data_4KBP
# 
_entry.id   4KBP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4KBP         
WWPDB D_1000179352 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4KBP 
_pdbx_database_status.recvd_initial_deposition_date   1995-10-02 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    BNL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Klabunde, T.' 1 
'Strater, N.'  2 
'Krebs, B.'    3 
# 
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 'Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures.'                 J.Mol.Biol. 259 737  
748 1996 JMOBAK UK 0022-2836 0070 ? 8683579 10.1006/jmbi.1996.0354 
1       'Crystal Structure of a Purple Acid Phosphatase Containing a Dinuclear Fe(III)-Zn(II) Active Site' Science     268 1489 ? 
1995 SCIEAS US 0036-8075 0038 ? ?       ?                      
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Klabunde, T.' 1  
primary 'Strater, N.'  2  
primary 'Frohlich, R.' 3  
primary 'Witzel, H.'   4  
primary 'Krebs, B.'    5  
1       'Strater, N.'  6  
1       'Klabunde, T.' 7  
1       'Tucker, P.'   8  
1       'Witzel, H.'   9  
1       'Krebs, B.'    10 
# 
_cell.entry_id           4KBP 
_cell.length_a           132.700 
_cell.length_b           347.300 
_cell.length_c           128.700 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              32 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         4KBP 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
# 
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     nat 'PURPLE ACID PHOSPHATASE' 50304.262 4  3.1.3.2 ? ? '111KDA DIMER COMPLEX WITH PHOSPHATE' 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE    221.208   20 ?       ? ? ?                                     
3 non-polymer syn 'FE (III) ION'            55.845    4  ?       ? ? ?                                     
4 non-polymer syn 'ZINC ION'                65.409    4  ?       ? ? ?                                     
5 non-polymer syn 'PHOSPHATE ION'           94.971    4  ?       ? ? ?                                     
6 water       nat water                     18.015    56 ?       ? ? ?                                     
# 
_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       
;FVRKTNKNRDMPLDSDVFRVPPGYNAPQQVHITQGDLVGRAMIISWVTMDEPGSSAVRYWSEKNGRKRIAKGKMSTYRFF
NYSSGFIHHTTIRKLKYNTKYYYEVGLRNTTRRFSFITPPQTGLDVPYTFGLIGDLGQSFDSNTTLSHYELSPKKGQTVL
FVGDLSYADRYPNHDNVRWDTWGRFTERSVAYQPWIWTAGNHEIEFAPEINETEPFKPFSYRYHVPYEASQSTSPFWYSI
KRASAHIIVLSSYSAYGRGTPQYTWLKKELRKVKRSETPWLIVLMHSPLYNSYNHHFMEGEAMRTKFEAWFVKYKVDVVF
AGHVHAYERSERVSNIAYKITDGLCTPVKDQSAPVYITIGDAGNYGVIDSNMIQPQPEYSAFREASFGHGMFDIKNRTHA
HFSWNRNQDGVAVEADSVWFFNRHWYPVDDST
;
_entity_poly.pdbx_seq_one_letter_code_can   
;FVRKTNKNRDMPLDSDVFRVPPGYNAPQQVHITQGDLVGRAMIISWVTMDEPGSSAVRYWSEKNGRKRIAKGKMSTYRFF
NYSSGFIHHTTIRKLKYNTKYYYEVGLRNTTRRFSFITPPQTGLDVPYTFGLIGDLGQSFDSNTTLSHYELSPKKGQTVL
FVGDLSYADRYPNHDNVRWDTWGRFTERSVAYQPWIWTAGNHEIEFAPEINETEPFKPFSYRYHVPYEASQSTSPFWYSI
KRASAHIIVLSSYSAYGRGTPQYTWLKKELRKVKRSETPWLIVLMHSPLYNSYNHHFMEGEAMRTKFEAWFVKYKVDVVF
AGHVHAYERSERVSNIAYKITDGLCTPVKDQSAPVYITIGDAGNYGVIDSNMIQPQPEYSAFREASFGHGMFDIKNRTHA
HFSWNRNQDGVAVEADSVWFFNRHWYPVDDST
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_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   PHE n 
1 2   VAL n 
1 3   ARG n 
1 4   LYS n 
1 5   THR n 
1 6   ASN n 
1 7   LYS n 
1 8   ASN n 
1 9   ARG n 
1 10  ASP n 
1 11  MET n 
1 12  PRO n 
1 13  LEU n 
1 14  ASP n 
1 15  SER n 
1 16  ASP n 
1 17  VAL n 
1 18  PHE n 
1 19  ARG n 
1 20  VAL n 
1 21  PRO n 
1 22  PRO n 
1 23  GLY n 
1 24  TYR n 
1 25  ASN n 
1 26  ALA n 
1 27  PRO n 
1 28  GLN n 
1 29  GLN n 
1 30  VAL n 
1 31  HIS n 
1 32  ILE n 
1 33  THR n 
1 34  GLN n 
1 35  GLY n 
1 36  ASP n 
1 37  LEU n 
1 38  VAL n 
1 39  GLY n 
1 40  ARG n 
1 41  ALA n 
1 42  MET n 
1 43  ILE n 
1 44  ILE n 
1 45  SER n 
1 46  TRP n 
1 47  VAL n 
1 48  THR n 
1 49  MET n 
1 50  ASP n 
1 51  GLU n 
1 52  PRO n 
1 53  GLY n 
1 54  SER n 
1 55  SER n 
1 56  ALA n 
1 57  VAL n 
1 58  ARG n 
1 59  TYR n 
1 60  TRP n 
1 61  SER n 
1 62  GLU n 
1 63  LYS n 
1 64  ASN n 
1 65  GLY n 
1 66  ARG n 
1 67  LYS n 
1 68  ARG n 
1 69  ILE n 
1 70  ALA n 
1 71  LYS n 
1 72  GLY n 
1 73  LYS n 
1 74  MET n 
1 75  SER n 
1 76  THR n 
1 77  TYR n 
1 78  ARG n 
1 79  PHE n 
1 80  PHE n 
1 81  ASN n 
1 82  TYR n 
1 83  SER n 
1 84  SER n 
1 85  GLY n 
1 86  PHE n 
1 87  ILE n 
1 88  HIS n 
1 89  HIS n 
1 90  THR n 
1 91  THR n 
1 92  ILE n 
1 93  ARG n 
1 94  LYS n 
1 95  LEU n 
1 96  LYS n 
1 97  TYR n 
1 98  ASN n 
1 99  THR n 
1 100 LYS n 
1 101 TYR n 
1 102 TYR n 
1 103 TYR n 
1 104 GLU n 
1 105 VAL n 
1 106 GLY n 
1 107 LEU n 
1 108 ARG n 
1 109 ASN n 
1 110 THR n 
1 111 THR n 
1 112 ARG n 
1 113 ARG n 
1 114 PHE n 
1 115 SER n 
1 116 PHE n 
1 117 ILE n 
1 118 THR n 
1 119 PRO n 
1 120 PRO n 
1 121 GLN n 
1 122 THR n 
1 123 GLY n 
1 124 LEU n 
1 125 ASP n 
1 126 VAL n 
1 127 PRO n 
1 128 TYR n 
1 129 THR n 
1 130 PHE n 
1 131 GLY n 
1 132 LEU n 
1 133 ILE n 
1 134 GLY n 
1 135 ASP n 
1 136 LEU n 
1 137 GLY n 
1 138 GLN n 
1 139 SER n 
1 140 PHE n 
1 141 ASP n 
1 142 SER n 
1 143 ASN n 
1 144 THR n 
1 145 THR n 
1 146 LEU n 
1 147 SER n 
1 148 HIS n 
1 149 TYR n 
1 150 GLU n 
1 151 LEU n 
1 152 SER n 
1 153 PRO n 
1 154 LYS n 
1 155 LYS n 
1 156 GLY n 
1 157 GLN n 
1 158 THR n 
1 159 VAL n 
1 160 LEU n 
1 161 PHE n 
1 162 VAL n 
1 163 GLY n 
1 164 ASP n 
1 165 LEU n 
1 166 SER n 
1 167 TYR n 
1 168 ALA n 
1 169 ASP n 
1 170 ARG n 
1 171 TYR n 
1 172 PRO n 
1 173 ASN n 
1 174 HIS n 
1 175 ASP n 
1 176 ASN n 
1 177 VAL n 
1 178 ARG n 
1 179 TRP n 
1 180 ASP n 
1 181 THR n 
1 182 TRP n 
1 183 GLY n 
1 184 ARG n 
1 185 PHE n 
1 186 THR n 
1 187 GLU n 
1 188 ARG n 
1 189 SER n 
1 190 VAL n 
1 191 ALA n 
1 192 TYR n 
1 193 GLN n 
1 194 PRO n 
1 195 TRP n 
1 196 ILE n 
1 197 TRP n 
1 198 THR n 
1 199 ALA n 
1 200 GLY n 
1 201 ASN n 
1 202 HIS n 
1 203 GLU n 
1 204 ILE n 
1 205 GLU n 
1 206 PHE n 
1 207 ALA n 
1 208 PRO n 
1 209 GLU n 
1 210 ILE n 
1 211 ASN n 
1 212 GLU n 
1 213 THR n 
1 214 GLU n 
1 215 PRO n 
1 216 PHE n 
1 217 LYS n 
1 218 PRO n 
1 219 PHE n 
1 220 SER n 
1 221 TYR n 
1 222 ARG n 
1 223 TYR n 
1 224 HIS n 
1 225 VAL n 
1 226 PRO n 
1 227 TYR n 
1 228 GLU n 
1 229 ALA n 
1 230 SER n 
1 231 GLN n 
1 232 SER n 
1 233 THR n 
1 234 SER n 
1 235 PRO n 
1 236 PHE n 
1 237 TRP n 
1 238 TYR n 
1 239 SER n 
1 240 ILE n 
1 241 LYS n 
1 242 ARG n 
1 243 ALA n 
1 244 SER n 
1 245 ALA n 
1 246 HIS n 
1 247 ILE n 
1 248 ILE n 
1 249 VAL n 
1 250 LEU n 
1 251 SER n 
1 252 SER n 
1 253 TYR n 
1 254 SER n 
1 255 ALA n 
1 256 TYR n 
1 257 GLY n 
1 258 ARG n 
1 259 GLY n 
1 260 THR n 
1 261 PRO n 
1 262 GLN n 
1 263 TYR n 
1 264 THR n 
1 265 TRP n 
1 266 LEU n 
1 267 LYS n 
1 268 LYS n 
1 269 GLU n 
1 270 LEU n 
1 271 ARG n 
1 272 LYS n 
1 273 VAL n 
1 274 LYS n 
1 275 ARG n 
1 276 SER n 
1 277 GLU n 
1 278 THR n 
1 279 PRO n 
1 280 TRP n 
1 281 LEU n 
1 282 ILE n 
1 283 VAL n 
1 284 LEU n 
1 285 MET n 
1 286 HIS n 
1 287 SER n 
1 288 PRO n 
1 289 LEU n 
1 290 TYR n 
1 291 ASN n 
1 292 SER n 
1 293 TYR n 
1 294 ASN n 
1 295 HIS n 
1 296 HIS n 
1 297 PHE n 
1 298 MET n 
1 299 GLU n 
1 300 GLY n 
1 301 GLU n 
1 302 ALA n 
1 303 MET n 
1 304 ARG n 
1 305 THR n 
1 306 LYS n 
1 307 PHE n 
1 308 GLU n 
1 309 ALA n 
1 310 TRP n 
1 311 PHE n 
1 312 VAL n 
1 313 LYS n 
1 314 TYR n 
1 315 LYS n 
1 316 VAL n 
1 317 ASP n 
1 318 VAL n 
1 319 VAL n 
1 320 PHE n 
1 321 ALA n 
1 322 GLY n 
1 323 HIS n 
1 324 VAL n 
1 325 HIS n 
1 326 ALA n 
1 327 TYR n 
1 328 GLU n 
1 329 ARG n 
1 330 SER n 
1 331 GLU n 
1 332 ARG n 
1 333 VAL n 
1 334 SER n 
1 335 ASN n 
1 336 ILE n 
1 337 ALA n 
1 338 TYR n 
1 339 LYS n 
1 340 ILE n 
1 341 THR n 
1 342 ASP n 
1 343 GLY n 
1 344 LEU n 
1 345 CYS n 
1 346 THR n 
1 347 PRO n 
1 348 VAL n 
1 349 LYS n 
1 350 ASP n 
1 351 GLN n 
1 352 SER n 
1 353 ALA n 
1 354 PRO n 
1 355 VAL n 
1 356 TYR n 
1 357 ILE n 
1 358 THR n 
1 359 ILE n 
1 360 GLY n 
1 361 ASP n 
1 362 ALA n 
1 363 GLY n 
1 364 ASN n 
1 365 TYR n 
1 366 GLY n 
1 367 VAL n 
1 368 ILE n 
1 369 ASP n 
1 370 SER n 
1 371 ASN n 
1 372 MET n 
1 373 ILE n 
1 374 GLN n 
1 375 PRO n 
1 376 GLN n 
1 377 PRO n 
1 378 GLU n 
1 379 TYR n 
1 380 SER n 
1 381 ALA n 
1 382 PHE n 
1 383 ARG n 
1 384 GLU n 
1 385 ALA n 
1 386 SER n 
1 387 PHE n 
1 388 GLY n 
1 389 HIS n 
1 390 GLY n 
1 391 MET n 
1 392 PHE n 
1 393 ASP n 
1 394 ILE n 
1 395 LYS n 
1 396 ASN n 
1 397 ARG n 
1 398 THR n 
1 399 HIS n 
1 400 ALA n 
1 401 HIS n 
1 402 PHE n 
1 403 SER n 
1 404 TRP n 
1 405 ASN n 
1 406 ARG n 
1 407 ASN n 
1 408 GLN n 
1 409 ASP n 
1 410 GLY n 
1 411 VAL n 
1 412 ALA n 
1 413 VAL n 
1 414 GLU n 
1 415 ALA n 
1 416 ASP n 
1 417 SER n 
1 418 VAL n 
1 419 TRP n 
1 420 PHE n 
1 421 PHE n 
1 422 ASN n 
1 423 ARG n 
1 424 HIS n 
1 425 TRP n 
1 426 TYR n 
1 427 PRO n 
1 428 VAL n 
1 429 ASP n 
1 430 ASP n 
1 431 SER n 
1 432 THR n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                ? 
_entity_src_nat.pdbx_organism_scientific   'Phaseolus vulgaris' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      3885 
_entity_src_nat.genus                      Phaseolus 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PPAF_PHAVU 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P80366 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;FVRKTNKNRDMPLDSDVFRVPPGYNAPQQVHITQGDLVGRAMIISWVTMDEPGSSAVRYWSEKNGRKRIAKGKMSTYRFF
NYSSGFIHHTTIRKLKYNTKYYYEVGLRNTTRRFSFITPPQTGLDVPYTFGLIGDLGQSFDSNTTLSHYELSPKKGQTVL
FVGDLSYADRYPNHDNVRWDTWGRFTERSVAYQPWIWTAGNHEIEFAPEINETEPFKPFSYRYHVPYEASQSTSPFWYSI
KRASAHIIVLSSHIAYGRGTPQYTWLKKELRKVKRSETPWLIVLMHSPLYNSYNHHFMEGEAMRTKFEAWFVKYKVDVVF
AGHVHAYERSERVSNIAYKITDGLCTPVKDQSAPVYITIGDAGNYGVIDSNMIQPQPEYSAFREASFGHGMFDIKNRTHA
HFSWNRNQDGVAVEADSVWFFNRHWYPVDDST
;
_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 4KBP A 1 ? 432 ? P80366 1 ? 432 ? 1 432 
2 1 4KBP B 1 ? 432 ? P80366 1 ? 432 ? 1 432 
3 1 4KBP C 1 ? 432 ? P80366 1 ? 432 ? 1 432 
4 1 4KBP D 1 ? 432 ? P80366 1 ? 432 ? 1 432 
# 
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 4KBP TYR A 253 ? UNP P80366 HIS 253 CONFLICT 253 1 
1 4KBP SER A 254 ? UNP P80366 ILE 254 CONFLICT 254 2 
2 4KBP TYR B 253 ? UNP P80366 HIS 253 CONFLICT 253 3 
2 4KBP SER B 254 ? UNP P80366 ILE 254 CONFLICT 254 4 
3 4KBP TYR C 253 ? UNP P80366 HIS 253 CONFLICT 253 5 
3 4KBP SER C 254 ? UNP P80366 ILE 254 CONFLICT 254 6 
4 4KBP TYR D 253 ? UNP P80366 HIS 253 CONFLICT 253 7 
4 4KBP SER D 254 ? UNP P80366 ILE 254 CONFLICT 254 8 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
FE  non-polymer         . 'FE (III) ION'         ? 'Fe 3'           55.845  
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 
PO4 non-polymer         . 'PHOSPHATE ION'        ? 'O4 P -3'        94.971  
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 
ZN  non-polymer         . 'ZINC ION'             ? 'Zn 2'           65.409  
# 
_exptl.entry_id          4KBP 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.68 
_exptl_crystal.density_percent_sol   64. 
_exptl_crystal.description           ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           277 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE AREA DETECTOR' 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   1995-04-15 
_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             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.95 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      ? 
_diffrn_source.type                        ? 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             0.95 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     4KBP 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             35.0 
_reflns.d_resolution_high            2.7 
_reflns.number_obs                   71089 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         87.5 
_reflns.pdbx_Rmerge_I_obs            0.086 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              4.6 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_refine.entry_id                                 4KBP 
_refine.ls_number_reflns_obs                     57954 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          3. 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             10.0 
_refine.ls_d_res_high                            2.7 
_refine.ls_percent_reflns_obs                    72.4 
_refine.ls_R_factor_obs                          0.192 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.192 
_refine.ls_R_factor_R_free                       0.228 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               37.8 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_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          ? 
# 
_refine_analyze.entry_id                        4KBP 
_refine_analyze.Luzzati_coordinate_error_obs    0.30 
_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_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        13976 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         308 
_refine_hist.number_atoms_solvent             56 
_refine_hist.number_atoms_total               14340 
_refine_hist.d_res_high                       2.7 
_refine_hist.d_res_low                        10.0 
# 
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 
x_bond_d                0.020 ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_na             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_prot           ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d               ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_na            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_prot          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg             2.503 ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_na          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_prot        ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d      24.65 ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d      1.725 ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_scbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_scangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
# 
loop_
_struct_ncs_oper.id 
_struct_ncs_oper.code 
_struct_ncs_oper.details 
_struct_ncs_oper.matrix[1][1] 
_struct_ncs_oper.matrix[1][2] 
_struct_ncs_oper.matrix[1][3] 
_struct_ncs_oper.matrix[2][1] 
_struct_ncs_oper.matrix[2][2] 
_struct_ncs_oper.matrix[2][3] 
_struct_ncs_oper.matrix[3][1] 
_struct_ncs_oper.matrix[3][2] 
_struct_ncs_oper.matrix[3][3] 
_struct_ncs_oper.vector[1] 
_struct_ncs_oper.vector[2] 
_struct_ncs_oper.vector[3] 
1 given ? 0.150159  -0.171470 -0.973679 0.001982 -0.984791 0.173732 -0.988660 -0.028018 -0.147535 123.28290 78.25470  79.34620  
2 given ? -0.145481 0.177203  0.973362  0.000633 -0.983812 0.179200 0.989361  0.026687  0.143014  9.19060   77.92360  -14.76130 
3 given ? -0.951406 -0.004091 -0.307913 0.003431 -0.999991 0.002683 -0.307921 0.001496  0.951411  139.87000 178.61330 21.83600  
# 
_struct.entry_id                  4KBP 
_struct.title                     'KIDNEY BEAN PURPLE ACID PHOSPHATASE' 
_struct.pdbx_descriptor           'PURPLE ACID PHOSPHATASE' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4KBP 
_struct_keywords.pdbx_keywords   'HYDROLASE (PHOSPHORIC MONOESTER)' 
_struct_keywords.text            'PURPLE ACID PHOSPHATASE, HYDROLASE (PHOSPHORIC MONOESTER)' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 2 ? 
G  N N 2 ? 
H  N N 2 ? 
I  N N 2 ? 
J  N N 3 ? 
K  N N 4 ? 
L  N N 5 ? 
M  N N 2 ? 
N  N N 2 ? 
O  N N 2 ? 
P  N N 2 ? 
Q  N N 2 ? 
R  N N 3 ? 
S  N N 4 ? 
T  N N 5 ? 
U  N N 2 ? 
V  N N 2 ? 
W  N N 2 ? 
X  N N 2 ? 
Y  N N 2 ? 
Z  N N 3 ? 
AA N N 4 ? 
BA N N 5 ? 
CA N N 2 ? 
DA N N 2 ? 
EA N N 2 ? 
FA N N 2 ? 
GA N N 2 ? 
HA N N 3 ? 
IA N N 4 ? 
JA N N 5 ? 
KA N N 6 ? 
LA N N 6 ? 
MA N N 6 ? 
NA N N 6 ? 
# 
loop_
_struct_biol.id 
1 
2 
3 
# 
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  ASP A 16  ? PHE A 18  ? ASP A 16  PHE A 18  5 ? 3  
HELX_P HELX_P2  2  PHE A 140 ? LEU A 151 ? PHE A 140 LEU A 151 1 ? 12 
HELX_P HELX_P3  3  ALA A 168 ? ARG A 170 ? ALA A 168 ARG A 170 5 ? 3  
HELX_P HELX_P4  4  PRO A 172 ? HIS A 174 ? PRO A 172 HIS A 174 5 ? 3  
HELX_P HELX_P5  5  ASN A 176 ? VAL A 190 ? ASN A 176 VAL A 190 5 ? 15 
HELX_P HELX_P6  6  ASN A 201 ? ILE A 204 ? ASN A 201 ILE A 204 1 ? 4  
HELX_P HELX_P7  7  PRO A 208 ? ILE A 210 ? PRO A 208 ILE A 210 5 ? 3  
HELX_P HELX_P8  8  LYS A 217 ? ARG A 222 ? LYS A 217 ARG A 222 1 ? 6  
HELX_P HELX_P9  9  TYR A 227 ? ALA A 229 ? TYR A 227 ALA A 229 5 ? 3  
HELX_P HELX_P10 10 PRO A 261 ? LYS A 272 ? PRO A 261 LYS A 272 1 ? 12 
HELX_P HELX_P11 11 GLU A 299 ? LYS A 313 ? GLU A 299 LYS A 313 5 ? 15 
HELX_P HELX_P12 12 ASP B 16  ? PHE B 18  ? ASP B 16  PHE B 18  5 ? 3  
HELX_P HELX_P13 13 PHE B 140 ? LEU B 151 ? PHE B 140 LEU B 151 1 ? 12 
HELX_P HELX_P14 14 ALA B 168 ? ARG B 170 ? ALA B 168 ARG B 170 5 ? 3  
HELX_P HELX_P15 15 PRO B 172 ? HIS B 174 ? PRO B 172 HIS B 174 5 ? 3  
HELX_P HELX_P16 16 ASN B 176 ? VAL B 190 ? ASN B 176 VAL B 190 5 ? 15 
HELX_P HELX_P17 17 ASN B 201 ? ILE B 204 ? ASN B 201 ILE B 204 1 ? 4  
HELX_P HELX_P18 18 PRO B 208 ? ILE B 210 ? PRO B 208 ILE B 210 5 ? 3  
HELX_P HELX_P19 19 LYS B 217 ? ARG B 222 ? LYS B 217 ARG B 222 1 ? 6  
HELX_P HELX_P20 20 PRO B 261 ? LYS B 272 ? PRO B 261 LYS B 272 1 ? 12 
HELX_P HELX_P21 21 GLU B 299 ? LYS B 313 ? GLU B 299 LYS B 313 5 ? 15 
HELX_P HELX_P22 22 ASP C 16  ? PHE C 18  ? ASP C 16  PHE C 18  5 ? 3  
HELX_P HELX_P23 23 PHE C 140 ? LEU C 151 ? PHE C 140 LEU C 151 1 ? 12 
HELX_P HELX_P24 24 ALA C 168 ? ARG C 170 ? ALA C 168 ARG C 170 5 ? 3  
HELX_P HELX_P25 25 PRO C 172 ? HIS C 174 ? PRO C 172 HIS C 174 5 ? 3  
HELX_P HELX_P26 26 ASN C 176 ? VAL C 190 ? ASN C 176 VAL C 190 5 ? 15 
HELX_P HELX_P27 27 ASN C 201 ? ILE C 204 ? ASN C 201 ILE C 204 1 ? 4  
HELX_P HELX_P28 28 PRO C 208 ? ILE C 210 ? PRO C 208 ILE C 210 5 ? 3  
HELX_P HELX_P29 29 LYS C 217 ? ARG C 222 ? LYS C 217 ARG C 222 1 ? 6  
HELX_P HELX_P30 30 PRO C 261 ? LYS C 272 ? PRO C 261 LYS C 272 1 ? 12 
HELX_P HELX_P31 31 GLU C 299 ? LYS C 313 ? GLU C 299 LYS C 313 5 ? 15 
HELX_P HELX_P32 32 ASP D 16  ? PHE D 18  ? ASP D 16  PHE D 18  5 ? 3  
HELX_P HELX_P33 33 PHE D 140 ? LEU D 151 ? PHE D 140 LEU D 151 1 ? 12 
HELX_P HELX_P34 34 ALA D 168 ? ARG D 170 ? ALA D 168 ARG D 170 5 ? 3  
HELX_P HELX_P35 35 PRO D 172 ? HIS D 174 ? PRO D 172 HIS D 174 5 ? 3  
HELX_P HELX_P36 36 ASN D 176 ? VAL D 190 ? ASN D 176 VAL D 190 5 ? 15 
HELX_P HELX_P37 37 ASN D 201 ? ILE D 204 ? ASN D 201 ILE D 204 1 ? 4  
HELX_P HELX_P38 38 PRO D 208 ? ILE D 210 ? PRO D 208 ILE D 210 5 ? 3  
HELX_P HELX_P39 39 LYS D 217 ? ARG D 222 ? LYS D 217 ARG D 222 1 ? 6  
HELX_P HELX_P40 40 PRO D 261 ? LYS D 272 ? PRO D 261 LYS D 272 1 ? 12 
HELX_P HELX_P41 41 GLU D 299 ? LYS D 313 ? GLU D 299 LYS D 313 5 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A  CYS 345 SG ? ? ? 1_555 A  CYS 345 SG  ? ? A CYS 345 A CYS 345 3_655 ? ? ? ? ? ? ? 2.209 ? 
disulf2  disulf ? ? B  CYS 345 SG ? ? ? 1_555 C  CYS 345 SG  ? ? B CYS 345 C CYS 345 1_555 ? ? ? ? ? ? ? 2.197 ? 
disulf3  disulf ? ? D  CYS 345 SG ? ? ? 3_655 D  CYS 345 SG  ? ? D CYS 345 D CYS 345 1_555 ? ? ? ? ? ? ? 2.159 ? 
covale1  covale ? ? E  NAG .   C1 ? A ? 1_555 A  ASN 81  ND2 ? ? A NAG 433 A ASN 81  1_555 ? ? ? ? ? ? ? 1.477 ? 
covale2  covale ? ? F  NAG .   C1 ? A ? 1_555 A  ASN 109 ND2 ? ? A NAG 434 A ASN 109 1_555 ? ? ? ? ? ? ? 1.473 ? 
covale3  covale ? ? G  NAG .   C1 ? A ? 1_555 A  ASN 143 ND2 ? ? A NAG 435 A ASN 143 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale4  covale ? ? H  NAG .   C1 ? A ? 1_555 A  ASN 211 ND2 ? ? A NAG 436 A ASN 211 1_555 ? ? ? ? ? ? ? 1.464 ? 
covale5  covale ? ? I  NAG .   C1 ? A ? 1_555 A  ASN 396 ND2 ? ? A NAG 437 A ASN 396 1_555 ? ? ? ? ? ? ? 1.470 ? 
metalc1  metalc ? ? J  FE  .   FE ? ? ? 1_555 A  ASP 135 OD1 ? ? A FE  438 A ASP 135 1_555 ? ? ? ? ? ? ? 2.043 ? 
metalc2  metalc ? ? J  FE  .   FE ? ? ? 1_555 A  ASP 164 OD2 ? ? A FE  438 A ASP 164 1_555 ? ? ? ? ? ? ? 2.346 ? 
metalc3  metalc ? ? J  FE  .   FE ? ? ? 1_555 A  TYR 167 OH  ? ? A FE  438 A TYR 167 1_555 ? ? ? ? ? ? ? 2.211 ? 
metalc4  metalc ? ? J  FE  .   FE ? ? ? 1_555 L  PO4 .   O2  ? ? A FE  438 A PO4 440 1_555 ? ? ? ? ? ? ? 1.729 ? 
metalc5  metalc ? ? K  ZN  .   ZN ? ? ? 1_555 A  ASP 164 OD2 ? ? A ZN  439 A ASP 164 1_555 ? ? ? ? ? ? ? 2.247 ? 
metalc6  metalc ? ? K  ZN  .   ZN ? ? ? 1_555 A  ASN 201 OD1 ? ? A ZN  439 A ASN 201 1_555 ? ? ? ? ? ? ? 2.139 ? 
metalc7  metalc ? ? K  ZN  .   ZN ? ? ? 1_555 A  HIS 286 NE2 ? ? A ZN  439 A HIS 286 1_555 ? ? ? ? ? ? ? 2.052 ? 
metalc8  metalc ? ? K  ZN  .   ZN ? ? ? 1_555 A  HIS 323 ND1 ? ? A ZN  439 A HIS 323 1_555 ? ? ? ? ? ? ? 2.140 ? 
metalc9  metalc ? ? K  ZN  .   ZN ? ? ? 1_555 L  PO4 .   O3  ? ? A ZN  439 A PO4 440 1_555 ? ? ? ? ? ? ? 1.965 ? 
covale6  covale ? ? M  NAG .   C1 ? A ? 1_555 B  ASN 81  ND2 ? ? B NAG 433 B ASN 81  1_555 ? ? ? ? ? ? ? 1.476 ? 
covale7  covale ? ? N  NAG .   C1 ? A ? 1_555 B  ASN 109 ND2 ? ? B NAG 434 B ASN 109 1_555 ? ? ? ? ? ? ? 1.470 ? 
covale8  covale ? ? O  NAG .   C1 ? A ? 1_555 B  ASN 143 ND2 ? ? B NAG 435 B ASN 143 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale9  covale ? ? P  NAG .   C1 ? A ? 1_555 B  ASN 211 ND2 ? ? B NAG 436 B ASN 211 1_555 ? ? ? ? ? ? ? 1.471 ? 
covale10 covale ? ? Q  NAG .   C1 ? A ? 1_555 B  ASN 396 ND2 ? ? B NAG 437 B ASN 396 1_555 ? ? ? ? ? ? ? 1.469 ? 
metalc10 metalc ? ? R  FE  .   FE ? ? ? 1_555 B  ASP 135 OD1 ? ? B FE  438 B ASP 135 1_555 ? ? ? ? ? ? ? 2.027 ? 
metalc11 metalc ? ? R  FE  .   FE ? ? ? 1_555 B  ASP 164 OD2 ? ? B FE  438 B ASP 164 1_555 ? ? ? ? ? ? ? 2.308 ? 
metalc12 metalc ? ? R  FE  .   FE ? ? ? 1_555 B  TYR 167 OH  ? ? B FE  438 B TYR 167 1_555 ? ? ? ? ? ? ? 2.194 ? 
metalc13 metalc ? ? R  FE  .   FE ? ? ? 1_555 T  PO4 .   O2  ? ? B FE  438 B PO4 440 1_555 ? ? ? ? ? ? ? 1.767 ? 
metalc14 metalc ? ? S  ZN  .   ZN ? ? ? 1_555 B  ASP 164 OD2 ? ? B ZN  439 B ASP 164 1_555 ? ? ? ? ? ? ? 2.286 ? 
metalc15 metalc ? ? S  ZN  .   ZN ? ? ? 1_555 B  ASN 201 OD1 ? ? B ZN  439 B ASN 201 1_555 ? ? ? ? ? ? ? 2.157 ? 
metalc16 metalc ? ? S  ZN  .   ZN ? ? ? 1_555 B  HIS 286 NE2 ? ? B ZN  439 B HIS 286 1_555 ? ? ? ? ? ? ? 2.017 ? 
metalc17 metalc ? ? S  ZN  .   ZN ? ? ? 1_555 B  HIS 323 ND1 ? ? B ZN  439 B HIS 323 1_555 ? ? ? ? ? ? ? 2.106 ? 
metalc18 metalc ? ? S  ZN  .   ZN ? ? ? 1_555 T  PO4 .   O3  ? ? B ZN  439 B PO4 440 1_555 ? ? ? ? ? ? ? 2.032 ? 
covale11 covale ? ? U  NAG .   C1 ? A ? 1_555 C  ASN 81  ND2 ? ? C NAG 433 C ASN 81  1_555 ? ? ? ? ? ? ? 1.484 ? 
covale12 covale ? ? V  NAG .   C1 ? A ? 1_555 C  ASN 109 ND2 ? ? C NAG 434 C ASN 109 1_555 ? ? ? ? ? ? ? 1.466 ? 
covale13 covale ? ? W  NAG .   C1 ? A ? 1_555 C  ASN 143 ND2 ? ? C NAG 435 C ASN 143 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale14 covale ? ? X  NAG .   C1 ? A ? 1_555 C  ASN 211 ND2 ? ? C NAG 436 C ASN 211 1_555 ? ? ? ? ? ? ? 1.475 ? 
covale15 covale ? ? Y  NAG .   C1 ? A ? 1_555 C  ASN 396 ND2 ? ? C NAG 437 C ASN 396 1_555 ? ? ? ? ? ? ? 1.460 ? 
metalc19 metalc ? ? Z  FE  .   FE ? ? ? 1_555 C  ASP 135 OD1 ? ? C FE  438 C ASP 135 1_555 ? ? ? ? ? ? ? 1.923 ? 
metalc20 metalc ? ? Z  FE  .   FE ? ? ? 1_555 C  ASP 164 OD2 ? ? C FE  438 C ASP 164 1_555 ? ? ? ? ? ? ? 2.311 ? 
metalc21 metalc ? ? Z  FE  .   FE ? ? ? 1_555 C  TYR 167 OH  ? ? C FE  438 C TYR 167 1_555 ? ? ? ? ? ? ? 2.245 ? 
metalc22 metalc ? ? Z  FE  .   FE ? ? ? 1_555 BA PO4 .   O2  ? ? C FE  438 C PO4 440 1_555 ? ? ? ? ? ? ? 1.768 ? 
metalc23 metalc ? ? AA ZN  .   ZN ? ? ? 1_555 C  ASP 164 OD2 ? ? C ZN  439 C ASP 164 1_555 ? ? ? ? ? ? ? 2.323 ? 
metalc24 metalc ? ? AA ZN  .   ZN ? ? ? 1_555 C  ASN 201 OD1 ? ? C ZN  439 C ASN 201 1_555 ? ? ? ? ? ? ? 2.187 ? 
metalc25 metalc ? ? AA ZN  .   ZN ? ? ? 1_555 C  HIS 286 NE2 ? ? C ZN  439 C HIS 286 1_555 ? ? ? ? ? ? ? 2.053 ? 
metalc26 metalc ? ? AA ZN  .   ZN ? ? ? 1_555 C  HIS 323 ND1 ? ? C ZN  439 C HIS 323 1_555 ? ? ? ? ? ? ? 2.111 ? 
metalc27 metalc ? ? AA ZN  .   ZN ? ? ? 1_555 BA PO4 .   O3  ? ? C ZN  439 C PO4 440 1_555 ? ? ? ? ? ? ? 1.971 ? 
covale16 covale ? ? CA NAG .   C1 ? A ? 1_555 D  ASN 81  ND2 ? ? D NAG 433 D ASN 81  1_555 ? ? ? ? ? ? ? 1.466 ? 
covale17 covale ? ? DA NAG .   C1 ? A ? 1_555 D  ASN 109 ND2 ? ? D NAG 434 D ASN 109 1_555 ? ? ? ? ? ? ? 1.464 ? 
covale18 covale ? ? EA NAG .   C1 ? A ? 1_555 D  ASN 143 ND2 ? ? D NAG 435 D ASN 143 1_555 ? ? ? ? ? ? ? 1.460 ? 
covale19 covale ? ? FA NAG .   C1 ? A ? 1_555 D  ASN 211 ND2 ? ? D NAG 436 D ASN 211 1_555 ? ? ? ? ? ? ? 1.473 ? 
covale20 covale ? ? GA NAG .   C1 ? A ? 1_555 D  ASN 396 ND2 ? ? D NAG 437 D ASN 396 1_555 ? ? ? ? ? ? ? 1.467 ? 
metalc28 metalc ? ? HA FE  .   FE ? ? ? 1_555 D  ASP 135 OD1 ? ? D FE  438 D ASP 135 1_555 ? ? ? ? ? ? ? 1.985 ? 
metalc29 metalc ? ? HA FE  .   FE ? ? ? 1_555 D  ASP 164 OD2 ? ? D FE  438 D ASP 164 1_555 ? ? ? ? ? ? ? 2.284 ? 
metalc30 metalc ? ? HA FE  .   FE ? ? ? 1_555 D  TYR 167 OH  ? ? D FE  438 D TYR 167 1_555 ? ? ? ? ? ? ? 2.212 ? 
metalc31 metalc ? ? HA FE  .   FE ? ? ? 1_555 JA PO4 .   O2  ? ? D FE  438 D PO4 440 1_555 ? ? ? ? ? ? ? 1.798 ? 
metalc32 metalc ? ? IA ZN  .   ZN ? ? ? 1_555 D  ASP 164 OD2 ? ? D ZN  439 D ASP 164 1_555 ? ? ? ? ? ? ? 2.185 ? 
metalc33 metalc ? ? IA ZN  .   ZN ? ? ? 1_555 D  ASN 201 OD1 ? ? D ZN  439 D ASN 201 1_555 ? ? ? ? ? ? ? 2.163 ? 
metalc34 metalc ? ? IA ZN  .   ZN ? ? ? 1_555 D  HIS 286 NE2 ? ? D ZN  439 D HIS 286 1_555 ? ? ? ? ? ? ? 2.066 ? 
metalc35 metalc ? ? IA ZN  .   ZN ? ? ? 1_555 D  HIS 323 ND1 ? ? D ZN  439 D HIS 323 1_555 ? ? ? ? ? ? ? 2.209 ? 
metalc36 metalc ? ? IA ZN  .   ZN ? ? ? 1_555 JA PO4 .   O3  ? ? D ZN  439 D PO4 440 1_555 ? ? ? ? ? ? ? 1.953 ? 
metalc37 metalc ? ? J  FE  .   FE ? ? ? 1_555 A  HIS 325 NE2 ? ? A FE  438 A HIS 325 1_555 ? ? ? ? ? ? ? 2.445 ? 
metalc38 metalc ? ? R  FE  .   FE ? ? ? 1_555 B  HIS 325 NE2 ? ? B FE  438 B HIS 325 1_555 ? ? ? ? ? ? ? 2.485 ? 
metalc39 metalc ? ? Z  FE  .   FE ? ? ? 1_555 C  HIS 325 NE2 ? ? C FE  438 C HIS 325 1_555 ? ? ? ? ? ? ? 2.465 ? 
metalc40 metalc ? ? HA FE  .   FE ? ? ? 1_555 D  HIS 325 NE2 ? ? D FE  438 D HIS 325 1_555 ? ? ? ? ? ? ? 2.512 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
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 GLN 374 A . ? GLN 374 A PRO 375 A ? PRO 375 A 1 -0.98 
2 GLN 374 B . ? GLN 374 B PRO 375 B ? PRO 375 B 1 3.35  
3 GLN 374 C . ? GLN 374 C PRO 375 C ? PRO 375 C 1 2.82  
4 GLN 374 D . ? GLN 374 D PRO 375 D ? PRO 375 D 1 -1.37 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 4 ? 
B ? 4 ? 
C ? 5 ? 
D ? 7 ? 
E ? 4 ? 
F ? 4 ? 
G ? 5 ? 
H ? 7 ? 
I ? 4 ? 
J ? 4 ? 
K ? 5 ? 
L ? 7 ? 
M ? 4 ? 
N ? 4 ? 
O ? 5 ? 
P ? 5 ? 
Q ? 2 ? 
# 
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 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? parallel      
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? parallel      
D 3 4 ? parallel      
D 4 5 ? parallel      
D 5 6 ? anti-parallel 
D 6 7 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
G 1 2 ? parallel      
G 2 3 ? anti-parallel 
G 3 4 ? anti-parallel 
G 4 5 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? parallel      
H 3 4 ? parallel      
H 4 5 ? parallel      
H 5 6 ? anti-parallel 
H 6 7 ? anti-parallel 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
I 3 4 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? anti-parallel 
J 3 4 ? anti-parallel 
K 1 2 ? parallel      
K 2 3 ? anti-parallel 
K 3 4 ? anti-parallel 
K 4 5 ? anti-parallel 
L 1 2 ? anti-parallel 
L 2 3 ? parallel      
L 3 4 ? parallel      
L 4 5 ? parallel      
L 5 6 ? anti-parallel 
L 6 7 ? anti-parallel 
M 1 2 ? anti-parallel 
M 2 3 ? anti-parallel 
M 3 4 ? anti-parallel 
N 1 2 ? anti-parallel 
N 2 3 ? anti-parallel 
N 3 4 ? anti-parallel 
O 1 2 ? parallel      
O 2 3 ? anti-parallel 
O 3 4 ? anti-parallel 
O 4 5 ? anti-parallel 
P 1 2 ? anti-parallel 
P 2 3 ? parallel      
P 3 4 ? parallel      
P 4 5 ? parallel      
Q 1 2 ? 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 
A 1 HIS A 31  ? GLN A 34  ? HIS A 31  GLN A 34  
A 2 MET A 42  ? THR A 48  ? MET A 42  THR A 48  
A 3 PHE A 86  ? ILE A 92  ? PHE A 86  ILE A 92  
A 4 LYS A 73  ? SER A 75  ? LYS A 73  SER A 75  
B 1 ARG A 68  ? LYS A 71  ? ARG A 68  LYS A 71  
B 2 ALA A 56  ? SER A 61  ? ALA A 56  SER A 61  
B 3 LYS A 100 ? VAL A 105 ? LYS A 100 VAL A 105 
B 4 ARG A 112 ? ILE A 117 ? ARG A 112 ILE A 117 
C 1 THR A 158 ? PHE A 161 ? THR A 158 PHE A 161 
C 2 TYR A 128 ? ILE A 133 ? TYR A 128 ILE A 133 
C 3 GLY A 388 ? ILE A 394 ? GLY A 388 ILE A 394 
C 4 HIS A 399 ? ARG A 406 ? HIS A 399 ARG A 406 
C 5 GLU A 414 ? PHE A 421 ? GLU A 414 PHE A 421 
D 1 TYR A 238 ? ARG A 242 ? TYR A 238 ARG A 242 
D 2 ALA A 245 ? VAL A 249 ? ALA A 245 VAL A 249 
D 3 TRP A 280 ? LEU A 284 ? TRP A 280 LEU A 284 
D 4 VAL A 318 ? ALA A 321 ? VAL A 318 ALA A 321 
D 5 VAL A 355 ? ILE A 359 ? VAL A 355 ILE A 359 
D 6 TYR A 327 ? SER A 330 ? TYR A 327 SER A 330 
D 7 SER A 380 ? GLU A 384 ? SER A 380 GLU A 384 
E 1 HIS B 31  ? GLN B 34  ? HIS B 31  GLN B 34  
E 2 MET B 42  ? THR B 48  ? MET B 42  THR B 48  
E 3 PHE B 86  ? ILE B 92  ? PHE B 86  ILE B 92  
E 4 LYS B 73  ? SER B 75  ? LYS B 73  SER B 75  
F 1 ARG B 68  ? LYS B 71  ? ARG B 68  LYS B 71  
F 2 ALA B 56  ? SER B 61  ? ALA B 56  SER B 61  
F 3 LYS B 100 ? VAL B 105 ? LYS B 100 VAL B 105 
F 4 ARG B 112 ? ILE B 117 ? ARG B 112 ILE B 117 
G 1 VAL B 159 ? PHE B 161 ? VAL B 159 PHE B 161 
G 2 TYR B 128 ? ILE B 133 ? TYR B 128 ILE B 133 
G 3 GLY B 388 ? ILE B 394 ? GLY B 388 ILE B 394 
G 4 HIS B 399 ? ARG B 406 ? HIS B 399 ARG B 406 
G 5 GLU B 414 ? PHE B 421 ? GLU B 414 PHE B 421 
H 1 TYR B 238 ? ARG B 242 ? TYR B 238 ARG B 242 
H 2 ALA B 245 ? VAL B 249 ? ALA B 245 VAL B 249 
H 3 TRP B 280 ? LEU B 284 ? TRP B 280 LEU B 284 
H 4 VAL B 318 ? ALA B 321 ? VAL B 318 ALA B 321 
H 5 VAL B 355 ? ILE B 359 ? VAL B 355 ILE B 359 
H 6 TYR B 327 ? SER B 330 ? TYR B 327 SER B 330 
H 7 SER B 380 ? GLU B 384 ? SER B 380 GLU B 384 
I 1 HIS C 31  ? GLN C 34  ? HIS C 31  GLN C 34  
I 2 MET C 42  ? THR C 48  ? MET C 42  THR C 48  
I 3 PHE C 86  ? ILE C 92  ? PHE C 86  ILE C 92  
I 4 LYS C 73  ? SER C 75  ? LYS C 73  SER C 75  
J 1 ARG C 68  ? LYS C 71  ? ARG C 68  LYS C 71  
J 2 ALA C 56  ? SER C 61  ? ALA C 56  SER C 61  
J 3 LYS C 100 ? VAL C 105 ? LYS C 100 VAL C 105 
J 4 ARG C 112 ? ILE C 117 ? ARG C 112 ILE C 117 
K 1 THR C 158 ? PHE C 161 ? THR C 158 PHE C 161 
K 2 TYR C 128 ? ILE C 133 ? TYR C 128 ILE C 133 
K 3 GLY C 388 ? ILE C 394 ? GLY C 388 ILE C 394 
K 4 HIS C 399 ? ARG C 406 ? HIS C 399 ARG C 406 
K 5 GLU C 414 ? PHE C 421 ? GLU C 414 PHE C 421 
L 1 TYR C 238 ? ARG C 242 ? TYR C 238 ARG C 242 
L 2 ALA C 245 ? VAL C 249 ? ALA C 245 VAL C 249 
L 3 TRP C 280 ? LEU C 284 ? TRP C 280 LEU C 284 
L 4 VAL C 318 ? ALA C 321 ? VAL C 318 ALA C 321 
L 5 VAL C 355 ? ILE C 359 ? VAL C 355 ILE C 359 
L 6 TYR C 327 ? SER C 330 ? TYR C 327 SER C 330 
L 7 SER C 380 ? GLU C 384 ? SER C 380 GLU C 384 
M 1 HIS D 31  ? GLN D 34  ? HIS D 31  GLN D 34  
M 2 MET D 42  ? THR D 48  ? MET D 42  THR D 48  
M 3 PHE D 86  ? ILE D 92  ? PHE D 86  ILE D 92  
M 4 LYS D 73  ? SER D 75  ? LYS D 73  SER D 75  
N 1 ARG D 68  ? LYS D 71  ? ARG D 68  LYS D 71  
N 2 ALA D 56  ? SER D 61  ? ALA D 56  SER D 61  
N 3 LYS D 100 ? VAL D 105 ? LYS D 100 VAL D 105 
N 4 ARG D 112 ? ILE D 117 ? ARG D 112 ILE D 117 
O 1 VAL D 159 ? PHE D 161 ? VAL D 159 PHE D 161 
O 2 TYR D 128 ? ILE D 133 ? TYR D 128 ILE D 133 
O 3 GLY D 388 ? ILE D 394 ? GLY D 388 ILE D 394 
O 4 HIS D 399 ? ARG D 406 ? HIS D 399 ARG D 406 
O 5 GLU D 414 ? PHE D 421 ? GLU D 414 PHE D 421 
P 1 TYR D 238 ? ARG D 242 ? TYR D 238 ARG D 242 
P 2 ALA D 245 ? VAL D 249 ? ALA D 245 VAL D 249 
P 3 TRP D 280 ? LEU D 284 ? TRP D 280 LEU D 284 
P 4 VAL D 318 ? ALA D 321 ? VAL D 318 ALA D 321 
P 5 VAL D 355 ? THR D 358 ? VAL D 355 THR D 358 
Q 1 TYR D 327 ? SER D 330 ? TYR D 327 SER D 330 
Q 2 SER D 380 ? GLU D 384 ? SER D 380 GLU D 384 
# 
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 
A 1 2 O HIS A 31  ? O HIS A 31  N SER A 45  ? N SER A 45  
A 2 3 O MET A 42  ? O MET A 42  N ILE A 92  ? N ILE A 92  
A 3 4 O ILE A 87  ? O ILE A 87  N SER A 75  ? N SER A 75  
B 1 2 O ARG A 68  ? O ARG A 68  N TYR A 59  ? N TYR A 59  
B 2 3 O ARG A 58  ? O ARG A 58  N GLU A 104 ? N GLU A 104 
B 3 4 O TYR A 101 ? O TYR A 101 N PHE A 116 ? N PHE A 116 
C 1 2 O THR A 158 ? O THR A 158 N GLY A 131 ? N GLY A 131 
C 2 3 O TYR A 128 ? O TYR A 128 N ILE A 394 ? N ILE A 394 
C 3 4 O HIS A 389 ? O HIS A 389 N ASN A 405 ? N ASN A 405 
C 4 5 O ALA A 400 ? O ALA A 400 N PHE A 420 ? N PHE A 420 
D 1 2 O TYR A 238 ? O TYR A 238 N VAL A 249 ? N VAL A 249 
D 2 3 O HIS A 246 ? O HIS A 246 N TRP A 280 ? N TRP A 280 
D 3 4 O VAL A 283 ? O VAL A 283 N VAL A 318 ? N VAL A 318 
D 4 5 O VAL A 319 ? O VAL A 319 N VAL A 355 ? N VAL A 355 
D 5 6 O THR A 358 ? O THR A 358 N GLU A 328 ? N GLU A 328 
D 6 7 O TYR A 327 ? O TYR A 327 N GLU A 384 ? N GLU A 384 
E 1 2 O HIS B 31  ? O HIS B 31  N SER B 45  ? N SER B 45  
E 2 3 O MET B 42  ? O MET B 42  N ILE B 92  ? N ILE B 92  
E 3 4 O ILE B 87  ? O ILE B 87  N SER B 75  ? N SER B 75  
F 1 2 O ARG B 68  ? O ARG B 68  N TYR B 59  ? N TYR B 59  
F 2 3 O ARG B 58  ? O ARG B 58  N GLU B 104 ? N GLU B 104 
F 3 4 O TYR B 101 ? O TYR B 101 N PHE B 116 ? N PHE B 116 
G 1 2 O LEU B 160 ? O LEU B 160 N GLY B 131 ? N GLY B 131 
G 2 3 O TYR B 128 ? O TYR B 128 N ILE B 394 ? N ILE B 394 
G 3 4 O HIS B 389 ? O HIS B 389 N ASN B 405 ? N ASN B 405 
G 4 5 O ALA B 400 ? O ALA B 400 N PHE B 420 ? N PHE B 420 
H 1 2 O TYR B 238 ? O TYR B 238 N VAL B 249 ? N VAL B 249 
H 2 3 O HIS B 246 ? O HIS B 246 N TRP B 280 ? N TRP B 280 
H 3 4 O VAL B 283 ? O VAL B 283 N VAL B 318 ? N VAL B 318 
H 4 5 O VAL B 319 ? O VAL B 319 N VAL B 355 ? N VAL B 355 
H 5 6 O THR B 358 ? O THR B 358 N GLU B 328 ? N GLU B 328 
H 6 7 O TYR B 327 ? O TYR B 327 N GLU B 384 ? N GLU B 384 
I 1 2 O HIS C 31  ? O HIS C 31  N SER C 45  ? N SER C 45  
I 2 3 O MET C 42  ? O MET C 42  N ILE C 92  ? N ILE C 92  
I 3 4 O ILE C 87  ? O ILE C 87  N SER C 75  ? N SER C 75  
J 1 2 O ARG C 68  ? O ARG C 68  N TYR C 59  ? N TYR C 59  
J 2 3 O ARG C 58  ? O ARG C 58  N GLU C 104 ? N GLU C 104 
J 3 4 O TYR C 101 ? O TYR C 101 N PHE C 116 ? N PHE C 116 
K 1 2 O THR C 158 ? O THR C 158 N GLY C 131 ? N GLY C 131 
K 2 3 O TYR C 128 ? O TYR C 128 N ILE C 394 ? N ILE C 394 
K 3 4 O HIS C 389 ? O HIS C 389 N ASN C 405 ? N ASN C 405 
K 4 5 O ALA C 400 ? O ALA C 400 N PHE C 420 ? N PHE C 420 
L 1 2 O TYR C 238 ? O TYR C 238 N VAL C 249 ? N VAL C 249 
L 2 3 O HIS C 246 ? O HIS C 246 N TRP C 280 ? N TRP C 280 
L 3 4 O VAL C 283 ? O VAL C 283 N VAL C 318 ? N VAL C 318 
L 4 5 O VAL C 319 ? O VAL C 319 N VAL C 355 ? N VAL C 355 
L 5 6 O THR C 358 ? O THR C 358 N GLU C 328 ? N GLU C 328 
L 6 7 O TYR C 327 ? O TYR C 327 N GLU C 384 ? N GLU C 384 
M 1 2 O HIS D 31  ? O HIS D 31  N SER D 45  ? N SER D 45  
M 2 3 O MET D 42  ? O MET D 42  N ILE D 92  ? N ILE D 92  
M 3 4 O ILE D 87  ? O ILE D 87  N SER D 75  ? N SER D 75  
N 1 2 O ARG D 68  ? O ARG D 68  N TYR D 59  ? N TYR D 59  
N 2 3 O ARG D 58  ? O ARG D 58  N GLU D 104 ? N GLU D 104 
N 3 4 O TYR D 101 ? O TYR D 101 N PHE D 116 ? N PHE D 116 
O 1 2 O LEU D 160 ? O LEU D 160 N GLY D 131 ? N GLY D 131 
O 2 3 O TYR D 128 ? O TYR D 128 N ILE D 394 ? N ILE D 394 
O 3 4 O HIS D 389 ? O HIS D 389 N ASN D 405 ? N ASN D 405 
O 4 5 O ALA D 400 ? O ALA D 400 N PHE D 420 ? N PHE D 420 
P 1 2 O TYR D 238 ? O TYR D 238 N VAL D 249 ? N VAL D 249 
P 2 3 O HIS D 246 ? O HIS D 246 N TRP D 280 ? N TRP D 280 
P 3 4 O VAL D 283 ? O VAL D 283 N VAL D 318 ? N VAL D 318 
P 4 5 O VAL D 319 ? O VAL D 319 N VAL D 355 ? N VAL D 355 
Q 1 2 O TYR D 327 ? O TYR D 327 N GLU D 384 ? N GLU D 384 
# 
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 
ACA Unknown  ? ? ? ? 2  'PHOSPHATASE ACTIVE SITE.'            
ACB Unknown  ? ? ? ? 2  'PHOSPHATASE ACTIVE SITE.'            
ACC Unknown  ? ? ? ? 2  'PHOSPHATASE ACTIVE SITE.'            
ACD Unknown  ? ? ? ? 2  'PHOSPHATASE ACTIVE SITE.'            
AC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG A 433A' 
AC2 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG A 434A' 
AC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG A 435A' 
AC4 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG A 436A' 
AC5 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG A 437A' 
AC6 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG B 433A' 
AC7 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG B 434A' 
AC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG B 435A' 
AC9 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG B 436A' 
BC1 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG B 437A' 
BC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG C 433A' 
BC3 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG C 434A' 
BC4 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG C 435A' 
BC5 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG C 436A' 
BC6 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG C 437A' 
BC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG D 433A' 
BC8 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG D 434A' 
BC9 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG D 435A' 
CC1 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG D 436A' 
CC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG D 437A' 
CC3 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE FE A 438'   
CC4 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE ZN A 439'   
CC5 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE PO4 A 440'  
CC6 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE FE B 438'   
CC7 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE ZN B 439'   
CC8 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE PO4 B 440'  
CC9 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE FE C 438'   
DC1 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE ZN C 439'   
DC2 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE PO4 C 440'  
DC3 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE FE D 438'   
DC4 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE ZN D 439'   
DC5 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE PO4 D 440'  
# 
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   ACA 2  FE  J  .   ? FE  A 438 . ? 1_555 ? 
2   ACA 2  ZN  K  .   ? ZN  A 439 . ? 1_555 ? 
3   ACB 2  FE  R  .   ? FE  B 438 . ? 1_555 ? 
4   ACB 2  ZN  S  .   ? ZN  B 439 . ? 1_555 ? 
5   ACC 2  FE  Z  .   ? FE  C 438 . ? 1_555 ? 
6   ACC 2  ZN  AA .   ? ZN  C 439 . ? 1_555 ? 
7   ACD 2  FE  HA .   ? FE  D 438 . ? 1_555 ? 
8   ACD 2  ZN  IA .   ? ZN  D 439 . ? 1_555 ? 
9   AC1 4  ASN A  81  ? ASN A 81  . ? 1_555 ? 
10  AC1 4  TYR D  24  ? TYR D 24  . ? 1_555 ? 
11  AC1 4  ASP D  50  ? ASP D 50  . ? 1_555 ? 
12  AC1 4  GLU D  51  ? GLU D 51  . ? 1_555 ? 
13  AC2 3  TYR A  24  ? TYR A 24  . ? 1_555 ? 
14  AC2 3  ARG A  108 ? ARG A 108 . ? 1_555 ? 
15  AC2 3  ASN A  109 ? ASN A 109 . ? 1_555 ? 
16  AC3 5  MET A  11  ? MET A 11  . ? 1_555 ? 
17  AC3 5  ASP A  16  ? ASP A 16  . ? 1_555 ? 
18  AC3 5  ASN A  143 ? ASN A 143 . ? 1_555 ? 
19  AC3 5  SER A  147 ? SER A 147 . ? 1_555 ? 
20  AC3 5  ARG A  188 ? ARG A 188 . ? 1_555 ? 
21  AC4 3  PRO A  208 ? PRO A 208 . ? 1_555 ? 
22  AC4 3  GLU A  209 ? GLU A 209 . ? 1_555 ? 
23  AC4 3  ASN A  211 ? ASN A 211 . ? 1_555 ? 
24  AC5 2  ASN A  396 ? ASN A 396 . ? 1_555 ? 
25  AC5 2  HIS A  399 ? HIS A 399 . ? 1_555 ? 
26  AC6 4  TYR B  24  ? TYR B 24  . ? 4_556 ? 
27  AC6 4  ASP B  50  ? ASP B 50  . ? 4_556 ? 
28  AC6 4  GLU B  51  ? GLU B 51  . ? 4_556 ? 
29  AC6 4  ASN B  81  ? ASN B 81  . ? 1_555 ? 
30  AC7 3  TYR B  24  ? TYR B 24  . ? 1_555 ? 
31  AC7 3  ARG B  108 ? ARG B 108 . ? 1_555 ? 
32  AC7 3  ASN B  109 ? ASN B 109 . ? 1_555 ? 
33  AC8 5  MET B  11  ? MET B 11  . ? 1_555 ? 
34  AC8 5  ASP B  16  ? ASP B 16  . ? 1_555 ? 
35  AC8 5  ASN B  143 ? ASN B 143 . ? 1_555 ? 
36  AC8 5  SER B  147 ? SER B 147 . ? 1_555 ? 
37  AC8 5  ARG B  188 ? ARG B 188 . ? 1_555 ? 
38  AC9 3  PRO B  208 ? PRO B 208 . ? 1_555 ? 
39  AC9 3  GLU B  209 ? GLU B 209 . ? 1_555 ? 
40  AC9 3  ASN B  211 ? ASN B 211 . ? 1_555 ? 
41  BC1 2  ASN B  396 ? ASN B 396 . ? 1_555 ? 
42  BC1 2  TRP B  419 ? TRP B 419 . ? 1_555 ? 
43  BC2 4  TYR C  24  ? TYR C 24  . ? 4_556 ? 
44  BC2 4  ASP C  50  ? ASP C 50  . ? 4_556 ? 
45  BC2 4  GLU C  51  ? GLU C 51  . ? 4_556 ? 
46  BC2 4  ASN C  81  ? ASN C 81  . ? 1_555 ? 
47  BC3 3  TYR C  24  ? TYR C 24  . ? 1_555 ? 
48  BC3 3  ARG C  108 ? ARG C 108 . ? 1_555 ? 
49  BC3 3  ASN C  109 ? ASN C 109 . ? 1_555 ? 
50  BC4 5  MET C  11  ? MET C 11  . ? 1_555 ? 
51  BC4 5  ASP C  16  ? ASP C 16  . ? 1_555 ? 
52  BC4 5  ASN C  143 ? ASN C 143 . ? 1_555 ? 
53  BC4 5  SER C  147 ? SER C 147 . ? 1_555 ? 
54  BC4 5  ARG C  188 ? ARG C 188 . ? 1_555 ? 
55  BC5 3  PRO C  208 ? PRO C 208 . ? 1_555 ? 
56  BC5 3  GLU C  209 ? GLU C 209 . ? 1_555 ? 
57  BC5 3  ASN C  211 ? ASN C 211 . ? 1_555 ? 
58  BC6 3  ASN C  396 ? ASN C 396 . ? 1_555 ? 
59  BC6 3  HIS C  399 ? HIS C 399 . ? 1_555 ? 
60  BC6 3  TRP C  419 ? TRP C 419 . ? 1_555 ? 
61  BC7 4  TYR A  24  ? TYR A 24  . ? 1_555 ? 
62  BC7 4  ASP A  50  ? ASP A 50  . ? 1_555 ? 
63  BC7 4  GLU A  51  ? GLU A 51  . ? 1_555 ? 
64  BC7 4  ASN D  81  ? ASN D 81  . ? 1_555 ? 
65  BC8 3  TYR D  24  ? TYR D 24  . ? 1_555 ? 
66  BC8 3  ARG D  108 ? ARG D 108 . ? 1_555 ? 
67  BC8 3  ASN D  109 ? ASN D 109 . ? 1_555 ? 
68  BC9 5  MET D  11  ? MET D 11  . ? 1_555 ? 
69  BC9 5  ASP D  16  ? ASP D 16  . ? 1_555 ? 
70  BC9 5  ASN D  143 ? ASN D 143 . ? 1_555 ? 
71  BC9 5  SER D  147 ? SER D 147 . ? 1_555 ? 
72  BC9 5  ARG D  188 ? ARG D 188 . ? 1_555 ? 
73  CC1 3  PRO D  208 ? PRO D 208 . ? 1_555 ? 
74  CC1 3  GLU D  209 ? GLU D 209 . ? 1_555 ? 
75  CC1 3  ASN D  211 ? ASN D 211 . ? 1_555 ? 
76  CC2 4  ARG C  397 ? ARG C 397 . ? 6_554 ? 
77  CC2 4  ASN D  396 ? ASN D 396 . ? 1_555 ? 
78  CC2 4  HIS D  399 ? HIS D 399 . ? 1_555 ? 
79  CC2 4  TRP D  419 ? TRP D 419 . ? 1_555 ? 
80  CC3 6  ASP A  135 ? ASP A 135 . ? 1_555 ? 
81  CC3 6  ASP A  164 ? ASP A 164 . ? 1_555 ? 
82  CC3 6  TYR A  167 ? TYR A 167 . ? 1_555 ? 
83  CC3 6  HIS A  325 ? HIS A 325 . ? 1_555 ? 
84  CC3 6  ZN  K  .   ? ZN  A 439 . ? 1_555 ? 
85  CC3 6  PO4 L  .   ? PO4 A 440 . ? 1_555 ? 
86  CC4 6  ASP A  164 ? ASP A 164 . ? 1_555 ? 
87  CC4 6  ASN A  201 ? ASN A 201 . ? 1_555 ? 
88  CC4 6  HIS A  286 ? HIS A 286 . ? 1_555 ? 
89  CC4 6  HIS A  323 ? HIS A 323 . ? 1_555 ? 
90  CC4 6  FE  J  .   ? FE  A 438 . ? 1_555 ? 
91  CC4 6  PO4 L  .   ? PO4 A 440 . ? 1_555 ? 
92  CC5 9  ASP A  164 ? ASP A 164 . ? 1_555 ? 
93  CC5 9  TYR A  167 ? TYR A 167 . ? 1_555 ? 
94  CC5 9  ASN A  201 ? ASN A 201 . ? 1_555 ? 
95  CC5 9  HIS A  202 ? HIS A 202 . ? 1_555 ? 
96  CC5 9  HIS A  296 ? HIS A 296 . ? 1_555 ? 
97  CC5 9  HIS A  323 ? HIS A 323 . ? 1_555 ? 
98  CC5 9  HIS A  325 ? HIS A 325 . ? 1_555 ? 
99  CC5 9  FE  J  .   ? FE  A 438 . ? 1_555 ? 
100 CC5 9  ZN  K  .   ? ZN  A 439 . ? 1_555 ? 
101 CC6 6  ASP B  135 ? ASP B 135 . ? 1_555 ? 
102 CC6 6  ASP B  164 ? ASP B 164 . ? 1_555 ? 
103 CC6 6  TYR B  167 ? TYR B 167 . ? 1_555 ? 
104 CC6 6  HIS B  325 ? HIS B 325 . ? 1_555 ? 
105 CC6 6  ZN  S  .   ? ZN  B 439 . ? 1_555 ? 
106 CC6 6  PO4 T  .   ? PO4 B 440 . ? 1_555 ? 
107 CC7 6  ASP B  164 ? ASP B 164 . ? 1_555 ? 
108 CC7 6  ASN B  201 ? ASN B 201 . ? 1_555 ? 
109 CC7 6  HIS B  286 ? HIS B 286 . ? 1_555 ? 
110 CC7 6  HIS B  323 ? HIS B 323 . ? 1_555 ? 
111 CC7 6  FE  R  .   ? FE  B 438 . ? 1_555 ? 
112 CC7 6  PO4 T  .   ? PO4 B 440 . ? 1_555 ? 
113 CC8 10 ASP B  164 ? ASP B 164 . ? 1_555 ? 
114 CC8 10 TYR B  167 ? TYR B 167 . ? 1_555 ? 
115 CC8 10 ASN B  201 ? ASN B 201 . ? 1_555 ? 
116 CC8 10 HIS B  202 ? HIS B 202 . ? 1_555 ? 
117 CC8 10 HIS B  295 ? HIS B 295 . ? 1_555 ? 
118 CC8 10 HIS B  296 ? HIS B 296 . ? 1_555 ? 
119 CC8 10 HIS B  323 ? HIS B 323 . ? 1_555 ? 
120 CC8 10 HIS B  325 ? HIS B 325 . ? 1_555 ? 
121 CC8 10 FE  R  .   ? FE  B 438 . ? 1_555 ? 
122 CC8 10 ZN  S  .   ? ZN  B 439 . ? 1_555 ? 
123 CC9 6  ASP C  135 ? ASP C 135 . ? 1_555 ? 
124 CC9 6  ASP C  164 ? ASP C 164 . ? 1_555 ? 
125 CC9 6  TYR C  167 ? TYR C 167 . ? 1_555 ? 
126 CC9 6  HIS C  325 ? HIS C 325 . ? 1_555 ? 
127 CC9 6  ZN  AA .   ? ZN  C 439 . ? 1_555 ? 
128 CC9 6  PO4 BA .   ? PO4 C 440 . ? 1_555 ? 
129 DC1 6  ASP C  164 ? ASP C 164 . ? 1_555 ? 
130 DC1 6  ASN C  201 ? ASN C 201 . ? 1_555 ? 
131 DC1 6  HIS C  286 ? HIS C 286 . ? 1_555 ? 
132 DC1 6  HIS C  323 ? HIS C 323 . ? 1_555 ? 
133 DC1 6  FE  Z  .   ? FE  C 438 . ? 1_555 ? 
134 DC1 6  PO4 BA .   ? PO4 C 440 . ? 1_555 ? 
135 DC2 10 ASP C  135 ? ASP C 135 . ? 1_555 ? 
136 DC2 10 ASP C  164 ? ASP C 164 . ? 1_555 ? 
137 DC2 10 TYR C  167 ? TYR C 167 . ? 1_555 ? 
138 DC2 10 ASN C  201 ? ASN C 201 . ? 1_555 ? 
139 DC2 10 HIS C  202 ? HIS C 202 . ? 1_555 ? 
140 DC2 10 HIS C  296 ? HIS C 296 . ? 1_555 ? 
141 DC2 10 HIS C  323 ? HIS C 323 . ? 1_555 ? 
142 DC2 10 HIS C  325 ? HIS C 325 . ? 1_555 ? 
143 DC2 10 FE  Z  .   ? FE  C 438 . ? 1_555 ? 
144 DC2 10 ZN  AA .   ? ZN  C 439 . ? 1_555 ? 
145 DC3 6  ASP D  135 ? ASP D 135 . ? 1_555 ? 
146 DC3 6  ASP D  164 ? ASP D 164 . ? 1_555 ? 
147 DC3 6  TYR D  167 ? TYR D 167 . ? 1_555 ? 
148 DC3 6  HIS D  325 ? HIS D 325 . ? 1_555 ? 
149 DC3 6  ZN  IA .   ? ZN  D 439 . ? 1_555 ? 
150 DC3 6  PO4 JA .   ? PO4 D 440 . ? 1_555 ? 
151 DC4 6  ASP D  164 ? ASP D 164 . ? 1_555 ? 
152 DC4 6  ASN D  201 ? ASN D 201 . ? 1_555 ? 
153 DC4 6  HIS D  286 ? HIS D 286 . ? 1_555 ? 
154 DC4 6  HIS D  323 ? HIS D 323 . ? 1_555 ? 
155 DC4 6  FE  HA .   ? FE  D 438 . ? 1_555 ? 
156 DC4 6  PO4 JA .   ? PO4 D 440 . ? 1_555 ? 
157 DC5 9  ASP D  164 ? ASP D 164 . ? 1_555 ? 
158 DC5 9  TYR D  167 ? TYR D 167 . ? 1_555 ? 
159 DC5 9  ASN D  201 ? ASN D 201 . ? 1_555 ? 
160 DC5 9  HIS D  202 ? HIS D 202 . ? 1_555 ? 
161 DC5 9  HIS D  296 ? HIS D 296 . ? 1_555 ? 
162 DC5 9  HIS D  323 ? HIS D 323 . ? 1_555 ? 
163 DC5 9  HIS D  325 ? HIS D 325 . ? 1_555 ? 
164 DC5 9  FE  HA .   ? FE  D 438 . ? 1_555 ? 
165 DC5 9  ZN  IA .   ? ZN  D 439 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4KBP 
_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                    4KBP 
_atom_sites.fract_transf_matrix[1][1]   0.007536 
_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]   0.002879 
_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]   0.007770 
_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  
FE 
N  
O  
P  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . ARG A  1 9   ? 63.181  63.672  64.588  1.00 53.09  ? 9   ARG A N   1 
ATOM   2     C  CA  . ARG A  1 9   ? 64.555  63.622  65.205  1.00 49.29  ? 9   ARG A CA  1 
ATOM   3     C  C   . ARG A  1 9   ? 65.514  64.724  64.723  1.00 44.35  ? 9   ARG A C   1 
ATOM   4     O  O   . ARG A  1 9   ? 66.736  64.618  64.902  1.00 41.09  ? 9   ARG A O   1 
ATOM   5     C  CB  . ARG A  1 9   ? 65.206  62.243  64.980  1.00 60.56  ? 9   ARG A CB  1 
ATOM   6     C  CG  . ARG A  1 9   ? 64.618  61.090  65.839  1.00 67.80  ? 9   ARG A CG  1 
ATOM   7     C  CD  . ARG A  1 9   ? 65.519  59.818  65.904  1.00 75.76  ? 9   ARG A CD  1 
ATOM   8     N  NE  . ARG A  1 9   ? 66.902  60.074  66.342  1.00 84.84  ? 9   ARG A NE  1 
ATOM   9     C  CZ  . ARG A  1 9   ? 67.280  60.537  67.544  1.00 85.70  ? 9   ARG A CZ  1 
ATOM   10    N  NH1 . ARG A  1 9   ? 66.388  60.812  68.489  1.00 90.18  ? 9   ARG A NH1 1 
ATOM   11    N  NH2 . ARG A  1 9   ? 68.569  60.756  67.801  1.00 83.94  ? 9   ARG A NH2 1 
ATOM   12    N  N   . ASP A  1 10  ? 64.974  65.718  64.017  1.00 39.92  ? 10  ASP A N   1 
ATOM   13    C  CA  . ASP A  1 10  ? 65.784  66.839  63.541  1.00 38.13  ? 10  ASP A CA  1 
ATOM   14    C  C   . ASP A  1 10  ? 66.156  67.734  64.758  1.00 33.99  ? 10  ASP A C   1 
ATOM   15    O  O   . ASP A  1 10  ? 65.326  67.972  65.632  1.00 30.47  ? 10  ASP A O   1 
ATOM   16    C  CB  . ASP A  1 10  ? 65.024  67.632  62.450  1.00 37.23  ? 10  ASP A CB  1 
ATOM   17    C  CG  . ASP A  1 10  ? 65.332  67.142  61.009  1.00 41.55  ? 10  ASP A CG  1 
ATOM   18    O  OD1 . ASP A  1 10  ? 66.499  66.774  60.712  1.00 45.92  ? 10  ASP A OD1 1 
ATOM   19    O  OD2 . ASP A  1 10  ? 64.421  67.171  60.142  1.00 40.86  ? 10  ASP A OD2 1 
ATOM   20    N  N   . MET A  1 11  ? 67.416  68.140  64.865  1.00 26.63  ? 11  MET A N   1 
ATOM   21    C  CA  . MET A  1 11  ? 67.848  68.973  65.961  1.00 22.72  ? 11  MET A CA  1 
ATOM   22    C  C   . MET A  1 11  ? 67.033  70.236  65.910  1.00 29.69  ? 11  MET A C   1 
ATOM   23    O  O   . MET A  1 11  ? 66.732  70.777  64.850  1.00 34.94  ? 11  MET A O   1 
ATOM   24    C  CB  . MET A  1 11  ? 69.315  69.309  65.820  1.00 18.57  ? 11  MET A CB  1 
ATOM   25    C  CG  . MET A  1 11  ? 70.165  68.122  65.584  1.00 18.37  ? 11  MET A CG  1 
ATOM   26    S  SD  . MET A  1 11  ? 71.808  68.609  65.741  1.00 31.96  ? 11  MET A SD  1 
ATOM   27    C  CE  . MET A  1 11  ? 72.330  68.786  64.071  1.00 27.33  ? 11  MET A CE  1 
ATOM   28    N  N   . PRO A  1 12  ? 66.598  70.701  67.056  1.00 34.45  ? 12  PRO A N   1 
ATOM   29    C  CA  . PRO A  1 12  ? 65.788  71.910  67.186  1.00 34.39  ? 12  PRO A CA  1 
ATOM   30    C  C   . PRO A  1 12  ? 66.574  73.157  66.826  1.00 34.36  ? 12  PRO A C   1 
ATOM   31    O  O   . PRO A  1 12  ? 67.811  73.201  66.930  1.00 30.29  ? 12  PRO A O   1 
ATOM   32    C  CB  . PRO A  1 12  ? 65.395  71.875  68.651  1.00 38.23  ? 12  PRO A CB  1 
ATOM   33    C  CG  . PRO A  1 12  ? 66.593  71.210  69.287  1.00 37.59  ? 12  PRO A CG  1 
ATOM   34    C  CD  . PRO A  1 12  ? 66.811  70.062  68.355  1.00 35.34  ? 12  PRO A CD  1 
ATOM   35    N  N   . LEU A  1 13  ? 65.840  74.195  66.453  1.00 34.39  ? 13  LEU A N   1 
ATOM   36    C  CA  . LEU A  1 13  ? 66.462  75.438  66.028  1.00 35.63  ? 13  LEU A CA  1 
ATOM   37    C  C   . LEU A  1 13  ? 67.472  76.012  66.962  1.00 40.03  ? 13  LEU A C   1 
ATOM   38    O  O   . LEU A  1 13  ? 68.428  76.651  66.519  1.00 44.96  ? 13  LEU A O   1 
ATOM   39    C  CB  . LEU A  1 13  ? 65.418  76.484  65.704  1.00 32.60  ? 13  LEU A CB  1 
ATOM   40    C  CG  . LEU A  1 13  ? 64.615  76.176  64.444  1.00 30.55  ? 13  LEU A CG  1 
ATOM   41    C  CD1 . LEU A  1 13  ? 63.645  77.278  64.172  1.00 35.12  ? 13  LEU A CD1 1 
ATOM   42    C  CD2 . LEU A  1 13  ? 65.550  76.035  63.266  1.00 33.03  ? 13  LEU A CD2 1 
ATOM   43    N  N   . ASP A  1 14  ? 67.270  75.783  68.257  1.00 48.17  ? 14  ASP A N   1 
ATOM   44    C  CA  . ASP A  1 14  ? 68.199  76.304  69.273  1.00 53.11  ? 14  ASP A CA  1 
ATOM   45    C  C   . ASP A  1 14  ? 69.503  75.538  69.440  1.00 47.87  ? 14  ASP A C   1 
ATOM   46    O  O   . ASP A  1 14  ? 70.478  76.077  69.949  1.00 50.89  ? 14  ASP A O   1 
ATOM   47    C  CB  . ASP A  1 14  ? 67.520  76.582  70.656  1.00 63.51  ? 14  ASP A CB  1 
ATOM   48    C  CG  . ASP A  1 14  ? 66.581  75.447  71.166  1.00 74.11  ? 14  ASP A CG  1 
ATOM   49    O  OD1 . ASP A  1 14  ? 65.409  75.330  70.711  1.00 82.49  ? 14  ASP A OD1 1 
ATOM   50    O  OD2 . ASP A  1 14  ? 66.973  74.740  72.122  1.00 84.38  ? 14  ASP A OD2 1 
ATOM   51    N  N   . SER A  1 15  ? 69.544  74.324  68.919  1.00 41.95  ? 15  SER A N   1 
ATOM   52    C  CA  . SER A  1 15  ? 70.707  73.506  69.050  1.00 38.90  ? 15  SER A CA  1 
ATOM   53    C  C   . SER A  1 15  ? 71.944  74.307  68.884  1.00 32.97  ? 15  SER A C   1 
ATOM   54    O  O   . SER A  1 15  ? 72.019  75.166  68.040  1.00 34.87  ? 15  SER A O   1 
ATOM   55    C  CB  . SER A  1 15  ? 70.649  72.395  68.046  1.00 40.71  ? 15  SER A CB  1 
ATOM   56    O  OG  . SER A  1 15  ? 69.422  71.724  68.228  1.00 50.17  ? 15  SER A OG  1 
ATOM   57    N  N   . ASP A  1 16  ? 72.834  74.142  69.833  1.00 28.45  ? 16  ASP A N   1 
ATOM   58    C  CA  . ASP A  1 16  ? 74.119  74.805  69.839  1.00 30.88  ? 16  ASP A CA  1 
ATOM   59    C  C   . ASP A  1 16  ? 74.774  74.769  68.496  1.00 27.58  ? 16  ASP A C   1 
ATOM   60    O  O   . ASP A  1 16  ? 75.608  75.601  68.136  1.00 23.54  ? 16  ASP A O   1 
ATOM   61    C  CB  . ASP A  1 16  ? 75.050  74.070  70.792  1.00 42.23  ? 16  ASP A CB  1 
ATOM   62    C  CG  . ASP A  1 16  ? 74.951  72.562  70.649  1.00 48.88  ? 16  ASP A CG  1 
ATOM   63    O  OD1 . ASP A  1 16  ? 73.914  71.986  71.055  1.00 60.86  ? 16  ASP A OD1 1 
ATOM   64    O  OD2 . ASP A  1 16  ? 75.886  71.957  70.116  1.00 48.41  ? 16  ASP A OD2 1 
ATOM   65    N  N   . VAL A  1 17  ? 74.449  73.725  67.777  1.00 28.28  ? 17  VAL A N   1 
ATOM   66    C  CA  . VAL A  1 17  ? 75.040  73.528  66.491  1.00 24.85  ? 17  VAL A CA  1 
ATOM   67    C  C   . VAL A  1 17  ? 74.615  74.599  65.468  1.00 23.73  ? 17  VAL A C   1 
ATOM   68    O  O   . VAL A  1 17  ? 75.399  75.027  64.633  1.00 27.40  ? 17  VAL A O   1 
ATOM   69    C  CB  . VAL A  1 17  ? 74.800  72.056  66.108  1.00 20.46  ? 17  VAL A CB  1 
ATOM   70    C  CG1 . VAL A  1 17  ? 73.414  71.833  65.493  1.00 22.98  ? 17  VAL A CG1 1 
ATOM   71    C  CG2 . VAL A  1 17  ? 75.945  71.567  65.282  1.00 27.81  ? 17  VAL A CG2 1 
ATOM   72    N  N   . PHE A  1 18  ? 73.414  75.132  65.637  1.00 27.04  ? 18  PHE A N   1 
ATOM   73    C  CA  . PHE A  1 18  ? 72.853  76.157  64.754  1.00 28.66  ? 18  PHE A CA  1 
ATOM   74    C  C   . PHE A  1 18  ? 73.127  77.617  65.161  1.00 38.06  ? 18  PHE A C   1 
ATOM   75    O  O   . PHE A  1 18  ? 72.632  78.533  64.509  1.00 41.64  ? 18  PHE A O   1 
ATOM   76    C  CB  . PHE A  1 18  ? 71.336  75.980  64.658  1.00 16.25  ? 18  PHE A CB  1 
ATOM   77    C  CG  . PHE A  1 18  ? 70.918  74.639  64.198  1.00 15.49  ? 18  PHE A CG  1 
ATOM   78    C  CD1 . PHE A  1 18  ? 71.620  73.982  63.196  1.00 16.28  ? 18  PHE A CD1 1 
ATOM   79    C  CD2 . PHE A  1 18  ? 69.767  74.048  64.707  1.00 19.91  ? 18  PHE A CD2 1 
ATOM   80    C  CE1 . PHE A  1 18  ? 71.193  72.770  62.699  1.00 13.60  ? 18  PHE A CE1 1 
ATOM   81    C  CE2 . PHE A  1 18  ? 69.319  72.830  64.213  1.00 13.15  ? 18  PHE A CE2 1 
ATOM   82    C  CZ  . PHE A  1 18  ? 70.034  72.193  63.208  1.00 15.16  ? 18  PHE A CZ  1 
ATOM   83    N  N   . ARG A  1 19  ? 73.842  77.844  66.266  1.00 46.90  ? 19  ARG A N   1 
ATOM   84    C  CA  . ARG A  1 19  ? 74.136  79.208  66.735  1.00 47.47  ? 19  ARG A CA  1 
ATOM   85    C  C   . ARG A  1 19  ? 74.795  80.075  65.691  1.00 40.71  ? 19  ARG A C   1 
ATOM   86    O  O   . ARG A  1 19  ? 75.671  79.622  64.952  1.00 42.83  ? 19  ARG A O   1 
ATOM   87    C  CB  . ARG A  1 19  ? 75.002  79.177  67.995  1.00 62.09  ? 19  ARG A CB  1 
ATOM   88    C  CG  . ARG A  1 19  ? 74.186  78.833  69.224  1.00 83.10  ? 19  ARG A CG  1 
ATOM   89    C  CD  . ARG A  1 19  ? 75.034  78.492  70.461  1.00 99.88  ? 19  ARG A CD  1 
ATOM   90    N  NE  . ARG A  1 19  ? 74.167  78.039  71.563  1.00 114.20 ? 19  ARG A NE  1 
ATOM   91    C  CZ  . ARG A  1 19  ? 74.584  77.461  72.692  1.00 117.65 ? 19  ARG A CZ  1 
ATOM   92    N  NH1 . ARG A  1 19  ? 75.889  77.241  72.909  1.00 119.66 ? 19  ARG A NH1 1 
ATOM   93    N  NH2 . ARG A  1 19  ? 73.681  77.096  73.607  1.00 123.30 ? 19  ARG A NH2 1 
ATOM   94    N  N   . VAL A  1 20  ? 74.387  81.334  65.639  1.00 30.77  ? 20  VAL A N   1 
ATOM   95    C  CA  . VAL A  1 20  ? 74.943  82.237  64.649  1.00 27.97  ? 20  VAL A CA  1 
ATOM   96    C  C   . VAL A  1 20  ? 76.065  83.007  65.194  1.00 25.32  ? 20  VAL A C   1 
ATOM   97    O  O   . VAL A  1 20  ? 75.956  83.610  66.257  1.00 27.27  ? 20  VAL A O   1 
ATOM   98    C  CB  . VAL A  1 20  ? 73.910  83.206  64.043  1.00 29.48  ? 20  VAL A CB  1 
ATOM   99    C  CG1 . VAL A  1 20  ? 72.778  83.395  64.962  1.00 28.32  ? 20  VAL A CG1 1 
ATOM   100   C  CG2 . VAL A  1 20  ? 74.547  84.554  63.687  1.00 32.32  ? 20  VAL A CG2 1 
ATOM   101   N  N   . PRO A  1 21  ? 77.164  83.021  64.459  1.00 26.11  ? 21  PRO A N   1 
ATOM   102   C  CA  . PRO A  1 21  ? 78.378  83.727  64.848  1.00 33.09  ? 21  PRO A CA  1 
ATOM   103   C  C   . PRO A  1 21  ? 78.021  85.138  65.198  1.00 37.18  ? 21  PRO A C   1 
ATOM   104   O  O   . PRO A  1 21  ? 77.185  85.755  64.556  1.00 45.34  ? 21  PRO A O   1 
ATOM   105   C  CB  . PRO A  1 21  ? 79.282  83.612  63.624  1.00 32.70  ? 21  PRO A CB  1 
ATOM   106   C  CG  . PRO A  1 21  ? 78.310  83.331  62.516  1.00 36.07  ? 21  PRO A CG  1 
ATOM   107   C  CD  . PRO A  1 21  ? 77.295  82.427  63.136  1.00 28.95  ? 21  PRO A CD  1 
ATOM   108   N  N   . PRO A  1 22  ? 78.537  85.608  66.327  1.00 39.51  ? 22  PRO A N   1 
ATOM   109   C  CA  . PRO A  1 22  ? 78.327  86.940  66.868  1.00 39.37  ? 22  PRO A CA  1 
ATOM   110   C  C   . PRO A  1 22  ? 79.086  87.975  66.078  1.00 42.14  ? 22  PRO A C   1 
ATOM   111   O  O   . PRO A  1 22  ? 80.190  87.707  65.572  1.00 47.23  ? 22  PRO A O   1 
ATOM   112   C  CB  . PRO A  1 22  ? 78.908  86.810  68.247  1.00 42.11  ? 22  PRO A CB  1 
ATOM   113   C  CG  . PRO A  1 22  ? 80.111  85.911  68.001  1.00 45.98  ? 22  PRO A CG  1 
ATOM   114   C  CD  . PRO A  1 22  ? 79.473  84.840  67.168  1.00 43.34  ? 22  PRO A CD  1 
ATOM   115   N  N   . GLY A  1 23  ? 78.529  89.184  66.054  1.00 43.00  ? 23  GLY A N   1 
ATOM   116   C  CA  . GLY A  1 23  ? 79.136  90.284  65.310  1.00 42.03  ? 23  GLY A CA  1 
ATOM   117   C  C   . GLY A  1 23  ? 78.141  90.837  64.304  1.00 41.72  ? 23  GLY A C   1 
ATOM   118   O  O   . GLY A  1 23  ? 77.215  90.110  63.888  1.00 49.00  ? 23  GLY A O   1 
ATOM   119   N  N   . TYR A  1 24  ? 78.253  92.118  63.960  1.00 37.91  ? 24  TYR A N   1 
ATOM   120   C  CA  . TYR A  1 24  ? 77.315  92.691  63.015  1.00 33.66  ? 24  TYR A CA  1 
ATOM   121   C  C   . TYR A  1 24  ? 77.685  92.216  61.637  1.00 34.11  ? 24  TYR A C   1 
ATOM   122   O  O   . TYR A  1 24  ? 78.816  92.411  61.189  1.00 32.90  ? 24  TYR A O   1 
ATOM   123   C  CB  . TYR A  1 24  ? 77.339  94.214  63.031  1.00 29.89  ? 24  TYR A CB  1 
ATOM   124   C  CG  . TYR A  1 24  ? 76.513  94.835  61.918  1.00 24.65  ? 24  TYR A CG  1 
ATOM   125   C  CD1 . TYR A  1 24  ? 75.127  94.876  62.015  1.00 23.25  ? 24  TYR A CD1 1 
ATOM   126   C  CD2 . TYR A  1 24  ? 77.109  95.340  60.749  1.00 15.00  ? 24  TYR A CD2 1 
ATOM   127   C  CE1 . TYR A  1 24  ? 74.343  95.392  60.984  1.00 23.41  ? 24  TYR A CE1 1 
ATOM   128   C  CE2 . TYR A  1 24  ? 76.324  95.856  59.709  1.00 15.32  ? 24  TYR A CE2 1 
ATOM   129   C  CZ  . TYR A  1 24  ? 74.940  95.880  59.845  1.00 22.50  ? 24  TYR A CZ  1 
ATOM   130   O  OH  . TYR A  1 24  ? 74.108  96.400  58.881  1.00 30.64  ? 24  TYR A OH  1 
ATOM   131   N  N   . ASN A  1 25  ? 76.714  91.605  60.970  1.00 31.86  ? 25  ASN A N   1 
ATOM   132   C  CA  . ASN A  1 25  ? 76.886  91.124  59.615  1.00 31.30  ? 25  ASN A CA  1 
ATOM   133   C  C   . ASN A  1 25  ? 78.103  90.241  59.597  1.00 35.10  ? 25  ASN A C   1 
ATOM   134   O  O   . ASN A  1 25  ? 79.101  90.550  58.927  1.00 39.98  ? 25  ASN A O   1 
ATOM   135   C  CB  . ASN A  1 25  ? 77.134  92.302  58.712  1.00 24.37  ? 25  ASN A CB  1 
ATOM   136   C  CG  . ASN A  1 25  ? 76.667  92.072  57.326  1.00 26.73  ? 25  ASN A CG  1 
ATOM   137   O  OD1 . ASN A  1 25  ? 77.308  92.539  56.406  1.00 28.38  ? 25  ASN A OD1 1 
ATOM   138   N  ND2 . ASN A  1 25  ? 75.523  91.392  57.152  1.00 14.74  ? 25  ASN A ND2 1 
ATOM   139   N  N   . ALA A  1 26  ? 78.048  89.208  60.427  1.00 36.05  ? 26  ALA A N   1 
ATOM   140   C  CA  . ALA A  1 26  ? 79.122  88.233  60.569  1.00 33.18  ? 26  ALA A CA  1 
ATOM   141   C  C   . ALA A  1 26  ? 78.866  87.106  59.602  1.00 32.62  ? 26  ALA A C   1 
ATOM   142   O  O   . ALA A  1 26  ? 77.758  86.528  59.581  1.00 41.51  ? 26  ALA A O   1 
ATOM   143   C  CB  . ALA A  1 26  ? 79.150  87.687  61.982  1.00 32.10  ? 26  ALA A CB  1 
ATOM   144   N  N   . PRO A  1 27  ? 79.886  86.751  58.818  1.00 27.47  ? 27  PRO A N   1 
ATOM   145   C  CA  . PRO A  1 27  ? 79.846  85.691  57.812  1.00 28.01  ? 27  PRO A CA  1 
ATOM   146   C  C   . PRO A  1 27  ? 79.390  84.415  58.436  1.00 30.05  ? 27  PRO A C   1 
ATOM   147   O  O   . PRO A  1 27  ? 79.991  83.959  59.393  1.00 34.08  ? 27  PRO A O   1 
ATOM   148   C  CB  . PRO A  1 27  ? 81.305  85.525  57.421  1.00 24.41  ? 27  PRO A CB  1 
ATOM   149   C  CG  . PRO A  1 27  ? 81.870  86.856  57.671  1.00 27.36  ? 27  PRO A CG  1 
ATOM   150   C  CD  . PRO A  1 27  ? 81.253  87.237  58.987  1.00 24.34  ? 27  PRO A CD  1 
ATOM   151   N  N   . GLN A  1 28  ? 78.306  83.853  57.940  1.00 27.59  ? 28  GLN A N   1 
ATOM   152   C  CA  . GLN A  1 28  ? 77.866  82.608  58.487  1.00 25.24  ? 28  GLN A CA  1 
ATOM   153   C  C   . GLN A  1 28  ? 77.725  81.654  57.342  1.00 25.45  ? 28  GLN A C   1 
ATOM   154   O  O   . GLN A  1 28  ? 77.841  82.035  56.180  1.00 32.52  ? 28  GLN A O   1 
ATOM   155   C  CB  . GLN A  1 28  ? 76.560  82.792  59.209  1.00 21.42  ? 28  GLN A CB  1 
ATOM   156   C  CG  . GLN A  1 28  ? 75.421  83.031  58.355  1.00 14.39  ? 28  GLN A CG  1 
ATOM   157   C  CD  . GLN A  1 28  ? 74.236  83.278  59.196  1.00 20.57  ? 28  GLN A CD  1 
ATOM   158   O  OE1 . GLN A  1 28  ? 74.193  84.274  59.887  1.00 27.58  ? 28  GLN A OE1 1 
ATOM   159   N  NE2 . GLN A  1 28  ? 73.298  82.346  59.228  1.00 18.87  ? 28  GLN A NE2 1 
ATOM   160   N  N   . GLN A  1 29  ? 77.565  80.393  57.673  1.00 22.71  ? 29  GLN A N   1 
ATOM   161   C  CA  . GLN A  1 29  ? 77.386  79.364  56.663  1.00 16.07  ? 29  GLN A CA  1 
ATOM   162   C  C   . GLN A  1 29  ? 78.572  79.294  55.740  1.00 14.13  ? 29  GLN A C   1 
ATOM   163   O  O   . GLN A  1 29  ? 78.404  79.093  54.565  1.00 14.18  ? 29  GLN A O   1 
ATOM   164   C  CB  . GLN A  1 29  ? 76.098  79.614  55.875  1.00 12.57  ? 29  GLN A CB  1 
ATOM   165   C  CG  . GLN A  1 29  ? 74.809  79.615  56.714  1.00 21.08  ? 29  GLN A CG  1 
ATOM   166   C  CD  . GLN A  1 29  ? 73.516  79.848  55.892  1.00 27.21  ? 29  GLN A CD  1 
ATOM   167   O  OE1 . GLN A  1 29  ? 73.279  79.215  54.868  1.00 34.59  ? 29  GLN A OE1 1 
ATOM   168   N  NE2 . GLN A  1 29  ? 72.668  80.730  56.373  1.00 25.32  ? 29  GLN A NE2 1 
ATOM   169   N  N   . VAL A  1 30  ? 79.785  79.423  56.268  1.00 16.81  ? 30  VAL A N   1 
ATOM   170   C  CA  . VAL A  1 30  ? 80.966  79.374  55.406  1.00 19.39  ? 30  VAL A CA  1 
ATOM   171   C  C   . VAL A  1 30  ? 81.200  77.968  54.886  1.00 21.98  ? 30  VAL A C   1 
ATOM   172   O  O   . VAL A  1 30  ? 80.956  76.994  55.594  1.00 24.03  ? 30  VAL A O   1 
ATOM   173   C  CB  . VAL A  1 30  ? 82.216  79.907  56.113  1.00 18.10  ? 30  VAL A CB  1 
ATOM   174   C  CG1 . VAL A  1 30  ? 83.427  79.843  55.198  1.00 13.40  ? 30  VAL A CG1 1 
ATOM   175   C  CG2 . VAL A  1 30  ? 82.002  81.335  56.491  1.00 16.82  ? 30  VAL A CG2 1 
ATOM   176   N  N   . HIS A  1 31  ? 81.556  77.855  53.607  1.00 25.97  ? 31  HIS A N   1 
ATOM   177   C  CA  . HIS A  1 31  ? 81.825  76.541  53.004  1.00 24.98  ? 31  HIS A CA  1 
ATOM   178   C  C   . HIS A  1 31  ? 82.692  76.669  51.778  1.00 23.55  ? 31  HIS A C   1 
ATOM   179   O  O   . HIS A  1 31  ? 82.550  77.653  51.069  1.00 23.24  ? 31  HIS A O   1 
ATOM   180   C  CB  . HIS A  1 31  ? 80.529  75.799  52.675  1.00 19.98  ? 31  HIS A CB  1 
ATOM   181   C  CG  . HIS A  1 31  ? 79.526  76.578  51.861  1.00 22.90  ? 31  HIS A CG  1 
ATOM   182   N  ND1 . HIS A  1 31  ? 79.236  76.278  50.544  1.00 32.18  ? 31  HIS A ND1 1 
ATOM   183   C  CD2 . HIS A  1 31  ? 78.645  77.545  52.214  1.00 26.80  ? 31  HIS A CD2 1 
ATOM   184   C  CE1 . HIS A  1 31  ? 78.221  77.013  50.128  1.00 28.45  ? 31  HIS A CE1 1 
ATOM   185   N  NE2 . HIS A  1 31  ? 77.844  77.790  51.123  1.00 29.88  ? 31  HIS A NE2 1 
ATOM   186   N  N   . ILE A  1 32  ? 83.602  75.712  51.559  1.00 24.41  ? 32  ILE A N   1 
ATOM   187   C  CA  . ILE A  1 32  ? 84.500  75.737  50.405  1.00 24.60  ? 32  ILE A CA  1 
ATOM   188   C  C   . ILE A  1 32  ? 84.403  74.496  49.504  1.00 23.79  ? 32  ILE A C   1 
ATOM   189   O  O   . ILE A  1 32  ? 83.719  73.549  49.869  1.00 24.07  ? 32  ILE A O   1 
ATOM   190   C  CB  . ILE A  1 32  ? 85.957  75.898  50.869  1.00 25.44  ? 32  ILE A CB  1 
ATOM   191   C  CG1 . ILE A  1 32  ? 86.448  74.650  51.565  1.00 30.10  ? 32  ILE A CG1 1 
ATOM   192   C  CG2 . ILE A  1 32  ? 86.070  76.974  51.874  1.00 27.27  ? 32  ILE A CG2 1 
ATOM   193   C  CD1 . ILE A  1 32  ? 87.912  74.760  51.954  1.00 31.26  ? 32  ILE A CD1 1 
ATOM   194   N  N   . THR A  1 33  ? 85.026  74.546  48.320  1.00 19.24  ? 33  THR A N   1 
ATOM   195   C  CA  . THR A  1 33  ? 85.075  73.429  47.345  1.00 25.02  ? 33  THR A CA  1 
ATOM   196   C  C   . THR A  1 33  ? 86.166  73.701  46.332  1.00 25.43  ? 33  THR A C   1 
ATOM   197   O  O   . THR A  1 33  ? 86.612  74.831  46.149  1.00 29.33  ? 33  THR A O   1 
ATOM   198   C  CB  . THR A  1 33  ? 83.882  73.256  46.417  1.00 23.26  ? 33  THR A CB  1 
ATOM   199   O  OG1 . THR A  1 33  ? 82.711  73.793  47.009  1.00 43.49  ? 33  THR A OG1 1 
ATOM   200   C  CG2 . THR A  1 33  ? 83.672  71.801  46.141  1.00 20.24  ? 33  THR A CG2 1 
ATOM   201   N  N   . GLN A  1 34  ? 86.478  72.681  45.564  1.00 21.01  ? 34  GLN A N   1 
ATOM   202   C  CA  . GLN A  1 34  ? 87.501  72.837  44.592  1.00 19.87  ? 34  GLN A CA  1 
ATOM   203   C  C   . GLN A  1 34  ? 86.984  73.775  43.549  1.00 24.20  ? 34  GLN A C   1 
ATOM   204   O  O   . GLN A  1 34  ? 85.859  73.651  43.088  1.00 29.05  ? 34  GLN A O   1 
ATOM   205   C  CB  . GLN A  1 34  ? 87.892  71.489  44.011  1.00 16.30  ? 34  GLN A CB  1 
ATOM   206   C  CG  . GLN A  1 34  ? 89.037  71.618  43.123  1.00 13.17  ? 34  GLN A CG  1 
ATOM   207   C  CD  . GLN A  1 34  ? 89.736  70.351  42.972  1.00 19.12  ? 34  GLN A CD  1 
ATOM   208   O  OE1 . GLN A  1 34  ? 90.117  69.994  41.878  1.00 26.10  ? 34  GLN A OE1 1 
ATOM   209   N  NE2 . GLN A  1 34  ? 89.957  69.653  44.080  1.00 20.17  ? 34  GLN A NE2 1 
ATOM   210   N  N   . GLY A  1 35  ? 87.814  74.728  43.174  1.00 27.77  ? 35  GLY A N   1 
ATOM   211   C  CA  . GLY A  1 35  ? 87.411  75.704  42.186  1.00 29.74  ? 35  GLY A CA  1 
ATOM   212   C  C   . GLY A  1 35  ? 87.956  75.536  40.789  1.00 29.67  ? 35  GLY A C   1 
ATOM   213   O  O   . GLY A  1 35  ? 87.654  76.327  39.896  1.00 34.13  ? 35  GLY A O   1 
ATOM   214   N  N   . ASP A  1 36  ? 88.763  74.515  40.577  1.00 30.04  ? 36  ASP A N   1 
ATOM   215   C  CA  . ASP A  1 36  ? 89.304  74.286  39.248  1.00 32.67  ? 36  ASP A CA  1 
ATOM   216   C  C   . ASP A  1 36  ? 89.363  72.806  38.991  1.00 32.98  ? 36  ASP A C   1 
ATOM   217   O  O   . ASP A  1 36  ? 88.992  72.001  39.860  1.00 34.83  ? 36  ASP A O   1 
ATOM   218   C  CB  . ASP A  1 36  ? 90.697  74.883  39.090  1.00 37.38  ? 36  ASP A CB  1 
ATOM   219   C  CG  . ASP A  1 36  ? 91.751  74.210  39.970  1.00 40.34  ? 36  ASP A CG  1 
ATOM   220   O  OD1 . ASP A  1 36  ? 91.459  73.308  40.773  1.00 42.11  ? 36  ASP A OD1 1 
ATOM   221   O  OD2 . ASP A  1 36  ? 92.914  74.610  39.854  1.00 50.84  ? 36  ASP A OD2 1 
ATOM   222   N  N   . LEU A  1 37  ? 89.926  72.435  37.850  1.00 28.41  ? 37  LEU A N   1 
ATOM   223   C  CA  . LEU A  1 37  ? 90.002  71.022  37.550  1.00 27.25  ? 37  LEU A CA  1 
ATOM   224   C  C   . LEU A  1 37  ? 91.033  70.214  38.318  1.00 27.15  ? 37  LEU A C   1 
ATOM   225   O  O   . LEU A  1 37  ? 90.787  69.051  38.623  1.00 31.11  ? 37  LEU A O   1 
ATOM   226   C  CB  . LEU A  1 37  ? 90.254  70.843  36.079  1.00 26.01  ? 37  LEU A CB  1 
ATOM   227   C  CG  . LEU A  1 37  ? 90.112  69.407  35.637  1.00 22.77  ? 37  LEU A CG  1 
ATOM   228   C  CD1 . LEU A  1 37  ? 88.713  68.925  35.940  1.00 31.25  ? 37  LEU A CD1 1 
ATOM   229   C  CD2 . LEU A  1 37  ? 90.373  69.340  34.168  1.00 24.49  ? 37  LEU A CD2 1 
ATOM   230   N  N   . VAL A  1 38  ? 92.132  70.840  38.731  1.00 24.82  ? 38  VAL A N   1 
ATOM   231   C  CA  . VAL A  1 38  ? 93.228  70.093  39.339  1.00 26.00  ? 38  VAL A CA  1 
ATOM   232   C  C   . VAL A  1 38  ? 93.708  70.327  40.767  1.00 26.54  ? 38  VAL A C   1 
ATOM   233   O  O   . VAL A  1 38  ? 94.690  69.694  41.213  1.00 30.77  ? 38  VAL A O   1 
ATOM   234   C  CB  . VAL A  1 38  ? 94.467  70.146  38.398  1.00 31.13  ? 38  VAL A CB  1 
ATOM   235   C  CG1 . VAL A  1 38  ? 94.045  70.008  36.938  1.00 38.77  ? 38  VAL A CG1 1 
ATOM   236   C  CG2 . VAL A  1 38  ? 95.190  71.435  38.564  1.00 33.42  ? 38  VAL A CG2 1 
ATOM   237   N  N   . GLY A  1 39  ? 93.069  71.236  41.481  1.00 23.77  ? 39  GLY A N   1 
ATOM   238   C  CA  . GLY A  1 39  ? 93.492  71.445  42.846  1.00 23.84  ? 39  GLY A CA  1 
ATOM   239   C  C   . GLY A  1 39  ? 94.006  72.812  43.250  1.00 26.69  ? 39  GLY A C   1 
ATOM   240   O  O   . GLY A  1 39  ? 94.103  73.115  44.438  1.00 33.43  ? 39  GLY A O   1 
ATOM   241   N  N   . ARG A  1 40  ? 94.291  73.685  42.311  1.00 26.41  ? 40  ARG A N   1 
ATOM   242   C  CA  . ARG A  1 40  ? 94.778  74.972  42.743  1.00 29.74  ? 40  ARG A CA  1 
ATOM   243   C  C   . ARG A  1 40  ? 93.837  76.167  42.711  1.00 27.58  ? 40  ARG A C   1 
ATOM   244   O  O   . ARG A  1 40  ? 94.245  77.262  42.393  1.00 27.49  ? 40  ARG A O   1 
ATOM   245   C  CB  . ARG A  1 40  ? 96.147  75.279  42.143  1.00 32.86  ? 40  ARG A CB  1 
ATOM   246   C  CG  . ARG A  1 40  ? 96.283  75.228  40.665  1.00 40.56  ? 40  ARG A CG  1 
ATOM   247   C  CD  . ARG A  1 40  ? 97.700  74.780  40.261  1.00 49.71  ? 40  ARG A CD  1 
ATOM   248   N  NE  . ARG A  1 40  ? 98.741  75.646  40.805  1.00 59.76  ? 40  ARG A NE  1 
ATOM   249   C  CZ  . ARG A  1 40  ? 99.186  76.753  40.216  1.00 69.00  ? 40  ARG A CZ  1 
ATOM   250   N  NH1 . ARG A  1 40  ? 98.694  77.148  39.032  1.00 70.34  ? 40  ARG A NH1 1 
ATOM   251   N  NH2 . ARG A  1 40  ? 100.108 77.482  40.835  1.00 74.34  ? 40  ARG A NH2 1 
ATOM   252   N  N   . ALA A  1 41  ? 92.590  75.964  43.111  1.00 22.25  ? 41  ALA A N   1 
ATOM   253   C  CA  . ALA A  1 41  ? 91.650  77.053  43.155  1.00 18.82  ? 41  ALA A CA  1 
ATOM   254   C  C   . ALA A  1 41  ? 90.629  76.587  44.117  1.00 21.07  ? 41  ALA A C   1 
ATOM   255   O  O   . ALA A  1 41  ? 90.442  75.390  44.233  1.00 23.85  ? 41  ALA A O   1 
ATOM   256   C  CB  . ALA A  1 41  ? 91.040  77.242  41.838  1.00 24.23  ? 41  ALA A CB  1 
ATOM   257   N  N   . MET A  1 42  ? 90.051  77.509  44.883  1.00 19.29  ? 42  MET A N   1 
ATOM   258   C  CA  . MET A  1 42  ? 88.997  77.178  45.856  1.00 20.32  ? 42  MET A CA  1 
ATOM   259   C  C   . MET A  1 42  ? 87.820  78.092  45.685  1.00 21.77  ? 42  MET A C   1 
ATOM   260   O  O   . MET A  1 42  ? 87.988  79.257  45.288  1.00 28.85  ? 42  MET A O   1 
ATOM   261   C  CB  . MET A  1 42  ? 89.490  77.375  47.254  1.00 13.47  ? 42  MET A CB  1 
ATOM   262   C  CG  . MET A  1 42  ? 90.217  76.231  47.720  1.00 26.48  ? 42  MET A CG  1 
ATOM   263   S  SD  . MET A  1 42  ? 89.058  75.023  48.233  1.00 31.84  ? 42  MET A SD  1 
ATOM   264   C  CE  . MET A  1 42  ? 90.148  73.926  48.844  1.00 28.94  ? 42  MET A CE  1 
ATOM   265   N  N   . ILE A  1 43  ? 86.624  77.591  45.946  1.00 16.56  ? 43  ILE A N   1 
ATOM   266   C  CA  . ILE A  1 43  ? 85.486  78.470  45.840  1.00 17.55  ? 43  ILE A CA  1 
ATOM   267   C  C   . ILE A  1 43  ? 85.063  78.703  47.265  1.00 23.91  ? 43  ILE A C   1 
ATOM   268   O  O   . ILE A  1 43  ? 84.712  77.747  47.960  1.00 33.96  ? 43  ILE A O   1 
ATOM   269   C  CB  . ILE A  1 43  ? 84.344  77.849  45.146  1.00 13.57  ? 43  ILE A CB  1 
ATOM   270   C  CG1 . ILE A  1 43  ? 84.618  77.718  43.667  1.00 17.74  ? 43  ILE A CG1 1 
ATOM   271   C  CG2 . ILE A  1 43  ? 83.117  78.675  45.364  1.00 16.54  ? 43  ILE A CG2 1 
ATOM   272   C  CD1 . ILE A  1 43  ? 83.540  76.965  42.980  1.00 15.20  ? 43  ILE A CD1 1 
ATOM   273   N  N   . ILE A  1 44  ? 85.116  79.949  47.706  1.00 21.17  ? 44  ILE A N   1 
ATOM   274   C  CA  . ILE A  1 44  ? 84.759  80.289  49.056  1.00 20.06  ? 44  ILE A CA  1 
ATOM   275   C  C   . ILE A  1 44  ? 83.360  80.834  48.981  1.00 22.16  ? 44  ILE A C   1 
ATOM   276   O  O   . ILE A  1 44  ? 83.122  81.728  48.169  1.00 26.07  ? 44  ILE A O   1 
ATOM   277   C  CB  . ILE A  1 44  ? 85.677  81.386  49.571  1.00 17.42  ? 44  ILE A CB  1 
ATOM   278   C  CG1 . ILE A  1 44  ? 87.126  81.091  49.177  1.00 11.73  ? 44  ILE A CG1 1 
ATOM   279   C  CG2 . ILE A  1 44  ? 85.581  81.406  51.067  1.00 17.18  ? 44  ILE A CG2 1 
ATOM   280   C  CD1 . ILE A  1 44  ? 87.692  79.859  49.907  1.00 14.16  ? 44  ILE A CD1 1 
ATOM   281   N  N   . SER A  1 45  ? 82.468  80.373  49.858  1.00 19.47  ? 45  SER A N   1 
ATOM   282   C  CA  . SER A  1 45  ? 81.085  80.827  49.845  1.00 22.60  ? 45  SER A CA  1 
ATOM   283   C  C   . SER A  1 45  ? 80.600  81.100  51.230  1.00 21.20  ? 45  SER A C   1 
ATOM   284   O  O   . SER A  1 45  ? 80.925  80.354  52.142  1.00 26.34  ? 45  SER A O   1 
ATOM   285   C  CB  . SER A  1 45  ? 80.159  79.738  49.294  1.00 25.83  ? 45  SER A CB  1 
ATOM   286   O  OG  . SER A  1 45  ? 80.659  79.133  48.105  1.00 35.91  ? 45  SER A OG  1 
ATOM   287   N  N   . TRP A  1 46  ? 79.808  82.145  51.410  1.00 22.08  ? 46  TRP A N   1 
ATOM   288   C  CA  . TRP A  1 46  ? 79.251  82.396  52.723  1.00 23.08  ? 46  TRP A CA  1 
ATOM   289   C  C   . TRP A  1 46  ? 78.042  83.253  52.596  1.00 22.45  ? 46  TRP A C   1 
ATOM   290   O  O   . TRP A  1 46  ? 77.698  83.714  51.508  1.00 22.78  ? 46  TRP A O   1 
ATOM   291   C  CB  . TRP A  1 46  ? 80.231  83.068  53.658  1.00 24.33  ? 46  TRP A CB  1 
ATOM   292   C  CG  . TRP A  1 46  ? 80.578  84.423  53.212  1.00 23.58  ? 46  TRP A CG  1 
ATOM   293   C  CD1 . TRP A  1 46  ? 80.116  85.592  53.713  1.00 23.02  ? 46  TRP A CD1 1 
ATOM   294   C  CD2 . TRP A  1 46  ? 81.504  84.756  52.192  1.00 20.65  ? 46  TRP A CD2 1 
ATOM   295   N  NE1 . TRP A  1 46  ? 80.704  86.644  53.058  1.00 26.71  ? 46  TRP A NE1 1 
ATOM   296   C  CE2 . TRP A  1 46  ? 81.561  86.150  52.126  1.00 21.41  ? 46  TRP A CE2 1 
ATOM   297   C  CE3 . TRP A  1 46  ? 82.292  84.011  51.338  1.00 23.92  ? 46  TRP A CE3 1 
ATOM   298   C  CZ2 . TRP A  1 46  ? 82.386  86.814  51.226  1.00 22.33  ? 46  TRP A CZ2 1 
ATOM   299   C  CZ3 . TRP A  1 46  ? 83.110  84.677  50.444  1.00 23.44  ? 46  TRP A CZ3 1 
ATOM   300   C  CH2 . TRP A  1 46  ? 83.150  86.062  50.395  1.00 16.40  ? 46  TRP A CH2 1 
ATOM   301   N  N   . VAL A  1 47  ? 77.422  83.500  53.729  1.00 19.74  ? 47  VAL A N   1 
ATOM   302   C  CA  . VAL A  1 47  ? 76.236  84.305  53.781  1.00 20.41  ? 47  VAL A CA  1 
ATOM   303   C  C   . VAL A  1 47  ? 76.310  85.354  54.876  1.00 23.20  ? 47  VAL A C   1 
ATOM   304   O  O   . VAL A  1 47  ? 76.799  85.071  55.968  1.00 28.24  ? 47  VAL A O   1 
ATOM   305   C  CB  . VAL A  1 47  ? 75.079  83.415  54.088  1.00 17.48  ? 47  VAL A CB  1 
ATOM   306   C  CG1 . VAL A  1 47  ? 73.838  84.228  54.212  1.00 10.53  ? 47  VAL A CG1 1 
ATOM   307   C  CG2 . VAL A  1 47  ? 74.967  82.342  53.037  1.00 9.93   ? 47  VAL A CG2 1 
ATOM   308   N  N   . THR A  1 48  ? 75.883  86.572  54.549  1.00 22.99  ? 48  THR A N   1 
ATOM   309   C  CA  . THR A  1 48  ? 75.830  87.706  55.488  1.00 23.19  ? 48  THR A CA  1 
ATOM   310   C  C   . THR A  1 48  ? 74.343  87.997  55.554  1.00 28.69  ? 48  THR A C   1 
ATOM   311   O  O   . THR A  1 48  ? 73.656  88.008  54.518  1.00 31.61  ? 48  THR A O   1 
ATOM   312   C  CB  . THR A  1 48  ? 76.500  88.981  54.952  1.00 19.45  ? 48  THR A CB  1 
ATOM   313   O  OG1 . THR A  1 48  ? 75.985  89.281  53.652  1.00 29.01  ? 48  THR A OG1 1 
ATOM   314   C  CG2 . THR A  1 48  ? 77.995  88.817  54.843  1.00 22.48  ? 48  THR A CG2 1 
ATOM   315   N  N   . MET A  1 49  ? 73.837  88.272  56.745  1.00 30.81  ? 49  MET A N   1 
ATOM   316   C  CA  . MET A  1 49  ? 72.405  88.515  56.898  1.00 31.53  ? 49  MET A CA  1 
ATOM   317   C  C   . MET A  1 49  ? 71.930  89.940  57.208  1.00 32.75  ? 49  MET A C   1 
ATOM   318   O  O   . MET A  1 49  ? 70.760  90.259  57.034  1.00 34.90  ? 49  MET A O   1 
ATOM   319   C  CB  . MET A  1 49  ? 71.847  87.589  57.995  1.00 33.62  ? 49  MET A CB  1 
ATOM   320   C  CG  . MET A  1 49  ? 71.971  86.111  57.739  1.00 41.75  ? 49  MET A CG  1 
ATOM   321   S  SD  . MET A  1 49  ? 70.486  85.414  57.008  1.00 41.02  ? 49  MET A SD  1 
ATOM   322   C  CE  . MET A  1 49  ? 70.186  84.003  58.237  1.00 55.31  ? 49  MET A CE  1 
ATOM   323   N  N   . ASP A  1 50  ? 72.819  90.776  57.727  1.00 34.99  ? 50  ASP A N   1 
ATOM   324   C  CA  . ASP A  1 50  ? 72.440  92.129  58.099  1.00 34.82  ? 50  ASP A CA  1 
ATOM   325   C  C   . ASP A  1 50  ? 72.416  93.059  56.914  1.00 33.62  ? 50  ASP A C   1 
ATOM   326   O  O   . ASP A  1 50  ? 71.496  93.835  56.741  1.00 32.74  ? 50  ASP A O   1 
ATOM   327   C  CB  . ASP A  1 50  ? 73.350  92.616  59.227  1.00 33.94  ? 50  ASP A CB  1 
ATOM   328   C  CG  . ASP A  1 50  ? 73.144  91.812  60.504  1.00 35.52  ? 50  ASP A CG  1 
ATOM   329   O  OD1 . ASP A  1 50  ? 71.975  91.581  60.854  1.00 35.02  ? 50  ASP A OD1 1 
ATOM   330   O  OD2 . ASP A  1 50  ? 74.118  91.364  61.135  1.00 34.79  ? 50  ASP A OD2 1 
ATOM   331   N  N   . GLU A  1 51  ? 73.439  92.986  56.093  1.00 31.65  ? 51  GLU A N   1 
ATOM   332   C  CA  . GLU A  1 51  ? 73.474  93.817  54.930  1.00 27.90  ? 51  GLU A CA  1 
ATOM   333   C  C   . GLU A  1 51  ? 74.426  93.127  54.017  1.00 29.63  ? 51  GLU A C   1 
ATOM   334   O  O   . GLU A  1 51  ? 75.171  92.235  54.441  1.00 30.21  ? 51  GLU A O   1 
ATOM   335   C  CB  . GLU A  1 51  ? 73.924  95.218  55.275  1.00 29.61  ? 51  GLU A CB  1 
ATOM   336   C  CG  . GLU A  1 51  ? 75.114  95.307  56.205  1.00 32.87  ? 51  GLU A CG  1 
ATOM   337   C  CD  . GLU A  1 51  ? 75.794  96.683  56.112  1.00 34.11  ? 51  GLU A CD  1 
ATOM   338   O  OE1 . GLU A  1 51  ? 76.370  96.986  55.027  1.00 33.75  ? 51  GLU A OE1 1 
ATOM   339   O  OE2 . GLU A  1 51  ? 75.735  97.464  57.094  1.00 27.01  ? 51  GLU A OE2 1 
ATOM   340   N  N   . PRO A  1 52  ? 74.319  93.423  52.727  1.00 28.46  ? 52  PRO A N   1 
ATOM   341   C  CA  . PRO A  1 52  ? 75.136  92.862  51.659  1.00 29.48  ? 52  PRO A CA  1 
ATOM   342   C  C   . PRO A  1 52  ? 76.569  92.522  52.018  1.00 32.61  ? 52  PRO A C   1 
ATOM   343   O  O   . PRO A  1 52  ? 76.945  91.351  51.929  1.00 36.84  ? 52  PRO A O   1 
ATOM   344   C  CB  . PRO A  1 52  ? 75.011  93.916  50.573  1.00 24.50  ? 52  PRO A CB  1 
ATOM   345   C  CG  . PRO A  1 52  ? 73.565  94.215  50.685  1.00 18.95  ? 52  PRO A CG  1 
ATOM   346   C  CD  . PRO A  1 52  ? 73.308  94.333  52.171  1.00 25.76  ? 52  PRO A CD  1 
ATOM   347   N  N   . GLY A  1 53  ? 77.370  93.523  52.388  1.00 35.66  ? 53  GLY A N   1 
ATOM   348   C  CA  . GLY A  1 53  ? 78.755  93.268  52.779  1.00 36.84  ? 53  GLY A CA  1 
ATOM   349   C  C   . GLY A  1 53  ? 79.703  93.178  51.602  1.00 35.98  ? 53  GLY A C   1 
ATOM   350   O  O   . GLY A  1 53  ? 79.253  93.416  50.487  1.00 40.39  ? 53  GLY A O   1 
ATOM   351   N  N   . SER A  1 54  ? 80.981  92.836  51.834  1.00 33.86  ? 54  SER A N   1 
ATOM   352   C  CA  . SER A  1 54  ? 81.978  92.718  50.769  1.00 31.09  ? 54  SER A CA  1 
ATOM   353   C  C   . SER A  1 54  ? 82.104  91.261  50.352  1.00 31.43  ? 54  SER A C   1 
ATOM   354   O  O   . SER A  1 54  ? 81.948  90.359  51.191  1.00 38.38  ? 54  SER A O   1 
ATOM   355   C  CB  . SER A  1 54  ? 83.343  93.188  51.271  1.00 30.86  ? 54  SER A CB  1 
ATOM   356   O  OG  . SER A  1 54  ? 84.368  93.072  50.284  1.00 34.21  ? 54  SER A OG  1 
ATOM   357   N  N   . SER A  1 55  ? 82.369  91.018  49.069  1.00 26.91  ? 55  SER A N   1 
ATOM   358   C  CA  . SER A  1 55  ? 82.551  89.655  48.601  1.00 23.99  ? 55  SER A CA  1 
ATOM   359   C  C   . SER A  1 55  ? 84.019  89.429  48.388  1.00 26.56  ? 55  SER A C   1 
ATOM   360   O  O   . SER A  1 55  ? 84.404  88.595  47.584  1.00 30.96  ? 55  SER A O   1 
ATOM   361   C  CB  . SER A  1 55  ? 81.801  89.415  47.316  1.00 21.33  ? 55  SER A CB  1 
ATOM   362   O  OG  . SER A  1 55  ? 80.428  89.683  47.533  1.00 28.97  ? 55  SER A OG  1 
ATOM   363   N  N   . ALA A  1 56  ? 84.849  90.220  49.060  1.00 24.15  ? 56  ALA A N   1 
ATOM   364   C  CA  . ALA A  1 56  ? 86.278  90.052  48.941  1.00 21.61  ? 56  ALA A CA  1 
ATOM   365   C  C   . ALA A  1 56  ? 86.708  89.013  49.939  1.00 24.06  ? 56  ALA A C   1 
ATOM   366   O  O   . ALA A  1 56  ? 86.065  88.847  50.984  1.00 21.95  ? 56  ALA A O   1 
ATOM   367   C  CB  . ALA A  1 56  ? 86.947  91.324  49.268  1.00 26.02  ? 56  ALA A CB  1 
ATOM   368   N  N   . VAL A  1 57  ? 87.794  88.326  49.628  1.00 21.96  ? 57  VAL A N   1 
ATOM   369   C  CA  . VAL A  1 57  ? 88.327  87.329  50.528  1.00 23.55  ? 57  VAL A CA  1 
ATOM   370   C  C   . VAL A  1 57  ? 89.810  87.637  50.675  1.00 25.86  ? 57  VAL A C   1 
ATOM   371   O  O   . VAL A  1 57  ? 90.503  87.951  49.703  1.00 24.23  ? 57  VAL A O   1 
ATOM   372   C  CB  . VAL A  1 57  ? 88.162  85.923  49.972  1.00 21.82  ? 57  VAL A CB  1 
ATOM   373   C  CG1 . VAL A  1 57  ? 88.820  84.932  50.883  1.00 26.66  ? 57  VAL A CG1 1 
ATOM   374   C  CG2 . VAL A  1 57  ? 86.724  85.578  49.871  1.00 26.81  ? 57  VAL A CG2 1 
ATOM   375   N  N   . ARG A  1 58  ? 90.281  87.674  51.902  1.00 27.70  ? 58  ARG A N   1 
ATOM   376   C  CA  . ARG A  1 58  ? 91.671  87.930  52.076  1.00 31.70  ? 58  ARG A CA  1 
ATOM   377   C  C   . ARG A  1 58  ? 92.310  86.614  52.378  1.00 33.65  ? 58  ARG A C   1 
ATOM   378   O  O   . ARG A  1 58  ? 91.809  85.854  53.220  1.00 35.76  ? 58  ARG A O   1 
ATOM   379   C  CB  . ARG A  1 58  ? 91.899  88.894  53.227  1.00 33.89  ? 58  ARG A CB  1 
ATOM   380   C  CG  . ARG A  1 58  ? 93.400  89.132  53.507  1.00 40.24  ? 58  ARG A CG  1 
ATOM   381   C  CD  . ARG A  1 58  ? 93.674  90.453  54.257  1.00 44.58  ? 58  ARG A CD  1 
ATOM   382   N  NE  . ARG A  1 58  ? 92.773  90.636  55.388  1.00 47.83  ? 58  ARG A NE  1 
ATOM   383   C  CZ  . ARG A  1 58  ? 92.047  91.734  55.590  1.00 47.34  ? 58  ARG A CZ  1 
ATOM   384   N  NH1 . ARG A  1 58  ? 92.124  92.761  54.740  1.00 45.56  ? 58  ARG A NH1 1 
ATOM   385   N  NH2 . ARG A  1 58  ? 91.207  91.792  56.624  1.00 48.56  ? 58  ARG A NH2 1 
ATOM   386   N  N   . TYR A  1 59  ? 93.434  86.352  51.743  1.00 31.62  ? 59  TYR A N   1 
ATOM   387   C  CA  . TYR A  1 59  ? 94.111  85.104  52.002  1.00 33.79  ? 59  TYR A CA  1 
ATOM   388   C  C   . TYR A  1 59  ? 95.626  85.218  51.817  1.00 36.80  ? 59  TYR A C   1 
ATOM   389   O  O   . TYR A  1 59  ? 96.126  86.047  51.037  1.00 37.94  ? 59  TYR A O   1 
ATOM   390   C  CB  . TYR A  1 59  ? 93.596  84.063  51.039  1.00 30.45  ? 59  TYR A CB  1 
ATOM   391   C  CG  . TYR A  1 59  ? 94.038  84.321  49.602  1.00 32.09  ? 59  TYR A CG  1 
ATOM   392   C  CD1 . TYR A  1 59  ? 93.370  85.242  48.793  1.00 30.43  ? 59  TYR A CD1 1 
ATOM   393   C  CD2 . TYR A  1 59  ? 95.082  83.592  49.030  1.00 29.85  ? 59  TYR A CD2 1 
ATOM   394   C  CE1 . TYR A  1 59  ? 93.722  85.410  47.437  1.00 27.30  ? 59  TYR A CE1 1 
ATOM   395   C  CE2 . TYR A  1 59  ? 95.440  83.761  47.676  1.00 29.88  ? 59  TYR A CE2 1 
ATOM   396   C  CZ  . TYR A  1 59  ? 94.754  84.661  46.891  1.00 29.14  ? 59  TYR A CZ  1 
ATOM   397   O  OH  . TYR A  1 59  ? 95.070  84.767  45.550  1.00 35.23  ? 59  TYR A OH  1 
ATOM   398   N  N   . TRP A  1 60  ? 96.341  84.306  52.451  1.00 35.73  ? 60  TRP A N   1 
ATOM   399   C  CA  . TRP A  1 60  ? 97.774  84.268  52.358  1.00 35.57  ? 60  TRP A CA  1 
ATOM   400   C  C   . TRP A  1 60  ? 98.208  82.890  52.821  1.00 37.79  ? 60  TRP A C   1 
ATOM   401   O  O   . TRP A  1 60  ? 97.453  82.188  53.526  1.00 36.75  ? 60  TRP A O   1 
ATOM   402   C  CB  . TRP A  1 60  ? 98.355  85.347  53.252  1.00 31.22  ? 60  TRP A CB  1 
ATOM   403   C  CG  . TRP A  1 60  ? 98.061  85.163  54.684  1.00 27.50  ? 60  TRP A CG  1 
ATOM   404   C  CD1 . TRP A  1 60  ? 98.852  84.560  55.603  1.00 27.51  ? 60  TRP A CD1 1 
ATOM   405   C  CD2 . TRP A  1 60  ? 96.874  85.568  55.374  1.00 29.31  ? 60  TRP A CD2 1 
ATOM   406   N  NE1 . TRP A  1 60  ? 98.231  84.555  56.840  1.00 33.21  ? 60  TRP A NE1 1 
ATOM   407   C  CE2 . TRP A  1 60  ? 97.014  85.166  56.729  1.00 25.18  ? 60  TRP A CE2 1 
ATOM   408   C  CE3 . TRP A  1 60  ? 95.699  86.219  54.977  1.00 29.51  ? 60  TRP A CE3 1 
ATOM   409   C  CZ2 . TRP A  1 60  ? 96.027  85.391  57.694  1.00 20.58  ? 60  TRP A CZ2 1 
ATOM   410   C  CZ3 . TRP A  1 60  ? 94.712  86.449  55.938  1.00 26.20  ? 60  TRP A CZ3 1 
ATOM   411   C  CH2 . TRP A  1 60  ? 94.888  86.030  57.288  1.00 24.27  ? 60  TRP A CH2 1 
ATOM   412   N  N   . SER A  1 61  ? 99.400  82.481  52.414  1.00 37.27  ? 61  SER A N   1 
ATOM   413   C  CA  . SER A  1 61  ? 99.874  81.167  52.814  1.00 44.64  ? 61  SER A CA  1 
ATOM   414   C  C   . SER A  1 61  ? 100.675 81.249  54.069  1.00 51.00  ? 61  SER A C   1 
ATOM   415   O  O   . SER A  1 61  ? 101.311 82.243  54.325  1.00 54.50  ? 61  SER A O   1 
ATOM   416   C  CB  . SER A  1 61  ? 100.752 80.579  51.751  1.00 45.00  ? 61  SER A CB  1 
ATOM   417   O  OG  . SER A  1 61  ? 101.922 81.329  51.650  1.00 45.36  ? 61  SER A OG  1 
ATOM   418   N  N   . GLU A  1 62  ? 100.721 80.164  54.811  1.00 62.33  ? 62  GLU A N   1 
ATOM   419   C  CA  . GLU A  1 62  ? 101.460 80.138  56.062  1.00 76.29  ? 62  GLU A CA  1 
ATOM   420   C  C   . GLU A  1 62  ? 102.923 80.590  55.905  1.00 82.35  ? 62  GLU A C   1 
ATOM   421   O  O   . GLU A  1 62  ? 103.465 81.317  56.741  1.00 82.77  ? 62  GLU A O   1 
ATOM   422   C  CB  . GLU A  1 62  ? 101.392 78.730  56.650  1.00 78.44  ? 62  GLU A CB  1 
ATOM   423   C  CG  . GLU A  1 62  ? 101.473 78.688  58.175  1.00 88.47  ? 62  GLU A CG  1 
ATOM   424   C  CD  . GLU A  1 62  ? 101.322 77.276  58.734  1.00 93.19  ? 62  GLU A CD  1 
ATOM   425   O  OE1 . GLU A  1 62  ? 101.912 76.343  58.130  1.00 94.16  ? 62  GLU A OE1 1 
ATOM   426   O  OE2 . GLU A  1 62  ? 100.620 77.106  59.769  1.00 93.55  ? 62  GLU A OE2 1 
ATOM   427   N  N   . LYS A  1 63  ? 103.548 80.159  54.821  1.00 89.30  ? 63  LYS A N   1 
ATOM   428   C  CA  . LYS A  1 63  ? 104.944 80.490  54.535  1.00 96.79  ? 63  LYS A CA  1 
ATOM   429   C  C   . LYS A  1 63  ? 105.169 81.930  54.052  1.00 99.79  ? 63  LYS A C   1 
ATOM   430   O  O   . LYS A  1 63  ? 105.782 82.735  54.748  1.00 100.93 ? 63  LYS A O   1 
ATOM   431   C  CB  . LYS A  1 63  ? 105.490 79.508  53.501  1.00 101.45 ? 63  LYS A CB  1 
ATOM   432   C  CG  . LYS A  1 63  ? 104.438 79.045  52.481  1.00 107.21 ? 63  LYS A CG  1 
ATOM   433   C  CD  . LYS A  1 63  ? 105.049 78.603  51.139  1.00 114.08 ? 63  LYS A CD  1 
ATOM   434   C  CE  . LYS A  1 63  ? 105.477 79.786  50.251  1.00 115.70 ? 63  LYS A CE  1 
ATOM   435   N  NZ  . LYS A  1 63  ? 104.329 80.572  49.719  1.00 116.91 ? 63  LYS A NZ  1 
ATOM   436   N  N   . ASN A  1 64  ? 104.747 82.217  52.820  1.00 101.86 ? 64  ASN A N   1 
ATOM   437   C  CA  . ASN A  1 64  ? 104.862 83.549  52.211  1.00 102.43 ? 64  ASN A CA  1 
ATOM   438   C  C   . ASN A  1 64  ? 103.607 84.334  52.626  1.00 102.02 ? 64  ASN A C   1 
ATOM   439   O  O   . ASN A  1 64  ? 102.578 84.340  51.925  1.00 105.07 ? 64  ASN A O   1 
ATOM   440   C  CB  . ASN A  1 64  ? 104.994 83.423  50.671  1.00 104.89 ? 64  ASN A CB  1 
ATOM   441   C  CG  . ASN A  1 64  ? 104.467 84.648  49.902  1.00 107.68 ? 64  ASN A CG  1 
ATOM   442   O  OD1 . ASN A  1 64  ? 103.552 84.527  49.090  1.00 109.45 ? 64  ASN A OD1 1 
ATOM   443   N  ND2 . ASN A  1 64  ? 105.069 85.812  50.129  1.00 107.91 ? 64  ASN A ND2 1 
ATOM   444   N  N   . GLY A  1 65  ? 103.690 84.955  53.799  1.00 98.06  ? 65  GLY A N   1 
ATOM   445   C  CA  . GLY A  1 65  ? 102.577 85.718  54.333  1.00 93.27  ? 65  GLY A CA  1 
ATOM   446   C  C   . GLY A  1 65  ? 102.024 86.897  53.531  1.00 89.93  ? 65  GLY A C   1 
ATOM   447   O  O   . GLY A  1 65  ? 101.290 87.705  54.114  1.00 89.43  ? 65  GLY A O   1 
ATOM   448   N  N   . ARG A  1 66  ? 102.334 87.006  52.230  1.00 83.34  ? 66  ARG A N   1 
ATOM   449   C  CA  . ARG A  1 66  ? 101.832 88.113  51.413  1.00 77.27  ? 66  ARG A CA  1 
ATOM   450   C  C   . ARG A  1 66  ? 100.328 87.977  51.381  1.00 71.35  ? 66  ARG A C   1 
ATOM   451   O  O   . ARG A  1 66  ? 99.823  86.992  50.847  1.00 71.68  ? 66  ARG A O   1 
ATOM   452   C  CB  . ARG A  1 66  ? 102.388 88.024  49.994  1.00 82.45  ? 66  ARG A CB  1 
ATOM   453   C  CG  . ARG A  1 66  ? 101.719 88.956  48.975  1.00 95.93  ? 66  ARG A CG  1 
ATOM   454   C  CD  . ARG A  1 66  ? 102.062 88.529  47.517  1.00 110.83 ? 66  ARG A CD  1 
ATOM   455   N  NE  . ARG A  1 66  ? 100.923 88.592  46.572  1.00 123.52 ? 66  ARG A NE  1 
ATOM   456   C  CZ  . ARG A  1 66  ? 100.486 87.576  45.806  1.00 127.73 ? 66  ARG A CZ  1 
ATOM   457   N  NH1 . ARG A  1 66  ? 101.075 86.380  45.846  1.00 129.18 ? 66  ARG A NH1 1 
ATOM   458   N  NH2 . ARG A  1 66  ? 99.416  87.738  45.024  1.00 129.12 ? 66  ARG A NH2 1 
ATOM   459   N  N   . LYS A  1 67  ? 99.618  88.914  52.012  1.00 63.99  ? 67  LYS A N   1 
ATOM   460   C  CA  . LYS A  1 67  ? 98.161  88.850  52.056  1.00 58.09  ? 67  LYS A CA  1 
ATOM   461   C  C   . LYS A  1 67  ? 97.611  89.349  50.748  1.00 56.52  ? 67  LYS A C   1 
ATOM   462   O  O   . LYS A  1 67  ? 98.004  90.418  50.298  1.00 62.32  ? 67  LYS A O   1 
ATOM   463   C  CB  . LYS A  1 67  ? 97.608  89.660  53.224  1.00 55.89  ? 67  LYS A CB  1 
ATOM   464   C  CG  . LYS A  1 67  ? 98.055  89.134  54.593  1.00 60.72  ? 67  LYS A CG  1 
ATOM   465   C  CD  . LYS A  1 67  ? 97.378  89.853  55.774  1.00 66.21  ? 67  LYS A CD  1 
ATOM   466   C  CE  . LYS A  1 67  ? 97.732  89.218  57.142  1.00 72.11  ? 67  LYS A CE  1 
ATOM   467   N  NZ  . LYS A  1 67  ? 96.819  89.690  58.281  1.00 76.77  ? 67  LYS A NZ  1 
ATOM   468   N  N   . ARG A  1 68  ? 96.792  88.528  50.086  1.00 52.99  ? 68  ARG A N   1 
ATOM   469   C  CA  . ARG A  1 68  ? 96.181  88.887  48.806  1.00 47.62  ? 68  ARG A CA  1 
ATOM   470   C  C   . ARG A  1 68  ? 94.664  88.923  48.958  1.00 42.58  ? 68  ARG A C   1 
ATOM   471   O  O   . ARG A  1 68  ? 94.098  88.354  49.903  1.00 41.13  ? 68  ARG A O   1 
ATOM   472   C  CB  . ARG A  1 68  ? 96.572  87.880  47.743  1.00 52.04  ? 68  ARG A CB  1 
ATOM   473   C  CG  . ARG A  1 68  ? 98.040  87.547  47.748  1.00 65.08  ? 68  ARG A CG  1 
ATOM   474   C  CD  . ARG A  1 68  ? 98.337  86.027  47.668  1.00 78.79  ? 68  ARG A CD  1 
ATOM   475   N  NE  . ARG A  1 68  ? 98.891  85.484  48.926  1.00 93.89  ? 68  ARG A NE  1 
ATOM   476   C  CZ  . ARG A  1 68  ? 99.664  84.392  49.036  1.00 100.04 ? 68  ARG A CZ  1 
ATOM   477   N  NH1 . ARG A  1 68  ? 100.002 83.674  47.951  1.00 102.90 ? 68  ARG A NH1 1 
ATOM   478   N  NH2 . ARG A  1 68  ? 100.118 84.032  50.242  1.00 96.84  ? 68  ARG A NH2 1 
ATOM   479   N  N   . ILE A  1 69  ? 94.005  89.587  48.020  1.00 37.68  ? 69  ILE A N   1 
ATOM   480   C  CA  . ILE A  1 69  ? 92.557  89.718  48.047  1.00 36.41  ? 69  ILE A CA  1 
ATOM   481   C  C   . ILE A  1 69  ? 91.885  89.264  46.773  1.00 39.34  ? 69  ILE A C   1 
ATOM   482   O  O   . ILE A  1 69  ? 92.275  89.678  45.674  1.00 38.01  ? 69  ILE A O   1 
ATOM   483   C  CB  . ILE A  1 69  ? 92.177  91.152  48.271  1.00 36.69  ? 69  ILE A CB  1 
ATOM   484   C  CG1 . ILE A  1 69  ? 91.984  91.365  49.756  1.00 40.19  ? 69  ILE A CG1 1 
ATOM   485   C  CG2 . ILE A  1 69  ? 90.900  91.524  47.550  1.00 39.30  ? 69  ILE A CG2 1 
ATOM   486   C  CD1 . ILE A  1 69  ? 91.550  92.794  50.112  1.00 38.66  ? 69  ILE A CD1 1 
ATOM   487   N  N   . ALA A  1 70  ? 90.828  88.471  46.918  1.00 38.85  ? 70  ALA A N   1 
ATOM   488   C  CA  . ALA A  1 70  ? 90.094  87.981  45.761  1.00 37.38  ? 70  ALA A CA  1 
ATOM   489   C  C   . ALA A  1 70  ? 88.743  88.599  45.854  1.00 38.11  ? 70  ALA A C   1 
ATOM   490   O  O   . ALA A  1 70  ? 88.215  88.748  46.957  1.00 39.20  ? 70  ALA A O   1 
ATOM   491   C  CB  . ALA A  1 70  ? 89.969  86.490  45.804  1.00 43.15  ? 70  ALA A CB  1 
ATOM   492   N  N   . LYS A  1 71  ? 88.171  88.945  44.711  1.00 39.04  ? 71  LYS A N   1 
ATOM   493   C  CA  . LYS A  1 71  ? 86.857  89.551  44.715  1.00 41.60  ? 71  LYS A CA  1 
ATOM   494   C  C   . LYS A  1 71  ? 85.826  88.636  44.076  1.00 36.37  ? 71  LYS A C   1 
ATOM   495   O  O   . LYS A  1 71  ? 86.005  88.191  42.962  1.00 40.30  ? 71  LYS A O   1 
ATOM   496   C  CB  . LYS A  1 71  ? 86.915  90.920  44.019  1.00 50.48  ? 71  LYS A CB  1 
ATOM   497   C  CG  . LYS A  1 71  ? 86.394  92.122  44.892  1.00 65.81  ? 71  LYS A CG  1 
ATOM   498   C  CD  . LYS A  1 71  ? 84.844  92.025  45.297  1.00 74.52  ? 71  LYS A CD  1 
ATOM   499   C  CE  . LYS A  1 71  ? 84.327  93.168  46.283  1.00 78.85  ? 71  LYS A CE  1 
ATOM   500   N  NZ  . LYS A  1 71  ? 82.849  93.101  46.686  1.00 78.52  ? 71  LYS A NZ  1 
ATOM   501   N  N   . GLY A  1 72  ? 84.770  88.318  44.806  1.00 33.03  ? 72  GLY A N   1 
ATOM   502   C  CA  . GLY A  1 72  ? 83.740  87.437  44.273  1.00 29.17  ? 72  GLY A CA  1 
ATOM   503   C  C   . GLY A  1 72  ? 82.454  88.149  43.887  1.00 32.69  ? 72  GLY A C   1 
ATOM   504   O  O   . GLY A  1 72  ? 82.525  89.298  43.481  1.00 30.97  ? 72  GLY A O   1 
ATOM   505   N  N   . LYS A  1 73  ? 81.299  87.469  43.969  1.00 34.52  ? 73  LYS A N   1 
ATOM   506   C  CA  . LYS A  1 73  ? 79.993  88.039  43.624  1.00 35.95  ? 73  LYS A CA  1 
ATOM   507   C  C   . LYS A  1 73  ? 78.929  87.755  44.675  1.00 36.58  ? 73  LYS A C   1 
ATOM   508   O  O   . LYS A  1 73  ? 79.028  86.790  45.435  1.00 43.73  ? 73  LYS A O   1 
ATOM   509   C  CB  . LYS A  1 73  ? 79.472  87.466  42.322  1.00 45.59  ? 73  LYS A CB  1 
ATOM   510   C  CG  . LYS A  1 73  ? 80.242  87.785  41.047  1.00 63.90  ? 73  LYS A CG  1 
ATOM   511   C  CD  . LYS A  1 73  ? 79.418  87.291  39.823  1.00 78.83  ? 73  LYS A CD  1 
ATOM   512   C  CE  . LYS A  1 73  ? 80.190  87.260  38.471  1.00 85.70  ? 73  LYS A CE  1 
ATOM   513   N  NZ  . LYS A  1 73  ? 79.380  86.758  37.287  1.00 91.43  ? 73  LYS A NZ  1 
ATOM   514   N  N   . MET A  1 74  ? 77.848  88.523  44.650  1.00 32.04  ? 74  MET A N   1 
ATOM   515   C  CA  . MET A  1 74  ? 76.801  88.328  45.628  1.00 29.15  ? 74  MET A CA  1 
ATOM   516   C  C   . MET A  1 74  ? 75.473  88.040  44.965  1.00 31.50  ? 74  MET A C   1 
ATOM   517   O  O   . MET A  1 74  ? 75.193  88.556  43.881  1.00 34.50  ? 74  MET A O   1 
ATOM   518   C  CB  . MET A  1 74  ? 76.669  89.574  46.489  1.00 28.15  ? 74  MET A CB  1 
ATOM   519   C  CG  . MET A  1 74  ? 75.687  89.405  47.629  1.00 33.49  ? 74  MET A CG  1 
ATOM   520   S  SD  . MET A  1 74  ? 74.392  90.634  47.703  1.00 36.54  ? 74  MET A SD  1 
ATOM   521   C  CE  . MET A  1 74  ? 73.271  90.014  46.685  1.00 39.58  ? 74  MET A CE  1 
ATOM   522   N  N   . SER A  1 75  ? 74.623  87.258  45.624  1.00 28.36  ? 75  SER A N   1 
ATOM   523   C  CA  . SER A  1 75  ? 73.326  86.944  45.062  1.00 24.66  ? 75  SER A CA  1 
ATOM   524   C  C   . SER A  1 75  ? 72.324  86.723  46.161  1.00 25.52  ? 75  SER A C   1 
ATOM   525   O  O   . SER A  1 75  ? 72.701  86.557  47.319  1.00 26.97  ? 75  SER A O   1 
ATOM   526   C  CB  . SER A  1 75  ? 73.422  85.724  44.147  1.00 28.78  ? 75  SER A CB  1 
ATOM   527   O  OG  . SER A  1 75  ? 74.458  84.807  44.512  1.00 36.79  ? 75  SER A OG  1 
ATOM   528   N  N   . THR A  1 76  ? 71.049  86.727  45.794  1.00 21.28  ? 76  THR A N   1 
ATOM   529   C  CA  . THR A  1 76  ? 69.955  86.519  46.721  1.00 18.83  ? 76  THR A CA  1 
ATOM   530   C  C   . THR A  1 76  ? 68.857  85.828  45.946  1.00 19.26  ? 76  THR A C   1 
ATOM   531   O  O   . THR A  1 76  ? 68.849  85.853  44.712  1.00 27.59  ? 76  THR A O   1 
ATOM   532   C  CB  . THR A  1 76  ? 69.413  87.809  47.197  1.00 24.87  ? 76  THR A CB  1 
ATOM   533   O  OG1 . THR A  1 76  ? 69.073  88.615  46.072  1.00 38.00  ? 76  THR A OG1 1 
ATOM   534   C  CG2 . THR A  1 76  ? 70.427  88.545  48.009  1.00 30.43  ? 76  THR A CG2 1 
ATOM   535   N  N   . TYR A  1 77  ? 67.978  85.111  46.625  1.00 15.38  ? 77  TYR A N   1 
ATOM   536   C  CA  . TYR A  1 77  ? 66.896  84.441  45.938  1.00 17.04  ? 77  TYR A CA  1 
ATOM   537   C  C   . TYR A  1 77  ? 65.746  84.439  46.909  1.00 20.68  ? 77  TYR A C   1 
ATOM   538   O  O   . TYR A  1 77  ? 65.947  84.701  48.102  1.00 22.95  ? 77  TYR A O   1 
ATOM   539   C  CB  . TYR A  1 77  ? 67.288  83.018  45.543  1.00 11.31  ? 77  TYR A CB  1 
ATOM   540   C  CG  . TYR A  1 77  ? 67.309  82.029  46.684  1.00 9.63   ? 77  TYR A CG  1 
ATOM   541   C  CD1 . TYR A  1 77  ? 66.163  81.325  47.058  1.00 6.12   ? 77  TYR A CD1 1 
ATOM   542   C  CD2 . TYR A  1 77  ? 68.471  81.832  47.417  1.00 8.33   ? 77  TYR A CD2 1 
ATOM   543   C  CE1 . TYR A  1 77  ? 66.166  80.440  48.151  1.00 7.48   ? 77  TYR A CE1 1 
ATOM   544   C  CE2 . TYR A  1 77  ? 68.485  80.956  48.493  1.00 17.06  ? 77  TYR A CE2 1 
ATOM   545   C  CZ  . TYR A  1 77  ? 67.327  80.256  48.865  1.00 14.02  ? 77  TYR A CZ  1 
ATOM   546   O  OH  . TYR A  1 77  ? 67.384  79.438  49.975  1.00 12.54  ? 77  TYR A OH  1 
ATOM   547   N  N   . ARG A  1 78  ? 64.533  84.266  46.383  1.00 22.72  ? 78  ARG A N   1 
ATOM   548   C  CA  . ARG A  1 78  ? 63.322  84.208  47.226  1.00 26.23  ? 78  ARG A CA  1 
ATOM   549   C  C   . ARG A  1 78  ? 62.708  82.864  46.929  1.00 24.28  ? 78  ARG A C   1 
ATOM   550   O  O   . ARG A  1 78  ? 62.721  82.430  45.787  1.00 24.51  ? 78  ARG A O   1 
ATOM   551   C  CB  . ARG A  1 78  ? 62.272  85.281  46.867  1.00 30.61  ? 78  ARG A CB  1 
ATOM   552   C  CG  . ARG A  1 78  ? 62.612  86.728  47.231  1.00 36.35  ? 78  ARG A CG  1 
ATOM   553   C  CD  . ARG A  1 78  ? 61.465  87.668  46.872  1.00 33.36  ? 78  ARG A CD  1 
ATOM   554   N  NE  . ARG A  1 78  ? 60.877  88.334  48.036  1.00 36.48  ? 78  ARG A NE  1 
ATOM   555   C  CZ  . ARG A  1 78  ? 60.919  89.650  48.242  1.00 30.28  ? 78  ARG A CZ  1 
ATOM   556   N  NH1 . ARG A  1 78  ? 61.521  90.463  47.399  1.00 36.97  ? 78  ARG A NH1 1 
ATOM   557   N  NH2 . ARG A  1 78  ? 60.297  90.172  49.262  1.00 29.33  ? 78  ARG A NH2 1 
ATOM   558   N  N   . PHE A  1 79  ? 62.272  82.166  47.962  1.00 25.14  ? 79  PHE A N   1 
ATOM   559   C  CA  . PHE A  1 79  ? 61.684  80.904  47.710  1.00 25.25  ? 79  PHE A CA  1 
ATOM   560   C  C   . PHE A  1 79  ? 60.202  81.049  47.733  1.00 29.81  ? 79  PHE A C   1 
ATOM   561   O  O   . PHE A  1 79  ? 59.613  81.125  46.685  1.00 42.08  ? 79  PHE A O   1 
ATOM   562   C  CB  . PHE A  1 79  ? 62.156  79.807  48.618  1.00 21.98  ? 79  PHE A CB  1 
ATOM   563   C  CG  . PHE A  1 79  ? 61.728  78.469  48.139  1.00 18.64  ? 79  PHE A CG  1 
ATOM   564   C  CD1 . PHE A  1 79  ? 62.216  77.976  46.956  1.00 11.90  ? 79  PHE A CD1 1 
ATOM   565   C  CD2 . PHE A  1 79  ? 60.753  77.735  48.816  1.00 21.27  ? 79  PHE A CD2 1 
ATOM   566   C  CE1 . PHE A  1 79  ? 61.733  76.778  46.461  1.00 13.27  ? 79  PHE A CE1 1 
ATOM   567   C  CE2 . PHE A  1 79  ? 60.263  76.527  48.313  1.00 7.52   ? 79  PHE A CE2 1 
ATOM   568   C  CZ  . PHE A  1 79  ? 60.754  76.053  47.137  1.00 8.99   ? 79  PHE A CZ  1 
ATOM   569   N  N   . PHE A  1 80  ? 59.520  81.086  48.851  1.00 23.82  ? 80  PHE A N   1 
ATOM   570   C  CA  . PHE A  1 80  ? 58.077  81.252  48.625  1.00 23.67  ? 80  PHE A CA  1 
ATOM   571   C  C   . PHE A  1 80  ? 57.815  82.520  49.374  1.00 27.89  ? 80  PHE A C   1 
ATOM   572   O  O   . PHE A  1 80  ? 57.923  83.586  48.792  1.00 32.02  ? 80  PHE A O   1 
ATOM   573   C  CB  . PHE A  1 80  ? 57.346  80.021  49.133  1.00 25.43  ? 80  PHE A CB  1 
ATOM   574   C  CG  . PHE A  1 80  ? 55.895  80.205  49.360  1.00 25.66  ? 80  PHE A CG  1 
ATOM   575   C  CD1 . PHE A  1 80  ? 55.045  80.464  48.312  1.00 34.06  ? 80  PHE A CD1 1 
ATOM   576   C  CD2 . PHE A  1 80  ? 55.358  80.066  50.634  1.00 24.91  ? 80  PHE A CD2 1 
ATOM   577   C  CE1 . PHE A  1 80  ? 53.646  80.579  48.531  1.00 28.57  ? 80  PHE A CE1 1 
ATOM   578   C  CE2 . PHE A  1 80  ? 53.978  80.180  50.866  1.00 23.63  ? 80  PHE A CE2 1 
ATOM   579   C  CZ  . PHE A  1 80  ? 53.126  80.436  49.816  1.00 28.24  ? 80  PHE A CZ  1 
ATOM   580   N  N   . ASN A  1 81  ? 57.564  82.439  50.678  1.00 28.77  ? 81  ASN A N   1 
ATOM   581   C  CA  . ASN A  1 81  ? 57.422  83.645  51.443  1.00 22.35  ? 81  ASN A CA  1 
ATOM   582   C  C   . ASN A  1 81  ? 58.783  83.856  52.103  1.00 22.68  ? 81  ASN A C   1 
ATOM   583   O  O   . ASN A  1 81  ? 58.882  84.737  52.959  1.00 28.42  ? 81  ASN A O   1 
ATOM   584   C  CB  . ASN A  1 81  ? 56.222  83.631  52.428  1.00 23.63  ? 81  ASN A CB  1 
ATOM   585   C  CG  . ASN A  1 81  ? 56.263  82.507  53.476  1.00 30.44  ? 81  ASN A CG  1 
ATOM   586   O  OD1 . ASN A  1 81  ? 57.059  81.586  53.391  1.00 31.12  ? 81  ASN A OD1 1 
ATOM   587   N  ND2 . ASN A  1 81  ? 55.368  82.629  54.469  1.00 44.95  ? 81  ASN A ND2 1 
ATOM   588   N  N   . TYR A  1 82  ? 59.822  83.106  51.640  1.00 17.44  ? 82  TYR A N   1 
ATOM   589   C  CA  . TYR A  1 82  ? 61.221  83.180  52.147  1.00 17.99  ? 82  TYR A CA  1 
ATOM   590   C  C   . TYR A  1 82  ? 62.070  84.145  51.318  1.00 20.55  ? 82  TYR A C   1 
ATOM   591   O  O   . TYR A  1 82  ? 61.773  84.342  50.157  1.00 29.76  ? 82  TYR A O   1 
ATOM   592   C  CB  . TYR A  1 82  ? 61.908  81.796  52.080  1.00 20.56  ? 82  TYR A CB  1 
ATOM   593   C  CG  . TYR A  1 82  ? 63.449  81.743  52.453  1.00 18.16  ? 82  TYR A CG  1 
ATOM   594   C  CD1 . TYR A  1 82  ? 63.855  81.717  53.764  1.00 14.82  ? 82  TYR A CD1 1 
ATOM   595   C  CD2 . TYR A  1 82  ? 64.459  81.752  51.492  1.00 20.50  ? 82  TYR A CD2 1 
ATOM   596   C  CE1 . TYR A  1 82  ? 65.225  81.717  54.128  1.00 14.71  ? 82  TYR A CE1 1 
ATOM   597   C  CE2 . TYR A  1 82  ? 65.836  81.747  51.866  1.00 17.36  ? 82  TYR A CE2 1 
ATOM   598   C  CZ  . TYR A  1 82  ? 66.197  81.735  53.202  1.00 15.62  ? 82  TYR A CZ  1 
ATOM   599   O  OH  . TYR A  1 82  ? 67.509  81.723  53.703  1.00 20.58  ? 82  TYR A OH  1 
ATOM   600   N  N   . SER A  1 83  ? 63.111  84.731  51.918  1.00 20.90  ? 83  SER A N   1 
ATOM   601   C  CA  . SER A  1 83  ? 64.064  85.674  51.256  1.00 26.89  ? 83  SER A CA  1 
ATOM   602   C  C   . SER A  1 83  ? 65.493  85.441  51.771  1.00 26.00  ? 83  SER A C   1 
ATOM   603   O  O   . SER A  1 83  ? 65.780  85.696  52.951  1.00 31.57  ? 83  SER A O   1 
ATOM   604   C  CB  . SER A  1 83  ? 63.712  87.114  51.565  1.00 30.25  ? 83  SER A CB  1 
ATOM   605   O  OG  . SER A  1 83  ? 62.364  87.379  51.245  1.00 44.48  ? 83  SER A OG  1 
ATOM   606   N  N   . SER A  1 84  ? 66.395  85.021  50.897  1.00 19.56  ? 84  SER A N   1 
ATOM   607   C  CA  . SER A  1 84  ? 67.724  84.722  51.325  1.00 17.41  ? 84  SER A CA  1 
ATOM   608   C  C   . SER A  1 84  ? 68.429  85.919  51.899  1.00 19.42  ? 84  SER A C   1 
ATOM   609   O  O   . SER A  1 84  ? 67.986  87.035  51.782  1.00 20.29  ? 84  SER A O   1 
ATOM   610   C  CB  . SER A  1 84  ? 68.514  84.300  50.136  1.00 13.77  ? 84  SER A CB  1 
ATOM   611   O  OG  . SER A  1 84  ? 68.610  85.400  49.285  1.00 17.83  ? 84  SER A OG  1 
ATOM   612   N  N   . GLY A  1 85  ? 69.532  85.666  52.570  1.00 18.45  ? 85  GLY A N   1 
ATOM   613   C  CA  . GLY A  1 85  ? 70.334  86.758  53.045  1.00 13.91  ? 85  GLY A CA  1 
ATOM   614   C  C   . GLY A  1 85  ? 71.219  87.012  51.836  1.00 15.90  ? 85  GLY A C   1 
ATOM   615   O  O   . GLY A  1 85  ? 70.833  86.623  50.734  1.00 20.73  ? 85  GLY A O   1 
ATOM   616   N  N   . PHE A  1 86  ? 72.425  87.524  52.013  1.00 15.15  ? 86  PHE A N   1 
ATOM   617   C  CA  . PHE A  1 86  ? 73.251  87.796  50.863  1.00 15.67  ? 86  PHE A CA  1 
ATOM   618   C  C   . PHE A  1 86  ? 74.299  86.730  50.672  1.00 17.93  ? 86  PHE A C   1 
ATOM   619   O  O   . PHE A  1 86  ? 75.236  86.582  51.476  1.00 21.02  ? 86  PHE A O   1 
ATOM   620   C  CB  . PHE A  1 86  ? 73.836  89.196  50.998  1.00 22.20  ? 86  PHE A CB  1 
ATOM   621   C  CG  . PHE A  1 86  ? 72.806  90.217  51.382  1.00 23.95  ? 86  PHE A CG  1 
ATOM   622   C  CD1 . PHE A  1 86  ? 71.986  90.785  50.415  1.00 28.70  ? 86  PHE A CD1 1 
ATOM   623   C  CD2 . PHE A  1 86  ? 72.538  90.501  52.710  1.00 23.48  ? 86  PHE A CD2 1 
ATOM   624   C  CE1 . PHE A  1 86  ? 70.896  91.609  50.772  1.00 22.58  ? 86  PHE A CE1 1 
ATOM   625   C  CE2 . PHE A  1 86  ? 71.452  91.322  53.070  1.00 20.74  ? 86  PHE A CE2 1 
ATOM   626   C  CZ  . PHE A  1 86  ? 70.638  91.863  52.099  1.00 21.37  ? 86  PHE A CZ  1 
ATOM   627   N  N   . ILE A  1 87  ? 74.120  85.963  49.608  1.00 13.46  ? 87  ILE A N   1 
ATOM   628   C  CA  . ILE A  1 87  ? 75.014  84.872  49.337  1.00 14.75  ? 87  ILE A CA  1 
ATOM   629   C  C   . ILE A  1 87  ? 76.224  85.310  48.597  1.00 18.95  ? 87  ILE A C   1 
ATOM   630   O  O   . ILE A  1 87  ? 76.115  85.979  47.582  1.00 22.75  ? 87  ILE A O   1 
ATOM   631   C  CB  . ILE A  1 87  ? 74.280  83.809  48.563  1.00 15.24  ? 87  ILE A CB  1 
ATOM   632   C  CG1 . ILE A  1 87  ? 73.014  83.423  49.335  1.00 8.88   ? 87  ILE A CG1 1 
ATOM   633   C  CG2 . ILE A  1 87  ? 75.138  82.559  48.446  1.00 11.57  ? 87  ILE A CG2 1 
ATOM   634   C  CD1 . ILE A  1 87  ? 72.088  82.524  48.555  1.00 21.90  ? 87  ILE A CD1 1 
ATOM   635   N  N   . HIS A  1 88  ? 77.390  84.876  49.047  1.00 21.62  ? 88  HIS A N   1 
ATOM   636   C  CA  . HIS A  1 88  ? 78.629  85.299  48.387  1.00 19.16  ? 88  HIS A CA  1 
ATOM   637   C  C   . HIS A  1 88  ? 79.425  84.106  47.898  1.00 22.93  ? 88  HIS A C   1 
ATOM   638   O  O   . HIS A  1 88  ? 79.566  83.098  48.629  1.00 21.96  ? 88  HIS A O   1 
ATOM   639   C  CB  . HIS A  1 88  ? 79.526  86.043  49.352  1.00 18.40  ? 88  HIS A CB  1 
ATOM   640   C  CG  . HIS A  1 88  ? 78.898  87.290  49.911  1.00 15.04  ? 88  HIS A CG  1 
ATOM   641   N  ND1 . HIS A  1 88  ? 78.164  87.281  51.076  1.00 17.44  ? 88  HIS A ND1 1 
ATOM   642   C  CD2 . HIS A  1 88  ? 78.945  88.560  49.501  1.00 12.11  ? 88  HIS A CD2 1 
ATOM   643   C  CE1 . HIS A  1 88  ? 77.793  88.501  51.364  1.00 13.05  ? 88  HIS A CE1 1 
ATOM   644   N  NE2 . HIS A  1 88  ? 78.256  89.298  50.412  1.00 19.12  ? 88  HIS A NE2 1 
ATOM   645   N  N   . HIS A  1 89  ? 80.030  84.262  46.715  1.00 20.05  ? 89  HIS A N   1 
ATOM   646   C  CA  . HIS A  1 89  ? 80.828  83.211  46.087  1.00 19.72  ? 89  HIS A CA  1 
ATOM   647   C  C   . HIS A  1 89  ? 82.067  83.842  45.456  1.00 18.56  ? 89  HIS A C   1 
ATOM   648   O  O   . HIS A  1 89  ? 81.975  84.593  44.498  1.00 20.09  ? 89  HIS A O   1 
ATOM   649   C  CB  . HIS A  1 89  ? 80.013  82.447  45.009  1.00 18.10  ? 89  HIS A CB  1 
ATOM   650   C  CG  . HIS A  1 89  ? 78.849  81.634  45.534  1.00 22.84  ? 89  HIS A CG  1 
ATOM   651   N  ND1 . HIS A  1 89  ? 79.000  80.490  46.301  1.00 24.64  ? 89  HIS A ND1 1 
ATOM   652   C  CD2 . HIS A  1 89  ? 77.509  81.798  45.387  1.00 21.65  ? 89  HIS A CD2 1 
ATOM   653   C  CE1 . HIS A  1 89  ? 77.805  80.002  46.603  1.00 24.42  ? 89  HIS A CE1 1 
ATOM   654   N  NE2 . HIS A  1 89  ? 76.883  80.780  46.062  1.00 12.24  ? 89  HIS A NE2 1 
ATOM   655   N  N   . THR A  1 90  ? 83.230  83.514  45.995  1.00 17.72  ? 90  THR A N   1 
ATOM   656   C  CA  . THR A  1 90  ? 84.477  84.067  45.513  1.00 21.74  ? 90  THR A CA  1 
ATOM   657   C  C   . THR A  1 90  ? 85.426  82.929  45.241  1.00 26.13  ? 90  THR A C   1 
ATOM   658   O  O   . THR A  1 90  ? 85.619  82.035  46.091  1.00 27.75  ? 90  THR A O   1 
ATOM   659   C  CB  . THR A  1 90  ? 85.131  84.965  46.568  1.00 19.27  ? 90  THR A CB  1 
ATOM   660   O  OG1 . THR A  1 90  ? 84.243  86.029  46.907  1.00 26.63  ? 90  THR A OG1 1 
ATOM   661   C  CG2 . THR A  1 90  ? 86.401  85.555  46.060  1.00 8.11   ? 90  THR A CG2 1 
ATOM   662   N  N   . THR A  1 91  ? 86.123  83.031  44.120  1.00 21.20  ? 91  THR A N   1 
ATOM   663   C  CA  . THR A  1 91  ? 87.018  81.984  43.727  1.00 21.69  ? 91  THR A CA  1 
ATOM   664   C  C   . THR A  1 91  ? 88.445  82.432  43.865  1.00 20.36  ? 91  THR A C   1 
ATOM   665   O  O   . THR A  1 91  ? 88.840  83.438  43.350  1.00 29.78  ? 91  THR A O   1 
ATOM   666   C  CB  . THR A  1 91  ? 86.731  81.620  42.259  1.00 23.86  ? 91  THR A CB  1 
ATOM   667   O  OG1 . THR A  1 91  ? 85.325  81.369  42.082  1.00 34.76  ? 91  THR A OG1 1 
ATOM   668   C  CG2 . THR A  1 91  ? 87.493  80.399  41.846  1.00 17.83  ? 91  THR A CG2 1 
ATOM   669   N  N   . ILE A  1 92  ? 89.227  81.690  44.585  1.00 18.73  ? 92  ILE A N   1 
ATOM   670   C  CA  . ILE A  1 92  ? 90.600  82.038  44.736  1.00 22.98  ? 92  ILE A CA  1 
ATOM   671   C  C   . ILE A  1 92  ? 91.386  81.198  43.767  1.00 25.73  ? 92  ILE A C   1 
ATOM   672   O  O   . ILE A  1 92  ? 91.273  79.992  43.787  1.00 32.20  ? 92  ILE A O   1 
ATOM   673   C  CB  . ILE A  1 92  ? 91.039  81.670  46.085  1.00 24.22  ? 92  ILE A CB  1 
ATOM   674   C  CG1 . ILE A  1 92  ? 90.232  82.430  47.110  1.00 23.28  ? 92  ILE A CG1 1 
ATOM   675   C  CG2 . ILE A  1 92  ? 92.474  82.044  46.262  1.00 37.64  ? 92  ILE A CG2 1 
ATOM   676   C  CD1 . ILE A  1 92  ? 90.706  82.099  48.458  1.00 27.90  ? 92  ILE A CD1 1 
ATOM   677   N  N   . ARG A  1 93  ? 92.229  81.802  42.949  1.00 34.57  ? 93  ARG A N   1 
ATOM   678   C  CA  . ARG A  1 93  ? 92.981  81.019  41.964  1.00 37.96  ? 93  ARG A CA  1 
ATOM   679   C  C   . ARG A  1 93  ? 94.476  80.977  42.122  1.00 40.27  ? 93  ARG A C   1 
ATOM   680   O  O   . ARG A  1 93  ? 95.069  81.734  42.889  1.00 44.73  ? 93  ARG A O   1 
ATOM   681   C  CB  . ARG A  1 93  ? 92.715  81.531  40.567  1.00 44.71  ? 93  ARG A CB  1 
ATOM   682   C  CG  . ARG A  1 93  ? 91.334  81.305  40.111  1.00 60.14  ? 93  ARG A CG  1 
ATOM   683   C  CD  . ARG A  1 93  ? 90.915  82.302  39.049  1.00 72.38  ? 93  ARG A CD  1 
ATOM   684   N  NE  . ARG A  1 93  ? 89.531  82.040  38.664  1.00 85.37  ? 93  ARG A NE  1 
ATOM   685   C  CZ  . ARG A  1 93  ? 89.110  80.897  38.110  1.00 93.57  ? 93  ARG A CZ  1 
ATOM   686   N  NH1 . ARG A  1 93  ? 89.972  79.896  37.850  1.00 96.81  ? 93  ARG A NH1 1 
ATOM   687   N  NH2 . ARG A  1 93  ? 87.807  80.723  37.882  1.00 94.69  ? 93  ARG A NH2 1 
ATOM   688   N  N   . LYS A  1 94  ? 95.082  80.112  41.326  1.00 41.98  ? 94  LYS A N   1 
ATOM   689   C  CA  . LYS A  1 94  ? 96.517  79.941  41.313  1.00 44.56  ? 94  LYS A CA  1 
ATOM   690   C  C   . LYS A  1 94  ? 97.171  79.711  42.681  1.00 44.17  ? 94  LYS A C   1 
ATOM   691   O  O   . LYS A  1 94  ? 98.112  80.393  43.049  1.00 48.40  ? 94  LYS A O   1 
ATOM   692   C  CB  . LYS A  1 94  ? 97.158  81.111  40.576  1.00 48.27  ? 94  LYS A CB  1 
ATOM   693   C  CG  . LYS A  1 94  ? 96.689  81.256  39.108  1.00 60.87  ? 94  LYS A CG  1 
ATOM   694   C  CD  . LYS A  1 94  ? 97.347  82.443  38.352  1.00 71.22  ? 94  LYS A CD  1 
ATOM   695   C  CE  . LYS A  1 94  ? 96.356  83.592  37.961  1.00 83.72  ? 94  LYS A CE  1 
ATOM   696   N  NZ  . LYS A  1 94  ? 95.301  83.294  36.906  1.00 93.49  ? 94  LYS A NZ  1 
ATOM   697   N  N   . LEU A  1 95  ? 96.657  78.764  43.453  1.00 43.30  ? 95  LEU A N   1 
ATOM   698   C  CA  . LEU A  1 95  ? 97.245  78.448  44.746  1.00 42.67  ? 95  LEU A CA  1 
ATOM   699   C  C   . LEU A  1 95  ? 98.460  77.531  44.528  1.00 46.10  ? 95  LEU A C   1 
ATOM   700   O  O   . LEU A  1 95  ? 98.648  76.966  43.449  1.00 48.26  ? 95  LEU A O   1 
ATOM   701   C  CB  . LEU A  1 95  ? 96.227  77.712  45.608  1.00 38.60  ? 95  LEU A CB  1 
ATOM   702   C  CG  . LEU A  1 95  ? 94.908  78.427  45.736  1.00 35.69  ? 95  LEU A CG  1 
ATOM   703   C  CD1 . LEU A  1 95  ? 93.931  77.625  46.557  1.00 35.00  ? 95  LEU A CD1 1 
ATOM   704   C  CD2 . LEU A  1 95  ? 95.198  79.754  46.374  1.00 29.51  ? 95  LEU A CD2 1 
ATOM   705   N  N   . LYS A  1 96  ? 99.318  77.420  45.531  1.00 47.60  ? 96  LYS A N   1 
ATOM   706   C  CA  . LYS A  1 96  ? 100.466 76.543  45.416  1.00 50.18  ? 96  LYS A CA  1 
ATOM   707   C  C   . LYS A  1 96  ? 99.914  75.233  45.941  1.00 48.34  ? 96  LYS A C   1 
ATOM   708   O  O   . LYS A  1 96  ? 98.961  75.233  46.739  1.00 44.60  ? 96  LYS A O   1 
ATOM   709   C  CB  . LYS A  1 96  ? 101.626 77.036  46.284  1.00 59.58  ? 96  LYS A CB  1 
ATOM   710   C  CG  . LYS A  1 96  ? 102.683 77.863  45.531  1.00 74.37  ? 96  LYS A CG  1 
ATOM   711   C  CD  . LYS A  1 96  ? 102.479 79.390  45.651  1.00 87.01  ? 96  LYS A CD  1 
ATOM   712   C  CE  . LYS A  1 96  ? 102.948 79.986  47.010  1.00 93.10  ? 96  LYS A CE  1 
ATOM   713   N  NZ  . LYS A  1 96  ? 102.637 81.470  47.217  1.00 92.93  ? 96  LYS A NZ  1 
ATOM   714   N  N   . TYR A  1 97  ? 100.453 74.116  45.464  1.00 46.98  ? 97  TYR A N   1 
ATOM   715   C  CA  . TYR A  1 97  ? 99.933  72.835  45.913  1.00 45.77  ? 97  TYR A CA  1 
ATOM   716   C  C   . TYR A  1 97  ? 100.484 72.547  47.288  1.00 46.45  ? 97  TYR A C   1 
ATOM   717   O  O   . TYR A  1 97  ? 101.506 73.086  47.675  1.00 44.02  ? 97  TYR A O   1 
ATOM   718   C  CB  . TYR A  1 97  ? 100.345 71.695  44.973  1.00 40.10  ? 97  TYR A CB  1 
ATOM   719   C  CG  . TYR A  1 97  ? 99.677  71.635  43.604  1.00 39.24  ? 97  TYR A CG  1 
ATOM   720   C  CD1 . TYR A  1 97  ? 98.437  71.048  43.438  1.00 39.67  ? 97  TYR A CD1 1 
ATOM   721   C  CD2 . TYR A  1 97  ? 100.338 72.083  42.462  1.00 38.31  ? 97  TYR A CD2 1 
ATOM   722   C  CE1 . TYR A  1 97  ? 97.882  70.896  42.173  1.00 42.18  ? 97  TYR A CE1 1 
ATOM   723   C  CE2 . TYR A  1 97  ? 99.788  71.936  41.198  1.00 38.91  ? 97  TYR A CE2 1 
ATOM   724   C  CZ  . TYR A  1 97  ? 98.563  71.332  41.060  1.00 41.99  ? 97  TYR A CZ  1 
ATOM   725   O  OH  . TYR A  1 97  ? 98.068  71.074  39.797  1.00 43.21  ? 97  TYR A OH  1 
ATOM   726   N  N   . ASN A  1 98  ? 99.761  71.738  48.045  1.00 48.33  ? 98  ASN A N   1 
ATOM   727   C  CA  . ASN A  1 98  ? 100.209 71.297  49.359  1.00 47.28  ? 98  ASN A CA  1 
ATOM   728   C  C   . ASN A  1 98  ? 100.641 72.443  50.215  1.00 46.96  ? 98  ASN A C   1 
ATOM   729   O  O   . ASN A  1 98  ? 101.750 72.450  50.712  1.00 54.65  ? 98  ASN A O   1 
ATOM   730   C  CB  . ASN A  1 98  ? 101.393 70.335  49.174  1.00 51.61  ? 98  ASN A CB  1 
ATOM   731   C  CG  . ASN A  1 98  ? 101.551 69.359  50.308  1.00 56.63  ? 98  ASN A CG  1 
ATOM   732   O  OD1 . ASN A  1 98  ? 100.571 68.862  50.888  1.00 66.24  ? 98  ASN A OD1 1 
ATOM   733   N  ND2 . ASN A  1 98  ? 102.797 69.019  50.592  1.00 64.09  ? 98  ASN A ND2 1 
ATOM   734   N  N   . THR A  1 99  ? 99.758  73.389  50.458  1.00 42.00  ? 99  THR A N   1 
ATOM   735   C  CA  . THR A  1 99  ? 100.142 74.532  51.262  1.00 32.30  ? 99  THR A CA  1 
ATOM   736   C  C   . THR A  1 99  ? 98.971  74.901  52.137  1.00 32.29  ? 99  THR A C   1 
ATOM   737   O  O   . THR A  1 99  ? 97.832  74.722  51.735  1.00 36.15  ? 99  THR A O   1 
ATOM   738   C  CB  . THR A  1 99  ? 100.424 75.688  50.357  1.00 32.05  ? 99  THR A CB  1 
ATOM   739   O  OG1 . THR A  1 99  ? 101.478 75.342  49.474  1.00 33.66  ? 99  THR A OG1 1 
ATOM   740   C  CG2 . THR A  1 99  ? 100.804 76.881  51.119  1.00 32.12  ? 99  THR A CG2 1 
ATOM   741   N  N   . LYS A  1 100 ? 99.230  75.341  53.358  1.00 29.29  ? 100 LYS A N   1 
ATOM   742   C  CA  . LYS A  1 100 ? 98.151  75.732  54.230  1.00 24.51  ? 100 LYS A CA  1 
ATOM   743   C  C   . LYS A  1 100 ? 97.951  77.174  53.917  1.00 27.38  ? 100 LYS A C   1 
ATOM   744   O  O   . LYS A  1 100 ? 98.908  77.888  53.705  1.00 29.28  ? 100 LYS A O   1 
ATOM   745   C  CB  . LYS A  1 100 ? 98.509  75.602  55.679  1.00 16.40  ? 100 LYS A CB  1 
ATOM   746   C  CG  . LYS A  1 100 ? 97.391  76.007  56.575  1.00 19.99  ? 100 LYS A CG  1 
ATOM   747   C  CD  . LYS A  1 100 ? 97.780  75.828  58.035  1.00 29.17  ? 100 LYS A CD  1 
ATOM   748   C  CE  . LYS A  1 100 ? 96.544  75.676  58.982  1.00 41.20  ? 100 LYS A CE  1 
ATOM   749   N  NZ  . LYS A  1 100 ? 96.859  75.386  60.461  1.00 43.76  ? 100 LYS A NZ  1 
ATOM   750   N  N   . TYR A  1 101 ? 96.699  77.584  53.819  1.00 31.57  ? 101 TYR A N   1 
ATOM   751   C  CA  . TYR A  1 101 ? 96.348  78.945  53.512  1.00 28.07  ? 101 TYR A CA  1 
ATOM   752   C  C   . TYR A  1 101 ? 95.386  79.394  54.527  1.00 30.80  ? 101 TYR A C   1 
ATOM   753   O  O   . TYR A  1 101 ? 94.628  78.600  55.098  1.00 32.24  ? 101 TYR A O   1 
ATOM   754   C  CB  . TYR A  1 101 ? 95.644  78.988  52.192  1.00 30.20  ? 101 TYR A CB  1 
ATOM   755   C  CG  . TYR A  1 101 ? 96.594  79.033  51.030  1.00 30.92  ? 101 TYR A CG  1 
ATOM   756   C  CD1 . TYR A  1 101 ? 97.064  77.871  50.441  1.00 30.74  ? 101 TYR A CD1 1 
ATOM   757   C  CD2 . TYR A  1 101 ? 97.003  80.246  50.504  1.00 27.46  ? 101 TYR A CD2 1 
ATOM   758   C  CE1 . TYR A  1 101 ? 97.913  77.923  49.366  1.00 31.61  ? 101 TYR A CE1 1 
ATOM   759   C  CE2 . TYR A  1 101 ? 97.839  80.310  49.437  1.00 24.07  ? 101 TYR A CE2 1 
ATOM   760   C  CZ  . TYR A  1 101 ? 98.299  79.142  48.863  1.00 31.16  ? 101 TYR A CZ  1 
ATOM   761   O  OH  . TYR A  1 101 ? 99.162  79.185  47.774  1.00 36.04  ? 101 TYR A OH  1 
ATOM   762   N  N   . TYR A  1 102 ? 95.390  80.691  54.735  1.00 34.13  ? 102 TYR A N   1 
ATOM   763   C  CA  . TYR A  1 102 ? 94.472  81.279  55.675  1.00 37.50  ? 102 TYR A CA  1 
ATOM   764   C  C   . TYR A  1 102 ? 93.612  82.177  54.852  1.00 36.85  ? 102 TYR A C   1 
ATOM   765   O  O   . TYR A  1 102 ? 94.104  82.769  53.869  1.00 38.78  ? 102 TYR A O   1 
ATOM   766   C  CB  . TYR A  1 102 ? 95.217  82.136  56.666  1.00 43.48  ? 102 TYR A CB  1 
ATOM   767   C  CG  . TYR A  1 102 ? 95.911  81.340  57.712  1.00 50.29  ? 102 TYR A CG  1 
ATOM   768   C  CD1 . TYR A  1 102 ? 95.185  80.771  58.751  1.00 55.77  ? 102 TYR A CD1 1 
ATOM   769   C  CD2 . TYR A  1 102 ? 97.294  81.125  57.670  1.00 50.96  ? 102 TYR A CD2 1 
ATOM   770   C  CE1 . TYR A  1 102 ? 95.820  79.988  59.746  1.00 57.93  ? 102 TYR A CE1 1 
ATOM   771   C  CE2 . TYR A  1 102 ? 97.942  80.337  58.652  1.00 56.72  ? 102 TYR A CE2 1 
ATOM   772   C  CZ  . TYR A  1 102 ? 97.195  79.767  59.688  1.00 58.45  ? 102 TYR A CZ  1 
ATOM   773   O  OH  . TYR A  1 102 ? 97.787  78.921  60.619  1.00 63.62  ? 102 TYR A OH  1 
ATOM   774   N  N   . TYR A  1 103 ? 92.329  82.233  55.194  1.00 32.42  ? 103 TYR A N   1 
ATOM   775   C  CA  . TYR A  1 103 ? 91.438  83.121  54.485  1.00 32.12  ? 103 TYR A CA  1 
ATOM   776   C  C   . TYR A  1 103 ? 90.541  83.780  55.476  1.00 32.32  ? 103 TYR A C   1 
ATOM   777   O  O   . TYR A  1 103 ? 90.285  83.221  56.551  1.00 36.30  ? 103 TYR A O   1 
ATOM   778   C  CB  . TYR A  1 103 ? 90.680  82.427  53.337  1.00 30.62  ? 103 TYR A CB  1 
ATOM   779   C  CG  . TYR A  1 103 ? 89.598  81.442  53.701  1.00 29.74  ? 103 TYR A CG  1 
ATOM   780   C  CD1 . TYR A  1 103 ? 88.284  81.871  53.897  1.00 29.31  ? 103 TYR A CD1 1 
ATOM   781   C  CD2 . TYR A  1 103 ? 89.874  80.085  53.858  1.00 27.26  ? 103 TYR A CD2 1 
ATOM   782   C  CE1 . TYR A  1 103 ? 87.265  80.987  54.251  1.00 21.42  ? 103 TYR A CE1 1 
ATOM   783   C  CE2 . TYR A  1 103 ? 88.853  79.189  54.224  1.00 24.52  ? 103 TYR A CE2 1 
ATOM   784   C  CZ  . TYR A  1 103 ? 87.552  79.658  54.417  1.00 22.17  ? 103 TYR A CZ  1 
ATOM   785   O  OH  . TYR A  1 103 ? 86.540  78.814  54.791  1.00 12.75  ? 103 TYR A OH  1 
ATOM   786   N  N   . GLU A  1 104 ? 90.235  85.038  55.195  1.00 30.37  ? 104 GLU A N   1 
ATOM   787   C  CA  . GLU A  1 104 ? 89.373  85.815  56.043  1.00 32.79  ? 104 GLU A CA  1 
ATOM   788   C  C   . GLU A  1 104 ? 88.218  86.287  55.194  1.00 30.87  ? 104 GLU A C   1 
ATOM   789   O  O   . GLU A  1 104 ? 88.366  86.698  54.041  1.00 31.05  ? 104 GLU A O   1 
ATOM   790   C  CB  . GLU A  1 104 ? 90.129  86.998  56.641  1.00 39.09  ? 104 GLU A CB  1 
ATOM   791   C  CG  . GLU A  1 104 ? 91.124  86.615  57.717  1.00 41.41  ? 104 GLU A CG  1 
ATOM   792   C  CD  . GLU A  1 104 ? 91.806  87.810  58.307  1.00 44.76  ? 104 GLU A CD  1 
ATOM   793   O  OE1 . GLU A  1 104 ? 92.406  88.577  57.515  1.00 49.19  ? 104 GLU A OE1 1 
ATOM   794   O  OE2 . GLU A  1 104 ? 91.735  87.979  59.554  1.00 46.21  ? 104 GLU A OE2 1 
ATOM   795   N  N   . VAL A  1 105 ? 87.067  86.332  55.806  1.00 28.51  ? 105 VAL A N   1 
ATOM   796   C  CA  . VAL A  1 105 ? 85.882  86.674  55.081  1.00 27.36  ? 105 VAL A CA  1 
ATOM   797   C  C   . VAL A  1 105 ? 85.097  87.622  55.983  1.00 29.80  ? 105 VAL A C   1 
ATOM   798   O  O   . VAL A  1 105 ? 85.182  87.511  57.193  1.00 37.17  ? 105 VAL A O   1 
ATOM   799   C  CB  . VAL A  1 105 ? 85.190  85.322  54.829  1.00 23.87  ? 105 VAL A CB  1 
ATOM   800   C  CG1 . VAL A  1 105 ? 84.053  85.101  55.754  1.00 22.20  ? 105 VAL A CG1 1 
ATOM   801   C  CG2 . VAL A  1 105 ? 84.874  85.140  53.405  1.00 22.74  ? 105 VAL A CG2 1 
ATOM   802   N  N   . GLY A  1 106 ? 84.383  88.576  55.415  1.00 31.34  ? 106 GLY A N   1 
ATOM   803   C  CA  . GLY A  1 106 ? 83.642  89.546  56.220  1.00 34.30  ? 106 GLY A CA  1 
ATOM   804   C  C   . GLY A  1 106 ? 84.514  90.757  56.554  1.00 35.94  ? 106 GLY A C   1 
ATOM   805   O  O   . GLY A  1 106 ? 84.454  91.321  57.664  1.00 37.58  ? 106 GLY A O   1 
ATOM   806   N  N   . LEU A  1 107 ? 85.253  91.221  55.549  1.00 31.86  ? 107 LEU A N   1 
ATOM   807   C  CA  . LEU A  1 107 ? 86.181  92.305  55.744  1.00 29.73  ? 107 LEU A CA  1 
ATOM   808   C  C   . LEU A  1 107 ? 85.598  93.626  56.171  1.00 35.09  ? 107 LEU A C   1 
ATOM   809   O  O   . LEU A  1 107 ? 86.266  94.374  56.853  1.00 44.36  ? 107 LEU A O   1 
ATOM   810   C  CB  . LEU A  1 107 ? 87.026  92.527  54.497  1.00 27.05  ? 107 LEU A CB  1 
ATOM   811   C  CG  . LEU A  1 107 ? 87.656  91.359  53.738  1.00 24.64  ? 107 LEU A CG  1 
ATOM   812   C  CD1 . LEU A  1 107 ? 88.602  91.854  52.706  1.00 27.99  ? 107 LEU A CD1 1 
ATOM   813   C  CD2 . LEU A  1 107 ? 88.387  90.457  54.635  1.00 30.95  ? 107 LEU A CD2 1 
ATOM   814   N  N   . ARG A  1 108 ? 84.386  93.948  55.754  1.00 37.57  ? 108 ARG A N   1 
ATOM   815   C  CA  . ARG A  1 108 ? 83.811  95.236  56.122  1.00 44.79  ? 108 ARG A CA  1 
ATOM   816   C  C   . ARG A  1 108 ? 83.455  95.372  57.583  1.00 45.14  ? 108 ARG A C   1 
ATOM   817   O  O   . ARG A  1 108 ? 83.789  96.364  58.194  1.00 54.71  ? 108 ARG A O   1 
ATOM   818   C  CB  . ARG A  1 108 ? 82.589  95.594  55.259  1.00 51.81  ? 108 ARG A CB  1 
ATOM   819   C  CG  . ARG A  1 108 ? 82.868  96.552  54.079  1.00 65.26  ? 108 ARG A CG  1 
ATOM   820   C  CD  . ARG A  1 108 ? 81.601  96.918  53.265  1.00 74.36  ? 108 ARG A CD  1 
ATOM   821   N  NE  . ARG A  1 108 ? 80.703  97.900  53.909  1.00 90.02  ? 108 ARG A NE  1 
ATOM   822   C  CZ  . ARG A  1 108 ? 79.804  97.636  54.874  1.00 98.45  ? 108 ARG A CZ  1 
ATOM   823   N  NH1 . ARG A  1 108 ? 79.660  96.396  55.361  1.00 103.41 ? 108 ARG A NH1 1 
ATOM   824   N  NH2 . ARG A  1 108 ? 78.982  98.606  55.314  1.00 101.95 ? 108 ARG A NH2 1 
ATOM   825   N  N   . ASN A  1 109 ? 82.738  94.426  58.153  1.00 45.40  ? 109 ASN A N   1 
ATOM   826   C  CA  . ASN A  1 109 ? 82.404  94.572  59.543  1.00 47.61  ? 109 ASN A CA  1 
ATOM   827   C  C   . ASN A  1 109 ? 83.011  93.513  60.435  1.00 52.64  ? 109 ASN A C   1 
ATOM   828   O  O   . ASN A  1 109 ? 84.085  93.733  61.008  1.00 58.37  ? 109 ASN A O   1 
ATOM   829   C  CB  . ASN A  1 109 ? 80.904  94.702  59.739  1.00 51.24  ? 109 ASN A CB  1 
ATOM   830   C  CG  . ASN A  1 109 ? 80.381  95.999  59.199  1.00 57.51  ? 109 ASN A CG  1 
ATOM   831   O  OD1 . ASN A  1 109 ? 79.931  96.016  58.055  1.00 56.26  ? 109 ASN A OD1 1 
ATOM   832   N  ND2 . ASN A  1 109 ? 80.463  97.072  60.011  1.00 61.93  ? 109 ASN A ND2 1 
ATOM   833   N  N   . THR A  1 110 ? 82.362  92.357  60.547  1.00 50.18  ? 110 THR A N   1 
ATOM   834   C  CA  . THR A  1 110 ? 82.881  91.304  61.410  1.00 40.73  ? 110 THR A CA  1 
ATOM   835   C  C   . THR A  1 110 ? 83.683  90.292  60.599  1.00 36.51  ? 110 THR A C   1 
ATOM   836   O  O   . THR A  1 110 ? 83.131  89.608  59.785  1.00 43.06  ? 110 THR A O   1 
ATOM   837   C  CB  . THR A  1 110 ? 81.738  90.651  62.126  1.00 37.24  ? 110 THR A CB  1 
ATOM   838   O  OG1 . THR A  1 110 ? 80.965  91.659  62.787  1.00 38.62  ? 110 THR A OG1 1 
ATOM   839   C  CG2 . THR A  1 110 ? 82.244  89.669  63.133  1.00 40.17  ? 110 THR A CG2 1 
ATOM   840   N  N   . THR A  1 111 ? 84.988  90.248  60.781  1.00 28.24  ? 111 THR A N   1 
ATOM   841   C  CA  . THR A  1 111 ? 85.836  89.344  60.053  1.00 27.60  ? 111 THR A CA  1 
ATOM   842   C  C   . THR A  1 111 ? 85.997  87.969  60.707  1.00 31.32  ? 111 THR A C   1 
ATOM   843   O  O   . THR A  1 111 ? 86.042  87.889  61.950  1.00 34.78  ? 111 THR A O   1 
ATOM   844   C  CB  . THR A  1 111 ? 87.181  89.998  59.905  1.00 25.24  ? 111 THR A CB  1 
ATOM   845   O  OG1 . THR A  1 111 ? 87.053  91.084  58.988  1.00 39.40  ? 111 THR A OG1 1 
ATOM   846   C  CG2 . THR A  1 111 ? 88.213  89.038  59.388  1.00 30.55  ? 111 THR A CG2 1 
ATOM   847   N  N   . ARG A  1 112 ? 86.038  86.889  59.893  1.00 26.36  ? 112 ARG A N   1 
ATOM   848   C  CA  . ARG A  1 112 ? 86.248  85.518  60.408  1.00 22.44  ? 112 ARG A CA  1 
ATOM   849   C  C   . ARG A  1 112 ? 87.328  84.905  59.573  1.00 24.93  ? 112 ARG A C   1 
ATOM   850   O  O   . ARG A  1 112 ? 87.421  85.168  58.369  1.00 26.98  ? 112 ARG A O   1 
ATOM   851   C  CB  . ARG A  1 112 ? 84.979  84.670  60.437  1.00 13.16  ? 112 ARG A CB  1 
ATOM   852   C  CG  . ARG A  1 112 ? 84.008  85.233  61.432  1.00 20.39  ? 112 ARG A CG  1 
ATOM   853   C  CD  . ARG A  1 112 ? 82.656  84.588  61.452  1.00 26.19  ? 112 ARG A CD  1 
ATOM   854   N  NE  . ARG A  1 112 ? 82.761  83.260  62.013  1.00 33.64  ? 112 ARG A NE  1 
ATOM   855   C  CZ  . ARG A  1 112 ? 82.179  82.167  61.511  1.00 35.85  ? 112 ARG A CZ  1 
ATOM   856   N  NH1 . ARG A  1 112 ? 81.410  82.182  60.419  1.00 29.27  ? 112 ARG A NH1 1 
ATOM   857   N  NH2 . ARG A  1 112 ? 82.396  81.025  62.122  1.00 36.32  ? 112 ARG A NH2 1 
ATOM   858   N  N   . ARG A  1 113 ? 88.197  84.173  60.249  1.00 25.35  ? 113 ARG A N   1 
ATOM   859   C  CA  . ARG A  1 113 ? 89.345  83.548  59.616  1.00 32.07  ? 113 ARG A CA  1 
ATOM   860   C  C   . ARG A  1 113 ? 89.267  82.010  59.602  1.00 33.22  ? 113 ARG A C   1 
ATOM   861   O  O   . ARG A  1 113 ? 88.746  81.381  60.559  1.00 29.14  ? 113 ARG A O   1 
ATOM   862   C  CB  . ARG A  1 113 ? 90.610  83.997  60.337  1.00 36.39  ? 113 ARG A CB  1 
ATOM   863   C  CG  . ARG A  1 113 ? 91.874  83.284  59.942  1.00 50.67  ? 113 ARG A CG  1 
ATOM   864   C  CD  . ARG A  1 113 ? 93.048  83.841  60.729  1.00 64.53  ? 113 ARG A CD  1 
ATOM   865   N  NE  . ARG A  1 113 ? 93.267  85.250  60.414  1.00 77.33  ? 113 ARG A NE  1 
ATOM   866   C  CZ  . ARG A  1 113 ? 94.251  85.997  60.908  1.00 82.69  ? 113 ARG A CZ  1 
ATOM   867   N  NH1 . ARG A  1 113 ? 95.135  85.472  61.761  1.00 82.08  ? 113 ARG A NH1 1 
ATOM   868   N  NH2 . ARG A  1 113 ? 94.347  87.280  60.544  1.00 84.83  ? 113 ARG A NH2 1 
ATOM   869   N  N   . PHE A  1 114 ? 89.808  81.419  58.532  1.00 27.65  ? 114 PHE A N   1 
ATOM   870   C  CA  . PHE A  1 114 ? 89.798  79.989  58.374  1.00 23.20  ? 114 PHE A CA  1 
ATOM   871   C  C   . PHE A  1 114 ? 91.064  79.594  57.649  1.00 26.70  ? 114 PHE A C   1 
ATOM   872   O  O   . PHE A  1 114 ? 91.871  80.456  57.258  1.00 27.48  ? 114 PHE A O   1 
ATOM   873   C  CB  . PHE A  1 114 ? 88.590  79.559  57.545  1.00 22.17  ? 114 PHE A CB  1 
ATOM   874   C  CG  . PHE A  1 114 ? 87.271  80.033  58.089  1.00 24.58  ? 114 PHE A CG  1 
ATOM   875   C  CD1 . PHE A  1 114 ? 86.553  79.252  59.012  1.00 22.12  ? 114 PHE A CD1 1 
ATOM   876   C  CD2 . PHE A  1 114 ? 86.736  81.260  57.683  1.00 22.39  ? 114 PHE A CD2 1 
ATOM   877   C  CE1 . PHE A  1 114 ? 85.327  79.686  59.533  1.00 18.41  ? 114 PHE A CE1 1 
ATOM   878   C  CE2 . PHE A  1 114 ? 85.499  81.706  58.198  1.00 28.16  ? 114 PHE A CE2 1 
ATOM   879   C  CZ  . PHE A  1 114 ? 84.796  80.913  59.130  1.00 25.54  ? 114 PHE A CZ  1 
ATOM   880   N  N   . SER A  1 115 ? 91.220  78.295  57.427  1.00 24.70  ? 115 SER A N   1 
ATOM   881   C  CA  . SER A  1 115 ? 92.380  77.814  56.722  1.00 27.92  ? 115 SER A CA  1 
ATOM   882   C  C   . SER A  1 115 ? 92.018  76.542  56.051  1.00 29.91  ? 115 SER A C   1 
ATOM   883   O  O   . SER A  1 115 ? 91.156  75.808  56.512  1.00 31.61  ? 115 SER A O   1 
ATOM   884   C  CB  . SER A  1 115 ? 93.493  77.497  57.683  1.00 34.06  ? 115 SER A CB  1 
ATOM   885   O  OG  . SER A  1 115 ? 93.038  76.574  58.669  1.00 45.30  ? 115 SER A OG  1 
ATOM   886   N  N   . PHE A  1 116 ? 92.719  76.267  54.975  1.00 27.31  ? 116 PHE A N   1 
ATOM   887   C  CA  . PHE A  1 116 ? 92.503  75.049  54.245  1.00 27.87  ? 116 PHE A CA  1 
ATOM   888   C  C   . PHE A  1 116 ? 93.888  74.722  53.684  1.00 32.76  ? 116 PHE A C   1 
ATOM   889   O  O   . PHE A  1 116 ? 94.767  75.594  53.659  1.00 35.18  ? 116 PHE A O   1 
ATOM   890   C  CB  . PHE A  1 116 ? 91.466  75.265  53.120  1.00 19.11  ? 116 PHE A CB  1 
ATOM   891   C  CG  . PHE A  1 116 ? 91.870  76.308  52.095  1.00 19.17  ? 116 PHE A CG  1 
ATOM   892   C  CD1 . PHE A  1 116 ? 92.831  76.038  51.128  1.00 19.42  ? 116 PHE A CD1 1 
ATOM   893   C  CD2 . PHE A  1 116 ? 91.257  77.545  52.081  1.00 14.83  ? 116 PHE A CD2 1 
ATOM   894   C  CE1 . PHE A  1 116 ? 93.174  76.976  50.166  1.00 21.09  ? 116 PHE A CE1 1 
ATOM   895   C  CE2 . PHE A  1 116 ? 91.588  78.478  51.129  1.00 18.40  ? 116 PHE A CE2 1 
ATOM   896   C  CZ  . PHE A  1 116 ? 92.558  78.190  50.158  1.00 15.21  ? 116 PHE A CZ  1 
ATOM   897   N  N   . ILE A  1 117 ? 94.087  73.481  53.241  1.00 32.21  ? 117 ILE A N   1 
ATOM   898   C  CA  . ILE A  1 117 ? 95.351  73.083  52.645  1.00 30.96  ? 117 ILE A CA  1 
ATOM   899   C  C   . ILE A  1 117 ? 95.182  72.570  51.218  1.00 30.02  ? 117 ILE A C   1 
ATOM   900   O  O   . ILE A  1 117 ? 94.393  71.640  50.971  1.00 31.85  ? 117 ILE A O   1 
ATOM   901   C  CB  . ILE A  1 117 ? 95.956  72.006  53.432  1.00 31.26  ? 117 ILE A CB  1 
ATOM   902   C  CG1 . ILE A  1 117 ? 96.013  72.439  54.875  1.00 36.14  ? 117 ILE A CG1 1 
ATOM   903   C  CG2 . ILE A  1 117 ? 97.314  71.715  52.910  1.00 31.73  ? 117 ILE A CG2 1 
ATOM   904   C  CD1 . ILE A  1 117 ? 96.554  71.382  55.758  1.00 34.73  ? 117 ILE A CD1 1 
ATOM   905   N  N   . THR A  1 118 ? 95.934  73.139  50.283  1.00 25.48  ? 118 THR A N   1 
ATOM   906   C  CA  . THR A  1 118 ? 95.782  72.718  48.918  1.00 24.39  ? 118 THR A CA  1 
ATOM   907   C  C   . THR A  1 118 ? 96.275  71.308  48.865  1.00 24.80  ? 118 THR A C   1 
ATOM   908   O  O   . THR A  1 118 ? 96.993  70.880  49.739  1.00 26.59  ? 118 THR A O   1 
ATOM   909   C  CB  . THR A  1 118 ? 96.550  73.636  47.993  1.00 27.59  ? 118 THR A CB  1 
ATOM   910   O  OG1 . THR A  1 118 ? 97.821  73.924  48.589  1.00 27.29  ? 118 THR A OG1 1 
ATOM   911   C  CG2 . THR A  1 118 ? 95.751  74.940  47.778  1.00 23.11  ? 118 THR A CG2 1 
ATOM   912   N  N   . PRO A  1 119 ? 95.807  70.536  47.900  1.00 23.62  ? 119 PRO A N   1 
ATOM   913   C  CA  . PRO A  1 119 ? 96.248  69.155  47.795  1.00 26.64  ? 119 PRO A CA  1 
ATOM   914   C  C   . PRO A  1 119 ? 97.535  69.063  46.990  1.00 27.90  ? 119 PRO A C   1 
ATOM   915   O  O   . PRO A  1 119 ? 97.984  70.028  46.370  1.00 30.73  ? 119 PRO A O   1 
ATOM   916   C  CB  . PRO A  1 119 ? 95.113  68.511  46.998  1.00 27.20  ? 119 PRO A CB  1 
ATOM   917   C  CG  . PRO A  1 119 ? 94.833  69.562  45.959  1.00 25.68  ? 119 PRO A CG  1 
ATOM   918   C  CD  . PRO A  1 119 ? 94.818  70.842  46.848  1.00 27.30  ? 119 PRO A CD  1 
ATOM   919   N  N   . PRO A  1 120 ? 98.111  67.874  46.946  1.00 26.76  ? 120 PRO A N   1 
ATOM   920   C  CA  . PRO A  1 120 ? 99.336  67.623  46.213  1.00 27.69  ? 120 PRO A CA  1 
ATOM   921   C  C   . PRO A  1 120 ? 99.033  67.749  44.755  1.00 28.38  ? 120 PRO A C   1 
ATOM   922   O  O   . PRO A  1 120 ? 97.885  67.679  44.337  1.00 31.66  ? 120 PRO A O   1 
ATOM   923   C  CB  . PRO A  1 120 ? 99.599  66.165  46.521  1.00 31.41  ? 120 PRO A CB  1 
ATOM   924   C  CG  . PRO A  1 120 ? 98.885  65.930  47.823  1.00 32.41  ? 120 PRO A CG  1 
ATOM   925   C  CD  . PRO A  1 120 ? 97.634  66.654  47.608  1.00 29.17  ? 120 PRO A CD  1 
ATOM   926   N  N   . GLN A  1 121 ? 100.070 67.931  43.969  1.00 33.50  ? 121 GLN A N   1 
ATOM   927   C  CA  . GLN A  1 121 ? 99.882  68.004  42.549  1.00 35.76  ? 121 GLN A CA  1 
ATOM   928   C  C   . GLN A  1 121 ? 99.371  66.628  42.162  1.00 37.37  ? 121 GLN A C   1 
ATOM   929   O  O   . GLN A  1 121 ? 99.746  65.657  42.791  1.00 42.78  ? 121 GLN A O   1 
ATOM   930   C  CB  . GLN A  1 121 ? 101.219 68.251  41.914  1.00 38.92  ? 121 GLN A CB  1 
ATOM   931   C  CG  . GLN A  1 121 ? 101.149 68.262  40.433  1.00 56.17  ? 121 GLN A CG  1 
ATOM   932   C  CD  . GLN A  1 121 ? 102.367 68.890  39.835  1.00 67.28  ? 121 GLN A CD  1 
ATOM   933   O  OE1 . GLN A  1 121 ? 103.333 69.195  40.547  1.00 77.08  ? 121 GLN A OE1 1 
ATOM   934   N  NE2 . GLN A  1 121 ? 102.325 69.132  38.525  1.00 75.03  ? 121 GLN A NE2 1 
ATOM   935   N  N   . THR A  1 122 ? 98.510  66.530  41.158  1.00 40.58  ? 122 THR A N   1 
ATOM   936   C  CA  . THR A  1 122 ? 97.986  65.216  40.757  1.00 41.28  ? 122 THR A CA  1 
ATOM   937   C  C   . THR A  1 122 ? 99.104  64.283  40.378  1.00 39.44  ? 122 THR A C   1 
ATOM   938   O  O   . THR A  1 122 ? 100.041 64.690  39.713  1.00 38.82  ? 122 THR A O   1 
ATOM   939   C  CB  . THR A  1 122 ? 96.980  65.294  39.587  1.00 41.23  ? 122 THR A CB  1 
ATOM   940   O  OG1 . THR A  1 122 ? 97.620  65.787  38.394  1.00 40.89  ? 122 THR A OG1 1 
ATOM   941   C  CG2 . THR A  1 122 ? 95.852  66.224  39.965  1.00 49.06  ? 122 THR A CG2 1 
ATOM   942   N  N   . GLY A  1 123 ? 99.008  63.030  40.799  1.00 42.45  ? 123 GLY A N   1 
ATOM   943   C  CA  . GLY A  1 123 ? 100.057 62.078  40.484  1.00 42.35  ? 123 GLY A CA  1 
ATOM   944   C  C   . GLY A  1 123 ? 99.646  60.630  40.647  1.00 40.54  ? 123 GLY A C   1 
ATOM   945   O  O   . GLY A  1 123 ? 98.683  60.316  41.353  1.00 44.34  ? 123 GLY A O   1 
ATOM   946   N  N   . LEU A  1 124 ? 100.454 59.752  40.066  1.00 39.41  ? 124 LEU A N   1 
ATOM   947   C  CA  . LEU A  1 124 ? 100.221 58.330  40.059  1.00 38.69  ? 124 LEU A CA  1 
ATOM   948   C  C   . LEU A  1 124 ? 100.204 57.672  41.421  1.00 38.92  ? 124 LEU A C   1 
ATOM   949   O  O   . LEU A  1 124 ? 99.318  56.873  41.722  1.00 40.33  ? 124 LEU A O   1 
ATOM   950   C  CB  . LEU A  1 124 ? 101.265 57.707  39.156  1.00 37.27  ? 124 LEU A CB  1 
ATOM   951   C  CG  . LEU A  1 124 ? 100.942 56.402  38.466  1.00 39.71  ? 124 LEU A CG  1 
ATOM   952   C  CD1 . LEU A  1 124 ? 99.498  56.316  38.029  1.00 44.74  ? 124 LEU A CD1 1 
ATOM   953   C  CD2 . LEU A  1 124 ? 101.852 56.317  37.285  1.00 43.63  ? 124 LEU A CD2 1 
ATOM   954   N  N   . ASP A  1 125 ? 101.167 58.022  42.263  1.00 41.26  ? 125 ASP A N   1 
ATOM   955   C  CA  . ASP A  1 125 ? 101.229 57.413  43.584  1.00 44.67  ? 125 ASP A CA  1 
ATOM   956   C  C   . ASP A  1 125 ? 100.924 58.365  44.752  1.00 44.85  ? 125 ASP A C   1 
ATOM   957   O  O   . ASP A  1 125 ? 101.262 58.088  45.903  1.00 52.17  ? 125 ASP A O   1 
ATOM   958   C  CB  . ASP A  1 125 ? 102.592 56.739  43.797  1.00 45.96  ? 125 ASP A CB  1 
ATOM   959   C  CG  . ASP A  1 125 ? 102.794 55.505  42.925  1.00 46.18  ? 125 ASP A CG  1 
ATOM   960   O  OD1 . ASP A  1 125 ? 102.002 54.534  43.009  1.00 44.95  ? 125 ASP A OD1 1 
ATOM   961   O  OD2 . ASP A  1 125 ? 103.769 55.523  42.158  1.00 41.88  ? 125 ASP A OD2 1 
ATOM   962   N  N   . VAL A  1 126 ? 100.263 59.478  44.471  1.00 41.00  ? 126 VAL A N   1 
ATOM   963   C  CA  . VAL A  1 126 ? 99.912  60.447  45.510  1.00 33.49  ? 126 VAL A CA  1 
ATOM   964   C  C   . VAL A  1 126 ? 98.740  59.911  46.313  1.00 32.10  ? 126 VAL A C   1 
ATOM   965   O  O   . VAL A  1 126 ? 97.631  59.691  45.811  1.00 34.75  ? 126 VAL A O   1 
ATOM   966   C  CB  . VAL A  1 126 ? 99.481  61.779  44.897  1.00 39.86  ? 126 VAL A CB  1 
ATOM   967   C  CG1 . VAL A  1 126 ? 99.175  62.784  45.990  1.00 32.59  ? 126 VAL A CG1 1 
ATOM   968   C  CG2 . VAL A  1 126 ? 100.545 62.282  43.904  1.00 38.00  ? 126 VAL A CG2 1 
ATOM   969   N  N   . PRO A  1 127 ? 98.965  59.686  47.578  1.00 30.28  ? 127 PRO A N   1 
ATOM   970   C  CA  . PRO A  1 127 ? 97.918  59.168  48.462  1.00 32.02  ? 127 PRO A CA  1 
ATOM   971   C  C   . PRO A  1 127 ? 97.027  60.320  48.891  1.00 31.42  ? 127 PRO A C   1 
ATOM   972   O  O   . PRO A  1 127 ? 97.449  61.488  48.858  1.00 32.69  ? 127 PRO A O   1 
ATOM   973   C  CB  . PRO A  1 127 ? 98.724  58.620  49.624  1.00 32.45  ? 127 PRO A CB  1 
ATOM   974   C  CG  . PRO A  1 127 ? 99.860  59.632  49.712  1.00 26.71  ? 127 PRO A CG  1 
ATOM   975   C  CD  . PRO A  1 127 ? 100.234 59.883  48.280  1.00 29.52  ? 127 PRO A CD  1 
ATOM   976   N  N   . TYR A  1 128 ? 95.817  60.007  49.326  1.00 27.54  ? 128 TYR A N   1 
ATOM   977   C  CA  . TYR A  1 128 ? 94.911  61.058  49.741  1.00 25.24  ? 128 TYR A CA  1 
ATOM   978   C  C   . TYR A  1 128 ? 93.770  60.323  50.360  1.00 26.39  ? 128 TYR A C   1 
ATOM   979   O  O   . TYR A  1 128 ? 93.482  59.198  49.979  1.00 29.65  ? 128 TYR A O   1 
ATOM   980   C  CB  . TYR A  1 128 ? 94.428  61.847  48.532  1.00 26.75  ? 128 TYR A CB  1 
ATOM   981   C  CG  . TYR A  1 128 ? 93.914  63.218  48.881  1.00 30.02  ? 128 TYR A CG  1 
ATOM   982   C  CD1 . TYR A  1 128 ? 94.795  64.248  49.109  1.00 30.64  ? 128 TYR A CD1 1 
ATOM   983   C  CD2 . TYR A  1 128 ? 92.544  63.486  48.990  1.00 31.16  ? 128 TYR A CD2 1 
ATOM   984   C  CE1 . TYR A  1 128 ? 94.352  65.516  49.445  1.00 34.69  ? 128 TYR A CE1 1 
ATOM   985   C  CE2 . TYR A  1 128 ? 92.093  64.759  49.322  1.00 37.08  ? 128 TYR A CE2 1 
ATOM   986   C  CZ  . TYR A  1 128 ? 93.001  65.767  49.558  1.00 39.70  ? 128 TYR A CZ  1 
ATOM   987   O  OH  . TYR A  1 128 ? 92.576  67.018  49.976  1.00 47.39  ? 128 TYR A OH  1 
ATOM   988   N  N   . THR A  1 129 ? 93.112  60.933  51.324  1.00 24.61  ? 129 THR A N   1 
ATOM   989   C  CA  . THR A  1 129 ? 92.023  60.230  51.945  1.00 28.66  ? 129 THR A CA  1 
ATOM   990   C  C   . THR A  1 129 ? 90.698  60.979  51.861  1.00 28.48  ? 129 THR A C   1 
ATOM   991   O  O   . THR A  1 129 ? 90.600  62.118  52.322  1.00 28.78  ? 129 THR A O   1 
ATOM   992   C  CB  . THR A  1 129 ? 92.405  59.755  53.366  1.00 26.51  ? 129 THR A CB  1 
ATOM   993   O  OG1 . THR A  1 129 ? 91.308  60.002  54.263  1.00 36.34  ? 129 THR A OG1 1 
ATOM   994   C  CG2 . THR A  1 129 ? 93.670  60.418  53.868  1.00 28.97  ? 129 THR A CG2 1 
ATOM   995   N  N   . PHE A  1 130 ? 89.682  60.336  51.274  1.00 21.91  ? 130 PHE A N   1 
ATOM   996   C  CA  . PHE A  1 130 ? 88.402  60.948  51.079  1.00 15.21  ? 130 PHE A CA  1 
ATOM   997   C  C   . PHE A  1 130 ? 87.426  60.456  52.096  1.00 16.53  ? 130 PHE A C   1 
ATOM   998   O  O   . PHE A  1 130 ? 87.470  59.309  52.502  1.00 20.41  ? 130 PHE A O   1 
ATOM   999   C  CB  . PHE A  1 130 ? 87.892  60.619  49.691  1.00 12.17  ? 130 PHE A CB  1 
ATOM   1000  C  CG  . PHE A  1 130 ? 88.721  61.197  48.587  1.00 9.31   ? 130 PHE A CG  1 
ATOM   1001  C  CD1 . PHE A  1 130 ? 88.523  62.483  48.157  1.00 8.94   ? 130 PHE A CD1 1 
ATOM   1002  C  CD2 . PHE A  1 130 ? 89.660  60.442  47.950  1.00 6.55   ? 130 PHE A CD2 1 
ATOM   1003  C  CE1 . PHE A  1 130 ? 89.237  62.989  47.130  1.00 8.30   ? 130 PHE A CE1 1 
ATOM   1004  C  CE2 . PHE A  1 130 ? 90.395  60.956  46.896  1.00 2.00   ? 130 PHE A CE2 1 
ATOM   1005  C  CZ  . PHE A  1 130 ? 90.185  62.211  46.484  1.00 7.35   ? 130 PHE A CZ  1 
ATOM   1006  N  N   . GLY A  1 131 ? 86.554  61.336  52.544  1.00 16.73  ? 131 GLY A N   1 
ATOM   1007  C  CA  . GLY A  1 131 ? 85.541  60.914  53.469  1.00 16.83  ? 131 GLY A CA  1 
ATOM   1008  C  C   . GLY A  1 131 ? 84.319  60.672  52.592  1.00 17.34  ? 131 GLY A C   1 
ATOM   1009  O  O   . GLY A  1 131 ? 84.202  61.253  51.523  1.00 19.57  ? 131 GLY A O   1 
ATOM   1010  N  N   . LEU A  1 132 ? 83.408  59.817  53.019  1.00 15.74  ? 132 LEU A N   1 
ATOM   1011  C  CA  . LEU A  1 132 ? 82.221  59.565  52.266  1.00 14.45  ? 132 LEU A CA  1 
ATOM   1012  C  C   . LEU A  1 132 ? 81.046  59.765  53.132  1.00 15.72  ? 132 LEU A C   1 
ATOM   1013  O  O   . LEU A  1 132 ? 80.875  59.087  54.123  1.00 16.22  ? 132 LEU A O   1 
ATOM   1014  C  CB  . LEU A  1 132 ? 82.231  58.175  51.742  1.00 18.84  ? 132 LEU A CB  1 
ATOM   1015  C  CG  . LEU A  1 132 ? 82.818  58.434  50.368  1.00 24.73  ? 132 LEU A CG  1 
ATOM   1016  C  CD1 . LEU A  1 132 ? 84.261  58.037  50.304  1.00 28.91  ? 132 LEU A CD1 1 
ATOM   1017  C  CD2 . LEU A  1 132 ? 82.008  57.699  49.351  1.00 30.93  ? 132 LEU A CD2 1 
ATOM   1018  N  N   . ILE A  1 133 ? 80.254  60.754  52.779  1.00 17.17  ? 133 ILE A N   1 
ATOM   1019  C  CA  . ILE A  1 133 ? 79.051  61.083  53.541  1.00 19.81  ? 133 ILE A CA  1 
ATOM   1020  C  C   . ILE A  1 133 ? 77.941  61.269  52.530  1.00 21.92  ? 133 ILE A C   1 
ATOM   1021  O  O   . ILE A  1 133 ? 78.141  61.854  51.439  1.00 27.63  ? 133 ILE A O   1 
ATOM   1022  C  CB  . ILE A  1 133 ? 79.223  62.390  54.304  1.00 13.27  ? 133 ILE A CB  1 
ATOM   1023  C  CG1 . ILE A  1 133 ? 80.518  62.343  55.106  1.00 17.71  ? 133 ILE A CG1 1 
ATOM   1024  C  CG2 . ILE A  1 133 ? 78.045  62.595  55.240  1.00 18.25  ? 133 ILE A CG2 1 
ATOM   1025  C  CD1 . ILE A  1 133 ? 80.609  63.352  56.209  1.00 8.22   ? 133 ILE A CD1 1 
ATOM   1026  N  N   . GLY A  1 134 ? 76.780  60.752  52.847  1.00 18.83  ? 134 GLY A N   1 
ATOM   1027  C  CA  . GLY A  1 134 ? 75.706  60.885  51.905  1.00 19.65  ? 134 GLY A CA  1 
ATOM   1028  C  C   . GLY A  1 134 ? 74.445  60.958  52.700  1.00 21.90  ? 134 GLY A C   1 
ATOM   1029  O  O   . GLY A  1 134 ? 74.374  60.435  53.797  1.00 28.52  ? 134 GLY A O   1 
ATOM   1030  N  N   . ASP A  1 135 ? 73.495  61.733  52.225  1.00 19.09  ? 135 ASP A N   1 
ATOM   1031  C  CA  . ASP A  1 135 ? 72.272  61.808  52.953  1.00 16.67  ? 135 ASP A CA  1 
ATOM   1032  C  C   . ASP A  1 135 ? 72.289  62.327  54.389  1.00 16.22  ? 135 ASP A C   1 
ATOM   1033  O  O   . ASP A  1 135 ? 71.464  61.888  55.178  1.00 21.13  ? 135 ASP A O   1 
ATOM   1034  C  CB  . ASP A  1 135 ? 71.765  60.397  52.890  1.00 20.79  ? 135 ASP A CB  1 
ATOM   1035  C  CG  . ASP A  1 135 ? 70.958  60.183  51.681  1.00 26.62  ? 135 ASP A CG  1 
ATOM   1036  O  OD1 . ASP A  1 135 ? 69.826  60.467  51.963  1.00 26.22  ? 135 ASP A OD1 1 
ATOM   1037  O  OD2 . ASP A  1 135 ? 71.421  59.780  50.602  1.00 21.83  ? 135 ASP A OD2 1 
ATOM   1038  N  N   . LEU A  1 136 ? 73.091  63.363  54.666  1.00 13.38  ? 136 LEU A N   1 
ATOM   1039  C  CA  . LEU A  1 136 ? 73.305  63.902  56.011  1.00 11.35  ? 136 LEU A CA  1 
ATOM   1040  C  C   . LEU A  1 136 ? 72.113  64.458  56.766  1.00 18.79  ? 136 LEU A C   1 
ATOM   1041  O  O   . LEU A  1 136 ? 71.815  64.013  57.876  1.00 25.40  ? 136 LEU A O   1 
ATOM   1042  C  CB  . LEU A  1 136 ? 74.438  64.947  56.002  1.00 18.01  ? 136 LEU A CB  1 
ATOM   1043  C  CG  . LEU A  1 136 ? 75.003  65.502  57.329  1.00 15.47  ? 136 LEU A CG  1 
ATOM   1044  C  CD1 . LEU A  1 136 ? 75.648  64.407  58.108  1.00 14.36  ? 136 LEU A CD1 1 
ATOM   1045  C  CD2 . LEU A  1 136 ? 76.009  66.572  57.052  1.00 13.93  ? 136 LEU A CD2 1 
ATOM   1046  N  N   . GLY A  1 137 ? 71.478  65.501  56.249  1.00 21.82  ? 137 GLY A N   1 
ATOM   1047  C  CA  . GLY A  1 137 ? 70.337  66.071  56.949  1.00 20.95  ? 137 GLY A CA  1 
ATOM   1048  C  C   . GLY A  1 137 ? 70.737  66.768  58.225  1.00 20.81  ? 137 GLY A C   1 
ATOM   1049  O  O   . GLY A  1 137 ? 71.898  67.146  58.395  1.00 21.53  ? 137 GLY A O   1 
ATOM   1050  N  N   . GLN A  1 138 ? 69.775  66.947  59.118  1.00 21.60  ? 138 GLN A N   1 
ATOM   1051  C  CA  . GLN A  1 138 ? 70.086  67.607  60.372  1.00 22.63  ? 138 GLN A CA  1 
ATOM   1052  C  C   . GLN A  1 138 ? 69.396  67.059  61.640  1.00 27.40  ? 138 GLN A C   1 
ATOM   1053  O  O   . GLN A  1 138 ? 68.897  67.839  62.485  1.00 26.63  ? 138 GLN A O   1 
ATOM   1054  C  CB  . GLN A  1 138 ? 69.898  69.120  60.242  1.00 24.37  ? 138 GLN A CB  1 
ATOM   1055  C  CG  . GLN A  1 138 ? 68.520  69.555  59.852  1.00 29.34  ? 138 GLN A CG  1 
ATOM   1056  C  CD  . GLN A  1 138 ? 68.465  70.997  59.444  1.00 26.33  ? 138 GLN A CD  1 
ATOM   1057  O  OE1 . GLN A  1 138 ? 68.565  71.324  58.270  1.00 26.99  ? 138 GLN A OE1 1 
ATOM   1058  N  NE2 . GLN A  1 138 ? 68.307  71.868  60.415  1.00 23.77  ? 138 GLN A NE2 1 
ATOM   1059  N  N   . SER A  1 139 ? 69.392  65.728  61.782  1.00 27.45  ? 139 SER A N   1 
ATOM   1060  C  CA  . SER A  1 139 ? 68.848  65.082  62.967  1.00 26.79  ? 139 SER A CA  1 
ATOM   1061  C  C   . SER A  1 139 ? 70.077  64.929  63.876  1.00 31.01  ? 139 SER A C   1 
ATOM   1062  O  O   . SER A  1 139 ? 71.231  65.141  63.460  1.00 31.67  ? 139 SER A O   1 
ATOM   1063  C  CB  . SER A  1 139 ? 68.292  63.709  62.617  1.00 26.04  ? 139 SER A CB  1 
ATOM   1064  O  OG  . SER A  1 139 ? 69.307  62.882  62.091  1.00 31.86  ? 139 SER A OG  1 
ATOM   1065  N  N   . PHE A  1 140 ? 69.863  64.496  65.106  1.00 30.24  ? 140 PHE A N   1 
ATOM   1066  C  CA  . PHE A  1 140 ? 70.983  64.331  66.003  1.00 24.44  ? 140 PHE A CA  1 
ATOM   1067  C  C   . PHE A  1 140 ? 71.926  63.354  65.417  1.00 23.74  ? 140 PHE A C   1 
ATOM   1068  O  O   . PHE A  1 140 ? 73.131  63.499  65.500  1.00 29.06  ? 140 PHE A O   1 
ATOM   1069  C  CB  . PHE A  1 140 ? 70.497  63.808  67.305  1.00 24.82  ? 140 PHE A CB  1 
ATOM   1070  C  CG  . PHE A  1 140 ? 69.589  64.737  67.987  1.00 23.60  ? 140 PHE A CG  1 
ATOM   1071  C  CD1 . PHE A  1 140 ? 70.090  65.757  68.775  1.00 25.73  ? 140 PHE A CD1 1 
ATOM   1072  C  CD2 . PHE A  1 140 ? 68.232  64.614  67.829  1.00 29.91  ? 140 PHE A CD2 1 
ATOM   1073  C  CE1 . PHE A  1 140 ? 69.251  66.639  69.393  1.00 25.37  ? 140 PHE A CE1 1 
ATOM   1074  C  CE2 . PHE A  1 140 ? 67.371  65.496  68.452  1.00 33.42  ? 140 PHE A CE2 1 
ATOM   1075  C  CZ  . PHE A  1 140 ? 67.879  66.510  69.235  1.00 26.84  ? 140 PHE A CZ  1 
ATOM   1076  N  N   . ASP A  1 141 ? 71.353  62.370  64.766  1.00 22.57  ? 141 ASP A N   1 
ATOM   1077  C  CA  . ASP A  1 141 ? 72.133  61.347  64.139  1.00 23.52  ? 141 ASP A CA  1 
ATOM   1078  C  C   . ASP A  1 141 ? 73.157  61.950  63.198  1.00 24.99  ? 141 ASP A C   1 
ATOM   1079  O  O   . ASP A  1 141 ? 74.340  61.630  63.196  1.00 26.87  ? 141 ASP A O   1 
ATOM   1080  C  CB  . ASP A  1 141 ? 71.184  60.444  63.424  1.00 21.46  ? 141 ASP A CB  1 
ATOM   1081  C  CG  . ASP A  1 141 ? 70.479  59.491  64.374  1.00 32.28  ? 141 ASP A CG  1 
ATOM   1082  O  OD1 . ASP A  1 141 ? 71.185  58.723  65.087  1.00 35.37  ? 141 ASP A OD1 1 
ATOM   1083  O  OD2 . ASP A  1 141 ? 69.223  59.495  64.400  1.00 41.96  ? 141 ASP A OD2 1 
ATOM   1084  N  N   . SER A  1 142 ? 72.718  62.945  62.478  1.00 25.85  ? 142 SER A N   1 
ATOM   1085  C  CA  . SER A  1 142 ? 73.607  63.574  61.554  1.00 25.67  ? 142 SER A CA  1 
ATOM   1086  C  C   . SER A  1 142 ? 74.773  64.168  62.328  1.00 26.03  ? 142 SER A C   1 
ATOM   1087  O  O   . SER A  1 142 ? 75.940  64.029  61.920  1.00 27.04  ? 142 SER A O   1 
ATOM   1088  C  CB  . SER A  1 142 ? 72.840  64.658  60.796  1.00 25.67  ? 142 SER A CB  1 
ATOM   1089  O  OG  . SER A  1 142 ? 71.484  64.285  60.585  1.00 26.06  ? 142 SER A OG  1 
ATOM   1090  N  N   . ASN A  1 143 ? 74.465  64.784  63.470  1.00 27.01  ? 143 ASN A N   1 
ATOM   1091  C  CA  . ASN A  1 143 ? 75.490  65.457  64.271  1.00 24.61  ? 143 ASN A CA  1 
ATOM   1092  C  C   . ASN A  1 143 ? 76.530  64.484  64.635  1.00 27.49  ? 143 ASN A C   1 
ATOM   1093  O  O   . ASN A  1 143 ? 77.705  64.733  64.446  1.00 32.97  ? 143 ASN A O   1 
ATOM   1094  C  CB  . ASN A  1 143 ? 74.947  66.076  65.548  1.00 24.91  ? 143 ASN A CB  1 
ATOM   1095  C  CG  . ASN A  1 143 ? 75.987  66.929  66.263  1.00 26.36  ? 143 ASN A CG  1 
ATOM   1096  O  OD1 . ASN A  1 143 ? 76.828  67.533  65.614  1.00 25.88  ? 143 ASN A OD1 1 
ATOM   1097  N  ND2 . ASN A  1 143 ? 75.923  67.021  67.587  1.00 26.32  ? 143 ASN A ND2 1 
ATOM   1098  N  N   . THR A  1 144 ? 76.077  63.302  65.011  1.00 30.70  ? 144 THR A N   1 
ATOM   1099  C  CA  . THR A  1 144 ? 76.978  62.237  65.404  1.00 30.14  ? 144 THR A CA  1 
ATOM   1100  C  C   . THR A  1 144 ? 77.894  61.800  64.270  1.00 28.72  ? 144 THR A C   1 
ATOM   1101  O  O   . THR A  1 144 ? 79.117  61.760  64.434  1.00 33.23  ? 144 THR A O   1 
ATOM   1102  C  CB  . THR A  1 144 ? 76.201  61.030  65.923  1.00 33.24  ? 144 THR A CB  1 
ATOM   1103  O  OG1 . THR A  1 144 ? 75.419  61.393  67.084  1.00 42.51  ? 144 THR A OG1 1 
ATOM   1104  C  CG2 . THR A  1 144 ? 77.152  59.942  66.280  1.00 34.77  ? 144 THR A CG2 1 
ATOM   1105  N  N   . THR A  1 145 ? 77.316  61.513  63.110  1.00 26.46  ? 145 THR A N   1 
ATOM   1106  C  CA  . THR A  1 145 ? 78.100  61.098  61.963  1.00 23.19  ? 145 THR A CA  1 
ATOM   1107  C  C   . THR A  1 145 ? 79.158  62.123  61.673  1.00 24.67  ? 145 THR A C   1 
ATOM   1108  O  O   . THR A  1 145 ? 80.341  61.800  61.560  1.00 25.48  ? 145 THR A O   1 
ATOM   1109  C  CB  . THR A  1 145 ? 77.251  60.998  60.780  1.00 21.60  ? 145 THR A CB  1 
ATOM   1110  O  OG1 . THR A  1 145 ? 76.075  60.265  61.149  1.00 26.99  ? 145 THR A OG1 1 
ATOM   1111  C  CG2 . THR A  1 145 ? 78.006  60.312  59.671  1.00 12.85  ? 145 THR A CG2 1 
ATOM   1112  N  N   . LEU A  1 146 ? 78.750  63.373  61.590  1.00 22.65  ? 146 LEU A N   1 
ATOM   1113  C  CA  . LEU A  1 146 ? 79.732  64.379  61.345  1.00 21.61  ? 146 LEU A CA  1 
ATOM   1114  C  C   . LEU A  1 146 ? 80.867  64.338  62.404  1.00 24.89  ? 146 LEU A C   1 
ATOM   1115  O  O   . LEU A  1 146 ? 82.031  64.498  62.064  1.00 28.21  ? 146 LEU A O   1 
ATOM   1116  C  CB  . LEU A  1 146 ? 79.060  65.721  61.280  1.00 20.67  ? 146 LEU A CB  1 
ATOM   1117  C  CG  . LEU A  1 146 ? 79.945  66.857  60.766  1.00 17.59  ? 146 LEU A CG  1 
ATOM   1118  C  CD1 . LEU A  1 146 ? 80.527  66.568  59.414  1.00 12.58  ? 146 LEU A CD1 1 
ATOM   1119  C  CD2 . LEU A  1 146 ? 79.076  68.092  60.690  1.00 18.61  ? 146 LEU A CD2 1 
ATOM   1120  N  N   . SER A  1 147 ? 80.560  64.047  63.665  1.00 26.43  ? 147 SER A N   1 
ATOM   1121  C  CA  . SER A  1 147 ? 81.627  63.997  64.686  1.00 30.79  ? 147 SER A CA  1 
ATOM   1122  C  C   . SER A  1 147 ? 82.542  62.824  64.418  1.00 31.96  ? 147 SER A C   1 
ATOM   1123  O  O   . SER A  1 147 ? 83.759  62.981  64.342  1.00 37.77  ? 147 SER A O   1 
ATOM   1124  C  CB  . SER A  1 147 ? 81.078  63.854  66.095  1.00 31.58  ? 147 SER A CB  1 
ATOM   1125  O  OG  . SER A  1 147 ? 79.791  64.448  66.180  1.00 48.83  ? 147 SER A OG  1 
ATOM   1126  N  N   . HIS A  1 148 ? 81.976  61.634  64.308  1.00 24.89  ? 148 HIS A N   1 
ATOM   1127  C  CA  . HIS A  1 148 ? 82.786  60.505  64.000  1.00 23.80  ? 148 HIS A CA  1 
ATOM   1128  C  C   . HIS A  1 148 ? 83.717  60.790  62.858  1.00 24.09  ? 148 HIS A C   1 
ATOM   1129  O  O   . HIS A  1 148 ? 84.867  60.406  62.866  1.00 24.92  ? 148 HIS A O   1 
ATOM   1130  C  CB  . HIS A  1 148 ? 81.924  59.345  63.617  1.00 32.72  ? 148 HIS A CB  1 
ATOM   1131  C  CG  . HIS A  1 148 ? 81.431  58.565  64.789  1.00 36.02  ? 148 HIS A CG  1 
ATOM   1132  N  ND1 . HIS A  1 148 ? 81.274  57.195  64.762  1.00 40.45  ? 148 HIS A ND1 1 
ATOM   1133  C  CD2 . HIS A  1 148 ? 81.018  58.965  66.010  1.00 34.23  ? 148 HIS A CD2 1 
ATOM   1134  C  CE1 . HIS A  1 148 ? 80.773  56.787  65.913  1.00 34.75  ? 148 HIS A CE1 1 
ATOM   1135  N  NE2 . HIS A  1 148 ? 80.610  57.841  66.690  1.00 36.68  ? 148 HIS A NE2 1 
ATOM   1136  N  N   . TYR A  1 149 ? 83.233  61.496  61.864  1.00 28.54  ? 149 TYR A N   1 
ATOM   1137  C  CA  . TYR A  1 149 ? 84.095  61.768  60.746  1.00 28.91  ? 149 TYR A CA  1 
ATOM   1138  C  C   . TYR A  1 149 ? 85.222  62.651  61.199  1.00 28.29  ? 149 TYR A C   1 
ATOM   1139  O  O   . TYR A  1 149 ? 86.374  62.462  60.801  1.00 32.45  ? 149 TYR A O   1 
ATOM   1140  C  CB  . TYR A  1 149 ? 83.342  62.462  59.630  1.00 25.74  ? 149 TYR A CB  1 
ATOM   1141  C  CG  . TYR A  1 149 ? 84.251  62.884  58.505  1.00 25.89  ? 149 TYR A CG  1 
ATOM   1142  C  CD1 . TYR A  1 149 ? 84.950  61.936  57.759  1.00 22.63  ? 149 TYR A CD1 1 
ATOM   1143  C  CD2 . TYR A  1 149 ? 84.424  64.243  58.186  1.00 23.20  ? 149 TYR A CD2 1 
ATOM   1144  C  CE1 . TYR A  1 149 ? 85.820  62.326  56.711  1.00 21.28  ? 149 TYR A CE1 1 
ATOM   1145  C  CE2 . TYR A  1 149 ? 85.296  64.648  57.122  1.00 21.90  ? 149 TYR A CE2 1 
ATOM   1146  C  CZ  . TYR A  1 149 ? 85.986  63.677  56.405  1.00 21.68  ? 149 TYR A CZ  1 
ATOM   1147  O  OH  . TYR A  1 149 ? 86.856  64.058  55.416  1.00 21.77  ? 149 TYR A OH  1 
ATOM   1148  N  N   . GLU A  1 150 ? 84.871  63.656  61.971  1.00 27.96  ? 150 GLU A N   1 
ATOM   1149  C  CA  . GLU A  1 150 ? 85.861  64.600  62.449  1.00 37.07  ? 150 GLU A CA  1 
ATOM   1150  C  C   . GLU A  1 150 ? 86.917  63.910  63.302  1.00 39.43  ? 150 GLU A C   1 
ATOM   1151  O  O   . GLU A  1 150 ? 88.057  64.351  63.366  1.00 43.16  ? 150 GLU A O   1 
ATOM   1152  C  CB  . GLU A  1 150 ? 85.205  65.678  63.313  1.00 42.67  ? 150 GLU A CB  1 
ATOM   1153  C  CG  . GLU A  1 150 ? 84.248  66.660  62.662  1.00 49.62  ? 150 GLU A CG  1 
ATOM   1154  C  CD  . GLU A  1 150 ? 83.578  67.564  63.707  1.00 57.97  ? 150 GLU A CD  1 
ATOM   1155  O  OE1 . GLU A  1 150 ? 82.728  67.084  64.497  1.00 60.32  ? 150 GLU A OE1 1 
ATOM   1156  O  OE2 . GLU A  1 150 ? 83.918  68.759  63.757  1.00 63.55  ? 150 GLU A OE2 1 
ATOM   1157  N  N   . LEU A  1 151 ? 86.532  62.838  63.977  1.00 39.79  ? 151 LEU A N   1 
ATOM   1158  C  CA  . LEU A  1 151 ? 87.465  62.154  64.844  1.00 36.74  ? 151 LEU A CA  1 
ATOM   1159  C  C   . LEU A  1 151 ? 88.205  61.006  64.203  1.00 35.92  ? 151 LEU A C   1 
ATOM   1160  O  O   . LEU A  1 151 ? 89.139  60.498  64.788  1.00 36.23  ? 151 LEU A O   1 
ATOM   1161  C  CB  . LEU A  1 151 ? 86.721  61.703  66.092  1.00 38.35  ? 151 LEU A CB  1 
ATOM   1162  C  CG  . LEU A  1 151 ? 86.018  62.907  66.744  1.00 42.05  ? 151 LEU A CG  1 
ATOM   1163  C  CD1 . LEU A  1 151 ? 85.138  62.530  67.918  1.00 38.07  ? 151 LEU A CD1 1 
ATOM   1164  C  CD2 . LEU A  1 151 ? 87.046  63.886  67.193  1.00 43.22  ? 151 LEU A CD2 1 
ATOM   1165  N  N   . SER A  1 152 ? 87.786  60.586  63.015  1.00 39.30  ? 152 SER A N   1 
ATOM   1166  C  CA  . SER A  1 152 ? 88.457  59.488  62.350  1.00 45.04  ? 152 SER A CA  1 
ATOM   1167  C  C   . SER A  1 152 ? 89.929  59.727  62.479  1.00 45.34  ? 152 SER A C   1 
ATOM   1168  O  O   . SER A  1 152 ? 90.412  60.842  62.286  1.00 45.84  ? 152 SER A O   1 
ATOM   1169  C  CB  . SER A  1 152 ? 88.058  59.315  60.861  1.00 50.06  ? 152 SER A CB  1 
ATOM   1170  O  OG  . SER A  1 152 ? 87.150  58.189  60.662  1.00 60.73  ? 152 SER A OG  1 
ATOM   1171  N  N   . PRO A  1 153 ? 90.606  58.753  63.082  1.00 48.65  ? 153 PRO A N   1 
ATOM   1172  C  CA  . PRO A  1 153 ? 92.049  58.731  63.323  1.00 51.60  ? 153 PRO A CA  1 
ATOM   1173  C  C   . PRO A  1 153 ? 92.828  58.888  61.999  1.00 54.63  ? 153 PRO A C   1 
ATOM   1174  O  O   . PRO A  1 153 ? 93.938  59.427  61.948  1.00 61.25  ? 153 PRO A O   1 
ATOM   1175  C  CB  . PRO A  1 153 ? 92.256  57.359  63.979  1.00 48.16  ? 153 PRO A CB  1 
ATOM   1176  C  CG  . PRO A  1 153 ? 90.993  56.589  63.651  1.00 46.64  ? 153 PRO A CG  1 
ATOM   1177  C  CD  . PRO A  1 153 ? 89.951  57.626  63.769  1.00 44.96  ? 153 PRO A CD  1 
ATOM   1178  N  N   . LYS A  1 154 ? 92.275  58.329  60.943  1.00 53.75  ? 154 LYS A N   1 
ATOM   1179  C  CA  . LYS A  1 154 ? 92.838  58.461  59.614  1.00 54.49  ? 154 LYS A CA  1 
ATOM   1180  C  C   . LYS A  1 154 ? 91.955  59.658  59.319  1.00 54.16  ? 154 LYS A C   1 
ATOM   1181  O  O   . LYS A  1 154 ? 90.722  59.536  59.303  1.00 55.56  ? 154 LYS A O   1 
ATOM   1182  C  CB  . LYS A  1 154 ? 92.419  57.250  58.768  1.00 61.95  ? 154 LYS A CB  1 
ATOM   1183  C  CG  . LYS A  1 154 ? 90.993  56.668  59.140  1.00 73.75  ? 154 LYS A CG  1 
ATOM   1184  C  CD  . LYS A  1 154 ? 90.823  55.136  58.888  1.00 80.63  ? 154 LYS A CD  1 
ATOM   1185  C  CE  . LYS A  1 154 ? 89.885  54.454  59.941  1.00 90.49  ? 154 LYS A CE  1 
ATOM   1186  N  NZ  . LYS A  1 154 ? 88.378  54.765  59.903  1.00 96.21  ? 154 LYS A NZ  1 
ATOM   1187  N  N   . LYS A  1 155 ? 92.537  60.841  59.298  1.00 51.59  ? 155 LYS A N   1 
ATOM   1188  C  CA  . LYS A  1 155 ? 91.728  62.024  59.060  1.00 55.04  ? 155 LYS A CA  1 
ATOM   1189  C  C   . LYS A  1 155 ? 91.422  62.220  57.587  1.00 50.52  ? 155 LYS A C   1 
ATOM   1190  O  O   . LYS A  1 155 ? 92.298  62.059  56.725  1.00 48.74  ? 155 LYS A O   1 
ATOM   1191  C  CB  . LYS A  1 155 ? 92.353  63.282  59.670  1.00 64.95  ? 155 LYS A CB  1 
ATOM   1192  C  CG  . LYS A  1 155 ? 93.864  63.241  59.794  1.00 84.45  ? 155 LYS A CG  1 
ATOM   1193  C  CD  . LYS A  1 155 ? 94.580  62.916  58.453  1.00 101.90 ? 155 LYS A CD  1 
ATOM   1194  C  CE  . LYS A  1 155 ? 96.137  62.857  58.588  1.00 111.12 ? 155 LYS A CE  1 
ATOM   1195  N  NZ  . LYS A  1 155 ? 96.651  61.839  59.580  1.00 118.52 ? 155 LYS A NZ  1 
ATOM   1196  N  N   . GLY A  1 156 ? 90.150  62.496  57.312  1.00 46.43  ? 156 GLY A N   1 
ATOM   1197  C  CA  . GLY A  1 156 ? 89.706  62.724  55.947  1.00 40.84  ? 156 GLY A CA  1 
ATOM   1198  C  C   . GLY A  1 156 ? 90.217  64.059  55.448  1.00 34.98  ? 156 GLY A C   1 
ATOM   1199  O  O   . GLY A  1 156 ? 90.383  64.975  56.242  1.00 37.54  ? 156 GLY A O   1 
ATOM   1200  N  N   . GLN A  1 157 ? 90.409  64.202  54.143  1.00 29.36  ? 157 GLN A N   1 
ATOM   1201  C  CA  . GLN A  1 157 ? 90.937  65.434  53.595  1.00 25.66  ? 157 GLN A CA  1 
ATOM   1202  C  C   . GLN A  1 157 ? 90.055  66.164  52.619  1.00 24.97  ? 157 GLN A C   1 
ATOM   1203  O  O   . GLN A  1 157 ? 90.434  67.236  52.144  1.00 26.65  ? 157 GLN A O   1 
ATOM   1204  C  CB  . GLN A  1 157 ? 92.252  65.149  52.912  1.00 28.25  ? 157 GLN A CB  1 
ATOM   1205  C  CG  . GLN A  1 157 ? 93.325  64.668  53.855  1.00 38.18  ? 157 GLN A CG  1 
ATOM   1206  C  CD  . GLN A  1 157 ? 94.600  64.256  53.129  1.00 45.72  ? 157 GLN A CD  1 
ATOM   1207  O  OE1 . GLN A  1 157 ? 95.576  64.997  53.064  1.00 52.95  ? 157 GLN A OE1 1 
ATOM   1208  N  NE2 . GLN A  1 157 ? 94.593  63.058  52.589  1.00 56.91  ? 157 GLN A NE2 1 
ATOM   1209  N  N   . THR A  1 158 ? 88.904  65.571  52.318  1.00 23.62  ? 158 THR A N   1 
ATOM   1210  C  CA  . THR A  1 158 ? 87.897  66.104  51.384  1.00 20.86  ? 158 THR A CA  1 
ATOM   1211  C  C   . THR A  1 158 ? 86.716  65.147  51.496  1.00 25.77  ? 158 THR A C   1 
ATOM   1212  O  O   . THR A  1 158 ? 86.917  63.926  51.504  1.00 32.29  ? 158 THR A O   1 
ATOM   1213  C  CB  . THR A  1 158 ? 88.373  66.005  49.953  1.00 17.01  ? 158 THR A CB  1 
ATOM   1214  O  OG1 . THR A  1 158 ? 89.441  66.932  49.739  1.00 13.08  ? 158 THR A OG1 1 
ATOM   1215  C  CG2 . THR A  1 158 ? 87.247  66.262  48.979  1.00 19.92  ? 158 THR A CG2 1 
ATOM   1216  N  N   . VAL A  1 159 ? 85.500  65.667  51.622  1.00 20.65  ? 159 VAL A N   1 
ATOM   1217  C  CA  . VAL A  1 159 ? 84.351  64.779  51.720  1.00 14.29  ? 159 VAL A CA  1 
ATOM   1218  C  C   . VAL A  1 159 ? 83.708  64.651  50.368  1.00 18.70  ? 159 VAL A C   1 
ATOM   1219  O  O   . VAL A  1 159 ? 83.625  65.623  49.651  1.00 26.67  ? 159 VAL A O   1 
ATOM   1220  C  CB  . VAL A  1 159 ? 83.331  65.351  52.630  1.00 14.61  ? 159 VAL A CB  1 
ATOM   1221  C  CG1 . VAL A  1 159 ? 82.077  64.521  52.570  1.00 10.83  ? 159 VAL A CG1 1 
ATOM   1222  C  CG2 . VAL A  1 159 ? 83.898  65.398  54.051  1.00 13.54  ? 159 VAL A CG2 1 
ATOM   1223  N  N   . LEU A  1 160 ? 83.353  63.443  49.957  1.00 16.26  ? 160 LEU A N   1 
ATOM   1224  C  CA  . LEU A  1 160 ? 82.673  63.293  48.691  1.00 15.11  ? 160 LEU A CA  1 
ATOM   1225  C  C   . LEU A  1 160 ? 81.219  63.122  49.178  1.00 17.58  ? 160 LEU A C   1 
ATOM   1226  O  O   . LEU A  1 160 ? 80.934  62.208  49.944  1.00 17.05  ? 160 LEU A O   1 
ATOM   1227  C  CB  . LEU A  1 160 ? 83.208  62.087  47.917  1.00 11.72  ? 160 LEU A CB  1 
ATOM   1228  C  CG  . LEU A  1 160 ? 84.709  62.177  47.587  1.00 13.98  ? 160 LEU A CG  1 
ATOM   1229  C  CD1 . LEU A  1 160 ? 85.166  60.919  46.937  1.00 13.40  ? 160 LEU A CD1 1 
ATOM   1230  C  CD2 . LEU A  1 160 ? 85.069  63.325  46.684  1.00 17.65  ? 160 LEU A CD2 1 
ATOM   1231  N  N   . PHE A  1 161 ? 80.380  64.116  48.885  1.00 17.45  ? 161 PHE A N   1 
ATOM   1232  C  CA  . PHE A  1 161 ? 79.015  64.145  49.331  1.00 13.77  ? 161 PHE A CA  1 
ATOM   1233  C  C   . PHE A  1 161 ? 78.133  63.623  48.257  1.00 15.39  ? 161 PHE A C   1 
ATOM   1234  O  O   . PHE A  1 161 ? 77.935  64.222  47.231  1.00 24.06  ? 161 PHE A O   1 
ATOM   1235  C  CB  . PHE A  1 161 ? 78.597  65.551  49.701  1.00 9.94   ? 161 PHE A CB  1 
ATOM   1236  C  CG  . PHE A  1 161 ? 77.350  65.591  50.450  1.00 12.11  ? 161 PHE A CG  1 
ATOM   1237  C  CD1 . PHE A  1 161 ? 76.137  65.602  49.806  1.00 19.71  ? 161 PHE A CD1 1 
ATOM   1238  C  CD2 . PHE A  1 161 ? 77.365  65.530  51.808  1.00 9.37   ? 161 PHE A CD2 1 
ATOM   1239  C  CE1 . PHE A  1 161 ? 74.965  65.564  50.528  1.00 16.96  ? 161 PHE A CE1 1 
ATOM   1240  C  CE2 . PHE A  1 161 ? 76.197  65.494  52.520  1.00 11.31  ? 161 PHE A CE2 1 
ATOM   1241  C  CZ  . PHE A  1 161 ? 75.002  65.503  51.882  1.00 11.43  ? 161 PHE A CZ  1 
ATOM   1242  N  N   . VAL A  1 162 ? 77.363  62.642  48.631  1.00 21.59  ? 162 VAL A N   1 
ATOM   1243  C  CA  . VAL A  1 162 ? 76.541  61.941  47.686  1.00 12.45  ? 162 VAL A CA  1 
ATOM   1244  C  C   . VAL A  1 162 ? 75.082  62.376  47.553  1.00 12.39  ? 162 VAL A C   1 
ATOM   1245  O  O   . VAL A  1 162 ? 74.231  61.664  47.022  1.00 18.21  ? 162 VAL A O   1 
ATOM   1246  C  CB  . VAL A  1 162 ? 76.845  60.458  48.011  1.00 11.07  ? 162 VAL A CB  1 
ATOM   1247  C  CG1 . VAL A  1 162 ? 75.670  59.622  48.248  1.00 12.77  ? 162 VAL A CG1 1 
ATOM   1248  C  CG2 . VAL A  1 162 ? 77.747  59.931  46.983  1.00 16.35  ? 162 VAL A CG2 1 
ATOM   1249  N  N   . GLY A  1 163 ? 74.745  63.563  47.995  1.00 9.72   ? 163 GLY A N   1 
ATOM   1250  C  CA  . GLY A  1 163 ? 73.375  63.965  47.775  1.00 11.79  ? 163 GLY A CA  1 
ATOM   1251  C  C   . GLY A  1 163 ? 72.496  64.000  48.979  1.00 13.25  ? 163 GLY A C   1 
ATOM   1252  O  O   . GLY A  1 163 ? 72.717  63.275  49.926  1.00 15.05  ? 163 GLY A O   1 
ATOM   1253  N  N   . ASP A  1 164 ? 71.404  64.739  48.845  1.00 16.68  ? 164 ASP A N   1 
ATOM   1254  C  CA  . ASP A  1 164 ? 70.427  64.996  49.905  1.00 22.06  ? 164 ASP A CA  1 
ATOM   1255  C  C   . ASP A  1 164 ? 71.142  65.733  51.007  1.00 27.72  ? 164 ASP A C   1 
ATOM   1256  O  O   . ASP A  1 164 ? 71.688  65.134  51.914  1.00 30.84  ? 164 ASP A O   1 
ATOM   1257  C  CB  . ASP A  1 164 ? 69.719  63.741  50.414  1.00 23.69  ? 164 ASP A CB  1 
ATOM   1258  C  CG  . ASP A  1 164 ? 68.752  63.161  49.381  1.00 30.91  ? 164 ASP A CG  1 
ATOM   1259  O  OD1 . ASP A  1 164 ? 68.700  63.633  48.223  1.00 39.46  ? 164 ASP A OD1 1 
ATOM   1260  O  OD2 . ASP A  1 164 ? 68.207  62.103  49.606  1.00 25.78  ? 164 ASP A OD2 1 
ATOM   1261  N  N   . LEU A  1 165 ? 71.211  67.052  50.878  1.00 28.18  ? 165 LEU A N   1 
ATOM   1262  C  CA  . LEU A  1 165 ? 71.926  67.804  51.872  1.00 25.28  ? 165 LEU A CA  1 
ATOM   1263  C  C   . LEU A  1 165 ? 71.179  68.100  53.153  1.00 26.06  ? 165 LEU A C   1 
ATOM   1264  O  O   . LEU A  1 165 ? 71.524  67.544  54.178  1.00 26.83  ? 165 LEU A O   1 
ATOM   1265  C  CB  . LEU A  1 165 ? 72.448  69.093  51.261  1.00 23.18  ? 165 LEU A CB  1 
ATOM   1266  C  CG  . LEU A  1 165 ? 73.540  68.941  50.238  1.00 20.44  ? 165 LEU A CG  1 
ATOM   1267  C  CD1 . LEU A  1 165 ? 73.029  68.364  48.952  1.00 22.79  ? 165 LEU A CD1 1 
ATOM   1268  C  CD2 . LEU A  1 165 ? 74.048  70.282  49.993  1.00 22.20  ? 165 LEU A CD2 1 
ATOM   1269  N  N   . SER A  1 166 ? 70.086  68.866  53.080  1.00 25.82  ? 166 SER A N   1 
ATOM   1270  C  CA  . SER A  1 166 ? 69.442  69.272  54.315  1.00 21.81  ? 166 SER A CA  1 
ATOM   1271  C  C   . SER A  1 166 ? 68.050  68.873  54.618  1.00 17.13  ? 166 SER A C   1 
ATOM   1272  O  O   . SER A  1 166 ? 67.555  69.196  55.669  1.00 16.79  ? 166 SER A O   1 
ATOM   1273  C  CB  . SER A  1 166 ? 69.496  70.778  54.414  1.00 21.26  ? 166 SER A CB  1 
ATOM   1274  O  OG  . SER A  1 166 ? 68.593  71.302  53.482  1.00 36.65  ? 166 SER A OG  1 
ATOM   1275  N  N   . TYR A  1 167 ? 67.336  68.348  53.641  1.00 20.54  ? 167 TYR A N   1 
ATOM   1276  C  CA  . TYR A  1 167 ? 65.959  67.940  53.912  1.00 17.75  ? 167 TYR A CA  1 
ATOM   1277  C  C   . TYR A  1 167 ? 65.026  69.058  54.293  1.00 18.98  ? 167 TYR A C   1 
ATOM   1278  O  O   . TYR A  1 167 ? 64.045  68.813  54.999  1.00 21.27  ? 167 TYR A O   1 
ATOM   1279  C  CB  . TYR A  1 167 ? 65.954  66.920  55.008  1.00 12.40  ? 167 TYR A CB  1 
ATOM   1280  C  CG  . TYR A  1 167 ? 66.498  65.653  54.467  1.00 17.29  ? 167 TYR A CG  1 
ATOM   1281  C  CD1 . TYR A  1 167 ? 67.863  65.429  54.385  1.00 11.86  ? 167 TYR A CD1 1 
ATOM   1282  C  CD2 . TYR A  1 167 ? 65.647  64.681  53.999  1.00 21.81  ? 167 TYR A CD2 1 
ATOM   1283  C  CE1 . TYR A  1 167 ? 68.345  64.270  53.838  1.00 12.51  ? 167 TYR A CE1 1 
ATOM   1284  C  CE2 . TYR A  1 167 ? 66.133  63.513  53.451  1.00 20.83  ? 167 TYR A CE2 1 
ATOM   1285  C  CZ  . TYR A  1 167 ? 67.469  63.309  53.393  1.00 17.73  ? 167 TYR A CZ  1 
ATOM   1286  O  OH  . TYR A  1 167 ? 67.959  62.089  53.079  1.00 21.04  ? 167 TYR A OH  1 
ATOM   1287  N  N   . ALA A  1 168 ? 65.335  70.284  53.853  1.00 17.68  ? 168 ALA A N   1 
ATOM   1288  C  CA  . ALA A  1 168 ? 64.479  71.424  54.169  1.00 17.99  ? 168 ALA A CA  1 
ATOM   1289  C  C   . ALA A  1 168 ? 63.134  71.216  53.488  1.00 17.64  ? 168 ALA A C   1 
ATOM   1290  O  O   . ALA A  1 168 ? 62.099  71.637  53.970  1.00 18.30  ? 168 ALA A O   1 
ATOM   1291  C  CB  . ALA A  1 168 ? 65.116  72.708  53.690  1.00 11.50  ? 168 ALA A CB  1 
ATOM   1292  N  N   . ASP A  1 169 ? 63.133  70.497  52.392  1.00 19.46  ? 169 ASP A N   1 
ATOM   1293  C  CA  . ASP A  1 169 ? 61.890  70.287  51.699  1.00 24.03  ? 169 ASP A CA  1 
ATOM   1294  C  C   . ASP A  1 169 ? 60.855  69.454  52.456  1.00 29.79  ? 169 ASP A C   1 
ATOM   1295  O  O   . ASP A  1 169 ? 59.732  69.257  51.973  1.00 38.00  ? 169 ASP A O   1 
ATOM   1296  C  CB  . ASP A  1 169 ? 62.149  69.688  50.322  1.00 23.73  ? 169 ASP A CB  1 
ATOM   1297  C  CG  . ASP A  1 169 ? 62.811  68.329  50.382  1.00 26.52  ? 169 ASP A CG  1 
ATOM   1298  O  OD1 . ASP A  1 169 ? 63.609  68.092  51.304  1.00 36.39  ? 169 ASP A OD1 1 
ATOM   1299  O  OD2 . ASP A  1 169 ? 62.564  67.504  49.478  1.00 27.13  ? 169 ASP A OD2 1 
ATOM   1300  N  N   . ARG A  1 170 ? 61.231  68.914  53.607  1.00 30.97  ? 170 ARG A N   1 
ATOM   1301  C  CA  . ARG A  1 170 ? 60.301  68.106  54.395  1.00 27.98  ? 170 ARG A CA  1 
ATOM   1302  C  C   . ARG A  1 170 ? 59.473  69.051  55.225  1.00 29.83  ? 170 ARG A C   1 
ATOM   1303  O  O   . ARG A  1 170 ? 58.408  68.697  55.744  1.00 28.52  ? 170 ARG A O   1 
ATOM   1304  C  CB  . ARG A  1 170 ? 61.056  67.200  55.335  1.00 29.52  ? 170 ARG A CB  1 
ATOM   1305  C  CG  . ARG A  1 170 ? 62.122  66.398  54.649  1.00 45.56  ? 170 ARG A CG  1 
ATOM   1306  C  CD  . ARG A  1 170 ? 62.679  65.346  55.550  1.00 47.93  ? 170 ARG A CD  1 
ATOM   1307  N  NE  . ARG A  1 170 ? 61.594  64.462  55.916  1.00 49.28  ? 170 ARG A NE  1 
ATOM   1308  C  CZ  . ARG A  1 170 ? 61.043  64.470  57.120  1.00 55.03  ? 170 ARG A CZ  1 
ATOM   1309  N  NH1 . ARG A  1 170 ? 61.509  65.326  58.065  1.00 52.33  ? 170 ARG A NH1 1 
ATOM   1310  N  NH2 . ARG A  1 170 ? 60.019  63.644  57.356  1.00 59.68  ? 170 ARG A NH2 1 
ATOM   1311  N  N   . TYR A  1 171 ? 60.019  70.243  55.415  1.00 28.12  ? 171 TYR A N   1 
ATOM   1312  C  CA  . TYR A  1 171 ? 59.351  71.258  56.171  1.00 26.36  ? 171 TYR A CA  1 
ATOM   1313  C  C   . TYR A  1 171 ? 58.313  71.891  55.285  1.00 29.31  ? 171 TYR A C   1 
ATOM   1314  O  O   . TYR A  1 171 ? 58.337  71.769  54.067  1.00 35.46  ? 171 TYR A O   1 
ATOM   1315  C  CB  . TYR A  1 171 ? 60.360  72.275  56.633  1.00 21.68  ? 171 TYR A CB  1 
ATOM   1316  C  CG  . TYR A  1 171 ? 61.242  71.692  57.678  1.00 29.12  ? 171 TYR A CG  1 
ATOM   1317  C  CD1 . TYR A  1 171 ? 60.867  71.744  59.010  1.00 33.96  ? 171 TYR A CD1 1 
ATOM   1318  C  CD2 . TYR A  1 171 ? 62.416  71.021  57.349  1.00 32.40  ? 171 TYR A CD2 1 
ATOM   1319  C  CE1 . TYR A  1 171 ? 61.611  71.158  60.006  1.00 30.37  ? 171 TYR A CE1 1 
ATOM   1320  C  CE2 . TYR A  1 171 ? 63.187  70.413  58.345  1.00 34.01  ? 171 TYR A CE2 1 
ATOM   1321  C  CZ  . TYR A  1 171 ? 62.761  70.493  59.689  1.00 35.13  ? 171 TYR A CZ  1 
ATOM   1322  O  OH  . TYR A  1 171 ? 63.461  69.927  60.746  1.00 32.03  ? 171 TYR A OH  1 
ATOM   1323  N  N   . PRO A  1 172 ? 57.327  72.519  55.889  1.00 29.78  ? 172 PRO A N   1 
ATOM   1324  C  CA  . PRO A  1 172 ? 56.297  73.155  55.069  1.00 31.21  ? 172 PRO A CA  1 
ATOM   1325  C  C   . PRO A  1 172 ? 56.867  74.321  54.232  1.00 32.67  ? 172 PRO A C   1 
ATOM   1326  O  O   . PRO A  1 172 ? 57.730  75.086  54.690  1.00 30.15  ? 172 PRO A O   1 
ATOM   1327  C  CB  . PRO A  1 172 ? 55.271  73.600  56.112  1.00 27.89  ? 172 PRO A CB  1 
ATOM   1328  C  CG  . PRO A  1 172 ? 56.056  73.763  57.341  1.00 25.58  ? 172 PRO A CG  1 
ATOM   1329  C  CD  . PRO A  1 172 ? 57.049  72.657  57.326  1.00 25.04  ? 172 PRO A CD  1 
ATOM   1330  N  N   . ASN A  1 173 ? 56.394  74.431  52.994  1.00 33.39  ? 173 ASN A N   1 
ATOM   1331  C  CA  . ASN A  1 173 ? 56.868  75.466  52.070  1.00 30.11  ? 173 ASN A CA  1 
ATOM   1332  C  C   . ASN A  1 173 ? 58.401  75.405  52.000  1.00 27.36  ? 173 ASN A C   1 
ATOM   1333  O  O   . ASN A  1 173 ? 59.087  76.424  51.748  1.00 25.94  ? 173 ASN A O   1 
ATOM   1334  C  CB  . ASN A  1 173 ? 56.416  76.868  52.495  1.00 36.41  ? 173 ASN A CB  1 
ATOM   1335  C  CG  . ASN A  1 173 ? 54.905  76.985  52.698  1.00 39.86  ? 173 ASN A CG  1 
ATOM   1336  O  OD1 . ASN A  1 173 ? 54.475  77.649  53.634  1.00 48.89  ? 173 ASN A OD1 1 
ATOM   1337  N  ND2 . ASN A  1 173 ? 54.099  76.374  51.821  1.00 44.28  ? 173 ASN A ND2 1 
ATOM   1338  N  N   . HIS A  1 174 ? 58.911  74.181  52.190  1.00 18.74  ? 174 HIS A N   1 
ATOM   1339  C  CA  . HIS A  1 174 ? 60.337  73.903  52.176  1.00 17.23  ? 174 HIS A CA  1 
ATOM   1340  C  C   . HIS A  1 174 ? 61.117  74.849  53.043  1.00 17.35  ? 174 HIS A C   1 
ATOM   1341  O  O   . HIS A  1 174 ? 62.286  75.055  52.791  1.00 23.80  ? 174 HIS A O   1 
ATOM   1342  C  CB  . HIS A  1 174 ? 60.881  74.012  50.746  1.00 13.31  ? 174 HIS A CB  1 
ATOM   1343  C  CG  . HIS A  1 174 ? 60.201  73.107  49.777  1.00 17.81  ? 174 HIS A CG  1 
ATOM   1344  N  ND1 . HIS A  1 174 ? 60.849  72.560  48.687  1.00 20.75  ? 174 HIS A ND1 1 
ATOM   1345  C  CD2 . HIS A  1 174 ? 58.917  72.674  49.711  1.00 15.81  ? 174 HIS A CD2 1 
ATOM   1346  C  CE1 . HIS A  1 174 ? 59.993  71.833  47.987  1.00 24.85  ? 174 HIS A CE1 1 
ATOM   1347  N  NE2 . HIS A  1 174 ? 58.811  71.888  48.585  1.00 19.63  ? 174 HIS A NE2 1 
ATOM   1348  N  N   . ASP A  1 175 ? 60.483  75.364  54.081  1.00 19.14  ? 175 ASP A N   1 
ATOM   1349  C  CA  . ASP A  1 175 ? 61.065  76.346  54.965  1.00 18.16  ? 175 ASP A CA  1 
ATOM   1350  C  C   . ASP A  1 175 ? 62.520  76.505  54.789  1.00 18.55  ? 175 ASP A C   1 
ATOM   1351  O  O   . ASP A  1 175 ? 63.265  75.810  55.464  1.00 20.04  ? 175 ASP A O   1 
ATOM   1352  C  CB  . ASP A  1 175 ? 60.783  76.000  56.401  1.00 23.07  ? 175 ASP A CB  1 
ATOM   1353  C  CG  . ASP A  1 175 ? 61.041  77.176  57.340  1.00 38.86  ? 175 ASP A CG  1 
ATOM   1354  O  OD1 . ASP A  1 175 ? 61.663  78.157  56.906  1.00 42.89  ? 175 ASP A OD1 1 
ATOM   1355  O  OD2 . ASP A  1 175 ? 60.605  77.148  58.517  1.00 54.37  ? 175 ASP A OD2 1 
ATOM   1356  N  N   . ASN A  1 176 ? 62.944  77.386  53.871  1.00 23.60  ? 176 ASN A N   1 
ATOM   1357  C  CA  . ASN A  1 176 ? 64.394  77.574  53.624  1.00 23.23  ? 176 ASN A CA  1 
ATOM   1358  C  C   . ASN A  1 176 ? 65.262  77.941  54.823  1.00 24.16  ? 176 ASN A C   1 
ATOM   1359  O  O   . ASN A  1 176 ? 66.486  78.046  54.713  1.00 29.37  ? 176 ASN A O   1 
ATOM   1360  C  CB  . ASN A  1 176 ? 64.684  78.524  52.462  1.00 20.42  ? 176 ASN A CB  1 
ATOM   1361  C  CG  . ASN A  1 176 ? 64.474  77.867  51.134  1.00 23.70  ? 176 ASN A CG  1 
ATOM   1362  O  OD1 . ASN A  1 176 ? 65.177  78.160  50.171  1.00 17.48  ? 176 ASN A OD1 1 
ATOM   1363  N  ND2 . ASN A  1 176 ? 63.486  76.968  51.060  1.00 23.75  ? 176 ASN A ND2 1 
ATOM   1364  N  N   . VAL A  1 177 ? 64.667  78.143  55.986  1.00 22.40  ? 177 VAL A N   1 
ATOM   1365  C  CA  . VAL A  1 177 ? 65.515  78.442  57.131  1.00 25.60  ? 177 VAL A CA  1 
ATOM   1366  C  C   . VAL A  1 177 ? 66.324  77.212  57.413  1.00 25.08  ? 177 VAL A C   1 
ATOM   1367  O  O   . VAL A  1 177 ? 67.459  77.315  57.841  1.00 26.85  ? 177 VAL A O   1 
ATOM   1368  C  CB  . VAL A  1 177 ? 64.730  78.755  58.396  1.00 26.46  ? 177 VAL A CB  1 
ATOM   1369  C  CG1 . VAL A  1 177 ? 65.657  78.699  59.605  1.00 24.78  ? 177 VAL A CG1 1 
ATOM   1370  C  CG2 . VAL A  1 177 ? 64.162  80.105  58.280  1.00 12.82  ? 177 VAL A CG2 1 
ATOM   1371  N  N   . ARG A  1 178 ? 65.707  76.054  57.194  1.00 25.05  ? 178 ARG A N   1 
ATOM   1372  C  CA  . ARG A  1 178 ? 66.368  74.802  57.406  1.00 27.26  ? 178 ARG A CA  1 
ATOM   1373  C  C   . ARG A  1 178 ? 67.582  74.623  56.493  1.00 31.23  ? 178 ARG A C   1 
ATOM   1374  O  O   . ARG A  1 178 ? 68.390  73.736  56.714  1.00 33.87  ? 178 ARG A O   1 
ATOM   1375  C  CB  . ARG A  1 178 ? 65.387  73.673  57.297  1.00 25.82  ? 178 ARG A CB  1 
ATOM   1376  C  CG  . ARG A  1 178 ? 64.518  73.551  58.549  1.00 30.02  ? 178 ARG A CG  1 
ATOM   1377  C  CD  . ARG A  1 178 ? 65.347  73.167  59.784  1.00 33.54  ? 178 ARG A CD  1 
ATOM   1378  N  NE  . ARG A  1 178 ? 64.527  72.910  60.970  1.00 35.68  ? 178 ARG A NE  1 
ATOM   1379  C  CZ  . ARG A  1 178 ? 64.997  72.451  62.125  1.00 31.57  ? 178 ARG A CZ  1 
ATOM   1380  N  NH1 . ARG A  1 178 ? 66.287  72.207  62.276  1.00 28.26  ? 178 ARG A NH1 1 
ATOM   1381  N  NH2 . ARG A  1 178 ? 64.156  72.185  63.115  1.00 42.20  ? 178 ARG A NH2 1 
ATOM   1382  N  N   . TRP A  1 179 ? 67.728  75.465  55.472  1.00 29.61  ? 179 TRP A N   1 
ATOM   1383  C  CA  . TRP A  1 179 ? 68.902  75.409  54.627  1.00 26.47  ? 179 TRP A CA  1 
ATOM   1384  C  C   . TRP A  1 179 ? 69.946  76.257  55.330  1.00 27.80  ? 179 TRP A C   1 
ATOM   1385  O  O   . TRP A  1 179 ? 71.129  75.979  55.224  1.00 30.54  ? 179 TRP A O   1 
ATOM   1386  C  CB  . TRP A  1 179 ? 68.657  76.038  53.266  1.00 26.07  ? 179 TRP A CB  1 
ATOM   1387  C  CG  . TRP A  1 179 ? 68.281  75.102  52.212  1.00 20.44  ? 179 TRP A CG  1 
ATOM   1388  C  CD1 . TRP A  1 179 ? 67.070  74.975  51.622  1.00 20.85  ? 179 TRP A CD1 1 
ATOM   1389  C  CD2 . TRP A  1 179 ? 69.140  74.160  51.565  1.00 17.74  ? 179 TRP A CD2 1 
ATOM   1390  N  NE1 . TRP A  1 179 ? 67.111  74.032  50.652  1.00 17.10  ? 179 TRP A NE1 1 
ATOM   1391  C  CE2 . TRP A  1 179 ? 68.381  73.506  50.600  1.00 13.13  ? 179 TRP A CE2 1 
ATOM   1392  C  CE3 . TRP A  1 179 ? 70.480  73.802  51.723  1.00 20.27  ? 179 TRP A CE3 1 
ATOM   1393  C  CZ2 . TRP A  1 179 ? 68.918  72.506  49.780  1.00 14.45  ? 179 TRP A CZ2 1 
ATOM   1394  C  CZ3 . TRP A  1 179 ? 71.021  72.810  50.909  1.00 17.27  ? 179 TRP A CZ3 1 
ATOM   1395  C  CH2 . TRP A  1 179 ? 70.239  72.175  49.953  1.00 16.47  ? 179 TRP A CH2 1 
ATOM   1396  N  N   . ASP A  1 180 ? 69.501  77.317  56.008  1.00 29.44  ? 180 ASP A N   1 
ATOM   1397  C  CA  . ASP A  1 180 ? 70.395  78.234  56.739  1.00 26.48  ? 180 ASP A CA  1 
ATOM   1398  C  C   . ASP A  1 180 ? 70.952  77.495  57.951  1.00 22.82  ? 180 ASP A C   1 
ATOM   1399  O  O   . ASP A  1 180 ? 72.136  77.550  58.204  1.00 27.14  ? 180 ASP A O   1 
ATOM   1400  C  CB  . ASP A  1 180 ? 69.656  79.508  57.198  1.00 24.14  ? 180 ASP A CB  1 
ATOM   1401  C  CG  . ASP A  1 180 ? 69.246  80.439  56.030  1.00 24.35  ? 180 ASP A CG  1 
ATOM   1402  O  OD1 . ASP A  1 180 ? 70.066  80.643  55.105  1.00 20.06  ? 180 ASP A OD1 1 
ATOM   1403  O  OD2 . ASP A  1 180 ? 68.119  80.990  56.068  1.00 26.25  ? 180 ASP A OD2 1 
ATOM   1404  N  N   . THR A  1 181 ? 70.114  76.783  58.693  1.00 17.85  ? 181 THR A N   1 
ATOM   1405  C  CA  . THR A  1 181 ? 70.608  76.043  59.822  1.00 14.54  ? 181 THR A CA  1 
ATOM   1406  C  C   . THR A  1 181 ? 71.592  74.961  59.384  1.00 15.22  ? 181 THR A C   1 
ATOM   1407  O  O   . THR A  1 181 ? 72.658  74.821  59.960  1.00 15.68  ? 181 THR A O   1 
ATOM   1408  C  CB  . THR A  1 181 ? 69.495  75.413  60.586  1.00 15.17  ? 181 THR A CB  1 
ATOM   1409  O  OG1 . THR A  1 181 ? 68.770  74.554  59.713  1.00 20.61  ? 181 THR A OG1 1 
ATOM   1410  C  CG2 . THR A  1 181 ? 68.574  76.451  61.100  1.00 20.53  ? 181 THR A CG2 1 
ATOM   1411  N  N   . TRP A  1 182 ? 71.263  74.204  58.350  1.00 17.56  ? 182 TRP A N   1 
ATOM   1412  C  CA  . TRP A  1 182 ? 72.150  73.150  57.872  1.00 17.77  ? 182 TRP A CA  1 
ATOM   1413  C  C   . TRP A  1 182 ? 73.518  73.710  57.508  1.00 17.95  ? 182 TRP A C   1 
ATOM   1414  O  O   . TRP A  1 182 ? 74.576  73.120  57.794  1.00 19.95  ? 182 TRP A O   1 
ATOM   1415  C  CB  . TRP A  1 182 ? 71.563  72.469  56.636  1.00 13.42  ? 182 TRP A CB  1 
ATOM   1416  C  CG  . TRP A  1 182 ? 72.274  71.178  56.301  1.00 18.31  ? 182 TRP A CG  1 
ATOM   1417  C  CD1 . TRP A  1 182 ? 72.094  69.974  56.904  1.00 14.62  ? 182 TRP A CD1 1 
ATOM   1418  C  CD2 . TRP A  1 182 ? 73.271  70.973  55.280  1.00 14.75  ? 182 TRP A CD2 1 
ATOM   1419  N  NE1 . TRP A  1 182 ? 72.903  69.025  56.316  1.00 20.20  ? 182 TRP A NE1 1 
ATOM   1420  C  CE2 . TRP A  1 182 ? 73.628  69.618  55.315  1.00 14.80  ? 182 TRP A CE2 1 
ATOM   1421  C  CE3 . TRP A  1 182 ? 73.894  71.808  54.349  1.00 15.01  ? 182 TRP A CE3 1 
ATOM   1422  C  CZ2 . TRP A  1 182 ? 74.569  69.076  54.450  1.00 22.70  ? 182 TRP A CZ2 1 
ATOM   1423  C  CZ3 . TRP A  1 182 ? 74.847  71.272  53.483  1.00 20.30  ? 182 TRP A CZ3 1 
ATOM   1424  C  CH2 . TRP A  1 182 ? 75.174  69.921  53.538  1.00 22.94  ? 182 TRP A CH2 1 
ATOM   1425  N  N   . GLY A  1 183 ? 73.496  74.867  56.900  1.00 13.18  ? 183 GLY A N   1 
ATOM   1426  C  CA  . GLY A  1 183 ? 74.751  75.455  56.492  1.00 21.32  ? 183 GLY A CA  1 
ATOM   1427  C  C   . GLY A  1 183 ? 75.627  75.919  57.622  1.00 23.97  ? 183 GLY A C   1 
ATOM   1428  O  O   . GLY A  1 183 ? 76.846  76.004  57.462  1.00 29.76  ? 183 GLY A O   1 
ATOM   1429  N  N   . ARG A  1 184 ? 74.994  76.278  58.733  1.00 25.61  ? 184 ARG A N   1 
ATOM   1430  C  CA  . ARG A  1 184 ? 75.689  76.728  59.916  1.00 24.52  ? 184 ARG A CA  1 
ATOM   1431  C  C   . ARG A  1 184 ? 76.185  75.450  60.628  1.00 29.34  ? 184 ARG A C   1 
ATOM   1432  O  O   . ARG A  1 184 ? 77.287  75.404  61.144  1.00 38.20  ? 184 ARG A O   1 
ATOM   1433  C  CB  . ARG A  1 184 ? 74.719  77.505  60.813  1.00 22.42  ? 184 ARG A CB  1 
ATOM   1434  C  CG  . ARG A  1 184 ? 74.686  79.020  60.657  1.00 20.25  ? 184 ARG A CG  1 
ATOM   1435  C  CD  . ARG A  1 184 ? 73.740  79.644  61.701  1.00 10.15  ? 184 ARG A CD  1 
ATOM   1436  N  NE  . ARG A  1 184 ? 72.656  80.344  61.022  1.00 22.39  ? 184 ARG A NE  1 
ATOM   1437  C  CZ  . ARG A  1 184 ? 71.375  80.248  61.355  1.00 30.48  ? 184 ARG A CZ  1 
ATOM   1438  N  NH1 . ARG A  1 184 ? 71.031  79.468  62.384  1.00 27.39  ? 184 ARG A NH1 1 
ATOM   1439  N  NH2 . ARG A  1 184 ? 70.445  80.969  60.688  1.00 36.67  ? 184 ARG A NH2 1 
ATOM   1440  N  N   . PHE A  1 185 ? 75.359  74.415  60.638  1.00 29.20  ? 185 PHE A N   1 
ATOM   1441  C  CA  . PHE A  1 185 ? 75.682  73.146  61.232  1.00 22.89  ? 185 PHE A CA  1 
ATOM   1442  C  C   . PHE A  1 185 ? 76.941  72.530  60.653  1.00 22.86  ? 185 PHE A C   1 
ATOM   1443  O  O   . PHE A  1 185 ? 77.843  72.170  61.392  1.00 31.69  ? 185 PHE A O   1 
ATOM   1444  C  CB  . PHE A  1 185 ? 74.490  72.230  61.041  1.00 24.42  ? 185 PHE A CB  1 
ATOM   1445  C  CG  . PHE A  1 185 ? 74.801  70.778  61.159  1.00 27.19  ? 185 PHE A CG  1 
ATOM   1446  C  CD1 . PHE A  1 185 ? 75.631  70.309  62.148  1.00 28.05  ? 185 PHE A CD1 1 
ATOM   1447  C  CD2 . PHE A  1 185 ? 74.227  69.877  60.279  1.00 30.59  ? 185 PHE A CD2 1 
ATOM   1448  C  CE1 . PHE A  1 185 ? 75.883  68.982  62.263  1.00 29.78  ? 185 PHE A CE1 1 
ATOM   1449  C  CE2 . PHE A  1 185 ? 74.470  68.549  60.384  1.00 27.90  ? 185 PHE A CE2 1 
ATOM   1450  C  CZ  . PHE A  1 185 ? 75.300  68.097  61.379  1.00 30.97  ? 185 PHE A CZ  1 
ATOM   1451  N  N   . THR A  1 186 ? 76.993  72.400  59.341  1.00 22.69  ? 186 THR A N   1 
ATOM   1452  C  CA  . THR A  1 186 ? 78.143  71.819  58.650  1.00 22.60  ? 186 THR A CA  1 
ATOM   1453  C  C   . THR A  1 186 ? 79.409  72.708  58.527  1.00 24.07  ? 186 THR A C   1 
ATOM   1454  O  O   . THR A  1 186 ? 80.498  72.233  58.197  1.00 28.77  ? 186 THR A O   1 
ATOM   1455  C  CB  . THR A  1 186 ? 77.720  71.362  57.233  1.00 16.84  ? 186 THR A CB  1 
ATOM   1456  O  OG1 . THR A  1 186 ? 77.134  72.467  56.546  1.00 26.77  ? 186 THR A OG1 1 
ATOM   1457  C  CG2 . THR A  1 186 ? 76.668  70.278  57.311  1.00 19.88  ? 186 THR A CG2 1 
ATOM   1458  N  N   . GLU A  1 187 ? 79.292  73.992  58.821  1.00 23.79  ? 187 GLU A N   1 
ATOM   1459  C  CA  . GLU A  1 187 ? 80.423  74.915  58.677  1.00 21.09  ? 187 GLU A CA  1 
ATOM   1460  C  C   . GLU A  1 187 ? 81.699  74.406  59.310  1.00 22.75  ? 187 GLU A C   1 
ATOM   1461  O  O   . GLU A  1 187 ? 82.776  74.569  58.735  1.00 23.04  ? 187 GLU A O   1 
ATOM   1462  C  CB  . GLU A  1 187 ? 80.092  76.296  59.265  1.00 20.51  ? 187 GLU A CB  1 
ATOM   1463  C  CG  . GLU A  1 187 ? 81.064  77.440  58.879  1.00 32.75  ? 187 GLU A CG  1 
ATOM   1464  C  CD  . GLU A  1 187 ? 80.824  78.695  59.707  1.00 35.08  ? 187 GLU A CD  1 
ATOM   1465  O  OE1 . GLU A  1 187 ? 81.312  78.712  60.840  1.00 42.16  ? 187 GLU A OE1 1 
ATOM   1466  O  OE2 . GLU A  1 187 ? 80.122  79.640  59.281  1.00 41.06  ? 187 GLU A OE2 1 
ATOM   1467  N  N   . ARG A  1 188 ? 81.582  73.778  60.486  1.00 23.14  ? 188 ARG A N   1 
