data_2DW2
# 
_entry.id   2DW2 
# 
_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   2DW2         
RCSB  RCSB025913   
WWPDB D_1000025913 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 2DW0 'the same protein(Form 2-1 crystal)' unspecified 
PDB 2DW1 'the same protein(Form 2-2 crystal)' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2DW2 
_pdbx_database_status.recvd_initial_deposition_date   2006-08-02 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Takeda, S.'   1 
'Igarashi, T.' 2 
'Araki, S.'    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 
'Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins' 
'Febs Lett.'               581 2416 2422 2007 FEBLAL NE 0014-5793 0165 ? 17485084 10.1016/j.febslet.2007.04.057      
1       
;Crystallization and preliminary X-ray crystallographic analysis of two vascular apoptosis-inducing proteins (VAPs) from Crotalus atrox venom.
;
'ACTA CRYSTALLOGR.,SECT.F' 62  688  691  2006 ?      DK 1744-3091 ?    ? 16820695 10.1107/S1744309106022548          
2       
;Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold
;
'Embo J.'                  25  2388 2396 2006 EMJODG UK 0261-4189 0897 ? 16688218 10.1038/sj.emboj.7601131           
3       'cDNA cloning and some additional peptide characterization of a single-chain vascular apoptosis-inducing protein, VAP2' 
ENDOTHELIUM                14  89   96   2007 ?      ?  1062-3329 0353 ? 17497365 10.1080/10623320701346882          
4       'Two vascular apoptosis-inducing proteins from snake venom are members of the metalloprotease/disintegrin family' 
Eur.J.Biochem.             253 36   41   1998 EJBCAI IX 0014-2956 0262 ? 9578458  10.1046/j.1432-1327.1998.2530036.x 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Igarashi, T.' 1  
primary 'Araki, S.'    2  
primary 'Mori, H.'     3  
primary 'Takeda, S.'   4  
1       'Igarashi, T.' 5  
1       'Oishi, Y.'    6  
1       'Araki, S.'    7  
1       'Mori, H.'     8  
1       'Takeda, S.'   9  
2       'Takeda, S.'   10 
2       'Igarashi, T.' 11 
2       'Mori, H.'     12 
2       'Araki, S.'    13 
3       'Masuda, S.'   14 
3       'Maeda, H.'    15 
3       'Miao, J.Y.'   16 
3       'Hayashi, H.'  17 
3       'Araki, S.'    18 
4       'Masuda, S.'   19 
4       'Hayashi, H.'  20 
4       'Araki, S.'    21 
# 
_cell.entry_id           2DW2 
_cell.length_a           220.742 
_cell.length_b           79.475 
_cell.length_c           58.690 
_cell.angle_alpha        90.00 
_cell.angle_beta         91.73 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2DW2 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
# 
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 Catrocollastatin       46912.762 2   ? ? 'residues 191-609' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   10  ? ? ?                  ? 
3 non-polymer man BETA-D-MANNOSE         180.156   2   ? ? ?                  ? 
4 non-polymer man ALPHA-D-MANNOSE        180.156   4   ? ? ?                  ? 
5 non-polymer man ALPHA-L-FUCOSE         164.156   2   ? ? ?                  ? 
6 non-polymer syn 'ZINC ION'             65.409    2   ? ? ?                  ? 
7 non-polymer syn 'CALCIUM ION'          40.078    6   ? ? ?                  ? 
8 water       nat water                  18.015    151 ? ? ?                  ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'VAP2, vascular apoptosis-inducing protein-2, catrocollastatin/VAP2B' 
# 
_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       
;HQKYNPFRFVELVLVVDKAMVTKNNGDLDKIKTRMYEIVNTVNEIYRYMYIHVALVGLEIWSNEDKITVKPEAGYTLNAF
GEWRKTDLLTRKKHDNAQLLTAIDLDRVIGLAYVGSMCHPKRSTGIIQDYSEINLVVAVIMAHEMGHNLGINHDSGYCSC
GDYACIMRPEISPEPSTFFSNCSYFECWDFIMNHNPECILNEPLGTDIISPPVCGNELLEVGEECDCGTPENCQNECCDA
ATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVFHKNGQPCLDNYGYCYNGNCPIMYHQC
YDLFGADVYEAEDSCFERNQKGNYYGYCRKENGNKIPCAPEDVKCGRLYCKDNSPGQNNPCKMFYSNEDEHKGMVLPGTK
CADGKVCSNGHCVDVATAY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HQKYNPFRFVELVLVVDKAMVTKNNGDLDKIKTRMYEIVNTVNEIYRYMYIHVALVGLEIWSNEDKITVKPEAGYTLNAF
GEWRKTDLLTRKKHDNAQLLTAIDLDRVIGLAYVGSMCHPKRSTGIIQDYSEINLVVAVIMAHEMGHNLGINHDSGYCSC
GDYACIMRPEISPEPSTFFSNCSYFECWDFIMNHNPECILNEPLGTDIISPPVCGNELLEVGEECDCGTPENCQNECCDA
ATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVFHKNGQPCLDNYGYCYNGNCPIMYHQC
YDLFGADVYEAEDSCFERNQKGNYYGYCRKENGNKIPCAPEDVKCGRLYCKDNSPGQNNPCKMFYSNEDEHKGMVLPGTK
CADGKVCSNGHCVDVATAY
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   GLN n 
1 3   LYS n 
1 4   TYR n 
1 5   ASN n 
1 6   PRO n 
1 7   PHE n 
1 8   ARG n 
1 9   PHE n 
1 10  VAL n 
1 11  GLU n 
1 12  LEU n 
1 13  VAL n 
1 14  LEU n 
1 15  VAL n 
1 16  VAL n 
1 17  ASP n 
1 18  LYS n 
1 19  ALA n 
1 20  MET n 
1 21  VAL n 
1 22  THR n 
1 23  LYS n 
1 24  ASN n 
1 25  ASN n 
1 26  GLY n 
1 27  ASP n 
1 28  LEU n 
1 29  ASP n 
1 30  LYS n 
1 31  ILE n 
1 32  LYS n 
1 33  THR n 
1 34  ARG n 
1 35  MET n 
1 36  TYR n 
1 37  GLU n 
1 38  ILE n 
1 39  VAL n 
1 40  ASN n 
1 41  THR n 
1 42  VAL n 
1 43  ASN n 
1 44  GLU n 
1 45  ILE n 
1 46  TYR n 
1 47  ARG n 
1 48  TYR n 
1 49  MET n 
1 50  TYR n 
1 51  ILE n 
1 52  HIS n 
1 53  VAL n 
1 54  ALA n 
1 55  LEU n 
1 56  VAL n 
1 57  GLY n 
1 58  LEU n 
1 59  GLU n 
1 60  ILE n 
1 61  TRP n 
1 62  SER n 
1 63  ASN n 
1 64  GLU n 
1 65  ASP n 
1 66  LYS n 
1 67  ILE n 
1 68  THR n 
1 69  VAL n 
1 70  LYS n 
1 71  PRO n 
1 72  GLU n 
1 73  ALA n 
1 74  GLY n 
1 75  TYR n 
1 76  THR n 
1 77  LEU n 
1 78  ASN n 
1 79  ALA n 
1 80  PHE n 
1 81  GLY n 
1 82  GLU n 
1 83  TRP n 
1 84  ARG n 
1 85  LYS n 
1 86  THR n 
1 87  ASP n 
1 88  LEU n 
1 89  LEU n 
1 90  THR n 
1 91  ARG n 
1 92  LYS n 
1 93  LYS n 
1 94  HIS n 
1 95  ASP n 
1 96  ASN n 
1 97  ALA n 
1 98  GLN n 
1 99  LEU n 
1 100 LEU n 
1 101 THR n 
1 102 ALA n 
1 103 ILE n 
1 104 ASP n 
1 105 LEU n 
1 106 ASP n 
1 107 ARG n 
1 108 VAL n 
1 109 ILE n 
1 110 GLY n 
1 111 LEU n 
1 112 ALA n 
1 113 TYR n 
1 114 VAL n 
1 115 GLY n 
1 116 SER n 
1 117 MET n 
1 118 CYS n 
1 119 HIS n 
1 120 PRO n 
1 121 LYS n 
1 122 ARG n 
1 123 SER n 
1 124 THR n 
1 125 GLY n 
1 126 ILE n 
1 127 ILE n 
1 128 GLN n 
1 129 ASP n 
1 130 TYR n 
1 131 SER n 
1 132 GLU n 
1 133 ILE n 
1 134 ASN n 
1 135 LEU n 
1 136 VAL n 
1 137 VAL n 
1 138 ALA n 
1 139 VAL n 
1 140 ILE n 
1 141 MET n 
1 142 ALA n 
1 143 HIS n 
1 144 GLU n 
1 145 MET n 
1 146 GLY n 
1 147 HIS n 
1 148 ASN n 
1 149 LEU n 
1 150 GLY n 
1 151 ILE n 
1 152 ASN n 
1 153 HIS n 
1 154 ASP n 
1 155 SER n 
1 156 GLY n 
1 157 TYR n 
1 158 CYS n 
1 159 SER n 
1 160 CYS n 
1 161 GLY n 
1 162 ASP n 
1 163 TYR n 
1 164 ALA n 
1 165 CYS n 
1 166 ILE n 
1 167 MET n 
1 168 ARG n 
1 169 PRO n 
1 170 GLU n 
1 171 ILE n 
1 172 SER n 
1 173 PRO n 
1 174 GLU n 
1 175 PRO n 
1 176 SER n 
1 177 THR n 
1 178 PHE n 
1 179 PHE n 
1 180 SER n 
1 181 ASN n 
1 182 CYS n 
1 183 SER n 
1 184 TYR n 
1 185 PHE n 
1 186 GLU n 
1 187 CYS n 
1 188 TRP n 
1 189 ASP n 
1 190 PHE n 
1 191 ILE n 
1 192 MET n 
1 193 ASN n 
1 194 HIS n 
1 195 ASN n 
1 196 PRO n 
1 197 GLU n 
1 198 CYS n 
1 199 ILE n 
1 200 LEU n 
1 201 ASN n 
1 202 GLU n 
1 203 PRO n 
1 204 LEU n 
1 205 GLY n 
1 206 THR n 
1 207 ASP n 
1 208 ILE n 
1 209 ILE n 
1 210 SER n 
1 211 PRO n 
1 212 PRO n 
1 213 VAL n 
1 214 CYS n 
1 215 GLY n 
1 216 ASN n 
1 217 GLU n 
1 218 LEU n 
1 219 LEU n 
1 220 GLU n 
1 221 VAL n 
1 222 GLY n 
1 223 GLU n 
1 224 GLU n 
1 225 CYS n 
1 226 ASP n 
1 227 CYS n 
1 228 GLY n 
1 229 THR n 
1 230 PRO n 
1 231 GLU n 
1 232 ASN n 
1 233 CYS n 
1 234 GLN n 
1 235 ASN n 
1 236 GLU n 
1 237 CYS n 
1 238 CYS n 
1 239 ASP n 
1 240 ALA n 
1 241 ALA n 
1 242 THR n 
1 243 CYS n 
1 244 LYS n 
1 245 LEU n 
1 246 LYS n 
1 247 SER n 
1 248 GLY n 
1 249 SER n 
1 250 GLN n 
1 251 CYS n 
1 252 GLY n 
1 253 HIS n 
1 254 GLY n 
1 255 ASP n 
1 256 CYS n 
1 257 CYS n 
1 258 GLU n 
1 259 GLN n 
1 260 CYS n 
1 261 LYS n 
1 262 PHE n 
1 263 SER n 
1 264 LYS n 
1 265 SER n 
1 266 GLY n 
1 267 THR n 
1 268 GLU n 
1 269 CYS n 
1 270 ARG n 
1 271 ALA n 
1 272 SER n 
1 273 MET n 
1 274 SER n 
1 275 GLU n 
1 276 CYS n 
1 277 ASP n 
1 278 PRO n 
1 279 ALA n 
1 280 GLU n 
1 281 HIS n 
1 282 CYS n 
1 283 THR n 
1 284 GLY n 
1 285 GLN n 
1 286 SER n 
1 287 SER n 
1 288 GLU n 
1 289 CYS n 
1 290 PRO n 
1 291 ALA n 
1 292 ASP n 
1 293 VAL n 
1 294 PHE n 
1 295 HIS n 
1 296 LYS n 
1 297 ASN n 
1 298 GLY n 
1 299 GLN n 
1 300 PRO n 
1 301 CYS n 
1 302 LEU n 
1 303 ASP n 
1 304 ASN n 
1 305 TYR n 
1 306 GLY n 
1 307 TYR n 
1 308 CYS n 
1 309 TYR n 
1 310 ASN n 
1 311 GLY n 
1 312 ASN n 
1 313 CYS n 
1 314 PRO n 
1 315 ILE n 
1 316 MET n 
1 317 TYR n 
1 318 HIS n 
1 319 GLN n 
1 320 CYS n 
1 321 TYR n 
1 322 ASP n 
1 323 LEU n 
1 324 PHE n 
1 325 GLY n 
1 326 ALA n 
1 327 ASP n 
1 328 VAL n 
1 329 TYR n 
1 330 GLU n 
1 331 ALA n 
1 332 GLU n 
1 333 ASP n 
1 334 SER n 
1 335 CYS n 
1 336 PHE n 
1 337 GLU n 
1 338 ARG n 
1 339 ASN n 
1 340 GLN n 
1 341 LYS n 
1 342 GLY n 
1 343 ASN n 
1 344 TYR n 
1 345 TYR n 
1 346 GLY n 
1 347 TYR n 
1 348 CYS n 
1 349 ARG n 
1 350 LYS n 
1 351 GLU n 
1 352 ASN n 
1 353 GLY n 
1 354 ASN n 
1 355 LYS n 
1 356 ILE n 
1 357 PRO n 
1 358 CYS n 
1 359 ALA n 
1 360 PRO n 
1 361 GLU n 
1 362 ASP n 
1 363 VAL n 
1 364 LYS n 
1 365 CYS n 
1 366 GLY n 
1 367 ARG n 
1 368 LEU n 
1 369 TYR n 
1 370 CYS n 
1 371 LYS n 
1 372 ASP n 
1 373 ASN n 
1 374 SER n 
1 375 PRO n 
1 376 GLY n 
1 377 GLN n 
1 378 ASN n 
1 379 ASN n 
1 380 PRO n 
1 381 CYS n 
1 382 LYS n 
1 383 MET n 
1 384 PHE n 
1 385 TYR n 
1 386 SER n 
1 387 ASN n 
1 388 GLU n 
1 389 ASP n 
1 390 GLU n 
1 391 HIS n 
1 392 LYS n 
1 393 GLY n 
1 394 MET n 
1 395 VAL n 
1 396 LEU n 
1 397 PRO n 
1 398 GLY n 
1 399 THR n 
1 400 LYS n 
1 401 CYS n 
1 402 ALA n 
1 403 ASP n 
1 404 GLY n 
1 405 LYS n 
1 406 VAL n 
1 407 CYS n 
1 408 SER n 
1 409 ASN n 
1 410 GLY n 
1 411 HIS n 
1 412 CYS n 
1 413 VAL n 
1 414 ASP n 
1 415 VAL n 
1 416 ALA n 
1 417 THR n 
1 418 ALA n 
1 419 TYR 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                'western diamondback rattlesnake' 
_entity_src_nat.pdbx_organism_scientific   'Crotalus atrox' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      8730 
_entity_src_nat.genus                      Crotalus 
_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                    Q90282_CROAT 
_struct_ref.pdbx_db_accession          Q90282 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;HQKYNPFRFVELFLVVDKAMVTKNNGDLDKIKTRMYEIVNTVNEIYRYMYIHVALVGLEIWSNEDKITVKPEAGYTLNAF
GEWRKTDLLTRKKHDNAQLLTAIDLDRVIGLAYVGSMCHPKRSTGIIQDYSEINLVVAVIMAHEMGHNLGINHDSGYCSC
GDYACIMRPEISPEPSTFFSNCSYFECWDFIMNHNPECILNEPLGTDIISPPVCGNELLEVGEECDCGTPENCQNECCDA
ATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVFHKNGQPCLDNYGYCYNGNCPIMYHQC
YDLFGADVYEAEDSCFERNQKGNYYGYCRKENGNKIPCAPEDVKCGRLYCKDNSPGQNNPCKMFYSNEDEHKGMVLPGTK
CADGKVCSNGHCVDVATAY
;
_struct_ref.pdbx_align_begin           191 
_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 2DW2 A 1 ? 419 ? Q90282 191 ? 609 ? 191 609 
2 1 2DW2 B 1 ? 419 ? Q90282 191 ? 609 ? 191 609 
# 
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 2DW2 VAL A 13 ? UNP Q90282 PHE 203 'SEE REMARK 999' 203 1 
2 2DW2 VAL B 13 ? UNP Q90282 PHE 203 'SEE REMARK 999' 203 2 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
BMA D-saccharide        . BETA-D-MANNOSE         ? 'C6 H12 O6'      180.156 
CA  non-polymer         . 'CALCIUM ION'          ? 'Ca 2'           40.078  
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
FUC saccharide          . ALPHA-L-FUCOSE         ? 'C6 H12 O5'      164.156 
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                  ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE             ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1' 147.195 
MAN D-saccharide        . ALPHA-D-MANNOSE        ? 'C6 H12 O6'      180.156 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE              ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'             ? 'Zn 2'           65.409  
# 
_exptl.entry_id          2DW2 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.74 
_exptl_crystal.density_percent_sol   55.13 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pdbx_details    
;4% n-propanol, 16.2% PEG8000, 0.18M calcium acetate, 0.09M sodium cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
;
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           90 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315' 
_diffrn_detector.pdbx_collection_date   2005-11-20 
_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                    'rotated-inclined double-crystal monochromator' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SPRING-8 BEAMLINE BL41XU' 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
_diffrn_source.pdbx_synchrotron_beamline   BL41XU 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0 
# 
_reflns.entry_id                     2DW2 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.d_resolution_high            2.7 
_reflns.d_resolution_low             50 
_reflns.number_all                   28047 
_reflns.number_obs                   26911 
_reflns.percent_possible_obs         95.9 
_reflns.pdbx_Rmerge_I_obs            0.085 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        10.1 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              3.4 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.7 
_reflns_shell.d_res_low              2.8 
_reflns_shell.percent_possible_all   82.5 
_reflns_shell.Rmerge_I_obs           0.231 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    5.5 
_reflns_shell.pdbx_redundancy        2.8 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      2313 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2DW2 
_refine.ls_d_res_high                            2.7 
_refine.ls_d_res_low                             50 
_refine.pdbx_ls_sigma_F                          0 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     28047 
_refine.ls_number_reflns_obs                     26907 
_refine.ls_number_reflns_R_free                  1334 
_refine.ls_percent_reflns_obs                    95.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_work                       0.199 
_refine.ls_R_factor_R_free                       0.26 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      2ERO 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            random 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.details                                  ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_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.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6438 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         234 
_refine_hist.number_atoms_solvent             151 
_refine_hist.number_atoms_total               6823 
_refine_hist.d_res_high                       2.7 
_refine_hist.d_res_low                        50 
# 
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 
c_bond_d           0.005 ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg        1.14  ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d 22.9  ? ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d 0.73  ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.d_res_high                       2.7 
_refine_ls_shell.d_res_low                        2.8 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.R_factor_R_work                  0.264 
_refine_ls_shell.percent_reflns_obs               81.7 
_refine_ls_shell.R_factor_R_free                  0.328 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             112 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                2276 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2DW2 
_struct.title                     'Crystal structure of VAP2 from Crotalus atrox venom (Form 2-5 crystal)' 
_struct.pdbx_descriptor           Catrocollastatin 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2DW2 
_struct_keywords.pdbx_keywords   'APOPTOSIS, TOXIN' 
_struct_keywords.text            'apoptotic toxin, SVMP, metalloproteinase, APOPTOSIS, TOXIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 2 ? 
D  N N 2 ? 
E  N N 3 ? 
F  N N 2 ? 
G  N N 4 ? 
H  N N 2 ? 
I  N N 4 ? 
J  N N 2 ? 
K  N N 5 ? 
L  N N 6 ? 
M  N N 7 ? 
N  N N 7 ? 
O  N N 7 ? 
P  N N 2 ? 
Q  N N 2 ? 
R  N N 3 ? 
S  N N 2 ? 
T  N N 4 ? 
U  N N 2 ? 
V  N N 4 ? 
W  N N 2 ? 
X  N N 5 ? 
Y  N N 6 ? 
Z  N N 7 ? 
AA N N 7 ? 
BA N N 7 ? 
CA N N 8 ? 
DA N N 8 ? 
# 
_struct_biol.id   1 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  ASP A 17  ? ASN A 24  ? ASP A 207 ASN A 214 1 ? 8  
HELX_P HELX_P2  2  ASP A 27  ? TYR A 46  ? ASP A 217 TYR A 236 1 ? 20 
HELX_P HELX_P3  3  GLU A 72  ? ASP A 87  ? GLU A 262 ASP A 277 1 ? 16 
HELX_P HELX_P4  4  LEU A 88  ? ARG A 91  ? LEU A 278 ARG A 281 5 ? 4  
HELX_P HELX_P5  5  ILE A 133 ? LEU A 149 ? ILE A 323 LEU A 339 1 ? 17 
HELX_P HELX_P6  6  SER A 180 ? HIS A 194 ? SER A 370 HIS A 384 1 ? 15 
HELX_P HELX_P7  7  PRO A 196 ? LEU A 200 ? PRO A 386 LEU A 390 5 ? 5  
HELX_P HELX_P8  8  LEU A 204 ? ILE A 208 ? LEU A 394 ILE A 398 5 ? 5  
HELX_P HELX_P9  9  ILE A 315 ? GLY A 325 ? ILE A 505 GLY A 515 1 ? 11 
HELX_P HELX_P10 10 GLU A 332 ? LYS A 341 ? GLU A 522 LYS A 531 5 ? 10 
HELX_P HELX_P11 11 ALA A 359 ? GLY A 366 ? ALA A 549 GLY A 556 5 ? 8  
HELX_P HELX_P12 12 ALA A 416 ? ALA A 418 ? ALA A 606 ALA A 608 5 ? 3  
HELX_P HELX_P13 13 ASP B 17  ? ASN B 24  ? ASP B 207 ASN B 214 1 ? 8  
HELX_P HELX_P14 14 ASP B 27  ? TYR B 46  ? ASP B 217 TYR B 236 1 ? 20 
HELX_P HELX_P15 15 GLU B 72  ? THR B 86  ? GLU B 262 THR B 276 1 ? 15 
HELX_P HELX_P16 16 ASP B 87  ? LYS B 92  ? ASP B 277 LYS B 282 1 ? 6  
HELX_P HELX_P17 17 ILE B 133 ? LEU B 149 ? ILE B 323 LEU B 339 1 ? 17 
HELX_P HELX_P18 18 SER B 180 ? HIS B 194 ? SER B 370 HIS B 384 1 ? 15 
HELX_P HELX_P19 19 PRO B 196 ? LEU B 200 ? PRO B 386 LEU B 390 5 ? 5  
HELX_P HELX_P20 20 ILE B 315 ? GLY B 325 ? ILE B 505 GLY B 515 1 ? 11 
HELX_P HELX_P21 21 GLU B 332 ? GLU B 337 ? GLU B 522 GLU B 527 1 ? 6  
HELX_P HELX_P22 22 ARG B 338 ? LYS B 341 ? ARG B 528 LYS B 531 5 ? 4  
HELX_P HELX_P23 23 ASP B 362 ? GLY B 366 ? ASP B 552 GLY B 556 5 ? 5  
HELX_P HELX_P24 24 ALA B 416 ? ALA B 418 ? ALA B 606 ALA B 608 5 ? 3  
# 
_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 118 SG  ? ? ? 1_555 A  CYS 198 SG  ? ? A CYS 308 A CYS 388 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf2  disulf ? ? A  CYS 158 SG  ? ? ? 1_555 A  CYS 182 SG  ? ? A CYS 348 A CYS 372 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf3  disulf ? ? A  CYS 160 SG  ? ? ? 1_555 A  CYS 165 SG  ? ? A CYS 350 A CYS 355 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf4  disulf ? ? A  CYS 214 SG  ? ? ? 1_555 A  CYS 243 SG  ? ? A CYS 404 A CYS 433 1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf5  disulf ? ? A  CYS 225 SG  ? ? ? 1_555 A  CYS 238 SG  ? ? A CYS 415 A CYS 428 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf6  disulf ? ? A  CYS 227 SG  ? ? ? 1_555 A  CYS 233 SG  ? ? A CYS 417 A CYS 423 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf7  disulf ? ? A  CYS 237 SG  ? ? ? 1_555 A  CYS 260 SG  ? ? A CYS 427 A CYS 450 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf8  disulf ? ? A  CYS 251 SG  ? ? ? 1_555 A  CYS 257 SG  ? ? A CYS 441 A CYS 447 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf9  disulf ? ? A  CYS 256 SG  ? ? ? 1_555 A  CYS 282 SG  ? ? A CYS 446 A CYS 472 1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf10 disulf ? ? A  CYS 269 SG  ? ? ? 1_555 A  CYS 289 SG  ? ? A CYS 459 A CYS 479 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf11 disulf ? ? A  CYS 276 SG  ? ? ? 1_555 A  CYS 308 SG  ? ? A CYS 466 A CYS 498 1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf12 disulf ? ? A  CYS 301 SG  ? ? ? 1_555 A  CYS 313 SG  ? ? A CYS 491 A CYS 503 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf13 disulf ? ? A  CYS 320 SG  ? ? ? 1_555 A  CYS 370 SG  ? ? A CYS 510 A CYS 560 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf14 disulf ? ? A  CYS 335 SG  ? ? ? 1_555 A  CYS 381 SG  ? ? A CYS 525 A CYS 571 1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf15 disulf ? ? A  CYS 348 SG  ? ? ? 1_555 A  CYS 358 SG  ? ? A CYS 538 A CYS 548 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf16 disulf ? ? A  CYS 365 SG  ? ? ? 1_555 A  CYS 407 SG  ? ? A CYS 555 A CYS 597 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf17 disulf ? ? A  CYS 401 SG  ? ? ? 1_555 A  CYS 412 SG  ? ? A CYS 591 A CYS 602 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf18 disulf ? ? B  CYS 118 SG  ? ? ? 1_555 B  CYS 198 SG  ? ? B CYS 308 B CYS 388 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf19 disulf ? ? B  CYS 158 SG  ? ? ? 1_555 B  CYS 182 SG  ? ? B CYS 348 B CYS 372 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf20 disulf ? ? B  CYS 160 SG  ? ? ? 1_555 B  CYS 165 SG  ? ? B CYS 350 B CYS 355 1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf21 disulf ? ? B  CYS 214 SG  ? ? ? 1_555 B  CYS 243 SG  ? ? B CYS 404 B CYS 433 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf22 disulf ? ? B  CYS 225 SG  ? ? ? 1_555 B  CYS 238 SG  ? ? B CYS 415 B CYS 428 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf23 disulf ? ? B  CYS 227 SG  ? ? ? 1_555 B  CYS 233 SG  ? ? B CYS 417 B CYS 423 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf24 disulf ? ? B  CYS 237 SG  ? ? ? 1_555 B  CYS 260 SG  ? ? B CYS 427 B CYS 450 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf25 disulf ? ? B  CYS 251 SG  ? ? ? 1_555 B  CYS 257 SG  ? ? B CYS 441 B CYS 447 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf26 disulf ? ? B  CYS 256 SG  ? ? ? 1_555 B  CYS 282 SG  ? ? B CYS 446 B CYS 472 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf27 disulf ? ? B  CYS 269 SG  ? ? ? 1_555 B  CYS 289 SG  ? ? B CYS 459 B CYS 479 1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf28 disulf ? ? B  CYS 276 SG  ? ? ? 1_555 B  CYS 308 SG  ? ? B CYS 466 B CYS 498 1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf29 disulf ? ? B  CYS 301 SG  ? ? ? 1_555 B  CYS 313 SG  ? ? B CYS 491 B CYS 503 1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf30 disulf ? ? B  CYS 320 SG  ? ? ? 1_555 B  CYS 370 SG  ? ? B CYS 510 B CYS 560 1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf31 disulf ? ? B  CYS 335 SG  ? ? ? 1_555 B  CYS 381 SG  ? ? B CYS 525 B CYS 571 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf32 disulf ? ? B  CYS 348 SG  ? ? ? 1_555 B  CYS 358 SG  ? ? B CYS 538 B CYS 548 1_555 ? ? ? ? ? ? ? 2.025 ? 
disulf33 disulf ? ? B  CYS 365 SG  ? ? ? 1_555 B  CYS 407 SG  ? ? B CYS 555 B CYS 597 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf34 disulf ? ? B  CYS 401 SG  ? ? ? 1_555 B  CYS 412 SG  ? ? B CYS 591 B CYS 602 1_555 ? ? ? ? ? ? ? 2.034 ? 
covale1  covale ? ? A  ASN 181 ND2 ? ? ? 1_555 C  NAG .   C1  ? ? A ASN 371 A NAG 801 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale2  covale ? ? B  ASN 181 ND2 ? ? ? 1_555 P  NAG .   C1  ? ? B ASN 371 B NAG 801 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale3  covale ? ? C  NAG .   O4  ? ? ? 1_555 D  NAG .   C1  ? ? A NAG 801 A NAG 802 1_555 ? ? ? ? ? ? ? 1.386 ? 
covale4  covale ? ? C  NAG .   O6  ? ? ? 1_555 K  FUC .   C1  ? ? A NAG 801 A FUC 809 1_555 ? ? ? ? ? ? ? 1.401 ? 
covale5  covale ? ? D  NAG .   O4  ? ? ? 1_555 E  BMA .   C1  ? ? A NAG 802 A BMA 803 1_555 ? ? ? ? ? ? ? 1.376 ? 
covale6  covale ? ? E  BMA .   O3  ? ? ? 1_555 G  MAN .   C1  ? ? A BMA 803 A MAN 805 1_555 ? ? ? ? ? ? ? 1.399 ? 
covale7  covale ? ? E  BMA .   O4  ? ? ? 1_555 F  NAG .   C1  ? ? A BMA 803 A NAG 804 1_555 ? ? ? ? ? ? ? 1.385 ? 
covale8  covale ? ? E  BMA .   O6  ? ? ? 1_555 I  MAN .   C1  ? ? A BMA 803 A MAN 807 1_555 ? ? ? ? ? ? ? 1.396 ? 
covale9  covale ? ? G  MAN .   O2  ? ? ? 1_555 H  NAG .   C1  ? ? A MAN 805 A NAG 806 1_555 ? ? ? ? ? ? ? 1.391 ? 
covale10 covale ? ? I  MAN .   O2  ? ? ? 1_555 J  NAG .   C1  ? ? A MAN 807 A NAG 808 1_555 ? ? ? ? ? ? ? 1.390 ? 
covale11 covale ? ? P  NAG .   O4  ? ? ? 1_555 Q  NAG .   C1  ? ? B NAG 801 B NAG 802 1_555 ? ? ? ? ? ? ? 1.381 ? 
covale12 covale ? ? P  NAG .   O6  ? ? ? 1_555 X  FUC .   C1  ? ? B NAG 801 B FUC 809 1_555 ? ? ? ? ? ? ? 1.406 ? 
covale13 covale ? ? Q  NAG .   O4  ? ? ? 1_555 R  BMA .   C1  ? ? B NAG 802 B BMA 803 1_555 ? ? ? ? ? ? ? 1.392 ? 
covale14 covale ? ? R  BMA .   O3  ? ? ? 1_555 T  MAN .   C1  ? ? B BMA 803 B MAN 805 1_555 ? ? ? ? ? ? ? 1.400 ? 
covale15 covale ? ? R  BMA .   O4  ? ? ? 1_555 S  NAG .   C1  ? ? B BMA 803 B NAG 804 1_555 ? ? ? ? ? ? ? 1.383 ? 
covale16 covale ? ? R  BMA .   O6  ? ? ? 1_555 V  MAN .   C1  ? ? B BMA 803 B MAN 807 1_555 ? ? ? ? ? ? ? 1.397 ? 
covale17 covale ? ? T  MAN .   O2  ? ? ? 1_555 U  NAG .   C1  ? ? B MAN 805 B NAG 806 1_555 ? ? ? ? ? ? ? 1.393 ? 
covale18 covale ? ? V  MAN .   O2  ? ? ? 1_555 W  NAG .   C1  ? ? B MAN 807 B NAG 808 1_555 ? ? ? ? ? ? ? 1.379 ? 
metalc1  metalc ? ? A  HIS 143 NE2 ? ? ? 1_555 L  ZN  .   ZN  ? ? A HIS 333 A ZN  700 1_555 ? ? ? ? ? ? ? 2.130 ? 
metalc2  metalc ? ? A  HIS 147 NE2 ? ? ? 1_555 L  ZN  .   ZN  ? ? A HIS 337 A ZN  700 1_555 ? ? ? ? ? ? ? 2.118 ? 
metalc3  metalc ? ? A  HIS 153 NE2 ? ? ? 1_555 L  ZN  .   ZN  ? ? A HIS 343 A ZN  700 1_555 ? ? ? ? ? ? ? 1.929 ? 
