  ? 9.973   -40.572 -58.682 1.00 127.81 ? 49   GLU B OE1 1 
ATOM   3382 O OE2 . GLU B 1 49  ? 10.837  -39.278 -57.120 1.00 115.42 ? 49   GLU B OE2 1 
ATOM   3383 N N   . ALA B 1 50  ? 6.728   -42.787 -57.419 1.00 87.77  ? 50   ALA B N   1 
ATOM   3384 C CA  . ALA B 1 50  ? 5.655   -42.778 -58.429 1.00 86.69  ? 50   ALA B CA  1 
ATOM   3385 C C   . ALA B 1 50  ? 6.178   -42.048 -59.677 1.00 88.60  ? 50   ALA B C   1 
ATOM   3386 O O   . ALA B 1 50  ? 6.678   -40.921 -59.573 1.00 86.99  ? 50   ALA B O   1 
ATOM   3387 C CB  . ALA B 1 50  ? 4.404   -42.091 -57.894 1.00 87.07  ? 50   ALA B CB  1 
ATOM   3388 N N   . LYS B 1 51  ? 6.132   -42.726 -60.833 1.00 85.05  ? 51   LYS B N   1 
ATOM   3389 C CA  . LYS B 1 51  ? 6.622   -42.144 -62.080 1.00 85.10  ? 51   LYS B CA  1 
ATOM   3390 C C   . LYS B 1 51  ? 5.555   -41.292 -62.759 1.00 87.44  ? 51   LYS B C   1 
ATOM   3391 O O   . LYS B 1 51  ? 4.557   -41.813 -63.277 1.00 85.55  ? 51   LYS B O   1 
ATOM   3392 C CB  . LYS B 1 51  ? 7.237   -43.198 -63.027 1.00 88.07  ? 51   LYS B CB  1 
ATOM   3393 C CG  . LYS B 1 51  ? 8.704   -43.506 -62.705 1.00 99.21  ? 51   LYS B CG  1 
ATOM   3394 C CD  . LYS B 1 51  ? 9.371   -44.431 -63.717 1.00 108.71 ? 51   LYS B CD  1 
ATOM   3395 C CE  . LYS B 1 51  ? 9.054   -45.898 -63.509 1.00 120.61 ? 51   LYS B CE  1 
ATOM   3396 N NZ  . LYS B 1 51  ? 9.897   -46.778 -64.368 1.00 126.35 ? 51   LYS B NZ  1 
ATOM   3397 N N   . GLN B 1 52  ? 5.782   -39.958 -62.699 1.00 83.81  ? 52   GLN B N   1 
ATOM   3398 C CA  . GLN B 1 52  ? 4.968   -38.850 -63.247 1.00 83.23  ? 52   GLN B CA  1 
ATOM   3399 C C   . GLN B 1 52  ? 3.420   -39.040 -62.995 1.00 82.87  ? 52   GLN B C   1 
ATOM   3400 O O   . GLN B 1 52  ? 2.673   -39.403 -63.919 1.00 82.27  ? 52   GLN B O   1 
ATOM   3401 C CB  . GLN B 1 52  ? 5.317   -38.592 -64.733 1.00 85.20  ? 52   GLN B CB  1 
ATOM   3402 C CG  . GLN B 1 52  ? 5.579   -37.108 -65.049 1.00 111.35 ? 52   GLN B CG  1 
ATOM   3403 C CD  . GLN B 1 52  ? 6.593   -36.809 -66.163 1.00 128.51 ? 52   GLN B CD  1 
ATOM   3404 O OE1 . GLN B 1 52  ? 6.627   -37.436 -67.241 1.00 123.96 ? 52   GLN B OE1 1 
ATOM   3405 N NE2 . GLN B 1 52  ? 7.405   -35.779 -65.949 1.00 114.66 ? 52   GLN B NE2 1 
ATOM   3406 N N   . PRO B 1 53  ? 2.936   -38.830 -61.735 1.00 75.21  ? 53   PRO B N   1 
ATOM   3407 C CA  . PRO B 1 53  ? 1.503   -39.001 -61.454 1.00 73.44  ? 53   PRO B CA  1 
ATOM   3408 C C   . PRO B 1 53  ? 0.684   -37.752 -61.785 1.00 75.04  ? 53   PRO B C   1 
ATOM   3409 O O   . PRO B 1 53  ? 1.150   -36.617 -61.624 1.00 74.89  ? 53   PRO B O   1 
ATOM   3410 C CB  . PRO B 1 53  ? 1.476   -39.319 -59.963 1.00 75.09  ? 53   PRO B CB  1 
ATOM   3411 C CG  . PRO B 1 53  ? 2.728   -38.737 -59.414 1.00 79.89  ? 53   PRO B CG  1 
ATOM   3412 C CD  . PRO B 1 53  ? 3.655   -38.378 -60.528 1.00 75.97  ? 53   PRO B CD  1 
ATOM   3413 N N   . ALA B 1 54  ? -0.550  -37.965 -62.244 1.00 68.80  ? 54   ALA B N   1 
ATOM   3414 C CA  . ALA B 1 54  ? -1.430  -36.872 -62.635 1.00 66.66  ? 54   ALA B CA  1 
ATOM   3415 C C   . ALA B 1 54  ? -2.057  -36.178 -61.449 1.00 66.02  ? 54   ALA B C   1 
ATOM   3416 O O   . ALA B 1 54  ? -2.846  -36.782 -60.714 1.00 66.37  ? 54   ALA B O   1 
ATOM   3417 C CB  . ALA B 1 54  ? -2.510  -37.368 -63.589 1.00 67.31  ? 54   ALA B CB  1 
ATOM   3418 N N   . THR B 1 55  ? -1.697  -34.908 -61.262 1.00 58.20  ? 55   THR B N   1 
ATOM   3419 C CA  . THR B 1 55  ? -2.293  -34.119 -60.203 1.00 56.33  ? 55   THR B CA  1 
ATOM   3420 C C   . THR B 1 55  ? -3.772  -34.069 -60.459 1.00 55.50  ? 55   THR B C   1 
ATOM   3421 O O   . THR B 1 55  ? -4.183  -33.715 -61.550 1.00 54.03  ? 55   THR B O   1 
ATOM   3422 C CB  . THR B 1 55  ? -1.691  -32.734 -60.112 1.00 66.37  ? 55   THR B CB  1 
ATOM   3423 O OG1 . THR B 1 55  ? -0.277  -32.811 -60.377 1.00 68.11  ? 55   THR B OG1 1 
ATOM   3424 C CG2 . THR B 1 55  ? -1.997  -32.075 -58.765 1.00 61.81  ? 55   THR B CG2 1 
ATOM   3425 N N   . LEU B 1 56  ? -4.552  -34.588 -59.519 1.00 50.87  ? 56   LEU B N   1 
ATOM   3426 C CA  . LEU B 1 56  ? -6.001  -34.602 -59.615 1.00 49.74  ? 56   LEU B CA  1 
ATOM   3427 C C   . LEU B 1 56  ? -6.541  -33.180 -59.414 1.00 53.78  ? 56   LEU B C   1 
ATOM   3428 O O   . LEU B 1 56  ? -7.155  -32.614 -60.322 1.00 53.70  ? 56   LEU B O   1 
ATOM   3429 C CB  . LEU B 1 56  ? -6.609  -35.586 -58.594 1.00 48.89  ? 56   LEU B CB  1 
ATOM   3430 C CG  . LEU B 1 56  ? -8.167  -35.745 -58.538 1.00 51.52  ? 56   LEU B CG  1 
ATOM   3431 C CD1 . LEU B 1 56  ? -8.794  -35.837 -59.902 1.00 50.59  ? 56   LEU B CD1 1 
ATOM   3432 C CD2 . LEU B 1 56  ? -8.549  -36.988 -57.798 1.00 52.10  ? 56   LEU B CD2 1 
ATOM   3433 N N   . ARG B 1 57  ? -6.255  -32.594 -58.245 1.00 48.93  ? 57   ARG B N   1 
ATOM   3434 C CA  . ARG B 1 57  ? -6.737  -31.282 -57.840 1.00 47.95  ? 57   ARG B CA  1 
ATOM   3435 C C   . ARG B 1 57  ? -5.748  -30.682 -56.828 1.00 52.22  ? 57   ARG B C   1 
ATOM   3436 O O   . ARG B 1 57  ? -5.063  -31.424 -56.128 1.00 52.62  ? 57   ARG B O   1 
ATOM   3437 C CB  . ARG B 1 57  ? -8.134  -31.499 -57.231 1.00 46.74  ? 57   ARG B CB  1 
ATOM   3438 C CG  . ARG B 1 57  ? -8.938  -30.283 -56.877 1.00 49.60  ? 57   ARG B CG  1 
ATOM   3439 C CD  . ARG B 1 57  ? -10.258 -30.726 -56.272 1.00 49.86  ? 57   ARG B CD  1 
ATOM   3440 N NE  . ARG B 1 57  ? -11.279 -30.962 -57.290 1.00 52.85  ? 57   ARG B NE  1 
ATOM   3441 C CZ  . ARG B 1 57  ? -12.546 -31.267 -57.030 1.00 69.43  ? 57   ARG B CZ  1 
ATOM   3442 N NH1 . ARG B 1 57  ? -12.962 -31.404 -55.778 1.00 59.26  ? 57   ARG B NH1 1 
ATOM   3443 N NH2 . ARG B 1 57  ? -13.407 -31.438 -58.018 1.00 65.47  ? 57   ARG B NH2 1 
ATOM   3444 N N   . LYS B 1 58  ? -5.648  -29.346 -56.788 1.00 49.44  ? 58   LYS B N   1 
ATOM   3445 C CA  . LYS B 1 58  ? -4.774  -28.565 -55.891 1.00 49.09  ? 58   LYS B CA  1 
ATOM   3446 C C   . LYS B 1 58  ? -5.692  -27.670 -55.035 1.00 52.13  ? 58   LYS B C   1 
ATOM   3447 O O   . LYS B 1 58  ? -6.533  -26.966 -55.611 1.00 51.93  ? 58   LYS B O   1 
ATOM   3448 C CB  . LYS B 1 58  ? -3.804  -27.720 -56.737 1.00 50.60  ? 58   LYS B CB  1 
ATOM   3449 C CG  . LYS B 1 58  ? -2.855  -26.818 -55.964 1.00 62.99  ? 58   LYS B CG  1 
ATOM   3450 C CD  . LYS B 1 58  ? -2.250  -25.707 -56.847 1.00 70.15  ? 58   LYS B CD  1 
ATOM   3451 C CE  . LYS B 1 58  ? -0.994  -26.102 -57.589 1.00 78.51  ? 58   LYS B CE  1 
ATOM   3452 N NZ  . LYS B 1 58  ? -0.463  -24.980 -58.420 1.00 86.84  ? 58   LYS B NZ  1 
ATOM   3453 N N   . TYR B 1 59  ? -5.574  -27.732 -53.682 1.00 45.70  ? 59   TYR B N   1 
ATOM   3454 C CA  . TYR B 1 59  ? -6.423  -26.931 -52.787 1.00 44.33  ? 59   TYR B CA  1 
ATOM   3455 C C   . TYR B 1 59  ? -5.705  -25.823 -52.054 1.00 52.60  ? 59   TYR B C   1 
ATOM   3456 O O   . TYR B 1 59  ? -4.549  -25.974 -51.688 1.00 53.10  ? 59   TYR B O   1 
ATOM   3457 C CB  . TYR B 1 59  ? -7.058  -27.793 -51.721 1.00 42.93  ? 59   TYR B CB  1 
ATOM   3458 C CG  . TYR B 1 59  ? -8.135  -28.736 -52.184 1.00 41.11  ? 59   TYR B CG  1 
ATOM   3459 C CD1 . TYR B 1 59  ? -9.469  -28.342 -52.195 1.00 42.50  ? 59   TYR B CD1 1 
ATOM   3460 C CD2 . TYR B 1 59  ? -7.856  -30.077 -52.412 1.00 41.41  ? 59   TYR B CD2 1 
ATOM   3461 C CE1 . TYR B 1 59  ? -10.490 -29.239 -52.494 1.00 43.59  ? 59   TYR B CE1 1 
ATOM   3462 C CE2 . TYR B 1 59  ? -8.870  -30.990 -52.675 1.00 42.74  ? 59   TYR B CE2 1 
ATOM   3463 C CZ  . TYR B 1 59  ? -10.185 -30.563 -52.737 1.00 50.24  ? 59   TYR B CZ  1 
ATOM   3464 O OH  . TYR B 1 59  ? -11.165 -31.451 -53.095 1.00 47.87  ? 59   TYR B OH  1 
ATOM   3465 N N   . CYS B 1 60  ? -6.415  -24.736 -51.766 1.00 52.92  ? 60   CYS B N   1 
ATOM   3466 C CA  . CYS B 1 60  ? -5.872  -23.638 -50.979 1.00 54.46  ? 60   CYS B CA  1 
ATOM   3467 C C   . CYS B 1 60  ? -6.223  -23.883 -49.529 1.00 58.76  ? 60   CYS B C   1 
ATOM   3468 O O   . CYS B 1 60  ? -7.399  -24.121 -49.211 1.00 57.31  ? 60   CYS B O   1 
ATOM   3469 C CB  . CYS B 1 60  ? -6.385  -22.285 -51.453 1.00 55.55  ? 60   CYS B CB  1 
ATOM   3470 S SG  . CYS B 1 60  ? -5.497  -20.886 -50.733 1.00 60.59  ? 60   CYS B SG  1 
ATOM   3471 N N   . ILE B 1 61  ? -5.195  -23.831 -48.653 1.00 56.39  ? 61   ILE B N   1 
ATOM   3472 C CA  . ILE B 1 61  ? -5.335  -24.052 -47.209 1.00 56.79  ? 61   ILE B CA  1 
ATOM   3473 C C   . ILE B 1 61  ? -5.055  -22.776 -46.401 1.00 57.38  ? 61   ILE B C   1 
ATOM   3474 O O   . ILE B 1 61  ? -5.511  -22.667 -45.262 1.00 56.29  ? 61   ILE B O   1 
ATOM   3475 C CB  . ILE B 1 61  ? -4.533  -25.280 -46.709 1.00 61.36  ? 61   ILE B CB  1 
ATOM   3476 C CG1 . ILE B 1 61  ? -3.030  -25.151 -46.956 1.00 61.59  ? 61   ILE B CG1 1 
ATOM   3477 C CG2 . ILE B 1 61  ? -5.069  -26.559 -47.334 1.00 63.88  ? 61   ILE B CG2 1 
ATOM   3478 C CD1 . ILE B 1 61  ? -2.291  -25.384 -45.778 1.00 70.90  ? 61   ILE B CD1 1 
ATOM   3479 N N   . GLU B 1 62  ? -4.391  -21.794 -47.004 1.00 54.09  ? 62   GLU B N   1 
ATOM   3480 C CA  . GLU B 1 62  ? -4.173  -20.506 -46.351 1.00 55.79  ? 62   GLU B CA  1 
ATOM   3481 C C   . GLU B 1 62  ? -4.306  -19.401 -47.400 1.00 65.83  ? 62   GLU B C   1 
ATOM   3482 O O   . GLU B 1 62  ? -3.631  -19.455 -48.433 1.00 64.88  ? 62   GLU B O   1 
ATOM   3483 C CB  . GLU B 1 62  ? -2.813  -20.436 -45.649 1.00 56.92  ? 62   GLU B CB  1 
ATOM   3484 C CG  . GLU B 1 62  ? -2.609  -19.177 -44.827 1.00 62.71  ? 62   GLU B CG  1 
ATOM   3485 C CD  . GLU B 1 62  ? -1.360  -19.119 -43.975 1.00 83.68  ? 62   GLU B CD  1 
ATOM   3486 O OE1 . GLU B 1 62  ? -0.761  -20.184 -43.699 1.00 107.18 ? 62   GLU B OE1 1 
ATOM   3487 O OE2 . GLU B 1 62  ? -1.009  -18.002 -43.536 1.00 69.63  ? 62   GLU B OE2 1 
ATOM   3488 N N   . ALA B 1 63  ? -5.175  -18.403 -47.125 1.00 66.23  ? 63   ALA B N   1 
ATOM   3489 C CA  . ALA B 1 63  ? -5.428  -17.319 -48.062 1.00 67.75  ? 63   ALA B CA  1 
ATOM   3490 C C   . ALA B 1 63  ? -5.236  -15.932 -47.496 1.00 75.33  ? 63   ALA B C   1 
ATOM   3491 O O   . ALA B 1 63  ? -5.076  -15.781 -46.295 1.00 73.75  ? 63   ALA B O   1 
ATOM   3492 C CB  . ALA B 1 63  ? -6.815  -17.458 -48.651 1.00 68.43  ? 63   ALA B CB  1 
ATOM   3493 N N   . LYS B 1 64  ? -5.240  -14.916 -48.387 1.00 76.19  ? 64   LYS B N   1 
ATOM   3494 C CA  . LYS B 1 64  ? -5.072  -13.492 -48.088 1.00 76.55  ? 64   LYS B CA  1 
ATOM   3495 C C   . LYS B 1 64  ? -6.033  -12.630 -48.917 1.00 82.04  ? 64   LYS B C   1 
ATOM   3496 O O   . LYS B 1 64  ? -6.086  -12.759 -50.147 1.00 82.16  ? 64   LYS B O   1 
ATOM   3497 C CB  . LYS B 1 64  ? -3.623  -13.074 -48.349 1.00 78.55  ? 64   LYS B CB  1 
ATOM   3498 C CG  . LYS B 1 64  ? -3.204  -11.866 -47.544 1.00 99.06  ? 64   LYS B CG  1 
ATOM   3499 C CD  . LYS B 1 64  ? -1.713  -11.554 -47.732 1.00 112.66 ? 64   LYS B CD  1 
ATOM   3500 C CE  . LYS B 1 64  ? -1.442  -10.440 -48.727 1.00 123.06 ? 64   LYS B CE  1 
ATOM   3501 N NZ  . LYS B 1 64  ? -1.711  -10.851 -50.135 1.00 132.75 ? 64   LYS B NZ  1 
ATOM   3502 N N   . LEU B 1 65  ? -6.797  -11.758 -48.239 1.00 78.83  ? 65   LEU B N   1 
ATOM   3503 C CA  . LEU B 1 65  ? -7.719  -10.849 -48.925 1.00 77.76  ? 65   LEU B CA  1 
ATOM   3504 C C   . LEU B 1 65  ? -7.140  -9.460  -48.937 1.00 81.65  ? 65   LEU B C   1 
ATOM   3505 O O   . LEU B 1 65  ? -6.802  -8.920  -47.881 1.00 81.00  ? 65   LEU B O   1 
ATOM   3506 C CB  . LEU B 1 65  ? -9.115  -10.818 -48.296 1.00 77.04  ? 65   LEU B CB  1 
ATOM   3507 C CG  . LEU B 1 65  ? -9.972  -12.036 -48.449 1.00 80.74  ? 65   LEU B CG  1 
ATOM   3508 C CD1 . LEU B 1 65  ? -11.180 -11.913 -47.569 1.00 80.57  ? 65   LEU B CD1 1 
ATOM   3509 C CD2 . LEU B 1 65  ? -10.354 -12.290 -49.903 1.00 82.59  ? 65   LEU B CD2 1 
ATOM   3510 N N   . THR B 1 66  ? -7.006  -8.904  -50.141 1.00 78.66  ? 66   THR B N   1 
ATOM   3511 C CA  . THR B 1 66  ? -6.488  -7.569  -50.430 1.00 78.88  ? 66   THR B CA  1 
ATOM   3512 C C   . THR B 1 66  ? -7.506  -6.818  -51.320 1.00 84.65  ? 66   THR B C   1 
ATOM   3513 O O   . THR B 1 66  ? -8.566  -7.366  -51.639 1.00 83.75  ? 66   THR B O   1 
ATOM   3514 C CB  . THR B 1 66  ? -5.120  -7.693  -51.154 1.00 84.25  ? 66   THR B CB  1 
ATOM   3515 O OG1 . THR B 1 66  ? -5.236  -8.565  -52.282 1.00 85.48  ? 66   THR B OG1 1 
ATOM   3516 C CG2 . THR B 1 66  ? -4.012  -8.190  -50.243 1.00 81.89  ? 66   THR B CG2 1 
ATOM   3517 N N   . ASN B 1 67  ? -7.179  -5.570  -51.711 1.00 82.51  ? 67   ASN B N   1 
ATOM   3518 C CA  . ASN B 1 67  ? -7.945  -4.729  -52.633 1.00 82.79  ? 67   ASN B CA  1 
ATOM   3519 C C   . ASN B 1 67  ? -9.466  -4.642  -52.354 1.00 90.12  ? 67   ASN B C   1 
ATOM   3520 O O   . ASN B 1 67  ? -10.258 -4.608  -53.307 1.00 91.01  ? 67   ASN B O   1 
ATOM   3521 C CB  . ASN B 1 67  ? -7.692  -5.213  -54.063 1.00 81.69  ? 67   ASN B CB  1 
ATOM   3522 C CG  . ASN B 1 67  ? -6.244  -5.203  -54.464 1.00 109.36 ? 67   ASN B CG  1 
ATOM   3523 O OD1 . ASN B 1 67  ? -5.474  -6.118  -54.113 1.00 99.67  ? 67   ASN B OD1 1 
ATOM   3524 N ND2 . ASN B 1 67  ? -5.863  -4.155  -55.207 1.00 105.65 ? 67   ASN B ND2 1 
ATOM   3525 N N   . THR B 1 68  ? -9.880  -4.606  -51.068 1.00 87.52  ? 68   THR B N   1 
ATOM   3526 C CA  . THR B 1 68  ? -11.303 -4.539  -50.718 1.00 87.98  ? 68   THR B CA  1 
ATOM   3527 C C   . THR B 1 68  ? -11.944 -3.249  -51.229 1.00 94.60  ? 68   THR B C   1 
ATOM   3528 O O   . THR B 1 68  ? -11.484 -2.152  -50.901 1.00 95.01  ? 68   THR B O   1 
ATOM   3529 C CB  . THR B 1 68  ? -11.515 -4.787  -49.235 1.00 96.76  ? 68   THR B CB  1 
ATOM   3530 O OG1 . THR B 1 68  ? -11.087 -6.117  -48.950 1.00 98.97  ? 68   THR B OG1 1 
ATOM   3531 C CG2 . THR B 1 68  ? -12.968 -4.630  -48.819 1.00 95.93  ? 68   THR B CG2 1 
ATOM   3532 N N   . THR B 1 69  ? -12.989 -3.403  -52.071 1.00 92.00  ? 69   THR B N   1 
ATOM   3533 C CA  . THR B 1 69  ? -13.742 -2.325  -52.734 1.00 91.82  ? 69   THR B CA  1 
ATOM   3534 C C   . THR B 1 69  ? -15.279 -2.502  -52.594 1.00 96.23  ? 69   THR B C   1 
ATOM   3535 O O   . THR B 1 69  ? -15.790 -3.602  -52.821 1.00 95.47  ? 69   THR B O   1 
ATOM   3536 C CB  . THR B 1 69  ? -13.305 -2.233  -54.212 1.00 98.58  ? 69   THR B CB  1 
ATOM   3537 O OG1 . THR B 1 69  ? -13.468 -3.504  -54.843 1.00 96.13  ? 69   THR B OG1 1 
ATOM   3538 C CG2 . THR B 1 69  ? -11.844 -1.788  -54.378 1.00 99.53  ? 69   THR B CG2 1 
ATOM   3539 N N   . THR B 1 70  ? -16.011 -1.421  -52.238 1.00 93.28  ? 70   THR B N   1 
ATOM   3540 C CA  . THR B 1 70  ? -17.478 -1.473  -52.077 1.00 93.00  ? 70   THR B CA  1 
ATOM   3541 C C   . THR B 1 70  ? -18.273 -0.402  -52.836 1.00 95.84  ? 70   THR B C   1 
ATOM   3542 O O   . THR B 1 70  ? -17.992 0.791   -52.691 1.00 95.86  ? 70   THR B O   1 
ATOM   3543 C CB  . THR B 1 70  ? -17.853 -1.434  -50.591 1.00 103.40 ? 70   THR B CB  1 
ATOM   3544 O OG1 . THR B 1 70  ? -17.333 -2.600  -49.954 1.00 104.00 ? 70   THR B OG1 1 
ATOM   3545 C CG2 . THR B 1 70  ? -19.368 -1.329  -50.356 1.00 102.80 ? 70   THR B CG2 1 
ATOM   3546 N N   . GLU B 1 71  ? -19.322 -0.830  -53.576 1.00 90.83  ? 71   GLU B N   1 
ATOM   3547 C CA  . GLU B 1 71  ? -20.242 0.085   -54.244 1.00 89.95  ? 71   GLU B CA  1 
ATOM   3548 C C   . GLU B 1 71  ? -21.647 -0.091  -53.683 1.00 91.23  ? 71   GLU B C   1 
ATOM   3549 O O   . GLU B 1 71  ? -22.144 -1.210  -53.577 1.00 89.79  ? 71   GLU B O   1 
ATOM   3550 C CB  . GLU B 1 71  ? -20.241 -0.077  -55.763 1.00 91.44  ? 71   GLU B CB  1 
ATOM   3551 C CG  . GLU B 1 71  ? -20.885 1.097   -56.488 1.00 101.89 ? 71   GLU B CG  1 
ATOM   3552 C CD  . GLU B 1 71  ? -20.883 1.008   -58.005 1.00 117.96 ? 71   GLU B CD  1 
ATOM   3553 O OE1 . GLU B 1 71  ? -19.843 1.335   -58.623 1.00 101.41 ? 71   GLU B OE1 1 
ATOM   3554 O OE2 . GLU B 1 71  ? -21.930 0.629   -58.578 1.00 110.69 ? 71   GLU B OE2 1 
ATOM   3555 N N   . SER B 1 72  ? -22.275 1.023   -53.308 1.00 86.74  ? 72   SER B N   1 
ATOM   3556 C CA  . SER B 1 72  ? -23.639 1.035   -52.785 1.00 85.52  ? 72   SER B CA  1 
ATOM   3557 C C   . SER B 1 72  ? -24.591 1.828   -53.702 1.00 88.84  ? 72   SER B C   1 
ATOM   3558 O O   . SER B 1 72  ? -24.156 2.456   -54.671 1.00 89.52  ? 72   SER B O   1 
ATOM   3559 C CB  . SER B 1 72  ? -23.671 1.570   -51.356 1.00 86.55  ? 72   SER B CB  1 
ATOM   3560 O OG  . SER B 1 72  ? -22.890 2.748   -51.264 1.00 91.70  ? 72   SER B OG  1 
ATOM   3561 N N   . ARG B 1 73  ? -25.895 1.725   -53.430 1.00 83.06  ? 73   ARG B N   1 
ATOM   3562 C CA  . ARG B 1 73  ? -26.977 2.406   -54.136 1.00 81.38  ? 73   ARG B CA  1 
ATOM   3563 C C   . ARG B 1 73  ? -28.025 2.782   -53.089 1.00 84.25  ? 73   ARG B C   1 
ATOM   3564 O O   . ARG B 1 73  ? -28.188 2.078   -52.092 1.00 83.90  ? 73   ARG B O   1 
ATOM   3565 C CB  . ARG B 1 73  ? -27.618 1.505   -55.223 1.00 77.52  ? 73   ARG B CB  1 
ATOM   3566 C CG  . ARG B 1 73  ? -26.776 1.256   -56.464 1.00 80.16  ? 73   ARG B CG  1 
ATOM   3567 C CD  . ARG B 1 73  ? -26.927 2.319   -57.530 1.00 93.77  ? 73   ARG B CD  1 
ATOM   3568 N NE  . ARG B 1 73  ? -26.296 1.931   -58.802 1.00 103.75 ? 73   ARG B NE  1 
ATOM   3569 C CZ  . ARG B 1 73  ? -25.035 2.197   -59.148 1.00 108.61 ? 73   ARG B CZ  1 
ATOM   3570 N NH1 . ARG B 1 73  ? -24.233 2.856   -58.316 1.00 74.44  ? 73   ARG B NH1 1 
ATOM   3571 N NH2 . ARG B 1 73  ? -24.566 1.798   -60.324 1.00 101.91 ? 73   ARG B NH2 1 
ATOM   3572 N N   . CYS B 1 74  ? -28.725 3.884   -53.304 1.00 80.43  ? 74   CYS B N   1 
ATOM   3573 C CA  . CYS B 1 74  ? -29.793 4.286   -52.402 1.00 80.89  ? 74   CYS B CA  1 
ATOM   3574 C C   . CYS B 1 74  ? -31.007 3.441   -52.738 1.00 85.63  ? 74   CYS B C   1 
ATOM   3575 O O   . CYS B 1 74  ? -31.018 2.839   -53.815 1.00 83.78  ? 74   CYS B O   1 
ATOM   3576 C CB  . CYS B 1 74  ? -30.092 5.775   -52.539 1.00 81.75  ? 74   CYS B CB  1 
ATOM   3577 S SG  . CYS B 1 74  ? -29.160 6.836   -51.402 1.00 85.94  ? 74   CYS B SG  1 
ATOM   3578 N N   . PRO B 1 75  ? -32.039 3.320   -51.867 1.00 85.24  ? 75   PRO B N   1 
ATOM   3579 C CA  . PRO B 1 75  ? -33.200 2.500   -52.252 1.00 86.21  ? 75   PRO B CA  1 
ATOM   3580 C C   . PRO B 1 75  ? -33.795 3.036   -53.543 1.00 95.14  ? 75   PRO B C   1 
ATOM   3581 O O   . PRO B 1 75  ? -33.726 4.254   -53.784 1.00 95.94  ? 75   PRO B O   1 
ATOM   3582 C CB  . PRO B 1 75  ? -34.160 2.679   -51.075 1.00 87.38  ? 75   PRO B CB  1 
ATOM   3583 C CG  . PRO B 1 75  ? -33.304 3.069   -49.958 1.00 91.24  ? 75   PRO B CG  1 
ATOM   3584 C CD  . PRO B 1 75  ? -32.252 3.932   -50.543 1.00 86.36  ? 75   PRO B CD  1 
ATOM   3585 N N   . THR B 1 76  ? -34.322 2.135   -54.406 1.00 93.66  ? 76   THR B N   1 
ATOM   3586 C CA  . THR B 1 76  ? -34.948 2.464   -55.707 1.00 94.09  ? 76   THR B CA  1 
ATOM   3587 C C   . THR B 1 76  ? -33.945 2.953   -56.771 1.00 98.11  ? 76   THR B C   1 
ATOM   3588 O O   . THR B 1 76  ? -34.369 3.241   -57.889 1.00 98.82  ? 76   THR B O   1 
ATOM   3589 C CB  . THR B 1 76  ? -36.153 3.481   -55.590 1.00 104.17 ? 76   THR B CB  1 
ATOM   3590 O OG1 . THR B 1 76  ? -35.679 4.838   -55.693 1.00 107.35 ? 76   THR B OG1 1 
ATOM   3591 C CG2 . THR B 1 76  ? -37.022 3.288   -54.329 1.00 98.92  ? 76   THR B CG2 1 
ATOM   3592 N N   . GLN B 1 77  ? -32.646 3.073   -56.435 1.00 93.90  ? 77   GLN B N   1 
ATOM   3593 C CA  . GLN B 1 77  ? -31.616 3.554   -57.376 1.00 93.58  ? 77   GLN B CA  1 
ATOM   3594 C C   . GLN B 1 77  ? -30.953 2.436   -58.188 1.00 96.15  ? 77   GLN B C   1 
ATOM   3595 O O   . GLN B 1 77  ? -29.985 2.694   -58.910 1.00 96.73  ? 77   GLN B O   1 
ATOM   3596 C CB  . GLN B 1 77  ? -30.540 4.428   -56.687 1.00 94.94  ? 77   GLN B CB  1 
ATOM   3597 C CG  . GLN B 1 77  ? -31.085 5.565   -55.828 1.00 117.75 ? 77   GLN B CG  1 
ATOM   3598 C CD  . GLN B 1 77  ? -31.549 6.782   -56.574 1.00 145.31 ? 77   GLN B CD  1 
ATOM   3599 O OE1 . GLN B 1 77  ? -30.897 7.247   -57.511 1.00 142.62 ? 77   GLN B OE1 1 
ATOM   3600 N NE2 . GLN B 1 77  ? -32.639 7.377   -56.099 1.00 141.50 ? 77   GLN B NE2 1 
ATOM   3601 N N   . GLY B 1 78  ? -31.480 1.222   -58.078 1.00 90.49  ? 78   GLY B N   1 
ATOM   3602 C CA  . GLY B 1 78  ? -30.937 0.069   -58.781 1.00 89.90  ? 78   GLY B CA  1 
ATOM   3603 C C   . GLY B 1 78  ? -29.983 -0.775  -57.956 1.00 92.23  ? 78   GLY B C   1 
ATOM   3604 O O   . GLY B 1 78  ? -29.830 -0.568  -56.739 1.00 93.15  ? 78   GLY B O   1 
ATOM   3605 N N   . GLU B 1 79  ? -29.353 -1.754  -58.634 1.00 85.38  ? 79   GLU B N   1 
ATOM   3606 C CA  . GLU B 1 79  ? -28.395 -2.703  -58.064 1.00 83.95  ? 79   GLU B CA  1 
ATOM   3607 C C   . GLU B 1 79  ? -26.977 -2.190  -58.347 1.00 83.18  ? 79   GLU B C   1 
ATOM   3608 O O   . GLU B 1 79  ? -26.722 -1.734  -59.463 1.00 84.26  ? 79   GLU B O   1 
ATOM   3609 C CB  . GLU B 1 79  ? -28.605 -4.099  -58.684 1.00 85.55  ? 79   GLU B CB  1 
ATOM   3610 C CG  . GLU B 1 79  ? -28.437 -5.266  -57.715 1.00 98.31  ? 79   GLU B CG  1 
ATOM   3611 C CD  . GLU B 1 79  ? -28.433 -6.650  -58.349 1.00 123.81 ? 79   GLU B CD  1 
ATOM   3612 O OE1 . GLU B 1 79  ? -27.906 -6.791  -59.477 1.00 124.29 ? 79   GLU B OE1 1 
ATOM   3613 O OE2 . GLU B 1 79  ? -28.930 -7.604  -57.706 1.00 110.19 ? 79   GLU B OE2 1 
ATOM   3614 N N   . PRO B 1 80  ? -26.045 -2.194  -57.379 1.00 74.30  ? 80   PRO B N   1 
ATOM   3615 C CA  . PRO B 1 80  ? -24.702 -1.687  -57.686 1.00 73.73  ? 80   PRO B CA  1 
ATOM   3616 C C   . PRO B 1 80  ? -23.842 -2.726  -58.401 1.00 79.46  ? 80   PRO B C   1 
ATOM   3617 O O   . PRO B 1 80  ? -24.160 -3.928  -58.397 1.00 80.90  ? 80   PRO B O   1 
ATOM   3618 C CB  . PRO B 1 80  ? -24.141 -1.289  -56.324 1.00 75.32  ? 80   PRO B CB  1 
ATOM   3619 C CG  . PRO B 1 80  ? -24.941 -2.059  -55.328 1.00 79.68  ? 80   PRO B CG  1 
ATOM   3620 C CD  . PRO B 1 80  ? -26.129 -2.695  -55.998 1.00 75.08  ? 80   PRO B CD  1 
ATOM   3621 N N   . SER B 1 81  ? -22.774 -2.263  -59.068 1.00 73.61  ? 81   SER B N   1 
ATOM   3622 C CA  . SER B 1 81  ? -21.909 -3.172  -59.812 1.00 71.68  ? 81   SER B CA  1 
ATOM   3623 C C   . SER B 1 81  ? -20.461 -2.706  -59.849 1.00 75.42  ? 81   SER B C   1 
ATOM   3624 O O   . SER B 1 81  ? -20.193 -1.499  -59.937 1.00 76.67  ? 81   SER B O   1 
ATOM   3625 C CB  . SER B 1 81  ? -22.428 -3.373  -61.232 1.00 71.95  ? 81   SER B CB  1 
ATOM   3626 O OG  . SER B 1 81  ? -22.070 -2.264  -62.037 1.00 79.61  ? 81   SER B OG  1 
ATOM   3627 N N   . LEU B 1 82  ? -19.530 -3.679  -59.815 1.00 68.57  ? 82   LEU B N   1 
ATOM   3628 C CA  . LEU B 1 82  ? -18.099 -3.457  -59.927 1.00 65.87  ? 82   LEU B CA  1 
ATOM   3629 C C   . LEU B 1 82  ? -17.632 -4.289  -61.097 1.00 66.97  ? 82   LEU B C   1 
ATOM   3630 O O   . LEU B 1 82  ? -18.314 -5.246  -61.474 1.00 63.80  ? 82   LEU B O   1 
ATOM   3631 C CB  . LEU B 1 82  ? -17.374 -3.846  -58.637 1.00 65.44  ? 82   LEU B CB  1 
ATOM   3632 C CG  . LEU B 1 82  ? -17.776 -3.084  -57.351 1.00 69.42  ? 82   LEU B CG  1 
ATOM   3633 C CD1 . LEU B 1 82  ? -17.132 -3.705  -56.127 1.00 68.84  ? 82   LEU B CD1 1 
ATOM   3634 C CD2 . LEU B 1 82  ? -17.391 -1.629  -57.427 1.00 72.53  ? 82   LEU B CD2 1 
ATOM   3635 N N   . ASN B 1 83  ? -16.509 -3.892  -61.724 1.00 65.85  ? 83   ASN B N   1 
ATOM   3636 C CA  . ASN B 1 83  ? -15.940 -4.620  -62.886 1.00 66.33  ? 83   ASN B CA  1 
ATOM   3637 C C   . ASN B 1 83  ? -15.438 -5.974  -62.398 1.00 68.86  ? 83   ASN B C   1 
ATOM   3638 O O   . ASN B 1 83  ? -15.664 -7.002  -63.045 1.00 66.90  ? 83   ASN B O   1 
ATOM   3639 C CB  . ASN B 1 83  ? -14.804 -3.823  -63.539 1.00 67.88  ? 83   ASN B CB  1 
ATOM   3640 C CG  . ASN B 1 83  ? -15.191 -2.391  -63.805 1.00 94.63  ? 83   ASN B CG  1 
ATOM   3641 O OD1 . ASN B 1 83  ? -15.786 -2.080  -64.843 1.00 88.65  ? 83   ASN B OD1 1 
ATOM   3642 N ND2 . ASN B 1 83  ? -14.956 -1.507  -62.822 1.00 84.47  ? 83   ASN B ND2 1 
ATOM   3643 N N   . GLU B 1 84  ? -14.820 -5.938  -61.193 1.00 64.28  ? 84   GLU B N   1 
ATOM   3644 C CA  . GLU B 1 84  ? -14.310 -7.007  -60.366 1.00 63.10  ? 84   GLU B CA  1 
ATOM   3645 C C   . GLU B 1 84  ? -15.154 -8.272  -60.414 1.00 68.94  ? 84   GLU B C   1 
ATOM   3646 O O   . GLU B 1 84  ? -14.598 -9.368  -60.341 1.00 70.66  ? 84   GLU B O   1 
ATOM   3647 C CB  . GLU B 1 84  ? -14.239 -6.487  -58.944 1.00 63.91  ? 84   GLU B CB  1 
ATOM   3648 C CG  . GLU B 1 84  ? -12.963 -5.731  -58.656 1.00 77.52  ? 84   GLU B CG  1 
ATOM   3649 C CD  . GLU B 1 84  ? -12.872 -4.289  -59.117 1.00 114.30 ? 84   GLU B CD  1 
ATOM   3650 O OE1 . GLU B 1 84  ? -12.970 -4.036  -60.342 1.00 112.54 ? 84   GLU B OE1 1 
ATOM   3651 O OE2 . GLU B 1 84  ? -12.592 -3.424  -58.254 1.00 113.96 ? 84   GLU B OE2 1 
ATOM   3652 N N   . GLU B 1 85  ? -16.483 -8.131  -60.557 1.00 65.00  ? 85   GLU B N   1 
ATOM   3653 C CA  . GLU B 1 85  ? -17.429 -9.247  -60.648 1.00 65.45  ? 85   GLU B CA  1 
ATOM   3654 C C   . GLU B 1 85  ? -17.170 -10.096 -61.873 1.00 71.03  ? 85   GLU B C   1 
ATOM   3655 O O   . GLU B 1 85  ? -17.736 -11.177 -62.008 1.00 70.50  ? 85   GLU B O   1 
ATOM   3656 C CB  . GLU B 1 85  ? -18.870 -8.743  -60.668 1.00 67.01  ? 85   GLU B CB  1 
ATOM   3657 C CG  . GLU B 1 85  ? -19.210 -7.842  -59.496 1.00 77.35  ? 85   GLU B CG  1 
ATOM   3658 C CD  . GLU B 1 85  ? -20.597 -7.264  -59.625 1.00 88.57  ? 85   GLU B CD  1 
ATOM   3659 O OE1 . GLU B 1 85  ? -21.570 -7.941  -59.224 1.00 79.11  ? 85   GLU B OE1 1 
ATOM   3660 O OE2 . GLU B 1 85  ? -20.715 -6.163  -60.202 1.00 76.37  ? 85   GLU B OE2 1 
ATOM   3661 N N   . GLN B 1 86  ? -16.285 -9.609  -62.748 1.00 70.00  ? 86   GLN B N   1 
ATOM   3662 C CA  . GLN B 1 86  ? -15.853 -10.250 -64.000 1.00 70.39  ? 86   GLN B CA  1 
ATOM   3663 C C   . GLN B 1 86  ? -14.363 -10.725 -63.895 1.00 70.58  ? 86   GLN B C   1 
ATOM   3664 O O   . GLN B 1 86  ? -13.921 -11.590 -64.662 1.00 68.40  ? 86   GLN B O   1 
ATOM   3665 C CB  . GLN B 1 86  ? -16.164 -9.330  -65.214 1.00 72.21  ? 86   GLN B CB  1 
ATOM   3666 C CG  . GLN B 1 86  ? -17.661 -8.886  -65.243 1.00 96.65  ? 86   GLN B CG  1 
ATOM   3667 C CD  . GLN B 1 86  ? -18.027 -7.738  -66.177 1.00 119.09 ? 86   GLN B CD  1 
ATOM   3668 O OE1 . GLN B 1 86  ? -17.300 -6.735  -66.321 1.00 114.84 ? 86   GLN B OE1 1 
ATOM   3669 N NE2 . GLN B 1 86  ? -19.219 -7.830  -66.776 1.00 104.65 ? 86   GLN B NE2 1 
ATOM   3670 N N   . ASP B 1 87  ? -13.637 -10.220 -62.868 1.00 65.59  ? 87   ASP B N   1 
ATOM   3671 C CA  . ASP B 1 87  ? -12.279 -10.660 -62.560 1.00 64.72  ? 87   ASP B CA  1 
ATOM   3672 C C   . ASP B 1 87  ? -12.396 -11.963 -61.743 1.00 69.28  ? 87   ASP B C   1 
ATOM   3673 O O   . ASP B 1 87  ? -13.014 -11.972 -60.662 1.00 70.77  ? 87   ASP B O   1 
ATOM   3674 C CB  . ASP B 1 87  ? -11.503 -9.579  -61.782 1.00 65.73  ? 87   ASP B CB  1 
ATOM   3675 C CG  . ASP B 1 87  ? -9.988  -9.763  -61.747 1.00 73.96  ? 87   ASP B CG  1 
ATOM   3676 O OD1 . ASP B 1 87  ? -9.497  -10.840 -62.166 1.00 72.35  ? 87   ASP B OD1 1 
ATOM   3677 O OD2 . ASP B 1 87  ? -9.293  -8.825  -61.331 1.00 83.82  ? 87   ASP B OD2 1 
ATOM   3678 N N   . LYS B 1 88  ? -11.838 -13.061 -62.271 1.00 63.53  ? 88   LYS B N   1 
ATOM   3679 C CA  . LYS B 1 88  ? -11.920 -14.360 -61.620 1.00 63.07  ? 88   LYS B CA  1 
ATOM   3680 C C   . LYS B 1 88  ? -10.923 -14.552 -60.463 1.00 67.11  ? 88   LYS B C   1 
ATOM   3681 O O   . LYS B 1 88  ? -10.751 -15.680 -59.989 1.00 68.91  ? 88   LYS B O   1 
ATOM   3682 C CB  . LYS B 1 88  ? -11.779 -15.479 -62.655 1.00 66.67  ? 88   LYS B CB  1 
ATOM   3683 C CG  . LYS B 1 88  ? -13.007 -15.744 -63.520 1.00 92.42  ? 88   LYS B CG  1 
ATOM   3684 C CD  . LYS B 1 88  ? -12.597 -16.530 -64.784 1.00 109.74 ? 88   LYS B CD  1 
ATOM   3685 C CE  . LYS B 1 88  ? -13.605 -17.564 -65.236 1.00 124.22 ? 88   LYS B CE  1 
ATOM   3686 N NZ  . LYS B 1 88  ? -13.185 -18.234 -66.500 1.00 132.13 ? 88   LYS B NZ  1 
ATOM   3687 N N   . ARG B 1 89  ? -10.289 -13.470 -59.993 1.00 61.31  ? 89   ARG B N   1 
ATOM   3688 C CA  . ARG B 1 89  ? -9.307  -13.491 -58.901 1.00 60.15  ? 89   ARG B CA  1 
ATOM   3689 C C   . ARG B 1 89  ? -9.885  -12.753 -57.715 1.00 65.52  ? 89   ARG B C   1 
ATOM   3690 O O   . ARG B 1 89  ? -9.234  -12.583 -56.678 1.00 66.66  ? 89   ARG B O   1 
ATOM   3691 C CB  . ARG B 1 89  ? -8.005  -12.818 -59.365 1.00 56.55  ? 89   ARG B CB  1 
ATOM   3692 C CG  . ARG B 1 89  ? -7.423  -13.518 -60.586 1.00 62.98  ? 89   ARG B CG  1 
ATOM   3693 C CD  . ARG B 1 89  ? -6.281  -12.760 -61.205 1.00 76.22  ? 89   ARG B CD  1 
ATOM   3694 N NE  . ARG B 1 89  ? -6.680  -11.489 -61.817 1.00 82.58  ? 89   ARG B NE  1 
ATOM   3695 C CZ  . ARG B 1 89  ? -5.956  -10.374 -61.753 1.00 92.65  ? 89   ARG B CZ  1 
ATOM   3696 N NH1 . ARG B 1 89  ? -4.797  -10.360 -61.096 1.00 64.94  ? 89   ARG B NH1 1 
ATOM   3697 N NH2 . ARG B 1 89  ? -6.384  -9.265  -62.339 1.00 83.86  ? 89   ARG B NH2 1 
ATOM   3698 N N   . PHE B 1 90  ? -11.117 -12.297 -57.887 1.00 61.26  ? 90   PHE B N   1 
ATOM   3699 C CA  . PHE B 1 90  ? -11.846 -11.519 -56.911 1.00 60.62  ? 90   PHE B CA  1 
ATOM   3700 C C   . PHE B 1 90  ? -12.992 -12.295 -56.346 1.00 64.56  ? 90   PHE B C   1 
ATOM   3701 O O   . PHE B 1 90  ? -13.553 -13.176 -57.019 1.00 65.27  ? 90   PHE B O   1 
ATOM   3702 C CB  . PHE B 1 90  ? -12.342 -10.214 -57.559 1.00 62.05  ? 90   PHE B CB  1 
ATOM   3703 C CG  . PHE B 1 90  ? -11.320 -9.113  -57.440 1.00 63.04  ? 90   PHE B CG  1 
ATOM   3704 C CD1 . PHE B 1 90  ? -11.267 -8.309  -56.305 1.00 65.19  ? 90   PHE B CD1 1 
ATOM   3705 C CD2 . PHE B 1 90  ? -10.366 -8.922  -58.426 1.00 64.60  ? 90   PHE B CD2 1 
ATOM   3706 C CE1 . PHE B 1 90  ? -10.294 -7.316  -56.173 1.00 67.18  ? 90   PHE B CE1 1 
ATOM   3707 C CE2 . PHE B 1 90  ? -9.391  -7.932  -58.293 1.00 65.06  ? 90   PHE B CE2 1 
ATOM   3708 C CZ  . PHE B 1 90  ? -9.364  -7.135  -57.171 1.00 64.52  ? 90   PHE B CZ  1 
ATOM   3709 N N   . ILE B 1 91  ? -13.352 -11.969 -55.111 1.00 59.34  ? 91   ILE B N   1 
ATOM   3710 C CA  . ILE B 1 91  ? -14.476 -12.615 -54.446 1.00 59.36  ? 91   ILE B CA  1 
ATOM   3711 C C   . ILE B 1 91  ? -15.532 -11.533 -54.175 1.00 67.78  ? 91   ILE B C   1 
ATOM   3712 O O   . ILE B 1 91  ? -15.207 -10.500 -53.565 1.00 67.02  ? 91   ILE B O   1 
ATOM   3713 C CB  . ILE B 1 91  ? -14.026 -13.495 -53.212 1.00 60.89  ? 91   ILE B CB  1 
ATOM   3714 C CG1 . ILE B 1 91  ? -15.206 -14.163 -52.487 1.00 60.19  ? 91   ILE B CG1 1 
ATOM   3715 C CG2 . ILE B 1 91  ? -13.136 -12.747 -52.224 1.00 59.46  ? 91   ILE B CG2 1 
ATOM   3716 C CD1 . ILE B 1 91  ? -15.699 -15.379 -53.109 1.00 66.04  ? 91   ILE B CD1 1 
ATOM   3717 N N   . CYS B 1 92  ? -16.765 -11.715 -54.727 1.00 66.85  ? 92   CYS B N   1 
ATOM   3718 C CA  . CYS B 1 92  ? -17.823 -10.709 -54.562 1.00 67.43  ? 92   CYS B CA  1 
ATOM   3719 C C   . CYS B 1 92  ? -19.075 -11.241 -53.888 1.00 71.40  ? 92   CYS B C   1 
ATOM   3720 O O   . CYS B 1 92  ? -19.373 -12.444 -53.943 1.00 70.62  ? 92   CYS B O   1 
ATOM   3721 C CB  . CYS B 1 92  ? -18.162 -10.018 -55.883 1.00 67.87  ? 92   CYS B CB  1 
ATOM   3722 S SG  . CYS B 1 92  ? -16.732 -9.310  -56.742 1.00 72.24  ? 92   CYS B SG  1 
ATOM   3723 N N   . LYS B 1 93  ? -19.826 -10.304 -53.281 1.00 67.52  ? 93   LYS B N   1 
ATOM   3724 C CA  . LYS B 1 93  ? -21.095 -10.570 -52.636 1.00 67.19  ? 93   LYS B CA  1 
ATOM   3725 C C   . LYS B 1 93  ? -21.932 -9.323  -52.647 1.00 72.54  ? 93   LYS B C   1 
ATOM   3726 O O   . LYS B 1 93  ? -21.447 -8.230  -52.329 1.00 70.99  ? 93   LYS B O   1 
ATOM   3727 C CB  . LYS B 1 93  ? -20.886 -11.072 -51.189 1.00 69.61  ? 93   LYS B CB  1 
ATOM   3728 C CG  . LYS B 1 93  ? -22.135 -11.163 -50.285 1.00 71.03  ? 93   LYS B CG  1 
ATOM   3729 C CD  . LYS B 1 93  ? -22.840 -12.510 -50.327 1.00 71.40  ? 93   LYS B CD  1 
ATOM   3730 C CE  . LYS B 1 93  ? -23.864 -12.668 -49.229 1.00 75.24  ? 93   LYS B CE  1 
ATOM   3731 N NZ  . LYS B 1 93  ? -23.246 -12.658 -47.873 1.00 90.70  ? 93   LYS B NZ  1 
ATOM   3732 N N   . HIS B 1 94  ? -23.212 -9.509  -52.997 1.00 72.12  ? 94   HIS B N   1 
ATOM   3733 C CA  . HIS B 1 94  ? -24.246 -8.490  -52.941 1.00 73.62  ? 94   HIS B CA  1 
ATOM   3734 C C   . HIS B 1 94  ? -25.007 -8.640  -51.638 1.00 77.86  ? 94   HIS B C   1 
ATOM   3735 O O   . HIS B 1 94  ? -25.291 -9.758  -51.211 1.00 77.55  ? 94   HIS B O   1 
ATOM   3736 C CB  . HIS B 1 94  ? -25.243 -8.683  -54.074 1.00 75.39  ? 94   HIS B CB  1 
ATOM   3737 C CG  . HIS B 1 94  ? -24.786 -8.109  -55.357 1.00 79.46  ? 94   HIS B CG  1 
ATOM   3738 N ND1 . HIS B 1 94  ? -25.197 -6.862  -55.766 1.00 81.51  ? 94   HIS B ND1 1 
ATOM   3739 C CD2 . HIS B 1 94  ? -23.962 -8.641  -56.291 1.00 81.90  ? 94   HIS B CD2 1 
ATOM   3740 C CE1 . HIS B 1 94  ? -24.611 -6.669  -56.936 1.00 81.53  ? 94   HIS B CE1 1 
ATOM   3741 N NE2 . HIS B 1 94  ? -23.859 -7.717  -57.294 1.00 81.88  ? 94   HIS B NE2 1 
ATOM   3742 N N   . SER B 1 95  ? -25.367 -7.525  -51.026 1.00 75.69  ? 95   SER B N   1 
ATOM   3743 C CA  . SER B 1 95  ? -26.168 -7.516  -49.812 1.00 76.42  ? 95   SER B CA  1 
ATOM   3744 C C   . SER B 1 95  ? -27.063 -6.288  -49.805 1.00 80.89  ? 95   SER B C   1 
ATOM   3745 O O   . SER B 1 95  ? -27.161 -5.592  -50.814 1.00 81.24  ? 95   SER B O   1 
ATOM   3746 C CB  . SER B 1 95  ? -25.292 -7.587  -48.563 1.00 81.62  ? 95   SER B CB  1 
ATOM   3747 O OG  . SER B 1 95  ? -25.838 -8.470  -47.595 1.00 91.84  ? 95   SER B OG  1 
ATOM   3748 N N   . MET B 1 96  ? -27.737 -6.042  -48.686 1.00 77.45  ? 96   MET B N   1 
ATOM   3749 C CA  . MET B 1 96  ? -28.683 -4.950  -48.497 1.00 76.68  ? 96   MET B CA  1 
ATOM   3750 C C   . MET B 1 96  ? -28.350 -4.239  -47.197 1.00 74.55  ? 96   MET B C   1 
ATOM   3751 O O   . MET B 1 96  ? -28.203 -4.884  -46.158 1.00 75.30  ? 96   MET B O   1 
ATOM   3752 C CB  . MET B 1 96  ? -30.108 -5.535  -48.362 1.00 79.87  ? 96   MET B CB  1 
ATOM   3753 C CG  . MET B 1 96  ? -30.605 -6.290  -49.575 1.00 84.59  ? 96   MET B CG  1 
ATOM   3754 S SD  . MET B 1 96  ? -31.552 -5.152  -50.615 1.00 90.20  ? 96   MET B SD  1 
ATOM   3755 C CE  . MET B 1 96  ? -30.729 -5.387  -52.206 1.00 87.30  ? 96   MET B CE  1 
ATOM   3756 N N   . VAL B 1 97  ? -28.275 -2.929  -47.237 1.00 65.62  ? 97   VAL B N   1 
ATOM   3757 C CA  . VAL B 1 97  ? -28.060 -2.128  -46.042 1.00 64.12  ? 97   VAL B CA  1 
ATOM   3758 C C   . VAL B 1 97  ? -29.254 -1.185  -45.817 1.00 69.09  ? 97   VAL B C   1 
ATOM   3759 O O   . VAL B 1 97  ? -30.027 -0.922  -46.737 1.00 69.52  ? 97   VAL B O   1 
ATOM   3760 C CB  . VAL B 1 97  ? -26.710 -1.364  -46.010 1.00 66.66  ? 97   VAL B CB  1 
ATOM   3761 C CG1 . VAL B 1 97  ? -25.535 -2.309  -45.981 1.00 66.35  ? 97   VAL B CG1 1 
ATOM   3762 C CG2 . VAL B 1 97  ? -26.576 -0.369  -47.141 1.00 66.15  ? 97   VAL B CG2 1 
ATOM   3763 N N   . ASP B 1 98  ? -29.395 -0.669  -44.599 1.00 64.86  ? 98   ASP B N   1 
ATOM   3764 C CA  . ASP B 1 98  ? -30.432 0.284   -44.273 1.00 63.95  ? 98   ASP B CA  1 
ATOM   3765 C C   . ASP B 1 98  ? -29.965 1.611   -44.767 1.00 68.24  ? 98   ASP B C   1 
ATOM   3766 O O   . ASP B 1 98  ? -28.875 2.085   -44.418 1.00 67.83  ? 98   ASP B O   1 
ATOM   3767 C CB  . ASP B 1 98  ? -30.708 0.378   -42.765 1.00 64.80  ? 98   ASP B CB  1 
ATOM   3768 C CG  . ASP B 1 98  ? -31.448 -0.791  -42.174 1.00 64.56  ? 98   ASP B CG  1 
ATOM   3769 O OD1 . ASP B 1 98  ? -32.197 -1.473  -42.929 1.00 59.99  ? 98   ASP B OD1 1 
ATOM   3770 O OD2 . ASP B 1 98  ? -31.304 -1.015  -40.951 1.00 70.95  ? 98   ASP B OD2 1 
ATOM   3771 N N   . ARG B 1 99  ? -30.788 2.189   -45.613 1.00 64.86  ? 99   ARG B N   1 
ATOM   3772 C CA  . ARG B 1 99  ? -30.567 3.494   -46.170 1.00 63.80  ? 99   ARG B CA  1 
ATOM   3773 C C   . ARG B 1 99  ? -31.716 4.387   -45.740 1.00 66.97  ? 99   ARG B C   1 
ATOM   3774 O O   . ARG B 1 99  ? -32.726 3.902   -45.228 1.00 63.51  ? 99   ARG B O   1 
ATOM   3775 C CB  . ARG B 1 99  ? -30.385 3.433   -47.698 1.00 60.65  ? 99   ARG B CB  1 
ATOM   3776 C CG  . ARG B 1 99  ? -29.112 2.751   -48.227 1.00 59.27  ? 99   ARG B CG  1 
ATOM   3777 C CD  . ARG B 1 99  ? -27.779 3.229   -47.660 1.00 59.49  ? 99   ARG B CD  1 
ATOM   3778 N NE  . ARG B 1 99  ? -27.370 4.567   -48.078 1.00 66.62  ? 99   ARG B NE  1 
ATOM   3779 C CZ  . ARG B 1 99  ? -26.694 4.846   -49.192 1.00 76.96  ? 99   ARG B CZ  1 
ATOM   3780 N NH1 . ARG B 1 99  ? -26.415 3.882   -50.074 1.00 53.22  ? 99   ARG B NH1 1 
ATOM   3781 N NH2 . ARG B 1 99  ? -26.346 6.096   -49.466 1.00 70.83  ? 99   ARG B NH2 1 
ATOM   3782 N N   . GLY B 1 100 ? -31.504 5.680   -45.906 1.00 67.41  ? 100  GLY B N   1 
ATOM   3783 C CA  . GLY B 1 100 ? -32.431 6.742   -45.550 1.00 69.03  ? 100  GLY B CA  1 
ATOM   3784 C C   . GLY B 1 100 ? -31.724 8.067   -45.341 1.00 75.48  ? 100  GLY B C   1 