ATOM   1468  C  CA  . ARG A  1 188 ? 82.752  73.269  61.195  1.00 20.32  ? 188 ARG A CA  1 
ATOM   1469  C  C   . ARG A  1 188 ? 83.584  72.319  60.381  1.00 25.16  ? 188 ARG A C   1 
ATOM   1470  O  O   . ARG A  1 188 ? 84.758  72.150  60.674  1.00 33.05  ? 188 ARG A O   1 
ATOM   1471  C  CB  . ARG A  1 188 ? 82.396  72.649  62.531  1.00 13.78  ? 188 ARG A CB  1 
ATOM   1472  C  CG  . ARG A  1 188 ? 81.768  71.282  62.473  1.00 26.62  ? 188 ARG A CG  1 
ATOM   1473  C  CD  . ARG A  1 188 ? 80.987  71.028  63.784  1.00 31.68  ? 188 ARG A CD  1 
ATOM   1474  N  NE  . ARG A  1 188 ? 80.956  69.618  64.168  1.00 35.06  ? 188 ARG A NE  1 
ATOM   1475  C  CZ  . ARG A  1 188 ? 79.880  69.020  64.659  1.00 37.15  ? 188 ARG A CZ  1 
ATOM   1476  N  NH1 . ARG A  1 188 ? 78.757  69.717  64.835  1.00 41.72  ? 188 ARG A NH1 1 
ATOM   1477  N  NH2 . ARG A  1 188 ? 79.903  67.717  64.875  1.00 34.30  ? 188 ARG A NH2 1 
ATOM   1478  N  N   . SER A  1 189 ? 83.017  71.720  59.342  1.00 22.75  ? 189 SER A N   1 
ATOM   1479  C  CA  . SER A  1 189 ? 83.805  70.846  58.522  1.00 21.51  ? 189 SER A CA  1 
ATOM   1480  C  C   . SER A  1 189 ? 84.148  71.531  57.217  1.00 20.82  ? 189 SER A C   1 
ATOM   1481  O  O   . SER A  1 189 ? 85.325  71.753  56.903  1.00 20.74  ? 189 SER A O   1 
ATOM   1482  C  CB  . SER A  1 189 ? 83.051  69.559  58.247  1.00 22.61  ? 189 SER A CB  1 
ATOM   1483  O  OG  . SER A  1 189 ? 83.873  68.653  57.544  1.00 38.92  ? 189 SER A OG  1 
ATOM   1484  N  N   . VAL A  1 190 ? 83.111  71.929  56.487  1.00 22.12  ? 190 VAL A N   1 
ATOM   1485  C  CA  . VAL A  1 190 ? 83.287  72.555  55.175  1.00 20.34  ? 190 VAL A CA  1 
ATOM   1486  C  C   . VAL A  1 190 ? 84.005  73.859  55.094  1.00 24.60  ? 190 VAL A C   1 
ATOM   1487  O  O   . VAL A  1 190 ? 84.327  74.291  53.989  1.00 29.88  ? 190 VAL A O   1 
ATOM   1488  C  CB  . VAL A  1 190 ? 82.010  72.910  54.489  1.00 15.52  ? 190 VAL A CB  1 
ATOM   1489  C  CG1 . VAL A  1 190 ? 82.015  72.309  53.184  1.00 16.05  ? 190 VAL A CG1 1 
ATOM   1490  C  CG2 . VAL A  1 190 ? 80.816  72.534  55.291  1.00 19.61  ? 190 VAL A CG2 1 
ATOM   1491  N  N   . ALA A  1 191 ? 84.116  74.583  56.193  1.00 22.55  ? 191 ALA A N   1 
ATOM   1492  C  CA  . ALA A  1 191 ? 84.809  75.840  56.115  1.00 22.35  ? 191 ALA A CA  1 
ATOM   1493  C  C   . ALA A  1 191 ? 86.298  75.549  56.043  1.00 24.62  ? 191 ALA A C   1 
ATOM   1494  O  O   . ALA A  1 191 ? 87.060  76.426  55.641  1.00 27.27  ? 191 ALA A O   1 
ATOM   1495  C  CB  . ALA A  1 191 ? 84.508  76.695  57.302  1.00 24.42  ? 191 ALA A CB  1 
ATOM   1496  N  N   . TYR A  1 192 ? 86.702  74.308  56.350  1.00 24.97  ? 192 TYR A N   1 
ATOM   1497  C  CA  . TYR A  1 192 ? 88.118  73.937  56.353  1.00 26.15  ? 192 TYR A CA  1 
ATOM   1498  C  C   . TYR A  1 192 ? 88.590  72.934  55.328  1.00 29.88  ? 192 TYR A C   1 
ATOM   1499  O  O   . TYR A  1 192 ? 89.812  72.886  54.998  1.00 34.17  ? 192 TYR A O   1 
ATOM   1500  C  CB  . TYR A  1 192 ? 88.513  73.426  57.712  1.00 28.96  ? 192 TYR A CB  1 
ATOM   1501  C  CG  . TYR A  1 192 ? 88.153  74.371  58.813  1.00 32.82  ? 192 TYR A CG  1 
ATOM   1502  C  CD1 . TYR A  1 192 ? 88.999  75.430  59.169  1.00 35.16  ? 192 TYR A CD1 1 
ATOM   1503  C  CD2 . TYR A  1 192 ? 86.953  74.220  59.481  1.00 35.32  ? 192 TYR A CD2 1 
ATOM   1504  C  CE1 . TYR A  1 192 ? 88.633  76.323  60.174  1.00 43.07  ? 192 TYR A CE1 1 
ATOM   1505  C  CE2 . TYR A  1 192 ? 86.574  75.092  60.476  1.00 44.56  ? 192 TYR A CE2 1 
ATOM   1506  C  CZ  . TYR A  1 192 ? 87.403  76.156  60.839  1.00 44.35  ? 192 TYR A CZ  1 
ATOM   1507  O  OH  . TYR A  1 192 ? 86.971  77.020  61.864  1.00 47.72  ? 192 TYR A OH  1 
ATOM   1508  N  N   . GLN A  1 193 ? 87.678  72.063  54.893  1.00 27.06  ? 193 GLN A N   1 
ATOM   1509  C  CA  . GLN A  1 193 ? 88.057  71.088  53.861  1.00 26.04  ? 193 GLN A CA  1 
ATOM   1510  C  C   . GLN A  1 193 ? 86.943  71.060  52.886  1.00 22.61  ? 193 GLN A C   1 
ATOM   1511  O  O   . GLN A  1 193 ? 85.787  71.198  53.268  1.00 31.07  ? 193 GLN A O   1 
ATOM   1512  C  CB  . GLN A  1 193 ? 88.359  69.679  54.403  1.00 23.35  ? 193 GLN A CB  1 
ATOM   1513  C  CG  . GLN A  1 193 ? 87.190  68.937  54.942  1.00 27.19  ? 193 GLN A CG  1 
ATOM   1514  C  CD  . GLN A  1 193 ? 87.536  67.518  55.251  1.00 25.94  ? 193 GLN A CD  1 
ATOM   1515  O  OE1 . GLN A  1 193 ? 87.236  66.593  54.486  1.00 38.28  ? 193 GLN A OE1 1 
ATOM   1516  N  NE2 . GLN A  1 193 ? 88.162  67.324  56.374  1.00 29.59  ? 193 GLN A NE2 1 
ATOM   1517  N  N   . PRO A  1 194 ? 87.277  70.981  51.605  1.00 18.15  ? 194 PRO A N   1 
ATOM   1518  C  CA  . PRO A  1 194 ? 86.253  70.956  50.589  1.00 16.37  ? 194 PRO A CA  1 
ATOM   1519  C  C   . PRO A  1 194 ? 85.342  69.798  50.693  1.00 18.13  ? 194 PRO A C   1 
ATOM   1520  O  O   . PRO A  1 194 ? 85.710  68.762  51.232  1.00 25.09  ? 194 PRO A O   1 
ATOM   1521  C  CB  . PRO A  1 194 ? 87.075  70.856  49.295  1.00 16.27  ? 194 PRO A CB  1 
ATOM   1522  C  CG  . PRO A  1 194 ? 88.309  70.211  49.722  1.00 13.02  ? 194 PRO A CG  1 
ATOM   1523  C  CD  . PRO A  1 194 ? 88.610  70.905  50.989  1.00 15.41  ? 194 PRO A CD  1 
ATOM   1524  N  N   . TRP A  1 195 ? 84.106  70.006  50.268  1.00 19.12  ? 195 TRP A N   1 
ATOM   1525  C  CA  . TRP A  1 195 ? 83.151  68.911  50.152  1.00 17.95  ? 195 TRP A CA  1 
ATOM   1526  C  C   . TRP A  1 195 ? 82.775  68.918  48.637  1.00 14.74  ? 195 TRP A C   1 
ATOM   1527  O  O   . TRP A  1 195 ? 82.632  69.984  48.036  1.00 18.04  ? 195 TRP A O   1 
ATOM   1528  C  CB  . TRP A  1 195 ? 81.926  69.128  51.050  1.00 16.54  ? 195 TRP A CB  1 
ATOM   1529  C  CG  . TRP A  1 195 ? 82.106  68.824  52.542  1.00 14.80  ? 195 TRP A CG  1 
ATOM   1530  C  CD1 . TRP A  1 195 ? 83.216  69.003  53.292  1.00 15.25  ? 195 TRP A CD1 1 
ATOM   1531  C  CD2 . TRP A  1 195 ? 81.088  68.350  53.453  1.00 15.59  ? 195 TRP A CD2 1 
ATOM   1532  N  NE1 . TRP A  1 195 ? 82.965  68.699  54.615  1.00 17.99  ? 195 TRP A NE1 1 
ATOM   1533  C  CE2 . TRP A  1 195 ? 81.659  68.280  54.743  1.00 11.25  ? 195 TRP A CE2 1 
ATOM   1534  C  CE3 . TRP A  1 195 ? 79.741  67.974  53.302  1.00 16.04  ? 195 TRP A CE3 1 
ATOM   1535  C  CZ2 . TRP A  1 195 ? 80.952  67.858  55.844  1.00 9.89   ? 195 TRP A CZ2 1 
ATOM   1536  C  CZ3 . TRP A  1 195 ? 79.030  67.546  54.435  1.00 13.63  ? 195 TRP A CZ3 1 
ATOM   1537  C  CH2 . TRP A  1 195 ? 79.630  67.492  55.682  1.00 14.33  ? 195 TRP A CH2 1 
ATOM   1538  N  N   . ILE A  1 196 ? 82.767  67.770  47.986  1.00 12.74  ? 196 ILE A N   1 
ATOM   1539  C  CA  . ILE A  1 196 ? 82.399  67.737  46.594  1.00 18.88  ? 196 ILE A CA  1 
ATOM   1540  C  C   . ILE A  1 196 ? 80.904  67.444  46.577  1.00 22.00  ? 196 ILE A C   1 
ATOM   1541  O  O   . ILE A  1 196 ? 80.470  66.459  47.175  1.00 23.17  ? 196 ILE A O   1 
ATOM   1542  C  CB  . ILE A  1 196 ? 83.179  66.669  45.869  1.00 18.13  ? 196 ILE A CB  1 
ATOM   1543  C  CG1 . ILE A  1 196 ? 84.668  66.869  46.150  1.00 21.58  ? 196 ILE A CG1 1 
ATOM   1544  C  CG2 . ILE A  1 196 ? 82.899  66.755  44.409  1.00 17.09  ? 196 ILE A CG2 1 
ATOM   1545  C  CD1 . ILE A  1 196 ? 85.154  68.251  45.866  1.00 14.03  ? 196 ILE A CD1 1 
ATOM   1546  N  N   . TRP A  1 197 ? 80.129  68.302  45.908  1.00 24.29  ? 197 TRP A N   1 
ATOM   1547  C  CA  . TRP A  1 197 ? 78.686  68.181  45.888  1.00 19.34  ? 197 TRP A CA  1 
ATOM   1548  C  C   . TRP A  1 197 ? 78.060  67.392  44.787  1.00 17.65  ? 197 TRP A C   1 
ATOM   1549  O  O   . TRP A  1 197 ? 78.412  67.517  43.608  1.00 21.95  ? 197 TRP A O   1 
ATOM   1550  C  CB  . TRP A  1 197 ? 78.057  69.558  45.915  1.00 20.33  ? 197 TRP A CB  1 
ATOM   1551  C  CG  . TRP A  1 197 ? 78.555  70.402  47.046  1.00 22.77  ? 197 TRP A CG  1 
ATOM   1552  C  CD1 . TRP A  1 197 ? 79.397  71.478  46.963  1.00 26.10  ? 197 TRP A CD1 1 
ATOM   1553  C  CD2 . TRP A  1 197 ? 78.273  70.227  48.432  1.00 18.88  ? 197 TRP A CD2 1 
ATOM   1554  N  NE1 . TRP A  1 197 ? 79.658  71.981  48.238  1.00 24.20  ? 197 TRP A NE1 1 
ATOM   1555  C  CE2 . TRP A  1 197 ? 78.981  71.224  49.144  1.00 18.90  ? 197 TRP A CE2 1 
ATOM   1556  C  CE3 . TRP A  1 197 ? 77.504  69.320  49.143  1.00 25.06  ? 197 TRP A CE3 1 
ATOM   1557  C  CZ2 . TRP A  1 197 ? 78.935  71.322  50.518  1.00 16.21  ? 197 TRP A CZ2 1 
ATOM   1558  C  CZ3 . TRP A  1 197 ? 77.462  69.426  50.531  1.00 24.12  ? 197 TRP A CZ3 1 
ATOM   1559  C  CH2 . TRP A  1 197 ? 78.172  70.411  51.199  1.00 14.70  ? 197 TRP A CH2 1 
ATOM   1560  N  N   . THR A  1 198 ? 77.022  66.677  45.179  1.00 11.96  ? 198 THR A N   1 
ATOM   1561  C  CA  . THR A  1 198 ? 76.251  65.860  44.276  1.00 15.62  ? 198 THR A CA  1 
ATOM   1562  C  C   . THR A  1 198 ? 74.805  66.177  44.603  1.00 16.92  ? 198 THR A C   1 
ATOM   1563  O  O   . THR A  1 198 ? 74.411  66.228  45.770  1.00 20.66  ? 198 THR A O   1 
ATOM   1564  C  CB  . THR A  1 198 ? 76.479  64.393  44.516  1.00 14.35  ? 198 THR A CB  1 
ATOM   1565  O  OG1 . THR A  1 198 ? 77.860  64.129  44.382  1.00 21.08  ? 198 THR A OG1 1 
ATOM   1566  C  CG2 . THR A  1 198 ? 75.801  63.590  43.476  1.00 23.10  ? 198 THR A CG2 1 
ATOM   1567  N  N   . ALA A  1 199 ? 74.016  66.381  43.568  1.00 15.75  ? 199 ALA A N   1 
ATOM   1568  C  CA  . ALA A  1 199 ? 72.625  66.726  43.727  1.00 15.71  ? 199 ALA A CA  1 
ATOM   1569  C  C   . ALA A  1 199 ? 71.701  65.511  43.911  1.00 15.24  ? 199 ALA A C   1 
ATOM   1570  O  O   . ALA A  1 199 ? 71.665  64.582  43.066  1.00 20.41  ? 199 ALA A O   1 
ATOM   1571  C  CB  . ALA A  1 199 ? 72.207  67.530  42.520  1.00 13.68  ? 199 ALA A CB  1 
ATOM   1572  N  N   . GLY A  1 200 ? 70.892  65.555  44.962  1.00 13.62  ? 200 GLY A N   1 
ATOM   1573  C  CA  . GLY A  1 200 ? 69.989  64.454  45.226  1.00 15.22  ? 200 GLY A CA  1 
ATOM   1574  C  C   . GLY A  1 200 ? 68.573  64.882  45.045  1.00 16.96  ? 200 GLY A C   1 
ATOM   1575  O  O   . GLY A  1 200 ? 68.326  66.027  44.760  1.00 26.96  ? 200 GLY A O   1 
ATOM   1576  N  N   . ASN A  1 201 ? 67.635  63.986  45.229  1.00 17.43  ? 201 ASN A N   1 
ATOM   1577  C  CA  . ASN A  1 201 ? 66.234  64.349  45.063  1.00 22.81  ? 201 ASN A CA  1 
ATOM   1578  C  C   . ASN A  1 201 ? 65.736  65.397  46.049  1.00 26.54  ? 201 ASN A C   1 
ATOM   1579  O  O   . ASN A  1 201 ? 64.888  66.237  45.722  1.00 34.28  ? 201 ASN A O   1 
ATOM   1580  C  CB  . ASN A  1 201 ? 65.315  63.126  45.086  1.00 26.34  ? 201 ASN A CB  1 
ATOM   1581  C  CG  . ASN A  1 201 ? 65.558  62.212  46.245  1.00 23.97  ? 201 ASN A CG  1 
ATOM   1582  O  OD1 . ASN A  1 201 ? 66.703  61.957  46.615  1.00 24.86  ? 201 ASN A OD1 1 
ATOM   1583  N  ND2 . ASN A  1 201 ? 64.490  61.656  46.762  1.00 25.56  ? 201 ASN A ND2 1 
ATOM   1584  N  N   . HIS A  1 202 ? 66.284  65.420  47.253  1.00 24.41  ? 202 HIS A N   1 
ATOM   1585  C  CA  . HIS A  1 202 ? 65.790  66.413  48.179  1.00 19.75  ? 202 HIS A CA  1 
ATOM   1586  C  C   . HIS A  1 202 ? 66.211  67.790  47.749  1.00 18.97  ? 202 HIS A C   1 
ATOM   1587  O  O   . HIS A  1 202 ? 65.831  68.750  48.367  1.00 27.95  ? 202 HIS A O   1 
ATOM   1588  C  CB  . HIS A  1 202 ? 66.199  66.089  49.581  1.00 17.72  ? 202 HIS A CB  1 
ATOM   1589  C  CG  . HIS A  1 202 ? 65.344  65.037  50.215  1.00 19.19  ? 202 HIS A CG  1 
ATOM   1590  N  ND1 . HIS A  1 202 ? 64.193  65.330  50.915  1.00 16.81  ? 202 HIS A ND1 1 
ATOM   1591  C  CD2 . HIS A  1 202 ? 65.422  63.681  50.188  1.00 17.78  ? 202 HIS A CD2 1 
ATOM   1592  C  CE1 . HIS A  1 202 ? 63.591  64.204  51.274  1.00 18.40  ? 202 HIS A CE1 1 
ATOM   1593  N  NE2 . HIS A  1 202 ? 64.318  63.189  50.848  1.00 20.55  ? 202 HIS A NE2 1 
ATOM   1594  N  N   . GLU A  1 203 ? 67.082  67.871  46.757  1.00 16.02  ? 203 GLU A N   1 
ATOM   1595  C  CA  . GLU A  1 203 ? 67.524  69.138  46.220  1.00 15.98  ? 203 GLU A CA  1 
ATOM   1596  C  C   . GLU A  1 203 ? 66.700  69.655  45.075  1.00 18.77  ? 203 GLU A C   1 
ATOM   1597  O  O   . GLU A  1 203 ? 66.810  70.834  44.766  1.00 24.08  ? 203 GLU A O   1 
ATOM   1598  C  CB  . GLU A  1 203 ? 68.962  69.051  45.720  1.00 16.22  ? 203 GLU A CB  1 
ATOM   1599  C  CG  . GLU A  1 203 ? 69.972  69.161  46.847  1.00 16.13  ? 203 GLU A CG  1 
ATOM   1600  C  CD  . GLU A  1 203 ? 69.912  67.996  47.841  1.00 17.62  ? 203 GLU A CD  1 
ATOM   1601  O  OE1 . GLU A  1 203 ? 70.492  66.934  47.463  1.00 15.44  ? 203 GLU A OE1 1 
ATOM   1602  O  OE2 . GLU A  1 203 ? 69.355  68.156  48.984  1.00 20.69  ? 203 GLU A OE2 1 
ATOM   1603  N  N   . ILE A  1 204 ? 65.958  68.779  44.392  1.00 17.47  ? 204 ILE A N   1 
ATOM   1604  C  CA  . ILE A  1 204 ? 65.138  69.180  43.263  1.00 14.00  ? 204 ILE A CA  1 
ATOM   1605  C  C   . ILE A  1 204 ? 64.130  70.221  43.652  1.00 17.38  ? 204 ILE A C   1 
ATOM   1606  O  O   . ILE A  1 204 ? 63.929  71.174  42.905  1.00 26.35  ? 204 ILE A O   1 
ATOM   1607  C  CB  . ILE A  1 204 ? 64.364  68.058  42.725  1.00 16.10  ? 204 ILE A CB  1 
ATOM   1608  C  CG1 . ILE A  1 204 ? 65.281  66.956  42.278  1.00 15.03  ? 204 ILE A CG1 1 
ATOM   1609  C  CG2 . ILE A  1 204 ? 63.516  68.496  41.558  1.00 19.20  ? 204 ILE A CG2 1 
ATOM   1610  C  CD1 . ILE A  1 204 ? 64.490  65.689  41.979  1.00 7.12   ? 204 ILE A CD1 1 
ATOM   1611  N  N   . GLU A  1 205 ? 63.400  69.982  44.729  1.00 17.38  ? 205 GLU A N   1 
ATOM   1612  C  CA  . GLU A  1 205 ? 62.429  70.978  45.195  1.00 21.36  ? 205 GLU A CA  1 
ATOM   1613  C  C   . GLU A  1 205 ? 61.481  71.562  44.164  1.00 19.52  ? 205 GLU A C   1 
ATOM   1614  O  O   . GLU A  1 205 ? 61.373  72.781  44.002  1.00 21.41  ? 205 GLU A O   1 
ATOM   1615  C  CB  . GLU A  1 205 ? 63.106  72.130  45.941  1.00 17.28  ? 205 GLU A CB  1 
ATOM   1616  C  CG  . GLU A  1 205 ? 63.733  71.667  47.221  1.00 29.49  ? 205 GLU A CG  1 
ATOM   1617  C  CD  . GLU A  1 205 ? 64.292  72.753  48.112  1.00 26.38  ? 205 GLU A CD  1 
ATOM   1618  O  OE1 . GLU A  1 205 ? 63.494  73.310  48.894  1.00 25.19  ? 205 GLU A OE1 1 
ATOM   1619  O  OE2 . GLU A  1 205 ? 65.527  72.990  48.067  1.00 36.80  ? 205 GLU A OE2 1 
ATOM   1620  N  N   . PHE A  1 206 ? 60.799  70.675  43.485  1.00 17.06  ? 206 PHE A N   1 
ATOM   1621  C  CA  . PHE A  1 206 ? 59.850  71.076  42.516  1.00 16.14  ? 206 PHE A CA  1 
ATOM   1622  C  C   . PHE A  1 206 ? 58.562  71.216  43.293  1.00 17.68  ? 206 PHE A C   1 
ATOM   1623  O  O   . PHE A  1 206 ? 57.959  70.232  43.663  1.00 20.54  ? 206 PHE A O   1 
ATOM   1624  C  CB  . PHE A  1 206 ? 59.734  69.983  41.497  1.00 15.25  ? 206 PHE A CB  1 
ATOM   1625  C  CG  . PHE A  1 206 ? 58.709  70.236  40.452  1.00 14.13  ? 206 PHE A CG  1 
ATOM   1626  C  CD1 . PHE A  1 206 ? 58.874  71.248  39.515  1.00 16.69  ? 206 PHE A CD1 1 
ATOM   1627  C  CD2 . PHE A  1 206 ? 57.635  69.378  40.313  1.00 13.87  ? 206 PHE A CD2 1 
ATOM   1628  C  CE1 . PHE A  1 206 ? 57.981  71.385  38.439  1.00 19.05  ? 206 PHE A CE1 1 
ATOM   1629  C  CE2 . PHE A  1 206 ? 56.738  69.499  39.244  1.00 12.04  ? 206 PHE A CE2 1 
ATOM   1630  C  CZ  . PHE A  1 206 ? 56.912  70.498  38.304  1.00 16.23  ? 206 PHE A CZ  1 
ATOM   1631  N  N   . ALA A  1 207 ? 58.151  72.445  43.548  1.00 20.39  ? 207 ALA A N   1 
ATOM   1632  C  CA  . ALA A  1 207 ? 56.926  72.733  44.304  1.00 18.81  ? 207 ALA A CA  1 
ATOM   1633  C  C   . ALA A  1 207 ? 55.910  73.605  43.592  1.00 24.09  ? 207 ALA A C   1 
ATOM   1634  O  O   . ALA A  1 207 ? 55.680  74.743  43.974  1.00 28.54  ? 207 ALA A O   1 
ATOM   1635  C  CB  . ALA A  1 207 ? 57.243  73.375  45.622  1.00 14.57  ? 207 ALA A CB  1 
ATOM   1636  N  N   . PRO A  1 208 ? 55.232  73.063  42.592  1.00 26.16  ? 208 PRO A N   1 
ATOM   1637  C  CA  . PRO A  1 208 ? 54.220  73.785  41.824  1.00 27.11  ? 208 PRO A CA  1 
ATOM   1638  C  C   . PRO A  1 208 ? 53.169  74.477  42.709  1.00 28.11  ? 208 PRO A C   1 
ATOM   1639  O  O   . PRO A  1 208 ? 52.732  75.570  42.430  1.00 31.57  ? 208 PRO A O   1 
ATOM   1640  C  CB  . PRO A  1 208 ? 53.565  72.660  41.024  1.00 29.71  ? 208 PRO A CB  1 
ATOM   1641  C  CG  . PRO A  1 208 ? 54.665  71.754  40.753  1.00 31.22  ? 208 PRO A CG  1 
ATOM   1642  C  CD  . PRO A  1 208 ? 55.428  71.704  42.061  1.00 30.88  ? 208 PRO A CD  1 
ATOM   1643  N  N   . GLU A  1 209 ? 52.750  73.811  43.766  1.00 30.16  ? 209 GLU A N   1 
ATOM   1644  C  CA  . GLU A  1 209 ? 51.753  74.325  44.696  1.00 27.68  ? 209 GLU A CA  1 
ATOM   1645  C  C   . GLU A  1 209 ? 52.085  75.678  45.239  1.00 27.00  ? 209 GLU A C   1 
ATOM   1646  O  O   . GLU A  1 209 ? 51.214  76.451  45.523  1.00 34.92  ? 209 GLU A O   1 
ATOM   1647  C  CB  . GLU A  1 209 ? 51.614  73.402  45.897  1.00 32.57  ? 209 GLU A CB  1 
ATOM   1648  C  CG  . GLU A  1 209 ? 52.191  72.014  45.748  1.00 52.42  ? 209 GLU A CG  1 
ATOM   1649  C  CD  . GLU A  1 209 ? 53.679  71.928  46.032  1.00 57.81  ? 209 GLU A CD  1 
ATOM   1650  O  OE1 . GLU A  1 209 ? 54.111  72.232  47.173  1.00 58.76  ? 209 GLU A OE1 1 
ATOM   1651  O  OE2 . GLU A  1 209 ? 54.401  71.504  45.108  1.00 69.90  ? 209 GLU A OE2 1 
ATOM   1652  N  N   . ILE A  1 210 ? 53.340  75.923  45.524  1.00 26.12  ? 210 ILE A N   1 
ATOM   1653  C  CA  . ILE A  1 210 ? 53.715  77.206  46.040  1.00 25.06  ? 210 ILE A CA  1 
ATOM   1654  C  C   . ILE A  1 210 ? 54.402  77.972  44.963  1.00 28.49  ? 210 ILE A C   1 
ATOM   1655  O  O   . ILE A  1 210 ? 55.230  78.829  45.216  1.00 37.54  ? 210 ILE A O   1 
ATOM   1656  C  CB  . ILE A  1 210 ? 54.628  77.062  47.212  1.00 27.72  ? 210 ILE A CB  1 
ATOM   1657  C  CG1 . ILE A  1 210 ? 55.774  76.107  46.934  1.00 24.22  ? 210 ILE A CG1 1 
ATOM   1658  C  CG2 . ILE A  1 210 ? 53.859  76.547  48.335  1.00 30.08  ? 210 ILE A CG2 1 
ATOM   1659  C  CD1 . ILE A  1 210 ? 56.710  76.027  48.057  1.00 21.97  ? 210 ILE A CD1 1 
ATOM   1660  N  N   . ASN A  1 211 ? 54.135  77.572  43.738  1.00 29.64  ? 211 ASN A N   1 
ATOM   1661  C  CA  . ASN A  1 211 ? 54.694  78.230  42.591  1.00 32.08  ? 211 ASN A CA  1 
ATOM   1662  C  C   . ASN A  1 211 ? 56.183  78.287  42.409  1.00 30.03  ? 211 ASN A C   1 
ATOM   1663  O  O   . ASN A  1 211 ? 56.685  79.134  41.692  1.00 34.95  ? 211 ASN A O   1 
ATOM   1664  C  CB  . ASN A  1 211 ? 54.093  79.603  42.467  1.00 48.42  ? 211 ASN A CB  1 
ATOM   1665  C  CG  . ASN A  1 211 ? 52.714  79.557  41.902  1.00 67.51  ? 211 ASN A CG  1 
ATOM   1666  O  OD1 . ASN A  1 211 ? 52.570  79.461  40.675  1.00 76.47  ? 211 ASN A OD1 1 
ATOM   1667  N  ND2 . ASN A  1 211 ? 51.726  79.525  42.800  1.00 76.52  ? 211 ASN A ND2 1 
ATOM   1668  N  N   . GLU A  1 212 ? 56.900  77.367  43.012  1.00 30.05  ? 212 GLU A N   1 
ATOM   1669  C  CA  . GLU A  1 212 ? 58.337  77.289  42.863  1.00 23.95  ? 212 GLU A CA  1 
ATOM   1670  C  C   . GLU A  1 212 ? 58.541  76.086  41.949  1.00 24.07  ? 212 GLU A C   1 
ATOM   1671  O  O   . GLU A  1 212 ? 58.354  74.956  42.359  1.00 22.36  ? 212 GLU A O   1 
ATOM   1672  C  CB  . GLU A  1 212 ? 58.929  77.035  44.212  1.00 25.29  ? 212 GLU A CB  1 
ATOM   1673  C  CG  . GLU A  1 212 ? 58.927  78.248  45.041  1.00 29.41  ? 212 GLU A CG  1 
ATOM   1674  C  CD  . GLU A  1 212 ? 59.715  79.324  44.377  1.00 34.98  ? 212 GLU A CD  1 
ATOM   1675  O  OE1 . GLU A  1 212 ? 60.769  79.016  43.756  1.00 36.38  ? 212 GLU A OE1 1 
ATOM   1676  O  OE2 . GLU A  1 212 ? 59.250  80.481  44.433  1.00 46.20  ? 212 GLU A OE2 1 
ATOM   1677  N  N   . THR A  1 213 ? 58.843  76.322  40.691  1.00 20.33  ? 213 THR A N   1 
ATOM   1678  C  CA  . THR A  1 213 ? 58.992  75.225  39.772  1.00 20.55  ? 213 THR A CA  1 
ATOM   1679  C  C   . THR A  1 213 ? 60.309  75.111  39.013  1.00 27.75  ? 213 THR A C   1 
ATOM   1680  O  O   . THR A  1 213 ? 60.359  74.472  37.961  1.00 30.09  ? 213 THR A O   1 
ATOM   1681  C  CB  . THR A  1 213 ? 57.890  75.271  38.755  1.00 18.63  ? 213 THR A CB  1 
ATOM   1682  O  OG1 . THR A  1 213 ? 57.978  76.476  38.002  1.00 21.75  ? 213 THR A OG1 1 
ATOM   1683  C  CG2 . THR A  1 213 ? 56.573  75.278  39.436  1.00 30.48  ? 213 THR A CG2 1 
ATOM   1684  N  N   . GLU A  1 214 ? 61.353  75.770  39.504  1.00 33.94  ? 214 GLU A N   1 
ATOM   1685  C  CA  . GLU A  1 214 ? 62.653  75.719  38.869  1.00 34.04  ? 214 GLU A CA  1 
ATOM   1686  C  C   . GLU A  1 214 ? 63.453  74.742  39.751  1.00 31.87  ? 214 GLU A C   1 
ATOM   1687  O  O   . GLU A  1 214 ? 63.758  75.028  40.925  1.00 40.88  ? 214 GLU A O   1 
ATOM   1688  C  CB  . GLU A  1 214 ? 63.281  77.118  38.861  1.00 47.10  ? 214 GLU A CB  1 
ATOM   1689  C  CG  . GLU A  1 214 ? 64.583  77.247  38.033  1.00 67.40  ? 214 GLU A CG  1 
ATOM   1690  C  CD  . GLU A  1 214 ? 65.544  78.364  38.540  1.00 76.15  ? 214 GLU A CD  1 
ATOM   1691  O  OE1 . GLU A  1 214 ? 65.068  79.508  38.765  1.00 78.24  ? 214 GLU A OE1 1 
ATOM   1692  O  OE2 . GLU A  1 214 ? 66.778  78.091  38.702  1.00 83.98  ? 214 GLU A OE2 1 
ATOM   1693  N  N   . PRO A  1 215 ? 63.712  73.538  39.238  1.00 26.81  ? 215 PRO A N   1 
ATOM   1694  C  CA  . PRO A  1 215 ? 64.446  72.510  39.967  1.00 26.20  ? 215 PRO A CA  1 
ATOM   1695  C  C   . PRO A  1 215 ? 65.777  72.985  40.485  1.00 28.61  ? 215 PRO A C   1 
ATOM   1696  O  O   . PRO A  1 215 ? 66.448  73.842  39.881  1.00 33.53  ? 215 PRO A O   1 
ATOM   1697  C  CB  . PRO A  1 215 ? 64.629  71.416  38.913  1.00 28.50  ? 215 PRO A CB  1 
ATOM   1698  C  CG  . PRO A  1 215 ? 63.430  71.559  38.044  1.00 22.40  ? 215 PRO A CG  1 
ATOM   1699  C  CD  . PRO A  1 215 ? 63.355  73.062  37.892  1.00 25.60  ? 215 PRO A CD  1 
ATOM   1700  N  N   . PHE A  1 216 ? 66.139  72.464  41.645  1.00 25.50  ? 216 PHE A N   1 
ATOM   1701  C  CA  . PHE A  1 216 ? 67.423  72.769  42.241  1.00 23.34  ? 216 PHE A CA  1 
ATOM   1702  C  C   . PHE A  1 216 ? 67.682  74.221  42.573  1.00 19.71  ? 216 PHE A C   1 
ATOM   1703  O  O   . PHE A  1 216 ? 68.829  74.586  42.846  1.00 25.38  ? 216 PHE A O   1 
ATOM   1704  C  CB  . PHE A  1 216 ? 68.558  72.254  41.333  1.00 17.44  ? 216 PHE A CB  1 
ATOM   1705  C  CG  . PHE A  1 216 ? 68.456  70.779  41.031  1.00 15.24  ? 216 PHE A CG  1 
ATOM   1706  C  CD1 . PHE A  1 216 ? 68.758  69.834  41.993  1.00 20.28  ? 216 PHE A CD1 1 
ATOM   1707  C  CD2 . PHE A  1 216 ? 68.018  70.339  39.807  1.00 9.65   ? 216 PHE A CD2 1 
ATOM   1708  C  CE1 . PHE A  1 216 ? 68.615  68.485  41.718  1.00 16.43  ? 216 PHE A CE1 1 
ATOM   1709  C  CE2 . PHE A  1 216 ? 67.886  68.997  39.547  1.00 11.46  ? 216 PHE A CE2 1 
ATOM   1710  C  CZ  . PHE A  1 216 ? 68.181  68.076  40.498  1.00 5.41   ? 216 PHE A CZ  1 
ATOM   1711  N  N   . LYS A  1 217 ? 66.641  75.020  42.737  1.00 13.19  ? 217 LYS A N   1 
ATOM   1712  C  CA  . LYS A  1 217 ? 66.878  76.412  42.981  1.00 11.26  ? 217 LYS A CA  1 
ATOM   1713  C  C   . LYS A  1 217 ? 67.659  76.770  44.232  1.00 12.52  ? 217 LYS A C   1 
ATOM   1714  O  O   . LYS A  1 217 ? 68.779  77.283  44.148  1.00 15.37  ? 217 LYS A O   1 
ATOM   1715  C  CB  . LYS A  1 217 ? 65.595  77.192  42.924  1.00 18.15  ? 217 LYS A CB  1 
ATOM   1716  C  CG  . LYS A  1 217 ? 65.811  78.690  43.094  1.00 17.87  ? 217 LYS A CG  1 
ATOM   1717  C  CD  . LYS A  1 217 ? 64.609  79.466  42.610  1.00 15.83  ? 217 LYS A CD  1 
ATOM   1718  C  CE  . LYS A  1 217 ? 63.950  80.203  43.714  1.00 15.71  ? 217 LYS A CE  1 
ATOM   1719  N  NZ  . LYS A  1 217 ? 62.719  80.832  43.221  1.00 23.26  ? 217 LYS A NZ  1 
ATOM   1720  N  N   . PRO A  1 218 ? 67.137  76.462  45.411  1.00 4.43   ? 218 PRO A N   1 
ATOM   1721  C  CA  . PRO A  1 218 ? 67.924  76.853  46.576  1.00 6.22   ? 218 PRO A CA  1 
ATOM   1722  C  C   . PRO A  1 218 ? 69.285  76.224  46.608  1.00 7.45   ? 218 PRO A C   1 
ATOM   1723  O  O   . PRO A  1 218 ? 70.268  76.870  46.987  1.00 9.01   ? 218 PRO A O   1 
ATOM   1724  C  CB  . PRO A  1 218 ? 67.072  76.390  47.744  1.00 7.54   ? 218 PRO A CB  1 
ATOM   1725  C  CG  . PRO A  1 218 ? 65.709  76.461  47.182  1.00 10.09  ? 218 PRO A CG  1 
ATOM   1726  C  CD  . PRO A  1 218 ? 65.880  75.864  45.822  1.00 3.28   ? 218 PRO A CD  1 
ATOM   1727  N  N   . PHE A  1 219 ? 69.350  74.961  46.191  1.00 11.84  ? 219 PHE A N   1 
ATOM   1728  C  CA  . PHE A  1 219 ? 70.623  74.256  46.197  1.00 13.32  ? 219 PHE A CA  1 
ATOM   1729  C  C   . PHE A  1 219 ? 71.634  74.985  45.336  1.00 17.26  ? 219 PHE A C   1 
ATOM   1730  O  O   . PHE A  1 219 ? 72.753  75.327  45.764  1.00 19.90  ? 219 PHE A O   1 
ATOM   1731  C  CB  . PHE A  1 219 ? 70.441  72.838  45.660  1.00 17.53  ? 219 PHE A CB  1 
ATOM   1732  C  CG  . PHE A  1 219 ? 71.736  72.082  45.471  1.00 12.84  ? 219 PHE A CG  1 
ATOM   1733  C  CD1 . PHE A  1 219 ? 72.557  71.800  46.537  1.00 22.08  ? 219 PHE A CD1 1 
ATOM   1734  C  CD2 . PHE A  1 219 ? 72.168  71.737  44.214  1.00 14.16  ? 219 PHE A CD2 1 
ATOM   1735  C  CE1 . PHE A  1 219 ? 73.796  71.211  46.351  1.00 17.14  ? 219 PHE A CE1 1 
ATOM   1736  C  CE2 . PHE A  1 219 ? 73.434  71.141  44.023  1.00 13.25  ? 219 PHE A CE2 1 
ATOM   1737  C  CZ  . PHE A  1 219 ? 74.229  70.886  45.087  1.00 4.84   ? 219 PHE A CZ  1 
ATOM   1738  N  N   . SER A  1 220 ? 71.204  75.288  44.128  1.00 21.63  ? 220 SER A N   1 
ATOM   1739  C  CA  . SER A  1 220 ? 72.080  75.949  43.197  1.00 27.39  ? 220 SER A CA  1 
ATOM   1740  C  C   . SER A  1 220 ? 72.487  77.346  43.602  1.00 30.03  ? 220 SER A C   1 
ATOM   1741  O  O   . SER A  1 220 ? 73.548  77.762  43.202  1.00 34.66  ? 220 SER A O   1 
ATOM   1742  C  CB  . SER A  1 220 ? 71.492  75.949  41.809  1.00 25.17  ? 220 SER A CB  1 
ATOM   1743  O  OG  . SER A  1 220 ? 70.237  76.564  41.837  1.00 36.62  ? 220 SER A OG  1 
ATOM   1744  N  N   . TYR A  1 221 ? 71.668  78.095  44.342  1.00 27.02  ? 221 TYR A N   1 
ATOM   1745  C  CA  . TYR A  1 221 ? 72.109  79.421  44.774  1.00 22.29  ? 221 TYR A CA  1 
ATOM   1746  C  C   . TYR A  1 221 ? 73.192  79.318  45.839  1.00 21.80  ? 221 TYR A C   1 
ATOM   1747  O  O   . TYR A  1 221 ? 74.180  80.084  45.840  1.00 23.32  ? 221 TYR A O   1 
ATOM   1748  C  CB  . TYR A  1 221 ? 70.970  80.213  45.363  1.00 24.74  ? 221 TYR A CB  1 
ATOM   1749  C  CG  . TYR A  1 221 ? 70.221  80.995  44.356  1.00 33.74  ? 221 TYR A CG  1 
ATOM   1750  C  CD1 . TYR A  1 221 ? 70.630  82.261  43.989  1.00 37.74  ? 221 TYR A CD1 1 
ATOM   1751  C  CD2 . TYR A  1 221 ? 69.130  80.444  43.715  1.00 38.73  ? 221 TYR A CD2 1 
ATOM   1752  C  CE1 . TYR A  1 221 ? 69.968  82.959  43.001  1.00 37.47  ? 221 TYR A CE1 1 
ATOM   1753  C  CE2 . TYR A  1 221 ? 68.473  81.121  42.732  1.00 36.96  ? 221 TYR A CE2 1 
ATOM   1754  C  CZ  . TYR A  1 221 ? 68.893  82.384  42.365  1.00 39.54  ? 221 TYR A CZ  1 
ATOM   1755  O  OH  . TYR A  1 221 ? 68.246  83.034  41.324  1.00 44.02  ? 221 TYR A OH  1 
ATOM   1756  N  N   . ARG A  1 222 ? 72.991  78.381  46.757  1.00 13.31  ? 222 ARG A N   1 
ATOM   1757  C  CA  . ARG A  1 222 ? 73.891  78.192  47.863  1.00 12.12  ? 222 ARG A CA  1 
ATOM   1758  C  C   . ARG A  1 222 ? 75.176  77.394  47.641  1.00 16.28  ? 222 ARG A C   1 
ATOM   1759  O  O   . ARG A  1 222 ? 76.204  77.684  48.267  1.00 15.30  ? 222 ARG A O   1 
ATOM   1760  C  CB  . ARG A  1 222 ? 73.101  77.566  48.983  1.00 6.89   ? 222 ARG A CB  1 
ATOM   1761  C  CG  . ARG A  1 222 ? 72.057  78.466  49.470  1.00 5.03   ? 222 ARG A CG  1 
ATOM   1762  C  CD  . ARG A  1 222 ? 70.880  77.700  49.956  1.00 14.26  ? 222 ARG A CD  1 
ATOM   1763  N  NE  . ARG A  1 222 ? 69.932  78.526  50.696  1.00 19.81  ? 222 ARG A NE  1 
ATOM   1764  C  CZ  . ARG A  1 222 ? 70.166  79.042  51.902  1.00 21.96  ? 222 ARG A CZ  1 
ATOM   1765  N  NH1 . ARG A  1 222 ? 71.319  78.816  52.494  1.00 22.94  ? 222 ARG A NH1 1 
ATOM   1766  N  NH2 . ARG A  1 222 ? 69.228  79.725  52.551  1.00 22.84  ? 222 ARG A NH2 1 
ATOM   1767  N  N   . TYR A  1 223 ? 75.131  76.383  46.787  1.00 11.22  ? 223 TYR A N   1 
ATOM   1768  C  CA  . TYR A  1 223 ? 76.287  75.557  46.576  1.00 11.92  ? 223 TYR A CA  1 
ATOM   1769  C  C   . TYR A  1 223 ? 76.735  75.643  45.142  1.00 17.94  ? 223 TYR A C   1 
ATOM   1770  O  O   . TYR A  1 223 ? 75.999  75.265  44.236  1.00 27.94  ? 223 TYR A O   1 
ATOM   1771  C  CB  . TYR A  1 223 ? 75.890  74.139  46.937  1.00 9.90   ? 223 TYR A CB  1 
ATOM   1772  C  CG  . TYR A  1 223 ? 75.605  74.038  48.387  1.00 16.14  ? 223 TYR A CG  1 
ATOM   1773  C  CD1 . TYR A  1 223 ? 76.648  74.035  49.297  1.00 18.15  ? 223 TYR A CD1 1 
ATOM   1774  C  CD2 . TYR A  1 223 ? 74.310  74.090  48.871  1.00 17.06  ? 223 TYR A CD2 1 
ATOM   1775  C  CE1 . TYR A  1 223 ? 76.430  74.107  50.646  1.00 19.16  ? 223 TYR A CE1 1 
ATOM   1776  C  CE2 . TYR A  1 223 ? 74.068  74.163  50.242  1.00 18.68  ? 223 TYR A CE2 1 
ATOM   1777  C  CZ  . TYR A  1 223 ? 75.158  74.176  51.123  1.00 25.49  ? 223 TYR A CZ  1 
ATOM   1778  O  OH  . TYR A  1 223 ? 75.027  74.298  52.488  1.00 34.24  ? 223 TYR A OH  1 
ATOM   1779  N  N   . HIS A  1 224 ? 77.947  76.134  44.917  1.00 19.34  ? 224 HIS A N   1 
ATOM   1780  C  CA  . HIS A  1 224 ? 78.481  76.277  43.556  1.00 15.29  ? 224 HIS A CA  1 
ATOM   1781  C  C   . HIS A  1 224 ? 79.550  75.258  43.309  1.00 17.24  ? 224 HIS A C   1 
ATOM   1782  O  O   . HIS A  1 224 ? 80.169  74.829  44.257  1.00 28.73  ? 224 HIS A O   1 
ATOM   1783  C  CB  . HIS A  1 224 ? 79.078  77.644  43.368  1.00 9.96   ? 224 HIS A CB  1 
ATOM   1784  C  CG  . HIS A  1 224 ? 78.066  78.712  43.067  1.00 23.39  ? 224 HIS A CG  1 
ATOM   1785  N  ND1 . HIS A  1 224 ? 78.378  79.860  42.372  1.00 28.03  ? 224 HIS A ND1 1 
ATOM   1786  C  CD2 . HIS A  1 224 ? 76.735  78.779  43.318  1.00 23.13  ? 224 HIS A CD2 1 
ATOM   1787  C  CE1 . HIS A  1 224 ? 77.281  80.586  42.199  1.00 25.82  ? 224 HIS A CE1 1 
ATOM   1788  N  NE2 . HIS A  1 224 ? 76.273  79.953  42.763  1.00 22.39  ? 224 HIS A NE2 1 
ATOM   1789  N  N   . VAL A  1 225 ? 79.819  74.928  42.051  1.00 14.09  ? 225 VAL A N   1 
ATOM   1790  C  CA  . VAL A  1 225 ? 80.818  73.924  41.693  1.00 12.92  ? 225 VAL A CA  1 
ATOM   1791  C  C   . VAL A  1 225 ? 81.543  74.380  40.437  1.00 12.90  ? 225 VAL A C   1 
ATOM   1792  O  O   . VAL A  1 225 ? 81.027  75.159  39.657  1.00 18.61  ? 225 VAL A O   1 
ATOM   1793  C  CB  . VAL A  1 225 ? 80.185  72.585  41.425  1.00 15.90  ? 225 VAL A CB  1 
ATOM   1794  C  CG1 . VAL A  1 225 ? 79.553  72.076  42.668  1.00 21.76  ? 225 VAL A CG1 1 
ATOM   1795  C  CG2 . VAL A  1 225 ? 79.135  72.717  40.337  1.00 12.14  ? 225 VAL A CG2 1 
ATOM   1796  N  N   . PRO A  1 226 ? 82.758  73.898  40.224  1.00 11.17  ? 226 PRO A N   1 
ATOM   1797  C  CA  . PRO A  1 226 ? 83.580  74.262  39.072  1.00 9.00   ? 226 PRO A CA  1 
ATOM   1798  C  C   . PRO A  1 226 ? 83.213  73.539  37.847  1.00 18.67  ? 226 PRO A C   1 
ATOM   1799  O  O   . PRO A  1 226 ? 84.088  73.090  37.099  1.00 24.83  ? 226 PRO A O   1 
ATOM   1800  C  CB  . PRO A  1 226 ? 84.953  73.848  39.510  1.00 9.05   ? 226 PRO A CB  1 
ATOM   1801  C  CG  . PRO A  1 226 ? 84.683  72.645  40.367  1.00 8.69   ? 226 PRO A CG  1 
ATOM   1802  C  CD  . PRO A  1 226 ? 83.502  73.051  41.171  1.00 8.11   ? 226 PRO A CD  1 
ATOM   1803  N  N   . TYR A  1 227 ? 81.928  73.515  37.545  1.00 17.06  ? 227 TYR A N   1 
ATOM   1804  C  CA  . TYR A  1 227 ? 81.535  72.752  36.399  1.00 14.77  ? 227 TYR A CA  1 
ATOM   1805  C  C   . TYR A  1 227 ? 82.106  73.188  35.095  1.00 17.26  ? 227 TYR A C   1 
ATOM   1806  O  O   . TYR A  1 227 ? 82.350  72.373  34.245  1.00 21.68  ? 227 TYR A O   1 
ATOM   1807  C  CB  . TYR A  1 227 ? 80.043  72.630  36.315  1.00 17.49  ? 227 TYR A CB  1 
ATOM   1808  C  CG  . TYR A  1 227 ? 79.360  73.882  35.943  1.00 19.76  ? 227 TYR A CG  1 
ATOM   1809  C  CD1 . TYR A  1 227 ? 79.114  74.180  34.625  1.00 26.08  ? 227 TYR A CD1 1 
ATOM   1810  C  CD2 . TYR A  1 227 ? 78.907  74.746  36.903  1.00 18.81  ? 227 TYR A CD2 1 
ATOM   1811  C  CE1 . TYR A  1 227 ? 78.441  75.293  34.288  1.00 26.01  ? 227 TYR A CE1 1 
ATOM   1812  C  CE2 . TYR A  1 227 ? 78.243  75.860  36.583  1.00 16.40  ? 227 TYR A CE2 1 
ATOM   1813  C  CZ  . TYR A  1 227 ? 78.006  76.136  35.276  1.00 24.72  ? 227 TYR A CZ  1 
ATOM   1814  O  OH  . TYR A  1 227 ? 77.302  77.261  34.931  1.00 33.19  ? 227 TYR A OH  1 
ATOM   1815  N  N   . GLU A  1 228 ? 82.430  74.441  34.949  1.00 18.01  ? 228 GLU A N   1 
ATOM   1816  C  CA  . GLU A  1 228 ? 82.952  74.824  33.659  1.00 19.44  ? 228 GLU A CA  1 
ATOM   1817  C  C   . GLU A  1 228 ? 84.382  74.362  33.530  1.00 14.61  ? 228 GLU A C   1 
ATOM   1818  O  O   . GLU A  1 228 ? 84.921  74.347  32.453  1.00 16.53  ? 228 GLU A O   1 
ATOM   1819  C  CB  . GLU A  1 228 ? 82.800  76.334  33.326  1.00 27.78  ? 228 GLU A CB  1 
ATOM   1820  C  CG  . GLU A  1 228 ? 81.935  77.163  34.279  1.00 48.25  ? 228 GLU A CG  1 
ATOM   1821  C  CD  . GLU A  1 228 ? 82.445  77.083  35.747  1.00 62.58  ? 228 GLU A CD  1 
ATOM   1822  O  OE1 . GLU A  1 228 ? 83.657  76.734  35.993  1.00 61.94  ? 228 GLU A OE1 1 
ATOM   1823  O  OE2 . GLU A  1 228 ? 81.605  77.333  36.656  1.00 66.26  ? 228 GLU A OE2 1 
ATOM   1824  N  N   . ALA A  1 229 ? 85.013  73.953  34.612  1.00 18.66  ? 229 ALA A N   1 
ATOM   1825  C  CA  . ALA A  1 229 ? 86.403  73.492  34.493  1.00 19.85  ? 229 ALA A CA  1 
ATOM   1826  C  C   . ALA A  1 229 ? 86.466  72.236  33.631  1.00 22.27  ? 229 ALA A C   1 
ATOM   1827  O  O   . ALA A  1 229 ? 87.430  72.090  32.907  1.00 28.10  ? 229 ALA A O   1 
ATOM   1828  C  CB  . ALA A  1 229 ? 87.016  73.263  35.828  1.00 20.05  ? 229 ALA A CB  1 
ATOM   1829  N  N   . SER A  1 230 ? 85.534  71.267  33.829  1.00 28.27  ? 230 SER A N   1 
ATOM   1830  C  CA  . SER A  1 230 ? 85.372  70.043  32.963  1.00 21.74  ? 230 SER A CA  1 
ATOM   1831  C  C   . SER A  1 230 ? 84.681  70.833  31.895  1.00 26.79  ? 230 SER A C   1 
ATOM   1832  O  O   . SER A  1 230 ? 84.421  72.015  32.102  1.00 34.46  ? 230 SER A O   1 
ATOM   1833  C  CB  . SER A  1 230 ? 84.341  69.080  33.538  1.00 17.61  ? 230 SER A CB  1 
ATOM   1834  O  OG  . SER A  1 230 ? 84.099  69.341  34.941  1.00 33.99  ? 230 SER A OG  1 
ATOM   1835  N  N   . GLN A  1 231 ? 84.306  70.327  30.758  1.00 23.29  ? 231 GLN A N   1 
ATOM   1836  C  CA  . GLN A  1 231 ? 83.658  71.373  29.939  1.00 24.28  ? 231 GLN A CA  1 
ATOM   1837  C  C   . GLN A  1 231 ? 82.148  71.242  29.995  1.00 23.86  ? 231 GLN A C   1 
ATOM   1838  O  O   . GLN A  1 231 ? 81.487  71.256  28.967  1.00 34.22  ? 231 GLN A O   1 
ATOM   1839  C  CB  . GLN A  1 231 ? 84.228  71.449  28.513  1.00 33.69  ? 231 GLN A CB  1 
ATOM   1840  C  CG  . GLN A  1 231 ? 85.680  72.007  28.404  1.00 51.54  ? 231 GLN A CG  1 
ATOM   1841  C  CD  . GLN A  1 231 ? 86.734  71.186  29.208  1.00 65.92  ? 231 GLN A CD  1 
ATOM   1842  O  OE1 . GLN A  1 231 ? 86.603  69.965  29.411  1.00 74.24  ? 231 GLN A OE1 1 
ATOM   1843  N  NE2 . GLN A  1 231 ? 87.773  71.868  29.673  1.00 72.26  ? 231 GLN A NE2 1 
ATOM   1844  N  N   . SER A  1 232 ? 81.617  71.046  31.208  1.00 21.48  ? 232 SER A N   1 
ATOM   1845  C  CA  . SER A  1 232 ? 80.179  70.862  31.458  1.00 18.49  ? 232 SER A CA  1 
ATOM   1846  C  C   . SER A  1 232 ? 79.413  72.141  31.283  1.00 19.01  ? 232 SER A C   1 
ATOM   1847  O  O   . SER A  1 232 ? 79.950  73.237  31.449  1.00 24.04  ? 232 SER A O   1 
ATOM   1848  C  CB  . SER A  1 232 ? 79.936  70.346  32.884  1.00 20.33  ? 232 SER A CB  1 
ATOM   1849  O  OG  . SER A  1 232 ? 78.566  70.346  33.242  1.00 17.60  ? 232 SER A OG  1 
ATOM   1850  N  N   . THR A  1 233 ? 78.131  72.005  30.997  1.00 16.66  ? 233 THR A N   1 
ATOM   1851  C  CA  . THR A  1 233 ? 77.324  73.184  30.804  1.00 13.73  ? 233 THR A CA  1 
ATOM   1852  C  C   . THR A  1 233 ? 76.323  73.256  31.893  1.00 14.54  ? 233 THR A C   1 
ATOM   1853  O  O   . THR A  1 233 ? 75.340  73.973  31.782  1.00 18.31  ? 233 THR A O   1 
ATOM   1854  C  CB  . THR A  1 233 ? 76.613  73.182  29.461  1.00 12.28  ? 233 THR A CB  1 
ATOM   1855  O  OG1 . THR A  1 233 ? 75.796  72.031  29.366  1.00 20.85  ? 233 THR A OG1 1 
ATOM   1856  C  CG2 . THR A  1 233 ? 77.589  73.129  28.376  1.00 10.45  ? 233 THR A CG2 1 
ATOM   1857  N  N   . SER A  1 234 ? 76.519  72.458  32.923  1.00 8.79   ? 234 SER A N   1 
ATOM   1858  C  CA  . SER A  1 234 ? 75.597  72.533  34.009  1.00 11.71  ? 234 SER A CA  1 
ATOM   1859  C  C   . SER A  1 234 ? 76.280  72.134  35.291  1.00 15.35  ? 234 SER A C   1 
ATOM   1860  O  O   . SER A  1 234 ? 77.163  71.258  35.312  1.00 19.85  ? 234 SER A O   1 
ATOM   1861  C  CB  . SER A  1 234 ? 74.434  71.648  33.743  1.00 8.57   ? 234 SER A CB  1 
ATOM   1862  O  OG  . SER A  1 234 ? 73.699  71.536  34.949  1.00 28.49  ? 234 SER A OG  1 
ATOM   1863  N  N   . PRO A  1 235 ? 75.871  72.747  36.398  1.00 16.44  ? 235 PRO A N   1 
ATOM   1864  C  CA  . PRO A  1 235 ? 76.501  72.409  37.671  1.00 18.54  ? 235 PRO A CA  1 
ATOM   1865  C  C   . PRO A  1 235 ? 76.077  71.108  38.231  1.00 20.79  ? 235 PRO A C   1 
ATOM   1866  O  O   . PRO A  1 235 ? 76.443  70.814  39.375  1.00 21.97  ? 235 PRO A O   1 
ATOM   1867  C  CB  . PRO A  1 235 ? 76.003  73.510  38.597  1.00 17.44  ? 235 PRO A CB  1 
ATOM   1868  C  CG  . PRO A  1 235 ? 74.657  73.792  38.086  1.00 11.56  ? 235 PRO A CG  1 
ATOM   1869  C  CD  . PRO A  1 235 ? 74.900  73.843  36.580  1.00 14.41  ? 235 PRO A CD  1 
ATOM   1870  N  N   . PHE A  1 236 ? 75.220  70.388  37.510  1.00 20.96  ? 236 PHE A N   1 
ATOM   1871  C  CA  . PHE A  1 236 ? 74.741  69.116  38.016  1.00 17.39  ? 236 PHE A CA  1 
ATOM   1872  C  C   . PHE A  1 236 ? 75.529  67.903  37.684  1.00 19.90  ? 236 PHE A C   1 
ATOM   1873  O  O   . PHE A  1 236 ? 75.216  66.827  38.177  1.00 26.77  ? 236 PHE A O   1 
ATOM   1874  C  CB  . PHE A  1 236 ? 73.307  68.929  37.695  1.00 10.54  ? 236 PHE A CB  1 
ATOM   1875  C  CG  . PHE A  1 236 ? 72.494  70.004  38.235  1.00 11.18  ? 236 PHE A CG  1 
ATOM   1876  C  CD1 . PHE A  1 236 ? 72.756  70.483  39.479  1.00 13.28  ? 236 PHE A CD1 1 
ATOM   1877  C  CD2 . PHE A  1 236 ? 71.559  70.657  37.469  1.00 16.79  ? 236 PHE A CD2 1 
ATOM   1878  C  CE1 . PHE A  1 236 ? 72.100  71.626  39.957  1.00 19.17  ? 236 PHE A CE1 1 
ATOM   1879  C  CE2 . PHE A  1 236 ? 70.909  71.795  37.941  1.00 12.36  ? 236 PHE A CE2 1 
ATOM   1880  C  CZ  . PHE A  1 236 ? 71.190  72.274  39.182  1.00 12.91  ? 236 PHE A CZ  1 
ATOM   1881  N  N   . TRP A  1 237 ? 76.527  68.064  36.825  1.00 16.46  ? 237 TRP A N   1 
ATOM   1882  C  CA  . TRP A  1 237 ? 77.435  67.006  36.457  1.00 13.33  ? 237 TRP A CA  1 
ATOM   1883  C  C   . TRP A  1 237 ? 78.697  67.722  36.045  1.00 14.77  ? 237 TRP A C   1 
ATOM   1884  O  O   . TRP A  1 237 ? 78.681  68.778  35.395  1.00 15.38  ? 237 TRP A O   1 
ATOM   1885  C  CB  . TRP A  1 237 ? 76.887  66.176  35.340  1.00 10.97  ? 237 TRP A CB  1 
ATOM   1886  C  CG  . TRP A  1 237 ? 76.567  66.924  34.118  1.00 10.62  ? 237 TRP A CG  1 
ATOM   1887  C  CD1 . TRP A  1 237 ? 77.403  67.178  33.101  1.00 11.69  ? 237 TRP A CD1 1 
ATOM   1888  C  CD2 . TRP A  1 237 ? 75.288  67.425  33.757  1.00 8.66   ? 237 TRP A CD2 1 
ATOM   1889  N  NE1 . TRP A  1 237 ? 76.705  67.775  32.070  1.00 12.14  ? 237 TRP A NE1 1 
ATOM   1890  C  CE2 . TRP A  1 237 ? 75.413  67.945  32.466  1.00 5.92   ? 237 TRP A CE2 1 
ATOM   1891  C  CE3 . TRP A  1 237 ? 74.032  67.462  34.391  1.00 16.05  ? 237 TRP A CE3 1 
ATOM   1892  C  CZ2 . TRP A  1 237 ? 74.341  68.497  31.786  1.00 7.67   ? 237 TRP A CZ2 1 
ATOM   1893  C  CZ3 . TRP A  1 237 ? 72.956  67.987  33.736  1.00 2.00   ? 237 TRP A CZ3 1 
ATOM   1894  C  CH2 . TRP A  1 237 ? 73.128  68.491  32.436  1.00 8.77   ? 237 TRP A CH2 1 
ATOM   1895  N  N   . TYR A  1 238 ? 79.798  67.148  36.483  1.00 15.57  ? 238 TYR A N   1 
ATOM   1896  C  CA  . TYR A  1 238 ? 81.107  67.729  36.230  1.00 15.28  ? 238 TYR A CA  1 
ATOM   1897  C  C   . TYR A  1 238 ? 82.127  66.749  36.770  1.00 17.28  ? 238 TYR A C   1 
ATOM   1898  O  O   . TYR A  1 238 ? 81.795  65.649  37.181  1.00 17.69  ? 238 TYR A O   1 
ATOM   1899  C  CB  . TYR A  1 238 ? 81.167  69.072  36.972  1.00 14.16  ? 238 TYR A CB  1 
ATOM   1900  C  CG  . TYR A  1 238 ? 80.986  68.989  38.482  1.00 13.41  ? 238 TYR A CG  1 
ATOM   1901  C  CD1 . TYR A  1 238 ? 79.734  68.881  39.046  1.00 14.77  ? 238 TYR A CD1 1 
ATOM   1902  C  CD2 . TYR A  1 238 ? 82.102  68.971  39.352  1.00 14.63  ? 238 TYR A CD2 1 
ATOM   1903  C  CE1 . TYR A  1 238 ? 79.584  68.740  40.512  1.00 16.54  ? 238 TYR A CE1 1 
ATOM   1904  C  CE2 . TYR A  1 238 ? 81.943  68.856  40.789  1.00 9.56   ? 238 TYR A CE2 1 
ATOM   1905  C  CZ  . TYR A  1 238 ? 80.682  68.732  41.350  1.00 14.68  ? 238 TYR A CZ  1 
ATOM   1906  O  OH  . TYR A  1 238 ? 80.524  68.608  42.725  1.00 19.26  ? 238 TYR A OH  1 
ATOM   1907  N  N   . SER A  1 239 ? 83.369  67.171  36.806  1.00 20.83  ? 239 SER A N   1 
ATOM   1908  C  CA  . SER A  1 239 ? 84.414  66.325  37.331  1.00 22.41  ? 239 SER A CA  1 
ATOM   1909  C  C   . SER A  1 239 ? 85.574  67.198  37.799  1.00 23.96  ? 239 SER A C   1 
ATOM   1910  O  O   . SER A  1 239 ? 85.679  68.367  37.410  1.00 20.81  ? 239 SER A O   1 
ATOM   1911  C  CB  . SER A  1 239 ? 84.913  65.404  36.251  1.00 21.21  ? 239 SER A CB  1 
ATOM   1912  O  OG  . SER A  1 239 ? 85.520  66.202  35.287  1.00 24.32  ? 239 SER A OG  1 
ATOM   1913  N  N   . ILE A  1 240 ? 86.420  66.610  38.632  1.00 21.12  ? 240 ILE A N   1 
ATOM   1914  C  CA  . ILE A  1 240 ? 87.557  67.286  39.189  1.00 20.57  ? 240 ILE A CA  1 
ATOM   1915  C  C   . ILE A  1 240 ? 88.593  66.221  39.384  1.00 23.94  ? 240 ILE A C   1 
ATOM   1916  O  O   . ILE A  1 240 ? 88.269  65.027  39.525  1.00 25.61  ? 240 ILE A O   1 
ATOM   1917  C  CB  . ILE A  1 240 ? 87.265  67.863  40.572  1.00 21.97  ? 240 ILE A CB  1 
ATOM   1918  C  CG1 . ILE A  1 240 ? 86.841  66.777  41.549  1.00 16.74  ? 240 ILE A CG1 1 
ATOM   1919  C  CG2 . ILE A  1 240 ? 86.172  68.889  40.500  1.00 20.77  ? 240 ILE A CG2 1 
ATOM   1920  C  CD1 . ILE A  1 240 ? 86.925  67.247  42.984  1.00 23.14  ? 240 ILE A CD1 1 
ATOM   1921  N  N   . LYS A  1 241 ? 89.849  66.628  39.347  1.00 24.14  ? 241 LYS A N   1 
ATOM   1922  C  CA  . LYS A  1 241 ? 90.937  65.688  39.565  1.00 25.36  ? 241 LYS A CA  1 
ATOM   1923  C  C   . LYS A  1 241 ? 91.515  66.179  40.874  1.00 26.92  ? 241 LYS A C   1 
ATOM   1924  O  O   . LYS A  1 241 ? 91.554  67.389  41.123  1.00 25.74  ? 241 LYS A O   1 
ATOM   1925  C  CB  . LYS A  1 241 ? 91.987  65.833  38.498  1.00 22.53  ? 241 LYS A CB  1 
ATOM   1926  C  CG  . LYS A  1 241 ? 91.543  65.510  37.085  1.00 30.13  ? 241 LYS A CG  1 
ATOM   1927  C  CD  . LYS A  1 241 ? 92.756  65.757  36.210  1.00 34.72  ? 241 LYS A CD  1 
ATOM   1928  C  CE  . LYS A  1 241 ? 92.596  65.316  34.798  1.00 41.04  ? 241 LYS A CE  1 
ATOM   1929  N  NZ  . LYS A  1 241 ? 93.711  65.957  34.038  1.00 54.07  ? 241 LYS A NZ  1 
ATOM   1930  N  N   . ARG A  1 242 ? 91.913  65.267  41.740  1.00 24.01  ? 242 ARG A N   1 
ATOM   1931  C  CA  . ARG A  1 242 ? 92.497  65.683  43.000  1.00 26.25  ? 242 ARG A CA  1 
ATOM   1932  C  C   . ARG A  1 242 ? 93.398  64.581  43.478  1.00 27.92  ? 242 ARG A C   1 
ATOM   1933  O  O   . ARG A  1 242 ? 92.972  63.450  43.610  1.00 28.31  ? 242 ARG A O   1 
ATOM   1934  C  CB  . ARG A  1 242 ? 91.416  65.986  44.012  1.00 27.54  ? 242 ARG A CB  1 
ATOM   1935  C  CG  . ARG A  1 242 ? 91.902  65.971  45.429  1.00 28.78  ? 242 ARG A CG  1 
ATOM   1936  C  CD  . ARG A  1 242 ? 90.919  66.664  46.369  1.00 31.78  ? 242 ARG A CD  1 
ATOM   1937  N  NE  . ARG A  1 242 ? 90.931  68.092  46.133  1.00 29.80  ? 242 ARG A NE  1 
ATOM   1938  C  CZ  . ARG A  1 242 ? 90.985  68.990  47.098  1.00 34.59  ? 242 ARG A CZ  1 
ATOM   1939  N  NH1 . ARG A  1 242 ? 91.023  68.626  48.382  1.00 32.82  ? 242 ARG A NH1 1 
ATOM   1940  N  NH2 . ARG A  1 242 ? 91.045  70.257  46.758  1.00 36.00  ? 242 ARG A NH2 1 
ATOM   1941  N  N   . ALA A  1 243 ? 94.648  64.917  43.735  1.00 27.08  ? 243 ALA A N   1 
ATOM   1942  C  CA  . ALA A  1 243 ? 95.625  63.926  44.156  1.00 27.67  ? 243 ALA A CA  1 
ATOM   1943  C  C   . ALA A  1 243 ? 95.721  62.874  43.052  1.00 31.06  ? 243 ALA A C   1 
ATOM   1944  O  O   . ALA A  1 243 ? 95.918  63.220  41.874  1.00 34.68  ? 243 ALA A O   1 
ATOM   1945  C  CB  . ALA A  1 243 ? 95.235  63.292  45.449  1.00 22.87  ? 243 ALA A CB  1 
ATOM   1946  N  N   . SER A  1 244 ? 95.506  61.614  43.398  1.00 28.41  ? 244 SER A N   1 
ATOM   1947  C  CA  . SER A  1 244 ? 95.586  60.553  42.416  1.00 29.03  ? 244 SER A CA  1 
ATOM   1948  C  C   . SER A  1 244 ? 94.226  60.102  41.881  1.00 31.76  ? 244 SER A C   1 
ATOM   1949  O  O   . SER A  1 244 ? 94.151  59.121  41.132  1.00 39.60  ? 244 SER A O   1 
ATOM   1950  C  CB  . SER A  1 244 ? 96.296  59.364  43.035  1.00 22.75  ? 244 SER A CB  1 
ATOM   1951  O  OG  . SER A  1 244 ? 95.710  59.085  44.292  1.00 28.37  ? 244 SER A OG  1 
ATOM   1952  N  N   . ALA A  1 245 ? 93.153  60.808  42.214  1.00 27.71  ? 245 ALA A N   1 
ATOM   1953  C  CA  . ALA A  1 245 ? 91.843  60.396  41.758  1.00 25.21  ? 245 ALA A CA  1 
ATOM   1954  C  C   . ALA A  1 245 ? 91.267  61.311  40.726  1.00 27.18  ? 245 ALA A C   1 
ATOM   1955  O  O   . ALA A  1 245 ? 91.591  62.498  40.705  1.00 28.40  ? 245 ALA A O   1 
ATOM   1956  C  CB  . ALA A  1 245 ? 90.894  60.319  42.912  1.00 27.69  ? 245 ALA A CB  1 
ATOM   1957  N  N   . HIS A  1 246 ? 90.386  60.751  39.887  1.00 27.66  ? 246 HIS A N   1 
ATOM   1958  C  CA  . HIS A  1 246 ? 89.638  61.486  38.843  1.00 22.95  ? 246 HIS A CA  1 
ATOM   1959  C  C   . HIS A  1 246 ? 88.212  61.173  39.246  1.00 23.48  ? 246 HIS A C   1 
ATOM   1960  O  O   . HIS A  1 246 ? 87.775  60.025  39.186  1.00 24.84  ? 246 HIS A O   1 
ATOM   1961  C  CB  . HIS A  1 246 ? 89.910  60.935  37.455  1.00 21.04  ? 246 HIS A CB  1 
ATOM   1962  C  CG  . HIS A  1 246 ? 89.378  61.795  36.352  1.00 18.01  ? 246 HIS A CG  1 
ATOM   1963  N  ND1 . HIS A  1 246 ? 90.182  62.318  35.364  1.00 24.91  ? 246 HIS A ND1 1 
ATOM   1964  C  CD2 . HIS A  1 246 ? 88.122  62.192  36.063  1.00 17.55  ? 246 HIS A CD2 1 
ATOM   1965  C  CE1 . HIS A  1 246 ? 89.438  62.996  34.504  1.00 21.51  ? 246 HIS A CE1 1 
ATOM   1966  N  NE2 . HIS A  1 246 ? 88.177  62.929  34.907  1.00 11.37  ? 246 HIS A NE2 1 
ATOM   1967  N  N   . ILE A  1 247 ? 87.514  62.175  39.738  1.00 21.06  ? 247 ILE A N   1 
ATOM   1968  C  CA  . ILE A  1 247 ? 86.172  61.986  40.232  1.00 18.08  ? 247 ILE A CA  1 
ATOM   1969  C  C   . ILE A  1 247 ? 85.197  62.543  39.239  1.00 21.80  ? 247 ILE A C   1 
ATOM   1970  O  O   . ILE A  1 247 ? 85.405  63.639  38.750  1.00 29.38  ? 247 ILE A O   1 
ATOM   1971  C  CB  . ILE A  1 247 ? 86.060  62.749  41.511  1.00 15.53  ? 247 ILE A CB  1 
ATOM   1972  C  CG1 . ILE A  1 247 ? 87.164  62.279  42.419  1.00 10.18  ? 247 ILE A CG1 1 
ATOM   1973  C  CG2 . ILE A  1 247 ? 84.698  62.580  42.146  1.00 9.72   ? 247 ILE A CG2 1 
ATOM   1974  C  CD1 . ILE A  1 247 ? 87.165  62.955  43.689  1.00 17.30  ? 247 ILE A CD1 1 
ATOM   1975  N  N   . ILE A  1 248 ? 84.141  61.799  38.945  1.00 20.08  ? 248 ILE A N   1 
ATOM   1976  C  CA  . ILE A  1 248 ? 83.124  62.227  37.989  1.00 16.97  ? 248 ILE A CA  1 
ATOM   1977  C  C   . ILE A  1 248 ? 81.813  62.262  38.765  1.00 21.43  ? 248 ILE A C   1 
ATOM   1978  O  O   . ILE A  1 248 ? 81.490  61.252  39.402  1.00 25.22  ? 248 ILE A O   1 
ATOM   1979  C  CB  . ILE A  1 248 ? 82.983  61.204  36.889  1.00 13.10  ? 248 ILE A CB  1 
ATOM   1980  C  CG1 . ILE A  1 248 ? 84.236  61.178  36.034  1.00 9.87   ? 248 ILE A CG1 1 
ATOM   1981  C  CG2 . ILE A  1 248 ? 81.739  61.456  36.091  1.00 15.98  ? 248 ILE A CG2 1 
ATOM   1982  C  CD1 . ILE A  1 248 ? 84.095  60.351  34.800  1.00 8.52   ? 248 ILE A CD1 1 
ATOM   1983  N  N   . VAL A  1 249 ? 81.077  63.383  38.730  1.00 16.85  ? 249 VAL A N   1 
ATOM   1984  C  CA  . VAL A  1 249 ? 79.833  63.506  39.463  1.00 14.63  ? 249 VAL A CA  1 
ATOM   1985  C  C   . VAL A  1 249 ? 78.703  63.508  38.481  1.00 16.90  ? 249 VAL A C   1 
ATOM   1986  O  O   . VAL A  1 249 ? 78.784  64.225  37.503  1.00 18.36  ? 249 VAL A O   1 
ATOM   1987  C  CB  . VAL A  1 249 ? 79.789  64.799  40.258  1.00 15.77  ? 249 VAL A CB  1 
ATOM   1988  C  CG1 . VAL A  1 249 ? 78.470  64.924  41.023  1.00 14.94  ? 249 VAL A CG1 1 
ATOM   1989  C  CG2 . VAL A  1 249 ? 80.965  64.868  41.200  1.00 16.99  ? 249 VAL A CG2 1 
ATOM   1990  N  N   . LEU A  1 250 ? 77.609  62.795  38.778  1.00 15.39  ? 250 LEU A N   1 
ATOM   1991  C  CA  . LEU A  1 250 ? 76.464  62.709  37.876  1.00 11.75  ? 250 LEU A CA  1 
ATOM   1992  C  C   . LEU A  1 250 ? 75.188  63.143  38.555  1.00 15.33  ? 250 LEU A C   1 
ATOM   1993  O  O   . LEU A  1 250 ? 75.139  63.267  39.785  1.00 18.05  ? 250 LEU A O   1 
ATOM   1994  C  CB  . LEU A  1 250 ? 76.296  61.328  37.323  1.00 4.04   ? 250 LEU A CB  1 
ATOM   1995  C  CG  . LEU A  1 250 ? 77.513  60.898  36.517  1.00 8.40   ? 250 LEU A CG  1 
ATOM   1996  C  CD1 . LEU A  1 250 ? 77.275  59.522  35.988  1.00 10.30  ? 250 LEU A CD1 1 
ATOM   1997  C  CD2 . LEU A  1 250 ? 77.818  61.812  35.403  1.00 2.00   ? 250 LEU A CD2 1 
ATOM   1998  N  N   . SER A  1 251 ? 74.132  63.321  37.765  1.00 10.57  ? 251 SER A N   1 
ATOM   1999  C  CA  . SER A  1 251 ? 72.881  63.825  38.293  1.00 13.45  ? 251 SER A CA  1 
ATOM   2000  C  C   . SER A  1 251 ? 71.755  62.870  37.972  1.00 18.52  ? 251 SER A C   1 
ATOM   2001  O  O   . SER A  1 251 ? 71.269  62.846  36.860  1.00 15.95  ? 251 SER A O   1 
ATOM   2002  C  CB  . SER A  1 251 ? 72.642  65.226  37.666  1.00 13.94  ? 251 SER A CB  1 
ATOM   2003  O  OG  . SER A  1 251 ? 71.421  65.878  38.017  1.00 8.22   ? 251 SER A OG  1 
ATOM   2004  N  N   . SER A  1 252 ? 71.358  62.071  38.957  1.00 21.79  ? 252 SER A N   1 
ATOM   2005  C  CA  . SER A  1 252 ? 70.302  61.078  38.782  1.00 21.63  ? 252 SER A CA  1 
ATOM   2006  C  C   . SER A  1 252 ? 68.979  61.695  38.360  1.00 24.06  ? 252 SER A C   1 
ATOM   2007  O  O   . SER A  1 252 ? 68.141  61.039  37.704  1.00 29.60  ? 252 SER A O   1 
ATOM   2008  C  CB  . SER A  1 252 ? 70.055  60.307  40.094  1.00 17.34  ? 252 SER A CB  1 
ATOM   2009  O  OG  . SER A  1 252 ? 71.184  59.558  40.499  1.00 28.33  ? 252 SER A OG  1 
ATOM   2010  N  N   . TYR A  1 253 ? 68.790  62.947  38.738  1.00 20.62  ? 253 TYR A N   1 
ATOM   2011  C  CA  . TYR A  1 253 ? 67.535  63.635  38.471  1.00 19.12  ? 253 TYR A CA  1 
ATOM   2012  C  C   . TYR A  1 253 ? 67.528  64.680  37.362  1.00 21.33  ? 253 TYR A C   1 
ATOM   2013  O  O   . TYR A  1 253 ? 66.553  65.413  37.175  1.00 25.26  ? 253 TYR A O   1 
ATOM   2014  C  CB  . TYR A  1 253 ? 66.994  64.147  39.781  1.00 12.79  ? 253 TYR A CB  1 
ATOM   2015  C  CG  . TYR A  1 253 ? 66.957  63.003  40.747  1.00 13.63  ? 253 TYR A CG  1 
ATOM   2016  C  CD1 . TYR A  1 253 ? 65.978  62.046  40.633  1.00 13.36  ? 253 TYR A CD1 1 
ATOM   2017  C  CD2 . TYR A  1 253 ? 67.905  62.850  41.746  1.00 19.34  ? 253 TYR A CD2 1 
ATOM   2018  C  CE1 . TYR A  1 253 ? 65.918  60.928  41.489  1.00 18.30  ? 253 TYR A CE1 1 
ATOM   2019  C  CE2 . TYR A  1 253 ? 67.859  61.714  42.630  1.00 22.61  ? 253 TYR A CE2 1 
ATOM   2020  C  CZ  . TYR A  1 253 ? 66.854  60.758  42.472  1.00 20.10  ? 253 TYR A CZ  1 
ATOM   2021  O  OH  . TYR A  1 253 ? 66.806  59.555  43.156  1.00 29.02  ? 253 TYR A OH  1 
ATOM   2022  N  N   . SER A  1 254 ? 68.657  64.781  36.681  1.00 20.29  ? 254 SER A N   1 
ATOM   2023  C  CA  . SER A  1 254 ? 68.800  65.604  35.516  1.00 17.57  ? 254 SER A CA  1 
ATOM   2024  C  C   . SER A  1 254 ? 68.501  64.583  34.390  1.00 20.27  ? 254 SER A C   1 
ATOM   2025  O  O   . SER A  1 254 ? 68.073  63.472  34.684  1.00 31.55  ? 254 SER A O   1 
ATOM   2026  C  CB  . SER A  1 254 ? 70.234  66.097  35.445  1.00 20.29  ? 254 SER A CB  1 
ATOM   2027  O  OG  . SER A  1 254 ? 70.302  67.449  35.844  1.00 34.16  ? 254 SER A OG  1 
ATOM   2028  N  N   . ALA A  1 255 ? 68.728  64.905  33.119  1.00 22.54  ? 255 ALA A N   1 
ATOM   2029  C  CA  . ALA A  1 255 ? 68.472  63.959  32.012  1.00 18.91  ? 255 ALA A CA  1 
ATOM   2030  C  C   . ALA A  1 255 ? 69.723  63.265  31.464  1.00 22.56  ? 255 ALA A C   1 
ATOM   2031  O  O   . ALA A  1 255 ? 70.768  63.925  31.278  1.00 26.51  ? 255 ALA A O   1 
ATOM   2032  C  CB  . ALA A  1 255 ? 67.810  64.689  30.881  1.00 10.41  ? 255 ALA A CB  1 
ATOM   2033  N  N   . TYR A  1 256 ? 69.580  61.979  31.102  1.00 26.05  ? 256 TYR A N   1 
ATOM   2034  C  CA  . TYR A  1 256 ? 70.681  61.188  30.547  1.00 26.57  ? 256 TYR A CA  1 
ATOM   2035  C  C   . TYR A  1 256 ? 70.362  60.494  29.242  1.00 26.41  ? 256 TYR A C   1 
ATOM   2036  O  O   . TYR A  1 256 ? 71.134  59.638  28.816  1.00 26.69  ? 256 TYR A O   1 
ATOM   2037  C  CB  . TYR A  1 256 ? 71.207  60.164  31.551  1.00 21.84  ? 256 TYR A CB  1 
ATOM   2038  C  CG  . TYR A  1 256 ? 70.153  59.619  32.494  1.00 22.49  ? 256 TYR A CG  1 
ATOM   2039  C  CD1 . TYR A  1 256 ? 69.301  58.604  32.120  1.00 21.28  ? 256 TYR A CD1 1 
ATOM   2040  C  CD2 . TYR A  1 256 ? 70.064  60.088  33.786  1.00 23.68  ? 256 TYR A CD2 1 
ATOM   2041  C  CE1 . TYR A  1 256 ? 68.383  58.070  33.016  1.00 20.14  ? 256 TYR A CE1 1 
ATOM   2042  C  CE2 . TYR A  1 256 ? 69.166  59.560  34.669  1.00 23.61  ? 256 TYR A CE2 1 
ATOM   2043  C  CZ  . TYR A  1 256 ? 68.325  58.546  34.273  1.00 23.19  ? 256 TYR A CZ  1 
ATOM   2044  O  OH  . TYR A  1 256 ? 67.425  58.012  35.175  1.00 31.40  ? 256 TYR A OH  1 
ATOM   2045  N  N   . GLY A  1 257 ? 69.244  60.875  28.613  1.00 25.79  ? 257 GLY A N   1 
ATOM   2046  C  CA  . GLY A  1 257 ? 68.852  60.282  27.343  1.00 19.79  ? 257 GLY A CA  1 
ATOM   2047  C  C   . GLY A  1 257 ? 69.979  60.413  26.349  1.00 20.95  ? 257 GLY A C   1 
ATOM   2048  O  O   . GLY A  1 257 ? 70.904  61.205  26.542  1.00 26.37  ? 257 GLY A O   1 
ATOM   2049  N  N   . ARG A  1 258 ? 69.917  59.679  25.259  1.00 21.52  ? 258 ARG A N   1 
ATOM   2050  C  CA  . ARG A  1 258 ? 71.013  59.751  24.306  1.00 23.97  ? 258 ARG A CA  1 
ATOM   2051  C  C   . ARG A  1 258 ? 70.939  61.075  23.567  1.00 23.31  ? 258 ARG A C   1 
ATOM   2052  O  O   . ARG A  1 258 ? 69.905  61.443  23.033  1.00 25.86  ? 258 ARG A O   1 
ATOM   2053  C  CB  . ARG A  1 258 ? 70.919  58.596  23.325  1.00 25.00  ? 258 ARG A CB  1 
ATOM   2054  C  CG  . ARG A  1 258 ? 71.927  58.599  22.239  1.00 29.96  ? 258 ARG A CG  1 
ATOM   2055  C  CD  . ARG A  1 258 ? 71.319  57.921  21.037  1.00 48.50  ? 258 ARG A CD  1 
ATOM   2056  N  NE  . ARG A  1 258 ? 72.181  57.834  19.860  1.00 60.52  ? 258 ARG A NE  1 
ATOM   2057  C  CZ  . ARG A  1 258 ? 73.443  57.406  19.878  1.00 67.10  ? 258 ARG A CZ  1 
ATOM   2058  N  NH1 . ARG A  1 258 ? 74.020  57.020  21.018  1.00 71.71  ? 258 ARG A NH1 1 
ATOM   2059  N  NH2 . ARG A  1 258 ? 74.127  57.342  18.738  1.00 69.93  ? 258 ARG A NH2 1 
ATOM   2060  N  N   . GLY A  1 259 ? 72.056  61.780  23.523  1.00 21.14  ? 259 GLY A N   1 
ATOM   2061  C  CA  . GLY A  1 259 ? 72.089  63.054  22.858  1.00 16.81  ? 259 GLY A CA  1 
ATOM   2062  C  C   . GLY A  1 259 ? 71.906  64.243  23.808  1.00 21.12  ? 259 GLY A C   1 
ATOM   2063  O  O   . GLY A  1 259 ? 72.192  65.377  23.405  1.00 21.10  ? 259 GLY A O   1 
ATOM   2064  N  N   . THR A  1 260 ? 71.334  64.015  24.999  1.00 16.14  ? 260 THR A N   1 
ATOM   2065  C  CA  . THR A  1 260 ? 71.168  65.089  25.976  1.00 14.68  ? 260 THR A CA  1 
ATOM   2066  C  C   . THR A  1 260 ? 72.527  65.603  26.422  1.00 19.90  ? 260 THR A C   1 
ATOM   2067  O  O   . THR A  1 260 ? 73.548  64.919  26.246  1.00 24.47  ? 260 THR A O   1 
ATOM   2068  C  CB  . THR A  1 260 ? 70.424  64.574  27.163  1.00 12.74  ? 260 THR A CB  1 
ATOM   2069  O  OG1 . THR A  1 260 ? 71.167  63.519  27.793  1.00 20.12  ? 260 THR A OG1 1 
ATOM   2070  C  CG2 . THR A  1 260 ? 69.105  64.058  26.696  1.00 9.24   ? 260 THR A CG2 1 
ATOM   2071  N  N   . PRO A  1 261 ? 72.573  66.792  27.044  1.00 19.85  ? 261 PRO A N   1 
ATOM   2072  C  CA  . PRO A  1 261 ? 73.878  67.312  27.478  1.00 15.63  ? 261 PRO A CA  1 
ATOM   2073  C  C   . PRO A  1 261 ? 74.635  66.432  28.464  1.00 17.10  ? 261 PRO A C   1 
ATOM   2074  O  O   . PRO A  1 261 ? 75.836  66.224  28.298  1.00 18.46  ? 261 PRO A O   1 
ATOM   2075  C  CB  . PRO A  1 261 ? 73.512  68.655  28.067  1.00 13.27  ? 261 PRO A CB  1 
ATOM   2076  C  CG  . PRO A  1 261 ? 72.309  69.073  27.259  1.00 5.00   ? 261 PRO A CG  1 
ATOM   2077  C  CD  . PRO A  1 261 ? 71.516  67.816  27.196  1.00 15.11  ? 261 PRO A CD  1 
ATOM   2078  N  N   . GLN A  1 262 ? 73.960  65.877  29.473  1.00 19.88  ? 262 GLN A N   1 
ATOM   2079  C  CA  . GLN A  1 262 ? 74.692  65.046  30.426  1.00 13.33  ? 262 GLN A CA  1 
ATOM   2080  C  C   . GLN A  1 262 ? 75.263  63.828  29.743  1.00 21.27  ? 262 GLN A C   1 
ATOM   2081  O  O   . GLN A  1 262 ? 76.411  63.483  29.972  1.00 26.91  ? 262 GLN A O   1 
ATOM   2082  C  CB  . GLN A  1 262 ? 73.808  64.563  31.570  1.00 12.47  ? 262 GLN A CB  1 
ATOM   2083  C  CG  . GLN A  1 262 ? 74.595  63.864  32.703  1.00 9.29   ? 262 GLN A CG  1 
ATOM   2084  C  CD  . GLN A  1 262 ? 73.739  63.490  33.915  1.00 12.58  ? 262 GLN A CD  1 
ATOM   2085  O  OE1 . GLN A  1 262 ? 74.239  63.205  35.015  1.00 21.28  ? 262 GLN A OE1 1 
ATOM   2086  N  NE2 . GLN A  1 262 ? 72.444  63.479  33.722  1.00 20.04  ? 262 GLN A NE2 1 
ATOM   2087  N  N   . TYR A  1 263 ? 74.443  63.145  28.945  1.00 21.26  ? 263 TYR A N   1 
ATOM   2088  C  CA  . TYR A  1 263 ? 74.884  61.973  28.224  1.00 18.04  ? 263 TYR A CA  1 
ATOM   2089  C  C   . TYR A  1 263 ? 76.101  62.342  27.366  1.00 17.32  ? 263 TYR A C   1 
ATOM   2090  O  O   . TYR A  1 263 ? 77.169  61.777  27.498  1.00 19.44  ? 263 TYR A O   1 
ATOM   2091  C  CB  . TYR A  1 263 ? 73.756  61.508  27.365  1.00 18.04  ? 263 TYR A CB  1 
ATOM   2092  C  CG  . TYR A  1 263 ? 74.078  60.299  26.549  1.00 20.21  ? 263 TYR A CG  1 
ATOM   2093  C  CD1 . TYR A  1 263 ? 74.889  60.376  25.438  1.00 18.92  ? 263 TYR A CD1 1 
ATOM   2094  C  CD2 . TYR A  1 263 ? 73.508  59.100  26.839  1.00 22.41  ? 263 TYR A CD2 1 
ATOM   2095  C  CE1 . TYR A  1 263 ? 75.111  59.296  24.627  1.00 15.63  ? 263 TYR A CE1 1 
ATOM   2096  C  CE2 . TYR A  1 263 ? 73.731  58.013  26.037  1.00 25.86  ? 263 TYR A CE2 1 
ATOM   2097  C  CZ  . TYR A  1 263 ? 74.524  58.121  24.941  1.00 22.92  ? 263 TYR A CZ  1 
ATOM   2098  O  OH  . TYR A  1 263 ? 74.694  57.018  24.163  1.00 31.92  ? 263 TYR A OH  1 
ATOM   2099  N  N   . THR A  1 264 ? 75.969  63.344  26.527  1.00 17.66  ? 264 THR A N   1 
ATOM   2100  C  CA  . THR A  1 264 ? 77.083  63.789  25.690  1.00 19.91  ? 264 THR A CA  1 
ATOM   2101  C  C   . THR A  1 264 ? 78.352  64.136  26.488  1.00 26.15  ? 264 THR A C   1 
ATOM   2102  O  O   . THR A  1 264 ? 79.470  63.769  26.098  1.00 29.01  ? 264 THR A O   1 
ATOM   2103  C  CB  . THR A  1 264 ? 76.689  65.018  24.966  1.00 15.47  ? 264 THR A CB  1 
ATOM   2104  O  OG1 . THR A  1 264 ? 75.653  64.689  24.043  1.00 21.59  ? 264 THR A OG1 1 
ATOM   2105  C  CG2 . THR A  1 264 ? 77.819  65.506  24.187  1.00 23.57  ? 264 THR A CG2 1 
ATOM   2106  N  N   . TRP A  1 265 ? 78.194  64.897  27.567  1.00 24.46  ? 265 TRP A N   1 
ATOM   2107  C  CA  . TRP A  1 265 ? 79.327  65.252  28.411  1.00 21.64  ? 265 TRP A CA  1 
ATOM   2108  C  C   . TRP A  1 265 ? 80.081  64.031  28.929  1.00 21.56  ? 265 TRP A C   1 
ATOM   2109  O  O   . TRP A  1 265 ? 81.259  63.897  28.696  1.00 26.64  ? 265 TRP A O   1 
ATOM   2110  C  CB  . TRP A  1 265 ? 78.864  66.055  29.608  1.00 20.29  ? 265 TRP A CB  1 
ATOM   2111  C  CG  . TRP A  1 265 ? 79.995  66.426  30.479  1.00 18.41  ? 265 TRP A CG  1 
ATOM   2112  C  CD1 . TRP A  1 265 ? 80.911  67.386  30.236  1.00 22.97  ? 265 TRP A CD1 1 
ATOM   2113  C  CD2 . TRP A  1 265 ? 80.360  65.833  31.713  1.00 15.34  ? 265 TRP A CD2 1 
ATOM   2114  N  NE1 . TRP A  1 265 ? 81.835  67.437  31.238  1.00 23.78  ? 265 TRP A NE1 1 
ATOM   2115  C  CE2 . TRP A  1 265 ? 81.513  66.482  32.167  1.00 20.75  ? 265 TRP A CE2 1 
ATOM   2116  C  CE3 . TRP A  1 265 ? 79.832  64.800  32.480  1.00 20.38  ? 265 TRP A CE3 1 
ATOM   2117  C  CZ2 . TRP A  1 265 ? 82.160  66.132  33.368  1.00 18.22  ? 265 TRP A CZ2 1 
ATOM   2118  C  CZ3 . TRP A  1 265 ? 80.479  64.452  33.665  1.00 17.28  ? 265 TRP A CZ3 1 
ATOM   2119  C  CH2 . TRP A  1 265 ? 81.631  65.124  34.092  1.00 18.02  ? 265 TRP A CH2 1 
ATOM   2120  N  N   . LEU A  1 266 ? 79.380  63.155  29.643  1.00 21.74  ? 266 LEU A N   1 
ATOM   2121  C  CA  . LEU A  1 266 ? 79.965  61.936  30.222  1.00 22.74  ? 266 LEU A CA  1 
ATOM   2122  C  C   . LEU A  1 266 ? 80.728  61.108  29.211  1.00 25.90  ? 266 LEU A C   1 
ATOM   2123  O  O   . LEU A  1 266 ? 81.822  60.598  29.499  1.00 28.87  ? 266 LEU A O   1 
ATOM   2124  C  CB  . LEU A  1 266 ? 78.894  61.062  30.856  1.00 13.64  ? 266 LEU A CB  1 
ATOM   2125  C  CG  . LEU A  1 266 ? 79.343  59.761  31.457  1.00 8.77   ? 266 LEU A CG  1 
ATOM   2126  C  CD1 . LEU A  1 266 ? 80.475  59.951  32.435  1.00 3.37   ? 266 LEU A CD1 1 
ATOM   2127  C  CD2 . LEU A  1 266 ? 78.129  59.170  32.158  1.00 14.36  ? 266 LEU A CD2 1 
ATOM   2128  N  N   . LYS A  1 267 ? 80.173  60.989  28.018  1.00 24.16  ? 267 LYS A N   1 
ATOM   2129  C  CA  . LYS A  1 267 ? 80.824  60.191  27.014  1.00 24.05  ? 267 LYS A CA  1 
ATOM   2130  C  C   . LYS A  1 267 ? 82.195  60.745  26.725  1.00 22.50  ? 267 LYS A C   1 
ATOM   2131  O  O   . LYS A  1 267 ? 83.136  60.011  26.820  1.00 25.51  ? 267 LYS A O   1 
ATOM   2132  C  CB  . LYS A  1 267 ? 79.985  60.134  25.765  1.00 31.31  ? 267 LYS A CB  1 
ATOM   2133  C  CG  . LYS A  1 267 ? 80.333  59.005  24.818  1.00 43.00  ? 267 LYS A CG  1 
ATOM   2134  C  CD  . LYS A  1 267 ? 79.429  59.058  23.580  1.00 51.60  ? 267 LYS A CD  1 
ATOM   2135  C  CE  . LYS A  1 267 ? 79.790  57.999  22.541  1.00 60.02  ? 267 LYS A CE  1 
ATOM   2136  N  NZ  . LYS A  1 267 ? 78.908  58.088  21.334  1.00 70.17  ? 267 LYS A NZ  1 
ATOM   2137  N  N   . LYS A  1 268 ? 82.319  62.035  26.423  1.00 21.92  ? 268 LYS A N   1 
ATOM   2138  C  CA  . LYS A  1 268 ? 83.623  62.623  26.140  1.00 24.38  ? 268 LYS A CA  1 
ATOM   2139  C  C   . LYS A  1 268 ? 84.516  62.614  27.370  1.00 25.06  ? 268 LYS A C   1 
ATOM   2140  O  O   . LYS A  1 268 ? 85.728  62.425  27.279  1.00 22.18  ? 268 LYS A O   1 
ATOM   2141  C  CB  . LYS A  1 268 ? 83.488  64.051  25.658  1.00 29.04  ? 268 LYS A CB  1 
ATOM   2142  C  CG  . LYS A  1 268 ? 82.791  64.150  24.313  1.00 54.13  ? 268 LYS A CG  1 
ATOM   2143  C  CD  . LYS A  1 268 ? 82.607  65.616  23.814  1.00 70.34  ? 268 LYS A CD  1 
ATOM   2144  C  CE  . LYS A  1 268 ? 81.793  65.711  22.482  1.00 74.79  ? 268 LYS A CE  1 
ATOM   2145  N  NZ  . LYS A  1 268 ? 81.332  67.115  22.097  1.00 78.73  ? 268 LYS A NZ  1 
ATOM   2146  N  N   . GLU A  1 269 ? 83.920  62.836  28.529  1.00 25.04  ? 269 GLU A N   1 
ATOM   2147  C  CA  . GLU A  1 269 ? 84.709  62.859  29.727  1.00 22.20  ? 269 GLU A CA  1 
ATOM   2148  C  C   . GLU A  1 269 ? 85.382  61.541  29.972  1.00 24.49  ? 269 GLU A C   1 
ATOM   2149  O  O   . GLU A  1 269 ? 86.563  61.510  30.241  1.00 30.54  ? 269 GLU A O   1 
ATOM   2150  C  CB  . GLU A  1 269 ? 83.892  63.267  30.935  1.00 17.68  ? 269 GLU A CB  1 
ATOM   2151  C  CG  . GLU A  1 269 ? 84.704  63.366  32.212  1.00 18.92  ? 269 GLU A CG  1 
ATOM   2152  C  CD  . GLU A  1 269 ? 85.658  64.549  32.256  1.00 25.04  ? 269 GLU A CD  1 
ATOM   2153  O  OE1 . GLU A  1 269 ? 85.600  65.453  31.385  1.00 24.36  ? 269 GLU A OE1 1 
ATOM   2154  O  OE2 . GLU A  1 269 ? 86.486  64.572  33.186  1.00 26.92  ? 269 GLU A OE2 1 
ATOM   2155  N  N   . LEU A  1 270 ? 84.670  60.443  29.829  1.00 26.67  ? 270 LEU A N   1 
ATOM   2156  C  CA  . LEU A  1 270 ? 85.293  59.186  30.093  1.00 26.54  ? 270 LEU A CA  1 
ATOM   2157  C  C   . LEU A  1 270 ? 86.510  59.049  29.215  1.00 34.45  ? 270 LEU A C   1 
ATOM   2158  O  O   . LEU A  1 270 ? 87.505  58.484  29.640  1.00 41.81  ? 270 LEU A O   1 
ATOM   2159  C  CB  . LEU A  1 270 ? 84.320  58.074  29.869  1.00 18.61  ? 270 LEU A CB  1 
ATOM   2160  C  CG  . LEU A  1 270 ? 83.470  57.941  31.102  1.00 16.43  ? 270 LEU A CG  1 
ATOM   2161  C  CD1 . LEU A  1 270 ? 82.380  56.960  30.785  1.00 22.76  ? 270 LEU A CD1 1 
ATOM   2162  C  CD2 . LEU A  1 270 ? 84.290  57.481  32.279  1.00 4.95   ? 270 LEU A CD2 1 
ATOM   2163  N  N   . ARG A  1 271 ? 86.483  59.636  28.024  1.00 38.00  ? 271 ARG A N   1 
ATOM   2164  C  CA  . ARG A  1 271 ? 87.645  59.551  27.128  1.00 41.51  ? 271 ARG A CA  1 
ATOM   2165  C  C   . ARG A  1 271 ? 88.791  60.449  27.591  1.00 41.11  ? 271 ARG A C   1 
ATOM   2166  O  O   . ARG A  1 271 ? 89.921  60.249  27.189  1.00 49.23  ? 271 ARG A O   1 
ATOM   2167  C  CB  . ARG A  1 271 ? 87.318  59.961  25.680  1.00 48.47  ? 271 ARG A CB  1 
ATOM   2168  C  CG  . ARG A  1 271 ? 86.255  59.167  24.948  1.00 62.13  ? 271 ARG A CG  1 
ATOM   2169  C  CD  . ARG A  1 271 ? 86.260  59.586  23.488  1.00 75.13  ? 271 ARG A CD  1 
ATOM   2170  N  NE  . ARG A  1 271 ? 84.965  59.416  22.819  1.00 88.87  ? 271 ARG A NE  1 
ATOM   2171  C  CZ  . ARG A  1 271 ? 84.316  60.393  22.172  1.00 96.66  ? 271 ARG A CZ  1 
ATOM   2172  N  NH1 . ARG A  1 271 ? 84.844  61.620  22.112  1.00 101.34 ? 271 ARG A NH1 1 
ATOM   2173  N  NH2 . ARG A  1 271 ? 83.153  60.149  21.551  1.00 99.26  ? 271 ARG A NH2 1 
ATOM   2174  N  N   . LYS A  1 272 ? 88.511  61.490  28.356  1.00 36.74  ? 272 LYS A N   1 
ATOM   2175  C  CA  . LYS A  1 272 ? 89.593  62.363  28.780  1.00 32.32  ? 272 LYS A CA  1 
ATOM   2176  C  C   . LYS A  1 272 ? 90.358  61.860  30.002  1.00 29.83  ? 272 LYS A C   1 
ATOM   2177  O  O   . LYS A  1 272 ? 91.290  62.495  30.454  1.00 31.47  ? 272 LYS A O   1 
ATOM   2178  C  CB  . LYS A  1 272 ? 89.068  63.763  29.056  1.00 32.23  ? 272 LYS A CB  1 
ATOM   2179  C  CG  . LYS A  1 272 ? 88.260  64.435  27.935  1.00 39.73  ? 272 LYS A CG  1 
ATOM   2180  C  CD  . LYS A  1 272 ? 88.159  65.965  28.206  1.00 54.06  ? 272 LYS A CD  1 
ATOM   2181  C  CE  . LYS A  1 272 ? 86.849  66.692  27.695  1.00 65.45  ? 272 LYS A CE  1 
ATOM   2182  N  NZ  . LYS A  1 272 ? 85.666  66.860  28.685  1.00 75.80  ? 272 LYS A NZ  1 
ATOM   2183  N  N   . VAL A  1 273 ? 89.904  60.772  30.599  1.00 29.67  ? 273 VAL A N   1 
ATOM   2184  C  CA  . VAL A  1 273 ? 90.551  60.219  31.782  1.00 29.85  ? 273 VAL A CA  1 
ATOM   2185  C  C   . VAL A  1 273 ? 91.860  59.579  31.439  1.00 31.46  ? 273 VAL A C   1 
ATOM   2186  O  O   . VAL A  1 273 ? 91.889  58.721  30.575  1.00 39.53  ? 273 VAL A O   1 
ATOM   2187  C  CB  . VAL A  1 273 ? 89.723  59.104  32.397  1.00 27.99  ? 273 VAL A CB  1 
ATOM   2188  C  CG1 . VAL A  1 273 ? 90.391  58.641  33.617  1.00 33.55  ? 273 VAL A CG1 1 
ATOM   2189  C  CG2 . VAL A  1 273 ? 88.336  59.600  32.745  1.00 34.19  ? 273 VAL A CG2 1 
ATOM   2190  N  N   . LYS A  1 274 ? 92.927  59.919  32.149  1.00 32.57  ? 274 LYS A N   1 
ATOM   2191  C  CA  . LYS A  1 274 ? 94.239  59.333  31.875  1.00 33.64  ? 274 LYS A CA  1 
ATOM   2192  C  C   . LYS A  1 274 ? 94.664  58.672  33.121  1.00 33.33  ? 274 LYS A C   1 
ATOM   2193  O  O   . LYS A  1 274 ? 94.968  59.357  34.084  1.00 33.17  ? 274 LYS A O   1 
ATOM   2194  C  CB  . LYS A  1 274 ? 95.260  60.403  31.518  1.00 40.13  ? 274 LYS A CB  1 
ATOM   2195  C  CG  . LYS A  1 274 ? 95.199  60.893  30.065  1.00 51.27  ? 274 LYS A CG  1 
ATOM   2196  C  CD  . LYS A  1 274 ? 95.937  62.228  29.854  1.00 67.80  ? 274 LYS A CD  1 
ATOM   2197  C  CE  . LYS A  1 274 ? 97.443  62.171  30.239  1.00 78.59  ? 274 LYS A CE  1 
ATOM   2198  N  NZ  . LYS A  1 274 ? 98.208  63.482  30.068  1.00 83.30  ? 274 LYS A NZ  1 
ATOM   2199  N  N   . ARG A  1 275 ? 94.712  57.346  33.116  1.00 35.04  ? 275 ARG A N   1 
ATOM   2200  C  CA  . ARG A  1 275 ? 95.084  56.614  34.325  1.00 37.33  ? 275 ARG A CA  1 
ATOM   2201  C  C   . ARG A  1 275 ? 96.545  56.608  34.685  1.00 38.28  ? 275 ARG A C   1 
ATOM   2202  O  O   . ARG A  1 275 ? 96.915  56.221  35.779  1.00 39.80  ? 275 ARG A O   1 
ATOM   2203  C  CB  . ARG A  1 275 ? 94.564  55.211  34.250  1.00 33.62  ? 275 ARG A CB  1 
ATOM   2204  C  CG  . ARG A  1 275 ? 93.078  55.225  34.110  1.00 29.38  ? 275 ARG A CG  1 
ATOM   2205  C  CD  . ARG A  1 275 ? 92.401  55.017  35.419  1.00 27.22  ? 275 ARG A CD  1 
ATOM   2206  N  NE  . ARG A  1 275 ? 91.238  54.188  35.175  1.00 22.92  ? 275 ARG A NE  1 
ATOM   2207  C  CZ  . ARG A  1 275 ? 90.742  53.324  36.035  1.00 21.40  ? 275 ARG A CZ  1 
ATOM   2208  N  NH1 . ARG A  1 275 ? 91.262  53.163  37.239  1.00 18.94  ? 275 ARG A NH1 1 
ATOM   2209  N  NH2 . ARG A  1 275 ? 89.755  52.566  35.641  1.00 26.00  ? 275 ARG A NH2 1 
ATOM   2210  N  N   . SER A  1 276 ? 97.377  56.980  33.732  1.00 41.54  ? 276 SER A N   1 
ATOM   2211  C  CA  . SER A  1 276 ? 98.808  57.078  33.953  1.00 42.44  ? 276 SER A CA  1 
ATOM   2212  C  C   . SER A  1 276 ? 98.978  58.326  34.801  1.00 44.56  ? 276 SER A C   1 
ATOM   2213  O  O   . SER A  1 276 ? 100.012 58.521  35.423  1.00 51.37  ? 276 SER A O   1 
ATOM   2214  C  CB  . SER A  1 276 ? 99.511  57.310  32.617  1.00 45.59  ? 276 SER A CB  1 
ATOM   2215  O  OG  . SER A  1 276 ? 98.574  57.623  31.582  1.00 52.54  ? 276 SER A OG  1 
ATOM   2216  N  N   . GLU A  1 277 ? 97.963  59.189  34.779  1.00 41.60  ? 277 GLU A N   1 
ATOM   2217  C  CA  . GLU A  1 277 ? 97.965  60.428  35.509  1.00 39.18  ? 277 GLU A CA  1 
ATOM   2218  C  C   . GLU A  1 277 ? 97.170  60.300  36.783  1.00 37.96  ? 277 GLU A C   1 
ATOM   2219  O  O   . GLU A  1 277 ? 97.668  60.583  37.833  1.00 43.46  ? 277 GLU A O   1 
ATOM   2220  C  CB  . GLU A  1 277 ? 97.400  61.509  34.637  1.00 46.40  ? 277 GLU A CB  1 
ATOM   2221  C  CG  . GLU A  1 277 ? 97.424  62.870  35.257  1.00 66.19  ? 277 GLU A CG  1 
ATOM   2222  C  CD  . GLU A  1 277 ? 97.160  63.985  34.230  1.00 80.43  ? 277 GLU A CD  1 
ATOM   2223  O  OE1 . GLU A  1 277 ? 97.756  63.920  33.121  1.00 85.83  ? 277 GLU A OE1 1 
ATOM   2224  O  OE2 . GLU A  1 277 ? 96.379  64.930  34.539  1.00 87.78  ? 277 GLU A OE2 1 
ATOM   2225  N  N   . THR A  1 278 ? 95.923  59.897  36.725  1.00 35.02  ? 278 THR A N   1 
ATOM   2226  C  CA  . THR A  1 278 ? 95.176  59.745  37.960  1.00 30.55  ? 278 THR A CA  1 
ATOM   2227  C  C   . THR A  1 278 ? 94.709  58.329  37.878  1.00 35.31  ? 278 THR A C   1 
ATOM   2228  O  O   . THR A  1 278 ? 93.814  58.002  37.109  1.00 40.37  ? 278 THR A O   1 
ATOM   2229  C  CB  . THR A  1 278 ? 93.979  60.660  37.999  1.00 29.00  ? 278 THR A CB  1 
ATOM   2230  O  OG1 . THR A  1 278 ? 93.333  60.658  36.715  1.00 32.11  ? 278 THR A OG1 1 
ATOM   2231  C  CG2 . THR A  1 278 ? 94.403  62.036  38.315  1.00 25.83  ? 278 THR A CG2 1 
ATOM   2232  N  N   . PRO A  1 279 ? 95.393  57.443  38.573  1.00 34.77  ? 279 PRO A N   1 
ATOM   2233  C  CA  . PRO A  1 279 ? 95.067  56.017  38.592  1.00 34.89  ? 279 PRO A CA  1 
ATOM   2234  C  C   . PRO A  1 279 ? 93.660  55.646  39.061  1.00 35.20  ? 279 PRO A C   1 
ATOM   2235  O  O   . PRO A  1 279 ? 93.012  54.748  38.515  1.00 34.56  ? 279 PRO A O   1 
ATOM   2236  C  CB  . PRO A  1 279 ? 96.115  55.456  39.539  1.00 38.53  ? 279 PRO A CB  1 
ATOM   2237  C  CG  . PRO A  1 279 ? 96.479  56.635  40.403  1.00 35.65  ? 279 PRO A CG  1 
ATOM   2238  C  CD  . PRO A  1 279 ? 96.555  57.744  39.421  1.00 31.56  ? 279 PRO A CD  1 
ATOM   2239  N  N   . TRP A  1 280 ? 93.174  56.354  40.069  1.00 32.75  ? 280 TRP A N   1 
ATOM   2240  C  CA  . TRP A  1 280 ? 91.857  56.058  40.627  1.00 28.27  ? 280 TRP A CA  1 
ATOM   2241  C  C   . TRP A  1 280 ? 90.703  56.767  40.002  1.00 28.27  ? 280 TRP A C   1 
ATOM   2242  O  O   . TRP A  1 280 ? 90.665  57.986  39.990  1.00 32.62  ? 280 TRP A O   1 
ATOM   2243  C  CB  . TRP A  1 280 ? 91.896  56.315  42.098  1.00 28.19  ? 280 TRP A CB  1 
ATOM   2244  C  CG  . TRP A  1 280 ? 92.854  55.387  42.734  1.00 33.43  ? 280 TRP A CG  1 
ATOM   2245  C  CD1 . TRP A  1 280 ? 94.161  55.639  43.093  1.00 36.51  ? 280 TRP A CD1 1 
ATOM   2246  C  CD2 . TRP A  1 280 ? 92.579  54.052  43.131  1.00 33.68  ? 280 TRP A CD2 1 
ATOM   2247  N  NE1 . TRP A  1 280 ? 94.694  54.527  43.711  1.00 36.73  ? 280 TRP A NE1 1 
ATOM   2248  C  CE2 . TRP A  1 280 ? 93.744  53.544  43.747  1.00 31.13  ? 280 TRP A CE2 1 
ATOM   2249  C  CE3 . TRP A  1 280 ? 91.456  53.236  43.037  1.00 28.43  ? 280 TRP A CE3 1 
ATOM   2250  C  CZ2 . TRP A  1 280 ? 93.808  52.277  44.263  1.00 30.97  ? 280 TRP A CZ2 1 
ATOM   2251  C  CZ3 . TRP A  1 280 ? 91.518  51.981  43.545  1.00 31.76  ? 280 TRP A CZ3 1 
ATOM   2252  C  CH2 . TRP A  1 280 ? 92.688  51.502  44.158  1.00 32.28  ? 280 TRP A CH2 1 
ATOM   2253  N  N   . LEU A  1 281 ? 89.748  56.000  39.495  1.00 28.81  ? 281 LEU A N   1 
ATOM   2254  C  CA  . LEU A  1 281 ? 88.601  56.576  38.821  1.00 27.17  ? 281 LEU A CA  1 
ATOM   2255  C  C   . LEU A  1 281 ? 87.382  56.315  39.650  1.00 31.53  ? 281 LEU A C   1 
ATOM   2256  O  O   . LEU A  1 281 ? 86.962  55.165  39.739  1.00 35.24  ? 281 LEU A O   1 
ATOM   2257  C  CB  . LEU A  1 281 ? 88.420  55.924  37.461  1.00 22.69  ? 281 LEU A CB  1 
ATOM   2258  C  CG  . LEU A  1 281 ? 87.260  56.396  36.579  1.00 21.88  ? 281 LEU A CG  1 
ATOM   2259  C  CD1 . LEU A  1 281 ? 87.423  57.887  36.257  1.00 19.88  ? 281 LEU A CD1 1 
ATOM   2260  C  CD2 . LEU A  1 281 ? 87.179  55.599  35.273  1.00 14.80  ? 281 LEU A CD2 1 
ATOM   2261  N  N   . ILE A  1 282 ? 86.793  57.388  40.193  1.00 31.01  ? 282 ILE A N   1 
ATOM   2262  C  CA  . ILE A  1 282 ? 85.611  57.352  41.067  1.00 23.08  ? 282 ILE A CA  1 
ATOM   2263  C  C   . ILE A  1 282 ? 84.419  58.068  40.462  1.00 20.93  ? 282 ILE A C   1 
ATOM   2264  O  O   . ILE A  1 282 ? 84.554  59.159  39.921  1.00 28.72  ? 282 ILE A O   1 
ATOM   2265  C  CB  . ILE A  1 282 ? 85.933  58.096  42.373  1.00 22.28  ? 282 ILE A CB  1 
ATOM   2266  C  CG1 . ILE A  1 282 ? 87.162  57.473  43.003  1.00 27.30  ? 282 ILE A CG1 1 
ATOM   2267  C  CG2 . ILE A  1 282 ? 84.789  58.039  43.345  1.00 20.53  ? 282 ILE A CG2 1 
ATOM   2268  C  CD1 . ILE A  1 282 ? 87.762  58.303  44.080  1.00 28.07  ? 282 ILE A CD1 1 
ATOM   2269  N  N   . VAL A  1 283 ? 83.241  57.511  40.656  1.00 14.44  ? 283 VAL A N   1 
ATOM   2270  C  CA  . VAL A  1 283 ? 82.027  58.121  40.160  1.00 14.86  ? 283 VAL A CA  1 
ATOM   2271  C  C   . VAL A  1 283 ? 81.015  58.292  41.270  1.00 19.79  ? 283 VAL A C   1 
ATOM   2272  O  O   . VAL A  1 283 ? 80.805  57.387  42.081  1.00 21.64  ? 283 VAL A O   1 
ATOM   2273  C  CB  . VAL A  1 283 ? 81.386  57.266  39.147  1.00 12.97  ? 283 VAL A CB  1 
ATOM   2274  C  CG1 . VAL A  1 283 ? 80.035  57.765  38.873  1.00 8.41   ? 283 VAL A CG1 1 
ATOM   2275  C  CG2 . VAL A  1 283 ? 82.249  57.234  37.877  1.00 14.25  ? 283 VAL A CG2 1 
ATOM   2276  N  N   . LEU A  1 284 ? 80.355  59.440  41.281  1.00 19.76  ? 284 LEU A N   1 
ATOM   2277  C  CA  . LEU A  1 284 ? 79.371  59.752  42.298  1.00 15.45  ? 284 LEU A CA  1 
ATOM   2278  C  C   . LEU A  1 284 ? 78.042  59.981  41.674  1.00 16.43  ? 284 LEU A C   1 
ATOM   2279  O  O   . LEU A  1 284 ? 77.959  60.570  40.609  1.00 20.39  ? 284 LEU A O   1 
ATOM   2280  C  CB  . LEU A  1 284 ? 79.745  61.031  43.009  1.00 16.30  ? 284 LEU A CB  1 
ATOM   2281  C  CG  . LEU A  1 284 ? 81.137  61.183  43.604  1.00 16.76  ? 284 LEU A CG  1 
ATOM   2282  C  CD1 . LEU A  1 284 ? 81.152  62.507  44.282  1.00 7.50   ? 284 LEU A CD1 1 
ATOM   2283  C  CD2 . LEU A  1 284 ? 81.458  60.079  44.557  1.00 17.94  ? 284 LEU A CD2 1 
ATOM   2284  N  N   . MET A  1 285 ? 76.990  59.568  42.361  1.00 13.93  ? 285 MET A N   1 
ATOM   2285  C  CA  . MET A  1 285 ? 75.606  59.734  41.903  1.00 17.36  ? 285 MET A CA  1 
ATOM   2286  C  C   . MET A  1 285 ? 74.730  59.488  43.129  1.00 21.32  ? 285 MET A C   1 
ATOM   2287  O  O   . MET A  1 285 ? 75.182  58.853  44.103  1.00 25.10  ? 285 MET A O   1 
ATOM   2288  C  CB  . MET A  1 285 ? 75.261  58.777  40.762  1.00 16.90  ? 285 MET A CB  1 
ATOM   2289  C  CG  . MET A  1 285 ? 75.530  57.310  41.092  1.00 23.30  ? 285 MET A CG  1 
ATOM   2290  S  SD  . MET A  1 285 ? 75.012  56.124  39.897  1.00 25.14  ? 285 MET A SD  1 
ATOM   2291  C  CE  . MET A  1 285 ? 76.337  56.196  38.705  1.00 17.42  ? 285 MET A CE  1 
ATOM   2292  N  N   . HIS A  1 286 ? 73.498  59.994  43.115  1.00 22.10  ? 286 HIS A N   1 
ATOM   2293  C  CA  . HIS A  1 286 ? 72.673  59.839  44.291  1.00 15.00  ? 286 HIS A CA  1 
ATOM   2294  C  C   . HIS A  1 286 ? 72.017  58.509  44.321  1.00 18.40  ? 286 HIS A C   1 
ATOM   2295  O  O   . HIS A  1 286 ? 72.187  57.798  45.313  1.00 25.67  ? 286 HIS A O   1 
ATOM   2296  C  CB  . HIS A  1 286 ? 71.612  60.919  44.374  1.00 9.07   ? 286 HIS A CB  1 
ATOM   2297  C  CG  . HIS A  1 286 ? 70.820  60.874  45.619  1.00 10.20  ? 286 HIS A CG  1 
ATOM   2298  N  ND1 . HIS A  1 286 ? 71.365  61.131  46.860  1.00 15.78  ? 286 HIS A ND1 1 
ATOM   2299  C  CD2 . HIS A  1 286 ? 69.491  60.629  45.838  1.00 14.62  ? 286 HIS A CD2 1 
ATOM   2300  C  CE1 . HIS A  1 286 ? 70.408  61.053  47.786  1.00 12.66  ? 286 HIS A CE1 1 
ATOM   2301  N  NE2 . HIS A  1 286 ? 69.273  60.750  47.200  1.00 8.22   ? 286 HIS A NE2 1 
ATOM   2302  N  N   . SER A  1 287 ? 71.219  58.205  43.286  1.00 21.81  ? 287 SER A N   1 
ATOM   2303  C  CA  . SER A  1 287 ? 70.467  56.919  43.160  1.00 22.65  ? 287 SER A CA  1 
ATOM   2304  C  C   . SER A  1 287 ? 71.386  55.823  42.716  1.00 26.16  ? 287 SER A C   1 
ATOM   2305  O  O   . SER A  1 287 ? 71.901  55.863  41.575  1.00 36.45  ? 287 SER A O   1 
ATOM   2306  C  CB  . SER A  1 287 ? 69.368  56.993  42.117  1.00 14.80  ? 287 SER A CB  1 
ATOM   2307  O  OG  . SER A  1 287 ? 68.258  56.257  42.575  1.00 31.30  ? 287 SER A OG  1 
ATOM   2308  N  N   . PRO A  1 288 ? 71.557  54.805  43.561  1.00 20.67  ? 288 PRO A N   1 
ATOM   2309  C  CA  . PRO A  1 288 ? 72.389  53.615  43.410  1.00 17.61  ? 288 PRO A CA  1 
ATOM   2310  C  C   . PRO A  1 288 ? 71.926  52.645  42.285  1.00 19.31  ? 288 PRO A C   1 
ATOM   2311  O  O   . PRO A  1 288 ? 70.713  52.335  42.184  1.00 26.18  ? 288 PRO A O   1 
ATOM   2312  C  CB  . PRO A  1 288 ? 72.279  53.015  44.783  1.00 14.09  ? 288 PRO A CB  1 
ATOM   2313  C  CG  . PRO A  1 288 ? 70.881  53.285  45.147  1.00 11.11  ? 288 PRO A CG  1 
ATOM   2314  C  CD  . PRO A  1 288 ? 70.659  54.677  44.724  1.00 19.11  ? 288 PRO A CD  1 
ATOM   2315  N  N   . LEU A  1 289 ? 72.873  52.197  41.434  1.00 14.88  ? 289 LEU A N   1 
ATOM   2316  C  CA  . LEU A  1 289 ? 72.588  51.289  40.298  1.00 16.05  ? 289 LEU A CA  1 
ATOM   2317  C  C   . LEU A  1 289 ? 72.288  49.860  40.742  1.00 21.84  ? 289 LEU A C   1 
ATOM   2318  O  O   . LEU A  1 289 ? 71.457  49.121  40.131  1.00 24.38  ? 289 LEU A O   1 
ATOM   2319  C  CB  . LEU A  1 289 ? 73.754  51.260  39.313  1.00 13.30  ? 289 LEU A CB  1 
ATOM   2320  C  CG  . LEU A  1 289 ? 74.088  52.613  38.682  1.00 19.08  ? 289 LEU A CG  1 
ATOM   2321  C  CD1 . LEU A  1 289 ? 75.087  52.463  37.560  1.00 13.19  ? 289 LEU A CD1 1 
ATOM   2322  C  CD2 . LEU A  1 289 ? 72.812  53.276  38.140  1.00 21.31  ? 289 LEU A CD2 1 
ATOM   2323  N  N   . TYR A  1 290 ? 73.012  49.480  41.800  1.00 17.55  ? 290 TYR A N   1 
ATOM   2324  C  CA  . TYR A  1 290 ? 72.927  48.172  42.441  1.00 14.78  ? 290 TYR A CA  1 
ATOM   2325  C  C   . TYR A  1 290 ? 72.502  48.443  43.892  1.00 18.39  ? 290 TYR A C   1 
ATOM   2326  O  O   . TYR A  1 290 ? 73.195  49.189  44.623  1.00 25.51  ? 290 TYR A O   1 
ATOM   2327  C  CB  . TYR A  1 290 ? 74.312  47.467  42.385  1.00 9.86   ? 290 TYR A CB  1 
ATOM   2328  C  CG  . TYR A  1 290 ? 74.623  46.809  41.079  1.00 11.03  ? 290 TYR A CG  1 
ATOM   2329  C  CD1 . TYR A  1 290 ? 74.109  45.549  40.781  1.00 12.00  ? 290 TYR A CD1 1 
ATOM   2330  C  CD2 . TYR A  1 290 ? 75.317  47.481  40.066  1.00 9.43   ? 290 TYR A CD2 1 
ATOM   2331  C  CE1 . TYR A  1 290 ? 74.245  44.965  39.508  1.00 11.35  ? 290 TYR A CE1 1 
ATOM   2332  C  CE2 . TYR A  1 290 ? 75.464  46.910  38.802  1.00 11.13  ? 290 TYR A CE2 1 
ATOM   2333  C  CZ  . TYR A  1 290 ? 74.910  45.655  38.551  1.00 15.85  ? 290 TYR A CZ  1 
ATOM   2334  O  OH  . TYR A  1 290 ? 75.003  45.117  37.315  1.00 17.62  ? 290 TYR A OH  1 
ATOM   2335  N  N   . ASN A  1 291 ? 71.363  47.878  44.312  1.00 19.70  ? 291 ASN A N   1 
ATOM   2336  C  CA  . ASN A  1 291 ? 70.835  48.059  45.683  1.00 23.40  ? 291 ASN A CA  1 
ATOM   2337  C  C   . ASN A  1 291 ? 69.812  46.952  46.041  1.00 29.83  ? 291 ASN A C   1 
ATOM   2338  O  O   . ASN A  1 291 ? 68.803  46.774  45.332  1.00 37.01  ? 291 ASN A O   1 
ATOM   2339  C  CB  . ASN A  1 291 ? 70.192  49.453  45.784  1.00 27.48  ? 291 ASN A CB  1 
ATOM   2340  C  CG  . ASN A  1 291 ? 69.120  49.567  46.860  1.00 32.28  ? 291 ASN A CG  1 
ATOM   2341  O  OD1 . ASN A  1 291 ? 67.987  49.957  46.564  1.00 32.53  ? 291 ASN A OD1 1 
ATOM   2342  N  ND2 . ASN A  1 291 ? 69.481  49.287  48.115  1.00 33.36  ? 291 ASN A ND2 1 
ATOM   2343  N  N   . SER A  1 292 ? 70.065  46.203  47.120  1.00 22.48  ? 292 SER A N   1 
ATOM   2344  C  CA  . SER A  1 292 ? 69.157  45.143  47.503  1.00 15.49  ? 292 SER A CA  1 
ATOM   2345  C  C   . SER A  1 292 ? 68.257  45.431  48.666  1.00 20.92  ? 292 SER A C   1 
ATOM   2346  O  O   . SER A  1 292 ? 67.864  44.478  49.362  1.00 19.69  ? 292 SER A O   1 
ATOM   2347  C  CB  . SER A  1 292 ? 69.929  43.895  47.825  1.00 17.60  ? 292 SER A CB  1 
ATOM   2348  O  OG  . SER A  1 292 ? 70.791  44.103  48.911  1.00 23.93  ? 292 SER A OG  1 
ATOM   2349  N  N   . TYR A  1 293 ? 68.031  46.716  48.986  1.00 20.85  ? 293 TYR A N   1 
ATOM   2350  C  CA  . TYR A  1 293 ? 67.093  47.060  50.064  1.00 19.78  ? 293 TYR A CA  1 
ATOM   2351  C  C   . TYR A  1 293 ? 65.760  47.273  49.398  1.00 24.76  ? 293 TYR A C   1 
ATOM   2352  O  O   . TYR A  1 293 ? 65.698  47.590  48.213  1.00 26.59  ? 293 TYR A O   1 
ATOM   2353  C  CB  . TYR A  1 293 ? 67.448  48.330  50.745  1.00 20.17  ? 293 TYR A CB  1 
ATOM   2354  C  CG  . TYR A  1 293 ? 68.595  48.197  51.662  1.00 23.95  ? 293 TYR A CG  1 
ATOM   2355  C  CD1 . TYR A  1 293 ? 69.874  48.001  51.172  1.00 26.09  ? 293 TYR A CD1 1 
ATOM   2356  C  CD2 . TYR A  1 293 ? 68.420  48.283  53.032  1.00 20.57  ? 293 TYR A CD2 1 
ATOM   2357  C  CE1 . TYR A  1 293 ? 70.955  47.894  52.034  1.00 25.30  ? 293 TYR A CE1 1 
ATOM   2358  C  CE2 . TYR A  1 293 ? 69.470  48.179  53.879  1.00 16.46  ? 293 TYR A CE2 1 
ATOM   2359  C  CZ  . TYR A  1 293 ? 70.739  47.977  53.389  1.00 23.24  ? 293 TYR A CZ  1 
ATOM   2360  O  OH  . TYR A  1 293 ? 71.806  47.815  54.261  1.00 27.38  ? 293 TYR A OH  1 
ATOM   2361  N  N   . ASN A  1 294 ? 64.685  47.219  50.163  1.00 31.32  ? 294 ASN A N   1 
ATOM   2362  C  CA  . ASN A  1 294 ? 63.373  47.372  49.548  1.00 32.95  ? 294 ASN A CA  1 
ATOM   2363  C  C   . ASN A  1 294 ? 63.088  48.783  49.150  1.00 37.20  ? 294 ASN A C   1 
ATOM   2364  O  O   . ASN A  1 294 ? 62.471  49.022  48.121  1.00 43.30  ? 294 ASN A O   1 
ATOM   2365  C  CB  . ASN A  1 294 ? 62.282  46.884  50.481  1.00 36.42  ? 294 ASN A CB  1 
ATOM   2366  C  CG  . ASN A  1 294 ? 62.299  45.388  50.670  1.00 46.20  ? 294 ASN A CG  1 
ATOM   2367  O  OD1 . ASN A  1 294 ? 61.555  44.669  50.023  1.00 57.11  ? 294 ASN A OD1 1 
ATOM   2368  N  ND2 . ASN A  1 294 ? 63.155  44.909  51.562  1.00 53.59  ? 294 ASN A ND2 1 
ATOM   2369  N  N   . HIS A  1 295 ? 63.515  49.720  49.991  1.00 38.96  ? 295 HIS A N   1 
ATOM   2370  C  CA  . HIS A  1 295 ? 63.312  51.158  49.765  1.00 33.43  ? 295 HIS A CA  1 
ATOM   2371  C  C   . HIS A  1 295 ? 64.090  51.619  48.563  1.00 29.58  ? 295 HIS A C   1 
ATOM   2372  O  O   . HIS A  1 295 ? 65.301  51.580  48.598  1.00 36.37  ? 295 HIS A O   1 
ATOM   2373  C  CB  . HIS A  1 295 ? 63.837  51.904  50.964  1.00 35.86  ? 295 HIS A CB  1 
ATOM   2374  C  CG  . HIS A  1 295 ? 63.461  53.343  50.984  1.00 38.63  ? 295 HIS A CG  1 
ATOM   2375  N  ND1 . HIS A  1 295 ? 64.297  54.324  51.487  1.00 36.81  ? 295 HIS A ND1 1 
ATOM   2376  C  CD2 . HIS A  1 295 ? 62.318  53.967  50.612  1.00 34.03  ? 295 HIS A CD2 1 
ATOM   2377  C  CE1 . HIS A  1 295 ? 63.679  55.488  51.429  1.00 38.28  ? 295 HIS A CE1 1 
ATOM   2378  N  NE2 . HIS A  1 295 ? 62.478  55.297  50.903  1.00 38.49  ? 295 HIS A NE2 1 
ATOM   2379  N  N   . HIS A  1 296 ? 63.412  52.131  47.545  1.00 22.63  ? 296 HIS A N   1 
ATOM   2380  C  CA  . HIS A  1 296 ? 64.077  52.590  46.313  1.00 24.72  ? 296 HIS A CA  1 
ATOM   2381  C  C   . HIS A  1 296 ? 64.675  51.463  45.536  1.00 27.26  ? 296 HIS A C   1 
ATOM   2382  O  O   . HIS A  1 296 ? 65.648  51.647  44.818  1.00 35.91  ? 296 HIS A O   1 
ATOM   2383  C  CB  . HIS A  1 296 ? 65.182  53.563  46.607  1.00 23.86  ? 296 HIS A CB  1 
ATOM   2384  C  CG  . HIS A  1 296 ? 64.713  54.796  47.285  1.00 27.88  ? 296 HIS A CG  1 
ATOM   2385  N  ND1 . HIS A  1 296 ? 63.610  55.501  46.845  1.00 26.48  ? 296 HIS A ND1 1 
ATOM   2386  C  CD2 . HIS A  1 296 ? 65.199  55.468  48.348  1.00 21.13  ? 296 HIS A CD2 1 
ATOM   2387  C  CE1 . HIS A  1 296 ? 63.441  56.562  47.603  1.00 28.21  ? 296 HIS A CE1 1 
ATOM   2388  N  NE2 . HIS A  1 296 ? 64.396  56.569  48.521  1.00 30.70  ? 296 HIS A NE2 1 
ATOM   2389  N  N   . PHE A  1 297 ? 64.076  50.294  45.663  1.00 27.43  ? 297 PHE A N   1 
ATOM   2390  C  CA  . PHE A  1 297 ? 64.575  49.135  44.988  1.00 26.83  ? 297 PHE A CA  1 
ATOM   2391  C  C   . PHE A  1 297 ? 64.316  49.297  43.515  1.00 28.27  ? 297 PHE A C   1 
ATOM   2392  O  O   . PHE A  1 297 ? 63.201  49.572  43.150  1.00 31.01  ? 297 PHE A O   1 
ATOM   2393  C  CB  . PHE A  1 297 ? 63.909  47.887  45.535  1.00 23.13  ? 297 PHE A CB  1 
ATOM   2394  C  CG  . PHE A  1 297 ? 64.282  46.649  44.801  1.00 25.70  ? 297 PHE A CG  1 
ATOM   2395  C  CD1 . PHE A  1 297 ? 65.599  46.176  44.823  1.00 24.65  ? 297 PHE A CD1 1 
ATOM   2396  C  CD2 . PHE A  1 297 ? 63.340  45.985  44.021  1.00 31.00  ? 297 PHE A CD2 1 
ATOM   2397  C  CE1 . PHE A  1 297 ? 65.968  45.069  44.071  1.00 23.73  ? 297 PHE A CE1 1 
ATOM   2398  C  CE2 . PHE A  1 297 ? 63.698  44.870  43.258  1.00 30.96  ? 297 PHE A CE2 1 
ATOM   2399  C  CZ  . PHE A  1 297 ? 65.014  44.414  43.282  1.00 28.34  ? 297 PHE A CZ  1 
ATOM   2400  N  N   . MET A  1 298 ? 65.381  49.231  42.702  1.00 31.91  ? 298 MET A N   1 
ATOM   2401  C  CA  . MET A  1 298 ? 65.334  49.329  41.234  1.00 28.17  ? 298 MET A CA  1 
ATOM   2402  C  C   . MET A  1 298 ? 65.098  50.700  40.559  1.00 26.53  ? 298 MET A C   1 
ATOM   2403  O  O   . MET A  1 298 ? 64.767  50.775  39.362  1.00 30.39  ? 298 MET A O   1 
ATOM   2404  C  CB  . MET A  1 298 ? 64.349  48.309  40.646  1.00 27.16  ? 298 MET A CB  1 
ATOM   2405  C  CG  . MET A  1 298 ? 64.738  46.829  40.755  1.00 28.98  ? 298 MET A CG  1 
ATOM   2406  S  SD  . MET A  1 298 ? 63.783  45.792  39.610  1.00 30.49  ? 298 MET A SD  1 
ATOM   2407  C  CE  . MET A  1 298 ? 62.200  45.843  40.313  1.00 25.09  ? 298 MET A CE  1 
ATOM   2408  N  N   . GLU A  1 299 ? 65.301  51.777  41.299  1.00 19.12  ? 299 GLU A N   1 
ATOM   2409  C  CA  . GLU A  1 299 ? 65.131  53.092  40.730  1.00 10.17  ? 299 GLU A CA  1 
ATOM   2410  C  C   . GLU A  1 299 ? 66.367  53.362  39.865  1.00 16.11  ? 299 GLU A C   1 
ATOM   2411  O  O   . GLU A  1 299 ? 66.289  54.110  38.912  1.00 23.64  ? 299 GLU A O   1 
ATOM   2412  C  CB  . GLU A  1 299 ? 65.044  54.128  41.858  1.00 9.44   ? 299 GLU A CB  1 
ATOM   2413  C  CG  . GLU A  1 299 ? 63.814  54.037  42.651  1.00 7.65   ? 299 GLU A CG  1 
ATOM   2414  C  CD  . GLU A  1 299 ? 63.578  55.193  43.621  1.00 18.54  ? 299 GLU A CD  1 
ATOM   2415  O  OE1 . GLU A  1 299 ? 64.362  56.215  43.600  1.00 18.68  ? 299 GLU A OE1 1 
ATOM   2416  O  OE2 . GLU A  1 299 ? 62.556  55.052  44.384  1.00 17.57  ? 299 GLU A OE2 1 
ATOM   2417  N  N   . GLY A  1 300 ? 67.509  52.760  40.204  1.00 13.42  ? 300 GLY A N   1 
ATOM   2418  C  CA  . GLY A  1 300 ? 68.701  53.009  39.431  1.00 11.84  ? 300 GLY A CA  1 
ATOM   2419  C  C   . GLY A  1 300 ? 68.700  52.298  38.105  1.00 15.28  ? 300 GLY A C   1 
ATOM   2420  O  O   . GLY A  1 300 ? 69.611  52.450  37.307  1.00 15.51  ? 300 GLY A O   1 
ATOM   2421  N  N   . GLU A  1 301 ? 67.687  51.493  37.853  1.00 15.93  ? 301 GLU A N   1 
ATOM   2422  C  CA  . GLU A  1 301 ? 67.656  50.792  36.586  1.00 18.58  ? 301 GLU A CA  1 
ATOM   2423  C  C   . GLU A  1 301 ? 67.859  51.686  35.324  1.00 21.70  ? 301 GLU A C   1 
ATOM   2424  O  O   . GLU A  1 301 ? 68.761  51.449  34.508  1.00 21.23  ? 301 GLU A O   1 
ATOM   2425  C  CB  . GLU A  1 301 ? 66.341  50.036  36.491  1.00 22.25  ? 301 GLU A CB  1 
ATOM   2426  C  CG  . GLU A  1 301 ? 66.257  48.854  37.409  1.00 25.08  ? 301 GLU A CG  1 
ATOM   2427  C  CD  . GLU A  1 301 ? 67.369  47.849  37.147  1.00 23.97  ? 301 GLU A CD  1 
ATOM   2428  O  OE1 . GLU A  1 301 ? 67.217  47.020  36.194  1.00 17.59  ? 301 GLU A OE1 1 
ATOM   2429  O  OE2 . GLU A  1 301 ? 68.382  47.897  37.899  1.00 16.13  ? 301 GLU A OE2 1 
ATOM   2430  N  N   . ALA A  1 302 ? 67.011  52.703  35.156  1.00 22.06  ? 302 ALA A N   1 
ATOM   2431  C  CA  . ALA A  1 302 ? 67.113  53.561  33.986  1.00 18.78  ? 302 ALA A CA  1 
ATOM   2432  C  C   . ALA A  1 302 ? 68.548  54.006  33.743  1.00 17.56  ? 302 ALA A C   1 
ATOM   2433  O  O   . ALA A  1 302 ? 69.145  53.648  32.712  1.00 17.14  ? 302 ALA A O   1 
ATOM   2434  C  CB  . ALA A  1 302 ? 66.188  54.734  34.113  1.00 21.29  ? 302 ALA A CB  1 
ATOM   2435  N  N   . MET A  1 303 ? 69.147  54.663  34.737  1.00 11.46  ? 303 MET A N   1 
ATOM   2436  C  CA  . MET A  1 303 ? 70.522  55.127  34.566  1.00 13.47  ? 303 MET A CA  1 
ATOM   2437  C  C   . MET A  1 303 ? 71.449  53.992  34.333  1.00 13.68  ? 303 MET A C   1 
ATOM   2438  O  O   . MET A  1 303 ? 72.397  54.128  33.580  1.00 19.21  ? 303 MET A O   1 
ATOM   2439  C  CB  . MET A  1 303 ? 71.057  55.955  35.739  1.00 16.38  ? 303 MET A CB  1 
ATOM   2440  C  CG  . MET A  1 303 ? 72.475  56.499  35.485  1.00 23.71  ? 303 MET A CG  1 
ATOM   2441  S  SD  . MET A  1 303 ? 72.844  58.070  36.292  1.00 20.32  ? 303 MET A SD  1 
ATOM   2442  C  CE  . MET A  1 303 ? 72.956  57.432  37.904  1.00 34.76  ? 303 MET A CE  1 
ATOM   2443  N  N   . ARG A  1 304 ? 71.163  52.858  34.946  1.00 16.31  ? 304 ARG A N   1 
ATOM   2444  C  CA  . ARG A  1 304 ? 72.019  51.685  34.797  1.00 18.72  ? 304 ARG A CA  1 
ATOM   2445  C  C   . ARG A  1 304 ? 72.058  51.242  33.396  1.00 16.87  ? 304 ARG A C   1 
ATOM   2446  O  O   . ARG A  1 304 ? 73.150  51.002  32.874  1.00 19.34  ? 304 ARG A O   1 
ATOM   2447  C  CB  . ARG A  1 304 ? 71.527  50.470  35.592  1.00 17.08  ? 304 ARG A CB  1 
ATOM   2448  C  CG  . ARG A  1 304 ? 72.645  49.517  35.813  1.00 11.19  ? 304 ARG A CG  1 
ATOM   2449  C  CD  . ARG A  1 304 ? 72.185  48.250  36.398  1.00 19.22  ? 304 ARG A CD  1 
ATOM   2450  N  NE  . ARG A  1 304 ? 71.917  47.352  35.306  1.00 26.03  ? 304 ARG A NE  1 
ATOM   2451  C  CZ  . ARG A  1 304 ? 70.734  46.806  35.098  1.00 25.48  ? 304 ARG A CZ  1 
ATOM   2452  N  NH1 . ARG A  1 304 ? 69.736  47.060  35.926  1.00 27.18  ? 304 ARG A NH1 1 
ATOM   2453  N  NH2 . ARG A  1 304 ? 70.504  46.125  33.992  1.00 24.45  ? 304 ARG A NH2 1 
ATOM   2454  N  N   . THR A  1 305 ? 70.867  51.180  32.784  1.00 16.94  ? 305 THR A N   1 
ATOM   2455  C  CA  . THR A  1 305 ? 70.768  50.724  31.406  1.00 15.70  ? 305 THR A CA  1 
ATOM   2456  C  C   . THR A  1 305 ? 71.472  51.680  30.471  1.00 19.63  ? 305 THR A C   1 
ATOM   2457  O  O   . THR A  1 305 ? 71.595  51.399  29.292  1.00 29.31  ? 305 THR A O   1 
ATOM   2458  C  CB  . THR A  1 305 ? 69.328  50.595  30.888  1.00 8.37   ? 305 THR A CB  1 
ATOM   2459  O  OG1 . THR A  1 305 ? 68.822  51.890  30.480  1.00 15.68  ? 305 THR A OG1 1 
ATOM   2460  C  CG2 . THR A  1 305 ? 68.439  49.942  31.916  1.00 2.00   ? 305 THR A CG2 1 
ATOM   2461  N  N   . LYS A  1 306 ? 71.846  52.844  30.978  1.00 20.71  ? 306 LYS A N   1 
ATOM   2462  C  CA  . LYS A  1 306 ? 72.496  53.799  30.145  1.00 17.01  ? 306 LYS A CA  1 
ATOM   2463  C  C   . LYS A  1 306 ? 73.977  53.975  30.410  1.00 20.47  ? 306 LYS A C   1 
ATOM   2464  O  O   . LYS A  1 306 ? 74.735  54.113  29.467  1.00 22.11  ? 306 LYS A O   1 
ATOM   2465  C  CB  . LYS A  1 306 ? 71.735  55.104  30.220  1.00 13.59  ? 306 LYS A CB  1 
ATOM   2466  C  CG  . LYS A  1 306 ? 71.406  55.643  28.856  1.00 17.58  ? 306 LYS A CG  1 
ATOM   2467  C  CD  . LYS A  1 306 ? 69.962  56.012  28.750  1.00 27.76  ? 306 LYS A CD  1 
ATOM   2468  C  CE  . LYS A  1 306 ? 69.548  56.085  27.277  1.00 24.76  ? 306 LYS A CE  1 
ATOM   2469  N  NZ  . LYS A  1 306 ? 69.350  54.784  26.534  1.00 35.79  ? 306 LYS A NZ  1 
ATOM   2470  N  N   . PHE A  1 307 ? 74.433  53.910  31.651  1.00 17.25  ? 307 PHE A N   1 
ATOM   2471  C  CA  . PHE A  1 307 ? 75.847  54.084  31.878  1.00 18.18  ? 307 PHE A CA  1 
ATOM   2472  C  C   . PHE A  1 307 ? 76.680  52.860  32.287  1.00 22.17  ? 307 PHE A C   1 
ATOM   2473  O  O   . PHE A  1 307 ? 77.903  52.899  32.160  1.00 25.30  ? 307 PHE A O   1 
ATOM   2474  C  CB  . PHE A  1 307 ? 76.027  55.219  32.845  1.00 11.73  ? 307 PHE A CB  1 
ATOM   2475  C  CG  . PHE A  1 307 ? 75.511  56.511  32.327  1.00 14.86  ? 307 PHE A CG  1 
ATOM   2476  C  CD1 . PHE A  1 307 ? 75.515  56.788  30.990  1.00 18.37  ? 307 PHE A CD1 1 
ATOM   2477  C  CD2 . PHE A  1 307 ? 75.050  57.478  33.170  1.00 19.98  ? 307 PHE A CD2 1 
ATOM   2478  C  CE1 . PHE A  1 307 ? 75.060  58.027  30.513  1.00 18.48  ? 307 PHE A CE1 1 
ATOM   2479  C  CE2 . PHE A  1 307 ? 74.603  58.710  32.690  1.00 17.10  ? 307 PHE A CE2 1 
ATOM   2480  C  CZ  . PHE A  1 307 ? 74.611  58.973  31.372  1.00 14.14  ? 307 PHE A CZ  1 
ATOM   2481  N  N   . GLU A  1 308 ? 76.040  51.762  32.701  1.00 20.60  ? 308 GLU A N   1 
ATOM   2482  C  CA  . GLU A  1 308 ? 76.803  50.608  33.149  1.00 22.60  ? 308 GLU A CA  1 
ATOM   2483  C  C   . GLU A  1 308 ? 77.927  50.167  32.242  1.00 22.21  ? 308 GLU A C   1 
ATOM   2484  O  O   . GLU A  1 308 ? 79.086  50.078  32.658  1.00 22.70  ? 308 GLU A O   1 
ATOM   2485  C  CB  . GLU A  1 308 ? 75.932  49.399  33.498  1.00 22.11  ? 308 GLU A CB  1 
ATOM   2486  C  CG  . GLU A  1 308 ? 76.829  48.318  34.117  1.00 31.74  ? 308 GLU A CG  1 
ATOM   2487  C  CD  . GLU A  1 308 ? 76.115  47.244  34.923  1.00 32.17  ? 308 GLU A CD  1 
ATOM   2488  O  OE1 . GLU A  1 308 ? 74.935  47.002  34.591  1.00 23.88  ? 308 GLU A OE1 1 
ATOM   2489  O  OE2 . GLU A  1 308 ? 76.774  46.651  35.845  1.00 30.27  ? 308 GLU A OE2 1 
ATOM   2490  N  N   . ALA A  1 309 ? 77.603  49.865  31.005  1.00 20.84  ? 309 ALA A N   1 
ATOM   2491  C  CA  . ALA A  1 309 ? 78.653  49.431  30.099  1.00 22.00  ? 309 ALA A CA  1 
ATOM   2492  C  C   . ALA A  1 309 ? 79.841  50.359  30.024  1.00 24.30  ? 309 ALA A C   1 
ATOM   2493  O  O   . ALA A  1 309 ? 80.967  49.893  29.967  1.00 30.29  ? 309 ALA A O   1 
ATOM   2494  C  CB  . ALA A  1 309 ? 78.124  49.223  28.764  1.00 17.67  ? 309 ALA A CB  1 
ATOM   2495  N  N   . TRP A  1 310 ? 79.604  51.662  30.030  1.00 22.92  ? 310 TRP A N   1 
ATOM   2496  C  CA  . TRP A  1 310 ? 80.694  52.620  29.964  1.00 22.00  ? 310 TRP A CA  1 
ATOM   2497  C  C   . TRP A  1 310 ? 81.589  52.430  31.169  1.00 22.27  ? 310 TRP A C   1 
ATOM   2498  O  O   . TRP A  1 310 ? 82.804  52.416  31.043  1.00 24.42  ? 310 TRP A O   1 
ATOM   2499  C  CB  . TRP A  1 310 ? 80.152  54.049  29.982  1.00 25.79  ? 310 TRP A CB  1 
ATOM   2500  C  CG  . TRP A  1 310 ? 79.385  54.384  28.779  1.00 32.55  ? 310 TRP A CG  1 
ATOM   2501  C  CD1 . TRP A  1 310 ? 79.095  53.548  27.756  1.00 34.99  ? 310 TRP A CD1 1 
ATOM   2502  C  CD2 . TRP A  1 310 ? 78.799  55.655  28.442  1.00 34.31  ? 310 TRP A CD2 1 
ATOM   2503  N  NE1 . TRP A  1 310 ? 78.372  54.208  26.786  1.00 40.05  ? 310 TRP A NE1 1 
ATOM   2504  C  CE2 . TRP A  1 310 ? 78.170  55.504  27.182  1.00 36.54  ? 310 TRP A CE2 1 
ATOM   2505  C  CE3 . TRP A  1 310 ? 78.737  56.899  29.078  1.00 32.05  ? 310 TRP A CE3 1 
ATOM   2506  C  CZ2 . TRP A  1 310 ? 77.485  56.544  26.550  1.00 34.14  ? 310 TRP A CZ2 1 
ATOM   2507  C  CZ3 . TRP A  1 310 ? 78.057  57.926  28.451  1.00 34.11  ? 310 TRP A CZ3 1 
ATOM   2508  C  CH2 . TRP A  1 310 ? 77.437  57.739  27.194  1.00 33.24  ? 310 TRP A CH2 1 
ATOM   2509  N  N   . PHE A  1 311 ? 80.988  52.304  32.340  1.00 20.53  ? 311 PHE A N   1 
ATOM   2510  C  CA  . PHE A  1 311 ? 81.760  52.132  33.552  1.00 22.40  ? 311 PHE A CA  1 
ATOM   2511  C  C   . PHE A  1 311 ? 82.651  50.904  33.448  1.00 28.96  ? 311 PHE A C   1 
ATOM   2512  O  O   . PHE A  1 311 ? 83.838  50.971  33.800  1.00 31.97  ? 311 PHE A O   1 
ATOM   2513  C  CB  . PHE A  1 311 ? 80.841  51.989  34.776  1.00 15.36  ? 311 PHE A CB  1 
ATOM   2514  C  CG  . PHE A  1 311 ? 80.002  53.212  35.068  1.00 12.04  ? 311 PHE A CG  1 
ATOM   2515  C  CD1 . PHE A  1 311 ? 80.241  54.414  34.381  1.00 7.69   ? 311 PHE A CD1 1 
ATOM   2516  C  CD2 . PHE A  1 311 ? 78.944  53.134  35.983  1.00 6.35   ? 311 PHE A CD2 1 
ATOM   2517  C  CE1 . PHE A  1 311 ? 79.465  55.497  34.603  1.00 5.74   ? 311 PHE A CE1 1 
ATOM   2518  C  CE2 . PHE A  1 311 ? 78.148  54.217  36.204  1.00 12.26  ? 311 PHE A CE2 1 
ATOM   2519  C  CZ  . PHE A  1 311 ? 78.403  55.417  35.509  1.00 12.82  ? 311 PHE A CZ  1 
ATOM   2520  N  N   . VAL A  1 312 ? 82.070  49.782  32.997  1.00 31.28  ? 312 VAL A N   1 
ATOM   2521  C  CA  . VAL A  1 312 ? 82.805  48.525  32.861  1.00 28.20  ? 312 VAL A CA  1 
ATOM   2522  C  C   . VAL A  1 312 ? 83.867  48.696  31.822  1.00 28.76  ? 312 VAL A C   1 
ATOM   2523  O  O   . VAL A  1 312 ? 85.030  48.387  32.034  1.00 35.37  ? 312 VAL A O   1 
ATOM   2524  C  CB  . VAL A  1 312 ? 81.925  47.390  32.440  1.00 25.48  ? 312 VAL A CB  1 
ATOM   2525  C  CG1 . VAL A  1 312 ? 82.753  46.211  32.276  1.00 17.70  ? 312 VAL A CG1 1 
ATOM   2526  C  CG2 . VAL A  1 312 ? 80.874  47.122  33.487  1.00 24.20  ? 312 VAL A CG2 1 
ATOM   2527  N  N   . LYS A  1 313 ? 83.472  49.241  30.697  1.00 27.01  ? 313 LYS A N   1 
ATOM   2528  C  CA  . LYS A  1 313 ? 84.413  49.474  29.628  1.00 25.10  ? 313 LYS A CA  1 
ATOM   2529  C  C   . LYS A  1 313 ? 85.637  50.267  30.070  1.00 25.98  ? 313 LYS A C   1 
ATOM   2530  O  O   . LYS A  1 313 ? 86.713  49.927  29.675  1.00 30.56  ? 313 LYS A O   1 
ATOM   2531  C  CB  . LYS A  1 313 ? 83.721  50.193  28.506  1.00 24.74  ? 313 LYS A CB  1 
ATOM   2532  C  CG  . LYS A  1 313 ? 84.622  50.706  27.442  1.00 32.89  ? 313 LYS A CG  1 
ATOM   2533  C  CD  . LYS A  1 313 ? 83.754  51.200  26.282  1.00 52.43  ? 313 LYS A CD  1 
ATOM   2534  C  CE  . LYS A  1 313 ? 84.569  51.936  25.209  1.00 62.61  ? 313 LYS A CE  1 
ATOM   2535  N  NZ  . LYS A  1 313 ? 85.711  51.081  24.719  1.00 70.18  ? 313 LYS A NZ  1 
ATOM   2536  N  N   . TYR A  1 314 ? 85.469  51.315  30.880  1.00 26.25  ? 314 TYR A N   1 
ATOM   2537  C  CA  . TYR A  1 314 ? 86.579  52.140  31.363  1.00 22.01  ? 314 TYR A CA  1 
ATOM   2538  C  C   . TYR A  1 314 ? 87.140  51.711  32.699  1.00 24.45  ? 314 TYR A C   1 
ATOM   2539  O  O   . TYR A  1 314 ? 87.941  52.408  33.324  1.00 23.26  ? 314 TYR A O   1 
ATOM   2540  C  CB  . TYR A  1 314 ? 86.145  53.564  31.444  1.00 15.22  ? 314 TYR A CB  1 
ATOM   2541  C  CG  . TYR A  1 314 ? 85.963  54.111  30.094  1.00 19.36  ? 314 TYR A CG  1 
ATOM   2542  C  CD1 . TYR A  1 314 ? 87.017  54.704  29.436  1.00 18.53  ? 314 TYR A CD1 1 
ATOM   2543  C  CD2 . TYR A  1 314 ? 84.753  54.043  29.452  1.00 21.00  ? 314 TYR A CD2 1 
ATOM   2544  C  CE1 . TYR A  1 314 ? 86.883  55.224  28.154  1.00 13.90  ? 314 TYR A CE1 1 
ATOM   2545  C  CE2 . TYR A  1 314 ? 84.606  54.574  28.152  1.00 24.57  ? 314 TYR A CE2 1 
ATOM   2546  C  CZ  . TYR A  1 314 ? 85.696  55.162  27.522  1.00 17.27  ? 314 TYR A CZ  1 
ATOM   2547  O  OH  . TYR A  1 314 ? 85.626  55.716  26.268  1.00 33.96  ? 314 TYR A OH  1 
ATOM   2548  N  N   . LYS A  1 315 ? 86.667  50.578  33.168  1.00 28.90  ? 315 LYS A N   1 
ATOM   2549  C  CA  . LYS A  1 315 ? 87.155  50.047  34.416  1.00 33.73  ? 315 LYS A CA  1 
ATOM   2550  C  C   . LYS A  1 315 ? 87.114  51.043  35.560  1.00 28.96  ? 315 LYS A C   1 
ATOM   2551  O  O   . LYS A  1 315 ? 88.074  51.187  36.272  1.00 27.25  ? 315 LYS A O   1 
ATOM   2552  C  CB  . LYS A  1 315 ? 88.581  49.545  34.193  1.00 42.82  ? 315 LYS A CB  1 
ATOM   2553  C  CG  . LYS A  1 315 ? 88.676  48.397  33.159  1.00 48.99  ? 315 LYS A CG  1 
ATOM   2554  C  CD  . LYS A  1 315 ? 89.927  48.509  32.275  1.00 57.28  ? 315 LYS A CD  1 
ATOM   2555  C  CE  . LYS A  1 315 ? 90.919  47.355  32.510  1.00 65.31  ? 315 LYS A CE  1 
ATOM   2556  N  NZ  . LYS A  1 315 ? 90.355  46.003  32.223  1.00 70.79  ? 315 LYS A NZ  1 
ATOM   2557  N  N   . VAL A  1 316 ? 85.995  51.707  35.787  1.00 27.43  ? 316 VAL A N   1 
ATOM   2558  C  CA  . VAL A  1 316 ? 85.978  52.622  36.921  1.00 28.54  ? 316 VAL A CA  1 
ATOM   2559  C  C   . VAL A  1 316 ? 86.106  51.761  38.196  1.00 27.60  ? 316 VAL A C   1 
ATOM   2560  O  O   . VAL A  1 316 ? 85.583  50.674  38.249  1.00 34.35  ? 316 VAL A O   1 
ATOM   2561  C  CB  . VAL A  1 316 ? 84.714  53.546  36.941  1.00 28.37  ? 316 VAL A CB  1 
ATOM   2562  C  CG1 . VAL A  1 316 ? 84.075  53.609  35.575  1.00 31.57  ? 316 VAL A CG1 1 
ATOM   2563  C  CG2 . VAL A  1 316 ? 83.728  53.103  37.971  1.00 24.11  ? 316 VAL A CG2 1 
ATOM   2564  N  N   . ASP A  1 317 ? 86.805  52.252  39.203  1.00 21.78  ? 317 ASP A N   1 
ATOM   2565  C  CA  . ASP A  1 317 ? 87.041  51.539  40.422  1.00 17.16  ? 317 ASP A CA  1 
ATOM   2566  C  C   . ASP A  1 317 ? 85.896  51.393  41.401  1.00 21.42  ? 317 ASP A C   1 
ATOM   2567  O  O   . ASP A  1 317 ? 85.646  50.301  41.878  1.00 25.31  ? 317 ASP A O   1 
ATOM   2568  C  CB  . ASP A  1 317 ? 88.184  52.200  41.140  1.00 17.99  ? 317 ASP A CB  1 
ATOM   2569  C  CG  . ASP A  1 317 ? 89.504  51.891  40.513  1.00 20.87  ? 317 ASP A CG  1 
ATOM   2570  O  OD1 . ASP A  1 317 ? 89.968  50.769  40.783  1.00 25.88  ? 317 ASP A OD1 1 
ATOM   2571  O  OD2 . ASP A  1 317 ? 90.043  52.736  39.763  1.00 14.35  ? 317 ASP A OD2 1 
ATOM   2572  N  N   . VAL A  1 318 ? 85.271  52.498  41.779  1.00 20.18  ? 318 VAL A N   1 
ATOM   2573  C  CA  . VAL A  1 318 ? 84.151  52.495  42.725  1.00 22.20  ? 318 VAL A CA  1 
ATOM   2574  C  C   . VAL A  1 318 ? 83.030  53.440  42.241  1.00 24.99  ? 318 VAL A C   1 
ATOM   2575  O  O   . VAL A  1 318 ? 83.308  54.408  41.535  1.00 28.49  ? 318 VAL A O   1 
ATOM   2576  C  CB  . VAL A  1 318 ? 84.518  53.125  44.059  1.00 26.47  ? 318 VAL A CB  1 
ATOM   2577  C  CG1 . VAL A  1 318 ? 83.939  52.347  45.175  1.00 26.41  ? 318 VAL A CG1 1 
ATOM   2578  C  CG2 . VAL A  1 318 ? 85.977  53.371  44.163  1.00 27.97  ? 318 VAL A CG2 1 
ATOM   2579  N  N   . VAL A  1 319 ? 81.799  53.238  42.707  1.00 21.56  ? 319 VAL A N   1 
ATOM   2580  C  CA  . VAL A  1 319 ? 80.698  54.130  42.348  1.00 21.52  ? 319 VAL A CA  1 
ATOM   2581  C  C   . VAL A  1 319 ? 79.956  54.322  43.632  1.00 21.95  ? 319 VAL A C   1 
ATOM   2582  O  O   . VAL A  1 319 ? 79.295  53.388  44.104  1.00 25.59  ? 319 VAL A O   1 
ATOM   2583  C  CB  . VAL A  1 319 ? 79.741  53.503  41.327  1.00 22.08  ? 319 VAL A CB  1 
ATOM   2584  C  CG1 . VAL A  1 319 ? 78.464  54.317  41.193  1.00 24.13  ? 319 VAL A CG1 1 
ATOM   2585  C  CG2 . VAL A  1 319 ? 80.406  53.402  39.995  1.00 23.05  ? 319 VAL A CG2 1 
ATOM   2586  N  N   . PHE A  1 320 ? 80.101  55.496  44.234  1.00 18.60  ? 320 PHE A N   1 
ATOM   2587  C  CA  . PHE A  1 320 ? 79.445  55.759  45.505  1.00 16.25  ? 320 PHE A CA  1 
ATOM   2588  C  C   . PHE A  1 320 ? 78.083  56.376  45.281  1.00 16.49  ? 320 PHE A C   1 
ATOM   2589  O  O   . PHE A  1 320 ? 77.909  57.164  44.383  1.00 19.07  ? 320 PHE A O   1 
ATOM   2590  C  CB  . PHE A  1 320 ? 80.297  56.686  46.352  1.00 14.92  ? 320 PHE A CB  1 
ATOM   2591  C  CG  . PHE A  1 320 ? 81.647  56.111  46.724  1.00 16.43  ? 320 PHE A CG  1 
ATOM   2592  C  CD1 . PHE A  1 320 ? 81.766  55.142  47.708  1.00 14.18  ? 320 PHE A CD1 1 
ATOM   2593  C  CD2 . PHE A  1 320 ? 82.798  56.554  46.093  1.00 17.95  ? 320 PHE A CD2 1 
ATOM   2594  C  CE1 . PHE A  1 320 ? 83.003  54.621  48.057  1.00 19.36  ? 320 PHE A CE1 1 
ATOM   2595  C  CE2 . PHE A  1 320 ? 84.032  56.028  46.438  1.00 23.85  ? 320 PHE A CE2 1 
ATOM   2596  C  CZ  . PHE A  1 320 ? 84.140  55.056  47.428  1.00 18.69  ? 320 PHE A CZ  1 
ATOM   2597  N  N   . ALA A  1 321 ? 77.099  55.969  46.057  1.00 13.45  ? 321 ALA A N   1 
ATOM   2598  C  CA  . ALA A  1 321 ? 75.769  56.517  45.908  1.00 12.70  ? 321 ALA A CA  1 
ATOM   2599  C  C   . ALA A  1 321 ? 75.156  56.656  47.297  1.00 15.72  ? 321 ALA A C   1 
ATOM   2600  O  O   . ALA A  1 321 ? 75.723  56.151  48.282  1.00 19.13  ? 321 ALA A O   1 
ATOM   2601  C  CB  . ALA A  1 321 ? 74.957  55.582  45.090  1.00 9.17   ? 321 ALA A CB  1 
ATOM   2602  N  N   . GLY A  1 322 ? 74.008  57.321  47.387  1.00 13.04  ? 322 GLY A N   1 
ATOM   2603  C  CA  . GLY A  1 322 ? 73.340  57.489  48.663  1.00 15.21  ? 322 GLY A CA  1 
ATOM   2604  C  C   . GLY A  1 322 ? 71.930  57.010  48.400  1.00 18.81  ? 322 GLY A C   1 
ATOM   2605  O  O   . GLY A  1 322 ? 71.730  55.923  47.849  1.00 17.11  ? 322 GLY A O   1 
ATOM   2606  N  N   . HIS A  1 323 ? 70.955  57.794  48.833  1.00 15.35  ? 323 HIS A N   1 
ATOM   2607  C  CA  . HIS A  1 323 ? 69.564  57.516  48.608  1.00 16.47  ? 323 HIS A CA  1 
ATOM   2608  C  C   . HIS A  1 323 ? 68.933  56.426  49.457  1.00 16.31  ? 323 HIS A C   1 
ATOM   2609  O  O   . HIS A  1 323 ? 67.786  56.540  49.868  1.00 23.68  ? 323 HIS A O   1 
ATOM   2610  C  CB  . HIS A  1 323 ? 69.323  57.339  47.105  1.00 17.62  ? 323 HIS A CB  1 
ATOM   2611  C  CG  . HIS A  1 323 ? 67.927  57.644  46.653  1.00 21.12  ? 323 HIS A CG  1 
ATOM   2612  N  ND1 . HIS A  1 323 ? 67.247  58.810  46.973  1.00 21.14  ? 323 HIS A ND1 1 
ATOM   2613  C  CD2 . HIS A  1 323 ? 67.080  56.914  45.877  1.00 17.75  ? 323 HIS A CD2 1 
ATOM   2614  C  CE1 . HIS A  1 323 ? 66.052  58.772  46.420  1.00 24.04  ? 323 HIS A CE1 1 
ATOM   2615  N  NE2 . HIS A  1 323 ? 65.924  57.638  45.752  1.00 23.53  ? 323 HIS A NE2 1 
ATOM   2616  N  N   . VAL A  1 324 ? 69.602  55.309  49.676  1.00 20.11  ? 324 VAL A N   1 
ATOM   2617  C  CA  . VAL A  1 324 ? 69.021  54.309  50.550  1.00 16.54  ? 324 VAL A CA  1 
ATOM   2618  C  C   . VAL A  1 324 ? 69.713  54.577  51.882  1.00 22.79  ? 324 VAL A C   1 
ATOM   2619  O  O   . VAL A  1 324 ? 70.954  54.624  51.937  1.00 24.00  ? 324 VAL A O   1 
ATOM   2620  C  CB  . VAL A  1 324 ? 69.323  52.940  50.049  1.00 8.76   ? 324 VAL A CB  1 
ATOM   2621  C  CG1 . VAL A  1 324 ? 68.793  51.963  50.983  1.00 11.05  ? 324 VAL A CG1 1 
ATOM   2622  C  CG2 . VAL A  1 324 ? 68.639  52.762  48.729  1.00 13.66  ? 324 VAL A CG2 1 
ATOM   2623  N  N   . HIS A  1 325 ? 68.934  54.895  52.914  1.00 23.90  ? 325 HIS A N   1 
ATOM   2624  C  CA  . HIS A  1 325 ? 69.478  55.213  54.235  1.00 23.19  ? 325 HIS A CA  1 
ATOM   2625  C  C   . HIS A  1 325 ? 69.960  53.965  54.955  1.00 24.23  ? 325 HIS A C   1 
ATOM   2626  O  O   . HIS A  1 325 ? 69.330  53.498  55.898  1.00 27.51  ? 325 HIS A O   1 
ATOM   2627  C  CB  . HIS A  1 325 ? 68.442  55.979  55.068  1.00 21.01  ? 325 HIS A CB  1 
ATOM   2628  C  CG  . HIS A  1 325 ? 67.869  57.186  54.374  1.00 20.16  ? 325 HIS A CG  1 
ATOM   2629  N  ND1 . HIS A  1 325 ? 66.593  57.646  54.608  1.00 23.78  ? 325 HIS A ND1 1 
ATOM   2630  C  CD2 . HIS A  1 325 ? 68.382  57.989  53.409  1.00 24.84  ? 325 HIS A CD2 1 
ATOM   2631  C  CE1 . HIS A  1 325 ? 66.345  58.670  53.803  1.00 28.91  ? 325 HIS A CE1 1 
ATOM   2632  N  NE2 . HIS A  1 325 ? 67.413  58.901  53.065  1.00 20.12  ? 325 HIS A NE2 1 
ATOM   2633  N  N   . ALA A  1 326 ? 71.068  53.421  54.458  1.00 20.43  ? 326 ALA A N   1 
ATOM   2634  C  CA  . ALA A  1 326 ? 71.694  52.222  54.994  1.00 21.54  ? 326 ALA A CA  1 
ATOM   2635  C  C   . ALA A  1 326 ? 73.025  52.031  54.259  1.00 23.42  ? 326 ALA A C   1 
ATOM   2636  O  O   . ALA A  1 326 ? 73.399  52.865  53.439  1.00 28.12  ? 326 ALA A O   1 
ATOM   2637  C  CB  . ALA A  1 326 ? 70.802  51.038  54.774  1.00 23.74  ? 326 ALA A CB  1 
ATOM   2638  N  N   . TYR A  1 327 ? 73.738  50.948  54.534  1.00 22.21  ? 327 TYR A N   1 
ATOM   2639  C  CA  . TYR A  1 327 ? 75.023  50.708  53.891  1.00 19.03  ? 327 TYR A CA  1 
ATOM   2640  C  C   . TYR A  1 327 ? 74.927  49.414  53.130  1.00 21.07  ? 327 TYR A C   1 
ATOM   2641  O  O   . TYR A  1 327 ? 74.211  48.500  53.530  1.00 21.40  ? 327 TYR A O   1 
ATOM   2642  C  CB  . TYR A  1 327 ? 76.096  50.569  54.962  1.00 16.17  ? 327 TYR A CB  1 
ATOM   2643  C  CG  . TYR A  1 327 ? 77.465  50.104  54.459  1.00 14.76  ? 327 TYR A CG  1 
ATOM   2644  C  CD1 . TYR A  1 327 ? 78.231  50.896  53.651  1.00 18.85  ? 327 TYR A CD1 1 
ATOM   2645  C  CD2 . TYR A  1 327 ? 78.006  48.905  54.866  1.00 20.62  ? 327 TYR A CD2 1 
ATOM   2646  C  CE1 . TYR A  1 327 ? 79.526  50.511  53.256  1.00 15.40  ? 327 TYR A CE1 1 
ATOM   2647  C  CE2 . TYR A  1 327 ? 79.271  48.519  54.484  1.00 18.24  ? 327 TYR A CE2 1 
ATOM   2648  C  CZ  . TYR A  1 327 ? 80.021  49.321  53.679  1.00 21.88  ? 327 TYR A CZ  1 
ATOM   2649  O  OH  . TYR A  1 327 ? 81.270  48.885  53.278  1.00 29.22  ? 327 TYR A OH  1 
ATOM   2650  N  N   . GLU A  1 328 ? 75.654  49.336  52.030  1.00 21.08  ? 328 GLU A N   1 
ATOM   2651  C  CA  . GLU A  1 328 ? 75.709  48.125  51.207  1.00 21.00  ? 328 GLU A CA  1 
ATOM   2652  C  C   . GLU A  1 328 ? 76.952  48.188  50.327  1.00 22.18  ? 328 GLU A C   1 
ATOM   2653  O  O   . GLU A  1 328 ? 77.366  49.260  49.942  1.00 27.16  ? 328 GLU A O   1 
ATOM   2654  C  CB  . GLU A  1 328 ? 74.453  47.971  50.372  1.00 17.82  ? 328 GLU A CB  1 
ATOM   2655  C  CG  . GLU A  1 328 ? 74.598  46.975  49.233  1.00 23.17  ? 328 GLU A CG  1 
ATOM   2656  C  CD  . GLU A  1 328 ? 73.269  46.315  48.817  1.00 23.20  ? 328 GLU A CD  1 
ATOM   2657  O  OE1 . GLU A  1 328 ? 72.206  46.970  48.931  1.00 15.75  ? 328 GLU A OE1 1 
ATOM   2658  O  OE2 . GLU A  1 328 ? 73.291  45.149  48.340  1.00 22.34  ? 328 GLU A OE2 1 
ATOM   2659  N  N   . ARG A  1 329 ? 77.582  47.054  50.071  1.00 25.91  ? 329 ARG A N   1 
ATOM   2660  C  CA  . ARG A  1 329 ? 78.795  46.999  49.267  1.00 25.83  ? 329 ARG A CA  1 
ATOM   2661  C  C   . ARG A  1 329 ? 78.609  45.856  48.315  1.00 26.55  ? 329 ARG A C   1 
ATOM   2662  O  O   . ARG A  1 329 ? 78.012  44.879  48.667  1.00 30.29  ? 329 ARG A O   1 
ATOM   2663  C  CB  . ARG A  1 329 ? 80.013  46.709  50.134  1.00 27.11  ? 329 ARG A CB  1 
ATOM   2664  C  CG  . ARG A  1 329 ? 81.319  46.902  49.396  1.00 32.87  ? 329 ARG A CG  1 
ATOM   2665  C  CD  . ARG A  1 329 ? 82.500  46.635  50.317  1.00 35.01  ? 329 ARG A CD  1 
ATOM   2666  N  NE  . ARG A  1 329 ? 82.802  45.213  50.395  1.00 33.58  ? 329 ARG A NE  1 
ATOM   2667  C  CZ  . ARG A  1 329 ? 82.706  44.506  51.504  1.00 37.89  ? 329 ARG A CZ  1 
ATOM   2668  N  NH1 . ARG A  1 329 ? 82.324  45.067  52.641  1.00 41.86  ? 329 ARG A NH1 1 
ATOM   2669  N  NH2 . ARG A  1 329 ? 82.959  43.223  51.457  1.00 44.34  ? 329 ARG A NH2 1 
ATOM   2670  N  N   . SER A  1 330 ? 79.116  45.958  47.112  1.00 32.02  ? 330 SER A N   1 
ATOM   2671  C  CA  . SER A  1 330 ? 78.927  44.888  46.176  1.00 37.34  ? 330 SER A CA  1 
ATOM   2672  C  C   . SER A  1 330 ? 80.134  44.175  45.724  1.00 41.04  ? 330 SER A C   1 
ATOM   2673  O  O   . SER A  1 330 ? 81.250  44.399  46.250  1.00 45.37  ? 330 SER A O   1 
ATOM   2674  C  CB  . SER A  1 330 ? 78.176  45.392  44.979  1.00 37.80  ? 330 SER A CB  1 
ATOM   2675  O  OG  . SER A  1 330 ? 76.840  45.524  45.445  1.00 59.83  ? 330 SER A OG  1 
ATOM   2676  N  N   . GLU A  1 331 ? 79.868  43.230  44.821  1.00 38.11  ? 331 GLU A N   1 
ATOM   2677  C  CA  . GLU A  1 331 ? 80.891  42.422  44.214  1.00 35.87  ? 331 GLU A CA  1 
ATOM   2678  C  C   . GLU A  1 331 ? 81.145  43.096  42.917  1.00 30.69  ? 331 GLU A C   1 
ATOM   2679  O  O   . GLU A  1 331 ? 80.271  43.815  42.453  1.00 37.82  ? 331 GLU A O   1 
ATOM   2680  C  CB  . GLU A  1 331 ? 80.353  41.018  43.954  1.00 45.34  ? 331 GLU A CB  1 
ATOM   2681  C  CG  . GLU A  1 331 ? 80.155  40.133  45.200  1.00 62.25  ? 331 GLU A CG  1 
ATOM   2682  C  CD  . GLU A  1 331 ? 81.466  39.800  45.991  1.00 74.11  ? 331 GLU A CD  1 
ATOM   2683  O  OE1 . GLU A  1 331 ? 82.560  40.369  45.682  1.00 78.92  ? 331 GLU A OE1 1 
ATOM   2684  O  OE2 . GLU A  1 331 ? 81.384  38.962  46.938  1.00 77.29  ? 331 GLU A OE2 1 
ATOM   2685  N  N   . ARG A  1 332 ? 82.358  42.983  42.379  1.00 26.99  ? 332 ARG A N   1 
ATOM   2686  C  CA  . ARG A  1 332 ? 82.616  43.577  41.076  1.00 21.65  ? 332 ARG A CA  1 
ATOM   2687  C  C   . ARG A  1 332 ? 81.720  42.738  40.221  1.00 27.04  ? 332 ARG A C   1 
ATOM   2688  O  O   . ARG A  1 332 ? 81.902  41.530  40.085  1.00 26.48  ? 332 ARG A O   1 
ATOM   2689  C  CB  . ARG A  1 332 ? 84.051  43.491  40.677  1.00 19.45  ? 332 ARG A CB  1 
ATOM   2690  C  CG  . ARG A  1 332 ? 84.876  44.361  41.583  1.00 21.51  ? 332 ARG A CG  1 
ATOM   2691  C  CD  . ARG A  1 332 ? 86.290  44.466  41.092  1.00 33.90  ? 332 ARG A CD  1 
ATOM   2692  N  NE  . ARG A  1 332 ? 87.074  45.392  41.898  1.00 33.37  ? 332 ARG A NE  1 
ATOM   2693  C  CZ  . ARG A  1 332 ? 87.069  46.699  41.729  1.00 34.09  ? 332 ARG A CZ  1 
ATOM   2694  N  NH1 . ARG A  1 332 ? 86.310  47.245  40.787  1.00 39.56  ? 332 ARG A NH1 1 
ATOM   2695  N  NH2 . ARG A  1 332 ? 87.888  47.452  42.430  1.00 33.64  ? 332 ARG A NH2 1 
ATOM   2696  N  N   . VAL A  1 333 ? 80.652  43.394  39.777  1.00 34.86  ? 333 VAL A N   1 
ATOM   2697  C  CA  . VAL A  1 333 ? 79.588  42.783  39.029  1.00 34.51  ? 333 VAL A CA  1 
ATOM   2698  C  C   . VAL A  1 333 ? 79.127  43.638  37.854  1.00 32.55  ? 333 VAL A C   1 
ATOM   2699  O  O   . VAL A  1 333 ? 79.114  44.858  37.914  1.00 28.83  ? 333 VAL A O   1 
ATOM   2700  C  CB  . VAL A  1 333 ? 78.431  42.541  40.017  1.00 33.02  ? 333 VAL A CB  1 
ATOM   2701  C  CG1 . VAL A  1 333 ? 77.178  42.277  39.310  1.00 41.70  ? 333 VAL A CG1 1 
ATOM   2702  C  CG2 . VAL A  1 333 ? 78.743  41.372  40.887  1.00 30.57  ? 333 VAL A CG2 1 
ATOM   2703  N  N   . SER A  1 334 ? 78.731  42.969  36.786  1.00 34.47  ? 334 SER A N   1 
ATOM   2704  C  CA  . SER A  1 334 ? 78.239  43.617  35.603  1.00 37.65  ? 334 SER A CA  1 
ATOM   2705  C  C   . SER A  1 334 ? 76.923  42.882  35.248  1.00 38.04  ? 334 SER A C   1 
ATOM   2706  O  O   . SER A  1 334 ? 76.655  41.788  35.759  1.00 40.31  ? 334 SER A O   1 
ATOM   2707  C  CB  . SER A  1 334 ? 79.260  43.451  34.476  1.00 35.80  ? 334 SER A CB  1 
ATOM   2708  O  OG  . SER A  1 334 ? 78.868  42.407  33.585  1.00 46.95  ? 334 SER A OG  1 
ATOM   2709  N  N   . ASN A  1 335 ? 76.083  43.499  34.422  1.00 35.52  ? 335 ASN A N   1 
ATOM   2710  C  CA  . ASN A  1 335 ? 74.840  42.879  33.972  1.00 31.46  ? 335 ASN A CA  1 
ATOM   2711  C  C   . ASN A  1 335 ? 74.597  43.519  32.639  1.00 30.36  ? 335 ASN A C   1 
ATOM   2712  O  O   . ASN A  1 335 ? 73.540  44.031  32.353  1.00 30.39  ? 335 ASN A O   1 
ATOM   2713  C  CB  . ASN A  1 335 ? 73.685  43.176  34.923  1.00 29.27  ? 335 ASN A CB  1 
ATOM   2714  C  CG  . ASN A  1 335 ? 72.373  42.550  34.460  1.00 28.72  ? 335 ASN A CG  1 
ATOM   2715  O  OD1 . ASN A  1 335 ? 72.311  41.888  33.392  1.00 37.68  ? 335 ASN A OD1 1 
ATOM   2716  N  ND2 . ASN A  1 335 ? 71.316  42.735  35.261  1.00 28.81  ? 335 ASN A ND2 1 
ATOM   2717  N  N   . ILE A  1 336 ? 75.572  43.399  31.771  1.00 31.59  ? 336 ILE A N   1 
ATOM   2718  C  CA  . ILE A  1 336 ? 75.447  44.089  30.526  1.00 33.28  ? 336 ILE A CA  1 
ATOM   2719  C  C   . ILE A  1 336 ? 75.255  43.241  29.284  1.00 38.43  ? 336 ILE A C   1 
ATOM   2720  O  O   . ILE A  1 336 ? 75.660  43.676  28.196  1.00 43.43  ? 336 ILE A O   1 
ATOM   2721  C  CB  . ILE A  1 336 ? 76.667  44.998  30.356  1.00 30.01  ? 336 ILE A CB  1 
ATOM   2722  C  CG1 . ILE A  1 336 ? 77.940  44.161  30.398  1.00 26.18  ? 336 ILE A CG1 1 
ATOM   2723  C  CG2 . ILE A  1 336 ? 76.738  45.990  31.503  1.00 34.60  ? 336 ILE A CG2 1 
ATOM   2724  C  CD1 . ILE A  1 336 ? 79.204  44.973  30.356  1.00 21.05  ? 336 ILE A CD1 1 
ATOM   2725  N  N   . ALA A  1 337 ? 74.587  42.087  29.394  1.00 40.21  ? 337 ALA A N   1 
ATOM   2726  C  CA  . ALA A  1 337 ? 74.430  41.231  28.211  1.00 33.46  ? 337 ALA A CA  1 
ATOM   2727  C  C   . ALA A  1 337 ? 73.047  41.080  27.663  1.00 33.13  ? 337 ALA A C   1 
ATOM   2728  O  O   . ALA A  1 337 ? 72.838  40.417  26.641  1.00 31.06  ? 337 ALA A O   1 
ATOM   2729  C  CB  . ALA A  1 337 ? 74.967  39.905  28.493  1.00 36.75  ? 337 ALA A CB  1 
ATOM   2730  N  N   . TYR A  1 338 ? 72.095  41.650  28.379  1.00 33.47  ? 338 TYR A N   1 
ATOM   2731  C  CA  . TYR A  1 338 ? 70.707  41.568  28.008  1.00 31.86  ? 338 TYR A CA  1 
ATOM   2732  C  C   . TYR A  1 338 ? 70.391  42.144  26.655  1.00 27.31  ? 338 TYR A C   1 
ATOM   2733  O  O   . TYR A  1 338 ? 70.902  43.174  26.265  1.00 33.96  ? 338 TYR A O   1 
ATOM   2734  C  CB  . TYR A  1 338 ? 69.884  42.243  29.056  1.00 31.89  ? 338 TYR A CB  1 
ATOM   2735  C  CG  . TYR A  1 338 ? 68.423  42.047  28.893  1.00 32.44  ? 338 TYR A CG  1 
ATOM   2736  C  CD1 . TYR A  1 338 ? 67.842  40.777  29.003  1.00 30.57  ? 338 TYR A CD1 1 
ATOM   2737  C  CD2 . TYR A  1 338 ? 67.594  43.144  28.706  1.00 26.95  ? 338 TYR A CD2 1 
ATOM   2738  C  CE1 . TYR A  1 338 ? 66.449  40.642  28.930  1.00 33.88  ? 338 TYR A CE1 1 
ATOM   2739  C  CE2 . TYR A  1 338 ? 66.224  43.005  28.639  1.00 29.50  ? 338 TYR A CE2 1 
ATOM   2740  C  CZ  . TYR A  1 338 ? 65.657  41.776  28.746  1.00 28.69  ? 338 TYR A CZ  1 
ATOM   2741  O  OH  . TYR A  1 338 ? 64.301  41.729  28.631  1.00 34.91  ? 338 TYR A OH  1 
ATOM   2742  N  N   . LYS A  1 339 ? 69.545  41.437  25.935  1.00 27.49  ? 339 LYS A N   1 
ATOM   2743  C  CA  . LYS A  1 339 ? 69.108  41.831  24.609  1.00 26.90  ? 339 LYS A CA  1 
ATOM   2744  C  C   . LYS A  1 339 ? 67.613  41.568  24.475  1.00 24.77  ? 339 LYS A C   1 
ATOM   2745  O  O   . LYS A  1 339 ? 67.140  41.173  23.423  1.00 21.73  ? 339 LYS A O   1 
ATOM   2746  C  CB  . LYS A  1 339 ? 69.841  41.032  23.561  1.00 30.21  ? 339 LYS A CB  1 
ATOM   2747  C  CG  . LYS A  1 339 ? 71.303  41.063  23.713  1.00 35.15  ? 339 LYS A CG  1 
ATOM   2748  C  CD  . LYS A  1 339 ? 71.805  42.440  23.439  1.00 47.65  ? 339 LYS A CD  1 
ATOM   2749  C  CE  . LYS A  1 339 ? 73.311  42.452  23.463  1.00 56.23  ? 339 LYS A CE  1 
ATOM   2750  N  NZ  . LYS A  1 339 ? 73.833  41.374  22.544  1.00 62.09  ? 339 LYS A NZ  1 
ATOM   2751  N  N   . ILE A  1 340 ? 66.894  41.710  25.585  1.00 26.47  ? 340 ILE A N   1 
ATOM   2752  C  CA  . ILE A  1 340 ? 65.452  41.540  25.649  1.00 25.40  ? 340 ILE A CA  1 
ATOM   2753  C  C   . ILE A  1 340 ? 65.025  40.104  25.618  1.00 26.10  ? 340 ILE A C   1 
ATOM   2754  O  O   . ILE A  1 340 ? 64.486  39.572  26.581  1.00 30.21  ? 340 ILE A O   1 
ATOM   2755  C  CB  . ILE A  1 340 ? 64.755  42.222  24.486  1.00 29.65  ? 340 ILE A CB  1 
ATOM   2756  C  CG1 . ILE A  1 340 ? 65.339  43.613  24.246  1.00 26.31  ? 340 ILE A CG1 1 
ATOM   2757  C  CG2 . ILE A  1 340 ? 63.282  42.277  24.770  1.00 27.97  ? 340 ILE A CG2 1 
ATOM   2758  C  CD1 . ILE A  1 340 ? 65.210  44.473  25.435  1.00 22.71  ? 340 ILE A CD1 1 
ATOM   2759  N  N   . THR A  1 341 ? 65.236  39.474  24.481  1.00 24.78  ? 341 THR A N   1 
ATOM   2760  C  CA  . THR A  1 341 ? 64.839  38.093  24.312  1.00 30.44  ? 341 THR A CA  1 
ATOM   2761  C  C   . THR A  1 341 ? 65.846  37.020  24.655  1.00 32.85  ? 341 THR A C   1 
ATOM   2762  O  O   . THR A  1 341 ? 65.464  35.903  24.847  1.00 39.24  ? 341 THR A O   1 
ATOM   2763  C  CB  . THR A  1 341 ? 64.403  37.862  22.902  1.00 29.10  ? 341 THR A CB  1 
ATOM   2764  O  OG1 . THR A  1 341 ? 65.469  38.223  22.006  1.00 38.29  ? 341 THR A OG1 1 
ATOM   2765  C  CG2 . THR A  1 341 ? 63.189  38.700  22.619  1.00 25.99  ? 341 THR A CG2 1 
ATOM   2766  N  N   . ASP A  1 342 ? 67.122  37.345  24.758  1.00 33.43  ? 342 ASP A N   1 
ATOM   2767  C  CA  . ASP A  1 342 ? 68.104  36.332  25.062  1.00 28.35  ? 342 ASP A CA  1 
ATOM   2768  C  C   . ASP A  1 342 ? 68.168  35.864  26.493  1.00 29.23  ? 342 ASP A C   1 
ATOM   2769  O  O   . ASP A  1 342 ? 69.045  35.097  26.834  1.00 34.93  ? 342 ASP A O   1 
ATOM   2770  C  CB  . ASP A  1 342 ? 69.491  36.740  24.563  1.00 26.75  ? 342 ASP A CB  1 
ATOM   2771  C  CG  . ASP A  1 342 ? 70.134  37.765  25.422  1.00 29.05  ? 342 ASP A CG  1 
ATOM   2772  O  OD1 . ASP A  1 342 ? 69.439  38.335  26.281  1.00 29.88  ? 342 ASP A OD1 1 
ATOM   2773  O  OD2 . ASP A  1 342 ? 71.345  37.988  25.256  1.00 37.98  ? 342 ASP A OD2 1 
ATOM   2774  N  N   . GLY A  1 343 ? 67.282  36.327  27.361  1.00 30.81  ? 343 GLY A N   1 
ATOM   2775  C  CA  . GLY A  1 343 ? 67.354  35.847  28.743  1.00 31.93  ? 343 GLY A CA  1 
ATOM   2776  C  C   . GLY A  1 343 ? 68.628  36.091  29.601  1.00 36.34  ? 343 GLY A C   1 
ATOM   2777  O  O   . GLY A  1 343 ? 68.682  35.653  30.748  1.00 43.35  ? 343 GLY A O   1 
ATOM   2778  N  N   . LEU A  1 344 ? 69.638  36.804  29.107  1.00 33.65  ? 344 LEU A N   1 
ATOM   2779  C  CA  . LEU A  1 344 ? 70.848  37.066  29.893  1.00 27.35  ? 344 LEU A CA  1 
ATOM   2780  C  C   . LEU A  1 344 ? 70.690  38.329  30.793  1.00 30.00  ? 344 LEU A C   1 
ATOM   2781  O  O   . LEU A  1 344 ? 71.358  39.403  30.616  1.00 26.17  ? 344 LEU A O   1 
ATOM   2782  C  CB  . LEU A  1 344 ? 72.022  37.255  28.926  1.00 29.07  ? 344 LEU A CB  1 
ATOM   2783  C  CG  . LEU A  1 344 ? 72.404  36.039  28.105  1.00 21.64  ? 344 LEU A CG  1 
ATOM   2784  C  CD1 . LEU A  1 344 ? 73.524  36.378  27.151  1.00 22.31  ? 344 LEU A CD1 1 
ATOM   2785  C  CD2 . LEU A  1 344 ? 72.836  35.012  29.046  1.00 21.46  ? 344 LEU A CD2 1 
ATOM   2786  N  N   . CYS A  1 345 ? 69.841  38.201  31.795  1.00 25.54  ? 345 CYS A N   1 
ATOM   2787  C  CA  . CYS A  1 345 ? 69.618  39.337  32.646  1.00 27.27  ? 345 CYS A CA  1 
ATOM   2788  C  C   . CYS A  1 345 ? 69.933  39.052  34.098  1.00 30.53  ? 345 CYS A C   1 
ATOM   2789  O  O   . CYS A  1 345 ? 69.104  39.279  34.972  1.00 27.32  ? 345 CYS A O   1 
ATOM   2790  C  CB  . CYS A  1 345 ? 68.173  39.738  32.518  1.00 27.20  ? 345 CYS A CB  1 
ATOM   2791  S  SG  . CYS A  1 345 ? 67.137  38.367  32.950  1.00 19.75  ? 345 CYS A SG  1 
ATOM   2792  N  N   . THR A  1 346 ? 71.116  38.512  34.365  1.00 35.92  ? 346 THR A N   1 
ATOM   2793  C  CA  . THR A  1 346 ? 71.495  38.216  35.739  1.00 36.74  ? 346 THR A CA  1 
ATOM   2794  C  C   . THR A  1 346 ? 72.939  38.642  35.989  1.00 35.36  ? 346 THR A C   1 
ATOM   2795  O  O   . THR A  1 346 ? 73.860  38.318  35.227  1.00 39.62  ? 346 THR A O   1 
ATOM   2796  C  CB  . THR A  1 346 ? 71.280  36.735  36.082  1.00 41.64  ? 346 THR A CB  1 
ATOM   2797  O  OG1 . THR A  1 346 ? 69.895  36.384  35.869  1.00 44.95  ? 346 THR A OG1 1 
ATOM   2798  C  CG2 . THR A  1 346 ? 71.675  36.492  37.547  1.00 40.39  ? 346 THR A CG2 1 
ATOM   2799  N  N   . PRO A  1 347 ? 73.125  39.480  37.006  1.00 30.66  ? 347 PRO A N   1 
ATOM   2800  C  CA  . PRO A  1 347 ? 74.436  40.005  37.378  1.00 26.22  ? 347 PRO A CA  1 
ATOM   2801  C  C   . PRO A  1 347 ? 75.421  38.872  37.550  1.00 29.50  ? 347 PRO A C   1 
ATOM   2802  O  O   . PRO A  1 347 ? 75.223  37.960  38.354  1.00 34.96  ? 347 PRO A O   1 
ATOM   2803  C  CB  . PRO A  1 347 ? 74.155  40.700  38.690  1.00 23.28  ? 347 PRO A CB  1 
ATOM   2804  C  CG  . PRO A  1 347 ? 72.702  41.058  38.589  1.00 27.70  ? 347 PRO A CG  1 
ATOM   2805  C  CD  . PRO A  1 347 ? 72.063  39.912  37.935  1.00 27.27  ? 347 PRO A CD  1 
ATOM   2806  N  N   . VAL A  1 348 ? 76.505  38.960  36.813  1.00 27.89  ? 348 VAL A N   1 
ATOM   2807  C  CA  . VAL A  1 348 ? 77.568  37.980  36.864  1.00 30.71  ? 348 VAL A CA  1 
ATOM   2808  C  C   . VAL A  1 348 ? 78.846  38.645  37.370  1.00 31.88  ? 348 VAL A C   1 
ATOM   2809  O  O   . VAL A  1 348 ? 79.037  39.823  37.170  1.00 38.71  ? 348 VAL A O   1 
ATOM   2810  C  CB  . VAL A  1 348 ? 77.831  37.435  35.478  1.00 34.20  ? 348 VAL A CB  1 
ATOM   2811  C  CG1 . VAL A  1 348 ? 76.603  36.739  34.982  1.00 44.32  ? 348 VAL A CG1 1 
ATOM   2812  C  CG2 . VAL A  1 348 ? 78.206  38.546  34.513  1.00 34.89  ? 348 VAL A CG2 1 
ATOM   2813  N  N   . LYS A  1 349 ? 79.727  37.925  38.042  1.00 33.87  ? 349 LYS A N   1 
ATOM   2814  C  CA  . LYS A  1 349 ? 80.940  38.580  38.512  1.00 35.08  ? 349 LYS A CA  1 
ATOM   2815  C  C   . LYS A  1 349 ? 81.714  39.070  37.302  1.00 31.96  ? 349 LYS A C   1 
ATOM   2816  O  O   . LYS A  1 349 ? 81.737  38.403  36.259  1.00 29.72  ? 349 LYS A O   1 
ATOM   2817  C  CB  . LYS A  1 349 ? 81.814  37.645  39.376  1.00 46.57  ? 349 LYS A CB  1 
ATOM   2818  C  CG  . LYS A  1 349 ? 83.145  38.320  39.857  1.00 65.48  ? 349 LYS A CG  1 
ATOM   2819  C  CD  . LYS A  1 349 ? 83.832  37.642  41.084  1.00 77.80  ? 349 LYS A CD  1 
ATOM   2820  C  CE  . LYS A  1 349 ? 83.008  37.749  42.410  1.00 84.37  ? 349 LYS A CE  1 
ATOM   2821  N  NZ  . LYS A  1 349 ? 81.751  36.894  42.447  1.00 90.45  ? 349 LYS A NZ  1 
ATOM   2822  N  N   . ASP A  1 350 ? 82.313  40.247  37.432  1.00 27.35  ? 350 ASP A N   1 
ATOM   2823  C  CA  . ASP A  1 350 ? 83.060  40.830  36.344  1.00 27.28  ? 350 ASP A CA  1 
ATOM   2824  C  C   . ASP A  1 350 ? 84.145  41.620  37.009  1.00 28.82  ? 350 ASP A C   1 
ATOM   2825  O  O   . ASP A  1 350 ? 83.891  42.517  37.809  1.00 32.69  ? 350 ASP A O   1 
ATOM   2826  C  CB  . ASP A  1 350 ? 82.125  41.747  35.540  1.00 32.54  ? 350 ASP A CB  1 
ATOM   2827  C  CG  . ASP A  1 350 ? 82.682  42.131  34.190  1.00 38.00  ? 350 ASP A CG  1 
ATOM   2828  O  OD1 . ASP A  1 350 ? 83.922  42.313  34.101  1.00 40.78  ? 350 ASP A OD1 1 
ATOM   2829  O  OD2 . ASP A  1 350 ? 81.875  42.256  33.220  1.00 37.53  ? 350 ASP A OD2 1 
ATOM   2830  N  N   . GLN A  1 351 ? 85.379  41.286  36.714  1.00 30.16  ? 351 GLN A N   1 
ATOM   2831  C  CA  . GLN A  1 351 ? 86.463  41.998  37.352  1.00 34.04  ? 351 GLN A CA  1 
ATOM   2832  C  C   . GLN A  1 351 ? 86.839  43.318  36.692  1.00 37.46  ? 351 GLN A C   1 
ATOM   2833  O  O   . GLN A  1 351 ? 87.896  43.866  36.998  1.00 43.68  ? 351 GLN A O   1 
ATOM   2834  C  CB  . GLN A  1 351 ? 87.693  41.094  37.504  1.00 38.51  ? 351 GLN A CB  1 
ATOM   2835  C  CG  . GLN A  1 351 ? 87.533  39.927  38.499  1.00 37.76  ? 351 GLN A CG  1 
ATOM   2836  C  CD  . GLN A  1 351 ? 87.644  40.344  39.940  1.00 41.70  ? 351 GLN A CD  1 
ATOM   2837  O  OE1 . GLN A  1 351 ? 88.691  40.800  40.374  1.00 46.85  ? 351 GLN A OE1 1 
ATOM   2838  N  NE2 . GLN A  1 351 ? 86.565  40.172  40.703  1.00 45.20  ? 351 GLN A NE2 1 
ATOM   2839  N  N   . SER A  1 352 ? 86.033  43.800  35.743  1.00 35.44  ? 352 SER A N   1 
ATOM   2840  C  CA  . SER A  1 352 ? 86.293  45.102  35.095  1.00 30.84  ? 352 SER A CA  1 
ATOM   2841  C  C   . SER A  1 352 ? 85.263  46.056  35.609  1.00 28.51  ? 352 SER A C   1 
ATOM   2842  O  O   . SER A  1 352 ? 85.346  47.256  35.389  1.00 31.34  ? 352 SER A O   1 
ATOM   2843  C  CB  . SER A  1 352 ? 86.135  45.060  33.591  1.00 25.60  ? 352 SER A CB  1 
ATOM   2844  O  OG  . SER A  1 352 ? 87.301  44.551  33.013  1.00 44.76  ? 352 SER A OG  1 
ATOM   2845  N  N   . ALA A  1 353 ? 84.242  45.489  36.228  1.00 23.50  ? 353 ALA A N   1 
ATOM   2846  C  CA  . ALA A  1 353 ? 83.178  46.279  36.738  1.00 21.01  ? 353 ALA A CA  1 
ATOM   2847  C  C   . ALA A  1 353 ? 83.677  46.816  38.002  1.00 23.01  ? 353 ALA A C   1 
ATOM   2848  O  O   . ALA A  1 353 ? 84.542  46.239  38.626  1.00 27.78  ? 353 ALA A O   1 
ATOM   2849  C  CB  . ALA A  1 353 ? 81.984  45.435  37.006  1.00 18.19  ? 353 ALA A CB  1 
ATOM   2850  N  N   . PRO A  1 354 ? 83.163  47.959  38.389  1.00 24.12  ? 354 PRO A N   1 
ATOM   2851  C  CA  . PRO A  1 354 ? 83.534  48.623  39.628  1.00 23.30  ? 354 PRO A CA  1 
ATOM   2852  C  C   . PRO A  1 354 ? 82.813  47.968  40.795  1.00 20.21  ? 354 PRO A C   1 
ATOM   2853  O  O   . PRO A  1 354 ? 81.981  47.108  40.594  1.00 21.00  ? 354 PRO A O   1 
ATOM   2854  C  CB  . PRO A  1 354 ? 82.962  50.024  39.411  1.00 27.65  ? 354 PRO A CB  1 
ATOM   2855  C  CG  . PRO A  1 354 ? 81.737  49.763  38.554  1.00 25.94  ? 354 PRO A CG  1 
ATOM   2856  C  CD  . PRO A  1 354 ? 82.342  48.835  37.544  1.00 28.01  ? 354 PRO A CD  1 
ATOM   2857  N  N   . VAL A  1 355 ? 83.136  48.391  42.009  1.00 16.41  ? 355 VAL A N   1 
ATOM   2858  C  CA  . VAL A  1 355 ? 82.449  47.943  43.205  1.00 21.91  ? 355 VAL A CA  1 
ATOM   2859  C  C   . VAL A  1 355 ? 81.382  49.068  43.450  1.00 25.69  ? 355 VAL A C   1 
ATOM   2860  O  O   . VAL A  1 355 ? 81.715  50.271  43.416  1.00 30.30  ? 355 VAL A O   1 
ATOM   2861  C  CB  . VAL A  1 355 ? 83.450  47.900  44.402  1.00 27.05  ? 355 VAL A CB  1 
ATOM   2862  C  CG1 . VAL A  1 355 ? 82.781  47.491  45.715  1.00 28.61  ? 355 VAL A CG1 1 
ATOM   2863  C  CG2 . VAL A  1 355 ? 84.589  46.960  44.074  1.00 30.21  ? 355 VAL A CG2 1 
ATOM   2864  N  N   . TYR A  1 356 ? 80.105  48.711  43.604  1.00 25.24  ? 356 TYR A N   1 
ATOM   2865  C  CA  . TYR A  1 356 ? 79.077  49.718  43.844  1.00 22.52  ? 356 TYR A CA  1 
ATOM   2866  C  C   . TYR A  1 356 ? 78.798  49.750  45.355  1.00 26.34  ? 356 TYR A C   1 
ATOM   2867  O  O   . TYR A  1 356 ? 78.314  48.773  45.938  1.00 32.77  ? 356 TYR A O   1 
ATOM   2868  C  CB  . TYR A  1 356 ? 77.780  49.414  43.061  1.00 22.60  ? 356 TYR A CB  1 
ATOM   2869  C  CG  . TYR A  1 356 ? 77.918  49.325  41.569  1.00 19.61  ? 356 TYR A CG  1 
ATOM   2870  C  CD1 . TYR A  1 356 ? 78.486  48.206  40.975  1.00 25.78  ? 356 TYR A CD1 1 
ATOM   2871  C  CD2 . TYR A  1 356 ? 77.496  50.353  40.748  1.00 22.17  ? 356 TYR A CD2 1 
ATOM   2872  C  CE1 . TYR A  1 356 ? 78.634  48.111  39.596  1.00 30.84  ? 356 TYR A CE1 1 
ATOM   2873  C  CE2 . TYR A  1 356 ? 77.643  50.272  39.342  1.00 23.84  ? 356 TYR A CE2 1 
ATOM   2874  C  CZ  . TYR A  1 356 ? 78.208  49.137  38.777  1.00 26.45  ? 356 TYR A CZ  1 
ATOM   2875  O  OH  . TYR A  1 356 ? 78.287  48.955  37.411  1.00 21.23  ? 356 TYR A OH  1 
ATOM   2876  N  N   . ILE A  1 357 ? 79.154  50.856  45.997  1.00 24.03  ? 357 ILE A N   1 
ATOM   2877  C  CA  . ILE A  1 357 ? 78.953  51.045  47.440  1.00 17.54  ? 357 ILE A CA  1 
ATOM   2878  C  C   . ILE A  1 357 ? 77.826  52.087  47.633  1.00 20.46  ? 357 ILE A C   1 
ATOM   2879  O  O   . ILE A  1 357 ? 77.579  52.944  46.742  1.00 27.38  ? 357 ILE A O   1 
ATOM   2880  C  CB  . ILE A  1 357 ? 80.255  51.564  48.106  1.00 18.46  ? 357 ILE A CB  1 
ATOM   2881  C  CG1 . ILE A  1 357 ? 81.303  50.462  48.143  1.00 25.61  ? 357 ILE A CG1 1 
ATOM   2882  C  CG2 . ILE A  1 357 ? 80.026  52.037  49.516  1.00 19.87  ? 357 ILE A CG2 1 
ATOM   2883  C  CD1 . ILE A  1 357 ? 82.589  50.893  48.726  1.00 26.72  ? 357 ILE A CD1 1 
ATOM   2884  N  N   . THR A  1 358 ? 77.077  51.958  48.733  1.00 11.48  ? 358 THR A N   1 
ATOM   2885  C  CA  . THR A  1 358 ? 76.045  52.915  49.014  1.00 11.07  ? 358 THR A CA  1 
ATOM   2886  C  C   . THR A  1 358 ? 76.140  53.410  50.439  1.00 14.64  ? 358 THR A C   1 
ATOM   2887  O  O   . THR A  1 358 ? 76.059  52.611  51.328  1.00 21.11  ? 358 THR A O   1 
ATOM   2888  C  CB  . THR A  1 358 ? 74.607  52.395  48.617  1.00 9.16   ? 358 THR A CB  1 
ATOM   2889  O  OG1 . THR A  1 358 ? 73.778  52.202  49.752  1.00 14.04  ? 358 THR A OG1 1 
ATOM   2890  C  CG2 . THR A  1 358 ? 74.641  51.202  47.731  1.00 3.04   ? 358 THR A CG2 1 
ATOM   2891  N  N   . ILE A  1 359 ? 76.392  54.705  50.644  1.00 17.91  ? 359 ILE A N   1 
ATOM   2892  C  CA  . ILE A  1 359 ? 76.505  55.261  51.979  1.00 19.79  ? 359 ILE A CA  1 
ATOM   2893  C  C   . ILE A  1 359 ? 75.512  56.388  52.259  1.00 24.25  ? 359 ILE A C   1 
ATOM   2894  O  O   . ILE A  1 359 ? 75.897  57.489  52.712  1.00 26.16  ? 359 ILE A O   1 
ATOM   2895  C  CB  . ILE A  1 359 ? 77.901  55.859  52.285  1.00 26.25  ? 359 ILE A CB  1 
ATOM   2896  C  CG1 . ILE A  1 359 ? 78.458  56.545  51.054  1.00 27.35  ? 359 ILE A CG1 1 
ATOM   2897  C  CG2 . ILE A  1 359 ? 78.830  54.897  52.979  1.00 17.62  ? 359 ILE A CG2 1 
ATOM   2898  C  CD1 . ILE A  1 359 ? 78.976  55.621  50.060  1.00 39.41  ? 359 ILE A CD1 1 
ATOM   2899  N  N   . GLY A  1 360 ? 74.230  56.142  52.039  1.00 23.49  ? 360 GLY A N   1 
ATOM   2900  C  CA  . GLY A  1 360 ? 73.256  57.181  52.320  1.00 26.03  ? 360 GLY A CA  1 
ATOM   2901  C  C   . GLY A  1 360 ? 72.772  57.058  53.745  1.00 26.66  ? 360 GLY A C   1 
ATOM   2902  O  O   . GLY A  1 360 ? 71.682  57.488  54.102  1.00 32.22  ? 360 GLY A O   1 
ATOM   2903  N  N   . ASP A  1 361 ? 73.635  56.567  54.611  1.00 26.51  ? 361 ASP A N   1 
ATOM   2904  C  CA  . ASP A  1 361 ? 73.213  56.349  55.986  1.00 27.08  ? 361 ASP A CA  1 
ATOM   2905  C  C   . ASP A  1 361 ? 73.800  57.337  56.974  1.00 27.15  ? 361 ASP A C   1 
ATOM   2906  O  O   . ASP A  1 361 ? 73.983  56.989  58.153  1.00 31.37  ? 361 ASP A O   1 
ATOM   2907  C  CB  . ASP A  1 361 ? 73.620  54.923  56.372  1.00 27.43  ? 361 ASP A CB  1 
ATOM   2908  C  CG  . ASP A  1 361 ? 75.124  54.738  56.392  1.00 25.18  ? 361 ASP A CG  1 
ATOM   2909  O  OD1 . ASP A  1 361 ? 75.813  55.421  55.610  1.00 30.76  ? 361 ASP A OD1 1 
ATOM   2910  O  OD2 . ASP A  1 361 ? 75.619  53.946  57.213  1.00 34.07  ? 361 ASP A OD2 1 
ATOM   2911  N  N   . ALA A  1 362 ? 74.100  58.554  56.532  1.00 21.86  ? 362 ALA A N   1 
ATOM   2912  C  CA  . ALA A  1 362 ? 74.717  59.504  57.464  1.00 18.16  ? 362 ALA A CA  1 
ATOM   2913  C  C   . ALA A  1 362 ? 73.749  60.091  58.463  1.00 19.16  ? 362 ALA A C   1 
ATOM   2914  O  O   . ALA A  1 362 ? 74.187  60.748  59.411  1.00 21.17  ? 362 ALA A O   1 
ATOM   2915  C  CB  . ALA A  1 362 ? 75.483  60.586  56.745  1.00 14.85  ? 362 ALA A CB  1 
ATOM   2916  N  N   . GLY A  1 363 ? 72.437  59.916  58.247  1.00 21.69  ? 363 GLY A N   1 
ATOM   2917  C  CA  . GLY A  1 363 ? 71.511  60.401  59.255  1.00 13.38  ? 363 GLY A CA  1 
ATOM   2918  C  C   . GLY A  1 363 ? 70.139  60.841  58.836  1.00 16.25  ? 363 GLY A C   1 
ATOM   2919  O  O   . GLY A  1 363 ? 69.145  60.477  59.459  1.00 13.26  ? 363 GLY A O   1 
ATOM   2920  N  N   . ASN A  1 364 ? 70.067  61.548  57.724  1.00 16.93  ? 364 ASN A N   1 
ATOM   2921  C  CA  . ASN A  1 364 ? 68.821  62.113  57.267  1.00 18.36  ? 364 ASN A CA  1 
ATOM   2922  C  C   . ASN A  1 364 ? 68.058  62.676  58.437  1.00 19.55  ? 364 ASN A C   1 
ATOM   2923  O  O   . ASN A  1 364 ? 68.654  63.288  59.323  1.00 24.26  ? 364 ASN A O   1 
ATOM   2924  C  CB  . ASN A  1 364 ? 67.969  61.182  56.392  1.00 21.21  ? 364 ASN A CB  1 
ATOM   2925  C  CG  . ASN A  1 364 ? 67.681  59.900  57.023  1.00 22.89  ? 364 ASN A CG  1 
ATOM   2926  O  OD1 . ASN A  1 364 ? 68.521  59.000  56.979  1.00 27.47  ? 364 ASN A OD1 1 
ATOM   2927  N  ND2 . ASN A  1 364 ? 66.487  59.762  57.596  1.00 14.98  ? 364 ASN A ND2 1 
ATOM   2928  N  N   . TYR A  1 365 ? 66.750  62.499  58.444  1.00 17.90  ? 365 TYR A N   1 
ATOM   2929  C  CA  . TYR A  1 365 ? 65.965  63.038  59.526  1.00 22.81  ? 365 TYR A CA  1 
ATOM   2930  C  C   . TYR A  1 365 ? 65.786  62.042  60.632  1.00 30.00  ? 365 TYR A C   1 
ATOM   2931  O  O   . TYR A  1 365 ? 64.735  62.015  61.298  1.00 30.03  ? 365 TYR A O   1 
ATOM   2932  C  CB  . TYR A  1 365 ? 64.623  63.495  59.033  1.00 23.12  ? 365 TYR A CB  1 
ATOM   2933  C  CG  . TYR A  1 365 ? 63.999  62.579  58.036  1.00 25.04  ? 365 TYR A CG  1 
ATOM   2934  C  CD1 . TYR A  1 365 ? 64.416  62.579  56.707  1.00 29.47  ? 365 TYR A CD1 1 
ATOM   2935  C  CD2 . TYR A  1 365 ? 62.967  61.726  58.402  1.00 27.61  ? 365 TYR A CD2 1 
ATOM   2936  C  CE1 . TYR A  1 365 ? 63.824  61.758  55.773  1.00 25.59  ? 365 TYR A CE1 1 
ATOM   2937  C  CE2 . TYR A  1 365 ? 62.355  60.894  57.467  1.00 28.02  ? 365 TYR A CE2 1 
ATOM   2938  C  CZ  . TYR A  1 365 ? 62.791  60.917  56.153  1.00 32.97  ? 365 TYR A CZ  1 
ATOM   2939  O  OH  . TYR A  1 365 ? 62.166  60.112  55.213  1.00 46.11  ? 365 TYR A OH  1 
ATOM   2940  N  N   . GLY A  1 366 ? 66.832  61.252  60.850  1.00 32.76  ? 366 GLY A N   1 
ATOM   2941  C  CA  . GLY A  1 366 ? 66.811  60.224  61.878  1.00 33.18  ? 366 GLY A CA  1 
ATOM   2942  C  C   . GLY A  1 366 ? 66.150  58.894  61.506  1.00 35.22  ? 366 GLY A C   1 
ATOM   2943  O  O   . GLY A  1 366 ? 65.705  58.183  62.395  1.00 40.63  ? 366 GLY A O   1 
ATOM   2944  N  N   . VAL A  1 367 ? 66.171  58.482  60.241  1.00 34.38  ? 367 VAL A N   1 
ATOM   2945  C  CA  . VAL A  1 367 ? 65.519  57.230  59.890  1.00 32.36  ? 367 VAL A CA  1 
ATOM   2946  C  C   . VAL A  1 367 ? 66.387  56.327  59.051  1.00 34.25  ? 367 VAL A C   1 
ATOM   2947  O  O   . VAL A  1 367 ? 66.988  56.787  58.063  1.00 32.78  ? 367 VAL A O   1 
ATOM   2948  C  CB  . VAL A  1 367 ? 64.219  57.506  59.148  1.00 29.71  ? 367 VAL A CB  1 
ATOM   2949  C  CG1 . VAL A  1 367 ? 63.801  56.330  58.352  1.00 29.91  ? 367 VAL A CG1 1 
ATOM   2950  C  CG2 . VAL A  1 367 ? 63.178  57.806  60.126  1.00 26.95  ? 367 VAL A CG2 1 
ATOM   2951  N  N   . ILE A  1 368 ? 66.335  55.035  59.383  1.00 31.78  ? 368 ILE A N   1 
ATOM   2952  C  CA  . ILE A  1 368 ? 67.105  54.002  58.690  1.00 34.20  ? 368 ILE A CA  1 
ATOM   2953  C  C   . ILE A  1 368 ? 66.249  53.059  57.819  1.00 32.12  ? 368 ILE A C   1 
ATOM   2954  O  O   . ILE A  1 368 ? 65.093  52.788  58.168  1.00 37.34  ? 368 ILE A O   1 
ATOM   2955  C  CB  . ILE A  1 368 ? 67.872  53.154  59.715  1.00 39.39  ? 368 ILE A CB  1 
ATOM   2956  C  CG1 . ILE A  1 368 ? 69.133  53.867  60.172  1.00 49.60  ? 368 ILE A CG1 1 
ATOM   2957  C  CG2 . ILE A  1 368 ? 68.338  51.878  59.088  1.00 45.92  ? 368 ILE A CG2 1 
ATOM   2958  C  CD1 . ILE A  1 368 ? 70.326  53.726  59.187  1.00 58.38  ? 368 ILE A CD1 1 
ATOM   2959  N  N   . ASP A  1 369 ? 66.795  52.584  56.694  1.00 25.14  ? 369 ASP A N   1 
ATOM   2960  C  CA  . ASP A  1 369 ? 66.084  51.653  55.845  1.00 27.51  ? 369 ASP A CA  1 
ATOM   2961  C  C   . ASP A  1 369 ? 66.584  50.283  56.227  1.00 30.69  ? 369 ASP A C   1 
ATOM   2962  O  O   . ASP A  1 369 ? 67.701  49.911  55.903  1.00 30.17  ? 369 ASP A O   1 
ATOM   2963  C  CB  . ASP A  1 369 ? 66.390  51.885  54.390  1.00 30.07  ? 369 ASP A CB  1 
ATOM   2964  C  CG  . ASP A  1 369 ? 65.825  53.160  53.893  1.00 29.83  ? 369 ASP A CG  1 
ATOM   2965  O  OD1 . ASP A  1 369 ? 64.703  53.514  54.304  1.00 27.96  ? 369 ASP A OD1 1 
ATOM   2966  O  OD2 . ASP A  1 369 ? 66.509  53.803  53.076  1.00 37.42  ? 369 ASP A OD2 1 
ATOM   2967  N  N   . SER A  1 370 ? 65.726  49.512  56.876  1.00 33.77  ? 370 SER A N   1 
ATOM   2968  C  CA  . SER A  1 370 ? 66.110  48.209  57.357  1.00 36.31  ? 370 SER A CA  1 
ATOM   2969  C  C   . SER A  1 370 ? 65.583  47.083  56.507  1.00 36.28  ? 370 SER A C   1 
ATOM   2970  O  O   . SER A  1 370 ? 66.187  46.012  56.475  1.00 42.00  ? 370 SER A O   1 
ATOM   2971  C  CB  . SER A  1 370 ? 65.603  48.027  58.783  1.00 41.08  ? 370 SER A CB  1 
ATOM   2972  O  OG  . SER A  1 370 ? 64.191  48.028  58.795  1.00 45.13  ? 370 SER A OG  1 
ATOM   2973  N  N   . ASN A  1 371 ? 64.448  47.299  55.851  1.00 30.55  ? 371 ASN A N   1 
ATOM   2974  C  CA  . ASN A  1 371 ? 63.886  46.245  55.032  1.00 23.98  ? 371 ASN A CA  1 
ATOM   2975  C  C   . ASN A  1 371 ? 64.802  45.935  53.857  1.00 26.49  ? 371 ASN A C   1 
ATOM   2976  O  O   . ASN A  1 371 ? 65.165  46.822  53.033  1.00 31.89  ? 371 ASN A O   1 
ATOM   2977  C  CB  . ASN A  1 371 ? 62.479  46.585  54.607  1.00 20.86  ? 371 ASN A CB  1 
ATOM   2978  C  CG  . ASN A  1 371 ? 61.487  46.561  55.770  1.00 26.40  ? 371 ASN A CG  1 
ATOM   2979  O  OD1 . ASN A  1 371 ? 60.295  46.642  55.525  1.00 31.77  ? 371 ASN A OD1 1 
ATOM   2980  N  ND2 . ASN A  1 371 ? 61.960  46.434  57.027  1.00 25.18  ? 371 ASN A ND2 1 
ATOM   2981  N  N   . MET A  1 372 ? 65.163  44.657  53.778  1.00 22.68  ? 372 MET A N   1 
ATOM   2982  C  CA  . MET A  1 372 ? 66.081  44.164  52.786  1.00 18.48  ? 372 MET A CA  1 
ATOM   2983  C  C   . MET A  1 372 ? 65.483  43.007  52.051  1.00 19.48  ? 372 MET A C   1 
ATOM   2984  O  O   . MET A  1 372 ? 64.624  42.328  52.570  1.00 16.54  ? 372 MET A O   1 
ATOM   2985  C  CB  . MET A  1 372 ? 67.345  43.700  53.479  1.00 15.33  ? 372 MET A CB  1 
ATOM   2986  C  CG  . MET A  1 372 ? 67.922  44.745  54.345  1.00 21.77  ? 372 MET A CG  1 
ATOM   2987  S  SD  . MET A  1 372 ? 69.208  44.008  55.188  1.00 21.90  ? 372 MET A SD  1 
ATOM   2988  C  CE  . MET A  1 372 ? 68.301  43.575  56.772  1.00 36.35  ? 372 MET A CE  1 
ATOM   2989  N  N   . ILE A  1 373 ? 65.916  42.845  50.813  1.00 21.99  ? 373 ILE A N   1 
ATOM   2990  C  CA  . ILE A  1 373 ? 65.459  41.795  49.951  1.00 27.66  ? 373 ILE A CA  1 
ATOM   2991  C  C   . ILE A  1 373 ? 66.052  40.506  50.538  1.00 35.28  ? 373 ILE A C   1 
ATOM   2992  O  O   . ILE A  1 373 ? 67.273  40.301  50.523  1.00 37.20  ? 373 ILE A O   1 
ATOM   2993  C  CB  . ILE A  1 373 ? 65.973  42.083  48.534  1.00 29.62  ? 373 ILE A CB  1 
ATOM   2994  C  CG1 . ILE A  1 373 ? 65.176  43.203  47.902  1.00 25.77  ? 373 ILE A CG1 1 
ATOM   2995  C  CG2 . ILE A  1 373 ? 65.894  40.933  47.675  1.00 31.78  ? 373 ILE A CG2 1 
ATOM   2996  C  CD1 . ILE A  1 373 ? 63.704  43.139  48.153  1.00 32.88  ? 373 ILE A CD1 1 
ATOM   2997  N  N   . GLN A  1 374 ? 65.191  39.692  51.149  1.00 40.04  ? 374 GLN A N   1 
ATOM   2998  C  CA  . GLN A  1 374 ? 65.611  38.434  51.767  1.00 38.75  ? 374 GLN A CA  1 
ATOM   2999  C  C   . GLN A  1 374 ? 65.392  37.355  50.734  1.00 39.43  ? 374 GLN A C   1 
ATOM   3000  O  O   . GLN A  1 374 ? 64.230  37.118  50.366  1.00 48.06  ? 374 GLN A O   1 
ATOM   3001  C  CB  . GLN A  1 374 ? 64.749  38.155  52.981  1.00 43.70  ? 374 GLN A CB  1 
ATOM   3002  C  CG  . GLN A  1 374 ? 65.044  39.014  54.189  1.00 49.10  ? 374 GLN A CG  1 
ATOM   3003  C  CD  . GLN A  1 374 ? 66.501  38.970  54.628  1.00 55.96  ? 374 GLN A CD  1 
ATOM   3004  O  OE1 . GLN A  1 374 ? 66.927  39.812  55.413  1.00 68.66  ? 374 GLN A OE1 1 
ATOM   3005  N  NE2 . GLN A  1 374 ? 67.272  37.987  54.144  1.00 62.67  ? 374 GLN A NE2 1 
ATOM   3006  N  N   . PRO A  1 375 ? 66.445  36.578  50.362  1.00 36.22  ? 375 PRO A N   1 
ATOM   3007  C  CA  . PRO A  1 375 ? 67.837  36.626  50.806  1.00 35.25  ? 375 PRO A CA  1 
ATOM   3008  C  C   . PRO A  1 375 ? 68.841  37.498  50.052  1.00 36.40  ? 375 PRO A C   1 
ATOM   3009  O  O   . PRO A  1 375 ? 68.686  37.813  48.869  1.00 43.78  ? 375 PRO A O   1 
ATOM   3010  C  CB  . PRO A  1 375 ? 68.228  35.174  50.714  1.00 35.66  ? 375 PRO A CB  1 
ATOM   3011  C  CG  . PRO A  1 375 ? 67.641  34.791  49.401  1.00 32.50  ? 375 PRO A CG  1 
ATOM   3012  C  CD  . PRO A  1 375 ? 66.253  35.423  49.459  1.00 34.23  ? 375 PRO A CD  1 
ATOM   3013  N  N   . GLN A  1 376 ? 69.915  37.833  50.748  1.00 35.03  ? 376 GLN A N   1 
ATOM   3014  C  CA  . GLN A  1 376 ? 70.930  38.668  50.187  1.00 31.38  ? 376 GLN A CA  1 
ATOM   3015  C  C   . GLN A  1 376 ? 71.362  38.080  48.877  1.00 31.53  ? 376 GLN A C   1 
ATOM   3016  O  O   . GLN A  1 376 ? 71.877  36.966  48.814  1.00 34.76  ? 376 GLN A O   1 
ATOM   3017  C  CB  . GLN A  1 376 ? 72.101  38.761  51.130  1.00 35.46  ? 376 GLN A CB  1 
ATOM   3018  C  CG  . GLN A  1 376 ? 73.252  39.583  50.565  1.00 47.68  ? 376 GLN A CG  1 
ATOM   3019  C  CD  . GLN A  1 376 ? 74.325  39.891  51.594  1.00 48.94  ? 376 GLN A CD  1 
ATOM   3020  O  OE1 . GLN A  1 376 ? 74.105  39.742  52.805  1.00 55.76  ? 376 GLN A OE1 1 
ATOM   3021  N  NE2 . GLN A  1 376 ? 75.485  40.355  51.124  1.00 48.73  ? 376 GLN A NE2 1 
ATOM   3022  N  N   . PRO A  1 377 ? 71.081  38.791  47.791  1.00 29.58  ? 377 PRO A N   1 
ATOM   3023  C  CA  . PRO A  1 377 ? 71.462  38.312  46.475  1.00 29.94  ? 377 PRO A CA  1 
ATOM   3024  C  C   . PRO A  1 377 ? 72.981  38.199  46.340  1.00 32.16  ? 377 PRO A C   1 
ATOM   3025  O  O   . PRO A  1 377 ? 73.729  38.842  47.023  1.00 37.02  ? 377 PRO A O   1 
ATOM   3026  C  CB  . PRO A  1 377 ? 70.877  39.383  45.563  1.00 31.14  ? 377 PRO A CB  1 
ATOM   3027  C  CG  . PRO A  1 377 ? 70.977  40.589  46.368  1.00 37.08  ? 377 PRO A CG  1 
ATOM   3028  C  CD  . PRO A  1 377 ? 70.464  40.115  47.702  1.00 31.29  ? 377 PRO A CD  1 
ATOM   3029  N  N   . GLU A  1 378 ? 73.404  37.411  45.379  1.00 38.91  ? 378 GLU A N   1 
ATOM   3030  C  CA  . GLU A  1 378 ? 74.801  37.155  45.090  1.00 44.69  ? 378 GLU A CA  1 
ATOM   3031  C  C   . GLU A  1 378 ? 75.649  38.392  44.902  1.00 40.20  ? 378 GLU A C   1 
ATOM   3032  O  O   . GLU A  1 378 ? 76.750  38.447  45.423  1.00 44.53  ? 378 GLU A O   1 
ATOM   3033  C  CB  . GLU A  1 378 ? 74.961  36.301  43.812  1.00 58.43  ? 378 GLU A CB  1 
ATOM   3034  C  CG  . GLU A  1 378 ? 73.719  35.465  43.346  1.00 82.91  ? 378 GLU A CG  1 
ATOM   3035  C  CD  . GLU A  1 378 ? 72.598  36.265  42.568  1.00 94.22  ? 378 GLU A CD  1 
ATOM   3036  O  OE1 . GLU A  1 378 ? 72.911  36.872  41.484  1.00 98.60  ? 378 GLU A OE1 1 
ATOM   3037  O  OE2 . GLU A  1 378 ? 71.408  36.237  43.039  1.00 96.01  ? 378 GLU A OE2 1 
ATOM   3038  N  N   . TYR A  1 379 ? 75.162  39.365  44.136  1.00 35.57  ? 379 TYR A N   1 
ATOM   3039  C  CA  . TYR A  1 379 ? 75.952  40.562  43.841  1.00 31.58  ? 379 TYR A CA  1 
ATOM   3040  C  C   . TYR A  1 379 ? 76.270  41.419  45.038  1.00 29.77  ? 379 TYR A C   1 
ATOM   3041  O  O   . TYR A  1 379 ? 77.229  42.213  45.002  1.00 29.18  ? 379 TYR A O   1 
ATOM   3042  C  CB  . TYR A  1 379 ? 75.275  41.408  42.770  1.00 30.09  ? 379 TYR A CB  1 
ATOM   3043  C  CG  . TYR A  1 379 ? 73.878  41.887  43.136  1.00 29.65  ? 379 TYR A CG  1 
ATOM   3044  C  CD1 . TYR A  1 379 ? 73.680  42.999  43.946  1.00 26.41  ? 379 TYR A CD1 1 
ATOM   3045  C  CD2 . TYR A  1 379 ? 72.762  41.249  42.626  1.00 29.96  ? 379 TYR A CD2 1 
ATOM   3046  C  CE1 . TYR A  1 379 ? 72.402  43.453  44.231  1.00 25.44  ? 379 TYR A CE1 1 
ATOM   3047  C  CE2 . TYR A  1 379 ? 71.486  41.700  42.907  1.00 26.95  ? 379 TYR A CE2 1 
ATOM   3048  C  CZ  . TYR A  1 379 ? 71.314  42.800  43.708  1.00 24.42  ? 379 TYR A CZ  1 
ATOM   3049  O  OH  . TYR A  1 379 ? 70.039  43.214  44.014  1.00 33.66  ? 379 TYR A OH  1 
ATOM   3050  N  N   . SER A  1 380 ? 75.488  41.226  46.096  1.00 23.26  ? 380 SER A N   1 
ATOM   3051  C  CA  . SER A  1 380 ? 75.644  41.983  47.303  1.00 18.93  ? 380 SER A CA  1 
ATOM   3052  C  C   . SER A  1 380 ? 76.711  41.353  48.162  1.00 21.43  ? 380 SER A C   1 
ATOM   3053  O  O   . SER A  1 380 ? 76.601  40.225  48.558  1.00 25.92  ? 380 SER A O   1 
ATOM   3054  C  CB  . SER A  1 380 ? 74.323  42.020  48.036  1.00 14.43  ? 380 SER A CB  1 
ATOM   3055  O  OG  . SER A  1 380 ? 74.473  42.836  49.159  1.00 24.13  ? 380 SER A OG  1 
ATOM   3056  N  N   . ALA A  1 381 ? 77.792  42.054  48.439  1.00 30.59  ? 381 ALA A N   1 
ATOM   3057  C  CA  . ALA A  1 381 ? 78.855  41.481  49.278  1.00 30.31  ? 381 ALA A CA  1 
ATOM   3058  C  C   . ALA A  1 381 ? 78.633  41.695  50.746  1.00 31.83  ? 381 ALA A C   1 
ATOM   3059  O  O   . ALA A  1 381 ? 79.017  40.872  51.542  1.00 40.23  ? 381 ALA A O   1 
ATOM   3060  C  CB  . ALA A  1 381 ? 80.185  42.062  48.923  1.00 30.37  ? 381 ALA A CB  1 
ATOM   3061  N  N   . PHE A  1 382 ? 77.997  42.795  51.109  1.00 31.54  ? 382 PHE A N   1 
ATOM   3062  C  CA  . PHE A  1 382 ? 77.798  43.129  52.506  1.00 26.69  ? 382 PHE A CA  1 
ATOM   3063  C  C   . PHE A  1 382 ? 76.747  44.235  52.662  1.00 23.38  ? 382 PHE A C   1 
ATOM   3064  O  O   . PHE A  1 382 ? 76.777  45.248  51.992  1.00 19.30  ? 382 PHE A O   1 
ATOM   3065  C  CB  . PHE A  1 382 ? 79.125  43.639  53.047  1.00 26.75  ? 382 PHE A CB  1 
ATOM   3066  C  CG  . PHE A  1 382 ? 79.044  44.116  54.443  1.00 37.05  ? 382 PHE A CG  1 
ATOM   3067  C  CD1 . PHE A  1 382 ? 78.346  45.277  54.764  1.00 45.20  ? 382 PHE A CD1 1 
ATOM   3068  C  CD2 . PHE A  1 382 ? 79.645  43.403  55.466  1.00 40.25  ? 382 PHE A CD2 1 
ATOM   3069  C  CE1 . PHE A  1 382 ? 78.245  45.723  56.100  1.00 49.28  ? 382 PHE A CE1 1 
ATOM   3070  C  CE2 . PHE A  1 382 ? 79.554  43.829  56.789  1.00 41.68  ? 382 PHE A CE2 1 
ATOM   3071  C  CZ  . PHE A  1 382 ? 78.853  44.992  57.111  1.00 46.02  ? 382 PHE A CZ  1 
ATOM   3072  N  N   . ARG A  1 383 ? 75.840  44.088  53.590  1.00 22.70  ? 383 ARG A N   1 
ATOM   3073  C  CA  . ARG A  1 383 ? 74.880  45.146  53.764  1.00 25.16  ? 383 ARG A CA  1 
ATOM   3074  C  C   . ARG A  1 383 ? 74.482  45.272  55.194  1.00 28.17  ? 383 ARG A C   1 
ATOM   3075  O  O   . ARG A  1 383 ? 74.416  44.279  55.904  1.00 34.53  ? 383 ARG A O   1 
ATOM   3076  C  CB  . ARG A  1 383 ? 73.630  44.990  52.901  1.00 20.98  ? 383 ARG A CB  1 
ATOM   3077  C  CG  . ARG A  1 383 ? 73.256  43.640  52.426  1.00 24.73  ? 383 ARG A CG  1 
ATOM   3078  C  CD  . ARG A  1 383 ? 71.840  43.265  52.925  1.00 31.08  ? 383 ARG A CD  1 
ATOM   3079  N  NE  . ARG A  1 383 ? 70.907  42.866  51.864  1.00 35.41  ? 383 ARG A NE  1 
ATOM   3080  C  CZ  . ARG A  1 383 ? 70.086  41.822  51.918  1.00 39.31  ? 383 ARG A CZ  1 
ATOM   3081  N  NH1 . ARG A  1 383 ? 70.055  41.012  52.961  1.00 43.77  ? 383 ARG A NH1 1 
ATOM   3082  N  NH2 . ARG A  1 383 ? 69.208  41.647  50.967  1.00 42.34  ? 383 ARG A NH2 1 
ATOM   3083  N  N   . GLU A  1 384 ? 74.274  46.503  55.640  1.00 32.85  ? 384 GLU A N   1 
ATOM   3084  C  CA  . GLU A  1 384 ? 73.845  46.729  57.003  1.00 29.67  ? 384 GLU A CA  1 
ATOM   3085  C  C   . GLU A  1 384 ? 73.102  48.021  57.114  1.00 26.33  ? 384 GLU A C   1 
ATOM   3086  O  O   . GLU A  1 384 ? 73.460  49.002  56.454  1.00 26.75  ? 384 GLU A O   1 
ATOM   3087  C  CB  . GLU A  1 384 ? 75.014  46.738  57.980  1.00 37.46  ? 384 GLU A CB  1 
ATOM   3088  C  CG  . GLU A  1 384 ? 74.534  46.642  59.425  1.00 39.04  ? 384 GLU A CG  1 
ATOM   3089  C  CD  . GLU A  1 384 ? 75.642  46.623  60.445  1.00 36.20  ? 384 GLU A CD  1 
ATOM   3090  O  OE1 . GLU A  1 384 ? 76.632  45.875  60.258  1.00 33.79  ? 384 GLU A OE1 1 
ATOM   3091  O  OE2 . GLU A  1 384 ? 75.496  47.359  61.446  1.00 34.83  ? 384 GLU A OE2 1 
ATOM   3092  N  N   . ALA A  1 385 ? 72.061  47.984  57.949  1.00 22.35  ? 385 ALA A N   1 
ATOM   3093  C  CA  . ALA A  1 385 ? 71.203  49.114  58.229  1.00 18.12  ? 385 ALA A CA  1 
ATOM   3094  C  C   . ALA A  1 385 ? 71.631  49.842  59.482  1.00 19.11  ? 385 ALA A C   1 
ATOM   3095  O  O   . ALA A  1 385 ? 70.964  49.713  60.494  1.00 24.38  ? 385 ALA A O   1 
ATOM   3096  C  CB  . ALA A  1 385 ? 69.775  48.652  58.397  1.00 13.32  ? 385 ALA A CB  1 
ATOM   3097  N  N   . SER A  1 386 ? 72.725  50.601  59.419  1.00 22.08  ? 386 SER A N   1 
ATOM   3098  C  CA  . SER A  1 386 ? 73.245  51.390  60.540  1.00 24.93  ? 386 SER A CA  1 
ATOM   3099  C  C   . SER A  1 386 ? 73.661  52.769  60.072  1.00 25.07  ? 386 SER A C   1 
ATOM   3100  O  O   . SER A  1 386 ? 73.982  52.951  58.918  1.00 27.93  ? 386 SER A O   1 
ATOM   3101  C  CB  . SER A  1 386 ? 74.462  50.725  61.164  1.00 25.68  ? 386 SER A CB  1 
ATOM   3102  O  OG  . SER A  1 386 ? 74.042  49.675  61.995  1.00 40.73  ? 386 SER A OG  1 
ATOM   3103  N  N   . PHE A  1 387 ? 73.644  53.752  60.952  1.00 22.20  ? 387 PHE A N   1 
ATOM   3104  C  CA  . PHE A  1 387 ? 74.055  55.064  60.546  1.00 24.11  ? 387 PHE A CA  1 
ATOM   3105  C  C   . PHE A  1 387 ? 75.563  55.066  60.574  1.00 27.69  ? 387 PHE A C   1 
ATOM   3106  O  O   . PHE A  1 387 ? 76.160  54.287  61.314  1.00 31.02  ? 387 PHE A O   1 
ATOM   3107  C  CB  . PHE A  1 387 ? 73.509  56.104  61.495  1.00 17.46  ? 387 PHE A CB  1 
ATOM   3108  C  CG  . PHE A  1 387 ? 72.053  56.352  61.316  1.00 19.07  ? 387 PHE A CG  1 
ATOM   3109  C  CD1 . PHE A  1 387 ? 71.564  56.845  60.131  1.00 17.78  ? 387 PHE A CD1 1 
ATOM   3110  C  CD2 . PHE A  1 387 ? 71.164  56.134  62.349  1.00 17.98  ? 387 PHE A CD2 1 
ATOM   3111  C  CE1 . PHE A  1 387 ? 70.185  57.125  59.988  1.00 21.17  ? 387 PHE A CE1 1 
ATOM   3112  C  CE2 . PHE A  1 387 ? 69.812  56.405  62.209  1.00 17.88  ? 387 PHE A CE2 1 
ATOM   3113  C  CZ  . PHE A  1 387 ? 69.324  56.904  61.022  1.00 18.31  ? 387 PHE A CZ  1 
ATOM   3114  N  N   . GLY A  1 388 ? 76.177  55.878  59.712  1.00 29.69  ? 388 GLY A N   1 
ATOM   3115  C  CA  . GLY A  1 388 ? 77.629  55.975  59.678  1.00 27.96  ? 388 GLY A CA  1 
ATOM   3116  C  C   . GLY A  1 388 ? 78.135  56.704  58.453  1.00 23.11  ? 388 GLY A C   1 
ATOM   3117  O  O   . GLY A  1 388 ? 77.348  57.205  57.677  1.00 24.34  ? 388 GLY A O   1 
ATOM   3118  N  N   . HIS A  1 389 ? 79.443  56.742  58.274  1.00 21.98  ? 389 HIS A N   1 
ATOM   3119  C  CA  . HIS A  1 389 ? 80.050  57.410  57.136  1.00 21.53  ? 389 HIS A CA  1 
ATOM   3120  C  C   . HIS A  1 389 ? 81.130  56.461  56.638  1.00 23.01  ? 389 HIS A C   1 
ATOM   3121  O  O   . HIS A  1 389 ? 81.366  55.443  57.286  1.00 27.16  ? 389 HIS A O   1 
ATOM   3122  C  CB  . HIS A  1 389 ? 80.698  58.714  57.606  1.00 20.59  ? 389 HIS A CB  1 
ATOM   3123  C  CG  . HIS A  1 389 ? 81.885  58.531  58.511  1.00 21.77  ? 389 HIS A CG  1 
ATOM   3124  N  ND1 . HIS A  1 389 ? 83.191  58.611  58.061  1.00 21.66  ? 389 HIS A ND1 1 
ATOM   3125  C  CD2 . HIS A  1 389 ? 81.960  58.288  59.843  1.00 22.58  ? 389 HIS A CD2 1 
ATOM   3126  C  CE1 . HIS A  1 389 ? 84.021  58.419  59.074  1.00 25.25  ? 389 HIS A CE1 1 
ATOM   3127  N  NE2 . HIS A  1 389 ? 83.298  58.221  60.163  1.00 30.71  ? 389 HIS A NE2 1 
ATOM   3128  N  N   . GLY A  1 390 ? 81.814  56.793  55.541  1.00 22.07  ? 390 GLY A N   1 
ATOM   3129  C  CA  . GLY A  1 390 ? 82.882  55.939  55.043  1.00 15.52  ? 390 GLY A CA  1 
ATOM   3130  C  C   . GLY A  1 390 ? 84.172  56.707  54.787  1.00 17.68  ? 390 GLY A C   1 
ATOM   3131  O  O   . GLY A  1 390 ? 84.201  57.921  54.943  1.00 23.59  ? 390 GLY A O   1 
ATOM   3132  N  N   . MET A  1 391 ? 85.268  56.009  54.526  1.00 16.73  ? 391 MET A N   1 
ATOM   3133  C  CA  . MET A  1 391 ? 86.525  56.676  54.225  1.00 18.49  ? 391 MET A CA  1 
ATOM   3134  C  C   . MET A  1 391 ? 87.132  55.840  53.111  1.00 17.15  ? 391 MET A C   1 
ATOM   3135  O  O   . MET A  1 391 ? 86.999  54.638  53.135  1.00 20.85  ? 391 MET A O   1 
ATOM   3136  C  CB  . MET A  1 391 ? 87.457  56.643  55.438  1.00 28.76  ? 391 MET A CB  1 
ATOM   3137  C  CG  . MET A  1 391 ? 86.938  57.290  56.711  1.00 33.62  ? 391 MET A CG  1 
ATOM   3138  S  SD  . MET A  1 391 ? 87.128  59.029  56.699  1.00 43.83  ? 391 MET A SD  1 
ATOM   3139  C  CE  . MET A  1 391 ? 88.892  59.133  56.343  1.00 31.96  ? 391 MET A CE  1 
ATOM   3140  N  N   . PHE A  1 392 ? 87.699  56.471  52.098  1.00 14.62  ? 392 PHE A N   1 
ATOM   3141  C  CA  . PHE A  1 392 ? 88.344  55.760  51.006  1.00 15.57  ? 392 PHE A CA  1 
ATOM   3142  C  C   . PHE A  1 392 ? 89.770  56.324  50.980  1.00 26.06  ? 392 PHE A C   1 
ATOM   3143  O  O   . PHE A  1 392 ? 90.006  57.503  50.625  1.00 24.00  ? 392 PHE A O   1 
ATOM   3144  C  CB  . PHE A  1 392 ? 87.646  56.093  49.749  1.00 14.96  ? 392 PHE A CB  1 
ATOM   3145  C  CG  . PHE A  1 392 ? 88.125  55.356  48.584  1.00 12.92  ? 392 PHE A CG  1 
ATOM   3146  C  CD1 . PHE A  1 392 ? 87.535  54.171  48.254  1.00 17.43  ? 392 PHE A CD1 1 
ATOM   3147  C  CD2 . PHE A  1 392 ? 89.101  55.882  47.762  1.00 15.61  ? 392 PHE A CD2 1 
ATOM   3148  C  CE1 . PHE A  1 392 ? 87.910  53.519  47.116  1.00 23.72  ? 392 PHE A CE1 1 
ATOM   3149  C  CE2 . PHE A  1 392 ? 89.483  55.246  46.616  1.00 14.23  ? 392 PHE A CE2 1 
ATOM   3150  C  CZ  . PHE A  1 392 ? 88.897  54.073  46.286  1.00 21.71  ? 392 PHE A CZ  1 
ATOM   3151  N  N   . ASP A  1 393 ? 90.703  55.476  51.412  1.00 31.81  ? 393 ASP A N   1 
ATOM   3152  C  CA  . ASP A  1 393 ? 92.095  55.835  51.575  1.00 34.43  ? 393 ASP A CA  1 
ATOM   3153  C  C   . ASP A  1 393 ? 93.028  55.371  50.514  1.00 34.73  ? 393 ASP A C   1 
ATOM   3154  O  O   . ASP A  1 393 ? 93.497  54.238  50.514  1.00 38.84  ? 393 ASP A O   1 
ATOM   3155  C  CB  . ASP A  1 393 ? 92.558  55.296  52.912  1.00 41.99  ? 393 ASP A CB  1 
ATOM   3156  C  CG  . ASP A  1 393 ? 93.815  55.959  53.416  1.00 50.48  ? 393 ASP A CG  1 
ATOM   3157  O  OD1 . ASP A  1 393 ? 94.384  56.858  52.723  1.00 54.01  ? 393 ASP A OD1 1 
ATOM   3158  O  OD2 . ASP A  1 393 ? 94.232  55.553  54.530  1.00 54.14  ? 393 ASP A OD2 1 
ATOM   3159  N  N   . ILE A  1 394 ? 93.373  56.280  49.640  1.00 31.22  ? 394 ILE A N   1 
ATOM   3160  C  CA  . ILE A  1 394 ? 94.254  55.934  48.561  1.00 30.89  ? 394 ILE A CA  1 
ATOM   3161  C  C   . ILE A  1 394 ? 95.655  55.876  49.104  1.00 33.71  ? 394 ILE A C   1 
ATOM   3162  O  O   . ILE A  1 394 ? 96.137  56.819  49.729  1.00 41.34  ? 394 ILE A O   1 
ATOM   3163  C  CB  . ILE A  1 394 ? 94.123  56.954  47.456  1.00 31.28  ? 394 ILE A CB  1 
ATOM   3164  C  CG1 . ILE A  1 394 ? 92.702  56.887  46.905  1.00 34.07  ? 394 ILE A CG1 1 
ATOM   3165  C  CG2 . ILE A  1 394 ? 95.185  56.752  46.396  1.00 27.70  ? 394 ILE A CG2 1 
ATOM   3166  C  CD1 . ILE A  1 394 ? 92.403  57.987  45.912  1.00 45.05  ? 394 ILE A CD1 1 
ATOM   3167  N  N   . LYS A  1 395 ? 96.307  54.754  48.882  1.00 35.11  ? 395 LYS A N   1 
ATOM   3168  C  CA  . LYS A  1 395 ? 97.670  54.553  49.347  1.00 32.41  ? 395 LYS A CA  1 
ATOM   3169  C  C   . LYS A  1 395 ? 98.677  54.588  48.212  1.00 37.43  ? 395 LYS A C   1 
ATOM   3170  O  O   . LYS A  1 395 ? 99.657  55.313  48.239  1.00 40.74  ? 395 LYS A O   1 
ATOM   3171  C  CB  . LYS A  1 395 ? 97.773  53.179  49.994  1.00 28.56  ? 395 LYS A CB  1 
ATOM   3172  C  CG  . LYS A  1 395 ? 97.125  53.055  51.324  1.00 30.68  ? 395 LYS A CG  1 
ATOM   3173  C  CD  . LYS A  1 395 ? 98.053  53.654  52.339  1.00 44.40  ? 395 LYS A CD  1 
ATOM   3174  C  CE  . LYS A  1 395 ? 97.356  53.893  53.695  1.00 55.13  ? 395 LYS A CE  1 
ATOM   3175  N  NZ  . LYS A  1 395 ? 96.656  52.697  54.335  1.00 63.13  ? 395 LYS A NZ  1 
ATOM   3176  N  N   . ASN A  1 396 ? 98.370  53.840  47.169  1.00 43.32  ? 396 ASN A N   1 
ATOM   3177  C  CA  . ASN A  1 396 ? 99.260  53.617  46.046  1.00 45.12  ? 396 ASN A CA  1 
ATOM   3178  C  C   . ASN A  1 396 ? 98.529  53.853  44.760  1.00 43.36  ? 396 ASN A C   1 
ATOM   3179  O  O   . ASN A  1 396 ? 97.380  54.249  44.753  1.00 42.88  ? 396 ASN A O   1 
ATOM   3180  C  CB  . ASN A  1 396 ? 99.566  52.110  46.072  1.00 57.32  ? 396 ASN A CB  1 
ATOM   3181  C  CG  . ASN A  1 396 ? 100.848 51.780  46.768  1.00 69.46  ? 396 ASN A CG  1 
ATOM   3182  O  OD1 . ASN A  1 396 ? 101.880 52.069  46.167  1.00 82.97  ? 396 ASN A OD1 1 
ATOM   3183  N  ND2 . ASN A  1 396 ? 100.826 51.310  48.035  1.00 71.13  ? 396 ASN A ND2 1 
ATOM   3184  N  N   . ARG A  1 397 ? 99.192  53.520  43.665  1.00 43.23  ? 397 ARG A N   1 
ATOM   3185  C  CA  . ARG A  1 397 ? 98.561  53.572  42.358  1.00 43.72  ? 397 ARG A CA  1 
ATOM   3186  C  C   . ARG A  1 397 ? 97.808  52.222  42.213  1.00 42.23  ? 397 ARG A C   1 
ATOM   3187  O  O   . ARG A  1 397 ? 97.056  52.018  41.255  1.00 41.46  ? 397 ARG A O   1 
ATOM   3188  C  CB  . ARG A  1 397 ? 99.607  53.662  41.256  1.00 44.26  ? 397 ARG A CB  1 
ATOM   3189  C  CG  . ARG A  1 397 ? 100.139 52.307  40.822  1.00 47.00  ? 397 ARG A CG  1 
ATOM   3190  C  CD  . ARG A  1 397 ? 101.159 52.439  39.735  1.00 58.56  ? 397 ARG A CD  1 
ATOM   3191  N  NE  . ARG A  1 397 ? 102.358 53.145  40.180  1.00 63.48  ? 397 ARG A NE  1 
ATOM   3192  C  CZ  . ARG A  1 397 ? 103.393 53.435  39.395  1.00 66.83  ? 397 ARG A CZ  1 
ATOM   3193  N  NH1 . ARG A  1 397 ? 103.409 53.095  38.109  1.00 70.87  ? 397 ARG A NH1 1 
ATOM   3194  N  NH2 . ARG A  1 397 ? 104.438 54.045  39.905  1.00 71.07  ? 397 ARG A NH2 1 
ATOM   3195  N  N   . THR A  1 398 ? 98.112  51.277  43.111  1.00 39.06  ? 398 THR A N   1 
ATOM   3196  C  CA  . THR A  1 398 ? 97.505  49.942  43.129  1.00 34.68  ? 398 THR A CA  1 
ATOM   3197  C  C   . THR A  1 398 ? 96.607  49.700  44.326  1.00 31.55  ? 398 THR A C   1 
ATOM   3198  O  O   . THR A  1 398 ? 95.676  48.928  44.237  1.00 34.81  ? 398 THR A O   1 
ATOM   3199  C  CB  . THR A  1 398 ? 98.582  48.793  43.145  1.00 38.53  ? 398 THR A CB  1 
ATOM   3200  O  OG1 . THR A  1 398 ? 99.617  49.051  44.116  1.00 39.71  ? 398 THR A OG1 1 
ATOM   3201  C  CG2 . THR A  1 398 ? 99.192  48.633  41.798  1.00 40.67  ? 398 THR A CG2 1 
ATOM   3202  N  N   . HIS A  1 399 ? 96.864  50.370  45.437  1.00 30.79  ? 399 HIS A N   1 
ATOM   3203  C  CA  . HIS A  1 399 ? 96.074  50.154  46.638  1.00 30.94  ? 399 HIS A CA  1 
ATOM   3204  C  C   . HIS A  1 399 ? 95.310  51.345  47.205  1.00 32.26  ? 399 HIS A C   1 
ATOM   3205  O  O   . HIS A  1 399 ? 95.822  52.465  47.237  1.00 37.69  ? 399 HIS A O   1 
ATOM   3206  C  CB  . HIS A  1 399 ? 96.954  49.585  47.738  1.00 27.22  ? 399 HIS A CB  1 
ATOM   3207  C  CG  . HIS A  1 399 ? 97.500  48.237  47.420  1.00 27.66  ? 399 HIS A CG  1 
ATOM   3208  N  ND1 . HIS A  1 399 ? 97.075  47.099  48.063  1.00 27.10  ? 399 HIS A ND1 1 
ATOM   3209  C  CD2 . HIS A  1 399 ? 98.403  47.836  46.492  1.00 26.29  ? 399 HIS A CD2 1 
ATOM   3210  C  CE1 . HIS A  1 399 ? 97.684  46.047  47.542  1.00 27.31  ? 399 HIS A CE1 1 
ATOM   3211  N  NE2 . HIS A  1 399 ? 98.499  46.469  46.585  1.00 25.67  ? 399 HIS A NE2 1 
ATOM   3212  N  N   . ALA A  1 400 ? 94.081  51.076  47.639  1.00 28.86  ? 400 ALA A N   1 
ATOM   3213  C  CA  . ALA A  1 400 ? 93.215  52.056  48.274  1.00 25.75  ? 400 ALA A CA  1 
ATOM   3214  C  C   . ALA A  1 400 ? 92.422  51.235  49.284  1.00 25.15  ? 400 ALA A C   1 
ATOM   3215  O  O   . ALA A  1 400 ? 92.040  50.111  49.014  1.00 26.02  ? 400 ALA A O   1 
ATOM   3216  C  CB  . ALA A  1 400 ? 92.304  52.679  47.285  1.00 20.67  ? 400 ALA A CB  1 
ATOM   3217  N  N   . HIS A  1 401 ? 92.180  51.778  50.456  1.00 19.83  ? 401 HIS A N   1 
ATOM   3218  C  CA  . HIS A  1 401 ? 91.487  51.015  51.451  1.00 18.94  ? 401 HIS A CA  1 
ATOM   3219  C  C   . HIS A  1 401 ? 90.211  51.680  51.905  1.00 22.00  ? 401 HIS A C   1 
ATOM   3220  O  O   . HIS A  1 401 ? 90.251  52.778  52.429  1.00 30.30  ? 401 HIS A O   1 
ATOM   3221  C  CB  . HIS A  1 401 ? 92.434  50.853  52.622  1.00 20.60  ? 401 HIS A CB  1 
ATOM   3222  C  CG  . HIS A  1 401 ? 91.803  50.237  53.825  1.00 26.17  ? 401 HIS A CG  1 
ATOM   3223  N  ND1 . HIS A  1 401 ? 91.972  50.750  55.086  1.00 34.22  ? 401 HIS A ND1 1 
ATOM   3224  C  CD2 . HIS A  1 401 ? 91.023  49.137  53.966  1.00 31.55  ? 401 HIS A CD2 1 
ATOM   3225  C  CE1 . HIS A  1 401 ? 91.330  49.990  55.958  1.00 37.61  ? 401 HIS A CE1 1 
ATOM   3226  N  NE2 . HIS A  1 401 ? 90.744  49.006  55.302  1.00 30.51  ? 401 HIS A NE2 1 
ATOM   3227  N  N   . PHE A  1 402 ? 89.084  51.001  51.749  1.00 18.41  ? 402 PHE A N   1 
ATOM   3228  C  CA  . PHE A  1 402 ? 87.799  51.554  52.122  1.00 20.12  ? 402 PHE A CA  1 
ATOM   3229  C  C   . PHE A  1 402 ? 87.369  51.055  53.484  1.00 20.59  ? 402 PHE A C   1 
ATOM   3230  O  O   . PHE A  1 402 ? 87.535  49.909  53.775  1.00 26.75  ? 402 PHE A O   1 
ATOM   3231  C  CB  . PHE A  1 402 ? 86.762  51.178  51.075  1.00 18.61  ? 402 PHE A CB  1 
ATOM   3232  C  CG  . PHE A  1 402 ? 85.392  51.658  51.408  1.00 22.15  ? 402 PHE A CG  1 
ATOM   3233  C  CD1 . PHE A  1 402 ? 85.030  52.979  51.157  1.00 21.88  ? 402 PHE A CD1 1 
ATOM   3234  C  CD2 . PHE A  1 402 ? 84.487  50.829  52.051  1.00 22.81  ? 402 PHE A CD2 1 
ATOM   3235  C  CE1 . PHE A  1 402 ? 83.804  53.462  51.550  1.00 16.71  ? 402 PHE A CE1 1 
ATOM   3236  C  CE2 . PHE A  1 402 ? 83.232  51.311  52.454  1.00 26.57  ? 402 PHE A CE2 1 
ATOM   3237  C  CZ  . PHE A  1 402 ? 82.896  52.627  52.205  1.00 23.91  ? 402 PHE A CZ  1 
ATOM   3238  N  N   . SER A  1 403 ? 86.762  51.895  54.299  1.00 25.23  ? 403 SER A N   1 
ATOM   3239  C  CA  . SER A  1 403 ? 86.338  51.509  55.647  1.00 25.20  ? 403 SER A CA  1 
ATOM   3240  C  C   . SER A  1 403 ? 84.948  52.071  55.840  1.00 25.36  ? 403 SER A C   1 
ATOM   3241  O  O   . SER A  1 403 ? 84.576  53.011  55.164  1.00 32.24  ? 403 SER A O   1 
ATOM   3242  C  CB  . SER A  1 403 ? 87.242  52.175  56.670  1.00 25.08  ? 403 SER A CB  1 
ATOM   3243  O  OG  . SER A  1 403 ? 88.463  52.632  56.060  1.00 48.13  ? 403 SER A OG  1 
ATOM   3244  N  N   . TRP A  1 404 ? 84.170  51.495  56.737  1.00 25.53  ? 404 TRP A N   1 
ATOM   3245  C  CA  . TRP A  1 404 ? 82.814  51.962  57.015  1.00 24.72  ? 404 TRP A CA  1 
ATOM   3246  C  C   . TRP A  1 404 ? 82.748  51.989  58.521  1.00 25.36  ? 404 TRP A C   1 
ATOM   3247  O  O   . TRP A  1 404 ? 82.854  50.920  59.119  1.00 23.51  ? 404 TRP A O   1 
ATOM   3248  C  CB  . TRP A  1 404 ? 81.758  50.962  56.515  1.00 25.05  ? 404 TRP A CB  1 
ATOM   3249  C  CG  . TRP A  1 404 ? 80.349  51.363  56.899  1.00 27.18  ? 404 TRP A CG  1 
ATOM   3250  C  CD1 . TRP A  1 404 ? 79.769  52.579  56.671  1.00 29.05  ? 404 TRP A CD1 1 
ATOM   3251  C  CD2 . TRP A  1 404 ? 79.346  50.574  57.590  1.00 28.95  ? 404 TRP A CD2 1 
ATOM   3252  N  NE1 . TRP A  1 404 ? 78.484  52.601  57.160  1.00 29.43  ? 404 TRP A NE1 1 
ATOM   3253  C  CE2 . TRP A  1 404 ? 78.199  51.393  57.737  1.00 27.45  ? 404 TRP A CE2 1 
ATOM   3254  C  CE3 . TRP A  1 404 ? 79.306  49.272  58.094  1.00 29.17  ? 404 TRP A CE3 1 
ATOM   3255  C  CZ2 . TRP A  1 404 ? 77.029  50.952  58.366  1.00 26.91  ? 404 TRP A CZ2 1 
ATOM   3256  C  CZ3 . TRP A  1 404 ? 78.127  48.829  58.725  1.00 27.28  ? 404 TRP A CZ3 1 
ATOM   3257  C  CH2 . TRP A  1 404 ? 77.010  49.674  58.851  1.00 30.05  ? 404 TRP A CH2 1 
ATOM   3258  N  N   . ASN A  1 405 ? 82.562  53.169  59.126  1.00 24.77  ? 405 ASN A N   1 
ATOM   3259  C  CA  . ASN A  1 405 ? 82.492  53.286  60.583  1.00 29.65  ? 405 ASN A CA  1 
ATOM   3260  C  C   . ASN A  1 405 ? 81.073  53.471  61.098  1.00 27.94  ? 405 ASN A C   1 
ATOM   3261  O  O   . ASN A  1 405 ? 80.455  54.465  60.794  1.00 31.93  ? 405 ASN A O   1 
ATOM   3262  C  CB  . ASN A  1 405 ? 83.382  54.428  61.075  1.00 32.88  ? 405 ASN A CB  1 
ATOM   3263  C  CG  . ASN A  1 405 ? 83.115  54.790  62.530  1.00 33.71  ? 405 ASN A CG  1 
ATOM   3264  O  OD1 . ASN A  1 405 ? 82.342  55.710  62.824  1.00 33.61  ? 405 ASN A OD1 1 
ATOM   3265  N  ND2 . ASN A  1 405 ? 83.747  54.069  63.442  1.00 40.58  ? 405 ASN A ND2 1 
ATOM   3266  N  N   . ARG A  1 406 ? 80.562  52.533  61.900  1.00 30.21  ? 406 ARG A N   1 
ATOM   3267  C  CA  . ARG A  1 406 ? 79.190  52.656  62.377  1.00 26.14  ? 406 ARG A CA  1 
ATOM   3268  C  C   . ARG A  1 406 ? 79.131  53.649  63.444  1.00 31.36  ? 406 ARG A C   1 
ATOM   3269  O  O   . ARG A  1 406 ? 80.111  53.852  64.157  1.00 38.70  ? 406 ARG A O   1 
ATOM   3270  C  CB  . ARG A  1 406 ? 78.650  51.359  62.883  1.00 14.19  ? 406 ARG A CB  1 
ATOM   3271  C  CG  . ARG A  1 406 ? 78.580  50.372  61.780  1.00 27.10  ? 406 ARG A CG  1 
ATOM   3272  C  CD  . ARG A  1 406 ? 77.854  49.160  62.219  1.00 31.84  ? 406 ARG A CD  1 
ATOM   3273  N  NE  . ARG A  1 406 ? 78.406  48.703  63.484  1.00 36.51  ? 406 ARG A NE  1 
ATOM   3274  C  CZ  . ARG A  1 406 ? 77.795  47.851  64.291  1.00 40.14  ? 406 ARG A CZ  1 
ATOM   3275  N  NH1 . ARG A  1 406 ? 76.615  47.352  63.967  1.00 44.08  ? 406 ARG A NH1 1 
ATOM   3276  N  NH2 . ARG A  1 406 ? 78.332  47.551  65.456  1.00 49.07  ? 406 ARG A NH2 1 
ATOM   3277  N  N   . ASN A  1 407 ? 77.971  54.259  63.585  1.00 35.53  ? 407 ASN A N   1 
ATOM   3278  C  CA  . ASN A  1 407 ? 77.816  55.294  64.581  1.00 37.53  ? 407 ASN A CA  1 
ATOM   3279  C  C   . ASN A  1 407 ? 77.872  54.708  65.955  1.00 40.67  ? 407 ASN A C   1 
ATOM   3280  O  O   . ASN A  1 407 ? 78.366  55.359  66.881  1.00 43.16  ? 407 ASN A O   1 
ATOM   3281  C  CB  . ASN A  1 407 ? 76.515  56.077  64.365  1.00 41.20  ? 407 ASN A CB  1 
ATOM   3282  C  CG  . ASN A  1 407 ? 76.712  57.306  63.501  1.00 37.83  ? 407 ASN A CG  1 
ATOM   3283  O  OD1 . ASN A  1 407 ? 77.786  57.512  62.900  1.00 36.32  ? 407 ASN A OD1 1 
ATOM   3284  N  ND2 . ASN A  1 407 ? 75.700  58.151  63.467  1.00 34.65  ? 407 ASN A ND2 1 
ATOM   3285  N  N   . GLN A  1 408 ? 77.402  53.464  66.079  1.00 43.17  ? 408 GLN A N   1 
ATOM   3286  C  CA  . GLN A  1 408 ? 77.367  52.771  67.376  1.00 40.31  ? 408 GLN A CA  1 
ATOM   3287  C  C   . GLN A  1 408 ? 78.754  52.379  67.859  1.00 36.69  ? 408 GLN A C   1 
ATOM   3288  O  O   . GLN A  1 408 ? 78.948  52.147  69.037  1.00 40.30  ? 408 GLN A O   1 
ATOM   3289  C  CB  . GLN A  1 408 ? 76.553  51.482  67.310  1.00 39.53  ? 408 GLN A CB  1 
ATOM   3290  C  CG  . GLN A  1 408 ? 75.314  51.541  66.544  1.00 47.98  ? 408 GLN A CG  1 
ATOM   3291  C  CD  . GLN A  1 408 ? 75.532  51.134  65.124  1.00 54.55  ? 408 GLN A CD  1 
ATOM   3292  O  OE1 . GLN A  1 408 ? 75.891  51.945  64.260  1.00 58.79  ? 408 GLN A OE1 1 
ATOM   3293  N  NE2 . GLN A  1 408 ? 75.317  49.872  64.862  1.00 63.76  ? 408 GLN A NE2 1 
ATOM   3294  N  N   . ASP A  1 409 ? 79.680  52.203  66.930  1.00 30.83  ? 409 ASP A N   1 
ATOM   3295  C  CA  . ASP A  1 409 ? 80.999  51.794  67.290  1.00 32.07  ? 409 ASP A CA  1 
ATOM   3296  C  C   . ASP A  1 409 ? 81.745  53.006  67.738  1.00 33.30  ? 409 ASP A C   1 
ATOM   3297  O  O   . ASP A  1 409 ? 81.266  54.109  67.659  1.00 41.38  ? 409 ASP A O   1 
ATOM   3298  C  CB  . ASP A  1 409 ? 81.734  51.189  66.095  1.00 38.07  ? 409 ASP A CB  1 
ATOM   3299  C  CG  . ASP A  1 409 ? 80.982  50.039  65.447  1.00 40.88  ? 409 ASP A CG  1 
ATOM   3300  O  OD1 . ASP A  1 409 ? 80.185  49.383  66.160  1.00 24.73  ? 409 ASP A OD1 1 
ATOM   3301  O  OD2 . ASP A  1 409 ? 81.197  49.834  64.218  1.00 46.99  ? 409 ASP A OD2 1 
ATOM   3302  N  N   . GLY A  1 410 ? 82.932  52.794  68.249  1.00 33.05  ? 410 GLY A N   1 
ATOM   3303  C  CA  . GLY A  1 410 ? 83.718  53.918  68.671  1.00 34.51  ? 410 GLY A CA  1 
ATOM   3304  C  C   . GLY A  1 410 ? 84.317  54.439  67.404  1.00 32.08  ? 410 GLY A C   1 
ATOM   3305  O  O   . GLY A  1 410 ? 84.407  53.743  66.406  1.00 28.07  ? 410 GLY A O   1 
ATOM   3306  N  N   . VAL A  1 411 ? 84.821  55.649  67.499  1.00 35.34  ? 411 VAL A N   1 
ATOM   3307  C  CA  . VAL A  1 411 ? 85.415  56.358  66.396  1.00 31.70  ? 411 VAL A CA  1 
ATOM   3308  C  C   . VAL A  1 411 ? 86.412  55.587  65.570  1.00 28.89  ? 411 VAL A C   1 
ATOM   3309  O  O   . VAL A  1 411 ? 86.543  55.819  64.365  1.00 32.12  ? 411 VAL A O   1 
ATOM   3310  C  CB  . VAL A  1 411 ? 86.065  57.604  66.954  1.00 37.98  ? 411 VAL A CB  1 
ATOM   3311  C  CG1 . VAL A  1 411 ? 87.132  58.159  66.003  1.00 46.18  ? 411 VAL A CG1 1 
ATOM   3312  C  CG2 . VAL A  1 411 ? 85.002  58.616  67.272  1.00 38.49  ? 411 VAL A CG2 1 
ATOM   3313  N  N   . ALA A  1 412 ? 87.113  54.656  66.189  1.00 30.71  ? 412 ALA A N   1 
ATOM   3314  C  CA  . ALA A  1 412 ? 88.123  53.915  65.426  1.00 37.37  ? 412 ALA A CA  1 
ATOM   3315  C  C   . ALA A  1 412 ? 87.767  52.493  64.954  1.00 38.36  ? 412 ALA A C   1 
ATOM   3316  O  O   . ALA A  1 412 ? 88.592  51.804  64.335  1.00 38.15  ? 412 ALA A O   1 
ATOM   3317  C  CB  . ALA A  1 412 ? 89.402  53.893  66.188  1.00 40.25  ? 412 ALA A CB  1 
ATOM   3318  N  N   . VAL A  1 413 ? 86.526  52.093  65.185  1.00 35.31  ? 413 VAL A N   1 
ATOM   3319  C  CA  . VAL A  1 413 ? 86.070  50.782  64.809  1.00 33.81  ? 413 VAL A CA  1 
ATOM   3320  C  C   . VAL A  1 413 ? 85.497  50.661  63.411  1.00 33.94  ? 413 VAL A C   1 
ATOM   3321  O  O   . VAL A  1 413 ? 84.310  50.982  63.150  1.00 35.42  ? 413 VAL A O   1 
ATOM   3322  C  CB  . VAL A  1 413 ? 85.022  50.316  65.789  1.00 37.33  ? 413 VAL A CB  1 
ATOM   3323  C  CG1 . VAL A  1 413 ? 84.501  48.953  65.410  1.00 39.05  ? 413 VAL A CG1 1 
ATOM   3324  C  CG2 . VAL A  1 413 ? 85.602  50.321  67.167  1.00 46.00  ? 413 VAL A CG2 1 
ATOM   3325  N  N   . GLU A  1 414 ? 86.291  50.067  62.542  1.00 30.75  ? 414 GLU A N   1 
ATOM   3326  C  CA  . GLU A  1 414 ? 85.848  49.874  61.183  1.00 34.79  ? 414 GLU A CA  1 
ATOM   3327  C  C   . GLU A  1 414 ? 84.933  48.662  61.110  1.00 33.48  ? 414 GLU A C   1 
ATOM   3328  O  O   . GLU A  1 414 ? 85.420  47.562  61.058  1.00 39.56  ? 414 GLU A O   1 
ATOM   3329  C  CB  . GLU A  1 414 ? 87.028  49.628  60.255  1.00 32.52  ? 414 GLU A CB  1 
ATOM   3330  C  CG  . GLU A  1 414 ? 88.089  50.714  60.249  1.00 49.25  ? 414 GLU A CG  1 
ATOM   3331  C  CD  . GLU A  1 414 ? 89.299  50.371  59.338  1.00 59.76  ? 414 GLU A CD  1 
ATOM   3332  O  OE1 . GLU A  1 414 ? 89.220  49.378  58.583  1.00 66.09  ? 414 GLU A OE1 1 
ATOM   3333  O  OE2 . GLU A  1 414 ? 90.345  51.082  59.366  1.00 68.95  ? 414 GLU A OE2 1 
ATOM   3334  N  N   . ALA A  1 415 ? 83.618  48.846  61.125  1.00 30.02  ? 415 ALA A N   1 
ATOM   3335  C  CA  . ALA A  1 415 ? 82.688  47.721  61.012  1.00 23.02  ? 415 ALA A CA  1 
ATOM   3336  C  C   . ALA A  1 415 ? 82.732  47.024  59.638  1.00 25.15  ? 415 ALA A C   1 
ATOM   3337  O  O   . ALA A  1 415 ? 82.012  46.069  59.400  1.00 27.12  ? 415 ALA A O   1 
ATOM   3338  C  CB  . ALA A  1 415 ? 81.272  48.179  61.295  1.00 26.85  ? 415 ALA A CB  1 
ATOM   3339  N  N   . ASP A  1 416 ? 83.474  47.563  58.692  1.00 23.14  ? 416 ASP A N   1 
ATOM   3340  C  CA  . ASP A  1 416 ? 83.608  46.924  57.398  1.00 20.16  ? 416 ASP A CA  1 
ATOM   3341  C  C   . ASP A  1 416 ? 84.876  47.525  56.839  1.00 22.02  ? 416 ASP A C   1 
ATOM   3342  O  O   . ASP A  1 416 ? 85.154  48.695  57.055  1.00 26.09  ? 416 ASP A O   1 
ATOM   3343  C  CB  . ASP A  1 416 ? 82.470  47.246  56.487  1.00 28.41  ? 416 ASP A CB  1 
ATOM   3344  C  CG  . ASP A  1 416 ? 82.494  46.410  55.245  1.00 35.98  ? 416 ASP A CG  1 
ATOM   3345  O  OD1 . ASP A  1 416 ? 83.565  46.042  54.750  1.00 36.46  ? 416 ASP A OD1 1 
ATOM   3346  O  OD2 . ASP A  1 416 ? 81.410  46.099  54.753  1.00 43.54  ? 416 ASP A OD2 1 
ATOM   3347  N  N   . SER A  1 417 ? 85.636  46.738  56.107  1.00 19.48  ? 417 SER A N   1 
ATOM   3348  C  CA  . SER A  1 417 ? 86.916  47.172  55.610  1.00 24.94  ? 417 SER A CA  1 
ATOM   3349  C  C   . SER A  1 417 ? 87.244  46.339  54.385  1.00 23.40  ? 417 SER A C   1 
ATOM   3350  O  O   . SER A  1 417 ? 86.971  45.137  54.350  1.00 25.48  ? 417 SER A O   1 
ATOM   3351  C  CB  . SER A  1 417 ? 87.960  46.948  56.709  1.00 30.28  ? 417 SER A CB  1 
ATOM   3352  O  OG  . SER A  1 417 ? 89.257  46.752  56.152  1.00 46.50  ? 417 SER A OG  1 
ATOM   3353  N  N   . VAL A  1 418 ? 87.870  46.964  53.403  1.00 18.67  ? 418 VAL A N   1 
ATOM   3354  C  CA  . VAL A  1 418 ? 88.154  46.284  52.169  1.00 22.71  ? 418 VAL A CA  1 
ATOM   3355  C  C   . VAL A  1 418 ? 89.284  46.957  51.440  1.00 24.07  ? 418 VAL A C   1 
ATOM   3356  O  O   . VAL A  1 418 ? 89.412  48.160  51.505  1.00 26.55  ? 418 VAL A O   1 
ATOM   3357  C  CB  . VAL A  1 418 ? 86.955  46.412  51.251  1.00 25.57  ? 418 VAL A CB  1 
ATOM   3358  C  CG1 . VAL A  1 418 ? 87.273  45.795  49.935  1.00 32.47  ? 418 VAL A CG1 1 
ATOM   3359  C  CG2 . VAL A  1 418 ? 85.713  45.762  51.866  1.00 32.81  ? 418 VAL A CG2 1 
ATOM   3360  N  N   . TRP A  1 419 ? 90.121  46.193  50.766  1.00 25.88  ? 419 TRP A N   1 
ATOM   3361  C  CA  . TRP A  1 419 ? 91.201  46.798  50.043  1.00 28.34  ? 419 TRP A CA  1 
ATOM   3362  C  C   . TRP A  1 419 ? 90.759  46.752  48.620  1.00 34.21  ? 419 TRP A C   1 
ATOM   3363  O  O   . TRP A  1 419 ? 90.193  45.764  48.170  1.00 41.33  ? 419 TRP A O   1 
ATOM   3364  C  CB  . TRP A  1 419 ? 92.495  46.004  50.192  1.00 31.12  ? 419 TRP A CB  1 
ATOM   3365  C  CG  . TRP A  1 419 ? 93.243  46.366  51.396  1.00 32.97  ? 419 TRP A CG  1 
ATOM   3366  C  CD1 . TRP A  1 419 ? 93.140  45.797  52.621  1.00 38.20  ? 419 TRP A CD1 1 
ATOM   3367  C  CD2 . TRP A  1 419 ? 94.169  47.438  51.532  1.00 36.51  ? 419 TRP A CD2 1 
ATOM   3368  N  NE1 . TRP A  1 419 ? 93.935  46.453  53.526  1.00 36.88  ? 419 TRP A NE1 1 
ATOM   3369  C  CE2 . TRP A  1 419 ? 94.576  47.472  52.878  1.00 35.17  ? 419 TRP A CE2 1 
ATOM   3370  C  CE3 . TRP A  1 419 ? 94.690  48.386  50.649  1.00 39.94  ? 419 TRP A CE3 1 
ATOM   3371  C  CZ2 . TRP A  1 419 ? 95.469  48.419  53.359  1.00 32.47  ? 419 TRP A CZ2 1 
ATOM   3372  C  CZ3 . TRP A  1 419 ? 95.581  49.325  51.135  1.00 36.03  ? 419 TRP A CZ3 1 
ATOM   3373  C  CH2 . TRP A  1 419 ? 95.958  49.333  52.473  1.00 32.00  ? 419 TRP A CH2 1 
ATOM   3374  N  N   . PHE A  1 420 ? 91.021  47.827  47.910  1.00 36.11  ? 420 PHE A N   1 
ATOM   3375  C  CA  . PHE A  1 420 ? 90.665  47.924  46.531  1.00 35.68  ? 420 PHE A CA  1 
ATOM   3376  C  C   . PHE A  1 420 ? 91.934  47.747  45.746  1.00 35.48  ? 420 PHE A C   1 
ATOM   3377  O  O   . PHE A  1 420 ? 92.933  48.356  46.064  1.00 40.75  ? 420 PHE A O   1 
ATOM   3378  C  CB  . PHE A  1 420 ? 90.081  49.318  46.243  1.00 37.32  ? 420 PHE A CB  1 
ATOM   3379  C  CG  . PHE A  1 420 ? 88.600  49.433  46.523  1.00 36.71  ? 420 PHE A CG  1 
ATOM   3380  C  CD1 . PHE A  1 420 ? 88.129  49.551  47.815  1.00 34.60  ? 420 PHE A CD1 1 
ATOM   3381  C  CD2 . PHE A  1 420 ? 87.681  49.388  45.482  1.00 39.06  ? 420 PHE A CD2 1 
ATOM   3382  C  CE1 . PHE A  1 420 ? 86.781  49.611  48.075  1.00 31.89  ? 420 PHE A CE1 1 
ATOM   3383  C  CE2 . PHE A  1 420 ? 86.329  49.447  45.736  1.00 39.56  ? 420 PHE A CE2 1 
ATOM   3384  C  CZ  . PHE A  1 420 ? 85.879  49.554  47.045  1.00 37.76  ? 420 PHE A CZ  1 
ATOM   3385  N  N   . PHE A  1 421 ? 91.904  46.889  44.743  1.00 31.26  ? 421 PHE A N   1 
ATOM   3386  C  CA  . PHE A  1 421 ? 93.039  46.709  43.878  1.00 29.68  ? 421 PHE A CA  1 
ATOM   3387  C  C   . PHE A  1 421 ? 92.650  47.429  42.639  1.00 30.89  ? 421 PHE A C   1 
ATOM   3388  O  O   . PHE A  1 421 ? 91.552  47.191  42.120  1.00 36.29  ? 421 PHE A O   1 
ATOM   3389  C  CB  . PHE A  1 421 ? 93.243  45.257  43.617  1.00 34.83  ? 421 PHE A CB  1 
ATOM   3390  C  CG  . PHE A  1 421 ? 93.659  44.533  44.827  1.00 40.61  ? 421 PHE A CG  1 
ATOM   3391  C  CD1 . PHE A  1 421 ? 94.506  45.152  45.749  1.00 38.56  ? 421 PHE A CD1 1 
ATOM   3392  C  CD2 . PHE A  1 421 ? 93.188  43.268  45.098  1.00 40.85  ? 421 PHE A CD2 1 
ATOM   3393  C  CE1 . PHE A  1 421 ? 94.871  44.512  46.922  1.00 32.39  ? 421 PHE A CE1 1 
ATOM   3394  C  CE2 . PHE A  1 421 ? 93.549  42.632  46.274  1.00 38.57  ? 421 PHE A CE2 1 
ATOM   3395  C  CZ  . PHE A  1 421 ? 94.392  43.260  47.183  1.00 35.10  ? 421 PHE A CZ  1 
ATOM   3396  N  N   . ASN A  1 422 ? 93.508  48.361  42.214  1.00 30.85  ? 422 ASN A N   1 
ATOM   3397  C  CA  . ASN A  1 422 ? 93.263  49.233  41.040  1.00 30.54  ? 422 ASN A CA  1 
ATOM   3398  C  C   . ASN A  1 422 ? 92.925  48.556  39.725  1.00 29.36  ? 422 ASN A C   1 
ATOM   3399  O  O   . ASN A  1 422 ? 93.787  47.928  39.131  1.00 34.13  ? 422 ASN A O   1 
ATOM   3400  C  CB  . ASN A  1 422 ? 94.427  50.165  40.831  1.00 28.42  ? 422 ASN A CB  1 
ATOM   3401  C  CG  . ASN A  1 422 ? 94.157  51.148  39.767  1.00 33.90  ? 422 ASN A CG  1 
ATOM   3402  O  OD1 . ASN A  1 422 ? 94.268  50.828  38.586  1.00 37.28  ? 422 ASN A OD1 1 
ATOM   3403  N  ND2 . ASN A  1 422 ? 93.754  52.364  40.159  1.00 38.90  ? 422 ASN A ND2 1 
ATOM   3404  N  N   . ARG A  1 423 ? 91.694  48.733  39.236  1.00 31.92  ? 423 ARG A N   1 
ATOM   3405  C  CA  . ARG A  1 423 ? 91.250  48.070  37.994  1.00 31.39  ? 423 ARG A CA  1 
ATOM   3406  C  C   . ARG A  1 423 ? 92.184  48.310  36.837  1.00 33.43  ? 423 ARG A C   1 
ATOM   3407  O  O   . ARG A  1 423 ? 92.075  47.613  35.834  1.00 39.88  ? 423 ARG A O   1 
ATOM   3408  C  CB  . ARG A  1 423 ? 89.828  48.461  37.557  1.00 27.44  ? 423 ARG A CB  1 
ATOM   3409  C  CG  . ARG A  1 423 ? 88.710  47.976  38.431  1.00 29.32  ? 423 ARG A CG  1 
ATOM   3410  C  CD  . ARG A  1 423 ? 88.728  46.505  38.596  1.00 22.82  ? 423 ARG A CD  1 
ATOM   3411  N  NE  . ARG A  1 423 ? 89.627  46.115  39.655  1.00 29.12  ? 423 ARG A NE  1 
ATOM   3412  C  CZ  . ARG A  1 423 ? 89.767  44.866  40.072  1.00 32.71  ? 423 ARG A CZ  1 
ATOM   3413  N  NH1 . ARG A  1 423 ? 89.056  43.902  39.501  1.00 29.50  ? 423 ARG A NH1 1 
ATOM   3414  N  NH2 . ARG A  1 423 ? 90.608  44.580  41.067  1.00 34.48  ? 423 ARG A NH2 1 
ATOM   3415  N  N   . HIS A  1 424 ? 93.035  49.331  36.926  1.00 28.50  ? 424 HIS A N   1 
ATOM   3416  C  CA  . HIS A  1 424 ? 93.961  49.574  35.858  1.00 30.31  ? 424 HIS A CA  1 
ATOM   3417  C  C   . HIS A  1 424 ? 95.414  49.173  36.125  1.00 36.19  ? 424 HIS A C   1 
ATOM   3418  O  O   . HIS A  1 424 ? 96.133  48.884  35.176  1.00 39.46  ? 424 HIS A O   1 
ATOM   3419  C  CB  . HIS A  1 424 ? 93.940  51.024  35.447  1.00 31.80  ? 424 HIS A CB  1 
ATOM   3420  C  CG  . HIS A  1 424 ? 94.823  51.320  34.263  1.00 39.15  ? 424 HIS A CG  1 
ATOM   3421  N  ND1 . HIS A  1 424 ? 94.321  51.550  32.997  1.00 43.57  ? 424 HIS A ND1 1 
ATOM   3422  C  CD2 . HIS A  1 424 ? 96.172  51.454  34.163  1.00 35.95  ? 424 HIS A CD2 1 
ATOM   3423  C  CE1 . HIS A  1 424 ? 95.321  51.824  32.173  1.00 42.42  ? 424 HIS A CE1 1 
ATOM   3424  N  NE2 . HIS A  1 424 ? 96.454  51.769  32.855  1.00 35.85  ? 424 HIS A NE2 1 
ATOM   3425  N  N   . TRP A  1 425 ? 95.869  49.188  37.381  1.00 37.23  ? 425 TRP A N   1 
ATOM   3426  C  CA  . TRP A  1 425 ? 97.260  48.869  37.691  1.00 32.36  ? 425 TRP A CA  1 
ATOM   3427  C  C   . TRP A  1 425 ? 97.495  47.571  38.401  1.00 34.18  ? 425 TRP A C   1 
ATOM   3428  O  O   . TRP A  1 425 ? 98.601  47.030  38.389  1.00 39.08  ? 425 TRP A O   1 
ATOM   3429  C  CB  . TRP A  1 425 ? 97.855  49.958  38.547  1.00 31.99  ? 425 TRP A CB  1 
ATOM   3430  C  CG  . TRP A  1 425 ? 97.971  51.218  37.836  1.00 31.30  ? 425 TRP A CG  1 
ATOM   3431  C  CD1 . TRP A  1 425 ? 97.074  52.240  37.828  1.00 30.21  ? 425 TRP A CD1 1 
ATOM   3432  C  CD2 . TRP A  1 425 ? 99.029  51.593  36.947  1.00 32.97  ? 425 TRP A CD2 1 
ATOM   3433  N  NE1 . TRP A  1 425 ? 97.506  53.233  36.978  1.00 28.32  ? 425 TRP A NE1 1 
ATOM   3434  C  CE2 . TRP A  1 425 ? 98.697  52.858  36.417  1.00 30.74  ? 425 TRP A CE2 1 
ATOM   3435  C  CE3 . TRP A  1 425 ? 100.231 50.977  36.541  1.00 32.04  ? 425 TRP A CE3 1 
ATOM   3436  C  CZ2 . TRP A  1 425 ? 99.521  53.519  35.486  1.00 35.27  ? 425 TRP A CZ2 1 
ATOM   3437  C  CZ3 . TRP A  1 425 ? 101.055 51.635  35.621  1.00 27.52  ? 425 TRP A CZ3 1 
ATOM   3438  C  CH2 . TRP A  1 425 ? 100.692 52.888  35.101  1.00 34.00  ? 425 TRP A CH2 1 