metalc4  metalc ? ? B  HIS 143 NE2 ? ? ? 1_555 Y  ZN  .   ZN  ? ? B HIS 333 B ZN  700 1_555 ? ? ? ? ? ? ? 2.029 ? 
metalc5  metalc ? ? B  HIS 147 NE2 ? ? ? 1_555 Y  ZN  .   ZN  ? ? B HIS 337 B ZN  700 1_555 ? ? ? ? ? ? ? 2.135 ? 
metalc6  metalc ? ? B  HIS 153 NE2 ? ? ? 1_555 Y  ZN  .   ZN  ? ? B HIS 343 B ZN  700 1_555 ? ? ? ? ? ? ? 1.967 ? 
metalc7  metalc ? ? L  ZN  .   ZN  ? ? ? 1_555 CA HOH .   O   ? ? A ZN  700 A HOH 153 1_555 ? ? ? ? ? ? ? 2.027 ? 
metalc8  metalc ? ? M  CA  .   CA  ? ? ? 1_555 A  GLU 11  OE1 ? ? A CA  701 A GLU 201 1_555 ? ? ? ? ? ? ? 2.130 ? 
metalc9  metalc ? ? M  CA  .   CA  ? ? ? 1_555 A  ASP 95  OD1 ? ? A CA  701 A ASP 285 1_555 ? ? ? ? ? ? ? 2.352 ? 
metalc10 metalc ? ? M  CA  .   CA  ? ? ? 1_555 A  ASP 95  OD2 ? ? A CA  701 A ASP 285 1_555 ? ? ? ? ? ? ? 2.668 ? 
metalc11 metalc ? ? M  CA  .   CA  ? ? ? 1_555 A  CYS 198 O   ? ? A CA  701 A CYS 388 1_555 ? ? ? ? ? ? ? 2.106 ? 
metalc12 metalc ? ? M  CA  .   CA  ? ? ? 1_555 A  ASN 201 ND2 ? ? A CA  701 A ASN 391 1_555 ? ? ? ? ? ? ? 2.412 ? 
metalc13 metalc ? ? M  CA  .   CA  ? ? ? 1_555 CA HOH .   O   ? ? A CA  701 A HOH 86  1_555 ? ? ? ? ? ? ? 2.501 ? 
metalc14 metalc ? ? M  CA  .   CA  ? ? ? 1_555 CA HOH .   O   ? ? A CA  701 A HOH 4   1_555 ? ? ? ? ? ? ? 2.130 ? 
metalc15 metalc ? ? M  CA  .   CA  ? ? ? 1_555 A  ASN 201 OD1 ? ? A CA  701 A ASN 391 1_555 ? ? ? ? ? ? ? 2.758 ? 
metalc16 metalc ? ? N  CA  .   CA  ? ? ? 1_555 A  VAL 213 O   ? ? A CA  702 A VAL 403 1_555 ? ? ? ? ? ? ? 2.305 ? 
metalc17 metalc ? ? N  CA  .   CA  ? ? ? 1_555 A  ASN 216 OD1 ? ? A CA  702 A ASN 406 1_555 ? ? ? ? ? ? ? 2.415 ? 
metalc18 metalc ? ? N  CA  .   CA  ? ? ? 1_555 A  GLU 220 OE1 ? ? A CA  702 A GLU 410 1_555 ? ? ? ? ? ? ? 2.310 ? 
metalc19 metalc ? ? N  CA  .   CA  ? ? ? 1_555 A  LEU 218 O   ? ? A CA  702 A LEU 408 1_555 ? ? ? ? ? ? ? 2.365 ? 
metalc20 metalc ? ? N  CA  .   CA  ? ? ? 1_555 A  GLU 223 OE1 ? ? A CA  702 A GLU 413 1_555 ? ? ? ? ? ? ? 2.511 ? 
metalc21 metalc ? ? N  CA  .   CA  ? ? ? 1_555 A  GLU 223 OE2 ? ? A CA  702 A GLU 413 1_555 ? ? ? ? ? ? ? 2.875 ? 
metalc22 metalc ? ? N  CA  .   CA  ? ? ? 1_555 A  ASP 226 OD2 ? ? A CA  702 A ASP 416 1_555 ? ? ? ? ? ? ? 2.382 ? 
metalc23 metalc ? ? O  CA  .   CA  ? ? ? 1_555 A  GLU 280 OE1 ? ? A CA  703 A GLU 470 1_555 ? ? ? ? ? ? ? 2.231 ? 
metalc24 metalc ? ? O  CA  .   CA  ? ? ? 1_555 A  PRO 278 O   ? ? A CA  703 A PRO 468 1_555 ? ? ? ? ? ? ? 2.400 ? 
metalc25 metalc ? ? O  CA  .   CA  ? ? ? 1_555 A  ASP 292 OD2 ? ? A CA  703 A ASP 482 1_555 ? ? ? ? ? ? ? 2.373 ? 
metalc26 metalc ? ? O  CA  .   CA  ? ? ? 1_555 A  GLU 280 OE2 ? ? A CA  703 A GLU 470 1_555 ? ? ? ? ? ? ? 2.698 ? 
metalc27 metalc ? ? O  CA  .   CA  ? ? ? 1_555 A  VAL 293 O   ? ? A CA  703 A VAL 483 1_555 ? ? ? ? ? ? ? 2.854 ? 
metalc28 metalc ? ? O  CA  .   CA  ? ? ? 1_555 A  ASP 277 OD2 ? ? A CA  703 A ASP 467 1_555 ? ? ? ? ? ? ? 2.462 ? 
metalc29 metalc ? ? Y  ZN  .   ZN  ? ? ? 1_555 DA HOH .   O   ? ? B ZN  700 B HOH 155 1_555 ? ? ? ? ? ? ? 2.163 ? 
metalc30 metalc ? ? Z  CA  .   CA  ? ? ? 1_555 B  ASP 95  OD2 ? ? B CA  711 B ASP 285 1_555 ? ? ? ? ? ? ? 2.644 ? 
metalc31 metalc ? ? Z  CA  .   CA  ? ? ? 1_555 B  ASN 201 OD1 ? ? B CA  711 B ASN 391 1_555 ? ? ? ? ? ? ? 3.040 ? 
metalc32 metalc ? ? Z  CA  .   CA  ? ? ? 1_555 B  ASP 95  OD1 ? ? B CA  711 B ASP 285 1_555 ? ? ? ? ? ? ? 2.401 ? 
metalc33 metalc ? ? Z  CA  .   CA  ? ? ? 1_555 B  GLU 11  OE1 ? ? B CA  711 B GLU 201 1_555 ? ? ? ? ? ? ? 2.358 ? 
metalc34 metalc ? ? Z  CA  .   CA  ? ? ? 1_555 B  CYS 198 O   ? ? B CA  711 B CYS 388 1_555 ? ? ? ? ? ? ? 2.405 ? 
metalc35 metalc ? ? Z  CA  .   CA  ? ? ? 1_555 B  ASN 201 ND2 ? ? B CA  711 B ASN 391 1_555 ? ? ? ? ? ? ? 2.347 ? 
metalc36 metalc ? ? AA CA  .   CA  ? ? ? 1_555 B  LEU 218 O   ? ? B CA  712 B LEU 408 1_555 ? ? ? ? ? ? ? 2.441 ? 
metalc37 metalc ? ? AA CA  .   CA  ? ? ? 1_555 B  ASP 226 OD2 ? ? B CA  712 B ASP 416 1_555 ? ? ? ? ? ? ? 2.263 ? 
metalc38 metalc ? ? AA CA  .   CA  ? ? ? 1_555 B  ASN 216 OD1 ? ? B CA  712 B ASN 406 1_555 ? ? ? ? ? ? ? 2.263 ? 
metalc39 metalc ? ? AA CA  .   CA  ? ? ? 1_555 B  VAL 213 O   ? ? B CA  712 B VAL 403 1_555 ? ? ? ? ? ? ? 2.355 ? 
metalc40 metalc ? ? AA CA  .   CA  ? ? ? 1_555 B  GLU 220 OE1 ? ? B CA  712 B GLU 410 1_555 ? ? ? ? ? ? ? 2.349 ? 
metalc41 metalc ? ? AA CA  .   CA  ? ? ? 1_555 B  GLU 223 OE1 ? ? B CA  712 B GLU 413 1_555 ? ? ? ? ? ? ? 2.457 ? 
metalc42 metalc ? ? AA CA  .   CA  ? ? ? 1_555 B  GLU 223 OE2 ? ? B CA  712 B GLU 413 1_555 ? ? ? ? ? ? ? 2.855 ? 
metalc43 metalc ? ? BA CA  .   CA  ? ? ? 1_555 B  VAL 293 O   ? ? B CA  713 B VAL 483 1_555 ? ? ? ? ? ? ? 2.581 ? 
metalc44 metalc ? ? BA CA  .   CA  ? ? ? 1_555 B  GLU 280 OE2 ? ? B CA  713 B GLU 470 1_555 ? ? ? ? ? ? ? 2.908 ? 
metalc45 metalc ? ? BA CA  .   CA  ? ? ? 1_555 B  PRO 278 O   ? ? B CA  713 B PRO 468 1_555 ? ? ? ? ? ? ? 2.319 ? 
metalc46 metalc ? ? BA CA  .   CA  ? ? ? 1_555 B  ASP 292 OD1 ? ? B CA  713 B ASP 482 1_555 ? ? ? ? ? ? ? 2.276 ? 
metalc47 metalc ? ? BA CA  .   CA  ? ? ? 1_555 B  GLU 280 OE1 ? ? B CA  713 B GLU 470 1_555 ? ? ? ? ? ? ? 2.354 ? 
metalc48 metalc ? ? BA CA  .   CA  ? ? ? 1_555 B  ASP 277 OD2 ? ? B CA  713 B ASP 467 1_555 ? ? ? ? ? ? ? 2.244 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 2 ? 
C ? 2 ? 
D ? 2 ? 
E ? 2 ? 
F ? 2 ? 
G ? 3 ? 
H ? 5 ? 
I ? 2 ? 
J ? 2 ? 
K ? 2 ? 
L ? 2 ? 
M ? 2 ? 
N ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? parallel      
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? anti-parallel 
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
D 1 2 ? anti-parallel 
E 1 2 ? anti-parallel 
F 1 2 ? anti-parallel 
G 1 2 ? anti-parallel 
G 2 3 ? anti-parallel 
H 1 2 ? parallel      
H 2 3 ? parallel      
H 3 4 ? parallel      
H 4 5 ? anti-parallel 
I 1 2 ? anti-parallel 
J 1 2 ? anti-parallel 
K 1 2 ? anti-parallel 
L 1 2 ? anti-parallel 
M 1 2 ? anti-parallel 
N 1 2 ? anti-parallel 
N 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ILE A 51  ? ILE A 60  ? ILE A 241 ILE A 250 
A 2 ARG A 8   ? VAL A 16  ? ARG A 198 VAL A 206 
A 3 ASN A 96  ? THR A 101 ? ASN A 286 THR A 291 
A 4 THR A 124 ? GLN A 128 ? THR A 314 GLN A 318 
A 5 GLY A 110 ? ALA A 112 ? GLY A 300 ALA A 302 
B 1 CYS A 257 ? GLU A 258 ? CYS A 447 GLU A 448 
B 2 LYS A 261 ? PHE A 262 ? LYS A 451 PHE A 452 
C 1 GLU A 268 ? ARG A 270 ? GLU A 458 ARG A 460 
C 2 GLU A 280 ? HIS A 281 ? GLU A 470 HIS A 471 
D 1 PRO A 300 ? CYS A 301 ? PRO A 490 CYS A 491 
D 2 GLY A 306 ? TYR A 307 ? GLY A 496 TYR A 497 
E 1 VAL A 328 ? GLU A 330 ? VAL A 518 GLU A 520 
E 2 CYS A 370 ? ASP A 372 ? CYS A 560 ASP A 562 
F 1 ARG A 349 ? GLU A 351 ? ARG A 539 GLU A 541 
F 2 ASN A 354 ? ILE A 356 ? ASN A 544 ILE A 546 
G 1 LYS A 400 ? ALA A 402 ? LYS A 590 ALA A 592 
G 2 LYS A 405 ? CYS A 407 ? LYS A 595 CYS A 597 
G 3 CYS A 412 ? ASP A 414 ? CYS A 602 ASP A 604 
H 1 ILE B 51  ? ILE B 60  ? ILE B 241 ILE B 250 
H 2 ARG B 8   ? VAL B 16  ? ARG B 198 VAL B 206 
H 3 ASN B 96  ? THR B 101 ? ASN B 286 THR B 291 
H 4 THR B 124 ? GLN B 128 ? THR B 314 GLN B 318 
H 5 GLY B 110 ? ALA B 112 ? GLY B 300 ALA B 302 
I 1 CYS B 257 ? GLU B 258 ? CYS B 447 GLU B 448 
I 2 LYS B 261 ? PHE B 262 ? LYS B 451 PHE B 452 
J 1 GLU B 268 ? ARG B 270 ? GLU B 458 ARG B 460 
J 2 GLU B 280 ? HIS B 281 ? GLU B 470 HIS B 471 
K 1 PRO B 300 ? CYS B 301 ? PRO B 490 CYS B 491 
K 2 GLY B 306 ? TYR B 307 ? GLY B 496 TYR B 497 
L 1 VAL B 328 ? GLU B 330 ? VAL B 518 GLU B 520 
L 2 CYS B 370 ? ASP B 372 ? CYS B 560 ASP B 562 
M 1 ARG B 349 ? GLU B 351 ? ARG B 539 GLU B 541 
M 2 ASN B 354 ? ILE B 356 ? ASN B 544 ILE B 546 
N 1 LYS B 400 ? ALA B 402 ? LYS B 590 ALA B 592 
N 2 LYS B 405 ? CYS B 407 ? LYS B 595 CYS B 597 
N 3 CYS B 412 ? ASP B 414 ? CYS B 602 ASP B 604 
# 
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 52  ? O HIS A 242 N ARG A 8   ? N ARG A 198 
A 2 3 N VAL A 15  ? N VAL A 205 O LEU A 100 ? O LEU A 290 
A 3 4 N THR A 101 ? N THR A 291 O ILE A 127 ? O ILE A 317 
A 4 5 O ILE A 126 ? O ILE A 316 N LEU A 111 ? N LEU A 301 
B 1 2 N GLU A 258 ? N GLU A 448 O LYS A 261 ? O LYS A 451 
C 1 2 N CYS A 269 ? N CYS A 459 O GLU A 280 ? O GLU A 470 
D 1 2 N CYS A 301 ? N CYS A 491 O GLY A 306 ? O GLY A 496 
E 1 2 N TYR A 329 ? N TYR A 519 O LYS A 371 ? O LYS A 561 
F 1 2 N ARG A 349 ? N ARG A 539 O ILE A 356 ? O ILE A 546 
G 1 2 N ALA A 402 ? N ALA A 592 O LYS A 405 ? O LYS A 595 
G 2 3 N VAL A 406 ? N VAL A 596 O VAL A 413 ? O VAL A 603 
H 1 2 O GLY B 57  ? O GLY B 247 N LEU B 14  ? N LEU B 204 
H 2 3 N VAL B 15  ? N VAL B 205 O LEU B 100 ? O LEU B 290 
H 3 4 N LEU B 99  ? N LEU B 289 O ILE B 127 ? O ILE B 317 
H 4 5 O ILE B 126 ? O ILE B 316 N LEU B 111 ? N LEU B 301 
I 1 2 N GLU B 258 ? N GLU B 448 O LYS B 261 ? O LYS B 451 
J 1 2 N CYS B 269 ? N CYS B 459 O GLU B 280 ? O GLU B 470 
K 1 2 N CYS B 301 ? N CYS B 491 O GLY B 306 ? O GLY B 496 
L 1 2 N TYR B 329 ? N TYR B 519 O LYS B 371 ? O LYS B 561 
M 1 2 N ARG B 349 ? N ARG B 539 O ILE B 356 ? O ILE B 546 
N 1 2 N ALA B 402 ? N ALA B 592 O LYS B 405 ? O LYS B 595 
N 2 3 N VAL B 406 ? N VAL B 596 O VAL B 413 ? O VAL B 603 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 801' 
AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 802' 
AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE BMA A 803' 
AC4 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 804' 
AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MAN A 805' 
AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 806' 
AC7 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MAN A 807' 
AC8 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 808' 
AC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE FUC A 809' 
BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG B 801' 
BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG B 802' 
BC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE BMA B 803' 
BC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG B 804' 
BC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MAN B 805' 
BC6 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG B 806' 
BC7 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE MAN B 807' 
BC8 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG B 808' 
BC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE FUC B 809' 
CC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 700'  
CC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA A 701'  
CC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA A 702'  
CC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 703'  
CC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 700'  
CC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CA B 711'  
CC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA B 712'  
CC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA B 713'  
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 6 TYR A  157 ? TYR A 347 . ? 1_555 ? 