ATOM   3785 O O   . GLY B 1 100 ? -30.529 8.203   -45.648 1.00 76.43  ? 100  GLY B O   1 
ATOM   3786 N N   . TRP B 1 101 ? -32.481 9.065   -44.836 1.00 71.52  ? 101  TRP B N   1 
ATOM   3787 C CA  . TRP B 1 101 ? -31.976 10.381  -44.503 1.00 71.62  ? 101  TRP B CA  1 
ATOM   3788 C C   . TRP B 1 101 ? -31.094 9.982   -43.313 1.00 80.02  ? 101  TRP B C   1 
ATOM   3789 O O   . TRP B 1 101 ? -31.427 9.049   -42.548 1.00 80.86  ? 101  TRP B O   1 
ATOM   3790 C CB  . TRP B 1 101 ? -33.071 11.312  -43.931 1.00 69.88  ? 101  TRP B CB  1 
ATOM   3791 C CG  . TRP B 1 101 ? -34.351 11.509  -44.699 1.00 70.68  ? 101  TRP B CG  1 
ATOM   3792 C CD1 . TRP B 1 101 ? -34.728 10.903  -45.861 1.00 73.73  ? 101  TRP B CD1 1 
ATOM   3793 C CD2 . TRP B 1 101 ? -35.456 12.341  -44.305 1.00 70.33  ? 101  TRP B CD2 1 
ATOM   3794 N NE1 . TRP B 1 101 ? -36.001 11.300  -46.214 1.00 73.22  ? 101  TRP B NE1 1 
ATOM   3795 C CE2 . TRP B 1 101 ? -36.467 12.189  -45.281 1.00 74.09  ? 101  TRP B CE2 1 
ATOM   3796 C CE3 . TRP B 1 101 ? -35.689 13.211  -43.219 1.00 71.47  ? 101  TRP B CE3 1 
ATOM   3797 C CZ2 . TRP B 1 101 ? -37.680 12.890  -45.221 1.00 72.93  ? 101  TRP B CZ2 1 
ATOM   3798 C CZ3 . TRP B 1 101 ? -36.906 13.876  -43.140 1.00 72.62  ? 101  TRP B CZ3 1 
ATOM   3799 C CH2 . TRP B 1 101 ? -37.878 13.724  -44.141 1.00 73.19  ? 101  TRP B CH2 1 
ATOM   3800 N N   . GLY B 1 102 ? -29.985 10.645  -43.150 1.00 77.53  ? 102  GLY B N   1 
ATOM   3801 C CA  . GLY B 1 102 ? -29.097 10.265  -42.063 1.00 77.17  ? 102  GLY B CA  1 
ATOM   3802 C C   . GLY B 1 102 ? -27.907 9.491   -42.559 1.00 81.36  ? 102  GLY B C   1 
ATOM   3803 O O   . GLY B 1 102 ? -26.895 9.419   -41.855 1.00 81.10  ? 102  GLY B O   1 
ATOM   3804 N N   . ASN B 1 103 ? -28.024 8.913   -43.779 1.00 78.81  ? 103  ASN B N   1 
ATOM   3805 C CA  . ASN B 1 103 ? -26.949 8.189   -44.478 1.00 79.17  ? 103  ASN B CA  1 
ATOM   3806 C C   . ASN B 1 103 ? -27.025 8.413   -46.019 1.00 84.12  ? 103  ASN B C   1 
ATOM   3807 O O   . ASN B 1 103 ? -26.568 7.591   -46.818 1.00 82.87  ? 103  ASN B O   1 
ATOM   3808 C CB  . ASN B 1 103 ? -26.844 6.711   -44.075 1.00 77.54  ? 103  ASN B CB  1 
ATOM   3809 C CG  . ASN B 1 103 ? -28.036 5.873   -44.429 1.00 92.91  ? 103  ASN B CG  1 
ATOM   3810 O OD1 . ASN B 1 103 ? -28.214 5.476   -45.576 1.00 76.96  ? 103  ASN B OD1 1 
ATOM   3811 N ND2 . ASN B 1 103 ? -28.841 5.525   -43.437 1.00 88.81  ? 103  ASN B ND2 1 
ATOM   3812 N N   . GLY B 1 104 ? -27.581 9.569   -46.386 1.00 81.67  ? 104  GLY B N   1 
ATOM   3813 C CA  . GLY B 1 104 ? -27.615 10.091  -47.743 1.00 81.35  ? 104  GLY B CA  1 
ATOM   3814 C C   . GLY B 1 104 ? -28.767 9.833   -48.677 1.00 85.62  ? 104  GLY B C   1 
ATOM   3815 O O   . GLY B 1 104 ? -28.694 10.299  -49.813 1.00 85.93  ? 104  GLY B O   1 
ATOM   3816 N N   . CYS B 1 105 ? -29.823 9.120   -48.256 1.00 82.13  ? 105  CYS B N   1 
ATOM   3817 C CA  . CYS B 1 105 ? -30.939 8.810   -49.163 1.00 81.41  ? 105  CYS B CA  1 
ATOM   3818 C C   . CYS B 1 105 ? -32.204 9.596   -48.895 1.00 83.82  ? 105  CYS B C   1 
ATOM   3819 O O   . CYS B 1 105 ? -32.625 9.716   -47.748 1.00 83.94  ? 105  CYS B O   1 
ATOM   3820 C CB  . CYS B 1 105 ? -31.231 7.316   -49.183 1.00 81.84  ? 105  CYS B CB  1 
ATOM   3821 S SG  . CYS B 1 105 ? -29.798 6.282   -49.567 1.00 85.90  ? 105  CYS B SG  1 
ATOM   3822 N N   . GLY B 1 106 ? -32.849 10.040  -49.971 1.00 78.24  ? 106  GLY B N   1 
ATOM   3823 C CA  . GLY B 1 106 ? -34.117 10.762  -49.898 1.00 76.74  ? 106  GLY B CA  1 
ATOM   3824 C C   . GLY B 1 106 ? -35.261 9.881   -49.434 1.00 77.23  ? 106  GLY B C   1 
ATOM   3825 O O   . GLY B 1 106 ? -36.206 10.360  -48.804 1.00 75.96  ? 106  GLY B O   1 
ATOM   3826 N N   . LEU B 1 107 ? -35.160 8.578   -49.739 1.00 72.39  ? 107  LEU B N   1 
ATOM   3827 C CA  . LEU B 1 107 ? -36.120 7.544   -49.356 1.00 72.02  ? 107  LEU B CA  1 
ATOM   3828 C C   . LEU B 1 107 ? -35.506 6.645   -48.278 1.00 74.91  ? 107  LEU B C   1 
ATOM   3829 O O   . LEU B 1 107 ? -34.280 6.535   -48.203 1.00 75.29  ? 107  LEU B O   1 
ATOM   3830 C CB  . LEU B 1 107 ? -36.468 6.663   -50.562 1.00 71.88  ? 107  LEU B CB  1 
ATOM   3831 C CG  . LEU B 1 107 ? -37.054 7.310   -51.791 1.00 75.24  ? 107  LEU B CG  1 
ATOM   3832 C CD1 . LEU B 1 107 ? -35.963 7.609   -52.813 1.00 75.21  ? 107  LEU B CD1 1 
ATOM   3833 C CD2 . LEU B 1 107 ? -38.084 6.366   -52.412 1.00 75.27  ? 107  LEU B CD2 1 
ATOM   3834 N N   . PHE B 1 108 ? -36.355 5.994   -47.470 1.00 69.21  ? 108  PHE B N   1 
ATOM   3835 C CA  . PHE B 1 108 ? -35.935 5.082   -46.411 1.00 67.66  ? 108  PHE B CA  1 
ATOM   3836 C C   . PHE B 1 108 ? -36.202 3.640   -46.828 1.00 70.08  ? 108  PHE B C   1 
ATOM   3837 O O   . PHE B 1 108 ? -37.369 3.255   -47.050 1.00 69.23  ? 108  PHE B O   1 
ATOM   3838 C CB  . PHE B 1 108 ? -36.715 5.353   -45.135 1.00 68.82  ? 108  PHE B CB  1 
ATOM   3839 C CG  . PHE B 1 108 ? -36.453 6.660   -44.452 1.00 69.82  ? 108  PHE B CG  1 
ATOM   3840 C CD1 . PHE B 1 108 ? -35.451 6.769   -43.491 1.00 72.08  ? 108  PHE B CD1 1 
ATOM   3841 C CD2 . PHE B 1 108 ? -37.290 7.754   -44.669 1.00 71.52  ? 108  PHE B CD2 1 
ATOM   3842 C CE1 . PHE B 1 108 ? -35.251 7.969   -42.802 1.00 73.10  ? 108  PHE B CE1 1 
ATOM   3843 C CE2 . PHE B 1 108 ? -37.098 8.951   -43.973 1.00 73.89  ? 108  PHE B CE2 1 
ATOM   3844 C CZ  . PHE B 1 108 ? -36.083 9.051   -43.042 1.00 71.91  ? 108  PHE B CZ  1 
ATOM   3845 N N   . GLY B 1 109 ? -35.140 2.837   -46.868 1.00 64.92  ? 109  GLY B N   1 
ATOM   3846 C CA  . GLY B 1 109 ? -35.286 1.437   -47.247 1.00 63.77  ? 109  GLY B CA  1 
ATOM   3847 C C   . GLY B 1 109 ? -33.998 0.665   -47.335 1.00 63.93  ? 109  GLY B C   1 
ATOM   3848 O O   . GLY B 1 109 ? -32.978 1.093   -46.812 1.00 62.24  ? 109  GLY B O   1 
ATOM   3849 N N   . LYS B 1 110 ? -34.053 -0.479  -47.996 1.00 60.02  ? 110  LYS B N   1 
ATOM   3850 C CA  . LYS B 1 110 ? -32.913 -1.358  -48.142 1.00 59.82  ? 110  LYS B CA  1 
ATOM   3851 C C   . LYS B 1 110 ? -32.108 -1.058  -49.424 1.00 64.07  ? 110  LYS B C   1 
ATOM   3852 O O   . LYS B 1 110 ? -32.490 -1.464  -50.534 1.00 61.56  ? 110  LYS B O   1 
ATOM   3853 C CB  . LYS B 1 110 ? -33.346 -2.842  -48.038 1.00 61.57  ? 110  LYS B CB  1 
ATOM   3854 C CG  . LYS B 1 110 ? -33.991 -3.257  -46.710 1.00 61.18  ? 110  LYS B CG  1 
ATOM   3855 C CD  . LYS B 1 110 ? -32.994 -3.423  -45.580 1.00 69.84  ? 110  LYS B CD  1 
ATOM   3856 C CE  . LYS B 1 110 ? -33.585 -4.173  -44.417 1.00 84.56  ? 110  LYS B CE  1 
ATOM   3857 N NZ  . LYS B 1 110 ? -32.683 -4.195  -43.232 1.00 94.96  ? 110  LYS B NZ  1 
ATOM   3858 N N   . GLY B 1 111 ? -31.013 -0.321  -49.239 1.00 62.12  ? 111  GLY B N   1 
ATOM   3859 C CA  . GLY B 1 111 ? -30.095 0.037   -50.307 1.00 62.48  ? 111  GLY B CA  1 
ATOM   3860 C C   . GLY B 1 111 ? -29.120 -1.078  -50.592 1.00 68.73  ? 111  GLY B C   1 
ATOM   3861 O O   . GLY B 1 111 ? -28.484 -1.586  -49.679 1.00 68.84  ? 111  GLY B O   1 
ATOM   3862 N N   . GLY B 1 112 ? -29.039 -1.478  -51.853 1.00 66.85  ? 112  GLY B N   1 
ATOM   3863 C CA  . GLY B 1 112 ? -28.158 -2.541  -52.314 1.00 66.91  ? 112  GLY B CA  1 
ATOM   3864 C C   . GLY B 1 112 ? -26.687 -2.199  -52.192 1.00 71.03  ? 112  GLY B C   1 
ATOM   3865 O O   . GLY B 1 112 ? -26.269 -1.086  -52.516 1.00 70.11  ? 112  GLY B O   1 
ATOM   3866 N N   . ILE B 1 113 ? -25.902 -3.160  -51.696 1.00 67.67  ? 113  ILE B N   1 
ATOM   3867 C CA  . ILE B 1 113 ? -24.464 -3.040  -51.498 1.00 66.37  ? 113  ILE B CA  1 
ATOM   3868 C C   . ILE B 1 113 ? -23.782 -4.183  -52.236 1.00 73.81  ? 113  ILE B C   1 
ATOM   3869 O O   . ILE B 1 113 ? -24.412 -5.210  -52.502 1.00 74.59  ? 113  ILE B O   1 
ATOM   3870 C CB  . ILE B 1 113 ? -24.127 -3.016  -49.981 1.00 67.70  ? 113  ILE B CB  1 
ATOM   3871 C CG1 . ILE B 1 113 ? -22.838 -2.223  -49.708 1.00 67.41  ? 113  ILE B CG1 1 
ATOM   3872 C CG2 . ILE B 1 113 ? -24.103 -4.410  -49.364 1.00 66.91  ? 113  ILE B CG2 1 
ATOM   3873 C CD1 . ILE B 1 113 ? -22.268 -2.289  -48.226 1.00 72.87  ? 113  ILE B CD1 1 
ATOM   3874 N N   . VAL B 1 114 ? -22.503 -3.994  -52.585 1.00 70.77  ? 114  VAL B N   1 
ATOM   3875 C CA  . VAL B 1 114 ? -21.667 -5.003  -53.236 1.00 69.41  ? 114  VAL B CA  1 
ATOM   3876 C C   . VAL B 1 114 ? -20.210 -4.805  -52.771 1.00 70.99  ? 114  VAL B C   1 
ATOM   3877 O O   . VAL B 1 114 ? -19.689 -3.682  -52.779 1.00 68.25  ? 114  VAL B O   1 
ATOM   3878 C CB  . VAL B 1 114 ? -21.848 -5.128  -54.784 1.00 72.26  ? 114  VAL B CB  1 
ATOM   3879 C CG1 . VAL B 1 114 ? -21.451 -3.855  -55.512 1.00 72.19  ? 114  VAL B CG1 1 
ATOM   3880 C CG2 . VAL B 1 114 ? -21.088 -6.327  -55.342 1.00 71.86  ? 114  VAL B CG2 1 
ATOM   3881 N N   . THR B 1 115 ? -19.589 -5.902  -52.315 1.00 67.50  ? 115  THR B N   1 
ATOM   3882 C CA  . THR B 1 115 ? -18.208 -5.891  -51.845 1.00 66.85  ? 115  THR B CA  1 
ATOM   3883 C C   . THR B 1 115 ? -17.393 -6.947  -52.626 1.00 68.90  ? 115  THR B C   1 
ATOM   3884 O O   . THR B 1 115 ? -17.855 -8.084  -52.783 1.00 66.65  ? 115  THR B O   1 
ATOM   3885 C CB  . THR B 1 115 ? -18.165 -6.107  -50.311 1.00 72.91  ? 115  THR B CB  1 
ATOM   3886 O OG1 . THR B 1 115 ? -19.194 -5.353  -49.636 1.00 73.67  ? 115  THR B OG1 1 
ATOM   3887 C CG2 . THR B 1 115 ? -16.795 -5.809  -49.721 1.00 64.79  ? 115  THR B CG2 1 
ATOM   3888 N N   . CYS B 1 116 ? -16.192 -6.547  -53.118 1.00 66.27  ? 116  CYS B N   1 
ATOM   3889 C CA  . CYS B 1 116 ? -15.224 -7.403  -53.816 1.00 66.55  ? 116  CYS B CA  1 
ATOM   3890 C C   . CYS B 1 116 ? -13.860 -7.272  -53.178 1.00 69.21  ? 116  CYS B C   1 
ATOM   3891 O O   . CYS B 1 116 ? -13.463 -6.168  -52.797 1.00 68.04  ? 116  CYS B O   1 
ATOM   3892 C CB  . CYS B 1 116 ? -15.148 -7.091  -55.301 1.00 67.61  ? 116  CYS B CB  1 
ATOM   3893 S SG  . CYS B 1 116 ? -16.690 -7.354  -56.187 1.00 72.40  ? 116  CYS B SG  1 
ATOM   3894 N N   . ALA B 1 117 ? -13.134 -8.395  -53.085 1.00 64.88  ? 117  ALA B N   1 
ATOM   3895 C CA  . ALA B 1 117 ? -11.778 -8.450  -52.541 1.00 63.41  ? 117  ALA B CA  1 
ATOM   3896 C C   . ALA B 1 117 ? -10.949 -9.453  -53.326 1.00 65.55  ? 117  ALA B C   1 
ATOM   3897 O O   . ALA B 1 117 ? -11.508 -10.370 -53.933 1.00 66.16  ? 117  ALA B O   1 
ATOM   3898 C CB  . ALA B 1 117 ? -11.815 -8.815  -51.079 1.00 63.95  ? 117  ALA B CB  1 
ATOM   3899 N N   . LYS B 1 118 ? -9.631  -9.241  -53.383 1.00 59.48  ? 118  LYS B N   1 
ATOM   3900 C CA  . LYS B 1 118 ? -8.731  -10.102 -54.151 1.00 58.64  ? 118  LYS B CA  1 
ATOM   3901 C C   . LYS B 1 118 ? -8.202  -11.254 -53.331 1.00 61.85  ? 118  LYS B C   1 
ATOM   3902 O O   . LYS B 1 118 ? -7.455  -11.059 -52.352 1.00 60.62  ? 118  LYS B O   1 
ATOM   3903 C CB  . LYS B 1 118 ? -7.584  -9.312  -54.806 1.00 61.33  ? 118  LYS B CB  1 
ATOM   3904 C CG  . LYS B 1 118 ? -7.127  -9.926  -56.119 1.00 73.42  ? 118  LYS B CG  1 
ATOM   3905 C CD  . LYS B 1 118 ? -5.760  -9.407  -56.531 1.00 87.19  ? 118  LYS B CD  1 
ATOM   3906 C CE  . LYS B 1 118 ? -5.197  -10.194 -57.693 1.00 97.54  ? 118  LYS B CE  1 
ATOM   3907 N NZ  . LYS B 1 118 ? -3.936  -9.600  -58.217 1.00 96.64  ? 118  LYS B NZ  1 
ATOM   3908 N N   . PHE B 1 119 ? -8.592  -12.465 -53.765 1.00 58.76  ? 119  PHE B N   1 
ATOM   3909 C CA  . PHE B 1 119 ? -8.221  -13.734 -53.153 1.00 58.71  ? 119  PHE B CA  1 
ATOM   3910 C C   . PHE B 1 119 ? -6.851  -14.189 -53.640 1.00 61.48  ? 119  PHE B C   1 
ATOM   3911 O O   . PHE B 1 119 ? -6.678  -14.547 -54.809 1.00 59.96  ? 119  PHE B O   1 
ATOM   3912 C CB  . PHE B 1 119 ? -9.274  -14.791 -53.457 1.00 60.90  ? 119  PHE B CB  1 
ATOM   3913 C CG  . PHE B 1 119 ? -9.062  -16.107 -52.754 1.00 63.29  ? 119  PHE B CG  1 
ATOM   3914 C CD1 . PHE B 1 119 ? -8.237  -17.087 -53.303 1.00 67.57  ? 119  PHE B CD1 1 
ATOM   3915 C CD2 . PHE B 1 119 ? -9.727  -16.393 -51.568 1.00 64.56  ? 119  PHE B CD2 1 
ATOM   3916 C CE1 . PHE B 1 119 ? -8.069  -18.320 -52.662 1.00 68.36  ? 119  PHE B CE1 1 
ATOM   3917 C CE2 . PHE B 1 119 ? -9.563  -17.626 -50.935 1.00 67.03  ? 119  PHE B CE2 1 
ATOM   3918 C CZ  . PHE B 1 119 ? -8.739  -18.583 -51.486 1.00 66.01  ? 119  PHE B CZ  1 
ATOM   3919 N N   . THR B 1 120 ? -5.890  -14.188 -52.710 1.00 58.95  ? 120  THR B N   1 
ATOM   3920 C CA  . THR B 1 120 ? -4.497  -14.560 -52.926 1.00 59.39  ? 120  THR B CA  1 
ATOM   3921 C C   . THR B 1 120 ? -4.165  -15.795 -52.072 1.00 62.71  ? 120  THR B C   1 
ATOM   3922 O O   . THR B 1 120 ? -4.273  -15.744 -50.847 1.00 62.14  ? 120  THR B O   1 
ATOM   3923 C CB  . THR B 1 120 ? -3.588  -13.373 -52.574 1.00 74.10  ? 120  THR B CB  1 
ATOM   3924 O OG1 . THR B 1 120 ? -4.268  -12.106 -52.774 1.00 75.94  ? 120  THR B OG1 1 
ATOM   3925 C CG2 . THR B 1 120 ? -2.265  -13.431 -53.316 1.00 73.94  ? 120  THR B CG2 1 
ATOM   3926 N N   . CYS B 1 121 ? -3.777  -16.903 -52.708 1.00 58.39  ? 121  CYS B N   1 
ATOM   3927 C CA  . CYS B 1 121 ? -3.440  -18.096 -51.950 1.00 57.15  ? 121  CYS B CA  1 
ATOM   3928 C C   . CYS B 1 121 ? -2.015  -18.032 -51.443 1.00 60.01  ? 121  CYS B C   1 
ATOM   3929 O O   . CYS B 1 121 ? -1.091  -17.711 -52.196 1.00 60.33  ? 121  CYS B O   1 
ATOM   3930 C CB  . CYS B 1 121 ? -3.690  -19.363 -52.758 1.00 57.30  ? 121  CYS B CB  1 
ATOM   3931 S SG  . CYS B 1 121 ? -3.708  -20.875 -51.757 1.00 61.16  ? 121  CYS B SG  1 
ATOM   3932 N N   . LYS B 1 122 ? -1.838  -18.350 -50.162 1.00 54.84  ? 122  LYS B N   1 
ATOM   3933 C CA  . LYS B 1 122 ? -0.551  -18.349 -49.470 1.00 53.67  ? 122  LYS B CA  1 
ATOM   3934 C C   . LYS B 1 122 ? 0.065   -19.763 -49.298 1.00 56.02  ? 122  LYS B C   1 
ATOM   3935 O O   . LYS B 1 122 ? 1.288   -19.881 -49.282 1.00 55.04  ? 122  LYS B O   1 
ATOM   3936 C CB  . LYS B 1 122 ? -0.713  -17.669 -48.108 1.00 56.33  ? 122  LYS B CB  1 
ATOM   3937 C CG  . LYS B 1 122 ? -0.805  -16.145 -48.196 1.00 72.86  ? 122  LYS B CG  1 
ATOM   3938 C CD  . LYS B 1 122 ? -1.328  -15.513 -46.894 1.00 81.20  ? 122  LYS B CD  1 
ATOM   3939 C CE  . LYS B 1 122 ? -0.325  -15.380 -45.765 1.00 81.09  ? 122  LYS B CE  1 
ATOM   3940 N NZ  . LYS B 1 122 ? -0.954  -14.807 -44.536 1.00 74.60  ? 122  LYS B NZ  1 
ATOM   3941 N N   . LYS B 1 123 ? -0.773  -20.832 -49.206 1.00 50.98  ? 123  LYS B N   1 
ATOM   3942 C CA  . LYS B 1 123 ? -0.290  -22.198 -48.981 1.00 49.25  ? 123  LYS B CA  1 
ATOM   3943 C C   . LYS B 1 123 ? -1.119  -23.241 -49.755 1.00 50.92  ? 123  LYS B C   1 
ATOM   3944 O O   . LYS B 1 123 ? -2.334  -23.113 -49.768 1.00 50.44  ? 123  LYS B O   1 
ATOM   3945 C CB  . LYS B 1 123 ? -0.341  -22.452 -47.457 1.00 51.47  ? 123  LYS B CB  1 
ATOM   3946 C CG  . LYS B 1 123 ? 0.728   -23.386 -46.943 1.00 70.34  ? 123  LYS B CG  1 
ATOM   3947 C CD  . LYS B 1 123 ? 1.342   -23.019 -45.597 1.00 76.81  ? 123  LYS B CD  1 
ATOM   3948 C CE  . LYS B 1 123 ? 2.417   -24.059 -45.317 1.00 86.50  ? 123  LYS B CE  1 
ATOM   3949 N NZ  . LYS B 1 123 ? 3.142   -23.850 -44.030 1.00 97.09  ? 123  LYS B NZ  1 
ATOM   3950 N N   . ASN B 1 124 ? -0.491  -24.264 -50.400 1.00 47.23  ? 124  ASN B N   1 
ATOM   3951 C CA  . ASN B 1 124 ? -1.266  -25.292 -51.152 1.00 46.65  ? 124  ASN B CA  1 
ATOM   3952 C C   . ASN B 1 124 ? -1.150  -26.738 -50.625 1.00 50.62  ? 124  ASN B C   1 
ATOM   3953 O O   . ASN B 1 124 ? -0.341  -27.052 -49.758 1.00 50.67  ? 124  ASN B O   1 
ATOM   3954 C CB  . ASN B 1 124 ? -0.889  -25.354 -52.643 1.00 43.71  ? 124  ASN B CB  1 
ATOM   3955 C CG  . ASN B 1 124 ? -0.798  -24.095 -53.463 1.00 83.39  ? 124  ASN B CG  1 
ATOM   3956 O OD1 . ASN B 1 124 ? -0.272  -24.151 -54.579 1.00 80.81  ? 124  ASN B OD1 1 
ATOM   3957 N ND2 . ASN B 1 124 ? -1.280  -22.940 -52.979 1.00 79.55  ? 124  ASN B ND2 1 
ATOM   3958 N N   . MET B 1 125 ? -1.933  -27.617 -51.241 1.00 46.48  ? 125  MET B N   1 
ATOM   3959 C CA  . MET B 1 125 ? -2.013  -29.061 -51.075 1.00 46.42  ? 125  MET B CA  1 
ATOM   3960 C C   . MET B 1 125 ? -2.120  -29.578 -52.490 1.00 54.62  ? 125  MET B C   1 
ATOM   3961 O O   . MET B 1 125 ? -2.837  -28.977 -53.315 1.00 54.50  ? 125  MET B O   1 
ATOM   3962 C CB  . MET B 1 125 ? -3.326  -29.496 -50.416 1.00 48.20  ? 125  MET B CB  1 
ATOM   3963 C CG  . MET B 1 125 ? -3.419  -29.215 -48.986 1.00 52.06  ? 125  MET B CG  1 
ATOM   3964 S SD  . MET B 1 125 ? -4.574  -30.394 -48.261 1.00 56.73  ? 125  MET B SD  1 
ATOM   3965 C CE  . MET B 1 125 ? -6.127  -29.677 -48.628 1.00 53.40  ? 125  MET B CE  1 
ATOM   3966 N N   . GLU B 1 126 ? -1.497  -30.736 -52.760 1.00 52.53  ? 126  GLU B N   1 
ATOM   3967 C CA  . GLU B 1 126 ? -1.615  -31.369 -54.066 1.00 52.77  ? 126  GLU B CA  1 
ATOM   3968 C C   . GLU B 1 126 ? -2.015  -32.785 -53.891 1.00 59.27  ? 126  GLU B C   1 
ATOM   3969 O O   . GLU B 1 126 ? -1.515  -33.472 -53.000 1.00 59.38  ? 126  GLU B O   1 
ATOM   3970 C CB  . GLU B 1 126 ? -0.327  -31.280 -54.867 1.00 54.14  ? 126  GLU B CB  1 
ATOM   3971 C CG  . GLU B 1 126 ? 0.038   -29.868 -55.286 1.00 63.51  ? 126  GLU B CG  1 
ATOM   3972 C CD  . GLU B 1 126 ? 0.658   -29.777 -56.664 1.00 92.22  ? 126  GLU B CD  1 
ATOM   3973 O OE1 . GLU B 1 126 ? 0.591   -30.773 -57.423 1.00 72.31  ? 126  GLU B OE1 1 
ATOM   3974 O OE2 . GLU B 1 126 ? 1.193   -28.693 -56.992 1.00 102.91 ? 126  GLU B OE2 1 
ATOM   3975 N N   . GLY B 1 127 ? -2.962  -33.202 -54.704 1.00 58.46  ? 127  GLY B N   1 
ATOM   3976 C CA  . GLY B 1 127 ? -3.446  -34.574 -54.695 1.00 59.64  ? 127  GLY B CA  1 
ATOM   3977 C C   . GLY B 1 127 ? -3.063  -35.227 -55.998 1.00 65.52  ? 127  GLY B C   1 
ATOM   3978 O O   . GLY B 1 127 ? -3.316  -34.640 -57.051 1.00 66.58  ? 127  GLY B O   1 
ATOM   3979 N N   . LYS B 1 128 ? -2.424  -36.405 -55.953 1.00 61.40  ? 128  LYS B N   1 
ATOM   3980 C CA  . LYS B 1 128 ? -2.008  -37.073 -57.183 1.00 61.09  ? 128  LYS B CA  1 
ATOM   3981 C C   . LYS B 1 128 ? -2.573  -38.456 -57.359 1.00 69.76  ? 128  LYS B C   1 
ATOM   3982 O O   . LYS B 1 128 ? -2.703  -39.197 -56.384 1.00 69.40  ? 128  LYS B O   1 
ATOM   3983 C CB  . LYS B 1 128 ? -0.493  -37.098 -57.304 1.00 61.19  ? 128  LYS B CB  1 
ATOM   3984 C CG  . LYS B 1 128 ? 0.036   -35.822 -57.910 1.00 58.81  ? 128  LYS B CG  1 
ATOM   3985 C CD  . LYS B 1 128 ? 1.099   -35.160 -57.057 1.00 60.26  ? 128  LYS B CD  1 
ATOM   3986 C CE  . LYS B 1 128 ? 2.130   -34.497 -57.944 1.00 53.35  ? 128  LYS B CE  1 
ATOM   3987 N NZ  . LYS B 1 128 ? 2.974   -33.528 -57.200 1.00 48.52  ? 128  LYS B NZ  1 
ATOM   3988 N N   . ILE B 1 129 ? -2.919  -38.810 -58.608 1.00 70.70  ? 129  ILE B N   1 
ATOM   3989 C CA  . ILE B 1 129 ? -3.382  -40.165 -58.894 1.00 72.84  ? 129  ILE B CA  1 
ATOM   3990 C C   . ILE B 1 129 ? -2.157  -41.031 -59.232 1.00 84.29  ? 129  ILE B C   1 
ATOM   3991 O O   . ILE B 1 129 ? -1.456  -40.776 -60.218 1.00 83.63  ? 129  ILE B O   1 
ATOM   3992 C CB  . ILE B 1 129 ? -4.549  -40.292 -59.898 1.00 75.15  ? 129  ILE B CB  1 
ATOM   3993 C CG1 . ILE B 1 129 ? -5.784  -39.531 -59.391 1.00 74.97  ? 129  ILE B CG1 1 
ATOM   3994 C CG2 . ILE B 1 129 ? -4.882  -41.779 -60.112 1.00 76.42  ? 129  ILE B CG2 1 
ATOM   3995 C CD1 . ILE B 1 129 ? -6.958  -39.421 -60.367 1.00 81.18  ? 129  ILE B CD1 1 
ATOM   3996 N N   . VAL B 1 130 ? -1.895  -42.022 -58.360 1.00 86.21  ? 130  VAL B N   1 
ATOM   3997 C CA  . VAL B 1 130 ? -0.762  -42.940 -58.416 1.00 88.22  ? 130  VAL B CA  1 
ATOM   3998 C C   . VAL B 1 130 ? -1.244  -44.380 -58.658 1.00 95.91  ? 130  VAL B C   1 
ATOM   3999 O O   . VAL B 1 130 ? -1.878  -44.992 -57.782 1.00 94.87  ? 130  VAL B O   1 
ATOM   4000 C CB  . VAL B 1 130 ? 0.066   -42.815 -57.112 1.00 92.71  ? 130  VAL B CB  1 
ATOM   4001 C CG1 . VAL B 1 130 ? 1.142   -43.894 -57.018 1.00 92.79  ? 130  VAL B CG1 1 
ATOM   4002 C CG2 . VAL B 1 130 ? 0.677   -41.426 -56.984 1.00 92.61  ? 130  VAL B CG2 1 
ATOM   4003 N N   . GLN B 1 131 ? -0.925  -44.921 -59.849 1.00 94.92  ? 131  GLN B N   1 
ATOM   4004 C CA  . GLN B 1 131 ? -1.312  -46.282 -60.177 1.00 95.57  ? 131  GLN B CA  1 
ATOM   4005 C C   . GLN B 1 131 ? -0.168  -47.267 -59.925 1.00 101.47 ? 131  GLN B C   1 
ATOM   4006 O O   . GLN B 1 131 ? 0.997   -46.896 -60.126 1.00 100.88 ? 131  GLN B O   1 
ATOM   4007 C CB  . GLN B 1 131 ? -1.913  -46.391 -61.583 1.00 97.03  ? 131  GLN B CB  1 
ATOM   4008 C CG  . GLN B 1 131 ? -3.405  -45.990 -61.648 1.00 113.64 ? 131  GLN B CG  1 
ATOM   4009 C CD  . GLN B 1 131 ? -4.246  -46.344 -60.422 1.00 124.38 ? 131  GLN B CD  1 
ATOM   4010 O OE1 . GLN B 1 131 ? -4.666  -45.458 -59.660 1.00 117.41 ? 131  GLN B OE1 1 
ATOM   4011 N NE2 . GLN B 1 131 ? -4.523  -47.634 -60.215 1.00 107.43 ? 131  GLN B NE2 1 
ATOM   4012 N N   . PRO B 1 132 ? -0.483  -48.495 -59.408 1.00 99.47  ? 132  PRO B N   1 
ATOM   4013 C CA  . PRO B 1 132 ? 0.575   -49.457 -59.059 1.00 99.37  ? 132  PRO B CA  1 
ATOM   4014 C C   . PRO B 1 132 ? 1.565   -49.801 -60.166 1.00 103.56 ? 132  PRO B C   1 
ATOM   4015 O O   . PRO B 1 132 ? 2.742   -49.989 -59.876 1.00 103.19 ? 132  PRO B O   1 
ATOM   4016 C CB  . PRO B 1 132 ? -0.209  -50.694 -58.605 1.00 101.17 ? 132  PRO B CB  1 
ATOM   4017 C CG  . PRO B 1 132 ? -1.495  -50.184 -58.155 1.00 105.59 ? 132  PRO B CG  1 
ATOM   4018 C CD  . PRO B 1 132 ? -1.812  -49.056 -59.085 1.00 101.32 ? 132  PRO B CD  1 
ATOM   4019 N N   . GLU B 1 133 ? 1.094   -49.890 -61.422 1.00 100.11 ? 133  GLU B N   1 
ATOM   4020 C CA  . GLU B 1 133 ? 1.918   -50.225 -62.587 1.00 99.81  ? 133  GLU B CA  1 
ATOM   4021 C C   . GLU B 1 133 ? 3.160   -49.350 -62.790 1.00 105.91 ? 133  GLU B C   1 
ATOM   4022 O O   . GLU B 1 133 ? 4.170   -49.853 -63.305 1.00 106.32 ? 133  GLU B O   1 
ATOM   4023 C CB  . GLU B 1 133 ? 1.080   -50.225 -63.870 1.00 100.77 ? 133  GLU B CB  1 
ATOM   4024 C CG  . GLU B 1 133 ? 0.119   -49.056 -63.999 1.00 106.54 ? 133  GLU B CG  1 
ATOM   4025 C CD  . GLU B 1 133 ? -1.313  -49.439 -63.688 1.00 119.21 ? 133  GLU B CD  1 
ATOM   4026 O OE1 . GLU B 1 133 ? -1.530  -50.230 -62.739 1.00 105.52 ? 133  GLU B OE1 1 
ATOM   4027 O OE2 . GLU B 1 133 ? -2.216  -48.975 -64.420 1.00 109.73 ? 133  GLU B OE2 1 
ATOM   4028 N N   . ASN B 1 134 ? 3.089   -48.051 -62.399 1.00 102.57 ? 134  ASN B N   1 
ATOM   4029 C CA  . ASN B 1 134 ? 4.177   -47.084 -62.617 1.00 102.18 ? 134  ASN B CA  1 
ATOM   4030 C C   . ASN B 1 134 ? 4.888   -46.661 -61.311 1.00 104.66 ? 134  ASN B C   1 
ATOM   4031 O O   . ASN B 1 134 ? 5.522   -45.599 -61.240 1.00 103.93 ? 134  ASN B O   1 
ATOM   4032 C CB  . ASN B 1 134 ? 3.668   -45.878 -63.435 1.00 103.85 ? 134  ASN B CB  1 
ATOM   4033 C CG  . ASN B 1 134 ? 2.502   -46.189 -64.365 1.00 118.90 ? 134  ASN B CG  1 
ATOM   4034 O OD1 . ASN B 1 134 ? 1.396   -45.660 -64.205 1.00 116.37 ? 134  ASN B OD1 1 
ATOM   4035 N ND2 . ASN B 1 134 ? 2.701   -47.089 -65.324 1.00 104.07 ? 134  ASN B ND2 1 
ATOM   4036 N N   . LEU B 1 135 ? 4.814   -47.543 -60.301 1.00 100.52 ? 135  LEU B N   1 
ATOM   4037 C CA  . LEU B 1 135 ? 5.465   -47.448 -58.989 1.00 99.73  ? 135  LEU B CA  1 
ATOM   4038 C C   . LEU B 1 135 ? 6.830   -48.137 -59.128 1.00 101.59 ? 135  LEU B C   1 
ATOM   4039 O O   . LEU B 1 135 ? 6.865   -49.339 -59.387 1.00 102.29 ? 135  LEU B O   1 
ATOM   4040 C CB  . LEU B 1 135 ? 4.610   -48.206 -57.960 1.00 99.88  ? 135  LEU B CB  1 
ATOM   4041 C CG  . LEU B 1 135 ? 4.592   -47.711 -56.523 1.00 105.02 ? 135  LEU B CG  1 
ATOM   4042 C CD1 . LEU B 1 135 ? 3.462   -48.352 -55.749 1.00 105.41 ? 135  LEU B CD1 1 
ATOM   4043 C CD2 . LEU B 1 135 ? 5.886   -48.005 -55.823 1.00 107.09 ? 135  LEU B CD2 1 
ATOM   4044 N N   . GLU B 1 136 ? 7.940   -47.397 -58.970 1.00 95.58  ? 136  GLU B N   1 
ATOM   4045 C CA  . GLU B 1 136 ? 9.292   -47.942 -59.123 1.00 94.92  ? 136  GLU B CA  1 
ATOM   4046 C C   . GLU B 1 136 ? 10.037  -48.152 -57.785 1.00 97.04  ? 136  GLU B C   1 
ATOM   4047 O O   . GLU B 1 136 ? 9.965   -47.309 -56.886 1.00 96.51  ? 136  GLU B O   1 
ATOM   4048 C CB  . GLU B 1 136 ? 10.107  -47.044 -60.071 1.00 96.60  ? 136  GLU B CB  1 
ATOM   4049 C CG  . GLU B 1 136 ? 11.471  -47.582 -60.476 1.00 109.34 ? 136  GLU B CG  1 
ATOM   4050 C CD  . GLU B 1 136 ? 12.329  -46.580 -61.226 1.00 130.71 ? 136  GLU B CD  1 
ATOM   4051 O OE1 . GLU B 1 136 ? 12.183  -46.483 -62.466 1.00 117.26 ? 136  GLU B OE1 1 
ATOM   4052 O OE2 . GLU B 1 136 ? 13.144  -45.885 -60.576 1.00 127.33 ? 136  GLU B OE2 1 
ATOM   4053 N N   . TYR B 1 137 ? 10.795  -49.264 -57.686 1.00 91.62  ? 137  TYR B N   1 
ATOM   4054 C CA  . TYR B 1 137 ? 11.609  -49.585 -56.507 1.00 89.63  ? 137  TYR B CA  1 
ATOM   4055 C C   . TYR B 1 137 ? 13.110  -49.529 -56.833 1.00 90.88  ? 137  TYR B C   1 
ATOM   4056 O O   . TYR B 1 137 ? 13.504  -49.875 -57.940 1.00 89.89  ? 137  TYR B O   1 
ATOM   4057 C CB  . TYR B 1 137 ? 11.222  -50.949 -55.922 1.00 89.31  ? 137  TYR B CB  1 
ATOM   4058 C CG  . TYR B 1 137 ? 9.740   -51.094 -55.658 1.00 88.79  ? 137  TYR B CG  1 
ATOM   4059 C CD1 . TYR B 1 137 ? 9.168   -50.606 -54.486 1.00 89.12  ? 137  TYR B CD1 1 
ATOM   4060 C CD2 . TYR B 1 137 ? 8.906   -51.720 -56.583 1.00 90.14  ? 137  TYR B CD2 1 
ATOM   4061 C CE1 . TYR B 1 137 ? 7.803   -50.747 -54.235 1.00 90.01  ? 137  TYR B CE1 1 
ATOM   4062 C CE2 . TYR B 1 137 ? 7.539   -51.858 -56.349 1.00 90.20  ? 137  TYR B CE2 1 
ATOM   4063 C CZ  . TYR B 1 137 ? 6.990   -51.375 -55.173 1.00 96.43  ? 137  TYR B CZ  1 
ATOM   4064 O OH  . TYR B 1 137 ? 5.640   -51.526 -54.959 1.00 94.36  ? 137  TYR B OH  1 
ATOM   4065 N N   . THR B 1 138 ? 13.929  -49.073 -55.876 1.00 86.75  ? 138  THR B N   1 
ATOM   4066 C CA  . THR B 1 138 ? 15.372  -48.953 -56.038 1.00 86.98  ? 138  THR B CA  1 
ATOM   4067 C C   . THR B 1 138 ? 16.091  -49.774 -54.966 1.00 90.60  ? 138  THR B C   1 
ATOM   4068 O O   . THR B 1 138 ? 16.118  -49.380 -53.794 1.00 90.41  ? 138  THR B O   1 
ATOM   4069 C CB  . THR B 1 138 ? 15.791  -47.477 -56.071 1.00 101.45 ? 138  THR B CB  1 
ATOM   4070 O OG1 . THR B 1 138 ? 15.129  -46.835 -57.159 1.00 105.98 ? 138  THR B OG1 1 
ATOM   4071 C CG2 . THR B 1 138 ? 17.305  -47.277 -56.186 1.00 99.94  ? 138  THR B CG2 1 
ATOM   4072 N N   . ILE B 1 139 ? 16.685  -50.913 -55.397 1.00 84.81  ? 139  ILE B N   1 
ATOM   4073 C CA  . ILE B 1 139 ? 17.432  -51.865 -54.576 1.00 82.54  ? 139  ILE B CA  1 
ATOM   4074 C C   . ILE B 1 139 ? 18.928  -51.704 -54.837 1.00 79.78  ? 139  ILE B C   1 
ATOM   4075 O O   . ILE B 1 139 ? 19.330  -51.532 -55.987 1.00 78.67  ? 139  ILE B O   1 
ATOM   4076 C CB  . ILE B 1 139 ? 16.934  -53.311 -54.880 1.00 86.09  ? 139  ILE B CB  1 
ATOM   4077 C CG1 . ILE B 1 139 ? 15.469  -53.498 -54.407 1.00 86.33  ? 139  ILE B CG1 1 
ATOM   4078 C CG2 . ILE B 1 139 ? 17.867  -54.393 -54.309 1.00 87.16  ? 139  ILE B CG2 1 
ATOM   4079 C CD1 . ILE B 1 139 ? 14.742  -54.686 -55.048 1.00 90.63  ? 139  ILE B CD1 1 
ATOM   4080 N N   . VAL B 1 140 ? 19.739  -51.760 -53.770 1.00 71.92  ? 140  VAL B N   1 
ATOM   4081 C CA  . VAL B 1 140 ? 21.198  -51.697 -53.847 1.00 69.91  ? 140  VAL B CA  1 
ATOM   4082 C C   . VAL B 1 140 ? 21.804  -53.031 -53.387 1.00 73.07  ? 140  VAL B C   1 
ATOM   4083 O O   . VAL B 1 140 ? 21.623  -53.427 -52.229 1.00 72.92  ? 140  VAL B O   1 
ATOM   4084 C CB  . VAL B 1 140 ? 21.788  -50.473 -53.103 1.00 72.67  ? 140  VAL B CB  1 
ATOM   4085 C CG1 . VAL B 1 140 ? 23.303  -50.561 -53.002 1.00 72.52  ? 140  VAL B CG1 1 
ATOM   4086 C CG2 . VAL B 1 140 ? 21.394  -49.196 -53.807 1.00 72.43  ? 140  VAL B CG2 1 
ATOM   4087 N N   . ILE B 1 141 ? 22.515  -53.725 -54.293 1.00 68.47  ? 141  ILE B N   1 
ATOM   4088 C CA  . ILE B 1 141 ? 23.149  -55.001 -53.950 1.00 67.53  ? 141  ILE B CA  1 
ATOM   4089 C C   . ILE B 1 141 ? 24.636  -54.786 -53.731 1.00 70.71  ? 141  ILE B C   1 
ATOM   4090 O O   . ILE B 1 141 ? 25.334  -54.393 -54.660 1.00 70.85  ? 141  ILE B O   1 
ATOM   4091 C CB  . ILE B 1 141 ? 22.870  -56.124 -54.971 1.00 69.95  ? 141  ILE B CB  1 
ATOM   4092 C CG1 . ILE B 1 141 ? 21.420  -56.136 -55.438 1.00 69.54  ? 141  ILE B CG1 1 
ATOM   4093 C CG2 . ILE B 1 141 ? 23.272  -57.464 -54.398 1.00 70.86  ? 141  ILE B CG2 1 
ATOM   4094 C CD1 . ILE B 1 141 ? 21.258  -55.806 -56.801 1.00 66.15  ? 141  ILE B CD1 1 
ATOM   4095 N N   . THR B 1 142 ? 25.110  -55.019 -52.512 1.00 65.96  ? 142  THR B N   1 
ATOM   4096 C CA  . THR B 1 142 ? 26.508  -54.836 -52.192 1.00 66.61  ? 142  THR B CA  1 
ATOM   4097 C C   . THR B 1 142 ? 27.169  -56.151 -51.810 1.00 74.94  ? 142  THR B C   1 
ATOM   4098 O O   . THR B 1 142 ? 26.893  -56.679 -50.732 1.00 75.66  ? 142  THR B O   1 
ATOM   4099 C CB  . THR B 1 142 ? 26.682  -53.764 -51.120 1.00 73.70  ? 142  THR B CB  1 
ATOM   4100 O OG1 . THR B 1 142 ? 25.962  -52.602 -51.511 1.00 75.77  ? 142  THR B OG1 1 
ATOM   4101 C CG2 . THR B 1 142 ? 28.154  -53.419 -50.861 1.00 69.64  ? 142  THR B CG2 1 
ATOM   4102 N N   . PRO B 1 143 ? 28.086  -56.691 -52.640 1.00 73.21  ? 143  PRO B N   1 
ATOM   4103 C CA  . PRO B 1 143 ? 28.776  -57.923 -52.237 1.00 73.51  ? 143  PRO B CA  1 
ATOM   4104 C C   . PRO B 1 143 ? 29.756  -57.693 -51.085 1.00 79.11  ? 143  PRO B C   1 
ATOM   4105 O O   . PRO B 1 143 ? 30.251  -56.560 -50.875 1.00 77.59  ? 143  PRO B O   1 
ATOM   4106 C CB  . PRO B 1 143 ? 29.488  -58.357 -53.519 1.00 74.81  ? 143  PRO B CB  1 
ATOM   4107 C CG  . PRO B 1 143 ? 29.691  -57.122 -54.274 1.00 78.24  ? 143  PRO B CG  1 
ATOM   4108 C CD  . PRO B 1 143 ? 28.548  -56.223 -53.964 1.00 73.88  ? 143  PRO B CD  1 
ATOM   4109 N N   . HIS B 1 144 ? 30.003  -58.787 -50.328 1.00 77.26  ? 144  HIS B N   1 
ATOM   4110 C CA  . HIS B 1 144 ? 30.945  -58.854 -49.210 1.00 77.77  ? 144  HIS B CA  1 
ATOM   4111 C C   . HIS B 1 144 ? 32.341  -59.178 -49.798 1.00 81.26  ? 144  HIS B C   1 
ATOM   4112 O O   . HIS B 1 144 ? 32.773  -60.328 -49.816 1.00 80.99  ? 144  HIS B O   1 
ATOM   4113 C CB  . HIS B 1 144 ? 30.496  -59.925 -48.201 1.00 79.01  ? 144  HIS B CB  1 
ATOM   4114 C CG  . HIS B 1 144 ? 29.673  -59.413 -47.063 1.00 82.24  ? 144  HIS B CG  1 
ATOM   4115 N ND1 . HIS B 1 144 ? 30.211  -59.261 -45.791 1.00 83.74  ? 144  HIS B ND1 1 
ATOM   4116 C CD2 . HIS B 1 144 ? 28.363  -59.083 -47.025 1.00 83.50  ? 144  HIS B CD2 1 
ATOM   4117 C CE1 . HIS B 1 144 ? 29.216  -58.840 -45.029 1.00 82.77  ? 144  HIS B CE1 1 
ATOM   4118 N NE2 . HIS B 1 144 ? 28.088  -58.708 -45.729 1.00 83.12  ? 144  HIS B NE2 1 
ATOM   4119 N N   . SER B 1 145 ? 32.961  -58.158 -50.399 1.00 77.11  ? 145  SER B N   1 
ATOM   4120 C CA  . SER B 1 145 ? 34.290  -58.113 -51.000 1.00 75.59  ? 145  SER B CA  1 
ATOM   4121 C C   . SER B 1 145 ? 34.881  -57.240 -49.938 1.00 76.37  ? 145  SER B C   1 
ATOM   4122 O O   . SER B 1 145 ? 34.295  -56.200 -49.680 1.00 79.06  ? 145  SER B O   1 
ATOM   4123 C CB  . SER B 1 145 ? 34.239  -57.345 -52.320 1.00 80.52  ? 145  SER B CB  1 
ATOM   4124 O OG  . SER B 1 145 ? 33.924  -55.967 -52.152 1.00 93.54  ? 145  SER B OG  1 
ATOM   4125 N N   . GLY B 1 146 ? 35.786  -57.748 -49.143 1.00 68.88  ? 146  GLY B N   1 
ATOM   4126 C CA  . GLY B 1 146 ? 36.388  -57.042 -48.011 1.00 66.92  ? 146  GLY B CA  1 
ATOM   4127 C C   . GLY B 1 146 ? 36.922  -55.648 -48.257 1.00 65.87  ? 146  GLY B C   1 
ATOM   4128 O O   . GLY B 1 146 ? 37.674  -55.138 -47.424 1.00 64.63  ? 146  GLY B O   1 
ATOM   4129 N N   . GLU B 1 147 ? 36.526  -55.012 -49.383 1.00 60.54  ? 147  GLU B N   1 
ATOM   4130 C CA  . GLU B 1 147 ? 36.914  -53.659 -49.762 1.00 60.42  ? 147  GLU B CA  1 
ATOM   4131 C C   . GLU B 1 147 ? 36.996  -52.735 -48.558 1.00 65.99  ? 147  GLU B C   1 
ATOM   4132 O O   . GLU B 1 147 ? 35.996  -52.504 -47.876 1.00 64.71  ? 147  GLU B O   1 
ATOM   4133 C CB  . GLU B 1 147 ? 36.022  -53.071 -50.870 1.00 61.46  ? 147  GLU B CB  1 
ATOM   4134 C CG  . GLU B 1 147 ? 36.729  -52.017 -51.730 1.00 70.16  ? 147  GLU B CG  1 
ATOM   4135 C CD  . GLU B 1 147 ? 37.343  -50.828 -51.007 1.00 94.76  ? 147  GLU B CD  1 
ATOM   4136 O OE1 . GLU B 1 147 ? 36.576  -49.950 -50.547 1.00 104.68 ? 147  GLU B OE1 1 
ATOM   4137 O OE2 . GLU B 1 147 ? 38.579  -50.832 -50.802 1.00 78.12  ? 147  GLU B OE2 1 
ATOM   4138 N N   . GLU B 1 148 ? 38.230  -52.270 -48.292 1.00 64.76  ? 148  GLU B N   1 
ATOM   4139 C CA  . GLU B 1 148 ? 38.655  -51.380 -47.222 1.00 65.54  ? 148  GLU B CA  1 
ATOM   4140 C C   . GLU B 1 148 ? 37.554  -50.413 -46.694 1.00 71.60  ? 148  GLU B C   1 
ATOM   4141 O O   . GLU B 1 148 ? 37.387  -50.320 -45.466 1.00 72.65  ? 148  GLU B O   1 
ATOM   4142 C CB  . GLU B 1 148 ? 39.906  -50.614 -47.675 1.00 66.93  ? 148  GLU B CB  1 
ATOM   4143 C CG  . GLU B 1 148 ? 40.437  -49.590 -46.679 1.00 74.61  ? 148  GLU B CG  1 
ATOM   4144 C CD  . GLU B 1 148 ? 41.517  -48.687 -47.234 1.00 93.96  ? 148  GLU B CD  1 
ATOM   4145 O OE1 . GLU B 1 148 ? 41.559  -48.474 -48.471 1.00 120.55 ? 148  GLU B OE1 1 
ATOM   4146 O OE2 . GLU B 1 148 ? 42.347  -48.218 -46.426 1.00 64.90  ? 148  GLU B OE2 1 
ATOM   4147 N N   . HIS B 1 149 ? 36.808  -49.712 -47.603 1.00 66.98  ? 149  HIS B N   1 
ATOM   4148 C CA  . HIS B 1 149 ? 35.790  -48.731 -47.201 1.00 66.14  ? 149  HIS B CA  1 
ATOM   4149 C C   . HIS B 1 149 ? 34.368  -49.233 -47.107 1.00 70.38  ? 149  HIS B C   1 
ATOM   4150 O O   . HIS B 1 149 ? 33.589  -48.624 -46.372 1.00 71.50  ? 149  HIS B O   1 
ATOM   4151 C CB  . HIS B 1 149 ? 35.833  -47.504 -48.100 1.00 66.58  ? 149  HIS B CB  1 
ATOM   4152 C CG  . HIS B 1 149 ? 37.060  -46.711 -47.851 1.00 70.24  ? 149  HIS B CG  1 
ATOM   4153 N ND1 . HIS B 1 149 ? 38.119  -46.741 -48.731 1.00 72.28  ? 149  HIS B ND1 1 
ATOM   4154 C CD2 . HIS B 1 149 ? 37.429  -46.019 -46.748 1.00 72.07  ? 149  HIS B CD2 1 
ATOM   4155 C CE1 . HIS B 1 149 ? 39.073  -46.005 -48.175 1.00 71.42  ? 149  HIS B CE1 1 
ATOM   4156 N NE2 . HIS B 1 149 ? 38.706  -45.550 -46.983 1.00 71.66  ? 149  HIS B NE2 1 
ATOM   4157 N N   . ALA B 1 150 ? 34.029  -50.327 -47.811 1.00 65.76  ? 150  ALA B N   1 
ATOM   4158 C CA  . ALA B 1 150 ? 32.686  -50.916 -47.936 1.00 65.49  ? 150  ALA B CA  1 
ATOM   4159 C C   . ALA B 1 150 ? 31.828  -50.998 -46.658 1.00 71.15  ? 150  ALA B C   1 
ATOM   4160 O O   . ALA B 1 150 ? 30.625  -50.768 -46.767 1.00 71.17  ? 150  ALA B O   1 
ATOM   4161 C CB  . ALA B 1 150 ? 32.772  -52.281 -48.578 1.00 66.13  ? 150  ALA B CB  1 
ATOM   4162 N N   . VAL B 1 151 ? 32.421  -51.303 -45.471 1.00 69.15  ? 151  VAL B N   1 
ATOM   4163 C CA  . VAL B 1 151 ? 31.735  -51.426 -44.162 1.00 68.75  ? 151  VAL B CA  1 
ATOM   4164 C C   . VAL B 1 151 ? 30.873  -50.189 -43.858 1.00 72.30  ? 151  VAL B C   1 
ATOM   4165 O O   . VAL B 1 151 ? 31.409  -49.082 -43.699 1.00 69.67  ? 151  VAL B O   1 
ATOM   4166 C CB  . VAL B 1 151 ? 32.721  -51.763 -42.996 1.00 72.23  ? 151  VAL B CB  1 
ATOM   4167 C CG1 . VAL B 1 151 ? 32.033  -51.752 -41.633 1.00 71.67  ? 151  VAL B CG1 1 
ATOM   4168 C CG2 . VAL B 1 151 ? 33.393  -53.098 -43.218 1.00 72.28  ? 151  VAL B CG2 1 
ATOM   4169 N N   . GLY B 1 152 ? 29.555  -50.410 -43.819 1.00 70.73  ? 152  GLY B N   1 
ATOM   4170 C CA  . GLY B 1 152 ? 28.539  -49.401 -43.555 1.00 71.92  ? 152  GLY B CA  1 
ATOM   4171 C C   . GLY B 1 152 ? 28.624  -48.155 -44.415 1.00 79.41  ? 152  GLY B C   1 
ATOM   4172 O O   . GLY B 1 152 ? 28.216  -47.079 -43.959 1.00 77.65  ? 152  GLY B O   1 
ATOM   4173 N N   . ASN B 1 153 ? 29.178  -48.277 -45.661 1.00 80.04  ? 153  ASN B N   1 
ATOM   4174 C CA  . ASN B 1 153 ? 29.336  -47.164 -46.604 1.00 81.00  ? 153  ASN B CA  1 
ATOM   4175 C C   . ASN B 1 153 ? 27.955  -46.851 -47.177 1.00 88.03  ? 153  ASN B C   1 
ATOM   4176 O O   . ASN B 1 153 ? 27.437  -47.583 -48.034 1.00 87.42  ? 153  ASN B O   1 
ATOM   4177 C CB  . ASN B 1 153 ? 30.369  -47.494 -47.698 1.00 81.47  ? 153  ASN B CB  1 
ATOM   4178 C CG  . ASN B 1 153 ? 31.001  -46.282 -48.367 1.00 103.40 ? 153  ASN B CG  1 
ATOM   4179 O OD1 . ASN B 1 153 ? 30.612  -45.910 -49.487 1.00 108.92 ? 153  ASN B OD1 1 
ATOM   4180 N ND2 . ASN B 1 153 ? 32.012  -45.686 -47.688 1.00 81.78  ? 153  ASN B ND2 1 
ATOM   4181 N N   . ASP B 1 154 ? 27.318  -45.815 -46.576 1.00 86.42  ? 154  ASP B N   1 
ATOM   4182 C CA  . ASP B 1 154 ? 25.980  -45.265 -46.866 1.00 86.37  ? 154  ASP B CA  1 
ATOM   4183 C C   . ASP B 1 154 ? 25.899  -44.661 -48.251 1.00 89.19  ? 154  ASP B C   1 
ATOM   4184 O O   . ASP B 1 154 ? 24.833  -44.699 -48.865 1.00 88.83  ? 154  ASP B O   1 
ATOM   4185 C CB  . ASP B 1 154 ? 25.587  -44.208 -45.805 1.00 88.63  ? 154  ASP B CB  1 
ATOM   4186 C CG  . ASP B 1 154 ? 26.699  -43.261 -45.320 1.00 107.42 ? 154  ASP B CG  1 
ATOM   4187 O OD1 . ASP B 1 154 ? 27.756  -43.145 -46.021 1.00 109.16 ? 154  ASP B OD1 1 
ATOM   4188 O OD2 . ASP B 1 154 ? 26.517  -42.634 -44.252 1.00 115.33 ? 154  ASP B OD2 1 