ATOM   3439  N  N   . TYR A  1 426 ? 96.445  47.009  38.948  1.00 29.50  ? 426 TYR A N   1 
ATOM   3440  C  CA  . TYR A  1 426 ? 96.616  45.804  39.706  1.00 27.48  ? 426 TYR A CA  1 
ATOM   3441  C  C   . TYR A  1 426 ? 95.264  45.154  39.819  1.00 26.78  ? 426 TYR A C   1 
ATOM   3442  O  O   . TYR A  1 426 ? 94.791  44.896  40.929  1.00 28.54  ? 426 TYR A O   1 
ATOM   3443  C  CB  . TYR A  1 426 ? 97.078  46.225  41.075  1.00 30.04  ? 426 TYR A CB  1 
ATOM   3444  C  CG  . TYR A  1 426 ? 97.540  45.128  41.924  1.00 31.54  ? 426 TYR A CG  1 
ATOM   3445  C  CD1 . TYR A  1 426 ? 98.731  44.481  41.625  1.00 33.91  ? 426 TYR A CD1 1 
ATOM   3446  C  CD2 . TYR A  1 426 ? 96.810  44.730  43.011  1.00 28.47  ? 426 TYR A CD2 1 
ATOM   3447  C  CE1 . TYR A  1 426 ? 99.194  43.464  42.384  1.00 36.55  ? 426 TYR A CE1 1 
ATOM   3448  C  CE2 . TYR A  1 426 ? 97.255  43.704  43.783  1.00 38.32  ? 426 TYR A CE2 1 
ATOM   3449  C  CZ  . TYR A  1 426 ? 98.461  43.066  43.463  1.00 37.54  ? 426 TYR A CZ  1 
ATOM   3450  O  OH  . TYR A  1 426 ? 98.945  42.025  44.227  1.00 42.75  ? 426 TYR A OH  1 
ATOM   3451  N  N   . PRO A  1 427 ? 94.658  44.825  38.670  1.00 24.31  ? 427 PRO A N   1 
ATOM   3452  C  CA  . PRO A  1 427 ? 93.354  44.205  38.462  1.00 26.93  ? 427 PRO A CA  1 
ATOM   3453  C  C   . PRO A  1 427 ? 93.220  42.777  38.928  1.00 30.08  ? 427 PRO A C   1 
ATOM   3454  O  O   . PRO A  1 427 ? 92.707  41.891  38.211  1.00 35.22  ? 427 PRO A O   1 
ATOM   3455  C  CB  . PRO A  1 427 ? 93.157  44.360  36.962  1.00 24.77  ? 427 PRO A CB  1 
ATOM   3456  C  CG  . PRO A  1 427 ? 94.496  44.189  36.454  1.00 31.30  ? 427 PRO A CG  1 
ATOM   3457  C  CD  . PRO A  1 427 ? 95.313  45.046  37.378  1.00 25.48  ? 427 PRO A CD  1 
ATOM   3458  N  N   . VAL A  1 428 ? 93.546  42.579  40.193  1.00 33.34  ? 428 VAL A N   1 
ATOM   3459  C  CA  . VAL A  1 428 ? 93.501  41.254  40.772  1.00 38.10  ? 428 VAL A CA  1 
ATOM   3460  C  C   . VAL A  1 428 ? 92.256  41.130  41.598  1.00 40.44  ? 428 VAL A C   1 
ATOM   3461  O  O   . VAL A  1 428 ? 91.782  42.113  42.147  1.00 42.75  ? 428 VAL A O   1 
ATOM   3462  C  CB  . VAL A  1 428 ? 94.732  41.013  41.632  1.00 36.41  ? 428 VAL A CB  1 
ATOM   3463  C  CG1 . VAL A  1 428 ? 94.750  39.585  42.022  1.00 45.93  ? 428 VAL A CG1 1 
ATOM   3464  C  CG2 . VAL A  1 428 ? 96.018  41.362  40.858  1.00 37.52  ? 428 VAL A CG2 1 
ATOM   3465  N  N   . ASP A  1 429 ? 91.742  39.920  41.739  1.00 46.07  ? 429 ASP A N   1 
ATOM   3466  C  CA  . ASP A  1 429 ? 90.511  39.766  42.490  1.00 51.68  ? 429 ASP A CA  1 
ATOM   3467  C  C   . ASP A  1 429 ? 90.562  40.334  43.900  1.00 56.79  ? 429 ASP A C   1 
ATOM   3468  O  O   . ASP A  1 429 ? 91.217  39.768  44.778  1.00 55.55  ? 429 ASP A O   1 
ATOM   3469  C  CB  . ASP A  1 429 ? 90.045  38.309  42.514  1.00 55.19  ? 429 ASP A CB  1 
ATOM   3470  C  CG  . ASP A  1 429 ? 88.602  38.151  43.039  1.00 66.02  ? 429 ASP A CG  1 
ATOM   3471  O  OD1 . ASP A  1 429 ? 88.360  38.414  44.243  1.00 72.49  ? 429 ASP A OD1 1 
ATOM   3472  O  OD2 . ASP A  1 429 ? 87.698  37.737  42.262  1.00 73.84  ? 429 ASP A OD2 1 
ATOM   3473  N  N   . ASP A  1 430 ? 89.959  41.514  44.079  1.00 64.47  ? 430 ASP A N   1 
ATOM   3474  C  CA  . ASP A  1 430 ? 89.855  42.129  45.409  1.00 70.79  ? 430 ASP A CA  1 
ATOM   3475  C  C   . ASP A  1 430 ? 88.562  41.686  46.106  1.00 78.43  ? 430 ASP A C   1 
ATOM   3476  O  O   . ASP A  1 430 ? 88.415  41.876  47.314  1.00 79.48  ? 430 ASP A O   1 
ATOM   3477  C  CB  . ASP A  1 430 ? 89.972  43.675  45.386  1.00 64.96  ? 430 ASP A CB  1 
ATOM   3478  C  CG  . ASP A  1 430 ? 89.175  44.327  44.293  1.00 57.85  ? 430 ASP A CG  1 
ATOM   3479  O  OD1 . ASP A  1 430 ? 88.246  43.709  43.760  1.00 63.30  ? 430 ASP A OD1 1 
ATOM   3480  O  OD2 . ASP A  1 430 ? 89.481  45.478  43.963  1.00 52.77  ? 430 ASP A OD2 1 
ATOM   3481  N  N   . SER A  1 431 ? 87.665  41.049  45.339  1.00 88.01  ? 431 SER A N   1 
ATOM   3482  C  CA  . SER A  1 431 ? 86.360  40.547  45.812  1.00 94.32  ? 431 SER A CA  1 
ATOM   3483  C  C   . SER A  1 431 ? 86.457  39.412  46.833  1.00 97.76  ? 431 SER A C   1 
ATOM   3484  O  O   . SER A  1 431 ? 87.164  38.434  46.597  1.00 98.01  ? 431 SER A O   1 
ATOM   3485  C  CB  . SER A  1 431 ? 85.494  40.096  44.618  1.00 94.17  ? 431 SER A CB  1 
ATOM   3486  O  OG  . SER A  1 431 ? 84.906  41.210  43.956  1.00 91.16  ? 431 SER A OG  1 
ATOM   3487  N  N   . THR A  1 432 ? 85.679  39.527  47.916  1.00 103.28 ? 432 THR A N   1 
ATOM   3488  C  CA  . THR A  1 432 ? 85.639  38.555  49.030  1.00 108.81 ? 432 THR A CA  1 
ATOM   3489  C  C   . THR A  1 432 ? 84.932  37.176  48.765  1.00 113.44 ? 432 THR A C   1 
ATOM   3490  O  O   . THR A  1 432 ? 85.566  36.265  48.151  1.00 115.27 ? 432 THR A O   1 
ATOM   3491  C  CB  . THR A  1 432 ? 85.043  39.244  50.325  1.00 106.78 ? 432 THR A CB  1 
ATOM   3492  O  OG1 . THR A  1 432 ? 83.685  39.671  50.093  1.00 107.37 ? 432 THR A OG1 1 
ATOM   3493  C  CG2 . THR A  1 432 ? 85.879  40.458  50.716  1.00 101.13 ? 432 THR A CG2 1 
ATOM   3494  O  OXT . THR A  1 432 ? 83.757  36.997  49.194  1.00 115.96 ? 432 THR A OXT 1 
ATOM   3495  N  N   . ARG B  1 9   ? 4.937   24.274  58.926  1.00 81.15  ? 9   ARG B N   1 
ATOM   3496  C  CA  . ARG B  1 9   ? 4.867   24.623  57.460  1.00 77.11  ? 9   ARG B CA  1 
ATOM   3497  C  C   . ARG B  1 9   ? 5.491   23.548  56.533  1.00 70.26  ? 9   ARG B C   1 
ATOM   3498  O  O   . ARG B  1 9   ? 5.346   23.597  55.298  1.00 63.62  ? 9   ARG B O   1 
ATOM   3499  C  CB  . ARG B  1 9   ? 5.539   25.980  57.216  1.00 83.63  ? 9   ARG B CB  1 
ATOM   3500  C  CG  . ARG B  1 9   ? 5.425   26.507  55.780  1.00 91.93  ? 9   ARG B CG  1 
ATOM   3501  C  CD  . ARG B  1 9   ? 4.100   27.233  55.515  1.00 100.84 ? 9   ARG B CD  1 
ATOM   3502  N  NE  . ARG B  1 9   ? 3.775   27.261  54.084  1.00 108.76 ? 9   ARG B NE  1 
ATOM   3503  C  CZ  . ARG B  1 9   ? 2.544   27.149  53.572  1.00 112.57 ? 9   ARG B CZ  1 
ATOM   3504  N  NH1 . ARG B  1 9   ? 1.471   27.011  54.368  1.00 113.96 ? 9   ARG B NH1 1 
ATOM   3505  N  NH2 . ARG B  1 9   ? 2.396   27.117  52.248  1.00 112.24 ? 9   ARG B NH2 1 
ATOM   3506  N  N   . ASP B  1 10  ? 6.213   22.608  57.147  1.00 65.96  ? 10  ASP B N   1 
ATOM   3507  C  CA  . ASP B  1 10  ? 6.870   21.514  56.435  1.00 62.10  ? 10  ASP B CA  1 
ATOM   3508  C  C   . ASP B  1 10  ? 5.778   20.516  56.036  1.00 54.40  ? 10  ASP B C   1 
ATOM   3509  O  O   . ASP B  1 10  ? 4.921   20.185  56.847  1.00 52.84  ? 10  ASP B O   1 
ATOM   3510  C  CB  . ASP B  1 10  ? 7.887   20.804  57.368  1.00 68.70  ? 10  ASP B CB  1 
ATOM   3511  C  CG  . ASP B  1 10  ? 9.350   21.249  57.159  1.00 75.31  ? 10  ASP B CG  1 
ATOM   3512  O  OD1 . ASP B  1 10  ? 9.773   21.482  56.003  1.00 83.31  ? 10  ASP B OD1 1 
ATOM   3513  O  OD2 . ASP B  1 10  ? 10.105  21.318  58.163  1.00 80.01  ? 10  ASP B OD2 1 
ATOM   3514  N  N   . MET B  1 11  ? 5.854   19.989  54.821  1.00 50.98  ? 11  MET B N   1 
ATOM   3515  C  CA  . MET B  1 11  ? 4.870   19.033  54.359  1.00 50.34  ? 11  MET B CA  1 
ATOM   3516  C  C   . MET B  1 11  ? 4.814   17.935  55.400  1.00 55.07  ? 11  MET B C   1 
ATOM   3517  O  O   . MET B  1 11  ? 5.830   17.511  55.952  1.00 54.06  ? 11  MET B O   1 
ATOM   3518  C  CB  . MET B  1 11  ? 5.236   18.437  53.002  1.00 44.45  ? 11  MET B CB  1 
ATOM   3519  C  CG  . MET B  1 11  ? 5.604   19.431  51.959  1.00 41.48  ? 11  MET B CG  1 
ATOM   3520  S  SD  . MET B  1 11  ? 5.755   18.574  50.412  1.00 46.46  ? 11  MET B SD  1 
ATOM   3521  C  CE  . MET B  1 11  ? 7.494   18.485  50.240  1.00 50.61  ? 11  MET B CE  1 
ATOM   3522  N  N   . PRO B  1 12  ? 3.602   17.517  55.738  1.00 59.91  ? 12  PRO B N   1 
ATOM   3523  C  CA  . PRO B  1 12  ? 3.338   16.472  56.715  1.00 63.00  ? 12  PRO B CA  1 
ATOM   3524  C  C   . PRO B  1 12  ? 3.815   15.110  56.200  1.00 63.67  ? 12  PRO B C   1 
ATOM   3525  O  O   . PRO B  1 12  ? 3.858   14.876  54.979  1.00 59.80  ? 12  PRO B O   1 
ATOM   3526  C  CB  . PRO B  1 12  ? 1.829   16.534  56.837  1.00 65.20  ? 12  PRO B CB  1 
ATOM   3527  C  CG  . PRO B  1 12  ? 1.411   16.934  55.439  1.00 64.35  ? 12  PRO B CG  1 
ATOM   3528  C  CD  . PRO B  1 12  ? 2.346   18.044  55.182  1.00 61.36  ? 12  PRO B CD  1 
ATOM   3529  N  N   . LEU B  1 13  ? 4.117   14.210  57.143  1.00 62.94  ? 13  LEU B N   1 
ATOM   3530  C  CA  . LEU B  1 13  ? 4.613   12.869  56.831  1.00 62.59  ? 13  LEU B CA  1 
ATOM   3531  C  C   . LEU B  1 13  ? 3.834   12.059  55.807  1.00 63.36  ? 13  LEU B C   1 
ATOM   3532  O  O   . LEU B  1 13  ? 4.395   11.201  55.099  1.00 62.20  ? 13  LEU B O   1 
ATOM   3533  C  CB  . LEU B  1 13  ? 4.760   12.069  58.109  1.00 62.54  ? 13  LEU B CB  1 
ATOM   3534  C  CG  . LEU B  1 13  ? 5.913   12.532  58.995  1.00 63.04  ? 13  LEU B CG  1 
ATOM   3535  C  CD1 . LEU B  1 13  ? 6.046   11.612  60.177  1.00 59.65  ? 13  LEU B CD1 1 
ATOM   3536  C  CD2 . LEU B  1 13  ? 7.220   12.517  58.204  1.00 68.14  ? 13  LEU B CD2 1 
ATOM   3537  N  N   . ASP B  1 14  ? 2.534   12.327  55.735  1.00 68.60  ? 14  ASP B N   1 
ATOM   3538  C  CA  . ASP B  1 14  ? 1.668   11.617  54.792  1.00 72.07  ? 14  ASP B CA  1 
ATOM   3539  C  C   . ASP B  1 14  ? 1.706   12.127  53.359  1.00 70.16  ? 14  ASP B C   1 
ATOM   3540  O  O   . ASP B  1 14  ? 1.356   11.382  52.430  1.00 69.08  ? 14  ASP B O   1 
ATOM   3541  C  CB  . ASP B  1 14  ? 0.195   11.443  55.307  1.00 77.55  ? 14  ASP B CB  1 
ATOM   3542  C  CG  . ASP B  1 14  ? -0.422  12.718  55.937  1.00 84.26  ? 14  ASP B CG  1 
ATOM   3543  O  OD1 . ASP B  1 14  ? -0.149  13.031  57.127  1.00 88.62  ? 14  ASP B OD1 1 
ATOM   3544  O  OD2 . ASP B  1 14  ? -1.271  13.361  55.273  1.00 90.96  ? 14  ASP B OD2 1 
ATOM   3545  N  N   . SER B  1 15  ? 2.208   13.355  53.185  1.00 66.17  ? 15  SER B N   1 
ATOM   3546  C  CA  . SER B  1 15  ? 2.282   13.991  51.884  1.00 60.12  ? 15  SER B CA  1 
ATOM   3547  C  C   . SER B  1 15  ? 2.649   13.000  50.830  1.00 55.32  ? 15  SER B C   1 
ATOM   3548  O  O   . SER B  1 15  ? 3.518   12.153  51.001  1.00 55.56  ? 15  SER B O   1 
ATOM   3549  C  CB  . SER B  1 15  ? 3.255   15.141  51.922  1.00 63.10  ? 15  SER B CB  1 
ATOM   3550  O  OG  . SER B  1 15  ? 2.906   15.992  53.000  1.00 61.88  ? 15  SER B OG  1 
ATOM   3551  N  N   . ASP B  1 16  ? 1.850   13.021  49.794  1.00 53.38  ? 16  ASP B N   1 
ATOM   3552  C  CA  . ASP B  1 16  ? 2.014   12.116  48.679  1.00 55.34  ? 16  ASP B CA  1 
ATOM   3553  C  C   . ASP B  1 16  ? 3.434   12.065  48.237  1.00 52.46  ? 16  ASP B C   1 
ATOM   3554  O  O   . ASP B  1 16  ? 3.884   11.114  47.612  1.00 50.88  ? 16  ASP B O   1 
ATOM   3555  C  CB  . ASP B  1 16  ? 1.187   12.632  47.512  1.00 61.34  ? 16  ASP B CB  1 
ATOM   3556  C  CG  . ASP B  1 16  ? 1.328   14.124  47.334  1.00 67.08  ? 16  ASP B CG  1 
ATOM   3557  O  OD1 . ASP B  1 16  ? 0.842   14.873  48.222  1.00 72.41  ? 16  ASP B OD1 1 
ATOM   3558  O  OD2 . ASP B  1 16  ? 1.945   14.530  46.328  1.00 64.11  ? 16  ASP B OD2 1 
ATOM   3559  N  N   . VAL B  1 17  ? 4.106   13.171  48.483  1.00 54.24  ? 17  VAL B N   1 
ATOM   3560  C  CA  . VAL B  1 17  ? 5.470   13.317  48.065  1.00 54.63  ? 17  VAL B CA  1 
ATOM   3561  C  C   . VAL B  1 17  ? 6.402   12.369  48.819  1.00 56.18  ? 17  VAL B C   1 
ATOM   3562  O  O   . VAL B  1 17  ? 7.342   11.830  48.248  1.00 56.80  ? 17  VAL B O   1 
ATOM   3563  C  CB  . VAL B  1 17  ? 5.835   14.811  48.125  1.00 51.92  ? 17  VAL B CB  1 
ATOM   3564  C  CG1 . VAL B  1 17  ? 6.257   15.236  49.512  1.00 49.73  ? 17  VAL B CG1 1 
ATOM   3565  C  CG2 . VAL B  1 17  ? 6.807   15.138  47.043  1.00 52.77  ? 17  VAL B CG2 1 
ATOM   3566  N  N   . PHE B  1 18  ? 6.027   12.041  50.046  1.00 57.05  ? 18  PHE B N   1 
ATOM   3567  C  CA  . PHE B  1 18  ? 6.798   11.136  50.890  1.00 56.27  ? 18  PHE B CA  1 
ATOM   3568  C  C   . PHE B  1 18  ? 6.418   9.652   50.842  1.00 60.10  ? 18  PHE B C   1 
ATOM   3569  O  O   . PHE B  1 18  ? 6.964   8.866   51.608  1.00 60.59  ? 18  PHE B O   1 
ATOM   3570  C  CB  . PHE B  1 18  ? 6.698   11.589  52.322  1.00 50.25  ? 18  PHE B CB  1 
ATOM   3571  C  CG  . PHE B  1 18  ? 7.098   13.009  52.532  1.00 47.02  ? 18  PHE B CG  1 
ATOM   3572  C  CD1 . PHE B  1 18  ? 8.196   13.547  51.876  1.00 47.73  ? 18  PHE B CD1 1 
ATOM   3573  C  CD2 . PHE B  1 18  ? 6.448   13.772  53.484  1.00 47.39  ? 18  PHE B CD2 1 
ATOM   3574  C  CE1 . PHE B  1 18  ? 8.655   14.826  52.180  1.00 49.73  ? 18  PHE B CE1 1 
ATOM   3575  C  CE2 . PHE B  1 18  ? 6.889   15.049  53.806  1.00 46.10  ? 18  PHE B CE2 1 
ATOM   3576  C  CZ  . PHE B  1 18  ? 8.002   15.579  53.154  1.00 49.34  ? 18  PHE B CZ  1 
ATOM   3577  N  N   . ARG B  1 19  ? 5.474   9.266   49.989  1.00 64.90  ? 19  ARG B N   1 
ATOM   3578  C  CA  . ARG B  1 19  ? 5.080   7.859   49.885  1.00 67.48  ? 19  ARG B CA  1 
ATOM   3579  C  C   . ARG B  1 19  ? 6.242   6.925   49.543  1.00 62.19  ? 19  ARG B C   1 
ATOM   3580  O  O   . ARG B  1 19  ? 7.090   7.247   48.724  1.00 62.05  ? 19  ARG B O   1 
ATOM   3581  C  CB  . ARG B  1 19  ? 3.948   7.680   48.871  1.00 77.99  ? 19  ARG B CB  1 
ATOM   3582  C  CG  . ARG B  1 19  ? 2.617   8.104   49.449  1.00 92.92  ? 19  ARG B CG  1 
ATOM   3583  C  CD  . ARG B  1 19  ? 1.518   8.247   48.390  1.00 106.19 ? 19  ARG B CD  1 
ATOM   3584  N  NE  . ARG B  1 19  ? 0.300   8.822   48.988  1.00 117.46 ? 19  ARG B NE  1 
ATOM   3585  C  CZ  . ARG B  1 19  ? -0.744  9.303   48.306  1.00 123.98 ? 19  ARG B CZ  1 
ATOM   3586  N  NH1 . ARG B  1 19  ? -0.749  9.294   46.969  1.00 128.32 ? 19  ARG B NH1 1 
ATOM   3587  N  NH2 . ARG B  1 19  ? -1.786  9.815   48.972  1.00 126.78 ? 19  ARG B NH2 1 
ATOM   3588  N  N   . VAL B  1 20  ? 6.252   5.746   50.156  1.00 57.43  ? 20  VAL B N   1 
ATOM   3589  C  CA  . VAL B  1 20  ? 7.309   4.791   49.919  1.00 52.98  ? 20  VAL B CA  1 
ATOM   3590  C  C   . VAL B  1 20  ? 6.940   3.820   48.853  1.00 50.17  ? 20  VAL B C   1 
ATOM   3591  O  O   . VAL B  1 20  ? 5.879   3.193   48.879  1.00 51.26  ? 20  VAL B O   1 
ATOM   3592  C  CB  . VAL B  1 20  ? 7.747   4.046   51.201  1.00 54.71  ? 20  VAL B CB  1 
ATOM   3593  C  CG1 . VAL B  1 20  ? 6.638   4.024   52.182  1.00 57.54  ? 20  VAL B CG1 1 
ATOM   3594  C  CG2 . VAL B  1 20  ? 8.240   2.627   50.891  1.00 56.11  ? 20  VAL B CG2 1 
ATOM   3595  N  N   . PRO B  1 21  ? 7.827   3.682   47.879  1.00 49.12  ? 21  PRO B N   1 
ATOM   3596  C  CA  . PRO B  1 21  ? 7.619   2.771   46.762  1.00 52.55  ? 21  PRO B CA  1 
ATOM   3597  C  C   . PRO B  1 21  ? 7.229   1.422   47.314  1.00 58.66  ? 21  PRO B C   1 
ATOM   3598  O  O   . PRO B  1 21  ? 7.765   0.958   48.321  1.00 65.27  ? 21  PRO B O   1 
ATOM   3599  C  CB  . PRO B  1 21  ? 8.973   2.761   46.057  1.00 49.04  ? 21  PRO B CB  1 
ATOM   3600  C  CG  . PRO B  1 21  ? 9.927   3.234   47.113  1.00 51.44  ? 21  PRO B CG  1 
ATOM   3601  C  CD  . PRO B  1 21  ? 9.163   4.282   47.839  1.00 47.57  ? 21  PRO B CD  1 
ATOM   3602  N  N   . PRO B  1 22  ? 6.207   0.824   46.728  1.00 62.68  ? 22  PRO B N   1 
ATOM   3603  C  CA  . PRO B  1 22  ? 5.645   -0.474  47.080  1.00 63.90  ? 22  PRO B CA  1 
ATOM   3604  C  C   . PRO B  1 22  ? 6.537   -1.631  46.643  1.00 62.09  ? 22  PRO B C   1 
ATOM   3605  O  O   . PRO B  1 22  ? 7.189   -1.560  45.579  1.00 59.46  ? 22  PRO B O   1 
ATOM   3606  C  CB  . PRO B  1 22  ? 4.356   -0.469  46.291  1.00 65.30  ? 22  PRO B CB  1 
ATOM   3607  C  CG  . PRO B  1 22  ? 4.796   0.167   45.030  1.00 66.72  ? 22  PRO B CG  1 
ATOM   3608  C  CD  . PRO B  1 22  ? 5.520   1.373   45.555  1.00 66.15  ? 22  PRO B CD  1 
ATOM   3609  N  N   . GLY B  1 23  ? 6.501   -2.705  47.435  1.00 61.10  ? 23  GLY B N   1 
ATOM   3610  C  CA  . GLY B  1 23  ? 7.295   -3.884  47.142  1.00 61.21  ? 23  GLY B CA  1 
ATOM   3611  C  C   . GLY B  1 23  ? 8.122   -4.227  48.360  1.00 61.10  ? 23  GLY B C   1 
ATOM   3612  O  O   . GLY B  1 23  ? 8.412   -3.335  49.176  1.00 65.30  ? 23  GLY B O   1 
ATOM   3613  N  N   . TYR B  1 24  ? 8.485   -5.497  48.521  1.00 59.23  ? 24  TYR B N   1 
ATOM   3614  C  CA  . TYR B  1 24  ? 9.260   -5.882  49.684  1.00 54.86  ? 24  TYR B CA  1 
ATOM   3615  C  C   . TYR B  1 24  ? 10.656  -5.442  49.446  1.00 54.54  ? 24  TYR B C   1 
ATOM   3616  O  O   . TYR B  1 24  ? 11.259  -5.827  48.442  1.00 54.65  ? 24  TYR B O   1 
ATOM   3617  C  CB  . TYR B  1 24  ? 9.292   -7.393  49.899  1.00 52.49  ? 24  TYR B CB  1 
ATOM   3618  C  CG  . TYR B  1 24  ? 10.274  -7.801  50.995  1.00 49.91  ? 24  TYR B CG  1 
ATOM   3619  C  CD1 . TYR B  1 24  ? 9.994   -7.548  52.336  1.00 48.55  ? 24  TYR B CD1 1 
ATOM   3620  C  CD2 . TYR B  1 24  ? 11.498  -8.415  50.694  1.00 47.26  ? 24  TYR B CD2 1 
ATOM   3621  C  CE1 . TYR B  1 24  ? 10.885  -7.876  53.342  1.00 45.21  ? 24  TYR B CE1 1 
ATOM   3622  C  CE2 . TYR B  1 24  ? 12.400  -8.756  51.710  1.00 42.58  ? 24  TYR B CE2 1 
ATOM   3623  C  CZ  . TYR B  1 24  ? 12.076  -8.479  53.037  1.00 44.40  ? 24  TYR B CZ  1 
ATOM   3624  O  OH  . TYR B  1 24  ? 12.909  -8.794  54.097  1.00 44.74  ? 24  TYR B OH  1 
ATOM   3625  N  N   . ASN B  1 25  ? 11.165  -4.665  50.394  1.00 53.85  ? 25  ASN B N   1 
ATOM   3626  C  CA  . ASN B  1 25  ? 12.534  -4.170  50.340  1.00 55.90  ? 25  ASN B CA  1 
ATOM   3627  C  C   . ASN B  1 25  ? 12.740  -3.477  48.987  1.00 58.34  ? 25  ASN B C   1 
ATOM   3628  O  O   . ASN B  1 25  ? 13.574  -3.898  48.147  1.00 60.79  ? 25  ASN B O   1 
ATOM   3629  C  CB  . ASN B  1 25  ? 13.485  -5.345  50.465  1.00 49.70  ? 25  ASN B CB  1 
ATOM   3630  C  CG  . ASN B  1 25  ? 14.794  -4.956  51.032  1.00 47.74  ? 25  ASN B CG  1 
ATOM   3631  O  OD1 . ASN B  1 25  ? 15.833  -5.473  50.590  1.00 48.48  ? 25  ASN B OD1 1 
ATOM   3632  N  ND2 . ASN B  1 25  ? 14.774  -4.078  52.057  1.00 33.30  ? 25  ASN B ND2 1 
ATOM   3633  N  N   . ALA B  1 26  ? 11.892  -2.478  48.753  1.00 55.94  ? 26  ALA B N   1 
ATOM   3634  C  CA  . ALA B  1 26  ? 11.918  -1.717  47.517  1.00 50.40  ? 26  ALA B CA  1 
ATOM   3635  C  C   . ALA B  1 26  ? 12.846  -0.549  47.709  1.00 48.33  ? 26  ALA B C   1 
ATOM   3636  O  O   . ALA B  1 26  ? 12.707  0.208   48.702  1.00 53.30  ? 26  ALA B O   1 
ATOM   3637  C  CB  . ALA B  1 26  ? 10.530  -1.215  47.194  1.00 51.63  ? 26  ALA B CB  1 
ATOM   3638  N  N   . PRO B  1 27  ? 13.786  -0.365  46.762  1.00 41.41  ? 27  PRO B N   1 
ATOM   3639  C  CA  . PRO B  1 27  ? 14.777  0.713   46.776  1.00 38.44  ? 27  PRO B CA  1 
ATOM   3640  C  C   . PRO B  1 27  ? 14.078  2.019   46.920  1.00 38.95  ? 27  PRO B C   1 
ATOM   3641  O  O   . PRO B  1 27  ? 13.141  2.310   46.174  1.00 43.78  ? 27  PRO B O   1 
ATOM   3642  C  CB  . PRO B  1 27  ? 15.403  0.635   45.394  1.00 37.82  ? 27  PRO B CB  1 
ATOM   3643  C  CG  . PRO B  1 27  ? 15.284  -0.833  45.040  1.00 38.72  ? 27  PRO B CG  1 
ATOM   3644  C  CD  . PRO B  1 27  ? 13.875  -1.150  45.521  1.00 38.51  ? 27  PRO B CD  1 
ATOM   3645  N  N   . GLN B  1 28  ? 14.444  2.769   47.939  1.00 35.84  ? 28  GLN B N   1 
ATOM   3646  C  CA  . GLN B  1 28  ? 13.854  4.072   48.068  1.00 41.50  ? 28  GLN B CA  1 
ATOM   3647  C  C   . GLN B  1 28  ? 14.976  5.102   48.202  1.00 42.19  ? 28  GLN B C   1 
ATOM   3648  O  O   . GLN B  1 28  ? 16.162  4.737   48.316  1.00 43.66  ? 28  GLN B O   1 
ATOM   3649  C  CB  . GLN B  1 28  ? 12.920  4.119   49.257  1.00 42.06  ? 28  GLN B CB  1 
ATOM   3650  C  CG  . GLN B  1 28  ? 13.603  4.118   50.571  1.00 38.31  ? 28  GLN B CG  1 
ATOM   3651  C  CD  . GLN B  1 28  ? 12.600  4.036   51.670  1.00 42.46  ? 28  GLN B CD  1 
ATOM   3652  O  OE1 . GLN B  1 28  ? 11.889  3.025   51.790  1.00 47.24  ? 28  GLN B OE1 1 
ATOM   3653  N  NE2 . GLN B  1 28  ? 12.466  5.118   52.446  1.00 36.04  ? 28  GLN B NE2 1 
ATOM   3654  N  N   . GLN B  1 29  ? 14.594  6.376   48.102  1.00 39.61  ? 29  GLN B N   1 
ATOM   3655  C  CA  . GLN B  1 29  ? 15.509  7.482   48.240  1.00 33.33  ? 29  GLN B CA  1 
ATOM   3656  C  C   . GLN B  1 29  ? 16.613  7.355   47.210  1.00 38.70  ? 29  GLN B C   1 
ATOM   3657  O  O   . GLN B  1 29  ? 17.786  7.588   47.524  1.00 40.86  ? 29  GLN B O   1 
ATOM   3658  C  CB  . GLN B  1 29  ? 16.079  7.491   49.649  1.00 25.65  ? 29  GLN B CB  1 
ATOM   3659  C  CG  . GLN B  1 29  ? 15.052  7.666   50.749  1.00 33.08  ? 29  GLN B CG  1 
ATOM   3660  C  CD  . GLN B  1 29  ? 15.637  7.697   52.161  1.00 39.88  ? 29  GLN B CD  1 
ATOM   3661  O  OE1 . GLN B  1 29  ? 16.627  8.367   52.425  1.00 48.41  ? 29  GLN B OE1 1 
ATOM   3662  N  NE2 . GLN B  1 29  ? 14.999  6.985   53.078  1.00 43.45  ? 29  GLN B NE2 1 
ATOM   3663  N  N   . VAL B  1 30  ? 16.271  6.944   45.984  1.00 38.94  ? 30  VAL B N   1 
ATOM   3664  C  CA  . VAL B  1 30  ? 17.302  6.815   44.928  1.00 40.22  ? 30  VAL B CA  1 
ATOM   3665  C  C   . VAL B  1 30  ? 17.889  8.199   44.522  1.00 44.58  ? 30  VAL B C   1 
ATOM   3666  O  O   . VAL B  1 30  ? 17.170  9.215   44.511  1.00 50.50  ? 30  VAL B O   1 
ATOM   3667  C  CB  . VAL B  1 30  ? 16.778  6.045   43.693  1.00 31.96  ? 30  VAL B CB  1 
ATOM   3668  C  CG1 . VAL B  1 30  ? 17.894  5.877   42.644  1.00 33.98  ? 30  VAL B CG1 1 
ATOM   3669  C  CG2 . VAL B  1 30  ? 16.316  4.683   44.117  1.00 31.83  ? 30  VAL B CG2 1 
ATOM   3670  N  N   . HIS B  1 31  ? 19.207  8.265   44.314  1.00 44.29  ? 31  HIS B N   1 
ATOM   3671  C  CA  . HIS B  1 31  ? 19.859  9.515   43.922  1.00 45.37  ? 31  HIS B CA  1 
ATOM   3672  C  C   . HIS B  1 31  ? 21.188  9.266   43.277  1.00 45.20  ? 31  HIS B C   1 
ATOM   3673  O  O   . HIS B  1 31  ? 21.877  8.333   43.636  1.00 50.99  ? 31  HIS B O   1 
ATOM   3674  C  CB  . HIS B  1 31  ? 19.981  10.501  45.099  1.00 50.68  ? 31  HIS B CB  1 
ATOM   3675  C  CG  . HIS B  1 31  ? 20.607  9.938   46.344  1.00 58.04  ? 31  HIS B CG  1 
ATOM   3676  N  ND1 . HIS B  1 31  ? 21.845  10.346  46.794  1.00 65.16  ? 31  HIS B ND1 1 
ATOM   3677  C  CD2 . HIS B  1 31  ? 20.127  9.085   47.286  1.00 58.86  ? 31  HIS B CD2 1 
ATOM   3678  C  CE1 . HIS B  1 31  ? 22.097  9.776   47.963  1.00 64.23  ? 31  HIS B CE1 1 
ATOM   3679  N  NE2 . HIS B  1 31  ? 21.073  9.008   48.283  1.00 61.24  ? 31  HIS B NE2 1 
ATOM   3680  N  N   . ILE B  1 32  ? 21.550  10.080  42.302  1.00 45.09  ? 32  ILE B N   1 
ATOM   3681  C  CA  . ILE B  1 32  ? 22.821  9.895   41.594  1.00 42.90  ? 32  ILE B CA  1 
ATOM   3682  C  C   . ILE B  1 32  ? 23.672  11.174  41.609  1.00 41.68  ? 32  ILE B C   1 
ATOM   3683  O  O   . ILE B  1 32  ? 23.197  12.210  42.092  1.00 42.31  ? 32  ILE B O   1 
ATOM   3684  C  CB  . ILE B  1 32  ? 22.560  9.473   40.136  1.00 42.03  ? 32  ILE B CB  1 
ATOM   3685  C  CG1 . ILE B  1 32  ? 21.929  10.617  39.330  1.00 43.27  ? 32  ILE B CG1 1 
ATOM   3686  C  CG2 . ILE B  1 32  ? 21.585  8.321   40.109  1.00 47.38  ? 32  ILE B CG2 1 
ATOM   3687  C  CD1 . ILE B  1 32  ? 21.754  10.337  37.824  1.00 42.33  ? 32  ILE B CD1 1 
ATOM   3688  N  N   . THR B  1 33  ? 24.938  11.081  41.171  1.00 39.86  ? 33  THR B N   1 
ATOM   3689  C  CA  . THR B  1 33  ? 25.890  12.231  41.075  1.00 39.96  ? 33  THR B CA  1 
ATOM   3690  C  C   . THR B  1 33  ? 27.004  11.827  40.194  1.00 38.36  ? 33  THR B C   1 
ATOM   3691  O  O   . THR B  1 33  ? 27.197  10.644  39.912  1.00 43.40  ? 33  THR B O   1 
ATOM   3692  C  CB  . THR B  1 33  ? 26.670  12.634  42.344  1.00 38.95  ? 33  THR B CB  1 
ATOM   3693  O  OG1 . THR B  1 33  ? 25.977  12.240  43.535  1.00 56.18  ? 33  THR B OG1 1 
ATOM   3694  C  CG2 . THR B  1 33  ? 26.855  14.124  42.344  1.00 25.85  ? 33  THR B CG2 1 
ATOM   3695  N  N   . GLN B  1 34  ? 27.832  12.787  39.862  1.00 35.22  ? 34  GLN B N   1 
ATOM   3696  C  CA  . GLN B  1 34  ? 28.935  12.444  38.998  1.00 37.14  ? 34  GLN B CA  1 
ATOM   3697  C  C   . GLN B  1 34  ? 29.908  11.628  39.815  1.00 37.35  ? 34  GLN B C   1 
ATOM   3698  O  O   . GLN B  1 34  ? 30.155  11.957  40.979  1.00 37.71  ? 34  GLN B O   1 
ATOM   3699  C  CB  . GLN B  1 34  ? 29.585  13.693  38.447  1.00 36.64  ? 34  GLN B CB  1 
ATOM   3700  C  CG  . GLN B  1 34  ? 30.689  13.371  37.515  1.00 33.38  ? 34  GLN B CG  1 
ATOM   3701  C  CD  . GLN B  1 34  ? 31.002  14.514  36.646  1.00 35.96  ? 34  GLN B CD  1 
ATOM   3702  O  OE1 . GLN B  1 34  ? 32.168  14.816  36.427  1.00 38.55  ? 34  GLN B OE1 1 
ATOM   3703  N  NE2 . GLN B  1 34  ? 29.970  15.155  36.107  1.00 33.82  ? 34  GLN B NE2 1 
ATOM   3704  N  N   . GLY B  1 35  ? 30.445  10.575  39.209  1.00 33.10  ? 35  GLY B N   1 
ATOM   3705  C  CA  . GLY B  1 35  ? 31.335  9.714   39.935  1.00 34.46  ? 35  GLY B CA  1 
ATOM   3706  C  C   . GLY B  1 35  ? 32.783  9.859   39.600  1.00 36.67  ? 35  GLY B C   1 
ATOM   3707  O  O   . GLY B  1 35  ? 33.606  9.175   40.181  1.00 42.05  ? 35  GLY B O   1 
ATOM   3708  N  N   . ASP B  1 36  ? 33.125  10.698  38.645  1.00 36.36  ? 36  ASP B N   1 
ATOM   3709  C  CA  . ASP B  1 36  ? 34.535  10.859  38.325  1.00 31.67  ? 36  ASP B CA  1 
ATOM   3710  C  C   . ASP B  1 36  ? 34.787  12.307  38.052  1.00 32.97  ? 36  ASP B C   1 
ATOM   3711  O  O   . ASP B  1 36  ? 33.875  13.145  38.139  1.00 31.25  ? 36  ASP B O   1 
ATOM   3712  C  CB  . ASP B  1 36  ? 34.923  10.032  37.110  1.00 28.88  ? 36  ASP B CB  1 
ATOM   3713  C  CG  . ASP B  1 36  ? 34.221  10.471  35.834  1.00 35.90  ? 36  ASP B CG  1 
ATOM   3714  O  OD1 . ASP B  1 36  ? 33.325  11.358  35.880  1.00 37.63  ? 36  ASP B OD1 1 
ATOM   3715  O  OD2 . ASP B  1 36  ? 34.586  9.915   34.771  1.00 35.48  ? 36  ASP B OD2 1 
ATOM   3716  N  N   . LEU B  1 37  ? 35.995  12.594  37.604  1.00 31.40  ? 37  LEU B N   1 
ATOM   3717  C  CA  . LEU B  1 37  ? 36.311  13.970  37.320  1.00 33.76  ? 37  LEU B CA  1 
ATOM   3718  C  C   . LEU B  1 37  ? 35.719  14.583  36.051  1.00 38.81  ? 37  LEU B C   1 
ATOM   3719  O  O   . LEU B  1 37  ? 35.397  15.767  36.034  1.00 36.75  ? 37  LEU B O   1 
ATOM   3720  C  CB  . LEU B  1 37  ? 37.810  14.133  37.289  1.00 28.88  ? 37  LEU B CB  1 
ATOM   3721  C  CG  . LEU B  1 37  ? 38.218  15.598  37.311  1.00 31.06  ? 37  LEU B CG  1 
ATOM   3722  C  CD1 . LEU B  1 37  ? 37.648  16.263  38.551  1.00 32.62  ? 37  LEU B CD1 1 
ATOM   3723  C  CD2 . LEU B  1 37  ? 39.701  15.745  37.290  1.00 26.80  ? 37  LEU B CD2 1 
ATOM   3724  N  N   . VAL B  1 38  ? 35.497  13.770  35.020  1.00 42.75  ? 38  VAL B N   1 
ATOM   3725  C  CA  . VAL B  1 38  ? 35.059  14.306  33.739  1.00 45.22  ? 38  VAL B CA  1 
ATOM   3726  C  C   . VAL B  1 38  ? 33.721  13.942  33.104  1.00 49.35  ? 38  VAL B C   1 
ATOM   3727  O  O   . VAL B  1 38  ? 33.416  14.357  31.957  1.00 50.84  ? 38  VAL B O   1 
ATOM   3728  C  CB  . VAL B  1 38  ? 36.134  14.052  32.736  1.00 47.09  ? 38  VAL B CB  1 
ATOM   3729  C  CG1 . VAL B  1 38  ? 37.489  14.277  33.370  1.00 50.24  ? 38  VAL B CG1 1 
ATOM   3730  C  CG2 . VAL B  1 38  ? 36.054  12.658  32.260  1.00 49.51  ? 38  VAL B CG2 1 
ATOM   3731  N  N   . GLY B  1 39  ? 32.929  13.151  33.808  1.00 52.22  ? 39  GLY B N   1 
ATOM   3732  C  CA  . GLY B  1 39  ? 31.626  12.820  33.261  1.00 52.37  ? 39  GLY B CA  1 
ATOM   3733  C  C   . GLY B  1 39  ? 31.277  11.392  32.928  1.00 49.99  ? 39  GLY B C   1 
ATOM   3734  O  O   . GLY B  1 39  ? 30.102  11.078  32.706  1.00 49.82  ? 39  GLY B O   1 
ATOM   3735  N  N   . ARG B  1 40  ? 32.254  10.501  32.930  1.00 46.89  ? 40  ARG B N   1 
ATOM   3736  C  CA  . ARG B  1 40  ? 31.913  9.140   32.601  1.00 46.99  ? 40  ARG B CA  1 
ATOM   3737  C  C   . ARG B  1 40  ? 31.811  8.106   33.726  1.00 45.76  ? 40  ARG B C   1 
ATOM   3738  O  O   . ARG B  1 40  ? 32.232  6.962   33.598  1.00 45.35  ? 40  ARG B O   1 
ATOM   3739  C  CB  . ARG B  1 40  ? 32.706  8.658   31.390  1.00 50.64  ? 40  ARG B CB  1 
ATOM   3740  C  CG  . ARG B  1 40  ? 34.201  8.738   31.463  1.00 63.36  ? 40  ARG B CG  1 
ATOM   3741  C  CD  . ARG B  1 40  ? 34.810  8.891   30.043  1.00 69.09  ? 40  ARG B CD  1 
ATOM   3742  N  NE  . ARG B  1 40  ? 34.414  7.846   29.090  1.00 72.21  ? 40  ARG B NE  1 
ATOM   3743  C  CZ  . ARG B  1 40  ? 35.051  6.688   28.934  1.00 75.58  ? 40  ARG B CZ  1 
ATOM   3744  N  NH1 . ARG B  1 40  ? 36.128  6.414   29.668  1.00 77.68  ? 40  ARG B NH1 1 
ATOM   3745  N  NH2 . ARG B  1 40  ? 34.610  5.803   28.043  1.00 77.90  ? 40  ARG B NH2 1 
ATOM   3746  N  N   . ALA B  1 41  ? 31.164  8.501   34.807  1.00 43.03  ? 41  ALA B N   1 
ATOM   3747  C  CA  . ALA B  1 41  ? 30.968  7.615   35.924  1.00 41.95  ? 41  ALA B CA  1 
ATOM   3748  C  C   . ALA B  1 41  ? 29.883  8.258   36.735  1.00 42.09  ? 41  ALA B C   1 
ATOM   3749  O  O   . ALA B  1 41  ? 29.795  9.469   36.805  1.00 41.37  ? 41  ALA B O   1 
ATOM   3750  C  CB  . ALA B  1 41  ? 32.222  7.504   36.737  1.00 41.25  ? 41  ALA B CB  1 
ATOM   3751  N  N   . MET B  1 42  ? 29.058  7.442   37.357  1.00 42.70  ? 42  MET B N   1 
ATOM   3752  C  CA  . MET B  1 42  ? 27.983  7.941   38.181  1.00 39.24  ? 42  MET B CA  1 
ATOM   3753  C  C   . MET B  1 42  ? 27.982  7.189   39.460  1.00 38.14  ? 42  MET B C   1 
ATOM   3754  O  O   . MET B  1 42  ? 28.361  6.031   39.504  1.00 39.71  ? 42  MET B O   1 
ATOM   3755  C  CB  . MET B  1 42  ? 26.674  7.642   37.531  1.00 41.68  ? 42  MET B CB  1 
ATOM   3756  C  CG  . MET B  1 42  ? 26.339  8.611   36.513  1.00 46.97  ? 42  MET B CG  1 
ATOM   3757  S  SD  . MET B  1 42  ? 25.657  9.985   37.370  1.00 51.80  ? 42  MET B SD  1 
ATOM   3758  C  CE  . MET B  1 42  ? 25.126  10.844  35.986  1.00 46.67  ? 42  MET B CE  1 
ATOM   3759  N  N   . ILE B  1 43  ? 27.514  7.826   40.504  1.00 35.27  ? 43  ILE B N   1 
ATOM   3760  C  CA  . ILE B  1 43  ? 27.435  7.153   41.772  1.00 31.20  ? 43  ILE B CA  1 
ATOM   3761  C  C   . ILE B  1 43  ? 25.955  7.000   42.012  1.00 33.98  ? 43  ILE B C   1 
ATOM   3762  O  O   . ILE B  1 43  ? 25.215  7.985   42.108  1.00 36.60  ? 43  ILE B O   1 
ATOM   3763  C  CB  . ILE B  1 43  ? 27.985  7.985   42.897  1.00 31.79  ? 43  ILE B CB  1 
ATOM   3764  C  CG1 . ILE B  1 43  ? 29.491  8.097   42.808  1.00 30.78  ? 43  ILE B CG1 1 
ATOM   3765  C  CG2 . ILE B  1 43  ? 27.613  7.380   44.192  1.00 27.66  ? 43  ILE B CG2 1 
ATOM   3766  C  CD1 . ILE B  1 43  ? 30.032  9.011   43.886  1.00 31.83  ? 43  ILE B CD1 1 
ATOM   3767  N  N   . ILE B  1 44  ? 25.518  5.760   42.078  1.00 36.40  ? 44  ILE B N   1 
ATOM   3768  C  CA  . ILE B  1 44  ? 24.123  5.439   42.315  1.00 33.51  ? 44  ILE B CA  1 
ATOM   3769  C  C   . ILE B  1 44  ? 23.989  5.104   43.801  1.00 35.33  ? 44  ILE B C   1 
ATOM   3770  O  O   . ILE B  1 44  ? 24.753  4.297   44.353  1.00 37.19  ? 44  ILE B O   1 
ATOM   3771  C  CB  . ILE B  1 44  ? 23.732  4.225   41.507  1.00 33.63  ? 44  ILE B CB  1 
ATOM   3772  C  CG1 . ILE B  1 44  ? 24.347  4.266   40.090  1.00 37.07  ? 44  ILE B CG1 1 
ATOM   3773  C  CG2 . ILE B  1 44  ? 22.270  4.160   41.439  1.00 37.60  ? 44  ILE B CG2 1 
ATOM   3774  C  CD1 . ILE B  1 44  ? 23.788  5.344   39.177  1.00 34.40  ? 44  ILE B CD1 1 
ATOM   3775  N  N   . SER B  1 45  ? 23.011  5.696   44.449  1.00 34.22  ? 45  SER B N   1 
ATOM   3776  C  CA  . SER B  1 45  ? 22.834  5.480   45.872  1.00 36.99  ? 45  SER B CA  1 
ATOM   3777  C  C   . SER B  1 45  ? 21.381  5.270   46.197  1.00 37.37  ? 45  SER B C   1 
ATOM   3778  O  O   . SER B  1 45  ? 20.532  5.923   45.631  1.00 41.98  ? 45  SER B O   1 
ATOM   3779  C  CB  . SER B  1 45  ? 23.269  6.729   46.653  1.00 35.68  ? 45  SER B CB  1 
ATOM   3780  O  OG  . SER B  1 45  ? 24.519  7.240   46.219  1.00 40.66  ? 45  SER B OG  1 
ATOM   3781  N  N   . TRP B  1 46  ? 21.069  4.366   47.100  1.00 37.52  ? 46  TRP B N   1 
ATOM   3782  C  CA  . TRP B  1 46  ? 19.677  4.209   47.488  1.00 38.88  ? 46  TRP B CA  1 
ATOM   3783  C  C   . TRP B  1 46  ? 19.609  3.583   48.826  1.00 38.06  ? 46  TRP B C   1 
ATOM   3784  O  O   . TRP B  1 46  ? 20.627  3.181   49.387  1.00 43.11  ? 46  TRP B O   1 
ATOM   3785  C  CB  . TRP B  1 46  ? 18.910  3.351   46.523  1.00 38.46  ? 46  TRP B CB  1 
ATOM   3786  C  CG  . TRP B  1 46  ? 19.415  2.001   46.494  1.00 36.46  ? 46  TRP B CG  1 
ATOM   3787  C  CD1 . TRP B  1 46  ? 18.851  0.922   47.069  1.00 32.11  ? 46  TRP B CD1 1 
ATOM   3788  C  CD2 . TRP B  1 46  ? 20.580  1.550   45.805  1.00 34.98  ? 46  TRP B CD2 1 
ATOM   3789  N  NE1 . TRP B  1 46  ? 19.593  -0.195  46.769  1.00 37.76  ? 46  TRP B NE1 1 
ATOM   3790  C  CE2 . TRP B  1 46  ? 20.664  0.168   45.998  1.00 35.84  ? 46  TRP B CE2 1 
ATOM   3791  C  CE3 . TRP B  1 46  ? 21.564  2.181   45.033  1.00 34.73  ? 46  TRP B CE3 1 
ATOM   3792  C  CZ2 . TRP B  1 46  ? 21.696  -0.610  45.449  1.00 37.55  ? 46  TRP B CZ2 1 
ATOM   3793  C  CZ3 . TRP B  1 46  ? 22.586  1.417   44.485  1.00 28.09  ? 46  TRP B CZ3 1 
ATOM   3794  C  CH2 . TRP B  1 46  ? 22.644  0.038   44.696  1.00 31.31  ? 46  TRP B CH2 1 
ATOM   3795  N  N   . VAL B  1 47  ? 18.399  3.385   49.294  1.00 32.75  ? 47  VAL B N   1 
ATOM   3796  C  CA  . VAL B  1 47  ? 18.216  2.816   50.606  1.00 33.26  ? 47  VAL B CA  1 
ATOM   3797  C  C   . VAL B  1 47  ? 17.183  1.720   50.545  1.00 34.84  ? 47  VAL B C   1 
ATOM   3798  O  O   . VAL B  1 47  ? 16.240  1.856   49.777  1.00 40.96  ? 47  VAL B O   1 
ATOM   3799  C  CB  . VAL B  1 47  ? 17.727  3.888   51.540  1.00 30.00  ? 47  VAL B CB  1 
ATOM   3800  C  CG1 . VAL B  1 47  ? 17.358  3.290   52.831  1.00 27.96  ? 47  VAL B CG1 1 
ATOM   3801  C  CG2 . VAL B  1 47  ? 18.788  4.972   51.683  1.00 34.92  ? 47  VAL B CG2 1 
ATOM   3802  N  N   . THR B  1 48  ? 17.400  0.627   51.284  1.00 33.14  ? 48  THR B N   1 
ATOM   3803  C  CA  . THR B  1 48  ? 16.466  -0.503  51.362  1.00 31.17  ? 48  THR B CA  1 
ATOM   3804  C  C   . THR B  1 48  ? 16.171  -0.517  52.820  1.00 35.58  ? 48  THR B C   1 
ATOM   3805  O  O   . THR B  1 48  ? 17.086  -0.328  53.620  1.00 39.54  ? 48  THR B O   1 
ATOM   3806  C  CB  . THR B  1 48  ? 17.104  -1.848  51.055  1.00 28.37  ? 48  THR B CB  1 
ATOM   3807  O  OG1 . THR B  1 48  ? 18.308  -1.991  51.813  1.00 36.51  ? 48  THR B OG1 1 
ATOM   3808  C  CG2 . THR B  1 48  ? 17.431  -1.983  49.584  1.00 31.64  ? 48  THR B CG2 1 
ATOM   3809  N  N   . MET B  1 49  ? 14.926  -0.769  53.194  1.00 40.70  ? 49  MET B N   1 
ATOM   3810  C  CA  . MET B  1 49  ? 14.576  -0.748  54.607  1.00 42.12  ? 49  MET B CA  1 
ATOM   3811  C  C   . MET B  1 49  ? 14.226  -2.068  55.286  1.00 44.88  ? 49  MET B C   1 
ATOM   3812  O  O   . MET B  1 49  ? 14.292  -2.183  56.519  1.00 47.82  ? 49  MET B O   1 
ATOM   3813  C  CB  . MET B  1 49  ? 13.416  0.206   54.784  1.00 43.13  ? 49  MET B CB  1 
ATOM   3814  C  CG  . MET B  1 49  ? 13.715  1.626   54.446  1.00 44.19  ? 49  MET B CG  1 
ATOM   3815  S  SD  . MET B  1 49  ? 14.151  2.529   55.920  1.00 54.33  ? 49  MET B SD  1 
ATOM   3816  C  CE  . MET B  1 49  ? 12.886  4.030   55.818  1.00 64.16  ? 49  MET B CE  1 
ATOM   3817  N  N   . ASP B  1 50  ? 13.823  -3.051  54.493  1.00 46.97  ? 50  ASP B N   1 
ATOM   3818  C  CA  . ASP B  1 50  ? 13.413  -4.331  55.052  1.00 50.39  ? 50  ASP B CA  1 
ATOM   3819  C  C   . ASP B  1 50  ? 14.568  -5.208  55.420  1.00 50.49  ? 50  ASP B C   1 
ATOM   3820  O  O   . ASP B  1 50  ? 14.618  -5.785  56.490  1.00 50.20  ? 50  ASP B O   1 
ATOM   3821  C  CB  . ASP B  1 50  ? 12.469  -5.015  54.088  1.00 52.62  ? 50  ASP B CB  1 
ATOM   3822  C  CG  . ASP B  1 50  ? 11.198  -4.267  53.964  1.00 58.53  ? 50  ASP B CG  1 
ATOM   3823  O  OD1 . ASP B  1 50  ? 10.699  -3.809  55.032  1.00 59.55  ? 50  ASP B OD1 1 
ATOM   3824  O  OD2 . ASP B  1 50  ? 10.736  -4.076  52.818  1.00 63.41  ? 50  ASP B OD2 1 
ATOM   3825  N  N   . GLU B  1 51  ? 15.511  -5.311  54.516  1.00 49.16  ? 51  GLU B N   1 
ATOM   3826  C  CA  . GLU B  1 51  ? 16.665  -6.088  54.794  1.00 45.43  ? 51  GLU B CA  1 
ATOM   3827  C  C   . GLU B  1 51  ? 17.749  -5.533  53.879  1.00 45.12  ? 51  GLU B C   1 
ATOM   3828  O  O   . GLU B  1 51  ? 17.469  -4.766  52.965  1.00 40.83  ? 51  GLU B O   1 
ATOM   3829  C  CB  . GLU B  1 51  ? 16.355  -7.575  54.579  1.00 40.24  ? 51  GLU B CB  1 
ATOM   3830  C  CG  . GLU B  1 51  ? 15.682  -7.906  53.275  1.00 42.67  ? 51  GLU B CG  1 
ATOM   3831  C  CD  . GLU B  1 51  ? 15.893  -9.369  52.835  1.00 43.25  ? 51  GLU B CD  1 
ATOM   3832  O  OE1 . GLU B  1 51  ? 17.038  -9.736  52.467  1.00 38.14  ? 51  GLU B OE1 1 
ATOM   3833  O  OE2 . GLU B  1 51  ? 14.918  -10.163 52.843  1.00 46.52  ? 51  GLU B OE2 1 
ATOM   3834  N  N   . PRO B  1 52  ? 19.010  -5.779  54.227  1.00 48.30  ? 52  PRO B N   1 
ATOM   3835  C  CA  . PRO B  1 52  ? 20.196  -5.355  53.500  1.00 48.45  ? 52  PRO B CA  1 
ATOM   3836  C  C   . PRO B  1 52  ? 20.059  -5.246  51.979  1.00 46.47  ? 52  PRO B C   1 
ATOM   3837  O  O   . PRO B  1 52  ? 20.226  -4.157  51.422  1.00 46.44  ? 52  PRO B O   1 
ATOM   3838  C  CB  . PRO B  1 52  ? 21.206  -6.401  53.935  1.00 48.30  ? 52  PRO B CB  1 
ATOM   3839  C  CG  . PRO B  1 52  ? 20.928  -6.436  55.399  1.00 49.51  ? 52  PRO B CG  1 
ATOM   3840  C  CD  . PRO B  1 52  ? 19.411  -6.462  55.475  1.00 52.98  ? 52  PRO B CD  1 
ATOM   3841  N  N   . GLY B  1 53  ? 19.766  -6.354  51.313  1.00 44.95  ? 53  GLY B N   1 
ATOM   3842  C  CA  . GLY B  1 53  ? 19.610  -6.333  49.866  1.00 41.06  ? 53  GLY B CA  1 
ATOM   3843  C  C   . GLY B  1 53  ? 20.932  -6.401  49.125  1.00 38.51  ? 53  GLY B C   1 
ATOM   3844  O  O   . GLY B  1 53  ? 21.972  -6.527  49.761  1.00 36.73  ? 53  GLY B O   1 
ATOM   3845  N  N   . SER B  1 54  ? 20.885  -6.310  47.792  1.00 39.45  ? 54  SER B N   1 
ATOM   3846  C  CA  . SER B  1 54  ? 22.071  -6.362  46.935  1.00 41.03  ? 54  SER B CA  1 
ATOM   3847  C  C   . SER B  1 54  ? 22.487  -4.946  46.614  1.00 42.12  ? 54  SER B C   1 
ATOM   3848  O  O   . SER B  1 54  ? 21.645  -4.060  46.489  1.00 47.87  ? 54  SER B O   1 
ATOM   3849  C  CB  . SER B  1 54  ? 21.751  -7.069  45.619  1.00 40.95  ? 54  SER B CB  1 
ATOM   3850  O  OG  . SER B  1 54  ? 22.879  -7.142  44.766  1.00 47.80  ? 54  SER B OG  1 
ATOM   3851  N  N   . SER B  1 55  ? 23.782  -4.730  46.486  1.00 41.81  ? 55  SER B N   1 
ATOM   3852  C  CA  . SER B  1 55  ? 24.273  -3.414  46.168  1.00 38.33  ? 55  SER B CA  1 
ATOM   3853  C  C   . SER B  1 55  ? 24.708  -3.414  44.731  1.00 39.44  ? 55  SER B C   1 
ATOM   3854  O  O   . SER B  1 55  ? 25.545  -2.618  44.344  1.00 40.49  ? 55  SER B O   1 
ATOM   3855  C  CB  . SER B  1 55  ? 25.439  -3.067  47.066  1.00 37.42  ? 55  SER B CB  1 
ATOM   3856  O  OG  . SER B  1 55  ? 25.014  -3.121  48.413  1.00 45.36  ? 55  SER B OG  1 
ATOM   3857  N  N   . ALA B  1 56  ? 24.201  -4.360  43.947  1.00 39.82  ? 56  ALA B N   1 
ATOM   3858  C  CA  . ALA B  1 56  ? 24.560  -4.426  42.531  1.00 41.26  ? 56  ALA B CA  1 
ATOM   3859  C  C   . ALA B  1 56  ? 23.617  -3.510  41.799  1.00 43.30  ? 56  ALA B C   1 
ATOM   3860  O  O   . ALA B  1 56  ? 22.503  -3.259  42.255  1.00 46.38  ? 56  ALA B O   1 
ATOM   3861  C  CB  . ALA B  1 56  ? 24.403  -5.803  41.995  1.00 38.39  ? 56  ALA B CB  1 
ATOM   3862  N  N   . VAL B  1 57  ? 24.056  -3.018  40.660  1.00 43.20  ? 57  VAL B N   1 
ATOM   3863  C  CA  . VAL B  1 57  ? 23.228  -2.136  39.873  1.00 44.49  ? 57  VAL B CA  1 
ATOM   3864  C  C   . VAL B  1 57  ? 23.333  -2.689  38.489  1.00 45.78  ? 57  VAL B C   1 
ATOM   3865  O  O   . VAL B  1 57  ? 24.432  -3.040  38.038  1.00 44.46  ? 57  VAL B O   1 
ATOM   3866  C  CB  . VAL B  1 57  ? 23.772  -0.701  39.863  1.00 47.32  ? 57  VAL B CB  1 
ATOM   3867  C  CG1 . VAL B  1 57  ? 23.030  0.135   38.850  1.00 46.29  ? 57  VAL B CG1 1 
ATOM   3868  C  CG2 . VAL B  1 57  ? 23.643  -0.078  41.234  1.00 49.29  ? 57  VAL B CG2 1 
ATOM   3869  N  N   . ARG B  1 58  ? 22.197  -2.846  37.830  1.00 47.92  ? 58  ARG B N   1 
ATOM   3870  C  CA  . ARG B  1 58  ? 22.246  -3.348  36.476  1.00 50.01  ? 58  ARG B CA  1 
ATOM   3871  C  C   . ARG B  1 58  ? 22.011  -2.151  35.590  1.00 47.76  ? 58  ARG B C   1 
ATOM   3872  O  O   . ARG B  1 58  ? 21.125  -1.328  35.853  1.00 43.70  ? 58  ARG B O   1 
ATOM   3873  C  CB  . ARG B  1 58  ? 21.185  -4.424  36.235  1.00 59.81  ? 58  ARG B CB  1 
ATOM   3874  C  CG  . ARG B  1 58  ? 21.112  -4.917  34.771  1.00 63.27  ? 58  ARG B CG  1 
ATOM   3875  C  CD  . ARG B  1 58  ? 20.398  -6.250  34.648  1.00 62.28  ? 58  ARG B CD  1 
ATOM   3876  N  NE  . ARG B  1 58  ? 19.141  -6.267  35.389  1.00 61.59  ? 58  ARG B NE  1 
ATOM   3877  C  CZ  . ARG B  1 58  ? 18.820  -7.202  36.281  1.00 60.95  ? 58  ARG B CZ  1 
ATOM   3878  N  NH1 . ARG B  1 58  ? 19.669  -8.192  36.529  1.00 61.56  ? 58  ARG B NH1 1 
ATOM   3879  N  NH2 . ARG B  1 58  ? 17.671  -7.132  36.952  1.00 57.53  ? 58  ARG B NH2 1 
ATOM   3880  N  N   . TYR B  1 59  ? 22.800  -2.053  34.534  1.00 45.67  ? 59  TYR B N   1 
ATOM   3881  C  CA  . TYR B  1 59  ? 22.672  -0.931  33.631  1.00 44.97  ? 59  TYR B CA  1 
ATOM   3882  C  C   . TYR B  1 59  ? 23.117  -1.307  32.240  1.00 45.95  ? 59  TYR B C   1 
ATOM   3883  O  O   . TYR B  1 59  ? 23.982  -2.186  32.064  1.00 41.23  ? 59  TYR B O   1 
ATOM   3884  C  CB  . TYR B  1 59  ? 23.562  0.189   34.102  1.00 46.95  ? 59  TYR B CB  1 
ATOM   3885  C  CG  . TYR B  1 59  ? 25.043  -0.125  33.917  1.00 51.34  ? 59  TYR B CG  1 
ATOM   3886  C  CD1 . TYR B  1 59  ? 25.744  -0.865  34.858  1.00 53.16  ? 59  TYR B CD1 1 
ATOM   3887  C  CD2 . TYR B  1 59  ? 25.752  0.379   32.838  1.00 52.64  ? 59  TYR B CD2 1 
ATOM   3888  C  CE1 . TYR B  1 59  ? 27.111  -1.075  34.740  1.00 54.61  ? 59  TYR B CE1 1 
ATOM   3889  C  CE2 . TYR B  1 59  ? 27.120  0.169   32.709  1.00 55.57  ? 59  TYR B CE2 1 
ATOM   3890  C  CZ  . TYR B  1 59  ? 27.796  -0.553  33.669  1.00 56.37  ? 59  TYR B CZ  1 
ATOM   3891  O  OH  . TYR B  1 59  ? 29.171  -0.723  33.593  1.00 59.88  ? 59  TYR B OH  1 
ATOM   3892  N  N   . TRP B  1 60  ? 22.597  -0.557  31.271  1.00 48.69  ? 60  TRP B N   1 
ATOM   3893  C  CA  . TRP B  1 60  ? 22.898  -0.763  29.854  1.00 55.89  ? 60  TRP B CA  1 
ATOM   3894  C  C   . TRP B  1 60  ? 22.505  0.510   29.147  1.00 61.02  ? 60  TRP B C   1 
ATOM   3895  O  O   . TRP B  1 60  ? 21.686  1.299   29.666  1.00 62.98  ? 60  TRP B O   1 
ATOM   3896  C  CB  . TRP B  1 60  ? 22.083  -1.946  29.279  1.00 56.95  ? 60  TRP B CB  1 
ATOM   3897  C  CG  . TRP B  1 60  ? 20.566  -1.768  29.345  1.00 56.78  ? 60  TRP B CG  1 
ATOM   3898  C  CD1 . TRP B  1 60  ? 19.752  -1.319  28.349  1.00 54.98  ? 60  TRP B CD1 1 
ATOM   3899  C  CD2 . TRP B  1 60  ? 19.717  -1.986  30.482  1.00 56.83  ? 60  TRP B CD2 1 
ATOM   3900  N  NE1 . TRP B  1 60  ? 18.458  -1.234  28.791  1.00 50.91  ? 60  TRP B NE1 1 
ATOM   3901  C  CE2 . TRP B  1 60  ? 18.409  -1.637  30.097  1.00 55.23  ? 60  TRP B CE2 1 
ATOM   3902  C  CE3 . TRP B  1 60  ? 19.937  -2.437  31.793  1.00 58.42  ? 60  TRP B CE3 1 
ATOM   3903  C  CZ2 . TRP B  1 60  ? 17.333  -1.726  30.966  1.00 55.94  ? 60  TRP B CZ2 1 
ATOM   3904  C  CZ3 . TRP B  1 60  ? 18.862  -2.529  32.662  1.00 57.20  ? 60  TRP B CZ3 1 
ATOM   3905  C  CH2 . TRP B  1 60  ? 17.577  -2.172  32.243  1.00 58.96  ? 60  TRP B CH2 1 
ATOM   3906  N  N   . SER B  1 61  ? 23.067  0.718   27.965  1.00 63.36  ? 61  SER B N   1 
ATOM   3907  C  CA  . SER B  1 61  ? 22.737  1.920   27.223  1.00 68.12  ? 61  SER B CA  1 
ATOM   3908  C  C   . SER B  1 61  ? 21.616  1.620   26.282  1.00 76.54  ? 61  SER B C   1 
ATOM   3909  O  O   . SER B  1 61  ? 21.474  0.492   25.814  1.00 78.29  ? 61  SER B O   1 
ATOM   3910  C  CB  . SER B  1 61  ? 23.920  2.402   26.417  1.00 60.99  ? 61  SER B CB  1 
ATOM   3911  O  OG  . SER B  1 61  ? 24.247  1.473   25.428  1.00 59.84  ? 61  SER B OG  1 
ATOM   3912  N  N   . GLU B  1 62  ? 20.857  2.651   25.957  1.00 86.36  ? 62  GLU B N   1 
ATOM   3913  C  CA  . GLU B  1 62  ? 19.732  2.525   25.040  1.00 98.34  ? 62  GLU B CA  1 
ATOM   3914  C  C   . GLU B  1 62  ? 20.107  1.847   23.700  1.00 104.09 ? 62  GLU B C   1 
ATOM   3915  O  O   . GLU B  1 62  ? 19.345  1.037   23.171  1.00 108.45 ? 62  GLU B O   1 
ATOM   3916  C  CB  . GLU B  1 62  ? 19.143  3.915   24.783  1.00 98.85  ? 62  GLU B CB  1 
ATOM   3917  C  CG  . GLU B  1 62  ? 17.662  3.918   24.443  1.00 104.53 ? 62  GLU B CG  1 
ATOM   3918  C  CD  . GLU B  1 62  ? 17.091  5.325   24.266  1.00 106.68 ? 62  GLU B CD  1 
ATOM   3919  O  OE1 . GLU B  1 62  ? 17.758  6.162   23.614  1.00 108.38 ? 62  GLU B OE1 1 
ATOM   3920  O  OE2 . GLU B  1 62  ? 15.969  5.592   24.769  1.00 107.31 ? 62  GLU B OE2 1 
ATOM   3921  N  N   . LYS B  1 63  ? 21.287  2.170   23.180  1.00 108.66 ? 63  LYS B N   1 
ATOM   3922  C  CA  . LYS B  1 63  ? 21.779  1.626   21.911  1.00 113.63 ? 63  LYS B CA  1 
ATOM   3923  C  C   . LYS B  1 63  ? 22.299  0.188   22.019  1.00 114.90 ? 63  LYS B C   1 
ATOM   3924  O  O   . LYS B  1 63  ? 21.711  -0.737  21.462  1.00 116.83 ? 63  LYS B O   1 
ATOM   3925  C  CB  . LYS B  1 63  ? 22.876  2.539   21.344  1.00 119.58 ? 63  LYS B CB  1 
ATOM   3926  C  CG  . LYS B  1 63  ? 23.749  3.208   22.425  1.00 127.22 ? 63  LYS B CG  1 
ATOM   3927  C  CD  . LYS B  1 63  ? 25.157  3.570   21.928  1.00 130.68 ? 63  LYS B CD  1 
ATOM   3928  C  CE  . LYS B  1 63  ? 26.091  2.343   21.869  1.00 131.78 ? 63  LYS B CE  1 
ATOM   3929  N  NZ  . LYS B  1 63  ? 26.400  1.753   23.214  1.00 130.92 ? 63  LYS B NZ  1 
ATOM   3930  N  N   . ASN B  1 64  ? 23.450  0.023   22.666  1.00 117.22 ? 64  ASN B N   1 
ATOM   3931  C  CA  . ASN B  1 64  ? 24.070  -1.285  22.876  1.00 119.13 ? 64  ASN B CA  1 
ATOM   3932  C  C   . ASN B  1 64  ? 23.462  -1.844  24.168  1.00 118.37 ? 64  ASN B C   1 
ATOM   3933  O  O   . ASN B  1 64  ? 23.980  -1.629  25.278  1.00 119.62 ? 64  ASN B O   1 
ATOM   3934  C  CB  . ASN B  1 64  ? 25.607  -1.125  22.960  1.00 121.59 ? 64  ASN B CB  1 
ATOM   3935  C  CG  . ASN B  1 64  ? 26.293  -2.213  23.797  1.00 123.75 ? 64  ASN B CG  1 
ATOM   3936  O  OD1 . ASN B  1 64  ? 26.957  -1.913  24.800  1.00 123.59 ? 64  ASN B OD1 1 
ATOM   3937  N  ND2 . ASN B  1 64  ? 26.166  -3.471  23.368  1.00 124.55 ? 64  ASN B ND2 1 
ATOM   3938  N  N   . GLY B  1 65  ? 22.324  -2.513  24.011  1.00 115.75 ? 65  GLY B N   1 
ATOM   3939  C  CA  . GLY B  1 65  ? 21.626  -3.083  25.147  1.00 113.25 ? 65  GLY B CA  1 
ATOM   3940  C  C   . GLY B  1 65  ? 22.334  -4.122  26.013  1.00 111.16 ? 65  GLY B C   1 
ATOM   3941  O  O   . GLY B  1 65  ? 21.649  -4.790  26.791  1.00 111.77 ? 65  GLY B O   1 
ATOM   3942  N  N   . ARG B  1 66  ? 23.661  -4.283  25.896  1.00 105.70 ? 66  ARG B N   1 
ATOM   3943  C  CA  . ARG B  1 66  ? 24.399  -5.257  26.718  1.00 100.25 ? 66  ARG B CA  1 
ATOM   3944  C  C   . ARG B  1 66  ? 24.196  -4.870  28.184  1.00 95.03  ? 66  ARG B C   1 
ATOM   3945  O  O   . ARG B  1 66  ? 24.612  -3.787  28.599  1.00 94.52  ? 66  ARG B O   1 
ATOM   3946  C  CB  . ARG B  1 66  ? 25.892  -5.235  26.376  1.00 105.54 ? 66  ARG B CB  1 
ATOM   3947  C  CG  . ARG B  1 66  ? 26.809  -6.005  27.354  1.00 115.49 ? 66  ARG B CG  1 
ATOM   3948  C  CD  . ARG B  1 66  ? 28.300  -5.594  27.158  1.00 127.27 ? 66  ARG B CD  1 
ATOM   3949  N  NE  . ARG B  1 66  ? 29.065  -5.427  28.414  1.00 135.87 ? 66  ARG B NE  1 
ATOM   3950  C  CZ  . ARG B  1 66  ? 29.755  -4.330  28.768  1.00 138.18 ? 66  ARG B CZ  1 
ATOM   3951  N  NH1 . ARG B  1 66  ? 29.809  -3.252  27.979  1.00 138.03 ? 66  ARG B NH1 1 
ATOM   3952  N  NH2 . ARG B  1 66  ? 30.370  -4.294  29.950  1.00 137.94 ? 66  ARG B NH2 1 
ATOM   3953  N  N   . LYS B  1 67  ? 23.497  -5.714  28.943  1.00 87.84  ? 67  LYS B N   1 
ATOM   3954  C  CA  . LYS B  1 67  ? 23.230  -5.414  30.337  1.00 79.71  ? 67  LYS B CA  1 
ATOM   3955  C  C   . LYS B  1 67  ? 24.453  -5.772  31.126  1.00 74.89  ? 67  LYS B C   1 
ATOM   3956  O  O   . LYS B  1 67  ? 24.989  -6.859  30.951  1.00 74.57  ? 67  LYS B O   1 
ATOM   3957  C  CB  . LYS B  1 67  ? 22.000  -6.174  30.824  1.00 78.68  ? 67  LYS B CB  1 
ATOM   3958  C  CG  . LYS B  1 67  ? 20.719  -5.744  30.099  1.00 80.06  ? 67  LYS B CG  1 
ATOM   3959  C  CD  . LYS B  1 67  ? 19.437  -6.283  30.753  1.00 83.08  ? 67  LYS B CD  1 
ATOM   3960  C  CE  . LYS B  1 67  ? 18.161  -5.717  30.101  1.00 79.33  ? 67  LYS B CE  1 
ATOM   3961  N  NZ  . LYS B  1 67  ? 16.924  -6.062  30.875  1.00 82.15  ? 67  LYS B NZ  1 
ATOM   3962  N  N   . ARG B  1 68  ? 24.938  -4.827  31.927  1.00 72.25  ? 68  ARG B N   1 
ATOM   3963  C  CA  . ARG B  1 68  ? 26.133  -5.034  32.736  1.00 68.86  ? 68  ARG B CA  1 
ATOM   3964  C  C   . ARG B  1 68  ? 25.750  -4.819  34.189  1.00 65.05  ? 68  ARG B C   1 
ATOM   3965  O  O   . ARG B  1 68  ? 24.690  -4.241  34.491  1.00 60.62  ? 68  ARG B O   1 
ATOM   3966  C  CB  . ARG B  1 68  ? 27.221  -4.034  32.334  1.00 74.77  ? 68  ARG B CB  1 
ATOM   3967  C  CG  . ARG B  1 68  ? 27.473  -3.928  30.839  1.00 82.26  ? 68  ARG B CG  1 
ATOM   3968  C  CD  . ARG B  1 68  ? 27.587  -2.456  30.306  1.00 93.18  ? 68  ARG B CD  1 
ATOM   3969  N  NE  . ARG B  1 68  ? 26.436  -2.044  29.471  1.00 101.76 ? 68  ARG B NE  1 
ATOM   3970  C  CZ  . ARG B  1 68  ? 26.454  -1.121  28.498  1.00 102.61 ? 68  ARG B CZ  1 
ATOM   3971  N  NH1 . ARG B  1 68  ? 27.573  -0.460  28.193  1.00 104.44 ? 68  ARG B NH1 1 
ATOM   3972  N  NH2 . ARG B  1 68  ? 25.342  -0.880  27.807  1.00 99.30  ? 68  ARG B NH2 1 
ATOM   3973  N  N   . ILE B  1 69  ? 26.633  -5.255  35.081  1.00 61.79  ? 69  ILE B N   1 
ATOM   3974  C  CA  . ILE B  1 69  ? 26.399  -5.139  36.508  1.00 61.32  ? 69  ILE B CA  1 
ATOM   3975  C  C   . ILE B  1 69  ? 27.543  -4.508  37.276  1.00 57.98  ? 69  ILE B C   1 
ATOM   3976  O  O   . ILE B  1 69  ? 28.692  -4.891  37.112  1.00 59.80  ? 69  ILE B O   1 
ATOM   3977  C  CB  . ILE B  1 69  ? 26.097  -6.517  37.102  1.00 63.81  ? 69  ILE B CB  1 
ATOM   3978  C  CG1 . ILE B  1 69  ? 24.601  -6.755  37.047  1.00 69.31  ? 69  ILE B CG1 1 
ATOM   3979  C  CG2 . ILE B  1 69  ? 26.559  -6.630  38.543  1.00 63.29  ? 69  ILE B CG2 1 
ATOM   3980  C  CD1 . ILE B  1 69  ? 24.206  -8.056  37.691  1.00 82.60  ? 69  ILE B CD1 1 
ATOM   3981  N  N   . ALA B  1 70  ? 27.223  -3.543  38.123  1.00 55.48  ? 70  ALA B N   1 
ATOM   3982  C  CA  . ALA B  1 70  ? 28.234  -2.893  38.945  1.00 53.15  ? 70  ALA B CA  1 
ATOM   3983  C  C   . ALA B  1 70  ? 27.961  -3.307  40.374  1.00 53.05  ? 70  ALA B C   1 
ATOM   3984  O  O   . ALA B  1 70  ? 26.789  -3.420  40.764  1.00 51.19  ? 70  ALA B O   1 
ATOM   3985  C  CB  . ALA B  1 70  ? 28.111  -1.419  38.831  1.00 53.70  ? 70  ALA B CB  1 
ATOM   3986  N  N   . LYS B  1 71  ? 29.013  -3.553  41.149  1.00 51.96  ? 71  LYS B N   1 
ATOM   3987  C  CA  . LYS B  1 71  ? 28.803  -3.941  42.529  1.00 55.47  ? 71  LYS B CA  1 
ATOM   3988  C  C   . LYS B  1 71  ? 29.280  -2.829  43.467  1.00 51.99  ? 71  LYS B C   1 
ATOM   3989  O  O   . LYS B  1 71  ? 30.406  -2.366  43.347  1.00 55.11  ? 71  LYS B O   1 
ATOM   3990  C  CB  . LYS B  1 71  ? 29.492  -5.285  42.817  1.00 62.32  ? 71  LYS B CB  1 
ATOM   3991  C  CG  . LYS B  1 71  ? 28.546  -6.387  43.391  1.00 76.20  ? 71  LYS B CG  1 
ATOM   3992  C  CD  . LYS B  1 71  ? 27.934  -6.010  44.812  1.00 88.32  ? 71  LYS B CD  1 
ATOM   3993  C  CE  . LYS B  1 71  ? 26.893  -7.056  45.396  1.00 95.35  ? 71  LYS B CE  1 
ATOM   3994  N  NZ  . LYS B  1 71  ? 26.258  -6.743  46.761  1.00 94.11  ? 71  LYS B NZ  1 
ATOM   3995  N  N   . GLY B  1 72  ? 28.394  -2.363  44.345  1.00 48.82  ? 72  GLY B N   1 
ATOM   3996  C  CA  . GLY B  1 72  ? 28.720  -1.289  45.282  1.00 49.50  ? 72  GLY B CA  1 
ATOM   3997  C  C   . GLY B  1 72  ? 28.934  -1.751  46.714  1.00 49.50  ? 72  GLY B C   1 
ATOM   3998  O  O   . GLY B  1 72  ? 29.363  -2.891  46.912  1.00 49.60  ? 72  GLY B O   1 
ATOM   3999  N  N   . LYS B  1 73  ? 28.673  -0.883  47.702  1.00 49.21  ? 73  LYS B N   1 
ATOM   4000  C  CA  . LYS B  1 73  ? 28.848  -1.223  49.127  1.00 50.43  ? 73  LYS B CA  1 
ATOM   4001  C  C   . LYS B  1 73  ? 27.655  -0.794  49.949  1.00 46.77  ? 73  LYS B C   1 
ATOM   4002  O  O   . LYS B  1 73  ? 26.918  0.094   49.557  1.00 46.89  ? 73  LYS B O   1 
ATOM   4003  C  CB  . LYS B  1 73  ? 30.054  -0.528  49.743  1.00 60.57  ? 73  LYS B CB  1 
ATOM   4004  C  CG  . LYS B  1 73  ? 31.422  -0.926  49.245  1.00 76.07  ? 73  LYS B CG  1 
ATOM   4005  C  CD  . LYS B  1 73  ? 32.480  -0.280  50.167  1.00 91.96  ? 73  LYS B CD  1 
ATOM   4006  C  CE  . LYS B  1 73  ? 33.941  -0.356  49.634  1.00 103.18 ? 73  LYS B CE  1 
ATOM   4007  N  NZ  . LYS B  1 73  ? 35.002  0.289   50.531  1.00 107.26 ? 73  LYS B NZ  1 
ATOM   4008  N  N   . MET B  1 74  ? 27.520  -1.351  51.142  1.00 45.56  ? 74  MET B N   1 
ATOM   4009  C  CA  . MET B  1 74  ? 26.389  -1.008  51.985  1.00 40.31  ? 74  MET B CA  1 
ATOM   4010  C  C   . MET B  1 74  ? 26.866  -0.502  53.342  1.00 39.79  ? 74  MET B C   1 
ATOM   4011  O  O   . MET B  1 74  ? 27.878  -0.978  53.868  1.00 38.90  ? 74  MET B O   1 
ATOM   4012  C  CB  . MET B  1 74  ? 25.498  -2.227  52.166  1.00 35.59  ? 74  MET B CB  1 
ATOM   4013  C  CG  . MET B  1 74  ? 24.271  -1.930  52.952  1.00 36.20  ? 74  MET B CG  1 
ATOM   4014  S  SD  . MET B  1 74  ? 24.147  -2.976  54.382  1.00 41.27  ? 74  MET B SD  1 
ATOM   4015  C  CE  . MET B  1 74  ? 24.890  -2.101  55.576  1.00 43.92  ? 74  MET B CE  1 
ATOM   4016  N  N   . SER B  1 75  ? 26.102  0.410   53.935  1.00 37.17  ? 75  SER B N   1 
ATOM   4017  C  CA  . SER B  1 75  ? 26.452  0.975   55.228  1.00 36.59  ? 75  SER B CA  1 
ATOM   4018  C  C   . SER B  1 75  ? 25.209  1.339   55.997  1.00 35.65  ? 75  SER B C   1 
ATOM   4019  O  O   . SER B  1 75  ? 24.120  1.411   55.435  1.00 41.85  ? 75  SER B O   1 
ATOM   4020  C  CB  . SER B  1 75  ? 27.344  2.201   55.044  1.00 41.94  ? 75  SER B CB  1 
ATOM   4021  O  OG  . SER B  1 75  ? 27.136  2.857   53.788  1.00 51.00  ? 75  SER B OG  1 
ATOM   4022  N  N   . THR B  1 76  ? 25.376  1.593   57.280  1.00 31.73  ? 76  THR B N   1 
ATOM   4023  C  CA  . THR B  1 76  ? 24.265  1.937   58.158  1.00 33.14  ? 76  THR B CA  1 
ATOM   4024  C  C   . THR B  1 76  ? 24.860  2.816   59.229  1.00 35.35  ? 76  THR B C   1 
ATOM   4025  O  O   . THR B  1 76  ? 26.072  2.768   59.457  1.00 40.53  ? 76  THR B O   1 
ATOM   4026  C  CB  . THR B  1 76  ? 23.678  0.683   58.859  1.00 36.62  ? 76  THR B CB  1 
ATOM   4027  O  OG1 . THR B  1 76  ? 24.720  -0.062  59.494  1.00 43.15  ? 76  THR B OG1 1 
ATOM   4028  C  CG2 . THR B  1 76  ? 23.010  -0.229  57.882  1.00 41.77  ? 76  THR B CG2 1 
ATOM   4029  N  N   . TYR B  1 77  ? 24.038  3.619   59.898  1.00 36.15  ? 77  TYR B N   1 
ATOM   4030  C  CA  . TYR B  1 77  ? 24.536  4.496   60.958  1.00 34.32  ? 77  TYR B CA  1 
ATOM   4031  C  C   . TYR B  1 77  ? 23.435  4.657   61.949  1.00 32.60  ? 77  TYR B C   1 
ATOM   4032  O  O   . TYR B  1 77  ? 22.294  4.324   61.667  1.00 32.55  ? 77  TYR B O   1 
ATOM   4033  C  CB  . TYR B  1 77  ? 24.965  5.869   60.407  1.00 36.67  ? 77  TYR B CB  1 
ATOM   4034  C  CG  . TYR B  1 77  ? 23.850  6.800   59.989  1.00 29.46  ? 77  TYR B CG  1 
ATOM   4035  C  CD1 . TYR B  1 77  ? 23.299  6.743   58.694  1.00 20.26  ? 77  TYR B CD1 1 
ATOM   4036  C  CD2 . TYR B  1 77  ? 23.327  7.722   60.906  1.00 27.49  ? 77  TYR B CD2 1 
ATOM   4037  C  CE1 . TYR B  1 77  ? 22.259  7.581   58.333  1.00 20.60  ? 77  TYR B CE1 1 
ATOM   4038  C  CE2 . TYR B  1 77  ? 22.281  8.576   60.549  1.00 26.97  ? 77  TYR B CE2 1 
ATOM   4039  C  CZ  . TYR B  1 77  ? 21.746  8.487   59.265  1.00 24.01  ? 77  TYR B CZ  1 
ATOM   4040  O  OH  . TYR B  1 77  ? 20.653  9.251   58.921  1.00 27.91  ? 77  TYR B OH  1 
ATOM   4041  N  N   . ARG B  1 78  ? 23.774  5.097   63.138  1.00 30.71  ? 78  ARG B N   1 
ATOM   4042  C  CA  . ARG B  1 78  ? 22.776  5.291   64.145  1.00 36.73  ? 78  ARG B CA  1 
ATOM   4043  C  C   . ARG B  1 78  ? 22.967  6.717   64.521  1.00 40.33  ? 78  ARG B C   1 
ATOM   4044  O  O   . ARG B  1 78  ? 24.105  7.148   64.596  1.00 42.15  ? 78  ARG B O   1 
ATOM   4045  C  CB  . ARG B  1 78  ? 23.052  4.443   65.384  1.00 38.07  ? 78  ARG B CB  1 
ATOM   4046  C  CG  . ARG B  1 78  ? 22.748  2.955   65.244  1.00 48.71  ? 78  ARG B CG  1 
ATOM   4047  C  CD  . ARG B  1 78  ? 22.902  2.245   66.598  1.00 55.16  ? 78  ARG B CD  1 
ATOM   4048  N  NE  . ARG B  1 78  ? 21.670  1.675   67.157  1.00 57.34  ? 78  ARG B NE  1 
ATOM   4049  C  CZ  . ARG B  1 78  ? 21.445  0.372   67.273  1.00 55.32  ? 78  ARG B CZ  1 
ATOM   4050  N  NH1 . ARG B  1 78  ? 22.344  -0.504  66.858  1.00 57.84  ? 78  ARG B NH1 1 
ATOM   4051  N  NH2 . ARG B  1 78  ? 20.352  -0.054  67.867  1.00 56.45  ? 78  ARG B NH2 1 
ATOM   4052  N  N   . PHE B  1 79  ? 21.875  7.468   64.668  1.00 44.42  ? 79  PHE B N   1 
ATOM   4053  C  CA  . PHE B  1 79  ? 22.015  8.851   65.061  1.00 44.80  ? 79  PHE B CA  1 
ATOM   4054  C  C   . PHE B  1 79  ? 21.799  8.994   66.544  1.00 47.60  ? 79  PHE B C   1 
ATOM   4055  O  O   . PHE B  1 79  ? 22.761  9.130   67.261  1.00 58.00  ? 79  PHE B O   1 
ATOM   4056  C  CB  . PHE B  1 79  ? 21.175  9.836   64.269  1.00 41.63  ? 79  PHE B CB  1 
ATOM   4057  C  CG  . PHE B  1 79  ? 21.570  11.239  64.515  1.00 33.20  ? 79  PHE B CG  1 
ATOM   4058  C  CD1 . PHE B  1 79  ? 22.795  11.678  64.120  1.00 33.04  ? 79  PHE B CD1 1 
ATOM   4059  C  CD2 . PHE B  1 79  ? 20.786  12.066  65.267  1.00 34.46  ? 79  PHE B CD2 1 
ATOM   4060  C  CE1 . PHE B  1 79  ? 23.242  12.920  64.484  1.00 34.23  ? 79  PHE B CE1 1 
ATOM   4061  C  CE2 . PHE B  1 79  ? 21.226  13.313  65.635  1.00 33.04  ? 79  PHE B CE2 1 
ATOM   4062  C  CZ  . PHE B  1 79  ? 22.452  13.737  65.249  1.00 34.40  ? 79  PHE B CZ  1 
ATOM   4063  N  N   . PHE B  1 80  ? 20.598  9.002   67.070  1.00 42.53  ? 80  PHE B N   1 
ATOM   4064  C  CA  . PHE B  1 80  ? 20.582  9.085   68.529  1.00 42.16  ? 80  PHE B CA  1 
ATOM   4065  C  C   . PHE B  1 80  ? 19.784  7.850   68.895  1.00 45.30  ? 80  PHE B C   1 
ATOM   4066  O  O   . PHE B  1 80  ? 20.366  6.778   69.055  1.00 51.09  ? 80  PHE B O   1 
ATOM   4067  C  CB  . PHE B  1 80  ? 20.009  10.403  68.973  1.00 40.35  ? 80  PHE B CB  1 
ATOM   4068  C  CG  . PHE B  1 80  ? 19.567  10.425  70.390  1.00 43.66  ? 80  PHE B CG  1 
ATOM   4069  C  CD1 . PHE B  1 80  ? 20.491  10.354  71.418  1.00 45.77  ? 80  PHE B CD1 1 
ATOM   4070  C  CD2 . PHE B  1 80  ? 18.211  10.632  70.701  1.00 45.74  ? 80  PHE B CD2 1 
ATOM   4071  C  CE1 . PHE B  1 80  ? 20.085  10.503  72.761  1.00 46.43  ? 80  PHE B CE1 1 
ATOM   4072  C  CE2 . PHE B  1 80  ? 17.794  10.779  72.013  1.00 45.00  ? 80  PHE B CE2 1 
ATOM   4073  C  CZ  . PHE B  1 80  ? 18.740  10.718  73.053  1.00 45.45  ? 80  PHE B CZ  1 
ATOM   4074  N  N   . ASN B  1 81  ? 18.461  7.949   68.939  1.00 42.37  ? 81  ASN B N   1 
ATOM   4075  C  CA  . ASN B  1 81  ? 17.691  6.767   69.161  1.00 36.73  ? 81  ASN B CA  1 
ATOM   4076  C  C   . ASN B  1 81  ? 17.223  6.344   67.766  1.00 34.25  ? 81  ASN B C   1 
ATOM   4077  O  O   . ASN B  1 81  ? 16.356  5.506   67.654  1.00 33.96  ? 81  ASN B O   1 
ATOM   4078  C  CB  . ASN B  1 81  ? 16.571  6.951   70.215  1.00 40.68  ? 81  ASN B CB  1 
ATOM   4079  C  CG  . ASN B  1 81  ? 15.560  8.053   69.875  1.00 46.26  ? 81  ASN B CG  1 
ATOM   4080  O  OD1 . ASN B  1 81  ? 15.830  8.873   69.001  1.00 50.13  ? 81  ASN B OD1 1 
ATOM   4081  N  ND2 . ASN B  1 81  ? 14.429  8.061   70.612  1.00 54.74  ? 81  ASN B ND2 1 
ATOM   4082  N  N   . TYR B  1 82  ? 17.866  6.867   66.708  1.00 33.19  ? 82  TYR B N   1 
ATOM   4083  C  CA  . TYR B  1 82  ? 17.554  6.537   65.300  1.00 34.51  ? 82  TYR B CA  1 
ATOM   4084  C  C   . TYR B  1 82  ? 18.490  5.450   64.786  1.00 37.90  ? 82  TYR B C   1 
ATOM   4085  O  O   . TYR B  1 82  ? 19.575  5.320   65.325  1.00 41.81  ? 82  TYR B O   1 
ATOM   4086  C  CB  . TYR B  1 82  ? 17.723  7.778   64.383  1.00 37.06  ? 82  TYR B CB  1 
ATOM   4087  C  CG  . TYR B  1 82  ? 17.570  7.566   62.844  1.00 32.44  ? 82  TYR B CG  1 
ATOM   4088  C  CD1 . TYR B  1 82  ? 16.337  7.468   62.262  1.00 29.55  ? 82  TYR B CD1 1 
ATOM   4089  C  CD2 . TYR B  1 82  ? 18.672  7.472   62.001  1.00 37.13  ? 82  TYR B CD2 1 
ATOM   4090  C  CE1 . TYR B  1 82  ? 16.191  7.276   60.884  1.00 33.81  ? 82  TYR B CE1 1 
ATOM   4091  C  CE2 . TYR B  1 82  ? 18.533  7.275   60.610  1.00 37.82  ? 82  TYR B CE2 1 
ATOM   4092  C  CZ  . TYR B  1 82  ? 17.279  7.172   60.068  1.00 37.02  ? 82  TYR B CZ  1 
ATOM   4093  O  OH  . TYR B  1 82  ? 17.086  6.912   58.723  1.00 40.68  ? 82  TYR B OH  1 
ATOM   4094  N  N   . SER B  1 83  ? 18.108  4.761   63.694  1.00 37.27  ? 83  SER B N   1 
ATOM   4095  C  CA  . SER B  1 83  ? 18.894  3.678   63.056  1.00 38.63  ? 83  SER B CA  1 
ATOM   4096  C  C   . SER B  1 83  ? 18.590  3.621   61.572  1.00 36.24  ? 83  SER B C   1 
ATOM   4097  O  O   . SER B  1 83  ? 17.495  3.272   61.142  1.00 40.63  ? 83  SER B O   1 
ATOM   4098  C  CB  . SER B  1 83  ? 18.554  2.316   63.632  1.00 44.56  ? 83  SER B CB  1 
ATOM   4099  O  OG  . SER B  1 83  ? 18.572  2.350   65.051  1.00 62.30  ? 83  SER B OG  1 
ATOM   4100  N  N   . SER B  1 84  ? 19.585  3.898   60.777  1.00 31.15  ? 84  SER B N   1 
ATOM   4101  C  CA  . SER B  1 84  ? 19.384  3.938   59.365  1.00 29.17  ? 84  SER B CA  1 
ATOM   4102  C  C   . SER B  1 84  ? 18.939  2.621   58.786  1.00 27.00  ? 84  SER B C   1 
ATOM   4103  O  O   . SER B  1 84  ? 19.056  1.585   59.391  1.00 25.44  ? 84  SER B O   1 
ATOM   4104  C  CB  . SER B  1 84  ? 20.695  4.296   58.718  1.00 34.12  ? 84  SER B CB  1 
ATOM   4105  O  OG  . SER B  1 84  ? 21.587  3.212   58.895  1.00 38.85  ? 84  SER B OG  1 
ATOM   4106  N  N   . GLY B  1 85  ? 18.451  2.676   57.565  1.00 26.99  ? 85  GLY B N   1 
ATOM   4107  C  CA  . GLY B  1 85  ? 18.097  1.455   56.882  1.00 23.51  ? 85  GLY B CA  1 
ATOM   4108  C  C   . GLY B  1 85  ? 19.429  1.092   56.265  1.00 26.11  ? 85  GLY B C   1 
ATOM   4109  O  O   . GLY B  1 85  ? 20.466  1.575   56.743  1.00 26.41  ? 85  GLY B O   1 
ATOM   4110  N  N   . PHE B  1 86  ? 19.436  0.370   55.159  1.00 21.87  ? 86  PHE B N   1 
ATOM   4111  C  CA  . PHE B  1 86  ? 20.691  -0.019  54.569  1.00 26.70  ? 86  PHE B CA  1 
ATOM   4112  C  C   . PHE B  1 86  ? 20.987  0.864   53.402  1.00 28.59  ? 86  PHE B C   1 
ATOM   4113  O  O   . PHE B  1 86  ? 20.342  0.803   52.368  1.00 30.14  ? 86  PHE B O   1 
ATOM   4114  C  CB  . PHE B  1 86  ? 20.620  -1.488  54.195  1.00 33.65  ? 86  PHE B CB  1 
ATOM   4115  C  CG  . PHE B  1 86  ? 20.097  -2.327  55.321  1.00 44.01  ? 86  PHE B CG  1 
ATOM   4116  C  CD1 . PHE B  1 86  ? 20.932  -2.680  56.375  1.00 52.33  ? 86  PHE B CD1 1 
ATOM   4117  C  CD2 . PHE B  1 86  ? 18.753  -2.647  55.412  1.00 47.57  ? 86  PHE B CD2 1 
ATOM   4118  C  CE1 . PHE B  1 86  ? 20.425  -3.339  57.523  1.00 53.27  ? 86  PHE B CE1 1 
ATOM   4119  C  CE2 . PHE B  1 86  ? 18.239  -3.303  56.548  1.00 52.91  ? 86  PHE B CE2 1 
ATOM   4120  C  CZ  . PHE B  1 86  ? 19.078  -3.643  57.601  1.00 54.86  ? 86  PHE B CZ  1 
ATOM   4121  N  N   . ILE B  1 87  ? 22.001  1.683   53.582  1.00 28.24  ? 87  ILE B N   1 
ATOM   4122  C  CA  . ILE B  1 87  ? 22.396  2.638   52.578  1.00 25.17  ? 87  ILE B CA  1 
ATOM   4123  C  C   . ILE B  1 87  ? 23.301  1.970   51.565  1.00 28.24  ? 87  ILE B C   1 
ATOM   4124  O  O   . ILE B  1 87  ? 24.222  1.256   51.927  1.00 30.98  ? 87  ILE B O   1 
ATOM   4125  C  CB  . ILE B  1 87  ? 23.111  3.819   53.257  1.00 20.28  ? 87  ILE B CB  1 
ATOM   4126  C  CG1 . ILE B  1 87  ? 22.222  4.383   54.352  1.00 13.79  ? 87  ILE B CG1 1 
ATOM   4127  C  CG2 . ILE B  1 87  ? 23.341  4.899   52.302  1.00 15.86  ? 87  ILE B CG2 1 
ATOM   4128  C  CD1 . ILE B  1 87  ? 22.849  5.442   55.158  1.00 18.76  ? 87  ILE B CD1 1 
ATOM   4129  N  N   . HIS B  1 88  ? 23.056  2.205   50.286  1.00 28.37  ? 88  HIS B N   1 
ATOM   4130  C  CA  . HIS B  1 88  ? 23.873  1.596   49.256  1.00 29.22  ? 88  HIS B CA  1 
ATOM   4131  C  C   . HIS B  1 88  ? 24.474  2.636   48.345  1.00 28.14  ? 88  HIS B C   1 
ATOM   4132  O  O   . HIS B  1 88  ? 23.759  3.513   47.897  1.00 30.11  ? 88  HIS B O   1 
ATOM   4133  C  CB  . HIS B  1 88  ? 23.032  0.681   48.382  1.00 33.58  ? 88  HIS B CB  1 
ATOM   4134  C  CG  . HIS B  1 88  ? 22.416  -0.456  49.107  1.00 37.12  ? 88  HIS B CG  1 
ATOM   4135  N  ND1 . HIS B  1 88  ? 21.165  -0.376  49.688  1.00 43.24  ? 88  HIS B ND1 1 
ATOM   4136  C  CD2 . HIS B  1 88  ? 22.859  -1.715  49.335  1.00 37.28  ? 88  HIS B CD2 1 
ATOM   4137  C  CE1 . HIS B  1 88  ? 20.855  -1.538  50.233  1.00 39.23  ? 88  HIS B CE1 1 
ATOM   4138  N  NE2 . HIS B  1 88  ? 21.865  -2.365  50.035  1.00 44.84  ? 88  HIS B NE2 1 
ATOM   4139  N  N   . HIS B  1 89  ? 25.736  2.444   47.958  1.00 26.91  ? 89  HIS B N   1 
ATOM   4140  C  CA  . HIS B  1 89  ? 26.470  3.339   47.075  1.00 26.39  ? 89  HIS B CA  1 
ATOM   4141  C  C   . HIS B  1 89  ? 27.282  2.493   46.095  1.00 30.19  ? 89  HIS B C   1 
ATOM   4142  O  O   . HIS B  1 89  ? 28.209  1.759   46.463  1.00 33.14  ? 89  HIS B O   1 
ATOM   4143  C  CB  . HIS B  1 89  ? 27.427  4.241   47.887  1.00 25.75  ? 89  HIS B CB  1 
ATOM   4144  C  CG  . HIS B  1 89  ? 26.747  5.216   48.812  1.00 26.13  ? 89  HIS B CG  1 
ATOM   4145  N  ND1 . HIS B  1 89  ? 25.988  6.279   48.358  1.00 26.84  ? 89  HIS B ND1 1 
ATOM   4146  C  CD2 . HIS B  1 89  ? 26.750  5.315   50.167  1.00 27.11  ? 89  HIS B CD2 1 
ATOM   4147  C  CE1 . HIS B  1 89  ? 25.555  6.982   49.393  1.00 31.51  ? 89  HIS B CE1 1 
ATOM   4148  N  NE2 . HIS B  1 89  ? 26.003  6.420   50.503  1.00 30.63  ? 89  HIS B NE2 1 
ATOM   4149  N  N   . THR B  1 90  ? 26.947  2.621   44.835  1.00 31.29  ? 90  THR B N   1 
ATOM   4150  C  CA  . THR B  1 90  ? 27.650  1.879   43.822  1.00 35.39  ? 90  THR B CA  1 
ATOM   4151  C  C   . THR B  1 90  ? 28.052  2.868   42.750  1.00 41.05  ? 90  THR B C   1 
ATOM   4152  O  O   . THR B  1 90  ? 27.272  3.732   42.360  1.00 41.49  ? 90  THR B O   1 
ATOM   4153  C  CB  . THR B  1 90  ? 26.734  0.842   43.221  1.00 35.32  ? 90  THR B CB  1 
ATOM   4154  O  OG1 . THR B  1 90  ? 26.306  -0.034  44.266  1.00 37.12  ? 90  THR B OG1 1 
ATOM   4155  C  CG2 . THR B  1 90  ? 27.430  0.070   42.110  1.00 26.32  ? 90  THR B CG2 1 
ATOM   4156  N  N   . THR B  1 91  ? 29.244  2.676   42.216  1.00 44.17  ? 91  THR B N   1 
ATOM   4157  C  CA  . THR B  1 91  ? 29.792  3.565   41.217  1.00 41.37  ? 91  THR B CA  1 
ATOM   4158  C  C   . THR B  1 91  ? 29.904  2.890   39.876  1.00 40.72  ? 91  THR B C   1 
ATOM   4159  O  O   . THR B  1 91  ? 30.540  1.866   39.744  1.00 43.19  ? 91  THR B O   1 
ATOM   4160  C  CB  . THR B  1 91  ? 31.173  4.018   41.663  1.00 43.63  ? 91  THR B CB  1 
ATOM   4161  O  OG1 . THR B  1 91  ? 31.112  4.532   43.012  1.00 47.04  ? 91  THR B OG1 1 
ATOM   4162  C  CG2 . THR B  1 91  ? 31.688  5.036   40.756  1.00 41.67  ? 91  THR B CG2 1 
ATOM   4163  N  N   . ILE B  1 92  ? 29.264  3.444   38.872  1.00 41.75  ? 92  ILE B N   1 
ATOM   4164  C  CA  . ILE B  1 92  ? 29.333  2.857   37.570  1.00 43.40  ? 92  ILE B CA  1 
ATOM   4165  C  C   . ILE B  1 92  ? 30.412  3.583   36.826  1.00 45.30  ? 92  ILE B C   1 
ATOM   4166  O  O   . ILE B  1 92  ? 30.382  4.793   36.748  1.00 44.06  ? 92  ILE B O   1 
ATOM   4167  C  CB  . ILE B  1 92  ? 28.041  3.056   36.870  1.00 41.63  ? 92  ILE B CB  1 
ATOM   4168  C  CG1 . ILE B  1 92  ? 26.925  2.425   37.662  1.00 43.70  ? 92  ILE B CG1 1 
ATOM   4169  C  CG2 . ILE B  1 92  ? 28.061  2.373   35.576  1.00 42.74  ? 92  ILE B CG2 1 
ATOM   4170  C  CD1 . ILE B  1 92  ? 25.622  2.639   37.012  1.00 49.73  ? 92  ILE B CD1 1 
ATOM   4171  N  N   . ARG B  1 93  ? 31.351  2.859   36.249  1.00 51.02  ? 93  ARG B N   1 
ATOM   4172  C  CA  . ARG B  1 93  ? 32.427  3.524   35.528  1.00 58.21  ? 93  ARG B CA  1 
ATOM   4173  C  C   . ARG B  1 93  ? 32.481  3.322   34.032  1.00 60.74  ? 93  ARG B C   1 
ATOM   4174  O  O   . ARG B  1 93  ? 31.775  2.478   33.478  1.00 62.93  ? 93  ARG B O   1 
ATOM   4175  C  CB  . ARG B  1 93  ? 33.769  3.102   36.082  1.00 61.28  ? 93  ARG B CB  1 
ATOM   4176  C  CG  . ARG B  1 93  ? 34.007  3.619   37.423  1.00 67.71  ? 93  ARG B CG  1 
ATOM   4177  C  CD  . ARG B  1 93  ? 34.974  2.728   38.141  1.00 81.37  ? 93  ARG B CD  1 
ATOM   4178  N  NE  . ARG B  1 93  ? 35.152  3.192   39.510  1.00 93.88  ? 93  ARG B NE  1 
ATOM   4179  C  CZ  . ARG B  1 93  ? 35.644  4.389   39.821  1.00 101.81 ? 93  ARG B CZ  1 
ATOM   4180  N  NH1 . ARG B  1 93  ? 36.021  5.234   38.849  1.00 104.52 ? 93  ARG B NH1 1 
ATOM   4181  N  NH2 . ARG B  1 93  ? 35.698  4.769   41.100  1.00 106.27 ? 93  ARG B NH2 1 
ATOM   4182  N  N   . LYS B  1 94  ? 33.368  4.094   33.404  1.00 60.81  ? 94  LYS B N   1 
ATOM   4183  C  CA  . LYS B  1 94  ? 33.613  4.030   31.978  1.00 60.69  ? 94  LYS B CA  1 
ATOM   4184  C  C   . LYS B  1 94  ? 32.367  4.120   31.081  1.00 58.62  ? 94  LYS B C   1 
ATOM   4185  O  O   . LYS B  1 94  ? 32.185  3.322   30.174  1.00 64.12  ? 94  LYS B O   1 
ATOM   4186  C  CB  . LYS B  1 94  ? 34.424  2.770   31.664  1.00 64.47  ? 94  LYS B CB  1 
ATOM   4187  C  CG  . LYS B  1 94  ? 35.753  2.699   32.391  1.00 76.45  ? 94  LYS B CG  1 
ATOM   4188  C  CD  . LYS B  1 94  ? 36.573  1.431   32.032  1.00 85.85  ? 94  LYS B CD  1 
ATOM   4189  C  CE  . LYS B  1 94  ? 36.877  0.521   33.270  1.00 94.49  ? 94  LYS B CE  1 
ATOM   4190  N  NZ  . LYS B  1 94  ? 37.766  1.059   34.401  1.00 100.82 ? 94  LYS B NZ  1 
ATOM   4191  N  N   . LEU B  1 95  ? 31.495  5.077   31.335  1.00 53.99  ? 95  LEU B N   1 
ATOM   4192  C  CA  . LEU B  1 95  ? 30.328  5.231   30.499  1.00 51.17  ? 95  LEU B CA  1 
ATOM   4193  C  C   . LEU B  1 95  ? 30.732  5.933   29.190  1.00 53.65  ? 95  LEU B C   1 
ATOM   4194  O  O   . LEU B  1 95  ? 31.826  6.471   29.067  1.00 54.62  ? 95  LEU B O   1 
ATOM   4195  C  CB  . LEU B  1 95  ? 29.306  6.077   31.225  1.00 48.73  ? 95  LEU B CB  1 
ATOM   4196  C  CG  . LEU B  1 95  ? 29.004  5.592   32.621  1.00 44.95  ? 95  LEU B CG  1 
ATOM   4197  C  CD1 . LEU B  1 95  ? 28.050  6.553   33.324  1.00 45.75  ? 95  LEU B CD1 1 
ATOM   4198  C  CD2 . LEU B  1 95  ? 28.417  4.244   32.473  1.00 42.92  ? 95  LEU B CD2 1 
ATOM   4199  N  N   . LYS B  1 96  ? 29.872  5.890   28.188  1.00 57.30  ? 96  LYS B N   1 
ATOM   4200  C  CA  . LYS B  1 96  ? 30.164  6.566   26.941  1.00 56.89  ? 96  LYS B CA  1 
ATOM   4201  C  C   . LYS B  1 96  ? 29.566  7.940   27.153  1.00 53.64  ? 96  LYS B C   1 
ATOM   4202  O  O   . LYS B  1 96  ? 28.606  8.083   27.901  1.00 52.71  ? 96  LYS B O   1 
ATOM   4203  C  CB  . LYS B  1 96  ? 29.480  5.849   25.785  1.00 66.92  ? 96  LYS B CB  1 
ATOM   4204  C  CG  . LYS B  1 96  ? 30.375  4.834   25.061  1.00 82.04  ? 96  LYS B CG  1 
ATOM   4205  C  CD  . LYS B  1 96  ? 30.201  3.383   25.567  1.00 94.54  ? 96  LYS B CD  1 
ATOM   4206  C  CE  . LYS B  1 96  ? 28.920  2.686   25.021  1.00 103.91 ? 96  LYS B CE  1 
ATOM   4207  N  NZ  . LYS B  1 96  ? 28.671  1.277   25.552  1.00 116.12 ? 96  LYS B NZ  1 
ATOM   4208  N  N   . TYR B  1 97  ? 30.143  8.968   26.559  1.00 51.16  ? 97  TYR B N   1 
ATOM   4209  C  CA  . TYR B  1 97  ? 29.580  10.295  26.762  1.00 52.06  ? 97  TYR B CA  1 
ATOM   4210  C  C   . TYR B  1 97  ? 28.308  10.463  25.977  1.00 52.32  ? 97  TYR B C   1 
ATOM   4211  O  O   . TYR B  1 97  ? 28.087  9.767   24.996  1.00 53.26  ? 97  TYR B O   1 
ATOM   4212  C  CB  . TYR B  1 97  ? 30.537  11.371  26.289  1.00 52.78  ? 97  TYR B CB  1 
ATOM   4213  C  CG  . TYR B  1 97  ? 31.763  11.559  27.125  1.00 53.95  ? 97  TYR B CG  1 
ATOM   4214  C  CD1 . TYR B  1 97  ? 31.727  12.342  28.292  1.00 53.55  ? 97  TYR B CD1 1 
ATOM   4215  C  CD2 . TYR B  1 97  ? 32.992  11.046  26.709  1.00 51.11  ? 97  TYR B CD2 1 
ATOM   4216  C  CE1 . TYR B  1 97  ? 32.901  12.619  29.021  1.00 48.02  ? 97  TYR B CE1 1 
ATOM   4217  C  CE2 . TYR B  1 97  ? 34.165  11.326  27.423  1.00 50.18  ? 97  TYR B CE2 1 
ATOM   4218  C  CZ  . TYR B  1 97  ? 34.112  12.115  28.565  1.00 48.17  ? 97  TYR B CZ  1 
ATOM   4219  O  OH  . TYR B  1 97  ? 35.281  12.477  29.174  1.00 47.04  ? 97  TYR B OH  1 
ATOM   4220  N  N   . ASN B  1 98  ? 27.472  11.388  26.412  1.00 53.51  ? 98  ASN B N   1 
ATOM   4221  C  CA  . ASN B  1 98  ? 26.239  11.675  25.697  1.00 58.31  ? 98  ASN B CA  1 
ATOM   4222  C  C   . ASN B  1 98  ? 25.448  10.418  25.326  1.00 57.83  ? 98  ASN B C   1 
ATOM   4223  O  O   . ASN B  1 98  ? 25.165  10.166  24.154  1.00 62.50  ? 98  ASN B O   1 
ATOM   4224  C  CB  . ASN B  1 98  ? 26.597  12.466  24.432  1.00 61.30  ? 98  ASN B CB  1 
ATOM   4225  C  CG  . ASN B  1 98  ? 25.467  13.356  23.942  1.00 64.85  ? 98  ASN B CG  1 
ATOM   4226  O  OD1 . ASN B  1 98  ? 24.739  13.996  24.727  1.00 68.78  ? 98  ASN B OD1 1 
ATOM   4227  N  ND2 . ASN B  1 98  ? 25.342  13.437  22.624  1.00 70.58  ? 98  ASN B ND2 1 
ATOM   4228  N  N   . THR B  1 99  ? 25.066  9.637   26.322  1.00 57.02  ? 99  THR B N   1 
ATOM   4229  C  CA  . THR B  1 99  ? 24.331  8.420   26.062  1.00 53.44  ? 99  THR B CA  1 
ATOM   4230  C  C   . THR B  1 99  ? 23.286  8.221   27.140  1.00 52.76  ? 99  THR B C   1 
ATOM   4231  O  O   . THR B  1 99  ? 23.493  8.630   28.296  1.00 50.49  ? 99  THR B O   1 
ATOM   4232  C  CB  . THR B  1 99  ? 25.274  7.263   26.081  1.00 51.27  ? 99  THR B CB  1 
ATOM   4233  O  OG1 . THR B  1 99  ? 26.298  7.483   25.110  1.00 50.66  ? 99  THR B OG1 1 
ATOM   4234  C  CG2 . THR B  1 99  ? 24.542  6.005   25.760  1.00 57.63  ? 99  THR B CG2 1 
ATOM   4235  N  N   . LYS B  1 100 ? 22.121  7.712   26.748  1.00 52.40  ? 100 LYS B N   1 
ATOM   4236  C  CA  . LYS B  1 100 ? 21.095  7.461   27.741  1.00 50.76  ? 100 LYS B CA  1 
ATOM   4237  C  C   . LYS B  1 100 ? 21.378  6.085   28.275  1.00 47.19  ? 100 LYS B C   1 
ATOM   4238  O  O   . LYS B  1 100 ? 21.651  5.151   27.524  1.00 43.55  ? 100 LYS B O   1 
ATOM   4239  C  CB  . LYS B  1 100 ? 19.693  7.483   27.151  1.00 52.30  ? 100 LYS B CB  1 
ATOM   4240  C  CG  . LYS B  1 100 ? 18.595  7.326   28.195  1.00 54.04  ? 100 LYS B CG  1 
ATOM   4241  C  CD  . LYS B  1 100 ? 17.204  7.395   27.560  1.00 60.48  ? 100 LYS B CD  1 
ATOM   4242  C  CE  . LYS B  1 100 ? 16.103  7.722   28.588  1.00 64.24  ? 100 LYS B CE  1 
ATOM   4243  N  NZ  . LYS B  1 100 ? 14.729  7.838   27.985  1.00 71.73  ? 100 LYS B NZ  1 
ATOM   4244  N  N   . TYR B  1 101 ? 21.341  5.971   29.583  1.00 43.62  ? 101 TYR B N   1 
ATOM   4245  C  CA  . TYR B  1 101 ? 21.570  4.711   30.205  1.00 42.97  ? 101 TYR B CA  1 
ATOM   4246  C  C   . TYR B  1 101 ? 20.368  4.377   31.046  1.00 49.00  ? 101 TYR B C   1 
ATOM   4247  O  O   . TYR B  1 101 ? 19.641  5.272   31.533  1.00 49.01  ? 101 TYR B O   1 
ATOM   4248  C  CB  . TYR B  1 101 ? 22.753  4.809   31.113  1.00 36.90  ? 101 TYR B CB  1 
ATOM   4249  C  CG  . TYR B  1 101 ? 24.008  4.607   30.408  1.00 31.66  ? 101 TYR B CG  1 
ATOM   4250  C  CD1 . TYR B  1 101 ? 24.538  3.342   30.268  1.00 26.35  ? 101 TYR B CD1 1 
ATOM   4251  C  CD2 . TYR B  1 101 ? 24.686  5.681   29.861  1.00 38.62  ? 101 TYR B CD2 1 
ATOM   4252  C  CE1 . TYR B  1 101 ? 25.752  3.139   29.581  1.00 35.18  ? 101 TYR B CE1 1 
ATOM   4253  C  CE2 . TYR B  1 101 ? 25.906  5.503   29.163  1.00 35.40  ? 101 TYR B CE2 1 
ATOM   4254  C  CZ  . TYR B  1 101 ? 26.424  4.230   29.031  1.00 35.31  ? 101 TYR B CZ  1 
ATOM   4255  O  OH  . TYR B  1 101 ? 27.579  4.024   28.338  1.00 39.96  ? 101 TYR B OH  1 
ATOM   4256  N  N   . TYR B  1 102 ? 20.186  3.083   31.257  1.00 48.35  ? 102 TYR B N   1 
ATOM   4257  C  CA  . TYR B  1 102 ? 19.102  2.613   32.076  1.00 50.25  ? 102 TYR B CA  1 
ATOM   4258  C  C   . TYR B  1 102 ? 19.790  1.874   33.189  1.00 48.58  ? 102 TYR B C   1 
ATOM   4259  O  O   . TYR B  1 102 ? 20.799  1.191   32.959  1.00 48.38  ? 102 TYR B O   1 
ATOM   4260  C  CB  . TYR B  1 102 ? 18.235  1.619   31.312  1.00 57.78  ? 102 TYR B CB  1 
ATOM   4261  C  CG  . TYR B  1 102 ? 17.272  2.244   30.358  1.00 57.07  ? 102 TYR B CG  1 
ATOM   4262  C  CD1 . TYR B  1 102 ? 16.146  2.900   30.826  1.00 57.69  ? 102 TYR B CD1 1 
ATOM   4263  C  CD2 . TYR B  1 102 ? 17.500  2.197   28.989  1.00 59.42  ? 102 TYR B CD2 1 
ATOM   4264  C  CE1 . TYR B  1 102 ? 15.258  3.512   29.952  1.00 65.63  ? 102 TYR B CE1 1 
ATOM   4265  C  CE2 . TYR B  1 102 ? 16.625  2.809   28.091  1.00 63.84  ? 102 TYR B CE2 1 
ATOM   4266  C  CZ  . TYR B  1 102 ? 15.498  3.477   28.570  1.00 66.62  ? 102 TYR B CZ  1 
ATOM   4267  O  OH  . TYR B  1 102 ? 14.648  4.159   27.688  1.00 68.92  ? 102 TYR B OH  1 
ATOM   4268  N  N   . TYR B  1 103 ? 19.274  2.033   34.394  1.00 44.80  ? 103 TYR B N   1 
ATOM   4269  C  CA  . TYR B  1 103 ? 19.834  1.331   35.518  1.00 43.79  ? 103 TYR B CA  1 
ATOM   4270  C  C   . TYR B  1 103 ? 18.668  0.840   36.381  1.00 48.79  ? 103 TYR B C   1 
ATOM   4271  O  O   . TYR B  1 103 ? 17.579  1.459   36.434  1.00 43.20  ? 103 TYR B O   1 
ATOM   4272  C  CB  . TYR B  1 103 ? 20.857  2.198   36.291  1.00 36.28  ? 103 TYR B CB  1 
ATOM   4273  C  CG  . TYR B  1 103 ? 20.288  3.339   37.107  1.00 29.73  ? 103 TYR B CG  1 
ATOM   4274  C  CD1 . TYR B  1 103 ? 19.833  3.126   38.395  1.00 34.48  ? 103 TYR B CD1 1 
ATOM   4275  C  CD2 . TYR B  1 103 ? 20.212  4.620   36.606  1.00 28.43  ? 103 TYR B CD2 1 
ATOM   4276  C  CE1 . TYR B  1 103 ? 19.311  4.158   39.179  1.00 33.21  ? 103 TYR B CE1 1 
ATOM   4277  C  CE2 . TYR B  1 103 ? 19.682  5.676   37.384  1.00 35.20  ? 103 TYR B CE2 1 
ATOM   4278  C  CZ  . TYR B  1 103 ? 19.235  5.426   38.678  1.00 35.85  ? 103 TYR B CZ  1 
ATOM   4279  O  OH  . TYR B  1 103 ? 18.711  6.425   39.475  1.00 36.62  ? 103 TYR B OH  1 
ATOM   4280  N  N   . GLU B  1 104 ? 18.857  -0.363  36.912  1.00 50.89  ? 104 GLU B N   1 
ATOM   4281  C  CA  . GLU B  1 104 ? 17.883  -1.003  37.778  1.00 49.27  ? 104 GLU B CA  1 
ATOM   4282  C  C   . GLU B  1 104 ? 18.578  -1.263  39.071  1.00 46.61  ? 104 GLU B C   1 
ATOM   4283  O  O   . GLU B  1 104 ? 19.732  -1.700  39.109  1.00 43.27  ? 104 GLU B O   1 
ATOM   4284  C  CB  . GLU B  1 104 ? 17.392  -2.300  37.202  1.00 52.04  ? 104 GLU B CB  1 
ATOM   4285  C  CG  . GLU B  1 104 ? 16.534  -2.113  36.007  1.00 57.65  ? 104 GLU B CG  1 
ATOM   4286  C  CD  . GLU B  1 104 ? 16.078  -3.443  35.422  1.00 64.90  ? 104 GLU B CD  1 
ATOM   4287  O  OE1 . GLU B  1 104 ? 16.940  -4.287  35.025  1.00 61.44  ? 104 GLU B OE1 1 
ATOM   4288  O  OE2 . GLU B  1 104 ? 14.838  -3.629  35.355  1.00 70.01  ? 104 GLU B OE2 1 
ATOM   4289  N  N   . VAL B  1 105 ? 17.820  -1.064  40.121  1.00 44.75  ? 105 VAL B N   1 
ATOM   4290  C  CA  . VAL B  1 105 ? 18.314  -1.164  41.453  1.00 47.18  ? 105 VAL B CA  1 
ATOM   4291  C  C   . VAL B  1 105 ? 17.310  -1.989  42.277  1.00 49.29  ? 105 VAL B C   1 
ATOM   4292  O  O   . VAL B  1 105 ? 16.127  -1.925  42.033  1.00 52.68  ? 105 VAL B O   1 
ATOM   4293  C  CB  . VAL B  1 105 ? 18.495  0.275   41.917  1.00 44.56  ? 105 VAL B CB  1 
ATOM   4294  C  CG1 . VAL B  1 105 ? 17.460  0.670   42.886  1.00 46.30  ? 105 VAL B CG1 1 
ATOM   4295  C  CG2 . VAL B  1 105 ? 19.881  0.508   42.423  1.00 52.06  ? 105 VAL B CG2 1 
ATOM   4296  N  N   . GLY B  1 106 ? 17.789  -2.799  43.213  1.00 53.19  ? 106 GLY B N   1 
ATOM   4297  C  CA  . GLY B  1 106 ? 16.907  -3.659  43.993  1.00 55.52  ? 106 GLY B CA  1 
ATOM   4298  C  C   . GLY B  1 106 ? 16.736  -5.008  43.303  1.00 57.64  ? 106 GLY B C   1 
ATOM   4299  O  O   . GLY B  1 106 ? 15.647  -5.576  43.280  1.00 58.44  ? 106 GLY B O   1 
ATOM   4300  N  N   . LEU B  1 107 ? 17.836  -5.559  42.802  1.00 59.22  ? 107 LEU B N   1 
ATOM   4301  C  CA  . LEU B  1 107 ? 17.798  -6.808  42.063  1.00 59.26  ? 107 LEU B CA  1 
ATOM   4302  C  C   . LEU B  1 107 ? 17.290  -8.037  42.788  1.00 64.54  ? 107 LEU B C   1 
ATOM   4303  O  O   . LEU B  1 107 ? 16.721  -8.907  42.144  1.00 70.15  ? 107 LEU B O   1 
ATOM   4304  C  CB  . LEU B  1 107 ? 19.161  -7.137  41.472  1.00 57.71  ? 107 LEU B CB  1 
ATOM   4305  C  CG  . LEU B  1 107 ? 19.980  -6.060  40.778  1.00 56.22  ? 107 LEU B CG  1 
ATOM   4306  C  CD1 . LEU B  1 107 ? 21.169  -6.707  40.078  1.00 59.62  ? 107 LEU B CD1 1 
ATOM   4307  C  CD2 . LEU B  1 107 ? 19.135  -5.305  39.778  1.00 60.56  ? 107 LEU B CD2 1 
ATOM   4308  N  N   . ARG B  1 108 ? 17.529  -8.153  44.096  1.00 67.19  ? 108 ARG B N   1 
ATOM   4309  C  CA  . ARG B  1 108 ? 17.076  -9.336  44.824  1.00 69.59  ? 108 ARG B CA  1 
ATOM   4310  C  C   . ARG B  1 108 ? 15.574  -9.438  44.959  1.00 69.71  ? 108 ARG B C   1 
ATOM   4311  O  O   . ARG B  1 108 ? 14.989  -10.458 44.637  1.00 71.69  ? 108 ARG B O   1 
ATOM   4312  C  CB  . ARG B  1 108 ? 17.714  -9.434  46.200  1.00 74.91  ? 108 ARG B CB  1 
ATOM   4313  C  CG  . ARG B  1 108 ? 18.914  -10.372 46.270  1.00 86.65  ? 108 ARG B CG  1 
ATOM   4314  C  CD  . ARG B  1 108 ? 19.522  -10.471 47.705  1.00 96.57  ? 108 ARG B CD  1 
ATOM   4315  N  NE  . ARG B  1 108 ? 18.765  -11.293 48.676  1.00 102.18 ? 108 ARG B NE  1 
ATOM   4316  C  CZ  . ARG B  1 108 ? 17.686  -10.900 49.365  1.00 103.22 ? 108 ARG B CZ  1 
ATOM   4317  N  NH1 . ARG B  1 108 ? 17.181  -9.681  49.206  1.00 103.13 ? 108 ARG B NH1 1 
ATOM   4318  N  NH2 . ARG B  1 108 ? 17.127  -11.719 50.258  1.00 100.08 ? 108 ARG B NH2 1 
ATOM   4319  N  N   . ASN B  1 109 ? 14.926  -8.390  45.429  1.00 71.13  ? 109 ASN B N   1 
ATOM   4320  C  CA  . ASN B  1 109 ? 13.496  -8.486  45.569  1.00 72.36  ? 109 ASN B CA  1 
ATOM   4321  C  C   . ASN B  1 109 ? 12.705  -7.580  44.638  1.00 71.51  ? 109 ASN B C   1 
ATOM   4322  O  O   . ASN B  1 109 ? 12.340  -7.981  43.525  1.00 73.37  ? 109 ASN B O   1 
ATOM   4323  C  CB  . ASN B  1 109 ? 13.090  -8.357  47.035  1.00 74.84  ? 109 ASN B CB  1 
ATOM   4324  C  CG  . ASN B  1 109 ? 13.547  -9.550  47.856  1.00 81.97  ? 109 ASN B CG  1 
ATOM   4325  O  OD1 . ASN B  1 109 ? 14.603  -9.474  48.490  1.00 83.53  ? 109 ASN B OD1 1 
ATOM   4326  N  ND2 . ASN B  1 109 ? 12.764  -10.645 47.810  1.00 87.02  ? 109 ASN B ND2 1 
ATOM   4327  N  N   . THR B  1 110 ? 12.470  -6.348  45.056  1.00 69.38  ? 110 THR B N   1 
ATOM   4328  C  CA  . THR B  1 110 ? 11.696  -5.425  44.246  1.00 62.43  ? 110 THR B CA  1 
ATOM   4329  C  C   . THR B  1 110 ? 12.612  -4.540  43.436  1.00 58.77  ? 110 THR B C   1 
ATOM   4330  O  O   . THR B  1 110 ? 13.301  -3.700  43.980  1.00 62.59  ? 110 THR B O   1 
ATOM   4331  C  CB  . THR B  1 110 ? 10.817  -4.575  45.149  1.00 61.58  ? 110 THR B CB  1 
ATOM   4332  O  OG1 . THR B  1 110 ? 10.041  -5.420  46.024  1.00 59.72  ? 110 THR B OG1 1 
ATOM   4333  C  CG2 . THR B  1 110 ? 9.912   -3.725  44.324  1.00 66.35  ? 110 THR B CG2 1 
ATOM   4334  N  N   . THR B  1 111 ? 12.654  -4.756  42.133  1.00 56.56  ? 111 THR B N   1 
ATOM   4335  C  CA  . THR B  1 111 ? 13.510  -3.964  41.236  1.00 55.80  ? 111 THR B CA  1 
ATOM   4336  C  C   . THR B  1 111 ? 12.885  -2.641  40.736  1.00 54.27  ? 111 THR B C   1 
ATOM   4337  O  O   . THR B  1 111 ? 11.672  -2.582  40.487  1.00 60.25  ? 111 THR B O   1 
ATOM   4338  C  CB  . THR B  1 111 ? 13.892  -4.818  40.020  1.00 56.33  ? 111 THR B CB  1 
ATOM   4339  O  OG1 . THR B  1 111 ? 14.766  -5.884  40.432  1.00 57.83  ? 111 THR B OG1 1 
ATOM   4340  C  CG2 . THR B  1 111 ? 14.553  -3.973  38.945  1.00 55.69  ? 111 THR B CG2 1 
ATOM   4341  N  N   . ARG B  1 112 ? 13.681  -1.575  40.634  1.00 48.36  ? 112 ARG B N   1 
ATOM   4342  C  CA  . ARG B  1 112 ? 13.192  -0.293  40.129  1.00 44.07  ? 112 ARG B CA  1 
ATOM   4343  C  C   . ARG B  1 112 ? 14.164  0.176   39.073  1.00 50.14  ? 112 ARG B C   1 
ATOM   4344  O  O   . ARG B  1 112 ? 15.373  -0.035  39.176  1.00 57.00  ? 112 ARG B O   1 
ATOM   4345  C  CB  . ARG B  1 112 ? 12.987  0.722   41.231  1.00 29.86  ? 112 ARG B CB  1 
ATOM   4346  C  CG  . ARG B  1 112 ? 11.863  0.314   42.120  1.00 29.69  ? 112 ARG B CG  1 
ATOM   4347  C  CD  . ARG B  1 112 ? 11.692  1.214   43.300  1.00 38.65  ? 112 ARG B CD  1 
ATOM   4348  N  NE  . ARG B  1 112 ? 11.146  2.493   42.895  1.00 48.42  ? 112 ARG B NE  1 
ATOM   4349  C  CZ  . ARG B  1 112 ? 11.511  3.670   43.389  1.00 52.60  ? 112 ARG B CZ  1 
ATOM   4350  N  NH1 . ARG B  1 112 ? 12.434  3.771   44.325  1.00 53.95  ? 112 ARG B NH1 1 
ATOM   4351  N  NH2 . ARG B  1 112 ? 10.980  4.767   42.892  1.00 61.84  ? 112 ARG B NH2 1 
ATOM   4352  N  N   . ARG B  1 113 ? 13.623  0.728   38.002  1.00 54.12  ? 113 ARG B N   1 
ATOM   4353  C  CA  . ARG B  1 113 ? 14.434  1.160   36.884  1.00 58.13  ? 113 ARG B CA  1 
ATOM   4354  C  C   . ARG B  1 113 ? 14.450  2.667   36.728  1.00 58.83  ? 113 ARG B C   1 
ATOM   4355  O  O   . ARG B  1 113 ? 13.455  3.358   37.035  1.00 61.52  ? 113 ARG B O   1 
ATOM   4356  C  CB  . ARG B  1 113 ? 13.886  0.509   35.614  1.00 62.65  ? 113 ARG B CB  1 
ATOM   4357  C  CG  . ARG B  1 113 ? 14.448  1.019   34.296  1.00 66.31  ? 113 ARG B CG  1 
ATOM   4358  C  CD  . ARG B  1 113 ? 13.866  0.221   33.137  1.00 70.38  ? 113 ARG B CD  1 
ATOM   4359  N  NE  . ARG B  1 113 ? 14.191  -1.206  33.252  1.00 79.62  ? 113 ARG B NE  1 
ATOM   4360  C  CZ  . ARG B  1 113 ? 13.833  -2.152  32.376  1.00 84.89  ? 113 ARG B CZ  1 
ATOM   4361  N  NH1 . ARG B  1 113 ? 13.120  -1.837  31.289  1.00 88.01  ? 113 ARG B NH1 1 
ATOM   4362  N  NH2 . ARG B  1 113 ? 14.198  -3.421  32.583  1.00 85.91  ? 113 ARG B NH2 1 
ATOM   4363  N  N   . PHE B  1 114 ? 15.588  3.174   36.267  1.00 56.06  ? 114 PHE B N   1 
ATOM   4364  C  CA  . PHE B  1 114 ? 15.746  4.600   36.035  1.00 54.43  ? 114 PHE B CA  1 
ATOM   4365  C  C   . PHE B  1 114 ? 16.687  4.801   34.853  1.00 56.74  ? 114 PHE B C   1 
ATOM   4366  O  O   . PHE B  1 114 ? 17.264  3.838   34.306  1.00 56.83  ? 114 PHE B O   1 
ATOM   4367  C  CB  . PHE B  1 114 ? 16.317  5.297   37.255  1.00 50.64  ? 114 PHE B CB  1 
ATOM   4368  C  CG  . PHE B  1 114 ? 15.577  5.016   38.518  1.00 47.27  ? 114 PHE B CG  1 
ATOM   4369  C  CD1 . PHE B  1 114 ? 15.928  3.935   39.325  1.00 48.99  ? 114 PHE B CD1 1 
ATOM   4370  C  CD2 . PHE B  1 114 ? 14.551  5.840   38.921  1.00 45.15  ? 114 PHE B CD2 1 
ATOM   4371  C  CE1 . PHE B  1 114 ? 15.254  3.690   40.527  1.00 49.52  ? 114 PHE B CE1 1 
ATOM   4372  C  CE2 . PHE B  1 114 ? 13.866  5.609   40.122  1.00 49.69  ? 114 PHE B CE2 1 
ATOM   4373  C  CZ  . PHE B  1 114 ? 14.215  4.534   40.931  1.00 47.88  ? 114 PHE B CZ  1 
ATOM   4374  N  N   . SER B  1 115 ? 16.843  6.056   34.459  1.00 56.64  ? 115 SER B N   1 
ATOM   4375  C  CA  . SER B  1 115 ? 17.711  6.383   33.343  1.00 57.52  ? 115 SER B CA  1 
ATOM   4376  C  C   . SER B  1 115 ? 18.343  7.740   33.563  1.00 58.14  ? 115 SER B C   1 
ATOM   4377  O  O   . SER B  1 115 ? 17.733  8.644   34.160  1.00 56.99  ? 115 SER B O   1 
ATOM   4378  C  CB  . SER B  1 115 ? 16.893  6.461   32.067  1.00 59.89  ? 115 SER B CB  1 
ATOM   4379  O  OG  . SER B  1 115 ? 15.834  7.406   32.220  1.00 60.63  ? 115 SER B OG  1 
ATOM   4380  N  N   . PHE B  1 116 ? 19.537  7.901   33.024  1.00 57.25  ? 116 PHE B N   1 
ATOM   4381  C  CA  . PHE B  1 116 ? 20.245  9.162   33.124  1.00 55.68  ? 116 PHE B CA  1 
ATOM   4382  C  C   . PHE B  1 116 ? 20.996  9.257   31.812  1.00 58.14  ? 116 PHE B C   1 
ATOM   4383  O  O   . PHE B  1 116 ? 21.149  8.250   31.085  1.00 60.66  ? 116 PHE B O   1 
ATOM   4384  C  CB  . PHE B  1 116 ? 21.213  9.183   34.324  1.00 51.67  ? 116 PHE B CB  1 
ATOM   4385  C  CG  . PHE B  1 116 ? 22.271  8.099   34.289  1.00 42.21  ? 116 PHE B CG  1 
ATOM   4386  C  CD1 . PHE B  1 116 ? 23.331  8.178   33.409  1.00 37.98  ? 116 PHE B CD1 1 
ATOM   4387  C  CD2 . PHE B  1 116 ? 22.196  7.004   35.138  1.00 39.72  ? 116 PHE B CD2 1 
ATOM   4388  C  CE1 . PHE B  1 116 ? 24.297  7.198   33.365  1.00 36.38  ? 116 PHE B CE1 1 
ATOM   4389  C  CE2 . PHE B  1 116 ? 23.166  6.013   35.103  1.00 37.50  ? 116 PHE B CE2 1 
ATOM   4390  C  CZ  . PHE B  1 116 ? 24.222  6.111   34.212  1.00 33.75  ? 116 PHE B CZ  1 
ATOM   4391  N  N   . ILE B  1 117 ? 21.483  10.449  31.501  1.00 57.32  ? 117 ILE B N   1 
ATOM   4392  C  CA  . ILE B  1 117 ? 22.214  10.611  30.256  1.00 53.77  ? 117 ILE B CA  1 
ATOM   4393  C  C   . ILE B  1 117 ? 23.580  11.169  30.534  1.00 51.07  ? 117 ILE B C   1 
ATOM   4394  O  O   . ILE B  1 117 ? 23.702  12.225  31.180  1.00 51.97  ? 117 ILE B O   1 
ATOM   4395  C  CB  . ILE B  1 117 ? 21.496  11.541  29.346  1.00 54.49  ? 117 ILE B CB  1 
ATOM   4396  C  CG1 . ILE B  1 117 ? 20.078  11.042  29.141  1.00 55.09  ? 117 ILE B CG1 1 
ATOM   4397  C  CG2 . ILE B  1 117 ? 22.215  11.596  28.040  1.00 59.00  ? 117 ILE B CG2 1 
ATOM   4398  C  CD1 . ILE B  1 117 ? 19.243  11.936  28.324  1.00 56.59  ? 117 ILE B CD1 1 
ATOM   4399  N  N   . THR B  1 118 ? 24.612  10.482  30.065  1.00 45.78  ? 118 THR B N   1 
ATOM   4400  C  CA  . THR B  1 118 ? 25.950  10.984  30.318  1.00 48.37  ? 118 THR B CA  1 
ATOM   4401  C  C   . THR B  1 118 ? 26.100  12.309  29.583  1.00 53.33  ? 118 THR B C   1 
ATOM   4402  O  O   . THR B  1 118 ? 25.389  12.560  28.621  1.00 59.20  ? 118 THR B O   1 
ATOM   4403  C  CB  . THR B  1 118 ? 26.981  10.011  29.863  1.00 42.78  ? 118 THR B CB  1 
ATOM   4404  O  OG1 . THR B  1 118 ? 26.591  9.518   28.589  1.00 43.97  ? 118 THR B OG1 1 
ATOM   4405  C  CG2 . THR B  1 118 ? 27.065  8.873   30.840  1.00 42.32  ? 118 THR B CG2 1 
ATOM   4406  N  N   . PRO B  1 119 ? 26.966  13.210  30.070  1.00 53.60  ? 119 PRO B N   1 
ATOM   4407  C  CA  . PRO B  1 119 ? 27.144  14.493  29.410  1.00 49.99  ? 119 PRO B CA  1 
ATOM   4408  C  C   . PRO B  1 119 ? 28.116  14.378  28.252  1.00 45.48  ? 119 PRO B C   1 
ATOM   4409  O  O   . PRO B  1 119 ? 28.772  13.337  28.042  1.00 43.56  ? 119 PRO B O   1 
ATOM   4410  C  CB  . PRO B  1 119 ? 27.729  15.350  30.528  1.00 54.08  ? 119 PRO B CB  1 
ATOM   4411  C  CG  . PRO B  1 119 ? 28.689  14.433  31.121  1.00 58.58  ? 119 PRO B CG  1 
ATOM   4412  C  CD  . PRO B  1 119 ? 27.837  13.145  31.255  1.00 60.89  ? 119 PRO B CD  1 
ATOM   4413  N  N   . PRO B  1 120 ? 28.227  15.464  27.481  1.00 44.34  ? 120 PRO B N   1 
ATOM   4414  C  CA  . PRO B  1 120 ? 29.131  15.499  26.334  1.00 45.30  ? 120 PRO B CA  1 
ATOM   4415  C  C   . PRO B  1 120 ? 30.540  15.474  26.868  1.00 48.36  ? 120 PRO B C   1 
ATOM   4416  O  O   . PRO B  1 120 ? 30.782  15.717  28.053  1.00 52.61  ? 120 PRO B O   1 
ATOM   4417  C  CB  . PRO B  1 120 ? 28.850  16.862  25.726  1.00 41.75  ? 120 PRO B CB  1 
ATOM   4418  C  CG  . PRO B  1 120 ? 27.482  17.223  26.267  1.00 43.28  ? 120 PRO B CG  1 
ATOM   4419  C  CD  . PRO B  1 120 ? 27.543  16.757  27.648  1.00 39.66  ? 120 PRO B CD  1 
ATOM   4420  N  N   . GLN B  1 121 ? 31.477  15.167  26.002  1.00 52.61  ? 121 GLN B N   1 
ATOM   4421  C  CA  . GLN B  1 121 ? 32.857  15.174  26.410  1.00 56.18  ? 121 GLN B CA  1 
ATOM   4422  C  C   . GLN B  1 121 ? 33.159  16.639  26.707  1.00 57.56  ? 121 GLN B C   1 
ATOM   4423  O  O   . GLN B  1 121 ? 32.624  17.513  26.015  1.00 60.69  ? 121 GLN B O   1 
ATOM   4424  C  CB  . GLN B  1 121 ? 33.705  14.692  25.262  1.00 61.69  ? 121 GLN B CB  1 
ATOM   4425  C  CG  . GLN B  1 121 ? 35.167  14.699  25.562  1.00 70.88  ? 121 GLN B CG  1 
ATOM   4426  C  CD  . GLN B  1 121 ? 35.942  13.847  24.593  1.00 76.35  ? 121 GLN B CD  1 
ATOM   4427  O  OE1 . GLN B  1 121 ? 35.380  13.327  23.614  1.00 74.50  ? 121 GLN B OE1 1 
ATOM   4428  N  NE2 . GLN B  1 121 ? 37.241  13.664  24.872  1.00 80.88  ? 121 GLN B NE2 1 
ATOM   4429  N  N   . THR B  1 122 ? 33.977  16.920  27.731  1.00 59.22  ? 122 THR B N   1 
ATOM   4430  C  CA  . THR B  1 122 ? 34.301  18.313  28.093  1.00 56.12  ? 122 THR B CA  1 
ATOM   4431  C  C   . THR B  1 122 ? 34.851  19.058  26.892  1.00 56.06  ? 122 THR B C   1 
ATOM   4432  O  O   . THR B  1 122 ? 35.642  18.524  26.108  1.00 56.81  ? 122 THR B O   1 
ATOM   4433  C  CB  . THR B  1 122 ? 35.281  18.435  29.302  1.00 52.95  ? 122 THR B CB  1 
ATOM   4434  O  OG1 . THR B  1 122 ? 36.549  17.875  28.971  1.00 58.91  ? 122 THR B OG1 1 
ATOM   4435  C  CG2 . THR B  1 122 ? 34.773  17.669  30.477  1.00 55.44  ? 122 THR B CG2 1 
ATOM   4436  N  N   . GLY B  1 123 ? 34.427  20.294  26.731  1.00 53.80  ? 123 GLY B N   1 
ATOM   4437  C  CA  . GLY B  1 123 ? 34.900  21.020  25.583  1.00 56.36  ? 123 GLY B CA  1 
ATOM   4438  C  C   . GLY B  1 123 ? 34.693  22.502  25.727  1.00 59.21  ? 123 GLY B C   1 
ATOM   4439  O  O   . GLY B  1 123 ? 33.880  22.948  26.550  1.00 60.42  ? 123 GLY B O   1 
ATOM   4440  N  N   . LEU B  1 124 ? 35.338  23.244  24.825  1.00 59.44  ? 124 LEU B N   1 
ATOM   4441  C  CA  . LEU B  1 124 ? 35.324  24.697  24.822  1.00 55.83  ? 124 LEU B CA  1 
ATOM   4442  C  C   . LEU B  1 124 ? 33.980  25.306  24.555  1.00 53.78  ? 124 LEU B C   1 
ATOM   4443  O  O   . LEU B  1 124 ? 33.538  26.182  25.288  1.00 49.46  ? 124 LEU B O   1 
ATOM   4444  C  CB  . LEU B  1 124 ? 36.349  25.191  23.803  1.00 60.21  ? 124 LEU B CB  1 
ATOM   4445  C  CG  . LEU B  1 124 ? 36.998  26.570  23.977  1.00 62.63  ? 124 LEU B CG  1 
ATOM   4446  C  CD1 . LEU B  1 124 ? 37.243  26.908  25.446  1.00 64.59  ? 124 LEU B CD1 1 
ATOM   4447  C  CD2 . LEU B  1 124 ? 38.304  26.544  23.218  1.00 61.35  ? 124 LEU B CD2 1 
ATOM   4448  N  N   . ASP B  1 125 ? 33.312  24.809  23.520  1.00 55.47  ? 125 ASP B N   1 
ATOM   4449  C  CA  . ASP B  1 125 ? 32.005  25.340  23.148  1.00 59.75  ? 125 ASP B CA  1 
ATOM   4450  C  C   . ASP B  1 125 ? 30.819  24.401  23.429  1.00 59.09  ? 125 ASP B C   1 
ATOM   4451  O  O   . ASP B  1 125 ? 29.756  24.547  22.832  1.00 61.57  ? 125 ASP B O   1 
ATOM   4452  C  CB  . ASP B  1 125 ? 32.002  25.750  21.664  1.00 64.91  ? 125 ASP B CB  1 
ATOM   4453  C  CG  . ASP B  1 125 ? 32.934  26.940  21.356  1.00 68.59  ? 125 ASP B CG  1 
ATOM   4454  O  OD1 . ASP B  1 125 ? 32.775  28.028  21.955  1.00 73.83  ? 125 ASP B OD1 1 
ATOM   4455  O  OD2 . ASP B  1 125 ? 33.797  26.790  20.472  1.00 65.65  ? 125 ASP B OD2 1 
ATOM   4456  N  N   . VAL B  1 126 ? 31.004  23.434  24.324  1.00 55.77  ? 126 VAL B N   1 
ATOM   4457  C  CA  . VAL B  1 126 ? 29.945  22.501  24.673  1.00 46.43  ? 126 VAL B CA  1 
ATOM   4458  C  C   . VAL B  1 126 ? 28.960  23.219  25.610  1.00 48.65  ? 126 VAL B C   1 
ATOM   4459  O  O   . VAL B  1 126 ? 29.327  23.668  26.706  1.00 48.03  ? 126 VAL B O   1 
ATOM   4460  C  CB  . VAL B  1 126 ? 30.513  21.295  25.390  1.00 42.53  ? 126 VAL B CB  1 
ATOM   4461  C  CG1 . VAL B  1 126 ? 29.414  20.330  25.705  1.00 45.90  ? 126 VAL B CG1 1 
ATOM   4462  C  CG2 . VAL B  1 126 ? 31.590  20.635  24.570  1.00 39.03  ? 126 VAL B CG2 1 
ATOM   4463  N  N   . PRO B  1 127 ? 27.705  23.383  25.167  1.00 48.16  ? 127 PRO B N   1 
ATOM   4464  C  CA  . PRO B  1 127 ? 26.667  24.048  25.958  1.00 46.65  ? 127 PRO B CA  1 
ATOM   4465  C  C   . PRO B  1 127 ? 26.138  23.048  26.948  1.00 47.46  ? 127 PRO B C   1 
ATOM   4466  O  O   . PRO B  1 127 ? 26.219  21.839  26.719  1.00 46.54  ? 127 PRO B O   1 
ATOM   4467  C  CB  . PRO B  1 127 ? 25.598  24.365  24.928  1.00 45.35  ? 127 PRO B CB  1 
ATOM   4468  C  CG  . PRO B  1 127 ? 25.682  23.184  24.022  1.00 46.54  ? 127 PRO B CG  1 
ATOM   4469  C  CD  . PRO B  1 127 ? 27.173  22.924  23.872  1.00 48.98  ? 127 PRO B CD  1 
ATOM   4470  N  N   . TYR B  1 128 ? 25.577  23.544  28.038  1.00 44.38  ? 128 TYR B N   1 
ATOM   4471  C  CA  . TYR B  1 128 ? 25.023  22.655  29.039  1.00 40.89  ? 128 TYR B CA  1 
ATOM   4472  C  C   . TYR B  1 128 ? 24.196  23.550  29.910  1.00 40.61  ? 128 TYR B C   1 
ATOM   4473  O  O   . TYR B  1 128 ? 24.459  24.756  29.979  1.00 44.91  ? 128 TYR B O   1 
ATOM   4474  C  CB  . TYR B  1 128 ? 26.140  21.989  29.840  1.00 41.00  ? 128 TYR B CB  1 
ATOM   4475  C  CG  . TYR B  1 128 ? 25.726  20.690  30.518  1.00 45.58  ? 128 TYR B CG  1 
ATOM   4476  C  CD1 . TYR B  1 128 ? 25.658  19.497  29.787  1.00 43.92  ? 128 TYR B CD1 1 
ATOM   4477  C  CD2 . TYR B  1 128 ? 25.380  20.654  31.868  1.00 44.11  ? 128 TYR B CD2 1 
ATOM   4478  C  CE1 . TYR B  1 128 ? 25.257  18.309  30.366  1.00 42.38  ? 128 TYR B CE1 1 
ATOM   4479  C  CE2 . TYR B  1 128 ? 24.978  19.465  32.461  1.00 47.20  ? 128 TYR B CE2 1 
ATOM   4480  C  CZ  . TYR B  1 128 ? 24.915  18.291  31.700  1.00 48.09  ? 128 TYR B CZ  1 
ATOM   4481  O  OH  . TYR B  1 128 ? 24.490  17.105  32.272  1.00 52.31  ? 128 TYR B OH  1 
ATOM   4482  N  N   . THR B  1 129 ? 23.183  23.001  30.558  1.00 38.27  ? 129 THR B N   1 
ATOM   4483  C  CA  . THR B  1 129 ? 22.369  23.863  31.395  1.00 44.14  ? 129 THR B CA  1 
ATOM   4484  C  C   . THR B  1 129 ? 22.221  23.335  32.821  1.00 44.07  ? 129 THR B C   1 
ATOM   4485  O  O   . THR B  1 129 ? 21.795  22.210  33.044  1.00 44.52  ? 129 THR B O   1 
ATOM   4486  C  CB  . THR B  1 129 ? 21.007  24.243  30.701  1.00 48.82  ? 129 THR B CB  1 
ATOM   4487  O  OG1 . THR B  1 129 ? 19.941  24.286  31.667  1.00 54.96  ? 129 THR B OG1 1 
ATOM   4488  C  CG2 . THR B  1 129 ? 20.675  23.317  29.518  1.00 47.53  ? 129 THR B CG2 1 
ATOM   4489  N  N   . PHE B  1 130 ? 22.662  24.138  33.776  1.00 43.31  ? 130 PHE B N   1 
ATOM   4490  C  CA  . PHE B  1 130 ? 22.654  23.750  35.181  1.00 39.96  ? 130 PHE B CA  1 
ATOM   4491  C  C   . PHE B  1 130 ? 21.513  24.391  35.888  1.00 39.21  ? 130 PHE B C   1 
ATOM   4492  O  O   . PHE B  1 130 ? 21.128  25.511  35.595  1.00 42.93  ? 130 PHE B O   1 
ATOM   4493  C  CB  . PHE B  1 130 ? 23.961  24.192  35.878  1.00 38.76  ? 130 PHE B CB  1 
ATOM   4494  C  CG  . PHE B  1 130 ? 25.195  23.541  35.322  1.00 34.55  ? 130 PHE B CG  1 
ATOM   4495  C  CD1 . PHE B  1 130 ? 25.591  22.309  35.764  1.00 35.43  ? 130 PHE B CD1 1 
ATOM   4496  C  CD2 . PHE B  1 130 ? 25.926  24.132  34.317  1.00 33.72  ? 130 PHE B CD2 1 
ATOM   4497  C  CE1 . PHE B  1 130 ? 26.699  21.665  35.208  1.00 35.92  ? 130 PHE B CE1 1 
ATOM   4498  C  CE2 . PHE B  1 130 ? 27.033  23.485  33.769  1.00 34.23  ? 130 PHE B CE2 1 
ATOM   4499  C  CZ  . PHE B  1 130 ? 27.418  22.245  34.216  1.00 28.30  ? 130 PHE B CZ  1 
ATOM   4500  N  N   . GLY B  1 131 ? 20.948  23.680  36.827  1.00 37.20  ? 131 GLY B N   1 
ATOM   4501  C  CA  . GLY B  1 131 ? 19.870  24.272  37.562  1.00 38.30  ? 131 GLY B CA  1 
ATOM   4502  C  C   . GLY B  1 131 ? 20.540  24.731  38.813  1.00 39.77  ? 131 GLY B C   1 
ATOM   4503  O  O   . GLY B  1 131 ? 21.586  24.200  39.145  1.00 42.33  ? 131 GLY B O   1 
ATOM   4504  N  N   . LEU B  1 132 ? 19.987  25.741  39.472  1.00 39.72  ? 132 LEU B N   1 
ATOM   4505  C  CA  . LEU B  1 132 ? 20.540  26.249  40.722  1.00 40.74  ? 132 LEU B CA  1 
ATOM   4506  C  C   . LEU B  1 132 ? 19.494  26.220  41.783  1.00 42.06  ? 132 LEU B C   1 
ATOM   4507  O  O   . LEU B  1 132 ? 18.483  26.874  41.666  1.00 44.89  ? 132 LEU B O   1 
ATOM   4508  C  CB  . LEU B  1 132 ? 21.088  27.653  40.558  1.00 40.07  ? 132 LEU B CB  1 
ATOM   4509  C  CG  . LEU B  1 132 ? 22.528  27.338  40.192  1.00 42.28  ? 132 LEU B CG  1 
ATOM   4510  C  CD1 . LEU B  1 132 ? 22.764  27.486  38.719  1.00 36.01  ? 132 LEU B CD1 1 
ATOM   4511  C  CD2 . LEU B  1 132 ? 23.434  28.168  41.015  1.00 38.92  ? 132 LEU B CD2 1 
ATOM   4512  N  N   . ILE B  1 133 ? 19.714  25.394  42.794  1.00 43.87  ? 133 ILE B N   1 
ATOM   4513  C  CA  . ILE B  1 133 ? 18.772  25.232  43.895  1.00 37.44  ? 133 ILE B CA  1 
ATOM   4514  C  C   . ILE B  1 133 ? 19.622  25.288  45.131  1.00 37.29  ? 133 ILE B C   1 
ATOM   4515  O  O   . ILE B  1 133 ? 20.736  24.752  45.162  1.00 42.45  ? 133 ILE B O   1 
ATOM   4516  C  CB  . ILE B  1 133 ? 18.071  23.860  43.853  1.00 31.60  ? 133 ILE B CB  1 
ATOM   4517  C  CG1 . ILE B  1 133 ? 17.490  23.602  42.463  1.00 28.96  ? 133 ILE B CG1 1 
ATOM   4518  C  CG2 . ILE B  1 133 ? 16.986  23.833  44.890  1.00 31.84  ? 133 ILE B CG2 1 
ATOM   4519  C  CD1 . ILE B  1 133 ? 16.470  22.546  42.416  1.00 27.50  ? 133 ILE B CD1 1 
ATOM   4520  N  N   . GLY B  1 134 ? 19.136  25.946  46.154  1.00 31.74  ? 134 GLY B N   1 
ATOM   4521  C  CA  . GLY B  1 134 ? 19.937  26.030  47.346  1.00 29.82  ? 134 GLY B CA  1 
ATOM   4522  C  C   . GLY B  1 134 ? 18.953  26.148  48.472  1.00 31.67  ? 134 GLY B C   1 
ATOM   4523  O  O   . GLY B  1 134 ? 17.831  26.610  48.239  1.00 35.93  ? 134 GLY B O   1 
ATOM   4524  N  N   . ASP B  1 135 ? 19.276  25.566  49.626  1.00 32.97  ? 135 ASP B N   1 
ATOM   4525  C  CA  . ASP B  1 135 ? 18.407  25.660  50.754  1.00 31.13  ? 135 ASP B CA  1 
ATOM   4526  C  C   . ASP B  1 135 ? 16.962  25.087  50.605  1.00 32.64  ? 135 ASP B C   1 
ATOM   4527  O  O   . ASP B  1 135 ? 16.014  25.582  51.217  1.00 34.90  ? 135 ASP B O   1 
ATOM   4528  C  CB  . ASP B  1 135 ? 18.400  27.128  51.010  1.00 34.61  ? 135 ASP B CB  1 
ATOM   4529  C  CG  . ASP B  1 135 ? 19.480  27.531  51.900  1.00 32.85  ? 135 ASP B CG  1 
ATOM   4530  O  OD1 . ASP B  1 135 ? 19.065  27.430  53.020  1.00 35.99  ? 135 ASP B OD1 1 
ATOM   4531  O  OD2 . ASP B  1 135 ? 20.594  27.906  51.483  1.00 30.91  ? 135 ASP B OD2 1 
ATOM   4532  N  N   . LEU B  1 136 ? 16.833  23.957  49.915  1.00 34.55  ? 136 LEU B N   1 
ATOM   4533  C  CA  . LEU B  1 136 ? 15.541  23.335  49.598  1.00 36.20  ? 136 LEU B CA  1 
ATOM   4534  C  C   . LEU B  1 136 ? 14.607  23.015  50.744  1.00 40.68  ? 136 LEU B C   1 
ATOM   4535  O  O   . LEU B  1 136 ? 13.529  23.607  50.838  1.00 43.33  ? 136 LEU B O   1 
ATOM   4536  C  CB  . LEU B  1 136 ? 15.774  22.105  48.728  1.00 33.47  ? 136 LEU B CB  1 
ATOM   4537  C  CG  . LEU B  1 136 ? 14.550  21.507  48.064  1.00 39.15  ? 136 LEU B CG  1 
ATOM   4538  C  CD1 . LEU B  1 136 ? 13.884  22.529  47.168  1.00 33.84  ? 136 LEU B CD1 1 
ATOM   4539  C  CD2 . LEU B  1 136 ? 14.978  20.293  47.230  1.00 41.02  ? 136 LEU B CD2 1 
ATOM   4540  N  N   . GLY B  1 137 ? 15.015  22.106  51.625  1.00 43.27  ? 137 GLY B N   1 
ATOM   4541  C  CA  . GLY B  1 137 ? 14.173  21.749  52.751  1.00 43.26  ? 137 GLY B CA  1 
ATOM   4542  C  C   . GLY B  1 137 ? 12.974  20.940  52.289  1.00 45.09  ? 137 GLY B C   1 
ATOM   4543  O  O   . GLY B  1 137 ? 13.001  20.357  51.183  1.00 39.27  ? 137 GLY B O   1 
ATOM   4544  N  N   . GLN B  1 138 ? 11.937  20.860  53.129  1.00 47.47  ? 138 GLN B N   1 
ATOM   4545  C  CA  . GLN B  1 138 ? 10.741  20.104  52.726  1.00 53.18  ? 138 GLN B CA  1 
ATOM   4546  C  C   . GLN B  1 138 ? 9.363   20.733  53.058  1.00 55.92  ? 138 GLN B C   1 
ATOM   4547  O  O   . GLN B  1 138 ? 8.445   20.044  53.492  1.00 56.13  ? 138 GLN B O   1 
ATOM   4548  C  CB  . GLN B  1 138 ? 10.824  18.654  53.216  1.00 51.90  ? 138 GLN B CB  1 
ATOM   4549  C  CG  . GLN B  1 138 ? 11.019  18.522  54.709  1.00 51.33  ? 138 GLN B CG  1 
ATOM   4550  C  CD  . GLN B  1 138 ? 11.404  17.146  55.079  1.00 52.75  ? 138 GLN B CD  1 
ATOM   4551  O  OE1 . GLN B  1 138 ? 12.566  16.847  55.154  1.00 60.07  ? 138 GLN B OE1 1 
ATOM   4552  N  NE2 . GLN B  1 138 ? 10.438  16.278  55.271  1.00 56.93  ? 138 GLN B NE2 1 
ATOM   4553  N  N   . SER B  1 139 ? 9.234   22.046  52.876  1.00 58.16  ? 139 SER B N   1 
ATOM   4554  C  CA  . SER B  1 139 ? 7.980   22.753  53.114  1.00 55.70  ? 139 SER B CA  1 
ATOM   4555  C  C   . SER B  1 139 ? 7.282   22.670  51.780  1.00 57.31  ? 139 SER B C   1 
ATOM   4556  O  O   . SER B  1 139 ? 7.851   22.211  50.790  1.00 60.64  ? 139 SER B O   1 
ATOM   4557  C  CB  . SER B  1 139 ? 8.241   24.225  53.478  1.00 55.68  ? 139 SER B CB  1 
ATOM   4558  O  OG  . SER B  1 139 ? 8.947   24.914  52.456  1.00 58.53  ? 139 SER B OG  1 
ATOM   4559  N  N   . PHE B  1 140 ? 6.045   23.110  51.728  1.00 58.05  ? 140 PHE B N   1 
ATOM   4560  C  CA  . PHE B  1 140 ? 5.322   23.059  50.462  1.00 57.88  ? 140 PHE B CA  1 
ATOM   4561  C  C   . PHE B  1 140 ? 6.048   23.856  49.408  1.00 55.09  ? 140 PHE B C   1 
ATOM   4562  O  O   . PHE B  1 140 ? 6.142   23.475  48.227  1.00 51.86  ? 140 PHE B O   1 
ATOM   4563  C  CB  . PHE B  1 140 ? 3.939   23.648  50.656  1.00 62.46  ? 140 PHE B CB  1 
ATOM   4564  C  CG  . PHE B  1 140 ? 3.110   22.876  51.615  1.00 64.52  ? 140 PHE B CG  1 
ATOM   4565  C  CD1 . PHE B  1 140 ? 2.399   21.750  51.180  1.00 59.51  ? 140 PHE B CD1 1 
ATOM   4566  C  CD2 . PHE B  1 140 ? 3.081   23.235  52.968  1.00 63.02  ? 140 PHE B CD2 1 
ATOM   4567  C  CE1 . PHE B  1 140 ? 1.675   20.989  52.081  1.00 61.69  ? 140 PHE B CE1 1 
ATOM   4568  C  CE2 . PHE B  1 140 ? 2.351   22.477  53.885  1.00 62.04  ? 140 PHE B CE2 1 
ATOM   4569  C  CZ  . PHE B  1 140 ? 1.647   21.350  53.444  1.00 62.31  ? 140 PHE B CZ  1 
ATOM   4570  N  N   . ASP B  1 141 ? 6.583   24.971  49.877  1.00 49.81  ? 141 ASP B N   1 
ATOM   4571  C  CA  . ASP B  1 141 ? 7.302   25.884  49.045  1.00 46.83  ? 141 ASP B CA  1 
ATOM   4572  C  C   . ASP B  1 141 ? 8.359   25.118  48.313  1.00 44.15  ? 141 ASP B C   1 
ATOM   4573  O  O   . ASP B  1 141 ? 8.469   25.201  47.099  1.00 42.02  ? 141 ASP B O   1 
ATOM   4574  C  CB  . ASP B  1 141 ? 7.902   26.958  49.935  1.00 56.03  ? 141 ASP B CB  1 
ATOM   4575  C  CG  . ASP B  1 141 ? 6.860   27.979  50.405  1.00 65.17  ? 141 ASP B CG  1 
ATOM   4576  O  OD1 . ASP B  1 141 ? 6.173   28.550  49.507  1.00 72.84  ? 141 ASP B OD1 1 
ATOM   4577  O  OD2 . ASP B  1 141 ? 6.730   28.219  51.641  1.00 64.11  ? 141 ASP B OD2 1 
ATOM   4578  N  N   . SER B  1 142 ? 9.048   24.266  49.044  1.00 42.54  ? 142 SER B N   1 
ATOM   4579  C  CA  . SER B  1 142 ? 10.098  23.490  48.451  1.00 43.69  ? 142 SER B CA  1 
ATOM   4580  C  C   . SER B  1 142 ? 9.518   22.661  47.345  1.00 44.01  ? 142 SER B C   1 
ATOM   4581  O  O   . SER B  1 142 ? 10.099  22.612  46.267  1.00 43.59  ? 142 SER B O   1 
ATOM   4582  C  CB  . SER B  1 142 ? 10.715  22.585  49.495  1.00 47.46  ? 142 SER B CB  1 
ATOM   4583  O  OG  . SER B  1 142 ? 10.739  23.261  50.733  1.00 46.54  ? 142 SER B OG  1 
ATOM   4584  N  N   . ASN B  1 143 ? 8.323   22.104  47.567  1.00 47.48  ? 143 ASN B N   1 
ATOM   4585  C  CA  . ASN B  1 143 ? 7.712   21.226  46.559  1.00 52.05  ? 143 ASN B CA  1 
ATOM   4586  C  C   . ASN B  1 143 ? 7.521   22.007  45.293  1.00 53.69  ? 143 ASN B C   1 
ATOM   4587  O  O   . ASN B  1 143 ? 7.882   21.564  44.187  1.00 49.88  ? 143 ASN B O   1 
ATOM   4588  C  CB  . ASN B  1 143 ? 6.358   20.651  47.001  1.00 51.08  ? 143 ASN B CB  1 
ATOM   4589  C  CG  . ASN B  1 143 ? 5.821   19.610  46.016  1.00 52.59  ? 143 ASN B CG  1 
ATOM   4590  O  OD1 . ASN B  1 143 ? 6.585   18.836  45.429  1.00 43.04  ? 143 ASN B OD1 1 
ATOM   4591  N  ND2 . ASN B  1 143 ? 4.504   19.569  45.836  1.00 64.06  ? 143 ASN B ND2 1 
ATOM   4592  N  N   . THR B  1 144 ? 7.064   23.237  45.492  1.00 54.18  ? 144 THR B N   1 
ATOM   4593  C  CA  . THR B  1 144 ? 6.795   24.111  44.375  1.00 52.30  ? 144 THR B CA  1 
ATOM   4594  C  C   . THR B  1 144 ? 8.049   24.374  43.541  1.00 51.03  ? 144 THR B C   1 
ATOM   4595  O  O   . THR B  1 144 ? 8.065   24.135  42.314  1.00 45.92  ? 144 THR B O   1 
ATOM   4596  C  CB  . THR B  1 144 ? 6.191   25.427  44.857  1.00 51.17  ? 144 THR B CB  1 
ATOM   4597  O  OG1 . THR B  1 144 ? 4.983   25.183  45.597  1.00 50.51  ? 144 THR B OG1 1 
ATOM   4598  C  CG2 . THR B  1 144 ? 5.880   26.277  43.664  1.00 56.69  ? 144 THR B CG2 1 
ATOM   4599  N  N   . THR B  1 145 ? 9.104   24.829  44.217  1.00 48.53  ? 145 THR B N   1 
ATOM   4600  C  CA  . THR B  1 145 ? 10.360  25.132  43.550  1.00 46.70  ? 145 THR B CA  1 
ATOM   4601  C  C   . THR B  1 145 ? 10.796  23.935  42.749  1.00 45.75  ? 145 THR B C   1 
ATOM   4602  O  O   . THR B  1 145 ? 11.057  24.031  41.550  1.00 50.47  ? 145 THR B O   1 
ATOM   4603  C  CB  . THR B  1 145 ? 11.423  25.469  44.548  1.00 46.88  ? 145 THR B CB  1 
ATOM   4604  O  OG1 . THR B  1 145 ? 10.864  26.406  45.468  1.00 49.28  ? 145 THR B OG1 1 
ATOM   4605  C  CG2 . THR B  1 145 ? 12.653  26.061  43.865  1.00 40.94  ? 145 THR B CG2 1 
ATOM   4606  N  N   . LEU B  1 146 ? 10.786  22.776  43.367  1.00 42.75  ? 146 LEU B N   1 
ATOM   4607  C  CA  . LEU B  1 146 ? 11.194  21.626  42.621  1.00 43.75  ? 146 LEU B CA  1 
ATOM   4608  C  C   . LEU B  1 146 ? 10.321  21.444  41.376  1.00 46.66  ? 146 LEU B C   1 
ATOM   4609  O  O   . LEU B  1 146 ? 10.823  21.111  40.306  1.00 45.73  ? 146 LEU B O   1 
ATOM   4610  C  CB  . LEU B  1 146 ? 11.168  20.413  43.514  1.00 44.61  ? 146 LEU B CB  1 
ATOM   4611  C  CG  . LEU B  1 146 ? 11.834  19.159  42.973  1.00 45.27  ? 146 LEU B CG  1 
ATOM   4612  C  CD1 . LEU B  1 146 ? 13.260  19.449  42.581  1.00 47.74  ? 146 LEU B CD1 1 
ATOM   4613  C  CD2 . LEU B  1 146 ? 11.780  18.074  44.044  1.00 49.86  ? 146 LEU B CD2 1 
ATOM   4614  N  N   . SER B  1 147 ? 9.035   21.754  41.463  1.00 50.50  ? 147 SER B N   1 
ATOM   4615  C  CA  . SER B  1 147 ? 8.180   21.576  40.276  1.00 52.11  ? 147 SER B CA  1 
ATOM   4616  C  C   . SER B  1 147 ? 8.589   22.553  39.212  1.00 48.64  ? 147 SER B C   1 
ATOM   4617  O  O   . SER B  1 147 ? 8.834   22.159  38.076  1.00 44.01  ? 147 SER B O   1 
ATOM   4618  C  CB  . SER B  1 147 ? 6.698   21.794  40.583  1.00 56.24  ? 147 SER B CB  1 
ATOM   4619  O  OG  . SER B  1 147 ? 6.405   21.467  41.932  1.00 59.24  ? 147 SER B OG  1 
ATOM   4620  N  N   . HIS B  1 148 ? 8.684   23.822  39.594  1.00 45.72  ? 148 HIS B N   1 
ATOM   4621  C  CA  . HIS B  1 148 ? 9.081   24.844  38.639  1.00 45.50  ? 148 HIS B CA  1 
ATOM   4622  C  C   . HIS B  1 148 ? 10.350  24.440  37.934  1.00 44.51  ? 148 HIS B C   1 
ATOM   4623  O  O   . HIS B  1 148 ? 10.510  24.646  36.734  1.00 45.43  ? 148 HIS B O   1 
ATOM   4624  C  CB  . HIS B  1 148 ? 9.321   26.174  39.314  1.00 45.01  ? 148 HIS B CB  1 
ATOM   4625  C  CG  . HIS B  1 148 ? 8.083   26.984  39.506  1.00 51.73  ? 148 HIS B CG  1 
ATOM   4626  N  ND1 . HIS B  1 148 ? 8.093   28.366  39.517  1.00 55.84  ? 148 HIS B ND1 1 
ATOM   4627  C  CD2 . HIS B  1 148 ? 6.802   26.619  39.745  1.00 52.89  ? 148 HIS B CD2 1 
ATOM   4628  C  CE1 . HIS B  1 148 ? 6.876   28.815  39.762  1.00 52.99  ? 148 HIS B CE1 1 
ATOM   4629  N  NE2 . HIS B  1 148 ? 6.073   27.774  39.907  1.00 54.56  ? 148 HIS B NE2 1 
ATOM   4630  N  N   . TYR B  1 149 ? 11.264  23.841  38.670  1.00 43.37  ? 149 TYR B N   1 
ATOM   4631  C  CA  . TYR B  1 149 ? 12.492  23.460  38.040  1.00 43.87  ? 149 TYR B CA  1 
ATOM   4632  C  C   . TYR B  1 149 ? 12.220  22.393  37.027  1.00 46.25  ? 149 TYR B C   1 
ATOM   4633  O  O   . TYR B  1 149 ? 12.754  22.435  35.925  1.00 46.27  ? 149 TYR B O   1 
ATOM   4634  C  CB  . TYR B  1 149 ? 13.495  22.955  39.059  1.00 43.00  ? 149 TYR B CB  1 
ATOM   4635  C  CG  . TYR B  1 149 ? 14.756  22.423  38.410  1.00 43.33  ? 149 TYR B CG  1 
ATOM   4636  C  CD1 . TYR B  1 149 ? 15.540  23.239  37.607  1.00 45.97  ? 149 TYR B CD1 1 
ATOM   4637  C  CD2 . TYR B  1 149 ? 15.117  21.090  38.530  1.00 41.03  ? 149 TYR B CD2 1 
ATOM   4638  C  CE1 . TYR B  1 149 ? 16.653  22.734  36.929  1.00 45.67  ? 149 TYR B CE1 1 
ATOM   4639  C  CE2 . TYR B  1 149 ? 16.223  20.572  37.853  1.00 41.74  ? 149 TYR B CE2 1 
ATOM   4640  C  CZ  . TYR B  1 149 ? 16.986  21.399  37.046  1.00 44.59  ? 149 TYR B CZ  1 
ATOM   4641  O  OH  . TYR B  1 149 ? 18.035  20.898  36.297  1.00 43.99  ? 149 TYR B OH  1 
ATOM   4642  N  N   . GLU B  1 150 ? 11.395  21.430  37.415  1.00 54.17  ? 150 GLU B N   1 
ATOM   4643  C  CA  . GLU B  1 150 ? 11.066  20.301  36.549  1.00 62.41  ? 150 GLU B CA  1 
ATOM   4644  C  C   . GLU B  1 150 ? 10.403  20.784  35.282  1.00 66.56  ? 150 GLU B C   1 
ATOM   4645  O  O   . GLU B  1 150 ? 10.502  20.149  34.231  1.00 68.38  ? 150 GLU B O   1 
ATOM   4646  C  CB  . GLU B  1 150 ? 10.080  19.355  37.232  1.00 68.03  ? 150 GLU B CB  1 
ATOM   4647  C  CG  . GLU B  1 150 ? 10.562  18.573  38.430  1.00 75.29  ? 150 GLU B CG  1 
ATOM   4648  C  CD  . GLU B  1 150 ? 9.427   17.765  39.080  1.00 81.20  ? 150 GLU B CD  1 
ATOM   4649  O  OE1 . GLU B  1 150 ? 8.524   18.385  39.699  1.00 80.80  ? 150 GLU B OE1 1 
ATOM   4650  O  OE2 . GLU B  1 150 ? 9.422   16.513  38.958  1.00 82.49  ? 150 GLU B OE2 1 
ATOM   4651  N  N   . LEU B  1 151 ? 9.680   21.892  35.400  1.00 70.16  ? 151 LEU B N   1 
ATOM   4652  C  CA  . LEU B  1 151 ? 8.957   22.436  34.263  1.00 71.05  ? 151 LEU B CA  1 
ATOM   4653  C  C   . LEU B  1 151 ? 9.684   23.492  33.448  1.00 72.73  ? 151 LEU B C   1 
ATOM   4654  O  O   . LEU B  1 151 ? 9.190   23.868  32.384  1.00 77.40  ? 151 LEU B O   1 
ATOM   4655  C  CB  . LEU B  1 151 ? 7.590   22.937  34.724  1.00 65.92  ? 151 LEU B CB  1 
ATOM   4656  C  CG  . LEU B  1 151 ? 6.854   21.809  35.460  1.00 64.82  ? 151 LEU B CG  1 
ATOM   4657  C  CD1 . LEU B  1 151 ? 5.587   22.305  36.141  1.00 62.04  ? 151 LEU B CD1 1 
ATOM   4658  C  CD2 . LEU B  1 151 ? 6.571   20.670  34.484  1.00 60.76  ? 151 LEU B CD2 1 
ATOM   4659  N  N   . SER B  1 152 ? 10.820  23.994  33.930  1.00 72.84  ? 152 SER B N   1 
ATOM   4660  C  CA  . SER B  1 152 ? 11.544  24.996  33.165  1.00 71.31  ? 152 SER B CA  1 
ATOM   4661  C  C   . SER B  1 152 ? 11.625  24.466  31.755  1.00 73.66  ? 152 SER B C   1 
ATOM   4662  O  O   . SER B  1 152 ? 11.886  23.283  31.533  1.00 72.95  ? 152 SER B O   1 
ATOM   4663  C  CB  . SER B  1 152 ? 12.948  25.270  33.712  1.00 69.88  ? 152 SER B CB  1 
ATOM   4664  O  OG  . SER B  1 152 ? 13.013  26.527  34.376  1.00 66.62  ? 152 SER B OG  1 
ATOM   4665  N  N   . PRO B  1 153 ? 11.151  25.273  30.811  1.00 77.36  ? 153 PRO B N   1 
ATOM   4666  C  CA  . PRO B  1 153 ? 11.103  25.027  29.364  1.00 80.08  ? 153 PRO B CA  1 
ATOM   4667  C  C   . PRO B  1 153 ? 12.503  24.770  28.810  1.00 81.43  ? 153 PRO B C   1 
ATOM   4668  O  O   . PRO B  1 153 ? 12.700  24.052  27.830  1.00 78.74  ? 153 PRO B O   1 
ATOM   4669  C  CB  . PRO B  1 153 ? 10.497  26.320  28.831  1.00 83.09  ? 153 PRO B CB  1 
ATOM   4670  C  CG  . PRO B  1 153 ? 10.671  27.327  29.985  1.00 81.97  ? 153 PRO B CG  1 
ATOM   4671  C  CD  . PRO B  1 153 ? 10.413  26.493  31.165  1.00 79.67  ? 153 PRO B CD  1 
ATOM   4672  N  N   . LYS B  1 154 ? 13.456  25.455  29.415  1.00 85.25  ? 154 LYS B N   1 
ATOM   4673  C  CA  . LYS B  1 154 ? 14.866  25.288  29.118  1.00 87.05  ? 154 LYS B CA  1 
ATOM   4674  C  C   . LYS B  1 154 ? 15.070  24.249  30.223  1.00 86.56  ? 154 LYS B C   1 
ATOM   4675  O  O   . LYS B  1 154 ? 14.978  24.581  31.411  1.00 90.13  ? 154 LYS B O   1 
ATOM   4676  C  CB  . LYS B  1 154 ? 15.603  26.603  29.437  1.00 88.65  ? 154 LYS B CB  1 
ATOM   4677  C  CG  . LYS B  1 154 ? 14.973  27.392  30.643  1.00 92.43  ? 154 LYS B CG  1 
ATOM   4678  C  CD  . LYS B  1 154 ? 15.230  28.925  30.630  1.00 97.60  ? 154 LYS B CD  1 
ATOM   4679  C  CE  . LYS B  1 154 ? 14.053  29.744  31.259  1.00 95.01  ? 154 LYS B CE  1 
ATOM   4680  N  NZ  . LYS B  1 154 ? 13.885  29.709  32.759  1.00 92.78  ? 154 LYS B NZ  1 
ATOM   4681  N  N   . LYS B  1 155 ? 15.167  22.977  29.857  1.00 83.48  ? 155 LYS B N   1 
ATOM   4682  C  CA  . LYS B  1 155 ? 15.313  21.941  30.883  1.00 80.51  ? 155 LYS B CA  1 
ATOM   4683  C  C   . LYS B  1 155 ? 16.711  21.837  31.503  1.00 74.61  ? 155 LYS B C   1 
ATOM   4684  O  O   . LYS B  1 155 ? 17.711  21.811  30.767  1.00 76.12  ? 155 LYS B O   1 
ATOM   4685  C  CB  . LYS B  1 155 ? 14.816  20.570  30.374  1.00 87.02  ? 155 LYS B CB  1 
ATOM   4686  C  CG  . LYS B  1 155 ? 14.879  20.367  28.864  1.00 95.18  ? 155 LYS B CG  1 
ATOM   4687  C  CD  . LYS B  1 155 ? 16.303  20.582  28.325  1.00 105.81 ? 155 LYS B CD  1 
ATOM   4688  C  CE  . LYS B  1 155 ? 16.403  20.386  26.801  1.00 110.30 ? 155 LYS B CE  1 
ATOM   4689  N  NZ  . LYS B  1 155 ? 15.486  21.278  26.016  1.00 114.68 ? 155 LYS B NZ  1 
ATOM   4690  N  N   . GLY B  1 156 ? 16.770  21.843  32.843  1.00 63.99  ? 156 GLY B N   1 
ATOM   4691  C  CA  . GLY B  1 156 ? 18.038  21.724  33.554  1.00 52.21  ? 156 GLY B CA  1 
ATOM   4692  C  C   . GLY B  1 156 ? 18.620  20.344  33.322  1.00 46.53  ? 156 GLY B C   1 
ATOM   4693  O  O   . GLY B  1 156 ? 17.874  19.419  33.138  1.00 50.96  ? 156 GLY B O   1 
ATOM   4694  N  N   . GLN B  1 157 ? 19.930  20.181  33.314  1.00 43.18  ? 157 GLN B N   1 
ATOM   4695  C  CA  . GLN B  1 157 ? 20.527  18.873  33.068  1.00 38.65  ? 157 GLN B CA  1 
ATOM   4696  C  C   . GLN B  1 157 ? 21.388  18.338  34.200  1.00 34.74  ? 157 GLN B C   1 
ATOM   4697  O  O   . GLN B  1 157 ? 21.951  17.266  34.052  1.00 33.96  ? 157 GLN B O   1 
ATOM   4698  C  CB  . GLN B  1 157 ? 21.382  18.919  31.821  1.00 46.52  ? 157 GLN B CB  1 
ATOM   4699  C  CG  . GLN B  1 157 ? 20.622  19.226  30.572  1.00 56.76  ? 157 GLN B CG  1 
ATOM   4700  C  CD  . GLN B  1 157 ? 21.546  19.415  29.392  1.00 63.16  ? 157 GLN B CD  1 
ATOM   4701  O  OE1 . GLN B  1 157 ? 21.782  18.491  28.619  1.00 63.44  ? 157 GLN B OE1 1 
ATOM   4702  N  NE2 . GLN B  1 157 ? 22.095  20.613  29.261  1.00 68.99  ? 157 GLN B NE2 1 
ATOM   4703  N  N   . THR B  1 158 ? 21.535  19.119  35.274  1.00 30.44  ? 158 THR B N   1 
ATOM   4704  C  CA  . THR B  1 158 ? 22.320  18.804  36.467  1.00 23.48  ? 158 THR B CA  1 
ATOM   4705  C  C   . THR B  1 158 ? 22.020  19.937  37.417  1.00 28.38  ? 158 THR B C   1 
ATOM   4706  O  O   . THR B  1 158 ? 21.995  21.100  37.013  1.00 37.48  ? 158 THR B O   1 
ATOM   4707  C  CB  . THR B  1 158 ? 23.814  18.916  36.206  1.00 22.25  ? 158 THR B CB  1 
ATOM   4708  O  OG1 . THR B  1 158 ? 24.250  17.876  35.338  1.00 23.52  ? 158 THR B OG1 1 
ATOM   4709  C  CG2 . THR B  1 158 ? 24.571  18.846  37.493  1.00 27.65  ? 158 THR B CG2 1 
ATOM   4710  N  N   . VAL B  1 159 ? 21.772  19.637  38.670  1.00 26.97  ? 159 VAL B N   1 
ATOM   4711  C  CA  . VAL B  1 159 ? 21.499  20.695  39.626  1.00 31.67  ? 159 VAL B CA  1 
ATOM   4712  C  C   . VAL B  1 159 ? 22.762  20.958  40.425  1.00 32.97  ? 159 VAL B C   1 
ATOM   4713  O  O   . VAL B  1 159 ? 23.482  20.038  40.736  1.00 39.02  ? 159 VAL B O   1 
ATOM   4714  C  CB  . VAL B  1 159 ? 20.394  20.284  40.609  1.00 31.67  ? 159 VAL B CB  1 
ATOM   4715  C  CG1 . VAL B  1 159 ? 20.249  21.325  41.717  1.00 33.49  ? 159 VAL B CG1 1 
ATOM   4716  C  CG2 . VAL B  1 159 ? 19.093  20.112  39.877  1.00 34.36  ? 159 VAL B CG2 1 
ATOM   4717  N  N   . LEU B  1 160 ? 23.110  22.211  40.656  1.00 32.39  ? 160 LEU B N   1 
ATOM   4718  C  CA  . LEU B  1 160 ? 24.264  22.509  41.480  1.00 30.70  ? 160 LEU B CA  1 
ATOM   4719  C  C   . LEU B  1 160 ? 23.584  22.903  42.797  1.00 32.99  ? 160 LEU B C   1 
ATOM   4720  O  O   . LEU B  1 160 ? 22.840  23.876  42.833  1.00 34.63  ? 160 LEU B O   1 
ATOM   4721  C  CB  . LEU B  1 160 ? 25.087  23.643  40.892  1.00 24.90  ? 160 LEU B CB  1 
ATOM   4722  C  CG  . LEU B  1 160 ? 25.605  23.354  39.473  1.00 34.21  ? 160 LEU B CG  1 
ATOM   4723  C  CD1 . LEU B  1 160 ? 26.306  24.599  38.916  1.00 29.16  ? 160 LEU B CD1 1 
ATOM   4724  C  CD2 . LEU B  1 160 ? 26.528  22.109  39.392  1.00 27.96  ? 160 LEU B CD2 1 
ATOM   4725  N  N   . PHE B  1 161 ? 23.687  22.034  43.804  1.00 32.73  ? 161 PHE B N   1 
ATOM   4726  C  CA  . PHE B  1 161 ? 23.052  22.263  45.086  1.00 32.70  ? 161 PHE B CA  1 
ATOM   4727  C  C   . PHE B  1 161 ? 23.981  23.007  46.030  1.00 36.43  ? 161 PHE B C   1 
ATOM   4728  O  O   . PHE B  1 161 ? 25.035  22.530  46.403  1.00 41.70  ? 161 PHE B O   1 
ATOM   4729  C  CB  . PHE B  1 161 ? 22.554  20.957  45.680  1.00 29.23  ? 161 PHE B CB  1 
ATOM   4730  C  CG  . PHE B  1 161 ? 21.598  21.152  46.795  1.00 24.29  ? 161 PHE B CG  1 
ATOM   4731  C  CD1 . PHE B  1 161 ? 22.051  21.359  48.079  1.00 31.02  ? 161 PHE B CD1 1 
ATOM   4732  C  CD2 . PHE B  1 161 ? 20.256  21.179  46.550  1.00 19.91  ? 161 PHE B CD2 1 
ATOM   4733  C  CE1 . PHE B  1 161 ? 21.173  21.601  49.114  1.00 32.37  ? 161 PHE B CE1 1 
ATOM   4734  C  CE2 . PHE B  1 161 ? 19.366  21.422  47.568  1.00 19.88  ? 161 PHE B CE2 1 
ATOM   4735  C  CZ  . PHE B  1 161 ? 19.827  21.636  48.858  1.00 26.10  ? 161 PHE B CZ  1 
ATOM   4736  N  N   . VAL B  1 162 ? 23.492  24.108  46.553  1.00 37.74  ? 162 VAL B N   1 
ATOM   4737  C  CA  . VAL B  1 162 ? 24.292  24.995  47.348  1.00 30.55  ? 162 VAL B CA  1 
ATOM   4738  C  C   . VAL B  1 162 ? 24.214  24.859  48.861  1.00 32.53  ? 162 VAL B C   1 
ATOM   4739  O  O   . VAL B  1 162 ? 24.682  25.731  49.630  1.00 29.52  ? 162 VAL B O   1 
ATOM   4740  C  CB  . VAL B  1 162 ? 24.013  26.405  46.748  1.00 31.09  ? 162 VAL B CB  1 
ATOM   4741  C  CG1 . VAL B  1 162 ? 23.700  27.423  47.756  1.00 31.52  ? 162 VAL B CG1 1 
ATOM   4742  C  CG2 . VAL B  1 162 ? 25.131  26.816  45.885  1.00 25.09  ? 162 VAL B CG2 1 
ATOM   4743  N  N   . GLY B  1 163 ? 23.671  23.743  49.321  1.00 31.36  ? 163 GLY B N   1 
ATOM   4744  C  CA  . GLY B  1 163 ? 23.638  23.578  50.762  1.00 32.75  ? 163 GLY B CA  1 
ATOM   4745  C  C   . GLY B  1 163 ? 22.326  23.667  51.479  1.00 34.05  ? 163 GLY B C   1 
ATOM   4746  O  O   . GLY B  1 163 ? 21.457  24.388  51.045  1.00 35.02  ? 163 GLY B O   1 
ATOM   4747  N  N   . ASP B  1 164 ? 22.288  23.110  52.689  1.00 39.02  ? 164 ASP B N   1 
ATOM   4748  C  CA  . ASP B  1 164 ? 21.087  22.973  53.522  1.00 36.76  ? 164 ASP B CA  1 
ATOM   4749  C  C   . ASP B  1 164 ? 20.093  22.085  52.780  1.00 41.74  ? 164 ASP B C   1 
ATOM   4750  O  O   . ASP B  1 164 ? 19.251  22.570  52.015  1.00 41.34  ? 164 ASP B O   1 
ATOM   4751  C  CB  . ASP B  1 164 ? 20.489  24.289  53.919  1.00 30.50  ? 164 ASP B CB  1 
ATOM   4752  C  CG  . ASP B  1 164 ? 21.380  25.040  54.853  1.00 39.46  ? 164 ASP B CG  1 
ATOM   4753  O  OD1 . ASP B  1 164 ? 22.520  24.607  55.070  1.00 46.30  ? 164 ASP B OD1 1 
ATOM   4754  O  OD2 . ASP B  1 164 ? 21.100  26.171  55.203  1.00 39.32  ? 164 ASP B OD2 1 
ATOM   4755  N  N   . LEU B  1 165 ? 20.262  20.767  52.937  1.00 41.44  ? 165 LEU B N   1 
ATOM   4756  C  CA  . LEU B  1 165 ? 19.396  19.841  52.250  1.00 38.42  ? 165 LEU B CA  1 
ATOM   4757  C  C   . LEU B  1 165 ? 18.022  19.641  52.843  1.00 41.91  ? 165 LEU B C   1 
ATOM   4758  O  O   . LEU B  1 165 ? 17.048  20.123  52.305  1.00 46.28  ? 165 LEU B O   1 
ATOM   4759  C  CB  . LEU B  1 165 ? 20.067  18.486  52.040  1.00 28.80  ? 165 LEU B CB  1 
ATOM   4760  C  CG  . LEU B  1 165 ? 21.247  18.509  51.082  1.00 28.52  ? 165 LEU B CG  1 
ATOM   4761  C  CD1 . LEU B  1 165 ? 22.441  19.228  51.690  1.00 27.13  ? 165 LEU B CD1 1 
ATOM   4762  C  CD2 . LEU B  1 165 ? 21.607  17.120  50.826  1.00 26.86  ? 165 LEU B CD2 1 
ATOM   4763  N  N   . SER B  1 166 ? 17.939  19.083  54.035  1.00 43.47  ? 166 SER B N   1 
ATOM   4764  C  CA  . SER B  1 166 ? 16.624  18.756  54.552  1.00 38.59  ? 166 SER B CA  1 
ATOM   4765  C  C   . SER B  1 166 ? 16.129  19.388  55.819  1.00 33.71  ? 166 SER B C   1 
ATOM   4766  O  O   . SER B  1 166 ? 15.020  19.144  56.231  1.00 33.37  ? 166 SER B O   1 
ATOM   4767  C  CB  . SER B  1 166 ? 16.586  17.272  54.766  1.00 42.83  ? 166 SER B CB  1 
ATOM   4768  O  OG  . SER B  1 166 ? 17.400  16.976  55.890  1.00 48.49  ? 166 SER B OG  1 
ATOM   4769  N  N   . TYR B  1 167 ? 16.995  20.014  56.568  1.00 34.11  ? 167 TYR B N   1 
ATOM   4770  C  CA  . TYR B  1 167 ? 16.504  20.654  57.761  1.00 29.74  ? 167 TYR B CA  1 
ATOM   4771  C  C   . TYR B  1 167 ? 15.973  19.721  58.807  1.00 31.25  ? 167 TYR B C   1 
ATOM   4772  O  O   . TYR B  1 167 ? 15.194  20.144  59.658  1.00 30.64  ? 167 TYR B O   1 
ATOM   4773  C  CB  . TYR B  1 167 ? 15.440  21.648  57.409  1.00 28.28  ? 167 TYR B CB  1 
ATOM   4774  C  CG  . TYR B  1 167 ? 16.028  22.842  56.737  1.00 27.03  ? 167 TYR B CG  1 
ATOM   4775  C  CD1 . TYR B  1 167 ? 16.264  22.849  55.352  1.00 23.21  ? 167 TYR B CD1 1 
ATOM   4776  C  CD2 . TYR B  1 167 ? 16.398  23.951  57.500  1.00 30.33  ? 167 TYR B CD2 1 
ATOM   4777  C  CE1 . TYR B  1 167 ? 16.849  23.922  54.752  1.00 22.30  ? 167 TYR B CE1 1 
ATOM   4778  C  CE2 . TYR B  1 167 ? 16.983  25.049  56.921  1.00 34.84  ? 167 TYR B CE2 1 
ATOM   4779  C  CZ  . TYR B  1 167 ? 17.204  25.029  55.548  1.00 34.48  ? 167 TYR B CZ  1 
ATOM   4780  O  OH  . TYR B  1 167 ? 17.627  26.157  54.936  1.00 37.06  ? 167 TYR B OH  1 
ATOM   4781  N  N   . ALA B  1 168 ? 16.432  18.471  58.792  1.00 31.37  ? 168 ALA B N   1 
ATOM   4782  C  CA  . ALA B  1 168 ? 16.005  17.503  59.794  1.00 29.18  ? 168 ALA B CA  1 
ATOM   4783  C  C   . ALA B  1 168 ? 16.484  17.958  61.152  1.00 29.36  ? 168 ALA B C   1 
ATOM   4784  O  O   . ALA B  1 168 ? 15.831  17.750  62.153  1.00 29.47  ? 168 ALA B O   1 
ATOM   4785  C  CB  . ALA B  1 168 ? 16.553  16.149  59.483  1.00 29.04  ? 168 ALA B CB  1 
ATOM   4786  N  N   . ASP B  1 169 ? 17.574  18.695  61.178  1.00 31.22  ? 169 ASP B N   1 
ATOM   4787  C  CA  . ASP B  1 169 ? 18.083  19.147  62.446  1.00 37.89  ? 169 ASP B CA  1 
ATOM   4788  C  C   . ASP B  1 169 ? 17.180  20.115  63.193  1.00 42.44  ? 169 ASP B C   1 
ATOM   4789  O  O   . ASP B  1 169 ? 17.468  20.496  64.337  1.00 48.07  ? 169 ASP B O   1 
ATOM   4790  C  CB  . ASP B  1 169 ? 19.499  19.717  62.298  1.00 42.22  ? 169 ASP B CB  1 
ATOM   4791  C  CG  . ASP B  1 169 ? 19.568  20.896  61.384  1.00 42.73  ? 169 ASP B CG  1 
ATOM   4792  O  OD1 . ASP B  1 169 ? 18.851  20.887  60.385  1.00 51.34  ? 169 ASP B OD1 1 
ATOM   4793  O  OD2 . ASP B  1 169 ? 20.350  21.822  61.650  1.00 42.37  ? 169 ASP B OD2 1 
ATOM   4794  N  N   . ARG B  1 170 ? 16.102  20.548  62.557  1.00 47.40  ? 170 ARG B N   1 
ATOM   4795  C  CA  . ARG B  1 170 ? 15.200  21.482  63.225  1.00 52.18  ? 170 ARG B CA  1 
ATOM   4796  C  C   . ARG B  1 170 ? 14.259  20.668  64.072  1.00 52.61  ? 170 ARG B C   1 
ATOM   4797  O  O   . ARG B  1 170 ? 13.636  21.184  64.999  1.00 53.80  ? 170 ARG B O   1 
ATOM   4798  C  CB  . ARG B  1 170 ? 14.399  22.266  62.215  1.00 58.07  ? 170 ARG B CB  1 
ATOM   4799  C  CG  . ARG B  1 170 ? 15.226  22.852  61.143  1.00 61.63  ? 170 ARG B CG  1 
ATOM   4800  C  CD  . ARG B  1 170 ? 14.399  23.748  60.324  1.00 67.35  ? 170 ARG B CD  1 
ATOM   4801  N  NE  . ARG B  1 170 ? 13.873  24.803  61.165  1.00 70.86  ? 170 ARG B NE  1 
ATOM   4802  C  CZ  . ARG B  1 170 ? 12.595  24.889  61.481  1.00 75.58  ? 170 ARG B CZ  1 
ATOM   4803  N  NH1 . ARG B  1 170 ? 11.744  23.967  61.019  1.00 77.73  ? 170 ARG B NH1 1 
ATOM   4804  N  NH2 . ARG B  1 170 ? 12.176  25.891  62.238  1.00 78.36  ? 170 ARG B NH2 1 
ATOM   4805  N  N   . TYR B  1 171 ? 14.110  19.405  63.696  1.00 51.38  ? 171 TYR B N   1 
ATOM   4806  C  CA  . TYR B  1 171 ? 13.267  18.496  64.430  1.00 50.81  ? 171 TYR B CA  1 
ATOM   4807  C  C   . TYR B  1 171 ? 13.977  18.077  65.684  1.00 53.19  ? 171 TYR B C   1 
ATOM   4808  O  O   . TYR B  1 171 ? 15.184  18.210  65.788  1.00 61.93  ? 171 TYR B O   1 
ATOM   4809  C  CB  . TYR B  1 171 ? 12.978  17.307  63.577  1.00 46.92  ? 171 TYR B CB  1 
ATOM   4810  C  CG  . TYR B  1 171 ? 12.080  17.692  62.475  1.00 47.43  ? 171 TYR B CG  1 
ATOM   4811  C  CD1 . TYR B  1 171 ? 10.711  17.655  62.650  1.00 53.01  ? 171 TYR B CD1 1 
ATOM   4812  C  CD2 . TYR B  1 171 ? 12.576  18.132  61.278  1.00 48.06  ? 171 TYR B CD2 1 
ATOM   4813  C  CE1 . TYR B  1 171 ? 9.855   18.041  61.670  1.00 55.04  ? 171 TYR B CE1 1 
ATOM   4814  C  CE2 . TYR B  1 171 ? 11.723  18.527  60.280  1.00 53.95  ? 171 TYR B CE2 1 
ATOM   4815  C  CZ  . TYR B  1 171 ? 10.357  18.477  60.490  1.00 54.64  ? 171 TYR B CZ  1 
ATOM   4816  O  OH  . TYR B  1 171 ? 9.489   18.868  59.507  1.00 60.91  ? 171 TYR B OH  1 
ATOM   4817  N  N   . PRO B  1 172 ? 13.245  17.578  66.671  1.00 53.52  ? 172 PRO B N   1 
ATOM   4818  C  CA  . PRO B  1 172 ? 13.904  17.163  67.912  1.00 52.50  ? 172 PRO B CA  1 
ATOM   4819  C  C   . PRO B  1 172 ? 14.804  15.941  67.697  1.00 50.23  ? 172 PRO B C   1 
ATOM   4820  O  O   . PRO B  1 172 ? 14.468  15.043  66.914  1.00 44.71  ? 172 PRO B O   1 
ATOM   4821  C  CB  . PRO B  1 172 ? 12.728  16.908  68.836  1.00 51.94  ? 172 PRO B CB  1 
ATOM   4822  C  CG  . PRO B  1 172 ? 11.651  16.470  67.894  1.00 51.76  ? 172 PRO B CG  1 
ATOM   4823  C  CD  . PRO B  1 172 ? 11.791  17.385  66.737  1.00 53.69  ? 172 PRO B CD  1 
ATOM   4824  N  N   . ASN B  1 173 ? 15.979  15.969  68.343  1.00 49.28  ? 173 ASN B N   1 
ATOM   4825  C  CA  . ASN B  1 173 ? 16.978  14.915  68.227  1.00 48.11  ? 173 ASN B CA  1 
ATOM   4826  C  C   . ASN B  1 173 ? 17.301  14.708  66.748  1.00 46.91  ? 173 ASN B C   1 
ATOM   4827  O  O   . ASN B  1 173 ? 17.611  13.577  66.304  1.00 46.48  ? 173 ASN B O   1 
ATOM   4828  C  CB  . ASN B  1 173 ? 16.467  13.604  68.824  1.00 56.81  ? 173 ASN B CB  1 
ATOM   4829  C  CG  . ASN B  1 173 ? 16.035  13.733  70.283  1.00 62.64  ? 173 ASN B CG  1 
ATOM   4830  O  OD1 . ASN B  1 173 ? 15.043  13.112  70.678  1.00 70.67  ? 173 ASN B OD1 1 
ATOM   4831  N  ND2 . ASN B  1 173 ? 16.774  14.512  71.096  1.00 60.87  ? 173 ASN B ND2 1 
ATOM   4832  N  N   . HIS B  1 174 ? 17.143  15.792  65.986  1.00 40.28  ? 174 HIS B N   1 
ATOM   4833  C  CA  . HIS B  1 174 ? 17.404  15.823  64.553  1.00 41.59  ? 174 HIS B CA  1 
ATOM   4834  C  C   . HIS B  1 174 ? 16.677  14.729  63.823  1.00 42.79  ? 174 HIS B C   1 
ATOM   4835  O  O   . HIS B  1 174 ? 17.122  14.301  62.756  1.00 41.09  ? 174 HIS B O   1 
ATOM   4836  C  CB  . HIS B  1 174 ? 18.912  15.675  64.264  1.00 40.52  ? 174 HIS B CB  1 
ATOM   4837  C  CG  . HIS B  1 174 ? 19.768  16.737  64.898  1.00 43.47  ? 174 HIS B CG  1 
ATOM   4838  N  ND1 . HIS B  1 174 ? 20.925  17.210  64.316  1.00 43.24  ? 174 HIS B ND1 1 
ATOM   4839  C  CD2 . HIS B  1 174 ? 19.647  17.393  66.079  1.00 44.70  ? 174 HIS B CD2 1 
ATOM   4840  C  CE1 . HIS B  1 174 ? 21.485  18.106  65.114  1.00 46.69  ? 174 HIS B CE1 1 
ATOM   4841  N  NE2 . HIS B  1 174 ? 20.729  18.239  66.190  1.00 42.37  ? 174 HIS B NE2 1 
ATOM   4842  N  N   . ASP B  1 175 ? 15.549  14.311  64.383  1.00 44.63  ? 175 ASP B N   1 
ATOM   4843  C  CA  . ASP B  1 175 ? 14.767  13.209  63.843  1.00 46.14  ? 175 ASP B CA  1 
ATOM   4844  C  C   . ASP B  1 175 ? 15.178  12.791  62.451  1.00 42.03  ? 175 ASP B C   1 
ATOM   4845  O  O   . ASP B  1 175 ? 14.603  13.255  61.480  1.00 42.34  ? 175 ASP B O   1 
ATOM   4846  C  CB  . ASP B  1 175 ? 13.291  13.564  63.856  1.00 55.21  ? 175 ASP B CB  1 
ATOM   4847  C  CG  . ASP B  1 175 ? 12.397  12.350  63.653  1.00 65.02  ? 175 ASP B CG  1 
ATOM   4848  O  OD1 . ASP B  1 175 ? 12.932  11.290  63.261  1.00 67.30  ? 175 ASP B OD1 1 
ATOM   4849  O  OD2 . ASP B  1 175 ? 11.163  12.448  63.896  1.00 73.33  ? 175 ASP B OD2 1 
ATOM   4850  N  N   . ASN B  1 176 ? 16.154  11.901  62.333  1.00 39.88  ? 176 ASN B N   1 
ATOM   4851  C  CA  . ASN B  1 176 ? 16.596  11.505  60.994  1.00 41.83  ? 176 ASN B CA  1 
ATOM   4852  C  C   . ASN B  1 176 ? 15.551  10.954  60.033  1.00 42.50  ? 176 ASN B C   1 
ATOM   4853  O  O   . ASN B  1 176 ? 15.844  10.635  58.879  1.00 39.89  ? 176 ASN B O   1 
ATOM   4854  C  CB  . ASN B  1 176 ? 17.784  10.554  61.053  1.00 40.75  ? 176 ASN B CB  1 
ATOM   4855  C  CG  . ASN B  1 176 ? 19.071  11.265  61.338  1.00 38.97  ? 176 ASN B CG  1 
ATOM   4856  O  OD1 . ASN B  1 176 ? 20.124  10.839  60.880  1.00 34.01  ? 176 ASN B OD1 1 
ATOM   4857  N  ND2 . ASN B  1 176 ? 19.009  12.329  62.150  1.00 30.69  ? 176 ASN B ND2 1 
ATOM   4858  N  N   . VAL B  1 177 ? 14.309  10.864  60.470  1.00 46.77  ? 177 VAL B N   1 
ATOM   4859  C  CA  . VAL B  1 177 ? 13.306  10.347  59.553  1.00 50.73  ? 177 VAL B CA  1 
ATOM   4860  C  C   . VAL B  1 177 ? 13.163  11.391  58.492  1.00 49.80  ? 177 VAL B C   1 
ATOM   4861  O  O   . VAL B  1 177 ? 12.961  11.067  57.306  1.00 48.68  ? 177 VAL B O   1 
ATOM   4862  C  CB  . VAL B  1 177 ? 11.927  10.146  60.196  1.00 49.78  ? 177 VAL B CB  1 
ATOM   4863  C  CG1 . VAL B  1 177 ? 10.874  9.921   59.111  1.00 53.99  ? 177 VAL B CG1 1 
ATOM   4864  C  CG2 . VAL B  1 177 ? 11.950  8.933   61.023  1.00 55.08  ? 177 VAL B CG2 1 
ATOM   4865  N  N   . ARG B  1 178 ? 13.294  12.643  58.937  1.00 45.03  ? 178 ARG B N   1 
ATOM   4866  C  CA  . ARG B  1 178 ? 13.158  13.766  58.058  1.00 44.55  ? 178 ARG B CA  1 
ATOM   4867  C  C   . ARG B  1 178 ? 14.222  13.730  56.984  1.00 46.25  ? 178 ARG B C   1 
ATOM   4868  O  O   . ARG B  1 178 ? 14.095  14.388  55.964  1.00 48.45  ? 178 ARG B O   1 
ATOM   4869  C  CB  . ARG B  1 178 ? 13.123  15.054  58.830  1.00 46.74  ? 178 ARG B CB  1 
ATOM   4870  C  CG  . ARG B  1 178 ? 11.734  15.322  59.454  1.00 55.78  ? 178 ARG B CG  1 
ATOM   4871  C  CD  . ARG B  1 178 ? 10.615  15.487  58.392  1.00 56.21  ? 178 ARG B CD  1 
ATOM   4872  N  NE  . ARG B  1 178 ? 9.331   15.899  58.981  1.00 58.11  ? 178 ARG B NE  1 
ATOM   4873  C  CZ  . ARG B  1 178 ? 8.249   16.259  58.281  1.00 54.49  ? 178 ARG B CZ  1 
ATOM   4874  N  NH1 . ARG B  1 178 ? 8.273   16.277  56.957  1.00 50.99  ? 178 ARG B NH1 1 
ATOM   4875  N  NH2 . ARG B  1 178 ? 7.128   16.587  58.913  1.00 54.15  ? 178 ARG B NH2 1 
ATOM   4876  N  N   . TRP B  1 179 ? 15.251  12.914  57.185  1.00 45.01  ? 179 TRP B N   1 
ATOM   4877  C  CA  . TRP B  1 179 ? 16.257  12.751  56.155  1.00 41.57  ? 179 TRP B CA  1 
ATOM   4878  C  C   . TRP B  1 179 ? 15.699  11.762  55.181  1.00 40.82  ? 179 TRP B C   1 
ATOM   4879  O  O   . TRP B  1 179 ? 15.927  11.879  53.988  1.00 45.03  ? 179 TRP B O   1 
ATOM   4880  C  CB  . TRP B  1 179 ? 17.569  12.214  56.709  1.00 38.19  ? 179 TRP B CB  1 
ATOM   4881  C  CG  . TRP B  1 179 ? 18.549  13.275  57.061  1.00 32.52  ? 179 TRP B CG  1 
ATOM   4882  C  CD1 . TRP B  1 179 ? 18.899  13.667  58.306  1.00 28.69  ? 179 TRP B CD1 1 
ATOM   4883  C  CD2 . TRP B  1 179 ? 19.310  14.082  56.150  1.00 31.08  ? 179 TRP B CD2 1 
ATOM   4884  N  NE1 . TRP B  1 179 ? 19.828  14.672  58.239  1.00 33.42  ? 179 TRP B NE1 1 
ATOM   4885  C  CE2 . TRP B  1 179 ? 20.099  14.946  56.923  1.00 32.37  ? 179 TRP B CE2 1 
ATOM   4886  C  CE3 . TRP B  1 179 ? 19.396  14.162  54.753  1.00 29.77  ? 179 TRP B CE3 1 
ATOM   4887  C  CZ2 . TRP B  1 179 ? 20.970  15.876  56.342  1.00 29.54  ? 179 TRP B CZ2 1 
ATOM   4888  C  CZ3 . TRP B  1 179 ? 20.253  15.080  54.184  1.00 24.05  ? 179 TRP B CZ3 1 
ATOM   4889  C  CH2 . TRP B  1 179 ? 21.028  15.925  54.969  1.00 25.86  ? 179 TRP B CH2 1 
ATOM   4890  N  N   . ASP B  1 180 ? 15.005  10.756  55.699  1.00 44.68  ? 180 ASP B N   1 
ATOM   4891  C  CA  . ASP B  1 180 ? 14.402  9.729   54.852  1.00 45.13  ? 180 ASP B CA  1 
ATOM   4892  C  C   . ASP B  1 180 ? 13.308  10.323  53.979  1.00 44.42  ? 180 ASP B C   1 
ATOM   4893  O  O   . ASP B  1 180 ? 13.245  10.033  52.781  1.00 44.15  ? 180 ASP B O   1 
ATOM   4894  C  CB  . ASP B  1 180 ? 13.817  8.597   55.696  1.00 46.78  ? 180 ASP B CB  1 
ATOM   4895  C  CG  . ASP B  1 180 ? 14.878  7.790   56.412  1.00 49.87  ? 180 ASP B CG  1 
ATOM   4896  O  OD1 . ASP B  1 180 ? 15.905  7.459   55.786  1.00 42.76  ? 180 ASP B OD1 1 
ATOM   4897  O  OD2 . ASP B  1 180 ? 14.667  7.481   57.611  1.00 54.01  ? 180 ASP B OD2 1 
ATOM   4898  N  N   . THR B  1 181 ? 12.454  11.158  54.558  1.00 40.13  ? 181 THR B N   1 
ATOM   4899  C  CA  . THR B  1 181 ? 11.392  11.761  53.783  1.00 37.18  ? 181 THR B CA  1 
ATOM   4900  C  C   . THR B  1 181 ? 11.966  12.648  52.710  1.00 39.70  ? 181 THR B C   1 
ATOM   4901  O  O   . THR B  1 181 ? 11.588  12.520  51.552  1.00 44.17  ? 181 THR B O   1 
ATOM   4902  C  CB  . THR B  1 181 ? 10.458  12.563  54.644  1.00 36.44  ? 181 THR B CB  1 
ATOM   4903  O  OG1 . THR B  1 181 ? 11.178  13.599  55.303  1.00 35.57  ? 181 THR B OG1 1 
ATOM   4904  C  CG2 . THR B  1 181 ? 9.837   11.656  55.702  1.00 39.26  ? 181 THR B CG2 1 
ATOM   4905  N  N   . TRP B  1 182 ? 12.962  13.455  53.060  1.00 38.45  ? 182 TRP B N   1 
ATOM   4906  C  CA  . TRP B  1 182 ? 13.576  14.348  52.085  1.00 37.33  ? 182 TRP B CA  1 
ATOM   4907  C  C   . TRP B  1 182 ? 14.146  13.572  50.922  1.00 36.14  ? 182 TRP B C   1 
ATOM   4908  O  O   . TRP B  1 182 ? 14.038  13.955  49.769  1.00 43.17  ? 182 TRP B O   1 
ATOM   4909  C  CB  . TRP B  1 182 ? 14.690  15.176  52.716  1.00 38.54  ? 182 TRP B CB  1 
ATOM   4910  C  CG  . TRP B  1 182 ? 15.132  16.345  51.864  1.00 39.62  ? 182 TRP B CG  1 
ATOM   4911  C  CD1 . TRP B  1 182 ? 14.549  17.577  51.797  1.00 37.91  ? 182 TRP B CD1 1 
ATOM   4912  C  CD2 . TRP B  1 182 ? 16.259  16.390  50.991  1.00 41.43  ? 182 TRP B CD2 1 
ATOM   4913  N  NE1 . TRP B  1 182 ? 15.239  18.385  50.944  1.00 40.24  ? 182 TRP B NE1 1 
ATOM   4914  C  CE2 . TRP B  1 182 ? 16.304  17.693  50.440  1.00 40.96  ? 182 TRP B CE2 1 
ATOM   4915  C  CE3 . TRP B  1 182 ? 17.244  15.466  50.632  1.00 40.04  ? 182 TRP B CE3 1 
ATOM   4916  C  CZ2 . TRP B  1 182 ? 17.292  18.096  49.558  1.00 42.66  ? 182 TRP B CZ2 1 
ATOM   4917  C  CZ3 . TRP B  1 182 ? 18.231  15.870  49.754  1.00 48.00  ? 182 TRP B CZ3 1 
ATOM   4918  C  CH2 . TRP B  1 182 ? 18.249  17.182  49.227  1.00 47.22  ? 182 TRP B CH2 1 
ATOM   4919  N  N   . GLY B  1 183 ? 14.746  12.452  51.217  1.00 33.86  ? 183 GLY B N   1 
ATOM   4920  C  CA  . GLY B  1 183 ? 15.340  11.683  50.152  1.00 39.37  ? 183 GLY B CA  1 
ATOM   4921  C  C   . GLY B  1 183 ? 14.347  11.065  49.224  1.00 45.80  ? 183 GLY B C   1 
ATOM   4922  O  O   . GLY B  1 183 ? 14.695  10.728  48.081  1.00 53.50  ? 183 GLY B O   1 
ATOM   4923  N  N   . ARG B  1 184 ? 13.147  10.814  49.746  1.00 48.89  ? 184 ARG B N   1 
ATOM   4924  C  CA  . ARG B  1 184 ? 12.062  10.215  48.956  1.00 47.55  ? 184 ARG B CA  1 
ATOM   4925  C  C   . ARG B  1 184 ? 11.444  11.334  48.111  1.00 46.50  ? 184 ARG B C   1 
ATOM   4926  O  O   . ARG B  1 184 ? 11.137  11.149  46.929  1.00 44.69  ? 184 ARG B O   1 
ATOM   4927  C  CB  . ARG B  1 184 ? 11.013  9.601   49.894  1.00 48.19  ? 184 ARG B CB  1 
ATOM   4928  C  CG  . ARG B  1 184 ? 11.193  8.115   50.206  1.00 50.16  ? 184 ARG B CG  1 
ATOM   4929  C  CD  . ARG B  1 184 ? 10.052  7.620   51.121  1.00 49.17  ? 184 ARG B CD  1 
ATOM   4930  N  NE  . ARG B  1 184 ? 10.532  7.123   52.415  1.00 50.53  ? 184 ARG B NE  1 
ATOM   4931  C  CZ  . ARG B  1 184 ? 9.982   7.419   53.592  1.00 55.01  ? 184 ARG B CZ  1 
ATOM   4932  N  NH1 . ARG B  1 184 ? 8.933   8.235   53.664  1.00 53.81  ? 184 ARG B NH1 1 
ATOM   4933  N  NH2 . ARG B  1 184 ? 10.465  6.879   54.712  1.00 61.24  ? 184 ARG B NH2 1 
ATOM   4934  N  N   . PHE B  1 185 ? 11.295  12.497  48.742  1.00 44.73  ? 185 PHE B N   1 
ATOM   4935  C  CA  . PHE B  1 185 ? 10.752  13.684  48.120  1.00 42.70  ? 185 PHE B CA  1 
ATOM   4936  C  C   . PHE B  1 185 ? 11.508  14.089  46.870  1.00 45.91  ? 185 PHE B C   1 
ATOM   4937  O  O   . PHE B  1 185 ? 10.904  14.267  45.813  1.00 53.26  ? 185 PHE B O   1 
ATOM   4938  C  CB  . PHE B  1 185 ? 10.753  14.813  49.143  1.00 40.28  ? 185 PHE B CB  1 
ATOM   4939  C  CG  . PHE B  1 185 ? 10.686  16.190  48.556  1.00 38.98  ? 185 PHE B CG  1 
ATOM   4940  C  CD1 . PHE B  1 185 ? 9.898   16.466  47.450  1.00 31.17  ? 185 PHE B CD1 1 
ATOM   4941  C  CD2 . PHE B  1 185 ? 11.374  17.231  49.164  1.00 40.49  ? 185 PHE B CD2 1 
ATOM   4942  C  CE1 . PHE B  1 185 ? 9.795   17.737  46.978  1.00 32.43  ? 185 PHE B CE1 1 
ATOM   4943  C  CE2 . PHE B  1 185 ? 11.270  18.514  48.690  1.00 39.48  ? 185 PHE B CE2 1 
ATOM   4944  C  CZ  . PHE B  1 185 ? 10.478  18.768  47.596  1.00 32.58  ? 185 PHE B CZ  1 
ATOM   4945  N  N   . THR B  1 186 ? 12.821  14.204  46.981  1.00 46.11  ? 186 THR B N   1 
ATOM   4946  C  CA  . THR B  1 186 ? 13.671  14.632  45.881  1.00 44.98  ? 186 THR B CA  1 
ATOM   4947  C  C   . THR B  1 186 ? 13.962  13.597  44.810  1.00 45.20  ? 186 THR B C   1 
ATOM   4948  O  O   . THR B  1 186 ? 14.382  13.957  43.712  1.00 48.99  ? 186 THR B O   1 
ATOM   4949  C  CB  . THR B  1 186 ? 15.009  15.187  46.436  1.00 44.68  ? 186 THR B CB  1 
ATOM   4950  O  OG1 . THR B  1 186 ? 15.629  14.203  47.279  1.00 52.35  ? 186 THR B OG1 1 
ATOM   4951  C  CG2 . THR B  1 186 ? 14.767  16.444  47.297  1.00 43.96  ? 186 THR B CG2 1 
ATOM   4952  N  N   . GLU B  1 187 ? 13.695  12.328  45.104  1.00 47.98  ? 187 GLU B N   1 
ATOM   4953  C  CA  . GLU B  1 187 ? 13.987  11.217  44.189  1.00 48.71  ? 187 GLU B CA  1 
ATOM   4954  C  C   . GLU B  1 187 ? 13.546  11.455  42.793  1.00 48.60  ? 187 GLU B C   1 
ATOM   4955  O  O   . GLU B  1 187 ? 14.236  11.058  41.850  1.00 52.41  ? 187 GLU B O   1 
ATOM   4956  C  CB  . GLU B  1 187 ? 13.343  9.915   44.654  1.00 54.60  ? 187 GLU B CB  1 
ATOM   4957  C  CG  . GLU B  1 187 ? 13.830  8.645   43.916  1.00 63.88  ? 187 GLU B CG  1 
ATOM   4958  C  CD  . GLU B  1 187 ? 13.018  7.396   44.288  1.00 68.35  ? 187 GLU B CD  1 
ATOM   4959  O  OE1 . GLU B  1 187 ? 11.988  7.210   43.646  1.00 72.21  ? 187 GLU B OE1 1 
ATOM   4960  O  OE2 . GLU B  1 187 ? 13.369  6.619   45.215  1.00 74.52  ? 187 GLU B OE2 1 
ATOM   4961  N  N   . ARG B  1 188 ? 12.414  12.137  42.654  1.00 46.25  ? 188 ARG B N   1 
ATOM   4962  C  CA  . ARG B  1 188 ? 11.878  12.391  41.329  1.00 44.26  ? 188 ARG B CA  1 
ATOM   4963  C  C   . ARG B  1 188 ? 12.836  13.158  40.433  1.00 45.08  ? 188 ARG B C   1 
ATOM   4964  O  O   . ARG B  1 188 ? 12.791  13.014  39.221  1.00 50.46  ? 188 ARG B O   1 
ATOM   4965  C  CB  . ARG B  1 188 ? 10.511  13.056  41.406  1.00 39.82  ? 188 ARG B CB  1 
ATOM   4966  C  CG  . ARG B  1 188 ? 10.480  14.486  41.841  1.00 39.88  ? 188 ARG B CG  1 
ATOM   4967  C  CD  . ARG B  1 188 ? 9.065   14.808  42.293  1.00 39.90  ? 188 ARG B CD  1 
ATOM   4968  N  NE  . ARG B  1 188 ? 8.646   16.174  41.982  1.00 46.25  ? 188 ARG B NE  1 
ATOM   4969  C  CZ  . ARG B  1 188 ? 7.995   16.951  42.843  1.00 47.95  ? 188 ARG B CZ  1 
ATOM   4970  N  NH1 . ARG B  1 188 ? 7.690   16.490  44.048  1.00 46.18  ? 188 ARG B NH1 1 
ATOM   4971  N  NH2 . ARG B  1 188 ? 7.699   18.204  42.523  1.00 54.91  ? 188 ARG B NH2 1 
ATOM   4972  N  N   . SER B  1 189 ? 13.722  13.943  41.022  1.00 41.27  ? 189 SER B N   1 
ATOM   4973  C  CA  . SER B  1 189 ? 14.663  14.660  40.227  1.00 37.39  ? 189 SER B CA  1 
ATOM   4974  C  C   . SER B  1 189 ? 15.993  13.938  40.202  1.00 38.14  ? 189 SER B C   1 
ATOM   4975  O  O   . SER B  1 189 ? 16.462  13.468  39.152  1.00 39.79  ? 189 SER B O   1 
ATOM   4976  C  CB  . SER B  1 189 ? 14.858  16.029  40.787  1.00 36.54  ? 189 SER B CB  1 
ATOM   4977  O  OG  . SER B  1 189 ? 15.663  16.727  39.871  1.00 38.83  ? 189 SER B OG  1 
ATOM   4978  N  N   . VAL B  1 190 ? 16.572  13.787  41.384  1.00 34.17  ? 190 VAL B N   1 
ATOM   4979  C  CA  . VAL B  1 190 ? 17.876  13.139  41.514  1.00 32.65  ? 190 VAL B CA  1 
ATOM   4980  C  C   . VAL B  1 190 ? 18.063  11.734  41.021  1.00 31.79  ? 190 VAL B C   1 
ATOM   4981  O  O   . VAL B  1 190 ? 19.198  11.284  40.882  1.00 34.39  ? 190 VAL B O   1 
ATOM   4982  C  CB  . VAL B  1 190 ? 18.358  13.052  42.919  1.00 28.73  ? 190 VAL B CB  1 
ATOM   4983  C  CG1 . VAL B  1 190 ? 19.675  13.693  43.001  1.00 31.00  ? 190 VAL B CG1 1 
ATOM   4984  C  CG2 . VAL B  1 190 ? 17.377  13.628  43.875  1.00 32.68  ? 190 VAL B CG2 1 
ATOM   4985  N  N   . ALA B  1 191 ? 16.986  10.989  40.858  1.00 28.31  ? 191 ALA B N   1 
ATOM   4986  C  CA  . ALA B  1 191 ? 17.161  9.637   40.411  1.00 28.03  ? 191 ALA B CA  1 
ATOM   4987  C  C   . ALA B  1 191 ? 17.503  9.674   38.972  1.00 31.97  ? 191 ALA B C   1 
ATOM   4988  O  O   . ALA B  1 191 ? 18.055  8.715   38.449  1.00 32.93  ? 191 ALA B O   1 
ATOM   4989  C  CB  . ALA B  1 191 ? 15.927  8.860   40.621  1.00 26.68  ? 191 ALA B CB  1 
ATOM   4990  N  N   . TYR B  1 192 ? 17.216  10.802  38.329  1.00 38.89  ? 192 TYR B N   1 
ATOM   4991  C  CA  . TYR B  1 192 ? 17.460  10.908  36.888  1.00 47.20  ? 192 TYR B CA  1 
ATOM   4992  C  C   . TYR B  1 192 ? 18.564  11.846  36.418  1.00 51.68  ? 192 TYR B C   1 
ATOM   4993  O  O   . TYR B  1 192 ? 19.152  11.646  35.325  1.00 51.94  ? 192 TYR B O   1 
ATOM   4994  C  CB  . TYR B  1 192 ? 16.182  11.265  36.178  1.00 49.11  ? 192 TYR B CB  1 
ATOM   4995  C  CG  . TYR B  1 192 ? 15.043  10.383  36.565  1.00 52.91  ? 192 TYR B CG  1 
ATOM   4996  C  CD1 . TYR B  1 192 ? 14.796  9.195   35.860  1.00 55.36  ? 192 TYR B CD1 1 
ATOM   4997  C  CD2 . TYR B  1 192 ? 14.204  10.733  37.629  1.00 50.27  ? 192 TYR B CD2 1 
ATOM   4998  C  CE1 . TYR B  1 192 ? 13.741  8.370   36.198  1.00 58.13  ? 192 TYR B CE1 1 
ATOM   4999  C  CE2 . TYR B  1 192 ? 13.155  9.929   37.977  1.00 54.70  ? 192 TYR B CE2 1 
ATOM   5000  C  CZ  . TYR B  1 192 ? 12.918  8.739   37.259  1.00 58.53  ? 192 TYR B CZ  1 
ATOM   5001  O  OH  . TYR B  1 192 ? 11.857  7.921   37.610  1.00 64.20  ? 192 TYR B OH  1 
ATOM   5002  N  N   . GLN B  1 193 ? 18.800  12.910  37.182  1.00 49.74  ? 193 GLN B N   1 
ATOM   5003  C  CA  . GLN B  1 193 ? 19.864  13.808  36.806  1.00 45.84  ? 193 GLN B CA  1 
ATOM   5004  C  C   . GLN B  1 193 ? 20.655  14.090  38.030  1.00 45.41  ? 193 GLN B C   1 
ATOM   5005  O  O   . GLN B  1 193 ? 20.085  14.258  39.113  1.00 46.15  ? 193 GLN B O   1 
ATOM   5006  C  CB  . GLN B  1 193 ? 19.327  15.095  36.208  1.00 48.80  ? 193 GLN B CB  1 
ATOM   5007  C  CG  . GLN B  1 193 ? 18.616  16.042  37.181  1.00 53.83  ? 193 GLN B CG  1 
ATOM   5008  C  CD  . GLN B  1 193 ? 18.343  17.419  36.560  1.00 50.70  ? 193 GLN B CD  1 
ATOM   5009  O  OE1 . GLN B  1 193 ? 19.075  18.376  36.784  1.00 52.28  ? 193 GLN B OE1 1 
ATOM   5010  N  NE2 . GLN B  1 193 ? 17.289  17.509  35.774  1.00 57.89  ? 193 GLN B NE2 1 
ATOM   5011  N  N   . PRO B  1 194 ? 21.989  14.085  37.897  1.00 44.98  ? 194 PRO B N   1 
ATOM   5012  C  CA  . PRO B  1 194 ? 22.866  14.351  39.033  1.00 42.78  ? 194 PRO B CA  1 
ATOM   5013  C  C   . PRO B  1 194 ? 22.658  15.690  39.692  1.00 38.57  ? 194 PRO B C   1 
ATOM   5014  O  O   . PRO B  1 194 ? 22.232  16.629  39.043  1.00 38.58  ? 194 PRO B O   1 
ATOM   5015  C  CB  . PRO B  1 194 ? 24.274  14.286  38.407  1.00 42.06  ? 194 PRO B CB  1 
ATOM   5016  C  CG  . PRO B  1 194 ? 24.049  14.673  37.009  1.00 45.44  ? 194 PRO B CG  1 
ATOM   5017  C  CD  . PRO B  1 194 ? 22.795  13.874  36.680  1.00 45.44  ? 194 PRO B CD  1 
ATOM   5018  N  N   . TRP B  1 195 ? 22.867  15.716  41.008  1.00 37.50  ? 195 TRP B N   1 
ATOM   5019  C  CA  . TRP B  1 195 ? 22.841  16.935  41.804  1.00 36.77  ? 195 TRP B CA  1 
ATOM   5020  C  C   . TRP B  1 195 ? 24.280  17.001  42.407  1.00 36.81  ? 195 TRP B C   1 
ATOM   5021  O  O   . TRP B  1 195 ? 24.844  15.990  42.833  1.00 37.66  ? 195 TRP B O   1 
ATOM   5022  C  CB  . TRP B  1 195 ? 21.757  16.920  42.900  1.00 34.97  ? 195 TRP B CB  1 
ATOM   5023  C  CG  . TRP B  1 195 ? 20.298  17.140  42.441  1.00 34.57  ? 195 TRP B CG  1 
ATOM   5024  C  CD1 . TRP B  1 195 ? 19.713  16.705  41.277  1.00 36.77  ? 195 TRP B CD1 1 
ATOM   5025  C  CD2 . TRP B  1 195 ? 19.248  17.759  43.198  1.00 29.20  ? 195 TRP B CD2 1 
ATOM   5026  N  NE1 . TRP B  1 195 ? 18.366  17.003  41.279  1.00 36.26  ? 195 TRP B NE1 1 
ATOM   5027  C  CE2 . TRP B  1 195 ? 18.059  17.652  42.442  1.00 28.25  ? 195 TRP B CE2 1 
ATOM   5028  C  CE3 . TRP B  1 195 ? 19.200  18.396  44.441  1.00 28.39  ? 195 TRP B CE3 1 
ATOM   5029  C  CZ2 . TRP B  1 195 ? 16.853  18.147  42.884  1.00 27.77  ? 195 TRP B CZ2 1 
ATOM   5030  C  CZ3 . TRP B  1 195 ? 17.988  18.901  44.879  1.00 27.80  ? 195 TRP B CZ3 1 
ATOM   5031  C  CH2 . TRP B  1 195 ? 16.834  18.774  44.102  1.00 28.62  ? 195 TRP B CH2 1 
ATOM   5032  N  N   . ILE B  1 196 ? 24.926  18.158  42.301  1.00 36.03  ? 196 ILE B N   1 
ATOM   5033  C  CA  . ILE B  1 196 ? 26.273  18.326  42.831  1.00 30.97  ? 196 ILE B CA  1 
ATOM   5034  C  C   . ILE B  1 196 ? 26.096  18.882  44.218  1.00 30.14  ? 196 ILE B C   1 
ATOM   5035  O  O   . ILE B  1 196 ? 25.510  19.955  44.382  1.00 27.93  ? 196 ILE B O   1 
ATOM   5036  C  CB  . ILE B  1 196 ? 27.079  19.270  41.971  1.00 32.00  ? 196 ILE B CB  1 
ATOM   5037  C  CG1 . ILE B  1 196 ? 27.040  18.798  40.508  1.00 36.14  ? 196 ILE B CG1 1 
ATOM   5038  C  CG2 . ILE B  1 196 ? 28.487  19.287  42.441  1.00 34.22  ? 196 ILE B CG2 1 
ATOM   5039  C  CD1 . ILE B  1 196 ? 27.339  17.309  40.322  1.00 34.77  ? 196 ILE B CD1 1 
ATOM   5040  N  N   . TRP B  1 197 ? 26.578  18.147  45.221  1.00 28.67  ? 197 TRP B N   1 
ATOM   5041  C  CA  . TRP B  1 197 ? 26.371  18.510  46.625  1.00 24.99  ? 197 TRP B CA  1 
ATOM   5042  C  C   . TRP B  1 197 ? 27.347  19.464  47.254  1.00 25.42  ? 197 TRP B C   1 
ATOM   5043  O  O   . TRP B  1 197 ? 28.544  19.414  47.015  1.00 31.80  ? 197 TRP B O   1 
ATOM   5044  C  CB  . TRP B  1 197 ? 26.228  17.249  47.496  1.00 23.33  ? 197 TRP B CB  1 
ATOM   5045  C  CG  . TRP B  1 197 ? 25.196  16.280  47.000  1.00 28.32  ? 197 TRP B CG  1 
ATOM   5046  C  CD1 . TRP B  1 197 ? 25.414  15.073  46.345  1.00 35.79  ? 197 TRP B CD1 1 
ATOM   5047  C  CD2 . TRP B  1 197 ? 23.792  16.460  47.022  1.00 27.57  ? 197 TRP B CD2 1 
ATOM   5048  N  NE1 . TRP B  1 197 ? 24.215  14.508  45.955  1.00 34.45  ? 197 TRP B NE1 1 
ATOM   5049  C  CE2 . TRP B  1 197 ? 23.205  15.345  46.355  1.00 29.82  ? 197 TRP B CE2 1 
ATOM   5050  C  CE3 . TRP B  1 197 ? 22.960  17.464  47.525  1.00 29.18  ? 197 TRP B CE3 1 
ATOM   5051  C  CZ2 . TRP B  1 197 ? 21.847  15.225  46.187  1.00 26.32  ? 197 TRP B CZ2 1 
ATOM   5052  C  CZ3 . TRP B  1 197 ? 21.610  17.350  47.361  1.00 29.43  ? 197 TRP B CZ3 1 
ATOM   5053  C  CH2 . TRP B  1 197 ? 21.059  16.242  46.698  1.00 31.45  ? 197 TRP B CH2 1 
ATOM   5054  N  N   . THR B  1 198 ? 26.819  20.260  48.162  1.00 21.66  ? 198 THR B N   1 
ATOM   5055  C  CA  . THR B  1 198 ? 27.606  21.235  48.850  1.00 24.63  ? 198 THR B CA  1 
ATOM   5056  C  C   . THR B  1 198 ? 27.095  21.177  50.248  1.00 27.12  ? 198 THR B C   1 
ATOM   5057  O  O   . THR B  1 198 ? 25.905  21.136  50.455  1.00 33.48  ? 198 THR B O   1 
ATOM   5058  C  CB  . THR B  1 198 ? 27.381  22.650  48.325  1.00 20.13  ? 198 THR B CB  1 
ATOM   5059  O  OG1 . THR B  1 198 ? 27.768  22.716  46.955  1.00 27.78  ? 198 THR B OG1 1 
ATOM   5060  C  CG2 . THR B  1 198 ? 28.250  23.583  49.064  1.00 26.35  ? 198 THR B CG2 1 
ATOM   5061  N  N   . ALA B  1 199 ? 27.987  21.256  51.213  1.00 25.29  ? 199 ALA B N   1 
ATOM   5062  C  CA  . ALA B  1 199 ? 27.606  21.135  52.580  1.00 22.90  ? 199 ALA B CA  1 
ATOM   5063  C  C   . ALA B  1 199 ? 27.244  22.430  53.207  1.00 23.56  ? 199 ALA B C   1 
ATOM   5064  O  O   . ALA B  1 199 ? 28.044  23.352  53.212  1.00 28.50  ? 199 ALA B O   1 
ATOM   5065  C  CB  . ALA B  1 199 ? 28.741  20.502  53.336  1.00 26.49  ? 199 ALA B CB  1 
ATOM   5066  N  N   . GLY B  1 200 ? 26.107  22.459  53.876  1.00 18.99  ? 200 GLY B N   1 
ATOM   5067  C  CA  . GLY B  1 200 ? 25.688  23.682  54.498  1.00 18.29  ? 200 GLY B CA  1 
ATOM   5068  C  C   . GLY B  1 200 ? 25.680  23.481  55.974  1.00 28.44  ? 200 GLY B C   1 
ATOM   5069  O  O   . GLY B  1 200 ? 25.922  22.359  56.406  1.00 33.81  ? 200 GLY B O   1 
ATOM   5070  N  N   . ASN B  1 201 ? 25.359  24.527  56.749  1.00 32.27  ? 201 ASN B N   1 
ATOM   5071  C  CA  . ASN B  1 201 ? 25.319  24.432  58.206  1.00 34.08  ? 201 ASN B CA  1 
ATOM   5072  C  C   . ASN B  1 201 ? 24.284  23.465  58.738  1.00 36.49  ? 201 ASN B C   1 
ATOM   5073  O  O   . ASN B  1 201 ? 24.480  22.818  59.768  1.00 37.63  ? 201 ASN B O   1 
ATOM   5074  C  CB  . ASN B  1 201 ? 25.177  25.815  58.901  1.00 37.76  ? 201 ASN B CB  1 
ATOM   5075  C  CG  . ASN B  1 201 ? 24.075  26.659  58.334  1.00 41.41  ? 201 ASN B CG  1 
ATOM   5076  O  OD1 . ASN B  1 201 ? 23.872  26.682  57.097  1.00 43.34  ? 201 ASN B OD1 1 
ATOM   5077  N  ND2 . ASN B  1 201 ? 23.396  27.403  59.210  1.00 38.72  ? 201 ASN B ND2 1 
ATOM   5078  N  N   . HIS B  1 202 ? 23.184  23.309  58.033  1.00 41.17  ? 202 HIS B N   1 
ATOM   5079  C  CA  . HIS B  1 202 ? 22.186  22.381  58.522  1.00 44.00  ? 202 HIS B CA  1 
ATOM   5080  C  C   . HIS B  1 202 ? 22.631  20.935  58.403  1.00 40.49  ? 202 HIS B C   1 
ATOM   5081  O  O   . HIS B  1 202 ? 21.919  20.044  58.868  1.00 48.65  ? 202 HIS B O   1 
ATOM   5082  C  CB  . HIS B  1 202 ? 20.816  22.625  57.862  1.00 44.82  ? 202 HIS B CB  1 
ATOM   5083  C  CG  . HIS B  1 202 ? 20.090  23.802  58.436  1.00 41.97  ? 202 HIS B CG  1 
ATOM   5084  N  ND1 . HIS B  1 202 ? 19.280  23.703  59.547  1.00 37.66  ? 202 HIS B ND1 1 
ATOM   5085  C  CD2 . HIS B  1 202 ? 20.107  25.113  58.100  1.00 47.16  ? 202 HIS B CD2 1 
ATOM   5086  C  CE1 . HIS B  1 202 ? 18.827  24.902  59.871  1.00 43.71  ? 202 HIS B CE1 1 
ATOM   5087  N  NE2 . HIS B  1 202 ? 19.314  25.776  59.008  1.00 48.34  ? 202 HIS B NE2 1 
ATOM   5088  N  N   . GLU B  1 203 ? 23.793  20.724  57.785  1.00 33.85  ? 203 GLU B N   1 
ATOM   5089  C  CA  . GLU B  1 203 ? 24.379  19.402  57.594  1.00 31.49  ? 203 GLU B CA  1 
ATOM   5090  C  C   . GLU B  1 203 ? 25.399  19.077  58.653  1.00 31.24  ? 203 GLU B C   1 
ATOM   5091  O  O   . GLU B  1 203 ? 25.752  17.926  58.822  1.00 34.19  ? 203 GLU B O   1 
ATOM   5092  C  CB  . GLU B  1 203 ? 25.067  19.289  56.250  1.00 29.02  ? 203 GLU B CB  1 
ATOM   5093  C  CG  . GLU B  1 203 ? 24.124  18.948  55.139  1.00 35.16  ? 203 GLU B CG  1 
ATOM   5094  C  CD  . GLU B  1 203 ? 23.138  20.062  54.822  1.00 37.99  ? 203 GLU B CD  1 
ATOM   5095  O  OE1 . GLU B  1 203 ? 23.595  21.037  54.177  1.00 32.76  ? 203 GLU B OE1 1 
ATOM   5096  O  OE2 . GLU B  1 203 ? 21.927  19.958  55.203  1.00 42.47  ? 203 GLU B OE2 1 
ATOM   5097  N  N   . ILE B  1 204 ? 25.942  20.095  59.291  1.00 28.47  ? 204 ILE B N   1 
ATOM   5098  C  CA  . ILE B  1 204 ? 26.912  19.872  60.338  1.00 32.17  ? 204 ILE B CA  1 
ATOM   5099  C  C   . ILE B  1 204 ? 26.341  18.964  61.428  1.00 33.54  ? 204 ILE B C   1 
ATOM   5100  O  O   . ILE B  1 204 ? 27.000  18.025  61.852  1.00 36.95  ? 204 ILE B O   1 
ATOM   5101  C  CB  . ILE B  1 204 ? 27.307  21.166  61.015  1.00 30.44  ? 204 ILE B CB  1 
ATOM   5102  C  CG1 . ILE B  1 204 ? 27.913  22.108  60.009  1.00 30.48  ? 204 ILE B CG1 1 
ATOM   5103  C  CG2 . ILE B  1 204 ? 28.282  20.903  62.148  1.00 33.11  ? 204 ILE B CG2 1 
ATOM   5104  C  CD1 . ILE B  1 204 ? 28.158  23.496  60.628  1.00 32.41  ? 204 ILE B CD1 1 
ATOM   5105  N  N   . GLU B  1 205 ? 25.200  19.339  61.993  1.00 32.73  ? 205 GLU B N   1 
ATOM   5106  C  CA  . GLU B  1 205 ? 24.575  18.530  63.023  1.00 29.34  ? 205 GLU B CA  1 
ATOM   5107  C  C   . GLU B  1 205 ? 25.485  18.186  64.203  1.00 29.70  ? 205 GLU B C   1 
ATOM   5108  O  O   . GLU B  1 205 ? 25.694  17.026  64.563  1.00 30.27  ? 205 GLU B O   1 
ATOM   5109  C  CB  . GLU B  1 205 ? 23.997  17.270  62.408  1.00 28.01  ? 205 GLU B CB  1 
ATOM   5110  C  CG  . GLU B  1 205 ? 22.862  17.611  61.509  1.00 37.54  ? 205 GLU B CG  1 
ATOM   5111  C  CD  . GLU B  1 205 ? 22.022  16.425  61.065  1.00 41.67  ? 205 GLU B CD  1 
ATOM   5112  O  OE1 . GLU B  1 205 ? 21.125  16.010  61.835  1.00 38.23  ? 205 GLU B OE1 1 
ATOM   5113  O  OE2 . GLU B  1 205 ? 22.225  15.951  59.916  1.00 46.80  ? 205 GLU B OE2 1 
ATOM   5114  N  N   . PHE B  1 206 ? 26.029  19.217  64.809  1.00 29.62  ? 206 PHE B N   1 
ATOM   5115  C  CA  . PHE B  1 206 ? 26.882  19.026  65.942  1.00 28.39  ? 206 PHE B CA  1 
ATOM   5116  C  C   . PHE B  1 206 ? 25.934  19.049  67.145  1.00 32.51  ? 206 PHE B C   1 
ATOM   5117  O  O   . PHE B  1 206 ? 25.493  20.107  67.562  1.00 37.32  ? 206 PHE B O   1 
ATOM   5118  C  CB  . PHE B  1 206 ? 27.866  20.181  65.992  1.00 23.60  ? 206 PHE B CB  1 
ATOM   5119  C  CG  . PHE B  1 206 ? 28.785  20.142  67.159  1.00 21.63  ? 206 PHE B CG  1 
ATOM   5120  C  CD1 . PHE B  1 206 ? 29.760  19.138  67.293  1.00 25.87  ? 206 PHE B CD1 1 
ATOM   5121  C  CD2 . PHE B  1 206 ? 28.732  21.134  68.101  1.00 21.89  ? 206 PHE B CD2 1 
ATOM   5122  C  CE1 . PHE B  1 206 ? 30.677  19.148  68.361  1.00 26.10  ? 206 PHE B CE1 1 
ATOM   5123  C  CE2 . PHE B  1 206 ? 29.642  21.161  69.167  1.00 24.93  ? 206 PHE B CE2 1 
ATOM   5124  C  CZ  . PHE B  1 206 ? 30.615  20.172  69.294  1.00 27.41  ? 206 PHE B CZ  1 
ATOM   5125  N  N   . ALA B  1 207 ? 25.612  17.881  67.685  1.00 34.25  ? 207 ALA B N   1 
ATOM   5126  C  CA  . ALA B  1 207 ? 24.702  17.788  68.803  1.00 31.16  ? 207 ALA B CA  1 
ATOM   5127  C  C   . ALA B  1 207 ? 25.270  17.122  70.015  1.00 34.14  ? 207 ALA B C   1 
ATOM   5128  O  O   . ALA B  1 207 ? 24.940  15.984  70.339  1.00 40.09  ? 207 ALA B O   1 
ATOM   5129  C  CB  . ALA B  1 207 ? 23.448  17.065  68.382  1.00 34.01  ? 207 ALA B CB  1 
ATOM   5130  N  N   . PRO B  1 208 ? 26.097  17.829  70.741  1.00 33.59  ? 208 PRO B N   1 
ATOM   5131  C  CA  . PRO B  1 208 ? 26.714  17.317  71.955  1.00 36.59  ? 208 PRO B CA  1 
ATOM   5132  C  C   . PRO B  1 208 ? 25.687  16.771  72.947  1.00 40.44  ? 208 PRO B C   1 
ATOM   5133  O  O   . PRO B  1 208 ? 25.906  15.755  73.566  1.00 46.18  ? 208 PRO B O   1 
ATOM   5134  C  CB  . PRO B  1 208 ? 27.379  18.565  72.527  1.00 35.44  ? 208 PRO B CB  1 
ATOM   5135  C  CG  . PRO B  1 208 ? 27.823  19.257  71.358  1.00 40.86  ? 208 PRO B CG  1 
ATOM   5136  C  CD  . PRO B  1 208 ? 26.655  19.136  70.385  1.00 38.71  ? 208 PRO B CD  1 
ATOM   5137  N  N   . GLU B  1 209 ? 24.592  17.492  73.133  1.00 44.56  ? 209 GLU B N   1 
ATOM   5138  C  CA  . GLU B  1 209 ? 23.509  17.123  74.058  1.00 44.65  ? 209 GLU B CA  1 
ATOM   5139  C  C   . GLU B  1 209 ? 23.012  15.702  73.918  1.00 45.79  ? 209 GLU B C   1 
ATOM   5140  O  O   . GLU B  1 209 ? 22.606  15.102  74.905  1.00 47.95  ? 209 GLU B O   1 
ATOM   5141  C  CB  . GLU B  1 209 ? 22.292  18.017  73.862  1.00 50.56  ? 209 GLU B CB  1 
ATOM   5142  C  CG  . GLU B  1 209 ? 22.494  19.300  73.032  1.00 63.93  ? 209 GLU B CG  1 
ATOM   5143  C  CD  . GLU B  1 209 ? 22.457  19.105  71.502  1.00 64.77  ? 209 GLU B CD  1 
ATOM   5144  O  OE1 . GLU B  1 209 ? 21.404  18.726  70.917  1.00 64.34  ? 209 GLU B OE1 1 
ATOM   5145  O  OE2 . GLU B  1 209 ? 23.491  19.407  70.876  1.00 70.80  ? 209 GLU B OE2 1 
ATOM   5146  N  N   . ILE B  1 210 ? 22.932  15.207  72.685  1.00 45.03  ? 210 ILE B N   1 
ATOM   5147  C  CA  . ILE B  1 210 ? 22.476  13.853  72.453  1.00 42.23  ? 210 ILE B CA  1 
ATOM   5148  C  C   . ILE B  1 210 ? 23.642  13.004  72.058  1.00 44.05  ? 210 ILE B C   1 
ATOM   5149  O  O   . ILE B  1 210 ? 23.500  11.991  71.383  1.00 44.59  ? 210 ILE B O   1 
ATOM   5150  C  CB  . ILE B  1 210 ? 21.453  13.787  71.388  1.00 42.88  ? 210 ILE B CB  1 
ATOM   5151  C  CG1 . ILE B  1 210 ? 21.941  14.506  70.139  1.00 46.11  ? 210 ILE B CG1 1 
ATOM   5152  C  CG2 . ILE B  1 210 ? 20.220  14.380  71.899  1.00 42.11  ? 210 ILE B CG2 1 
ATOM   5153  C  CD1 . ILE B  1 210 ? 20.951  14.448  69.015  1.00 53.69  ? 210 ILE B CD1 1 
ATOM   5154  N  N   . ASN B  1 211 ? 24.817  13.509  72.383  1.00 45.16  ? 211 ASN B N   1 
ATOM   5155  C  CA  . ASN B  1 211 ? 26.044  12.792  72.163  1.00 50.20  ? 211 ASN B CA  1 
ATOM   5156  C  C   . ASN B  1 211 ? 26.422  12.466  70.762  1.00 45.22  ? 211 ASN B C   1 
ATOM   5157  O  O   . ASN B  1 211 ? 27.185  11.547  70.516  1.00 43.28  ? 211 ASN B O   1 
ATOM   5158  C  CB  . ASN B  1 211 ? 26.063  11.546  73.025  1.00 69.97  ? 211 ASN B CB  1 
ATOM   5159  C  CG  . ASN B  1 211 ? 26.409  11.859  74.446  1.00 88.72  ? 211 ASN B CG  1 
ATOM   5160  O  OD1 . ASN B  1 211 ? 27.605  12.033  74.740  1.00 95.16  ? 211 ASN B OD1 1 
ATOM   5161  N  ND2 . ASN B  1 211 ? 25.373  12.039  75.279  1.00 100.60 ? 211 ASN B ND2 1 
ATOM   5162  N  N   . GLU B  1 212 ? 25.935  13.264  69.843  1.00 42.49  ? 212 GLU B N   1 
ATOM   5163  C  CA  . GLU B  1 212 ? 26.278  13.106  68.455  1.00 42.88  ? 212 GLU B CA  1 
ATOM   5164  C  C   . GLU B  1 212 ? 27.215  14.283  68.210  1.00 43.47  ? 212 GLU B C   1 
ATOM   5165  O  O   . GLU B  1 212 ? 26.778  15.428  68.260  1.00 46.41  ? 212 GLU B O   1 
ATOM   5166  C  CB  . GLU B  1 212 ? 25.019  13.232  67.641  1.00 43.24  ? 212 GLU B CB  1 
ATOM   5167  C  CG  . GLU B  1 212 ? 24.233  11.999  67.733  1.00 42.90  ? 212 GLU B CG  1 
ATOM   5168  C  CD  . GLU B  1 212 ? 25.072  10.828  67.310  1.00 45.18  ? 212 GLU B CD  1 
ATOM   5169  O  OE1 . GLU B  1 212 ? 25.824  10.925  66.312  1.00 51.60  ? 212 GLU B OE1 1 
ATOM   5170  O  OE2 . GLU B  1 212 ? 25.019  9.812   67.996  1.00 46.98  ? 212 GLU B OE2 1 
ATOM   5171  N  N   . THR B  1 213 ? 28.504  14.028  68.012  1.00 41.60  ? 213 THR B N   1 
ATOM   5172  C  CA  . THR B  1 213 ? 29.449  15.133  67.857  1.00 40.60  ? 213 THR B CA  1 
ATOM   5173  C  C   . THR B  1 213 ? 30.414  15.027  66.702  1.00 42.40  ? 213 THR B C   1 
ATOM   5174  O  O   . THR B  1 213 ? 31.469  15.682  66.720  1.00 41.73  ? 213 THR B O   1 
ATOM   5175  C  CB  . THR B  1 213 ? 30.310  15.310  69.109  1.00 46.16  ? 213 THR B CB  1 
ATOM   5176  O  OG1 . THR B  1 213 ? 31.093  14.123  69.331  1.00 56.46  ? 213 THR B OG1 1 
ATOM   5177  C  CG2 . THR B  1 213 ? 29.443  15.563  70.319  1.00 50.37  ? 213 THR B CG2 1 
ATOM   5178  N  N   . GLU B  1 214 ? 30.092  14.177  65.729  1.00 43.67  ? 214 GLU B N   1 
ATOM   5179  C  CA  . GLU B  1 214 ? 30.924  14.013  64.550  1.00 41.59  ? 214 GLU B CA  1 
ATOM   5180  C  C   . GLU B  1 214 ? 30.155  14.777  63.484  1.00 38.45  ? 214 GLU B C   1 
ATOM   5181  O  O   . GLU B  1 214 ? 29.045  14.378  63.078  1.00 43.69  ? 214 GLU B O   1 
ATOM   5182  C  CB  . GLU B  1 214 ? 31.036  12.544  64.177  1.00 53.72  ? 214 GLU B CB  1 
ATOM   5183  C  CG  . GLU B  1 214 ? 32.056  12.233  63.074  1.00 73.26  ? 214 GLU B CG  1 
ATOM   5184  C  CD  . GLU B  1 214 ? 31.693  10.969  62.255  1.00 85.75  ? 214 GLU B CD  1 
ATOM   5185  O  OE1 . GLU B  1 214 ? 31.361  9.917   62.872  1.00 92.14  ? 214 GLU B OE1 1 
ATOM   5186  O  OE2 . GLU B  1 214 ? 31.730  11.037  60.989  1.00 92.79  ? 214 GLU B OE2 1 
ATOM   5187  N  N   . PRO B  1 215 ? 30.696  15.927  63.071  1.00 32.76  ? 215 PRO B N   1 
ATOM   5188  C  CA  . PRO B  1 215 ? 30.110  16.809  62.071  1.00 30.06  ? 215 PRO B CA  1 
ATOM   5189  C  C   . PRO B  1 215 ? 29.800  16.133  60.785  1.00 31.54  ? 215 PRO B C   1 
ATOM   5190  O  O   . PRO B  1 215 ? 30.515  15.251  60.343  1.00 37.31  ? 215 PRO B O   1 
ATOM   5191  C  CB  . PRO B  1 215 ? 31.179  17.848  61.879  1.00 28.97  ? 215 PRO B CB  1 
ATOM   5192  C  CG  . PRO B  1 215 ? 31.776  17.955  63.266  1.00 30.91  ? 215 PRO B CG  1 
ATOM   5193  C  CD  . PRO B  1 215 ? 31.938  16.503  63.604  1.00 30.75  ? 215 PRO B CD  1 
ATOM   5194  N  N   . PHE B  1 216 ? 28.717  16.565  60.174  1.00 29.33  ? 216 PHE B N   1 
ATOM   5195  C  CA  . PHE B  1 216 ? 28.309  16.037  58.908  1.00 29.57  ? 216 PHE B CA  1 
ATOM   5196  C  C   . PHE B  1 216 ? 28.039  14.550  58.890  1.00 32.31  ? 216 PHE B C   1 
ATOM   5197  O  O   . PHE B  1 216 ? 27.980  13.967  57.810  1.00 32.72  ? 216 PHE B O   1 
ATOM   5198  C  CB  . PHE B  1 216 ? 29.351  16.369  57.857  1.00 31.76  ? 216 PHE B CB  1 
ATOM   5199  C  CG  . PHE B  1 216 ? 29.617  17.844  57.708  1.00 33.98  ? 216 PHE B CG  1 
ATOM   5200  C  CD1 . PHE B  1 216 ? 28.687  18.681  57.138  1.00 34.83  ? 216 PHE B CD1 1 
ATOM   5201  C  CD2 . PHE B  1 216 ? 30.797  18.389  58.169  1.00 28.22  ? 216 PHE B CD2 1 
ATOM   5202  C  CE1 . PHE B  1 216 ? 28.936  20.021  57.037  1.00 36.05  ? 216 PHE B CE1 1 
ATOM   5203  C  CE2 . PHE B  1 216 ? 31.051  19.716  58.075  1.00 24.61  ? 216 PHE B CE2 1 
ATOM   5204  C  CZ  . PHE B  1 216 ? 30.133  20.533  57.514  1.00 32.81  ? 216 PHE B CZ  1 
ATOM   5205  N  N   . LYS B  1 217 ? 27.741  13.937  60.033  1.00 33.84  ? 217 LYS B N   1 
ATOM   5206  C  CA  . LYS B  1 217 ? 27.483  12.490  60.010  1.00 35.69  ? 217 LYS B CA  1 
ATOM   5207  C  C   . LYS B  1 217 ? 26.349  11.950  59.091  1.00 32.57  ? 217 LYS B C   1 
ATOM   5208  O  O   . LYS B  1 217 ? 26.596  11.261  58.082  1.00 33.69  ? 217 LYS B O   1 
ATOM   5209  C  CB  . LYS B  1 217 ? 27.326  11.937  61.417  1.00 33.43  ? 217 LYS B CB  1 
ATOM   5210  C  CG  . LYS B  1 217 ? 27.181  10.451  61.367  1.00 30.43  ? 217 LYS B CG  1 
ATOM   5211  C  CD  . LYS B  1 217 ? 27.472  9.885   62.695  1.00 37.38  ? 217 LYS B CD  1 
ATOM   5212  C  CE  . LYS B  1 217 ? 26.272  9.224   63.258  1.00 35.69  ? 217 LYS B CE  1 
ATOM   5213  N  NZ  . LYS B  1 217 ? 26.603  8.847   64.654  1.00 50.16  ? 217 LYS B NZ  1 
ATOM   5214  N  N   . PRO B  1 218 ? 25.097  12.259  59.404  1.00 27.00  ? 218 PRO B N   1 
ATOM   5215  C  CA  . PRO B  1 218 ? 24.063  11.733  58.524  1.00 26.17  ? 218 PRO B CA  1 
ATOM   5216  C  C   . PRO B  1 218 ? 24.263  12.136  57.061  1.00 28.30  ? 218 PRO B C   1 
ATOM   5217  O  O   . PRO B  1 218 ? 24.093  11.320  56.154  1.00 25.37  ? 218 PRO B O   1 
ATOM   5218  C  CB  . PRO B  1 218 ? 22.807  12.365  59.087  1.00 19.09  ? 218 PRO B CB  1 
ATOM   5219  C  CG  . PRO B  1 218 ? 23.123  12.522  60.492  1.00 26.08  ? 218 PRO B CG  1 
ATOM   5220  C  CD  . PRO B  1 218 ? 24.505  13.058  60.478  1.00 25.85  ? 218 PRO B CD  1 
ATOM   5221  N  N   . PHE B  1 219 ? 24.633  13.395  56.834  1.00 30.16  ? 219 PHE B N   1 
ATOM   5222  C  CA  . PHE B  1 219 ? 24.829  13.875  55.485  1.00 28.85  ? 219 PHE B CA  1 
ATOM   5223  C  C   . PHE B  1 219 ? 25.813  13.003  54.752  1.00 30.71  ? 219 PHE B C   1 
ATOM   5224  O  O   . PHE B  1 219 ? 25.518  12.476  53.673  1.00 30.83  ? 219 PHE B O   1 
ATOM   5225  C  CB  . PHE B  1 219 ? 25.339  15.334  55.486  1.00 30.30  ? 219 PHE B CB  1 
ATOM   5226  C  CG  . PHE B  1 219 ? 25.729  15.856  54.107  1.00 33.28  ? 219 PHE B CG  1 
ATOM   5227  C  CD1 . PHE B  1 219 ? 24.792  15.930  53.086  1.00 36.72  ? 219 PHE B CD1 1 
ATOM   5228  C  CD2 . PHE B  1 219 ? 27.042  16.207  53.816  1.00 30.34  ? 219 PHE B CD2 1 
ATOM   5229  C  CE1 . PHE B  1 219 ? 25.157  16.329  51.800  1.00 37.70  ? 219 PHE B CE1 1 
ATOM   5230  C  CE2 . PHE B  1 219 ? 27.407  16.609  52.530  1.00 32.21  ? 219 PHE B CE2 1 
ATOM   5231  C  CZ  . PHE B  1 219 ? 26.464  16.667  51.525  1.00 33.50  ? 219 PHE B CZ  1 
ATOM   5232  N  N   . SER B  1 220 ? 26.946  12.777  55.402  1.00 34.35  ? 220 SER B N   1 
ATOM   5233  C  CA  . SER B  1 220 ? 28.013  12.016  54.789  1.00 37.25  ? 220 SER B CA  1 
ATOM   5234  C  C   . SER B  1 220 ? 27.687  10.590  54.526  1.00 37.62  ? 220 SER B C   1 
ATOM   5235  O  O   . SER B  1 220 ? 28.166  10.038  53.533  1.00 42.10  ? 220 SER B O   1 
ATOM   5236  C  CB  . SER B  1 220 ? 29.309  12.155  55.577  1.00 42.78  ? 220 SER B CB  1 
ATOM   5237  O  OG  . SER B  1 220 ? 29.122  11.772  56.911  1.00 52.22  ? 220 SER B OG  1 
ATOM   5238  N  N   . TYR B  1 221 ? 26.864  9.969   55.364  1.00 38.77  ? 221 TYR B N   1 
ATOM   5239  C  CA  . TYR B  1 221 ? 26.512  8.569   55.101  1.00 34.14  ? 221 TYR B CA  1 
ATOM   5240  C  C   . TYR B  1 221 ? 25.641  8.445   53.904  1.00 31.91  ? 221 TYR B C   1 
ATOM   5241  O  O   . TYR B  1 221 ? 25.837  7.539   53.094  1.00 31.11  ? 221 TYR B O   1 
ATOM   5242  C  CB  . TYR B  1 221 ? 25.760  7.970   56.253  1.00 34.79  ? 221 TYR B CB  1 
ATOM   5243  C  CG  . TYR B  1 221 ? 26.684  7.403   57.249  1.00 36.07  ? 221 TYR B CG  1 
ATOM   5244  C  CD1 . TYR B  1 221 ? 27.136  6.108   57.124  1.00 37.74  ? 221 TYR B CD1 1 
ATOM   5245  C  CD2 . TYR B  1 221 ? 27.139  8.164   58.310  1.00 38.41  ? 221 TYR B CD2 1 
ATOM   5246  C  CE1 . TYR B  1 221 ? 28.023  5.576   58.031  1.00 40.08  ? 221 TYR B CE1 1 
ATOM   5247  C  CE2 . TYR B  1 221 ? 28.025  7.646   59.228  1.00 44.53  ? 221 TYR B CE2 1 
ATOM   5248  C  CZ  . TYR B  1 221 ? 28.470  6.340   59.082  1.00 44.30  ? 221 TYR B CZ  1 
ATOM   5249  O  OH  . TYR B  1 221 ? 29.371  5.797   59.988  1.00 53.27  ? 221 TYR B OH  1 
ATOM   5250  N  N   . ARG B  1 222 ? 24.689  9.375   53.806  1.00 32.17  ? 222 ARG B N   1 
ATOM   5251  C  CA  . ARG B  1 222 ? 23.713  9.399   52.738  1.00 29.74  ? 222 ARG B CA  1 
ATOM   5252  C  C   . ARG B  1 222 ? 24.154  9.934   51.397  1.00 30.42  ? 222 ARG B C   1 
ATOM   5253  O  O   . ARG B  1 222 ? 23.778  9.366   50.371  1.00 30.06  ? 222 ARG B O   1 
ATOM   5254  C  CB  . ARG B  1 222 ? 22.493  10.162  53.207  1.00 24.79  ? 222 ARG B CB  1 
ATOM   5255  C  CG  . ARG B  1 222 ? 21.779  9.450   54.264  1.00 24.09  ? 222 ARG B CG  1 
ATOM   5256  C  CD  . ARG B  1 222 ? 21.204  10.416  55.272  1.00 27.60  ? 222 ARG B CD  1 
ATOM   5257  N  NE  . ARG B  1 222 ? 20.337  9.783   56.262  1.00 31.58  ? 222 ARG B NE  1 
ATOM   5258  C  CZ  . ARG B  1 222 ? 19.218  9.139   55.953  1.00 36.43  ? 222 ARG B CZ  1 
ATOM   5259  N  NH1 . ARG B  1 222 ? 18.845  9.037   54.676  1.00 42.22  ? 222 ARG B NH1 1 
ATOM   5260  N  NH2 . ARG B  1 222 ? 18.451  8.632   56.916  1.00 38.03  ? 222 ARG B NH2 1 
ATOM   5261  N  N   . TYR B  1 223 ? 24.952  11.000  51.408  1.00 30.91  ? 223 TYR B N   1 
ATOM   5262  C  CA  . TYR B  1 223 ? 25.382  11.666  50.186  1.00 31.72  ? 223 TYR B CA  1 
ATOM   5263  C  C   . TYR B  1 223 ? 26.875  11.563  49.942  1.00 36.20  ? 223 TYR B C   1 
ATOM   5264  O  O   . TYR B  1 223 ? 27.687  12.142  50.681  1.00 37.27  ? 223 TYR B O   1 
ATOM   5265  C  CB  . TYR B  1 223 ? 24.932  13.143  50.240  1.00 30.58  ? 223 TYR B CB  1 
ATOM   5266  C  CG  . TYR B  1 223 ? 23.432  13.267  50.279  1.00 26.65  ? 223 TYR B CG  1 
ATOM   5267  C  CD1 . TYR B  1 223 ? 22.693  12.977  49.154  1.00 29.45  ? 223 TYR B CD1 1 
ATOM   5268  C  CD2 . TYR B  1 223 ? 22.758  13.476  51.462  1.00 19.10  ? 223 TYR B CD2 1 
ATOM   5269  C  CE1 . TYR B  1 223 ? 21.331  12.869  49.199  1.00 29.87  ? 223 TYR B CE1 1 
ATOM   5270  C  CE2 . TYR B  1 223 ? 21.375  13.371  51.519  1.00 23.49  ? 223 TYR B CE2 1 
ATOM   5271  C  CZ  . TYR B  1 223 ? 20.664  13.063  50.381  1.00 28.69  ? 223 TYR B CZ  1 
ATOM   5272  O  OH  . TYR B  1 223 ? 19.279  12.946  50.371  1.00 36.71  ? 223 TYR B OH  1 
ATOM   5273  N  N   . HIS B  1 224 ? 27.247  10.831  48.900  1.00 36.44  ? 224 HIS B N   1 
ATOM   5274  C  CA  . HIS B  1 224 ? 28.669  10.667  48.577  1.00 39.23  ? 224 HIS B CA  1 
ATOM   5275  C  C   . HIS B  1 224 ? 29.055  11.490  47.372  1.00 40.49  ? 224 HIS B C   1 
ATOM   5276  O  O   . HIS B  1 224 ? 28.205  11.723  46.520  1.00 44.98  ? 224 HIS B O   1 
ATOM   5277  C  CB  . HIS B  1 224 ? 29.003  9.214   48.281  1.00 37.54  ? 224 HIS B CB  1 
ATOM   5278  C  CG  . HIS B  1 224 ? 29.134  8.373   49.502  1.00 39.03  ? 224 HIS B CG  1 
ATOM   5279  N  ND1 . HIS B  1 224 ? 29.847  7.196   49.504  1.00 38.30  ? 224 HIS B ND1 1 
ATOM   5280  C  CD2 . HIS B  1 224 ? 28.678  8.548   50.766  1.00 37.12  ? 224 HIS B CD2 1 
ATOM   5281  C  CE1 . HIS B  1 224 ? 29.831  6.686   50.724  1.00 44.67  ? 224 HIS B CE1 1 
ATOM   5282  N  NE2 . HIS B  1 224 ? 29.126  7.486   51.510  1.00 37.39  ? 224 HIS B NE2 1 
ATOM   5283  N  N   . VAL B  1 225 ? 30.337  11.848  47.265  1.00 36.54  ? 225 VAL B N   1 
ATOM   5284  C  CA  . VAL B  1 225 ? 30.838  12.657  46.151  1.00 30.87  ? 225 VAL B CA  1 
ATOM   5285  C  C   . VAL B  1 225 ? 32.178  12.115  45.774  1.00 32.11  ? 225 VAL B C   1 
ATOM   5286  O  O   . VAL B  1 225 ? 32.876  11.570  46.624  1.00 31.72  ? 225 VAL B O   1 
ATOM   5287  C  CB  . VAL B  1 225 ? 31.027  14.082  46.560  1.00 30.68  ? 225 VAL B CB  1 
ATOM   5288  C  CG1 . VAL B  1 225 ? 29.705  14.691  46.919  1.00 37.61  ? 225 VAL B CG1 1 
ATOM   5289  C  CG2 . VAL B  1 225 ? 31.925  14.163  47.761  1.00 35.79  ? 225 VAL B CG2 1 
ATOM   5290  N  N   . PRO B  1 226 ? 32.579  12.285  44.510  1.00 31.10  ? 226 PRO B N   1 
ATOM   5291  C  CA  . PRO B  1 226 ? 33.855  11.822  43.930  1.00 33.11  ? 226 PRO B CA  1 
ATOM   5292  C  C   . PRO B  1 226 ? 35.043  12.671  44.340  1.00 35.22  ? 226 PRO B C   1 
ATOM   5293  O  O   . PRO B  1 226 ? 35.913  13.002  43.507  1.00 38.03  ? 226 PRO B O   1 
ATOM   5294  C  CB  . PRO B  1 226 ? 33.600  11.944  42.438  1.00 35.09  ? 226 PRO B CB  1 
ATOM   5295  C  CG  . PRO B  1 226 ? 32.736  13.177  42.385  1.00 33.17  ? 226 PRO B CG  1 
ATOM   5296  C  CD  . PRO B  1 226 ? 31.757  12.962  43.502  1.00 31.43  ? 226 PRO B CD  1 
ATOM   5297  N  N   . TYR B  1 227 ? 35.142  12.957  45.630  1.00 32.57  ? 227 TYR B N   1 
ATOM   5298  C  CA  . TYR B  1 227 ? 36.203  13.823  46.049  1.00 32.43  ? 227 TYR B CA  1 
ATOM   5299  C  C   . TYR B  1 227 ? 37.590  13.323  45.767  1.00 31.90  ? 227 TYR B C   1 
ATOM   5300  O  O   . TYR B  1 227 ? 38.470  14.096  45.530  1.00 36.16  ? 227 TYR B O   1 
ATOM   5301  C  CB  . TYR B  1 227 ? 36.053  14.207  47.495  1.00 33.90  ? 227 TYR B CB  1 
ATOM   5302  C  CG  . TYR B  1 227 ? 36.318  13.096  48.416  1.00 37.41  ? 227 TYR B CG  1 
ATOM   5303  C  CD1 . TYR B  1 227 ? 37.595  12.835  48.856  1.00 38.00  ? 227 TYR B CD1 1 
ATOM   5304  C  CD2 . TYR B  1 227 ? 35.290  12.317  48.873  1.00 39.68  ? 227 TYR B CD2 1 
ATOM   5305  C  CE1 . TYR B  1 227 ? 37.847  11.824  49.730  1.00 37.80  ? 227 TYR B CE1 1 
ATOM   5306  C  CE2 . TYR B  1 227 ? 35.522  11.302  49.758  1.00 44.75  ? 227 TYR B CE2 1 
ATOM   5307  C  CZ  . TYR B  1 227 ? 36.812  11.053  50.195  1.00 41.59  ? 227 TYR B CZ  1 
ATOM   5308  O  OH  . TYR B  1 227 ? 37.042  10.066  51.145  1.00 45.89  ? 227 TYR B OH  1 
ATOM   5309  N  N   . GLU B  1 228 ? 37.814  12.036  45.751  1.00 34.03  ? 228 GLU B N   1 
ATOM   5310  C  CA  . GLU B  1 228 ? 39.172  11.609  45.466  1.00 35.87  ? 228 GLU B CA  1 
ATOM   5311  C  C   . GLU B  1 228 ? 39.496  11.784  44.009  1.00 33.69  ? 228 GLU B C   1 
ATOM   5312  O  O   . GLU B  1 228 ? 40.641  11.615  43.660  1.00 32.81  ? 228 GLU B O   1 
ATOM   5313  C  CB  . GLU B  1 228 ? 39.456  10.146  45.878  1.00 46.51  ? 228 GLU B CB  1 
ATOM   5314  C  CG  . GLU B  1 228 ? 38.392  9.427   46.711  1.00 65.48  ? 228 GLU B CG  1 
ATOM   5315  C  CD  . GLU B  1 228 ? 37.018  9.353   45.998  1.00 80.18  ? 228 GLU B CD  1 
ATOM   5316  O  OE1 . GLU B  1 228 ? 36.936  9.463   44.726  1.00 86.36  ? 228 GLU B OE1 1 
ATOM   5317  O  OE2 . GLU B  1 228 ? 36.007  9.216   46.732  1.00 88.66  ? 228 GLU B OE2 1 
ATOM   5318  N  N   . ALA B  1 229 ? 38.510  12.101  43.162  1.00 35.93  ? 229 ALA B N   1 
ATOM   5319  C  CA  . ALA B  1 229 ? 38.767  12.286  41.731  1.00 36.18  ? 229 ALA B CA  1 
ATOM   5320  C  C   . ALA B  1 229 ? 39.617  13.543  41.549  1.00 41.37  ? 229 ALA B C   1 
ATOM   5321  O  O   . ALA B  1 229 ? 40.489  13.565  40.684  1.00 46.47  ? 229 ALA B O   1 
ATOM   5322  C  CB  . ALA B  1 229 ? 37.521  12.373  40.973  1.00 38.51  ? 229 ALA B CB  1 
ATOM   5323  N  N   . SER B  1 230 ? 39.283  14.616  42.284  1.00 43.55  ? 230 SER B N   1 
ATOM   5324  C  CA  . SER B  1 230 ? 40.110  15.848  42.360  1.00 42.30  ? 230 SER B CA  1 
ATOM   5325  C  C   . SER B  1 230 ? 41.082  15.197  43.346  1.00 45.76  ? 230 SER B C   1 
ATOM   5326  O  O   . SER B  1 230 ? 40.842  14.069  43.785  1.00 52.17  ? 230 SER B O   1 
ATOM   5327  C  CB  . SER B  1 230 ? 39.376  16.950  43.128  1.00 40.32  ? 230 SER B CB  1 
ATOM   5328  O  OG  . SER B  1 230 ? 37.966  16.677  43.212  1.00 46.88  ? 230 SER B OG  1 
ATOM   5329  N  N   . GLN B  1 231 ? 42.153  15.795  43.792  1.00 41.56  ? 231 GLN B N   1 
ATOM   5330  C  CA  . GLN B  1 231 ? 42.876  14.922  44.707  1.00 35.24  ? 231 GLN B CA  1 
ATOM   5331  C  C   . GLN B  1 231 ? 42.591  15.332  46.147  1.00 35.47  ? 231 GLN B C   1 
ATOM   5332  O  O   . GLN B  1 231 ? 43.491  15.450  46.979  1.00 40.69  ? 231 GLN B O   1 
ATOM   5333  C  CB  . GLN B  1 231 ? 44.360  14.823  44.350  1.00 46.77  ? 231 GLN B CB  1 
ATOM   5334  C  CG  . GLN B  1 231 ? 44.706  14.031  43.050  1.00 61.18  ? 231 GLN B CG  1 
ATOM   5335  C  CD  . GLN B  1 231 ? 44.107  14.627  41.747  1.00 72.56  ? 231 GLN B CD  1 
ATOM   5336  O  OE1 . GLN B  1 231 ? 43.922  15.852  41.614  1.00 82.06  ? 231 GLN B OE1 1 
ATOM   5337  N  NE2 . GLN B  1 231 ? 43.812  13.754  40.781  1.00 76.58  ? 231 GLN B NE2 1 
ATOM   5338  N  N   . SER B  1 232 ? 41.307  15.531  46.440  1.00 31.77  ? 232 SER B N   1 
ATOM   5339  C  CA  . SER B  1 232 ? 40.849  15.975  47.751  1.00 27.16  ? 232 SER B CA  1 
ATOM   5340  C  C   . SER B  1 232 ? 40.934  14.857  48.732  1.00 31.12  ? 232 SER B C   1 
ATOM   5341  O  O   . SER B  1 232 ? 40.884  13.695  48.346  1.00 39.58  ? 232 SER B O   1 
ATOM   5342  C  CB  . SER B  1 232 ? 39.410  16.429  47.681  1.00 25.30  ? 232 SER B CB  1 
ATOM   5343  O  OG  . SER B  1 232 ? 38.954  16.808  48.952  1.00 29.56  ? 232 SER B OG  1 
ATOM   5344  N  N   . THR B  1 233 ? 41.040  15.198  50.005  1.00 27.17  ? 233 THR B N   1 
ATOM   5345  C  CA  . THR B  1 233 ? 41.122  14.191  51.026  1.00 19.44  ? 233 THR B CA  1 
ATOM   5346  C  C   . THR B  1 233 ? 39.868  14.259  51.872  1.00 23.68  ? 233 THR B C   1 
ATOM   5347  O  O   . THR B  1 233 ? 39.839  13.728  52.965  1.00 32.78  ? 233 THR B O   1 
ATOM   5348  C  CB  . THR B  1 233 ? 42.361  14.383  51.922  1.00 19.56  ? 233 THR B CB  1 
ATOM   5349  O  OG1 . THR B  1 233 ? 42.338  15.657  52.583  1.00 19.09  ? 233 THR B OG1 1 
ATOM   5350  C  CG2 . THR B  1 233 ? 43.587  14.292  51.124  1.00 19.42  ? 233 THR B CG2 1 
ATOM   5351  N  N   . SER B  1 234 ? 38.849  14.956  51.408  1.00 21.42  ? 234 SER B N   1 
ATOM   5352  C  CA  . SER B  1 234 ? 37.625  15.050  52.172  1.00 22.59  ? 234 SER B CA  1 
ATOM   5353  C  C   . SER B  1 234 ? 36.491  15.288  51.237  1.00 27.94  ? 234 SER B C   1 
ATOM   5354  O  O   . SER B  1 234 ? 36.650  15.954  50.224  1.00 34.49  ? 234 SER B O   1 
ATOM   5355  C  CB  . SER B  1 234 ? 37.685  16.186  53.148  1.00 20.96  ? 234 SER B CB  1 
ATOM   5356  O  OG  . SER B  1 234 ? 36.383  16.425  53.646  1.00 25.17  ? 234 SER B OG  1 
ATOM   5357  N  N   . PRO B  1 235 ? 35.320  14.740  51.544  1.00 25.96  ? 235 PRO B N   1 
ATOM   5358  C  CA  . PRO B  1 235 ? 34.157  14.914  50.695  1.00 28.27  ? 235 PRO B CA  1 
ATOM   5359  C  C   . PRO B  1 235 ? 33.543  16.293  50.805  1.00 28.79  ? 235 PRO B C   1 
ATOM   5360  O  O   . PRO B  1 235 ? 32.549  16.574  50.138  1.00 34.83  ? 235 PRO B O   1 
ATOM   5361  C  CB  . PRO B  1 235 ? 33.200  13.859  51.232  1.00 28.96  ? 235 PRO B CB  1 
ATOM   5362  C  CG  . PRO B  1 235 ? 33.480  13.867  52.636  1.00 24.00  ? 235 PRO B CG  1 
ATOM   5363  C  CD  . PRO B  1 235 ? 34.992  13.834  52.638  1.00 26.18  ? 235 PRO B CD  1 
ATOM   5364  N  N   . PHE B  1 236 ? 34.116  17.157  51.626  1.00 28.61  ? 236 PHE B N   1 
ATOM   5365  C  CA  . PHE B  1 236 ? 33.538  18.482  51.769  1.00 28.52  ? 236 PHE B CA  1 
ATOM   5366  C  C   . PHE B  1 236 ? 34.000  19.544  50.832  1.00 28.71  ? 236 PHE B C   1 
ATOM   5367  O  O   . PHE B  1 236 ? 33.547  20.682  50.935  1.00 35.26  ? 236 PHE B O   1 
ATOM   5368  C  CB  . PHE B  1 236 ? 33.647  18.940  53.195  1.00 28.47  ? 236 PHE B CB  1 
ATOM   5369  C  CG  . PHE B  1 236 ? 32.988  17.991  54.101  1.00 35.46  ? 236 PHE B CG  1 
ATOM   5370  C  CD1 . PHE B  1 236 ? 31.778  17.437  53.742  1.00 35.95  ? 236 PHE B CD1 1 
ATOM   5371  C  CD2 . PHE B  1 236 ? 33.601  17.540  55.249  1.00 35.28  ? 236 PHE B CD2 1 
ATOM   5372  C  CE1 . PHE B  1 236 ? 31.195  16.437  54.515  1.00 34.78  ? 236 PHE B CE1 1 
ATOM   5373  C  CE2 . PHE B  1 236 ? 33.002  16.534  56.019  1.00 28.85  ? 236 PHE B CE2 1 
ATOM   5374  C  CZ  . PHE B  1 236 ? 31.812  15.993  55.645  1.00 26.50  ? 236 PHE B CZ  1 
ATOM   5375  N  N   . TRP B  1 237 ? 34.931  19.198  49.966  1.00 19.97  ? 237 TRP B N   1 
ATOM   5376  C  CA  . TRP B  1 237 ? 35.432  20.126  48.991  1.00 17.79  ? 237 TRP B CA  1 
ATOM   5377  C  C   . TRP B  1 237 ? 36.052  19.266  47.908  1.00 20.83  ? 237 TRP B C   1 
ATOM   5378  O  O   . TRP B  1 237 ? 36.801  18.322  48.159  1.00 18.75  ? 237 TRP B O   1 
ATOM   5379  C  CB  . TRP B  1 237 ? 36.462  21.074  49.598  1.00 19.48  ? 237 TRP B CB  1 
ATOM   5380  C  CG  . TRP B  1 237 ? 37.661  20.409  50.212  1.00 20.40  ? 237 TRP B CG  1 
ATOM   5381  C  CD1 . TRP B  1 237 ? 38.833  20.051  49.592  1.00 22.85  ? 237 TRP B CD1 1 
ATOM   5382  C  CD2 . TRP B  1 237 ? 37.850  20.146  51.586  1.00 19.66  ? 237 TRP B CD2 1 
ATOM   5383  N  NE1 . TRP B  1 237 ? 39.745  19.604  50.515  1.00 22.61  ? 237 TRP B NE1 1 
ATOM   5384  C  CE2 . TRP B  1 237 ? 39.167  19.657  51.752  1.00 19.19  ? 237 TRP B CE2 1 
ATOM   5385  C  CE3 . TRP B  1 237 ? 37.034  20.273  52.714  1.00 26.59  ? 237 TRP B CE3 1 
ATOM   5386  C  CZ2 . TRP B  1 237 ? 39.681  19.319  52.979  1.00 22.44  ? 237 TRP B CZ2 1 
ATOM   5387  C  CZ3 . TRP B  1 237 ? 37.544  19.934  53.947  1.00 21.74  ? 237 TRP B CZ3 1 
ATOM   5388  C  CH2 . TRP B  1 237 ? 38.852  19.462  54.071  1.00 24.44  ? 237 TRP B CH2 1 
ATOM   5389  N  N   . TYR B  1 238 ? 35.759  19.595  46.680  1.00 19.47  ? 238 TYR B N   1 
ATOM   5390  C  CA  . TYR B  1 238 ? 36.269  18.792  45.620  1.00 23.63  ? 238 TYR B CA  1 
ATOM   5391  C  C   . TYR B  1 238 ? 35.905  19.565  44.380  1.00 28.24  ? 238 TYR B C   1 
ATOM   5392  O  O   . TYR B  1 238 ? 35.439  20.691  44.491  1.00 32.60  ? 238 TYR B O   1 
ATOM   5393  C  CB  . TYR B  1 238 ? 35.538  17.444  45.656  1.00 24.24  ? 238 TYR B CB  1 
ATOM   5394  C  CG  . TYR B  1 238 ? 34.009  17.554  45.587  1.00 25.06  ? 238 TYR B CG  1 
ATOM   5395  C  CD1 . TYR B  1 238 ? 33.248  17.887  46.715  1.00 25.18  ? 238 TYR B CD1 1 
ATOM   5396  C  CD2 . TYR B  1 238 ? 33.327  17.304  44.389  1.00 22.58  ? 238 TYR B CD2 1 
ATOM   5397  C  CE1 . TYR B  1 238 ? 31.834  17.980  46.638  1.00 20.17  ? 238 TYR B CE1 1 
ATOM   5398  C  CE2 . TYR B  1 238 ? 31.910  17.396  44.323  1.00 18.91  ? 238 TYR B CE2 1 
ATOM   5399  C  CZ  . TYR B  1 238 ? 31.193  17.730  45.443  1.00 24.63  ? 238 TYR B CZ  1 
ATOM   5400  O  OH  . TYR B  1 238 ? 29.831  17.850  45.326  1.00 33.61  ? 238 TYR B OH  1 
ATOM   5401  N  N   . SER B  1 239 ? 36.099  18.976  43.207  1.00 30.46  ? 239 SER B N   1 
ATOM   5402  C  CA  . SER B  1 239 ? 35.702  19.618  41.974  1.00 27.80  ? 239 SER B CA  1 
ATOM   5403  C  C   . SER B  1 239 ? 35.386  18.561  40.958  1.00 29.82  ? 239 SER B C   1 
ATOM   5404  O  O   . SER B  1 239 ? 35.840  17.418  41.073  1.00 27.69  ? 239 SER B O   1 
ATOM   5405  C  CB  . SER B  1 239 ? 36.835  20.427  41.437  1.00 30.83  ? 239 SER B CB  1 
ATOM   5406  O  OG  . SER B  1 239 ? 37.835  19.540  41.020  1.00 25.44  ? 239 SER B OG  1 
ATOM   5407  N  N   . ILE B  1 240 ? 34.710  18.981  39.907  1.00 32.47  ? 240 ILE B N   1 
ATOM   5408  C  CA  . ILE B  1 240 ? 34.335  18.088  38.823  1.00 36.90  ? 240 ILE B CA  1 
ATOM   5409  C  C   . ILE B  1 240 ? 34.313  18.954  37.588  1.00 36.39  ? 240 ILE B C   1 
ATOM   5410  O  O   . ILE B  1 240 ? 34.112  20.155  37.687  1.00 39.63  ? 240 ILE B O   1 