2   AC1 6 SER A  159 ? SER A 349 . ? 1_555 ? 
3   AC1 6 ASN A  181 ? ASN A 371 . ? 1_555 ? 
4   AC1 6 PHE A  185 ? PHE A 375 . ? 1_555 ? 
5   AC1 6 NAG D  .   ? NAG A 802 . ? 1_555 ? 
6   AC1 6 FUC K  .   ? FUC A 809 . ? 1_555 ? 
7   AC2 5 HOH CA .   ? HOH A 131 . ? 1_555 ? 
8   AC2 5 TYR A  157 ? TYR A 347 . ? 1_555 ? 
9   AC2 5 NAG C  .   ? NAG A 801 . ? 1_555 ? 
10  AC2 5 BMA E  .   ? BMA A 803 . ? 1_555 ? 
11  AC2 5 FUC K  .   ? FUC A 809 . ? 1_555 ? 
12  AC3 5 TYR A  157 ? TYR A 347 . ? 1_555 ? 
13  AC3 5 NAG D  .   ? NAG A 802 . ? 1_555 ? 
14  AC3 5 NAG F  .   ? NAG A 804 . ? 1_555 ? 
15  AC3 5 MAN G  .   ? MAN A 805 . ? 1_555 ? 
16  AC3 5 MAN I  .   ? MAN A 807 . ? 1_555 ? 
17  AC4 8 HOH CA .   ? HOH A 89  . ? 1_555 ? 
18  AC4 8 TYR A  157 ? TYR A 347 . ? 1_555 ? 
19  AC4 8 BMA E  .   ? BMA A 803 . ? 1_555 ? 
20  AC4 8 MAN G  .   ? MAN A 805 . ? 1_555 ? 
21  AC4 8 NAG H  .   ? NAG A 806 . ? 1_555 ? 
22  AC4 8 GLY B  156 ? GLY B 346 . ? 1_554 ? 
23  AC4 8 TYR B  157 ? TYR B 347 . ? 1_554 ? 
24  AC4 8 ARG B  168 ? ARG B 358 . ? 1_554 ? 
25  AC5 6 BMA E  .   ? BMA A 803 . ? 1_555 ? 
26  AC5 6 NAG F  .   ? NAG A 804 . ? 1_555 ? 
27  AC5 6 NAG H  .   ? NAG A 806 . ? 1_555 ? 
28  AC5 6 MET B  273 ? MET B 463 . ? 1_555 ? 
29  AC5 6 SER B  274 ? SER B 464 . ? 1_555 ? 
30  AC5 6 GLU B  275 ? GLU B 465 . ? 1_555 ? 
31  AC6 6 HOH CA .   ? HOH A 89  . ? 1_555 ? 
32  AC6 6 NAG F  .   ? NAG A 804 . ? 1_555 ? 
33  AC6 6 MAN G  .   ? MAN A 805 . ? 1_555 ? 
34  AC6 6 PRO B  169 ? PRO B 359 . ? 1_554 ? 
35  AC6 6 GLU B  275 ? GLU B 465 . ? 1_555 ? 
36  AC6 6 LEU B  302 ? LEU B 492 . ? 1_555 ? 
37  AC7 2 BMA E  .   ? BMA A 803 . ? 1_555 ? 
38  AC7 2 NAG J  .   ? NAG A 808 . ? 1_555 ? 
39  AC8 2 HOH CA .   ? HOH A 131 . ? 1_555 ? 
40  AC8 2 MAN I  .   ? MAN A 807 . ? 1_555 ? 
41  AC9 3 SER A  159 ? SER A 349 . ? 1_555 ? 
42  AC9 3 NAG C  .   ? NAG A 801 . ? 1_555 ? 
43  AC9 3 NAG D  .   ? NAG A 802 . ? 1_555 ? 
44  BC1 5 TYR B  157 ? TYR B 347 . ? 1_555 ? 
45  BC1 5 ASN B  181 ? ASN B 371 . ? 1_555 ? 
46  BC1 5 PHE B  185 ? PHE B 375 . ? 1_555 ? 
47  BC1 5 NAG Q  .   ? NAG B 802 . ? 1_555 ? 
48  BC1 5 FUC X  .   ? FUC B 809 . ? 1_555 ? 
49  BC2 4 TYR B  157 ? TYR B 347 . ? 1_555 ? 
50  BC2 4 NAG P  .   ? NAG B 801 . ? 1_555 ? 
51  BC2 4 BMA R  .   ? BMA B 803 . ? 1_555 ? 
52  BC2 4 FUC X  .   ? FUC B 809 . ? 1_555 ? 
53  BC3 5 TYR B  157 ? TYR B 347 . ? 1_555 ? 
54  BC3 5 NAG Q  .   ? NAG B 802 . ? 1_555 ? 
55  BC3 5 NAG S  .   ? NAG B 804 . ? 1_555 ? 
56  BC3 5 MAN T  .   ? MAN B 805 . ? 1_555 ? 
57  BC3 5 MAN V  .   ? MAN B 807 . ? 1_555 ? 
58  BC4 6 GLY A  156 ? GLY A 346 . ? 1_556 ? 
59  BC4 6 TYR A  157 ? TYR A 347 . ? 1_556 ? 
60  BC4 6 ARG A  168 ? ARG A 358 . ? 1_556 ? 
61  BC4 6 BMA R  .   ? BMA B 803 . ? 1_555 ? 
62  BC4 6 MAN T  .   ? MAN B 805 . ? 1_555 ? 
63  BC4 6 NAG U  .   ? NAG B 806 . ? 1_555 ? 
64  BC5 6 MET A  273 ? MET A 463 . ? 1_555 ? 
65  BC5 6 SER A  274 ? SER A 464 . ? 1_555 ? 
66  BC5 6 GLU A  275 ? GLU A 465 . ? 1_555 ? 
67  BC5 6 BMA R  .   ? BMA B 803 . ? 1_555 ? 
68  BC5 6 NAG S  .   ? NAG B 804 . ? 1_555 ? 
69  BC5 6 NAG U  .   ? NAG B 806 . ? 1_555 ? 
70  BC6 7 HOH CA .   ? HOH A 67  . ? 1_556 ? 
71  BC6 7 PRO A  169 ? PRO A 359 . ? 1_556 ? 
72  BC6 7 GLU A  275 ? GLU A 465 . ? 1_555 ? 
73  BC6 7 LEU A  302 ? LEU A 492 . ? 1_555 ? 
74  BC6 7 ASP A  303 ? ASP A 493 . ? 1_555 ? 
75  BC6 7 NAG S  .   ? NAG B 804 . ? 1_555 ? 
76  BC6 7 MAN T  .   ? MAN B 805 . ? 1_555 ? 
77  BC7 3 HOH DA .   ? HOH B 123 . ? 1_555 ? 
78  BC7 3 BMA R  .   ? BMA B 803 . ? 1_555 ? 
79  BC7 3 NAG W  .   ? NAG B 808 . ? 1_555 ? 
80  BC8 1 MAN V  .   ? MAN B 807 . ? 1_555 ? 
81  BC9 3 SER B  159 ? SER B 349 . ? 1_555 ? 
82  BC9 3 NAG P  .   ? NAG B 801 . ? 1_555 ? 
83  BC9 3 NAG Q  .   ? NAG B 802 . ? 1_555 ? 
84  CC1 4 HOH CA .   ? HOH A 153 . ? 1_555 ? 
85  CC1 4 HIS A  143 ? HIS A 333 . ? 1_555 ? 
86  CC1 4 HIS A  147 ? HIS A 337 . ? 1_555 ? 
87  CC1 4 HIS A  153 ? HIS A 343 . ? 1_555 ? 
88  CC2 6 HOH CA .   ? HOH A 4   . ? 1_555 ? 
89  CC2 6 HOH CA .   ? HOH A 86  . ? 1_555 ? 
90  CC2 6 GLU A  11  ? GLU A 201 . ? 1_555 ? 
91  CC2 6 ASP A  95  ? ASP A 285 . ? 1_555 ? 
92  CC2 6 CYS A  198 ? CYS A 388 . ? 1_555 ? 
93  CC2 6 ASN A  201 ? ASN A 391 . ? 1_555 ? 
94  CC3 6 VAL A  213 ? VAL A 403 . ? 1_555 ? 
95  CC3 6 ASN A  216 ? ASN A 406 . ? 1_555 ? 
96  CC3 6 LEU A  218 ? LEU A 408 . ? 1_555 ? 
97  CC3 6 GLU A  220 ? GLU A 410 . ? 1_555 ? 
98  CC3 6 GLU A  223 ? GLU A 413 . ? 1_555 ? 
99  CC3 6 ASP A  226 ? ASP A 416 . ? 1_555 ? 
100 CC4 5 ASP A  277 ? ASP A 467 . ? 1_555 ? 
101 CC4 5 PRO A  278 ? PRO A 468 . ? 1_555 ? 
102 CC4 5 GLU A  280 ? GLU A 470 . ? 1_555 ? 
103 CC4 5 ASP A  292 ? ASP A 482 . ? 1_555 ? 
104 CC4 5 VAL A  293 ? VAL A 483 . ? 1_555 ? 
105 CC5 4 HOH DA .   ? HOH B 155 . ? 1_555 ? 
106 CC5 4 HIS B  143 ? HIS B 333 . ? 1_555 ? 
107 CC5 4 HIS B  147 ? HIS B 337 . ? 1_555 ? 
108 CC5 4 HIS B  153 ? HIS B 343 . ? 1_555 ? 
109 CC6 4 GLU B  11  ? GLU B 201 . ? 1_555 ? 
110 CC6 4 ASP B  95  ? ASP B 285 . ? 1_555 ? 
111 CC6 4 CYS B  198 ? CYS B 388 . ? 1_555 ? 
112 CC6 4 ASN B  201 ? ASN B 391 . ? 1_555 ? 
113 CC7 6 VAL B  213 ? VAL B 403 . ? 1_555 ? 
114 CC7 6 ASN B  216 ? ASN B 406 . ? 1_555 ? 
115 CC7 6 LEU B  218 ? LEU B 408 . ? 1_555 ? 
116 CC7 6 GLU B  220 ? GLU B 410 . ? 1_555 ? 
117 CC7 6 GLU B  223 ? GLU B 413 . ? 1_555 ? 
118 CC7 6 ASP B  226 ? ASP B 416 . ? 1_555 ? 
119 CC8 5 ASP B  277 ? ASP B 467 . ? 1_555 ? 
120 CC8 5 PRO B  278 ? PRO B 468 . ? 1_555 ? 
121 CC8 5 GLU B  280 ? GLU B 470 . ? 1_555 ? 
122 CC8 5 ASP B  292 ? ASP B 482 . ? 1_555 ? 
123 CC8 5 VAL B  293 ? VAL B 483 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2DW2 
_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                    2DW2 
_atom_sites.fract_transf_matrix[1][1]   0.004530 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000137 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012583 
_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]   0.017046 
_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  
CA 
N  
O  
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   . ASN A  1 5   ? 93.117  9.929   48.169 1.00 44.35 ? 195 ASN A N   1 
ATOM   2    C  CA  . ASN A  1 5   ? 93.042  9.275   46.828 1.00 47.75 ? 195 ASN A CA  1 
ATOM   3    C  C   . ASN A  1 5   ? 91.982  9.917   45.935 1.00 45.09 ? 195 ASN A C   1 
ATOM   4    O  O   . ASN A  1 5   ? 90.800  9.956   46.279 1.00 46.98 ? 195 ASN A O   1 
ATOM   5    C  CB  . ASN A  1 5   ? 92.745  7.780   46.982 1.00 50.41 ? 195 ASN A CB  1 
ATOM   6    C  CG  . ASN A  1 5   ? 92.426  7.110   45.656 1.00 53.57 ? 195 ASN A CG  1 
ATOM   7    O  OD1 . ASN A  1 5   ? 93.185  7.218   44.690 1.00 51.13 ? 195 ASN A OD1 1 
ATOM   8    N  ND2 . ASN A  1 5   ? 91.297  6.410   45.604 1.00 52.95 ? 195 ASN A ND2 1 
ATOM   9    N  N   . PRO A  1 6   ? 92.399  10.424  44.766 1.00 42.13 ? 196 PRO A N   1 
ATOM   10   C  CA  . PRO A  1 6   ? 91.500  11.074  43.807 1.00 39.72 ? 196 PRO A CA  1 
ATOM   11   C  C   . PRO A  1 6   ? 90.708  10.112  42.921 1.00 37.10 ? 196 PRO A C   1 
ATOM   12   O  O   . PRO A  1 6   ? 89.588  10.414  42.512 1.00 37.15 ? 196 PRO A O   1 
ATOM   13   C  CB  . PRO A  1 6   ? 92.454  11.944  42.998 1.00 39.36 ? 196 PRO A CB  1 
ATOM   14   C  CG  . PRO A  1 6   ? 93.676  11.080  42.924 1.00 35.56 ? 196 PRO A CG  1 
ATOM   15   C  CD  . PRO A  1 6   ? 93.805  10.552  44.338 1.00 36.64 ? 196 PRO A CD  1 
ATOM   16   N  N   . PHE A  1 7   ? 91.299  8.956   42.634 1.00 33.95 ? 197 PHE A N   1 
ATOM   17   C  CA  . PHE A  1 7   ? 90.684  7.941   41.780 1.00 27.41 ? 197 PHE A CA  1 
ATOM   18   C  C   . PHE A  1 7   ? 89.314  7.410   42.187 1.00 23.94 ? 197 PHE A C   1 
ATOM   19   O  O   . PHE A  1 7   ? 89.009  7.259   43.367 1.00 23.11 ? 197 PHE A O   1 
ATOM   20   C  CB  . PHE A  1 7   ? 91.638  6.758   41.627 1.00 22.80 ? 197 PHE A CB  1 
ATOM   21   C  CG  . PHE A  1 7   ? 92.608  6.909   40.502 1.00 18.74 ? 197 PHE A CG  1 
ATOM   22   C  CD1 . PHE A  1 7   ? 92.236  6.592   39.204 1.00 23.71 ? 197 PHE A CD1 1 
ATOM   23   C  CD2 . PHE A  1 7   ? 93.889  7.382   40.733 1.00 16.53 ? 197 PHE A CD2 1 
ATOM   24   C  CE1 . PHE A  1 7   ? 93.131  6.743   38.148 1.00 23.27 ? 197 PHE A CE1 1 
ATOM   25   C  CE2 . PHE A  1 7   ? 94.792  7.539   39.684 1.00 23.23 ? 197 PHE A CE2 1 
ATOM   26   C  CZ  . PHE A  1 7   ? 94.412  7.219   38.390 1.00 20.28 ? 197 PHE A CZ  1 
ATOM   27   N  N   . ARG A  1 8   ? 88.499  7.125   41.175 1.00 26.15 ? 198 ARG A N   1 
ATOM   28   C  CA  . ARG A  1 8   ? 87.161  6.572   41.353 1.00 21.80 ? 198 ARG A CA  1 
ATOM   29   C  C   . ARG A  1 8   ? 87.203  5.181   40.737 1.00 23.07 ? 198 ARG A C   1 
ATOM   30   O  O   . ARG A  1 8   ? 88.011  4.926   39.844 1.00 26.75 ? 198 ARG A O   1 
ATOM   31   C  CB  . ARG A  1 8   ? 86.126  7.423   40.623 1.00 22.19 ? 198 ARG A CB  1 
ATOM   32   C  CG  . ARG A  1 8   ? 85.802  8.738   41.304 1.00 26.67 ? 198 ARG A CG  1 
ATOM   33   C  CD  . ARG A  1 8   ? 85.097  8.508   42.630 1.00 23.29 ? 198 ARG A CD  1 
ATOM   34   N  NE  . ARG A  1 8   ? 84.542  9.745   43.177 1.00 26.02 ? 198 ARG A NE  1 
ATOM   35   C  CZ  . ARG A  1 8   ? 85.268  10.763  43.629 1.00 25.67 ? 198 ARG A CZ  1 
ATOM   36   N  NH1 . ARG A  1 8   ? 86.593  10.702  43.606 1.00 23.73 ? 198 ARG A NH1 1 
ATOM   37   N  NH2 . ARG A  1 8   ? 84.666  11.844  44.105 1.00 25.50 ? 198 ARG A NH2 1 
ATOM   38   N  N   . PHE A  1 9   ? 86.340  4.281   41.199 1.00 23.88 ? 199 PHE A N   1 
ATOM   39   C  CA  . PHE A  1 9   ? 86.344  2.924   40.668 1.00 20.75 ? 199 PHE A CA  1 
ATOM   40   C  C   . PHE A  1 9   ? 84.999  2.485   40.114 1.00 19.16 ? 199 PHE A C   1 
ATOM   41   O  O   . PHE A  1 9   ? 83.983  2.553   40.801 1.00 22.17 ? 199 PHE A O   1 
ATOM   42   C  CB  . PHE A  1 9   ? 86.791  1.933   41.751 1.00 15.08 ? 199 PHE A CB  1 
ATOM   43   C  CG  . PHE A  1 9   ? 88.066  2.321   42.440 1.00 17.12 ? 199 PHE A CG  1 
ATOM   44   C  CD1 . PHE A  1 9   ? 88.074  3.326   43.407 1.00 20.90 ? 199 PHE A CD1 1 
ATOM   45   C  CD2 . PHE A  1 9   ? 89.267  1.705   42.106 1.00 20.68 ? 199 PHE A CD2 1 
ATOM   46   C  CE1 . PHE A  1 9   ? 89.261  3.713   44.031 1.00 13.80 ? 199 PHE A CE1 1 
ATOM   47   C  CE2 . PHE A  1 9   ? 90.460  2.084   42.724 1.00 20.66 ? 199 PHE A CE2 1 
ATOM   48   C  CZ  . PHE A  1 9   ? 90.455  3.092   43.688 1.00 18.19 ? 199 PHE A CZ  1 
ATOM   49   N  N   . VAL A  1 10  ? 85.001  2.028   38.866 1.00 20.82 ? 200 VAL A N   1 
ATOM   50   C  CA  . VAL A  1 10  ? 83.780  1.554   38.228 1.00 20.30 ? 200 VAL A CA  1 
ATOM   51   C  C   . VAL A  1 10  ? 83.778  0.027   38.205 1.00 21.79 ? 200 VAL A C   1 
ATOM   52   O  O   . VAL A  1 10  ? 84.447  -0.596  37.377 1.00 18.42 ? 200 VAL A O   1 
ATOM   53   C  CB  . VAL A  1 10  ? 83.656  2.059   36.773 1.00 20.99 ? 200 VAL A CB  1 
ATOM   54   C  CG1 . VAL A  1 10  ? 82.283  1.691   36.219 1.00 24.16 ? 200 VAL A CG1 1 
ATOM   55   C  CG2 . VAL A  1 10  ? 83.867  3.561   36.715 1.00 18.67 ? 200 VAL A CG2 1 
ATOM   56   N  N   . GLU A  1 11  ? 83.037  -0.572  39.130 1.00 23.97 ? 201 GLU A N   1 
ATOM   57   C  CA  . GLU A  1 11  ? 82.946  -2.024  39.199 1.00 19.30 ? 201 GLU A CA  1 
ATOM   58   C  C   . GLU A  1 11  ? 81.999  -2.448  38.089 1.00 18.55 ? 201 GLU A C   1 
ATOM   59   O  O   . GLU A  1 11  ? 80.777  -2.321  38.206 1.00 13.58 ? 201 GLU A O   1 
ATOM   60   C  CB  . GLU A  1 11  ? 82.421  -2.457  40.568 1.00 17.61 ? 201 GLU A CB  1 
ATOM   61   C  CG  . GLU A  1 11  ? 83.358  -2.098  41.706 1.00 14.16 ? 201 GLU A CG  1 
ATOM   62   C  CD  . GLU A  1 11  ? 82.748  -2.348  43.069 1.00 24.33 ? 201 GLU A CD  1 
ATOM   63   O  OE1 . GLU A  1 11  ? 81.728  -1.703  43.393 1.00 22.28 ? 201 GLU A OE1 1 
ATOM   64   O  OE2 . GLU A  1 11  ? 83.286  -3.191  43.819 1.00 27.82 ? 201 GLU A OE2 1 
ATOM   65   N  N   . LEU A  1 12  ? 82.588  -2.948  37.009 1.00 15.31 ? 202 LEU A N   1 
ATOM   66   C  CA  . LEU A  1 12  ? 81.848  -3.361  35.825 1.00 14.02 ? 202 LEU A CA  1 
ATOM   67   C  C   . LEU A  1 12  ? 81.553  -4.851  35.677 1.00 15.50 ? 202 LEU A C   1 
ATOM   68   O  O   . LEU A  1 12  ? 82.310  -5.716  36.132 1.00 17.37 ? 202 LEU A O   1 
ATOM   69   C  CB  . LEU A  1 12  ? 82.605  -2.882  34.580 1.00 7.70  ? 202 LEU A CB  1 
ATOM   70   C  CG  . LEU A  1 12  ? 82.132  -3.343  33.202 1.00 5.97  ? 202 LEU A CG  1 
ATOM   71   C  CD1 . LEU A  1 12  ? 80.793  -2.714  32.887 1.00 4.83  ? 202 LEU A CD1 1 
ATOM   72   C  CD2 . LEU A  1 12  ? 83.163  -2.958  32.155 1.00 10.94 ? 202 LEU A CD2 1 
ATOM   73   N  N   . VAL A  1 13  ? 80.433  -5.127  35.020 1.00 13.45 ? 203 VAL A N   1 
ATOM   74   C  CA  . VAL A  1 13  ? 79.999  -6.482  34.722 1.00 15.66 ? 203 VAL A CA  1 
ATOM   75   C  C   . VAL A  1 13  ? 79.685  -6.480  33.227 1.00 17.32 ? 203 VAL A C   1 
ATOM   76   O  O   . VAL A  1 13  ? 78.969  -5.604  32.736 1.00 15.42 ? 203 VAL A O   1 
ATOM   77   C  CB  . VAL A  1 13  ? 78.722  -6.869  35.516 1.00 20.00 ? 203 VAL A CB  1 
ATOM   78   C  CG1 . VAL A  1 13  ? 78.196  -8.227  35.049 1.00 17.10 ? 203 VAL A CG1 1 
ATOM   79   C  CG2 . VAL A  1 13  ? 79.037  -6.918  37.000 1.00 22.42 ? 203 VAL A CG2 1 
ATOM   80   N  N   . LEU A  1 14  ? 80.251  -7.436  32.500 1.00 14.40 ? 204 LEU A N   1 
ATOM   81   C  CA  . LEU A  1 14  ? 80.011  -7.539  31.069 1.00 13.03 ? 204 LEU A CA  1 
ATOM   82   C  C   . LEU A  1 14  ? 79.115  -8.719  30.768 1.00 15.70 ? 204 LEU A C   1 
ATOM   83   O  O   . LEU A  1 14  ? 79.312  -9.816  31.294 1.00 12.68 ? 204 LEU A O   1 
ATOM   84   C  CB  . LEU A  1 14  ? 81.318  -7.724  30.301 1.00 14.49 ? 204 LEU A CB  1 
ATOM   85   C  CG  . LEU A  1 14  ? 82.122  -6.489  29.915 1.00 19.35 ? 204 LEU A CG  1 
ATOM   86   C  CD1 . LEU A  1 14  ? 83.397  -6.931  29.204 1.00 16.67 ? 204 LEU A CD1 1 
ATOM   87   C  CD2 . LEU A  1 14  ? 81.285  -5.590  29.015 1.00 8.85  ? 204 LEU A CD2 1 
ATOM   88   N  N   . VAL A  1 15  ? 78.129  -8.484  29.913 1.00 16.32 ? 205 VAL A N   1 
ATOM   89   C  CA  . VAL A  1 15  ? 77.212  -9.530  29.508 1.00 14.39 ? 205 VAL A CA  1 
ATOM   90   C  C   . VAL A  1 15  ? 77.405  -9.745  28.013 1.00 14.75 ? 205 VAL A C   1 
ATOM   91   O  O   . VAL A  1 15  ? 77.433  -8.789  27.235 1.00 12.92 ? 205 VAL A O   1 
ATOM   92   C  CB  . VAL A  1 15  ? 75.753  -9.134  29.799 1.00 15.71 ? 205 VAL A CB  1 
ATOM   93   C  CG1 . VAL A  1 15  ? 74.805  -10.238 29.336 1.00 9.61  ? 205 VAL A CG1 1 
ATOM   94   C  CG2 . VAL A  1 15  ? 75.583  -8.874  31.286 1.00 13.97 ? 205 VAL A CG2 1 
ATOM   95   N  N   . VAL A  1 16  ? 77.561  -11.004 27.624 1.00 16.24 ? 206 VAL A N   1 
ATOM   96   C  CA  . VAL A  1 16  ? 77.757  -11.362 26.225 1.00 17.60 ? 206 VAL A CA  1 
ATOM   97   C  C   . VAL A  1 16  ? 76.581  -12.212 25.745 1.00 16.23 ? 206 VAL A C   1 
ATOM   98   O  O   . VAL A  1 16  ? 76.290  -13.267 26.314 1.00 14.80 ? 206 VAL A O   1 
ATOM   99   C  CB  . VAL A  1 16  ? 79.081  -12.128 26.045 1.00 12.88 ? 206 VAL A CB  1 
ATOM   100  C  CG1 . VAL A  1 16  ? 79.260  -12.537 24.601 1.00 14.09 ? 206 VAL A CG1 1 
ATOM   101  C  CG2 . VAL A  1 16  ? 80.239  -11.251 26.481 1.00 2.21  ? 206 VAL A CG2 1 
ATOM   102  N  N   . ASP A  1 17  ? 75.911  -11.741 24.695 1.00 16.32 ? 207 ASP A N   1 
ATOM   103  C  CA  . ASP A  1 17  ? 74.741  -12.424 24.150 1.00 15.77 ? 207 ASP A CA  1 
ATOM   104  C  C   . ASP A  1 17  ? 75.062  -13.661 23.318 1.00 11.66 ? 207 ASP A C   1 
ATOM   105  O  O   . ASP A  1 17  ? 76.214  -13.935 23.003 1.00 10.46 ? 207 ASP A O   1 
ATOM   106  C  CB  . ASP A  1 17  ? 73.896  -11.439 23.327 1.00 17.85 ? 207 ASP A CB  1 
ATOM   107  C  CG  . ASP A  1 17  ? 74.533  -11.085 21.991 1.00 25.90 ? 207 ASP A CG  1 
ATOM   108  O  OD1 . ASP A  1 17  ? 75.773  -11.175 21.867 1.00 29.00 ? 207 ASP A OD1 1 
ATOM   109  O  OD2 . ASP A  1 17  ? 73.790  -10.701 21.063 1.00 25.56 ? 207 ASP A OD2 1 
ATOM   110  N  N   . LYS A  1 18  ? 74.019  -14.405 22.974 1.00 14.99 ? 208 LYS A N   1 
ATOM   111  C  CA  . LYS A  1 18  ? 74.143  -15.630 22.196 1.00 16.63 ? 208 LYS A CA  1 
ATOM   112  C  C   . LYS A  1 18  ? 74.819  -15.403 20.847 1.00 15.87 ? 208 LYS A C   1 
ATOM   113  O  O   . LYS A  1 18  ? 75.695  -16.173 20.445 1.00 17.54 ? 208 LYS A O   1 
ATOM   114  C  CB  . LYS A  1 18  ? 72.753  -16.247 21.992 1.00 15.51 ? 208 LYS A CB  1 
ATOM   115  C  CG  . LYS A  1 18  ? 72.748  -17.578 21.263 1.00 15.74 ? 208 LYS A CG  1 
ATOM   116  C  CD  . LYS A  1 18  ? 73.581  -18.623 21.986 1.00 20.94 ? 208 LYS A CD  1 
ATOM   117  C  CE  . LYS A  1 18  ? 73.418  -19.987 21.331 1.00 14.69 ? 208 LYS A CE  1 
ATOM   118  N  NZ  . LYS A  1 18  ? 71.978  -20.377 21.294 1.00 15.48 ? 208 LYS A NZ  1 
ATOM   119  N  N   . ALA A  1 19  ? 74.409  -14.348 20.149 1.00 12.17 ? 209 ALA A N   1 
ATOM   120  C  CA  . ALA A  1 19  ? 74.983  -14.030 18.845 1.00 11.13 ? 209 ALA A CA  1 
ATOM   121  C  C   . ALA A  1 19  ? 76.501  -13.996 18.949 1.00 6.34  ? 209 ALA A C   1 
ATOM   122  O  O   . ALA A  1 19  ? 77.205  -14.506 18.081 1.00 7.27  ? 209 ALA A O   1 
ATOM   123  C  CB  . ALA A  1 19  ? 74.464  -12.690 18.356 1.00 5.96  ? 209 ALA A CB  1 
ATOM   124  N  N   . MET A  1 20  ? 76.996  -13.387 20.020 1.00 8.89  ? 210 MET A N   1 
ATOM   125  C  CA  . MET A  1 20  ? 78.430  -13.295 20.248 1.00 11.86 ? 210 MET A CA  1 
ATOM   126  C  C   . MET A  1 20  ? 79.046  -14.678 20.348 1.00 11.79 ? 210 MET A C   1 
ATOM   127  O  O   . MET A  1 20  ? 80.120  -14.925 19.799 1.00 15.66 ? 210 MET A O   1 
ATOM   128  C  CB  . MET A  1 20  ? 78.718  -12.518 21.530 1.00 12.73 ? 210 MET A CB  1 
ATOM   129  C  CG  . MET A  1 20  ? 78.793  -11.022 21.338 1.00 13.20 ? 210 MET A CG  1 
ATOM   130  S  SD  . MET A  1 20  ? 80.181  -10.592 20.275 1.00 29.16 ? 210 MET A SD  1 
ATOM   131  C  CE  . MET A  1 20  ? 81.540  -10.653 21.465 1.00 12.71 ? 210 MET A CE  1 
ATOM   132  N  N   . VAL A  1 21  ? 78.364  -15.577 21.050 1.00 10.96 ? 211 VAL A N   1 
ATOM   133  C  CA  . VAL A  1 21  ? 78.859  -16.937 21.212 1.00 10.54 ? 211 VAL A CA  1 
ATOM   134  C  C   . VAL A  1 21  ? 78.903  -17.642 19.864 1.00 11.73 ? 211 VAL A C   1 
ATOM   135  O  O   . VAL A  1 21  ? 79.916  -18.246 19.507 1.00 11.66 ? 211 VAL A O   1 
ATOM   136  C  CB  . VAL A  1 21  ? 77.977  -17.737 22.180 1.00 9.74  ? 211 VAL A CB  1 
ATOM   137  C  CG1 . VAL A  1 21  ? 78.421  -19.194 22.211 1.00 4.06  ? 211 VAL A CG1 1 
ATOM   138  C  CG2 . VAL A  1 21  ? 78.071  -17.126 23.569 1.00 10.62 ? 211 VAL A CG2 1 
ATOM   139  N  N   . THR A  1 22  ? 77.805  -17.554 19.117 1.00 12.37 ? 212 THR A N   1 
ATOM   140  C  CA  . THR A  1 22  ? 77.731  -18.170 17.796 1.00 13.58 ? 212 THR A CA  1 
ATOM   141  C  C   . THR A  1 22  ? 78.834  -17.592 16.907 1.00 15.03 ? 212 THR A C   1 
ATOM   142  O  O   . THR A  1 22  ? 79.489  -18.316 16.156 1.00 14.57 ? 212 THR A O   1 
ATOM   143  C  CB  . THR A  1 22  ? 76.372  -17.898 17.130 1.00 10.32 ? 212 THR A CB  1 
ATOM   144  O  OG1 . THR A  1 22  ? 75.321  -18.309 18.011 1.00 16.63 ? 212 THR A OG1 1 
ATOM   145  C  CG2 . THR A  1 22  ? 76.255  -18.670 15.819 1.00 3.65  ? 212 THR A CG2 1 
ATOM   146  N  N   . LYS A  1 23  ? 79.034  -16.281 17.005 1.00 12.32 ? 213 LYS A N   1 
ATOM   147  C  CA  . LYS A  1 23  ? 80.057  -15.609 16.220 1.00 15.95 ? 213 LYS A CA  1 
ATOM   148  C  C   . LYS A  1 23  ? 81.434  -16.204 16.493 1.00 17.12 ? 213 LYS A C   1 
ATOM   149  O  O   . LYS A  1 23  ? 82.258  -16.323 15.588 1.00 14.06 ? 213 LYS A O   1 
ATOM   150  C  CB  . LYS A  1 23  ? 80.079  -14.110 16.541 1.00 11.25 ? 213 LYS A CB  1 
ATOM   151  C  CG  . LYS A  1 23  ? 81.080  -13.314 15.705 1.00 6.77  ? 213 LYS A CG  1 
ATOM   152  C  CD  . LYS A  1 23  ? 80.989  -11.827 16.019 1.00 11.99 ? 213 LYS A CD  1 
ATOM   153  C  CE  . LYS A  1 23  ? 81.772  -10.983 15.024 1.00 6.65  ? 213 LYS A CE  1 
ATOM   154  N  NZ  . LYS A  1 23  ? 81.579  -9.522  15.265 1.00 1.00  ? 213 LYS A NZ  1 
ATOM   155  N  N   . ASN A  1 24  ? 81.677  -16.584 17.742 1.00 13.78 ? 214 ASN A N   1 
ATOM   156  C  CA  . ASN A  1 24  ? 82.967  -17.142 18.116 1.00 14.58 ? 214 ASN A CA  1 
ATOM   157  C  C   . ASN A  1 24  ? 82.998  -18.664 18.153 1.00 19.95 ? 214 ASN A C   1 
ATOM   158  O  O   . ASN A  1 24  ? 83.810  -19.268 18.862 1.00 23.86 ? 214 ASN A O   1 
ATOM   159  C  CB  . ASN A  1 24  ? 83.403  -16.559 19.455 1.00 7.83  ? 214 ASN A CB  1 
ATOM   160  C  CG  . ASN A  1 24  ? 83.825  -15.113 19.337 1.00 7.53  ? 214 ASN A CG  1 
ATOM   161  O  OD1 . ASN A  1 24  ? 85.014  -14.805 19.325 1.00 8.07  ? 214 ASN A OD1 1 
ATOM   162  N  ND2 . ASN A  1 24  ? 82.850  -14.215 19.224 1.00 5.45  ? 214 ASN A ND2 1 
ATOM   163  N  N   . ASN A  1 25  ? 82.103  -19.274 17.382 1.00 15.36 ? 215 ASN A N   1 
ATOM   164  C  CA  . ASN A  1 25  ? 82.026  -20.724 17.267 1.00 11.44 ? 215 ASN A CA  1 
ATOM   165  C  C   . ASN A  1 25  ? 81.925  -21.480 18.586 1.00 11.91 ? 215 ASN A C   1 
ATOM   166  O  O   . ASN A  1 25  ? 82.370  -22.619 18.683 1.00 10.58 ? 215 ASN A O   1 
ATOM   167  C  CB  . ASN A  1 25  ? 83.236  -21.224 16.483 1.00 11.25 ? 215 ASN A CB  1 
ATOM   168  C  CG  . ASN A  1 25  ? 83.489  -20.406 15.231 1.00 12.55 ? 215 ASN A CG  1 
ATOM   169  O  OD1 . ASN A  1 25  ? 82.646  -20.344 14.335 1.00 11.85 ? 215 ASN A OD1 1 
ATOM   170  N  ND2 . ASN A  1 25  ? 84.653  -19.763 15.166 1.00 15.15 ? 215 ASN A ND2 1 
ATOM   171  N  N   . GLY A  1 26  ? 81.343  -20.843 19.597 1.00 14.86 ? 216 GLY A N   1 
ATOM   172  C  CA  . GLY A  1 26  ? 81.179  -21.489 20.888 1.00 15.96 ? 216 GLY A CA  1 
ATOM   173  C  C   . GLY A  1 26  ? 82.401  -21.553 21.786 1.00 21.47 ? 216 GLY A C   1 
ATOM   174  O  O   . GLY A  1 26  ? 82.352  -22.164 22.854 1.00 30.02 ? 216 GLY A O   1 
ATOM   175  N  N   . ASP A  1 27  ? 83.494  -20.920 21.372 1.00 21.95 ? 217 ASP A N   1 
ATOM   176  C  CA  . ASP A  1 27  ? 84.725  -20.930 22.158 1.00 21.17 ? 217 ASP A CA  1 
ATOM   177  C  C   . ASP A  1 27  ? 84.689  -19.877 23.273 1.00 20.10 ? 217 ASP A C   1 