ATOM   4189 N N   . THR B 1 155 ? 27.036  -44.098 -48.719 1.00 85.63  ? 155  THR B N   1 
ATOM   4190 C CA  . THR B 1 155 ? 27.295  -43.430 -49.996 1.00 85.69  ? 155  THR B CA  1 
ATOM   4191 C C   . THR B 1 155 ? 26.665  -44.179 -51.203 1.00 93.54  ? 155  THR B C   1 
ATOM   4192 O O   . THR B 1 155 ? 25.865  -43.583 -51.932 1.00 95.20  ? 155  THR B O   1 
ATOM   4193 C CB  . THR B 1 155 ? 28.802  -43.173 -50.135 1.00 84.84  ? 155  THR B CB  1 
ATOM   4194 O OG1 . THR B 1 155 ? 29.228  -42.352 -49.050 1.00 76.03  ? 155  THR B OG1 1 
ATOM   4195 C CG2 . THR B 1 155 ? 29.151  -42.488 -51.417 1.00 86.08  ? 155  THR B CG2 1 
ATOM   4196 N N   . GLY B 1 156 ? 27.009  -45.444 -51.414 1.00 89.24  ? 156  GLY B N   1 
ATOM   4197 C CA  . GLY B 1 156 ? 26.398  -46.196 -52.512 1.00 87.77  ? 156  GLY B CA  1 
ATOM   4198 C C   . GLY B 1 156 ? 27.322  -46.571 -53.651 1.00 86.46  ? 156  GLY B C   1 
ATOM   4199 O O   . GLY B 1 156 ? 26.915  -47.301 -54.571 1.00 86.41  ? 156  GLY B O   1 
ATOM   4200 N N   . LYS B 1 157 ? 28.579  -46.093 -53.567 1.00 77.44  ? 157  LYS B N   1 
ATOM   4201 C CA  . LYS B 1 157 ? 29.634  -46.360 -54.537 1.00 75.18  ? 157  LYS B CA  1 
ATOM   4202 C C   . LYS B 1 157 ? 30.002  -47.878 -54.655 1.00 75.32  ? 157  LYS B C   1 
ATOM   4203 O O   . LYS B 1 157 ? 30.231  -48.377 -55.761 1.00 74.64  ? 157  LYS B O   1 
ATOM   4204 C CB  . LYS B 1 157 ? 30.853  -45.478 -54.228 1.00 76.67  ? 157  LYS B CB  1 
ATOM   4205 C CG  . LYS B 1 157 ? 30.586  -44.015 -54.560 1.00 90.18  ? 157  LYS B CG  1 
ATOM   4206 C CD  . LYS B 1 157 ? 31.626  -43.060 -53.972 1.00 96.41  ? 157  LYS B CD  1 
ATOM   4207 C CE  . LYS B 1 157 ? 31.347  -41.613 -54.336 1.00 89.63  ? 157  LYS B CE  1 
ATOM   4208 N NZ  . LYS B 1 157 ? 32.076  -40.661 -53.464 1.00 84.69  ? 157  LYS B NZ  1 
ATOM   4209 N N   . HIS B 1 158 ? 29.950  -48.619 -53.535 1.00 68.20  ? 158  HIS B N   1 
ATOM   4210 C CA  . HIS B 1 158 ? 30.338  -50.027 -53.515 1.00 65.70  ? 158  HIS B CA  1 
ATOM   4211 C C   . HIS B 1 158 ? 29.302  -51.010 -54.059 1.00 70.10  ? 158  HIS B C   1 
ATOM   4212 O O   . HIS B 1 158 ? 29.648  -52.178 -54.255 1.00 70.49  ? 158  HIS B O   1 
ATOM   4213 C CB  . HIS B 1 158 ? 30.783  -50.453 -52.109 1.00 64.55  ? 158  HIS B CB  1 
ATOM   4214 C CG  . HIS B 1 158 ? 31.951  -49.674 -51.580 1.00 66.47  ? 158  HIS B CG  1 
ATOM   4215 N ND1 . HIS B 1 158 ? 31.800  -48.375 -51.108 1.00 67.22  ? 158  HIS B ND1 1 
ATOM   4216 C CD2 . HIS B 1 158 ? 33.245  -50.049 -51.427 1.00 66.74  ? 158  HIS B CD2 1 
ATOM   4217 C CE1 . HIS B 1 158 ? 32.999  -48.010 -50.680 1.00 65.92  ? 158  HIS B CE1 1 
ATOM   4218 N NE2 . HIS B 1 158 ? 33.899  -48.987 -50.840 1.00 66.16  ? 158  HIS B NE2 1 
ATOM   4219 N N   . GLY B 1 159 ? 28.069  -50.572 -54.287 1.00 65.96  ? 159  GLY B N   1 
ATOM   4220 C CA  . GLY B 1 159 ? 27.032  -51.489 -54.741 1.00 65.66  ? 159  GLY B CA  1 
ATOM   4221 C C   . GLY B 1 159 ? 26.412  -51.140 -56.066 1.00 69.68  ? 159  GLY B C   1 
ATOM   4222 O O   . GLY B 1 159 ? 26.386  -49.967 -56.455 1.00 70.51  ? 159  GLY B O   1 
ATOM   4223 N N   . LYS B 1 160 ? 25.870  -52.170 -56.735 1.00 64.93  ? 160  LYS B N   1 
ATOM   4224 C CA  . LYS B 1 160 ? 25.166  -52.059 -58.012 1.00 64.27  ? 160  LYS B CA  1 
ATOM   4225 C C   . LYS B 1 160 ? 23.678  -51.746 -57.770 1.00 67.63  ? 160  LYS B C   1 
ATOM   4226 O O   . LYS B 1 160 ? 22.950  -52.563 -57.195 1.00 67.66  ? 160  LYS B O   1 
ATOM   4227 C CB  . LYS B 1 160 ? 25.334  -53.352 -58.850 1.00 65.86  ? 160  LYS B CB  1 
ATOM   4228 C CG  . LYS B 1 160 ? 24.654  -53.345 -60.218 1.00 71.65  ? 160  LYS B CG  1 
ATOM   4229 C CD  . LYS B 1 160 ? 25.559  -52.817 -61.330 1.00 87.81  ? 160  LYS B CD  1 
ATOM   4230 C CE  . LYS B 1 160 ? 24.795  -52.657 -62.624 1.00 104.98 ? 160  LYS B CE  1 
ATOM   4231 N NZ  . LYS B 1 160 ? 24.301  -51.264 -62.812 1.00 113.86 ? 160  LYS B NZ  1 
ATOM   4232 N N   . GLU B 1 161 ? 23.243  -50.560 -58.219 1.00 62.93  ? 161  GLU B N   1 
ATOM   4233 C CA  . GLU B 1 161 ? 21.858  -50.107 -58.149 1.00 62.20  ? 161  GLU B CA  1 
ATOM   4234 C C   . GLU B 1 161 ? 21.004  -50.914 -59.143 1.00 65.41  ? 161  GLU B C   1 
ATOM   4235 O O   . GLU B 1 161 ? 21.485  -51.263 -60.222 1.00 62.64  ? 161  GLU B O   1 
ATOM   4236 C CB  . GLU B 1 161 ? 21.779  -48.616 -58.489 1.00 63.49  ? 161  GLU B CB  1 
ATOM   4237 C CG  . GLU B 1 161 ? 21.796  -47.699 -57.277 1.00 75.39  ? 161  GLU B CG  1 
ATOM   4238 C CD  . GLU B 1 161 ? 21.151  -46.330 -57.443 1.00 96.42  ? 161  GLU B CD  1 
ATOM   4239 O OE1 . GLU B 1 161 ? 20.161  -46.212 -58.202 1.00 85.45  ? 161  GLU B OE1 1 
ATOM   4240 O OE2 . GLU B 1 161 ? 21.620  -45.377 -56.781 1.00 89.65  ? 161  GLU B OE2 1 
ATOM   4241 N N   . ILE B 1 162 ? 19.763  -51.246 -58.764 1.00 64.97  ? 162  ILE B N   1 
ATOM   4242 C CA  . ILE B 1 162 ? 18.851  -51.989 -59.642 1.00 66.54  ? 162  ILE B CA  1 
ATOM   4243 C C   . ILE B 1 162 ? 17.389  -51.530 -59.432 1.00 75.12  ? 162  ILE B C   1 
ATOM   4244 O O   . ILE B 1 162 ? 16.999  -51.213 -58.298 1.00 75.34  ? 162  ILE B O   1 
ATOM   4245 C CB  . ILE B 1 162 ? 19.042  -53.524 -59.566 1.00 69.39  ? 162  ILE B CB  1 
ATOM   4246 C CG1 . ILE B 1 162 ? 18.689  -54.222 -60.882 1.00 69.79  ? 162  ILE B CG1 1 
ATOM   4247 C CG2 . ILE B 1 162 ? 18.337  -54.150 -58.384 1.00 70.96  ? 162  ILE B CG2 1 
ATOM   4248 C CD1 . ILE B 1 162 ? 19.516  -53.823 -62.207 1.00 81.13  ? 162  ILE B CD1 1 
ATOM   4249 N N   . LYS B 1 163 ? 16.603  -51.467 -60.537 1.00 72.80  ? 163  LYS B N   1 
ATOM   4250 C CA  . LYS B 1 163 ? 15.226  -50.978 -60.555 1.00 73.01  ? 163  LYS B CA  1 
ATOM   4251 C C   . LYS B 1 163 ? 14.215  -52.072 -60.809 1.00 83.23  ? 163  LYS B C   1 
ATOM   4252 O O   . LYS B 1 163 ? 14.379  -52.891 -61.722 1.00 83.37  ? 163  LYS B O   1 
ATOM   4253 C CB  . LYS B 1 163 ? 15.053  -49.852 -61.590 1.00 73.50  ? 163  LYS B CB  1 
ATOM   4254 C CG  . LYS B 1 163 ? 16.189  -48.823 -61.650 1.00 73.54  ? 163  LYS B CG  1 
ATOM   4255 C CD  . LYS B 1 163 ? 16.014  -47.665 -60.672 1.00 77.66  ? 163  LYS B CD  1 
ATOM   4256 C CE  . LYS B 1 163 ? 17.187  -46.715 -60.667 1.00 91.03  ? 163  LYS B CE  1 
ATOM   4257 N NZ  . LYS B 1 163 ? 16.948  -45.540 -59.776 1.00 104.51 ? 163  LYS B NZ  1 
ATOM   4258 N N   . ILE B 1 164 ? 13.130  -52.064 -60.035 1.00 84.61  ? 164  ILE B N   1 
ATOM   4259 C CA  . ILE B 1 164 ? 12.062  -53.056 -60.179 1.00 86.45  ? 164  ILE B CA  1 
ATOM   4260 C C   . ILE B 1 164 ? 10.683  -52.358 -60.290 1.00 94.34  ? 164  ILE B C   1 
ATOM   4261 O O   . ILE B 1 164 ? 10.381  -51.411 -59.552 1.00 94.20  ? 164  ILE B O   1 
ATOM   4262 C CB  . ILE B 1 164 ? 12.168  -54.159 -59.068 1.00 89.45  ? 164  ILE B CB  1 
ATOM   4263 C CG1 . ILE B 1 164 ? 12.941  -55.397 -59.573 1.00 90.49  ? 164  ILE B CG1 1 
ATOM   4264 C CG2 . ILE B 1 164 ? 10.837  -54.552 -58.422 1.00 89.80  ? 164  ILE B CG2 1 
ATOM   4265 C CD1 . ILE B 1 164 ? 12.268  -56.277 -60.734 1.00 103.80 ? 164  ILE B CD1 1 
ATOM   4266 N N   . THR B 1 165 ? 9.883   -52.827 -61.251 1.00 93.00  ? 165  THR B N   1 
ATOM   4267 C CA  . THR B 1 165 ? 8.546   -52.331 -61.551 1.00 94.26  ? 165  THR B CA  1 
ATOM   4268 C C   . THR B 1 165 ? 7.571   -53.508 -61.620 1.00 101.44 ? 165  THR B C   1 
ATOM   4269 O O   . THR B 1 165 ? 7.913   -54.522 -62.236 1.00 100.69 ? 165  THR B O   1 
ATOM   4270 C CB  . THR B 1 165 ? 8.538   -51.506 -62.865 1.00 107.24 ? 165  THR B CB  1 
ATOM   4271 O OG1 . THR B 1 165 ? 7.239   -51.562 -63.475 1.00 111.01 ? 165  THR B OG1 1 
ATOM   4272 C CG2 . THR B 1 165 ? 9.590   -51.964 -63.881 1.00 104.31 ? 165  THR B CG2 1 
ATOM   4273 N N   . PRO B 1 166 ? 6.330   -53.382 -61.071 1.00 100.47 ? 166  PRO B N   1 
ATOM   4274 C CA  . PRO B 1 166 ? 5.368   -54.499 -61.157 1.00 100.99 ? 166  PRO B CA  1 
ATOM   4275 C C   . PRO B 1 166 ? 5.255   -55.119 -62.546 1.00 108.14 ? 166  PRO B C   1 
ATOM   4276 O O   . PRO B 1 166 ? 5.210   -56.344 -62.650 1.00 108.11 ? 166  PRO B O   1 
ATOM   4277 C CB  . PRO B 1 166 ? 4.058   -53.870 -60.686 1.00 102.20 ? 166  PRO B CB  1 
ATOM   4278 C CG  . PRO B 1 166 ? 4.480   -52.820 -59.745 1.00 106.21 ? 166  PRO B CG  1 
ATOM   4279 C CD  . PRO B 1 166 ? 5.755   -52.251 -60.313 1.00 101.80 ? 166  PRO B CD  1 
ATOM   4280 N N   . GLN B 1 167 ? 5.294   -54.287 -63.604 1.00 107.28 ? 167  GLN B N   1 
ATOM   4281 C CA  . GLN B 1 167 ? 5.231   -54.743 -64.996 1.00 108.63 ? 167  GLN B CA  1 
ATOM   4282 C C   . GLN B 1 167 ? 6.439   -55.637 -65.344 1.00 115.10 ? 167  GLN B C   1 
ATOM   4283 O O   . GLN B 1 167 ? 6.236   -56.747 -65.846 1.00 114.11 ? 167  GLN B O   1 
ATOM   4284 C CB  . GLN B 1 167 ? 5.071   -53.557 -65.973 1.00 110.10 ? 167  GLN B CB  1 
ATOM   4285 C CG  . GLN B 1 167 ? 3.754   -52.780 -65.796 1.00 122.76 ? 167  GLN B CG  1 
ATOM   4286 C CD  . GLN B 1 167 ? 3.639   -51.530 -66.646 1.00 141.11 ? 167  GLN B CD  1 
ATOM   4287 O OE1 . GLN B 1 167 ? 2.610   -51.286 -67.288 1.00 135.85 ? 167  GLN B OE1 1 
ATOM   4288 N NE2 . GLN B 1 167 ? 4.659   -50.678 -66.626 1.00 134.01 ? 167  GLN B NE2 1 
ATOM   4289 N N   . SER B 1 168 ? 7.678   -55.188 -65.011 1.00 114.34 ? 168  SER B N   1 
ATOM   4290 C CA  . SER B 1 168 ? 8.891   -55.985 -65.235 1.00 115.43 ? 168  SER B CA  1 
ATOM   4291 C C   . SER B 1 168 ? 9.166   -56.879 -64.004 1.00 123.14 ? 168  SER B C   1 
ATOM   4292 O O   . SER B 1 168 ? 9.708   -56.423 -62.987 1.00 123.05 ? 168  SER B O   1 
ATOM   4293 C CB  . SER B 1 168 ? 10.087  -55.121 -65.656 1.00 118.26 ? 168  SER B CB  1 
ATOM   4294 O OG  . SER B 1 168 ? 10.935  -54.676 -64.607 1.00 124.88 ? 168  SER B OG  1 
ATOM   4295 N N   . SER B 1 169 ? 8.705   -58.150 -64.094 1.00 121.62 ? 169  SER B N   1 
ATOM   4296 C CA  . SER B 1 169 ? 8.796   -59.184 -63.051 1.00 121.65 ? 169  SER B CA  1 
ATOM   4297 C C   . SER B 1 169 ? 10.254  -59.525 -62.643 1.00 124.46 ? 169  SER B C   1 
ATOM   4298 O O   . SER B 1 169 ? 10.591  -59.414 -61.455 1.00 124.18 ? 169  SER B O   1 
ATOM   4299 C CB  . SER B 1 169 ? 8.033   -60.444 -63.475 1.00 125.06 ? 169  SER B CB  1 
ATOM   4300 O OG  . SER B 1 169 ? 6.690   -60.176 -63.851 1.00 131.05 ? 169  SER B OG  1 
ATOM   4301 N N   . THR B 1 170 ? 11.114  -59.887 -63.638 1.00 118.94 ? 170  THR B N   1 
ATOM   4302 C CA  . THR B 1 170 ? 12.516  -60.279 -63.429 1.00 117.39 ? 170  THR B CA  1 
ATOM   4303 C C   . THR B 1 170 ? 13.577  -59.260 -63.893 1.00 118.54 ? 170  THR B C   1 
ATOM   4304 O O   . THR B 1 170 ? 13.417  -58.609 -64.931 1.00 118.04 ? 170  THR B O   1 
ATOM   4305 C CB  . THR B 1 170 ? 12.804  -61.664 -64.074 1.00 120.14 ? 170  THR B CB  1 
ATOM   4306 O OG1 . THR B 1 170 ? 14.190  -61.997 -63.907 1.00 119.92 ? 170  THR B OG1 1 
ATOM   4307 C CG2 . THR B 1 170 ? 12.413  -61.741 -65.556 1.00 114.78 ? 170  THR B CG2 1 
ATOM   4308 N N   . THR B 1 171 ? 14.685  -59.187 -63.117 1.00 112.65 ? 171  THR B N   1 
ATOM   4309 C CA  . THR B 1 171 ? 15.906  -58.438 -63.404 1.00 111.11 ? 171  THR B CA  1 
ATOM   4310 C C   . THR B 1 171 ? 17.078  -59.365 -63.104 1.00 111.64 ? 171  THR B C   1 
ATOM   4311 O O   . THR B 1 171 ? 17.263  -59.812 -61.971 1.00 111.07 ? 171  THR B O   1 
ATOM   4312 C CB  . THR B 1 171 ? 16.016  -57.060 -62.695 1.00 116.95 ? 171  THR B CB  1 
ATOM   4313 O OG1 . THR B 1 171 ? 14.742  -56.429 -62.612 1.00 118.92 ? 171  THR B OG1 1 
ATOM   4314 C CG2 . THR B 1 171 ? 16.982  -56.141 -63.397 1.00 112.49 ? 171  THR B CG2 1 
ATOM   4315 N N   . GLU B 1 172 ? 17.793  -59.734 -64.149 1.00 105.74 ? 172  GLU B N   1 
ATOM   4316 C CA  . GLU B 1 172 ? 18.990  -60.555 -64.076 1.00 104.08 ? 172  GLU B CA  1 
ATOM   4317 C C   . GLU B 1 172 ? 20.078  -59.469 -63.971 1.00 104.19 ? 172  GLU B C   1 
ATOM   4318 O O   . GLU B 1 172 ? 20.342  -58.798 -64.953 1.00 103.05 ? 172  GLU B O   1 
ATOM   4319 C CB  . GLU B 1 172 ? 19.121  -61.342 -65.393 1.00 105.42 ? 172  GLU B CB  1 
ATOM   4320 C CG  . GLU B 1 172 ? 19.490  -62.809 -65.283 1.00 117.31 ? 172  GLU B CG  1 
ATOM   4321 C CD  . GLU B 1 172 ? 19.922  -63.451 -66.595 1.00 142.91 ? 172  GLU B CD  1 
ATOM   4322 O OE1 . GLU B 1 172 ? 19.447  -63.017 -67.671 1.00 135.08 ? 172  GLU B OE1 1 
ATOM   4323 O OE2 . GLU B 1 172 ? 20.743  -64.395 -66.543 1.00 140.05 ? 172  GLU B OE2 1 
ATOM   4324 N N   . ALA B 1 173 ? 20.592  -59.185 -62.772 1.00 99.00  ? 173  ALA B N   1 
ATOM   4325 C CA  . ALA B 1 173 ? 21.575  -58.114 -62.638 1.00 97.64  ? 173  ALA B CA  1 
ATOM   4326 C C   . ALA B 1 173 ? 22.968  -58.641 -62.466 1.00 99.60  ? 173  ALA B C   1 
ATOM   4327 O O   . ALA B 1 173 ? 23.220  -59.507 -61.627 1.00 98.35  ? 173  ALA B O   1 
ATOM   4328 C CB  . ALA B 1 173 ? 21.208  -57.174 -61.505 1.00 98.26  ? 173  ALA B CB  1 
ATOM   4329 N N   . GLU B 1 174 ? 23.878  -58.087 -63.266 1.00 95.89  ? 174  GLU B N   1 
ATOM   4330 C CA  . GLU B 1 174 ? 25.296  -58.426 -63.313 1.00 95.23  ? 174  GLU B CA  1 
ATOM   4331 C C   . GLU B 1 174 ? 26.088  -57.696 -62.219 1.00 97.53  ? 174  GLU B C   1 
ATOM   4332 O O   . GLU B 1 174 ? 25.893  -56.497 -62.001 1.00 96.52  ? 174  GLU B O   1 
ATOM   4333 C CB  . GLU B 1 174 ? 25.843  -58.096 -64.717 1.00 96.49  ? 174  GLU B CB  1 
ATOM   4334 C CG  . GLU B 1 174 ? 27.206  -58.678 -65.045 1.00 107.69 ? 174  GLU B CG  1 
ATOM   4335 C CD  . GLU B 1 174 ? 27.246  -60.139 -65.447 1.00 133.36 ? 174  GLU B CD  1 
ATOM   4336 O OE1 . GLU B 1 174 ? 26.276  -60.607 -66.088 1.00 127.23 ? 174  GLU B OE1 1 
ATOM   4337 O OE2 . GLU B 1 174 ? 28.277  -60.799 -65.175 1.00 128.66 ? 174  GLU B OE2 1 
ATOM   4338 N N   . LEU B 1 175 ? 26.989  -58.443 -61.554 1.00 93.38  ? 175  LEU B N   1 
ATOM   4339 C CA  . LEU B 1 175 ? 27.915  -58.006 -60.509 1.00 92.82  ? 175  LEU B CA  1 
ATOM   4340 C C   . LEU B 1 175 ? 29.371  -58.245 -60.978 1.00 95.77  ? 175  LEU B C   1 
ATOM   4341 O O   . LEU B 1 175 ? 29.771  -59.383 -61.267 1.00 94.14  ? 175  LEU B O   1 
ATOM   4342 C CB  . LEU B 1 175 ? 27.620  -58.730 -59.173 1.00 92.48  ? 175  LEU B CB  1 
ATOM   4343 C CG  . LEU B 1 175 ? 26.258  -58.446 -58.534 1.00 95.89  ? 175  LEU B CG  1 
ATOM   4344 C CD1 . LEU B 1 175 ? 25.869  -59.536 -57.588 1.00 95.46  ? 175  LEU B CD1 1 
ATOM   4345 C CD2 . LEU B 1 175 ? 26.260  -57.121 -57.801 1.00 97.30  ? 175  LEU B CD2 1 
ATOM   4346 N N   . THR B 1 176 ? 30.127  -57.138 -61.101 1.00 92.03  ? 176  THR B N   1 
ATOM   4347 C CA  . THR B 1 176 ? 31.522  -57.081 -61.538 1.00 91.56  ? 176  THR B CA  1 
ATOM   4348 C C   . THR B 1 176 ? 32.456  -57.947 -60.645 1.00 93.33  ? 176  THR B C   1 
ATOM   4349 O O   . THR B 1 176 ? 32.945  -57.506 -59.593 1.00 91.73  ? 176  THR B O   1 
ATOM   4350 C CB  . THR B 1 176 ? 31.971  -55.606 -61.650 1.00 105.39 ? 176  THR B CB  1 
ATOM   4351 O OG1 . THR B 1 176 ? 30.903  -54.816 -62.187 1.00 108.03 ? 176  THR B OG1 1 
ATOM   4352 C CG2 . THR B 1 176 ? 33.233  -55.428 -62.492 1.00 105.06 ? 176  THR B CG2 1 
ATOM   4353 N N   . GLY B 1 177 ? 32.689  -59.176 -61.103 1.00 88.73  ? 177  GLY B N   1 
ATOM   4354 C CA  . GLY B 1 177 ? 33.577  -60.124 -60.440 1.00 87.50  ? 177  GLY B CA  1 
ATOM   4355 C C   . GLY B 1 177 ? 32.879  -61.317 -59.833 1.00 90.01  ? 177  GLY B C   1 
ATOM   4356 O O   . GLY B 1 177 ? 33.555  -62.254 -59.405 1.00 90.76  ? 177  GLY B O   1 
ATOM   4357 N N   . TYR B 1 178 ? 31.531  -61.309 -59.797 1.00 83.98  ? 178  TYR B N   1 
ATOM   4358 C CA  . TYR B 1 178 ? 30.760  -62.381 -59.161 1.00 82.49  ? 178  TYR B CA  1 
ATOM   4359 C C   . TYR B 1 178 ? 29.739  -63.054 -60.084 1.00 84.23  ? 178  TYR B C   1 
ATOM   4360 O O   . TYR B 1 178 ? 29.144  -64.060 -59.718 1.00 82.37  ? 178  TYR B O   1 
ATOM   4361 C CB  . TYR B 1 178 ? 30.087  -61.844 -57.872 1.00 82.89  ? 178  TYR B CB  1 
ATOM   4362 C CG  . TYR B 1 178 ? 31.075  -61.254 -56.877 1.00 83.13  ? 178  TYR B CG  1 
ATOM   4363 C CD1 . TYR B 1 178 ? 31.722  -62.060 -55.948 1.00 84.99  ? 178  TYR B CD1 1 
ATOM   4364 C CD2 . TYR B 1 178 ? 31.404  -59.900 -56.904 1.00 83.11  ? 178  TYR B CD2 1 
ATOM   4365 C CE1 . TYR B 1 178 ? 32.646  -61.532 -55.044 1.00 85.36  ? 178  TYR B CE1 1 
ATOM   4366 C CE2 . TYR B 1 178 ? 32.337  -59.359 -56.010 1.00 83.64  ? 178  TYR B CE2 1 
ATOM   4367 C CZ  . TYR B 1 178 ? 32.952  -60.178 -55.077 1.00 90.76  ? 178  TYR B CZ  1 
ATOM   4368 O OH  . TYR B 1 178 ? 33.871  -59.651 -54.192 1.00 92.07  ? 178  TYR B OH  1 
ATOM   4369 N N   . GLY B 1 179 ? 29.535  -62.484 -61.259 1.00 81.31  ? 179  GLY B N   1 
ATOM   4370 C CA  . GLY B 1 179 ? 28.559  -62.982 -62.222 1.00 81.29  ? 179  GLY B CA  1 
ATOM   4371 C C   . GLY B 1 179 ? 27.215  -62.279 -62.125 1.00 84.99  ? 179  GLY B C   1 
ATOM   4372 O O   . GLY B 1 179 ? 27.140  -61.130 -61.681 1.00 82.95  ? 179  GLY B O   1 
ATOM   4373 N N   . THR B 1 180 ? 26.140  -62.971 -62.527 1.00 83.16  ? 180  THR B N   1 
ATOM   4374 C CA  . THR B 1 180 ? 24.794  -62.405 -62.520 1.00 84.46  ? 180  THR B CA  1 
ATOM   4375 C C   . THR B 1 180 ? 23.926  -63.011 -61.408 1.00 93.96  ? 180  THR B C   1 
ATOM   4376 O O   . THR B 1 180 ? 24.129  -64.154 -60.996 1.00 94.37  ? 180  THR B O   1 
ATOM   4377 C CB  . THR B 1 180 ? 24.171  -62.504 -63.945 1.00 89.64  ? 180  THR B CB  1 
ATOM   4378 O OG1 . THR B 1 180 ? 23.813  -61.214 -64.443 1.00 87.84  ? 180  THR B OG1 1 
ATOM   4379 C CG2 . THR B 1 180 ? 23.002  -63.477 -64.058 1.00 86.05  ? 180  THR B CG2 1 
ATOM   4380 N N   . VAL B 1 181 ? 22.958  -62.225 -60.927 1.00 94.09  ? 181  VAL B N   1 
ATOM   4381 C CA  . VAL B 1 181 ? 21.988  -62.634 -59.914 1.00 94.60  ? 181  VAL B CA  1 
ATOM   4382 C C   . VAL B 1 181 ? 20.587  -62.385 -60.445 1.00 99.30  ? 181  VAL B C   1 
ATOM   4383 O O   . VAL B 1 181 ? 20.278  -61.261 -60.838 1.00 98.74  ? 181  VAL B O   1 
ATOM   4384 C CB  . VAL B 1 181 ? 22.254  -62.007 -58.510 1.00 98.25  ? 181  VAL B CB  1 
ATOM   4385 C CG1 . VAL B 1 181 ? 22.230  -60.473 -58.532 1.00 97.82  ? 181  VAL B CG1 1 
ATOM   4386 C CG2 . VAL B 1 181 ? 21.302  -62.566 -57.457 1.00 98.04  ? 181  VAL B CG2 1 
ATOM   4387 N N   . THR B 1 182 ? 19.769  -63.442 -60.498 1.00 96.57  ? 182  THR B N   1 
ATOM   4388 C CA  . THR B 1 182 ? 18.403  -63.342 -61.000 1.00 97.00  ? 182  THR B CA  1 
ATOM   4389 C C   . THR B 1 182 ? 17.495  -62.959 -59.832 1.00 101.13 ? 182  THR B C   1 
ATOM   4390 O O   . THR B 1 182 ? 17.457  -63.680 -58.840 1.00 100.33 ? 182  THR B O   1 
ATOM   4391 C CB  . THR B 1 182 ? 17.973  -64.645 -61.727 1.00 107.15 ? 182  THR B CB  1 
ATOM   4392 O OG1 . THR B 1 182 ? 19.077  -65.222 -62.448 1.00 104.38 ? 182  THR B OG1 1 
ATOM   4393 C CG2 . THR B 1 182 ? 16.780  -64.425 -62.661 1.00 105.63 ? 182  THR B CG2 1 
ATOM   4394 N N   . MET B 1 183 ? 16.803  -61.806 -59.930 1.00 98.79  ? 183  MET B N   1 
ATOM   4395 C CA  . MET B 1 183 ? 15.917  -61.307 -58.878 1.00 98.81  ? 183  MET B CA  1 
ATOM   4396 C C   . MET B 1 183 ? 14.491  -61.233 -59.400 1.00 101.81 ? 183  MET B C   1 
ATOM   4397 O O   . MET B 1 183 ? 14.255  -60.632 -60.446 1.00 101.37 ? 183  MET B O   1 
ATOM   4398 C CB  . MET B 1 183 ? 16.393  -59.927 -58.433 1.00 101.59 ? 183  MET B CB  1 
ATOM   4399 C CG  . MET B 1 183 ? 16.132  -59.611 -56.999 1.00 106.18 ? 183  MET B CG  1 
ATOM   4400 S SD  . MET B 1 183 ? 16.944  -58.013 -56.551 1.00 111.32 ? 183  MET B SD  1 
ATOM   4401 C CE  . MET B 1 183 ? 18.674  -58.446 -56.708 1.00 107.82 ? 183  MET B CE  1 
ATOM   4402 N N   . GLU B 1 184 ? 13.544  -61.854 -58.693 1.00 98.23  ? 184  GLU B N   1 
ATOM   4403 C CA  . GLU B 1 184 ? 12.131  -61.862 -59.085 1.00 98.00  ? 184  GLU B CA  1 
ATOM   4404 C C   . GLU B 1 184 ? 11.290  -61.266 -57.970 1.00 103.05 ? 184  GLU B C   1 
ATOM   4405 O O   . GLU B 1 184 ? 10.962  -61.961 -57.004 1.00 102.93 ? 184  GLU B O   1 
ATOM   4406 C CB  . GLU B 1 184 ? 11.682  -63.276 -59.502 1.00 99.21  ? 184  GLU B CB  1 
ATOM   4407 C CG  . GLU B 1 184 ? 11.839  -63.519 -60.995 1.00 110.42 ? 184  GLU B CG  1 
ATOM   4408 C CD  . GLU B 1 184 ? 12.342  -64.883 -61.437 1.00 132.32 ? 184  GLU B CD  1 
ATOM   4409 O OE1 . GLU B 1 184 ? 11.567  -65.862 -61.354 1.00 122.79 ? 184  GLU B OE1 1 
ATOM   4410 O OE2 . GLU B 1 184 ? 13.493  -64.964 -61.924 1.00 134.13 ? 184  GLU B OE2 1 
ATOM   4411 N N   . CYS B 1 185 ? 10.962  -59.961 -58.095 1.00 100.88 ? 185  CYS B N   1 
ATOM   4412 C CA  . CYS B 1 185 ? 10.249  -59.221 -57.055 1.00 101.59 ? 185  CYS B CA  1 
ATOM   4413 C C   . CYS B 1 185 ? 8.770   -59.014 -57.303 1.00 108.35 ? 185  CYS B C   1 
ATOM   4414 O O   . CYS B 1 185 ? 8.340   -58.761 -58.432 1.00 108.59 ? 185  CYS B O   1 
ATOM   4415 C CB  . CYS B 1 185 ? 10.946  -57.900 -56.774 1.00 101.75 ? 185  CYS B CB  1 
ATOM   4416 S SG  . CYS B 1 185 ? 12.640  -58.103 -56.176 1.00 105.72 ? 185  CYS B SG  1 
ATOM   4417 N N   . SER B 1 186 ? 8.007   -59.106 -56.194 1.00 106.39 ? 186  SER B N   1 
ATOM   4418 C CA  . SER B 1 186 ? 6.558   -58.946 -56.120 1.00 107.03 ? 186  SER B CA  1 
ATOM   4419 C C   . SER B 1 186 ? 6.169   -57.803 -55.172 1.00 113.01 ? 186  SER B C   1 
ATOM   4420 O O   . SER B 1 186 ? 6.574   -57.802 -54.003 1.00 112.56 ? 186  SER B O   1 
ATOM   4421 C CB  . SER B 1 186 ? 5.898   -60.240 -55.658 1.00 110.64 ? 186  SER B CB  1 
ATOM   4422 O OG  . SER B 1 186 ? 6.205   -61.308 -56.538 1.00 120.59 ? 186  SER B OG  1 
ATOM   4423 N N   . PRO B 1 187 ? 5.372   -56.826 -55.664 1.00 110.90 ? 187  PRO B N   1 
ATOM   4424 C CA  . PRO B 1 187 ? 4.947   -55.709 -54.793 1.00 110.87 ? 187  PRO B CA  1 
ATOM   4425 C C   . PRO B 1 187 ? 3.956   -56.111 -53.690 1.00 114.60 ? 187  PRO B C   1 
ATOM   4426 O O   . PRO B 1 187 ? 3.051   -56.905 -53.950 1.00 114.54 ? 187  PRO B O   1 
ATOM   4427 C CB  . PRO B 1 187 ? 4.290   -54.738 -55.779 1.00 112.81 ? 187  PRO B CB  1 
ATOM   4428 C CG  . PRO B 1 187 ? 3.821   -55.593 -56.923 1.00 117.30 ? 187  PRO B CG  1 
ATOM   4429 C CD  . PRO B 1 187 ? 4.833   -56.690 -57.037 1.00 112.67 ? 187  PRO B CD  1 
ATOM   4430 N N   . ARG B 1 188 ? 4.112   -55.573 -52.467 1.00 111.03 ? 188  ARG B N   1 
ATOM   4431 C CA  . ARG B 1 188 ? 3.173   -55.851 -51.376 1.00 111.45 ? 188  ARG B CA  1 
ATOM   4432 C C   . ARG B 1 188 ? 2.786   -54.551 -50.641 1.00 117.12 ? 188  ARG B C   1 
ATOM   4433 O O   . ARG B 1 188 ? 3.472   -54.090 -49.717 1.00 116.83 ? 188  ARG B O   1 
ATOM   4434 C CB  . ARG B 1 188 ? 3.657   -56.973 -50.434 1.00 112.71 ? 188  ARG B CB  1 
ATOM   4435 C CG  . ARG B 1 188 ? 2.678   -57.318 -49.290 1.00 128.23 ? 188  ARG B CG  1 
ATOM   4436 C CD  . ARG B 1 188 ? 1.762   -58.509 -49.556 1.00 144.04 ? 188  ARG B CD  1 
ATOM   4437 N NE  . ARG B 1 188 ? 1.626   -59.372 -48.370 1.00 154.72 ? 188  ARG B NE  1 
ATOM   4438 C CZ  . ARG B 1 188 ? 0.512   -59.534 -47.655 1.00 164.57 ? 188  ARG B CZ  1 
ATOM   4439 N NH1 . ARG B 1 188 ? -0.606  -58.904 -47.999 1.00 148.28 ? 188  ARG B NH1 1 
ATOM   4440 N NH2 . ARG B 1 188 ? 0.505   -60.334 -46.597 1.00 148.20 ? 188  ARG B NH2 1 
ATOM   4441 N N   . THR B 1 189 ? 1.678   -53.955 -51.114 1.00 114.39 ? 189  THR B N   1 
ATOM   4442 C CA  . THR B 1 189 ? 1.060   -52.718 -50.624 1.00 113.89 ? 189  THR B CA  1 
ATOM   4443 C C   . THR B 1 189 ? -0.064  -53.046 -49.614 1.00 118.14 ? 189  THR B C   1 
ATOM   4444 O O   . THR B 1 189 ? -0.420  -54.215 -49.450 1.00 118.07 ? 189  THR B O   1 
ATOM   4445 C CB  . THR B 1 189 ? 0.620   -51.841 -51.827 1.00 118.15 ? 189  THR B CB  1 
ATOM   4446 O OG1 . THR B 1 189 ? -0.245  -50.795 -51.380 1.00 117.88 ? 189  THR B OG1 1 
ATOM   4447 C CG2 . THR B 1 189 ? -0.067  -52.642 -52.941 1.00 115.09 ? 189  THR B CG2 1 
ATOM   4448 N N   . GLY B 1 190 ? -0.591  -52.020 -48.949 1.00 114.46 ? 190  GLY B N   1 
ATOM   4449 C CA  . GLY B 1 190 ? -1.653  -52.150 -47.956 1.00 113.97 ? 190  GLY B CA  1 
ATOM   4450 C C   . GLY B 1 190 ? -3.079  -52.134 -48.479 1.00 116.60 ? 190  GLY B C   1 
ATOM   4451 O O   . GLY B 1 190 ? -3.872  -52.993 -48.079 1.00 117.03 ? 190  GLY B O   1 
ATOM   4452 N N   . LEU B 1 191 ? -3.434  -51.140 -49.340 1.00 110.76 ? 191  LEU B N   1 
ATOM   4453 C CA  . LEU B 1 191 ? -4.781  -50.982 -49.928 1.00 109.86 ? 191  LEU B CA  1 
ATOM   4454 C C   . LEU B 1 191 ? -4.680  -50.953 -51.463 1.00 111.55 ? 191  LEU B C   1 
ATOM   4455 O O   . LEU B 1 191 ? -3.564  -50.838 -51.981 1.00 110.67 ? 191  LEU B O   1 
ATOM   4456 C CB  . LEU B 1 191 ? -5.418  -49.644 -49.433 1.00 110.01 ? 191  LEU B CB  1 
ATOM   4457 C CG  . LEU B 1 191 ? -6.938  -49.586 -49.057 1.00 114.06 ? 191  LEU B CG  1 
ATOM   4458 C CD1 . LEU B 1 191 ? -7.254  -48.377 -48.210 1.00 113.82 ? 191  LEU B CD1 1 
ATOM   4459 C CD2 . LEU B 1 191 ? -7.866  -49.567 -50.269 1.00 115.25 ? 191  LEU B CD2 1 
ATOM   4460 N N   . ASP B 1 192 ? -5.844  -51.043 -52.190 1.00 106.94 ? 192  ASP B N   1 
ATOM   4461 C CA  . ASP B 1 192 ? -5.902  -50.916 -53.656 1.00 106.04 ? 192  ASP B CA  1 
ATOM   4462 C C   . ASP B 1 192 ? -5.661  -49.452 -53.971 1.00 104.68 ? 192  ASP B C   1 
ATOM   4463 O O   . ASP B 1 192 ? -6.417  -48.578 -53.536 1.00 104.71 ? 192  ASP B O   1 
ATOM   4464 C CB  . ASP B 1 192 ? -7.238  -51.400 -54.278 1.00 108.84 ? 192  ASP B CB  1 
ATOM   4465 C CG  . ASP B 1 192 ? -7.402  -51.097 -55.784 1.00 125.54 ? 192  ASP B CG  1 
ATOM   4466 O OD1 . ASP B 1 192 ? -6.468  -51.419 -56.571 1.00 126.01 ? 192  ASP B OD1 1 
ATOM   4467 O OD2 . ASP B 1 192 ? -8.470  -50.550 -56.175 1.00 133.32 ? 192  ASP B OD2 1 
ATOM   4468 N N   . PHE B 1 193 ? -4.586  -49.202 -54.705 1.00 96.36  ? 193  PHE B N   1 
ATOM   4469 C CA  . PHE B 1 193 ? -4.107  -47.887 -55.064 1.00 93.99  ? 193  PHE B CA  1 
ATOM   4470 C C   . PHE B 1 193 ? -4.945  -47.079 -56.008 1.00 96.90  ? 193  PHE B C   1 
ATOM   4471 O O   . PHE B 1 193 ? -4.641  -45.898 -56.158 1.00 95.94  ? 193  PHE B O   1 
ATOM   4472 C CB  . PHE B 1 193 ? -2.732  -48.030 -55.660 1.00 95.07  ? 193  PHE B CB  1 
ATOM   4473 C CG  . PHE B 1 193 ? -1.634  -47.665 -54.719 1.00 95.90  ? 193  PHE B CG  1 
ATOM   4474 C CD1 . PHE B 1 193 ? -1.366  -48.446 -53.604 1.00 98.48  ? 193  PHE B CD1 1 
ATOM   4475 C CD2 . PHE B 1 193 ? -0.833  -46.562 -54.966 1.00 97.84  ? 193  PHE B CD2 1 
ATOM   4476 C CE1 . PHE B 1 193 ? -0.338  -48.109 -52.735 1.00 99.31  ? 193  PHE B CE1 1 
ATOM   4477 C CE2 . PHE B 1 193 ? 0.208   -46.236 -54.107 1.00 100.53 ? 193  PHE B CE2 1 
ATOM   4478 C CZ  . PHE B 1 193 ? 0.454   -47.015 -53.001 1.00 98.64  ? 193  PHE B CZ  1 
ATOM   4479 N N   . ASN B 1 194 ? -5.951  -47.671 -56.691 1.00 94.33  ? 194  ASN B N   1 
ATOM   4480 C CA  . ASN B 1 194 ? -6.717  -46.868 -57.653 1.00 94.44  ? 194  ASN B CA  1 
ATOM   4481 C C   . ASN B 1 194 ? -7.553  -45.777 -57.017 1.00 96.15  ? 194  ASN B C   1 
ATOM   4482 O O   . ASN B 1 194 ? -7.434  -44.610 -57.450 1.00 97.45  ? 194  ASN B O   1 
ATOM   4483 C CB  . ASN B 1 194 ? -7.581  -47.667 -58.633 1.00 97.80  ? 194  ASN B CB  1 
ATOM   4484 C CG  . ASN B 1 194 ? -8.267  -46.732 -59.627 1.00 121.64 ? 194  ASN B CG  1 
ATOM   4485 O OD1 . ASN B 1 194 ? -7.636  -45.838 -60.225 1.00 115.53 ? 194  ASN B OD1 1 
ATOM   4486 N ND2 . ASN B 1 194 ? -9.589  -46.813 -59.713 1.00 111.49 ? 194  ASN B ND2 1 
ATOM   4487 N N   . GLU B 1 195 ? -8.406  -46.142 -56.017 1.00 86.77  ? 195  GLU B N   1 
ATOM   4488 C CA  . GLU B 1 195 ? -9.262  -45.152 -55.380 1.00 83.42  ? 195  GLU B CA  1 
ATOM   4489 C C   . GLU B 1 195 ? -8.485  -44.170 -54.489 1.00 79.95  ? 195  GLU B C   1 
ATOM   4490 O O   . GLU B 1 195 ? -9.002  -43.119 -54.128 1.00 77.62  ? 195  GLU B O   1 
ATOM   4491 C CB  . GLU B 1 195 ? -10.410 -45.818 -54.643 1.00 84.75  ? 195  GLU B CB  1 
ATOM   4492 C CG  . GLU B 1 195 ? -11.658 -44.979 -54.722 1.00 94.64  ? 195  GLU B CG  1 
ATOM   4493 C CD  . GLU B 1 195 ? -12.473 -45.259 -55.957 1.00 125.28 ? 195  GLU B CD  1 
ATOM   4494 O OE1 . GLU B 1 195 ? -13.323 -46.177 -55.898 1.00 122.40 ? 195  GLU B OE1 1 
ATOM   4495 O OE2 . GLU B 1 195 ? -12.247 -44.584 -56.989 1.00 124.72 ? 195  GLU B OE2 1 
ATOM   4496 N N   . MET B 1 196 ? -7.221  -44.481 -54.208 1.00 73.76  ? 196  MET B N   1 
ATOM   4497 C CA  . MET B 1 196 ? -6.385  -43.633 -53.381 1.00 72.84  ? 196  MET B CA  1 
ATOM   4498 C C   . MET B 1 196 ? -5.703  -42.496 -54.159 1.00 73.64  ? 196  MET B C   1 
ATOM   4499 O O   . MET B 1 196 ? -5.403  -42.606 -55.361 1.00 73.18  ? 196  MET B O   1 
ATOM   4500 C CB  . MET B 1 196 ? -5.372  -44.452 -52.554 1.00 75.35  ? 196  MET B CB  1 
ATOM   4501 C CG  . MET B 1 196 ? -6.012  -45.368 -51.481 1.00 79.46  ? 196  MET B CG  1 
ATOM   4502 S SD  . MET B 1 196 ? -7.611  -44.832 -50.760 1.00 84.26  ? 196  MET B SD  1 
ATOM   4503 C CE  . MET B 1 196 ? -8.715  -46.093 -51.379 1.00 81.13  ? 196  MET B CE  1 
ATOM   4504 N N   . VAL B 1 197 ? -5.502  -41.380 -53.432 1.00 66.99  ? 197  VAL B N   1 
ATOM   4505 C CA  . VAL B 1 197 ? -4.898  -40.134 -53.876 1.00 65.45  ? 197  VAL B CA  1 
ATOM   4506 C C   . VAL B 1 197 ? -3.708  -39.841 -52.953 1.00 67.19  ? 197  VAL B C   1 
ATOM   4507 O O   . VAL B 1 197 ? -3.850  -39.903 -51.729 1.00 66.21  ? 197  VAL B O   1 
ATOM   4508 C CB  . VAL B 1 197 ? -5.924  -38.957 -53.867 1.00 68.67  ? 197  VAL B CB  1 
ATOM   4509 C CG1 . VAL B 1 197 ? -5.322  -37.689 -54.462 1.00 68.57  ? 197  VAL B CG1 1 
ATOM   4510 C CG2 . VAL B 1 197 ? -7.198  -39.311 -54.611 1.00 68.26  ? 197  VAL B CG2 1 
ATOM   4511 N N   . LEU B 1 198 ? -2.554  -39.502 -53.545 1.00 62.28  ? 198  LEU B N   1 
ATOM   4512 C CA  . LEU B 1 198 ? -1.359  -39.143 -52.799 1.00 61.73  ? 198  LEU B CA  1 
ATOM   4513 C C   . LEU B 1 198 ? -1.390  -37.644 -52.359 1.00 65.60  ? 198  LEU B C   1 
ATOM   4514 O O   . LEU B 1 198 ? -0.820  -36.754 -53.014 1.00 65.27  ? 198  LEU B O   1 
ATOM   4515 C CB  . LEU B 1 198 ? -0.075  -39.541 -53.566 1.00 61.47  ? 198  LEU B CB  1 
ATOM   4516 C CG  . LEU B 1 198 ? 1.324   -39.184 -52.973 1.00 65.47  ? 198  LEU B CG  1 
ATOM   4517 C CD1 . LEU B 1 198 ? 1.548   -39.754 -51.542 1.00 64.72  ? 198  LEU B CD1 1 
ATOM   4518 C CD2 . LEU B 1 198 ? 2.432   -39.655 -53.910 1.00 68.27  ? 198  LEU B CD2 1 
ATOM   4519 N N   . LEU B 1 199 ? -2.062  -37.392 -51.218 1.00 60.66  ? 199  LEU B N   1 
ATOM   4520 C CA  . LEU B 1 199 ? -2.182  -36.057 -50.641 1.00 59.08  ? 199  LEU B CA  1 
ATOM   4521 C C   . LEU B 1 199 ? -0.853  -35.559 -50.096 1.00 63.88  ? 199  LEU B C   1 
ATOM   4522 O O   . LEU B 1 199 ? -0.483  -35.881 -48.980 1.00 65.22  ? 199  LEU B O   1 
ATOM   4523 C CB  . LEU B 1 199 ? -3.297  -36.001 -49.557 1.00 57.67  ? 199  LEU B CB  1 
ATOM   4524 C CG  . LEU B 1 199 ? -3.666  -34.622 -48.991 1.00 58.88  ? 199  LEU B CG  1 
ATOM   4525 C CD1 . LEU B 1 199 ? -3.705  -33.545 -50.071 1.00 58.11  ? 199  LEU B CD1 1 
ATOM   4526 C CD2 . LEU B 1 199 ? -4.964  -34.678 -48.258 1.00 56.36  ? 199  LEU B CD2 1 
ATOM   4527 N N   . GLN B 1 200 ? -0.139  -34.791 -50.879 1.00 59.45  ? 200  GLN B N   1 
ATOM   4528 C CA  . GLN B 1 200 ? 1.096   -34.202 -50.401 1.00 59.27  ? 200  GLN B CA  1 
ATOM   4529 C C   . GLN B 1 200 ? 0.738   -32.850 -49.847 1.00 63.81  ? 200  GLN B C   1 
ATOM   4530 O O   . GLN B 1 200 ? 0.149   -32.024 -50.550 1.00 62.53  ? 200  GLN B O   1 
ATOM   4531 C CB  . GLN B 1 200 ? 2.094   -33.997 -51.544 1.00 60.96  ? 200  GLN B CB  1 
ATOM   4532 C CG  . GLN B 1 200 ? 2.792   -35.250 -52.018 1.00 90.56  ? 200  GLN B CG  1 
ATOM   4533 C CD  . GLN B 1 200 ? 3.600   -34.968 -53.262 1.00 121.80 ? 200  GLN B CD  1 
ATOM   4534 O OE1 . GLN B 1 200 ? 3.062   -34.675 -54.339 1.00 117.25 ? 200  GLN B OE1 1 
ATOM   4535 N NE2 . GLN B 1 200 ? 4.911   -35.057 -53.135 1.00 121.29 ? 200  GLN B NE2 1 
ATOM   4536 N N   . MET B 1 201 ? 1.104   -32.596 -48.598 1.00 62.90  ? 201  MET B N   1 
ATOM   4537 C CA  . MET B 1 201 ? 0.879   -31.274 -48.038 1.00 63.83  ? 201  MET B CA  1 
ATOM   4538 C C   . MET B 1 201 ? 2.131   -30.406 -48.255 1.00 74.51  ? 201  MET B C   1 
ATOM   4539 O O   . MET B 1 201 ? 2.273   -29.793 -49.326 1.00 76.36  ? 201  MET B O   1 
ATOM   4540 C CB  . MET B 1 201 ? 0.358   -31.309 -46.596 1.00 65.21  ? 201  MET B CB  1 
ATOM   4541 C CG  . MET B 1 201 ? -1.158  -31.220 -46.559 1.00 67.77  ? 201  MET B CG  1 
ATOM   4542 S SD  . MET B 1 201 ? -1.946  -30.659 -45.035 1.00 70.75  ? 201  MET B SD  1 
ATOM   4543 C CE  . MET B 1 201 ? -1.285  -28.994 -44.914 1.00 67.36  ? 201  MET B CE  1 
ATOM   4544 N N   . GLU B 1 202 ? 3.057   -30.404 -47.299 1.00 73.25  ? 202  GLU B N   1 
ATOM   4545 C CA  . GLU B 1 202 ? 4.299   -29.640 -47.400 1.00 73.90  ? 202  GLU B CA  1 
ATOM   4546 C C   . GLU B 1 202 ? 5.392   -30.678 -47.644 1.00 78.55  ? 202  GLU B C   1 
ATOM   4547 O O   . GLU B 1 202 ? 5.601   -31.117 -48.775 1.00 76.78  ? 202  GLU B O   1 
ATOM   4548 C CB  . GLU B 1 202 ? 4.530   -28.866 -46.082 1.00 75.33  ? 202  GLU B CB  1 
ATOM   4549 C CG  . GLU B 1 202 ? 4.168   -27.393 -46.149 1.00 87.54  ? 202  GLU B CG  1 
ATOM   4550 C CD  . GLU B 1 202 ? 5.220   -26.455 -46.718 1.00 113.66 ? 202  GLU B CD  1 
ATOM   4551 O OE1 . GLU B 1 202 ? 6.431   -26.765 -46.612 1.00 120.75 ? 202  GLU B OE1 1 
ATOM   4552 O OE2 . GLU B 1 202 ? 4.829   -25.373 -47.213 1.00 96.87  ? 202  GLU B OE2 1 
ATOM   4553 N N   . ASP B 1 203 ? 6.007   -31.124 -46.545 1.00 77.43  ? 203  ASP B N   1 
ATOM   4554 C CA  . ASP B 1 203 ? 7.019   -32.162 -46.434 1.00 78.32  ? 203  ASP B CA  1 
ATOM   4555 C C   . ASP B 1 203 ? 6.328   -33.422 -45.895 1.00 79.87  ? 203  ASP B C   1 
ATOM   4556 O O   . ASP B 1 203 ? 6.915   -34.509 -45.923 1.00 80.72  ? 203  ASP B O   1 
ATOM   4557 C CB  . ASP B 1 203 ? 8.146   -31.708 -45.476 1.00 81.98  ? 203  ASP B CB  1 
ATOM   4558 C CG  . ASP B 1 203 ? 7.703   -30.905 -44.254 1.00 103.66 ? 203  ASP B CG  1 
ATOM   4559 O OD1 . ASP B 1 203 ? 6.539   -31.108 -43.783 1.00 106.18 ? 203  ASP B OD1 1 
ATOM   4560 O OD2 . ASP B 1 203 ? 8.512   -30.076 -43.764 1.00 110.87 ? 203  ASP B OD2 1 
ATOM   4561 N N   . LYS B 1 204 ? 5.097   -33.265 -45.374 1.00 72.68  ? 204  LYS B N   1 
ATOM   4562 C CA  . LYS B 1 204 ? 4.275   -34.377 -44.893 1.00 71.14  ? 204  LYS B CA  1 
ATOM   4563 C C   . LYS B 1 204 ? 3.439   -34.900 -46.101 1.00 68.06  ? 204  LYS B C   1 
ATOM   4564 O O   . LYS B 1 204 ? 3.269   -34.156 -47.060 1.00 68.71  ? 204  LYS B O   1 
ATOM   4565 C CB  . LYS B 1 204 ? 3.385   -33.929 -43.705 1.00 75.29  ? 204  LYS B CB  1 
ATOM   4566 C CG  . LYS B 1 204 ? 4.141   -33.461 -42.427 1.00 91.91  ? 204  LYS B CG  1 
ATOM   4567 C CD  . LYS B 1 204 ? 3.209   -33.119 -41.211 1.00 98.04  ? 204  LYS B CD  1 
ATOM   4568 C CE  . LYS B 1 204 ? 2.825   -34.312 -40.333 1.00 105.76 ? 204  LYS B CE  1 
ATOM   4569 N NZ  . LYS B 1 204 ? 1.822   -33.974 -39.267 1.00 103.79 ? 204  LYS B NZ  1 
ATOM   4570 N N   . ALA B 1 205 ? 2.996   -36.170 -46.096 1.00 59.34  ? 205  ALA B N   1 
ATOM   4571 C CA  . ALA B 1 205 ? 2.255   -36.794 -47.212 1.00 57.86  ? 205  ALA B CA  1 
ATOM   4572 C C   . ALA B 1 205 ? 1.444   -37.981 -46.752 1.00 59.61  ? 205  ALA B C   1 
ATOM   4573 O O   . ALA B 1 205 ? 1.826   -38.617 -45.790 1.00 61.71  ? 205  ALA B O   1 
ATOM   4574 C CB  . ALA B 1 205 ? 3.204   -37.235 -48.306 1.00 58.78  ? 205  ALA B CB  1 
ATOM   4575 N N   . TRP B 1 206 ? 0.330   -38.279 -47.413 1.00 53.23  ? 206  TRP B N   1 
ATOM   4576 C CA  . TRP B 1 206 ? -0.612  -39.328 -47.011 1.00 52.30  ? 206  TRP B CA  1 
ATOM   4577 C C   . TRP B 1 206 ? -1.315  -39.910 -48.234 1.00 57.93  ? 206  TRP B C   1 
ATOM   4578 O O   . TRP B 1 206 ? -1.394  -39.253 -49.267 1.00 57.03  ? 206  TRP B O   1 
ATOM   4579 C CB  . TRP B 1 206 ? -1.735  -38.709 -46.157 1.00 50.25  ? 206  TRP B CB  1 
ATOM   4580 C CG  . TRP B 1 206 ? -1.373  -38.125 -44.834 1.00 50.50  ? 206  TRP B CG  1 
ATOM   4581 C CD1 . TRP B 1 206 ? -1.630  -38.677 -43.626 1.00 53.34  ? 206  TRP B CD1 1 
ATOM   4582 C CD2 . TRP B 1 206 ? -0.929  -36.786 -44.572 1.00 50.61  ? 206  TRP B CD2 1 
ATOM   4583 N NE1 . TRP B 1 206 ? -1.256  -37.819 -42.622 1.00 52.90  ? 206  TRP B NE1 1 
ATOM   4584 C CE2 . TRP B 1 206 ? -0.816  -36.650 -43.174 1.00 54.09  ? 206  TRP B CE2 1 
ATOM   4585 C CE3 . TRP B 1 206 ? -0.584  -35.687 -45.382 1.00 52.47  ? 206  TRP B CE3 1 
ATOM   4586 C CZ2 . TRP B 1 206 ? -0.355  -35.473 -42.563 1.00 53.31  ? 206  TRP B CZ2 1 
ATOM   4587 C CZ3 . TRP B 1 206 ? -0.106  -34.524 -44.775 1.00 53.74  ? 206  TRP B CZ3 1 
ATOM   4588 C CH2 . TRP B 1 206 ? -0.017  -34.421 -43.381 1.00 54.01  ? 206  TRP B CH2 1 
ATOM   4589 N N   . LEU B 1 207 ? -1.932  -41.075 -48.076 1.00 56.63  ? 207  LEU B N   1 
ATOM   4590 C CA  . LEU B 1 207 ? -2.680  -41.727 -49.131 1.00 58.93  ? 207  LEU B CA  1 
ATOM   4591 C C   . LEU B 1 207 ? -4.078  -41.802 -48.662 1.00 64.37  ? 207  LEU B C   1 
ATOM   4592 O O   . LEU B 1 207 ? -4.319  -42.276 -47.555 1.00 65.00  ? 207  LEU B O   1 