ATOM   5411  C  CB  . ILE B  1 240 ? 32.873  17.490  38.974  1.00 35.38  ? 240 ILE B CB  1 
ATOM   5412  C  CG1 . ILE B  1 240 ? 31.821  18.590  39.040  1.00 32.51  ? 240 ILE B CG1 1 
ATOM   5413  C  CG2 . ILE B  1 240 ? 32.740  16.702  40.206  1.00 30.85  ? 240 ILE B CG2 1 
ATOM   5414  C  CD1 . ILE B  1 240 ? 30.461  18.053  38.896  1.00 29.97  ? 240 ILE B CD1 1 
ATOM   5415  N  N   . LYS B  1 241 ? 34.547  18.351  36.445  1.00 33.77  ? 241 LYS B N   1 
ATOM   5416  C  CA  . LYS B  1 241 ? 34.482  19.058  35.203  1.00 32.90  ? 241 LYS B CA  1 
ATOM   5417  C  C   . LYS B  1 241 ? 33.255  18.440  34.542  1.00 37.17  ? 241 LYS B C   1 
ATOM   5418  O  O   . LYS B  1 241 ? 33.029  17.242  34.656  1.00 38.43  ? 241 LYS B O   1 
ATOM   5419  C  CB  . LYS B  1 241 ? 35.685  18.721  34.355  1.00 30.29  ? 241 LYS B CB  1 
ATOM   5420  C  CG  . LYS B  1 241 ? 37.011  19.169  34.894  1.00 31.72  ? 241 LYS B CG  1 
ATOM   5421  C  CD  . LYS B  1 241 ? 38.051  18.700  33.893  1.00 33.37  ? 241 LYS B CD  1 
ATOM   5422  C  CE  . LYS B  1 241 ? 39.458  19.150  34.177  1.00 41.97  ? 241 LYS B CE  1 
ATOM   5423  N  NZ  . LYS B  1 241 ? 40.384  18.313  33.315  1.00 43.92  ? 241 LYS B NZ  1 
ATOM   5424  N  N   . ARG B  1 242 ? 32.448  19.236  33.861  1.00 40.13  ? 242 ARG B N   1 
ATOM   5425  C  CA  . ARG B  1 242 ? 31.281  18.687  33.176  1.00 39.97  ? 242 ARG B CA  1 
ATOM   5426  C  C   . ARG B  1 242 ? 30.942  19.606  32.022  1.00 38.26  ? 242 ARG B C   1 
ATOM   5427  O  O   . ARG B  1 242 ? 30.682  20.802  32.222  1.00 37.81  ? 242 ARG B O   1 
ATOM   5428  C  CB  . ARG B  1 242 ? 30.106  18.563  34.143  1.00 43.71  ? 242 ARG B CB  1 
ATOM   5429  C  CG  . ARG B  1 242 ? 28.784  18.399  33.465  1.00 46.38  ? 242 ARG B CG  1 
ATOM   5430  C  CD  . ARG B  1 242 ? 27.734  17.895  34.429  1.00 48.98  ? 242 ARG B CD  1 
ATOM   5431  N  NE  . ARG B  1 242 ? 27.920  16.479  34.670  1.00 49.86  ? 242 ARG B NE  1 
ATOM   5432  C  CZ  . ARG B  1 242 ? 26.957  15.563  34.601  1.00 50.06  ? 242 ARG B CZ  1 
ATOM   5433  N  NH1 . ARG B  1 242 ? 25.716  15.914  34.308  1.00 46.17  ? 242 ARG B NH1 1 
ATOM   5434  N  NH2 . ARG B  1 242 ? 27.264  14.277  34.766  1.00 51.68  ? 242 ARG B NH2 1 
ATOM   5435  N  N   . ALA B  1 243 ? 30.956  19.047  30.814  1.00 36.89  ? 243 ALA B N   1 
ATOM   5436  C  CA  . ALA B  1 243 ? 30.683  19.825  29.613  1.00 32.65  ? 243 ALA B CA  1 
ATOM   5437  C  C   . ALA B  1 243 ? 31.787  20.852  29.501  1.00 34.49  ? 243 ALA B C   1 
ATOM   5438  O  O   . ALA B  1 243 ? 32.971  20.511  29.475  1.00 32.16  ? 243 ALA B O   1 
ATOM   5439  C  CB  . ALA B  1 243 ? 29.331  20.514  29.705  1.00 32.80  ? 243 ALA B CB  1 
ATOM   5440  N  N   . SER B  1 244 ? 31.403  22.117  29.501  1.00 38.05  ? 244 SER B N   1 
ATOM   5441  C  CA  . SER B  1 244 ? 32.356  23.192  29.358  1.00 41.47  ? 244 SER B CA  1 
ATOM   5442  C  C   . SER B  1 244 ? 32.683  23.871  30.673  1.00 43.42  ? 244 SER B C   1 
ATOM   5443  O  O   . SER B  1 244 ? 33.420  24.859  30.695  1.00 50.18  ? 244 SER B O   1 
ATOM   5444  C  CB  . SER B  1 244 ? 31.804  24.223  28.356  1.00 47.56  ? 244 SER B CB  1 
ATOM   5445  O  OG  . SER B  1 244 ? 30.466  24.600  28.673  1.00 52.62  ? 244 SER B OG  1 
ATOM   5446  N  N   . ALA B  1 245 ? 32.149  23.362  31.773  1.00 41.49  ? 245 ALA B N   1 
ATOM   5447  C  CA  . ALA B  1 245 ? 32.398  23.984  33.067  1.00 39.19  ? 245 ALA B CA  1 
ATOM   5448  C  C   . ALA B  1 245 ? 33.342  23.222  33.960  1.00 38.92  ? 245 ALA B C   1 
ATOM   5449  O  O   . ALA B  1 245 ? 33.431  22.007  33.880  1.00 36.43  ? 245 ALA B O   1 
ATOM   5450  C  CB  . ALA B  1 245 ? 31.116  24.213  33.795  1.00 37.76  ? 245 ALA B CB  1 
ATOM   5451  N  N   . HIS B  1 246 ? 34.037  23.961  34.825  1.00 39.72  ? 246 HIS B N   1 
ATOM   5452  C  CA  . HIS B  1 246 ? 34.951  23.409  35.816  1.00 36.24  ? 246 HIS B CA  1 
ATOM   5453  C  C   . HIS B  1 246 ? 34.341  23.977  37.087  1.00 36.75  ? 246 HIS B C   1 
ATOM   5454  O  O   . HIS B  1 246 ? 34.322  25.188  37.310  1.00 38.77  ? 246 HIS B O   1 
ATOM   5455  C  CB  . HIS B  1 246 ? 36.368  23.915  35.633  1.00 39.20  ? 246 HIS B CB  1 
ATOM   5456  C  CG  . HIS B  1 246 ? 37.386  23.194  36.471  1.00 42.00  ? 246 HIS B CG  1 
ATOM   5457  N  ND1 . HIS B  1 246 ? 38.466  22.527  35.932  1.00 40.31  ? 246 HIS B ND1 1 
ATOM   5458  C  CD2 . HIS B  1 246 ? 37.522  23.095  37.814  1.00 41.21  ? 246 HIS B CD2 1 
ATOM   5459  C  CE1 . HIS B  1 246 ? 39.222  22.055  36.904  1.00 37.51  ? 246 HIS B CE1 1 
ATOM   5460  N  NE2 . HIS B  1 246 ? 38.672  22.387  38.054  1.00 37.91  ? 246 HIS B NE2 1 
ATOM   5461  N  N   . ILE B  1 247 ? 33.759  23.088  37.874  1.00 34.75  ? 247 ILE B N   1 
ATOM   5462  C  CA  . ILE B  1 247 ? 33.084  23.452  39.094  1.00 32.58  ? 247 ILE B CA  1 
ATOM   5463  C  C   . ILE B  1 247 ? 33.928  23.075  40.280  1.00 34.77  ? 247 ILE B C   1 
ATOM   5464  O  O   . ILE B  1 247 ? 34.449  21.963  40.342  1.00 41.19  ? 247 ILE B O   1 
ATOM   5465  C  CB  . ILE B  1 247 ? 31.790  22.702  39.125  1.00 33.44  ? 247 ILE B CB  1 
ATOM   5466  C  CG1 . ILE B  1 247 ? 31.040  22.984  37.819  1.00 32.41  ? 247 ILE B CG1 1 
ATOM   5467  C  CG2 . ILE B  1 247 ? 30.962  23.125  40.299  1.00 32.37  ? 247 ILE B CG2 1 
ATOM   5468  C  CD1 . ILE B  1 247 ? 29.752  22.281  37.690  1.00 34.21  ? 247 ILE B CD1 1 
ATOM   5469  N  N   . ILE B  1 248 ? 34.061  23.997  41.220  1.00 33.29  ? 248 ILE B N   1 
ATOM   5470  C  CA  . ILE B  1 248 ? 34.837  23.807  42.448  1.00 30.22  ? 248 ILE B CA  1 
ATOM   5471  C  C   . ILE B  1 248 ? 33.880  24.001  43.611  1.00 29.22  ? 248 ILE B C   1 
ATOM   5472  O  O   . ILE B  1 248 ? 33.263  25.066  43.729  1.00 35.68  ? 248 ILE B O   1 
ATOM   5473  C  CB  . ILE B  1 248 ? 35.932  24.909  42.556  1.00 33.01  ? 248 ILE B CB  1 
ATOM   5474  C  CG1 . ILE B  1 248 ? 36.996  24.674  41.485  1.00 30.01  ? 248 ILE B CG1 1 
ATOM   5475  C  CG2 . ILE B  1 248 ? 36.547  24.971  43.945  1.00 29.53  ? 248 ILE B CG2 1 
ATOM   5476  C  CD1 . ILE B  1 248 ? 38.138  25.588  41.605  1.00 28.90  ? 248 ILE B CD1 1 
ATOM   5477  N  N   . VAL B  1 249 ? 33.768  23.007  44.480  1.00 25.70  ? 249 VAL B N   1 
ATOM   5478  C  CA  . VAL B  1 249 ? 32.864  23.087  45.635  1.00 21.77  ? 249 VAL B CA  1 
ATOM   5479  C  C   . VAL B  1 249 ? 33.671  23.300  46.900  1.00 17.30  ? 249 VAL B C   1 
ATOM   5480  O  O   . VAL B  1 249 ? 34.617  22.574  47.139  1.00 23.65  ? 249 VAL B O   1 
ATOM   5481  C  CB  . VAL B  1 249 ? 32.050  21.775  45.810  1.00 22.48  ? 249 VAL B CB  1 
ATOM   5482  C  CG1 . VAL B  1 249 ? 31.042  21.917  46.955  1.00 18.71  ? 249 VAL B CG1 1 
ATOM   5483  C  CG2 . VAL B  1 249 ? 31.343  21.395  44.510  1.00 24.30  ? 249 VAL B CG2 1 
ATOM   5484  N  N   . LEU B  1 250 ? 33.266  24.229  47.745  1.00 12.95  ? 250 LEU B N   1 
ATOM   5485  C  CA  . LEU B  1 250 ? 33.993  24.495  48.979  1.00 15.96  ? 250 LEU B CA  1 
ATOM   5486  C  C   . LEU B  1 250 ? 33.132  24.267  50.234  1.00 20.10  ? 250 LEU B C   1 
ATOM   5487  O  O   . LEU B  1 250 ? 31.905  24.122  50.139  1.00 26.72  ? 250 LEU B O   1 
ATOM   5488  C  CB  . LEU B  1 250 ? 34.550  25.906  48.963  1.00 17.13  ? 250 LEU B CB  1 
ATOM   5489  C  CG  . LEU B  1 250 ? 35.442  26.209  47.771  1.00 17.20  ? 250 LEU B CG  1 
ATOM   5490  C  CD1 . LEU B  1 250 ? 35.902  27.612  47.887  1.00 12.96  ? 250 LEU B CD1 1 
ATOM   5491  C  CD2 . LEU B  1 250 ? 36.590  25.276  47.751  1.00 15.34  ? 250 LEU B CD2 1 
ATOM   5492  N  N   . SER B  1 251 ? 33.741  24.340  51.413  1.00 18.66  ? 251 SER B N   1 
ATOM   5493  C  CA  . SER B  1 251 ? 33.024  24.036  52.617  1.00 19.42  ? 251 SER B CA  1 
ATOM   5494  C  C   . SER B  1 251 ? 33.172  25.156  53.581  1.00 23.02  ? 251 SER B C   1 
ATOM   5495  O  O   . SER B  1 251 ? 34.176  25.272  54.244  1.00 24.41  ? 251 SER B O   1 
ATOM   5496  C  CB  . SER B  1 251 ? 33.584  22.720  53.167  1.00 19.07  ? 251 SER B CB  1 
ATOM   5497  O  OG  . SER B  1 251 ? 33.024  22.307  54.394  1.00 27.24  ? 251 SER B OG  1 
ATOM   5498  N  N   . SER B  1 252 ? 32.148  25.986  53.666  1.00 25.30  ? 252 SER B N   1 
ATOM   5499  C  CA  . SER B  1 252 ? 32.180  27.117  54.569  1.00 26.13  ? 252 SER B CA  1 
ATOM   5500  C  C   . SER B  1 252 ? 32.380  26.740  56.008  1.00 25.53  ? 252 SER B C   1 
ATOM   5501  O  O   . SER B  1 252 ? 32.877  27.533  56.800  1.00 32.87  ? 252 SER B O   1 
ATOM   5502  C  CB  . SER B  1 252 ? 30.855  27.863  54.500  1.00 28.65  ? 252 SER B CB  1 
ATOM   5503  O  OG  . SER B  1 252 ? 30.606  28.348  53.194  1.00 40.01  ? 252 SER B OG  1 
ATOM   5504  N  N   . TYR B  1 253 ? 31.974  25.536  56.354  1.00 22.92  ? 253 TYR B N   1 
ATOM   5505  C  CA  . TYR B  1 253 ? 32.028  25.113  57.739  1.00 27.19  ? 253 TYR B CA  1 
ATOM   5506  C  C   . TYR B  1 253 ? 33.131  24.150  58.103  1.00 29.20  ? 253 TYR B C   1 
ATOM   5507  O  O   . TYR B  1 253 ? 33.202  23.639  59.247  1.00 30.83  ? 253 TYR B O   1 
ATOM   5508  C  CB  . TYR B  1 253 ? 30.643  24.638  58.162  1.00 25.46  ? 253 TYR B CB  1 
ATOM   5509  C  CG  . TYR B  1 253 ? 29.640  25.747  57.918  1.00 24.67  ? 253 TYR B CG  1 
ATOM   5510  C  CD1 . TYR B  1 253 ? 29.658  26.907  58.707  1.00 17.66  ? 253 TYR B CD1 1 
ATOM   5511  C  CD2 . TYR B  1 253 ? 28.739  25.696  56.832  1.00 23.03  ? 253 TYR B CD2 1 
ATOM   5512  C  CE1 . TYR B  1 253 ? 28.817  27.982  58.420  1.00 25.45  ? 253 TYR B CE1 1 
ATOM   5513  C  CE2 . TYR B  1 253 ? 27.878  26.799  56.529  1.00 24.95  ? 253 TYR B CE2 1 
ATOM   5514  C  CZ  . TYR B  1 253 ? 27.931  27.939  57.324  1.00 28.65  ? 253 TYR B CZ  1 
ATOM   5515  O  OH  . TYR B  1 253 ? 27.198  29.083  56.996  1.00 27.50  ? 253 TYR B OH  1 
ATOM   5516  N  N   . SER B  1 254 ? 33.954  23.876  57.094  1.00 29.38  ? 254 SER B N   1 
ATOM   5517  C  CA  . SER B  1 254 ? 35.146  23.067  57.262  1.00 30.47  ? 254 SER B CA  1 
ATOM   5518  C  C   . SER B  1 254 ? 36.202  24.174  57.532  1.00 32.01  ? 254 SER B C   1 
ATOM   5519  O  O   . SER B  1 254 ? 35.828  25.349  57.725  1.00 36.67  ? 254 SER B O   1 
ATOM   5520  C  CB  . SER B  1 254 ? 35.469  22.308  55.983  1.00 30.78  ? 254 SER B CB  1 
ATOM   5521  O  OG  . SER B  1 254 ? 34.994  20.974  56.029  1.00 39.53  ? 254 SER B OG  1 
ATOM   5522  N  N   . ALA B  1 255 ? 37.487  23.828  57.589  1.00 28.99  ? 255 ALA B N   1 
ATOM   5523  C  CA  . ALA B  1 255 ? 38.534  24.819  57.839  1.00 25.93  ? 255 ALA B CA  1 
ATOM   5524  C  C   . ALA B  1 255 ? 39.268  25.309  56.584  1.00 29.73  ? 255 ALA B C   1 
ATOM   5525  O  O   . ALA B  1 255 ? 39.532  24.529  55.692  1.00 36.49  ? 255 ALA B O   1 
ATOM   5526  C  CB  . ALA B  1 255 ? 39.527  24.286  58.831  1.00 18.02  ? 255 ALA B CB  1 
ATOM   5527  N  N   . TYR B  1 256 ? 39.641  26.593  56.545  1.00 33.56  ? 256 TYR B N   1 
ATOM   5528  C  CA  . TYR B  1 256 ? 40.348  27.182  55.409  1.00 26.86  ? 256 TYR B CA  1 
ATOM   5529  C  C   . TYR B  1 256 ? 41.568  27.969  55.817  1.00 29.71  ? 256 TYR B C   1 
ATOM   5530  O  O   . TYR B  1 256 ? 42.126  28.673  55.003  1.00 28.91  ? 256 TYR B O   1 
ATOM   5531  C  CB  . TYR B  1 256 ? 39.425  28.072  54.581  1.00 24.77  ? 256 TYR B CB  1 
ATOM   5532  C  CG  . TYR B  1 256 ? 38.307  28.782  55.357  1.00 29.81  ? 256 TYR B CG  1 
ATOM   5533  C  CD1 . TYR B  1 256 ? 38.551  29.909  56.143  1.00 28.48  ? 256 TYR B CD1 1 
ATOM   5534  C  CD2 . TYR B  1 256 ? 37.001  28.329  55.277  1.00 32.42  ? 256 TYR B CD2 1 
ATOM   5535  C  CE1 . TYR B  1 256 ? 37.503  30.556  56.818  1.00 30.01  ? 256 TYR B CE1 1 
ATOM   5536  C  CE2 . TYR B  1 256 ? 35.966  28.970  55.954  1.00 34.03  ? 256 TYR B CE2 1 
ATOM   5537  C  CZ  . TYR B  1 256 ? 36.219  30.067  56.712  1.00 29.15  ? 256 TYR B CZ  1 
ATOM   5538  O  OH  . TYR B  1 256 ? 35.147  30.645  57.336  1.00 32.70  ? 256 TYR B OH  1 
ATOM   5539  N  N   . GLY B  1 257 ? 41.988  27.843  57.077  1.00 33.92  ? 257 GLY B N   1 
ATOM   5540  C  CA  . GLY B  1 257 ? 43.182  28.545  57.525  1.00 30.57  ? 257 GLY B CA  1 
ATOM   5541  C  C   . GLY B  1 257 ? 44.333  28.241  56.588  1.00 32.15  ? 257 GLY B C   1 
ATOM   5542  O  O   . GLY B  1 257 ? 44.297  27.315  55.806  1.00 35.24  ? 257 GLY B O   1 
ATOM   5543  N  N   . ARG B  1 258 ? 45.408  28.972  56.701  1.00 32.17  ? 258 ARG B N   1 
ATOM   5544  C  CA  . ARG B  1 258 ? 46.513  28.742  55.813  1.00 31.37  ? 258 ARG B CA  1 
ATOM   5545  C  C   . ARG B  1 258 ? 47.201  27.453  56.237  1.00 30.42  ? 258 ARG B C   1 
ATOM   5546  O  O   . ARG B  1 258 ? 47.511  27.258  57.400  1.00 28.44  ? 258 ARG B O   1 
ATOM   5547  C  CB  . ARG B  1 258 ? 47.482  29.910  55.903  1.00 31.37  ? 258 ARG B CB  1 
ATOM   5548  C  CG  . ARG B  1 258 ? 48.697  29.795  55.021  1.00 41.07  ? 258 ARG B CG  1 
ATOM   5549  C  CD  . ARG B  1 258 ? 49.828  30.564  55.668  1.00 62.14  ? 258 ARG B CD  1 
ATOM   5550  N  NE  . ARG B  1 258 ? 51.117  30.477  54.986  1.00 73.10  ? 258 ARG B NE  1 
ATOM   5551  C  CZ  . ARG B  1 258 ? 51.291  30.653  53.679  1.00 79.93  ? 258 ARG B CZ  1 
ATOM   5552  N  NH1 . ARG B  1 258 ? 50.257  30.921  52.881  1.00 85.02  ? 258 ARG B NH1 1 
ATOM   5553  N  NH2 . ARG B  1 258 ? 52.519  30.606  53.180  1.00 84.08  ? 258 ARG B NH2 1 
ATOM   5554  N  N   . GLY B  1 259 ? 47.408  26.561  55.286  1.00 29.62  ? 259 GLY B N   1 
ATOM   5555  C  CA  . GLY B  1 259 ? 48.084  25.323  55.594  1.00 32.44  ? 259 GLY B CA  1 
ATOM   5556  C  C   . GLY B  1 259 ? 47.149  24.141  55.788  1.00 33.12  ? 259 GLY B C   1 
ATOM   5557  O  O   . GLY B  1 259 ? 47.562  22.976  55.667  1.00 34.73  ? 259 GLY B O   1 
ATOM   5558  N  N   . THR B  1 260 ? 45.880  24.428  56.052  1.00 29.73  ? 260 THR B N   1 
ATOM   5559  C  CA  . THR B  1 260 ? 44.908  23.388  56.277  1.00 22.54  ? 260 THR B CA  1 
ATOM   5560  C  C   . THR B  1 260 ? 44.681  22.622  54.981  1.00 24.37  ? 260 THR B C   1 
ATOM   5561  O  O   . THR B  1 260 ? 44.972  23.110  53.887  1.00 26.25  ? 260 THR B O   1 
ATOM   5562  C  CB  . THR B  1 260 ? 43.639  24.023  56.751  1.00 23.74  ? 260 THR B CB  1 
ATOM   5563  O  OG1 . THR B  1 260 ? 43.222  25.007  55.784  1.00 20.05  ? 260 THR B OG1 1 
ATOM   5564  C  CG2 . THR B  1 260 ? 43.894  24.684  58.090  1.00 15.05  ? 260 THR B CG2 1 
ATOM   5565  N  N   . PRO B  1 261 ? 44.083  21.443  55.071  1.00 19.28  ? 261 PRO B N   1 
ATOM   5566  C  CA  . PRO B  1 261 ? 43.870  20.697  53.838  1.00 16.74  ? 261 PRO B CA  1 
ATOM   5567  C  C   . PRO B  1 261 ? 43.016  21.394  52.824  1.00 16.60  ? 261 PRO B C   1 
ATOM   5568  O  O   . PRO B  1 261 ? 43.370  21.370  51.682  1.00 17.51  ? 261 PRO B O   1 
ATOM   5569  C  CB  . PRO B  1 261 ? 43.209  19.422  54.331  1.00 20.36  ? 261 PRO B CB  1 
ATOM   5570  C  CG  . PRO B  1 261 ? 43.793  19.258  55.711  1.00 18.62  ? 261 PRO B CG  1 
ATOM   5571  C  CD  . PRO B  1 261 ? 43.707  20.652  56.247  1.00 16.48  ? 261 PRO B CD  1 
ATOM   5572  N  N   . GLN B  1 262 ? 41.902  22.009  53.217  1.00 19.43  ? 262 GLN B N   1 
ATOM   5573  C  CA  . GLN B  1 262 ? 41.056  22.669  52.227  1.00 21.00  ? 262 GLN B CA  1 
ATOM   5574  C  C   . GLN B  1 262 ? 41.795  23.840  51.531  1.00 22.71  ? 262 GLN B C   1 
ATOM   5575  O  O   . GLN B  1 262 ? 41.744  24.002  50.298  1.00 23.20  ? 262 GLN B O   1 
ATOM   5576  C  CB  . GLN B  1 262 ? 39.759  23.182  52.850  1.00 24.59  ? 262 GLN B CB  1 
ATOM   5577  C  CG  . GLN B  1 262 ? 38.736  23.757  51.806  1.00 30.44  ? 262 GLN B CG  1 
ATOM   5578  C  CD  . GLN B  1 262 ? 37.396  24.311  52.387  1.00 32.46  ? 262 GLN B CD  1 
ATOM   5579  O  OE1 . GLN B  1 262 ? 36.414  24.468  51.662  1.00 32.62  ? 262 GLN B OE1 1 
ATOM   5580  N  NE2 . GLN B  1 262 ? 37.367  24.608  53.682  1.00 38.69  ? 262 GLN B NE2 1 
ATOM   5581  N  N   . TYR B  1 263 ? 42.442  24.683  52.316  1.00 17.17  ? 263 TYR B N   1 
ATOM   5582  C  CA  . TYR B  1 263 ? 43.184  25.787  51.767  1.00 18.72  ? 263 TYR B CA  1 
ATOM   5583  C  C   . TYR B  1 263 ? 44.221  25.236  50.773  1.00 24.12  ? 263 TYR B C   1 
ATOM   5584  O  O   . TYR B  1 263 ? 44.264  25.630  49.609  1.00 27.87  ? 263 TYR B O   1 
ATOM   5585  C  CB  . TYR B  1 263 ? 43.854  26.472  52.921  1.00 26.12  ? 263 TYR B CB  1 
ATOM   5586  C  CG  . TYR B  1 263 ? 44.737  27.598  52.558  1.00 29.95  ? 263 TYR B CG  1 
ATOM   5587  C  CD1 . TYR B  1 263 ? 45.976  27.385  51.938  1.00 29.92  ? 263 TYR B CD1 1 
ATOM   5588  C  CD2 . TYR B  1 263 ? 44.367  28.880  52.875  1.00 35.51  ? 263 TYR B CD2 1 
ATOM   5589  C  CE1 . TYR B  1 263 ? 46.819  28.431  51.648  1.00 34.80  ? 263 TYR B CE1 1 
ATOM   5590  C  CE2 . TYR B  1 263 ? 45.191  29.933  52.596  1.00 38.65  ? 263 TYR B CE2 1 
ATOM   5591  C  CZ  . TYR B  1 263 ? 46.415  29.708  51.984  1.00 41.53  ? 263 TYR B CZ  1 
ATOM   5592  O  OH  . TYR B  1 263 ? 47.217  30.787  51.722  1.00 48.50  ? 263 TYR B OH  1 
ATOM   5593  N  N   . THR B  1 264 ? 45.051  24.306  51.227  1.00 26.00  ? 264 THR B N   1 
ATOM   5594  C  CA  . THR B  1 264 ? 46.068  23.690  50.386  1.00 25.09  ? 264 THR B CA  1 
ATOM   5595  C  C   . THR B  1 264 ? 45.489  23.110  49.106  1.00 27.75  ? 264 THR B C   1 
ATOM   5596  O  O   . THR B  1 264 ? 46.056  23.240  48.017  1.00 30.52  ? 264 THR B O   1 
ATOM   5597  C  CB  . THR B  1 264 ? 46.729  22.566  51.124  1.00 21.66  ? 264 THR B CB  1 
ATOM   5598  O  OG1 . THR B  1 264 ? 47.486  23.086  52.216  1.00 28.57  ? 264 THR B OG1 1 
ATOM   5599  C  CG2 . THR B  1 264 ? 47.627  21.854  50.218  1.00 24.10  ? 264 THR B CG2 1 
ATOM   5600  N  N   . TRP B  1 265 ? 44.362  22.438  49.241  1.00 29.78  ? 265 TRP B N   1 
ATOM   5601  C  CA  . TRP B  1 265 ? 43.729  21.842  48.083  1.00 29.70  ? 265 TRP B CA  1 
ATOM   5602  C  C   . TRP B  1 265 ? 43.316  22.894  47.070  1.00 27.22  ? 265 TRP B C   1 
ATOM   5603  O  O   . TRP B  1 265 ? 43.742  22.837  45.927  1.00 32.23  ? 265 TRP B O   1 
ATOM   5604  C  CB  . TRP B  1 265 ? 42.508  21.004  48.482  1.00 31.53  ? 265 TRP B CB  1 
ATOM   5605  C  CG  . TRP B  1 265 ? 41.819  20.415  47.279  1.00 28.36  ? 265 TRP B CG  1 
ATOM   5606  C  CD1 . TRP B  1 265 ? 42.226  19.340  46.553  1.00 26.86  ? 265 TRP B CD1 1 
ATOM   5607  C  CD2 . TRP B  1 265 ? 40.631  20.914  46.639  1.00 24.93  ? 265 TRP B CD2 1 
ATOM   5608  N  NE1 . TRP B  1 265 ? 41.362  19.134  45.495  1.00 28.89  ? 265 TRP B NE1 1 
ATOM   5609  C  CE2 . TRP B  1 265 ? 40.380  20.089  45.526  1.00 23.29  ? 265 TRP B CE2 1 
ATOM   5610  C  CE3 . TRP B  1 265 ? 39.769  21.992  46.897  1.00 24.53  ? 265 TRP B CE3 1 
ATOM   5611  C  CZ2 . TRP B  1 265 ? 39.300  20.302  44.667  1.00 26.88  ? 265 TRP B CZ2 1 
ATOM   5612  C  CZ3 . TRP B  1 265 ? 38.703  22.210  46.045  1.00 23.90  ? 265 TRP B CZ3 1 
ATOM   5613  C  CH2 . TRP B  1 265 ? 38.477  21.363  44.939  1.00 27.56  ? 265 TRP B CH2 1 
ATOM   5614  N  N   . LEU B  1 266 ? 42.509  23.859  47.500  1.00 25.40  ? 266 LEU B N   1 
ATOM   5615  C  CA  . LEU B  1 266 ? 42.016  24.886  46.614  1.00 23.72  ? 266 LEU B CA  1 
ATOM   5616  C  C   . LEU B  1 266 ? 43.132  25.572  45.873  1.00 28.92  ? 266 LEU B C   1 
ATOM   5617  O  O   . LEU B  1 266 ? 43.024  25.827  44.677  1.00 33.51  ? 266 LEU B O   1 
ATOM   5618  C  CB  . LEU B  1 266 ? 41.223  25.902  47.403  1.00 18.89  ? 266 LEU B CB  1 
ATOM   5619  C  CG  . LEU B  1 266 ? 40.700  27.081  46.598  1.00 17.54  ? 266 LEU B CG  1 
ATOM   5620  C  CD1 . LEU B  1 266 ? 39.873  26.637  45.444  1.00 16.60  ? 266 LEU B CD1 1 
ATOM   5621  C  CD2 . LEU B  1 266 ? 39.861  27.862  47.531  1.00 22.02  ? 266 LEU B CD2 1 
ATOM   5622  N  N   . LYS B  1 267 ? 44.234  25.830  46.571  1.00 32.31  ? 267 LYS B N   1 
ATOM   5623  C  CA  . LYS B  1 267 ? 45.353  26.522  45.958  1.00 32.07  ? 267 LYS B CA  1 
ATOM   5624  C  C   . LYS B  1 267 ? 45.853  25.755  44.776  1.00 32.70  ? 267 LYS B C   1 
ATOM   5625  O  O   . LYS B  1 267 ? 45.948  26.310  43.718  1.00 38.21  ? 267 LYS B O   1 
ATOM   5626  C  CB  . LYS B  1 267 ? 46.459  26.739  46.951  1.00 36.28  ? 267 LYS B CB  1 
ATOM   5627  C  CG  . LYS B  1 267 ? 47.475  27.748  46.522  1.00 44.89  ? 267 LYS B CG  1 
ATOM   5628  C  CD  . LYS B  1 267 ? 48.550  27.902  47.587  1.00 48.61  ? 267 LYS B CD  1 
ATOM   5629  C  CE  . LYS B  1 267 ? 49.594  28.929  47.193  1.00 58.68  ? 267 LYS B CE  1 
ATOM   5630  N  NZ  . LYS B  1 267 ? 50.635  29.086  48.250  1.00 72.65  ? 267 LYS B NZ  1 
ATOM   5631  N  N   . LYS B  1 268 ? 46.137  24.474  44.929  1.00 32.66  ? 268 LYS B N   1 
ATOM   5632  C  CA  . LYS B  1 268 ? 46.594  23.694  43.788  1.00 36.63  ? 268 LYS B CA  1 
ATOM   5633  C  C   . LYS B  1 268 ? 45.518  23.483  42.739  1.00 33.50  ? 268 LYS B C   1 
ATOM   5634  O  O   . LYS B  1 268 ? 45.814  23.380  41.546  1.00 32.67  ? 268 LYS B O   1 
ATOM   5635  C  CB  . LYS B  1 268 ? 47.092  22.325  44.214  1.00 48.09  ? 268 LYS B CB  1 
ATOM   5636  C  CG  . LYS B  1 268 ? 48.336  22.368  45.102  1.00 65.55  ? 268 LYS B CG  1 
ATOM   5637  C  CD  . LYS B  1 268 ? 48.796  20.972  45.567  1.00 75.61  ? 268 LYS B CD  1 
ATOM   5638  C  CE  . LYS B  1 268 ? 49.971  21.076  46.565  1.00 82.74  ? 268 LYS B CE  1 
ATOM   5639  N  NZ  . LYS B  1 268 ? 50.292  19.803  47.318  1.00 98.89  ? 268 LYS B NZ  1 
ATOM   5640  N  N   . GLU B  1 269 ? 44.269  23.400  43.163  1.00 28.16  ? 269 GLU B N   1 
ATOM   5641  C  CA  . GLU B  1 269 ? 43.226  23.155  42.212  1.00 28.70  ? 269 GLU B CA  1 
ATOM   5642  C  C   . GLU B  1 269 ? 43.086  24.322  41.281  1.00 31.58  ? 269 GLU B C   1 
ATOM   5643  O  O   . GLU B  1 269 ? 42.970  24.118  40.075  1.00 38.34  ? 269 GLU B O   1 
ATOM   5644  C  CB  . GLU B  1 269 ? 41.894  22.873  42.901  1.00 30.28  ? 269 GLU B CB  1 
ATOM   5645  C  CG  . GLU B  1 269 ? 40.741  22.569  41.940  1.00 31.06  ? 269 GLU B CG  1 
ATOM   5646  C  CD  . GLU B  1 269 ? 40.933  21.273  41.177  1.00 38.00  ? 269 GLU B CD  1 
ATOM   5647  O  OE1 . GLU B  1 269 ? 41.832  20.475  41.529  1.00 42.67  ? 269 GLU B OE1 1 
ATOM   5648  O  OE2 . GLU B  1 269 ? 40.171  21.037  40.213  1.00 44.23  ? 269 GLU B OE2 1 
ATOM   5649  N  N   . LEU B  1 270 ? 43.139  25.543  41.798  1.00 27.43  ? 270 LEU B N   1 
ATOM   5650  C  CA  . LEU B  1 270 ? 42.985  26.692  40.931  1.00 26.40  ? 270 LEU B CA  1 
ATOM   5651  C  C   . LEU B  1 270 ? 44.012  26.649  39.812  1.00 33.33  ? 270 LEU B C   1 
ATOM   5652  O  O   . LEU B  1 270 ? 43.706  26.977  38.677  1.00 37.89  ? 270 LEU B O   1 
ATOM   5653  C  CB  . LEU B  1 270 ? 43.078  27.974  41.738  1.00 16.72  ? 270 LEU B CB  1 
ATOM   5654  C  CG  . LEU B  1 270 ? 41.739  28.210  42.447  1.00 20.10  ? 270 LEU B CG  1 
ATOM   5655  C  CD1 . LEU B  1 270 ? 41.902  29.347  43.420  1.00 15.06  ? 270 LEU B CD1 1 
ATOM   5656  C  CD2 . LEU B  1 270 ? 40.618  28.500  41.442  1.00 12.29  ? 270 LEU B CD2 1 
ATOM   5657  N  N   . ARG B  1 271 ? 45.207  26.151  40.110  1.00 38.64  ? 271 ARG B N   1 
ATOM   5658  C  CA  . ARG B  1 271 ? 46.256  26.032  39.110  1.00 41.68  ? 271 ARG B CA  1 
ATOM   5659  C  C   . ARG B  1 271 ? 45.974  24.926  38.111  1.00 42.41  ? 271 ARG B C   1 
ATOM   5660  O  O   . ARG B  1 271 ? 46.539  24.929  37.042  1.00 49.21  ? 271 ARG B O   1 
ATOM   5661  C  CB  . ARG B  1 271 ? 47.620  25.719  39.726  1.00 47.95  ? 271 ARG B CB  1 
ATOM   5662  C  CG  . ARG B  1 271 ? 48.165  26.701  40.769  1.00 64.06  ? 271 ARG B CG  1 
ATOM   5663  C  CD  . ARG B  1 271 ? 49.643  26.376  41.061  1.00 76.06  ? 271 ARG B CD  1 
ATOM   5664  N  NE  . ARG B  1 271 ? 50.111  26.779  42.393  1.00 85.81  ? 271 ARG B NE  1 
ATOM   5665  C  CZ  . ARG B  1 271 ? 50.643  25.935  43.286  1.00 92.98  ? 271 ARG B CZ  1 
ATOM   5666  N  NH1 . ARG B  1 271 ? 50.775  24.633  43.006  1.00 95.12  ? 271 ARG B NH1 1 
ATOM   5667  N  NH2 . ARG B  1 271 ? 51.073  26.396  44.456  1.00 95.21  ? 271 ARG B NH2 1 
ATOM   5668  N  N   . LYS B  1 272 ? 45.173  23.936  38.458  1.00 43.43  ? 272 LYS B N   1 
ATOM   5669  C  CA  . LYS B  1 272 ? 44.917  22.852  37.522  1.00 42.13  ? 272 LYS B CA  1 
ATOM   5670  C  C   . LYS B  1 272 ? 43.816  23.185  36.511  1.00 43.09  ? 272 LYS B C   1 
ATOM   5671  O  O   . LYS B  1 272 ? 43.528  22.365  35.609  1.00 42.79  ? 272 LYS B O   1 
ATOM   5672  C  CB  . LYS B  1 272 ? 44.533  21.569  38.271  1.00 46.85  ? 272 LYS B CB  1 
ATOM   5673  C  CG  . LYS B  1 272 ? 45.524  21.050  39.314  1.00 56.80  ? 272 LYS B CG  1 
ATOM   5674  C  CD  . LYS B  1 272 ? 45.226  19.561  39.631  1.00 69.24  ? 272 LYS B CD  1 
ATOM   5675  C  CE  . LYS B  1 272 ? 45.554  19.095  41.087  1.00 78.10  ? 272 LYS B CE  1 
ATOM   5676  N  NZ  . LYS B  1 272 ? 44.381  19.114  42.083  1.00 85.13  ? 272 LYS B NZ  1 
ATOM   5677  N  N   . VAL B  1 273 ? 43.170  24.347  36.674  1.00 40.73  ? 273 VAL B N   1 
ATOM   5678  C  CA  . VAL B  1 273 ? 42.085  24.752  35.786  1.00 40.02  ? 273 VAL B CA  1 
ATOM   5679  C  C   . VAL B  1 273 ? 42.638  25.157  34.440  1.00 45.34  ? 273 VAL B C   1 
ATOM   5680  O  O   . VAL B  1 273 ? 43.549  25.966  34.393  1.00 51.32  ? 273 VAL B O   1 
ATOM   5681  C  CB  . VAL B  1 273 ? 41.352  25.957  36.328  1.00 31.40  ? 273 VAL B CB  1 
ATOM   5682  C  CG1 . VAL B  1 273 ? 40.242  26.292  35.460  1.00 28.74  ? 273 VAL B CG1 1 
ATOM   5683  C  CG2 . VAL B  1 273 ? 40.808  25.657  37.654  1.00 38.74  ? 273 VAL B CG2 1 
ATOM   5684  N  N   . LYS B  1 274 ? 42.109  24.605  33.352  1.00 47.56  ? 274 LYS B N   1 
ATOM   5685  C  CA  . LYS B  1 274 ? 42.554  24.972  31.994  1.00 48.47  ? 274 LYS B CA  1 
ATOM   5686  C  C   . LYS B  1 274 ? 41.348  25.561  31.263  1.00 48.12  ? 274 LYS B C   1 
ATOM   5687  O  O   . LYS B  1 274 ? 40.406  24.844  30.929  1.00 51.36  ? 274 LYS B O   1 
ATOM   5688  C  CB  . LYS B  1 274 ? 43.063  23.744  31.232  1.00 49.80  ? 274 LYS B CB  1 
ATOM   5689  C  CG  . LYS B  1 274 ? 44.447  23.279  31.630  1.00 61.68  ? 274 LYS B CG  1 
ATOM   5690  C  CD  . LYS B  1 274 ? 44.739  21.836  31.166  1.00 76.26  ? 274 LYS B CD  1 
ATOM   5691  C  CE  . LYS B  1 274 ? 44.620  21.619  29.632  1.00 84.48  ? 274 LYS B CE  1 
ATOM   5692  N  NZ  . LYS B  1 274 ? 44.889  20.189  29.183  1.00 88.98  ? 274 LYS B NZ  1 
ATOM   5693  N  N   . ARG B  1 275 ? 41.345  26.860  31.016  1.00 44.65  ? 275 ARG B N   1 
ATOM   5694  C  CA  . ARG B  1 275 ? 40.203  27.461  30.340  1.00 37.44  ? 275 ARG B CA  1 
ATOM   5695  C  C   . ARG B  1 275 ? 40.109  27.210  28.854  1.00 39.80  ? 275 ARG B C   1 
ATOM   5696  O  O   . ARG B  1 275 ? 39.122  27.564  28.237  1.00 38.42  ? 275 ARG B O   1 
ATOM   5697  C  CB  . ARG B  1 275 ? 40.218  28.912  30.587  1.00 31.14  ? 275 ARG B CB  1 
ATOM   5698  C  CG  . ARG B  1 275 ? 40.168  29.190  32.029  1.00 32.25  ? 275 ARG B CG  1 
ATOM   5699  C  CD  . ARG B  1 275 ? 38.756  29.414  32.489  1.00 30.82  ? 275 ARG B CD  1 
ATOM   5700  N  NE  . ARG B  1 275 ? 38.810  30.433  33.522  1.00 32.93  ? 275 ARG B NE  1 
ATOM   5701  C  CZ  . ARG B  1 275 ? 37.868  31.348  33.742  1.00 35.17  ? 275 ARG B CZ  1 
ATOM   5702  N  NH1 . ARG B  1 275 ? 36.756  31.380  33.007  1.00 29.76  ? 275 ARG B NH1 1 
ATOM   5703  N  NH2 . ARG B  1 275 ? 38.062  32.272  34.671  1.00 24.72  ? 275 ARG B NH2 1 
ATOM   5704  N  N   . SER B  1 276 ? 41.179  26.690  28.275  1.00 40.64  ? 276 SER B N   1 
ATOM   5705  C  CA  . SER B  1 276 ? 41.202  26.334  26.876  1.00 44.44  ? 276 SER B CA  1 
ATOM   5706  C  C   . SER B  1 276 ? 40.412  25.066  26.780  1.00 46.25  ? 276 SER B C   1 
ATOM   5707  O  O   . SER B  1 276 ? 40.010  24.673  25.710  1.00 50.05  ? 276 SER B O   1 
ATOM   5708  C  CB  . SER B  1 276 ? 42.628  26.025  26.434  1.00 51.87  ? 276 SER B CB  1 
ATOM   5709  O  OG  . SER B  1 276 ? 43.524  25.969  27.549  1.00 60.73  ? 276 SER B OG  1 
ATOM   5710  N  N   . GLU B  1 277 ? 40.231  24.413  27.920  1.00 48.97  ? 277 GLU B N   1 
ATOM   5711  C  CA  . GLU B  1 277 ? 39.508  23.160  28.026  1.00 48.15  ? 277 GLU B CA  1 
ATOM   5712  C  C   . GLU B  1 277 ? 38.097  23.375  28.578  1.00 45.34  ? 277 GLU B C   1 
ATOM   5713  O  O   . GLU B  1 277 ? 37.132  22.934  27.985  1.00 45.90  ? 277 GLU B O   1 
ATOM   5714  C  CB  . GLU B  1 277 ? 40.308  22.191  28.897  1.00 55.75  ? 277 GLU B CB  1 
ATOM   5715  C  CG  . GLU B  1 277 ? 39.704  20.794  29.060  1.00 74.27  ? 277 GLU B CG  1 
ATOM   5716  C  CD  . GLU B  1 277 ? 40.686  19.747  29.653  1.00 83.83  ? 277 GLU B CD  1 
ATOM   5717  O  OE1 . GLU B  1 277 ? 41.872  19.703  29.223  1.00 87.30  ? 277 GLU B OE1 1 
ATOM   5718  O  OE2 . GLU B  1 277 ? 40.258  18.937  30.524  1.00 91.51  ? 277 GLU B OE2 1 
ATOM   5719  N  N   . THR B  1 278 ? 37.963  24.015  29.726  1.00 43.19  ? 278 THR B N   1 
ATOM   5720  C  CA  . THR B  1 278 ? 36.639  24.257  30.288  1.00 41.15  ? 278 THR B CA  1 
ATOM   5721  C  C   . THR B  1 278 ? 36.637  25.720  30.526  1.00 41.40  ? 278 THR B C   1 
ATOM   5722  O  O   . THR B  1 278 ? 37.160  26.213  31.510  1.00 41.72  ? 278 THR B O   1 
ATOM   5723  C  CB  . THR B  1 278 ? 36.423  23.551  31.609  1.00 40.20  ? 278 THR B CB  1 
ATOM   5724  O  OG1 . THR B  1 278 ? 37.579  23.733  32.439  1.00 35.41  ? 278 THR B OG1 1 
ATOM   5725  C  CG2 . THR B  1 278 ? 36.160  22.083  31.368  1.00 42.52  ? 278 THR B CG2 1 
ATOM   5726  N  N   . PRO B  1 279 ? 36.112  26.451  29.572  1.00 41.47  ? 279 PRO B N   1 
ATOM   5727  C  CA  . PRO B  1 279 ? 36.046  27.900  29.642  1.00 40.79  ? 279 PRO B CA  1 
ATOM   5728  C  C   . PRO B  1 279 ? 35.388  28.452  30.877  1.00 41.81  ? 279 PRO B C   1 
ATOM   5729  O  O   . PRO B  1 279 ? 35.870  29.422  31.477  1.00 41.80  ? 279 PRO B O   1 
ATOM   5730  C  CB  . PRO B  1 279 ? 35.270  28.266  28.369  1.00 42.18  ? 279 PRO B CB  1 
ATOM   5731  C  CG  . PRO B  1 279 ? 34.475  27.032  28.064  1.00 44.37  ? 279 PRO B CG  1 
ATOM   5732  C  CD  . PRO B  1 279 ? 35.473  25.946  28.346  1.00 42.62  ? 279 PRO B CD  1 
ATOM   5733  N  N   . TRP B  1 280 ? 34.311  27.818  31.293  1.00 41.62  ? 280 TRP B N   1 
ATOM   5734  C  CA  . TRP B  1 280 ? 33.556  28.330  32.426  1.00 42.72  ? 280 TRP B CA  1 
ATOM   5735  C  C   . TRP B  1 280 ? 34.016  27.838  33.769  1.00 42.80  ? 280 TRP B C   1 
ATOM   5736  O  O   . TRP B  1 280 ? 34.013  26.640  34.019  1.00 49.26  ? 280 TRP B O   1 
ATOM   5737  C  CB  . TRP B  1 280 ? 32.092  27.999  32.214  1.00 42.86  ? 280 TRP B CB  1 
ATOM   5738  C  CG  . TRP B  1 280 ? 31.561  28.722  31.059  1.00 41.12  ? 280 TRP B CG  1 
ATOM   5739  C  CD1 . TRP B  1 280 ? 31.419  28.252  29.775  1.00 43.32  ? 280 TRP B CD1 1 
ATOM   5740  C  CD2 . TRP B  1 280 ? 31.132  30.077  31.046  1.00 41.59  ? 280 TRP B CD2 1 
ATOM   5741  N  NE1 . TRP B  1 280 ? 30.921  29.248  28.961  1.00 42.43  ? 280 TRP B NE1 1 
ATOM   5742  C  CE2 . TRP B  1 280 ? 30.737  30.380  29.716  1.00 41.81  ? 280 TRP B CE2 1 
ATOM   5743  C  CE3 . TRP B  1 280 ? 31.055  31.078  32.025  1.00 42.93  ? 280 TRP B CE3 1 
ATOM   5744  C  CZ2 . TRP B  1 280 ? 30.268  31.643  29.345  1.00 40.62  ? 280 TRP B CZ2 1 
ATOM   5745  C  CZ3 . TRP B  1 280 ? 30.594  32.338  31.656  1.00 41.57  ? 280 TRP B CZ3 1 
ATOM   5746  C  CH2 . TRP B  1 280 ? 30.207  32.606  30.325  1.00 41.85  ? 280 TRP B CH2 1 
ATOM   5747  N  N   . LEU B  1 281 ? 34.331  28.766  34.658  1.00 35.84  ? 281 LEU B N   1 
ATOM   5748  C  CA  . LEU B  1 281 ? 34.825  28.406  35.981  1.00 32.78  ? 281 LEU B CA  1 
ATOM   5749  C  C   . LEU B  1 281 ? 33.803  28.842  37.005  1.00 33.16  ? 281 LEU B C   1 
ATOM   5750  O  O   . LEU B  1 281 ? 33.665  30.037  37.233  1.00 34.50  ? 281 LEU B O   1 
ATOM   5751  C  CB  . LEU B  1 281 ? 36.160  29.109  36.243  1.00 28.73  ? 281 LEU B CB  1 
ATOM   5752  C  CG  . LEU B  1 281 ? 36.815  28.913  37.592  1.00 27.81  ? 281 LEU B CG  1 
ATOM   5753  C  CD1 . LEU B  1 281 ? 37.208  27.470  37.769  1.00 28.34  ? 281 LEU B CD1 1 
ATOM   5754  C  CD2 . LEU B  1 281 ? 38.032  29.758  37.630  1.00 30.86  ? 281 LEU B CD2 1 
ATOM   5755  N  N   . ILE B  1 282 ? 33.182  27.871  37.680  1.00 28.67  ? 282 ILE B N   1 
ATOM   5756  C  CA  . ILE B  1 282 ? 32.143  28.115  38.669  1.00 23.09  ? 282 ILE B CA  1 
ATOM   5757  C  C   . ILE B  1 282 ? 32.564  27.678  40.038  1.00 22.38  ? 282 ILE B C   1 
ATOM   5758  O  O   . ILE B  1 282 ? 33.152  26.625  40.175  1.00 28.51  ? 282 ILE B O   1 
ATOM   5759  C  CB  . ILE B  1 282 ? 30.920  27.280  38.310  1.00 23.91  ? 282 ILE B CB  1 
ATOM   5760  C  CG1 . ILE B  1 282 ? 30.478  27.643  36.905  1.00 26.76  ? 282 ILE B CG1 1 
ATOM   5761  C  CG2 . ILE B  1 282 ? 29.764  27.504  39.294  1.00 16.11  ? 282 ILE B CG2 1 
ATOM   5762  C  CD1 . ILE B  1 282 ? 29.454  26.709  36.361  1.00 27.20  ? 282 ILE B CD1 1 
ATOM   5763  N  N   . VAL B  1 283 ? 32.156  28.393  41.065  1.00 14.30  ? 283 VAL B N   1 
ATOM   5764  C  CA  . VAL B  1 283 ? 32.526  27.982  42.394  1.00 16.39  ? 283 VAL B CA  1 
ATOM   5765  C  C   . VAL B  1 283 ? 31.271  27.908  43.210  1.00 23.32  ? 283 VAL B C   1 
ATOM   5766  O  O   . VAL B  1 283 ? 30.432  28.792  43.083  1.00 30.80  ? 283 VAL B O   1 
ATOM   5767  C  CB  . VAL B  1 283 ? 33.479  29.002  43.067  1.00 14.66  ? 283 VAL B CB  1 
ATOM   5768  C  CG1 . VAL B  1 283 ? 33.629  28.710  44.564  1.00 7.35   ? 283 VAL B CG1 1 
ATOM   5769  C  CG2 . VAL B  1 283 ? 34.822  28.921  42.427  1.00 7.85   ? 283 VAL B CG2 1 
ATOM   5770  N  N   . LEU B  1 284 ? 31.167  26.907  44.096  1.00 25.80  ? 284 LEU B N   1 
ATOM   5771  C  CA  . LEU B  1 284 ? 30.006  26.744  44.981  1.00 22.80  ? 284 LEU B CA  1 
ATOM   5772  C  C   . LEU B  1 284 ? 30.451  26.791  46.434  1.00 22.41  ? 284 LEU B C   1 
ATOM   5773  O  O   . LEU B  1 284 ? 31.537  26.326  46.772  1.00 24.61  ? 284 LEU B O   1 
ATOM   5774  C  CB  . LEU B  1 284 ? 29.344  25.413  44.759  1.00 23.02  ? 284 LEU B CB  1 
ATOM   5775  C  CG  . LEU B  1 284 ? 28.975  25.032  43.342  1.00 28.59  ? 284 LEU B CG  1 
ATOM   5776  C  CD1 . LEU B  1 284 ? 28.360  23.623  43.331  1.00 27.66  ? 284 LEU B CD1 1 
ATOM   5777  C  CD2 . LEU B  1 284 ? 28.030  26.074  42.780  1.00 29.04  ? 284 LEU B CD2 1 
ATOM   5778  N  N   . MET B  1 285 ? 29.590  27.333  47.284  1.00 18.17  ? 285 MET B N   1 
ATOM   5779  C  CA  . MET B  1 285 ? 29.811  27.466  48.708  1.00 22.62  ? 285 MET B CA  1 
ATOM   5780  C  C   . MET B  1 285 ? 28.448  27.816  49.349  1.00 27.55  ? 285 MET B C   1 
ATOM   5781  O  O   . MET B  1 285 ? 27.519  28.291  48.679  1.00 31.03  ? 285 MET B O   1 
ATOM   5782  C  CB  . MET B  1 285 ? 30.885  28.528  49.011  1.00 22.74  ? 285 MET B CB  1 
ATOM   5783  C  CG  . MET B  1 285 ? 30.593  29.916  48.517  1.00 23.14  ? 285 MET B CG  1 
ATOM   5784  S  SD  . MET B  1 285 ? 31.732  31.162  49.126  1.00 30.31  ? 285 MET B SD  1 
ATOM   5785  C  CE  . MET B  1 285 ? 33.042  30.962  47.880  1.00 25.74  ? 285 MET B CE  1 
ATOM   5786  N  N   . HIS B  1 286 ? 28.304  27.576  50.639  1.00 28.03  ? 286 HIS B N   1 
ATOM   5787  C  CA  . HIS B  1 286 ? 27.023  27.841  51.239  1.00 30.05  ? 286 HIS B CA  1 
ATOM   5788  C  C   . HIS B  1 286 ? 26.901  29.254  51.680  1.00 29.72  ? 286 HIS B C   1 
ATOM   5789  O  O   . HIS B  1 286 ? 26.000  29.933  51.246  1.00 36.85  ? 286 HIS B O   1 
ATOM   5790  C  CB  . HIS B  1 286 ? 26.753  26.906  52.398  1.00 30.54  ? 286 HIS B CB  1 
ATOM   5791  C  CG  . HIS B  1 286 ? 25.403  27.064  52.995  1.00 30.00  ? 286 HIS B CG  1 
ATOM   5792  N  ND1 . HIS B  1 286 ? 24.270  26.617  52.351  1.00 28.98  ? 286 HIS B ND1 1 
ATOM   5793  C  CD2 . HIS B  1 286 ? 24.996  27.535  54.203  1.00 30.68  ? 286 HIS B CD2 1 
ATOM   5794  C  CE1 . HIS B  1 286 ? 23.229  26.812  53.143  1.00 33.38  ? 286 HIS B CE1 1 
ATOM   5795  N  NE2 . HIS B  1 286 ? 23.646  27.359  54.265  1.00 29.77  ? 286 HIS B NE2 1 
ATOM   5796  N  N   . SER B  1 287 ? 27.809  29.703  52.531  1.00 32.64  ? 287 SER B N   1 
ATOM   5797  C  CA  . SER B  1 287 ? 27.766  31.071  53.038  1.00 36.72  ? 287 SER B CA  1 
ATOM   5798  C  C   . SER B  1 287 ? 28.366  31.962  51.997  1.00 41.45  ? 287 SER B C   1 
ATOM   5799  O  O   . SER B  1 287 ? 29.551  31.816  51.639  1.00 46.06  ? 287 SER B O   1 
ATOM   5800  C  CB  . SER B  1 287 ? 28.563  31.239  54.334  1.00 40.71  ? 287 SER B CB  1 
ATOM   5801  O  OG  . SER B  1 287 ? 27.958  32.182  55.222  1.00 42.37  ? 287 SER B OG  1 
ATOM   5802  N  N   . PRO B  1 288 ? 27.570  32.933  51.532  1.00 42.15  ? 288 PRO B N   1 
ATOM   5803  C  CA  . PRO B  1 288 ? 27.855  33.948  50.522  1.00 38.83  ? 288 PRO B CA  1 
ATOM   5804  C  C   . PRO B  1 288 ? 28.884  35.005  50.999  1.00 38.18  ? 288 PRO B C   1 
ATOM   5805  O  O   . PRO B  1 288 ? 28.779  35.515  52.139  1.00 35.05  ? 288 PRO B O   1 
ATOM   5806  C  CB  . PRO B  1 288 ? 26.487  34.543  50.317  1.00 43.15  ? 288 PRO B CB  1 
ATOM   5807  C  CG  . PRO B  1 288 ? 25.908  34.523  51.738  1.00 37.96  ? 288 PRO B CG  1 
ATOM   5808  C  CD  . PRO B  1 288 ? 26.272  33.183  52.201  1.00 41.84  ? 288 PRO B CD  1 
ATOM   5809  N  N   . LEU B  1 289 ? 29.849  35.331  50.120  1.00 32.47  ? 289 LEU B N   1 
ATOM   5810  C  CA  . LEU B  1 289 ? 30.904  36.318  50.421  1.00 32.96  ? 289 LEU B CA  1 
ATOM   5811  C  C   . LEU B  1 289 ? 30.438  37.788  50.409  1.00 34.25  ? 289 LEU B C   1 
ATOM   5812  O  O   . LEU B  1 289 ? 30.905  38.658  51.192  1.00 36.56  ? 289 LEU B O   1 
ATOM   5813  C  CB  . LEU B  1 289 ? 32.047  36.145  49.440  1.00 26.05  ? 289 LEU B CB  1 
ATOM   5814  C  CG  . LEU B  1 289 ? 32.778  34.799  49.506  1.00 27.90  ? 289 LEU B CG  1 
ATOM   5815  C  CD1 . LEU B  1 289 ? 34.085  34.775  48.704  1.00 20.20  ? 289 LEU B CD1 1 
ATOM   5816  C  CD2 . LEU B  1 289 ? 33.098  34.519  50.953  1.00 30.26  ? 289 LEU B CD2 1 
ATOM   5817  N  N   . TYR B  1 290 ? 29.517  38.027  49.479  1.00 37.09  ? 290 TYR B N   1 
ATOM   5818  C  CA  . TYR B  1 290 ? 28.850  39.300  49.206  1.00 35.09  ? 290 TYR B CA  1 
ATOM   5819  C  C   . TYR B  1 290 ? 27.342  39.060  49.412  1.00 34.21  ? 290 TYR B C   1 
ATOM   5820  O  O   . TYR B  1 290 ? 26.725  38.210  48.714  1.00 30.55  ? 290 TYR B O   1 
ATOM   5821  C  CB  . TYR B  1 290 ? 29.117  39.708  47.744  1.00 37.52  ? 290 TYR B CB  1 
ATOM   5822  C  CG  . TYR B  1 290 ? 30.478  40.351  47.539  1.00 36.81  ? 290 TYR B CG  1 
ATOM   5823  C  CD1 . TYR B  1 290 ? 30.693  41.676  47.940  1.00 39.63  ? 290 TYR B CD1 1 
ATOM   5824  C  CD2 . TYR B  1 290 ? 31.570  39.615  47.084  1.00 33.26  ? 290 TYR B CD2 1 
ATOM   5825  C  CE1 . TYR B  1 290 ? 31.960  42.252  47.919  1.00 36.62  ? 290 TYR B CE1 1 
ATOM   5826  C  CE2 . TYR B  1 290 ? 32.843  40.188  47.058  1.00 36.27  ? 290 TYR B CE2 1 
ATOM   5827  C  CZ  . TYR B  1 290 ? 33.019  41.505  47.485  1.00 34.96  ? 290 TYR B CZ  1 
ATOM   5828  O  OH  . TYR B  1 290 ? 34.253  42.078  47.516  1.00 35.52  ? 290 TYR B OH  1 
ATOM   5829  N  N   . ASN B  1 291 ? 26.774  39.760  50.404  1.00 35.73  ? 291 ASN B N   1 
ATOM   5830  C  CA  . ASN B  1 291 ? 25.338  39.658  50.768  1.00 36.61  ? 291 ASN B CA  1 
ATOM   5831  C  C   . ASN B  1 291 ? 24.866  40.900  51.534  1.00 40.30  ? 291 ASN B C   1 
ATOM   5832  O  O   . ASN B  1 291 ? 25.447  41.254  52.585  1.00 38.99  ? 291 ASN B O   1 
ATOM   5833  C  CB  . ASN B  1 291 ? 25.092  38.399  51.613  1.00 36.31  ? 291 ASN B CB  1 
ATOM   5834  C  CG  . ASN B  1 291 ? 23.872  38.516  52.534  1.00 35.51  ? 291 ASN B CG  1 
ATOM   5835  O  OD1 . ASN B  1 291 ? 23.987  38.407  53.761  1.00 35.20  ? 291 ASN B OD1 1 
ATOM   5836  N  ND2 . ASN B  1 291 ? 22.704  38.699  51.947  1.00 36.53  ? 291 ASN B ND2 1 
ATOM   5837  N  N   . SER B  1 292 ? 23.786  41.517  51.039  1.00 41.97  ? 292 SER B N   1 
ATOM   5838  C  CA  . SER B  1 292 ? 23.267  42.742  51.646  1.00 45.28  ? 292 SER B CA  1 
ATOM   5839  C  C   . SER B  1 292 ? 21.989  42.573  52.428  1.00 47.12  ? 292 SER B C   1 
ATOM   5840  O  O   . SER B  1 292 ? 21.252  43.551  52.597  1.00 47.61  ? 292 SER B O   1 
ATOM   5841  C  CB  . SER B  1 292 ? 23.057  43.827  50.591  1.00 45.13  ? 292 SER B CB  1 
ATOM   5842  O  OG  . SER B  1 292 ? 22.051  43.441  49.661  1.00 45.19  ? 292 SER B OG  1 
ATOM   5843  N  N   . TYR B  1 293 ? 21.659  41.343  52.822  1.00 44.35  ? 293 TYR B N   1 
ATOM   5844  C  CA  . TYR B  1 293 ? 20.466  41.139  53.632  1.00 41.37  ? 293 TYR B CA  1 
ATOM   5845  C  C   . TYR B  1 293 ? 20.919  41.168  55.049  1.00 44.69  ? 293 TYR B C   1 
ATOM   5846  O  O   . TYR B  1 293 ? 22.066  40.907  55.311  1.00 49.76  ? 293 TYR B O   1 
ATOM   5847  C  CB  . TYR B  1 293 ? 19.858  39.824  53.381  1.00 36.06  ? 293 TYR B CB  1 
ATOM   5848  C  CG  . TYR B  1 293 ? 19.142  39.801  52.100  1.00 34.27  ? 293 TYR B CG  1 
ATOM   5849  C  CD1 . TYR B  1 293 ? 19.828  39.781  50.903  1.00 32.21  ? 293 TYR B CD1 1 
ATOM   5850  C  CD2 . TYR B  1 293 ? 17.768  39.700  52.078  1.00 36.13  ? 293 TYR B CD2 1 
ATOM   5851  C  CE1 . TYR B  1 293 ? 19.148  39.635  49.687  1.00 33.90  ? 293 TYR B CE1 1 
ATOM   5852  C  CE2 . TYR B  1 293 ? 17.074  39.567  50.892  1.00 33.91  ? 293 TYR B CE2 1 
ATOM   5853  C  CZ  . TYR B  1 293 ? 17.765  39.530  49.694  1.00 36.95  ? 293 TYR B CZ  1 
ATOM   5854  O  OH  . TYR B  1 293 ? 17.083  39.383  48.511  1.00 39.91  ? 293 TYR B OH  1 
ATOM   5855  N  N   . ASN B  1 294 ? 20.017  41.410  55.981  1.00 47.97  ? 294 ASN B N   1 
ATOM   5856  C  CA  . ASN B  1 294 ? 20.411  41.503  57.384  1.00 54.70  ? 294 ASN B CA  1 
ATOM   5857  C  C   . ASN B  1 294 ? 20.730  40.153  57.975  1.00 57.79  ? 294 ASN B C   1 
ATOM   5858  O  O   . ASN B  1 294 ? 21.580  40.017  58.868  1.00 58.03  ? 294 ASN B O   1 
ATOM   5859  C  CB  . ASN B  1 294 ? 19.320  42.154  58.233  1.00 59.81  ? 294 ASN B CB  1 
ATOM   5860  C  CG  . ASN B  1 294 ? 19.155  43.634  57.950  1.00 70.83  ? 294 ASN B CG  1 
ATOM   5861  O  OD1 . ASN B  1 294 ? 19.674  44.491  58.688  1.00 75.97  ? 294 ASN B OD1 1 
ATOM   5862  N  ND2 . ASN B  1 294 ? 18.415  43.954  56.885  1.00 79.26  ? 294 ASN B ND2 1 
ATOM   5863  N  N   . HIS B  1 295 ? 19.992  39.157  57.509  1.00 58.71  ? 295 HIS B N   1 
ATOM   5864  C  CA  . HIS B  1 295 ? 20.174  37.803  57.977  1.00 56.86  ? 295 HIS B CA  1 
ATOM   5865  C  C   . HIS B  1 295 ? 21.496  37.248  57.470  1.00 54.10  ? 295 HIS B C   1 
ATOM   5866  O  O   . HIS B  1 295 ? 21.665  37.069  56.255  1.00 48.94  ? 295 HIS B O   1 
ATOM   5867  C  CB  . HIS B  1 295 ? 19.059  36.938  57.430  1.00 64.26  ? 295 HIS B CB  1 
ATOM   5868  C  CG  . HIS B  1 295 ? 19.002  35.578  58.050  1.00 71.33  ? 295 HIS B CG  1 
ATOM   5869  N  ND1 . HIS B  1 295 ? 18.647  34.452  57.334  1.00 72.92  ? 295 HIS B ND1 1 
ATOM   5870  C  CD2 . HIS B  1 295 ? 19.232  35.164  59.321  1.00 71.96  ? 295 HIS B CD2 1 
ATOM   5871  C  CE1 . HIS B  1 295 ? 18.649  33.404  58.140  1.00 75.11  ? 295 HIS B CE1 1 
ATOM   5872  N  NE2 . HIS B  1 295 ? 19.004  33.809  59.349  1.00 74.82  ? 295 HIS B NE2 1 
ATOM   5873  N  N   . HIS B  1 296 ? 22.389  36.897  58.399  1.00 50.76  ? 296 HIS B N   1 
ATOM   5874  C  CA  . HIS B  1 296 ? 23.692  36.353  58.031  1.00 49.52  ? 296 HIS B CA  1 
ATOM   5875  C  C   . HIS B  1 296 ? 24.545  37.388  57.356  1.00 49.15  ? 296 HIS B C   1 
ATOM   5876  O  O   . HIS B  1 296 ? 25.401  37.075  56.513  1.00 53.06  ? 296 HIS B O   1 
ATOM   5877  C  CB  . HIS B  1 296 ? 23.560  35.191  57.070  1.00 49.33  ? 296 HIS B CB  1 
ATOM   5878  C  CG  . HIS B  1 296 ? 22.879  34.015  57.658  1.00 51.23  ? 296 HIS B CG  1 
ATOM   5879  N  ND1 . HIS B  1 296 ? 23.149  33.560  58.929  1.00 49.43  ? 296 HIS B ND1 1 
ATOM   5880  C  CD2 . HIS B  1 296 ? 21.944  33.189  57.141  1.00 52.99  ? 296 HIS B CD2 1 
ATOM   5881  C  CE1 . HIS B  1 296 ? 22.412  32.490  59.168  1.00 57.18  ? 296 HIS B CE1 1 
ATOM   5882  N  NE2 . HIS B  1 296 ? 21.674  32.244  58.098  1.00 57.12  ? 296 HIS B NE2 1 
ATOM   5883  N  N   . PHE B  1 297 ? 24.320  38.628  57.726  1.00 49.05  ? 297 PHE B N   1 
ATOM   5884  C  CA  . PHE B  1 297 ? 25.085  39.699  57.137  1.00 48.52  ? 297 PHE B CA  1 
ATOM   5885  C  C   . PHE B  1 297 ? 26.544  39.577  57.638  1.00 48.12  ? 297 PHE B C   1 
ATOM   5886  O  O   . PHE B  1 297 ? 26.777  39.433  58.854  1.00 45.72  ? 297 PHE B O   1 
ATOM   5887  C  CB  . PHE B  1 297 ? 24.439  41.055  57.518  1.00 43.91  ? 297 PHE B CB  1 
ATOM   5888  C  CG  . PHE B  1 297 ? 25.212  42.247  57.047  1.00 36.69  ? 297 PHE B CG  1 
ATOM   5889  C  CD1 . PHE B  1 297 ? 25.431  42.456  55.689  1.00 35.47  ? 297 PHE B CD1 1 
ATOM   5890  C  CD2 . PHE B  1 297 ? 25.798  43.110  57.961  1.00 34.55  ? 297 PHE B CD2 1 
ATOM   5891  C  CE1 . PHE B  1 297 ? 26.223  43.492  55.257  1.00 34.60  ? 297 PHE B CE1 1 
ATOM   5892  C  CE2 . PHE B  1 297 ? 26.603  44.154  57.534  1.00 32.17  ? 297 PHE B CE2 1 
ATOM   5893  C  CZ  . PHE B  1 297 ? 26.814  44.342  56.183  1.00 35.57  ? 297 PHE B CZ  1 
ATOM   5894  N  N   . MET B  1 298 ? 27.494  39.513  56.696  1.00 45.28  ? 298 MET B N   1 
ATOM   5895  C  CA  . MET B  1 298 ? 28.927  39.458  57.011  1.00 43.86  ? 298 MET B CA  1 
ATOM   5896  C  C   . MET B  1 298 ? 29.526  38.169  57.614  1.00 40.24  ? 298 MET B C   1 
ATOM   5897  O  O   . MET B  1 298 ? 30.601  38.181  58.241  1.00 39.49  ? 298 MET B O   1 
ATOM   5898  C  CB  . MET B  1 298 ? 29.341  40.666  57.882  1.00 43.20  ? 298 MET B CB  1 
ATOM   5899  C  CG  . MET B  1 298 ? 29.307  42.039  57.207  1.00 37.68  ? 298 MET B CG  1 
ATOM   5900  S  SD  . MET B  1 298 ? 30.318  43.282  58.076  1.00 40.35  ? 298 MET B SD  1 
ATOM   5901  C  CE  . MET B  1 298 ? 29.350  43.471  59.601  1.00 41.49  ? 298 MET B CE  1 
ATOM   5902  N  N   . GLU B  1 299 ? 28.847  37.057  57.421  1.00 33.42  ? 299 GLU B N   1 
ATOM   5903  C  CA  . GLU B  1 299 ? 29.376  35.808  57.894  1.00 33.27  ? 299 GLU B CA  1 
ATOM   5904  C  C   . GLU B  1 299 ? 30.434  35.351  56.904  1.00 38.06  ? 299 GLU B C   1 
ATOM   5905  O  O   . GLU B  1 299 ? 31.418  34.711  57.282  1.00 45.88  ? 299 GLU B O   1 
ATOM   5906  C  CB  . GLU B  1 299 ? 28.281  34.774  57.993  1.00 33.43  ? 299 GLU B CB  1 
ATOM   5907  C  CG  . GLU B  1 299 ? 27.410  35.008  59.211  1.00 36.84  ? 299 GLU B CG  1 
ATOM   5908  C  CD  . GLU B  1 299 ? 26.332  33.957  59.437  1.00 39.15  ? 299 GLU B CD  1 
ATOM   5909  O  OE1 . GLU B  1 299 ? 26.383  32.843  58.815  1.00 45.32  ? 299 GLU B OE1 1 
ATOM   5910  O  OE2 . GLU B  1 299 ? 25.443  34.275  60.273  1.00 34.09  ? 299 GLU B OE2 1 
ATOM   5911  N  N   . GLY B  1 300 ? 30.276  35.741  55.642  1.00 35.56  ? 300 GLY B N   1 
ATOM   5912  C  CA  . GLY B  1 300 ? 31.224  35.359  54.611  1.00 32.51  ? 300 GLY B CA  1 
ATOM   5913  C  C   . GLY B  1 300 ? 32.544  36.101  54.678  1.00 32.32  ? 300 GLY B C   1 
ATOM   5914  O  O   . GLY B  1 300 ? 33.467  35.842  53.917  1.00 32.28  ? 300 GLY B O   1 
ATOM   5915  N  N   . GLU B  1 301 ? 32.657  37.016  55.611  1.00 30.87  ? 301 GLU B N   1 
ATOM   5916  C  CA  . GLU B  1 301 ? 33.884  37.760  55.731  1.00 35.75  ? 301 GLU B CA  1 
ATOM   5917  C  C   . GLU B  1 301 ? 35.111  36.904  55.862  1.00 36.98  ? 301 GLU B C   1 
ATOM   5918  O  O   . GLU B  1 301 ? 35.998  36.974  55.023  1.00 39.76  ? 301 GLU B O   1 
ATOM   5919  C  CB  . GLU B  1 301 ? 33.811  38.723  56.895  1.00 43.04  ? 301 GLU B CB  1 
ATOM   5920  C  CG  . GLU B  1 301 ? 32.854  39.869  56.615  1.00 50.63  ? 301 GLU B CG  1 
ATOM   5921  C  CD  . GLU B  1 301 ? 33.268  40.675  55.402  1.00 49.65  ? 301 GLU B CD  1 
ATOM   5922  O  OE1 . GLU B  1 301 ? 34.197  41.528  55.581  1.00 47.77  ? 301 GLU B OE1 1 
ATOM   5923  O  OE2 . GLU B  1 301 ? 32.675  40.419  54.308  1.00 51.06  ? 301 GLU B OE2 1 
ATOM   5924  N  N   . ALA B  1 302 ? 35.157  36.061  56.885  1.00 38.48  ? 302 ALA B N   1 
ATOM   5925  C  CA  . ALA B  1 302 ? 36.332  35.214  57.073  1.00 37.87  ? 302 ALA B CA  1 
ATOM   5926  C  C   . ALA B  1 302 ? 36.811  34.534  55.776  1.00 36.24  ? 302 ALA B C   1 
ATOM   5927  O  O   . ALA B  1 302 ? 37.905  34.813  55.272  1.00 30.28  ? 302 ALA B O   1 
ATOM   5928  C  CB  . ALA B  1 302 ? 36.072  34.207  58.131  1.00 37.18  ? 302 ALA B CB  1 
ATOM   5929  N  N   . MET B  1 303 ? 35.943  33.738  55.169  1.00 32.95  ? 303 MET B N   1 
ATOM   5930  C  CA  . MET B  1 303 ? 36.330  33.050  53.951  1.00 28.73  ? 303 MET B CA  1 
ATOM   5931  C  C   . MET B  1 303 ? 36.677  34.035  52.892  1.00 29.90  ? 303 MET B C   1 
ATOM   5932  O  O   . MET B  1 303 ? 37.542  33.764  52.068  1.00 32.98  ? 303 MET B O   1 
ATOM   5933  C  CB  . MET B  1 303 ? 35.253  32.112  53.416  1.00 20.90  ? 303 MET B CB  1 
ATOM   5934  C  CG  . MET B  1 303 ? 35.727  31.359  52.196  1.00 17.92  ? 303 MET B CG  1 
ATOM   5935  S  SD  . MET B  1 303 ? 35.006  29.727  51.947  1.00 29.33  ? 303 MET B SD  1 
ATOM   5936  C  CE  . MET B  1 303 ? 33.453  30.245  51.443  1.00 32.36  ? 303 MET B CE  1 
ATOM   5937  N  N   . ARG B  1 304 ? 36.040  35.198  52.922  1.00 30.85  ? 304 ARG B N   1 
ATOM   5938  C  CA  . ARG B  1 304 ? 36.302  36.198  51.898  1.00 31.15  ? 304 ARG B CA  1 
ATOM   5939  C  C   . ARG B  1 304 ? 37.724  36.653  51.966  1.00 30.21  ? 304 ARG B C   1 
ATOM   5940  O  O   . ARG B  1 304 ? 38.438  36.677  50.938  1.00 29.58  ? 304 ARG B O   1 
ATOM   5941  C  CB  . ARG B  1 304 ? 35.398  37.426  52.033  1.00 29.18  ? 304 ARG B CB  1 
ATOM   5942  C  CG  . ARG B  1 304 ? 35.256  38.152  50.695  1.00 34.65  ? 304 ARG B CG  1 
ATOM   5943  C  CD  . ARG B  1 304 ? 34.715  39.564  50.803  1.00 34.59  ? 304 ARG B CD  1 
ATOM   5944  N  NE  . ARG B  1 304 ? 35.791  40.489  51.112  1.00 31.56  ? 304 ARG B NE  1 
ATOM   5945  C  CZ  . ARG B  1 304 ? 35.793  41.248  52.196  1.00 34.20  ? 304 ARG B CZ  1 
ATOM   5946  N  NH1 . ARG B  1 304 ? 34.765  41.193  53.026  1.00 29.97  ? 304 ARG B NH1 1 
ATOM   5947  N  NH2 . ARG B  1 304 ? 36.833  42.031  52.463  1.00 35.07  ? 304 ARG B NH2 1 
ATOM   5948  N  N   . THR B  1 305 ? 38.156  36.935  53.195  1.00 26.93  ? 305 THR B N   1 
ATOM   5949  C  CA  . THR B  1 305 ? 39.490  37.432  53.420  1.00 25.57  ? 305 THR B CA  1 
ATOM   5950  C  C   . THR B  1 305 ? 40.513  36.429  53.031  1.00 31.33  ? 305 THR B C   1 
ATOM   5951  O  O   . THR B  1 305 ? 41.691  36.724  53.002  1.00 41.77  ? 305 THR B O   1 
ATOM   5952  C  CB  . THR B  1 305 ? 39.760  37.782  54.883  1.00 24.66  ? 305 THR B CB  1 
ATOM   5953  O  OG1 . THR B  1 305 ? 40.073  36.595  55.650  1.00 26.69  ? 305 THR B OG1 1 
ATOM   5954  C  CG2 . THR B  1 305 ? 38.602  38.540  55.469  1.00 20.38  ? 305 THR B CG2 1 
ATOM   5955  N  N   . LYS B  1 306 ? 40.087  35.219  52.761  1.00 33.59  ? 306 LYS B N   1 
ATOM   5956  C  CA  . LYS B  1 306 ? 41.034  34.210  52.409  1.00 27.73  ? 306 LYS B CA  1 
ATOM   5957  C  C   . LYS B  1 306 ? 40.964  33.779  50.980  1.00 30.59  ? 306 LYS B C   1 
ATOM   5958  O  O   . LYS B  1 306 ? 41.989  33.510  50.403  1.00 35.92  ? 306 LYS B O   1 
ATOM   5959  C  CB  . LYS B  1 306 ? 40.860  33.022  53.339  1.00 31.63  ? 306 LYS B CB  1 
ATOM   5960  C  CG  . LYS B  1 306 ? 42.145  32.619  54.008  1.00 28.71  ? 306 LYS B CG  1 
ATOM   5961  C  CD  . LYS B  1 306 ? 41.995  32.568  55.509  1.00 35.05  ? 306 LYS B CD  1 
ATOM   5962  C  CE  . LYS B  1 306 ? 43.342  32.579  56.191  1.00 35.59  ? 306 LYS B CE  1 
ATOM   5963  N  NZ  . LYS B  1 306 ? 44.064  33.904  56.167  1.00 43.19  ? 306 LYS B NZ  1 
ATOM   5964  N  N   . PHE B  1 307 ? 39.800  33.791  50.354  1.00 29.63  ? 307 PHE B N   1 
ATOM   5965  C  CA  . PHE B  1 307 ? 39.783  33.323  48.993  1.00 30.40  ? 307 PHE B CA  1 
ATOM   5966  C  C   . PHE B  1 307 ? 39.489  34.347  47.912  1.00 32.05  ? 307 PHE B C   1 
ATOM   5967  O  O   . PHE B  1 307 ? 39.793  34.109  46.744  1.00 32.30  ? 307 PHE B O   1 
ATOM   5968  C  CB  . PHE B  1 307 ? 38.815  32.145  48.883  1.00 32.55  ? 307 PHE B CB  1 
ATOM   5969  C  CG  . PHE B  1 307 ? 39.266  30.912  49.653  1.00 38.10  ? 307 PHE B CG  1 
ATOM   5970  C  CD1 . PHE B  1 307 ? 40.624  30.678  49.913  1.00 32.36  ? 307 PHE B CD1 1 
ATOM   5971  C  CD2 . PHE B  1 307 ? 38.331  29.997  50.136  1.00 36.01  ? 307 PHE B CD2 1 
ATOM   5972  C  CE1 . PHE B  1 307 ? 41.034  29.567  50.643  1.00 30.22  ? 307 PHE B CE1 1 
ATOM   5973  C  CE2 . PHE B  1 307 ? 38.744  28.890  50.867  1.00 33.99  ? 307 PHE B CE2 1 
ATOM   5974  C  CZ  . PHE B  1 307 ? 40.107  28.683  51.120  1.00 31.29  ? 307 PHE B CZ  1 
ATOM   5975  N  N   . GLU B  1 308 ? 38.978  35.516  48.283  1.00 31.83  ? 308 GLU B N   1 
ATOM   5976  C  CA  . GLU B  1 308 ? 38.611  36.479  47.260  1.00 30.28  ? 308 GLU B CA  1 
ATOM   5977  C  C   . GLU B  1 308 ? 39.658  36.757  46.226  1.00 32.77  ? 308 GLU B C   1 
ATOM   5978  O  O   . GLU B  1 308 ? 39.413  36.626  45.021  1.00 33.10  ? 308 GLU B O   1 
ATOM   5979  C  CB  . GLU B  1 308 ? 38.119  37.786  47.823  1.00 31.03  ? 308 GLU B CB  1 
ATOM   5980  C  CG  . GLU B  1 308 ? 37.613  38.638  46.680  1.00 37.68  ? 308 GLU B CG  1 
ATOM   5981  C  CD  . GLU B  1 308 ? 36.733  39.806  47.081  1.00 44.80  ? 308 GLU B CD  1 
ATOM   5982  O  OE1 . GLU B  1 308 ? 36.880  40.294  48.240  1.00 40.76  ? 308 GLU B OE1 1 
ATOM   5983  O  OE2 . GLU B  1 308 ? 35.923  40.239  46.196  1.00 47.07  ? 308 GLU B OE2 1 
ATOM   5984  N  N   . ALA B  1 309 ? 40.840  37.132  46.669  1.00 32.97  ? 309 ALA B N   1 
ATOM   5985  C  CA  . ALA B  1 309 ? 41.886  37.408  45.694  1.00 30.20  ? 309 ALA B CA  1 
ATOM   5986  C  C   . ALA B  1 309 ? 42.123  36.285  44.687  1.00 32.72  ? 309 ALA B C   1 
ATOM   5987  O  O   . ALA B  1 309 ? 42.343  36.536  43.500  1.00 36.66  ? 309 ALA B O   1 
ATOM   5988  C  CB  . ALA B  1 309 ? 43.168  37.732  46.384  1.00 31.96  ? 309 ALA B CB  1 
ATOM   5989  N  N   . TRP B  1 310 ? 42.074  35.048  45.156  1.00 32.94  ? 310 TRP B N   1 
ATOM   5990  C  CA  . TRP B  1 310 ? 42.343  33.936  44.267  1.00 33.78  ? 310 TRP B CA  1 
ATOM   5991  C  C   . TRP B  1 310 ? 41.320  33.928  43.186  1.00 34.89  ? 310 TRP B C   1 
ATOM   5992  O  O   . TRP B  1 310 ? 41.654  33.751  42.024  1.00 37.34  ? 310 TRP B O   1 
ATOM   5993  C  CB  . TRP B  1 310 ? 42.308  32.603  45.017  1.00 38.94  ? 310 TRP B CB  1 
ATOM   5994  C  CG  . TRP B  1 310 ? 43.436  32.405  46.004  1.00 37.07  ? 310 TRP B CG  1 
ATOM   5995  C  CD1 . TRP B  1 310 ? 44.391  33.291  46.300  1.00 37.26  ? 310 TRP B CD1 1 
ATOM   5996  C  CD2 . TRP B  1 310 ? 43.655  31.275  46.863  1.00 41.19  ? 310 TRP B CD2 1 
ATOM   5997  N  NE1 . TRP B  1 310 ? 45.192  32.820  47.293  1.00 45.29  ? 310 TRP B NE1 1 
ATOM   5998  C  CE2 . TRP B  1 310 ? 44.762  31.579  47.665  1.00 43.92  ? 310 TRP B CE2 1 
ATOM   5999  C  CE3 . TRP B  1 310 ? 43.015  30.040  47.037  1.00 40.56  ? 310 TRP B CE3 1 
ATOM   6000  C  CZ2 . TRP B  1 310 ? 45.254  30.703  48.638  1.00 44.02  ? 310 TRP B CZ2 1 
ATOM   6001  C  CZ3 . TRP B  1 310 ? 43.502  29.167  48.000  1.00 43.03  ? 310 TRP B CZ3 1 
ATOM   6002  C  CH2 . TRP B  1 310 ? 44.613  29.504  48.791  1.00 42.97  ? 310 TRP B CH2 1 
ATOM   6003  N  N   . PHE B  1 311 ? 40.069  34.164  43.569  1.00 33.74  ? 311 PHE B N   1 
ATOM   6004  C  CA  . PHE B  1 311 ? 38.960  34.171  42.617  1.00 29.07  ? 311 PHE B CA  1 
ATOM   6005  C  C   . PHE B  1 311 ? 39.180  35.227  41.570  1.00 27.13  ? 311 PHE B C   1 
ATOM   6006  O  O   . PHE B  1 311 ? 39.016  34.981  40.384  1.00 28.20  ? 311 PHE B O   1 
ATOM   6007  C  CB  . PHE B  1 311 ? 37.630  34.433  43.330  1.00 28.30  ? 311 PHE B CB  1 
ATOM   6008  C  CG  . PHE B  1 311 ? 37.254  33.385  44.352  1.00 24.99  ? 311 PHE B CG  1 
ATOM   6009  C  CD1 . PHE B  1 311 ? 37.875  32.150  44.359  1.00 24.94  ? 311 PHE B CD1 1 
ATOM   6010  C  CD2 . PHE B  1 311 ? 36.266  33.640  45.284  1.00 23.91  ? 311 PHE B CD2 1 
ATOM   6011  C  CE1 . PHE B  1 311 ? 37.517  31.210  45.252  1.00 24.41  ? 311 PHE B CE1 1 
ATOM   6012  C  CE2 . PHE B  1 311 ? 35.899  32.701  46.186  1.00 23.42  ? 311 PHE B CE2 1 
ATOM   6013  C  CZ  . PHE B  1 311 ? 36.522  31.484  46.171  1.00 30.46  ? 311 PHE B CZ  1 
ATOM   6014  N  N   . VAL B  1 312 ? 39.549  36.418  42.018  1.00 25.08  ? 312 VAL B N   1 
ATOM   6015  C  CA  . VAL B  1 312 ? 39.782  37.504  41.093  1.00 24.10  ? 312 VAL B CA  1 
ATOM   6016  C  C   . VAL B  1 312 ? 40.974  37.165  40.235  1.00 26.67  ? 312 VAL B C   1 
ATOM   6017  O  O   . VAL B  1 312 ? 40.918  37.215  39.021  1.00 29.20  ? 312 VAL B O   1 
ATOM   6018  C  CB  . VAL B  1 312 ? 40.088  38.784  41.808  1.00 25.06  ? 312 VAL B CB  1 
ATOM   6019  C  CG1 . VAL B  1 312 ? 40.395  39.831  40.824  1.00 27.53  ? 312 VAL B CG1 1 
ATOM   6020  C  CG2 . VAL B  1 312 ? 38.905  39.219  42.629  1.00 31.82  ? 312 VAL B CG2 1 
ATOM   6021  N  N   . LYS B  1 313 ? 42.053  36.767  40.879  1.00 28.61  ? 313 LYS B N   1 
ATOM   6022  C  CA  . LYS B  1 313 ? 43.267  36.397  40.172  1.00 27.14  ? 313 LYS B CA  1 
ATOM   6023  C  C   . LYS B  1 313 ? 43.031  35.355  39.094  1.00 27.35  ? 313 LYS B C   1 
ATOM   6024  O  O   . LYS B  1 313 ? 43.700  35.379  38.079  1.00 30.45  ? 313 LYS B O   1 
ATOM   6025  C  CB  . LYS B  1 313 ? 44.292  35.896  41.158  1.00 29.41  ? 313 LYS B CB  1 
ATOM   6026  C  CG  . LYS B  1 313 ? 45.455  35.250  40.531  1.00 36.27  ? 313 LYS B CG  1 
ATOM   6027  C  CD  . LYS B  1 313 ? 46.435  34.888  41.631  1.00 55.50  ? 313 LYS B CD  1 
ATOM   6028  C  CE  . LYS B  1 313 ? 47.594  34.058  41.102  1.00 64.19  ? 313 LYS B CE  1 
ATOM   6029  N  NZ  . LYS B  1 313 ? 48.239  34.725  39.910  1.00 78.07  ? 313 LYS B NZ  1 
ATOM   6030  N  N   . TYR B  1 314 ? 42.109  34.419  39.303  1.00 27.10  ? 314 TYR B N   1 
ATOM   6031  C  CA  . TYR B  1 314 ? 41.853  33.391  38.294  1.00 28.97  ? 314 TYR B CA  1 
ATOM   6032  C  C   . TYR B  1 314 ? 40.621  33.673  37.450  1.00 33.55  ? 314 TYR B C   1 
ATOM   6033  O  O   . TYR B  1 314 ? 40.161  32.836  36.657  1.00 34.77  ? 314 TYR B O   1 
ATOM   6034  C  CB  . TYR B  1 314 ? 41.749  32.044  38.949  1.00 28.96  ? 314 TYR B CB  1 
ATOM   6035  C  CG  . TYR B  1 314 ? 43.066  31.542  39.422  1.00 31.15  ? 314 TYR B CG  1 
ATOM   6036  C  CD1 . TYR B  1 314 ? 43.545  31.871  40.685  1.00 32.23  ? 314 TYR B CD1 1 
ATOM   6037  C  CD2 . TYR B  1 314 ? 43.856  30.743  38.597  1.00 33.70  ? 314 TYR B CD2 1 
ATOM   6038  C  CE1 . TYR B  1 314 ? 44.793  31.412  41.117  1.00 34.46  ? 314 TYR B CE1 1 
ATOM   6039  C  CE2 . TYR B  1 314 ? 45.091  30.285  39.009  1.00 34.45  ? 314 TYR B CE2 1 
ATOM   6040  C  CZ  . TYR B  1 314 ? 45.557  30.621  40.265  1.00 34.18  ? 314 TYR B CZ  1 
ATOM   6041  O  OH  . TYR B  1 314 ? 46.785  30.148  40.651  1.00 39.83  ? 314 TYR B OH  1 
ATOM   6042  N  N   . LYS B  1 315 ? 40.042  34.838  37.696  1.00 33.86  ? 315 LYS B N   1 
ATOM   6043  C  CA  . LYS B  1 315 ? 38.914  35.266  36.926  1.00 32.31  ? 315 LYS B CA  1 
ATOM   6044  C  C   . LYS B  1 315 ? 37.806  34.258  36.984  1.00 29.26  ? 315 LYS B C   1 
ATOM   6045  O  O   . LYS B  1 315 ? 37.277  33.868  35.980  1.00 33.21  ? 315 LYS B O   1 
ATOM   6046  C  CB  . LYS B  1 315 ? 39.359  35.470  35.474  1.00 34.80  ? 315 LYS B CB  1 
ATOM   6047  C  CG  . LYS B  1 315 ? 40.377  36.604  35.301  1.00 46.31  ? 315 LYS B CG  1 
ATOM   6048  C  CD  . LYS B  1 315 ? 41.404  36.300  34.178  1.00 50.71  ? 315 LYS B CD  1 
ATOM   6049  C  CE  . LYS B  1 315 ? 41.321  37.278  32.979  1.00 53.59  ? 315 LYS B CE  1 
ATOM   6050  N  NZ  . LYS B  1 315 ? 41.542  38.714  33.330  1.00 57.90  ? 315 LYS B NZ  1 
ATOM   6051  N  N   . VAL B  1 316 ? 37.410  33.832  38.155  1.00 28.84  ? 316 VAL B N   1 
ATOM   6052  C  CA  . VAL B  1 316 ? 36.302  32.885  38.153  1.00 38.83  ? 316 VAL B CA  1 
ATOM   6053  C  C   . VAL B  1 316 ? 35.043  33.653  37.698  1.00 33.09  ? 316 VAL B C   1 
ATOM   6054  O  O   . VAL B  1 316 ? 34.862  34.791  38.062  1.00 33.94  ? 316 VAL B O   1 
ATOM   6055  C  CB  . VAL B  1 316 ? 36.090  32.181  39.544  1.00 41.55  ? 316 VAL B CB  1 
ATOM   6056  C  CG1 . VAL B  1 316 ? 37.319  32.313  40.386  1.00 47.24  ? 316 VAL B CG1 1 
ATOM   6057  C  CG2 . VAL B  1 316 ? 34.920  32.739  40.273  1.00 41.52  ? 316 VAL B CG2 1 
ATOM   6058  N  N   . ASP B  1 317 ? 34.208  33.033  36.887  1.00 30.68  ? 317 ASP B N   1 
ATOM   6059  C  CA  . ASP B  1 317 ? 33.006  33.655  36.384  1.00 27.50  ? 317 ASP B CA  1 
ATOM   6060  C  C   . ASP B  1 317 ? 31.902  33.961  37.354  1.00 31.09  ? 317 ASP B C   1 
ATOM   6061  O  O   . ASP B  1 317 ? 31.424  35.082  37.383  1.00 34.49  ? 317 ASP B O   1 
ATOM   6062  C  CB  . ASP B  1 317 ? 32.440  32.797  35.288  1.00 31.96  ? 317 ASP B CB  1 
ATOM   6063  C  CG  . ASP B  1 317 ? 33.264  32.864  34.051  1.00 42.10  ? 317 ASP B CG  1 
ATOM   6064  O  OD1 . ASP B  1 317 ? 33.096  33.886  33.337  1.00 50.81  ? 317 ASP B OD1 1 
ATOM   6065  O  OD2 . ASP B  1 317 ? 34.075  31.938  33.797  1.00 40.64  ? 317 ASP B OD2 1 
ATOM   6066  N  N   . VAL B  1 318 ? 31.408  32.945  38.062  1.00 35.28  ? 318 VAL B N   1 
ATOM   6067  C  CA  . VAL B  1 318 ? 30.316  33.104  39.046  1.00 32.33  ? 318 VAL B CA  1 
ATOM   6068  C  C   . VAL B  1 318 ? 30.626  32.373  40.352  1.00 34.16  ? 318 VAL B C   1 
ATOM   6069  O  O   . VAL B  1 318 ? 31.365  31.386  40.357  1.00 34.85  ? 318 VAL B O   1 
ATOM   6070  C  CB  . VAL B  1 318 ? 29.036  32.410  38.606  1.00 33.98  ? 318 VAL B CB  1 
ATOM   6071  C  CG1 . VAL B  1 318 ? 27.871  33.308  38.817  1.00 36.50  ? 318 VAL B CG1 1 
ATOM   6072  C  CG2 . VAL B  1 318 ? 29.156  31.816  37.221  1.00 32.26  ? 318 VAL B CG2 1 
ATOM   6073  N  N   . VAL B  1 319 ? 29.983  32.786  41.434  1.00 33.18  ? 319 VAL B N   1 
ATOM   6074  C  CA  . VAL B  1 319 ? 30.146  32.097  42.717  1.00 37.33  ? 319 VAL B CA  1 
ATOM   6075  C  C   . VAL B  1 319 ? 28.747  31.979  43.305  1.00 36.99  ? 319 VAL B C   1 
ATOM   6076  O  O   . VAL B  1 319 ? 28.199  32.956  43.749  1.00 37.94  ? 319 VAL B O   1 
ATOM   6077  C  CB  . VAL B  1 319 ? 31.023  32.875  43.692  1.00 37.15  ? 319 VAL B CB  1 
ATOM   6078  C  CG1 . VAL B  1 319 ? 30.936  32.270  45.084  1.00 35.32  ? 319 VAL B CG1 1 
ATOM   6079  C  CG2 . VAL B  1 319 ? 32.422  32.871  43.206  1.00 36.30  ? 319 VAL B CG2 1 
ATOM   6080  N  N   . PHE B  1 320 ? 28.135  30.808  43.238  1.00 36.84  ? 320 PHE B N   1 
ATOM   6081  C  CA  . PHE B  1 320 ? 26.782  30.612  43.769  1.00 33.93  ? 320 PHE B CA  1 
ATOM   6082  C  C   . PHE B  1 320 ? 26.797  30.254  45.241  1.00 31.71  ? 320 PHE B C   1 
ATOM   6083  O  O   . PHE B  1 320 ? 27.656  29.531  45.668  1.00 36.63  ? 320 PHE B O   1 
ATOM   6084  C  CB  . PHE B  1 320 ? 26.099  29.517  42.972  1.00 28.87  ? 320 PHE B CB  1 
ATOM   6085  C  CG  . PHE B  1 320 ? 25.981  29.840  41.517  1.00 34.11  ? 320 PHE B CG  1 
ATOM   6086  C  CD1 . PHE B  1 320 ? 25.030  30.787  41.074  1.00 32.54  ? 320 PHE B CD1 1 
ATOM   6087  C  CD2 . PHE B  1 320 ? 26.772  29.197  40.577  1.00 29.27  ? 320 PHE B CD2 1 
ATOM   6088  C  CE1 . PHE B  1 320 ? 24.870  31.081  39.713  1.00 24.05  ? 320 PHE B CE1 1 
ATOM   6089  C  CE2 . PHE B  1 320 ? 26.619  29.489  39.196  1.00 32.65  ? 320 PHE B CE2 1 
ATOM   6090  C  CZ  . PHE B  1 320 ? 25.662  30.433  38.768  1.00 29.13  ? 320 PHE B CZ  1 
ATOM   6091  N  N   . ALA B  1 321 ? 25.872  30.773  46.025  1.00 29.23  ? 321 ALA B N   1 
ATOM   6092  C  CA  . ALA B  1 321 ? 25.828  30.458  47.446  1.00 27.29  ? 321 ALA B CA  1 
ATOM   6093  C  C   . ALA B  1 321 ? 24.382  30.420  47.820  1.00 26.86  ? 321 ALA B C   1 
ATOM   6094  O  O   . ALA B  1 321 ? 23.518  30.690  47.013  1.00 30.64  ? 321 ALA B O   1 
ATOM   6095  C  CB  . ALA B  1 321 ? 26.515  31.524  48.270  1.00 23.00  ? 321 ALA B CB  1 
ATOM   6096  N  N   . GLY B  1 322 ? 24.110  30.038  49.039  1.00 28.49  ? 322 GLY B N   1 
ATOM   6097  C  CA  . GLY B  1 322 ? 22.738  29.964  49.510  1.00 27.89  ? 322 GLY B CA  1 
ATOM   6098  C  C   . GLY B  1 322 ? 22.799  30.620  50.864  1.00 26.58  ? 322 GLY B C   1 
ATOM   6099  O  O   . GLY B  1 322 ? 23.367  31.692  50.980  1.00 27.60  ? 322 GLY B O   1 
ATOM   6100  N  N   . HIS B  1 323 ? 22.230  29.995  51.884  1.00 26.85  ? 323 HIS B N   1 
ATOM   6101  C  CA  . HIS B  1 323 ? 22.279  30.493  53.262  1.00 32.18  ? 323 HIS B CA  1 
ATOM   6102  C  C   . HIS B  1 323 ? 21.347  31.651  53.575  1.00 34.99  ? 323 HIS B C   1 
ATOM   6103  O  O   . HIS B  1 323 ? 20.766  31.715  54.652  1.00 41.38  ? 323 HIS B O   1 
ATOM   6104  C  CB  . HIS B  1 323 ? 23.741  30.761  53.673  1.00 33.49  ? 323 HIS B CB  1 
ATOM   6105  C  CG  . HIS B  1 323 ? 23.993  30.695  55.154  1.00 33.87  ? 323 HIS B CG  1 
ATOM   6106  N  ND1 . HIS B  1 323 ? 23.568  29.657  55.962  1.00 32.49  ? 323 HIS B ND1 1 
ATOM   6107  C  CD2 . HIS B  1 323 ? 24.618  31.577  55.974  1.00 36.54  ? 323 HIS B CD2 1 
ATOM   6108  C  CE1 . HIS B  1 323 ? 23.913  29.908  57.211  1.00 33.80  ? 323 HIS B CE1 1 
ATOM   6109  N  NE2 . HIS B  1 323 ? 24.551  31.065  57.249  1.00 34.15  ? 323 HIS B NE2 1 
ATOM   6110  N  N   . VAL B  1 324 ? 21.224  32.620  52.685  1.00 40.03  ? 324 VAL B N   1 
ATOM   6111  C  CA  . VAL B  1 324 ? 20.272  33.686  52.937  1.00 38.52  ? 324 VAL B CA  1 
ATOM   6112  C  C   . VAL B  1 324 ? 19.051  33.271  52.120  1.00 43.41  ? 324 VAL B C   1 
ATOM   6113  O  O   . VAL B  1 324 ? 19.165  32.967  50.927  1.00 45.75  ? 324 VAL B O   1 
ATOM   6114  C  CB  . VAL B  1 324 ? 20.821  35.004  52.517  1.00 35.59  ? 324 VAL B CB  1 
ATOM   6115  C  CG1 . VAL B  1 324 ? 19.775  36.037  52.702  1.00 41.83  ? 324 VAL B CG1 1 
ATOM   6116  C  CG2 . VAL B  1 324 ? 22.007  35.351  53.397  1.00 33.01  ? 324 VAL B CG2 1 
ATOM   6117  N  N   . HIS B  1 325 ? 17.926  33.086  52.790  1.00 46.35  ? 325 HIS B N   1 
ATOM   6118  C  CA  . HIS B  1 325 ? 16.725  32.650  52.110  1.00 48.00  ? 325 HIS B CA  1 
ATOM   6119  C  C   . HIS B  1 325 ? 16.078  33.781  51.332  1.00 47.91  ? 325 HIS B C   1 
ATOM   6120  O  O   . HIS B  1 325 ? 15.076  34.334  51.760  1.00 47.10  ? 325 HIS B O   1 
ATOM   6121  C  CB  . HIS B  1 325 ? 15.762  32.046  53.123  1.00 52.02  ? 325 HIS B CB  1 
ATOM   6122  C  CG  . HIS B  1 325 ? 16.378  30.988  53.982  1.00 48.42  ? 325 HIS B CG  1 
ATOM   6123  N  ND1 . HIS B  1 325 ? 15.976  30.760  55.277  1.00 51.13  ? 325 HIS B ND1 1 
ATOM   6124  C  CD2 . HIS B  1 325 ? 17.387  30.122  53.741  1.00 48.66  ? 325 HIS B CD2 1 
ATOM   6125  C  CE1 . HIS B  1 325 ? 16.722  29.802  55.802  1.00 55.00  ? 325 HIS B CE1 1 
ATOM   6126  N  NE2 . HIS B  1 325 ? 17.588  29.397  54.888  1.00 47.50  ? 325 HIS B NE2 1 
ATOM   6127  N  N   . ALA B  1 326 ? 16.673  34.103  50.181  1.00 48.46  ? 326 ALA B N   1 
ATOM   6128  C  CA  . ALA B  1 326 ? 16.251  35.178  49.274  1.00 44.02  ? 326 ALA B CA  1 
ATOM   6129  C  C   . ALA B  1 326 ? 17.173  35.137  48.063  1.00 42.77  ? 326 ALA B C   1 
ATOM   6130  O  O   . ALA B  1 326 ? 18.029  34.268  47.980  1.00 45.25  ? 326 ALA B O   1 
ATOM   6131  C  CB  . ALA B  1 326 ? 16.364  36.520  49.965  1.00 39.10  ? 326 ALA B CB  1 
ATOM   6132  N  N   . TYR B  1 327 ? 17.034  36.087  47.147  1.00 39.87  ? 327 TYR B N   1 
ATOM   6133  C  CA  . TYR B  1 327 ? 17.848  36.123  45.951  1.00 35.36  ? 327 TYR B CA  1 
ATOM   6134  C  C   . TYR B  1 327 ? 18.597  37.413  45.941  1.00 36.61  ? 327 TYR B C   1 
ATOM   6135  O  O   . TYR B  1 327 ? 18.143  38.380  46.536  1.00 39.04  ? 327 TYR B O   1 
ATOM   6136  C  CB  . TYR B  1 327 ? 16.959  36.069  44.733  1.00 37.79  ? 327 TYR B CB  1 
ATOM   6137  C  CG  . TYR B  1 327 ? 17.679  36.273  43.431  1.00 43.11  ? 327 TYR B CG  1 
ATOM   6138  C  CD1 . TYR B  1 327 ? 18.614  35.358  42.956  1.00 48.31  ? 327 TYR B CD1 1 
ATOM   6139  C  CD2 . TYR B  1 327 ? 17.370  37.331  42.630  1.00 45.64  ? 327 TYR B CD2 1 
ATOM   6140  C  CE1 . TYR B  1 327 ? 19.214  35.503  41.684  1.00 46.29  ? 327 TYR B CE1 1 
ATOM   6141  C  CE2 . TYR B  1 327 ? 17.958  37.486  41.369  1.00 48.16  ? 327 TYR B CE2 1 
ATOM   6142  C  CZ  . TYR B  1 327 ? 18.876  36.572  40.899  1.00 45.71  ? 327 TYR B CZ  1 
ATOM   6143  O  OH  . TYR B  1 327 ? 19.435  36.749  39.646  1.00 42.55  ? 327 TYR B OH  1 
ATOM   6144  N  N   . GLU B  1 328 ? 19.756  37.419  45.288  1.00 32.79  ? 328 GLU B N   1 
ATOM   6145  C  CA  . GLU B  1 328 ? 20.601  38.609  45.176  1.00 29.79  ? 328 GLU B CA  1 
ATOM   6146  C  C   . GLU B  1 328 ? 21.656  38.335  44.149  1.00 32.31  ? 328 GLU B C   1 
ATOM   6147  O  O   . GLU B  1 328 ? 22.064  37.204  43.985  1.00 33.59  ? 328 GLU B O   1 
ATOM   6148  C  CB  . GLU B  1 328 ? 21.229  39.004  46.500  1.00 28.43  ? 328 GLU B CB  1 
ATOM   6149  C  CG  . GLU B  1 328 ? 22.342  40.007  46.360  1.00 30.98  ? 328 GLU B CG  1 
ATOM   6150  C  CD  . GLU B  1 328 ? 22.558  40.861  47.627  1.00 41.35  ? 328 GLU B CD  1 
ATOM   6151  O  OE1 . GLU B  1 328 ? 22.346  40.384  48.786  1.00 40.04  ? 328 GLU B OE1 1 
ATOM   6152  O  OE2 . GLU B  1 328 ? 22.957  42.037  47.450  1.00 41.86  ? 328 GLU B OE2 1 
ATOM   6153  N  N   . ARG B  1 329 ? 22.004  39.352  43.374  1.00 38.01  ? 329 ARG B N   1 
ATOM   6154  C  CA  . ARG B  1 329 ? 22.980  39.237  42.296  1.00 44.13  ? 329 ARG B CA  1 
ATOM   6155  C  C   . ARG B  1 329 ? 23.901  40.425  42.437  1.00 48.03  ? 329 ARG B C   1 
ATOM   6156  O  O   . ARG B  1 329 ? 23.455  41.490  42.800  1.00 52.55  ? 329 ARG B O   1 
ATOM   6157  C  CB  . ARG B  1 329 ? 22.290  39.308  40.936  1.00 43.01  ? 329 ARG B CB  1 
ATOM   6158  C  CG  . ARG B  1 329 ? 23.199  38.873  39.802  1.00 51.72  ? 329 ARG B CG  1 
ATOM   6159  C  CD  . ARG B  1 329 ? 22.494  38.874  38.475  1.00 53.83  ? 329 ARG B CD  1 
ATOM   6160  N  NE  . ARG B  1 329 ? 22.435  40.226  37.932  1.00 62.81  ? 329 ARG B NE  1 
ATOM   6161  C  CZ  . ARG B  1 329 ? 21.323  40.942  37.785  1.00 59.30  ? 329 ARG B CZ  1 
ATOM   6162  N  NH1 . ARG B  1 329 ? 20.154  40.458  38.143  1.00 54.52  ? 329 ARG B NH1 1 
ATOM   6163  N  NH2 . ARG B  1 329 ? 21.389  42.153  37.266  1.00 66.72  ? 329 ARG B NH2 1 
ATOM   6164  N  N   . SER B  1 330 ? 25.178  40.277  42.135  1.00 52.97  ? 330 SER B N   1 
ATOM   6165  C  CA  . SER B  1 330 ? 26.083  41.397  42.305  1.00 55.77  ? 330 SER B CA  1 
ATOM   6166  C  C   . SER B  1 330 ? 26.722  41.909  41.063  1.00 57.32  ? 330 SER B C   1 
ATOM   6167  O  O   . SER B  1 330 ? 26.373  41.493  39.945  1.00 62.83  ? 330 SER B O   1 
ATOM   6168  C  CB  . SER B  1 330 ? 27.152  41.068  43.333  1.00 55.10  ? 330 SER B CB  1 
ATOM   6169  O  OG  . SER B  1 330 ? 26.511  41.091  44.601  1.00 57.77  ? 330 SER B OG  1 
ATOM   6170  N  N   . GLU B  1 331 ? 27.544  42.927  41.273  1.00 53.37  ? 331 GLU B N   1 
ATOM   6171  C  CA  . GLU B  1 331 ? 28.285  43.550  40.212  1.00 52.03  ? 331 GLU B CA  1 
ATOM   6172  C  C   . GLU B  1 331 ? 29.630  42.884  40.280  1.00 49.39  ? 331 GLU B C   1 
ATOM   6173  O  O   . GLU B  1 331 ? 29.978  42.379  41.339  1.00 53.22  ? 331 GLU B O   1 
ATOM   6174  C  CB  . GLU B  1 331 ? 28.450  45.034  40.508  1.00 56.25  ? 331 GLU B CB  1 
ATOM   6175  C  CG  . GLU B  1 331 ? 27.182  45.861  40.402  1.00 62.16  ? 331 GLU B CG  1 
ATOM   6176  C  CD  . GLU B  1 331 ? 26.607  45.932  38.975  1.00 69.75  ? 331 GLU B CD  1 
ATOM   6177  O  OE1 . GLU B  1 331 ? 27.055  45.171  38.076  1.00 74.59  ? 331 GLU B OE1 1 
ATOM   6178  O  OE2 . GLU B  1 331 ? 25.686  46.754  38.755  1.00 70.68  ? 331 GLU B OE2 1 
ATOM   6179  N  N   . ARG B  1 332 ? 30.347  42.789  39.161  1.00 43.70  ? 332 ARG B N   1 
ATOM   6180  C  CA  . ARG B  1 332 ? 31.660  42.205  39.210  1.00 37.49  ? 332 ARG B CA  1 
ATOM   6181  C  C   . ARG B  1 332 ? 32.373  43.218  40.075  1.00 42.23  ? 332 ARG B C   1 
ATOM   6182  O  O   . ARG B  1 332 ? 32.565  44.349  39.691  1.00 44.91  ? 332 ARG B O   1 
ATOM   6183  C  CB  . ARG B  1 332 ? 32.245  42.102  37.836  1.00 29.77  ? 332 ARG B CB  1 
ATOM   6184  C  CG  . ARG B  1 332 ? 31.512  41.075  37.046  1.00 30.64  ? 332 ARG B CG  1 
ATOM   6185  C  CD  . ARG B  1 332 ? 32.243  40.734  35.796  1.00 28.91  ? 332 ARG B CD  1 
ATOM   6186  N  NE  . ARG B  1 332 ? 31.571  39.667  35.068  1.00 37.36  ? 332 ARG B NE  1 
ATOM   6187  C  CZ  . ARG B  1 332 ? 31.729  38.368  35.338  1.00 42.57  ? 332 ARG B CZ  1 
ATOM   6188  N  NH1 . ARG B  1 332 ? 32.530  37.999  36.333  1.00 42.83  ? 332 ARG B NH1 1 
ATOM   6189  N  NH2 . ARG B  1 332 ? 31.187  37.427  34.555  1.00 41.26  ? 332 ARG B NH2 1 
ATOM   6190  N  N   . VAL B  1 333 ? 32.702  42.794  41.282  1.00 43.33  ? 333 VAL B N   1 
ATOM   6191  C  CA  . VAL B  1 333 ? 33.288  43.625  42.284  1.00 39.41  ? 333 VAL B CA  1 
ATOM   6192  C  C   . VAL B  1 333 ? 34.367  42.886  43.067  1.00 38.40  ? 333 VAL B C   1 
ATOM   6193  O  O   . VAL B  1 333 ? 34.297  41.685  43.308  1.00 37.40  ? 333 VAL B O   1 
ATOM   6194  C  CB  . VAL B  1 333 ? 32.155  43.966  43.230  1.00 42.34  ? 333 VAL B CB  1 
ATOM   6195  C  CG1 . VAL B  1 333 ? 32.654  44.459  44.522  1.00 46.85  ? 333 VAL B CG1 1 
ATOM   6196  C  CG2 . VAL B  1 333 ? 31.273  44.971  42.606  1.00 42.81  ? 333 VAL B CG2 1 
ATOM   6197  N  N   . SER B  1 334 ? 35.343  43.638  43.532  1.00 37.16  ? 334 SER B N   1 
ATOM   6198  C  CA  . SER B  1 334 ? 36.412  43.076  44.315  1.00 35.58  ? 334 SER B CA  1 
ATOM   6199  C  C   . SER B  1 334 ? 36.562  44.004  45.514  1.00 35.86  ? 334 SER B C   1 
ATOM   6200  O  O   . SER B  1 334 ? 36.035  45.093  45.497  1.00 41.14  ? 334 SER B O   1 
ATOM   6201  C  CB  . SER B  1 334 ? 37.693  43.109  43.496  1.00 33.62  ? 334 SER B CB  1 
ATOM   6202  O  OG  . SER B  1 334 ? 38.473  44.252  43.831  1.00 37.28  ? 334 SER B OG  1 
ATOM   6203  N  N   . ASN B  1 335 ? 37.246  43.575  46.562  1.00 33.82  ? 335 ASN B N   1 
ATOM   6204  C  CA  . ASN B  1 335 ? 37.494  44.413  47.725  1.00 31.97  ? 335 ASN B CA  1 
ATOM   6205  C  C   . ASN B  1 335 ? 38.779  43.868  48.280  1.00 33.64  ? 335 ASN B C   1 
ATOM   6206  O  O   . ASN B  1 335 ? 38.886  43.512  49.440  1.00 41.71  ? 335 ASN B O   1 
ATOM   6207  C  CB  . ASN B  1 335 ? 36.404  44.262  48.766  1.00 33.87  ? 335 ASN B CB  1 
ATOM   6208  C  CG  . ASN B  1 335 ? 36.657  45.132  50.008  1.00 39.34  ? 335 ASN B CG  1 
ATOM   6209  O  OD1 . ASN B  1 335 ? 37.681  45.851  50.086  1.00 44.23  ? 335 ASN B OD1 1 
ATOM   6210  N  ND2 . ASN B  1 335 ? 35.723  45.088  50.972  1.00 31.73  ? 335 ASN B ND2 1 
ATOM   6211  N  N   . ILE B  1 336 ? 39.787  43.830  47.438  1.00 32.77  ? 336 ILE B N   1 
ATOM   6212  C  CA  . ILE B  1 336 ? 41.025  43.222  47.838  1.00 30.26  ? 336 ILE B CA  1 
ATOM   6213  C  C   . ILE B  1 336 ? 42.223  44.136  48.014  1.00 37.84  ? 336 ILE B C   1 
ATOM   6214  O  O   . ILE B  1 336 ? 43.361  43.720  47.744  1.00 41.77  ? 336 ILE B O   1 
ATOM   6215  C  CB  . ILE B  1 336 ? 41.374  42.123  46.815  1.00 25.85  ? 336 ILE B CB  1 
ATOM   6216  C  CG1 . ILE B  1 336 ? 41.613  42.736  45.447  1.00 19.31  ? 336 ILE B CG1 1 
ATOM   6217  C  CG2 . ILE B  1 336 ? 40.225  41.125  46.707  1.00 27.48  ? 336 ILE B CG2 1 
ATOM   6218  C  CD1 . ILE B  1 336 ? 41.734  41.735  44.359  1.00 20.98  ? 336 ILE B CD1 1 
ATOM   6219  N  N   . ALA B  1 337 ? 42.013  45.340  48.538  1.00 41.19  ? 337 ALA B N   1 
ATOM   6220  C  CA  . ALA B  1 337 ? 43.143  46.259  48.689  1.00 38.39  ? 337 ALA B CA  1 
ATOM   6221  C  C   . ALA B  1 337 ? 43.482  46.676  50.100  1.00 37.08  ? 337 ALA B C   1 
ATOM   6222  O  O   . ALA B  1 337 ? 44.498  47.348  50.347  1.00 37.07  ? 337 ALA B O   1 
ATOM   6223  C  CB  . ALA B  1 337 ? 42.910  47.450  47.859  1.00 38.31  ? 337 ALA B CB  1 
ATOM   6224  N  N   . TYR B  1 338 ? 42.649  46.233  51.024  1.00 34.63  ? 338 TYR B N   1 
ATOM   6225  C  CA  . TYR B  1 338 ? 42.790  46.581  52.416  1.00 30.80  ? 338 TYR B CA  1 
ATOM   6226  C  C   . TYR B  1 338 ? 44.095  46.148  52.998  1.00 31.11  ? 338 TYR B C   1 
ATOM   6227  O  O   . TYR B  1 338 ? 44.601  45.090  52.671  1.00 35.64  ? 338 TYR B O   1 
ATOM   6228  C  CB  . TYR B  1 338 ? 41.659  45.969  53.184  1.00 27.53  ? 338 TYR B CB  1 
ATOM   6229  C  CG  . TYR B  1 338 ? 41.591  46.422  54.579  1.00 29.72  ? 338 TYR B CG  1 
ATOM   6230  C  CD1 . TYR B  1 338 ? 41.463  47.771  54.910  1.00 32.28  ? 338 TYR B CD1 1 
ATOM   6231  C  CD2 . TYR B  1 338 ? 41.597  45.500  55.592  1.00 33.28  ? 338 TYR B CD2 1 
ATOM   6232  C  CE1 . TYR B  1 338 ? 41.329  48.177  56.257  1.00 35.40  ? 338 TYR B CE1 1 
ATOM   6233  C  CE2 . TYR B  1 338 ? 41.466  45.880  56.928  1.00 38.03  ? 338 TYR B CE2 1 
ATOM   6234  C  CZ  . TYR B  1 338 ? 41.331  47.202  57.257  1.00 38.49  ? 338 TYR B CZ  1 
ATOM   6235  O  OH  . TYR B  1 338 ? 41.212  47.485  58.588  1.00 42.02  ? 338 TYR B OH  1 
ATOM   6236  N  N   . LYS B  1 339 ? 44.657  47.008  53.821  1.00 24.69  ? 339 LYS B N   1 
ATOM   6237  C  CA  . LYS B  1 339 ? 45.891  46.713  54.474  1.00 24.98  ? 339 LYS B CA  1 
ATOM   6238  C  C   . LYS B  1 339 ? 45.796  47.253  55.862  1.00 27.95  ? 339 LYS B C   1 
ATOM   6239  O  O   . LYS B  1 339 ? 46.752  47.799  56.372  1.00 30.59  ? 339 LYS B O   1 
ATOM   6240  C  CB  . LYS B  1 339 ? 47.054  47.378  53.796  1.00 28.52  ? 339 LYS B CB  1 
ATOM   6241  C  CG  . LYS B  1 339 ? 47.116  47.087  52.373  1.00 35.81  ? 339 LYS B CG  1 
ATOM   6242  C  CD  . LYS B  1 339 ? 47.408  45.670  52.150  1.00 45.25  ? 339 LYS B CD  1 
ATOM   6243  C  CE  . LYS B  1 339 ? 47.609  45.412  50.676  1.00 57.03  ? 339 LYS B CE  1 
ATOM   6244  N  NZ  . LYS B  1 339 ? 48.592  46.417  50.117  1.00 66.30  ? 339 LYS B NZ  1 
ATOM   6245  N  N   . ILE B  1 340 ? 44.612  47.163  56.447  1.00 31.50  ? 340 ILE B N   1 
ATOM   6246  C  CA  . ILE B  1 340 ? 44.362  47.587  57.820  1.00 31.16  ? 340 ILE B CA  1 
ATOM   6247  C  C   . ILE B  1 340 ? 44.296  49.074  57.989  1.00 33.70  ? 340 ILE B C   1 
ATOM   6248  O  O   . ILE B  1 340 ? 43.237  49.653  58.246  1.00 39.56  ? 340 ILE B O   1 
ATOM   6249  C  CB  . ILE B  1 340 ? 45.439  47.087  58.788  1.00 28.78  ? 340 ILE B CB  1 
ATOM   6250  C  CG1 . ILE B  1 340 ? 45.760  45.624  58.536  1.00 26.19  ? 340 ILE B CG1 1 
ATOM   6251  C  CG2 . ILE B  1 340 ? 44.961  47.284  60.203  1.00 34.03  ? 340 ILE B CG2 1 
ATOM   6252  C  CD1 . ILE B  1 340 ? 44.570  44.724  58.635  1.00 33.35  ? 340 ILE B CD1 1 
ATOM   6253  N  N   . THR B  1 341 ? 45.440  49.701  57.815  1.00 32.00  ? 341 THR B N   1 
ATOM   6254  C  CA  . THR B  1 341 ? 45.529  51.126  57.997  1.00 37.20  ? 341 THR B CA  1 
ATOM   6255  C  C   . THR B  1 341 ? 45.330  51.984  56.773  1.00 38.59  ? 341 THR B C   1 
ATOM   6256  O  O   . THR B  1 341 ? 45.061  53.166  56.899  1.00 46.82  ? 341 THR B O   1 
ATOM   6257  C  CB  . THR B  1 341 ? 46.868  51.491  58.603  1.00 36.53  ? 341 THR B CB  1 
ATOM   6258  O  OG1 . THR B  1 341 ? 47.925  50.991  57.764  1.00 42.01  ? 341 THR B OG1 1 
ATOM   6259  C  CG2 . THR B  1 341 ? 46.991  50.902  59.985  1.00 39.60  ? 341 THR B CG2 1 
ATOM   6260  N  N   . ASP B  1 342 ? 45.412  51.417  55.584  1.00 35.90  ? 342 ASP B N   1 
ATOM   6261  C  CA  . ASP B  1 342 ? 45.282  52.261  54.425  1.00 31.71  ? 342 ASP B CA  1 
ATOM   6262  C  C   . ASP B  1 342 ? 43.883  52.665  54.061  1.00 37.01  ? 342 ASP B C   1 
ATOM   6263  O  O   . ASP B  1 342 ? 43.663  53.244  53.000  1.00 39.95  ? 342 ASP B O   1 
ATOM   6264  C  CB  . ASP B  1 342 ? 45.985  51.666  53.226  1.00 32.56  ? 342 ASP B CB  1 
ATOM   6265  C  CG  . ASP B  1 342 ? 45.253  50.504  52.639  1.00 33.87  ? 342 ASP B CG  1 
ATOM   6266  O  OD1 . ASP B  1 342 ? 44.348  49.990  53.311  1.00 40.15  ? 342 ASP B OD1 1 
ATOM   6267  O  OD2 . ASP B  1 342 ? 45.589  50.094  51.501  1.00 30.69  ? 342 ASP B OD2 1 
ATOM   6268  N  N   . GLY B  1 343 ? 42.907  52.316  54.885  1.00 42.32  ? 343 GLY B N   1 
ATOM   6269  C  CA  . GLY B  1 343 ? 41.549  52.729  54.562  1.00 45.56  ? 343 GLY B CA  1 
ATOM   6270  C  C   . GLY B  1 343 ? 40.897  52.296  53.238  1.00 46.52  ? 343 GLY B C   1 
ATOM   6271  O  O   . GLY B  1 343 ? 39.785  52.724  52.918  1.00 54.10  ? 343 GLY B O   1 
ATOM   6272  N  N   . LEU B  1 344 ? 41.545  51.441  52.464  1.00 41.84  ? 344 LEU B N   1 
ATOM   6273  C  CA  . LEU B  1 344 ? 40.959  50.962  51.210  1.00 40.70  ? 344 LEU B CA  1 
ATOM   6274  C  C   . LEU B  1 344 ? 40.003  49.729  51.386  1.00 41.73  ? 344 LEU B C   1 
ATOM   6275  O  O   . LEU B  1 344 ? 40.209  48.590  50.839  1.00 36.43  ? 344 LEU B O   1 
ATOM   6276  C  CB  . LEU B  1 344 ? 42.090  50.617  50.269  1.00 44.53  ? 344 LEU B CB  1 
ATOM   6277  C  CG  . LEU B  1 344 ? 42.941  51.797  49.827  1.00 41.85  ? 344 LEU B CG  1 
ATOM   6278  C  CD1 . LEU B  1 344 ? 44.130  51.355  48.931  1.00 37.95  ? 344 LEU B CD1 1 
ATOM   6279  C  CD2 . LEU B  1 344 ? 42.012  52.716  49.089  1.00 45.74  ? 344 LEU B CD2 1 
ATOM   6280  N  N   . CYS B  1 345 ? 38.939  49.957  52.141  1.00 38.71  ? 345 CYS B N   1 
ATOM   6281  C  CA  . CYS B  1 345 ? 38.020  48.882  52.403  1.00 39.07  ? 345 CYS B CA  1 
ATOM   6282  C  C   . CYS B  1 345 ? 36.639  49.066  51.813  1.00 39.58  ? 345 CYS B C   1 
ATOM   6283  O  O   . CYS B  1 345 ? 35.637  48.972  52.525  1.00 41.95  ? 345 CYS B O   1 
ATOM   6284  C  CB  . CYS B  1 345 ? 37.918  48.709  53.893  1.00 37.89  ? 345 CYS B CB  1 
ATOM   6285  S  SG  . CYS B  1 345 ? 37.265  50.160  54.573  1.00 31.50  ? 345 CYS B SG  1 
ATOM   6286  N  N   . THR B  1 346 ? 36.567  49.310  50.516  1.00 37.07  ? 346 THR B N   1 
ATOM   6287  C  CA  . THR B  1 346 ? 35.270  49.484  49.915  1.00 35.49  ? 346 THR B CA  1 
ATOM   6288  C  C   . THR B  1 346 ? 35.257  48.812  48.586  1.00 34.00  ? 346 THR B C   1 
ATOM   6289  O  O   . THR B  1 346 ? 36.152  49.006  47.770  1.00 38.89  ? 346 THR B O   1 
ATOM   6290  C  CB  . THR B  1 346 ? 34.889  50.961  49.785  1.00 36.26  ? 346 THR B CB  1 
ATOM   6291  O  OG1 . THR B  1 346 ? 34.859  51.568  51.085  1.00 42.28  ? 346 THR B OG1 1 
ATOM   6292  C  CG2 . THR B  1 346 ? 33.531  51.073  49.198  1.00 35.90  ? 346 THR B CG2 1 
ATOM   6293  N  N   . PRO B  1 347 ? 34.285  47.939  48.387  1.00 32.96  ? 347 PRO B N   1 
ATOM   6294  C  CA  . PRO B  1 347 ? 34.090  47.176  47.167  1.00 33.08  ? 347 PRO B CA  1 
ATOM   6295  C  C   . PRO B  1 347 ? 34.059  48.108  45.969  1.00 41.88  ? 347 PRO B C   1 
ATOM   6296  O  O   . PRO B  1 347 ? 33.194  49.001  45.900  1.00 49.37  ? 347 PRO B O   1 
ATOM   6297  C  CB  . PRO B  1 347 ? 32.714  46.579  47.375  1.00 34.66  ? 347 PRO B CB  1 
ATOM   6298  C  CG  . PRO B  1 347 ? 32.603  46.469  48.825  1.00 34.06  ? 347 PRO B CG  1 
ATOM   6299  C  CD  . PRO B  1 347 ? 33.192  47.716  49.340  1.00 33.73  ? 347 PRO B CD  1 
ATOM   6300  N  N   . VAL B  1 348 ? 34.941  47.856  45.000  1.00 45.31  ? 348 VAL B N   1 
ATOM   6301  C  CA  . VAL B  1 348 ? 35.053  48.652  43.778  1.00 44.77  ? 348 VAL B CA  1 
ATOM   6302  C  C   . VAL B  1 348 ? 34.758  47.771  42.572  1.00 46.65  ? 348 VAL B C   1 
ATOM   6303  O  O   . VAL B  1 348 ? 34.985  46.559  42.617  1.00 48.30  ? 348 VAL B O   1 
ATOM   6304  C  CB  . VAL B  1 348 ? 36.472  49.204  43.631  1.00 45.60  ? 348 VAL B CB  1 
ATOM   6305  C  CG1 . VAL B  1 348 ? 36.803  50.074  44.812  1.00 45.07  ? 348 VAL B CG1 1 
ATOM   6306  C  CG2 . VAL B  1 348 ? 37.462  48.091  43.524  1.00 44.46  ? 348 VAL B CG2 1 
ATOM   6307  N  N   . LYS B  1 349 ? 34.221  48.343  41.498  1.00 48.20  ? 349 LYS B N   1 
ATOM   6308  C  CA  . LYS B  1 349 ? 33.939  47.491  40.350  1.00 49.05  ? 349 LYS B CA  1 
ATOM   6309  C  C   . LYS B  1 349 ? 35.248  46.888  39.887  1.00 45.81  ? 349 LYS B C   1 
ATOM   6310  O  O   . LYS B  1 349 ? 36.276  47.554  39.927  1.00 47.15  ? 349 LYS B O   1 
ATOM   6311  C  CB  . LYS B  1 349 ? 33.229  48.230  39.203  1.00 53.33  ? 349 LYS B CB  1 
ATOM   6312  C  CG  . LYS B  1 349 ? 32.905  47.279  38.003  1.00 65.68  ? 349 LYS B CG  1 
ATOM   6313  C  CD  . LYS B  1 349 ? 31.813  47.779  37.035  1.00 74.57  ? 349 LYS B CD  1 
ATOM   6314  C  CE  . LYS B  1 349 ? 30.408  47.823  37.676  1.00 81.42  ? 349 LYS B CE  1 
ATOM   6315  N  NZ  . LYS B  1 349 ? 30.190  48.935  38.709  1.00 85.90  ? 349 LYS B NZ  1 
ATOM   6316  N  N   . ASP B  1 350 ? 35.223  45.605  39.545  1.00 43.32  ? 350 ASP B N   1 
ATOM   6317  C  CA  . ASP B  1 350 ? 36.408  44.926  39.075  1.00 38.90  ? 350 ASP B CA  1 
ATOM   6318  C  C   . ASP B  1 350 ? 35.923  43.968  38.036  1.00 38.01  ? 350 ASP B C   1 
ATOM   6319  O  O   . ASP B  1 350 ? 35.076  43.150  38.319  1.00 40.82  ? 350 ASP B O   1 
ATOM   6320  C  CB  . ASP B  1 350 ? 37.044  44.181  40.225  1.00 39.85  ? 350 ASP B CB  1 
ATOM   6321  C  CG  . ASP B  1 350 ? 38.457  43.735  39.911  1.00 44.42  ? 350 ASP B CG  1 
ATOM   6322  O  OD1 . ASP B  1 350 ? 38.704  43.363  38.734  1.00 43.36  ? 350 ASP B OD1 1 
ATOM   6323  O  OD2 . ASP B  1 350 ? 39.320  43.757  40.835  1.00 43.04  ? 350 ASP B OD2 1 
ATOM   6324  N  N   . GLN B  1 351 ? 36.435  44.066  36.825  1.00 39.23  ? 351 GLN B N   1 
ATOM   6325  C  CA  . GLN B  1 351 ? 35.949  43.183  35.776  1.00 43.32  ? 351 GLN B CA  1 
ATOM   6326  C  C   . GLN B  1 351 ? 36.650  41.857  35.736  1.00 43.40  ? 351 GLN B C   1 
ATOM   6327  O  O   . GLN B  1 351 ? 36.502  41.113  34.779  1.00 48.25  ? 351 GLN B O   1 
ATOM   6328  C  CB  . GLN B  1 351 ? 35.976  43.871  34.394  1.00 49.71  ? 351 GLN B CB  1 
ATOM   6329  C  CG  . GLN B  1 351 ? 34.930  45.005  34.190  1.00 57.34  ? 351 GLN B CG  1 
ATOM   6330  C  CD  . GLN B  1 351 ? 33.496  44.495  33.949  1.00 61.14  ? 351 GLN B CD  1 
ATOM   6331  O  OE1 . GLN B  1 351 ? 33.229  43.803  32.956  1.00 65.09  ? 351 GLN B OE1 1 
ATOM   6332  N  NE2 . GLN B  1 351 ? 32.567  44.859  34.839  1.00 59.43  ? 351 GLN B NE2 1 
ATOM   6333  N  N   . SER B  1 352 ? 37.498  41.598  36.718  1.00 43.19  ? 352 SER B N   1 
ATOM   6334  C  CA  . SER B  1 352 ? 38.169  40.297  36.782  1.00 44.69  ? 352 SER B CA  1 
ATOM   6335  C  C   . SER B  1 352 ? 37.529  39.481  37.861  1.00 44.56  ? 352 SER B C   1 
ATOM   6336  O  O   . SER B  1 352 ? 37.778  38.270  37.967  1.00 49.55  ? 352 SER B O   1 
ATOM   6337  C  CB  . SER B  1 352 ? 39.623  40.415  37.110  1.00 45.09  ? 352 SER B CB  1 
ATOM   6338  O  OG  . SER B  1 352 ? 40.329  40.764  35.944  1.00 61.00  ? 352 SER B OG  1 
ATOM   6339  N  N   . ALA B  1 353 ? 36.774  40.181  38.704  1.00 40.36  ? 353 ALA B N   1 
ATOM   6340  C  CA  . ALA B  1 353 ? 36.063  39.579  39.792  1.00 36.85  ? 353 ALA B CA  1 
ATOM   6341  C  C   . ALA B  1 353 ? 34.853  38.886  39.200  1.00 39.73  ? 353 ALA B C   1 
ATOM   6342  O  O   . ALA B  1 353 ? 34.390  39.231  38.113  1.00 45.09  ? 353 ALA B O   1 
ATOM   6343  C  CB  . ALA B  1 353 ? 35.625  40.637  40.763  1.00 31.61  ? 353 ALA B CB  1 
ATOM   6344  N  N   . PRO B  1 354 ? 34.405  37.811  39.846  1.00 40.91  ? 354 PRO B N   1 
ATOM   6345  C  CA  . PRO B  1 354 ? 33.241  37.047  39.407  1.00 38.70  ? 354 PRO B CA  1 
ATOM   6346  C  C   . PRO B  1 354 ? 31.963  37.782  39.851  1.00 40.64  ? 354 PRO B C   1 
ATOM   6347  O  O   . PRO B  1 354 ? 32.012  38.782  40.552  1.00 38.91  ? 354 PRO B O   1 
ATOM   6348  C  CB  . PRO B  1 354 ? 33.390  35.779  40.216  1.00 36.29  ? 354 PRO B CB  1 
ATOM   6349  C  CG  . PRO B  1 354 ? 34.004  36.299  41.520  1.00 37.75  ? 354 PRO B CG  1 
ATOM   6350  C  CD  . PRO B  1 354 ? 35.082  37.137  40.970  1.00 39.63  ? 354 PRO B CD  1 
ATOM   6351  N  N   . VAL B  1 355 ? 30.822  37.275  39.436  1.00 42.82  ? 355 VAL B N   1 
ATOM   6352  C  CA  . VAL B  1 355 ? 29.547  37.833  39.838  1.00 45.06  ? 355 VAL B CA  1 
ATOM   6353  C  C   . VAL B  1 355 ? 29.154  36.944  41.020  1.00 45.86  ? 355 VAL B C   1 
ATOM   6354  O  O   . VAL B  1 355 ? 29.193  35.718  40.887  1.00 45.90  ? 355 VAL B O   1 
ATOM   6355  C  CB  . VAL B  1 355 ? 28.531  37.636  38.701  1.00 47.42  ? 355 VAL B CB  1 
ATOM   6356  C  CG1 . VAL B  1 355 ? 27.154  38.148  39.088  1.00 48.49  ? 355 VAL B CG1 1 
ATOM   6357  C  CG2 . VAL B  1 355 ? 29.040  38.306  37.460  1.00 48.48  ? 355 VAL B CG2 1 
ATOM   6358  N  N   . TYR B  1 356 ? 28.835  37.537  42.173  1.00 46.35  ? 356 TYR B N   1 
ATOM   6359  C  CA  . TYR B  1 356 ? 28.414  36.745  43.327  1.00 47.18  ? 356 TYR B CA  1 
ATOM   6360  C  C   . TYR B  1 356 ? 26.873  36.698  43.378  1.00 46.67  ? 356 TYR B C   1 
ATOM   6361  O  O   . TYR B  1 356 ? 26.242  37.727  43.614  1.00 49.43  ? 356 TYR B O   1 
ATOM   6362  C  CB  . TYR B  1 356 ? 28.974  37.290  44.671  1.00 47.95  ? 356 TYR B CB  1 
ATOM   6363  C  CG  . TYR B  1 356 ? 30.478  37.369  44.743  1.00 52.34  ? 356 TYR B CG  1 
ATOM   6364  C  CD1 . TYR B  1 356 ? 31.155  38.409  44.129  1.00 57.44  ? 356 TYR B CD1 1 
ATOM   6365  C  CD2 . TYR B  1 356 ? 31.228  36.409  45.401  1.00 56.88  ? 356 TYR B CD2 1 
ATOM   6366  C  CE1 . TYR B  1 356 ? 32.552  38.506  44.162  1.00 59.13  ? 356 TYR B CE1 1 
ATOM   6367  C  CE2 . TYR B  1 356 ? 32.645  36.497  45.437  1.00 57.26  ? 356 TYR B CE2 1 
ATOM   6368  C  CZ  . TYR B  1 356 ? 33.293  37.558  44.814  1.00 57.53  ? 356 TYR B CZ  1 
ATOM   6369  O  OH  . TYR B  1 356 ? 34.660  37.723  44.846  1.00 52.03  ? 356 TYR B OH  1 
ATOM   6370  N  N   . ILE B  1 357 ? 26.285  35.522  43.103  1.00 44.23  ? 357 ILE B N   1 
ATOM   6371  C  CA  . ILE B  1 357 ? 24.835  35.291  43.139  1.00 39.43  ? 357 ILE B CA  1 
ATOM   6372  C  C   . ILE B  1 357 ? 24.491  34.455  44.379  1.00 41.85  ? 357 ILE B C   1 
ATOM   6373  O  O   . ILE B  1 357 ? 25.329  33.690  44.862  1.00 45.42  ? 357 ILE B O   1 
ATOM   6374  C  CB  . ILE B  1 357 ? 24.363  34.518  41.891  1.00 34.11  ? 357 ILE B CB  1 
ATOM   6375  C  CG1 . ILE B  1 357 ? 24.456  35.419  40.674  1.00 36.89  ? 357 ILE B CG1 1 
ATOM   6376  C  CG2 . ILE B  1 357 ? 22.940  34.097  42.021  1.00 31.96  ? 357 ILE B CG2 1 
ATOM   6377  C  CD1 . ILE B  1 357 ? 24.117  34.734  39.380  1.00 35.91  ? 357 ILE B CD1 1 
ATOM   6378  N  N   . THR B  1 358 ? 23.295  34.651  44.943  1.00 40.30  ? 358 THR B N   1 
ATOM   6379  C  CA  . THR B  1 358 ? 22.877  33.868  46.095  1.00 34.78  ? 358 THR B CA  1 
ATOM   6380  C  C   . THR B  1 358 ? 21.454  33.337  45.901  1.00 36.03  ? 358 THR B C   1 
ATOM   6381  O  O   . THR B  1 358 ? 20.543  34.123  45.734  1.00 40.25  ? 358 THR B O   1 
ATOM   6382  C  CB  . THR B  1 358 ? 23.087  34.624  47.422  1.00 28.86  ? 358 THR B CB  1 
ATOM   6383  O  OG1 . THR B  1 358 ? 21.848  34.999  47.985  1.00 24.82  ? 358 THR B OG1 1 
ATOM   6384  C  CG2 . THR B  1 358 ? 24.017  35.803  47.256  1.00 29.25  ? 358 THR B CG2 1 
ATOM   6385  N  N   . ILE B  1 359 ? 21.297  32.018  45.775  1.00 34.00  ? 359 ILE B N   1 
ATOM   6386  C  CA  . ILE B  1 359 ? 19.993  31.422  45.577  1.00 36.93  ? 359 ILE B CA  1 
ATOM   6387  C  C   . ILE B  1 359 ? 19.539  30.500  46.682  1.00 39.82  ? 359 ILE B C   1 
ATOM   6388  O  O   . ILE B  1 359 ? 19.066  29.388  46.411  1.00 40.21  ? 359 ILE B O   1 
ATOM   6389  C  CB  . ILE B  1 359 ? 19.888  30.572  44.304  1.00 41.93  ? 359 ILE B CB  1 
ATOM   6390  C  CG1 . ILE B  1 359 ? 21.180  29.829  44.055  1.00 46.35  ? 359 ILE B CG1 1 
ATOM   6391  C  CG2 . ILE B  1 359 ? 19.363  31.365  43.123  1.00 45.38  ? 359 ILE B CG2 1 
ATOM   6392  C  CD1 . ILE B  1 359 ? 22.250  30.687  43.521  1.00 55.57  ? 359 ILE B CD1 1 
ATOM   6393  N  N   . GLY B  1 360 ? 19.592  30.961  47.924  1.00 41.58  ? 360 GLY B N   1 
ATOM   6394  C  CA  . GLY B  1 360 ? 19.133  30.092  48.998  1.00 48.04  ? 360 GLY B CA  1 
ATOM   6395  C  C   . GLY B  1 360 ? 17.646  30.269  49.256  1.00 52.05  ? 360 GLY B C   1 
ATOM   6396  O  O   . GLY B  1 360 ? 17.133  30.086  50.374  1.00 54.22  ? 360 GLY B O   1 
ATOM   6397  N  N   . ASP B  1 361 ? 16.919  30.557  48.192  1.00 53.20  ? 361 ASP B N   1 
ATOM   6398  C  CA  . ASP B  1 361 ? 15.507  30.829  48.338  1.00 51.25  ? 361 ASP B CA  1 
ATOM   6399  C  C   . ASP B  1 361 ? 14.652  29.711  47.768  1.00 49.76  ? 361 ASP B C   1 
ATOM   6400  O  O   . ASP B  1 361 ? 13.554  29.981  47.285  1.00 49.48  ? 361 ASP B O   1 
ATOM   6401  C  CB  . ASP B  1 361 ? 15.189  32.154  47.635  1.00 50.03  ? 361 ASP B CB  1 
ATOM   6402  C  CG  . ASP B  1 361 ? 15.371  32.062  46.105  1.00 50.61  ? 361 ASP B CG  1 
ATOM   6403  O  OD1 . ASP B  1 361 ? 16.224  31.272  45.644  1.00 49.50  ? 361 ASP B OD1 1 
ATOM   6404  O  OD2 . ASP B  1 361 ? 14.631  32.722  45.345  1.00 46.36  ? 361 ASP B OD2 1 
ATOM   6405  N  N   . ALA B  1 362 ? 15.135  28.471  47.774  1.00 45.58  ? 362 ALA B N   1 
ATOM   6406  C  CA  . ALA B  1 362 ? 14.309  27.414  47.213  1.00 40.51  ? 362 ALA B CA  1 
ATOM   6407  C  C   . ALA B  1 362 ? 13.185  26.970  48.128  1.00 41.53  ? 362 ALA B C   1 
ATOM   6408  O  O   . ALA B  1 362 ? 12.329  26.195  47.696  1.00 42.78  ? 362 ALA B O   1 
ATOM   6409  C  CB  . ALA B  1 362 ? 15.133  26.230  46.729  1.00 33.65  ? 362 ALA B CB  1 
ATOM   6410  N  N   . GLY B  1 363 ? 13.174  27.422  49.388  1.00 46.48  ? 363 GLY B N   1 
ATOM   6411  C  CA  . GLY B  1 363 ? 12.069  27.037  50.262  1.00 48.76  ? 363 GLY B CA  1 
ATOM   6412  C  C   . GLY B  1 363 ? 12.273  26.820  51.746  1.00 50.08  ? 363 GLY B C   1 
ATOM   6413  O  O   . GLY B  1 363 ? 11.461  27.300  52.570  1.00 48.57  ? 363 GLY B O   1 
ATOM   6414  N  N   . ASN B  1 364 ? 13.366  26.144  52.090  1.00 48.66  ? 364 ASN B N   1 
ATOM   6415  C  CA  . ASN B  1 364 ? 13.653  25.797  53.459  1.00 48.88  ? 364 ASN B CA  1 
ATOM   6416  C  C   . ASN B  1 364 ? 12.382  25.355  54.155  1.00 53.02  ? 364 ASN B C   1 
ATOM   6417  O  O   . ASN B  1 364 ? 11.591  24.616  53.574  1.00 53.13  ? 364 ASN B O   1 
ATOM   6418  C  CB  . ASN B  1 364 ? 14.372  26.907  54.223  1.00 47.24  ? 364 ASN B CB  1 
ATOM   6419  C  CG  . ASN B  1 364 ? 13.654  28.205  54.210  1.00 45.78  ? 364 ASN B CG  1 
ATOM   6420  O  OD1 . ASN B  1 364 ? 13.796  28.985  53.262  1.00 43.82  ? 364 ASN B OD1 1 
ATOM   6421  N  ND2 . ASN B  1 364 ? 12.958  28.503  55.299  1.00 37.20  ? 364 ASN B ND2 1 
ATOM   6422  N  N   . TYR B  1 365 ? 12.158  25.804  55.383  1.00 51.06  ? 365 TYR B N   1 
ATOM   6423  C  CA  . TYR B  1 365 ? 10.972  25.383  56.082  1.00 50.27  ? 365 TYR B CA  1 
ATOM   6424  C  C   . TYR B  1 365 ? 9.893   26.409  55.890  1.00 54.80  ? 365 TYR B C   1 
ATOM   6425  O  O   . TYR B  1 365 ? 9.127   26.686  56.822  1.00 55.33  ? 365 TYR B O   1 
ATOM   6426  C  CB  . TYR B  1 365 ? 11.264  25.175  57.547  1.00 44.30  ? 365 TYR B CB  1 
ATOM   6427  C  CG  . TYR B  1 365 ? 12.147  26.216  58.122  1.00 47.58  ? 365 TYR B CG  1 
ATOM   6428  C  CD1 . TYR B  1 365 ? 13.505  26.192  57.892  1.00 50.43  ? 365 TYR B CD1 1 
ATOM   6429  C  CD2 . TYR B  1 365 ? 11.638  27.202  58.935  1.00 52.38  ? 365 TYR B CD2 1 
ATOM   6430  C  CE1 . TYR B  1 365 ? 14.338  27.115  58.460  1.00 55.36  ? 365 TYR B CE1 1 
ATOM   6431  C  CE2 . TYR B  1 365 ? 12.461  28.145  59.519  1.00 56.29  ? 365 TYR B CE2 1 
ATOM   6432  C  CZ  . TYR B  1 365 ? 13.811  28.097  59.280  1.00 59.45  ? 365 TYR B CZ  1 
ATOM   6433  O  OH  . TYR B  1 365 ? 14.648  29.029  59.867  1.00 68.05  ? 365 TYR B OH  1 
ATOM   6434  N  N   . GLY B  1 366 ? 9.830   26.946  54.671  1.00 55.90  ? 366 GLY B N   1 
ATOM   6435  C  CA  . GLY B  1 366 ? 8.839   27.937  54.328  1.00 56.16  ? 366 GLY B CA  1 
ATOM   6436  C  C   . GLY B  1 366 ? 9.055   29.341  54.839  1.00 54.53  ? 366 GLY B C   1 
ATOM   6437  O  O   . GLY B  1 366 ? 8.103   30.064  55.047  1.00 55.92  ? 366 GLY B O   1 
ATOM   6438  N  N   . VAL B  1 367 ? 10.288  29.777  54.967  1.00 55.48  ? 367 VAL B N   1 
ATOM   6439  C  CA  . VAL B  1 367 ? 10.512  31.133  55.458  1.00 56.37  ? 367 VAL B CA  1 
ATOM   6440  C  C   . VAL B  1 367 ? 11.472  31.922  54.567  1.00 61.99  ? 367 VAL B C   1 
ATOM   6441  O  O   . VAL B  1 367 ? 12.489  31.376  54.108  1.00 66.55  ? 367 VAL B O   1 
ATOM   6442  C  CB  . VAL B  1 367 ? 11.022  31.120  56.891  1.00 49.80  ? 367 VAL B CB  1 
ATOM   6443  C  CG1 . VAL B  1 367 ? 11.714  32.401  57.227  1.00 49.31  ? 367 VAL B CG1 1 
ATOM   6444  C  CG2 . VAL B  1 367 ? 9.905   30.950  57.803  1.00 46.85  ? 367 VAL B CG2 1 
ATOM   6445  N  N   . ILE B  1 368 ? 11.148  33.203  54.347  1.00 62.63  ? 368 ILE B N   1 
ATOM   6446  C  CA  . ILE B  1 368 ? 11.950  34.103  53.527  1.00 59.88  ? 368 ILE B CA  1 
ATOM   6447  C  C   . ILE B  1 368 ? 12.627  35.206  54.337  1.00 58.93  ? 368 ILE B C   1 
ATOM   6448  O  O   . ILE B  1 368 ? 12.070  35.679  55.321  1.00 55.28  ? 368 ILE B O   1 
ATOM   6449  C  CB  . ILE B  1 368 ? 11.073  34.760  52.466  1.00 59.43  ? 368 ILE B CB  1 
ATOM   6450  C  CG1 . ILE B  1 368 ? 10.868  33.814  51.295  1.00 62.82  ? 368 ILE B CG1 1 
ATOM   6451  C  CG2 . ILE B  1 368 ? 11.727  36.002  51.917  1.00 62.43  ? 368 ILE B CG2 1 
ATOM   6452  C  CD1 . ILE B  1 368 ? 12.014  33.811  50.268  1.00 61.32  ? 368 ILE B CD1 1 
ATOM   6453  N  N   . ASP B  1 369 ? 13.836  35.586  53.923  1.00 61.12  ? 369 ASP B N   1 
ATOM   6454  C  CA  . ASP B  1 369 ? 14.583  36.656  54.558  1.00 63.59  ? 369 ASP B CA  1 
ATOM   6455  C  C   . ASP B  1 369 ? 14.270  37.895  53.749  1.00 66.32  ? 369 ASP B C   1 
ATOM   6456  O  O   . ASP B  1 369 ? 14.719  38.030  52.609  1.00 61.74  ? 369 ASP B O   1 
ATOM   6457  C  CB  . ASP B  1 369 ? 16.079  36.383  54.501  1.00 64.49  ? 369 ASP B CB  1 
ATOM   6458  C  CG  . ASP B  1 369 ? 16.471  35.213  55.334  1.00 62.87  ? 369 ASP B CG  1 
ATOM   6459  O  OD1 . ASP B  1 369 ? 15.943  35.094  56.459  1.00 64.37  ? 369 ASP B OD1 1 
ATOM   6460  O  OD2 . ASP B  1 369 ? 17.296  34.417  54.866  1.00 59.31  ? 369 ASP B OD2 1 
ATOM   6461  N  N   . SER B  1 370 ? 13.484  38.786  54.347  1.00 71.45  ? 370 SER B N   1 
ATOM   6462  C  CA  . SER B  1 370 ? 13.062  40.020  53.703  1.00 74.30  ? 370 SER B CA  1 
ATOM   6463  C  C   . SER B  1 370 ? 13.810  41.306  54.107  1.00 73.94  ? 370 SER B C   1 
ATOM   6464  O  O   . SER B  1 370 ? 13.860  42.231  53.298  1.00 78.38  ? 370 SER B O   1 
ATOM   6465  C  CB  . SER B  1 370 ? 11.563  40.218  53.921  1.00 78.91  ? 370 SER B CB  1 
ATOM   6466  O  OG  . SER B  1 370 ? 11.269  40.343  55.316  1.00 89.01  ? 370 SER B OG  1 
ATOM   6467  N  N   . ASN B  1 371 ? 14.336  41.418  55.339  1.00 70.21  ? 371 ASN B N   1 
ATOM   6468  C  CA  . ASN B  1 371 ? 15.057  42.643  55.736  1.00 69.42  ? 371 ASN B CA  1 
ATOM   6469  C  C   . ASN B  1 371 ? 16.300  42.803  54.901  1.00 65.77  ? 371 ASN B C   1 
ATOM   6470  O  O   . ASN B  1 371 ? 17.137  41.898  54.848  1.00 71.68  ? 371 ASN B O   1 
ATOM   6471  C  CB  . ASN B  1 371 ? 15.519  42.643  57.189  1.00 78.49  ? 371 ASN B CB  1 
ATOM   6472  C  CG  . ASN B  1 371 ? 14.646  41.815  58.080  1.00 94.74  ? 371 ASN B CG  1 
ATOM   6473  O  OD1 . ASN B  1 371 ? 13.404  41.878  58.001  1.00 102.95 ? 371 ASN B OD1 1 
ATOM   6474  N  ND2 . ASN B  1 371 ? 15.283  41.002  58.941  1.00 101.75 ? 371 ASN B ND2 1 
ATOM   6475  N  N   . MET B  1 372 ? 16.470  43.966  54.298  1.00 58.09  ? 372 MET B N   1 
ATOM   6476  C  CA  . MET B  1 372 ? 17.633  44.187  53.495  1.00 51.12  ? 372 MET B CA  1 
ATOM   6477  C  C   . MET B  1 372 ? 18.362  45.313  54.121  1.00 51.52  ? 372 MET B C   1 
ATOM   6478  O  O   . MET B  1 372 ? 17.849  45.953  55.039  1.00 52.25  ? 372 MET B O   1 
ATOM   6479  C  CB  . MET B  1 372 ? 17.201  44.506  52.111  1.00 47.41  ? 372 MET B CB  1 
ATOM   6480  C  CG  . MET B  1 372 ? 16.502  43.335  51.569  1.00 41.96  ? 372 MET B CG  1 
ATOM   6481  S  SD  . MET B  1 372 ? 15.449  43.847  50.340  1.00 43.99  ? 372 MET B SD  1 
ATOM   6482  C  CE  . MET B  1 372 ? 15.756  42.670  49.119  1.00 42.67  ? 372 MET B CE  1 
ATOM   6483  N  N   . ILE B  1 373 ? 19.615  45.466  53.759  1.00 53.02  ? 373 ILE B N   1 
ATOM   6484  C  CA  . ILE B  1 373 ? 20.366  46.551  54.332  1.00 57.37  ? 373 ILE B CA  1 
ATOM   6485  C  C   . ILE B  1 373 ? 19.931  47.737  53.480  1.00 60.37  ? 373 ILE B C   1 
ATOM   6486  O  O   . ILE B  1 373 ? 20.020  47.699  52.235  1.00 56.49  ? 373 ILE B O   1 
ATOM   6487  C  CB  . ILE B  1 373 ? 21.857  46.272  54.242  1.00 58.89  ? 373 ILE B CB  1 
ATOM   6488  C  CG1 . ILE B  1 373 ? 22.182  44.988  54.999  1.00 59.67  ? 373 ILE B CG1 1 
ATOM   6489  C  CG2 . ILE B  1 373 ? 22.641  47.407  54.858  1.00 60.64  ? 373 ILE B CG2 1 
ATOM   6490  C  CD1 . ILE B  1 373 ? 22.000  45.119  56.498  1.00 63.00  ? 373 ILE B CD1 1 
ATOM   6491  N  N   . GLN B  1 374 ? 19.326  48.735  54.129  1.00 62.51  ? 374 GLN B N   1 
ATOM   6492  C  CA  . GLN B  1 374 ? 18.841  49.896  53.385  1.00 61.93  ? 374 GLN B CA  1 
ATOM   6493  C  C   . GLN B  1 374 ? 19.728  51.124  53.532  1.00 58.46  ? 374 GLN B C   1 
ATOM   6494  O  O   . GLN B  1 374 ? 19.975  51.624  54.632  1.00 59.48  ? 374 GLN B O   1 
ATOM   6495  C  CB  . GLN B  1 374 ? 17.358  50.202  53.714  1.00 61.15  ? 374 GLN B CB  1 
ATOM   6496  C  CG  . GLN B  1 374 ? 16.418  50.371  52.468  1.00 67.82  ? 374 GLN B CG  1 
ATOM   6497  C  CD  . GLN B  1 374 ? 16.053  49.064  51.686  1.00 69.01  ? 374 GLN B CD  1 
ATOM   6498  O  OE1 . GLN B  1 374 ? 15.473  48.113  52.241  1.00 68.36  ? 374 GLN B OE1 1 
ATOM   6499  N  NE2 . GLN B  1 374 ? 16.310  49.074  50.371  1.00 71.47  ? 374 GLN B NE2 1 
ATOM   6500  N  N   . PRO B  1 375 ? 20.139  51.682  52.392  1.00 56.16  ? 375 PRO B N   1 
ATOM   6501  C  CA  . PRO B  1 375 ? 19.838  51.363  50.989  1.00 56.32  ? 375 PRO B CA  1 
ATOM   6502  C  C   . PRO B  1 375 ? 20.726  50.316  50.269  1.00 56.77  ? 375 PRO B C   1 
ATOM   6503  O  O   . PRO B  1 375 ? 21.874  50.085  50.660  1.00 59.19  ? 375 PRO B O   1 
ATOM   6504  C  CB  . PRO B  1 375 ? 19.984  52.711  50.335  1.00 54.10  ? 375 PRO B CB  1 
ATOM   6505  C  CG  . PRO B  1 375 ? 21.198  53.225  51.020  1.00 50.05  ? 375 PRO B CG  1 
ATOM   6506  C  CD  . PRO B  1 375 ? 20.964  52.894  52.474  1.00 52.91  ? 375 PRO B CD  1 
ATOM   6507  N  N   . GLN B  1 376 ? 20.192  49.753  49.177  1.00 56.73  ? 376 GLN B N   1 
ATOM   6508  C  CA  . GLN B  1 376 ? 20.889  48.751  48.378  1.00 53.50  ? 376 GLN B CA  1 
ATOM   6509  C  C   . GLN B  1 376 ? 22.256  49.291  48.051  1.00 54.66  ? 376 GLN B C   1 
ATOM   6510  O  O   . GLN B  1 376 ? 22.385  50.306  47.397  1.00 61.20  ? 376 GLN B O   1 
ATOM   6511  C  CB  . GLN B  1 376 ? 20.135  48.454  47.096  1.00 47.64  ? 376 GLN B CB  1 
ATOM   6512  C  CG  . GLN B  1 376 ? 20.879  47.502  46.197  1.00 53.21  ? 376 GLN B CG  1 
ATOM   6513  C  CD  . GLN B  1 376 ? 20.023  46.964  45.068  1.00 57.72  ? 376 GLN B CD  1 
ATOM   6514  O  OE1 . GLN B  1 376 ? 18.799  47.123  45.062  1.00 64.56  ? 376 GLN B OE1 1 
ATOM   6515  N  NE2 . GLN B  1 376 ? 20.654  46.276  44.130  1.00 55.05  ? 376 GLN B NE2 1 
ATOM   6516  N  N   . PRO B  1 377 ? 23.298  48.656  48.572  1.00 55.44  ? 377 PRO B N   1 
ATOM   6517  C  CA  . PRO B  1 377 ? 24.657  49.108  48.323  1.00 49.76  ? 377 PRO B CA  1 
ATOM   6518  C  C   . PRO B  1 377 ? 25.013  48.932  46.883  1.00 46.56  ? 377 PRO B C   1 
ATOM   6519  O  O   . PRO B  1 377 ? 24.422  48.137  46.153  1.00 41.80  ? 377 PRO B O   1 
ATOM   6520  C  CB  . PRO B  1 377 ? 25.470  48.216  49.220  1.00 53.97  ? 377 PRO B CB  1 
ATOM   6521  C  CG  . PRO B  1 377 ? 24.674  46.936  49.158  1.00 58.58  ? 377 PRO B CG  1 
ATOM   6522  C  CD  . PRO B  1 377 ? 23.285  47.414  49.354  1.00 56.29  ? 377 PRO B CD  1 
ATOM   6523  N  N   . GLU B  1 378 ? 26.026  49.682  46.508  1.00 49.86  ? 378 GLU B N   1 
ATOM   6524  C  CA  . GLU B  1 378 ? 26.536  49.731  45.150  1.00 57.85  ? 378 GLU B CA  1 
ATOM   6525  C  C   . GLU B  1 378 ? 26.831  48.374  44.567  1.00 58.62  ? 378 GLU B C   1 
ATOM   6526  O  O   . GLU B  1 378 ? 26.434  48.101  43.436  1.00 65.30  ? 378 GLU B O   1 
ATOM   6527  C  CB  . GLU B  1 378 ? 27.819  50.582  45.052  1.00 67.32  ? 378 GLU B CB  1 
ATOM   6528  C  CG  . GLU B  1 378 ? 28.084  51.629  46.194  1.00 82.94  ? 378 GLU B CG  1 
ATOM   6529  C  CD  . GLU B  1 378 ? 28.667  51.031  47.528  1.00 86.49  ? 378 GLU B CD  1 
ATOM   6530  O  OE1 . GLU B  1 378 ? 29.758  50.380  47.492  1.00 83.42  ? 378 GLU B OE1 1 
ATOM   6531  O  OE2 . GLU B  1 378 ? 28.032  51.243  48.606  1.00 84.06  ? 378 GLU B OE2 1 
ATOM   6532  N  N   . TYR B  1 379 ? 27.550  47.530  45.314  1.00 55.00  ? 379 TYR B N   1 
ATOM   6533  C  CA  . TYR B  1 379 ? 27.927  46.204  44.813  1.00 47.71  ? 379 TYR B CA  1 
ATOM   6534  C  C   . TYR B  1 379 ? 26.763  45.271  44.479  1.00 44.56  ? 379 TYR B C   1 
ATOM   6535  O  O   . TYR B  1 379 ? 26.888  44.358  43.647  1.00 42.31  ? 379 TYR B O   1 
ATOM   6536  C  CB  . TYR B  1 379 ? 28.908  45.538  45.762  1.00 42.65  ? 379 TYR B CB  1 
ATOM   6537  C  CG  . TYR B  1 379 ? 28.368  45.298  47.127  1.00 38.17  ? 379 TYR B CG  1 
ATOM   6538  C  CD1 . TYR B  1 379 ? 27.511  44.220  47.384  1.00 39.51  ? 379 TYR B CD1 1 
ATOM   6539  C  CD2 . TYR B  1 379 ? 28.727  46.130  48.176  1.00 35.01  ? 379 TYR B CD2 1 
ATOM   6540  C  CE1 . TYR B  1 379 ? 27.015  43.975  48.684  1.00 39.93  ? 379 TYR B CE1 1 
ATOM   6541  C  CE2 . TYR B  1 379 ? 28.250  45.906  49.475  1.00 38.13  ? 379 TYR B CE2 1 
ATOM   6542  C  CZ  . TYR B  1 379 ? 27.388  44.832  49.733  1.00 42.51  ? 379 TYR B CZ  1 
ATOM   6543  O  OH  . TYR B  1 379 ? 26.892  44.659  51.029  1.00 43.76  ? 379 TYR B OH  1 
ATOM   6544  N  N   . SER B  1 380 ? 25.624  45.551  45.091  1.00 41.09  ? 380 SER B N   1 
ATOM   6545  C  CA  . SER B  1 380 ? 24.446  44.763  44.870  1.00 42.19  ? 380 SER B CA  1 
ATOM   6546  C  C   . SER B  1 380 ? 23.737  45.184  43.595  1.00 43.73  ? 380 SER B C   1 
ATOM   6547  O  O   . SER B  1 380 ? 23.232  46.291  43.520  1.00 46.53  ? 380 SER B O   1 
ATOM   6548  C  CB  . SER B  1 380 ? 23.499  44.961  46.017  1.00 40.47  ? 380 SER B CB  1 
ATOM   6549  O  OG  . SER B  1 380 ? 22.373  44.153  45.784  1.00 47.80  ? 380 SER B OG  1 
ATOM   6550  N  N   . ALA B  1 381 ? 23.680  44.309  42.602  1.00 43.28  ? 381 ALA B N   1 
ATOM   6551  C  CA  . ALA B  1 381 ? 23.020  44.642  41.355  1.00 45.49  ? 381 ALA B CA  1 
ATOM   6552  C  C   . ALA B  1 381 ? 21.532  44.415  41.384  1.00 50.92  ? 381 ALA B C   1 
ATOM   6553  O  O   . ALA B  1 381 ? 20.793  45.120  40.712  1.00 62.04  ? 381 ALA B O   1 
ATOM   6554  C  CB  . ALA B  1 381 ? 23.621  43.856  40.183  1.00 38.78  ? 381 ALA B CB  1 
ATOM   6555  N  N   . PHE B  1 382 ? 21.068  43.448  42.155  1.00 53.94  ? 382 PHE B N   1 
ATOM   6556  C  CA  . PHE B  1 382 ? 19.651  43.129  42.163  1.00 52.44  ? 382 PHE B CA  1 
ATOM   6557  C  C   . PHE B  1 382 ? 19.345  42.240  43.349  1.00 50.78  ? 382 PHE B C   1 
ATOM   6558  O  O   . PHE B  1 382 ? 20.056  41.293  43.594  1.00 54.71  ? 382 PHE B O   1 
ATOM   6559  C  CB  . PHE B  1 382 ? 19.322  42.361  40.862  1.00 50.90  ? 382 PHE B CB  1 
ATOM   6560  C  CG  . PHE B  1 382 ? 17.916  41.871  40.794  1.00 57.68  ? 382 PHE B CG  1 
ATOM   6561  C  CD1 . PHE B  1 382 ? 17.481  40.861  41.633  1.00 59.22  ? 382 PHE B CD1 1 
ATOM   6562  C  CD2 . PHE B  1 382 ? 17.003  42.439  39.918  1.00 59.98  ? 382 PHE B CD2 1 
ATOM   6563  C  CE1 . PHE B  1 382 ? 16.151  40.425  41.604  1.00 62.38  ? 382 PHE B CE1 1 
ATOM   6564  C  CE2 . PHE B  1 382 ? 15.673  42.000  39.889  1.00 60.35  ? 382 PHE B CE2 1 
ATOM   6565  C  CZ  . PHE B  1 382 ? 15.248  40.996  40.729  1.00 58.67  ? 382 PHE B CZ  1 
ATOM   6566  N  N   . ARG B  1 383 ? 18.295  42.516  44.092  1.00 49.00  ? 383 ARG B N   1 
ATOM   6567  C  CA  . ARG B  1 383 ? 17.964  41.629  45.185  1.00 48.64  ? 383 ARG B CA  1 
ATOM   6568  C  C   . ARG B  1 383 ? 16.500  41.542  45.356  1.00 54.83  ? 383 ARG B C   1 
ATOM   6569  O  O   . ARG B  1 383 ? 15.797  42.518  45.122  1.00 63.28  ? 383 ARG B O   1 
ATOM   6570  C  CB  . ARG B  1 383 ? 18.574  42.045  46.511  1.00 40.54  ? 383 ARG B CB  1 
ATOM   6571  C  CG  . ARG B  1 383 ? 19.014  43.449  46.632  1.00 39.61  ? 383 ARG B CG  1 
ATOM   6572  C  CD  . ARG B  1 383 ? 18.357  44.041  47.828  1.00 47.00  ? 383 ARG B CD  1 
ATOM   6573  N  NE  . ARG B  1 383 ? 19.283  44.605  48.812  1.00 56.12  ? 383 ARG B NE  1 
ATOM   6574  C  CZ  . ARG B  1 383 ? 19.067  45.744  49.477  1.00 61.60  ? 383 ARG B CZ  1 
ATOM   6575  N  NH1 . ARG B  1 383 ? 17.977  46.472  49.259  1.00 66.94  ? 383 ARG B NH1 1 
ATOM   6576  N  NH2 . ARG B  1 383 ? 19.876  46.107  50.452  1.00 65.55  ? 383 ARG B NH2 1 
ATOM   6577  N  N   . GLU B  1 384 ? 16.022  40.355  45.699  1.00 59.94  ? 384 GLU B N   1 
ATOM   6578  C  CA  . GLU B  1 384 ? 14.594  40.156  45.937  1.00 61.56  ? 384 GLU B CA  1 
ATOM   6579  C  C   . GLU B  1 384 ? 14.347  38.999  46.866  1.00 59.77  ? 384 GLU B C   1 
ATOM   6580  O  O   . GLU B  1 384 ? 15.013  37.967  46.767  1.00 62.81  ? 384 GLU B O   1 
ATOM   6581  C  CB  . GLU B  1 384 ? 13.802  39.934  44.656  1.00 64.44  ? 384 GLU B CB  1 
ATOM   6582  C  CG  . GLU B  1 384 ? 12.301  40.069  44.920  1.00 73.67  ? 384 GLU B CG  1 
ATOM   6583  C  CD  . GLU B  1 384 ? 11.438  39.859  43.687  1.00 78.44  ? 384 GLU B CD  1 
ATOM   6584  O  OE1 . GLU B  1 384 ? 11.763  40.423  42.614  1.00 84.19  ? 384 GLU B OE1 1 
ATOM   6585  O  OE2 . GLU B  1 384 ? 10.413  39.145  43.804  1.00 77.33  ? 384 GLU B OE2 1 
ATOM   6586  N  N   . ALA B  1 385 ? 13.394  39.203  47.772  1.00 55.33  ? 385 ALA B N   1 
ATOM   6587  C  CA  . ALA B  1 385 ? 13.003  38.223  48.764  1.00 52.51  ? 385 ALA B CA  1 
ATOM   6588  C  C   . ALA B  1 385 ? 11.822  37.392  48.287  1.00 52.66  ? 385 ALA B C   1 
ATOM   6589  O  O   . ALA B  1 385 ? 10.699  37.614  48.733  1.00 55.40  ? 385 ALA B O   1 
ATOM   6590  C  CB  . ALA B  1 385 ? 12.655  38.918  50.093  1.00 50.41  ? 385 ALA B CB  1 
ATOM   6591  N  N   . SER B  1 386 ? 12.070  36.478  47.352  1.00 50.43  ? 386 SER B N   1 
ATOM   6592  C  CA  . SER B  1 386 ? 11.044  35.572  46.839  1.00 51.89  ? 386 SER B CA  1 
ATOM   6593  C  C   . SER B  1 386 ? 11.586  34.150  46.758  1.00 48.22  ? 386 SER B C   1 
ATOM   6594  O  O   . SER B  1 386 ? 12.785  33.946  46.711  1.00 53.21  ? 386 SER B O   1 
ATOM   6595  C  CB  . SER B  1 386 ? 10.577  36.019  45.451  1.00 55.99  ? 386 SER B CB  1 
ATOM   6596  O  OG  . SER B  1 386 ? 9.693   37.121  45.559  1.00 68.72  ? 386 SER B OG  1 
ATOM   6597  N  N   . PHE B  1 387 ? 10.713  33.165  46.738  1.00 41.95  ? 387 PHE B N   1 
ATOM   6598  C  CA  . PHE B  1 387 ? 11.185  31.816  46.654  1.00 39.88  ? 387 PHE B CA  1 
ATOM   6599  C  C   . PHE B  1 387 ? 11.414  31.577  45.185  1.00 39.25  ? 387 PHE B C   1 
ATOM   6600  O  O   . PHE B  1 387 ? 10.851  32.280  44.367  1.00 39.91  ? 387 PHE B O   1 
ATOM   6601  C  CB  . PHE B  1 387 ? 10.158  30.845  47.252  1.00 37.68  ? 387 PHE B CB  1 
ATOM   6602  C  CG  . PHE B  1 387 ? 10.097  30.876  48.769  1.00 45.84  ? 387 PHE B CG  1 
ATOM   6603  C  CD1 . PHE B  1 387 ? 11.208  30.527  49.538  1.00 51.43  ? 387 PHE B CD1 1 
ATOM   6604  C  CD2 . PHE B  1 387 ? 8.930   31.208  49.435  1.00 47.55  ? 387 PHE B CD2 1 
ATOM   6605  C  CE1 . PHE B  1 387 ? 11.156  30.499  50.957  1.00 52.36  ? 387 PHE B CE1 1 
ATOM   6606  C  CE2 . PHE B  1 387 ? 8.875   31.180  50.851  1.00 55.31  ? 387 PHE B CE2 1 
ATOM   6607  C  CZ  . PHE B  1 387 ? 9.998   30.820  51.606  1.00 53.36  ? 387 PHE B CZ  1 
ATOM   6608  N  N   . GLY B  1 388 ? 12.312  30.662  44.858  1.00 39.02  ? 388 GLY B N   1 
ATOM   6609  C  CA  . GLY B  1 388 ? 12.569  30.342  43.476  1.00 40.46  ? 388 GLY B CA  1 
ATOM   6610  C  C   . GLY B  1 388 ? 13.845  29.551  43.314  1.00 43.58  ? 388 GLY B C   1 
ATOM   6611  O  O   . GLY B  1 388 ? 14.494  29.210  44.284  1.00 47.63  ? 388 GLY B O   1 
ATOM   6612  N  N   . HIS B  1 389 ? 14.211  29.274  42.077  1.00 41.83  ? 389 HIS B N   1 
ATOM   6613  C  CA  . HIS B  1 389 ? 15.407  28.536  41.758  1.00 43.41  ? 389 HIS B CA  1 
ATOM   6614  C  C   . HIS B  1 389 ? 16.062  29.308  40.613  1.00 47.85  ? 389 HIS B C   1 
ATOM   6615  O  O   . HIS B  1 389 ? 15.502  30.298  40.181  1.00 53.82  ? 389 HIS B O   1 
ATOM   6616  C  CB  . HIS B  1 389 ? 15.015  27.156  41.278  1.00 44.63  ? 389 HIS B CB  1 
ATOM   6617  C  CG  . HIS B  1 389 ? 14.298  27.143  39.957  1.00 48.32  ? 389 HIS B CG  1 
ATOM   6618  N  ND1 . HIS B  1 389 ? 14.920  26.807  38.766  1.00 54.06  ? 389 HIS B ND1 1 
ATOM   6619  C  CD2 . HIS B  1 389 ? 12.995  27.342  39.648  1.00 47.40  ? 389 HIS B CD2 1 
ATOM   6620  C  CE1 . HIS B  1 389 ? 14.035  26.793  37.786  1.00 51.15  ? 389 HIS B CE1 1 
ATOM   6621  N  NE2 . HIS B  1 389 ? 12.860  27.111  38.295  1.00 54.56  ? 389 HIS B NE2 1 
ATOM   6622  N  N   . GLY B  1 390 ? 17.190  28.845  40.067  1.00 47.05  ? 390 GLY B N   1 
ATOM   6623  C  CA  . GLY B  1 390 ? 17.828  29.557  38.970  1.00 38.46  ? 390 GLY B CA  1 
ATOM   6624  C  C   . GLY B  1 390 ? 18.281  28.592  37.906  1.00 39.78  ? 390 GLY B C   1 
ATOM   6625  O  O   . GLY B  1 390 ? 18.139  27.381  38.078  1.00 41.69  ? 390 GLY B O   1 
ATOM   6626  N  N   . MET B  1 391 ? 18.733  29.105  36.768  1.00 39.33  ? 391 MET B N   1 
ATOM   6627  C  CA  . MET B  1 391 ? 19.246  28.255  35.697  1.00 39.14  ? 391 MET B CA  1 
ATOM   6628  C  C   . MET B  1 391 ? 20.443  29.001  35.165  1.00 38.23  ? 391 MET B C   1 
ATOM   6629  O  O   . MET B  1 391 ? 20.436  30.216  35.151  1.00 41.71  ? 391 MET B O   1 
ATOM   6630  C  CB  . MET B  1 391 ? 18.227  28.101  34.594  1.00 43.60  ? 391 MET B CB  1 
ATOM   6631  C  CG  . MET B  1 391 ? 16.908  27.476  35.047  1.00 59.80  ? 391 MET B CG  1 
ATOM   6632  S  SD  . MET B  1 391 ? 16.929  25.660  35.182  1.00 67.07  ? 391 MET B SD  1 
ATOM   6633  C  CE  . MET B  1 391 ? 17.567  25.285  33.531  1.00 54.76  ? 391 MET B CE  1 
ATOM   6634  N  N   . PHE B  1 392 ? 21.502  28.287  34.821  1.00 37.72  ? 392 PHE B N   1 
ATOM   6635  C  CA  . PHE B  1 392 ? 22.716  28.893  34.281  1.00 38.08  ? 392 PHE B CA  1 
ATOM   6636  C  C   . PHE B  1 392 ? 22.946  28.158  32.967  1.00 39.72  ? 392 PHE B C   1 
ATOM   6637  O  O   . PHE B  1 392 ? 23.386  27.001  32.927  1.00 39.84  ? 392 PHE B O   1 
ATOM   6638  C  CB  . PHE B  1 392 ? 23.872  28.688  35.252  1.00 36.30  ? 392 PHE B CB  1 
ATOM   6639  C  CG  . PHE B  1 392 ? 25.115  29.393  34.856  1.00 38.74  ? 392 PHE B CG  1 
ATOM   6640  C  CD1 . PHE B  1 392 ? 25.339  30.706  35.253  1.00 37.59  ? 392 PHE B CD1 1 
ATOM   6641  C  CD2 . PHE B  1 392 ? 26.073  28.746  34.085  1.00 39.50  ? 392 PHE B CD2 1 
ATOM   6642  C  CE1 . PHE B  1 392 ? 26.507  31.363  34.886  1.00 33.27  ? 392 PHE B CE1 1 
ATOM   6643  C  CE2 . PHE B  1 392 ? 27.242  29.397  33.716  1.00 40.23  ? 392 PHE B CE2 1 
ATOM   6644  C  CZ  . PHE B  1 392 ? 27.455  30.713  34.122  1.00 34.51  ? 392 PHE B CZ  1 
ATOM   6645  N  N   . ASP B  1 393 ? 22.663  28.851  31.879  1.00 41.69  ? 393 ASP B N   1 
ATOM   6646  C  CA  . ASP B  1 393 ? 22.725  28.231  30.583  1.00 44.65  ? 393 ASP B CA  1 
ATOM   6647  C  C   . ASP B  1 393 ? 23.928  28.525  29.774  1.00 43.13  ? 393 ASP B C   1 
ATOM   6648  O  O   . ASP B  1 393 ? 24.012  29.548  29.104  1.00 49.14  ? 393 ASP B O   1 
ATOM   6649  C  CB  . ASP B  1 393 ? 21.485  28.644  29.818  1.00 53.68  ? 393 ASP B CB  1 
ATOM   6650  C  CG  . ASP B  1 393 ? 21.203  27.757  28.608  1.00 59.65  ? 393 ASP B CG  1 
ATOM   6651  O  OD1 . ASP B  1 393 ? 21.999  26.825  28.281  1.00 59.98  ? 393 ASP B OD1 1 
ATOM   6652  O  OD2 . ASP B  1 393 ? 20.151  28.030  27.980  1.00 65.76  ? 393 ASP B OD2 1 
ATOM   6653  N  N   . ILE B  1 394 ? 24.830  27.584  29.740  1.00 41.48  ? 394 ILE B N   1 
ATOM   6654  C  CA  . ILE B  1 394 ? 26.018  27.804  28.972  1.00 43.19  ? 394 ILE B CA  1 
ATOM   6655  C  C   . ILE B  1 394 ? 25.692  27.604  27.507  1.00 43.10  ? 394 ILE B C   1 
ATOM   6656  O  O   . ILE B  1 394 ? 25.160  26.563  27.102  1.00 44.19  ? 394 ILE B O   1 
ATOM   6657  C  CB  . ILE B  1 394 ? 27.096  26.849  29.431  1.00 43.87  ? 394 ILE B CB  1 
ATOM   6658  C  CG1 . ILE B  1 394 ? 27.453  27.179  30.882  1.00 42.84  ? 394 ILE B CG1 1 
ATOM   6659  C  CG2 . ILE B  1 394 ? 28.296  26.884  28.501  1.00 39.21  ? 394 ILE B CG2 1 
ATOM   6660  C  CD1 . ILE B  1 394 ? 28.409  26.188  31.486  1.00 33.21  ? 394 ILE B CD1 1 
ATOM   6661  N  N   . LYS B  1 395 ? 25.994  28.624  26.724  1.00 43.09  ? 395 LYS B N   1 
ATOM   6662  C  CA  . LYS B  1 395 ? 25.765  28.563  25.294  1.00 45.86  ? 395 LYS B CA  1 
ATOM   6663  C  C   . LYS B  1 395 ? 27.039  28.404  24.471  1.00 49.19  ? 395 LYS B C   1 
ATOM   6664  O  O   . LYS B  1 395 ? 27.139  27.562  23.589  1.00 48.97  ? 395 LYS B O   1 
ATOM   6665  C  CB  . LYS B  1 395 ? 25.132  29.863  24.866  1.00 44.44  ? 395 LYS B CB  1 
ATOM   6666  C  CG  . LYS B  1 395 ? 23.730  30.003  25.268  1.00 55.81  ? 395 LYS B CG  1 
ATOM   6667  C  CD  . LYS B  1 395 ? 22.855  29.224  24.292  1.00 67.77  ? 395 LYS B CD  1 
ATOM   6668  C  CE  . LYS B  1 395 ? 21.396  29.096  24.773  1.00 72.96  ? 395 LYS B CE  1 
ATOM   6669  N  NZ  . LYS B  1 395 ? 20.682  30.405  25.100  1.00 82.29  ? 395 LYS B NZ  1 
ATOM   6670  N  N   . ASN B  1 396 ? 28.019  29.238  24.785  1.00 55.39  ? 396 ASN B N   1 
ATOM   6671  C  CA  . ASN B  1 396 ? 29.263  29.337  24.034  1.00 59.48  ? 396 ASN B CA  1 
ATOM   6672  C  C   . ASN B  1 396 ? 30.436  29.242  24.985  1.00 58.76  ? 396 ASN B C   1 
ATOM   6673  O  O   . ASN B  1 396 ? 30.273  29.010  26.175  1.00 58.93  ? 396 ASN B O   1 
ATOM   6674  C  CB  . ASN B  1 396 ? 29.291  30.773  23.441  1.00 64.93  ? 396 ASN B CB  1 
ATOM   6675  C  CG  . ASN B  1 396 ? 28.809  30.832  22.012  1.00 73.65  ? 396 ASN B CG  1 
ATOM   6676  O  OD1 . ASN B  1 396 ? 29.549  30.367  21.152  1.00 76.01  ? 396 ASN B OD1 1 
ATOM   6677  N  ND2 . ASN B  1 396 ? 27.557  31.251  21.746  1.00 81.56  ? 396 ASN B ND2 1 
ATOM   6678  N  N   . ARG B  1 397 ? 31.621  29.498  24.449  1.00 55.83  ? 397 ARG B N   1 
ATOM   6679  C  CA  . ARG B  1 397 ? 32.818  29.584  25.262  1.00 49.62  ? 397 ARG B CA  1 
ATOM   6680  C  C   . ARG B  1 397 ? 32.832  31.044  25.775  1.00 48.60  ? 397 ARG B C   1 
ATOM   6681  O  O   . ARG B  1 397 ? 33.618  31.370  26.654  1.00 49.17  ? 397 ARG B O   1 
ATOM   6682  C  CB  . ARG B  1 397 ? 34.071  29.337  24.422  1.00 49.31  ? 397 ARG B CB  1 
ATOM   6683  C  CG  . ARG B  1 397 ? 34.586  30.576  23.715  1.00 48.51  ? 397 ARG B CG  1 
ATOM   6684  C  CD  . ARG B  1 397 ? 35.822  30.277  22.934  1.00 49.64  ? 397 ARG B CD  1 
ATOM   6685  N  NE  . ARG B  1 397 ? 35.545  29.399  21.812  1.00 53.45  ? 397 ARG B NE  1 
ATOM   6686  C  CZ  . ARG B  1 397 ? 36.467  28.997  20.940  1.00 61.64  ? 397 ARG B CZ  1 
ATOM   6687  N  NH1 . ARG B  1 397 ? 37.732  29.377  21.055  1.00 60.30  ? 397 ARG B NH1 1 
ATOM   6688  N  NH2 . ARG B  1 397 ? 36.122  28.248  19.901  1.00 70.40  ? 397 ARG B NH2 1 
ATOM   6689  N  N   . THR B  1 398 ? 32.001  31.915  25.177  1.00 47.56  ? 398 THR B N   1 
ATOM   6690  C  CA  . THR B  1 398 ? 31.888  33.347  25.538  1.00 46.86  ? 398 THR B CA  1 
ATOM   6691  C  C   . THR B  1 398 ? 30.583  33.725  26.220  1.00 50.22  ? 398 THR B C   1 
ATOM   6692  O  O   . THR B  1 398 ? 30.527  34.690  27.022  1.00 45.04  ? 398 THR B O   1 
ATOM   6693  C  CB  . THR B  1 398 ? 31.981  34.282  24.304  1.00 45.34  ? 398 THR B CB  1 
ATOM   6694  O  OG1 . THR B  1 398 ? 31.170  33.771  23.231  1.00 49.67  ? 398 THR B OG1 1 
ATOM   6695  C  CG2 . THR B  1 398 ? 33.415  34.424  23.850  1.00 46.44  ? 398 THR B CG2 1 
ATOM   6696  N  N   . HIS B  1 399 ? 29.536  32.960  25.911  1.00 53.65  ? 399 HIS B N   1 
ATOM   6697  C  CA  . HIS B  1 399 ? 28.216  33.245  26.465  1.00 53.43  ? 399 HIS B CA  1 
ATOM   6698  C  C   . HIS B  1 399 ? 27.533  32.167  27.293  1.00 50.18  ? 399 HIS B C   1 
ATOM   6699  O  O   . HIS B  1 399 ? 27.555  30.956  26.971  1.00 43.84  ? 399 HIS B O   1 
ATOM   6700  C  CB  . HIS B  1 399 ? 27.261  33.676  25.347  1.00 59.55  ? 399 HIS B CB  1 
ATOM   6701  C  CG  . HIS B  1 399 ? 27.662  34.942  24.659  1.00 57.72  ? 399 HIS B CG  1 
ATOM   6702  N  ND1 . HIS B  1 399 ? 26.972  36.129  24.819  1.00 53.61  ? 399 HIS B ND1 1 
ATOM   6703  C  CD2 . HIS B  1 399 ? 28.702  35.211  23.830  1.00 56.88  ? 399 HIS B CD2 1 
ATOM   6704  C  CE1 . HIS B  1 399 ? 27.576  37.073  24.117  1.00 58.20  ? 399 HIS B CE1 1 
ATOM   6705  N  NE2 . HIS B  1 399 ? 28.625  36.542  23.510  1.00 56.86  ? 399 HIS B NE2 1 
ATOM   6706  N  N   . ALA B  1 400 ? 26.852  32.662  28.312  1.00 45.09  ? 400 ALA B N   1 
ATOM   6707  C  CA  . ALA B  1 400 ? 26.098  31.839  29.211  1.00 43.46  ? 400 ALA B CA  1 
ATOM   6708  C  C   . ALA B  1 400 ? 25.004  32.758  29.692  1.00 41.58  ? 400 ALA B C   1 
ATOM   6709  O  O   . ALA B  1 400 ? 25.220  33.935  29.929  1.00 39.46  ? 400 ALA B O   1 
ATOM   6710  C  CB  . ALA B  1 400 ? 26.969  31.359  30.374  1.00 47.35  ? 400 ALA B CB  1 
ATOM   6711  N  N   . HIS B  1 401 ? 23.833  32.209  29.899  1.00 42.24  ? 401 HIS B N   1 
ATOM   6712  C  CA  . HIS B  1 401 ? 22.750  33.033  30.321  1.00 45.90  ? 401 HIS B CA  1 
ATOM   6713  C  C   . HIS B  1 401 ? 22.130  32.562  31.626  1.00 42.42  ? 401 HIS B C   1 
ATOM   6714  O  O   . HIS B  1 401 ? 21.681  31.422  31.723  1.00 42.65  ? 401 HIS B O   1 
ATOM   6715  C  CB  . HIS B  1 401 ? 21.739  33.028  29.192  1.00 56.86  ? 401 HIS B CB  1 
ATOM   6716  C  CG  . HIS B  1 401 ? 20.452  33.701  29.524  1.00 66.84  ? 401 HIS B CG  1 
ATOM   6717  N  ND1 . HIS B  1 401 ? 19.229  33.138  29.234  1.00 73.97  ? 401 HIS B ND1 1 
ATOM   6718  C  CD2 . HIS B  1 401 ? 20.193  34.890  30.118  1.00 71.48  ? 401 HIS B CD2 1 
ATOM   6719  C  CE1 . HIS B  1 401 ? 18.268  33.955  29.634  1.00 77.78  ? 401 HIS B CE1 1 
ATOM   6720  N  NE2 . HIS B  1 401 ? 18.827  35.025  30.173  1.00 73.84  ? 401 HIS B NE2 1 
ATOM   6721  N  N   . PHE B  1 402 ? 22.092  33.444  32.611  1.00 33.17  ? 402 PHE B N   1 
ATOM   6722  C  CA  . PHE B  1 402 ? 21.538  33.098  33.892  1.00 36.59  ? 402 PHE B CA  1 
ATOM   6723  C  C   . PHE B  1 402 ? 20.108  33.599  34.007  1.00 40.09  ? 402 PHE B C   1 
ATOM   6724  O  O   . PHE B  1 402 ? 19.808  34.674  33.537  1.00 45.30  ? 402 PHE B O   1 
ATOM   6725  C  CB  . PHE B  1 402 ? 22.402  33.679  35.010  1.00 37.48  ? 402 PHE B CB  1 
ATOM   6726  C  CG  . PHE B  1 402 ? 21.858  33.420  36.375  1.00 37.37  ? 402 PHE B CG  1 
ATOM   6727  C  CD1 . PHE B  1 402 ? 22.033  32.187  36.967  1.00 38.80  ? 402 PHE B CD1 1 
ATOM   6728  C  CD2 . PHE B  1 402 ? 21.130  34.388  37.039  1.00 36.65  ? 402 PHE B CD2 1 
ATOM   6729  C  CE1 . PHE B  1 402 ? 21.489  31.925  38.196  1.00 41.92  ? 402 PHE B CE1 1 
ATOM   6730  C  CE2 . PHE B  1 402 ? 20.574  34.141  38.283  1.00 40.46  ? 402 PHE B CE2 1 
ATOM   6731  C  CZ  . PHE B  1 402 ? 20.750  32.911  38.863  1.00 38.80  ? 402 PHE B CZ  1 
ATOM   6732  N  N   . SER B  1 403 ? 19.239  32.856  34.688  1.00 44.34  ? 403 SER B N   1 
ATOM   6733  C  CA  . SER B  1 403 ? 17.826  33.237  34.831  1.00 45.75  ? 403 SER B CA  1 
ATOM   6734  C  C   . SER B  1 403 ? 17.415  32.964  36.246  1.00 47.02  ? 403 SER B C   1 
ATOM   6735  O  O   . SER B  1 403 ? 18.015  32.122  36.879  1.00 53.96  ? 403 SER B O   1 
ATOM   6736  C  CB  . SER B  1 403 ? 16.955  32.362  33.931  1.00 44.03  ? 403 SER B CB  1 
ATOM   6737  O  OG  . SER B  1 403 ? 17.729  31.737  32.901  1.00 49.08  ? 403 SER B OG  1 
ATOM   6738  N  N   . TRP B  1 404 ? 16.409  33.665  36.743  1.00 46.17  ? 404 TRP B N   1 
ATOM   6739  C  CA  . TRP B  1 404 ? 15.907  33.457  38.095  1.00 49.55  ? 404 TRP B CA  1 
ATOM   6740  C  C   . TRP B  1 404 ? 14.407  33.408  37.948  1.00 54.35  ? 404 TRP B C   1 
ATOM   6741  O  O   . TRP B  1 404 ? 13.796  34.420  37.644  1.00 59.37  ? 404 TRP B O   1 
ATOM   6742  C  CB  . TRP B  1 404 ? 16.228  34.629  39.036  1.00 49.04  ? 404 TRP B CB  1 
ATOM   6743  C  CG  . TRP B  1 404 ? 15.642  34.457  40.438  1.00 48.13  ? 404 TRP B CG  1 
ATOM   6744  C  CD1 . TRP B  1 404 ? 15.814  33.384  41.251  1.00 52.94  ? 404 TRP B CD1 1 
ATOM   6745  C  CD2 . TRP B  1 404 ? 14.845  35.388  41.187  1.00 47.43  ? 404 TRP B CD2 1 
ATOM   6746  N  NE1 . TRP B  1 404 ? 15.187  33.584  42.457  1.00 54.08  ? 404 TRP B NE1 1 
ATOM   6747  C  CE2 . TRP B  1 404 ? 14.588  34.806  42.442  1.00 47.75  ? 404 TRP B CE2 1 
ATOM   6748  C  CE3 . TRP B  1 404 ? 14.333  36.652  40.925  1.00 48.36  ? 404 TRP B CE3 1 
ATOM   6749  C  CZ2 . TRP B  1 404 ? 13.844  35.438  43.424  1.00 48.93  ? 404 TRP B CZ2 1 
ATOM   6750  C  CZ3 . TRP B  1 404 ? 13.586  37.289  41.915  1.00 43.66  ? 404 TRP B CZ3 1 
ATOM   6751  C  CH2 . TRP B  1 404 ? 13.352  36.677  43.144  1.00 47.72  ? 404 TRP B CH2 1 
ATOM   6752  N  N   . ASN B  1 405 ? 13.804  32.247  38.153  1.00 54.39  ? 405 ASN B N   1 
ATOM   6753  C  CA  . ASN B  1 405 ? 12.349  32.114  38.053  1.00 53.66  ? 405 ASN B CA  1 
ATOM   6754  C  C   . ASN B  1 405 ? 11.620  32.164  39.418  1.00 50.97  ? 405 ASN B C   1 
ATOM   6755  O  O   . ASN B  1 405 ? 11.774  31.261  40.224  1.00 52.31  ? 405 ASN B O   1 
ATOM   6756  C  CB  . ASN B  1 405 ? 12.007  30.816  37.340  1.00 54.29  ? 405 ASN B CB  1 
ATOM   6757  C  CG  . ASN B  1 405 ? 10.543  30.473  37.452  1.00 54.78  ? 405 ASN B CG  1 
ATOM   6758  O  OD1 . ASN B  1 405 ? 10.119  29.758  38.349  1.00 57.18  ? 405 ASN B OD1 1 
ATOM   6759  N  ND2 . ASN B  1 405 ? 9.762   31.018  36.567  1.00 56.65  ? 405 ASN B ND2 1 
ATOM   6760  N  N   . ARG B  1 406 ? 10.813  33.189  39.675  1.00 50.10  ? 406 ARG B N   1 
ATOM   6761  C  CA  . ARG B  1 406 ? 10.122  33.243  40.959  1.00 49.45  ? 406 ARG B CA  1 
ATOM   6762  C  C   . ARG B  1 406 ? 9.035   32.193  41.053  1.00 51.79  ? 406 ARG B C   1 
ATOM   6763  O  O   . ARG B  1 406 ? 8.530   31.687  40.043  1.00 45.97  ? 406 ARG B O   1 
ATOM   6764  C  CB  . ARG B  1 406 ? 9.541   34.601  41.221  1.00 44.48  ? 406 ARG B CB  1 
ATOM   6765  C  CG  . ARG B  1 406 ? 10.583  35.625  41.266  1.00 52.70  ? 406 ARG B CG  1 
ATOM   6766  C  CD  . ARG B  1 406 ? 10.007  36.901  41.743  1.00 60.60  ? 406 ARG B CD  1 
ATOM   6767  N  NE  . ARG B  1 406 ? 8.848   37.256  40.927  1.00 68.15  ? 406 ARG B NE  1 
ATOM   6768  C  CZ  . ARG B  1 406 ? 7.948   38.181  41.250  1.00 66.36  ? 406 ARG B CZ  1 
ATOM   6769  N  NH1 . ARG B  1 406 ? 8.054   38.884  42.377  1.00 56.92  ? 406 ARG B NH1 1 
ATOM   6770  N  NH2 . ARG B  1 406 ? 6.906   38.366  40.457  1.00 66.42  ? 406 ARG B NH2 1 
ATOM   6771  N  N   . ASN B  1 407 ? 8.694   31.833  42.277  1.00 56.48  ? 407 ASN B N   1 
ATOM   6772  C  CA  . ASN B  1 407 ? 7.690   30.819  42.468  1.00 62.68  ? 407 ASN B CA  1 
ATOM   6773  C  C   . ASN B  1 407 ? 6.350   31.359  42.120  1.00 65.17  ? 407 ASN B C   1 
ATOM   6774  O  O   . ASN B  1 407 ? 5.523   30.616  41.620  1.00 68.75  ? 407 ASN B O   1 
ATOM   6775  C  CB  . ASN B  1 407 ? 7.699   30.270  43.892  1.00 69.18  ? 407 ASN B CB  1 
ATOM   6776  C  CG  . ASN B  1 407 ? 8.629   29.044  44.053  1.00 75.56  ? 407 ASN B CG  1 
ATOM   6777  O  OD1 . ASN B  1 407 ? 9.402   28.681  43.135  1.00 77.66  ? 407 ASN B OD1 1 
ATOM   6778  N  ND2 . ASN B  1 407 ? 8.540   28.391  45.219  1.00 76.18  ? 407 ASN B ND2 1 
ATOM   6779  N  N   . GLN B  1 408 ? 6.150   32.659  42.335  1.00 67.96  ? 408 GLN B N   1 
ATOM   6780  C  CA  . GLN B  1 408 ? 4.870   33.326  42.038  1.00 67.63  ? 408 GLN B CA  1 
ATOM   6781  C  C   . GLN B  1 408 ? 4.591   33.472  40.553  1.00 66.39  ? 408 GLN B C   1 
ATOM   6782  O  O   . GLN B  1 408 ? 3.460   33.647  40.146  1.00 68.52  ? 408 GLN B O   1 
ATOM   6783  C  CB  . GLN B  1 408 ? 4.813   34.741  42.606  1.00 68.82  ? 408 GLN B CB  1 
ATOM   6784  C  CG  . GLN B  1 408 ? 5.383   34.911  43.972  1.00 78.37  ? 408 GLN B CG  1 
ATOM   6785  C  CD  . GLN B  1 408 ? 6.831   35.318  43.922  1.00 82.28  ? 408 GLN B CD  1 
ATOM   6786  O  OE1 . GLN B  1 408 ? 7.725   34.472  43.853  1.00 89.33  ? 408 GLN B OE1 1 
ATOM   6787  N  NE2 . GLN B  1 408 ? 7.078   36.616  43.918  1.00 82.03  ? 408 GLN B NE2 1 
ATOM   6788  N  N   . ASP B  1 409 ? 5.637   33.550  39.758  1.00 64.95  ? 409 ASP B N   1 
ATOM   6789  C  CA  . ASP B  1 409 ? 5.470   33.704  38.329  1.00 63.29  ? 409 ASP B CA  1 
ATOM   6790  C  C   . ASP B  1 409 ? 5.166   32.347  37.779  1.00 64.75  ? 409 ASP B C   1 
ATOM   6791  O  O   . ASP B  1 409 ? 5.197   31.343  38.489  1.00 64.10  ? 409 ASP B O   1 
ATOM   6792  C  CB  . ASP B  1 409 ? 6.755   34.218  37.680  1.00 67.25  ? 409 ASP B CB  1 
ATOM   6793  C  CG  . ASP B  1 409 ? 7.326   35.462  38.388  1.00 75.97  ? 409 ASP B CG  1 
ATOM   6794  O  OD1 . ASP B  1 409 ? 6.507   36.208  39.002  1.00 73.89  ? 409 ASP B OD1 1 
ATOM   6795  O  OD2 . ASP B  1 409 ? 8.589   35.669  38.341  1.00 76.55  ? 409 ASP B OD2 1 
ATOM   6796  N  N   . GLY B  1 410 ? 4.871   32.312  36.493  1.00 66.71  ? 410 GLY B N   1 
ATOM   6797  C  CA  . GLY B  1 410 ? 4.572   31.048  35.869  1.00 62.84  ? 410 GLY B CA  1 
ATOM   6798  C  C   . GLY B  1 410 ? 5.896   30.446  35.554  1.00 59.91  ? 410 GLY B C   1 
ATOM   6799  O  O   . GLY B  1 410 ? 6.909   31.131  35.493  1.00 58.40  ? 410 GLY B O   1 
ATOM   6800  N  N   . VAL B  1 411 ? 5.854   29.167  35.272  1.00 60.11  ? 411 VAL B N   1 
ATOM   6801  C  CA  . VAL B  1 411 ? 7.026   28.397  34.944  1.00 62.55  ? 411 VAL B CA  1 
ATOM   6802  C  C   . VAL B  1 411 ? 8.021   29.007  33.978  1.00 64.58  ? 411 VAL B C   1 
ATOM   6803  O  O   . VAL B  1 411 ? 9.231   28.767  34.083  1.00 70.00  ? 411 VAL B O   1 
ATOM   6804  C  CB  . VAL B  1 411 ? 6.582   27.041  34.420  1.00 61.57  ? 411 VAL B CB  1 
ATOM   6805  C  CG1 . VAL B  1 411 ? 7.677   26.358  33.602  1.00 61.81  ? 411 VAL B CG1 1 
ATOM   6806  C  CG2 . VAL B  1 411 ? 6.166   26.198  35.606  1.00 63.51  ? 411 VAL B CG2 1 
ATOM   6807  N  N   . ALA B  1 412 ? 7.529   29.793  33.035  1.00 65.05  ? 412 ALA B N   1 
ATOM   6808  C  CA  . ALA B  1 412 ? 8.435   30.372  32.060  1.00 63.98  ? 412 ALA B CA  1 
ATOM   6809  C  C   . ALA B  1 412 ? 8.821   31.829  32.269  1.00 62.64  ? 412 ALA B C   1 
ATOM   6810  O  O   . ALA B  1 412 ? 9.554   32.390  31.469  1.00 64.05  ? 412 ALA B O   1 
ATOM   6811  C  CB  . ALA B  1 412 ? 7.886   30.164  30.678  1.00 68.01  ? 412 ALA B CB  1 
ATOM   6812  N  N   . VAL B  1 413 ? 8.393   32.420  33.370  1.00 61.44  ? 413 VAL B N   1 
ATOM   6813  C  CA  . VAL B  1 413 ? 8.706   33.808  33.628  1.00 65.01  ? 413 VAL B CA  1 
ATOM   6814  C  C   . VAL B  1 413 ? 10.017  34.076  34.377  1.00 65.99  ? 413 VAL B C   1 
ATOM   6815  O  O   . VAL B  1 413 ? 10.112  33.908  35.612  1.00 67.36  ? 413 VAL B O   1 
ATOM   6816  C  CB  . VAL B  1 413 ? 7.568   34.455  34.379  1.00 69.72  ? 413 VAL B CB  1 
ATOM   6817  C  CG1 . VAL B  1 413 ? 7.864   35.939  34.645  1.00 72.48  ? 413 VAL B CG1 1 
ATOM   6818  C  CG2 . VAL B  1 413 ? 6.285   34.274  33.588  1.00 77.53  ? 413 VAL B CG2 1 
ATOM   6819  N  N   . GLU B  1 414 ? 11.008  34.559  33.637  1.00 60.81  ? 414 GLU B N   1 
ATOM   6820  C  CA  . GLU B  1 414 ? 12.287  34.861  34.223  1.00 56.59  ? 414 GLU B CA  1 
ATOM   6821  C  C   . GLU B  1 414 ? 12.210  36.211  34.903  1.00 53.82  ? 414 GLU B C   1 
ATOM   6822  O  O   . GLU B  1 414 ? 12.354  37.206  34.244  1.00 56.88  ? 414 GLU B O   1 
ATOM   6823  C  CB  . GLU B  1 414 ? 13.346  34.917  33.135  1.00 59.56  ? 414 GLU B CB  1 
ATOM   6824  C  CG  . GLU B  1 414 ? 13.477  33.661  32.269  1.00 65.06  ? 414 GLU B CG  1 
ATOM   6825  C  CD  . GLU B  1 414 ? 14.577  33.798  31.189  1.00 69.46  ? 414 GLU B CD  1 
ATOM   6826  O  OE1 . GLU B  1 414 ? 15.329  34.814  31.200  1.00 74.54  ? 414 GLU B OE1 1 
ATOM   6827  O  OE2 . GLU B  1 414 ? 14.702  32.883  30.330  1.00 67.81  ? 414 GLU B OE2 1 
ATOM   6828  N  N   . ALA B  1 415 ? 11.984  36.261  36.211  1.00 51.66  ? 415 ALA B N   1 
ATOM   6829  C  CA  . ALA B  1 415 ? 11.920  37.537  36.922  1.00 48.26  ? 415 ALA B CA  1 
ATOM   6830  C  C   . ALA B  1 415 ? 13.288  38.268  36.961  1.00 51.74  ? 415 ALA B C   1 
ATOM   6831  O  O   . ALA B  1 415 ? 13.406  39.384  37.506  1.00 55.25  ? 415 ALA B O   1 
ATOM   6832  C  CB  . ALA B  1 415 ? 11.373  37.332  38.319  1.00 49.13  ? 415 ALA B CB  1 
ATOM   6833  N  N   . ASP B  1 416 ? 14.333  37.635  36.438  1.00 47.23  ? 416 ASP B N   1 
ATOM   6834  C  CA  . ASP B  1 416 ? 15.634  38.274  36.380  1.00 45.71  ? 416 ASP B CA  1 
ATOM   6835  C  C   . ASP B  1 416 ? 16.343  37.498  35.314  1.00 42.13  ? 416 ASP B C   1 
ATOM   6836  O  O   . ASP B  1 416 ? 16.097  36.317  35.143  1.00 41.31  ? 416 ASP B O   1 
ATOM   6837  C  CB  . ASP B  1 416 ? 16.373  38.203  37.704  1.00 46.66  ? 416 ASP B CB  1 
ATOM   6838  C  CG  . ASP B  1 416 ? 17.585  39.102  37.733  1.00 52.79  ? 416 ASP B CG  1 
ATOM   6839  O  OD1 . ASP B  1 416 ? 18.213  39.330  36.670  1.00 55.85  ? 416 ASP B OD1 1 
ATOM   6840  O  OD2 . ASP B  1 416 ? 17.909  39.603  38.824  1.00 53.26  ? 416 ASP B OD2 1 
ATOM   6841  N  N   . SER B  1 417 ? 17.203  38.163  34.574  1.00 41.38  ? 417 SER B N   1 
ATOM   6842  C  CA  . SER B  1 417 ? 17.901  37.512  33.488  1.00 45.41  ? 417 SER B CA  1 
ATOM   6843  C  C   . SER B  1 417 ? 19.144  38.342  33.223  1.00 47.36  ? 417 SER B C   1 
ATOM   6844  O  O   . SER B  1 417 ? 19.089  39.579  33.323  1.00 52.44  ? 417 SER B O   1 
ATOM   6845  C  CB  . SER B  1 417 ? 16.983  37.471  32.271  1.00 44.39  ? 417 SER B CB  1 
ATOM   6846  O  OG  . SER B  1 417 ? 17.720  37.533  31.066  1.00 50.45  ? 417 SER B OG  1 
ATOM   6847  N  N   . VAL B  1 418 ? 20.244  37.675  32.864  1.00 44.79  ? 418 VAL B N   1 
ATOM   6848  C  CA  . VAL B  1 418 ? 21.525  38.326  32.650  1.00 41.68  ? 418 VAL B CA  1 
ATOM   6849  C  C   . VAL B  1 418 ? 22.415  37.493  31.747  1.00 40.19  ? 418 VAL B C   1 
ATOM   6850  O  O   . VAL B  1 418 ? 22.419  36.260  31.829  1.00 39.74  ? 418 VAL B O   1 
ATOM   6851  C  CB  . VAL B  1 418 ? 22.279  38.411  33.995  1.00 45.86  ? 418 VAL B CB  1 
ATOM   6852  C  CG1 . VAL B  1 418 ? 23.614  39.045  33.792  1.00 53.25  ? 418 VAL B CG1 1 
ATOM   6853  C  CG2 . VAL B  1 418 ? 21.494  39.166  35.040  1.00 43.90  ? 418 VAL B CG2 1 
ATOM   6854  N  N   . TRP B  1 419 ? 23.171  38.139  30.876  1.00 39.90  ? 419 TRP B N   1 
ATOM   6855  C  CA  . TRP B  1 419 ? 24.078  37.364  30.045  1.00 45.70  ? 419 TRP B CA  1 
ATOM   6856  C  C   . TRP B  1 419 ? 25.429  37.444  30.699  1.00 48.17  ? 419 TRP B C   1 
ATOM   6857  O  O   . TRP B  1 419 ? 25.786  38.494  31.212  1.00 55.71  ? 419 TRP B O   1 
ATOM   6858  C  CB  . TRP B  1 419 ? 24.159  37.909  28.636  1.00 45.09  ? 419 TRP B CB  1 
ATOM   6859  C  CG  . TRP B  1 419 ? 23.103  37.382  27.816  1.00 49.91  ? 419 TRP B CG  1 
ATOM   6860  C  CD1 . TRP B  1 419 ? 21.877  37.919  27.651  1.00 51.91  ? 419 TRP B CD1 1 
ATOM   6861  C  CD2 . TRP B  1 419 ? 23.113  36.145  27.089  1.00 53.33  ? 419 TRP B CD2 1 
ATOM   6862  N  NE1 . TRP B  1 419 ? 21.103  37.096  26.866  1.00 60.82  ? 419 TRP B NE1 1 
ATOM   6863  C  CE2 . TRP B  1 419 ? 21.838  35.997  26.504  1.00 55.48  ? 419 TRP B CE2 1 
ATOM   6864  C  CE3 . TRP B  1 419 ? 24.071  35.143  26.884  1.00 51.76  ? 419 TRP B CE3 1 
ATOM   6865  C  CZ2 . TRP B  1 419 ? 21.485  34.885  25.721  1.00 55.91  ? 419 TRP B CZ2 1 
ATOM   6866  C  CZ3 . TRP B  1 419 ? 23.719  34.037  26.109  1.00 52.13  ? 419 TRP B CZ3 1 
ATOM   6867  C  CH2 . TRP B  1 419 ? 22.434  33.919  25.535  1.00 53.31  ? 419 TRP B CH2 1 
ATOM   6868  N  N   . PHE B  1 420 ? 26.156  36.338  30.739  1.00 44.91  ? 420 PHE B N   1 
ATOM   6869  C  CA  . PHE B  1 420 ? 27.464  36.328  31.337  1.00 40.20  ? 420 PHE B CA  1 
ATOM   6870  C  C   . PHE B  1 420 ? 28.462  36.297  30.188  1.00 42.15  ? 420 PHE B C   1 
ATOM   6871  O  O   . PHE B  1 420 ? 28.306  35.534  29.223  1.00 41.23  ? 420 PHE B O   1 
ATOM   6872  C  CB  . PHE B  1 420 ? 27.631  35.074  32.201  1.00 43.21  ? 420 PHE B CB  1 
ATOM   6873  C  CG  . PHE B  1 420 ? 27.147  35.225  33.628  1.00 45.02  ? 420 PHE B CG  1 
ATOM   6874  C  CD1 . PHE B  1 420 ? 25.794  35.214  33.919  1.00 47.83  ? 420 PHE B CD1 1 
ATOM   6875  C  CD2 . PHE B  1 420 ? 28.056  35.409  34.687  1.00 48.79  ? 420 PHE B CD2 1 
ATOM   6876  C  CE1 . PHE B  1 420 ? 25.335  35.391  35.252  1.00 47.30  ? 420 PHE B CE1 1 
ATOM   6877  C  CE2 . PHE B  1 420 ? 27.607  35.589  36.024  1.00 45.61  ? 420 PHE B CE2 1 
ATOM   6878  C  CZ  . PHE B  1 420 ? 26.245  35.582  36.299  1.00 43.76  ? 420 PHE B CZ  1 
ATOM   6879  N  N   . PHE B  1 421 ? 29.457  37.167  30.256  1.00 42.79  ? 421 PHE B N   1 
ATOM   6880  C  CA  . PHE B  1 421 ? 30.484  37.202  29.227  1.00 43.16  ? 421 PHE B CA  1 
ATOM   6881  C  C   . PHE B  1 421 ? 31.669  36.597  29.911  1.00 43.60  ? 421 PHE B C   1 
ATOM   6882  O  O   . PHE B  1 421 ? 32.095  37.025  31.003  1.00 39.60  ? 421 PHE B O   1 
ATOM   6883  C  CB  . PHE B  1 421 ? 30.754  38.631  28.792  1.00 47.29  ? 421 PHE B CB  1 
ATOM   6884  C  CG  . PHE B  1 421 ? 29.596  39.249  28.089  1.00 45.76  ? 421 PHE B CG  1 
ATOM   6885  C  CD1 . PHE B  1 421 ? 28.824  38.475  27.219  1.00 43.40  ? 421 PHE B CD1 1 
ATOM   6886  C  CD2 . PHE B  1 421 ? 29.241  40.573  28.317  1.00 45.30  ? 421 PHE B CD2 1 
ATOM   6887  C  CE1 . PHE B  1 421 ? 27.716  39.000  26.585  1.00 40.87  ? 421 PHE B CE1 1 
ATOM   6888  C  CE2 . PHE B  1 421 ? 28.140  41.118  27.693  1.00 41.63  ? 421 PHE B CE2 1 
ATOM   6889  C  CZ  . PHE B  1 421 ? 27.374  40.327  26.824  1.00 48.97  ? 421 PHE B CZ  1 
ATOM   6890  N  N   . ASN B  1 422 ? 32.156  35.535  29.304  1.00 42.72  ? 422 ASN B N   1 
ATOM   6891  C  CA  . ASN B  1 422 ? 33.248  34.796  29.891  1.00 44.29  ? 422 ASN B CA  1 
ATOM   6892  C  C   . ASN B  1 422 ? 34.460  35.616  30.290  1.00 45.21  ? 422 ASN B C   1 
ATOM   6893  O  O   . ASN B  1 422 ? 35.124  36.175  29.421  1.00 51.79  ? 422 ASN B O   1 
ATOM   6894  C  CB  . ASN B  1 422 ? 33.662  33.701  28.949  1.00 45.61  ? 422 ASN B CB  1 
ATOM   6895  C  CG  . ASN B  1 422 ? 34.694  32.825  29.543  1.00 50.06  ? 422 ASN B CG  1 
ATOM   6896  O  OD1 . ASN B  1 422 ? 35.872  33.153  29.535  1.00 52.87  ? 422 ASN B OD1 1 
ATOM   6897  N  ND2 . ASN B  1 422 ? 34.266  31.723  30.116  1.00 52.13  ? 422 ASN B ND2 1 
ATOM   6898  N  N   . ARG B  1 423 ? 34.794  35.628  31.582  1.00 41.67  ? 423 ARG B N   1 
ATOM   6899  C  CA  . ARG B  1 423 ? 35.957  36.377  32.085  1.00 38.39  ? 423 ARG B CA  1 
ATOM   6900  C  C   . ARG B  1 423 ? 37.278  36.044  31.421  1.00 39.48  ? 423 ARG B C   1 
ATOM   6901  O  O   . ARG B  1 423 ? 38.279  36.746  31.619  1.00 41.56  ? 423 ARG B O   1 
ATOM   6902  C  CB  . ARG B  1 423 ? 36.150  36.180  33.573  1.00 31.39  ? 423 ARG B CB  1 
ATOM   6903  C  CG  . ARG B  1 423 ? 35.123  36.839  34.435  1.00 29.57  ? 423 ARG B CG  1 
ATOM   6904  C  CD  . ARG B  1 423 ? 34.992  38.303  34.146  1.00 30.45  ? 423 ARG B CD  1 
ATOM   6905  N  NE  . ARG B  1 423 ? 34.116  38.534  33.014  1.00 37.06  ? 423 ARG B NE  1 
ATOM   6906  C  CZ  . ARG B  1 423 ? 33.727  39.736  32.610  1.00 41.44  ? 423 ARG B CZ  1 
ATOM   6907  N  NH1 . ARG B  1 423 ? 34.141  40.822  33.244  1.00 38.85  ? 423 ARG B NH1 1 
ATOM   6908  N  NH2 . ARG B  1 423 ? 32.907  39.847  31.572  1.00 46.96  ? 423 ARG B NH2 1 
ATOM   6909  N  N   . HIS B  1 424 ? 37.307  34.939  30.701  1.00 37.77  ? 424 HIS B N   1 
ATOM   6910  C  CA  . HIS B  1 424 ? 38.508  34.565  30.024  1.00 37.64  ? 424 HIS B CA  1 
ATOM   6911  C  C   . HIS B  1 424 ? 38.434  34.807  28.564  1.00 41.34  ? 424 HIS B C   1 
ATOM   6912  O  O   . HIS B  1 424 ? 39.454  35.067  27.983  1.00 52.54  ? 424 HIS B O   1 
ATOM   6913  C  CB  . HIS B  1 424 ? 38.818  33.118  30.224  1.00 36.98  ? 424 HIS B CB  1 
ATOM   6914  C  CG  . HIS B  1 424 ? 40.048  32.679  29.519  1.00 37.42  ? 424 HIS B CG  1 
ATOM   6915  N  ND1 . HIS B  1 424 ? 41.307  32.871  30.044  1.00 39.51  ? 424 HIS B ND1 1 
ATOM   6916  C  CD2 . HIS B  1 424 ? 40.227  32.079  28.319  1.00 45.35  ? 424 HIS B CD2 1 
ATOM   6917  C  CE1 . HIS B  1 424 ? 42.213  32.408  29.200  1.00 40.35  ? 424 HIS B CE1 1 
ATOM   6918  N  NE2 . HIS B  1 424 ? 41.585  31.922  28.143  1.00 49.29  ? 424 HIS B NE2 1 
ATOM   6919  N  N   . TRP B  1 425 ? 37.283  34.646  27.929  1.00 38.05  ? 425 TRP B N   1 
ATOM   6920  C  CA  . TRP B  1 425 ? 37.230  34.882  26.498  1.00 33.29  ? 425 TRP B CA  1 
ATOM   6921  C  C   . TRP B  1 425 ? 36.278  36.013  26.142  1.00 35.01  ? 425 TRP B C   1 
ATOM   6922  O  O   . TRP B  1 425 ? 35.867  36.163  24.995  1.00 39.63  ? 425 TRP B O   1 
ATOM   6923  C  CB  . TRP B  1 425 ? 36.707  33.670  25.773  1.00 32.31  ? 425 TRP B CB  1 
ATOM   6924  C  CG  . TRP B  1 425 ? 37.268  32.444  26.114  1.00 31.74  ? 425 TRP B CG  1 
ATOM   6925  C  CD1 . TRP B  1 425 ? 36.986  31.701  27.189  1.00 35.74  ? 425 TRP B CD1 1 
ATOM   6926  C  CD2 . TRP B  1 425 ? 38.200  31.721  25.347  1.00 35.15  ? 425 TRP B CD2 1 
ATOM   6927  N  NE1 . TRP B  1 425 ? 37.695  30.533  27.153  1.00 37.95  ? 425 TRP B NE1 1 
ATOM   6928  C  CE2 . TRP B  1 425 ? 38.453  30.526  26.022  1.00 33.61  ? 425 TRP B CE2 1 
ATOM   6929  C  CE3 . TRP B  1 425 ? 38.853  31.970  24.149  1.00 39.81  ? 425 TRP B CE3 1 
ATOM   6930  C  CZ2 . TRP B  1 425 ? 39.330  29.579  25.550  1.00 35.45  ? 425 TRP B CZ2 1 
ATOM   6931  C  CZ3 . TRP B  1 425 ? 39.736  31.019  23.675  1.00 40.41  ? 425 TRP B CZ3 1 
ATOM   6932  C  CH2 . TRP B  1 425 ? 39.966  29.841  24.376  1.00 37.23  ? 425 TRP B CH2 1 
ATOM   6933  N  N   . TYR B  1 426 ? 35.876  36.817  27.081  1.00 31.24  ? 426 TYR B N   1 
ATOM   6934  C  CA  . TYR B  1 426 ? 34.950  37.800  26.656  1.00 32.12  ? 426 TYR B CA  1 
ATOM   6935  C  C   . TYR B  1 426 ? 34.766  38.778  27.754  1.00 39.31  ? 426 TYR B C   1 
ATOM   6936  O  O   . TYR B  1 426 ? 33.649  39.088  28.145  1.00 46.54  ? 426 TYR B O   1 
ATOM   6937  C  CB  . TYR B  1 426 ? 33.667  37.088  26.351  1.00 34.50  ? 426 TYR B CB  1 
ATOM   6938  C  CG  . TYR B  1 426 ? 32.885  37.871  25.410  1.00 40.64  ? 426 TYR B CG  1 
ATOM   6939  C  CD1 . TYR B  1 426 ? 33.477  38.362  24.266  1.00 41.10  ? 426 TYR B CD1 1 
ATOM   6940  C  CD2 . TYR B  1 426 ? 31.603  38.267  25.723  1.00 42.99  ? 426 TYR B CD2 1 
ATOM   6941  C  CE1 . TYR B  1 426 ? 32.813  39.261  23.446  1.00 45.27  ? 426 TYR B CE1 1 
ATOM   6942  C  CE2 . TYR B  1 426 ? 30.922  39.166  24.924  1.00 48.47  ? 426 TYR B CE2 1 
ATOM   6943  C  CZ  . TYR B  1 426 ? 31.536  39.674  23.779  1.00 48.52  ? 426 TYR B CZ  1 
ATOM   6944  O  OH  . TYR B  1 426 ? 30.888  40.635  23.011  1.00 53.92  ? 426 TYR B OH  1 
ATOM   6945  N  N   . PRO B  1 427 ? 35.873  39.353  28.224  1.00 40.86  ? 427 PRO B N   1 
ATOM   6946  C  CA  . PRO B  1 427 ? 35.963  40.332  29.309  1.00 41.65  ? 427 PRO B CA  1 
ATOM   6947  C  C   . PRO B  1 427 ? 35.157  41.608  29.197  1.00 45.62  ? 427 PRO B C   1 
ATOM   6948  O  O   . PRO B  1 427 ? 35.335  42.513  30.019  1.00 46.76  ? 427 PRO B O   1 
ATOM   6949  C  CB  . PRO B  1 427 ? 37.455  40.654  29.348  1.00 44.36  ? 427 PRO B CB  1 
ATOM   6950  C  CG  . PRO B  1 427 ? 38.113  39.409  28.782  1.00 43.13  ? 427 PRO B CG  1 
ATOM   6951  C  CD  . PRO B  1 427 ? 37.202  39.120  27.629  1.00 41.68  ? 427 PRO B CD  1 
ATOM   6952  N  N   . VAL B  1 428 ? 34.288  41.718  28.198  1.00 50.14  ? 428 VAL B N   1 
ATOM   6953  C  CA  . VAL B  1 428 ? 33.532  42.953  28.078  1.00 55.36  ? 428 VAL B CA  1 
ATOM   6954  C  C   . VAL B  1 428 ? 32.577  43.022  29.204  1.00 59.55  ? 428 VAL B C   1 
ATOM   6955  O  O   . VAL B  1 428 ? 32.091  42.012  29.676  1.00 56.21  ? 428 VAL B O   1 
ATOM   6956  C  CB  . VAL B  1 428 ? 32.730  43.115  26.787  1.00 52.30  ? 428 VAL B CB  1 
ATOM   6957  C  CG1 . VAL B  1 428 ? 33.586  42.813  25.587  1.00 51.30  ? 428 VAL B CG1 1 
ATOM   6958  C  CG2 . VAL B  1 428 ? 31.489  42.286  26.846  1.00 53.12  ? 428 VAL B CG2 1 
ATOM   6959  N  N   . ASP B  1 429 ? 32.323  44.251  29.597  1.00 70.45  ? 429 ASP B N   1 
ATOM   6960  C  CA  . ASP B  1 429 ? 31.435  44.567  30.688  1.00 81.28  ? 429 ASP B CA  1 
ATOM   6961  C  C   . ASP B  1 429 ? 30.060  43.941  30.596  1.00 88.93  ? 429 ASP B C   1 
ATOM   6962  O  O   . ASP B  1 429 ? 29.266  44.274  29.699  1.00 90.36  ? 429 ASP B O   1 
ATOM   6963  C  CB  . ASP B  1 429 ? 31.307  46.086  30.870  1.00 83.11  ? 429 ASP B CB  1 
ATOM   6964  C  CG  . ASP B  1 429 ? 30.571  46.474  32.175  1.00 83.81  ? 429 ASP B CG  1 
ATOM   6965  O  OD1 . ASP B  1 429 ? 29.353  46.221  32.286  1.00 83.39  ? 429 ASP B OD1 1 
ATOM   6966  O  OD2 . ASP B  1 429 ? 31.206  47.051  33.087  1.00 87.23  ? 429 ASP B OD2 1 
ATOM   6967  N  N   . ASP B  1 430 ? 29.821  43.112  31.631  1.00 97.36  ? 430 ASP B N   1 
ATOM   6968  C  CA  . ASP B  1 430 ? 28.611  42.330  31.948  1.00 100.34 ? 430 ASP B CA  1 
ATOM   6969  C  C   . ASP B  1 430 ? 27.741  43.247  32.794  1.00 104.50 ? 430 ASP B C   1 
ATOM   6970  O  O   . ASP B  1 430 ? 26.624  43.619  32.422  1.00 102.99 ? 430 ASP B O   1 
ATOM   6971  C  CB  . ASP B  1 430 ? 28.972  41.150  32.887  1.00 97.55  ? 430 ASP B CB  1 
ATOM   6972  C  CG  . ASP B  1 430 ? 29.382  39.897  32.158  1.00 95.16  ? 430 ASP B CG  1 
ATOM   6973  O  OD1 . ASP B  1 430 ? 28.796  39.591  31.114  1.00 93.72  ? 430 ASP B OD1 1 
ATOM   6974  O  OD2 . ASP B  1 430 ? 30.268  39.185  32.654  1.00 93.52  ? 430 ASP B OD2 1 
ATOM   6975  N  N   . SER B  1 431 ? 28.282  43.524  33.984  1.00 109.97 ? 431 SER B N   1 
ATOM   6976  C  CA  . SER B  1 431 ? 27.689  44.365  35.016  1.00 112.72 ? 431 SER B CA  1 
ATOM   6977  C  C   . SER B  1 431 ? 26.516  45.258  34.569  1.00 113.34 ? 431 SER B C   1 
ATOM   6978  O  O   . SER B  1 431 ? 26.682  46.206  33.798  1.00 112.08 ? 431 SER B O   1 
ATOM   6979  C  CB  . SER B  1 431 ? 28.809  45.171  35.698  1.00 112.50 ? 431 SER B CB  1 
ATOM   6980  O  OG  . SER B  1 431 ? 29.720  44.302  36.373  1.00 108.35 ? 431 SER B OG  1 
ATOM   6981  N  N   . THR B  1 432 ? 25.326  44.888  35.032  1.00 114.86 ? 432 THR B N   1 
ATOM   6982  C  CA  . THR B  1 432 ? 24.099  45.603  34.722  1.00 116.96 ? 432 THR B CA  1 
ATOM   6983  C  C   . THR B  1 432 ? 23.600  46.297  35.992  1.00 119.15 ? 432 THR B C   1 
ATOM   6984  O  O   . THR B  1 432 ? 23.587  47.554  36.015  1.00 120.64 ? 432 THR B O   1 
ATOM   6985  C  CB  . THR B  1 432 ? 23.023  44.624  34.196  1.00 115.60 ? 432 THR B CB  1 
ATOM   6986  O  OG1 . THR B  1 432 ? 23.393  44.162  32.891  1.00 117.75 ? 432 THR B OG1 1 
ATOM   6987  C  CG2 . THR B  1 432 ? 21.663  45.290  34.122  1.00 115.31 ? 432 THR B CG2 1 
ATOM   6988  O  OXT . THR B  1 432 ? 23.262  45.567  36.956  1.00 118.74 ? 432 THR B OXT 1 
ATOM   6989  N  N   . ARG C  1 9   ? 70.423  25.717  61.469  1.00 48.32  ? 9   ARG C N   1 
ATOM   6990  C  CA  . ARG C  1 9   ? 71.151  25.999  62.764  1.00 44.68  ? 9   ARG C CA  1 
ATOM   6991  C  C   . ARG C  1 9   ? 70.594  25.052  63.818  1.00 42.19  ? 9   ARG C C   1 
ATOM   6992  O  O   . ARG C  1 9   ? 70.598  25.345  65.022  1.00 38.72  ? 9   ARG C O   1 
ATOM   6993  C  CB  . ARG C  1 9   ? 70.904  27.446  63.235  1.00 47.03  ? 9   ARG C CB  1 
ATOM   6994  C  CG  . ARG C  1 9   ? 71.400  28.555  62.291  1.00 53.72  ? 9   ARG C CG  1 
ATOM   6995  C  CD  . ARG C  1 9   ? 71.310  29.997  62.875  1.00 63.67  ? 9   ARG C CD  1 
ATOM   6996  N  NE  . ARG C  1 9   ? 71.687  30.132  64.294  1.00 76.25  ? 9   ARG C NE  1 
ATOM   6997  C  CZ  . ARG C  1 9   ? 72.760  29.586  64.897  1.00 82.90  ? 9   ARG C CZ  1 
ATOM   6998  N  NH1 . ARG C  1 9   ? 73.634  28.813  64.248  1.00 88.68  ? 9   ARG C NH1 1 
ATOM   6999  N  NH2 . ARG C  1 9   ? 73.029  29.899  66.161  1.00 81.97  ? 9   ARG C NH2 1 
ATOM   7000  N  N   . ASP C  1 10  ? 70.034  23.946  63.345  1.00 40.41  ? 10  ASP C N   1 
ATOM   7001  C  CA  . ASP C  1 10  ? 69.452  22.982  64.248  1.00 38.03  ? 10  ASP C CA  1 
ATOM   7002  C  C   . ASP C  1 10  ? 70.565  22.242  64.988  1.00 34.35  ? 10  ASP C C   1 
ATOM   7003  O  O   . ASP C  1 10  ? 71.640  21.958  64.434  1.00 33.62  ? 10  ASP C O   1 
ATOM   7004  C  CB  . ASP C  1 10  ? 68.482  22.041  63.491  1.00 45.35  ? 10  ASP C CB  1 
ATOM   7005  C  CG  . ASP C  1 10  ? 67.006  22.533  63.521  1.00 49.46  ? 10  ASP C CG  1 
ATOM   7006  O  OD1 . ASP C  1 10  ? 66.652  23.395  64.354  1.00 61.23  ? 10  ASP C OD1 1 
ATOM   7007  O  OD2 . ASP C  1 10  ? 66.163  22.058  62.728  1.00 52.02  ? 10  ASP C OD2 1 
ATOM   7008  N  N   . MET C  1 11  ? 70.357  22.028  66.278  1.00 30.93  ? 11  MET C N   1 
ATOM   7009  C  CA  . MET C  1 11  ? 71.357  21.344  67.061  1.00 27.11  ? 11  MET C CA  1 
ATOM   7010  C  C   . MET C  1 11  ? 71.410  19.962  66.495  1.00 35.42  ? 11  MET C C   1 
ATOM   7011  O  O   . MET C  1 11  ? 70.375  19.344  66.183  1.00 39.33  ? 11  MET C O   1 
ATOM   7012  C  CB  . MET C  1 11  ? 70.981  21.270  68.525  1.00 22.93  ? 11  MET C CB  1 
ATOM   7013  C  CG  . MET C  1 11  ? 70.607  22.569  69.122  1.00 20.45  ? 11  MET C CG  1 
ATOM   7014  S  SD  . MET C  1 11  ? 70.507  22.417  70.807  1.00 23.68  ? 11  MET C SD  1 
ATOM   7015  C  CE  . MET C  1 11  ? 68.799  22.230  71.069  1.00 24.52  ? 11  MET C CE  1 
ATOM   7016  N  N   . PRO C  1 12  ? 72.627  19.469  66.281  1.00 38.44  ? 12  PRO C N   1 
ATOM   7017  C  CA  . PRO C  1 12  ? 72.894  18.137  65.735  1.00 40.38  ? 12  PRO C CA  1 
ATOM   7018  C  C   . PRO C  1 12  ? 72.409  17.028  66.677  1.00 39.93  ? 12  PRO C C   1 
ATOM   7019  O  O   . PRO C  1 12  ? 72.333  17.224  67.900  1.00 38.29  ? 12  PRO C O   1 
ATOM   7020  C  CB  . PRO C  1 12  ? 74.401  18.147  65.586  1.00 38.89  ? 12  PRO C CB  1 
ATOM   7021  C  CG  . PRO C  1 12  ? 74.823  19.045  66.720  1.00 40.80  ? 12  PRO C CG  1 
ATOM   7022  C  CD  . PRO C  1 12  ? 73.882  20.179  66.551  1.00 39.42  ? 12  PRO C CD  1 
ATOM   7023  N  N   . LEU C  1 13  ? 72.129  15.859  66.098  1.00 38.54  ? 13  LEU C N   1 
ATOM   7024  C  CA  . LEU C  1 13  ? 71.617  14.727  66.852  1.00 34.54  ? 13  LEU C CA  1 
ATOM   7025  C  C   . LEU C  1 13  ? 72.435  14.351  68.051  1.00 34.91  ? 13  LEU C C   1 
ATOM   7026  O  O   . LEU C  1 13  ? 71.892  13.829  69.012  1.00 44.28  ? 13  LEU C O   1 
ATOM   7027  C  CB  . LEU C  1 13  ? 71.454  13.513  65.959  1.00 33.85  ? 13  LEU C CB  1 
ATOM   7028  C  CG  . LEU C  1 13  ? 70.307  13.637  64.980  1.00 37.53  ? 13  LEU C CG  1 
ATOM   7029  C  CD1 . LEU C  1 13  ? 70.236  12.393  64.177  1.00 36.16  ? 13  LEU C CD1 1 
ATOM   7030  C  CD2 . LEU C  1 13  ? 68.976  13.888  65.707  1.00 37.05  ? 13  LEU C CD2 1 
ATOM   7031  N  N   . ASP C  1 14  ? 73.739  14.561  67.991  1.00 33.09  ? 14  ASP C N   1 
ATOM   7032  C  CA  . ASP C  1 14  ? 74.573  14.234  69.121  1.00 38.20  ? 14  ASP C CA  1 
ATOM   7033  C  C   . ASP C  1 14  ? 74.538  15.246  70.266  1.00 38.20  ? 14  ASP C C   1 
ATOM   7034  O  O   . ASP C  1 14  ? 74.932  14.925  71.386  1.00 44.55  ? 14  ASP C O   1 
ATOM   7035  C  CB  . ASP C  1 14  ? 76.030  13.896  68.714  1.00 45.60  ? 14  ASP C CB  1 
ATOM   7036  C  CG  . ASP C  1 14  ? 76.647  14.880  67.683  1.00 57.62  ? 14  ASP C CG  1 
ATOM   7037  O  OD1 . ASP C  1 14  ? 76.362  14.748  66.463  1.00 63.72  ? 14  ASP C OD1 1 
ATOM   7038  O  OD2 . ASP C  1 14  ? 77.487  15.733  68.066  1.00 67.34  ? 14  ASP C OD2 1 
ATOM   7039  N  N   . SER C  1 15  ? 74.013  16.433  70.020  1.00 34.09  ? 15  SER C N   1 
ATOM   7040  C  CA  . SER C  1 15  ? 73.980  17.449  71.044  1.00 33.53  ? 15  SER C CA  1 
ATOM   7041  C  C   . SER C  1 15  ? 73.617  16.892  72.412  1.00 33.72  ? 15  SER C C   1 
ATOM   7042  O  O   . SER C  1 15  ? 72.716  16.062  72.555  1.00 33.79  ? 15  SER C O   1 
ATOM   7043  C  CB  . SER C  1 15  ? 73.014  18.521  70.615  1.00 32.08  ? 15  SER C CB  1 
ATOM   7044  O  OG  . SER C  1 15  ? 73.384  18.919  69.316  1.00 35.31  ? 15  SER C OG  1 
ATOM   7045  N  N   . ASP C  1 16  ? 74.434  17.252  73.384  1.00 30.54  ? 16  ASP C N   1 
ATOM   7046  C  CA  . ASP C  1 16  ? 74.238  16.829  74.752  1.00 31.79  ? 16  ASP C CA  1 
ATOM   7047  C  C   . ASP C  1 16  ? 72.825  16.954  75.198  1.00 28.86  ? 16  ASP C C   1 
ATOM   7048  O  O   . ASP C  1 16  ? 72.366  16.248  76.085  1.00 31.41  ? 16  ASP C O   1 
ATOM   7049  C  CB  . ASP C  1 16  ? 75.044  17.708  75.651  1.00 39.38  ? 16  ASP C CB  1 
ATOM   7050  C  CG  . ASP C  1 16  ? 74.911  19.143  75.291  1.00 47.43  ? 16  ASP C CG  1 
ATOM   7051  O  OD1 . ASP C  1 16  ? 75.459  19.553  74.230  1.00 62.27  ? 16  ASP C OD1 1 
ATOM   7052  O  OD2 . ASP C  1 16  ? 74.234  19.841  76.050  1.00 49.70  ? 16  ASP C OD2 1 
ATOM   7053  N  N   . VAL C  1 17  ? 72.148  17.901  74.598  1.00 27.46  ? 17  VAL C N   1 
ATOM   7054  C  CA  . VAL C  1 17  ? 70.797  18.182  74.941  1.00 23.51  ? 17  VAL C CA  1 
ATOM   7055  C  C   . VAL C  1 17  ? 69.880  17.043  74.539  1.00 27.13  ? 17  VAL C C   1 
ATOM   7056  O  O   . VAL C  1 17  ? 68.933  16.749  75.215  1.00 30.72  ? 17  VAL C O   1 
ATOM   7057  C  CB  . VAL C  1 17  ? 70.433  19.543  74.365  1.00 21.89  ? 17  VAL C CB  1 
ATOM   7058  C  CG1 . VAL C  1 17  ? 69.970  19.459  72.925  1.00 17.96  ? 17  VAL C CG1 1 
ATOM   7059  C  CG2 . VAL C  1 17  ? 69.500  20.219  75.260  1.00 29.79  ? 17  VAL C CG2 1 
ATOM   7060  N  N   . PHE C  1 18  ? 70.239  16.302  73.510  1.00 31.49  ? 18  PHE C N   1 
ATOM   7061  C  CA  . PHE C  1 18  ? 69.413  15.187  73.054  1.00 28.90  ? 18  PHE C CA  1 
ATOM   7062  C  C   . PHE C  1 18  ? 69.791  13.806  73.629  1.00 34.55  ? 18  PHE C C   1 
ATOM   7063  O  O   . PHE C  1 18  ? 69.203  12.792  73.231  1.00 32.67  ? 18  PHE C O   1 
ATOM   7064  C  CB  . PHE C  1 18  ? 69.512  15.090  71.546  1.00 23.45  ? 18  PHE C CB  1 
ATOM   7065  C  CG  . PHE C  1 18  ? 69.119  16.317  70.834  1.00 20.81  ? 18  PHE C CG  1 
ATOM   7066  C  CD1 . PHE C  1 18  ? 68.020  17.046  71.258  1.00 21.08  ? 18  PHE C CD1 1 
ATOM   7067  C  CD2 . PHE C  1 18  ? 69.783  16.694  69.669  1.00 16.65  ? 18  PHE C CD2 1 
ATOM   7068  C  CE1 . PHE C  1 18  ? 67.584  18.126  70.523  1.00 15.90  ? 18  PHE C CE1 1 
ATOM   7069  C  CE2 . PHE C  1 18  ? 69.353  17.775  68.918  1.00 12.86  ? 18  PHE C CE2 1 
ATOM   7070  C  CZ  . PHE C  1 18  ? 68.254  18.492  69.340  1.00 16.67  ? 18  PHE C CZ  1 
ATOM   7071  N  N   . ARG C  1 19  ? 70.767  13.732  74.536  1.00 41.46  ? 19  ARG C N   1 
ATOM   7072  C  CA  . ARG C  1 19  ? 71.186  12.432  75.101  1.00 45.12  ? 19  ARG C CA  1 
ATOM   7073  C  C   . ARG C  1 19  ? 70.058  11.633  75.725  1.00 41.46  ? 19  ARG C C   1 
ATOM   7074  O  O   . ARG C  1 19  ? 69.196  12.183  76.403  1.00 47.64  ? 19  ARG C O   1 
ATOM   7075  C  CB  . ARG C  1 19  ? 72.312  12.613  76.124  1.00 58.42  ? 19  ARG C CB  1 
ATOM   7076  C  CG  . ARG C  1 19  ? 73.661  12.813  75.448  1.00 76.40  ? 19  ARG C CG  1 
ATOM   7077  C  CD  . ARG C  1 19  ? 74.767  13.353  76.391  1.00 91.76  ? 19  ARG C CD  1 
ATOM   7078  N  NE  . ARG C  1 19  ? 75.992  13.683  75.633  1.00 105.24 ? 19  ARG C NE  1 
ATOM   7079  C  CZ  . ARG C  1 19  ? 77.038  14.377  76.097  1.00 109.66 ? 19  ARG C CZ  1 
ATOM   7080  N  NH1 . ARG C  1 19  ? 77.049  14.839  77.346  1.00 110.66 ? 19  ARG C NH1 1 
ATOM   7081  N  NH2 . ARG C  1 19  ? 78.080  14.621  75.299  1.00 113.79 ? 19  ARG C NH2 1 
ATOM   7082  N  N   . VAL C  1 20  ? 70.053  10.329  75.509  1.00 33.15  ? 20  VAL C N   1 
ATOM   7083  C  CA  . VAL C  1 20  ? 69.007  9.531   76.089  1.00 28.68  ? 20  VAL C CA  1 
ATOM   7084  C  C   . VAL C  1 20  ? 69.402  9.012   77.443  1.00 29.62  ? 20  VAL C C   1 
ATOM   7085  O  O   . VAL C  1 20  ? 70.512  8.513   77.643  1.00 32.38  ? 20  VAL C O   1 
ATOM   7086  C  CB  . VAL C  1 20  ? 68.545  8.424   75.168  1.00 27.92  ? 20  VAL C CB  1 
ATOM   7087  C  CG1 . VAL C  1 20  ? 69.586  8.106   74.245  1.00 31.09  ? 20  VAL C CG1 1 
ATOM   7088  C  CG2 . VAL C  1 20  ? 68.117  7.198   75.956  1.00 31.02  ? 20  VAL C CG2 1 
ATOM   7089  N  N   . PRO C  1 21  ? 68.504  9.181   78.409  1.00 25.16  ? 21  PRO C N   1 
ATOM   7090  C  CA  . PRO C  1 21  ? 68.711  8.753   79.768  1.00 25.52  ? 21  PRO C CA  1 
ATOM   7091  C  C   . PRO C  1 21  ? 69.084  7.307   79.723  1.00 32.72  ? 21  PRO C C   1 
ATOM   7092  O  O   . PRO C  1 21  ? 68.516  6.550   78.947  1.00 37.31  ? 21  PRO C O   1 
ATOM   7093  C  CB  . PRO C  1 21  ? 67.370  9.021   80.404  1.00 25.19  ? 21  PRO C CB  1 
ATOM   7094  C  CG  . PRO C  1 21  ? 66.423  9.050   79.240  1.00 26.56  ? 21  PRO C CG  1 
ATOM   7095  C  CD  . PRO C  1 21  ? 67.167  9.742   78.225  1.00 21.82  ? 21  PRO C CD  1 
ATOM   7096  N  N   . PRO C  1 22  ? 70.115  6.922   80.489  1.00 36.16  ? 22  PRO C N   1 
ATOM   7097  C  CA  . PRO C  1 22  ? 70.687  5.590   80.619  1.00 35.41  ? 22  PRO C CA  1 
ATOM   7098  C  C   . PRO C  1 22  ? 69.810  4.660   81.434  1.00 37.32  ? 22  PRO C C   1 
ATOM   7099  O  O   . PRO C  1 22  ? 69.135  5.125   82.401  1.00 41.37  ? 22  PRO C O   1 
ATOM   7100  C  CB  . PRO C  1 22  ? 71.973  5.887   81.340  1.00 34.74  ? 22  PRO C CB  1 
ATOM   7101  C  CG  . PRO C  1 22  ? 71.535  6.883   82.305  1.00 35.73  ? 22  PRO C CG  1 
ATOM   7102  C  CD  . PRO C  1 22  ? 70.797  7.834   81.415  1.00 39.56  ? 22  PRO C CD  1 
ATOM   7103  N  N   . GLY C  1 23  ? 69.875  3.361   81.074  1.00 33.14  ? 23  GLY C N   1 
ATOM   7104  C  CA  . GLY C  1 23  ? 69.095  2.337   81.746  1.00 31.16  ? 23  GLY C CA  1 
ATOM   7105  C  C   . GLY C  1 23  ? 68.235  1.612   80.728  1.00 35.05  ? 23  GLY C C   1 
ATOM   7106  O  O   . GLY C  1 23  ? 67.894  2.183   79.685  1.00 38.49  ? 23  GLY C O   1 
ATOM   7107  N  N   . TYR C  1 24  ? 67.872  0.359   81.013  1.00 31.51  ? 24  TYR C N   1 
ATOM   7108  C  CA  . TYR C  1 24  ? 67.071  -0.394  80.068  1.00 23.65  ? 24  TYR C CA  1 
ATOM   7109  C  C   . TYR C  1 24  ? 65.678  0.126   80.139  1.00 25.38  ? 24  TYR C C   1 
ATOM   7110  O  O   . TYR C  1 24  ? 65.099  0.165   81.224  1.00 25.27  ? 24  TYR C O   1 
ATOM   7111  C  CB  . TYR C  1 24  ? 67.041  -1.882  80.398  1.00 15.47  ? 24  TYR C CB  1 
ATOM   7112  C  CG  . TYR C  1 24  ? 66.059  -2.674  79.509  1.00 13.95  ? 24  TYR C CG  1 
ATOM   7113  C  CD1 . TYR C  1 24  ? 66.372  -2.988  78.165  1.00 11.15  ? 24  TYR C CD1 1 
ATOM   7114  C  CD2 . TYR C  1 24  ? 64.799  -3.046  79.975  1.00 9.80   ? 24  TYR C CD2 1 
ATOM   7115  C  CE1 . TYR C  1 24  ? 65.484  -3.637  77.353  1.00 6.42   ? 24  TYR C CE1 1 
ATOM   7116  C  CE2 . TYR C  1 24  ? 63.880  -3.714  79.147  1.00 6.14   ? 24  TYR C CE2 1 
ATOM   7117  C  CZ  . TYR C  1 24  ? 64.231  -3.993  77.842  1.00 14.15  ? 24  TYR C CZ  1 
ATOM   7118  O  OH  . TYR C  1 24  ? 63.324  -4.633  77.011  1.00 22.49  ? 24  TYR C OH  1 
ATOM   7119  N  N   . ASN C  1 25  ? 65.135  0.473   78.979  1.00 24.77  ? 25  ASN C N   1 
ATOM   7120  C  CA  . ASN C  1 25  ? 63.774  0.967   78.877  1.00 24.14  ? 25  ASN C CA  1 
ATOM   7121  C  C   . ASN C  1 25  ? 63.583  2.080   79.898  1.00 28.07  ? 25  ASN C C   1 
ATOM   7122  O  O   . ASN C  1 25  ? 62.731  1.984   80.802  1.00 37.01  ? 25  ASN C O   1 
ATOM   7123  C  CB  . ASN C  1 25  ? 62.807  -0.153  79.172  1.00 19.31  ? 25  ASN C CB  1 
ATOM   7124  C  CG  . ASN C  1 25  ? 61.514  0.036   78.496  1.00 17.79  ? 25  ASN C CG  1 
ATOM   7125  O  OD1 . ASN C  1 25  ? 60.470  -0.278  79.044  1.00 22.67  ? 25  ASN C OD1 1 
ATOM   7126  N  ND2 . ASN C  1 25  ? 61.565  0.484   77.263  1.00 18.86  ? 25  ASN C ND2 1 
ATOM   7127  N  N   . ALA C  1 26  ? 64.442  3.088   79.807  1.00 30.98  ? 26  ALA C N   1 
ATOM   7128  C  CA  . ALA C  1 26  ? 64.382  4.236   80.694  1.00 33.29  ? 26  ALA C CA  1 
ATOM   7129  C  C   . ALA C  1 26  ? 63.427  5.286   80.107  1.00 33.26  ? 26  ALA C C   1 
ATOM   7130  O  O   . ALA C  1 26  ? 63.511  5.623   78.917  1.00 42.58  ? 26  ALA C O   1 
ATOM   7131  C  CB  . ALA C  1 26  ? 65.767  4.809   80.860  1.00 36.15  ? 26  ALA C CB  1 
ATOM   7132  N  N   . PRO C  1 27  ? 62.496  5.791   80.923  1.00 25.97  ? 27  PRO C N   1 
ATOM   7133  C  CA  . PRO C  1 27  ? 61.512  6.788   80.535  1.00 26.59  ? 27  PRO C CA  1 
ATOM   7134  C  C   . PRO C  1 27  ? 62.229  7.994   79.952  1.00 29.36  ? 27  PRO C C   1 
ATOM   7135  O  O   . PRO C  1 27  ? 63.149  8.543   80.566  1.00 28.03  ? 27  PRO C O   1 
ATOM   7136  C  CB  . PRO C  1 27  ? 60.876  7.173   81.867  1.00 24.85  ? 27  PRO C CB  1 
ATOM   7137  C  CG  . PRO C  1 27  ? 61.008  5.974   82.690  1.00 25.60  ? 27  PRO C CG  1 
ATOM   7138  C  CD  . PRO C  1 27  ? 62.406  5.519   82.360  1.00 33.52  ? 27  PRO C CD  1 
ATOM   7139  N  N   . GLN C  1 28  ? 61.848  8.380   78.752  1.00 23.21  ? 28  GLN C N   1 
ATOM   7140  C  CA  . GLN C  1 28  ? 62.471  9.521   78.181  1.00 21.11  ? 28  GLN C CA  1 
ATOM   7141  C  C   . GLN C  1 28  ? 61.342  10.362  77.673  1.00 23.83  ? 28  GLN C C   1 
ATOM   7142  O  O   . GLN C  1 28  ? 60.178  9.932   77.607  1.00 22.15  ? 28  GLN C O   1 
ATOM   7143  C  CB  . GLN C  1 28  ? 63.396  9.132   77.047  1.00 22.01  ? 28  GLN C CB  1 
ATOM   7144  C  CG  . GLN C  1 28  ? 62.689  8.714   75.793  1.00 23.42  ? 28  GLN C CG  1 
ATOM   7145  C  CD  . GLN C  1 28  ? 63.680  8.275   74.802  1.00 24.46  ? 28  GLN C CD  1 
ATOM   7146  O  OE1 . GLN C  1 28  ? 64.370  7.318   75.036  1.00 25.99  ? 28  GLN C OE1 1 
ATOM   7147  N  NE2 . GLN C  1 28  ? 63.828  9.010   73.726  1.00 19.10  ? 28  GLN C NE2 1 
ATOM   7148  N  N   . GLN C  1 29  ? 61.695  11.596  77.356  1.00 28.05  ? 29  GLN C N   1 
ATOM   7149  C  CA  . GLN C  1 29  ? 60.745  12.570  76.856  1.00 25.32  ? 29  GLN C CA  1 
ATOM   7150  C  C   . GLN C  1 29  ? 59.653  12.845  77.886  1.00 28.93  ? 29  GLN C C   1 
ATOM   7151  O  O   . GLN C  1 29  ? 58.479  12.956  77.535  1.00 33.06  ? 29  GLN C O   1 
ATOM   7152  C  CB  . GLN C  1 29  ? 60.158  12.056  75.526  1.00 23.88  ? 29  GLN C CB  1 
ATOM   7153  C  CG  . GLN C  1 29  ? 61.180  11.884  74.394  1.00 20.46  ? 29  GLN C CG  1 
ATOM   7154  C  CD  . GLN C  1 29  ? 60.569  11.403  73.103  1.00 23.57  ? 29  GLN C CD  1 
ATOM   7155  O  OE1 . GLN C  1 29  ? 59.556  11.927  72.642  1.00 26.57  ? 29  GLN C OE1 1 
ATOM   7156  N  NE2 . GLN C  1 29  ? 61.194  10.398  72.495  1.00 28.93  ? 29  GLN C NE2 1 
ATOM   7157  N  N   . VAL C  1 30  ? 60.021  12.972  79.160  1.00 31.48  ? 30  VAL C N   1 
ATOM   7158  C  CA  . VAL C  1 30  ? 58.998  13.220  80.187  1.00 33.77  ? 30  VAL C CA  1 
ATOM   7159  C  C   . VAL C  1 30  ? 58.420  14.633  80.110  1.00 33.29  ? 30  VAL C C   1 
ATOM   7160  O  O   . VAL C  1 30  ? 59.126  15.587  79.861  1.00 36.58  ? 30  VAL C O   1 
ATOM   7161  C  CB  . VAL C  1 30  ? 59.505  12.933  81.602  1.00 31.14  ? 30  VAL C CB  1 
ATOM   7162  C  CG1 . VAL C  1 30  ? 58.405  13.219  82.631  1.00 28.28  ? 30  VAL C CG1 1 
ATOM   7163  C  CG2 . VAL C  1 30  ? 59.919  11.490  81.688  1.00 31.71  ? 30  VAL C CG2 1 
ATOM   7164  N  N   . HIS C  1 31  ? 57.108  14.742  80.237  1.00 32.27  ? 31  HIS C N   1 
ATOM   7165  C  CA  . HIS C  1 31  ? 56.444  16.029  80.165  1.00 28.46  ? 31  HIS C CA  1 
ATOM   7166  C  C   . HIS C  1 31  ? 55.077  16.028  80.815  1.00 28.98  ? 31  HIS C C   1 
ATOM   7167  O  O   . HIS C  1 31  ? 54.330  15.063  80.685  1.00 28.20  ? 31  HIS C O   1 
ATOM   7168  C  CB  . HIS C  1 31  ? 56.360  16.511  78.719  1.00 26.71  ? 31  HIS C CB  1 
ATOM   7169  C  CG  . HIS C  1 31  ? 55.705  15.559  77.768  1.00 24.91  ? 31  HIS C CG  1 
ATOM   7170  N  ND1 . HIS C  1 31  ? 54.453  15.782  77.232  1.00 30.14  ? 31  HIS C ND1 1 
ATOM   7171  C  CD2 . HIS C  1 31  ? 56.177  14.443  77.161  1.00 20.20  ? 31  HIS C CD2 1 
ATOM   7172  C  CE1 . HIS C  1 31  ? 54.189  14.854  76.329  1.00 25.59  ? 31  HIS C CE1 1 
ATOM   7173  N  NE2 . HIS C  1 31  ? 55.220  14.029  76.271  1.00 22.93  ? 31  HIS C NE2 1 
ATOM   7174  N  N   . ILE C  1 32  ? 54.752  17.108  81.521  1.00 29.93  ? 32  ILE C N   1 
ATOM   7175  C  CA  . ILE C  1 32  ? 53.470  17.212  82.227  1.00 33.24  ? 32  ILE C CA  1 
ATOM   7176  C  C   . ILE C  1 32  ? 52.606  18.399  81.774  1.00 32.97  ? 32  ILE C C   1 
ATOM   7177  O  O   . ILE C  1 32  ? 53.061  19.192  80.985  1.00 38.56  ? 32  ILE C O   1 
ATOM   7178  C  CB  . ILE C  1 32  ? 53.712  17.332  83.761  1.00 34.65  ? 32  ILE C CB  1 
ATOM   7179  C  CG1 . ILE C  1 32  ? 54.291  18.694  84.120  1.00 39.58  ? 32  ILE C CG1 1 
ATOM   7180  C  CG2 . ILE C  1 32  ? 54.734  16.307  84.217  1.00 35.52  ? 32  ILE C CG2 1 
ATOM   7181  C  CD1 . ILE C  1 32  ? 54.480  18.897  85.603  1.00 33.62  ? 32  ILE C CD1 1 
ATOM   7182  N  N   . THR C  1 33  ? 51.337  18.457  82.205  1.00 34.61  ? 33  THR C N   1 
ATOM   7183  C  CA  . THR C  1 33  ? 50.383  19.566  81.928  1.00 31.01  ? 33  THR C CA  1 
ATOM   7184  C  C   . THR C  1 33  ? 49.266  19.468  82.910  1.00 32.27  ? 33  THR C C   1 
ATOM   7185  O  O   . THR C  1 33  ? 49.060  18.446  83.551  1.00 39.20  ? 33  THR C O   1 
ATOM   7186  C  CB  . THR C  1 33  ? 49.600  19.484  80.653  1.00 25.18  ? 33  THR C CB  1 
ATOM   7187  O  OG1 . THR C  1 33  ? 50.321  18.730  79.708  1.00 48.31  ? 33  THR C OG1 1 
ATOM   7188  C  CG2 . THR C  1 33  ? 49.433  20.864  80.112  1.00 25.23  ? 33  THR C CG2 1 
ATOM   7189  N  N   . GLN C  1 34  ? 48.447  20.489  82.937  1.00 29.62  ? 34  GLN C N   1 
ATOM   7190  C  CA  . GLN C  1 34  ? 47.356  20.457  83.850  1.00 27.20  ? 34  GLN C CA  1 
ATOM   7191  C  C   . GLN C  1 34  ? 46.397  19.413  83.336  1.00 29.29  ? 34  GLN C C   1 
ATOM   7192  O  O   . GLN C  1 34  ? 46.127  19.362  82.142  1.00 31.25  ? 34  GLN C O   1 
ATOM   7193  C  CB  . GLN C  1 34  ? 46.709  21.811  83.887  1.00 27.24  ? 34  GLN C CB  1 
ATOM   7194  C  CG  . GLN C  1 34  ? 45.627  21.893  84.867  1.00 26.18  ? 34  GLN C CG  1 
ATOM   7195  C  CD  . GLN C  1 34  ? 45.370  23.305  85.285  1.00 30.98  ? 34  GLN C CD  1 
ATOM   7196  O  OE1 . GLN C  1 34  ? 44.219  23.693  85.398  1.00 31.63  ? 34  GLN C OE1 1 
ATOM   7197  N  NE2 . GLN C  1 34  ? 46.434  24.078  85.562  1.00 14.58  ? 34  GLN C NE2 1 
ATOM   7198  N  N   . GLY C  1 35  ? 45.907  18.573  84.239  1.00 28.70  ? 35  GLY C N   1 
ATOM   7199  C  CA  . GLY C  1 35  ? 44.986  17.521  83.865  1.00 28.88  ? 35  GLY C CA  1 
ATOM   7200  C  C   . GLY C  1 35  ? 43.499  17.760  84.128  1.00 29.92  ? 35  GLY C C   1 
ATOM   7201  O  O   . GLY C  1 35  ? 42.657  16.914  83.781  1.00 28.20  ? 35  GLY C O   1 
ATOM   7202  N  N   . ASP C  1 36  ? 43.160  18.880  84.759  1.00 33.21  ? 36  ASP C N   1 
ATOM   7203  C  CA  . ASP C  1 36  ? 41.766  19.205  85.038  1.00 32.96  ? 36  ASP C CA  1 
ATOM   7204  C  C   . ASP C  1 36  ? 41.497  20.670  84.806  1.00 36.01  ? 36  ASP C C   1 
ATOM   7205  O  O   . ASP C  1 36  ? 42.404  21.435  84.491  1.00 42.31  ? 36  ASP C O   1 
ATOM   7206  C  CB  . ASP C  1 36  ? 41.421  18.871  86.482  1.00 34.65  ? 36  ASP C CB  1 
ATOM   7207  C  CG  . ASP C  1 36  ? 42.159  19.742  87.499  1.00 40.25  ? 36  ASP C CG  1 
ATOM   7208  O  OD1 . ASP C  1 36  ? 42.993  20.599  87.134  1.00 34.07  ? 36  ASP C OD1 1 
ATOM   7209  O  OD2 . ASP C  1 36  ? 41.887  19.560  88.705  1.00 50.44  ? 36  ASP C OD2 1 
ATOM   7210  N  N   . LEU C  1 37  ? 40.286  21.102  85.094  1.00 34.27  ? 37  LEU C N   1 
ATOM   7211  C  CA  . LEU C  1 37  ? 39.986  22.492  84.902  1.00 34.32  ? 37  LEU C CA  1 
ATOM   7212  C  C   . LEU C  1 37  ? 40.584  23.497  85.878  1.00 35.58  ? 37  LEU C C   1 
ATOM   7213  O  O   . LEU C  1 37  ? 40.888  24.631  85.489  1.00 37.73  ? 37  LEU C O   1 
ATOM   7214  C  CB  . LEU C  1 37  ? 38.496  22.678  84.918  1.00 39.10  ? 37  LEU C CB  1 
ATOM   7215  C  CG  . LEU C  1 37  ? 38.097  24.053  84.414  1.00 37.37  ? 37  LEU C CG  1 
ATOM   7216  C  CD1 . LEU C  1 37  ? 38.637  24.218  83.027  1.00 45.27  ? 37  LEU C CD1 1 
ATOM   7217  C  CD2 . LEU C  1 37  ? 36.633  24.155  84.383  1.00 41.09  ? 37  LEU C CD2 1 
ATOM   7218  N  N   . VAL C  1 38  ? 40.804  23.077  87.120  1.00 34.32  ? 38  VAL C N   1 
ATOM   7219  C  CA  . VAL C  1 38  ? 41.250  24.010  88.145  1.00 32.83  ? 38  VAL C CA  1 
ATOM   7220  C  C   . VAL C  1 38  ? 42.590  23.894  88.858  1.00 35.52  ? 38  VAL C C   1 
ATOM   7221  O  O   . VAL C  1 38  ? 42.892  24.695  89.783  1.00 37.28  ? 38  VAL C O   1 
ATOM   7222  C  CB  . VAL C  1 38  ? 40.167  24.142  89.196  1.00 34.86  ? 38  VAL C CB  1 
ATOM   7223  C  CG1 . VAL C  1 38  ? 38.776  24.131  88.540  1.00 34.93  ? 38  VAL C CG1 1 
ATOM   7224  C  CG2 . VAL C  1 38  ? 40.245  23.011  90.119  1.00 36.84  ? 38  VAL C CG2 1 
ATOM   7225  N  N   . GLY C  1 39  ? 43.397  22.917  88.464  1.00 34.42  ? 39  GLY C N   1 
ATOM   7226  C  CA  . GLY C  1 39  ? 44.710  22.824  89.073  1.00 35.62  ? 39  GLY C CA  1 
ATOM   7227  C  C   . GLY C  1 39  ? 45.037  21.609  89.898  1.00 37.58  ? 39  GLY C C   1 
ATOM   7228  O  O   . GLY C  1 39  ? 46.203  21.417  90.250  1.00 39.54  ? 39  GLY C O   1 
ATOM   7229  N  N   . ARG C  1 40  ? 44.061  20.757  90.192  1.00 35.48  ? 40  ARG C N   1 
ATOM   7230  C  CA  . ARG C  1 40  ? 44.418  19.593  90.988  1.00 37.50  ? 40  ARG C CA  1 
ATOM   7231  C  C   . ARG C  1 40  ? 44.538  18.244  90.308  1.00 35.14  ? 40  ARG C C   1 
ATOM   7232  O  O   . ARG C  1 40  ? 44.187  17.228  90.874  1.00 39.05  ? 40  ARG C O   1 
ATOM   7233  C  CB  . ARG C  1 40  ? 43.616  19.530  92.297  1.00 40.16  ? 40  ARG C CB  1 
ATOM   7234  C  CG  . ARG C  1 40  ? 42.127  19.550  92.201  1.00 42.32  ? 40  ARG C CG  1 
ATOM   7235  C  CD  . ARG C  1 40  ? 41.536  20.256  93.428  1.00 48.41  ? 40  ARG C CD  1 
ATOM   7236  N  NE  . ARG C  1 40  ? 41.927  19.640  94.687  1.00 60.76  ? 40  ARG C NE  1 
ATOM   7237  C  CZ  . ARG C  1 40  ? 41.293  18.612  95.238  1.00 67.83  ? 40  ARG C CZ  1 
ATOM   7238  N  NH1 . ARG C  1 40  ? 40.229  18.090  94.629  1.00 69.16  ? 40  ARG C NH1 1 
ATOM   7239  N  NH2 . ARG C  1 40  ? 41.736  18.097  96.386  1.00 73.95  ? 40  ARG C NH2 1 
ATOM   7240  N  N   . ALA C  1 41  ? 45.137  18.229  89.128  1.00 31.19  ? 41  ALA C N   1 
ATOM   7241  C  CA  . ALA C  1 41  ? 45.334  16.997  88.385  1.00 28.82  ? 41  ALA C CA  1 
ATOM   7242  C  C   . ALA C  1 41  ? 46.419  17.307  87.413  1.00 28.80  ? 41  ALA C C   1 
ATOM   7243  O  O   . ALA C  1 41  ? 46.538  18.428  86.975  1.00 31.23  ? 41  ALA C O   1 
ATOM   7244  C  CB  . ALA C  1 41  ? 44.111  16.620  87.641  1.00 22.80  ? 41  ALA C CB  1 
ATOM   7245  N  N   . MET C  1 42  ? 47.234  16.324  87.089  1.00 28.62  ? 42  MET C N   1 
ATOM   7246  C  CA  . MET C  1 42  ? 48.309  16.542  86.148  1.00 24.93  ? 42  MET C CA  1 
ATOM   7247  C  C   . MET C  1 42  ? 48.291  15.429  85.199  1.00 25.85  ? 42  MET C C   1 
ATOM   7248  O  O   . MET C  1 42  ? 47.872  14.343  85.545  1.00 29.56  ? 42  MET C O   1 
ATOM   7249  C  CB  . MET C  1 42  ? 49.641  16.466  86.849  1.00 29.78  ? 42  MET C CB  1 
ATOM   7250  C  CG  . MET C  1 42  ? 50.026  17.718  87.497  1.00 32.50  ? 42  MET C CG  1 
ATOM   7251  S  SD  . MET C  1 42  ? 50.570  18.720  86.233  1.00 32.15  ? 42  MET C SD  1 
ATOM   7252  C  CE  . MET C  1 42  ? 51.240  19.964  87.218  1.00 35.90  ? 42  MET C CE  1 
ATOM   7253  N  N   . ILE C  1 43  ? 48.778  15.659  84.000  1.00 26.66  ? 43  ILE C N   1 
ATOM   7254  C  CA  . ILE C  1 43  ? 48.839  14.574  83.056  1.00 23.77  ? 43  ILE C CA  1 
ATOM   7255  C  C   . ILE C  1 43  ? 50.294  14.314  82.896  1.00 26.48  ? 43  ILE C C   1 
ATOM   7256  O  O   . ILE C  1 43  ? 51.026  15.216  82.470  1.00 33.88  ? 43  ILE C O   1 
ATOM   7257  C  CB  . ILE C  1 43  ? 48.306  14.975  81.714  1.00 19.85  ? 43  ILE C CB  1 
ATOM   7258  C  CG1 . ILE C  1 43  ? 46.803  15.118  81.786  1.00 14.20  ? 43  ILE C CG1 1 
ATOM   7259  C  CG2 . ILE C  1 43  ? 48.668  13.942  80.696  1.00 12.83  ? 43  ILE C CG2 1 
ATOM   7260  C  CD1 . ILE C  1 43  ? 46.245  15.537  80.491  1.00 10.24  ? 43  ILE C CD1 1 
ATOM   7261  N  N   . ILE C  1 44  ? 50.723  13.115  83.256  1.00 25.27  ? 44  ILE C N   1 
ATOM   7262  C  CA  . ILE C  1 44  ? 52.136  12.746  83.124  1.00 25.38  ? 44  ILE C CA  1 
ATOM   7263  C  C   . ILE C  1 44  ? 52.279  11.955  81.833  1.00 24.11  ? 44  ILE C C   1 
ATOM   7264  O  O   . ILE C  1 44  ? 51.485  11.047  81.577  1.00 30.33  ? 44  ILE C O   1 
ATOM   7265  C  CB  . ILE C  1 44  ? 52.586  11.890  84.288  1.00 23.99  ? 44  ILE C CB  1 
ATOM   7266  C  CG1 . ILE C  1 44  ? 51.987  12.414  85.594  1.00 22.90  ? 44  ILE C CG1 1 
ATOM   7267  C  CG2 . ILE C  1 44  ? 54.081  11.925  84.384  1.00 25.28  ? 44  ILE C CG2 1 
ATOM   7268  C  CD1 . ILE C  1 44  ? 52.599  13.710  86.084  1.00 29.07  ? 44  ILE C CD1 1 
ATOM   7269  N  N   . SER C  1 45  ? 53.240  12.320  80.995  1.00 20.87  ? 45  SER C N   1 
ATOM   7270  C  CA  . SER C  1 45  ? 53.443  11.630  79.720  1.00 20.95  ? 45  SER C CA  1 
ATOM   7271  C  C   . SER C  1 45  ? 54.904  11.310  79.480  1.00 23.65  ? 45  SER C C   1 
ATOM   7272  O  O   . SER C  1 45  ? 55.767  12.154  79.741  1.00 28.46  ? 45  SER C O   1 
ATOM   7273  C  CB  . SER C  1 45  ? 53.029  12.532  78.564  1.00 16.32  ? 45  SER C CB  1 
ATOM   7274  O  OG  . SER C  1 45  ? 51.767  13.122  78.762  1.00 24.70  ? 45  SER C OG  1 
ATOM   7275  N  N   . TRP C  1 46  ? 55.214  10.123  78.970  1.00 25.19  ? 46  TRP C N   1 
ATOM   7276  C  CA  . TRP C  1 46  ? 56.620  9.828   78.650  1.00 24.19  ? 46  TRP C CA  1 
ATOM   7277  C  C   . TRP C  1 46  ? 56.681  8.785   77.589  1.00 23.34  ? 46  TRP C C   1 
ATOM   7278  O  O   . TRP C  1 46  ? 55.633  8.234   77.151  1.00 26.92  ? 46  TRP C O   1 
ATOM   7279  C  CB  . TRP C  1 46  ? 57.419  9.363   79.859  1.00 24.68  ? 46  TRP C CB  1 
ATOM   7280  C  CG  . TRP C  1 46  ? 56.913  8.074   80.425  1.00 31.78  ? 46  TRP C CG  1 
ATOM   7281  C  CD1 . TRP C  1 46  ? 57.450  6.845   80.245  1.00 32.14  ? 46  TRP C CD1 1 
ATOM   7282  C  CD2 . TRP C  1 46  ? 55.732  7.883   81.209  1.00 29.21  ? 46  TRP C CD2 1 
ATOM   7283  N  NE1 . TRP C  1 46  ? 56.668  5.902   80.862  1.00 31.23  ? 46  TRP C NE1 1 
ATOM   7284  C  CE2 . TRP C  1 46  ? 55.611  6.529   81.455  1.00 25.38  ? 46  TRP C CE2 1 
ATOM   7285  C  CE3 . TRP C  1 46  ? 54.765  8.740   81.725  1.00 30.64  ? 46  TRP C CE3 1 
ATOM   7286  C  CZ2 . TRP C  1 46  ? 54.571  6.006   82.187  1.00 26.38  ? 46  TRP C CZ2 1 
ATOM   7287  C  CZ3 . TRP C  1 46  ? 53.727  8.205   82.463  1.00 33.58  ? 46  TRP C CZ3 1 
ATOM   7288  C  CH2 . TRP C  1 46  ? 53.639  6.859   82.685  1.00 22.44  ? 46  TRP C CH2 1 
ATOM   7289  N  N   . VAL C  1 47  ? 57.906  8.456   77.227  1.00 17.41  ? 47  VAL C N   1 
ATOM   7290  C  CA  . VAL C  1 47  ? 58.113  7.463   76.210  1.00 19.98  ? 47  VAL C CA  1 
ATOM   7291  C  C   . VAL C  1 47  ? 59.167  6.462   76.652  1.00 22.79  ? 47  VAL C C   1 
ATOM   7292  O  O   . VAL C  1 47  ? 60.144  6.841   77.318  1.00 23.07  ? 47  VAL C O   1 
ATOM   7293  C  CB  . VAL C  1 47  ? 58.582  8.123   74.975  1.00 14.98  ? 47  VAL C CB  1 
ATOM   7294  C  CG1 . VAL C  1 47  ? 58.880  7.120   73.986  1.00 19.72  ? 47  VAL C CG1 1 
ATOM   7295  C  CG2 . VAL C  1 47  ? 57.554  9.096   74.475  1.00 20.92  ? 47  VAL C CG2 1 
ATOM   7296  N  N   . THR C  1 48  ? 58.917  5.183   76.349  1.00 21.82  ? 48  THR C N   1 
ATOM   7297  C  CA  . THR C  1 48  ? 59.817  4.060   76.658  1.00 22.32  ? 48  THR C CA  1 
ATOM   7298  C  C   . THR C  1 48  ? 60.104  3.508   75.288  1.00 25.34  ? 48  THR C C   1 
ATOM   7299  O  O   . THR C  1 48  ? 59.180  3.342   74.498  1.00 25.90  ? 48  THR C O   1 
ATOM   7300  C  CB  . THR C  1 48  ? 59.151  2.926   77.438  1.00 15.92  ? 48  THR C CB  1 
ATOM   7301  O  OG1 . THR C  1 48  ? 57.944  2.525   76.776  1.00 23.72  ? 48  THR C OG1 1 
ATOM   7302  C  CG2 . THR C  1 48  ? 58.867  3.332   78.840  1.00 19.53  ? 48  THR C CG2 1 
ATOM   7303  N  N   . MET C  1 49  ? 61.352  3.143   75.033  1.00 27.13  ? 49  MET C N   1 
ATOM   7304  C  CA  . MET C  1 49  ? 61.712  2.681   73.699  1.00 31.32  ? 49  MET C CA  1 
ATOM   7305  C  C   . MET C  1 49  ? 62.052  1.221   73.518  1.00 32.30  ? 49  MET C C   1 
ATOM   7306  O  O   . MET C  1 49  ? 61.964  0.704   72.396  1.00 35.63  ? 49  MET C O   1 
ATOM   7307  C  CB  . MET C  1 49  ? 62.878  3.512   73.155  1.00 30.20  ? 49  MET C CB  1 
ATOM   7308  C  CG  . MET C  1 49  ? 62.614  4.988   72.990  1.00 39.58  ? 49  MET C CG  1 
ATOM   7309  S  SD  . MET C  1 49  ? 62.089  5.383   71.344  1.00 42.27  ? 49  MET C SD  1 
ATOM   7310  C  CE  . MET C  1 49  ? 63.378  6.777   70.901  1.00 63.75  ? 49  MET C CE  1 
ATOM   7311  N  N   . ASP C  1 50  ? 62.505  0.578   74.593  1.00 32.92  ? 50  ASP C N   1 
ATOM   7312  C  CA  . ASP C  1 50  ? 62.893  -0.827  74.548  1.00 28.94  ? 50  ASP C CA  1 
ATOM   7313  C  C   . ASP C  1 50  ? 61.709  -1.765  74.523  1.00 28.22  ? 50  ASP C C   1 
ATOM   7314  O  O   . ASP C  1 50  ? 61.618  -2.669  73.707  1.00 27.26  ? 50  ASP C O   1 
ATOM   7315  C  CB  . ASP C  1 50  ? 63.846  -1.110  75.684  1.00 29.75  ? 50  ASP C CB  1 
ATOM   7316  C  CG  . ASP C  1 50  ? 65.124  -0.330  75.518  1.00 36.13  ? 50  ASP C CG  1 
ATOM   7317  O  OD1 . ASP C  1 50  ? 65.626  -0.283  74.364  1.00 33.43  ? 50  ASP C OD1 1 
ATOM   7318  O  OD2 . ASP C  1 50  ? 65.596  0.302   76.490  1.00 34.15  ? 50  ASP C OD2 1 
ATOM   7319  N  N   . GLU C  1 51  ? 60.770  -1.538  75.404  1.00 24.19  ? 51  GLU C N   1 
ATOM   7320  C  CA  . GLU C  1 51  ? 59.612  -2.363  75.377  1.00 24.71  ? 51  GLU C CA  1 
ATOM   7321  C  C   . GLU C  1 51  ? 58.545  -1.528  76.024  1.00 25.52  ? 51  GLU C C   1 
ATOM   7322  O  O   . GLU C  1 51  ? 58.824  -0.492  76.632  1.00 24.89  ? 51  GLU C O   1 
ATOM   7323  C  CB  . GLU C  1 51  ? 59.871  -3.683  76.121  1.00 27.48  ? 51  GLU C CB  1 
ATOM   7324  C  CG  . GLU C  1 51  ? 60.660  -3.559  77.382  1.00 29.25  ? 51  GLU C CG  1 
ATOM   7325  C  CD  . GLU C  1 51  ? 60.464  -4.729  78.296  1.00 32.71  ? 51  GLU C CD  1 
ATOM   7326  O  OE1 . GLU C  1 51  ? 59.329  -4.956  78.761  1.00 31.88  ? 51  GLU C OE1 1 
ATOM   7327  O  OE2 . GLU C  1 51  ? 61.449  -5.415  78.582  1.00 39.76  ? 51  GLU C OE2 1 
ATOM   7328  N  N   . PRO C  1 52  ? 57.299  -1.922  75.830  1.00 23.56  ? 52  PRO C N   1 
ATOM   7329  C  CA  . PRO C  1 52  ? 56.135  -1.257  76.364  1.00 27.42  ? 52  PRO C CA  1 
ATOM   7330  C  C   . PRO C  1 52  ? 56.277  -0.612  77.738  1.00 32.92  ? 52  PRO C C   1 
ATOM   7331  O  O   . PRO C  1 52  ? 56.104  0.608   77.862  1.00 40.03  ? 52  PRO C O   1 
ATOM   7332  C  CB  . PRO C  1 52  ? 55.111  -2.358  76.307  1.00 23.94  ? 52  PRO C CB  1 
ATOM   7333  C  CG  . PRO C  1 52  ? 55.389  -2.905  74.940  1.00 14.13  ? 52  PRO C CG  1 
ATOM   7334  C  CD  . PRO C  1 52  ? 56.892  -2.998  74.911  1.00 22.66  ? 52  PRO C CD  1 
ATOM   7335  N  N   . GLY C  1 53  ? 56.586  -1.404  78.758  1.00 33.79  ? 53  GLY C N   1 
ATOM   7336  C  CA  . GLY C  1 53  ? 56.749  -0.876  80.114  1.00 30.55  ? 53  GLY C CA  1 
ATOM   7337  C  C   . GLY C  1 53  ? 55.413  -0.686  80.822  1.00 31.02  ? 53  GLY C C   1 
ATOM   7338  O  O   . GLY C  1 53  ? 54.350  -0.993  80.248  1.00 27.13  ? 53  GLY C O   1 
ATOM   7339  N  N   . SER C  1 54  ? 55.463  -0.176  82.058  1.00 36.00  ? 54  SER C N   1 
ATOM   7340  C  CA  . SER C  1 54  ? 54.249  0.064   82.863  1.00 36.17  ? 54  SER C CA  1 
ATOM   7341  C  C   . SER C  1 54  ? 53.821  1.480   82.658  1.00 35.62  ? 54  SER C C   1 
ATOM   7342  O  O   . SER C  1 54  ? 54.679  2.343   82.436  1.00 40.52  ? 54  SER C O   1 
ATOM   7343  C  CB  . SER C  1 54  ? 54.547  -0.090  84.354  1.00 40.09  ? 54  SER C CB  1 
ATOM   7344  O  OG  . SER C  1 54  ? 53.395  0.185   85.152  1.00 48.68  ? 54  SER C OG  1 
ATOM   7345  N  N   . SER C  1 55  ? 52.515  1.717   82.752  1.00 31.40  ? 55  SER C N   1 
ATOM   7346  C  CA  . SER C  1 55  ? 51.975  3.053   82.614  1.00 28.93  ? 55  SER C CA  1 
ATOM   7347  C  C   . SER C  1 55  ? 51.563  3.561   83.968  1.00 31.01  ? 55  SER C C   1 
ATOM   7348  O  O   . SER C  1 55  ? 50.746  4.464   84.079  1.00 34.95  ? 55  SER C O   1 
ATOM   7349  C  CB  . SER C  1 55  ? 50.805  3.093   81.651  1.00 31.22  ? 55  SER C CB  1 
ATOM   7350  O  OG  . SER C  1 55  ? 51.182  2.544   80.393  1.00 41.70  ? 55  SER C OG  1 
ATOM   7351  N  N   . ALA C  1 56  ? 52.106  2.950   85.009  1.00 29.47  ? 56  ALA C N   1 
ATOM   7352  C  CA  . ALA C  1 56  ? 51.812  3.395   86.344  1.00 25.71  ? 56  ALA C CA  1 
ATOM   7353  C  C   . ALA C  1 56  ? 52.741  4.534   86.693  1.00 27.03  ? 56  ALA C C   1 
ATOM   7354  O  O   . ALA C  1 56  ? 53.851  4.597   86.185  1.00 28.17  ? 56  ALA C O   1 
ATOM   7355  C  CB  . ALA C  1 56  ? 52.038  2.310   87.282  1.00 25.61  ? 56  ALA C CB  1 
ATOM   7356  N  N   . VAL C  1 57  ? 52.293  5.423   87.566  1.00 28.28  ? 57  VAL C N   1 
ATOM   7357  C  CA  . VAL C  1 57  ? 53.126  6.528   87.998  1.00 31.77  ? 57  VAL C CA  1 
ATOM   7358  C  C   . VAL C  1 57  ? 53.078  6.480   89.507  1.00 34.90  ? 57  VAL C C   1 
ATOM   7359  O  O   . VAL C  1 57  ? 51.989  6.296   90.065  1.00 40.93  ? 57  VAL C O   1 
ATOM   7360  C  CB  . VAL C  1 57  ? 52.550  7.886   87.527  1.00 31.86  ? 57  VAL C CB  1 
ATOM   7361  C  CG1 . VAL C  1 57  ? 53.319  9.059   88.193  1.00 26.84  ? 57  VAL C CG1 1 
ATOM   7362  C  CG2 . VAL C  1 57  ? 52.619  7.990   85.999  1.00 31.56  ? 57  VAL C CG2 1 
ATOM   7363  N  N   . ARG C  1 58  ? 54.222  6.522   90.176  1.00 29.21  ? 58  ARG C N   1 
ATOM   7364  C  CA  . ARG C  1 58  ? 54.155  6.530   91.612  1.00 32.24  ? 58  ARG C CA  1 
ATOM   7365  C  C   . ARG C  1 58  ? 54.348  7.946   92.065  1.00 33.16  ? 58  ARG C C   1 
ATOM   7366  O  O   . ARG C  1 58  ? 55.243  8.613   91.552  1.00 36.51  ? 58  ARG C O   1 
ATOM   7367  C  CB  . ARG C  1 58  ? 55.226  5.649   92.222  1.00 36.46  ? 58  ARG C CB  1 
ATOM   7368  C  CG  . ARG C  1 58  ? 55.270  5.709   93.777  1.00 36.27  ? 58  ARG C CG  1 
ATOM   7369  C  CD  . ARG C  1 58  ? 55.998  4.519   94.372  1.00 41.89  ? 58  ARG C CD  1 
ATOM   7370  N  NE  . ARG C  1 58  ? 57.241  4.245   93.655  1.00 51.54  ? 58  ARG C NE  1 
ATOM   7371  C  CZ  . ARG C  1 58  ? 57.544  3.072   93.103  1.00 56.29  ? 58  ARG C CZ  1 
ATOM   7372  N  NH1 . ARG C  1 58  ? 56.690  2.052   93.193  1.00 59.43  ? 58  ARG C NH1 1 
ATOM   7373  N  NH2 . ARG C  1 58  ? 58.701  2.918   92.458  1.00 59.76  ? 58  ARG C NH2 1 
ATOM   7374  N  N   . TYR C  1 59  ? 53.536  8.411   93.013  1.00 30.33  ? 59  TYR C N   1 
ATOM   7375  C  CA  . TYR C  1 59  ? 53.698  9.773   93.494  1.00 30.20  ? 59  TYR C CA  1 
ATOM   7376  C  C   . TYR C  1 59  ? 53.297  9.919   94.927  1.00 30.73  ? 59  TYR C C   1 
ATOM   7377  O  O   . TYR C  1 59  ? 52.420  9.223   95.411  1.00 31.05  ? 59  TYR C O   1 
ATOM   7378  C  CB  . TYR C  1 59  ? 52.824  10.687  92.706  1.00 22.59  ? 59  TYR C CB  1 
ATOM   7379  C  CG  . TYR C  1 59  ? 51.371  10.443  92.985  1.00 22.58  ? 59  TYR C CG  1 
ATOM   7380  C  CD1 . TYR C  1 59  ? 50.678  9.413   92.358  1.00 23.11  ? 59  TYR C CD1 1 
ATOM   7381  C  CD2 . TYR C  1 59  ? 50.652  11.311  93.785  1.00 20.04  ? 59  TYR C CD2 1 