ATOM   178  O  O   . ASP A  1 27  ? 85.220  -18.777 23.120 1.00 15.93 ? 217 ASP A O   1 
ATOM   179  C  CB  . ASP A  1 27  ? 85.921  -20.683 21.234 1.00 20.45 ? 217 ASP A CB  1 
ATOM   180  C  CG  . ASP A  1 27  ? 87.250  -20.845 21.940 1.00 24.50 ? 217 ASP A CG  1 
ATOM   181  O  OD1 . ASP A  1 27  ? 88.291  -20.646 21.279 1.00 32.05 ? 217 ASP A OD1 1 
ATOM   182  O  OD2 . ASP A  1 27  ? 87.259  -21.172 23.148 1.00 23.76 ? 217 ASP A OD2 1 
ATOM   183  N  N   . LEU A  1 28  ? 84.069  -20.234 24.395 1.00 19.41 ? 218 LEU A N   1 
ATOM   184  C  CA  . LEU A  1 28  ? 83.931  -19.337 25.542 1.00 17.50 ? 218 LEU A CA  1 
ATOM   185  C  C   . LEU A  1 28  ? 85.269  -18.840 26.074 1.00 18.57 ? 218 LEU A C   1 
ATOM   186  O  O   . LEU A  1 28  ? 85.403  -17.681 26.474 1.00 16.19 ? 218 LEU A O   1 
ATOM   187  C  CB  . LEU A  1 28  ? 83.172  -20.044 26.665 1.00 16.55 ? 218 LEU A CB  1 
ATOM   188  C  CG  . LEU A  1 28  ? 81.907  -20.813 26.265 1.00 13.43 ? 218 LEU A CG  1 
ATOM   189  C  CD1 . LEU A  1 28  ? 81.165  -21.204 27.526 1.00 6.91  ? 218 LEU A CD1 1 
ATOM   190  C  CD2 . LEU A  1 28  ? 81.016  -19.965 25.373 1.00 6.81  ? 218 LEU A CD2 1 
ATOM   191  N  N   . ASP A  1 29  ? 86.254  -19.730 26.085 1.00 22.06 ? 219 ASP A N   1 
ATOM   192  C  CA  . ASP A  1 29  ? 87.589  -19.400 26.561 1.00 23.14 ? 219 ASP A CA  1 
ATOM   193  C  C   . ASP A  1 29  ? 88.166  -18.229 25.770 1.00 21.87 ? 219 ASP A C   1 
ATOM   194  O  O   . ASP A  1 29  ? 88.817  -17.344 26.329 1.00 17.15 ? 219 ASP A O   1 
ATOM   195  C  CB  . ASP A  1 29  ? 88.502  -20.617 26.419 1.00 29.46 ? 219 ASP A CB  1 
ATOM   196  C  CG  . ASP A  1 29  ? 89.963  -20.276 26.632 1.00 44.50 ? 219 ASP A CG  1 
ATOM   197  O  OD1 . ASP A  1 29  ? 90.330  -19.890 27.765 1.00 49.36 ? 219 ASP A OD1 1 
ATOM   198  O  OD2 . ASP A  1 29  ? 90.744  -20.388 25.662 1.00 51.46 ? 219 ASP A OD2 1 
ATOM   199  N  N   . LYS A  1 30  ? 87.922  -18.238 24.463 1.00 21.10 ? 220 LYS A N   1 
ATOM   200  C  CA  . LYS A  1 30  ? 88.406  -17.190 23.578 1.00 16.60 ? 220 LYS A CA  1 
ATOM   201  C  C   . LYS A  1 30  ? 87.670  -15.896 23.907 1.00 18.35 ? 220 LYS A C   1 
ATOM   202  O  O   . LYS A  1 30  ? 88.269  -14.820 23.950 1.00 19.71 ? 220 LYS A O   1 
ATOM   203  C  CB  . LYS A  1 30  ? 88.148  -17.572 22.119 1.00 16.07 ? 220 LYS A CB  1 
ATOM   204  C  CG  . LYS A  1 30  ? 89.203  -17.062 21.160 1.00 23.13 ? 220 LYS A CG  1 
ATOM   205  C  CD  . LYS A  1 30  ? 88.732  -17.107 19.721 1.00 25.18 ? 220 LYS A CD  1 
ATOM   206  C  CE  . LYS A  1 30  ? 87.671  -16.051 19.468 1.00 30.57 ? 220 LYS A CE  1 
ATOM   207  N  NZ  . LYS A  1 30  ? 87.323  -15.952 18.020 1.00 35.99 ? 220 LYS A NZ  1 
ATOM   208  N  N   . ILE A  1 31  ? 86.366  -16.010 24.141 1.00 13.96 ? 221 ILE A N   1 
ATOM   209  C  CA  . ILE A  1 31  ? 85.544  -14.857 24.476 1.00 14.76 ? 221 ILE A CA  1 
ATOM   210  C  C   . ILE A  1 31  ? 86.010  -14.208 25.774 1.00 17.79 ? 221 ILE A C   1 
ATOM   211  O  O   . ILE A  1 31  ? 86.193  -12.992 25.839 1.00 20.96 ? 221 ILE A O   1 
ATOM   212  C  CB  . ILE A  1 31  ? 84.054  -15.253 24.622 1.00 15.67 ? 221 ILE A CB  1 
ATOM   213  C  CG1 . ILE A  1 31  ? 83.482  -15.626 23.251 1.00 13.67 ? 221 ILE A CG1 1 
ATOM   214  C  CG2 . ILE A  1 31  ? 83.261  -14.112 25.256 1.00 8.59  ? 221 ILE A CG2 1 
ATOM   215  C  CD1 . ILE A  1 31  ? 81.989  -15.921 23.261 1.00 14.35 ? 221 ILE A CD1 1 
ATOM   216  N  N   . LYS A  1 32  ? 86.203  -15.023 26.805 1.00 16.89 ? 222 LYS A N   1 
ATOM   217  C  CA  . LYS A  1 32  ? 86.639  -14.515 28.099 1.00 15.71 ? 222 LYS A CA  1 
ATOM   218  C  C   . LYS A  1 32  ? 87.999  -13.838 28.008 1.00 17.35 ? 222 LYS A C   1 
ATOM   219  O  O   . LYS A  1 32  ? 88.194  -12.735 28.525 1.00 13.94 ? 222 LYS A O   1 
ATOM   220  C  CB  . LYS A  1 32  ? 86.704  -15.650 29.116 1.00 14.78 ? 222 LYS A CB  1 
ATOM   221  C  CG  . LYS A  1 32  ? 85.402  -16.402 29.281 1.00 15.17 ? 222 LYS A CG  1 
ATOM   222  C  CD  . LYS A  1 32  ? 85.544  -17.503 30.317 1.00 14.69 ? 222 LYS A CD  1 
ATOM   223  C  CE  . LYS A  1 32  ? 84.299  -18.356 30.386 1.00 13.51 ? 222 LYS A CE  1 
ATOM   224  N  NZ  . LYS A  1 32  ? 84.423  -19.367 31.464 1.00 25.76 ? 222 LYS A NZ  1 
ATOM   225  N  N   . THR A  1 33  ? 88.939  -14.503 27.350 1.00 17.83 ? 223 THR A N   1 
ATOM   226  C  CA  . THR A  1 33  ? 90.278  -13.951 27.204 1.00 20.89 ? 223 THR A CA  1 
ATOM   227  C  C   . THR A  1 33  ? 90.218  -12.578 26.552 1.00 16.73 ? 223 THR A C   1 
ATOM   228  O  O   . THR A  1 33  ? 90.867  -11.641 27.006 1.00 15.11 ? 223 THR A O   1 
ATOM   229  C  CB  . THR A  1 33  ? 91.172  -14.869 26.353 1.00 21.95 ? 223 THR A CB  1 
ATOM   230  O  OG1 . THR A  1 33  ? 91.298  -16.139 27.002 1.00 30.85 ? 223 THR A OG1 1 
ATOM   231  C  CG2 . THR A  1 33  ? 92.552  -14.258 26.182 1.00 12.89 ? 223 THR A CG2 1 
ATOM   232  N  N   . ARG A  1 34  ? 89.428  -12.463 25.490 1.00 16.49 ? 224 ARG A N   1 
ATOM   233  C  CA  . ARG A  1 34  ? 89.298  -11.199 24.784 1.00 16.59 ? 224 ARG A CA  1 
ATOM   234  C  C   . ARG A  1 34  ? 88.638  -10.127 25.655 1.00 18.89 ? 224 ARG A C   1 
ATOM   235  O  O   . ARG A  1 34  ? 89.075  -8.978  25.666 1.00 18.09 ? 224 ARG A O   1 
ATOM   236  C  CB  . ARG A  1 34  ? 88.491  -11.385 23.498 1.00 17.68 ? 224 ARG A CB  1 
ATOM   237  C  CG  . ARG A  1 34  ? 88.620  -10.204 22.561 1.00 17.38 ? 224 ARG A CG  1 
ATOM   238  C  CD  . ARG A  1 34  ? 87.700  -10.279 21.360 1.00 13.28 ? 224 ARG A CD  1 
ATOM   239  N  NE  . ARG A  1 34  ? 87.856  -9.080  20.540 1.00 16.73 ? 224 ARG A NE  1 
ATOM   240  C  CZ  . ARG A  1 34  ? 86.964  -8.648  19.657 1.00 13.69 ? 224 ARG A CZ  1 
ATOM   241  N  NH1 . ARG A  1 34  ? 85.837  -9.316  19.467 1.00 20.20 ? 224 ARG A NH1 1 
ATOM   242  N  NH2 . ARG A  1 34  ? 87.198  -7.538  18.973 1.00 18.91 ? 224 ARG A NH2 1 
ATOM   243  N  N   . MET A  1 35  ? 87.586  -10.502 26.379 1.00 17.20 ? 225 MET A N   1 
ATOM   244  C  CA  . MET A  1 35  ? 86.891  -9.559  27.249 1.00 14.63 ? 225 MET A CA  1 
ATOM   245  C  C   . MET A  1 35  ? 87.847  -8.999  28.289 1.00 13.29 ? 225 MET A C   1 
ATOM   246  O  O   . MET A  1 35  ? 87.796  -7.814  28.611 1.00 15.49 ? 225 MET A O   1 
ATOM   247  C  CB  . MET A  1 35  ? 85.720  -10.232 27.966 1.00 13.58 ? 225 MET A CB  1 
ATOM   248  C  CG  . MET A  1 35  ? 84.622  -10.725 27.050 1.00 20.15 ? 225 MET A CG  1 
ATOM   249  S  SD  . MET A  1 35  ? 83.994  -9.437  25.965 1.00 18.23 ? 225 MET A SD  1 
ATOM   250  C  CE  . MET A  1 35  ? 84.569  -10.052 24.402 1.00 24.38 ? 225 MET A CE  1 
ATOM   251  N  N   . TYR A  1 36  ? 88.714  -9.856  28.817 1.00 11.84 ? 226 TYR A N   1 
ATOM   252  C  CA  . TYR A  1 36  ? 89.679  -9.424  29.823 1.00 13.65 ? 226 TYR A CA  1 
ATOM   253  C  C   . TYR A  1 36  ? 90.578  -8.336  29.253 1.00 14.22 ? 226 TYR A C   1 
ATOM   254  O  O   . TYR A  1 36  ? 90.782  -7.296  29.877 1.00 16.03 ? 226 TYR A O   1 
ATOM   255  C  CB  . TYR A  1 36  ? 90.544  -10.598 30.280 1.00 8.42  ? 226 TYR A CB  1 
ATOM   256  C  CG  . TYR A  1 36  ? 89.777  -11.746 30.892 1.00 18.05 ? 226 TYR A CG  1 
ATOM   257  C  CD1 . TYR A  1 36  ? 90.351  -13.014 30.979 1.00 16.36 ? 226 TYR A CD1 1 
ATOM   258  C  CD2 . TYR A  1 36  ? 88.474  -11.579 31.364 1.00 12.39 ? 226 TYR A CD2 1 
ATOM   259  C  CE1 . TYR A  1 36  ? 89.650  -14.086 31.512 1.00 13.82 ? 226 TYR A CE1 1 
ATOM   260  C  CE2 . TYR A  1 36  ? 87.765  -12.649 31.902 1.00 13.84 ? 226 TYR A CE2 1 
ATOM   261  C  CZ  . TYR A  1 36  ? 88.361  -13.902 31.969 1.00 15.07 ? 226 TYR A CZ  1 
ATOM   262  O  OH  . TYR A  1 36  ? 87.669  -14.981 32.471 1.00 15.49 ? 226 TYR A OH  1 
ATOM   263  N  N   . GLU A  1 37  ? 91.108  -8.576  28.060 1.00 15.61 ? 227 GLU A N   1 
ATOM   264  C  CA  . GLU A  1 37  ? 91.989  -7.609  27.427 1.00 23.10 ? 227 GLU A CA  1 
ATOM   265  C  C   . GLU A  1 37  ? 91.292  -6.286  27.142 1.00 20.22 ? 227 GLU A C   1 
ATOM   266  O  O   . GLU A  1 37  ? 91.860  -5.216  27.358 1.00 21.26 ? 227 GLU A O   1 
ATOM   267  C  CB  . GLU A  1 37  ? 92.551  -8.168  26.121 1.00 29.93 ? 227 GLU A CB  1 
ATOM   268  C  CG  . GLU A  1 37  ? 93.514  -7.206  25.441 1.00 48.32 ? 227 GLU A CG  1 
ATOM   269  C  CD  . GLU A  1 37  ? 94.037  -7.730  24.123 1.00 57.38 ? 227 GLU A CD  1 
ATOM   270  O  OE1 . GLU A  1 37  ? 94.583  -8.855  24.109 1.00 63.57 ? 227 GLU A OE1 1 
ATOM   271  O  OE2 . GLU A  1 37  ? 93.906  -7.014  23.106 1.00 57.07 ? 227 GLU A OE2 1 
ATOM   272  N  N   . ILE A  1 38  ? 90.060  -6.364  26.653 1.00 15.15 ? 228 ILE A N   1 
ATOM   273  C  CA  . ILE A  1 38  ? 89.300  -5.171  26.322 1.00 12.34 ? 228 ILE A CA  1 
ATOM   274  C  C   . ILE A  1 38  ? 89.055  -4.296  27.547 1.00 9.81  ? 228 ILE A C   1 
ATOM   275  O  O   . ILE A  1 38  ? 89.288  -3.089  27.507 1.00 2.40  ? 228 ILE A O   1 
ATOM   276  C  CB  . ILE A  1 38  ? 87.959  -5.554  25.644 1.00 14.15 ? 228 ILE A CB  1 
ATOM   277  C  CG1 . ILE A  1 38  ? 88.253  -6.183  24.277 1.00 5.56  ? 228 ILE A CG1 1 
ATOM   278  C  CG2 . ILE A  1 38  ? 87.059  -4.329  25.494 1.00 7.48  ? 228 ILE A CG2 1 
ATOM   279  C  CD1 . ILE A  1 38  ? 87.021  -6.663  23.544 1.00 9.47  ? 228 ILE A CD1 1 
ATOM   280  N  N   . VAL A  1 39  ? 88.596  -4.903  28.636 1.00 14.64 ? 229 VAL A N   1 
ATOM   281  C  CA  . VAL A  1 39  ? 88.339  -4.153  29.861 1.00 14.97 ? 229 VAL A CA  1 
ATOM   282  C  C   . VAL A  1 39  ? 89.652  -3.598  30.417 1.00 16.00 ? 229 VAL A C   1 
ATOM   283  O  O   . VAL A  1 39  ? 89.658  -2.589  31.121 1.00 16.53 ? 229 VAL A O   1 
ATOM   284  C  CB  . VAL A  1 39  ? 87.669  -5.039  30.934 1.00 17.56 ? 229 VAL A CB  1 
ATOM   285  C  CG1 . VAL A  1 39  ? 87.348  -4.208  32.171 1.00 17.58 ? 229 VAL A CG1 1 
ATOM   286  C  CG2 . VAL A  1 39  ? 86.402  -5.663  30.373 1.00 13.95 ? 229 VAL A CG2 1 
ATOM   287  N  N   . ASN A  1 40  ? 90.763  -4.259  30.096 1.00 13.67 ? 230 ASN A N   1 
ATOM   288  C  CA  . ASN A  1 40  ? 92.074  -3.807  30.553 1.00 12.96 ? 230 ASN A CA  1 
ATOM   289  C  C   . ASN A  1 40  ? 92.482  -2.550  29.795 1.00 15.86 ? 230 ASN A C   1 
ATOM   290  O  O   . ASN A  1 40  ? 93.172  -1.683  30.335 1.00 19.67 ? 230 ASN A O   1 
ATOM   291  C  CB  . ASN A  1 40  ? 93.120  -4.907  30.356 1.00 19.15 ? 230 ASN A CB  1 
ATOM   292  C  CG  . ASN A  1 40  ? 94.546  -4.391  30.473 1.00 23.95 ? 230 ASN A CG  1 
ATOM   293  O  OD1 . ASN A  1 40  ? 95.118  -3.876  29.507 1.00 21.49 ? 230 ASN A OD1 1 
ATOM   294  N  ND2 . ASN A  1 40  ? 95.124  -4.518  31.662 1.00 27.40 ? 230 ASN A ND2 1 
ATOM   295  N  N   . THR A  1 41  ? 92.049  -2.452  28.543 1.00 16.53 ? 231 THR A N   1 
ATOM   296  C  CA  . THR A  1 41  ? 92.354  -1.287  27.724 1.00 15.15 ? 231 THR A CA  1 
ATOM   297  C  C   . THR A  1 41  ? 91.407  -0.145  28.101 1.00 16.23 ? 231 THR A C   1 
ATOM   298  O  O   . THR A  1 41  ? 91.794  1.027   28.072 1.00 14.44 ? 231 THR A O   1 
ATOM   299  C  CB  . THR A  1 41  ? 92.208  -1.605  26.231 1.00 16.99 ? 231 THR A CB  1 
ATOM   300  O  OG1 . THR A  1 41  ? 93.076  -2.692  25.889 1.00 16.09 ? 231 THR A OG1 1 
ATOM   301  C  CG2 . THR A  1 41  ? 92.580  -0.400  25.395 1.00 22.06 ? 231 THR A CG2 1 
ATOM   302  N  N   . VAL A  1 42  ? 90.169  -0.488  28.457 1.00 8.50  ? 232 VAL A N   1 
ATOM   303  C  CA  . VAL A  1 42  ? 89.198  0.518   28.871 1.00 11.98 ? 232 VAL A CA  1 
ATOM   304  C  C   . VAL A  1 42  ? 89.741  1.187   30.131 1.00 19.94 ? 232 VAL A C   1 
ATOM   305  O  O   . VAL A  1 42  ? 89.612  2.398   30.310 1.00 25.40 ? 232 VAL A O   1 
ATOM   306  C  CB  . VAL A  1 42  ? 87.811  -0.110  29.200 1.00 13.66 ? 232 VAL A CB  1 
ATOM   307  C  CG1 . VAL A  1 42  ? 86.928  0.906   29.922 1.00 1.27  ? 232 VAL A CG1 1 
ATOM   308  C  CG2 . VAL A  1 42  ? 87.128  -0.571  27.922 1.00 10.62 ? 232 VAL A CG2 1 
ATOM   309  N  N   . ASN A  1 43  ? 90.357  0.390   30.999 1.00 20.68 ? 233 ASN A N   1 
ATOM   310  C  CA  . ASN A  1 43  ? 90.919  0.909   32.239 1.00 19.58 ? 233 ASN A CA  1 
ATOM   311  C  C   . ASN A  1 43  ? 92.058  1.896   31.973 1.00 18.46 ? 233 ASN A C   1 
ATOM   312  O  O   . ASN A  1 43  ? 92.214  2.877   32.699 1.00 22.21 ? 233 ASN A O   1 
ATOM   313  C  CB  . ASN A  1 43  ? 91.420  -0.241  33.120 1.00 18.46 ? 233 ASN A CB  1 
ATOM   314  C  CG  . ASN A  1 43  ? 91.875  0.230   34.491 1.00 17.41 ? 233 ASN A CG  1 
ATOM   315  O  OD1 . ASN A  1 43  ? 91.099  0.805   35.252 1.00 13.33 ? 233 ASN A OD1 1 
ATOM   316  N  ND2 . ASN A  1 43  ? 93.141  -0.009  34.808 1.00 17.68 ? 233 ASN A ND2 1 
ATOM   317  N  N   . GLU A  1 44  ? 92.852  1.639   30.937 1.00 17.44 ? 234 GLU A N   1 
ATOM   318  C  CA  . GLU A  1 44  ? 93.960  2.531   30.597 1.00 16.65 ? 234 GLU A CA  1 
ATOM   319  C  C   . GLU A  1 44  ? 93.365  3.848   30.106 1.00 13.08 ? 234 GLU A C   1 
ATOM   320  O  O   . GLU A  1 44  ? 93.725  4.926   30.574 1.00 9.62  ? 234 GLU A O   1 
ATOM   321  C  CB  . GLU A  1 44  ? 94.832  1.922   29.489 1.00 19.06 ? 234 GLU A CB  1 
ATOM   322  C  CG  . GLU A  1 44  ? 95.284  0.489   29.747 1.00 33.71 ? 234 GLU A CG  1 
ATOM   323  C  CD  . GLU A  1 44  ? 96.144  -0.079  28.622 1.00 41.47 ? 234 GLU A CD  1 
ATOM   324  O  OE1 . GLU A  1 44  ? 95.727  0.001   27.444 1.00 45.68 ? 234 GLU A OE1 1 
ATOM   325  O  OE2 . GLU A  1 44  ? 97.235  -0.614  28.917 1.00 43.98 ? 234 GLU A OE2 1 
ATOM   326  N  N   . ILE A  1 45  ? 92.440  3.737   29.160 1.00 10.79 ? 235 ILE A N   1 
ATOM   327  C  CA  . ILE A  1 45  ? 91.769  4.889   28.581 1.00 11.16 ? 235 ILE A CA  1 
ATOM   328  C  C   . ILE A  1 45  ? 91.201  5.830   29.645 1.00 12.57 ? 235 ILE A C   1 
ATOM   329  O  O   . ILE A  1 45  ? 91.117  7.043   29.433 1.00 15.16 ? 235 ILE A O   1 
ATOM   330  C  CB  . ILE A  1 45  ? 90.628  4.425   27.640 1.00 8.80  ? 235 ILE A CB  1 
ATOM   331  C  CG1 . ILE A  1 45  ? 91.228  3.683   26.441 1.00 10.94 ? 235 ILE A CG1 1 
ATOM   332  C  CG2 . ILE A  1 45  ? 89.801  5.611   27.181 1.00 9.69  ? 235 ILE A CG2 1 
ATOM   333  C  CD1 . ILE A  1 45  ? 90.211  3.146   25.461 1.00 4.54  ? 235 ILE A CD1 1 
ATOM   334  N  N   . TYR A  1 46  ? 90.826  5.272   30.791 1.00 7.22  ? 236 TYR A N   1 
ATOM   335  C  CA  . TYR A  1 46  ? 90.252  6.063   31.871 1.00 9.74  ? 236 TYR A CA  1 
ATOM   336  C  C   . TYR A  1 46  ? 91.253  6.556   32.911 1.00 13.74 ? 236 TYR A C   1 
ATOM   337  O  O   . TYR A  1 46  ? 90.882  7.284   33.839 1.00 16.46 ? 236 TYR A O   1 
ATOM   338  C  CB  . TYR A  1 46  ? 89.149  5.264   32.561 1.00 7.43  ? 236 TYR A CB  1 
ATOM   339  C  CG  . TYR A  1 46  ? 87.782  5.486   31.973 1.00 2.13  ? 236 TYR A CG  1 
ATOM   340  C  CD1 . TYR A  1 46  ? 87.016  6.590   32.345 1.00 12.12 ? 236 TYR A CD1 1 
ATOM   341  C  CD2 . TYR A  1 46  ? 87.251  4.598   31.041 1.00 7.79  ? 236 TYR A CD2 1 
ATOM   342  C  CE1 . TYR A  1 46  ? 85.748  6.804   31.803 1.00 16.12 ? 236 TYR A CE1 1 
ATOM   343  C  CE2 . TYR A  1 46  ? 85.986  4.799   30.490 1.00 5.79  ? 236 TYR A CE2 1 
ATOM   344  C  CZ  . TYR A  1 46  ? 85.240  5.903   30.875 1.00 13.28 ? 236 TYR A CZ  1 
ATOM   345  O  OH  . TYR A  1 46  ? 83.992  6.106   30.332 1.00 11.92 ? 236 TYR A OH  1 
ATOM   346  N  N   . ARG A  1 47  ? 92.513  6.160   32.764 1.00 9.06  ? 237 ARG A N   1 
ATOM   347  C  CA  . ARG A  1 47  ? 93.545  6.586   33.700 1.00 12.69 ? 237 ARG A CA  1 
ATOM   348  C  C   . ARG A  1 47  ? 93.563  8.111   33.739 1.00 17.34 ? 237 ARG A C   1 
ATOM   349  O  O   . ARG A  1 47  ? 93.654  8.721   34.805 1.00 21.33 ? 237 ARG A O   1 
ATOM   350  C  CB  . ARG A  1 47  ? 94.909  6.051   33.254 1.00 16.65 ? 237 ARG A CB  1 
ATOM   351  C  CG  . ARG A  1 47  ? 96.067  6.429   34.162 1.00 19.99 ? 237 ARG A CG  1 
ATOM   352  C  CD  . ARG A  1 47  ? 97.342  5.716   33.740 1.00 22.59 ? 237 ARG A CD  1 
ATOM   353  N  NE  . ARG A  1 47  ? 98.460  6.014   34.632 1.00 31.77 ? 237 ARG A NE  1 
ATOM   354  C  CZ  . ARG A  1 47  ? 99.105  7.176   34.670 1.00 33.29 ? 237 ARG A CZ  1 
ATOM   355  N  NH1 . ARG A  1 47  ? 98.749  8.161   33.859 1.00 33.77 ? 237 ARG A NH1 1 
ATOM   356  N  NH2 . ARG A  1 47  ? 100.104 7.356   35.524 1.00 33.16 ? 237 ARG A NH2 1 
ATOM   357  N  N   . TYR A  1 48  ? 93.463  8.714   32.559 1.00 19.54 ? 238 TYR A N   1 
ATOM   358  C  CA  . TYR A  1 48  ? 93.460  10.164  32.405 1.00 20.20 ? 238 TYR A CA  1 
ATOM   359  C  C   . TYR A  1 48  ? 92.347  10.813  33.214 1.00 21.63 ? 238 TYR A C   1 
ATOM   360  O  O   . TYR A  1 48  ? 92.545  11.865  33.810 1.00 28.10 ? 238 TYR A O   1 
ATOM   361  C  CB  . TYR A  1 48  ? 93.284  10.512  30.927 1.00 26.65 ? 238 TYR A CB  1 
ATOM   362  C  CG  . TYR A  1 48  ? 93.056  11.976  30.636 1.00 31.25 ? 238 TYR A CG  1 
ATOM   363  C  CD1 . TYR A  1 48  ? 94.090  12.902  30.759 1.00 33.58 ? 238 TYR A CD1 1 
ATOM   364  C  CD2 . TYR A  1 48  ? 91.806  12.434  30.213 1.00 33.09 ? 238 TYR A CD2 1 
ATOM   365  C  CE1 . TYR A  1 48  ? 93.890  14.251  30.462 1.00 34.64 ? 238 TYR A CE1 1 
ATOM   366  C  CE2 . TYR A  1 48  ? 91.592  13.780  29.915 1.00 35.36 ? 238 TYR A CE2 1 
ATOM   367  C  CZ  . TYR A  1 48  ? 92.639  14.682  30.040 1.00 37.12 ? 238 TYR A CZ  1 
ATOM   368  O  OH  . TYR A  1 48  ? 92.442  16.010  29.735 1.00 34.89 ? 238 TYR A OH  1 
ATOM   369  N  N   . MET A  1 49  ? 91.178  10.176  33.226 1.00 22.29 ? 239 MET A N   1 
ATOM   370  C  CA  . MET A  1 49  ? 90.006  10.683  33.945 1.00 20.09 ? 239 MET A CA  1 
ATOM   371  C  C   . MET A  1 49  ? 90.057  10.369  35.437 1.00 21.59 ? 239 MET A C   1 
ATOM   372  O  O   . MET A  1 49  ? 89.052  10.508  36.138 1.00 15.94 ? 239 MET A O   1 
ATOM   373  C  CB  . MET A  1 49  ? 88.733  10.060  33.368 1.00 20.67 ? 239 MET A CB  1 
ATOM   374  C  CG  . MET A  1 49  ? 88.592  10.170  31.862 1.00 22.07 ? 239 MET A CG  1 
ATOM   375  S  SD  . MET A  1 49  ? 88.105  11.801  31.314 1.00 22.69 ? 239 MET A SD  1 
ATOM   376  C  CE  . MET A  1 49  ? 86.342  11.607  31.185 1.00 18.03 ? 239 MET A CE  1 
ATOM   377  N  N   . TYR A  1 50  ? 91.222  9.945   35.917 1.00 22.48 ? 240 TYR A N   1 
ATOM   378  C  CA  . TYR A  1 50  ? 91.384  9.589   37.323 1.00 22.63 ? 240 TYR A CA  1 
ATOM   379  C  C   . TYR A  1 50  ? 90.340  8.565   37.751 1.00 22.75 ? 240 TYR A C   1 
ATOM   380  O  O   . TYR A  1 50  ? 89.838  8.597   38.877 1.00 23.62 ? 240 TYR A O   1 
ATOM   381  C  CB  . TYR A  1 50  ? 91.300  10.831  38.220 1.00 24.00 ? 240 TYR A CB  1 
ATOM   382  C  CG  . TYR A  1 50  ? 92.565  11.658  38.206 1.00 29.52 ? 240 TYR A CG  1 
ATOM   383  C  CD1 . TYR A  1 50  ? 92.703  12.746  37.344 1.00 29.40 ? 240 TYR A CD1 1 
ATOM   384  C  CD2 . TYR A  1 50  ? 93.649  11.318  39.020 1.00 31.16 ? 240 TYR A CD2 1 
ATOM   385  C  CE1 . TYR A  1 50  ? 93.893  13.475  37.290 1.00 34.27 ? 240 TYR A CE1 1 
ATOM   386  C  CE2 . TYR A  1 50  ? 94.843  12.036  38.975 1.00 29.97 ? 240 TYR A CE2 1 
ATOM   387  C  CZ  . TYR A  1 50  ? 94.960  13.113  38.107 1.00 36.15 ? 240 TYR A CZ  1 
ATOM   388  O  OH  . TYR A  1 50  ? 96.143  13.823  38.050 1.00 33.07 ? 240 TYR A OH  1 
ATOM   389  N  N   . ILE A  1 51  ? 90.024  7.650   36.839 1.00 19.92 ? 241 ILE A N   1 
ATOM   390  C  CA  . ILE A  1 51  ? 89.050  6.601   37.112 1.00 15.00 ? 241 ILE A CA  1 
ATOM   391  C  C   . ILE A  1 51  ? 89.631  5.242   36.734 1.00 12.20 ? 241 ILE A C   1 
ATOM   392  O  O   . ILE A  1 51  ? 90.402  5.127   35.783 1.00 9.35  ? 241 ILE A O   1 
ATOM   393  C  CB  . ILE A  1 51  ? 87.741  6.814   36.307 1.00 14.33 ? 241 ILE A CB  1 
ATOM   394  C  CG1 . ILE A  1 51  ? 87.094  8.142   36.700 1.00 11.43 ? 241 ILE A CG1 1 
ATOM   395  C  CG2 . ILE A  1 51  ? 86.771  5.660   36.558 1.00 7.60  ? 241 ILE A CG2 1 
ATOM   396  C  CD1 . ILE A  1 51  ? 85.773  8.416   35.988 1.00 6.47  ? 241 ILE A CD1 1 
ATOM   397  N  N   . HIS A  1 52  ? 89.269  4.221   37.499 1.00 10.81 ? 242 HIS A N   1 
ATOM   398  C  CA  . HIS A  1 52  ? 89.721  2.864   37.233 1.00 7.76  ? 242 HIS A CA  1 
ATOM   399  C  C   . HIS A  1 52  ? 88.490  2.034   36.912 1.00 11.45 ? 242 HIS A C   1 
ATOM   400  O  O   . HIS A  1 52  ? 87.394  2.316   37.403 1.00 13.13 ? 242 HIS A O   1 
ATOM   401  C  CB  . HIS A  1 52  ? 90.426  2.269   38.451 1.00 7.85  ? 242 HIS A CB  1 
ATOM   402  C  CG  . HIS A  1 52  ? 91.789  2.836   38.703 1.00 16.67 ? 242 HIS A CG  1 
ATOM   403  N  ND1 . HIS A  1 52  ? 92.764  2.891   37.731 1.00 17.62 ? 242 HIS A ND1 1 
ATOM   404  C  CD2 . HIS A  1 52  ? 92.351  3.341   39.827 1.00 14.33 ? 242 HIS A CD2 1 
ATOM   405  C  CE1 . HIS A  1 52  ? 93.868  3.404   38.244 1.00 17.23 ? 242 HIS A CE1 1 
ATOM   406  N  NE2 . HIS A  1 52  ? 93.644  3.686   39.514 1.00 18.10 ? 242 HIS A NE2 1 
ATOM   407  N  N   . VAL A  1 53  ? 88.670  1.017   36.078 1.00 12.54 ? 243 VAL A N   1 
ATOM   408  C  CA  . VAL A  1 53  ? 87.575  0.135   35.703 1.00 11.90 ? 243 VAL A CA  1 
ATOM   409  C  C   . VAL A  1 53  ? 88.007  -1.307  35.946 1.00 13.31 ? 243 VAL A C   1 
ATOM   410  O  O   . VAL A  1 53  ? 89.000  -1.773  35.379 1.00 10.73 ? 243 VAL A O   1 
ATOM   411  C  CB  . VAL A  1 53  ? 87.193  0.317   34.222 1.00 13.33 ? 243 VAL A CB  1 
ATOM   412  C  CG1 . VAL A  1 53  ? 86.047  -0.618  33.865 1.00 11.35 ? 243 VAL A CG1 1 
ATOM   413  C  CG2 . VAL A  1 53  ? 86.796  1.767   33.965 1.00 6.71  ? 243 VAL A CG2 1 
ATOM   414  N  N   . ALA A  1 54  ? 87.267  -2.006  36.799 1.00 10.49 ? 244 ALA A N   1 
ATOM   415  C  CA  . ALA A  1 54  ? 87.596  -3.385  37.120 1.00 10.88 ? 244 ALA A CA  1 
ATOM   416  C  C   . ALA A  1 54  ? 86.453  -4.323  36.770 1.00 13.60 ? 244 ALA A C   1 
ATOM   417  O  O   . ALA A  1 54  ? 85.290  -4.024  37.040 1.00 16.89 ? 244 ALA A O   1 
ATOM   418  C  CB  . ALA A  1 54  ? 87.938  -3.499  38.596 1.00 11.64 ? 244 ALA A CB  1 
ATOM   419  N  N   . LEU A  1 55  ? 86.786  -5.458  36.166 1.00 17.35 ? 245 LEU A N   1 
ATOM   420  C  CA  . LEU A  1 55  ? 85.777  -6.438  35.782 1.00 18.09 ? 245 LEU A CA  1 
ATOM   421  C  C   . LEU A  1 55  ? 85.448  -7.320  36.982 1.00 17.55 ? 245 LEU A C   1 