ATOM   4593 C CB  . LEU B 1 207 ? -2.134  -43.118 -49.451 1.00 60.49  ? 207  LEU B CB  1 
ATOM   4594 C CG  . LEU B 1 207 ? -2.036  -43.404 -50.969 1.00 67.95  ? 207  LEU B CG  1 
ATOM   4595 C CD1 . LEU B 1 207 ? -0.757  -42.826 -51.580 1.00 68.03  ? 207  LEU B CD1 1 
ATOM   4596 C CD2 . LEU B 1 207 ? -2.127  -44.882 -51.262 1.00 73.68  ? 207  LEU B CD2 1 
ATOM   4597 N N   . VAL B 1 208 ? -5.007  -41.262 -49.451 1.00 61.87  ? 208  VAL B N   1 
ATOM   4598 C CA  . VAL B 1 208 ? -6.390  -41.138 -49.016 1.00 62.28  ? 208  VAL B CA  1 
ATOM   4599 C C   . VAL B 1 208 ? -7.395  -41.294 -50.144 1.00 65.78  ? 208  VAL B C   1 
ATOM   4600 O O   . VAL B 1 208 ? -7.081  -40.987 -51.290 1.00 66.46  ? 208  VAL B O   1 
ATOM   4601 C CB  . VAL B 1 208 ? -6.587  -39.802 -48.234 1.00 67.36  ? 208  VAL B CB  1 
ATOM   4602 C CG1 . VAL B 1 208 ? -6.524  -38.577 -49.145 1.00 67.12  ? 208  VAL B CG1 1 
ATOM   4603 C CG2 . VAL B 1 208 ? -7.886  -39.820 -47.456 1.00 68.01  ? 208  VAL B CG2 1 
ATOM   4604 N N   . HIS B 1 209 ? -8.622  -41.718 -49.785 1.00 60.96  ? 209  HIS B N   1 
ATOM   4605 C CA  . HIS B 1 209 ? -9.752  -41.950 -50.656 1.00 60.60  ? 209  HIS B CA  1 
ATOM   4606 C C   . HIS B 1 209 ? -10.120 -40.773 -51.545 1.00 61.64  ? 209  HIS B C   1 
ATOM   4607 O O   . HIS B 1 209 ? -10.194 -39.626 -51.083 1.00 61.51  ? 209  HIS B O   1 
ATOM   4608 C CB  . HIS B 1 209 ? -10.944 -42.385 -49.827 1.00 62.79  ? 209  HIS B CB  1 
ATOM   4609 C CG  . HIS B 1 209 ? -11.953 -43.130 -50.639 1.00 67.83  ? 209  HIS B CG  1 
ATOM   4610 N ND1 . HIS B 1 209 ? -11.659 -44.371 -51.203 1.00 69.94  ? 209  HIS B ND1 1 
ATOM   4611 C CD2 . HIS B 1 209 ? -13.217 -42.775 -50.984 1.00 70.34  ? 209  HIS B CD2 1 
ATOM   4612 C CE1 . HIS B 1 209 ? -12.758 -44.729 -51.853 1.00 69.68  ? 209  HIS B CE1 1 
ATOM   4613 N NE2 . HIS B 1 209 ? -13.720 -43.798 -51.760 1.00 69.98  ? 209  HIS B NE2 1 
ATOM   4614 N N   . ARG B 1 210 ? -10.330 -41.077 -52.838 1.00 56.09  ? 210  ARG B N   1 
ATOM   4615 C CA  . ARG B 1 210 ? -10.693 -40.136 -53.894 1.00 55.18  ? 210  ARG B CA  1 
ATOM   4616 C C   . ARG B 1 210 ? -11.870 -39.264 -53.488 1.00 59.56  ? 210  ARG B C   1 
ATOM   4617 O O   . ARG B 1 210 ? -11.752 -38.039 -53.533 1.00 61.02  ? 210  ARG B O   1 
ATOM   4618 C CB  . ARG B 1 210 ? -11.003 -40.865 -55.209 1.00 53.84  ? 210  ARG B CB  1 
ATOM   4619 C CG  . ARG B 1 210 ? -11.443 -39.910 -56.303 1.00 67.23  ? 210  ARG B CG  1 
ATOM   4620 C CD  . ARG B 1 210 ? -12.162 -40.555 -57.475 1.00 75.79  ? 210  ARG B CD  1 
ATOM   4621 N NE  . ARG B 1 210 ? -12.102 -39.689 -58.658 1.00 76.38  ? 210  ARG B NE  1 
ATOM   4622 C CZ  . ARG B 1 210 ? -11.084 -39.669 -59.518 1.00 91.28  ? 210  ARG B CZ  1 
ATOM   4623 N NH1 . ARG B 1 210 ? -10.044 -40.482 -59.348 1.00 84.07  ? 210  ARG B NH1 1 
ATOM   4624 N NH2 . ARG B 1 210 ? -11.103 -38.845 -60.560 1.00 69.71  ? 210  ARG B NH2 1 
ATOM   4625 N N   . GLN B 1 211 ? -12.992 -39.898 -53.085 1.00 53.32  ? 211  GLN B N   1 
ATOM   4626 C CA  . GLN B 1 211 ? -14.223 -39.221 -52.689 1.00 51.55  ? 211  GLN B CA  1 
ATOM   4627 C C   . GLN B 1 211 ? -13.993 -38.237 -51.556 1.00 52.81  ? 211  GLN B C   1 
ATOM   4628 O O   . GLN B 1 211 ? -14.430 -37.099 -51.673 1.00 52.22  ? 211  GLN B O   1 
ATOM   4629 C CB  . GLN B 1 211 ? -15.351 -40.230 -52.350 1.00 52.37  ? 211  GLN B CB  1 
ATOM   4630 C CG  . GLN B 1 211 ? -16.772 -39.656 -52.437 1.00 67.41  ? 211  GLN B CG  1 
ATOM   4631 C CD  . GLN B 1 211 ? -17.110 -39.030 -53.796 1.00 102.89 ? 211  GLN B CD  1 
ATOM   4632 O OE1 . GLN B 1 211 ? -17.466 -37.841 -53.896 1.00 94.81  ? 211  GLN B OE1 1 
ATOM   4633 N NE2 . GLN B 1 211 ? -17.013 -39.817 -54.878 1.00 102.33 ? 211  GLN B NE2 1 
ATOM   4634 N N   . TRP B 1 212 ? -13.294 -38.661 -50.477 1.00 47.34  ? 212  TRP B N   1 
ATOM   4635 C CA  . TRP B 1 212 ? -13.014 -37.804 -49.322 1.00 45.67  ? 212  TRP B CA  1 
ATOM   4636 C C   . TRP B 1 212 ? -12.260 -36.565 -49.817 1.00 49.34  ? 212  TRP B C   1 
ATOM   4637 O O   . TRP B 1 212 ? -12.680 -35.423 -49.543 1.00 48.69  ? 212  TRP B O   1 
ATOM   4638 C CB  . TRP B 1 212 ? -12.206 -38.564 -48.257 1.00 43.90  ? 212  TRP B CB  1 
ATOM   4639 C CG  . TRP B 1 212 ? -11.900 -37.767 -47.026 1.00 44.91  ? 212  TRP B CG  1 
ATOM   4640 C CD1 . TRP B 1 212 ? -12.700 -37.609 -45.934 1.00 47.77  ? 212  TRP B CD1 1 
ATOM   4641 C CD2 . TRP B 1 212 ? -10.692 -37.019 -46.755 1.00 44.94  ? 212  TRP B CD2 1 
ATOM   4642 N NE1 . TRP B 1 212 ? -12.084 -36.782 -45.009 1.00 47.50  ? 212  TRP B NE1 1 
ATOM   4643 C CE2 . TRP B 1 212 ? -10.857 -36.397 -45.495 1.00 48.45  ? 212  TRP B CE2 1 
ATOM   4644 C CE3 . TRP B 1 212 ? -9.532  -36.724 -47.506 1.00 45.66  ? 212  TRP B CE3 1 
ATOM   4645 C CZ2 . TRP B 1 212 ? -9.896  -35.536 -44.953 1.00 46.71  ? 212  TRP B CZ2 1 
ATOM   4646 C CZ3 . TRP B 1 212 ? -8.578  -35.883 -46.954 1.00 46.31  ? 212  TRP B CZ3 1 
ATOM   4647 C CH2 . TRP B 1 212 ? -8.770  -35.294 -45.700 1.00 46.60  ? 212  TRP B CH2 1 
ATOM   4648 N N   . PHE B 1 213 ? -11.182 -36.803 -50.611 1.00 44.13  ? 213  PHE B N   1 
ATOM   4649 C CA  . PHE B 1 213 ? -10.377 -35.746 -51.189 1.00 42.02  ? 213  PHE B CA  1 
ATOM   4650 C C   . PHE B 1 213 ? -11.241 -34.742 -51.944 1.00 44.37  ? 213  PHE B C   1 
ATOM   4651 O O   . PHE B 1 213 ? -11.271 -33.595 -51.550 1.00 45.32  ? 213  PHE B O   1 
ATOM   4652 C CB  . PHE B 1 213 ? -9.298  -36.327 -52.098 1.00 42.86  ? 213  PHE B CB  1 
ATOM   4653 C CG  . PHE B 1 213 ? -8.464  -35.306 -52.857 1.00 43.01  ? 213  PHE B CG  1 
ATOM   4654 C CD1 . PHE B 1 213 ? -7.436  -34.617 -52.229 1.00 44.43  ? 213  PHE B CD1 1 
ATOM   4655 C CD2 . PHE B 1 213 ? -8.668  -35.085 -54.214 1.00 43.84  ? 213  PHE B CD2 1 
ATOM   4656 C CE1 . PHE B 1 213 ? -6.643  -33.705 -52.945 1.00 44.82  ? 213  PHE B CE1 1 
ATOM   4657 C CE2 . PHE B 1 213 ? -7.878  -34.171 -54.918 1.00 45.22  ? 213  PHE B CE2 1 
ATOM   4658 C CZ  . PHE B 1 213 ? -6.876  -33.482 -54.278 1.00 42.86  ? 213  PHE B CZ  1 
ATOM   4659 N N   . LEU B 1 214 ? -11.990 -35.157 -52.964 1.00 39.07  ? 214  LEU B N   1 
ATOM   4660 C CA  . LEU B 1 214 ? -12.801 -34.220 -53.763 1.00 38.16  ? 214  LEU B CA  1 
ATOM   4661 C C   . LEU B 1 214 ? -13.779 -33.409 -52.933 1.00 46.58  ? 214  LEU B C   1 
ATOM   4662 O O   . LEU B 1 214 ? -13.893 -32.195 -53.149 1.00 48.53  ? 214  LEU B O   1 
ATOM   4663 C CB  . LEU B 1 214 ? -13.528 -34.892 -54.956 1.00 37.03  ? 214  LEU B CB  1 
ATOM   4664 C CG  . LEU B 1 214 ? -12.721 -35.882 -55.864 1.00 38.98  ? 214  LEU B CG  1 
ATOM   4665 C CD1 . LEU B 1 214 ? -13.655 -36.834 -56.593 1.00 39.29  ? 214  LEU B CD1 1 
ATOM   4666 C CD2 . LEU B 1 214 ? -11.709 -35.184 -56.791 1.00 31.72  ? 214  LEU B CD2 1 
ATOM   4667 N N   . ASP B 1 215 ? -14.426 -34.056 -51.931 1.00 44.05  ? 215  ASP B N   1 
ATOM   4668 C CA  . ASP B 1 215 ? -15.435 -33.474 -51.016 1.00 42.99  ? 215  ASP B CA  1 
ATOM   4669 C C   . ASP B 1 215 ? -14.856 -32.490 -49.944 1.00 45.03  ? 215  ASP B C   1 
ATOM   4670 O O   . ASP B 1 215 ? -15.584 -32.073 -49.036 1.00 45.51  ? 215  ASP B O   1 
ATOM   4671 C CB  . ASP B 1 215 ? -16.254 -34.601 -50.352 1.00 44.49  ? 215  ASP B CB  1 
ATOM   4672 C CG  . ASP B 1 215 ? -17.072 -35.446 -51.303 1.00 67.08  ? 215  ASP B CG  1 
ATOM   4673 O OD1 . ASP B 1 215 ? -16.717 -35.507 -52.500 1.00 71.29  ? 215  ASP B OD1 1 
ATOM   4674 O OD2 . ASP B 1 215 ? -18.064 -36.062 -50.850 1.00 78.71  ? 215  ASP B OD2 1 
ATOM   4675 N N   . LEU B 1 216 ? -13.572 -32.110 -50.051 1.00 38.35  ? 216  LEU B N   1 
ATOM   4676 C CA  . LEU B 1 216 ? -13.004 -31.200 -49.085 1.00 37.16  ? 216  LEU B CA  1 
ATOM   4677 C C   . LEU B 1 216 ? -13.559 -29.829 -49.329 1.00 44.69  ? 216  LEU B C   1 
ATOM   4678 O O   . LEU B 1 216 ? -13.529 -29.339 -50.472 1.00 45.07  ? 216  LEU B O   1 
ATOM   4679 C CB  . LEU B 1 216 ? -11.474 -31.172 -49.080 1.00 36.51  ? 216  LEU B CB  1 
ATOM   4680 C CG  . LEU B 1 216 ? -10.711 -32.430 -48.651 1.00 40.26  ? 216  LEU B CG  1 
ATOM   4681 C CD1 . LEU B 1 216 ? -9.224  -32.188 -48.706 1.00 40.15  ? 216  LEU B CD1 1 
ATOM   4682 C CD2 . LEU B 1 216 ? -11.130 -32.927 -47.297 1.00 40.54  ? 216  LEU B CD2 1 
ATOM   4683 N N   . PRO B 1 217 ? -14.098 -29.218 -48.232 1.00 42.05  ? 217  PRO B N   1 
ATOM   4684 C CA  . PRO B 1 217 ? -14.661 -27.857 -48.316 1.00 40.48  ? 217  PRO B CA  1 
ATOM   4685 C C   . PRO B 1 217 ? -13.581 -26.771 -48.459 1.00 44.65  ? 217  PRO B C   1 
ATOM   4686 O O   . PRO B 1 217 ? -13.452 -25.951 -47.549 1.00 46.40  ? 217  PRO B O   1 
ATOM   4687 C CB  . PRO B 1 217 ? -15.352 -27.722 -46.957 1.00 41.73  ? 217  PRO B CB  1 
ATOM   4688 C CG  . PRO B 1 217 ? -14.485 -28.516 -46.012 1.00 46.41  ? 217  PRO B CG  1 
ATOM   4689 C CD  . PRO B 1 217 ? -14.150 -29.733 -46.838 1.00 43.04  ? 217  PRO B CD  1 
ATOM   4690 N N   . LEU B 1 218 ? -12.792 -26.754 -49.545 1.00 39.58  ? 218  LEU B N   1 
ATOM   4691 C CA  . LEU B 1 218 ? -11.738 -25.738 -49.684 1.00 40.11  ? 218  LEU B CA  1 
ATOM   4692 C C   . LEU B 1 218 ? -11.644 -25.181 -51.117 1.00 48.57  ? 218  LEU B C   1 
ATOM   4693 O O   . LEU B 1 218 ? -12.080 -25.883 -52.047 1.00 51.56  ? 218  LEU B O   1 
ATOM   4694 C CB  . LEU B 1 218 ? -10.365 -26.311 -49.275 1.00 39.81  ? 218  LEU B CB  1 
ATOM   4695 C CG  . LEU B 1 218 ? -10.145 -26.803 -47.855 1.00 42.79  ? 218  LEU B CG  1 
ATOM   4696 C CD1 . LEU B 1 218 ? -8.885  -27.583 -47.787 1.00 42.14  ? 218  LEU B CD1 1 
ATOM   4697 C CD2 . LEU B 1 218 ? -10.111 -25.656 -46.864 1.00 43.70  ? 218  LEU B CD2 1 
ATOM   4698 N N   . PRO B 1 219 ? -11.052 -23.971 -51.350 1.00 43.49  ? 219  PRO B N   1 
ATOM   4699 C CA  . PRO B 1 219 ? -10.924 -23.487 -52.735 1.00 43.49  ? 219  PRO B CA  1 
ATOM   4700 C C   . PRO B 1 219 ? -9.967  -24.387 -53.527 1.00 49.55  ? 219  PRO B C   1 
ATOM   4701 O O   . PRO B 1 219 ? -9.006  -24.877 -52.952 1.00 49.00  ? 219  PRO B O   1 
ATOM   4702 C CB  . PRO B 1 219 ? -10.395 -22.054 -52.566 1.00 44.79  ? 219  PRO B CB  1 
ATOM   4703 C CG  . PRO B 1 219 ? -10.673 -21.702 -51.114 1.00 48.61  ? 219  PRO B CG  1 
ATOM   4704 C CD  . PRO B 1 219 ? -10.472 -22.997 -50.406 1.00 44.29  ? 219  PRO B CD  1 
ATOM   4705 N N   . TRP B 1 220 ? -10.253 -24.667 -54.809 1.00 48.20  ? 220  TRP B N   1 
ATOM   4706 C CA  . TRP B 1 220 ? -9.408  -25.564 -55.603 1.00 48.95  ? 220  TRP B CA  1 
ATOM   4707 C C   . TRP B 1 220 ? -9.185  -25.138 -57.048 1.00 55.74  ? 220  TRP B C   1 
ATOM   4708 O O   . TRP B 1 220 ? -9.859  -24.241 -57.538 1.00 54.55  ? 220  TRP B O   1 
ATOM   4709 C CB  . TRP B 1 220 ? -9.960  -26.986 -55.558 1.00 48.03  ? 220  TRP B CB  1 
ATOM   4710 C CG  . TRP B 1 220 ? -11.329 -27.120 -56.161 1.00 48.86  ? 220  TRP B CG  1 
ATOM   4711 C CD1 . TRP B 1 220 ? -12.520 -26.827 -55.566 1.00 51.79  ? 220  TRP B CD1 1 
ATOM   4712 C CD2 . TRP B 1 220 ? -11.643 -27.546 -57.497 1.00 48.36  ? 220  TRP B CD2 1 
ATOM   4713 N NE1 . TRP B 1 220 ? -13.558 -27.052 -56.448 1.00 51.07  ? 220  TRP B NE1 1 
ATOM   4714 C CE2 . TRP B 1 220 ? -13.050 -27.501 -57.635 1.00 51.46  ? 220  TRP B CE2 1 
ATOM   4715 C CE3 . TRP B 1 220 ? -10.871 -27.961 -58.593 1.00 49.30  ? 220  TRP B CE3 1 
ATOM   4716 C CZ2 . TRP B 1 220 ? -13.700 -27.887 -58.801 1.00 49.66  ? 220  TRP B CZ2 1 
ATOM   4717 C CZ3 . TRP B 1 220 ? -11.524 -28.389 -59.735 1.00 50.25  ? 220  TRP B CZ3 1 
ATOM   4718 C CH2 . TRP B 1 220 ? -12.922 -28.345 -59.832 1.00 50.47  ? 220  TRP B CH2 1 
ATOM   4719 N N   . LEU B 1 221 ? -8.185  -25.752 -57.709 1.00 57.10  ? 221  LEU B N   1 
ATOM   4720 C CA  . LEU B 1 221 ? -7.821  -25.564 -59.134 1.00 58.84  ? 221  LEU B CA  1 
ATOM   4721 C C   . LEU B 1 221 ? -7.623  -26.947 -59.760 1.00 67.45  ? 221  LEU B C   1 
ATOM   4722 O O   . LEU B 1 221 ? -6.963  -27.771 -59.117 1.00 68.88  ? 221  LEU B O   1 
ATOM   4723 C CB  . LEU B 1 221 ? -6.522  -24.781 -59.311 1.00 58.85  ? 221  LEU B CB  1 
ATOM   4724 C CG  . LEU B 1 221 ? -6.493  -23.346 -58.843 1.00 63.97  ? 221  LEU B CG  1 
ATOM   4725 C CD1 . LEU B 1 221 ? -5.070  -22.894 -58.651 1.00 64.17  ? 221  LEU B CD1 1 
ATOM   4726 C CD2 . LEU B 1 221 ? -7.221  -22.430 -59.815 1.00 67.02  ? 221  LEU B CD2 1 
ATOM   4727 N N   . PRO B 1 222 ? -8.157  -27.246 -60.985 1.00 65.09  ? 222  PRO B N   1 
ATOM   4728 C CA  . PRO B 1 222 ? -7.988  -28.596 -61.569 1.00 64.44  ? 222  PRO B CA  1 
ATOM   4729 C C   . PRO B 1 222 ? -6.535  -28.961 -61.770 1.00 68.27  ? 222  PRO B C   1 
ATOM   4730 O O   . PRO B 1 222 ? -5.692  -28.065 -61.922 1.00 68.91  ? 222  PRO B O   1 
ATOM   4731 C CB  . PRO B 1 222 ? -8.744  -28.515 -62.891 1.00 65.69  ? 222  PRO B CB  1 
ATOM   4732 C CG  . PRO B 1 222 ? -9.680  -27.377 -62.719 1.00 70.46  ? 222  PRO B CG  1 
ATOM   4733 C CD  . PRO B 1 222 ? -8.916  -26.384 -61.907 1.00 66.74  ? 222  PRO B CD  1 
ATOM   4734 N N   . GLY B 1 223 ? -6.257  -30.263 -61.648 1.00 63.36  ? 223  GLY B N   1 
ATOM   4735 C CA  . GLY B 1 223 ? -4.917  -30.837 -61.725 1.00 63.33  ? 223  GLY B CA  1 
ATOM   4736 C C   . GLY B 1 223 ? -4.082  -30.369 -62.894 1.00 66.85  ? 223  GLY B C   1 
ATOM   4737 O O   . GLY B 1 223 ? -2.880  -30.118 -62.738 1.00 64.73  ? 223  GLY B O   1 
ATOM   4738 N N   . ALA B 1 224 ? -4.745  -30.246 -64.068 1.00 64.12  ? 224  ALA B N   1 
ATOM   4739 C CA  . ALA B 1 224 ? -4.200  -29.755 -65.323 1.00 64.75  ? 224  ALA B CA  1 
ATOM   4740 C C   . ALA B 1 224 ? -3.741  -28.254 -65.262 1.00 69.98  ? 224  ALA B C   1 
ATOM   4741 O O   . ALA B 1 224 ? -2.698  -27.915 -65.839 1.00 69.03  ? 224  ALA B O   1 
ATOM   4742 C CB  . ALA B 1 224 ? -5.234  -29.942 -66.411 1.00 65.47  ? 224  ALA B CB  1 
ATOM   4743 N N   . ASP B 1 225 ? -4.522  -27.379 -64.555 1.00 67.93  ? 225  ASP B N   1 
ATOM   4744 C CA  . ASP B 1 225 ? -4.256  -25.946 -64.433 1.00 68.69  ? 225  ASP B CA  1 
ATOM   4745 C C   . ASP B 1 225 ? -3.005  -25.621 -63.611 1.00 76.54  ? 225  ASP B C   1 
ATOM   4746 O O   . ASP B 1 225 ? -3.012  -25.619 -62.373 1.00 76.74  ? 225  ASP B O   1 
ATOM   4747 C CB  . ASP B 1 225 ? -5.478  -25.150 -63.922 1.00 70.69  ? 225  ASP B CB  1 
ATOM   4748 C CG  . ASP B 1 225 ? -5.258  -23.642 -64.041 1.00 80.60  ? 225  ASP B CG  1 
ATOM   4749 O OD1 . ASP B 1 225 ? -4.317  -23.243 -64.750 1.00 88.75  ? 225  ASP B OD1 1 
ATOM   4750 O OD2 . ASP B 1 225 ? -6.052  -22.857 -63.433 1.00 78.67  ? 225  ASP B OD2 1 
ATOM   4751 N N   . THR B 1 226 ? -1.938  -25.294 -64.333 1.00 75.73  ? 226  THR B N   1 
ATOM   4752 C CA  . THR B 1 226 ? -0.640  -24.929 -63.771 1.00 76.54  ? 226  THR B CA  1 
ATOM   4753 C C   . THR B 1 226 ? -0.499  -23.409 -63.838 1.00 82.08  ? 226  THR B C   1 
ATOM   4754 O O   . THR B 1 226 ? -0.246  -22.766 -62.817 1.00 82.47  ? 226  THR B O   1 
ATOM   4755 C CB  . THR B 1 226 ? 0.479   -25.691 -64.511 1.00 86.68  ? 226  THR B CB  1 
ATOM   4756 O OG1 . THR B 1 226 ? 0.007   -26.144 -65.790 1.00 82.76  ? 226  THR B OG1 1 
ATOM   4757 C CG2 . THR B 1 226 ? 0.997   -26.879 -63.712 1.00 86.79  ? 226  THR B CG2 1 
ATOM   4758 N N   . GLN B 1 227 ? -0.776  -22.845 -65.036 1.00 78.35  ? 227  GLN B N   1 
ATOM   4759 C CA  . GLN B 1 227 ? -0.738  -21.424 -65.410 1.00 77.78  ? 227  GLN B CA  1 
ATOM   4760 C C   . GLN B 1 227 ? -1.666  -20.486 -64.610 1.00 79.46  ? 227  GLN B C   1 
ATOM   4761 O O   . GLN B 1 227 ? -1.309  -19.341 -64.353 1.00 79.21  ? 227  GLN B O   1 
ATOM   4762 C CB  . GLN B 1 227 ? -1.066  -21.244 -66.922 1.00 79.39  ? 227  GLN B CB  1 
ATOM   4763 C CG  . GLN B 1 227 ? -0.626  -22.373 -67.871 1.00 99.98  ? 227  GLN B CG  1 
ATOM   4764 C CD  . GLN B 1 227 ? -1.776  -23.243 -68.346 1.00 115.88 ? 227  GLN B CD  1 
ATOM   4765 O OE1 . GLN B 1 227 ? -2.401  -23.995 -67.578 1.00 108.99 ? 227  GLN B OE1 1 
ATOM   4766 N NE2 . GLN B 1 227 ? -2.042  -23.197 -69.643 1.00 105.24 ? 227  GLN B NE2 1 
ATOM   4767 N N   . GLY B 1 228 ? -2.861  -20.949 -64.296 1.00 75.43  ? 228  GLY B N   1 
ATOM   4768 C CA  . GLY B 1 228 ? -3.905  -20.137 -63.677 1.00 75.40  ? 228  GLY B CA  1 
ATOM   4769 C C   . GLY B 1 228 ? -4.028  -20.101 -62.174 1.00 78.63  ? 228  GLY B C   1 
ATOM   4770 O O   . GLY B 1 228 ? -3.603  -21.030 -61.470 1.00 79.58  ? 228  GLY B O   1 
ATOM   4771 N N   . SER B 1 229 ? -4.683  -19.018 -61.706 1.00 71.68  ? 229  SER B N   1 
ATOM   4772 C CA  . SER B 1 229 ? -4.884  -18.643 -60.314 1.00 70.08  ? 229  SER B CA  1 
ATOM   4773 C C   . SER B 1 229 ? -6.350  -18.254 -60.006 1.00 69.95  ? 229  SER B C   1 
ATOM   4774 O O   . SER B 1 229 ? -6.591  -17.405 -59.124 1.00 68.96  ? 229  SER B O   1 
ATOM   4775 C CB  . SER B 1 229 ? -3.975  -17.461 -60.006 1.00 76.08  ? 229  SER B CB  1 
ATOM   4776 O OG  . SER B 1 229 ? -4.325  -16.357 -60.831 1.00 89.77  ? 229  SER B OG  1 
ATOM   4777 N N   . ASN B 1 230 ? -7.323  -18.883 -60.731 1.00 63.67  ? 230  ASN B N   1 
ATOM   4778 C CA  . ASN B 1 230 ? -8.772  -18.641 -60.580 1.00 60.69  ? 230  ASN B CA  1 
ATOM   4779 C C   . ASN B 1 230 ? -9.379  -19.717 -59.730 1.00 58.46  ? 230  ASN B C   1 
ATOM   4780 O O   . ASN B 1 230 ? -10.075 -20.593 -60.232 1.00 59.23  ? 230  ASN B O   1 
ATOM   4781 C CB  . ASN B 1 230 ? -9.496  -18.554 -61.934 1.00 57.30  ? 230  ASN B CB  1 
ATOM   4782 C CG  . ASN B 1 230 ? -8.949  -17.534 -62.889 1.00 72.90  ? 230  ASN B CG  1 
ATOM   4783 O OD1 . ASN B 1 230 ? -8.175  -16.626 -62.518 1.00 65.49  ? 230  ASN B OD1 1 
ATOM   4784 N ND2 . ASN B 1 230 ? -9.372  -17.654 -64.148 1.00 63.99  ? 230  ASN B ND2 1 
ATOM   4785 N N   . TRP B 1 231 ? -9.067  -19.672 -58.445 1.00 50.04  ? 231  TRP B N   1 
ATOM   4786 C CA  . TRP B 1 231 ? -9.530  -20.603 -57.424 1.00 48.10  ? 231  TRP B CA  1 
ATOM   4787 C C   . TRP B 1 231 ? -11.056 -20.793 -57.382 1.00 46.97  ? 231  TRP B C   1 
ATOM   4788 O O   . TRP B 1 231 ? -11.785 -19.844 -57.077 1.00 48.88  ? 231  TRP B O   1 
ATOM   4789 C CB  . TRP B 1 231 ? -9.016  -20.144 -56.054 1.00 46.93  ? 231  TRP B CB  1 
ATOM   4790 C CG  . TRP B 1 231 ? -7.539  -20.322 -55.869 1.00 48.40  ? 231  TRP B CG  1 
ATOM   4791 C CD1 . TRP B 1 231 ? -6.585  -19.348 -55.870 1.00 51.37  ? 231  TRP B CD1 1 
ATOM   4792 C CD2 . TRP B 1 231 ? -6.859  -21.550 -55.606 1.00 48.59  ? 231  TRP B CD2 1 
ATOM   4793 N NE1 . TRP B 1 231 ? -5.351  -19.895 -55.618 1.00 50.71  ? 231  TRP B NE1 1 
ATOM   4794 C CE2 . TRP B 1 231 ? -5.489  -21.248 -55.459 1.00 52.53  ? 231  TRP B CE2 1 
ATOM   4795 C CE3 . TRP B 1 231 ? -7.285  -22.870 -55.406 1.00 50.62  ? 231  TRP B CE3 1 
ATOM   4796 C CZ2 . TRP B 1 231 ? -4.537  -22.225 -55.149 1.00 52.86  ? 231  TRP B CZ2 1 
ATOM   4797 C CZ3 . TRP B 1 231 ? -6.341  -23.842 -55.122 1.00 53.07  ? 231  TRP B CZ3 1 
ATOM   4798 C CH2 . TRP B 1 231 ? -4.981  -23.520 -55.000 1.00 53.88  ? 231  TRP B CH2 1 
ATOM   4799 N N   . ILE B 1 232 ? -11.533 -22.005 -57.681 1.00 37.27  ? 232  ILE B N   1 
ATOM   4800 C CA  . ILE B 1 232 ? -12.948 -22.361 -57.573 1.00 37.20  ? 232  ILE B CA  1 
ATOM   4801 C C   . ILE B 1 232 ? -13.296 -22.441 -56.050 1.00 46.49  ? 232  ILE B C   1 
ATOM   4802 O O   . ILE B 1 232 ? -12.412 -22.762 -55.267 1.00 46.69  ? 232  ILE B O   1 
ATOM   4803 C CB  . ILE B 1 232 ? -13.199 -23.724 -58.261 1.00 39.49  ? 232  ILE B CB  1 
ATOM   4804 C CG1 . ILE B 1 232 ? -12.873 -23.669 -59.749 1.00 39.94  ? 232  ILE B CG1 1 
ATOM   4805 C CG2 . ILE B 1 232 ? -14.613 -24.234 -58.031 1.00 39.16  ? 232  ILE B CG2 1 
ATOM   4806 C CD1 . ILE B 1 232 ? -11.895 -24.692 -60.222 1.00 44.21  ? 232  ILE B CD1 1 
ATOM   4807 N N   . GLN B 1 233 ? -14.548 -22.123 -55.634 1.00 45.34  ? 233  GLN B N   1 
ATOM   4808 C CA  . GLN B 1 233 ? -15.040 -22.174 -54.244 1.00 45.89  ? 233  GLN B CA  1 
ATOM   4809 C C   . GLN B 1 233 ? -14.354 -21.224 -53.225 1.00 48.31  ? 233  GLN B C   1 
ATOM   4810 O O   . GLN B 1 233 ? -14.378 -21.537 -52.046 1.00 48.40  ? 233  GLN B O   1 
ATOM   4811 C CB  . GLN B 1 233 ? -14.991 -23.619 -53.695 1.00 48.59  ? 233  GLN B CB  1 
ATOM   4812 C CG  . GLN B 1 233 ? -16.038 -24.573 -54.253 1.00 81.42  ? 233  GLN B CG  1 
ATOM   4813 C CD  . GLN B 1 233 ? -15.654 -26.043 -54.090 1.00 113.45 ? 233  GLN B CD  1 
ATOM   4814 O OE1 . GLN B 1 233 ? -16.055 -26.897 -54.914 1.00 114.25 ? 233  GLN B OE1 1 
ATOM   4815 N NE2 . GLN B 1 233 ? -14.872 -26.384 -53.038 1.00 93.78  ? 233  GLN B NE2 1 
ATOM   4816 N N   . LYS B 1 234 ? -13.802 -20.074 -53.620 1.00 45.34  ? 234  LYS B N   1 
ATOM   4817 C CA  . LYS B 1 234 ? -13.163 -19.126 -52.669 1.00 45.36  ? 234  LYS B CA  1 
ATOM   4818 C C   . LYS B 1 234 ? -13.992 -18.901 -51.410 1.00 53.85  ? 234  LYS B C   1 
ATOM   4819 O O   . LYS B 1 234 ? -13.444 -18.715 -50.330 1.00 53.93  ? 234  LYS B O   1 
ATOM   4820 C CB  . LYS B 1 234 ? -12.844 -17.762 -53.328 1.00 47.33  ? 234  LYS B CB  1 
ATOM   4821 C CG  . LYS B 1 234 ? -11.702 -17.821 -54.374 1.00 55.58  ? 234  LYS B CG  1 
ATOM   4822 C CD  . LYS B 1 234 ? -11.588 -16.648 -55.330 1.00 57.51  ? 234  LYS B CD  1 
ATOM   4823 C CE  . LYS B 1 234 ? -12.551 -16.711 -56.489 1.00 72.75  ? 234  LYS B CE  1 
ATOM   4824 N NZ  . LYS B 1 234 ? -11.871 -16.904 -57.783 1.00 77.59  ? 234  LYS B NZ  1 
ATOM   4825 N N   . GLU B 1 235 ? -15.320 -18.991 -51.560 1.00 55.00  ? 235  GLU B N   1 
ATOM   4826 C CA  . GLU B 1 235 ? -16.364 -18.871 -50.542 1.00 57.40  ? 235  GLU B CA  1 
ATOM   4827 C C   . GLU B 1 235 ? -16.106 -19.756 -49.303 1.00 63.52  ? 235  GLU B C   1 
ATOM   4828 O O   . GLU B 1 235 ? -16.605 -19.462 -48.217 1.00 66.14  ? 235  GLU B O   1 
ATOM   4829 C CB  . GLU B 1 235 ? -17.713 -19.275 -51.160 1.00 59.78  ? 235  GLU B CB  1 
ATOM   4830 C CG  . GLU B 1 235 ? -18.131 -18.465 -52.381 1.00 81.74  ? 235  GLU B CG  1 
ATOM   4831 C CD  . GLU B 1 235 ? -17.633 -18.965 -53.728 1.00 125.64 ? 235  GLU B CD  1 
ATOM   4832 O OE1 . GLU B 1 235 ? -17.684 -20.192 -53.977 1.00 135.62 ? 235  GLU B OE1 1 
ATOM   4833 O OE2 . GLU B 1 235 ? -17.241 -18.114 -54.558 1.00 125.02 ? 235  GLU B OE2 1 
ATOM   4834 N N   . THR B 1 236 ? -15.343 -20.838 -49.467 1.00 58.11  ? 236  THR B N   1 
ATOM   4835 C CA  . THR B 1 236 ? -15.034 -21.763 -48.385 1.00 57.10  ? 236  THR B CA  1 
ATOM   4836 C C   . THR B 1 236 ? -13.991 -21.176 -47.404 1.00 62.25  ? 236  THR B C   1 
ATOM   4837 O O   . THR B 1 236 ? -13.881 -21.663 -46.283 1.00 63.54  ? 236  THR B O   1 
ATOM   4838 C CB  . THR B 1 236 ? -14.651 -23.117 -48.946 1.00 56.13  ? 236  THR B CB  1 
ATOM   4839 O OG1 . THR B 1 236 ? -13.471 -22.960 -49.713 1.00 60.50  ? 236  THR B OG1 1 
ATOM   4840 C CG2 . THR B 1 236 ? -15.736 -23.719 -49.825 1.00 49.94  ? 236  THR B CG2 1 
ATOM   4841 N N   . LEU B 1 237 ? -13.265 -20.126 -47.799 1.00 57.59  ? 237  LEU B N   1 
ATOM   4842 C CA  . LEU B 1 237 ? -12.296 -19.470 -46.914 1.00 57.73  ? 237  LEU B CA  1 
ATOM   4843 C C   . LEU B 1 237 ? -12.663 -18.002 -46.687 1.00 67.37  ? 237  LEU B C   1 
ATOM   4844 O O   . LEU B 1 237 ? -12.016 -17.300 -45.891 1.00 66.43  ? 237  LEU B O   1 
ATOM   4845 C CB  . LEU B 1 237 ? -10.862 -19.540 -47.471 1.00 56.70  ? 237  LEU B CB  1 
ATOM   4846 C CG  . LEU B 1 237 ? -10.085 -20.839 -47.396 1.00 58.56  ? 237  LEU B CG  1 
ATOM   4847 C CD1 . LEU B 1 237 ? -8.618  -20.569 -47.404 1.00 56.00  ? 237  LEU B CD1 1 
ATOM   4848 C CD2 . LEU B 1 237 ? -10.406 -21.611 -46.159 1.00 60.90  ? 237  LEU B CD2 1 
ATOM   4849 N N   . VAL B 1 238 ? -13.671 -17.524 -47.438 1.00 67.38  ? 238  VAL B N   1 
ATOM   4850 C CA  . VAL B 1 238 ? -14.093 -16.133 -47.363 1.00 67.76  ? 238  VAL B CA  1 
ATOM   4851 C C   . VAL B 1 238 ? -15.454 -16.063 -46.693 1.00 74.91  ? 238  VAL B C   1 
ATOM   4852 O O   . VAL B 1 238 ? -16.310 -16.926 -46.916 1.00 74.29  ? 238  VAL B O   1 
ATOM   4853 C CB  . VAL B 1 238 ? -14.030 -15.432 -48.751 1.00 70.34  ? 238  VAL B CB  1 
ATOM   4854 C CG1 . VAL B 1 238 ? -14.189 -13.948 -48.612 1.00 69.73  ? 238  VAL B CG1 1 
ATOM   4855 C CG2 . VAL B 1 238 ? -12.723 -15.722 -49.475 1.00 69.92  ? 238  VAL B CG2 1 
ATOM   4856 N N   . THR B 1 239 ? -15.646 -15.035 -45.854 1.00 74.47  ? 239  THR B N   1 
ATOM   4857 C CA  . THR B 1 239 ? -16.899 -14.790 -45.129 1.00 74.82  ? 239  THR B CA  1 
ATOM   4858 C C   . THR B 1 239 ? -17.291 -13.314 -45.237 1.00 75.48  ? 239  THR B C   1 
ATOM   4859 O O   . THR B 1 239 ? -16.462 -12.436 -44.981 1.00 73.82  ? 239  THR B O   1 
ATOM   4860 C CB  . THR B 1 239 ? -16.762 -15.274 -43.669 1.00 92.22  ? 239  THR B CB  1 
ATOM   4861 O OG1 . THR B 1 239 ? -16.388 -16.651 -43.686 1.00 99.59  ? 239  THR B OG1 1 
ATOM   4862 C CG2 . THR B 1 239 ? -18.040 -15.118 -42.859 1.00 91.71  ? 239  THR B CG2 1 
ATOM   4863 N N   . PHE B 1 240 ? -18.554 -13.050 -45.620 1.00 71.31  ? 240  PHE B N   1 
ATOM   4864 C CA  . PHE B 1 240 ? -19.087 -11.696 -45.691 1.00 71.27  ? 240  PHE B CA  1 
ATOM   4865 C C   . PHE B 1 240 ? -20.011 -11.485 -44.485 1.00 81.74  ? 240  PHE B C   1 
ATOM   4866 O O   . PHE B 1 240 ? -20.911 -12.302 -44.247 1.00 81.56  ? 240  PHE B O   1 
ATOM   4867 C CB  . PHE B 1 240 ? -19.803 -11.466 -47.024 1.00 71.63  ? 240  PHE B CB  1 
ATOM   4868 C CG  . PHE B 1 240 ? -18.883 -11.425 -48.226 1.00 71.46  ? 240  PHE B CG  1 
ATOM   4869 C CD1 . PHE B 1 240 ? -18.569 -12.582 -48.927 1.00 72.58  ? 240  PHE B CD1 1 
ATOM   4870 C CD2 . PHE B 1 240 ? -18.330 -10.235 -48.656 1.00 72.48  ? 240  PHE B CD2 1 
ATOM   4871 C CE1 . PHE B 1 240 ? -17.714 -12.544 -50.037 1.00 72.54  ? 240  PHE B CE1 1 
ATOM   4872 C CE2 . PHE B 1 240 ? -17.484 -10.199 -49.776 1.00 74.46  ? 240  PHE B CE2 1 
ATOM   4873 C CZ  . PHE B 1 240 ? -17.183 -11.351 -50.459 1.00 71.74  ? 240  PHE B CZ  1 
ATOM   4874 N N   . LYS B 1 241 ? -19.720 -10.446 -43.662 1.00 83.07  ? 241  LYS B N   1 
ATOM   4875 C CA  . LYS B 1 241 ? -20.464 -10.154 -42.433 1.00 85.29  ? 241  LYS B CA  1 
ATOM   4876 C C   . LYS B 1 241 ? -21.253 -8.858  -42.473 1.00 92.62  ? 241  LYS B C   1 
ATOM   4877 O O   . LYS B 1 241 ? -20.689 -7.768  -42.607 1.00 91.96  ? 241  LYS B O   1 
ATOM   4878 C CB  . LYS B 1 241 ? -19.568 -10.169 -41.177 1.00 88.72  ? 241  LYS B CB  1 
ATOM   4879 C CG  . LYS B 1 241 ? -18.929 -11.487 -40.839 1.00 101.82 ? 241  LYS B CG  1 
ATOM   4880 C CD  . LYS B 1 241 ? -17.932 -11.315 -39.689 1.00 111.37 ? 241  LYS B CD  1 
ATOM   4881 C CE  . LYS B 1 241 ? -17.479 -12.660 -39.194 1.00 124.05 ? 241  LYS B CE  1 
ATOM   4882 N NZ  . LYS B 1 241 ? -16.518 -12.546 -38.066 1.00 132.24 ? 241  LYS B NZ  1 
ATOM   4883 N N   . ASN B 1 242 ? -22.577 -8.990  -42.319 1.00 92.27  ? 242  ASN B N   1 
ATOM   4884 C CA  . ASN B 1 242 ? -23.521 -7.884  -42.297 1.00 94.00  ? 242  ASN B CA  1 
ATOM   4885 C C   . ASN B 1 242 ? -24.596 -8.211  -41.239 1.00 101.31 ? 242  ASN B C   1 
ATOM   4886 O O   . ASN B 1 242 ? -25.698 -8.660  -41.589 1.00 101.64 ? 242  ASN B O   1 
ATOM   4887 C CB  . ASN B 1 242 ? -24.123 -7.666  -43.695 1.00 94.76  ? 242  ASN B CB  1 
ATOM   4888 C CG  . ASN B 1 242 ? -24.958 -6.422  -43.815 1.00 99.68  ? 242  ASN B CG  1 
ATOM   4889 O OD1 . ASN B 1 242 ? -25.032 -5.591  -42.902 1.00 93.50  ? 242  ASN B OD1 1 
ATOM   4890 N ND2 . ASN B 1 242 ? -25.584 -6.260  -44.966 1.00 82.07  ? 242  ASN B ND2 1 
ATOM   4891 N N   . PRO B 1 243 ? -24.279 -8.021  -39.932 1.00 98.70  ? 243  PRO B N   1 
ATOM   4892 C CA  . PRO B 1 243 ? -25.241 -8.421  -38.889 1.00 98.72  ? 243  PRO B CA  1 
ATOM   4893 C C   . PRO B 1 243 ? -26.350 -7.432  -38.560 1.00 104.01 ? 243  PRO B C   1 
ATOM   4894 O O   . PRO B 1 243 ? -27.370 -7.838  -37.999 1.00 103.47 ? 243  PRO B O   1 
ATOM   4895 C CB  . PRO B 1 243 ? -24.351 -8.670  -37.672 1.00 100.32 ? 243  PRO B CB  1 
ATOM   4896 C CG  . PRO B 1 243 ? -23.183 -7.747  -37.863 1.00 104.77 ? 243  PRO B CG  1 
ATOM   4897 C CD  . PRO B 1 243 ? -23.007 -7.536  -39.345 1.00 100.28 ? 243  PRO B CD  1 
ATOM   4898 N N   . HIS B 1 244 ? -26.140 -6.139  -38.845 1.00 101.43 ? 244  HIS B N   1 
ATOM   4899 C CA  . HIS B 1 244 ? -27.124 -5.122  -38.473 1.00 101.01 ? 244  HIS B CA  1 
ATOM   4900 C C   . HIS B 1 244 ? -27.644 -4.301  -39.658 1.00 101.37 ? 244  HIS B C   1 
ATOM   4901 O O   . HIS B 1 244 ? -28.324 -3.293  -39.450 1.00 100.75 ? 244  HIS B O   1 
ATOM   4902 C CB  . HIS B 1 244 ? -26.552 -4.211  -37.361 1.00 102.08 ? 244  HIS B CB  1 
ATOM   4903 C CG  . HIS B 1 244 ? -25.966 -4.951  -36.197 1.00 105.87 ? 244  HIS B CG  1 
ATOM   4904 N ND1 . HIS B 1 244 ? -26.723 -5.845  -35.451 1.00 107.85 ? 244  HIS B ND1 1 
ATOM   4905 C CD2 . HIS B 1 244 ? -24.716 -4.894  -35.678 1.00 108.02 ? 244  HIS B CD2 1 
ATOM   4906 C CE1 . HIS B 1 244 ? -25.910 -6.298  -34.508 1.00 107.55 ? 244  HIS B CE1 1 
ATOM   4907 N NE2 . HIS B 1 244 ? -24.692 -5.753  -34.603 1.00 107.87 ? 244  HIS B NE2 1 
ATOM   4908 N N   . ALA B 1 245 ? -27.357 -4.755  -40.898 1.00 94.57  ? 245  ALA B N   1 
ATOM   4909 C CA  . ALA B 1 245 ? -27.715 -4.081  -42.143 1.00 92.66  ? 245  ALA B CA  1 
ATOM   4910 C C   . ALA B 1 245 ? -27.135 -2.650  -42.172 1.00 94.96  ? 245  ALA B C   1 
ATOM   4911 O O   . ALA B 1 245 ? -27.705 -1.768  -42.782 1.00 93.91  ? 245  ALA B O   1 
ATOM   4912 C CB  . ALA B 1 245 ? -29.225 -4.101  -42.368 1.00 92.87  ? 245  ALA B CB  1 
ATOM   4913 N N   . LYS B 1 246 ? -25.978 -2.438  -41.515 1.00 91.75  ? 246  LYS B N   1 
ATOM   4914 C CA  . LYS B 1 246 ? -25.292 -1.141  -41.447 1.00 91.86  ? 246  LYS B CA  1 
ATOM   4915 C C   . LYS B 1 246 ? -24.067 -1.117  -42.375 1.00 97.05  ? 246  LYS B C   1 
ATOM   4916 O O   . LYS B 1 246 ? -23.735 -0.065  -42.938 1.00 97.95  ? 246  LYS B O   1 
ATOM   4917 C CB  . LYS B 1 246 ? -24.886 -0.801  -39.992 1.00 93.92  ? 246  LYS B CB  1 
ATOM   4918 C CG  . LYS B 1 246 ? -26.071 -0.781  -39.005 1.00 107.67 ? 246  LYS B CG  1 
ATOM   4919 C CD  . LYS B 1 246 ? -25.681 -0.385  -37.579 1.00 116.49 ? 246  LYS B CD  1 
ATOM   4920 C CE  . LYS B 1 246 ? -26.862 -0.361  -36.629 1.00 122.77 ? 246  LYS B CE  1 
ATOM   4921 N NZ  . LYS B 1 246 ? -26.492 0.176   -35.287 1.00 131.90 ? 246  LYS B NZ  1 
ATOM   4922 N N   . LYS B 1 247 ? -23.412 -2.290  -42.549 1.00 92.15  ? 247  LYS B N   1 
ATOM   4923 C CA  . LYS B 1 247 ? -22.207 -2.464  -43.365 1.00 90.66  ? 247  LYS B CA  1 
ATOM   4924 C C   . LYS B 1 247 ? -21.899 -3.944  -43.658 1.00 92.58  ? 247  LYS B C   1 
ATOM   4925 O O   . LYS B 1 247 ? -22.261 -4.819  -42.879 1.00 89.96  ? 247  LYS B O   1 
ATOM   4926 C CB  . LYS B 1 247 ? -20.973 -1.772  -42.696 1.00 92.03  ? 247  LYS B CB  1 
ATOM   4927 C CG  . LYS B 1 247 ? -20.895 -1.896  -41.169 1.00 96.70  ? 247  LYS B CG  1 
ATOM   4928 C CD  . LYS B 1 247 ? -19.487 -2.089  -40.622 1.00 106.01 ? 247  LYS B CD  1 
ATOM   4929 C CE  . LYS B 1 247 ? -19.542 -2.808  -39.284 1.00 121.21 ? 247  LYS B CE  1 
ATOM   4930 N NZ  . LYS B 1 247 ? -18.223 -3.363  -38.868 1.00 128.66 ? 247  LYS B NZ  1 
ATOM   4931 N N   . GLN B 1 248 ? -21.209 -4.211  -44.790 1.00 90.31  ? 248  GLN B N   1 
ATOM   4932 C CA  . GLN B 1 248 ? -20.733 -5.542  -45.190 1.00 89.93  ? 248  GLN B CA  1 
ATOM   4933 C C   . GLN B 1 248 ? -19.204 -5.615  -45.051 1.00 96.47  ? 248  GLN B C   1 
ATOM   4934 O O   . GLN B 1 248 ? -18.470 -4.832  -45.671 1.00 96.00  ? 248  GLN B O   1 
ATOM   4935 C CB  . GLN B 1 248 ? -21.167 -5.926  -46.609 1.00 90.35  ? 248  GLN B CB  1 
ATOM   4936 C CG  . GLN B 1 248 ? -21.010 -7.418  -46.852 1.00 87.89  ? 248  GLN B CG  1 
ATOM   4937 C CD  . GLN B 1 248 ? -21.803 -7.950  -48.025 1.00 92.30  ? 248  GLN B CD  1 
ATOM   4938 O OE1 . GLN B 1 248 ? -22.589 -8.902  -47.883 1.00 79.58  ? 248  GLN B OE1 1 
ATOM   4939 N NE2 . GLN B 1 248 ? -21.558 -7.413  -49.222 1.00 77.10  ? 248  GLN B NE2 1 
ATOM   4940 N N   . ASP B 1 249 ? -18.738 -6.559  -44.213 1.00 95.02  ? 249  ASP B N   1 
ATOM   4941 C CA  . ASP B 1 249 ? -17.314 -6.806  -43.941 1.00 94.88  ? 249  ASP B CA  1 
ATOM   4942 C C   . ASP B 1 249 ? -16.827 -8.124  -44.512 1.00 95.48  ? 249  ASP B C   1 
ATOM   4943 O O   . ASP B 1 249 ? -17.537 -9.118  -44.428 1.00 93.97  ? 249  ASP B O   1 
ATOM   4944 C CB  . ASP B 1 249 ? -17.031 -6.705  -42.437 1.00 97.49  ? 249  ASP B CB  1 
ATOM   4945 C CG  . ASP B 1 249 ? -16.941 -5.267  -41.974 1.00 112.94 ? 249  ASP B CG  1 
ATOM   4946 O OD1 . ASP B 1 249 ? -17.915 -4.513  -42.193 1.00 113.94 ? 249  ASP B OD1 1 
ATOM   4947 O OD2 . ASP B 1 249 ? -15.877 -4.884  -41.425 1.00 120.14 ? 249  ASP B OD2 1 
ATOM   4948 N N   . VAL B 1 250 ? -15.631 -8.126  -45.116 1.00 90.51  ? 250  VAL B N   1 
ATOM   4949 C CA  . VAL B 1 250 ? -15.081 -9.337  -45.722 1.00 89.73  ? 250  VAL B CA  1 
ATOM   4950 C C   . VAL B 1 250 ? -13.912 -9.914  -44.863 1.00 93.99  ? 250  VAL B C   1 
ATOM   4951 O O   . VAL B 1 250 ? -12.901 -9.237  -44.610 1.00 92.64  ? 250  VAL B O   1 
ATOM   4952 C CB  . VAL B 1 250 ? -14.736 -9.114  -47.218 1.00 92.48  ? 250  VAL B CB  1 
ATOM   4953 C CG1 . VAL B 1 250 ? -13.585 -8.131  -47.413 1.00 91.99  ? 250  VAL B CG1 1 
ATOM   4954 C CG2 . VAL B 1 250 ? -14.484 -10.422 -47.942 1.00 91.91  ? 250  VAL B CG2 1 
ATOM   4955 N N   . VAL B 1 251 ? -14.073 -11.180 -44.424 1.00 90.71  ? 251  VAL B N   1 
ATOM   4956 C CA  . VAL B 1 251 ? -13.105 -11.849 -43.541 1.00 89.97  ? 251  VAL B CA  1 
ATOM   4957 C C   . VAL B 1 251 ? -12.560 -13.242 -44.061 1.00 90.05  ? 251  VAL B C   1 
ATOM   4958 O O   . VAL B 1 251 ? -13.319 -14.129 -44.480 1.00 88.54  ? 251  VAL B O   1 
ATOM   4959 C CB  . VAL B 1 251 ? -13.698 -11.944 -42.107 1.00 94.13  ? 251  VAL B CB  1 
ATOM   4960 C CG1 . VAL B 1 251 ? -15.038 -12.680 -42.067 1.00 94.08  ? 251  VAL B CG1 1 
ATOM   4961 C CG2 . VAL B 1 251 ? -12.701 -12.476 -41.076 1.00 93.88  ? 251  VAL B CG2 1 
ATOM   4962 N N   . VAL B 1 252 ? -11.214 -13.403 -43.969 1.00 84.72  ? 252  VAL B N   1 
ATOM   4963 C CA  . VAL B 1 252 ? -10.457 -14.624 -44.288 1.00 83.79  ? 252  VAL B CA  1 
ATOM   4964 C C   . VAL B 1 252 ? -10.723 -15.642 -43.166 1.00 84.71  ? 252  VAL B C   1 
ATOM   4965 O O   . VAL B 1 252 ? -10.870 -15.237 -42.014 1.00 84.26  ? 252  VAL B O   1 
ATOM   4966 C CB  . VAL B 1 252 ? -8.948  -14.365 -44.440 1.00 87.97  ? 252  VAL B CB  1 
ATOM   4967 C CG1 . VAL B 1 252 ? -8.322  -15.427 -45.336 1.00 87.90  ? 252  VAL B CG1 1 
ATOM   4968 C CG2 . VAL B 1 252 ? -8.662  -12.955 -44.984 1.00 87.77  ? 252  VAL B CG2 1 
ATOM   4969 N N   . LEU B 1 253 ? -10.784 -16.941 -43.487 1.00 78.62  ? 253  LEU B N   1 
ATOM   4970 C CA  . LEU B 1 253 ? -11.163 -17.935 -42.502 1.00 76.91  ? 253  LEU B CA  1 
ATOM   4971 C C   . LEU B 1 253 ? -10.023 -18.557 -41.687 1.00 80.20  ? 253  LEU B C   1 
ATOM   4972 O O   . LEU B 1 253 ? -10.304 -19.397 -40.831 1.00 81.52  ? 253  LEU B O   1 
ATOM   4973 C CB  . LEU B 1 253 ? -12.017 -19.022 -43.141 1.00 76.48  ? 253  LEU B CB  1 
ATOM   4974 C CG  . LEU B 1 253 ? -13.378 -19.279 -42.502 1.00 80.63  ? 253  LEU B CG  1 
ATOM   4975 C CD1 . LEU B 1 253 ? -13.923 -18.037 -41.800 1.00 83.09  ? 253  LEU B CD1 1 
ATOM   4976 C CD2 . LEU B 1 253 ? -14.387 -19.732 -43.547 1.00 80.10  ? 253  LEU B CD2 1 
ATOM   4977 N N   . GLY B 1 254 ? -8.778  -18.126 -41.882 1.00 73.34  ? 254  GLY B N   1 
ATOM   4978 C CA  . GLY B 1 254 ? -7.668  -18.643 -41.078 1.00 70.61  ? 254  GLY B CA  1 
ATOM   4979 C C   . GLY B 1 254 ? -7.128  -19.969 -41.556 1.00 68.51  ? 254  GLY B C   1 
ATOM   4980 O O   . GLY B 1 254 ? -7.900  -20.836 -41.972 1.00 68.98  ? 254  GLY B O   1 
ATOM   4981 N N   . SER B 1 255 ? -5.798  -20.137 -41.495 1.00 60.40  ? 255  SER B N   1 
ATOM   4982 C CA  . SER B 1 255 ? -5.095  -21.306 -41.998 1.00 58.40  ? 255  SER B CA  1 
ATOM   4983 C C   . SER B 1 255 ? -5.707  -22.596 -41.582 1.00 62.73  ? 255  SER B C   1 
ATOM   4984 O O   . SER B 1 255 ? -6.063  -22.783 -40.416 1.00 62.14  ? 255  SER B O   1 
ATOM   4985 C CB  . SER B 1 255 ? -3.625  -21.267 -41.634 1.00 60.30  ? 255  SER B CB  1 
ATOM   4986 O OG  . SER B 1 255 ? -2.937  -22.261 -42.372 1.00 68.49  ? 255  SER B OG  1 
ATOM   4987 N N   . GLN B 1 256 ? -5.870  -23.476 -42.575 1.00 59.72  ? 256  GLN B N   1 
ATOM   4988 C CA  . GLN B 1 256 ? -6.472  -24.808 -42.466 1.00 58.03  ? 256  GLN B CA  1 
ATOM   4989 C C   . GLN B 1 256 ? -5.410  -25.920 -42.413 1.00 58.81  ? 256  GLN B C   1 
ATOM   4990 O O   . GLN B 1 256 ? -5.749  -27.100 -42.523 1.00 58.58  ? 256  GLN B O   1 
ATOM   4991 C CB  . GLN B 1 256 ? -7.424  -25.009 -43.654 1.00 58.62  ? 256  GLN B CB  1 
ATOM   4992 C CG  . GLN B 1 256 ? -8.648  -24.102 -43.599 1.00 52.59  ? 256  GLN B CG  1 
ATOM   4993 C CD  . GLN B 1 256 ? -9.482  -24.257 -42.343 1.00 67.45  ? 256  GLN B CD  1 
ATOM   4994 O OE1 . GLN B 1 256 ? -9.697  -23.299 -41.603 1.00 66.42  ? 256  GLN B OE1 1 
ATOM   4995 N NE2 . GLN B 1 256 ? -9.993  -25.458 -42.083 1.00 52.10  ? 256  GLN B NE2 1 
ATOM   4996 N N   . GLU B 1 257 ? -4.134  -25.539 -42.237 1.00 52.33  ? 257  GLU B N   1 