ATOM   7382  C  CE1 . TYR C  1 59  ? 49.259  9.282   92.505  1.00 22.32  ? 59  TYR C CE1 1 
ATOM   7383  C  CE2 . TYR C  1 59  ? 49.257  11.178  93.951  1.00 22.24  ? 59  TYR C CE2 1 
ATOM   7384  C  CZ  . TYR C  1 59  ? 48.566  10.171  93.301  1.00 21.40  ? 59  TYR C CZ  1 
ATOM   7385  O  OH  . TYR C  1 59  ? 47.187  10.092  93.418  1.00 31.52  ? 59  TYR C OH  1 
ATOM   7386  N  N   . TRP C  1 60  ? 53.830  10.947  95.550  1.00 35.34  ? 60  TRP C N   1 
ATOM   7387  C  CA  . TRP C  1 60  ? 53.527  11.249  96.950  1.00 41.13  ? 60  TRP C CA  1 
ATOM   7388  C  C   . TRP C  1 60  ? 53.950  12.700  97.200  1.00 43.91  ? 60  TRP C C   1 
ATOM   7389  O  O   . TRP C  1 60  ? 54.823  13.238  96.497  1.00 43.63  ? 60  TRP C O   1 
ATOM   7390  C  CB  . TRP C  1 60  ? 54.316  10.332  97.878  1.00 38.60  ? 60  TRP C CB  1 
ATOM   7391  C  CG  . TRP C  1 60  ? 55.807  10.523  97.733  1.00 37.05  ? 60  TRP C CG  1 
ATOM   7392  C  CD1 . TRP C  1 60  ? 56.623  11.312  98.504  1.00 37.09  ? 60  TRP C CD1 1 
ATOM   7393  C  CD2 . TRP C  1 60  ? 56.644  9.940   96.739  1.00 33.72  ? 60  TRP C CD2 1 
ATOM   7394  N  NE1 . TRP C  1 60  ? 57.924  11.260  98.049  1.00 30.71  ? 60  TRP C NE1 1 
ATOM   7395  C  CE2 . TRP C  1 60  ? 57.967  10.418  96.970  1.00 32.99  ? 60  TRP C CE2 1 
ATOM   7396  C  CE3 . TRP C  1 60  ? 56.411  9.057   95.676  1.00 32.74  ? 60  TRP C CE3 1 
ATOM   7397  C  CZ2 . TRP C  1 60  ? 59.053  10.036  96.177  1.00 29.03  ? 60  TRP C CZ2 1 
ATOM   7398  C  CZ3 . TRP C  1 60  ? 57.498  8.675   94.889  1.00 35.05  ? 60  TRP C CZ3 1 
ATOM   7399  C  CH2 . TRP C  1 60  ? 58.809  9.167   95.148  1.00 28.56  ? 60  TRP C CH2 1 
ATOM   7400  N  N   . SER C  1 61  ? 53.367  13.319  98.216  1.00 47.24  ? 61  SER C N   1 
ATOM   7401  C  CA  . SER C  1 61  ? 53.678  14.703  98.515  1.00 48.51  ? 61  SER C CA  1 
ATOM   7402  C  C   . SER C  1 61  ? 54.780  14.752  99.496  1.00 53.60  ? 61  SER C C   1 
ATOM   7403  O  O   . SER C  1 61  ? 54.906  13.864  100.322 1.00 55.89  ? 61  SER C O   1 
ATOM   7404  C  CB  . SER C  1 61  ? 52.483  15.413  99.100  1.00 43.45  ? 61  SER C CB  1 
ATOM   7405  O  OG  . SER C  1 61  ? 52.181  14.894  100.363 1.00 41.29  ? 61  SER C OG  1 
ATOM   7406  N  N   . GLU C  1 62  ? 55.519  15.843  99.459  1.00 63.40  ? 62  GLU C N   1 
ATOM   7407  C  CA  . GLU C  1 62  ? 56.661  16.046  100.335 1.00 75.59  ? 62  GLU C CA  1 
ATOM   7408  C  C   . GLU C  1 62  ? 56.295  15.877  101.806 1.00 81.81  ? 62  GLU C C   1 
ATOM   7409  O  O   . GLU C  1 62  ? 57.069  15.301  102.581 1.00 85.58  ? 62  GLU C O   1 
ATOM   7410  C  CB  . GLU C  1 62  ? 57.257  17.437  100.092 1.00 79.94  ? 62  GLU C CB  1 
ATOM   7411  C  CG  . GLU C  1 62  ? 58.740  17.548  100.414 1.00 85.25  ? 62  GLU C CG  1 
ATOM   7412  C  CD  . GLU C  1 62  ? 59.295  18.917  100.084 1.00 90.64  ? 62  GLU C CD  1 
ATOM   7413  O  OE1 . GLU C  1 62  ? 58.591  19.912  100.368 1.00 96.28  ? 62  GLU C OE1 1 
ATOM   7414  O  OE2 . GLU C  1 62  ? 60.426  18.999  99.540  1.00 94.69  ? 62  GLU C OE2 1 
ATOM   7415  N  N   . LYS C  1 63  ? 55.110  16.362  102.173 1.00 85.32  ? 63  LYS C N   1 
ATOM   7416  C  CA  . LYS C  1 63  ? 54.614  16.283  103.545 1.00 90.27  ? 63  LYS C CA  1 
ATOM   7417  C  C   . LYS C  1 63  ? 54.104  14.885  103.974 1.00 91.66  ? 63  LYS C C   1 
ATOM   7418  O  O   . LYS C  1 63  ? 54.702  14.212  104.826 1.00 93.23  ? 63  LYS C O   1 
ATOM   7419  C  CB  . LYS C  1 63  ? 53.513  17.323  103.736 1.00 95.45  ? 63  LYS C CB  1 
ATOM   7420  C  CG  . LYS C  1 63  ? 52.666  17.572  102.487 1.00 102.64 ? 63  LYS C CG  1 
ATOM   7421  C  CD  . LYS C  1 63  ? 51.262  18.081  102.812 1.00 106.94 ? 63  LYS C CD  1 
ATOM   7422  C  CE  . LYS C  1 63  ? 50.335  16.952  103.310 1.00 109.37 ? 63  LYS C CE  1 
ATOM   7423  N  NZ  . LYS C  1 63  ? 49.981  15.945  102.257 1.00 106.76 ? 63  LYS C NZ  1 
ATOM   7424  N  N   . ASN C  1 64  ? 52.956  14.491  103.431 1.00 91.80  ? 64  ASN C N   1 
ATOM   7425  C  CA  . ASN C  1 64  ? 52.347  13.196  103.709 1.00 90.12  ? 64  ASN C CA  1 
ATOM   7426  C  C   . ASN C  1 64  ? 52.956  12.232  102.685 1.00 88.03  ? 64  ASN C C   1 
ATOM   7427  O  O   . ASN C  1 64  ? 52.434  12.038  101.586 1.00 87.94  ? 64  ASN C O   1 
ATOM   7428  C  CB  . ASN C  1 64  ? 50.816  13.320  103.582 1.00 95.05  ? 64  ASN C CB  1 
ATOM   7429  C  CG  . ASN C  1 64  ? 50.129  12.015  103.181 1.00 100.16 ? 64  ASN C CG  1 
ATOM   7430  O  OD1 . ASN C  1 64  ? 49.467  11.951  102.143 1.00 101.64 ? 64  ASN C OD1 1 
ATOM   7431  N  ND2 . ASN C  1 64  ? 50.251  10.985  104.016 1.00 101.87 ? 64  ASN C ND2 1 
ATOM   7432  N  N   . GLY C  1 65  ? 54.108  11.682  103.039 1.00 84.97  ? 65  GLY C N   1 
ATOM   7433  C  CA  . GLY C  1 65  ? 54.806  10.777  102.153 1.00 83.80  ? 65  GLY C CA  1 
ATOM   7434  C  C   . GLY C  1 65  ? 54.091  9.522   101.681 1.00 84.32  ? 65  GLY C C   1 
ATOM   7435  O  O   . GLY C  1 65  ? 54.770  8.654   101.144 1.00 87.79  ? 65  GLY C O   1 
ATOM   7436  N  N   . ARG C  1 66  ? 52.770  9.399   101.855 1.00 82.22  ? 66  ARG C N   1 
ATOM   7437  C  CA  . ARG C  1 66  ? 52.036  8.192   101.413 1.00 80.35  ? 66  ARG C CA  1 
ATOM   7438  C  C   . ARG C  1 66  ? 52.235  8.042   99.905  1.00 72.67  ? 66  ARG C C   1 
ATOM   7439  O  O   . ARG C  1 66  ? 51.829  8.907   99.143  1.00 73.61  ? 66  ARG C O   1 
ATOM   7440  C  CB  . ARG C  1 66  ? 50.524  8.301   101.749 1.00 91.12  ? 66  ARG C CB  1 
ATOM   7441  C  CG  . ARG C  1 66  ? 49.582  7.210   101.131 1.00 102.94 ? 66  ARG C CG  1 
ATOM   7442  C  CD  . ARG C  1 66  ? 48.087  7.635   101.194 1.00 113.96 ? 66  ARG C CD  1 
ATOM   7443  N  NE  . ARG C  1 66  ? 47.334  7.364   99.950  1.00 124.34 ? 66  ARG C NE  1 
ATOM   7444  C  CZ  . ARG C  1 66  ? 46.651  8.274   99.229  1.00 127.15 ? 66  ARG C CZ  1 
ATOM   7445  N  NH1 . ARG C  1 66  ? 46.593  9.552   99.595  1.00 129.52 ? 66  ARG C NH1 1 
ATOM   7446  N  NH2 . ARG C  1 66  ? 46.042  7.915   98.102  1.00 125.67 ? 66  ARG C NH2 1 
ATOM   7447  N  N   . LYS C  1 67  ? 52.942  6.998   99.488  1.00 64.60  ? 67  LYS C N   1 
ATOM   7448  C  CA  . LYS C  1 67  ? 53.196  6.764   98.079  1.00 55.33  ? 67  LYS C CA  1 
ATOM   7449  C  C   . LYS C  1 67  ? 51.976  6.124   97.482  1.00 53.44  ? 67  LYS C C   1 
ATOM   7450  O  O   . LYS C  1 67  ? 51.470  5.137   97.994  1.00 50.99  ? 67  LYS C O   1 
ATOM   7451  C  CB  . LYS C  1 67  ? 54.418  5.881   97.890  1.00 51.25  ? 67  LYS C CB  1 
ATOM   7452  C  CG  . LYS C  1 67  ? 55.693  6.518   98.444  1.00 56.79  ? 67  LYS C CG  1 
ATOM   7453  C  CD  . LYS C  1 67  ? 56.969  5.775   98.055  1.00 62.64  ? 67  LYS C CD  1 
ATOM   7454  C  CE  . LYS C  1 67  ? 58.246  6.564   98.444  1.00 63.65  ? 67  LYS C CE  1 
ATOM   7455  N  NZ  . LYS C  1 67  ? 59.493  6.015   97.771  1.00 70.54  ? 67  LYS C NZ  1 
ATOM   7456  N  N   . ARG C  1 68  ? 51.460  6.741   96.431  1.00 53.73  ? 68  ARG C N   1 
ATOM   7457  C  CA  . ARG C  1 68  ? 50.272  6.262   95.756  1.00 50.11  ? 68  ARG C CA  1 
ATOM   7458  C  C   . ARG C  1 68  ? 50.652  5.981   94.300  1.00 45.62  ? 68  ARG C C   1 
ATOM   7459  O  O   . ARG C  1 68  ? 51.660  6.502   93.793  1.00 43.31  ? 68  ARG C O   1 
ATOM   7460  C  CB  . ARG C  1 68  ? 49.163  7.325   95.825  1.00 59.13  ? 68  ARG C CB  1 
ATOM   7461  C  CG  . ARG C  1 68  ? 48.922  7.936   97.197  1.00 66.29  ? 68  ARG C CG  1 
ATOM   7462  C  CD  . ARG C  1 68  ? 48.787  9.489   97.172  1.00 79.35  ? 68  ARG C CD  1 
ATOM   7463  N  NE  . ARG C  1 68  ? 49.957  10.172  97.770  1.00 93.25  ? 68  ARG C NE  1 
ATOM   7464  C  CZ  . ARG C  1 68  ? 49.948  11.383  98.344  1.00 96.63  ? 68  ARG C CZ  1 
ATOM   7465  N  NH1 . ARG C  1 68  ? 48.827  12.110  98.404  1.00 100.97 ? 68  ARG C NH1 1 
ATOM   7466  N  NH2 . ARG C  1 68  ? 51.062  11.846  98.909  1.00 94.70  ? 68  ARG C NH2 1 
ATOM   7467  N  N   . ILE C  1 69  ? 49.806  5.197   93.633  1.00 40.52  ? 69  ILE C N   1 
ATOM   7468  C  CA  . ILE C  1 69  ? 49.984  4.805   92.238  1.00 35.13  ? 69  ILE C CA  1 
ATOM   7469  C  C   . ILE C  1 69  ? 48.810  5.148   91.291  1.00 33.97  ? 69  ILE C C   1 
ATOM   7470  O  O   . ILE C  1 69  ? 47.649  4.858   91.584  1.00 32.90  ? 69  ILE C O   1 
ATOM   7471  C  CB  . ILE C  1 69  ? 50.278  3.313   92.164  1.00 33.84  ? 69  ILE C CB  1 
ATOM   7472  C  CG1 . ILE C  1 69  ? 51.768  3.101   92.344  1.00 38.32  ? 69  ILE C CG1 1 
ATOM   7473  C  CG2 . ILE C  1 69  ? 49.818  2.710   90.850  1.00 30.34  ? 69  ILE C CG2 1 
ATOM   7474  C  CD1 . ILE C  1 69  ? 52.172  1.667   92.163  1.00 44.18  ? 69  ILE C CD1 1 
ATOM   7475  N  N   . ALA C  1 70  ? 49.120  5.758   90.154  1.00 31.31  ? 70  ALA C N   1 
ATOM   7476  C  CA  . ALA C  1 70  ? 48.103  6.105   89.191  1.00 31.72  ? 70  ALA C CA  1 
ATOM   7477  C  C   . ALA C  1 70  ? 48.397  5.258   88.014  1.00 34.73  ? 70  ALA C C   1 
ATOM   7478  O  O   . ALA C  1 70  ? 49.561  5.066   87.684  1.00 35.87  ? 70  ALA C O   1 
ATOM   7479  C  CB  . ALA C  1 70  ? 48.236  7.505   88.793  1.00 37.27  ? 70  ALA C CB  1 
ATOM   7480  N  N   . LYS C  1 71  ? 47.358  4.772   87.357  1.00 37.83  ? 71  LYS C N   1 
ATOM   7481  C  CA  . LYS C  1 71  ? 47.580  3.935   86.207  1.00 44.71  ? 71  LYS C CA  1 
ATOM   7482  C  C   . LYS C  1 71  ? 47.085  4.639   84.947  1.00 43.91  ? 71  LYS C C   1 
ATOM   7483  O  O   . LYS C  1 71  ? 45.929  5.066   84.889  1.00 46.34  ? 71  LYS C O   1 
ATOM   7484  C  CB  . LYS C  1 71  ? 46.898  2.554   86.413  1.00 56.95  ? 71  LYS C CB  1 
ATOM   7485  C  CG  . LYS C  1 71  ? 47.837  1.275   86.240  1.00 68.34  ? 71  LYS C CG  1 
ATOM   7486  C  CD  . LYS C  1 71  ? 48.436  1.112   84.774  1.00 76.21  ? 71  LYS C CD  1 
ATOM   7487  C  CE  . LYS C  1 71  ? 49.472  -0.052  84.610  1.00 81.26  ? 71  LYS C CE  1 
ATOM   7488  N  NZ  . LYS C  1 71  ? 50.068  -0.244  83.212  1.00 83.35  ? 71  LYS C NZ  1 
ATOM   7489  N  N   . GLY C  1 72  ? 47.969  4.772   83.957  1.00 39.28  ? 72  GLY C N   1 
ATOM   7490  C  CA  . GLY C  1 72  ? 47.612  5.416   82.698  1.00 35.95  ? 72  GLY C CA  1 
ATOM   7491  C  C   . GLY C  1 72  ? 47.383  4.495   81.505  1.00 31.90  ? 72  GLY C C   1 
ATOM   7492  O  O   . GLY C  1 72  ? 46.928  3.379   81.684  1.00 32.48  ? 72  GLY C O   1 
ATOM   7493  N  N   . LYS C  1 73  ? 47.619  4.992   80.285  1.00 30.57  ? 73  LYS C N   1 
ATOM   7494  C  CA  . LYS C  1 73  ? 47.460  4.187   79.059  1.00 31.47  ? 73  LYS C CA  1 
ATOM   7495  C  C   . LYS C  1 73  ? 48.648  4.318   78.125  1.00 27.27  ? 73  LYS C C   1 
ATOM   7496  O  O   . LYS C  1 73  ? 49.370  5.346   78.142  1.00 32.80  ? 73  LYS C O   1 
ATOM   7497  C  CB  . LYS C  1 73  ? 46.230  4.585   78.252  1.00 41.78  ? 73  LYS C CB  1 
ATOM   7498  C  CG  . LYS C  1 73  ? 44.879  4.370   78.866  1.00 51.16  ? 73  LYS C CG  1 
ATOM   7499  C  CD  . LYS C  1 73  ? 43.839  4.648   77.782  1.00 65.98  ? 73  LYS C CD  1 
ATOM   7500  C  CE  . LYS C  1 73  ? 42.404  4.809   78.339  1.00 78.30  ? 73  LYS C CE  1 
ATOM   7501  N  NZ  . LYS C  1 73  ? 41.332  5.124   77.300  1.00 86.61  ? 73  LYS C NZ  1 
ATOM   7502  N  N   . MET C  1 74  ? 48.757  3.368   77.205  1.00 20.66  ? 74  MET C N   1 
ATOM   7503  C  CA  . MET C  1 74  ? 49.887  3.347   76.286  1.00 28.18  ? 74  MET C CA  1 
ATOM   7504  C  C   . MET C  1 74  ? 49.434  3.360   74.857  1.00 31.79  ? 74  MET C C   1 
ATOM   7505  O  O   . MET C  1 74  ? 48.410  2.744   74.536  1.00 38.29  ? 74  MET C O   1 
ATOM   7506  C  CB  . MET C  1 74  ? 50.726  2.092   76.497  1.00 29.18  ? 74  MET C CB  1 
ATOM   7507  C  CG  . MET C  1 74  ? 51.971  2.105   75.696  1.00 33.08  ? 74  MET C CG  1 
ATOM   7508  S  SD  . MET C  1 74  ? 52.097  0.622   74.881  1.00 37.83  ? 74  MET C SD  1 
ATOM   7509  C  CE  . MET C  1 74  ? 51.365  1.009   73.419  1.00 37.86  ? 74  MET C CE  1 
ATOM   7510  N  N   . SER C  1 75  ? 50.205  4.010   73.986  1.00 28.95  ? 75  SER C N   1 
ATOM   7511  C  CA  . SER C  1 75  ? 49.853  4.081   72.578  1.00 24.58  ? 75  SER C CA  1 
ATOM   7512  C  C   . SER C  1 75  ? 51.084  4.144   71.705  1.00 22.59  ? 75  SER C C   1 
ATOM   7513  O  O   . SER C  1 75  ? 52.191  4.360   72.184  1.00 25.08  ? 75  SER C O   1 
ATOM   7514  C  CB  . SER C  1 75  ? 48.956  5.289   72.309  1.00 30.18  ? 75  SER C CB  1 
ATOM   7515  O  OG  . SER C  1 75  ? 49.242  6.359   73.209  1.00 43.34  ? 75  SER C OG  1 
ATOM   7516  N  N   . THR C  1 76  ? 50.891  3.886   70.428  1.00 14.83  ? 76  THR C N   1 
ATOM   7517  C  CA  . THR C  1 76  ? 51.966  3.941   69.491  1.00 14.24  ? 76  THR C CA  1 
ATOM   7518  C  C   . THR C  1 76  ? 51.363  4.393   68.175  1.00 16.25  ? 76  THR C C   1 
ATOM   7519  O  O   . THR C  1 76  ? 50.147  4.300   67.970  1.00 18.18  ? 76  THR C O   1 
ATOM   7520  C  CB  . THR C  1 76  ? 52.528  2.600   69.301  1.00 19.02  ? 76  THR C CB  1 
ATOM   7521  O  OG1 . THR C  1 76  ? 51.468  1.688   69.034  1.00 28.57  ? 76  THR C OG1 1 
ATOM   7522  C  CG2 . THR C  1 76  ? 53.224  2.164   70.545  1.00 19.75  ? 76  THR C CG2 1 
ATOM   7523  N  N   . TYR C  1 77  ? 52.201  4.909   67.291  1.00 16.28  ? 77  TYR C N   1 
ATOM   7524  C  CA  . TYR C  1 77  ? 51.726  5.387   65.989  1.00 17.64  ? 77  TYR C CA  1 
ATOM   7525  C  C   . TYR C  1 77  ? 52.847  5.227   65.002  1.00 17.97  ? 77  TYR C C   1 
ATOM   7526  O  O   . TYR C  1 77  ? 53.999  5.079   65.391  1.00 23.42  ? 77  TYR C O   1 
ATOM   7527  C  CB  . TYR C  1 77  ? 51.265  6.861   66.051  1.00 21.01  ? 77  TYR C CB  1 
ATOM   7528  C  CG  . TYR C  1 77  ? 52.394  7.932   66.101  1.00 14.53  ? 77  TYR C CG  1 
ATOM   7529  C  CD1 . TYR C  1 77  ? 52.957  8.403   64.921  1.00 10.40  ? 77  TYR C CD1 1 
ATOM   7530  C  CD2 . TYR C  1 77  ? 52.882  8.410   67.317  1.00 10.75  ? 77  TYR C CD2 1 
ATOM   7531  C  CE1 . TYR C  1 77  ? 54.002  9.311   64.948  1.00 9.38   ? 77  TYR C CE1 1 
ATOM   7532  C  CE2 . TYR C  1 77  ? 53.938  9.313   67.341  1.00 9.01   ? 77  TYR C CE2 1 
ATOM   7533  C  CZ  . TYR C  1 77  ? 54.489  9.760   66.155  1.00 6.62   ? 77  TYR C CZ  1 
ATOM   7534  O  OH  . TYR C  1 77  ? 55.596  10.551  66.180  1.00 10.46  ? 77  TYR C OH  1 
ATOM   7535  N  N   . ARG C  1 78  ? 52.506  5.200   63.740  1.00 16.79  ? 78  ARG C N   1 
ATOM   7536  C  CA  . ARG C  1 78  ? 53.513  5.058   62.713  1.00 20.75  ? 78  ARG C CA  1 
ATOM   7537  C  C   . ARG C  1 78  ? 53.294  6.270   61.845  1.00 25.92  ? 78  ARG C C   1 
ATOM   7538  O  O   . ARG C  1 78  ? 52.154  6.636   61.562  1.00 26.20  ? 78  ARG C O   1 
ATOM   7539  C  CB  . ARG C  1 78  ? 53.286  3.828   61.829  1.00 18.84  ? 78  ARG C CB  1 
ATOM   7540  C  CG  . ARG C  1 78  ? 53.488  2.483   62.471  1.00 24.96  ? 78  ARG C CG  1 
ATOM   7541  C  CD  . ARG C  1 78  ? 53.321  1.344   61.480  1.00 18.60  ? 78  ARG C CD  1 
ATOM   7542  N  NE  . ARG C  1 78  ? 54.578  0.659   61.172  1.00 28.30  ? 78  ARG C NE  1 
ATOM   7543  C  CZ  . ARG C  1 78  ? 54.816  -0.619  61.470  1.00 31.80  ? 78  ARG C CZ  1 
ATOM   7544  N  NH1 . ARG C  1 78  ? 53.898  -1.363  62.092  1.00 37.93  ? 78  ARG C NH1 1 
ATOM   7545  N  NH2 . ARG C  1 78  ? 55.946  -1.180  61.085  1.00 34.03  ? 78  ARG C NH2 1 
ATOM   7546  N  N   . PHE C  1 79  ? 54.368  6.919   61.448  1.00 28.13  ? 79  PHE C N   1 
ATOM   7547  C  CA  . PHE C  1 79  ? 54.196  8.051   60.602  1.00 29.51  ? 79  PHE C CA  1 
ATOM   7548  C  C   . PHE C  1 79  ? 54.405  7.657   59.169  1.00 32.57  ? 79  PHE C C   1 
ATOM   7549  O  O   . PHE C  1 79  ? 53.453  7.556   58.431  1.00 45.02  ? 79  PHE C O   1 
ATOM   7550  C  CB  . PHE C  1 79  ? 55.029  9.263   60.992  1.00 31.26  ? 79  PHE C CB  1 
ATOM   7551  C  CG  . PHE C  1 79  ? 54.618  10.502  60.258  1.00 22.54  ? 79  PHE C CG  1 
ATOM   7552  C  CD1 . PHE C  1 79  ? 53.385  11.060  60.483  1.00 16.70  ? 79  PHE C CD1 1 
ATOM   7553  C  CD2 . PHE C  1 79  ? 55.409  11.019  59.253  1.00 26.55  ? 79  PHE C CD2 1 
ATOM   7554  C  CE1 . PHE C  1 79  ? 52.940  12.084  59.723  1.00 17.14  ? 79  PHE C CE1 1 
ATOM   7555  C  CE2 . PHE C  1 79  ? 54.966  12.063  58.475  1.00 21.31  ? 79  PHE C CE2 1 
ATOM   7556  C  CZ  . PHE C  1 79  ? 53.726  12.586  58.715  1.00 17.38  ? 79  PHE C CZ  1 
ATOM   7557  N  N   . PHE C  1 80  ? 55.598  7.457   58.688  1.00 28.47  ? 80  PHE C N   1 
ATOM   7558  C  CA  . PHE C  1 80  ? 55.591  7.044   57.279  1.00 25.43  ? 80  PHE C CA  1 
ATOM   7559  C  C   . PHE C  1 80  ? 56.352  5.743   57.365  1.00 28.23  ? 80  PHE C C   1 
ATOM   7560  O  O   . PHE C  1 80  ? 55.756  4.685   57.604  1.00 25.61  ? 80  PHE C O   1 
ATOM   7561  C  CB  . PHE C  1 80  ? 56.233  8.147   56.432  1.00 25.45  ? 80  PHE C CB  1 
ATOM   7562  C  CG  . PHE C  1 80  ? 56.645  7.725   55.072  1.00 24.99  ? 80  PHE C CG  1 
ATOM   7563  C  CD1 . PHE C  1 80  ? 55.704  7.275   54.144  1.00 26.82  ? 80  PHE C CD1 1 
ATOM   7564  C  CD2 . PHE C  1 80  ? 57.982  7.818   54.696  1.00 23.25  ? 80  PHE C CD2 1 
ATOM   7565  C  CE1 . PHE C  1 80  ? 56.102  6.928   52.853  1.00 25.64  ? 80  PHE C CE1 1 
ATOM   7566  C  CE2 . PHE C  1 80  ? 58.391  7.476   53.423  1.00 22.47  ? 80  PHE C CE2 1 
ATOM   7567  C  CZ  . PHE C  1 80  ? 57.453  7.033   52.498  1.00 24.07  ? 80  PHE C CZ  1 
ATOM   7568  N  N   . ASN C  1 81  ? 57.674  5.828   57.275  1.00 30.99  ? 81  ASN C N   1 
ATOM   7569  C  CA  . ASN C  1 81  ? 58.473  4.650   57.453  1.00 32.53  ? 81  ASN C CA  1 
ATOM   7570  C  C   . ASN C  1 81  ? 58.930  4.707   58.924  1.00 32.88  ? 81  ASN C C   1 
ATOM   7571  O  O   . ASN C  1 81  ? 59.732  3.899   59.332  1.00 39.78  ? 81  ASN C O   1 
ATOM   7572  C  CB  . ASN C  1 81  ? 59.609  4.509   56.382  1.00 33.08  ? 81  ASN C CB  1 
ATOM   7573  C  CG  . ASN C  1 81  ? 60.642  5.652   56.388  1.00 31.09  ? 81  ASN C CG  1 
ATOM   7574  O  OD1 . ASN C  1 81  ? 60.391  6.693   56.976  1.00 29.96  ? 81  ASN C OD1 1 
ATOM   7575  N  ND2 . ASN C  1 81  ? 61.770  5.413   55.680  1.00 39.76  ? 81  ASN C ND2 1 
ATOM   7576  N  N   . TYR C  1 82  ? 58.326  5.597   59.730  1.00 30.68  ? 82  TYR C N   1 
ATOM   7577  C  CA  . TYR C  1 82  ? 58.645  5.772   61.168  1.00 27.92  ? 82  TYR C CA  1 
ATOM   7578  C  C   . TYR C  1 82  ? 57.698  4.955   62.050  1.00 31.01  ? 82  TYR C C   1 
ATOM   7579  O  O   . TYR C  1 82  ? 56.557  4.706   61.657  1.00 35.65  ? 82  TYR C O   1 
ATOM   7580  C  CB  . TYR C  1 82  ? 58.497  7.255   61.596  1.00 26.28  ? 82  TYR C CB  1 
ATOM   7581  C  CG  . TYR C  1 82  ? 58.637  7.560   63.130  1.00 17.45  ? 82  TYR C CG  1 
ATOM   7582  C  CD1 . TYR C  1 82  ? 59.860  7.665   63.720  1.00 8.95   ? 82  TYR C CD1 1 
ATOM   7583  C  CD2 . TYR C  1 82  ? 57.526  7.754   63.972  1.00 13.59  ? 82  TYR C CD2 1 
ATOM   7584  C  CE1 . TYR C  1 82  ? 59.999  7.962   65.090  1.00 11.40  ? 82  TYR C CE1 1 
ATOM   7585  C  CE2 . TYR C  1 82  ? 57.672  8.034   65.351  1.00 13.18  ? 82  TYR C CE2 1 
ATOM   7586  C  CZ  . TYR C  1 82  ? 58.926  8.144   65.897  1.00 14.44  ? 82  TYR C CZ  1 
ATOM   7587  O  OH  . TYR C  1 82  ? 59.148  8.495   67.227  1.00 18.56  ? 82  TYR C OH  1 
ATOM   7588  N  N   . SER C  1 83  ? 58.129  4.640   63.278  1.00 31.80  ? 83  SER C N   1 
ATOM   7589  C  CA  . SER C  1 83  ? 57.326  3.889   64.259  1.00 30.96  ? 83  SER C CA  1 
ATOM   7590  C  C   . SER C  1 83  ? 57.672  4.392   65.658  1.00 31.49  ? 83  SER C C   1 
ATOM   7591  O  O   . SER C  1 83  ? 58.809  4.223   66.150  1.00 31.35  ? 83  SER C O   1 
ATOM   7592  C  CB  . SER C  1 83  ? 57.649  2.402   64.225  1.00 35.71  ? 83  SER C CB  1 
ATOM   7593  O  OG  . SER C  1 83  ? 57.534  1.835   62.930  1.00 47.50  ? 83  SER C OG  1 
ATOM   7594  N  N   . SER C  1 84  ? 56.690  4.963   66.324  1.00 28.02  ? 84  SER C N   1 
ATOM   7595  C  CA  . SER C  1 84  ? 56.917  5.512   67.625  1.00 25.59  ? 84  SER C CA  1 
ATOM   7596  C  C   . SER C  1 84  ? 57.345  4.472   68.611  1.00 24.92  ? 84  SER C C   1 
ATOM   7597  O  O   . SER C  1 84  ? 57.226  3.303   68.372  1.00 25.16  ? 84  SER C O   1 
ATOM   7598  C  CB  . SER C  1 84  ? 55.609  6.041   68.128  1.00 25.23  ? 84  SER C CB  1 
ATOM   7599  O  OG  . SER C  1 84  ? 54.723  4.968   68.315  1.00 29.42  ? 84  SER C OG  1 
ATOM   7600  N  N   . GLY C  1 85  ? 57.848  4.930   69.742  1.00 27.12  ? 85  GLY C N   1 
ATOM   7601  C  CA  . GLY C  1 85  ? 58.177  4.032   70.823  1.00 15.25  ? 85  GLY C CA  1 
ATOM   7602  C  C   . GLY C  1 85  ? 56.837  3.884   71.536  1.00 20.25  ? 85  GLY C C   1 
ATOM   7603  O  O   . GLY C  1 85  ? 55.771  4.122   70.947  1.00 20.79  ? 85  GLY C O   1 
ATOM   7604  N  N   . PHE C  1 86  ? 56.859  3.622   72.820  1.00 19.22  ? 86  PHE C N   1 
ATOM   7605  C  CA  . PHE C  1 86  ? 55.620  3.413   73.508  1.00 23.82  ? 86  PHE C CA  1 
ATOM   7606  C  C   . PHE C  1 86  ? 55.315  4.655   74.280  1.00 27.79  ? 86  PHE C C   1 
ATOM   7607  O  O   . PHE C  1 86  ? 56.007  5.004   75.233  1.00 32.46  ? 86  PHE C O   1 
ATOM   7608  C  CB  . PHE C  1 86  ? 55.726  2.151   74.364  1.00 22.67  ? 86  PHE C CB  1 
ATOM   7609  C  CG  . PHE C  1 86  ? 56.214  0.971   73.592  1.00 20.38  ? 86  PHE C CG  1 
ATOM   7610  C  CD1 . PHE C  1 86  ? 55.363  0.257   72.745  1.00 19.19  ? 86  PHE C CD1 1 
ATOM   7611  C  CD2 . PHE C  1 86  ? 57.540  0.638   73.615  1.00 22.55  ? 86  PHE C CD2 1 
ATOM   7612  C  CE1 . PHE C  1 86  ? 55.850  -0.770  71.921  1.00 15.00  ? 86  PHE C CE1 1 
ATOM   7613  C  CE2 . PHE C  1 86  ? 58.027  -0.402  72.780  1.00 23.93  ? 86  PHE C CE2 1 
ATOM   7614  C  CZ  . PHE C  1 86  ? 57.179  -1.089  71.941  1.00 13.26  ? 86  PHE C CZ  1 
ATOM   7615  N  N   . ILE C  1 87  ? 54.250  5.325   73.860  1.00 28.29  ? 87  ILE C N   1 
ATOM   7616  C  CA  . ILE C  1 87  ? 53.843  6.585   74.467  1.00 24.09  ? 87  ILE C CA  1 
ATOM   7617  C  C   . ILE C  1 87  ? 52.940  6.334   75.652  1.00 24.53  ? 87  ILE C C   1 
ATOM   7618  O  O   . ILE C  1 87  ? 51.943  5.628   75.519  1.00 26.18  ? 87  ILE C O   1 
ATOM   7619  C  CB  . ILE C  1 87  ? 53.133  7.441   73.425  1.00 22.03  ? 87  ILE C CB  1 
ATOM   7620  C  CG1 . ILE C  1 87  ? 54.056  7.629   72.207  1.00 20.34  ? 87  ILE C CG1 1 
ATOM   7621  C  CG2 . ILE C  1 87  ? 52.795  8.779   73.987  1.00 25.61  ? 87  ILE C CG2 1 
ATOM   7622  C  CD1 . ILE C  1 87  ? 53.426  8.357   71.032  1.00 20.69  ? 87  ILE C CD1 1 
ATOM   7623  N  N   . HIS C  1 88  ? 53.224  6.970   76.786  1.00 21.52  ? 88  HIS C N   1 
ATOM   7624  C  CA  . HIS C  1 88  ? 52.417  6.742   77.965  1.00 18.49  ? 88  HIS C CA  1 
ATOM   7625  C  C   . HIS C  1 88  ? 51.788  7.991   78.428  1.00 21.42  ? 88  HIS C C   1 
ATOM   7626  O  O   . HIS C  1 88  ? 52.455  9.013   78.509  1.00 27.26  ? 88  HIS C O   1 
ATOM   7627  C  CB  . HIS C  1 88  ? 53.310  6.244   79.093  1.00 27.50  ? 88  HIS C CB  1 
ATOM   7628  C  CG  . HIS C  1 88  ? 53.946  4.917   78.834  1.00 29.78  ? 88  HIS C CG  1 
ATOM   7629  N  ND1 . HIS C  1 88  ? 55.211  4.784   78.305  1.00 34.62  ? 88  HIS C ND1 1 
ATOM   7630  C  CD2 . HIS C  1 88  ? 53.479  3.649   78.973  1.00 22.90  ? 88  HIS C CD2 1 
ATOM   7631  C  CE1 . HIS C  1 88  ? 55.497  3.506   78.121  1.00 23.17  ? 88  HIS C CE1 1 
ATOM   7632  N  NE2 . HIS C  1 88  ? 54.465  2.796   78.521  1.00 28.98  ? 88  HIS C NE2 1 
ATOM   7633  N  N   . HIS C  1 89  ? 50.544  7.911   78.855  1.00 23.96  ? 89  HIS C N   1 
ATOM   7634  C  CA  . HIS C  1 89  ? 49.845  9.094   79.368  1.00 24.27  ? 89  HIS C CA  1 
ATOM   7635  C  C   . HIS C  1 89  ? 49.023  8.670   80.606  1.00 26.97  ? 89  HIS C C   1 
ATOM   7636  O  O   . HIS C  1 89  ? 48.067  7.896   80.512  1.00 29.03  ? 89  HIS C O   1 
ATOM   7637  C  CB  . HIS C  1 89  ? 48.891  9.665   78.307  1.00 20.94  ? 89  HIS C CB  1 
ATOM   7638  C  CG  . HIS C  1 89  ? 49.562  10.274  77.106  1.00 19.74  ? 89  HIS C CG  1 
ATOM   7639  N  ND1 . HIS C  1 89  ? 50.367  11.398  77.178  1.00 17.30  ? 89  HIS C ND1 1 
ATOM   7640  C  CD2 . HIS C  1 89  ? 49.479  9.953   75.790  1.00 23.65  ? 89  HIS C CD2 1 
ATOM   7641  C  CE1 . HIS C  1 89  ? 50.745  11.735  75.959  1.00 24.46  ? 89  HIS C CE1 1 
ATOM   7642  N  NE2 . HIS C  1 89  ? 50.223  10.875  75.096  1.00 21.74  ? 89  HIS C NE2 1 
ATOM   7643  N  N   . THR C  1 90  ? 49.376  9.212   81.752  1.00 23.42  ? 90  THR C N   1 
ATOM   7644  C  CA  . THR C  1 90  ? 48.705  8.872   82.973  1.00 24.93  ? 90  THR C CA  1 
ATOM   7645  C  C   . THR C  1 90  ? 48.276  10.155  83.622  1.00 27.39  ? 90  THR C C   1 
ATOM   7646  O  O   . THR C  1 90  ? 49.080  11.098  83.715  1.00 28.47  ? 90  THR C O   1 
ATOM   7647  C  CB  . THR C  1 90  ? 49.698  8.151   83.911  1.00 25.09  ? 90  THR C CB  1 
ATOM   7648  O  OG1 . THR C  1 90  ? 50.162  6.972   83.256  1.00 21.76  ? 90  THR C OG1 1 
ATOM   7649  C  CG2 . THR C  1 90  ? 49.052  7.783   85.259  1.00 25.05  ? 90  THR C CG2 1 
ATOM   7650  N  N   . THR C  1 91  ? 47.062  10.152  84.170  1.00 29.21  ? 91  THR C N   1 
ATOM   7651  C  CA  . THR C  1 91  ? 46.516  11.337  84.816  1.00 33.54  ? 91  THR C CA  1 
ATOM   7652  C  C   . THR C  1 91  ? 46.412  11.140  86.335  1.00 36.31  ? 91  THR C C   1 
ATOM   7653  O  O   . THR C  1 91  ? 45.781  10.204  86.831  1.00 42.49  ? 91  THR C O   1 
ATOM   7654  C  CB  . THR C  1 91  ? 45.125  11.667  84.233  1.00 35.76  ? 91  THR C CB  1 
ATOM   7655  O  OG1 . THR C  1 91  ? 45.170  11.719  82.796  1.00 34.07  ? 91  THR C OG1 1 
ATOM   7656  C  CG2 . THR C  1 91  ? 44.637  12.959  84.737  1.00 33.84  ? 91  THR C CG2 1 
ATOM   7657  N  N   . ILE C  1 92  ? 47.055  12.010  87.085  1.00 37.23  ? 92  ILE C N   1 
ATOM   7658  C  CA  . ILE C  1 92  ? 47.019  11.927  88.517  1.00 35.61  ? 92  ILE C CA  1 
ATOM   7659  C  C   . ILE C  1 92  ? 45.933  12.902  88.985  1.00 41.26  ? 92  ILE C C   1 
ATOM   7660  O  O   . ILE C  1 92  ? 45.991  14.104  88.670  1.00 42.86  ? 92  ILE C O   1 
ATOM   7661  C  CB  . ILE C  1 92  ? 48.325  12.402  89.062  1.00 33.42  ? 92  ILE C CB  1 
ATOM   7662  C  CG1 . ILE C  1 92  ? 49.456  11.555  88.553  1.00 31.13  ? 92  ILE C CG1 1 
ATOM   7663  C  CG2 . ILE C  1 92  ? 48.320  12.292  90.520  1.00 40.04  ? 92  ILE C CG2 1 
ATOM   7664  C  CD1 . ILE C  1 92  ? 50.724  12.057  89.100  1.00 27.33  ? 92  ILE C CD1 1 
ATOM   7665  N  N   . ARG C  1 93  ? 44.976  12.428  89.776  1.00 44.64  ? 93  ARG C N   1 
ATOM   7666  C  CA  . ARG C  1 93  ? 43.899  13.314  90.226  1.00 45.23  ? 93  ARG C CA  1 
ATOM   7667  C  C   . ARG C  1 93  ? 43.862  13.641  91.685  1.00 48.46  ? 93  ARG C C   1 
ATOM   7668  O  O   . ARG C  1 93  ? 44.593  13.065  92.495  1.00 51.43  ? 93  ARG C O   1 
ATOM   7669  C  CB  . ARG C  1 93  ? 42.542  12.746  89.869  1.00 41.36  ? 93  ARG C CB  1 
ATOM   7670  C  CG  . ARG C  1 93  ? 42.318  12.697  88.433  1.00 51.08  ? 93  ARG C CG  1 
ATOM   7671  C  CD  . ARG C  1 93  ? 41.357  11.599  88.037  1.00 64.66  ? 93  ARG C CD  1 
ATOM   7672  N  NE  . ARG C  1 93  ? 41.173  11.597  86.579  1.00 75.77  ? 93  ARG C NE  1 
ATOM   7673  C  CZ  . ARG C  1 93  ? 40.670  12.621  85.878  1.00 81.00  ? 93  ARG C CZ  1 
ATOM   7674  N  NH1 . ARG C  1 93  ? 40.266  13.746  86.481  1.00 87.21  ? 93  ARG C NH1 1 
ATOM   7675  N  NH2 . ARG C  1 93  ? 40.640  12.558  84.554  1.00 84.47  ? 93  ARG C NH2 1 
ATOM   7676  N  N   . LYS C  1 94  ? 42.971  14.575  92.004  1.00 50.61  ? 94  LYS C N   1 
ATOM   7677  C  CA  . LYS C  1 94  ? 42.748  15.008  93.367  1.00 50.42  ? 94  LYS C CA  1 
ATOM   7678  C  C   . LYS C  1 94  ? 44.005  15.392  94.148  1.00 45.86  ? 94  LYS C C   1 
ATOM   7679  O  O   . LYS C  1 94  ? 44.225  14.900  95.253  1.00 53.35  ? 94  LYS C O   1 
ATOM   7680  C  CB  . LYS C  1 94  ? 41.959  13.926  94.106  1.00 56.08  ? 94  LYS C CB  1 
ATOM   7681  C  CG  . LYS C  1 94  ? 40.635  13.599  93.426  1.00 72.96  ? 94  LYS C CG  1 
ATOM   7682  C  CD  . LYS C  1 94  ? 39.805  12.547  94.194  1.00 84.57  ? 94  LYS C CD  1 
ATOM   7683  C  CE  . LYS C  1 94  ? 39.521  11.257  93.350  1.00 95.07  ? 94  LYS C CE  1 
ATOM   7684  N  NZ  . LYS C  1 94  ? 38.640  11.354  92.112  1.00 99.38  ? 94  LYS C NZ  1 
ATOM   7685  N  N   . LEU C  1 95  ? 44.843  16.239  93.576  1.00 39.90  ? 95  LEU C N   1 
ATOM   7686  C  CA  . LEU C  1 95  ? 46.030  16.672  94.282  1.00 40.05  ? 95  LEU C CA  1 
ATOM   7687  C  C   . LEU C  1 95  ? 45.642  17.795  95.250  1.00 43.99  ? 95  LEU C C   1 
ATOM   7688  O  O   . LEU C  1 95  ? 44.562  18.374  95.142  1.00 43.69  ? 95  LEU C O   1 
ATOM   7689  C  CB  . LEU C  1 95  ? 47.039  17.212  93.293  1.00 39.42  ? 95  LEU C CB  1 
ATOM   7690  C  CG  . LEU C  1 95  ? 47.365  16.254  92.167  1.00 38.84  ? 95  LEU C CG  1 
ATOM   7691  C  CD1 . LEU C  1 95  ? 48.343  16.874  91.216  1.00 43.64  ? 95  LEU C CD1 1 
ATOM   7692  C  CD2 . LEU C  1 95  ? 47.962  15.059  92.777  1.00 33.27  ? 95  LEU C CD2 1 
ATOM   7693  N  N   . LYS C  1 96  ? 46.500  18.080  96.222  1.00 49.29  ? 96  LYS C N   1 
ATOM   7694  C  CA  . LYS C  1 96  ? 46.240  19.159  97.175  1.00 47.39  ? 96  LYS C CA  1 
ATOM   7695  C  C   . LYS C  1 96  ? 46.868  20.361  96.494  1.00 41.71  ? 96  LYS C C   1 
ATOM   7696  O  O   . LYS C  1 96  ? 47.833  20.212  95.751  1.00 36.83  ? 96  LYS C O   1 
ATOM   7697  C  CB  . LYS C  1 96  ? 46.919  18.897  98.534  1.00 58.62  ? 96  LYS C CB  1 
ATOM   7698  C  CG  . LYS C  1 96  ? 46.019  18.226  99.621  1.00 73.40  ? 96  LYS C CG  1 
ATOM   7699  C  CD  . LYS C  1 96  ? 46.181  16.691  99.731  1.00 86.80  ? 96  LYS C CD  1 
ATOM   7700  C  CE  . LYS C  1 96  ? 47.494  16.253  100.449 1.00 96.69  ? 96  LYS C CE  1 
ATOM   7701  N  NZ  . LYS C  1 96  ? 47.788  14.749  100.412 1.00 97.67  ? 96  LYS C NZ  1 
ATOM   7702  N  N   . TYR C  1 97  ? 46.283  21.539  96.684  1.00 40.29  ? 97  TYR C N   1 
ATOM   7703  C  CA  . TYR C  1 97  ? 46.811  22.750  96.059  1.00 35.33  ? 97  TYR C CA  1 
ATOM   7704  C  C   . TYR C  1 97  ? 48.065  23.177  96.743  1.00 35.94  ? 97  TYR C C   1 
ATOM   7705  O  O   . TYR C  1 97  ? 48.291  22.847  97.890  1.00 37.15  ? 97  TYR C O   1 
ATOM   7706  C  CB  . TYR C  1 97  ? 45.842  23.904  96.142  1.00 29.61  ? 97  TYR C CB  1 
ATOM   7707  C  CG  . TYR C  1 97  ? 44.613  23.779  95.289  1.00 36.36  ? 97  TYR C CG  1 
ATOM   7708  C  CD1 . TYR C  1 97  ? 44.646  24.078  93.923  1.00 37.52  ? 97  TYR C CD1 1 
ATOM   7709  C  CD2 . TYR C  1 97  ? 43.385  23.460  95.862  1.00 35.53  ? 97  TYR C CD2 1 
ATOM   7710  C  CE1 . TYR C  1 97  ? 43.477  24.076  93.166  1.00 42.46  ? 97  TYR C CE1 1 
ATOM   7711  C  CE2 . TYR C  1 97  ? 42.222  23.453  95.112  1.00 41.47  ? 97  TYR C CE2 1 
ATOM   7712  C  CZ  . TYR C  1 97  ? 42.270  23.769  93.780  1.00 42.32  ? 97  TYR C CZ  1 
ATOM   7713  O  OH  . TYR C  1 97  ? 41.078  23.871  93.106  1.00 51.67  ? 97  TYR C OH  1 
ATOM   7714  N  N   . ASN C  1 98  ? 48.907  23.886  96.014  1.00 40.32  ? 98  ASN C N   1 
ATOM   7715  C  CA  . ASN C  1 98  ? 50.150  24.392  96.560  1.00 44.80  ? 98  ASN C CA  1 
ATOM   7716  C  C   . ASN C  1 98  ? 50.948  23.347  97.342  1.00 46.55  ? 98  ASN C C   1 
ATOM   7717  O  O   . ASN C  1 98  ? 51.281  23.555  98.505  1.00 49.81  ? 98  ASN C O   1 
ATOM   7718  C  CB  . ASN C  1 98  ? 49.831  25.582  97.458  1.00 50.19  ? 98  ASN C CB  1 
ATOM   7719  C  CG  . ASN C  1 98  ? 51.003  26.565  97.592  1.00 60.48  ? 98  ASN C CG  1 
ATOM   7720  O  OD1 . ASN C  1 98  ? 51.695  26.902  96.612  1.00 65.34  ? 98  ASN C OD1 1 
ATOM   7721  N  ND2 . ASN C  1 98  ? 51.201  27.067  98.806  1.00 66.19  ? 98  ASN C ND2 1 
ATOM   7722  N  N   . THR C  1 99  ? 51.285  22.232  96.704  1.00 44.32  ? 99  THR C N   1 
ATOM   7723  C  CA  . THR C  1 99  ? 52.038  21.193  97.378  1.00 38.02  ? 99  THR C CA  1 
ATOM   7724  C  C   . THR C  1 99  ? 53.069  20.650  96.425  1.00 36.81  ? 99  THR C C   1 
ATOM   7725  O  O   . THR C  1 99  ? 52.799  20.553  95.225  1.00 38.97  ? 99  THR C O   1 
ATOM   7726  C  CB  . THR C  1 99  ? 51.119  20.072  97.711  1.00 38.70  ? 99  THR C CB  1 
ATOM   7727  O  OG1 . THR C  1 99  ? 50.027  20.566  98.479  1.00 45.35  ? 99  THR C OG1 1 
ATOM   7728  C  CG2 . THR C  1 99  ? 51.845  19.032  98.494  1.00 39.74  ? 99  THR C CG2 1 
ATOM   7729  N  N   . LYS C  1 100 ? 54.267  20.355  96.918  1.00 36.13  ? 100 LYS C N   1 
ATOM   7730  C  CA  . LYS C  1 100 ? 55.286  19.772  96.033  1.00 35.80  ? 100 LYS C CA  1 
ATOM   7731  C  C   . LYS C  1 100 ? 54.986  18.289  96.022  1.00 39.44  ? 100 LYS C C   1 
ATOM   7732  O  O   . LYS C  1 100 ? 54.669  17.706  97.066  1.00 46.73  ? 100 LYS C O   1 
ATOM   7733  C  CB  . LYS C  1 100 ? 56.706  19.952  96.575  1.00 32.23  ? 100 LYS C CB  1 
ATOM   7734  C  CG  . LYS C  1 100 ? 57.788  19.420  95.654  1.00 27.99  ? 100 LYS C CG  1 
ATOM   7735  C  CD  . LYS C  1 100 ? 59.161  19.689  96.247  1.00 27.41  ? 100 LYS C CD  1 
ATOM   7736  C  CE  . LYS C  1 100 ? 60.236  19.659  95.188  1.00 38.02  ? 100 LYS C CE  1 
ATOM   7737  N  NZ  . LYS C  1 100 ? 61.596  19.976  95.732  1.00 47.90  ? 100 LYS C NZ  1 
ATOM   7738  N  N   . TYR C  1 101 ? 55.029  17.686  94.850  1.00 37.93  ? 101 TYR C N   1 
ATOM   7739  C  CA  . TYR C  1 101 ? 54.802  16.273  94.720  1.00 33.85  ? 101 TYR C CA  1 
ATOM   7740  C  C   . TYR C  1 101 ? 55.979  15.662  94.027  1.00 34.15  ? 101 TYR C C   1 
ATOM   7741  O  O   . TYR C  1 101 ? 56.659  16.333  93.239  1.00 36.23  ? 101 TYR C O   1 
ATOM   7742  C  CB  . TYR C  1 101 ? 53.619  16.049  93.855  1.00 32.47  ? 101 TYR C CB  1 
ATOM   7743  C  CG  . TYR C  1 101 ? 52.370  16.149  94.610  1.00 39.18  ? 101 TYR C CG  1 
ATOM   7744  C  CD1 . TYR C  1 101 ? 51.835  15.021  95.209  1.00 47.46  ? 101 TYR C CD1 1 
ATOM   7745  C  CD2 . TYR C  1 101 ? 51.690  17.349  94.726  1.00 41.44  ? 101 TYR C CD2 1 
ATOM   7746  C  CE1 . TYR C  1 101 ? 50.632  15.082  95.914  1.00 50.52  ? 101 TYR C CE1 1 
ATOM   7747  C  CE2 . TYR C  1 101 ? 50.489  17.425  95.431  1.00 44.24  ? 101 TYR C CE2 1 
ATOM   7748  C  CZ  . TYR C  1 101 ? 49.977  16.289  96.015  1.00 46.33  ? 101 TYR C CZ  1 
ATOM   7749  O  OH  . TYR C  1 101 ? 48.814  16.327  96.707  1.00 49.14  ? 101 TYR C OH  1 
ATOM   7750  N  N   . TYR C  1 102 ? 56.245  14.401  94.350  1.00 33.70  ? 102 TYR C N   1 
ATOM   7751  C  CA  . TYR C  1 102 ? 57.311  13.652  93.712  1.00 29.74  ? 102 TYR C CA  1 
ATOM   7752  C  C   . TYR C  1 102 ? 56.615  12.593  92.921  1.00 28.95  ? 102 TYR C C   1 
ATOM   7753  O  O   . TYR C  1 102 ? 55.574  12.055  93.366  1.00 30.90  ? 102 TYR C O   1 
ATOM   7754  C  CB  . TYR C  1 102 ? 58.172  12.975  94.730  1.00 31.29  ? 102 TYR C CB  1 
ATOM   7755  C  CG  . TYR C  1 102 ? 59.098  13.916  95.384  1.00 41.35  ? 102 TYR C CG  1 
ATOM   7756  C  CD1 . TYR C  1 102 ? 60.223  14.391  94.707  1.00 48.66  ? 102 TYR C CD1 1 
ATOM   7757  C  CD2 . TYR C  1 102 ? 58.863  14.372  96.662  1.00 45.74  ? 102 TYR C CD2 1 
ATOM   7758  C  CE1 . TYR C  1 102 ? 61.107  15.309  95.296  1.00 46.51  ? 102 TYR C CE1 1 
ATOM   7759  C  CE2 . TYR C  1 102 ? 59.738  15.303  97.266  1.00 46.48  ? 102 TYR C CE2 1 
ATOM   7760  C  CZ  . TYR C  1 102 ? 60.855  15.764  96.571  1.00 47.46  ? 102 TYR C CZ  1 
ATOM   7761  O  OH  . TYR C  1 102 ? 61.709  16.702  97.123  1.00 60.37  ? 102 TYR C OH  1 
ATOM   7762  N  N   . TYR C  1 103 ? 57.119  12.345  91.722  1.00 26.30  ? 103 TYR C N   1 
ATOM   7763  C  CA  . TYR C  1 103 ? 56.549  11.298  90.908  1.00 24.78  ? 103 TYR C CA  1 
ATOM   7764  C  C   . TYR C  1 103 ? 57.702  10.521  90.283  1.00 28.04  ? 103 TYR C C   1 
ATOM   7765  O  O   . TYR C  1 103 ? 58.806  11.054  90.055  1.00 26.52  ? 103 TYR C O   1 
ATOM   7766  C  CB  . TYR C  1 103 ? 55.512  11.817  89.881  1.00 22.04  ? 103 TYR C CB  1 
ATOM   7767  C  CG  . TYR C  1 103 ? 56.036  12.618  88.692  1.00 27.33  ? 103 TYR C CG  1 
ATOM   7768  C  CD1 . TYR C  1 103 ? 56.404  11.980  87.508  1.00 27.88  ? 103 TYR C CD1 1 
ATOM   7769  C  CD2 . TYR C  1 103 ? 56.160  14.003  88.739  1.00 28.16  ? 103 TYR C CD2 1 
ATOM   7770  C  CE1 . TYR C  1 103 ? 56.888  12.683  86.398  1.00 23.46  ? 103 TYR C CE1 1 
ATOM   7771  C  CE2 . TYR C  1 103 ? 56.650  14.714  87.622  1.00 26.48  ? 103 TYR C CE2 1 
ATOM   7772  C  CZ  . TYR C  1 103 ? 57.015  14.034  86.459  1.00 23.07  ? 103 TYR C CZ  1 
ATOM   7773  O  OH  . TYR C  1 103 ? 57.572  14.678  85.378  1.00 21.74  ? 103 TYR C OH  1 
ATOM   7774  N  N   . GLU C  1 104 ? 57.483  9.215   90.172  1.00 30.92  ? 104 GLU C N   1 
ATOM   7775  C  CA  . GLU C  1 104 ? 58.444  8.321   89.582  1.00 28.17  ? 104 GLU C CA  1 
ATOM   7776  C  C   . GLU C  1 104 ? 57.738  7.633   88.436  1.00 25.85  ? 104 GLU C C   1 
ATOM   7777  O  O   . GLU C  1 104 ? 56.588  7.213   88.527  1.00 28.71  ? 104 GLU C O   1 
ATOM   7778  C  CB  . GLU C  1 104 ? 58.926  7.321   90.613  1.00 37.58  ? 104 GLU C CB  1 
ATOM   7779  C  CG  . GLU C  1 104 ? 59.840  7.921   91.665  1.00 44.70  ? 104 GLU C CG  1 
ATOM   7780  C  CD  . GLU C  1 104 ? 60.316  6.894   92.663  1.00 49.75  ? 104 GLU C CD  1 
ATOM   7781  O  OE1 . GLU C  1 104 ? 59.487  6.193   93.297  1.00 55.29  ? 104 GLU C OE1 1 
ATOM   7782  O  OE2 . GLU C  1 104 ? 61.543  6.778   92.808  1.00 60.14  ? 104 GLU C OE2 1 
ATOM   7783  N  N   . VAL C  1 105 ? 58.483  7.437   87.380  1.00 24.63  ? 105 VAL C N   1 
ATOM   7784  C  CA  . VAL C  1 105 ? 57.948  6.869   86.196  1.00 25.41  ? 105 VAL C CA  1 
ATOM   7785  C  C   . VAL C  1 105 ? 58.987  5.817   85.723  1.00 31.31  ? 105 VAL C C   1 
ATOM   7786  O  O   . VAL C  1 105 ? 60.190  6.005   85.903  1.00 37.38  ? 105 VAL C O   1 
ATOM   7787  C  CB  . VAL C  1 105 ? 57.773  8.054   85.259  1.00 22.72  ? 105 VAL C CB  1 
ATOM   7788  C  CG1 . VAL C  1 105 ? 58.868  8.139   84.256  1.00 23.81  ? 105 VAL C CG1 1 
ATOM   7789  C  CG2 . VAL C  1 105 ? 56.418  8.075   84.694  1.00 24.57  ? 105 VAL C CG2 1 
ATOM   7790  N  N   . GLY C  1 106 ? 58.526  4.703   85.168  1.00 29.54  ? 106 GLY C N   1 
ATOM   7791  C  CA  . GLY C  1 106 ? 59.430  3.656   84.731  1.00 30.46  ? 106 GLY C CA  1 
ATOM   7792  C  C   . GLY C  1 106 ? 59.599  2.639   85.843  1.00 29.87  ? 106 GLY C C   1 
ATOM   7793  O  O   . GLY C  1 106 ? 60.678  2.110   86.078  1.00 30.35  ? 106 GLY C O   1 
ATOM   7794  N  N   . LEU C  1 107 ? 58.497  2.292   86.477  1.00 30.81  ? 107 LEU C N   1 
ATOM   7795  C  CA  . LEU C  1 107 ? 58.522  1.368   87.593  1.00 34.06  ? 107 LEU C CA  1 
ATOM   7796  C  C   . LEU C  1 107 ? 59.048  -0.026  87.346  1.00 39.47  ? 107 LEU C C   1 
ATOM   7797  O  O   . LEU C  1 107 ? 59.640  -0.601  88.246  1.00 45.01  ? 107 LEU C O   1 
ATOM   7798  C  CB  . LEU C  1 107 ? 57.152  1.249   88.231  1.00 30.17  ? 107 LEU C CB  1 
ATOM   7799  C  CG  . LEU C  1 107 ? 56.363  2.509   88.544  1.00 29.16  ? 107 LEU C CG  1 
ATOM   7800  C  CD1 . LEU C  1 107 ? 55.227  2.118   89.435  1.00 33.56  ? 107 LEU C CD1 1 
ATOM   7801  C  CD2 . LEU C  1 107 ? 57.210  3.568   89.221  1.00 25.58  ? 107 LEU C CD2 1 
ATOM   7802  N  N   . ARG C  1 108 ? 58.768  -0.617  86.189  1.00 44.47  ? 108 ARG C N   1 
ATOM   7803  C  CA  . ARG C  1 108 ? 59.276  -1.974  85.905  1.00 46.82  ? 108 ARG C CA  1 
ATOM   7804  C  C   . ARG C  1 108 ? 60.813  -2.089  85.766  1.00 47.04  ? 108 ARG C C   1 
ATOM   7805  O  O   . ARG C  1 108 ? 61.428  -2.932  86.383  1.00 50.30  ? 108 ARG C O   1 
ATOM   7806  C  CB  . ARG C  1 108 ? 58.618  -2.568  84.656  1.00 51.17  ? 108 ARG C CB  1 
ATOM   7807  C  CG  . ARG C  1 108 ? 57.414  -3.450  84.930  1.00 56.64  ? 108 ARG C CG  1 
ATOM   7808  C  CD  . ARG C  1 108 ? 56.809  -4.032  83.622  1.00 70.37  ? 108 ARG C CD  1 
ATOM   7809  N  NE  . ARG C  1 108 ? 57.562  -5.138  82.990  1.00 83.90  ? 108 ARG C NE  1 
ATOM   7810  C  CZ  . ARG C  1 108 ? 58.638  -5.007  82.197  1.00 91.96  ? 108 ARG C CZ  1 
ATOM   7811  N  NH1 . ARG C  1 108 ? 59.140  -3.795  81.915  1.00 97.17  ? 108 ARG C NH1 1 
ATOM   7812  N  NH2 . ARG C  1 108 ? 59.202  -6.095  81.650  1.00 95.45  ? 108 ARG C NH2 1 
ATOM   7813  N  N   . ASN C  1 109 ? 61.454  -1.270  84.954  1.00 46.73  ? 109 ASN C N   1 
ATOM   7814  C  CA  . ASN C  1 109 ? 62.876  -1.430  84.863  1.00 43.04  ? 109 ASN C CA  1 
ATOM   7815  C  C   . ASN C  1 109 ? 63.683  -0.273  85.393  1.00 43.69  ? 109 ASN C C   1 
ATOM   7816  O  O   . ASN C  1 109 ? 64.102  -0.313  86.533  1.00 50.17  ? 109 ASN C O   1 
ATOM   7817  C  CB  . ASN C  1 109 ? 63.280  -1.840  83.463  1.00 44.78  ? 109 ASN C CB  1 
ATOM   7818  C  CG  . ASN C  1 109 ? 62.794  -3.203  83.134  1.00 44.89  ? 109 ASN C CG  1 
ATOM   7819  O  OD1 . ASN C  1 109 ? 61.707  -3.316  82.587  1.00 45.36  ? 109 ASN C OD1 1 
ATOM   7820  N  ND2 . ASN C  1 109 ? 63.579  -4.224  83.511  1.00 54.62  ? 109 ASN C ND2 1 
ATOM   7821  N  N   . THR C  1 110 ? 63.891  0.766   84.604  1.00 42.07  ? 110 THR C N   1 
ATOM   7822  C  CA  . THR C  1 110 ? 64.679  1.907   85.059  1.00 37.12  ? 110 THR C CA  1 
ATOM   7823  C  C   . THR C  1 110 ? 63.727  3.028   85.516  1.00 37.01  ? 110 THR C C   1 
ATOM   7824  O  O   . THR C  1 110 ? 62.968  3.591   84.713  1.00 41.95  ? 110 THR C O   1 
ATOM   7825  C  CB  . THR C  1 110 ? 65.567  2.385   83.910  1.00 39.48  ? 110 THR C CB  1 
ATOM   7826  O  OG1 . THR C  1 110 ? 66.356  1.289   83.441  1.00 45.90  ? 110 THR C OG1 1 
ATOM   7827  C  CG2 . THR C  1 110 ? 66.453  3.493   84.322  1.00 38.34  ? 110 THR C CG2 1 
ATOM   7828  N  N   . THR C  1 111 ? 63.740  3.324   86.808  1.00 30.35  ? 111 THR C N   1 
ATOM   7829  C  CA  . THR C  1 111 ? 62.888  4.358   87.389  1.00 26.67  ? 111 THR C CA  1 
ATOM   7830  C  C   . THR C  1 111 ? 63.517  5.778   87.396  1.00 28.24  ? 111 THR C C   1 
ATOM   7831  O  O   . THR C  1 111 ? 64.721  5.931   87.637  1.00 31.69  ? 111 THR C O   1 
ATOM   7832  C  CB  . THR C  1 111 ? 62.524  3.952   88.817  1.00 21.33  ? 111 THR C CB  1 
ATOM   7833  O  OG1 . THR C  1 111 ? 61.623  2.846   88.782  1.00 26.95  ? 111 THR C OG1 1 
ATOM   7834  C  CG2 . THR C  1 111 ? 61.873  5.060   89.545  1.00 25.66  ? 111 THR C CG2 1 
ATOM   7835  N  N   . ARG C  1 112 ? 62.729  6.804   87.064  1.00 27.81  ? 112 ARG C N   1 
ATOM   7836  C  CA  . ARG C  1 112 ? 63.197  8.191   87.112  1.00 21.51  ? 112 ARG C CA  1 
ATOM   7837  C  C   . ARG C  1 112 ? 62.184  9.008   87.906  1.00 23.96  ? 112 ARG C C   1 
ATOM   7838  O  O   . ARG C  1 112 ? 60.959  8.793   87.849  1.00 19.26  ? 112 ARG C O   1 
ATOM   7839  C  CB  . ARG C  1 112 ? 63.407  8.755   85.751  1.00 17.79  ? 112 ARG C CB  1 
ATOM   7840  C  CG  . ARG C  1 112 ? 64.443  8.018   85.042  1.00 17.99  ? 112 ARG C CG  1 
ATOM   7841  C  CD  . ARG C  1 112 ? 64.579  8.529   83.637  1.00 21.76  ? 112 ARG C CD  1 
ATOM   7842  N  NE  . ARG C  1 112 ? 65.155  9.861   83.616  1.00 25.06  ? 112 ARG C NE  1 
ATOM   7843  C  CZ  . ARG C  1 112 ? 64.844  10.787  82.719  1.00 30.84  ? 112 ARG C CZ  1 
ATOM   7844  N  NH1 . ARG C  1 112 ? 63.953  10.558  81.765  1.00 27.92  ? 112 ARG C NH1 1 
ATOM   7845  N  NH2 . ARG C  1 112 ? 65.472  11.936  82.753  1.00 28.12  ? 112 ARG C NH2 1 
ATOM   7846  N  N   . ARG C  1 113 ? 62.731  9.869   88.748  1.00 28.80  ? 113 ARG C N   1 
ATOM   7847  C  CA  . ARG C  1 113 ? 61.942  10.697  89.659  1.00 32.82  ? 113 ARG C CA  1 
ATOM   7848  C  C   . ARG C  1 113 ? 61.912  12.178  89.326  1.00 31.90  ? 113 ARG C C   1 
ATOM   7849  O  O   . ARG C  1 113 ? 62.886  12.761  88.880  1.00 35.34  ? 113 ARG C O   1 
ATOM   7850  C  CB  . ARG C  1 113 ? 62.502  10.518  91.059  1.00 35.62  ? 113 ARG C CB  1 
ATOM   7851  C  CG  . ARG C  1 113 ? 61.932  11.402  92.124  1.00 44.60  ? 113 ARG C CG  1 
ATOM   7852  C  CD  . ARG C  1 113 ? 62.528  11.047  93.488  1.00 50.57  ? 113 ARG C CD  1 
ATOM   7853  N  NE  . ARG C  1 113 ? 62.160  9.682   93.898  1.00 61.76  ? 113 ARG C NE  1 
ATOM   7854  C  CZ  . ARG C  1 113 ? 62.509  9.104   95.049  1.00 66.80  ? 113 ARG C CZ  1 
ATOM   7855  N  NH1 . ARG C  1 113 ? 63.252  9.767   95.946  1.00 71.92  ? 113 ARG C NH1 1 
ATOM   7856  N  NH2 . ARG C  1 113 ? 62.123  7.851   95.297  1.00 69.45  ? 113 ARG C NH2 1 
ATOM   7857  N  N   . PHE C  1 114 ? 60.771  12.790  89.536  1.00 29.84  ? 114 PHE C N   1 
ATOM   7858  C  CA  . PHE C  1 114 ? 60.651  14.192  89.272  1.00 31.41  ? 114 PHE C CA  1 
ATOM   7859  C  C   . PHE C  1 114 ? 59.735  14.773  90.337  1.00 36.04  ? 114 PHE C C   1 
ATOM   7860  O  O   . PHE C  1 114 ? 59.202  14.043  91.195  1.00 36.83  ? 114 PHE C O   1 
ATOM   7861  C  CB  . PHE C  1 114 ? 60.017  14.396  87.896  1.00 30.80  ? 114 PHE C CB  1 
ATOM   7862  C  CG  . PHE C  1 114 ? 60.738  13.711  86.776  1.00 31.34  ? 114 PHE C CG  1 
ATOM   7863  C  CD1 . PHE C  1 114 ? 61.785  14.339  86.119  1.00 26.67  ? 114 PHE C CD1 1 
ATOM   7864  C  CD2 . PHE C  1 114 ? 60.367  12.432  86.364  1.00 33.58  ? 114 PHE C CD2 1 
ATOM   7865  C  CE1 . PHE C  1 114 ? 62.460  13.703  85.067  1.00 25.70  ? 114 PHE C CE1 1 
ATOM   7866  C  CE2 . PHE C  1 114 ? 61.046  11.794  85.301  1.00 32.50  ? 114 PHE C CE2 1 
ATOM   7867  C  CZ  . PHE C  1 114 ? 62.098  12.434  84.653  1.00 21.72  ? 114 PHE C CZ  1 
ATOM   7868  N  N   . SER C  1 115 ? 59.521  16.081  90.255  1.00 36.42  ? 115 SER C N   1 
ATOM   7869  C  CA  . SER C  1 115 ? 58.649  16.769  91.189  1.00 35.97  ? 115 SER C CA  1 
ATOM   7870  C  C   . SER C  1 115 ? 57.979  17.923  90.518  1.00 32.74  ? 115 SER C C   1 
ATOM   7871  O  O   . SER C  1 115 ? 58.538  18.519  89.622  1.00 36.92  ? 115 SER C O   1 
ATOM   7872  C  CB  . SER C  1 115 ? 59.463  17.318  92.349  1.00 37.28  ? 115 SER C CB  1 
ATOM   7873  O  OG  . SER C  1 115 ? 60.537  18.099  91.863  1.00 41.04  ? 115 SER C OG  1 
ATOM   7874  N  N   . PHE C  1 116 ? 56.798  18.261  90.977  1.00 31.50  ? 116 PHE C N   1 
ATOM   7875  C  CA  . PHE C  1 116 ? 56.082  19.407  90.441  1.00 35.88  ? 116 PHE C CA  1 
ATOM   7876  C  C   . PHE C  1 116 ? 55.323  20.010  91.628  1.00 37.93  ? 116 PHE C C   1 
ATOM   7877  O  O   . PHE C  1 116 ? 55.180  19.369  92.672  1.00 43.54  ? 116 PHE C O   1 
ATOM   7878  C  CB  . PHE C  1 116 ? 55.129  19.006  89.309  1.00 27.86  ? 116 PHE C CB  1 
ATOM   7879  C  CG  . PHE C  1 116 ? 54.064  18.027  89.718  1.00 25.21  ? 116 PHE C CG  1 
ATOM   7880  C  CD1 . PHE C  1 116 ? 52.981  18.434  90.477  1.00 24.04  ? 116 PHE C CD1 1 
ATOM   7881  C  CD2 . PHE C  1 116 ? 54.137  16.696  89.325  1.00 18.74  ? 116 PHE C CD2 1 
ATOM   7882  C  CE1 . PHE C  1 116 ? 51.998  17.528  90.836  1.00 23.15  ? 116 PHE C CE1 1 
ATOM   7883  C  CE2 . PHE C  1 116 ? 53.169  15.801  89.674  1.00 13.99  ? 116 PHE C CE2 1 
ATOM   7884  C  CZ  . PHE C  1 116 ? 52.097  16.211  90.434  1.00 18.46  ? 116 PHE C CZ  1 
ATOM   7885  N  N   . ILE C  1 117 ? 54.849  21.231  91.491  1.00 35.98  ? 117 ILE C N   1 
ATOM   7886  C  CA  . ILE C  1 117 ? 54.128  21.826  92.595  1.00 38.55  ? 117 ILE C CA  1 
ATOM   7887  C  C   . ILE C  1 117 ? 52.755  22.231  92.182  1.00 39.48  ? 117 ILE C C   1 
ATOM   7888  O  O   . ILE C  1 117 ? 52.615  22.977  91.210  1.00 48.00  ? 117 ILE C O   1 
ATOM   7889  C  CB  . ILE C  1 117 ? 54.832  23.040  93.083  1.00 38.73  ? 117 ILE C CB  1 
ATOM   7890  C  CG1 . ILE C  1 117 ? 56.253  22.647  93.445  1.00 46.22  ? 117 ILE C CG1 1 
ATOM   7891  C  CG2 . ILE C  1 117 ? 54.100  23.619  94.275  1.00 38.28  ? 117 ILE C CG2 1 
ATOM   7892  C  CD1 . ILE C  1 117 ? 57.051  23.762  93.992  1.00 46.63  ? 117 ILE C CD1 1 
ATOM   7893  N  N   . THR C  1 118 ? 51.733  21.758  92.883  1.00 34.86  ? 118 THR C N   1 
ATOM   7894  C  CA  . THR C  1 118 ? 50.394  22.130  92.478  1.00 30.95  ? 118 THR C CA  1 
ATOM   7895  C  C   . THR C  1 118 ? 50.259  23.632  92.705  1.00 36.37  ? 118 THR C C   1 
ATOM   7896  O  O   . THR C  1 118 ? 50.988  24.205  93.514  1.00 38.10  ? 118 THR C O   1 
ATOM   7897  C  CB  . THR C  1 118 ? 49.375  21.347  93.232  1.00 23.22  ? 118 THR C CB  1 
ATOM   7898  O  OG1 . THR C  1 118 ? 49.806  21.254  94.579  1.00 29.83  ? 118 THR C OG1 1 
ATOM   7899  C  CG2 . THR C  1 118 ? 49.301  19.967  92.698  1.00 22.81  ? 118 THR C CG2 1 
ATOM   7900  N  N   . PRO C  1 119 ? 49.382  24.312  91.929  1.00 40.09  ? 119 PRO C N   1 
ATOM   7901  C  CA  . PRO C  1 119 ? 49.205  25.752  92.095  1.00 36.98  ? 119 PRO C CA  1 
ATOM   7902  C  C   . PRO C  1 119 ? 48.209  26.028  93.217  1.00 37.85  ? 119 PRO C C   1 
ATOM   7903  O  O   . PRO C  1 119 ? 47.508  25.123  93.731  1.00 35.93  ? 119 PRO C O   1 
ATOM   7904  C  CB  . PRO C  1 119 ? 48.597  26.160  90.750  1.00 34.30  ? 119 PRO C CB  1 
ATOM   7905  C  CG  . PRO C  1 119 ? 47.619  25.075  90.514  1.00 31.94  ? 119 PRO C CG  1 
ATOM   7906  C  CD  . PRO C  1 119 ? 48.471  23.820  90.867  1.00 42.34  ? 119 PRO C CD  1 
ATOM   7907  N  N   . PRO C  1 120 ? 48.102  27.306  93.584  1.00 37.94  ? 120 PRO C N   1 
ATOM   7908  C  CA  . PRO C  1 120 ? 47.195  27.751  94.635  1.00 34.99  ? 120 PRO C CA  1 
ATOM   7909  C  C   . PRO C  1 120 ? 45.792  27.558  94.136  1.00 35.22  ? 120 PRO C C   1 
ATOM   7910  O  O   . PRO C  1 120 ? 45.545  27.376  92.936  1.00 29.99  ? 120 PRO C O   1 
ATOM   7911  C  CB  . PRO C  1 120 ? 47.482  29.225  94.718  1.00 35.25  ? 120 PRO C CB  1 
ATOM   7912  C  CG  . PRO C  1 120 ? 48.856  29.351  94.124  1.00 33.94  ? 120 PRO C CG  1 
ATOM   7913  C  CD  . PRO C  1 120 ? 48.825  28.447  92.999  1.00 32.69  ? 120 PRO C CD  1 
ATOM   7914  N  N   . GLN C  1 121 ? 44.867  27.596  95.067  1.00 37.77  ? 121 GLN C N   1 
ATOM   7915  C  CA  . GLN C  1 121 ? 43.483  27.437  94.703  1.00 39.23  ? 121 GLN C CA  1 
ATOM   7916  C  C   . GLN C  1 121 ? 43.173  28.676  93.913  1.00 37.78  ? 121 GLN C C   1 
ATOM   7917  O  O   . GLN C  1 121 ? 43.717  29.734  94.216  1.00 36.44  ? 121 GLN C O   1 
ATOM   7918  C  CB  . GLN C  1 121 ? 42.647  27.419  95.955  1.00 45.25  ? 121 GLN C CB  1 
ATOM   7919  C  CG  . GLN C  1 121 ? 41.188  27.311  95.682  1.00 52.17  ? 121 GLN C CG  1 
ATOM   7920  C  CD  . GLN C  1 121 ? 40.430  26.863  96.913  1.00 67.70  ? 121 GLN C CD  1 
ATOM   7921  O  OE1 . GLN C  1 121 ? 40.999  26.731  98.017  1.00 74.43  ? 121 GLN C OE1 1 
ATOM   7922  N  NE2 . GLN C  1 121 ? 39.147  26.561  96.730  1.00 77.77  ? 121 GLN C NE2 1 
ATOM   7923  N  N   . THR C  1 122 ? 42.317  28.565  92.906  1.00 39.57  ? 122 THR C N   1 
ATOM   7924  C  CA  . THR C  1 122 ? 42.005  29.732  92.092  1.00 45.01  ? 122 THR C CA  1 
ATOM   7925  C  C   . THR C  1 122 ? 41.457  30.843  92.949  1.00 47.70  ? 122 THR C C   1 
ATOM   7926  O  O   . THR C  1 122 ? 40.675  30.604  93.853  1.00 52.76  ? 122 THR C O   1 
ATOM   7927  C  CB  . THR C  1 122 ? 41.013  29.436  90.934  1.00 49.14  ? 122 THR C CB  1 
ATOM   7928  O  OG1 . THR C  1 122 ? 39.733  29.052  91.448  1.00 55.11  ? 122 THR C OG1 1 
ATOM   7929  C  CG2 . THR C  1 122 ? 41.528  28.330  90.064  1.00 51.83  ? 122 THR C CG2 1 
ATOM   7930  N  N   . GLY C  1 123 ? 41.849  32.069  92.659  1.00 50.91  ? 123 GLY C N   1 
ATOM   7931  C  CA  . GLY C  1 123 ? 41.361  33.161  93.457  1.00 49.74  ? 123 GLY C CA  1 
ATOM   7932  C  C   . GLY C  1 123 ? 41.597  34.489  92.803  1.00 51.96  ? 123 GLY C C   1 
ATOM   7933  O  O   . GLY C  1 123 ? 42.424  34.614  91.907  1.00 51.93  ? 123 GLY C O   1 
ATOM   7934  N  N   . LEU C  1 124 ? 40.934  35.498  93.354  1.00 55.07  ? 124 LEU C N   1 
ATOM   7935  C  CA  . LEU C  1 124 ? 40.976  36.879  92.884  1.00 54.21  ? 124 LEU C CA  1 
ATOM   7936  C  C   . LEU C  1 124 ? 42.327  37.552  92.932  1.00 53.49  ? 124 LEU C C   1 
ATOM   7937  O  O   . LEU C  1 124 ? 42.739  38.180  91.946  1.00 56.99  ? 124 LEU C O   1 
ATOM   7938  C  CB  . LEU C  1 124 ? 39.977  37.697  93.691  1.00 56.93  ? 124 LEU C CB  1 
ATOM   7939  C  CG  . LEU C  1 124 ? 39.309  38.900  93.051  1.00 58.19  ? 124 LEU C CG  1 
ATOM   7940  C  CD1 . LEU C  1 124 ? 39.032  38.701  91.555  1.00 62.37  ? 124 LEU C CD1 1 
ATOM   7941  C  CD2 . LEU C  1 124 ? 38.019  39.120  93.806  1.00 58.43  ? 124 LEU C CD2 1 
ATOM   7942  N  N   . ASP C  1 125 ? 43.029  37.410  94.054  1.00 52.18  ? 125 ASP C N   1 
ATOM   7943  C  CA  . ASP C  1 125 ? 44.333  38.050  94.201  1.00 51.20  ? 125 ASP C CA  1 
ATOM   7944  C  C   . ASP C  1 125 ? 45.527  37.106  94.242  1.00 48.76  ? 125 ASP C C   1 
ATOM   7945  O  O   . ASP C  1 125 ? 46.607  37.481  94.717  1.00 46.82  ? 125 ASP C O   1 
ATOM   7946  C  CB  . ASP C  1 125 ? 44.327  38.949  95.435  1.00 59.52  ? 125 ASP C CB  1 
ATOM   7947  C  CG  . ASP C  1 125 ? 43.374  40.148  95.297  1.00 62.31  ? 125 ASP C CG  1 
ATOM   7948  O  OD1 . ASP C  1 125 ? 43.573  41.000  94.385  1.00 68.49  ? 125 ASP C OD1 1 
ATOM   7949  O  OD2 . ASP C  1 125 ? 42.441  40.245  96.127  1.00 62.71  ? 125 ASP C OD2 1 
ATOM   7950  N  N   . VAL C  1 126 ? 45.326  35.887  93.745  1.00 46.01  ? 126 VAL C N   1 
ATOM   7951  C  CA  . VAL C  1 126 ? 46.380  34.879  93.720  1.00 42.74  ? 126 VAL C CA  1 
ATOM   7952  C  C   . VAL C  1 126 ? 47.363  35.225  92.613  1.00 36.60  ? 126 VAL C C   1 
ATOM   7953  O  O   . VAL C  1 126 ? 47.010  35.299  91.426  1.00 32.33  ? 126 VAL C O   1 
ATOM   7954  C  CB  . VAL C  1 126 ? 45.814  33.487  93.439  1.00 48.82  ? 126 VAL C CB  1 
ATOM   7955  C  CG1 . VAL C  1 126 ? 46.918  32.469  93.487  1.00 54.89  ? 126 VAL C CG1 1 
ATOM   7956  C  CG2 . VAL C  1 126 ? 44.725  33.134  94.436  1.00 53.59  ? 126 VAL C CG2 1 
ATOM   7957  N  N   . PRO C  1 127 ? 48.603  35.488  92.996  1.00 30.83  ? 127 PRO C N   1 
ATOM   7958  C  CA  . PRO C  1 127 ? 49.646  35.841  92.028  1.00 31.48  ? 127 PRO C CA  1 
ATOM   7959  C  C   . PRO C  1 127 ? 50.188  34.581  91.436  1.00 34.01  ? 127 PRO C C   1 
ATOM   7960  O  O   . PRO C  1 127 ? 50.106  33.523  92.052  1.00 36.72  ? 127 PRO C O   1 
ATOM   7961  C  CB  . PRO C  1 127 ? 50.696  36.518  92.889  1.00 34.85  ? 127 PRO C CB  1 
ATOM   7962  C  CG  . PRO C  1 127 ? 50.580  35.756  94.199  1.00 31.70  ? 127 PRO C CG  1 
ATOM   7963  C  CD  . PRO C  1 127 ? 49.097  35.510  94.380  1.00 26.46  ? 127 PRO C CD  1 
ATOM   7964  N  N   . TYR C  1 128 ? 50.806  34.691  90.278  1.00 36.03  ? 128 TYR C N   1 
ATOM   7965  C  CA  . TYR C  1 128 ? 51.329  33.514  89.616  1.00 35.96  ? 128 TYR C CA  1 
ATOM   7966  C  C   . TYR C  1 128 ? 52.139  34.070  88.494  1.00 34.57  ? 128 TYR C C   1 
ATOM   7967  O  O   . TYR C  1 128 ? 51.852  35.157  88.021  1.00 39.54  ? 128 TYR C O   1 
ATOM   7968  C  CB  . TYR C  1 128 ? 50.182  32.644  89.059  1.00 36.27  ? 128 TYR C CB  1 
ATOM   7969  C  CG  . TYR C  1 128 ? 50.545  31.170  88.881  1.00 41.99  ? 128 TYR C CG  1 
ATOM   7970  C  CD1 . TYR C  1 128 ? 50.645  30.323  89.985  1.00 43.27  ? 128 TYR C CD1 1 
ATOM   7971  C  CD2 . TYR C  1 128 ? 50.847  30.651  87.635  1.00 42.22  ? 128 TYR C CD2 1 
ATOM   7972  C  CE1 . TYR C  1 128 ? 51.042  29.026  89.864  1.00 43.92  ? 128 TYR C CE1 1 
ATOM   7973  C  CE2 . TYR C  1 128 ? 51.240  29.340  87.508  1.00 47.24  ? 128 TYR C CE2 1 
ATOM   7974  C  CZ  . TYR C  1 128 ? 51.345  28.543  88.636  1.00 44.69  ? 128 TYR C CZ  1 
ATOM   7975  O  OH  . TYR C  1 128 ? 51.806  27.268  88.583  1.00 50.37  ? 128 TYR C OH  1 
ATOM   7976  N  N   . THR C  1 129 ? 53.154  33.355  88.062  1.00 31.20  ? 129 THR C N   1 
ATOM   7977  C  CA  . THR C  1 129 ? 53.934  33.883  86.965  1.00 31.68  ? 129 THR C CA  1 
ATOM   7978  C  C   . THR C  1 129 ? 54.081  32.873  85.808  1.00 32.09  ? 129 THR C C   1 
ATOM   7979  O  O   . THR C  1 129 ? 54.518  31.735  86.003  1.00 32.16  ? 129 THR C O   1 
ATOM   7980  C  CB  . THR C  1 129 ? 55.257  34.490  87.443  1.00 30.91  ? 129 THR C CB  1 
ATOM   7981  O  OG1 . THR C  1 129 ? 56.291  34.129  86.533  1.00 41.01  ? 129 THR C OG1 1 
ATOM   7982  C  CG2 . THR C  1 129 ? 55.615  34.039  88.840  1.00 34.78  ? 129 THR C CG2 1 
ATOM   7983  N  N   . PHE C  1 130 ? 53.616  33.276  84.626  1.00 31.15  ? 130 PHE C N   1 
ATOM   7984  C  CA  . PHE C  1 130 ? 53.628  32.425  83.450  1.00 30.35  ? 130 PHE C CA  1 
ATOM   7985  C  C   . PHE C  1 130 ? 54.773  32.766  82.554  1.00 29.23  ? 130 PHE C C   1 
ATOM   7986  O  O   . PHE C  1 130 ? 55.175  33.909  82.457  1.00 31.88  ? 130 PHE C O   1 
ATOM   7987  C  CB  . PHE C  1 130 ? 52.323  32.580  82.663  1.00 30.83  ? 130 PHE C CB  1 
ATOM   7988  C  CG  . PHE C  1 130 ? 51.104  32.152  83.428  1.00 31.72  ? 130 PHE C CG  1 
ATOM   7989  C  CD1 . PHE C  1 130 ? 50.708  30.840  83.432  1.00 36.35  ? 130 PHE C CD1 1 
ATOM   7990  C  CD2 . PHE C  1 130 ? 50.354  33.062  84.165  1.00 35.00  ? 130 PHE C CD2 1 
ATOM   7991  C  CE1 . PHE C  1 130 ? 49.566  30.431  84.171  1.00 39.83  ? 130 PHE C CE1 1 
ATOM   7992  C  CE2 . PHE C  1 130 ? 49.211  32.658  84.907  1.00 33.42  ? 130 PHE C CE2 1 
ATOM   7993  C  CZ  . PHE C  1 130 ? 48.824  31.345  84.906  1.00 33.64  ? 130 PHE C CZ  1 
ATOM   7994  N  N   . GLY C  1 131 ? 55.364  31.759  81.950  1.00 28.57  ? 131 GLY C N   1 
ATOM   7995  C  CA  . GLY C  1 131 ? 56.444  32.046  81.042  1.00 23.77  ? 131 GLY C CA  1 
ATOM   7996  C  C   . GLY C  1 131 ? 55.772  32.024  79.697  1.00 25.92  ? 131 GLY C C   1 
ATOM   7997  O  O   . GLY C  1 131 ? 54.747  31.334  79.572  1.00 30.69  ? 131 GLY C O   1 
ATOM   7998  N  N   . LEU C  1 132 ? 56.271  32.812  78.735  1.00 24.62  ? 132 LEU C N   1 
ATOM   7999  C  CA  . LEU C  1 132 ? 55.719  32.845  77.359  1.00 22.86  ? 132 LEU C CA  1 
ATOM   8000  C  C   . LEU C  1 132 ? 56.751  32.447  76.338  1.00 21.58  ? 132 LEU C C   1 
ATOM   8001  O  O   . LEU C  1 132 ? 57.789  33.074  76.199  1.00 26.02  ? 132 LEU C O   1 
ATOM   8002  C  CB  . LEU C  1 132 ? 55.157  34.209  77.018  1.00 22.27  ? 132 LEU C CB  1 
ATOM   8003  C  CG  . LEU C  1 132 ? 53.725  34.039  77.468  1.00 23.09  ? 132 LEU C CG  1 
ATOM   8004  C  CD1 . LEU C  1 132 ? 53.481  34.760  78.755  1.00 24.86  ? 132 LEU C CD1 1 
ATOM   8005  C  CD2 . LEU C  1 132 ? 52.814  34.503  76.417  1.00 28.14  ? 132 LEU C CD2 1 
ATOM   8006  N  N   . ILE C  1 133 ? 56.487  31.342  75.682  1.00 17.48  ? 133 ILE C N   1 
ATOM   8007  C  CA  . ILE C  1 133 ? 57.422  30.830  74.723  1.00 15.79  ? 133 ILE C CA  1 
ATOM   8008  C  C   . ILE C  1 133 ? 56.557  30.404  73.572  1.00 18.19  ? 133 ILE C C   1 
ATOM   8009  O  O   . ILE C  1 133 ? 55.484  29.801  73.759  1.00 21.59  ? 133 ILE C O   1 
ATOM   8010  C  CB  . ILE C  1 133 ? 58.155  29.568  75.264  1.00 18.74  ? 133 ILE C CB  1 
ATOM   8011  C  CG1 . ILE C  1 133 ? 58.838  29.864  76.571  1.00 12.55  ? 133 ILE C CG1 1 
ATOM   8012  C  CG2 . ILE C  1 133 ? 59.206  29.092  74.312  1.00 21.23  ? 133 ILE C CG2 1 
ATOM   8013  C  CD1 . ILE C  1 133 ? 59.775  28.786  76.995  1.00 19.23  ? 133 ILE C CD1 1 
ATOM   8014  N  N   . GLY C  1 134 ? 57.004  30.738  72.377  1.00 16.00  ? 134 GLY C N   1 
ATOM   8015  C  CA  . GLY C  1 134 ? 56.250  30.359  71.207  1.00 15.03  ? 134 GLY C CA  1 
ATOM   8016  C  C   . GLY C  1 134 ? 57.273  30.049  70.132  1.00 16.70  ? 134 GLY C C   1 
ATOM   8017  O  O   . GLY C  1 134 ? 58.424  30.459  70.205  1.00 18.33  ? 134 GLY C O   1 
ATOM   8018  N  N   . ASP C  1 135 ? 56.931  29.163  69.225  1.00 16.85  ? 135 ASP C N   1 
ATOM   8019  C  CA  . ASP C  1 135 ? 57.837  28.860  68.174  1.00 19.41  ? 135 ASP C CA  1 
ATOM   8020  C  C   . ASP C  1 135 ? 59.264  28.327  68.492  1.00 20.35  ? 135 ASP C C   1 
ATOM   8021  O  O   . ASP C  1 135 ? 60.185  28.506  67.699  1.00 22.01  ? 135 ASP C O   1 
ATOM   8022  C  CB  . ASP C  1 135 ? 57.843  30.137  67.428  1.00 22.29  ? 135 ASP C CB  1 
ATOM   8023  C  CG  . ASP C  1 135 ? 56.749  30.182  66.387  1.00 25.68  ? 135 ASP C CG  1 
ATOM   8024  O  OD1 . ASP C  1 135 ? 57.185  29.700  65.388  1.00 22.58  ? 135 ASP C OD1 1 
ATOM   8025  O  OD2 . ASP C  1 135 ? 55.599  30.632  66.560  1.00 18.95  ? 135 ASP C OD2 1 
ATOM   8026  N  N   . LEU C  1 136 ? 59.391  27.534  69.553  1.00 20.33  ? 136 LEU C N   1 
ATOM   8027  C  CA  . LEU C  1 136 ? 60.675  27.027  70.040  1.00 22.66  ? 136 LEU C CA  1 
ATOM   8028  C  C   . LEU C  1 136 ? 61.619  26.322  69.094  1.00 25.14  ? 136 LEU C C   1 
ATOM   8029  O  O   . LEU C  1 136 ? 62.748  26.761  68.890  1.00 31.60  ? 136 LEU C O   1 
ATOM   8030  C  CB  . LEU C  1 136 ? 60.476  26.179  71.284  1.00 16.96  ? 136 LEU C CB  1 
ATOM   8031  C  CG  . LEU C  1 136 ? 61.715  25.822  72.088  1.00 18.50  ? 136 LEU C CG  1 
ATOM   8032  C  CD1 . LEU C  1 136 ? 62.402  27.075  72.540  1.00 16.18  ? 136 LEU C CD1 1 
ATOM   8033  C  CD2 . LEU C  1 136 ? 61.339  24.979  73.304  1.00 23.09  ? 136 LEU C CD2 1 
ATOM   8034  N  N   . GLY C  1 137 ? 61.189  25.199  68.551  1.00 26.40  ? 137 GLY C N   1 
ATOM   8035  C  CA  . GLY C  1 137 ? 62.050  24.465  67.635  1.00 28.17  ? 137 GLY C CA  1 
ATOM   8036  C  C   . GLY C  1 137 ? 63.260  23.878  68.315  1.00 27.62  ? 137 GLY C C   1 
ATOM   8037  O  O   . GLY C  1 137 ? 63.239  23.672  69.518  1.00 27.01  ? 137 GLY C O   1 
ATOM   8038  N  N   . GLN C  1 138 ? 64.293  23.541  67.550  1.00 28.94  ? 138 GLN C N   1 
ATOM   8039  C  CA  . GLN C  1 138 ? 65.484  22.958  68.189  1.00 27.60  ? 138 GLN C CA  1 
ATOM   8040  C  C   . GLN C  1 138 ? 66.832  23.426  67.648  1.00 27.79  ? 138 GLN C C   1 
ATOM   8041  O  O   . GLN C  1 138 ? 67.727  22.618  67.426  1.00 34.86  ? 138 GLN C O   1 
ATOM   8042  C  CB  . GLN C  1 138 ? 65.412  21.404  68.222  1.00 23.18  ? 138 GLN C CB  1 
ATOM   8043  C  CG  . GLN C  1 138 ? 65.221  20.727  66.875  1.00 19.39  ? 138 GLN C CG  1 
ATOM   8044  C  CD  . GLN C  1 138 ? 64.791  19.318  67.010  1.00 18.24  ? 138 GLN C CD  1 
ATOM   8045  O  OE1 . GLN C  1 138 ? 63.609  19.020  67.052  1.00 20.15  ? 138 GLN C OE1 1 
ATOM   8046  N  NE2 . GLN C  1 138 ? 65.750  18.430  67.102  1.00 26.69  ? 138 GLN C NE2 1 
ATOM   8047  N  N   . SER C  1 139 ? 66.954  24.720  67.385  1.00 26.95  ? 139 SER C N   1 
ATOM   8048  C  CA  . SER C  1 139 ? 68.196  25.290  66.899  1.00 24.00  ? 139 SER C CA  1 
ATOM   8049  C  C   . SER C  1 139 ? 68.930  25.683  68.170  1.00 25.34  ? 139 SER C C   1 
ATOM   8050  O  O   . SER C  1 139 ? 68.361  25.626  69.270  1.00 22.49  ? 139 SER C O   1 
ATOM   8051  C  CB  . SER C  1 139 ? 67.918  26.529  66.077  1.00 24.63  ? 139 SER C CB  1 
ATOM   8052  O  OG  . SER C  1 139 ? 67.298  27.506  66.902  1.00 28.71  ? 139 SER C OG  1 
ATOM   8053  N  N   . PHE C  1 140 ? 70.176  26.100  68.043  1.00 20.99  ? 140 PHE C N   1 
ATOM   8054  C  CA  . PHE C  1 140 ? 70.905  26.474  69.221  1.00 21.72  ? 140 PHE C CA  1 
ATOM   8055  C  C   . PHE C  1 140 ? 70.219  27.591  69.927  1.00 27.43  ? 140 PHE C C   1 
ATOM   8056  O  O   . PHE C  1 140 ? 70.231  27.688  71.174  1.00 31.47  ? 140 PHE C O   1 
ATOM   8057  C  CB  . PHE C  1 140 ? 72.245  26.949  68.812  1.00 20.46  ? 140 PHE C CB  1 
ATOM   8058  C  CG  . PHE C  1 140 ? 73.057  25.894  68.198  1.00 26.19  ? 140 PHE C CG  1 
ATOM   8059  C  CD1 . PHE C  1 140 ? 73.792  25.022  68.990  1.00 28.11  ? 140 PHE C CD1 1 
ATOM   8060  C  CD2 . PHE C  1 140 ? 73.054  25.732  66.834  1.00 21.99  ? 140 PHE C CD2 1 
ATOM   8061  C  CE1 . PHE C  1 140 ? 74.508  24.003  68.419  1.00 28.04  ? 140 PHE C CE1 1 
ATOM   8062  C  CE2 . PHE C  1 140 ? 73.768  24.717  66.252  1.00 25.19  ? 140 PHE C CE2 1 
ATOM   8063  C  CZ  . PHE C  1 140 ? 74.498  23.845  67.044  1.00 25.20  ? 140 PHE C CZ  1 
ATOM   8064  N  N   . ASP C  1 141 ? 69.622  28.442  69.108  1.00 29.59  ? 141 ASP C N   1 
ATOM   8065  C  CA  . ASP C  1 141 ? 68.909  29.598  69.590  1.00 28.38  ? 141 ASP C CA  1 
ATOM   8066  C  C   . ASP C  1 141 ? 67.825  29.141  70.547  1.00 30.13  ? 141 ASP C C   1 
ATOM   8067  O  O   . ASP C  1 141 ? 67.636  29.702  71.642  1.00 30.10  ? 141 ASP C O   1 
ATOM   8068  C  CB  . ASP C  1 141 ? 68.323  30.313  68.385  1.00 33.59  ? 141 ASP C CB  1 
ATOM   8069  C  CG  . ASP C  1 141 ? 69.363  31.093  67.621  1.00 34.00  ? 141 ASP C CG  1 
ATOM   8070  O  OD1 . ASP C  1 141 ? 70.005  31.955  68.276  1.00 37.70  ? 141 ASP C OD1 1 
ATOM   8071  O  OD2 . ASP C  1 141 ? 69.536  30.842  66.400  1.00 29.17  ? 141 ASP C OD2 1 
ATOM   8072  N  N   . SER C  1 142 ? 67.166  28.054  70.167  1.00 28.60  ? 142 SER C N   1 
ATOM   8073  C  CA  . SER C  1 142 ? 66.110  27.542  71.008  1.00 26.18  ? 142 SER C CA  1 
ATOM   8074  C  C   . SER C  1 142 ? 66.711  27.156  72.342  1.00 25.87  ? 142 SER C C   1 
ATOM   8075  O  O   . SER C  1 142 ? 66.145  27.489  73.369  1.00 30.05  ? 142 SER C O   1 
ATOM   8076  C  CB  . SER C  1 142 ? 65.437  26.346  70.360  1.00 23.20  ? 142 SER C CB  1 
ATOM   8077  O  OG  . SER C  1 142 ? 65.395  26.498  68.957  1.00 24.29  ? 142 SER C OG  1 
ATOM   8078  N  N   . ASN C  1 143 ? 67.889  26.535  72.336  1.00 24.23  ? 143 ASN C N   1 
ATOM   8079  C  CA  . ASN C  1 143 ? 68.532  26.108  73.598  1.00 25.76  ? 143 ASN C CA  1 
ATOM   8080  C  C   . ASN C  1 143 ? 68.749  27.299  74.506  1.00 26.13  ? 143 ASN C C   1 
ATOM   8081  O  O   . ASN C  1 143 ? 68.425  27.273  75.692  1.00 26.86  ? 143 ASN C O   1 
ATOM   8082  C  CB  . ASN C  1 143 ? 69.876  25.379  73.373  1.00 26.70  ? 143 ASN C CB  1 
ATOM   8083  C  CG  . ASN C  1 143 ? 70.424  24.746  74.654  1.00 29.56  ? 143 ASN C CG  1 
ATOM   8084  O  OD1 . ASN C  1 143 ? 69.690  24.246  75.502  1.00 25.64  ? 143 ASN C OD1 1 
ATOM   8085  N  ND2 . ASN C  1 143 ? 71.738  24.717  74.782  1.00 32.35  ? 143 ASN C ND2 1 
ATOM   8086  N  N   . THR C  1 144 ? 69.216  28.381  73.910  1.00 26.48  ? 144 THR C N   1 
ATOM   8087  C  CA  . THR C  1 144 ? 69.470  29.582  74.665  1.00 25.03  ? 144 THR C CA  1 
ATOM   8088  C  C   . THR C  1 144 ? 68.205  30.155  75.296  1.00 25.75  ? 144 THR C C   1 
ATOM   8089  O  O   . THR C  1 144 ? 68.195  30.410  76.500  1.00 29.46  ? 144 THR C O   1 
ATOM   8090  C  CB  . THR C  1 144 ? 70.094  30.635  73.785  1.00 25.68  ? 144 THR C CB  1 
ATOM   8091  O  OG1 . THR C  1 144 ? 71.345  30.157  73.261  1.00 25.78  ? 144 THR C OG1 1 
ATOM   8092  C  CG2 . THR C  1 144 ? 70.289  31.865  74.572  1.00 19.78  ? 144 THR C CG2 1 
ATOM   8093  N  N   . THR C  1 145 ? 67.150  30.357  74.504  1.00 20.40  ? 145 THR C N   1 
ATOM   8094  C  CA  . THR C  1 145 ? 65.899  30.885  75.031  1.00 16.99  ? 145 THR C CA  1 
ATOM   8095  C  C   . THR C  1 145 ? 65.448  30.046  76.205  1.00 19.62  ? 145 THR C C   1 
ATOM   8096  O  O   . THR C  1 145 ? 65.201  30.561  77.268  1.00 22.21  ? 145 THR C O   1 
ATOM   8097  C  CB  . THR C  1 145 ? 64.842  30.839  73.964  1.00 20.85  ? 145 THR C CB  1 
ATOM   8098  O  OG1 . THR C  1 145 ? 65.404  31.409  72.773  1.00 20.58  ? 145 THR C OG1 1 
ATOM   8099  C  CG2 . THR C  1 145 ? 63.562  31.591  74.403  1.00 10.26  ? 145 THR C CG2 1 
ATOM   8100  N  N   . LEU C  1 146 ? 65.420  28.730  76.053  1.00 22.54  ? 146 LEU C N   1 
ATOM   8101  C  CA  . LEU C  1 146 ? 65.024  27.880  77.146  1.00 21.56  ? 146 LEU C CA  1 
ATOM   8102  C  C   . LEU C  1 146 ? 65.932  28.161  78.360  1.00 29.16  ? 146 LEU C C   1 
ATOM   8103  O  O   . LEU C  1 146 ? 65.429  28.275  79.459  1.00 35.88  ? 146 LEU C O   1 
ATOM   8104  C  CB  . LEU C  1 146 ? 65.065  26.421  76.731  1.00 16.64  ? 146 LEU C CB  1 
ATOM   8105  C  CG  . LEU C  1 146 ? 64.390  25.396  77.629  1.00 20.42  ? 146 LEU C CG  1 
ATOM   8106  C  CD1 . LEU C  1 146 ? 62.950  25.809  77.826  1.00 22.24  ? 146 LEU C CD1 1 
ATOM   8107  C  CD2 . LEU C  1 146 ? 64.436  24.017  76.957  1.00 14.16  ? 146 LEU C CD2 1 
ATOM   8108  N  N   . SER C  1 147 ? 67.235  28.395  78.182  1.00 32.20  ? 147 SER C N   1 
ATOM   8109  C  CA  . SER C  1 147 ? 68.099  28.649  79.362  1.00 29.01  ? 147 SER C CA  1 
ATOM   8110  C  C   . SER C  1 147 ? 67.696  29.953  80.028  1.00 31.86  ? 147 SER C C   1 
ATOM   8111  O  O   . SER C  1 147 ? 67.453  30.006  81.240  1.00 34.87  ? 147 SER C O   1 
ATOM   8112  C  CB  . SER C  1 147 ? 69.581  28.727  79.009  1.00 24.05  ? 147 SER C CB  1 
ATOM   8113  O  OG  . SER C  1 147 ? 69.869  27.924  77.874  1.00 30.15  ? 147 SER C OG  1 
ATOM   8114  N  N   . HIS C  1 148 ? 67.576  31.006  79.231  1.00 26.86  ? 148 HIS C N   1 
ATOM   8115  C  CA  . HIS C  1 148 ? 67.188  32.271  79.790  1.00 25.73  ? 148 HIS C CA  1 
ATOM   8116  C  C   . HIS C  1 148 ? 65.938  32.123  80.594  1.00 23.81  ? 148 HIS C C   1 
ATOM   8117  O  O   . HIS C  1 148 ? 65.825  32.680  81.662  1.00 26.70  ? 148 HIS C O   1 
ATOM   8118  C  CB  . HIS C  1 148 ? 66.935  33.287  78.700  1.00 36.86  ? 148 HIS C CB  1 
ATOM   8119  C  CG  . HIS C  1 148 ? 68.174  33.970  78.218  1.00 43.67  ? 148 HIS C CG  1 
ATOM   8120  N  ND1 . HIS C  1 148 ? 68.177  35.281  77.792  1.00 45.69  ? 148 HIS C ND1 1 
ATOM   8121  C  CD2 . HIS C  1 148 ? 69.449  33.529  78.092  1.00 42.63  ? 148 HIS C CD2 1 
ATOM   8122  C  CE1 . HIS C  1 148 ? 69.397  35.619  77.428  1.00 45.73  ? 148 HIS C CE1 1 
ATOM   8123  N  NE2 . HIS C  1 148 ? 70.189  34.573  77.600  1.00 45.02  ? 148 HIS C NE2 1 
ATOM   8124  N  N   . TYR C  1 149 ? 65.003  31.336  80.097  1.00 26.39  ? 149 TYR C N   1 
ATOM   8125  C  CA  . TYR C  1 149 ? 63.777  31.175  80.817  1.00 28.16  ? 149 TYR C CA  1 
ATOM   8126  C  C   . TYR C  1 149 ? 64.072  30.562  82.132  1.00 32.61  ? 149 TYR C C   1 
ATOM   8127  O  O   . TYR C  1 149 ? 63.590  31.024  83.176  1.00 35.74  ? 149 TYR C O   1 
ATOM   8128  C  CB  . TYR C  1 149 ? 62.835  30.269  80.105  1.00 23.78  ? 149 TYR C CB  1 
ATOM   8129  C  CG  . TYR C  1 149 ? 61.591  30.017  80.904  1.00 27.58  ? 149 TYR C CG  1 
ATOM   8130  C  CD1 . TYR C  1 149 ? 60.779  31.063  81.329  1.00 30.42  ? 149 TYR C CD1 1 
ATOM   8131  C  CD2 . TYR C  1 149 ? 61.214  28.737  81.238  1.00 29.61  ? 149 TYR C CD2 1 
ATOM   8132  C  CE1 . TYR C  1 149 ? 59.610  30.825  82.074  1.00 37.74  ? 149 TYR C CE1 1 
ATOM   8133  C  CE2 . TYR C  1 149 ? 60.038  28.492  81.986  1.00 32.00  ? 149 TYR C CE2 1 
ATOM   8134  C  CZ  . TYR C  1 149 ? 59.252  29.539  82.401  1.00 34.34  ? 149 TYR C CZ  1 
ATOM   8135  O  OH  . TYR C  1 149 ? 58.134  29.330  83.179  1.00 41.98  ? 149 TYR C OH  1 
ATOM   8136  N  N   . GLU C  1 150 ? 64.873  29.509  82.074  1.00 36.95  ? 150 GLU C N   1 
ATOM   8137  C  CA  . GLU C  1 150 ? 65.251  28.761  83.268  1.00 41.28  ? 150 GLU C CA  1 
ATOM   8138  C  C   . GLU C  1 150 ? 65.931  29.680  84.270  1.00 42.71  ? 150 GLU C C   1 
ATOM   8139  O  O   . GLU C  1 150 ? 65.797  29.497  85.477  1.00 48.14  ? 150 GLU C O   1 
ATOM   8140  C  CB  . GLU C  1 150 ? 66.228  27.611  82.942  1.00 41.21  ? 150 GLU C CB  1 
ATOM   8141  C  CG  . GLU C  1 150 ? 65.717  26.400  82.186  1.00 42.84  ? 150 GLU C CG  1 
ATOM   8142  C  CD  . GLU C  1 150 ? 66.851  25.447  81.887  1.00 47.94  ? 150 GLU C CD  1 
ATOM   8143  O  OE1 . GLU C  1 150 ? 67.781  25.804  81.122  1.00 53.27  ? 150 GLU C OE1 1 
ATOM   8144  O  OE2 . GLU C  1 150 ? 66.835  24.336  82.450  1.00 53.74  ? 150 GLU C OE2 1 
ATOM   8145  N  N   . LEU C  1 151 ? 66.664  30.664  83.775  1.00 43.02  ? 151 LEU C N   1 
ATOM   8146  C  CA  . LEU C  1 151 ? 67.366  31.547  84.670  1.00 42.56  ? 151 LEU C CA  1 
ATOM   8147  C  C   . LEU C  1 151 ? 66.635  32.809  85.044  1.00 46.41  ? 151 LEU C C   1 
ATOM   8148  O  O   . LEU C  1 151 ? 67.122  33.542  85.888  1.00 49.84  ? 151 LEU C O   1 
ATOM   8149  C  CB  . LEU C  1 151 ? 68.716  31.873  84.106  1.00 41.43  ? 151 LEU C CB  1 
ATOM   8150  C  CG  . LEU C  1 151 ? 69.441  30.573  83.806  1.00 46.93  ? 151 LEU C CG  1 
ATOM   8151  C  CD1 . LEU C  1 151 ? 70.678  30.844  83.006  1.00 50.04  ? 151 LEU C CD1 1 
ATOM   8152  C  CD2 . LEU C  1 151 ? 69.753  29.841  85.095  1.00 42.73  ? 151 LEU C CD2 1 
ATOM   8153  N  N   . SER C  1 152 ? 65.469  33.078  84.457  1.00 48.75  ? 152 SER C N   1 
ATOM   8154  C  CA  . SER C  1 152 ? 64.750  34.284  84.828  1.00 50.21  ? 152 SER C CA  1 
ATOM   8155  C  C   . SER C  1 152 ? 64.677  34.319  86.332  1.00 51.43  ? 152 SER C C   1 
ATOM   8156  O  O   . SER C  1 152 ? 64.350  33.315  86.961  1.00 57.77  ? 152 SER C O   1 
ATOM   8157  C  CB  . SER C  1 152 ? 63.339  34.323  84.233  1.00 55.34  ? 152 SER C CB  1 
ATOM   8158  O  OG  . SER C  1 152 ? 63.274  35.248  83.136  1.00 70.28  ? 152 SER C OG  1 
ATOM   8159  N  N   . PRO C  1 153 ? 65.189  35.403  86.931  1.00 51.48  ? 153 PRO C N   1 
ATOM   8160  C  CA  . PRO C  1 153 ? 65.227  35.671  88.380  1.00 54.37  ? 153 PRO C CA  1 
ATOM   8161  C  C   . PRO C  1 153 ? 63.808  35.632  88.998  1.00 58.16  ? 153 PRO C C   1 
ATOM   8162  O  O   . PRO C  1 153 ? 63.599  35.321  90.185  1.00 62.45  ? 153 PRO C O   1 
ATOM   8163  C  CB  . PRO C  1 153 ? 65.885  37.047  88.448  1.00 50.52  ? 153 PRO C CB  1 
ATOM   8164  C  CG  . PRO C  1 153 ? 65.757  37.593  87.026  1.00 51.04  ? 153 PRO C CG  1 
ATOM   8165  C  CD  . PRO C  1 153 ? 65.958  36.413  86.191  1.00 48.55  ? 153 PRO C CD  1 
ATOM   8166  N  N   . LYS C  1 154 ? 62.845  36.017  88.176  1.00 58.45  ? 154 LYS C N   1 
ATOM   8167  C  CA  . LYS C  1 154 ? 61.431  35.954  88.524  1.00 61.68  ? 154 LYS C CA  1 
ATOM   8168  C  C   . LYS C  1 154 ? 61.216  34.583  87.870  1.00 57.97  ? 154 LYS C C   1 
ATOM   8169  O  O   . LYS C  1 154 ? 61.290  34.468  86.639  1.00 60.34  ? 154 LYS C O   1 
ATOM   8170  C  CB  . LYS C  1 154 ? 60.667  37.080  87.780  1.00 67.87  ? 154 LYS C CB  1 
ATOM   8171  C  CG  . LYS C  1 154 ? 61.240  37.414  86.366  1.00 74.16  ? 154 LYS C CG  1 
ATOM   8172  C  CD  . LYS C  1 154 ? 60.989  38.860  85.883  1.00 77.49  ? 154 LYS C CD  1 
ATOM   8173  C  CE  . LYS C  1 154 ? 62.180  39.396  85.008  1.00 79.88  ? 154 LYS C CE  1 
ATOM   8174  N  NZ  . LYS C  1 154 ? 62.362  38.846  83.599  1.00 86.58  ? 154 LYS C NZ  1 
ATOM   8175  N  N   . LYS C  1 155 ? 61.138  33.522  88.661  1.00 51.20  ? 155 LYS C N   1 
ATOM   8176  C  CA  . LYS C  1 155 ? 61.001  32.212  88.052  1.00 48.53  ? 155 LYS C CA  1 
ATOM   8177  C  C   . LYS C  1 155 ? 59.622  31.929  87.539  1.00 41.33  ? 155 LYS C C   1 
ATOM   8178  O  O   . LYS C  1 155 ? 58.659  32.194  88.222  1.00 39.97  ? 155 LYS C O   1 
ATOM   8179  C  CB  . LYS C  1 155 ? 61.481  31.107  88.988  1.00 59.61  ? 155 LYS C CB  1 
ATOM   8180  C  CG  . LYS C  1 155 ? 61.418  31.448  90.460  1.00 75.87  ? 155 LYS C CG  1 
ATOM   8181  C  CD  . LYS C  1 155 ? 59.999  31.868  90.897  1.00 87.29  ? 155 LYS C CD  1 
ATOM   8182  C  CE  . LYS C  1 155 ? 59.923  32.217  92.404  1.00 93.61  ? 155 LYS C CE  1 
ATOM   8183  N  NZ  . LYS C  1 155 ? 60.877  33.306  92.851  1.00 94.75  ? 155 LYS C NZ  1 
ATOM   8184  N  N   . GLY C  1 156 ? 59.541  31.452  86.300  1.00 37.32  ? 156 GLY C N   1 
ATOM   8185  C  CA  . GLY C  1 156 ? 58.257  31.130  85.706  1.00 32.12  ? 156 GLY C CA  1 
ATOM   8186  C  C   . GLY C  1 156 ? 57.687  29.911  86.385  1.00 29.67  ? 156 GLY C C   1 
ATOM   8187  O  O   . GLY C  1 156 ? 58.449  29.105  86.869  1.00 34.71  ? 156 GLY C O   1 
ATOM   8188  N  N   . GLN C  1 157 ? 56.368  29.769  86.425  1.00 28.63  ? 157 GLN C N   1 
ATOM   8189  C  CA  . GLN C  1 157 ? 55.724  28.630  87.074  1.00 25.50  ? 157 GLN C CA  1 
ATOM   8190  C  C   . GLN C  1 157 ? 54.900  27.707  86.164  1.00 23.86  ? 157 GLN C C   1 
ATOM   8191  O  O   . GLN C  1 157 ? 54.417  26.650  86.590  1.00 24.06  ? 157 GLN C O   1 
ATOM   8192  C  CB  . GLN C  1 157 ? 54.850  29.124  88.212  1.00 30.24  ? 157 GLN C CB  1 
ATOM   8193  C  CG  . GLN C  1 157 ? 55.614  29.824  89.321  1.00 44.62  ? 157 GLN C CG  1 
ATOM   8194  C  CD  . GLN C  1 157 ? 54.688  30.392  90.384  1.00 48.77  ? 157 GLN C CD  1 
ATOM   8195  O  OE1 . GLN C  1 157 ? 54.494  29.811  91.456  1.00 55.57  ? 157 GLN C OE1 1 
ATOM   8196  N  NE2 . GLN C  1 157 ? 54.121  31.542  90.092  1.00 52.76  ? 157 GLN C NE2 1 
ATOM   8197  N  N   . THR C  1 158 ? 54.707  28.144  84.928  1.00 22.73  ? 158 THR C N   1 
ATOM   8198  C  CA  . THR C  1 158 ? 53.972  27.404  83.917  1.00 23.26  ? 158 THR C CA  1 
ATOM   8199  C  C   . THR C  1 158 ? 54.285  28.122  82.632  1.00 23.88  ? 158 THR C C   1 
ATOM   8200  O  O   . THR C  1 158 ? 54.384  29.329  82.606  1.00 25.57  ? 158 THR C O   1 
ATOM   8201  C  CB  . THR C  1 158 ? 52.488  27.512  84.138  1.00 22.13  ? 158 THR C CB  1 
ATOM   8202  O  OG1 . THR C  1 158 ? 52.139  26.754  85.292  1.00 25.66  ? 158 THR C OG1 1 
ATOM   8203  C  CG2 . THR C  1 158 ? 51.702  27.004  82.943  1.00 16.69  ? 158 THR C CG2 1 
ATOM   8204  N  N   . VAL C  1 159 ? 54.540  27.380  81.582  1.00 20.43  ? 159 VAL C N   1 
ATOM   8205  C  CA  . VAL C  1 159 ? 54.795  28.020  80.337  1.00 21.71  ? 159 VAL C CA  1 
ATOM   8206  C  C   . VAL C  1 159 ? 53.529  27.967  79.494  1.00 23.00  ? 159 VAL C C   1 
ATOM   8207  O  O   . VAL C  1 159 ? 52.821  26.974  79.516  1.00 25.33  ? 159 VAL C O   1 
ATOM   8208  C  CB  . VAL C  1 159 ? 55.874  27.309  79.603  1.00 21.84  ? 159 VAL C CB  1 
ATOM   8209  C  CG1 . VAL C  1 159 ? 55.989  27.865  78.193  1.00 26.45  ? 159 VAL C CG1 1 
ATOM   8210  C  CG2 . VAL C  1 159 ? 57.169  27.447  80.356  1.00 24.61  ? 159 VAL C CG2 1 
ATOM   8211  N  N   . LEU C  1 160 ? 53.169  29.050  78.825  1.00 20.99  ? 160 LEU C N   1 
ATOM   8212  C  CA  . LEU C  1 160 ? 52.005  29.000  77.973  1.00 17.31  ? 160 LEU C CA  1 
ATOM   8213  C  C   . LEU C  1 160 ? 52.701  28.953  76.628  1.00 23.34  ? 160 LEU C C   1 
ATOM   8214  O  O   . LEU C  1 160 ? 53.504  29.844  76.299  1.00 23.48  ? 160 LEU C O   1 
ATOM   8215  C  CB  . LEU C  1 160 ? 51.147  30.241  78.144  1.00 13.29  ? 160 LEU C CB  1 
ATOM   8216  C  CG  . LEU C  1 160 ? 50.635  30.525  79.566  1.00 16.87  ? 160 LEU C CG  1 
ATOM   8217  C  CD1 . LEU C  1 160 ? 49.948  31.832  79.634  1.00 9.47   ? 160 LEU C CD1 1 
ATOM   8218  C  CD2 . LEU C  1 160 ? 49.693  29.479  80.052  1.00 19.05  ? 160 LEU C CD2 1 
ATOM   8219  N  N   . PHE C  1 161 ? 52.572  27.805  75.966  1.00 27.80  ? 161 PHE C N   1 
ATOM   8220  C  CA  . PHE C  1 161 ? 53.191  27.572  74.666  1.00 26.08  ? 161 PHE C CA  1 
ATOM   8221  C  C   . PHE C  1 161 ? 52.265  27.918  73.518  1.00 26.84  ? 161 PHE C C   1 
ATOM   8222  O  O   . PHE C  1 161 ? 51.233  27.307  73.286  1.00 24.89  ? 161 PHE C O   1 
ATOM   8223  C  CB  . PHE C  1 161 ? 53.654  26.140  74.548  1.00 25.24  ? 161 PHE C CB  1 
ATOM   8224  C  CG  . PHE C  1 161 ? 54.589  25.933  73.441  1.00 20.70  ? 161 PHE C CG  1 
ATOM   8225  C  CD1 . PHE C  1 161 ? 54.121  25.659  72.190  1.00 15.75  ? 161 PHE C CD1 1 
ATOM   8226  C  CD2 . PHE C  1 161 ? 55.952  26.093  73.648  1.00 23.27  ? 161 PHE C CD2 1 
ATOM   8227  C  CE1 . PHE C  1 161 ? 54.998  25.552  71.150  1.00 24.25  ? 161 PHE C CE1 1 
ATOM   8228  C  CE2 . PHE C  1 161 ? 56.856  25.992  72.596  1.00 13.54  ? 161 PHE C CE2 1 
ATOM   8229  C  CZ  . PHE C  1 161 ? 56.390  25.724  71.361  1.00 20.60  ? 161 PHE C CZ  1 
ATOM   8230  N  N   . VAL C  1 162 ? 52.771  28.767  72.664  1.00 29.34  ? 162 VAL C N   1 
ATOM   8231  C  CA  . VAL C  1 162 ? 51.967  29.311  71.617  1.00 23.91  ? 162 VAL C CA  1 
ATOM   8232  C  C   . VAL C  1 162 ? 52.013  28.614  70.258  1.00 22.61  ? 162 VAL C C   1 
ATOM   8233  O  O   . VAL C  1 162 ? 51.549  29.144  69.239  1.00 24.31  ? 162 VAL C O   1 
ATOM   8234  C  CB  . VAL C  1 162 ? 52.253  30.831  71.671  1.00 18.33  ? 162 VAL C CB  1 
ATOM   8235  C  CG1 . VAL C  1 162 ? 52.553  31.404  70.379  1.00 19.95  ? 162 VAL C CG1 1 
ATOM   8236  C  CG2 . VAL C  1 162 ? 51.151  31.546  72.375  1.00 14.15  ? 162 VAL C CG2 1 
ATOM   8237  N  N   . GLY C  1 163 ? 52.482  27.380  70.219  1.00 15.82  ? 163 GLY C N   1 
ATOM   8238  C  CA  . GLY C  1 163 ? 52.498  26.749  68.917  1.00 19.50  ? 163 GLY C CA  1 
ATOM   8239  C  C   . GLY C  1 163 ? 53.825  26.580  68.216  1.00 20.92  ? 163 GLY C C   1 
ATOM   8240  O  O   . GLY C  1 163 ? 54.727  27.354  68.414  1.00 25.93  ? 163 GLY C O   1 
ATOM   8241  N  N   . ASP C  1 164 ? 53.861  25.653  67.259  1.00 26.05  ? 164 ASP C N   1 
ATOM   8242  C  CA  . ASP C  1 164 ? 55.055  25.240  66.483  1.00 22.76  ? 164 ASP C CA  1 
ATOM   8243  C  C   . ASP C  1 164 ? 56.056  24.700  67.470  1.00 25.70  ? 164 ASP C C   1 
ATOM   8244  O  O   . ASP C  1 164 ? 56.897  25.435  68.004  1.00 25.96  ? 164 ASP C O   1 
ATOM   8245  C  CB  . ASP C  1 164 ? 55.665  26.352  65.659  1.00 25.85  ? 164 ASP C CB  1 
ATOM   8246  C  CG  . ASP C  1 164 ? 54.813  26.729  64.479  1.00 31.28  ? 164 ASP C CG  1 
ATOM   8247  O  OD1 . ASP C  1 164 ? 53.694  26.180  64.343  1.00 37.42  ? 164 ASP C OD1 1 
ATOM   8248  O  OD2 . ASP C  1 164 ? 55.103  27.729  63.820  1.00 25.98  ? 164 ASP C OD2 1 
ATOM   8249  N  N   . LEU C  1 165 ? 55.917  23.414  67.759  1.00 24.72  ? 165 LEU C N   1 
ATOM   8250  C  CA  . LEU C  1 165 ? 56.770  22.785  68.725  1.00 21.89  ? 165 LEU C CA  1 
ATOM   8251  C  C   . LEU C  1 165 ? 58.168  22.385  68.247  1.00 27.22  ? 165 LEU C C   1 
ATOM   8252  O  O   . LEU C  1 165 ? 59.150  23.028  68.597  1.00 27.98  ? 165 LEU C O   1 
ATOM   8253  C  CB  . LEU C  1 165 ? 56.051  21.590  69.354  1.00 13.55  ? 165 LEU C CB  1 
ATOM   8254  C  CG  . LEU C  1 165 ? 54.909  21.942  70.297  1.00 13.07  ? 165 LEU C CG  1 
ATOM   8255  C  CD1 . LEU C  1 165 ? 53.702  22.344  69.538  1.00 7.74   ? 165 LEU C CD1 1 
ATOM   8256  C  CD2 . LEU C  1 165 ? 54.590  20.767  71.089  1.00 16.16  ? 165 LEU C CD2 1 
ATOM   8257  N  N   . SER C  1 166 ? 58.281  21.435  67.320  1.00 28.80  ? 166 SER C N   1 
ATOM   8258  C  CA  . SER C  1 166 ? 59.626  20.977  66.979  1.00 22.49  ? 166 SER C CA  1 
ATOM   8259  C  C   . SER C  1 166 ? 60.117  21.166  65.594  1.00 20.68  ? 166 SER C C   1 
ATOM   8260  O  O   . SER C  1 166 ? 61.257  20.856  65.311  1.00 20.74  ? 166 SER C O   1 
ATOM   8261  C  CB  . SER C  1 166 ? 59.703  19.503  67.233  1.00 23.99  ? 166 SER C CB  1 
ATOM   8262  O  OG  . SER C  1 166 ? 58.839  18.862  66.293  1.00 30.87  ? 166 SER C OG  1 
ATOM   8263  N  N   . TYR C  1 167 ? 59.231  21.496  64.682  1.00 22.37  ? 167 TYR C N   1 
ATOM   8264  C  CA  . TYR C  1 167 ? 59.693  21.694  63.322  1.00 20.05  ? 167 TYR C CA  1 
ATOM   8265  C  C   . TYR C  1 167 ? 60.210  20.444  62.684  1.00 20.81  ? 167 TYR C C   1 
ATOM   8266  O  O   . TYR C  1 167 ? 61.017  20.515  61.771  1.00 23.77  ? 167 TYR C O   1 
ATOM   8267  C  CB  . TYR C  1 167 ? 60.778  22.728  63.287  1.00 19.53  ? 167 TYR C CB  1 
ATOM   8268  C  CG  . TYR C  1 167 ? 60.192  24.058  63.494  1.00 20.65  ? 167 TYR C CG  1 
ATOM   8269  C  CD1 . TYR C  1 167 ? 59.971  24.547  64.755  1.00 17.20  ? 167 TYR C CD1 1 
ATOM   8270  C  CD2 . TYR C  1 167 ? 59.802  24.831  62.421  1.00 21.21  ? 167 TYR C CD2 1 
ATOM   8271  C  CE1 . TYR C  1 167 ? 59.378  25.790  64.946  1.00 20.35  ? 167 TYR C CE1 1 
ATOM   8272  C  CE2 . TYR C  1 167 ? 59.201  26.071  62.593  1.00 17.93  ? 167 TYR C CE2 1 
ATOM   8273  C  CZ  . TYR C  1 167 ? 59.001  26.550  63.862  1.00 18.98  ? 167 TYR C CZ  1 
ATOM   8274  O  OH  . TYR C  1 167 ? 58.597  27.825  64.103  1.00 23.46  ? 167 TYR C OH  1 
ATOM   8275  N  N   . ALA C  1 168 ? 59.699  19.291  63.099  1.00 25.53  ? 168 ALA C N   1 
ATOM   8276  C  CA  . ALA C  1 168 ? 60.155  18.039  62.487  1.00 23.08  ? 168 ALA C CA  1 
ATOM   8277  C  C   . ALA C  1 168 ? 59.672  17.944  61.078  1.00 19.99  ? 168 ALA C C   1 
ATOM   8278  O  O   . ALA C  1 168 ? 60.273  17.274  60.270  1.00 22.97  ? 168 ALA C O   1 
ATOM   8279  C  CB  . ALA C  1 168 ? 59.671  16.864  63.253  1.00 20.22  ? 168 ALA C CB  1 
ATOM   8280  N  N   . ASP C  1 169 ? 58.599  18.651  60.757  1.00 20.79  ? 169 ASP C N   1 
ATOM   8281  C  CA  . ASP C  1 169 ? 58.075  18.596  59.403  1.00 20.08  ? 169 ASP C CA  1 
ATOM   8282  C  C   . ASP C  1 169 ? 58.970  19.247  58.396  1.00 21.64  ? 169 ASP C C   1 
ATOM   8283  O  O   . ASP C  1 169 ? 58.684  19.173  57.217  1.00 29.58  ? 169 ASP C O   1 
ATOM   8284  C  CB  . ASP C  1 169 ? 56.682  19.210  59.310  1.00 16.62  ? 169 ASP C CB  1 
ATOM   8285  C  CG  . ASP C  1 169 ? 56.638  20.659  59.749  1.00 19.74  ? 169 ASP C CG  1 
ATOM   8286  O  OD1 . ASP C  1 169 ? 57.446  21.035  60.591  1.00 29.77  ? 169 ASP C OD1 1 
ATOM   8287  O  OD2 . ASP C  1 169 ? 55.757  21.438  59.307  1.00 25.39  ? 169 ASP C OD2 1 
ATOM   8288  N  N   . ARG C  1 170 ? 60.036  19.905  58.842  1.00 21.12  ? 170 ARG C N   1 
ATOM   8289  C  CA  . ARG C  1 170 ? 60.948  20.549  57.899  1.00 22.48  ? 170 ARG C CA  1 
ATOM   8290  C  C   . ARG C  1 170 ? 61.875  19.501  57.386  1.00 25.32  ? 170 ARG C C   1 
ATOM   8291  O  O   . ARG C  1 170 ? 62.496  19.671  56.357  1.00 32.21  ? 170 ARG C O   1 
ATOM   8292  C  CB  . ARG C  1 170 ? 61.779  21.607  58.575  1.00 24.79  ? 170 ARG C CB  1 
ATOM   8293  C  CG  . ARG C  1 170 ? 60.968  22.562  59.356  1.00 36.97  ? 170 ARG C CG  1 
ATOM   8294  C  CD  . ARG C  1 170 ? 61.803  23.708  59.834  1.00 46.15  ? 170 ARG C CD  1 
ATOM   8295  N  NE  . ARG C  1 170 ? 62.336  24.427  58.689  1.00 46.05  ? 170 ARG C NE  1 
ATOM   8296  C  CZ  . ARG C  1 170 ? 63.618  24.369  58.344  1.00 46.96  ? 170 ARG C CZ  1 
ATOM   8297  N  NH1 . ARG C  1 170 ? 64.471  23.632  59.089  1.00 43.69  ? 170 ARG C NH1 1 
ATOM   8298  N  NH2 . ARG C  1 170 ? 64.025  24.974  57.227  1.00 35.63  ? 170 ARG C NH2 1 
ATOM   8299  N  N   . TYR C  1 171 ? 62.034  18.435  58.156  1.00 29.90  ? 171 TYR C N   1 
ATOM   8300  C  CA  . TYR C  1 171 ? 62.893  17.331  57.769  1.00 28.48  ? 171 TYR C CA  1 
ATOM   8301  C  C   . TYR C  1 171 ? 62.160  16.499  56.764  1.00 32.41  ? 171 TYR C C   1 
ATOM   8302  O  O   . TYR C  1 171 ? 60.931  16.554  56.662  1.00 43.45  ? 171 TYR C O   1 
ATOM   8303  C  CB  . TYR C  1 171 ? 63.232  16.506  58.978  1.00 24.62  ? 171 TYR C CB  1 
ATOM   8304  C  CG  . TYR C  1 171 ? 64.128  17.259  59.882  1.00 27.27  ? 171 TYR C CG  1 
ATOM   8305  C  CD1 . TYR C  1 171 ? 63.631  18.097  60.854  1.00 27.14  ? 171 TYR C CD1 1 
ATOM   8306  C  CD2 . TYR C  1 171 ? 65.491  17.166  59.733  1.00 28.13  ? 171 TYR C CD2 1 
ATOM   8307  C  CE1 . TYR C  1 171 ? 64.492  18.822  61.639  1.00 26.19  ? 171 TYR C CE1 1 
ATOM   8308  C  CE2 . TYR C  1 171 ? 66.337  17.872  60.515  1.00 24.40  ? 171 TYR C CE2 1 
ATOM   8309  C  CZ  . TYR C  1 171 ? 65.844  18.694  61.455  1.00 24.66  ? 171 TYR C CZ  1 
ATOM   8310  O  OH  . TYR C  1 171 ? 66.760  19.403  62.192  1.00 38.65  ? 171 TYR C OH  1 
ATOM   8311  N  N   . PRO C  1 172 ? 62.892  15.721  55.983  1.00 33.02  ? 172 PRO C N   1 
ATOM   8312  C  CA  . PRO C  1 172 ? 62.234  14.885  54.973  1.00 31.05  ? 172 PRO C CA  1 
ATOM   8313  C  C   . PRO C  1 172 ? 61.345  13.845  55.613  1.00 30.07  ? 172 PRO C C   1 
ATOM   8314  O  O   . PRO C  1 172 ? 61.650  13.323  56.677  1.00 29.62  ? 172 PRO C O   1 
ATOM   8315  C  CB  . PRO C  1 172 ? 63.409  14.287  54.212  1.00 32.24  ? 172 PRO C CB  1 
ATOM   8316  C  CG  . PRO C  1 172 ? 64.509  14.293  55.190  1.00 30.70  ? 172 PRO C CG  1 
ATOM   8317  C  CD  . PRO C  1 172 ? 64.353  15.557  55.970  1.00 31.56  ? 172 PRO C CD  1 
ATOM   8318  N  N   . ASN C  1 173 ? 60.207  13.588  54.988  1.00 32.22  ? 173 ASN C N   1 
ATOM   8319  C  CA  . ASN C  1 173 ? 59.213  12.638  55.523  1.00 24.64  ? 173 ASN C CA  1 
ATOM   8320  C  C   . ASN C  1 173 ? 58.886  13.012  56.993  1.00 20.78  ? 173 ASN C C   1 
ATOM   8321  O  O   . ASN C  1 173 ? 58.481  12.169  57.805  1.00 22.86  ? 173 ASN C O   1 
ATOM   8322  C  CB  . ASN C  1 173 ? 59.677  11.178  55.375  1.00 26.96  ? 173 ASN C CB  1 
ATOM   8323  C  CG  . ASN C  1 173 ? 60.115  10.802  53.923  1.00 29.20  ? 173 ASN C CG  1 
ATOM   8324  O  OD1 . ASN C  1 173 ? 61.126  10.128  53.745  1.00 31.32  ? 173 ASN C OD1 1 
ATOM   8325  N  ND2 . ASN C  1 173 ? 59.333  11.190  52.909  1.00 30.31  ? 173 ASN C ND2 1 
ATOM   8326  N  N   . HIS C  1 174 ? 59.073  14.297  57.311  1.00 14.39  ? 174 HIS C N   1 
ATOM   8327  C  CA  . HIS C  1 174 ? 58.806  14.843  58.622  1.00 17.99  ? 174 HIS C CA  1 
ATOM   8328  C  C   . HIS C  1 174 ? 59.548  14.062  59.696  1.00 20.64  ? 174 HIS C C   1 
ATOM   8329  O  O   . HIS C  1 174 ? 59.132  14.068  60.855  1.00 22.26  ? 174 HIS C O   1 
ATOM   8330  C  CB  . HIS C  1 174 ? 57.317  14.772  58.952  1.00 14.24  ? 174 HIS C CB  1 
ATOM   8331  C  CG  . HIS C  1 174 ? 56.459  15.550  58.014  1.00 18.34  ? 174 HIS C CG  1 
ATOM   8332  N  ND1 . HIS C  1 174 ? 55.274  16.139  58.402  1.00 24.88  ? 174 HIS C ND1 1 
ATOM   8333  C  CD2 . HIS C  1 174 ? 56.575  15.787  56.691  1.00 15.86  ? 174 HIS C CD2 1 
ATOM   8334  C  CE1 . HIS C  1 174 ? 54.694  16.696  57.359  1.00 20.06  ? 174 HIS C CE1 1 
ATOM   8335  N  NE2 . HIS C  1 174 ? 55.461  16.499  56.313  1.00 18.03  ? 174 HIS C NE2 1 
ATOM   8336  N  N   . ASP C  1 175 ? 60.606  13.362  59.297  1.00 21.35  ? 175 ASP C N   1 
ATOM   8337  C  CA  . ASP C  1 175 ? 61.427  12.540  60.192  1.00 20.03  ? 175 ASP C CA  1 
ATOM   8338  C  C   . ASP C  1 175 ? 61.020  12.668  61.634  1.00 15.84  ? 175 ASP C C   1 
ATOM   8339  O  O   . ASP C  1 175 ? 61.569  13.473  62.358  1.00 12.07  ? 175 ASP C O   1 
ATOM   8340  C  CB  . ASP C  1 175 ? 62.910  12.906  60.042  1.00 24.31  ? 175 ASP C CB  1 
ATOM   8341  C  CG  . ASP C  1 175 ? 63.820  11.876  60.670  1.00 34.53  ? 175 ASP C CG  1 
ATOM   8342  O  OD1 . ASP C  1 175 ? 63.280  10.992  61.394  1.00 38.83  ? 175 ASP C OD1 1 
ATOM   8343  O  OD2 . ASP C  1 175 ? 65.060  11.928  60.438  1.00 38.45  ? 175 ASP C OD2 1 
ATOM   8344  N  N   . ASN C  1 176 ? 60.056  11.873  62.066  1.00 16.74  ? 176 ASN C N   1 
ATOM   8345  C  CA  . ASN C  1 176 ? 59.606  11.998  63.464  1.00 19.37  ? 176 ASN C CA  1 
ATOM   8346  C  C   . ASN C  1 176 ? 60.672  11.843  64.550  1.00 20.24  ? 176 ASN C C   1 
ATOM   8347  O  O   . ASN C  1 176 ? 60.380  12.005  65.716  1.00 22.46  ? 176 ASN C O   1 
ATOM   8348  C  CB  . ASN C  1 176 ? 58.423  11.080  63.780  1.00 20.90  ? 176 ASN C CB  1 
ATOM   8349  C  CG  . ASN C  1 176 ? 57.113  11.617  63.255  1.00 26.27  ? 176 ASN C CG  1 
ATOM   8350  O  OD1 . ASN C  1 176 ? 56.044  11.356  63.818  1.00 22.64  ? 176 ASN C OD1 1 
ATOM   8351  N  ND2 . ASN C  1 176 ? 57.178  12.369  62.180  1.00 25.55  ? 176 ASN C ND2 1 
ATOM   8352  N  N   . VAL C  1 177 ? 61.906  11.514  64.192  1.00 19.45  ? 177 VAL C N   1 
ATOM   8353  C  CA  . VAL C  1 177 ? 62.915  11.376  65.219  1.00 17.83  ? 177 VAL C CA  1 
ATOM   8354  C  C   . VAL C  1 177 ? 63.075  12.728  65.818  1.00 23.26  ? 177 VAL C C   1 
ATOM   8355  O  O   . VAL C  1 177 ? 63.354  12.866  67.008  1.00 27.89  ? 177 VAL C O   1 
ATOM   8356  C  CB  . VAL C  1 177 ? 64.266  11.001  64.652  1.00 16.71  ? 177 VAL C CB  1 
ATOM   8357  C  CG1 . VAL C  1 177 ? 65.358  11.220  65.701  1.00 13.34  ? 177 VAL C CG1 1 
ATOM   8358  C  CG2 . VAL C  1 177 ? 64.253  9.586   64.244  1.00 12.50  ? 177 VAL C CG2 1 
ATOM   8359  N  N   . ARG C  1 178 ? 62.924  13.737  64.965  1.00 23.18  ? 178 ARG C N   1 
ATOM   8360  C  CA  . ARG C  1 178 ? 63.049  15.102  65.390  1.00 19.14  ? 178 ARG C CA  1 
ATOM   8361  C  C   . ARG C  1 178 ? 61.991  15.455  66.432  1.00 19.70  ? 178 ARG C C   1 
ATOM   8362  O  O   . ARG C  1 178 ? 62.132  16.434  67.154  1.00 26.35  ? 178 ARG C O   1 
ATOM   8363  C  CB  . ARG C  1 178 ? 63.080  16.005  64.182  1.00 19.04  ? 178 ARG C CB  1 
ATOM   8364  C  CG  . ARG C  1 178 ? 64.493  16.032  63.487  1.00 20.60  ? 178 ARG C CG  1 
ATOM   8365  C  CD  . ARG C  1 178 ? 65.588  16.591  64.442  1.00 24.47  ? 178 ARG C CD  1 
ATOM   8366  N  NE  . ARG C  1 178 ? 66.882  16.746  63.790  1.00 26.65  ? 178 ARG C NE  1 
ATOM   8367  C  CZ  . ARG C  1 178 ? 67.949  17.342  64.339  1.00 25.65  ? 178 ARG C CZ  1 
ATOM   8368  N  NH1 . ARG C  1 178 ? 67.924  17.836  65.556  1.00 22.36  ? 178 ARG C NH1 1 
ATOM   8369  N  NH2 . ARG C  1 178 ? 69.054  17.484  63.639  1.00 31.87  ? 178 ARG C NH2 1 
ATOM   8370  N  N   . TRP C  1 179 ? 60.958  14.630  66.550  1.00 17.00  ? 179 TRP C N   1 
ATOM   8371  C  CA  . TRP C  1 179 ? 59.960  14.854  67.589  1.00 12.63  ? 179 TRP C CA  1 
ATOM   8372  C  C   . TRP C  1 179 ? 60.534  14.243  68.833  1.00 17.12  ? 179 TRP C C   1 
ATOM   8373  O  O   . TRP C  1 179 ? 60.306  14.743  69.940  1.00 21.16  ? 179 TRP C O   1 
ATOM   8374  C  CB  . TRP C  1 179 ? 58.655  14.142  67.290  1.00 11.94  ? 179 TRP C CB  1 
ATOM   8375  C  CG  . TRP C  1 179 ? 57.672  15.005  66.582  1.00 16.67  ? 179 TRP C CG  1 
ATOM   8376  C  CD1 . TRP C  1 179 ? 57.254  14.879  65.280  1.00 14.61  ? 179 TRP C CD1 1 
ATOM   8377  C  CD2 . TRP C  1 179 ? 56.961  16.097  67.144  1.00 12.11  ? 179 TRP C CD2 1 
ATOM   8378  N  NE1 . TRP C  1 179 ? 56.299  15.852  65.016  1.00 16.71  ? 179 TRP C NE1 1 
ATOM   8379  C  CE2 . TRP C  1 179 ? 56.110  16.602  66.157  1.00 12.05  ? 179 TRP C CE2 1 
ATOM   8380  C  CE3 . TRP C  1 179 ? 56.949  16.707  68.397  1.00 12.08  ? 179 TRP C CE3 1 
ATOM   8381  C  CZ2 . TRP C  1 179 ? 55.251  17.674  66.361  1.00 11.75  ? 179 TRP C CZ2 1 
ATOM   8382  C  CZ3 . TRP C  1 179 ? 56.101  17.767  68.628  1.00 14.09  ? 179 TRP C CZ3 1 
ATOM   8383  C  CH2 . TRP C  1 179 ? 55.266  18.237  67.612  1.00 12.60  ? 179 TRP C CH2 1 
ATOM   8384  N  N   . ASP C  1 180 ? 61.265  13.137  68.671  1.00 19.58  ? 180 ASP C N   1 
ATOM   8385  C  CA  . ASP C  1 180 ? 61.869  12.452  69.802  1.00 16.62  ? 180 ASP C CA  1 
ATOM   8386  C  C   . ASP C  1 180 ? 62.935  13.324  70.407  1.00 19.09  ? 180 ASP C C   1 
ATOM   8387  O  O   . ASP C  1 180 ? 62.946  13.545  71.613  1.00 23.70  ? 180 ASP C O   1 
ATOM   8388  C  CB  . ASP C  1 180 ? 62.462  11.110  69.383  1.00 19.25  ? 180 ASP C CB  1 
ATOM   8389  C  CG  . ASP C  1 180 ? 61.384  10.060  69.031  1.00 27.94  ? 180 ASP C CG  1 
ATOM   8390  O  OD1 . ASP C  1 180 ? 60.353  9.929   69.747  1.00 21.18  ? 180 ASP C OD1 1 
ATOM   8391  O  OD2 . ASP C  1 180 ? 61.574  9.351   68.020  1.00 30.60  ? 180 ASP C OD2 1 
ATOM   8392  N  N   . THR C  1 181 ? 63.810  13.885  69.576  1.00 20.68  ? 181 THR C N   1 
ATOM   8393  C  CA  . THR C  1 181 ? 64.872  14.733  70.101  1.00 19.10  ? 181 THR C CA  1 
ATOM   8394  C  C   . THR C  1 181 ? 64.316  15.944  70.830  1.00 22.78  ? 181 THR C C   1 
ATOM   8395  O  O   . THR C  1 181 ? 64.735  16.232  71.963  1.00 19.08  ? 181 THR C O   1 
ATOM   8396  C  CB  . THR C  1 181 ? 65.816  15.192  69.005  1.00 21.89  ? 181 THR C CB  1 
ATOM   8397  O  OG1 . THR C  1 181 ? 65.088  15.893  68.010  1.00 30.91  ? 181 THR C OG1 1 
ATOM   8398  C  CG2 . THR C  1 181 ? 66.423  14.007  68.328  1.00 21.64  ? 181 THR C CG2 1 
ATOM   8399  N  N   . TRP C  1 182 ? 63.316  16.607  70.228  1.00 24.40  ? 182 TRP C N   1 
ATOM   8400  C  CA  . TRP C  1 182 ? 62.716  17.804  70.839  1.00 21.73  ? 182 TRP C CA  1 
ATOM   8401  C  C   . TRP C  1 182 ? 62.158  17.486  72.200  1.00 22.25  ? 182 TRP C C   1 
ATOM   8402  O  O   . TRP C  1 182 ? 62.303  18.247  73.142  1.00 25.61  ? 182 TRP C O   1 
ATOM   8403  C  CB  . TRP C  1 182 ? 61.593  18.333  69.986  1.00 20.33  ? 182 TRP C CB  1 
ATOM   8404  C  CG  . TRP C  1 182 ? 61.145  19.685  70.399  1.00 22.21  ? 182 TRP C CG  1 
ATOM   8405  C  CD1 . TRP C  1 182 ? 61.721  20.856  70.043  1.00 22.71  ? 182 TRP C CD1 1 
ATOM   8406  C  CD2 . TRP C  1 182 ? 60.006  20.026  71.197  1.00 16.90  ? 182 TRP C CD2 1 
ATOM   8407  N  NE1 . TRP C  1 182 ? 61.024  21.894  70.553  1.00 21.97  ? 182 TRP C NE1 1 
ATOM   8408  C  CE2 . TRP C  1 182 ? 59.960  21.421  71.267  1.00 15.53  ? 182 TRP C CE2 1 
ATOM   8409  C  CE3 . TRP C  1 182 ? 59.009  19.282  71.831  1.00 18.12  ? 182 TRP C CE3 1 
ATOM   8410  C  CZ2 . TRP C  1 182 ? 58.961  22.108  71.946  1.00 15.32  ? 182 TRP C CZ2 1 
ATOM   8411  C  CZ3 . TRP C  1 182 ? 57.989  19.966  72.506  1.00 21.84  ? 182 TRP C CZ3 1 
ATOM   8412  C  CH2 . TRP C  1 182 ? 57.978  21.367  72.557  1.00 19.65  ? 182 TRP C CH2 1 
ATOM   8413  N  N   . GLY C  1 183 ? 61.575  16.312  72.318  1.00 21.33  ? 183 GLY C N   1 
ATOM   8414  C  CA  . GLY C  1 183 ? 60.972  15.945  73.574  1.00 22.18  ? 183 GLY C CA  1 
ATOM   8415  C  C   . GLY C  1 183 ? 61.981  15.685  74.645  1.00 22.42  ? 183 GLY C C   1 
ATOM   8416  O  O   . GLY C  1 183 ? 61.704  15.833  75.846  1.00 27.08  ? 183 GLY C O   1 
ATOM   8417  N  N   . ARG C  1 184 ? 63.147  15.250  74.215  1.00 21.54  ? 184 ARG C N   1 
ATOM   8418  C  CA  . ARG C  1 184 ? 64.219  14.969  75.154  1.00 21.84  ? 184 ARG C CA  1 
ATOM   8419  C  C   . ARG C  1 184 ? 64.843  16.292  75.551  1.00 23.43  ? 184 ARG C C   1 
ATOM   8420  O  O   . ARG C  1 184 ? 65.204  16.520  76.706  1.00 22.09  ? 184 ARG C O   1 
ATOM   8421  C  CB  . ARG C  1 184 ? 65.271  14.051  74.479  1.00 27.33  ? 184 ARG C CB  1 
ATOM   8422  C  CG  . ARG C  1 184 ? 65.076  12.494  74.651  1.00 22.58  ? 184 ARG C CG  1 
ATOM   8423  C  CD  . ARG C  1 184 ? 66.230  11.702  74.041  1.00 13.51  ? 184 ARG C CD  1 
ATOM   8424  N  NE  . ARG C  1 184 ? 65.749  10.797  73.013  1.00 22.36  ? 184 ARG C NE  1 
ATOM   8425  C  CZ  . ARG C  1 184 ? 66.281  10.685  71.793  1.00 26.01  ? 184 ARG C CZ  1 
ATOM   8426  N  NH1 . ARG C  1 184 ? 67.314  11.432  71.456  1.00 24.46  ? 184 ARG C NH1 1 
ATOM   8427  N  NH2 . ARG C  1 184 ? 65.799  9.809   70.893  1.00 33.76  ? 184 ARG C NH2 1 
ATOM   8428  N  N   . PHE C  1 185 ? 64.958  17.171  74.561  1.00 24.84  ? 185 PHE C N   1 
ATOM   8429  C  CA  . PHE C  1 185 ? 65.518  18.507  74.737  1.00 22.92  ? 185 PHE C CA  1 
ATOM   8430  C  C   . PHE C  1 185 ? 64.770  19.332  75.785  1.00 23.78  ? 185 PHE C C   1 
ATOM   8431  O  O   . PHE C  1 185 ? 65.392  19.831  76.744  1.00 24.47  ? 185 PHE C O   1 
ATOM   8432  C  CB  . PHE C  1 185 ? 65.494  19.200  73.383  1.00 23.57  ? 185 PHE C CB  1 
ATOM   8433  C  CG  . PHE C  1 185 ? 65.628  20.686  73.428  1.00 13.34  ? 185 PHE C CG  1 
ATOM   8434  C  CD1 . PHE C  1 185 ? 66.446  21.316  74.326  1.00 18.02  ? 185 PHE C CD1 1 
ATOM   8435  C  CD2 . PHE C  1 185 ? 64.899  21.460  72.532  1.00 13.84  ? 185 PHE C CD2 1 
ATOM   8436  C  CE1 . PHE C  1 185 ? 66.534  22.709  74.354  1.00 17.05  ? 185 PHE C CE1 1 
ATOM   8437  C  CE2 . PHE C  1 185 ? 64.983  22.823  72.545  1.00 11.59  ? 185 PHE C CE2 1 
ATOM   8438  C  CZ  . PHE C  1 185 ? 65.800  23.449  73.462  1.00 15.85  ? 185 PHE C CZ  1 
ATOM   8439  N  N   . THR C  1 186 ? 63.445  19.419  75.634  1.00 19.92  ? 186 THR C N   1 
ATOM   8440  C  CA  . THR C  1 186 ? 62.592  20.191  76.536  1.00 19.96  ? 186 THR C CA  1 
ATOM   8441  C  C   . THR C  1 186 ? 62.315  19.553  77.900  1.00 24.58  ? 186 THR C C   1 
ATOM   8442  O  O   . THR C  1 186 ? 61.879  20.234  78.823  1.00 29.99  ? 186 THR C O   1 
ATOM   8443  C  CB  . THR C  1 186 ? 61.259  20.489  75.846  1.00 17.57  ? 186 THR C CB  1 
ATOM   8444  O  OG1 . THR C  1 186 ? 60.693  19.261  75.352  1.00 31.04  ? 186 THR C OG1 1 
ATOM   8445  C  CG2 . THR C  1 186 ? 61.471  21.400  74.638  1.00 19.89  ? 186 THR C CG2 1 
ATOM   8446  N  N   . GLU C  1 187 ? 62.573  18.257  78.061  1.00 29.10  ? 187 GLU C N   1 
ATOM   8447  C  CA  . GLU C  1 187 ? 62.279  17.562  79.333  1.00 26.27  ? 187 GLU C CA  1 
ATOM   8448  C  C   . GLU C  1 187 ? 62.742  18.292  80.570  1.00 24.39  ? 187 GLU C C   1 
ATOM   8449  O  O   . GLU C  1 187 ? 62.049  18.296  81.602  1.00 21.11  ? 187 GLU C O   1 
ATOM   8450  C  CB  . GLU C  1 187 ? 62.879  16.163  79.353  1.00 31.49  ? 187 GLU C CB  1 
ATOM   8451  C  CG  . GLU C  1 187 ? 62.398  15.209  80.482  1.00 33.06  ? 187 GLU C CG  1 
ATOM   8452  C  CD  . GLU C  1 187 ? 63.253  13.948  80.548  1.00 37.10  ? 187 GLU C CD  1 
ATOM   8453  O  OE1 . GLU C  1 187 ? 64.362  14.062  81.108  1.00 38.10  ? 187 GLU C OE1 1 
ATOM   8454  O  OE2 . GLU C  1 187 ? 62.860  12.886  80.006  1.00 32.56  ? 187 GLU C OE2 1 
ATOM   8455  N  N   . ARG C  1 188 ? 63.914  18.905  80.467  1.00 18.95  ? 188 ARG C N   1 
ATOM   8456  C  CA  . ARG C  1 188 ? 64.436  19.630  81.596  1.00 23.02  ? 188 ARG C CA  1 
ATOM   8457  C  C   . ARG C  1 188 ? 63.521  20.699  82.135  1.00 26.46  ? 188 ARG C C   1 
ATOM   8458  O  O   . ARG C  1 188 ? 63.723  21.144  83.247  1.00 32.26  ? 188 ARG C O   1 
ATOM   8459  C  CB  . ARG C  1 188 ? 65.784  20.237  81.297  1.00 27.88  ? 188 ARG C CB  1 
ATOM   8460  C  CG  . ARG C  1 188 ? 65.816  21.501  80.458  1.00 34.08  ? 188 ARG C CG  1 
ATOM   8461  C  CD  . ARG C  1 188 ? 67.247  21.655  79.882  1.00 40.48  ? 188 ARG C CD  1 
ATOM   8462  N  NE  . ARG C  1 188 ? 67.713  23.022  79.682  1.00 37.96  ? 188 ARG C NE  1 
ATOM   8463  C  CZ  . ARG C  1 188 ? 68.349  23.435  78.591  1.00 42.06  ? 188 ARG C CZ  1 
ATOM   8464  N  NH1 . ARG C  1 188 ? 68.619  22.595  77.605  1.00 49.19  ? 188 ARG C NH1 1 
ATOM   8465  N  NH2 . ARG C  1 188 ? 68.614  24.708  78.422  1.00 42.99  ? 188 ARG C NH2 1 
ATOM   8466  N  N   . SER C  1 189 ? 62.551  21.160  81.359  1.00 25.08  ? 189 SER C N   1 
ATOM   8467  C  CA  . SER C  1 189 ? 61.635  22.136  81.880  1.00 20.84  ? 189 SER C CA  1 
ATOM   8468  C  C   . SER C  1 189 ? 60.304  21.469  82.143  1.00 19.13  ? 189 SER C C   1 
ATOM   8469  O  O   . SER C  1 189 ? 59.855  21.388  83.284  1.00 19.45  ? 189 SER C O   1 
ATOM   8470  C  CB  . SER C  1 189 ? 61.464  23.277  80.894  1.00 26.85  ? 189 SER C CB  1 
ATOM   8471  O  OG  . SER C  1 189 ? 60.686  24.301  81.466  1.00 25.62  ? 189 SER C OG  1 
ATOM   8472  N  N   . VAL C  1 190 ? 59.752  20.869  81.099  1.00 18.28  ? 190 VAL C N   1 
ATOM   8473  C  CA  . VAL C  1 190 ? 58.432  20.244  81.190  1.00 21.36  ? 190 VAL C CA  1 
ATOM   8474  C  C   . VAL C  1 190 ? 58.262  19.092  82.111  1.00 25.21  ? 190 VAL C C   1 
ATOM   8475  O  O   . VAL C  1 190 ? 57.125  18.652  82.318  1.00 29.86  ? 190 VAL C O   1 
ATOM   8476  C  CB  . VAL C  1 190 ? 57.929  19.645  79.884  1.00 21.76  ? 190 VAL C CB  1 
ATOM   8477  C  CG1 . VAL C  1 190 ? 56.605  20.215  79.538  1.00 21.23  ? 190 VAL C CG1 1 
ATOM   8478  C  CG2 . VAL C  1 190 ? 58.906  19.812  78.798  1.00 28.23  ? 190 VAL C CG2 1 
ATOM   8479  N  N   . ALA C  1 191 ? 59.359  18.486  82.555  1.00 23.35  ? 191 ALA C N   1 
ATOM   8480  C  CA  . ALA C  1 191 ? 59.191  17.346  83.421  1.00 21.74  ? 191 ALA C CA  1 
ATOM   8481  C  C   . ALA C  1 191 ? 58.875  17.887  84.762  1.00 23.70  ? 191 ALA C C   1 
ATOM   8482  O  O   . ALA C  1 191 ? 58.377  17.164  85.587  1.00 25.22  ? 191 ALA C O   1 
ATOM   8483  C  CB  . ALA C  1 191 ? 60.422  16.543  83.477  1.00 21.44  ? 191 ALA C CB  1 
ATOM   8484  N  N   . TYR C  1 192 ? 59.109  19.180  84.958  1.00 27.86  ? 192 TYR C N   1 
ATOM   8485  C  CA  . TYR C  1 192 ? 58.869  19.799  86.239  1.00 32.34  ? 192 TYR C CA  1 
ATOM   8486  C  C   . TYR C  1 192 ? 57.759  20.829  86.355  1.00 34.75  ? 192 TYR C C   1 
ATOM   8487  O  O   . TYR C  1 192 ? 57.219  21.085  87.460  1.00 40.39  ? 192 TYR C O   1 
ATOM   8488  C  CB  . TYR C  1 192 ? 60.139  20.406  86.720  1.00 35.03  ? 192 TYR C CB  1 
ATOM   8489  C  CG  . TYR C  1 192 ? 61.250  19.415  86.710  1.00 43.40  ? 192 TYR C CG  1 
ATOM   8490  C  CD1 . TYR C  1 192 ? 61.516  18.584  87.805  1.00 44.99  ? 192 TYR C CD1 1 
ATOM   8491  C  CD2 . TYR C  1 192 ? 62.065  19.317  85.600  1.00 49.77  ? 192 TYR C CD2 1 
ATOM   8492  C  CE1 . TYR C  1 192 ? 62.590  17.674  87.765  1.00 49.90  ? 192 TYR C CE1 1 
ATOM   8493  C  CE2 . TYR C  1 192 ? 63.127  18.433  85.550  1.00 49.52  ? 192 TYR C CE2 1 
ATOM   8494  C  CZ  . TYR C  1 192 ? 63.393  17.613  86.621  1.00 49.48  ? 192 TYR C CZ  1 
ATOM   8495  O  OH  . TYR C  1 192 ? 64.469  16.739  86.505  1.00 58.22  ? 192 TYR C OH  1 
ATOM   8496  N  N   . GLN C  1 193 ? 57.485  21.532  85.273  1.00 32.22  ? 193 GLN C N   1 
ATOM   8497  C  CA  . GLN C  1 193 ? 56.404  22.507  85.353  1.00 29.61  ? 193 GLN C CA  1 
ATOM   8498  C  C   . GLN C  1 193 ? 55.613  22.339  84.105  1.00 24.28  ? 193 GLN C C   1 
ATOM   8499  O  O   . GLN C  1 193 ? 56.160  22.093  83.051  1.00 30.94  ? 193 GLN C O   1 
ATOM   8500  C  CB  . GLN C  1 193 ? 56.907  23.950  85.510  1.00 31.09  ? 193 GLN C CB  1 
ATOM   8501  C  CG  . GLN C  1 193 ? 57.611  24.514  84.312  1.00 40.80  ? 193 GLN C CG  1 
ATOM   8502  C  CD  . GLN C  1 193 ? 57.875  26.007  84.419  1.00 44.65  ? 193 GLN C CD  1 
ATOM   8503  O  OE1 . GLN C  1 193 ? 57.147  26.854  83.846  1.00 50.19  ? 193 GLN C OE1 1 
ATOM   8504  N  NE2 . GLN C  1 193 ? 58.935  26.344  85.139  1.00 52.93  ? 193 GLN C NE2 1 
ATOM   8505  N  N   . PRO C  1 194 ? 54.303  22.375  84.220  1.00 16.51  ? 194 PRO C N   1 
ATOM   8506  C  CA  . PRO C  1 194 ? 53.447  22.217  83.070  1.00 13.75  ? 194 PRO C CA  1 
ATOM   8507  C  C   . PRO C  1 194 ? 53.666  23.244  82.026  1.00 15.18  ? 194 PRO C C   1 
ATOM   8508  O  O   . PRO C  1 194 ? 54.118  24.354  82.288  1.00 23.10  ? 194 PRO C O   1 
ATOM   8509  C  CB  . PRO C  1 194 ? 52.056  22.375  83.661  1.00 12.00  ? 194 PRO C CB  1 
ATOM   8510  C  CG  . PRO C  1 194 ? 52.282  23.210  84.820  1.00 19.90  ? 194 PRO C CG  1 
ATOM   8511  C  CD  . PRO C  1 194 ? 53.501  22.604  85.417  1.00 17.35  ? 194 PRO C CD  1 
ATOM   8512  N  N   . TRP C  1 195 ? 53.384  22.842  80.799  1.00 15.60  ? 195 TRP C N   1 
ATOM   8513  C  CA  . TRP C  1 195 ? 53.446  23.737  79.650  1.00 16.97  ? 195 TRP C CA  1 
ATOM   8514  C  C   . TRP C  1 195 ? 52.008  23.582  79.087  1.00 20.66  ? 195 TRP C C   1 
ATOM   8515  O  O   . TRP C  1 195 ? 51.439  22.451  79.067  1.00 20.50  ? 195 TRP C O   1 
ATOM   8516  C  CB  . TRP C  1 195 ? 54.521  23.301  78.626  1.00 12.26  ? 195 TRP C CB  1 
ATOM   8517  C  CG  . TRP C  1 195 ? 55.985  23.693  78.931  1.00 13.59  ? 195 TRP C CG  1 
ATOM   8518  C  CD1 . TRP C  1 195 ? 56.568  23.761  80.156  1.00 17.51  ? 195 TRP C CD1 1 
ATOM   8519  C  CD2 . TRP C  1 195 ? 57.051  23.974  77.971  1.00 12.71  ? 195 TRP C CD2 1 
ATOM   8520  N  NE1 . TRP C  1 195 ? 57.923  24.033  80.032  1.00 15.57  ? 195 TRP C NE1 1 
ATOM   8521  C  CE2 . TRP C  1 195 ? 58.235  24.173  78.710  1.00 10.19  ? 195 TRP C CE2 1 
ATOM   8522  C  CE3 . TRP C  1 195 ? 57.103  24.076  76.574  1.00 7.05   ? 195 TRP C CE3 1 
ATOM   8523  C  CZ2 . TRP C  1 195 ? 59.450  24.475  78.110  1.00 7.67   ? 195 TRP C CZ2 1 
ATOM   8524  C  CZ3 . TRP C  1 195 ? 58.324  24.382  75.968  1.00 8.82   ? 195 TRP C CZ3 1 
ATOM   8525  C  CH2 . TRP C  1 195 ? 59.476  24.580  76.741  1.00 14.04  ? 195 TRP C CH2 1 
ATOM   8526  N  N   . ILE C  1 196 ? 51.356  24.705  78.780  1.00 19.58  ? 196 ILE C N   1 
ATOM   8527  C  CA  . ILE C  1 196 ? 50.014  24.652  78.200  1.00 19.60  ? 196 ILE C CA  1 
ATOM   8528  C  C   . ILE C  1 196 ? 50.215  24.678  76.693  1.00 20.40  ? 196 ILE C C   1 
ATOM   8529  O  O   . ILE C  1 196 ? 50.868  25.592  76.180  1.00 21.51  ? 196 ILE C O   1 
ATOM   8530  C  CB  . ILE C  1 196 ? 49.190  25.781  78.677  1.00 21.30  ? 196 ILE C CB  1 
ATOM   8531  C  CG1 . ILE C  1 196 ? 49.282  25.857  80.198  1.00 25.60  ? 196 ILE C CG1 1 
ATOM   8532  C  CG2 . ILE C  1 196 ? 47.775  25.551  78.263  1.00 23.85  ? 196 ILE C CG2 1 
ATOM   8533  C  CD1 . ILE C  1 196 ? 48.914  24.591  80.901  1.00 26.24  ? 196 ILE C CD1 1 
ATOM   8534  N  N   . TRP C  1 197 ? 49.664  23.679  76.003  1.00 17.69  ? 197 TRP C N   1 
ATOM   8535  C  CA  . TRP C  1 197 ? 49.884  23.508  74.582  1.00 18.37  ? 197 TRP C CA  1 
ATOM   8536  C  C   . TRP C  1 197 ? 48.881  24.140  73.657  1.00 25.47  ? 197 TRP C C   1 
ATOM   8537  O  O   . TRP C  1 197 ? 47.662  24.030  73.867  1.00 29.88  ? 197 TRP C O   1 
ATOM   8538  C  CB  . TRP C  1 197 ? 50.011  22.015  74.216  1.00 16.71  ? 197 TRP C CB  1 
ATOM   8539  C  CG  . TRP C  1 197 ? 51.050  21.291  74.994  1.00 19.89  ? 197 TRP C CG  1 
ATOM   8540  C  CD1 . TRP C  1 197 ? 50.847  20.393  76.013  1.00 23.20  ? 197 TRP C CD1 1 
ATOM   8541  C  CD2 . TRP C  1 197 ? 52.455  21.454  74.896  1.00 16.86  ? 197 TRP C CD2 1 
ATOM   8542  N  NE1 . TRP C  1 197 ? 52.044  19.997  76.566  1.00 19.57  ? 197 TRP C NE1 1 
ATOM   8543  C  CE2 . TRP C  1 197 ? 53.051  20.634  75.888  1.00 21.65  ? 197 TRP C CE2 1 
ATOM   8544  C  CE3 . TRP C  1 197 ? 53.276  22.212  74.080  1.00 18.64  ? 197 TRP C CE3 1 
ATOM   8545  C  CZ2 . TRP C  1 197 ? 54.427  20.572  76.065  1.00 16.67  ? 197 TRP C CZ2 1 
ATOM   8546  C  CZ3 . TRP C  1 197 ? 54.642  22.144  74.256  1.00 15.70  ? 197 TRP C CZ3 1 
ATOM   8547  C  CH2 . TRP C  1 197 ? 55.202  21.340  75.234  1.00 17.08  ? 197 TRP C CH2 1 
ATOM   8548  N  N   . THR C  1 198 ? 49.409  24.671  72.556  1.00 25.28  ? 198 THR C N   1 
ATOM   8549  C  CA  . THR C  1 198 ? 48.621  25.321  71.533  1.00 24.55  ? 198 THR C CA  1 
ATOM   8550  C  C   . THR C  1 198 ? 49.152  24.745  70.237  1.00 27.10  ? 198 THR C C   1 
ATOM   8551  O  O   . THR C  1 198 ? 50.359  24.628  70.027  1.00 29.32  ? 198 THR C O   1 
ATOM   8552  C  CB  . THR C  1 198 ? 48.848  26.814  71.500  1.00 22.53  ? 198 THR C CB  1 
ATOM   8553  O  OG1 . THR C  1 198 ? 48.589  27.370  72.773  1.00 23.05  ? 198 THR C OG1 1 
ATOM   8554  C  CG2 . THR C  1 198 ? 47.887  27.430  70.554  1.00 26.49  ? 198 THR C CG2 1 
ATOM   8555  N  N   . ALA C  1 199 ? 48.246  24.417  69.350  1.00 22.55  ? 199 ALA C N   1 
ATOM   8556  C  CA  . ALA C  1 199 ? 48.623  23.839  68.112  1.00 18.99  ? 199 ALA C CA  1 
ATOM   8557  C  C   . ALA C  1 199 ? 48.956  24.866  67.049  1.00 22.09  ? 199 ALA C C   1 
ATOM   8558  O  O   . ALA C  1 199 ? 48.133  25.744  66.756  1.00 24.96  ? 199 ALA C O   1 
ATOM   8559  C  CB  . ALA C  1 199 ? 47.507  22.968  67.650  1.00 20.95  ? 199 ALA C CB  1 
ATOM   8560  N  N   . GLY C  1 200 ? 50.111  24.696  66.407  1.00 19.80  ? 200 GLY C N   1 
ATOM   8561  C  CA  . GLY C  1 200 ? 50.514  25.618  65.360  1.00 18.80  ? 200 GLY C CA  1 
ATOM   8562  C  C   . GLY C  1 200 ? 50.528  24.936  64.007  1.00 21.29  ? 200 GLY C C   1 
ATOM   8563  O  O   . GLY C  1 200 ? 50.285  23.741  63.920  1.00 27.34  ? 200 GLY C O   1 
ATOM   8564  N  N   . ASN C  1 201 ? 50.892  25.654  62.951  1.00 17.51  ? 201 ASN C N   1 
ATOM   8565  C  CA  . ASN C  1 201 ? 50.870  25.060  61.628  1.00 18.84  ? 201 ASN C CA  1 
ATOM   8566  C  C   . ASN C  1 201 ? 51.902  24.013  61.482  1.00 20.96  ? 201 ASN C C   1 
ATOM   8567  O  O   . ASN C  1 201 ? 51.681  23.059  60.743  1.00 31.51  ? 201 ASN C O   1 
ATOM   8568  C  CB  . ASN C  1 201 ? 50.993  26.091  60.503  1.00 23.94  ? 201 ASN C CB  1 
ATOM   8569  C  CG  . ASN C  1 201 ? 52.104  27.072  60.736  1.00 26.74  ? 201 ASN C CG  1 
ATOM   8570  O  OD1 . ASN C  1 201 ? 52.292  27.559  61.859  1.00 28.53  ? 201 ASN C OD1 1 
ATOM   8571  N  ND2 . ASN C  1 201 ? 52.786  27.413  59.694  1.00 31.06  ? 201 ASN C ND2 1 
ATOM   8572  N  N   . HIS C  1 202 ? 53.017  24.121  62.186  1.00 17.76  ? 202 HIS C N   1 
ATOM   8573  C  CA  . HIS C  1 202 ? 54.007  23.079  62.038  1.00 16.91  ? 202 HIS C CA  1 
ATOM   8574  C  C   . HIS C  1 202 ? 53.574  21.780  62.667  1.00 20.18  ? 202 HIS C C   1 
ATOM   8575  O  O   . HIS C  1 202 ? 54.306  20.791  62.574  1.00 31.71  ? 202 HIS C O   1 
ATOM   8576  C  CB  . HIS C  1 202 ? 55.334  23.508  62.572  1.00 18.50  ? 202 HIS C CB  1 
ATOM   8577  C  CG  . HIS C  1 202 ? 56.073  24.383  61.641  1.00 21.55  ? 202 HIS C CG  1 
ATOM   8578  N  ND1 . HIS C  1 202 ? 56.929  23.896  60.683  1.00 26.33  ? 202 HIS C ND1 1 
ATOM   8579  C  CD2 . HIS C  1 202 ? 56.054  25.722  61.492  1.00 27.82  ? 202 HIS C CD2 1 
ATOM   8580  C  CE1 . HIS C  1 202 ? 57.402  24.904  59.973  1.00 30.51  ? 202 HIS C CE1 1 
ATOM   8581  N  NE2 . HIS C  1 202 ? 56.889  26.024  60.445  1.00 33.60  ? 202 HIS C NE2 1 
ATOM   8582  N  N   . GLU C  1 203 ? 52.438  21.799  63.364  1.00 14.70  ? 203 GLU C N   1 
ATOM   8583  C  CA  . GLU C  1 203 ? 51.848  20.613  63.954  1.00 12.50  ? 203 GLU C CA  1 
ATOM   8584  C  C   . GLU C  1 203 ? 50.804  19.924  63.032  1.00 16.95  ? 203 GLU C C   1 
ATOM   8585  O  O   . GLU C  1 203 ? 50.494  18.776  63.227  1.00 27.65  ? 203 GLU C O   1 
ATOM   8586  C  CB  . GLU C  1 203 ? 51.166  20.950  65.268  1.00 6.36   ? 203 GLU C CB  1 
ATOM   8587  C  CG  . GLU C  1 203 ? 52.095  20.995  66.382  1.00 13.35  ? 203 GLU C CG  1 
ATOM   8588  C  CD  . GLU C  1 203 ? 53.059  22.128  66.257  1.00 20.39  ? 203 GLU C CD  1 
ATOM   8589  O  OE1 . GLU C  1 203 ? 52.608  23.236  66.552  1.00 21.88  ? 203 GLU C OE1 1 
ATOM   8590  O  OE2 . GLU C  1 203 ? 54.246  21.931  65.894  1.00 29.78  ? 203 GLU C OE2 1 
ATOM   8591  N  N   . ILE C  1 204 ? 50.225  20.622  62.068  1.00 15.41  ? 204 ILE C N   1 
ATOM   8592  C  CA  . ILE C  1 204 ? 49.247  20.036  61.207  1.00 11.75  ? 204 ILE C CA  1 
ATOM   8593  C  C   . ILE C  1 204 ? 49.783  18.840  60.505  1.00 17.48  ? 204 ILE C C   1 
ATOM   8594  O  O   . ILE C  1 204 ? 49.095  17.837  60.418  1.00 22.28  ? 204 ILE C O   1 
ATOM   8595  C  CB  . ILE C  1 204 ? 48.858  20.972  60.141  1.00 13.48  ? 204 ILE C CB  1 
ATOM   8596  C  CG1 . ILE C  1 204 ? 48.283  22.219  60.763  1.00 15.11  ? 204 ILE C CG1 1 
ATOM   8597  C  CG2 . ILE C  1 204 ? 47.792  20.366  59.250  1.00 10.77  ? 204 ILE C CG2 1 
ATOM   8598  C  CD1 . ILE C  1 204 ? 47.982  23.254  59.699  1.00 19.47  ? 204 ILE C CD1 1 
ATOM   8599  N  N   . GLU C  1 205 ? 50.950  18.975  59.892  1.00 19.67  ? 205 GLU C N   1 
ATOM   8600  C  CA  . GLU C  1 205 ? 51.567  17.839  59.196  1.00 20.20  ? 205 GLU C CA  1 
ATOM   8601  C  C   . GLU C  1 205 ? 50.735  17.100  58.205  1.00 19.72  ? 205 GLU C C   1 
ATOM   8602  O  O   . GLU C  1 205 ? 50.656  15.889  58.257  1.00 28.22  ? 205 GLU C O   1 
ATOM   8603  C  CB  . GLU C  1 205 ? 52.148  16.841  60.178  1.00 14.16  ? 205 GLU C CB  1 
ATOM   8604  C  CG  . GLU C  1 205 ? 53.284  17.474  60.928  1.00 32.03  ? 205 GLU C CG  1 
ATOM   8605  C  CD  . GLU C  1 205 ? 54.166  16.547  61.765  1.00 34.54  ? 205 GLU C CD  1 
ATOM   8606  O  OE1 . GLU C  1 205 ? 55.123  15.956  61.196  1.00 27.97  ? 205 GLU C OE1 1 
ATOM   8607  O  OE2 . GLU C  1 205 ? 53.949  16.502  63.009  1.00 39.77  ? 205 GLU C OE2 1 
ATOM   8608  N  N   . PHE C  1 206 ? 50.084  17.830  57.324  1.00 22.33  ? 206 PHE C N   1 
ATOM   8609  C  CA  . PHE C  1 206 ? 49.279  17.244  56.270  1.00 21.26  ? 206 PHE C CA  1 
ATOM   8610  C  C   . PHE C  1 206 ? 50.238  16.874  55.124  1.00 23.67  ? 206 PHE C C   1 
ATOM   8611  O  O   . PHE C  1 206 ? 50.730  17.746  54.414  1.00 28.40  ? 206 PHE C O   1 
ATOM   8612  C  CB  . PHE C  1 206 ? 48.304  18.302  55.796  1.00 21.55  ? 206 PHE C CB  1 
ATOM   8613  C  CG  . PHE C  1 206 ? 47.409  17.859  54.682  1.00 20.79  ? 206 PHE C CG  1 
ATOM   8614  C  CD1 . PHE C  1 206 ? 46.438  16.902  54.894  1.00 24.11  ? 206 PHE C CD1 1 
ATOM   8615  C  CD2 . PHE C  1 206 ? 47.464  18.473  53.462  1.00 16.54  ? 206 PHE C CD2 1 
ATOM   8616  C  CE1 . PHE C  1 206 ? 45.530  16.569  53.909  1.00 23.17  ? 206 PHE C CE1 1 
ATOM   8617  C  CE2 . PHE C  1 206 ? 46.574  18.155  52.483  1.00 15.49  ? 206 PHE C CE2 1 
ATOM   8618  C  CZ  . PHE C  1 206 ? 45.601  17.196  52.706  1.00 23.03  ? 206 PHE C CZ  1 
ATOM   8619  N  N   . ALA C  1 207 ? 50.560  15.594  54.998  1.00 23.98  ? 207 ALA C N   1 
ATOM   8620  C  CA  . ALA C  1 207 ? 51.482  15.115  53.984  1.00 18.77  ? 207 ALA C CA  1 
ATOM   8621  C  C   . ALA C  1 207 ? 50.910  14.077  53.073  1.00 19.84  ? 207 ALA C C   1 
ATOM   8622  O  O   . ALA C  1 207 ? 51.265  12.919  53.148  1.00 16.23  ? 207 ALA C O   1 
ATOM   8623  C  CB  . ALA C  1 207 ? 52.685  14.542  54.643  1.00 21.22  ? 207 ALA C CB  1 
ATOM   8624  N  N   . PRO C  1 208 ? 50.056  14.482  52.166  1.00 19.97  ? 208 PRO C N   1 
ATOM   8625  C  CA  . PRO C  1 208 ? 49.431  13.593  51.212  1.00 23.17  ? 208 PRO C CA  1 
ATOM   8626  C  C   . PRO C  1 208 ? 50.465  12.777  50.454  1.00 29.03  ? 208 PRO C C   1 
ATOM   8627  O  O   . PRO C  1 208 ? 50.254  11.601  50.162  1.00 33.17  ? 208 PRO C O   1 
ATOM   8628  C  CB  . PRO C  1 208 ? 48.783  14.573  50.258  1.00 22.56  ? 208 PRO C CB  1 
ATOM   8629  C  CG  . PRO C  1 208 ? 48.301  15.595  51.151  1.00 23.41  ? 208 PRO C CG  1 
ATOM   8630  C  CD  . PRO C  1 208 ? 49.498  15.828  52.054  1.00 25.16  ? 208 PRO C CD  1 
ATOM   8631  N  N   . GLU C  1 209 ? 51.563  13.415  50.101  1.00 29.93  ? 209 GLU C N   1 
ATOM   8632  C  CA  . GLU C  1 209 ? 52.615  12.735  49.351  1.00 38.18  ? 209 GLU C CA  1 
ATOM   8633  C  C   . GLU C  1 209 ? 53.118  11.440  49.960  1.00 38.98  ? 209 GLU C C   1 
ATOM   8634  O  O   . GLU C  1 209 ? 53.565  10.547  49.246  1.00 49.25  ? 209 GLU C O   1 
ATOM   8635  C  CB  . GLU C  1 209 ? 53.830  13.641  49.163  1.00 43.77  ? 209 GLU C CB  1 
ATOM   8636  C  CG  . GLU C  1 209 ? 53.600  15.109  49.451  1.00 53.51  ? 209 GLU C CG  1 
ATOM   8637  C  CD  . GLU C  1 209 ? 53.631  15.436  50.918  1.00 57.45  ? 209 GLU C CD  1 
ATOM   8638  O  OE1 . GLU C  1 209 ? 54.696  15.239  51.571  1.00 55.93  ? 209 GLU C OE1 1 
ATOM   8639  O  OE2 . GLU C  1 209 ? 52.580  15.914  51.394  1.00 64.46  ? 209 GLU C OE2 1 
ATOM   8640  N  N   . ILE C  1 210 ? 53.162  11.378  51.282  1.00 37.47  ? 210 ILE C N   1 
ATOM   8641  C  CA  . ILE C  1 210 ? 53.651  10.180  51.942  1.00 32.58  ? 210 ILE C CA  1 
ATOM   8642  C  C   . ILE C  1 210 ? 52.485  9.506   52.584  1.00 36.33  ? 210 ILE C C   1 
ATOM   8643  O  O   . ILE C  1 210 ? 52.635  8.765   53.547  1.00 43.57  ? 210 ILE C O   1 
ATOM   8644  C  CB  . ILE C  1 210 ? 54.701  10.473  52.989  1.00 25.91  ? 210 ILE C CB  1 
ATOM   8645  C  CG1 . ILE C  1 210 ? 54.261  11.603  53.900  1.00 24.68  ? 210 ILE C CG1 1 
ATOM   8646  C  CG2 . ILE C  1 210 ? 55.952  10.796  52.314  1.00 29.23  ? 210 ILE C CG2 1 
ATOM   8647  C  CD1 . ILE C  1 210 ? 55.245  11.926  54.968  1.00 24.52  ? 210 ILE C CD1 1 
ATOM   8648  N  N   . ASN C  1 211 ? 51.306  9.839   52.080  1.00 32.52  ? 211 ASN C N   1 
ATOM   8649  C  CA  . ASN C  1 211 ? 50.086  9.266   52.552  1.00 31.20  ? 211 ASN C CA  1 
ATOM   8650  C  C   . ASN C  1 211 ? 49.716  9.458   53.967  1.00 29.58  ? 211 ASN C C   1 
ATOM   8651  O  O   . ASN C  1 211 ? 48.957  8.687   54.493  1.00 33.20  ? 211 ASN C O   1 
ATOM   8652  C  CB  . ASN C  1 211 ? 50.065  7.820   52.209  1.00 44.61  ? 211 ASN C CB  1 
ATOM   8653  C  CG  . ASN C  1 211 ? 49.727  7.614   50.784  1.00 68.55  ? 211 ASN C CG  1 
ATOM   8654  O  OD1 . ASN C  1 211 ? 48.535  7.675   50.459  1.00 78.53  ? 211 ASN C OD1 1 
ATOM   8655  N  ND2 . ASN C  1 211 ? 50.758  7.516   49.926  1.00 84.96  ? 211 ASN C ND2 1 
ATOM   8656  N  N   . GLU C  1 212 ? 50.225  10.504  54.583  1.00 29.98  ? 212 GLU C N   1 
ATOM   8657  C  CA  . GLU C  1 212 ? 49.902  10.844  55.951  1.00 26.34  ? 212 GLU C CA  1 
ATOM   8658  C  C   . GLU C  1 212 ? 49.005  12.016  55.785  1.00 29.47  ? 212 GLU C C   1 
ATOM   8659  O  O   . GLU C  1 212 ? 49.492  13.070  55.393  1.00 29.06  ? 212 GLU C O   1 
ATOM   8660  C  CB  . GLU C  1 212 ? 51.152  11.279  56.668  1.00 22.95  ? 212 GLU C CB  1 
ATOM   8661  C  CG  . GLU C  1 212 ? 51.952  10.112  57.062  1.00 24.67  ? 212 GLU C CG  1 
ATOM   8662  C  CD  . GLU C  1 212 ? 51.120  9.155   57.892  1.00 30.57  ? 212 GLU C CD  1 
ATOM   8663  O  OE1 . GLU C  1 212 ? 50.370  9.613   58.801  1.00 25.31  ? 212 GLU C OE1 1 
ATOM   8664  O  OE2 . GLU C  1 212 ? 51.173  7.942   57.601  1.00 29.76  ? 212 GLU C OE2 1 
ATOM   8665  N  N   . THR C  1 213 ? 47.701  11.833  56.017  1.00 33.01  ? 213 THR C N   1 
ATOM   8666  C  CA  . THR C  1 213 ? 46.705  12.905  55.825  1.00 32.47  ? 213 THR C CA  1 
ATOM   8667  C  C   . THR C  1 213 ? 45.764  13.231  56.967  1.00 34.22  ? 213 THR C C   1 
ATOM   8668  O  O   . THR C  1 213 ? 44.718  13.851  56.750  1.00 35.36  ? 213 THR C O   1 
ATOM   8669  C  CB  . THR C  1 213 ? 45.823  12.635  54.603  1.00 35.20  ? 213 THR C CB  1 
ATOM   8670  O  OG1 . THR C  1 213 ? 45.049  11.441  54.828  1.00 44.66  ? 213 THR C OG1 1 
ATOM   8671  C  CG2 . THR C  1 213 ? 46.685  12.481  53.342  1.00 43.85  ? 213 THR C CG2 1 
ATOM   8672  N  N   . GLU C  1 214 ? 46.134  12.815  58.169  1.00 36.77  ? 214 GLU C N   1 
ATOM   8673  C  CA  . GLU C  1 214 ? 45.316  13.096  59.324  1.00 40.73  ? 214 GLU C CA  1 
ATOM   8674  C  C   . GLU C  1 214 ? 46.079  14.208  60.046  1.00 35.87  ? 214 GLU C C   1 
ATOM   8675  O  O   . GLU C  1 214 ? 47.202  14.011  60.541  1.00 41.93  ? 214 GLU C O   1 
ATOM   8676  C  CB  . GLU C  1 214 ? 45.171  11.833  60.190  1.00 53.66  ? 214 GLU C CB  1 
ATOM   8677  C  CG  . GLU C  1 214 ? 44.137  11.898  61.346  1.00 72.36  ? 214 GLU C CG  1 
ATOM   8678  C  CD  . GLU C  1 214 ? 44.486  10.959  62.537  1.00 83.65  ? 214 GLU C CD  1 
ATOM   8679  O  OE1 . GLU C  1 214 ? 44.814  9.761   62.283  1.00 88.98  ? 214 GLU C OE1 1 
ATOM   8680  O  OE2 . GLU C  1 214 ? 44.431  11.431  63.717  1.00 90.45  ? 214 GLU C OE2 1 
ATOM   8681  N  N   . PRO C  1 215 ? 45.526  15.420  60.015  1.00 28.77  ? 215 PRO C N   1 
ATOM   8682  C  CA  . PRO C  1 215 ? 46.095  16.601  60.641  1.00 26.13  ? 215 PRO C CA  1 
ATOM   8683  C  C   . PRO C  1 215 ? 46.383  16.375  62.075  1.00 25.18  ? 215 PRO C C   1 
ATOM   8684  O  O   . PRO C  1 215 ? 45.657  15.683  62.763  1.00 28.28  ? 215 PRO C O   1 
ATOM   8685  C  CB  . PRO C  1 215 ? 44.974  17.609  60.531  1.00 25.94  ? 215 PRO C CB  1 
ATOM   8686  C  CG  . PRO C  1 215 ? 44.350  17.253  59.235  1.00 26.22  ? 215 PRO C CG  1 
ATOM   8687  C  CD  . PRO C  1 215 ? 44.277  15.760  59.324  1.00 28.41  ? 215 PRO C CD  1 
ATOM   8688  N  N   . PHE C  1 216 ? 47.477  16.962  62.511  1.00 24.60  ? 216 PHE C N   1 
ATOM   8689  C  CA  . PHE C  1 216 ? 47.887  16.915  63.890  1.00 24.35  ? 216 PHE C CA  1 
ATOM   8690  C  C   . PHE C  1 216 ? 48.197  15.529  64.448  1.00 25.37  ? 216 PHE C C   1 
ATOM   8691  O  O   . PHE C  1 216 ? 48.314  15.362  65.679  1.00 26.94  ? 216 PHE C O   1 
ATOM   8692  C  CB  . PHE C  1 216 ? 46.836  17.617  64.774  1.00 23.77  ? 216 PHE C CB  1 
ATOM   8693  C  CG  . PHE C  1 216 ? 46.534  19.041  64.373  1.00 20.10  ? 216 PHE C CG  1 
ATOM   8694  C  CD1 . PHE C  1 216 ? 47.451  20.051  64.633  1.00 18.65  ? 216 PHE C CD1 1 
ATOM   8695  C  CD2 . PHE C  1 216 ? 45.344  19.357  63.708  1.00 12.45  ? 216 PHE C CD2 1 
ATOM   8696  C  CE1 . PHE C  1 216 ? 47.192  21.335  64.237  1.00 20.24  ? 216 PHE C CE1 1 
ATOM   8697  C  CE2 . PHE C  1 216 ? 45.084  20.650  63.313  1.00 10.27  ? 216 PHE C CE2 1 
ATOM   8698  C  CZ  . PHE C  1 216 ? 46.005  21.643  63.572  1.00 8.39   ? 216 PHE C CZ  1 
ATOM   8699  N  N   . LYS C  1 217 ? 48.493  14.563  63.580  1.00 22.47  ? 217 LYS C N   1 
ATOM   8700  C  CA  . LYS C  1 217 ? 48.755  13.218  64.100  1.00 21.18  ? 217 LYS C CA  1 
ATOM   8701  C  C   . LYS C  1 217 ? 49.881  13.032  65.115  1.00 15.62  ? 217 LYS C C   1 
ATOM   8702  O  O   . LYS C  1 217 ? 49.644  12.804  66.299  1.00 21.57  ? 217 LYS C O   1 
ATOM   8703  C  CB  . LYS C  1 217 ? 48.905  12.234  62.982  1.00 18.25  ? 217 LYS C CB  1 
ATOM   8704  C  CG  . LYS C  1 217 ? 49.017  10.877  63.538  1.00 13.39  ? 217 LYS C CG  1 
ATOM   8705  C  CD  . LYS C  1 217 ? 48.709  9.880   62.459  1.00 12.65  ? 217 LYS C CD  1 
ATOM   8706  C  CE  . LYS C  1 217 ? 49.902  9.041   62.113  1.00 20.15  ? 217 LYS C CE  1 
ATOM   8707  N  NZ  . LYS C  1 217 ? 49.577  8.141   60.951  1.00 29.96  ? 217 LYS C NZ  1 
ATOM   8708  N  N   . PRO C  1 218 ? 51.115  13.231  64.705  1.00 8.62   ? 218 PRO C N   1 
ATOM   8709  C  CA  . PRO C  1 218 ? 52.135  13.015  65.727  1.00 5.89   ? 218 PRO C CA  1 
ATOM   8710  C  C   . PRO C  1 218 ? 51.953  13.876  66.957  1.00 10.38  ? 218 PRO C C   1 
ATOM   8711  O  O   . PRO C  1 218 ? 52.148  13.391  68.072  1.00 14.84  ? 218 PRO C O   1 
ATOM   8712  C  CB  . PRO C  1 218 ? 53.422  13.368  65.008  1.00 3.82   ? 218 PRO C CB  1 
ATOM   8713  C  CG  . PRO C  1 218 ? 53.078  13.096  63.543  1.00 9.75   ? 218 PRO C CG  1 
ATOM   8714  C  CD  . PRO C  1 218 ? 51.696  13.630  63.417  1.00 7.16   ? 218 PRO C CD  1 
ATOM   8715  N  N   . PHE C  1 219 ? 51.521  15.119  66.767  1.00 12.76  ? 219 PHE C N   1 
ATOM   8716  C  CA  . PHE C  1 219 ? 51.379  16.060  67.887  1.00 13.22  ? 219 PHE C CA  1 
ATOM   8717  C  C   . PHE C  1 219 ? 50.382  15.534  68.856  1.00 16.52  ? 219 PHE C C   1 
ATOM   8718  O  O   . PHE C  1 219 ? 50.640  15.407  70.064  1.00 20.06  ? 219 PHE C O   1 
ATOM   8719  C  CB  . PHE C  1 219 ? 50.911  17.433  67.397  1.00 18.01  ? 219 PHE C CB  1 
ATOM   8720  C  CG  . PHE C  1 219 ? 50.522  18.381  68.501  1.00 16.39  ? 219 PHE C CG  1 
ATOM   8721  C  CD1 . PHE C  1 219 ? 51.468  18.838  69.399  1.00 12.19  ? 219 PHE C CD1 1 
ATOM   8722  C  CD2 . PHE C  1 219 ? 49.196  18.812  68.652  1.00 15.48  ? 219 PHE C CD2 1 
ATOM   8723  C  CE1 . PHE C  1 219 ? 51.116  19.700  70.430  1.00 12.13  ? 219 PHE C CE1 1 
ATOM   8724  C  CE2 . PHE C  1 219 ? 48.845  19.676  69.688  1.00 13.65  ? 219 PHE C CE2 1 
ATOM   8725  C  CZ  . PHE C  1 219 ? 49.817  20.117  70.574  1.00 11.96  ? 219 PHE C CZ  1 
ATOM   8726  N  N   . SER C  1 220 ? 49.255  15.139  68.312  1.00 16.57  ? 220 SER C N   1 
ATOM   8727  C  CA  . SER C  1 220 ? 48.214  14.635  69.155  1.00 20.90  ? 220 SER C CA  1 
ATOM   8728  C  C   . SER C  1 220 ? 48.594  13.366  69.889  1.00 24.33  ? 220 SER C C   1 
ATOM   8729  O  O   . SER C  1 220 ? 48.125  13.192  71.005  1.00 29.21  ? 220 SER C O   1 
ATOM   8730  C  CB  . SER C  1 220 ? 46.907  14.463  68.382  1.00 23.75  ? 220 SER C CB  1 
ATOM   8731  O  OG  . SER C  1 220 ? 47.082  13.597  67.284  1.00 37.61  ? 220 SER C OG  1 
ATOM   8732  N  N   . TYR C  1 221 ? 49.398  12.479  69.298  1.00 18.26  ? 221 TYR C N   1 
ATOM   8733  C  CA  . TYR C  1 221 ? 49.769  11.272  70.030  1.00 17.03  ? 221 TYR C CA  1 
ATOM   8734  C  C   . TYR C  1 221 ? 50.647  11.557  71.189  1.00 20.78  ? 221 TYR C C   1 
ATOM   8735  O  O   . TYR C  1 221 ? 50.496  10.984  72.270  1.00 30.98  ? 221 TYR C O   1 
ATOM   8736  C  CB  . TYR C  1 221 ? 50.507  10.293  69.170  1.00 17.35  ? 221 TYR C CB  1 
ATOM   8737  C  CG  . TYR C  1 221 ? 49.576  9.405   68.447  1.00 20.32  ? 221 TYR C CG  1 
ATOM   8738  C  CD1 . TYR C  1 221 ? 49.086  9.751   67.220  1.00 24.39  ? 221 TYR C CD1 1 
ATOM   8739  C  CD2 . TYR C  1 221 ? 49.153  8.228   69.007  1.00 26.87  ? 221 TYR C CD2 1 
ATOM   8740  C  CE1 . TYR C  1 221 ? 48.192  8.947   66.554  1.00 26.35  ? 221 TYR C CE1 1 
ATOM   8741  C  CE2 . TYR C  1 221 ? 48.270  7.412   68.348  1.00 29.85  ? 221 TYR C CE2 1 
ATOM   8742  C  CZ  . TYR C  1 221 ? 47.785  7.773   67.121  1.00 30.19  ? 221 TYR C CZ  1 
ATOM   8743  O  OH  . TYR C  1 221 ? 46.887  6.943   66.455  1.00 41.07  ? 221 TYR C OH  1 
ATOM   8744  N  N   . ARG C  1 222 ? 51.563  12.471  70.970  1.00 21.59  ? 222 ARG C N   1 
ATOM   8745  C  CA  . ARG C  1 222 ? 52.519  12.842  71.986  1.00 21.32  ? 222 ARG C CA  1 
ATOM   8746  C  C   . ARG C  1 222 ? 52.101  13.860  73.045  1.00 22.85  ? 222 ARG C C   1 
ATOM   8747  O  O   . ARG C  1 222 ? 52.520  13.767  74.205  1.00 25.28  ? 222 ARG C O   1 
ATOM   8748  C  CB  . ARG C  1 222 ? 53.747  13.329  71.268  1.00 23.69  ? 222 ARG C CB  1 
ATOM   8749  C  CG  . ARG C  1 222 ? 54.363  12.264  70.441  1.00 18.47  ? 222 ARG C CG  1 
ATOM   8750  C  CD  . ARG C  1 222 ? 55.015  12.854  69.242  1.00 18.43  ? 222 ARG C CD  1 
ATOM   8751  N  NE  . ARG C  1 222 ? 55.864  11.901  68.553  1.00 21.79  ? 222 ARG C NE  1 
ATOM   8752  C  CZ  . ARG C  1 222 ? 57.023  11.453  69.023  1.00 21.38  ? 222 ARG C CZ  1 
ATOM   8753  N  NH1 . ARG C  1 222 ? 57.451  11.872  70.213  1.00 22.18  ? 222 ARG C NH1 1 
ATOM   8754  N  NH2 . ARG C  1 222 ? 57.774  10.640  68.272  1.00 20.63  ? 222 ARG C NH2 1 
ATOM   8755  N  N   . TYR C  1 223 ? 51.288  14.840  72.672  1.00 22.67  ? 223 TYR C N   1 
ATOM   8756  C  CA  . TYR C  1 223 ? 50.893  15.876  73.624  1.00 20.37  ? 223 TYR C CA  1 
ATOM   8757  C  C   . TYR C  1 223 ? 49.417  15.872  73.904  1.00 22.33  ? 223 TYR C C   1 
ATOM   8758  O  O   . TYR C  1 223 ? 48.599  16.140  73.020  1.00 27.86  ? 223 TYR C O   1 
ATOM   8759  C  CB  . TYR C  1 223 ? 51.348  17.199  73.070  1.00 14.24  ? 223 TYR C CB  1 
ATOM   8760  C  CG  . TYR C  1 223 ? 52.847  17.226  72.984  1.00 13.47  ? 223 TYR C CG  1 
ATOM   8761  C  CD1 . TYR C  1 223 ? 53.595  17.425  74.125  1.00 18.29  ? 223 TYR C CD1 1 
ATOM   8762  C  CD2 . TYR C  1 223 ? 53.518  16.975  71.795  1.00 12.02  ? 223 TYR C CD2 1 
ATOM   8763  C  CE1 . TYR C  1 223 ? 54.987  17.375  74.114  1.00 15.33  ? 223 TYR C CE1 1 
ATOM   8764  C  CE2 . TYR C  1 223 ? 54.923  16.920  71.763  1.00 16.53  ? 223 TYR C CE2 1 
ATOM   8765  C  CZ  . TYR C  1 223 ? 55.654  17.120  72.945  1.00 18.43  ? 223 TYR C CZ  1 
ATOM   8766  O  OH  . TYR C  1 223 ? 57.039  17.039  73.028  1.00 16.57  ? 223 TYR C OH  1 
ATOM   8767  N  N   . HIS C  1 224 ? 49.055  15.553  75.141  1.00 21.91  ? 224 HIS C N   1 
ATOM   8768  C  CA  . HIS C  1 224 ? 47.619  15.471  75.477  1.00 21.53  ? 224 HIS C CA  1 
ATOM   8769  C  C   . HIS C  1 224 ? 47.197  16.638  76.296  1.00 19.15  ? 224 HIS C C   1 
ATOM   8770  O  O   . HIS C  1 224 ? 48.030  17.175  77.038  1.00 14.72  ? 224 HIS C O   1 
ATOM   8771  C  CB  . HIS C  1 224 ? 47.307  14.198  76.265  1.00 23.28  ? 224 HIS C CB  1 
ATOM   8772  C  CG  . HIS C  1 224 ? 47.167  12.950  75.426  1.00 28.33  ? 224 HIS C CG  1 
ATOM   8773  N  ND1 . HIS C  1 224 ? 46.412  11.867  75.823  1.00 25.79  ? 224 HIS C ND1 1 
ATOM   8774  C  CD2 . HIS C  1 224 ? 47.651  12.627  74.202  1.00 35.74  ? 224 HIS C CD2 1 
ATOM   8775  C  CE1 . HIS C  1 224 ? 46.428  10.941  74.883  1.00 27.75  ? 224 HIS C CE1 1 
ATOM   8776  N  NE2 . HIS C  1 224 ? 47.173  11.375  73.889  1.00 32.54  ? 224 HIS C NE2 1 
ATOM   8777  N  N   . VAL C  1 225 ? 45.907  16.982  76.238  1.00 17.93  ? 225 VAL C N   1 
ATOM   8778  C  CA  . VAL C  1 225 ? 45.410  18.147  76.995  1.00 18.65  ? 225 VAL C CA  1 
ATOM   8779  C  C   . VAL C  1 225 ? 44.048  17.800  77.588  1.00 21.34  ? 225 VAL C C   1 
ATOM   8780  O  O   . VAL C  1 225 ? 43.335  16.950  77.034  1.00 24.16  ? 225 VAL C O   1 
ATOM   8781  C  CB  . VAL C  1 225 ? 45.248  19.360  76.117  1.00 16.10  ? 225 VAL C CB  1 
ATOM   8782  C  CG1 . VAL C  1 225 ? 46.571  19.855  75.620  1.00 11.74  ? 225 VAL C CG1 1 
ATOM   8783  C  CG2 . VAL C  1 225 ? 44.385  19.005  74.946  1.00 14.12  ? 225 VAL C CG2 1 
ATOM   8784  N  N   . PRO C  1 226 ? 43.667  18.446  78.718  1.00 19.73  ? 226 PRO C N   1 
ATOM   8785  C  CA  . PRO C  1 226 ? 42.391  18.228  79.438  1.00 20.41  ? 226 PRO C CA  1 
ATOM   8786  C  C   . PRO C  1 226 ? 41.231  18.858  78.758  1.00 21.80  ? 226 PRO C C   1 
ATOM   8787  O  O   . PRO C  1 226 ? 40.392  19.532  79.380  1.00 23.06  ? 226 PRO C O   1 
ATOM   8788  C  CB  . PRO C  1 226 ? 42.637  18.923  80.769  1.00 16.96  ? 226 PRO C CB  1 
ATOM   8789  C  CG  . PRO C  1 226 ? 43.547  20.044  80.403  1.00 12.29  ? 226 PRO C CG  1 
ATOM   8790  C  CD  . PRO C  1 226 ? 44.528  19.404  79.445  1.00 15.27  ? 226 PRO C CD  1 
ATOM   8791  N  N   . TYR C  1 227 ? 41.106  18.576  77.485  1.00 21.38  ? 227 TYR C N   1 
ATOM   8792  C  CA  . TYR C  1 227 ? 40.068  19.269  76.793  1.00 25.94  ? 227 TYR C CA  1 
ATOM   8793  C  C   . TYR C  1 227 ? 38.686  18.946  77.233  1.00 28.36  ? 227 TYR C C   1 
ATOM   8794  O  O   . TYR C  1 227 ? 37.820  19.782  77.161  1.00 34.59  ? 227 TYR C O   1 
ATOM   8795  C  CB  . TYR C  1 227 ? 40.224  19.123  75.314  1.00 19.91  ? 227 TYR C CB  1 
ATOM   8796  C  CG  . TYR C  1 227 ? 39.960  17.776  74.864  1.00 22.65  ? 227 TYR C CG  1 
ATOM   8797  C  CD1 . TYR C  1 227 ? 38.689  17.404  74.494  1.00 27.95  ? 227 TYR C CD1 1 
ATOM   8798  C  CD2 . TYR C  1 227 ? 40.986  16.878  74.718  1.00 27.07  ? 227 TYR C CD2 1 
ATOM   8799  C  CE1 . TYR C  1 227 ? 38.452  16.161  73.970  1.00 35.10  ? 227 TYR C CE1 1 
ATOM   8800  C  CE2 . TYR C  1 227 ? 40.775  15.622  74.187  1.00 30.20  ? 227 TYR C CE2 1 
ATOM   8801  C  CZ  . TYR C  1 227 ? 39.509  15.266  73.812  1.00 34.88  ? 227 TYR C CZ  1 
ATOM   8802  O  OH  . TYR C  1 227 ? 39.309  14.022  73.248  1.00 33.56  ? 227 TYR C OH  1 
ATOM   8803  N  N   . GLU C  1 228 ? 38.463  17.754  77.727  1.00 32.78  ? 228 GLU C N   1 
ATOM   8804  C  CA  . GLU C  1 228 ? 37.098  17.440  78.129  1.00 38.85  ? 228 GLU C CA  1 
ATOM   8805  C  C   . GLU C  1 228 ? 36.741  18.127  79.431  1.00 36.48  ? 228 GLU C C   1 
ATOM   8806  O  O   . GLU C  1 228 ? 35.566  18.180  79.788  1.00 30.60  ? 228 GLU C O   1 
ATOM   8807  C  CB  . GLU C  1 228 ? 36.797  15.920  78.205  1.00 50.43  ? 228 GLU C CB  1 
ATOM   8808  C  CG  . GLU C  1 228 ? 37.898  14.944  77.700  1.00 72.28  ? 228 GLU C CG  1 
ATOM   8809  C  CD  . GLU C  1 228 ? 39.292  15.115  78.419  1.00 88.47  ? 228 GLU C CD  1 
ATOM   8810  O  OE1 . GLU C  1 228 ? 39.378  15.636  79.583  1.00 91.90  ? 228 GLU C OE1 1 
ATOM   8811  O  OE2 . GLU C  1 228 ? 40.319  14.739  77.786  1.00 96.74  ? 228 GLU C OE2 1 
ATOM   8812  N  N   . ALA C  1 229 ? 37.738  18.691  80.119  1.00 39.03  ? 229 ALA C N   1 
ATOM   8813  C  CA  . ALA C  1 229 ? 37.491  19.386  81.391  1.00 40.47  ? 229 ALA C CA  1 
ATOM   8814  C  C   . ALA C  1 229 ? 36.619  20.617  81.127  1.00 41.71  ? 229 ALA C C   1 
ATOM   8815  O  O   . ALA C  1 229 ? 35.771  20.940  81.943  1.00 41.40  ? 229 ALA C O   1 
ATOM   8816  C  CB  . ALA C  1 229 ? 38.783  19.765  82.066  1.00 45.71  ? 229 ALA C CB  1 
ATOM   8817  N  N   . SER C  1 230 ? 36.952  21.375  80.073  1.00 44.95  ? 230 SER C N   1 
ATOM   8818  C  CA  . SER C  1 230 ? 36.135  22.501  79.568  1.00 42.29  ? 230 SER C CA  1 
ATOM   8819  C  C   . SER C  1 230 ? 35.190  21.567  78.866  1.00 42.27  ? 230 SER C C   1 
ATOM   8820  O  O   . SER C  1 230 ? 35.451  20.372  78.811  1.00 48.22  ? 230 SER C O   1 
ATOM   8821  C  CB  . SER C  1 230 ? 36.868  23.260  78.457  1.00 42.94  ? 230 SER C CB  1 
ATOM   8822  O  OG  . SER C  1 230 ? 38.271  22.985  78.482  1.00 50.18  ? 230 SER C OG  1 
ATOM   8823  N  N   . GLN C  1 231 ? 34.114  21.981  78.267  1.00 37.98  ? 231 GLN C N   1 
ATOM   8824  C  CA  . GLN C  1 231 ? 33.398  20.850  77.687  1.00 39.00  ? 231 GLN C CA  1 
ATOM   8825  C  C   . GLN C  1 231 ? 33.681  20.683  76.210  1.00 33.67  ? 231 GLN C C   1 
ATOM   8826  O  O   . GLN C  1 231 ? 32.782  20.446  75.408  1.00 32.31  ? 231 GLN C O   1 
ATOM   8827  C  CB  . GLN C  1 231 ? 31.913  20.863  78.055  1.00 51.47  ? 231 GLN C CB  1 
ATOM   8828  C  CG  . GLN C  1 231 ? 31.610  20.559  79.546  1.00 65.39  ? 231 GLN C CG  1 
ATOM   8829  C  CD  . GLN C  1 231 ? 32.249  21.564  80.534  1.00 79.44  ? 231 GLN C CD  1 
ATOM   8830  O  OE1 . GLN C  1 231 ? 32.483  22.746  80.202  1.00 87.30  ? 231 GLN C OE1 1 
ATOM   8831  N  NE2 . GLN C  1 231 ? 32.528  21.097  81.755  1.00 85.57  ? 231 GLN C NE2 1 
ATOM   8832  N  N   . SER C  1 232 ? 34.964  20.793  75.867  1.00 31.67  ? 232 SER C N   1 
ATOM   8833  C  CA  . SER C  1 232 ? 35.424  20.714  74.479  1.00 27.79  ? 232 SER C CA  1 
ATOM   8834  C  C   . SER C  1 232 ? 35.325  19.321  73.930  1.00 29.23  ? 232 SER C C   1 
ATOM   8835  O  O   . SER C  1 232 ? 35.330  18.356  74.674  1.00 32.50  ? 232 SER C O   1 
ATOM   8836  C  CB  . SER C  1 232 ? 36.865  21.204  74.337  1.00 26.17  ? 232 SER C CB  1 
ATOM   8837  O  OG  . SER C  1 232 ? 37.273  21.133  72.995  1.00 11.99  ? 232 SER C OG  1 
ATOM   8838  N  N   . THR C  1 233 ? 35.249  19.228  72.612  1.00 27.51  ? 233 THR C N   1 
ATOM   8839  C  CA  . THR C  1 233 ? 35.144  17.940  71.977  1.00 26.08  ? 233 THR C CA  1 
ATOM   8840  C  C   . THR C  1 233 ? 36.367  17.672  71.140  1.00 27.98  ? 233 THR C C   1 
ATOM   8841  O  O   . THR C  1 233 ? 36.348  16.786  70.267  1.00 27.09  ? 233 THR C O   1 
ATOM   8842  C  CB  . THR C  1 233 ? 33.881  17.838  71.072  1.00 27.33  ? 233 THR C CB  1 
ATOM   8843  O  OG1 . THR C  1 233 ? 33.908  18.800  69.991  1.00 25.88  ? 233 THR C OG1 1 
ATOM   8844  C  CG2 . THR C  1 233 ? 32.690  18.069  71.872  1.00 25.96  ? 233 THR C CG2 1 
ATOM   8845  N  N   . SER C  1 234 ? 37.398  18.488  71.340  1.00 22.12  ? 234 SER C N   1 
ATOM   8846  C  CA  . SER C  1 234 ? 38.621  18.323  70.594  1.00 18.30  ? 234 SER C CA  1 
ATOM   8847  C  C   . SER C  1 234 ? 39.754  18.881  71.376  1.00 18.13  ? 234 SER C C   1 
ATOM   8848  O  O   . SER C  1 234 ? 39.603  19.862  72.052  1.00 23.89  ? 234 SER C O   1 
ATOM   8849  C  CB  . SER C  1 234 ? 38.530  19.017  69.282  1.00 19.08  ? 234 SER C CB  1 
ATOM   8850  O  OG  . SER C  1 234 ? 39.821  19.091  68.743  1.00 30.08  ? 234 SER C OG  1 
ATOM   8851  N  N   . PRO C  1 235 ? 40.913  18.252  71.311  1.00 20.90  ? 235 PRO C N   1 
ATOM   8852  C  CA  . PRO C  1 235 ? 42.078  18.735  72.066  1.00 20.20  ? 235 PRO C CA  1 
ATOM   8853  C  C   . PRO C  1 235 ? 42.679  19.978  71.508  1.00 21.11  ? 235 PRO C C   1 
ATOM   8854  O  O   . PRO C  1 235 ? 43.661  20.465  72.044  1.00 24.44  ? 235 PRO C O   1 
ATOM   8855  C  CB  . PRO C  1 235 ? 43.075  17.592  71.935  1.00 23.84  ? 235 PRO C CB  1 
ATOM   8856  C  CG  . PRO C  1 235 ? 42.703  16.990  70.608  1.00 24.73  ? 235 PRO C CG  1 
ATOM   8857  C  CD  . PRO C  1 235 ? 41.201  16.983  70.631  1.00 15.30  ? 235 PRO C CD  1 
ATOM   8858  N  N   . PHE C  1 236 ? 42.118  20.485  70.418  1.00 22.16  ? 236 PHE C N   1 
ATOM   8859  C  CA  . PHE C  1 236 ? 42.708  21.665  69.822  1.00 22.03  ? 236 PHE C CA  1 
ATOM   8860  C  C   . PHE C  1 236 ? 42.286  22.985  70.326  1.00 22.98  ? 236 PHE C C   1 
ATOM   8861  O  O   . PHE C  1 236 ? 42.831  24.009  69.889  1.00 25.15  ? 236 PHE C O   1 
ATOM   8862  C  CB  . PHE C  1 236 ? 42.594  21.596  68.332  1.00 20.25  ? 236 PHE C CB  1 
ATOM   8863  C  CG  . PHE C  1 236 ? 43.260  20.426  67.799  1.00 18.71  ? 236 PHE C CG  1 
ATOM   8864  C  CD1 . PHE C  1 236 ? 44.474  20.062  68.304  1.00 19.73  ? 236 PHE C CD1 1 
ATOM   8865  C  CD2 . PHE C  1 236 ? 42.634  19.596  66.879  1.00 25.47  ? 236 PHE C CD2 1 
ATOM   8866  C  CE1 . PHE C  1 236 ? 45.058  18.867  67.909  1.00 28.77  ? 236 PHE C CE1 1 
ATOM   8867  C  CE2 . PHE C  1 236 ? 43.212  18.394  66.468  1.00 24.78  ? 236 PHE C CE2 1 
ATOM   8868  C  CZ  . PHE C  1 236 ? 44.418  18.030  66.987  1.00 25.90  ? 236 PHE C CZ  1 
ATOM   8869  N  N   . TRP C  1 237 ? 41.247  22.978  71.145  1.00 22.43  ? 237 TRP C N   1 
ATOM   8870  C  CA  . TRP C  1 237 ? 40.730  24.187  71.784  1.00 18.08  ? 237 TRP C CA  1 
ATOM   8871  C  C   . TRP C  1 237 ? 40.130  23.767  73.101  1.00 18.93  ? 237 TRP C C   1 
ATOM   8872  O  O   . TRP C  1 237 ? 39.393  22.766  73.200  1.00 17.01  ? 237 TRP C O   1 
ATOM   8873  C  CB  . TRP C  1 237 ? 39.712  24.865  70.941  1.00 10.46  ? 237 TRP C CB  1 
ATOM   8874  C  CG  . TRP C  1 237 ? 38.580  24.016  70.611  1.00 15.27  ? 237 TRP C CG  1 
ATOM   8875  C  CD1 . TRP C  1 237 ? 37.423  23.870  71.328  1.00 19.66  ? 237 TRP C CD1 1 
ATOM   8876  C  CD2 . TRP C  1 237 ? 38.380  23.307  69.394  1.00 16.35  ? 237 TRP C CD2 1 
ATOM   8877  N  NE1 . TRP C  1 237 ? 36.498  23.119  70.607  1.00 23.69  ? 237 TRP C NE1 1 
ATOM   8878  C  CE2 . TRP C  1 237 ? 37.070  22.764  69.415  1.00 16.25  ? 237 TRP C CE2 1 
ATOM   8879  C  CE3 . TRP C  1 237 ? 39.187  23.068  68.271  1.00 19.68  ? 237 TRP C CE3 1 
ATOM   8880  C  CZ2 . TRP C  1 237 ? 36.554  22.021  68.377  1.00 15.39  ? 237 TRP C CZ2 1 
ATOM   8881  C  CZ3 . TRP C  1 237 ? 38.670  22.311  67.211  1.00 15.57  ? 237 TRP C CZ3 1 
ATOM   8882  C  CH2 . TRP C  1 237 ? 37.373  21.794  67.277  1.00 16.09  ? 237 TRP C CH2 1 
ATOM   8883  N  N   . TYR C  1 238 ? 40.498  24.494  74.133  1.00 14.22  ? 238 TYR C N   1 
ATOM   8884  C  CA  . TYR C  1 238 ? 40.028  24.147  75.430  1.00 18.75  ? 238 TYR C CA  1 
ATOM   8885  C  C   . TYR C  1 238 ? 40.420  25.297  76.345  1.00 24.28  ? 238 TYR C C   1 
ATOM   8886  O  O   . TYR C  1 238 ? 40.947  26.296  75.857  1.00 31.03  ? 238 TYR C O   1 
ATOM   8887  C  CB  . TYR C  1 238 ? 40.748  22.851  75.840  1.00 21.92  ? 238 TYR C CB  1 
ATOM   8888  C  CG  . TYR C  1 238 ? 42.271  22.944  75.900  1.00 16.84  ? 238 TYR C CG  1 
ATOM   8889  C  CD1 . TYR C  1 238 ? 43.060  22.762  74.758  1.00 18.87  ? 238 TYR C CD1 1 
ATOM   8890  C  CD2 . TYR C  1 238 ? 42.955  23.255  77.108  1.00 16.02  ? 238 TYR C CD2 1 
ATOM   8891  C  CE1 . TYR C  1 238 ? 44.478  22.900  74.801  1.00 14.63  ? 238 TYR C CE1 1 
ATOM   8892  C  CE2 . TYR C  1 238 ? 44.387  23.383  77.165  1.00 11.29  ? 238 TYR C CE2 1 
ATOM   8893  C  CZ  . TYR C  1 238 ? 45.111  23.216  75.999  1.00 15.63  ? 238 TYR C CZ  1 
ATOM   8894  O  OH  . TYR C  1 238 ? 46.459  23.414  76.036  1.00 24.88  ? 238 TYR C OH  1 
ATOM   8895  N  N   . SER C  1 239 ? 40.160  25.177  77.646  1.00 24.37  ? 239 SER C N   1 
ATOM   8896  C  CA  . SER C  1 239 ? 40.550  26.200  78.602  1.00 23.32  ? 239 SER C CA  1 
ATOM   8897  C  C   . SER C  1 239 ? 40.868  25.568  79.925  1.00 25.19  ? 239 SER C C   1 
ATOM   8898  O  O   . SER C  1 239 ? 40.447  24.422  80.195  1.00 30.81  ? 239 SER C O   1 
ATOM   8899  C  CB  . SER C  1 239 ? 39.446  27.147  78.861  1.00 21.16  ? 239 SER C CB  1 
ATOM   8900  O  OG  . SER C  1 239 ? 38.400  26.441  79.465  1.00 27.82  ? 239 SER C OG  1 
ATOM   8901  N  N   . ILE C  1 240 ? 41.589  26.312  80.753  1.00 21.09  ? 240 ILE C N   1 
ATOM   8902  C  CA  . ILE C  1 240 ? 41.955  25.817  82.071  1.00 21.99  ? 240 ILE C CA  1 
ATOM   8903  C  C   . ILE C  1 240 ? 41.980  27.005  82.946  1.00 21.84  ? 240 ILE C C   1 
ATOM   8904  O  O   . ILE C  1 240 ? 42.147  28.107  82.456  1.00 27.48  ? 240 ILE C O   1 
ATOM   8905  C  CB  . ILE C  1 240 ? 43.380  25.218  82.121  1.00 20.99  ? 240 ILE C CB  1 
ATOM   8906  C  CG1 . ILE C  1 240 ? 44.411  26.228  81.708  1.00 23.80  ? 240 ILE C CG1 1 
ATOM   8907  C  CG2 . ILE C  1 240 ? 43.520  24.076  81.200  1.00 18.94  ? 240 ILE C CG2 1 
ATOM   8908  C  CD1 . ILE C  1 240 ? 45.818  25.775  82.050  1.00 25.85  ? 240 ILE C CD1 1 
ATOM   8909  N  N   . LYS C  1 241 ? 41.763  26.821  84.222  1.00 19.97  ? 241 LYS C N   1 
ATOM   8910  C  CA  . LYS C  1 241 ? 41.841  27.956  85.103  1.00 23.77  ? 241 LYS C CA  1 
ATOM   8911  C  C   . LYS C  1 241 ? 43.050  27.630  85.936  1.00 26.71  ? 241 LYS C C   1 
ATOM   8912  O  O   . LYS C  1 241 ? 43.278  26.463  86.224  1.00 29.33  ? 241 LYS C O   1 
ATOM   8913  C  CB  . LYS C  1 241 ? 40.645  28.009  86.021  1.00 22.16  ? 241 LYS C CB  1 
ATOM   8914  C  CG  . LYS C  1 241 ? 39.311  28.217  85.360  1.00 27.16  ? 241 LYS C CG  1 
ATOM   8915  C  CD  . LYS C  1 241 ? 38.276  28.148  86.456  1.00 33.92  ? 241 LYS C CD  1 
ATOM   8916  C  CE  . LYS C  1 241 ? 36.893  28.438  85.959  1.00 41.64  ? 241 LYS C CE  1 
ATOM   8917  N  NZ  . LYS C  1 241 ? 35.952  28.144  87.074  1.00 63.03  ? 241 LYS C NZ  1 
ATOM   8918  N  N   . ARG C  1 242 ? 43.853  28.621  86.289  1.00 24.64  ? 242 ARG C N   1 
ATOM   8919  C  CA  . ARG C  1 242 ? 45.003  28.348  87.115  1.00 28.11  ? 242 ARG C CA  1 
ATOM   8920  C  C   . ARG C  1 242 ? 45.342  29.591  87.895  1.00 31.01  ? 242 ARG C C   1 
ATOM   8921  O  O   . ARG C  1 242 ? 45.597  30.648  87.302  1.00 31.09  ? 242 ARG C O   1 
ATOM   8922  C  CB  . ARG C  1 242 ? 46.190  27.884  86.263  1.00 28.40  ? 242 ARG C CB  1 
ATOM   8923  C  CG  . ARG C  1 242 ? 47.540  27.982  86.969  1.00 33.21  ? 242 ARG C CG  1 
ATOM   8924  C  CD  . ARG C  1 242 ? 48.584  27.177  86.272  1.00 31.74  ? 242 ARG C CD  1 
ATOM   8925  N  NE  . ARG C  1 242 ? 48.346  25.764  86.533  1.00 38.10  ? 242 ARG C NE  1 
ATOM   8926  C  CZ  . ARG C  1 242 ? 49.296  24.888  86.875  1.00 36.74  ? 242 ARG C CZ  1 
ATOM   8927  N  NH1 . ARG C  1 242 ? 50.560  25.261  86.994  1.00 31.83  ? 242 ARG C NH1 1 
ATOM   8928  N  NH2 . ARG C  1 242 ? 48.982  23.628  87.111  1.00 35.00  ? 242 ARG C NH2 1 
ATOM   8929  N  N   . ALA C  1 243 ? 45.374  29.466  89.224  1.00 30.25  ? 243 ALA C N   1 
ATOM   8930  C  CA  . ALA C  1 243 ? 45.672  30.623  90.047  1.00 31.52  ? 243 ALA C CA  1 
ATOM   8931  C  C   . ALA C  1 243 ? 44.570  31.640  89.797  1.00 33.57  ? 243 ALA C C   1 
ATOM   8932  O  O   . ALA C  1 243 ? 43.394  31.299  89.862  1.00 33.00  ? 243 ALA C O   1 
ATOM   8933  C  CB  . ALA C  1 243 ? 47.014  31.211  89.660  1.00 33.24  ? 243 ALA C CB  1 
ATOM   8934  N  N   . SER C  1 244 ? 44.947  32.847  89.394  1.00 33.61  ? 244 SER C N   1 
ATOM   8935  C  CA  . SER C  1 244 ? 43.978  33.895  89.149  1.00 34.89  ? 244 SER C CA  1 
ATOM   8936  C  C   . SER C  1 244 ? 43.616  34.077  87.690  1.00 35.86  ? 244 SER C C   1 
ATOM   8937  O  O   . SER C  1 244 ? 42.830  34.966  87.360  1.00 44.05  ? 244 SER C O   1 
ATOM   8938  C  CB  . SER C  1 244 ? 44.533  35.212  89.703  1.00 40.80  ? 244 SER C CB  1 
ATOM   8939  O  OG  . SER C  1 244 ? 45.879  35.416  89.295  1.00 46.31  ? 244 SER C OG  1 
ATOM   8940  N  N   . ALA C  1 245 ? 44.158  33.242  86.814  1.00 32.58  ? 245 ALA C N   1 
ATOM   8941  C  CA  . ALA C  1 245 ? 43.898  33.394  85.396  1.00 24.32  ? 245 ALA C CA  1 
ATOM   8942  C  C   . ALA C  1 245 ? 42.928  32.399  84.821  1.00 20.48  ? 245 ALA C C   1 
ATOM   8943  O  O   . ALA C  1 245 ? 42.828  31.299  85.331  1.00 24.64  ? 245 ALA C O   1 
ATOM   8944  C  CB  . ALA C  1 245 ? 45.216  33.317  84.626  1.00 22.20  ? 245 ALA C CB  1 
ATOM   8945  N  N   . HIS C  1 246 ? 42.207  32.799  83.779  1.00 17.68  ? 246 HIS C N   1 
ATOM   8946  C  CA  . HIS C  1 246 ? 41.305  31.921  83.043  1.00 22.52  ? 246 HIS C CA  1 
ATOM   8947  C  C   . HIS C  1 246 ? 41.897  31.965  81.620  1.00 26.93  ? 246 HIS C C   1 
ATOM   8948  O  O   . HIS C  1 246 ? 41.803  32.967  80.928  1.00 29.83  ? 246 HIS C O   1 
ATOM   8949  C  CB  . HIS C  1 246 ? 39.880  32.423  83.049  1.00 22.31  ? 246 HIS C CB  1 
ATOM   8950  C  CG  . HIS C  1 246 ? 38.881  31.436  82.509  1.00 27.97  ? 246 HIS C CG  1 
ATOM   8951  N  ND1 . HIS C  1 246 ? 37.788  30.999  83.237  1.00 31.50  ? 246 HIS C ND1 1 
ATOM   8952  C  CD2 . HIS C  1 246 ? 38.779  30.824  81.299  1.00 30.15  ? 246 HIS C CD2 1 
ATOM   8953  C  CE1 . HIS C  1 246 ? 37.062  30.166  82.503  1.00 30.00  ? 246 HIS C CE1 1 
ATOM   8954  N  NE2 . HIS C  1 246 ? 37.639  30.042  81.325  1.00 28.68  ? 246 HIS C NE2 1 
ATOM   8955  N  N   . ILE C  1 247 ? 42.506  30.862  81.201  1.00 27.85  ? 247 ILE C N   1 
ATOM   8956  C  CA  . ILE C  1 247 ? 43.184  30.738  79.923  1.00 22.54  ? 247 ILE C CA  1 
ATOM   8957  C  C   . ILE C  1 247 ? 42.340  29.983  78.945  1.00 20.45  ? 247 ILE C C   1 
ATOM   8958  O  O   . ILE C  1 247 ? 41.768  28.946  79.294  1.00 26.61  ? 247 ILE C O   1 
ATOM   8959  C  CB  . ILE C  1 247 ? 44.473  29.994  80.170  1.00 23.05  ? 247 ILE C CB  1 
ATOM   8960  C  CG1 . ILE C  1 247 ? 45.216  30.720  81.293  1.00 22.77  ? 247 ILE C CG1 1 
ATOM   8961  C  CG2 . ILE C  1 247 ? 45.278  29.904  78.908  1.00 23.57  ? 247 ILE C CG2 1 
ATOM   8962  C  CD1 . ILE C  1 247 ? 46.488  30.142  81.646  1.00 25.47  ? 247 ILE C CD1 1 
ATOM   8963  N  N   . ILE C  1 248 ? 42.254  30.503  77.731  1.00 16.33  ? 248 ILE C N   1 
ATOM   8964  C  CA  . ILE C  1 248 ? 41.459  29.892  76.695  1.00 19.86  ? 248 ILE C CA  1 
ATOM   8965  C  C   . ILE C  1 248 ? 42.419  29.660  75.565  1.00 23.21  ? 248 ILE C C   1 
ATOM   8966  O  O   . ILE C  1 248 ? 43.130  30.594  75.170  1.00 27.13  ? 248 ILE C O   1 
ATOM   8967  C  CB  . ILE C  1 248 ? 40.380  30.879  76.189  1.00 23.61  ? 248 ILE C CB  1 
ATOM   8968  C  CG1 . ILE C  1 248 ? 39.345  31.138  77.281  1.00 18.58  ? 248 ILE C CG1 1 
ATOM   8969  C  CG2 . ILE C  1 248 ? 39.750  30.390  74.889  1.00 17.72  ? 248 ILE C CG2 1 
ATOM   8970  C  CD1 . ILE C  1 248 ? 38.182  31.934  76.798  1.00 21.73  ? 248 ILE C CD1 1 
ATOM   8971  N  N   . VAL C  1 249 ? 42.443  28.441  75.042  1.00 19.76  ? 249 VAL C N   1 
ATOM   8972  C  CA  . VAL C  1 249 ? 43.327  28.106  73.947  1.00 16.62  ? 249 VAL C CA  1 
ATOM   8973  C  C   . VAL C  1 249 ? 42.535  27.832  72.684  1.00 20.43  ? 249 VAL C C   1 
ATOM   8974  O  O   . VAL C  1 249 ? 41.588  27.027  72.725  1.00 20.23  ? 249 VAL C O   1 
ATOM   8975  C  CB  . VAL C  1 249 ? 44.149  26.860  74.258  1.00 14.86  ? 249 VAL C CB  1 
ATOM   8976  C  CG1 . VAL C  1 249 ? 45.143  26.600  73.105  1.00 11.20  ? 249 VAL C CG1 1 
ATOM   8977  C  CG2 . VAL C  1 249 ? 44.870  27.015  75.614  1.00 5.52   ? 249 VAL C CG2 1 
ATOM   8978  N  N   . LEU C  1 250 ? 42.932  28.469  71.575  1.00 18.11  ? 250 LEU C N   1 
ATOM   8979  C  CA  . LEU C  1 250 ? 42.242  28.288  70.282  1.00 22.42  ? 250 LEU C CA  1 
ATOM   8980  C  C   . LEU C  1 250 ? 43.112  27.676  69.208  1.00 26.96  ? 250 LEU C C   1 
ATOM   8981  O  O   . LEU C  1 250 ? 44.348  27.611  69.315  1.00 35.66  ? 250 LEU C O   1 
ATOM   8982  C  CB  . LEU C  1 250 ? 41.660  29.579  69.777  1.00 23.41  ? 250 LEU C CB  1 
ATOM   8983  C  CG  . LEU C  1 250 ? 40.775  30.257  70.817  1.00 31.14  ? 250 LEU C CG  1 
ATOM   8984  C  CD1 . LEU C  1 250 ? 40.333  31.577  70.288  1.00 33.26  ? 250 LEU C CD1 1 
ATOM   8985  C  CD2 . LEU C  1 250 ? 39.590  29.383  71.160  1.00 24.38  ? 250 LEU C CD2 1 
ATOM   8986  N  N   . SER C  1 251 ? 42.473  27.296  68.123  1.00 26.71  ? 251 SER C N   1 
ATOM   8987  C  CA  . SER C  1 251 ? 43.154  26.606  67.054  1.00 26.86  ? 251 SER C CA  1 
ATOM   8988  C  C   . SER C  1 251 ? 43.030  27.336  65.742  1.00 27.50  ? 251 SER C C   1 
ATOM   8989  O  O   . SER C  1 251 ? 42.060  27.188  65.042  1.00 30.51  ? 251 SER C O   1 
ATOM   8990  C  CB  . SER C  1 251 ? 42.558  25.197  66.972  1.00 25.55  ? 251 SER C CB  1 
ATOM   8991  O  OG  . SER C  1 251 ? 43.090  24.418  65.914  1.00 26.27  ? 251 SER C OG  1 
ATOM   8992  N  N   . SER C  1 252 ? 44.031  28.117  65.389  1.00 28.98  ? 252 SER C N   1 
ATOM   8993  C  CA  . SER C  1 252 ? 43.989  28.863  64.144  1.00 27.29  ? 252 SER C CA  1 
ATOM   8994  C  C   . SER C  1 252 ? 43.792  28.009  62.891  1.00 29.97  ? 252 SER C C   1 
ATOM   8995  O  O   . SER C  1 252 ? 43.323  28.508  61.863  1.00 33.62  ? 252 SER C O   1 
ATOM   8996  C  CB  . SER C  1 252 ? 45.301  29.618  63.972  1.00 26.57  ? 252 SER C CB  1 
ATOM   8997  O  OG  . SER C  1 252 ? 45.591  30.528  65.046  1.00 24.74  ? 252 SER C OG  1 
ATOM   8998  N  N   . TYR C  1 253 ? 44.178  26.736  62.975  1.00 28.81  ? 253 TYR C N   1 
ATOM   8999  C  CA  . TYR C  1 253 ? 44.136  25.825  61.844  1.00 21.55  ? 253 TYR C CA  1 
ATOM   9000  C  C   . TYR C  1 253 ? 43.054  24.794  61.892  1.00 21.95  ? 253 TYR C C   1 
ATOM   9001  O  O   . TYR C  1 253 ? 42.987  23.906  61.052  1.00 23.25  ? 253 TYR C O   1 
ATOM   9002  C  CB  . TYR C  1 253 ? 45.516  25.259  61.632  1.00 15.08  ? 253 TYR C CB  1 
ATOM   9003  C  CG  . TYR C  1 253 ? 46.519  26.383  61.477  1.00 18.19  ? 253 TYR C CG  1 
ATOM   9004  C  CD1 . TYR C  1 253 ? 46.532  27.172  60.338  1.00 18.73  ? 253 TYR C CD1 1 
ATOM   9005  C  CD2 . TYR C  1 253 ? 47.396  26.713  62.497  1.00 20.83  ? 253 TYR C CD2 1 
ATOM   9006  C  CE1 . TYR C  1 253 ? 47.388  28.259  60.223  1.00 27.38  ? 253 TYR C CE1 1 
ATOM   9007  C  CE2 . TYR C  1 253 ? 48.277  27.834  62.398  1.00 25.19  ? 253 TYR C CE2 1 
ATOM   9008  C  CZ  . TYR C  1 253 ? 48.256  28.607  61.268  1.00 28.42  ? 253 TYR C CZ  1 
ATOM   9009  O  OH  . TYR C  1 253 ? 48.990  29.797  61.221  1.00 32.05  ? 253 TYR C OH  1 
ATOM   9010  N  N   . SER C  1 254 ? 42.207  24.921  62.901  1.00 22.28  ? 254 SER C N   1 
ATOM   9011  C  CA  . SER C  1 254 ? 41.038  24.079  63.028  1.00 27.86  ? 254 SER C CA  1 
ATOM   9012  C  C   . SER C  1 254 ? 39.997  24.988  62.380  1.00 29.52  ? 254 SER C C   1 
ATOM   9013  O  O   . SER C  1 254 ? 40.372  25.965  61.748  1.00 35.20  ? 254 SER C O   1 
ATOM   9014  C  CB  . SER C  1 254 ? 40.695  23.840  64.502  1.00 30.81  ? 254 SER C CB  1 
ATOM   9015  O  OG  . SER C  1 254 ? 41.084  22.545  64.902  1.00 38.10  ? 254 SER C OG  1 
ATOM   9016  N  N   . ALA C  1 255 ? 38.719  24.650  62.461  1.00 32.91  ? 255 ALA C N   1 
ATOM   9017  C  CA  . ALA C  1 255 ? 37.658  25.493  61.885  1.00 37.93  ? 255 ALA C CA  1 
ATOM   9018  C  C   . ALA C  1 255 ? 36.907  26.366  62.899  1.00 41.59  ? 255 ALA C C   1 
ATOM   9019  O  O   . ALA C  1 255 ? 36.604  25.904  64.022  1.00 48.55  ? 255 ALA C O   1 
ATOM   9020  C  CB  . ALA C  1 255 ? 36.662  24.658  61.134  1.00 38.58  ? 255 ALA C CB  1 
ATOM   9021  N  N   . TYR C  1 256 ? 36.561  27.597  62.482  1.00 43.44  ? 256 TYR C N   1 
ATOM   9022  C  CA  . TYR C  1 256 ? 35.852  28.568  63.333  1.00 39.06  ? 256 TYR C CA  1 
ATOM   9023  C  C   . TYR C  1 256 ? 34.597  29.151  62.703  1.00 37.93  ? 256 TYR C C   1 
ATOM   9024  O  O   . TYR C  1 256 ? 34.029  30.104  63.233  1.00 38.62  ? 256 TYR C O   1 
ATOM   9025  C  CB  . TYR C  1 256 ? 36.781  29.707  63.805  1.00 35.96  ? 256 TYR C CB  1 
ATOM   9026  C  CG  . TYR C  1 256 ? 37.908  30.125  62.840  1.00 34.81  ? 256 TYR C CG  1 
ATOM   9027  C  CD1 . TYR C  1 256 ? 37.668  30.896  61.718  1.00 36.80  ? 256 TYR C CD1 1 
ATOM   9028  C  CD2 . TYR C  1 256 ? 39.206  29.751  63.069  1.00 36.20  ? 256 TYR C CD2 1 
ATOM   9029  C  CE1 . TYR C  1 256 ? 38.696  31.270  60.852  1.00 28.81  ? 256 TYR C CE1 1 
ATOM   9030  C  CE2 . TYR C  1 256 ? 40.223  30.117  62.217  1.00 37.64  ? 256 TYR C CE2 1 
ATOM   9031  C  CZ  . TYR C  1 256 ? 39.968  30.872  61.113  1.00 33.79  ? 256 TYR C CZ  1 
ATOM   9032  O  OH  . TYR C  1 256 ? 41.032  31.182  60.283  1.00 30.41  ? 256 TYR C OH  1 
ATOM   9033  N  N   . GLY C  1 257 ? 34.171  28.593  61.572  1.00 36.81  ? 257 GLY C N   1 
ATOM   9034  C  CA  . GLY C  1 257 ? 32.968  29.082  60.940  1.00 38.22  ? 257 GLY C CA  1 
ATOM   9035  C  C   . GLY C  1 257 ? 31.823  29.119  61.937  1.00 40.08  ? 257 GLY C C   1 
ATOM   9036  O  O   . GLY C  1 257 ? 31.871  28.519  62.994  1.00 45.22  ? 257 GLY C O   1 
ATOM   9037  N  N   . ARG C  1 258 ? 30.750  29.783  61.590  1.00 41.18  ? 258 ARG C N   1 
ATOM   9038  C  CA  . ARG C  1 258 ? 29.634  29.883  62.485  1.00 42.79  ? 258 ARG C CA  1 
ATOM   9039  C  C   . ARG C  1 258 ? 28.939  28.554  62.531  1.00 43.70  ? 258 ARG C C   1 
ATOM   9040  O  O   . ARG C  1 258 ? 28.549  27.993  61.506  1.00 44.99  ? 258 ARG C O   1 
ATOM   9041  C  CB  . ARG C  1 258 ? 28.678  30.935  61.968  1.00 49.37  ? 258 ARG C CB  1 
ATOM   9042  C  CG  . ARG C  1 258 ? 27.483  31.162  62.823  1.00 62.29  ? 258 ARG C CG  1 
ATOM   9043  C  CD  . ARG C  1 258 ? 26.329  31.627  61.948  1.00 71.09  ? 258 ARG C CD  1 
ATOM   9044  N  NE  . ARG C  1 258 ? 25.062  31.823  62.664  1.00 81.59  ? 258 ARG C NE  1 
ATOM   9045  C  CZ  . ARG C  1 258 ? 24.921  32.463  63.837  1.00 88.52  ? 258 ARG C CZ  1 
ATOM   9046  N  NH1 . ARG C  1 258 ? 25.966  32.995  64.488  1.00 87.44  ? 258 ARG C NH1 1 
ATOM   9047  N  NH2 . ARG C  1 258 ? 23.702  32.607  64.353  1.00 91.68  ? 258 ARG C NH2 1 
ATOM   9048  N  N   . GLY C  1 259 ? 28.771  28.035  63.732  1.00 44.78  ? 259 GLY C N   1 
ATOM   9049  C  CA  . GLY C  1 259 ? 28.098  26.747  63.858  1.00 44.34  ? 259 GLY C CA  1 
ATOM   9050  C  C   . GLY C  1 259 ? 29.037  25.563  64.049  1.00 40.65  ? 259 GLY C C   1 
ATOM   9051  O  O   . GLY C  1 259 ? 28.621  24.505  64.506  1.00 41.81  ? 259 GLY C O   1 
ATOM   9052  N  N   . THR C  1 260 ? 30.306  25.737  63.693  1.00 37.10  ? 260 THR C N   1 
ATOM   9053  C  CA  . THR C  1 260 ? 31.302  24.685  63.843  1.00 27.94  ? 260 THR C CA  1 
ATOM   9054  C  C   . THR C  1 260 ? 31.540  24.454  65.333  1.00 24.78  ? 260 THR C C   1 
ATOM   9055  O  O   . THR C  1 260 ? 31.250  25.332  66.158  1.00 30.38  ? 260 THR C O   1 
ATOM   9056  C  CB  . THR C  1 260 ? 32.577  25.127  63.202  1.00 22.01  ? 260 THR C CB  1 
ATOM   9057  O  OG1 . THR C  1 260 ? 32.970  26.368  63.779  1.00 20.15  ? 260 THR C OG1 1 
ATOM   9058  C  CG2 . THR C  1 260 ? 32.334  25.352  61.779  1.00 16.22  ? 260 THR C CG2 1 
ATOM   9059  N  N   . PRO C  1 261 ? 32.121  23.311  65.696  1.00 17.85  ? 261 PRO C N   1 
ATOM   9060  C  CA  . PRO C  1 261 ? 32.359  23.052  67.114  1.00 15.63  ? 261 PRO C CA  1 
ATOM   9061  C  C   . PRO C  1 261 ? 33.235  24.085  67.809  1.00 20.08  ? 261 PRO C C   1 
ATOM   9062  O  O   . PRO C  1 261 ? 32.904  24.517  68.916  1.00 21.02  ? 261 PRO C O   1 
ATOM   9063  C  CB  . PRO C  1 261 ? 33.004  21.694  67.106  1.00 14.67  ? 261 PRO C CB  1 
ATOM   9064  C  CG  . PRO C  1 261 ? 32.405  21.064  65.862  1.00 16.66  ? 261 PRO C CG  1 
ATOM   9065  C  CD  . PRO C  1 261 ? 32.472  22.147  64.876  1.00 19.57  ? 261 PRO C CD  1 
ATOM   9066  N  N   . GLN C  1 262 ? 34.316  24.537  67.173  1.00 19.67  ? 262 GLN C N   1 
ATOM   9067  C  CA  . GLN C  1 262 ? 35.161  25.503  67.862  1.00 21.39  ? 262 GLN C CA  1 
ATOM   9068  C  C   . GLN C  1 262 ? 34.428  26.785  68.149  1.00 25.63  ? 262 GLN C C   1 
ATOM   9069  O  O   . GLN C  1 262 ? 34.512  27.325  69.242  1.00 29.80  ? 262 GLN C O   1 
ATOM   9070  C  CB  . GLN C  1 262 ? 36.451  25.809  67.100  1.00 14.85  ? 262 GLN C CB  1 
ATOM   9071  C  CG  . GLN C  1 262 ? 37.450  26.584  67.975  1.00 13.91  ? 262 GLN C CG  1 
ATOM   9072  C  CD  . GLN C  1 262 ? 38.775  26.899  67.279  1.00 17.09  ? 262 GLN C CD  1 
ATOM   9073  O  OE1 . GLN C  1 262 ? 39.729  27.371  67.907  1.00 17.09  ? 262 GLN C OE1 1 
ATOM   9074  N  NE2 . GLN C  1 262 ? 38.830  26.672  65.988  1.00 21.98  ? 262 GLN C NE2 1 
ATOM   9075  N  N   . TYR C  1 263 ? 33.733  27.286  67.145  1.00 30.70  ? 263 TYR C N   1 
ATOM   9076  C  CA  . TYR C  1 263 ? 32.985  28.514  67.266  1.00 33.90  ? 263 TYR C CA  1 
ATOM   9077  C  C   . TYR C  1 263 ? 31.968  28.371  68.406  1.00 36.34  ? 263 TYR C C   1 
ATOM   9078  O  O   . TYR C  1 263 ? 31.925  29.152  69.349  1.00 37.95  ? 263 TYR C O   1 
ATOM   9079  C  CB  . TYR C  1 263 ? 32.286  28.719  65.959  1.00 42.47  ? 263 TYR C CB  1 
ATOM   9080  C  CG  . TYR C  1 263 ? 31.425  29.936  65.933  1.00 51.03  ? 263 TYR C CG  1 
ATOM   9081  C  CD1 . TYR C  1 263 ? 30.195  29.949  66.567  1.00 49.64  ? 263 TYR C CD1 1 
ATOM   9082  C  CD2 . TYR C  1 263 ? 31.819  31.061  65.230  1.00 51.11  ? 263 TYR C CD2 1 
ATOM   9083  C  CE1 . TYR C  1 263 ? 29.389  31.042  66.493  1.00 55.38  ? 263 TYR C CE1 1 
ATOM   9084  C  CE2 . TYR C  1 263 ? 31.021  32.149  65.157  1.00 50.78  ? 263 TYR C CE2 1 
ATOM   9085  C  CZ  . TYR C  1 263 ? 29.805  32.140  65.778  1.00 52.80  ? 263 TYR C CZ  1 
ATOM   9086  O  OH  . TYR C  1 263 ? 28.955  33.199  65.622  1.00 59.80  ? 263 TYR C OH  1 
ATOM   9087  N  N   . THR C  1 264 ? 31.146  27.351  68.319  1.00 33.90  ? 264 THR C N   1 
ATOM   9088  C  CA  . THR C  1 264 ? 30.161  27.067  69.341  1.00 32.94  ? 264 THR C CA  1 
ATOM   9089  C  C   . THR C  1 264 ? 30.762  26.948  70.728  1.00 31.35  ? 264 THR C C   1 
ATOM   9090  O  O   . THR C  1 264 ? 30.204  27.416  71.695  1.00 37.25  ? 264 THR C O   1 
ATOM   9091  C  CB  . THR C  1 264 ? 29.507  25.738  69.068  1.00 33.22  ? 264 THR C CB  1 
ATOM   9092  O  OG1 . THR C  1 264 ? 28.783  25.782  67.822  1.00 38.48  ? 264 THR C OG1 1 
ATOM   9093  C  CG2 . THR C  1 264 ? 28.608  25.394  70.190  1.00 31.25  ? 264 THR C CG2 1 
ATOM   9094  N  N   . TRP C  1 265 ? 31.872  26.249  70.840  1.00 30.70  ? 265 TRP C N   1 
ATOM   9095  C  CA  . TRP C  1 265 ? 32.500  26.079  72.132  1.00 27.56  ? 265 TRP C CA  1 
ATOM   9096  C  C   . TRP C  1 265 ? 32.896  27.407  72.732  1.00 27.56  ? 265 TRP C C   1 
ATOM   9097  O  O   . TRP C  1 265 ? 32.500  27.728  73.851  1.00 30.22  ? 265 TRP C O   1 
ATOM   9098  C  CB  . TRP C  1 265 ? 33.741  25.174  72.023  1.00 24.37  ? 265 TRP C CB  1 
ATOM   9099  C  CG  . TRP C  1 265 ? 34.447  25.030  73.324  1.00 23.37  ? 265 TRP C CG  1 
ATOM   9100  C  CD1 . TRP C  1 265 ? 34.074  24.245  74.398  1.00 26.64  ? 265 TRP C CD1 1 
ATOM   9101  C  CD2 . TRP C  1 265 ? 35.605  25.756  73.753  1.00 20.04  ? 265 TRP C CD2 1 
ATOM   9102  N  NE1 . TRP C  1 265 ? 34.916  24.447  75.465  1.00 21.79  ? 265 TRP C NE1 1 
ATOM   9103  C  CE2 . TRP C  1 265 ? 35.871  25.367  75.107  1.00 13.50  ? 265 TRP C CE2 1 
ATOM   9104  C  CE3 . TRP C  1 265 ? 36.443  26.698  73.136  1.00 16.78  ? 265 TRP C CE3 1 
ATOM   9105  C  CZ2 . TRP C  1 265 ? 36.931  25.886  75.828  1.00 14.47  ? 265 TRP C CZ2 1 
ATOM   9106  C  CZ3 . TRP C  1 265 ? 37.503  27.219  73.870  1.00 18.81  ? 265 TRP C CZ3 1 
ATOM   9107  C  CH2 . TRP C  1 265 ? 37.740  26.806  75.212  1.00 17.43  ? 265 TRP C CH2 1 
ATOM   9108  N  N   . LEU C  1 266 ? 33.685  28.175  71.991  1.00 31.26  ? 266 LEU C N   1 
ATOM   9109  C  CA  . LEU C  1 266 ? 34.194  29.473  72.467  1.00 30.45  ? 266 LEU C CA  1 
ATOM   9110  C  C   . LEU C  1 266 ? 33.096  30.378  72.925  1.00 33.68  ? 266 LEU C C   1 
ATOM   9111  O  O   . LEU C  1 266 ? 33.234  31.061  73.951  1.00 37.70  ? 266 LEU C O   1 
ATOM   9112  C  CB  . LEU C  1 266 ? 34.978  30.171  71.368  1.00 26.12  ? 266 LEU C CB  1 
ATOM   9113  C  CG  . LEU C  1 266 ? 35.486  31.566  71.711  1.00 21.49  ? 266 LEU C CG  1 
ATOM   9114  C  CD1 . LEU C  1 266 ? 36.273  31.561  72.992  1.00 18.92  ? 266 LEU C CD1 1 
ATOM   9115  C  CD2 . LEU C  1 266 ? 36.311  32.061  70.537  1.00 26.62  ? 266 LEU C CD2 1 
ATOM   9116  N  N   . LYS C  1 267 ? 32.002  30.381  72.171  1.00 32.62  ? 267 LYS C N   1 
ATOM   9117  C  CA  . LYS C  1 267 ? 30.889  31.223  72.526  1.00 37.60  ? 267 LYS C CA  1 
ATOM   9118  C  C   . LYS C  1 267 ? 30.421  30.906  73.933  1.00 36.44  ? 267 LYS C C   1 
ATOM   9119  O  O   . LYS C  1 267 ? 30.416  31.778  74.773  1.00 44.42  ? 267 LYS C O   1 
ATOM   9120  C  CB  . LYS C  1 267 ? 29.748  31.076  71.521  1.00 44.88  ? 267 LYS C CB  1 
ATOM   9121  C  CG  . LYS C  1 267 ? 28.746  32.224  71.526  1.00 49.10  ? 267 LYS C CG  1 
ATOM   9122  C  CD  . LYS C  1 267 ? 27.710  31.983  70.452  1.00 52.46  ? 267 LYS C CD  1 
ATOM   9123  C  CE  . LYS C  1 267 ? 26.647  33.061  70.462  1.00 63.24  ? 267 LYS C CE  1 
ATOM   9124  N  NZ  . LYS C  1 267 ? 25.623  32.789  69.408  1.00 71.25  ? 267 LYS C NZ  1 
ATOM   9125  N  N   . LYS C  1 268 ? 30.132  29.652  74.225  1.00 33.40  ? 268 LYS C N   1 
ATOM   9126  C  CA  . LYS C  1 268 ? 29.672  29.310  75.548  1.00 35.20  ? 268 LYS C CA  1 
ATOM   9127  C  C   . LYS C  1 268 ? 30.747  29.510  76.567  1.00 33.37  ? 268 LYS C C   1 
ATOM   9128  O  O   . LYS C  1 268 ? 30.490  29.923  77.696  1.00 31.20  ? 268 LYS C O   1 
ATOM   9129  C  CB  . LYS C  1 268 ? 29.185  27.859  75.612  1.00 44.26  ? 268 LYS C CB  1 
ATOM   9130  C  CG  . LYS C  1 268 ? 27.955  27.595  74.741  1.00 60.20  ? 268 LYS C CG  1 
ATOM   9131  C  CD  . LYS C  1 268 ? 27.493  26.127  74.764  1.00 69.22  ? 268 LYS C CD  1 
ATOM   9132  C  CE  . LYS C  1 268 ? 26.330  25.878  73.767  1.00 76.14  ? 268 LYS C CE  1 
ATOM   9133  N  NZ  . LYS C  1 268 ? 26.024  24.412  73.518  1.00 83.58  ? 268 LYS C NZ  1 
ATOM   9134  N  N   . GLU C  1 269 ? 31.979  29.260  76.175  1.00 34.18  ? 269 GLU C N   1 
ATOM   9135  C  CA  . GLU C  1 269 ? 33.026  29.372  77.150  1.00 31.92  ? 269 GLU C CA  1 
ATOM   9136  C  C   . GLU C  1 269 ? 33.167  30.766  77.626  1.00 32.50  ? 269 GLU C C   1 
ATOM   9137  O  O   . GLU C  1 269 ? 33.297  30.963  78.812  1.00 34.49  ? 269 GLU C O   1 
ATOM   9138  C  CB  . GLU C  1 269 ? 34.345  28.868  76.620  1.00 32.35  ? 269 GLU C CB  1 
ATOM   9139  C  CG  . GLU C  1 269 ? 35.487  28.940  77.655  1.00 28.81  ? 269 GLU C CG  1 
ATOM   9140  C  CD  . GLU C  1 269 ? 35.339  27.963  78.808  1.00 30.59  ? 269 GLU C CD  1 
ATOM   9141  O  OE1 . GLU C  1 269 ? 34.500  27.055  78.727  1.00 28.02  ? 269 GLU C OE1 1 
ATOM   9142  O  OE2 . GLU C  1 269 ? 36.067  28.096  79.824  1.00 34.15  ? 269 GLU C OE2 1 
ATOM   9143  N  N   . LEU C  1 270 ? 33.111  31.739  76.721  1.00 32.22  ? 270 LEU C N   1 
ATOM   9144  C  CA  . LEU C  1 270 ? 33.269  33.123  77.125  1.00 31.17  ? 270 LEU C CA  1 
ATOM   9145  C  C   . LEU C  1 270 ? 32.246  33.466  78.193  1.00 39.46  ? 270 LEU C C   1 
ATOM   9146  O  O   . LEU C  1 270 ? 32.556  34.182  79.157  1.00 40.79  ? 270 LEU C O   1 
ATOM   9147  C  CB  . LEU C  1 270 ? 33.164  34.041  75.925  1.00 22.41  ? 270 LEU C CB  1 
ATOM   9148  C  CG  . LEU C  1 270 ? 34.502  34.058  75.232  1.00 22.05  ? 270 LEU C CG  1 
ATOM   9149  C  CD1 . LEU C  1 270 ? 34.391  34.768  73.928  1.00 18.97  ? 270 LEU C CD1 1 
ATOM   9150  C  CD2 . LEU C  1 270 ? 35.502  34.728  76.148  1.00 10.56  ? 270 LEU C CD2 1 
ATOM   9151  N  N   . ARG C  1 271 ? 31.057  32.874  78.089  1.00 44.59  ? 271 ARG C N   1 
ATOM   9152  C  CA  . ARG C  1 271 ? 30.016  33.144  79.080  1.00 52.72  ? 271 ARG C CA  1 
ATOM   9153  C  C   . ARG C  1 271 ? 30.332  32.488  80.422  1.00 55.20  ? 271 ARG C C   1 
ATOM   9154  O  O   . ARG C  1 271 ? 29.842  32.925  81.454  1.00 61.62  ? 271 ARG C O   1 
ATOM   9155  C  CB  . ARG C  1 271 ? 28.639  32.634  78.638  1.00 58.53  ? 271 ARG C CB  1 
ATOM   9156  C  CG  . ARG C  1 271 ? 28.073  33.180  77.339  1.00 72.17  ? 271 ARG C CG  1 
ATOM   9157  C  CD  . ARG C  1 271 ? 26.608  32.704  77.194  1.00 80.87  ? 271 ARG C CD  1 
ATOM   9158  N  NE  . ARG C  1 271 ? 26.130  32.620  75.799  1.00 88.32  ? 271 ARG C NE  1 
ATOM   9159  C  CZ  . ARG C  1 271 ? 25.578  31.527  75.247  1.00 87.26  ? 271 ARG C CZ  1 
ATOM   9160  N  NH1 . ARG C  1 271 ? 25.436  30.413  75.972  1.00 87.07  ? 271 ARG C NH1 1 
ATOM   9161  N  NH2 . ARG C  1 271 ? 25.137  31.553  73.979  1.00 83.69  ? 271 ARG C NH2 1 
ATOM   9162  N  N   . LYS C  1 272 ? 31.094  31.403  80.422  1.00 55.30  ? 272 LYS C N   1 
ATOM   9163  C  CA  . LYS C  1 272 ? 31.374  30.731  81.684  1.00 50.57  ? 272 LYS C CA  1 
ATOM   9164  C  C   . LYS C  1 272 ? 32.474  31.403  82.495  1.00 48.33  ? 272 LYS C C   1 
ATOM   9165  O  O   . LYS C  1 272 ? 32.813  30.945  83.599  1.00 51.09  ? 272 LYS C O   1 
ATOM   9166  C  CB  . LYS C  1 272 ? 31.734  29.259  81.454  1.00 49.69  ? 272 LYS C CB  1 
ATOM   9167  C  CG  . LYS C  1 272 ? 30.757  28.407  80.604  1.00 51.83  ? 272 LYS C CG  1 
ATOM   9168  C  CD  . LYS C  1 272 ? 31.056  26.894  80.832  1.00 55.00  ? 272 LYS C CD  1 
ATOM   9169  C  CE  . LYS C  1 272 ? 30.748  25.957  79.642  1.00 59.83  ? 272 LYS C CE  1 
ATOM   9170  N  NZ  . LYS C  1 272 ? 31.911  25.615  78.698  1.00 64.40  ? 272 LYS C NZ  1 
ATOM   9171  N  N   . VAL C  1 273 ? 33.054  32.466  81.956  1.00 47.26  ? 273 VAL C N   1 
ATOM   9172  C  CA  . VAL C  1 273 ? 34.153  33.132  82.652  1.00 48.72  ? 273 VAL C CA  1 
ATOM   9173  C  C   . VAL C  1 273 ? 33.597  33.967  83.773  1.00 48.76  ? 273 VAL C C   1 
ATOM   9174  O  O   . VAL C  1 273 ? 32.667  34.707  83.542  1.00 56.45  ? 273 VAL C O   1 
ATOM   9175  C  CB  . VAL C  1 273 ? 34.934  34.071  81.717  1.00 46.45  ? 273 VAL C CB  1 
ATOM   9176  C  CG1 . VAL C  1 273 ? 36.088  34.657  82.441  1.00 45.00  ? 273 VAL C CG1 1 
ATOM   9177  C  CG2 . VAL C  1 273 ? 35.435  33.327  80.517  1.00 48.30  ? 273 VAL C CG2 1 
ATOM   9178  N  N   . LYS C  1 274 ? 34.148  33.847  84.978  1.00 49.02  ? 274 LYS C N   1 
ATOM   9179  C  CA  . LYS C  1 274 ? 33.709  34.641  86.136  1.00 45.07  ? 274 LYS C CA  1 
ATOM   9180  C  C   . LYS C  1 274 ? 34.901  35.401  86.629  1.00 42.10  ? 274 LYS C C   1 
ATOM   9181  O  O   . LYS C  1 274 ? 35.798  34.810  87.234  1.00 43.48  ? 274 LYS C O   1 
ATOM   9182  C  CB  . LYS C  1 274 ? 33.242  33.740  87.260  1.00 52.28  ? 274 LYS C CB  1 
ATOM   9183  C  CG  . LYS C  1 274 ? 31.852  33.140  87.043  1.00 67.34  ? 274 LYS C CG  1 
ATOM   9184  C  CD  . LYS C  1 274 ? 31.591  31.924  87.988  1.00 82.43  ? 274 LYS C CD  1 
ATOM   9185  C  CE  . LYS C  1 274 ? 31.760  32.259  89.511  1.00 90.04  ? 274 LYS C CE  1 
ATOM   9186  N  NZ  . LYS C  1 274 ? 31.509  31.109  90.465  1.00 89.58  ? 274 LYS C NZ  1 
ATOM   9187  N  N   . ARG C  1 275 ? 34.908  36.713  86.411  1.00 41.08  ? 275 ARG C N   1 
ATOM   9188  C  CA  . ARG C  1 275 ? 36.049  37.562  86.804  1.00 40.88  ? 275 ARG C CA  1 
ATOM   9189  C  C   . ARG C  1 275 ? 36.225  37.842  88.267  1.00 43.32  ? 275 ARG C C   1 
ATOM   9190  O  O   . ARG C  1 275 ? 37.246  38.417  88.681  1.00 43.38  ? 275 ARG C O   1 
ATOM   9191  C  CB  . ARG C  1 275 ? 36.013  38.862  86.051  1.00 34.76  ? 275 ARG C CB  1 
ATOM   9192  C  CG  . ARG C  1 275 ? 36.100  38.651  84.578  1.00 31.07  ? 275 ARG C CG  1 
ATOM   9193  C  CD  . ARG C  1 275 ? 37.530  38.662  84.104  1.00 26.90  ? 275 ARG C CD  1 
ATOM   9194  N  NE  . ARG C  1 275 ? 37.465  39.242  82.785  1.00 27.76  ? 275 ARG C NE  1 
ATOM   9195  C  CZ  . ARG C  1 275 ? 38.378  40.027  82.250  1.00 24.77  ? 275 ARG C CZ  1 
ATOM   9196  N  NH1 . ARG C  1 275 ? 39.491  40.315  82.897  1.00 20.70  ? 275 ARG C NH1 1 
ATOM   9197  N  NH2 . ARG C  1 275 ? 38.114  40.603  81.100  1.00 21.42  ? 275 ARG C NH2 1 
ATOM   9198  N  N   . SER C  1 276 ? 35.162  37.544  89.017  1.00 48.06  ? 276 SER C N   1 
ATOM   9199  C  CA  . SER C  1 276 ? 35.121  37.655  90.488  1.00 46.57  ? 276 SER C CA  1 
ATOM   9200  C  C   . SER C  1 276 ? 35.931  36.462  91.025  1.00 47.65  ? 276 SER C C   1 
ATOM   9201  O  O   . SER C  1 276 ? 36.388  36.449  92.172  1.00 45.17  ? 276 SER C O   1 
ATOM   9202  C  CB  . SER C  1 276 ? 33.669  37.565  91.022  1.00 41.58  ? 276 SER C CB  1 
ATOM   9203  O  OG  . SER C  1 276 ? 32.718  37.077  90.071  1.00 41.56  ? 276 SER C OG  1 
ATOM   9204  N  N   . GLU C  1 277 ? 36.100  35.464  90.155  1.00 49.33  ? 277 GLU C N   1 
ATOM   9205  C  CA  . GLU C  1 277 ? 36.814  34.258  90.466  1.00 46.03  ? 277 GLU C CA  1 
ATOM   9206  C  C   . GLU C  1 277 ? 38.214  34.311  89.901  1.00 41.78  ? 277 GLU C C   1 
ATOM   9207  O  O   . GLU C  1 277 ? 39.180  34.178  90.638  1.00 43.66  ? 277 GLU C O   1 
ATOM   9208  C  CB  . GLU C  1 277 ? 36.030  33.088  89.913  1.00 53.40  ? 277 GLU C CB  1 
ATOM   9209  C  CG  . GLU C  1 277 ? 36.598  31.758  90.296  1.00 72.64  ? 277 GLU C CG  1 
ATOM   9210  C  CD  . GLU C  1 277 ? 35.616  30.619  90.053  1.00 82.94  ? 277 GLU C CD  1 
ATOM   9211  O  OE1 . GLU C  1 277 ? 34.421  30.743  90.450  1.00 89.06  ? 277 GLU C OE1 1 
ATOM   9212  O  OE2 . GLU C  1 277 ? 36.053  29.594  89.485  1.00 85.69  ? 277 GLU C OE2 1 
ATOM   9213  N  N   . THR C  1 278 ? 38.334  34.493  88.596  1.00 36.60  ? 278 THR C N   1 
ATOM   9214  C  CA  . THR C  1 278 ? 39.644  34.568  87.977  1.00 35.70  ? 278 THR C CA  1 
ATOM   9215  C  C   . THR C  1 278 ? 39.641  35.864  87.250  1.00 34.92  ? 278 THR C C   1 
ATOM   9216  O  O   . THR C  1 278 ? 39.092  35.989  86.165  1.00 34.90  ? 278 THR C O   1 
ATOM   9217  C  CB  . THR C  1 278 ? 39.853  33.446  86.974  1.00 41.35  ? 278 THR C CB  1 
ATOM   9218  O  OG1 . THR C  1 278 ? 38.697  33.323  86.124  1.00 44.61  ? 278 THR C OG1 1 
ATOM   9219  C  CG2 . THR C  1 278 ? 40.072  32.165  87.698  1.00 44.07  ? 278 THR C CG2 1 
ATOM   9220  N  N   . PRO C  1 279 ? 40.175  36.882  87.877  1.00 33.81  ? 279 PRO C N   1 
ATOM   9221  C  CA  . PRO C  1 279 ? 40.242  38.230  87.313  1.00 30.41  ? 279 PRO C CA  1 
ATOM   9222  C  C   . PRO C  1 279 ? 40.912  38.323  85.951  1.00 34.30  ? 279 PRO C C   1 
ATOM   9223  O  O   . PRO C  1 279 ? 40.425  39.030  85.050  1.00 38.58  ? 279 PRO C O   1 
ATOM   9224  C  CB  . PRO C  1 279 ? 41.027  39.001  88.362  1.00 29.22  ? 279 PRO C CB  1 
ATOM   9225  C  CG  . PRO C  1 279 ? 41.846  37.950  89.027  1.00 33.71  ? 279 PRO C CG  1 
ATOM   9226  C  CD  . PRO C  1 279 ? 40.884  36.781  89.150  1.00 28.99  ? 279 PRO C CD  1 
ATOM   9227  N  N   . TRP C  1 280 ? 42.015  37.603  85.772  1.00 30.11  ? 280 TRP C N   1 
ATOM   9228  C  CA  . TRP C  1 280 ? 42.745  37.664  84.516  1.00 28.15  ? 280 TRP C CA  1 
ATOM   9229  C  C   . TRP C  1 280 ? 42.265  36.731  83.430  1.00 30.34  ? 280 TRP C C   1 
ATOM   9230  O  O   . TRP C  1 280 ? 42.238  35.521  83.653  1.00 37.03  ? 280 TRP C O   1 
ATOM   9231  C  CB  . TRP C  1 280 ? 44.175  37.406  84.823  1.00 22.81  ? 280 TRP C CB  1 
ATOM   9232  C  CG  . TRP C  1 280 ? 44.688  38.499  85.644  1.00 35.08  ? 280 TRP C CG  1 
ATOM   9233  C  CD1 . TRP C  1 280 ? 44.894  38.492  86.994  1.00 37.08  ? 280 TRP C CD1 1 
ATOM   9234  C  CD2 . TRP C  1 280 ? 45.125  39.779  85.171  1.00 34.60  ? 280 TRP C CD2 1 
ATOM   9235  N  NE1 . TRP C  1 280 ? 45.450  39.687  87.388  1.00 39.40  ? 280 TRP C NE1 1 
ATOM   9236  C  CE2 . TRP C  1 280 ? 45.606  40.490  86.284  1.00 36.90  ? 280 TRP C CE2 1 
ATOM   9237  C  CE3 . TRP C  1 280 ? 45.162  40.392  83.907  1.00 33.37  ? 280 TRP C CE3 1 
ATOM   9238  C  CZ2 . TRP C  1 280 ? 46.126  41.782  86.169  1.00 42.35  ? 280 TRP C CZ2 1 
ATOM   9239  C  CZ3 . TRP C  1 280 ? 45.678  41.678  83.795  1.00 31.74  ? 280 TRP C CZ3 1 
ATOM   9240  C  CH2 . TRP C  1 280 ? 46.153  42.358  84.912  1.00 36.17  ? 280 TRP C CH2 1 
ATOM   9241  N  N   . LEU C  1 281 ? 41.906  37.269  82.258  1.00 27.39  ? 281 LEU C N   1 
ATOM   9242  C  CA  . LEU C  1 281 ? 41.418  36.438  81.158  1.00 23.86  ? 281 LEU C CA  1 
ATOM   9243  C  C   . LEU C  1 281 ? 42.435  36.513  80.041  1.00 29.91  ? 281 LEU C C   1 
ATOM   9244  O  O   . LEU C  1 281 ? 42.600  37.581  79.457  1.00 38.43  ? 281 LEU C O   1 
ATOM   9245  C  CB  . LEU C  1 281 ? 40.089  36.963  80.667  1.00 19.45  ? 281 LEU C CB  1 
ATOM   9246  C  CG  . LEU C  1 281 ? 39.491  36.312  79.435  1.00 27.55  ? 281 LEU C CG  1 
ATOM   9247  C  CD1 . LEU C  1 281 ? 39.105  34.879  79.755  1.00 29.04  ? 281 LEU C CD1 1 
ATOM   9248  C  CD2 . LEU C  1 281 ? 38.261  37.076  79.003  1.00 31.15  ? 281 LEU C CD2 1 
ATOM   9249  N  N   . ILE C  1 282 ? 43.083  35.381  79.734  1.00 26.72  ? 282 ILE C N   1 
ATOM   9250  C  CA  . ILE C  1 282 ? 44.121  35.255  78.712  1.00 19.65  ? 282 ILE C CA  1 
ATOM   9251  C  C   . ILE C  1 282 ? 43.718  34.355  77.574  1.00 20.21  ? 282 ILE C C   1 
ATOM   9252  O  O   . ILE C  1 282 ? 43.127  33.313  77.792  1.00 31.85  ? 282 ILE C O   1 
ATOM   9253  C  CB  . ILE C  1 282 ? 45.338  34.634  79.324  1.00 15.82  ? 282 ILE C CB  1 
ATOM   9254  C  CG1 . ILE C  1 282 ? 45.757  35.498  80.522  1.00 16.82  ? 282 ILE C CG1 1 
ATOM   9255  C  CG2 . ILE C  1 282 ? 46.452  34.532  78.299  1.00 14.02  ? 282 ILE C CG2 1 
ATOM   9256  C  CD1 . ILE C  1 282 ? 46.850  34.913  81.421  1.00 12.64  ? 282 ILE C CD1 1 
ATOM   9257  N  N   . VAL C  1 283 ? 44.115  34.672  76.365  1.00 14.03  ? 283 VAL C N   1 
ATOM   9258  C  CA  . VAL C  1 283 ? 43.744  33.810  75.272  1.00 19.22  ? 283 VAL C CA  1 
ATOM   9259  C  C   . VAL C  1 283 ? 45.017  33.487  74.518  1.00 23.44  ? 283 VAL C C   1 
ATOM   9260  O  O   . VAL C  1 283 ? 45.897  34.348  74.380  1.00 28.77  ? 283 VAL C O   1 
ATOM   9261  C  CB  . VAL C  1 283 ? 42.787  34.498  74.321  1.00 18.65  ? 283 VAL C CB  1 
ATOM   9262  C  CG1 . VAL C  1 283 ? 42.635  33.690  73.036  1.00 15.38  ? 283 VAL C CG1 1 
ATOM   9263  C  CG2 . VAL C  1 283 ? 41.476  34.695  74.980  1.00 18.75  ? 283 VAL C CG2 1 
ATOM   9264  N  N   . LEU C  1 284 ? 45.093  32.268  73.997  1.00 19.04  ? 284 LEU C N   1 
ATOM   9265  C  CA  . LEU C  1 284 ? 46.251  31.824  73.256  1.00 18.55  ? 284 LEU C CA  1 
ATOM   9266  C  C   . LEU C  1 284 ? 45.823  31.349  71.882  1.00 21.83  ? 284 LEU C C   1 
ATOM   9267  O  O   . LEU C  1 284 ? 44.724  30.752  71.750  1.00 26.75  ? 284 LEU C O   1 
ATOM   9268  C  CB  . LEU C  1 284 ? 46.888  30.651  73.957  1.00 23.94  ? 284 LEU C CB  1 
ATOM   9269  C  CG  . LEU C  1 284 ? 47.259  30.804  75.436  1.00 29.77  ? 284 LEU C CG  1 
ATOM   9270  C  CD1 . LEU C  1 284 ? 47.909  29.525  75.901  1.00 30.08  ? 284 LEU C CD1 1 
ATOM   9271  C  CD2 . LEU C  1 284 ? 48.188  31.977  75.678  1.00 29.04  ? 284 LEU C CD2 1 
ATOM   9272  N  N   . MET C  1 285 ? 46.679  31.581  70.885  1.00 12.04  ? 285 MET C N   1 
ATOM   9273  C  CA  . MET C  1 285 ? 46.430  31.179  69.510  1.00 15.33  ? 285 MET C CA  1 
ATOM   9274  C  C   . MET C  1 285 ? 47.746  31.310  68.781  1.00 19.39  ? 285 MET C C   1 
ATOM   9275  O  O   . MET C  1 285 ? 48.609  32.065  69.204  1.00 24.71  ? 285 MET C O   1 
ATOM   9276  C  CB  . MET C  1 285 ? 45.352  32.040  68.841  1.00 22.41  ? 285 MET C CB  1 
ATOM   9277  C  CG  . MET C  1 285 ? 45.629  33.530  68.867  1.00 36.30  ? 285 MET C CG  1 
ATOM   9278  S  SD  . MET C  1 285 ? 44.499  34.490  67.931  1.00 36.67  ? 285 MET C SD  1 
ATOM   9279  C  CE  . MET C  1 285 ? 43.160  34.621  69.139  1.00 36.10  ? 285 MET C CE  1 
ATOM   9280  N  N   . HIS C  1 286 ? 47.914  30.589  67.690  1.00 21.22  ? 286 HIS C N   1 
ATOM   9281  C  CA  . HIS C  1 286 ? 49.178  30.649  67.005  1.00 21.61  ? 286 HIS C CA  1 
ATOM   9282  C  C   . HIS C  1 286 ? 49.292  31.861  66.102  1.00 25.35  ? 286 HIS C C   1 
ATOM   9283  O  O   . HIS C  1 286 ? 50.207  32.661  66.272  1.00 29.20  ? 286 HIS C O   1 
ATOM   9284  C  CB  . HIS C  1 286 ? 49.413  29.365  66.206  1.00 21.67  ? 286 HIS C CB  1 
ATOM   9285  C  CG  . HIS C  1 286 ? 50.767  29.279  65.580  1.00 20.99  ? 286 HIS C CG  1 
ATOM   9286  N  ND1 . HIS C  1 286 ? 51.922  29.159  66.330  1.00 23.66  ? 286 HIS C ND1 1 
ATOM   9287  C  CD2 . HIS C  1 286 ? 51.160  29.294  64.284  1.00 18.69  ? 286 HIS C CD2 1 
ATOM   9288  C  CE1 . HIS C  1 286 ? 52.961  29.116  65.516  1.00 19.47  ? 286 HIS C CE1 1 
ATOM   9289  N  NE2 . HIS C  1 286 ? 52.525  29.194  64.278  1.00 18.57  ? 286 HIS C NE2 1 
ATOM   9290  N  N   . SER C  1 287 ? 48.361  32.001  65.154  1.00 25.76  ? 287 SER C N   1 
ATOM   9291  C  CA  . SER C  1 287 ? 48.388  33.105  64.198  1.00 26.92  ? 287 SER C CA  1 
ATOM   9292  C  C   . SER C  1 287 ? 47.804  34.325  64.847  1.00 26.43  ? 287 SER C C   1 
ATOM   9293  O  O   . SER C  1 287 ? 46.642  34.346  65.246  1.00 30.00  ? 287 SER C O   1 
ATOM   9294  C  CB  . SER C  1 287 ? 47.587  32.805  62.954  1.00 29.08  ? 287 SER C CB  1 
ATOM   9295  O  OG  . SER C  1 287 ? 48.258  33.368  61.834  1.00 38.75  ? 287 SER C OG  1 
ATOM   9296  N  N   . PRO C  1 288 ? 48.608  35.365  64.947  1.00 22.61  ? 288 PRO C N   1 
ATOM   9297  C  CA  . PRO C  1 288 ? 48.341  36.665  65.526  1.00 20.09  ? 288 PRO C CA  1 
ATOM   9298  C  C   . PRO C  1 288 ? 47.322  37.473  64.716  1.00 25.67  ? 288 PRO C C   1 
ATOM   9299  O  O   . PRO C  1 288 ? 47.428  37.531  63.478  1.00 28.77  ? 288 PRO C O   1 
ATOM   9300  C  CB  . PRO C  1 288 ? 49.714  37.276  65.515  1.00 15.44  ? 288 PRO C CB  1 
ATOM   9301  C  CG  . PRO C  1 288 ? 50.303  36.799  64.262  1.00 16.58  ? 288 PRO C CG  1 
ATOM   9302  C  CD  . PRO C  1 288 ? 49.883  35.363  64.206  1.00 27.21  ? 288 PRO C CD  1 
ATOM   9303  N  N   . LEU C  1 289 ? 46.317  38.052  65.404  1.00 28.18  ? 289 LEU C N   1 
ATOM   9304  C  CA  . LEU C  1 289 ? 45.227  38.847  64.774  1.00 22.38  ? 289 LEU C CA  1 
ATOM   9305  C  C   . LEU C  1 289 ? 45.699  40.242  64.353  1.00 27.01  ? 289 LEU C C   1 
ATOM   9306  O  O   . LEU C  1 289 ? 45.204  40.798  63.350  1.00 36.30  ? 289 LEU C O   1 
ATOM   9307  C  CB  . LEU C  1 289 ? 44.088  39.009  65.746  1.00 15.40  ? 289 LEU C CB  1 
ATOM   9308  C  CG  . LEU C  1 289 ? 43.375  37.742  66.157  1.00 14.10  ? 289 LEU C CG  1 
ATOM   9309  C  CD1 . LEU C  1 289 ? 42.127  38.058  66.953  1.00 10.79  ? 289 LEU C CD1 1 
ATOM   9310  C  CD2 . LEU C  1 289 ? 42.983  37.071  64.911  1.00 8.51   ? 289 LEU C CD2 1 
ATOM   9311  N  N   . TYR C  1 290 ? 46.643  40.775  65.144  1.00 25.28  ? 290 TYR C N   1 
ATOM   9312  C  CA  . TYR C  1 290 ? 47.302  42.059  64.958  1.00 27.91  ? 290 TYR C CA  1 
ATOM   9313  C  C   . TYR C  1 290 ? 48.832  41.804  64.789  1.00 30.59  ? 290 TYR C C   1 
ATOM   9314  O  O   . TYR C  1 290 ? 49.491  41.355  65.747  1.00 36.09  ? 290 TYR C O   1 
ATOM   9315  C  CB  . TYR C  1 290 ? 47.030  42.978  66.166  1.00 26.16  ? 290 TYR C CB  1 
ATOM   9316  C  CG  . TYR C  1 290 ? 45.686  43.660  66.103  1.00 30.06  ? 290 TYR C CG  1 
ATOM   9317  C  CD1 . TYR C  1 290 ? 45.493  44.779  65.290  1.00 31.16  ? 290 TYR C CD1 1 
ATOM   9318  C  CD2 . TYR C  1 290 ? 44.591  43.132  66.770  1.00 29.77  ? 290 TYR C CD2 1 
ATOM   9319  C  CE1 . TYR C  1 290 ? 44.240  45.345  65.126  1.00 36.67  ? 290 TYR C CE1 1 
ATOM   9320  C  CE2 . TYR C  1 290 ? 43.337  43.689  66.625  1.00 30.62  ? 290 TYR C CE2 1 
ATOM   9321  C  CZ  . TYR C  1 290 ? 43.160  44.798  65.795  1.00 37.82  ? 290 TYR C CZ  1 
ATOM   9322  O  OH  . TYR C  1 290 ? 41.913  45.359  65.602  1.00 40.23  ? 290 TYR C OH  1 
ATOM   9323  N  N   . ASN C  1 291 ? 49.378  42.110  63.601  1.00 28.42  ? 291 ASN C N   1 
ATOM   9324  C  CA  . ASN C  1 291 ? 50.788  41.898  63.291  1.00 26.58  ? 291 ASN C CA  1 
ATOM   9325  C  C   . ASN C  1 291 ? 51.242  42.824  62.135  1.00 32.51  ? 291 ASN C C   1 
ATOM   9326  O  O   . ASN C  1 291 ? 50.642  42.803  61.041  1.00 30.04  ? 291 ASN C O   1 
ATOM   9327  C  CB  . ASN C  1 291 ? 50.990  40.424  62.909  1.00 24.90  ? 291 ASN C CB  1 
ATOM   9328  C  CG  . ASN C  1 291 ? 52.193  40.191  62.021  1.00 26.98  ? 291 ASN C CG  1 
ATOM   9329  O  OD1 . ASN C  1 291 ? 52.051  39.658  60.927  1.00 26.30  ? 291 ASN C OD1 1 
ATOM   9330  N  ND2 . ASN C  1 291 ? 53.385  40.572  62.484  1.00 30.11  ? 291 ASN C ND2 1 
ATOM   9331  N  N   . SER C  1 292 ? 52.326  43.581  62.378  1.00 28.33  ? 292 SER C N   1 
ATOM   9332  C  CA  . SER C  1 292 ? 52.858  44.492  61.405  1.00 22.62  ? 292 SER C CA  1 
ATOM   9333  C  C   . SER C  1 292 ? 54.136  44.057  60.760  1.00 24.14  ? 292 SER C C   1 
ATOM   9334  O  O   . SER C  1 292 ? 54.933  44.922  60.336  1.00 26.10  ? 292 SER C O   1 
ATOM   9335  C  CB  . SER C  1 292 ? 53.086  45.843  62.034  1.00 22.97  ? 292 SER C CB  1 
ATOM   9336  O  OG  . SER C  1 292 ? 54.102  45.751  63.009  1.00 26.46  ? 292 SER C OG  1 
ATOM   9337  N  N   . TYR C  1 293 ? 54.401  42.756  60.764  1.00 20.62  ? 293 TYR C N   1 
ATOM   9338  C  CA  . TYR C  1 293 ? 55.593  42.277  60.101  1.00 21.52  ? 293 TYR C CA  1 
ATOM   9339  C  C   . TYR C  1 293 ? 55.144  41.825  58.751  1.00 27.85  ? 293 TYR C C   1 
ATOM   9340  O  O   . TYR C  1 293 ? 53.968  41.528  58.555  1.00 29.12  ? 293 TYR C O   1 
ATOM   9341  C  CB  . TYR C  1 293 ? 56.218  41.126  60.809  1.00 18.72  ? 293 TYR C CB  1 
ATOM   9342  C  CG  . TYR C  1 293 ? 57.009  41.545  62.007  1.00 19.88  ? 293 TYR C CG  1 
ATOM   9343  C  CD1 . TYR C  1 293 ? 56.369  41.977  63.146  1.00 16.82  ? 293 TYR C CD1 1 
ATOM   9344  C  CD2 . TYR C  1 293 ? 58.398  41.459  62.030  1.00 21.94  ? 293 TYR C CD2 1 
ATOM   9345  C  CE1 . TYR C  1 293 ? 57.081  42.307  64.289  1.00 12.48  ? 293 TYR C CE1 1 
ATOM   9346  C  CE2 . TYR C  1 293 ? 59.112  41.792  63.173  1.00 17.65  ? 293 TYR C CE2 1 
ATOM   9347  C  CZ  . TYR C  1 293 ? 58.442  42.217  64.288  1.00 16.67  ? 293 TYR C CZ  1 
ATOM   9348  O  OH  . TYR C  1 293 ? 59.128  42.583  65.422  1.00 26.07  ? 293 TYR C OH  1 
ATOM   9349  N  N   . ASN C  1 294 ? 56.075  41.753  57.811  1.00 30.62  ? 294 ASN C N   1 
ATOM   9350  C  CA  . ASN C  1 294 ? 55.697  41.371  56.483  1.00 33.66  ? 294 ASN C CA  1 
ATOM   9351  C  C   . ASN C  1 294 ? 55.347  39.904  56.437  1.00 36.49  ? 294 ASN C C   1 
ATOM   9352  O  O   . ASN C  1 294 ? 54.382  39.495  55.771  1.00 40.09  ? 294 ASN C O   1 