ATOM   422  O  O   . LEU A  1 55  ? 86.244  -8.183  37.361 1.00 17.97 ? 245 LEU A O   1 
ATOM   423  C  CB  . LEU A  1 55  ? 86.294  -7.300  34.622 1.00 16.46 ? 245 LEU A CB  1 
ATOM   424  C  CG  . LEU A  1 55  ? 85.321  -8.307  33.997 1.00 19.10 ? 245 LEU A CG  1 
ATOM   425  C  CD1 . LEU A  1 55  ? 84.171  -7.568  33.322 1.00 18.21 ? 245 LEU A CD1 1 
ATOM   426  C  CD2 . LEU A  1 55  ? 86.060  -9.172  32.984 1.00 14.64 ? 245 LEU A CD2 1 
ATOM   427  N  N   . VAL A  1 56  ? 84.280  -7.101  37.582 1.00 13.04 ? 246 VAL A N   1 
ATOM   428  C  CA  . VAL A  1 56  ? 83.866  -7.884  38.741 1.00 10.45 ? 246 VAL A CA  1 
ATOM   429  C  C   . VAL A  1 56  ? 82.927  -9.030  38.370 1.00 17.55 ? 246 VAL A C   1 
ATOM   430  O  O   . VAL A  1 56  ? 82.571  -9.850  39.219 1.00 19.81 ? 246 VAL A O   1 
ATOM   431  C  CB  . VAL A  1 56  ? 83.155  -7.008  39.782 1.00 8.34  ? 246 VAL A CB  1 
ATOM   432  C  CG1 . VAL A  1 56  ? 84.052  -5.853  40.184 1.00 13.48 ? 246 VAL A CG1 1 
ATOM   433  C  CG2 . VAL A  1 56  ? 81.829  -6.509  39.229 1.00 8.46  ? 246 VAL A CG2 1 
ATOM   434  N  N   . GLY A  1 57  ? 82.524  -9.083  37.104 1.00 16.55 ? 247 GLY A N   1 
ATOM   435  C  CA  . GLY A  1 57  ? 81.627  -10.136 36.669 1.00 13.65 ? 247 GLY A CA  1 
ATOM   436  C  C   . GLY A  1 57  ? 81.553  -10.265 35.162 1.00 14.23 ? 247 GLY A C   1 
ATOM   437  O  O   . GLY A  1 57  ? 81.636  -9.276  34.437 1.00 15.29 ? 247 GLY A O   1 
ATOM   438  N  N   . LEU A  1 58  ? 81.406  -11.497 34.689 1.00 10.57 ? 248 LEU A N   1 
ATOM   439  C  CA  . LEU A  1 58  ? 81.316  -11.763 33.264 1.00 12.94 ? 248 LEU A CA  1 
ATOM   440  C  C   . LEU A  1 58  ? 80.286  -12.858 33.023 1.00 18.86 ? 248 LEU A C   1 
ATOM   441  O  O   . LEU A  1 58  ? 80.500  -14.015 33.389 1.00 25.99 ? 248 LEU A O   1 
ATOM   442  C  CB  . LEU A  1 58  ? 82.678  -12.197 32.722 1.00 6.70  ? 248 LEU A CB  1 
ATOM   443  C  CG  . LEU A  1 58  ? 82.761  -12.436 31.212 1.00 12.50 ? 248 LEU A CG  1 
ATOM   444  C  CD1 . LEU A  1 58  ? 82.274  -11.204 30.465 1.00 13.51 ? 248 LEU A CD1 1 
ATOM   445  C  CD2 . LEU A  1 58  ? 84.197  -12.769 30.826 1.00 13.76 ? 248 LEU A CD2 1 
ATOM   446  N  N   . GLU A  1 59  ? 79.169  -12.487 32.409 1.00 15.98 ? 249 GLU A N   1 
ATOM   447  C  CA  . GLU A  1 59  ? 78.101  -13.436 32.128 1.00 20.25 ? 249 GLU A CA  1 
ATOM   448  C  C   . GLU A  1 59  ? 77.959  -13.670 30.624 1.00 21.22 ? 249 GLU A C   1 
ATOM   449  O  O   . GLU A  1 59  ? 77.768  -12.725 29.858 1.00 21.81 ? 249 GLU A O   1 
ATOM   450  C  CB  . GLU A  1 59  ? 76.792  -12.912 32.729 1.00 22.99 ? 249 GLU A CB  1 
ATOM   451  C  CG  . GLU A  1 59  ? 75.573  -13.788 32.499 1.00 23.35 ? 249 GLU A CG  1 
ATOM   452  C  CD  . GLU A  1 59  ? 74.518  -13.601 33.575 1.00 23.40 ? 249 GLU A CD  1 
ATOM   453  O  OE1 . GLU A  1 59  ? 73.356  -13.992 33.348 1.00 28.95 ? 249 GLU A OE1 1 
ATOM   454  O  OE2 . GLU A  1 59  ? 74.851  -13.074 34.656 1.00 28.32 ? 249 GLU A OE2 1 
ATOM   455  N  N   . ILE A  1 60  ? 78.065  -14.932 30.210 1.00 20.99 ? 250 ILE A N   1 
ATOM   456  C  CA  . ILE A  1 60  ? 77.964  -15.307 28.799 1.00 19.83 ? 250 ILE A CA  1 
ATOM   457  C  C   . ILE A  1 60  ? 76.683  -16.092 28.551 1.00 21.59 ? 250 ILE A C   1 
ATOM   458  O  O   . ILE A  1 60  ? 76.523  -17.188 29.082 1.00 26.06 ? 250 ILE A O   1 
ATOM   459  C  CB  . ILE A  1 60  ? 79.141  -16.218 28.364 1.00 22.75 ? 250 ILE A CB  1 
ATOM   460  C  CG1 . ILE A  1 60  ? 80.487  -15.543 28.649 1.00 15.93 ? 250 ILE A CG1 1 
ATOM   461  C  CG2 . ILE A  1 60  ? 79.013  -16.559 26.885 1.00 18.40 ? 250 ILE A CG2 1 
ATOM   462  C  CD1 . ILE A  1 60  ? 80.780  -14.365 27.778 1.00 22.33 ? 250 ILE A CD1 1 
ATOM   463  N  N   . TRP A  1 61  ? 75.781  -15.544 27.741 1.00 21.16 ? 251 TRP A N   1 
ATOM   464  C  CA  . TRP A  1 61  ? 74.524  -16.225 27.429 1.00 20.26 ? 251 TRP A CA  1 
ATOM   465  C  C   . TRP A  1 61  ? 74.714  -17.249 26.305 1.00 23.00 ? 251 TRP A C   1 
ATOM   466  O  O   . TRP A  1 61  ? 74.154  -17.109 25.218 1.00 23.70 ? 251 TRP A O   1 
ATOM   467  C  CB  . TRP A  1 61  ? 73.454  -15.211 27.015 1.00 24.08 ? 251 TRP A CB  1 
ATOM   468  C  CG  . TRP A  1 61  ? 73.041  -14.253 28.097 1.00 22.79 ? 251 TRP A CG  1 
ATOM   469  C  CD1 . TRP A  1 61  ? 73.163  -14.432 29.446 1.00 20.45 ? 251 TRP A CD1 1 
ATOM   470  C  CD2 . TRP A  1 61  ? 72.382  -12.993 27.918 1.00 21.11 ? 251 TRP A CD2 1 
ATOM   471  N  NE1 . TRP A  1 61  ? 72.618  -13.362 30.118 1.00 19.87 ? 251 TRP A NE1 1 
ATOM   472  C  CE2 . TRP A  1 61  ? 72.129  -12.466 29.205 1.00 24.02 ? 251 TRP A CE2 1 
ATOM   473  C  CE3 . TRP A  1 61  ? 71.974  -12.260 26.795 1.00 21.97 ? 251 TRP A CE3 1 
ATOM   474  C  CZ2 . TRP A  1 61  ? 71.491  -11.233 29.399 1.00 28.90 ? 251 TRP A CZ2 1 
ATOM   475  C  CZ3 . TRP A  1 61  ? 71.340  -11.034 26.988 1.00 22.05 ? 251 TRP A CZ3 1 
ATOM   476  C  CH2 . TRP A  1 61  ? 71.103  -10.535 28.282 1.00 23.67 ? 251 TRP A CH2 1 
ATOM   477  N  N   . SER A  1 62  ? 75.499  -18.285 26.574 1.00 25.87 ? 252 SER A N   1 
ATOM   478  C  CA  . SER A  1 62  ? 75.771  -19.318 25.581 1.00 25.55 ? 252 SER A CA  1 
ATOM   479  C  C   . SER A  1 62  ? 74.553  -20.158 25.206 1.00 25.60 ? 252 SER A C   1 
ATOM   480  O  O   . SER A  1 62  ? 74.483  -20.685 24.096 1.00 28.30 ? 252 SER A O   1 
ATOM   481  C  CB  . SER A  1 62  ? 76.897  -20.229 26.073 1.00 22.17 ? 252 SER A CB  1 
ATOM   482  O  OG  . SER A  1 62  ? 76.622  -20.713 27.373 1.00 26.86 ? 252 SER A OG  1 
ATOM   483  N  N   . ASN A  1 63  ? 73.598  -20.293 26.120 1.00 26.34 ? 253 ASN A N   1 
ATOM   484  C  CA  . ASN A  1 63  ? 72.396  -21.071 25.829 1.00 28.78 ? 253 ASN A CA  1 
ATOM   485  C  C   . ASN A  1 63  ? 71.314  -20.194 25.218 1.00 28.14 ? 253 ASN A C   1 
ATOM   486  O  O   . ASN A  1 63  ? 70.980  -20.342 24.044 1.00 26.99 ? 253 ASN A O   1 
ATOM   487  C  CB  . ASN A  1 63  ? 71.872  -21.745 27.095 1.00 35.29 ? 253 ASN A CB  1 
ATOM   488  C  CG  . ASN A  1 63  ? 72.780  -22.862 27.569 1.00 51.21 ? 253 ASN A CG  1 
ATOM   489  O  OD1 . ASN A  1 63  ? 73.922  -22.623 27.964 1.00 58.81 ? 253 ASN A OD1 1 
ATOM   490  N  ND2 . ASN A  1 63  ? 72.281  -24.095 27.519 1.00 54.70 ? 253 ASN A ND2 1 
ATOM   491  N  N   . GLU A  1 64  ? 70.770  -19.277 26.009 1.00 25.54 ? 254 GLU A N   1 
ATOM   492  C  CA  . GLU A  1 64  ? 69.737  -18.377 25.513 1.00 27.03 ? 254 GLU A CA  1 
ATOM   493  C  C   . GLU A  1 64  ? 69.889  -16.976 26.099 1.00 24.14 ? 254 GLU A C   1 
ATOM   494  O  O   . GLU A  1 64  ? 70.346  -16.813 27.230 1.00 19.69 ? 254 GLU A O   1 
ATOM   495  C  CB  . GLU A  1 64  ? 68.348  -18.932 25.843 1.00 28.98 ? 254 GLU A CB  1 
ATOM   496  C  CG  . GLU A  1 64  ? 68.083  -19.121 27.329 1.00 44.14 ? 254 GLU A CG  1 
ATOM   497  C  CD  . GLU A  1 64  ? 66.687  -19.659 27.609 1.00 51.54 ? 254 GLU A CD  1 
ATOM   498  O  OE1 . GLU A  1 64  ? 66.376  -20.775 27.144 1.00 57.25 ? 254 GLU A OE1 1 
ATOM   499  O  OE2 . GLU A  1 64  ? 65.900  -18.966 28.291 1.00 51.70 ? 254 GLU A OE2 1 
ATOM   500  N  N   . ASP A  1 65  ? 69.523  -15.962 25.322 1.00 19.57 ? 255 ASP A N   1 
ATOM   501  C  CA  . ASP A  1 65  ? 69.608  -14.595 25.808 1.00 22.63 ? 255 ASP A CA  1 
ATOM   502  C  C   . ASP A  1 65  ? 68.526  -14.423 26.865 1.00 23.67 ? 255 ASP A C   1 
ATOM   503  O  O   . ASP A  1 65  ? 67.419  -14.940 26.717 1.00 20.02 ? 255 ASP A O   1 
ATOM   504  C  CB  . ASP A  1 65  ? 69.382  -13.587 24.677 1.00 24.58 ? 255 ASP A CB  1 
ATOM   505  C  CG  . ASP A  1 65  ? 70.457  -13.653 23.603 1.00 24.11 ? 255 ASP A CG  1 
ATOM   506  O  OD1 . ASP A  1 65  ? 71.646  -13.822 23.946 1.00 23.30 ? 255 ASP A OD1 1 
ATOM   507  O  OD2 . ASP A  1 65  ? 70.110  -13.519 22.413 1.00 21.57 ? 255 ASP A OD2 1 
ATOM   508  N  N   . LYS A  1 66  ? 68.848  -13.701 27.932 1.00 26.11 ? 256 LYS A N   1 
ATOM   509  C  CA  . LYS A  1 66  ? 67.891  -13.482 29.005 1.00 24.97 ? 256 LYS A CA  1 
ATOM   510  C  C   . LYS A  1 66  ? 66.906  -12.356 28.686 1.00 26.83 ? 256 LYS A C   1 
ATOM   511  O  O   . LYS A  1 66  ? 65.964  -12.103 29.439 1.00 28.50 ? 256 LYS A O   1 
ATOM   512  C  CB  . LYS A  1 66  ? 68.642  -13.238 30.314 1.00 26.68 ? 256 LYS A CB  1 
ATOM   513  C  CG  . LYS A  1 66  ? 69.534  -14.426 30.671 1.00 28.61 ? 256 LYS A CG  1 
ATOM   514  C  CD  . LYS A  1 66  ? 70.060  -14.382 32.091 1.00 33.37 ? 256 LYS A CD  1 
ATOM   515  C  CE  . LYS A  1 66  ? 70.844  -15.651 32.403 1.00 33.65 ? 256 LYS A CE  1 
ATOM   516  N  NZ  . LYS A  1 66  ? 71.328  -15.704 33.814 1.00 38.43 ? 256 LYS A NZ  1 
ATOM   517  N  N   . ILE A  1 67  ? 67.136  -11.688 27.559 1.00 24.64 ? 257 ILE A N   1 
ATOM   518  C  CA  . ILE A  1 67  ? 66.252  -10.632 27.068 1.00 21.23 ? 257 ILE A CA  1 
ATOM   519  C  C   . ILE A  1 67  ? 66.229  -10.830 25.562 1.00 23.57 ? 257 ILE A C   1 
ATOM   520  O  O   . ILE A  1 67  ? 67.022  -11.613 25.027 1.00 19.43 ? 257 ILE A O   1 
ATOM   521  C  CB  . ILE A  1 67  ? 66.784  -9.200  27.331 1.00 18.24 ? 257 ILE A CB  1 
ATOM   522  C  CG1 . ILE A  1 67  ? 68.130  -9.009  26.636 1.00 14.13 ? 257 ILE A CG1 1 
ATOM   523  C  CG2 . ILE A  1 67  ? 66.871  -8.931  28.818 1.00 13.95 ? 257 ILE A CG2 1 
ATOM   524  C  CD1 . ILE A  1 67  ? 68.595  -7.570  26.597 1.00 15.87 ? 257 ILE A CD1 1 
ATOM   525  N  N   . THR A  1 68  ? 65.328  -10.137 24.876 1.00 21.34 ? 258 THR A N   1 
ATOM   526  C  CA  . THR A  1 68  ? 65.270  -10.253 23.426 1.00 23.91 ? 258 THR A CA  1 
ATOM   527  C  C   . THR A  1 68  ? 66.205  -9.191  22.854 1.00 22.17 ? 258 THR A C   1 
ATOM   528  O  O   . THR A  1 68  ? 65.952  -7.995  22.995 1.00 22.53 ? 258 THR A O   1 
ATOM   529  C  CB  . THR A  1 68  ? 63.846  -10.016 22.895 1.00 28.86 ? 258 THR A CB  1 
ATOM   530  O  OG1 . THR A  1 68  ? 62.954  -10.972 23.478 1.00 33.17 ? 258 THR A OG1 1 
ATOM   531  C  CG2 . THR A  1 68  ? 63.814  -10.161 21.380 1.00 29.08 ? 258 THR A CG2 1 
ATOM   532  N  N   . VAL A  1 69  ? 67.291  -9.623  22.222 1.00 16.99 ? 259 VAL A N   1 
ATOM   533  C  CA  . VAL A  1 69  ? 68.243  -8.673  21.661 1.00 16.71 ? 259 VAL A CA  1 
ATOM   534  C  C   . VAL A  1 69  ? 67.825  -8.248  20.265 1.00 17.92 ? 259 VAL A C   1 
ATOM   535  O  O   . VAL A  1 69  ? 68.122  -8.932  19.284 1.00 11.77 ? 259 VAL A O   1 
ATOM   536  C  CB  . VAL A  1 69  ? 69.665  -9.264  21.590 1.00 16.07 ? 259 VAL A CB  1 
ATOM   537  C  CG1 . VAL A  1 69  ? 70.647  -8.179  21.184 1.00 16.64 ? 259 VAL A CG1 1 
ATOM   538  C  CG2 . VAL A  1 69  ? 70.057  -9.852  22.934 1.00 16.08 ? 259 VAL A CG2 1 
ATOM   539  N  N   . LYS A  1 70  ? 67.140  -7.111  20.181 1.00 17.72 ? 260 LYS A N   1 
ATOM   540  C  CA  . LYS A  1 70  ? 66.672  -6.602  18.899 1.00 18.02 ? 260 LYS A CA  1 
ATOM   541  C  C   . LYS A  1 70  ? 67.633  -5.583  18.314 1.00 15.52 ? 260 LYS A C   1 
ATOM   542  O  O   . LYS A  1 70  ? 68.281  -4.840  19.050 1.00 10.49 ? 260 LYS A O   1 
ATOM   543  C  CB  . LYS A  1 70  ? 65.293  -5.954  19.050 1.00 19.09 ? 260 LYS A CB  1 
ATOM   544  C  CG  . LYS A  1 70  ? 64.200  -6.890  19.534 1.00 20.26 ? 260 LYS A CG  1 
ATOM   545  C  CD  . LYS A  1 70  ? 62.867  -6.167  19.583 1.00 25.01 ? 260 LYS A CD  1 
ATOM   546  C  CE  . LYS A  1 70  ? 61.784  -7.044  20.179 1.00 29.75 ? 260 LYS A CE  1 
ATOM   547  N  NZ  . LYS A  1 70  ? 60.510  -6.300  20.361 1.00 32.82 ? 260 LYS A NZ  1 
ATOM   548  N  N   . PRO A  1 71  ? 67.744  -5.544  16.975 1.00 16.75 ? 261 PRO A N   1 
ATOM   549  C  CA  . PRO A  1 71  ? 68.642  -4.591  16.315 1.00 17.08 ? 261 PRO A CA  1 
ATOM   550  C  C   . PRO A  1 71  ? 68.215  -3.157  16.599 1.00 15.70 ? 261 PRO A C   1 
ATOM   551  O  O   . PRO A  1 71  ? 68.927  -2.206  16.279 1.00 18.35 ? 261 PRO A O   1 
ATOM   552  C  CB  . PRO A  1 71  ? 68.528  -4.967  14.834 1.00 16.73 ? 261 PRO A CB  1 
ATOM   553  C  CG  . PRO A  1 71  ? 67.177  -5.616  14.737 1.00 15.80 ? 261 PRO A CG  1 
ATOM   554  C  CD  . PRO A  1 71  ? 67.121  -6.445  15.990 1.00 11.31 ? 261 PRO A CD  1 
ATOM   555  N  N   . GLU A  1 72  ? 67.041  -3.018  17.205 1.00 15.98 ? 262 GLU A N   1 
ATOM   556  C  CA  . GLU A  1 72  ? 66.501  -1.714  17.570 1.00 21.47 ? 262 GLU A CA  1 
ATOM   557  C  C   . GLU A  1 72  ? 67.115  -1.390  18.939 1.00 19.91 ? 262 GLU A C   1 
ATOM   558  O  O   . GLU A  1 72  ? 66.623  -1.844  19.978 1.00 17.12 ? 262 GLU A O   1 
ATOM   559  C  CB  . GLU A  1 72  ? 64.972  -1.808  17.646 1.00 28.03 ? 262 GLU A CB  1 
ATOM   560  C  CG  . GLU A  1 72  ? 64.230  -0.483  17.640 1.00 40.35 ? 262 GLU A CG  1 
ATOM   561  C  CD  . GLU A  1 72  ? 64.232  0.197   18.992 1.00 46.54 ? 262 GLU A CD  1 
ATOM   562  O  OE1 . GLU A  1 72  ? 65.320  0.593   19.459 1.00 47.65 ? 262 GLU A OE1 1 
ATOM   563  O  OE2 . GLU A  1 72  ? 63.141  0.330   19.589 1.00 48.20 ? 262 GLU A OE2 1 
ATOM   564  N  N   . ALA A  1 73  ? 68.201  -0.616  18.920 1.00 14.35 ? 263 ALA A N   1 
ATOM   565  C  CA  . ALA A  1 73  ? 68.944  -0.242  20.127 1.00 9.91  ? 263 ALA A CA  1 
ATOM   566  C  C   . ALA A  1 73  ? 68.098  0.146   21.342 1.00 8.15  ? 263 ALA A C   1 
ATOM   567  O  O   . ALA A  1 73  ? 68.249  -0.435  22.421 1.00 4.74  ? 263 ALA A O   1 
ATOM   568  C  CB  . ALA A  1 73  ? 69.933  0.881   19.796 1.00 6.29  ? 263 ALA A CB  1 
ATOM   569  N  N   . GLY A  1 74  ? 67.222  1.132   21.163 1.00 9.83  ? 264 GLY A N   1 
ATOM   570  C  CA  . GLY A  1 74  ? 66.364  1.588   22.244 1.00 1.33  ? 264 GLY A CA  1 
ATOM   571  C  C   . GLY A  1 74  ? 65.706  0.444   22.984 1.00 5.51  ? 264 GLY A C   1 
ATOM   572  O  O   . GLY A  1 74  ? 65.824  0.333   24.204 1.00 8.23  ? 264 GLY A O   1 
ATOM   573  N  N   . TYR A  1 75  ? 65.013  -0.415  22.248 1.00 5.47  ? 265 TYR A N   1 
ATOM   574  C  CA  . TYR A  1 75  ? 64.346  -1.554  22.860 1.00 9.04  ? 265 TYR A CA  1 
ATOM   575  C  C   . TYR A  1 75  ? 65.335  -2.403  23.656 1.00 12.56 ? 265 TYR A C   1 
ATOM   576  O  O   . TYR A  1 75  ? 65.054  -2.812  24.782 1.00 15.95 ? 265 TYR A O   1 
ATOM   577  C  CB  . TYR A  1 75  ? 63.692  -2.430  21.791 1.00 11.50 ? 265 TYR A CB  1 
ATOM   578  C  CG  . TYR A  1 75  ? 63.122  -3.711  22.346 1.00 9.70  ? 265 TYR A CG  1 
ATOM   579  C  CD1 . TYR A  1 75  ? 61.788  -3.789  22.740 1.00 10.15 ? 265 TYR A CD1 1 
ATOM   580  C  CD2 . TYR A  1 75  ? 63.937  -4.826  22.545 1.00 11.35 ? 265 TYR A CD2 1 
ATOM   581  C  CE1 . TYR A  1 75  ? 61.276  -4.947  23.324 1.00 13.80 ? 265 TYR A CE1 1 
ATOM   582  C  CE2 . TYR A  1 75  ? 63.440  -5.986  23.130 1.00 17.44 ? 265 TYR A CE2 1 
ATOM   583  C  CZ  . TYR A  1 75  ? 62.108  -6.040  23.518 1.00 17.87 ? 265 TYR A CZ  1 
ATOM   584  O  OH  . TYR A  1 75  ? 61.617  -7.180  24.111 1.00 19.01 ? 265 TYR A OH  1 
ATOM   585  N  N   . THR A  1 76  ? 66.487  -2.674  23.055 1.00 14.37 ? 266 THR A N   1 
ATOM   586  C  CA  . THR A  1 76  ? 67.510  -3.492  23.694 1.00 15.84 ? 266 THR A CA  1 
ATOM   587  C  C   . THR A  1 76  ? 68.137  -2.835  24.924 1.00 15.91 ? 266 THR A C   1 
ATOM   588  O  O   . THR A  1 76  ? 68.297  -3.478  25.964 1.00 11.56 ? 266 THR A O   1 
ATOM   589  C  CB  . THR A  1 76  ? 68.609  -3.858  22.689 1.00 12.74 ? 266 THR A CB  1 
ATOM   590  O  OG1 . THR A  1 76  ? 68.045  -4.675  21.652 1.00 10.45 ? 266 THR A OG1 1 
ATOM   591  C  CG2 . THR A  1 76  ? 69.730  -4.614  23.381 1.00 13.89 ? 266 THR A CG2 1 
ATOM   592  N  N   . LEU A  1 77  ? 68.490  -1.559  24.815 1.00 14.55 ? 267 LEU A N   1 
ATOM   593  C  CA  . LEU A  1 77  ? 69.077  -0.865  25.952 1.00 14.61 ? 267 LEU A CA  1 
ATOM   594  C  C   . LEU A  1 77  ? 68.098  -0.916  27.115 1.00 15.56 ? 267 LEU A C   1 
ATOM   595  O  O   . LEU A  1 77  ? 68.465  -1.253  28.238 1.00 13.30 ? 267 LEU A O   1 
ATOM   596  C  CB  . LEU A  1 77  ? 69.367  0.591   25.607 1.00 12.85 ? 267 LEU A CB  1 
ATOM   597  C  CG  . LEU A  1 77  ? 69.934  1.399   26.775 1.00 12.22 ? 267 LEU A CG  1 
ATOM   598  C  CD1 . LEU A  1 77  ? 71.259  0.797   27.205 1.00 14.21 ? 267 LEU A CD1 1 
ATOM   599  C  CD2 . LEU A  1 77  ? 70.113  2.846   26.364 1.00 16.63 ? 267 LEU A CD2 1 
ATOM   600  N  N   . ASN A  1 78  ? 66.845  -0.583  26.828 1.00 16.67 ? 268 ASN A N   1 
ATOM   601  C  CA  . ASN A  1 78  ? 65.796  -0.584  27.836 1.00 17.27 ? 268 ASN A CA  1 
ATOM   602  C  C   . ASN A  1 78  ? 65.579  -1.965  28.443 1.00 17.14 ? 268 ASN A C   1 
ATOM   603  O  O   . ASN A  1 78  ? 65.450  -2.101  29.659 1.00 16.19 ? 268 ASN A O   1 
ATOM   604  C  CB  . ASN A  1 78  ? 64.482  -0.106  27.232 1.00 16.97 ? 268 ASN A CB  1 
ATOM   605  C  CG  . ASN A  1 78  ? 63.396  0.005   28.261 1.00 16.65 ? 268 ASN A CG  1 
ATOM   606  O  OD1 . ASN A  1 78  ? 63.384  0.936   29.068 1.00 18.06 ? 268 ASN A OD1 1 
ATOM   607  N  ND2 . ASN A  1 78  ? 62.486  -0.960  28.264 1.00 18.40 ? 268 ASN A ND2 1 
ATOM   608  N  N   . ALA A  1 79  ? 65.521  -2.984  27.589 1.00 15.84 ? 269 ALA A N   1 
ATOM   609  C  CA  . ALA A  1 79  ? 65.327  -4.356  28.047 1.00 13.74 ? 269 ALA A CA  1 
ATOM   610  C  C   . ALA A  1 79  ? 66.522  -4.792  28.887 1.00 15.02 ? 269 ALA A C   1 
ATOM   611  O  O   . ALA A  1 79  ? 66.360  -5.421  29.929 1.00 22.79 ? 269 ALA A O   1 
ATOM   612  C  CB  . ALA A  1 79  ? 65.151  -5.294  26.856 1.00 8.19  ? 269 ALA A CB  1 
ATOM   613  N  N   . PHE A  1 80  ? 67.725  -4.458  28.436 1.00 13.60 ? 270 PHE A N   1 
ATOM   614  C  CA  . PHE A  1 80  ? 68.924  -4.823  29.181 1.00 12.75 ? 270 PHE A CA  1 
ATOM   615  C  C   . PHE A  1 80  ? 68.967  -4.107  30.529 1.00 14.60 ? 270 PHE A C   1 
ATOM   616  O  O   . PHE A  1 80  ? 69.497  -4.636  31.508 1.00 10.94 ? 270 PHE A O   1 
ATOM   617  C  CB  . PHE A  1 80  ? 70.180  -4.469  28.389 1.00 5.51  ? 270 PHE A CB  1 
ATOM   618  C  CG  . PHE A  1 80  ? 71.449  -4.863  29.076 1.00 11.47 ? 270 PHE A CG  1 
ATOM   619  C  CD1 . PHE A  1 80  ? 71.712  -6.202  29.359 1.00 10.96 ? 270 PHE A CD1 1 
ATOM   620  C  CD2 . PHE A  1 80  ? 72.378  -3.898  29.454 1.00 13.76 ? 270 PHE A CD2 1 
ATOM   621  C  CE1 . PHE A  1 80  ? 72.881  -6.575  30.009 1.00 13.67 ? 270 PHE A CE1 1 
ATOM   622  C  CE2 . PHE A  1 80  ? 73.551  -4.258  30.104 1.00 14.83 ? 270 PHE A CE2 1 
ATOM   623  C  CZ  . PHE A  1 80  ? 73.806  -5.600  30.383 1.00 19.81 ? 270 PHE A CZ  1 
ATOM   624  N  N   . GLY A  1 81  ? 68.414  -2.897  30.569 1.00 17.21 ? 271 GLY A N   1 
ATOM   625  C  CA  . GLY A  1 81  ? 68.394  -2.126  31.799 1.00 17.08 ? 271 GLY A CA  1 
ATOM   626  C  C   . GLY A  1 81  ? 67.489  -2.757  32.841 1.00 19.87 ? 271 GLY A C   1 
ATOM   627  O  O   . GLY A  1 81  ? 67.905  -2.989  33.980 1.00 17.54 ? 271 GLY A O   1 
ATOM   628  N  N   . GLU A  1 82  ? 66.248  -3.033  32.448 1.00 16.60 ? 272 GLU A N   1 
ATOM   629  C  CA  . GLU A  1 82  ? 65.274  -3.648  33.339 1.00 18.79 ? 272 GLU A CA  1 
ATOM   630  C  C   . GLU A  1 82  ? 65.822  -4.969  33.854 1.00 16.73 ? 272 GLU A C   1 
ATOM   631  O  O   . GLU A  1 82  ? 65.660  -5.307  35.024 1.00 19.65 ? 272 GLU A O   1 
ATOM   632  C  CB  . GLU A  1 82  ? 63.960  -3.911  32.597 1.00 21.49 ? 272 GLU A CB  1 
ATOM   633  C  CG  . GLU A  1 82  ? 63.222  -2.663  32.131 1.00 29.84 ? 272 GLU A CG  1 
ATOM   634  C  CD  . GLU A  1 82  ? 62.600  -1.872  33.271 1.00 31.87 ? 272 GLU A CD  1 
ATOM   635  O  OE1 . GLU A  1 82  ? 61.932  -0.856  32.983 1.00 30.09 ? 272 GLU A OE1 1 
ATOM   636  O  OE2 . GLU A  1 82  ? 62.775  -2.263  34.447 1.00 35.65 ? 272 GLU A OE2 1 
ATOM   637  N  N   . TRP A  1 83  ? 66.469  -5.714  32.966 1.00 16.09 ? 273 TRP A N   1 
ATOM   638  C  CA  . TRP A  1 83  ? 67.039  -7.004  33.322 1.00 17.50 ? 273 TRP A CA  1 
ATOM   639  C  C   . TRP A  1 83  ? 68.102  -6.865  34.410 1.00 20.26 ? 273 TRP A C   1 
ATOM   640  O  O   . TRP A  1 83  ? 68.187  -7.694  35.315 1.00 21.31 ? 273 TRP A O   1 
ATOM   641  C  CB  . TRP A  1 83  ? 67.649  -7.671  32.089 1.00 13.64 ? 273 TRP A CB  1 
ATOM   642  C  CG  . TRP A  1 83  ? 68.223  -9.011  32.385 1.00 21.20 ? 273 TRP A CG  1 
ATOM   643  C  CD1 . TRP A  1 83  ? 67.534  -10.166 32.626 1.00 21.22 ? 273 TRP A CD1 1 
ATOM   644  C  CD2 . TRP A  1 83  ? 69.611  -9.328  32.553 1.00 21.81 ? 273 TRP A CD2 1 
ATOM   645  N  NE1 . TRP A  1 83  ? 68.407  -11.182 32.939 1.00 23.73 ? 273 TRP A NE1 1 
ATOM   646  C  CE2 . TRP A  1 83  ? 69.687  -10.694 32.903 1.00 22.12 ? 273 TRP A CE2 1 
ATOM   647  C  CE3 . TRP A  1 83  ? 70.796  -8.587  32.449 1.00 18.96 ? 273 TRP A CE3 1 
ATOM   648  C  CZ2 . TRP A  1 83  ? 70.904  -11.336 33.148 1.00 27.47 ? 273 TRP A CZ2 1 
ATOM   649  C  CZ3 . TRP A  1 83  ? 72.008  -9.226  32.693 1.00 19.47 ? 273 TRP A CZ3 1 
ATOM   650  C  CH2 . TRP A  1 83  ? 72.051  -10.587 33.040 1.00 28.99 ? 273 TRP A CH2 1 
ATOM   651  N  N   . ARG A  1 84  ? 68.914  -5.818  34.322 1.00 23.55 ? 274 ARG A N   1 
ATOM   652  C  CA  . ARG A  1 84  ? 69.962  -5.597  35.312 1.00 26.56 ? 274 ARG A CA  1 
ATOM   653  C  C   . ARG A  1 84  ? 69.353  -5.295  36.683 1.00 30.20 ? 274 ARG A C   1 
ATOM   654  O  O   . ARG A  1 84  ? 69.806  -5.817  37.701 1.00 32.97 ? 274 ARG A O   1 
ATOM   655  C  CB  . ARG A  1 84  ? 70.861  -4.431  34.892 1.00 20.53 ? 274 ARG A CB  1 
ATOM   656  C  CG  . ARG A  1 84  ? 72.133  -4.336  35.712 1.00 18.58 ? 274 ARG A CG  1 
ATOM   657  C  CD  . ARG A  1 84  ? 72.468  -2.905  36.079 1.00 21.08 ? 274 ARG A CD  1 
ATOM   658  N  NE  . ARG A  1 84  ? 73.614  -2.839  36.982 1.00 19.56 ? 274 ARG A NE  1 
ATOM   659  C  CZ  . ARG A  1 84  ? 73.934  -1.775  37.712 1.00 22.40 ? 274 ARG A CZ  1 
ATOM   660  N  NH1 . ARG A  1 84  ? 73.193  -0.676  37.655 1.00 21.93 ? 274 ARG A NH1 1 
ATOM   661  N  NH2 . ARG A  1 84  ? 75.001  -1.809  38.500 1.00 17.97 ? 274 ARG A NH2 1 
ATOM   662  N  N   . LYS A  1 85  ? 68.322  -4.455  36.695 1.00 29.03 ? 275 LYS A N   1 
ATOM   663  C  CA  . LYS A  1 85  ? 67.649  -4.060  37.927 1.00 30.79 ? 275 LYS A CA  1 
ATOM   664  C  C   . LYS A  1 85  ? 66.856  -5.164  38.624 1.00 29.82 ? 275 LYS A C   1 
ATOM   665  O  O   . LYS A  1 85  ? 66.844  -5.241  39.851 1.00 29.11 ? 275 LYS A O   1 
ATOM   666  C  CB  . LYS A  1 85  ? 66.699  -2.891  37.655 1.00 35.34 ? 275 LYS A CB  1 