ATOM   4997 C CA  . GLU B 1 257 ? -3.001  -26.456 -42.197 1.00 50.25  ? 257  GLU B CA  1 
ATOM   4998 C C   . GLU B 1 257 ? -3.132  -27.498 -41.091 1.00 51.93  ? 257  GLU B C   1 
ATOM   4999 O O   . GLU B 1 257 ? -3.152  -28.695 -41.395 1.00 51.70  ? 257  GLU B O   1 
ATOM   5000 C CB  . GLU B 1 257 ? -1.694  -25.673 -42.081 1.00 51.20  ? 257  GLU B CB  1 
ATOM   5001 C CG  . GLU B 1 257 ? -0.468  -26.529 -42.249 1.00 62.83  ? 257  GLU B CG  1 
ATOM   5002 C CD  . GLU B 1 257 ? 0.824   -25.757 -42.136 1.00 101.59 ? 257  GLU B CD  1 
ATOM   5003 O OE1 . GLU B 1 257 ? 0.852   -24.732 -41.414 1.00 98.59  ? 257  GLU B OE1 1 
ATOM   5004 O OE2 . GLU B 1 257 ? 1.806   -26.164 -42.799 1.00 109.86 ? 257  GLU B OE2 1 
ATOM   5005 N N   . GLY B 1 258 ? -3.249  -27.033 -39.846 1.00 46.92  ? 258  GLY B N   1 
ATOM   5006 C CA  . GLY B 1 258 ? -3.389  -27.864 -38.660 1.00 46.35  ? 258  GLY B CA  1 
ATOM   5007 C C   . GLY B 1 258 ? -4.709  -28.588 -38.641 1.00 49.58  ? 258  GLY B C   1 
ATOM   5008 O O   . GLY B 1 258 ? -4.793  -29.740 -38.206 1.00 49.05  ? 258  GLY B O   1 
ATOM   5009 N N   . ALA B 1 259 ? -5.735  -27.914 -39.139 1.00 47.28  ? 259  ALA B N   1 
ATOM   5010 C CA  . ALA B 1 259 ? -7.085  -28.453 -39.253 1.00 48.50  ? 259  ALA B CA  1 
ATOM   5011 C C   . ALA B 1 259 ? -7.032  -29.733 -40.111 1.00 53.08  ? 259  ALA B C   1 
ATOM   5012 O O   . ALA B 1 259 ? -7.526  -30.791 -39.679 1.00 52.59  ? 259  ALA B O   1 
ATOM   5013 C CB  . ALA B 1 259 ? -7.982  -27.420 -39.902 1.00 49.70  ? 259  ALA B CB  1 
ATOM   5014 N N   . MET B 1 260 ? -6.354  -29.633 -41.294 1.00 48.39  ? 260  MET B N   1 
ATOM   5015 C CA  . MET B 1 260 ? -6.109  -30.718 -42.229 1.00 47.13  ? 260  MET B CA  1 
ATOM   5016 C C   . MET B 1 260 ? -5.350  -31.857 -41.556 1.00 53.81  ? 260  MET B C   1 
ATOM   5017 O O   . MET B 1 260 ? -5.829  -32.983 -41.660 1.00 53.83  ? 260  MET B O   1 
ATOM   5018 C CB  . MET B 1 260 ? -5.336  -30.229 -43.453 1.00 48.67  ? 260  MET B CB  1 
ATOM   5019 C CG  . MET B 1 260 ? -6.204  -29.792 -44.602 1.00 52.02  ? 260  MET B CG  1 
ATOM   5020 S SD  . MET B 1 260 ? -7.544  -30.921 -45.101 1.00 56.44  ? 260  MET B SD  1 
ATOM   5021 C CE  . MET B 1 260 ? -6.626  -32.255 -45.864 1.00 53.65  ? 260  MET B CE  1 
ATOM   5022 N N   . HIS B 1 261 ? -4.204  -31.576 -40.830 1.00 50.20  ? 261  HIS B N   1 
ATOM   5023 C CA  . HIS B 1 261 ? -3.416  -32.599 -40.117 1.00 49.78  ? 261  HIS B CA  1 
ATOM   5024 C C   . HIS B 1 261 ? -4.279  -33.414 -39.174 1.00 53.90  ? 261  HIS B C   1 
ATOM   5025 O O   . HIS B 1 261 ? -4.161  -34.637 -39.161 1.00 55.58  ? 261  HIS B O   1 
ATOM   5026 C CB  . HIS B 1 261 ? -2.237  -32.006 -39.336 1.00 50.94  ? 261  HIS B CB  1 
ATOM   5027 C CG  . HIS B 1 261 ? -1.197  -31.299 -40.154 1.00 55.08  ? 261  HIS B CG  1 
ATOM   5028 N ND1 . HIS B 1 261 ? -0.394  -30.319 -39.593 1.00 57.36  ? 261  HIS B ND1 1 
ATOM   5029 C CD2 . HIS B 1 261 ? -0.844  -31.458 -41.456 1.00 57.76  ? 261  HIS B CD2 1 
ATOM   5030 C CE1 . HIS B 1 261 ? 0.406   -29.900 -40.568 1.00 57.56  ? 261  HIS B CE1 1 
ATOM   5031 N NE2 . HIS B 1 261 ? 0.179   -30.560 -41.710 1.00 57.75  ? 261  HIS B NE2 1 
ATOM   5032 N N   . THR B 1 262 ? -5.176  -32.748 -38.422 1.00 49.04  ? 262  THR B N   1 
ATOM   5033 C CA  . THR B 1 262 ? -6.098  -33.396 -37.488 1.00 48.99  ? 262  THR B CA  1 
ATOM   5034 C C   . THR B 1 262 ? -7.077  -34.294 -38.228 1.00 56.34  ? 262  THR B C   1 
ATOM   5035 O O   . THR B 1 262 ? -7.354  -35.402 -37.771 1.00 56.69  ? 262  THR B O   1 
ATOM   5036 C CB  . THR B 1 262 ? -6.830  -32.340 -36.667 1.00 53.42  ? 262  THR B CB  1 
ATOM   5037 O OG1 . THR B 1 262 ? -5.868  -31.535 -35.995 1.00 59.37  ? 262  THR B OG1 1 
ATOM   5038 C CG2 . THR B 1 262 ? -7.811  -32.941 -35.670 1.00 46.80  ? 262  THR B CG2 1 
ATOM   5039 N N   . ALA B 1 263 ? -7.611  -33.808 -39.372 1.00 54.47  ? 263  ALA B N   1 
ATOM   5040 C CA  . ALA B 1 263 ? -8.560  -34.557 -40.200 1.00 54.33  ? 263  ALA B CA  1 
ATOM   5041 C C   . ALA B 1 263 ? -7.901  -35.802 -40.782 1.00 58.69  ? 263  ALA B C   1 
ATOM   5042 O O   . ALA B 1 263 ? -8.566  -36.811 -40.961 1.00 60.41  ? 263  ALA B O   1 
ATOM   5043 C CB  . ALA B 1 263 ? -9.057  -33.671 -41.327 1.00 55.04  ? 263  ALA B CB  1 
ATOM   5044 N N   . LEU B 1 264 ? -6.588  -35.717 -41.063 1.00 52.26  ? 264  LEU B N   1 
ATOM   5045 C CA  . LEU B 1 264 ? -5.791  -36.760 -41.672 1.00 50.48  ? 264  LEU B CA  1 
ATOM   5046 C C   . LEU B 1 264 ? -5.206  -37.711 -40.632 1.00 54.58  ? 264  LEU B C   1 
ATOM   5047 O O   . LEU B 1 264 ? -4.269  -38.457 -40.971 1.00 54.15  ? 264  LEU B O   1 
ATOM   5048 C CB  . LEU B 1 264 ? -4.642  -36.094 -42.456 1.00 49.68  ? 264  LEU B CB  1 
ATOM   5049 C CG  . LEU B 1 264 ? -4.970  -35.279 -43.682 1.00 51.65  ? 264  LEU B CG  1 
ATOM   5050 C CD1 . LEU B 1 264 ? -3.808  -34.340 -44.026 1.00 50.26  ? 264  LEU B CD1 1 
ATOM   5051 C CD2 . LEU B 1 264 ? -5.349  -36.175 -44.836 1.00 52.35  ? 264  LEU B CD2 1 
ATOM   5052 N N   . THR B 1 265 ? -5.736  -37.711 -39.385 1.00 51.00  ? 265  THR B N   1 
ATOM   5053 C CA  . THR B 1 265 ? -5.149  -38.576 -38.358 1.00 52.08  ? 265  THR B CA  1 
ATOM   5054 C C   . THR B 1 265 ? -5.376  -40.068 -38.660 1.00 58.01  ? 265  THR B C   1 
ATOM   5055 O O   . THR B 1 265 ? -4.379  -40.809 -38.788 1.00 58.61  ? 265  THR B O   1 
ATOM   5056 C CB  . THR B 1 265 ? -5.510  -38.177 -36.955 1.00 64.13  ? 265  THR B CB  1 
ATOM   5057 O OG1 . THR B 1 265 ? -6.909  -37.910 -36.858 1.00 75.65  ? 265  THR B OG1 1 
ATOM   5058 C CG2 . THR B 1 265 ? -4.670  -36.996 -36.474 1.00 58.39  ? 265  THR B CG2 1 
ATOM   5059 N N   . GLY B 1 266 ? -6.623  -40.475 -38.884 1.00 54.33  ? 266  GLY B N   1 
ATOM   5060 C CA  . GLY B 1 266 ? -6.890  -41.877 -39.222 1.00 54.54  ? 266  GLY B CA  1 
ATOM   5061 C C   . GLY B 1 266 ? -6.265  -42.426 -40.509 1.00 57.69  ? 266  GLY B C   1 
ATOM   5062 O O   . GLY B 1 266 ? -6.131  -43.643 -40.665 1.00 55.86  ? 266  GLY B O   1 
ATOM   5063 N N   . ALA B 1 267 ? -5.867  -41.528 -41.431 1.00 55.63  ? 267  ALA B N   1 
ATOM   5064 C CA  . ALA B 1 267 ? -5.327  -41.821 -42.761 1.00 56.54  ? 267  ALA B CA  1 
ATOM   5065 C C   . ALA B 1 267 ? -3.947  -42.449 -42.799 1.00 59.36  ? 267  ALA B C   1 
ATOM   5066 O O   . ALA B 1 267 ? -3.155  -42.281 -41.857 1.00 60.53  ? 267  ALA B O   1 
ATOM   5067 C CB  . ALA B 1 267 ? -5.317  -40.559 -43.598 1.00 57.92  ? 267  ALA B CB  1 
ATOM   5068 N N   . THR B 1 268 ? -3.643  -43.107 -43.945 1.00 52.24  ? 268  THR B N   1 
ATOM   5069 C CA  . THR B 1 268 ? -2.374  -43.775 -44.229 1.00 51.20  ? 268  THR B CA  1 
ATOM   5070 C C   . THR B 1 268 ? -1.282  -42.764 -44.491 1.00 57.59  ? 268  THR B C   1 
ATOM   5071 O O   . THR B 1 268 ? -1.176  -42.236 -45.595 1.00 57.23  ? 268  THR B O   1 
ATOM   5072 C CB  . THR B 1 268 ? -2.538  -44.746 -45.398 1.00 48.38  ? 268  THR B CB  1 
ATOM   5073 O OG1 . THR B 1 268 ? -3.636  -45.625 -45.140 1.00 55.04  ? 268  THR B OG1 1 
ATOM   5074 C CG2 . THR B 1 268 ? -1.296  -45.538 -45.680 1.00 35.67  ? 268  THR B CG2 1 
ATOM   5075 N N   . GLU B 1 269 ? -0.465  -42.495 -43.477 1.00 57.08  ? 269  GLU B N   1 
ATOM   5076 C CA  . GLU B 1 269 ? 0.643   -41.552 -43.580 1.00 58.07  ? 269  GLU B CA  1 
ATOM   5077 C C   . GLU B 1 269 ? 1.786   -42.126 -44.411 1.00 63.51  ? 269  GLU B C   1 
ATOM   5078 O O   . GLU B 1 269 ? 2.028   -43.328 -44.395 1.00 62.37  ? 269  GLU B O   1 
ATOM   5079 C CB  . GLU B 1 269 ? 1.127   -41.155 -42.181 1.00 59.98  ? 269  GLU B CB  1 
ATOM   5080 C CG  . GLU B 1 269 ? 1.791   -39.786 -42.131 1.00 80.04  ? 269  GLU B CG  1 
ATOM   5081 C CD  . GLU B 1 269 ? 2.172   -39.227 -40.765 1.00 109.45 ? 269  GLU B CD  1 
ATOM   5082 O OE1 . GLU B 1 269 ? 2.150   -39.985 -39.764 1.00 98.48  ? 269  GLU B OE1 1 
ATOM   5083 O OE2 . GLU B 1 269 ? 2.522   -38.023 -40.705 1.00 99.48  ? 269  GLU B OE2 1 
ATOM   5084 N N   . ILE B 1 270 ? 2.432   -41.276 -45.194 1.00 63.53  ? 270  ILE B N   1 
ATOM   5085 C CA  . ILE B 1 270 ? 3.600   -41.604 -46.022 1.00 65.02  ? 270  ILE B CA  1 
ATOM   5086 C C   . ILE B 1 270 ? 4.725   -40.683 -45.581 1.00 79.23  ? 270  ILE B C   1 
ATOM   5087 O O   . ILE B 1 270 ? 4.490   -39.501 -45.312 1.00 78.98  ? 270  ILE B O   1 
ATOM   5088 C CB  . ILE B 1 270 ? 3.319   -41.560 -47.565 1.00 65.61  ? 270  ILE B CB  1 
ATOM   5089 C CG1 . ILE B 1 270 ? 3.024   -42.956 -48.126 1.00 63.72  ? 270  ILE B CG1 1 
ATOM   5090 C CG2 . ILE B 1 270 ? 4.452   -40.894 -48.367 1.00 64.06  ? 270  ILE B CG2 1 
ATOM   5091 C CD1 . ILE B 1 270 ? 1.715   -43.497 -47.827 1.00 64.07  ? 270  ILE B CD1 1 
ATOM   5092 N N   . GLN B 1 271 ? 5.922   -41.225 -45.440 1.00 83.96  ? 271  GLN B N   1 
ATOM   5093 C CA  . GLN B 1 271 ? 7.019   -40.374 -45.024 1.00 88.54  ? 271  GLN B CA  1 
ATOM   5094 C C   . GLN B 1 271 ? 7.779   -39.789 -46.219 1.00 103.15 ? 271  GLN B C   1 
ATOM   5095 O O   . GLN B 1 271 ? 7.725   -40.328 -47.336 1.00 103.24 ? 271  GLN B O   1 
ATOM   5096 C CB  . GLN B 1 271 ? 7.947   -41.109 -44.045 1.00 90.08  ? 271  GLN B CB  1 
ATOM   5097 C CG  . GLN B 1 271 ? 8.010   -40.456 -42.663 1.00 105.56 ? 271  GLN B CG  1 
ATOM   5098 C CD  . GLN B 1 271 ? 6.776   -40.680 -41.810 1.00 117.89 ? 271  GLN B CD  1 
ATOM   5099 O OE1 . GLN B 1 271 ? 5.993   -41.626 -42.006 1.00 107.08 ? 271  GLN B OE1 1 
ATOM   5100 N NE2 . GLN B 1 271 ? 6.598   -39.819 -40.818 1.00 109.96 ? 271  GLN B NE2 1 
ATOM   5101 N N   . MET B 1 272 ? 8.434   -38.643 -45.984 1.00 106.73 ? 272  MET B N   1 
ATOM   5102 C CA  . MET B 1 272 ? 9.292   -37.952 -46.941 1.00 110.15 ? 272  MET B CA  1 
ATOM   5103 C C   . MET B 1 272 ? 10.491  -37.499 -46.109 1.00 118.70 ? 272  MET B C   1 
ATOM   5104 O O   . MET B 1 272 ? 10.557  -36.344 -45.665 1.00 119.37 ? 272  MET B O   1 
ATOM   5105 C CB  . MET B 1 272 ? 8.567   -36.803 -47.694 1.00 113.50 ? 272  MET B CB  1 
ATOM   5106 C CG  . MET B 1 272 ? 7.459   -37.293 -48.644 1.00 118.80 ? 272  MET B CG  1 
ATOM   5107 S SD  . MET B 1 272 ? 7.016   -36.224 -50.056 1.00 124.69 ? 272  MET B SD  1 
ATOM   5108 C CE  . MET B 1 272 ? 6.058   -34.893 -49.216 1.00 121.37 ? 272  MET B CE  1 
ATOM   5109 N N   . SER B 1 273 ? 11.381  -38.479 -45.800 1.00 116.94 ? 273  SER B N   1 
ATOM   5110 C CA  . SER B 1 273 ? 12.581  -38.338 -44.954 1.00 117.18 ? 273  SER B CA  1 
ATOM   5111 C C   . SER B 1 273 ? 13.566  -37.294 -45.471 1.00 121.57 ? 273  SER B C   1 
ATOM   5112 O O   . SER B 1 273 ? 14.160  -36.557 -44.679 1.00 121.34 ? 273  SER B O   1 
ATOM   5113 C CB  . SER B 1 273 ? 13.267  -39.687 -44.762 1.00 120.50 ? 273  SER B CB  1 
ATOM   5114 O OG  . SER B 1 273 ? 13.674  -40.224 -46.009 1.00 129.46 ? 273  SER B OG  1 
ATOM   5115 N N   . SER B 1 274 ? 13.729  -37.245 -46.800 1.00 118.25 ? 274  SER B N   1 
ATOM   5116 C CA  . SER B 1 274 ? 14.562  -36.287 -47.518 1.00 118.44 ? 274  SER B CA  1 
ATOM   5117 C C   . SER B 1 274 ? 13.953  -36.109 -48.917 1.00 121.60 ? 274  SER B C   1 
ATOM   5118 O O   . SER B 1 274 ? 14.510  -36.543 -49.939 1.00 120.78 ? 274  SER B O   1 
ATOM   5119 C CB  . SER B 1 274 ? 16.032  -36.711 -47.540 1.00 123.43 ? 274  SER B CB  1 
ATOM   5120 O OG  . SER B 1 274 ? 16.207  -38.063 -47.932 1.00 136.95 ? 274  SER B OG  1 
ATOM   5121 N N   . GLY B 1 275 ? 12.747  -35.534 -48.905 1.00 117.16 ? 275  GLY B N   1 
ATOM   5122 C CA  . GLY B 1 275 ? 11.943  -35.236 -50.085 1.00 116.06 ? 275  GLY B CA  1 
ATOM   5123 C C   . GLY B 1 275 ? 11.531  -36.414 -50.943 1.00 117.15 ? 275  GLY B C   1 
ATOM   5124 O O   . GLY B 1 275 ? 11.200  -36.216 -52.114 1.00 116.32 ? 275  GLY B O   1 
ATOM   5125 N N   . ASN B 1 276 ? 11.541  -37.642 -50.389 1.00 112.22 ? 276  ASN B N   1 
ATOM   5126 C CA  . ASN B 1 276 ? 11.136  -38.797 -51.179 1.00 111.21 ? 276  ASN B CA  1 
ATOM   5127 C C   . ASN B 1 276 ? 10.090  -39.668 -50.491 1.00 112.76 ? 276  ASN B C   1 
ATOM   5128 O O   . ASN B 1 276 ? 9.953   -39.668 -49.271 1.00 111.89 ? 276  ASN B O   1 
ATOM   5129 C CB  . ASN B 1 276 ? 12.319  -39.629 -51.683 1.00 112.21 ? 276  ASN B CB  1 
ATOM   5130 C CG  . ASN B 1 276 ? 12.084  -40.178 -53.091 1.00 137.22 ? 276  ASN B CG  1 
ATOM   5131 O OD1 . ASN B 1 276 ? 10.962  -40.145 -53.633 1.00 129.94 ? 276  ASN B OD1 1 
ATOM   5132 N ND2 . ASN B 1 276 ? 13.132  -40.698 -53.724 1.00 127.54 ? 276  ASN B ND2 1 
ATOM   5133 N N   . LEU B 1 277 ? 9.347   -40.401 -51.323 1.00 107.96 ? 277  LEU B N   1 
ATOM   5134 C CA  . LEU B 1 277 ? 8.223   -41.264 -50.987 1.00 107.20 ? 277  LEU B CA  1 
ATOM   5135 C C   . LEU B 1 277 ? 8.672   -42.596 -50.324 1.00 110.50 ? 277  LEU B C   1 
ATOM   5136 O O   . LEU B 1 277 ? 9.030   -43.556 -51.009 1.00 109.77 ? 277  LEU B O   1 
ATOM   5137 C CB  . LEU B 1 277 ? 7.353   -41.466 -52.266 1.00 107.05 ? 277  LEU B CB  1 
ATOM   5138 C CG  . LEU B 1 277 ? 7.202   -40.225 -53.217 1.00 110.75 ? 277  LEU B CG  1 
ATOM   5139 C CD1 . LEU B 1 277 ? 6.868   -40.630 -54.644 1.00 109.98 ? 277  LEU B CD1 1 
ATOM   5140 C CD2 . LEU B 1 277 ? 6.215   -39.176 -52.661 1.00 112.32 ? 277  LEU B CD2 1 
ATOM   5141 N N   . LEU B 1 278 ? 8.660   -42.623 -48.970 1.00 106.94 ? 278  LEU B N   1 
ATOM   5142 C CA  . LEU B 1 278 ? 9.090   -43.752 -48.135 1.00 106.80 ? 278  LEU B CA  1 
ATOM   5143 C C   . LEU B 1 278 ? 7.893   -44.515 -47.560 1.00 113.43 ? 278  LEU B C   1 
ATOM   5144 O O   . LEU B 1 278 ? 7.462   -44.249 -46.431 1.00 113.32 ? 278  LEU B O   1 
ATOM   5145 C CB  . LEU B 1 278 ? 10.000  -43.226 -47.008 1.00 106.47 ? 278  LEU B CB  1 
ATOM   5146 C CG  . LEU B 1 278 ? 11.511  -43.301 -47.226 1.00 110.97 ? 278  LEU B CG  1 
ATOM   5147 C CD1 . LEU B 1 278 ? 12.023  -42.207 -48.189 1.00 110.68 ? 278  LEU B CD1 1 
ATOM   5148 C CD2 . LEU B 1 278 ? 12.234  -43.200 -45.900 1.00 113.97 ? 278  LEU B CD2 1 
ATOM   5149 N N   . PHE B 1 279 ? 7.364   -45.475 -48.337 1.00 112.01 ? 279  PHE B N   1 
ATOM   5150 C CA  . PHE B 1 279 ? 6.186   -46.272 -47.989 1.00 113.00 ? 279  PHE B CA  1 
ATOM   5151 C C   . PHE B 1 279 ? 6.429   -47.380 -46.946 1.00 119.94 ? 279  PHE B C   1 
ATOM   5152 O O   . PHE B 1 279 ? 7.532   -47.925 -46.873 1.00 119.95 ? 279  PHE B O   1 
ATOM   5153 C CB  . PHE B 1 279 ? 5.563   -46.850 -49.268 1.00 115.14 ? 279  PHE B CB  1 
ATOM   5154 C CG  . PHE B 1 279 ? 4.236   -47.551 -49.094 1.00 117.35 ? 279  PHE B CG  1 
ATOM   5155 C CD1 . PHE B 1 279 ? 3.248   -47.018 -48.266 1.00 119.97 ? 279  PHE B CD1 1 
ATOM   5156 C CD2 . PHE B 1 279 ? 3.967   -48.738 -49.761 1.00 121.09 ? 279  PHE B CD2 1 
ATOM   5157 C CE1 . PHE B 1 279 ? 2.037   -47.685 -48.074 1.00 123.10 ? 279  PHE B CE1 1 
ATOM   5158 C CE2 . PHE B 1 279 ? 2.744   -49.395 -49.586 1.00 122.42 ? 279  PHE B CE2 1 
ATOM   5159 C CZ  . PHE B 1 279 ? 1.789   -48.863 -48.744 1.00 121.61 ? 279  PHE B CZ  1 
ATOM   5160 N N   . THR B 1 280 ? 5.366   -47.713 -46.149 1.00 118.80 ? 280  THR B N   1 
ATOM   5161 C CA  . THR B 1 280 ? 5.329   -48.753 -45.089 1.00 119.25 ? 280  THR B CA  1 
ATOM   5162 C C   . THR B 1 280 ? 5.264   -50.183 -45.677 1.00 122.48 ? 280  THR B C   1 
ATOM   5163 O O   . THR B 1 280 ? 5.518   -51.149 -44.955 1.00 121.88 ? 280  THR B O   1 
ATOM   5164 C CB  . THR B 1 280 ? 4.205   -48.477 -44.038 1.00 129.12 ? 280  THR B CB  1 
ATOM   5165 O OG1 . THR B 1 280 ? 4.620   -48.952 -42.755 1.00 129.45 ? 280  THR B OG1 1 
ATOM   5166 C CG2 . THR B 1 280 ? 2.849   -49.093 -44.409 1.00 127.49 ? 280  THR B CG2 1 
ATOM   5167 N N   . GLY B 1 281 ? 4.921   -50.286 -46.963 1.00 118.67 ? 281  GLY B N   1 
ATOM   5168 C CA  . GLY B 1 281 ? 4.857   -51.544 -47.698 1.00 118.27 ? 281  GLY B CA  1 
ATOM   5169 C C   . GLY B 1 281 ? 6.229   -52.139 -47.953 1.00 121.09 ? 281  GLY B C   1 
ATOM   5170 O O   . GLY B 1 281 ? 7.258   -51.461 -47.802 1.00 120.67 ? 281  GLY B O   1 
ATOM   5171 N N   . HIS B 1 282 ? 6.248   -53.421 -48.336 1.00 116.05 ? 282  HIS B N   1 
ATOM   5172 C CA  . HIS B 1 282 ? 7.487   -54.152 -48.568 1.00 115.22 ? 282  HIS B CA  1 
ATOM   5173 C C   . HIS B 1 282 ? 7.525   -54.882 -49.913 1.00 114.12 ? 282  HIS B C   1 
ATOM   5174 O O   . HIS B 1 282 ? 6.485   -55.088 -50.547 1.00 114.13 ? 282  HIS B O   1 
ATOM   5175 C CB  . HIS B 1 282 ? 7.770   -55.107 -47.394 1.00 116.93 ? 282  HIS B CB  1 
ATOM   5176 C CG  . HIS B 1 282 ? 6.651   -56.063 -47.103 1.00 121.13 ? 282  HIS B CG  1 
ATOM   5177 N ND1 . HIS B 1 282 ? 5.616   -55.721 -46.250 1.00 123.23 ? 282  HIS B ND1 1 
ATOM   5178 C CD2 . HIS B 1 282 ? 6.434   -57.315 -47.575 1.00 123.29 ? 282  HIS B CD2 1 
ATOM   5179 C CE1 . HIS B 1 282 ? 4.810   -56.773 -46.225 1.00 122.80 ? 282  HIS B CE1 1 
ATOM   5180 N NE2 . HIS B 1 282 ? 5.267   -57.761 -46.999 1.00 123.12 ? 282  HIS B NE2 1 
ATOM   5181 N N   . LEU B 1 283 ? 8.741   -55.269 -50.341 1.00 106.01 ? 283  LEU B N   1 
ATOM   5182 C CA  . LEU B 1 283 ? 8.995   -55.954 -51.603 1.00 103.24 ? 283  LEU B CA  1 
ATOM   5183 C C   . LEU B 1 283 ? 9.424   -57.402 -51.363 1.00 104.79 ? 283  LEU B C   1 
ATOM   5184 O O   . LEU B 1 283 ? 10.514  -57.642 -50.832 1.00 103.95 ? 283  LEU B O   1 
ATOM   5185 C CB  . LEU B 1 283 ? 10.078  -55.179 -52.359 1.00 102.32 ? 283  LEU B CB  1 
ATOM   5186 C CG  . LEU B 1 283 ? 10.140  -55.354 -53.854 1.00 105.39 ? 283  LEU B CG  1 
ATOM   5187 C CD1 . LEU B 1 283 ? 8.796   -55.050 -54.516 1.00 105.40 ? 283  LEU B CD1 1 
ATOM   5188 C CD2 . LEU B 1 283 ? 11.182  -54.459 -54.412 1.00 105.66 ? 283  LEU B CD2 1 
ATOM   5189 N N   . LYS B 1 284 ? 8.550   -58.364 -51.728 1.00 99.78  ? 284  LYS B N   1 
ATOM   5190 C CA  . LYS B 1 284 ? 8.817   -59.797 -51.560 1.00 98.68  ? 284  LYS B CA  1 
ATOM   5191 C C   . LYS B 1 284 ? 9.500   -60.356 -52.792 1.00 102.58 ? 284  LYS B C   1 
ATOM   5192 O O   . LYS B 1 284 ? 8.885   -60.509 -53.850 1.00 102.12 ? 284  LYS B O   1 
ATOM   5193 C CB  . LYS B 1 284 ? 7.555   -60.598 -51.176 1.00 99.92  ? 284  LYS B CB  1 
ATOM   5194 C CG  . LYS B 1 284 ? 7.160   -60.467 -49.701 1.00 101.58 ? 284  LYS B CG  1 
ATOM   5195 C CD  . LYS B 1 284 ? 5.926   -61.318 -49.344 1.00 98.91  ? 284  LYS B CD  1 
ATOM   5196 C CE  . LYS B 1 284 ? 5.568   -61.243 -47.875 1.00 87.51  ? 284  LYS B CE  1 
ATOM   5197 N NZ  . LYS B 1 284 ? 4.484   -62.192 -47.531 1.00 82.53  ? 284  LYS B NZ  1 
ATOM   5198 N N   . CYS B 1 285 ? 10.797  -60.625 -52.655 1.00 99.81  ? 285  CYS B N   1 
ATOM   5199 C CA  . CYS B 1 285 ? 11.607  -61.127 -53.752 1.00 100.19 ? 285  CYS B CA  1 
ATOM   5200 C C   . CYS B 1 285 ? 12.017  -62.567 -53.603 1.00 102.54 ? 285  CYS B C   1 
ATOM   5201 O O   . CYS B 1 285 ? 12.022  -63.135 -52.504 1.00 102.93 ? 285  CYS B O   1 
ATOM   5202 C CB  . CYS B 1 285 ? 12.822  -60.236 -53.980 1.00 101.16 ? 285  CYS B CB  1 
ATOM   5203 S SG  . CYS B 1 285 ? 12.415  -58.492 -54.189 1.00 105.60 ? 285  CYS B SG  1 
ATOM   5204 N N   . ARG B 1 286 ? 12.384  -63.136 -54.742 1.00 96.29  ? 286  ARG B N   1 
ATOM   5205 C CA  . ARG B 1 286 ? 12.927  -64.458 -54.887 1.00 95.13  ? 286  ARG B CA  1 
ATOM   5206 C C   . ARG B 1 286 ? 14.287  -64.242 -55.518 1.00 99.99  ? 286  ARG B C   1 
ATOM   5207 O O   . ARG B 1 286 ? 14.443  -63.360 -56.369 1.00 99.87  ? 286  ARG B O   1 
ATOM   5208 C CB  . ARG B 1 286 ? 12.022  -65.330 -55.741 1.00 92.32  ? 286  ARG B CB  1 
ATOM   5209 C CG  . ARG B 1 286 ? 12.186  -66.786 -55.392 1.00 102.24 ? 286  ARG B CG  1 
ATOM   5210 C CD  . ARG B 1 286 ? 11.008  -67.614 -55.850 1.00 113.54 ? 286  ARG B CD  1 
ATOM   5211 N NE  . ARG B 1 286 ? 10.341  -68.287 -54.736 1.00 120.72 ? 286  ARG B NE  1 
ATOM   5212 C CZ  . ARG B 1 286 ? 10.712  -69.460 -54.229 1.00 137.63 ? 286  ARG B CZ  1 
ATOM   5213 N NH1 . ARG B 1 286 ? 11.769  -70.097 -54.716 1.00 121.97 ? 286  ARG B NH1 1 
ATOM   5214 N NH2 . ARG B 1 286 ? 10.043  -69.994 -53.219 1.00 130.98 ? 286  ARG B NH2 1 
ATOM   5215 N N   . LEU B 1 287 ? 15.280  -65.004 -55.060 1.00 96.61  ? 287  LEU B N   1 
ATOM   5216 C CA  . LEU B 1 287 ? 16.642  -64.819 -55.512 1.00 96.21  ? 287  LEU B CA  1 
ATOM   5217 C C   . LEU B 1 287 ? 17.303  -66.101 -55.977 1.00 101.20 ? 287  LEU B C   1 
ATOM   5218 O O   . LEU B 1 287 ? 17.430  -67.041 -55.198 1.00 100.35 ? 287  LEU B O   1 
ATOM   5219 C CB  . LEU B 1 287 ? 17.437  -64.188 -54.368 1.00 95.92  ? 287  LEU B CB  1 
ATOM   5220 C CG  . LEU B 1 287 ? 18.518  -63.235 -54.757 1.00 100.01 ? 287  LEU B CG  1 
ATOM   5221 C CD1 . LEU B 1 287 ? 18.061  -61.818 -54.566 1.00 99.75  ? 287  LEU B CD1 1 
ATOM   5222 C CD2 . LEU B 1 287 ? 19.748  -63.490 -53.939 1.00 103.12 ? 287  LEU B CD2 1 
ATOM   5223 N N   . ARG B 1 288 ? 17.727  -66.127 -57.254 1.00 99.34  ? 288  ARG B N   1 
ATOM   5224 C CA  . ARG B 1 288 ? 18.462  -67.231 -57.861 1.00 99.46  ? 288  ARG B CA  1 
ATOM   5225 C C   . ARG B 1 288 ? 19.911  -66.822 -57.973 1.00 105.63 ? 288  ARG B C   1 
ATOM   5226 O O   . ARG B 1 288 ? 20.233  -65.719 -58.439 1.00 105.44 ? 288  ARG B O   1 
ATOM   5227 C CB  . ARG B 1 288 ? 17.848  -67.700 -59.180 1.00 98.31  ? 288  ARG B CB  1 
ATOM   5228 C CG  . ARG B 1 288 ? 16.786  -68.763 -58.923 1.00 110.03 ? 288  ARG B CG  1 
ATOM   5229 C CD  . ARG B 1 288 ? 16.120  -69.309 -60.175 1.00 125.49 ? 288  ARG B CD  1 
ATOM   5230 N NE  . ARG B 1 288 ? 16.877  -70.385 -60.832 1.00 134.79 ? 288  ARG B NE  1 
ATOM   5231 C CZ  . ARG B 1 288 ? 16.841  -71.671 -60.482 1.00 143.48 ? 288  ARG B CZ  1 
ATOM   5232 N NH1 . ARG B 1 288 ? 16.130  -72.061 -59.429 1.00 129.38 ? 288  ARG B NH1 1 
ATOM   5233 N NH2 . ARG B 1 288 ? 17.541  -72.570 -61.162 1.00 123.56 ? 288  ARG B NH2 1 
ATOM   5234 N N   . MET B 1 289 ? 20.771  -67.691 -57.442 1.00 103.65 ? 289  MET B N   1 
ATOM   5235 C CA  . MET B 1 289 ? 22.211  -67.516 -57.292 1.00 104.14 ? 289  MET B CA  1 
ATOM   5236 C C   . MET B 1 289 ? 23.028  -68.542 -58.073 1.00 109.57 ? 289  MET B C   1 
ATOM   5237 O O   . MET B 1 289 ? 24.246  -68.600 -57.919 1.00 108.78 ? 289  MET B O   1 
ATOM   5238 C CB  . MET B 1 289 ? 22.537  -67.571 -55.799 1.00 106.43 ? 289  MET B CB  1 
ATOM   5239 C CG  . MET B 1 289 ? 22.072  -66.346 -55.057 1.00 109.88 ? 289  MET B CG  1 
ATOM   5240 S SD  . MET B 1 289 ? 22.070  -66.575 -53.275 1.00 113.67 ? 289  MET B SD  1 
ATOM   5241 C CE  . MET B 1 289 ? 23.009  -65.154 -52.735 1.00 109.92 ? 289  MET B CE  1 
ATOM   5242 N N   . ASP B 1 290 ? 22.359  -69.323 -58.947 1.00 107.45 ? 290  ASP B N   1 
ATOM   5243 C CA  . ASP B 1 290 ? 22.982  -70.335 -59.806 1.00 107.52 ? 290  ASP B CA  1 
ATOM   5244 C C   . ASP B 1 290 ? 24.066  -69.711 -60.693 1.00 110.56 ? 290  ASP B C   1 
ATOM   5245 O O   . ASP B 1 290 ? 25.121  -70.317 -60.881 1.00 110.59 ? 290  ASP B O   1 
ATOM   5246 C CB  . ASP B 1 290 ? 21.919  -71.054 -60.662 1.00 110.01 ? 290  ASP B CB  1 
ATOM   5247 C CG  . ASP B 1 290 ? 21.087  -70.140 -61.550 1.00 128.91 ? 290  ASP B CG  1 
ATOM   5248 O OD1 . ASP B 1 290 ? 20.106  -69.541 -61.038 1.00 131.55 ? 290  ASP B OD1 1 
ATOM   5249 O OD2 . ASP B 1 290 ? 21.405  -70.037 -62.761 1.00 136.42 ? 290  ASP B OD2 1 
ATOM   5250 N N   . LYS B 1 291 ? 23.820  -68.474 -61.188 1.00 105.61 ? 291  LYS B N   1 
ATOM   5251 C CA  . LYS B 1 291 ? 24.743  -67.740 -62.055 1.00 104.14 ? 291  LYS B CA  1 
ATOM   5252 C C   . LYS B 1 291 ? 25.777  -66.890 -61.282 1.00 104.70 ? 291  LYS B C   1 
ATOM   5253 O O   . LYS B 1 291 ? 26.632  -66.249 -61.894 1.00 103.35 ? 291  LYS B O   1 
ATOM   5254 C CB  . LYS B 1 291 ? 23.959  -66.912 -63.084 1.00 106.43 ? 291  LYS B CB  1 
ATOM   5255 C CG  . LYS B 1 291 ? 23.628  -67.699 -64.363 1.00 114.26 ? 291  LYS B CG  1 
ATOM   5256 C CD  . LYS B 1 291 ? 22.804  -66.893 -65.347 1.00 121.16 ? 291  LYS B CD  1 
ATOM   5257 C CE  . LYS B 1 291 ? 23.352  -66.953 -66.754 1.00 125.98 ? 291  LYS B CE  1 
ATOM   5258 N NZ  . LYS B 1 291 ? 22.976  -65.739 -67.524 1.00 129.57 ? 291  LYS B NZ  1 
ATOM   5259 N N   . LEU B 1 292 ? 25.710  -66.912 -59.945 1.00 100.27 ? 292  LEU B N   1 
ATOM   5260 C CA  . LEU B 1 292 ? 26.661  -66.223 -59.079 1.00 99.38  ? 292  LEU B CA  1 
ATOM   5261 C C   . LEU B 1 292 ? 27.824  -67.156 -58.779 1.00 100.15 ? 292  LEU B C   1 
ATOM   5262 O O   . LEU B 1 292 ? 27.625  -68.359 -58.591 1.00 100.21 ? 292  LEU B O   1 
ATOM   5263 C CB  . LEU B 1 292 ? 26.013  -65.832 -57.748 1.00 99.62  ? 292  LEU B CB  1 
ATOM   5264 C CG  . LEU B 1 292 ? 25.412  -64.456 -57.605 1.00 104.18 ? 292  LEU B CG  1 
ATOM   5265 C CD1 . LEU B 1 292 ? 24.962  -64.244 -56.187 1.00 104.42 ? 292  LEU B CD1 1 
ATOM   5266 C CD2 . LEU B 1 292 ? 26.390  -63.353 -58.005 1.00 105.20 ? 292  LEU B CD2 1 
ATOM   5267 N N   . GLN B 1 293 ? 29.022  -66.586 -58.670 1.00 93.16  ? 293  GLN B N   1 
ATOM   5268 C CA  . GLN B 1 293 ? 30.239  -67.314 -58.377 1.00 91.38  ? 293  GLN B CA  1 
ATOM   5269 C C   . GLN B 1 293 ? 31.164  -66.502 -57.479 1.00 93.22  ? 293  GLN B C   1 
ATOM   5270 O O   . GLN B 1 293 ? 31.186  -65.266 -57.548 1.00 91.89  ? 293  GLN B O   1 
ATOM   5271 C CB  . GLN B 1 293 ? 30.939  -67.747 -59.680 1.00 92.87  ? 293  GLN B CB  1 
ATOM   5272 C CG  . GLN B 1 293 ? 31.168  -66.611 -60.680 1.00 121.14 ? 293  GLN B CG  1 
ATOM   5273 C CD  . GLN B 1 293 ? 31.622  -67.102 -62.030 1.00 147.25 ? 293  GLN B CD  1 
ATOM   5274 O OE1 . GLN B 1 293 ? 32.766  -66.863 -62.440 1.00 143.49 ? 293  GLN B OE1 1 
ATOM   5275 N NE2 . GLN B 1 293 ? 30.726  -67.765 -62.766 1.00 139.93 ? 293  GLN B NE2 1 
ATOM   5276 N N   . LEU B 1 294 ? 31.938  -67.211 -56.641 1.00 90.27  ? 294  LEU B N   1 
ATOM   5277 C CA  . LEU B 1 294 ? 32.913  -66.637 -55.712 1.00 90.57  ? 294  LEU B CA  1 
ATOM   5278 C C   . LEU B 1 294 ? 34.090  -66.038 -56.465 1.00 98.77  ? 294  LEU B C   1 
ATOM   5279 O O   . LEU B 1 294 ? 34.662  -66.721 -57.314 1.00 98.99  ? 294  LEU B O   1 
ATOM   5280 C CB  . LEU B 1 294 ? 33.406  -67.731 -54.787 1.00 90.02  ? 294  LEU B CB  1 
ATOM   5281 C CG  . LEU B 1 294 ? 32.536  -68.036 -53.610 1.00 94.42  ? 294  LEU B CG  1 
ATOM   5282 C CD1 . LEU B 1 294 ? 32.990  -69.294 -52.959 1.00 95.06  ? 294  LEU B CD1 1 
ATOM   5283 C CD2 . LEU B 1 294 ? 32.583  -66.906 -52.620 1.00 97.47  ? 294  LEU B CD2 1 
ATOM   5284 N N   . LYS B 1 295 ? 34.470  -64.790 -56.153 1.00 97.90  ? 295  LYS B N   1 
ATOM   5285 C CA  . LYS B 1 295 ? 35.543  -64.136 -56.896 1.00 99.36  ? 295  LYS B CA  1 
ATOM   5286 C C   . LYS B 1 295 ? 36.856  -64.922 -56.943 1.00 109.11 ? 295  LYS B C   1 
ATOM   5287 O O   . LYS B 1 295 ? 37.229  -65.294 -58.051 1.00 109.22 ? 295  LYS B O   1 
ATOM   5288 C CB  . LYS B 1 295 ? 35.772  -62.675 -56.479 1.00 101.28 ? 295  LYS B CB  1 
ATOM   5289 C CG  . LYS B 1 295 ? 36.592  -61.870 -57.501 1.00 106.98 ? 295  LYS B CG  1 
ATOM   5290 C CD  . LYS B 1 295 ? 37.145  -60.559 -56.944 1.00 111.33 ? 295  LYS B CD  1 
ATOM   5291 C CE  . LYS B 1 295 ? 37.612  -59.580 -58.009 1.00 116.87 ? 295  LYS B CE  1 
ATOM   5292 N NZ  . LYS B 1 295 ? 38.738  -60.113 -58.816 1.00 122.79 ? 295  LYS B NZ  1 
ATOM   5293 N N   . GLY B 1 296 ? 37.554  -65.140 -55.837 1.00 109.96 ? 296  GLY B N   1 
ATOM   5294 C CA  . GLY B 1 296 ? 38.842  -65.829 -55.912 1.00 111.85 ? 296  GLY B CA  1 
ATOM   5295 C C   . GLY B 1 296 ? 38.900  -67.294 -55.518 1.00 120.10 ? 296  GLY B C   1 
ATOM   5296 O O   . GLY B 1 296 ? 39.864  -67.692 -54.858 1.00 119.80 ? 296  GLY B O   1 
ATOM   5297 N N   . MET B 1 297 ? 37.913  -68.127 -55.954 1.00 119.40 ? 297  MET B N   1 
ATOM   5298 C CA  . MET B 1 297 ? 37.848  -69.565 -55.609 1.00 120.11 ? 297  MET B CA  1 
ATOM   5299 C C   . MET B 1 297 ? 39.000  -70.371 -56.253 1.00 122.77 ? 297  MET B C   1 
ATOM   5300 O O   . MET B 1 297 ? 39.305  -71.483 -55.800 1.00 122.78 ? 297  MET B O   1 
ATOM   5301 C CB  . MET B 1 297 ? 36.455  -70.190 -55.902 1.00 122.94 ? 297  MET B CB  1 
ATOM   5302 C CG  . MET B 1 297 ? 36.086  -71.374 -54.983 1.00 127.47 ? 297  MET B CG  1 
ATOM   5303 S SD  . MET B 1 297 ? 36.543  -71.209 -53.220 1.00 132.68 ? 297  MET B SD  1 
ATOM   5304 C CE  . MET B 1 297 ? 36.064  -72.842 -52.600 1.00 129.69 ? 297  MET B CE  1 
ATOM   5305 N N   . SER B 1 298 ? 39.672  -69.770 -57.257 1.00 117.08 ? 298  SER B N   1 
ATOM   5306 C CA  . SER B 1 298 ? 40.794  -70.358 -57.984 1.00 115.87 ? 298  SER B CA  1 
ATOM   5307 C C   . SER B 1 298 ? 42.143  -69.759 -57.570 1.00 117.84 ? 298  SER B C   1 
ATOM   5308 O O   . SER B 1 298 ? 43.190  -70.303 -57.938 1.00 117.43 ? 298  SER B O   1 
ATOM   5309 C CB  . SER B 1 298 ? 40.572  -70.258 -59.493 1.00 118.83 ? 298  SER B CB  1 
ATOM   5310 O OG  . SER B 1 298 ? 40.256  -68.942 -59.926 1.00 125.42 ? 298  SER B OG  1 
ATOM   5311 N N   . TYR B 1 299 ? 42.127  -68.662 -56.783 1.00 113.23 ? 299  TYR B N   1 
ATOM   5312 C CA  . TYR B 1 299 ? 43.367  -68.036 -56.312 1.00 112.59 ? 299  TYR B CA  1 
ATOM   5313 C C   . TYR B 1 299 ? 44.026  -68.935 -55.274 1.00 113.39 ? 299  TYR B C   1 
ATOM   5314 O O   . TYR B 1 299 ? 43.352  -69.699 -54.580 1.00 112.29 ? 299  TYR B O   1 
ATOM   5315 C CB  . TYR B 1 299 ? 43.138  -66.652 -55.663 1.00 114.57 ? 299  TYR B CB  1 
ATOM   5316 C CG  . TYR B 1 299 ? 42.562  -65.531 -56.513 1.00 117.38 ? 299  TYR B CG  1 
ATOM   5317 C CD1 . TYR B 1 299 ? 42.448  -65.654 -57.897 1.00 119.10 ? 299  TYR B CD1 1 
ATOM   5318 C CD2 . TYR B 1 299 ? 42.174  -64.328 -55.936 1.00 119.07 ? 299  TYR B CD2 1 
ATOM   5319 C CE1 . TYR B 1 299 ? 41.929  -64.619 -58.679 1.00 119.96 ? 299  TYR B CE1 1 
ATOM   5320 C CE2 . TYR B 1 299 ? 41.637  -63.293 -56.703 1.00 120.55 ? 299  TYR B CE2 1 
ATOM   5321 C CZ  . TYR B 1 299 ? 41.508  -63.442 -58.073 1.00 129.01 ? 299  TYR B CZ  1 
ATOM   5322 O OH  . TYR B 1 299 ? 40.953  -62.408 -58.798 1.00 131.80 ? 299  TYR B OH  1 
ATOM   5323 N N   . SER B 1 300 ? 45.335  -68.821 -55.158 1.00 108.50 ? 300  SER B N   1 
ATOM   5324 C CA  . SER B 1 300 ? 46.135  -69.586 -54.209 1.00 107.69 ? 300  SER B CA  1 
ATOM   5325 C C   . SER B 1 300 ? 46.028  -68.977 -52.801 1.00 109.86 ? 300  SER B C   1 
ATOM   5326 O O   . SER B 1 300 ? 45.598  -67.832 -52.680 1.00 109.71 ? 300  SER B O   1 
ATOM   5327 C CB  . SER B 1 300 ? 47.586  -69.605 -54.677 1.00 111.26 ? 300  SER B CB  1 
ATOM   5328 O OG  . SER B 1 300 ? 48.047  -68.294 -54.976 1.00 120.71 ? 300  SER B OG  1 
ATOM   5329 N N   . MET B 1 301 ? 46.398  -69.737 -51.748 1.00 104.87 ? 301  MET B N   1 
ATOM   5330 C CA  . MET B 1 301 ? 46.356  -69.269 -50.361 1.00 104.34 ? 301  MET B CA  1 
ATOM   5331 C C   . MET B 1 301 ? 47.495  -68.320 -50.057 1.00 107.70 ? 301  MET B C   1 
ATOM   5332 O O   . MET B 1 301 ? 48.633  -68.594 -50.443 1.00 107.77 ? 301  MET B O   1 
ATOM   5333 C CB  . MET B 1 301 ? 46.415  -70.451 -49.394 1.00 106.96 ? 301  MET B CB  1 
ATOM   5334 C CG  . MET B 1 301 ? 45.207  -71.355 -49.466 1.00 111.25 ? 301  MET B CG  1 
ATOM   5335 S SD  . MET B 1 301 ? 43.740  -70.546 -48.788 1.00 116.42 ? 301  MET B SD  1 
ATOM   5336 C CE  . MET B 1 301 ? 44.013  -70.779 -47.032 1.00 113.14 ? 301  MET B CE  1 
ATOM   5337 N N   . CYS B 1 302 ? 47.203  -67.210 -49.355 1.00 104.06 ? 302  CYS B N   1 
ATOM   5338 C CA  . CYS B 1 302 ? 48.236  -66.244 -48.958 1.00 103.85 ? 302  CYS B CA  1 
ATOM   5339 C C   . CYS B 1 302 ? 49.216  -66.995 -48.050 1.00 106.20 ? 302  CYS B C   1 
ATOM   5340 O O   . CYS B 1 302 ? 48.799  -67.878 -47.293 1.00 105.40 ? 302  CYS B O   1 
ATOM   5341 C CB  . CYS B 1 302 ? 47.635  -65.036 -48.233 1.00 104.27 ? 302  CYS B CB  1 
ATOM   5342 S SG  . CYS B 1 302 ? 46.548  -63.989 -49.242 1.00 108.22 ? 302  CYS B SG  1 
ATOM   5343 N N   . THR B 1 303 ? 50.510  -66.678 -48.157 1.00 101.71 ? 303  THR B N   1 
ATOM   5344 C CA  . THR B 1 303 ? 51.533  -67.337 -47.334 1.00 101.19 ? 303  THR B CA  1 
ATOM   5345 C C   . THR B 1 303 ? 52.144  -66.373 -46.303 1.00 103.60 ? 303  THR B C   1 
ATOM   5346 O O   . THR B 1 303 ? 52.616  -66.805 -45.245 1.00 102.88 ? 303  THR B O   1 
ATOM   5347 C CB  . THR B 1 303 ? 52.606  -68.052 -48.203 1.00 108.71 ? 303  THR B CB  1 
ATOM   5348 O OG1 . THR B 1 303 ? 53.281  -67.113 -49.045 1.00 108.99 ? 303  THR B OG1 1 
ATOM   5349 C CG2 . THR B 1 303 ? 52.039  -69.210 -49.027 1.00 105.55 ? 303  THR B CG2 1 
ATOM   5350 N N   . GLY B 1 304 ? 52.098  -65.081 -46.623 1.00 98.58  ? 304  GLY B N   1 
ATOM   5351 C CA  . GLY B 1 304 ? 52.667  -64.017 -45.808 1.00 97.33  ? 304  GLY B CA  1 
ATOM   5352 C C   . GLY B 1 304 ? 52.039  -63.765 -44.457 1.00 98.14  ? 304  GLY B C   1 
ATOM   5353 O O   . GLY B 1 304 ? 51.226  -64.551 -43.958 1.00 96.71  ? 304  GLY B O   1 
ATOM   5354 N N   . LYS B 1 305 ? 52.457  -62.645 -43.862 1.00 93.58  ? 305  LYS B N   1 
ATOM   5355 C CA  . LYS B 1 305 ? 52.019  -62.177 -42.552 1.00 92.52  ? 305  LYS B CA  1 
ATOM   5356 C C   . LYS B 1 305 ? 51.008  -61.033 -42.704 1.00 93.96  ? 305  LYS B C   1 
ATOM   5357 O O   . LYS B 1 305 ? 51.040  -60.294 -43.695 1.00 92.48  ? 305  LYS B O   1 
ATOM   5358 C CB  . LYS B 1 305 ? 53.221  -61.746 -41.683 1.00 94.37  ? 305  LYS B CB  1 
ATOM   5359 C CG  . LYS B 1 305 ? 54.204  -62.854 -41.363 1.00 105.70 ? 305  LYS B CG  1 
ATOM   5360 C CD  . LYS B 1 305 ? 55.238  -62.406 -40.333 1.00 116.65 ? 305  LYS B CD  1 
ATOM   5361 C CE  . LYS B 1 305 ? 56.312  -63.447 -40.108 1.00 133.89 ? 305  LYS B CE  1 
ATOM   5362 N NZ  . LYS B 1 305 ? 56.523  -63.741 -38.664 1.00 146.12 ? 305  LYS B NZ  1 
ATOM   5363 N N   . PHE B 1 306 ? 50.115  -60.902 -41.713 1.00 89.08  ? 306  PHE B N   1 
ATOM   5364 C CA  . PHE B 1 306 ? 49.062  -59.900 -41.695 1.00 87.91  ? 306  PHE B CA  1 
ATOM   5365 C C   . PHE B 1 306 ? 49.164  -58.965 -40.508 1.00 91.80  ? 306  PHE B C   1 
ATOM   5366 O O   . PHE B 1 306 ? 49.523  -59.390 -39.416 1.00 91.08  ? 306  PHE B O   1 
ATOM   5367 C CB  . PHE B 1 306 ? 47.697  -60.588 -41.701 1.00 89.01  ? 306  PHE B CB  1 
ATOM   5368 C CG  . PHE B 1 306 ? 47.382  -61.339 -42.970 1.00 89.62  ? 306  PHE B CG  1 
ATOM   5369 C CD1 . PHE B 1 306 ? 46.839  -60.685 -44.068 1.00 90.59  ? 306  PHE B CD1 1 
ATOM   5370 C CD2 . PHE B 1 306 ? 47.615  -62.701 -43.065 1.00 92.60  ? 306  PHE B CD2 1 
ATOM   5371 C CE1 . PHE B 1 306 ? 46.511  -61.384 -45.228 1.00 93.23  ? 306  PHE B CE1 1 
ATOM   5372 C CE2 . PHE B 1 306 ? 47.305  -63.396 -44.235 1.00 93.66  ? 306  PHE B CE2 1 
ATOM   5373 C CZ  . PHE B 1 306 ? 46.768  -62.731 -45.313 1.00 91.83  ? 306  PHE B CZ  1 
ATOM   5374 N N   . LYS B 1 307 ? 48.821  -57.695 -40.721 1.00 89.43  ? 307  LYS B N   1 
ATOM   5375 C CA  . LYS B 1 307 ? 48.820  -56.647 -39.698 1.00 89.59  ? 307  LYS B CA  1 
ATOM   5376 C C   . LYS B 1 307 ? 47.365  -56.261 -39.360 1.00 95.09  ? 307  LYS B C   1 
ATOM   5377 O O   . LYS B 1 307 ? 46.484  -56.384 -40.210 1.00 94.05  ? 307  LYS B O   1 
ATOM   5378 C CB  . LYS B 1 307 ? 49.620  -55.429 -40.179 1.00 91.19  ? 307  LYS B CB  1 
ATOM   5379 C CG  . LYS B 1 307 ? 50.246  -54.640 -39.042 1.00 98.00  ? 307  LYS B CG  1 
ATOM   5380 C CD  . LYS B 1 307 ? 51.569  -55.303 -38.563 1.00 108.77 ? 307  LYS B CD  1 
ATOM   5381 C CE  . LYS B 1 307 ? 52.786  -54.435 -38.752 1.00 118.78 ? 307  LYS B CE  1 
ATOM   5382 N NZ  . LYS B 1 307 ? 53.961  -54.942 -37.982 1.00 127.56 ? 307  LYS B NZ  1 
ATOM   5383 N N   . ILE B 1 308 ? 47.128  -55.779 -38.130 1.00 93.00  ? 308  ILE B N   1 
ATOM   5384 C CA  . ILE B 1 308 ? 45.798  -55.418 -37.622 1.00 92.78  ? 308  ILE B CA  1 
ATOM   5385 C C   . ILE B 1 308 ? 45.524  -53.906 -37.686 1.00 95.58  ? 308  ILE B C   1 
ATOM   5386 O O   . ILE B 1 308 ? 45.805  -53.166 -36.744 1.00 95.17  ? 308  ILE B O   1 
ATOM   5387 C CB  . ILE B 1 308 ? 45.536  -56.012 -36.208 1.00 95.92  ? 308  ILE B CB  1 
ATOM   5388 C CG1 . ILE B 1 308 ? 46.862  -56.462 -35.461 1.00 96.17  ? 308  ILE B CG1 1 
ATOM   5389 C CG2 . ILE B 1 308 ? 44.570  -57.186 -36.343 1.00 96.46  ? 308  ILE B CG2 1 
ATOM   5390 C CD1 . ILE B 1 308 ? 47.941  -55.343 -34.953 1.00 95.22  ? 308  ILE B CD1 1 
ATOM   5391 N N   . VAL B 1 309 ? 44.940  -53.475 -38.816 1.00 91.55  ? 309  VAL B N   1 
ATOM   5392 C CA  . VAL B 1 309 ? 44.561  -52.096 -39.177 1.00 90.61  ? 309  VAL B CA  1 
ATOM   5393 C C   . VAL B 1 309 ? 43.458  -51.550 -38.226 1.00 91.40  ? 309  VAL B C   1 
ATOM   5394 O O   . VAL B 1 309 ? 43.583  -50.453 -37.675 1.00 90.36  ? 309  VAL B O   1 
ATOM   5395 C CB  . VAL B 1 309 ? 44.106  -52.075 -40.671 1.00 95.04  ? 309  VAL B CB  1 
ATOM   5396 C CG1 . VAL B 1 309 ? 43.635  -50.692 -41.115 1.00 95.30  ? 309  VAL B CG1 1 
ATOM   5397 C CG2 . VAL B 1 309 ? 45.193  -52.606 -41.597 1.00 94.85  ? 309  VAL B CG2 1 
ATOM   5398 N N   . LYS B 1 310 ? 42.371  -52.315 -38.074 1.00 85.78  ? 310  LYS B N   1 
ATOM   5399 C CA  . LYS B 1 310 ? 41.248  -51.964 -37.224 1.00 83.84  ? 310  LYS B CA  1 
ATOM   5400 C C   . LYS B 1 310 ? 40.941  -53.142 -36.307 1.00 83.71  ? 310  LYS B C   1 