ATOM   9353  C  CB  . ASN C  1 294 ? 56.808  41.695  55.483  1.00 43.09  ? 294 ASN C CB  1 
ATOM   9354  C  CG  . ASN C  1 294 ? 56.984  43.194  55.259  1.00 55.67  ? 294 ASN C CG  1 
ATOM   9355  O  OD1 . ASN C  1 294 ? 56.479  43.772  54.288  1.00 70.28  ? 294 ASN C OD1 1 
ATOM   9356  N  ND2 . ASN C  1 294 ? 57.706  43.830  56.155  1.00 57.81  ? 294 ASN C ND2 1 
ATOM   9357  N  N   . HIS C  1 295 ? 56.159  39.105  57.121  1.00 34.98  ? 295 HIS C N   1 
ATOM   9358  C  CA  . HIS C  1 295 ? 55.964  37.670  57.150  1.00 32.53  ? 295 HIS C CA  1 
ATOM   9359  C  C   . HIS C  1 295 ? 54.627  37.345  57.806  1.00 30.55  ? 295 HIS C C   1 
ATOM   9360  O  O   . HIS C  1 295 ? 54.393  37.714  58.955  1.00 30.58  ? 295 HIS C O   1 
ATOM   9361  C  CB  . HIS C  1 295 ? 57.114  37.051  57.930  1.00 40.39  ? 295 HIS C CB  1 
ATOM   9362  C  CG  . HIS C  1 295 ? 57.194  35.560  57.824  1.00 47.69  ? 295 HIS C CG  1 
ATOM   9363  N  ND1 . HIS C  1 295 ? 57.585  34.763  58.875  1.00 48.92  ? 295 HIS C ND1 1 
ATOM   9364  C  CD2 . HIS C  1 295 ? 56.912  34.722  56.799  1.00 53.51  ? 295 HIS C CD2 1 
ATOM   9365  C  CE1 . HIS C  1 295 ? 57.541  33.493  58.506  1.00 54.43  ? 295 HIS C CE1 1 
ATOM   9366  N  NE2 . HIS C  1 295 ? 57.133  33.442  57.248  1.00 54.32  ? 295 HIS C NE2 1 
ATOM   9367  N  N   . HIS C  1 296 ? 53.754  36.660  57.078  1.00 28.43  ? 296 HIS C N   1 
ATOM   9368  C  CA  . HIS C  1 296 ? 52.445  36.292  57.615  1.00 32.60  ? 296 HIS C CA  1 
ATOM   9369  C  C   . HIS C  1 296 ? 51.608  37.507  57.902  1.00 32.32  ? 296 HIS C C   1 
ATOM   9370  O  O   . HIS C  1 296 ? 50.781  37.514  58.810  1.00 39.34  ? 296 HIS C O   1 
ATOM   9371  C  CB  . HIS C  1 296 ? 52.562  35.515  58.921  1.00 30.93  ? 296 HIS C CB  1 
ATOM   9372  C  CG  . HIS C  1 296 ? 53.240  34.193  58.781  1.00 34.63  ? 296 HIS C CG  1 
ATOM   9373  N  ND1 . HIS C  1 296 ? 52.956  33.308  57.768  1.00 30.12  ? 296 HIS C ND1 1 
ATOM   9374  C  CD2 . HIS C  1 296 ? 54.190  33.603  59.542  1.00 35.63  ? 296 HIS C CD2 1 
ATOM   9375  C  CE1 . HIS C  1 296 ? 53.705  32.229  57.906  1.00 32.68  ? 296 HIS C CE1 1 
ATOM   9376  N  NE2 . HIS C  1 296 ? 54.461  32.384  58.974  1.00 33.07  ? 296 HIS C NE2 1 
ATOM   9377  N  N   . PHE C  1 297 ? 51.833  38.541  57.135  1.00 30.59  ? 297 PHE C N   1 
ATOM   9378  C  CA  . PHE C  1 297 ? 51.090  39.751  57.332  1.00 30.47  ? 297 PHE C CA  1 
ATOM   9379  C  C   . PHE C  1 297 ? 49.662  39.484  56.902  1.00 29.95  ? 297 PHE C C   1 
ATOM   9380  O  O   . PHE C  1 297 ? 49.468  38.957  55.813  1.00 30.86  ? 297 PHE C O   1 
ATOM   9381  C  CB  . PHE C  1 297 ? 51.719  40.862  56.503  1.00 28.36  ? 297 PHE C CB  1 
ATOM   9382  C  CG  . PHE C  1 297 ? 50.940  42.098  56.516  1.00 32.66  ? 297 PHE C CG  1 
ATOM   9383  C  CD1 . PHE C  1 297 ? 50.732  42.763  57.716  1.00 40.24  ? 297 PHE C CD1 1 
ATOM   9384  C  CD2 . PHE C  1 297 ? 50.323  42.569  55.348  1.00 34.78  ? 297 PHE C CD2 1 
ATOM   9385  C  CE1 . PHE C  1 297 ? 49.897  43.892  57.767  1.00 41.49  ? 297 PHE C CE1 1 
ATOM   9386  C  CE2 . PHE C  1 297 ? 49.487  43.685  55.375  1.00 33.61  ? 297 PHE C CE2 1 
ATOM   9387  C  CZ  . PHE C  1 297 ? 49.267  44.353  56.587  1.00 37.90  ? 297 PHE C CZ  1 
ATOM   9388  N  N   . MET C  1 298 ? 48.700  39.755  57.794  1.00 31.41  ? 298 MET C N   1 
ATOM   9389  C  CA  . MET C  1 298 ? 47.245  39.578  57.545  1.00 32.61  ? 298 MET C CA  1 
ATOM   9390  C  C   . MET C  1 298 ? 46.607  38.175  57.455  1.00 35.67  ? 298 MET C C   1 
ATOM   9391  O  O   . MET C  1 298 ? 45.481  38.009  56.932  1.00 41.33  ? 298 MET C O   1 
ATOM   9392  C  CB  . MET C  1 298 ? 46.790  40.403  56.331  1.00 33.16  ? 298 MET C CB  1 
ATOM   9393  C  CG  . MET C  1 298 ? 46.785  41.934  56.532  1.00 33.36  ? 298 MET C CG  1 
ATOM   9394  S  SD  . MET C  1 298 ? 45.880  42.839  55.312  1.00 28.42  ? 298 MET C SD  1 
ATOM   9395  C  CE  . MET C  1 298 ? 46.781  42.348  53.809  1.00 23.80  ? 298 MET C CE  1 
ATOM   9396  N  N   . GLU C  1 299 ? 47.283  37.168  58.000  1.00 36.65  ? 299 GLU C N   1 
ATOM   9397  C  CA  . GLU C  1 299 ? 46.742  35.812  57.985  1.00 33.24  ? 299 GLU C CA  1 
ATOM   9398  C  C   . GLU C  1 299 ? 45.680  35.719  59.080  1.00 35.10  ? 299 GLU C C   1 
ATOM   9399  O  O   . GLU C  1 299 ? 44.696  35.007  58.931  1.00 37.82  ? 299 GLU C O   1 
ATOM   9400  C  CB  . GLU C  1 299 ? 47.865  34.788  58.186  1.00 30.58  ? 299 GLU C CB  1 
ATOM   9401  C  CG  . GLU C  1 299 ? 48.714  34.567  56.954  1.00 15.85  ? 299 GLU C CG  1 
ATOM   9402  C  CD  . GLU C  1 299 ? 49.811  33.547  57.146  1.00 22.53  ? 299 GLU C CD  1 
ATOM   9403  O  OE1 . GLU C  1 299 ? 49.796  32.789  58.169  1.00 28.09  ? 299 GLU C OE1 1 
ATOM   9404  O  OE2 . GLU C  1 299 ? 50.675  33.493  56.229  1.00 18.94  ? 299 GLU C OE2 1 
ATOM   9405  N  N   . GLY C  1 300 ? 45.851  36.500  60.149  1.00 36.95  ? 300 GLY C N   1 
ATOM   9406  C  CA  . GLY C  1 300 ? 44.895  36.510  61.252  1.00 35.89  ? 300 GLY C CA  1 
ATOM   9407  C  C   . GLY C  1 300 ? 43.570  37.207  60.952  1.00 35.15  ? 300 GLY C C   1 
ATOM   9408  O  O   . GLY C  1 300 ? 42.662  37.252  61.786  1.00 34.58  ? 300 GLY C O   1 
ATOM   9409  N  N   . GLU C  1 301 ? 43.445  37.749  59.752  1.00 32.99  ? 301 GLU C N   1 
ATOM   9410  C  CA  . GLU C  1 301 ? 42.229  38.429  59.356  1.00 32.26  ? 301 GLU C CA  1 
ATOM   9411  C  C   . GLU C  1 301 ? 40.999  37.584  59.540  1.00 32.53  ? 301 GLU C C   1 
ATOM   9412  O  O   . GLU C  1 301 ? 40.109  37.950  60.293  1.00 30.01  ? 301 GLU C O   1 
ATOM   9413  C  CB  . GLU C  1 301 ? 42.331  38.892  57.916  1.00 31.46  ? 301 GLU C CB  1 
ATOM   9414  C  CG  . GLU C  1 301 ? 43.269  40.048  57.799  1.00 39.30  ? 301 GLU C CG  1 
ATOM   9415  C  CD  . GLU C  1 301 ? 42.871  41.177  58.718  1.00 39.44  ? 301 GLU C CD  1 
ATOM   9416  O  OE1 . GLU C  1 301 ? 41.927  41.906  58.307  1.00 38.04  ? 301 GLU C OE1 1 
ATOM   9417  O  OE2 . GLU C  1 301 ? 43.482  41.297  59.826  1.00 38.31  ? 301 GLU C OE2 1 
ATOM   9418  N  N   . ALA C  1 302 ? 40.940  36.446  58.853  1.00 36.40  ? 302 ALA C N   1 
ATOM   9419  C  CA  . ALA C  1 302 ? 39.786  35.576  58.972  1.00 32.46  ? 302 ALA C CA  1 
ATOM   9420  C  C   . ALA C  1 302 ? 39.377  35.350  60.435  1.00 31.64  ? 302 ALA C C   1 
ATOM   9421  O  O   . ALA C  1 302 ? 38.269  35.741  60.825  1.00 31.90  ? 302 ALA C O   1 
ATOM   9422  C  CB  . ALA C  1 302 ? 40.048  34.294  58.284  1.00 41.21  ? 302 ALA C CB  1 
ATOM   9423  N  N   . MET C  1 303 ? 40.283  34.840  61.280  1.00 26.48  ? 303 MET C N   1 
ATOM   9424  C  CA  . MET C  1 303 ? 39.894  34.610  62.670  1.00 25.45  ? 303 MET C CA  1 
ATOM   9425  C  C   . MET C  1 303 ? 39.494  35.881  63.338  1.00 25.62  ? 303 MET C C   1 
ATOM   9426  O  O   . MET C  1 303 ? 38.547  35.892  64.127  1.00 24.92  ? 303 MET C O   1 
ATOM   9427  C  CB  . MET C  1 303 ? 40.951  33.903  63.511  1.00 21.76  ? 303 MET C CB  1 
ATOM   9428  C  CG  . MET C  1 303 ? 40.426  33.660  64.916  1.00 23.31  ? 303 MET C CG  1 
ATOM   9429  S  SD  . MET C  1 303 ? 41.094  32.268  65.647  1.00 33.89  ? 303 MET C SD  1 
ATOM   9430  C  CE  . MET C  1 303 ? 42.734  32.943  65.917  1.00 31.72  ? 303 MET C CE  1 
ATOM   9431  N  N   . ARG C  1 304 ? 40.189  36.962  62.994  1.00 29.85  ? 304 ARG C N   1 
ATOM   9432  C  CA  . ARG C  1 304 ? 39.911  38.267  63.553  1.00 31.29  ? 304 ARG C CA  1 
ATOM   9433  C  C   . ARG C  1 304 ? 38.472  38.669  63.299  1.00 33.69  ? 304 ARG C C   1 
ATOM   9434  O  O   . ARG C  1 304 ? 37.759  39.048  64.238  1.00 38.87  ? 304 ARG C O   1 
ATOM   9435  C  CB  . ARG C  1 304 ? 40.791  39.340  62.946  1.00 20.44  ? 304 ARG C CB  1 
ATOM   9436  C  CG  . ARG C  1 304 ? 40.901  40.509  63.896  1.00 27.93  ? 304 ARG C CG  1 
ATOM   9437  C  CD  . ARG C  1 304 ? 41.500  41.753  63.309  1.00 24.75  ? 304 ARG C CD  1 
ATOM   9438  N  NE  . ARG C  1 304 ? 40.456  42.578  62.736  1.00 32.55  ? 304 ARG C NE  1 
ATOM   9439  C  CZ  . ARG C  1 304 ? 40.420  42.914  61.455  1.00 33.75  ? 304 ARG C CZ  1 
ATOM   9440  N  NH1 . ARG C  1 304 ? 41.390  42.501  60.671  1.00 35.64  ? 304 ARG C NH1 1 
ATOM   9441  N  NH2 . ARG C  1 304 ? 39.376  43.556  60.941  1.00 36.74  ? 304 ARG C NH2 1 
ATOM   9442  N  N   . THR C  1 305 ? 38.035  38.553  62.043  1.00 34.06  ? 305 THR C N   1 
ATOM   9443  C  CA  . THR C  1 305 ? 36.665  38.935  61.686  1.00 31.57  ? 305 THR C CA  1 
ATOM   9444  C  C   . THR C  1 305 ? 35.659  38.110  62.409  1.00 34.11  ? 305 THR C C   1 
ATOM   9445  O  O   . THR C  1 305 ? 34.487  38.402  62.321  1.00 39.33  ? 305 THR C O   1 
ATOM   9446  C  CB  . THR C  1 305 ? 36.335  38.774  60.185  1.00 29.56  ? 305 THR C CB  1 
ATOM   9447  O  OG1 . THR C  1 305 ? 35.938  37.420  59.878  1.00 32.09  ? 305 THR C OG1 1 
ATOM   9448  C  CG2 . THR C  1 305 ? 37.525  39.207  59.336  1.00 31.29  ? 305 THR C CG2 1 
ATOM   9449  N  N   . LYS C  1 306 ? 36.107  37.034  63.053  1.00 35.78  ? 306 LYS C N   1 
ATOM   9450  C  CA  . LYS C  1 306 ? 35.201  36.183  63.747  1.00 27.51  ? 306 LYS C CA  1 
ATOM   9451  C  C   . LYS C  1 306 ? 35.272  36.256  65.245  1.00 29.89  ? 306 LYS C C   1 
ATOM   9452  O  O   . LYS C  1 306 ? 34.262  36.101  65.892  1.00 36.67  ? 306 LYS C O   1 
ATOM   9453  C  CB  . LYS C  1 306 ? 35.347  34.773  63.266  1.00 26.43  ? 306 LYS C CB  1 
ATOM   9454  C  CG  . LYS C  1 306 ? 34.044  34.227  62.817  1.00 24.29  ? 306 LYS C CG  1 
ATOM   9455  C  CD  . LYS C  1 306 ? 34.181  33.566  61.484  1.00 32.15  ? 306 LYS C CD  1 
ATOM   9456  C  CE  . LYS C  1 306 ? 32.832  33.303  60.846  1.00 36.37  ? 306 LYS C CE  1 
ATOM   9457  N  NZ  . LYS C  1 306 ? 32.124  34.516  60.328  1.00 49.85  ? 306 LYS C NZ  1 
ATOM   9458  N  N   . PHE C  1 307 ? 36.402  36.567  65.849  1.00 27.98  ? 307 PHE C N   1 
ATOM   9459  C  CA  . PHE C  1 307 ? 36.370  36.568  67.303  1.00 26.03  ? 307 PHE C CA  1 
ATOM   9460  C  C   . PHE C  1 307 ? 36.669  37.871  67.960  1.00 28.36  ? 307 PHE C C   1 
ATOM   9461  O  O   . PHE C  1 307 ? 36.417  38.024  69.157  1.00 29.46  ? 307 PHE C O   1 
ATOM   9462  C  CB  . PHE C  1 307 ? 37.312  35.482  67.857  1.00 28.80  ? 307 PHE C CB  1 
ATOM   9463  C  CG  . PHE C  1 307 ? 36.900  34.091  67.503  1.00 26.99  ? 307 PHE C CG  1 
ATOM   9464  C  CD1 . PHE C  1 307 ? 35.555  33.779  67.329  1.00 26.16  ? 307 PHE C CD1 1 
ATOM   9465  C  CD2 . PHE C  1 307 ? 37.841  33.088  67.331  1.00 32.61  ? 307 PHE C CD2 1 
ATOM   9466  C  CE1 . PHE C  1 307 ? 35.143  32.477  66.978  1.00 28.82  ? 307 PHE C CE1 1 
ATOM   9467  C  CE2 . PHE C  1 307 ? 37.434  31.757  66.977  1.00 25.57  ? 307 PHE C CE2 1 
ATOM   9468  C  CZ  . PHE C  1 307 ? 36.093  31.459  66.802  1.00 25.54  ? 307 PHE C CZ  1 
ATOM   9469  N  N   . GLU C  1 308 ? 37.135  38.847  67.188  1.00 33.76  ? 308 GLU C N   1 
ATOM   9470  C  CA  . GLU C  1 308 ? 37.521  40.129  67.780  1.00 34.18  ? 308 GLU C CA  1 
ATOM   9471  C  C   . GLU C  1 308 ? 36.478  40.768  68.634  1.00 32.93  ? 308 GLU C C   1 
ATOM   9472  O  O   . GLU C  1 308 ? 36.745  41.120  69.778  1.00 36.06  ? 308 GLU C O   1 
ATOM   9473  C  CB  . GLU C  1 308 ? 38.053  41.165  66.786  1.00 35.38  ? 308 GLU C CB  1 
ATOM   9474  C  CG  . GLU C  1 308 ? 38.558  42.379  67.584  1.00 34.89  ? 308 GLU C CG  1 
ATOM   9475  C  CD  . GLU C  1 308 ? 39.415  43.337  66.828  1.00 36.68  ? 308 GLU C CD  1 
ATOM   9476  O  OE1 . GLU C  1 308 ? 39.329  43.371  65.579  1.00 33.59  ? 308 GLU C OE1 1 
ATOM   9477  O  OE2 . GLU C  1 308 ? 40.152  44.090  67.523  1.00 44.64  ? 308 GLU C OE2 1 
ATOM   9478  N  N   . ALA C  1 309 ? 35.293  40.961  68.090  1.00 28.71  ? 309 ALA C N   1 
ATOM   9479  C  CA  . ALA C  1 309 ? 34.261  41.562  68.911  1.00 30.43  ? 309 ALA C CA  1 
ATOM   9480  C  C   . ALA C  1 309 ? 34.032  40.851  70.244  1.00 35.04  ? 309 ALA C C   1 
ATOM   9481  O  O   . ALA C  1 309 ? 33.810  41.526  71.268  1.00 38.78  ? 309 ALA C O   1 
ATOM   9482  C  CB  . ALA C  1 309 ? 33.009  41.621  68.183  1.00 34.80  ? 309 ALA C CB  1 
ATOM   9483  N  N   . TRP C  1 310 ? 34.108  39.510  70.239  1.00 30.54  ? 310 TRP C N   1 
ATOM   9484  C  CA  . TRP C  1 310 ? 33.891  38.744  71.445  1.00 26.71  ? 310 TRP C CA  1 
ATOM   9485  C  C   . TRP C  1 310 ? 34.926  39.131  72.460  1.00 24.24  ? 310 TRP C C   1 
ATOM   9486  O  O   . TRP C  1 310 ? 34.626  39.444  73.606  1.00 25.77  ? 310 TRP C O   1 
ATOM   9487  C  CB  . TRP C  1 310 ? 33.968  37.253  71.172  1.00 31.05  ? 310 TRP C CB  1 
ATOM   9488  C  CG  . TRP C  1 310 ? 32.841  36.747  70.365  1.00 38.10  ? 310 TRP C CG  1 
ATOM   9489  C  CD1 . TRP C  1 310 ? 31.884  37.497  69.759  1.00 41.21  ? 310 TRP C CD1 1 
ATOM   9490  C  CD2 . TRP C  1 310 ? 32.587  35.378  69.969  1.00 43.71  ? 310 TRP C CD2 1 
ATOM   9491  N  NE1 . TRP C  1 310 ? 31.055  36.694  68.984  1.00 46.81  ? 310 TRP C NE1 1 
ATOM   9492  C  CE2 . TRP C  1 310 ? 31.465  35.391  69.089  1.00 44.71  ? 310 TRP C CE2 1 
ATOM   9493  C  CE3 . TRP C  1 310 ? 33.198  34.154  70.254  1.00 40.72  ? 310 TRP C CE3 1 
ATOM   9494  C  CZ2 . TRP C  1 310 ? 30.950  34.218  68.485  1.00 34.61  ? 310 TRP C CZ2 1 
ATOM   9495  C  CZ3 . TRP C  1 310 ? 32.673  32.988  69.646  1.00 39.77  ? 310 TRP C CZ3 1 
ATOM   9496  C  CH2 . TRP C  1 310 ? 31.562  33.042  68.772  1.00 32.79  ? 310 TRP C CH2 1 
ATOM   9497  N  N   . PHE C  1 311 ? 36.154  39.175  72.014  1.00 25.48  ? 311 PHE C N   1 
ATOM   9498  C  CA  . PHE C  1 311 ? 37.234  39.533  72.908  1.00 31.89  ? 311 PHE C CA  1 
ATOM   9499  C  C   . PHE C  1 311 ? 36.977  40.874  73.540  1.00 35.08  ? 311 PHE C C   1 
ATOM   9500  O  O   . PHE C  1 311 ? 37.066  41.000  74.758  1.00 39.16  ? 311 PHE C O   1 
ATOM   9501  C  CB  . PHE C  1 311 ? 38.575  39.551  72.151  1.00 33.20  ? 311 PHE C CB  1 
ATOM   9502  C  CG  . PHE C  1 311 ? 38.954  38.220  71.559  1.00 37.31  ? 311 PHE C CG  1 
ATOM   9503  C  CD1 . PHE C  1 311 ? 38.278  37.050  71.930  1.00 39.17  ? 311 PHE C CD1 1 
ATOM   9504  C  CD2 . PHE C  1 311 ? 39.963  38.127  70.631  1.00 35.72  ? 311 PHE C CD2 1 
ATOM   9505  C  CE1 . PHE C  1 311 ? 38.605  35.835  71.383  1.00 34.85  ? 311 PHE C CE1 1 
ATOM   9506  C  CE2 . PHE C  1 311 ? 40.296  36.880  70.074  1.00 36.21  ? 311 PHE C CE2 1 
ATOM   9507  C  CZ  . PHE C  1 311 ? 39.617  35.749  70.450  1.00 35.46  ? 311 PHE C CZ  1 
ATOM   9508  N  N   . VAL C  1 312 ? 36.633  41.864  72.713  1.00 37.08  ? 312 VAL C N   1 
ATOM   9509  C  CA  . VAL C  1 312 ? 36.390  43.212  73.192  1.00 35.30  ? 312 VAL C CA  1 
ATOM   9510  C  C   . VAL C  1 312 ? 35.195  43.198  74.094  1.00 38.33  ? 312 VAL C C   1 
ATOM   9511  O  O   . VAL C  1 312 ? 35.234  43.725  75.213  1.00 40.58  ? 312 VAL C O   1 
ATOM   9512  C  CB  . VAL C  1 312 ? 36.134  44.191  72.085  1.00 32.04  ? 312 VAL C CB  1 
ATOM   9513  C  CG1 . VAL C  1 312 ? 35.908  45.522  72.680  1.00 31.11  ? 312 VAL C CG1 1 
ATOM   9514  C  CG2 . VAL C  1 312 ? 37.318  44.273  71.184  1.00 33.00  ? 312 VAL C CG2 1 
ATOM   9515  N  N   . LYS C  1 313 ? 34.148  42.539  73.632  1.00 35.85  ? 313 LYS C N   1 
ATOM   9516  C  CA  . LYS C  1 313 ? 32.951  42.449  74.420  1.00 40.04  ? 313 LYS C CA  1 
ATOM   9517  C  C   . LYS C  1 313 ? 33.189  41.892  75.824  1.00 45.02  ? 313 LYS C C   1 
ATOM   9518  O  O   . LYS C  1 313 ? 32.541  42.331  76.774  1.00 49.92  ? 313 LYS C O   1 
ATOM   9519  C  CB  . LYS C  1 313 ? 31.957  41.599  73.708  1.00 36.88  ? 313 LYS C CB  1 
ATOM   9520  C  CG  . LYS C  1 313 ? 30.789  41.243  74.545  1.00 46.76  ? 313 LYS C CG  1 
ATOM   9521  C  CD  . LYS C  1 313 ? 29.763  40.555  73.656  1.00 64.31  ? 313 LYS C CD  1 
ATOM   9522  C  CE  . LYS C  1 313 ? 28.589  39.981  74.443  1.00 70.74  ? 313 LYS C CE  1 
ATOM   9523  N  NZ  . LYS C  1 313 ? 27.936  41.000  75.350  1.00 77.56  ? 313 LYS C NZ  1 
ATOM   9524  N  N   . TYR C  1 314 ? 34.107  40.932  75.971  1.00 44.69  ? 314 TYR C N   1 
ATOM   9525  C  CA  . TYR C  1 314 ? 34.369  40.341  77.284  1.00 39.24  ? 314 TYR C CA  1 
ATOM   9526  C  C   . TYR C  1 314 ? 35.573  40.898  77.981  1.00 41.31  ? 314 TYR C C   1 
ATOM   9527  O  O   . TYR C  1 314 ? 36.006  40.410  79.030  1.00 44.76  ? 314 TYR C O   1 
ATOM   9528  C  CB  . TYR C  1 314 ? 34.477  38.843  77.154  1.00 34.24  ? 314 TYR C CB  1 
ATOM   9529  C  CG  . TYR C  1 314 ? 33.145  38.214  76.856  1.00 33.66  ? 314 TYR C CG  1 
ATOM   9530  C  CD1 . TYR C  1 314 ? 32.681  38.056  75.554  1.00 33.15  ? 314 TYR C CD1 1 
ATOM   9531  C  CD2 . TYR C  1 314 ? 32.335  37.793  77.892  1.00 34.03  ? 314 TYR C CD2 1 
ATOM   9532  C  CE1 . TYR C  1 314 ? 31.437  37.487  75.306  1.00 34.36  ? 314 TYR C CE1 1 
ATOM   9533  C  CE2 . TYR C  1 314 ? 31.104  37.235  77.670  1.00 32.76  ? 314 TYR C CE2 1 
ATOM   9534  C  CZ  . TYR C  1 314 ? 30.648  37.076  76.389  1.00 40.06  ? 314 TYR C CZ  1 
ATOM   9535  O  OH  . TYR C  1 314 ? 29.400  36.486  76.239  1.00 47.46  ? 314 TYR C OH  1 
ATOM   9536  N  N   . LYS C  1 315 ? 36.138  41.918  77.378  1.00 42.59  ? 315 LYS C N   1 
ATOM   9537  C  CA  . LYS C  1 315 ? 37.290  42.553  77.972  1.00 47.33  ? 315 LYS C CA  1 
ATOM   9538  C  C   . LYS C  1 315 ? 38.444  41.591  78.238  1.00 42.99  ? 315 LYS C C   1 
ATOM   9539  O  O   . LYS C  1 315 ? 39.028  41.641  79.301  1.00 44.87  ? 315 LYS C O   1 
ATOM   9540  C  CB  . LYS C  1 315 ? 36.860  43.259  79.265  1.00 53.33  ? 315 LYS C CB  1 
ATOM   9541  C  CG  . LYS C  1 315 ? 35.864  44.356  79.002  1.00 66.89  ? 315 LYS C CG  1 
ATOM   9542  C  CD  . LYS C  1 315 ? 34.827  44.435  80.086  1.00 80.91  ? 315 LYS C CD  1 
ATOM   9543  C  CE  . LYS C  1 315 ? 34.914  45.772  80.844  1.00 93.57  ? 315 LYS C CE  1 
ATOM   9544  N  NZ  . LYS C  1 315 ? 34.702  47.026  80.011  1.00 102.26 ? 315 LYS C NZ  1 
ATOM   9545  N  N   . VAL C  1 316 ? 38.835  40.757  77.279  1.00 37.58  ? 316 VAL C N   1 
ATOM   9546  C  CA  . VAL C  1 316 ? 39.944  39.859  77.571  1.00 32.11  ? 316 VAL C CA  1 
ATOM   9547  C  C   . VAL C  1 316 ? 41.172  40.743  77.697  1.00 32.43  ? 316 VAL C C   1 
ATOM   9548  O  O   . VAL C  1 316 ? 41.313  41.698  76.945  1.00 32.62  ? 316 VAL C O   1 
ATOM   9549  C  CB  . VAL C  1 316 ? 40.147  38.714  76.515  1.00 28.53  ? 316 VAL C CB  1 
ATOM   9550  C  CG1 . VAL C  1 316 ? 38.910  38.484  75.662  1.00 19.34  ? 316 VAL C CG1 1 
ATOM   9551  C  CG2 . VAL C  1 316 ? 41.315  38.987  75.676  1.00 31.11  ? 316 VAL C CG2 1 
ATOM   9552  N  N   . ASP C  1 317 ? 41.990  40.482  78.710  1.00 30.44  ? 317 ASP C N   1 
ATOM   9553  C  CA  . ASP C  1 317 ? 43.202  41.237  78.959  1.00 30.32  ? 317 ASP C CA  1 
ATOM   9554  C  C   . ASP C  1 317 ? 44.306  41.193  77.926  1.00 36.95  ? 317 ASP C C   1 
ATOM   9555  O  O   . ASP C  1 317 ? 44.723  42.267  77.481  1.00 43.61  ? 317 ASP C O   1 
ATOM   9556  C  CB  . ASP C  1 317 ? 43.767  40.823  80.267  1.00 30.08  ? 317 ASP C CB  1 
ATOM   9557  C  CG  . ASP C  1 317 ? 42.983  41.332  81.370  1.00 35.56  ? 317 ASP C CG  1 
ATOM   9558  O  OD1 . ASP C  1 317 ? 43.141  42.553  81.619  1.00 40.94  ? 317 ASP C OD1 1 
ATOM   9559  O  OD2 . ASP C  1 317 ? 42.208  40.534  81.947  1.00 38.22  ? 317 ASP C OD2 1 
ATOM   9560  N  N   . VAL C  1 318 ? 44.820  39.989  77.592  1.00 36.47  ? 318 VAL C N   1 
ATOM   9561  C  CA  . VAL C  1 318 ? 45.917  39.805  76.599  1.00 28.36  ? 318 VAL C CA  1 
ATOM   9562  C  C   . VAL C  1 318 ? 45.599  38.684  75.631  1.00 28.13  ? 318 VAL C C   1 
ATOM   9563  O  O   . VAL C  1 318 ? 44.826  37.789  75.956  1.00 28.17  ? 318 VAL C O   1 
ATOM   9564  C  CB  . VAL C  1 318 ? 47.223  39.316  77.230  1.00 26.47  ? 318 VAL C CB  1 
ATOM   9565  C  CG1 . VAL C  1 318 ? 48.373  40.093  76.711  1.00 24.44  ? 318 VAL C CG1 1 
ATOM   9566  C  CG2 . VAL C  1 318 ? 47.146  39.307  78.716  1.00 24.93  ? 318 VAL C CG2 1 
ATOM   9567  N  N   . VAL C  1 319 ? 46.244  38.692  74.471  1.00 23.50  ? 319 VAL C N   1 
ATOM   9568  C  CA  . VAL C  1 319 ? 46.043  37.620  73.534  1.00 23.73  ? 319 VAL C CA  1 
ATOM   9569  C  C   . VAL C  1 319 ? 47.423  37.344  73.030  1.00 30.63  ? 319 VAL C C   1 
ATOM   9570  O  O   . VAL C  1 319 ? 47.965  38.168  72.273  1.00 32.73  ? 319 VAL C O   1 
ATOM   9571  C  CB  . VAL C  1 319 ? 45.173  38.018  72.370  1.00 22.35  ? 319 VAL C CB  1 
ATOM   9572  C  CG1 . VAL C  1 319 ? 45.233  36.967  71.296  1.00 22.62  ? 319 VAL C CG1 1 
ATOM   9573  C  CG2 . VAL C  1 319 ? 43.781  38.186  72.817  1.00 18.37  ? 319 VAL C CG2 1 
ATOM   9574  N  N   . PHE C  1 320 ? 48.020  36.234  73.490  1.00 29.01  ? 320 PHE C N   1 
ATOM   9575  C  CA  . PHE C  1 320 ? 49.348  35.862  73.052  1.00 20.76  ? 320 PHE C CA  1 
ATOM   9576  C  C   . PHE C  1 320 ? 49.336  34.981  71.807  1.00 20.52  ? 320 PHE C C   1 
ATOM   9577  O  O   . PHE C  1 320 ? 48.457  34.112  71.695  1.00 20.38  ? 320 PHE C O   1 
ATOM   9578  C  CB  . PHE C  1 320 ? 50.027  35.175  74.174  1.00 13.78  ? 320 PHE C CB  1 
ATOM   9579  C  CG  . PHE C  1 320 ? 50.156  36.006  75.375  1.00 16.92  ? 320 PHE C CG  1 
ATOM   9580  C  CD1 . PHE C  1 320 ? 51.144  36.990  75.457  1.00 23.69  ? 320 PHE C CD1 1 
ATOM   9581  C  CD2 . PHE C  1 320 ? 49.396  35.743  76.473  1.00 14.45  ? 320 PHE C CD2 1 
ATOM   9582  C  CE1 . PHE C  1 320 ? 51.380  37.698  76.658  1.00 21.74  ? 320 PHE C CE1 1 
ATOM   9583  C  CE2 . PHE C  1 320 ? 49.617  36.437  77.670  1.00 20.62  ? 320 PHE C CE2 1 
ATOM   9584  C  CZ  . PHE C  1 320 ? 50.609  37.409  77.762  1.00 19.33  ? 320 PHE C CZ  1 
ATOM   9585  N  N   . ALA C  1 321 ? 50.254  35.249  70.855  1.00 15.98  ? 321 ALA C N   1 
ATOM   9586  C  CA  . ALA C  1 321 ? 50.357  34.457  69.632  1.00 14.14  ? 321 ALA C CA  1 
ATOM   9587  C  C   . ALA C  1 321 ? 51.811  34.269  69.265  1.00 19.37  ? 321 ALA C C   1 
ATOM   9588  O  O   . ALA C  1 321 ? 52.699  34.842  69.899  1.00 27.62  ? 321 ALA C O   1 
ATOM   9589  C  CB  . ALA C  1 321 ? 49.652  35.114  68.543  1.00 18.08  ? 321 ALA C CB  1 
ATOM   9590  N  N   . GLY C  1 322 ? 52.076  33.429  68.274  1.00 19.78  ? 322 GLY C N   1 
ATOM   9591  C  CA  . GLY C  1 322 ? 53.447  33.211  67.847  1.00 21.62  ? 322 GLY C CA  1 
ATOM   9592  C  C   . GLY C  1 322 ? 53.382  33.370  66.349  1.00 23.46  ? 322 GLY C C   1 
ATOM   9593  O  O   . GLY C  1 322 ? 52.824  34.338  65.875  1.00 26.41  ? 322 GLY C O   1 
ATOM   9594  N  N   . HIS C  1 323 ? 53.923  32.419  65.607  1.00 21.36  ? 323 HIS C N   1 
ATOM   9595  C  CA  . HIS C  1 323 ? 53.893  32.439  64.156  1.00 21.05  ? 323 HIS C CA  1 
ATOM   9596  C  C   . HIS C  1 323 ? 54.843  33.431  63.487  1.00 23.17  ? 323 HIS C C   1 
ATOM   9597  O  O   . HIS C  1 323 ? 55.443  33.140  62.483  1.00 31.57  ? 323 HIS C O   1 
ATOM   9598  C  CB  . HIS C  1 323 ? 52.449  32.569  63.688  1.00 16.86  ? 323 HIS C CB  1 
ATOM   9599  C  CG  . HIS C  1 323 ? 52.212  32.037  62.314  1.00 18.20  ? 323 HIS C CG  1 
ATOM   9600  N  ND1 . HIS C  1 323 ? 52.635  30.790  61.904  1.00 21.95  ? 323 HIS C ND1 1 
ATOM   9601  C  CD2 . HIS C  1 323 ? 51.572  32.580  61.262  1.00 20.71  ? 323 HIS C CD2 1 
ATOM   9602  C  CE1 . HIS C  1 323 ? 52.267  30.603  60.659  1.00 27.33  ? 323 HIS C CE1 1 
ATOM   9603  N  NE2 . HIS C  1 323 ? 51.614  31.677  60.244  1.00 23.05  ? 323 HIS C NE2 1 
ATOM   9604  N  N   . VAL C  1 324 ? 54.946  34.644  63.968  1.00 22.67  ? 324 VAL C N   1 
ATOM   9605  C  CA  . VAL C  1 324 ? 55.899  35.521  63.349  1.00 22.55  ? 324 VAL C CA  1 
ATOM   9606  C  C   . VAL C  1 324 ? 57.135  35.444  64.247  1.00 26.05  ? 324 VAL C C   1 
ATOM   9607  O  O   . VAL C  1 324 ? 57.050  35.626  65.455  1.00 32.77  ? 324 VAL C O   1 
ATOM   9608  C  CB  . VAL C  1 324 ? 55.339  36.904  63.274  1.00 23.87  ? 324 VAL C CB  1 
ATOM   9609  C  CG1 . VAL C  1 324 ? 56.381  37.857  62.763  1.00 22.01  ? 324 VAL C CG1 1 
ATOM   9610  C  CG2 . VAL C  1 324 ? 54.119  36.894  62.398  1.00 23.36  ? 324 VAL C CG2 1 
ATOM   9611  N  N   . HIS C  1 325 ? 58.256  35.054  63.680  1.00 25.55  ? 325 HIS C N   1 
ATOM   9612  C  CA  . HIS C  1 325 ? 59.479  34.896  64.443  1.00 26.06  ? 325 HIS C CA  1 
ATOM   9613  C  C   . HIS C  1 325 ? 60.115  36.214  64.823  1.00 26.89  ? 325 HIS C C   1 
ATOM   9614  O  O   . HIS C  1 325 ? 61.185  36.556  64.343  1.00 29.22  ? 325 HIS C O   1 
ATOM   9615  C  CB  . HIS C  1 325 ? 60.448  33.972  63.677  1.00 29.21  ? 325 HIS C CB  1 
ATOM   9616  C  CG  . HIS C  1 325 ? 59.824  32.666  63.249  1.00 28.37  ? 325 HIS C CG  1 
ATOM   9617  N  ND1 . HIS C  1 325 ? 60.208  31.992  62.107  1.00 22.70  ? 325 HIS C ND1 1 
ATOM   9618  C  CD2 . HIS C  1 325 ? 58.814  31.931  63.799  1.00 23.88  ? 325 HIS C CD2 1 
ATOM   9619  C  CE1 . HIS C  1 325 ? 59.459  30.904  61.980  1.00 26.20  ? 325 HIS C CE1 1 
ATOM   9620  N  NE2 . HIS C  1 325 ? 58.606  30.847  62.990  1.00 20.55  ? 325 HIS C NE2 1 
ATOM   9621  N  N   . ALA C  1 326 ? 59.473  36.913  65.751  1.00 25.12  ? 326 ALA C N   1 
ATOM   9622  C  CA  . ALA C  1 326 ? 59.921  38.221  66.203  1.00 23.73  ? 326 ALA C CA  1 
ATOM   9623  C  C   . ALA C  1 326 ? 58.997  38.604  67.326  1.00 20.91  ? 326 ALA C C   1 
ATOM   9624  O  O   . ALA C  1 326 ? 58.135  37.800  67.668  1.00 19.11  ? 326 ALA C O   1 
ATOM   9625  C  CB  . ALA C  1 326 ? 59.808  39.213  65.079  1.00 24.56  ? 326 ALA C CB  1 
ATOM   9626  N  N   . TYR C  1 327 ? 59.186  39.792  67.904  1.00 20.80  ? 327 TYR C N   1 
ATOM   9627  C  CA  . TYR C  1 327 ? 58.361  40.272  69.017  1.00 23.06  ? 327 TYR C CA  1 
ATOM   9628  C  C   . TYR C  1 327 ? 57.611  41.516  68.619  1.00 26.49  ? 327 TYR C C   1 
ATOM   9629  O  O   . TYR C  1 327 ? 58.112  42.314  67.828  1.00 28.93  ? 327 TYR C O   1 
ATOM   9630  C  CB  . TYR C  1 327 ? 59.243  40.618  70.195  1.00 20.94  ? 327 TYR C CB  1 
ATOM   9631  C  CG  . TYR C  1 327 ? 58.540  41.296  71.331  1.00 22.14  ? 327 TYR C CG  1 
ATOM   9632  C  CD1 . TYR C  1 327 ? 57.545  40.656  72.042  1.00 26.89  ? 327 TYR C CD1 1 
ATOM   9633  C  CD2 . TYR C  1 327 ? 58.925  42.554  71.742  1.00 22.88  ? 327 TYR C CD2 1 
ATOM   9634  C  CE1 . TYR C  1 327 ? 56.948  41.252  73.159  1.00 29.48  ? 327 TYR C CE1 1 
ATOM   9635  C  CE2 . TYR C  1 327 ? 58.345  43.159  72.846  1.00 27.62  ? 327 TYR C CE2 1 
ATOM   9636  C  CZ  . TYR C  1 327 ? 57.354  42.505  73.558  1.00 31.79  ? 327 TYR C CZ  1 
ATOM   9637  O  OH  . TYR C  1 327 ? 56.811  43.140  74.669  1.00 34.29  ? 327 TYR C OH  1 
ATOM   9638  N  N   . GLU C  1 328 ? 56.431  41.707  69.200  1.00 27.03  ? 328 GLU C N   1 
ATOM   9639  C  CA  . GLU C  1 328 ? 55.590  42.864  68.912  1.00 26.54  ? 328 GLU C CA  1 
ATOM   9640  C  C   . GLU C  1 328 ? 54.548  42.969  70.006  1.00 31.34  ? 328 GLU C C   1 
ATOM   9641  O  O   . GLU C  1 328 ? 54.107  41.972  70.529  1.00 37.39  ? 328 GLU C O   1 
ATOM   9642  C  CB  . GLU C  1 328 ? 54.915  42.739  67.541  1.00 20.15  ? 328 GLU C CB  1 
ATOM   9643  C  CG  . GLU C  1 328 ? 53.786  43.717  67.317  1.00 27.01  ? 328 GLU C CG  1 
ATOM   9644  C  CD  . GLU C  1 328 ? 53.588  44.110  65.839  1.00 33.81  ? 328 GLU C CD  1 
ATOM   9645  O  OE1 . GLU C  1 328 ? 53.712  43.249  64.945  1.00 36.42  ? 328 GLU C OE1 1 
ATOM   9646  O  OE2 . GLU C  1 328 ? 53.270  45.288  65.567  1.00 34.82  ? 328 GLU C OE2 1 
ATOM   9647  N  N   . ARG C  1 329 ? 54.196  44.189  70.380  1.00 37.33  ? 329 ARG C N   1 
ATOM   9648  C  CA  . ARG C  1 329 ? 53.212  44.449  71.418  1.00 36.97  ? 329 ARG C CA  1 
ATOM   9649  C  C   . ARG C  1 329 ? 52.306  45.521  70.877  1.00 40.64  ? 329 ARG C C   1 
ATOM   9650  O  O   . ARG C  1 329 ? 52.773  46.429  70.200  1.00 47.68  ? 329 ARG C O   1 
ATOM   9651  C  CB  . ARG C  1 329 ? 53.893  45.009  72.648  1.00 35.09  ? 329 ARG C CB  1 
ATOM   9652  C  CG  . ARG C  1 329 ? 52.974  45.038  73.824  1.00 34.59  ? 329 ARG C CG  1 
ATOM   9653  C  CD  . ARG C  1 329 ? 53.707  45.490  75.035  1.00 35.36  ? 329 ARG C CD  1 
ATOM   9654  N  NE  . ARG C  1 329 ? 53.737  46.937  75.084  1.00 42.90  ? 329 ARG C NE  1 
ATOM   9655  C  CZ  . ARG C  1 329 ? 54.849  47.653  75.052  1.00 40.78  ? 329 ARG C CZ  1 
ATOM   9656  N  NH1 . ARG C  1 329 ? 56.020  47.049  74.952  1.00 43.03  ? 329 ARG C NH1 1 
ATOM   9657  N  NH2 . ARG C  1 329 ? 54.774  48.964  75.205  1.00 38.52  ? 329 ARG C NH2 1 
ATOM   9658  N  N   . SER C  1 330 ? 51.033  45.473  71.215  1.00 41.33  ? 330 SER C N   1 
ATOM   9659  C  CA  . SER C  1 330 ? 50.121  46.460  70.696  1.00 44.02  ? 330 SER C CA  1 
ATOM   9660  C  C   . SER C  1 330 ? 49.502  47.372  71.679  1.00 45.15  ? 330 SER C C   1 
ATOM   9661  O  O   . SER C  1 330 ? 49.861  47.386  72.878  1.00 48.50  ? 330 SER C O   1 
ATOM   9662  C  CB  . SER C  1 330 ? 49.042  45.792  69.878  1.00 38.41  ? 330 SER C CB  1 
ATOM   9663  O  OG  . SER C  1 330 ? 49.674  45.406  68.667  1.00 55.46  ? 330 SER C OG  1 
ATOM   9664  N  N   . GLU C  1 331 ? 48.671  48.234  71.118  1.00 44.35  ? 331 GLU C N   1 
ATOM   9665  C  CA  . GLU C  1 331 ? 47.910  49.172  71.891  1.00 45.95  ? 331 GLU C CA  1 
ATOM   9666  C  C   . GLU C  1 331 ? 46.552  48.508  72.090  1.00 39.33  ? 331 GLU C C   1 
ATOM   9667  O  O   . GLU C  1 331 ? 46.177  47.638  71.333  1.00 37.10  ? 331 GLU C O   1 
ATOM   9668  C  CB  . GLU C  1 331 ? 47.737  50.476  71.099  1.00 52.92  ? 331 GLU C CB  1 
ATOM   9669  C  CG  . GLU C  1 331 ? 49.011  51.323  70.923  1.00 62.81  ? 331 GLU C CG  1 
ATOM   9670  C  CD  . GLU C  1 331 ? 49.579  51.916  72.236  1.00 71.38  ? 331 GLU C CD  1 
ATOM   9671  O  OE1 . GLU C  1 331 ? 49.148  51.511  73.357  1.00 75.95  ? 331 GLU C OE1 1 
ATOM   9672  O  OE2 . GLU C  1 331 ? 50.486  52.784  72.140  1.00 75.97  ? 331 GLU C OE2 1 
ATOM   9673  N  N   . ARG C  1 332 ? 45.843  48.852  73.145  1.00 34.26  ? 332 ARG C N   1 
ATOM   9674  C  CA  . ARG C  1 332 ? 44.526  48.287  73.290  1.00 33.39  ? 332 ARG C CA  1 
ATOM   9675  C  C   . ARG C  1 332 ? 43.825  48.921  72.119  1.00 33.69  ? 332 ARG C C   1 
ATOM   9676  O  O   . ARG C  1 332 ? 43.674  50.127  72.053  1.00 37.51  ? 332 ARG C O   1 
ATOM   9677  C  CB  . ARG C  1 332 ? 43.915  48.660  74.627  1.00 31.27  ? 332 ARG C CB  1 
ATOM   9678  C  CG  . ARG C  1 332 ? 44.670  47.987  75.752  1.00 32.71  ? 332 ARG C CG  1 
ATOM   9679  C  CD  . ARG C  1 332 ? 43.931  48.048  76.997  1.00 29.45  ? 332 ARG C CD  1 
ATOM   9680  N  NE  . ARG C  1 332 ? 44.632  47.331  78.032  1.00 38.05  ? 332 ARG C NE  1 
ATOM   9681  C  CZ  . ARG C  1 332 ? 44.489  46.033  78.239  1.00 38.53  ? 332 ARG C CZ  1 
ATOM   9682  N  NH1 . ARG C  1 332 ? 43.671  45.349  77.423  1.00 34.81  ? 332 ARG C NH1 1 
ATOM   9683  N  NH2 . ARG C  1 332 ? 45.054  45.454  79.323  1.00 37.45  ? 332 ARG C NH2 1 
ATOM   9684  N  N   . VAL C  1 333 ? 43.425  48.092  71.182  1.00 30.01  ? 333 VAL C N   1 
ATOM   9685  C  CA  . VAL C  1 333 ? 42.869  48.567  69.971  1.00 26.05  ? 333 VAL C CA  1 
ATOM   9686  C  C   . VAL C  1 333 ? 41.811  47.623  69.508  1.00 31.24  ? 333 VAL C C   1 
ATOM   9687  O  O   . VAL C  1 333 ? 41.891  46.411  69.730  1.00 36.37  ? 333 VAL C O   1 
ATOM   9688  C  CB  . VAL C  1 333 ? 44.003  48.544  68.966  1.00 28.11  ? 333 VAL C CB  1 
ATOM   9689  C  CG1 . VAL C  1 333 ? 43.500  48.504  67.578  1.00 27.92  ? 333 VAL C CG1 1 
ATOM   9690  C  CG2 . VAL C  1 333 ? 44.889  49.721  69.181  1.00 21.94  ? 333 VAL C CG2 1 
ATOM   9691  N  N   . SER C  1 334 ? 40.833  48.169  68.805  1.00 32.08  ? 334 SER C N   1 
ATOM   9692  C  CA  . SER C  1 334 ? 39.762  47.355  68.254  1.00 36.16  ? 334 SER C CA  1 
ATOM   9693  C  C   . SER C  1 334 ? 39.595  47.797  66.814  1.00 38.36  ? 334 SER C C   1 
ATOM   9694  O  O   . SER C  1 334 ? 40.105  48.860  66.444  1.00 45.60  ? 334 SER C O   1 
ATOM   9695  C  CB  . SER C  1 334 ? 38.469  47.637  69.004  1.00 40.89  ? 334 SER C CB  1 
ATOM   9696  O  OG  . SER C  1 334 ? 37.637  48.548  68.308  1.00 46.82  ? 334 SER C OG  1 
ATOM   9697  N  N   . ASN C  1 335 ? 38.897  47.018  65.998  1.00 35.24  ? 335 ASN C N   1 
ATOM   9698  C  CA  . ASN C  1 335 ? 38.649  47.398  64.602  1.00 36.00  ? 335 ASN C CA  1 
ATOM   9699  C  C   . ASN C  1 335 ? 37.362  46.679  64.265  1.00 37.03  ? 335 ASN C C   1 
ATOM   9700  O  O   . ASN C  1 335 ? 37.248  45.932  63.281  1.00 36.80  ? 335 ASN C O   1 
ATOM   9701  C  CB  . ASN C  1 335 ? 39.790  46.945  63.672  1.00 39.65  ? 335 ASN C CB  1 
ATOM   9702  C  CG  . ASN C  1 335 ? 39.526  47.289  62.197  1.00 45.09  ? 335 ASN C CG  1 
ATOM   9703  O  OD1 . ASN C  1 335 ? 38.508  47.923  61.865  1.00 56.73  ? 335 ASN C OD1 1 
ATOM   9704  N  ND2 . ASN C  1 335 ? 40.428  46.861  61.309  1.00 41.33  ? 335 ASN C ND2 1 
ATOM   9705  N  N   . ILE C  1 336 ? 36.354  46.941  65.074  1.00 39.19  ? 336 ILE C N   1 
ATOM   9706  C  CA  . ILE C  1 336 ? 35.119  46.218  64.911  1.00 38.97  ? 336 ILE C CA  1 
ATOM   9707  C  C   . ILE C  1 336 ? 33.937  46.992  64.428  1.00 44.78  ? 336 ILE C C   1 
ATOM   9708  O  O   . ILE C  1 336 ? 32.827  46.652  64.808  1.00 53.38  ? 336 ILE C O   1 
ATOM   9709  C  CB  . ILE C  1 336 ? 34.742  45.544  66.251  1.00 36.19  ? 336 ILE C CB  1 
ATOM   9710  C  CG1 . ILE C  1 336 ? 34.595  46.612  67.313  1.00 30.81  ? 336 ILE C CG1 1 
ATOM   9711  C  CG2 . ILE C  1 336 ? 35.857  44.585  66.706  1.00 35.88  ? 336 ILE C CG2 1 
ATOM   9712  C  CD1 . ILE C  1 336 ? 34.465  46.041  68.654  1.00 33.35  ? 336 ILE C CD1 1 
ATOM   9713  N  N   . ALA C  1 337 ? 34.133  47.970  63.541  1.00 47.75  ? 337 ALA C N   1 
ATOM   9714  C  CA  . ALA C  1 337 ? 33.001  48.786  63.078  1.00 44.57  ? 337 ALA C CA  1 
ATOM   9715  C  C   . ALA C  1 337 ? 32.685  48.680  61.601  1.00 45.01  ? 337 ALA C C   1 
ATOM   9716  O  O   . ALA C  1 337 ? 31.667  49.210  61.123  1.00 48.77  ? 337 ALA C O   1 
ATOM   9717  C  CB  . ALA C  1 337 ? 33.213  50.219  63.460  1.00 40.87  ? 337 ALA C CB  1 
ATOM   9718  N  N   . TYR C  1 338 ? 33.526  47.948  60.893  1.00 40.64  ? 338 TYR C N   1 
ATOM   9719  C  CA  . TYR C  1 338 ? 33.362  47.802  59.478  1.00 35.84  ? 338 TYR C CA  1 
ATOM   9720  C  C   . TYR C  1 338 ? 32.045  47.151  59.090  1.00 35.56  ? 338 TYR C C   1 
ATOM   9721  O  O   . TYR C  1 338 ? 31.584  46.227  59.736  1.00 33.84  ? 338 TYR C O   1 
ATOM   9722  C  CB  . TYR C  1 338 ? 34.522  47.012  58.945  1.00 33.01  ? 338 TYR C CB  1 
ATOM   9723  C  CG  . TYR C  1 338 ? 34.544  46.933  57.477  1.00 31.52  ? 338 TYR C CG  1 
ATOM   9724  C  CD1 . TYR C  1 338 ? 34.756  48.057  56.709  1.00 39.14  ? 338 TYR C CD1 1 
ATOM   9725  C  CD2 . TYR C  1 338 ? 34.445  45.720  56.849  1.00 35.77  ? 338 TYR C CD2 1 
ATOM   9726  C  CE1 . TYR C  1 338 ? 34.887  47.961  55.317  1.00 47.68  ? 338 TYR C CE1 1 
ATOM   9727  C  CE2 . TYR C  1 338 ? 34.578  45.594  55.478  1.00 42.21  ? 338 TYR C CE2 1 
ATOM   9728  C  CZ  . TYR C  1 338 ? 34.798  46.703  54.706  1.00 46.87  ? 338 TYR C CZ  1 
ATOM   9729  O  OH  . TYR C  1 338 ? 34.911  46.512  53.336  1.00 47.30  ? 338 TYR C OH  1 
ATOM   9730  N  N   . LYS C  1 339 ? 31.442  47.671  58.029  1.00 35.49  ? 339 LYS C N   1 
ATOM   9731  C  CA  . LYS C  1 339 ? 30.203  47.159  57.505  1.00 34.27  ? 339 LYS C CA  1 
ATOM   9732  C  C   . LYS C  1 339 ? 30.308  47.180  56.013  1.00 35.07  ? 339 LYS C C   1 
ATOM   9733  O  O   . LYS C  1 339 ? 29.359  47.457  55.338  1.00 41.42  ? 339 LYS C O   1 
ATOM   9734  C  CB  . LYS C  1 339 ? 29.061  48.030  57.905  1.00 41.33  ? 339 LYS C CB  1 
ATOM   9735  C  CG  . LYS C  1 339 ? 29.024  48.273  59.337  1.00 52.06  ? 339 LYS C CG  1 
ATOM   9736  C  CD  . LYS C  1 339 ? 28.691  47.009  60.048  1.00 67.87  ? 339 LYS C CD  1 
ATOM   9737  C  CE  . LYS C  1 339 ? 28.498  47.283  61.532  1.00 76.81  ? 339 LYS C CE  1 
ATOM   9738  N  NZ  . LYS C  1 339 ? 27.504  48.400  61.733  1.00 85.01  ? 339 LYS C NZ  1 
ATOM   9739  N  N   . ILE C  1 340 ? 31.501  46.970  55.501  1.00 35.72  ? 340 ILE C N   1 
ATOM   9740  C  CA  . ILE C  1 340 ? 31.746  46.889  54.065  1.00 39.45  ? 340 ILE C CA  1 
ATOM   9741  C  C   . ILE C  1 340 ? 31.808  48.220  53.360  1.00 42.91  ? 340 ILE C C   1 
ATOM   9742  O  O   . ILE C  1 340 ? 32.859  48.684  52.894  1.00 46.46  ? 340 ILE C O   1 
ATOM   9743  C  CB  . ILE C  1 340 ? 30.682  46.047  53.333  1.00 36.63  ? 340 ILE C CB  1 
ATOM   9744  C  CG1 . ILE C  1 340 ? 30.361  44.770  54.101  1.00 31.87  ? 340 ILE C CG1 1 
ATOM   9745  C  CG2 . ILE C  1 340 ? 31.177  45.738  51.941  1.00 37.40  ? 340 ILE C CG2 1 
ATOM   9746  C  CD1 . ILE C  1 340 ? 31.551  43.894  54.276  1.00 33.65  ? 340 ILE C CD1 1 
ATOM   9747  N  N   . THR C  1 341 ? 30.661  48.854  53.303  1.00 44.89  ? 341 THR C N   1 
ATOM   9748  C  CA  . THR C  1 341 ? 30.557  50.116  52.616  1.00 48.80  ? 341 THR C CA  1 
ATOM   9749  C  C   . THR C  1 341 ? 30.761  51.347  53.476  1.00 48.14  ? 341 THR C C   1 
ATOM   9750  O  O   . THR C  1 341 ? 31.050  52.412  52.947  1.00 53.24  ? 341 THR C O   1 
ATOM   9751  C  CB  . THR C  1 341 ? 29.198  50.220  51.930  1.00 49.20  ? 341 THR C CB  1 
ATOM   9752  O  OG1 . THR C  1 341 ? 28.164  50.030  52.917  1.00 54.82  ? 341 THR C OG1 1 
ATOM   9753  C  CG2 . THR C  1 341 ? 29.087  49.162  50.816  1.00 47.53  ? 341 THR C CG2 1 
ATOM   9754  N  N   . ASP C  1 342 ? 30.637  51.217  54.787  1.00 44.88  ? 342 ASP C N   1 
ATOM   9755  C  CA  . ASP C  1 342 ? 30.780  52.395  55.621  1.00 43.96  ? 342 ASP C CA  1 
ATOM   9756  C  C   . ASP C  1 342 ? 32.186  52.936  55.835  1.00 44.57  ? 342 ASP C C   1 
ATOM   9757  O  O   . ASP C  1 342 ? 32.369  53.862  56.628  1.00 44.08  ? 342 ASP C O   1 
ATOM   9758  C  CB  . ASP C  1 342 ? 30.063  52.208  56.951  1.00 44.04  ? 342 ASP C CB  1 
ATOM   9759  C  CG  . ASP C  1 342 ? 30.836  51.375  57.913  1.00 48.13  ? 342 ASP C CG  1 
ATOM   9760  O  OD1 . ASP C  1 342 ? 31.784  50.693  57.489  1.00 54.66  ? 342 ASP C OD1 1 
ATOM   9761  O  OD2 . ASP C  1 342 ? 30.497  51.404  59.114  1.00 52.12  ? 342 ASP C OD2 1 
ATOM   9762  N  N   . GLY C  1 343 ? 33.181  52.315  55.200  1.00 46.02  ? 343 GLY C N   1 
ATOM   9763  C  CA  . GLY C  1 343 ? 34.559  52.790  55.330  1.00 45.72  ? 343 GLY C CA  1 
ATOM   9764  C  C   . GLY C  1 343 ? 35.238  52.870  56.698  1.00 44.40  ? 343 GLY C C   1 
ATOM   9765  O  O   . GLY C  1 343 ? 36.357  53.405  56.815  1.00 46.93  ? 343 GLY C O   1 
ATOM   9766  N  N   . LEU C  1 344 ? 34.595  52.337  57.733  1.00 42.07  ? 344 LEU C N   1 
ATOM   9767  C  CA  . LEU C  1 344 ? 35.175  52.341  59.083  1.00 42.67  ? 344 LEU C CA  1 
ATOM   9768  C  C   . LEU C  1 344 ? 36.097  51.143  59.285  1.00 43.45  ? 344 LEU C C   1 
ATOM   9769  O  O   . LEU C  1 344 ? 35.849  50.256  60.120  1.00 51.16  ? 344 LEU C O   1 
ATOM   9770  C  CB  . LEU C  1 344 ? 34.058  52.309  60.114  1.00 41.44  ? 344 LEU C CB  1 
ATOM   9771  C  CG  . LEU C  1 344 ? 33.203  53.566  60.151  1.00 39.98  ? 344 LEU C CG  1 
ATOM   9772  C  CD1 . LEU C  1 344 ? 32.040  53.374  61.097  1.00 35.55  ? 344 LEU C CD1 1 
ATOM   9773  C  CD2 . LEU C  1 344 ? 34.092  54.721  60.600  1.00 30.34  ? 344 LEU C CD2 1 
ATOM   9774  N  N   . CYS C  1 345 ? 37.176  51.107  58.527  1.00 41.75  ? 345 CYS C N   1 
ATOM   9775  C  CA  . CYS C  1 345 ? 38.083  49.987  58.627  1.00 37.93  ? 345 CYS C CA  1 
ATOM   9776  C  C   . CYS C  1 345 ? 39.470  50.356  59.120  1.00 35.83  ? 345 CYS C C   1 
ATOM   9777  O  O   . CYS C  1 345 ? 40.472  50.027  58.489  1.00 36.60  ? 345 CYS C O   1 
ATOM   9778  C  CB  . CYS C  1 345 ? 38.156  49.335  57.277  1.00 35.45  ? 345 CYS C CB  1 
ATOM   9779  S  SG  . CYS C  1 345 ? 38.720  50.531  56.177  1.00 32.54  ? 345 CYS C SG  1 
ATOM   9780  N  N   . THR C  1 346 ? 39.528  51.068  60.233  1.00 35.38  ? 346 THR C N   1 
ATOM   9781  C  CA  . THR C  1 346 ? 40.813  51.453  60.774  1.00 40.61  ? 346 THR C CA  1 
ATOM   9782  C  C   . THR C  1 346 ? 40.861  51.285  62.278  1.00 39.87  ? 346 THR C C   1 
ATOM   9783  O  O   . THR C  1 346 ? 39.971  51.746  63.003  1.00 36.65  ? 346 THR C O   1 
ATOM   9784  C  CB  . THR C  1 346 ? 41.211  52.870  60.327  1.00 44.98  ? 346 THR C CB  1 
ATOM   9785  O  OG1 . THR C  1 346 ? 41.299  52.888  58.882  1.00 54.10  ? 346 THR C OG1 1 
ATOM   9786  C  CG2 . THR C  1 346 ? 42.562  53.279  60.935  1.00 41.02  ? 346 THR C CG2 1 
ATOM   9787  N  N   . PRO C  1 347 ? 41.870  50.537  62.751  1.00 40.48  ? 347 PRO C N   1 
ATOM   9788  C  CA  . PRO C  1 347 ? 42.078  50.249  64.162  1.00 42.15  ? 347 PRO C CA  1 
ATOM   9789  C  C   . PRO C  1 347 ? 42.091  51.534  64.973  1.00 44.90  ? 347 PRO C C   1 
ATOM   9790  O  O   . PRO C  1 347 ? 42.914  52.427  64.751  1.00 49.99  ? 347 PRO C O   1 
ATOM   9791  C  CB  . PRO C  1 347 ? 43.451  49.585  64.162  1.00 42.72  ? 347 PRO C CB  1 
ATOM   9792  C  CG  . PRO C  1 347 ? 43.544  48.949  62.828  1.00 43.34  ? 347 PRO C CG  1 
ATOM   9793  C  CD  . PRO C  1 347 ? 42.968  49.983  61.933  1.00 40.17  ? 347 PRO C CD  1 
ATOM   9794  N  N   . VAL C  1 348 ? 41.205  51.610  65.942  1.00 45.98  ? 348 VAL C N   1 
ATOM   9795  C  CA  . VAL C  1 348 ? 41.116  52.784  66.797  1.00 48.83  ? 348 VAL C CA  1 
ATOM   9796  C  C   . VAL C  1 348 ? 41.439  52.360  68.224  1.00 48.45  ? 348 VAL C C   1 
ATOM   9797  O  O   . VAL C  1 348 ? 41.200  51.200  68.603  1.00 50.55  ? 348 VAL C O   1 
ATOM   9798  C  CB  . VAL C  1 348 ? 39.680  53.361  66.763  1.00 47.77  ? 348 VAL C CB  1 
ATOM   9799  C  CG1 . VAL C  1 348 ? 39.333  53.760  65.377  1.00 55.16  ? 348 VAL C CG1 1 
ATOM   9800  C  CG2 . VAL C  1 348 ? 38.684  52.333  67.188  1.00 51.08  ? 348 VAL C CG2 1 
ATOM   9801  N  N   . LYS C  1 349 ? 42.008  53.253  69.024  1.00 48.51  ? 349 LYS C N   1 
ATOM   9802  C  CA  . LYS C  1 349 ? 42.283  52.848  70.395  1.00 51.29  ? 349 LYS C CA  1 
ATOM   9803  C  C   . LYS C  1 349 ? 40.967  52.449  71.069  1.00 48.73  ? 349 LYS C C   1 
ATOM   9804  O  O   . LYS C  1 349 ? 39.933  53.056  70.819  1.00 52.22  ? 349 LYS C O   1 
ATOM   9805  C  CB  . LYS C  1 349 ? 42.989  53.945  71.199  1.00 58.08  ? 349 LYS C CB  1 
ATOM   9806  C  CG  . LYS C  1 349 ? 43.299  53.506  72.672  1.00 74.69  ? 349 LYS C CG  1 
ATOM   9807  C  CD  . LYS C  1 349 ? 44.415  54.327  73.413  1.00 81.04  ? 349 LYS C CD  1 
ATOM   9808  C  CE  . LYS C  1 349 ? 45.836  54.148  72.814  1.00 84.51  ? 349 LYS C CE  1 
ATOM   9809  N  NZ  . LYS C  1 349 ? 46.042  54.784  71.450  1.00 85.38  ? 349 LYS C NZ  1 
ATOM   9810  N  N   . ASP C  1 350 ? 40.987  51.382  71.852  1.00 43.72  ? 350 ASP C N   1 
ATOM   9811  C  CA  . ASP C  1 350 ? 39.787  50.935  72.535  1.00 41.36  ? 350 ASP C CA  1 
ATOM   9812  C  C   . ASP C  1 350 ? 40.279  50.392  73.864  1.00 44.00  ? 350 ASP C C   1 
ATOM   9813  O  O   . ASP C  1 350 ? 41.147  49.526  73.903  1.00 47.50  ? 350 ASP C O   1 
ATOM   9814  C  CB  . ASP C  1 350 ? 39.119  49.844  71.704  1.00 42.36  ? 350 ASP C CB  1 
ATOM   9815  C  CG  . ASP C  1 350 ? 37.698  49.545  72.158  1.00 46.37  ? 350 ASP C CG  1 
ATOM   9816  O  OD1 . ASP C  1 350 ? 37.448  49.604  73.394  1.00 42.33  ? 350 ASP C OD1 1 
ATOM   9817  O  OD2 . ASP C  1 350 ? 36.836  49.250  71.275  1.00 45.23  ? 350 ASP C OD2 1 
ATOM   9818  N  N   . GLN C  1 351 ? 39.754  50.899  74.966  1.00 46.90  ? 351 GLN C N   1 
ATOM   9819  C  CA  . GLN C  1 351 ? 40.230  50.427  76.262  1.00 49.99  ? 351 GLN C CA  1 
ATOM   9820  C  C   . GLN C  1 351 ? 39.503  49.194  76.775  1.00 51.47  ? 351 GLN C C   1 
ATOM   9821  O  O   . GLN C  1 351 ? 39.610  48.833  77.949  1.00 53.73  ? 351 GLN C O   1 
ATOM   9822  C  CB  . GLN C  1 351 ? 40.227  51.548  77.305  1.00 51.08  ? 351 GLN C CB  1 
ATOM   9823  C  CG  . GLN C  1 351 ? 41.254  52.663  77.046  1.00 60.70  ? 351 GLN C CG  1 
ATOM   9824  C  CD  . GLN C  1 351 ? 42.681  52.299  77.457  1.00 66.64  ? 351 GLN C CD  1 
ATOM   9825  O  OE1 . GLN C  1 351 ? 42.958  52.063  78.639  1.00 67.50  ? 351 GLN C OE1 1 
ATOM   9826  N  NE2 . GLN C  1 351 ? 43.604  52.303  76.491  1.00 71.93  ? 351 GLN C NE2 1 
ATOM   9827  N  N   . SER C  1 352 ? 38.700  48.586  75.917  1.00 49.83  ? 352 SER C N   1 
ATOM   9828  C  CA  . SER C  1 352 ? 38.033  47.354  76.302  1.00 50.56  ? 352 SER C CA  1 
ATOM   9829  C  C   . SER C  1 352 ? 38.702  46.242  75.568  1.00 48.30  ? 352 SER C C   1 
ATOM   9830  O  O   . SER C  1 352 ? 38.458  45.088  75.856  1.00 53.43  ? 352 SER C O   1 
ATOM   9831  C  CB  . SER C  1 352 ? 36.577  47.347  75.901  1.00 53.51  ? 352 SER C CB  1 
ATOM   9832  O  OG  . SER C  1 352 ? 35.858  48.110  76.835  1.00 67.70  ? 352 SER C OG  1 
ATOM   9833  N  N   . ALA C  1 353 ? 39.492  46.605  74.568  1.00 44.75  ? 353 ALA C N   1 
ATOM   9834  C  CA  . ALA C  1 353 ? 40.176  45.634  73.760  1.00 39.64  ? 353 ALA C CA  1 
ATOM   9835  C  C   . ALA C  1 353 ? 41.380  45.185  74.524  1.00 33.66  ? 353 ALA C C   1 
ATOM   9836  O  O   . ALA C  1 353 ? 41.872  45.869  75.420  1.00 32.54  ? 353 ALA C O   1 
ATOM   9837  C  CB  . ALA C  1 353 ? 40.599  46.245  72.431  1.00 45.74  ? 353 ALA C CB  1 
ATOM   9838  N  N   . PRO C  1 354 ? 41.823  43.979  74.228  1.00 31.41  ? 354 PRO C N   1 
ATOM   9839  C  CA  . PRO C  1 354 ? 42.996  43.416  74.883  1.00 28.36  ? 354 PRO C CA  1 
ATOM   9840  C  C   . PRO C  1 354 ? 44.246  43.933  74.188  1.00 27.82  ? 354 PRO C C   1 
ATOM   9841  O  O   . PRO C  1 354 ? 44.192  44.518  73.131  1.00 24.35  ? 354 PRO C O   1 
ATOM   9842  C  CB  . PRO C  1 354 ? 42.853  41.939  74.555  1.00 23.33  ? 354 PRO C CB  1 
ATOM   9843  C  CG  . PRO C  1 354 ? 42.206  41.981  73.165  1.00 20.94  ? 354 PRO C CG  1 
ATOM   9844  C  CD  . PRO C  1 354 ? 41.142  42.977  73.380  1.00 25.68  ? 354 PRO C CD  1 
ATOM   9845  N  N   . VAL C  1 355 ? 45.385  43.642  74.767  1.00 30.39  ? 355 VAL C N   1 
ATOM   9846  C  CA  . VAL C  1 355 ? 46.665  43.996  74.190  1.00 28.95  ? 355 VAL C CA  1 
ATOM   9847  C  C   . VAL C  1 355 ? 47.036  42.749  73.383  1.00 29.56  ? 355 VAL C C   1 
ATOM   9848  O  O   . VAL C  1 355 ? 46.913  41.641  73.893  1.00 35.19  ? 355 VAL C O   1 
ATOM   9849  C  CB  . VAL C  1 355 ? 47.689  44.197  75.318  1.00 23.57  ? 355 VAL C CB  1 
ATOM   9850  C  CG1 . VAL C  1 355 ? 49.067  44.555  74.771  1.00 27.09  ? 355 VAL C CG1 1 
ATOM   9851  C  CG2 . VAL C  1 355 ? 47.184  45.243  76.255  1.00 27.12  ? 355 VAL C CG2 1 
ATOM   9852  N  N   . TYR C  1 356 ? 47.397  42.890  72.118  1.00 26.60  ? 356 TYR C N   1 
ATOM   9853  C  CA  . TYR C  1 356 ? 47.768  41.718  71.339  1.00 25.90  ? 356 TYR C CA  1 
ATOM   9854  C  C   . TYR C  1 356 ? 49.286  41.641  71.297  1.00 31.02  ? 356 TYR C C   1 
ATOM   9855  O  O   . TYR C  1 356 ? 49.921  42.537  70.738  1.00 39.63  ? 356 TYR C O   1 
ATOM   9856  C  CB  . TYR C  1 356 ? 47.201  41.796  69.926  1.00 23.76  ? 356 TYR C CB  1 
ATOM   9857  C  CG  . TYR C  1 356 ? 45.690  41.855  69.853  1.00 30.05  ? 356 TYR C CG  1 
ATOM   9858  C  CD1 . TYR C  1 356 ? 45.018  43.039  70.091  1.00 36.07  ? 356 TYR C CD1 1 
ATOM   9859  C  CD2 . TYR C  1 356 ? 44.933  40.732  69.528  1.00 35.29  ? 356 TYR C CD2 1 
ATOM   9860  C  CE1 . TYR C  1 356 ? 43.638  43.112  70.002  1.00 35.41  ? 356 TYR C CE1 1 
ATOM   9861  C  CE2 . TYR C  1 356 ? 43.534  40.785  69.438  1.00 34.54  ? 356 TYR C CE2 1 
ATOM   9862  C  CZ  . TYR C  1 356 ? 42.899  41.979  69.678  1.00 37.67  ? 356 TYR C CZ  1 
ATOM   9863  O  OH  . TYR C  1 356 ? 41.521  42.066  69.608  1.00 43.25  ? 356 TYR C OH  1 
ATOM   9864  N  N   . ILE C  1 357 ? 49.881  40.602  71.905  1.00 34.42  ? 357 ILE C N   1 
ATOM   9865  C  CA  . ILE C  1 357 ? 51.348  40.439  71.959  1.00 31.89  ? 357 ILE C CA  1 
ATOM   9866  C  C   . ILE C  1 357 ? 51.695  39.270  71.101  1.00 29.92  ? 357 ILE C C   1 
ATOM   9867  O  O   . ILE C  1 357 ? 50.842  38.418  70.917  1.00 35.48  ? 357 ILE C O   1 
ATOM   9868  C  CB  . ILE C  1 357 ? 51.833  40.155  73.412  1.00 33.56  ? 357 ILE C CB  1 
ATOM   9869  C  CG1 . ILE C  1 357 ? 51.748  41.426  74.248  1.00 36.50  ? 357 ILE C CG1 1 
ATOM   9870  C  CG2 . ILE C  1 357 ? 53.291  39.740  73.444  1.00 34.88  ? 357 ILE C CG2 1 
ATOM   9871  C  CD1 . ILE C  1 357 ? 52.097  41.215  75.694  1.00 42.84  ? 357 ILE C CD1 1 
ATOM   9872  N  N   . THR C  1 358 ? 52.889  39.264  70.495  1.00 27.83  ? 358 THR C N   1 
ATOM   9873  C  CA  . THR C  1 358 ? 53.319  38.120  69.686  1.00 25.91  ? 358 THR C CA  1 
ATOM   9874  C  C   . THR C  1 358 ? 54.744  37.709  70.054  1.00 28.32  ? 358 THR C C   1 
ATOM   9875  O  O   . THR C  1 358 ? 55.660  38.527  69.963  1.00 31.62  ? 358 THR C O   1 
ATOM   9876  C  CB  . THR C  1 358 ? 53.104  38.352  68.164  1.00 22.99  ? 358 THR C CB  1 
ATOM   9877  O  OG1 . THR C  1 358 ? 54.326  38.585  67.498  1.00 21.06  ? 358 THR C OG1 1 
ATOM   9878  C  CG2 . THR C  1 358 ? 52.146  39.495  67.911  1.00 22.97  ? 358 THR C CG2 1 
ATOM   9879  N  N   . ILE C  1 359 ? 54.903  36.497  70.598  1.00 27.95  ? 359 ILE C N   1 
ATOM   9880  C  CA  . ILE C  1 359 ? 56.213  35.992  71.010  1.00 26.43  ? 359 ILE C CA  1 
ATOM   9881  C  C   . ILE C  1 359 ? 56.630  34.726  70.319  1.00 27.99  ? 359 ILE C C   1 
ATOM   9882  O  O   . ILE C  1 359 ? 57.005  33.753  70.963  1.00 25.81  ? 359 ILE C O   1 
ATOM   9883  C  CB  . ILE C  1 359 ? 56.336  35.669  72.507  1.00 26.31  ? 359 ILE C CB  1 
ATOM   9884  C  CG1 . ILE C  1 359 ? 55.047  35.077  72.999  1.00 31.83  ? 359 ILE C CG1 1 
ATOM   9885  C  CG2 . ILE C  1 359 ? 56.898  36.826  73.341  1.00 19.41  ? 359 ILE C CG2 1 
ATOM   9886  C  CD1 . ILE C  1 359 ? 53.990  36.060  73.202  1.00 42.06  ? 359 ILE C CD1 1 
ATOM   9887  N  N   . GLY C  1 360 ? 56.586  34.727  69.002  1.00 32.74  ? 360 GLY C N   1 
ATOM   9888  C  CA  . GLY C  1 360 ? 57.044  33.549  68.280  1.00 34.58  ? 360 GLY C CA  1 
ATOM   9889  C  C   . GLY C  1 360 ? 58.540  33.639  67.987  1.00 36.38  ? 360 GLY C C   1 
ATOM   9890  O  O   . GLY C  1 360 ? 59.064  33.072  67.011  1.00 41.55  ? 360 GLY C O   1 
ATOM   9891  N  N   . ASP C  1 361 ? 59.266  34.288  68.879  1.00 32.55  ? 361 ASP C N   1 
ATOM   9892  C  CA  . ASP C  1 361 ? 60.675  34.469  68.632  1.00 30.06  ? 361 ASP C CA  1 
ATOM   9893  C  C   . ASP C  1 361 ? 61.542  33.636  69.532  1.00 29.95  ? 361 ASP C C   1 
ATOM   9894  O  O   . ASP C  1 361 ? 62.644  34.050  69.833  1.00 33.65  ? 361 ASP C O   1 
ATOM   9895  C  CB  . ASP C  1 361 ? 61.025  35.949  68.801  1.00 27.98  ? 361 ASP C CB  1 
ATOM   9896  C  CG  . ASP C  1 361 ? 60.837  36.433  70.235  1.00 27.97  ? 361 ASP C CG  1 
ATOM   9897  O  OD1 . ASP C  1 361 ? 59.973  35.881  70.951  1.00 31.60  ? 361 ASP C OD1 1 
ATOM   9898  O  OD2 . ASP C  1 361 ? 61.562  37.352  70.655  1.00 26.22  ? 361 ASP C OD2 1 
ATOM   9899  N  N   . ALA C  1 362 ? 61.089  32.478  69.981  1.00 26.77  ? 362 ALA C N   1 
ATOM   9900  C  CA  . ALA C  1 362 ? 61.938  31.688  70.876  1.00 23.92  ? 362 ALA C CA  1 
ATOM   9901  C  C   . ALA C  1 362 ? 63.063  30.920  70.173  1.00 25.11  ? 362 ALA C C   1 
ATOM   9902  O  O   . ALA C  1 362 ? 63.925  30.337  70.847  1.00 24.89  ? 362 ALA C O   1 
ATOM   9903  C  CB  . ALA C  1 362 ? 61.127  30.766  71.733  1.00 24.73  ? 362 ALA C CB  1 
ATOM   9904  N  N   . GLY C  1 363 ? 63.046  30.854  68.843  1.00 24.49  ? 363 GLY C N   1 
ATOM   9905  C  CA  . GLY C  1 363 ? 64.145  30.180  68.165  1.00 23.59  ? 363 GLY C CA  1 
ATOM   9906  C  C   . GLY C  1 363 ? 63.908  29.473  66.837  1.00 25.32  ? 363 GLY C C   1 
ATOM   9907  O  O   . GLY C  1 363 ? 64.685  29.638  65.908  1.00 23.76  ? 363 GLY C O   1 
ATOM   9908  N  N   . ASN C  1 364 ? 62.812  28.739  66.727  1.00 27.39  ? 364 ASN C N   1 
ATOM   9909  C  CA  . ASN C  1 364 ? 62.529  27.968  65.534  1.00 28.75  ? 364 ASN C CA  1 
ATOM   9910  C  C   . ASN C  1 364 ? 63.797  27.308  65.053  1.00 29.79  ? 364 ASN C C   1 
ATOM   9911  O  O   . ASN C  1 364 ? 64.573  26.815  65.863  1.00 27.42  ? 364 ASN C O   1 
ATOM   9912  C  CB  . ASN C  1 364 ? 61.815  28.760  64.427  1.00 31.51  ? 364 ASN C CB  1 
ATOM   9913  C  CG  . ASN C  1 364 ? 62.538  30.000  64.002  1.00 36.41  ? 364 ASN C CG  1 
ATOM   9914  O  OD1 . ASN C  1 364 ? 62.419  31.060  64.631  1.00 42.01  ? 364 ASN C OD1 1 
ATOM   9915  N  ND2 . ASN C  1 364 ? 63.228  29.912  62.889  1.00 29.83  ? 364 ASN C ND2 1 
ATOM   9916  N  N   . TYR C  1 365 ? 64.002  27.250  63.750  1.00 31.38  ? 365 TYR C N   1 
ATOM   9917  C  CA  . TYR C  1 365 ? 65.209  26.643  63.221  1.00 34.05  ? 365 TYR C CA  1 
ATOM   9918  C  C   . TYR C  1 365 ? 66.339  27.661  63.021  1.00 40.70  ? 365 TYR C C   1 
ATOM   9919  O  O   . TYR C  1 365 ? 67.179  27.508  62.106  1.00 42.39  ? 365 TYR C O   1 
ATOM   9920  C  CB  . TYR C  1 365 ? 64.903  25.950  61.921  1.00 32.84  ? 365 TYR C CB  1 
ATOM   9921  C  CG  . TYR C  1 365 ? 64.003  26.722  60.991  1.00 35.34  ? 365 TYR C CG  1 
ATOM   9922  C  CD1 . TYR C  1 365 ? 62.637  26.752  61.196  1.00 38.37  ? 365 TYR C CD1 1 
ATOM   9923  C  CD2 . TYR C  1 365 ? 64.511  27.402  59.885  1.00 36.86  ? 365 TYR C CD2 1 
ATOM   9924  C  CE1 . TYR C  1 365 ? 61.793  27.439  60.335  1.00 37.77  ? 365 TYR C CE1 1 
ATOM   9925  C  CE2 . TYR C  1 365 ? 63.678  28.093  59.013  1.00 35.33  ? 365 TYR C CE2 1 
ATOM   9926  C  CZ  . TYR C  1 365 ? 62.314  28.102  59.249  1.00 36.92  ? 365 TYR C CZ  1 
ATOM   9927  O  OH  . TYR C  1 365 ? 61.455  28.769  58.409  1.00 43.27  ? 365 TYR C OH  1 
ATOM   9928  N  N   . GLY C  1 366 ? 66.361  28.664  63.909  1.00 43.17  ? 366 GLY C N   1 
ATOM   9929  C  CA  . GLY C  1 366 ? 67.354  29.725  63.903  1.00 41.96  ? 366 GLY C CA  1 
ATOM   9930  C  C   . GLY C  1 366 ? 67.124  30.898  62.975  1.00 40.11  ? 366 GLY C C   1 
ATOM   9931  O  O   . GLY C  1 366 ? 68.072  31.536  62.537  1.00 44.41  ? 366 GLY C O   1 
ATOM   9932  N  N   . VAL C  1 367 ? 65.878  31.251  62.731  1.00 37.12  ? 367 VAL C N   1 
ATOM   9933  C  CA  . VAL C  1 367 ? 65.615  32.342  61.814  1.00 32.58  ? 367 VAL C CA  1 
ATOM   9934  C  C   . VAL C  1 367 ? 64.648  33.386  62.362  1.00 35.60  ? 367 VAL C C   1 
ATOM   9935  O  O   . VAL C  1 367 ? 63.586  33.053  62.922  1.00 36.61  ? 367 VAL C O   1 
ATOM   9936  C  CB  . VAL C  1 367 ? 65.091  31.803  60.514  1.00 24.81  ? 367 VAL C CB  1 
ATOM   9937  C  CG1 . VAL C  1 367 ? 64.347  32.846  59.763  1.00 35.29  ? 367 VAL C CG1 1 
ATOM   9938  C  CG2 . VAL C  1 367 ? 66.214  31.352  59.701  1.00 29.07  ? 367 VAL C CG2 1 
ATOM   9939  N  N   . ILE C  1 368 ? 64.991  34.647  62.116  1.00 31.67  ? 368 ILE C N   1 
ATOM   9940  C  CA  . ILE C  1 368 ? 64.201  35.759  62.583  1.00 29.51  ? 368 ILE C CA  1 
ATOM   9941  C  C   . ILE C  1 368 ? 63.515  36.518  61.446  1.00 30.54  ? 368 ILE C C   1 
ATOM   9942  O  O   . ILE C  1 368 ? 64.068  36.653  60.373  1.00 34.57  ? 368 ILE C O   1 
ATOM   9943  C  CB  . ILE C  1 368 ? 65.110  36.736  63.298  1.00 25.57  ? 368 ILE C CB  1 
ATOM   9944  C  CG1 . ILE C  1 368 ? 65.327  36.313  64.734  1.00 41.61  ? 368 ILE C CG1 1 
ATOM   9945  C  CG2 . ILE C  1 368 ? 64.449  38.014  63.431  1.00 31.71  ? 368 ILE C CG2 1 
ATOM   9946  C  CD1 . ILE C  1 368 ? 64.160  36.691  65.702  1.00 47.66  ? 368 ILE C CD1 1 
ATOM   9947  N  N   . ASP C  1 369 ? 62.305  37.001  61.682  1.00 27.03  ? 369 ASP C N   1 
ATOM   9948  C  CA  . ASP C  1 369 ? 61.588  37.791  60.716  1.00 25.53  ? 369 ASP C CA  1 
ATOM   9949  C  C   . ASP C  1 369 ? 61.896  39.248  61.027  1.00 29.88  ? 369 ASP C C   1 
ATOM   9950  O  O   . ASP C  1 369 ? 61.376  39.827  61.984  1.00 31.53  ? 369 ASP C O   1 
ATOM   9951  C  CB  . ASP C  1 369 ? 60.099  37.573  60.851  1.00 31.72  ? 369 ASP C CB  1 
ATOM   9952  C  CG  . ASP C  1 369 ? 59.679  36.194  60.451  1.00 33.64  ? 369 ASP C CG  1 
ATOM   9953  O  OD1 . ASP C  1 369 ? 60.127  35.704  59.391  1.00 35.26  ? 369 ASP C OD1 1 
ATOM   9954  O  OD2 . ASP C  1 369 ? 58.886  35.596  61.194  1.00 42.09  ? 369 ASP C OD2 1 
ATOM   9955  N  N   . SER C  1 370 ? 62.691  39.853  60.173  1.00 30.26  ? 370 SER C N   1 
ATOM   9956  C  CA  . SER C  1 370 ? 63.089  41.208  60.377  1.00 35.60  ? 370 SER C CA  1 
ATOM   9957  C  C   . SER C  1 370 ? 62.339  42.280  59.562  1.00 35.28  ? 370 SER C C   1 
ATOM   9958  O  O   . SER C  1 370 ? 62.202  43.433  60.016  1.00 42.62  ? 370 SER C O   1 
ATOM   9959  C  CB  . SER C  1 370 ? 64.581  41.306  60.100  1.00 38.38  ? 370 SER C CB  1 
ATOM   9960  O  OG  . SER C  1 370 ? 64.853  41.018  58.730  1.00 50.40  ? 370 SER C OG  1 
ATOM   9961  N  N   . ASN C  1 371 ? 61.947  41.971  58.334  1.00 28.37  ? 371 ASN C N   1 
ATOM   9962  C  CA  . ASN C  1 371 ? 61.262  42.979  57.553  1.00 27.19  ? 371 ASN C CA  1 
ATOM   9963  C  C   . ASN C  1 371 ? 59.927  43.331  58.208  1.00 32.36  ? 371 ASN C C   1 
ATOM   9964  O  O   . ASN C  1 371 ? 59.193  42.439  58.639  1.00 41.66  ? 371 ASN C O   1 
ATOM   9965  C  CB  . ASN C  1 371 ? 61.057  42.521  56.116  1.00 23.54  ? 371 ASN C CB  1 
ATOM   9966  C  CG  . ASN C  1 371 ? 62.374  42.359  55.334  1.00 31.48  ? 371 ASN C CG  1 
ATOM   9967  O  OD1 . ASN C  1 371 ? 63.466  42.656  55.825  1.00 41.27  ? 371 ASN C OD1 1 
ATOM   9968  N  ND2 . ASN C  1 371 ? 62.265  41.867  54.112  1.00 36.30  ? 371 ASN C ND2 1 
ATOM   9969  N  N   . MET C  1 372 ? 59.605  44.616  58.315  1.00 31.37  ? 372 MET C N   1 
ATOM   9970  C  CA  . MET C  1 372 ? 58.351  44.985  58.919  1.00 28.35  ? 372 MET C CA  1 
ATOM   9971  C  C   . MET C  1 372 ? 57.603  45.934  58.026  1.00 31.62  ? 372 MET C C   1 
ATOM   9972  O  O   . MET C  1 372 ? 58.111  46.368  57.002  1.00 29.71  ? 372 MET C O   1 
ATOM   9973  C  CB  . MET C  1 372 ? 58.591  45.603  60.268  1.00 25.03  ? 372 MET C CB  1 
ATOM   9974  C  CG  . MET C  1 372 ? 60.032  45.843  60.540  1.00 27.97  ? 372 MET C CG  1 
ATOM   9975  S  SD  . MET C  1 372 ? 60.106  46.104  62.276  1.00 30.37  ? 372 MET C SD  1 
ATOM   9976  C  CE  . MET C  1 372 ? 60.982  44.646  62.723  1.00 24.94  ? 372 MET C CE  1 
ATOM   9977  N  N   . ILE C  1 373 ? 56.336  46.140  58.329  1.00 34.01  ? 373 ILE C N   1 
ATOM   9978  C  CA  . ILE C  1 373 ? 55.558  47.077  57.559  1.00 34.18  ? 373 ILE C CA  1 
ATOM   9979  C  C   . ILE C  1 373 ? 56.098  48.435  57.940  1.00 37.60  ? 373 ILE C C   1 
ATOM   9980  O  O   . ILE C  1 373 ? 56.052  48.806  59.105  1.00 36.49  ? 373 ILE C O   1 
ATOM   9981  C  CB  . ILE C  1 373 ? 54.117  47.026  57.987  1.00 31.83  ? 373 ILE C CB  1 
ATOM   9982  C  CG1 . ILE C  1 373 ? 53.517  45.752  57.489  1.00 31.38  ? 373 ILE C CG1 1 
ATOM   9983  C  CG2 . ILE C  1 373 ? 53.343  48.136  57.398  1.00 30.73  ? 373 ILE C CG2 1 
ATOM   9984  C  CD1 . ILE C  1 373 ? 54.019  45.413  56.126  1.00 31.49  ? 373 ILE C CD1 1 
ATOM   9985  N  N   . GLN C  1 374 ? 56.699  49.154  57.005  1.00 42.06  ? 374 GLN C N   1 
ATOM   9986  C  CA  . GLN C  1 374 ? 57.192  50.477  57.358  1.00 42.06  ? 374 GLN C CA  1 
ATOM   9987  C  C   . GLN C  1 374 ? 56.293  51.566  56.807  1.00 43.10  ? 374 GLN C C   1 
ATOM   9988  O  O   . GLN C  1 374 ? 55.963  51.576  55.612  1.00 49.20  ? 374 GLN C O   1 
ATOM   9989  C  CB  . GLN C  1 374 ? 58.621  50.661  56.881  1.00 42.48  ? 374 GLN C CB  1 
ATOM   9990  C  CG  . GLN C  1 374 ? 59.591  50.741  58.014  1.00 47.00  ? 374 GLN C CG  1 
ATOM   9991  C  CD  . GLN C  1 374 ? 59.479  49.545  58.891  1.00 55.96  ? 374 GLN C CD  1 
ATOM   9992  O  OE1 . GLN C  1 374 ? 60.178  48.542  58.688  1.00 66.04  ? 374 GLN C OE1 1 
ATOM   9993  N  NE2 . GLN C  1 374 ? 58.541  49.590  59.836  1.00 60.84  ? 374 GLN C NE2 1 
ATOM   9994  N  N   . PRO C  1 375 ? 55.918  52.536  57.650  1.00 41.81  ? 375 PRO C N   1 
ATOM   9995  C  CA  . PRO C  1 375 ? 56.273  52.780  59.057  1.00 42.38  ? 375 PRO C CA  1 
ATOM   9996  C  C   . PRO C  1 375 ? 55.396  52.071  60.117  1.00 39.33  ? 375 PRO C C   1 
ATOM   9997  O  O   . PRO C  1 375 ? 54.237  51.695  59.869  1.00 40.56  ? 375 PRO C O   1 
ATOM   9998  C  CB  . PRO C  1 375 ? 56.143  54.296  59.167  1.00 42.06  ? 375 PRO C CB  1 
ATOM   9999  C  CG  . PRO C  1 375 ? 54.913  54.535  58.357  1.00 43.67  ? 375 PRO C CG  1 
ATOM   10000 C  CD  . PRO C  1 375 ? 55.087  53.642  57.132  1.00 44.52  ? 375 PRO C CD  1 
ATOM   10001 N  N   . GLN C  1 376 ? 55.947  51.960  61.320  1.00 34.21  ? 376 GLN C N   1 
ATOM   10002 C  CA  . GLN C  1 376 ? 55.248  51.287  62.389  1.00 35.74  ? 376 GLN C CA  1 
ATOM   10003 C  C   . GLN C  1 376 ? 53.871  51.854  62.520  1.00 35.30  ? 376 GLN C C   1 
ATOM   10004 O  O   . GLN C  1 376 ? 53.707  53.016  62.795  1.00 43.79  ? 376 GLN C O   1 
ATOM   10005 C  CB  . GLN C  1 376 ? 56.003  51.446  63.681  1.00 34.09  ? 376 GLN C CB  1 
ATOM   10006 C  CG  . GLN C  1 376 ? 55.258  50.878  64.853  1.00 42.01  ? 376 GLN C CG  1 
ATOM   10007 C  CD  . GLN C  1 376 ? 56.141  50.769  66.066  1.00 46.78  ? 376 GLN C CD  1 
ATOM   10008 O  OE1 . GLN C  1 376 ? 57.361  50.916  65.970  1.00 50.09  ? 376 GLN C OE1 1 
ATOM   10009 N  NE2 . GLN C  1 376 ? 55.539  50.473  67.221  1.00 55.44  ? 376 GLN C NE2 1 
ATOM   10010 N  N   . PRO C  1 377 ? 52.858  51.061  62.251  1.00 35.81  ? 377 PRO C N   1 
ATOM   10011 C  CA  . PRO C  1 377 ? 51.497  51.563  62.355  1.00 39.35  ? 377 PRO C CA  1 
ATOM   10012 C  C   . PRO C  1 377 ? 51.153  51.900  63.750  1.00 38.57  ? 377 PRO C C   1 
ATOM   10013 O  O   . PRO C  1 377 ? 51.724  51.374  64.693  1.00 39.43  ? 377 PRO C O   1 
ATOM   10014 C  CB  . PRO C  1 377 ? 50.659  50.408  61.844  1.00 37.43  ? 377 PRO C CB  1 
ATOM   10015 C  CG  . PRO C  1 377 ? 51.449  49.274  62.257  1.00 42.39  ? 377 PRO C CG  1 
ATOM   10016 C  CD  . PRO C  1 377 ? 52.851  49.666  61.853  1.00 36.47  ? 377 PRO C CD  1 
ATOM   10017 N  N   . GLU C  1 378 ? 50.152  52.751  63.837  1.00 45.57  ? 378 GLU C N   1 
ATOM   10018 C  CA  . GLU C  1 378 ? 49.646  53.285  65.087  1.00 51.64  ? 378 GLU C CA  1 
ATOM   10019 C  C   . GLU C  1 378 ? 49.351  52.230  66.116  1.00 44.91  ? 378 GLU C C   1 
ATOM   10020 O  O   . GLU C  1 378 ? 49.751  52.386  67.260  1.00 44.53  ? 378 GLU C O   1 
ATOM   10021 C  CB  . GLU C  1 378 ? 48.359  54.134  64.873  1.00 67.27  ? 378 GLU C CB  1 
ATOM   10022 C  CG  . GLU C  1 378 ? 48.103  54.762  63.458  1.00 78.71  ? 378 GLU C CG  1 
ATOM   10023 C  CD  . GLU C  1 378 ? 47.516  53.771  62.428  1.00 84.68  ? 378 GLU C CD  1 
ATOM   10024 O  OE1 . GLU C  1 378 ? 46.397  53.223  62.674  1.00 89.82  ? 378 GLU C OE1 1 
ATOM   10025 O  OE2 . GLU C  1 378 ? 48.184  53.566  61.375  1.00 78.98  ? 378 GLU C OE2 1 
ATOM   10026 N  N   . TYR C  1 379 ? 48.660  51.164  65.701  1.00 36.77  ? 379 TYR C N   1 
ATOM   10027 C  CA  . TYR C  1 379 ? 48.268  50.112  66.629  1.00 26.92  ? 379 TYR C CA  1 
ATOM   10028 C  C   . TYR C  1 379 ? 49.418  49.384  67.253  1.00 25.42  ? 379 TYR C C   1 
ATOM   10029 O  O   . TYR C  1 379 ? 49.294  48.787  68.340  1.00 23.55  ? 379 TYR C O   1 
ATOM   10030 C  CB  . TYR C  1 379 ? 47.300  49.132  65.990  1.00 23.81  ? 379 TYR C CB  1 
ATOM   10031 C  CG  . TYR C  1 379 ? 47.823  48.438  64.770  1.00 27.20  ? 379 TYR C CG  1 
ATOM   10032 C  CD1 . TYR C  1 379 ? 48.700  47.375  64.875  1.00 27.13  ? 379 TYR C CD1 1 
ATOM   10033 C  CD2 . TYR C  1 379 ? 47.427  48.827  63.501  1.00 30.34  ? 379 TYR C CD2 1 
ATOM   10034 C  CE1 . TYR C  1 379 ? 49.179  46.705  63.741  1.00 24.12  ? 379 TYR C CE1 1 
ATOM   10035 C  CE2 . TYR C  1 379 ? 47.899  48.170  62.370  1.00 29.99  ? 379 TYR C CE2 1 
ATOM   10036 C  CZ  . TYR C  1 379 ? 48.776  47.110  62.498  1.00 31.86  ? 379 TYR C CZ  1 
ATOM   10037 O  OH  . TYR C  1 379 ? 49.244  46.474  61.364  1.00 41.51  ? 379 TYR C OH  1 
ATOM   10038 N  N   . SER C  1 380 ? 50.557  49.488  66.601  1.00 22.01  ? 380 SER C N   1 
ATOM   10039 C  CA  . SER C  1 380 ? 51.710  48.807  67.101  1.00 23.50  ? 380 SER C CA  1 
ATOM   10040 C  C   . SER C  1 380 ? 52.397  49.607  68.146  1.00 23.93  ? 380 SER C C   1 
ATOM   10041 O  O   . SER C  1 380 ? 52.881  50.670  67.846  1.00 28.07  ? 380 SER C O   1 
ATOM   10042 C  CB  . SER C  1 380 ? 52.676  48.587  65.985  1.00 23.34  ? 380 SER C CB  1 
ATOM   10043 O  OG  . SER C  1 380 ? 53.754  47.873  66.539  1.00 37.73  ? 380 SER C OG  1 
ATOM   10044 N  N   . ALA C  1 381 ? 52.501  49.099  69.363  1.00 25.05  ? 381 ALA C N   1 
ATOM   10045 C  CA  . ALA C  1 381 ? 53.183  49.854  70.417  1.00 25.35  ? 381 ALA C CA  1 
ATOM   10046 C  C   . ALA C  1 381 ? 54.674  49.641  70.458  1.00 27.12  ? 381 ALA C C   1 
ATOM   10047 O  O   . ALA C  1 381 ? 55.429  50.516  70.824  1.00 29.25  ? 381 ALA C O   1 
ATOM   10048 C  CB  . ALA C  1 381 ? 52.617  49.522  71.762  1.00 26.16  ? 381 ALA C CB  1 
ATOM   10049 N  N   . PHE C  1 382 ? 55.120  48.466  70.078  1.00 33.35  ? 382 PHE C N   1 
ATOM   10050 C  CA  . PHE C  1 382 ? 56.537  48.199  70.155  1.00 33.72  ? 382 PHE C CA  1 
ATOM   10051 C  C   . PHE C  1 382 ? 56.814  46.951  69.375  1.00 35.69  ? 382 PHE C C   1 
ATOM   10052 O  O   . PHE C  1 382 ? 56.076  45.984  69.497  1.00 35.57  ? 382 PHE C O   1 
ATOM   10053 C  CB  . PHE C  1 382 ? 56.885  47.932  71.607  1.00 32.44  ? 382 PHE C CB  1 
ATOM   10054 C  CG  . PHE C  1 382 ? 58.296  47.486  71.810  1.00 34.58  ? 382 PHE C CG  1 
ATOM   10055 C  CD1 . PHE C  1 382 ? 58.727  46.247  71.399  1.00 39.78  ? 382 PHE C CD1 1 
ATOM   10056 C  CD2 . PHE C  1 382 ? 59.211  48.299  72.410  1.00 37.75  ? 382 PHE C CD2 1 
ATOM   10057 C  CE1 . PHE C  1 382 ? 60.063  45.833  71.587  1.00 37.85  ? 382 PHE C CE1 1 
ATOM   10058 C  CE2 . PHE C  1 382 ? 60.546  47.875  72.593  1.00 34.40  ? 382 PHE C CE2 1 
ATOM   10059 C  CZ  . PHE C  1 382 ? 60.959  46.658  72.183  1.00 26.58  ? 382 PHE C CZ  1 
ATOM   10060 N  N   . ARG C  1 383 ? 57.883  46.943  68.597  1.00 35.91  ? 383 ARG C N   1 
ATOM   10061 C  CA  . ARG C  1 383 ? 58.225  45.737  67.864  1.00 33.76  ? 383 ARG C CA  1 
ATOM   10062 C  C   . ARG C  1 383 ? 59.707  45.587  67.700  1.00 34.35  ? 383 ARG C C   1 
ATOM   10063 O  O   . ARG C  1 383 ? 60.431  46.574  67.541  1.00 34.89  ? 383 ARG C O   1 
ATOM   10064 C  CB  . ARG C  1 383 ? 57.537  45.632  66.489  1.00 34.23  ? 383 ARG C CB  1 
ATOM   10065 C  CG  . ARG C  1 383 ? 57.099  46.910  65.815  1.00 34.89  ? 383 ARG C CG  1 
ATOM   10066 C  CD  . ARG C  1 383 ? 57.812  47.103  64.518  1.00 34.38  ? 383 ARG C CD  1 
ATOM   10067 N  NE  . ARG C  1 383 ? 56.911  47.230  63.385  1.00 32.91  ? 383 ARG C NE  1 
ATOM   10068 C  CZ  . ARG C  1 383 ? 57.122  48.058  62.371  1.00 36.34  ? 383 ARG C CZ  1 
ATOM   10069 N  NH1 . ARG C  1 383 ? 58.184  48.858  62.361  1.00 35.75  ? 383 ARG C NH1 1 
ATOM   10070 N  NH2 . ARG C  1 383 ? 56.328  48.015  61.325  1.00 38.21  ? 383 ARG C NH2 1 
ATOM   10071 N  N   . GLU C  1 384 ? 60.175  44.349  67.794  1.00 34.35  ? 384 GLU C N   1 
ATOM   10072 C  CA  . GLU C  1 384 ? 61.588  44.091  67.595  1.00 32.01  ? 384 GLU C CA  1 
ATOM   10073 C  C   . GLU C  1 384 ? 61.816  42.666  67.101  1.00 30.44  ? 384 GLU C C   1 
ATOM   10074 O  O   . GLU C  1 384 ? 61.113  41.720  67.508  1.00 31.53  ? 384 GLU C O   1 
ATOM   10075 C  CB  . GLU C  1 384 ? 62.395  44.363  68.856  1.00 30.89  ? 384 GLU C CB  1 
ATOM   10076 C  CG  . GLU C  1 384 ? 63.869  44.377  68.566  1.00 35.09  ? 384 GLU C CG  1 
ATOM   10077 C  CD  . GLU C  1 384 ? 64.726  44.603  69.785  1.00 37.98  ? 384 GLU C CD  1 
ATOM   10078 O  OE1 . GLU C  1 384 ? 64.402  45.507  70.590  1.00 46.57  ? 384 GLU C OE1 1 
ATOM   10079 O  OE2 . GLU C  1 384 ? 65.742  43.891  69.923  1.00 39.70  ? 384 GLU C OE2 1 
ATOM   10080 N  N   . ALA C  1 385 ? 62.794  42.537  66.210  1.00 25.69  ? 385 ALA C N   1 
ATOM   10081 C  CA  . ALA C  1 385 ? 63.174  41.257  65.639  1.00 23.39  ? 385 ALA C CA  1 
ATOM   10082 C  C   . ALA C  1 385 ? 64.361  40.644  66.393  1.00 22.40  ? 385 ALA C C   1 
ATOM   10083 O  O   . ALA C  1 385 ? 65.492  40.691  65.934  1.00 28.08  ? 385 ALA C O   1 
ATOM   10084 C  CB  . ALA C  1 385 ? 63.512  41.423  64.169  1.00 17.02  ? 385 ALA C CB  1 
ATOM   10085 N  N   . SER C  1 386 ? 64.112  40.088  67.557  1.00 21.06  ? 386 SER C N   1 
ATOM   10086 C  CA  . SER C  1 386 ? 65.164  39.461  68.316  1.00 23.81  ? 386 SER C CA  1 
ATOM   10087 C  C   . SER C  1 386 ? 64.607  38.195  68.903  1.00 24.51  ? 386 SER C C   1 
ATOM   10088 O  O   . SER C  1 386 ? 63.391  38.060  69.027  1.00 24.89  ? 386 SER C O   1 
ATOM   10089 C  CB  . SER C  1 386 ? 65.628  40.356  69.454  1.00 24.38  ? 386 SER C CB  1 
ATOM   10090 O  OG  . SER C  1 386 ? 66.563  41.288  68.963  1.00 36.47  ? 386 SER C OG  1 
ATOM   10091 N  N   . PHE C  1 387 ? 65.488  37.244  69.199  1.00 24.52  ? 387 PHE C N   1 
ATOM   10092 C  CA  . PHE C  1 387 ? 65.054  35.994  69.819  1.00 25.77  ? 387 PHE C CA  1 
ATOM   10093 C  C   . PHE C  1 387 ? 64.878  36.253  71.327  1.00 25.87  ? 387 PHE C C   1 
ATOM   10094 O  O   . PHE C  1 387 ? 65.543  37.122  71.892  1.00 26.35  ? 387 PHE C O   1 
ATOM   10095 C  CB  . PHE C  1 387 ? 66.061  34.865  69.579  1.00 18.95  ? 387 PHE C CB  1 
ATOM   10096 C  CG  . PHE C  1 387 ? 66.117  34.371  68.152  1.00 17.65  ? 387 PHE C CG  1 
ATOM   10097 C  CD1 . PHE C  1 387 ? 65.007  33.785  67.559  1.00 19.83  ? 387 PHE C CD1 1 
ATOM   10098 C  CD2 . PHE C  1 387 ? 67.288  34.436  67.423  1.00 17.03  ? 387 PHE C CD2 1 
ATOM   10099 C  CE1 . PHE C  1 387 ? 65.049  33.258  66.254  1.00 22.44  ? 387 PHE C CE1 1 
ATOM   10100 C  CE2 . PHE C  1 387 ? 67.353  33.918  66.129  1.00 26.07  ? 387 PHE C CE2 1 
ATOM   10101 C  CZ  . PHE C  1 387 ? 66.224  33.319  65.533  1.00 27.35  ? 387 PHE C CZ  1 
ATOM   10102 N  N   . GLY C  1 388 ? 63.918  35.570  71.946  1.00 27.11  ? 388 GLY C N   1 
ATOM   10103 C  CA  . GLY C  1 388 ? 63.671  35.723  73.369  1.00 29.07  ? 388 GLY C CA  1 
ATOM   10104 C  C   . GLY C  1 388 ? 62.399  35.014  73.816  1.00 30.39  ? 388 GLY C C   1 
ATOM   10105 O  O   . GLY C  1 388 ? 61.756  34.280  73.041  1.00 36.89  ? 388 GLY C O   1 
ATOM   10106 N  N   . HIS C  1 389 ? 62.001  35.252  75.053  1.00 25.33  ? 389 HIS C N   1 
ATOM   10107 C  CA  . HIS C  1 389 ? 60.807  34.642  75.601  1.00 26.04  ? 389 HIS C CA  1 
ATOM   10108 C  C   . HIS C  1 389 ? 60.186  35.750  76.429  1.00 28.36  ? 389 HIS C C   1 
ATOM   10109 O  O   . HIS C  1 389 ? 60.805  36.794  76.585  1.00 31.60  ? 389 HIS C O   1 
ATOM   10110 C  CB  . HIS C  1 389 ? 61.207  33.487  76.518  1.00 28.89  ? 389 HIS C CB  1 
ATOM   10111 C  CG  . HIS C  1 389 ? 61.965  33.922  77.743  1.00 28.40  ? 389 HIS C CG  1 
ATOM   10112 N  ND1 . HIS C  1 389 ? 61.352  34.088  78.971  1.00 31.21  ? 389 HIS C ND1 1 
ATOM   10113 C  CD2 . HIS C  1 389 ? 63.283  34.192  77.944  1.00 24.14  ? 389 HIS C CD2 1 
ATOM   10114 C  CE1 . HIS C  1 389 ? 62.261  34.428  79.874  1.00 31.75  ? 389 HIS C CE1 1 
ATOM   10115 N  NE2 . HIS C  1 389 ? 63.440  34.494  79.279  1.00 23.11  ? 389 HIS C NE2 1 
ATOM   10116 N  N   . GLY C  1 390 ? 59.026  35.515  77.035  1.00 29.20  ? 390 GLY C N   1 
ATOM   10117 C  CA  . GLY C  1 390 ? 58.400  36.558  77.826  1.00 26.84  ? 390 GLY C CA  1 
ATOM   10118 C  C   . GLY C  1 390 ? 57.956  36.022  79.162  1.00 33.00  ? 390 GLY C C   1 
ATOM   10119 O  O   . GLY C  1 390 ? 58.094  34.813  79.394  1.00 35.77  ? 390 GLY C O   1 
ATOM   10120 N  N   . MET C  1 391 ? 57.513  36.902  80.068  1.00 30.33  ? 391 MET C N   1 
ATOM   10121 C  CA  . MET C  1 391 ? 57.024  36.468  81.379  1.00 28.89  ? 391 MET C CA  1 
ATOM   10122 C  C   . MET C  1 391 ? 55.828  37.351  81.659  1.00 27.40  ? 391 MET C C   1 
ATOM   10123 O  O   . MET C  1 391 ? 55.867  38.523  81.355  1.00 34.39  ? 391 MET C O   1 
ATOM   10124 C  CB  . MET C  1 391 ? 58.073  36.690  82.457  1.00 30.01  ? 391 MET C CB  1 
ATOM   10125 C  CG  . MET C  1 391 ? 59.395  35.966  82.268  1.00 36.29  ? 391 MET C CG  1 
ATOM   10126 S  SD  . MET C  1 391 ? 59.383  34.278  82.868  1.00 42.46  ? 391 MET C SD  1 
ATOM   10127 C  CE  . MET C  1 391 ? 58.746  34.485  84.383  1.00 43.25  ? 391 MET C CE  1 
ATOM   10128 N  N   . PHE C  1 392 ? 54.761  36.787  82.179  1.00 26.06  ? 392 PHE C N   1 
ATOM   10129 C  CA  . PHE C  1 392 ? 53.572  37.553  82.490  1.00 29.68  ? 392 PHE C CA  1 
ATOM   10130 C  C   . PHE C  1 392 ? 53.378  37.299  83.969  1.00 31.46  ? 392 PHE C C   1 
ATOM   10131 O  O   . PHE C  1 392 ? 52.955  36.224  84.364  1.00 37.18  ? 392 PHE C O   1 
ATOM   10132 C  CB  . PHE C  1 392 ? 52.391  37.012  81.700  1.00 29.42  ? 392 PHE C CB  1 
ATOM   10133 C  CG  . PHE C  1 392 ? 51.159  37.822  81.844  1.00 29.13  ? 392 PHE C CG  1 
ATOM   10134 C  CD1 . PHE C  1 392 ? 50.942  38.929  81.044  1.00 34.21  ? 392 PHE C CD1 1 
ATOM   10135 C  CD2 . PHE C  1 392 ? 50.187  37.454  82.731  1.00 31.61  ? 392 PHE C CD2 1 
ATOM   10136 C  CE1 . PHE C  1 392 ? 49.754  39.646  81.134  1.00 33.06  ? 392 PHE C CE1 1 
ATOM   10137 C  CE2 . PHE C  1 392 ? 48.997  38.164  82.820  1.00 32.58  ? 392 PHE C CE2 1 
ATOM   10138 C  CZ  . PHE C  1 392 ? 48.782  39.259  82.019  1.00 24.43  ? 392 PHE C CZ  1 
ATOM   10139 N  N   . ASP C  1 393 ? 53.684  38.286  84.786  1.00 31.07  ? 393 ASP C N   1 
ATOM   10140 C  CA  . ASP C  1 393 ? 53.618  38.140  86.218  1.00 24.65  ? 393 ASP C CA  1 
ATOM   10141 C  C   . ASP C  1 393 ? 52.416  38.735  86.885  1.00 24.77  ? 393 ASP C C   1 
ATOM   10142 O  O   . ASP C  1 393 ? 52.365  39.930  87.133  1.00 28.84  ? 393 ASP C O   1 
ATOM   10143 C  CB  . ASP C  1 393 ? 54.841  38.799  86.760  1.00 29.44  ? 393 ASP C CB  1 
ATOM   10144 C  CG  . ASP C  1 393 ? 55.141  38.396  88.163  1.00 40.97  ? 393 ASP C CG  1 
ATOM   10145 O  OD1 . ASP C  1 393 ? 54.354  37.608  88.774  1.00 48.94  ? 393 ASP C OD1 1 
ATOM   10146 O  OD2 . ASP C  1 393 ? 56.191  38.899  88.653  1.00 44.51  ? 393 ASP C OD2 1 
ATOM   10147 N  N   . ILE C  1 394 ? 51.469  37.897  87.238  1.00 23.96  ? 394 ILE C N   1 
ATOM   10148 C  CA  . ILE C  1 394 ? 50.265  38.367  87.885  1.00 26.85  ? 394 ILE C CA  1 
ATOM   10149 C  C   . ILE C  1 394 ? 50.592  38.684  89.324  1.00 31.43  ? 394 ILE C C   1 
ATOM   10150 O  O   . ILE C  1 394 ? 51.142  37.846  90.053  1.00 37.21  ? 394 ILE C O   1 
ATOM   10151 C  CB  . ILE C  1 394 ? 49.192  37.297  87.802  1.00 24.64  ? 394 ILE C CB  1 
ATOM   10152 C  CG1 . ILE C  1 394 ? 48.831  37.090  86.330  1.00 22.79  ? 394 ILE C CG1 1 
ATOM   10153 C  CG2 . ILE C  1 394 ? 47.990  37.667  88.614  1.00 22.23  ? 394 ILE C CG2 1 
ATOM   10154 C  CD1 . ILE C  1 394 ? 47.835  35.983  86.116  1.00 24.17  ? 394 ILE C CD1 1 
ATOM   10155 N  N   . LYS C  1 395 ? 50.266  39.905  89.719  1.00 33.85  ? 395 LYS C N   1 
ATOM   10156 C  CA  . LYS C  1 395 ? 50.513  40.379  91.069  1.00 38.10  ? 395 LYS C CA  1 
ATOM   10157 C  C   . LYS C  1 395 ? 49.242  40.486  91.909  1.00 41.44  ? 395 LYS C C   1 
ATOM   10158 O  O   . LYS C  1 395 ? 49.133  39.932  93.001  1.00 43.14  ? 395 LYS C O   1 
ATOM   10159 C  CB  . LYS C  1 395 ? 51.141  41.778  91.009  1.00 35.66  ? 395 LYS C CB  1 
ATOM   10160 C  CG  . LYS C  1 395 ? 52.583  41.811  90.593  1.00 41.82  ? 395 LYS C CG  1 
ATOM   10161 C  CD  . LYS C  1 395 ? 53.463  41.403  91.765  1.00 53.37  ? 395 LYS C CD  1 
ATOM   10162 C  CE  . LYS C  1 395 ? 54.906  41.081  91.361  1.00 59.94  ? 395 LYS C CE  1 
ATOM   10163 N  NZ  . LYS C  1 395 ? 55.641  42.179  90.639  1.00 71.80  ? 395 LYS C NZ  1 
ATOM   10164 N  N   . ASN C  1 396 ? 48.265  41.176  91.345  1.00 45.61  ? 396 ASN C N   1 
ATOM   10165 C  CA  . ASN C  1 396 ? 47.025  41.531  92.011  1.00 46.44  ? 396 ASN C CA  1 
ATOM   10166 C  C   . ASN C  1 396 ? 45.840  41.103  91.180  1.00 47.21  ? 396 ASN C C   1 
ATOM   10167 O  O   . ASN C  1 396 ? 45.977  40.460  90.159  1.00 50.66  ? 396 ASN C O   1 
ATOM   10168 C  CB  . ASN C  1 396 ? 47.020  43.080  92.033  1.00 49.16  ? 396 ASN C CB  1 
ATOM   10169 C  CG  . ASN C  1 396 ? 47.527  43.647  93.316  1.00 59.56  ? 396 ASN C CG  1 
ATOM   10170 O  OD1 . ASN C  1 396 ? 46.814  43.539  94.288  1.00 74.73  ? 396 ASN C OD1 1 
ATOM   10171 N  ND2 . ASN C  1 396 ? 48.775  44.117  93.398  1.00 66.26  ? 396 ASN C ND2 1 
ATOM   10172 N  N   . ARG C  1 397 ? 44.665  41.545  91.582  1.00 46.75  ? 397 ARG C N   1 
ATOM   10173 C  CA  . ARG C  1 397 ? 43.492  41.297  90.779  1.00 49.14  ? 397 ARG C CA  1 
ATOM   10174 C  C   . ARG C  1 397 ? 43.497  42.490  89.823  1.00 51.20  ? 397 ARG C C   1 
ATOM   10175 O  O   . ARG C  1 397 ? 42.678  42.532  88.898  1.00 56.19  ? 397 ARG C O   1 
ATOM   10176 C  CB  . ARG C  1 397 ? 42.202  41.356  91.601  1.00 50.59  ? 397 ARG C CB  1 
ATOM   10177 C  CG  . ARG C  1 397 ? 41.677  42.761  91.831  1.00 52.53  ? 397 ARG C CG  1 
ATOM   10178 C  CD  . ARG C  1 397 ? 40.450  42.783  92.682  1.00 55.30  ? 397 ARG C CD  1 
ATOM   10179 N  NE  . ARG C  1 397 ? 40.747  42.369  94.052  1.00 59.11  ? 397 ARG C NE  1 
ATOM   10180 C  CZ  . ARG C  1 397 ? 39.840  42.290  95.024  1.00 60.33  ? 397 ARG C CZ  1 
ATOM   10181 N  NH1 . ARG C  1 397 ? 38.570  42.606  94.809  1.00 64.13  ? 397 ARG C NH1 1 
ATOM   10182 N  NH2 . ARG C  1 397 ? 40.189  41.862  96.217  1.00 61.43  ? 397 ARG C NH2 1 
ATOM   10183 N  N   . THR C  1 398 ? 44.351  43.488  90.098  1.00 47.34  ? 398 THR C N   1 
ATOM   10184 C  CA  . THR C  1 398 ? 44.440  44.707  89.272  1.00 50.17  ? 398 THR C CA  1 
ATOM   10185 C  C   . THR C  1 398 ? 45.728  44.842  88.493  1.00 52.25  ? 398 THR C C   1 
ATOM   10186 O  O   . THR C  1 398 ? 45.759  45.476  87.428  1.00 50.79  ? 398 THR C O   1 
ATOM   10187 C  CB  . THR C  1 398 ? 44.315  46.024  90.110  1.00 47.87  ? 398 THR C CB  1 
ATOM   10188 O  OG1 . THR C  1 398 ? 45.109  45.940  91.307  1.00 49.75  ? 398 THR C OG1 1 
ATOM   10189 C  CG2 . THR C  1 398 ? 42.856  46.341  90.436  1.00 50.12  ? 398 THR C CG2 1 
ATOM   10190 N  N   . HIS C  1 399 ? 46.792  44.255  89.036  1.00 55.91  ? 399 HIS C N   1 
ATOM   10191 C  CA  . HIS C  1 399 ? 48.108  44.341  88.400  1.00 53.43  ? 399 HIS C CA  1 
ATOM   10192 C  C   . HIS C  1 399 ? 48.793  43.067  87.950  1.00 49.77  ? 399 HIS C C   1 
ATOM   10193 O  O   . HIS C  1 399 ? 48.799  42.054  88.666  1.00 50.24  ? 399 HIS C O   1 
ATOM   10194 C  CB  . HIS C  1 399 ? 49.056  45.102  89.301  1.00 51.62  ? 399 HIS C CB  1 
ATOM   10195 C  CG  . HIS C  1 399 ? 48.651  46.519  89.505  1.00 50.89  ? 399 HIS C CG  1 
ATOM   10196 N  ND1 . HIS C  1 399 ? 49.348  47.578  88.966  1.00 50.03  ? 399 HIS C ND1 1 
ATOM   10197 C  CD2 . HIS C  1 399 ? 47.602  47.052  90.168  1.00 48.94  ? 399 HIS C CD2 1 
ATOM   10198 C  CE1 . HIS C  1 399 ? 48.749  48.706  89.295  1.00 50.90  ? 399 HIS C CE1 1 
ATOM   10199 N  NE2 . HIS C  1 399 ? 47.689  48.411  90.023  1.00 50.96  ? 399 HIS C NE2 1 
ATOM   10200 N  N   . ALA C  1 400 ? 49.415  43.167  86.782  1.00 45.18  ? 400 ALA C N   1 
ATOM   10201 C  CA  . ALA C  1 400 ? 50.168  42.079  86.175  1.00 43.81  ? 400 ALA C CA  1 
ATOM   10202 C  C   . ALA C  1 400 ? 51.261  42.760  85.403  1.00 40.01  ? 400 ALA C C   1 
ATOM   10203 O  O   . ALA C  1 400 ? 51.048  43.792  84.789  1.00 40.25  ? 400 ALA C O   1 
ATOM   10204 C  CB  . ALA C  1 400 ? 49.309  41.272  85.247  1.00 49.73  ? 400 ALA C CB  1 
ATOM   10205 N  N   . HIS C  1 401 ? 52.430  42.173  85.390  1.00 35.67  ? 401 HIS C N   1 
ATOM   10206 C  CA  . HIS C  1 401 ? 53.497  42.830  84.724  1.00 36.23  ? 401 HIS C CA  1 
ATOM   10207 C  C   . HIS C  1 401 ? 54.105  41.919  83.696  1.00 41.12  ? 401 HIS C C   1 
ATOM   10208 O  O   . HIS C  1 401 ? 54.539  40.809  84.015  1.00 45.50  ? 401 HIS C O   1 
ATOM   10209 C  CB  . HIS C  1 401 ? 54.504  43.237  85.775  1.00 38.15  ? 401 HIS C CB  1 
ATOM   10210 C  CG  . HIS C  1 401 ? 55.798  43.736  85.228  1.00 43.39  ? 401 HIS C CG  1 
ATOM   10211 N  ND1 . HIS C  1 401 ? 57.017  43.330  85.722  1.00 49.58  ? 401 HIS C ND1 1 
ATOM   10212 C  CD2 . HIS C  1 401 ? 56.065  44.616  84.238  1.00 43.21  ? 401 HIS C CD2 1 
ATOM   10213 C  CE1 . HIS C  1 401 ? 57.985  43.941  85.058  1.00 51.68  ? 401 HIS C CE1 1 
ATOM   10214 N  NE2 . HIS C  1 401 ? 57.432  44.727  84.153  1.00 48.75  ? 401 HIS C NE2 1 
ATOM   10215 N  N   . PHE C  1 402 ? 54.130  42.387  82.454  1.00 40.07  ? 402 PHE C N   1 
ATOM   10216 C  CA  . PHE C  1 402 ? 54.686  41.625  81.364  1.00 34.59  ? 402 PHE C CA  1 
ATOM   10217 C  C   . PHE C  1 402 ? 56.120  42.082  81.077  1.00 35.15  ? 402 PHE C C   1 
ATOM   10218 O  O   . PHE C  1 402 ? 56.418  43.271  81.180  1.00 36.89  ? 402 PHE C O   1 
ATOM   10219 C  CB  . PHE C  1 402 ? 53.798  41.769  80.140  1.00 30.28  ? 402 PHE C CB  1 
ATOM   10220 C  CG  . PHE C  1 402 ? 54.331  41.048  78.943  1.00 33.39  ? 402 PHE C CG  1 
ATOM   10221 C  CD1 . PHE C  1 402 ? 54.100  39.688  78.780  1.00 32.13  ? 402 PHE C CD1 1 
ATOM   10222 C  CD2 . PHE C  1 402 ? 55.116  41.710  78.007  1.00 31.23  ? 402 PHE C CD2 1 
ATOM   10223 C  CE1 . PHE C  1 402 ? 54.642  38.995  77.703  1.00 29.34  ? 402 PHE C CE1 1 
ATOM   10224 C  CE2 . PHE C  1 402 ? 55.670  41.040  76.927  1.00 30.94  ? 402 PHE C CE2 1 
ATOM   10225 C  CZ  . PHE C  1 402 ? 55.431  39.681  76.772  1.00 33.76  ? 402 PHE C CZ  1 
ATOM   10226 N  N   . SER C  1 403 ? 56.998  41.162  80.685  1.00 34.39  ? 403 SER C N   1 
ATOM   10227 C  CA  . SER C  1 403 ? 58.402  41.505  80.416  1.00 36.54  ? 403 SER C CA  1 
ATOM   10228 C  C   . SER C  1 403 ? 58.822  40.733  79.192  1.00 33.32  ? 403 SER C C   1 
ATOM   10229 O  O   . SER C  1 403 ? 58.214  39.721  78.914  1.00 39.93  ? 403 SER C O   1 
ATOM   10230 C  CB  . SER C  1 403 ? 59.284  41.044  81.572  1.00 42.93  ? 403 SER C CB  1 
ATOM   10231 O  OG  . SER C  1 403 ? 58.510  40.801  82.745  1.00 59.24  ? 403 SER C OG  1 
ATOM   10232 N  N   . TRP C  1 404 ? 59.833  41.197  78.470  1.00 23.83  ? 404 TRP C N   1 
ATOM   10233 C  CA  . TRP C  1 404 ? 60.323  40.508  77.293  1.00 23.34  ? 404 TRP C CA  1 
ATOM   10234 C  C   . TRP C  1 404 ? 61.809  40.527  77.436  1.00 26.25  ? 404 TRP C C   1 
ATOM   10235 O  O   . TRP C  1 404 ? 62.393  41.592  77.433  1.00 28.83  ? 404 TRP C O   1 
ATOM   10236 C  CB  . TRP C  1 404 ? 59.996  41.270  76.021  1.00 29.21  ? 404 TRP C CB  1 
ATOM   10237 C  CG  . TRP C  1 404 ? 60.577  40.622  74.773  1.00 33.83  ? 404 TRP C CG  1 
ATOM   10238 C  CD1 . TRP C  1 404 ? 60.410  39.334  74.389  1.00 33.80  ? 404 TRP C CD1 1 
ATOM   10239 C  CD2 . TRP C  1 404 ? 61.389  41.237  73.753  1.00 35.33  ? 404 TRP C CD2 1 
ATOM   10240 N  NE1 . TRP C  1 404 ? 61.054  39.103  73.207  1.00 34.99  ? 404 TRP C NE1 1 
ATOM   10241 C  CE2 . TRP C  1 404 ? 61.664  40.249  72.794  1.00 32.34  ? 404 TRP C CE2 1 
ATOM   10242 C  CE3 . TRP C  1 404 ? 61.903  42.521  73.559  1.00 36.71  ? 404 TRP C CE3 1 
ATOM   10243 C  CZ2 . TRP C  1 404 ? 62.426  40.499  71.661  1.00 34.75  ? 404 TRP C CZ2 1 
ATOM   10244 C  CZ3 . TRP C  1 404 ? 62.666  42.768  72.417  1.00 30.82  ? 404 TRP C CZ3 1 
ATOM   10245 C  CH2 . TRP C  1 404 ? 62.917  41.765  71.491  1.00 34.75  ? 404 TRP C CH2 1 
ATOM   10246 N  N   . ASN C  1 405 ? 62.436  39.367  77.541  1.00 25.88  ? 405 ASN C N   1 
ATOM   10247 C  CA  . ASN C  1 405 ? 63.882  39.296  77.718  1.00 25.07  ? 405 ASN C CA  1 
ATOM   10248 C  C   . ASN C  1 405 ? 64.588  38.865  76.453  1.00 25.42  ? 405 ASN C C   1 
ATOM   10249 O  O   . ASN C  1 405 ? 64.373  37.765  75.965  1.00 30.15  ? 405 ASN C O   1 
ATOM   10250 C  CB  . ASN C  1 405 ? 64.220  38.327  78.848  1.00 30.52  ? 405 ASN C CB  1 
ATOM   10251 C  CG  . ASN C  1 405 ? 65.691  37.947  78.864  1.00 36.04  ? 405 ASN C CG  1 
ATOM   10252 O  OD1 . ASN C  1 405 ? 66.086  36.919  78.290  1.00 41.08  ? 405 ASN C OD1 1 
ATOM   10253 N  ND2 . ASN C  1 405 ? 66.513  38.775  79.510  1.00 35.11  ? 405 ASN C ND2 1 
ATOM   10254 N  N   . ARG C  1 406 ? 65.431  39.718  75.900  1.00 26.47  ? 406 ARG C N   1 
ATOM   10255 C  CA  . ARG C  1 406 ? 66.117  39.336  74.663  1.00 29.01  ? 406 ARG C CA  1 
ATOM   10256 C  C   . ARG C  1 406 ? 67.205  38.325  74.896  1.00 28.87  ? 406 ARG C C   1 
ATOM   10257 O  O   . ARG C  1 406 ? 67.798  38.273  75.969  1.00 28.48  ? 406 ARG C O   1 
ATOM   10258 C  CB  . ARG C  1 406 ? 66.692  40.543  73.967  1.00 24.27  ? 406 ARG C CB  1 
ATOM   10259 C  CG  . ARG C  1 406 ? 65.625  41.456  73.551  1.00 29.93  ? 406 ARG C CG  1 
ATOM   10260 C  CD  . ARG C  1 406 ? 66.210  42.469  72.685  1.00 37.15  ? 406 ARG C CD  1 
ATOM   10261 N  NE  . ARG C  1 406 ? 67.365  43.069  73.335  1.00 38.81  ? 406 ARG C NE  1 
ATOM   10262 C  CZ  . ARG C  1 406 ? 68.249  43.834  72.703  1.00 45.36  ? 406 ARG C CZ  1 
ATOM   10263 N  NH1 . ARG C  1 406 ? 68.114  44.103  71.406  1.00 48.04  ? 406 ARG C NH1 1 
ATOM   10264 N  NH2 . ARG C  1 406 ? 69.286  44.325  73.361  1.00 50.64  ? 406 ARG C NH2 1 
ATOM   10265 N  N   . ASN C  1 407 ? 67.487  37.517  73.893  1.00 32.33  ? 407 ASN C N   1 
ATOM   10266 C  CA  . ASN C  1 407 ? 68.514  36.499  74.073  1.00 35.40  ? 407 ASN C CA  1 
ATOM   10267 C  C   . ASN C  1 407 ? 69.884  37.149  74.180  1.00 38.80  ? 407 ASN C C   1 
ATOM   10268 O  O   . ASN C  1 407 ? 70.767  36.608  74.826  1.00 37.44  ? 407 ASN C O   1 
ATOM   10269 C  CB  . ASN C  1 407 ? 68.510  35.465  72.943  1.00 31.32  ? 407 ASN C CB  1 
ATOM   10270 C  CG  . ASN C  1 407 ? 67.579  34.273  73.212  1.00 31.54  ? 407 ASN C CG  1 
ATOM   10271 O  OD1 . ASN C  1 407 ? 66.782  34.289  74.163  1.00 34.17  ? 407 ASN C OD1 1 
ATOM   10272 N  ND2 . ASN C  1 407 ? 67.715  33.208  72.400  1.00 23.86  ? 407 ASN C ND2 1 
ATOM   10273 N  N   . GLN C  1 408 ? 70.059  38.301  73.543  1.00 39.62  ? 408 GLN C N   1 
ATOM   10274 C  CA  . GLN C  1 408 ? 71.339  38.998  73.574  1.00 40.13  ? 408 GLN C CA  1 
ATOM   10275 C  C   . GLN C  1 408 ? 71.634  39.630  74.918  1.00 43.48  ? 408 GLN C C   1 
ATOM   10276 O  O   . GLN C  1 408 ? 72.796  39.883  75.229  1.00 48.35  ? 408 GLN C O   1 
ATOM   10277 C  CB  . GLN C  1 408 ? 71.382  40.141  72.560  1.00 39.21  ? 408 GLN C CB  1 
ATOM   10278 C  CG  . GLN C  1 408 ? 70.814  39.847  71.233  1.00 43.99  ? 408 GLN C CG  1 
ATOM   10279 C  CD  . GLN C  1 408 ? 69.389  40.247  71.156  1.00 46.27  ? 408 GLN C CD  1 
ATOM   10280 O  OE1 . GLN C  1 408 ? 68.493  39.490  71.531  1.00 50.68  ? 408 GLN C OE1 1 
ATOM   10281 N  NE2 . GLN C  1 408 ? 69.156  41.454  70.712  1.00 50.82  ? 408 GLN C NE2 1 
ATOM   10282 N  N   . ASP C  1 409 ? 70.587  40.006  75.652  1.00 39.32  ? 409 ASP C N   1 
ATOM   10283 C  CA  . ASP C  1 409 ? 70.769  40.646  76.942  1.00 34.32  ? 409 ASP C CA  1 
ATOM   10284 C  C   . ASP C  1 409 ? 71.100  39.579  77.964  1.00 32.66  ? 409 ASP C C   1 
ATOM   10285 O  O   . ASP C  1 409 ? 71.092  38.401  77.691  1.00 34.67  ? 409 ASP C O   1 
ATOM   10286 C  CB  . ASP C  1 409 ? 69.494  41.374  77.383  1.00 35.77  ? 409 ASP C CB  1 
ATOM   10287 C  CG  . ASP C  1 409 ? 68.920  42.292  76.312  1.00 43.18  ? 409 ASP C CG  1 
ATOM   10288 O  OD1 . ASP C  1 409 ? 69.747  42.772  75.496  1.00 36.30  ? 409 ASP C OD1 1 
ATOM   10289 O  OD2 . ASP C  1 409 ? 67.653  42.509  76.306  1.00 45.62  ? 409 ASP C OD2 1 
ATOM   10290 N  N   . GLY C  1 410 ? 71.415  40.003  79.163  1.00 35.03  ? 410 GLY C N   1 
ATOM   10291 C  CA  . GLY C  1 410 ? 71.712  39.041  80.186  1.00 32.97  ? 410 GLY C CA  1 
ATOM   10292 C  C   . GLY C  1 410 ? 70.368  38.603  80.706  1.00 31.70  ? 410 GLY C C   1 
ATOM   10293 O  O   . GLY C  1 410 ? 69.349  39.273  80.558  1.00 29.87  ? 410 GLY C O   1 
ATOM   10294 N  N   . VAL C  1 411 ? 70.396  37.486  81.388  1.00 30.91  ? 411 VAL C N   1 
ATOM   10295 C  CA  . VAL C  1 411 ? 69.218  36.893  81.934  1.00 35.59  ? 411 VAL C CA  1 
ATOM   10296 C  C   . VAL C  1 411 ? 68.226  37.791  82.647  1.00 36.95  ? 411 VAL C C   1 
ATOM   10297 O  O   . VAL C  1 411 ? 66.999  37.531  82.636  1.00 41.11  ? 411 VAL C O   1 
ATOM   10298 C  CB  . VAL C  1 411 ? 69.652  35.781  82.851  1.00 41.05  ? 411 VAL C CB  1 
ATOM   10299 C  CG1 . VAL C  1 411 ? 68.533  35.379  83.837  1.00 46.57  ? 411 VAL C CG1 1 
ATOM   10300 C  CG2 . VAL C  1 411 ? 70.112  34.598  81.998  1.00 44.58  ? 411 VAL C CG2 1 
ATOM   10301 N  N   . ALA C  1 412 ? 68.734  38.842  83.266  1.00 38.74  ? 412 ALA C N   1 
ATOM   10302 C  CA  . ALA C  1 412 ? 67.846  39.714  84.008  1.00 39.94  ? 412 ALA C CA  1 
ATOM   10303 C  C   . ALA C  1 412 ? 67.452  41.020  83.341  1.00 40.31  ? 412 ALA C C   1 
ATOM   10304 O  O   . ALA C  1 412 ? 66.738  41.809  83.941  1.00 42.69  ? 412 ALA C O   1 
ATOM   10305 C  CB  . ALA C  1 412 ? 68.412  39.969  85.348  1.00 39.16  ? 412 ALA C CB  1 
ATOM   10306 N  N   . VAL C  1 413 ? 67.849  41.213  82.090  1.00 37.88  ? 413 VAL C N   1 
ATOM   10307 C  CA  . VAL C  1 413 ? 67.533  42.436  81.383  1.00 36.09  ? 413 VAL C CA  1 
ATOM   10308 C  C   . VAL C  1 413 ? 66.239  42.402  80.574  1.00 39.75  ? 413 VAL C C   1 
ATOM   10309 O  O   . VAL C  1 413 ? 66.173  41.836  79.454  1.00 45.41  ? 413 VAL C O   1 
ATOM   10310 C  CB  . VAL C  1 413 ? 68.657  42.791  80.457  1.00 36.40  ? 413 VAL C CB  1 
ATOM   10311 C  CG1 . VAL C  1 413 ? 68.357  44.071  79.697  1.00 38.85  ? 413 VAL C CG1 1 
ATOM   10312 C  CG2 . VAL C  1 413 ? 69.931  42.871  81.215  1.00 38.42  ? 413 VAL C CG2 1 
ATOM   10313 N  N   . GLU C  1 414 ? 65.232  43.088  81.092  1.00 41.85  ? 414 GLU C N   1 
ATOM   10314 C  CA  . GLU C  1 414 ? 63.943  43.161  80.425  1.00 47.79  ? 414 GLU C CA  1 
ATOM   10315 C  C   . GLU C  1 414 ? 64.016  44.200  79.291  1.00 47.90  ? 414 GLU C C   1 
ATOM   10316 O  O   . GLU C  1 414 ? 63.882  45.389  79.544  1.00 54.97  ? 414 GLU C O   1 
ATOM   10317 C  CB  . GLU C  1 414 ? 62.876  43.597  81.421  1.00 51.48  ? 414 GLU C CB  1 
ATOM   10318 C  CG  . GLU C  1 414 ? 62.750  42.767  82.676  1.00 66.27  ? 414 GLU C CG  1 
ATOM   10319 C  CD  . GLU C  1 414 ? 61.666  43.314  83.648  1.00 79.42  ? 414 GLU C CD  1 
ATOM   10320 O  OE1 . GLU C  1 414 ? 60.905  44.258  83.296  1.00 84.09  ? 414 GLU C OE1 1 
ATOM   10321 O  OE2 . GLU C  1 414 ? 61.566  42.792  84.782  1.00 88.42  ? 414 GLU C OE2 1 
ATOM   10322 N  N   . ALA C  1 415 ? 64.203  43.776  78.045  1.00 44.67  ? 415 ALA C N   1 
ATOM   10323 C  CA  . ALA C  1 415 ? 64.265  44.733  76.938  1.00 40.80  ? 415 ALA C CA  1 
ATOM   10324 C  C   . ALA C  1 415 ? 62.931  45.440  76.668  1.00 40.75  ? 415 ALA C C   1 
ATOM   10325 O  O   . ALA C  1 415 ? 62.840  46.294  75.800  1.00 46.28  ? 415 ALA C O   1 
ATOM   10326 C  CB  . ALA C  1 415 ? 64.761  44.060  75.692  1.00 40.00  ? 415 ALA C CB  1 
ATOM   10327 N  N   . ASP C  1 416 ? 61.880  45.029  77.355  1.00 39.21  ? 416 ASP C N   1 
ATOM   10328 C  CA  . ASP C  1 416 ? 60.561  45.639  77.240  1.00 36.62  ? 416 ASP C CA  1 
ATOM   10329 C  C   . ASP C  1 416 ? 59.821  45.249  78.510  1.00 40.95  ? 416 ASP C C   1 
ATOM   10330 O  O   . ASP C  1 416 ? 59.966  44.136  79.030  1.00 44.94  ? 416 ASP C O   1 
ATOM   10331 C  CB  . ASP C  1 416 ? 59.813  45.112  76.052  1.00 39.67  ? 416 ASP C CB  1 
ATOM   10332 C  CG  . ASP C  1 416 ? 58.591  45.917  75.739  1.00 42.38  ? 416 ASP C CG  1 
ATOM   10333 O  OD1 . ASP C  1 416 ? 57.956  46.470  76.647  1.00 41.50  ? 416 ASP C OD1 1 
ATOM   10334 O  OD2 . ASP C  1 416 ? 58.260  46.003  74.553  1.00 50.86  ? 416 ASP C OD2 1 
ATOM   10335 N  N   . SER C  1 417 ? 59.002  46.147  79.004  1.00 37.95  ? 417 SER C N   1 
ATOM   10336 C  CA  . SER C  1 417 ? 58.334  45.883  80.232  1.00 39.34  ? 417 SER C CA  1 
ATOM   10337 C  C   . SER C  1 417 ? 57.103  46.739  80.201  1.00 41.31  ? 417 SER C C   1 
ATOM   10338 O  O   . SER C  1 417 ? 57.141  47.840  79.677  1.00 47.10  ? 417 SER C O   1 
ATOM   10339 C  CB  . SER C  1 417 ? 59.294  46.264  81.361  1.00 33.50  ? 417 SER C CB  1 
ATOM   10340 O  OG  . SER C  1 417 ? 58.613  46.689  82.503  1.00 45.19  ? 417 SER C OG  1 
ATOM   10341 N  N   . VAL C  1 418 ? 56.009  46.220  80.737  1.00 42.33  ? 418 VAL C N   1 
ATOM   10342 C  CA  . VAL C  1 418 ? 54.737  46.912  80.736  1.00 42.62  ? 418 VAL C CA  1 
ATOM   10343 C  C   . VAL C  1 418 ? 53.843  46.440  81.882  1.00 43.38  ? 418 VAL C C   1 
ATOM   10344 O  O   . VAL C  1 418 ? 53.878  45.261  82.244  1.00 48.64  ? 418 VAL C O   1 
ATOM   10345 C  CB  . VAL C  1 418 ? 53.995  46.566  79.459  1.00 43.98  ? 418 VAL C CB  1 
ATOM   10346 C  CG1 . VAL C  1 418 ? 52.621  47.224  79.441  1.00 48.74  ? 418 VAL C CG1 1 
ATOM   10347 C  CG2 . VAL C  1 418 ? 54.807  46.956  78.259  1.00 46.87  ? 418 VAL C CG2 1 
ATOM   10348 N  N   . TRP C  1 419 ? 53.061  47.340  82.470  1.00 40.36  ? 419 TRP C N   1 
ATOM   10349 C  CA  . TRP C  1 419 ? 52.157  46.916  83.518  1.00 36.33  ? 419 TRP C CA  1 
ATOM   10350 C  C   . TRP C  1 419 ? 50.796  46.758  82.891  1.00 33.45  ? 419 TRP C C   1 
ATOM   10351 O  O   . TRP C  1 419 ? 50.398  47.546  82.066  1.00 39.95  ? 419 TRP C O   1 
ATOM   10352 C  CB  . TRP C  1 419 ? 52.117  47.927  84.647  1.00 36.51  ? 419 TRP C CB  1 
ATOM   10353 C  CG  . TRP C  1 419 ? 53.203  47.714  85.612  1.00 36.74  ? 419 TRP C CG  1 
ATOM   10354 C  CD1 . TRP C  1 419 ? 54.421  48.300  85.597  1.00 42.50  ? 419 TRP C CD1 1 
ATOM   10355 C  CD2 . TRP C  1 419 ? 53.200  46.818  86.728  1.00 41.04  ? 419 TRP C CD2 1 
ATOM   10356 N  NE1 . TRP C  1 419 ? 55.199  47.833  86.643  1.00 46.92  ? 419 TRP C NE1 1 
ATOM   10357 C  CE2 . TRP C  1 419 ? 54.473  46.919  87.352  1.00 41.66  ? 419 TRP C CE2 1 
ATOM   10358 C  CE3 . TRP C  1 419 ? 52.251  45.938  87.260  1.00 41.43  ? 419 TRP C CE3 1 
ATOM   10359 C  CZ2 . TRP C  1 419 ? 54.824  46.178  88.473  1.00 33.88  ? 419 TRP C CZ2 1 
ATOM   10360 C  CZ3 . TRP C  1 419 ? 52.598  45.199  88.382  1.00 44.79  ? 419 TRP C CZ3 1 
ATOM   10361 C  CH2 . TRP C  1 419 ? 53.885  45.328  88.975  1.00 40.89  ? 419 TRP C CH2 1 
ATOM   10362 N  N   . PHE C  1 420 ? 50.083  45.718  83.237  1.00 30.73  ? 420 PHE C N   1 
ATOM   10363 C  CA  . PHE C  1 420 ? 48.776  45.537  82.674  1.00 34.29  ? 420 PHE C CA  1 
ATOM   10364 C  C   . PHE C  1 420 ? 47.795  45.926  83.757  1.00 37.27  ? 420 PHE C C   1 
ATOM   10365 O  O   . PHE C  1 420 ? 47.989  45.564  84.919  1.00 41.67  ? 420 PHE C O   1 
ATOM   10366 C  CB  . PHE C  1 420 ? 48.576  44.062  82.307  1.00 38.81  ? 420 PHE C CB  1 
ATOM   10367 C  CG  . PHE C  1 420 ? 49.107  43.695  80.961  1.00 36.78  ? 420 PHE C CG  1 
ATOM   10368 C  CD1 . PHE C  1 420 ? 50.464  43.597  80.717  1.00 34.38  ? 420 PHE C CD1 1 
ATOM   10369 C  CD2 . PHE C  1 420 ? 48.233  43.501  79.909  1.00 43.40  ? 420 PHE C CD2 1 
ATOM   10370 C  CE1 . PHE C  1 420 ? 50.932  43.315  79.429  1.00 37.75  ? 420 PHE C CE1 1 
ATOM   10371 C  CE2 . PHE C  1 420 ? 48.703  43.216  78.605  1.00 42.18  ? 420 PHE C CE2 1 
ATOM   10372 C  CZ  . PHE C  1 420 ? 50.044  43.126  78.371  1.00 34.97  ? 420 PHE C CZ  1 
ATOM   10373 N  N   . PHE C  1 421 ? 46.787  46.713  83.403  1.00 36.43  ? 421 PHE C N   1 
ATOM   10374 C  CA  . PHE C  1 421 ? 45.764  47.108  84.354  1.00 34.30  ? 421 PHE C CA  1 
ATOM   10375 C  C   . PHE C  1 421 ? 44.587  46.282  83.934  1.00 33.03  ? 421 PHE C C   1 
ATOM   10376 O  O   . PHE C  1 421 ? 44.189  46.292  82.776  1.00 33.73  ? 421 PHE C O   1 
ATOM   10377 C  CB  . PHE C  1 421 ? 45.488  48.587  84.259  1.00 31.62  ? 421 PHE C CB  1 
ATOM   10378 C  CG  . PHE C  1 421 ? 46.623  49.394  84.716  1.00 32.92  ? 421 PHE C CG  1 
ATOM   10379 C  CD1 . PHE C  1 421 ? 47.402  48.959  85.777  1.00 37.64  ? 421 PHE C CD1 1 
ATOM   10380 C  CD2 . PHE C  1 421 ? 46.970  50.543  84.066  1.00 35.44  ? 421 PHE C CD2 1 
ATOM   10381 C  CE1 . PHE C  1 421 ? 48.523  49.668  86.178  1.00 42.08  ? 421 PHE C CE1 1 
ATOM   10382 C  CE2 . PHE C  1 421 ? 48.089  51.259  84.457  1.00 42.38  ? 421 PHE C CE2 1 
ATOM   10383 C  CZ  . PHE C  1 421 ? 48.868  50.817  85.517  1.00 42.08  ? 421 PHE C CZ  1 
ATOM   10384 N  N   . ASN C  1 422 ? 44.081  45.506  84.873  1.00 32.72  ? 422 ASN C N   1 
ATOM   10385 C  CA  . ASN C  1 422 ? 42.999  44.592  84.604  1.00 33.55  ? 422 ASN C CA  1 
ATOM   10386 C  C   . ASN C  1 422 ? 41.781  45.209  83.985  1.00 35.70  ? 422 ASN C C   1 
ATOM   10387 O  O   . ASN C  1 422 ? 41.120  46.024  84.624  1.00 41.23  ? 422 ASN C O   1 
ATOM   10388 C  CB  . ASN C  1 422 ? 42.613  43.885  85.883  1.00 37.48  ? 422 ASN C CB  1 
ATOM   10389 C  CG  . ASN C  1 422 ? 41.574  42.826  85.653  1.00 39.85  ? 422 ASN C CG  1 
ATOM   10390 O  OD1 . ASN C  1 422 ? 40.401  43.128  85.587  1.00 41.30  ? 422 ASN C OD1 1 
ATOM   10391 N  ND2 . ASN C  1 422 ? 42.001  41.574  85.505  1.00 39.74  ? 422 ASN C ND2 1 
ATOM   10392 N  N   . ARG C  1 423 ? 41.445  44.772  82.771  1.00 36.11  ? 423 ARG C N   1 
ATOM   10393 C  CA  . ARG C  1 423 ? 40.273  45.282  82.040  1.00 36.67  ? 423 ARG C CA  1 
ATOM   10394 C  C   . ARG C  1 423 ? 38.979  45.208  82.797  1.00 36.20  ? 423 ARG C C   1 
ATOM   10395 O  O   . ARG C  1 423 ? 37.990  45.764  82.356  1.00 42.24  ? 423 ARG C O   1 
ATOM   10396 C  CB  . ARG C  1 423 ? 40.052  44.571  80.700  1.00 36.52  ? 423 ARG C CB  1 
ATOM   10397 C  CG  . ARG C  1 423 ? 41.058  44.916  79.613  1.00 32.54  ? 423 ARG C CG  1 
ATOM   10398 C  CD  . ARG C  1 423 ? 41.194  46.403  79.441  1.00 31.13  ? 423 ARG C CD  1 
ATOM   10399 N  NE  . ARG C  1 423 ? 42.115  46.980  80.410  1.00 31.24  ? 423 ARG C NE  1 
ATOM   10400 C  CZ  . ARG C  1 423 ? 42.509  48.243  80.377  1.00 30.80  ? 423 ARG C CZ  1 
ATOM   10401 N  NH1 . ARG C  1 423 ? 42.041  49.028  79.429  1.00 37.60  ? 423 ARG C NH1 1 
ATOM   10402 N  NH2 . ARG C  1 423 ? 43.411  48.701  81.239  1.00 31.46  ? 423 ARG C NH2 1 
ATOM   10403 N  N   . HIS C  1 424 ? 38.955  44.469  83.893  1.00 35.40  ? 424 HIS C N   1 
ATOM   10404 C  CA  . HIS C  1 424 ? 37.747  44.360  84.705  1.00 35.81  ? 424 HIS C CA  1 
ATOM   10405 C  C   . HIS C  1 424 ? 37.815  45.148  86.018  1.00 36.28  ? 424 HIS C C   1 
ATOM   10406 O  O   . HIS C  1 424 ? 36.963  45.970  86.287  1.00 35.70  ? 424 HIS C O   1 
ATOM   10407 C  CB  . HIS C  1 424 ? 37.451  42.910  84.987  1.00 32.89  ? 424 HIS C CB  1 
ATOM   10408 C  CG  . HIS C  1 424 ? 36.278  42.710  85.863  1.00 37.17  ? 424 HIS C CG  1 
ATOM   10409 N  ND1 . HIS C  1 424 ? 34.987  42.702  85.376  1.00 40.61  ? 424 HIS C ND1 1 
ATOM   10410 C  CD2 . HIS C  1 424 ? 36.186  42.486  87.196  1.00 40.85  ? 424 HIS C CD2 1 
ATOM   10411 C  CE1 . HIS C  1 424 ? 34.149  42.477  86.377  1.00 40.86  ? 424 HIS C CE1 1 
ATOM   10412 N  NE2 . HIS C  1 424 ? 34.849  42.342  87.493  1.00 39.21  ? 424 HIS C NE2 1 
ATOM   10413 N  N   . TRP C  1 425 ? 38.806  44.879  86.851  1.00 38.93  ? 425 TRP C N   1 
ATOM   10414 C  CA  . TRP C  1 425 ? 38.903  45.596  88.105  1.00 39.36  ? 425 TRP C CA  1 
ATOM   10415 C  C   . TRP C  1 425 ? 39.697  46.874  87.992  1.00 43.85  ? 425 TRP C C   1 
ATOM   10416 O  O   . TRP C  1 425 ? 39.878  47.536  89.001  1.00 52.29  ? 425 TRP C O   1 
ATOM   10417 C  CB  . TRP C  1 425 ? 39.522  44.735  89.230  1.00 34.83  ? 425 TRP C CB  1 
ATOM   10418 C  CG  . TRP C  1 425 ? 38.787  43.538  89.512  1.00 31.52  ? 425 TRP C CG  1 
ATOM   10419 C  CD1 . TRP C  1 425 ? 38.869  42.375  88.832  1.00 34.36  ? 425 TRP C CD1 1 
ATOM   10420 C  CD2 . TRP C  1 425 ? 37.760  43.372  90.484  1.00 32.92  ? 425 TRP C CD2 1 
ATOM   10421 N  NE1 . TRP C  1 425 ? 37.940  41.480  89.304  1.00 34.58  ? 425 TRP C NE1 1 
ATOM   10422 C  CE2 . TRP C  1 425 ? 37.238  42.074  90.322  1.00 38.34  ? 425 TRP C CE2 1 
ATOM   10423 C  CE3 . TRP C  1 425 ? 37.211  44.192  91.469  1.00 32.13  ? 425 TRP C CE3 1 
ATOM   10424 C  CZ2 . TRP C  1 425 ? 36.172  41.575  91.122  1.00 40.89  ? 425 TRP C CZ2 1 
ATOM   10425 C  CZ3 . TRP C  1 425 ? 36.150  43.695  92.261  1.00 33.83  ? 425 TRP C CZ3 1 
ATOM   10426 C  CH2 . TRP C  1 425 ? 35.646  42.406  92.081  1.00 34.09  ? 425 TRP C CH2 1 
ATOM   10427 N  N   . TYR C  1 426 ? 40.201  47.259  86.832  1.00 43.30  ? 426 TYR C N   1 
ATOM   10428 C  CA  . TYR C  1 426 ? 40.989  48.490  86.845  1.00 46.15  ? 426 TYR C CA  1 
ATOM   10429 C  C   . TYR C  1 426 ? 41.303  48.979  85.469  1.00 46.24  ? 426 TYR C C   1 
ATOM   10430 O  O   . TYR C  1 426 ? 42.454  49.236  85.136  1.00 46.73  ? 426 TYR C O   1 
ATOM   10431 C  CB  . TYR C  1 426 ? 42.277  48.270  87.645  1.00 48.46  ? 426 TYR C CB  1 
ATOM   10432 C  CG  . TYR C  1 426 ? 43.205  49.448  87.766  1.00 55.56  ? 426 TYR C CG  1 
ATOM   10433 C  CD1 . TYR C  1 426 ? 42.878  50.546  88.539  1.00 60.87  ? 426 TYR C CD1 1 
ATOM   10434 C  CD2 . TYR C  1 426 ? 44.462  49.430  87.159  1.00 60.47  ? 426 TYR C CD2 1 
ATOM   10435 C  CE1 . TYR C  1 426 ? 43.804  51.624  88.712  1.00 67.35  ? 426 TYR C CE1 1 
ATOM   10436 C  CE2 . TYR C  1 426 ? 45.383  50.487  87.320  1.00 64.84  ? 426 TYR C CE2 1 
ATOM   10437 C  CZ  . TYR C  1 426 ? 45.058  51.583  88.096  1.00 67.07  ? 426 TYR C CZ  1 
ATOM   10438 O  OH  . TYR C  1 426 ? 45.981  52.614  88.243  1.00 67.25  ? 426 TYR C OH  1 
ATOM   10439 N  N   . PRO C  1 427 ? 40.262  49.163  84.654  1.00 47.99  ? 427 PRO C N   1 
ATOM   10440 C  CA  . PRO C  1 427 ? 40.361  49.633  83.274  1.00 50.49  ? 427 PRO C CA  1 
ATOM   10441 C  C   . PRO C  1 427 ? 40.887  51.042  83.194  1.00 57.25  ? 427 PRO C C   1 
ATOM   10442 O  O   . PRO C  1 427 ? 40.184  51.950  82.800  1.00 61.59  ? 427 PRO C O   1 
ATOM   10443 C  CB  . PRO C  1 427 ? 38.925  49.562  82.795  1.00 46.76  ? 427 PRO C CB  1 
ATOM   10444 C  CG  . PRO C  1 427 ? 38.159  49.842  84.027  1.00 46.87  ? 427 PRO C CG  1 
ATOM   10445 C  CD  . PRO C  1 427 ? 38.856  49.038  85.068  1.00 45.53  ? 427 PRO C CD  1 
ATOM   10446 N  N   . VAL C  1 428 ? 42.117  51.226  83.625  1.00 64.46  ? 428 VAL C N   1 
ATOM   10447 C  CA  . VAL C  1 428 ? 42.767  52.517  83.588  1.00 72.45  ? 428 VAL C CA  1 
ATOM   10448 C  C   . VAL C  1 428 ? 43.697  52.429  82.369  1.00 76.76  ? 428 VAL C C   1 
ATOM   10449 O  O   . VAL C  1 428 ? 44.232  51.356  82.077  1.00 79.35  ? 428 VAL C O   1 
ATOM   10450 C  CB  . VAL C  1 428 ? 43.574  52.723  84.910  1.00 74.77  ? 428 VAL C CB  1 
ATOM   10451 C  CG1 . VAL C  1 428 ? 44.995  53.232  84.643  1.00 74.03  ? 428 VAL C CG1 1 
ATOM   10452 C  CG2 . VAL C  1 428 ? 42.834  53.675  85.825  1.00 77.61  ? 428 VAL C CG2 1 
ATOM   10453 N  N   . ASP C  1 429 ? 43.892  53.523  81.649  1.00 80.05  ? 429 ASP C N   1 
ATOM   10454 C  CA  . ASP C  1 429 ? 44.774  53.464  80.493  1.00 85.21  ? 429 ASP C CA  1 
ATOM   10455 C  C   . ASP C  1 429 ? 46.179  52.971  80.845  1.00 86.21  ? 429 ASP C C   1 
ATOM   10456 O  O   . ASP C  1 429 ? 46.927  53.638  81.569  1.00 84.11  ? 429 ASP C O   1 
ATOM   10457 C  CB  . ASP C  1 429 ? 44.862  54.827  79.772  1.00 90.28  ? 429 ASP C CB  1 
ATOM   10458 C  CG  . ASP C  1 429 ? 45.611  54.752  78.411  1.00 93.77  ? 429 ASP C CG  1 
ATOM   10459 O  OD1 . ASP C  1 429 ? 46.841  54.496  78.394  1.00 95.86  ? 429 ASP C OD1 1 
ATOM   10460 O  OD2 . ASP C  1 429 ? 44.970  54.979  77.354  1.00 97.63  ? 429 ASP C OD2 1 
ATOM   10461 N  N   . ASP C  1 430 ? 46.478  51.747  80.419  1.00 88.97  ? 430 ASP C N   1 
ATOM   10462 C  CA  . ASP C  1 430 ? 47.813  51.190  80.590  1.00 90.46  ? 430 ASP C CA  1 
ATOM   10463 C  C   . ASP C  1 430 ? 48.485  51.402  79.248  1.00 93.07  ? 430 ASP C C   1 
ATOM   10464 O  O   . ASP C  1 430 ? 49.698  51.470  79.170  1.00 89.53  ? 430 ASP C O   1 
ATOM   10465 C  CB  . ASP C  1 430 ? 47.815  49.692  80.991  1.00 87.77  ? 430 ASP C CB  1 
ATOM   10466 C  CG  . ASP C  1 430 ? 46.791  48.846  80.242  1.00 89.80  ? 430 ASP C CG  1 
ATOM   10467 O  OD1 . ASP C  1 430 ? 46.211  49.308  79.234  1.00 92.39  ? 430 ASP C OD1 1 
ATOM   10468 O  OD2 . ASP C  1 430 ? 46.574  47.696  80.683  1.00 89.81  ? 430 ASP C OD2 1 
ATOM   10469 N  N   . SER C  1 431 ? 47.658  51.578  78.212  1.00 100.58 ? 431 SER C N   1 
ATOM   10470 C  CA  . SER C  1 431 ? 48.101  51.791  76.835  1.00 104.80 ? 431 SER C CA  1 
ATOM   10471 C  C   . SER C  1 431 ? 48.987  53.002  76.683  1.00 107.76 ? 431 SER C C   1 
ATOM   10472 O  O   . SER C  1 431 ? 48.515  54.094  76.346  1.00 107.06 ? 431 SER C O   1 
ATOM   10473 C  CB  . SER C  1 431 ? 46.905  51.907  75.875  1.00 104.72 ? 431 SER C CB  1 
ATOM   10474 O  OG  . SER C  1 431 ? 46.583  50.650  75.306  1.00 103.33 ? 431 SER C OG  1 
ATOM   10475 N  N   . THR C  1 432 ? 50.264  52.792  76.986  1.00 114.34 ? 432 THR C N   1 
ATOM   10476 C  CA  . THR C  1 432 ? 51.299  53.812  76.863  1.00 121.72 ? 432 THR C CA  1 
ATOM   10477 C  C   . THR C  1 432 ? 52.250  53.367  75.721  1.00 124.89 ? 432 THR C C   1 
ATOM   10478 O  O   . THR C  1 432 ? 52.534  54.210  74.825  1.00 127.11 ? 432 THR C O   1 
ATOM   10479 C  CB  . THR C  1 432 ? 52.109  54.029  78.210  1.00 122.72 ? 432 THR C CB  1 
ATOM   10480 O  OG1 . THR C  1 432 ? 52.801  52.824  78.586  1.00 123.92 ? 432 THR C OG1 1 
ATOM   10481 C  CG2 . THR C  1 432 ? 51.176  54.474  79.352  1.00 121.30 ? 432 THR C CG2 1 
ATOM   10482 O  OXT . THR C  1 432 ? 52.655  52.165  75.707  1.00 125.38 ? 432 THR C OXT 1 
ATOM   10483 N  N   . ARG D  1 9   ? 58.954  116.016 63.154  1.00 59.74  ? 9   ARG D N   1 
ATOM   10484 C  CA  . ARG D  1 9   ? 58.028  115.365 64.122  1.00 58.83  ? 9   ARG D CA  1 
ATOM   10485 C  C   . ARG D  1 9   ? 57.217  114.267 63.427  1.00 55.06  ? 9   ARG D C   1 
ATOM   10486 O  O   . ARG D  1 9   ? 56.001  114.401 63.214  1.00 50.70  ? 9   ARG D O   1 
ATOM   10487 C  CB  . ARG D  1 9   ? 57.120  116.428 64.751  1.00 65.91  ? 9   ARG D CB  1 
ATOM   10488 C  CG  . ARG D  1 9   ? 56.371  117.312 63.756  1.00 73.18  ? 9   ARG D CG  1 
ATOM   10489 C  CD  . ARG D  1 9   ? 56.084  118.700 64.338  1.00 79.79  ? 9   ARG D CD  1 
ATOM   10490 N  NE  . ARG D  1 9   ? 55.603  118.656 65.717  1.00 86.01  ? 9   ARG D NE  1 
ATOM   10491 C  CZ  . ARG D  1 9   ? 54.337  118.452 66.070  1.00 90.07  ? 9   ARG D CZ  1 
ATOM   10492 N  NH1 . ARG D  1 9   ? 53.415  118.273 65.140  1.00 90.04  ? 9   ARG D NH1 1 
ATOM   10493 N  NH2 . ARG D  1 9   ? 53.997  118.393 67.355  1.00 95.49  ? 9   ARG D NH2 1 
ATOM   10494 N  N   . ASP D  1 10  ? 57.931  113.206 63.035  1.00 51.31  ? 10  ASP D N   1 
ATOM   10495 C  CA  . ASP D  1 10  ? 57.345  112.065 62.333  1.00 46.99  ? 10  ASP D CA  1 
ATOM   10496 C  C   . ASP D  1 10  ? 56.602  111.139 63.321  1.00 40.49  ? 10  ASP D C   1 
ATOM   10497 O  O   . ASP D  1 10  ? 57.130  110.769 64.358  1.00 40.00  ? 10  ASP D O   1 
ATOM   10498 C  CB  . ASP D  1 10  ? 58.447  111.312 61.550  1.00 50.91  ? 10  ASP D CB  1 
ATOM   10499 C  CG  . ASP D  1 10  ? 58.714  111.890 60.132  1.00 53.87  ? 10  ASP D CG  1 
ATOM   10500 O  OD1 . ASP D  1 10  ? 57.824  112.583 59.560  1.00 54.03  ? 10  ASP D OD1 1 
ATOM   10501 O  OD2 . ASP D  1 10  ? 59.811  111.594 59.566  1.00 57.84  ? 10  ASP D OD2 1 
ATOM   10502 N  N   . MET D  1 11  ? 55.352  110.822 63.024  1.00 35.55  ? 11  MET D N   1 
ATOM   10503 C  CA  . MET D  1 11  ? 54.579  109.970 63.904  1.00 32.46  ? 11  MET D CA  1 
ATOM   10504 C  C   . MET D  1 11  ? 55.364  108.726 64.083  1.00 35.07  ? 11  MET D C   1 
ATOM   10505 O  O   . MET D  1 11  ? 55.940  108.179 63.151  1.00 41.03  ? 11  MET D O   1 
ATOM   10506 C  CB  . MET D  1 11  ? 53.220  109.586 63.330  1.00 32.27  ? 11  MET D CB  1 
ATOM   10507 C  CG  . MET D  1 11  ? 52.428  110.746 62.813  1.00 37.90  ? 11  MET D CG  1 
ATOM   10508 S  SD  . MET D  1 11  ? 50.793  110.274 62.373  1.00 45.26  ? 11  MET D SD  1 
ATOM   10509 C  CE  . MET D  1 11  ? 50.950  110.233 60.593  1.00 42.48  ? 11  MET D CE  1 
ATOM   10510 N  N   . PRO D  1 12  ? 55.444  108.280 65.306  1.00 37.25  ? 12  PRO D N   1 
ATOM   10511 C  CA  . PRO D  1 12  ? 56.159  107.080 65.699  1.00 39.25  ? 12  PRO D CA  1 
ATOM   10512 C  C   . PRO D  1 12  ? 55.502  105.811 65.126  1.00 38.17  ? 12  PRO D C   1 
ATOM   10513 O  O   . PRO D  1 12  ? 54.278  105.753 64.926  1.00 35.33  ? 12  PRO D O   1 
ATOM   10514 C  CB  . PRO D  1 12  ? 56.041  107.145 67.212  1.00 45.77  ? 12  PRO D CB  1 
ATOM   10515 C  CG  . PRO D  1 12  ? 54.686  107.774 67.414  1.00 43.05  ? 12  PRO D CG  1 
ATOM   10516 C  CD  . PRO D  1 12  ? 54.824  108.922 66.469  1.00 39.45  ? 12  PRO D CD  1 
ATOM   10517 N  N   . LEU D  1 13  ? 56.323  104.789 64.911  1.00 36.80  ? 13  LEU D N   1 
ATOM   10518 C  CA  . LEU D  1 13  ? 55.868  103.538 64.346  1.00 37.93  ? 13  LEU D CA  1 
ATOM   10519 C  C   . LEU D  1 13  ? 54.660  102.945 64.970  1.00 41.41  ? 13  LEU D C   1 
ATOM   10520 O  O   . LEU D  1 13  ? 53.940  102.216 64.296  1.00 44.67  ? 13  LEU D O   1 
ATOM   10521 C  CB  . LEU D  1 13  ? 56.973  102.503 64.349  1.00 39.82  ? 13  LEU D CB  1 
ATOM   10522 C  CG  . LEU D  1 13  ? 58.113  102.820 63.383  1.00 40.56  ? 13  LEU D CG  1 
ATOM   10523 C  CD1 . LEU D  1 13  ? 59.111  101.729 63.416  1.00 42.36  ? 13  LEU D CD1 1 
ATOM   10524 C  CD2 . LEU D  1 13  ? 57.591  102.958 61.980  1.00 44.64  ? 13  LEU D CD2 1 
ATOM   10525 N  N   . ASP D  1 14  ? 54.447  103.208 66.258  1.00 45.85  ? 14  ASP D N   1 
ATOM   10526 C  CA  . ASP D  1 14  ? 53.267  102.666 66.926  1.00 49.24  ? 14  ASP D CA  1 
ATOM   10527 C  C   . ASP D  1 14  ? 51.966  103.424 66.678  1.00 45.04  ? 14  ASP D C   1 
ATOM   10528 O  O   . ASP D  1 14  ? 50.872  102.873 66.867  1.00 46.38  ? 14  ASP D O   1 
ATOM   10529 C  CB  . ASP D  1 14  ? 53.494  102.389 68.438  1.00 60.59  ? 14  ASP D CB  1 
ATOM   10530 C  CG  . ASP D  1 14  ? 54.201  103.538 69.208  1.00 75.00  ? 14  ASP D CG  1 
ATOM   10531 O  OD1 . ASP D  1 14  ? 55.452  103.631 69.125  1.00 80.44  ? 14  ASP D OD1 1 
ATOM   10532 O  OD2 . ASP D  1 14  ? 53.526  104.265 70.000  1.00 85.55  ? 14  ASP D OD2 1 
ATOM   10533 N  N   . SER D  1 15  ? 52.087  104.649 66.189  1.00 39.55  ? 15  SER D N   1 
ATOM   10534 C  CA  . SER D  1 15  ? 50.923  105.458 65.940  1.00 39.15  ? 15  SER D CA  1 
ATOM   10535 C  C   . SER D  1 15  ? 49.776  104.655 65.387  1.00 37.14  ? 15  SER D C   1 
ATOM   10536 O  O   . SER D  1 15  ? 49.917  103.824 64.504  1.00 38.06  ? 15  SER D O   1 
ATOM   10537 C  CB  . SER D  1 15  ? 51.288  106.582 65.009  1.00 38.75  ? 15  SER D CB  1 
ATOM   10538 O  OG  . SER D  1 15  ? 52.415  107.237 65.543  1.00 39.08  ? 15  SER D OG  1 
ATOM   10539 N  N   . ASP D  1 16  ? 48.655  104.810 66.034  1.00 36.26  ? 16  ASP D N   1 
ATOM   10540 C  CA  . ASP D  1 16  ? 47.434  104.131 65.630  1.00 42.87  ? 16  ASP D CA  1 
ATOM   10541 C  C   . ASP D  1 16  ? 47.238  104.154 64.147  1.00 42.12  ? 16  ASP D C   1 
ATOM   10542 O  O   . ASP D  1 16  ? 46.542  103.323 63.547  1.00 35.60  ? 16  ASP D O   1 
ATOM   10543 C  CB  . ASP D  1 16  ? 46.249  104.872 66.237  1.00 51.66  ? 16  ASP D CB  1 
ATOM   10544 C  CG  . ASP D  1 16  ? 46.388  106.368 66.115  1.00 60.52  ? 16  ASP D CG  1 
ATOM   10545 O  OD1 . ASP D  1 16  ? 47.299  106.962 66.753  1.00 71.71  ? 16  ASP D OD1 1 
ATOM   10546 O  OD2 . ASP D  1 16  ? 45.607  106.942 65.349  1.00 68.04  ? 16  ASP D OD2 1 
ATOM   10547 N  N   . VAL D  1 17  ? 47.758  105.221 63.579  1.00 43.88  ? 17  VAL D N   1 
ATOM   10548 C  CA  . VAL D  1 17  ? 47.617  105.440 62.182  1.00 43.43  ? 17  VAL D CA  1 
ATOM   10549 C  C   . VAL D  1 17  ? 48.340  104.366 61.366  1.00 43.35  ? 17  VAL D C   1 
ATOM   10550 O  O   . VAL D  1 17  ? 47.838  103.919 60.352  1.00 48.62  ? 17  VAL D O   1 
ATOM   10551 C  CB  . VAL D  1 17  ? 47.991  106.893 61.892  1.00 38.93  ? 17  VAL D CB  1 
ATOM   10552 C  CG1 . VAL D  1 17  ? 49.460  107.054 61.634  1.00 31.50  ? 17  VAL D CG1 1 
ATOM   10553 C  CG2 . VAL D  1 17  ? 47.116  107.411 60.800  1.00 52.87  ? 17  VAL D CG2 1 
ATOM   10554 N  N   . PHE D  1 18  ? 49.422  103.837 61.908  1.00 39.45  ? 18  PHE D N   1 
ATOM   10555 C  CA  . PHE D  1 18  ? 50.182  102.807 61.227  1.00 35.78  ? 18  PHE D CA  1 
ATOM   10556 C  C   . PHE D  1 18  ? 49.806  101.343 61.572  1.00 41.12  ? 18  PHE D C   1 
ATOM   10557 O  O   . PHE D  1 18  ? 50.494  100.408 61.176  1.00 36.70  ? 18  PHE D O   1 
ATOM   10558 C  CB  . PHE D  1 18  ? 51.638  102.999 61.548  1.00 29.80  ? 18  PHE D CB  1 
ATOM   10559 C  CG  . PHE D  1 18  ? 52.148  104.351 61.232  1.00 29.02  ? 18  PHE D CG  1 
ATOM   10560 C  CD1 . PHE D  1 18  ? 51.794  104.982 60.043  1.00 28.65  ? 18  PHE D CD1 1 
ATOM   10561 C  CD2 . PHE D  1 18  ? 53.073  104.965 62.081  1.00 24.19  ? 18  PHE D CD2 1 
ATOM   10562 C  CE1 . PHE D  1 18  ? 52.364  106.197 59.700  1.00 26.43  ? 18  PHE D CE1 1 
ATOM   10563 C  CE2 . PHE D  1 18  ? 53.648  106.181 61.747  1.00 23.34  ? 18  PHE D CE2 1 
ATOM   10564 C  CZ  . PHE D  1 18  ? 53.296  106.795 60.558  1.00 22.41  ? 18  PHE D CZ  1 
ATOM   10565 N  N   . ARG D  1 19  ? 48.754  101.131 62.343  1.00 48.38  ? 19  ARG D N   1 
ATOM   10566 C  CA  . ARG D  1 19  ? 48.375  99.763  62.703  1.00 56.70  ? 19  ARG D CA  1 
ATOM   10567 C  C   . ARG D  1 19  ? 48.090  98.888  61.507  1.00 56.52  ? 19  ARG D C   1 
ATOM   10568 O  O   . ARG D  1 19  ? 47.493  99.348  60.526  1.00 63.49  ? 19  ARG D O   1 
ATOM   10569 C  CB  . ARG D  1 19  ? 47.164  99.752  63.636  1.00 64.87  ? 19  ARG D CB  1 
ATOM   10570 C  CG  . ARG D  1 19  ? 47.577  100.071 65.063  1.00 82.38  ? 19  ARG D CG  1 
ATOM   10571 C  CD  . ARG D  1 19  ? 46.396  100.353 66.009  1.00 95.08  ? 19  ARG D CD  1 
ATOM   10572 N  NE  . ARG D  1 19  ? 46.881  100.831 67.317  1.00 104.09 ? 19  ARG D NE  1 
ATOM   10573 C  CZ  . ARG D  1 19  ? 46.130  101.412 68.257  1.00 108.95 ? 19  ARG D CZ  1 
ATOM   10574 N  NH1 . ARG D  1 19  ? 44.818  101.604 68.068  1.00 112.09 ? 19  ARG D NH1 1 
ATOM   10575 N  NH2 . ARG D  1 19  ? 46.709  101.839 69.385  1.00 109.50 ? 19  ARG D NH2 1 
ATOM   10576 N  N   . VAL D  1 20  ? 48.513  97.624  61.581  1.00 52.23  ? 20  VAL D N   1 
ATOM   10577 C  CA  . VAL D  1 20  ? 48.283  96.687  60.480  1.00 43.23  ? 20  VAL D CA  1 
ATOM   10578 C  C   . VAL D  1 20  ? 47.017  95.913  60.652  1.00 40.95  ? 20  VAL D C   1 
ATOM   10579 O  O   . VAL D  1 20  ? 46.739  95.350  61.703  1.00 44.13  ? 20  VAL D O   1 
ATOM   10580 C  CB  . VAL D  1 20  ? 49.464  95.747  60.211  1.00 37.74  ? 20  VAL D CB  1 
ATOM   10581 C  CG1 . VAL D  1 20  ? 50.256  95.578  61.414  1.00 35.41  ? 20  VAL D CG1 1 
ATOM   10582 C  CG2 . VAL D  1 20  ? 48.982  94.421  59.663  1.00 37.06  ? 20  VAL D CG2 1 
ATOM   10583 N  N   . PRO D  1 21  ? 46.208  95.912  59.613  1.00 41.01  ? 21  PRO D N   1 
ATOM   10584 C  CA  . PRO D  1 21  ? 44.940  95.214  59.618  1.00 42.03  ? 21  PRO D CA  1 
ATOM   10585 C  C   . PRO D  1 21  ? 45.160  93.795  60.028  1.00 44.00  ? 21  PRO D C   1 
ATOM   10586 O  O   . PRO D  1 21  ? 46.115  93.146  59.612  1.00 50.16  ? 21  PRO D O   1 
ATOM   10587 C  CB  . PRO D  1 21  ? 44.458  95.358  58.185  1.00 45.44  ? 21  PRO D CB  1 
ATOM   10588 C  CG  . PRO D  1 21  ? 45.722  95.650  57.413  1.00 52.28  ? 21  PRO D CG  1 
ATOM   10589 C  CD  . PRO D  1 21  ? 46.471  96.539  58.316  1.00 44.28  ? 21  PRO D CD  1 
ATOM   10590 N  N   . PRO D  1 22  ? 44.321  93.318  60.937  1.00 46.76  ? 22  PRO D N   1 
ATOM   10591 C  CA  . PRO D  1 22  ? 44.334  91.977  61.500  1.00 45.12  ? 22  PRO D CA  1 
ATOM   10592 C  C   . PRO D  1 22  ? 43.864  90.916  60.539  1.00 43.02  ? 22  PRO D C   1 
ATOM   10593 O  O   . PRO D  1 22  ? 42.937  91.120  59.757  1.00 43.07  ? 22  PRO D O   1 
ATOM   10594 C  CB  . PRO D  1 22  ? 43.351  92.114  62.628  1.00 46.37  ? 22  PRO D CB  1 
ATOM   10595 C  CG  . PRO D  1 22  ? 42.299  92.985  62.016  1.00 44.70  ? 22  PRO D CG  1 
ATOM   10596 C  CD  . PRO D  1 22  ? 43.173  94.077  61.466  1.00 48.34  ? 22  PRO D CD  1 
ATOM   10597 N  N   . GLY D  1 23  ? 44.434  89.738  60.710  1.00 41.12  ? 23  GLY D N   1 
ATOM   10598 C  CA  . GLY D  1 23  ? 44.100  88.619  59.856  1.00 41.90  ? 23  GLY D CA  1 
ATOM   10599 C  C   . GLY D  1 23  ? 45.380  88.103  59.194  1.00 43.26  ? 23  GLY D C   1 
ATOM   10600 O  O   . GLY D  1 23  ? 46.358  88.857  59.018  1.00 47.23  ? 23  GLY D O   1 
ATOM   10601 N  N   . TYR D  1 24  ? 45.409  86.811  58.883  1.00 39.61  ? 24  TYR D N   1 
ATOM   10602 C  CA  . TYR D  1 24  ? 46.571  86.240  58.245  1.00 34.39  ? 24  TYR D CA  1 
ATOM   10603 C  C   . TYR D  1 24  ? 46.634  86.709  56.811  1.00 37.53  ? 24  TYR D C   1 
ATOM   10604 O  O   . TYR D  1 24  ? 45.712  86.427  56.026  1.00 39.74  ? 24  TYR D O   1 
ATOM   10605 C  CB  . TYR D  1 24  ? 46.526  84.718  58.226  1.00 28.53  ? 24  TYR D CB  1 
ATOM   10606 C  CG  . TYR D  1 24  ? 47.660  84.100  57.416  1.00 27.32  ? 24  TYR D CG  1 
ATOM   10607 C  CD1 . TYR D  1 24  ? 48.962  84.074  57.933  1.00 29.96  ? 24  TYR D CD1 1 
ATOM   10608 C  CD2 . TYR D  1 24  ? 47.454  83.591  56.113  1.00 24.66  ? 24  TYR D CD2 1 
ATOM   10609 C  CE1 . TYR D  1 24  ? 50.048  83.579  57.197  1.00 30.27  ? 24  TYR D CE1 1 
ATOM   10610 C  CE2 . TYR D  1 24  ? 48.539  83.084  55.366  1.00 23.72  ? 24  TYR D CE2 1 
ATOM   10611 C  CZ  . TYR D  1 24  ? 49.836  83.087  55.923  1.00 32.13  ? 24  TYR D CZ  1 
ATOM   10612 O  OH  . TYR D  1 24  ? 50.949  82.607  55.254  1.00 36.47  ? 24  TYR D OH  1 
ATOM   10613 N  N   . ASN D  1 25  ? 47.757  87.352  56.471  1.00 36.32  ? 25  ASN D N   1 
ATOM   10614 C  CA  . ASN D  1 25  ? 48.035  87.836  55.126  1.00 35.37  ? 25  ASN D CA  1 
ATOM   10615 C  C   . ASN D  1 25  ? 46.883  88.734  54.723  1.00 40.58  ? 25  ASN D C   1 
ATOM   10616 O  O   . ASN D  1 25  ? 46.171  88.484  53.730  1.00 46.42  ? 25  ASN D O   1 
ATOM   10617 C  CB  . ASN D  1 25  ? 48.139  86.658  54.188  1.00 30.73  ? 25  ASN D CB  1 
ATOM   10618 C  CG  . ASN D  1 25  ? 48.960  86.942  53.002  1.00 25.31  ? 25  ASN D CG  1 
ATOM   10619 O  OD1 . ASN D  1 25  ? 48.632  86.535  51.875  1.00 31.18  ? 25  ASN D OD1 1 
ATOM   10620 N  ND2 . ASN D  1 25  ? 50.075  87.572  53.230  1.00 18.75  ? 25  ASN D ND2 1 
ATOM   10621 N  N   . ALA D  1 26  ? 46.653  89.732  55.568  1.00 41.92  ? 26  ALA D N   1 
ATOM   10622 C  CA  . ALA D  1 26  ? 45.590  90.709  55.359  1.00 40.83  ? 26  ALA D CA  1 
ATOM   10623 C  C   . ALA D  1 26  ? 46.109  91.836  54.507  1.00 38.07  ? 26  ALA D C   1 
ATOM   10624 O  O   . ALA D  1 26  ? 47.155  92.436  54.850  1.00 42.46  ? 26  ALA D O   1 
ATOM   10625 C  CB  . ALA D  1 26  ? 45.103  91.261  56.687  1.00 43.45  ? 26  ALA D CB  1 
ATOM   10626 N  N   . PRO D  1 27  ? 45.375  92.161  53.409  1.00 32.59  ? 27  PRO D N   1 
ATOM   10627 C  CA  . PRO D  1 27  ? 45.719  93.216  52.460  1.00 26.66  ? 27  PRO D CA  1 
ATOM   10628 C  C   . PRO D  1 27  ? 45.978  94.503  53.202  1.00 26.21  ? 27  PRO D C   1 
ATOM   10629 O  O   . PRO D  1 27  ? 45.156  94.944  53.962  1.00 33.20  ? 27  PRO D O   1 
ATOM   10630 C  CB  . PRO D  1 27  ? 44.449  93.340  51.634  1.00 21.93  ? 27  PRO D CB  1 
ATOM   10631 C  CG  . PRO D  1 27  ? 43.834  92.003  51.693  1.00 19.32  ? 27  PRO D CG  1 
ATOM   10632 C  CD  . PRO D  1 27  ? 44.038  91.605  53.097  1.00 28.40  ? 27  PRO D CD  1 
ATOM   10633 N  N   . GLN D  1 28  ? 47.124  95.099  53.025  1.00 20.91  ? 28  GLN D N   1 
ATOM   10634 C  CA  . GLN D  1 28  ? 47.345  96.312  53.704  1.00 21.13  ? 28  GLN D CA  1 
ATOM   10635 C  C   . GLN D  1 28  ? 47.845  97.246  52.670  1.00 26.16  ? 28  GLN D C   1 
ATOM   10636 O  O   . GLN D  1 28  ? 48.151  96.843  51.553  1.00 28.56  ? 28  GLN D O   1 
ATOM   10637 C  CB  . GLN D  1 28  ? 48.376  96.104  54.769  1.00 21.80  ? 28  GLN D CB  1 
ATOM   10638 C  CG  . GLN D  1 28  ? 49.738  95.909  54.281  1.00 19.55  ? 28  GLN D CG  1 
ATOM   10639 C  CD  . GLN D  1 28  ? 50.632  95.637  55.417  1.00 26.08  ? 28  GLN D CD  1 
ATOM   10640 O  OE1 . GLN D  1 28  ? 50.478  94.629  56.097  1.00 34.19  ? 28  GLN D OE1 1 
ATOM   10641 N  NE2 . GLN D  1 28  ? 51.506  96.581  55.720  1.00 26.31  ? 28  GLN D NE2 1 
ATOM   10642 N  N   . GLN D  1 29  ? 47.927  98.508  53.041  1.00 28.29  ? 29  GLN D N   1 
ATOM   10643 C  CA  . GLN D  1 29  ? 48.399  99.535  52.136  1.00 26.36  ? 29  GLN D CA  1 
ATOM   10644 C  C   . GLN D  1 29  ? 47.515  99.639  50.877  1.00 29.18  ? 29  GLN D C   1 
ATOM   10645 O  O   . GLN D  1 29  ? 48.016  99.876  49.793  1.00 34.30  ? 29  GLN D O   1 
ATOM   10646 C  CB  . GLN D  1 29  ? 49.866  99.255  51.783  1.00 22.12  ? 29  GLN D CB  1 
ATOM   10647 C  CG  . GLN D  1 29  ? 50.801  99.308  52.975  1.00 25.64  ? 29  GLN D CG  1 
ATOM   10648 C  CD  . GLN D  1 29  ? 52.256  99.080  52.613  1.00 31.52  ? 29  GLN D CD  1 
ATOM   10649 O  OE1 . GLN D  1 29  ? 52.787  99.696  51.689  1.00 37.55  ? 29  GLN D OE1 1 
ATOM   10650 N  NE2 . GLN D  1 29  ? 52.918  98.215  53.365  1.00 23.83  ? 29  GLN D NE2 1 
ATOM   10651 N  N   . VAL D  1 30  ? 46.195  99.517  51.008  1.00 29.42  ? 30  VAL D N   1 
ATOM   10652 C  CA  . VAL D  1 30  ? 45.353  99.566  49.813  1.00 27.44  ? 30  VAL D CA  1 
ATOM   10653 C  C   . VAL D  1 30  ? 45.267  100.943 49.217  1.00 26.37  ? 30  VAL D C   1 
ATOM   10654 O  O   . VAL D  1 30  ? 45.217  101.927 49.919  1.00 28.39  ? 30  VAL D O   1 
ATOM   10655 C  CB  . VAL D  1 30  ? 43.961  99.035  50.095  1.00 28.61  ? 30  VAL D CB  1 
ATOM   10656 C  CG1 . VAL D  1 30  ? 43.105  99.101  48.836  1.00 24.89  ? 30  VAL D CG1 1 
ATOM   10657 C  CG2 . VAL D  1 30  ? 44.061  97.594  50.615  1.00 27.38  ? 30  VAL D CG2 1 
ATOM   10658 N  N   . HIS D  1 31  ? 45.366  101.020 47.906  1.00 29.41  ? 31  HIS D N   1 
ATOM   10659 C  CA  . HIS D  1 31  ? 45.276  102.307 47.235  1.00 31.36  ? 31  HIS D CA  1 
ATOM   10660 C  C   . HIS D  1 31  ? 44.824  102.180 45.802  1.00 32.89  ? 31  HIS D C   1 
ATOM   10661 O  O   . HIS D  1 31  ? 45.198  101.222 45.143  1.00 37.33  ? 31  HIS D O   1 
ATOM   10662 C  CB  . HIS D  1 31  ? 46.599  103.067 47.331  1.00 33.06  ? 31  HIS D CB  1 
ATOM   10663 C  CG  . HIS D  1 31  ? 47.807  102.309 46.862  1.00 34.27  ? 31  HIS D CG  1 
ATOM   10664 N  ND1 . HIS D  1 31  ? 48.521  102.664 45.734  1.00 37.71  ? 31  HIS D ND1 1 
ATOM   10665 C  CD2 . HIS D  1 31  ? 48.503  101.299 47.431  1.00 35.40  ? 31  HIS D CD2 1 
ATOM   10666 C  CE1 . HIS D  1 31  ? 49.603  101.912 45.634  1.00 34.07  ? 31  HIS D CE1 1 
ATOM   10667 N  NE2 . HIS D  1 31  ? 49.616  101.073 46.654  1.00 34.26  ? 31  HIS D NE2 1 
ATOM   10668 N  N   . ILE D  1 32  ? 44.056  103.152 45.307  1.00 33.25  ? 32  ILE D N   1 
ATOM   10669 C  CA  . ILE D  1 32  ? 43.543  103.104 43.933  1.00 31.97  ? 32  ILE D CA  1 
ATOM   10670 C  C   . ILE D  1 32  ? 43.907  104.350 43.098  1.00 30.33  ? 32  ILE D C   1 
ATOM   10671 O  O   . ILE D  1 32  ? 44.435  105.309 43.647  1.00 30.94  ? 32  ILE D O   1 
ATOM   10672 C  CB  . ILE D  1 32  ? 41.979  102.918 43.931  1.00 31.40  ? 32  ILE D CB  1 
ATOM   10673 C  CG1 . ILE D  1 32  ? 41.280  104.181 44.426  1.00 32.33  ? 32  ILE D CG1 1 
ATOM   10674 C  CG2 . ILE D  1 32  ? 41.553  101.810 44.883  1.00 30.04  ? 32  ILE D CG2 1 
ATOM   10675 C  CD1 . ILE D  1 32  ? 39.767  104.108 44.361  1.00 20.96  ? 32  ILE D CD1 1 
ATOM   10676 N  N   . THR D  1 33  ? 43.699  104.301 41.774  1.00 31.53  ? 33  THR D N   1 
ATOM   10677 C  CA  . THR D  1 33  ? 43.927  105.444 40.859  1.00 31.10  ? 33  THR D CA  1 
ATOM   10678 C  C   . THR D  1 33  ? 43.126  105.191 39.624  1.00 30.45  ? 33  THR D C   1 
ATOM   10679 O  O   . THR D  1 33  ? 42.622  104.094 39.417  1.00 33.50  ? 33  THR D O   1 
ATOM   10680 C  CB  . THR D  1 33  ? 45.320  105.571 40.295  1.00 28.75  ? 33  THR D CB  1 
ATOM   10681 O  OG1 . THR D  1 33  ? 46.269  104.950 41.161  1.00 45.90  ? 33  THR D OG1 1 
ATOM   10682 C  CG2 . THR D  1 33  ? 45.628  107.051 40.122  1.00 35.62  ? 33  THR D CG2 1 
ATOM   10683 N  N   . GLN D  1 34  ? 43.075  106.175 38.752  1.00 29.39  ? 34  GLN D N   1 
ATOM   10684 C  CA  . GLN D  1 34  ? 42.350  106.001 37.529  1.00 26.90  ? 34  GLN D CA  1 
ATOM   10685 C  C   . GLN D  1 34  ? 43.203  105.068 36.688  1.00 31.68  ? 34  GLN D C   1 
ATOM   10686 O  O   . GLN D  1 34  ? 44.435  105.211 36.615  1.00 28.65  ? 34  GLN D O   1 
ATOM   10687 C  CB  . GLN D  1 34  ? 42.187  107.321 36.838  1.00 24.94  ? 34  GLN D CB  1 
ATOM   10688 C  CG  . GLN D  1 34  ? 41.420  107.202 35.623  1.00 24.36  ? 34  GLN D CG  1 
ATOM   10689 C  CD  . GLN D  1 34  ? 40.862  108.502 35.223  1.00 29.70  ? 34  GLN D CD  1 
ATOM   10690 O  OE1 . GLN D  1 34  ? 40.929  108.881 34.076  1.00 37.76  ? 34  GLN D OE1 1 
ATOM   10691 N  NE2 . GLN D  1 34  ? 40.247  109.183 36.161  1.00 33.80  ? 34  GLN D NE2 1 
ATOM   10692 N  N   . GLY D  1 35  ? 42.535  104.100 36.069  1.00 33.41  ? 35  GLY D N   1 
ATOM   10693 C  CA  . GLY D  1 35  ? 43.224  103.119 35.264  1.00 31.93  ? 35  GLY D CA  1 
ATOM   10694 C  C   . GLY D  1 35  ? 43.186  103.317 33.783  1.00 32.78  ? 35  GLY D C   1 
ATOM   10695 O  O   . GLY D  1 35  ? 43.815  102.577 33.058  1.00 40.90  ? 35  GLY D O   1 
ATOM   10696 N  N   . ASP D  1 36  ? 42.471  104.322 33.317  1.00 33.92  ? 36  ASP D N   1 
ATOM   10697 C  CA  . ASP D  1 36  ? 42.383  104.579 31.895  1.00 32.54  ? 36  ASP D CA  1 
ATOM   10698 C  C   . ASP D  1 36  ? 42.429  106.070 31.622  1.00 29.98  ? 36  ASP D C   1 
ATOM   10699 O  O   . ASP D  1 36  ? 42.579  106.871 32.521  1.00 30.59  ? 36  ASP D O   1 
ATOM   10700 C  CB  . ASP D  1 36  ? 41.115  103.955 31.305  1.00 30.48  ? 36  ASP D CB  1 
ATOM   10701 C  CG  . ASP D  1 36  ? 39.854  104.615 31.776  1.00 33.00  ? 36  ASP D CG  1 
ATOM   10702 O  OD1 . ASP D  1 36  ? 39.908  105.516 32.618  1.00 40.19  ? 36  ASP D OD1 1 
ATOM   10703 O  OD2 . ASP D  1 36  ? 38.774  104.238 31.294  1.00 39.75  ? 36  ASP D OD2 1 
ATOM   10704 N  N   . LEU D  1 37  ? 42.252  106.441 30.377  1.00 27.87  ? 37  LEU D N   1 
ATOM   10705 C  CA  . LEU D  1 37  ? 42.267  107.834 30.049  1.00 26.91  ? 37  LEU D CA  1 
ATOM   10706 C  C   . LEU D  1 37  ? 41.001  108.624 30.401  1.00 27.90  ? 37  LEU D C   1 
ATOM   10707 O  O   . LEU D  1 37  ? 41.088  109.803 30.648  1.00 29.27  ? 37  LEU D O   1 
ATOM   10708 C  CB  . LEU D  1 37  ? 42.509  107.988 28.572  1.00 24.62  ? 37  LEU D CB  1 
ATOM   10709 C  CG  . LEU D  1 37  ? 42.782  109.427 28.190  1.00 28.05  ? 37  LEU D CG  1 
ATOM   10710 C  CD1 . LEU D  1 37  ? 44.025  109.894 28.929  1.00 30.52  ? 37  LEU D CD1 1 
ATOM   10711 C  CD2 . LEU D  1 37  ? 42.998  109.539 26.702  1.00 27.96  ? 37  LEU D CD2 1 
ATOM   10712 N  N   . VAL D  1 38  ? 39.839  107.988 30.476  1.00 28.19  ? 38  VAL D N   1 
ATOM   10713 C  CA  . VAL D  1 38  ? 38.623  108.761 30.691  1.00 29.00  ? 38  VAL D CA  1 
ATOM   10714 C  C   . VAL D  1 38  ? 37.720  108.516 31.893  1.00 33.56  ? 38  VAL D C   1 
ATOM   10715 O  O   . VAL D  1 38  ? 36.612  109.074 31.961  1.00 38.83  ? 38  VAL D O   1 
ATOM   10716 C  CB  . VAL D  1 38  ? 37.755  108.696 29.434  1.00 25.32  ? 38  VAL D CB  1 
ATOM   10717 C  CG1 . VAL D  1 38  ? 38.632  108.774 28.224  1.00 24.54  ? 38  VAL D CG1 1 
ATOM   10718 C  CG2 . VAL D  1 38  ? 37.020  107.422 29.373  1.00 19.72  ? 38  VAL D CG2 1 
ATOM   10719 N  N   . GLY D  1 39  ? 38.141  107.665 32.818  1.00 34.94  ? 39  GLY D N   1 
ATOM   10720 C  CA  . GLY D  1 39  ? 37.306  107.420 33.983  1.00 34.69  ? 39  GLY D CA  1 
ATOM   10721 C  C   . GLY D  1 39  ? 36.678  106.059 34.233  1.00 35.26  ? 39  GLY D C   1 
ATOM   10722 O  O   . GLY D  1 39  ? 36.180  105.810 35.361  1.00 31.27  ? 39  GLY D O   1 
ATOM   10723 N  N   . ARG D  1 40  ? 36.738  105.159 33.256  1.00 34.97  ? 40  ARG D N   1 
ATOM   10724 C  CA  . ARG D  1 40  ? 36.138  103.858 33.495  1.00 41.73  ? 40  ARG D CA  1 
ATOM   10725 C  C   . ARG D  1 40  ? 37.045  102.639 33.754  1.00 39.56  ? 40  ARG D C   1 
ATOM   10726 O  O   . ARG D  1 40  ? 36.774  101.519 33.325  1.00 44.81  ? 40  ARG D O   1 
ATOM   10727 C  CB  . ARG D  1 40  ? 35.000  103.568 32.495  1.00 44.01  ? 40  ARG D CB  1 
ATOM   10728 C  CG  . ARG D  1 40  ? 35.345  103.576 31.034  1.00 44.58  ? 40  ARG D CG  1 
ATOM   10729 C  CD  . ARG D  1 40  ? 34.114  103.974 30.227  1.00 52.11  ? 40  ARG D CD  1 
ATOM   10730 N  NE  . ARG D  1 40  ? 32.958  103.096 30.447  1.00 60.25  ? 40  ARG D NE  1 
ATOM   10731 C  CZ  . ARG D  1 40  ? 32.704  101.979 29.760  1.00 62.15  ? 40  ARG D CZ  1 
ATOM   10732 N  NH1 . ARG D  1 40  ? 33.525  101.590 28.786  1.00 60.51  ? 40  ARG D NH1 1 
ATOM   10733 N  NH2 . ARG D  1 40  ? 31.631  101.242 30.053  1.00 62.65  ? 40  ARG D NH2 1 
ATOM   10734 N  N   . ALA D  1 41  ? 38.064  102.846 34.566  1.00 35.24  ? 41  ALA D N   1 
ATOM   10735 C  CA  . ALA D  1 41  ? 38.971  101.774 34.894  1.00 31.13  ? 41  ALA D CA  1 
ATOM   10736 C  C   . ALA D  1 41  ? 39.684  102.249 36.114  1.00 29.15  ? 41  ALA D C   1 
ATOM   10737 O  O   . ALA D  1 41  ? 39.982  103.419 36.241  1.00 27.44  ? 41  ALA D O   1 
ATOM   10738 C  CB  . ALA D  1 41  ? 39.949  101.576 33.793  1.00 34.23  ? 41  ALA D CB  1 
ATOM   10739 N  N   . MET D  1 42  ? 39.986  101.337 37.008  1.00 29.03  ? 42  MET D N   1 
ATOM   10740 C  CA  . MET D  1 42  ? 40.671  101.701 38.223  1.00 29.68  ? 42  MET D CA  1 
ATOM   10741 C  C   . MET D  1 42  ? 41.820  100.778 38.382  1.00 29.58  ? 42  MET D C   1 
ATOM   10742 O  O   . MET D  1 42  ? 41.764  99.649  37.904  1.00 31.86  ? 42  MET D O   1 
ATOM   10743 C  CB  . MET D  1 42  ? 39.766  101.473 39.407  1.00 30.70  ? 42  MET D CB  1 
ATOM   10744 C  CG  . MET D  1 42  ? 38.904  102.608 39.651  1.00 37.36  ? 42  MET D CG  1 
ATOM   10745 S  SD  . MET D  1 42  ? 39.914  103.831 40.343  1.00 39.31  ? 42  MET D SD  1 
ATOM   10746 C  CE  . MET D  1 42  ? 38.642  104.882 40.716  1.00 45.87  ? 42  MET D CE  1 
ATOM   10747 N  N   . ILE D  1 43  ? 42.860  101.250 39.044  1.00 26.01  ? 43  ILE D N   1 
ATOM   10748 C  CA  . ILE D  1 43  ? 43.993  100.410 39.316  1.00 24.02  ? 43  ILE D CA  1 
ATOM   10749 C  C   . ILE D  1 43  ? 43.941  100.182 40.826  1.00 28.62  ? 43  ILE D C   1 
ATOM   10750 O  O   . ILE D  1 43  ? 44.063  101.153 41.608  1.00 32.97  ? 43  ILE D O   1 
ATOM   10751 C  CB  . ILE D  1 43  ? 45.320  101.088 38.993  1.00 19.06  ? 43  ILE D CB  1 
ATOM   10752 C  CG1 . ILE D  1 43  ? 45.533  101.164 37.505  1.00 19.92  ? 43  ILE D CG1 1 
ATOM   10753 C  CG2 . ILE D  1 43  ? 46.430  100.277 39.492  1.00 19.10  ? 43  ILE D CG2 1 
ATOM   10754 C  CD1 . ILE D  1 43  ? 46.830  101.859 37.161  1.00 18.73  ? 43  ILE D CD1 1 
ATOM   10755 N  N   . ILE D  1 44  ? 43.726  98.929  41.231  1.00 25.19  ? 44  ILE D N   1 
ATOM   10756 C  CA  . ILE D  1 44  ? 43.676  98.549  42.638  1.00 21.26  ? 44  ILE D CA  1 
ATOM   10757 C  C   . ILE D  1 44  ? 45.051  97.985  43.003  1.00 22.34  ? 44  ILE D C   1 
ATOM   10758 O  O   . ILE D  1 44  ? 45.577  97.130  42.292  1.00 26.09  ? 44  ILE D O   1 
ATOM   10759 C  CB  . ILE D  1 44  ? 42.664  97.483  42.861  1.00 19.86  ? 44  ILE D CB  1 
ATOM   10760 C  CG1 . ILE D  1 44  ? 41.394  97.760  42.025  1.00 20.16  ? 44  ILE D CG1 1 
ATOM   10761 C  CG2 . ILE D  1 44  ? 42.326  97.459  44.300  1.00 18.89  ? 44  ILE D CG2 1 
ATOM   10762 C  CD1 . ILE D  1 44  ? 40.552  98.977  42.474  1.00 19.48  ? 44  ILE D CD1 1 
ATOM   10763 N  N   . SER D  1 45  ? 45.629  98.473  44.094  1.00 18.34  ? 45  SER D N   1 
ATOM   10764 C  CA  . SER D  1 45  ? 46.940  98.058  44.505  1.00 17.99  ? 45  SER D CA  1 
ATOM   10765 C  C   . SER D  1 45  ? 46.959  97.811  45.982  1.00 21.75  ? 45  SER D C   1 
ATOM   10766 O  O   . SER D  1 45  ? 46.349  98.554  46.736  1.00 31.72  ? 45  SER D O   1 
ATOM   10767 C  CB  . SER D  1 45  ? 47.955  99.176  44.234  1.00 20.26  ? 45  SER D CB  1 
ATOM   10768 O  OG  . SER D  1 45  ? 47.795  99.790  42.951  1.00 25.08  ? 45  SER D OG  1 
ATOM   10769 N  N   . TRP D  1 46  ? 47.674  96.786  46.418  1.00 22.74  ? 46  TRP D N   1 
ATOM   10770 C  CA  . TRP D  1 46  ? 47.797  96.520  47.837  1.00 21.05  ? 46  TRP D CA  1 
ATOM   10771 C  C   . TRP D  1 46  ? 49.023  95.677  48.093  1.00 21.30  ? 46  TRP D C   1 
ATOM   10772 O  O   . TRP D  1 46  ? 49.741  95.249  47.176  1.00 24.18  ? 46  TRP D O   1 
ATOM   10773 C  CB  . TRP D  1 46  ? 46.560  95.846  48.406  1.00 19.95  ? 46  TRP D CB  1 
ATOM   10774 C  CG  . TRP D  1 46  ? 46.359  94.497  47.873  1.00 21.50  ? 46  TRP D CG  1 
ATOM   10775 C  CD1 . TRP D  1 46  ? 46.676  93.329  48.481  1.00 23.99  ? 46  TRP D CD1 1 
ATOM   10776 C  CD2 . TRP D  1 46  ? 45.815  94.158  46.592  1.00 20.99  ? 46  TRP D CD2 1 
ATOM   10777 N  NE1 . TRP D  1 46  ? 46.368  92.269  47.655  1.00 30.24  ? 46  TRP D NE1 1 
ATOM   10778 C  CE2 . TRP D  1 46  ? 45.839  92.760  46.485  1.00 25.41  ? 46  TRP D CE2 1 
ATOM   10779 C  CE3 . TRP D  1 46  ? 45.306  94.894  45.528  1.00 21.47  ? 46  TRP D CE3 1 
ATOM   10780 C  CZ2 . TRP D  1 46  ? 45.371  92.090  45.340  1.00 21.53  ? 46  TRP D CZ2 1 
ATOM   10781 C  CZ3 . TRP D  1 46  ? 44.840  94.224  44.395  1.00 19.93  ? 46  TRP D CZ3 1 
ATOM   10782 C  CH2 . TRP D  1 46  ? 44.877  92.840  44.315  1.00 14.15  ? 46  TRP D CH2 1 
ATOM   10783 N  N   . VAL D  1 47  ? 49.221  95.373  49.350  1.00 21.67  ? 47  VAL D N   1 
ATOM   10784 C  CA  . VAL D  1 47  ? 50.376  94.613  49.741  1.00 19.96  ? 47  VAL D CA  1 
ATOM   10785 C  C   . VAL D  1 47  ? 49.960  93.571  50.762  1.00 21.59  ? 47  VAL D C   1 
ATOM   10786 O  O   . VAL D  1 47  ? 49.141  93.880  51.633  1.00 22.45  ? 47  VAL D O   1 
ATOM   10787 C  CB  . VAL D  1 47  ? 51.386  95.545  50.372  1.00 15.73  ? 47  VAL D CB  1 
ATOM   10788 C  CG1 . VAL D  1 47  ? 52.509  94.797  50.907  1.00 14.95  ? 47  VAL D CG1 1 
ATOM   10789 C  CG2 . VAL D  1 47  ? 51.870  96.504  49.352  1.00 12.97  ? 47  VAL D CG2 1 
ATOM   10790 N  N   . THR D  1 48  ? 50.494  92.346  50.599  1.00 21.34  ? 48  THR D N   1 
ATOM   10791 C  CA  . THR D  1 48  ? 50.272  91.197  51.478  1.00 20.78  ? 48  THR D CA  1 
ATOM   10792 C  C   . THR D  1 48  ? 51.666  90.924  51.995  1.00 23.30  ? 48  THR D C   1 
ATOM   10793 O  O   . THR D  1 48  ? 52.619  90.951  51.231  1.00 20.31  ? 48  THR D O   1 
ATOM   10794 C  CB  . THR D  1 48  ? 49.835  89.920  50.736  1.00 20.90  ? 48  THR D CB  1 
ATOM   10795 O  OG1 . THR D  1 48  ? 50.718  89.683  49.630  1.00 28.41  ? 48  THR D OG1 1 
ATOM   10796 C  CG2 . THR D  1 48  ? 48.417  90.014  50.241  1.00 15.17  ? 48  THR D CG2 1 
ATOM   10797 N  N   . MET D  1 49  ? 51.797  90.659  53.286  1.00 28.12  ? 49  MET D N   1 
ATOM   10798 C  CA  . MET D  1 49  ? 53.112  90.435  53.853  1.00 29.98  ? 49  MET D CA  1 
ATOM   10799 C  C   . MET D  1 49  ? 53.454  89.006  54.262  1.00 31.54  ? 49  MET D C   1 
ATOM   10800 O  O   . MET D  1 49  ? 54.623  88.669  54.331  1.00 38.93  ? 49  MET D O   1 
ATOM   10801 C  CB  . MET D  1 49  ? 53.280  91.348  55.063  1.00 33.49  ? 49  MET D CB  1 
ATOM   10802 C  CG  . MET D  1 49  ? 53.230  92.824  54.782  1.00 38.87  ? 49  MET D CG  1 
ATOM   10803 S  SD  . MET D  1 49  ? 54.874  93.551  54.550  1.00 38.52  ? 49  MET D SD  1 
ATOM   10804 C  CE  . MET D  1 49  ? 54.786  94.918  55.847  1.00 54.38  ? 49  MET D CE  1 
ATOM   10805 N  N   . ASP D  1 50  ? 52.450  88.188  54.574  1.00 32.88  ? 50  ASP D N   1 
ATOM   10806 C  CA  . ASP D  1 50  ? 52.681  86.814  55.020  1.00 29.95  ? 50  ASP D CA  1 
ATOM   10807 C  C   . ASP D  1 50  ? 53.072  85.891  53.905  1.00 28.81  ? 50  ASP D C   1 
ATOM   10808 O  O   . ASP D  1 50  ? 54.031  85.144  53.998  1.00 28.77  ? 50  ASP D O   1 
ATOM   10809 C  CB  . ASP D  1 50  ? 51.468  86.321  55.769  1.00 31.42  ? 50  ASP D CB  1 
ATOM   10810 C  CG  . ASP D  1 50  ? 51.285  87.082  57.058  1.00 39.76  ? 50  ASP D CG  1 
ATOM   10811 O  OD1 . ASP D  1 50  ? 52.304  87.306  57.747  1.00 36.56  ? 50  ASP D OD1 1 
ATOM   10812 O  OD2 . ASP D  1 50  ? 50.154  87.506  57.377  1.00 42.59  ? 50  ASP D OD2 1 
ATOM   10813 N  N   . GLU D  1 51  ? 52.326  85.944  52.835  1.00 27.97  ? 51  GLU D N   1 
ATOM   10814 C  CA  . GLU D  1 51  ? 52.658  85.141  51.706  1.00 27.75  ? 51  GLU D CA  1 
ATOM   10815 C  C   . GLU D  1 51  ? 52.042  85.830  50.529  1.00 28.93  ? 51  GLU D C   1 
ATOM   10816 O  O   . GLU D  1 51  ? 51.186  86.708  50.679  1.00 27.89  ? 51  GLU D O   1 
ATOM   10817 C  CB  . GLU D  1 51  ? 52.136  83.722  51.871  1.00 25.91  ? 51  GLU D CB  1 
ATOM   10818 C  CG  . GLU D  1 51  ? 50.758  83.635  52.362  1.00 26.09  ? 51  GLU D CG  1 
ATOM   10819 C  CD  . GLU D  1 51  ? 50.192  82.289  52.088  1.00 29.10  ? 51  GLU D CD  1 
ATOM   10820 O  OE1 . GLU D  1 51  ? 50.031  81.982  50.892  1.00 34.26  ? 51  GLU D OE1 1 
ATOM   10821 O  OE2 . GLU D  1 51  ? 49.918  81.530  53.045  1.00 30.78  ? 51  GLU D OE2 1 
ATOM   10822 N  N   . PRO D  1 52  ? 52.548  85.525  49.341  1.00 31.76  ? 52  PRO D N   1 
ATOM   10823 C  CA  . PRO D  1 52  ? 52.108  86.069  48.069  1.00 35.58  ? 52  PRO D CA  1 
ATOM   10824 C  C   . PRO D  1 52  ? 50.635  86.420  47.960  1.00 35.69  ? 52  PRO D C   1 
ATOM   10825 O  O   . PRO D  1 52  ? 50.324  87.578  47.709  1.00 47.52  ? 52  PRO D O   1 
ATOM   10826 C  CB  . PRO D  1 52  ? 52.541  84.992  47.100  1.00 32.19  ? 52  PRO D CB  1 
ATOM   10827 C  CG  . PRO D  1 52  ? 53.872  84.690  47.628  1.00 29.47  ? 52  PRO D CG  1 
ATOM   10828 C  CD  . PRO D  1 52  ? 53.662  84.598  49.122  1.00 30.04  ? 52  PRO D CD  1 
ATOM   10829 N  N   . GLY D  1 53  ? 49.739  85.458  48.155  1.00 31.06  ? 53  GLY D N   1 
ATOM   10830 C  CA  . GLY D  1 53  ? 48.312  85.736  48.077  1.00 33.39  ? 53  GLY D CA  1 
ATOM   10831 C  C   . GLY D  1 53  ? 47.800  85.801  46.651  1.00 34.79  ? 53  GLY D C   1 
ATOM   10832 O  O   . GLY D  1 53  ? 48.593  85.606  45.731  1.00 36.15  ? 53  GLY D O   1 
ATOM   10833 N  N   . SER D  1 54  ? 46.495  86.070  46.468  1.00 38.34  ? 54  SER D N   1 
ATOM   10834 C  CA  . SER D  1 54  ? 45.859  86.159  45.125  1.00 37.93  ? 54  SER D CA  1 
ATOM   10835 C  C   . SER D  1 54  ? 45.862  87.607  44.689  1.00 39.99  ? 54  SER D C   1 
ATOM   10836 O  O   . SER D  1 54  ? 45.777  88.507  45.549  1.00 47.83  ? 54  SER D O   1 
ATOM   10837 C  CB  . SER D  1 54  ? 44.388  85.688  45.189  1.00 40.05  ? 54  SER D CB  1 
ATOM   10838 O  OG  . SER D  1 54  ? 43.688  85.746  43.948  1.00 38.64  ? 54  SER D OG  1 
ATOM   10839 N  N   . SER D  1 55  ? 46.021  87.843  43.391  1.00 34.48  ? 55  SER D N   1 
ATOM   10840 C  CA  . SER D  1 55  ? 45.979  89.195  42.882  1.00 31.59  ? 55  SER D CA  1 
ATOM   10841 C  C   . SER D  1 55  ? 44.636  89.429  42.229  1.00 32.75  ? 55  SER D C   1 
ATOM   10842 O  O   . SER D  1 55  ? 44.516  90.277  41.357  1.00 36.82  ? 55  SER D O   1 
ATOM   10843 C  CB  . SER D  1 55  ? 47.087  89.436  41.878  1.00 32.38  ? 55  SER D CB  1 
ATOM   10844 O  OG  . SER D  1 55  ? 48.314  89.216  42.517  1.00 34.08  ? 55  SER D OG  1 
ATOM   10845 N  N   . ALA D  1 56  ? 43.639  88.637  42.603  1.00 30.99  ? 56  ALA D N   1 
ATOM   10846 C  CA  . ALA D  1 56  ? 42.312  88.805  42.034  1.00 30.98  ? 56  ALA D CA  1 
ATOM   10847 C  C   . ALA D  1 56  ? 41.619  89.866  42.863  1.00 35.26  ? 56  ALA D C   1 
ATOM   10848 O  O   . ALA D  1 56  ? 41.920  90.038  44.052  1.00 39.43  ? 56  ALA D O   1 
ATOM   10849 C  CB  . ALA D  1 56  ? 41.527  87.522  42.108  1.00 25.03  ? 56  ALA D CB  1 
ATOM   10850 N  N   . VAL D  1 57  ? 40.682  90.567  42.244  1.00 31.23  ? 57  VAL D N   1 
ATOM   10851 C  CA  . VAL D  1 57  ? 39.918  91.591  42.926  1.00 25.42  ? 57  VAL D CA  1 
ATOM   10852 C  C   . VAL D  1 57  ? 38.470  91.260  42.607  1.00 28.29  ? 57  VAL D C   1 
ATOM   10853 O  O   . VAL D  1 57  ? 38.143  90.951  41.456  1.00 29.86  ? 57  VAL D O   1 
ATOM   10854 C  CB  . VAL D  1 57  ? 40.260  92.981  42.371  1.00 23.14  ? 57  VAL D CB  1 
ATOM   10855 C  CG1 . VAL D  1 57  ? 39.265  94.003  42.866  1.00 16.74  ? 57  VAL D CG1 1 
ATOM   10856 C  CG2 . VAL D  1 57  ? 41.683  93.366  42.766  1.00 25.58  ? 57  VAL D CG2 1 
ATOM   10857 N  N   . ARG D  1 58  ? 37.621  91.205  43.620  1.00 30.11  ? 58  ARG D N   1 
ATOM   10858 C  CA  . ARG D  1 58  ? 36.233  90.912  43.352  1.00 33.59  ? 58  ARG D CA  1 
ATOM   10859 C  C   . ARG D  1 58  ? 35.508  92.228  43.458  1.00 35.45  ? 58  ARG D C   1 
ATOM   10860 O  O   . ARG D  1 58  ? 35.734  92.997  44.402  1.00 38.46  ? 58  ARG D O   1 
ATOM   10861 C  CB  . ARG D  1 58  ? 35.682  89.899  44.336  1.00 36.11  ? 58  ARG D CB  1 
ATOM   10862 C  CG  . ARG D  1 58  ? 34.216  89.653  44.124  1.00 43.10  ? 58  ARG D CG  1 
ATOM   10863 C  CD  . ARG D  1 58  ? 33.747  88.388  44.804  1.00 50.98  ? 58  ARG D CD  1 
ATOM   10864 N  NE  . ARG D  1 58  ? 34.244  88.243  46.170  1.00 56.98  ? 58  ARG D NE  1 
ATOM   10865 C  CZ  . ARG D  1 58  ? 34.858  87.143  46.609  1.00 61.23  ? 58  ARG D CZ  1 
ATOM   10866 N  NH1 . ARG D  1 58  ? 35.040  86.101  45.773  1.00 62.29  ? 58  ARG D NH1 1 
ATOM   10867 N  NH2 . ARG D  1 58  ? 35.297  87.080  47.871  1.00 55.01  ? 58  ARG D NH2 1 
ATOM   10868 N  N   . TYR D  1 59  ? 34.637  92.503  42.502  1.00 34.89  ? 59  TYR D N   1 
ATOM   10869 C  CA  . TYR D  1 59  ? 33.938  93.762  42.521  1.00 37.42  ? 59  TYR D CA  1 
ATOM   10870 C  C   . TYR D  1 59  ? 32.600  93.633  41.868  1.00 41.30  ? 59  TYR D C   1 
ATOM   10871 O  O   . TYR D  1 59  ? 32.424  92.817  40.951  1.00 37.14  ? 59  TYR D O   1 
ATOM   10872 C  CB  . TYR D  1 59  ? 34.721  94.802  41.757  1.00 29.34  ? 59  TYR D CB  1 
ATOM   10873 C  CG  . TYR D  1 59  ? 34.732  94.548  40.274  1.00 28.19  ? 59  TYR D CG  1 
ATOM   10874 C  CD1 . TYR D  1 59  ? 35.602  93.647  39.719  1.00 31.80  ? 59  TYR D CD1 1 
ATOM   10875 C  CD2 . TYR D  1 59  ? 33.920  95.265  39.421  1.00 28.91  ? 59  TYR D CD2 1 
ATOM   10876 C  CE1 . TYR D  1 59  ? 35.676  93.469  38.347  1.00 31.48  ? 59  TYR D CE1 1 
ATOM   10877 C  CE2 . TYR D  1 59  ? 33.984  95.096  38.050  1.00 25.82  ? 59  TYR D CE2 1 
ATOM   10878 C  CZ  . TYR D  1 59  ? 34.860  94.201  37.518  1.00 28.57  ? 59  TYR D CZ  1 
ATOM   10879 O  OH  . TYR D  1 59  ? 34.933  94.053  36.144  1.00 38.09  ? 59  TYR D OH  1 
ATOM   10880 N  N   . TRP D  1 60  ? 31.687  94.503  42.306  1.00 45.98  ? 60  TRP D N   1 
ATOM   10881 C  CA  . TRP D  1 60  ? 30.318  94.563  41.795  1.00 46.97  ? 60  TRP D CA  1 
ATOM   10882 C  C   . TRP D  1 60  ? 29.760  95.936  42.119  1.00 47.70  ? 60  TRP D C   1 
ATOM   10883 O  O   . TRP D  1 60  ? 30.243  96.599  43.048  1.00 45.61  ? 60  TRP D O   1 
ATOM   10884 C  CB  . TRP D  1 60  ? 29.455  93.502  42.451  1.00 44.64  ? 60  TRP D CB  1 
ATOM   10885 C  CG  . TRP D  1 60  ? 29.325  93.717  43.883  1.00 43.40  ? 60  TRP D CG  1 
ATOM   10886 C  CD1 . TRP D  1 60  ? 28.295  94.326  44.520  1.00 47.28  ? 60  TRP D CD1 1 
ATOM   10887 C  CD2 . TRP D  1 60  ? 30.253  93.328  44.895  1.00 46.21  ? 60  TRP D CD2 1 
ATOM   10888 N  NE1 . TRP D  1 60  ? 28.515  94.341  45.880  1.00 47.06  ? 60  TRP D NE1 1 
ATOM   10889 C  CE2 . TRP D  1 60  ? 29.714  93.738  46.139  1.00 44.57  ? 60  TRP D CE2 1 
ATOM   10890 C  CE3 . TRP D  1 60  ? 31.481  92.663  44.879  1.00 46.49  ? 60  TRP D CE3 1 
ATOM   10891 C  CZ2 . TRP D  1 60  ? 30.357  93.507  47.351  1.00 41.97  ? 60  TRP D CZ2 1 
ATOM   10892 C  CZ3 . TRP D  1 60  ? 32.124  92.423  46.091  1.00 47.78  ? 60  TRP D CZ3 1 
ATOM   10893 C  CH2 . TRP D  1 60  ? 31.557  92.846  47.311  1.00 46.71  ? 60  TRP D CH2 1 
ATOM   10894 N  N   . SER D  1 61  ? 28.757  96.357  41.349  1.00 48.17  ? 61  SER D N   1 
ATOM   10895 C  CA  . SER D  1 61  ? 28.157  97.669  41.533  1.00 49.23  ? 61  SER D CA  1 
ATOM   10896 C  C   . SER D  1 61  ? 27.026  97.534  42.478  1.00 53.21  ? 61  SER D C   1 
ATOM   10897 O  O   . SER D  1 61  ? 26.404  96.494  42.545  1.00 53.04  ? 61  SER D O   1 
ATOM   10898 C  CB  . SER D  1 61  ? 27.641  98.248  40.222  1.00 45.87  ? 61  SER D CB  1 
ATOM   10899 O  OG  . SER D  1 61  ? 26.630  97.427  39.676  1.00 45.60  ? 61  SER D OG  1 
ATOM   10900 N  N   . GLU D  1 62  ? 26.721  98.621  43.162  1.00 65.86  ? 62  GLU D N   1 
ATOM   10901 C  CA  . GLU D  1 62  ? 25.656  98.654  44.153  1.00 77.02  ? 62  GLU D CA  1 
ATOM   10902 C  C   . GLU D  1 62  ? 24.325  98.208  43.563  1.00 83.86  ? 62  GLU D C   1 
ATOM   10903 O  O   . GLU D  1 62  ? 23.583  97.467  44.213  1.00 87.55  ? 62  GLU D O   1 
ATOM   10904 C  CB  . GLU D  1 62  ? 25.545  100.063 44.727  1.00 80.04  ? 62  GLU D CB  1 
ATOM   10905 C  CG  . GLU D  1 62  ? 24.992  100.126 46.138  1.00 90.68  ? 62  GLU D CG  1 
ATOM   10906 C  CD  . GLU D  1 62  ? 24.974  101.553 46.702  1.00 96.62  ? 62  GLU D CD  1 
ATOM   10907 O  OE1 . GLU D  1 62  ? 24.614  102.502 45.954  1.00 98.33  ? 62  GLU D OE1 1 
ATOM   10908 O  OE2 . GLU D  1 62  ? 25.318  101.723 47.900  1.00 98.29  ? 62  GLU D OE2 1 
ATOM   10909 N  N   . LYS D  1 63  ? 24.054  98.636  42.326  1.00 90.71  ? 63  LYS D N   1 
ATOM   10910 C  CA  . LYS D  1 63  ? 22.812  98.313  41.595  1.00 96.33  ? 63  LYS D CA  1 
ATOM   10911 C  C   . LYS D  1 63  ? 22.749  96.865  41.061  1.00 97.90  ? 63  LYS D C   1 
ATOM   10912 O  O   . LYS D  1 63  ? 21.947  96.048  41.530  1.00 98.83  ? 63  LYS D O   1 
ATOM   10913 C  CB  . LYS D  1 63  ? 22.604  99.317  40.446  1.00 100.02 ? 63  LYS D CB  1 
ATOM   10914 C  CG  . LYS D  1 63  ? 23.908  99.806  39.800  1.00 105.38 ? 63  LYS D CG  1 
ATOM   10915 C  CD  . LYS D  1 63  ? 23.735  100.231 38.341  1.00 109.95 ? 63  LYS D CD  1 
ATOM   10916 C  CE  . LYS D  1 63  ? 23.631  99.025  37.381  1.00 113.77 ? 63  LYS D CE  1 
ATOM   10917 N  NZ  . LYS D  1 63  ? 24.898  98.219  37.255  1.00 117.10 ? 63  LYS D NZ  1 
ATOM   10918 N  N   . ASN D  1 64  ? 23.554  96.578  40.041  1.00 99.52  ? 64  ASN D N   1 
ATOM   10919 C  CA  . ASN D  1 64  ? 23.643  95.248  39.441  1.00 100.06 ? 64  ASN D CA  1 
ATOM   10920 C  C   . ASN D  1 64  ? 24.723  94.479  40.235  1.00 98.63  ? 64  ASN D C   1 
ATOM   10921 O  O   . ASN D  1 64  ? 25.923  94.507  39.898  1.00 97.78  ? 64  ASN D O   1 
ATOM   10922 C  CB  . ASN D  1 64  ? 23.993  95.393  37.947  1.00 103.94 ? 64  ASN D CB  1 
ATOM   10923 C  CG  . ASN D  1 64  ? 24.723  94.191  37.378  1.00 107.28 ? 64  ASN D CG  1 
ATOM   10924 O  OD1 . ASN D  1 64  ? 25.855  94.321  36.903  1.00 108.03 ? 64  ASN D OD1 1 
ATOM   10925 N  ND2 . ASN D  1 64  ? 24.073  93.021  37.397  1.00 110.31 ? 64  ASN D ND2 1 
ATOM   10926 N  N   . GLY D  1 65  ? 24.283  93.841  41.322  1.00 94.89  ? 65  GLY D N   1 
ATOM   10927 C  CA  . GLY D  1 65  ? 25.181  93.101  42.188  1.00 88.51  ? 65  GLY D CA  1 
ATOM   10928 C  C   . GLY D  1 65  ? 25.974  91.943  41.605  1.00 87.01  ? 65  GLY D C   1 
ATOM   10929 O  O   . GLY D  1 65  ? 26.533  91.170  42.381  1.00 86.64  ? 65  GLY D O   1 
ATOM   10930 N  N   . ARG D  1 66  ? 26.036  91.798  40.277  1.00 85.72  ? 66  ARG D N   1 
ATOM   10931 C  CA  . ARG D  1 66  ? 26.792  90.696  39.649  1.00 81.87  ? 66  ARG D CA  1 
ATOM   10932 C  C   . ARG D  1 66  ? 28.237  90.832  40.074  1.00 74.84  ? 66  ARG D C   1 
ATOM   10933 O  O   . ARG D  1 66  ? 28.901  91.800  39.715  1.00 75.12  ? 66  ARG D O   1 
ATOM   10934 C  CB  . ARG D  1 66  ? 26.702  90.759  38.114  1.00 88.67  ? 66  ARG D CB  1 
ATOM   10935 C  CG  . ARG D  1 66  ? 27.685  89.845  37.350  1.00 99.96  ? 66  ARG D CG  1 
ATOM   10936 C  CD  . ARG D  1 66  ? 27.784  90.252  35.858  1.00 112.76 ? 66  ARG D CD  1 
ATOM   10937 N  NE  . ARG D  1 66  ? 29.152  90.194  35.306  1.00 122.52 ? 66  ARG D NE  1 
ATOM   10938 C  CZ  . ARG D  1 66  ? 29.783  91.203  34.687  1.00 124.82 ? 66  ARG D CZ  1 
ATOM   10939 N  NH1 . ARG D  1 66  ? 29.192  92.383  34.518  1.00 125.71 ? 66  ARG D NH1 1 
ATOM   10940 N  NH2 . ARG D  1 66  ? 31.041  91.050  34.279  1.00 125.26 ? 66  ARG D NH2 1 
ATOM   10941 N  N   . LYS D  1 67  ? 28.698  89.903  40.898  1.00 65.01  ? 67  LYS D N   1 
ATOM   10942 C  CA  . LYS D  1 67  ? 30.075  89.953  41.369  1.00 56.02  ? 67  LYS D CA  1 
ATOM   10943 C  C   . LYS D  1 67  ? 30.983  89.441  40.288  1.00 50.53  ? 67  LYS D C   1 
ATOM   10944 O  O   . LYS D  1 67  ? 30.743  88.388  39.741  1.00 44.24  ? 67  LYS D O   1 
ATOM   10945 C  CB  . LYS D  1 67  ? 30.237  89.151  42.652  1.00 51.93  ? 67  LYS D CB  1 
ATOM   10946 C  CG  . LYS D  1 67  ? 29.381  89.693  43.805  1.00 53.66  ? 67  LYS D CG  1 
ATOM   10947 C  CD  . LYS D  1 67  ? 29.693  88.999  45.150  1.00 61.13  ? 67  LYS D CD  1 
ATOM   10948 C  CE  . LYS D  1 67  ? 28.924  89.604  46.338  1.00 64.04  ? 67  LYS D CE  1 
ATOM   10949 N  NZ  . LYS D  1 67  ? 29.430  89.140  47.685  1.00 68.57  ? 67  LYS D NZ  1 
ATOM   10950 N  N   . ARG D  1 68  ? 31.983  90.235  39.940  1.00 50.71  ? 68  ARG D N   1 
ATOM   10951 C  CA  . ARG D  1 68  ? 32.924  89.886  38.893  1.00 48.98  ? 68  ARG D CA  1 
ATOM   10952 C  C   . ARG D  1 68  ? 34.315  89.847  39.488  1.00 44.19  ? 68  ARG D C   1 
ATOM   10953 O  O   . ARG D  1 68  ? 34.531  90.362  40.589  1.00 48.59  ? 68  ARG D O   1 
ATOM   10954 C  CB  . ARG D  1 68  ? 32.854  90.930  37.792  1.00 56.69  ? 68  ARG D CB  1 
ATOM   10955 C  CG  . ARG D  1 68  ? 31.445  91.249  37.345  1.00 71.00  ? 68  ARG D CG  1 
ATOM   10956 C  CD  . ARG D  1 68  ? 31.218  92.771  37.151  1.00 87.63  ? 68  ARG D CD  1 
ATOM   10957 N  NE  . ARG D  1 68  ? 30.282  93.322  38.145  1.00 96.49  ? 68  ARG D NE  1 
ATOM   10958 C  CZ  . ARG D  1 68  ? 29.520  94.415  37.987  1.00 101.97 ? 68  ARG D CZ  1 
ATOM   10959 N  NH1 . ARG D  1 68  ? 29.551  95.149  36.861  1.00 103.49 ? 68  ARG D NH1 1 
ATOM   10960 N  NH2 . ARG D  1 68  ? 28.679  94.761  38.965  1.00 102.71 ? 68  ARG D NH2 1 
ATOM   10961 N  N   . ILE D  1 69  ? 35.256  89.245  38.763  1.00 37.87  ? 69  ILE D N   1 
ATOM   10962 C  CA  . ILE D  1 69  ? 36.639  89.125  39.223  1.00 33.54  ? 69  ILE D CA  1 
ATOM   10963 C  C   . ILE D  1 69  ? 37.681  89.607  38.229  1.00 32.14  ? 69  ILE D C   1 
ATOM   10964 O  O   . ILE D  1 69  ? 37.654  89.235  37.067  1.00 34.74  ? 69  ILE D O   1 
ATOM   10965 C  CB  . ILE D  1 69  ? 36.941  87.665  39.592  1.00 35.64  ? 69  ILE D CB  1 
ATOM   10966 C  CG1 . ILE D  1 69  ? 36.574  87.434  41.044  1.00 38.14  ? 69  ILE D CG1 1 
ATOM   10967 C  CG2 . ILE D  1 69  ? 38.398  87.297  39.367  1.00 39.76  ? 69  ILE D CG2 1 
ATOM   10968 C  CD1 . ILE D  1 69  ? 36.882  86.045  41.511  1.00 51.21  ? 69  ILE D CD1 1 
ATOM   10969 N  N   . ALA D  1 70  ? 38.609  90.436  38.679  1.00 30.80  ? 70  ALA D N   1 
ATOM   10970 C  CA  . ALA D  1 70  ? 39.680  90.922  37.810  1.00 29.72  ? 70  ALA D CA  1 
ATOM   10971 C  C   . ALA D  1 70  ? 40.937  90.266  38.307  1.00 33.24  ? 70  ALA D C   1 
ATOM   10972 O  O   . ALA D  1 70  ? 41.103  90.097  39.524  1.00 35.96  ? 70  ALA D O   1 
ATOM   10973 C  CB  . ALA D  1 70  ? 39.821  92.383  37.965  1.00 29.98  ? 70  ALA D CB  1 
ATOM   10974 N  N   . LYS D  1 71  ? 41.839  89.909  37.407  1.00 34.11  ? 71  LYS D N   1 
ATOM   10975 C  CA  . LYS D  1 71  ? 43.078  89.285  37.847  1.00 38.65  ? 71  LYS D CA  1 
ATOM   10976 C  C   . LYS D  1 71  ? 44.267  90.186  37.558  1.00 38.56  ? 71  LYS D C   1 
ATOM   10977 O  O   . LYS D  1 71  ? 44.451  90.582  36.435  1.00 45.21  ? 71  LYS D O   1 
ATOM   10978 C  CB  . LYS D  1 71  ? 43.245  87.927  37.176  1.00 50.63  ? 71  LYS D CB  1 
ATOM   10979 C  CG  . LYS D  1 71  ? 43.455  86.746  38.176  1.00 70.57  ? 71  LYS D CG  1 
ATOM   10980 C  CD  . LYS D  1 71  ? 44.828  86.843  39.010  1.00 83.76  ? 71  LYS D CD  1 
ATOM   10981 C  CE  . LYS D  1 71  ? 45.038  85.698  40.117  1.00 88.55  ? 71  LYS D CE  1 
ATOM   10982 N  NZ  . LYS D  1 71  ? 46.309  85.748  40.973  1.00 84.03  ? 71  LYS D NZ  1 
ATOM   10983 N  N   . GLY D  1 72  ? 45.028  90.561  38.585  1.00 40.29  ? 72  GLY D N   1 
ATOM   10984 C  CA  . GLY D  1 72  ? 46.180  91.438  38.426  1.00 36.69  ? 72  GLY D CA  1 
ATOM   10985 C  C   . GLY D  1 72  ? 47.518  90.723  38.425  1.00 35.97  ? 72  GLY D C   1 
ATOM   10986 O  O   . GLY D  1 72  ? 47.565  89.581  38.007  1.00 36.26  ? 72  GLY D O   1 
ATOM   10987 N  N   . LYS D  1 73  ? 48.592  91.408  38.840  1.00 34.77  ? 73  LYS D N   1 
ATOM   10988 C  CA  . LYS D  1 73  ? 49.935  90.845  38.895  1.00 32.87  ? 73  LYS D CA  1 
ATOM   10989 C  C   . LYS D  1 73  ? 50.600  91.135  40.237  1.00 36.44  ? 73  LYS D C   1 
ATOM   10990 O  O   . LYS D  1 73  ? 50.204  92.060  40.944  1.00 42.96  ? 73  LYS D O   1 
ATOM   10991 C  CB  . LYS D  1 73  ? 50.828  91.436  37.835  1.00 36.06  ? 73  LYS D CB  1 
ATOM   10992 C  CG  . LYS D  1 73  ? 50.513  91.107  36.425  1.00 54.12  ? 73  LYS D CG  1 
ATOM   10993 C  CD  . LYS D  1 73  ? 51.707  91.573  35.550  1.00 76.23  ? 73  LYS D CD  1 
ATOM   10994 C  CE  . LYS D  1 73  ? 51.420  91.623  34.010  1.00 86.50  ? 73  LYS D CE  1 
ATOM   10995 N  NZ  . LYS D  1 73  ? 52.584  92.160  33.156  1.00 91.32  ? 73  LYS D NZ  1 
ATOM   10996 N  N   . MET D  1 74  ? 51.656  90.385  40.559  1.00 35.20  ? 74  MET D N   1 
ATOM   10997 C  CA  . MET D  1 74  ? 52.370  90.563  41.809  1.00 27.94  ? 74  MET D CA  1 
ATOM   10998 C  C   . MET D  1 74  ? 53.823  90.816  41.561  1.00 28.28  ? 74  MET D C   1 
ATOM   10999 O  O   . MET D  1 74  ? 54.407  90.241  40.628  1.00 28.63  ? 74  MET D O   1 
ATOM   11000 C  CB  . MET D  1 74  ? 52.250  89.323  42.645  1.00 26.88  ? 74  MET D CB  1 
ATOM   11001 C  CG  . MET D  1 74  ? 52.770  89.525  44.000  1.00 29.14  ? 74  MET D CG  1 
ATOM   11002 S  SD  . MET D  1 74  ? 53.883  88.243  44.354  1.00 39.53  ? 74  MET D SD  1 
ATOM   11003 C  CE  . MET D  1 74  ? 55.353  88.873  43.769  1.00 42.12  ? 74  MET D CE  1 
ATOM   11004 N  N   . SER D  1 75  ? 54.419  91.620  42.439  1.00 25.58  ? 75  SER D N   1 
ATOM   11005 C  CA  . SER D  1 75  ? 55.835  91.971  42.342  1.00 23.93  ? 75  SER D CA  1 
ATOM   11006 C  C   . SER D  1 75  ? 56.477  92.214  43.699  1.00 22.12  ? 75  SER D C   1 
ATOM   11007 O  O   . SER D  1 75  ? 55.789  92.393  44.715  1.00 25.12  ? 75  SER D O   1 
ATOM   11008 C  CB  . SER D  1 75  ? 56.030  93.197  41.439  1.00 29.18  ? 75  SER D CB  1 
ATOM   11009 O  OG  . SER D  1 75  ? 54.942  94.125  41.504  1.00 42.92  ? 75  SER D OG  1 
ATOM   11010 N  N   . THR D  1 76  ? 57.798  92.178  43.724  1.00 16.94  ? 76  THR D N   1 
ATOM   11011 C  CA  . THR D  1 76  ? 58.533  92.415  44.942  1.00 16.74  ? 76  THR D CA  1 
ATOM   11012 C  C   . THR D  1 76  ? 59.826  93.095  44.534  1.00 19.11  ? 76  THR D C   1 
ATOM   11013 O  O   . THR D  1 76  ? 60.252  92.982  43.391  1.00 21.03  ? 76  THR D O   1 
ATOM   11014 C  CB  . THR D  1 76  ? 58.909  91.134  45.556  1.00 16.57  ? 76  THR D CB  1 
ATOM   11015 O  OG1 . THR D  1 76  ? 59.571  90.339  44.558  1.00 15.22  ? 76  THR D OG1 1 
ATOM   11016 C  CG2 . THR D  1 76  ? 57.688  90.412  46.088  1.00 13.56  ? 76  THR D CG2 1 
ATOM   11017 N  N   . TYR D  1 77  ? 60.443  93.803  45.463  1.00 21.80  ? 77  TYR D N   1 
ATOM   11018 C  CA  . TYR D  1 77  ? 61.690  94.478  45.186  1.00 25.12  ? 77  TYR D CA  1 
ATOM   11019 C  C   . TYR D  1 77  ? 62.528  94.449  46.462  1.00 28.06  ? 77  TYR D C   1 
ATOM   11020 O  O   . TYR D  1 77  ? 62.015  94.147  47.545  1.00 29.74  ? 77  TYR D O   1 
ATOM   11021 C  CB  . TYR D  1 77  ? 61.436  95.928  44.713  1.00 22.39  ? 77  TYR D CB  1 
ATOM   11022 C  CG  . TYR D  1 77  ? 61.050  96.918  45.776  1.00 18.46  ? 77  TYR D CG  1 
ATOM   11023 C  CD1 . TYR D  1 77  ? 59.715  97.115  46.116  1.00 20.46  ? 77  TYR D CD1 1 
ATOM   11024 C  CD2 . TYR D  1 77  ? 62.024  97.671  46.470  1.00 15.72  ? 77  TYR D CD2 1 
ATOM   11025 C  CE1 . TYR D  1 77  ? 59.353  98.011  47.121  1.00 15.03  ? 77  TYR D CE1 1 
ATOM   11026 C  CE2 . TYR D  1 77  ? 61.687  98.571  47.479  1.00 5.78   ? 77  TYR D CE2 1 
ATOM   11027 C  CZ  . TYR D  1 77  ? 60.345  98.725  47.795  1.00 15.43  ? 77  TYR D CZ  1 
ATOM   11028 O  OH  . TYR D  1 77  ? 59.945  99.500  48.856  1.00 22.62  ? 77  TYR D OH  1 
ATOM   11029 N  N   . ARG D  1 78  ? 63.833  94.654  46.326  1.00 26.65  ? 78  ARG D N   1 
ATOM   11030 C  CA  . ARG D  1 78  ? 64.678  94.711  47.498  1.00 30.14  ? 78  ARG D CA  1 
ATOM   11031 C  C   . ARG D  1 78  ? 65.315  96.056  47.402  1.00 33.74  ? 78  ARG D C   1 
ATOM   11032 O  O   . ARG D  1 78  ? 65.688  96.469  46.311  1.00 35.98  ? 78  ARG D O   1 
ATOM   11033 C  CB  . ARG D  1 78  ? 65.804  93.683  47.440  1.00 36.36  ? 78  ARG D CB  1 
ATOM   11034 C  CG  . ARG D  1 78  ? 65.381  92.227  47.626  1.00 41.58  ? 78  ARG D CG  1 
ATOM   11035 C  CD  . ARG D  1 78  ? 66.584  91.281  47.634  1.00 35.58  ? 78  ARG D CD  1 
ATOM   11036 N  NE  . ARG D  1 78  ? 66.826  90.648  48.931  1.00 41.47  ? 78  ARG D NE  1 
ATOM   11037 C  CZ  . ARG D  1 78  ? 66.678  89.349  49.176  1.00 34.15  ? 78  ARG D CZ  1 
ATOM   11038 N  NH1 . ARG D  1 78  ? 66.284  88.523  48.229  1.00 35.24  ? 78  ARG D NH1 1 
ATOM   11039 N  NH2 . ARG D  1 78  ? 66.906  88.879  50.385  1.00 30.63  ? 78  ARG D NH2 1 
ATOM   11040 N  N   . PHE D  1 79  ? 65.372  96.779  48.513  1.00 37.02  ? 79  PHE D N   1 
ATOM   11041 C  CA  . PHE D  1 79  ? 66.015  98.056  48.458  1.00 33.67  ? 79  PHE D CA  1 
ATOM   11042 C  C   . PHE D  1 79  ? 67.453  97.904  48.903  1.00 34.53  ? 79  PHE D C   1 
ATOM   11043 O  O   . PHE D  1 79  ? 68.333  97.832  48.056  1.00 46.81  ? 79  PHE D O   1 
ATOM   11044 C  CB  . PHE D  1 79  ? 65.275  99.182  49.172  1.00 35.72  ? 79  PHE D CB  1 
ATOM   11045 C  CG  . PHE D  1 79  ? 65.835  100.527 48.842  1.00 28.78  ? 79  PHE D CG  1 
ATOM   11046 C  CD1 . PHE D  1 79  ? 65.753  101.003 47.559  1.00 24.11  ? 79  PHE D CD1 1 
ATOM   11047 C  CD2 . PHE D  1 79  ? 66.592  101.233 49.771  1.00 31.55  ? 79  PHE D CD2 1 
ATOM   11048 C  CE1 . PHE D  1 79  ? 66.428  102.141 47.205  1.00 27.52  ? 79  PHE D CE1 1 
ATOM   11049 C  CE2 . PHE D  1 79  ? 67.280  102.391 49.424  1.00 29.24  ? 79  PHE D CE2 1 
ATOM   11050 C  CZ  . PHE D  1 79  ? 67.205  102.838 48.148  1.00 26.02  ? 79  PHE D CZ  1 
ATOM   11051 N  N   . PHE D  1 80  ? 67.776  97.830  50.174  1.00 26.85  ? 80  PHE D N   1 
ATOM   11052 C  CA  . PHE D  1 80  ? 69.234  97.665  50.418  1.00 24.98  ? 80  PHE D CA  1 
ATOM   11053 C  C   . PHE D  1 80  ? 69.286  96.412  51.217  1.00 22.53  ? 80  PHE D C   1 
ATOM   11054 O  O   . PHE D  1 80  ? 69.368  95.348  50.649  1.00 21.61  ? 80  PHE D O   1 
ATOM   11055 C  CB  . PHE D  1 80  ? 69.784  98.905  51.116  1.00 29.74  ? 80  PHE D CB  1 
ATOM   11056 C  CG  . PHE D  1 80  ? 71.108  98.722  51.765  1.00 32.07  ? 80  PHE D CG  1 
ATOM   11057 C  CD1 . PHE D  1 80  ? 72.247  98.489  51.011  1.00 34.72  ? 80  PHE D CD1 1 
ATOM   11058 C  CD2 . PHE D  1 80  ? 71.225  98.836  53.153  1.00 32.94  ? 80  PHE D CD2 1 
ATOM   11059 C  CE1 . PHE D  1 80  ? 73.500  98.370  51.638  1.00 30.40  ? 80  PHE D CE1 1 
ATOM   11060 C  CE2 . PHE D  1 80  ? 72.461  98.721  53.781  1.00 30.49  ? 80  PHE D CE2 1 
ATOM   11061 C  CZ  . PHE D  1 80  ? 73.598  98.488  53.025  1.00 25.95  ? 80  PHE D CZ  1 
ATOM   11062 N  N   . ASN D  1 81  ? 69.139  96.519  52.525  1.00 22.26  ? 81  ASN D N   1 
ATOM   11063 C  CA  . ASN D  1 81  ? 69.037  95.327  53.296  1.00 20.70  ? 81  ASN D CA  1 
ATOM   11064 C  C   . ASN D  1 81  ? 67.532  95.153  53.506  1.00 25.74  ? 81  ASN D C   1 
ATOM   11065 O  O   . ASN D  1 81  ? 67.165  94.331  54.312  1.00 34.51  ? 81  ASN D O   1 
ATOM   11066 C  CB  . ASN D  1 81  ? 69.873  95.347  54.581  1.00 20.79  ? 81  ASN D CB  1 
ATOM   11067 C  CG  . ASN D  1 81  ? 69.539  96.503  55.551  1.00 34.33  ? 81  ASN D CG  1 
ATOM   11068 O  OD1 . ASN D  1 81  ? 68.848  97.464  55.174  1.00 41.03  ? 81  ASN D OD1 1 
ATOM   11069 N  ND2 . ASN D  1 81  ? 70.064  96.375  56.793  1.00 38.59  ? 81  ASN D ND2 1 
ATOM   11070 N  N   . TYR D  1 82  ? 66.670  95.868  52.739  1.00 23.83  ? 82  TYR D N   1 
ATOM   11071 C  CA  . TYR D  1 82  ? 65.184  95.768  52.820  1.00 22.58  ? 82  TYR D CA  1 
ATOM   11072 C  C   . TYR D  1 82  ? 64.609  94.762  51.790  1.00 29.20  ? 82  TYR D C   1 
ATOM   11073 O  O   . TYR D  1 82  ? 65.235  94.537  50.746  1.00 37.23  ? 82  TYR D O   1 
ATOM   11074 C  CB  . TYR D  1 82  ? 64.525  97.137  52.501  1.00 20.58  ? 82  TYR D CB  1 
ATOM   11075 C  CG  . TYR D  1 82  ? 62.966  97.167  52.394  1.00 15.02  ? 82  TYR D CG  1 
ATOM   11076 C  CD1 . TYR D  1 82  ? 62.147  97.183  53.532  1.00 16.64  ? 82  TYR D CD1 1 
ATOM   11077 C  CD2 . TYR D  1 82  ? 62.295  97.164  51.163  1.00 18.61  ? 82  TYR D CD2 1 
ATOM   11078 C  CE1 . TYR D  1 82  ? 60.718  97.202  53.457  1.00 11.93  ? 82  TYR D CE1 1 
ATOM   11079 C  CE2 . TYR D  1 82  ? 60.853  97.182  51.093  1.00 18.27  ? 82  TYR D CE2 1 
ATOM   11080 C  CZ  . TYR D  1 82  ? 60.095  97.193  52.248  1.00 13.70  ? 82  TYR D CZ  1 
ATOM   11081 O  OH  . TYR D  1 82  ? 58.723  97.182  52.218  1.00 16.74  ? 82  TYR D OH  1 
ATOM   11082 N  N   . SER D  1 83  ? 63.405  94.231  52.036  1.00 26.70  ? 83  SER D N   1 
ATOM   11083 C  CA  . SER D  1 83  ? 62.716  93.304  51.113  1.00 27.24  ? 83  SER D CA  1 
ATOM   11084 C  C   . SER D  1 83  ? 61.222  93.537  51.155  1.00 24.39  ? 83  SER D C   1 
ATOM   11085 O  O   . SER D  1 83  ? 60.577  93.358  52.176  1.00 33.70  ? 83  SER D O   1 
ATOM   11086 C  CB  . SER D  1 83  ? 62.977  91.862  51.489  1.00 30.43  ? 83  SER D CB  1 
ATOM   11087 O  OG  . SER D  1 83  ? 64.370  91.615  51.627  1.00 44.78  ? 83  SER D OG  1 
ATOM   11088 N  N   . SER D  1 84  ? 60.657  93.930  50.046  1.00 21.66  ? 84  SER D N   1 
ATOM   11089 C  CA  . SER D  1 84  ? 59.264  94.228  50.037  1.00 22.83  ? 84  SER D CA  1 
ATOM   11090 C  C   . SER D  1 84  ? 58.443  93.026  50.369  1.00 19.46  ? 84  SER D C   1 
ATOM   11091 O  O   . SER D  1 84  ? 58.910  91.926  50.379  1.00 23.01  ? 84  SER D O   1 
ATOM   11092 C  CB  . SER D  1 84  ? 58.872  94.645  48.645  1.00 23.49  ? 84  SER D CB  1 
ATOM   11093 O  OG  . SER D  1 84  ? 59.027  93.541  47.776  1.00 31.13  ? 84  SER D OG  1 
ATOM   11094 N  N   . GLY D  1 85  ? 57.172  93.274  50.571  1.00 23.47  ? 85  GLY D N   1 
ATOM   11095 C  CA  . GLY D  1 85  ? 56.217  92.219  50.807  1.00 21.85  ? 85  GLY D CA  1 
ATOM   11096 C  C   . GLY D  1 85  ? 55.747  91.955  49.399  1.00 21.50  ? 85  GLY D C   1 
ATOM   11097 O  O   . GLY D  1 85  ? 56.466  92.300  48.449  1.00 27.28  ? 85  GLY D O   1 
ATOM   11098 N  N   . PHE D  1 86  ? 54.541  91.462  49.218  1.00 14.91  ? 86  PHE D N   1 
ATOM   11099 C  CA  . PHE D  1 86  ? 54.118  91.155  47.883  1.00 14.46  ? 86  PHE D CA  1 
ATOM   11100 C  C   . PHE D  1 86  ? 53.204  92.234  47.398  1.00 17.61  ? 86  PHE D C   1 
ATOM   11101 O  O   . PHE D  1 86  ? 52.097  92.411  47.874  1.00 25.65  ? 86  PHE D O   1 
ATOM   11102 C  CB  . PHE D  1 86  ? 53.515  89.751  47.855  1.00 17.87  ? 86  PHE D CB  1 
ATOM   11103 C  CG  . PHE D  1 86  ? 54.407  88.738  48.505  1.00 21.70  ? 86  PHE D CG  1 
ATOM   11104 C  CD1 . PHE D  1 86  ? 55.504  88.244  47.850  1.00 22.46  ? 86  PHE D CD1 1 
ATOM   11105 C  CD2 . PHE D  1 86  ? 54.219  88.378  49.816  1.00 24.31  ? 86  PHE D CD2 1 
ATOM   11106 C  CE1 . PHE D  1 86  ? 56.419  87.408  48.511  1.00 20.70  ? 86  PHE D CE1 1 
ATOM   11107 C  CE2 . PHE D  1 86  ? 55.119  87.554  50.473  1.00 22.72  ? 86  PHE D CE2 1 
ATOM   11108 C  CZ  . PHE D  1 86  ? 56.222  87.073  49.809  1.00 19.09  ? 86  PHE D CZ  1 
ATOM   11109 N  N   . ILE D  1 87  ? 53.682  92.968  46.420  1.00 16.71  ? 87  ILE D N   1 
ATOM   11110 C  CA  . ILE D  1 87  ? 52.920  94.069  45.898  1.00 20.15  ? 87  ILE D CA  1 
ATOM   11111 C  C   . ILE D  1 87  ? 51.974  93.582  44.813  1.00 21.24  ? 87  ILE D C   1 
ATOM   11112 O  O   . ILE D  1 87  ? 52.358  92.813  43.934  1.00 20.74  ? 87  ILE D O   1 
ATOM   11113 C  CB  . ILE D  1 87  ? 53.881  95.140  45.361  1.00 20.01  ? 87  ILE D CB  1 
ATOM   11114 C  CG1 . ILE D  1 87  ? 54.855  95.556  46.462  1.00 21.33  ? 87  ILE D CG1 1 
ATOM   11115 C  CG2 . ILE D  1 87  ? 53.142  96.356  44.982  1.00 21.63  ? 87  ILE D CG2 1 
ATOM   11116 C  CD1 . ILE D  1 87  ? 56.001  96.436  46.014  1.00 20.40  ? 87  ILE D CD1 1 
ATOM   11117 N  N   . HIS D  1 88  ? 50.725  94.010  44.886  1.00 23.78  ? 88  HIS D N   1 
ATOM   11118 C  CA  . HIS D  1 88  ? 49.736  93.607  43.891  1.00 26.08  ? 88  HIS D CA  1 
ATOM   11119 C  C   . HIS D  1 88  ? 49.103  94.769  43.163  1.00 25.63  ? 88  HIS D C   1 
ATOM   11120 O  O   . HIS D  1 88  ? 48.692  95.721  43.786  1.00 30.60  ? 88  HIS D O   1 
ATOM   11121 C  CB  . HIS D  1 88  ? 48.619  92.850  44.556  1.00 29.65  ? 88  HIS D CB  1 
ATOM   11122 C  CG  . HIS D  1 88  ? 49.071  91.622  45.257  1.00 28.83  ? 88  HIS D CG  1 
ATOM   11123 N  ND1 . HIS D  1 88  ? 49.407  91.607  46.590  1.00 28.66  ? 88  HIS D ND1 1 
ATOM   11124 C  CD2 . HIS D  1 88  ? 49.226  90.353  44.821  1.00 26.03  ? 88  HIS D CD2 1 
ATOM   11125 C  CE1 . HIS D  1 88  ? 49.743  90.380  46.954  1.00 25.92  ? 88  HIS D CE1 1 
ATOM   11126 N  NE2 . HIS D  1 88  ? 49.641  89.602  45.896  1.00 31.90  ? 88  HIS D NE2 1 
ATOM   11127 N  N   . HIS D  1 89  ? 48.964  94.657  41.851  1.00 21.48  ? 89  HIS D N   1 
ATOM   11128 C  CA  . HIS D  1 89  ? 48.375  95.692  41.039  1.00 18.02  ? 89  HIS D CA  1 
ATOM   11129 C  C   . HIS D  1 89  ? 47.407  95.026  40.056  1.00 20.89  ? 89  HIS D C   1 
ATOM   11130 O  O   . HIS D  1 89  ? 47.800  94.274  39.153  1.00 18.82  ? 89  HIS D O   1 
ATOM   11131 C  CB  . HIS D  1 89  ? 49.467  96.454  40.251  1.00 15.88  ? 89  HIS D CB  1 
ATOM   11132 C  CG  . HIS D  1 89  ? 50.430  97.260  41.094  1.00 19.08  ? 89  HIS D CG  1 
ATOM   11133 N  ND1 . HIS D  1 89  ? 50.055  98.371  41.827  1.00 20.34  ? 89  HIS D ND1 1 
ATOM   11134 C  CD2 . HIS D  1 89  ? 51.780  97.151  41.257  1.00 17.13  ? 89  HIS D CD2 1 
ATOM   11135 C  CE1 . HIS D  1 89  ? 51.127  98.914  42.399  1.00 19.84  ? 89  HIS D CE1 1 
ATOM   11136 N  NE2 . HIS D  1 89  ? 52.187  98.187  42.065  1.00 10.38  ? 89  HIS D NE2 1 
ATOM   11137 N  N   . THR D  1 90  ? 46.140  95.342  40.212  1.00 20.52  ? 90  THR D N   1 
ATOM   11138 C  CA  . THR D  1 90  ? 45.109  94.803  39.363  1.00 25.13  ? 90  THR D CA  1 
ATOM   11139 C  C   . THR D  1 90  ? 44.292  95.936  38.777  1.00 29.82  ? 90  THR D C   1 
ATOM   11140 O  O   . THR D  1 90  ? 43.831  96.793  39.496  1.00 37.09  ? 90  THR D O   1 
ATOM   11141 C  CB  . THR D  1 90  ? 44.206  93.919  40.182  1.00 22.66  ? 90  THR D CB  1 
ATOM   11142 O  OG1 . THR D  1 90  ? 45.000  92.840  40.676  1.00 24.20  ? 90  THR D OG1 1 
ATOM   11143 C  CG2 . THR D  1 90  ? 43.041  93.395  39.348  1.00 21.04  ? 90  THR D CG2 1 
ATOM   11144 N  N   . THR D  1 91  ? 44.025  95.883  37.488  1.00 31.14  ? 91  THR D N   1 
ATOM   11145 C  CA  . THR D  1 91  ? 43.265  96.926  36.838  1.00 27.62  ? 91  THR D CA  1 
ATOM   11146 C  C   . THR D  1 91  ? 41.857  96.455  36.500  1.00 30.63  ? 91  THR D C   1 
ATOM   11147 O  O   . THR D  1 91  ? 41.696  95.468  35.811  1.00 35.90  ? 91  THR D O   1 
ATOM   11148 C  CB  . THR D  1 91  ? 43.966  97.287  35.546  1.00 32.75  ? 91  THR D CB  1 
ATOM   11149 O  OG1 . THR D  1 91  ? 45.369  97.529  35.783  1.00 36.24  ? 91  THR D OG1 1 
ATOM   11150 C  CG2 . THR D  1 91  ? 43.346  98.485  34.949  1.00 28.06  ? 91  THR D CG2 1 
ATOM   11151 N  N   . ILE D  1 92  ? 40.834  97.148  36.979  1.00 33.52  ? 92  ILE D N   1 
ATOM   11152 C  CA  . ILE D  1 92  ? 39.460  96.774  36.693  1.00 32.61  ? 92  ILE D CA  1 
ATOM   11153 C  C   . ILE D  1 92  ? 39.037  97.630  35.517  1.00 35.27  ? 92  ILE D C   1 
ATOM   11154 O  O   . ILE D  1 92  ? 39.179  98.856  35.574  1.00 41.75  ? 92  ILE D O   1 
ATOM   11155 C  CB  . ILE D  1 92  ? 38.592  97.131  37.852  1.00 32.10  ? 92  ILE D CB  1 
ATOM   11156 C  CG1 . ILE D  1 92  ? 39.006  96.354  39.068  1.00 36.50  ? 92  ILE D CG1 1 
ATOM   11157 C  CG2 . ILE D  1 92  ? 37.224  96.689  37.609  1.00 36.72  ? 92  ILE D CG2 1 
ATOM   11158 C  CD1 . ILE D  1 92  ? 38.203  96.753  40.257  1.00 39.32  ? 92  ILE D CD1 1 
ATOM   11159 N  N   . ARG D  1 93  ? 38.477  97.035  34.470  1.00 34.34  ? 93  ARG D N   1 
ATOM   11160 C  CA  . ARG D  1 93  ? 38.100  97.843  33.306  1.00 34.79  ? 93  ARG D CA  1 
ATOM   11161 C  C   . ARG D  1 93  ? 36.632  97.894  33.003  1.00 35.19  ? 93  ARG D C   1 
ATOM   11162 O  O   . ARG D  1 93  ? 35.846  97.155  33.573  1.00 39.69  ? 93  ARG D O   1 
ATOM   11163 C  CB  . ARG D  1 93  ? 38.793  97.343  32.056  1.00 40.30  ? 93  ARG D CB  1 
ATOM   11164 C  CG  . ARG D  1 93  ? 40.220  97.584  32.047  1.00 46.21  ? 93  ARG D CG  1 
ATOM   11165 C  CD  . ARG D  1 93  ? 40.915  96.572  31.198  1.00 61.01  ? 93  ARG D CD  1 
ATOM   11166 N  NE  . ARG D  1 93  ? 42.349  96.824  31.258  1.00 75.60  ? 93  ARG D NE  1 
ATOM   11167 C  CZ  . ARG D  1 93  ? 42.924  97.961  30.851  1.00 84.17  ? 93  ARG D CZ  1 
ATOM   11168 N  NH1 . ARG D  1 93  ? 42.171  98.945  30.344  1.00 85.94  ? 93  ARG D NH1 1 
ATOM   11169 N  NH2 . ARG D  1 93  ? 44.244  98.144  30.995  1.00 90.67  ? 93  ARG D NH2 1 
ATOM   11170 N  N   . LYS D  1 94  ? 36.279  98.754  32.061  1.00 35.50  ? 94  LYS D N   1 
ATOM   11171 C  CA  . LYS D  1 94  ? 34.908  98.890  31.627  1.00 38.82  ? 94  LYS D CA  1 
ATOM   11172 C  C   . LYS D  1 94  ? 33.861  99.097  32.706  1.00 38.78  ? 94  LYS D C   1 
ATOM   11173 O  O   . LYS D  1 94  ? 32.835  98.436  32.728  1.00 41.62  ? 94  LYS D O   1 
ATOM   11174 C  CB  . LYS D  1 94  ? 34.540  97.712  30.748  1.00 47.65  ? 94  LYS D CB  1 
ATOM   11175 C  CG  . LYS D  1 94  ? 35.463  97.566  29.513  1.00 63.99  ? 94  LYS D CG  1 
ATOM   11176 C  CD  . LYS D  1 94  ? 35.075  96.380  28.571  1.00 76.63  ? 94  LYS D CD  1 
ATOM   11177 C  CE  . LYS D  1 94  ? 36.166  95.242  28.474  1.00 88.28  ? 94  LYS D CE  1 
ATOM   11178 N  NZ  . LYS D  1 94  ? 37.511  95.553  27.830  1.00 94.65  ? 94  LYS D NZ  1 
ATOM   11179 N  N   . LEU D  1 95  ? 34.093  100.059 33.581  1.00 38.88  ? 95  LEU D N   1 
ATOM   11180 C  CA  . LEU D  1 95  ? 33.132  100.352 34.627  1.00 37.35  ? 95  LEU D CA  1 
ATOM   11181 C  C   . LEU D  1 95  ? 32.065  101.262 34.039  1.00 36.50  ? 95  LEU D C   1 
ATOM   11182 O  O   . LEU D  1 95  ? 32.224  101.830 32.973  1.00 33.92  ? 95  LEU D O   1 
ATOM   11183 C  CB  . LEU D  1 95  ? 33.819  101.092 35.771  1.00 35.85  ? 95  LEU D CB  1 
ATOM   11184 C  CG  . LEU D  1 95  ? 35.047  100.391 36.325  1.00 35.82  ? 95  LEU D CG  1 
ATOM   11185 C  CD1 . LEU D  1 95  ? 35.725  101.214 37.401  1.00 37.42  ? 95  LEU D CD1 1 
ATOM   11186 C  CD2 . LEU D  1 95  ? 34.590  99.088  36.884  1.00 30.24  ? 95  LEU D CD2 1 
ATOM   11187 N  N   . LYS D  1 96  ? 30.944  101.352 34.713  1.00 39.30  ? 96  LYS D N   1 
ATOM   11188 C  CA  . LYS D  1 96  ? 29.896  102.245 34.272  1.00 45.24  ? 96  LYS D CA  1 
ATOM   11189 C  C   . LYS D  1 96  ? 30.241  103.579 34.928  1.00 42.22  ? 96  LYS D C   1 
ATOM   11190 O  O   . LYS D  1 96  ? 30.842  103.591 36.006  1.00 41.81  ? 96  LYS D O   1 
ATOM   11191 C  CB  . LYS D  1 96  ? 28.529  101.734 34.757  1.00 57.16  ? 96  LYS D CB  1 
ATOM   11192 C  CG  . LYS D  1 96  ? 27.763  100.855 33.721  1.00 72.61  ? 96  LYS D CG  1 
ATOM   11193 C  CD  . LYS D  1 96  ? 27.939  99.342  33.894  1.00 81.80  ? 96  LYS D CD  1 
ATOM   11194 C  CE  . LYS D  1 96  ? 27.098  98.783  35.056  1.00 89.33  ? 96  LYS D CE  1 
ATOM   11195 N  NZ  . LYS D  1 96  ? 27.357  97.331  35.389  1.00 93.41  ? 96  LYS D NZ  1 
ATOM   11196 N  N   . TYR D  1 97  ? 29.903  104.696 34.297  1.00 40.63  ? 97  TYR D N   1 
ATOM   11197 C  CA  . TYR D  1 97  ? 30.238  105.984 34.901  1.00 41.35  ? 97  TYR D CA  1 
ATOM   11198 C  C   . TYR D  1 97  ? 29.303  106.297 36.037  1.00 43.35  ? 97  TYR D C   1 
ATOM   11199 O  O   . TYR D  1 97  ? 28.197  105.756 36.099  1.00 46.02  ? 97  TYR D O   1 
ATOM   11200 C  CB  . TYR D  1 97  ? 30.138  107.120 33.904  1.00 37.78  ? 97  TYR D CB  1 
ATOM   11201 C  CG  . TYR D  1 97  ? 31.183  107.155 32.822  1.00 34.77  ? 97  TYR D CG  1 
ATOM   11202 C  CD1 . TYR D  1 97  ? 32.419  107.737 33.054  1.00 29.98  ? 97  TYR D CD1 1 
ATOM   11203 C  CD2 . TYR D  1 97  ? 30.893  106.718 31.529  1.00 35.52  ? 97  TYR D CD2 1 
ATOM   11204 C  CE1 . TYR D  1 97  ? 33.350  107.909 32.022  1.00 35.97  ? 97  TYR D CE1 1 
ATOM   11205 C  CE2 . TYR D  1 97  ? 31.817  106.884 30.490  1.00 41.86  ? 97  TYR D CE2 1 
ATOM   11206 C  CZ  . TYR D  1 97  ? 33.043  107.496 30.755  1.00 40.10  ? 97  TYR D CZ  1 
ATOM   11207 O  OH  . TYR D  1 97  ? 33.932  107.790 29.747  1.00 53.07  ? 97  TYR D OH  1 
ATOM   11208 N  N   . ASN D  1 98  ? 29.763  107.130 36.958  1.00 42.27  ? 98  ASN D N   1 
ATOM   11209 C  CA  . ASN D  1 98  ? 28.928  107.541 38.066  1.00 46.04  ? 98  ASN D CA  1 
ATOM   11210 C  C   . ASN D  1 98  ? 28.226  106.389 38.739  1.00 46.03  ? 98  ASN D C   1 
ATOM   11211 O  O   . ASN D  1 98  ? 27.007  106.394 38.862  1.00 48.39  ? 98  ASN D O   1 
ATOM   11212 C  CB  . ASN D  1 98  ? 27.874  108.527 37.555  1.00 54.64  ? 98  ASN D CB  1 
ATOM   11213 C  CG  . ASN D  1 98  ? 27.333  109.451 38.650  1.00 62.82  ? 98  ASN D CG  1 
ATOM   11214 O  OD1 . ASN D  1 98  ? 28.081  109.946 39.505  1.00 69.64  ? 98  ASN D OD1 1 
ATOM   11215 N  ND2 . ASN D  1 98  ? 26.040  109.731 38.594  1.00 71.67  ? 98  ASN D ND2 1 
ATOM   11216 N  N   . THR D  1 99  ? 28.986  105.430 39.242  1.00 49.80  ? 99  THR D N   1 
ATOM   11217 C  CA  . THR D  1 99  ? 28.377  104.283 39.898  1.00 48.17  ? 99  THR D CA  1 
ATOM   11218 C  C   . THR D  1 99  ? 29.216  103.910 41.086  1.00 46.33  ? 99  THR D C   1 
ATOM   11219 O  O   . THR D  1 99  ? 30.441  104.055 41.027  1.00 45.64  ? 99  THR D O   1 
ATOM   11220 C  CB  . THR D  1 99  ? 28.372  103.102 38.951  1.00 52.95  ? 99  THR D CB  1 
ATOM   11221 O  OG1 . THR D  1 99  ? 27.663  103.429 37.745  1.00 46.65  ? 99  THR D OG1 1 
ATOM   11222 C  CG2 . THR D  1 99  ? 27.728  101.930 39.615  1.00 59.33  ? 99  THR D CG2 1 
ATOM   11223 N  N   . LYS D  1 100 ? 28.580  103.480 42.173  1.00 46.30  ? 100 LYS D N   1 
ATOM   11224 C  CA  . LYS D  1 100 ? 29.357  103.077 43.355  1.00 47.81  ? 100 LYS D CA  1 
ATOM   11225 C  C   . LYS D  1 100 ? 29.670  101.641 43.152  1.00 43.08  ? 100 LYS D C   1 
ATOM   11226 O  O   . LYS D  1 100 ? 28.808  100.884 42.737  1.00 37.63  ? 100 LYS D O   1 
ATOM   11227 C  CB  . LYS D  1 100 ? 28.585  103.188 44.657  1.00 53.01  ? 100 LYS D CB  1 
ATOM   11228 C  CG  . LYS D  1 100 ? 29.413  102.833 45.886  1.00 60.34  ? 100 LYS D CG  1 
ATOM   11229 C  CD  . LYS D  1 100 ? 28.581  103.029 47.158  1.00 68.47  ? 100 LYS D CD  1 
ATOM   11230 C  CE  . LYS D  1 100 ? 29.453  103.185 48.408  1.00 75.95  ? 100 LYS D CE  1 
ATOM   11231 N  NZ  . LYS D  1 100 ? 28.671  103.442 49.670  1.00 81.96  ? 100 LYS D NZ  1 
ATOM   11232 N  N   . TYR D  1 101 ? 30.908  101.287 43.425  1.00 41.37  ? 101 TYR D N   1 
ATOM   11233 C  CA  . TYR D  1 101 ? 31.347  99.942  43.266  1.00 41.33  ? 101 TYR D CA  1 
ATOM   11234 C  C   . TYR D  1 101 ? 31.926  99.475  44.555  1.00 43.30  ? 101 TYR D C   1 
ATOM   11235 O  O   . TYR D  1 101 ? 32.422  100.282 45.342  1.00 41.21  ? 101 TYR D O   1 
ATOM   11236 C  CB  . TYR D  1 101 ? 32.420  99.889  42.223  1.00 41.14  ? 101 TYR D CB  1 
ATOM   11237 C  CG  . TYR D  1 101 ? 31.856  99.813  40.862  1.00 44.73  ? 101 TYR D CG  1 
ATOM   11238 C  CD1 . TYR D  1 101 ? 31.578  98.599  40.280  1.00 42.75  ? 101 TYR D CD1 1 
ATOM   11239 C  CD2 . TYR D  1 101 ? 31.635  100.957 40.125  1.00 52.17  ? 101 TYR D CD2 1 
ATOM   11240 C  CE1 . TYR D  1 101 ? 31.098  98.527  38.989  1.00 46.90  ? 101 TYR D CE1 1 
ATOM   11241 C  CE2 . TYR D  1 101 ? 31.151  100.891 38.817  1.00 51.97  ? 101 TYR D CE2 1 
ATOM   11242 C  CZ  . TYR D  1 101 ? 30.892  99.670  38.261  1.00 47.92  ? 101 TYR D CZ  1 
ATOM   11243 O  OH  . TYR D  1 101 ? 30.466  99.578  36.955  1.00 55.84  ? 101 TYR D OH  1 
ATOM   11244 N  N   . TYR D  1 102 ? 31.858  98.167  44.766  1.00 45.51  ? 102 TYR D N   1 
ATOM   11245 C  CA  . TYR D  1 102 ? 32.433  97.547  45.932  1.00 43.05  ? 102 TYR D CA  1 
ATOM   11246 C  C   . TYR D  1 102 ? 33.503  96.632  45.397  1.00 42.09  ? 102 TYR D C   1 
ATOM   11247 O  O   . TYR D  1 102 ? 33.327  95.983  44.339  1.00 38.12  ? 102 TYR D O   1 
ATOM   11248 C  CB  . TYR D  1 102 ? 31.408  96.696  46.629  1.00 50.18  ? 102 TYR D CB  1 
ATOM   11249 C  CG  . TYR D  1 102 ? 30.440  97.499  47.423  1.00 58.05  ? 102 TYR D CG  1 
ATOM   11250 C  CD1 . TYR D  1 102 ? 30.817  98.065  48.635  1.00 62.46  ? 102 TYR D CD1 1 
ATOM   11251 C  CD2 . TYR D  1 102 ? 29.148  97.713  46.966  1.00 63.38  ? 102 TYR D CD2 1 
ATOM   11252 C  CE1 . TYR D  1 102 ? 29.932  98.833  49.377  1.00 67.91  ? 102 TYR D CE1 1 
ATOM   11253 C  CE2 . TYR D  1 102 ? 28.247  98.478  47.697  1.00 68.84  ? 102 TYR D CE2 1 
ATOM   11254 C  CZ  . TYR D  1 102 ? 28.650  99.039  48.896  1.00 71.55  ? 102 TYR D CZ  1 
ATOM   11255 O  OH  . TYR D  1 102 ? 27.793  99.858  49.587  1.00 80.58  ? 102 TYR D OH  1 
ATOM   11256 N  N   . TYR D  1 103 ? 34.620  96.597  46.094  1.00 37.41  ? 103 TYR D N   1 
ATOM   11257 C  CA  . TYR D  1 103 ? 35.679  95.712  45.688  1.00 35.48  ? 103 TYR D CA  1 
ATOM   11258 C  C   . TYR D  1 103 ? 36.246  95.075  46.964  1.00 36.70  ? 103 TYR D C   1 
ATOM   11259 O  O   . TYR D  1 103 ? 36.190  95.651  48.072  1.00 33.61  ? 103 TYR D O   1 
ATOM   11260 C  CB  . TYR D  1 103 ? 36.731  96.434  44.829  1.00 31.54  ? 103 TYR D CB  1 
ATOM   11261 C  CG  . TYR D  1 103 ? 37.629  97.421  45.560  1.00 32.73  ? 103 TYR D CG  1 
ATOM   11262 C  CD1 . TYR D  1 103 ? 38.789  96.998  46.196  1.00 30.33  ? 103 TYR D CD1 1 
ATOM   11263 C  CD2 . TYR D  1 103 ? 37.341  98.784  45.590  1.00 31.98  ? 103 TYR D CD2 1 
ATOM   11264 C  CE1 . TYR D  1 103 ? 39.639  97.901  46.837  1.00 29.21  ? 103 TYR D CE1 1 
ATOM   11265 C  CE2 . TYR D  1 103 ? 38.201  99.696  46.236  1.00 28.35  ? 103 TYR D CE2 1 
ATOM   11266 C  CZ  . TYR D  1 103 ? 39.342  99.244  46.848  1.00 26.83  ? 103 TYR D CZ  1 
ATOM   11267 O  OH  . TYR D  1 103 ? 40.207  100.132 47.435  1.00 23.81  ? 103 TYR D OH  1 
ATOM   11268 N  N   . GLU D  1 104 ? 36.632  93.818  46.830  1.00 36.36  ? 104 GLU D N   1 
ATOM   11269 C  CA  . GLU D  1 104 ? 37.188  93.063  47.923  1.00 34.33  ? 104 GLU D CA  1 
ATOM   11270 C  C   . GLU D  1 104 ? 38.536  92.612  47.456  1.00 32.69  ? 104 GLU D C   1 
ATOM   11271 O  O   . GLU D  1 104 ? 38.730  92.241  46.319  1.00 35.61  ? 104 GLU D O   1 
ATOM   11272 C  CB  . GLU D  1 104 ? 36.308  91.874  48.255  1.00 36.03  ? 104 GLU D CB  1 
ATOM   11273 C  CG  . GLU D  1 104 ? 35.014  92.257  48.909  1.00 37.53  ? 104 GLU D CG  1 
ATOM   11274 C  CD  . GLU D  1 104 ? 34.156  91.057  49.243  1.00 40.56  ? 104 GLU D CD  1 
ATOM   11275 O  OE1 . GLU D  1 104 ? 33.800  90.255  48.342  1.00 38.53  ? 104 GLU D OE1 1 
ATOM   11276 O  OE2 . GLU D  1 104 ? 33.839  90.911  50.435  1.00 45.66  ? 104 GLU D OE2 1 
ATOM   11277 N  N   . VAL D  1 105 ? 39.450  92.528  48.383  1.00 33.42  ? 105 VAL D N   1 
ATOM   11278 C  CA  . VAL D  1 105 ? 40.799  92.189  48.047  1.00 28.58  ? 105 VAL D CA  1 
ATOM   11279 C  C   . VAL D  1 105 ? 41.261  91.272  49.182  1.00 32.87  ? 105 VAL D C   1 
ATOM   11280 O  O   . VAL D  1 105 ? 40.821  91.414  50.320  1.00 34.10  ? 105 VAL D O   1 
ATOM   11281 C  CB  . VAL D  1 105 ? 41.545  93.539  47.949  1.00 27.24  ? 105 VAL D CB  1 
ATOM   11282 C  CG1 . VAL D  1 105 ? 42.331  93.838  49.161  1.00 22.06  ? 105 VAL D CG1 1 
ATOM   11283 C  CG2 . VAL D  1 105 ? 42.287  93.652  46.681  1.00 27.85  ? 105 VAL D CG2 1 
ATOM   11284 N  N   . GLY D  1 106 ? 42.108  90.303  48.866  1.00 35.22  ? 106 GLY D N   1 
ATOM   11285 C  CA  . GLY D  1 106 ? 42.581  89.358  49.866  1.00 34.61  ? 106 GLY D CA  1 
ATOM   11286 C  C   . GLY D  1 106 ? 41.660  88.165  49.858  1.00 34.99  ? 106 GLY D C   1 
ATOM   11287 O  O   . GLY D  1 106 ? 41.333  87.626  50.902  1.00 35.34  ? 106 GLY D O   1 
ATOM   11288 N  N   . LEU D  1 107 ? 41.313  87.693  48.669  1.00 33.78  ? 107 LEU D N   1 
ATOM   11289 C  CA  . LEU D  1 107 ? 40.368  86.590  48.555  1.00 42.23  ? 107 LEU D CA  1 
ATOM   11290 C  C   . LEU D  1 107 ? 40.777  85.255  49.178  1.00 47.03  ? 107 LEU D C   1 
ATOM   11291 O  O   . LEU D  1 107 ? 39.913  84.515  49.660  1.00 51.62  ? 107 LEU D O   1 
ATOM   11292 C  CB  . LEU D  1 107 ? 39.934  86.344  47.091  1.00 36.64  ? 107 LEU D CB  1 
ATOM   11293 C  CG  . LEU D  1 107 ? 39.534  87.513  46.179  1.00 37.47  ? 107 LEU D CG  1 
ATOM   11294 C  CD1 . LEU D  1 107 ? 38.918  86.965  44.919  1.00 31.16  ? 107 LEU D CD1 1 
ATOM   11295 C  CD2 . LEU D  1 107 ? 38.592  88.498  46.847  1.00 34.49  ? 107 LEU D CD2 1 
ATOM   11296 N  N   . ARG D  1 108 ? 42.071  84.932  49.164  1.00 48.90  ? 108 ARG D N   1 
ATOM   11297 C  CA  . ARG D  1 108 ? 42.510  83.638  49.690  1.00 47.78  ? 108 ARG D CA  1 
ATOM   11298 C  C   . ARG D  1 108 ? 42.413  83.530  51.184  1.00 45.60  ? 108 ARG D C   1 
ATOM   11299 O  O   . ARG D  1 108 ? 41.925  82.547  51.693  1.00 52.23  ? 108 ARG D O   1 
ATOM   11300 C  CB  . ARG D  1 108 ? 43.933  83.272  49.239  1.00 50.23  ? 108 ARG D CB  1 
ATOM   11301 C  CG  . ARG D  1 108 ? 44.031  82.305  48.027  1.00 55.56  ? 108 ARG D CG  1 
ATOM   11302 C  CD  . ARG D  1 108 ? 45.499  81.946  47.611  1.00 63.09  ? 108 ARG D CD  1 
ATOM   11303 N  NE  . ARG D  1 108 ? 46.188  80.991  48.498  1.00 78.39  ? 108 ARG D NE  1 
ATOM   11304 C  CZ  . ARG D  1 108 ? 46.734  81.274  49.697  1.00 88.80  ? 108 ARG D CZ  1 
ATOM   11305 N  NH1 . ARG D  1 108 ? 46.691  82.511  50.218  1.00 94.16  ? 108 ARG D NH1 1 
ATOM   11306 N  NH2 . ARG D  1 108 ? 47.366  80.313  50.384  1.00 90.67  ? 108 ARG D NH2 1 
ATOM   11307 N  N   . ASN D  1 109 ? 42.918  84.502  51.909  1.00 46.50  ? 109 ASN D N   1 
ATOM   11308 C  CA  . ASN D  1 109 ? 42.829  84.369  53.335  1.00 46.15  ? 109 ASN D CA  1 
ATOM   11309 C  C   . ASN D  1 109 ? 41.969  85.402  53.998  1.00 46.04  ? 109 ASN D C   1 
ATOM   11310 O  O   . ASN D  1 109 ? 40.802  85.147  54.254  1.00 53.59  ? 109 ASN D O   1 
ATOM   11311 C  CB  . ASN D  1 109 ? 44.212  84.238  53.972  1.00 46.99  ? 109 ASN D CB  1 
ATOM   11312 C  CG  . ASN D  1 109 ? 44.859  82.925  53.628  1.00 50.93  ? 109 ASN D CG  1 
ATOM   11313 O  OD1 . ASN D  1 109 ? 45.612  82.882  52.667  1.00 51.48  ? 109 ASN D OD1 1 
ATOM   11314 N  ND2 . ASN D  1 109 ? 44.502  81.861  54.364  1.00 54.29  ? 109 ASN D ND2 1 
ATOM   11315 N  N   . THR D  1 110 ? 42.518  86.570  54.280  1.00 45.02  ? 110 THR D N   1 
ATOM   11316 C  CA  . THR D  1 110 ? 41.747  87.622  54.933  1.00 40.02  ? 110 THR D CA  1 
ATOM   11317 C  C   . THR D  1 110 ? 41.258  88.641  53.890  1.00 41.84  ? 110 THR D C   1 
ATOM   11318 O  O   . THR D  1 110 ? 42.044  89.344  53.246  1.00 46.99  ? 110 THR D O   1 
ATOM   11319 C  CB  . THR D  1 110 ? 42.605  88.275  55.995  1.00 37.61  ? 110 THR D CB  1 
ATOM   11320 O  OG1 . THR D  1 110 ? 43.070  87.264  56.891  1.00 41.59  ? 110 THR D OG1 1 
ATOM   11321 C  CG2 . THR D  1 110 ? 41.845  89.301  56.777  1.00 43.07  ? 110 THR D CG2 1 
ATOM   11322 N  N   . THR D  1 111 ? 39.952  88.674  53.684  1.00 40.49  ? 111 THR D N   1 
ATOM   11323 C  CA  . THR D  1 111 ? 39.346  89.565  52.711  1.00 38.11  ? 111 THR D CA  1 
ATOM   11324 C  C   . THR D  1 111 ? 38.959  90.927  53.294  1.00 36.43  ? 111 THR D C   1 