ATOM   667  C  CG  . LYS A  1 85  ? 65.843  -2.508  38.859 1.00 39.61 ? 275 LYS A CG  1 
ATOM   668  C  CD  . LYS A  1 85  ? 64.560  -1.795  38.448 1.00 46.22 ? 275 LYS A CD  1 
ATOM   669  C  CE  . LYS A  1 85  ? 64.832  -0.432  37.838 1.00 52.36 ? 275 LYS A CE  1 
ATOM   670  N  NZ  . LYS A  1 85  ? 65.461  0.500   38.820 1.00 59.81 ? 275 LYS A NZ  1 
ATOM   671  N  N   . THR A  1 86  ? 66.191  -6.011  37.847 1.00 28.60 ? 276 THR A N   1 
ATOM   672  C  CA  . THR A  1 86  ? 65.369  -7.071  38.424 1.00 31.54 ? 276 THR A CA  1 
ATOM   673  C  C   . THR A  1 86  ? 66.003  -8.456  38.485 1.00 29.94 ? 276 THR A C   1 
ATOM   674  O  O   . THR A  1 86  ? 65.433  -9.361  39.091 1.00 32.10 ? 276 THR A O   1 
ATOM   675  C  CB  . THR A  1 86  ? 64.030  -7.209  37.663 1.00 31.68 ? 276 THR A CB  1 
ATOM   676  O  OG1 . THR A  1 86  ? 64.276  -7.720  36.346 1.00 34.29 ? 276 THR A OG1 1 
ATOM   677  C  CG2 . THR A  1 86  ? 63.342  -5.859  37.545 1.00 33.14 ? 276 THR A CG2 1 
ATOM   678  N  N   . ASP A  1 87  ? 67.171  -8.628  37.875 1.00 27.69 ? 277 ASP A N   1 
ATOM   679  C  CA  . ASP A  1 87  ? 67.814  -9.935  37.866 1.00 27.02 ? 277 ASP A CA  1 
ATOM   680  C  C   . ASP A  1 87  ? 69.291  -9.924  38.242 1.00 28.77 ? 277 ASP A C   1 
ATOM   681  O  O   . ASP A  1 87  ? 69.667  -10.411 39.305 1.00 31.93 ? 277 ASP A O   1 
ATOM   682  C  CB  . ASP A  1 87  ? 67.634  -10.581 36.486 1.00 29.87 ? 277 ASP A CB  1 
ATOM   683  C  CG  . ASP A  1 87  ? 68.073  -12.040 36.451 1.00 31.49 ? 277 ASP A CG  1 
ATOM   684  O  OD1 . ASP A  1 87  ? 67.751  -12.727 35.459 1.00 28.44 ? 277 ASP A OD1 1 
ATOM   685  O  OD2 . ASP A  1 87  ? 68.738  -12.501 37.405 1.00 31.81 ? 277 ASP A OD2 1 
ATOM   686  N  N   . LEU A  1 88  ? 70.130  -9.375  37.372 1.00 28.94 ? 278 LEU A N   1 
ATOM   687  C  CA  . LEU A  1 88  ? 71.567  -9.338  37.630 1.00 31.02 ? 278 LEU A CA  1 
ATOM   688  C  C   . LEU A  1 88  ? 71.966  -8.692  38.960 1.00 33.12 ? 278 LEU A C   1 
ATOM   689  O  O   . LEU A  1 88  ? 72.578  -9.334  39.819 1.00 28.08 ? 278 LEU A O   1 
ATOM   690  C  CB  . LEU A  1 88  ? 72.287  -8.615  36.490 1.00 27.48 ? 278 LEU A CB  1 
ATOM   691  C  CG  . LEU A  1 88  ? 73.812  -8.597  36.606 1.00 18.08 ? 278 LEU A CG  1 
ATOM   692  C  CD1 . LEU A  1 88  ? 74.325  -10.020 36.596 1.00 15.99 ? 278 LEU A CD1 1 
ATOM   693  C  CD2 . LEU A  1 88  ? 74.414  -7.804  35.460 1.00 22.12 ? 278 LEU A CD2 1 
ATOM   694  N  N   . LEU A  1 89  ? 71.620  -7.418  39.117 1.00 34.44 ? 279 LEU A N   1 
ATOM   695  C  CA  . LEU A  1 89  ? 71.956  -6.661  40.319 1.00 32.88 ? 279 LEU A CA  1 
ATOM   696  C  C   . LEU A  1 89  ? 71.418  -7.307  41.594 1.00 33.78 ? 279 LEU A C   1 
ATOM   697  O  O   . LEU A  1 89  ? 71.823  -6.946  42.700 1.00 35.01 ? 279 LEU A O   1 
ATOM   698  C  CB  . LEU A  1 89  ? 71.417  -5.234  40.191 1.00 31.32 ? 279 LEU A CB  1 
ATOM   699  C  CG  . LEU A  1 89  ? 71.986  -4.155  41.113 1.00 31.99 ? 279 LEU A CG  1 
ATOM   700  C  CD1 . LEU A  1 89  ? 73.498  -4.051  40.929 1.00 26.88 ? 279 LEU A CD1 1 
ATOM   701  C  CD2 . LEU A  1 89  ? 71.320  -2.827  40.793 1.00 29.50 ? 279 LEU A CD2 1 
ATOM   702  N  N   . THR A  1 90  ? 70.516  -8.269  41.433 1.00 31.63 ? 280 THR A N   1 
ATOM   703  C  CA  . THR A  1 90  ? 69.919  -8.954  42.572 1.00 31.95 ? 280 THR A CA  1 
ATOM   704  C  C   . THR A  1 90  ? 70.791  -10.106 43.071 1.00 31.35 ? 280 THR A C   1 
ATOM   705  O  O   . THR A  1 90  ? 70.589  -10.609 44.174 1.00 34.22 ? 280 THR A O   1 
ATOM   706  C  CB  . THR A  1 90  ? 68.508  -9.500  42.211 1.00 33.33 ? 280 THR A CB  1 
ATOM   707  O  OG1 . THR A  1 90  ? 67.632  -9.338  43.332 1.00 37.72 ? 280 THR A OG1 1 
ATOM   708  C  CG2 . THR A  1 90  ? 68.569  -10.982 41.853 1.00 29.59 ? 280 THR A CG2 1 
ATOM   709  N  N   . ARG A  1 91  ? 71.760  -10.520 42.261 1.00 29.96 ? 281 ARG A N   1 
ATOM   710  C  CA  . ARG A  1 91  ? 72.642  -11.620 42.636 1.00 29.56 ? 281 ARG A CA  1 
ATOM   711  C  C   . ARG A  1 91  ? 74.122  -11.284 42.464 1.00 33.11 ? 281 ARG A C   1 
ATOM   712  O  O   . ARG A  1 91  ? 74.989  -12.145 42.628 1.00 32.84 ? 281 ARG A O   1 
ATOM   713  C  CB  . ARG A  1 91  ? 72.291  -12.864 41.817 1.00 28.83 ? 281 ARG A CB  1 
ATOM   714  C  CG  . ARG A  1 91  ? 72.248  -12.625 40.319 1.00 28.56 ? 281 ARG A CG  1 
ATOM   715  C  CD  . ARG A  1 91  ? 71.591  -13.786 39.586 1.00 28.84 ? 281 ARG A CD  1 
ATOM   716  N  NE  . ARG A  1 91  ? 71.412  -13.491 38.166 1.00 30.43 ? 281 ARG A NE  1 
ATOM   717  C  CZ  . ARG A  1 91  ? 72.413  -13.297 37.313 1.00 29.50 ? 281 ARG A CZ  1 
ATOM   718  N  NH1 . ARG A  1 91  ? 73.668  -13.369 37.734 1.00 34.27 ? 281 ARG A NH1 1 
ATOM   719  N  NH2 . ARG A  1 91  ? 72.160  -13.024 36.040 1.00 28.68 ? 281 ARG A NH2 1 
ATOM   720  N  N   . LYS A  1 92  ? 74.409  -10.031 42.127 1.00 32.25 ? 282 LYS A N   1 
ATOM   721  C  CA  . LYS A  1 92  ? 75.789  -9.596  41.955 1.00 33.07 ? 282 LYS A CA  1 
ATOM   722  C  C   . LYS A  1 92  ? 75.848  -8.086  42.079 1.00 31.54 ? 282 LYS A C   1 
ATOM   723  O  O   . LYS A  1 92  ? 75.254  -7.368  41.279 1.00 34.82 ? 282 LYS A O   1 
ATOM   724  C  CB  . LYS A  1 92  ? 76.328  -10.015 40.585 1.00 35.81 ? 282 LYS A CB  1 
ATOM   725  C  CG  . LYS A  1 92  ? 77.801  -10.429 40.595 1.00 39.82 ? 282 LYS A CG  1 
ATOM   726  C  CD  . LYS A  1 92  ? 78.696  -9.417  41.301 1.00 32.01 ? 282 LYS A CD  1 
ATOM   727  C  CE  . LYS A  1 92  ? 80.136  -9.916  41.352 1.00 39.34 ? 282 LYS A CE  1 
ATOM   728  N  NZ  . LYS A  1 92  ? 81.039  -9.013  42.124 1.00 41.20 ? 282 LYS A NZ  1 
ATOM   729  N  N   . LYS A  1 93  ? 76.566  -7.608  43.087 1.00 30.87 ? 283 LYS A N   1 
ATOM   730  C  CA  . LYS A  1 93  ? 76.691  -6.179  43.316 1.00 30.54 ? 283 LYS A CA  1 
ATOM   731  C  C   . LYS A  1 93  ? 77.767  -5.567  42.428 1.00 29.00 ? 283 LYS A C   1 
ATOM   732  O  O   . LYS A  1 93  ? 78.935  -5.944  42.493 1.00 27.14 ? 283 LYS A O   1 
ATOM   733  C  CB  . LYS A  1 93  ? 76.996  -5.907  44.793 1.00 34.95 ? 283 LYS A CB  1 
ATOM   734  C  CG  . LYS A  1 93  ? 75.817  -6.171  45.734 1.00 43.78 ? 283 LYS A CG  1 
ATOM   735  C  CD  . LYS A  1 93  ? 75.399  -7.642  45.741 1.00 49.83 ? 283 LYS A CD  1 
ATOM   736  C  CE  . LYS A  1 93  ? 74.126  -7.874  46.554 1.00 50.45 ? 283 LYS A CE  1 
ATOM   737  N  NZ  . LYS A  1 93  ? 74.281  -7.505  47.990 1.00 50.87 ? 283 LYS A NZ  1 
ATOM   738  N  N   . HIS A  1 94  ? 77.353  -4.629  41.584 1.00 26.56 ? 284 HIS A N   1 
ATOM   739  C  CA  . HIS A  1 94  ? 78.262  -3.945  40.678 1.00 24.26 ? 284 HIS A CA  1 
ATOM   740  C  C   . HIS A  1 94  ? 77.743  -2.537  40.418 1.00 22.46 ? 284 HIS A C   1 
ATOM   741  O  O   . HIS A  1 94  ? 76.596  -2.224  40.725 1.00 25.16 ? 284 HIS A O   1 
ATOM   742  C  CB  . HIS A  1 94  ? 78.381  -4.711  39.361 1.00 24.80 ? 284 HIS A CB  1 
ATOM   743  C  CG  . HIS A  1 94  ? 77.085  -4.859  38.628 1.00 21.50 ? 284 HIS A CG  1 
ATOM   744  N  ND1 . HIS A  1 94  ? 76.039  -5.616  39.111 1.00 18.61 ? 284 HIS A ND1 1 
ATOM   745  C  CD2 . HIS A  1 94  ? 76.666  -4.348  37.447 1.00 19.82 ? 284 HIS A CD2 1 
ATOM   746  C  CE1 . HIS A  1 94  ? 75.032  -5.566  38.257 1.00 20.88 ? 284 HIS A CE1 1 
ATOM   747  N  NE2 . HIS A  1 94  ? 75.387  -4.804  37.239 1.00 20.58 ? 284 HIS A NE2 1 
ATOM   748  N  N   . ASP A  1 95  ? 78.584  -1.695  39.837 1.00 24.79 ? 285 ASP A N   1 
ATOM   749  C  CA  . ASP A  1 95  ? 78.212  -0.309  39.578 1.00 26.24 ? 285 ASP A CA  1 
ATOM   750  C  C   . ASP A  1 95  ? 77.683  -0.040  38.173 1.00 27.24 ? 285 ASP A C   1 
ATOM   751  O  O   . ASP A  1 95  ? 76.811  0.808   37.987 1.00 32.65 ? 285 ASP A O   1 
ATOM   752  C  CB  . ASP A  1 95  ? 79.423  0.588   39.834 1.00 23.72 ? 285 ASP A CB  1 
ATOM   753  C  CG  . ASP A  1 95  ? 80.084  0.299   41.163 1.00 26.09 ? 285 ASP A CG  1 
ATOM   754  O  OD1 . ASP A  1 95  ? 81.309  0.510   41.276 1.00 21.89 ? 285 ASP A OD1 1 
ATOM   755  O  OD2 . ASP A  1 95  ? 79.377  -0.134  42.098 1.00 31.87 ? 285 ASP A OD2 1 
ATOM   756  N  N   . ASN A  1 96  ? 78.200  -0.768  37.189 1.00 26.41 ? 286 ASN A N   1 
ATOM   757  C  CA  . ASN A  1 96  ? 77.800  -0.553  35.805 1.00 21.53 ? 286 ASN A CA  1 
ATOM   758  C  C   . ASN A  1 96  ? 77.827  -1.860  35.012 1.00 21.98 ? 286 ASN A C   1 
ATOM   759  O  O   . ASN A  1 96  ? 78.639  -2.744  35.293 1.00 23.60 ? 286 ASN A O   1 
ATOM   760  C  CB  . ASN A  1 96  ? 78.753  0.480   35.195 1.00 16.30 ? 286 ASN A CB  1 
ATOM   761  C  CG  . ASN A  1 96  ? 78.287  0.998   33.859 1.00 18.80 ? 286 ASN A CG  1 
ATOM   762  O  OD1 . ASN A  1 96  ? 78.601  0.428   32.813 1.00 16.30 ? 286 ASN A OD1 1 
ATOM   763  N  ND2 . ASN A  1 96  ? 77.528  2.090   33.884 1.00 11.02 ? 286 ASN A ND2 1 
ATOM   764  N  N   . ALA A  1 97  ? 76.933  -1.983  34.031 1.00 19.31 ? 287 ALA A N   1 
ATOM   765  C  CA  . ALA A  1 97  ? 76.864  -3.188  33.200 1.00 16.98 ? 287 ALA A CA  1 
ATOM   766  C  C   . ALA A  1 97  ? 76.730  -2.861  31.716 1.00 16.53 ? 287 ALA A C   1 
ATOM   767  O  O   . ALA A  1 97  ? 75.943  -1.999  31.325 1.00 19.29 ? 287 ALA A O   1 
ATOM   768  C  CB  . ALA A  1 97  ? 75.702  -4.067  33.640 1.00 6.05  ? 287 ALA A CB  1 
ATOM   769  N  N   . GLN A  1 98  ? 77.510  -3.560  30.897 1.00 15.24 ? 288 GLN A N   1 
ATOM   770  C  CA  . GLN A  1 98  ? 77.501  -3.364  29.456 1.00 12.71 ? 288 GLN A CA  1 
ATOM   771  C  C   . GLN A  1 98  ? 77.201  -4.690  28.759 1.00 16.99 ? 288 GLN A C   1 
ATOM   772  O  O   . GLN A  1 98  ? 77.668  -5.753  29.185 1.00 11.28 ? 288 GLN A O   1 
ATOM   773  C  CB  . GLN A  1 98  ? 78.861  -2.838  28.989 1.00 14.20 ? 288 GLN A CB  1 
ATOM   774  C  CG  . GLN A  1 98  ? 79.311  -1.562  29.676 1.00 24.25 ? 288 GLN A CG  1 
ATOM   775  C  CD  . GLN A  1 98  ? 78.523  -0.346  29.232 1.00 31.71 ? 288 GLN A CD  1 
ATOM   776  O  OE1 . GLN A  1 98  ? 78.592  0.715   29.853 1.00 36.20 ? 288 GLN A OE1 1 
ATOM   777  N  NE2 . GLN A  1 98  ? 77.776  -0.492  28.146 1.00 38.15 ? 288 GLN A NE2 1 
ATOM   778  N  N   . LEU A  1 99  ? 76.416  -4.621  27.689 1.00 19.88 ? 289 LEU A N   1 
ATOM   779  C  CA  . LEU A  1 99  ? 76.053  -5.804  26.916 1.00 16.34 ? 289 LEU A CA  1 
ATOM   780  C  C   . LEU A  1 99  ? 76.779  -5.792  25.581 1.00 15.23 ? 289 LEU A C   1 
ATOM   781  O  O   . LEU A  1 99  ? 76.612  -4.868  24.787 1.00 14.32 ? 289 LEU A O   1 
ATOM   782  C  CB  . LEU A  1 99  ? 74.550  -5.834  26.656 1.00 9.25  ? 289 LEU A CB  1 
ATOM   783  C  CG  . LEU A  1 99  ? 74.130  -6.956  25.705 1.00 12.66 ? 289 LEU A CG  1 
ATOM   784  C  CD1 . LEU A  1 99  ? 74.254  -8.285  26.423 1.00 15.01 ? 289 LEU A CD1 1 
ATOM   785  C  CD2 . LEU A  1 99  ? 72.702  -6.737  25.227 1.00 14.01 ? 289 LEU A CD2 1 
ATOM   786  N  N   . LEU A  1 100 ? 77.588  -6.815  25.334 1.00 14.76 ? 290 LEU A N   1 
ATOM   787  C  CA  . LEU A  1 100 ? 78.320  -6.900  24.076 1.00 15.03 ? 290 LEU A CA  1 
ATOM   788  C  C   . LEU A  1 100 ? 77.529  -7.802  23.144 1.00 13.87 ? 290 LEU A C   1 
ATOM   789  O  O   . LEU A  1 100 ? 77.394  -9.000  23.401 1.00 16.71 ? 290 LEU A O   1 
ATOM   790  C  CB  . LEU A  1 100 ? 79.716  -7.478  24.303 1.00 14.32 ? 290 LEU A CB  1 
ATOM   791  C  CG  . LEU A  1 100 ? 80.684  -7.332  23.129 1.00 15.91 ? 290 LEU A CG  1 
ATOM   792  C  CD1 . LEU A  1 100 ? 80.935  -5.856  22.861 1.00 13.33 ? 290 LEU A CD1 1 
ATOM   793  C  CD2 . LEU A  1 100 ? 81.993  -8.039  23.452 1.00 16.90 ? 290 LEU A CD2 1 
ATOM   794  N  N   . THR A  1 101 ? 77.001  -7.225  22.070 1.00 7.14  ? 291 THR A N   1 
ATOM   795  C  CA  . THR A  1 101 ? 76.203  -7.988  21.120 1.00 11.76 ? 291 THR A CA  1 
ATOM   796  C  C   . THR A  1 101 ? 76.852  -8.080  19.744 1.00 11.20 ? 291 THR A C   1 
ATOM   797  O  O   . THR A  1 101 ? 77.478  -7.130  19.277 1.00 10.91 ? 291 THR A O   1 
ATOM   798  C  CB  . THR A  1 101 ? 74.781  -7.372  20.965 1.00 12.74 ? 291 THR A CB  1 
ATOM   799  O  OG1 . THR A  1 101 ? 74.021  -8.133  20.015 1.00 7.29  ? 291 THR A OG1 1 
ATOM   800  C  CG2 . THR A  1 101 ? 74.874  -5.926  20.493 1.00 6.60  ? 291 THR A CG2 1 
ATOM   801  N  N   . ALA A  1 102 ? 76.687  -9.232  19.100 1.00 11.71 ? 292 ALA A N   1 
ATOM   802  C  CA  . ALA A  1 102 ? 77.244  -9.461  17.773 1.00 15.52 ? 292 ALA A CA  1 
ATOM   803  C  C   . ALA A  1 102 ? 76.210  -9.110  16.714 1.00 18.71 ? 292 ALA A C   1 
ATOM   804  O  O   . ALA A  1 102 ? 76.480  -9.183  15.515 1.00 25.35 ? 292 ALA A O   1 
ATOM   805  C  CB  . ALA A  1 102 ? 77.671  -10.919 17.624 1.00 7.84  ? 292 ALA A CB  1 
ATOM   806  N  N   . ILE A  1 103 ? 75.021  -8.730  17.165 1.00 13.81 ? 293 ILE A N   1 
ATOM   807  C  CA  . ILE A  1 103 ? 73.948  -8.369  16.252 1.00 16.53 ? 293 ILE A CA  1 
ATOM   808  C  C   . ILE A  1 103 ? 74.225  -7.017  15.600 1.00 21.39 ? 293 ILE A C   1 
ATOM   809  O  O   . ILE A  1 103 ? 74.843  -6.136  16.199 1.00 22.99 ? 293 ILE A O   1 
ATOM   810  C  CB  . ILE A  1 103 ? 72.595  -8.338  16.995 1.00 19.76 ? 293 ILE A CB  1 
ATOM   811  C  CG1 . ILE A  1 103 ? 72.227  -9.763  17.421 1.00 21.16 ? 293 ILE A CG1 1 
ATOM   812  C  CG2 . ILE A  1 103 ? 71.518  -7.725  16.115 1.00 16.79 ? 293 ILE A CG2 1 
ATOM   813  C  CD1 . ILE A  1 103 ? 70.898  -9.888  18.113 1.00 34.81 ? 293 ILE A CD1 1 
ATOM   814  N  N   . ASP A  1 104 ? 73.772  -6.859  14.363 1.00 19.57 ? 294 ASP A N   1 
ATOM   815  C  CA  . ASP A  1 104 ? 73.990  -5.619  13.641 1.00 20.35 ? 294 ASP A CA  1 
ATOM   816  C  C   . ASP A  1 104 ? 72.894  -4.613  13.973 1.00 20.73 ? 294 ASP A C   1 
ATOM   817  O  O   . ASP A  1 104 ? 71.820  -4.618  13.373 1.00 23.49 ? 294 ASP A O   1 
ATOM   818  C  CB  . ASP A  1 104 ? 74.040  -5.899  12.139 1.00 20.15 ? 294 ASP A CB  1 
ATOM   819  C  CG  . ASP A  1 104 ? 74.627  -4.749  11.356 1.00 24.00 ? 294 ASP A CG  1 
ATOM   820  O  OD1 . ASP A  1 104 ? 75.424  -3.979  11.938 1.00 22.72 ? 294 ASP A OD1 1 
ATOM   821  O  OD2 . ASP A  1 104 ? 74.303  -4.624  10.157 1.00 24.78 ? 294 ASP A OD2 1 
ATOM   822  N  N   . LEU A  1 105 ? 73.185  -3.753  14.942 1.00 22.12 ? 295 LEU A N   1 
ATOM   823  C  CA  . LEU A  1 105 ? 72.247  -2.738  15.406 1.00 21.89 ? 295 LEU A CA  1 
ATOM   824  C  C   . LEU A  1 105 ? 71.812  -1.777  14.305 1.00 23.37 ? 295 LEU A C   1 
ATOM   825  O  O   . LEU A  1 105 ? 72.546  -1.547  13.344 1.00 23.77 ? 295 LEU A O   1 
ATOM   826  C  CB  . LEU A  1 105 ? 72.878  -1.947  16.552 1.00 20.00 ? 295 LEU A CB  1 
ATOM   827  C  CG  . LEU A  1 105 ? 73.393  -2.765  17.737 1.00 20.45 ? 295 LEU A CG  1 
ATOM   828  C  CD1 . LEU A  1 105 ? 74.160  -1.853  18.683 1.00 22.07 ? 295 LEU A CD1 1 
ATOM   829  C  CD2 . LEU A  1 105 ? 72.229  -3.438  18.451 1.00 15.49 ? 295 LEU A CD2 1 
ATOM   830  N  N   . ASP A  1 106 ? 70.620  -1.208  14.454 1.00 22.38 ? 296 ASP A N   1 
ATOM   831  C  CA  . ASP A  1 106 ? 70.113  -0.272  13.460 1.00 26.49 ? 296 ASP A CA  1 
ATOM   832  C  C   . ASP A  1 106 ? 70.705  1.121   13.630 1.00 29.47 ? 296 ASP A C   1 
ATOM   833  O  O   . ASP A  1 106 ? 70.586  1.734   14.691 1.00 32.89 ? 296 ASP A O   1 
ATOM   834  C  CB  . ASP A  1 106 ? 68.584  -0.170  13.527 1.00 24.91 ? 296 ASP A CB  1 
ATOM   835  C  CG  . ASP A  1 106 ? 67.889  -1.482  13.208 1.00 30.41 ? 296 ASP A CG  1 
ATOM   836  O  OD1 . ASP A  1 106 ? 68.238  -2.119  12.193 1.00 30.25 ? 296 ASP A OD1 1 
ATOM   837  O  OD2 . ASP A  1 106 ? 66.978  -1.871  13.970 1.00 37.16 ? 296 ASP A OD2 1 
ATOM   838  N  N   . ARG A  1 107 ? 71.359  1.604   12.578 1.00 31.71 ? 297 ARG A N   1 
ATOM   839  C  CA  . ARG A  1 107 ? 71.942  2.942   12.563 1.00 29.12 ? 297 ARG A CA  1 
ATOM   840  C  C   . ARG A  1 107 ? 73.095  3.226   13.523 1.00 29.49 ? 297 ARG A C   1 
ATOM   841  O  O   . ARG A  1 107 ? 74.031  3.942   13.169 1.00 34.40 ? 297 ARG A O   1 
ATOM   842  C  CB  . ARG A  1 107 ? 70.834  3.967   12.790 1.00 25.23 ? 297 ARG A CB  1 
ATOM   843  C  CG  . ARG A  1 107 ? 69.716  3.873   11.768 1.00 25.05 ? 297 ARG A CG  1 
ATOM   844  C  CD  . ARG A  1 107 ? 68.623  4.870   12.073 1.00 25.84 ? 297 ARG A CD  1 
ATOM   845  N  NE  . ARG A  1 107 ? 67.954  4.562   13.330 1.00 20.71 ? 297 ARG A NE  1 
ATOM   846  C  CZ  . ARG A  1 107 ? 67.603  5.478   14.224 1.00 28.41 ? 297 ARG A CZ  1 
ATOM   847  N  NH1 . ARG A  1 107 ? 67.864  6.760   13.997 1.00 31.12 ? 297 ARG A NH1 1 
ATOM   848  N  NH2 . ARG A  1 107 ? 66.990  5.112   15.343 1.00 30.15 ? 297 ARG A NH2 1 
ATOM   849  N  N   . VAL A  1 108 ? 73.033  2.683   14.733 1.00 26.59 ? 298 VAL A N   1 
ATOM   850  C  CA  . VAL A  1 108 ? 74.090  2.916   15.712 1.00 19.84 ? 298 VAL A CA  1 
ATOM   851  C  C   . VAL A  1 108 ? 74.917  1.663   15.978 1.00 18.87 ? 298 VAL A C   1 
ATOM   852  O  O   . VAL A  1 108 ? 74.528  0.559   15.592 1.00 14.75 ? 298 VAL A O   1 
ATOM   853  C  CB  . VAL A  1 108 ? 73.504  3.401   17.053 1.00 18.66 ? 298 VAL A CB  1 
ATOM   854  C  CG1 . VAL A  1 108 ? 72.731  4.677   16.844 1.00 13.96 ? 298 VAL A CG1 1 
ATOM   855  C  CG2 . VAL A  1 108 ? 72.604  2.328   17.652 1.00 17.82 ? 298 VAL A CG2 1 
ATOM   856  N  N   . ILE A  1 109 ? 76.064  1.844   16.628 1.00 14.60 ? 299 ILE A N   1 
ATOM   857  C  CA  . ILE A  1 109 ? 76.930  0.721   16.971 1.00 14.32 ? 299 ILE A CA  1 
ATOM   858  C  C   . ILE A  1 109 ? 77.013  0.609   18.488 1.00 13.44 ? 299 ILE A C   1 
ATOM   859  O  O   . ILE A  1 109 ? 77.805  -0.168  19.024 1.00 8.00  ? 299 ILE A O   1 
ATOM   860  C  CB  . ILE A  1 109 ? 78.359  0.894   16.424 1.00 14.63 ? 299 ILE A CB  1 
ATOM   861  C  CG1 . ILE A  1 109 ? 78.949  2.215   16.922 1.00 13.52 ? 299 ILE A CG1 1 
ATOM   862  C  CG2 . ILE A  1 109 ? 78.349  0.805   14.910 1.00 9.05  ? 299 ILE A CG2 1 
ATOM   863  C  CD1 . ILE A  1 109 ? 80.423  2.371   16.614 1.00 18.96 ? 299 ILE A CD1 1 
ATOM   864  N  N   . GLY A  1 110 ? 76.186  1.399   19.166 1.00 10.58 ? 300 GLY A N   1 
ATOM   865  C  CA  . GLY A  1 110 ? 76.154  1.392   20.616 1.00 8.67  ? 300 GLY A CA  1 
ATOM   866  C  C   . GLY A  1 110 ? 75.065  2.314   21.131 1.00 10.19 ? 300 GLY A C   1 
ATOM   867  O  O   . GLY A  1 110 ? 74.514  3.108   20.371 1.00 11.00 ? 300 GLY A O   1 
ATOM   868  N  N   . LEU A  1 111 ? 74.750  2.211   22.418 1.00 7.25  ? 301 LEU A N   1 
ATOM   869  C  CA  . LEU A  1 111 ? 73.725  3.053   23.019 1.00 6.75  ? 301 LEU A CA  1 
ATOM   870  C  C   . LEU A  1 111 ? 73.794  2.978   24.541 1.00 11.33 ? 301 LEU A C   1 
ATOM   871  O  O   . LEU A  1 111 ? 74.016  1.905   25.105 1.00 13.85 ? 301 LEU A O   1 
ATOM   872  C  CB  . LEU A  1 111 ? 72.334  2.615   22.556 1.00 5.14  ? 301 LEU A CB  1 
ATOM   873  C  CG  . LEU A  1 111 ? 71.213  3.581   22.952 1.00 9.54  ? 301 LEU A CG  1 
ATOM   874  C  CD1 . LEU A  1 111 ? 71.389  4.890   22.180 1.00 1.00  ? 301 LEU A CD1 1 
ATOM   875  C  CD2 . LEU A  1 111 ? 69.855  2.961   22.658 1.00 6.47  ? 301 LEU A CD2 1 
ATOM   876  N  N   . ALA A  1 112 ? 73.595  4.116   25.203 1.00 11.45 ? 302 ALA A N   1 
ATOM   877  C  CA  . ALA A  1 112 ? 73.643  4.159   26.658 1.00 10.93 ? 302 ALA A CA  1 
ATOM   878  C  C   . ALA A  1 112 ? 73.012  5.419   27.226 1.00 12.83 ? 302 ALA A C   1 
ATOM   879  O  O   . ALA A  1 112 ? 73.129  6.494   26.644 1.00 18.41 ? 302 ALA A O   1 
ATOM   880  C  CB  . ALA A  1 112 ? 75.086  4.062   27.124 1.00 8.47  ? 302 ALA A CB  1 
ATOM   881  N  N   . TYR A  1 113 ? 72.347  5.275   28.370 1.00 12.21 ? 303 TYR A N   1 
ATOM   882  C  CA  . TYR A  1 113 ? 71.715  6.399   29.058 1.00 12.99 ? 303 TYR A CA  1 
ATOM   883  C  C   . TYR A  1 113 ? 72.808  7.404   29.461 1.00 16.76 ? 303 TYR A C   1 
ATOM   884  O  O   . TYR A  1 113 ? 73.968  7.024   29.629 1.00 18.86 ? 303 TYR A O   1 
ATOM   885  C  CB  . TYR A  1 113 ? 71.003  5.895   30.313 1.00 9.83  ? 303 TYR A CB  1 
ATOM   886  C  CG  . TYR A  1 113 ? 69.934  4.857   30.053 1.00 8.76  ? 303 TYR A CG  1 
ATOM   887  C  CD1 . TYR A  1 113 ? 68.722  5.208   29.461 1.00 6.36  ? 303 TYR A CD1 1 
ATOM   888  C  CD2 . TYR A  1 113 ? 70.134  3.521   30.402 1.00 14.80 ? 303 TYR A CD2 1 
ATOM   889  C  CE1 . TYR A  1 113 ? 67.734  4.259   29.224 1.00 8.01  ? 303 TYR A CE1 1 
ATOM   890  C  CE2 . TYR A  1 113 ? 69.152  2.560   30.170 1.00 13.74 ? 303 TYR A CE2 1 
ATOM   891  C  CZ  . TYR A  1 113 ? 67.954  2.936   29.579 1.00 11.88 ? 303 TYR A CZ  1 
ATOM   892  O  OH  . TYR A  1 113 ? 66.982  1.992   29.332 1.00 12.88 ? 303 TYR A OH  1 
ATOM   893  N  N   . VAL A  1 114 ? 72.449  8.676   29.623 1.00 16.13 ? 304 VAL A N   1 
ATOM   894  C  CA  . VAL A  1 114 ? 73.438  9.689   29.999 1.00 14.83 ? 304 VAL A CA  1 
ATOM   895  C  C   . VAL A  1 114 ? 73.358  10.104  31.467 1.00 17.72 ? 304 VAL A C   1 
ATOM   896  O  O   . VAL A  1 114 ? 72.268  10.230  32.031 1.00 14.73 ? 304 VAL A O   1 
ATOM   897  C  CB  . VAL A  1 114 ? 73.310  10.973  29.136 1.00 11.35 ? 304 VAL A CB  1 
ATOM   898  C  CG1 . VAL A  1 114 ? 73.537  10.650  27.668 1.00 10.42 ? 304 VAL A CG1 1 
ATOM   899  C  CG2 . VAL A  1 114 ? 71.947  11.596  29.339 1.00 22.45 ? 304 VAL A CG2 1 
ATOM   900  N  N   . GLY A  1 115 ? 74.526  10.323  32.069 1.00 19.76 ? 305 GLY A N   1 
ATOM   901  C  CA  . GLY A  1 115 ? 74.597  10.731  33.461 1.00 15.37 ? 305 GLY A CA  1 
ATOM   902  C  C   . GLY A  1 115 ? 73.733  9.857   34.338 1.00 15.52 ? 305 GLY A C   1 
ATOM   903  O  O   . GLY A  1 115 ? 72.870  10.352  35.058 1.00 11.09 ? 305 GLY A O   1 
ATOM   904  N  N   . SER A  1 116 ? 73.977  8.552   34.290 1.00 18.13 ? 306 SER A N   1 
ATOM   905  C  CA  . SER A  1 116 ? 73.190  7.607   35.063 1.00 17.59 ? 306 SER A CA  1 
ATOM   906  C  C   . SER A  1 116 ? 74.015  6.573   35.824 1.00 20.24 ? 306 SER A C   1 
ATOM   907  O  O   . SER A  1 116 ? 73.488  5.543   36.249 1.00 24.20 ? 306 SER A O   1 
ATOM   908  C  CB  . SER A  1 116 ? 72.214  6.904   34.127 1.00 20.34 ? 306 SER A CB  1 
ATOM   909  O  OG  . SER A  1 116 ? 72.875  6.515   32.938 1.00 24.81 ? 306 SER A OG  1 
ATOM   910  N  N   . MET A  1 117 ? 75.305  6.841   35.999 1.00 19.63 ? 307 MET A N   1 
ATOM   911  C  CA  . MET A  1 117 ? 76.171  5.916   36.721 1.00 19.26 ? 307 MET A CA  1 