ATOM   5401 O O   . LYS B 1 310 ? 40.680  -54.267 -36.773 1.00 82.49  ? 310  LYS B O   1 
ATOM   5402 C CB  . LYS B 1 310 ? 40.018  -51.560 -38.063 1.00 85.96  ? 310  LYS B CB  1 
ATOM   5403 C CG  . LYS B 1 310 ? 39.127  -50.529 -37.399 1.00 94.33  ? 310  LYS B CG  1 
ATOM   5404 C CD  . LYS B 1 310 ? 38.246  -49.796 -38.392 1.00 90.86  ? 310  LYS B CD  1 
ATOM   5405 C CE  . LYS B 1 310 ? 37.448  -48.732 -37.685 1.00 87.14  ? 310  LYS B CE  1 
ATOM   5406 N NZ  . LYS B 1 310 ? 38.253  -47.504 -37.515 1.00 94.36  ? 310  LYS B NZ  1 
ATOM   5407 N N   . GLU B 1 311 ? 41.014  -52.866 -34.995 1.00 77.25  ? 311  GLU B N   1 
ATOM   5408 C CA  . GLU B 1 311 ? 40.757  -53.783 -33.900 1.00 75.96  ? 311  GLU B CA  1 
ATOM   5409 C C   . GLU B 1 311 ? 39.403  -54.493 -34.056 1.00 76.09  ? 311  GLU B C   1 
ATOM   5410 O O   . GLU B 1 311 ? 38.477  -53.928 -34.637 1.00 74.44  ? 311  GLU B O   1 
ATOM   5411 C CB  . GLU B 1 311 ? 40.800  -52.988 -32.586 1.00 77.79  ? 311  GLU B CB  1 
ATOM   5412 C CG  . GLU B 1 311 ? 40.652  -53.821 -31.322 1.00 94.96  ? 311  GLU B CG  1 
ATOM   5413 C CD  . GLU B 1 311 ? 40.919  -53.089 -30.022 1.00 137.45 ? 311  GLU B CD  1 
ATOM   5414 O OE1 . GLU B 1 311 ? 41.878  -52.283 -29.969 1.00 133.55 ? 311  GLU B OE1 1 
ATOM   5415 O OE2 . GLU B 1 311 ? 40.190  -53.359 -29.040 1.00 146.47 ? 311  GLU B OE2 1 
ATOM   5416 N N   . ILE B 1 312 ? 39.290  -55.728 -33.533 1.00 72.09  ? 312  ILE B N   1 
ATOM   5417 C CA  . ILE B 1 312 ? 38.039  -56.473 -33.572 1.00 72.00  ? 312  ILE B CA  1 
ATOM   5418 C C   . ILE B 1 312 ? 36.977  -55.603 -32.892 1.00 77.23  ? 312  ILE B C   1 
ATOM   5419 O O   . ILE B 1 312 ? 37.211  -55.085 -31.787 1.00 77.42  ? 312  ILE B O   1 
ATOM   5420 C CB  . ILE B 1 312 ? 38.096  -57.871 -32.899 1.00 74.96  ? 312  ILE B CB  1 
ATOM   5421 C CG1 . ILE B 1 312 ? 39.257  -58.731 -33.426 1.00 75.94  ? 312  ILE B CG1 1 
ATOM   5422 C CG2 . ILE B 1 312 ? 36.748  -58.600 -33.052 1.00 75.26  ? 312  ILE B CG2 1 
ATOM   5423 C CD1 . ILE B 1 312 ? 39.358  -60.181 -32.799 1.00 90.43  ? 312  ILE B CD1 1 
ATOM   5424 N N   . ALA B 1 313 ? 35.847  -55.398 -33.601 1.00 71.85  ? 313  ALA B N   1 
ATOM   5425 C CA  . ALA B 1 313 ? 34.686  -54.666 -33.133 1.00 70.26  ? 313  ALA B CA  1 
ATOM   5426 C C   . ALA B 1 313 ? 33.500  -55.578 -33.277 1.00 70.96  ? 313  ALA B C   1 
ATOM   5427 O O   . ALA B 1 313 ? 33.398  -56.296 -34.269 1.00 68.28  ? 313  ALA B O   1 
ATOM   5428 C CB  . ALA B 1 313 ? 34.488  -53.412 -33.953 1.00 71.31  ? 313  ALA B CB  1 
ATOM   5429 N N   . GLU B 1 314 ? 32.636  -55.610 -32.251 1.00 69.44  ? 314  GLU B N   1 
ATOM   5430 C CA  . GLU B 1 314 ? 31.445  -56.465 -32.267 1.00 69.94  ? 314  GLU B CA  1 
ATOM   5431 C C   . GLU B 1 314 ? 30.215  -55.679 -32.720 1.00 74.96  ? 314  GLU B C   1 
ATOM   5432 O O   . GLU B 1 314 ? 29.961  -54.564 -32.233 1.00 73.40  ? 314  GLU B O   1 
ATOM   5433 C CB  . GLU B 1 314 ? 31.215  -57.134 -30.899 1.00 71.08  ? 314  GLU B CB  1 
ATOM   5434 C CG  . GLU B 1 314 ? 30.151  -58.227 -30.910 1.00 83.41  ? 314  GLU B CG  1 
ATOM   5435 C CD  . GLU B 1 314 ? 29.854  -58.847 -29.552 1.00 107.73 ? 314  GLU B CD  1 
ATOM   5436 O OE1 . GLU B 1 314 ? 29.600  -58.081 -28.594 1.00 81.33  ? 314  GLU B OE1 1 
ATOM   5437 O OE2 . GLU B 1 314 ? 29.867  -60.097 -29.442 1.00 109.11 ? 314  GLU B OE2 1 
ATOM   5438 N N   . THR B 1 315 ? 29.469  -56.254 -33.672 1.00 73.45  ? 315  THR B N   1 
ATOM   5439 C CA  . THR B 1 315 ? 28.249  -55.632 -34.176 1.00 74.33  ? 315  THR B CA  1 
ATOM   5440 C C   . THR B 1 315 ? 27.109  -55.910 -33.204 1.00 81.68  ? 315  THR B C   1 
ATOM   5441 O O   . THR B 1 315 ? 27.245  -56.742 -32.297 1.00 83.61  ? 315  THR B O   1 
ATOM   5442 C CB  . THR B 1 315 ? 27.914  -56.023 -35.639 1.00 72.26  ? 315  THR B CB  1 
ATOM   5443 O OG1 . THR B 1 315 ? 27.303  -57.321 -35.684 1.00 54.19  ? 315  THR B OG1 1 
ATOM   5444 C CG2 . THR B 1 315 ? 29.117  -55.905 -36.576 1.00 73.19  ? 315  THR B CG2 1 
ATOM   5445 N N   . GLN B 1 316 ? 25.976  -55.238 -33.414 1.00 76.38  ? 316  GLN B N   1 
ATOM   5446 C CA  . GLN B 1 316 ? 24.797  -55.382 -32.584 1.00 74.64  ? 316  GLN B CA  1 
ATOM   5447 C C   . GLN B 1 316 ? 24.215  -56.810 -32.596 1.00 77.18  ? 316  GLN B C   1 
ATOM   5448 O O   . GLN B 1 316 ? 23.482  -57.155 -31.674 1.00 75.74  ? 316  GLN B O   1 
ATOM   5449 C CB  . GLN B 1 316 ? 23.758  -54.312 -32.969 1.00 75.74  ? 316  GLN B CB  1 
ATOM   5450 C CG  . GLN B 1 316 ? 24.143  -52.926 -32.418 1.00 85.92  ? 316  GLN B CG  1 
ATOM   5451 C CD  . GLN B 1 316 ? 23.276  -51.784 -32.876 1.00 82.34  ? 316  GLN B CD  1 
ATOM   5452 O OE1 . GLN B 1 316 ? 22.062  -51.785 -32.656 1.00 65.50  ? 316  GLN B OE1 1 
ATOM   5453 N NE2 . GLN B 1 316 ? 23.905  -50.750 -33.466 1.00 69.57  ? 316  GLN B NE2 1 
ATOM   5454 N N   . HIS B 1 317 ? 24.598  -57.661 -33.581 1.00 74.45  ? 317  HIS B N   1 
ATOM   5455 C CA  . HIS B 1 317 ? 24.082  -59.037 -33.697 1.00 73.84  ? 317  HIS B CA  1 
ATOM   5456 C C   . HIS B 1 317 ? 25.090  -60.099 -33.283 1.00 75.54  ? 317  HIS B C   1 
ATOM   5457 O O   . HIS B 1 317 ? 24.970  -61.253 -33.694 1.00 73.92  ? 317  HIS B O   1 
ATOM   5458 C CB  . HIS B 1 317 ? 23.531  -59.297 -35.104 1.00 75.11  ? 317  HIS B CB  1 
ATOM   5459 C CG  . HIS B 1 317 ? 22.731  -58.145 -35.610 1.00 79.39  ? 317  HIS B CG  1 
ATOM   5460 N ND1 . HIS B 1 317 ? 21.455  -57.915 -35.161 1.00 81.40  ? 317  HIS B ND1 1 
ATOM   5461 C CD2 . HIS B 1 317 ? 23.103  -57.120 -36.419 1.00 82.46  ? 317  HIS B CD2 1 
ATOM   5462 C CE1 . HIS B 1 317 ? 21.064  -56.792 -35.741 1.00 81.50  ? 317  HIS B CE1 1 
ATOM   5463 N NE2 . HIS B 1 317 ? 22.021  -56.279 -36.511 1.00 82.19  ? 317  HIS B NE2 1 
ATOM   5464 N N   . GLY B 1 318 ? 26.047  -59.711 -32.441 1.00 73.19  ? 318  GLY B N   1 
ATOM   5465 C CA  . GLY B 1 318 ? 27.076  -60.606 -31.928 1.00 73.99  ? 318  GLY B CA  1 
ATOM   5466 C C   . GLY B 1 318 ? 28.238  -60.896 -32.867 1.00 80.50  ? 318  GLY B C   1 
ATOM   5467 O O   . GLY B 1 318 ? 29.287  -61.381 -32.411 1.00 81.88  ? 318  GLY B O   1 
ATOM   5468 N N   . THR B 1 319 ? 28.076  -60.595 -34.193 1.00 74.87  ? 319  THR B N   1 
ATOM   5469 C CA  . THR B 1 319 ? 29.108  -60.797 -35.214 1.00 72.62  ? 319  THR B CA  1 
ATOM   5470 C C   . THR B 1 319 ? 30.271  -59.838 -34.961 1.00 75.95  ? 319  THR B C   1 
ATOM   5471 O O   . THR B 1 319 ? 30.117  -58.823 -34.285 1.00 74.88  ? 319  THR B O   1 
ATOM   5472 C CB  . THR B 1 319 ? 28.565  -60.679 -36.645 1.00 71.51  ? 319  THR B CB  1 
ATOM   5473 O OG1 . THR B 1 319 ? 28.534  -59.312 -37.030 1.00 75.19  ? 319  THR B OG1 1 
ATOM   5474 C CG2 . THR B 1 319 ? 27.206  -61.332 -36.839 1.00 65.94  ? 319  THR B CG2 1 
ATOM   5475 N N   . ILE B 1 320 ? 31.444  -60.184 -35.475 1.00 72.28  ? 320  ILE B N   1 
ATOM   5476 C CA  . ILE B 1 320 ? 32.633  -59.364 -35.300 1.00 70.53  ? 320  ILE B CA  1 
ATOM   5477 C C   . ILE B 1 320 ? 33.205  -58.967 -36.638 1.00 72.37  ? 320  ILE B C   1 
ATOM   5478 O O   . ILE B 1 320 ? 32.997  -59.662 -37.642 1.00 71.56  ? 320  ILE B O   1 
ATOM   5479 C CB  . ILE B 1 320 ? 33.683  -60.023 -34.383 1.00 73.03  ? 320  ILE B CB  1 
ATOM   5480 C CG1 . ILE B 1 320 ? 34.147  -61.406 -34.898 1.00 72.23  ? 320  ILE B CG1 1 
ATOM   5481 C CG2 . ILE B 1 320 ? 33.175  -60.097 -32.961 1.00 74.84  ? 320  ILE B CG2 1 
ATOM   5482 C CD1 . ILE B 1 320 ? 35.543  -61.416 -35.316 1.00 69.60  ? 320  ILE B CD1 1 
ATOM   5483 N N   . VAL B 1 321 ? 33.931  -57.839 -36.641 1.00 66.98  ? 321  VAL B N   1 
ATOM   5484 C CA  . VAL B 1 321 ? 34.568  -57.269 -37.828 1.00 64.96  ? 321  VAL B CA  1 
ATOM   5485 C C   . VAL B 1 321 ? 36.040  -56.987 -37.546 1.00 65.27  ? 321  VAL B C   1 
ATOM   5486 O O   . VAL B 1 321 ? 36.386  -56.409 -36.513 1.00 62.53  ? 321  VAL B O   1 
ATOM   5487 C CB  . VAL B 1 321 ? 33.800  -56.027 -38.411 1.00 67.95  ? 321  VAL B CB  1 
ATOM   5488 C CG1 . VAL B 1 321 ? 34.386  -55.574 -39.757 1.00 67.33  ? 321  VAL B CG1 1 
ATOM   5489 C CG2 . VAL B 1 321 ? 32.321  -56.349 -38.599 1.00 67.51  ? 321  VAL B CG2 1 
ATOM   5490 N N   . ILE B 1 322 ? 36.894  -57.392 -38.490 1.00 61.87  ? 322  ILE B N   1 
ATOM   5491 C CA  . ILE B 1 322 ? 38.328  -57.200 -38.421 1.00 61.48  ? 322  ILE B CA  1 
ATOM   5492 C C   . ILE B 1 322 ? 38.842  -56.588 -39.726 1.00 64.08  ? 322  ILE B C   1 
ATOM   5493 O O   . ILE B 1 322 ? 38.485  -57.029 -40.819 1.00 60.95  ? 322  ILE B O   1 
ATOM   5494 C CB  . ILE B 1 322 ? 39.028  -58.547 -38.020 1.00 64.94  ? 322  ILE B CB  1 
ATOM   5495 C CG1 . ILE B 1 322 ? 40.562  -58.413 -37.882 1.00 66.00  ? 322  ILE B CG1 1 
ATOM   5496 C CG2 . ILE B 1 322 ? 38.660  -59.719 -38.928 1.00 65.05  ? 322  ILE B CG2 1 
ATOM   5497 C CD1 . ILE B 1 322 ? 41.027  -57.755 -36.590 1.00 77.47  ? 322  ILE B CD1 1 
ATOM   5498 N N   . ARG B 1 323 ? 39.690  -55.588 -39.595 1.00 63.87  ? 323  ARG B N   1 
ATOM   5499 C CA  . ARG B 1 323 ? 40.304  -54.973 -40.757 1.00 65.63  ? 323  ARG B CA  1 
ATOM   5500 C C   . ARG B 1 323 ? 41.798  -55.246 -40.665 1.00 71.14  ? 323  ARG B C   1 
ATOM   5501 O O   . ARG B 1 323 ? 42.429  -54.920 -39.642 1.00 67.87  ? 323  ARG B O   1 
ATOM   5502 C CB  . ARG B 1 323 ? 39.934  -53.478 -40.876 1.00 69.18  ? 323  ARG B CB  1 
ATOM   5503 C CG  . ARG B 1 323 ? 40.750  -52.651 -41.879 1.00 81.14  ? 323  ARG B CG  1 
ATOM   5504 C CD  . ARG B 1 323 ? 39.969  -52.135 -43.084 1.00 90.46  ? 323  ARG B CD  1 
ATOM   5505 N NE  . ARG B 1 323 ? 38.818  -51.286 -42.742 1.00 90.27  ? 323  ARG B NE  1 
ATOM   5506 C CZ  . ARG B 1 323 ? 38.868  -49.974 -42.510 1.00 93.41  ? 323  ARG B CZ  1 
ATOM   5507 N NH1 . ARG B 1 323 ? 40.031  -49.326 -42.554 1.00 78.66  ? 323  ARG B NH1 1 
ATOM   5508 N NH2 . ARG B 1 323 ? 37.762  -49.305 -42.221 1.00 66.17  ? 323  ARG B NH2 1 
ATOM   5509 N N   . VAL B 1 324 ? 42.336  -55.927 -41.724 1.00 71.90  ? 324  VAL B N   1 
ATOM   5510 C CA  . VAL B 1 324 ? 43.742  -56.379 -41.814 1.00 72.74  ? 324  VAL B CA  1 
ATOM   5511 C C   . VAL B 1 324 ? 44.453  -56.028 -43.125 1.00 83.35  ? 324  VAL B C   1 
ATOM   5512 O O   . VAL B 1 324 ? 43.831  -56.064 -44.187 1.00 82.68  ? 324  VAL B O   1 
ATOM   5513 C CB  . VAL B 1 324 ? 43.879  -57.901 -41.539 1.00 74.33  ? 324  VAL B CB  1 
ATOM   5514 C CG1 . VAL B 1 324 ? 43.723  -58.214 -40.057 1.00 74.12  ? 324  VAL B CG1 1 
ATOM   5515 C CG2 . VAL B 1 324 ? 42.915  -58.726 -42.387 1.00 73.28  ? 324  VAL B CG2 1 
ATOM   5516 N N   . GLN B 1 325 ? 45.780  -55.773 -43.049 1.00 85.44  ? 325  GLN B N   1 
ATOM   5517 C CA  . GLN B 1 325 ? 46.635  -55.495 -44.217 1.00 87.51  ? 325  GLN B CA  1 
ATOM   5518 C C   . GLN B 1 325 ? 47.639  -56.639 -44.451 1.00 97.91  ? 325  GLN B C   1 
ATOM   5519 O O   . GLN B 1 325 ? 48.271  -57.091 -43.494 1.00 97.06  ? 325  GLN B O   1 
ATOM   5520 C CB  . GLN B 1 325 ? 47.379  -54.171 -44.040 1.00 88.14  ? 325  GLN B CB  1 
ATOM   5521 C CG  . GLN B 1 325 ? 47.299  -53.276 -45.265 1.00 89.07  ? 325  GLN B CG  1 
ATOM   5522 C CD  . GLN B 1 325 ? 48.306  -52.138 -45.231 1.00 93.41  ? 325  GLN B CD  1 
ATOM   5523 O OE1 . GLN B 1 325 ? 48.916  -51.814 -44.203 1.00 66.74  ? 325  GLN B OE1 1 
ATOM   5524 N NE2 . GLN B 1 325 ? 48.535  -51.520 -46.382 1.00 99.94  ? 325  GLN B NE2 1 
ATOM   5525 N N   . TYR B 1 326 ? 47.766  -57.117 -45.712 1.00 100.21 ? 326  TYR B N   1 
ATOM   5526 C CA  . TYR B 1 326 ? 48.688  -58.209 -46.081 1.00 102.34 ? 326  TYR B CA  1 
ATOM   5527 C C   . TYR B 1 326 ? 50.088  -57.662 -46.306 1.00 109.02 ? 326  TYR B C   1 
ATOM   5528 O O   . TYR B 1 326 ? 50.260  -56.647 -46.991 1.00 108.09 ? 326  TYR B O   1 
ATOM   5529 C CB  . TYR B 1 326 ? 48.193  -58.976 -47.327 1.00 104.07 ? 326  TYR B CB  1 
ATOM   5530 C CG  . TYR B 1 326 ? 49.041  -60.156 -47.783 1.00 106.64 ? 326  TYR B CG  1 
ATOM   5531 C CD1 . TYR B 1 326 ? 49.373  -61.188 -46.904 1.00 108.35 ? 326  TYR B CD1 1 
ATOM   5532 C CD2 . TYR B 1 326 ? 49.396  -60.307 -49.123 1.00 108.01 ? 326  TYR B CD2 1 
ATOM   5533 C CE1 . TYR B 1 326 ? 50.060  -62.321 -47.343 1.00 109.24 ? 326  TYR B CE1 1 
ATOM   5534 C CE2 . TYR B 1 326 ? 50.093  -61.431 -49.571 1.00 108.88 ? 326  TYR B CE2 1 
ATOM   5535 C CZ  . TYR B 1 326 ? 50.425  -62.435 -48.677 1.00 116.09 ? 326  TYR B CZ  1 
ATOM   5536 O OH  . TYR B 1 326 ? 51.146  -63.519 -49.125 1.00 116.33 ? 326  TYR B OH  1 
ATOM   5537 N N   . GLU B 1 327 ? 51.086  -58.337 -45.721 1.00 107.60 ? 327  GLU B N   1 
ATOM   5538 C CA  . GLU B 1 327 ? 52.482  -57.917 -45.820 1.00 107.91 ? 327  GLU B CA  1 
ATOM   5539 C C   . GLU B 1 327 ? 53.361  -58.901 -46.606 1.00 113.57 ? 327  GLU B C   1 
ATOM   5540 O O   . GLU B 1 327 ? 54.586  -58.740 -46.632 1.00 113.34 ? 327  GLU B O   1 
ATOM   5541 C CB  . GLU B 1 327 ? 53.043  -57.626 -44.424 1.00 108.97 ? 327  GLU B CB  1 
ATOM   5542 C CG  . GLU B 1 327 ? 52.376  -56.421 -43.791 1.00 115.68 ? 327  GLU B CG  1 
ATOM   5543 C CD  . GLU B 1 327 ? 52.712  -56.208 -42.334 1.00 124.22 ? 327  GLU B CD  1 
ATOM   5544 O OE1 . GLU B 1 327 ? 52.362  -57.076 -41.502 1.00 116.17 ? 327  GLU B OE1 1 
ATOM   5545 O OE2 . GLU B 1 327 ? 53.281  -55.142 -42.015 1.00 110.73 ? 327  GLU B OE2 1 
ATOM   5546 N N   . GLY B 1 328 ? 52.717  -59.869 -47.270 1.00 110.80 ? 328  GLY B N   1 
ATOM   5547 C CA  . GLY B 1 328 ? 53.360  -60.902 -48.075 1.00 110.68 ? 328  GLY B CA  1 
ATOM   5548 C C   . GLY B 1 328 ? 53.520  -60.498 -49.522 1.00 115.57 ? 328  GLY B C   1 
ATOM   5549 O O   . GLY B 1 328 ? 53.551  -59.298 -49.815 1.00 114.88 ? 328  GLY B O   1 
ATOM   5550 N N   . ASP B 1 329 ? 53.635  -61.485 -50.445 1.00 113.49 ? 329  ASP B N   1 
ATOM   5551 C CA  . ASP B 1 329 ? 53.877  -61.188 -51.866 1.00 113.70 ? 329  ASP B CA  1 
ATOM   5552 C C   . ASP B 1 329 ? 52.944  -61.885 -52.889 1.00 116.76 ? 329  ASP B C   1 
ATOM   5553 O O   . ASP B 1 329 ? 52.826  -61.392 -54.018 1.00 116.39 ? 329  ASP B O   1 
ATOM   5554 C CB  . ASP B 1 329 ? 55.350  -61.471 -52.244 1.00 115.86 ? 329  ASP B CB  1 
ATOM   5555 C CG  . ASP B 1 329 ? 56.394  -60.717 -51.430 1.00 127.37 ? 329  ASP B CG  1 
ATOM   5556 O OD1 . ASP B 1 329 ? 56.711  -59.550 -51.788 1.00 132.65 ? 329  ASP B OD1 1 
ATOM   5557 O OD2 . ASP B 1 329 ? 56.910  -61.296 -50.445 1.00 127.90 ? 329  ASP B OD2 1 
ATOM   5558 N N   . GLY B 1 330 ? 52.313  -62.994 -52.501 1.00 112.22 ? 330  GLY B N   1 
ATOM   5559 C CA  . GLY B 1 330 ? 51.445  -63.791 -53.370 1.00 111.67 ? 330  GLY B CA  1 
ATOM   5560 C C   . GLY B 1 330 ? 50.244  -63.139 -54.046 1.00 114.12 ? 330  GLY B C   1 
ATOM   5561 O O   . GLY B 1 330 ? 49.756  -63.675 -55.050 1.00 114.02 ? 330  GLY B O   1 
ATOM   5562 N N   . SER B 1 331 ? 49.722  -62.017 -53.469 1.00 108.40 ? 331  SER B N   1 
ATOM   5563 C CA  . SER B 1 331 ? 48.543  -61.258 -53.916 1.00 106.71 ? 331  SER B CA  1 
ATOM   5564 C C   . SER B 1 331 ? 48.409  -61.099 -55.458 1.00 108.31 ? 331  SER B C   1 
ATOM   5565 O O   . SER B 1 331 ? 49.411  -60.796 -56.105 1.00 107.33 ? 331  SER B O   1 
ATOM   5566 C CB  . SER B 1 331 ? 48.506  -59.900 -53.235 1.00 109.13 ? 331  SER B CB  1 
ATOM   5567 O OG  . SER B 1 331 ? 49.643  -59.161 -53.634 1.00 115.34 ? 331  SER B OG  1 
ATOM   5568 N N   . PRO B 1 332 ? 47.216  -61.342 -56.069 1.00 104.08 ? 332  PRO B N   1 
ATOM   5569 C CA  . PRO B 1 332 ? 45.938  -61.703 -55.433 1.00 103.96 ? 332  PRO B CA  1 
ATOM   5570 C C   . PRO B 1 332 ? 45.914  -63.110 -54.852 1.00 108.59 ? 332  PRO B C   1 
ATOM   5571 O O   . PRO B 1 332 ? 46.264  -64.079 -55.538 1.00 108.79 ? 332  PRO B O   1 
ATOM   5572 C CB  . PRO B 1 332 ? 44.908  -61.472 -56.546 1.00 105.50 ? 332  PRO B CB  1 
ATOM   5573 C CG  . PRO B 1 332 ? 45.655  -61.743 -57.796 1.00 109.78 ? 332  PRO B CG  1 
ATOM   5574 C CD  . PRO B 1 332 ? 47.059  -61.227 -57.533 1.00 105.46 ? 332  PRO B CD  1 
ATOM   5575 N N   . CYS B 1 333 ? 45.553  -63.204 -53.554 1.00 104.25 ? 333  CYS B N   1 
ATOM   5576 C CA  . CYS B 1 333 ? 45.505  -64.477 -52.835 1.00 103.32 ? 333  CYS B CA  1 
ATOM   5577 C C   . CYS B 1 333 ? 44.360  -64.564 -51.802 1.00 103.12 ? 333  CYS B C   1 
ATOM   5578 O O   . CYS B 1 333 ? 43.892  -63.533 -51.317 1.00 103.14 ? 333  CYS B O   1 
ATOM   5579 C CB  . CYS B 1 333 ? 46.864  -64.801 -52.208 1.00 103.93 ? 333  CYS B CB  1 
ATOM   5580 S SG  . CYS B 1 333 ? 47.468  -63.566 -51.023 1.00 108.15 ? 333  CYS B SG  1 
ATOM   5581 N N   . LYS B 1 334 ? 43.924  -65.799 -51.464 1.00 95.83  ? 334  LYS B N   1 
ATOM   5582 C CA  . LYS B 1 334 ? 42.902  -66.065 -50.438 1.00 93.73  ? 334  LYS B CA  1 
ATOM   5583 C C   . LYS B 1 334 ? 43.522  -65.870 -49.027 1.00 94.21  ? 334  LYS B C   1 
ATOM   5584 O O   . LYS B 1 334 ? 44.522  -66.529 -48.697 1.00 92.61  ? 334  LYS B O   1 
ATOM   5585 C CB  . LYS B 1 334 ? 42.380  -67.520 -50.525 1.00 95.02  ? 334  LYS B CB  1 
ATOM   5586 C CG  . LYS B 1 334 ? 41.561  -67.924 -51.747 1.00 91.20  ? 334  LYS B CG  1 
ATOM   5587 C CD  . LYS B 1 334 ? 41.113  -69.375 -51.541 1.00 89.06  ? 334  LYS B CD  1 
ATOM   5588 C CE  . LYS B 1 334 ? 40.503  -70.029 -52.753 1.00 86.95  ? 334  LYS B CE  1 
ATOM   5589 N NZ  . LYS B 1 334 ? 39.816  -71.311 -52.411 1.00 90.77  ? 334  LYS B NZ  1 
ATOM   5590 N N   . ILE B 1 335 ? 42.922  -64.993 -48.193 1.00 89.58  ? 335  ILE B N   1 
ATOM   5591 C CA  . ILE B 1 335 ? 43.376  -64.791 -46.812 1.00 88.95  ? 335  ILE B CA  1 
ATOM   5592 C C   . ILE B 1 335 ? 42.930  -66.016 -46.009 1.00 93.17  ? 335  ILE B C   1 
ATOM   5593 O O   . ILE B 1 335 ? 41.731  -66.337 -46.032 1.00 92.28  ? 335  ILE B O   1 
ATOM   5594 C CB  . ILE B 1 335 ? 42.778  -63.541 -46.143 1.00 91.70  ? 335  ILE B CB  1 
ATOM   5595 C CG1 . ILE B 1 335 ? 42.855  -62.309 -47.029 1.00 92.29  ? 335  ILE B CG1 1 
ATOM   5596 C CG2 . ILE B 1 335 ? 43.420  -63.310 -44.785 1.00 92.50  ? 335  ILE B CG2 1 
ATOM   5597 C CD1 . ILE B 1 335 ? 41.673  -61.381 -46.879 1.00 98.93  ? 335  ILE B CD1 1 
ATOM   5598 N N   . PRO B 1 336 ? 43.849  -66.711 -45.287 1.00 89.32  ? 336  PRO B N   1 
ATOM   5599 C CA  . PRO B 1 336 ? 43.414  -67.865 -44.484 1.00 88.00  ? 336  PRO B CA  1 
ATOM   5600 C C   . PRO B 1 336 ? 42.672  -67.359 -43.245 1.00 88.11  ? 336  PRO B C   1 
ATOM   5601 O O   . PRO B 1 336 ? 43.128  -66.428 -42.573 1.00 86.03  ? 336  PRO B O   1 
ATOM   5602 C CB  . PRO B 1 336 ? 44.736  -68.583 -44.131 1.00 89.91  ? 336  PRO B CB  1 
ATOM   5603 C CG  . PRO B 1 336 ? 45.809  -67.893 -44.950 1.00 94.71  ? 336  PRO B CG  1 
ATOM   5604 C CD  . PRO B 1 336 ? 45.306  -66.499 -45.155 1.00 90.59  ? 336  PRO B CD  1 
ATOM   5605 N N   . PHE B 1 337 ? 41.499  -67.937 -42.979 1.00 83.72  ? 337  PHE B N   1 
ATOM   5606 C CA  . PHE B 1 337 ? 40.702  -67.505 -41.837 1.00 82.94  ? 337  PHE B CA  1 
ATOM   5607 C C   . PHE B 1 337 ? 40.025  -68.668 -41.154 1.00 89.06  ? 337  PHE B C   1 
ATOM   5608 O O   . PHE B 1 337 ? 39.451  -69.536 -41.824 1.00 87.52  ? 337  PHE B O   1 
ATOM   5609 C CB  . PHE B 1 337 ? 39.656  -66.472 -42.272 1.00 83.55  ? 337  PHE B CB  1 
ATOM   5610 C CG  . PHE B 1 337 ? 39.026  -65.701 -41.140 1.00 83.80  ? 337  PHE B CG  1 
ATOM   5611 C CD1 . PHE B 1 337 ? 39.644  -64.567 -40.618 1.00 84.45  ? 337  PHE B CD1 1 
ATOM   5612 C CD2 . PHE B 1 337 ? 37.803  -66.088 -40.608 1.00 86.23  ? 337  PHE B CD2 1 
ATOM   5613 C CE1 . PHE B 1 337 ? 39.056  -63.840 -39.578 1.00 86.76  ? 337  PHE B CE1 1 
ATOM   5614 C CE2 . PHE B 1 337 ? 37.220  -65.367 -39.560 1.00 87.17  ? 337  PHE B CE2 1 
ATOM   5615 C CZ  . PHE B 1 337 ? 37.852  -64.243 -39.054 1.00 85.55  ? 337  PHE B CZ  1 
ATOM   5616 N N   . GLU B 1 338 ? 40.077  -68.656 -39.802 1.00 88.30  ? 338  GLU B N   1 
ATOM   5617 C CA  . GLU B 1 338 ? 39.453  -69.659 -38.942 1.00 89.14  ? 338  GLU B CA  1 
ATOM   5618 C C   . GLU B 1 338 ? 39.128  -69.139 -37.539 1.00 94.83  ? 338  GLU B C   1 
ATOM   5619 O O   . GLU B 1 338 ? 39.843  -68.300 -36.983 1.00 92.52  ? 338  GLU B O   1 
ATOM   5620 C CB  . GLU B 1 338 ? 40.309  -70.923 -38.867 1.00 90.82  ? 338  GLU B CB  1 
ATOM   5621 C CG  . GLU B 1 338 ? 39.463  -72.176 -38.881 1.00 105.78 ? 338  GLU B CG  1 
ATOM   5622 C CD  . GLU B 1 338 ? 39.999  -73.325 -39.713 1.00 138.13 ? 338  GLU B CD  1 
ATOM   5623 O OE1 . GLU B 1 338 ? 40.726  -74.179 -39.151 1.00 143.32 ? 338  GLU B OE1 1 
ATOM   5624 O OE2 . GLU B 1 338 ? 39.589  -73.438 -40.893 1.00 128.46 ? 338  GLU B OE2 1 
ATOM   5625 N N   . ILE B 1 339 ? 37.999  -69.615 -36.999 1.00 96.06  ? 339  ILE B N   1 
ATOM   5626 C CA  . ILE B 1 339 ? 37.528  -69.324 -35.640 1.00 98.48  ? 339  ILE B CA  1 
ATOM   5627 C C   . ILE B 1 339 ? 37.414  -70.691 -34.950 1.00 107.47 ? 339  ILE B C   1 
ATOM   5628 O O   . ILE B 1 339 ? 36.310  -71.200 -34.746 1.00 107.73 ? 339  ILE B O   1 
ATOM   5629 C CB  . ILE B 1 339 ? 36.185  -68.517 -35.534 1.00 101.58 ? 339  ILE B CB  1 
ATOM   5630 C CG1 . ILE B 1 339 ? 36.003  -67.484 -36.658 1.00 101.79 ? 339  ILE B CG1 1 
ATOM   5631 C CG2 . ILE B 1 339 ? 36.053  -67.864 -34.149 1.00 101.68 ? 339  ILE B CG2 1 
ATOM   5632 C CD1 . ILE B 1 339 ? 34.560  -67.167 -36.929 1.00 105.23 ? 339  ILE B CD1 1 
ATOM   5633 N N   . THR B 1 340 ? 38.563  -71.306 -34.645 1.00 106.61 ? 340  THR B N   1 
ATOM   5634 C CA  . THR B 1 340 ? 38.640  -72.616 -33.981 1.00 107.19 ? 340  THR B CA  1 
ATOM   5635 C C   . THR B 1 340 ? 38.489  -72.451 -32.453 1.00 111.90 ? 340  THR B C   1 
ATOM   5636 O O   . THR B 1 340 ? 38.366  -71.323 -31.961 1.00 112.13 ? 340  THR B O   1 
ATOM   5637 C CB  . THR B 1 340 ? 39.988  -73.304 -34.318 1.00 115.13 ? 340  THR B CB  1 
ATOM   5638 O OG1 . THR B 1 340 ? 41.041  -72.338 -34.260 1.00 115.17 ? 340  THR B OG1 1 
ATOM   5639 C CG2 . THR B 1 340 ? 39.980  -74.015 -35.666 1.00 112.46 ? 340  THR B CG2 1 
ATOM   5640 N N   . ASP B 1 341 ? 38.546  -73.572 -31.701 1.00 107.75 ? 341  ASP B N   1 
ATOM   5641 C CA  . ASP B 1 341 ? 38.493  -73.567 -30.233 1.00 106.75 ? 341  ASP B CA  1 
ATOM   5642 C C   . ASP B 1 341 ? 39.777  -72.935 -29.602 1.00 110.06 ? 341  ASP B C   1 
ATOM   5643 O O   . ASP B 1 341 ? 40.612  -72.337 -30.308 1.00 108.29 ? 341  ASP B O   1 
ATOM   5644 C CB  . ASP B 1 341 ? 38.169  -74.982 -29.645 1.00 107.53 ? 341  ASP B CB  1 
ATOM   5645 C CG  . ASP B 1 341 ? 38.567  -76.213 -30.465 1.00 105.81 ? 341  ASP B CG  1 
ATOM   5646 O OD1 . ASP B 1 341 ? 39.566  -76.141 -31.200 1.00 104.02 ? 341  ASP B OD1 1 
ATOM   5647 O OD2 . ASP B 1 341 ? 37.914  -77.264 -30.313 1.00 106.26 ? 341  ASP B OD2 1 
ATOM   5648 N N   . LEU B 1 342 ? 39.897  -73.042 -28.265 1.00 106.90 ? 342  LEU B N   1 
ATOM   5649 C CA  . LEU B 1 342 ? 41.039  -72.533 -27.504 1.00 106.57 ? 342  LEU B CA  1 
ATOM   5650 C C   . LEU B 1 342 ? 42.215  -73.496 -27.713 1.00 111.59 ? 342  LEU B C   1 
ATOM   5651 O O   . LEU B 1 342 ? 43.381  -73.079 -27.757 1.00 111.81 ? 342  LEU B O   1 
ATOM   5652 C CB  . LEU B 1 342 ? 40.671  -72.413 -26.014 1.00 106.07 ? 342  LEU B CB  1 
ATOM   5653 C CG  . LEU B 1 342 ? 39.576  -71.395 -25.671 1.00 109.31 ? 342  LEU B CG  1 
ATOM   5654 C CD1 . LEU B 1 342 ? 38.228  -72.080 -25.443 1.00 109.04 ? 342  LEU B CD1 1 
ATOM   5655 C CD2 . LEU B 1 342 ? 39.969  -70.579 -24.471 1.00 110.41 ? 342  LEU B CD2 1 
ATOM   5656 N N   . GLU B 1 343 ? 41.872  -74.788 -27.893 1.00 107.43 ? 343  GLU B N   1 
ATOM   5657 C CA  . GLU B 1 343 ? 42.778  -75.895 -28.161 1.00 106.87 ? 343  GLU B CA  1 
ATOM   5658 C C   . GLU B 1 343 ? 43.445  -75.759 -29.547 1.00 109.98 ? 343  GLU B C   1 
ATOM   5659 O O   . GLU B 1 343 ? 44.655  -75.958 -29.651 1.00 110.43 ? 343  GLU B O   1 
ATOM   5660 C CB  . GLU B 1 343 ? 42.004  -77.225 -28.094 1.00 108.18 ? 343  GLU B CB  1 
ATOM   5661 C CG  . GLU B 1 343 ? 41.649  -77.675 -26.688 1.00 118.23 ? 343  GLU B CG  1 
ATOM   5662 C CD  . GLU B 1 343 ? 41.322  -79.151 -26.559 1.00 137.09 ? 343  GLU B CD  1 
ATOM   5663 O OE1 . GLU B 1 343 ? 40.642  -79.694 -27.461 1.00 139.05 ? 343  GLU B OE1 1 
ATOM   5664 O OE2 . GLU B 1 343 ? 41.755  -79.767 -25.555 1.00 109.93 ? 343  GLU B OE2 1 
ATOM   5665 N N   . LYS B 1 344 ? 42.637  -75.428 -30.596 1.00 104.13 ? 344  LYS B N   1 
ATOM   5666 C CA  . LYS B 1 344 ? 42.945  -75.286 -32.033 1.00 102.82 ? 344  LYS B CA  1 
ATOM   5667 C C   . LYS B 1 344 ? 42.435  -76.491 -32.835 1.00 106.46 ? 344  LYS B C   1 
ATOM   5668 O O   . LYS B 1 344 ? 42.604  -76.543 -34.061 1.00 105.14 ? 344  LYS B O   1 
ATOM   5669 C CB  . LYS B 1 344 ? 44.428  -75.006 -32.328 1.00 104.22 ? 344  LYS B CB  1 
ATOM   5670 C CG  . LYS B 1 344 ? 44.873  -73.574 -32.026 1.00 106.70 ? 344  LYS B CG  1 
ATOM   5671 C CD  . LYS B 1 344 ? 46.219  -73.253 -32.677 1.00 104.90 ? 344  LYS B CD  1 
ATOM   5672 C CE  . LYS B 1 344 ? 46.140  -73.182 -34.187 1.00 98.65  ? 344  LYS B CE  1 
ATOM   5673 N NZ  . LYS B 1 344 ? 47.478  -72.989 -34.800 1.00 105.43 ? 344  LYS B NZ  1 
ATOM   5674 N N   . ARG B 1 345 ? 41.786  -77.440 -32.123 1.00 103.97 ? 345  ARG B N   1 
ATOM   5675 C CA  . ARG B 1 345 ? 41.198  -78.688 -32.612 1.00 104.31 ? 345  ARG B CA  1 
ATOM   5676 C C   . ARG B 1 345 ? 40.301  -78.491 -33.831 1.00 108.52 ? 345  ARG B C   1 
ATOM   5677 O O   . ARG B 1 345 ? 40.811  -78.498 -34.952 1.00 106.59 ? 345  ARG B O   1 
ATOM   5678 C CB  . ARG B 1 345 ? 40.465  -79.419 -31.460 1.00 105.77 ? 345  ARG B CB  1 
ATOM   5679 C CG  . ARG B 1 345 ? 40.432  -80.950 -31.586 1.00 119.91 ? 345  ARG B CG  1 
ATOM   5680 C CD  . ARG B 1 345 ? 41.746  -81.552 -32.112 1.00 130.64 ? 345  ARG B CD  1 
ATOM   5681 N NE  . ARG B 1 345 ? 42.481  -82.349 -31.124 1.00 131.38 ? 345  ARG B NE  1 
ATOM   5682 C CZ  . ARG B 1 345 ? 43.804  -82.499 -31.112 1.00 135.99 ? 345  ARG B CZ  1 
ATOM   5683 N NH1 . ARG B 1 345 ? 44.560  -81.877 -32.013 1.00 119.43 ? 345  ARG B NH1 1 
ATOM   5684 N NH2 . ARG B 1 345 ? 44.384  -83.254 -30.189 1.00 116.60 ? 345  ARG B NH2 1 
ATOM   5685 N N   . HIS B 1 346 ? 38.979  -78.285 -33.618 1.00 107.53 ? 346  HIS B N   1 
ATOM   5686 C CA  . HIS B 1 346 ? 38.004  -78.046 -34.698 1.00 107.97 ? 346  HIS B CA  1 
ATOM   5687 C C   . HIS B 1 346 ? 37.559  -76.574 -34.846 1.00 111.52 ? 346  HIS B C   1 
ATOM   5688 O O   . HIS B 1 346 ? 37.674  -75.768 -33.923 1.00 110.26 ? 346  HIS B O   1 
ATOM   5689 C CB  . HIS B 1 346 ? 36.745  -78.968 -34.631 1.00 108.81 ? 346  HIS B CB  1 
ATOM   5690 C CG  . HIS B 1 346 ? 36.432  -79.614 -33.311 1.00 112.21 ? 346  HIS B CG  1 
ATOM   5691 N ND1 . HIS B 1 346 ? 36.687  -78.984 -32.102 1.00 113.99 ? 346  HIS B ND1 1 
ATOM   5692 C CD2 . HIS B 1 346 ? 35.827  -80.799 -33.062 1.00 113.85 ? 346  HIS B CD2 1 
ATOM   5693 C CE1 . HIS B 1 346 ? 36.260  -79.816 -31.165 1.00 113.36 ? 346  HIS B CE1 1 
ATOM   5694 N NE2 . HIS B 1 346 ? 35.734  -80.920 -31.694 1.00 113.62 ? 346  HIS B NE2 1 
ATOM   5695 N N   . VAL B 1 347 ? 37.051  -76.256 -36.046 1.00 108.70 ? 347  VAL B N   1 
ATOM   5696 C CA  . VAL B 1 347 ? 36.465  -74.979 -36.474 1.00 108.08 ? 347  VAL B CA  1 
ATOM   5697 C C   . VAL B 1 347 ? 35.176  -74.748 -35.638 1.00 110.27 ? 347  VAL B C   1 
ATOM   5698 O O   . VAL B 1 347 ? 34.475  -75.722 -35.325 1.00 110.64 ? 347  VAL B O   1 
ATOM   5699 C CB  . VAL B 1 347 ? 36.180  -74.991 -38.018 1.00 111.82 ? 347  VAL B CB  1 
ATOM   5700 C CG1 . VAL B 1 347 ? 37.456  -75.218 -38.816 1.00 111.38 ? 347  VAL B CG1 1 
ATOM   5701 C CG2 . VAL B 1 347 ? 35.131  -76.041 -38.411 1.00 111.70 ? 347  VAL B CG2 1 
ATOM   5702 N N   . LEU B 1 348 ? 34.880  -73.496 -35.247 1.00 103.96 ? 348  LEU B N   1 
ATOM   5703 C CA  . LEU B 1 348 ? 33.675  -73.252 -34.450 1.00 102.37 ? 348  LEU B CA  1 
ATOM   5704 C C   . LEU B 1 348 ? 32.701  -72.271 -35.093 1.00 104.61 ? 348  LEU B C   1 
ATOM   5705 O O   . LEU B 1 348 ? 31.617  -72.696 -35.516 1.00 104.96 ? 348  LEU B O   1 
ATOM   5706 C CB  . LEU B 1 348 ? 34.003  -72.850 -33.008 1.00 101.90 ? 348  LEU B CB  1 
ATOM   5707 C CG  . LEU B 1 348 ? 34.009  -74.009 -32.044 1.00 105.64 ? 348  LEU B CG  1 
ATOM   5708 C CD1 . LEU B 1 348 ? 35.332  -74.665 -32.034 1.00 106.03 ? 348  LEU B CD1 1 
ATOM   5709 C CD2 . LEU B 1 348 ? 33.644  -73.570 -30.646 1.00 106.88 ? 348  LEU B CD2 1 
ATOM   5710 N N   . GLY B 1 349 ? 33.078  -70.993 -35.151 1.00 98.76  ? 349  GLY B N   1 
ATOM   5711 C CA  . GLY B 1 349 ? 32.248  -69.948 -35.739 1.00 97.49  ? 349  GLY B CA  1 
ATOM   5712 C C   . GLY B 1 349 ? 32.291  -69.939 -37.254 1.00 98.12  ? 349  GLY B C   1 
ATOM   5713 O O   . GLY B 1 349 ? 33.257  -70.455 -37.838 1.00 97.19  ? 349  GLY B O   1 
ATOM   5714 N N   . ARG B 1 350 ? 31.243  -69.329 -37.906 1.00 92.27  ? 350  ARG B N   1 
ATOM   5715 C CA  . ARG B 1 350 ? 31.164  -69.250 -39.378 1.00 90.29  ? 350  ARG B CA  1 
ATOM   5716 C C   . ARG B 1 350 ? 31.663  -67.915 -39.950 1.00 89.67  ? 350  ARG B C   1 
ATOM   5717 O O   . ARG B 1 350 ? 31.810  -66.929 -39.215 1.00 90.12  ? 350  ARG B O   1 
ATOM   5718 C CB  . ARG B 1 350 ? 29.746  -69.594 -39.910 1.00 89.83  ? 350  ARG B CB  1 
ATOM   5719 C CG  . ARG B 1 350 ? 28.642  -68.567 -39.633 1.00 95.87  ? 350  ARG B CG  1 
ATOM   5720 C CD  . ARG B 1 350 ? 27.438  -68.859 -40.505 1.00 102.59 ? 350  ARG B CD  1 
ATOM   5721 N NE  . ARG B 1 350 ? 26.333  -67.926 -40.266 1.00 113.55 ? 350  ARG B NE  1 
ATOM   5722 C CZ  . ARG B 1 350 ? 25.247  -68.201 -39.543 1.00 123.21 ? 350  ARG B CZ  1 
ATOM   5723 N NH1 . ARG B 1 350 ? 25.106  -69.395 -38.969 1.00 107.15 ? 350  ARG B NH1 1 
ATOM   5724 N NH2 . ARG B 1 350 ? 24.292  -67.285 -39.391 1.00 100.68 ? 350  ARG B NH2 1 
ATOM   5725 N N   . LEU B 1 351 ? 31.922  -67.902 -41.268 1.00 81.76  ? 351  LEU B N   1 
ATOM   5726 C CA  . LEU B 1 351 ? 32.328  -66.679 -41.954 1.00 79.45  ? 351  LEU B CA  1 
ATOM   5727 C C   . LEU B 1 351 ? 31.123  -66.025 -42.627 1.00 81.39  ? 351  LEU B C   1 
ATOM   5728 O O   . LEU B 1 351 ? 30.295  -66.720 -43.250 1.00 78.61  ? 351  LEU B O   1 
ATOM   5729 C CB  . LEU B 1 351 ? 33.427  -66.927 -43.016 1.00 78.28  ? 351  LEU B CB  1 
ATOM   5730 C CG  . LEU B 1 351 ? 34.710  -66.094 -42.902 1.00 80.53  ? 351  LEU B CG  1 
ATOM   5731 C CD1 . LEU B 1 351 ? 35.689  -66.501 -43.941 1.00 80.29  ? 351  LEU B CD1 1 
ATOM   5732 C CD2 . LEU B 1 351 ? 34.452  -64.628 -43.031 1.00 79.32  ? 351  LEU B CD2 1 
ATOM   5733 N N   . ILE B 1 352 ? 31.022  -64.680 -42.478 1.00 77.95  ? 352  ILE B N   1 
ATOM   5734 C CA  . ILE B 1 352 ? 30.002  -63.932 -43.201 1.00 77.47  ? 352  ILE B CA  1 
ATOM   5735 C C   . ILE B 1 352 ? 30.653  -63.499 -44.525 1.00 78.86  ? 352  ILE B C   1 
ATOM   5736 O O   . ILE B 1 352 ? 30.163  -63.912 -45.580 1.00 79.24  ? 352  ILE B O   1 
ATOM   5737 C CB  . ILE B 1 352 ? 29.337  -62.769 -42.416 1.00 80.93  ? 352  ILE B CB  1 
ATOM   5738 C CG1 . ILE B 1 352 ? 28.841  -63.209 -41.000 1.00 81.52  ? 352  ILE B CG1 1 
ATOM   5739 C CG2 . ILE B 1 352 ? 28.223  -62.110 -43.242 1.00 81.86  ? 352  ILE B CG2 1 
ATOM   5740 C CD1 . ILE B 1 352 ? 27.664  -64.218 -40.906 1.00 84.86  ? 352  ILE B CD1 1 
ATOM   5741 N N   . THR B 1 353 ? 31.791  -62.748 -44.471 1.00 71.15  ? 353  THR B N   1 
ATOM   5742 C CA  . THR B 1 353 ? 32.547  -62.321 -45.664 1.00 69.36  ? 353  THR B CA  1 
ATOM   5743 C C   . THR B 1 353 ? 33.307  -63.545 -46.238 1.00 67.36  ? 353  THR B C   1 
ATOM   5744 O O   . THR B 1 353 ? 34.532  -63.625 -46.113 1.00 65.22  ? 353  THR B O   1 
ATOM   5745 C CB  . THR B 1 353 ? 33.513  -61.153 -45.310 1.00 84.83  ? 353  THR B CB  1 
ATOM   5746 O OG1 . THR B 1 353 ? 32.886  -60.238 -44.412 1.00 89.35  ? 353  THR B OG1 1 
ATOM   5747 C CG2 . THR B 1 353 ? 34.048  -60.420 -46.544 1.00 82.45  ? 353  THR B CG2 1 
ATOM   5748 N N   . VAL B 1 354 ? 32.567  -64.500 -46.848 1.00 61.61  ? 354  VAL B N   1 
ATOM   5749 C CA  . VAL B 1 354 ? 33.103  -65.743 -47.411 1.00 60.84  ? 354  VAL B CA  1 
ATOM   5750 C C   . VAL B 1 354 ? 34.188  -65.487 -48.469 1.00 70.99  ? 354  VAL B C   1 
ATOM   5751 O O   . VAL B 1 354 ? 34.091  -64.512 -49.235 1.00 72.51  ? 354  VAL B O   1 
ATOM   5752 C CB  . VAL B 1 354 ? 32.044  -66.757 -47.933 1.00 61.92  ? 354  VAL B CB  1 
ATOM   5753 C CG1 . VAL B 1 354 ? 31.004  -67.102 -46.883 1.00 60.99  ? 354  VAL B CG1 1 
ATOM   5754 C CG2 . VAL B 1 354 ? 31.396  -66.298 -49.222 1.00 61.19  ? 354  VAL B CG2 1 
ATOM   5755 N N   . ASN B 1 355 ? 35.197  -66.408 -48.511 1.00 68.41  ? 355  ASN B N   1 
ATOM   5756 C CA  . ASN B 1 355 ? 36.367  -66.414 -49.395 1.00 68.47  ? 355  ASN B CA  1 
ATOM   5757 C C   . ASN B 1 355 ? 37.117  -65.076 -49.372 1.00 71.49  ? 355  ASN B C   1 
ATOM   5758 O O   . ASN B 1 355 ? 37.233  -64.442 -50.423 1.00 71.56  ? 355  ASN B O   1 
ATOM   5759 C CB  . ASN B 1 355 ? 35.998  -66.852 -50.813 1.00 72.07  ? 355  ASN B CB  1 
ATOM   5760 C CG  . ASN B 1 355 ? 37.181  -67.355 -51.602 1.00 110.73 ? 355  ASN B CG  1 
ATOM   5761 O OD1 . ASN B 1 355 ? 37.719  -68.444 -51.340 1.00 118.16 ? 355  ASN B OD1 1 
ATOM   5762 N ND2 . ASN B 1 355 ? 37.615  -66.565 -52.577 1.00 96.47  ? 355  ASN B ND2 1 
ATOM   5763 N N   . PRO B 1 356 ? 37.579  -64.596 -48.185 1.00 67.85  ? 356  PRO B N   1 
ATOM   5764 C CA  . PRO B 1 356 ? 38.256  -63.296 -48.138 1.00 68.81  ? 356  PRO B CA  1 
ATOM   5765 C C   . PRO B 1 356 ? 39.531  -63.301 -48.958 1.00 76.56  ? 356  PRO B C   1 
ATOM   5766 O O   . PRO B 1 356 ? 40.315  -64.234 -48.839 1.00 78.24  ? 356  PRO B O   1 
ATOM   5767 C CB  . PRO B 1 356 ? 38.502  -63.066 -46.641 1.00 70.59  ? 356  PRO B CB  1 
ATOM   5768 C CG  . PRO B 1 356 ? 38.476  -64.403 -46.034 1.00 74.90  ? 356  PRO B CG  1 
ATOM   5769 C CD  . PRO B 1 356 ? 37.513  -65.201 -46.843 1.00 69.95  ? 356  PRO B CD  1 
ATOM   5770 N N   . ILE B 1 357 ? 39.686  -62.321 -49.860 1.00 74.16  ? 357  ILE B N   1 
ATOM   5771 C CA  . ILE B 1 357 ? 40.847  -62.260 -50.747 1.00 74.29  ? 357  ILE B CA  1 
ATOM   5772 C C   . ILE B 1 357 ? 41.612  -60.918 -50.690 1.00 82.51  ? 357  ILE B C   1 
ATOM   5773 O O   . ILE B 1 357 ? 41.042  -59.889 -50.316 1.00 84.28  ? 357  ILE B O   1 
ATOM   5774 C CB  . ILE B 1 357 ? 40.458  -62.628 -52.204 1.00 76.50  ? 357  ILE B CB  1 
ATOM   5775 C CG1 . ILE B 1 357 ? 39.537  -61.584 -52.845 1.00 77.84  ? 357  ILE B CG1 1 
ATOM   5776 C CG2 . ILE B 1 357 ? 39.872  -64.036 -52.321 1.00 74.75  ? 357  ILE B CG2 1 
ATOM   5777 C CD1 . ILE B 1 357 ? 39.935  -61.163 -54.294 1.00 87.17  ? 357  ILE B CD1 1 
ATOM   5778 N N   . VAL B 1 358 ? 42.907  -60.942 -51.045 1.00 79.51  ? 358  VAL B N   1 
ATOM   5779 C CA  . VAL B 1 358 ? 43.745  -59.739 -51.144 1.00 79.74  ? 358  VAL B CA  1 
ATOM   5780 C C   . VAL B 1 358 ? 43.820  -59.474 -52.636 1.00 89.57  ? 358  VAL B C   1 
ATOM   5781 O O   . VAL B 1 358 ? 43.898  -60.420 -53.424 1.00 89.70  ? 358  VAL B O   1 
ATOM   5782 C CB  . VAL B 1 358 ? 45.168  -59.859 -50.512 1.00 81.81  ? 358  VAL B CB  1 
ATOM   5783 C CG1 . VAL B 1 358 ? 45.898  -58.519 -50.508 1.00 80.58  ? 358  VAL B CG1 1 
ATOM   5784 C CG2 . VAL B 1 358 ? 45.117  -60.433 -49.101 1.00 81.50  ? 358  VAL B CG2 1 
ATOM   5785 N N   . THR B 1 359 ? 43.738  -58.201 -53.022 1.00 89.93  ? 359  THR B N   1 
ATOM   5786 C CA  . THR B 1 359 ? 43.793  -57.768 -54.418 1.00 91.40  ? 359  THR B CA  1 
ATOM   5787 C C   . THR B 1 359 ? 45.085  -56.970 -54.620 1.00 100.38 ? 359  THR B C   1 
ATOM   5788 O O   . THR B 1 359 ? 45.782  -57.165 -55.620 1.00 101.41 ? 359  THR B O   1 
ATOM   5789 C CB  . THR B 1 359 ? 42.466  -57.085 -54.795 1.00 94.47  ? 359  THR B CB  1 
ATOM   5790 O OG1 . THR B 1 359 ? 41.514  -58.122 -55.103 1.00 90.36  ? 359  THR B OG1 1 
ATOM   5791 C CG2 . THR B 1 359 ? 42.587  -56.105 -55.969 1.00 92.84  ? 359  THR B CG2 1 
ATOM   5792 N N   . GLU B 1 360 ? 45.414  -56.113 -53.638 1.00 98.57  ? 360  GLU B N   1 
ATOM   5793 C CA  . GLU B 1 360 ? 46.616  -55.271 -53.548 1.00 98.78  ? 360  GLU B CA  1 
ATOM   5794 C C   . GLU B 1 360 ? 47.075  -55.268 -52.080 1.00 103.27 ? 360  GLU B C   1 
ATOM   5795 O O   . GLU B 1 360 ? 46.230  -55.165 -51.185 1.00 103.85 ? 360  GLU B O   1 
ATOM   5796 C CB  . GLU B 1 360 ? 46.303  -53.820 -53.975 1.00 100.21 ? 360  GLU B CB  1 
ATOM   5797 C CG  . GLU B 1 360 ? 45.883  -53.640 -55.423 1.00 111.28 ? 360  GLU B CG  1 
ATOM   5798 C CD  . GLU B 1 360 ? 44.845  -52.554 -55.636 1.00 134.97 ? 360  GLU B CD  1 
ATOM   5799 O OE1 . GLU B 1 360 ? 45.106  -51.395 -55.236 1.00 132.35 ? 360  GLU B OE1 1 
ATOM   5800 O OE2 . GLU B 1 360 ? 43.763  -52.866 -56.186 1.00 121.07 ? 360  GLU B OE2 1 
ATOM   5801 N N   . LYS B 1 361 ? 48.394  -55.364 -51.829 1.00 99.30  ? 361  LYS B N   1 
ATOM   5802 C CA  . LYS B 1 361 ? 48.979  -55.344 -50.479 1.00 99.08  ? 361  LYS B CA  1 
ATOM   5803 C C   . LYS B 1 361 ? 48.637  -54.036 -49.744 1.00 101.86 ? 361  LYS B C   1 
ATOM   5804 O O   . LYS B 1 361 ? 48.352  -54.050 -48.541 1.00 100.44 ? 361  LYS B O   1 