ATOM   11325 O  O   . THR D  1 111 ? 38.504  91.005  54.435  1.00 40.63  ? 111 THR D O   1 
ATOM   11326 C  CB  . THR D  1 111 ? 38.105  88.889  52.113  1.00 38.77  ? 111 THR D CB  1 
ATOM   11327 O  OG1 . THR D  1 111 ? 38.496  87.801  51.249  1.00 36.63  ? 111 THR D OG1 1 
ATOM   11328 C  CG2 . THR D  1 111 ? 37.303  89.880  51.332  1.00 43.52  ? 111 THR D CG2 1 
ATOM   11329 N  N   . ARG D  1 112 ? 39.209  92.005  52.541  1.00 37.98  ? 112 ARG D N   1 
ATOM   11330 C  CA  . ARG D  1 112 ? 38.837  93.362  52.961  1.00 31.72  ? 112 ARG D CA  1 
ATOM   11331 C  C   . ARG D  1 112 ? 38.092  93.994  51.843  1.00 33.09  ? 112 ARG D C   1 
ATOM   11332 O  O   . ARG D  1 112 ? 38.403  93.761  50.670  1.00 32.63  ? 112 ARG D O   1 
ATOM   11333 C  CB  . ARG D  1 112 ? 40.023  94.173  53.356  1.00 27.51  ? 112 ARG D CB  1 
ATOM   11334 C  CG  . ARG D  1 112 ? 40.629  93.619  54.619  1.00 30.19  ? 112 ARG D CG  1 
ATOM   11335 C  CD  . ARG D  1 112 ? 41.892  94.335  54.989  1.00 30.05  ? 112 ARG D CD  1 
ATOM   11336 N  NE  . ARG D  1 112 ? 41.608  95.670  55.470  1.00 32.60  ? 112 ARG D NE  1 
ATOM   11337 C  CZ  . ARG D  1 112 ? 42.363  96.743  55.233  1.00 31.34  ? 112 ARG D CZ  1 
ATOM   11338 N  NH1 . ARG D  1 112 ? 43.468  96.671  54.520  1.00 38.53  ? 112 ARG D NH1 1 
ATOM   11339 N  NH2 . ARG D  1 112 ? 42.001  97.909  55.722  1.00 31.17  ? 112 ARG D NH2 1 
ATOM   11340 N  N   . ARG D  1 113 ? 37.032  94.703  52.218  1.00 37.60  ? 113 ARG D N   1 
ATOM   11341 C  CA  . ARG D  1 113 ? 36.120  95.334  51.267  1.00 41.54  ? 113 ARG D CA  1 
ATOM   11342 C  C   . ARG D  1 113 ? 36.224  96.837  51.243  1.00 42.95  ? 113 ARG D C   1 
ATOM   11343 O  O   . ARG D  1 113 ? 36.502  97.484  52.269  1.00 47.06  ? 113 ARG D O   1 
ATOM   11344 C  CB  . ARG D  1 113 ? 34.679  94.943  51.618  1.00 44.11  ? 113 ARG D CB  1 
ATOM   11345 C  CG  . ARG D  1 113 ? 33.570  95.637  50.832  1.00 54.52  ? 113 ARG D CG  1 
ATOM   11346 C  CD  . ARG D  1 113 ? 32.201  95.063  51.204  1.00 60.64  ? 113 ARG D CD  1 
ATOM   11347 N  NE  . ARG D  1 113 ? 32.128  93.647  50.814  1.00 73.73  ? 113 ARG D NE  1 
ATOM   11348 C  CZ  . ARG D  1 113 ? 31.067  92.855  50.985  1.00 78.78  ? 113 ARG D CZ  1 
ATOM   11349 N  NH1 . ARG D  1 113 ? 29.964  93.343  51.544  1.00 83.28  ? 113 ARG D NH1 1 
ATOM   11350 N  NH2 . ARG D  1 113 ? 31.107  91.570  50.608  1.00 80.95  ? 113 ARG D NH2 1 
ATOM   11351 N  N   . PHE D  1 114 ? 36.026  97.395  50.061  1.00 38.10  ? 114 PHE D N   1 
ATOM   11352 C  CA  . PHE D  1 114 ? 36.056  98.827  49.923  1.00 34.62  ? 114 PHE D CA  1 
ATOM   11353 C  C   . PHE D  1 114 ? 35.036  99.216  48.827  1.00 37.39  ? 114 PHE D C   1 
ATOM   11354 O  O   . PHE D  1 114 ? 34.368  98.333  48.210  1.00 32.17  ? 114 PHE D O   1 
ATOM   11355 C  CB  . PHE D  1 114 ? 37.472  99.285  49.552  1.00 32.32  ? 114 PHE D CB  1 
ATOM   11356 C  CG  . PHE D  1 114 ? 38.538  98.824  50.494  1.00 27.32  ? 114 PHE D CG  1 
ATOM   11357 C  CD1 . PHE D  1 114 ? 38.887  99.577  51.610  1.00 27.48  ? 114 PHE D CD1 1 
ATOM   11358 C  CD2 . PHE D  1 114 ? 39.227  97.650  50.244  1.00 29.54  ? 114 PHE D CD2 1 
ATOM   11359 C  CE1 . PHE D  1 114 ? 39.902  99.170  52.463  1.00 22.10  ? 114 PHE D CE1 1 
ATOM   11360 C  CE2 . PHE D  1 114 ? 40.266  97.227  51.097  1.00 24.98  ? 114 PHE D CE2 1 
ATOM   11361 C  CZ  . PHE D  1 114 ? 40.595  97.988  52.198  1.00 24.51  ? 114 PHE D CZ  1 
ATOM   11362 N  N   . SER D  1 115 ? 34.937  100.523 48.575  1.00 36.04  ? 115 SER D N   1 
ATOM   11363 C  CA  . SER D  1 115 ? 34.058  101.044 47.562  1.00 36.50  ? 115 SER D CA  1 
ATOM   11364 C  C   . SER D  1 115 ? 34.630  102.325 47.000  1.00 38.08  ? 115 SER D C   1 
ATOM   11365 O  O   . SER D  1 115 ? 35.312  103.100 47.695  1.00 40.97  ? 115 SER D O   1 
ATOM   11366 C  CB  . SER D  1 115 ? 32.693  101.353 48.158  1.00 39.54  ? 115 SER D CB  1 
ATOM   11367 O  OG  . SER D  1 115 ? 32.810  102.297 49.210  1.00 51.66  ? 115 SER D OG  1 
ATOM   11368 N  N   . PHE D  1 116 ? 34.308  102.572 45.747  1.00 37.23  ? 116 PHE D N   1 
ATOM   11369 C  CA  . PHE D  1 116 ? 34.726  103.783 45.104  1.00 36.66  ? 116 PHE D CA  1 
ATOM   11370 C  C   . PHE D  1 116 ? 33.574  104.118 44.166  1.00 36.72  ? 116 PHE D C   1 
ATOM   11371 O  O   . PHE D  1 116 ? 32.690  103.276 43.922  1.00 36.39  ? 116 PHE D O   1 
ATOM   11372 C  CB  . PHE D  1 116 ? 36.053  103.573 44.350  1.00 37.69  ? 116 PHE D CB  1 
ATOM   11373 C  CG  . PHE D  1 116 ? 36.002  102.531 43.258  1.00 39.14  ? 116 PHE D CG  1 
ATOM   11374 C  CD1 . PHE D  1 116 ? 35.308  102.762 42.069  1.00 35.96  ? 116 PHE D CD1 1 
ATOM   11375 C  CD2 . PHE D  1 116 ? 36.665  101.323 43.416  1.00 41.14  ? 116 PHE D CD2 1 
ATOM   11376 C  CE1 . PHE D  1 116 ? 35.272  101.816 41.069  1.00 35.69  ? 116 PHE D CE1 1 
ATOM   11377 C  CE2 . PHE D  1 116 ? 36.641  100.365 42.416  1.00 38.64  ? 116 PHE D CE2 1 
ATOM   11378 C  CZ  . PHE D  1 116 ? 35.940  100.613 41.240  1.00 38.45  ? 116 PHE D CZ  1 
ATOM   11379 N  N   . ILE D  1 117 ? 33.568  105.341 43.652  1.00 36.10  ? 117 ILE D N   1 
ATOM   11380 C  CA  . ILE D  1 117 ? 32.524  105.748 42.723  1.00 36.41  ? 117 ILE D CA  1 
ATOM   11381 C  C   . ILE D  1 117 ? 33.094  106.244 41.416  1.00 34.11  ? 117 ILE D C   1 
ATOM   11382 O  O   . ILE D  1 117 ? 33.928  107.155 41.415  1.00 39.98  ? 117 ILE D O   1 
ATOM   11383 C  CB  . ILE D  1 117 ? 31.704  106.834 43.303  1.00 36.48  ? 117 ILE D CB  1 
ATOM   11384 C  CG1 . ILE D  1 117 ? 31.166  106.376 44.649  1.00 37.10  ? 117 ILE D CG1 1 
ATOM   11385 C  CG2 . ILE D  1 117 ? 30.586  107.152 42.371  1.00 40.81  ? 117 ILE D CG2 1 
ATOM   11386 C  CD1 . ILE D  1 117 ? 30.403  107.416 45.367  1.00 33.27  ? 117 ILE D CD1 1 
ATOM   11387 N  N   . THR D  1 118 ? 32.659  105.665 40.305  1.00 29.59  ? 118 THR D N   1 
ATOM   11388 C  CA  . THR D  1 118 ? 33.208  106.094 39.037  1.00 30.95  ? 118 THR D CA  1 
ATOM   11389 C  C   . THR D  1 118 ? 32.757  107.503 38.800  1.00 35.27  ? 118 THR D C   1 
ATOM   11390 O  O   . THR D  1 118 ? 31.762  107.930 39.353  1.00 40.53  ? 118 THR D O   1 
ATOM   11391 C  CB  . THR D  1 118 ? 32.773  105.191 37.943  1.00 26.84  ? 118 THR D CB  1 
ATOM   11392 O  OG1 . THR D  1 118 ? 31.392  104.902 38.157  1.00 28.50  ? 118 THR D OG1 1 
ATOM   11393 C  CG2 . THR D  1 118 ? 33.591  103.887 37.984  1.00 21.14  ? 118 THR D CG2 1 
ATOM   11394 N  N   . PRO D  1 119 ? 33.545  108.284 38.060  1.00 36.99  ? 119 PRO D N   1 
ATOM   11395 C  CA  . PRO D  1 119 ? 33.148  109.657 37.807  1.00 37.82  ? 119 PRO D CA  1 
ATOM   11396 C  C   . PRO D  1 119 ? 32.162  109.745 36.665  1.00 40.76  ? 119 PRO D C   1 
ATOM   11397 O  O   . PRO D  1 119 ? 31.867  108.762 35.968  1.00 38.34  ? 119 PRO D O   1 
ATOM   11398 C  CB  . PRO D  1 119 ? 34.470  110.305 37.415  1.00 40.40  ? 119 PRO D CB  1 
ATOM   11399 C  CG  . PRO D  1 119 ? 35.078  109.260 36.572  1.00 37.17  ? 119 PRO D CG  1 
ATOM   11400 C  CD  . PRO D  1 119 ? 34.842  107.998 37.410  1.00 37.72  ? 119 PRO D CD  1 
ATOM   11401 N  N   . PRO D  1 120 ? 31.628  110.939 36.462  1.00 43.75  ? 120 PRO D N   1 
ATOM   11402 C  CA  . PRO D  1 120 ? 30.670  111.164 35.395  1.00 44.21  ? 120 PRO D CA  1 
ATOM   11403 C  C   . PRO D  1 120 ? 31.412  111.057 34.093  1.00 44.53  ? 120 PRO D C   1 
ATOM   11404 O  O   . PRO D  1 120 ? 32.653  111.160 34.042  1.00 45.94  ? 120 PRO D O   1 
ATOM   11405 C  CB  . PRO D  1 120 ? 30.254  112.617 35.628  1.00 46.30  ? 120 PRO D CB  1 
ATOM   11406 C  CG  . PRO D  1 120 ? 30.566  112.869 37.071  1.00 46.29  ? 120 PRO D CG  1 
ATOM   11407 C  CD  . PRO D  1 120 ? 31.859  112.173 37.232  1.00 44.63  ? 120 PRO D CD  1 
ATOM   11408 N  N   . GLN D  1 121 ? 30.659  110.874 33.031  1.00 44.21  ? 121 GLN D N   1 
ATOM   11409 C  CA  . GLN D  1 121 ? 31.282  110.802 31.732  1.00 50.31  ? 121 GLN D CA  1 
ATOM   11410 C  C   . GLN D  1 121 ? 31.881  112.169 31.485  1.00 48.68  ? 121 GLN D C   1 
ATOM   11411 O  O   . GLN D  1 121 ? 31.279  113.142 31.910  1.00 48.89  ? 121 GLN D O   1 
ATOM   11412 C  CB  . GLN D  1 121 ? 30.216  110.508 30.707  1.00 57.97  ? 121 GLN D CB  1 
ATOM   11413 C  CG  . GLN D  1 121 ? 30.726  110.455 29.306  1.00 68.85  ? 121 GLN D CG  1 
ATOM   11414 C  CD  . GLN D  1 121 ? 29.721  109.804 28.385  1.00 74.58  ? 121 GLN D CD  1 
ATOM   11415 O  OE1 . GLN D  1 121 ? 28.601  109.471 28.798  1.00 74.72  ? 121 GLN D OE1 1 
ATOM   11416 N  NE2 . GLN D  1 121 ? 30.122  109.587 27.135  1.00 82.53  ? 121 GLN D NE2 1 
ATOM   11417 N  N   . THR D  1 122 ? 33.035  112.260 30.818  1.00 50.74  ? 122 THR D N   1 
ATOM   11418 C  CA  . THR D  1 122 ? 33.632  113.585 30.572  1.00 53.21  ? 122 THR D CA  1 
ATOM   11419 C  C   . THR D  1 122 ? 32.665  114.525 29.856  1.00 55.49  ? 122 THR D C   1 
ATOM   11420 O  O   . THR D  1 122 ? 31.964  114.112 28.938  1.00 54.93  ? 122 THR D O   1 
ATOM   11421 C  CB  . THR D  1 122 ? 34.973  113.534 29.809  1.00 51.36  ? 122 THR D CB  1 
ATOM   11422 O  OG1 . THR D  1 122 ? 34.772  113.115 28.462  1.00 55.93  ? 122 THR D OG1 1 
ATOM   11423 C  CG2 . THR D  1 122 ? 35.883  112.559 30.472  1.00 60.70  ? 122 THR D CG2 1 
ATOM   11424 N  N   . GLY D  1 123 ? 32.605  115.782 30.293  1.00 58.13  ? 123 GLY D N   1 
ATOM   11425 C  CA  . GLY D  1 123 ? 31.692  116.725 29.680  1.00 54.04  ? 123 GLY D CA  1 
ATOM   11426 C  C   . GLY D  1 123 ? 32.080  118.151 29.962  1.00 52.09  ? 123 GLY D C   1 
ATOM   11427 O  O   . GLY D  1 123 ? 32.800  118.458 30.911  1.00 54.50  ? 123 GLY D O   1 
ATOM   11428 N  N   . LEU D  1 124 ? 31.472  119.034 29.192  1.00 53.06  ? 124 LEU D N   1 
ATOM   11429 C  CA  . LEU D  1 124 ? 31.732  120.469 29.238  1.00 47.58  ? 124 LEU D CA  1 
ATOM   11430 C  C   . LEU D  1 124 ? 31.358  121.137 30.544  1.00 45.80  ? 124 LEU D C   1 
ATOM   11431 O  O   . LEU D  1 124 ? 32.160  121.896 31.107  1.00 44.62  ? 124 LEU D O   1 
ATOM   11432 C  CB  . LEU D  1 124 ? 31.014  121.120 28.060  1.00 43.41  ? 124 LEU D CB  1 
ATOM   11433 C  CG  . LEU D  1 124 ? 31.544  122.408 27.468  1.00 45.34  ? 124 LEU D CG  1 
ATOM   11434 C  CD1 . LEU D  1 124 ? 33.068  122.480 27.484  1.00 47.27  ? 124 LEU D CD1 1 
ATOM   11435 C  CD2 . LEU D  1 124 ? 31.000  122.492 26.081  1.00 43.47  ? 124 LEU D CD2 1 
ATOM   11436 N  N   . ASP D  1 125 ? 30.169  120.817 31.052  1.00 46.30  ? 125 ASP D N   1 
ATOM   11437 C  CA  . ASP D  1 125 ? 29.675  121.420 32.301  1.00 47.20  ? 125 ASP D CA  1 
ATOM   11438 C  C   . ASP D  1 125 ? 29.589  120.441 33.500  1.00 46.92  ? 125 ASP D C   1 
ATOM   11439 O  O   . ASP D  1 125 ? 28.863  120.662 34.464  1.00 48.00  ? 125 ASP D O   1 
ATOM   11440 C  CB  . ASP D  1 125 ? 28.307  122.088 32.052  1.00 48.13  ? 125 ASP D CB  1 
ATOM   11441 C  CG  . ASP D  1 125 ? 28.389  123.297 31.117  1.00 46.47  ? 125 ASP D CG  1 
ATOM   11442 O  OD1 . ASP D  1 125 ? 29.145  124.248 31.405  1.00 48.56  ? 125 ASP D OD1 1 
ATOM   11443 O  OD2 . ASP D  1 125 ? 27.674  123.301 30.096  1.00 46.64  ? 125 ASP D OD2 1 
ATOM   11444 N  N   . VAL D  1 126 ? 30.345  119.360 33.432  1.00 46.65  ? 126 VAL D N   1 
ATOM   11445 C  CA  . VAL D  1 126 ? 30.341  118.378 34.490  1.00 39.22  ? 126 VAL D CA  1 
ATOM   11446 C  C   . VAL D  1 126 ? 31.200  118.918 35.616  1.00 35.11  ? 126 VAL D C   1 
ATOM   11447 O  O   . VAL D  1 126 ? 32.402  119.150 35.455  1.00 36.76  ? 126 VAL D O   1 
ATOM   11448 C  CB  . VAL D  1 126 ? 30.942  117.055 34.010  1.00 40.28  ? 126 VAL D CB  1 
ATOM   11449 C  CG1 . VAL D  1 126 ? 30.897  116.034 35.110  1.00 45.86  ? 126 VAL D CG1 1 
ATOM   11450 C  CG2 . VAL D  1 126 ? 30.218  116.556 32.799  1.00 37.52  ? 126 VAL D CG2 1 
ATOM   11451 N  N   . PRO D  1 127 ? 30.592  119.135 36.767  1.00 29.43  ? 127 PRO D N   1 
ATOM   11452 C  CA  . PRO D  1 127 ? 31.306  119.648 37.927  1.00 30.23  ? 127 PRO D CA  1 
ATOM   11453 C  C   . PRO D  1 127 ? 32.018  118.511 38.611  1.00 33.16  ? 127 PRO D C   1 
ATOM   11454 O  O   . PRO D  1 127 ? 31.578  117.356 38.533  1.00 37.05  ? 127 PRO D O   1 
ATOM   11455 C  CB  . PRO D  1 127 ? 30.186  120.159 38.799  1.00 32.95  ? 127 PRO D CB  1 
ATOM   11456 C  CG  . PRO D  1 127 ? 29.080  119.146 38.532  1.00 27.95  ? 127 PRO D CG  1 
ATOM   11457 C  CD  . PRO D  1 127 ? 29.167  118.910 37.051  1.00 27.53  ? 127 PRO D CD  1 
ATOM   11458 N  N   . TYR D  1 128 ? 33.061  118.830 39.358  1.00 32.66  ? 128 TYR D N   1 
ATOM   11459 C  CA  . TYR D  1 128 ? 33.801  117.795 40.050  1.00 32.95  ? 128 TYR D CA  1 
ATOM   11460 C  C   . TYR D  1 128 ? 34.684  118.547 41.017  1.00 34.84  ? 128 TYR D C   1 
ATOM   11461 O  O   . TYR D  1 128 ? 35.077  119.688 40.750  1.00 38.74  ? 128 TYR D O   1 
ATOM   11462 C  CB  . TYR D  1 128 ? 34.651  117.005 39.023  1.00 33.53  ? 128 TYR D CB  1 
ATOM   11463 C  CG  . TYR D  1 128 ? 35.041  115.594 39.450  1.00 34.59  ? 128 TYR D CG  1 
ATOM   11464 C  CD1 . TYR D  1 128 ? 34.106  114.555 39.400  1.00 31.48  ? 128 TYR D CD1 1 
ATOM   11465 C  CD2 . TYR D  1 128 ? 36.315  115.322 39.996  1.00 35.92  ? 128 TYR D CD2 1 
ATOM   11466 C  CE1 . TYR D  1 128 ? 34.403  113.305 39.885  1.00 28.95  ? 128 TYR D CE1 1 
ATOM   11467 C  CE2 . TYR D  1 128 ? 36.614  114.058 40.487  1.00 32.71  ? 128 TYR D CE2 1 
ATOM   11468 C  CZ  . TYR D  1 128 ? 35.644  113.066 40.427  1.00 32.05  ? 128 TYR D CZ  1 
ATOM   11469 O  OH  . TYR D  1 128 ? 35.891  111.831 40.931  1.00 38.59  ? 128 TYR D OH  1 
ATOM   11470 N  N   . THR D  1 129 ? 34.998  117.944 42.146  1.00 32.73  ? 129 THR D N   1 
ATOM   11471 C  CA  . THR D  1 129 ? 35.855  118.645 43.067  1.00 33.22  ? 129 THR D CA  1 
ATOM   11472 C  C   . THR D  1 129 ? 37.138  117.885 43.397  1.00 31.36  ? 129 THR D C   1 
ATOM   11473 O  O   . THR D  1 129 ? 37.098  116.753 43.829  1.00 33.57  ? 129 THR D O   1 
ATOM   11474 C  CB  . THR D  1 129 ? 35.059  119.095 44.299  1.00 32.83  ? 129 THR D CB  1 
ATOM   11475 O  OG1 . THR D  1 129 ? 35.838  118.898 45.464  1.00 40.86  ? 129 THR D OG1 1 
ATOM   11476 C  CG2 . THR D  1 129 ? 33.743  118.351 44.428  1.00 33.86  ? 129 THR D CG2 1 
ATOM   11477 N  N   . PHE D  1 130 ? 38.271  118.492 43.092  1.00 28.08  ? 130 PHE D N   1 
ATOM   11478 C  CA  . PHE D  1 130 ? 39.545  117.857 43.341  1.00 30.28  ? 130 PHE D CA  1 
ATOM   11479 C  C   . PHE D  1 130 ? 40.176  118.337 44.611  1.00 31.76  ? 130 PHE D C   1 
ATOM   11480 O  O   . PHE D  1 130 ? 40.022  119.486 44.966  1.00 42.87  ? 130 PHE D O   1 
ATOM   11481 C  CB  . PHE D  1 130 ? 40.499  118.178 42.198  1.00 28.57  ? 130 PHE D CB  1 
ATOM   11482 C  CG  . PHE D  1 130 ? 40.073  117.608 40.893  1.00 27.51  ? 130 PHE D CG  1 
ATOM   11483 C  CD1 . PHE D  1 130 ? 40.385  116.317 40.552  1.00 21.41  ? 130 PHE D CD1 1 
ATOM   11484 C  CD2 . PHE D  1 130 ? 39.303  118.346 40.036  1.00 30.24  ? 130 PHE D CD2 1 
ATOM   11485 C  CE1 . PHE D  1 130 ? 39.934  115.779 39.392  1.00 21.37  ? 130 PHE D CE1 1 
ATOM   11486 C  CE2 . PHE D  1 130 ? 38.846  117.800 38.861  1.00 28.03  ? 130 PHE D CE2 1 
ATOM   11487 C  CZ  . PHE D  1 130 ? 39.159  116.517 38.540  1.00 23.10  ? 130 PHE D CZ  1 
ATOM   11488 N  N   . GLY D  1 131 ? 40.860  117.466 45.330  1.00 30.66  ? 131 GLY D N   1 
ATOM   11489 C  CA  . GLY D  1 131 ? 41.552  117.906 46.520  1.00 28.52  ? 131 GLY D CA  1 
ATOM   11490 C  C   . GLY D  1 131 ? 42.995  118.152 46.090  1.00 29.54  ? 131 GLY D C   1 
ATOM   11491 O  O   . GLY D  1 131 ? 43.475  117.497 45.158  1.00 28.67  ? 131 GLY D O   1 
ATOM   11492 N  N   . LEU D  1 132 ? 43.690  119.091 46.736  1.00 27.54  ? 132 LEU D N   1 
ATOM   11493 C  CA  . LEU D  1 132 ? 45.067  119.366 46.415  1.00 26.77  ? 132 LEU D CA  1 
ATOM   11494 C  C   . LEU D  1 132 ? 45.933  119.141 47.603  1.00 29.49  ? 132 LEU D C   1 
ATOM   11495 O  O   . LEU D  1 132 ? 45.745  119.751 48.639  1.00 35.04  ? 132 LEU D O   1 
ATOM   11496 C  CB  . LEU D  1 132 ? 45.222  120.771 45.900  1.00 26.02  ? 132 LEU D CB  1 
ATOM   11497 C  CG  . LEU D  1 132 ? 45.048  120.592 44.391  1.00 29.06  ? 132 LEU D CG  1 
ATOM   11498 C  CD1 . LEU D  1 132 ? 43.700  121.048 43.877  1.00 20.74  ? 132 LEU D CD1 1 
ATOM   11499 C  CD2 . LEU D  1 132 ? 46.181  121.279 43.684  1.00 27.16  ? 132 LEU D CD2 1 
ATOM   11500 N  N   . ILE D  1 133 ? 46.796  118.148 47.501  1.00 31.05  ? 133 ILE D N   1 
ATOM   11501 C  CA  . ILE D  1 133 ? 47.705  117.809 48.589  1.00 27.00  ? 133 ILE D CA  1 
ATOM   11502 C  C   . ILE D  1 133 ? 49.069  117.646 47.956  1.00 27.21  ? 133 ILE D C   1 
ATOM   11503 O  O   . ILE D  1 133 ? 49.206  117.140 46.840  1.00 25.93  ? 133 ILE D O   1 
ATOM   11504 C  CB  . ILE D  1 133 ? 47.302  116.513 49.271  1.00 19.96  ? 133 ILE D CB  1 
ATOM   11505 C  CG1 . ILE D  1 133 ? 45.841  116.614 49.709  1.00 24.68  ? 133 ILE D CG1 1 
ATOM   11506 C  CG2 . ILE D  1 133 ? 48.159  116.280 50.456  1.00 23.38  ? 133 ILE D CG2 1 
ATOM   11507 C  CD1 . ILE D  1 133 ? 45.384  115.571 50.670  1.00 19.29  ? 133 ILE D CD1 1 
ATOM   11508 N  N   . GLY D  1 134 ? 50.072  118.178 48.602  1.00 26.04  ? 134 GLY D N   1 
ATOM   11509 C  CA  . GLY D  1 134 ? 51.372  118.062 48.027  1.00 25.55  ? 134 GLY D CA  1 
ATOM   11510 C  C   . GLY D  1 134 ? 52.272  117.992 49.219  1.00 27.04  ? 134 GLY D C   1 
ATOM   11511 O  O   . GLY D  1 134 ? 51.890  118.430 50.300  1.00 25.53  ? 134 GLY D O   1 
ATOM   11512 N  N   . ASP D  1 135 ? 53.345  117.232 49.083  1.00 27.26  ? 135 ASP D N   1 
ATOM   11513 C  CA  . ASP D  1 135 ? 54.309  117.154 50.134  1.00 29.32  ? 135 ASP D CA  1 
ATOM   11514 C  C   . ASP D  1 135 ? 53.815  116.660 51.520  1.00 32.32  ? 135 ASP D C   1 
ATOM   11515 O  O   . ASP D  1 135 ? 54.299  117.106 52.552  1.00 41.03  ? 135 ASP D O   1 
ATOM   11516 C  CB  . ASP D  1 135 ? 54.828  118.558 50.183  1.00 32.87  ? 135 ASP D CB  1 
ATOM   11517 C  CG  . ASP D  1 135 ? 55.976  118.759 49.275  1.00 30.22  ? 135 ASP D CG  1 
ATOM   11518 O  OD1 . ASP D  1 135 ? 56.957  118.401 49.877  1.00 27.37  ? 135 ASP D OD1 1 
ATOM   11519 O  OD2 . ASP D  1 135 ? 55.874  119.266 48.133  1.00 16.15  ? 135 ASP D OD2 1 
ATOM   11520 N  N   . LEU D  1 136 ? 52.968  115.632 51.524  1.00 34.12  ? 136 LEU D N   1 
ATOM   11521 C  CA  . LEU D  1 136 ? 52.344  115.068 52.734  1.00 29.44  ? 136 LEU D CA  1 
ATOM   11522 C  C   . LEU D  1 136 ? 53.274  114.544 53.829  1.00 35.29  ? 136 LEU D C   1 
ATOM   11523 O  O   . LEU D  1 136 ? 53.293  115.078 54.947  1.00 38.96  ? 136 LEU D O   1 
ATOM   11524 C  CB  . LEU D  1 136 ? 51.335  113.985 52.327  1.00 27.22  ? 136 LEU D CB  1 
ATOM   11525 C  CG  . LEU D  1 136 ? 50.428  113.455 53.426  1.00 22.32  ? 136 LEU D CG  1 
ATOM   11526 C  CD1 . LEU D  1 136 ? 49.609  114.573 53.905  1.00 19.12  ? 136 LEU D CD1 1 
ATOM   11527 C  CD2 . LEU D  1 136 ? 49.519  112.350 52.912  1.00 24.52  ? 136 LEU D CD2 1 
ATOM   11528 N  N   . GLY D  1 137 ? 54.035  113.500 53.524  1.00 37.85  ? 137 GLY D N   1 
ATOM   11529 C  CA  . GLY D  1 137 ? 54.931  112.940 54.522  1.00 37.80  ? 137 GLY D CA  1 
ATOM   11530 C  C   . GLY D  1 137 ? 54.160  112.240 55.631  1.00 36.28  ? 137 GLY D C   1 
ATOM   11531 O  O   . GLY D  1 137 ? 52.980  111.853 55.438  1.00 33.07  ? 137 GLY D O   1 
ATOM   11532 N  N   . GLN D  1 138 ? 54.820  112.014 56.771  1.00 36.39  ? 138 GLN D N   1 
ATOM   11533 C  CA  . GLN D  1 138 ? 54.134  111.349 57.869  1.00 37.94  ? 138 GLN D CA  1 
ATOM   11534 C  C   . GLN D  1 138 ? 54.348  111.932 59.280  1.00 40.08  ? 138 GLN D C   1 
ATOM   11535 O  O   . GLN D  1 138 ? 54.513  111.190 60.253  1.00 39.99  ? 138 GLN D O   1 
ATOM   11536 C  CB  . GLN D  1 138 ? 54.380  109.833 57.828  1.00 39.06  ? 138 GLN D CB  1 
ATOM   11537 C  CG  . GLN D  1 138 ? 55.838  109.407 57.874  1.00 40.48  ? 138 GLN D CG  1 
ATOM   11538 C  CD  . GLN D  1 138 ? 56.049  107.946 57.510  1.00 39.76  ? 138 GLN D CD  1 
ATOM   11539 O  OE1 . GLN D  1 138 ? 56.281  107.622 56.362  1.00 43.45  ? 138 GLN D OE1 1 
ATOM   11540 N  NE2 . GLN D  1 138 ? 55.972  107.066 58.485  1.00 40.84  ? 138 GLN D NE2 1 
ATOM   11541 N  N   . SER D  1 139 ? 54.375  113.263 59.376  1.00 38.50  ? 139 SER D N   1 
ATOM   11542 C  CA  . SER D  1 139 ? 54.500  113.938 60.644  1.00 30.46  ? 139 SER D CA  1 
ATOM   11543 C  C   . SER D  1 139 ? 53.063  114.089 61.121  1.00 33.30  ? 139 SER D C   1 
ATOM   11544 O  O   . SER D  1 139 ? 52.101  113.825 60.375  1.00 33.92  ? 139 SER D O   1 
ATOM   11545 C  CB  . SER D  1 139 ? 55.125  115.285 60.438  1.00 28.50  ? 139 SER D CB  1 
ATOM   11546 O  OG  . SER D  1 139 ? 54.339  116.081 59.575  1.00 24.48  ? 139 SER D OG  1 
ATOM   11547 N  N   . PHE D  1 140 ? 52.893  114.526 62.358  1.00 36.43  ? 140 PHE D N   1 
ATOM   11548 C  CA  . PHE D  1 140 ? 51.542  114.650 62.910  1.00 40.66  ? 140 PHE D CA  1 
ATOM   11549 C  C   . PHE D  1 140 ? 50.756  115.584 62.087  1.00 42.37  ? 140 PHE D C   1 
ATOM   11550 O  O   . PHE D  1 140 ? 49.562  115.379 61.851  1.00 42.59  ? 140 PHE D O   1 
ATOM   11551 C  CB  . PHE D  1 140 ? 51.600  115.177 64.307  1.00 38.70  ? 140 PHE D CB  1 
ATOM   11552 C  CG  . PHE D  1 140 ? 52.281  114.263 65.227  1.00 41.71  ? 140 PHE D CG  1 
ATOM   11553 C  CD1 . PHE D  1 140 ? 51.557  113.260 65.861  1.00 42.74  ? 140 PHE D CD1 1 
ATOM   11554 C  CD2 . PHE D  1 140 ? 53.651  114.369 65.444  1.00 41.75  ? 140 PHE D CD2 1 
ATOM   11555 C  CE1 . PHE D  1 140 ? 52.181  112.379 66.697  1.00 45.85  ? 140 PHE D CE1 1 
ATOM   11556 C  CE2 . PHE D  1 140 ? 54.295  113.487 66.286  1.00 47.13  ? 140 PHE D CE2 1 
ATOM   11557 C  CZ  . PHE D  1 140 ? 53.563  112.489 66.917  1.00 46.01  ? 140 PHE D CZ  1 
ATOM   11558 N  N   . ASP D  1 141 ? 51.478  116.602 61.642  1.00 43.20  ? 141 ASP D N   1 
ATOM   11559 C  CA  . ASP D  1 141 ? 50.949  117.644 60.807  1.00 41.35  ? 141 ASP D CA  1 
ATOM   11560 C  C   . ASP D  1 141 ? 50.306  117.016 59.619  1.00 40.63  ? 141 ASP D C   1 
ATOM   11561 O  O   . ASP D  1 141 ? 49.175  117.336 59.292  1.00 42.42  ? 141 ASP D O   1 
ATOM   11562 C  CB  . ASP D  1 141 ? 52.088  118.535 60.390  1.00 48.39  ? 141 ASP D CB  1 
ATOM   11563 C  CG  . ASP D  1 141 ? 52.517  119.473 61.507  1.00 54.81  ? 141 ASP D CG  1 
ATOM   11564 O  OD1 . ASP D  1 141 ? 51.609  120.217 61.974  1.00 61.45  ? 141 ASP D OD1 1 
ATOM   11565 O  OD2 . ASP D  1 141 ? 53.727  119.467 61.901  1.00 53.37  ? 141 ASP D OD2 1 
ATOM   11566 N  N   . SER D  1 142 ? 50.982  116.039 59.038  1.00 36.73  ? 142 SER D N   1 
ATOM   11567 C  CA  . SER D  1 142 ? 50.444  115.359 57.889  1.00 26.67  ? 142 SER D CA  1 
ATOM   11568 C  C   . SER D  1 142 ? 49.133  114.718 58.303  1.00 23.61  ? 142 SER D C   1 
ATOM   11569 O  O   . SER D  1 142 ? 48.151  114.840 57.578  1.00 22.98  ? 142 SER D O   1 
ATOM   11570 C  CB  . SER D  1 142 ? 51.435  114.311 57.439  1.00 27.79  ? 142 SER D CB  1 
ATOM   11571 O  OG  . SER D  1 142 ? 52.764  114.797 57.592  1.00 24.00  ? 142 SER D OG  1 
ATOM   11572 N  N   . ASN D  1 143 ? 49.083  114.115 59.494  1.00 21.39  ? 143 ASN D N   1 
ATOM   11573 C  CA  . ASN D  1 143 ? 47.858  113.472 59.916  1.00 27.22  ? 143 ASN D CA  1 
ATOM   11574 C  C   . ASN D  1 143 ? 46.718  114.448 59.921  1.00 33.02  ? 143 ASN D C   1 
ATOM   11575 O  O   . ASN D  1 143 ? 45.633  114.184 59.427  1.00 35.83  ? 143 ASN D O   1 
ATOM   11576 C  CB  . ASN D  1 143 ? 47.969  112.859 61.290  1.00 28.50  ? 143 ASN D CB  1 
ATOM   11577 C  CG  . ASN D  1 143 ? 46.723  112.024 61.643  1.00 37.95  ? 143 ASN D CG  1 
ATOM   11578 O  OD1 . ASN D  1 143 ? 46.125  111.407 60.753  1.00 39.28  ? 143 ASN D OD1 1 
ATOM   11579 N  ND2 . ASN D  1 143 ? 46.343  111.970 62.926  1.00 43.17  ? 143 ASN D ND2 1 
ATOM   11580 N  N   . THR D  1 144 ? 47.002  115.618 60.451  1.00 41.85  ? 144 THR D N   1 
ATOM   11581 C  CA  . THR D  1 144 ? 46.023  116.676 60.525  1.00 43.97  ? 144 THR D CA  1 
ATOM   11582 C  C   . THR D  1 144 ? 45.504  117.088 59.156  1.00 43.17  ? 144 THR D C   1 
ATOM   11583 O  O   . THR D  1 144 ? 44.280  117.061 58.937  1.00 45.50  ? 144 THR D O   1 
ATOM   11584 C  CB  . THR D  1 144 ? 46.600  117.881 61.246  1.00 48.44  ? 144 THR D CB  1 
ATOM   11585 O  OG1 . THR D  1 144 ? 47.002  117.484 62.570  1.00 57.39  ? 144 THR D OG1 1 
ATOM   11586 C  CG2 . THR D  1 144 ? 45.559  118.992 61.328  1.00 53.63  ? 144 THR D CG2 1 
ATOM   11587 N  N   . THR D  1 145 ? 46.409  117.458 58.246  1.00 38.91  ? 145 THR D N   1 
ATOM   11588 C  CA  . THR D  1 145 ? 46.019  117.852 56.893  1.00 35.11  ? 145 THR D CA  1 
ATOM   11589 C  C   . THR D  1 145 ? 45.088  116.826 56.295  1.00 37.98  ? 145 THR D C   1 
ATOM   11590 O  O   . THR D  1 145 ? 43.984  117.172 55.853  1.00 40.81  ? 145 THR D O   1 
ATOM   11591 C  CB  . THR D  1 145 ? 47.208  117.967 55.998  1.00 30.32  ? 145 THR D CB  1 
ATOM   11592 O  OG1 . THR D  1 145 ? 48.167  118.760 56.673  1.00 28.61  ? 145 THR D OG1 1 
ATOM   11593 C  CG2 . THR D  1 145 ? 46.834  118.641 54.671  1.00 26.44  ? 145 THR D CG2 1 
ATOM   11594 N  N   . LEU D  1 146 ? 45.483  115.555 56.373  1.00 37.04  ? 146 LEU D N   1 
ATOM   11595 C  CA  . LEU D  1 146 ? 44.651  114.508 55.833  1.00 33.32  ? 146 LEU D CA  1 
ATOM   11596 C  C   . LEU D  1 146 ? 43.255  114.540 56.501  1.00 34.49  ? 146 LEU D C   1 
ATOM   11597 O  O   . LEU D  1 146 ? 42.258  114.386 55.815  1.00 36.50  ? 146 LEU D O   1 
ATOM   11598 C  CB  . LEU D  1 146 ? 45.344  113.170 55.964  1.00 26.87  ? 146 LEU D CB  1 
ATOM   11599 C  CG  . LEU D  1 146 ? 44.678  112.012 55.221  1.00 29.84  ? 146 LEU D CG  1 
ATOM   11600 C  CD1 . LEU D  1 146 ? 44.529  112.318 53.748  1.00 30.73  ? 146 LEU D CD1 1 
ATOM   11601 C  CD2 . LEU D  1 146 ? 45.510  110.750 55.407  1.00 26.86  ? 146 LEU D CD2 1 
ATOM   11602 N  N   . SER D  1 147 ? 43.160  114.828 57.797  1.00 32.59  ? 147 SER D N   1 
ATOM   11603 C  CA  . SER D  1 147 ? 41.846  114.896 58.443  1.00 36.24  ? 147 SER D CA  1 
ATOM   11604 C  C   . SER D  1 147 ? 41.024  116.074 57.904  1.00 38.98  ? 147 SER D C   1 
ATOM   11605 O  O   . SER D  1 147 ? 39.886  115.905 57.484  1.00 40.88  ? 147 SER D O   1 
ATOM   11606 C  CB  . SER D  1 147 ? 41.983  115.075 59.937  1.00 35.33  ? 147 SER D CB  1 
ATOM   11607 O  OG  . SER D  1 147 ? 43.167  114.464 60.414  1.00 40.79  ? 147 SER D OG  1 
ATOM   11608 N  N   . HIS D  1 148 ? 41.601  117.264 57.889  1.00 35.79  ? 148 HIS D N   1 
ATOM   11609 C  CA  . HIS D  1 148 ? 40.880  118.406 57.385  1.00 35.82  ? 148 HIS D CA  1 
ATOM   11610 C  C   . HIS D  1 148 ? 40.334  118.140 56.013  1.00 39.32  ? 148 HIS D C   1 
ATOM   11611 O  O   . HIS D  1 148 ? 39.247  118.579 55.673  1.00 38.65  ? 148 HIS D O   1 
ATOM   11612 C  CB  . HIS D  1 148 ? 41.793  119.581 57.270  1.00 45.37  ? 148 HIS D CB  1 
ATOM   11613 C  CG  . HIS D  1 148 ? 41.933  120.354 58.533  1.00 51.67  ? 148 HIS D CG  1 
ATOM   11614 N  ND1 . HIS D  1 148 ? 42.168  121.713 58.546  1.00 56.12  ? 148 HIS D ND1 1 
ATOM   11615 C  CD2 . HIS D  1 148 ? 41.938  119.957 59.824  1.00 56.25  ? 148 HIS D CD2 1 
ATOM   11616 C  CE1 . HIS D  1 148 ? 42.319  122.120 59.790  1.00 56.60  ? 148 HIS D CE1 1 
ATOM   11617 N  NE2 . HIS D  1 148 ? 42.184  121.072 60.587  1.00 63.67  ? 148 HIS D NE2 1 
ATOM   11618 N  N   . TYR D  1 149 ? 41.122  117.474 55.190  1.00 41.42  ? 149 TYR D N   1 
ATOM   11619 C  CA  . TYR D  1 149 ? 40.669  117.178 53.846  1.00 42.21  ? 149 TYR D CA  1 
ATOM   11620 C  C   . TYR D  1 149 ? 39.457  116.273 53.933  1.00 43.02  ? 149 TYR D C   1 
ATOM   11621 O  O   . TYR D  1 149 ? 38.467  116.500 53.226  1.00 42.85  ? 149 TYR D O   1 
ATOM   11622 C  CB  . TYR D  1 149 ? 41.751  116.478 53.012  1.00 43.10  ? 149 TYR D CB  1 
ATOM   11623 C  CG  . TYR D  1 149 ? 41.249  116.033 51.646  1.00 43.61  ? 149 TYR D CG  1 
ATOM   11624 C  CD1 . TYR D  1 149 ? 40.792  116.956 50.726  1.00 42.89  ? 149 TYR D CD1 1 
ATOM   11625 C  CD2 . TYR D  1 149 ? 41.155  114.685 51.309  1.00 45.77  ? 149 TYR D CD2 1 
ATOM   11626 C  CE1 . TYR D  1 149 ? 40.245  116.561 49.519  1.00 42.17  ? 149 TYR D CE1 1 
ATOM   11627 C  CE2 . TYR D  1 149 ? 40.600  114.281 50.092  1.00 45.72  ? 149 TYR D CE2 1 
ATOM   11628 C  CZ  . TYR D  1 149 ? 40.146  115.227 49.211  1.00 46.78  ? 149 TYR D CZ  1 
ATOM   11629 O  OH  . TYR D  1 149 ? 39.544  114.835 48.044  1.00 47.69  ? 149 TYR D OH  1 
ATOM   11630 N  N   . GLU D  1 150 ? 39.544  115.250 54.794  1.00 44.40  ? 150 GLU D N   1 
ATOM   11631 C  CA  . GLU D  1 150 ? 38.465  114.271 54.972  1.00 47.90  ? 150 GLU D CA  1 
ATOM   11632 C  C   . GLU D  1 150 ? 37.190  114.975 55.451  1.00 54.63  ? 150 GLU D C   1 
ATOM   11633 O  O   . GLU D  1 150 ? 36.046  114.538 55.192  1.00 53.15  ? 150 GLU D O   1 
ATOM   11634 C  CB  . GLU D  1 150 ? 38.843  113.222 56.026  1.00 49.60  ? 150 GLU D CB  1 
ATOM   11635 C  CG  . GLU D  1 150 ? 39.927  112.216 55.695  1.00 52.05  ? 150 GLU D CG  1 
ATOM   11636 C  CD  . GLU D  1 150 ? 40.244  111.349 56.891  1.00 54.09  ? 150 GLU D CD  1 
ATOM   11637 O  OE1 . GLU D  1 150 ? 40.814  111.865 57.876  1.00 58.32  ? 150 GLU D OE1 1 
ATOM   11638 O  OE2 . GLU D  1 150 ? 39.884  110.162 56.867  1.00 54.86  ? 150 GLU D OE2 1 
ATOM   11639 N  N   . LEU D  1 151 ? 37.390  116.057 56.190  1.00 58.27  ? 151 LEU D N   1 
ATOM   11640 C  CA  . LEU D  1 151 ? 36.266  116.771 56.725  1.00 57.14  ? 151 LEU D CA  1 
ATOM   11641 C  C   . LEU D  1 151 ? 35.771  117.927 55.885  1.00 57.55  ? 151 LEU D C   1 
ATOM   11642 O  O   . LEU D  1 151 ? 34.705  118.465 56.175  1.00 59.63  ? 151 LEU D O   1 
ATOM   11643 C  CB  . LEU D  1 151 ? 36.592  117.191 58.147  1.00 58.99  ? 151 LEU D CB  1 
ATOM   11644 C  CG  . LEU D  1 151 ? 36.986  115.960 58.970  1.00 58.97  ? 151 LEU D CG  1 
ATOM   11645 C  CD1 . LEU D  1 151 ? 37.523  116.346 60.335  1.00 61.91  ? 151 LEU D CD1 1 
ATOM   11646 C  CD2 . LEU D  1 151 ? 35.794  115.020 59.077  1.00 58.07  ? 151 LEU D CD2 1 
ATOM   11647 N  N   . SER D  1 152 ? 36.507  118.317 54.848  1.00 56.84  ? 152 SER D N   1 
ATOM   11648 C  CA  . SER D  1 152 ? 36.040  119.413 54.025  1.00 56.41  ? 152 SER D CA  1 
ATOM   11649 C  C   . SER D  1 152 ? 34.600  119.139 53.705  1.00 57.08  ? 152 SER D C   1 
ATOM   11650 O  O   . SER D  1 152 ? 34.243  118.031 53.337  1.00 49.94  ? 152 SER D O   1 
ATOM   11651 C  CB  . SER D  1 152 ? 36.846  119.575 52.737  1.00 59.53  ? 152 SER D CB  1 
ATOM   11652 O  OG  . SER D  1 152 ? 37.774  120.664 52.822  1.00 65.85  ? 152 SER D OG  1 
ATOM   11653 N  N   . PRO D  1 153 ? 33.732  120.086 54.082  1.00 64.41  ? 153 PRO D N   1 
ATOM   11654 C  CA  . PRO D  1 153 ? 32.274  120.097 53.897  1.00 67.07  ? 153 PRO D CA  1 
ATOM   11655 C  C   . PRO D  1 153 ? 31.942  119.951 52.418  1.00 70.37  ? 153 PRO D C   1 
ATOM   11656 O  O   . PRO D  1 153 ? 30.905  119.397 52.041  1.00 72.57  ? 153 PRO D O   1 
ATOM   11657 C  CB  . PRO D  1 153 ? 31.867  121.462 54.461  1.00 66.04  ? 153 PRO D CB  1 
ATOM   11658 C  CG  . PRO D  1 153 ? 33.165  122.260 54.509  1.00 66.69  ? 153 PRO D CG  1 
ATOM   11659 C  CD  . PRO D  1 153 ? 34.156  121.234 54.904  1.00 66.83  ? 153 PRO D CD  1 
ATOM   11660 N  N   . LYS D  1 154 ? 32.797  120.542 51.597  1.00 71.85  ? 154 LYS D N   1 
ATOM   11661 C  CA  . LYS D  1 154 ? 32.711  120.424 50.155  1.00 74.60  ? 154 LYS D CA  1 
ATOM   11662 C  C   . LYS D  1 154 ? 33.630  119.209 50.104  1.00 72.06  ? 154 LYS D C   1 
ATOM   11663 O  O   . LYS D  1 154 ? 34.813  119.325 50.425  1.00 76.15  ? 154 LYS D O   1 
ATOM   11664 C  CB  . LYS D  1 154 ? 33.363  121.660 49.505  1.00 80.35  ? 154 LYS D CB  1 
ATOM   11665 C  CG  . LYS D  1 154 ? 34.588  122.217 50.280  1.00 86.55  ? 154 LYS D CG  1 
ATOM   11666 C  CD  . LYS D  1 154 ? 34.852  123.724 50.042  1.00 96.41  ? 154 LYS D CD  1 
ATOM   11667 C  CE  . LYS D  1 154 ? 35.409  124.451 51.319  1.00 101.07 ? 154 LYS D CE  1 
ATOM   11668 N  NZ  . LYS D  1 154 ? 36.837  124.152 51.735  1.00 104.81 ? 154 LYS D NZ  1 
ATOM   11669 N  N   . LYS D  1 155 ? 33.076  118.027 49.890  1.00 68.60  ? 155 LYS D N   1 
ATOM   11670 C  CA  . LYS D  1 155 ? 33.925  116.846 49.896  1.00 70.43  ? 155 LYS D CA  1 
ATOM   11671 C  C   . LYS D  1 155 ? 34.709  116.632 48.618  1.00 64.18  ? 155 LYS D C   1 
ATOM   11672 O  O   . LYS D  1 155 ? 34.136  116.753 47.531  1.00 62.59  ? 155 LYS D O   1 
ATOM   11673 C  CB  . LYS D  1 155 ? 33.135  115.593 50.268  1.00 79.68  ? 155 LYS D CB  1 
ATOM   11674 C  CG  . LYS D  1 155 ? 31.656  115.657 49.943  1.00 92.08  ? 155 LYS D CG  1 
ATOM   11675 C  CD  . LYS D  1 155 ? 31.404  115.956 48.460  1.00 101.19 ? 155 LYS D CD  1 
ATOM   11676 C  CE  . LYS D  1 155 ? 29.899  116.020 48.127  1.00 109.19 ? 155 LYS D CE  1 
ATOM   11677 N  NZ  . LYS D  1 155 ? 29.138  117.041 48.940  1.00 112.37 ? 155 LYS D NZ  1 
ATOM   11678 N  N   . GLY D  1 156 ? 36.025  116.413 48.763  1.00 57.63  ? 156 GLY D N   1 
ATOM   11679 C  CA  . GLY D  1 156 ? 36.888  116.167 47.625  1.00 48.59  ? 156 GLY D CA  1 
ATOM   11680 C  C   . GLY D  1 156 ? 36.528  114.828 47.008  1.00 46.72  ? 156 GLY D C   1 
ATOM   11681 O  O   . GLY D  1 156 ? 36.088  113.921 47.711  1.00 48.21  ? 156 GLY D O   1 
ATOM   11682 N  N   . GLN D  1 157 ? 36.722  114.682 45.703  1.00 43.72  ? 157 GLN D N   1 
ATOM   11683 C  CA  . GLN D  1 157 ? 36.388  113.444 45.010  1.00 40.78  ? 157 GLN D CA  1 
ATOM   11684 C  C   . GLN D  1 157 ? 37.574  112.730 44.332  1.00 35.76  ? 157 GLN D C   1 
ATOM   11685 O  O   . GLN D  1 157 ? 37.404  111.669 43.752  1.00 37.46  ? 157 GLN D O   1 
ATOM   11686 C  CB  . GLN D  1 157 ? 35.321  113.729 43.970  1.00 47.98  ? 157 GLN D CB  1 
ATOM   11687 C  CG  . GLN D  1 157 ? 34.026  114.228 44.541  1.00 57.11  ? 157 GLN D CG  1 
ATOM   11688 C  CD  . GLN D  1 157 ? 33.034  114.621 43.475  1.00 60.28  ? 157 GLN D CD  1 
ATOM   11689 O  OE1 . GLN D  1 157 ? 32.143  113.853 43.144  1.00 71.01  ? 157 GLN D OE1 1 
ATOM   11690 N  NE2 . GLN D  1 157 ? 33.183  115.820 42.932  1.00 63.61  ? 157 GLN D NE2 1 
ATOM   11691 N  N   . THR D  1 158 ? 38.753  113.329 44.385  1.00 28.19  ? 158 THR D N   1 
ATOM   11692 C  CA  . THR D  1 158 ? 39.977  112.798 43.789  1.00 24.21  ? 158 THR D CA  1 
ATOM   11693 C  C   . THR D  1 158 ? 41.064  113.755 44.255  1.00 27.16  ? 158 THR D C   1 
ATOM   11694 O  O   . THR D  1 158 ? 40.863  114.967 44.211  1.00 31.70  ? 158 THR D O   1 
ATOM   11695 C  CB  . THR D  1 158 ? 39.945  112.878 42.259  1.00 23.67  ? 158 THR D CB  1 
ATOM   11696 O  OG1 . THR D  1 158 ? 38.995  111.942 41.750  1.00 19.41  ? 158 THR D OG1 1 
ATOM   11697 C  CG2 . THR D  1 158 ? 41.327  112.623 41.660  1.00 19.27  ? 158 THR D CG2 1 
ATOM   11698 N  N   . VAL D  1 159 ? 42.194  113.241 44.727  1.00 22.37  ? 159 VAL D N   1 
ATOM   11699 C  CA  . VAL D  1 159 ? 43.232  114.120 45.189  1.00 17.52  ? 159 VAL D CA  1 
ATOM   11700 C  C   . VAL D  1 159 ? 44.234  114.211 44.119  1.00 20.92  ? 159 VAL D C   1 
ATOM   11701 O  O   . VAL D  1 159 ? 44.545  113.218 43.478  1.00 29.58  ? 159 VAL D O   1 
ATOM   11702 C  CB  . VAL D  1 159 ? 43.927  113.558 46.409  1.00 16.63  ? 159 VAL D CB  1 
ATOM   11703 C  CG1 . VAL D  1 159 ? 45.147  114.358 46.761  1.00 17.42  ? 159 VAL D CG1 1 
ATOM   11704 C  CG2 . VAL D  1 159 ? 42.980  113.542 47.556  1.00 19.16  ? 159 VAL D CG2 1 
ATOM   11705 N  N   . LEU D  1 160 ? 44.668  115.410 43.821  1.00 23.50  ? 160 LEU D N   1 
ATOM   11706 C  CA  . LEU D  1 160 ? 45.724  115.515 42.845  1.00 28.93  ? 160 LEU D CA  1 
ATOM   11707 C  C   . LEU D  1 160 ? 46.982  115.663 43.753  1.00 31.60  ? 160 LEU D C   1 
ATOM   11708 O  O   . LEU D  1 160 ? 47.094  116.590 44.570  1.00 32.74  ? 160 LEU D O   1 
ATOM   11709 C  CB  . LEU D  1 160 ? 45.474  116.709 41.913  1.00 28.87  ? 160 LEU D CB  1 
ATOM   11710 C  CG  . LEU D  1 160 ? 44.107  116.697 41.201  1.00 23.24  ? 160 LEU D CG  1 
ATOM   11711 C  CD1 . LEU D  1 160 ? 43.904  117.964 40.447  1.00 25.03  ? 160 LEU D CD1 1 
ATOM   11712 C  CD2 . LEU D  1 160 ? 44.010  115.556 40.241  1.00 26.07  ? 160 LEU D CD2 1 
ATOM   11713 N  N   . PHE D  1 161 ? 47.844  114.662 43.739  1.00 27.87  ? 161 PHE D N   1 
ATOM   11714 C  CA  . PHE D  1 161 ? 49.028  114.699 44.571  1.00 24.48  ? 161 PHE D CA  1 
ATOM   11715 C  C   . PHE D  1 161 ? 50.201  115.268 43.823  1.00 23.88  ? 161 PHE D C   1 
ATOM   11716 O  O   . PHE D  1 161 ? 50.669  114.711 42.833  1.00 30.80  ? 161 PHE D O   1 
ATOM   11717 C  CB  . PHE D  1 161 ? 49.350  113.310 45.073  1.00 26.44  ? 161 PHE D CB  1 
ATOM   11718 C  CG  . PHE D  1 161 ? 50.290  113.293 46.198  1.00 22.52  ? 161 PHE D CG  1 
ATOM   11719 C  CD1 . PHE D  1 161 ? 51.660  113.276 45.964  1.00 25.71  ? 161 PHE D CD1 1 
ATOM   11720 C  CD2 . PHE D  1 161 ? 49.820  113.351 47.497  1.00 13.40  ? 161 PHE D CD2 1 
ATOM   11721 C  CE1 . PHE D  1 161 ? 52.568  113.330 47.016  1.00 21.52  ? 161 PHE D CE1 1 
ATOM   11722 C  CE2 . PHE D  1 161 ? 50.714  113.405 48.545  1.00 23.14  ? 161 PHE D CE2 1 
ATOM   11723 C  CZ  . PHE D  1 161 ? 52.101  113.396 48.306  1.00 23.72  ? 161 PHE D CZ  1 
ATOM   11724 N  N   . VAL D  1 162 ? 50.813  116.258 44.426  1.00 25.33  ? 162 VAL D N   1 
ATOM   11725 C  CA  . VAL D  1 162 ? 51.874  116.978 43.776  1.00 24.55  ? 162 VAL D CA  1 
ATOM   11726 C  C   . VAL D  1 162 ? 53.331  116.563 44.065  1.00 26.05  ? 162 VAL D C   1 
ATOM   11727 O  O   . VAL D  1 162 ? 54.281  117.282 43.749  1.00 26.84  ? 162 VAL D O   1 
ATOM   11728 C  CB  . VAL D  1 162 ? 51.492  118.456 43.985  1.00 26.82  ? 162 VAL D CB  1 
ATOM   11729 C  CG1 . VAL D  1 162 ? 52.583  119.302 44.520  1.00 31.50  ? 162 VAL D CG1 1 
ATOM   11730 C  CG2 . VAL D  1 162 ? 50.916  118.992 42.734  1.00 23.14  ? 162 VAL D CG2 1 
ATOM   11731 N  N   . GLY D  1 163 ? 53.536  115.361 44.586  1.00 25.73  ? 163 GLY D N   1 
ATOM   11732 C  CA  . GLY D  1 163 ? 54.916  114.975 44.821  1.00 28.63  ? 163 GLY D CA  1 
ATOM   11733 C  C   . GLY D  1 163 ? 55.385  114.911 46.260  1.00 32.30  ? 163 GLY D C   1 
ATOM   11734 O  O   . GLY D  1 163 ? 54.845  115.582 47.123  1.00 35.56  ? 163 GLY D O   1 
ATOM   11735 N  N   . ASP D  1 164 ? 56.473  114.167 46.472  1.00 30.42  ? 164 ASP D N   1 
ATOM   11736 C  CA  . ASP D  1 164 ? 57.067  113.918 47.799  1.00 23.43  ? 164 ASP D CA  1 
ATOM   11737 C  C   . ASP D  1 164 ? 56.028  113.224 48.657  1.00 25.43  ? 164 ASP D C   1 
ATOM   11738 O  O   . ASP D  1 164 ? 55.235  113.861 49.330  1.00 23.71  ? 164 ASP D O   1 
ATOM   11739 C  CB  . ASP D  1 164 ? 57.596  115.171 48.484  1.00 28.06  ? 164 ASP D CB  1 
ATOM   11740 C  CG  . ASP D  1 164 ? 58.855  115.751 47.790  1.00 28.17  ? 164 ASP D CG  1 
ATOM   11741 O  OD1 . ASP D  1 164 ? 59.297  115.292 46.728  1.00 28.36  ? 164 ASP D OD1 1 
ATOM   11742 O  OD2 . ASP D  1 164 ? 59.278  116.820 48.157  1.00 22.00  ? 164 ASP D OD2 1 
ATOM   11743 N  N   . LEU D  1 165 ? 55.979  111.897 48.519  1.00 30.48  ? 165 LEU D N   1 
ATOM   11744 C  CA  . LEU D  1 165 ? 55.021  111.081 49.224  1.00 28.21  ? 165 LEU D CA  1 
ATOM   11745 C  C   . LEU D  1 165 ? 55.333  110.784 50.651  1.00 27.13  ? 165 LEU D C   1 
ATOM   11746 O  O   . LEU D  1 165 ? 54.694  111.331 51.525  1.00 32.29  ? 165 LEU D O   1 
ATOM   11747 C  CB  . LEU D  1 165 ? 54.734  109.776 48.467  1.00 23.26  ? 165 LEU D CB  1 
ATOM   11748 C  CG  . LEU D  1 165 ? 54.000  109.916 47.136  1.00 20.39  ? 165 LEU D CG  1 
ATOM   11749 C  CD1 . LEU D  1 165 ? 54.904  110.465 46.093  1.00 15.74  ? 165 LEU D CD1 1 
ATOM   11750 C  CD2 . LEU D  1 165 ? 53.575  108.582 46.712  1.00 12.57  ? 165 LEU D CD2 1 
ATOM   11751 N  N   . SER D  1 166 ? 56.400  110.051 50.919  1.00 25.78  ? 166 SER D N   1 
ATOM   11752 C  CA  . SER D  1 166 ? 56.620  109.656 52.293  1.00 24.12  ? 166 SER D CA  1 
ATOM   11753 C  C   . SER D  1 166 ? 57.873  110.070 52.989  1.00 23.44  ? 166 SER D C   1 
ATOM   11754 O  O   . SER D  1 166 ? 58.025  109.780 54.144  1.00 27.76  ? 166 SER D O   1 
ATOM   11755 C  CB  . SER D  1 166 ? 56.602  108.168 52.335  1.00 17.14  ? 166 SER D CB  1 
ATOM   11756 O  OG  . SER D  1 166 ? 57.819  107.772 51.745  1.00 21.73  ? 166 SER D OG  1 
ATOM   11757 N  N   . TYR D  1 167 ? 58.850  110.587 52.280  1.00 25.42  ? 167 TYR D N   1 
ATOM   11758 C  CA  . TYR D  1 167 ? 60.058  110.998 52.976  1.00 21.23  ? 167 TYR D CA  1 
ATOM   11759 C  C   . TYR D  1 167 ? 60.825  109.894 53.651  1.00 24.88  ? 167 TYR D C   1 
ATOM   11760 O  O   . TYR D  1 167 ? 61.558  110.147 54.595  1.00 26.90  ? 167 TYR D O   1 
ATOM   11761 C  CB  . TYR D  1 167 ? 59.727  112.032 54.010  1.00 20.55  ? 167 TYR D CB  1 
ATOM   11762 C  CG  . TYR D  1 167 ? 59.373  113.295 53.348  1.00 24.86  ? 167 TYR D CG  1 
ATOM   11763 C  CD1 . TYR D  1 167 ? 58.069  113.521 52.903  1.00 23.27  ? 167 TYR D CD1 1 
ATOM   11764 C  CD2 . TYR D  1 167 ? 60.361  114.273 53.114  1.00 20.51  ? 167 TYR D CD2 1 
ATOM   11765 C  CE1 . TYR D  1 167 ? 57.759  114.714 52.241  1.00 29.51  ? 167 TYR D CE1 1 
ATOM   11766 C  CE2 . TYR D  1 167 ? 60.075  115.444 52.463  1.00 16.93  ? 167 TYR D CE2 1 
ATOM   11767 C  CZ  . TYR D  1 167 ? 58.778  115.681 52.040  1.00 26.68  ? 167 TYR D CZ  1 
ATOM   11768 O  OH  . TYR D  1 167 ? 58.409  116.916 51.619  1.00 25.52  ? 167 TYR D OH  1 
ATOM   11769 N  N   . ALA D  1 168 ? 60.653  108.668 53.173  1.00 26.00  ? 168 ALA D N   1 
ATOM   11770 C  CA  . ALA D  1 168 ? 61.385  107.559 53.734  1.00 19.75  ? 168 ALA D CA  1 
ATOM   11771 C  C   . ALA D  1 168 ? 62.859  107.793 53.482  1.00 20.08  ? 168 ALA D C   1 
ATOM   11772 O  O   . ALA D  1 168 ? 63.674  107.414 54.279  1.00 25.64  ? 168 ALA D O   1 
ATOM   11773 C  CB  . ALA D  1 168 ? 60.948  106.273 53.108  1.00 16.83  ? 168 ALA D CB  1 
ATOM   11774 N  N   . ASP D  1 169 ? 63.224  108.480 52.414  1.00 20.09  ? 169 ASP D N   1 
ATOM   11775 C  CA  . ASP D  1 169 ? 64.634  108.677 52.144  1.00 22.95  ? 169 ASP D CA  1 
ATOM   11776 C  C   . ASP D  1 169 ? 65.351  109.541 53.163  1.00 28.82  ? 169 ASP D C   1 
ATOM   11777 O  O   . ASP D  1 169 ? 66.560  109.768 53.069  1.00 34.09  ? 169 ASP D O   1 
ATOM   11778 C  CB  . ASP D  1 169 ? 64.818  109.249 50.758  1.00 24.49  ? 169 ASP D CB  1 
ATOM   11779 C  CG  . ASP D  1 169 ? 64.125  110.568 50.593  1.00 29.44  ? 169 ASP D CG  1 
ATOM   11780 O  OD1 . ASP D  1 169 ? 63.073  110.765 51.222  1.00 37.09  ? 169 ASP D OD1 1 
ATOM   11781 O  OD2 . ASP D  1 169 ? 64.623  111.415 49.836  1.00 35.78  ? 169 ASP D OD2 1 
ATOM   11782 N  N   . ARG D  1 170 ? 64.626  110.048 54.142  1.00 35.44  ? 170 ARG D N   1 
ATOM   11783 C  CA  . ARG D  1 170 ? 65.263  110.868 55.176  1.00 40.30  ? 170 ARG D CA  1 
ATOM   11784 C  C   . ARG D  1 170 ? 65.829  109.910 56.195  1.00 40.26  ? 170 ARG D C   1 
ATOM   11785 O  O   . ARG D  1 170 ? 66.762  110.243 56.935  1.00 44.58  ? 170 ARG D O   1 
ATOM   11786 C  CB  . ARG D  1 170 ? 64.250  111.770 55.856  1.00 39.03  ? 170 ARG D CB  1 
ATOM   11787 C  CG  . ARG D  1 170 ? 63.458  112.563 54.878  1.00 53.65  ? 170 ARG D CG  1 
ATOM   11788 C  CD  . ARG D  1 170 ? 62.659  113.604 55.575  1.00 62.50  ? 170 ARG D CD  1 
ATOM   11789 N  NE  . ARG D  1 170 ? 63.572  114.498 56.261  1.00 66.37  ? 170 ARG D NE  1 
ATOM   11790 C  CZ  . ARG D  1 170 ? 63.695  114.524 57.575  1.00 67.02  ? 170 ARG D CZ  1 
ATOM   11791 N  NH1 . ARG D  1 170 ? 62.936  113.691 58.317  1.00 61.86  ? 170 ARG D NH1 1 
ATOM   11792 N  NH2 . ARG D  1 170 ? 64.607  115.334 58.125  1.00 67.13  ? 170 ARG D NH2 1 
ATOM   11793 N  N   . TYR D  1 171 ? 65.229  108.729 56.257  1.00 36.57  ? 171 TYR D N   1 
ATOM   11794 C  CA  . TYR D  1 171 ? 65.676  107.715 57.166  1.00 32.59  ? 171 TYR D CA  1 
ATOM   11795 C  C   . TYR D  1 171 ? 66.944  107.081 56.637  1.00 37.31  ? 171 TYR D C   1 
ATOM   11796 O  O   . TYR D  1 171 ? 67.277  107.173 55.453  1.00 42.85  ? 171 TYR D O   1 
ATOM   11797 C  CB  . TYR D  1 171 ? 64.596  106.706 57.336  1.00 31.24  ? 171 TYR D CB  1 
ATOM   11798 C  CG  . TYR D  1 171 ? 63.439  107.308 58.054  1.00 33.88  ? 171 TYR D CG  1 
ATOM   11799 C  CD1 . TYR D  1 171 ? 62.428  107.977 57.374  1.00 35.57  ? 171 TYR D CD1 1 
ATOM   11800 C  CD2 . TYR D  1 171 ? 63.369  107.238 59.427  1.00 36.19  ? 171 TYR D CD2 1 
ATOM   11801 C  CE1 . TYR D  1 171 ? 61.383  108.569 58.056  1.00 40.87  ? 171 TYR D CE1 1 
ATOM   11802 C  CE2 . TYR D  1 171 ? 62.336  107.818 60.122  1.00 42.04  ? 171 TYR D CE2 1 
ATOM   11803 C  CZ  . TYR D  1 171 ? 61.347  108.487 59.436  1.00 43.26  ? 171 TYR D CZ  1 
ATOM   11804 O  OH  . TYR D  1 171 ? 60.342  109.090 60.157  1.00 46.62  ? 171 TYR D OH  1 
ATOM   11805 N  N   . PRO D  1 172 ? 67.731  106.490 57.522  1.00 35.06  ? 172 PRO D N   1 
ATOM   11806 C  CA  . PRO D  1 172 ? 68.969  105.863 57.064  1.00 35.05  ? 172 PRO D CA  1 
ATOM   11807 C  C   . PRO D  1 172 ? 68.707  104.696 56.107  1.00 34.67  ? 172 PRO D C   1 
ATOM   11808 O  O   . PRO D  1 172 ? 67.757  103.934 56.266  1.00 39.35  ? 172 PRO D O   1 
ATOM   11809 C  CB  . PRO D  1 172 ? 69.633  105.457 58.369  1.00 34.48  ? 172 PRO D CB  1 
ATOM   11810 C  CG  . PRO D  1 172 ? 68.479  105.231 59.275  1.00 30.84  ? 172 PRO D CG  1 
ATOM   11811 C  CD  . PRO D  1 172 ? 67.522  106.305 58.961  1.00 30.41  ? 172 PRO D CD  1 
ATOM   11812 N  N   . ASN D  1 173 ? 69.517  104.602 55.063  1.00 36.07  ? 173 ASN D N   1 
ATOM   11813 C  CA  . ASN D  1 173 ? 69.347  103.552 54.051  1.00 31.71  ? 173 ASN D CA  1 
ATOM   11814 C  C   . ASN D  1 173 ? 67.931  103.601 53.507  1.00 29.40  ? 173 ASN D C   1 
ATOM   11815 O  O   . ASN D  1 173 ? 67.372  102.575 53.093  1.00 30.66  ? 173 ASN D O   1 
ATOM   11816 C  CB  . ASN D  1 173 ? 69.609  102.164 54.619  1.00 36.73  ? 173 ASN D CB  1 
ATOM   11817 C  CG  . ASN D  1 173 ? 70.981  102.023 55.269  1.00 39.59  ? 173 ASN D CG  1 
ATOM   11818 O  OD1 . ASN D  1 173 ? 71.096  101.359 56.282  1.00 39.55  ? 173 ASN D OD1 1 
ATOM   11819 N  ND2 . ASN D  1 173 ? 72.017  102.622 54.684  1.00 41.45  ? 173 ASN D ND2 1 
ATOM   11820 N  N   . HIS D  1 174 ? 67.350  104.804 53.551  1.00 27.03  ? 174 HIS D N   1 
ATOM   11821 C  CA  . HIS D  1 174 ? 65.989  105.074 53.080  1.00 24.29  ? 174 HIS D CA  1 
ATOM   11822 C  C   . HIS D  1 174 ? 64.976  104.111 53.659  1.00 25.28  ? 174 HIS D C   1 
ATOM   11823 O  O   . HIS D  1 174 ? 63.930  103.890 53.038  1.00 29.57  ? 174 HIS D O   1 
ATOM   11824 C  CB  . HIS D  1 174 ? 65.911  104.995 51.554  1.00 22.98  ? 174 HIS D CB  1 
ATOM   11825 C  CG  . HIS D  1 174 ? 66.839  105.917 50.847  1.00 22.44  ? 174 HIS D CG  1 
ATOM   11826 N  ND1 . HIS D  1 174 ? 66.548  106.458 49.621  1.00 26.04  ? 174 HIS D ND1 1 
ATOM   11827 C  CD2 . HIS D  1 174 ? 68.075  106.355 51.172  1.00 20.52  ? 174 HIS D CD2 1 
ATOM   11828 C  CE1 . HIS D  1 174 ? 67.575  107.194 49.208  1.00 26.23  ? 174 HIS D CE1 1 
ATOM   11829 N  NE2 . HIS D  1 174 ? 68.517  107.139 50.131  1.00 19.50  ? 174 HIS D NE2 1 
ATOM   11830 N  N   . ASP D  1 175 ? 65.273  103.578 54.846  1.00 24.15  ? 175 ASP D N   1 
ATOM   11831 C  CA  . ASP D  1 175 ? 64.434  102.602 55.530  1.00 25.03  ? 175 ASP D CA  1 
ATOM   11832 C  C   . ASP D  1 175 ? 63.068  102.449 54.892  1.00 26.48  ? 175 ASP D C   1 
ATOM   11833 O  O   . ASP D  1 175 ? 62.105  103.092 55.337  1.00 24.82  ? 175 ASP D O   1 
ATOM   11834 C  CB  . ASP D  1 175 ? 64.265  102.980 56.976  1.00 22.41  ? 175 ASP D CB  1 
ATOM   11835 C  CG  . ASP D  1 175 ? 63.724  101.851 57.791  1.00 33.18  ? 175 ASP D CG  1 
ATOM   11836 O  OD1 . ASP D  1 175 ? 63.246  100.867 57.191  1.00 40.53  ? 175 ASP D OD1 1 
ATOM   11837 O  OD2 . ASP D  1 175 ? 63.783  101.932 59.039  1.00 39.69  ? 175 ASP D OD2 1 
ATOM   11838 N  N   . ASN D  1 176 ? 62.964  101.564 53.893  1.00 26.69  ? 176 ASN D N   1 
ATOM   11839 C  CA  . ASN D  1 176 ? 61.689  101.420 53.197  1.00 25.69  ? 176 ASN D CA  1 
ATOM   11840 C  C   . ASN D  1 176 ? 60.509  101.067 54.067  1.00 25.91  ? 176 ASN D C   1 
ATOM   11841 O  O   . ASN D  1 176 ? 59.380  100.995 53.570  1.00 28.87  ? 176 ASN D O   1 
ATOM   11842 C  CB  . ASN D  1 176 ? 61.776  100.466 52.017  1.00 26.93  ? 176 ASN D CB  1 
ATOM   11843 C  CG  . ASN D  1 176 ? 62.364  101.102 50.813  1.00 26.21  ? 176 ASN D CG  1 
ATOM   11844 O  OD1 . ASN D  1 176 ? 62.010  100.775 49.695  1.00 30.85  ? 176 ASN D OD1 1 
ATOM   11845 N  ND2 . ASN D  1 176 ? 63.283  102.017 51.023  1.00 25.96  ? 176 ASN D ND2 1 
ATOM   11846 N  N   . VAL D  1 177 ? 60.726  100.866 55.364  1.00 22.98  ? 177 VAL D N   1 
ATOM   11847 C  CA  . VAL D  1 177 ? 59.576  100.552 56.220  1.00 27.40  ? 177 VAL D CA  1 
ATOM   11848 C  C   . VAL D  1 177 ? 58.677  101.740 56.241  1.00 28.74  ? 177 VAL D C   1 
ATOM   11849 O  O   . VAL D  1 177 ? 57.439  101.607 56.244  1.00 28.72  ? 177 VAL D O   1 
ATOM   11850 C  CB  . VAL D  1 177 ? 59.934  100.254 57.652  1.00 24.77  ? 177 VAL D CB  1 
ATOM   11851 C  CG1 . VAL D  1 177 ? 58.682  100.266 58.498  1.00 32.36  ? 177 VAL D CG1 1 
ATOM   11852 C  CG2 . VAL D  1 177 ? 60.520  98.899  57.753  1.00 25.55  ? 177 VAL D CG2 1 
ATOM   11853 N  N   . ARG D  1 178 ? 59.330  102.895 56.178  1.00 28.65  ? 178 ARG D N   1 
ATOM   11854 C  CA  . ARG D  1 178 ? 58.642  104.157 56.174  1.00 31.19  ? 178 ARG D CA  1 
ATOM   11855 C  C   . ARG D  1 178 ? 57.754  104.314 54.947  1.00 30.85  ? 178 ARG D C   1 
ATOM   11856 O  O   . ARG D  1 178 ? 56.829  105.111 54.950  1.00 31.04  ? 178 ARG D O   1 
ATOM   11857 C  CB  . ARG D  1 178 ? 59.634  105.298 56.363  1.00 34.28  ? 178 ARG D CB  1 
ATOM   11858 C  CG  . ARG D  1 178 ? 60.069  105.496 57.850  1.00 35.03  ? 178 ARG D CG  1 
ATOM   11859 C  CD  . ARG D  1 178 ? 58.879  105.810 58.785  1.00 33.42  ? 178 ARG D CD  1 
ATOM   11860 N  NE  . ARG D  1 178 ? 59.306  106.105 60.153  1.00 33.00  ? 178 ARG D NE  1 
ATOM   11861 C  CZ  . ARG D  1 178 ? 58.501  106.576 61.116  1.00 34.97  ? 178 ARG D CZ  1 
ATOM   11862 N  NH1 . ARG D  1 178 ? 57.216  106.819 60.899  1.00 27.08  ? 178 ARG D NH1 1 
ATOM   11863 N  NH2 . ARG D  1 178 ? 58.998  106.855 62.307  1.00 40.54  ? 178 ARG D NH2 1 
ATOM   11864 N  N   . TRP D  1 179 ? 57.971  103.479 53.936  1.00 27.79  ? 179 TRP D N   1 
ATOM   11865 C  CA  . TRP D  1 179 ? 57.105  103.518 52.779  1.00 23.15  ? 179 TRP D CA  1 
ATOM   11866 C  C   . TRP D  1 179 ? 55.913  102.680 53.159  1.00 26.76  ? 179 TRP D C   1 
ATOM   11867 O  O   . TRP D  1 179 ? 54.795  102.961 52.740  1.00 36.51  ? 179 TRP D O   1 
ATOM   11868 C  CB  . TRP D  1 179 ? 57.751  102.878 51.579  1.00 19.84  ? 179 TRP D CB  1 
ATOM   11869 C  CG  . TRP D  1 179 ? 58.438  103.832 50.684  1.00 18.35  ? 179 TRP D CG  1 
ATOM   11870 C  CD1 . TRP D  1 179 ? 59.790  103.966 50.495  1.00 13.60  ? 179 TRP D CD1 1 
ATOM   11871 C  CD2 . TRP D  1 179 ? 57.812  104.773 49.805  1.00 20.95  ? 179 TRP D CD2 1 
ATOM   11872 N  NE1 . TRP D  1 179 ? 60.042  104.914 49.556  1.00 15.71  ? 179 TRP D NE1 1 
ATOM   11873 C  CE2 . TRP D  1 179 ? 58.853  105.449 49.115  1.00 20.79  ? 179 TRP D CE2 1 
ATOM   11874 C  CE3 . TRP D  1 179 ? 56.464  105.125 49.542  1.00 17.31  ? 179 TRP D CE3 1 
ATOM   11875 C  CZ2 . TRP D  1 179 ? 58.571  106.476 48.159  1.00 17.03  ? 179 TRP D CZ2 1 
ATOM   11876 C  CZ3 . TRP D  1 179 ? 56.194  106.154 48.594  1.00 16.85  ? 179 TRP D CZ3 1 
ATOM   11877 C  CH2 . TRP D  1 179 ? 57.238  106.810 47.922  1.00 7.58   ? 179 TRP D CH2 1 
ATOM   11878 N  N   . ASP D  1 180 ? 56.154  101.621 53.922  1.00 23.79  ? 180 ASP D N   1 
ATOM   11879 C  CA  . ASP D  1 180 ? 55.077  100.757 54.336  1.00 24.58  ? 180 ASP D CA  1 
ATOM   11880 C  C   . ASP D  1 180 ? 54.117  101.505 55.292  1.00 26.70  ? 180 ASP D C   1 
ATOM   11881 O  O   . ASP D  1 180 ? 52.885  101.431 55.143  1.00 28.55  ? 180 ASP D O   1 
ATOM   11882 C  CB  . ASP D  1 180 ? 55.645  99.510  55.020  1.00 24.42  ? 180 ASP D CB  1 
ATOM   11883 C  CG  . ASP D  1 180 ? 56.327  98.544  54.056  1.00 28.72  ? 180 ASP D CG  1 
ATOM   11884 O  OD1 . ASP D  1 180 ? 55.844  98.289  52.925  1.00 23.04  ? 180 ASP D OD1 1 
ATOM   11885 O  OD2 . ASP D  1 180 ? 57.361  98.005  54.473  1.00 36.28  ? 180 ASP D OD2 1 
ATOM   11886 N  N   . THR D  1 181 ? 54.663  102.229 56.267  1.00 23.53  ? 181 THR D N   1 
ATOM   11887 C  CA  . THR D  1 181 ? 53.825  102.931 57.204  1.00 19.27  ? 181 THR D CA  1 
ATOM   11888 C  C   . THR D  1 181 ? 53.018  103.984 56.468  1.00 21.89  ? 181 THR D C   1 
ATOM   11889 O  O   . THR D  1 181 ? 51.803  104.046 56.626  1.00 22.85  ? 181 THR D O   1 
ATOM   11890 C  CB  . THR D  1 181 ? 54.638  103.582 58.296  1.00 22.44  ? 181 THR D CB  1 
ATOM   11891 O  OG1 . THR D  1 181 ? 55.619  104.429 57.707  1.00 33.03  ? 181 THR D OG1 1 
ATOM   11892 C  CG2 . THR D  1 181 ? 55.371  102.557 59.064  1.00 26.18  ? 181 THR D CG2 1 
ATOM   11893 N  N   . TRP D  1 182 ? 53.664  104.733 55.579  1.00 18.43  ? 182 TRP D N   1 
ATOM   11894 C  CA  . TRP D  1 182 ? 52.969  105.766 54.857  1.00 18.02  ? 182 TRP D CA  1 
ATOM   11895 C  C   . TRP D  1 182 ? 51.801  105.186 54.127  1.00 17.81  ? 182 TRP D C   1 
ATOM   11896 O  O   . TRP D  1 182 ? 50.708  105.721 54.133  1.00 20.62  ? 182 TRP D O   1 
ATOM   11897 C  CB  . TRP D  1 182 ? 53.869  106.415 53.825  1.00 25.57  ? 182 TRP D CB  1 
ATOM   11898 C  CG  . TRP D  1 182 ? 53.288  107.720 53.284  1.00 31.62  ? 182 TRP D CG  1 
ATOM   11899 C  CD1 . TRP D  1 182 ? 53.317  108.933 53.891  1.00 36.21  ? 182 TRP D CD1 1 
ATOM   11900 C  CD2 . TRP D  1 182 ? 52.637  107.936 52.021  1.00 34.14  ? 182 TRP D CD2 1 
ATOM   11901 N  NE1 . TRP D  1 182 ? 52.743  109.894 53.094  1.00 36.74  ? 182 TRP D NE1 1 
ATOM   11902 C  CE2 . TRP D  1 182 ? 52.316  109.306 51.937  1.00 37.65  ? 182 TRP D CE2 1 
ATOM   11903 C  CE3 . TRP D  1 182 ? 52.312  107.113 50.947  1.00 36.83  ? 182 TRP D CE3 1 
ATOM   11904 C  CZ2 . TRP D  1 182 ? 51.690  109.860 50.825  1.00 34.43  ? 182 TRP D CZ2 1 
ATOM   11905 C  CZ3 . TRP D  1 182 ? 51.693  107.668 49.847  1.00 34.31  ? 182 TRP D CZ3 1 
ATOM   11906 C  CH2 . TRP D  1 182 ? 51.392  109.026 49.797  1.00 34.80  ? 182 TRP D CH2 1 
ATOM   11907 N  N   . GLY D  1 183 ? 52.035  104.047 53.521  1.00 18.86  ? 183 GLY D N   1 
ATOM   11908 C  CA  . GLY D  1 183 ? 50.990  103.433 52.743  1.00 25.06  ? 183 GLY D CA  1 
ATOM   11909 C  C   . GLY D  1 183 ? 49.806  103.022 53.565  1.00 29.60  ? 183 GLY D C   1 
ATOM   11910 O  O   . GLY D  1 183 ? 48.688  102.944 53.054  1.00 39.38  ? 183 GLY D O   1 
ATOM   11911 N  N   . ARG D  1 184 ? 50.060  102.698 54.824  1.00 35.13  ? 184 ARG D N   1 
ATOM   11912 C  CA  . ARG D  1 184 ? 49.019  102.241 55.736  1.00 36.16  ? 184 ARG D CA  1 
ATOM   11913 C  C   . ARG D  1 184 ? 48.333  103.486 56.259  1.00 34.10  ? 184 ARG D C   1 
ATOM   11914 O  O   . ARG D  1 184 ? 47.127  103.527 56.441  1.00 38.17  ? 184 ARG D O   1 
ATOM   11915 C  CB  . ARG D  1 184 ? 49.656  101.454 56.891  1.00 33.69  ? 184 ARG D CB  1 
ATOM   11916 C  CG  . ARG D  1 184 ? 49.704  99.932  56.747  1.00 32.46  ? 184 ARG D CG  1 
ATOM   11917 C  CD  . ARG D  1 184 ? 50.280  99.253  58.010  1.00 21.81  ? 184 ARG D CD  1 
ATOM   11918 N  NE  . ARG D  1 184 ? 51.556  98.602  57.705  1.00 27.46  ? 184 ARG D NE  1 
ATOM   11919 C  CZ  . ARG D  1 184 ? 52.661  98.686  58.454  1.00 24.55  ? 184 ARG D CZ  1 
ATOM   11920 N  NH1 . ARG D  1 184 ? 52.627  99.399  59.558  1.00 19.45  ? 184 ARG D NH1 1 
ATOM   11921 N  NH2 . ARG D  1 184 ? 53.795  98.040  58.120  1.00 33.63  ? 184 ARG D NH2 1 
ATOM   11922 N  N   . PHE D  1 185 ? 49.113  104.533 56.416  1.00 31.81  ? 185 PHE D N   1 
ATOM   11923 C  CA  . PHE D  1 185 ? 48.596  105.782 56.931  1.00 30.67  ? 185 PHE D CA  1 
ATOM   11924 C  C   . PHE D  1 185 ? 47.537  106.379 56.025  1.00 30.23  ? 185 PHE D C   1 
ATOM   11925 O  O   . PHE D  1 185 ? 46.433  106.687 56.466  1.00 40.14  ? 185 PHE D O   1 
ATOM   11926 C  CB  . PHE D  1 185 ? 49.786  106.716 57.132  1.00 30.17  ? 185 PHE D CB  1 
ATOM   11927 C  CG  . PHE D  1 185 ? 49.448  108.153 57.146  1.00 27.39  ? 185 PHE D CG  1 
ATOM   11928 C  CD1 . PHE D  1 185 ? 48.311  108.614 57.762  1.00 30.39  ? 185 PHE D CD1 1 
ATOM   11929 C  CD2 . PHE D  1 185 ? 50.310  109.070 56.561  1.00 33.36  ? 185 PHE D CD2 1 
ATOM   11930 C  CE1 . PHE D  1 185 ? 48.040  109.965 57.801  1.00 30.49  ? 185 PHE D CE1 1 
ATOM   11931 C  CE2 . PHE D  1 185 ? 50.054  110.430 56.592  1.00 27.61  ? 185 PHE D CE2 1 
ATOM   11932 C  CZ  . PHE D  1 185 ? 48.916  110.871 57.216  1.00 29.57  ? 185 PHE D CZ  1 
ATOM   11933 N  N   . THR D  1 186 ? 47.878  106.528 54.761  1.00 27.41  ? 186 THR D N   1 
ATOM   11934 C  CA  . THR D  1 186 ? 47.007  107.116 53.760  1.00 26.54  ? 186 THR D CA  1 
ATOM   11935 C  C   . THR D  1 186 ? 45.823  106.251 53.276  1.00 30.14  ? 186 THR D C   1 
ATOM   11936 O  O   . THR D  1 186 ? 44.857  106.767 52.699  1.00 30.45  ? 186 THR D O   1 
ATOM   11937 C  CB  . THR D  1 186 ? 47.871  107.573 52.532  1.00 20.95  ? 186 THR D CB  1 
ATOM   11938 O  OG1 . THR D  1 186 ? 48.716  106.500 52.105  1.00 28.15  ? 186 THR D OG1 1 
ATOM   11939 C  CG2 . THR D  1 186 ? 48.827  108.698 52.901  1.00 28.27  ? 186 THR D CG2 1 
ATOM   11940 N  N   . GLU D  1 187 ? 45.883  104.944 53.509  1.00 34.96  ? 187 GLU D N   1 
ATOM   11941 C  CA  . GLU D  1 187 ? 44.843  104.007 53.047  1.00 36.24  ? 187 GLU D CA  1 
ATOM   11942 C  C   . GLU D  1 187 ? 43.443  104.485 53.271  1.00 38.59  ? 187 GLU D C   1 
ATOM   11943 O  O   . GLU D  1 187 ? 42.576  104.261 52.433  1.00 40.91  ? 187 GLU D O   1 
ATOM   11944 C  CB  . GLU D  1 187 ? 44.972  102.634 53.717  1.00 40.50  ? 187 GLU D CB  1 
ATOM   11945 C  CG  . GLU D  1 187 ? 44.145  101.469 53.106  1.00 49.95  ? 187 GLU D CG  1 
ATOM   11946 C  CD  . GLU D  1 187 ? 44.158  100.200 53.987  1.00 52.95  ? 187 GLU D CD  1 
ATOM   11947 O  OE1 . GLU D  1 187 ? 43.334  100.164 54.920  1.00 55.42  ? 187 GLU D OE1 1 
ATOM   11948 O  OE2 . GLU D  1 187 ? 44.983  99.261  53.784  1.00 53.93  ? 187 GLU D OE2 1 
ATOM   11949 N  N   . ARG D  1 188 ? 43.225  105.173 54.383  1.00 42.39  ? 188 ARG D N   1 
ATOM   11950 C  CA  . ARG D  1 188 ? 41.882  105.623 54.716  1.00 41.78  ? 188 ARG D CA  1 
ATOM   11951 C  C   . ARG D  1 188 ? 41.304  106.536 53.666  1.00 39.31  ? 188 ARG D C   1 
ATOM   11952 O  O   . ARG D  1 188 ? 40.079  106.669 53.567  1.00 37.55  ? 188 ARG D O   1 
ATOM   11953 C  CB  . ARG D  1 188 ? 41.838  106.274 56.103  1.00 46.84  ? 188 ARG D CB  1 
ATOM   11954 C  CG  . ARG D  1 188 ? 42.522  107.643 56.245  1.00 47.91  ? 188 ARG D CG  1 
ATOM   11955 C  CD  . ARG D  1 188 ? 42.765  107.937 57.709  1.00 46.51  ? 188 ARG D CD  1 
ATOM   11956 N  NE  . ARG D  1 188 ? 42.667  109.349 58.044  1.00 41.37  ? 188 ARG D NE  1 
ATOM   11957 C  CZ  . ARG D  1 188 ? 43.549  109.970 58.816  1.00 45.63  ? 188 ARG D CZ  1 
ATOM   11958 N  NH1 . ARG D  1 188 ? 44.583  109.310 59.321  1.00 47.66  ? 188 ARG D NH1 1 
ATOM   11959 N  NH2 . ARG D  1 188 ? 43.413  111.255 59.074  1.00 46.93  ? 188 ARG D NH2 1 
ATOM   11960 N  N   . SER D  1 189 ? 42.175  107.173 52.889  1.00 34.91  ? 189 SER D N   1 
ATOM   11961 C  CA  . SER D  1 189 ? 41.679  108.047 51.863  1.00 35.19  ? 189 SER D CA  1 
ATOM   11962 C  C   . SER D  1 189 ? 41.744  107.328 50.535  1.00 36.52  ? 189 SER D C   1 
ATOM   11963 O  O   . SER D  1 189 ? 40.698  107.028 49.923  1.00 36.40  ? 189 SER D O   1 
ATOM   11964 C  CB  . SER D  1 189 ? 42.505  109.321 51.810  1.00 36.27  ? 189 SER D CB  1 
ATOM   11965 O  OG  . SER D  1 189 ? 41.880  110.252 50.961  1.00 40.29  ? 189 SER D OG  1 
ATOM   11966 N  N   . VAL D  1 190 ? 42.967  106.986 50.132  1.00 31.67  ? 190 VAL D N   1 
ATOM   11967 C  CA  . VAL D  1 190 ? 43.203  106.322 48.855  1.00 26.32  ? 190 VAL D CA  1 
ATOM   11968 C  C   . VAL D  1 190 ? 42.526  105.003 48.579  1.00 28.01  ? 190 VAL D C   1 
ATOM   11969 O  O   . VAL D  1 190 ? 42.489  104.562 47.436  1.00 31.15  ? 190 VAL D O   1 
ATOM   11970 C  CB  . VAL D  1 190 ? 44.639  106.025 48.598  1.00 22.28  ? 190 VAL D CB  1 
ATOM   11971 C  CG1 . VAL D  1 190 ? 45.056  106.693 47.374  1.00 24.32  ? 190 VAL D CG1 1 
ATOM   11972 C  CG2 . VAL D  1 190 ? 45.474  106.392 49.726  1.00 27.97  ? 190 VAL D CG2 1 
ATOM   11973 N  N   . ALA D  1 191 ? 42.103  104.288 49.594  1.00 25.06  ? 191 ALA D N   1 
ATOM   11974 C  CA  . ALA D  1 191 ? 41.457  103.045 49.289  1.00 27.33  ? 191 ALA D CA  1 
ATOM   11975 C  C   . ALA D  1 191 ? 40.068  103.341 48.734  1.00 26.88  ? 191 ALA D C   1 
ATOM   11976 O  O   . ALA D  1 191 ? 39.463  102.469 48.140  1.00 25.26  ? 191 ALA D O   1 
ATOM   11977 C  CB  . ALA D  1 191 ? 41.358  102.195 50.522  1.00 25.54  ? 191 ALA D CB  1 
ATOM   11978 N  N   . TYR D  1 192 ? 39.576  104.573 48.910  1.00 28.29  ? 192 TYR D N   1 
ATOM   11979 C  CA  . TYR D  1 192 ? 38.234  104.919 48.468  1.00 23.68  ? 192 TYR D CA  1 
ATOM   11980 C  C   . TYR D  1 192 ? 38.093  105.946 47.375  1.00 28.92  ? 192 TYR D C   1 
ATOM   11981 O  O   . TYR D  1 192 ? 37.026  106.030 46.737  1.00 30.81  ? 192 TYR D O   1 
ATOM   11982 C  CB  . TYR D  1 192 ? 37.437  105.385 49.614  1.00 22.70  ? 192 TYR D CB  1 
ATOM   11983 C  CG  . TYR D  1 192 ? 37.493  104.455 50.751  1.00 27.11  ? 192 TYR D CG  1 
ATOM   11984 C  CD1 . TYR D  1 192 ? 36.569  103.424 50.873  1.00 28.80  ? 192 TYR D CD1 1 
ATOM   11985 C  CD2 . TYR D  1 192 ? 38.460  104.612 51.740  1.00 35.61  ? 192 TYR D CD2 1 
ATOM   11986 C  CE1 . TYR D  1 192 ? 36.598  102.550 51.964  1.00 38.38  ? 192 TYR D CE1 1 
ATOM   11987 C  CE2 . TYR D  1 192 ? 38.513  103.753 52.844  1.00 44.28  ? 192 TYR D CE2 1 
ATOM   11988 C  CZ  . TYR D  1 192 ? 37.583  102.713 52.962  1.00 46.87  ? 192 TYR D CZ  1 
ATOM   11989 O  OH  . TYR D  1 192 ? 37.669  101.842 54.067  1.00 51.67  ? 192 TYR D OH  1 
ATOM   11990 N  N   . GLN D  1 193 ? 39.086  106.814 47.213  1.00 28.76  ? 193 GLN D N   1 
ATOM   11991 C  CA  . GLN D  1 193 ? 39.036  107.792 46.122  1.00 27.67  ? 193 GLN D CA  1 
ATOM   11992 C  C   . GLN D  1 193 ? 40.412  107.869 45.537  1.00 25.43  ? 193 GLN D C   1 
ATOM   11993 O  O   . GLN D  1 193 ? 41.401  107.901 46.250  1.00 34.97  ? 193 GLN D O   1 
ATOM   11994 C  CB  . GLN D  1 193 ? 38.571  109.169 46.588  1.00 36.69  ? 193 GLN D CB  1 
ATOM   11995 C  CG  . GLN D  1 193 ? 39.528  109.926 47.448  1.00 41.93  ? 193 GLN D CG  1 
ATOM   11996 C  CD  . GLN D  1 193 ? 39.099  111.360 47.641  1.00 45.76  ? 193 GLN D CD  1 
ATOM   11997 O  OE1 . GLN D  1 193 ? 39.618  112.266 46.987  1.00 46.52  ? 193 GLN D OE1 1 
ATOM   11998 N  NE2 . GLN D  1 193 ? 38.171  111.587 48.567  1.00 52.11  ? 193 GLN D NE2 1 
ATOM   11999 N  N   . PRO D  1 194 ? 40.505  107.876 44.224  1.00 20.29  ? 194 PRO D N   1 
ATOM   12000 C  CA  . PRO D  1 194 ? 41.798  107.927 43.553  1.00 19.78  ? 194 PRO D CA  1 
ATOM   12001 C  C   . PRO D  1 194 ? 42.636  109.070 43.881  1.00 19.24  ? 194 PRO D C   1 
ATOM   12002 O  O   . PRO D  1 194 ? 42.110  110.095 44.200  1.00 29.78  ? 194 PRO D O   1 
ATOM   12003 C  CB  . PRO D  1 194 ? 41.418  108.001 42.084  1.00 18.54  ? 194 PRO D CB  1 
ATOM   12004 C  CG  . PRO D  1 194 ? 40.079  108.614 42.122  1.00 16.88  ? 194 PRO D CG  1 
ATOM   12005 C  CD  . PRO D  1 194 ? 39.421  107.889 43.245  1.00 19.97  ? 194 PRO D CD  1 
ATOM   12006 N  N   . TRP D  1 195 ? 43.940  108.868 43.892  1.00 18.89  ? 195 TRP D N   1 
ATOM   12007 C  CA  . TRP D  1 195 ? 44.859  109.981 44.097  1.00 21.14  ? 195 TRP D CA  1 
ATOM   12008 C  C   . TRP D  1 195 ? 45.685  109.981 42.803  1.00 26.90  ? 195 TRP D C   1 
ATOM   12009 O  O   . TRP D  1 195 ? 46.060  108.899 42.305  1.00 31.45  ? 195 TRP D O   1 
ATOM   12010 C  CB  . TRP D  1 195 ? 45.772  109.784 45.323  1.00 23.13  ? 195 TRP D CB  1 
ATOM   12011 C  CG  . TRP D  1 195 ? 45.138  110.055 46.728  1.00 26.18  ? 195 TRP D CG  1 
ATOM   12012 C  CD1 . TRP D  1 195 ? 43.848  109.818 47.117  1.00 23.62  ? 195 TRP D CD1 1 
ATOM   12013 C  CD2 . TRP D  1 195 ? 45.822  110.556 47.894  1.00 21.88  ? 195 TRP D CD2 1 
ATOM   12014 N  NE1 . TRP D  1 195 ? 43.687  110.126 48.451  1.00 23.15  ? 195 TRP D NE1 1 
ATOM   12015 C  CE2 . TRP D  1 195 ? 44.871  110.571 48.955  1.00 20.51  ? 195 TRP D CE2 1 
ATOM   12016 C  CE3 . TRP D  1 195 ? 47.141  110.976 48.146  1.00 23.27  ? 195 TRP D CE3 1 
ATOM   12017 C  CZ2 . TRP D  1 195 ? 45.201  110.987 50.257  1.00 18.13  ? 195 TRP D CZ2 1 
ATOM   12018 C  CZ3 . TRP D  1 195 ? 47.478  111.400 49.453  1.00 17.51  ? 195 TRP D CZ3 1 
ATOM   12019 C  CH2 . TRP D  1 195 ? 46.504  111.397 50.485  1.00 15.21  ? 195 TRP D CH2 1 
ATOM   12020 N  N   . ILE D  1 196 ? 45.869  111.147 42.185  1.00 22.95  ? 196 ILE D N   1 
ATOM   12021 C  CA  . ILE D  1 196 ? 46.659  111.186 40.969  1.00 21.53  ? 196 ILE D CA  1 
ATOM   12022 C  C   . ILE D  1 196 ? 48.086  111.468 41.382  1.00 25.05  ? 196 ILE D C   1 
ATOM   12023 O  O   . ILE D  1 196 ? 48.342  112.504 41.996  1.00 29.22  ? 196 ILE D O   1 
ATOM   12024 C  CB  . ILE D  1 196 ? 46.128  112.243 40.044  1.00 16.40  ? 196 ILE D CB  1 
ATOM   12025 C  CG1 . ILE D  1 196 ? 44.629  112.016 39.830  1.00 14.24  ? 196 ILE D CG1 1 
ATOM   12026 C  CG2 . ILE D  1 196 ? 46.834  112.181 38.703  1.00 22.77  ? 196 ILE D CG2 1 
ATOM   12027 C  CD1 . ILE D  1 196 ? 44.274  110.672 39.369  1.00 10.58  ? 196 ILE D CD1 1 
ATOM   12028 N  N   . TRP D  1 197 ? 49.018  110.585 41.010  1.00 25.12  ? 197 TRP D N   1 
ATOM   12029 C  CA  . TRP D  1 197 ? 50.429  110.698 41.427  1.00 24.28  ? 197 TRP D CA  1 
ATOM   12030 C  C   . TRP D  1 197 ? 51.365  111.521 40.578  1.00 24.88  ? 197 TRP D C   1 
ATOM   12031 O  O   . TRP D  1 197 ? 51.384  111.401 39.345  1.00 27.53  ? 197 TRP D O   1 
ATOM   12032 C  CB  . TRP D  1 197 ? 51.063  109.290 41.632  1.00 23.38  ? 197 TRP D CB  1 
ATOM   12033 C  CG  . TRP D  1 197 ? 50.268  108.425 42.570  1.00 26.55  ? 197 TRP D CG  1 
ATOM   12034 C  CD1 . TRP D  1 197 ? 49.454  107.364 42.236  1.00 26.07  ? 197 TRP D CD1 1 
ATOM   12035 C  CD2 . TRP D  1 197 ? 50.084  108.632 43.974  1.00 21.75  ? 197 TRP D CD2 1 
ATOM   12036 N  NE1 . TRP D  1 197 ? 48.765  106.916 43.352  1.00 21.93  ? 197 TRP D NE1 1 
ATOM   12037 C  CE2 . TRP D  1 197 ? 49.138  107.688 44.422  1.00 23.56  ? 197 TRP D CE2 1 
ATOM   12038 C  CE3 . TRP D  1 197 ? 50.607  109.541 44.887  1.00 21.33  ? 197 TRP D CE3 1 
ATOM   12039 C  CZ2 . TRP D  1 197 ? 48.717  107.638 45.733  1.00 24.40  ? 197 TRP D CZ2 1 
ATOM   12040 C  CZ3 . TRP D  1 197 ? 50.195  109.486 46.179  1.00 28.18  ? 197 TRP D CZ3 1 
ATOM   12041 C  CH2 . TRP D  1 197 ? 49.259  108.547 46.598  1.00 23.38  ? 197 TRP D CH2 1 
ATOM   12042 N  N   . THR D  1 198 ? 52.232  112.252 41.269  1.00 20.14  ? 198 THR D N   1 
ATOM   12043 C  CA  . THR D  1 198 ? 53.229  113.064 40.618  1.00 20.70  ? 198 THR D CA  1 
ATOM   12044 C  C   . THR D  1 198 ? 54.502  112.748 41.368  1.00 22.05  ? 198 THR D C   1 
ATOM   12045 O  O   . THR D  1 198 ? 54.488  112.692 42.579  1.00 21.88  ? 198 THR D O   1 
ATOM   12046 C  CB  . THR D  1 198 ? 52.959  114.524 40.762  1.00 18.03  ? 198 THR D CB  1 
ATOM   12047 O  OG1 . THR D  1 198 ? 51.657  114.827 40.266  1.00 20.52  ? 198 THR D OG1 1 
ATOM   12048 C  CG2 . THR D  1 198 ? 53.963  115.281 39.954  1.00 18.02  ? 198 THR D CG2 1 
ATOM   12049 N  N   . ALA D  1 199 ? 55.600  112.592 40.642  1.00 24.47  ? 199 ALA D N   1 
ATOM   12050 C  CA  . ALA D  1 199 ? 56.865  112.231 41.231  1.00 21.70  ? 199 ALA D CA  1 
ATOM   12051 C  C   . ALA D  1 199 ? 57.612  113.426 41.645  1.00 23.05  ? 199 ALA D C   1 
ATOM   12052 O  O   . ALA D  1 199 ? 57.864  114.308 40.817  1.00 26.64  ? 199 ALA D O   1 
ATOM   12053 C  CB  . ALA D  1 199 ? 57.697  111.456 40.242  1.00 23.25  ? 199 ALA D CB  1 
ATOM   12054 N  N   . GLY D  1 200 ? 58.099  113.370 42.879  1.00 23.71  ? 200 GLY D N   1 
ATOM   12055 C  CA  . GLY D  1 200 ? 58.880  114.455 43.455  1.00 29.11  ? 200 GLY D CA  1 
ATOM   12056 C  C   . GLY D  1 200 ? 60.313  114.046 43.738  1.00 28.38  ? 200 GLY D C   1 
ATOM   12057 O  O   . GLY D  1 200 ? 60.645  112.880 43.552  1.00 32.04  ? 200 GLY D O   1 
ATOM   12058 N  N   . ASN D  1 201 ? 61.129  114.949 44.274  1.00 19.93  ? 201 ASN D N   1 
ATOM   12059 C  CA  . ASN D  1 201 ? 62.508  114.596 44.487  1.00 25.38  ? 201 ASN D CA  1 
ATOM   12060 C  C   . ASN D  1 201 ? 62.678  113.591 45.556  1.00 26.85  ? 201 ASN D C   1 
ATOM   12061 O  O   . ASN D  1 201 ? 63.588  112.776 45.514  1.00 38.07  ? 201 ASN D O   1 
ATOM   12062 C  CB  . ASN D  1 201 ? 63.396  115.812 44.757  1.00 32.68  ? 201 ASN D CB  1 
ATOM   12063 C  CG  . ASN D  1 201 ? 62.808  116.733 45.745  1.00 32.91  ? 201 ASN D CG  1 
ATOM   12064 O  OD1 . ASN D  1 201 ? 61.585  116.969 45.738  1.00 30.05  ? 201 ASN D OD1 1 
ATOM   12065 N  ND2 . ASN D  1 201 ? 63.644  117.271 46.585  1.00 33.86  ? 201 ASN D ND2 1 
ATOM   12066 N  N   . HIS D  1 202 ? 61.787  113.572 46.516  1.00 27.98  ? 202 HIS D N   1 
ATOM   12067 C  CA  . HIS D  1 202 ? 61.962  112.572 47.540  1.00 27.16  ? 202 HIS D CA  1 
ATOM   12068 C  C   . HIS D  1 202 ? 61.712  111.162 47.036  1.00 24.23  ? 202 HIS D C   1 
ATOM   12069 O  O   . HIS D  1 202 ? 61.901  110.215 47.781  1.00 33.14  ? 202 HIS D O   1 
ATOM   12070 C  CB  . HIS D  1 202 ? 61.150  112.911 48.775  1.00 26.35  ? 202 HIS D CB  1 
ATOM   12071 C  CG  . HIS D  1 202 ? 61.782  113.976 49.609  1.00 28.62  ? 202 HIS D CG  1 
ATOM   12072 N  ND1 . HIS D  1 202 ? 62.707  113.702 50.592  1.00 27.94  ? 202 HIS D ND1 1 
ATOM   12073 C  CD2 . HIS D  1 202 ? 61.650  115.319 49.586  1.00 30.30  ? 202 HIS D CD2 1 
ATOM   12074 C  CE1 . HIS D  1 202 ? 63.111  114.828 51.141  1.00 24.64  ? 202 HIS D CE1 1 
ATOM   12075 N  NE2 . HIS D  1 202 ? 62.482  115.824 50.552  1.00 23.95  ? 202 HIS D NE2 1 
ATOM   12076 N  N   . GLU D  1 203 ? 61.221  111.051 45.808  1.00 16.67  ? 203 GLU D N   1 
ATOM   12077 C  CA  . GLU D  1 203 ? 60.967  109.785 45.158  1.00 15.77  ? 203 GLU D CA  1 
ATOM   12078 C  C   . GLU D  1 203 ? 62.120  109.284 44.298  1.00 16.84  ? 203 GLU D C   1 
ATOM   12079 O  O   . GLU D  1 203 ? 62.197  108.126 43.974  1.00 22.78  ? 203 GLU D O   1 
ATOM   12080 C  CB  . GLU D  1 203 ? 59.752  109.898 44.265  1.00 12.52  ? 203 GLU D CB  1 
ATOM   12081 C  CG  . GLU D  1 203 ? 58.475  109.731 45.016  1.00 24.01  ? 203 GLU D CG  1 
ATOM   12082 C  CD  . GLU D  1 203 ? 58.217  110.865 45.962  1.00 23.31  ? 203 GLU D CD  1 
ATOM   12083 O  OE1 . GLU D  1 203 ? 57.818  111.920 45.451  1.00 30.61  ? 203 GLU D OE1 1 
ATOM   12084 O  OE2 . GLU D  1 203 ? 58.373  110.698 47.197  1.00 36.00  ? 203 GLU D OE2 1 
ATOM   12085 N  N   . ILE D  1 204 ? 63.003  110.159 43.899  1.00 14.46  ? 204 ILE D N   1 
ATOM   12086 C  CA  . ILE D  1 204 ? 64.111  109.736 43.094  1.00 14.85  ? 204 ILE D CA  1 
ATOM   12087 C  C   . ILE D  1 204 ? 64.919  108.662 43.765  1.00 18.24  ? 204 ILE D C   1 
ATOM   12088 O  O   . ILE D  1 204 ? 65.292  107.710 43.129  1.00 20.39  ? 204 ILE D O   1 
ATOM   12089 C  CB  . ILE D  1 204 ? 65.075  110.854 42.858  1.00 13.14  ? 204 ILE D CB  1 
ATOM   12090 C  CG1 . ILE D  1 204 ? 64.357  111.981 42.138  1.00 17.82  ? 204 ILE D CG1 1 
ATOM   12091 C  CG2 . ILE D  1 204 ? 66.190  110.405 42.009  1.00 8.53   ? 204 ILE D CG2 1 
ATOM   12092 C  CD1 . ILE D  1 204 ? 65.220  113.198 42.041  1.00 19.70  ? 204 ILE D CD1 1 
ATOM   12093 N  N   . GLU D  1 205 ? 65.303  108.894 45.007  1.00 21.67  ? 205 GLU D N   1 
ATOM   12094 C  CA  . GLU D  1 205 ? 66.085  107.917 45.774  1.00 18.23  ? 205 GLU D CA  1 
ATOM   12095 C  C   . GLU D  1 205 ? 67.316  107.363 45.114  1.00 18.02  ? 205 GLU D C   1 
ATOM   12096 O  O   . GLU D  1 205 ? 67.466  106.152 44.981  1.00 22.25  ? 205 GLU D O   1 
ATOM   12097 C  CB  . GLU D  1 205 ? 65.214  106.791 46.234  1.00 6.89   ? 205 GLU D CB  1 
ATOM   12098 C  CG  . GLU D  1 205 ? 64.204  107.308 47.218  1.00 27.78  ? 205 GLU D CG  1 
ATOM   12099 C  CD  . GLU D  1 205 ? 63.421  106.221 47.955  1.00 32.49  ? 205 GLU D CD  1 
ATOM   12100 O  OE1 . GLU D  1 205 ? 63.987  105.653 48.912  1.00 26.99  ? 205 GLU D OE1 1 
ATOM   12101 O  OE2 . GLU D  1 205 ? 62.238  105.959 47.577  1.00 40.75  ? 205 GLU D OE2 1 
ATOM   12102 N  N   . PHE D  1 206 ? 68.170  108.256 44.650  1.00 14.78  ? 206 PHE D N   1 
ATOM   12103 C  CA  . PHE D  1 206 ? 69.402  107.877 44.006  1.00 16.74  ? 206 PHE D CA  1 
ATOM   12104 C  C   . PHE D  1 206 ? 70.428  107.719 45.134  1.00 21.81  ? 206 PHE D C   1 
ATOM   12105 O  O   . PHE D  1 206 ? 70.931  108.698 45.665  1.00 27.00  ? 206 PHE D O   1 
ATOM   12106 C  CB  . PHE D  1 206 ? 69.795  108.978 43.024  1.00 13.60  ? 206 PHE D CB  1 
ATOM   12107 C  CG  . PHE D  1 206 ? 71.099  108.771 42.371  1.00 16.82  ? 206 PHE D CG  1 
ATOM   12108 C  CD1 . PHE D  1 206 ? 71.240  107.797 41.424  1.00 25.17  ? 206 PHE D CD1 1 
ATOM   12109 C  CD2 . PHE D  1 206 ? 72.173  109.621 42.619  1.00 19.84  ? 206 PHE D CD2 1 
ATOM   12110 C  CE1 . PHE D  1 206 ? 72.444  107.660 40.707  1.00 31.43  ? 206 PHE D CE1 1 
ATOM   12111 C  CE2 . PHE D  1 206 ? 73.380  109.498 41.907  1.00 14.88  ? 206 PHE D CE2 1 
ATOM   12112 C  CZ  . PHE D  1 206 ? 73.517  108.529 40.959  1.00 25.10  ? 206 PHE D CZ  1 
ATOM   12113 N  N   . ALA D  1 207 ? 70.702  106.488 45.543  1.00 22.47  ? 207 ALA D N   1 
ATOM   12114 C  CA  . ALA D  1 207 ? 71.640  106.239 46.624  1.00 18.61  ? 207 ALA D CA  1 
ATOM   12115 C  C   . ALA D  1 207 ? 72.817  105.401 46.241  1.00 19.28  ? 207 ALA D C   1 
ATOM   12116 O  O   . ALA D  1 207 ? 72.917  104.241 46.605  1.00 24.74  ? 207 ALA D O   1 
ATOM   12117 C  CB  . ALA D  1 207 ? 70.925  105.597 47.795  1.00 13.81  ? 207 ALA D CB  1 
ATOM   12118 N  N   . PRO D  1 208 ? 73.757  105.976 45.537  1.00 18.95  ? 208 PRO D N   1 
ATOM   12119 C  CA  . PRO D  1 208 ? 74.959  105.267 45.117  1.00 25.89  ? 208 PRO D CA  1 
ATOM   12120 C  C   . PRO D  1 208 ? 75.666  104.578 46.288  1.00 30.05  ? 208 PRO D C   1 
ATOM   12121 O  O   . PRO D  1 208 ? 76.102  103.452 46.159  1.00 36.13  ? 208 PRO D O   1 
ATOM   12122 C  CB  . PRO D  1 208 ? 75.822  106.384 44.540  1.00 17.13  ? 208 PRO D CB  1 
ATOM   12123 C  CG  . PRO D  1 208 ? 74.869  107.212 43.902  1.00 23.98  ? 208 PRO D CG  1 
ATOM   12124 C  CD  . PRO D  1 208 ? 73.694  107.283 44.899  1.00 23.43  ? 208 PRO D CD  1 
ATOM   12125 N  N   . GLU D  1 209 ? 75.807  105.282 47.400  1.00 32.05  ? 209 GLU D N   1 
ATOM   12126 C  CA  . GLU D  1 209 ? 76.445  104.741 48.581  1.00 37.69  ? 209 GLU D CA  1 
ATOM   12127 C  C   . GLU D  1 209 ? 75.949  103.346 49.017  1.00 38.92  ? 209 GLU D C   1 
ATOM   12128 O  O   . GLU D  1 209 ? 76.709  102.557 49.573  1.00 43.94  ? 209 GLU D O   1 
ATOM   12129 C  CB  . GLU D  1 209 ? 76.241  105.680 49.754  1.00 44.88  ? 209 GLU D CB  1 
ATOM   12130 C  CG  . GLU D  1 209 ? 75.700  107.059 49.437  1.00 59.66  ? 209 GLU D CG  1 
ATOM   12131 C  CD  . GLU D  1 209 ? 74.183  107.100 49.236  1.00 68.56  ? 209 GLU D CD  1 
ATOM   12132 O  OE1 . GLU D  1 209 ? 73.390  106.821 50.170  1.00 76.93  ? 209 GLU D OE1 1 
ATOM   12133 O  OE2 . GLU D  1 209 ? 73.783  107.466 48.127  1.00 77.02  ? 209 GLU D OE2 1 
ATOM   12134 N  N   . ILE D  1 210 ? 74.662  103.077 48.873  1.00 33.80  ? 210 ILE D N   1 
ATOM   12135 C  CA  . ILE D  1 210 ? 74.147  101.798 49.255  1.00 29.70  ? 210 ILE D CA  1 
ATOM   12136 C  C   . ILE D  1 210 ? 73.833  101.028 48.020  1.00 30.60  ? 210 ILE D C   1 
ATOM   12137 O  O   . ILE D  1 210 ? 72.993  100.156 47.996  1.00 36.45  ? 210 ILE D O   1 
ATOM   12138 C  CB  . ILE D  1 210 ? 72.923  101.912 50.101  1.00 27.84  ? 210 ILE D CB  1 
ATOM   12139 C  CG1 . ILE D  1 210 ? 71.910  102.829 49.467  1.00 30.77  ? 210 ILE D CG1 1 
ATOM   12140 C  CG2 . ILE D  1 210 ? 73.289  102.438 51.388  1.00 27.92  ? 210 ILE D CG2 1 
ATOM   12141 C  CD1 . ILE D  1 210 ? 70.670  102.975 50.275  1.00 34.35  ? 210 ILE D CD1 1 
ATOM   12142 N  N   . ASN D  1 211 ? 74.445  101.440 46.945  1.00 30.54  ? 211 ASN D N   1 
ATOM   12143 C  CA  . ASN D  1 211 ? 74.286  100.756 45.711  1.00 34.39  ? 211 ASN D CA  1 
ATOM   12144 C  C   . ASN D  1 211 ? 72.933  100.690 45.109  1.00 32.03  ? 211 ASN D C   1 
ATOM   12145 O  O   . ASN D  1 211 ? 72.678  99.840  44.286  1.00 35.49  ? 211 ASN D O   1 
ATOM   12146 C  CB  . ASN D  1 211 ? 74.882  99.377  45.823  1.00 49.64  ? 211 ASN D CB  1 
ATOM   12147 C  CG  . ASN D  1 211 ? 76.376  99.407  45.688  1.00 75.23  ? 211 ASN D CG  1 
ATOM   12148 O  OD1 . ASN D  1 211 ? 76.875  99.515  44.547  1.00 83.68  ? 211 ASN D OD1 1 
ATOM   12149 N  ND2 . ASN D  1 211 ? 77.065  99.429  46.842  1.00 91.10  ? 211 ASN D ND2 1 
ATOM   12150 N  N   . GLU D  1 212 ? 72.066  101.606 45.481  1.00 30.42  ? 212 GLU D N   1 
ATOM   12151 C  CA  . GLU D  1 212 ? 70.740  101.683 44.893  1.00 28.02  ? 212 GLU D CA  1 
ATOM   12152 C  C   . GLU D  1 212 ? 70.834  102.864 43.947  1.00 32.36  ? 212 GLU D C   1 
ATOM   12153 O  O   . GLU D  1 212 ? 70.941  103.997 44.412  1.00 36.61  ? 212 GLU D O   1 
ATOM   12154 C  CB  . GLU D  1 212 ? 69.759  101.978 45.981  1.00 31.70  ? 212 GLU D CB  1 
ATOM   12155 C  CG  . GLU D  1 212 ? 69.468  100.774 46.743  1.00 35.95  ? 212 GLU D CG  1 
ATOM   12156 C  CD  . GLU D  1 212 ? 69.018  99.699  45.825  1.00 39.80  ? 212 GLU D CD  1 
ATOM   12157 O  OE1 . GLU D  1 212 ? 68.235  100.005 44.882  1.00 45.71  ? 212 GLU D OE1 1 
ATOM   12158 O  OE2 . GLU D  1 212 ? 69.477  98.560  46.018  1.00 44.96  ? 212 GLU D OE2 1 
ATOM   12159 N  N   . THR D  1 213 ? 70.869  102.619 42.634  1.00 31.61  ? 213 THR D N   1 
ATOM   12160 C  CA  . THR D  1 213 ? 71.039  103.705 41.686  1.00 25.85  ? 213 THR D CA  1 
ATOM   12161 C  C   . THR D  1 213 ? 70.038  103.797 40.571  1.00 28.38  ? 213 THR D C   1 
ATOM   12162 O  O   . THR D  1 213 ? 70.309  104.414 39.532  1.00 31.23  ? 213 THR D O   1 
ATOM   12163 C  CB  . THR D  1 213 ? 72.428  103.659 41.060  1.00 22.11  ? 213 THR D CB  1 
ATOM   12164 O  OG1 . THR D  1 213 ? 72.584  102.452 40.344  1.00 24.50  ? 213 THR D OG1 1 
ATOM   12165 C  CG2 . THR D  1 213 ? 73.472  103.653 42.089  1.00 22.53  ? 213 THR D CG2 1 
ATOM   12166 N  N   . GLU D  1 214 ? 68.897  103.163 40.746  1.00 29.66  ? 214 GLU D N   1 
ATOM   12167 C  CA  . GLU D  1 214 ? 67.872  103.232 39.720  1.00 32.74  ? 214 GLU D CA  1 
ATOM   12168 C  C   . GLU D  1 214 ? 66.843  104.192 40.304  1.00 28.58  ? 214 GLU D C   1 
ATOM   12169 O  O   . GLU D  1 214 ? 66.154  103.871 41.311  1.00 39.30  ? 214 GLU D O   1 
ATOM   12170 C  CB  . GLU D  1 214 ? 67.264  101.852 39.502  1.00 44.79  ? 214 GLU D CB  1 
ATOM   12171 C  CG  . GLU D  1 214 ? 66.286  101.708 38.301  1.00 66.36  ? 214 GLU D CG  1 
ATOM   12172 C  CD  . GLU D  1 214 ? 65.212  100.572 38.496  1.00 78.45  ? 214 GLU D CD  1 
ATOM   12173 O  OE1 . GLU D  1 214 ? 65.580  99.436  38.938  1.00 85.99  ? 214 GLU D OE1 1 
ATOM   12174 O  OE2 . GLU D  1 214 ? 63.998  100.829 38.212  1.00 85.34  ? 214 GLU D OE2 1 
ATOM   12175 N  N   . PRO D  1 215 ? 66.757  105.393 39.723  1.00 18.24  ? 215 PRO D N   1 
ATOM   12176 C  CA  . PRO D  1 215 ? 65.837  106.440 40.163  1.00 17.32  ? 215 PRO D CA  1 
ATOM   12177 C  C   . PRO D  1 215 ? 64.405  105.978 40.244  1.00 20.40  ? 215 PRO D C   1 
ATOM   12178 O  O   . PRO D  1 215 ? 63.953  105.218 39.407  1.00 27.93  ? 215 PRO D O   1 
ATOM   12179 C  CB  . PRO D  1 215 ? 65.970  107.479 39.064  1.00 12.76  ? 215 PRO D CB  1 
ATOM   12180 C  CG  . PRO D  1 215 ? 67.364  107.316 38.592  1.00 7.19   ? 215 PRO D CG  1 
ATOM   12181 C  CD  . PRO D  1 215 ? 67.486  105.815 38.518  1.00 12.53  ? 215 PRO D CD  1 
ATOM   12182 N  N   . PHE D  1 216 ? 63.696  106.456 41.250  1.00 20.16  ? 216 PHE D N   1 
ATOM   12183 C  CA  . PHE D  1 216 ? 62.279  106.157 41.412  1.00 20.06  ? 216 PHE D CA  1 
ATOM   12184 C  C   . PHE D  1 216 ? 61.940  104.714 41.662  1.00 17.38  ? 216 PHE D C   1 
ATOM   12185 O  O   . PHE D  1 216 ? 60.765  104.348 41.594  1.00 18.25  ? 216 PHE D O   1 
ATOM   12186 C  CB  . PHE D  1 216 ? 61.484  106.669 40.207  1.00 18.59  ? 216 PHE D CB  1 
ATOM   12187 C  CG  . PHE D  1 216 ? 61.654  108.153 39.951  1.00 21.23  ? 216 PHE D CG  1 
ATOM   12188 C  CD1 . PHE D  1 216 ? 61.049  109.106 40.780  1.00 25.01  ? 216 PHE D CD1 1 
ATOM   12189 C  CD2 . PHE D  1 216 ? 62.440  108.605 38.898  1.00 19.26  ? 216 PHE D CD2 1 
ATOM   12190 C  CE1 . PHE D  1 216 ? 61.231  110.469 40.545  1.00 16.62  ? 216 PHE D CE1 1 
ATOM   12191 C  CE2 . PHE D  1 216 ? 62.624  109.951 38.667  1.00 13.08  ? 216 PHE D CE2 1 
ATOM   12192 C  CZ  . PHE D  1 216 ? 62.020  110.875 39.489  1.00 14.45  ? 216 PHE D CZ  1 
ATOM   12193 N  N   . LYS D  1 217 ? 62.921  103.910 42.044  1.00 15.59  ? 217 LYS D N   1 
ATOM   12194 C  CA  . LYS D  1 217 ? 62.611  102.508 42.282  1.00 14.32  ? 217 LYS D CA  1 
ATOM   12195 C  C   . LYS D  1 217 ? 61.468  102.123 43.245  1.00 10.03  ? 217 LYS D C   1 
ATOM   12196 O  O   . LYS D  1 217 ? 60.434  101.597 42.821  1.00 7.73   ? 217 LYS D O   1 
ATOM   12197 C  CB  . LYS D  1 217 ? 63.867  101.757 42.642  1.00 18.54  ? 217 LYS D CB  1 
ATOM   12198 C  CG  . LYS D  1 217 ? 63.582  100.287 42.749  1.00 17.91  ? 217 LYS D CG  1 
ATOM   12199 C  CD  . LYS D  1 217 ? 64.879  99.521  42.644  1.00 19.99  ? 217 LYS D CD  1 
ATOM   12200 C  CE  . LYS D  1 217 ? 65.139  98.742  43.888  1.00 21.25  ? 217 LYS D CE  1 
ATOM   12201 N  NZ  . LYS D  1 217 ? 66.473  98.115  43.785  1.00 25.41  ? 217 LYS D NZ  1 
ATOM   12202 N  N   . PRO D  1 218 ? 61.598  102.430 44.550  1.00 9.69   ? 218 PRO D N   1 
ATOM   12203 C  CA  . PRO D  1 218 ? 60.486  102.031 45.415  1.00 8.54   ? 218 PRO D CA  1 
ATOM   12204 C  C   . PRO D  1 218 ? 59.177  102.669 44.997  1.00 12.78  ? 218 PRO D C   1 
ATOM   12205 O  O   . PRO D  1 218 ? 58.128  102.025 44.991  1.00 15.32  ? 218 PRO D O   1 
ATOM   12206 C  CB  . PRO D  1 218 ? 60.928  102.523 46.788  1.00 8.63   ? 218 PRO D CB  1 
ATOM   12207 C  CG  . PRO D  1 218 ? 62.404  102.530 46.720  1.00 12.55  ? 218 PRO D CG  1 
ATOM   12208 C  CD  . PRO D  1 218 ? 62.659  103.074 45.343  1.00 9.12   ? 218 PRO D CD  1 
ATOM   12209 N  N   . PHE D  1 219 ? 59.230  103.935 44.596  1.00 19.51  ? 219 PHE D N   1 
ATOM   12210 C  CA  . PHE D  1 219 ? 58.004  104.639 44.203  1.00 16.79  ? 219 PHE D CA  1 
ATOM   12211 C  C   . PHE D  1 219 ? 57.324  103.880 43.096  1.00 20.36  ? 219 PHE D C   1 
ATOM   12212 O  O   . PHE D  1 219 ? 56.147  103.463 43.192  1.00 22.56  ? 219 PHE D O   1 
ATOM   12213 C  CB  . PHE D  1 219 ? 58.339  106.062 43.732  1.00 20.75  ? 219 PHE D CB  1 
ATOM   12214 C  CG  . PHE D  1 219 ? 57.156  106.844 43.186  1.00 16.30  ? 219 PHE D CG  1 
ATOM   12215 C  CD1 . PHE D  1 219 ? 56.043  107.135 43.971  1.00 20.79  ? 219 PHE D CD1 1 
ATOM   12216 C  CD2 . PHE D  1 219 ? 57.131  107.230 41.865  1.00 14.42  ? 219 PHE D CD2 1 
ATOM   12217 C  CE1 . PHE D  1 219 ? 54.900  107.789 43.439  1.00 15.94  ? 219 PHE D CE1 1 
ATOM   12218 C  CE2 . PHE D  1 219 ? 55.998  107.884 41.316  1.00 15.65  ? 219 PHE D CE2 1 
ATOM   12219 C  CZ  . PHE D  1 219 ? 54.877  108.155 42.123  1.00 14.90  ? 219 PHE D CZ  1 
ATOM   12220 N  N   . SER D  1 220 ? 58.124  103.582 42.089  1.00 17.17  ? 220 SER D N   1 
ATOM   12221 C  CA  . SER D  1 220 ? 57.567  102.943 40.950  1.00 15.17  ? 220 SER D CA  1 
ATOM   12222 C  C   . SER D  1 220 ? 57.031  101.593 41.212  1.00 19.61  ? 220 SER D C   1 
ATOM   12223 O  O   . SER D  1 220 ? 56.112  101.195 40.525  1.00 27.76  ? 220 SER D O   1 
ATOM   12224 C  CB  . SER D  1 220 ? 58.550  102.928 39.806  1.00 10.18  ? 220 SER D CB  1 
ATOM   12225 O  OG  . SER D  1 220 ? 59.728  102.307 40.209  1.00 25.03  ? 220 SER D OG  1 
ATOM   12226 N  N   . TYR D  1 221 ? 57.551  100.864 42.193  1.00 19.92  ? 221 TYR D N   1 
ATOM   12227 C  CA  . TYR D  1 221 ? 57.012  99.522  42.424  1.00 17.88  ? 221 TYR D CA  1 
ATOM   12228 C  C   . TYR D  1 221 ? 55.687  99.606  43.075  1.00 17.34  ? 221 TYR D C   1 
ATOM   12229 O  O   . TYR D  1 221 ? 54.779  98.863  42.737  1.00 24.13  ? 221 TYR D O   1 
ATOM   12230 C  CB  . TYR D  1 221 ? 57.929  98.706  43.334  1.00 19.63  ? 221 TYR D CB  1 
ATOM   12231 C  CG  . TYR D  1 221 ? 58.982  97.948  42.581  1.00 20.91  ? 221 TYR D CG  1 
ATOM   12232 C  CD1 . TYR D  1 221 ? 58.718  96.699  42.071  1.00 23.34  ? 221 TYR D CD1 1 
ATOM   12233 C  CD2 . TYR D  1 221 ? 60.217  98.506  42.324  1.00 22.93  ? 221 TYR D CD2 1 
ATOM   12234 C  CE1 . TYR D  1 221 ? 59.644  96.025  41.325  1.00 18.91  ? 221 TYR D CE1 1 
ATOM   12235 C  CE2 . TYR D  1 221 ? 61.137  97.842  41.579  1.00 23.98  ? 221 TYR D CE2 1 
ATOM   12236 C  CZ  . TYR D  1 221 ? 60.850  96.591  41.071  1.00 24.48  ? 221 TYR D CZ  1 
ATOM   12237 O  OH  . TYR D  1 221 ? 61.784  95.932  40.265  1.00 34.38  ? 221 TYR D OH  1 
ATOM   12238 N  N   . ARG D  1 222 ? 55.576  100.551 43.979  1.00 17.37  ? 222 ARG D N   1 
ATOM   12239 C  CA  . ARG D  1 222 ? 54.393  100.711 44.757  1.00 21.86  ? 222 ARG D CA  1 
ATOM   12240 C  C   . ARG D  1 222 ? 53.264  101.480 44.137  1.00 24.21  ? 222 ARG D C   1 
ATOM   12241 O  O   . ARG D  1 222 ? 52.093  101.106 44.291  1.00 27.22  ? 222 ARG D O   1 
ATOM   12242 C  CB  . ARG D  1 222 ? 54.791  101.345 46.076  1.00 24.33  ? 222 ARG D CB  1 
ATOM   12243 C  CG  . ARG D  1 222 ? 55.653  100.431 46.885  1.00 21.82  ? 222 ARG D CG  1 
ATOM   12244 C  CD  . ARG D  1 222 ? 56.648  101.184 47.684  1.00 19.52  ? 222 ARG D CD  1 
ATOM   12245 N  NE  . ARG D  1 222 ? 57.345  100.376 48.696  1.00 18.82  ? 222 ARG D NE  1 
ATOM   12246 C  CZ  . ARG D  1 222 ? 56.777  99.866  49.784  1.00 12.93  ? 222 ARG D CZ  1 
ATOM   12247 N  NH1 . ARG D  1 222 ? 55.473  100.057 50.018  1.00 12.91  ? 222 ARG D NH1 1 
ATOM   12248 N  NH2 . ARG D  1 222 ? 57.512  99.188  50.650  1.00 9.55   ? 222 ARG D NH2 1 
ATOM   12249 N  N   . TYR D  1 223 ? 53.603  102.535 43.410  1.00 21.78  ? 223 TYR D N   1 
ATOM   12250 C  CA  . TYR D  1 223 ? 52.573  103.375 42.823  1.00 21.36  ? 223 TYR D CA  1 
ATOM   12251 C  C   . TYR D  1 223 ? 52.581  103.273 41.325  1.00 22.90  ? 223 TYR D C   1 
ATOM   12252 O  O   . TYR D  1 223 ? 53.573  103.606 40.677  1.00 26.51  ? 223 TYR D O   1 
ATOM   12253 C  CB  . TYR D  1 223 ? 52.791  104.796 43.288  1.00 13.97  ? 223 TYR D CB  1 
ATOM   12254 C  CG  . TYR D  1 223 ? 52.607  104.865 44.771  1.00 18.88  ? 223 TYR D CG  1 
ATOM   12255 C  CD1 . TYR D  1 223 ? 51.343  104.783 45.305  1.00 23.11  ? 223 TYR D CD1 1 
ATOM   12256 C  CD2 . TYR D  1 223 ? 53.681  104.898 45.643  1.00 20.86  ? 223 TYR D CD2 1 
ATOM   12257 C  CE1 . TYR D  1 223 ? 51.123  104.724 46.676  1.00 20.75  ? 223 TYR D CE1 1 
ATOM   12258 C  CE2 . TYR D  1 223 ? 53.491  104.832 47.027  1.00 23.14  ? 223 TYR D CE2 1 
ATOM   12259 C  CZ  . TYR D  1 223 ? 52.191  104.742 47.539  1.00 26.84  ? 223 TYR D CZ  1 
ATOM   12260 O  OH  . TYR D  1 223 ? 51.895  104.628 48.893  1.00 27.26  ? 223 TYR D OH  1 
ATOM   12261 N  N   . HIS D  1 224 ? 51.481  102.803 40.761  1.00 22.46  ? 224 HIS D N   1 
ATOM   12262 C  CA  . HIS D  1 224 ? 51.424  102.652 39.319  1.00 23.12  ? 224 HIS D CA  1 
ATOM   12263 C  C   . HIS D  1 224 ? 50.429  103.662 38.770  1.00 30.15  ? 224 HIS D C   1 
ATOM   12264 O  O   . HIS D  1 224 ? 49.488  104.031 39.487  1.00 35.75  ? 224 HIS D O   1 
ATOM   12265 C  CB  . HIS D  1 224 ? 50.931  101.271 38.944  1.00 25.74  ? 224 HIS D CB  1 
ATOM   12266 C  CG  . HIS D  1 224 ? 51.980  100.197 38.967  1.00 31.02  ? 224 HIS D CG  1 
ATOM   12267 N  ND1 . HIS D  1 224 ? 51.867  99.033  38.234  1.00 30.02  ? 224 HIS D ND1 1 
ATOM   12268 C  CD2 . HIS D  1 224 ? 53.158  100.110 39.627  1.00 34.29  ? 224 HIS D CD2 1 
ATOM   12269 C  CE1 . HIS D  1 224 ? 52.938  98.283  38.433  1.00 34.33  ? 224 HIS D CE1 1 
ATOM   12270 N  NE2 . HIS D  1 224 ? 53.735  98.909  39.277  1.00 33.74  ? 224 HIS D NE2 1 
ATOM   12271 N  N   . VAL D  1 225 ? 50.577  104.023 37.486  1.00 29.71  ? 225 VAL D N   1 
ATOM   12272 C  CA  . VAL D  1 225 ? 49.702  104.989 36.826  1.00 23.72  ? 225 VAL D CA  1 
ATOM   12273 C  C   . VAL D  1 225 ? 49.446  104.510 35.414  1.00 25.45  ? 225 VAL D C   1 
ATOM   12274 O  O   . VAL D  1 225 ? 50.272  103.791 34.852  1.00 36.83  ? 225 VAL D O   1 
ATOM   12275 C  CB  . VAL D  1 225 ? 50.398  106.323 36.747  1.00 23.68  ? 225 VAL D CB  1 
ATOM   12276 C  CG1 . VAL D  1 225 ? 50.629  106.829 38.114  1.00 26.15  ? 225 VAL D CG1 1 
ATOM   12277 C  CG2 . VAL D  1 225 ? 51.747  106.185 36.036  1.00 25.61  ? 225 VAL D CG2 1 
ATOM   12278 N  N   . PRO D  1 226 ? 48.331  104.922 34.798  1.00 18.94  ? 226 PRO D N   1 
ATOM   12279 C  CA  . PRO D  1 226 ? 47.901  104.570 33.439  1.00 16.38  ? 226 PRO D CA  1 
ATOM   12280 C  C   . PRO D  1 226 ? 48.644  105.342 32.371  1.00 23.61  ? 226 PRO D C   1 
ATOM   12281 O  O   . PRO D  1 226 ? 48.038  105.887 31.416  1.00 30.18  ? 226 PRO D O   1 
ATOM   12282 C  CB  . PRO D  1 226 ? 46.433  104.956 33.455  1.00 16.01  ? 226 PRO D CB  1 
ATOM   12283 C  CG  . PRO D  1 226 ? 46.422  106.123 34.355  1.00 17.22  ? 226 PRO D CG  1 
ATOM   12284 C  CD  . PRO D  1 226 ? 47.306  105.720 35.476  1.00 16.32  ? 226 PRO D CD  1 
ATOM   12285 N  N   . TYR D  1 227 ? 49.967  105.350 32.472  1.00 20.81  ? 227 TYR D N   1 
ATOM   12286 C  CA  . TYR D  1 227 ? 50.701  106.149 31.533  1.00 16.40  ? 227 TYR D CA  1 
ATOM   12287 C  C   . TYR D  1 227 ? 50.573  105.710 30.109  1.00 19.39  ? 227 TYR D C   1 
ATOM   12288 O  O   . TYR D  1 227 ? 50.690  106.529 29.199  1.00 21.78  ? 227 TYR D O   1 
ATOM   12289 C  CB  . TYR D  1 227 ? 52.145  106.282 31.931  1.00 12.15  ? 227 TYR D CB  1 
ATOM   12290 C  CG  . TYR D  1 227 ? 52.904  105.037 31.789  1.00 18.62  ? 227 TYR D CG  1 
ATOM   12291 C  CD1 . TYR D  1 227 ? 53.498  104.711 30.593  1.00 22.36  ? 227 TYR D CD1 1 
ATOM   12292 C  CD2 . TYR D  1 227 ? 53.070  104.190 32.861  1.00 26.74  ? 227 TYR D CD2 1 
ATOM   12293 C  CE1 . TYR D  1 227 ? 54.232  103.581 30.471  1.00 23.87  ? 227 TYR D CE1 1 
ATOM   12294 C  CE2 . TYR D  1 227 ? 53.813  103.054 32.762  1.00 27.66  ? 227 TYR D CE2 1 
ATOM   12295 C  CZ  . TYR D  1 227 ? 54.396  102.755 31.562  1.00 29.53  ? 227 TYR D CZ  1 
ATOM   12296 O  OH  . TYR D  1 227 ? 55.209  101.649 31.453  1.00 41.86  ? 227 TYR D OH  1 
ATOM   12297 N  N   . GLU D  1 228 ? 50.281  104.448 29.871  1.00 19.03  ? 228 GLU D N   1 
ATOM   12298 C  CA  . GLU D  1 228 ? 50.181  104.057 28.473  1.00 26.32  ? 228 GLU D CA  1 
ATOM   12299 C  C   . GLU D  1 228 ? 48.845  104.496 27.877  1.00 24.85  ? 228 GLU D C   1 
ATOM   12300 O  O   . GLU D  1 228 ? 48.694  104.467 26.676  1.00 25.06  ? 228 GLU D O   1 
ATOM   12301 C  CB  . GLU D  1 228 ? 50.449  102.548 28.217  1.00 36.58  ? 228 GLU D CB  1 
ATOM   12302 C  CG  . GLU D  1 228 ? 50.938  101.682 29.385  1.00 52.06  ? 228 GLU D CG  1 
ATOM   12303 C  CD  . GLU D  1 228 ? 49.988  101.723 30.611  1.00 68.87  ? 228 GLU D CD  1 
ATOM   12304 O  OE1 . GLU D  1 228 ? 48.748  102.034 30.496  1.00 71.29  ? 228 GLU D OE1 1 
ATOM   12305 O  OE2 . GLU D  1 228 ? 50.516  101.462 31.722  1.00 79.62  ? 228 GLU D OE2 1 
ATOM   12306 N  N   . ALA D  1 229 ? 47.878  104.908 28.701  1.00 26.00  ? 229 ALA D N   1 
ATOM   12307 C  CA  . ALA D  1 229 ? 46.573  105.363 28.201  1.00 23.17  ? 229 ALA D CA  1 
ATOM   12308 C  C   . ALA D  1 229 ? 46.770  106.631 27.367  1.00 28.22  ? 229 ALA D C   1 
ATOM   12309 O  O   . ALA D  1 229 ? 46.055  106.836 26.412  1.00 30.28  ? 229 ALA D O   1 
ATOM   12310 C  CB  . ALA D  1 229 ? 45.637  105.628 29.343  1.00 24.76  ? 229 ALA D CB  1 
ATOM   12311 N  N   . SER D  1 230 ? 47.592  107.565 27.861  1.00 32.27  ? 230 SER D N   1 
ATOM   12312 C  CA  . SER D  1 230 ? 48.015  108.769 27.096  1.00 29.93  ? 230 SER D CA  1 
ATOM   12313 C  C   . SER D  1 230 ? 49.043  107.959 26.298  1.00 36.39  ? 230 SER D C   1 
ATOM   12314 O  O   . SER D  1 230 ? 49.266  106.789 26.631  1.00 41.62  ? 230 SER D O   1 
ATOM   12315 C  CB  . SER D  1 230 ? 48.811  109.732 27.988  1.00 22.82  ? 230 SER D CB  1 
ATOM   12316 O  OG  . SER D  1 230 ? 48.612  109.447 29.393  1.00 33.56  ? 230 SER D OG  1 
ATOM   12317 N  N   . GLN D  1 231 ? 49.751  108.467 25.309  1.00 35.28  ? 231 GLN D N   1 
ATOM   12318 C  CA  . GLN D  1 231 ? 50.645  107.486 24.712  1.00 30.96  ? 231 GLN D CA  1 
ATOM   12319 C  C   . GLN D  1 231 ? 52.078  107.626 25.246  1.00 31.42  ? 231 GLN D C   1 
ATOM   12320 O  O   . GLN D  1 231 ? 53.065  107.564 24.502  1.00 36.56  ? 231 GLN D O   1 
ATOM   12321 C  CB  . GLN D  1 231 ? 50.499  107.465 23.188  1.00 44.88  ? 231 GLN D CB  1 
ATOM   12322 C  CG  . GLN D  1 231 ? 49.159  106.885 22.638  1.00 59.12  ? 231 GLN D CG  1 
ATOM   12323 C  CD  . GLN D  1 231 ? 47.909  107.690 23.055  1.00 73.15  ? 231 GLN D CD  1 
ATOM   12324 O  OE1 . GLN D  1 231 ? 47.976  108.900 23.271  1.00 82.44  ? 231 GLN D OE1 1 
ATOM   12325 N  NE2 . GLN D  1 231 ? 46.763  107.016 23.162  1.00 83.22  ? 231 GLN D NE2 1 
ATOM   12326 N  N   . SER D  1 232 ? 52.170  107.795 26.568  1.00 29.98  ? 232 SER D N   1 
ATOM   12327 C  CA  . SER D  1 232 ? 53.442  107.971 27.266  1.00 22.72  ? 232 SER D CA  1 
ATOM   12328 C  C   . SER D  1 232 ? 54.207  106.686 27.326  1.00 25.45  ? 232 SER D C   1 
ATOM   12329 O  O   . SER D  1 232 ? 53.651  105.585 27.295  1.00 27.09  ? 232 SER D O   1 
ATOM   12330 C  CB  . SER D  1 232 ? 53.225  108.476 28.684  1.00 18.21  ? 232 SER D CB  1 
ATOM   12331 O  OG  . SER D  1 232 ? 54.469  108.696 29.311  1.00 20.32  ? 232 SER D OG  1 
ATOM   12332 N  N   . THR D  1 233 ? 55.509  106.829 27.422  1.00 27.96  ? 233 THR D N   1 
ATOM   12333 C  CA  . THR D  1 233 ? 56.372  105.673 27.492  1.00 25.92  ? 233 THR D CA  1 
ATOM   12334 C  C   . THR D  1 233 ? 57.027  105.611 28.832  1.00 26.63  ? 233 THR D C   1 
ATOM   12335 O  O   . THR D  1 233 ? 58.065  104.964 28.977  1.00 31.82  ? 233 THR D O   1 
ATOM   12336 C  CB  . THR D  1 233 ? 57.483  105.715 26.433  1.00 26.52  ? 233 THR D CB  1 
ATOM   12337 O  OG1 . THR D  1 233 ? 58.333  106.854 26.643  1.00 26.03  ? 233 THR D OG1 1 
ATOM   12338 C  CG2 . THR D  1 233 ? 56.883  105.776 25.058  1.00 26.31  ? 233 THR D CG2 1 
ATOM   12339 N  N   . SER D  1 234 ? 56.487  106.368 29.783  1.00 25.91  ? 234 SER D N   1 
ATOM   12340 C  CA  . SER D  1 234 ? 57.022  106.378 31.129  1.00 23.12  ? 234 SER D CA  1 
ATOM   12341 C  C   . SER D  1 234 ? 55.961  106.772 32.108  1.00 20.83  ? 234 SER D C   1 
ATOM   12342 O  O   . SER D  1 234 ? 55.115  107.603 31.830  1.00 22.66  ? 234 SER D O   1 
ATOM   12343 C  CB  . SER D  1 234 ? 58.204  107.298 31.242  1.00 17.89  ? 234 SER D CB  1 
ATOM   12344 O  OG  . SER D  1 234 ? 58.485  107.459 32.589  1.00 28.03  ? 234 SER D OG  1 
ATOM   12345 N  N   . PRO D  1 235 ? 55.971  106.150 33.275  1.00 19.35  ? 235 PRO D N   1 
ATOM   12346 C  CA  . PRO D  1 235 ? 54.964  106.478 34.272  1.00 21.01  ? 235 PRO D CA  1 
ATOM   12347 C  C   . PRO D  1 235 ? 55.193  107.806 34.927  1.00 26.63  ? 235 PRO D C   1 
ATOM   12348 O  O   . PRO D  1 235 ? 54.433  108.189 35.811  1.00 32.07  ? 235 PRO D O   1 
ATOM   12349 C  CB  . PRO D  1 235 ? 55.139  105.353 35.283  1.00 19.10  ? 235 PRO D CB  1 
ATOM   12350 C  CG  . PRO D  1 235 ? 56.600  105.052 35.218  1.00 15.64  ? 235 PRO D CG  1 
ATOM   12351 C  CD  . PRO D  1 235 ? 56.814  105.033 33.729  1.00 14.68  ? 235 PRO D CD  1 
ATOM   12352 N  N   . PHE D  1 236 ? 56.259  108.501 34.544  1.00 29.36  ? 236 PHE D N   1 
ATOM   12353 C  CA  . PHE D  1 236 ? 56.561  109.768 35.188  1.00 24.45  ? 236 PHE D CA  1 
ATOM   12354 C  C   . PHE D  1 236 ? 55.928  110.967 34.617  1.00 25.54  ? 236 PHE D C   1 
ATOM   12355 O  O   . PHE D  1 236 ? 56.093  112.035 35.164  1.00 36.97  ? 236 PHE D O   1 
ATOM   12356 C  CB  . PHE D  1 236 ? 58.038  109.952 35.287  1.00 23.41  ? 236 PHE D CB  1 
ATOM   12357 C  CG  . PHE D  1 236 ? 58.662  108.888 36.071  1.00 22.49  ? 236 PHE D CG  1 
ATOM   12358 C  CD1 . PHE D  1 236 ? 58.042  108.440 37.197  1.00 23.51  ? 236 PHE D CD1 1 
ATOM   12359 C  CD2 . PHE D  1 236 ? 59.783  108.231 35.631  1.00 25.47  ? 236 PHE D CD2 1 
ATOM   12360 C  CE1 . PHE D  1 236 ? 58.532  107.337 37.867  1.00 28.38  ? 236 PHE D CE1 1 
ATOM   12361 C  CE2 . PHE D  1 236 ? 60.270  107.134 36.298  1.00 17.59  ? 236 PHE D CE2 1 
ATOM   12362 C  CZ  . PHE D  1 236 ? 59.647  106.683 37.410  1.00 19.16  ? 236 PHE D CZ  1 
ATOM   12363 N  N   . TRP D  1 237 ? 55.254  110.806 33.491  1.00 26.71  ? 237 TRP D N   1 
ATOM   12364 C  CA  . TRP D  1 237 ? 54.535  111.870 32.833  1.00 20.97  ? 237 TRP D CA  1 
ATOM   12365 C  C   . TRP D  1 237 ? 53.441  111.195 32.062  1.00 21.47  ? 237 TRP D C   1 
ATOM   12366 O  O   . TRP D  1 237 ? 53.664  110.178 31.399  1.00 23.60  ? 237 TRP D O   1 
ATOM   12367 C  CB  . TRP D  1 237 ? 55.413  112.689 31.924  1.00 17.96  ? 237 TRP D CB  1 
ATOM   12368 C  CG  . TRP D  1 237 ? 56.064  111.928 30.884  1.00 18.11  ? 237 TRP D CG  1 
ATOM   12369 C  CD1 . TRP D  1 237 ? 55.596  111.651 29.633  1.00 24.05  ? 237 TRP D CD1 1 
ATOM   12370 C  CD2 . TRP D  1 237 ? 57.385  111.431 30.931  1.00 19.46  ? 237 TRP D CD2 1 
ATOM   12371 N  NE1 . TRP D  1 237 ? 56.565  111.021 28.880  1.00 18.84  ? 237 TRP D NE1 1 
ATOM   12372 C  CE2 . TRP D  1 237 ? 57.672  110.880 29.644  1.00 14.84  ? 237 TRP D CE2 1 
ATOM   12373 C  CE3 . TRP D  1 237 ? 58.367  111.399 31.931  1.00 18.93  ? 237 TRP D CE3 1 
ATOM   12374 C  CZ2 . TRP D  1 237 ? 58.888  110.322 29.345  1.00 13.66  ? 237 TRP D CZ2 1 
ATOM   12375 C  CZ3 . TRP D  1 237 ? 59.588  110.834 31.627  1.00 15.94  ? 237 TRP D CZ3 1 
ATOM   12376 C  CH2 . TRP D  1 237 ? 59.843  110.297 30.332  1.00 13.59  ? 237 TRP D CH2 1 
ATOM   12377 N  N   . TYR D  1 238 ? 52.251  111.738 32.184  1.00 20.64  ? 238 TYR D N   1 
ATOM   12378 C  CA  . TYR D  1 238 ? 51.111  111.157 31.536  1.00 21.84  ? 238 TYR D CA  1 
ATOM   12379 C  C   . TYR D  1 238 ? 49.968  112.112 31.754  1.00 24.15  ? 238 TYR D C   1 
ATOM   12380 O  O   . TYR D  1 238 ? 50.169  113.162 32.343  1.00 24.17  ? 238 TYR D O   1 
ATOM   12381 C  CB  . TYR D  1 238 ? 50.801  109.820 32.226  1.00 19.29  ? 238 TYR D CB  1 
ATOM   12382 C  CG  . TYR D  1 238 ? 50.522  109.939 33.692  1.00 10.51  ? 238 TYR D CG  1 
ATOM   12383 C  CD1 . TYR D  1 238 ? 51.550  110.043 34.626  1.00 13.58  ? 238 TYR D CD1 1 
ATOM   12384 C  CD2 . TYR D  1 238 ? 49.219  109.964 34.165  1.00 14.18  ? 238 TYR D CD2 1 
ATOM   12385 C  CE1 . TYR D  1 238 ? 51.288  110.165 36.023  1.00 13.00  ? 238 TYR D CE1 1 
ATOM   12386 C  CE2 . TYR D  1 238 ? 48.922  110.078 35.554  1.00 17.06  ? 238 TYR D CE2 1 
ATOM   12387 C  CZ  . TYR D  1 238 ? 49.961  110.188 36.474  1.00 20.26  ? 238 TYR D CZ  1 
ATOM   12388 O  OH  . TYR D  1 238 ? 49.681  110.277 37.836  1.00 19.41  ? 238 TYR D OH  1 
ATOM   12389 N  N   . SER D  1 239 ? 48.780  111.743 31.294  1.00 27.54  ? 239 SER D N   1 
ATOM   12390 C  CA  . SER D  1 239 ? 47.597  112.564 31.514  1.00 29.15  ? 239 SER D CA  1 
ATOM   12391 C  C   . SER D  1 239 ? 46.365  111.702 31.637  1.00 29.06  ? 239 SER D C   1 
ATOM   12392 O  O   . SER D  1 239 ? 46.363  110.530 31.243  1.00 34.15  ? 239 SER D O   1 
ATOM   12393 C  CB  . SER D  1 239 ? 47.389  113.482 30.349  1.00 29.42  ? 239 SER D CB  1 
ATOM   12394 O  OG  . SER D  1 239 ? 47.032  112.700 29.242  1.00 40.76  ? 239 SER D OG  1 
ATOM   12395 N  N   . ILE D  1 240 ? 45.323  112.277 32.201  1.00 29.62  ? 240 ILE D N   1 
ATOM   12396 C  CA  . ILE D  1 240 ? 44.048  111.580 32.359  1.00 31.83  ? 240 ILE D CA  1 
ATOM   12397 C  C   . ILE D  1 240 ? 42.966  112.622 32.204  1.00 31.13  ? 240 ILE D C   1 
ATOM   12398 O  O   . ILE D  1 240 ? 43.217  113.798 32.392  1.00 37.06  ? 240 ILE D O   1 
ATOM   12399 C  CB  . ILE D  1 240 ? 43.857  110.972 33.741  1.00 27.68  ? 240 ILE D CB  1 
ATOM   12400 C  CG1 . ILE D  1 240 ? 43.932  112.032 34.798  1.00 27.33  ? 240 ILE D CG1 1 
ATOM   12401 C  CG2 . ILE D  1 240 ? 44.930  109.988 34.018  1.00 30.69  ? 240 ILE D CG2 1 
ATOM   12402 C  CD1 . ILE D  1 240 ? 43.439  111.532 36.112  1.00 32.49  ? 240 ILE D CD1 1 
ATOM   12403 N  N   . LYS D  1 241 ? 41.790  112.221 31.796  1.00 24.34  ? 241 LYS D N   1 
ATOM   12404 C  CA  . LYS D  1 241 ? 40.736  113.167 31.653  1.00 24.43  ? 241 LYS D CA  1 
ATOM   12405 C  C   . LYS D  1 241 ? 39.792  112.700 32.701  1.00 26.65  ? 241 LYS D C   1 
ATOM   12406 O  O   . LYS D  1 241 ? 39.642  111.510 32.870  1.00 27.91  ? 241 LYS D O   1 
ATOM   12407 C  CB  . LYS D  1 241 ? 40.044  113.038 30.315  1.00 21.68  ? 241 LYS D CB  1 
ATOM   12408 C  CG  . LYS D  1 241 ? 40.817  113.444 29.099  1.00 22.07  ? 241 LYS D CG  1 
ATOM   12409 C  CD  . LYS D  1 241 ? 39.926  113.129 27.896  1.00 27.35  ? 241 LYS D CD  1 
ATOM   12410 C  CE  . LYS D  1 241 ? 40.547  113.476 26.553  1.00 39.88  ? 241 LYS D CE  1 
ATOM   12411 N  NZ  . LYS D  1 241 ? 39.656  112.922 25.469  1.00 42.84  ? 241 LYS D NZ  1 
ATOM   12412 N  N   . ARG D  1 242 ? 39.159  113.614 33.419  1.00 28.61  ? 242 ARG D N   1 
ATOM   12413 C  CA  . ARG D  1 242 ? 38.212  113.196 34.442  1.00 33.93  ? 242 ARG D CA  1 
ATOM   12414 C  C   . ARG D  1 242 ? 37.166  114.281 34.622  1.00 36.97  ? 242 ARG D C   1 
ATOM   12415 O  O   . ARG D  1 242 ? 37.517  115.431 34.874  1.00 43.91  ? 242 ARG D O   1 
ATOM   12416 C  CB  . ARG D  1 242 ? 38.931  112.895 35.754  1.00 25.41  ? 242 ARG D CB  1 
ATOM   12417 C  CG  . ARG D  1 242 ? 38.012  112.826 36.898  1.00 31.59  ? 242 ARG D CG  1 
ATOM   12418 C  CD  . ARG D  1 242 ? 38.633  112.163 38.086  1.00 32.46  ? 242 ARG D CD  1 
ATOM   12419 N  NE  . ARG D  1 242 ? 38.629  110.728 37.880  1.00 30.17  ? 242 ARG D NE  1 
ATOM   12420 C  CZ  . ARG D  1 242 ? 38.283  109.832 38.794  1.00 26.85  ? 242 ARG D CZ  1 
ATOM   12421 N  NH1 . ARG D  1 242 ? 37.899  110.199 40.005  1.00 23.07  ? 242 ARG D NH1 1 
ATOM   12422 N  NH2 . ARG D  1 242 ? 38.308  108.554 38.471  1.00 31.81  ? 242 ARG D NH2 1 
ATOM   12423 N  N   . ALA D  1 243 ? 35.890  113.925 34.458  1.00 35.92  ? 243 ALA D N   1 
ATOM   12424 C  CA  . ALA D  1 243 ? 34.799  114.890 34.572  1.00 32.46  ? 243 ALA D CA  1 
ATOM   12425 C  C   . ALA D  1 243 ? 35.033  115.928 33.496  1.00 36.49  ? 243 ALA D C   1 
ATOM   12426 O  O   . ALA D  1 243 ? 35.165  115.566 32.318  1.00 38.45  ? 243 ALA D O   1 
ATOM   12427 C  CB  . ALA D  1 243 ? 34.803  115.540 35.910  1.00 31.30  ? 243 ALA D CB  1 
ATOM   12428 N  N   . SER D  1 244 ? 35.172  117.197 33.886  1.00 36.47  ? 244 SER D N   1 
ATOM   12429 C  CA  . SER D  1 244 ? 35.395  118.257 32.911  1.00 33.32  ? 244 SER D CA  1 
ATOM   12430 C  C   . SER D  1 244 ? 36.847  118.704 32.800  1.00 33.06  ? 244 SER D C   1 
ATOM   12431 O  O   . SER D  1 244 ? 37.128  119.696 32.113  1.00 41.81  ? 244 SER D O   1 
ATOM   12432 C  CB  . SER D  1 244 ? 34.509  119.437 33.267  1.00 28.25  ? 244 SER D CB  1 
ATOM   12433 O  OG  . SER D  1 244 ? 34.653  119.752 34.638  1.00 32.73  ? 244 SER D OG  1 
ATOM   12434 N  N   . ALA D  1 245 ? 37.775  117.988 33.428  1.00 25.67  ? 245 ALA D N   1 
ATOM   12435 C  CA  . ALA D  1 245 ? 39.165  118.416 33.404  1.00 26.72  ? 245 ALA D CA  1 
ATOM   12436 C  C   . ALA D  1 245 ? 40.064  117.528 32.638  1.00 28.85  ? 245 ALA D C   1 
ATOM   12437 O  O   . ALA D  1 245 ? 39.834  116.321 32.591  1.00 31.99  ? 245 ALA D O   1 
ATOM   12438 C  CB  . ALA D  1 245 ? 39.692  118.488 34.783  1.00 30.22  ? 245 ALA D CB  1 
ATOM   12439 N  N   . HIS D  1 246 ? 41.114  118.118 32.081  1.00 23.84  ? 246 HIS D N   1 
ATOM   12440 C  CA  . HIS D  1 246 ? 42.107  117.368 31.335  1.00 29.03  ? 246 HIS D CA  1 
ATOM   12441 C  C   . HIS D  1 246 ? 43.348  117.678 32.149  1.00 32.19  ? 246 HIS D C   1 
ATOM   12442 O  O   . HIS D  1 246 ? 43.772  118.825 32.196  1.00 39.27  ? 246 HIS D O   1 
ATOM   12443 C  CB  . HIS D  1 246 ? 42.246  117.883 29.902  1.00 29.39  ? 246 HIS D CB  1 
ATOM   12444 C  CG  . HIS D  1 246 ? 43.131  117.039 29.017  1.00 38.36  ? 246 HIS D CG  1 
ATOM   12445 N  ND1 . HIS D  1 246 ? 42.679  116.451 27.851  1.00 39.76  ? 246 HIS D ND1 1 
ATOM   12446 C  CD2 . HIS D  1 246 ? 44.444  116.702 29.114  1.00 39.53  ? 246 HIS D CD2 1 
ATOM   12447 C  CE1 . HIS D  1 246 ? 43.670  115.787 27.276  1.00 40.92  ? 246 HIS D CE1 1 
ATOM   12448 N  NE2 . HIS D  1 246 ? 44.752  115.922 28.023  1.00 36.45  ? 246 HIS D NE2 1 
ATOM   12449 N  N   . ILE D  1 247 ? 43.901  116.659 32.807  1.00 31.28  ? 247 ILE D N   1 
ATOM   12450 C  CA  . ILE D  1 247 ? 45.055  116.787 33.695  1.00 25.94  ? 247 ILE D CA  1 
ATOM   12451 C  C   . ILE D  1 247 ? 46.286  116.240 33.071  1.00 26.04  ? 247 ILE D C   1 
ATOM   12452 O  O   . ILE D  1 247 ? 46.270  115.136 32.555  1.00 31.58  ? 247 ILE D O   1 
ATOM   12453 C  CB  . ILE D  1 247 ? 44.757  116.035 34.958  1.00 21.40  ? 247 ILE D CB  1 
ATOM   12454 C  CG1 . ILE D  1 247 ? 43.405  116.545 35.476  1.00 19.02  ? 247 ILE D CG1 1 
ATOM   12455 C  CG2 . ILE D  1 247 ? 45.878  116.213 35.944  1.00 26.46  ? 247 ILE D CG2 1 
ATOM   12456 C  CD1 . ILE D  1 247 ? 42.901  115.891 36.657  1.00 22.63  ? 247 ILE D CD1 1 
ATOM   12457 N  N   . ILE D  1 248 ? 47.353  117.009 33.117  1.00 22.41  ? 248 ILE D N   1 
ATOM   12458 C  CA  . ILE D  1 248 ? 48.601  116.607 32.521  1.00 20.02  ? 248 ILE D CA  1 
ATOM   12459 C  C   . ILE D  1 248 ? 49.592  116.589 33.664  1.00 25.13  ? 248 ILE D C   1 
ATOM   12460 O  O   . ILE D  1 248 ? 49.695  117.597 34.352  1.00 31.00  ? 248 ILE D O   1 
ATOM   12461 C  CB  . ILE D  1 248 ? 49.055  117.647 31.499  1.00 17.81  ? 248 ILE D CB  1 
ATOM   12462 C  CG1 . ILE D  1 248 ? 48.126  117.645 30.303  1.00 13.92  ? 248 ILE D CG1 1 
ATOM   12463 C  CG2 . ILE D  1 248 ? 50.496  117.402 31.049  1.00 16.02  ? 248 ILE D CG2 1 
ATOM   12464 C  CD1 . ILE D  1 248 ? 48.706  118.425 29.188  1.00 6.96   ? 248 ILE D CD1 1 
ATOM   12465 N  N   . VAL D  1 249 ? 50.272  115.459 33.893  1.00 19.90  ? 249 VAL D N   1 
ATOM   12466 C  CA  . VAL D  1 249 ? 51.266  115.337 34.949  1.00 15.89  ? 249 VAL D CA  1 
ATOM   12467 C  C   . VAL D  1 249 ? 52.690  115.324 34.354  1.00 17.52  ? 249 VAL D C   1 
ATOM   12468 O  O   . VAL D  1 249 ? 52.949  114.607 33.419  1.00 16.34  ? 249 VAL D O   1 
ATOM   12469 C  CB  . VAL D  1 249 ? 51.072  114.034 35.715  1.00 16.92  ? 249 VAL D CB  1 
ATOM   12470 C  CG1 . VAL D  1 249 ? 52.091  113.925 36.859  1.00 20.59  ? 249 VAL D CG1 1 
ATOM   12471 C  CG2 . VAL D  1 249 ? 49.655  113.894 36.218  1.00 10.88  ? 249 VAL D CG2 1 
ATOM   12472 N  N   . LEU D  1 250 ? 53.613  116.087 34.917  1.00 16.56  ? 250 LEU D N   1 
ATOM   12473 C  CA  . LEU D  1 250 ? 54.973  116.134 34.397  1.00 18.14  ? 250 LEU D CA  1 
ATOM   12474 C  C   . LEU D  1 250 ? 55.986  115.700 35.476  1.00 23.73  ? 250 LEU D C   1 
ATOM   12475 O  O   . LEU D  1 250 ? 55.644  115.574 36.691  1.00 19.76  ? 250 LEU D O   1 
ATOM   12476 C  CB  . LEU D  1 250 ? 55.295  117.539 33.893  1.00 17.43  ? 250 LEU D CB  1 
ATOM   12477 C  CG  . LEU D  1 250 ? 54.375  118.038 32.806  1.00 19.45  ? 250 LEU D CG  1 
ATOM   12478 C  CD1 . LEU D  1 250 ? 54.772  119.388 32.360  1.00 21.69  ? 250 LEU D CD1 1 
ATOM   12479 C  CD2 . LEU D  1 250 ? 54.451  117.110 31.650  1.00 24.42  ? 250 LEU D CD2 1 
ATOM   12480 N  N   . SER D  1 251 ? 57.242  115.556 35.062  1.00 17.82  ? 251 SER D N   1 
ATOM   12481 C  CA  . SER D  1 251 ? 58.258  115.076 35.978  1.00 20.79  ? 251 SER D CA  1 
ATOM   12482 C  C   . SER D  1 251 ? 59.417  116.041 36.017  1.00 21.98  ? 251 SER D C   1 
ATOM   12483 O  O   . SER D  1 251 ? 60.235  116.080 35.093  1.00 24.50  ? 251 SER D O   1 
ATOM   12484 C  CB  . SER D  1 251 ? 58.665  113.685 35.487  1.00 20.76  ? 251 SER D CB  1 
ATOM   12485 O  OG  . SER D  1 251 ? 59.750  113.103 36.160  1.00 28.11  ? 251 SER D OG  1 
ATOM   12486 N  N   . SER D  1 252 ? 59.513  116.789 37.104  1.00 17.54  ? 252 SER D N   1 
ATOM   12487 C  CA  . SER D  1 252 ? 60.562  117.794 37.213  1.00 18.69  ? 252 SER D CA  1 
ATOM   12488 C  C   . SER D  1 252 ? 61.938  117.218 37.213  1.00 20.72  ? 252 SER D C   1 
ATOM   12489 O  O   . SER D  1 252 ? 62.935  117.902 36.859  1.00 28.30  ? 252 SER D O   1 
ATOM   12490 C  CB  . SER D  1 252 ? 60.394  118.624 38.488  1.00 16.83  ? 252 SER D CB  1 
ATOM   12491 O  OG  . SER D  1 252 ? 59.175  119.378 38.578  1.00 24.93  ? 252 SER D OG  1 
ATOM   12492 N  N   . TYR D  1 253 ? 61.998  115.959 37.625  1.00 25.34  ? 253 TYR D N   1 
ATOM   12493 C  CA  . TYR D  1 253 ? 63.288  115.266 37.788  1.00 27.91  ? 253 TYR D CA  1 
ATOM   12494 C  C   . TYR D  1 253 ? 63.635  114.226 36.732  1.00 30.93  ? 253 TYR D C   1 
ATOM   12495 O  O   . TYR D  1 253 ? 64.614  113.476 36.849  1.00 32.66  ? 253 TYR D O   1 
ATOM   12496 C  CB  . TYR D  1 253 ? 63.395  114.745 39.212  1.00 17.68  ? 253 TYR D CB  1 
ATOM   12497 C  CG  . TYR D  1 253 ? 63.161  115.892 40.171  1.00 18.65  ? 253 TYR D CG  1 
ATOM   12498 C  CD1 . TYR D  1 253 ? 64.100  116.920 40.279  1.00 20.29  ? 253 TYR D CD1 1 
ATOM   12499 C  CD2 . TYR D  1 253 ? 61.957  116.022 40.905  1.00 17.99  ? 253 TYR D CD2 1 
ATOM   12500 C  CE1 . TYR D  1 253 ? 63.853  118.046 41.078  1.00 23.54  ? 253 TYR D CE1 1 
ATOM   12501 C  CE2 . TYR D  1 253 ? 61.697  117.191 41.738  1.00 14.98  ? 253 TYR D CE2 1 
ATOM   12502 C  CZ  . TYR D  1 253 ? 62.653  118.179 41.786  1.00 17.90  ? 253 TYR D CZ  1 
ATOM   12503 O  OH  . TYR D  1 253 ? 62.427  119.385 42.409  1.00 28.56  ? 253 TYR D OH  1 
ATOM   12504 N  N   . SER D  1 254 ? 62.754  114.150 35.743  1.00 29.87  ? 254 SER D N   1 
ATOM   12505 C  CA  . SER D  1 254 ? 62.974  113.347 34.572  1.00 27.54  ? 254 SER D CA  1 
ATOM   12506 C  C   . SER D  1 254 ? 63.603  114.389 33.595  1.00 29.28  ? 254 SER D C   1 
ATOM   12507 O  O   . SER D  1 254 ? 63.952  115.502 34.020  1.00 40.80  ? 254 SER D O   1 
ATOM   12508 C  CB  . SER D  1 254 ? 61.644  112.814 34.090  1.00 22.98  ? 254 SER D CB  1 
ATOM   12509 O  OG  . SER D  1 254 ? 61.485  111.474 34.508  1.00 32.88  ? 254 SER D OG  1 
ATOM   12510 N  N   . ALA D  1 255 ? 63.817  114.047 32.334  1.00 26.31  ? 255 ALA D N   1 
ATOM   12511 C  CA  . ALA D  1 255 ? 64.400  114.994 31.373  1.00 23.11  ? 255 ALA D CA  1 
ATOM   12512 C  C   . ALA D  1 255 ? 63.385  115.711 30.443  1.00 29.63  ? 255 ALA D C   1 
ATOM   12513 O  O   . ALA D  1 255 ? 62.391  115.113 29.979  1.00 32.34  ? 255 ALA D O   1 
ATOM   12514 C  CB  . ALA D  1 255 ? 65.445  114.300 30.535  1.00 18.53  ? 255 ALA D CB  1 
ATOM   12515 N  N   . TYR D  1 256 ? 63.658  116.978 30.117  1.00 30.45  ? 256 TYR D N   1 
ATOM   12516 C  CA  . TYR D  1 256 ? 62.752  117.717 29.258  1.00 28.69  ? 256 TYR D CA  1 
ATOM   12517 C  C   . TYR D  1 256 ? 63.449  118.404 28.122  1.00 31.31  ? 256 TYR D C   1 
ATOM   12518 O  O   . TYR D  1 256 ? 62.848  119.225 27.444  1.00 29.41  ? 256 TYR D O   1 
ATOM   12519 C  CB  . TYR D  1 256 ? 61.940  118.723 30.053  1.00 26.63  ? 256 TYR D CB  1 
ATOM   12520 C  CG  . TYR D  1 256 ? 62.631  119.271 31.277  1.00 30.11  ? 256 TYR D CG  1 
ATOM   12521 C  CD1 . TYR D  1 256 ? 63.611  120.254 31.180  1.00 29.79  ? 256 TYR D CD1 1 
ATOM   12522 C  CD2 . TYR D  1 256 ? 62.253  118.840 32.548  1.00 37.55  ? 256 TYR D CD2 1 
ATOM   12523 C  CE1 . TYR D  1 256 ? 64.203  120.807 32.334  1.00 36.07  ? 256 TYR D CE1 1 
ATOM   12524 C  CE2 . TYR D  1 256 ? 62.835  119.375 33.703  1.00 41.85  ? 256 TYR D CE2 1 
ATOM   12525 C  CZ  . TYR D  1 256 ? 63.813  120.360 33.598  1.00 39.77  ? 256 TYR D CZ  1 
ATOM   12526 O  OH  . TYR D  1 256 ? 64.391  120.815 34.777  1.00 34.63  ? 256 TYR D OH  1 
ATOM   12527 N  N   . GLY D  1 257 ? 64.715  118.062 27.902  1.00 31.73  ? 257 GLY D N   1 
ATOM   12528 C  CA  . GLY D  1 257 ? 65.441  118.672 26.800  1.00 30.81  ? 257 GLY D CA  1 
ATOM   12529 C  C   . GLY D  1 257 ? 64.646  118.543 25.516  1.00 31.19  ? 257 GLY D C   1 
ATOM   12530 O  O   . GLY D  1 257 ? 63.664  117.825 25.436  1.00 29.71  ? 257 GLY D O   1 
ATOM   12531 N  N   . ARG D  1 258 ? 65.077  119.218 24.480  1.00 36.00  ? 258 ARG D N   1 
ATOM   12532 C  CA  . ARG D  1 258 ? 64.357  119.158 23.242  1.00 37.36  ? 258 ARG D CA  1 
ATOM   12533 C  C   . ARG D  1 258 ? 64.669  117.836 22.572  1.00 36.54  ? 258 ARG D C   1 
ATOM   12534 O  O   . ARG D  1 258 ? 65.818  117.486 22.349  1.00 34.07  ? 258 ARG D O   1 
ATOM   12535 C  CB  . ARG D  1 258 ? 64.794  120.319 22.364  1.00 44.18  ? 258 ARG D CB  1 
ATOM   12536 C  CG  . ARG D  1 258 ? 64.120  120.406 21.017  1.00 49.34  ? 258 ARG D CG  1 
ATOM   12537 C  CD  . ARG D  1 258 ? 65.074  121.086 20.037  1.00 53.85  ? 258 ARG D CD  1 
ATOM   12538 N  NE  . ARG D  1 258 ? 64.609  121.119 18.659  1.00 61.51  ? 258 ARG D NE  1 
ATOM   12539 C  CZ  . ARG D  1 258 ? 63.390  121.486 18.286  1.00 65.98  ? 258 ARG D CZ  1 
ATOM   12540 N  NH1 . ARG D  1 258 ? 62.478  121.855 19.179  1.00 67.50  ? 258 ARG D NH1 1 
ATOM   12541 N  NH2 . ARG D  1 258 ? 63.092  121.490 17.002  1.00 70.35  ? 258 ARG D NH2 1 
ATOM   12542 N  N   . GLY D  1 259 ? 63.623  117.091 22.256  1.00 39.42  ? 259 GLY D N   1 
ATOM   12543 C  CA  . GLY D  1 259 ? 63.822  115.813 21.588  1.00 40.84  ? 259 GLY D CA  1 
ATOM   12544 C  C   . GLY D  1 259 ? 63.677  114.614 22.509  1.00 38.59  ? 259 GLY D C   1 
ATOM   12545 O  O   . GLY D  1 259 ? 63.466  113.491 22.073  1.00 40.22  ? 259 GLY D O   1 
ATOM   12546 N  N   . THR D  1 260 ? 63.827  114.849 23.799  1.00 36.23  ? 260 THR D N   1 
ATOM   12547 C  CA  . THR D  1 260 ? 63.689  113.801 24.777  1.00 31.98  ? 260 THR D CA  1 
ATOM   12548 C  C   . THR D  1 260 ? 62.239  113.292 24.811  1.00 28.23  ? 260 THR D C   1 
ATOM   12549 O  O   . THR D  1 260 ? 61.293  114.006 24.452  1.00 27.26  ? 260 THR D O   1 
ATOM   12550 C  CB  . THR D  1 260 ? 64.023  114.363 26.128  1.00 31.35  ? 260 THR D CB  1 
ATOM   12551 O  OG1 . THR D  1 260 ? 63.109  115.440 26.410  1.00 31.73  ? 260 THR D OG1 1 
ATOM   12552 C  CG2 . THR D  1 260 ? 65.452  114.840 26.126  1.00 22.73  ? 260 THR D CG2 1 
ATOM   12553 N  N   . PRO D  1 261 ? 62.047  112.088 25.352  1.00 22.86  ? 261 PRO D N   1 
ATOM   12554 C  CA  . PRO D  1 261 ? 60.689  111.580 25.393  1.00 20.69  ? 261 PRO D CA  1 
ATOM   12555 C  C   . PRO D  1 261 ? 59.688  112.475 26.098  1.00 25.35  ? 261 PRO D C   1 
ATOM   12556 O  O   . PRO D  1 261 ? 58.572  112.660 25.579  1.00 29.73  ? 261 PRO D O   1 
ATOM   12557 C  CB  . PRO D  1 261 ? 60.847  110.255 26.112  1.00 14.83  ? 261 PRO D CB  1 
ATOM   12558 C  CG  . PRO D  1 261 ? 62.220  109.844 25.740  1.00 21.33  ? 261 PRO D CG  1 
ATOM   12559 C  CD  . PRO D  1 261 ? 63.000  111.099 25.885  1.00 18.89  ? 261 PRO D CD  1 
ATOM   12560 N  N   . GLN D  1 262 ? 60.052  113.075 27.234  1.00 22.05  ? 262 GLN D N   1 
ATOM   12561 C  CA  . GLN D  1 262 ? 59.027  113.874 27.930  1.00 23.46  ? 262 GLN D CA  1 
ATOM   12562 C  C   . GLN D  1 262 ? 58.646  115.112 27.126  1.00 24.06  ? 262 GLN D C   1 
ATOM   12563 O  O   . GLN D  1 262 ? 57.468  115.494 27.030  1.00 23.61  ? 262 GLN D O   1 
ATOM   12564 C  CB  . GLN D  1 262 ? 59.470  114.290 29.338  1.00 25.84  ? 262 GLN D CB  1 
ATOM   12565 C  CG  . GLN D  1 262 ? 58.331  114.923 30.183  1.00 21.28  ? 262 GLN D CG  1 
ATOM   12566 C  CD  . GLN D  1 262 ? 58.753  115.428 31.578  1.00 26.65  ? 262 GLN D CD  1 
ATOM   12567 O  OE1 . GLN D  1 262 ? 57.888  115.713 32.428  1.00 28.26  ? 262 GLN D OE1 1 
ATOM   12568 N  NE2 . GLN D  1 262 ? 60.063  115.556 31.821  1.00 21.88  ? 262 GLN D NE2 1 
ATOM   12569 N  N   . TYR D  1 263 ? 59.666  115.733 26.552  1.00 22.69  ? 263 TYR D N   1 
ATOM   12570 C  CA  . TYR D  1 263 ? 59.453  116.918 25.772  1.00 21.38  ? 263 TYR D CA  1 
ATOM   12571 C  C   . TYR D  1 263 ? 58.529  116.568 24.595  1.00 24.03  ? 263 TYR D C   1 
ATOM   12572 O  O   . TYR D  1 263 ? 57.479  117.168 24.382  1.00 27.59  ? 263 TYR D O   1 
ATOM   12573 C  CB  . TYR D  1 263 ? 60.793  117.390 25.308  1.00 22.75  ? 263 TYR D CB  1 
ATOM   12574 C  CG  . TYR D  1 263 ? 60.725  118.581 24.435  1.00 34.73  ? 263 TYR D CG  1 
ATOM   12575 C  CD1 . TYR D  1 263 ? 60.284  118.488 23.128  1.00 35.82  ? 263 TYR D CD1 1 
ATOM   12576 C  CD2 . TYR D  1 263 ? 61.160  119.806 24.892  1.00 40.17  ? 263 TYR D CD2 1 
ATOM   12577 C  CE1 . TYR D  1 263 ? 60.291  119.598 22.306  1.00 39.41  ? 263 TYR D CE1 1 
ATOM   12578 C  CE2 . TYR D  1 263 ? 61.167  120.924 24.074  1.00 36.48  ? 263 TYR D CE2 1 
ATOM   12579 C  CZ  . TYR D  1 263 ? 60.745  120.812 22.798  1.00 37.55  ? 263 TYR D CZ  1 
ATOM   12580 O  OH  . TYR D  1 263 ? 60.834  121.911 22.008  1.00 45.60  ? 263 TYR D OH  1 
ATOM   12581 N  N   . THR D  1 264 ? 58.914  115.561 23.843  1.00 24.14  ? 264 THR D N   1 
ATOM   12582 C  CA  . THR D  1 264 ? 58.135  115.096 22.721  1.00 20.56  ? 264 THR D CA  1 
ATOM   12583 C  C   . THR D  1 264 ? 56.694  114.731 23.089  1.00 19.88  ? 264 THR D C   1 
ATOM   12584 O  O   . THR D  1 264 ? 55.746  115.051 22.393  1.00 24.40  ? 264 THR D O   1 
ATOM   12585 C  CB  . THR D  1 264 ? 58.766  113.856 22.173  1.00 17.82  ? 264 THR D CB  1 
ATOM   12586 O  OG1 . THR D  1 264 ? 60.057  114.180 21.642  1.00 33.55  ? 264 THR D OG1 1 
ATOM   12587 C  CG2 . THR D  1 264 ? 57.925  113.321 21.097  1.00 23.02  ? 264 THR D CG2 1 
ATOM   12588 N  N   . TRP D  1 265 ? 56.518  114.048 24.193  1.00 18.57  ? 265 TRP D N   1 
ATOM   12589 C  CA  . TRP D  1 265 ? 55.183  113.665 24.587  1.00 20.41  ? 265 TRP D CA  1 
ATOM   12590 C  C   . TRP D  1 265 ? 54.301  114.867 24.852  1.00 26.66  ? 265 TRP D C   1 
ATOM   12591 O  O   . TRP D  1 265 ? 53.210  114.966 24.306  1.00 28.66  ? 265 TRP D O   1 
ATOM   12592 C  CB  . TRP D  1 265 ? 55.250  112.828 25.844  1.00 19.31  ? 265 TRP D CB  1 
ATOM   12593 C  CG  . TRP D  1 265 ? 53.922  112.428 26.318  1.00 17.44  ? 265 TRP D CG  1 
ATOM   12594 C  CD1 . TRP D  1 265 ? 53.113  111.457 25.786  1.00 20.46  ? 265 TRP D CD1 1 
ATOM   12595 C  CD2 . TRP D  1 265 ? 53.193  113.019 27.400  1.00 18.08  ? 265 TRP D CD2 1 
ATOM   12596 N  NE1 . TRP D  1 265 ? 51.903  111.420 26.473  1.00 28.20  ? 265 TRP D NE1 1 
ATOM   12597 C  CE2 . TRP D  1 265 ? 51.932  112.373 27.462  1.00 21.83  ? 265 TRP D CE2 1 
ATOM   12598 C  CE3 . TRP D  1 265 ? 53.479  114.027 28.310  1.00 19.18  ? 265 TRP D CE3 1 
ATOM   12599 C  CZ2 . TRP D  1 265 ? 50.968  112.721 28.405  1.00 22.45  ? 265 TRP D CZ2 1 
ATOM   12600 C  CZ3 . TRP D  1 265 ? 52.515  114.364 29.247  1.00 23.45  ? 265 TRP D CZ3 1 
ATOM   12601 C  CH2 . TRP D  1 265 ? 51.278  113.716 29.285  1.00 23.81  ? 265 TRP D CH2 1 
ATOM   12602 N  N   . LEU D  1 266 ? 54.765  115.750 25.733  1.00 31.74  ? 266 LEU D N   1 
ATOM   12603 C  CA  . LEU D  1 266 ? 54.014  116.951 26.099  1.00 31.90  ? 266 LEU D CA  1 
ATOM   12604 C  C   . LEU D  1 266 ? 53.587  117.765 24.906  1.00 33.68  ? 266 LEU D C   1 
ATOM   12605 O  O   . LEU D  1 266 ? 52.473  118.280 24.854  1.00 33.88  ? 266 LEU D O   1 
ATOM   12606 C  CB  . LEU D  1 266 ? 54.836  117.843 27.007  1.00 26.21  ? 266 LEU D CB  1 
ATOM   12607 C  CG  . LEU D  1 266 ? 54.158  119.142 27.443  1.00 19.26  ? 266 LEU D CG  1 
ATOM   12608 C  CD1 . LEU D  1 266 ? 52.787  118.899 28.072  1.00 12.35  ? 266 LEU D CD1 1 
ATOM   12609 C  CD2 . LEU D  1 266 ? 55.094  119.824 28.407  1.00 19.82  ? 266 LEU D CD2 1 
ATOM   12610 N  N   . LYS D  1 267 ? 54.482  117.892 23.942  1.00 35.57  ? 267 LYS D N   1 
ATOM   12611 C  CA  . LYS D  1 267 ? 54.181  118.653 22.756  1.00 32.61  ? 267 LYS D CA  1 
ATOM   12612 C  C   . LYS D  1 267 ? 52.977  118.074 22.083  1.00 33.80  ? 267 LYS D C   1 
ATOM   12613 O  O   . LYS D  1 267 ? 51.980  118.764 21.913  1.00 40.97  ? 267 LYS D O   1 
ATOM   12614 C  CB  . LYS D  1 267 ? 55.360  118.680 21.823  1.00 33.45  ? 267 LYS D CB  1 
ATOM   12615 C  CG  . LYS D  1 267 ? 55.331  119.837 20.847  1.00 46.05  ? 267 LYS D CG  1 
ATOM   12616 C  CD  . LYS D  1 267 ? 56.586  119.835 19.988  1.00 57.39  ? 267 LYS D CD  1 
ATOM   12617 C  CE  . LYS D  1 267 ? 56.518  120.836 18.850  1.00 66.48  ? 267 LYS D CE  1 
ATOM   12618 N  NZ  . LYS D  1 267 ? 57.717  120.707 17.954  1.00 77.32  ? 267 LYS D NZ  1 
ATOM   12619 N  N   . LYS D  1 268 ? 52.998  116.795 21.753  1.00 32.35  ? 268 LYS D N   1 
ATOM   12620 C  CA  . LYS D  1 268 ? 51.808  116.219 21.118  1.00 30.48  ? 268 LYS D CA  1 
ATOM   12621 C  C   . LYS D  1 268 ? 50.607  116.236 22.024  1.00 27.39  ? 268 LYS D C   1 
ATOM   12622 O  O   . LYS D  1 268 ? 49.511  116.515 21.585  1.00 30.78  ? 268 LYS D O   1 
ATOM   12623 C  CB  . LYS D  1 268 ? 52.048  114.800 20.652  1.00 33.60  ? 268 LYS D CB  1 
ATOM   12624 C  CG  . LYS D  1 268 ? 53.160  114.707 19.611  1.00 54.30  ? 268 LYS D CG  1 
ATOM   12625 C  CD  . LYS D  1 268 ? 53.485  113.256 19.207  1.00 71.60  ? 268 LYS D CD  1 
ATOM   12626 C  CE  . LYS D  1 268 ? 54.681  113.169 18.209  1.00 82.43  ? 268 LYS D CE  1 
ATOM   12627 N  NZ  . LYS D  1 268 ? 55.219  111.754 17.959  1.00 91.64  ? 268 LYS D NZ  1 
ATOM   12628 N  N   . GLU D  1 269 ? 50.807  116.009 23.310  1.00 24.77  ? 269 GLU D N   1 
ATOM   12629 C  CA  . GLU D  1 269 ? 49.671  115.969 24.188  1.00 23.72  ? 269 GLU D CA  1 
ATOM   12630 C  C   . GLU D  1 269 ? 48.914  117.268 24.226  1.00 26.37  ? 269 GLU D C   1 
ATOM   12631 O  O   . GLU D  1 269 ? 47.691  117.266 24.194  1.00 27.24  ? 269 GLU D O   1 
ATOM   12632 C  CB  . GLU D  1 269 ? 50.064  115.543 25.579  1.00 20.02  ? 269 GLU D CB  1 
ATOM   12633 C  CG  . GLU D  1 269 ? 48.869  115.490 26.513  1.00 22.93  ? 269 GLU D CG  1 
ATOM   12634 C  CD  . GLU D  1 269 ? 47.940  114.349 26.240  1.00 25.99  ? 269 GLU D CD  1 
ATOM   12635 O  OE1 . GLU D  1 269 ? 48.290  113.459 25.430  1.00 34.92  ? 269 GLU D OE1 1 
ATOM   12636 O  OE2 . GLU D  1 269 ? 46.855  114.327 26.859  1.00 25.00  ? 269 GLU D OE2 1 
ATOM   12637 N  N   . LEU D  1 270 ? 49.627  118.382 24.258  1.00 28.63  ? 270 LEU D N   1 
ATOM   12638 C  CA  . LEU D  1 270 ? 48.954  119.667 24.321  1.00 30.21  ? 270 LEU D CA  1 
ATOM   12639 C  C   . LEU D  1 270 ? 48.065  119.821 23.093  1.00 36.05  ? 270 LEU D C   1 
ATOM   12640 O  O   . LEU D  1 270 ? 46.966  120.351 23.157  1.00 41.44  ? 270 LEU D O   1 
ATOM   12641 C  CB  . LEU D  1 270 ? 49.966  120.785 24.437  1.00 21.35  ? 270 LEU D CB  1 
ATOM   12642 C  CG  . LEU D  1 270 ? 50.441  120.923 25.881  1.00 21.67  ? 270 LEU D CG  1 
ATOM   12643 C  CD1 . LEU D  1 270 ? 51.639  121.870 25.926  1.00 12.75  ? 270 LEU D CD1 1 
ATOM   12644 C  CD2 . LEU D  1 270 ? 49.277  121.403 26.803  1.00 6.99   ? 270 LEU D CD2 1 
ATOM   12645 N  N   . ARG D  1 271 ? 48.500  119.266 21.981  1.00 38.88  ? 271 ARG D N   1 
ATOM   12646 C  CA  . ARG D  1 271 ? 47.662  119.315 20.797  1.00 42.43  ? 271 ARG D CA  1 
ATOM   12647 C  C   . ARG D  1 271 ? 46.434  118.403 20.920  1.00 40.55  ? 271 ARG D C   1 
ATOM   12648 O  O   . ARG D  1 271 ? 45.457  118.624 20.245  1.00 48.70  ? 271 ARG D O   1 
ATOM   12649 C  CB  . ARG D  1 271 ? 48.419  118.858 19.544  1.00 47.35  ? 271 ARG D CB  1 
ATOM   12650 C  CG  . ARG D  1 271 ? 49.681  119.616 19.191  1.00 60.99  ? 271 ARG D CG  1 
ATOM   12651 C  CD  . ARG D  1 271 ? 50.113  119.237 17.780  1.00 67.31  ? 271 ARG D CD  1 
ATOM   12652 N  NE  . ARG D  1 271 ? 51.540  119.423 17.535  1.00 81.57  ? 271 ARG D NE  1 
ATOM   12653 C  CZ  . ARG D  1 271 ? 52.353  118.451 17.111  1.00 89.70  ? 271 ARG D CZ  1 
ATOM   12654 N  NH1 . ARG D  1 271 ? 51.871  117.222 16.895  1.00 92.87  ? 271 ARG D NH1 1 
ATOM   12655 N  NH2 . ARG D  1 271 ? 53.650  118.702 16.889  1.00 96.97  ? 271 ARG D NH2 1 
ATOM   12656 N  N   . LYS D  1 272 ? 46.478  117.348 21.715  1.00 35.71  ? 272 LYS D N   1 
ATOM   12657 C  CA  . LYS D  1 272 ? 45.324  116.480 21.768  1.00 33.26  ? 272 LYS D CA  1 
ATOM   12658 C  C   . LYS D  1 272 ? 44.225  116.983 22.692  1.00 30.55  ? 272 LYS D C   1 
ATOM   12659 O  O   . LYS D  1 272 ? 43.179  116.342 22.843  1.00 31.16  ? 272 LYS D O   1 
ATOM   12660 C  CB  . LYS D  1 272 ? 45.736  115.071 22.193  1.00 38.69  ? 272 LYS D CB  1 
ATOM   12661 C  CG  . LYS D  1 272 ? 46.867  114.390 21.406  1.00 42.48  ? 272 LYS D CG  1 
ATOM   12662 C  CD  . LYS D  1 272 ? 46.881  112.870 21.746  1.00 47.51  ? 272 LYS D CD  1 
ATOM   12663 C  CE  . LYS D  1 272 ? 48.240  112.156 21.647  1.00 54.73  ? 272 LYS D CE  1 
ATOM   12664 N  NZ  . LYS D  1 272 ? 49.027  112.031 22.983  1.00 64.63  ? 272 LYS D NZ  1 
ATOM   12665 N  N   . VAL D  1 273 ? 44.471  118.100 23.359  1.00 33.21  ? 273 VAL D N   1 
ATOM   12666 C  CA  . VAL D  1 273 ? 43.477  118.634 24.296  1.00 38.62  ? 273 VAL D CA  1 
ATOM   12667 C  C   . VAL D  1 273 ? 42.307  119.260 23.571  1.00 39.48  ? 273 VAL D C   1 
ATOM   12668 O  O   . VAL D  1 273 ? 42.523  120.100 22.728  1.00 45.51  ? 273 VAL D O   1 
ATOM   12669 C  CB  . VAL D  1 273 ? 44.078  119.714 25.177  1.00 35.78  ? 273 VAL D CB  1 
ATOM   12670 C  CG1 . VAL D  1 273 ? 43.052  120.162 26.181  1.00 35.31  ? 273 VAL D CG1 1 
ATOM   12671 C  CG2 . VAL D  1 273 ? 45.319  119.203 25.876  1.00 35.31  ? 273 VAL D CG2 1 
ATOM   12672 N  N   . LYS D  1 274 ? 41.082  118.904 23.915  1.00 39.00  ? 274 LYS D N   1 
ATOM   12673 C  CA  . LYS D  1 274 ? 39.932  119.491 23.243  1.00 42.48  ? 274 LYS D CA  1 
ATOM   12674 C  C   . LYS D  1 274 ? 39.143  120.189 24.300  1.00 42.51  ? 274 LYS D C   1 
ATOM   12675 O  O   . LYS D  1 274 ? 38.542  119.527 25.129  1.00 47.22  ? 274 LYS D O   1 
ATOM   12676 C  CB  . LYS D  1 274 ? 39.074  118.405 22.620  1.00 45.83  ? 274 LYS D CB  1 
ATOM   12677 C  CG  . LYS D  1 274 ? 39.624  117.861 21.327  1.00 57.06  ? 274 LYS D CG  1 
ATOM   12678 C  CD  . LYS D  1 274 ? 38.972  116.517 20.933  1.00 70.73  ? 274 LYS D CD  1 
ATOM   12679 C  CE  . LYS D  1 274 ? 37.428  116.584 20.805  1.00 80.14  ? 274 LYS D CE  1 
ATOM   12680 N  NZ  . LYS D  1 274 ? 36.746  115.279 20.413  1.00 88.72  ? 274 LYS D NZ  1 
ATOM   12681 N  N   . ARG D  1 275 ? 39.094  121.510 24.273  1.00 38.59  ? 275 ARG D N   1 
ATOM   12682 C  CA  . ARG D  1 275 ? 38.363  122.240 25.320  1.00 38.54  ? 275 ARG D CA  1 
ATOM   12683 C  C   . ARG D  1 275 ? 36.841  122.263 25.205  1.00 41.49  ? 275 ARG D C   1 
ATOM   12684 O  O   . ARG D  1 275 ? 36.120  122.737 26.112  1.00 41.40  ? 275 ARG D O   1 
ATOM   12685 C  CB  . ARG D  1 275 ? 38.871  123.647 25.401  1.00 35.20  ? 275 ARG D CB  1 
ATOM   12686 C  CG  . ARG D  1 275 ? 40.310  123.715 25.722  1.00 30.88  ? 275 ARG D CG  1 
ATOM   12687 C  CD  . ARG D  1 275 ? 40.541  123.824 27.200  1.00 29.10  ? 275 ARG D CD  1 
ATOM   12688 N  NE  . ARG D  1 275 ? 41.737  124.626 27.354  1.00 28.54  ? 275 ARG D NE  1 
ATOM   12689 C  CZ  . ARG D  1 275 ? 41.962  125.465 28.346  1.00 32.94  ? 275 ARG D CZ  1 
ATOM   12690 N  NH1 . ARG D  1 275 ? 41.084  125.625 29.333  1.00 30.97  ? 275 ARG D NH1 1 
ATOM   12691 N  NH2 . ARG D  1 275 ? 43.021  126.247 28.263  1.00 33.09  ? 275 ARG D NH2 1 
ATOM   12692 N  N   . SER D  1 276 ? 36.368  121.845 24.041  1.00 43.49  ? 276 SER D N   1 
ATOM   12693 C  CA  . SER D  1 276 ? 34.949  121.733 23.797  1.00 46.41  ? 276 SER D CA  1 
ATOM   12694 C  C   . SER D  1 276 ? 34.518  120.493 24.554  1.00 48.17  ? 276 SER D C   1 
ATOM   12695 O  O   . SER D  1 276 ? 33.344  120.303 24.802  1.00 50.42  ? 276 SER D O   1 
ATOM   12696 C  CB  . SER D  1 276 ? 34.716  121.516 22.314  1.00 50.65  ? 276 SER D CB  1 
ATOM   12697 O  OG  . SER D  1 276 ? 35.960  121.293 21.647  1.00 54.01  ? 276 SER D OG  1 
ATOM   12698 N  N   . GLU D  1 277 ? 35.493  119.644 24.896  1.00 51.41  ? 277 GLU D N   1 
ATOM   12699 C  CA  . GLU D  1 277 ? 35.262  118.394 25.612  1.00 50.74  ? 277 GLU D CA  1 
ATOM   12700 C  C   . GLU D  1 277 ? 35.571  118.514 27.098  1.00 44.86  ? 277 GLU D C   1 
ATOM   12701 O  O   . GLU D  1 277 ? 34.747  118.181 27.943  1.00 42.18  ? 277 GLU D O   1 
ATOM   12702 C  CB  . GLU D  1 277 ? 36.098  117.287 24.970  1.00 63.16  ? 277 GLU D CB  1 
ATOM   12703 C  CG  . GLU D  1 277 ? 35.850  115.887 25.525  1.00 79.27  ? 277 GLU D CG  1 
ATOM   12704 C  CD  . GLU D  1 277 ? 36.439  114.786 24.638  1.00 89.43  ? 277 GLU D CD  1 
ATOM   12705 O  OE1 . GLU D  1 277 ? 36.229  114.834 23.397  1.00 91.53  ? 277 GLU D OE1 1 
ATOM   12706 O  OE2 . GLU D  1 277 ? 37.089  113.866 25.196  1.00 94.70  ? 277 GLU D OE2 1 
ATOM   12707 N  N   . THR D  1 278 ? 36.782  118.931 27.418  1.00 39.63  ? 278 THR D N   1 
ATOM   12708 C  CA  . THR D  1 278 ? 37.178  119.104 28.807  1.00 37.86  ? 278 THR D CA  1 
ATOM   12709 C  C   . THR D  1 278 ? 37.635  120.526 28.859  1.00 35.05  ? 278 THR D C   1 
ATOM   12710 O  O   . THR D  1 278 ? 38.741  120.854 28.433  1.00 39.36  ? 278 THR D O   1 
ATOM   12711 C  CB  . THR D  1 278 ? 38.320  118.155 29.218  1.00 36.82  ? 278 THR D CB  1 
ATOM   12712 O  OG1 . THR D  1 278 ? 39.379  118.186 28.238  1.00 37.40  ? 278 THR D OG1 1 
ATOM   12713 C  CG2 . THR D  1 278 ? 37.774  116.760 29.369  1.00 39.28  ? 278 THR D CG2 1 
ATOM   12714 N  N   . PRO D  1 279 ? 36.756  121.412 29.302  1.00 31.25  ? 279 PRO D N   1 
ATOM   12715 C  CA  . PRO D  1 279 ? 37.055  122.835 29.391  1.00 25.50  ? 279 PRO D CA  1 
ATOM   12716 C  C   . PRO D  1 279 ? 38.247  123.172 30.247  1.00 26.31  ? 279 PRO D C   1 
ATOM   12717 O  O   . PRO D  1 279 ? 39.090  123.988 29.876  1.00 23.96  ? 279 PRO D O   1 
ATOM   12718 C  CB  . PRO D  1 279 ? 35.757  123.401 29.948  1.00 29.20  ? 279 PRO D CB  1 
ATOM   12719 C  CG  . PRO D  1 279 ? 35.145  122.230 30.682  1.00 31.17  ? 279 PRO D CG  1 
ATOM   12720 C  CD  . PRO D  1 279 ? 35.390  121.115 29.754  1.00 30.85  ? 279 PRO D CD  1 
ATOM   12721 N  N   . TRP D  1 280 ? 38.367  122.485 31.370  1.00 28.59  ? 280 TRP D N   1 
ATOM   12722 C  CA  . TRP D  1 280 ? 39.452  122.768 32.303  1.00 29.71  ? 280 TRP D CA  1 
ATOM   12723 C  C   . TRP D  1 280 ? 40.748  122.061 32.074  1.00 27.51  ? 280 TRP D C   1 
ATOM   12724 O  O   . TRP D  1 280 ? 40.812  120.834 32.126  1.00 29.09  ? 280 TRP D O   1 
ATOM   12725 C  CB  . TRP D  1 280 ? 38.954  122.490 33.677  1.00 31.41  ? 280 TRP D CB  1 
ATOM   12726 C  CG  . TRP D  1 280 ? 37.847  123.421 33.989  1.00 38.74  ? 280 TRP D CG  1 
ATOM   12727 C  CD1 . TRP D  1 280 ? 36.496  123.160 33.953  1.00 35.41  ? 280 TRP D CD1 1 
ATOM   12728 C  CD2 . TRP D  1 280 ? 37.993  124.774 34.455  1.00 38.40  ? 280 TRP D CD2 1 
ATOM   12729 N  NE1 . TRP D  1 280 ? 35.801  124.271 34.391  1.00 35.69  ? 280 TRP D NE1 1 
ATOM   12730 C  CE2 . TRP D  1 280 ? 36.687  125.268 34.716  1.00 33.51  ? 280 TRP D CE2 1 
ATOM   12731 C  CE3 . TRP D  1 280 ? 39.108  125.610 34.688  1.00 36.21  ? 280 TRP D CE3 1 
ATOM   12732 C  CZ2 . TRP D  1 280 ? 36.462  126.551 35.209  1.00 34.94  ? 280 TRP D CZ2 1 
ATOM   12733 C  CZ3 . TRP D  1 280 ? 38.887  126.887 35.174  1.00 37.47  ? 280 TRP D CZ3 1 
ATOM   12734 C  CH2 . TRP D  1 280 ? 37.569  127.347 35.434  1.00 40.33  ? 280 TRP D CH2 1 
ATOM   12735 N  N   . LEU D  1 281 ? 41.799  122.830 31.861  1.00 26.01  ? 281 LEU D N   1 
ATOM   12736 C  CA  . LEU D  1 281 ? 43.097  122.258 31.600  1.00 24.01  ? 281 LEU D CA  1 
ATOM   12737 C  C   . LEU D  1 281 ? 43.991  122.547 32.798  1.00 28.55  ? 281 LEU D C   1 
ATOM   12738 O  O   . LEU D  1 281 ? 44.330  123.719 33.046  1.00 28.94  ? 281 LEU D O   1 
ATOM   12739 C  CB  . LEU D  1 281 ? 43.668  122.878 30.330  1.00 22.50  ? 281 LEU D CB  1 
ATOM   12740 C  CG  . LEU D  1 281 ? 45.082  122.472 29.922  1.00 29.74  ? 281 LEU D CG  1 
ATOM   12741 C  CD1 . LEU D  1 281 ? 45.108  120.997 29.569  1.00 37.36  ? 281 LEU D CD1 1 
ATOM   12742 C  CD2 . LEU D  1 281 ? 45.563  123.264 28.751  1.00 29.26  ? 281 LEU D CD2 1 
ATOM   12743 N  N   . ILE D  1 282 ? 44.408  121.475 33.490  1.00 27.76  ? 282 ILE D N   1 
ATOM   12744 C  CA  . ILE D  1 282 ? 45.251  121.506 34.690  1.00 23.34  ? 282 ILE D CA  1 
ATOM   12745 C  C   . ILE D  1 282 ? 46.567  120.814 34.500  1.00 24.49  ? 282 ILE D C   1 
ATOM   12746 O  O   . ILE D  1 282 ? 46.601  119.725 33.969  1.00 35.96  ? 282 ILE D O   1 
ATOM   12747 C  CB  . ILE D  1 282 ? 44.571  120.737 35.781  1.00 15.83  ? 282 ILE D CB  1 
ATOM   12748 C  CG1 . ILE D  1 282 ? 43.208  121.333 35.998  1.00 19.05  ? 282 ILE D CG1 1 
ATOM   12749 C  CG2 . ILE D  1 282 ? 45.361  120.803 37.062  1.00 21.52  ? 282 ILE D CG2 1 
ATOM   12750 C  CD1 . ILE D  1 282 ? 42.365  120.496 36.922  1.00 24.88  ? 282 ILE D CD1 1 
ATOM   12751 N  N   . VAL D  1 283 ? 47.638  121.374 35.034  1.00 24.85  ? 283 VAL D N   1 
ATOM   12752 C  CA  . VAL D  1 283 ? 48.960  120.760 34.941  1.00 22.74  ? 283 VAL D CA  1 
ATOM   12753 C  C   . VAL D  1 283 ? 49.537  120.559 36.323  1.00 24.72  ? 283 VAL D C   1 
ATOM   12754 O  O   . VAL D  1 283 ? 49.400  121.424 37.185  1.00 32.69  ? 283 VAL D O   1 
ATOM   12755 C  CB  . VAL D  1 283 ? 49.929  121.645 34.162  1.00 19.89  ? 283 VAL D CB  1 
ATOM   12756 C  CG1 . VAL D  1 283 ? 51.328  121.147 34.293  1.00 16.87  ? 283 VAL D CG1 1 
ATOM   12757 C  CG2 . VAL D  1 283 ? 49.536  121.660 32.683  1.00 23.55  ? 283 VAL D CG2 1 
ATOM   12758 N  N   . LEU D  1 284 ? 50.195  119.421 36.530  1.00 21.50  ? 284 LEU D N   1 
ATOM   12759 C  CA  . LEU D  1 284 ? 50.821  119.110 37.797  1.00 15.87  ? 284 LEU D CA  1 
ATOM   12760 C  C   . LEU D  1 284 ? 52.322  118.933 37.601  1.00 17.21  ? 284 LEU D C   1 
ATOM   12761 O  O   . LEU D  1 284 ? 52.755  118.423 36.571  1.00 19.22  ? 284 LEU D O   1 
ATOM   12762 C  CB  . LEU D  1 284 ? 50.285  117.817 38.356  1.00 10.32  ? 284 LEU D CB  1 
ATOM   12763 C  CG  . LEU D  1 284 ? 48.779  117.716 38.461  1.00 18.94  ? 284 LEU D CG  1 
ATOM   12764 C  CD1 . LEU D  1 284 ? 48.441  116.337 39.062  1.00 15.31  ? 284 LEU D CD1 1 
ATOM   12765 C  CD2 . LEU D  1 284 ? 48.168  118.868 39.252  1.00 13.42  ? 284 LEU D CD2 1 
ATOM   12766 N  N   . MET D  1 285 ? 53.118  119.382 38.564  1.00 13.24  ? 285 MET D N   1 
ATOM   12767 C  CA  . MET D  1 285 ? 54.567  119.196 38.548  1.00 14.95  ? 285 MET D CA  1 
ATOM   12768 C  C   . MET D  1 285 ? 55.028  119.397 39.968  1.00 23.56  ? 285 MET D C   1 
ATOM   12769 O  O   . MET D  1 285 ? 54.300  119.972 40.781  1.00 33.03  ? 285 MET D O   1 
ATOM   12770 C  CB  . MET D  1 285 ? 55.260  120.139 37.619  1.00 6.92   ? 285 MET D CB  1 
ATOM   12771 C  CG  . MET D  1 285 ? 54.826  121.567 37.824  1.00 25.93  ? 285 MET D CG  1 
ATOM   12772 S  SD  . MET D  1 285 ? 55.737  122.761 36.882  1.00 29.61  ? 285 MET D SD  1 
ATOM   12773 C  CE  . MET D  1 285 ? 54.853  122.709 35.303  1.00 27.18  ? 285 MET D CE  1 
ATOM   12774 N  N   . HIS D  1 286 ? 56.232  118.966 40.309  1.00 24.92  ? 286 HIS D N   1 
ATOM   12775 C  CA  . HIS D  1 286 ? 56.604  119.103 41.711  1.00 22.06  ? 286 HIS D CA  1 
ATOM   12776 C  C   . HIS D  1 286 ? 57.212  120.448 41.950  1.00 25.83  ? 286 HIS D C   1 
ATOM   12777 O  O   . HIS D  1 286 ? 56.725  121.200 42.800  1.00 28.27  ? 286 HIS D O   1 
ATOM   12778 C  CB  . HIS D  1 286 ? 57.568  118.001 42.143  1.00 17.97  ? 286 HIS D CB  1 
ATOM   12779 C  CG  . HIS D  1 286 ? 57.937  118.052 43.593  1.00 15.10  ? 286 HIS D CG  1 
ATOM   12780 N  ND1 . HIS D  1 286 ? 57.037  117.772 44.596  1.00 21.67  ? 286 HIS D ND1 1 
ATOM   12781 C  CD2 . HIS D  1 286 ? 59.123  118.274 44.203  1.00 20.48  ? 286 HIS D CD2 1 
ATOM   12782 C  CE1 . HIS D  1 286 ? 57.651  117.815 45.767  1.00 13.84  ? 286 HIS D CE1 1 
ATOM   12783 N  NE2 . HIS D  1 286 ? 58.917  118.121 45.554  1.00 19.05  ? 286 HIS D NE2 1 
ATOM   12784 N  N   . SER D  1 287 ? 58.282  120.744 41.206  1.00 28.26  ? 287 SER D N   1 
ATOM   12785 C  CA  . SER D  1 287 ? 59.018  122.003 41.358  1.00 29.26  ? 287 SER D CA  1 
ATOM   12786 C  C   . SER D  1 287 ? 58.267  123.075 40.648  1.00 36.67  ? 287 SER D C   1 
ATOM   12787 O  O   . SER D  1 287 ? 58.077  123.013 39.420  1.00 44.00  ? 287 SER D O   1 
ATOM   12788 C  CB  . SER D  1 287 ? 60.395  121.926 40.750  1.00 22.40  ? 287 SER D CB  1 
ATOM   12789 O  OG  . SER D  1 287 ? 61.276  122.724 41.488  1.00 35.03  ? 287 SER D OG  1 
ATOM   12790 N  N   . PRO D  1 288 ? 57.873  124.105 41.391  1.00 38.10  ? 288 PRO D N   1 
ATOM   12791 C  CA  . PRO D  1 288 ? 57.120  125.296 40.978  1.00 38.28  ? 288 PRO D CA  1 
ATOM   12792 C  C   . PRO D  1 288 ? 57.930  126.266 40.055  1.00 37.82  ? 288 PRO D C   1 
ATOM   12793 O  O   . PRO D  1 288 ? 59.131  126.544 40.319  1.00 40.74  ? 288 PRO D O   1 
ATOM   12794 C  CB  . PRO D  1 288 ? 56.766  125.900 42.325  1.00 38.10  ? 288 PRO D CB  1 
ATOM   12795 C  CG  . PRO D  1 288 ? 58.024  125.620 43.104  1.00 34.16  ? 288 PRO D CG  1 
ATOM   12796 C  CD  . PRO D  1 288 ? 58.364  124.231 42.773  1.00 35.30  ? 288 PRO D CD  1 
ATOM   12797 N  N   . LEU D  1 289 ? 57.291  126.740 38.973  1.00 35.50  ? 289 LEU D N   1 
ATOM   12798 C  CA  . LEU D  1 289 ? 57.932  127.638 37.975  1.00 34.36  ? 289 LEU D CA  1 
ATOM   12799 C  C   . LEU D  1 289 ? 58.060  129.082 38.470  1.00 32.16  ? 289 LEU D C   1 
ATOM   12800 O  O   . LEU D  1 289 ? 59.022  129.819 38.162  1.00 34.68  ? 289 LEU D O   1 
ATOM   12801 C  CB  . LEU D  1 289 ? 57.140  127.615 36.642  1.00 31.74  ? 289 LEU D CB  1 
ATOM   12802 C  CG  . LEU D  1 289 ? 57.062  126.283 35.889  1.00 27.61  ? 289 LEU D CG  1 
ATOM   12803 C  CD1 . LEU D  1 289 ? 56.490  126.506 34.509  1.00 23.97  ? 289 LEU D CD1 1 
ATOM   12804 C  CD2 . LEU D  1 289 ? 58.458  125.707 35.774  1.00 23.87  ? 289 LEU D CD2 1 
ATOM   12805 N  N   . TYR D  1 290 ? 57.044  129.447 39.245  1.00 33.56  ? 290 TYR D N   1 
ATOM   12806 C  CA  . TYR D  1 290 ? 56.847  130.755 39.886  1.00 31.39  ? 290 TYR D CA  1 
ATOM   12807 C  C   . TYR D  1 290 ? 56.805  130.495 41.409  1.00 28.46  ? 290 TYR D C   1 
ATOM   12808 O  O   . TYR D  1 290 ? 55.901  129.793 41.914  1.00 26.74  ? 290 TYR D O   1 
ATOM   12809 C  CB  . TYR D  1 290 ? 55.500  131.398 39.399  1.00 29.78  ? 290 TYR D CB  1 
ATOM   12810 C  CG  . TYR D  1 290 ? 55.638  132.072 38.049  1.00 34.22  ? 290 TYR D CG  1 
ATOM   12811 C  CD1 . TYR D  1 290 ? 56.314  133.310 37.934  1.00 31.53  ? 290 TYR D CD1 1 
ATOM   12812 C  CD2 . TYR D  1 290 ? 55.254  131.425 36.886  1.00 34.08  ? 290 TYR D CD2 1 
ATOM   12813 C  CE1 . TYR D  1 290 ? 56.624  133.882 36.706  1.00 27.63  ? 290 TYR D CE1 1 
ATOM   12814 C  CE2 . TYR D  1 290 ? 55.561  131.989 35.639  1.00 38.76  ? 290 TYR D CE2 1 
ATOM   12815 C  CZ  . TYR D  1 290 ? 56.253  133.216 35.568  1.00 37.23  ? 290 TYR D CZ  1 
ATOM   12816 O  OH  . TYR D  1 290 ? 56.621  133.756 34.367  1.00 42.91  ? 290 TYR D OH  1 
ATOM   12817 N  N   . ASN D  1 291 ? 57.823  130.995 42.118  1.00 27.32  ? 291 ASN D N   1 
ATOM   12818 C  CA  . ASN D  1 291 ? 57.903  130.844 43.558  1.00 28.77  ? 291 ASN D CA  1 
ATOM   12819 C  C   . ASN D  1 291 ? 58.740  131.970 44.177  1.00 33.41  ? 291 ASN D C   1 
ATOM   12820 O  O   . ASN D  1 291 ? 59.887  132.202 43.759  1.00 37.41  ? 291 ASN D O   1 
ATOM   12821 C  CB  . ASN D  1 291 ? 58.480  129.478 43.857  1.00 29.48  ? 291 ASN D CB  1 
ATOM   12822 C  CG  . ASN D  1 291 ? 59.146  129.391 45.197  1.00 36.81  ? 291 ASN D CG  1 
ATOM   12823 O  OD1 . ASN D  1 291 ? 60.327  129.036 45.278  1.00 41.95  ? 291 ASN D OD1 1 
ATOM   12824 N  ND2 . ASN D  1 291 ? 58.402  129.683 46.264  1.00 42.26  ? 291 ASN D ND2 1 
ATOM   12825 N  N   . SER D  1 292 ? 58.154  132.692 45.135  1.00 33.18  ? 292 SER D N   1 
ATOM   12826 C  CA  . SER D  1 292 ? 58.870  133.770 45.796  1.00 36.20  ? 292 SER D CA  1 
ATOM   12827 C  C   . SER D  1 292 ? 59.393  133.448 47.200  1.00 38.35  ? 292 SER D C   1 
ATOM   12828 O  O   . SER D  1 292 ? 59.529  134.367 48.012  1.00 42.35  ? 292 SER D O   1 
ATOM   12829 C  CB  . SER D  1 292 ? 57.981  134.991 45.866  1.00 32.31  ? 292 SER D CB  1 
ATOM   12830 O  OG  . SER D  1 292 ? 56.862  134.739 46.693  1.00 28.38  ? 292 SER D OG  1 
ATOM   12831 N  N   . TYR D  1 293 ? 59.572  132.169 47.543  1.00 36.10  ? 293 TYR D N   1 
ATOM   12832 C  CA  . TYR D  1 293 ? 60.126  131.833 48.852  1.00 32.46  ? 293 TYR D CA  1 
ATOM   12833 C  C   . TYR D  1 293 ? 61.567  131.631 48.630  1.00 34.72  ? 293 TYR D C   1 
ATOM   12834 O  O   . TYR D  1 293 ? 61.969  131.412 47.508  1.00 31.17  ? 293 TYR D O   1 
ATOM   12835 C  CB  . TYR D  1 293 ? 59.556  130.595 49.428  1.00 24.18  ? 293 TYR D CB  1 
ATOM   12836 C  CG  . TYR D  1 293 ? 58.195  130.822 49.951  1.00 20.33  ? 293 TYR D CG  1 
ATOM   12837 C  CD1 . TYR D  1 293 ? 57.127  130.974 49.097  1.00 21.73  ? 293 TYR D CD1 1 
ATOM   12838 C  CD2 . TYR D  1 293 ? 57.953  130.773 51.296  1.00 22.51  ? 293 TYR D CD2 1 
ATOM   12839 C  CE1 . TYR D  1 293 ? 55.810  131.051 49.574  1.00 26.31  ? 293 TYR D CE1 1 
ATOM   12840 C  CE2 . TYR D  1 293 ? 56.662  130.848 51.796  1.00 26.81  ? 293 TYR D CE2 1 
ATOM   12841 C  CZ  . TYR D  1 293 ? 55.591  130.979 50.929  1.00 28.07  ? 293 TYR D CZ  1 
ATOM   12842 O  OH  . TYR D  1 293 ? 54.309  130.993 51.436  1.00 31.71  ? 293 TYR D OH  1 
ATOM   12843 N  N   . ASN D  1 294 ? 62.355  131.677 49.695  1.00 42.75  ? 294 ASN D N   1 
ATOM   12844 C  CA  . ASN D  1 294 ? 63.803  131.548 49.539  1.00 50.57  ? 294 ASN D CA  1 
ATOM   12845 C  C   . ASN D  1 294 ? 64.214  130.128 49.294  1.00 49.36  ? 294 ASN D C   1 
ATOM   12846 O  O   . ASN D  1 294 ? 65.199  129.857 48.598  1.00 50.14  ? 294 ASN D O   1 
ATOM   12847 C  CB  . ASN D  1 294 ? 64.540  132.070 50.771  1.00 62.58  ? 294 ASN D CB  1 
ATOM   12848 C  CG  . ASN D  1 294 ? 64.471  133.590 50.907  1.00 75.63  ? 294 ASN D CG  1 
ATOM   12849 O  OD1 . ASN D  1 294 ? 65.406  134.315 50.522  1.00 83.49  ? 294 ASN D OD1 1 
ATOM   12850 N  ND2 . ASN D  1 294 ? 63.364  134.082 51.462  1.00 81.79  ? 294 ASN D ND2 1 
ATOM   12851 N  N   . HIS D  1 295 ? 63.501  129.226 49.946  1.00 47.84  ? 295 HIS D N   1 
ATOM   12852 C  CA  . HIS D  1 295 ? 63.766  127.810 49.814  1.00 45.85  ? 295 HIS D CA  1 
ATOM   12853 C  C   . HIS D  1 295 ? 63.387  127.361 48.428  1.00 46.57  ? 295 HIS D C   1 
ATOM   12854 O  O   . HIS D  1 295 ? 62.210  127.413 48.085  1.00 49.06  ? 295 HIS D O   1 
ATOM   12855 C  CB  . HIS D  1 295 ? 62.897  127.050 50.800  1.00 49.68  ? 295 HIS D CB  1 
ATOM   12856 C  CG  . HIS D  1 295 ? 63.270  125.607 50.939  1.00 53.63  ? 295 HIS D CG  1 
ATOM   12857 N  ND1 . HIS D  1 295 ? 62.338  124.619 51.172  1.00 55.66  ? 295 HIS D ND1 1 
ATOM   12858 C  CD2 . HIS D  1 295 ? 64.474  124.978 50.876  1.00 52.84  ? 295 HIS D CD2 1 
ATOM   12859 C  CE1 . HIS D  1 295 ? 62.946  123.447 51.250  1.00 54.16  ? 295 HIS D CE1 1 
ATOM   12860 N  NE2 . HIS D  1 295 ? 64.242  123.635 51.075  1.00 50.74  ? 295 HIS D NE2 1 
ATOM   12861 N  N   . HIS D  1 296 ? 64.355  126.846 47.667  1.00 46.69  ? 296 HIS D N   1 
ATOM   12862 C  CA  . HIS D  1 296 ? 64.121  126.371 46.285  1.00 41.85  ? 296 HIS D CA  1 
ATOM   12863 C  C   . HIS D  1 296 ? 63.777  127.503 45.373  1.00 41.59  ? 296 HIS D C   1 
ATOM   12864 O  O   . HIS D  1 296 ? 63.003  127.340 44.415  1.00 48.14  ? 296 HIS D O   1 
ATOM   12865 C  CB  . HIS D  1 296 ? 62.978  125.366 46.212  1.00 40.04  ? 296 HIS D CB  1 
ATOM   12866 C  CG  . HIS D  1 296 ? 63.238  124.125 46.987  1.00 35.28  ? 296 HIS D CG  1 
ATOM   12867 N  ND1 . HIS D  1 296 ? 64.447  123.460 46.942  1.00 27.74  ? 296 HIS D ND1 1 
ATOM   12868 C  CD2 . HIS D  1 296 ? 62.455  123.440 47.846  1.00 27.40  ? 296 HIS D CD2 1 
ATOM   12869 C  CE1 . HIS D  1 296 ? 64.392  122.415 47.740  1.00 31.67  ? 296 HIS D CE1 1 
ATOM   12870 N  NE2 . HIS D  1 296 ? 63.196  122.379 48.300  1.00 31.26  ? 296 HIS D NE2 1 
ATOM   12871 N  N   . PHE D  1 297 ? 64.369  128.649 45.656  1.00 41.00  ? 297 PHE D N   1 
ATOM   12872 C  CA  . PHE D  1 297 ? 64.088  129.810 44.866  1.00 40.72  ? 297 PHE D CA  1 
ATOM   12873 C  C   . PHE D  1 297 ? 64.783  129.599 43.538  1.00 39.09  ? 297 PHE D C   1 
ATOM   12874 O  O   . PHE D  1 297 ? 65.944  129.204 43.521  1.00 34.74  ? 297 PHE D O   1 
ATOM   12875 C  CB  . PHE D  1 297 ? 64.580  131.082 45.581  1.00 38.72  ? 297 PHE D CB  1 
ATOM   12876 C  CG  . PHE D  1 297 ? 64.434  132.335 44.754  1.00 37.32  ? 297 PHE D CG  1 
ATOM   12877 C  CD1 . PHE D  1 297 ? 63.158  132.800 44.362  1.00 38.47  ? 297 PHE D CD1 1 
ATOM   12878 C  CD2 . PHE D  1 297 ? 65.565  133.010 44.305  1.00 30.49  ? 297 PHE D CD2 1 
ATOM   12879 C  CE1 . PHE D  1 297 ? 63.018  133.902 43.532  1.00 30.30  ? 297 PHE D CE1 1 
ATOM   12880 C  CE2 . PHE D  1 297 ? 65.446  134.106 43.475  1.00 25.19  ? 297 PHE D CE2 1 
ATOM   12881 C  CZ  . PHE D  1 297 ? 64.165  134.557 43.083  1.00 28.76  ? 297 PHE D CZ  1 
ATOM   12882 N  N   . MET D  1 298 ? 64.012  129.711 42.449  1.00 43.06  ? 298 MET D N   1 
ATOM   12883 C  CA  . MET D  1 298 ? 64.500  129.595 41.056  1.00 44.31  ? 298 MET D CA  1 
ATOM   12884 C  C   . MET D  1 298 ? 64.945  128.210 40.501  1.00 45.07  ? 298 MET D C   1 
ATOM   12885 O  O   . MET D  1 298 ? 65.693  128.113 39.498  1.00 41.63  ? 298 MET D O   1 
ATOM   12886 C  CB  . MET D  1 298 ? 65.588  130.647 40.778  1.00 45.21  ? 298 MET D CB  1 
ATOM   12887 C  CG  . MET D  1 298 ? 65.129  132.104 40.748  1.00 40.06  ? 298 MET D CG  1 
ATOM   12888 S  SD  . MET D  1 298 ? 66.340  133.108 39.968  1.00 43.15  ? 298 MET D SD  1 
ATOM   12889 C  CE  . MET D  1 298 ? 67.745  133.059 41.086  1.00 40.76  ? 298 MET D CE  1 
ATOM   12890 N  N   . GLU D  1 299 ? 64.420  127.146 41.100  1.00 44.60  ? 299 GLU D N   1 
ATOM   12891 C  CA  . GLU D  1 299 ? 64.748  125.812 40.648  1.00 40.36  ? 299 GLU D CA  1 
ATOM   12892 C  C   . GLU D  1 299 ? 63.908  125.548 39.427  1.00 36.80  ? 299 GLU D C   1 
ATOM   12893 O  O   . GLU D  1 299 ? 64.370  124.925 38.471  1.00 39.58  ? 299 GLU D O   1 
ATOM   12894 C  CB  . GLU D  1 299 ? 64.494  124.775 41.762  1.00 43.61  ? 299 GLU D CB  1 
ATOM   12895 C  CG  . GLU D  1 299 ? 65.609  124.771 42.846  1.00 40.02  ? 299 GLU D CG  1 
ATOM   12896 C  CD  . GLU D  1 299 ? 65.468  123.696 43.911  1.00 38.47  ? 299 GLU D CD  1 
ATOM   12897 O  OE1 . GLU D  1 299 ? 64.618  122.779 43.711  1.00 35.06  ? 299 GLU D OE1 1 
ATOM   12898 O  OE2 . GLU D  1 299 ? 66.232  123.782 44.927  1.00 28.08  ? 299 GLU D OE2 1 
ATOM   12899 N  N   . GLY D  1 300 ? 62.694  126.094 39.429  1.00 34.46  ? 300 GLY D N   1 
ATOM   12900 C  CA  . GLY D  1 300 ? 61.791  125.910 38.308  1.00 31.03  ? 300 GLY D CA  1 
ATOM   12901 C  C   . GLY D  1 300 ? 62.227  126.644 37.051  1.00 33.24  ? 300 GLY D C   1 
ATOM   12902 O  O   . GLY D  1 300 ? 61.556  126.556 36.038  1.00 37.12  ? 300 GLY D O   1 
ATOM   12903 N  N   . GLU D  1 301 ? 63.368  127.315 37.081  1.00 27.37  ? 301 GLU D N   1 
ATOM   12904 C  CA  . GLU D  1 301 ? 63.779  128.074 35.936  1.00 29.55  ? 301 GLU D CA  1 
ATOM   12905 C  C   . GLU D  1 301 ? 63.948  127.246 34.725  1.00 32.04  ? 301 GLU D C   1 
ATOM   12906 O  O   . GLU D  1 301 ? 63.308  127.508 33.702  1.00 35.33  ? 301 GLU D O   1 
ATOM   12907 C  CB  . GLU D  1 301 ? 65.064  128.847 36.211  1.00 34.90  ? 301 GLU D CB  1 
ATOM   12908 C  CG  . GLU D  1 301 ? 64.862  130.092 37.090  1.00 33.29  ? 301 GLU D CG  1 
ATOM   12909 C  CD  . GLU D  1 301 ? 63.824  131.048 36.517  1.00 33.08  ? 301 GLU D CD  1 
ATOM   12910 O  OE1 . GLU D  1 301 ? 64.283  131.861 35.642  1.00 25.93  ? 301 GLU D OE1 1 
ATOM   12911 O  OE2 . GLU D  1 301 ? 62.590  130.943 36.917  1.00 28.73  ? 301 GLU D OE2 1 
ATOM   12912 N  N   . ALA D  1 302 ? 64.788  126.224 34.830  1.00 32.12  ? 302 ALA D N   1 
ATOM   12913 C  CA  . ALA D  1 302 ? 65.017  125.345 33.675  1.00 28.85  ? 302 ALA D CA  1 
ATOM   12914 C  C   . ALA D  1 302 ? 63.748  124.861 33.007  1.00 23.14  ? 302 ALA D C   1 
ATOM   12915 O  O   . ALA D  1 302 ? 63.537  125.102 31.831  1.00 26.26  ? 302 ALA D O   1 
ATOM   12916 C  CB  . ALA D  1 302 ? 65.850  124.194 34.044  1.00 32.14  ? 302 ALA D CB  1 
ATOM   12917 N  N   . MET D  1 303 ? 62.867  124.232 33.757  1.00 18.98  ? 303 MET D N   1 
ATOM   12918 C  CA  . MET D  1 303 ? 61.628  123.774 33.144  1.00 22.57  ? 303 MET D CA  1 
ATOM   12919 C  C   . MET D  1 303 ? 60.789  124.923 32.651  1.00 25.62  ? 303 MET D C   1 
ATOM   12920 O  O   . MET D  1 303 ? 60.067  124.783 31.674  1.00 32.49  ? 303 MET D O   1 
ATOM   12921 C  CB  . MET D  1 303 ? 60.786  122.901 34.072  1.00 23.44  ? 303 MET D CB  1 
ATOM   12922 C  CG  . MET D  1 303 ? 59.537  122.374 33.365  1.00 23.05  ? 303 MET D CG  1 
ATOM   12923 S  SD  . MET D  1 303 ? 58.923  120.794 34.004  1.00 27.01  ? 303 MET D SD  1 
ATOM   12924 C  CE  . MET D  1 303 ? 58.309  121.421 35.532  1.00 34.16  ? 303 MET D CE  1 
ATOM   12925 N  N   . ARG D  1 304 ? 60.872  126.063 33.320  1.00 32.06  ? 304 ARG D N   1 
ATOM   12926 C  CA  . ARG D  1 304 ? 60.102  127.231 32.902  1.00 35.74  ? 304 ARG D CA  1 
ATOM   12927 C  C   . ARG D  1 304 ? 60.521  127.652 31.519  1.00 34.93  ? 304 ARG D C   1 
ATOM   12928 O  O   . ARG D  1 304 ? 59.654  127.840 30.629  1.00 34.24  ? 304 ARG D O   1 
ATOM   12929 C  CB  . ARG D  1 304 ? 60.337  128.420 33.799  1.00 39.13  ? 304 ARG D CB  1 
ATOM   12930 C  CG  . ARG D  1 304 ? 59.142  129.355 33.774  1.00 42.67  ? 304 ARG D CG  1 
ATOM   12931 C  CD  . ARG D  1 304 ? 59.421  130.723 34.424  1.00 38.02  ? 304 ARG D CD  1 
ATOM   12932 N  NE  . ARG D  1 304 ? 60.007  131.616 33.447  1.00 32.30  ? 304 ARG D NE  1 
ATOM   12933 C  CZ  . ARG D  1 304 ? 61.201  132.153 33.592  1.00 32.59  ? 304 ARG D CZ  1 
ATOM   12934 N  NH1 . ARG D  1 304 ? 61.865  131.886 34.692  1.00 31.80  ? 304 ARG D NH1 1 
ATOM   12935 N  NH2 . ARG D  1 304 ? 61.782  132.840 32.599  1.00 34.38  ? 304 ARG D NH2 1 
ATOM   12936 N  N   . THR D  1 305 ? 61.839  127.755 31.322  1.00 28.98  ? 305 THR D N   1 
ATOM   12937 C  CA  . THR D  1 305 ? 62.368  128.160 30.024  1.00 31.88  ? 305 THR D CA  1 
ATOM   12938 C  C   . THR D  1 305 ? 61.973  127.214 28.922  1.00 34.67  ? 305 THR D C   1 
ATOM   12939 O  O   . THR D  1 305 ? 62.164  127.493 27.739  1.00 41.85  ? 305 THR D O   1 
ATOM   12940 C  CB  . THR D  1 305 ? 63.918  128.310 29.963  1.00 28.59  ? 305 THR D CB  1 
ATOM   12941 O  OG1 . THR D  1 305 ? 64.569  127.045 29.686  1.00 29.02  ? 305 THR D OG1 1 
ATOM   12942 C  CG2 . THR D  1 305 ? 64.438  128.982 31.213  1.00 28.06  ? 305 THR D CG2 1 
ATOM   12943 N  N   . LYS D  1 306 ? 61.420  126.080 29.301  1.00 36.93  ? 306 LYS D N   1 
ATOM   12944 C  CA  . LYS D  1 306 ? 61.064  125.121 28.298  1.00 32.81  ? 306 LYS D CA  1 
ATOM   12945 C  C   . LYS D  1 306 ? 59.594  124.938 28.088  1.00 30.78  ? 306 LYS D C   1 
ATOM   12946 O  O   . LYS D  1 306 ? 59.185  124.766 26.962  1.00 33.14  ? 306 LYS D O   1 
ATOM   12947 C  CB  . LYS D  1 306 ? 61.751  123.798 28.589  1.00 33.26  ? 306 LYS D CB  1 
ATOM   12948 C  CG  . LYS D  1 306 ? 62.539  123.317 27.403  1.00 34.16  ? 306 LYS D CG  1 
ATOM   12949 C  CD  . LYS D  1 306 ? 63.941  122.898 27.764  1.00 33.02  ? 306 LYS D CD  1 
ATOM   12950 C  CE  . LYS D  1 306 ? 64.829  122.783 26.529  1.00 22.83  ? 306 LYS D CE  1 
ATOM   12951 N  NZ  . LYS D  1 306 ? 65.212  124.082 25.880  1.00 40.09  ? 306 LYS D NZ  1 
ATOM   12952 N  N   . PHE D  1 307 ? 58.781  125.060 29.128  1.00 26.26  ? 307 PHE D N   1 
ATOM   12953 C  CA  . PHE D  1 307 ? 57.374  124.849 28.916  1.00 27.04  ? 307 PHE D CA  1 
ATOM   12954 C  C   . PHE D  1 307 ? 56.460  126.049 29.086  1.00 30.33  ? 307 PHE D C   1 
ATOM   12955 O  O   . PHE D  1 307 ? 55.279  125.979 28.716  1.00 29.36  ? 307 PHE D O   1 
ATOM   12956 C  CB  . PHE D  1 307 ? 56.907  123.702 29.810  1.00 29.58  ? 307 PHE D CB  1 
ATOM   12957 C  CG  . PHE D  1 307 ? 57.558  122.377 29.490  1.00 35.56  ? 307 PHE D CG  1 
ATOM   12958 C  CD1 . PHE D  1 307 ? 58.001  122.100 28.211  1.00 38.15  ? 307 PHE D CD1 1 
ATOM   12959 C  CD2 . PHE D  1 307 ? 57.733  121.411 30.472  1.00 36.03  ? 307 PHE D CD2 1 
ATOM   12960 C  CE1 . PHE D  1 307 ? 58.611  120.893 27.908  1.00 37.13  ? 307 PHE D CE1 1 
ATOM   12961 C  CE2 . PHE D  1 307 ? 58.341  120.209 30.173  1.00 34.09  ? 307 PHE D CE2 1 
ATOM   12962 C  CZ  . PHE D  1 307 ? 58.780  119.951 28.891  1.00 33.09  ? 307 PHE D CZ  1 
ATOM   12963 N  N   . GLU D  1 308 ? 56.971  127.171 29.584  1.00 27.64  ? 308 GLU D N   1 
ATOM   12964 C  CA  . GLU D  1 308 ? 56.061  128.264 29.820  1.00 24.64  ? 308 GLU D CA  1 
ATOM   12965 C  C   . GLU D  1 308 ? 55.271  128.731 28.629  1.00 27.23  ? 308 GLU D C   1 
ATOM   12966 O  O   . GLU D  1 308 ? 54.045  128.799 28.650  1.00 28.70  ? 308 GLU D O   1 
ATOM   12967 C  CB  . GLU D  1 308 ? 56.739  129.446 30.475  1.00 32.16  ? 308 GLU D CB  1 
ATOM   12968 C  CG  . GLU D  1 308 ? 55.681  130.537 30.797  1.00 34.14  ? 308 GLU D CG  1 
ATOM   12969 C  CD  . GLU D  1 308 ? 56.106  131.625 31.791  1.00 33.45  ? 308 GLU D CD  1 
ATOM   12970 O  OE1 . GLU D  1 308 ? 57.350  131.895 31.873  1.00 21.16  ? 308 GLU D OE1 1 
ATOM   12971 O  OE2 . GLU D  1 308 ? 55.154  132.207 32.434  1.00 22.95  ? 308 GLU D OE2 1 
ATOM   12972 N  N   . ALA D  1 309 ? 55.966  129.048 27.564  1.00 24.87  ? 309 ALA D N   1 
ATOM   12973 C  CA  . ALA D  1 309 ? 55.232  129.499 26.407  1.00 25.22  ? 309 ALA D CA  1 
ATOM   12974 C  C   . ALA D  1 309 ? 54.094  128.566 26.001  1.00 31.11  ? 309 ALA D C   1 
ATOM   12975 O  O   . ALA D  1 309 ? 53.031  129.042 25.625  1.00 35.02  ? 309 ALA D O   1 
ATOM   12976 C  CB  . ALA D  1 309 ? 56.153  129.645 25.293  1.00 25.65  ? 309 ALA D CB  1 
ATOM   12977 N  N   . TRP D  1 310 ? 54.323  127.242 26.072  1.00 31.71  ? 310 TRP D N   1 
ATOM   12978 C  CA  . TRP D  1 310 ? 53.332  126.261 25.658  1.00 23.17  ? 310 TRP D CA  1 
ATOM   12979 C  C   . TRP D  1 310 ? 52.128  126.431 26.508  1.00 22.02  ? 310 TRP D C   1 
ATOM   12980 O  O   . TRP D  1 310 ? 51.016  126.411 26.015  1.00 23.57  ? 310 TRP D O   1 
ATOM   12981 C  CB  . TRP D  1 310 ? 53.850  124.835 25.790  1.00 24.89  ? 310 TRP D CB  1 
ATOM   12982 C  CG  . TRP D  1 310 ? 54.993  124.483 24.867  1.00 33.50  ? 310 TRP D CG  1 
ATOM   12983 C  CD1 . TRP D  1 310 ? 55.651  125.324 24.042  1.00 36.91  ? 310 TRP D CD1 1 
ATOM   12984 C  CD2 . TRP D  1 310 ? 55.657  123.205 24.729  1.00 38.57  ? 310 TRP D CD2 1 
ATOM   12985 N  NE1 . TRP D  1 310 ? 56.688  124.676 23.393  1.00 36.29  ? 310 TRP D NE1 1 
ATOM   12986 C  CE2 . TRP D  1 310 ? 56.712  123.375 23.801  1.00 38.11  ? 310 TRP D CE2 1 
ATOM   12987 C  CE3 . TRP D  1 310 ? 55.474  121.949 25.305  1.00 37.32  ? 310 TRP D CE3 1 
ATOM   12988 C  CZ2 . TRP D  1 310 ? 57.571  122.339 23.438  1.00 34.14  ? 310 TRP D CZ2 1 
ATOM   12989 C  CZ3 . TRP D  1 310 ? 56.343  120.923 24.940  1.00 39.93  ? 310 TRP D CZ3 1 
ATOM   12990 C  CH2 . TRP D  1 310 ? 57.374  121.130 24.017  1.00 33.55  ? 310 TRP D CH2 1 
ATOM   12991 N  N   . PHE D  1 311 ? 52.347  126.625 27.789  1.00 19.11  ? 311 PHE D N   1 
ATOM   12992 C  CA  . PHE D  1 311 ? 51.240  126.761 28.704  1.00 27.79  ? 311 PHE D CA  1 
ATOM   12993 C  C   . PHE D  1 311 ? 50.417  127.976 28.364  1.00 32.51  ? 311 PHE D C   1 
ATOM   12994 O  O   . PHE D  1 311 ? 49.168  127.946 28.413  1.00 34.41  ? 311 PHE D O   1 
ATOM   12995 C  CB  . PHE D  1 311 ? 51.747  126.894 30.140  1.00 32.22  ? 311 PHE D CB  1 
ATOM   12996 C  CG  . PHE D  1 311 ? 52.482  125.669 30.669  1.00 33.50  ? 311 PHE D CG  1 
ATOM   12997 C  CD1 . PHE D  1 311 ? 52.396  124.459 30.028  1.00 29.53  ? 311 PHE D CD1 1 
ATOM   12998 C  CD2 . PHE D  1 311 ? 53.307  125.768 31.789  1.00 36.33  ? 311 PHE D CD2 1 
ATOM   12999 C  CE1 . PHE D  1 311 ? 53.108  123.401 30.465  1.00 24.30  ? 311 PHE D CE1 1 
ATOM   13000 C  CE2 . PHE D  1 311 ? 54.032  124.693 32.250  1.00 28.23  ? 311 PHE D CE2 1 
ATOM   13001 C  CZ  . PHE D  1 311 ? 53.936  123.515 31.583  1.00 34.50  ? 311 PHE D CZ  1 
ATOM   13002 N  N   . VAL D  1 312 ? 51.119  129.063 28.059  1.00 33.60  ? 312 VAL D N   1 
ATOM   13003 C  CA  . VAL D  1 312 ? 50.448  130.306 27.728  1.00 34.97  ? 312 VAL D CA  1 
ATOM   13004 C  C   . VAL D  1 312 ? 49.754  130.093 26.413  1.00 34.93  ? 312 VAL D C   1 
ATOM   13005 O  O   . VAL D  1 312 ? 48.554  130.281 26.290  1.00 35.43  ? 312 VAL D O   1 
ATOM   13006 C  CB  . VAL D  1 312 ? 51.413  131.479 27.609  1.00 36.81  ? 312 VAL D CB  1 
ATOM   13007 C  CG1 . VAL D  1 312 ? 50.677  132.690 27.217  1.00 35.70  ? 312 VAL D CG1 1 
ATOM   13008 C  CG2 . VAL D  1 312 ? 52.060  131.764 28.937  1.00 41.23  ? 312 VAL D CG2 1 
ATOM   13009 N  N   . LYS D  1 313 ? 50.510  129.633 25.440  1.00 33.78  ? 313 LYS D N   1 
ATOM   13010 C  CA  . LYS D  1 313 ? 49.952  129.361 24.140  1.00 36.23  ? 313 LYS D CA  1 
ATOM   13011 C  C   . LYS D  1 313 ? 48.650  128.516 24.167  1.00 36.66  ? 313 LYS D C   1 
ATOM   13012 O  O   . LYS D  1 313 ? 47.770  128.744 23.343  1.00 41.48  ? 313 LYS D O   1 
ATOM   13013 C  CB  . LYS D  1 313 ? 51.001  128.682 23.288  1.00 39.31  ? 313 LYS D CB  1 
ATOM   13014 C  CG  . LYS D  1 313 ? 50.472  128.107 22.024  1.00 45.79  ? 313 LYS D CG  1 
ATOM   13015 C  CD  . LYS D  1 313 ? 51.625  127.547 21.242  1.00 61.02  ? 313 LYS D CD  1 
ATOM   13016 C  CE  . LYS D  1 313 ? 51.145  126.813 20.002  1.00 75.79  ? 313 LYS D CE  1 
ATOM   13017 N  NZ  . LYS D  1 313 ? 50.189  127.659 19.177  1.00 93.73  ? 313 LYS D NZ  1 
ATOM   13018 N  N   . TYR D  1 314 ? 48.511  127.560 25.096  1.00 34.15  ? 314 TYR D N   1 
ATOM   13019 C  CA  . TYR D  1 314 ? 47.304  126.729 25.162  1.00 26.22  ? 314 TYR D CA  1 
ATOM   13020 C  C   . TYR D  1 314 ? 46.348  127.159 26.231  1.00 29.24  ? 314 TYR D C   1 
ATOM   13021 O  O   . TYR D  1 314 ? 45.342  126.502 26.535  1.00 27.47  ? 314 TYR D O   1 
ATOM   13022 C  CB  . TYR D  1 314 ? 47.665  125.294 25.319  1.00 21.33  ? 314 TYR D CB  1 
ATOM   13023 C  CG  . TYR D  1 314 ? 48.290  124.766 24.070  1.00 26.89  ? 314 TYR D CG  1 
ATOM   13024 C  CD1 . TYR D  1 314 ? 49.671  124.870 23.832  1.00 20.18  ? 314 TYR D CD1 1 
ATOM   13025 C  CD2 . TYR D  1 314 ? 47.501  124.158 23.105  1.00 25.70  ? 314 TYR D CD2 1 
ATOM   13026 C  CE1 . TYR D  1 314 ? 50.228  124.365 22.638  1.00 29.23  ? 314 TYR D CE1 1 
ATOM   13027 C  CE2 . TYR D  1 314 ? 48.048  123.665 21.934  1.00 26.59  ? 314 TYR D CE2 1 
ATOM   13028 C  CZ  . TYR D  1 314 ? 49.396  123.766 21.707  1.00 29.47  ? 314 TYR D CZ  1 
ATOM   13029 O  OH  . TYR D  1 314 ? 49.899  123.251 20.544  1.00 41.40  ? 314 TYR D OH  1 
ATOM   13030 N  N   . LYS D  1 315 ? 46.683  128.272 26.844  1.00 33.70  ? 315 LYS D N   1 
ATOM   13031 C  CA  . LYS D  1 315 ? 45.816  128.811 27.851  1.00 39.22  ? 315 LYS D CA  1 
ATOM   13032 C  C   . LYS D  1 315 ? 45.540  127.826 28.950  1.00 36.39  ? 315 LYS D C   1 
ATOM   13033 O  O   . LYS D  1 315 ? 44.392  127.677 29.314  1.00 37.78  ? 315 LYS D O   1 
ATOM   13034 C  CB  . LYS D  1 315 ? 44.503  129.242 27.195  1.00 39.37  ? 315 LYS D CB  1 
ATOM   13035 C  CG  . LYS D  1 315 ? 44.724  130.379 26.204  1.00 49.90  ? 315 LYS D CG  1 
ATOM   13036 C  CD  . LYS D  1 315 ? 43.817  130.290 24.996  1.00 60.71  ? 315 LYS D CD  1 
ATOM   13037 C  CE  . LYS D  1 315 ? 42.808  131.461 24.913  1.00 70.11  ? 315 LYS D CE  1 
ATOM   13038 N  NZ  . LYS D  1 315 ? 43.420  132.821 24.771  1.00 73.27  ? 315 LYS D NZ  1 
ATOM   13039 N  N   . VAL D  1 316 ? 46.568  127.199 29.528  1.00 32.54  ? 316 VAL D N   1 
ATOM   13040 C  CA  . VAL D  1 316 ? 46.248  126.253 30.588  1.00 33.83  ? 316 VAL D CA  1 
ATOM   13041 C  C   . VAL D  1 316 ? 45.690  127.104 31.758  1.00 35.47  ? 316 VAL D C   1 
ATOM   13042 O  O   . VAL D  1 316 ? 46.097  128.245 31.926  1.00 35.28  ? 316 VAL D O   1 
ATOM   13043 C  CB  . VAL D  1 316 ? 47.447  125.321 30.974  1.00 30.74  ? 316 VAL D CB  1 
ATOM   13044 C  CG1 . VAL D  1 316 ? 48.493  125.306 29.915  1.00 28.57  ? 316 VAL D CG1 1 
ATOM   13045 C  CG2 . VAL D  1 316 ? 48.066  125.724 32.266  1.00 30.32  ? 316 VAL D CG2 1 
ATOM   13046 N  N   . ASP D  1 317 ? 44.690  126.595 32.474  1.00 35.75  ? 317 ASP D N   1 
ATOM   13047 C  CA  . ASP D  1 317 ? 44.083  127.306 33.595  1.00 32.85  ? 317 ASP D CA  1 
ATOM   13048 C  C   . ASP D  1 317 ? 44.922  127.469 34.848  1.00 32.94  ? 317 ASP D C   1 
ATOM   13049 O  O   . ASP D  1 317 ? 45.124  128.586 35.301  1.00 36.34  ? 317 ASP D O   1 
ATOM   13050 C  CB  . ASP D  1 317 ? 42.783  126.641 33.966  1.00 31.71  ? 317 ASP D CB  1 
ATOM   13051 C  CG  . ASP D  1 317 ? 41.747  126.906 32.973  1.00 36.58  ? 317 ASP D CG  1 
ATOM   13052 O  OD1 . ASP D  1 317 ? 41.272  128.055 33.021  1.00 45.73  ? 317 ASP D OD1 1 
ATOM   13053 O  OD2 . ASP D  1 317 ? 41.441  126.023 32.138  1.00 29.67  ? 317 ASP D OD2 1 
ATOM   13054 N  N   . VAL D  1 318 ? 45.395  126.360 35.416  1.00 32.01  ? 318 VAL D N   1 
ATOM   13055 C  CA  . VAL D  1 318 ? 46.202  126.363 36.648  1.00 27.86  ? 318 VAL D CA  1 
ATOM   13056 C  C   . VAL D  1 318 ? 47.398  125.435 36.510  1.00 29.98  ? 318 VAL D C   1 
ATOM   13057 O  O   . VAL D  1 318 ? 47.370  124.488 35.742  1.00 37.31  ? 318 VAL D O   1 
ATOM   13058 C  CB  . VAL D  1 318 ? 45.463  125.728 37.866  1.00 28.57  ? 318 VAL D CB  1 
ATOM   13059 C  CG1 . VAL D  1 318 ? 45.614  126.593 39.054  1.00 31.27  ? 318 VAL D CG1 1 
ATOM   13060 C  CG2 . VAL D  1 318 ? 44.021  125.358 37.577  1.00 31.77  ? 318 VAL D CG2 1 
ATOM   13061 N  N   . VAL D  1 319 ? 48.416  125.640 37.325  1.00 27.52  ? 319 VAL D N   1 
ATOM   13062 C  CA  . VAL D  1 319 ? 49.558  124.743 37.346  1.00 20.30  ? 319 VAL D CA  1 
ATOM   13063 C  C   . VAL D  1 319 ? 49.851  124.576 38.816  1.00 19.80  ? 319 VAL D C   1 
ATOM   13064 O  O   . VAL D  1 319 ? 50.300  125.517 39.470  1.00 21.52  ? 319 VAL D O   1 
ATOM   13065 C  CB  . VAL D  1 319 ? 50.708  125.349 36.686  1.00 18.02  ? 319 VAL D CB  1 
ATOM   13066 C  CG1 . VAL D  1 319 ? 51.957  124.537 36.943  1.00 24.95  ? 319 VAL D CG1 1 
ATOM   13067 C  CG2 . VAL D  1 319 ? 50.416  125.414 35.265  1.00 16.42  ? 319 VAL D CG2 1 
ATOM   13068 N  N   . PHE D  1 320 ? 49.516  123.416 39.359  1.00 18.79  ? 320 PHE D N   1 
ATOM   13069 C  CA  . PHE D  1 320 ? 49.756  123.163 40.779  1.00 21.46  ? 320 PHE D CA  1 
ATOM   13070 C  C   . PHE D  1 320 ? 51.129  122.545 41.003  1.00 21.56  ? 320 PHE D C   1 
ATOM   13071 O  O   . PHE D  1 320 ? 51.532  121.704 40.215  1.00 27.64  ? 320 PHE D O   1 
ATOM   13072 C  CB  . PHE D  1 320 ? 48.674  122.246 41.307  1.00 19.68  ? 320 PHE D CB  1 
ATOM   13073 C  CG  . PHE D  1 320 ? 47.319  122.830 41.221  1.00 19.25  ? 320 PHE D CG  1 
ATOM   13074 C  CD1 . PHE D  1 320 ? 46.890  123.771 42.160  1.00 20.53  ? 320 PHE D CD1 1 
ATOM   13075 C  CD2 . PHE D  1 320 ? 46.439  122.394 40.262  1.00 20.87  ? 320 PHE D CD2 1 
ATOM   13076 C  CE1 . PHE D  1 320 ? 45.595  124.258 42.152  1.00 19.74  ? 320 PHE D CE1 1 
ATOM   13077 C  CE2 . PHE D  1 320 ? 45.126  122.875 40.235  1.00 23.41  ? 320 PHE D CE2 1 
ATOM   13078 C  CZ  . PHE D  1 320 ? 44.702  123.810 41.186  1.00 23.48  ? 320 PHE D CZ  1 
ATOM   13079 N  N   . ALA D  1 321 ? 51.850  122.956 42.040  1.00 19.54  ? 321 ALA D N   1 
ATOM   13080 C  CA  . ALA D  1 321 ? 53.180  122.406 42.347  1.00 19.93  ? 321 ALA D CA  1 
ATOM   13081 C  C   . ALA D  1 321 ? 53.326  122.258 43.858  1.00 23.15  ? 321 ALA D C   1 
ATOM   13082 O  O   . ALA D  1 321 ? 52.471  122.725 44.619  1.00 31.62  ? 321 ALA D O   1 
ATOM   13083 C  CB  . ALA D  1 321 ? 54.253  123.329 41.830  1.00 18.70  ? 321 ALA D CB  1 
ATOM   13084 N  N   . GLY D  1 322 ? 54.382  121.610 44.316  1.00 19.86  ? 322 GLY D N   1 
ATOM   13085 C  CA  . GLY D  1 322 ? 54.583  121.455 45.748  1.00 19.64  ? 322 GLY D CA  1 
ATOM   13086 C  C   . GLY D  1 322 ? 56.002  121.892 45.933  1.00 20.23  ? 322 GLY D C   1 
ATOM   13087 O  O   . GLY D  1 322 ? 56.356  122.909 45.404  1.00 15.49  ? 322 GLY D O   1 
ATOM   13088 N  N   . HIS D  1 323 ? 56.827  121.109 46.616  1.00 20.78  ? 323 HIS D N   1 
ATOM   13089 C  CA  . HIS D  1 323 ? 58.237  121.401 46.811  1.00 26.71  ? 323 HIS D CA  1 
ATOM   13090 C  C   . HIS D  1 323 ? 58.584  122.501 47.809  1.00 29.57  ? 323 HIS D C   1 
ATOM   13091 O  O   . HIS D  1 323 ? 59.570  122.418 48.548  1.00 33.16  ? 323 HIS D O   1 
ATOM   13092 C  CB  . HIS D  1 323 ? 58.923  121.612 45.454  1.00 22.59  ? 323 HIS D CB  1 
ATOM   13093 C  CG  . HIS D  1 323 ? 60.391  121.336 45.465  1.00 19.90  ? 323 HIS D CG  1 
ATOM   13094 N  ND1 . HIS D  1 323 ? 60.938  120.167 45.965  1.00 23.13  ? 323 HIS D ND1 1 
ATOM   13095 C  CD2 . HIS D  1 323 ? 61.426  122.079 45.005  1.00 22.85  ? 323 HIS D CD2 1 
ATOM   13096 C  CE1 . HIS D  1 323 ? 62.252  120.215 45.811  1.00 29.60  ? 323 HIS D CE1 1 
ATOM   13097 N  NE2 . HIS D  1 323 ? 62.572  121.362 45.233  1.00 27.54  ? 323 HIS D NE2 1 
ATOM   13098 N  N   . VAL D  1 324 ? 57.839  123.584 47.805  1.00 31.20  ? 324 VAL D N   1 
ATOM   13099 C  CA  . VAL D  1 324 ? 58.113  124.605 48.807  1.00 31.91  ? 324 VAL D CA  1 
ATOM   13100 C  C   . VAL D  1 324 ? 57.047  124.338 49.879  1.00 35.49  ? 324 VAL D C   1 
ATOM   13101 O  O   . VAL D  1 324 ? 55.858  124.220 49.581  1.00 36.92  ? 324 VAL D O   1 
ATOM   13102 C  CB  . VAL D  1 324 ? 58.050  125.990 48.225  1.00 27.78  ? 324 VAL D CB  1 
ATOM   13103 C  CG1 . VAL D  1 324 ? 58.191  127.007 49.324  1.00 27.87  ? 324 VAL D CG1 1 
ATOM   13104 C  CG2 . VAL D  1 324 ? 59.177  126.140 47.227  1.00 22.54  ? 324 VAL D CG2 1 
ATOM   13105 N  N   . HIS D  1 325 ? 57.494  124.049 51.090  1.00 38.45  ? 325 HIS D N   1 
ATOM   13106 C  CA  . HIS D  1 325 ? 56.565  123.730 52.156  1.00 39.54  ? 325 HIS D CA  1 
ATOM   13107 C  C   . HIS D  1 325 ? 55.887  124.997 52.683  1.00 40.89  ? 325 HIS D C   1 
ATOM   13108 O  O   . HIS D  1 325 ? 56.184  125.475 53.789  1.00 41.50  ? 325 HIS D O   1 
ATOM   13109 C  CB  . HIS D  1 325 ? 57.281  122.945 53.260  1.00 38.66  ? 325 HIS D CB  1 
ATOM   13110 C  CG  . HIS D  1 325 ? 58.054  121.754 52.767  1.00 38.26  ? 325 HIS D CG  1 
ATOM   13111 N  ND1 . HIS D  1 325 ? 59.240  121.338 53.340  1.00 38.12  ? 325 HIS D ND1 1 
ATOM   13112 C  CD2 . HIS D  1 325 ? 57.830  120.914 51.728  1.00 39.09  ? 325 HIS D CD2 1 
ATOM   13113 C  CE1 . HIS D  1 325 ? 59.714  120.303 52.666  1.00 35.30  ? 325 HIS D CE1 1 
ATOM   13114 N  NE2 . HIS D  1 325 ? 58.880  120.023 51.680  1.00 33.21  ? 325 HIS D NE2 1 
ATOM   13115 N  N   . ALA D  1 326 ? 54.969  125.517 51.865  1.00 37.35  ? 326 ALA D N   1 
ATOM   13116 C  CA  . ALA D  1 326 ? 54.217  126.736 52.130  1.00 34.70  ? 326 ALA D CA  1 
ATOM   13117 C  C   . ALA D  1 326 ? 53.172  126.876 51.048  1.00 34.51  ? 326 ALA D C   1 
ATOM   13118 O  O   . ALA D  1 326 ? 53.069  126.025 50.192  1.00 38.01  ? 326 ALA D O   1 
ATOM   13119 C  CB  . ALA D  1 326 ? 55.124  127.930 52.100  1.00 28.15  ? 326 ALA D CB  1 
ATOM   13120 N  N   . TYR D  1 327 ? 52.397  127.946 51.086  1.00 35.82  ? 327 TYR D N   1 
ATOM   13121 C  CA  . TYR D  1 327 ? 51.359  128.180 50.107  1.00 30.84  ? 327 TYR D CA  1 
ATOM   13122 C  C   . TYR D  1 327 ? 51.684  129.463 49.421  1.00 31.63  ? 327 TYR D C   1 
ATOM   13123 O  O   . TYR D  1 327 ? 52.320  130.334 49.991  1.00 35.25  ? 327 TYR D O   1 
ATOM   13124 C  CB  . TYR D  1 327 ? 50.051  128.356 50.795  1.00 30.82  ? 327 TYR D CB  1 
ATOM   13125 C  CG  . TYR D  1 327 ? 48.959  128.807 49.882  1.00 39.97  ? 327 TYR D CG  1 
ATOM   13126 C  CD1 . TYR D  1 327 ? 48.502  127.999 48.845  1.00 46.35  ? 327 TYR D CD1 1 
ATOM   13127 C  CD2 . TYR D  1 327 ? 48.280  129.993 50.115  1.00 42.38  ? 327 TYR D CD2 1 
ATOM   13128 C  CE1 . TYR D  1 327 ? 47.357  128.374 48.064  1.00 47.58  ? 327 TYR D CE1 1 
ATOM   13129 C  CE2 . TYR D  1 327 ? 47.158  130.375 49.349  1.00 39.72  ? 327 TYR D CE2 1 
ATOM   13130 C  CZ  . TYR D  1 327 ? 46.697  129.567 48.334  1.00 44.27  ? 327 TYR D CZ  1 
ATOM   13131 O  OH  . TYR D  1 327 ? 45.590  129.949 47.599  1.00 38.54  ? 327 TYR D OH  1 
ATOM   13132 N  N   . GLU D  1 328 ? 51.258  129.586 48.184  1.00 31.45  ? 328 GLU D N   1 
ATOM   13133 C  CA  . GLU D  1 328 ? 51.489  130.805 47.401  1.00 36.12  ? 328 GLU D CA  1 
ATOM   13134 C  C   . GLU D  1 328 ? 50.571  130.717 46.177  1.00 41.28  ? 328 GLU D C   1 
ATOM   13135 O  O   . GLU D  1 328 ? 50.274  129.625 45.697  1.00 50.03  ? 328 GLU D O   1 
ATOM   13136 C  CB  . GLU D  1 328 ? 52.981  130.981 47.026  1.00 25.34  ? 328 GLU D CB  1 
ATOM   13137 C  CG  . GLU D  1 328 ? 53.197  131.950 45.892  1.00 25.87  ? 328 GLU D CG  1 
ATOM   13138 C  CD  . GLU D  1 328 ? 54.584  132.579 45.855  1.00 36.13  ? 328 GLU D CD  1 
ATOM   13139 O  OE1 . GLU D  1 328 ? 55.572  131.925 46.233  1.00 36.30  ? 328 GLU D OE1 1 
ATOM   13140 O  OE2 . GLU D  1 328 ? 54.705  133.750 45.425  1.00 43.77  ? 328 GLU D OE2 1 
ATOM   13141 N  N   . ARG D  1 329 ? 50.039  131.849 45.739  1.00 43.44  ? 329 ARG D N   1 
ATOM   13142 C  CA  . ARG D  1 329 ? 49.146  131.916 44.582  1.00 43.65  ? 329 ARG D CA  1 
ATOM   13143 C  C   . ARG D  1 329 ? 49.646  133.048 43.695  1.00 44.00  ? 329 ARG D C   1 
ATOM   13144 O  O   . ARG D  1 329 ? 50.166  134.037 44.198  1.00 53.50  ? 329 ARG D O   1 
ATOM   13145 C  CB  . ARG D  1 329 ? 47.732  132.228 45.033  1.00 41.55  ? 329 ARG D CB  1 
ATOM   13146 C  CG  . ARG D  1 329 ? 46.770  132.038 43.934  1.00 51.58  ? 329 ARG D CG  1 
ATOM   13147 C  CD  . ARG D  1 329 ? 45.391  132.272 44.389  1.00 59.60  ? 329 ARG D CD  1 
ATOM   13148 N  NE  . ARG D  1 329 ? 45.089  133.690 44.360  1.00 65.22  ? 329 ARG D NE  1 
ATOM   13149 C  CZ  . ARG D  1 329 ? 44.811  134.393 45.445  1.00 66.45  ? 329 ARG D CZ  1 
ATOM   13150 N  NH1 . ARG D  1 329 ? 44.802  133.815 46.639  1.00 65.58  ? 329 ARG D NH1 1 
ATOM   13151 N  NH2 . ARG D  1 329 ? 44.514  135.675 45.326  1.00 70.88  ? 329 ARG D NH2 1 
ATOM   13152 N  N   . SER D  1 330 ? 49.515  132.934 42.386  1.00 44.53  ? 330 SER D N   1 
ATOM   13153 C  CA  . SER D  1 330 ? 50.009  133.993 41.537  1.00 42.85  ? 330 SER D CA  1 
ATOM   13154 C  C   . SER D  1 330 ? 48.988  134.695 40.743  1.00 44.22  ? 330 SER D C   1 
ATOM   13155 O  O   . SER D  1 330 ? 47.776  134.496 40.925  1.00 44.03  ? 330 SER D O   1 
ATOM   13156 C  CB  . SER D  1 330 ? 51.111  133.502 40.617  1.00 38.50  ? 330 SER D CB  1 
ATOM   13157 O  OG  . SER D  1 330 ? 52.276  133.409 41.424  1.00 53.00  ? 330 SER D OG  1 
ATOM   13158 N  N   . GLU D  1 331 ? 49.516  135.639 39.975  1.00 46.34  ? 331 GLU D N   1 
ATOM   13159 C  CA  . GLU D  1 331 ? 48.734  136.453 39.070  1.00 48.34  ? 331 GLU D CA  1 
ATOM   13160 C  C   . GLU D  1 331 ? 48.899  135.765 37.725  1.00 41.47  ? 331 GLU D C   1 
ATOM   13161 O  O   . GLU D  1 331 ? 49.909  135.065 37.527  1.00 44.76  ? 331 GLU D O   1 
ATOM   13162 C  CB  . GLU D  1 331 ? 49.324  137.881 38.995  1.00 57.18  ? 331 GLU D CB  1 
ATOM   13163 C  CG  . GLU D  1 331 ? 49.137  138.755 40.252  1.00 71.01  ? 331 GLU D CG  1 
ATOM   13164 C  CD  . GLU D  1 331 ? 47.644  139.071 40.610  1.00 80.17  ? 331 GLU D CD  1 
ATOM   13165 O  OE1 . GLU D  1 331 ? 46.699  138.493 39.999  1.00 84.51  ? 331 GLU D OE1 1 
ATOM   13166 O  OE2 . GLU D  1 331 ? 47.417  139.904 41.529  1.00 84.50  ? 331 GLU D OE2 1 
ATOM   13167 N  N   . ARG D  1 332 ? 47.902  135.864 36.849  1.00 26.84  ? 332 ARG D N   1 
ATOM   13168 C  CA  . ARG D  1 332 ? 48.070  135.284 35.548  1.00 21.44  ? 332 ARG D CA  1 
ATOM   13169 C  C   . ARG D  1 332 ? 49.193  136.119 35.031  1.00 29.03  ? 332 ARG D C   1 
ATOM   13170 O  O   . ARG D  1 332 ? 49.092  137.327 34.924  1.00 33.60  ? 332 ARG D O   1 
ATOM   13171 C  CB  . ARG D  1 332 ? 46.827  135.405 34.747  1.00 17.89  ? 332 ARG D CB  1 
ATOM   13172 C  CG  . ARG D  1 332 ? 45.776  134.579 35.376  1.00 17.44  ? 332 ARG D CG  1 
ATOM   13173 C  CD  . ARG D  1 332 ? 44.652  134.402 34.468  1.00 20.07  ? 332 ARG D CD  1 
ATOM   13174 N  NE  . ARG D  1 332 ? 43.656  133.502 35.039  1.00 27.24  ? 332 ARG D NE  1 
ATOM   13175 C  CZ  . ARG D  1 332 ? 43.666  132.197 34.872  1.00 26.29  ? 332 ARG D CZ  1 
ATOM   13176 N  NH1 . ARG D  1 332 ? 44.665  131.659 34.187  1.00 31.41  ? 332 ARG D NH1 1 
ATOM   13177 N  NH2 . ARG D  1 332 ? 42.595  131.471 35.219  1.00 28.45  ? 332 ARG D NH2 1 
ATOM   13178 N  N   . VAL D  1 333 ? 50.328  135.470 34.862  1.00 36.47  ? 333 VAL D N   1 
ATOM   13179 C  CA  . VAL D  1 333 ? 51.551  136.124 34.490  1.00 39.21  ? 333 VAL D CA  1 
ATOM   13180 C  C   . VAL D  1 333 ? 52.366  135.281 33.520  1.00 39.65  ? 333 VAL D C   1 
ATOM   13181 O  O   . VAL D  1 333 ? 52.355  134.052 33.558  1.00 44.62  ? 333 VAL D O   1 
ATOM   13182 C  CB  . VAL D  1 333 ? 52.343  136.319 35.793  1.00 44.57  ? 333 VAL D CB  1 
ATOM   13183 C  CG1 . VAL D  1 333 ? 53.788  136.595 35.548  1.00 49.68  ? 333 VAL D CG1 1 
ATOM   13184 C  CG2 . VAL D  1 333 ? 51.748  137.442 36.554  1.00 50.55  ? 333 VAL D CG2 1 
ATOM   13185 N  N   . SER D  1 334 ? 53.120  135.954 32.670  1.00 36.31  ? 334 SER D N   1 
ATOM   13186 C  CA  . SER D  1 334 ? 53.965  135.279 31.722  1.00 33.76  ? 334 SER D CA  1 
ATOM   13187 C  C   . SER D  1 334 ? 55.307  135.985 31.812  1.00 30.88  ? 334 SER D C   1 
ATOM   13188 O  O   . SER D  1 334 ? 55.411  137.045 32.387  1.00 35.83  ? 334 SER D O   1 
ATOM   13189 C  CB  . SER D  1 334 ? 53.375  135.451 30.317  1.00 33.63  ? 334 SER D CB  1 
ATOM   13190 O  OG  . SER D  1 334 ? 54.012  136.520 29.627  1.00 34.29  ? 334 SER D OG  1 
ATOM   13191 N  N   . ASN D  1 335 ? 56.341  135.392 31.266  1.00 29.80  ? 335 ASN D N   1 
ATOM   13192 C  CA  . ASN D  1 335 ? 57.655  136.013 31.244  1.00 28.10  ? 335 ASN D CA  1 
ATOM   13193 C  C   . ASN D  1 335 ? 58.314  135.347 30.053  1.00 33.41  ? 335 ASN D C   1 
ATOM   13194 O  O   . ASN D  1 335 ? 59.395  134.780 30.147  1.00 34.27  ? 335 ASN D O   1 
ATOM   13195 C  CB  . ASN D  1 335 ? 58.457  135.714 32.498  1.00 26.09  ? 335 ASN D CB  1 
ATOM   13196 C  CG  . ASN D  1 335 ? 59.878  136.317 32.440  1.00 32.54  ? 335 ASN D CG  1 
ATOM   13197 O  OD1 . ASN D  1 335 ? 60.233  136.971 31.461  1.00 42.35  ? 335 ASN D OD1 1 
ATOM   13198 N  ND2 . ASN D  1 335 ? 60.674  136.125 33.497  1.00 31.58  ? 335 ASN D ND2 1 
ATOM   13199 N  N   . ILE D  1 336 ? 57.668  135.447 28.904  1.00 35.15  ? 336 ILE D N   1 
ATOM   13200 C  CA  . ILE D  1 336 ? 58.164  134.770 27.735  1.00 34.74  ? 336 ILE D CA  1 
ATOM   13201 C  C   . ILE D  1 336 ? 58.721  135.631 26.610  1.00 43.43  ? 336 ILE D C   1 
ATOM   13202 O  O   . ILE D  1 336 ? 58.636  135.223 25.443  1.00 52.52  ? 336 ILE D O   1 
ATOM   13203 C  CB  . ILE D  1 336 ? 57.030  133.865 27.187  1.00 33.39  ? 336 ILE D CB  1 
ATOM   13204 C  CG1 . ILE D  1 336 ? 55.826  134.702 26.779  1.00 30.66  ? 336 ILE D CG1 1 
ATOM   13205 C  CG2 . ILE D  1 336 ? 56.537  132.917 28.284  1.00 29.19  ? 336 ILE D CG2 1 
ATOM   13206 C  CD1 . ILE D  1 336 ? 54.588  133.901 26.545  1.00 32.46  ? 336 ILE D CD1 1 
ATOM   13207 N  N   . ALA D  1 337 ? 59.365  136.760 26.923  1.00 45.10  ? 337 ALA D N   1 
ATOM   13208 C  CA  . ALA D  1 337 ? 59.864  137.634 25.850  1.00 42.45  ? 337 ALA D CA  1 
ATOM   13209 C  C   . ALA D  1 337 ? 61.342  137.798 25.782  1.00 40.15  ? 337 ALA D C   1 
ATOM   13210 O  O   . ALA D  1 337 ? 61.882  138.417 24.872  1.00 43.58  ? 337 ALA D O   1 
ATOM   13211 C  CB  . ALA D  1 337 ? 59.234  138.978 25.964  1.00 46.11  ? 337 ALA D CB  1 
ATOM   13212 N  N   . TYR D  1 338 ? 62.003  137.251 26.767  1.00 36.50  ? 338 TYR D N   1 
ATOM   13213 C  CA  . TYR D  1 338 ? 63.420  137.371 26.829  1.00 36.37  ? 338 TYR D CA  1 
ATOM   13214 C  C   . TYR D  1 338 ? 64.116  136.814 25.608  1.00 36.34  ? 338 TYR D C   1 
ATOM   13215 O  O   . TYR D  1 338 ? 63.706  135.799 25.041  1.00 41.47  ? 338 TYR D O   1 
ATOM   13216 C  CB  . TYR D  1 338 ? 63.892  136.685 28.078  1.00 35.21  ? 338 TYR D CB  1 
ATOM   13217 C  CG  . TYR D  1 338 ? 65.341  136.850 28.365  1.00 36.08  ? 338 TYR D CG  1 
ATOM   13218 C  CD1 . TYR D  1 338 ? 65.875  138.092 28.600  1.00 41.49  ? 338 TYR D CD1 1 
ATOM   13219 C  CD2 . TYR D  1 338 ? 66.171  135.751 28.485  1.00 36.24  ? 338 TYR D CD2 1 
ATOM   13220 C  CE1 . TYR D  1 338 ? 67.214  138.238 28.958  1.00 41.02  ? 338 TYR D CE1 1 
ATOM   13221 C  CE2 . TYR D  1 338 ? 67.500  135.891 28.842  1.00 35.23  ? 338 TYR D CE2 1 
ATOM   13222 C  CZ  . TYR D  1 338 ? 68.013  137.134 29.077  1.00 33.85  ? 338 TYR D CZ  1 
ATOM   13223 O  OH  . TYR D  1 338 ? 69.335  137.255 29.398  1.00 39.89  ? 338 TYR D OH  1 
ATOM   13224 N  N   . LYS D  1 339 ? 65.177  137.497 25.214  1.00 34.89  ? 339 LYS D N   1 
ATOM   13225 C  CA  . LYS D  1 339 ? 65.967  137.093 24.084  1.00 35.78  ? 339 LYS D CA  1 
ATOM   13226 C  C   . LYS D  1 339 ? 67.415  137.353 24.421  1.00 36.32  ? 339 LYS D C   1 
ATOM   13227 O  O   . LYS D  1 339 ? 68.187  137.713 23.559  1.00 37.80  ? 339 LYS D O   1 
ATOM   13228 C  CB  . LYS D  1 339 ? 65.599  137.895 22.856  1.00 39.51  ? 339 LYS D CB  1 
ATOM   13229 C  CG  . LYS D  1 339 ? 64.169  137.855 22.540  1.00 48.03  ? 339 LYS D CG  1 
ATOM   13230 C  CD  . LYS D  1 339 ? 63.785  136.481 22.157  1.00 58.89  ? 339 LYS D CD  1 
ATOM   13231 C  CE  . LYS D  1 339 ? 62.346  136.481 21.730  1.00 67.27  ? 339 LYS D CE  1 
ATOM   13232 N  NZ  . LYS D  1 339 ? 62.150  137.549 20.703  1.00 75.56  ? 339 LYS D NZ  1 
ATOM   13233 N  N   . ILE D  1 340 ? 67.768  137.199 25.690  1.00 37.57  ? 340 ILE D N   1 
ATOM   13234 C  CA  . ILE D  1 340 ? 69.144  137.385 26.166  1.00 40.02  ? 340 ILE D CA  1 
ATOM   13235 C  C   . ILE D  1 340 ? 69.565  138.819 26.313  1.00 44.11  ? 340 ILE D C   1 
ATOM   13236 O  O   . ILE D  1 340 ? 69.761  139.329 27.420  1.00 45.74  ? 340 ILE D O   1 
ATOM   13237 C  CB  . ILE D  1 340 ? 70.187  136.748 25.242  1.00 36.75  ? 340 ILE D CB  1 
ATOM   13238 C  CG1 . ILE D  1 340 ? 69.771  135.343 24.845  1.00 38.56  ? 340 ILE D CG1 1 
ATOM   13239 C  CG2 . ILE D  1 340 ? 71.514  136.727 25.938  1.00 35.95  ? 340 ILE D CG2 1 
ATOM   13240 C  CD1 . ILE D  1 340 ? 69.512  134.460 26.029  1.00 40.89  ? 340 ILE D CD1 1 
ATOM   13241 N  N   . THR D  1 341 ? 69.721  139.462 25.170  1.00 45.44  ? 341 THR D N   1 
ATOM   13242 C  CA  . THR D  1 341 ? 70.139  140.835 25.118  1.00 46.14  ? 341 THR D CA  1 
ATOM   13243 C  C   . THR D  1 341 ? 69.034  141.893 25.140  1.00 45.94  ? 341 THR D C   1 
ATOM   13244 O  O   . THR D  1 341 ? 69.278  143.021 25.516  1.00 49.70  ? 341 THR D O   1 
ATOM   13245 C  CB  . THR D  1 341 ? 71.005  141.030 23.892  1.00 44.33  ? 341 THR D CB  1 
ATOM   13246 O  OG1 . THR D  1 341 ? 70.278  140.630 22.720  1.00 52.06  ? 341 THR D OG1 1 
ATOM   13247 C  CG2 . THR D  1 341 ? 72.232  140.179 24.009  1.00 41.28  ? 341 THR D CG2 1 
ATOM   13248 N  N   . ASP D  1 342 ? 67.808  141.538 24.818  1.00 44.25  ? 342 ASP D N   1 
ATOM   13249 C  CA  . ASP D  1 342 ? 66.791  142.550 24.789  1.00 43.22  ? 342 ASP D CA  1 
ATOM   13250 C  C   . ASP D  1 342 ? 66.281  143.043 26.135  1.00 44.97  ? 342 ASP D C   1 
ATOM   13251 O  O   . ASP D  1 342 ? 65.335  143.824 26.192  1.00 54.23  ? 342 ASP D O   1 
ATOM   13252 C  CB  . ASP D  1 342 ? 65.645  142.103 23.885  1.00 45.51  ? 342 ASP D CB  1 
ATOM   13253 C  CG  . ASP D  1 342 ? 64.727  141.100 24.548  1.00 41.62  ? 342 ASP D CG  1 
ATOM   13254 O  OD1 . ASP D  1 342 ? 65.119  140.516 25.572  1.00 39.60  ? 342 ASP D OD1 1 
ATOM   13255 O  OD2 . ASP D  1 342 ? 63.600  140.905 24.046  1.00 38.07  ? 342 ASP D OD2 1 
ATOM   13256 N  N   . GLY D  1 343 ? 66.859  142.569 27.224  1.00 42.19  ? 343 GLY D N   1 
ATOM   13257 C  CA  . GLY D  1 343 ? 66.391  143.019 28.521  1.00 41.29  ? 343 GLY D CA  1 
ATOM   13258 C  C   . GLY D  1 343 ? 64.926  142.808 28.915  1.00 43.55  ? 343 GLY D C   1 
ATOM   13259 O  O   . GLY D  1 343 ? 64.485  143.283 29.957  1.00 45.97  ? 343 GLY D O   1 
ATOM   13260 N  N   . LEU D  1 344 ? 64.152  142.082 28.126  1.00 48.45  ? 344 LEU D N   1 
ATOM   13261 C  CA  . LEU D  1 344 ? 62.748  141.830 28.491  1.00 55.46  ? 344 LEU D CA  1 
ATOM   13262 C  C   . LEU D  1 344 ? 62.597  140.601 29.434  1.00 56.93  ? 344 LEU D C   1 
ATOM   13263 O  O   . LEU D  1 344 ? 61.987  139.544 29.068  1.00 62.84  ? 344 LEU D O   1 
ATOM   13264 C  CB  . LEU D  1 344 ? 61.934  141.632 27.218  1.00 60.90  ? 344 LEU D CB  1 
ATOM   13265 C  CG  . LEU D  1 344 ? 61.840  142.875 26.343  1.00 61.20  ? 344 LEU D CG  1 
ATOM   13266 C  CD1 . LEU D  1 344 ? 61.117  142.569 25.047  1.00 65.92  ? 344 LEU D CD1 1 
ATOM   13267 C  CD2 . LEU D  1 344 ? 61.092  143.912 27.120  1.00 62.44  ? 344 LEU D CD2 1 
ATOM   13268 N  N   . CYS D  1 345 ? 63.124  140.737 30.650  1.00 46.97  ? 345 CYS D N   1 
ATOM   13269 C  CA  . CYS D  1 345 ? 63.057  139.639 31.568  1.00 37.23  ? 345 CYS D CA  1 
ATOM   13270 C  C   . CYS D  1 345 ? 62.289  139.911 32.834  1.00 34.55  ? 345 CYS D C   1 
ATOM   13271 O  O   . CYS D  1 345 ? 62.760  139.649 33.931  1.00 35.97  ? 345 CYS D O   1 
ATOM   13272 C  CB  . CYS D  1 345 ? 64.452  139.172 31.874  1.00 37.85  ? 345 CYS D CB  1 
ATOM   13273 S  SG  . CYS D  1 345 ? 65.352  140.433 32.587  1.00 31.42  ? 345 CYS D SG  1 
ATOM   13274 N  N   . THR D  1 346 ? 61.076  140.407 32.696  1.00 34.32  ? 346 THR D N   1 
ATOM   13275 C  CA  . THR D  1 346 ? 60.281  140.651 33.877  1.00 35.35  ? 346 THR D CA  1 
ATOM   13276 C  C   . THR D  1 346 ? 58.852  140.208 33.677  1.00 34.98  ? 346 THR D C   1 
ATOM   13277 O  O   . THR D  1 346 ? 58.199  140.508 32.673  1.00 38.41  ? 346 THR D O   1 
ATOM   13278 C  CB  . THR D  1 346 ? 60.350  142.109 34.288  1.00 39.76  ? 346 THR D CB  1 
ATOM   13279 O  OG1 . THR D  1 346 ? 61.722  142.462 34.514  1.00 46.28  ? 346 THR D OG1 1 
ATOM   13280 C  CG2 . THR D  1 346 ? 59.544  142.331 35.563  1.00 38.55  ? 346 THR D CG2 1 
ATOM   13281 N  N   . PRO D  1 347 ? 58.371  139.410 34.606  1.00 33.47  ? 347 PRO D N   1 
ATOM   13282 C  CA  . PRO D  1 347 ? 57.020  138.878 34.583  1.00 34.53  ? 347 PRO D CA  1 
ATOM   13283 C  C   . PRO D  1 347 ? 56.016  140.007 34.414  1.00 38.15  ? 347 PRO D C   1 
ATOM   13284 O  O   . PRO D  1 347 ? 55.949  140.925 35.245  1.00 45.82  ? 347 PRO D O   1 
ATOM   13285 C  CB  . PRO D  1 347 ? 56.894  138.243 35.971  1.00 33.21  ? 347 PRO D CB  1 
ATOM   13286 C  CG  . PRO D  1 347 ? 58.277  137.865 36.312  1.00 30.85  ? 347 PRO D CG  1 
ATOM   13287 C  CD  . PRO D  1 347 ? 59.112  138.980 35.801  1.00 36.24  ? 347 PRO D CD  1 
ATOM   13288 N  N   . VAL D  1 348 ? 55.195  139.908 33.384  1.00 38.50  ? 348 VAL D N   1 
ATOM   13289 C  CA  . VAL D  1 348 ? 54.172  140.904 33.116  1.00 41.36  ? 348 VAL D CA  1 
ATOM   13290 C  C   . VAL D  1 348 ? 52.813  140.245 33.194  1.00 43.99  ? 348 VAL D C   1 
ATOM   13291 O  O   . VAL D  1 348 ? 52.704  139.059 32.904  1.00 49.63  ? 348 VAL D O   1 
ATOM   13292 C  CB  . VAL D  1 348 ? 54.353  141.449 31.731  1.00 43.64  ? 348 VAL D CB  1 
ATOM   13293 C  CG1 . VAL D  1 348 ? 55.697  142.139 31.637  1.00 53.53  ? 348 VAL D CG1 1 
ATOM   13294 C  CG2 . VAL D  1 348 ? 54.299  140.326 30.723  1.00 50.36  ? 348 VAL D CG2 1 
ATOM   13295 N  N   . LYS D  1 349 ? 51.765  140.962 33.599  1.00 48.34  ? 349 LYS D N   1 