ATOM   912  C  C   . MET A  1 117 ? 75.570  5.599   38.089 1.00 23.58 ? 307 MET A C   1 
ATOM   913  O  O   . MET A  1 117 ? 75.168  6.504   38.822 1.00 25.16 ? 307 MET A O   1 
ATOM   914  C  CB  . MET A  1 117 ? 77.566  6.522   36.898 1.00 17.93 ? 307 MET A CB  1 
ATOM   915  C  CG  . MET A  1 117 ? 78.569  5.615   37.601 1.00 18.34 ? 307 MET A CG  1 
ATOM   916  S  SD  . MET A  1 117 ? 78.885  4.058   36.723 1.00 21.64 ? 307 MET A SD  1 
ATOM   917  C  CE  . MET A  1 117 ? 79.664  4.676   35.222 1.00 13.25 ? 307 MET A CE  1 
ATOM   918  N  N   . CYS A  1 118 ? 75.506  4.308   38.410 1.00 23.52 ? 308 CYS A N   1 
ATOM   919  C  CA  . CYS A  1 118 ? 74.973  3.813   39.680 1.00 23.47 ? 308 CYS A CA  1 
ATOM   920  C  C   . CYS A  1 118 ? 73.472  3.553   39.697 1.00 21.18 ? 308 CYS A C   1 
ATOM   921  O  O   . CYS A  1 118 ? 72.989  2.815   40.549 1.00 22.79 ? 308 CYS A O   1 
ATOM   922  C  CB  . CYS A  1 118 ? 75.326  4.756   40.837 1.00 25.27 ? 308 CYS A CB  1 
ATOM   923  S  SG  . CYS A  1 118 ? 77.110  5.003   41.116 1.00 36.61 ? 308 CYS A SG  1 
ATOM   924  N  N   . HIS A  1 119 ? 72.723  4.155   38.780 1.00 22.53 ? 309 HIS A N   1 
ATOM   925  C  CA  . HIS A  1 119 ? 71.285  3.918   38.760 1.00 23.46 ? 309 HIS A CA  1 
ATOM   926  C  C   . HIS A  1 119 ? 71.046  2.446   38.451 1.00 25.79 ? 309 HIS A C   1 
ATOM   927  O  O   . HIS A  1 119 ? 71.602  1.909   37.493 1.00 29.16 ? 309 HIS A O   1 
ATOM   928  C  CB  . HIS A  1 119 ? 70.595  4.783   37.708 1.00 22.60 ? 309 HIS A CB  1 
ATOM   929  C  CG  . HIS A  1 119 ? 69.114  4.575   37.642 1.00 26.54 ? 309 HIS A CG  1 
ATOM   930  N  ND1 . HIS A  1 119 ? 68.548  3.399   37.197 1.00 29.47 ? 309 HIS A ND1 1 
ATOM   931  C  CD2 . HIS A  1 119 ? 68.083  5.379   37.991 1.00 26.23 ? 309 HIS A CD2 1 
ATOM   932  C  CE1 . HIS A  1 119 ? 67.232  3.488   37.273 1.00 28.17 ? 309 HIS A CE1 1 
ATOM   933  N  NE2 . HIS A  1 119 ? 66.924  4.680   37.752 1.00 30.60 ? 309 HIS A NE2 1 
ATOM   934  N  N   . PRO A  1 120 ? 70.212  1.772   39.259 1.00 26.79 ? 310 PRO A N   1 
ATOM   935  C  CA  . PRO A  1 120 ? 69.921  0.351   39.050 1.00 29.06 ? 310 PRO A CA  1 
ATOM   936  C  C   . PRO A  1 120 ? 69.611  -0.062  37.610 1.00 30.74 ? 310 PRO A C   1 
ATOM   937  O  O   . PRO A  1 120 ? 70.048  -1.123  37.160 1.00 31.73 ? 310 PRO A O   1 
ATOM   938  C  CB  . PRO A  1 120 ? 68.754  0.089   40.008 1.00 27.57 ? 310 PRO A CB  1 
ATOM   939  C  CG  . PRO A  1 120 ? 68.142  1.444   40.205 1.00 26.26 ? 310 PRO A CG  1 
ATOM   940  C  CD  . PRO A  1 120 ? 69.345  2.329   40.309 1.00 22.15 ? 310 PRO A CD  1 
ATOM   941  N  N   . LYS A  1 121 ? 68.876  0.776   36.885 1.00 29.54 ? 311 LYS A N   1 
ATOM   942  C  CA  . LYS A  1 121 ? 68.521  0.465   35.504 1.00 28.16 ? 311 LYS A CA  1 
ATOM   943  C  C   . LYS A  1 121 ? 69.328  1.233   34.460 1.00 27.51 ? 311 LYS A C   1 
ATOM   944  O  O   . LYS A  1 121 ? 69.834  0.651   33.498 1.00 28.36 ? 311 LYS A O   1 
ATOM   945  C  CB  . LYS A  1 121 ? 67.034  0.736   35.274 1.00 29.41 ? 311 LYS A CB  1 
ATOM   946  C  CG  . LYS A  1 121 ? 66.569  0.481   33.845 1.00 30.09 ? 311 LYS A CG  1 
ATOM   947  C  CD  . LYS A  1 121 ? 65.153  0.989   33.632 1.00 29.59 ? 311 LYS A CD  1 
ATOM   948  C  CE  . LYS A  1 121 ? 64.726  0.842   32.182 1.00 31.63 ? 311 LYS A CE  1 
ATOM   949  N  NZ  . LYS A  1 121 ? 63.390  1.449   31.934 1.00 28.58 ? 311 LYS A NZ  1 
ATOM   950  N  N   . ARG A  1 122 ? 69.447  2.542   34.652 1.00 26.80 ? 312 ARG A N   1 
ATOM   951  C  CA  . ARG A  1 122 ? 70.155  3.387   33.703 1.00 22.85 ? 312 ARG A CA  1 
ATOM   952  C  C   . ARG A  1 122 ? 71.679  3.386   33.747 1.00 21.75 ? 312 ARG A C   1 
ATOM   953  O  O   . ARG A  1 122 ? 72.321  4.104   32.985 1.00 20.92 ? 312 ARG A O   1 
ATOM   954  C  CB  . ARG A  1 122 ? 69.631  4.816   33.814 1.00 25.89 ? 312 ARG A CB  1 
ATOM   955  C  CG  . ARG A  1 122 ? 68.233  4.978   33.247 1.00 30.46 ? 312 ARG A CG  1 
ATOM   956  C  CD  . ARG A  1 122 ? 67.813  6.431   33.226 1.00 42.84 ? 312 ARG A CD  1 
ATOM   957  N  NE  . ARG A  1 122 ? 67.255  6.871   34.500 1.00 52.59 ? 312 ARG A NE  1 
ATOM   958  C  CZ  . ARG A  1 122 ? 66.042  6.543   34.934 1.00 58.10 ? 312 ARG A CZ  1 
ATOM   959  N  NH1 . ARG A  1 122 ? 65.256  5.772   34.192 1.00 58.14 ? 312 ARG A NH1 1 
ATOM   960  N  NH2 . ARG A  1 122 ? 65.612  6.990   36.109 1.00 58.01 ? 312 ARG A NH2 1 
ATOM   961  N  N   . SER A  1 123 ? 72.268  2.586   34.627 1.00 20.71 ? 313 SER A N   1 
ATOM   962  C  CA  . SER A  1 123 ? 73.723  2.519   34.694 1.00 19.41 ? 313 SER A CA  1 
ATOM   963  C  C   . SER A  1 123 ? 74.156  1.404   33.745 1.00 20.43 ? 313 SER A C   1 
ATOM   964  O  O   . SER A  1 123 ? 74.920  0.509   34.113 1.00 20.80 ? 313 SER A O   1 
ATOM   965  C  CB  . SER A  1 123 ? 74.185  2.210   36.119 1.00 14.14 ? 313 SER A CB  1 
ATOM   966  O  OG  . SER A  1 123 ? 75.590  2.367   36.240 1.00 14.88 ? 313 SER A OG  1 
ATOM   967  N  N   . THR A  1 124 ? 73.652  1.468   32.516 1.00 18.38 ? 314 THR A N   1 
ATOM   968  C  CA  . THR A  1 124 ? 73.955  0.459   31.512 1.00 21.98 ? 314 THR A CA  1 
ATOM   969  C  C   . THR A  1 124 ? 74.161  1.036   30.115 1.00 22.90 ? 314 THR A C   1 
ATOM   970  O  O   . THR A  1 124 ? 73.955  2.229   29.877 1.00 24.05 ? 314 THR A O   1 
ATOM   971  C  CB  . THR A  1 124 ? 72.827  -0.587  31.434 1.00 23.11 ? 314 THR A CB  1 
ATOM   972  O  OG1 . THR A  1 124 ? 71.563  0.084   31.353 1.00 21.69 ? 314 THR A OG1 1 
ATOM   973  C  CG2 . THR A  1 124 ? 72.847  -1.490  32.660 1.00 20.74 ? 314 THR A CG2 1 
ATOM   974  N  N   . GLY A  1 125 ? 74.573  0.165   29.198 1.00 18.37 ? 315 GLY A N   1 
ATOM   975  C  CA  . GLY A  1 125 ? 74.800  0.560   27.822 1.00 12.09 ? 315 GLY A CA  1 
ATOM   976  C  C   . GLY A  1 125 ? 75.006  -0.681  26.976 1.00 13.62 ? 315 GLY A C   1 
ATOM   977  O  O   . GLY A  1 125 ? 75.499  -1.690  27.477 1.00 13.73 ? 315 GLY A O   1 
ATOM   978  N  N   . ILE A  1 126 ? 74.610  -0.635  25.708 1.00 11.67 ? 316 ILE A N   1 
ATOM   979  C  CA  . ILE A  1 126 ? 74.809  -1.785  24.838 1.00 11.30 ? 316 ILE A CA  1 
ATOM   980  C  C   . ILE A  1 126 ? 75.896  -1.440  23.829 1.00 11.42 ? 316 ILE A C   1 
ATOM   981  O  O   . ILE A  1 126 ? 76.035  -0.287  23.425 1.00 13.17 ? 316 ILE A O   1 
ATOM   982  C  CB  . ILE A  1 126 ? 73.517  -2.188  24.091 1.00 9.34  ? 316 ILE A CB  1 
ATOM   983  C  CG1 . ILE A  1 126 ? 73.115  -1.103  23.097 1.00 13.01 ? 316 ILE A CG1 1 
ATOM   984  C  CG2 . ILE A  1 126 ? 72.404  -2.429  25.088 1.00 5.09  ? 316 ILE A CG2 1 
ATOM   985  C  CD1 . ILE A  1 126 ? 71.970  -1.518  22.191 1.00 21.64 ? 316 ILE A CD1 1 
ATOM   986  N  N   . ILE A  1 127 ? 76.663  -2.446  23.431 1.00 11.45 ? 317 ILE A N   1 
ATOM   987  C  CA  . ILE A  1 127 ? 77.761  -2.258  22.497 1.00 9.55  ? 317 ILE A CA  1 
ATOM   988  C  C   . ILE A  1 127 ? 77.763  -3.367  21.456 1.00 14.46 ? 317 ILE A C   1 
ATOM   989  O  O   . ILE A  1 127 ? 77.519  -4.531  21.782 1.00 16.04 ? 317 ILE A O   1 
ATOM   990  C  CB  . ILE A  1 127 ? 79.102  -2.295  23.255 1.00 13.46 ? 317 ILE A CB  1 
ATOM   991  C  CG1 . ILE A  1 127 ? 79.101  -1.222  24.346 1.00 13.58 ? 317 ILE A CG1 1 
ATOM   992  C  CG2 . ILE A  1 127 ? 80.265  -2.106  22.297 1.00 4.47  ? 317 ILE A CG2 1 
ATOM   993  C  CD1 . ILE A  1 127 ? 80.193  -1.408  25.369 1.00 20.61 ? 317 ILE A CD1 1 
ATOM   994  N  N   . GLN A  1 128 ? 78.043  -3.009  20.206 1.00 17.27 ? 318 GLN A N   1 
ATOM   995  C  CA  . GLN A  1 128 ? 78.090  -3.991  19.124 1.00 16.57 ? 318 GLN A CA  1 
ATOM   996  C  C   . GLN A  1 128 ? 79.531  -4.416  18.861 1.00 15.38 ? 318 GLN A C   1 
ATOM   997  O  O   . GLN A  1 128 ? 80.431  -3.579  18.864 1.00 12.53 ? 318 GLN A O   1 
ATOM   998  C  CB  . GLN A  1 128 ? 77.489  -3.407  17.840 1.00 13.08 ? 318 GLN A CB  1 
ATOM   999  C  CG  . GLN A  1 128 ? 77.674  -4.308  16.623 1.00 15.15 ? 318 GLN A CG  1 
ATOM   1000 C  CD  . GLN A  1 128 ? 77.010  -3.772  15.364 1.00 14.48 ? 318 GLN A CD  1 
ATOM   1001 O  OE1 . GLN A  1 128 ? 77.180  -4.328  14.279 1.00 12.46 ? 318 GLN A OE1 1 
ATOM   1002 N  NE2 . GLN A  1 128 ? 76.248  -2.693  15.503 1.00 8.80  ? 318 GLN A NE2 1 
ATOM   1003 N  N   . ASP A  1 129 ? 79.746  -5.714  18.643 1.00 16.49 ? 319 ASP A N   1 
ATOM   1004 C  CA  . ASP A  1 129 ? 81.084  -6.232  18.363 1.00 17.53 ? 319 ASP A CA  1 
ATOM   1005 C  C   . ASP A  1 129 ? 81.427  -5.844  16.924 1.00 20.44 ? 319 ASP A C   1 
ATOM   1006 O  O   . ASP A  1 129 ? 81.676  -6.687  16.063 1.00 23.04 ? 319 ASP A O   1 
ATOM   1007 C  CB  . ASP A  1 129 ? 81.116  -7.751  18.526 1.00 19.13 ? 319 ASP A CB  1 
ATOM   1008 C  CG  . ASP A  1 129 ? 82.532  -8.298  18.626 1.00 26.91 ? 319 ASP A CG  1 
ATOM   1009 O  OD1 . ASP A  1 129 ? 82.698  -9.535  18.572 1.00 33.11 ? 319 ASP A OD1 1 
ATOM   1010 O  OD2 . ASP A  1 129 ? 83.480  -7.496  18.767 1.00 22.60 ? 319 ASP A OD2 1 
ATOM   1011 N  N   . TYR A  1 130 ? 81.424  -4.535  16.703 1.00 23.67 ? 320 TYR A N   1 
ATOM   1012 C  CA  . TYR A  1 130 ? 81.684  -3.881  15.427 1.00 22.08 ? 320 TYR A CA  1 
ATOM   1013 C  C   . TYR A  1 130 ? 82.981  -4.264  14.703 1.00 22.42 ? 320 TYR A C   1 
ATOM   1014 O  O   . TYR A  1 130 ? 83.029  -4.242  13.472 1.00 22.41 ? 320 TYR A O   1 
ATOM   1015 C  CB  . TYR A  1 130 ? 81.641  -2.370  15.683 1.00 26.02 ? 320 TYR A CB  1 
ATOM   1016 C  CG  . TYR A  1 130 ? 81.880  -1.462  14.503 1.00 29.13 ? 320 TYR A CG  1 
ATOM   1017 C  CD1 . TYR A  1 130 ? 81.045  -1.490  13.390 1.00 34.98 ? 320 TYR A CD1 1 
ATOM   1018 C  CD2 . TYR A  1 130 ? 82.905  -0.516  14.535 1.00 32.26 ? 320 TYR A CD2 1 
ATOM   1019 C  CE1 . TYR A  1 130 ? 81.220  -0.593  12.336 1.00 40.97 ? 320 TYR A CE1 1 
ATOM   1020 C  CE2 . TYR A  1 130 ? 83.091  0.383   13.492 1.00 37.16 ? 320 TYR A CE2 1 
ATOM   1021 C  CZ  . TYR A  1 130 ? 82.245  0.341   12.395 1.00 42.74 ? 320 TYR A CZ  1 
ATOM   1022 O  OH  . TYR A  1 130 ? 82.425  1.236   11.361 1.00 49.23 ? 320 TYR A OH  1 
ATOM   1023 N  N   . SER A  1 131 ? 84.022  -4.625  15.450 1.00 18.97 ? 321 SER A N   1 
ATOM   1024 C  CA  . SER A  1 131 ? 85.303  -4.962  14.833 1.00 13.26 ? 321 SER A CA  1 
ATOM   1025 C  C   . SER A  1 131 ? 86.134  -6.000  15.575 1.00 17.49 ? 321 SER A C   1 
ATOM   1026 O  O   . SER A  1 131 ? 85.920  -6.256  16.759 1.00 20.60 ? 321 SER A O   1 
ATOM   1027 C  CB  . SER A  1 131 ? 86.134  -3.687  14.672 1.00 14.59 ? 321 SER A CB  1 
ATOM   1028 O  OG  . SER A  1 131 ? 87.499  -3.985  14.427 1.00 12.18 ? 321 SER A OG  1 
ATOM   1029 N  N   . GLU A  1 132 ? 87.092  -6.589  14.865 1.00 18.54 ? 322 GLU A N   1 
ATOM   1030 C  CA  . GLU A  1 132 ? 87.986  -7.586  15.445 1.00 20.61 ? 322 GLU A CA  1 
ATOM   1031 C  C   . GLU A  1 132 ? 89.154  -6.937  16.182 1.00 19.85 ? 322 GLU A C   1 
ATOM   1032 O  O   . GLU A  1 132 ? 89.836  -7.588  16.969 1.00 25.16 ? 322 GLU A O   1 
ATOM   1033 C  CB  . GLU A  1 132 ? 88.526  -8.521  14.360 1.00 24.71 ? 322 GLU A CB  1 
ATOM   1034 C  CG  . GLU A  1 132 ? 87.750  -9.823  14.243 1.00 42.49 ? 322 GLU A CG  1 
ATOM   1035 C  CD  . GLU A  1 132 ? 87.840  -10.670 15.506 1.00 49.99 ? 322 GLU A CD  1 
ATOM   1036 O  OE1 . GLU A  1 132 ? 87.077  -11.654 15.622 1.00 53.91 ? 322 GLU A OE1 1 
ATOM   1037 O  OE2 . GLU A  1 132 ? 88.679  -10.355 16.380 1.00 52.05 ? 322 GLU A OE2 1 
ATOM   1038 N  N   . ILE A  1 133 ? 89.381  -5.653  15.919 1.00 15.42 ? 323 ILE A N   1 
ATOM   1039 C  CA  . ILE A  1 133 ? 90.459  -4.913  16.561 1.00 10.73 ? 323 ILE A CA  1 
ATOM   1040 C  C   . ILE A  1 133 ? 90.055  -4.521  17.983 1.00 14.63 ? 323 ILE A C   1 
ATOM   1041 O  O   . ILE A  1 133 ? 89.319  -3.550  18.181 1.00 13.85 ? 323 ILE A O   1 
ATOM   1042 C  CB  . ILE A  1 133 ? 90.779  -3.626  15.790 1.00 11.05 ? 323 ILE A CB  1 
ATOM   1043 C  CG1 . ILE A  1 133 ? 91.036  -3.947  14.319 1.00 4.69  ? 323 ILE A CG1 1 
ATOM   1044 C  CG2 . ILE A  1 133 ? 91.987  -2.948  16.405 1.00 7.94  ? 323 ILE A CG2 1 
ATOM   1045 C  CD1 . ILE A  1 133 ? 91.208  -2.711  13.458 1.00 10.57 ? 323 ILE A CD1 1 
ATOM   1046 N  N   . ASN A  1 134 ? 90.549  -5.271  18.965 1.00 16.56 ? 324 ASN A N   1 
ATOM   1047 C  CA  . ASN A  1 134 ? 90.235  -5.016  20.367 1.00 14.27 ? 324 ASN A CA  1 
ATOM   1048 C  C   . ASN A  1 134 ? 90.109  -3.543  20.738 1.00 13.20 ? 324 ASN A C   1 
ATOM   1049 O  O   . ASN A  1 134 ? 89.160  -3.155  21.416 1.00 16.21 ? 324 ASN A O   1 
ATOM   1050 C  CB  . ASN A  1 134 ? 91.273  -5.680  21.272 1.00 12.23 ? 324 ASN A CB  1 
ATOM   1051 C  CG  . ASN A  1 134 ? 91.142  -7.190  21.293 1.00 18.26 ? 324 ASN A CG  1 
ATOM   1052 O  OD1 . ASN A  1 134 ? 90.035  -7.721  21.311 1.00 21.39 ? 324 ASN A OD1 1 
ATOM   1053 N  ND2 . ASN A  1 134 ? 92.270  -7.888  21.308 1.00 22.16 ? 324 ASN A ND2 1 
ATOM   1054 N  N   . LEU A  1 135 ? 91.053  -2.722  20.291 1.00 15.48 ? 325 LEU A N   1 
ATOM   1055 C  CA  . LEU A  1 135 ? 91.020  -1.297  20.610 1.00 16.51 ? 325 LEU A CA  1 
ATOM   1056 C  C   . LEU A  1 135 ? 89.737  -0.618  20.150 1.00 16.63 ? 325 LEU A C   1 
ATOM   1057 O  O   . LEU A  1 135 ? 89.170  0.201   20.874 1.00 20.59 ? 325 LEU A O   1 
ATOM   1058 C  CB  . LEU A  1 135 ? 92.230  -0.576  20.002 1.00 11.37 ? 325 LEU A CB  1 
ATOM   1059 C  CG  . LEU A  1 135 ? 92.197  0.954   20.096 1.00 11.56 ? 325 LEU A CG  1 
ATOM   1060 C  CD1 . LEU A  1 135 ? 91.967  1.393   21.531 1.00 4.73  ? 325 LEU A CD1 1 
ATOM   1061 C  CD2 . LEU A  1 135 ? 93.498  1.523   19.562 1.00 12.41 ? 325 LEU A CD2 1 
ATOM   1062 N  N   . VAL A  1 136 ? 89.277  -0.955  18.952 1.00 17.82 ? 326 VAL A N   1 
ATOM   1063 C  CA  . VAL A  1 136 ? 88.057  -0.354  18.429 1.00 14.64 ? 326 VAL A CA  1 
ATOM   1064 C  C   . VAL A  1 136 ? 86.875  -0.637  19.349 1.00 14.08 ? 326 VAL A C   1 
ATOM   1065 O  O   . VAL A  1 136 ? 86.118  0.274   19.691 1.00 19.03 ? 326 VAL A O   1 
ATOM   1066 C  CB  . VAL A  1 136 ? 87.738  -0.872  17.010 1.00 13.21 ? 326 VAL A CB  1 
ATOM   1067 C  CG1 . VAL A  1 136 ? 86.419  -0.311  16.537 1.00 1.00  ? 326 VAL A CG1 1 
ATOM   1068 C  CG2 . VAL A  1 136 ? 88.844  -0.461  16.050 1.00 14.44 ? 326 VAL A CG2 1 
ATOM   1069 N  N   . VAL A  1 137 ? 86.719  -1.891  19.759 1.00 6.86  ? 327 VAL A N   1 
ATOM   1070 C  CA  . VAL A  1 137 ? 85.613  -2.248  20.640 1.00 10.15 ? 327 VAL A CA  1 
ATOM   1071 C  C   . VAL A  1 137 ? 85.796  -1.618  22.018 1.00 15.48 ? 327 VAL A C   1 
ATOM   1072 O  O   . VAL A  1 137 ? 84.830  -1.158  22.632 1.00 15.84 ? 327 VAL A O   1 
ATOM   1073 C  CB  . VAL A  1 137 ? 85.471  -3.785  20.788 1.00 9.00  ? 327 VAL A CB  1 
ATOM   1074 C  CG1 . VAL A  1 137 ? 84.354  -4.120  21.770 1.00 1.00  ? 327 VAL A CG1 1 
ATOM   1075 C  CG2 . VAL A  1 137 ? 85.165  -4.407  19.430 1.00 1.00  ? 327 VAL A CG2 1 
ATOM   1076 N  N   . ALA A  1 138 ? 87.036  -1.590  22.499 1.00 16.30 ? 328 ALA A N   1 
ATOM   1077 C  CA  . ALA A  1 138 ? 87.321  -1.002  23.802 1.00 13.95 ? 328 ALA A CA  1 
ATOM   1078 C  C   . ALA A  1 138 ? 86.888  0.459   23.793 1.00 16.22 ? 328 ALA A C   1 
ATOM   1079 O  O   . ALA A  1 138 ? 86.246  0.932   24.734 1.00 16.24 ? 328 ALA A O   1 
ATOM   1080 C  CB  . ALA A  1 138 ? 88.804  -1.112  24.118 1.00 12.60 ? 328 ALA A CB  1 
ATOM   1081 N  N   . VAL A  1 139 ? 87.232  1.172   22.724 1.00 15.07 ? 329 VAL A N   1 
ATOM   1082 C  CA  . VAL A  1 139 ? 86.857  2.579   22.611 1.00 15.12 ? 329 VAL A CA  1 
ATOM   1083 C  C   . VAL A  1 139 ? 85.338  2.739   22.652 1.00 14.42 ? 329 VAL A C   1 
ATOM   1084 O  O   . VAL A  1 139 ? 84.833  3.637   23.319 1.00 15.08 ? 329 VAL A O   1 
ATOM   1085 C  CB  . VAL A  1 139 ? 87.408  3.216   21.307 1.00 16.44 ? 329 VAL A CB  1 
ATOM   1086 C  CG1 . VAL A  1 139 ? 86.927  4.654   21.181 1.00 2.92  ? 329 VAL A CG1 1 
ATOM   1087 C  CG2 . VAL A  1 139 ? 88.933  3.181   21.317 1.00 13.72 ? 329 VAL A CG2 1 
ATOM   1088 N  N   . ILE A  1 140 ? 84.609  1.872   21.951 1.00 12.99 ? 330 ILE A N   1 
ATOM   1089 C  CA  . ILE A  1 140 ? 83.148  1.951   21.956 1.00 14.74 ? 330 ILE A CA  1 
ATOM   1090 C  C   . ILE A  1 140 ? 82.626  1.722   23.377 1.00 14.65 ? 330 ILE A C   1 
ATOM   1091 O  O   . ILE A  1 140 ? 81.723  2.418   23.842 1.00 14.50 ? 330 ILE A O   1 
ATOM   1092 C  CB  . ILE A  1 140 ? 82.499  0.894   21.014 1.00 15.31 ? 330 ILE A CB  1 
ATOM   1093 C  CG1 . ILE A  1 140 ? 82.885  1.171   19.561 1.00 14.73 ? 330 ILE A CG1 1 
ATOM   1094 C  CG2 . ILE A  1 140 ? 80.983  0.938   21.142 1.00 4.26  ? 330 ILE A CG2 1 
ATOM   1095 C  CD1 . ILE A  1 140 ? 82.354  0.150   18.582 1.00 9.65  ? 330 ILE A CD1 1 
ATOM   1096 N  N   . MET A  1 141 ? 83.204  0.742   24.060 1.00 16.66 ? 331 MET A N   1 
ATOM   1097 C  CA  . MET A  1 141 ? 82.810  0.418   25.424 1.00 17.20 ? 331 MET A CA  1 
ATOM   1098 C  C   . MET A  1 141 ? 83.012  1.646   26.316 1.00 20.07 ? 331 MET A C   1 
ATOM   1099 O  O   . MET A  1 141 ? 82.102  2.054   27.043 1.00 20.74 ? 331 MET A O   1 
ATOM   1100 C  CB  . MET A  1 141 ? 83.649  -0.759  25.928 1.00 21.25 ? 331 MET A CB  1 
ATOM   1101 C  CG  . MET A  1 141 ? 83.085  -1.489  27.136 1.00 28.94 ? 331 MET A CG  1 
ATOM   1102 S  SD  . MET A  1 141 ? 83.949  -3.063  27.437 1.00 28.35 ? 331 MET A SD  1 
ATOM   1103 C  CE  . MET A  1 141 ? 83.367  -4.027  26.056 1.00 20.68 ? 331 MET A CE  1 
ATOM   1104 N  N   . ALA A  1 142 ? 84.201  2.240   26.242 1.00 16.99 ? 332 ALA A N   1 
ATOM   1105 C  CA  . ALA A  1 142 ? 84.523  3.427   27.032 1.00 15.21 ? 332 ALA A CA  1 
ATOM   1106 C  C   . ALA A  1 142 ? 83.557  4.560   26.713 1.00 16.79 ? 332 ALA A C   1 
ATOM   1107 O  O   . ALA A  1 142 ? 83.026  5.213   27.614 1.00 15.32 ? 332 ALA A O   1 
ATOM   1108 C  CB  . ALA A  1 142 ? 85.952  3.874   26.746 1.00 15.64 ? 332 ALA A CB  1 
ATOM   1109 N  N   . HIS A  1 143 ? 83.346  4.784   25.418 1.00 17.41 ? 333 HIS A N   1 
ATOM   1110 C  CA  . HIS A  1 143 ? 82.452  5.827   24.930 1.00 15.37 ? 333 HIS A CA  1 
ATOM   1111 C  C   . HIS A  1 143 ? 81.074  5.704   25.577 1.00 20.39 ? 333 HIS A C   1 
ATOM   1112 O  O   . HIS A  1 143 ? 80.523  6.688   26.072 1.00 24.74 ? 333 HIS A O   1 
ATOM   1113 C  CB  . HIS A  1 143 ? 82.318  5.718   23.410 1.00 13.36 ? 333 HIS A CB  1 
ATOM   1114 C  CG  . HIS A  1 143 ? 81.449  6.772   22.795 1.00 13.28 ? 333 HIS A CG  1 
ATOM   1115 N  ND1 . HIS A  1 143 ? 81.962  7.887   22.167 1.00 7.67  ? 333 HIS A ND1 1 
ATOM   1116 C  CD2 . HIS A  1 143 ? 80.101  6.871   22.698 1.00 7.48  ? 333 HIS A CD2 1 
ATOM   1117 C  CE1 . HIS A  1 143 ? 80.967  8.626   21.707 1.00 7.65  ? 333 HIS A CE1 1 
ATOM   1118 N  NE2 . HIS A  1 143 ? 79.828  8.032   22.016 1.00 6.58  ? 333 HIS A NE2 1 
ATOM   1119 N  N   . GLU A  1 144 ? 80.521  4.494   25.574 1.00 19.15 ? 334 GLU A N   1 
ATOM   1120 C  CA  . GLU A  1 144 ? 79.206  4.274   26.159 1.00 20.35 ? 334 GLU A CA  1 
ATOM   1121 C  C   . GLU A  1 144 ? 79.204  4.480   27.671 1.00 20.78 ? 334 GLU A C   1 
ATOM   1122 O  O   . GLU A  1 144 ? 78.226  4.977   28.233 1.00 20.29 ? 334 GLU A O   1 
ATOM   1123 C  CB  . GLU A  1 144 ? 78.691  2.875   25.808 1.00 17.08 ? 334 GLU A CB  1 
ATOM   1124 C  CG  . GLU A  1 144 ? 78.378  2.683   24.329 1.00 17.62 ? 334 GLU A CG  1 
ATOM   1125 C  CD  . GLU A  1 144 ? 77.623  3.856   23.735 1.00 19.21 ? 334 GLU A CD  1 
ATOM   1126 O  OE1 . GLU A  1 144 ? 76.768  4.427   24.440 1.00 24.52 ? 334 GLU A OE1 1 
ATOM   1127 O  OE2 . GLU A  1 144 ? 77.877  4.204   22.563 1.00 22.82 ? 334 GLU A OE2 1 
ATOM   1128 N  N   . MET A  1 145 ? 80.288  4.093   28.335 1.00 22.37 ? 335 MET A N   1 
ATOM   1129 C  CA  . MET A  1 145 ? 80.377  4.291   29.777 1.00 23.63 ? 335 MET A CA  1 
ATOM   1130 C  C   . MET A  1 145 ? 80.495  5.789   30.028 1.00 22.89 ? 335 MET A C   1 
ATOM   1131 O  O   . MET A  1 145 ? 80.049  6.296   31.057 1.00 21.56 ? 335 MET A O   1 
ATOM   1132 C  CB  . MET A  1 145 ? 81.595  3.568   30.357 1.00 22.17 ? 335 MET A CB  1 
ATOM   1133 C  CG  . MET A  1 145 ? 81.350  2.103   30.671 1.00 30.74 ? 335 MET A CG  1 
ATOM   1134 S  SD  . MET A  1 145 ? 82.750  1.324   31.498 1.00 39.65 ? 335 MET A SD  1 
ATOM   1135 C  CE  . MET A  1 145 ? 82.948  2.418   32.917 1.00 29.46 ? 335 MET A CE  1 
ATOM   1136 N  N   . GLY A  1 146 ? 81.096  6.489   29.069 1.00 22.06 ? 336 GLY A N   1 
ATOM   1137 C  CA  . GLY A  1 146 ? 81.255  7.926   29.180 1.00 18.41 ? 336 GLY A CA  1 
ATOM   1138 C  C   . GLY A  1 146 ? 79.900  8.587   29.319 1.00 21.70 ? 336 GLY A C   1 
ATOM   1139 O  O   . GLY A  1 146 ? 79.681  9.382   30.233 1.00 26.65 ? 336 GLY A O   1 
ATOM   1140 N  N   . HIS A  1 147 ? 78.982  8.267   28.412 1.00 17.84 ? 337 HIS A N   1 
ATOM   1141 C  CA  . HIS A  1 147 ? 77.649  8.840   28.483 1.00 13.80 ? 337 HIS A CA  1 
ATOM   1142 C  C   . HIS A  1 147 ? 77.093  8.571   29.869 1.00 17.16 ? 337 HIS A C   1 
ATOM   1143 O  O   . HIS A  1 147 ? 76.438  9.429   30.454 1.00 23.72 ? 337 HIS A O   1 
ATOM   1144 C  CB  . HIS A  1 147 ? 76.725  8.226   27.427 1.00 11.96 ? 337 HIS A CB  1 
ATOM   1145 C  CG  . HIS A  1 147 ? 77.016  8.678   26.029 1.00 15.89 ? 337 HIS A CG  1 
ATOM   1146 N  ND1 . HIS A  1 147 ? 77.164  10.007  25.691 1.00 17.97 ? 337 HIS A ND1 1 
ATOM   1147 C  CD2 . HIS A  1 147 ? 77.163  7.980   24.878 1.00 12.29 ? 337 HIS A CD2 1 
ATOM   1148 C  CE1 . HIS A  1 147 ? 77.390  10.107  24.393 1.00 12.73 ? 337 HIS A CE1 1 
ATOM   1149 N  NE2 . HIS A  1 147 ? 77.394  8.892   23.876 1.00 8.98  ? 337 HIS A NE2 1 
ATOM   1150 N  N   . ASN A  1 148 ? 77.360  7.378   30.395 1.00 18.65 ? 338 ASN A N   1 
ATOM   1151 C  CA  . ASN A  1 148 ? 76.885  7.010   31.727 1.00 23.23 ? 338 ASN A CA  1 
ATOM   1152 C  C   . ASN A  1 148 ? 77.431  7.982   32.775 1.00 25.98 ? 338 ASN A C   1 
ATOM   1153 O  O   . ASN A  1 148 ? 76.736  8.353   33.726 1.00 26.49 ? 338 ASN A O   1 
ATOM   1154 C  CB  . ASN A  1 148 ? 77.318  5.581   32.074 1.00 22.43 ? 338 ASN A CB  1 
ATOM   1155 C  CG  . ASN A  1 148 ? 76.453  4.523   31.407 1.00 27.55 ? 338 ASN A CG  1 
ATOM   1156 O  OD1 . ASN A  1 148 ? 76.714  3.324   31.533 1.00 22.07 ? 338 ASN A OD1 1 