ATOM   5805 C CB  . LYS B 1 361 ? 50.512  -55.517 -50.552 1.00 101.99 ? 361  LYS B CB  1 
ATOM   5806 C CG  . LYS B 1 361 ? 51.032  -56.938 -50.275 1.00 116.18 ? 361  LYS B CG  1 
ATOM   5807 C CD  . LYS B 1 361 ? 51.104  -57.830 -51.526 1.00 123.89 ? 361  LYS B CD  1 
ATOM   5808 C CE  . LYS B 1 361 ? 52.345  -57.642 -52.381 1.00 131.96 ? 361  LYS B CE  1 
ATOM   5809 N NZ  . LYS B 1 361 ? 52.390  -58.595 -53.522 1.00 135.86 ? 361  LYS B NZ  1 
ATOM   5810 N N   . ASP B 1 362 ? 48.650  -52.919 -50.496 1.00 98.52  ? 362  ASP B N   1 
ATOM   5811 C CA  . ASP B 1 362 ? 48.348  -51.564 -50.028 1.00 98.47  ? 362  ASP B CA  1 
ATOM   5812 C C   . ASP B 1 362 ? 46.935  -51.434 -49.431 1.00 99.67  ? 362  ASP B C   1 
ATOM   5813 O O   . ASP B 1 362 ? 46.766  -50.785 -48.399 1.00 98.86  ? 362  ASP B O   1 
ATOM   5814 C CB  . ASP B 1 362 ? 48.537  -50.547 -51.183 1.00 100.99 ? 362  ASP B CB  1 
ATOM   5815 C CG  . ASP B 1 362 ? 49.964  -50.394 -51.706 1.00 114.57 ? 362  ASP B CG  1 
ATOM   5816 O OD1 . ASP B 1 362 ? 50.842  -51.196 -51.299 1.00 115.38 ? 362  ASP B OD1 1 
ATOM   5817 O OD2 . ASP B 1 362 ? 50.201  -49.478 -52.526 1.00 119.67 ? 362  ASP B OD2 1 
ATOM   5818 N N   . SER B 1 363 ? 45.933  -52.046 -50.093 1.00 94.19  ? 363  SER B N   1 
ATOM   5819 C CA  . SER B 1 363 ? 44.525  -52.018 -49.706 1.00 92.62  ? 363  SER B CA  1 
ATOM   5820 C C   . SER B 1 363 ? 44.186  -53.035 -48.590 1.00 92.10  ? 363  SER B C   1 
ATOM   5821 O O   . SER B 1 363 ? 44.193  -54.247 -48.850 1.00 91.68  ? 363  SER B O   1 
ATOM   5822 C CB  . SER B 1 363 ? 43.634  -52.218 -50.933 1.00 97.09  ? 363  SER B CB  1 
ATOM   5823 O OG  . SER B 1 363 ? 42.249  -52.269 -50.631 1.00 111.74 ? 363  SER B OG  1 
ATOM   5824 N N   . PRO B 1 364 ? 43.835  -52.556 -47.360 1.00 84.31  ? 364  PRO B N   1 
ATOM   5825 C CA  . PRO B 1 364 ? 43.439  -53.482 -46.288 1.00 82.70  ? 364  PRO B CA  1 
ATOM   5826 C C   . PRO B 1 364 ? 42.107  -54.168 -46.596 1.00 82.75  ? 364  PRO B C   1 
ATOM   5827 O O   . PRO B 1 364 ? 41.392  -53.780 -47.532 1.00 83.62  ? 364  PRO B O   1 
ATOM   5828 C CB  . PRO B 1 364 ? 43.341  -52.580 -45.044 1.00 84.56  ? 364  PRO B CB  1 
ATOM   5829 C CG  . PRO B 1 364 ? 43.969  -51.306 -45.416 1.00 89.26  ? 364  PRO B CG  1 
ATOM   5830 C CD  . PRO B 1 364 ? 43.762  -51.167 -46.891 1.00 85.21  ? 364  PRO B CD  1 
ATOM   5831 N N   . VAL B 1 365 ? 41.791  -55.204 -45.829 1.00 75.39  ? 365  VAL B N   1 
ATOM   5832 C CA  . VAL B 1 365 ? 40.598  -56.015 -46.025 1.00 74.72  ? 365  VAL B CA  1 
ATOM   5833 C C   . VAL B 1 365 ? 39.742  -56.052 -44.776 1.00 76.88  ? 365  VAL B C   1 
ATOM   5834 O O   . VAL B 1 365 ? 40.266  -56.045 -43.660 1.00 76.59  ? 365  VAL B O   1 
ATOM   5835 C CB  . VAL B 1 365 ? 40.974  -57.440 -46.514 1.00 79.39  ? 365  VAL B CB  1 
ATOM   5836 C CG1 . VAL B 1 365 ? 39.759  -58.366 -46.575 1.00 79.35  ? 365  VAL B CG1 1 
ATOM   5837 C CG2 . VAL B 1 365 ? 41.689  -57.397 -47.867 1.00 79.19  ? 365  VAL B CG2 1 
ATOM   5838 N N   . ASN B 1 366 ? 38.418  -56.127 -44.981 1.00 72.06  ? 366  ASN B N   1 
ATOM   5839 C CA  . ASN B 1 366 ? 37.417  -56.203 -43.934 1.00 71.41  ? 366  ASN B CA  1 
ATOM   5840 C C   . ASN B 1 366 ? 36.774  -57.565 -43.908 1.00 75.26  ? 366  ASN B C   1 
ATOM   5841 O O   . ASN B 1 366 ? 36.252  -58.030 -44.935 1.00 73.86  ? 366  ASN B O   1 
ATOM   5842 C CB  . ASN B 1 366 ? 36.368  -55.140 -44.129 1.00 69.92  ? 366  ASN B CB  1 
ATOM   5843 C CG  . ASN B 1 366 ? 36.900  -53.783 -43.825 1.00 107.25 ? 366  ASN B CG  1 
ATOM   5844 O OD1 . ASN B 1 366 ? 37.044  -53.380 -42.665 1.00 106.95 ? 366  ASN B OD1 1 
ATOM   5845 N ND2 . ASN B 1 366 ? 37.225  -53.061 -44.866 1.00 103.19 ? 366  ASN B ND2 1 
ATOM   5846 N N   . ILE B 1 367 ? 36.818  -58.222 -42.728 1.00 72.25  ? 367  ILE B N   1 
ATOM   5847 C CA  . ILE B 1 367 ? 36.217  -59.536 -42.593 1.00 72.73  ? 367  ILE B CA  1 
ATOM   5848 C C   . ILE B 1 367 ? 35.187  -59.536 -41.476 1.00 75.21  ? 367  ILE B C   1 
ATOM   5849 O O   . ILE B 1 367 ? 35.472  -59.090 -40.362 1.00 71.60  ? 367  ILE B O   1 
ATOM   5850 C CB  . ILE B 1 367 ? 37.275  -60.669 -42.425 1.00 76.63  ? 367  ILE B CB  1 
ATOM   5851 C CG1 . ILE B 1 367 ? 38.350  -60.661 -43.533 1.00 76.65  ? 367  ILE B CG1 1 
ATOM   5852 C CG2 . ILE B 1 367 ? 36.604  -62.039 -42.376 1.00 78.71  ? 367  ILE B CG2 1 
ATOM   5853 C CD1 . ILE B 1 367 ? 39.650  -60.338 -43.039 1.00 80.50  ? 367  ILE B CD1 1 
ATOM   5854 N N   . GLU B 1 368 ? 33.987  -60.039 -41.796 1.00 74.44  ? 368  GLU B N   1 
ATOM   5855 C CA  . GLU B 1 368 ? 32.904  -60.193 -40.844 1.00 75.40  ? 368  GLU B CA  1 
ATOM   5856 C C   . GLU B 1 368 ? 32.691  -61.671 -40.643 1.00 80.62  ? 368  GLU B C   1 
ATOM   5857 O O   . GLU B 1 368 ? 32.511  -62.413 -41.625 1.00 78.44  ? 368  GLU B O   1 
ATOM   5858 C CB  . GLU B 1 368 ? 31.590  -59.519 -41.306 1.00 77.06  ? 368  GLU B CB  1 
ATOM   5859 C CG  . GLU B 1 368 ? 30.513  -59.500 -40.215 1.00 88.62  ? 368  GLU B CG  1 
ATOM   5860 C CD  . GLU B 1 368 ? 29.143  -58.938 -40.552 1.00 94.06  ? 368  GLU B CD  1 
ATOM   5861 O OE1 . GLU B 1 368 ? 28.651  -59.174 -41.679 1.00 92.92  ? 368  GLU B OE1 1 
ATOM   5862 O OE2 . GLU B 1 368 ? 28.544  -58.287 -39.665 1.00 70.62  ? 368  GLU B OE2 1 
ATOM   5863 N N   . ALA B 1 369 ? 32.691  -62.083 -39.353 1.00 79.74  ? 369  ALA B N   1 
ATOM   5864 C CA  . ALA B 1 369 ? 32.475  -63.465 -38.945 1.00 80.68  ? 369  ALA B CA  1 
ATOM   5865 C C   . ALA B 1 369 ? 31.628  -63.544 -37.702 1.00 86.33  ? 369  ALA B C   1 
ATOM   5866 O O   . ALA B 1 369 ? 31.637  -62.605 -36.900 1.00 85.13  ? 369  ALA B O   1 
ATOM   5867 C CB  . ALA B 1 369 ? 33.808  -64.143 -38.696 1.00 81.37  ? 369  ALA B CB  1 
ATOM   5868 N N   . GLU B 1 370 ? 30.911  -64.681 -37.541 1.00 84.67  ? 370  GLU B N   1 
ATOM   5869 C CA  . GLU B 1 370 ? 30.090  -64.975 -36.371 1.00 85.49  ? 370  GLU B CA  1 
ATOM   5870 C C   . GLU B 1 370 ? 30.901  -65.839 -35.382 1.00 91.43  ? 370  GLU B C   1 
ATOM   5871 O O   . GLU B 1 370 ? 31.054  -67.039 -35.624 1.00 90.26  ? 370  GLU B O   1 
ATOM   5872 C CB  . GLU B 1 370 ? 28.784  -65.681 -36.772 1.00 86.98  ? 370  GLU B CB  1 
ATOM   5873 C CG  . GLU B 1 370 ? 27.801  -65.854 -35.616 1.00 98.34  ? 370  GLU B CG  1 
ATOM   5874 C CD  . GLU B 1 370 ? 26.327  -65.737 -35.972 1.00 122.05 ? 370  GLU B CD  1 
ATOM   5875 O OE1 . GLU B 1 370 ? 25.928  -66.292 -37.020 1.00 104.50 ? 370  GLU B OE1 1 
ATOM   5876 O OE2 . GLU B 1 370 ? 25.569  -65.099 -35.203 1.00 124.78 ? 370  GLU B OE2 1 
ATOM   5877 N N   . PRO B 1 371 ? 31.414  -65.263 -34.262 1.00 90.61  ? 371  PRO B N   1 
ATOM   5878 C CA  . PRO B 1 371 ? 32.163  -66.080 -33.299 1.00 91.56  ? 371  PRO B CA  1 
ATOM   5879 C C   . PRO B 1 371 ? 31.250  -67.009 -32.511 1.00 100.45 ? 371  PRO B C   1 
ATOM   5880 O O   . PRO B 1 371 ? 30.062  -66.703 -32.392 1.00 100.76 ? 371  PRO B O   1 
ATOM   5881 C CB  . PRO B 1 371 ? 32.807  -65.047 -32.377 1.00 92.85  ? 371  PRO B CB  1 
ATOM   5882 C CG  . PRO B 1 371 ? 31.935  -63.887 -32.432 1.00 97.05  ? 371  PRO B CG  1 
ATOM   5883 C CD  . PRO B 1 371 ? 31.326  -63.861 -33.809 1.00 92.64  ? 371  PRO B CD  1 
ATOM   5884 N N   . PRO B 1 372 ? 31.758  -68.136 -31.954 1.00 100.27 ? 372  PRO B N   1 
ATOM   5885 C CA  . PRO B 1 372 ? 30.874  -69.014 -31.177 1.00 100.65 ? 372  PRO B CA  1 
ATOM   5886 C C   . PRO B 1 372 ? 30.610  -68.444 -29.783 1.00 104.87 ? 372  PRO B C   1 
ATOM   5887 O O   . PRO B 1 372 ? 31.366  -67.574 -29.297 1.00 103.66 ? 372  PRO B O   1 
ATOM   5888 C CB  . PRO B 1 372 ? 31.667  -70.321 -31.116 1.00 102.29 ? 372  PRO B CB  1 
ATOM   5889 C CG  . PRO B 1 372 ? 33.077  -69.887 -31.122 1.00 106.50 ? 372  PRO B CG  1 
ATOM   5890 C CD  . PRO B 1 372 ? 33.140  -68.667 -31.985 1.00 102.20 ? 372  PRO B CD  1 
ATOM   5891 N N   . PHE B 1 373 ? 29.546  -68.961 -29.133 1.00 101.75 ? 373  PHE B N   1 
ATOM   5892 C CA  . PHE B 1 373 ? 29.210  -68.565 -27.773 1.00 101.57 ? 373  PHE B CA  1 
ATOM   5893 C C   . PHE B 1 373 ? 30.311  -69.014 -26.822 1.00 107.04 ? 373  PHE B C   1 
ATOM   5894 O O   . PHE B 1 373 ? 30.634  -70.208 -26.746 1.00 107.01 ? 373  PHE B O   1 
ATOM   5895 C CB  . PHE B 1 373 ? 27.857  -69.127 -27.328 1.00 102.73 ? 373  PHE B CB  1 
ATOM   5896 C CG  . PHE B 1 373 ? 26.700  -68.277 -27.764 1.00 103.15 ? 373  PHE B CG  1 
ATOM   5897 C CD1 . PHE B 1 373 ? 26.417  -67.076 -27.123 1.00 105.11 ? 373  PHE B CD1 1 
ATOM   5898 C CD2 . PHE B 1 373 ? 25.897  -68.669 -28.824 1.00 104.32 ? 373  PHE B CD2 1 
ATOM   5899 C CE1 . PHE B 1 373 ? 25.359  -66.274 -27.548 1.00 105.54 ? 373  PHE B CE1 1 
ATOM   5900 C CE2 . PHE B 1 373 ? 24.818  -67.886 -29.227 1.00 106.53 ? 373  PHE B CE2 1 
ATOM   5901 C CZ  . PHE B 1 373 ? 24.559  -66.691 -28.591 1.00 104.48 ? 373  PHE B CZ  1 
ATOM   5902 N N   . GLY B 1 374 ? 30.921  -68.031 -26.178 1.00 103.74 ? 374  GLY B N   1 
ATOM   5903 C CA  . GLY B 1 374 ? 32.001  -68.227 -25.232 1.00 103.64 ? 374  GLY B CA  1 
ATOM   5904 C C   . GLY B 1 374 ? 33.350  -67.906 -25.819 1.00 108.49 ? 374  GLY B C   1 
ATOM   5905 O O   . GLY B 1 374 ? 33.469  -67.079 -26.737 1.00 107.54 ? 374  GLY B O   1 
ATOM   5906 N N   . ASP B 1 375 ? 34.377  -68.576 -25.274 1.00 106.26 ? 375  ASP B N   1 
ATOM   5907 C CA  . ASP B 1 375 ? 35.755  -68.366 -25.671 1.00 106.28 ? 375  ASP B CA  1 
ATOM   5908 C C   . ASP B 1 375 ? 36.094  -69.077 -26.949 1.00 108.46 ? 375  ASP B C   1 
ATOM   5909 O O   . ASP B 1 375 ? 35.690  -70.217 -27.211 1.00 106.38 ? 375  ASP B O   1 
ATOM   5910 C CB  . ASP B 1 375 ? 36.748  -68.661 -24.554 1.00 108.90 ? 375  ASP B CB  1 
ATOM   5911 C CG  . ASP B 1 375 ? 36.755  -67.597 -23.467 1.00 124.89 ? 375  ASP B CG  1 
ATOM   5912 O OD1 . ASP B 1 375 ? 37.068  -66.415 -23.783 1.00 126.38 ? 375  ASP B OD1 1 
ATOM   5913 O OD2 . ASP B 1 375 ? 36.409  -67.929 -22.314 1.00 132.35 ? 375  ASP B OD2 1 
ATOM   5914 N N   . SER B 1 376 ? 36.809  -68.314 -27.774 1.00 105.74 ? 376  SER B N   1 
ATOM   5915 C CA  . SER B 1 376 ? 37.201  -68.619 -29.135 1.00 105.15 ? 376  SER B CA  1 
ATOM   5916 C C   . SER B 1 376 ? 38.550  -68.003 -29.498 1.00 108.23 ? 376  SER B C   1 
ATOM   5917 O O   . SER B 1 376 ? 39.044  -67.083 -28.841 1.00 107.21 ? 376  SER B O   1 
ATOM   5918 C CB  . SER B 1 376 ? 36.127  -68.106 -30.096 1.00 108.37 ? 376  SER B CB  1 
ATOM   5919 O OG  . SER B 1 376 ? 35.414  -66.970 -29.620 1.00 114.59 ? 376  SER B OG  1 
ATOM   5920 N N   . TYR B 1 377 ? 39.126  -68.516 -30.572 1.00 105.71 ? 377  TYR B N   1 
ATOM   5921 C CA  . TYR B 1 377 ? 40.380  -68.049 -31.118 1.00 106.38 ? 377  TYR B CA  1 
ATOM   5922 C C   . TYR B 1 377 ? 40.139  -67.640 -32.584 1.00 105.60 ? 377  TYR B C   1 
ATOM   5923 O O   . TYR B 1 377 ? 39.673  -68.451 -33.396 1.00 103.22 ? 377  TYR B O   1 
ATOM   5924 C CB  . TYR B 1 377 ? 41.456  -69.162 -31.003 1.00 110.46 ? 377  TYR B CB  1 
ATOM   5925 C CG  . TYR B 1 377 ? 42.492  -68.998 -29.901 1.00 115.98 ? 377  TYR B CG  1 
ATOM   5926 C CD1 . TYR B 1 377 ? 42.920  -67.733 -29.497 1.00 119.21 ? 377  TYR B CD1 1 
ATOM   5927 C CD2 . TYR B 1 377 ? 43.117  -70.107 -29.330 1.00 117.40 ? 377  TYR B CD2 1 
ATOM   5928 C CE1 . TYR B 1 377 ? 43.891  -67.575 -28.503 1.00 121.62 ? 377  TYR B CE1 1 
ATOM   5929 C CE2 . TYR B 1 377 ? 44.091  -69.962 -28.336 1.00 118.93 ? 377  TYR B CE2 1 
ATOM   5930 C CZ  . TYR B 1 377 ? 44.479  -68.690 -27.928 1.00 129.38 ? 377  TYR B CZ  1 
ATOM   5931 O OH  . TYR B 1 377 ? 45.446  -68.507 -26.961 1.00 130.88 ? 377  TYR B OH  1 
ATOM   5932 N N   . ILE B 1 378 ? 40.370  -66.359 -32.893 1.00 100.95 ? 378  ILE B N   1 
ATOM   5933 C CA  . ILE B 1 378 ? 40.242  -65.858 -34.253 1.00 100.37 ? 378  ILE B CA  1 
ATOM   5934 C C   . ILE B 1 378 ? 41.622  -65.881 -34.843 1.00 101.08 ? 378  ILE B C   1 
ATOM   5935 O O   . ILE B 1 378 ? 42.495  -65.111 -34.435 1.00 99.86  ? 378  ILE B O   1 
ATOM   5936 C CB  . ILE B 1 378 ? 39.530  -64.484 -34.383 1.00 103.89 ? 378  ILE B CB  1 
ATOM   5937 C CG1 . ILE B 1 378 ? 38.049  -64.631 -34.006 1.00 104.21 ? 378  ILE B CG1 1 
ATOM   5938 C CG2 . ILE B 1 378 ? 39.668  -63.919 -35.824 1.00 105.24 ? 378  ILE B CG2 1 
ATOM   5939 C CD1 . ILE B 1 378 ? 37.521  -63.495 -33.256 1.00 109.68 ? 378  ILE B CD1 1 
ATOM   5940 N N   . ILE B 1 379 ? 41.824  -66.823 -35.761 1.00 95.85  ? 379  ILE B N   1 
ATOM   5941 C CA  . ILE B 1 379 ? 43.091  -67.021 -36.415 1.00 94.94  ? 379  ILE B CA  1 
ATOM   5942 C C   . ILE B 1 379 ? 42.983  -66.609 -37.866 1.00 98.25  ? 379  ILE B C   1 
ATOM   5943 O O   . ILE B 1 379 ? 42.215  -67.179 -38.660 1.00 96.47  ? 379  ILE B O   1 
ATOM   5944 C CB  . ILE B 1 379 ? 43.644  -68.446 -36.160 1.00 97.69  ? 379  ILE B CB  1 
ATOM   5945 C CG1 . ILE B 1 379 ? 44.369  -68.485 -34.814 1.00 97.91  ? 379  ILE B CG1 1 
ATOM   5946 C CG2 . ILE B 1 379 ? 44.579  -68.921 -37.257 1.00 97.95  ? 379  ILE B CG2 1 
ATOM   5947 C CD1 . ILE B 1 379 ? 43.544  -68.919 -33.665 1.00 102.65 ? 379  ILE B CD1 1 
ATOM   5948 N N   . VAL B 1 380 ? 43.727  -65.545 -38.172 1.00 95.71  ? 380  VAL B N   1 
ATOM   5949 C CA  . VAL B 1 380 ? 43.826  -64.955 -39.498 1.00 95.89  ? 380  VAL B CA  1 
ATOM   5950 C C   . VAL B 1 380 ? 45.261  -65.042 -39.970 1.00 101.19 ? 380  VAL B C   1 
ATOM   5951 O O   . VAL B 1 380 ? 46.188  -64.575 -39.296 1.00 100.81 ? 380  VAL B O   1 
ATOM   5952 C CB  . VAL B 1 380 ? 43.193  -63.530 -39.637 1.00 98.95  ? 380  VAL B CB  1 
ATOM   5953 C CG1 . VAL B 1 380 ? 43.650  -62.578 -38.533 1.00 98.67  ? 380  VAL B CG1 1 
ATOM   5954 C CG2 . VAL B 1 380 ? 43.415  -62.932 -41.028 1.00 98.29  ? 380  VAL B CG2 1 
ATOM   5955 N N   . GLY B 1 381 ? 45.413  -65.686 -41.117 1.00 98.30  ? 381  GLY B N   1 
ATOM   5956 C CA  . GLY B 1 381 ? 46.702  -65.888 -41.740 1.00 98.34  ? 381  GLY B CA  1 
ATOM   5957 C C   . GLY B 1 381 ? 47.261  -67.250 -41.441 1.00 103.34 ? 381  GLY B C   1 
ATOM   5958 O O   . GLY B 1 381 ? 46.580  -68.112 -40.868 1.00 102.96 ? 381  GLY B O   1 
ATOM   5959 N N   . VAL B 1 382 ? 48.511  -67.431 -41.844 1.00 100.10 ? 382  VAL B N   1 
ATOM   5960 C CA  . VAL B 1 382 ? 49.255  -68.672 -41.674 1.00 99.71  ? 382  VAL B CA  1 
ATOM   5961 C C   . VAL B 1 382 ? 50.603  -68.363 -40.987 1.00 104.97 ? 382  VAL B C   1 
ATOM   5962 O O   . VAL B 1 382 ? 51.101  -67.231 -41.091 1.00 105.33 ? 382  VAL B O   1 
ATOM   5963 C CB  . VAL B 1 382 ? 49.411  -69.446 -43.013 1.00 102.72 ? 382  VAL B CB  1 
ATOM   5964 C CG1 . VAL B 1 382 ? 48.162  -70.240 -43.363 1.00 102.17 ? 382  VAL B CG1 1 
ATOM   5965 C CG2 . VAL B 1 382 ? 49.837  -68.528 -44.161 1.00 102.54 ? 382  VAL B CG2 1 
ATOM   5966 N N   . GLU B 1 383 ? 51.162  -69.359 -40.258 1.00 100.05 ? 383  GLU B N   1 
ATOM   5967 C CA  . GLU B 1 383 ? 52.426  -69.260 -39.519 1.00 98.29  ? 383  GLU B CA  1 
ATOM   5968 C C   . GLU B 1 383 ? 53.627  -69.230 -40.489 1.00 99.58  ? 383  GLU B C   1 
ATOM   5969 O O   . GLU B 1 383 ? 53.551  -69.897 -41.522 1.00 98.19  ? 383  GLU B O   1 
ATOM   5970 C CB  . GLU B 1 383 ? 52.522  -70.350 -38.444 1.00 99.36  ? 383  GLU B CB  1 
ATOM   5971 C CG  . GLU B 1 383 ? 52.375  -71.761 -38.989 1.00 107.51 ? 383  GLU B CG  1 
ATOM   5972 C CD  . GLU B 1 383 ? 50.987  -72.371 -38.991 1.00 112.57 ? 383  GLU B CD  1 
ATOM   5973 O OE1 . GLU B 1 383 ? 50.089  -71.815 -39.664 1.00 89.53  ? 383  GLU B OE1 1 
ATOM   5974 O OE2 . GLU B 1 383 ? 50.817  -73.447 -38.372 1.00 106.38 ? 383  GLU B OE2 1 
ATOM   5975 N N   . PRO B 1 384 ? 54.690  -68.410 -40.255 1.00 96.31  ? 384  PRO B N   1 
ATOM   5976 C CA  . PRO B 1 384 ? 54.934  -67.543 -39.086 1.00 96.61  ? 384  PRO B CA  1 
ATOM   5977 C C   . PRO B 1 384 ? 54.084  -66.292 -39.158 1.00 103.70 ? 384  PRO B C   1 
ATOM   5978 O O   . PRO B 1 384 ? 53.550  -65.967 -40.232 1.00 104.66 ? 384  PRO B O   1 
ATOM   5979 C CB  . PRO B 1 384 ? 56.426  -67.201 -39.214 1.00 97.80  ? 384  PRO B CB  1 
ATOM   5980 C CG  . PRO B 1 384 ? 56.656  -67.179 -40.698 1.00 101.67 ? 384  PRO B CG  1 
ATOM   5981 C CD  . PRO B 1 384 ? 55.804  -68.310 -41.224 1.00 97.36  ? 384  PRO B CD  1 
ATOM   5982 N N   . GLY B 1 385 ? 53.946  -65.624 -38.016 1.00 99.93  ? 385  GLY B N   1 
ATOM   5983 C CA  . GLY B 1 385 ? 53.146  -64.409 -37.909 1.00 99.09  ? 385  GLY B CA  1 
ATOM   5984 C C   . GLY B 1 385 ? 51.655  -64.651 -38.050 1.00 100.08 ? 385  GLY B C   1 
ATOM   5985 O O   . GLY B 1 385 ? 50.913  -63.740 -38.447 1.00 99.69  ? 385  GLY B O   1 
ATOM   5986 N N   . GLN B 1 386 ? 51.210  -65.897 -37.737 1.00 93.85  ? 386  GLN B N   1 
ATOM   5987 C CA  . GLN B 1 386 ? 49.801  -66.260 -37.745 1.00 92.36  ? 386  GLN B CA  1 
ATOM   5988 C C   . GLN B 1 386 ? 49.127  -65.429 -36.627 1.00 98.12  ? 386  GLN B C   1 
ATOM   5989 O O   . GLN B 1 386 ? 49.524  -65.535 -35.451 1.00 97.50  ? 386  GLN B O   1 
ATOM   5990 C CB  . GLN B 1 386 ? 49.605  -67.771 -37.525 1.00 92.25  ? 386  GLN B CB  1 
ATOM   5991 C CG  . GLN B 1 386 ? 48.146  -68.196 -37.613 1.00 86.28  ? 386  GLN B CG  1 
ATOM   5992 C CD  . GLN B 1 386 ? 47.917  -69.682 -37.529 1.00 105.87 ? 386  GLN B CD  1 
ATOM   5993 O OE1 . GLN B 1 386 ? 48.088  -70.318 -36.485 1.00 99.35  ? 386  GLN B OE1 1 
ATOM   5994 N NE2 . GLN B 1 386 ? 47.419  -70.258 -38.608 1.00 105.48 ? 386  GLN B NE2 1 
ATOM   5995 N N   . LEU B 1 387 ? 48.181  -64.528 -37.017 1.00 95.11  ? 387  LEU B N   1 
ATOM   5996 C CA  . LEU B 1 387 ? 47.474  -63.723 -36.030 1.00 95.35  ? 387  LEU B CA  1 
ATOM   5997 C C   . LEU B 1 387 ? 46.522  -64.631 -35.264 1.00 101.14 ? 387  LEU B C   1 
ATOM   5998 O O   . LEU B 1 387 ? 45.713  -65.337 -35.878 1.00 100.68 ? 387  LEU B O   1 
ATOM   5999 C CB  . LEU B 1 387 ? 46.734  -62.536 -36.660 1.00 95.46  ? 387  LEU B CB  1 
ATOM   6000 C CG  . LEU B 1 387 ? 47.588  -61.419 -37.288 1.00 100.19 ? 387  LEU B CG  1 
ATOM   6001 C CD1 . LEU B 1 387 ? 46.719  -60.417 -38.021 1.00 100.07 ? 387  LEU B CD1 1 
ATOM   6002 C CD2 . LEU B 1 387 ? 48.397  -60.671 -36.246 1.00 101.63 ? 387  LEU B CD2 1 
ATOM   6003 N N   . LYS B 1 388 ? 46.709  -64.702 -33.931 1.00 98.92  ? 388  LYS B N   1 
ATOM   6004 C CA  . LYS B 1 388 ? 45.911  -65.560 -33.064 1.00 99.79  ? 388  LYS B CA  1 
ATOM   6005 C C   . LYS B 1 388 ? 45.215  -64.705 -32.013 1.00 106.09 ? 388  LYS B C   1 
ATOM   6006 O O   . LYS B 1 388 ? 45.711  -64.526 -30.897 1.00 106.47 ? 388  LYS B O   1 
ATOM   6007 C CB  . LYS B 1 388 ? 46.766  -66.687 -32.441 1.00 103.15 ? 388  LYS B CB  1 
ATOM   6008 C CG  . LYS B 1 388 ? 47.635  -67.452 -33.438 1.00 125.51 ? 388  LYS B CG  1 
ATOM   6009 C CD  . LYS B 1 388 ? 48.772  -68.200 -32.746 1.00 137.81 ? 388  LYS B CD  1 
ATOM   6010 C CE  . LYS B 1 388 ? 49.837  -68.698 -33.707 1.00 143.90 ? 388  LYS B CE  1 
ATOM   6011 N NZ  . LYS B 1 388 ? 50.774  -67.615 -34.119 1.00 148.09 ? 388  LYS B NZ  1 
ATOM   6012 N N   . LEU B 1 389 ? 44.074  -64.136 -32.404 1.00 103.78 ? 389  LEU B N   1 
ATOM   6013 C CA  . LEU B 1 389 ? 43.255  -63.264 -31.568 1.00 104.14 ? 389  LEU B CA  1 
ATOM   6014 C C   . LEU B 1 389 ? 42.288  -64.076 -30.730 1.00 107.30 ? 389  LEU B C   1 
ATOM   6015 O O   . LEU B 1 389 ? 41.899  -65.166 -31.128 1.00 106.21 ? 389  LEU B O   1 
ATOM   6016 C CB  . LEU B 1 389 ? 42.519  -62.227 -32.439 1.00 104.55 ? 389  LEU B CB  1 
ATOM   6017 C CG  . LEU B 1 389 ? 43.434  -61.314 -33.286 1.00 109.84 ? 389  LEU B CG  1 
ATOM   6018 C CD1 . LEU B 1 389 ? 42.739  -60.822 -34.550 1.00 110.39 ? 389  LEU B CD1 1 
ATOM   6019 C CD2 . LEU B 1 389 ? 44.028  -60.170 -32.455 1.00 112.44 ? 389  LEU B CD2 1 
ATOM   6020 N N   . ASN B 1 390 ? 41.929  -63.557 -29.557 1.00 103.79 ? 390  ASN B N   1 
ATOM   6021 C CA  . ASN B 1 390 ? 41.036  -64.224 -28.604 1.00 103.49 ? 390  ASN B CA  1 
ATOM   6022 C C   . ASN B 1 390 ? 39.747  -63.457 -28.424 1.00 107.12 ? 390  ASN B C   1 
ATOM   6023 O O   . ASN B 1 390 ? 39.767  -62.235 -28.249 1.00 107.04 ? 390  ASN B O   1 
ATOM   6024 C CB  . ASN B 1 390 ? 41.727  -64.420 -27.255 1.00 103.15 ? 390  ASN B CB  1 
ATOM   6025 C CG  . ASN B 1 390 ? 42.765  -63.366 -26.927 1.00 125.65 ? 390  ASN B CG  1 
ATOM   6026 O OD1 . ASN B 1 390 ? 42.649  -62.186 -27.279 1.00 123.48 ? 390  ASN B OD1 1 
ATOM   6027 N ND2 . ASN B 1 390 ? 43.817  -63.776 -26.254 1.00 116.70 ? 390  ASN B ND2 1 
ATOM   6028 N N   . TRP B 1 391 ? 38.625  -64.180 -28.442 1.00 103.06 ? 391  TRP B N   1 
ATOM   6029 C CA  . TRP B 1 391 ? 37.301  -63.576 -28.322 1.00 102.57 ? 391  TRP B CA  1 
ATOM   6030 C C   . TRP B 1 391 ? 36.379  -64.282 -27.333 1.00 106.58 ? 391  TRP B C   1 
ATOM   6031 O O   . TRP B 1 391 ? 36.555  -65.468 -27.063 1.00 105.68 ? 391  TRP B O   1 
ATOM   6032 C CB  . TRP B 1 391 ? 36.622  -63.551 -29.711 1.00 100.91 ? 391  TRP B CB  1 
ATOM   6033 C CG  . TRP B 1 391 ? 35.476  -62.586 -29.794 1.00 101.28 ? 391  TRP B CG  1 
ATOM   6034 C CD1 . TRP B 1 391 ? 34.142  -62.887 -29.831 1.00 103.99 ? 391  TRP B CD1 1 
ATOM   6035 C CD2 . TRP B 1 391 ? 35.566  -61.164 -29.690 1.00 100.86 ? 391  TRP B CD2 1 
ATOM   6036 N NE1 . TRP B 1 391 ? 33.400  -61.733 -29.825 1.00 103.16 ? 391  TRP B NE1 1 
ATOM   6037 C CE2 . TRP B 1 391 ? 34.247  -60.660 -29.697 1.00 104.43 ? 391  TRP B CE2 1 
ATOM   6038 C CE3 . TRP B 1 391 ? 36.641  -60.261 -29.574 1.00 101.94 ? 391  TRP B CE3 1 
ATOM   6039 C CZ2 . TRP B 1 391 ? 33.971  -59.293 -29.603 1.00 103.58 ? 391  TRP B CZ2 1 
ATOM   6040 C CZ3 . TRP B 1 391 ? 36.368  -58.907 -29.490 1.00 103.33 ? 391  TRP B CZ3 1 
ATOM   6041 C CH2 . TRP B 1 391 ? 35.047  -58.434 -29.526 1.00 103.99 ? 391  TRP B CH2 1 
ATOM   6042 N N   . LEU B 1 392 ? 35.340  -63.567 -26.849 1.00 103.39 ? 392  LEU B N   1 
ATOM   6043 C CA  . LEU B 1 392 ? 34.281  -64.107 -25.995 1.00 103.20 ? 392  LEU B CA  1 
ATOM   6044 C C   . LEU B 1 392 ? 32.905  -63.523 -26.358 1.00 106.21 ? 392  LEU B C   1 
ATOM   6045 O O   . LEU B 1 392 ? 32.730  -62.305 -26.329 1.00 105.53 ? 392  LEU B O   1 
ATOM   6046 C CB  . LEU B 1 392 ? 34.571  -63.946 -24.489 1.00 103.36 ? 392  LEU B CB  1 
ATOM   6047 C CG  . LEU B 1 392 ? 33.444  -64.447 -23.555 1.00 107.74 ? 392  LEU B CG  1 
ATOM   6048 C CD1 . LEU B 1 392 ? 33.809  -65.750 -22.886 1.00 107.85 ? 392  LEU B CD1 1 
ATOM   6049 C CD2 . LEU B 1 392 ? 33.018  -63.381 -22.552 1.00 108.63 ? 392  LEU B CD2 1 
ATOM   6050 N N   . ARG B 1 393 ? 31.932  -64.402 -26.664 1.00 102.67 ? 393  ARG B N   1 
ATOM   6051 C CA  . ARG B 1 393 ? 30.545  -64.044 -26.967 1.00 102.53 ? 393  ARG B CA  1 
ATOM   6052 C C   . ARG B 1 393 ? 29.622  -64.674 -25.875 1.00 108.97 ? 393  ARG B C   1 
ATOM   6053 O O   . ARG B 1 393 ? 29.260  -65.846 -25.983 1.00 107.95 ? 393  ARG B O   1 
ATOM   6054 C CB  . ARG B 1 393 ? 30.170  -64.491 -28.387 1.00 99.90  ? 393  ARG B CB  1 
ATOM   6055 C CG  . ARG B 1 393 ? 28.845  -63.917 -28.878 1.00 96.31  ? 393  ARG B CG  1 
ATOM   6056 C CD  . ARG B 1 393 ? 28.253  -64.800 -29.944 1.00 81.42  ? 393  ARG B CD  1 
ATOM   6057 N NE  . ARG B 1 393 ? 26.901  -64.391 -30.301 1.00 76.44  ? 393  ARG B NE  1 
ATOM   6058 C CZ  . ARG B 1 393 ? 26.227  -64.858 -31.351 1.00 94.45  ? 393  ARG B CZ  1 
ATOM   6059 N NH1 . ARG B 1 393 ? 26.781  -65.754 -32.164 1.00 77.04  ? 393  ARG B NH1 1 
ATOM   6060 N NH2 . ARG B 1 393 ? 24.992  -64.435 -31.596 1.00 84.34  ? 393  ARG B NH2 1 
ATOM   6061 N N   . PRO B 1 394 ? 29.262  -63.914 -24.806 1.00 108.49 ? 394  PRO B N   1 
ATOM   6062 C CA  . PRO B 1 394 ? 28.482  -64.497 -23.693 1.00 109.29 ? 394  PRO B CA  1 
ATOM   6063 C C   . PRO B 1 394 ? 27.066  -64.949 -24.031 1.00 115.34 ? 394  PRO B C   1 
ATOM   6064 O O   . PRO B 1 394 ? 26.504  -64.505 -25.039 1.00 115.31 ? 394  PRO B O   1 
ATOM   6065 C CB  . PRO B 1 394 ? 28.486  -63.391 -22.636 1.00 111.06 ? 394  PRO B CB  1 
ATOM   6066 C CG  . PRO B 1 394 ? 28.719  -62.139 -23.400 1.00 115.28 ? 394  PRO B CG  1 
ATOM   6067 C CD  . PRO B 1 394 ? 29.643  -62.519 -24.507 1.00 110.56 ? 394  PRO B CD  1 
ATOM   6068 N N   . LEU B 1 395 ? 26.503  -65.854 -23.185 1.00 112.30 ? 395  LEU B N   1 
ATOM   6069 C CA  . LEU B 1 395 ? 25.158  -66.406 -23.361 1.00 140.70 ? 395  LEU B CA  1 
ATOM   6070 C C   . LEU B 1 395 ? 24.096  -65.517 -22.721 1.00 157.38 ? 395  LEU B C   1 
ATOM   6071 O O   . LEU B 1 395 ? 23.512  -64.669 -23.397 1.00 117.77 ? 395  LEU B O   1 
ATOM   6072 C CB  . LEU B 1 395 ? 25.082  -67.830 -22.803 1.00 140.75 ? 395  LEU B CB  1 
HETATM 6073 C C1  . NAG C 2 .   ? -26.154 15.269  -37.798 1.00 136.15 ? 501  NAG A C1  1 
HETATM 6074 C C2  . NAG C 2 .   ? -26.301 15.777  -39.237 1.00 136.95 ? 501  NAG A C2  1 
HETATM 6075 C C3  . NAG C 2 .   ? -25.196 16.777  -39.583 1.00 138.90 ? 501  NAG A C3  1 
HETATM 6076 C C4  . NAG C 2 .   ? -25.140 17.873  -38.527 1.00 140.19 ? 501  NAG A C4  1 
HETATM 6077 C C5  . NAG C 2 .   ? -24.874 17.222  -37.174 1.00 136.07 ? 501  NAG A C5  1 
HETATM 6078 C C6  . NAG C 2 .   ? -24.654 18.209  -36.046 1.00 132.06 ? 501  NAG A C6  1 
HETATM 6079 C C7  . NAG C 2 .   ? -27.470 14.128  -40.652 1.00 132.65 ? 501  NAG A C7  1 
HETATM 6080 C C8  . NAG C 2 .   ? -27.314 13.170  -41.792 1.00 132.28 ? 501  NAG A C8  1 
HETATM 6081 N N2  . NAG C 2 .   ? -26.341 14.702  -40.215 1.00 134.43 ? 501  NAG A N2  1 
HETATM 6082 O O3  . NAG C 2 .   ? -25.404 17.333  -40.877 1.00 139.27 ? 501  NAG A O3  1 
HETATM 6083 O O4  . NAG C 2 .   ? -24.146 18.838  -38.855 1.00 145.54 ? 501  NAG A O4  1 
HETATM 6084 O O5  . NAG C 2 .   ? -25.961 16.335  -36.842 1.00 136.48 ? 501  NAG A O5  1 
HETATM 6085 O O6  . NAG C 2 .   ? -25.636 18.185  -35.024 1.00 129.73 ? 501  NAG A O6  1 
HETATM 6086 O O7  . NAG C 2 .   ? -28.567 14.387  -40.167 1.00 132.44 ? 501  NAG A O7  1 
HETATM 6087 C C1  . FUC D 3 .   ? -26.458 19.322  -34.929 1.00 126.93 ? 502  FUC A C1  1 
HETATM 6088 C C2  . FUC D 3 .   ? -27.042 19.387  -33.502 1.00 125.62 ? 502  FUC A C2  1 
HETATM 6089 C C3  . FUC D 3 .   ? -27.375 20.808  -33.063 1.00 124.58 ? 502  FUC A C3  1 
HETATM 6090 C C4  . FUC D 3 .   ? -27.732 21.700  -34.246 1.00 126.14 ? 502  FUC A C4  1 
HETATM 6091 C C5  . FUC D 3 .   ? -26.538 21.817  -35.198 1.00 125.52 ? 502  FUC A C5  1 
HETATM 6092 C C6  . FUC D 3 .   ? -26.914 22.275  -36.587 1.00 125.72 ? 502  FUC A C6  1 
HETATM 6093 O O2  . FUC D 3 .   ? -26.165 18.804  -32.544 1.00 125.34 ? 502  FUC A O2  1 
HETATM 6094 O O3  . FUC D 3 .   ? -28.435 20.774  -32.114 1.00 123.05 ? 502  FUC A O3  1 
HETATM 6095 O O4  . FUC D 3 .   ? -28.904 21.236  -34.914 1.00 127.82 ? 502  FUC A O4  1 
HETATM 6096 O O5  . FUC D 3 .   ? -25.828 20.562  -35.291 1.00 125.02 ? 502  FUC A O5  1 
HETATM 6097 C C1  . NAG E 2 .   ? -24.566 20.181  -39.041 1.00 149.85 ? 503  NAG A C1  1 
HETATM 6098 C C2  . NAG E 2 .   ? -23.487 21.108  -38.486 1.00 150.83 ? 503  NAG A C2  1 
HETATM 6099 C C3  . NAG E 2 .   ? -24.059 22.520  -38.586 1.00 153.85 ? 503  NAG A C3  1 
HETATM 6100 C C4  . NAG E 2 .   ? -24.408 22.867  -40.032 1.00 155.54 ? 503  NAG A C4  1 
HETATM 6101 C C5  . NAG E 2 .   ? -25.311 21.800  -40.648 1.00 155.16 ? 503  NAG A C5  1 
HETATM 6102 C C6  . NAG E 2 .   ? -25.491 21.948  -42.143 1.00 156.49 ? 503  NAG A C6  1 
HETATM 6103 C C7  . NAG E 2 .   ? -21.896 20.583  -36.681 1.00 146.63 ? 503  NAG A C7  1 
HETATM 6104 C C8  . NAG E 2 .   ? -21.694 20.633  -35.198 1.00 146.58 ? 503  NAG A C8  1 
HETATM 6105 N N2  . NAG E 2 .   ? -23.143 20.804  -37.106 1.00 148.67 ? 503  NAG A N2  1 
HETATM 6106 O O3  . NAG E 2 .   ? -23.111 23.434  -38.050 1.00 154.91 ? 503  NAG A O3  1 
HETATM 6107 O O4  . NAG E 2 .   ? -25.064 24.131  -40.076 1.00 156.65 ? 503  NAG A O4  1 
HETATM 6108 O O5  . NAG E 2 .   ? -24.748 20.496  -40.424 1.00 152.71 ? 503  NAG A O5  1 
HETATM 6109 O O6  . NAG E 2 .   ? -26.372 20.963  -42.673 1.00 156.90 ? 503  NAG A O6  1 
HETATM 6110 O O7  . NAG E 2 .   ? -20.970 20.362  -37.455 1.00 145.63 ? 503  NAG A O7  1 
HETATM 6111 C C1  . NAG F 2 .   ? 19.902  -18.634 -35.197 1.00 119.61 ? 567  NAG A C1  1 
HETATM 6112 C C2  . NAG F 2 .   ? 20.583  -17.918 -34.032 1.00 119.57 ? 567  NAG A C2  1 
HETATM 6113 C C3  . NAG F 2 .   ? 21.110  -16.559 -34.495 1.00 123.34 ? 567  NAG A C3  1 
HETATM 6114 C C4  . NAG F 2 .   ? 22.050  -16.718 -35.687 1.00 126.14 ? 567  NAG A C4  1 
HETATM 6115 C C5  . NAG F 2 .   ? 21.348  -17.475 -36.815 1.00 123.00 ? 567  NAG A C5  1 
HETATM 6116 C C6  . NAG F 2 .   ? 22.287  -17.868 -37.936 1.00 118.98 ? 567  NAG A C6  1 
HETATM 6117 C C7  . NAG F 2 .   ? 20.050  -17.750 -31.628 1.00 114.61 ? 567  NAG A C7  1 
HETATM 6118 C C8  . NAG F 2 .   ? 19.026  -17.283 -30.644 1.00 114.16 ? 567  NAG A C8  1 
HETATM 6119 N N2  . NAG F 2 .   ? 19.661  -17.764 -32.917 1.00 116.34 ? 567  NAG A N2  1 
HETATM 6120 O O3  . NAG F 2 .   ? 21.814  -15.940 -33.425 1.00 124.79 ? 567  NAG A O3  1 
HETATM 6121 O O4  . NAG F 2 .   ? 22.471  -15.425 -36.120 1.00 132.17 ? 567  NAG A O4  1 
HETATM 6122 O O5  . NAG F 2 .   ? 20.798  -18.707 -36.317 1.00 123.23 ? 567  NAG A O5  1 
HETATM 6123 O O6  . NAG F 2 .   ? 21.587  -18.424 -39.033 1.00 118.05 ? 567  NAG A O6  1 
HETATM 6124 O O7  . NAG F 2 .   ? 21.181  -18.077 -31.277 1.00 113.76 ? 567  NAG A O7  1 
HETATM 6125 C C1  . NAG G 2 .   ? 23.827  -15.220 -36.540 1.00 138.68 ? 569  NAG A C1  1 
HETATM 6126 C C2  . NAG G 2 .   ? 23.833  -14.193 -37.673 1.00 143.98 ? 569  NAG A C2  1 
HETATM 6127 C C3  . NAG G 2 .   ? 24.825  -13.080 -37.341 1.00 146.02 ? 569  NAG A C3  1 
HETATM 6128 C C4  . NAG G 2 .   ? 24.578  -12.563 -35.928 1.00 145.58 ? 569  NAG A C4  1 
HETATM 6129 C C5  . NAG G 2 .   ? 24.834  -13.652 -34.886 1.00 144.49 ? 569  NAG A C5  1 
HETATM 6130 C C6  . NAG G 2 .   ? 23.899  -13.580 -33.696 1.00 146.14 ? 569  NAG A C6  1 
HETATM 6131 C C7  . NAG G 2 .   ? 23.291  -15.025 -39.940 1.00 147.77 ? 569  NAG A C7  1 
HETATM 6132 C C8  . NAG G 2 .   ? 23.825  -15.737 -41.148 1.00 148.19 ? 569  NAG A C8  1 
HETATM 6133 N N2  . NAG G 2 .   ? 24.172  -14.823 -38.940 1.00 146.93 ? 569  NAG A N2  1 
HETATM 6134 O O3  . NAG G 2 .   ? 24.683  -12.014 -38.275 1.00 147.27 ? 569  NAG A O3  1 
HETATM 6135 O O4  . NAG G 2 .   ? 25.403  -11.430 -35.665 1.00 145.07 ? 569  NAG A O4  1 
HETATM 6136 O O5  . NAG G 2 .   ? 24.738  -14.978 -35.451 1.00 141.02 ? 569  NAG A O5  1 
HETATM 6137 O O6  . NAG G 2 .   ? 24.136  -14.629 -32.764 1.00 146.65 ? 569  NAG A O6  1 
HETATM 6138 O O7  . NAG G 2 .   ? 22.121  -14.656 -39.870 1.00 147.22 ? 569  NAG A O7  1 
HETATM 6139 C C1  . NAG H 2 .   ? 32.722  -44.524 -48.151 1.00 81.59  ? 501  NAG B C1  1 
HETATM 6140 C C2  . NAG H 2 .   ? 33.787  -44.090 -47.140 1.00 82.21  ? 501  NAG B C2  1 
HETATM 6141 C C3  . NAG H 2 .   ? 34.550  -42.878 -47.671 1.00 80.42  ? 501  NAG B C3  1 
HETATM 6142 C C4  . NAG H 2 .   ? 35.116  -43.185 -49.051 1.00 80.88  ? 501  NAG B C4  1 
HETATM 6143 C C5  . NAG H 2 .   ? 33.949  -43.543 -49.968 1.00 80.40  ? 501  NAG B C5  1 
HETATM 6144 C C6  . NAG H 2 .   ? 34.323  -43.727 -51.424 1.00 76.83  ? 501  NAG B C6  1 
HETATM 6145 C C7  . NAG H 2 .   ? 33.132  -44.666 -44.838 1.00 88.79  ? 501  NAG B C7  1 
HETATM 6146 C C8  . NAG H 2 .   ? 32.580  -44.130 -43.553 1.00 87.87  ? 501  NAG B C8  1 
HETATM 6147 N N2  . NAG H 2 .   ? 33.191  -43.791 -45.851 1.00 86.39  ? 501  NAG B N2  1 
HETATM 6148 O O3  . NAG H 2 .   ? 35.574  -42.464 -46.771 1.00 80.11  ? 501  NAG B O3  1 
HETATM 6149 O O4  . NAG H 2 .   ? 35.834  -42.064 -49.552 1.00 82.85  ? 501  NAG B O4  1 
HETATM 6150 O O5  . NAG H 2 .   ? 33.286  -44.724 -49.470 1.00 82.01  ? 501  NAG B O5  1 
HETATM 6151 O O6  . NAG H 2 .   ? 34.162  -45.038 -51.923 1.00 75.89  ? 501  NAG B O6  1 
HETATM 6152 O O7  . NAG H 2 .   ? 33.488  -45.838 -44.958 1.00 90.59  ? 501  NAG B O7  1 
HETATM 6153 C C1  . FUC I 3 .   ? 35.350  -45.728 -52.227 1.00 73.27  ? 502  FUC B C1  1 
HETATM 6154 C C2  . FUC I 3 .   ? 35.026  -46.841 -53.251 1.00 70.49  ? 502  FUC B C2  1 
HETATM 6155 C C3  . FUC I 3 .   ? 36.212  -47.159 -54.148 1.00 67.29  ? 502  FUC B C3  1 
HETATM 6156 C C4  . FUC I 3 .   ? 37.539  -46.949 -53.418 1.00 69.48  ? 502  FUC B C4  1 
HETATM 6157 C C5  . FUC I 3 .   ? 37.705  -45.467 -53.077 1.00 69.14  ? 502  FUC B C5  1 
HETATM 6158 C C6  . FUC I 3 .   ? 38.742  -45.194 -52.010 1.00 61.99  ? 502  FUC B C6  1 
HETATM 6159 O O2  . FUC I 3 .   ? 33.872  -46.576 -54.037 1.00 72.26  ? 502  FUC B O2  1 
HETATM 6160 O O3  . FUC I 3 .   ? 36.086  -48.499 -54.602 1.00 66.65  ? 502  FUC B O3  1 
HETATM 6161 O O4  . FUC I 3 .   ? 37.645  -47.771 -52.258 1.00 69.82  ? 502  FUC B O4  1 
HETATM 6162 O O5  . FUC I 3 .   ? 36.438  -44.899 -52.671 1.00 72.54  ? 502  FUC B O5  1 
HETATM 6163 C C1  . NAG J 2 .   ? 37.200  -42.234 -49.865 1.00 83.86  ? 503  NAG B C1  1 
HETATM 6164 C C2  . NAG J 2 .   ? 37.508  -41.393 -51.101 1.00 86.10  ? 503  NAG B C2  1 
HETATM 6165 C C3  . NAG J 2 .   ? 38.949  -41.726 -51.466 1.00 87.81  ? 503  NAG B C3  1 
HETATM 6166 C C4  . NAG J 2 .   ? 39.905  -41.342 -50.334 1.00 87.86  ? 503  NAG B C4  1 
HETATM 6167 C C5  . NAG J 2 .   ? 39.447  -41.946 -49.005 1.00 86.94  ? 503  NAG B C5  1 
HETATM 6168 C C6  . NAG J 2 .   ? 40.137  -41.322 -47.813 1.00 87.86  ? 503  NAG B C6  1 
HETATM 6169 C C7  . NAG J 2 .   ? 35.949  -40.764 -52.903 1.00 86.11  ? 503  NAG B C7  1 
HETATM 6170 C C8  . NAG J 2 .   ? 35.395  -41.210 -54.223 1.00 86.25  ? 503  NAG B C8  1 
HETATM 6171 N N2  . NAG J 2 .   ? 36.631  -41.691 -52.219 1.00 87.83  ? 503  NAG B N2  1 
HETATM 6172 O O3  . NAG J 2 .   ? 39.257  -41.016 -52.660 1.00 88.31  ? 503  NAG B O3  1 
HETATM 6173 O O4  . NAG J 2 .   ? 41.222  -41.830 -50.623 1.00 89.32  ? 503  NAG B O4  1 
HETATM 6174 O O5  . NAG J 2 .   ? 38.033  -41.754 -48.808 1.00 84.64  ? 503  NAG B O5  1 
HETATM 6175 O O6  . NAG J 2 .   ? 39.698  -41.904 -46.597 1.00 88.80  ? 503  NAG B O6  1 
HETATM 6176 O O7  . NAG J 2 .   ? 35.791  -39.621 -52.480 1.00 83.05  ? 503  NAG B O7  1 
HETATM 6177 C C1  . BMA K 4 .   ? 42.291  -41.022 -51.217 1.00 93.05  ? 504  BMA B C1  1 
HETATM 6178 C C2  . BMA K 4 .   ? 41.765  -40.046 -52.283 1.00 98.00  ? 504  BMA B C2  1 
HETATM 6179 C C3  . BMA K 4 .   ? 42.965  -39.382 -52.950 1.00 98.03  ? 504  BMA B C3  1 
HETATM 6180 C C4  . BMA K 4 .   ? 43.744  -38.622 -51.879 1.00 94.44  ? 504  BMA B C4  1 
HETATM 6181 C C5  . BMA K 4 .   ? 44.202  -39.597 -50.793 1.00 93.81  ? 504  BMA B C5  1 
HETATM 6182 C C6  . BMA K 4 .   ? 44.914  -38.917 -49.641 1.00 94.39  ? 504  BMA B C6  1 
HETATM 6183 O O2  . BMA K 4 .   ? 40.969  -39.057 -51.629 1.00 101.45 ? 504  BMA B O2  1 
HETATM 6184 O O3  . BMA K 4 .   ? 42.715  -38.599 -54.137 1.00 102.55 ? 504  BMA B O3  1 
HETATM 6185 O O4  . BMA K 4 .   ? 44.858  -37.931 -52.429 1.00 94.20  ? 504  BMA B O4  1 
HETATM 6186 O O5  . BMA K 4 .   ? 43.072  -40.309 -50.247 1.00 92.74  ? 504  BMA B O5  1 
HETATM 6187 O O6  . BMA K 4 .   ? 45.645  -39.804 -48.790 1.00 93.07  ? 504  BMA B O6  1 
HETATM 6188 C C1  . BMA L 4 .   ? 46.535  -40.667 -49.442 1.00 95.20  ? 505  BMA B C1  1 
HETATM 6189 C C2  . BMA L 4 .   ? 47.979  -40.339 -49.020 1.00 94.47  ? 505  BMA B C2  1 
HETATM 6190 C C3  . BMA L 4 .   ? 48.829  -41.602 -48.966 1.00 93.68  ? 505  BMA B C3  1 
HETATM 6191 C C4  . BMA L 4 .   ? 48.275  -42.608 -47.958 1.00 94.05  ? 505  BMA B C4  1 
HETATM 6192 C C5  . BMA L 4 .   ? 46.757  -42.770 -48.082 1.00 96.66  ? 505  BMA B C5  1 
HETATM 6193 C C6  . BMA L 4 .   ? 45.959  -42.434 -46.834 1.00 95.19  ? 505  BMA B C6  1 
HETATM 6194 O O2  . BMA L 4 .   ? 48.015  -39.658 -47.770 1.00 93.51  ? 505  BMA B O2  1 
HETATM 6195 O O3  . BMA L 4 .   ? 50.174  -41.256 -48.653 1.00 92.31  ? 505  BMA B O3  1 
HETATM 6196 O O4  . BMA L 4 .   ? 48.875  -43.882 -48.167 1.00 92.87  ? 505  BMA B O4  1 
HETATM 6197 O O5  . BMA L 4 .   ? 46.209  -42.054 -49.215 1.00 98.30  ? 505  BMA B O5  1 
HETATM 6198 O O6  . BMA L 4 .   ? 46.160  -41.105 -46.349 1.00 93.16  ? 505  BMA B O6  1 
HETATM 6199 C C1  . BMA M 4 .   ? 41.421  -38.263 -54.851 1.00 104.39 ? 506  BMA B C1  1 
HETATM 6200 C C2  . BMA M 4 .   ? 41.205  -39.165 -56.089 1.00 104.48 ? 506  BMA B C2  1 
HETATM 6201 C C3  . BMA M 4 .   ? 39.761  -39.663 -56.218 1.00 100.28 ? 506  BMA B C3  1 
HETATM 6202 C C4  . BMA M 4 .   ? 38.711  -38.592 -55.916 1.00 97.56  ? 506  BMA B C4  1 
HETATM 6203 C C5  . BMA M 4 .   ? 39.128  -37.665 -54.775 1.00 100.96 ? 506  BMA B C5  1 
HETATM 6204 C C6  . BMA M 4 .   ? 38.026  -37.384 -53.776 1.00 100.22 ? 506  BMA B C6  1 
HETATM 6205 O O2  . BMA M 4 .   ? 42.124  -40.254 -56.144 1.00 108.11 ? 506  BMA B O2  1 
HETATM 6206 O O3  . BMA M 4 .   ? 39.531  -40.819 -55.423 1.00 101.23 ? 506  BMA B O3  1 
HETATM 6207 O O4  . BMA M 4 .   ? 38.456  -37.817 -57.077 1.00 95.18  ? 506  BMA B O4  1 
HETATM 6208 O O5  . BMA M 4 .   ? 40.237  -38.228 -54.052 1.00 104.29 ? 506  BMA B O5  1 