ATOM   13296 C  CA  . LYS D  1 349 ? 50.458  140.296 33.665  1.00 51.11  ? 349 LYS D CA  1 
ATOM   13297 C  C   . LYS D  1 349 ? 50.104  139.778 32.267  1.00 50.25  ? 349 LYS D C   1 
ATOM   13298 O  O   . LYS D  1 349 ? 50.406  140.427 31.259  1.00 53.16  ? 349 LYS D O   1 
ATOM   13299 C  CB  . LYS D  1 349 ? 49.344  141.206 34.206  1.00 57.70  ? 349 LYS D CB  1 
ATOM   13300 C  CG  . LYS D  1 349 ? 47.947  140.472 34.294  1.00 72.59  ? 349 LYS D CG  1 
ATOM   13301 C  CD  . LYS D  1 349 ? 46.902  141.121 35.239  1.00 81.05  ? 349 LYS D CD  1 
ATOM   13302 C  CE  . LYS D  1 349 ? 47.308  141.082 36.730  1.00 85.94  ? 349 LYS D CE  1 
ATOM   13303 N  NZ  . LYS D  1 349 ? 48.452  142.017 37.151  1.00 86.91  ? 349 LYS D NZ  1 
ATOM   13304 N  N   . ASP D  1 350 ? 49.526  138.586 32.206  1.00 47.38  ? 350 ASP D N   1 
ATOM   13305 C  CA  . ASP D  1 350 ? 49.150  137.982 30.942  1.00 43.01  ? 350 ASP D CA  1 
ATOM   13306 C  C   . ASP D  1 350 ? 47.881  137.212 31.225  1.00 41.86  ? 350 ASP D C   1 
ATOM   13307 O  O   . ASP D  1 350 ? 47.867  136.336 32.076  1.00 43.58  ? 350 ASP D O   1 
ATOM   13308 C  CB  . ASP D  1 350 ? 50.264  137.050 30.468  1.00 39.98  ? 350 ASP D CB  1 
ATOM   13309 C  CG  . ASP D  1 350 ? 50.131  136.680 29.012  1.00 44.54  ? 350 ASP D CG  1 
ATOM   13310 O  OD1 . ASP D  1 350 ? 48.976  136.453 28.550  1.00 45.01  ? 350 ASP D OD1 1 
ATOM   13311 O  OD2 . ASP D  1 350 ? 51.185  136.608 28.334  1.00 43.99  ? 350 ASP D OD2 1 
ATOM   13312 N  N   . GLN D  1 351 ? 46.805  137.537 30.529  1.00 42.06  ? 351 GLN D N   1 
ATOM   13313 C  CA  . GLN D  1 351 ? 45.565  136.845 30.804  1.00 45.49  ? 351 GLN D CA  1 
ATOM   13314 C  C   . GLN D  1 351 ? 45.416  135.540 30.068  1.00 45.19  ? 351 GLN D C   1 
ATOM   13315 O  O   . GLN D  1 351 ? 44.339  134.951 30.035  1.00 46.33  ? 351 GLN D O   1 
ATOM   13316 C  CB  . GLN D  1 351 ? 44.348  137.750 30.588  1.00 50.73  ? 351 GLN D CB  1 
ATOM   13317 C  CG  . GLN D  1 351 ? 44.210  138.900 31.603  1.00 55.74  ? 351 GLN D CG  1 
ATOM   13318 C  CD  . GLN D  1 351 ? 43.661  138.479 32.952  1.00 57.82  ? 351 GLN D CD  1 
ATOM   13319 O  OE1 . GLN D  1 351 ? 42.513  138.043 33.048  1.00 62.64  ? 351 GLN D OE1 1 
ATOM   13320 N  NE2 . GLN D  1 351 ? 44.470  138.636 34.009  1.00 60.24  ? 351 GLN D NE2 1 
ATOM   13321 N  N   . SER D  1 352 ? 46.479  135.110 29.421  1.00 45.73  ? 352 SER D N   1 
ATOM   13322 C  CA  . SER D  1 352 ? 46.424  133.833 28.743  1.00 47.00  ? 352 SER D CA  1 
ATOM   13323 C  C   . SER D  1 352 ? 47.218  132.862 29.561  1.00 45.84  ? 352 SER D C   1 
ATOM   13324 O  O   . SER D  1 352 ? 47.118  131.657 29.364  1.00 50.65  ? 352 SER D O   1 
ATOM   13325 C  CB  . SER D  1 352 ? 47.034  133.926 27.369  1.00 50.76  ? 352 SER D CB  1 
ATOM   13326 O  OG  . SER D  1 352 ? 46.111  134.536 26.501  1.00 66.59  ? 352 SER D OG  1 
ATOM   13327 N  N   . ALA D  1 353 ? 48.038  133.408 30.453  1.00 40.88  ? 353 ALA D N   1 
ATOM   13328 C  CA  . ALA D  1 353 ? 48.881  132.607 31.290  1.00 31.44  ? 353 ALA D CA  1 
ATOM   13329 C  C   . ALA D  1 353 ? 48.028  132.057 32.355  1.00 29.13  ? 353 ALA D C   1 
ATOM   13330 O  O   . ALA D  1 353 ? 47.016  132.613 32.717  1.00 30.39  ? 353 ALA D O   1 
ATOM   13331 C  CB  . ALA D  1 353 ? 49.966  133.445 31.900  1.00 35.51  ? 353 ALA D CB  1 
ATOM   13332 N  N   . PRO D  1 354 ? 48.405  130.913 32.843  1.00 30.30  ? 354 PRO D N   1 
ATOM   13333 C  CA  . PRO D  1 354 ? 47.664  130.254 33.913  1.00 33.58  ? 354 PRO D CA  1 
ATOM   13334 C  C   . PRO D  1 354 ? 48.012  130.930 35.245  1.00 35.11  ? 354 PRO D C   1 
ATOM   13335 O  O   . PRO D  1 354 ? 48.892  131.808 35.299  1.00 34.57  ? 354 PRO D O   1 
ATOM   13336 C  CB  . PRO D  1 354 ? 48.267  128.845 33.892  1.00 29.90  ? 354 PRO D CB  1 
ATOM   13337 C  CG  . PRO D  1 354 ? 49.727  129.124 33.486  1.00 24.23  ? 354 PRO D CG  1 
ATOM   13338 C  CD  . PRO D  1 354 ? 49.498  130.068 32.338  1.00 26.69  ? 354 PRO D CD  1 
ATOM   13339 N  N   . VAL D  1 355 ? 47.343  130.479 36.305  1.00 33.83  ? 355 VAL D N   1 
ATOM   13340 C  CA  . VAL D  1 355 ? 47.610  130.922 37.666  1.00 35.48  ? 355 VAL D CA  1 
ATOM   13341 C  C   . VAL D  1 355 ? 48.531  129.811 38.238  1.00 38.43  ? 355 VAL D C   1 
ATOM   13342 O  O   . VAL D  1 355 ? 48.148  128.631 38.190  1.00 38.40  ? 355 VAL D O   1 
ATOM   13343 C  CB  . VAL D  1 355 ? 46.306  130.943 38.487  1.00 36.48  ? 355 VAL D CB  1 
ATOM   13344 C  CG1 . VAL D  1 355 ? 46.557  131.438 39.909  1.00 31.96  ? 355 VAL D CG1 1 
ATOM   13345 C  CG2 . VAL D  1 355 ? 45.286  131.797 37.792  1.00 40.47  ? 355 VAL D CG2 1 
ATOM   13346 N  N   . TYR D  1 356 ? 49.742  130.163 38.701  1.00 36.81  ? 356 TYR D N   1 
ATOM   13347 C  CA  . TYR D  1 356 ? 50.671  129.194 39.280  1.00 34.38  ? 356 TYR D CA  1 
ATOM   13348 C  C   . TYR D  1 356 ? 50.457  129.126 40.802  1.00 38.41  ? 356 TYR D C   1 
ATOM   13349 O  O   . TYR D  1 356 ? 50.742  130.080 41.499  1.00 44.45  ? 356 TYR D O   1 
ATOM   13350 C  CB  . TYR D  1 356 ? 52.128  129.552 38.964  1.00 31.32  ? 356 TYR D CB  1 
ATOM   13351 C  CG  . TYR D  1 356 ? 52.446  129.611 37.509  1.00 32.42  ? 356 TYR D CG  1 
ATOM   13352 C  CD1 . TYR D  1 356 ? 52.113  130.712 36.768  1.00 41.00  ? 356 TYR D CD1 1 
ATOM   13353 C  CD2 . TYR D  1 356 ? 53.055  128.558 36.856  1.00 36.34  ? 356 TYR D CD2 1 
ATOM   13354 C  CE1 . TYR D  1 356 ? 52.371  130.779 35.417  1.00 39.69  ? 356 TYR D CE1 1 
ATOM   13355 C  CE2 . TYR D  1 356 ? 53.319  128.613 35.479  1.00 32.90  ? 356 TYR D CE2 1 
ATOM   13356 C  CZ  . TYR D  1 356 ? 52.973  129.729 34.789  1.00 34.21  ? 356 TYR D CZ  1 
ATOM   13357 O  OH  . TYR D  1 356 ? 53.258  129.860 33.469  1.00 44.27  ? 356 TYR D OH  1 
ATOM   13358 N  N   . ILE D  1 357 ? 49.907  128.022 41.307  1.00 39.06  ? 357 ILE D N   1 
ATOM   13359 C  CA  . ILE D  1 357 ? 49.645  127.852 42.748  1.00 35.21  ? 357 ILE D CA  1 
ATOM   13360 C  C   . ILE D  1 357 ? 50.657  126.821 43.271  1.00 36.42  ? 357 ILE D C   1 
ATOM   13361 O  O   . ILE D  1 357 ? 51.116  125.971 42.479  1.00 39.66  ? 357 ILE D O   1 
ATOM   13362 C  CB  . ILE D  1 357 ? 48.179  127.332 42.998  1.00 31.23  ? 357 ILE D CB  1 
ATOM   13363 C  CG1 . ILE D  1 357 ? 47.179  128.441 42.738  1.00 24.82  ? 357 ILE D CG1 1 
ATOM   13364 C  CG2 . ILE D  1 357 ? 47.959  126.884 44.428  1.00 27.40  ? 357 ILE D CG2 1 
ATOM   13365 C  CD1 . ILE D  1 357 ? 45.748  127.971 42.864  1.00 29.28  ? 357 ILE D CD1 1 
ATOM   13366 N  N   . THR D  1 358 ? 51.068  126.941 44.547  1.00 30.60  ? 358 THR D N   1 
ATOM   13367 C  CA  . THR D  1 358 ? 51.981  125.986 45.132  1.00 26.00  ? 358 THR D CA  1 
ATOM   13368 C  C   . THR D  1 358 ? 51.469  125.507 46.475  1.00 27.49  ? 358 THR D C   1 
ATOM   13369 O  O   . THR D  1 358 ? 51.276  126.336 47.352  1.00 32.49  ? 358 THR D O   1 
ATOM   13370 C  CB  . THR D  1 358 ? 53.436  126.519 45.194  1.00 27.83  ? 358 THR D CB  1 
ATOM   13371 O  OG1 . THR D  1 358 ? 53.813  126.803 46.532  1.00 22.44  ? 358 THR D OG1 1 
ATOM   13372 C  CG2 . THR D  1 358 ? 53.667  127.687 44.244  1.00 20.42  ? 358 THR D CG2 1 
ATOM   13373 N  N   . ILE D  1 359 ? 51.134  124.210 46.596  1.00 27.12  ? 359 ILE D N   1 
ATOM   13374 C  CA  . ILE D  1 359 ? 50.597  123.638 47.846  1.00 27.64  ? 359 ILE D CA  1 
ATOM   13375 C  C   . ILE D  1 359 ? 51.437  122.510 48.435  1.00 31.70  ? 359 ILE D C   1 
ATOM   13376 O  O   . ILE D  1 359 ? 50.920  121.434 48.765  1.00 31.79  ? 359 ILE D O   1 
ATOM   13377 C  CB  . ILE D  1 359 ? 49.143  123.053 47.727  1.00 28.12  ? 359 ILE D CB  1 
ATOM   13378 C  CG1 . ILE D  1 359 ? 48.966  122.331 46.420  1.00 30.66  ? 359 ILE D CG1 1 
ATOM   13379 C  CG2 . ILE D  1 359 ? 48.041  124.075 48.029  1.00 18.73  ? 359 ILE D CG2 1 
ATOM   13380 C  CD1 . ILE D  1 359 ? 48.819  123.223 45.293  1.00 48.39  ? 359 ILE D CD1 1 
ATOM   13381 N  N   . GLY D  1 360 ? 52.725  122.753 48.610  1.00 35.33  ? 360 GLY D N   1 
ATOM   13382 C  CA  . GLY D  1 360 ? 53.567  121.729 49.211  1.00 38.64  ? 360 GLY D CA  1 
ATOM   13383 C  C   . GLY D  1 360 ? 53.607  121.887 50.728  1.00 38.14  ? 360 GLY D C   1 
ATOM   13384 O  O   . GLY D  1 360 ? 54.563  121.501 51.427  1.00 37.14  ? 360 GLY D O   1 
ATOM   13385 N  N   . ASP D  1 361 ? 52.508  122.379 51.263  1.00 41.02  ? 361 ASP D N   1 
ATOM   13386 C  CA  . ASP D  1 361 ? 52.455  122.623 52.685  1.00 41.17  ? 361 ASP D CA  1 
ATOM   13387 C  C   . ASP D  1 361 ? 51.573  121.619 53.423  1.00 38.43  ? 361 ASP D C   1 
ATOM   13388 O  O   . ASP D  1 361 ? 51.001  121.965 54.440  1.00 41.08  ? 361 ASP D O   1 
ATOM   13389 C  CB  . ASP D  1 361 ? 51.952  124.053 52.907  1.00 37.42  ? 361 ASP D CB  1 
ATOM   13390 C  CG  . ASP D  1 361 ? 50.511  124.220 52.475  1.00 37.62  ? 361 ASP D CG  1 
ATOM   13391 O  OD1 . ASP D  1 361 ? 50.103  123.475 51.578  1.00 33.04  ? 361 ASP D OD1 1 
ATOM   13392 O  OD2 . ASP D  1 361 ? 49.770  125.029 53.068  1.00 43.19  ? 361 ASP D OD2 1 
ATOM   13393 N  N   . ALA D  1 362 ? 51.457  120.388 52.946  1.00 33.47  ? 362 ALA D N   1 
ATOM   13394 C  CA  . ALA D  1 362 ? 50.588  119.465 53.648  1.00 30.05  ? 362 ALA D CA  1 
ATOM   13395 C  C   . ALA D  1 362 ? 51.215  118.853 54.878  1.00 28.21  ? 362 ALA D C   1 
ATOM   13396 O  O   . ALA D  1 362 ? 50.512  118.150 55.609  1.00 27.60  ? 362 ALA D O   1 
ATOM   13397 C  CB  . ALA D  1 362 ? 50.070  118.387 52.733  1.00 36.81  ? 362 ALA D CB  1 
ATOM   13398 N  N   . GLY D  1 363 ? 52.526  119.037 55.093  1.00 22.88  ? 363 GLY D N   1 
ATOM   13399 C  CA  . GLY D  1 363 ? 53.081  118.464 56.303  1.00 23.42  ? 363 GLY D CA  1 
ATOM   13400 C  C   . GLY D  1 363 ? 54.518  118.029 56.351  1.00 29.60  ? 363 GLY D C   1 
ATOM   13401 O  O   . GLY D  1 363 ? 55.286  118.361 57.277  1.00 28.48  ? 363 GLY D O   1 
ATOM   13402 N  N   . ASN D  1 364 ? 54.920  117.313 55.321  1.00 29.97  ? 364 ASN D N   1 
ATOM   13403 C  CA  . ASN D  1 364 ? 56.264  116.758 55.279  1.00 31.13  ? 364 ASN D CA  1 
ATOM   13404 C  C   . ASN D  1 364 ? 56.644  116.210 56.626  1.00 30.96  ? 364 ASN D C   1 
ATOM   13405 O  O   . ASN D  1 364 ? 55.818  115.585 57.303  1.00 29.50  ? 364 ASN D O   1 
ATOM   13406 C  CB  . ASN D  1 364 ? 57.331  117.722 54.714  1.00 35.03  ? 364 ASN D CB  1 
ATOM   13407 C  CG  . ASN D  1 364 ? 57.402  118.988 55.430  1.00 34.66  ? 364 ASN D CG  1 
ATOM   13408 O  OD1 . ASN D  1 364 ? 56.632  119.921 55.163  1.00 37.82  ? 364 ASN D OD1 1 
ATOM   13409 N  ND2 . ASN D  1 364 ? 58.355  119.075 56.328  1.00 39.53  ? 364 ASN D ND2 1 
ATOM   13410 N  N   . TYR D  1 365 ? 57.879  116.439 57.032  1.00 29.55  ? 365 TYR D N   1 
ATOM   13411 C  CA  . TYR D  1 365 ? 58.314  115.919 58.301  1.00 30.46  ? 365 TYR D CA  1 
ATOM   13412 C  C   . TYR D  1 365 ? 58.153  116.963 59.346  1.00 32.58  ? 365 TYR D C   1 
ATOM   13413 O  O   . TYR D  1 365 ? 58.988  117.064 60.245  1.00 28.94  ? 365 TYR D O   1 
ATOM   13414 C  CB  . TYR D  1 365 ? 59.755  115.479 58.247  1.00 28.15  ? 365 TYR D CB  1 
ATOM   13415 C  CG  . TYR D  1 365 ? 60.617  116.418 57.481  1.00 30.82  ? 365 TYR D CG  1 
ATOM   13416 C  CD1 . TYR D  1 365 ? 60.625  116.409 56.101  1.00 30.21  ? 365 TYR D CD1 1 
ATOM   13417 C  CD2 . TYR D  1 365 ? 61.478  117.272 58.134  1.00 36.39  ? 365 TYR D CD2 1 
ATOM   13418 C  CE1 . TYR D  1 365 ? 61.457  117.219 55.388  1.00 36.18  ? 365 TYR D CE1 1 
ATOM   13419 C  CE2 . TYR D  1 365 ? 62.345  118.093 57.424  1.00 38.56  ? 365 TYR D CE2 1 
ATOM   13420 C  CZ  . TYR D  1 365 ? 62.329  118.060 56.047  1.00 41.19  ? 365 TYR D CZ  1 
ATOM   13421 O  OH  . TYR D  1 365 ? 63.190  118.860 55.314  1.00 56.87  ? 365 TYR D OH  1 
ATOM   13422 N  N   . GLY D  1 366 ? 57.063  117.717 59.228  1.00 35.94  ? 366 GLY D N   1 
ATOM   13423 C  CA  . GLY D  1 366 ? 56.763  118.763 60.189  1.00 43.86  ? 366 GLY D CA  1 
ATOM   13424 C  C   . GLY D  1 366 ? 57.519  120.092 60.088  1.00 43.97  ? 366 GLY D C   1 
ATOM   13425 O  O   . GLY D  1 366 ? 57.669  120.798 61.072  1.00 49.36  ? 366 GLY D O   1 
ATOM   13426 N  N   . VAL D  1 367 ? 57.931  120.487 58.898  1.00 40.95  ? 367 VAL D N   1 
ATOM   13427 C  CA  . VAL D  1 367 ? 58.645  121.742 58.756  1.00 37.03  ? 367 VAL D CA  1 
ATOM   13428 C  C   . VAL D  1 367 ? 58.063  122.678 57.692  1.00 40.73  ? 367 VAL D C   1 
ATOM   13429 O  O   . VAL D  1 367 ? 57.742  122.258 56.583  1.00 46.45  ? 367 VAL D O   1 
ATOM   13430 C  CB  . VAL D  1 367 ? 60.074  121.474 58.460  1.00 29.03  ? 367 VAL D CB  1 
ATOM   13431 C  CG1 . VAL D  1 367 ? 60.708  122.672 57.817  1.00 34.33  ? 367 VAL D CG1 1 
ATOM   13432 C  CG2 . VAL D  1 367 ? 60.737  121.169 59.714  1.00 21.63  ? 367 VAL D CG2 1 
ATOM   13433 N  N   . ILE D  1 368 ? 57.982  123.955 58.031  1.00 40.28  ? 368 ILE D N   1 
ATOM   13434 C  CA  . ILE D  1 368 ? 57.464  124.972 57.134  1.00 41.22  ? 368 ILE D CA  1 
ATOM   13435 C  C   . ILE D  1 368 ? 58.556  125.923 56.605  1.00 43.48  ? 368 ILE D C   1 
ATOM   13436 O  O   . ILE D  1 368 ? 59.522  126.202 57.303  1.00 47.02  ? 368 ILE D O   1 
ATOM   13437 C  CB  . ILE D  1 368 ? 56.411  125.794 57.847  1.00 39.00  ? 368 ILE D CB  1 
ATOM   13438 C  CG1 . ILE D  1 368 ? 55.073  125.062 57.863  1.00 43.66  ? 368 ILE D CG1 1 
ATOM   13439 C  CG2 . ILE D  1 368 ? 56.210  127.087 57.137  1.00 43.24  ? 368 ILE D CG2 1 
ATOM   13440 C  CD1 . ILE D  1 368 ? 54.210  125.274 56.585  1.00 43.11  ? 368 ILE D CD1 1 
ATOM   13441 N  N   . ASP D  1 369 ? 58.426  126.367 55.350  1.00 47.39  ? 369 ASP D N   1 
ATOM   13442 C  CA  . ASP D  1 369 ? 59.362  127.321 54.743  1.00 48.96  ? 369 ASP D CA  1 
ATOM   13443 C  C   . ASP D  1 369 ? 58.733  128.681 54.944  1.00 53.10  ? 369 ASP D C   1 
ATOM   13444 O  O   . ASP D  1 369 ? 57.742  129.029 54.288  1.00 51.48  ? 369 ASP D O   1 
ATOM   13445 C  CB  . ASP D  1 369 ? 59.511  127.081 53.261  1.00 46.23  ? 369 ASP D CB  1 
ATOM   13446 C  CG  . ASP D  1 369 ? 60.211  125.816 52.977  1.00 45.71  ? 369 ASP D CG  1 
ATOM   13447 O  OD1 . ASP D  1 369 ? 61.191  125.533 53.694  1.00 40.76  ? 369 ASP D OD1 1 
ATOM   13448 O  OD2 . ASP D  1 369 ? 59.770  125.098 52.061  1.00 45.92  ? 369 ASP D OD2 1 
ATOM   13449 N  N   . SER D  1 370 ? 59.324  129.449 55.851  1.00 57.00  ? 370 SER D N   1 
ATOM   13450 C  CA  . SER D  1 370 ? 58.801  130.755 56.204  1.00 58.32  ? 370 SER D CA  1 
ATOM   13451 C  C   . SER D  1 370 ? 59.535  131.899 55.558  1.00 56.86  ? 370 SER D C   1 
ATOM   13452 O  O   . SER D  1 370 ? 58.983  132.994 55.447  1.00 63.05  ? 370 SER D O   1 
ATOM   13453 C  CB  . SER D  1 370 ? 58.816  130.932 57.715  1.00 58.29  ? 370 SER D CB  1 
ATOM   13454 O  OG  . SER D  1 370 ? 60.154  130.882 58.194  1.00 66.68  ? 370 SER D OG  1 
ATOM   13455 N  N   . ASN D  1 371 ? 60.767  131.662 55.126  1.00 55.21  ? 371 ASN D N   1 
ATOM   13456 C  CA  . ASN D  1 371 ? 61.510  132.731 54.494  1.00 54.46  ? 371 ASN D CA  1 
ATOM   13457 C  C   . ASN D  1 371 ? 61.047  132.991 53.061  1.00 51.75  ? 371 ASN D C   1 
ATOM   13458 O  O   . ASN D  1 371 ? 61.057  132.101 52.191  1.00 55.30  ? 371 ASN D O   1 
ATOM   13459 C  CB  . ASN D  1 371 ? 63.006  132.480 54.578  1.00 64.23  ? 371 ASN D CB  1 
ATOM   13460 C  CG  . ASN D  1 371 ? 63.825  133.778 54.633  1.00 78.60  ? 371 ASN D CG  1 
ATOM   13461 O  OD1 . ASN D  1 371 ? 65.054  133.754 54.451  1.00 84.42  ? 371 ASN D OD1 1 
ATOM   13462 N  ND2 . ASN D  1 371 ? 63.159  134.917 54.909  1.00 90.13  ? 371 ASN D ND2 1 
ATOM   13463 N  N   . MET D  1 372 ? 60.585  134.219 52.858  1.00 48.56  ? 372 MET D N   1 
ATOM   13464 C  CA  . MET D  1 372 ? 60.088  134.701 51.590  1.00 45.32  ? 372 MET D CA  1 
ATOM   13465 C  C   . MET D  1 372 ? 60.980  135.828 51.176  1.00 45.47  ? 372 MET D C   1 
ATOM   13466 O  O   . MET D  1 372 ? 61.651  136.454 51.996  1.00 46.67  ? 372 MET D O   1 
ATOM   13467 C  CB  . MET D  1 372 ? 58.698  135.238 51.773  1.00 37.91  ? 372 MET D CB  1 
ATOM   13468 C  CG  . MET D  1 372 ? 58.020  134.466 52.834  1.00 39.19  ? 372 MET D CG  1 
ATOM   13469 S  SD  . MET D  1 372 ? 56.378  134.972 53.111  1.00 43.46  ? 372 MET D SD  1 
ATOM   13470 C  CE  . MET D  1 372 ? 55.630  133.477 53.851  1.00 42.35  ? 372 MET D CE  1 
ATOM   13471 N  N   . ILE D  1 373 ? 61.100  135.989 49.879  1.00 46.98  ? 373 ILE D N   1 
ATOM   13472 C  CA  . ILE D  1 373 ? 61.888  137.065 49.349  1.00 49.05  ? 373 ILE D CA  1 
ATOM   13473 C  C   . ILE D  1 373 ? 61.105  138.301 49.743  1.00 51.41  ? 373 ILE D C   1 
ATOM   13474 O  O   . ILE D  1 373 ? 59.903  138.371 49.512  1.00 47.19  ? 373 ILE D O   1 
ATOM   13475 C  CB  . ILE D  1 373 ? 61.897  137.005 47.825  1.00 48.19  ? 373 ILE D CB  1 
ATOM   13476 C  CG1 . ILE D  1 373 ? 62.986  136.066 47.327  1.00 46.30  ? 373 ILE D CG1 1 
ATOM   13477 C  CG2 . ILE D  1 373 ? 61.909  138.397 47.221  1.00 51.53  ? 373 ILE D CG2 1 
ATOM   13478 C  CD1 . ILE D  1 373 ? 62.400  134.812 46.733  1.00 53.44  ? 373 ILE D CD1 1 
ATOM   13479 N  N   . GLN D  1 374 ? 61.755  139.252 50.392  1.00 56.84  ? 374 GLN D N   1 
ATOM   13480 C  CA  . GLN D  1 374 ? 61.045  140.476 50.728  1.00 61.24  ? 374 GLN D CA  1 
ATOM   13481 C  C   . GLN D  1 374 ? 61.529  141.534 49.740  1.00 63.43  ? 374 GLN D C   1 
ATOM   13482 O  O   . GLN D  1 374 ? 62.698  141.513 49.355  1.00 66.41  ? 374 GLN D O   1 
ATOM   13483 C  CB  . GLN D  1 374 ? 61.318  140.896 52.166  1.00 60.03  ? 374 GLN D CB  1 
ATOM   13484 C  CG  . GLN D  1 374 ? 60.847  139.880 53.180  1.00 62.50  ? 374 GLN D CG  1 
ATOM   13485 C  CD  . GLN D  1 374 ? 59.378  139.466 53.002  1.00 65.07  ? 374 GLN D CD  1 
ATOM   13486 O  OE1 . GLN D  1 374 ? 58.956  138.434 53.542  1.00 73.85  ? 374 GLN D OE1 1 
ATOM   13487 N  NE2 . GLN D  1 374 ? 58.590  140.273 52.277  1.00 63.28  ? 374 GLN D NE2 1 
ATOM   13488 N  N   . PRO D  1 375 ? 60.608  142.339 49.168  1.00 63.38  ? 375 PRO D N   1 
ATOM   13489 C  CA  . PRO D  1 375 ? 59.151  142.334 49.339  1.00 61.36  ? 375 PRO D CA  1 
ATOM   13490 C  C   . PRO D  1 375 ? 58.431  141.459 48.301  1.00 60.07  ? 375 PRO D C   1 
ATOM   13491 O  O   . PRO D  1 375 ? 58.957  141.190 47.195  1.00 56.94  ? 375 PRO D O   1 
ATOM   13492 C  CB  . PRO D  1 375 ? 58.802  143.795 49.134  1.00 63.36  ? 375 PRO D CB  1 
ATOM   13493 C  CG  . PRO D  1 375 ? 59.745  144.174 47.999  1.00 60.09  ? 375 PRO D CG  1 
ATOM   13494 C  CD  . PRO D  1 375 ? 61.046  143.545 48.433  1.00 60.84  ? 375 PRO D CD  1 
ATOM   13495 N  N   . GLN D  1 376 ? 57.197  141.098 48.648  1.00 58.73  ? 376 GLN D N   1 
ATOM   13496 C  CA  . GLN D  1 376 ? 56.366  140.262 47.817  1.00 59.62  ? 376 GLN D CA  1 
ATOM   13497 C  C   . GLN D  1 376 ? 56.368  140.848 46.432  1.00 58.12  ? 376 GLN D C   1 
ATOM   13498 O  O   . GLN D  1 376 ? 55.942  141.977 46.238  1.00 58.45  ? 376 GLN D O   1 
ATOM   13499 C  CB  . GLN D  1 376 ? 54.944  140.191 48.363  1.00 62.44  ? 376 GLN D CB  1 
ATOM   13500 C  CG  . GLN D  1 376 ? 54.009  139.390 47.482  1.00 71.82  ? 376 GLN D CG  1 
ATOM   13501 C  CD  . GLN D  1 376 ? 52.684  139.050 48.157  1.00 76.94  ? 376 GLN D CD  1 
ATOM   13502 O  OE1 . GLN D  1 376 ? 52.517  139.215 49.372  1.00 76.38  ? 376 GLN D OE1 1 
ATOM   13503 N  NE2 . GLN D  1 376 ? 51.736  138.545 47.370  1.00 84.50  ? 376 GLN D NE2 1 
ATOM   13504 N  N   . PRO D  1 377 ? 56.927  140.114 45.461  1.00 58.24  ? 377 PRO D N   1 
ATOM   13505 C  CA  . PRO D  1 377 ? 56.985  140.585 44.089  1.00 55.33  ? 377 PRO D CA  1 
ATOM   13506 C  C   . PRO D  1 377 ? 55.587  140.660 43.501  1.00 53.44  ? 377 PRO D C   1 
ATOM   13507 O  O   . PRO D  1 377 ? 54.659  139.987 43.942  1.00 51.84  ? 377 PRO D O   1 
ATOM   13508 C  CB  . PRO D  1 377 ? 57.825  139.522 43.422  1.00 55.11  ? 377 PRO D CB  1 
ATOM   13509 C  CG  . PRO D  1 377 ? 57.387  138.294 44.135  1.00 54.55  ? 377 PRO D CG  1 
ATOM   13510 C  CD  . PRO D  1 377 ? 57.466  138.751 45.551  1.00 58.29  ? 377 PRO D CD  1 
ATOM   13511 N  N   . GLU D  1 378 ? 55.482  141.499 42.485  1.00 53.70  ? 378 GLU D N   1 
ATOM   13512 C  CA  . GLU D  1 378 ? 54.256  141.772 41.770  1.00 55.17  ? 378 GLU D CA  1 
ATOM   13513 C  C   . GLU D  1 378 ? 53.520  140.525 41.362  1.00 54.67  ? 378 GLU D C   1 
ATOM   13514 O  O   . GLU D  1 378 ? 52.321  140.431 41.599  1.00 60.61  ? 378 GLU D O   1 
ATOM   13515 C  CB  . GLU D  1 378 ? 54.523  142.597 40.502  1.00 67.20  ? 378 GLU D CB  1 
ATOM   13516 C  CG  . GLU D  1 378 ? 55.825  143.453 40.468  1.00 87.41  ? 378 GLU D CG  1 
ATOM   13517 C  CD  . GLU D  1 378 ? 57.122  142.664 40.088  1.00 98.45  ? 378 GLU D CD  1 
ATOM   13518 O  OE1 . GLU D  1 378 ? 57.164  142.058 38.965  1.00 103.31 ? 378 GLU D OE1 1 
ATOM   13519 O  OE2 . GLU D  1 378 ? 58.093  142.686 40.915  1.00 97.14  ? 378 GLU D OE2 1 
ATOM   13520 N  N   . TYR D  1 379 ? 54.218  139.571 40.740  1.00 49.86  ? 379 TYR D N   1 
ATOM   13521 C  CA  . TYR D  1 379 ? 53.575  138.343 40.266  1.00 41.82  ? 379 TYR D CA  1 
ATOM   13522 C  C   . TYR D  1 379 ? 52.888  137.487 41.316  1.00 37.39  ? 379 TYR D C   1 
ATOM   13523 O  O   . TYR D  1 379 ? 51.940  136.746 41.008  1.00 35.05  ? 379 TYR D O   1 
ATOM   13524 C  CB  . TYR D  1 379 ? 54.556  137.507 39.470  1.00 37.03  ? 379 TYR D CB  1 
ATOM   13525 C  CG  . TYR D  1 379 ? 55.756  137.084 40.240  1.00 29.78  ? 379 TYR D CG  1 
ATOM   13526 C  CD1 . TYR D  1 379 ? 55.699  135.984 41.102  1.00 27.46  ? 379 TYR D CD1 1 
ATOM   13527 C  CD2 . TYR D  1 379 ? 56.969  137.706 40.040  1.00 29.02  ? 379 TYR D CD2 1 
ATOM   13528 C  CE1 . TYR D  1 379 ? 56.844  135.493 41.749  1.00 29.63  ? 379 TYR D CE1 1 
ATOM   13529 C  CE2 . TYR D  1 379 ? 58.137  137.217 40.682  1.00 35.95  ? 379 TYR D CE2 1 
ATOM   13530 C  CZ  . TYR D  1 379 ? 58.070  136.107 41.539  1.00 31.59  ? 379 TYR D CZ  1 
ATOM   13531 O  OH  . TYR D  1 379 ? 59.226  135.627 42.140  1.00 30.93  ? 379 TYR D OH  1 
ATOM   13532 N  N   . SER D  1 380 ? 53.347  137.632 42.548  1.00 30.36  ? 380 SER D N   1 
ATOM   13533 C  CA  . SER D  1 380 ? 52.806  136.874 43.631  1.00 33.77  ? 380 SER D CA  1 
ATOM   13534 C  C   . SER D  1 380 ? 51.525  137.499 44.118  1.00 34.34  ? 380 SER D C   1 
ATOM   13535 O  O   . SER D  1 380 ? 51.523  138.617 44.584  1.00 46.64  ? 380 SER D O   1 
ATOM   13536 C  CB  . SER D  1 380 ? 53.817  136.846 44.738  1.00 34.13  ? 380 SER D CB  1 
ATOM   13537 O  OG  . SER D  1 380 ? 53.295  136.064 45.776  1.00 48.10  ? 380 SER D OG  1 
ATOM   13538 N  N   . ALA D  1 381 ? 50.419  136.805 44.019  1.00 33.69  ? 381 ALA D N   1 
ATOM   13539 C  CA  . ALA D  1 381 ? 49.177  137.385 44.475  1.00 31.00  ? 381 ALA D CA  1 
ATOM   13540 C  C   . ALA D  1 381 ? 48.924  137.170 45.948  1.00 33.74  ? 381 ALA D C   1 
ATOM   13541 O  O   . ALA D  1 381 ? 48.232  137.953 46.564  1.00 43.00  ? 381 ALA D O   1 
ATOM   13542 C  CB  . ALA D  1 381 ? 48.021  136.820 43.696  1.00 29.57  ? 381 ALA D CB  1 
ATOM   13543 N  N   . PHE D  1 382 ? 49.441  136.096 46.518  1.00 33.73  ? 382 PHE D N   1 
ATOM   13544 C  CA  . PHE D  1 382 ? 49.166  135.809 47.918  1.00 32.43  ? 382 PHE D CA  1 
ATOM   13545 C  C   . PHE D  1 382 ? 50.101  134.742 48.385  1.00 32.81  ? 382 PHE D C   1 
ATOM   13546 O  O   . PHE D  1 382 ? 50.272  133.755 47.696  1.00 33.91  ? 382 PHE D O   1 
ATOM   13547 C  CB  . PHE D  1 382 ? 47.755  135.267 48.031  1.00 26.84  ? 382 PHE D CB  1 
ATOM   13548 C  CG  . PHE D  1 382 ? 47.409  134.800 49.389  1.00 40.64  ? 382 PHE D CG  1 
ATOM   13549 C  CD1 . PHE D  1 382 ? 47.978  133.654 49.916  1.00 45.39  ? 382 PHE D CD1 1 
ATOM   13550 C  CD2 . PHE D  1 382 ? 46.502  135.497 50.160  1.00 48.19  ? 382 PHE D CD2 1 
ATOM   13551 C  CE1 . PHE D  1 382 ? 47.644  133.206 51.209  1.00 55.50  ? 382 PHE D CE1 1 
ATOM   13552 C  CE2 . PHE D  1 382 ? 46.159  135.057 51.453  1.00 52.34  ? 382 PHE D CE2 1 
ATOM   13553 C  CZ  . PHE D  1 382 ? 46.728  133.912 51.977  1.00 53.66  ? 382 PHE D CZ  1 
ATOM   13554 N  N   . ARG D  1 383 ? 50.671  134.893 49.566  1.00 31.90  ? 383 ARG D N   1 
ATOM   13555 C  CA  . ARG D  1 383 ? 51.533  133.842 50.048  1.00 31.03  ? 383 ARG D CA  1 
ATOM   13556 C  C   . ARG D  1 383 ? 51.491  133.709 51.520  1.00 34.32  ? 383 ARG D C   1 
ATOM   13557 O  O   . ARG D  1 383 ? 51.383  134.698 52.204  1.00 39.63  ? 383 ARG D O   1 
ATOM   13558 C  CB  . ARG D  1 383 ? 52.976  134.009 49.601  1.00 28.69  ? 383 ARG D CB  1 
ATOM   13559 C  CG  . ARG D  1 383 ? 53.431  135.362 49.229  1.00 22.27  ? 383 ARG D CG  1 
ATOM   13560 C  CD  . ARG D  1 383 ? 54.597  135.725 50.104  1.00 28.09  ? 383 ARG D CD  1 
ATOM   13561 N  NE  . ARG D  1 383 ? 55.806  136.126 49.368  1.00 33.04  ? 383 ARG D NE  1 
ATOM   13562 C  CZ  . ARG D  1 383 ? 56.590  137.154 49.718  1.00 33.67  ? 383 ARG D CZ  1 
ATOM   13563 N  NH1 . ARG D  1 383 ? 56.296  137.927 50.767  1.00 29.67  ? 383 ARG D NH1 1 
ATOM   13564 N  NH2 . ARG D  1 383 ? 57.748  137.324 49.120  1.00 34.81  ? 383 ARG D NH2 1 
ATOM   13565 N  N   . GLU D  1 384 ? 51.519  132.480 52.012  1.00 39.20  ? 384 GLU D N   1 
ATOM   13566 C  CA  . GLU D  1 384 ? 51.528  132.260 53.442  1.00 41.99  ? 384 GLU D CA  1 
ATOM   13567 C  C   . GLU D  1 384 ? 52.212  130.962 53.791  1.00 43.70  ? 384 GLU D C   1 
ATOM   13568 O  O   . GLU D  1 384 ? 52.072  129.961 53.083  1.00 47.90  ? 384 GLU D O   1 
ATOM   13569 C  CB  . GLU D  1 384 ? 50.123  132.260 54.032  1.00 42.13  ? 384 GLU D CB  1 
ATOM   13570 C  CG  . GLU D  1 384 ? 50.173  132.322 55.556  1.00 43.34  ? 384 GLU D CG  1 
ATOM   13571 C  CD  . GLU D  1 384 ? 48.811  132.354 56.199  1.00 46.31  ? 384 GLU D CD  1 
ATOM   13572 O  OE1 . GLU D  1 384 ? 47.916  133.094 55.735  1.00 55.00  ? 384 GLU D OE1 1 
ATOM   13573 O  OE2 . GLU D  1 384 ? 48.641  131.661 57.203  1.00 47.17  ? 384 GLU D OE2 1 
ATOM   13574 N  N   . ALA D  1 385 ? 52.929  131.001 54.907  1.00 41.52  ? 385 ALA D N   1 
ATOM   13575 C  CA  . ALA D  1 385 ? 53.654  129.856 55.411  1.00 39.84  ? 385 ALA D CA  1 
ATOM   13576 C  C   . ALA D  1 385 ? 52.849  129.087 56.466  1.00 39.92  ? 385 ALA D C   1 
ATOM   13577 O  O   . ALA D  1 385 ? 53.109  129.214 57.650  1.00 46.15  ? 385 ALA D O   1 
ATOM   13578 C  CB  . ALA D  1 385 ? 54.993  130.312 55.987  1.00 35.33  ? 385 ALA D CB  1 
ATOM   13579 N  N   . SER D  1 386 ? 51.872  128.296 56.051  1.00 37.11  ? 386 SER D N   1 
ATOM   13580 C  CA  . SER D  1 386 ? 51.093  127.530 57.016  1.00 37.31  ? 386 SER D CA  1 
ATOM   13581 C  C   . SER D  1 386 ? 50.838  126.176 56.428  1.00 39.34  ? 386 SER D C   1 
ATOM   13582 O  O   . SER D  1 386 ? 50.938  126.003 55.221  1.00 39.07  ? 386 SER D O   1 
ATOM   13583 C  CB  . SER D  1 386 ? 49.756  128.190 57.319  1.00 35.46  ? 386 SER D CB  1 
ATOM   13584 O  OG  . SER D  1 386 ? 49.959  129.245 58.229  1.00 35.12  ? 386 SER D OG  1 
ATOM   13585 N  N   . PHE D  1 387 ? 50.509  125.209 57.271  1.00 39.44  ? 387 PHE D N   1 
ATOM   13586 C  CA  . PHE D  1 387 ? 50.248  123.879 56.761  1.00 37.72  ? 387 PHE D CA  1 
ATOM   13587 C  C   . PHE D  1 387 ? 48.810  123.851 56.342  1.00 37.74  ? 387 PHE D C   1 
ATOM   13588 O  O   . PHE D  1 387 ? 48.008  124.596 56.902  1.00 39.79  ? 387 PHE D O   1 
ATOM   13589 C  CB  . PHE D  1 387 ? 50.513  122.819 57.831  1.00 37.92  ? 387 PHE D CB  1 
ATOM   13590 C  CG  . PHE D  1 387 ? 51.989  122.603 58.134  1.00 35.26  ? 387 PHE D CG  1 
ATOM   13591 C  CD1 . PHE D  1 387 ? 52.855  122.121 57.152  1.00 37.13  ? 387 PHE D CD1 1 
ATOM   13592 C  CD2 . PHE D  1 387 ? 52.499  122.843 59.399  1.00 33.35  ? 387 PHE D CD2 1 
ATOM   13593 C  CE1 . PHE D  1 387 ? 54.215  121.873 57.417  1.00 38.94  ? 387 PHE D CE1 1 
ATOM   13594 C  CE2 . PHE D  1 387 ? 53.855  122.598 59.676  1.00 43.03  ? 387 PHE D CE2 1 
ATOM   13595 C  CZ  . PHE D  1 387 ? 54.712  122.108 58.672  1.00 40.62  ? 387 PHE D CZ  1 
ATOM   13596 N  N   . GLY D  1 388 ? 48.499  123.076 55.302  1.00 41.28  ? 388 GLY D N   1 
ATOM   13597 C  CA  . GLY D  1 388 ? 47.126  122.949 54.839  1.00 43.34  ? 388 GLY D CA  1 
ATOM   13598 C  C   . GLY D  1 388 ? 47.051  122.225 53.517  1.00 44.95  ? 388 GLY D C   1 
ATOM   13599 O  O   . GLY D  1 388 ? 48.067  121.762 52.989  1.00 46.01  ? 388 GLY D O   1 
ATOM   13600 N  N   . HIS D  1 389 ? 45.841  122.117 52.981  1.00 44.79  ? 389 HIS D N   1 
ATOM   13601 C  CA  . HIS D  1 389 ? 45.600  121.473 51.685  1.00 40.72  ? 389 HIS D CA  1 
ATOM   13602 C  C   . HIS D  1 389 ? 44.706  122.420 50.870  1.00 40.66  ? 389 HIS D C   1 
ATOM   13603 O  O   . HIS D  1 389 ? 44.276  123.436 51.375  1.00 43.47  ? 389 HIS D O   1 
ATOM   13604 C  CB  . HIS D  1 389 ? 44.845  120.190 51.916  1.00 39.54  ? 389 HIS D CB  1 
ATOM   13605 C  CG  . HIS D  1 389 ? 43.455  120.395 52.428  1.00 36.30  ? 389 HIS D CG  1 
ATOM   13606 N  ND1 . HIS D  1 389 ? 42.348  120.279 51.618  1.00 34.03  ? 389 HIS D ND1 1 
ATOM   13607 C  CD2 . HIS D  1 389 ? 42.985  120.635 53.680  1.00 39.58  ? 389 HIS D CD2 1 
ATOM   13608 C  CE1 . HIS D  1 389 ? 41.253  120.425 52.347  1.00 38.07  ? 389 HIS D CE1 1 
ATOM   13609 N  NE2 . HIS D  1 389 ? 41.610  120.638 53.600  1.00 41.52  ? 389 HIS D NE2 1 
ATOM   13610 N  N   . GLY D  1 390 ? 44.385  122.080 49.634  1.00 41.89  ? 390 GLY D N   1 
ATOM   13611 C  CA  . GLY D  1 390 ? 43.516  122.937 48.831  1.00 36.43  ? 390 GLY D CA  1 
ATOM   13612 C  C   . GLY D  1 390 ? 42.363  122.168 48.185  1.00 33.71  ? 390 GLY D C   1 
ATOM   13613 O  O   . GLY D  1 390 ? 42.276  120.951 48.290  1.00 34.98  ? 390 GLY D O   1 
ATOM   13614 N  N   . MET D  1 391 ? 41.423  122.865 47.581  1.00 30.99  ? 391 MET D N   1 
ATOM   13615 C  CA  . MET D  1 391 ? 40.315  122.197 46.916  1.00 36.26  ? 391 MET D CA  1 
ATOM   13616 C  C   . MET D  1 391 ? 40.084  123.036 45.665  1.00 39.08  ? 391 MET D C   1 
ATOM   13617 O  O   . MET D  1 391 ? 40.207  124.260 45.721  1.00 48.45  ? 391 MET D O   1 
ATOM   13618 C  CB  . MET D  1 391 ? 39.056  122.223 47.764  1.00 39.93  ? 391 MET D CB  1 
ATOM   13619 C  CG  . MET D  1 391 ? 39.180  121.581 49.129  1.00 49.39  ? 391 MET D CG  1 
ATOM   13620 S  SD  . MET D  1 391 ? 39.034  119.835 49.091  1.00 50.68  ? 391 MET D SD  1 
ATOM   13621 C  CE  . MET D  1 391 ? 37.490  119.679 48.208  1.00 42.11  ? 391 MET D CE  1 
ATOM   13622 N  N   . PHE D  1 392 ? 39.797  122.397 44.536  1.00 34.82  ? 392 PHE D N   1 
ATOM   13623 C  CA  . PHE D  1 392 ? 39.568  123.089 43.274  1.00 33.23  ? 392 PHE D CA  1 
ATOM   13624 C  C   . PHE D  1 392 ? 38.251  122.535 42.834  1.00 35.50  ? 392 PHE D C   1 
ATOM   13625 O  O   . PHE D  1 392 ? 38.143  121.376 42.417  1.00 36.72  ? 392 PHE D O   1 
ATOM   13626 C  CB  . PHE D  1 392 ? 40.629  122.729 42.298  1.00 33.50  ? 392 PHE D CB  1 
ATOM   13627 C  CG  . PHE D  1 392 ? 40.547  123.475 41.056  1.00 33.52  ? 392 PHE D CG  1 
ATOM   13628 C  CD1 . PHE D  1 392 ? 41.199  124.687 40.927  1.00 39.21  ? 392 PHE D CD1 1 
ATOM   13629 C  CD2 . PHE D  1 392 ? 39.878  122.942 39.972  1.00 39.95  ? 392 PHE D CD2 1 
ATOM   13630 C  CE1 . PHE D  1 392 ? 41.199  125.388 39.707  1.00 42.88  ? 392 PHE D CE1 1 
ATOM   13631 C  CE2 . PHE D  1 392 ? 39.860  123.613 38.741  1.00 42.76  ? 392 PHE D CE2 1 
ATOM   13632 C  CZ  . PHE D  1 392 ? 40.532  124.855 38.612  1.00 44.59  ? 392 PHE D CZ  1 
ATOM   13633 N  N   . ASP D  1 393 ? 37.239  123.378 42.966  1.00 38.68  ? 393 ASP D N   1 
ATOM   13634 C  CA  . ASP D  1 393 ? 35.867  123.008 42.702  1.00 37.38  ? 393 ASP D CA  1 
ATOM   13635 C  C   . ASP D  1 393 ? 35.318  123.455 41.381  1.00 38.10  ? 393 ASP D C   1 
ATOM   13636 O  O   . ASP D  1 393 ? 34.893  124.601 41.208  1.00 37.08  ? 393 ASP D O   1 
ATOM   13637 C  CB  . ASP D  1 393 ? 35.021  123.594 43.799  1.00 39.51  ? 393 ASP D CB  1 
ATOM   13638 C  CG  . ASP D  1 393 ? 33.697  122.933 43.894  1.00 46.10  ? 393 ASP D CG  1 
ATOM   13639 O  OD1 . ASP D  1 393 ? 33.389  122.053 43.042  1.00 45.04  ? 393 ASP D OD1 1 
ATOM   13640 O  OD2 . ASP D  1 393 ? 32.969  123.308 44.844  1.00 48.40  ? 393 ASP D OD2 1 
ATOM   13641 N  N   . ILE D  1 394 ? 35.250  122.527 40.459  1.00 39.50  ? 394 ILE D N   1 
ATOM   13642 C  CA  . ILE D  1 394 ? 34.765  122.857 39.139  1.00 39.93  ? 394 ILE D CA  1 
ATOM   13643 C  C   . ILE D  1 394 ? 33.267  122.907 39.201  1.00 41.46  ? 394 ILE D C   1 
ATOM   13644 O  O   . ILE D  1 394 ? 32.616  121.958 39.651  1.00 40.45  ? 394 ILE D O   1 
ATOM   13645 C  CB  . ILE D  1 394 ? 35.228  121.833 38.143  1.00 38.85  ? 394 ILE D CB  1 
ATOM   13646 C  CG1 . ILE D  1 394 ? 36.744  121.949 38.006  1.00 40.78  ? 394 ILE D CG1 1 
ATOM   13647 C  CG2 . ILE D  1 394 ? 34.533  122.021 36.835  1.00 39.43  ? 394 ILE D CG2 1 
ATOM   13648 C  CD1 . ILE D  1 394 ? 37.361  120.863 37.184  1.00 43.43  ? 394 ILE D CD1 1 
ATOM   13649 N  N   . LYS D  1 395 ? 32.721  124.028 38.755  1.00 43.76  ? 395 LYS D N   1 
ATOM   13650 C  CA  . LYS D  1 395 ? 31.288  124.243 38.787  1.00 42.15  ? 395 LYS D CA  1 
ATOM   13651 C  C   . LYS D  1 395 ? 30.653  124.210 37.412  1.00 42.97  ? 395 LYS D C   1 
ATOM   13652 O  O   . LYS D  1 395 ? 29.691  123.490 37.162  1.00 42.33  ? 395 LYS D O   1 
ATOM   13653 C  CB  . LYS D  1 395 ? 31.015  125.620 39.408  1.00 40.15  ? 395 LYS D CB  1 
ATOM   13654 C  CG  . LYS D  1 395 ? 31.194  125.719 40.905  1.00 39.77  ? 395 LYS D CG  1 
ATOM   13655 C  CD  . LYS D  1 395 ? 29.976  125.170 41.588  1.00 50.13  ? 395 LYS D CD  1 
ATOM   13656 C  CE  . LYS D  1 395 ? 30.177  124.945 43.089  1.00 56.44  ? 395 LYS D CE  1 
ATOM   13657 N  NZ  . LYS D  1 395 ? 30.551  126.168 43.876  1.00 72.91  ? 395 LYS D NZ  1 
ATOM   13658 N  N   . ASN D  1 396 ? 31.247  124.980 36.514  1.00 44.32  ? 396 ASN D N   1 
ATOM   13659 C  CA  . ASN D  1 396 ? 30.728  125.207 35.187  1.00 43.70  ? 396 ASN D CA  1 
ATOM   13660 C  C   . ASN D  1 396 ? 31.805  124.973 34.188  1.00 44.47  ? 396 ASN D C   1 
ATOM   13661 O  O   . ASN D  1 396 ? 32.899  124.565 34.526  1.00 48.08  ? 396 ASN D O   1 
ATOM   13662 C  CB  . ASN D  1 396 ? 30.424  126.711 35.131  1.00 51.25  ? 396 ASN D CB  1 
ATOM   13663 C  CG  . ASN D  1 396 ? 28.986  127.014 35.411  1.00 62.23  ? 396 ASN D CG  1 
ATOM   13664 O  OD1 . ASN D  1 396 ? 28.177  126.674 34.571  1.00 76.35  ? 396 ASN D OD1 1 
ATOM   13665 N  ND2 . ASN D  1 396 ? 28.614  127.487 36.611  1.00 70.02  ? 396 ASN D ND2 1 
ATOM   13666 N  N   . ARG D  1 397 ? 31.523  125.320 32.944  1.00 43.02  ? 397 ARG D N   1 
ATOM   13667 C  CA  . ARG D  1 397 ? 32.548  125.251 31.911  1.00 41.87  ? 397 ARG D CA  1 
ATOM   13668 C  C   . ARG D  1 397 ? 33.284  126.603 32.008  1.00 43.17  ? 397 ARG D C   1 
ATOM   13669 O  O   . ARG D  1 397 ? 34.299  126.819 31.344  1.00 45.27  ? 397 ARG D O   1 
ATOM   13670 C  CB  . ARG D  1 397 ? 31.930  125.118 30.514  1.00 40.58  ? 397 ARG D CB  1 
ATOM   13671 C  CG  . ARG D  1 397 ? 31.556  126.435 29.890  1.00 42.13  ? 397 ARG D CG  1 
ATOM   13672 C  CD  . ARG D  1 397 ? 30.950  126.241 28.541  1.00 40.44  ? 397 ARG D CD  1 
ATOM   13673 N  NE  . ARG D  1 397 ? 29.659  125.577 28.653  1.00 42.98  ? 397 ARG D NE  1 
ATOM   13674 C  CZ  . ARG D  1 397 ? 28.889  125.288 27.614  1.00 44.69  ? 397 ARG D CZ  1 
ATOM   13675 N  NH1 . ARG D  1 397 ? 29.288  125.601 26.399  1.00 47.17  ? 397 ARG D NH1 1 
ATOM   13676 N  NH2 . ARG D  1 397 ? 27.714  124.712 27.782  1.00 42.34  ? 397 ARG D NH2 1 
ATOM   13677 N  N   . THR D  1 398 ? 32.713  127.540 32.780  1.00 47.00  ? 398 THR D N   1 
ATOM   13678 C  CA  . THR D  1 398 ? 33.283  128.893 32.975  1.00 44.30  ? 398 THR D CA  1 
ATOM   13679 C  C   . THR D  1 398 ? 33.804  129.141 34.394  1.00 43.13  ? 398 THR D C   1 
ATOM   13680 O  O   . THR D  1 398 ? 34.758  129.913 34.589  1.00 37.38  ? 398 THR D O   1 
ATOM   13681 C  CB  . THR D  1 398 ? 32.233  130.025 32.661  1.00 43.52  ? 398 THR D CB  1 
ATOM   13682 O  OG1 . THR D  1 398 ? 30.941  129.672 33.204  1.00 44.92  ? 398 THR D OG1 1 
ATOM   13683 C  CG2 . THR D  1 398 ? 32.120  130.290 31.153  1.00 41.58  ? 398 THR D CG2 1 
ATOM   13684 N  N   . HIS D  1 399 ? 33.209  128.453 35.367  1.00 41.86  ? 399 HIS D N   1 
ATOM   13685 C  CA  . HIS D  1 399 ? 33.576  128.664 36.756  1.00 42.68  ? 399 HIS D CA  1 
ATOM   13686 C  C   . HIS D  1 399 ? 34.118  127.492 37.516  1.00 41.97  ? 399 HIS D C   1 
ATOM   13687 O  O   . HIS D  1 399 ? 33.581  126.384 37.451  1.00 43.10  ? 399 HIS D O   1 
ATOM   13688 C  CB  . HIS D  1 399 ? 32.373  129.209 37.534  1.00 43.56  ? 399 HIS D CB  1 
ATOM   13689 C  CG  . HIS D  1 399 ? 31.937  130.557 37.078  1.00 47.08  ? 399 HIS D CG  1 
ATOM   13690 N  ND1 . HIS D  1 399 ? 32.201  131.704 37.790  1.00 51.85  ? 399 HIS D ND1 1 
ATOM   13691 C  CD2 . HIS D  1 399 ? 31.340  130.956 35.933  1.00 45.55  ? 399 HIS D CD2 1 
ATOM   13692 C  CE1 . HIS D  1 399 ? 31.795  132.753 37.099  1.00 48.40  ? 399 HIS D CE1 1 
ATOM   13693 N  NE2 . HIS D  1 399 ? 31.267  132.324 35.969  1.00 48.00  ? 399 HIS D NE2 1 
ATOM   13694 N  N   . ALA D  1 400 ? 35.129  127.785 38.314  1.00 39.48  ? 400 ALA D N   1 
ATOM   13695 C  CA  . ALA D  1 400 ? 35.751  126.805 39.174  1.00 35.69  ? 400 ALA D CA  1 
ATOM   13696 C  C   . ALA D  1 400 ? 36.188  127.629 40.353  1.00 35.78  ? 400 ALA D C   1 
ATOM   13697 O  O   . ALA D  1 400 ? 36.640  128.757 40.187  1.00 35.30  ? 400 ALA D O   1 
ATOM   13698 C  CB  . ALA D  1 400 ? 36.922  126.206 38.497  1.00 35.55  ? 400 ALA D CB  1 
ATOM   13699 N  N   . HIS D  1 401 ? 36.079  127.074 41.540  1.00 35.28  ? 401 HIS D N   1 
ATOM   13700 C  CA  . HIS D  1 401 ? 36.447  127.818 42.707  1.00 38.06  ? 401 HIS D CA  1 
ATOM   13701 C  C   . HIS D  1 401 ? 37.522  127.122 43.539  1.00 41.03  ? 401 HIS D C   1 
ATOM   13702 O  O   . HIS D  1 401 ? 37.313  126.004 44.015  1.00 47.93  ? 401 HIS D O   1 
ATOM   13703 C  CB  . HIS D  1 401 ? 35.179  128.026 43.508  1.00 41.78  ? 401 HIS D CB  1 
ATOM   13704 C  CG  . HIS D  1 401 ? 35.404  128.634 44.842  1.00 44.56  ? 401 HIS D CG  1 
ATOM   13705 N  ND1 . HIS D  1 401 ? 34.840  128.121 45.986  1.00 52.04  ? 401 HIS D ND1 1 
ATOM   13706 C  CD2 . HIS D  1 401 ? 36.147  129.700 45.219  1.00 43.73  ? 401 HIS D CD2 1 
ATOM   13707 C  CE1 . HIS D  1 401 ? 35.228  128.852 47.018  1.00 53.65  ? 401 HIS D CE1 1 
ATOM   13708 N  NE2 . HIS D  1 401 ? 36.022  129.812 46.578  1.00 48.04  ? 401 HIS D NE2 1 
ATOM   13709 N  N   . PHE D  1 402 ? 38.665  127.789 43.705  1.00 37.87  ? 402 PHE D N   1 
ATOM   13710 C  CA  . PHE D  1 402 ? 39.780  127.265 44.486  1.00 34.39  ? 402 PHE D CA  1 
ATOM   13711 C  C   . PHE D  1 402 ? 39.726  127.756 45.939  1.00 37.80  ? 402 PHE D C   1 
ATOM   13712 O  O   . PHE D  1 402 ? 39.392  128.900 46.197  1.00 42.84  ? 402 PHE D O   1 
ATOM   13713 C  CB  . PHE D  1 402 ? 41.083  127.707 43.849  1.00 28.94  ? 402 PHE D CB  1 
ATOM   13714 C  CG  . PHE D  1 402 ? 42.280  127.208 44.556  1.00 29.43  ? 402 PHE D CG  1 
ATOM   13715 C  CD1 . PHE D  1 402 ? 42.670  125.885 44.451  1.00 29.07  ? 402 PHE D CD1 1 
ATOM   13716 C  CD2 . PHE D  1 402 ? 42.981  128.040 45.383  1.00 28.64  ? 402 PHE D CD2 1 
ATOM   13717 C  CE1 . PHE D  1 402 ? 43.735  125.405 45.175  1.00 30.38  ? 402 PHE D CE1 1 
ATOM   13718 C  CE2 . PHE D  1 402 ? 44.059  127.556 46.115  1.00 34.38  ? 402 PHE D CE2 1 
ATOM   13719 C  CZ  . PHE D  1 402 ? 44.428  126.238 46.009  1.00 28.05  ? 402 PHE D CZ  1 
ATOM   13720 N  N   . SER D  1 403 ? 40.096  126.918 46.889  1.00 38.41  ? 403 SER D N   1 
ATOM   13721 C  CA  . SER D  1 403 ? 40.071  127.309 48.297  1.00 38.68  ? 403 SER D CA  1 
ATOM   13722 C  C   . SER D  1 403 ? 41.354  126.786 48.923  1.00 41.52  ? 403 SER D C   1 
ATOM   13723 O  O   . SER D  1 403 ? 41.960  125.865 48.374  1.00 46.21  ? 403 SER D O   1 
ATOM   13724 C  CB  . SER D  1 403 ? 38.890  126.653 48.983  1.00 34.07  ? 403 SER D CB  1 
ATOM   13725 O  OG  . SER D  1 403 ? 37.936  126.238 48.003  1.00 43.83  ? 403 SER D OG  1 
ATOM   13726 N  N   . TRP D  1 404 ? 41.819  127.423 49.997  1.00 41.43  ? 404 TRP D N   1 
ATOM   13727 C  CA  . TRP D  1 404 ? 43.004  126.986 50.728  1.00 40.12  ? 404 TRP D CA  1 
ATOM   13728 C  C   . TRP D  1 404 ? 42.613  126.975 52.188  1.00 44.26  ? 404 TRP D C   1 
ATOM   13729 O  O   . TRP D  1 404 ? 42.372  128.035 52.746  1.00 45.70  ? 404 TRP D O   1 
ATOM   13730 C  CB  . TRP D  1 404 ? 44.161  127.958 50.595  1.00 31.75  ? 404 TRP D CB  1 
ATOM   13731 C  CG  . TRP D  1 404 ? 45.347  127.512 51.432  1.00 35.41  ? 404 TRP D CG  1 
ATOM   13732 C  CD1 . TRP D  1 404 ? 45.963  126.291 51.387  1.00 37.47  ? 404 TRP D CD1 1 
ATOM   13733 C  CD2 . TRP D  1 404 ? 46.103  128.290 52.361  1.00 37.58  ? 404 TRP D CD2 1 
ATOM   13734 N  NE1 . TRP D  1 404 ? 47.062  126.270 52.213  1.00 34.89  ? 404 TRP D NE1 1 
ATOM   13735 C  CE2 . TRP D  1 404 ? 47.177  127.481 52.822  1.00 34.36  ? 404 TRP D CE2 1 
ATOM   13736 C  CE3 . TRP D  1 404 ? 45.992  129.594 52.840  1.00 43.85  ? 404 TRP D CE3 1 
ATOM   13737 C  CZ2 . TRP D  1 404 ? 48.130  127.927 53.728  1.00 35.85  ? 404 TRP D CZ2 1 
ATOM   13738 C  CZ3 . TRP D  1 404 ? 46.950  130.050 53.753  1.00 50.16  ? 404 TRP D CZ3 1 
ATOM   13739 C  CH2 . TRP D  1 404 ? 48.010  129.207 54.187  1.00 47.09  ? 404 TRP D CH2 1 
ATOM   13740 N  N   . ASN D  1 405 ? 42.524  125.795 52.793  1.00 48.88  ? 405 ASN D N   1 
ATOM   13741 C  CA  . ASN D  1 405 ? 42.170  125.646 54.207  1.00 52.84  ? 405 ASN D CA  1 
ATOM   13742 C  C   . ASN D  1 405 ? 43.393  125.439 55.121  1.00 53.71  ? 405 ASN D C   1 
ATOM   13743 O  O   . ASN D  1 405 ? 44.056  124.396 55.066  1.00 56.19  ? 405 ASN D O   1 
ATOM   13744 C  CB  . ASN D  1 405 ? 41.192  124.484 54.377  1.00 59.41  ? 405 ASN D CB  1 
ATOM   13745 C  CG  . ASN D  1 405 ? 41.021  124.079 55.819  1.00 65.56  ? 405 ASN D CG  1 
ATOM   13746 O  OD1 . ASN D  1 405 ? 41.685  123.154 56.302  1.00 70.17  ? 405 ASN D OD1 1 
ATOM   13747 N  ND2 . ASN D  1 405 ? 40.152  124.786 56.526  1.00 73.86  ? 405 ASN D ND2 1 
ATOM   13748 N  N   . ARG D  1 406 ? 43.660  126.395 56.003  1.00 54.54  ? 406 ARG D N   1 
ATOM   13749 C  CA  . ARG D  1 406 ? 44.808  126.241 56.870  1.00 49.88  ? 406 ARG D CA  1 
ATOM   13750 C  C   . ARG D  1 406 ? 44.533  125.216 57.925  1.00 48.74  ? 406 ARG D C   1 
ATOM   13751 O  O   . ARG D  1 406 ? 43.391  124.975 58.315  1.00 49.74  ? 406 ARG D O   1 
ATOM   13752 C  CB  . ARG D  1 406 ? 45.171  127.552 57.508  1.00 53.02  ? 406 ARG D CB  1 
ATOM   13753 C  CG  . ARG D  1 406 ? 45.553  128.562 56.505  1.00 57.60  ? 406 ARG D CG  1 
ATOM   13754 C  CD  . ARG D  1 406 ? 46.099  129.765 57.172  1.00 60.93  ? 406 ARG D CD  1 
ATOM   13755 N  NE  . ARG D  1 406 ? 45.197  130.228 58.218  1.00 66.60  ? 406 ARG D NE  1 
ATOM   13756 C  CZ  . ARG D  1 406 ? 45.529  131.105 59.166  1.00 71.24  ? 406 ARG D CZ  1 
ATOM   13757 N  NH1 . ARG D  1 406 ? 46.749  131.640 59.211  1.00 73.46  ? 406 ARG D NH1 1 
ATOM   13758 N  NH2 . ARG D  1 406 ? 44.649  131.425 60.103  1.00 74.76  ? 406 ARG D NH2 1 
ATOM   13759 N  N   . ASN D  1 407 ? 45.588  124.596 58.398  1.00 48.10  ? 407 ASN D N   1 
ATOM   13760 C  CA  . ASN D  1 407 ? 45.418  123.590 59.415  1.00 49.58  ? 407 ASN D CA  1 
ATOM   13761 C  C   . ASN D  1 407 ? 44.932  124.213 60.715  1.00 51.14  ? 407 ASN D C   1 
ATOM   13762 O  O   . ASN D  1 407 ? 44.157  123.588 61.440  1.00 48.62  ? 407 ASN D O   1 
ATOM   13763 C  CB  . ASN D  1 407 ? 46.729  122.820 59.626  1.00 53.05  ? 407 ASN D CB  1 
ATOM   13764 C  CG  . ASN D  1 407 ? 46.849  121.609 58.723  1.00 50.62  ? 407 ASN D CG  1 
ATOM   13765 O  OD1 . ASN D  1 407 ? 46.048  121.426 57.791  1.00 50.35  ? 407 ASN D OD1 1 
ATOM   13766 N  ND2 . ASN D  1 407 ? 47.822  120.759 59.012  1.00 47.30  ? 407 ASN D ND2 1 
ATOM   13767 N  N   . GLN D  1 408 ? 45.377  125.447 60.988  1.00 54.01  ? 408 GLN D N   1 
ATOM   13768 C  CA  . GLN D  1 408 ? 45.003  126.178 62.207  1.00 55.41  ? 408 GLN D CA  1 
ATOM   13769 C  C   . GLN D  1 408 ? 43.535  126.571 62.244  1.00 53.40  ? 408 GLN D C   1 
ATOM   13770 O  O   . GLN D  1 408 ? 42.970  126.799 63.323  1.00 60.27  ? 408 GLN D O   1 
ATOM   13771 C  CB  . GLN D  1 408 ? 45.792  127.466 62.367  1.00 54.23  ? 408 GLN D CB  1 
ATOM   13772 C  CG  . GLN D  1 408 ? 47.218  127.368 62.079  1.00 62.58  ? 408 GLN D CG  1 
ATOM   13773 C  CD  . GLN D  1 408 ? 47.508  127.782 60.687  1.00 65.98  ? 408 GLN D CD  1 
ATOM   13774 O  OE1 . GLN D  1 408 ? 47.491  126.961 59.762  1.00 72.35  ? 408 GLN D OE1 1 
ATOM   13775 N  NE2 . GLN D  1 408 ? 47.779  129.066 60.508  1.00 66.71  ? 408 GLN D NE2 1 
ATOM   13776 N  N   . ASP D  1 409 ? 42.957  126.778 61.074  1.00 45.50  ? 409 ASP D N   1 
ATOM   13777 C  CA  . ASP D  1 409 ? 41.569  127.146 61.006  1.00 45.27  ? 409 ASP D CA  1 
ATOM   13778 C  C   . ASP D  1 409 ? 40.751  125.896 61.211  1.00 45.33  ? 409 ASP D C   1 
ATOM   13779 O  O   . ASP D  1 409 ? 41.269  124.799 61.278  1.00 45.08  ? 409 ASP D O   1 
ATOM   13780 C  CB  . ASP D  1 409 ? 41.229  127.749 59.653  1.00 49.49  ? 409 ASP D CB  1 
ATOM   13781 C  CG  . ASP D  1 409 ? 42.179  128.854 59.252  1.00 54.57  ? 409 ASP D CG  1 
ATOM   13782 O  OD1 . ASP D  1 409 ? 42.737  129.499 60.174  1.00 50.58  ? 409 ASP D OD1 1 
ATOM   13783 O  OD2 . ASP D  1 409 ? 42.372  129.045 58.012  1.00 58.91  ? 409 ASP D OD2 1 
ATOM   13784 N  N   . GLY D  1 410 ? 39.453  126.072 61.346  1.00 48.45  ? 410 GLY D N   1 
ATOM   13785 C  CA  . GLY D  1 410 ? 38.598  124.934 61.548  1.00 44.97  ? 410 GLY D CA  1 
ATOM   13786 C  C   . GLY D  1 410 ? 38.412  124.426 60.167  1.00 44.32  ? 410 GLY D C   1 
ATOM   13787 O  O   . GLY D  1 410 ? 38.671  125.098 59.197  1.00 41.33  ? 410 GLY D O   1 
ATOM   13788 N  N   . VAL D  1 411 ? 37.894  123.231 60.102  1.00 49.49  ? 411 VAL D N   1 
ATOM   13789 C  CA  . VAL D  1 411 ? 37.665  122.538 58.861  1.00 50.50  ? 411 VAL D CA  1 
ATOM   13790 C  C   . VAL D  1 411 ? 36.998  123.297 57.726  1.00 53.32  ? 411 VAL D C   1 
ATOM   13791 O  O   . VAL D  1 411 ? 37.307  123.045 56.554  1.00 57.13  ? 411 VAL D O   1 
ATOM   13792 C  CB  . VAL D  1 411 ? 36.876  121.285 59.181  1.00 49.26  ? 411 VAL D CB  1 
ATOM   13793 C  CG1 . VAL D  1 411 ? 36.134  120.754 57.962  1.00 52.06  ? 411 VAL D CG1 1 
ATOM   13794 C  CG2 . VAL D  1 411 ? 37.820  120.264 59.759  1.00 52.90  ? 411 VAL D CG2 1 
ATOM   13795 N  N   . ALA D  1 412 ? 36.117  124.236 58.065  1.00 56.90  ? 412 ALA D N   1 
ATOM   13796 C  CA  . ALA D  1 412 ? 35.371  124.978 57.055  1.00 58.14  ? 412 ALA D CA  1 
ATOM   13797 C  C   . ALA D  1 412 ? 35.865  126.375 56.718  1.00 58.45  ? 412 ALA D C   1 
ATOM   13798 O  O   . ALA D  1 412 ? 35.295  127.063 55.878  1.00 62.76  ? 412 ALA D O   1 
ATOM   13799 C  CB  . ALA D  1 412 ? 33.910  125.022 57.446  1.00 60.26  ? 412 ALA D CB  1 
ATOM   13800 N  N   . VAL D  1 413 ? 36.959  126.773 57.332  1.00 59.37  ? 413 VAL D N   1 
ATOM   13801 C  CA  . VAL D  1 413 ? 37.518  128.094 57.109  1.00 58.66  ? 413 VAL D CA  1 
ATOM   13802 C  C   . VAL D  1 413 ? 38.510  128.218 55.955  1.00 56.14  ? 413 VAL D C   1 
ATOM   13803 O  O   . VAL D  1 413 ? 39.710  127.877 56.078  1.00 53.20  ? 413 VAL D O   1 
ATOM   13804 C  CB  . VAL D  1 413 ? 38.198  128.594 58.376  1.00 60.35  ? 413 VAL D CB  1 
ATOM   13805 C  CG1 . VAL D  1 413 ? 38.798  129.978 58.131  1.00 56.13  ? 413 VAL D CG1 1 
ATOM   13806 C  CG2 . VAL D  1 413 ? 37.203  128.550 59.548  1.00 62.13  ? 413 VAL D CG2 1 
ATOM   13807 N  N   . GLU D  1 414 ? 38.021  128.799 54.871  1.00 51.11  ? 414 GLU D N   1 
ATOM   13808 C  CA  . GLU D  1 414 ? 38.845  128.998 53.705  1.00 50.27  ? 414 GLU D CA  1 
ATOM   13809 C  C   . GLU D  1 414 ? 39.748  130.217 53.905  1.00 49.03  ? 414 GLU D C   1 
ATOM   13810 O  O   . GLU D  1 414 ? 39.314  131.335 53.659  1.00 52.95  ? 414 GLU D O   1 
ATOM   13811 C  CB  . GLU D  1 414 ? 37.964  129.242 52.494  1.00 51.88  ? 414 GLU D CB  1 
ATOM   13812 C  CG  . GLU D  1 414 ? 36.945  128.171 52.209  1.00 57.46  ? 414 GLU D CG  1 
ATOM   13813 C  CD  . GLU D  1 414 ? 36.094  128.500 50.989  1.00 65.45  ? 414 GLU D CD  1 
ATOM   13814 O  OE1 . GLU D  1 414 ? 36.420  129.496 50.274  1.00 71.89  ? 414 GLU D OE1 1 
ATOM   13815 O  OE2 . GLU D  1 414 ? 35.094  127.769 50.755  1.00 67.68  ? 414 GLU D OE2 1 
ATOM   13816 N  N   . ALA D  1 415 ? 41.002  130.017 54.307  1.00 46.64  ? 415 ALA D N   1 
ATOM   13817 C  CA  . ALA D  1 415 ? 41.930  131.136 54.526  1.00 41.86  ? 415 ALA D CA  1 
ATOM   13818 C  C   . ALA D  1 415 ? 42.299  131.866 53.240  1.00 38.65  ? 415 ALA D C   1 
ATOM   13819 O  O   . ALA D  1 415 ? 43.052  132.844 53.260  1.00 43.73  ? 415 ALA D O   1 
ATOM   13820 C  CB  . ALA D  1 415 ? 43.189  130.646 55.243  1.00 36.25  ? 415 ALA D CB  1 
ATOM   13821 N  N   . ASP D  1 416 ? 41.841  131.339 52.116  1.00 35.12  ? 416 ASP D N   1 
ATOM   13822 C  CA  . ASP D  1 416 ? 42.081  131.941 50.812  1.00 35.19  ? 416 ASP D CA  1 
ATOM   13823 C  C   . ASP D  1 416 ? 41.027  131.359 49.905  1.00 34.87  ? 416 ASP D C   1 
ATOM   13824 O  O   . ASP D  1 416 ? 40.676  130.210 50.018  1.00 39.27  ? 416 ASP D O   1 
ATOM   13825 C  CB  . ASP D  1 416 ? 43.451  131.602 50.263  1.00 37.12  ? 416 ASP D CB  1 
ATOM   13826 C  CG  . ASP D  1 416 ? 43.839  132.469 49.083  1.00 41.34  ? 416 ASP D CG  1 
ATOM   13827 O  OD1 . ASP D  1 416 ? 42.979  132.828 48.250  1.00 39.36  ? 416 ASP D OD1 1 
ATOM   13828 O  OD2 . ASP D  1 416 ? 45.026  132.811 48.998  1.00 44.10  ? 416 ASP D OD2 1 
ATOM   13829 N  N   . SER D  1 417 ? 40.526  132.144 48.986  1.00 34.97  ? 417 SER D N   1 
ATOM   13830 C  CA  . SER D  1 417 ? 39.492  131.669 48.128  1.00 38.06  ? 417 SER D CA  1 
ATOM   13831 C  C   . SER D  1 417 ? 39.570  132.542 46.872  1.00 41.61  ? 417 SER D C   1 
ATOM   13832 O  O   . SER D  1 417 ? 39.911  133.721 46.945  1.00 43.83  ? 417 SER D O   1 
ATOM   13833 C  CB  . SER D  1 417 ? 38.179  131.799 48.871  1.00 41.29  ? 417 SER D CB  1 
ATOM   13834 O  OG  . SER D  1 417 ? 37.119  132.040 47.978  1.00 55.24  ? 417 SER D OG  1 
ATOM   13835 N  N   . VAL D  1 418 ? 39.315  131.945 45.710  1.00 42.32  ? 418 VAL D N   1 
ATOM   13836 C  CA  . VAL D  1 418 ? 39.418  132.635 44.429  1.00 39.39  ? 418 VAL D CA  1 
ATOM   13837 C  C   . VAL D  1 418 ? 38.526  131.968 43.384  1.00 42.05  ? 418 VAL D C   1 
ATOM   13838 O  O   . VAL D  1 418 ? 38.358  130.749 43.411  1.00 49.02  ? 418 VAL D O   1 
ATOM   13839 C  CB  . VAL D  1 418 ? 40.854  132.519 43.921  1.00 36.64  ? 418 VAL D CB  1 
ATOM   13840 C  CG1 . VAL D  1 418 ? 40.991  133.146 42.578  1.00 40.51  ? 418 VAL D CG1 1 
ATOM   13841 C  CG2 . VAL D  1 418 ? 41.818  133.147 44.890  1.00 41.37  ? 418 VAL D CG2 1 
ATOM   13842 N  N   . TRP D  1 419 ? 37.928  132.741 42.483  1.00 39.23  ? 419 TRP D N   1 
ATOM   13843 C  CA  . TRP D  1 419 ? 37.127  132.120 41.449  1.00 39.18  ? 419 TRP D CA  1 
ATOM   13844 C  C   . TRP D  1 419 ? 37.979  132.113 40.212  1.00 41.57  ? 419 TRP D C   1 
ATOM   13845 O  O   . TRP D  1 419 ? 38.706  133.079 39.960  1.00 41.33  ? 419 TRP D O   1 
ATOM   13846 C  CB  . TRP D  1 419 ? 35.865  132.884 41.183  1.00 40.89  ? 419 TRP D CB  1 
ATOM   13847 C  CG  . TRP D  1 419 ? 34.795  132.508 42.104  1.00 42.66  ? 419 TRP D CG  1 
ATOM   13848 C  CD1 . TRP D  1 419 ? 34.510  133.093 43.291  1.00 40.67  ? 419 TRP D CD1 1 
ATOM   13849 C  CD2 . TRP D  1 419 ? 33.874  131.417 41.954  1.00 42.87  ? 419 TRP D CD2 1 
ATOM   13850 N  NE1 . TRP D  1 419 ? 33.468  132.434 43.899  1.00 42.32  ? 419 TRP D NE1 1 
ATOM   13851 C  CE2 . TRP D  1 419 ? 33.060  131.397 43.103  1.00 41.67  ? 419 TRP D CE2 1 
ATOM   13852 C  CE3 . TRP D  1 419 ? 33.669  130.453 40.969  1.00 44.32  ? 419 TRP D CE3 1 
ATOM   13853 C  CZ2 . TRP D  1 419 ? 32.048  130.439 43.302  1.00 41.57  ? 419 TRP D CZ2 1 
ATOM   13854 C  CZ3 . TRP D  1 419 ? 32.661  129.498 41.168  1.00 44.09  ? 419 TRP D CZ3 1 
ATOM   13855 C  CH2 . TRP D  1 419 ? 31.868  129.500 42.325  1.00 37.19  ? 419 TRP D CH2 1 
ATOM   13856 N  N   . PHE D  1 420 ? 37.934  131.011 39.467  1.00 40.58  ? 420 PHE D N   1 
ATOM   13857 C  CA  . PHE D  1 420 ? 38.742  130.878 38.277  1.00 38.30  ? 420 PHE D CA  1 
ATOM   13858 C  C   . PHE D  1 420 ? 37.788  131.021 37.139  1.00 39.33  ? 420 PHE D C   1 
ATOM   13859 O  O   . PHE D  1 420 ? 36.718  130.422 37.157  1.00 40.12  ? 420 PHE D O   1 
ATOM   13860 C  CB  . PHE D  1 420 ? 39.417  129.501 38.196  1.00 38.83  ? 420 PHE D CB  1 
ATOM   13861 C  CG  . PHE D  1 420 ? 40.741  129.405 38.920  1.00 31.54  ? 420 PHE D CG  1 
ATOM   13862 C  CD1 . PHE D  1 420 ? 40.797  129.303 40.298  1.00 35.08  ? 420 PHE D CD1 1 
ATOM   13863 C  CD2 . PHE D  1 420 ? 41.920  129.465 38.228  1.00 27.40  ? 420 PHE D CD2 1 
ATOM   13864 C  CE1 . PHE D  1 420 ? 42.023  129.278 40.981  1.00 35.52  ? 420 PHE D CE1 1 
ATOM   13865 C  CE2 . PHE D  1 420 ? 43.148  129.441 38.902  1.00 28.36  ? 420 PHE D CE2 1 
ATOM   13866 C  CZ  . PHE D  1 420 ? 43.194  129.353 40.281  1.00 32.08  ? 420 PHE D CZ  1 
ATOM   13867 N  N   . PHE D  1 421 ? 38.145  131.891 36.207  1.00 38.42  ? 421 PHE D N   1 
ATOM   13868 C  CA  . PHE D  1 421 ? 37.353  132.119 35.025  1.00 42.57  ? 421 PHE D CA  1 
ATOM   13869 C  C   . PHE D  1 421 ? 38.106  131.395 33.946  1.00 44.99  ? 421 PHE D C   1 
ATOM   13870 O  O   . PHE D  1 421 ? 39.304  131.656 33.691  1.00 44.96  ? 421 PHE D O   1 
ATOM   13871 C  CB  . PHE D  1 421 ? 37.248  133.605 34.710  1.00 43.32  ? 421 PHE D CB  1 
ATOM   13872 C  CG  . PHE D  1 421 ? 36.447  134.343 35.701  1.00 41.70  ? 421 PHE D CG  1 
ATOM   13873 C  CD1 . PHE D  1 421 ? 35.355  133.728 36.310  1.00 44.00  ? 421 PHE D CD1 1 
ATOM   13874 C  CD2 . PHE D  1 421 ? 36.813  135.604 36.110  1.00 42.56  ? 421 PHE D CD2 1 
ATOM   13875 C  CE1 . PHE D  1 421 ? 34.653  134.359 37.320  1.00 39.17  ? 421 PHE D CE1 1 
ATOM   13876 C  CE2 . PHE D  1 421 ? 36.121  136.235 37.113  1.00 44.23  ? 421 PHE D CE2 1 
ATOM   13877 C  CZ  . PHE D  1 421 ? 35.037  135.602 37.722  1.00 38.59  ? 421 PHE D CZ  1 
ATOM   13878 N  N   . ASN D  1 422 ? 37.390  130.485 33.303  1.00 41.26  ? 422 ASN D N   1 
ATOM   13879 C  CA  . ASN D  1 422 ? 37.992  129.640 32.288  1.00 40.70  ? 422 ASN D CA  1 
ATOM   13880 C  C   . ASN D  1 422 ? 38.732  130.355 31.192  1.00 37.07  ? 422 ASN D C   1 
ATOM   13881 O  O   . ASN D  1 422 ? 38.103  131.050 30.417  1.00 42.91  ? 422 ASN D O   1 
ATOM   13882 C  CB  . ASN D  1 422 ? 36.940  128.707 31.680  1.00 38.56  ? 422 ASN D CB  1 
ATOM   13883 C  CG  . ASN D  1 422 ? 37.556  127.678 30.749  1.00 39.59  ? 422 ASN D CG  1 
ATOM   13884 O  OD1 . ASN D  1 422 ? 37.826  127.976 29.584  1.00 34.80  ? 422 ASN D OD1 1 
ATOM   13885 N  ND2 . ASN D  1 422 ? 37.834  126.478 31.268  1.00 40.85  ? 422 ASN D ND2 1 
ATOM   13886 N  N   . ARG D  1 423 ? 40.040  130.119 31.071  1.00 35.29  ? 423 ARG D N   1 
ATOM   13887 C  CA  . ARG D  1 423 ? 40.850  130.748 30.010  1.00 37.49  ? 423 ARG D CA  1 
ATOM   13888 C  C   . ARG D  1 423 ? 40.351  130.550 28.564  1.00 41.54  ? 423 ARG D C   1 
ATOM   13889 O  O   . ARG D  1 423 ? 40.833  131.219 27.647  1.00 46.02  ? 423 ARG D O   1 
ATOM   13890 C  CB  . ARG D  1 423 ? 42.316  130.305 30.043  1.00 30.91  ? 423 ARG D CB  1 
ATOM   13891 C  CG  . ARG D  1 423 ? 43.119  130.827 31.180  1.00 40.50  ? 423 ARG D CG  1 
ATOM   13892 C  CD  . ARG D  1 423 ? 43.026  132.337 31.315  1.00 40.85  ? 423 ARG D CD  1 
ATOM   13893 N  NE  . ARG D  1 423 ? 41.829  132.719 32.055  1.00 43.54  ? 423 ARG D NE  1 
ATOM   13894 C  CZ  . ARG D  1 423 ? 41.543  133.963 32.402  1.00 42.79  ? 423 ARG D CZ  1 
ATOM   13895 N  NH1 . ARG D  1 423 ? 42.383  134.936 32.066  1.00 43.92  ? 423 ARG D NH1 1 
ATOM   13896 N  NH2 . ARG D  1 423 ? 40.425  134.225 33.085  1.00 40.90  ? 423 ARG D NH2 1 
ATOM   13897 N  N   . HIS D  1 424 ? 39.382  129.672 28.340  1.00 41.12  ? 424 HIS D N   1 
ATOM   13898 C  CA  . HIS D  1 424 ? 38.895  129.432 26.987  1.00 39.23  ? 424 HIS D CA  1 
ATOM   13899 C  C   . HIS D  1 424 ? 37.447  129.854 26.702  1.00 37.83  ? 424 HIS D C   1 
ATOM   13900 O  O   . HIS D  1 424 ? 37.116  130.293 25.606  1.00 40.57  ? 424 HIS D O   1 
ATOM   13901 C  CB  . HIS D  1 424 ? 39.054  127.954 26.670  1.00 38.49  ? 424 HIS D CB  1 
ATOM   13902 C  CG  . HIS D  1 424 ? 38.395  127.543 25.399  1.00 42.19  ? 424 HIS D CG  1 
ATOM   13903 N  ND1 . HIS D  1 424 ? 39.104  127.337 24.232  1.00 42.56  ? 424 HIS D ND1 1 
ATOM   13904 C  CD2 . HIS D  1 424 ? 37.088  127.333 25.097  1.00 43.64  ? 424 HIS D CD2 1 
ATOM   13905 C  CE1 . HIS D  1 424 ? 38.254  127.027 23.264  1.00 45.37  ? 424 HIS D CE1 1 
ATOM   13906 N  NE2 . HIS D  1 424 ? 37.025  127.017 23.762  1.00 44.99  ? 424 HIS D NE2 1 
ATOM   13907 N  N   . TRP D  1 425 ? 36.580  129.626 27.663  1.00 35.45  ? 425 TRP D N   1 
ATOM   13908 C  CA  . TRP D  1 425 ? 35.184  129.922 27.534  1.00 33.33  ? 425 TRP D CA  1 
ATOM   13909 C  C   . TRP D  1 425 ? 34.766  131.195 28.190  1.00 35.33  ? 425 TRP D C   1 
ATOM   13910 O  O   . TRP D  1 425 ? 33.612  131.620 28.021  1.00 38.51  ? 425 TRP D O   1 
ATOM   13911 C  CB  . TRP D  1 425 ? 34.437  128.819 28.227  1.00 36.39  ? 425 TRP D CB  1 
ATOM   13912 C  CG  . TRP D  1 425 ? 34.408  127.618 27.432  1.00 41.17  ? 425 TRP D CG  1 
ATOM   13913 C  CD1 . TRP D  1 425 ? 35.203  126.502 27.541  1.00 39.76  ? 425 TRP D CD1 1 
ATOM   13914 C  CD2 . TRP D  1 425 ? 33.488  127.357 26.410  1.00 42.10  ? 425 TRP D CD2 1 
ATOM   13915 N  NE1 . TRP D  1 425 ? 34.803  125.546 26.643  1.00 38.01  ? 425 TRP D NE1 1 
ATOM   13916 C  CE2 . TRP D  1 425 ? 33.746  126.055 25.933  1.00 42.71  ? 425 TRP D CE2 1 
ATOM   13917 C  CE3 . TRP D  1 425 ? 32.454  128.103 25.842  1.00 38.33  ? 425 TRP D CE3 1 
ATOM   13918 C  CZ2 . TRP D  1 425 ? 33.005  125.493 24.917  1.00 42.92  ? 425 TRP D CZ2 1 
ATOM   13919 C  CZ3 . TRP D  1 425 ? 31.731  127.551 24.847  1.00 36.01  ? 425 TRP D CZ3 1 
ATOM   13920 C  CH2 . TRP D  1 425 ? 31.999  126.255 24.387  1.00 39.96  ? 425 TRP D CH2 1 
ATOM   13921 N  N   . TYR D  1 426 ? 35.678  131.783 28.956  1.00 30.09  ? 426 TYR D N   1 
ATOM   13922 C  CA  . TYR D  1 426 ? 35.346  132.970 29.700  1.00 33.82  ? 426 TYR D CA  1 
ATOM   13923 C  C   . TYR D  1 426 ? 36.536  133.725 30.270  1.00 36.74  ? 426 TYR D C   1 
ATOM   13924 O  O   . TYR D  1 426 ? 36.652  133.918 31.496  1.00 34.62  ? 426 TYR D O   1 
ATOM   13925 C  CB  . TYR D  1 426 ? 34.469  132.559 30.850  1.00 39.21  ? 426 TYR D CB  1 
ATOM   13926 C  CG  . TYR D  1 426 ? 33.705  133.685 31.438  1.00 46.40  ? 426 TYR D CG  1 
ATOM   13927 C  CD1 . TYR D  1 426 ? 32.883  134.474 30.642  1.00 49.54  ? 426 TYR D CD1 1 
ATOM   13928 C  CD2 . TYR D  1 426 ? 33.730  133.907 32.790  1.00 48.91  ? 426 TYR D CD2 1 
ATOM   13929 C  CE1 . TYR D  1 426 ? 32.088  135.448 31.190  1.00 56.42  ? 426 TYR D CE1 1 
ATOM   13930 C  CE2 . TYR D  1 426 ? 32.941  134.877 33.361  1.00 57.94  ? 426 TYR D CE2 1 
ATOM   13931 C  CZ  . TYR D  1 426 ? 32.109  135.642 32.564  1.00 60.53  ? 426 TYR D CZ  1 
ATOM   13932 O  OH  . TYR D  1 426 ? 31.244  136.540 33.167  1.00 65.32  ? 426 TYR D OH  1 
ATOM   13933 N  N   . PRO D  1 427 ? 37.325  134.318 29.380  1.00 36.70  ? 427 PRO D N   1 
ATOM   13934 C  CA  . PRO D  1 427 ? 38.527  135.084 29.656  1.00 40.94  ? 427 PRO D CA  1 
ATOM   13935 C  C   . PRO D  1 427 ? 38.315  136.443 30.247  1.00 48.13  ? 427 PRO D C   1 
ATOM   13936 O  O   . PRO D  1 427 ? 38.771  137.453 29.701  1.00 53.47  ? 427 PRO D O   1 
ATOM   13937 C  CB  . PRO D  1 427 ? 39.199  135.187 28.286  1.00 41.87  ? 427 PRO D CB  1 
ATOM   13938 C  CG  . PRO D  1 427 ? 38.396  134.290 27.386  1.00 38.35  ? 427 PRO D CG  1 
ATOM   13939 C  CD  . PRO D  1 427 ? 37.029  134.337 27.949  1.00 33.79  ? 427 PRO D CD  1 
ATOM   13940 N  N   . VAL D  1 428 ? 37.642  136.471 31.377  1.00 54.00  ? 428 VAL D N   1 
ATOM   13941 C  CA  . VAL D  1 428 ? 37.427  137.719 32.053  1.00 62.35  ? 428 VAL D CA  1 
ATOM   13942 C  C   . VAL D  1 428 ? 38.436  137.721 33.197  1.00 68.02  ? 428 VAL D C   1 
ATOM   13943 O  O   . VAL D  1 428 ? 38.620  136.690 33.830  1.00 68.79  ? 428 VAL D O   1 
ATOM   13944 C  CB  . VAL D  1 428 ? 35.984  137.817 32.545  1.00 60.42  ? 428 VAL D CB  1 
ATOM   13945 C  CG1 . VAL D  1 428 ? 35.043  137.680 31.368  1.00 59.17  ? 428 VAL D CG1 1 
ATOM   13946 C  CG2 . VAL D  1 428 ? 35.698  136.750 33.543  1.00 60.22  ? 428 VAL D CG2 1 
ATOM   13947 N  N   . ASP D  1 429 ? 39.126  138.850 33.408  1.00 77.33  ? 429 ASP D N   1 
ATOM   13948 C  CA  . ASP D  1 429 ? 40.131  139.005 34.485  1.00 85.96  ? 429 ASP D CA  1 
ATOM   13949 C  C   . ASP D  1 429 ? 39.639  138.509 35.851  1.00 90.44  ? 429 ASP D C   1 
ATOM   13950 O  O   . ASP D  1 429 ? 38.714  139.071 36.442  1.00 93.01  ? 429 ASP D O   1 
ATOM   13951 C  CB  . ASP D  1 429 ? 40.575  140.483 34.627  1.00 90.22  ? 429 ASP D CB  1 
ATOM   13952 C  CG  . ASP D  1 429 ? 41.765  140.682 35.608  1.00 94.41  ? 429 ASP D CG  1 
ATOM   13953 O  OD1 . ASP D  1 429 ? 41.604  140.462 36.840  1.00 97.42  ? 429 ASP D OD1 1 
ATOM   13954 O  OD2 . ASP D  1 429 ? 42.855  141.119 35.146  1.00 98.08  ? 429 ASP D OD2 1 
ATOM   13955 N  N   . ASP D  1 430 ? 40.228  137.430 36.339  1.00 93.46  ? 430 ASP D N   1 
ATOM   13956 C  CA  . ASP D  1 430 ? 39.871  136.931 37.651  1.00 96.61  ? 430 ASP D CA  1 
ATOM   13957 C  C   . ASP D  1 430 ? 40.959  137.436 38.599  1.00 103.03 ? 430 ASP D C   1 
ATOM   13958 O  O   . ASP D  1 430 ? 40.773  137.461 39.817  1.00 104.09 ? 430 ASP D O   1 
ATOM   13959 C  CB  . ASP D  1 430 ? 39.772  135.391 37.656  1.00 93.73  ? 430 ASP D CB  1 
ATOM   13960 C  CG  . ASP D  1 430 ? 40.821  134.704 36.765  1.00 91.16  ? 430 ASP D CG  1 
ATOM   13961 O  OD1 . ASP D  1 430 ? 41.914  135.281 36.538  1.00 91.02  ? 430 ASP D OD1 1 
ATOM   13962 O  OD2 . ASP D  1 430 ? 40.549  133.567 36.303  1.00 86.25  ? 430 ASP D OD2 1 
ATOM   13963 N  N   . SER D  1 431 ? 42.053  137.927 37.997  1.00 108.79 ? 431 SER D N   1 
ATOM   13964 C  CA  . SER D  1 431 ? 43.245  138.425 38.696  1.00 112.97 ? 431 SER D CA  1 
ATOM   13965 C  C   . SER D  1 431 ? 43.055  139.537 39.735  1.00 114.42 ? 431 SER D C   1 
ATOM   13966 O  O   . SER D  1 431 ? 42.672  140.669 39.408  1.00 109.53 ? 431 SER D O   1 
ATOM   13967 C  CB  . SER D  1 431 ? 44.362  138.792 37.686  1.00 114.69 ? 431 SER D CB  1 
ATOM   13968 O  OG  . SER D  1 431 ? 44.855  137.648 36.983  1.00 110.74 ? 431 SER D OG  1 
ATOM   13969 N  N   . THR D  1 432 ? 43.375  139.156 40.979  1.00 120.73 ? 432 THR D N   1 
ATOM   13970 C  CA  . THR D  1 432 ? 43.315  139.969 42.206  1.00 125.38 ? 432 THR D CA  1 
ATOM   13971 C  C   . THR D  1 432 ? 44.098  139.267 43.351  1.00 124.32 ? 432 THR D C   1 
ATOM   13972 O  O   . THR D  1 432 ? 43.603  138.252 43.902  1.00 121.51 ? 432 THR D O   1 
ATOM   13973 C  CB  . THR D  1 432 ? 41.848  140.173 42.703  1.00 129.57 ? 432 THR D CB  1 
ATOM   13974 O  OG1 . THR D  1 432 ? 41.173  138.904 42.754  1.00 130.52 ? 432 THR D OG1 1 
ATOM   13975 C  CG2 . THR D  1 432 ? 41.076  141.184 41.810  1.00 133.39 ? 432 THR D CG2 1 
ATOM   13976 O  OXT . THR D  1 432 ? 45.199  139.745 43.701  1.00 124.53 ? 432 THR D OXT 1 
HETATM 13977 C  C1  . NAG E  2 .   A 55.147  81.644  55.547  1.00 53.42  ? 433 NAG A C1  1 
HETATM 13978 C  C2  . NAG E  2 .   A 55.478  82.302  56.911  1.00 58.42  ? 433 NAG A C2  1 
HETATM 13979 C  C3  . NAG E  2 .   A 55.117  81.407  58.137  1.00 61.70  ? 433 NAG A C3  1 
HETATM 13980 C  C4  . NAG E  2 .   A 53.610  81.103  58.029  1.00 60.65  ? 433 NAG A C4  1 
HETATM 13981 C  C5  . NAG E  2 .   A 53.398  80.367  56.666  1.00 56.25  ? 433 NAG A C5  1 
HETATM 13982 C  C6  . NAG E  2 .   A 51.964  79.940  56.395  1.00 60.02  ? 433 NAG A C6  1 
HETATM 13983 C  C7  . NAG E  2 .   A 57.222  83.901  56.568  1.00 58.08  ? 433 NAG A C7  1 
HETATM 13984 C  C8  . NAG E  2 .   A 58.701  84.153  56.618  1.00 66.39  ? 433 NAG A C8  1 
HETATM 13985 N  N2  . NAG E  2 .   A 56.870  82.670  56.924  1.00 58.15  ? 433 NAG A N2  1 
HETATM 13986 O  O3  . NAG E  2 .   A 55.437  82.046  59.392  1.00 57.40  ? 433 NAG A O3  1 
HETATM 13987 O  O4  . NAG E  2 .   A 53.143  80.348  59.168  1.00 56.70  ? 433 NAG A O4  1 
HETATM 13988 O  O5  . NAG E  2 .   A 53.759  81.232  55.559  1.00 56.55  ? 433 NAG A O5  1 
HETATM 13989 O  O6  . NAG E  2 .   A 51.689  79.861  54.996  1.00 54.62  ? 433 NAG A O6  1 
HETATM 13990 O  O7  . NAG E  2 .   A 56.428  84.788  56.227  1.00 56.53  ? 433 NAG A O7  1 
HETATM 13991 C  C1  . NAG F  2 .   A 80.330  98.460  59.536  1.00 63.66  ? 434 NAG A C1  1 
HETATM 13992 C  C2  . NAG F  2 .   A 80.165  99.410  60.731  1.00 68.90  ? 434 NAG A C2  1 
HETATM 13993 C  C3  . NAG F  2 .   A 79.876  100.852 60.203  1.00 68.63  ? 434 NAG A C3  1 
HETATM 13994 C  C4  . NAG F  2 .   A 81.192  101.249 59.522  1.00 66.20  ? 434 NAG A C4  1 
HETATM 13995 C  C5  . NAG F  2 .   A 81.412  100.265 58.327  1.00 65.93  ? 434 NAG A C5  1 
HETATM 13996 C  C6  . NAG F  2 .   A 82.677  100.505 57.514  1.00 68.52  ? 434 NAG A C6  1 
HETATM 13997 C  C7  . NAG F  2 .   A 77.938  98.745  61.295  1.00 78.20  ? 434 NAG A C7  1 
HETATM 13998 C  C8  . NAG F  2 .   A 77.024  98.221  62.396  1.00 76.79  ? 434 NAG A C8  1 
HETATM 13999 N  N2  . NAG F  2 .   A 79.187  98.919  61.673  1.00 72.72  ? 434 NAG A N2  1 
HETATM 14000 O  O3  . NAG F  2 .   A 79.483  101.795 61.230  1.00 66.24  ? 434 NAG A O3  1 
HETATM 14001 O  O4  . NAG F  2 .   A 81.183  102.624 59.121  1.00 64.49  ? 434 NAG A O4  1 
HETATM 14002 O  O5  . NAG F  2 .   A 81.488  98.884  58.794  1.00 63.48  ? 434 NAG A O5  1 
HETATM 14003 O  O6  . NAG F  2 .   A 83.743  99.677  57.966  1.00 75.00  ? 434 NAG A O6  1 
HETATM 14004 O  O7  . NAG F  2 .   A 77.534  99.007  60.145  1.00 84.83  ? 434 NAG A O7  1 
HETATM 14005 C  C1  . NAG G  2 .   A 76.834  67.901  68.289  1.00 27.56  ? 435 NAG A C1  1 
HETATM 14006 C  C2  . NAG G  2 .   A 76.248  68.273  69.637  1.00 30.87  ? 435 NAG A C2  1 
HETATM 14007 C  C3  . NAG G  2 .   A 77.206  69.227  70.336  1.00 36.92  ? 435 NAG A C3  1 
HETATM 14008 C  C4  . NAG G  2 .   A 78.598  68.608  70.501  1.00 39.60  ? 435 NAG A C4  1 
HETATM 14009 C  C5  . NAG G  2 .   A 79.110  68.141  69.107  1.00 33.69  ? 435 NAG A C5  1 
HETATM 14010 C  C6  . NAG G  2 .   A 80.380  67.317  69.257  1.00 39.11  ? 435 NAG A C6  1 
HETATM 14011 C  C7  . NAG G  2 .   A 73.844  68.239  69.330  1.00 37.02  ? 435 NAG A C7  1 
HETATM 14012 C  C8  . NAG G  2 .   A 72.561  69.059  69.262  1.00 41.97  ? 435 NAG A C8  1 
HETATM 14013 N  N2  . NAG G  2 .   A 74.961  68.934  69.516  1.00 31.22  ? 435 NAG A N2  1 
HETATM 14014 O  O3  . NAG G  2 .   A 76.677  69.610  71.599  1.00 47.19  ? 435 NAG A O3  1 
HETATM 14015 O  O4  . NAG G  2 .   A 79.500  69.565  71.120  1.00 39.36  ? 435 NAG A O4  1 
HETATM 14016 O  O5  . NAG G  2 .   A 78.130  67.281  68.462  1.00 34.60  ? 435 NAG A O5  1 
HETATM 14017 O  O6  . NAG G  2 .   A 80.770  66.698  68.043  1.00 49.03  ? 435 NAG A O6  1 
HETATM 14018 O  O7  . NAG G  2 .   A 73.833  67.017  69.170  1.00 42.95  ? 435 NAG A O7  1 
HETATM 14019 C  C1  . NAG H  2 .   A 50.316  79.753  42.481  1.00 94.42  ? 436 NAG A C1  1 
HETATM 14020 C  C2  . NAG H  2 .   A 49.935  79.734  40.976  1.00 103.07 ? 436 NAG A C2  1 
HETATM 14021 C  C3  . NAG H  2 .   A 48.387  79.745  40.891  1.00 110.01 ? 436 NAG A C3  1 
HETATM 14022 C  C4  . NAG H  2 .   A 47.939  78.322  41.294  1.00 112.09 ? 436 NAG A C4  1 
HETATM 14023 C  C5  . NAG H  2 .   A 48.771  77.791  42.520  1.00 109.09 ? 436 NAG A C5  1 
HETATM 14024 C  C6  . NAG H  2 .   A 49.778  76.637  42.291  1.00 107.74 ? 436 NAG A C6  1 
HETATM 14025 C  C7  . NAG H  2 .   A 50.369  82.092  40.408  1.00 98.84  ? 436 NAG A C7  1 
HETATM 14026 C  C8  . NAG H  2 .   A 51.142  82.974  39.443  1.00 97.07  ? 436 NAG A C8  1 
HETATM 14027 N  N2  . NAG H  2 .   A 50.560  80.795  40.186  1.00 102.38 ? 436 NAG A N2  1 
HETATM 14028 O  O3  . NAG H  2 .   A 47.899  80.099  39.582  1.00 112.85 ? 436 NAG A O3  1 
HETATM 14029 O  O4  . NAG H  2 .   A 46.529  78.291  41.575  1.00 117.25 ? 436 NAG A O4  1 
HETATM 14030 O  O5  . NAG H  2 .   A 49.458  78.873  43.260  1.00 102.08 ? 436 NAG A O5  1 
HETATM 14031 O  O6  . NAG H  2 .   A 50.148  76.465  40.921  1.00 109.64 ? 436 NAG A O6  1 
HETATM 14032 O  O7  . NAG H  2 .   A 49.651  82.559  41.310  1.00 99.02  ? 436 NAG A O7  1 
HETATM 14033 C  C1  . NAG I  2 .   A 100.750 49.894  48.423  1.00 68.24  ? 437 NAG A C1  1 
HETATM 14034 C  C2  . NAG I  2 .   A 102.142 49.182  48.349  1.00 70.79  ? 437 NAG A C2  1 
HETATM 14035 C  C3  . NAG I  2 .   A 102.096 47.771  48.979  1.00 68.48  ? 437 NAG A C3  1 
HETATM 14036 C  C4  . NAG I  2 .   A 101.612 47.929  50.435  1.00 66.48  ? 437 NAG A C4  1 
HETATM 14037 C  C5  . NAG I  2 .   A 100.195 48.566  50.375  1.00 66.54  ? 437 NAG A C5  1 
HETATM 14038 C  C6  . NAG I  2 .   A 99.566  48.806  51.743  1.00 71.33  ? 437 NAG A C6  1 
HETATM 14039 C  C7  . NAG I  2 .   A 103.668 49.696  46.539  1.00 84.26  ? 437 NAG A C7  1 
HETATM 14040 C  C8  . NAG I  2 .   A 103.960 49.553  45.046  1.00 85.45  ? 437 NAG A C8  1 
HETATM 14041 N  N2  . NAG I  2 .   A 102.561 49.083  46.962  1.00 78.08  ? 437 NAG A N2  1 
HETATM 14042 O  O3  . NAG I  2 .   A 103.372 47.108  48.894  1.00 66.95  ? 437 NAG A O3  1 
HETATM 14043 O  O4  . NAG I  2 .   A 101.603 46.672  51.138  1.00 65.39  ? 437 NAG A O4  1 
HETATM 14044 O  O5  . NAG I  2 .   A 100.242 49.866  49.758  1.00 63.38  ? 437 NAG A O5  1 
HETATM 14045 O  O6  . NAG I  2 .   A 99.881  50.116  52.233  1.00 71.39  ? 437 NAG A O6  1 
HETATM 14046 O  O7  . NAG I  2 .   A 104.446 50.308  47.297  1.00 88.04  ? 437 NAG A O7  1 
HETATM 14047 FE FE  . FE  J  3 .   ? 67.867  60.642  51.410  1.00 29.09  ? 438 FE  A FE  1 
HETATM 14048 ZN ZN  . ZN  K  4 .   ? 67.438  60.614  48.109  1.00 25.39  ? 439 ZN  A ZN  1 
HETATM 14049 P  P   . PO4 L  5 .   ? 65.492  59.834  50.352  1.00 28.85  ? 440 PO4 A P   1 
HETATM 14050 O  O1  . PO4 L  5 .   ? 65.877  58.421  50.551  1.00 34.45  ? 440 PO4 A O1  1 
HETATM 14051 O  O2  . PO4 L  5 .   ? 66.148  60.707  51.232  1.00 22.26  ? 440 PO4 A O2  1 
HETATM 14052 O  O3  . PO4 L  5 .   ? 65.715  60.239  48.977  1.00 20.63  ? 440 PO4 A O3  1 
HETATM 14053 O  O4  . PO4 L  5 .   ? 63.887  59.926  50.754  1.00 36.43  ? 440 PO4 A O4  1 
HETATM 14054 C  C1  . NAG M  2 .   A 13.319  9.024   70.472  1.00 63.18  ? 433 NAG B C1  1 
HETATM 14055 C  C2  . NAG M  2 .   A 12.020  8.272   70.067  1.00 68.40  ? 433 NAG B C2  1 
HETATM 14056 C  C3  . NAG M  2 .   A 10.755  9.196   70.074  1.00 69.46  ? 433 NAG B C3  1 
HETATM 14057 C  C4  . NAG M  2 .   A 10.642  9.776   71.488  1.00 69.63  ? 433 NAG B C4  1 
HETATM 14058 C  C5  . NAG M  2 .   A 11.939  10.573  71.754  1.00 66.96  ? 433 NAG B C5  1 
HETATM 14059 C  C6  . NAG M  2 .   A 11.953  11.248  73.110  1.00 69.46  ? 433 NAG B C6  1 
HETATM 14060 C  C7  . NAG M  2 .   A 12.668  6.421   68.666  1.00 80.67  ? 433 NAG B C7  1 
HETATM 14061 C  C8  . NAG M  2 .   A 12.854  5.924   67.242  1.00 82.22  ? 433 NAG B C8  1 
HETATM 14062 N  N2  . NAG M  2 .   A 12.223  7.674   68.766  1.00 76.36  ? 433 NAG B N2  1 
HETATM 14063 O  O3  . NAG M  2 .   A 9.548   8.493   69.707  1.00 68.42  ? 433 NAG B O3  1 
HETATM 14064 O  O4  . NAG M  2 .   A 9.469   10.596  71.637  1.00 71.58  ? 433 NAG B O4  1 
HETATM 14065 O  O5  . NAG M  2 .   A 13.099  9.698   71.726  1.00 65.95  ? 433 NAG B O5  1 
HETATM 14066 O  O6  . NAG M  2 .   A 13.283  11.397  73.603  1.00 73.51  ? 433 NAG B O6  1 
HETATM 14067 O  O7  . NAG M  2 .   A 12.874  5.682   69.648  1.00 83.55  ? 433 NAG B O7  1 
HETATM 14068 C  C1  . NAG N  2 .   A 13.203  -11.977 48.251  1.00 89.13  ? 434 NAG B C1  1 
HETATM 14069 C  C2  . NAG N  2 .   A 11.986  -12.913 48.421  1.00 93.83  ? 434 NAG B C2  1 
HETATM 14070 C  C3  . NAG N  2 .   A 12.460  -14.274 49.014  1.00 95.32  ? 434 NAG B C3  1 
HETATM 14071 C  C4  . NAG N  2 .   A 13.327  -14.875 47.900  1.00 91.74  ? 434 NAG B C4  1 
HETATM 14072 C  C5  . NAG N  2 .   A 14.527  -13.920 47.674  1.00 88.69  ? 434 NAG B C5  1 
HETATM 14073 C  C6  . NAG N  2 .   A 15.464  -14.390 46.582  1.00 87.82  ? 434 NAG B C6  1 
HETATM 14074 C  C7  . NAG N  2 .   A 11.117  -11.875 50.415  1.00 100.68 ? 434 NAG B C7  1 
HETATM 14075 C  C8  . NAG N  2 .   A 9.890   -11.250 51.057  1.00 98.00  ? 434 NAG B C8  1 
HETATM 14076 N  N2  . NAG N  2 .   A 10.915  -12.297 49.177  1.00 97.04  ? 434 NAG B N2  1 
HETATM 14077 O  O3  . NAG N  2 .   A 11.373  -15.155 49.387  1.00 95.07  ? 434 NAG B O3  1 
HETATM 14078 O  O4  . NAG N  2 .   A 13.751  -16.196 48.239  1.00 93.64  ? 434 NAG B O4  1 
HETATM 14079 O  O5  . NAG N  2 .   A 14.082  -12.582 47.294  1.00 84.41  ? 434 NAG B O5  1 
HETATM 14080 O  O6  . NAG N  2 .   A 15.107  -13.826 45.328  1.00 90.01  ? 434 NAG B O6  1 
HETATM 14081 O  O7  . NAG N  2 .   A 12.198  -12.009 51.020  1.00 105.64 ? 434 NAG B O7  1 
HETATM 14082 C  C1  . NAG O  2 .   A 3.915   18.513  45.026  1.00 71.47  ? 435 NAG B C1  1 
HETATM 14083 C  C2  . NAG O  2 .   A 2.481   18.188  45.490  1.00 75.54  ? 435 NAG B C2  1 
HETATM 14084 C  C3  . NAG O  2 .   A 1.939   17.057  44.606  1.00 80.54  ? 435 NAG B C3  1 
HETATM 14085 C  C4  . NAG O  2 .   A 1.993   17.430  43.128  1.00 80.24  ? 435 NAG B C4  1 
HETATM 14086 C  C5  . NAG O  2 .   A 3.433   17.851  42.757  1.00 77.47  ? 435 NAG B C5  1 
HETATM 14087 C  C6  . NAG O  2 .   A 3.509   18.408  41.340  1.00 80.95  ? 435 NAG B C6  1 
HETATM 14088 C  C7  . NAG O  2 .   A 2.450   18.628  47.895  1.00 66.80  ? 435 NAG B C7  1 
HETATM 14089 C  C8  . NAG O  2 .   A 2.362   18.027  49.286  1.00 69.17  ? 435 NAG B C8  1 
HETATM 14090 N  N2  . NAG O  2 .   A 2.423   17.758  46.887  1.00 71.55  ? 435 NAG B N2  1 
HETATM 14091 O  O3  . NAG O  2 .   A 0.602   16.722  44.973  1.00 88.31  ? 435 NAG B O3  1 
HETATM 14092 O  O4  . NAG O  2 .   A 1.563   16.304  42.348  1.00 81.89  ? 435 NAG B O4  1 
HETATM 14093 O  O5  . NAG O  2 .   A 3.902   18.896  43.645  1.00 71.93  ? 435 NAG B O5  1 
HETATM 14094 O  O6  . NAG O  2 .   A 4.788   18.958  41.037  1.00 87.58  ? 435 NAG B O6  1 
HETATM 14095 O  O7  . NAG O  2 .   A 2.602   19.838  47.736  1.00 67.70  ? 435 NAG B O7  1 
HETATM 14096 C  C1  . NAG P  2 .   A 25.489  12.098  76.744  1.00 116.88 ? 436 NAG B C1  1 
HETATM 14097 C  C2  . NAG P  2 .   A 26.935  12.217  77.342  1.00 126.10 ? 436 NAG B C2  1 
HETATM 14098 C  C3  . NAG P  2 .   A 26.791  12.494  78.868  1.00 128.81 ? 436 NAG B C3  1 
HETATM 14099 C  C4  . NAG P  2 .   A 26.302  13.948  79.002  1.00 127.81 ? 436 NAG B C4  1 
HETATM 14100 C  C5  . NAG P  2 .   A 25.210  14.285  77.918  1.00 127.03 ? 436 NAG B C5  1 
HETATM 14101 C  C6  . NAG P  2 .   A 25.601  15.240  76.772  1.00 129.76 ? 436 NAG B C6  1 
HETATM 14102 C  C7  . NAG P  2 .   A 27.597  9.809   77.425  1.00 134.14 ? 436 NAG B C7  1 
HETATM 14103 C  C8  . NAG P  2 .   A 28.657  8.806   76.983  1.00 131.89 ? 436 NAG B C8  1 
HETATM 14104 N  N2  . NAG P  2 .   A 27.819  11.077  77.039  1.00 132.79 ? 436 NAG B N2  1 
HETATM 14105 O  O3  . NAG P  2 .   A 28.018  12.291  79.591  1.00 128.40 ? 436 NAG B O3  1 
HETATM 14106 O  O4  . NAG P  2 .   A 25.811  14.203  80.326  1.00 126.78 ? 436 NAG B O4  1 
HETATM 14107 O  O5  . NAG P  2 .   A 24.581  13.088  77.319  1.00 121.21 ? 436 NAG B O5  1 
HETATM 14108 O  O6  . NAG P  2 .   A 27.012  15.388  76.609  1.00 130.72 ? 436 NAG B O6  1 
HETATM 14109 O  O7  . NAG P  2 .   A 26.613  9.440   78.081  1.00 139.33 ? 436 NAG B O7  1 
HETATM 14110 C  C1  . NAG Q  2 .   A 27.151  32.649  21.551  1.00 86.19  ? 437 NAG B C1  1 
HETATM 14111 C  C2  . NAG Q  2 .   A 27.419  33.112  20.096  1.00 90.69  ? 437 NAG B C2  1 
HETATM 14112 C  C3  . NAG Q  2 .   A 26.782  34.503  19.812  1.00 93.51  ? 437 NAG B C3  1 
HETATM 14113 C  C4  . NAG Q  2 .   A 25.276  34.397  20.104  1.00 93.62  ? 437 NAG B C4  1 
HETATM 14114 C  C5  . NAG Q  2 .   A 25.139  34.021  21.598  1.00 92.46  ? 437 NAG B C5  1 
HETATM 14115 C  C6  . NAG Q  2 .   A 23.696  33.882  22.071  1.00 98.25  ? 437 NAG B C6  1 
HETATM 14116 C  C7  . NAG Q  2 .   A 29.439  32.388  18.977  1.00 95.12  ? 437 NAG B C7  1 
HETATM 14117 C  C8  . NAG Q  2 .   A 30.953  32.525  18.891  1.00 94.45  ? 437 NAG B C8  1 
HETATM 14118 N  N2  . NAG Q  2 .   A 28.854  33.166  19.882  1.00 91.98  ? 437 NAG B N2  1 
HETATM 14119 O  O3  . NAG Q  2 .   A 27.027  34.940  18.464  1.00 98.09  ? 437 NAG B O3  1 
HETATM 14120 O  O4  . NAG Q  2 .   A 24.585  35.620  19.797  1.00 88.02  ? 437 NAG B O4  1 
HETATM 14121 O  O5  . NAG Q  2 .   A 25.752  32.739  21.855  1.00 87.45  ? 437 NAG B O5  1 
HETATM 14122 O  O6  . NAG Q  2 .   A 23.228  32.541  21.903  1.00 103.48 ? 437 NAG B O6  1 
HETATM 14123 O  O7  . NAG Q  2 .   A 28.810  31.628  18.228  1.00 97.86  ? 437 NAG B O7  1 
HETATM 14124 FE FE  . FE  R  3 .   ? 19.287  27.589  55.029  1.00 50.04  ? 438 FE  B FE  1 
HETATM 14125 ZN ZN  . ZN  S  4 .   ? 22.521  27.832  55.871  1.00 43.93  ? 439 ZN  B ZN  1 
HETATM 14126 P  P   . PO4 T  5 .   ? 19.939  28.867  57.388  1.00 34.01  ? 440 PO4 B P   1 
HETATM 14127 O  O1  . PO4 T  5 .   ? 19.746  30.189  56.744  1.00 44.77  ? 440 PO4 B O1  1 
HETATM 14128 O  O2  . PO4 T  5 .   ? 19.170  27.826  56.776  1.00 36.37  ? 440 PO4 B O2  1 
HETATM 14129 O  O3  . PO4 T  5 .   ? 21.394  28.519  57.416  1.00 38.76  ? 440 PO4 B O3  1 
HETATM 14130 O  O4  . PO4 T  5 .   ? 19.432  28.967  58.895  1.00 47.97  ? 440 PO4 B O4  1 
HETATM 14131 C  C1  . NAG U  2 .   A 62.877  6.373   55.445  1.00 50.46  ? 433 NAG C C1  1 
HETATM 14132 C  C2  . NAG U  2 .   A 64.170  5.817   56.091  1.00 55.39  ? 433 NAG C C2  1 
HETATM 14133 C  C3  . NAG U  2 .   A 65.443  6.670   55.745  1.00 58.56  ? 433 NAG C C3  1 
HETATM 14134 C  C4  . NAG U  2 .   A 65.560  6.716   54.198  1.00 57.92  ? 433 NAG C C4  1 
HETATM 14135 C  C5  . NAG U  2 .   A 64.264  7.373   53.680  1.00 51.31  ? 433 NAG C C5  1 
HETATM 14136 C  C6  . NAG U  2 .   A 64.246  7.544   52.186  1.00 52.41  ? 433 NAG C C6  1 
HETATM 14137 C  C7  . NAG U  2 .   A 63.549  4.548   58.060  1.00 65.16  ? 433 NAG C C7  1 
HETATM 14138 C  C8  . NAG U  2 .   A 63.396  4.550   59.565  1.00 68.95  ? 433 NAG C C8  1 
HETATM 14139 N  N2  . NAG U  2 .   A 63.983  5.697   57.524  1.00 59.89  ? 433 NAG C N2  1 
HETATM 14140 O  O3  . NAG U  2 .   A 66.655  6.145   56.354  1.00 56.82  ? 433 NAG C O3  1 
HETATM 14141 O  O4  . NAG U  2 .   A 66.758  7.398   53.748  1.00 60.25  ? 433 NAG C O4  1 
HETATM 14142 O  O5  . NAG U  2 .   A 63.107  6.555   54.017  1.00 53.29  ? 433 NAG C O5  1 
HETATM 14143 O  O6  . NAG U  2 .   A 62.917  7.500   51.701  1.00 66.49  ? 433 NAG C O6  1 
HETATM 14144 O  O7  . NAG U  2 .   A 63.288  3.531   57.405  1.00 64.60  ? 433 NAG C O7  1 
HETATM 14145 C  C1  . NAG V  2 .   A 63.125  -5.618  83.537  1.00 59.47  ? 434 NAG C C1  1 
HETATM 14146 C  C2  . NAG V  2 .   A 64.318  -6.553  83.700  1.00 65.81  ? 434 NAG C C2  1 
HETATM 14147 C  C3  . NAG V  2 .   A 63.834  -8.039  83.586  1.00 71.11  ? 434 NAG C C3  1 
HETATM 14148 C  C4  . NAG V  2 .   A 62.971  -8.230  84.852  1.00 74.12  ? 434 NAG C C4  1 
HETATM 14149 C  C5  . NAG V  2 .   A 61.785  -7.231  84.743  1.00 71.45  ? 434 NAG C C5  1 
HETATM 14150 C  C6  . NAG V  2 .   A 60.835  -7.285  85.935  1.00 68.78  ? 434 NAG C C6  1 
HETATM 14151 C  C7  . NAG V  2 .   A 65.167  -6.304  81.490  1.00 59.45  ? 434 NAG C C7  1 
HETATM 14152 C  C8  . NAG V  2 .   A 66.366  -5.906  80.646  1.00 57.86  ? 434 NAG C C8  1 
HETATM 14153 N  N2  . NAG V  2 .   A 65.375  -6.210  82.785  1.00 64.06  ? 434 NAG C N2  1 
HETATM 14154 O  O3  . NAG V  2 .   A 64.913  -9.006  83.509  1.00 71.28  ? 434 NAG C O3  1 
HETATM 14155 O  O4  . NAG V  2 .   A 62.523  -9.590  85.018  1.00 73.48  ? 434 NAG C O4  1 
HETATM 14156 O  O5  . NAG V  2 .   A 62.260  -5.847  84.645  1.00 67.43  ? 434 NAG C O5  1 
HETATM 14157 O  O6  . NAG V  2 .   A 61.193  -6.312  86.911  1.00 71.04  ? 434 NAG C O6  1 
HETATM 14158 O  O7  . NAG V  2 .   A 64.088  -6.693  81.004  1.00 58.03  ? 434 NAG C O7  1 
HETATM 14159 C  C1  . NAG W  2 .   A 72.328  24.065  75.923  1.00 28.93  ? 435 NAG C C1  1 
HETATM 14160 C  C2  . NAG W  2 .   A 73.756  23.689  75.590  1.00 33.74  ? 435 NAG C C2  1 
HETATM 14161 C  C3  . NAG W  2 .   A 74.341  22.967  76.792  1.00 43.81  ? 435 NAG C C3  1 
HETATM 14162 C  C4  . NAG W  2 .   A 74.294  23.825  78.039  1.00 41.63  ? 435 NAG C C4  1 
HETATM 14163 C  C5  . NAG W  2 .   A 72.826  24.296  78.266  1.00 40.07  ? 435 NAG C C5  1 
HETATM 14164 C  C6  . NAG W  2 .   A 72.757  25.342  79.380  1.00 51.94  ? 435 NAG C C6  1 
HETATM 14165 C  C7  . NAG W  2 .   A 73.784  23.238  73.198  1.00 35.16  ? 435 NAG C C7  1 
HETATM 14166 C  C8  . NAG W  2 .   A 73.876  22.167  72.118  1.00 28.19  ? 435 NAG C C8  1 
HETATM 14167 N  N2  . NAG W  2 .   A 73.810  22.792  74.446  1.00 29.52  ? 435 NAG C N2  1 
HETATM 14168 O  O3  . NAG W  2 .   A 75.680  22.564  76.527  1.00 54.78  ? 435 NAG C O3  1 
HETATM 14169 O  O4  . NAG W  2 .   A 74.822  23.077  79.161  1.00 43.63  ? 435 NAG C O4  1 
HETATM 14170 O  O5  . NAG W  2 .   A 72.295  24.924  77.068  1.00 32.69  ? 435 NAG C O5  1 
HETATM 14171 O  O6  . NAG W  2 .   A 71.486  25.977  79.470  1.00 64.84  ? 435 NAG C O6  1 
HETATM 14172 O  O7  . NAG W  2 .   A 73.626  24.424  72.910  1.00 44.70  ? 435 NAG C O7  1 
HETATM 14173 C  C1  . NAG X  2 .   A 50.654  7.027   48.538  1.00 104.63 ? 436 NAG C C1  1 
HETATM 14174 C  C2  . NAG X  2 .   A 49.212  6.924   47.932  1.00 114.37 ? 436 NAG C C2  1 
HETATM 14175 C  C3  . NAG X  2 .   A 49.366  6.639   46.414  1.00 118.40 ? 436 NAG C C3  1 
HETATM 14176 C  C4  . NAG X  2 .   A 49.848  7.965   45.780  1.00 119.07 ? 436 NAG C C4  1 
HETATM 14177 C  C5  . NAG X  2 .   A 50.950  8.660   46.662  1.00 116.22 ? 436 NAG C C5  1 
HETATM 14178 C  C6  . NAG X  2 .   A 50.576  9.972   47.391  1.00 116.98 ? 436 NAG C C6  1 
HETATM 14179 C  C7  . NAG X  2 .   A 48.552  4.653   48.652  1.00 120.19 ? 436 NAG C C7  1 
HETATM 14180 C  C8  . NAG X  2 .   A 47.489  3.875   49.408  1.00 121.11 ? 436 NAG C C8  1 
HETATM 14181 N  N2  . NAG X  2 .   A 48.326  5.967   48.605  1.00 117.30 ? 436 NAG C N2  1 
HETATM 14182 O  O3  . NAG X  2 .   A 48.138  6.181   45.814  1.00 121.14 ? 436 NAG C O3  1 
HETATM 14183 O  O4  . NAG X  2 .   A 50.328  7.747   44.449  1.00 120.17 ? 436 NAG C O4  1 
HETATM 14184 O  O5  . NAG X  2 .   A 51.570  7.743   47.644  1.00 109.42 ? 436 NAG C O5  1 
HETATM 14185 O  O6  . NAG X  2 .   A 49.169  10.177  47.523  1.00 122.11 ? 436 NAG C O6  1 
HETATM 14186 O  O7  . NAG X  2 .   A 49.539  4.089   48.152  1.00 122.73 ? 436 NAG C O7  1 
HETATM 14187 C  C1  . NAG Y  2 .   A 49.161  45.495  93.110  1.00 73.33  ? 437 NAG C C1  1 
HETATM 14188 C  C2  . NAG Y  2 .   A 48.887  46.416  94.310  1.00 82.95  ? 437 NAG C C2  1 
HETATM 14189 C  C3  . NAG Y  2 .   A 49.524  47.824  94.107  1.00 84.98  ? 437 NAG C C3  1 
HETATM 14190 C  C4  . NAG Y  2 .   A 51.033  47.631  93.868  1.00 84.17  ? 437 NAG C C4  1 
HETATM 14191 C  C5  . NAG Y  2 .   A 51.164  46.770  92.606  1.00 81.45  ? 437 NAG C C5  1 
HETATM 14192 C  C6  . NAG Y  2 .   A 52.607  46.487  92.236  1.00 85.95  ? 437 NAG C C6  1 
HETATM 14193 C  C7  . NAG Y  2 .   A 46.873  46.132  95.623  1.00 94.51  ? 437 NAG C C7  1 
HETATM 14194 C  C8  . NAG Y  2 .   A 45.357  46.286  95.647  1.00 96.90  ? 437 NAG C C8  1 
HETATM 14195 N  N2  . NAG Y  2 .   A 47.451  46.531  94.490  1.00 89.37  ? 437 NAG C N2  1 
HETATM 14196 O  O3  . NAG Y  2 .   A 49.281  48.688  95.229  1.00 90.37  ? 437 NAG C O3  1 
HETATM 14197 O  O4  . NAG Y  2 .   A 51.728  48.885  93.725  1.00 82.53  ? 437 NAG C O4  1 
HETATM 14198 O  O5  . NAG Y  2 .   A 50.556  45.480  92.809  1.00 74.58  ? 437 NAG C O5  1 
HETATM 14199 O  O6  . NAG Y  2 .   A 53.058  45.277  92.844  1.00 90.85  ? 437 NAG C O6  1 
HETATM 14200 O  O7  . NAG Y  2 .   A 47.505  45.698  96.607  1.00 98.63  ? 437 NAG C O7  1 
HETATM 14201 FE FE  . FE  Z  3 .   ? 56.887  29.176  63.562  1.00 27.79  ? 438 FE  C FE  1 
HETATM 14202 ZN ZN  . ZN  AA 4 .   ? 53.679  29.086  62.584  1.00 31.04  ? 439 ZN  C ZN  1 
HETATM 14203 P  P   . PO4 BA 5 .   ? 56.211  29.539  60.878  1.00 26.39  ? 440 PO4 C P   1 
HETATM 14204 O  O1  . PO4 BA 5 .   ? 56.421  30.988  61.036  1.00 36.40  ? 440 PO4 C O1  1 
HETATM 14205 O  O2  . PO4 BA 5 .   ? 56.975  28.800  61.837  1.00 25.98  ? 440 PO4 C O2  1 
HETATM 14206 O  O3  . PO4 BA 5 .   ? 54.793  29.159  60.960  1.00 29.32  ? 440 PO4 C O3  1 
HETATM 14207 O  O4  . PO4 BA 5 .   ? 56.730  29.134  59.396  1.00 42.35  ? 440 PO4 C O4  1 
HETATM 14208 C  C1  . NAG CA 2 .   A 69.922  97.350  57.879  1.00 45.17  ? 433 NAG D C1  1 
HETATM 14209 C  C2  . NAG CA 2 .   A 69.202  96.692  59.075  1.00 50.91  ? 433 NAG D C2  1 
HETATM 14210 C  C3  . NAG CA 2 .   A 69.157  97.589  60.333  1.00 52.67  ? 433 NAG D C3  1 
HETATM 14211 C  C4  . NAG CA 2 .   A 70.609  97.890  60.698  1.00 56.18  ? 433 NAG D C4  1 
HETATM 14212 C  C5  . NAG CA 2 .   A 71.224  98.612  59.470  1.00 54.52  ? 433 NAG D C5  1 
HETATM 14213 C  C6  . NAG CA 2 .   A 72.668  99.036  59.666  1.00 57.47  ? 433 NAG D C6  1 
HETATM 14214 C  C7  . NAG CA 2 .   A 67.611  95.135  58.215  1.00 63.33  ? 433 NAG D C7  1 
HETATM 14215 C  C8  . NAG CA 2 .   A 66.170  94.901  57.825  1.00 64.61  ? 433 NAG D C8  1 
HETATM 14216 N  N2  . NAG CA 2 .   A 67.860  96.354  58.676  1.00 60.98  ? 433 NAG D N2  1 
HETATM 14217 O  O3  . NAG CA 2 .   A 68.459  96.958  61.427  1.00 55.02  ? 433 NAG D O3  1 
HETATM 14218 O  O4  . NAG CA 2 .   A 70.695  98.682  61.903  1.00 62.15  ? 433 NAG D O4  1 
HETATM 14219 O  O5  . NAG CA 2 .   A 71.218  97.753  58.299  1.00 46.47  ? 433 NAG D O5  1 
HETATM 14220 O  O6  . NAG CA 2 .   A 73.390  99.029  58.431  1.00 51.41  ? 433 NAG D O6  1 
HETATM 14221 O  O7  . NAG CA 2 .   A 68.476  94.246  58.121  1.00 62.36  ? 433 NAG D O7  1 
HETATM 14222 C  C1  . NAG DA 2 .   A 44.760  80.479  53.954  1.00 59.36  ? 434 NAG D C1  1 
HETATM 14223 C  C2  . NAG DA 2 .   A 44.580  79.536  55.153  1.00 67.29  ? 434 NAG D C2  1 
HETATM 14224 C  C3  . NAG DA 2 .   A 45.024  78.086  54.745  1.00 74.21  ? 434 NAG D C3  1 
HETATM 14225 C  C4  . NAG DA 2 .   A 43.974  77.668  53.685  1.00 73.13  ? 434 NAG D C4  1 
HETATM 14226 C  C5  . NAG DA 2 .   A 44.078  78.671  52.499  1.00 66.23  ? 434 NAG D C5  1 
HETATM 14227 C  C6  . NAG DA 2 .   A 43.073  78.389  51.380  1.00 69.20  ? 434 NAG D C6  1 
HETATM 14228 C  C7  . NAG DA 2 .   A 46.538  80.217  56.356  1.00 63.99  ? 434 NAG D C7  1 
HETATM 14229 C  C8  . NAG DA 2 .   A 47.064  80.723  57.678  1.00 59.20  ? 434 NAG D C8  1 
HETATM 14230 N  N2  . NAG DA 2 .   A 45.236  80.031  56.344  1.00 63.88  ? 434 NAG D N2  1 
HETATM 14231 O  O3  . NAG DA 2 .   A 45.083  77.159  55.865  1.00 76.94  ? 434 NAG D O3  1 
HETATM 14232 O  O4  . NAG DA 2 .   A 44.128  76.294  53.267  1.00 76.79  ? 434 NAG D O4  1 
HETATM 14233 O  O5  . NAG DA 2 .   A 43.847  80.050  52.942  1.00 57.26  ? 434 NAG D O5  1 
HETATM 14234 O  O6  . NAG DA 2 .   A 41.872  79.152  51.522  1.00 70.16  ? 434 NAG D O6  1 
HETATM 14235 O  O7  . NAG DA 2 .   A 47.274  79.969  55.386  1.00 72.44  ? 434 NAG D O7  1 
HETATM 14236 C  C1  . NAG EA 2 .   A 45.276  111.069 63.352  1.00 44.71  ? 435 NAG D C1  1 
HETATM 14237 C  C2  . NAG EA 2 .   A 45.423  110.708 64.818  1.00 47.38  ? 435 NAG D C2  1 
HETATM 14238 C  C3  . NAG EA 2 .   A 44.293  109.746 65.179  1.00 53.24  ? 435 NAG D C3  1 
HETATM 14239 C  C4  . NAG EA 2 .   A 42.925  110.328 64.920  1.00 54.10  ? 435 NAG D C4  1 
HETATM 14240 C  C5  . NAG EA 2 .   A 42.871  110.800 63.447  1.00 53.64  ? 435 NAG D C5  1 
HETATM 14241 C  C6  . NAG EA 2 .   A 41.590  111.591 63.139  1.00 62.47  ? 435 NAG D C6  1 
HETATM 14242 C  C7  . NAG EA 2 .   A 47.815  110.729 65.250  1.00 48.09  ? 435 NAG D C7  1 
HETATM 14243 C  C8  . NAG EA 2 .   A 49.038  109.883 65.569  1.00 48.17  ? 435 NAG D C8  1 
HETATM 14244 N  N2  . NAG EA 2 .   A 46.686  110.047 65.093  1.00 48.30  ? 435 NAG D N2  1 
HETATM 14245 O  O3  . NAG EA 2 .   A 44.377  109.388 66.543  1.00 66.67  ? 435 NAG D O3  1 
HETATM 14246 O  O4  . NAG EA 2 .   A 41.930  109.328 65.226  1.00 43.14  ? 435 NAG D O4  1 
HETATM 14247 O  O5  . NAG EA 2 .   A 43.996  111.680 63.157  1.00 48.75  ? 435 NAG D O5  1 
HETATM 14248 O  O6  . NAG EA 2 .   A 41.589  112.199 61.842  1.00 75.02  ? 435 NAG D O6  1 
HETATM 14249 O  O7  . NAG EA 2 .   A 47.898  111.952 65.086  1.00 51.74  ? 435 NAG D O7  1 
HETATM 14250 C  C1  . NAG FA 2 .   A 78.523  99.251  46.956  1.00 109.62 ? 436 NAG D C1  1 
HETATM 14251 C  C2  . NAG FA 2 .   A 79.347  99.271  45.638  1.00 118.48 ? 436 NAG D C2  1 
HETATM 14252 C  C3  . NAG FA 2 .   A 80.855  99.289  46.028  1.00 121.81 ? 436 NAG D C3  1 
HETATM 14253 C  C4  . NAG FA 2 .   A 81.156  100.704 46.554  1.00 120.63 ? 436 NAG D C4  1 
HETATM 14254 C  C5  . NAG FA 2 .   A 79.985  101.224 47.461  1.00 117.40 ? 436 NAG D C5  1 
HETATM 14255 C  C6  . NAG FA 2 .   A 79.100  102.363 46.910  1.00 118.80 ? 436 NAG D C6  1 
HETATM 14256 C  C7  . NAG FA 2 .   A 79.120  96.886  44.979  1.00 124.86 ? 436 NAG D C7  1 
HETATM 14257 C  C8  . NAG FA 2 .   A 78.681  95.962  43.838  1.00 124.33 ? 436 NAG D C8  1 
HETATM 14258 N  N2  . NAG FA 2 .   A 78.998  98.192  44.707  1.00 124.64 ? 436 NAG D N2  1 
HETATM 14259 O  O3  . NAG FA 2 .   A 81.721  98.967  44.928  1.00 123.28 ? 436 NAG D O3  1 
HETATM 14260 O  O4  . NAG FA 2 .   A 82.408  100.736 47.258  1.00 120.86 ? 436 NAG D O4  1 
HETATM 14261 O  O5  . NAG FA 2 .   A 79.102  100.142 47.960  1.00 112.21 ? 436 NAG D O5  1 
HETATM 14262 O  O6  . NAG FA 2 .   A 79.187  102.519 45.493  1.00 122.41 ? 436 NAG D O6  1 
HETATM 14263 O  O7  . NAG FA 2 .   A 79.545  96.431  46.052  1.00 124.41 ? 436 NAG D O7  1 
HETATM 14264 C  C1  . NAG GA 2 .   A 28.578  128.904 36.989  1.00 73.02  ? 437 NAG D C1  1 
HETATM 14265 C  C2  . NAG GA 2 .   A 27.229  129.559 36.541  1.00 74.15  ? 437 NAG D C2  1 
HETATM 14266 C  C3  . NAG GA 2 .   A 27.079  130.996 37.126  1.00 78.18  ? 437 NAG D C3  1 
HETATM 14267 C  C4  . NAG GA 2 .   A 27.149  130.842 38.680  1.00 78.19  ? 437 NAG D C4  1 
HETATM 14268 C  C5  . NAG GA 2 .   A 28.555  130.262 39.013  1.00 79.46  ? 437 NAG D C5  1 
HETATM 14269 C  C6  . NAG GA 2 .   A 28.760  130.038 40.506  1.00 85.07  ? 437 NAG D C6  1 
HETATM 14270 C  C7  . NAG GA 2 .   A 26.287  128.976 34.359  1.00 69.47  ? 437 NAG D C7  1 
HETATM 14271 C  C8  . NAG GA 2 .   A 26.490  129.105 32.834  1.00 71.17  ? 437 NAG D C8  1 
HETATM 14272 N  N2  . NAG GA 2 .   A 27.218  129.605 35.088  1.00 77.20  ? 437 NAG D N2  1 
HETATM 14273 O  O3  . NAG GA 2 .   A 25.876  131.667 36.656  1.00 75.08  ? 437 NAG D O3  1 
HETATM 14274 O  O4  . NAG GA 2 .   A 26.926  132.079 39.398  1.00 74.61  ? 437 NAG D O4  1 
HETATM 14275 O  O5  . NAG GA 2 .   A 28.744  128.966 38.412  1.00 71.82  ? 437 NAG D O5  1 
HETATM 14276 O  O6  . NAG GA 2 .   A 28.321  128.732 40.894  1.00 86.09  ? 437 NAG D O6  1 
HETATM 14277 O  O7  . NAG GA 2 .   A 25.305  128.376 34.850  1.00 46.26  ? 437 NAG D O7  1 
HETATM 14278 FE FE  . FE  HA 3 .   ? 58.934  118.231 49.920  1.00 31.84  ? 438 FE  D FE  1 
HETATM 14279 ZN ZN  . ZN  IA 4 .   ? 60.400  118.282 46.983  1.00 32.97  ? 439 ZN  D ZN  1 
HETATM 14280 P  P   . PO4 JA 5 .   ? 61.610  119.088 49.703  1.00 34.08  ? 440 PO4 D P   1 
HETATM 14281 O  O1  . PO4 JA 5 .   ? 61.104  120.510 49.883  1.00 46.06  ? 440 PO4 D O1  1 
HETATM 14282 O  O2  . PO4 JA 5 .   ? 60.688  118.174 50.313  1.00 28.64  ? 440 PO4 D O2  1 
HETATM 14283 O  O3  . PO4 JA 5 .   ? 61.786  118.696 48.295  1.00 31.50  ? 440 PO4 D O3  1 
HETATM 14284 O  O4  . PO4 JA 5 .   ? 63.042  119.005 50.456  1.00 49.42  ? 440 PO4 D O4  1 
HETATM 14285 O  O   . HOH KA 6 .   ? 81.467  92.347  54.847  1.00 6.34   ? 441 HOH A O   1 
HETATM 14286 O  O   . HOH KA 6 .   ? 62.560  90.907  45.065  1.00 16.60  ? 442 HOH A O   1 
HETATM 14287 O  O   . HOH KA 6 .   ? 76.846  69.765  29.544  1.00 17.97  ? 443 HOH A O   1 
HETATM 14288 O  O   . HOH KA 6 .   ? 77.409  58.874  54.911  1.00 26.10  ? 444 HOH A O   1 
HETATM 14289 O  O   . HOH KA 6 .   ? 85.389  84.760  42.181  1.00 33.93  ? 445 HOH A O   1 
HETATM 14290 O  O   . HOH KA 6 .   ? 73.152  53.399  63.822  1.00 39.92  ? 446 HOH A O   1 
HETATM 14291 O  O   . HOH KA 6 .   ? 75.103  74.147  42.081  1.00 45.50  ? 447 HOH A O   1 
HETATM 14292 O  O   . HOH KA 6 .   ? 102.712 74.812  43.704  1.00 34.33  ? 448 HOH A O   1 
HETATM 14293 O  O   . HOH KA 6 .   ? 67.751  55.338  37.188  1.00 33.08  ? 449 HOH A O   1 
HETATM 14294 O  O   . HOH KA 6 .   ? 70.218  65.186  40.186  1.00 13.90  ? 450 HOH A O   1 
HETATM 14295 O  O   . HOH KA 6 .   ? 81.814  70.188  44.290  1.00 51.76  ? 451 HOH A O   1 
HETATM 14296 O  O   . HOH KA 6 .   ? 75.063  66.264  40.665  1.00 27.49  ? 452 HOH A O   1 
HETATM 14297 O  O   . HOH KA 6 .   ? 72.138  49.996  48.754  1.00 22.76  ? 453 HOH A O   1 
HETATM 14298 O  O   . HOH KA 6 .   ? 84.402  89.586  52.883  1.00 38.20  ? 454 HOH A O   1 
HETATM 14299 O  O   . HOH KA 6 .   ? 89.497  54.188  32.523  1.00 29.49  ? 455 HOH A O   1 
HETATM 14300 O  O   . HOH KA 6 .   ? 92.671  61.699  34.243  1.00 28.51  ? 456 HOH A O   1 
HETATM 14301 O  O   . HOH LA 6 .   ? 17.754  -5.956  46.347  1.00 15.93  ? 441 HOH B O   1 
HETATM 14302 O  O   . HOH LA 6 .   ? 42.627  17.974  50.877  1.00 29.81  ? 442 HOH B O   1 
HETATM 14303 O  O   . HOH LA 6 .   ? 16.669  27.991  45.024  1.00 43.82  ? 443 HOH B O   1 
HETATM 14304 O  O   . HOH LA 6 .   ? 5.519   37.423  45.629  1.00 69.20  ? 444 HOH B O   1 
HETATM 14305 O  O   . HOH LA 6 .   ? 30.164  17.727  49.291  1.00 68.53  ? 445 HOH B O   1 
HETATM 14306 O  O   . HOH LA 6 .   ? 33.504  33.317  56.042  1.00 25.00  ? 446 HOH B O   1 
HETATM 14307 O  O   . HOH LA 6 .   ? 30.640  23.333  55.100  1.00 30.49  ? 447 HOH B O   1 
HETATM 14308 O  O   . HOH LA 6 .   ? 28.279  15.869  44.136  1.00 36.20  ? 448 HOH B O   1 
HETATM 14309 O  O   . HOH LA 6 .   ? 30.635  21.053  50.540  1.00 35.22  ? 449 HOH B O   1 
HETATM 14310 O  O   . HOH LA 6 .   ? 22.769  37.362  49.432  1.00 25.79  ? 450 HOH B O   1 
HETATM 14311 O  O   . HOH LA 6 .   ? 20.770  -4.171  43.856  1.00 37.08  ? 451 HOH B O   1 
HETATM 14312 O  O   . HOH LA 6 .   ? 41.854  30.893  35.052  1.00 46.54  ? 452 HOH B O   1 
HETATM 14313 O  O   . HOH LA 6 .   ? 39.888  22.444  33.584  1.00 42.59  ? 453 HOH B O   1 
HETATM 14314 O  O   . HOH MA 6 .   ? 58.786  0.537   82.916  1.00 9.45   ? 441 HOH C O   1 
HETATM 14315 O  O   . HOH MA 6 .   ? 33.783  21.387  70.628  1.00 35.31  ? 442 HOH C O   1 
HETATM 14316 O  O   . HOH MA 6 .   ? 58.865  32.821  72.728  1.00 25.35  ? 443 HOH C O   1 
HETATM 14317 O  O   . HOH MA 6 .   ? 45.364  8.395   82.867  1.00 46.17  ? 444 HOH C O   1 
HETATM 14318 O  O   . HOH MA 6 .   ? 68.393  37.751  69.464  1.00 32.39  ? 445 HOH C O   1 
HETATM 14319 O  O   . HOH MA 6 .   ? 46.217  21.627  72.187  1.00 51.75  ? 446 HOH C O   1 
HETATM 14320 O  O   . HOH MA 6 .   ? 43.802  33.821  61.034  1.00 34.09  ? 447 HOH C O   1 
HETATM 14321 O  O   . HOH MA 6 .   ? 45.497  25.275  64.993  1.00 38.54  ? 448 HOH C O   1 
HETATM 14322 O  O   . HOH MA 6 .   ? 47.763  21.748  77.890  1.00 44.90  ? 449 HOH C O   1 
HETATM 14323 O  O   . HOH MA 6 .   ? 45.657  24.916  69.871  1.00 32.92  ? 450 HOH C O   1 
HETATM 14324 O  O   . HOH MA 6 .   ? 53.215  40.295  65.136  1.00 35.98  ? 451 HOH C O   1 
HETATM 14325 O  O   . HOH MA 6 .   ? 56.212  3.211   84.800  1.00 41.68  ? 452 HOH C O   1 
HETATM 14326 O  O   . HOH MA 6 .   ? 35.350  39.503  81.405  1.00 44.09  ? 453 HOH C O   1 
HETATM 14327 O  O   . HOH MA 6 .   ? 36.515  31.998  85.437  1.00 21.90  ? 454 HOH C O   1 
HETATM 14328 O  O   . HOH NA 6 .   ? 45.060  86.669  49.492  1.00 16.52  ? 441 HOH D O   1 
HETATM 14329 O  O   . HOH NA 6 .   ? 66.355  87.732  45.792  1.00 47.50  ? 442 HOH D O   1 
HETATM 14330 O  O   . HOH NA 6 .   ? 56.712  109.358 26.179  1.00 34.74  ? 443 HOH D O   1 
HETATM 14331 O  O   . HOH NA 6 .   ? 49.177  120.423 50.640  1.00 46.02  ? 444 HOH D O   1 
HETATM 14332 O  O   . HOH NA 6 .   ? 54.164  108.921 38.647  1.00 52.25  ? 445 HOH D O   1 
HETATM 14333 O  O   . HOH NA 6 .   ? 28.364  104.132 31.606  1.00 51.97  ? 446 HOH D O   1 
HETATM 14334 O  O   . HOH NA 6 .   ? 63.012  123.284 36.209  1.00 22.27  ? 447 HOH D O   1 
HETATM 14335 O  O   . HOH NA 6 .   ? 60.170  114.256 38.710  1.00 25.36  ? 448 HOH D O   1 
HETATM 14336 O  O   . HOH NA 6 .   ? 55.961  112.982 37.902  1.00 36.45  ? 449 HOH D O   1 
HETATM 14337 O  O   . HOH NA 6 .   ? 55.826  128.830 45.834  1.00 23.79  ? 450 HOH D O   1 
HETATM 14338 O  O   . HOH NA 6 .   ? 42.354  89.140  46.549  1.00 48.24  ? 451 HOH D O   1 
HETATM 14339 O  O   . HOH NA 6 .   ? 43.795  125.057 25.271  1.00 29.30  ? 452 HOH D O   1 
HETATM 14340 O  O   . HOH NA 6 .   ? 40.686  116.968 25.967  1.00 33.65  ? 453 HOH D 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   PHE 1   1   ?   ?   ?   A . n 
A 1 2   VAL 2   2   ?   ?   ?   A . n 
A 1 3   ARG 3   3   ?   ?   ?   A . n 
A 1 4   LYS 4   4   ?   ?   ?   A . n 
A 1 5   THR 5   5   ?   ?   ?   A . n 
A 1 6   ASN 6   6   ?   ?   ?   A . n 
A 1 7   LYS 7   7   ?   ?   ?   A . n 
A 1 8   ASN 8   8   ?   ?   ?   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  MET 11  11  11  MET MET A . n 
A 1 12  PRO 12  12  12  PRO PRO A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  PHE 18  18  18  PHE PHE A . n 
A 1 19  ARG 19  19  19  ARG ARG A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  PRO 22  22  22  PRO PRO A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  ASN 25  25  25  ASN ASN A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  PRO 27  27  27  PRO PRO A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  GLN 29  29  29  GLN GLN A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  HIS 31  31  31  HIS HIS A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  GLN 34  34  34  GLN GLN A . n 
A 1 35  GLY 35  35  35  GLY GLY A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  MET 42  42  42  MET MET A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  TRP 46  46  46  TRP TRP A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  THR 48  48  48  THR THR A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  SER 55  55  55  SER SER A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  TRP 60  60  60  TRP TRP A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  LYS 63  63  63  LYS LYS A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  MET 74  74  74  MET MET A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  THR 76  76  76  THR THR A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  ARG 78  78  78  ARG ARG A . n 
A 1 79  PHE 79  79  79  PHE PHE A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  ASN 81  81  81  ASN ASN A . n 
A 1 82  TYR 82  82  82  TYR TYR A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  PHE 86  86  86  PHE PHE A . n 
A 1 87  ILE 87  87  87  ILE ILE A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  HIS 89  89  89  HIS HIS A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 TYR 102 102 102 TYR TYR A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 VAL 105 105 105 VAL VAL 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 ARG 108 108 108 ARG ARG A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 THR 110 110 110 THR THR A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 PRO 119 119 119 PRO PRO A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 GLN 121 121 121 GLN GLN A . n 
A 1 122 THR 122 122 122 THR THR A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 TYR 128 128 128 TYR TYR A . n 
A 1 129 THR 129 129 129 THR THR A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 ILE 133 133 133 ILE ILE A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ASN 143 143 143 ASN ASN A . n 
A 1 144 THR 144 144 144 THR THR A . n 
A 1 145 THR 145 145 145 THR THR A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 HIS 148 148 148 HIS HIS A . n 
A 1 149 TYR 149 149 149 TYR TYR A . n 
A 1 150 GLU 150 150 150 GLU GLU A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 LYS 154 154 154 LYS LYS A . n 
A 1 155 LYS 155 155 155 LYS LYS A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 ASP 169 169 169 ASP ASP A . n 
A 1 170 ARG 170 170 170 ARG ARG A . n 
A 1 171 TYR 171 171 171 TYR TYR A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 ASN 173 173 173 ASN ASN A . n 
A 1 174 HIS 174 174 174 HIS HIS A . n 
A 1 175 ASP 175 175 175 ASP ASP A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 ARG 178 178 178 ARG ARG A . n 
A 1 179 TRP 179 179 179 TRP TRP A . n 
A 1 180 ASP 180 180 180 ASP ASP A . n 
A 1 181 THR 181 181 181 THR THR A . n 
A 1 182 TRP 182 182 182 TRP TRP A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 THR 186 186 186 THR THR A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 GLN 193 193 193 GLN GLN A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 TRP 195 195 195 TRP TRP A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 TRP 197 197 197 TRP TRP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 GLY 200 200 200 GLY GLY A . n 
A 1 201 ASN 201 201 201 ASN ASN A . n 
A 1 202 HIS 202 202 202 HIS HIS A . n 
A 1 203 GLU 203 203 203 GLU GLU A . n 
A 1 204 ILE 204 204 204 ILE ILE A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 PHE 206 206 206 PHE PHE A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 PRO 208 208 208 PRO PRO A . n 
A 1 209 GLU 209 209 209 GLU GLU A . n 
A 1 210 ILE 210 210 210 ILE ILE A . n 
A 1 211 ASN 211 211 211 ASN ASN A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 PHE 216 216 216 PHE PHE A . n 
A 1 217 LYS 217 217 217 LYS LYS A . n 
A 1 218 PRO 218 218 218 PRO PRO A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 TYR 221 221 221 TYR TYR A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 TYR 223 223 223 TYR TYR A . n 
A 1 224 HIS 224 224 224 HIS HIS A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 PRO 226 226 226 PRO PRO A . n 
A 1 227 TYR 227 227 227 TYR TYR A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 GLN 231 231 231 GLN GLN A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 THR 233 233 233 THR THR A . n 
A 1 234 SER 234 234 234 SER SER A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 PHE 236 236 236 PHE PHE A . n 
A 1 237 TRP 237 237 237 TRP TRP A . n 
A 1 238 TYR 238 238 238 TYR TYR A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 ILE 240 240 240 ILE ILE A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 ARG 242 242 242 ARG ARG A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 ALA 245 245 245 ALA ALA A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 ILE 247 247 247 ILE ILE A . n 
A 1 248 ILE 248 248 248 ILE ILE A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 SER 251 251 251 SER SER A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 TYR 253 253 253 TYR TYR A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 GLY 257 257 257 GLY GLY A . n 
A 1 258 ARG 258 258 258 ARG ARG A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 THR 260 260 260 THR THR A . n 
A 1 261 PRO 261 261 261 PRO PRO A . n 
A 1 262 GLN 262 262 262 GLN GLN A . n 
A 1 263 TYR 263 263 263 TYR TYR A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 TRP 265 265 265 TRP TRP A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 LYS 267 267 267 LYS LYS A . n 
A 1 268 LYS 268 268 268 LYS LYS A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 ARG 271 271 271 ARG ARG A . n 
A 1 272 LYS 272 272 272 LYS LYS A . n 
A 1 273 VAL 273 273 273 VAL VAL A . n 
A 1 274 LYS 274 274 274 LYS LYS A . n 
A 1 275 ARG 275 275 275 ARG ARG A . n 
A 1 276 SER 276 276 276 SER SER A . n 
A 1 277 GLU 277 277 277 GLU GLU A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 PRO 279 279 279 PRO PRO A . n 
A 1 280 TRP 280 280 280 TRP TRP A . n 
A 1 281 LEU 281 281 281 LEU LEU A . n 
A 1 282 ILE 282 282 282 ILE ILE A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 LEU 284 284 284 LEU LEU A . n 
A 1 285 MET 285 285 285 MET MET A . n 
A 1 286 HIS 286 286 286 HIS HIS A . n 
A 1 287 SER 287 287 287 SER SER A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 LEU 289 289 289 LEU LEU A . n 
A 1 290 TYR 290 290 290 TYR TYR A . n 
A 1 291 ASN 291 291 291 ASN ASN A . n 
A 1 292 SER 292 292 292 SER SER A . n 
A 1 293 TYR 293 293 293 TYR TYR A . n 
A 1 294 ASN 294 294 294 ASN ASN A . n 
A 1 295 HIS 295 295 295 HIS HIS A . n 
A 1 296 HIS 296 296 296 HIS HIS A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 MET 298 298 298 MET MET A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 GLY 300 300 300 GLY GLY A . n 
A 1 301 GLU 301 301 301 GLU GLU A . n 
A 1 302 ALA 302 302 302 ALA ALA A . n 
A 1 303 MET 303 303 303 MET MET A . n 
A 1 304 ARG 304 304 304 ARG ARG A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 LYS 306 306 306 LYS LYS A . n 
A 1 307 PHE 307 307 307 PHE PHE A . n 
A 1 308 GLU 308 308 308 GLU GLU A . n 
A 1 309 ALA 309 309 309 ALA ALA A . n 
A 1 310 TRP 310 310 310 TRP TRP A . n 
A 1 311 PHE 311 311 311 PHE PHE A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 LYS 313 313 313 LYS LYS A . n 
A 1 314 TYR 314 314 314 TYR TYR A . n 
A 1 315 LYS 315 315 315 LYS LYS A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 ASP 317 317 317 ASP ASP A . n 
A 1 318 VAL 318 318 318 VAL VAL A . n 
A 1 319 VAL 319 319 319 VAL VAL A . n 
A 1 320 PHE 320 320 320 PHE PHE A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 GLY 322 322 322 GLY GLY A . n 
A 1 323 HIS 323 323 323 HIS HIS A . n 
A 1 324 VAL 324 324 324 VAL VAL A . n 
A 1 325 HIS 325 325 325 HIS HIS A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 TYR 327 327 327 TYR TYR A . n 
A 1 328 GLU 328 328 328 GLU GLU A . n 
A 1 329 ARG 329 329 329 ARG ARG A . n 
A 1 330 SER 330 330 330 SER SER A . n 
A 1 331 GLU 331 331 331 GLU GLU A . n 
A 1 332 ARG 332 332 332 ARG ARG A . n 
A 1 333 VAL 333 333 333 VAL VAL A . n 
A 1 334 SER 334 334 334 SER SER A . n 
A 1 335 ASN 335 335 335 ASN ASN A . n 
A 1 336 ILE 336 336 336 ILE ILE A . n 
A 1 337 ALA 337 337 337 ALA ALA A . n 
A 1 338 TYR 338 338 338 TYR TYR A . n 
A 1 339 LYS 339 339 339 LYS LYS A . n 
A 1 340 ILE 340 340 340 ILE ILE A . n 
A 1 341 THR 341 341 341 THR THR A . n 
A 1 342 ASP 342 342 342 ASP ASP A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 LEU 344 344 344 LEU LEU A . n 
A 1 345 CYS 345 345 345 CYS CYS A . n 
A 1 346 THR 346 346 346 THR THR A . n 
A 1 347 PRO 347 347 347 PRO PRO A . n 
A 1 348 VAL 348 348 348 VAL VAL A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 ASP 350 350 350 ASP ASP A . n 
A 1 351 GLN 351 351 351 GLN GLN A . n 
A 1 352 SER 352 352 352 SER SER A . n 
A 1 353 ALA 353 353 353 ALA ALA A . n 
A 1 354 PRO 354 354 354 PRO PRO A . n 
A 1 355 VAL 355 355 355 VAL VAL A . n 
A 1 356 TYR 356 356 356 TYR TYR A . n 
A 1 357 ILE 357 357 357 ILE ILE A . n 
A 1 358 THR 358 358 358 THR THR A . n 
A 1 359 ILE 359 359 359 ILE ILE A . n 
A 1 360 GLY 360 360 360 GLY GLY A . n 
A 1 361 ASP 361 361 361 ASP ASP A . n 
A 1 362 ALA 362 362 362 ALA ALA A . n 
A 1 363 GLY 363 363 363 GLY GLY A . n 
A 1 364 ASN 364 364 364 ASN ASN A . n 
A 1 365 TYR 365 365 365 TYR TYR A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 ILE 368 368 368 ILE ILE A . n 
A 1 369 ASP 369 369 369 ASP ASP A . n 
A 1 370 SER 370 370 370 SER SER A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 MET 372 372 372 MET MET A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 GLN 374 374 374 GLN GLN A . n 
A 1 375 PRO 375 375 375 PRO PRO A . n 
A 1 376 GLN 376 376 376 GLN GLN A . n 
A 1 377 PRO 377 377 377 PRO PRO A . n 
A 1 378 GLU 378 378 378 GLU GLU A . n 
A 1 379 TYR 379 379 379 TYR TYR A . n 
A 1 380 SER 380 380 380 SER SER A . n 
A 1 381 ALA 381 381 381 ALA ALA A . n 
A 1 382 PHE 382 382 382 PHE PHE A . n 
A 1 383 ARG 383 383 383 ARG ARG A . n 
A 1 384 GLU 384 384 384 GLU GLU A . n 
A 1 385 ALA 385 385 385 ALA ALA A . n 
A 1 386 SER 386 386 386 SER SER A . n 
A 1 387 PHE 387 387 387 PHE PHE A . n 
A 1 388 GLY 388 388 388 GLY GLY A . n 
A 1 389 HIS 389 389 389 HIS HIS A . n 
A 1 390 GLY 390 390 390 GLY GLY A . n 
A 1 391 MET 391 391 391 MET MET A . n 
A 1 392 PHE 392 392 392 PHE PHE A . n 
A 1 393 ASP 393 393 393 ASP ASP A . n 
A 1 394 ILE 394 394 394 ILE ILE A . n 
A 1 395 LYS 395 395 395 LYS LYS A . n 
A 1 396 ASN 396 396 396 ASN ASN A . n 
A 1 397 ARG 397 397 397 ARG ARG A . n 
A 1 398 THR 398 398 398 THR THR A . n 
A 1 399 HIS 399 399 399 HIS HIS A . n 
A 1 400 ALA 400 400 400 ALA ALA A . n 
A 1 401 HIS 401 401 401 HIS HIS A . n 
A 1 402 PHE 402 402 402 PHE PHE A . n 
A 1 403 SER 403 403 403 SER SER A . n 
A 1 404 TRP 404 404 404 TRP TRP A . n 
A 1 405 ASN 405 405 405 ASN ASN A . n 
A 1 406 ARG 406 406 406 ARG ARG A . n 
A 1 407 ASN 407 407 407 ASN ASN A . n 
A 1 408 GLN 408 408 408 GLN GLN A . n 
A 1 409 ASP 409 409 409 ASP ASP A . n 
A 1 410 GLY 410 410 410 GLY GLY A . n 
A 1 411 VAL 411 411 411 VAL VAL A . n 
A 1 412 ALA 412 412 412 ALA ALA A . n 
A 1 413 VAL 413 413 413 VAL VAL A . n 
A 1 414 GLU 414 414 414 GLU GLU A . n 
A 1 415 ALA 415 415 415 ALA ALA A . n 
A 1 416 ASP 416 416 416 ASP ASP A . n 
A 1 417 SER 417 417 417 SER SER A . n 
A 1 418 VAL 418 418 418 VAL VAL A . n 
A 1 419 TRP 419 419 419 TRP TRP A . n 
A 1 420 PHE 420 420 420 PHE PHE A . n 
A 1 421 PHE 421 421 421 PHE PHE A . n 
A 1 422 ASN 422 422 422 ASN ASN A . n 
A 1 423 ARG 423 423 423 ARG ARG A . n 
A 1 424 HIS 424 424 424 HIS HIS A . n 
A 1 425 TRP 425 425 425 TRP TRP A . n 
A 1 426 TYR 426 426 426 TYR TYR A . n 
A 1 427 PRO 427 427 427 PRO PRO A . n 
A 1 428 VAL 428 428 428 VAL VAL A . n 
A 1 429 ASP 429 429 429 ASP ASP A . n 
A 1 430 ASP 430 430 430 ASP ASP A . n 
A 1 431 SER 431 431 431 SER SER A . n 
A 1 432 THR 432 432 432 THR THR A . n 
B 1 1   PHE 1   1   ?   ?   ?   B . n 
B 1 2   VAL 2   2   ?   ?   ?   B . n 
B 1 3   ARG 3   3   ?   ?   ?   B . n 
B 1 4   LYS 4   4   ?   ?   ?   B . n 
B 1 5   THR 5   5   ?   ?   ?   B . n 
B 1 6   ASN 6   6   ?   ?   ?   B . n 
B 1 7   LYS 7   7   ?   ?   ?   B . n 
B 1 8   ASN 8   8   ?   ?   ?   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  MET 11  11  11  MET MET B . n 
B 1 12  PRO 12  12  12  PRO PRO B . n 
B 1 13  LEU 13  13  13  LEU LEU B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  SER 15  15  15  SER SER B . n 
B 1 16  ASP 16  16  16  ASP ASP B . n 
B 1 17  VAL 17  17  17  VAL VAL B . n 
B 1 18  PHE 18  18  18  PHE PHE B . n 
B 1 19  ARG 19  19  19  ARG ARG B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  PRO 21  21  21  PRO PRO B . n 
B 1 22  PRO 22  22  22  PRO PRO B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  TYR 24  24  24  TYR TYR B . n 
B 1 25  ASN 25  25  25  ASN ASN B . n 
B 1 26  ALA 26  26  26  ALA ALA B . n 
B 1 27  PRO 27  27  27  PRO PRO B . n 
B 1 28  GLN 28  28  28  GLN GLN B . n 
B 1 29  GLN 29  29  29  GLN GLN B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  HIS 31  31  31  HIS HIS B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  GLN 34  34  34  GLN GLN B . n 
B 1 35  GLY 35  35  35  GLY GLY B . n 
B 1 36  ASP 36  36  36  ASP ASP B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  VAL 38  38  38  VAL VAL B . n 
B 1 39  GLY 39  39  39  GLY GLY B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  MET 42  42  42  MET MET B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  ILE 44  44  44  ILE ILE B . n 
B 1 45  SER 45  45  45  SER SER B . n 
B 1 46  TRP 46  46  46  TRP TRP B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  THR 48  48  48  THR THR B . n 
B 1 49  MET 49  49  49  MET MET B . n 
B 1 50  ASP 50  50  50  ASP ASP B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  GLY 53  53  53  GLY GLY B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  SER 55  55  55  SER SER B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  VAL 57  57  57  VAL VAL B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  TYR 59  59  59  TYR TYR B . n 
B 1 60  TRP 60  60  60  TRP TRP B . n 
B 1 61  SER 61  61  61  SER SER B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  LYS 63  63  63  LYS LYS B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  LYS 67  67  67  LYS LYS B . n 
B 1 68  ARG 68  68  68  ARG ARG B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  LYS 71  71  71  LYS LYS B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  LYS 73  73  73  LYS LYS B . n 
B 1 74  MET 74  74  74  MET MET B . n 
B 1 75  SER 75  75  75  SER SER B . n 
B 1 76  THR 76  76  76  THR THR B . n 
B 1 77  TYR 77  77  77  TYR TYR B . n 
B 1 78  ARG 78  78  78  ARG ARG B . n 
B 1 79  PHE 79  79  79  PHE PHE B . n 
B 1 80  PHE 80  80  80  PHE PHE B . n 
B 1 81  ASN 81  81  81  ASN ASN B . n 
B 1 82  TYR 82  82  82  TYR TYR B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  PHE 86  86  86  PHE PHE B . n 
B 1 87  ILE 87  87  87  ILE ILE B . n 
B 1 88  HIS 88  88  88  HIS HIS B . n 
B 1 89  HIS 89  89  89  HIS HIS B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  THR 91  91  91  THR THR B . n 
B 1 92  ILE 92  92  92  ILE ILE B . n 
B 1 93  ARG 93  93  93  ARG ARG B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  LYS 96  96  96  LYS LYS B . n 
B 1 97  TYR 97  97  97  TYR TYR B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 TYR 102 102 102 TYR TYR B . n 
B 1 103 TYR 103 103 103 TYR TYR B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 VAL 105 105 105 VAL VAL 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 ARG 108 108 108 ARG ARG B . n 
B 1 109 ASN 109 109 109 ASN ASN B . n 
B 1 110 THR 110 110 110 THR THR B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 ARG 112 112 112 ARG ARG B . n 
B 1 113 ARG 113 113 113 ARG ARG B . n 
B 1 114 PHE 114 114 114 PHE PHE B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ILE 117 117 117 ILE ILE B . n 
B 1 118 THR 118 118 118 THR THR B . n 
B 1 119 PRO 119 119 119 PRO PRO B . n 
B 1 120 PRO 120 120 120 PRO PRO B . n 
B 1 121 GLN 121 121 121 GLN GLN B . n 
B 1 122 THR 122 122 122 THR THR B . n 
B 1 123 GLY 123 123 123 GLY GLY B . n 
B 1 124 LEU 124 124 124 LEU LEU B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 VAL 126 126 126 VAL VAL B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 TYR 128 128 128 TYR TYR B . n 
B 1 129 THR 129 129 129 THR THR B . n 
B 1 130 PHE 130 130 130 PHE PHE B . n 
B 1 131 GLY 131 131 131 GLY GLY B . n 
B 1 132 LEU 132 132 132 LEU LEU B . n 
B 1 133 ILE 133 133 133 ILE ILE B . n 
B 1 134 GLY 134 134 134 GLY GLY B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 LEU 136 136 136 LEU LEU B . n 
B 1 137 GLY 137 137 137 GLY GLY B . n 
B 1 138 GLN 138 138 138 GLN GLN B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 ASP 141 141 141 ASP ASP B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ASN 143 143 143 ASN ASN B . n 
B 1 144 THR 144 144 144 THR THR B . n 
B 1 145 THR 145 145 145 THR THR B . n 
B 1 146 LEU 146 146 146 LEU LEU B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 HIS 148 148 148 HIS HIS B . n 
B 1 149 TYR 149 149 149 TYR TYR B . n 
B 1 150 GLU 150 150 150 GLU GLU B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 SER 152 152 152 SER SER B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 LYS 154 154 154 LYS LYS B . n 
B 1 155 LYS 155 155 155 LYS LYS B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 GLN 157 157 157 GLN GLN B . n 
B 1 158 THR 158 158 158 THR THR B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 PHE 161 161 161 PHE PHE B . n 
B 1 162 VAL 162 162 162 VAL VAL B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 ASP 164 164 164 ASP ASP B . n 
B 1 165 LEU 165 165 165 LEU LEU B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 ALA 168 168 168 ALA ALA B . n 
B 1 169 ASP 169 169 169 ASP ASP B . n 
B 1 170 ARG 170 170 170 ARG ARG B . n 
B 1 171 TYR 171 171 171 TYR TYR B . n 
B 1 172 PRO 172 172 172 PRO PRO B . n 
B 1 173 ASN 173 173 173 ASN ASN B . n 
B 1 174 HIS 174 174 174 HIS HIS B . n 
B 1 175 ASP 175 175 175 ASP ASP B . n 
B 1 176 ASN 176 176 176 ASN ASN B . n 
B 1 177 VAL 177 177 177 VAL VAL B . n 
B 1 178 ARG 178 178 178 ARG ARG B . n 
B 1 179 TRP 179 179 179 TRP TRP B . n 
B 1 180 ASP 180 180 180 ASP ASP B . n 
B 1 181 THR 181 181 181 THR THR B . n 
B 1 182 TRP 182 182 182 TRP TRP B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 ARG 184 184 184 ARG ARG B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 THR 186 186 186 THR THR B . n 
B 1 187 GLU 187 187 187 GLU GLU B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 SER 189 189 189 SER SER B . n 
B 1 190 VAL 190 190 190 VAL VAL B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 TYR 192 192 192 TYR TYR B . n 
B 1 193 GLN 193 193 193 GLN GLN B . n 
B 1 194 PRO 194 194 194 PRO PRO B . n 
B 1 195 TRP 195 195 195 TRP TRP B . n 
B 1 196 ILE 196 196 196 ILE ILE B . n 
B 1 197 TRP 197 197 197 TRP TRP B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 ALA 199 199 199 ALA ALA B . n 
B 1 200 GLY 200 200 200 GLY GLY B . n 
B 1 201 ASN 201 201 201 ASN ASN B . n 
B 1 202 HIS 202 202 202 HIS HIS B . n 
B 1 203 GLU 203 203 203 GLU GLU B . n 
B 1 204 ILE 204 204 204 ILE ILE B . n 
B 1 205 GLU 205 205 205 GLU GLU B . n 
B 1 206 PHE 206 206 206 PHE PHE B . n 
B 1 207 ALA 207 207 207 ALA ALA B . n 
B 1 208 PRO 208 208 208 PRO PRO B . n 
B 1 209 GLU 209 209 209 GLU GLU B . n 
B 1 210 ILE 210 210 210 ILE ILE B . n 
B 1 211 ASN 211 211 211 ASN ASN B . n 
B 1 212 GLU 212 212 212 GLU GLU B . n 
B 1 213 THR 213 213 213 THR THR B . n 
B 1 214 GLU 214 214 214 GLU GLU B . n 
B 1 215 PRO 215 215 215 PRO PRO B . n 
B 1 216 PHE 216 216 216 PHE PHE B . n 
B 1 217 LYS 217 217 217 LYS LYS B . n 
B 1 218 PRO 218 218 218 PRO PRO B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 SER 220 220 220 SER SER B . n 
B 1 221 TYR 221 221 221 TYR TYR B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 TYR 223 223 223 TYR TYR B . n 
B 1 224 HIS 224 224 224 HIS HIS B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 PRO 226 226 226 PRO PRO B . n 
B 1 227 TYR 227 227 227 TYR TYR B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 ALA 229 229 229 ALA ALA B . n 
B 1 230 SER 230 230 230 SER SER B . n 
B 1 231 GLN 231 231 231 GLN GLN B . n 
B 1 232 SER 232 232 232 SER SER B . n 
B 1 233 THR 233 233 233 THR THR B . n 
B 1 234 SER 234 234 234 SER SER B . n 
B 1 235 PRO 235 235 235 PRO PRO B . n 
B 1 236 PHE 236 236 236 PHE PHE B . n 
B 1 237 TRP 237 237 237 TRP TRP B . n 
B 1 238 TYR 238 238 238 TYR TYR B . n 
B 1 239 SER 239 239 239 SER SER B . n 
B 1 240 ILE 240 240 240 ILE ILE B . n 
B 1 241 LYS 241 241 241 LYS LYS B . n 
B 1 242 ARG 242 242 242 ARG ARG B . n 
B 1 243 ALA 243 243 243 ALA ALA B . n 
B 1 244 SER 244 244 244 SER SER B . n 
B 1 245 ALA 245 245 245 ALA ALA B . n 
B 1 246 HIS 246 246 246 HIS HIS B . n 
B 1 247 ILE 247 247 247 ILE ILE B . n 
B 1 248 ILE 248 248 248 ILE ILE B . n 
B 1 249 VAL 249 249 249 VAL VAL B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 SER 251 251 251 SER SER B . n 
B 1 252 SER 252 252 252 SER SER B . n 
B 1 253 TYR 253 253 253 TYR TYR B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 TYR 256 256 256 TYR TYR B . n 
B 1 257 GLY 257 257 257 GLY GLY B . n 
B 1 258 ARG 258 258 258 ARG ARG B . n 
B 1 259 GLY 259 259 259 GLY GLY B . n 
B 1 260 THR 260 260 260 THR THR B . n 
B 1 261 PRO 261 261 261 PRO PRO B . n 
B 1 262 GLN 262 262 262 GLN GLN B . n 
B 1 263 TYR 263 263 263 TYR TYR B . n 
B 1 264 THR 264 264 264 THR THR B . n 
B 1 265 TRP 265 265 265 TRP TRP B . n 
B 1 266 LEU 266 266 266 LEU LEU B . n 
B 1 267 LYS 267 267 267 LYS LYS B . n 
B 1 268 LYS 268 268 268 LYS LYS B . n 
B 1 269 GLU 269 269 269 GLU GLU B . n 
B 1 270 LEU 270 270 270 LEU LEU B . n 
B 1 271 ARG 271 271 271 ARG ARG B . n 
B 1 272 LYS 272 272 272 LYS LYS B . n 
B 1 273 VAL 273 273 273 VAL VAL B . n 
B 1 274 LYS 274 274 274 LYS LYS B . n 
B 1 275 ARG 275 275 275 ARG ARG B . n 
B 1 276 SER 276 276 276 SER SER B . n 
B 1 277 GLU 277 277 277 GLU GLU B . n 
B 1 278 THR 278 278 278 THR THR B . n 
B 1 279 PRO 279 279 279 PRO PRO B . n 
B 1 280 TRP 280 280 280 TRP TRP B . n 
B 1 281 LEU 281 281 281 LEU LEU B . n 
B 1 282 ILE 282 282 282 ILE ILE B . n 
B 1 283 VAL 283 283 283 VAL VAL B . n 
B 1 284 LEU 284 284 284 LEU LEU B . n 
B 1 285 MET 285 285 285 MET MET B . n 
B 1 286 HIS 286 286 286 HIS HIS B . n 
B 1 287 SER 287 287 287 SER SER B . n 
B 1 288 PRO 288 288 288 PRO PRO B . n 
B 1 289 LEU 289 289 289 LEU LEU B . n 
B 1 290 TYR 290 290 290 TYR TYR B . n 
B 1 291 ASN 291 291 291 ASN ASN B . n 
B 1 292 SER 292 292 292 SER SER B . n 
B 1 293 TYR 293 293 293 TYR TYR B . n 
B 1 294 ASN 294 294 294 ASN ASN B . n 
B 1 295 HIS 295 295 295 HIS HIS B . n 
B 1 296 HIS 296 296 296 HIS HIS B . n 
B 1 297 PHE 297 297 297 PHE PHE B . n 
B 1 298 MET 298 298 298 MET MET B . n 
B 1 299 GLU 299 299 299 GLU GLU B . n 
B 1 300 GLY 300 300 300 GLY GLY B . n 
B 1 301 GLU 301 301 301 GLU GLU B . n 
B 1 302 ALA 302 302 302 ALA ALA B . n 
B 1 303 MET 303 303 303 MET MET B . n 
B 1 304 ARG 304 304 304 ARG ARG B . n 
B 1 305 THR 305 305 305 THR THR B . n 
B 1 306 LYS 306 306 306 LYS LYS B . n 
B 1 307 PHE 307 307 307 PHE PHE B . n 
B 1 308 GLU 308 308 308 GLU GLU B . n 
B 1 309 ALA 309 309 309 ALA ALA B . n 
B 1 310 TRP 310 310 310 TRP TRP B . n 
B 1 311 PHE 311 311 311 PHE PHE B . n 
B 1 312 VAL 312 312 312 VAL VAL B . n 
B 1 313 LYS 313 313 313 LYS LYS B . n 
B 1 314 TYR 314 314 314 TYR TYR B . n 
B 1 315 LYS 315 315 315 LYS LYS B . n 
B 1 316 VAL 316 316 316 VAL VAL B . n 
B 1 317 ASP 317 317 317 ASP ASP B . n 
B 1 318 VAL 318 318 318 VAL VAL B . n 
B 1 319 VAL 319 319 319 VAL VAL B . n 
B 1 320 PHE 320 320 320 PHE PHE B . n 
B 1 321 ALA 321 321 321 ALA ALA B . n 
B 1 322 GLY 322 322 322 GLY GLY B . n 
B 1 323 HIS 323 323 323 HIS HIS B . n 
B 1 324 VAL 324 324 324 VAL VAL B . n 
B 1 325 HIS 325 325 325 HIS HIS B . n 
B 1 326 ALA 326 326 326 ALA ALA B . n 
B 1 327 TYR 327 327 327 TYR TYR B . n 
B 1 328 GLU 328 328 328 GLU GLU B . n 
B 1 329 ARG 329 329 329 ARG ARG B . n 
B 1 330 SER 330 330 330 SER SER B . n 
B 1 331 GLU 331 331 331 GLU GLU B . n 
B 1 332 ARG 332 332 332 ARG ARG B . n 
B 1 333 VAL 333 333 333 VAL VAL B . n 
B 1 334 SER 334 334 334 SER SER B . n 
B 1 335 ASN 335 335 335 ASN ASN B . n 
B 1 336 ILE 336 336 336 ILE ILE B . n 
B 1 337 ALA 337 337 337 ALA ALA B . n 
B 1 338 TYR 338 338 338 TYR TYR B . n 
B 1 339 LYS 339 339 339 LYS LYS B . n 
B 1 340 ILE 340 340 340 ILE ILE B . n 
B 1 341 THR 341 341 341 THR THR B . n 
B 1 342 ASP 342 342 342 ASP ASP B . n 
B 1 343 GLY 343 343 343 GLY GLY B . n 
B 1 344 LEU 344 344 344 LEU LEU B . n 
B 1 345 CYS 345 345 345 CYS CYS B . n 
B 1 346 THR 346 346 346 THR THR B . n 
B 1 347 PRO 347 347 347 PRO PRO B . n 
B 1 348 VAL 348 348 348 VAL VAL B . n 
B 1 349 LYS 349 349 349 LYS LYS B . n 
B 1 350 ASP 350 350 350 ASP ASP B . n 
B 1 351 GLN 351 351 351 GLN GLN B . n 
B 1 352 SER 352 352 352 SER SER B . n 
B 1 353 ALA 353 353 353 ALA ALA B . n 
B 1 354 PRO 354 354 354 PRO PRO B . n 
B 1 355 VAL 355 355 355 VAL VAL B . n 
B 1 356 TYR 356 356 356 TYR TYR B . n 
B 1 357 ILE 357 357 357 ILE ILE B . n 
B 1 358 THR 358 358 358 THR THR B . n 
B 1 359 ILE 359 359 359 ILE ILE B . n 
B 1 360 GLY 360 360 360 GLY GLY B . n 
B 1 361 ASP 361 361 361 ASP ASP B . n 
B 1 362 ALA 362 362 362 ALA ALA B . n 
B 1 363 GLY 363 363 363 GLY GLY B . n 
B 1 364 ASN 364 364 364 ASN ASN B . n 
B 1 365 TYR 365 365 365 TYR TYR B . n 
B 1 366 GLY 366 366 366 GLY GLY B . n 
B 1 367 VAL 367 367 367 VAL VAL B . n 
B 1 368 ILE 368 368 368 ILE ILE B . n 
B 1 369 ASP 369 369 369 ASP ASP B . n 
B 1 370 SER 370 370 370 SER SER B . n 
B 1 371 ASN 371 371 371 ASN ASN B . n 
B 1 372 MET 372 372 372 MET MET B . n 
B 1 373 ILE 373 373 373 ILE ILE B . n 
B 1 374 GLN 374 374 374 GLN GLN B . n 
B 1 375 PRO 375 375 375 PRO PRO B . n 
B 1 376 GLN 376 376 376 GLN GLN B . n 
B 1 377 PRO 377 377 377 PRO PRO B . n 
B 1 378 GLU 378 378 378 GLU GLU B . n 
B 1 379 TYR 379 379 379 TYR TYR B . n 
B 1 380 SER 380 380 380 SER SER B . n 
B 1 381 ALA 381 381 381 ALA ALA B . n 
B 1 382 PHE 382 382 382 PHE PHE B . n 
B 1 383 ARG 383 383 383 ARG ARG B . n 
B 1 384 GLU 384 384 384 GLU GLU B . n 
B 1 385 ALA 385 385 385 ALA ALA B . n 
B 1 386 SER 386 386 386 SER SER B . n 
B 1 387 PHE 387 387 387 PHE PHE B . n 
B 1 388 GLY 388 388 388 GLY GLY B . n 
B 1 389 HIS 389 389 389 HIS HIS B . n 
B 1 390 GLY 390 390 390 GLY GLY B . n 
B 1 391 MET 391 391 391 MET MET B . n 
B 1 392 PHE 392 392 392 PHE PHE B . n 
B 1 393 ASP 393 393 393 ASP ASP B . n 
B 1 394 ILE 394 394 394 ILE ILE B . n 
B 1 395 LYS 395 395 395 LYS LYS B . n 
B 1 396 ASN 396 396 396 ASN ASN B . n 
B 1 397 ARG 397 397 397 ARG ARG B . n 
B 1 398 THR 398 398 398 THR THR B . n 
B 1 399 HIS 399 399 399 HIS HIS B . n 
B 1 400 ALA 400 400 400 ALA ALA B . n 
B 1 401 HIS 401 401 401 HIS HIS B . n 
B 1 402 PHE 402 402 402 PHE PHE B . n 
B 1 403 SER 403 403 403 SER SER B . n 
B 1 404 TRP 404 404 404 TRP TRP B . n 
B 1 405 ASN 405 405 405 ASN ASN B . n 
B 1 406 ARG 406 406 406 ARG ARG B . n 
B 1 407 ASN 407 407 407 ASN ASN B . n 
B 1 408 GLN 408 408 408 GLN GLN B . n 
B 1 409 ASP 409 409 409 ASP ASP B . n 
B 1 410 GLY 410 410 410 GLY GLY B . n 
B 1 411 VAL 411 411 411 VAL VAL B . n 
B 1 412 ALA 412 412 412 ALA ALA B . n 
B 1 413 VAL 413 413 413 VAL VAL B . n 
B 1 414 GLU 414 414 414 GLU GLU B . n 
B 1 415 ALA 415 415 415 ALA ALA B . n 
B 1 416 ASP 416 416 416 ASP ASP B . n 
B 1 417 SER 417 417 417 SER SER B . n 
B 1 418 VAL 418 418 418 VAL VAL B . n 
B 1 419 TRP 419 419 419 TRP TRP B . n 
B 1 420 PHE 420 420 420 PHE PHE B . n 
B 1 421 PHE 421 421 421 PHE PHE B . n 
B 1 422 ASN 422 422 422 ASN ASN B . n 
B 1 423 ARG 423 423 423 ARG ARG B . n 
B 1 424 HIS 424 424 424 HIS HIS B . n 
B 1 425 TRP 425 425 425 TRP TRP B . n 
B 1 426 TYR 426 426 426 TYR TYR B . n 
B 1 427 PRO 427 427 427 PRO PRO B . n 
B 1 428 VAL 428 428 428 VAL VAL B . n 
B 1 429 ASP 429 429 429 ASP ASP B . n 
B 1 430 ASP 430 430 430 ASP ASP B . n 
B 1 431 SER 431 431 431 SER SER B . n 
B 1 432 THR 432 432 432 THR THR B . n 
C 1 1   PHE 1   1   ?   ?   ?   C . n 
C 1 2   VAL 2   2   ?   ?   ?   C . n 
C 1 3   ARG 3   3   ?   ?   ?   C . n 
C 1 4   LYS 4   4   ?   ?   ?   C . n 
C 1 5   THR 5   5   ?   ?   ?   C . n 
C 1 6   ASN 6   6   ?   ?   ?   C . n 
C 1 7   LYS 7   7   ?   ?   ?   C . n 
C 1 8   ASN 8   8   ?   ?   ?   C . n 
C 1 9   ARG 9   9   9   ARG ARG C . n 
C 1 10  ASP 10  10  10  ASP ASP C . n 
C 1 11  MET 11  11  11  MET MET C . n 
C 1 12  PRO 12  12  12  PRO PRO C . n 
C 1 13  LEU 13  13  13  LEU LEU C . n 
C 1 14  ASP 14  14  14  ASP ASP C . n 
C 1 15  SER 15  15  15  SER SER C . n 
C 1 16  ASP 16  16  16  ASP ASP C . n 
C 1 17  VAL 17  17  17  VAL VAL C . n 
C 1 18  PHE 18  18  18  PHE PHE C . n 
C 1 19  ARG 19  19  19  ARG ARG C . n 
C 1 20  VAL 20  20  20  VAL VAL C . n 
C 1 21  PRO 21  21  21  PRO PRO C . n 
C 1 22  PRO 22  22  22  PRO PRO C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  TYR 24  24  24  TYR TYR C . n 
C 1 25  ASN 25  25  25  ASN ASN C . n 
C 1 26  ALA 26  26  26  ALA ALA C . n 
C 1 27  PRO 27  27  27  PRO PRO C . n 
C 1 28  GLN 28  28  28  GLN GLN C . n 
C 1 29  GLN 29  29  29  GLN GLN C . n 
C 1 30  VAL 30  30  30  VAL VAL C . n 
C 1 31  HIS 31  31  31  HIS HIS C . n 
C 1 32  ILE 32  32  32  ILE ILE C . n 
C 1 33  THR 33  33  33  THR THR C . n 
C 1 34  GLN 34  34  34  GLN GLN C . n 
C 1 35  GLY 35  35  35  GLY GLY C . n 
C 1 36  ASP 36  36  36  ASP ASP C . n 
C 1 37  LEU 37  37  37  LEU LEU C . n 
C 1 38  VAL 38  38  38  VAL VAL C . n 
C 1 39  GLY 39  39  39  GLY GLY C . n 
C 1 40  ARG 40  40  40  ARG ARG C . n 
C 1 41  ALA 41  41  41  ALA ALA C . n 
C 1 42  MET 42  42  42  MET MET C . n 
C 1 43  ILE 43  43  43  ILE ILE C . n 
C 1 44  ILE 44  44  44  ILE ILE C . n 
C 1 45  SER 45  45  45  SER SER C . n 
C 1 46  TRP 46  46  46  TRP TRP C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  THR 48  48  48  THR THR C . n 
C 1 49  MET 49  49  49  MET MET C . n 
C 1 50  ASP 50  50  50  ASP ASP C . n 
C 1 51  GLU 51  51  51  GLU GLU C . n 
C 1 52  PRO 52  52  52  PRO PRO C . n 
C 1 53  GLY 53  53  53  GLY GLY C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  SER 55  55  55  SER SER C . n 
C 1 56  ALA 56  56  56  ALA ALA C . n 
C 1 57  VAL 57  57  57  VAL VAL C . n 
C 1 58  ARG 58  58  58  ARG ARG C . n 
C 1 59  TYR 59  59  59  TYR TYR C . n 
C 1 60  TRP 60  60  60  TRP TRP C . n 
C 1 61  SER 61  61  61  SER SER C . n 
C 1 62  GLU 62  62  62  GLU GLU C . n 
C 1 63  LYS 63  63  63  LYS LYS C . n 
C 1 64  ASN 64  64  64  ASN ASN C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  ARG 66  66  66  ARG ARG C . n 
C 1 67  LYS 67  67  67  LYS LYS C . n 
C 1 68  ARG 68  68  68  ARG ARG C . n 
C 1 69  ILE 69  69  69  ILE ILE C . n 
C 1 70  ALA 70  70  70  ALA ALA C . n 
C 1 71  LYS 71  71  71  LYS LYS C . n 
C 1 72  GLY 72  72  72  GLY GLY C . n 
C 1 73  LYS 73  73  73  LYS LYS C . n 
C 1 74  MET 74  74  74  MET MET C . n 
C 1 75  SER 75  75  75  SER SER C . n 
C 1 76  THR 76  76  76  THR THR C . n 
C 1 77  TYR 77  77  77  TYR TYR C . n 
C 1 78  ARG 78  78  78  ARG ARG C . n 
C 1 79  PHE 79  79  79  PHE PHE C . n 
C 1 80  PHE 80  80  80  PHE PHE C . n 
C 1 81  ASN 81  81  81  ASN ASN C . n 
C 1 82  TYR 82  82  82  TYR TYR C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  SER 84  84  84  SER SER C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  PHE 86  86  86  PHE PHE C . n 
C 1 87  ILE 87  87  87  ILE ILE C . n 
C 1 88  HIS 88  88  88  HIS HIS C . n 
C 1 89  HIS 89  89  89  HIS HIS C . n 
C 1 90  THR 90  90  90  THR THR C . n 
C 1 91  THR 91  91  91  THR THR C . n 
C 1 92  ILE 92  92  92  ILE ILE C . n 
C 1 93  ARG 93  93  93  ARG ARG C . n 
C 1 94  LYS 94  94  94  LYS LYS C . n 
C 1 95  LEU 95  95  95  LEU LEU C . n 
C 1 96  LYS 96  96  96  LYS LYS C . n 
C 1 97  TYR 97  97  97  TYR TYR C . n 
C 1 98  ASN 98  98  98  ASN ASN C . n 
C 1 99  THR 99  99  99  THR THR C . n 
C 1 100 LYS 100 100 100 LYS LYS C . n 
C 1 101 TYR 101 101 101 TYR TYR C . n 
C 1 102 TYR 102 102 102 TYR TYR C . n 
C 1 103 TYR 103 103 103 TYR TYR C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 VAL 105 105 105 VAL VAL C . n 
C 1 106 GLY 106 106 106 GLY GLY C . n 
C 1 107 LEU 107 107 107 LEU LEU C . n 
C 1 108 ARG 108 108 108 ARG ARG C . n 
C 1 109 ASN 109 109 109 ASN ASN C . n 
C 1 110 THR 110 110 110 THR THR C . n 
C 1 111 THR 111 111 111 THR THR C . n 
C 1 112 ARG 112 112 112 ARG ARG C . n 
C 1 113 ARG 113 113 113 ARG ARG C . n 
C 1 114 PHE 114 114 114 PHE PHE C . n 
C 1 115 SER 115 115 115 SER SER C . n 
C 1 116 PHE 116 116 116 PHE PHE C . n 
C 1 117 ILE 117 117 117 ILE ILE C . n 
C 1 118 THR 118 118 118 THR THR C . n 
C 1 119 PRO 119 119 119 PRO PRO C . n 
C 1 120 PRO 120 120 120 PRO PRO C . n 
C 1 121 GLN 121 121 121 GLN GLN C . n 
C 1 122 THR 122 122 122 THR THR C . n 
C 1 123 GLY 123 123 123 GLY GLY C . n 
C 1 124 LEU 124 124 124 LEU LEU C . n 
C 1 125 ASP 125 125 125 ASP ASP C . n 
C 1 126 VAL 126 126 126 VAL VAL C . n 
C 1 127 PRO 127 127 127 PRO PRO C . n 
C 1 128 TYR 128 128 128 TYR TYR C . n 
C 1 129 THR 129 129 129 THR THR C . n 
C 1 130 PHE 130 130 130 PHE PHE C . n 
C 1 131 GLY 131 131 131 GLY GLY C . n 
C 1 132 LEU 132 132 132 LEU LEU C . n 
C 1 133 ILE 133 133 133 ILE ILE C . n 
C 1 134 GLY 134 134 134 GLY GLY C . n 
C 1 135 ASP 135 135 135 ASP ASP C . n 
C 1 136 LEU 136 136 136 LEU LEU C . n 
C 1 137 GLY 137 137 137 GLY GLY C . n 
C 1 138 GLN 138 138 138 GLN GLN C . n 
C 1 139 SER 139 139 139 SER SER C . n 
C 1 140 PHE 140 140 140 PHE PHE C . n 
C 1 141 ASP 141 141 141 ASP ASP C . n 
C 1 142 SER 142 142 142 SER SER C . n 
C 1 143 ASN 143 143 143 ASN ASN C . n 
C 1 144 THR 144 144 144 THR THR C . n 
C 1 145 THR 145 145 145 THR THR C . n 
C 1 146 LEU 146 146 146 LEU LEU C . n 
C 1 147 SER 147 147 147 SER SER C . n 
C 1 148 HIS 148 148 148 HIS HIS C . n 
C 1 149 TYR 149 149 149 TYR TYR C . n 
C 1 150 GLU 150 150 150 GLU GLU C . n 
C 1 151 LEU 151 151 151 LEU LEU C . n 
C 1 152 SER 152 152 152 SER SER C . n 
C 1 153 PRO 153 153 153 PRO PRO C . n 
C 1 154 LYS 154 154 154 LYS LYS C . n 
C 1 155 LYS 155 155 155 LYS LYS C . n 
C 1 156 GLY 156 156 156 GLY GLY C . n 
C 1 157 GLN 157 157 157 GLN GLN C . n 
C 1 158 THR 158 158 158 THR THR C . n 
C 1 159 VAL 159 159 159 VAL VAL C . n 
C 1 160 LEU 160 160 160 LEU LEU C . n 
C 1 161 PHE 161 161 161 PHE PHE C . n 
C 1 162 VAL 162 162 162 VAL VAL C . n 
C 1 163 GLY 163 163 163 GLY GLY C . n 
C 1 164 ASP 164 164 164 ASP ASP C . n 
C 1 165 LEU 165 165 165 LEU LEU C . n 
C 1 166 SER 166 166 166 SER SER C . n 
C 1 167 TYR 167 167 167 TYR TYR C . n 
C 1 168 ALA 168 168 168 ALA ALA C . n 
C 1 169 ASP 169 169 169 ASP ASP C . n 
C 1 170 ARG 170 170 170 ARG ARG C . n 
C 1 171 TYR 171 171 171 TYR TYR C . n 
C 1 172 PRO 172 172 172 PRO PRO C . n 
C 1 173 ASN 173 173 173 ASN ASN C . n 
C 1 174 HIS 174 174 174 HIS HIS C . n 
C 1 175 ASP 175 175 175 ASP ASP C . n 
C 1 176 ASN 176 176 176 ASN ASN C . n 
C 1 177 VAL 177 177 177 VAL VAL C . n 
C 1 178 ARG 178 178 178 ARG ARG C . n 
C 1 179 TRP 179 179 179 TRP TRP C . n 
C 1 180 ASP 180 180 180 ASP ASP C . n 
C 1 181 THR 181 181 181 THR THR C . n 
C 1 182 TRP 182 182 182 TRP TRP C . n 
C 1 183 GLY 183 183 183 GLY GLY C . n 
C 1 184 ARG 184 184 184 ARG ARG C . n 
C 1 185 PHE 185 185 185 PHE PHE C . n 
C 1 186 THR 186 186 186 THR THR C . n 
C 1 187 GLU 187 187 187 GLU GLU C . n 
C 1 188 ARG 188 188 188 ARG ARG C . n 
C 1 189 SER 189 189 189 SER SER C . n 
C 1 190 VAL 190 190 190 VAL VAL C . n 
C 1 191 ALA 191 191 191 ALA ALA C . n 
C 1 192 TYR 192 192 192 TYR TYR C . n 
C 1 193 GLN 193 193 193 GLN GLN C . n 
C 1 194 PRO 194 194 194 PRO PRO C . n 
C 1 195 TRP 195 195 195 TRP TRP C . n 
C 1 196 ILE 196 196 196 ILE ILE C . n 
C 1 197 TRP 197 197 197 TRP TRP C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 ALA 199 199 199 ALA ALA C . n 
C 1 200 GLY 200 200 200 GLY GLY C . n 
C 1 201 ASN 201 201 201 ASN ASN C . n 
C 1 202 HIS 202 202 202 HIS HIS C . n 
C 1 203 GLU 203 203 203 GLU GLU C . n 
C 1 204 ILE 204 204 204 ILE ILE C . n 
C 1 205 GLU 205 205 205 GLU GLU C . n 
C 1 206 PHE 206 206 206 PHE PHE C . n 
C 1 207 ALA 207 207 207 ALA ALA C . n 
C 1 208 PRO 208 208 208 PRO PRO C . n 
C 1 209 GLU 209 209 209 GLU GLU C . n 
C 1 210 ILE 210 210 210 ILE ILE C . n 
C 1 211 ASN 211 211 211 ASN ASN C . n 
C 1 212 GLU 212 212 212 GLU GLU C . n 
C 1 213 THR 213 213 213 THR THR C . n 
C 1 214 GLU 214 214 214 GLU GLU C . n 
C 1 215 PRO 215 215 215 PRO PRO C . n 
C 1 216 PHE 216 216 216 PHE PHE C . n 
C 1 217 LYS 217 217 217 LYS LYS C . n 
C 1 218 PRO 218 218 218 PRO PRO C . n 
C 1 219 PHE 219 219 219 PHE PHE C . n 
C 1 220 SER 220 220 220 SER SER C . n 
C 1 221 TYR 221 221 221 TYR TYR C . n 
C 1 222 ARG 222 222 222 ARG ARG C . n 
C 1 223 TYR 223 223 223 TYR TYR C . n 
C 1 224 HIS 224 224 224 HIS HIS C . n 
C 1 225 VAL 225 225 225 VAL VAL C . n 
C 1 226 PRO 226 226 226 PRO PRO C . n 
C 1 227 TYR 227 227 227 TYR TYR C . n 
C 1 228 GLU 228 228 228 GLU GLU C . n 
C 1 229 ALA 229 229 229 ALA ALA C . n 
C 1 230 SER 230 230 230 SER SER C . n 
C 1 231 GLN 231 231 231 GLN GLN C . n 
C 1 232 SER 232 232 232 SER SER C . n 
C 1 233 THR 233 233 233 THR THR C . n 
C 1 234 SER 234 234 234 SER SER C . n 
C 1 235 PRO 235 235 235 PRO PRO C . n 
C 1 236 PHE 236 236 236 PHE PHE C . n 
C 1 237 TRP 237 237 237 TRP TRP C . n 
C 1 238 TYR 238 238 238 TYR TYR C . n 
C 1 239 SER 239 239 239 SER SER C . n 
C 1 240 ILE 240 240 240 ILE ILE C . n 
C 1 241 LYS 241 241 241 LYS LYS C . n 
C 1 242 ARG 242 242 242 ARG ARG C . n 
C 1 243 ALA 243 243 243 ALA ALA C . n 
C 1 244 SER 244 244 244 SER SER C . n 
C 1 245 ALA 245 245 245 ALA ALA C . n 
C 1 246 HIS 246 246 246 HIS HIS C . n 
C 1 247 ILE 247 247 247 ILE ILE C . n 
C 1 248 ILE 248 248 248 ILE ILE C . n 
C 1 249 VAL 249 249 249 VAL VAL C . n 
C 1 250 LEU 250 250 250 LEU LEU C . n 
C 1 251 SER 251 251 251 SER SER C . n 
C 1 252 SER 252 252 252 SER SER C . n 
C 1 253 TYR 253 253 253 TYR TYR C . n 
C 1 254 SER 254 254 254 SER SER C . n 
C 1 255 ALA 255 255 255 ALA ALA C . n 
C 1 256 TYR 256 256 256 TYR TYR C . n 
C 1 257 GLY 257 257 257 GLY GLY C . n 
C 1 258 ARG 258 258 258 ARG ARG C . n 
C 1 259 GLY 259 259 259 GLY GLY C . n 
C 1 260 THR 260 260 260 THR THR C . n 
C 1 261 PRO 261 261 261 PRO PRO C . n 
C 1 262 GLN 262 262 262 GLN GLN C . n 
C 1 263 TYR 263 263 263 TYR TYR C . n 
C 1 264 THR 264 264 264 THR THR C . n 
C 1 265 TRP 265 265 265 TRP TRP C . n 
C 1 266 LEU 266 266 266 LEU LEU C . n 
C 1 267 LYS 267 267 267 LYS LYS C . n 
C 1 268 LYS 268 268 268 LYS LYS C . n 
C 1 269 GLU 269 269 269 GLU GLU C . n 
C 1 270 LEU 270 270 270 LEU LEU C . n 
C 1 271 ARG 271 271 271 ARG ARG C . n 
C 1 272 LYS 272 272 272 LYS LYS C . n 
C 1 273 VAL 273 273 273 VAL VAL C . n 
C 1 274 LYS 274 274 274 LYS LYS C . n 
C 1 275 ARG 275 275 275 ARG ARG C . n 
C 1 276 SER 276 276 276 SER SER C . n 
C 1 277 GLU 277 277 277 GLU GLU C . n 
C 1 278 THR 278 278 278 THR THR C . n 
C 1 279 PRO 279 279 279 PRO PRO C . n 
C 1 280 TRP 280 280 280 TRP TRP C . n 
C 1 281 LEU 281 281 281 LEU LEU C . n 
C 1 282 ILE 282 282 282 ILE ILE C . n 
C 1 283 VAL 283 283 283 VAL VAL C . n 
C 1 284 LEU 284 284 284 LEU LEU C . n 
C 1 285 MET 285 285 285 MET MET C . n 
C 1 286 HIS 286 286 286 HIS HIS C . n 
C 1 287 SER 287 287 287 SER SER C . n 
C 1 288 PRO 288 288 288 PRO PRO C . n 
C 1 289 LEU 289 289 289 LEU LEU C . n 
C 1 290 TYR 290 290 290 TYR TYR C . n 
C 1 291 ASN 291 291 291 ASN ASN C . n 
C 1 292 SER 292 292 292 SER SER C . n 
C 1 293 TYR 293 293 293 TYR TYR C . n 
C 1 294 ASN 294 294 294 ASN ASN C . n 
C 1 295 HIS 295 295 295 HIS HIS C . n 
C 1 296 HIS 296 296 296 HIS HIS C . n 
C 1 297 PHE 297 297 297 PHE PHE C . n 
C 1 298 MET 298 298 298 MET MET C . n 
C 1 299 GLU 299 299 299 GLU GLU C . n 
C 1 300 GLY 300 300 300 GLY GLY C . n 
C 1 301 GLU 301 301 301 GLU GLU C . n 
C 1 302 ALA 302 302 302 ALA ALA C . n 
C 1 303 MET 303 303 303 MET MET C . n 
C 1 304 ARG 304 304 304 ARG ARG C . n 
C 1 305 THR 305 305 305 THR THR C . n 
C 1 306 LYS 306 306 306 LYS LYS C . n 
C 1 307 PHE 307 307 307 PHE PHE C . n 
C 1 308 GLU 308 308 308 GLU GLU C . n 
C 1 309 ALA 309 309 309 ALA ALA C . n 
C 1 310 TRP 310 310 310 TRP TRP C . n 
C 1 311 PHE 311 311 311 PHE PHE C . n 
C 1 312 VAL 312 312 312 VAL VAL C . n 
C 1 313 LYS 313 313 313 LYS LYS C . n 
C 1 314 TYR 314 314 314 TYR TYR C . n 
C 1 315 LYS 315 315 315 LYS LYS C . n 
C 1 316 VAL 316 316 316 VAL VAL C . n 
C 1 317 ASP 317 317 317 ASP ASP C . n 
C 1 318 VAL 318 318 318 VAL VAL C . n 
C 1 319 VAL 319 319 319 VAL VAL C . n 
C 1 320 PHE 320 320 320 PHE PHE C . n 
C 1 321 ALA 321 321 321 ALA ALA C . n 
C 1 322 GLY 322 322 322 GLY GLY C . n 
C 1 323 HIS 323 323 323 HIS HIS C . n 
C 1 324 VAL 324 324 324 VAL VAL C . n 
C 1 325 HIS 325 325 325 HIS HIS C . n 
C 1 326 ALA 326 326 326 ALA ALA C . n 
C 1 327 TYR 327 327 327 TYR TYR C . n 
C 1 328 GLU 328 328 328 GLU GLU C . n 
C 1 329 ARG 329 329 329 ARG ARG C . n 
C 1 330 SER 330 330 330 SER SER C . n 
C 1 331 GLU 331 331 331 GLU GLU C . n 
C 1 332 ARG 332 332 332 ARG ARG C . n 
C 1 333 VAL 333 333 333 VAL VAL C . n 
C 1 334 SER 334 334 334 SER SER C . n 
C 1 335 ASN 335 335 335 ASN ASN C . n 
C 1 336 ILE 336 336 336 ILE ILE C . n 
C 1 337 ALA 337 337 337 ALA ALA C . n 
C 1 338 TYR 338 338 338 TYR TYR C . n 
C 1 339 LYS 339 339 339 LYS LYS C . n 
C 1 340 ILE 340 340 340 ILE ILE C . n 
C 1 341 THR 341 341 341 THR THR C . n 
C 1 342 ASP 342 342 342 ASP ASP C . n 
C 1 343 GLY 343 343 343 GLY GLY C . n 
C 1 344 LEU 344 344 344 LEU LEU C . n 
C 1 345 CYS 345 345 345 CYS CYS C . n 
C 1 346 THR 346 346 346 THR THR C . n 
C 1 347 PRO 347 347 347 PRO PRO C . n 
C 1 348 VAL 348 348 348 VAL VAL C . n 
C 1 349 LYS 349 349 349 LYS LYS C . n 
C 1 350 ASP 350 350 350 ASP ASP C . n 
C 1 351 GLN 351 351 351 GLN GLN C . n 
C 1 352 SER 352 352 352 SER SER C . n 
C 1 353 ALA 353 353 353 ALA ALA C . n 
C 1 354 PRO 354 354 354 PRO PRO C . n 
C 1 355 VAL 355 355 355 VAL VAL C . n 
C 1 356 TYR 356 356 356 TYR TYR C . n 
C 1 357 ILE 357 357 357 ILE ILE C . n 
C 1 358 THR 358 358 358 THR THR C . n 
C 1 359 ILE 359 359 359 ILE ILE C . n 
C 1 360 GLY 360 360 360 GLY GLY C . n 
C 1 361 ASP 361 361 361 ASP ASP C . n 
C 1 362 ALA 362 362 362 ALA ALA C . n 
C 1 363 GLY 363 363 363 GLY GLY C . n 
C 1 364 ASN 364 364 364 ASN ASN C . n 
C 1 365 TYR 365 365 365 TYR TYR C . n 
C 1 366 GLY 366 366 366 GLY GLY C . n 
C 1 367 VAL 367 367 367 VAL VAL C . n 
C 1 368 ILE 368 368 368 ILE ILE C . n 
C 1 369 ASP 369 369 369 ASP ASP C . n 
C 1 370 SER 370 370 370 SER SER C . n 
C 1 371 ASN 371 371 371 ASN ASN C . n 
C 1 372 MET 372 372 372 MET MET C . n 
C 1 373 ILE 373 373 373 ILE ILE C . n 
C 1 374 GLN 374 374 374 GLN GLN C . n 
C 1 375 PRO 375 375 375 PRO PRO C . n 
C 1 376 GLN 376 376 376 GLN GLN C . n 
C 1 377 PRO 377 377 377 PRO PRO C . n 
C 1 378 GLU 378 378 378 GLU GLU C . n 
C 1 379 TYR 379 379 379 TYR TYR C . n 
C 1 380 SER 380 380 380 SER SER C . n 
C 1 381 ALA 381 381 381 ALA ALA C . n 
C 1 382 PHE 382 382 382 PHE PHE C . n 
C 1 383 ARG 383 383 383 ARG ARG C . n 
C 1 384 GLU 384 384 384 GLU GLU C . n 
C 1 385 ALA 385 385 385 ALA ALA C . n 
C 1 386 SER 386 386 386 SER SER C . n 
C 1 387 PHE 387 387 387 PHE PHE C . n 
C 1 388 GLY 388 388 388 GLY GLY C . n 
C 1 389 HIS 389 389 389 HIS HIS C . n 
C 1 390 GLY 390 390 390 GLY GLY C . n 
C 1 391 MET 391 391 391 MET MET C . n 
C 1 392 PHE 392 392 392 PHE PHE C . n 
C 1 393 ASP 393 393 393 ASP ASP C . n 
C 1 394 ILE 394 394 394 ILE ILE C . n 
C 1 395 LYS 395 395 395 LYS LYS C . n 
C 1 396 ASN 396 396 396 ASN ASN C . n 
C 1 397 ARG 397 397 397 ARG ARG C . n 
C 1 398 THR 398 398 398 THR THR C . n 
C 1 399 HIS 399 399 399 HIS HIS C . n 
C 1 400 ALA 400 400 400 ALA ALA C . n 
C 1 401 HIS 401 401 401 HIS HIS C . n 
C 1 402 PHE 402 402 402 PHE PHE C . n 
C 1 403 SER 403 403 403 SER SER C . n 
C 1 404 TRP 404 404 404 TRP TRP C . n 
C 1 405 ASN 405 405 405 ASN ASN C . n 
C 1 406 ARG 406 406 406 ARG ARG C . n 
C 1 407 ASN 407 407 407 ASN ASN C . n 
C 1 408 GLN 408 408 408 GLN GLN C . n 
C 1 409 ASP 409 409 409 ASP ASP C . n 
C 1 410 GLY 410 410 410 GLY GLY C . n 
C 1 411 VAL 411 411 411 VAL VAL C . n 
C 1 412 ALA 412 412 412 ALA ALA C . n 
C 1 413 VAL 413 413 413 VAL VAL C . n 
C 1 414 GLU 414 414 414 GLU GLU C . n 
C 1 415 ALA 415 415 415 ALA ALA C . n 
C 1 416 ASP 416 416 416 ASP ASP C . n 
C 1 417 SER 417 417 417 SER SER C . n 
C 1 418 VAL 418 418 418 VAL VAL C . n 
C 1 419 TRP 419 419 419 TRP TRP C . n 
C 1 420 PHE 420 420 420 PHE PHE C . n 
C 1 421 PHE 421 421 421 PHE PHE C . n 
C 1 422 ASN 422 422 422 ASN ASN C . n 
C 1 423 ARG 423 423 423 ARG ARG C . n 
C 1 424 HIS 424 424 424 HIS HIS C . n 
C 1 425 TRP 425 425 425 TRP TRP C . n 
C 1 426 TYR 426 426 426 TYR TYR C . n 
C 1 427 PRO 427 427 427 PRO PRO C . n 
C 1 428 VAL 428 428 428 VAL VAL C . n 
C 1 429 ASP 429 429 429 ASP ASP C . n 
C 1 430 ASP 430 430 430 ASP ASP C . n 
C 1 431 SER 431 431 431 SER SER C . n 
C 1 432 THR 432 432 432 THR THR C . n 
D 1 1   PHE 1   1   ?   ?   ?   D . n 
D 1 2   VAL 2   2   ?   ?   ?   D . n 
D 1 3   ARG 3   3   ?   ?   ?   D . n 
D 1 4   LYS 4   4   ?   ?   ?   D . n 
D 1 5   THR 5   5   ?   ?   ?   D . n 
D 1 6   ASN 6   6   ?   ?   ?   D . n 
D 1 7   LYS 7   7   ?   ?   ?   D . n 
D 1 8   ASN 8   8   ?   ?   ?   D . n 
D 1 9   ARG 9   9   9   ARG ARG D . n 
D 1 10  ASP 10  10  10  ASP ASP D . n 
D 1 11  MET 11  11  11  MET MET D . n 
D 1 12  PRO 12  12  12  PRO PRO D . n 
D 1 13  LEU 13  13  13  LEU LEU D . n 
D 1 14  ASP 14  14  14  ASP ASP D . n 
D 1 15  SER 15  15  15  SER SER D . n 
D 1 16  ASP 16  16  16  ASP ASP D . n 
D 1 17  VAL 17  17  17  VAL VAL D . n 
D 1 18  PHE 18  18  18  PHE PHE D . n 
D 1 19  ARG 19  19  19  ARG ARG D . n 
D 1 20  VAL 20  20  20  VAL VAL D . n 
D 1 21  PRO 21  21  21  PRO PRO D . n 
D 1 22  PRO 22  22  22  PRO PRO D . n 
D 1 23  GLY 23  23  23  GLY GLY D . n 
D 1 24  TYR 24  24  24  TYR TYR D . n 
D 1 25  ASN 25  25  25  ASN ASN D . n 
D 1 26  ALA 26  26  26  ALA ALA D . n 
D 1 27  PRO 27  27  27  PRO PRO D . n 
D 1 28  GLN 28  28  28  GLN GLN D . n 
D 1 29  GLN 29  29  29  GLN GLN D . n 
D 1 30  VAL 30  30  30  VAL VAL D . n 
D 1 31  HIS 31  31  31  HIS HIS D . n 
D 1 32  ILE 32  32  32  ILE ILE D . n 
D 1 33  THR 33  33  33  THR THR D . n 
D 1 34  GLN 34  34  34  GLN GLN D . n 
D 1 35  GLY 35  35  35  GLY GLY D . n 
D 1 36  ASP 36  36  36  ASP ASP D . n 
D 1 37  LEU 37  37  37  LEU LEU D . n 
D 1 38  VAL 38  38  38  VAL VAL D . n 
D 1 39  GLY 39  39  39  GLY GLY D . n 
D 1 40  ARG 40  40  40  ARG ARG D . n 
D 1 41  ALA 41  41  41  ALA ALA D . n 
D 1 42  MET 42  42  42  MET MET D . n 
D 1 43  ILE 43  43  43  ILE ILE D . n 
D 1 44  ILE 44  44  44  ILE ILE D . n 
D 1 45  SER 45  45  45  SER SER D . n 
D 1 46  TRP 46  46  46  TRP TRP D . n 
D 1 47  VAL 47  47  47  VAL VAL D . n 
D 1 48  THR 48  48  48  THR THR D . n 
D 1 49  MET 49  49  49  MET MET D . n 
D 1 50  ASP 50  50  50  ASP ASP D . n 
D 1 51  GLU 51  51  51  GLU GLU D . n 
D 1 52  PRO 52  52  52  PRO PRO D . n 
D 1 53  GLY 53  53  53  GLY GLY D . n 
D 1 54  SER 54  54  54  SER SER D . n 
D 1 55  SER 55  55  55  SER SER D . n 
D 1 56  ALA 56  56  56  ALA ALA D . n 
D 1 57  VAL 57  57  57  VAL VAL D . n 
D 1 58  ARG 58  58  58  ARG ARG D . n 
D 1 59  TYR 59  59  59  TYR TYR D . n 
D 1 60  TRP 60  60  60  TRP TRP D . n 
D 1 61  SER 61  61  61  SER SER D . n 
D 1 62  GLU 62  62  62  GLU GLU D . n 
D 1 63  LYS 63  63  63  LYS LYS D . n 
D 1 64  ASN 64  64  64  ASN ASN D . n 
D 1 65  GLY 65  65  65  GLY GLY D . n 
D 1 66  ARG 66  66  66  ARG ARG D . n 
D 1 67  LYS 67  67  67  LYS LYS D . n 
D 1 68  ARG 68  68  68  ARG ARG D . n 
D 1 69  ILE 69  69  69  ILE ILE D . n 
D 1 70  ALA 70  70  70  ALA ALA D . n 
D 1 71  LYS 71  71  71  LYS LYS D . n 
D 1 72  GLY 72  72  72  GLY GLY D . n 
D 1 73  LYS 73  73  73  LYS LYS D . n 
D 1 74  MET 74  74  74  MET MET D . n 
D 1 75  SER 75  75  75  SER SER D . n 
D 1 76  THR 76  76  76  THR THR D . n 
D 1 77  TYR 77  77  77  TYR TYR D . n 
D 1 78  ARG 78  78  78  ARG ARG D . n 
D 1 79  PHE 79  79  79  PHE PHE D . n 
D 1 80  PHE 80  80  80  PHE PHE D . n 
D 1 81  ASN 81  81  81  ASN ASN D . n 
D 1 82  TYR 82  82  82  TYR TYR D . n 
D 1 83  SER 83  83  83  SER SER D . n 
D 1 84  SER 84  84  84  SER SER D . n 
D 1 85  GLY 85  85  85  GLY GLY D . n 
D 1 86  PHE 86  86  86  PHE PHE D . n 
D 1 87  ILE 87  87  87  ILE ILE D . n 
D 1 88  HIS 88  88  88  HIS HIS D . n 
D 1 89  HIS 89  89  89  HIS HIS D . n 
D 1 90  THR 90  90  90  THR THR D . n 
D 1 91  THR 91  91  91  THR THR D . n 
D 1 92  ILE 92  92  92  ILE ILE D . n 
D 1 93  ARG 93  93  93  ARG ARG D . n 
D 1 94  LYS 94  94  94  LYS LYS D . n 
D 1 95  LEU 95  95  95  LEU LEU D . n 
D 1 96  LYS 96  96  96  LYS LYS D . n 
D 1 97  TYR 97  97  97  TYR TYR D . n 
D 1 98  ASN 98  98  98  ASN ASN D . n 
D 1 99  THR 99  99  99  THR THR D . n 
D 1 100 LYS 100 100 100 LYS LYS D . n 
D 1 101 TYR 101 101 101 TYR TYR D . n 
D 1 102 TYR 102 102 102 TYR TYR D . n 
D 1 103 TYR 103 103 103 TYR TYR D . n 
D 1 104 GLU 104 104 104 GLU GLU D . n 
D 1 105 VAL 105 105 105 VAL VAL D . n 
D 1 106 GLY 106 106 106 GLY GLY D . n 
D 1 107 LEU 107 107 107 LEU LEU D . n 
D 1 108 ARG 108 108 108 ARG ARG D . n 
D 1 109 ASN 109 109 109 ASN ASN D . n 
D 1 110 THR 110 110 110 THR THR D . n 
D 1 111 THR 111 111 111 THR THR D . n 
D 1 112 ARG 112 112 112 ARG ARG D . n 
D 1 113 ARG 113 113 113 ARG ARG D . n 
D 1 114 PHE 114 114 114 PHE PHE D . n 
D 1 115 SER 115 115 115 SER SER D . n 
D 1 116 PHE 116 116 116 PHE PHE D . n 
D 1 117 ILE 117 117 117 ILE ILE D . n 
D 1 118 THR 118 118 118 THR THR D . n 
D 1 119 PRO 119 119 119 PRO PRO D . n 
D 1 120 PRO 120 120 120 PRO PRO D . n 
D 1 121 GLN 121 121 121 GLN GLN D . n 
D 1 122 THR 122 122 122 THR THR D . n 
D 1 123 GLY 123 123 123 GLY GLY D . n 
D 1 124 LEU 124 124 124 LEU LEU D . n 
D 1 125 ASP 125 125 125 ASP ASP D . n 
D 1 126 VAL 126 126 126 VAL VAL D . n 
D 1 127 PRO 127 127 127 PRO PRO D . n 
D 1 128 TYR 128 128 128 TYR TYR D . n 
D 1 129 THR 129 129 129 THR THR D . n 
D 1 130 PHE 130 130 130 PHE PHE D . n 
D 1 131 GLY 131 131 131 GLY GLY D . n 
D 1 132 LEU 132 132 132 LEU LEU D . n 
D 1 133 ILE 133 133 133 ILE ILE D . n 
D 1 134 GLY 134 134 134 GLY GLY D . n 
D 1 135 ASP 135 135 135 ASP ASP D . n 
D 1 136 LEU 136 136 136 LEU LEU D . n 
D 1 137 GLY 137 137 137 GLY GLY D . n 
D 1 138 GLN 138 138 138 GLN GLN D . n 
D 1 139 SER 139 139 139 SER SER D . n 
D 1 140 PHE 140 140 140 PHE PHE D . n 
D 1 141 ASP 141 141 141 ASP ASP D . n 
D 1 142 SER 142 142 142 SER SER D . n 
D 1 143 ASN 143 143 143 ASN ASN D . n 
D 1 144 THR 144 144 144 THR THR D . n 
D 1 145 THR 145 145 145 THR THR D . n 
D 1 146 LEU 146 146 146 LEU LEU D . n 
D 1 147 SER 147 147 147 SER SER D . n 
D 1 148 HIS 148 148 148 HIS HIS D . n 
D 1 149 TYR 149 149 149 TYR TYR D . n 
D 1 150 GLU 150 150 150 GLU GLU D . n 
D 1 151 LEU 151 151 151 LEU LEU D . n 
D 1 152 SER 152 152 152 SER SER D . n 
D 1 153 PRO 153 153 153 PRO PRO D . n 
D 1 154 LYS 154 154 154 LYS LYS D . n 
D 1 155 LYS 155 155 155 LYS LYS D . n 
D 1 156 GLY 156 156 156 GLY GLY D . n 
D 1 157 GLN 157 157 157 GLN GLN D . n 
D 1 158 THR 158 158 158 THR THR D . n 
D 1 159 VAL 159 159 159 VAL VAL D . n 
D 1 160 LEU 160 160 160 LEU LEU D . n 
D 1 161 PHE 161 161 161 PHE PHE D . n 
D 1 162 VAL 162 162 162 VAL VAL D . n 
D 1 163 GLY 163 163 163 GLY GLY D . n 
D 1 164 ASP 164 164 164 ASP ASP D . n 
D 1 165 LEU 165 165 165 LEU LEU D . n 
D 1 166 SER 166 166 166 SER SER D . n 
D 1 167 TYR 167 167 167 TYR TYR D . n 
D 1 168 ALA 168 168 168 ALA ALA D . n 
D 1 169 ASP 169 169 169 ASP ASP D . n 
D 1 170 ARG 170 170 170 ARG ARG D . n 
D 1 171 TYR 171 171 171 TYR TYR D . n 
D 1 172 PRO 172 172 172 PRO PRO D . n 
D 1 173 ASN 173 173 173 ASN ASN D . n 
D 1 174 HIS 174 174 174 HIS HIS D . n 
D 1 175 ASP 175 175 175 ASP ASP D . n 
D 1 176 ASN 176 176 176 ASN ASN D . n 
D 1 177 VAL 177 177 177 VAL VAL D . n 
D 1 178 ARG 178 178 178 ARG ARG D . n 
D 1 179 TRP 179 179 179 TRP TRP D . n 
D 1 180 ASP 180 180 180 ASP ASP D . n 
D 1 181 THR 181 181 181 THR THR D . n 
D 1 182 TRP 182 182 182 TRP TRP D . n 
D 1 183 GLY 183 183 183 GLY GLY D . n 
D 1 184 ARG 184 184 184 ARG ARG D . n 
D 1 185 PHE 185 185 185 PHE PHE D . n 
D 1 186 THR 186 186 186 THR THR D . n 
D 1 187 GLU 187 187 187 GLU GLU D . n 
D 1 188 ARG 188 188 188 ARG ARG D . n 
D 1 189 SER 189 189 189 SER SER D . n 
D 1 190 VAL 190 190 190 VAL VAL D . n 
D 1 191 ALA 191 191 191 ALA ALA D . n 
D 1 192 TYR 192 192 192 TYR TYR D . n 
D 1 193 GLN 193 193 193 GLN GLN D . n 
D 1 194 PRO 194 194 194 PRO PRO D . n 
D 1 195 TRP 195 195 195 TRP TRP D . n 
D 1 196 ILE 196 196 196 ILE ILE D . n 
D 1 197 TRP 197 197 197 TRP TRP D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 ALA 199 199 199 ALA ALA D . n 
D 1 200 GLY 200 200 200 GLY GLY D . n 
D 1 201 ASN 201 201 201 ASN ASN D . n 
D 1 202 HIS 202 202 202 HIS HIS D . n 
D 1 203 GLU 203 203 203 GLU GLU D . n 
D 1 204 ILE 204 204 204 ILE ILE D . n 
D 1 205 GLU 205 205 205 GLU GLU D . n 
D 1 206 PHE 206 206 206 PHE PHE D . n 
D 1 207 ALA 207 207 207 ALA ALA D . n 
D 1 208 PRO 208 208 208 PRO PRO D . n 
D 1 209 GLU 209 209 209 GLU GLU D . n 
D 1 210 ILE 210 210 210 ILE ILE D . n 
D 1 211 ASN 211 211 211 ASN ASN D . n 
D 1 212 GLU 212 212 212 GLU GLU D . n 
D 1 213 THR 213 213 213 THR THR D . n 
D 1 214 GLU 214 214 214 GLU GLU D . n 
D 1 215 PRO 215 215 215 PRO PRO D . n 
D 1 216 PHE 216 216 216 PHE PHE D . n 
D 1 217 LYS 217 217 217 LYS LYS D . n 
D 1 218 PRO 218 218 218 PRO PRO D . n 
D 1 219 PHE 219 219 219 PHE PHE D . n 
D 1 220 SER 220 220 220 SER SER D . n 
D 1 221 TYR 221 221 221 TYR TYR D . n 
D 1 222 ARG 222 222 222 ARG ARG D . n 
D 1 223 TYR 223 223 223 TYR TYR D . n 
D 1 224 HIS 224 224 224 HIS HIS D . n 
D 1 225 VAL 225 225 225 VAL VAL D . n 
D 1 226 PRO 226 226 226 PRO PRO D . n 
D 1 227 TYR 227 227 227 TYR TYR D . n 
D 1 228 GLU 228 228 228 GLU GLU D . n 
D 1 229 ALA 229 229 229 ALA ALA D . n 
D 1 230 SER 230 230 230 SER SER D . n 
D 1 231 GLN 231 231 231 GLN GLN D . n 
D 1 232 SER 232 232 232 SER SER D . n 
D 1 233 THR 233 233 233 THR THR D . n 
D 1 234 SER 234 234 234 SER SER D . n 
D 1 235 PRO 235 235 235 PRO PRO D . n 
D 1 236 PHE 236 236 236 PHE PHE D . n 
D 1 237 TRP 237 237 237 TRP TRP D . n 
D 1 238 TYR 238 238 238 TYR TYR D . n 
D 1 239 SER 239 239 239 SER SER D . n 
D 1 240 ILE 240 240 240 ILE ILE D . n 
D 1 241 LYS 241 241 241 LYS LYS D . n 
D 1 242 ARG 242 242 242 ARG ARG D . n 
D 1 243 ALA 243 243 243 ALA ALA D . n 
D 1 244 SER 244 244 244 SER SER D . n 
D 1 245 ALA 245 245 245 ALA ALA D . n 
D 1 246 HIS 246 246 246 HIS HIS D . n 
D 1 247 ILE 247 247 247 ILE ILE D . n 
D 1 248 ILE 248 248 248 ILE ILE D . n 
D 1 249 VAL 249 249 249 VAL VAL D . n 
D 1 250 LEU 250 250 250 LEU LEU D . n 
D 1 251 SER 251 251 251 SER SER D . n 
D 1 252 SER 252 252 252 SER SER D . n 
D 1 253 TYR 253 253 253 TYR TYR D . n 
D 1 254 SER 254 254 254 SER SER D . n 
D 1 255 ALA 255 255 255 ALA ALA D . n 
D 1 256 TYR 256 256 256 TYR TYR D . n 
D 1 257 GLY 257 257 257 GLY GLY D . n 
D 1 258 ARG 258 258 258 ARG ARG D . n 
D 1 259 GLY 259 259 259 GLY GLY D . n 
D 1 260 THR 260 260 260 THR THR D . n 
D 1 261 PRO 261 261 261 PRO PRO D . n 
D 1 262 GLN 262 262 262 GLN GLN D . n 
D 1 263 TYR 263 263 263 TYR TYR D . n 
D 1 264 THR 264 264 264 THR THR D . n 
D 1 265 TRP 265 265 265 TRP TRP D . n 
D 1 266 LEU 266 266 266 LEU LEU D . n 
D 1 267 LYS 267 267 267 LYS LYS D . n 
D 1 268 LYS 268 268 268 LYS LYS D . n 
D 1 269 GLU 269 269 269 GLU GLU D . n 
D 1 270 LEU 270 270 270 LEU LEU D . n 
D 1 271 ARG 271 271 271 ARG ARG D . n 
D 1 272 LYS 272 272 272 LYS LYS D . n 
D 1 273 VAL 273 273 273 VAL VAL D . n 
D 1 274 LYS 274 274 274 LYS LYS D . n 
D 1 275 ARG 275 275 275 ARG ARG D . n 
D 1 276 SER 276 276 276 SER SER D . n 
D 1 277 GLU 277 277 277 GLU GLU D . n 
D 1 278 THR 278 278 278 THR THR D . n 
D 1 279 PRO 279 279 279 PRO PRO D . n 
D 1 280 TRP 280 280 280 TRP TRP D . n 
D 1 281 LEU 281 281 281 LEU LEU D . n 
D 1 282 ILE 282 282 282 ILE ILE D . n 
D 1 283 VAL 283 283 283 VAL VAL D . n 
D 1 284 LEU 284 284 284 LEU LEU D . n 
D 1 285 MET 285 285 285 MET MET D . n 
D 1 286 HIS 286 286 286 HIS HIS D . n 
D 1 287 SER 287 287 287 SER SER D . n 
D 1 288 PRO 288 288 288 PRO PRO D . n 
D 1 289 LEU 289 289 289 LEU LEU D . n 
D 1 290 TYR 290 290 290 TYR TYR D . n 
D 1 291 ASN 291 291 291 ASN ASN D . n 
D 1 292 SER 292 292 292 SER SER D . n 
D 1 293 TYR 293 293 293 TYR TYR D . n 
D 1 294 ASN 294 294 294 ASN ASN D . n 
D 1 295 HIS 295 295 295 HIS HIS D . n 
D 1 296 HIS 296 296 296 HIS HIS D . n 
D 1 297 PHE 297 297 297 PHE PHE D . n 
D 1 298 MET 298 298 298 MET MET D . n 
D 1 299 GLU 299 299 299 GLU GLU D . n 
D 1 300 GLY 300 300 300 GLY GLY D . n 
D 1 301 GLU 301 301 301 GLU GLU D . n 
D 1 302 ALA 302 302 302 ALA ALA D . n 
D 1 303 MET 303 303 303 MET MET D . n 
D 1 304 ARG 304 304 304 ARG ARG D . n 
D 1 305 THR 305 305 305 THR THR D . n 
D 1 306 LYS 306 306 306 LYS LYS D . n 
D 1 307 PHE 307 307 307 PHE PHE D . n 
D 1 308 GLU 308 308 308 GLU GLU D . n 
D 1 309 ALA 309 309 309 ALA ALA D . n 
D 1 310 TRP 310 310 310 TRP TRP D . n 
D 1 311 PHE 311 311 311 PHE PHE D . n 
D 1 312 VAL 312 312 312 VAL VAL D . n 
D 1 313 LYS 313 313 313 LYS LYS D . n 
D 1 314 TYR 314 314 314 TYR TYR D . n 
D 1 315 LYS 315 315 315 LYS LYS D . n 
D 1 316 VAL 316 316 316 VAL VAL D . n 
D 1 317 ASP 317 317 317 ASP ASP D . n 
D 1 318 VAL 318 318 318 VAL VAL D . n 
D 1 319 VAL 319 319 319 VAL VAL D . n 
D 1 320 PHE 320 320 320 PHE PHE D . n 
D 1 321 ALA 321 321 321 ALA ALA D . n 
D 1 322 GLY 322 322 322 GLY GLY D . n 
D 1 323 HIS 323 323 323 HIS HIS D . n 
D 1 324 VAL 324 324 324 VAL VAL D . n 
D 1 325 HIS 325 325 325 HIS HIS D . n 
D 1 326 ALA 326 326 326 ALA ALA D . n 
D 1 327 TYR 327 327 327 TYR TYR D . n 
D 1 328 GLU 328 328 328 GLU GLU D . n 
D 1 329 ARG 329 329 329 ARG ARG D . n 
D 1 330 SER 330 330 330 SER SER D . n 
D 1 331 GLU 331 331 331 GLU GLU D . n 
D 1 332 ARG 332 332 332 ARG ARG D . n 
D 1 333 VAL 333 333 333 VAL VAL D . n 
D 1 334 SER 334 334 334 SER SER D . n 
D 1 335 ASN 335 335 335 ASN ASN D . n 
D 1 336 ILE 336 336 336 ILE ILE D . n 
D 1 337 ALA 337 337 337 ALA ALA D . n 
D 1 338 TYR 338 338 338 TYR TYR D . n 
D 1 339 LYS 339 339 339 LYS LYS D . n 
D 1 340 ILE 340 340 340 ILE ILE D . n 
D 1 341 THR 341 341 341 THR THR D . n 
D 1 342 ASP 342 342 342 ASP ASP D . n 
D 1 343 GLY 343 343 343 GLY GLY D . n 
D 1 344 LEU 344 344 344 LEU LEU D . n 
D 1 345 CYS 345 345 345 CYS CYS D . n 
D 1 346 THR 346 346 346 THR THR D . n 
D 1 347 PRO 347 347 347 PRO PRO D . n 
D 1 348 VAL 348 348 348 VAL VAL D . n 
D 1 349 LYS 349 349 349 LYS LYS D . n 
D 1 350 ASP 350 350 350 ASP ASP D . n 
D 1 351 GLN 351 351 351 GLN GLN D . n 
D 1 352 SER 352 352 352 SER SER D . n 
D 1 353 ALA 353 353 353 ALA ALA D . n 
D 1 354 PRO 354 354 354 PRO PRO D . n 
D 1 355 VAL 355 355 355 VAL VAL D . n 
D 1 356 TYR 356 356 356 TYR TYR D . n 
D 1 357 ILE 357 357 357 ILE ILE D . n 
D 1 358 THR 358 358 358 THR THR D . n 
D 1 359 ILE 359 359 359 ILE ILE D . n 
D 1 360 GLY 360 360 360 GLY GLY D . n 
D 1 361 ASP 361 361 361 ASP ASP D . n 
D 1 362 ALA 362 362 362 ALA ALA D . n 
D 1 363 GLY 363 363 363 GLY GLY D . n 
D 1 364 ASN 364 364 364 ASN ASN D . n 
D 1 365 TYR 365 365 365 TYR TYR D . n 
D 1 366 GLY 366 366 366 GLY GLY D . n 
D 1 367 VAL 367 367 367 VAL VAL D . n 
D 1 368 ILE 368 368 368 ILE ILE D . n 
D 1 369 ASP 369 369 369 ASP ASP D . n 
D 1 370 SER 370 370 370 SER SER D . n 
D 1 371 ASN 371 371 371 ASN ASN D . n 
D 1 372 MET 372 372 372 MET MET D . n 
D 1 373 ILE 373 373 373 ILE ILE D . n 
D 1 374 GLN 374 374 374 GLN GLN D . n 
D 1 375 PRO 375 375 375 PRO PRO D . n 
D 1 376 GLN 376 376 376 GLN GLN D . n 
D 1 377 PRO 377 377 377 PRO PRO D . n 
D 1 378 GLU 378 378 378 GLU GLU D . n 
D 1 379 TYR 379 379 379 TYR TYR D . n 
D 1 380 SER 380 380 380 SER SER D . n 
D 1 381 ALA 381 381 381 ALA ALA D . n 
D 1 382 PHE 382 382 382 PHE PHE D . n 
D 1 383 ARG 383 383 383 ARG ARG D . n 
D 1 384 GLU 384 384 384 GLU GLU D . n 
D 1 385 ALA 385 385 385 ALA ALA D . n 
D 1 386 SER 386 386 386 SER SER D . n 
D 1 387 PHE 387 387 387 PHE PHE D . n 
D 1 388 GLY 388 388 388 GLY GLY D . n 
D 1 389 HIS 389 389 389 HIS HIS D . n 
D 1 390 GLY 390 390 390 GLY GLY D . n 
D 1 391 MET 391 391 391 MET MET D . n 
D 1 392 PHE 392 392 392 PHE PHE D . n 
D 1 393 ASP 393 393 393 ASP ASP D . n 
D 1 394 ILE 394 394 394 ILE ILE D . n 
D 1 395 LYS 395 395 395 LYS LYS D . n 
D 1 396 ASN 396 396 396 ASN ASN D . n 
D 1 397 ARG 397 397 397 ARG ARG D . n 
D 1 398 THR 398 398 398 THR THR D . n 
D 1 399 HIS 399 399 399 HIS HIS D . n 
D 1 400 ALA 400 400 400 ALA ALA D . n 
D 1 401 HIS 401 401 401 HIS HIS D . n 
D 1 402 PHE 402 402 402 PHE PHE D . n 
D 1 403 SER 403 403 403 SER SER D . n 
D 1 404 TRP 404 404 404 TRP TRP D . n 
D 1 405 ASN 405 405 405 ASN ASN D . n 
D 1 406 ARG 406 406 406 ARG ARG D . n 
D 1 407 ASN 407 407 407 ASN ASN D . n 
D 1 408 GLN 408 408 408 GLN GLN D . n 
D 1 409 ASP 409 409 409 ASP ASP D . n 
D 1 410 GLY 410 410 410 GLY GLY D . n 
D 1 411 VAL 411 411 411 VAL VAL D . n 
D 1 412 ALA 412 412 412 ALA ALA D . n 
D 1 413 VAL 413 413 413 VAL VAL D . n 
D 1 414 GLU 414 414 414 GLU GLU D . n 
D 1 415 ALA 415 415 415 ALA ALA D . n 
D 1 416 ASP 416 416 416 ASP ASP D . n 
D 1 417 SER 417 417 417 SER SER D . n 
D 1 418 VAL 418 418 418 VAL VAL D . n 
D 1 419 TRP 419 419 419 TRP TRP D . n 
D 1 420 PHE 420 420 420 PHE PHE D . n 
D 1 421 PHE 421 421 421 PHE PHE D . n 
D 1 422 ASN 422 422 422 ASN ASN D . n 
D 1 423 ARG 423 423 423 ARG ARG D . n 
D 1 424 HIS 424 424 424 HIS HIS D . n 
D 1 425 TRP 425 425 425 TRP TRP D . n 
D 1 426 TYR 426 426 426 TYR TYR D . n 
D 1 427 PRO 427 427 427 PRO PRO D . n 
D 1 428 VAL 428 428 428 VAL VAL D . n 
D 1 429 ASP 429 429 429 ASP ASP D . n 
D 1 430 ASP 430 430 430 ASP ASP D . n 
D 1 431 SER 431 431 431 SER SER D . n 
D 1 432 THR 432 432 432 THR THR D . n 
# 
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 81  A ASN 81  ? ASN 'GLYCOSYLATION SITE' 
2  A ASN 109 A ASN 109 ? ASN 'GLYCOSYLATION SITE' 
3  A ASN 143 A ASN 143 ? ASN 'GLYCOSYLATION SITE' 
4  A ASN 211 A ASN 211 ? ASN 'GLYCOSYLATION SITE' 
5  A ASN 396 A ASN 396 ? ASN 'GLYCOSYLATION SITE' 
6  B ASN 81  B ASN 81  ? ASN 'GLYCOSYLATION SITE' 
7  B ASN 109 B ASN 109 ? ASN 'GLYCOSYLATION SITE' 
8  B ASN 143 B ASN 143 ? ASN 'GLYCOSYLATION SITE' 
9  B ASN 211 B ASN 211 ? ASN 'GLYCOSYLATION SITE' 
10 B ASN 396 B ASN 396 ? ASN 'GLYCOSYLATION SITE' 
11 C ASN 81  C ASN 81  ? ASN 'GLYCOSYLATION SITE' 
12 C ASN 109 C ASN 109 ? ASN 'GLYCOSYLATION SITE' 
13 C ASN 143 C ASN 143 ? ASN 'GLYCOSYLATION SITE' 
14 C ASN 211 C ASN 211 ? ASN 'GLYCOSYLATION SITE' 
15 C ASN 396 C ASN 396 ? ASN 'GLYCOSYLATION SITE' 
16 D ASN 81  D ASN 81  ? ASN 'GLYCOSYLATION SITE' 
17 D ASN 109 D ASN 109 ? ASN 'GLYCOSYLATION SITE' 
18 D ASN 143 D ASN 143 ? ASN 'GLYCOSYLATION SITE' 
19 D ASN 211 D ASN 211 ? ASN 'GLYCOSYLATION SITE' 
20 D ASN 396 D ASN 396 ? 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_defined_assembly              ?    dimeric    2 
2 author_and_software_defined_assembly PISA dimeric    2 
3 author_defined_assembly              ?    dimeric    2 
4 software_defined_assembly            PISA tetrameric 4 
5 software_defined_assembly            PISA tetrameric 4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1,2 A,E,F,G,H,I,J,K,L,KA                              
2 1   B,C,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,LA,MA       
3 1,2 D,CA,DA,EA,FA,GA,HA,IA,JA,NA                      
4 1,2 A,D,E,F,G,H,I,J,K,L,CA,DA,EA,FA,GA,HA,IA,JA,KA,NA 
5 1,3 B,C,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,LA,MA       
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
2 'ABSA (A^2)' 6320  ? 
2 MORE         -116  ? 
2 'SSA (A^2)'  30160 ? 
4 'ABSA (A^2)' 15200 ? 
4 MORE         -219  ? 
4 'SSA (A^2)'  57800 ? 
5 'ABSA (A^2)' 15310 ? 
5 MORE         -220  ? 
5 'SSA (A^2)'  57650 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z         1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 
1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 3_655 -x+1,y,-z+1/2 -1.0000000000 0.0000000000 0.0000000000 132.7000000000 0.0000000000 
1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 64.3500000000  
3 'crystal symmetry operation' 4_556 x,-y,-z+1     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 
-1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 128.7000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A  ASP 135 ? A ASP 135 ? 1_555 FE ? J  FE . ? A FE 438 ? 1_555 OD2 ? A  ASP 164 ? A ASP 164 ? 1_555 97.0  ? 
2  OD1 ? A  ASP 135 ? A ASP 135 ? 1_555 FE ? J  FE . ? A FE 438 ? 1_555 OH  ? A  TYR 167 ? A TYR 167 ? 1_555 79.2  ? 
3  OD2 ? A  ASP 164 ? A ASP 164 ? 1_555 FE ? J  FE . ? A FE 438 ? 1_555 OH  ? A  TYR 167 ? A TYR 167 ? 1_555 99.6  ? 
4  OD1 ? A  ASP 135 ? A ASP 135 ? 1_555 FE ? J  FE . ? A FE 438 ? 1_555 O2  ? L  PO4 .   ? A PO4 440 ? 1_555 169.8 ? 
5  OD2 ? A  ASP 164 ? A ASP 164 ? 1_555 FE ? J  FE . ? A FE 438 ? 1_555 O2  ? L  PO4 .   ? A PO4 440 ? 1_555 92.4  ? 
6  OH  ? A  TYR 167 ? A TYR 167 ? 1_555 FE ? J  FE . ? A FE 438 ? 1_555 O2  ? L  PO4 .   ? A PO4 440 ? 1_555 95.4  ? 
7  OD1 ? A  ASP 135 ? A ASP 135 ? 1_555 FE ? J  FE . ? A FE 438 ? 1_555 NE2 ? A  HIS 325 ? A HIS 325 ? 1_555 86.2  ? 
8  OD2 ? A  ASP 164 ? A ASP 164 ? 1_555 FE ? J  FE . ? A FE 438 ? 1_555 NE2 ? A  HIS 325 ? A HIS 325 ? 1_555 172.3 ? 
9  OH  ? A  TYR 167 ? A TYR 167 ? 1_555 FE ? J  FE . ? A FE 438 ? 1_555 NE2 ? A  HIS 325 ? A HIS 325 ? 1_555 87.9  ? 
10 O2  ? L  PO4 .   ? A PO4 440 ? 1_555 FE ? J  FE . ? A FE 438 ? 1_555 NE2 ? A  HIS 325 ? A HIS 325 ? 1_555 84.9  ? 
11 OD2 ? A  ASP 164 ? A ASP 164 ? 1_555 ZN ? K  ZN . ? A ZN 439 ? 1_555 OD1 ? A  ASN 201 ? A ASN 201 ? 1_555 99.6  ? 
12 OD2 ? A  ASP 164 ? A ASP 164 ? 1_555 ZN ? K  ZN . ? A ZN 439 ? 1_555 NE2 ? A  HIS 286 ? A HIS 286 ? 1_555 86.9  ? 
13 OD1 ? A  ASN 201 ? A ASN 201 ? 1_555 ZN ? K  ZN . ? A ZN 439 ? 1_555 NE2 ? A  HIS 286 ? A HIS 286 ? 1_555 87.5  ? 
14 OD2 ? A  ASP 164 ? A ASP 164 ? 1_555 ZN ? K  ZN . ? A ZN 439 ? 1_555 ND1 ? A  HIS 323 ? A HIS 323 ? 1_555 160.5 ? 
15 OD1 ? A  ASN 201 ? A ASN 201 ? 1_555 ZN ? K  ZN . ? A ZN 439 ? 1_555 ND1 ? A  HIS 323 ? A HIS 323 ? 1_555 97.3  ? 
16 NE2 ? A  HIS 286 ? A HIS 286 ? 1_555 ZN ? K  ZN . ? A ZN 439 ? 1_555 ND1 ? A  HIS 323 ? A HIS 323 ? 1_555 84.3  ? 
17 OD2 ? A  ASP 164 ? A ASP 164 ? 1_555 ZN ? K  ZN . ? A ZN 439 ? 1_555 O3  ? L  PO4 .   ? A PO4 440 ? 1_555 97.6  ? 
18 OD1 ? A  ASN 201 ? A ASN 201 ? 1_555 ZN ? K  ZN . ? A ZN 439 ? 1_555 O3  ? L  PO4 .   ? A PO4 440 ? 1_555 97.3  ? 
19 NE2 ? A  HIS 286 ? A HIS 286 ? 1_555 ZN ? K  ZN . ? A ZN 439 ? 1_555 O3  ? L  PO4 .   ? A PO4 440 ? 1_555 172.8 ? 
20 ND1 ? A  HIS 323 ? A HIS 323 ? 1_555 ZN ? K  ZN . ? A ZN 439 ? 1_555 O3  ? L  PO4 .   ? A PO4 440 ? 1_555 89.7  ? 
21 OD1 ? B  ASP 135 ? B ASP 135 ? 1_555 FE ? R  FE . ? B FE 438 ? 1_555 OD2 ? B  ASP 164 ? B ASP 164 ? 1_555 96.5  ? 
22 OD1 ? B  ASP 135 ? B ASP 135 ? 1_555 FE ? R  FE . ? B FE 438 ? 1_555 OH  ? B  TYR 167 ? B TYR 167 ? 1_555 79.9  ? 
23 OD2 ? B  ASP 164 ? B ASP 164 ? 1_555 FE ? R  FE . ? B FE 438 ? 1_555 OH  ? B  TYR 167 ? B TYR 167 ? 1_555 101.3 ? 
24 OD1 ? B  ASP 135 ? B ASP 135 ? 1_555 FE ? R  FE . ? B FE 438 ? 1_555 O2  ? T  PO4 .   ? B PO4 440 ? 1_555 169.4 ? 
25 OD2 ? B  ASP 164 ? B ASP 164 ? 1_555 FE ? R  FE . ? B FE 438 ? 1_555 O2  ? T  PO4 .   ? B PO4 440 ? 1_555 93.4  ? 
26 OH  ? B  TYR 167 ? B TYR 167 ? 1_555 FE ? R  FE . ? B FE 438 ? 1_555 O2  ? T  PO4 .   ? B PO4 440 ? 1_555 94.6  ? 
27 OD1 ? B  ASP 135 ? B ASP 135 ? 1_555 FE ? R  FE . ? B FE 438 ? 1_555 NE2 ? B  HIS 325 ? B HIS 325 ? 1_555 85.8  ? 
28 OD2 ? B  ASP 164 ? B ASP 164 ? 1_555 FE ? R  FE . ? B FE 438 ? 1_555 NE2 ? B  HIS 325 ? B HIS 325 ? 1_555 171.2 ? 
29 OH  ? B  TYR 167 ? B TYR 167 ? 1_555 FE ? R  FE . ? B FE 438 ? 1_555 NE2 ? B  HIS 325 ? B HIS 325 ? 1_555 87.4  ? 
30 O2  ? T  PO4 .   ? B PO4 440 ? 1_555 FE ? R  FE . ? B FE 438 ? 1_555 NE2 ? B  HIS 325 ? B HIS 325 ? 1_555 85.0  ? 
31 OD2 ? B  ASP 164 ? B ASP 164 ? 1_555 ZN ? S  ZN . ? B ZN 439 ? 1_555 OD1 ? B  ASN 201 ? B ASN 201 ? 1_555 99.7  ? 
32 OD2 ? B  ASP 164 ? B ASP 164 ? 1_555 ZN ? S  ZN . ? B ZN 439 ? 1_555 NE2 ? B  HIS 286 ? B HIS 286 ? 1_555 86.8  ? 
33 OD1 ? B  ASN 201 ? B ASN 201 ? 1_555 ZN ? S  ZN . ? B ZN 439 ? 1_555 NE2 ? B  HIS 286 ? B HIS 286 ? 1_555 88.8  ? 
34 OD2 ? B  ASP 164 ? B ASP 164 ? 1_555 ZN ? S  ZN . ? B ZN 439 ? 1_555 ND1 ? B  HIS 323 ? B HIS 323 ? 1_555 162.1 ? 
35 OD1 ? B  ASN 201 ? B ASN 201 ? 1_555 ZN ? S  ZN . ? B ZN 439 ? 1_555 ND1 ? B  HIS 323 ? B HIS 323 ? 1_555 97.2  ? 
36 NE2 ? B  HIS 286 ? B HIS 286 ? 1_555 ZN ? S  ZN . ? B ZN 439 ? 1_555 ND1 ? B  HIS 323 ? B HIS 323 ? 1_555 87.7  ? 
37 OD2 ? B  ASP 164 ? B ASP 164 ? 1_555 ZN ? S  ZN . ? B ZN 439 ? 1_555 O3  ? T  PO4 .   ? B PO4 440 ? 1_555 97.1  ? 
38 OD1 ? B  ASN 201 ? B ASN 201 ? 1_555 ZN ? S  ZN . ? B ZN 439 ? 1_555 O3  ? T  PO4 .   ? B PO4 440 ? 1_555 95.5  ? 
39 NE2 ? B  HIS 286 ? B HIS 286 ? 1_555 ZN ? S  ZN . ? B ZN 439 ? 1_555 O3  ? T  PO4 .   ? B PO4 440 ? 1_555 173.7 ? 
40 ND1 ? B  HIS 323 ? B HIS 323 ? 1_555 ZN ? S  ZN . ? B ZN 439 ? 1_555 O3  ? T  PO4 .   ? B PO4 440 ? 1_555 87.1  ? 
41 OD1 ? C  ASP 135 ? C ASP 135 ? 1_555 FE ? Z  FE . ? C FE 438 ? 1_555 OD2 ? C  ASP 164 ? C ASP 164 ? 1_555 100.6 ? 
42 OD1 ? C  ASP 135 ? C ASP 135 ? 1_555 FE ? Z  FE . ? C FE 438 ? 1_555 OH  ? C  TYR 167 ? C TYR 167 ? 1_555 79.5  ? 
43 OD2 ? C  ASP 164 ? C ASP 164 ? 1_555 FE ? Z  FE . ? C FE 438 ? 1_555 OH  ? C  TYR 167 ? C TYR 167 ? 1_555 100.6 ? 
44 OD1 ? C  ASP 135 ? C ASP 135 ? 1_555 FE ? Z  FE . ? C FE 438 ? 1_555 O2  ? BA PO4 .   ? C PO4 440 ? 1_555 167.7 ? 
45 OD2 ? C  ASP 164 ? C ASP 164 ? 1_555 FE ? Z  FE . ? C FE 438 ? 1_555 O2  ? BA PO4 .   ? C PO4 440 ? 1_555 90.8  ? 
46 OH  ? C  TYR 167 ? C TYR 167 ? 1_555 FE ? Z  FE . ? C FE 438 ? 1_555 O2  ? BA PO4 .   ? C PO4 440 ? 1_555 94.0  ? 
47 OD1 ? C  ASP 135 ? C ASP 135 ? 1_555 FE ? Z  FE . ? C FE 438 ? 1_555 NE2 ? C  HIS 325 ? C HIS 325 ? 1_555 85.8  ? 
48 OD2 ? C  ASP 164 ? C ASP 164 ? 1_555 FE ? Z  FE . ? C FE 438 ? 1_555 NE2 ? C  HIS 325 ? C HIS 325 ? 1_555 171.4 ? 
49 OH  ? C  TYR 167 ? C TYR 167 ? 1_555 FE ? Z  FE . ? C FE 438 ? 1_555 NE2 ? C  HIS 325 ? C HIS 325 ? 1_555 86.1  ? 
50 O2  ? BA PO4 .   ? C PO4 440 ? 1_555 FE ? Z  FE . ? C FE 438 ? 1_555 NE2 ? C  HIS 325 ? C HIS 325 ? 1_555 83.3  ? 
51 OD2 ? C  ASP 164 ? C ASP 164 ? 1_555 ZN ? AA ZN . ? C ZN 439 ? 1_555 OD1 ? C  ASN 201 ? C ASN 201 ? 1_555 99.1  ? 
52 OD2 ? C  ASP 164 ? C ASP 164 ? 1_555 ZN ? AA ZN . ? C ZN 439 ? 1_555 NE2 ? C  HIS 286 ? C HIS 286 ? 1_555 86.3  ? 
53 OD1 ? C  ASN 201 ? C ASN 201 ? 1_555 ZN ? AA ZN . ? C ZN 439 ? 1_555 NE2 ? C  HIS 286 ? C HIS 286 ? 1_555 87.3  ? 
54 OD2 ? C  ASP 164 ? C ASP 164 ? 1_555 ZN ? AA ZN . ? C ZN 439 ? 1_555 ND1 ? C  HIS 323 ? C HIS 323 ? 1_555 161.1 ? 
55 OD1 ? C  ASN 201 ? C ASN 201 ? 1_555 ZN ? AA ZN . ? C ZN 439 ? 1_555 ND1 ? C  HIS 323 ? C HIS 323 ? 1_555 98.2  ? 
56 NE2 ? C  HIS 286 ? C HIS 286 ? 1_555 ZN ? AA ZN . ? C ZN 439 ? 1_555 ND1 ? C  HIS 323 ? C HIS 323 ? 1_555 86.9  ? 
57 OD2 ? C  ASP 164 ? C ASP 164 ? 1_555 ZN ? AA ZN . ? C ZN 439 ? 1_555 O3  ? BA PO4 .   ? C PO4 440 ? 1_555 96.5  ? 
58 OD1 ? C  ASN 201 ? C ASN 201 ? 1_555 ZN ? AA ZN . ? C ZN 439 ? 1_555 O3  ? BA PO4 .   ? C PO4 440 ? 1_555 96.4  ? 
59 NE2 ? C  HIS 286 ? C HIS 286 ? 1_555 ZN ? AA ZN . ? C ZN 439 ? 1_555 O3  ? BA PO4 .   ? C PO4 440 ? 1_555 174.9 ? 
60 ND1 ? C  HIS 323 ? C HIS 323 ? 1_555 ZN ? AA ZN . ? C ZN 439 ? 1_555 O3  ? BA PO4 .   ? C PO4 440 ? 1_555 89.1  ? 
61 OD1 ? D  ASP 135 ? D ASP 135 ? 1_555 FE ? HA FE . ? D FE 438 ? 1_555 OD2 ? D  ASP 164 ? D ASP 164 ? 1_555 100.7 ? 
62 OD1 ? D  ASP 135 ? D ASP 135 ? 1_555 FE ? HA FE . ? D FE 438 ? 1_555 OH  ? D  TYR 167 ? D TYR 167 ? 1_555 80.3  ? 
63 OD2 ? D  ASP 164 ? D ASP 164 ? 1_555 FE ? HA FE . ? D FE 438 ? 1_555 OH  ? D  TYR 167 ? D TYR 167 ? 1_555 105.2 ? 
64 OD1 ? D  ASP 135 ? D ASP 135 ? 1_555 FE ? HA FE . ? D FE 438 ? 1_555 O2  ? JA PO4 .   ? D PO4 440 ? 1_555 168.2 ? 
65 OD2 ? D  ASP 164 ? D ASP 164 ? 1_555 FE ? HA FE . ? D FE 438 ? 1_555 O2  ? JA PO4 .   ? D PO4 440 ? 1_555 90.1  ? 
66 OH  ? D  TYR 167 ? D TYR 167 ? 1_555 FE ? HA FE . ? D FE 438 ? 1_555 O2  ? JA PO4 .   ? D PO4 440 ? 1_555 92.6  ? 
67 OD1 ? D  ASP 135 ? D ASP 135 ? 1_555 FE ? HA FE . ? D FE 438 ? 1_555 NE2 ? D  HIS 325 ? D HIS 325 ? 1_555 86.1  ? 
68 OD2 ? D  ASP 164 ? D ASP 164 ? 1_555 FE ? HA FE . ? D FE 438 ? 1_555 NE2 ? D  HIS 325 ? D HIS 325 ? 1_555 169.9 ? 
69 OH  ? D  TYR 167 ? D TYR 167 ? 1_555 FE ? HA FE . ? D FE 438 ? 1_555 NE2 ? D  HIS 325 ? D HIS 325 ? 1_555 83.2  ? 
70 O2  ? JA PO4 .   ? D PO4 440 ? 1_555 FE ? HA FE . ? D FE 438 ? 1_555 NE2 ? D  HIS 325 ? D HIS 325 ? 1_555 83.7  ? 
71 OD2 ? D  ASP 164 ? D ASP 164 ? 1_555 ZN ? IA ZN . ? D ZN 439 ? 1_555 OD1 ? D  ASN 201 ? D ASN 201 ? 1_555 100.6 ? 
72 OD2 ? D  ASP 164 ? D ASP 164 ? 1_555 ZN ? IA ZN . ? D ZN 439 ? 1_555 NE2 ? D  HIS 286 ? D HIS 286 ? 1_555 87.2  ? 
73 OD1 ? D  ASN 201 ? D ASN 201 ? 1_555 ZN ? IA ZN . ? D ZN 439 ? 1_555 NE2 ? D  HIS 286 ? D HIS 286 ? 1_555 87.0  ? 
74 OD2 ? D  ASP 164 ? D ASP 164 ? 1_555 ZN ? IA ZN . ? D ZN 439 ? 1_555 ND1 ? D  HIS 323 ? D HIS 323 ? 1_555 160.7 ? 
75 OD1 ? D  ASN 201 ? D ASN 201 ? 1_555 ZN ? IA ZN . ? D ZN 439 ? 1_555 ND1 ? D  HIS 323 ? D HIS 323 ? 1_555 96.9  ? 
76 NE2 ? D  HIS 286 ? D HIS 286 ? 1_555 ZN ? IA ZN . ? D ZN 439 ? 1_555 ND1 ? D  HIS 323 ? D HIS 323 ? 1_555 85.6  ? 
77 OD2 ? D  ASP 164 ? D ASP 164 ? 1_555 ZN ? IA ZN . ? D ZN 439 ? 1_555 O3  ? JA PO4 .   ? D PO4 440 ? 1_555 98.4  ? 
78 OD1 ? D  ASN 201 ? D ASN 201 ? 1_555 ZN ? IA ZN . ? D ZN 439 ? 1_555 O3  ? JA PO4 .   ? D PO4 440 ? 1_555 97.3  ? 
79 NE2 ? D  HIS 286 ? D HIS 286 ? 1_555 ZN ? IA ZN . ? D ZN 439 ? 1_555 O3  ? JA PO4 .   ? D PO4 440 ? 1_555 172.2 ? 
80 ND1 ? D  HIS 323 ? D HIS 323 ? 1_555 ZN ? IA ZN . ? D ZN 439 ? 1_555 O3  ? JA PO4 .   ? D PO4 440 ? 1_555 87.5  ? 
# 
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 1996-12-07 
2 'Structure model' 1 1 2008-03-25 
3 'Structure model' 1 2 2011-07-13 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Non-polymer description'   
3 3 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
DENZO     'data reduction' .   ? 1 
SCALEPACK 'data scaling'   .   ? 2 
X-PLOR    'model building' 3.1 ? 3 
X-PLOR    refinement       3.1 ? 4 
X-PLOR    phasing          3.1 ? 5 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD1 A TYR 238 ? ? CE1 A TYR 238 ? ? 1.480 1.389 0.091  0.015 N 
2 1 CB  D CYS 345 ? ? SG  D CYS 345 ? ? 1.705 1.812 -0.107 0.016 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CA A LEU 132 ? ? CB A LEU 132 ? ? CG  A LEU 132 ? ? 99.35  115.30 -15.95 2.30 N 
2  1 CB A ASP 135 ? ? CG A ASP 135 ? ? OD1 A ASP 135 ? ? 106.87 118.30 -11.43 0.90 N 
3  1 CB A ASP 135 ? ? CG A ASP 135 ? ? OD2 A ASP 135 ? ? 123.89 118.30 5.59   0.90 N 
4  1 N  A LYS 154 ? ? CA A LYS 154 ? ? C   A LYS 154 ? ? 91.38  111.00 -19.62 2.70 N 
5  1 N  A SER 230 ? ? CA A SER 230 ? ? C   A SER 230 ? ? 91.77  111.00 -19.23 2.70 N 
6  1 C  A SER 287 ? ? N  A PRO 288 ? ? CA  A PRO 288 ? ? 129.02 119.30 9.72   1.50 Y 
7  1 C  A TYR 426 ? ? N  A PRO 427 ? ? CA  A PRO 427 ? ? 129.11 119.30 9.81   1.50 Y 
8  1 CA B LEU 132 ? ? CB B LEU 132 ? ? CG  B LEU 132 ? ? 100.18 115.30 -15.12 2.30 N 
9  1 CB B ASP 135 ? ? CG B ASP 135 ? ? OD1 B ASP 135 ? ? 106.91 118.30 -11.39 0.90 N 
10 1 N  B LYS 154 ? ? CA B LYS 154 ? ? C   B LYS 154 ? ? 93.43  111.00 -17.57 2.70 N 
11 1 N  B SER 230 ? ? CA B SER 230 ? ? C   B SER 230 ? ? 91.93  111.00 -19.07 2.70 N 
12 1 C  B SER 287 ? ? N  B PRO 288 ? ? CA  B PRO 288 ? ? 128.93 119.30 9.63   1.50 Y 
13 1 CA C LEU 132 ? ? CB C LEU 132 ? ? CG  C LEU 132 ? ? 100.57 115.30 -14.73 2.30 N 
14 1 CB C ASP 135 ? ? CG C ASP 135 ? ? OD1 C ASP 135 ? ? 107.49 118.30 -10.81 0.90 N 
15 1 CB C ASP 135 ? ? CG C ASP 135 ? ? OD2 C ASP 135 ? ? 125.66 118.30 7.36   0.90 N 
16 1 N  C LYS 154 ? ? CA C LYS 154 ? ? C   C LYS 154 ? ? 94.17  111.00 -16.83 2.70 N 
17 1 N  C SER 230 ? ? CA C SER 230 ? ? C   C SER 230 ? ? 91.93  111.00 -19.07 2.70 N 
18 1 C  C SER 287 ? ? N  C PRO 288 ? ? CA  C PRO 288 ? ? 128.77 119.30 9.47   1.50 Y 
19 1 CB D ASP 135 ? ? CG D ASP 135 ? ? OD1 D ASP 135 ? ? 106.56 118.30 -11.74 0.90 N 
20 1 N  D LYS 154 ? ? CA D LYS 154 ? ? C   D LYS 154 ? ? 93.58  111.00 -17.42 2.70 N 
21 1 N  D SER 230 ? ? CA D SER 230 ? ? C   D SER 230 ? ? 91.76  111.00 -19.24 2.70 N 
22 1 C  D SER 287 ? ? N  D PRO 288 ? ? CA  D PRO 288 ? ? 128.54 119.30 9.24   1.50 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 40  ? ? -103.59 41.24   
2  1 LYS A 63  ? ? -74.85  -71.61  
3  1 PHE A 79  ? ? -99.45  -80.37  
4  1 PHE A 80  ? ? -121.17 -85.86  
5  1 ASN A 109 ? ? -115.61 -84.24  
6  1 GLN A 138 ? ? -141.51 45.48   
7  1 THR A 158 ? ? -174.16 133.46  
8  1 ASP A 164 ? ? 62.24   85.85   
9  1 HIS A 174 ? ? 49.12   28.32   
10 1 ASP A 175 ? ? -12.72  87.90   
11 1 ASN A 176 ? ? -55.82  -3.75   
12 1 PRO A 226 ? ? -79.95  48.47   
13 1 GLN A 231 ? ? -101.09 45.48   
14 1 TYR A 238 ? ? -175.28 -170.91 
15 1 ALA A 243 ? ? 59.49   -124.24 
16 1 HIS A 323 ? ? 75.67   -42.28  
17 1 ALA A 326 ? ? -173.10 -176.23 
18 1 ASN A 335 ? ? -152.43 56.16   
19 1 ILE A 340 ? ? 75.83   -68.01  
20 1 ASN A 364 ? ? 41.13   -140.65 
21 1 TYR A 365 ? ? -92.02  35.66   
22 1 TYR A 426 ? ? -161.75 59.51   
23 1 PRO A 427 ? ? -67.36  54.45   
24 1 ASP A 429 ? ? -55.28  102.54  
25 1 SER B 15  ? ? -38.52  129.45  
26 1 ARG B 40  ? ? -103.64 44.38   
27 1 LYS B 63  ? ? -76.93  -71.34  
28 1 PHE B 79  ? ? -97.77  -78.74  
29 1 PHE B 80  ? ? -123.42 -86.92  
30 1 ASN B 109 ? ? -113.10 -86.86  
31 1 THR B 158 ? ? -173.76 135.59  
32 1 ASP B 164 ? ? 62.38   84.64   
33 1 ASP B 175 ? ? -12.63  86.88   
34 1 ASN B 176 ? ? -55.95  -0.19   
35 1 SER B 189 ? ? -98.90  -60.77  
36 1 PRO B 226 ? ? -75.70  47.11   
37 1 GLN B 231 ? ? -101.43 47.41   
38 1 TYR B 238 ? ? -172.25 -171.37 
39 1 ALA B 243 ? ? 63.85   -120.71 
40 1 HIS B 323 ? ? 76.59   -41.52  
41 1 ALA B 326 ? ? -177.29 -175.38 
42 1 ASN B 335 ? ? -152.41 55.45   
43 1 LYS B 339 ? ? -141.32 36.49   
44 1 ILE B 340 ? ? 74.89   -68.56  
45 1 CYS B 345 ? ? -114.34 54.11   
46 1 ILE B 359 ? ? -116.84 51.34   
47 1 ASN B 364 ? ? 40.84   -136.74 
48 1 TYR B 365 ? ? -95.06  39.03   
49 1 TYR B 426 ? ? -170.18 54.82   
50 1 PRO B 427 ? ? -56.23  7.57    
51 1 SER B 431 ? ? -15.04  109.05  
52 1 ARG C 40  ? ? -104.33 41.63   
53 1 LYS C 63  ? ? -75.81  -71.48  
54 1 PHE C 79  ? ? -97.67  -76.20  
55 1 PHE C 80  ? ? -123.63 -87.41  
56 1 ASN C 109 ? ? -114.03 -83.07  
57 1 ASP C 164 ? ? 60.83   86.61   
58 1 ASP C 175 ? ? -5.11   86.57   
59 1 ASN C 176 ? ? -56.38  -4.75   
60 1 GLN C 231 ? ? -98.55  44.71   
61 1 TYR C 238 ? ? -170.32 -176.05 
62 1 ALA C 243 ? ? 62.19   -124.20 
63 1 HIS C 323 ? ? 74.49   -43.62  
64 1 ALA C 326 ? ? -175.25 -178.82 
65 1 ASN C 335 ? ? -153.53 55.48   
66 1 ILE C 340 ? ? 78.70   -68.55  
67 1 CYS C 345 ? ? -116.37 51.18   
68 1 ASN C 364 ? ? 41.52   -141.29 
69 1 TYR C 365 ? ? -91.42  32.93   
70 1 TYR C 426 ? ? -169.49 54.71   
71 1 PRO C 427 ? ? -64.88  63.94   
72 1 ASP C 429 ? ? -56.46  108.33  
73 1 SER C 431 ? ? -58.48  82.58   
74 1 SER D 15  ? ? -38.70  128.11  
75 1 ARG D 40  ? ? -105.71 43.12   
76 1 LYS D 63  ? ? -74.57  -71.18  
77 1 PHE D 79  ? ? -95.37  -79.42  
78 1 PHE D 80  ? ? -123.18 -86.37  
79 1 ASN D 109 ? ? -115.25 -83.81  
80 1 THR D 158 ? ? -173.75 133.92  
81 1 ASP D 164 ? ? 60.26   85.28   
82 1 ASP D 175 ? ? -11.01  87.34   
83 1 ASN D 176 ? ? -57.23  -2.59   
84 1 SER D 189 ? ? -100.96 -62.48  
85 1 ALA D 207 ? ? -120.00 75.61   
86 1 PRO D 226 ? ? -77.68  49.87   
87 1 GLN D 231 ? ? -99.09  44.28   
88 1 TYR D 238 ? ? -173.56 -176.64 
89 1 ALA D 243 ? ? 61.21   -121.35 
90 1 HIS D 323 ? ? 74.48   -41.14  
91 1 ALA D 326 ? ? -173.05 -178.33 
92 1 ASN D 335 ? ? -155.40 55.96   
93 1 LYS D 339 ? ? -141.43 33.51   
94 1 ILE D 340 ? ? 77.19   -70.24  
95 1 CYS D 345 ? ? -118.50 51.53   
96 1 ASN D 364 ? ? 41.55   -139.11 
97 1 TYR D 365 ? ? -95.09  38.03   
98 1 TYR D 426 ? ? -166.33 68.50   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 TYR B 223 ? ? 0.061 'SIDE CHAIN' 
2 1 TYR B 426 ? ? 0.065 'SIDE CHAIN' 
3 1 TYR D 167 ? ? 0.060 'SIDE CHAIN' 
4 1 TYR D 253 ? ? 0.066 'SIDE CHAIN' 
# 
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 PHE 1 ? A PHE 1 
2  1 Y 1 A VAL 2 ? A VAL 2 
3  1 Y 1 A ARG 3 ? A ARG 3 
4  1 Y 1 A LYS 4 ? A LYS 4 
5  1 Y 1 A THR 5 ? A THR 5 
6  1 Y 1 A ASN 6 ? A ASN 6 
7  1 Y 1 A LYS 7 ? A LYS 7 
8  1 Y 1 A ASN 8 ? A ASN 8 
9  1 Y 1 B PHE 1 ? B PHE 1 
10 1 Y 1 B VAL 2 ? B VAL 2 
11 1 Y 1 B ARG 3 ? B ARG 3 
12 1 Y 1 B LYS 4 ? B LYS 4 
13 1 Y 1 B THR 5 ? B THR 5 
14 1 Y 1 B ASN 6 ? B ASN 6 
15 1 Y 1 B LYS 7 ? B LYS 7 
16 1 Y 1 B ASN 8 ? B ASN 8 
17 1 Y 1 C PHE 1 ? C PHE 1 
18 1 Y 1 C VAL 2 ? C VAL 2 
19 1 Y 1 C ARG 3 ? C ARG 3 
20 1 Y 1 C LYS 4 ? C LYS 4 
21 1 Y 1 C THR 5 ? C THR 5 
22 1 Y 1 C ASN 6 ? C ASN 6 
23 1 Y 1 C LYS 7 ? C LYS 7 
24 1 Y 1 C ASN 8 ? C ASN 8 
25 1 Y 1 D PHE 1 ? D PHE 1 
26 1 Y 1 D VAL 2 ? D VAL 2 
27 1 Y 1 D ARG 3 ? D ARG 3 
28 1 Y 1 D LYS 4 ? D LYS 4 
29 1 Y 1 D THR 5 ? D THR 5 
30 1 Y 1 D ASN 6 ? D ASN 6 
31 1 Y 1 D LYS 7 ? D LYS 7 
32 1 Y 1 D ASN 8 ? D ASN 8 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 'FE (III) ION'         FE  
4 'ZINC ION'             ZN  
5 'PHOSPHATE ION'        PO4 
6 water                  HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  2 NAG 1  433 81  NAG NAG A A 
F  2 NAG 1  434 109 NAG NAG A A 
G  2 NAG 1  435 143 NAG NAG A A 
H  2 NAG 1  436 211 NAG NAG A A 
I  2 NAG 1  437 396 NAG NAG A A 
J  3 FE  1  438 433 FE  FE  A . 
K  4 ZN  1  439 434 ZN  ZN  A . 
L  5 PO4 1  440 435 PO4 PO4 A . 
M  2 NAG 1  433 81  NAG NAG B A 
N  2 NAG 1  434 109 NAG NAG B A 
O  2 NAG 1  435 143 NAG NAG B A 
P  2 NAG 1  436 211 NAG NAG B A 
Q  2 NAG 1  437 396 NAG NAG B A 
R  3 FE  1  438 433 FE  FE  B . 
S  4 ZN  1  439 434 ZN  ZN  B . 
T  5 PO4 1  440 435 PO4 PO4 B . 
U  2 NAG 1  433 81  NAG NAG C A 
V  2 NAG 1  434 109 NAG NAG C A 
W  2 NAG 1  435 143 NAG NAG C A 
X  2 NAG 1  436 211 NAG NAG C A 
Y  2 NAG 1  437 396 NAG NAG C A 
Z  3 FE  1  438 433 FE  FE  C . 
AA 4 ZN  1  439 434 ZN  ZN  C . 
BA 5 PO4 1  440 435 PO4 PO4 C . 
CA 2 NAG 1  433 81  NAG NAG D A 
DA 2 NAG 1  434 109 NAG NAG D A 
EA 2 NAG 1  435 143 NAG NAG D A 
FA 2 NAG 1  436 211 NAG NAG D A 
GA 2 NAG 1  437 396 NAG NAG D A 
HA 3 FE  1  438 433 FE  FE  D . 
IA 4 ZN  1  439 434 ZN  ZN  D . 
JA 5 PO4 1  440 435 PO4 PO4 D . 
KA 6 HOH 1  441 1   HOH HOH A . 
KA 6 HOH 2  442 2   HOH HOH A . 
KA 6 HOH 3  443 3   HOH HOH A . 
KA 6 HOH 4  444 4   HOH HOH A . 
KA 6 HOH 5  445 5   HOH HOH A . 
KA 6 HOH 6  446 6   HOH HOH A . 
KA 6 HOH 7  447 7   HOH HOH A . 
KA 6 HOH 8  448 8   HOH HOH A . 
KA 6 HOH 9  449 9   HOH HOH A . 
KA 6 HOH 10 450 10  HOH HOH A . 
KA 6 HOH 11 451 11  HOH HOH A . 
KA 6 HOH 12 452 12  HOH HOH A . 
KA 6 HOH 13 453 14  HOH HOH A . 
KA 6 HOH 14 454 16  HOH HOH A . 
KA 6 HOH 15 455 17  HOH HOH A . 
KA 6 HOH 16 456 18  HOH HOH A . 
LA 6 HOH 1  441 19  HOH HOH B . 
LA 6 HOH 2  442 21  HOH HOH B . 
LA 6 HOH 3  443 22  HOH HOH B . 
LA 6 HOH 4  444 24  HOH HOH B . 
LA 6 HOH 5  445 25  HOH HOH B . 
LA 6 HOH 6  446 27  HOH HOH B . 
LA 6 HOH 7  447 28  HOH HOH B . 
LA 6 HOH 8  448 29  HOH HOH B . 
LA 6 HOH 9  449 30  HOH HOH B . 
LA 6 HOH 10 450 32  HOH HOH B . 
LA 6 HOH 11 451 34  HOH HOH B . 
LA 6 HOH 12 452 35  HOH HOH B . 
LA 6 HOH 13 453 36  HOH HOH B . 
MA 6 HOH 1  441 37  HOH HOH C . 
MA 6 HOH 2  442 39  HOH HOH C . 
MA 6 HOH 3  443 40  HOH HOH C . 
MA 6 HOH 4  444 41  HOH HOH C . 
MA 6 HOH 5  445 42  HOH HOH C . 
MA 6 HOH 6  446 43  HOH HOH C . 
MA 6 HOH 7  447 45  HOH HOH C . 
MA 6 HOH 8  448 46  HOH HOH C . 
MA 6 HOH 9  449 47  HOH HOH C . 
MA 6 HOH 10 450 48  HOH HOH C . 
MA 6 HOH 11 451 50  HOH HOH C . 
MA 6 HOH 12 452 52  HOH HOH C . 
MA 6 HOH 13 453 53  HOH HOH C . 
MA 6 HOH 14 454 54  HOH HOH C . 
NA 6 HOH 1  441 55  HOH HOH D . 
NA 6 HOH 2  442 56  HOH HOH D . 
NA 6 HOH 3  443 57  HOH HOH D . 
NA 6 HOH 4  444 58  HOH HOH D . 
NA 6 HOH 5  445 61  HOH HOH D . 
NA 6 HOH 6  446 62  HOH HOH D . 
NA 6 HOH 7  447 63  HOH HOH D . 
NA 6 HOH 8  448 64  HOH HOH D . 
NA 6 HOH 9  449 66  HOH HOH D . 
NA 6 HOH 10 450 68  HOH HOH D . 
NA 6 HOH 11 451 70  HOH HOH D . 
NA 6 HOH 12 452 71  HOH HOH D . 
NA 6 HOH 13 453 72  HOH HOH D . 
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