HETATM 6209 O O6  . BMA M 4 .   ? 36.975  -36.603 -54.339 1.00 98.30  ? 506  BMA B O6  1 
HETATM 6210 C C1  . NAG N 2 .   ? -4.527  -3.985  -55.691 1.00 105.76 ? 567  NAG B C1  1 
HETATM 6211 C C2  . NAG N 2 .   ? -4.493  -3.984  -57.220 1.00 106.06 ? 567  NAG B C2  1 
HETATM 6212 C C3  . NAG N 2 .   ? -3.055  -3.723  -57.666 1.00 108.98 ? 567  NAG B C3  1 
HETATM 6213 C C4  . NAG N 2 .   ? -2.521  -2.425  -57.072 1.00 110.73 ? 567  NAG B C4  1 
HETATM 6214 C C5  . NAG N 2 .   ? -2.679  -2.432  -55.550 1.00 109.13 ? 567  NAG B C5  1 
HETATM 6215 C C6  . NAG N 2 .   ? -2.368  -1.100  -54.907 1.00 112.46 ? 567  NAG B C6  1 
HETATM 6216 C C7  . NAG N 2 .   ? -5.532  -5.421  -58.931 1.00 102.25 ? 567  NAG B C7  1 
HETATM 6217 C C8  . NAG N 2 .   ? -5.616  -6.831  -59.438 1.00 100.11 ? 567  NAG B C8  1 
HETATM 6218 N N2  . NAG N 2 .   ? -4.951  -5.263  -57.737 1.00 103.49 ? 567  NAG B N2  1 
HETATM 6219 O O3  . NAG N 2 .   ? -3.011  -3.661  -59.087 1.00 109.77 ? 567  NAG B O3  1 
HETATM 6220 O O4  . NAG N 2 .   ? -1.144  -2.331  -57.434 1.00 115.87 ? 567  NAG B O4  1 
HETATM 6221 O O5  . NAG N 2 .   ? -4.038  -2.737  -55.193 1.00 105.97 ? 567  NAG B O5  1 
HETATM 6222 O O6  . NAG N 2 .   ? -2.355  -1.195  -53.488 1.00 113.74 ? 567  NAG B O6  1 
HETATM 6223 O O7  . NAG N 2 .   ? -5.942  -4.467  -59.585 1.00 103.24 ? 567  NAG B O7  1 
HETATM 6224 C C1  . NAG O 2 .   ? -0.592  -1.068  -57.807 1.00 121.75 ? 569  NAG B C1  1 
HETATM 6225 C C2  . NAG O 2 .   ? 0.852   -1.011  -57.306 1.00 124.45 ? 569  NAG B C2  1 
HETATM 6226 C C3  . NAG O 2 .   ? 1.789   -0.661  -58.460 1.00 124.10 ? 569  NAG B C3  1 
HETATM 6227 C C4  . NAG O 2 .   ? 1.473   -1.517  -59.685 1.00 124.02 ? 569  NAG B C4  1 
HETATM 6228 C C5  . NAG O 2 .   ? 0.054   -1.272  -60.204 1.00 123.84 ? 569  NAG B C5  1 
HETATM 6229 C C6  . NAG O 2 .   ? -0.606  -2.513  -60.767 1.00 122.79 ? 569  NAG B C6  1 
HETATM 6230 C C7  . NAG O 2 .   ? 1.169   -0.359  -54.940 1.00 126.40 ? 569  NAG B C7  1 
HETATM 6231 C C8  . NAG O 2 .   ? 1.200   0.789   -53.976 1.00 125.27 ? 569  NAG B C8  1 
HETATM 6232 N N2  . NAG O 2 .   ? 0.970   -0.034  -56.233 1.00 126.30 ? 569  NAG B N2  1 
HETATM 6233 O O3  . NAG O 2 .   ? 3.130   -0.896  -58.044 1.00 122.99 ? 569  NAG B O3  1 
HETATM 6234 O O4  . NAG O 2 .   ? 2.400   -1.233  -60.729 1.00 123.14 ? 569  NAG B O4  1 
HETATM 6235 O O5  . NAG O 2 .   ? -0.818  -0.729  -59.189 1.00 123.40 ? 569  NAG B O5  1 
HETATM 6236 O O6  . NAG O 2 .   ? -1.950  -2.273  -61.179 1.00 121.51 ? 569  NAG B O6  1 
HETATM 6237 O O7  . NAG O 2 .   ? 1.315   -1.522  -54.571 1.00 127.12 ? 569  NAG B O7  1 
HETATM 6238 O O   . HOH P 5 .   ? -16.573 -19.277 -35.140 1.00 67.45  ? 2001 HOH A O   1 
HETATM 6239 O O   . HOH P 5 .   ? -5.970  -24.465 -38.350 1.00 69.49  ? 2002 HOH A O   1 
HETATM 6240 O O   . HOH P 5 .   ? -54.071 11.981  -35.725 1.00 22.51  ? 2003 HOH A O   1 
HETATM 6241 O O   . HOH Q 5 .   ? -13.033 -25.542 -43.468 1.00 43.75  ? 2001 HOH B O   1 
HETATM 6242 O O   . HOH Q 5 .   ? -11.116 -28.485 -43.401 1.00 26.63  ? 2002 HOH B O   1 
HETATM 6243 O O   . HOH Q 5 .   ? 23.647  -64.414 -37.166 1.00 33.66  ? 2003 HOH B O   1 
# 
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   1   MET MET A . n 
A 1 2   ARG 2   2   2   ARG ARG A . n 
A 1 3   CYS 3   3   3   CYS CYS A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   GLY 5   5   5   GLY GLY A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   ASN 8   8   8   ASN ASN A . n 
A 1 9   ARG 9   9   9   ARG ARG A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  PHE 11  11  11  PHE PHE A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  TRP 20  20  20  TRP TRP A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  HIS 27  27  27  HIS HIS A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  CYS 30  30  30  CYS CYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  MET 34  34  34  MET MET A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  ASP 42  42  42  ASP ASP A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  THR 48  48  48  THR THR A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  GLN 52  52  52  GLN GLN A . n 
A 1 53  PRO 53  53  53  PRO PRO A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  ARG 57  57  57  ARG ARG A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  CYS 60  60  60  CYS CYS A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  LYS 64  64  64  LYS LYS A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  THR 68  68  68  THR THR A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  CYS 74  74  74  CYS CYS A . n 
A 1 75  PRO 75  75  75  PRO PRO A . n 
A 1 76  THR 76  76  76  THR THR A . n 
A 1 77  GLN 77  77  77  GLN GLN A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  PRO 80  80  80  PRO PRO A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ASN 83  83  83  ASN ASN A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  GLN 86  86  86  GLN GLN A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  MET 96  96  96  MET MET A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 TRP 101 101 101 TRP TRP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 CYS 105 105 105 CYS CYS A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 PHE 108 108 108 PHE PHE A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 CYS 116 116 116 CYS CYS A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 CYS 121 121 121 CYS CYS A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 LYS 123 123 123 LYS LYS A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 MET 125 125 125 MET MET A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 THR 138 138 138 THR THR A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 VAL 140 140 140 VAL VAL A . n 
A 1 141 ILE 141 141 141 ILE ILE A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 HIS 144 144 144 HIS HIS A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 HIS 149 149 149 HIS HIS A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 ASN 153 153 153 ASN ASN A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 THR 155 155 155 THR THR A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 HIS 158 158 158 HIS HIS A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 LYS 160 160 160 LYS LYS A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 ILE 162 162 162 ILE ILE A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 THR 165 165 165 THR THR A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 GLN 167 167 167 GLN GLN A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 THR 171 171 171 THR THR A . n 
A 1 172 GLU 172 172 172 GLU GLU A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 TYR 178 178 178 TYR TYR A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 MET 183 183 183 MET MET A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 CYS 185 185 185 CYS CYS A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 PRO 187 187 187 PRO PRO A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 GLY 190 190 ?   ?   ?   A . n 
A 1 191 LEU 191 191 ?   ?   ?   A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 PHE 193 193 193 PHE PHE A . n 
A 1 194 ASN 194 194 194 ASN ASN A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 MET 196 196 196 MET MET A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 GLN 200 200 200 GLN GLN A . n 
A 1 201 MET 201 201 201 MET MET A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 TRP 206 206 206 TRP TRP A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 HIS 209 209 209 HIS HIS A . n 
A 1 210 ARG 210 210 210 ARG ARG A . n 
A 1 211 GLN 211 211 211 GLN GLN A . n 
A 1 212 TRP 212 212 212 TRP TRP A . n 
A 1 213 PHE 213 213 213 PHE PHE A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 PRO 217 217 217 PRO PRO A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 PRO 219 219 219 PRO PRO A . n 
A 1 220 TRP 220 220 220 TRP TRP A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 GLY 223 223 223 GLY GLY A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 ASP 225 225 225 ASP ASP A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 GLY 228 228 228 GLY GLY A . n 
A 1 229 SER 229 229 229 SER SER A . n 
A 1 230 ASN 230 230 230 ASN ASN A . n 
A 1 231 TRP 231 231 231 TRP TRP A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 GLN 233 233 233 GLN GLN A . n 
A 1 234 LYS 234 234 234 LYS LYS A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 THR 236 236 236 THR THR A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 THR 239 239 239 THR THR A . n 
A 1 240 PHE 240 240 240 PHE PHE A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 ASN 242 242 242 ASN ASN A . n 
A 1 243 PRO 243 243 243 PRO PRO A . n 
A 1 244 HIS 244 244 244 HIS HIS A . n 
A 1 245 ALA 245 245 245 ALA ALA A . n 
A 1 246 LYS 246 246 246 LYS LYS A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 ASP 249 249 249 ASP ASP A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 VAL 251 251 251 VAL VAL A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 GLY 254 254 254 GLY GLY A . n 
A 1 255 SER 255 255 255 SER SER A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 GLU 257 257 257 GLU GLU A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 MET 260 260 260 MET MET A . n 
A 1 261 HIS 261 261 261 HIS HIS A . n 
A 1 262 THR 262 262 262 THR THR A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 ALA 267 267 267 ALA ALA A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 ILE 270 270 270 ILE ILE A . n 
A 1 271 GLN 271 271 271 GLN GLN A . n 
A 1 272 MET 272 272 272 MET MET A . n 
A 1 273 SER 273 273 273 SER SER A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 ASN 276 276 276 ASN ASN A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 THR 280 280 ?   ?   ?   A . n 
A 1 281 GLY 281 281 ?   ?   ?   A . n 
A 1 282 HIS 282 282 282 HIS HIS A . n 
A 1 283 LEU 283 283 283 LEU LEU A . n 
A 1 284 LYS 284 284 284 LYS LYS A . n 
A 1 285 CYS 285 285 285 CYS CYS A . n 
A 1 286 ARG 286 286 286 ARG ARG A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 ARG 288 288 288 ARG ARG A . n 
A 1 289 MET 289 289 289 MET MET A . n 
A 1 290 ASP 290 290 290 ASP ASP A . n 
A 1 291 LYS 291 291 291 LYS LYS A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 GLN 293 293 293 GLN GLN A . n 
A 1 294 LEU 294 294 294 LEU LEU A . n 
A 1 295 LYS 295 295 295 LYS LYS A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 MET 297 297 297 MET MET A . n 
A 1 298 SER 298 298 298 SER SER A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 SER 300 300 300 SER SER A . n 
A 1 301 MET 301 301 301 MET MET A . n 
A 1 302 CYS 302 302 302 CYS CYS A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 GLY 304 304 304 GLY GLY A . n 
A 1 305 LYS 305 305 305 LYS LYS A . n 
A 1 306 PHE 306 306 306 PHE PHE A . n 
A 1 307 LYS 307 307 307 LYS LYS A . n 
A 1 308 ILE 308 308 308 ILE ILE A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 ILE 312 312 312 ILE ILE A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 GLU 314 314 314 GLU GLU A . n 
A 1 315 THR 315 315 315 THR THR A . n 
A 1 316 GLN 316 316 316 GLN GLN A . n 
A 1 317 HIS 317 317 317 HIS HIS A . n 
A 1 318 GLY 318 318 318 GLY GLY A . n 
A 1 319 THR 319 319 319 THR THR A . n 
A 1 320 ILE 320 320 320 ILE ILE A . n 
A 1 321 VAL 321 321 321 VAL VAL A . n 
A 1 322 ILE 322 322 322 ILE ILE A . n 
A 1 323 ARG 323 323 323 ARG ARG A . n 
A 1 324 VAL 324 324 324 VAL VAL A . n 
A 1 325 GLN 325 325 325 GLN GLN A . n 
A 1 326 TYR 326 326 326 TYR TYR A . n 
A 1 327 GLU 327 327 327 GLU GLU A . n 
A 1 328 GLY 328 328 328 GLY GLY A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 GLY 330 330 330 GLY GLY A . n 
A 1 331 SER 331 331 331 SER SER A . n 
A 1 332 PRO 332 332 332 PRO PRO A . n 
A 1 333 CYS 333 333 333 CYS CYS A . n 
A 1 334 LYS 334 334 334 LYS LYS A . n 
A 1 335 ILE 335 335 335 ILE ILE A . n 
A 1 336 PRO 336 336 336 PRO PRO A . n 
A 1 337 PHE 337 337 337 PHE PHE A . n 
A 1 338 GLU 338 338 338 GLU GLU A . n 
A 1 339 ILE 339 339 339 ILE ILE A . n 
A 1 340 THR 340 340 340 THR THR A . n 
A 1 341 ASP 341 341 341 ASP ASP A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 GLU 343 343 343 GLU GLU A . n 
A 1 344 LYS 344 344 344 LYS LYS A . n 
A 1 345 ARG 345 345 345 ARG ARG A . n 
A 1 346 HIS 346 346 346 HIS HIS A . n 
A 1 347 VAL 347 347 347 VAL VAL A . n 
A 1 348 LEU 348 348 348 LEU LEU A . n 
A 1 349 GLY 349 349 349 GLY GLY A . n 
A 1 350 ARG 350 350 350 ARG ARG A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 ILE 352 352 352 ILE ILE A . n 
A 1 353 THR 353 353 353 THR THR A . n 
A 1 354 VAL 354 354 354 VAL VAL A . n 
A 1 355 ASN 355 355 355 ASN ASN A . n 
A 1 356 PRO 356 356 356 PRO PRO A . n 
A 1 357 ILE 357 357 357 ILE ILE A . n 
A 1 358 VAL 358 358 358 VAL VAL A . n 
A 1 359 THR 359 359 359 THR THR A . n 
A 1 360 GLU 360 360 360 GLU GLU A . n 
A 1 361 LYS 361 361 361 LYS LYS A . n 
A 1 362 ASP 362 362 362 ASP ASP A . n 
A 1 363 SER 363 363 363 SER SER A . n 
A 1 364 PRO 364 364 364 PRO PRO A . n 
A 1 365 VAL 365 365 365 VAL VAL A . n 
A 1 366 ASN 366 366 366 ASN ASN A . n 
A 1 367 ILE 367 367 367 ILE ILE A . n 
A 1 368 GLU 368 368 368 GLU GLU A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 GLU 370 370 370 GLU GLU A . n 
A 1 371 PRO 371 371 371 PRO PRO A . n 
A 1 372 PRO 372 372 372 PRO PRO A . n 
A 1 373 PHE 373 373 373 PHE PHE A . n 
A 1 374 GLY 374 374 374 GLY GLY A . n 
A 1 375 ASP 375 375 375 ASP ASP A . n 
A 1 376 SER 376 376 376 SER SER A . n 
A 1 377 TYR 377 377 377 TYR TYR A . n 
A 1 378 ILE 378 378 378 ILE ILE A . n 
A 1 379 ILE 379 379 379 ILE ILE A . n 
A 1 380 VAL 380 380 380 VAL VAL A . n 
A 1 381 GLY 381 381 381 GLY GLY A . n 
A 1 382 VAL 382 382 382 VAL VAL A . n 
A 1 383 GLU 383 383 383 GLU GLU A . n 
A 1 384 PRO 384 384 384 PRO PRO A . n 
A 1 385 GLY 385 385 385 GLY GLY A . n 
A 1 386 GLN 386 386 386 GLN GLN A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 LYS 388 388 388 LYS LYS A . n 
A 1 389 LEU 389 389 389 LEU LEU A . n 
A 1 390 ASN 390 390 390 ASN ASN A . n 
A 1 391 TRP 391 391 391 TRP TRP A . n 
A 1 392 LEU 392 392 392 LEU LEU A . n 
A 1 393 ARG 393 393 393 ARG ARG A . n 
A 1 394 PRO 394 394 394 PRO PRO A . n 
A 1 395 LEU 395 395 395 LEU LEU A . n 
A 1 396 GLU 396 396 ?   ?   ?   A . n 
A 1 397 SER 397 397 ?   ?   ?   A . n 
A 1 398 ARG 398 398 ?   ?   ?   A . n 
A 1 399 GLY 399 399 ?   ?   ?   A . n 
A 1 400 PRO 400 400 ?   ?   ?   A . n 
A 1 401 PHE 401 401 ?   ?   ?   A . n 
A 1 402 GLU 402 402 ?   ?   ?   A . n 
A 1 403 GLY 403 403 ?   ?   ?   A . n 
A 1 404 LYS 404 404 ?   ?   ?   A . n 
A 1 405 PRO 405 405 ?   ?   ?   A . n 
A 1 406 ILE 406 406 ?   ?   ?   A . n 
A 1 407 PRO 407 407 ?   ?   ?   A . n 
A 1 408 ASN 408 408 ?   ?   ?   A . n 
A 1 409 PRO 409 409 ?   ?   ?   A . n 
A 1 410 LEU 410 410 ?   ?   ?   A . n 
A 1 411 LEU 411 411 ?   ?   ?   A . n 
A 1 412 GLY 412 412 ?   ?   ?   A . n 
A 1 413 LEU 413 413 ?   ?   ?   A . n 
A 1 414 ASP 414 414 ?   ?   ?   A . n 
A 1 415 SER 415 415 ?   ?   ?   A . n 
A 1 416 THR 416 416 ?   ?   ?   A . n 
A 1 417 ARG 417 417 ?   ?   ?   A . n 
A 1 418 THR 418 418 ?   ?   ?   A . n 
A 1 419 GLY 419 419 ?   ?   ?   A . n 
A 1 420 HIS 420 420 ?   ?   ?   A . n 
A 1 421 HIS 421 421 ?   ?   ?   A . n 
A 1 422 HIS 422 422 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   ARG 2   2   2   ARG ARG B . n 
B 1 3   CYS 3   3   3   CYS CYS B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   GLY 5   5   5   GLY GLY B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   ASN 8   8   8   ASN ASN B . n 
B 1 9   ARG 9   9   9   ARG ARG B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  PHE 11  11  11  PHE PHE B . n 
B 1 12  VAL 12  12  12  VAL VAL B . n 
B 1 13  GLU 13  13  13  GLU GLU B . n 
B 1 14  GLY 14  14  14  GLY GLY B . n 
B 1 15  VAL 15  15  ?   ?   ?   B . n 
B 1 16  SER 16  16  ?   ?   ?   B . n 
B 1 17  GLY 17  17  ?   ?   ?   B . n 
B 1 18  GLY 18  18  ?   ?   ?   B . n 
B 1 19  SER 19  19  ?   ?   ?   B . n 
B 1 20  TRP 20  20  20  TRP TRP B . n 
B 1 21  VAL 21  21  21  VAL VAL B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  HIS 27  27  27  HIS HIS B . n 
B 1 28  GLY 28  28  28  GLY GLY B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  CYS 30  30  30  CYS CYS B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  MET 34  34  34  MET MET B . n 
B 1 35  ALA 35  35  35  ALA ALA B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  LYS 38  38  38  LYS LYS B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  LEU 41  41  41  LEU LEU B . n 
B 1 42  ASP 42  42  42  ASP ASP B . n 
B 1 43  PHE 43  43  43  PHE PHE B . n 
B 1 44  GLU 44  44  44  GLU GLU B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  LYS 47  47  47  LYS LYS B . n 
B 1 48  THR 48  48  48  THR THR B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  LYS 51  51  51  LYS LYS B . n 
B 1 52  GLN 52  52  52  GLN GLN B . n 
B 1 53  PRO 53  53  53  PRO PRO B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  THR 55  55  55  THR THR B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  ARG 57  57  57  ARG ARG B . n 
B 1 58  LYS 58  58  58  LYS LYS B . n 
B 1 59  TYR 59  59  59  TYR TYR B . n 
B 1 60  CYS 60  60  60  CYS CYS B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  ALA 63  63  63  ALA ALA B . n 
B 1 64  LYS 64  64  64  LYS LYS B . n 
B 1 65  LEU 65  65  65  LEU LEU B . n 
B 1 66  THR 66  66  66  THR THR B . n 
B 1 67  ASN 67  67  67  ASN ASN B . n 
B 1 68  THR 68  68  68  THR THR B . n 
B 1 69  THR 69  69  69  THR THR B . n 
B 1 70  THR 70  70  70  THR THR B . n 
B 1 71  GLU 71  71  71  GLU GLU B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  ARG 73  73  73  ARG ARG B . n 
B 1 74  CYS 74  74  74  CYS CYS B . n 
B 1 75  PRO 75  75  75  PRO PRO B . n 
B 1 76  THR 76  76  76  THR THR B . n 
B 1 77  GLN 77  77  77  GLN GLN B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLU 79  79  79  GLU GLU B . n 
B 1 80  PRO 80  80  80  PRO PRO B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  LEU 82  82  82  LEU LEU B . n 
B 1 83  ASN 83  83  83  ASN ASN B . n 
B 1 84  GLU 84  84  84  GLU GLU B . n 
B 1 85  GLU 85  85  85  GLU GLU B . n 
B 1 86  GLN 86  86  86  GLN GLN B . n 
B 1 87  ASP 87  87  87  ASP ASP B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  ARG 89  89  89  ARG ARG B . n 
B 1 90  PHE 90  90  90  PHE PHE B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LYS 93  93  93  LYS LYS B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  SER 95  95  95  SER SER B . n 
B 1 96  MET 96  96  96  MET MET B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  ASP 98  98  98  ASP ASP B . n 
B 1 99  ARG 99  99  99  ARG ARG B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 TRP 101 101 101 TRP TRP B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 ASN 103 103 103 ASN ASN B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 CYS 105 105 105 CYS CYS B . n 
B 1 106 GLY 106 106 106 GLY GLY B . n 
B 1 107 LEU 107 107 107 LEU LEU B . n 
B 1 108 PHE 108 108 108 PHE PHE B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 GLY 111 111 111 GLY GLY B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 THR 115 115 115 THR THR B . n 
B 1 116 CYS 116 116 116 CYS CYS B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 LYS 118 118 118 LYS LYS B . n 
B 1 119 PHE 119 119 119 PHE PHE B . n 
B 1 120 THR 120 120 120 THR THR B . n 
B 1 121 CYS 121 121 121 CYS CYS B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 LYS 123 123 123 LYS LYS B . n 
B 1 124 ASN 124 124 124 ASN ASN B . n 
B 1 125 MET 125 125 125 MET MET B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 ILE 129 129 129 ILE ILE B . n 
B 1 130 VAL 130 130 130 VAL VAL B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 GLU 136 136 136 GLU GLU B . n 
B 1 137 TYR 137 137 137 TYR TYR B . n 
B 1 138 THR 138 138 138 THR THR B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 VAL 140 140 140 VAL VAL B . n 
B 1 141 ILE 141 141 141 ILE ILE B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 PRO 143 143 143 PRO PRO B . n 
B 1 144 HIS 144 144 144 HIS HIS B . n 
B 1 145 SER 145 145 145 SER SER B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 HIS 149 149 149 HIS HIS B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 GLY 152 152 152 GLY GLY B . n 
B 1 153 ASN 153 153 153 ASN ASN B . n 
B 1 154 ASP 154 154 154 ASP ASP B . n 
B 1 155 THR 155 155 155 THR THR B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 LYS 157 157 157 LYS LYS B . n 
B 1 158 HIS 158 158 158 HIS HIS B . n 
B 1 159 GLY 159 159 159 GLY GLY B . n 
B 1 160 LYS 160 160 160 LYS LYS B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 ILE 162 162 162 ILE ILE B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 ILE 164 164 164 ILE ILE B . n 
B 1 165 THR 165 165 165 THR THR B . n 
B 1 166 PRO 166 166 166 PRO PRO B . n 
B 1 167 GLN 167 167 167 GLN GLN B . n 
B 1 168 SER 168 168 168 SER SER B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 THR 170 170 170 THR THR B . n 
B 1 171 THR 171 171 171 THR THR B . n 
B 1 172 GLU 172 172 172 GLU GLU B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 GLU 174 174 174 GLU GLU B . n 
B 1 175 LEU 175 175 175 LEU LEU B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 GLY 177 177 177 GLY GLY B . n 
B 1 178 TYR 178 178 178 TYR TYR B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 THR 180 180 180 THR THR B . n 
B 1 181 VAL 181 181 181 VAL VAL B . n 
B 1 182 THR 182 182 182 THR THR B . n 
B 1 183 MET 183 183 183 MET MET B . n 
B 1 184 GLU 184 184 184 GLU GLU B . n 
B 1 185 CYS 185 185 185 CYS CYS B . n 
B 1 186 SER 186 186 186 SER SER B . n 
B 1 187 PRO 187 187 187 PRO PRO B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 THR 189 189 189 THR THR B . n 
B 1 190 GLY 190 190 190 GLY GLY B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 ASP 192 192 192 ASP ASP B . n 
B 1 193 PHE 193 193 193 PHE PHE B . n 
B 1 194 ASN 194 194 194 ASN ASN B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 MET 196 196 196 MET MET B . n 
B 1 197 VAL 197 197 197 VAL VAL B . n 
B 1 198 LEU 198 198 198 LEU LEU B . n 
B 1 199 LEU 199 199 199 LEU LEU B . n 
B 1 200 GLN 200 200 200 GLN GLN B . n 
B 1 201 MET 201 201 201 MET MET B . n 
B 1 202 GLU 202 202 202 GLU GLU B . n 
B 1 203 ASP 203 203 203 ASP ASP B . n 
B 1 204 LYS 204 204 204 LYS LYS B . n 
B 1 205 ALA 205 205 205 ALA ALA B . n 
B 1 206 TRP 206 206 206 TRP TRP B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 VAL 208 208 208 VAL VAL B . n 
B 1 209 HIS 209 209 209 HIS HIS B . n 
B 1 210 ARG 210 210 210 ARG ARG B . n 
B 1 211 GLN 211 211 211 GLN GLN B . n 
B 1 212 TRP 212 212 212 TRP TRP B . n 
B 1 213 PHE 213 213 213 PHE PHE B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 ASP 215 215 215 ASP ASP B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 PRO 217 217 217 PRO PRO B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 PRO 219 219 219 PRO PRO B . n 
B 1 220 TRP 220 220 220 TRP TRP B . n 
B 1 221 LEU 221 221 221 LEU LEU B . n 
B 1 222 PRO 222 222 222 PRO PRO B . n 
B 1 223 GLY 223 223 223 GLY GLY B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 ASP 225 225 225 ASP ASP B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 GLN 227 227 227 GLN GLN B . n 
B 1 228 GLY 228 228 228 GLY GLY B . n 
B 1 229 SER 229 229 229 SER SER B . n 
B 1 230 ASN 230 230 230 ASN ASN B . n 
B 1 231 TRP 231 231 231 TRP TRP B . n 
B 1 232 ILE 232 232 232 ILE ILE B . n 
B 1 233 GLN 233 233 233 GLN GLN B . n 
B 1 234 LYS 234 234 234 LYS LYS B . n 
B 1 235 GLU 235 235 235 GLU GLU B . n 
B 1 236 THR 236 236 236 THR THR B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 VAL 238 238 238 VAL VAL B . n 
B 1 239 THR 239 239 239 THR THR B . n 
B 1 240 PHE 240 240 240 PHE PHE B . n 
B 1 241 LYS 241 241 241 LYS LYS B . n 
B 1 242 ASN 242 242 242 ASN ASN B . n 
B 1 243 PRO 243 243 243 PRO PRO B . n 
B 1 244 HIS 244 244 244 HIS HIS B . n 
B 1 245 ALA 245 245 245 ALA ALA B . n 
B 1 246 LYS 246 246 246 LYS LYS B . n 
B 1 247 LYS 247 247 247 LYS LYS B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 ASP 249 249 249 ASP ASP B . n 
B 1 250 VAL 250 250 250 VAL VAL B . n 
B 1 251 VAL 251 251 251 VAL VAL B . n 
B 1 252 VAL 252 252 252 VAL VAL B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 GLY 254 254 254 GLY GLY B . n 
B 1 255 SER 255 255 255 SER SER B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 GLU 257 257 257 GLU GLU B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 ALA 259 259 259 ALA ALA B . n 
B 1 260 MET 260 260 260 MET MET B . n 
B 1 261 HIS 261 261 261 HIS HIS B . n 
B 1 262 THR 262 262 262 THR THR B . n 
B 1 263 ALA 263 263 263 ALA ALA B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 THR 265 265 265 THR THR B . n 
B 1 266 GLY 266 266 266 GLY GLY B . n 
B 1 267 ALA 267 267 267 ALA ALA B . n 
B 1 268 THR 268 268 268 THR THR B . n 
B 1 269 GLU 269 269 269 GLU GLU B . n 
B 1 270 ILE 270 270 270 ILE ILE B . n 
B 1 271 GLN 271 271 271 GLN GLN B . n 
B 1 272 MET 272 272 272 MET MET B . n 
B 1 273 SER 273 273 273 SER SER B . n 
B 1 274 SER 274 274 274 SER SER B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 ASN 276 276 276 ASN ASN B . n 
B 1 277 LEU 277 277 277 LEU LEU B . n 
B 1 278 LEU 278 278 278 LEU LEU B . n 
B 1 279 PHE 279 279 279 PHE PHE B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 GLY 281 281 281 GLY GLY B . n 
B 1 282 HIS 282 282 282 HIS HIS B . n 
B 1 283 LEU 283 283 283 LEU LEU B . n 
B 1 284 LYS 284 284 284 LYS LYS B . n 
B 1 285 CYS 285 285 285 CYS CYS B . n 
B 1 286 ARG 286 286 286 ARG ARG B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 ARG 288 288 288 ARG ARG B . n 
B 1 289 MET 289 289 289 MET MET B . n 
B 1 290 ASP 290 290 290 ASP ASP B . n 
B 1 291 LYS 291 291 291 LYS LYS B . n 
B 1 292 LEU 292 292 292 LEU LEU B . n 
B 1 293 GLN 293 293 293 GLN GLN B . n 
B 1 294 LEU 294 294 294 LEU LEU B . n 
B 1 295 LYS 295 295 295 LYS LYS B . n 
B 1 296 GLY 296 296 296 GLY GLY B . n 
B 1 297 MET 297 297 297 MET MET B . n 
B 1 298 SER 298 298 298 SER SER B . n 
B 1 299 TYR 299 299 299 TYR TYR B . n 
B 1 300 SER 300 300 300 SER SER B . n 
B 1 301 MET 301 301 301 MET MET B . n 
B 1 302 CYS 302 302 302 CYS CYS B . n 
B 1 303 THR 303 303 303 THR THR B . n 
B 1 304 GLY 304 304 304 GLY GLY B . n 
B 1 305 LYS 305 305 305 LYS LYS B . n 
B 1 306 PHE 306 306 306 PHE PHE B . n 
B 1 307 LYS 307 307 307 LYS LYS B . n 
B 1 308 ILE 308 308 308 ILE ILE B . n 
B 1 309 VAL 309 309 309 VAL VAL B . n 
B 1 310 LYS 310 310 310 LYS LYS B . n 
B 1 311 GLU 311 311 311 GLU GLU B . n 
B 1 312 ILE 312 312 312 ILE ILE B . n 
B 1 313 ALA 313 313 313 ALA ALA B . n 
B 1 314 GLU 314 314 314 GLU GLU B . n 
B 1 315 THR 315 315 315 THR THR B . n 
B 1 316 GLN 316 316 316 GLN GLN B . n 
B 1 317 HIS 317 317 317 HIS HIS B . n 
B 1 318 GLY 318 318 318 GLY GLY B . n 
B 1 319 THR 319 319 319 THR THR B . n 
B 1 320 ILE 320 320 320 ILE ILE B . n 
B 1 321 VAL 321 321 321 VAL VAL B . n 
B 1 322 ILE 322 322 322 ILE ILE B . n 
B 1 323 ARG 323 323 323 ARG ARG B . n 
B 1 324 VAL 324 324 324 VAL VAL B . n 
B 1 325 GLN 325 325 325 GLN GLN B . n 
B 1 326 TYR 326 326 326 TYR TYR B . n 
B 1 327 GLU 327 327 327 GLU GLU B . n 
B 1 328 GLY 328 328 328 GLY GLY B . n 
B 1 329 ASP 329 329 329 ASP ASP B . n 
B 1 330 GLY 330 330 330 GLY GLY B . n 
B 1 331 SER 331 331 331 SER SER B . n 
B 1 332 PRO 332 332 332 PRO PRO B . n 
B 1 333 CYS 333 333 333 CYS CYS B . n 
B 1 334 LYS 334 334 334 LYS LYS B . n 
B 1 335 ILE 335 335 335 ILE ILE B . n 
B 1 336 PRO 336 336 336 PRO PRO B . n 
B 1 337 PHE 337 337 337 PHE PHE B . n 
B 1 338 GLU 338 338 338 GLU GLU B . n 
B 1 339 ILE 339 339 339 ILE ILE B . n 
B 1 340 THR 340 340 340 THR THR B . n 
B 1 341 ASP 341 341 341 ASP ASP B . n 
B 1 342 LEU 342 342 342 LEU LEU B . n 
B 1 343 GLU 343 343 343 GLU GLU B . n 
B 1 344 LYS 344 344 344 LYS LYS B . n 
B 1 345 ARG 345 345 345 ARG ARG B . n 
B 1 346 HIS 346 346 346 HIS HIS B . n 
B 1 347 VAL 347 347 347 VAL VAL B . n 
B 1 348 LEU 348 348 348 LEU LEU B . n 
B 1 349 GLY 349 349 349 GLY GLY B . n 
B 1 350 ARG 350 350 350 ARG ARG B . n 
B 1 351 LEU 351 351 351 LEU LEU B . n 
B 1 352 ILE 352 352 352 ILE ILE B . n 
B 1 353 THR 353 353 353 THR THR B . n 
B 1 354 VAL 354 354 354 VAL VAL B . n 
B 1 355 ASN 355 355 355 ASN ASN B . n 
B 1 356 PRO 356 356 356 PRO PRO B . n 
B 1 357 ILE 357 357 357 ILE ILE B . n 
B 1 358 VAL 358 358 358 VAL VAL B . n 
B 1 359 THR 359 359 359 THR THR B . n 
B 1 360 GLU 360 360 360 GLU GLU B . n 
B 1 361 LYS 361 361 361 LYS LYS B . n 
B 1 362 ASP 362 362 362 ASP ASP B . n 
B 1 363 SER 363 363 363 SER SER B . n 
B 1 364 PRO 364 364 364 PRO PRO B . n 
B 1 365 VAL 365 365 365 VAL VAL B . n 
B 1 366 ASN 366 366 366 ASN ASN B . n 
B 1 367 ILE 367 367 367 ILE ILE B . n 
B 1 368 GLU 368 368 368 GLU GLU B . n 
B 1 369 ALA 369 369 369 ALA ALA B . n 
B 1 370 GLU 370 370 370 GLU GLU B . n 
B 1 371 PRO 371 371 371 PRO PRO B . n 
B 1 372 PRO 372 372 372 PRO PRO B . n 
B 1 373 PHE 373 373 373 PHE PHE B . n 
B 1 374 GLY 374 374 374 GLY GLY B . n 
B 1 375 ASP 375 375 375 ASP ASP B . n 
B 1 376 SER 376 376 376 SER SER B . n 
B 1 377 TYR 377 377 377 TYR TYR B . n 
B 1 378 ILE 378 378 378 ILE ILE B . n 
B 1 379 ILE 379 379 379 ILE ILE B . n 
B 1 380 VAL 380 380 380 VAL VAL B . n 
B 1 381 GLY 381 381 381 GLY GLY B . n 
B 1 382 VAL 382 382 382 VAL VAL B . n 
B 1 383 GLU 383 383 383 GLU GLU B . n 
B 1 384 PRO 384 384 384 PRO PRO B . n 
B 1 385 GLY 385 385 385 GLY GLY B . n 
B 1 386 GLN 386 386 386 GLN GLN B . n 
B 1 387 LEU 387 387 387 LEU LEU B . n 
B 1 388 LYS 388 388 388 LYS LYS B . n 
B 1 389 LEU 389 389 389 LEU LEU B . n 
B 1 390 ASN 390 390 390 ASN ASN B . n 
B 1 391 TRP 391 391 391 TRP TRP B . n 
B 1 392 LEU 392 392 392 LEU LEU B . n 
B 1 393 ARG 393 393 393 ARG ARG B . n 
B 1 394 PRO 394 394 394 PRO PRO B . n 
B 1 395 LEU 395 395 395 LEU LEU B . n 
B 1 396 GLU 396 396 ?   ?   ?   B . n 
B 1 397 SER 397 397 ?   ?   ?   B . n 
B 1 398 ARG 398 398 ?   ?   ?   B . n 
B 1 399 GLY 399 399 ?   ?   ?   B . n 
B 1 400 PRO 400 400 ?   ?   ?   B . n 
B 1 401 PHE 401 401 ?   ?   ?   B . n 
B 1 402 GLU 402 402 ?   ?   ?   B . n 
B 1 403 GLY 403 403 ?   ?   ?   B . n 
B 1 404 LYS 404 404 ?   ?   ?   B . n 
B 1 405 PRO 405 405 ?   ?   ?   B . n 
B 1 406 ILE 406 406 ?   ?   ?   B . n 
B 1 407 PRO 407 407 ?   ?   ?   B . n 
B 1 408 ASN 408 408 ?   ?   ?   B . n 
B 1 409 PRO 409 409 ?   ?   ?   B . n 
B 1 410 LEU 410 410 ?   ?   ?   B . n 
B 1 411 LEU 411 411 ?   ?   ?   B . n 
B 1 412 GLY 412 412 ?   ?   ?   B . n 
B 1 413 LEU 413 413 ?   ?   ?   B . n 
B 1 414 ASP 414 414 ?   ?   ?   B . n 
B 1 415 SER 415 415 ?   ?   ?   B . n 
B 1 416 THR 416 416 ?   ?   ?   B . n 
B 1 417 ARG 417 417 ?   ?   ?   B . n 
B 1 418 THR 418 418 ?   ?   ?   B . n 
B 1 419 GLY 419 419 ?   ?   ?   B . n 
B 1 420 HIS 420 420 ?   ?   ?   B . n 
B 1 421 HIS 421 421 ?   ?   ?   B . n 
B 1 422 HIS 422 422 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 NAG 1 501  501  NAG NAG A . 
D 3 FUC 2 502  502  FUC FUC A . 
E 2 NAG 3 503  503  NAG NAG A . 
F 2 NAG 1 567  567  NAG NAG A . 
G 2 NAG 2 569  569  NAG NAG A . 
H 2 NAG 1 501  501  NAG NAG B . 
I 3 FUC 2 502  502  FUC FUC B . 
J 2 NAG 3 503  503  NAG NAG B . 
K 4 BMA 4 504  504  BMA BMA B . 
L 4 BMA 5 505  505  BMA BMA B . 
M 4 BMA 6 506  506  BMA BMA B . 
N 2 NAG 1 567  567  NAG NAG B . 
O 2 NAG 2 569  569  NAG NAG B . 
P 5 HOH 1 2001 2001 HOH HOH A . 
P 5 HOH 2 2002 2002 HOH HOH A . 
P 5 HOH 3 2003 2003 HOH HOH A . 
Q 5 HOH 1 2001 2001 HOH HOH B . 
Q 5 HOH 2 2002 2002 HOH HOH B . 
Q 5 HOH 3 2003 2003 HOH HOH B . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 67  A ASN 67  ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 153 A ASN 153 ? ASN 'GLYCOSYLATION SITE' 
3 B ASN 67  B ASN 67  ? ASN 'GLYCOSYLATION SITE' 
4 B ASN 153 B ASN 153 ? ASN 'GLYCOSYLATION SITE' 
# 
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 monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,P       
2 1 B,H,I,J,K,L,M,N,O,Q 
# 
_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_
_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 
1 'Structure model' 1 0 2015-01-28 
2 'Structure model' 1 1 2015-04-08 
# 
_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_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_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
BUSTER refinement       2.11.4 ? 1 
XDS    'data reduction' .      ? 2 
SCALA  'data scaling'   .      ? 3 
PHASER phasing          .      ? 4 
# 
_pdbx_entry_details.entry_id             4UTC 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     
;THE RESIDUES AFTER W391 DERIVE FROM THE VECTOR. RESIDUES
392 TO 394 COMPLETE THE G STRAND OF ENVELOPE GLYCOPROTEIN
DOMAIN III. GB KM087965
;
# 
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 GLN A 52  ? ? 53.88   75.41   
2  1 THR A 76  ? ? 71.70   -2.72   
3  1 ASN A 103 ? ? -147.82 27.94   
4  1 GLU A 148 ? ? -26.60  -45.41  
5  1 ALA A 150 ? ? -30.22  -37.68  
6  1 LYS A 157 ? ? -36.30  -39.44  
7  1 THR A 176 ? ? -55.07  92.88   
8  1 PHE A 193 ? ? 67.54   -16.39  
9  1 GLU A 195 ? ? -99.30  56.24   
10 1 MET A 201 ? ? -92.02  -85.36  
11 1 GLU A 202 ? ? -118.03 -95.41  
12 1 ASP A 215 ? ? -101.13 49.62   
13 1 SER A 229 ? ? -140.45 -47.67  
14 1 GLN B 52  ? ? 43.36   74.46   
15 1 THR B 76  ? ? 69.99   -1.83   
16 1 GLU B 84  ? ? -35.77  -33.78  
17 1 ASN B 103 ? ? -144.93 27.57   
18 1 GLU B 147 ? ? -37.33  115.14  
19 1 GLU B 148 ? ? -26.98  -47.66  
20 1 THR B 176 ? ? -57.58  95.04   
21 1 LEU B 199 ? ? -69.45  96.06   
22 1 MET B 201 ? ? -92.46  -91.06  
23 1 GLU B 202 ? ? -107.16 -93.13  
24 1 SER B 274 ? ? -152.07 65.97   
25 1 SER B 331 ? ? -39.79  132.91  
26 1 ASP B 341 ? ? -68.53  -171.74 
27 1 LYS B 344 ? ? 104.05  1.23    
28 1 ARG B 345 ? ? -49.51  -91.84  
29 1 LEU B 348 ? ? -121.68 -69.93  
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 288 ? CG  ? A ARG 288 CG  
2  1 Y 1 A ARG 288 ? CD  ? A ARG 288 CD  
3  1 Y 1 A ARG 288 ? NE  ? A ARG 288 NE  
4  1 Y 1 A ARG 288 ? CZ  ? A ARG 288 CZ  
5  1 Y 1 A ARG 288 ? NH1 ? A ARG 288 NH1 
6  1 Y 1 A ARG 288 ? NH2 ? A ARG 288 NH2 
7  1 Y 1 A LEU 395 ? CG  ? A LEU 395 CG  
8  1 Y 1 A LEU 395 ? CD1 ? A LEU 395 CD1 
9  1 Y 1 A LEU 395 ? CD2 ? A LEU 395 CD2 
10 1 Y 1 B LEU 395 ? CG  ? B LEU 395 CG  
11 1 Y 1 B LEU 395 ? CD1 ? B LEU 395 CD1 
12 1 Y 1 B LEU 395 ? CD2 ? B LEU 395 CD2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 190 ? A GLY 190 
2  1 Y 1 A LEU 191 ? A LEU 191 
3  1 Y 1 A THR 280 ? A THR 280 
4  1 Y 1 A GLY 281 ? A GLY 281 
5  1 Y 1 A GLU 396 ? A GLU 396 
6  1 Y 1 A SER 397 ? A SER 397 
7  1 Y 1 A ARG 398 ? A ARG 398 
8  1 Y 1 A GLY 399 ? A GLY 399 
9  1 Y 1 A PRO 400 ? A PRO 400 
10 1 Y 1 A PHE 401 ? A PHE 401 
11 1 Y 1 A GLU 402 ? A GLU 402 
12 1 Y 1 A GLY 403 ? A GLY 403 
13 1 Y 1 A LYS 404 ? A LYS 404 
14 1 Y 1 A PRO 405 ? A PRO 405 
15 1 Y 1 A ILE 406 ? A ILE 406 
16 1 Y 1 A PRO 407 ? A PRO 407 
17 1 Y 1 A ASN 408 ? A ASN 408 
18 1 Y 1 A PRO 409 ? A PRO 409 
19 1 Y 1 A LEU 410 ? A LEU 410 
20 1 Y 1 A LEU 411 ? A LEU 411 
21 1 Y 1 A GLY 412 ? A GLY 412 
22 1 Y 1 A LEU 413 ? A LEU 413 
23 1 Y 1 A ASP 414 ? A ASP 414 
24 1 Y 1 A SER 415 ? A SER 415 
25 1 Y 1 A THR 416 ? A THR 416 
26 1 Y 1 A ARG 417 ? A ARG 417 
27 1 Y 1 A THR 418 ? A THR 418 
28 1 Y 1 A GLY 419 ? A GLY 419 
29 1 Y 1 A HIS 420 ? A HIS 420 
30 1 Y 1 A HIS 421 ? A HIS 421 
31 1 Y 1 A HIS 422 ? A HIS 422 
32 1 Y 1 B VAL 15  ? B VAL 15  
33 1 Y 1 B SER 16  ? B SER 16  
34 1 Y 1 B GLY 17  ? B GLY 17  
35 1 Y 1 B GLY 18  ? B GLY 18  
36 1 Y 1 B SER 19  ? B SER 19  
37 1 Y 1 B GLU 396 ? B GLU 396 
38 1 Y 1 B SER 397 ? B SER 397 
39 1 Y 1 B ARG 398 ? B ARG 398 
40 1 Y 1 B GLY 399 ? B GLY 399 
41 1 Y 1 B PRO 400 ? B PRO 400 
42 1 Y 1 B PHE 401 ? B PHE 401 
43 1 Y 1 B GLU 402 ? B GLU 402 
44 1 Y 1 B GLY 403 ? B GLY 403 
45 1 Y 1 B LYS 404 ? B LYS 404 
46 1 Y 1 B PRO 405 ? B PRO 405 
47 1 Y 1 B ILE 406 ? B ILE 406 
48 1 Y 1 B PRO 407 ? B PRO 407 
49 1 Y 1 B ASN 408 ? B ASN 408 
50 1 Y 1 B PRO 409 ? B PRO 409 
51 1 Y 1 B LEU 410 ? B LEU 410 
52 1 Y 1 B LEU 411 ? B LEU 411 
53 1 Y 1 B GLY 412 ? B GLY 412 
54 1 Y 1 B LEU 413 ? B LEU 413 
55 1 Y 1 B ASP 414 ? B ASP 414 
56 1 Y 1 B SER 415 ? B SER 415 
57 1 Y 1 B THR 416 ? B THR 416 
58 1 Y 1 B ARG 417 ? B ARG 417 
59 1 Y 1 B THR 418 ? B THR 418 
60 1 Y 1 B GLY 419 ? B GLY 419 
61 1 Y 1 B HIS 420 ? B HIS 420 
62 1 Y 1 B HIS 421 ? B HIS 421 
63 1 Y 1 B HIS 422 ? B HIS 422 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 ALPHA-L-FUCOSE         FUC 
4 BETA-D-MANNOSE         BMA 
5 water                  HOH 
# 