ATOM   1157 N  ND2 . ASN A  1 148 ? 75.415  4.961   30.701 1.00 25.59 ? 338 ASN A ND2 1 
ATOM   1158 N  N   . LEU A  1 149 ? 78.683  8.389   32.589 1.00 23.69 ? 339 LEU A N   1 
ATOM   1159 C  CA  . LEU A  1 149 ? 79.339  9.317   33.501 1.00 21.40 ? 339 LEU A CA  1 
ATOM   1160 C  C   . LEU A  1 149 ? 79.011  10.764  33.140 1.00 21.17 ? 339 LEU A C   1 
ATOM   1161 O  O   . LEU A  1 149 ? 79.832  11.664  33.326 1.00 22.40 ? 339 LEU A O   1 
ATOM   1162 C  CB  . LEU A  1 149 ? 80.855  9.099   33.466 1.00 18.07 ? 339 LEU A CB  1 
ATOM   1163 C  CG  . LEU A  1 149 ? 81.347  7.785   34.075 1.00 14.91 ? 339 LEU A CG  1 
ATOM   1164 C  CD1 . LEU A  1 149 ? 82.824  7.611   33.810 1.00 13.61 ? 339 LEU A CD1 1 
ATOM   1165 C  CD2 . LEU A  1 149 ? 81.066  7.789   35.570 1.00 18.79 ? 339 LEU A CD2 1 
ATOM   1166 N  N   . GLY A  1 150 ? 77.807  10.974  32.616 1.00 18.89 ? 340 GLY A N   1 
ATOM   1167 C  CA  . GLY A  1 150 ? 77.379  12.308  32.239 1.00 20.88 ? 340 GLY A CA  1 
ATOM   1168 C  C   . GLY A  1 150 ? 78.227  12.999  31.183 1.00 23.94 ? 340 GLY A C   1 
ATOM   1169 O  O   . GLY A  1 150 ? 78.222  14.228  31.094 1.00 21.58 ? 340 GLY A O   1 
ATOM   1170 N  N   . ILE A  1 151 ? 78.955  12.229  30.379 1.00 21.92 ? 341 ILE A N   1 
ATOM   1171 C  CA  . ILE A  1 151 ? 79.789  12.825  29.340 1.00 24.29 ? 341 ILE A CA  1 
ATOM   1172 C  C   . ILE A  1 151 ? 79.056  12.837  27.999 1.00 21.75 ? 341 ILE A C   1 
ATOM   1173 O  O   . ILE A  1 151 ? 78.348  11.889  27.657 1.00 17.25 ? 341 ILE A O   1 
ATOM   1174 C  CB  . ILE A  1 151 ? 81.126  12.061  29.164 1.00 23.09 ? 341 ILE A CB  1 
ATOM   1175 C  CG1 . ILE A  1 151 ? 81.774  11.805  30.525 1.00 24.82 ? 341 ILE A CG1 1 
ATOM   1176 C  CG2 . ILE A  1 151 ? 82.081  12.883  28.317 1.00 20.95 ? 341 ILE A CG2 1 
ATOM   1177 C  CD1 . ILE A  1 151 ? 83.103  11.081  30.437 1.00 19.66 ? 341 ILE A CD1 1 
ATOM   1178 N  N   . ASN A  1 152 ? 79.224  13.921  27.249 1.00 19.49 ? 342 ASN A N   1 
ATOM   1179 C  CA  . ASN A  1 152 ? 78.582  14.049  25.948 1.00 22.69 ? 342 ASN A CA  1 
ATOM   1180 C  C   . ASN A  1 152 ? 79.617  14.109  24.828 1.00 23.51 ? 342 ASN A C   1 
ATOM   1181 O  O   . ASN A  1 152 ? 80.821  14.183  25.079 1.00 25.70 ? 342 ASN A O   1 
ATOM   1182 C  CB  . ASN A  1 152 ? 77.684  15.290  25.912 1.00 24.24 ? 342 ASN A CB  1 
ATOM   1183 C  CG  . ASN A  1 152 ? 76.402  15.109  26.722 1.00 32.29 ? 342 ASN A CG  1 
ATOM   1184 O  OD1 . ASN A  1 152 ? 75.549  14.283  26.385 1.00 31.73 ? 342 ASN A OD1 1 
ATOM   1185 N  ND2 . ASN A  1 152 ? 76.265  15.883  27.795 1.00 28.60 ? 342 ASN A ND2 1 
ATOM   1186 N  N   . HIS A  1 153 ? 79.135  14.070  23.591 1.00 19.79 ? 343 HIS A N   1 
ATOM   1187 C  CA  . HIS A  1 153 ? 80.002  14.089  22.422 1.00 19.21 ? 343 HIS A CA  1 
ATOM   1188 C  C   . HIS A  1 153 ? 80.852  15.339  22.295 1.00 17.12 ? 343 HIS A C   1 
ATOM   1189 O  O   . HIS A  1 153 ? 80.470  16.415  22.752 1.00 17.94 ? 343 HIS A O   1 
ATOM   1190 C  CB  . HIS A  1 153 ? 79.158  13.910  21.159 1.00 20.98 ? 343 HIS A CB  1 
ATOM   1191 C  CG  . HIS A  1 153 ? 78.552  12.549  21.032 1.00 23.52 ? 343 HIS A CG  1 
ATOM   1192 N  ND1 . HIS A  1 153 ? 77.405  12.309  20.309 1.00 21.56 ? 343 HIS A ND1 1 
ATOM   1193 C  CD2 . HIS A  1 153 ? 78.945  11.350  21.523 1.00 25.08 ? 343 HIS A CD2 1 
ATOM   1194 C  CE1 . HIS A  1 153 ? 77.116  11.022  20.361 1.00 26.09 ? 343 HIS A CE1 1 
ATOM   1195 N  NE2 . HIS A  1 153 ? 78.035  10.418  21.092 1.00 24.41 ? 343 HIS A NE2 1 
ATOM   1196 N  N   . ASP A  1 154 ? 82.015  15.187  21.670 1.00 14.03 ? 344 ASP A N   1 
ATOM   1197 C  CA  . ASP A  1 154 ? 82.909  16.311  21.465 1.00 20.76 ? 344 ASP A CA  1 
ATOM   1198 C  C   . ASP A  1 154 ? 82.385  17.200  20.342 1.00 23.76 ? 344 ASP A C   1 
ATOM   1199 O  O   . ASP A  1 154 ? 81.599  16.769  19.498 1.00 23.55 ? 344 ASP A O   1 
ATOM   1200 C  CB  . ASP A  1 154 ? 84.320  15.830  21.115 1.00 20.29 ? 344 ASP A CB  1 
ATOM   1201 C  CG  . ASP A  1 154 ? 84.998  15.117  22.268 1.00 24.74 ? 344 ASP A CG  1 
ATOM   1202 O  OD1 . ASP A  1 154 ? 84.754  15.498  23.433 1.00 27.86 ? 344 ASP A OD1 1 
ATOM   1203 O  OD2 . ASP A  1 154 ? 85.790  14.189  22.008 1.00 20.62 ? 344 ASP A OD2 1 
ATOM   1204 N  N   . SER A  1 155 ? 82.825  18.449  20.343 1.00 26.84 ? 345 SER A N   1 
ATOM   1205 C  CA  . SER A  1 155 ? 82.417  19.398  19.323 1.00 29.33 ? 345 SER A CA  1 
ATOM   1206 C  C   . SER A  1 155 ? 83.370  20.574  19.380 1.00 28.61 ? 345 SER A C   1 
ATOM   1207 O  O   . SER A  1 155 ? 84.199  20.665  20.286 1.00 29.88 ? 345 SER A O   1 
ATOM   1208 C  CB  . SER A  1 155 ? 80.984  19.873  19.573 1.00 27.35 ? 345 SER A CB  1 
ATOM   1209 O  OG  . SER A  1 155 ? 80.876  20.526  20.823 1.00 28.00 ? 345 SER A OG  1 
ATOM   1210 N  N   . GLY A  1 156 ? 83.256  21.470  18.408 1.00 28.83 ? 346 GLY A N   1 
ATOM   1211 C  CA  . GLY A  1 156 ? 84.125  22.628  18.382 1.00 26.92 ? 346 GLY A CA  1 
ATOM   1212 C  C   . GLY A  1 156 ? 85.580  22.286  18.639 1.00 26.62 ? 346 GLY A C   1 
ATOM   1213 O  O   . GLY A  1 156 ? 86.094  21.271  18.169 1.00 28.31 ? 346 GLY A O   1 
ATOM   1214 N  N   . TYR A  1 157 ? 86.241  23.130  19.418 1.00 27.88 ? 347 TYR A N   1 
ATOM   1215 C  CA  . TYR A  1 157 ? 87.650  22.946  19.713 1.00 24.95 ? 347 TYR A CA  1 
ATOM   1216 C  C   . TYR A  1 157 ? 88.005  22.022  20.876 1.00 23.74 ? 347 TYR A C   1 
ATOM   1217 O  O   . TYR A  1 157 ? 88.928  22.310  21.639 1.00 23.48 ? 347 TYR A O   1 
ATOM   1218 C  CB  . TYR A  1 157 ? 88.308  24.317  19.909 1.00 22.43 ? 347 TYR A CB  1 
ATOM   1219 C  CG  . TYR A  1 157 ? 88.359  25.129  18.635 1.00 21.38 ? 347 TYR A CG  1 
ATOM   1220 C  CD1 . TYR A  1 157 ? 87.204  25.696  18.094 1.00 23.44 ? 347 TYR A CD1 1 
ATOM   1221 C  CD2 . TYR A  1 157 ? 89.552  25.272  17.931 1.00 22.94 ? 347 TYR A CD2 1 
ATOM   1222 C  CE1 . TYR A  1 157 ? 87.239  26.377  16.878 1.00 19.93 ? 347 TYR A CE1 1 
ATOM   1223 C  CE2 . TYR A  1 157 ? 89.598  25.950  16.719 1.00 18.90 ? 347 TYR A CE2 1 
ATOM   1224 C  CZ  . TYR A  1 157 ? 88.442  26.496  16.197 1.00 20.25 ? 347 TYR A CZ  1 
ATOM   1225 O  OH  . TYR A  1 157 ? 88.494  27.137  14.981 1.00 22.05 ? 347 TYR A OH  1 
ATOM   1226 N  N   . CYS A  1 158 ? 87.276  20.920  21.023 1.00 23.23 ? 348 CYS A N   1 
ATOM   1227 C  CA  . CYS A  1 158 ? 87.598  19.964  22.079 1.00 24.38 ? 348 CYS A CA  1 
ATOM   1228 C  C   . CYS A  1 158 ? 88.744  19.133  21.514 1.00 23.20 ? 348 CYS A C   1 
ATOM   1229 O  O   . CYS A  1 158 ? 88.659  18.662  20.382 1.00 20.61 ? 348 CYS A O   1 
ATOM   1230 C  CB  . CYS A  1 158 ? 86.411  19.047  22.394 1.00 25.16 ? 348 CYS A CB  1 
ATOM   1231 S  SG  . CYS A  1 158 ? 85.001  19.843  23.233 1.00 33.63 ? 348 CYS A SG  1 
ATOM   1232 N  N   . SER A  1 159 ? 89.820  18.961  22.278 1.00 22.29 ? 349 SER A N   1 
ATOM   1233 C  CA  . SER A  1 159 ? 90.943  18.179  21.774 1.00 22.80 ? 349 SER A CA  1 
ATOM   1234 C  C   . SER A  1 159 ? 91.545  17.208  22.777 1.00 21.65 ? 349 SER A C   1 
ATOM   1235 O  O   . SER A  1 159 ? 91.245  17.241  23.972 1.00 20.30 ? 349 SER A O   1 
ATOM   1236 C  CB  . SER A  1 159 ? 92.052  19.099  21.236 1.00 21.87 ? 349 SER A CB  1 
ATOM   1237 O  OG  . SER A  1 159 ? 92.731  19.775  22.281 1.00 20.11 ? 349 SER A OG  1 
ATOM   1238 N  N   . CYS A  1 160 ? 92.400  16.341  22.251 1.00 21.82 ? 350 CYS A N   1 
ATOM   1239 C  CA  . CYS A  1 160 ? 93.104  15.325  23.019 1.00 27.05 ? 350 CYS A CA  1 
ATOM   1240 C  C   . CYS A  1 160 ? 94.392  15.098  22.232 1.00 30.23 ? 350 CYS A C   1 
ATOM   1241 O  O   . CYS A  1 160 ? 94.940  13.996  22.207 1.00 30.83 ? 350 CYS A O   1 
ATOM   1242 C  CB  . CYS A  1 160 ? 92.274  14.031  23.074 1.00 27.62 ? 350 CYS A CB  1 
ATOM   1243 S  SG  . CYS A  1 160 ? 91.863  13.321  21.440 1.00 28.96 ? 350 CYS A SG  1 
ATOM   1244 N  N   . GLY A  1 161 ? 94.864  16.166  21.593 1.00 32.07 ? 351 GLY A N   1 
ATOM   1245 C  CA  . GLY A  1 161 ? 96.057  16.086  20.771 1.00 34.83 ? 351 GLY A CA  1 
ATOM   1246 C  C   . GLY A  1 161 ? 95.575  15.850  19.353 1.00 39.44 ? 351 GLY A C   1 
ATOM   1247 O  O   . GLY A  1 161 ? 94.372  15.937  19.099 1.00 40.35 ? 351 GLY A O   1 
ATOM   1248 N  N   . ASP A  1 162 ? 96.479  15.560  18.424 1.00 43.52 ? 352 ASP A N   1 
ATOM   1249 C  CA  . ASP A  1 162 ? 96.055  15.308  17.049 1.00 50.45 ? 352 ASP A CA  1 
ATOM   1250 C  C   . ASP A  1 162 ? 95.552  13.868  16.928 1.00 50.01 ? 352 ASP A C   1 
ATOM   1251 O  O   . ASP A  1 162 ? 95.949  13.127  16.025 1.00 49.33 ? 352 ASP A O   1 
ATOM   1252 C  CB  . ASP A  1 162 ? 97.209  15.550  16.063 1.00 55.48 ? 352 ASP A CB  1 
ATOM   1253 C  CG  . ASP A  1 162 ? 98.373  14.596  16.269 1.00 59.43 ? 352 ASP A CG  1 
ATOM   1254 O  OD1 . ASP A  1 162 ? 99.295  14.597  15.424 1.00 55.67 ? 352 ASP A OD1 1 
ATOM   1255 O  OD2 . ASP A  1 162 ? 98.369  13.850  17.272 1.00 63.28 ? 352 ASP A OD2 1 
ATOM   1256 N  N   . TYR A  1 163 ? 94.672  13.486  17.851 1.00 46.31 ? 353 TYR A N   1 
ATOM   1257 C  CA  . TYR A  1 163 ? 94.110  12.139  17.880 1.00 41.70 ? 353 TYR A CA  1 
ATOM   1258 C  C   . TYR A  1 163 ? 92.590  12.163  17.969 1.00 37.64 ? 353 TYR A C   1 
ATOM   1259 O  O   . TYR A  1 163 ? 92.003  13.090  18.528 1.00 38.63 ? 353 TYR A O   1 
ATOM   1260 C  CB  . TYR A  1 163 ? 94.658  11.367  19.082 1.00 42.55 ? 353 TYR A CB  1 
ATOM   1261 C  CG  . TYR A  1 163 ? 96.163  11.276  19.133 1.00 44.34 ? 353 TYR A CG  1 
ATOM   1262 C  CD1 . TYR A  1 163 ? 96.867  10.523  18.199 1.00 45.63 ? 353 TYR A CD1 1 
ATOM   1263 C  CD2 . TYR A  1 163 ? 96.887  11.951  20.118 1.00 45.56 ? 353 TYR A CD2 1 
ATOM   1264 C  CE1 . TYR A  1 163 ? 98.259  10.442  18.241 1.00 48.80 ? 353 TYR A CE1 1 
ATOM   1265 C  CE2 . TYR A  1 163 ? 98.279  11.877  20.169 1.00 44.52 ? 353 TYR A CE2 1 
ATOM   1266 C  CZ  . TYR A  1 163 ? 98.957  11.122  19.227 1.00 44.71 ? 353 TYR A CZ  1 
ATOM   1267 O  OH  . TYR A  1 163 ? 100.330 11.054  19.260 1.00 43.98 ? 353 TYR A OH  1 
ATOM   1268 N  N   . ALA A  1 164 ? 91.962  11.132  17.413 1.00 33.09 ? 354 ALA A N   1 
ATOM   1269 C  CA  . ALA A  1 164 ? 90.514  11.001  17.443 1.00 26.21 ? 354 ALA A CA  1 
ATOM   1270 C  C   . ALA A  1 164 ? 90.151  10.626  18.875 1.00 25.53 ? 354 ALA A C   1 
ATOM   1271 O  O   . ALA A  1 164 ? 90.468  9.529   19.330 1.00 26.88 ? 354 ALA A O   1 
ATOM   1272 C  CB  . ALA A  1 164 ? 90.079  9.912   16.485 1.00 27.23 ? 354 ALA A CB  1 
ATOM   1273 N  N   . CYS A  1 165 ? 89.488  11.534  19.583 1.00 22.36 ? 355 CYS A N   1 
ATOM   1274 C  CA  . CYS A  1 165 ? 89.130  11.294  20.977 1.00 21.66 ? 355 CYS A CA  1 
ATOM   1275 C  C   . CYS A  1 165 ? 87.937  10.362  21.167 1.00 20.67 ? 355 CYS A C   1 
ATOM   1276 O  O   . CYS A  1 165 ? 87.078  10.242  20.296 1.00 20.59 ? 355 CYS A O   1 
ATOM   1277 C  CB  . CYS A  1 165 ? 88.882  12.631  21.675 1.00 23.78 ? 355 CYS A CB  1 
ATOM   1278 S  SG  . CYS A  1 165 ? 89.969  13.958  21.056 1.00 31.94 ? 355 CYS A SG  1 
ATOM   1279 N  N   . ILE A  1 166 ? 87.898  9.708   22.325 1.00 22.98 ? 356 ILE A N   1 
ATOM   1280 C  CA  . ILE A  1 166 ? 86.845  8.754   22.668 1.00 21.68 ? 356 ILE A CA  1 
ATOM   1281 C  C   . ILE A  1 166 ? 85.403  9.246   22.534 1.00 20.46 ? 356 ILE A C   1 
ATOM   1282 O  O   . ILE A  1 166 ? 84.529  8.486   22.120 1.00 16.53 ? 356 ILE A O   1 
ATOM   1283 C  CB  . ILE A  1 166 ? 87.039  8.207   24.115 1.00 19.84 ? 356 ILE A CB  1 
ATOM   1284 C  CG1 . ILE A  1 166 ? 88.174  7.181   24.150 1.00 23.42 ? 356 ILE A CG1 1 
ATOM   1285 C  CG2 . ILE A  1 166 ? 85.771  7.514   24.594 1.00 21.36 ? 356 ILE A CG2 1 
ATOM   1286 C  CD1 . ILE A  1 166 ? 89.514  7.712   23.761 1.00 25.66 ? 356 ILE A CD1 1 
ATOM   1287 N  N   . MET A  1 167 ? 85.140  10.503  22.874 1.00 18.91 ? 357 MET A N   1 
ATOM   1288 C  CA  . MET A  1 167 ? 83.771  10.997  22.794 1.00 19.35 ? 357 MET A CA  1 
ATOM   1289 C  C   . MET A  1 167 ? 83.355  11.724  21.517 1.00 21.65 ? 357 MET A C   1 
ATOM   1290 O  O   . MET A  1 167 ? 82.614  12.702  21.566 1.00 24.83 ? 357 MET A O   1 
ATOM   1291 C  CB  . MET A  1 167 ? 83.450  11.866  24.015 1.00 11.47 ? 357 MET A CB  1 
ATOM   1292 C  CG  . MET A  1 167 ? 83.461  11.095  25.323 1.00 11.81 ? 357 MET A CG  1 
ATOM   1293 S  SD  . MET A  1 167 ? 82.661  9.466   25.189 1.00 18.81 ? 357 MET A SD  1 
ATOM   1294 C  CE  . MET A  1 167 ? 80.910  9.943   25.116 1.00 23.92 ? 357 MET A CE  1 
ATOM   1295 N  N   . ARG A  1 168 ? 83.827  11.242  20.372 1.00 24.89 ? 358 ARG A N   1 
ATOM   1296 C  CA  . ARG A  1 168 ? 83.448  11.828  19.090 1.00 27.17 ? 358 ARG A CA  1 
ATOM   1297 C  C   . ARG A  1 168 ? 82.094  11.234  18.695 1.00 26.53 ? 358 ARG A C   1 
ATOM   1298 O  O   . ARG A  1 168 ? 81.768  10.114  19.085 1.00 29.85 ? 358 ARG A O   1 
ATOM   1299 C  CB  . ARG A  1 168 ? 84.483  11.484  18.016 1.00 27.22 ? 358 ARG A CB  1 
ATOM   1300 C  CG  . ARG A  1 168 ? 85.557  12.535  17.793 1.00 32.80 ? 358 ARG A CG  1 
ATOM   1301 C  CD  . ARG A  1 168 ? 86.547  12.053  16.738 1.00 42.30 ? 358 ARG A CD  1 
ATOM   1302 N  NE  . ARG A  1 168 ? 87.400  13.120  16.219 1.00 46.96 ? 358 ARG A NE  1 
ATOM   1303 C  CZ  . ARG A  1 168 ? 88.197  13.878  16.967 1.00 50.89 ? 358 ARG A CZ  1 
ATOM   1304 N  NH1 . ARG A  1 168 ? 88.255  13.694  18.278 1.00 55.11 ? 358 ARG A NH1 1 
ATOM   1305 N  NH2 . ARG A  1 168 ? 88.941  14.818  16.400 1.00 51.35 ? 358 ARG A NH2 1 
ATOM   1306 N  N   . PRO A  1 169 ? 81.286  11.974  17.922 1.00 26.35 ? 359 PRO A N   1 
ATOM   1307 C  CA  . PRO A  1 169 ? 79.978  11.447  17.514 1.00 24.89 ? 359 PRO A CA  1 
ATOM   1308 C  C   . PRO A  1 169 ? 80.047  10.037  16.910 1.00 25.40 ? 359 PRO A C   1 
ATOM   1309 O  O   . PRO A  1 169 ? 79.205  9.191   17.207 1.00 29.51 ? 359 PRO A O   1 
ATOM   1310 C  CB  . PRO A  1 169 ? 79.464  12.506  16.533 1.00 20.59 ? 359 PRO A CB  1 
ATOM   1311 C  CG  . PRO A  1 169 ? 80.714  13.220  16.077 1.00 25.06 ? 359 PRO A CG  1 
ATOM   1312 C  CD  . PRO A  1 169 ? 81.522  13.302  17.334 1.00 24.38 ? 359 PRO A CD  1 
ATOM   1313 N  N   . GLU A  1 170 ? 81.036  9.780   16.061 1.00 23.62 ? 360 GLU A N   1 
ATOM   1314 C  CA  . GLU A  1 170 ? 81.184  8.444   15.487 1.00 28.43 ? 360 GLU A CA  1 
ATOM   1315 C  C   . GLU A  1 170 ? 82.618  7.922   15.591 1.00 26.15 ? 360 GLU A C   1 
ATOM   1316 O  O   . GLU A  1 170 ? 83.582  8.661   15.400 1.00 28.89 ? 360 GLU A O   1 
ATOM   1317 C  CB  . GLU A  1 170 ? 80.702  8.393   14.026 1.00 29.65 ? 360 GLU A CB  1 
ATOM   1318 C  CG  . GLU A  1 170 ? 80.996  9.607   13.172 1.00 34.93 ? 360 GLU A CG  1 
ATOM   1319 C  CD  . GLU A  1 170 ? 79.923  10.673  13.289 1.00 39.97 ? 360 GLU A CD  1 
ATOM   1320 O  OE1 . GLU A  1 170 ? 78.726  10.325  13.196 1.00 33.33 ? 360 GLU A OE1 1 
ATOM   1321 O  OE2 . GLU A  1 170 ? 80.274  11.858  13.462 1.00 43.34 ? 360 GLU A OE2 1 
ATOM   1322 N  N   . ILE A  1 171 ? 82.745  6.637   15.901 1.00 24.18 ? 361 ILE A N   1 
ATOM   1323 C  CA  . ILE A  1 171 ? 84.048  6.004   16.058 1.00 24.14 ? 361 ILE A CA  1 
ATOM   1324 C  C   . ILE A  1 171 ? 84.969  6.180   14.855 1.00 21.52 ? 361 ILE A C   1 
ATOM   1325 O  O   . ILE A  1 171 ? 84.544  6.061   13.707 1.00 24.49 ? 361 ILE A O   1 
ATOM   1326 C  CB  . ILE A  1 171 ? 83.892  4.497   16.358 1.00 24.68 ? 361 ILE A CB  1 
ATOM   1327 C  CG1 . ILE A  1 171 ? 85.262  3.887   16.646 1.00 28.36 ? 361 ILE A CG1 1 
ATOM   1328 C  CG2 . ILE A  1 171 ? 83.241  3.791   15.181 1.00 24.69 ? 361 ILE A CG2 1 
ATOM   1329 C  CD1 . ILE A  1 171 ? 85.191  2.503   17.221 1.00 37.54 ? 361 ILE A CD1 1 
ATOM   1330 N  N   . SER A  1 172 ? 86.238  6.459   15.133 1.00 21.60 ? 362 SER A N   1 
ATOM   1331 C  CA  . SER A  1 172 ? 87.235  6.660   14.087 1.00 27.44 ? 362 SER A CA  1 
ATOM   1332 C  C   . SER A  1 172 ? 87.863  5.357   13.601 1.00 33.17 ? 362 SER A C   1 
ATOM   1333 O  O   . SER A  1 172 ? 87.961  4.384   14.348 1.00 37.55 ? 362 SER A O   1 
ATOM   1334 C  CB  . SER A  1 172 ? 88.341  7.588   14.593 1.00 27.06 ? 362 SER A CB  1 
ATOM   1335 O  OG  . SER A  1 172 ? 89.432  7.621   13.689 1.00 25.85 ? 362 SER A OG  1 
ATOM   1336 N  N   . PRO A  1 173 ? 88.295  5.325   12.330 1.00 36.55 ? 363 PRO A N   1 
ATOM   1337 C  CA  . PRO A  1 173 ? 88.922  4.138   11.739 1.00 36.34 ? 363 PRO A CA  1 
ATOM   1338 C  C   . PRO A  1 173 ? 90.340  3.959   12.275 1.00 34.92 ? 363 PRO A C   1 
ATOM   1339 O  O   . PRO A  1 173 ? 90.955  2.906   12.111 1.00 34.27 ? 363 PRO A O   1 
ATOM   1340 C  CB  . PRO A  1 173 ? 88.903  4.451   10.248 1.00 38.96 ? 363 PRO A CB  1 
ATOM   1341 C  CG  . PRO A  1 173 ? 89.100  5.939   10.232 1.00 41.73 ? 363 PRO A CG  1 
ATOM   1342 C  CD  . PRO A  1 173 ? 88.160  6.399   11.328 1.00 37.39 ? 363 PRO A CD  1 
ATOM   1343 N  N   . GLU A  1 174 ? 90.848  5.009   12.912 1.00 33.01 ? 364 GLU A N   1 
ATOM   1344 C  CA  . GLU A  1 174 ? 92.181  5.003   13.498 1.00 32.29 ? 364 GLU A CA  1 
ATOM   1345 C  C   . GLU A  1 174 ? 92.026  5.603   14.895 1.00 27.03 ? 364 GLU A C   1 
ATOM   1346 O  O   . GLU A  1 174 ? 92.631  6.628   15.219 1.00 22.43 ? 364 GLU A O   1 
ATOM   1347 C  CB  . GLU A  1 174 ? 93.130  5.852   12.647 1.00 38.22 ? 364 GLU A CB  1 
ATOM   1348 C  CG  . GLU A  1 174 ? 94.602  5.702   13.006 1.00 51.79 ? 364 GLU A CG  1 
ATOM   1349 C  CD  . GLU A  1 174 ? 95.515  6.532   12.113 1.00 58.53 ? 364 GLU A CD  1 
ATOM   1350 O  OE1 . GLU A  1 174 ? 95.478  6.345   10.876 1.00 57.65 ? 364 GLU A OE1 1 
ATOM   1351 O  OE2 . GLU A  1 174 ? 96.273  7.370   12.652 1.00 60.25 ? 364 GLU A OE2 1 
ATOM   1352 N  N   . PRO A  1 175 ? 91.211  4.953   15.744 1.00 24.00 ? 365 PRO A N   1 
ATOM   1353 C  CA  . PRO A  1 175 ? 90.910  5.357   17.124 1.00 20.27 ? 365 PRO A CA  1 
ATOM   1354 C  C   . PRO A  1 175 ? 92.097  5.472   18.072 1.00 17.91 ? 365 PRO A C   1 
ATOM   1355 O  O   . PRO A  1 175 ? 93.111  4.794   17.914 1.00 12.90 ? 365 PRO A O   1 
ATOM   1356 C  CB  . PRO A  1 175 ? 89.925  4.286   17.582 1.00 17.59 ? 365 PRO A CB  1 
ATOM   1357 C  CG  . PRO A  1 175 ? 90.430  3.069   16.873 1.00 16.97 ? 365 PRO A CG  1 
ATOM   1358 C  CD  . PRO A  1 175 ? 90.673  3.605   15.477 1.00 19.63 ? 365 PRO A CD  1 
ATOM   1359 N  N   . SER A  1 176 ? 91.950  6.338   19.067 1.00 18.61 ? 366 SER A N   1 
ATOM   1360 C  CA  . SER A  1 176 ? 92.988  6.538   20.062 1.00 20.94 ? 366 SER A CA  1 
ATOM   1361 C  C   . SER A  1 176 ? 92.416  6.135   21.418 1.00 24.25 ? 366 SER A C   1 
ATOM   1362 O  O   . SER A  1 176 ? 91.255  5.742   21.521 1.00 24.52 ? 366 SER A O   1 
ATOM   1363 C  CB  . SER A  1 176 ? 93.425  8.004   20.103 1.00 19.79 ? 366 SER A CB  1 
ATOM   1364 O  OG  . SER A  1 176 ? 92.501  8.794   20.831 1.00 23.25 ? 366 SER A OG  1 
ATOM   1365 N  N   . THR A  1 177 ? 93.238  6.243   22.453 1.00 24.39 ? 367 THR A N   1 
ATOM   1366 C  CA  . THR A  1 177 ? 92.842  5.887   23.809 1.00 19.86 ? 367 THR A CA  1 
ATOM   1367 C  C   . THR A  1 177 ? 92.647  7.143   24.657 1.00 19.91 ? 367 THR A C   1 
ATOM   1368 O  O   . THR A  1 177 ? 92.419  7.053   25.866 1.00 12.70 ? 367 THR A O   1 
ATOM   1369 C  CB  . THR A  1 177 ? 93.934  5.019   24.472 1.00 22.49 ? 367 THR A CB  1 
ATOM   1370 O  OG1 . THR A  1 177 ? 95.204  5.676   24.338 1.00 20.14 ? 367 THR A OG1 1 
ATOM   1371 C  CG2 . THR A  1 177 ? 94.013  3.644   23.816 1.00 13.40 ? 367 THR A CG2 1 
ATOM   1372 N  N   . PHE A  1 178 ? 92.721  8.309   24.013 1.00 18.09 ? 368 PHE A N   1 
ATOM   1373 C  CA  . PHE A  1 178 ? 92.600  9.591   24.711 1.00 17.77 ? 368 PHE A CA  1 
ATOM   1374 C  C   . PHE A  1 178 ? 91.232  10.265  24.700 1.00 14.10 ? 368 PHE A C   1 
ATOM   1375 O  O   . PHE A  1 178 ? 90.571  10.330  23.669 1.00 9.51  ? 368 PHE A O   1 
ATOM   1376 C  CB  . PHE A  1 178 ? 93.610  10.588  24.139 1.00 20.28 ? 368 PHE A CB  1 
ATOM   1377 C  CG  . PHE A  1 178 ? 95.013  10.065  24.074 1.00 22.64 ? 368 PHE A CG  1 
ATOM   1378 C  CD1 . PHE A  1 178 ? 95.718  10.090  22.874 1.00 19.68 ? 368 PHE A CD1 1 
ATOM   1379 C  CD2 . PHE A  1 178 ? 95.636  9.551   25.211 1.00 21.52 ? 368 PHE A CD2 1 
ATOM   1380 C  CE1 . PHE A  1 178 ? 97.028  9.609   22.803 1.00 25.41 ? 368 PHE A CE1 1 
ATOM   1381 C  CE2 . PHE A  1 178 ? 96.943  9.069   25.155 1.00 22.56 ? 368 PHE A CE2 1 
ATOM   1382 C  CZ  . PHE A  1 178 ? 97.642  9.097   23.948 1.00 22.11 ? 368 PHE A CZ  1 
ATOM   1383 N  N   . PHE A  1 179 ? 90.836  10.776  25.864 1.00 17.80 ? 369 PHE A N   1 
ATOM   1384 C  CA  . PHE A  1 179 ? 89.583  11.512  26.045 1.00 16.42 ? 369 PHE A CA  1 
ATOM   1385 C  C   . PHE A  1 179 ? 89.895  12.978  25.717 1.00 18.48 ? 369 PHE A C   1 
ATOM   1386 O  O   . PHE A  1 179 ? 91.057  13.382  25.701 1.00 17.83 ? 369 PHE A O   1 
ATOM   1387 C  CB  . PHE A  1 179 ? 89.126  11.436  27.509 1.00 14.95 ? 369 PHE A CB  1 
ATOM   1388 C  CG  . PHE A  1 179 ? 88.111  10.365  27.787 1.00 12.02 ? 369 PHE A CG  1 
ATOM   1389 C  CD1 . PHE A  1 179 ? 86.808  10.480  27.311 1.00 12.10 ? 369 PHE A CD1 1 
ATOM   1390 C  CD2 . PHE A  1 179 ? 88.447  9.257   28.554 1.00 11.25 ? 369 PHE A CD2 1 
ATOM   1391 C  CE1 . PHE A  1 179 ? 85.852  9.507   27.599 1.00 17.91 ? 369 PHE A CE1 1 
ATOM   1392 C  CE2 . PHE A  1 179 ? 87.501  8.277   28.849 1.00 14.80 ? 369 PHE A CE2 1 
ATOM   1393 C  CZ  . PHE A  1 179 ? 86.199  8.401   28.372 1.00 17.66 ? 369 PHE A CZ  1 
ATOM   1394 N  N   . SER A  1 180 ? 88.869  13.777  25.459 1.00 24.54 ? 370 SER A N   1 
ATOM   1395 C  CA  . SER A  1 180 ? 89.097  15.191  25.171 1.00 24.75 ? 370 SER A CA  1 
ATOM   1396 C  C   . SER A  1 180 ? 89.057  15.946  26.499 1.00 27.07 ? 370 SER A C   1 
ATOM   1397 O  O   . SER A  1 180 ? 88.449  15.481  27.468 1.00 27.16 ? 370 SER A O   1 
ATOM   1398 C  CB  . SER A  1 180 ? 88.011  15.742  24.241 1.00 21.08 ? 370 SER A CB  1 
ATOM   1399 O  OG  . SER A  1 180 ? 86.814  16.013  24.952 1.00 13.14 ? 370 SER A OG  1 
ATOM   1400 N  N   . ASN A  1 181 ? 89.709  17.102  26.552 1.00 26.26 ? 371 ASN A N   1 
ATOM   1401 C  CA  . ASN A  1 181 ? 89.705  17.890  27.774 1.00 23.04 ? 371 ASN A CA  1 
ATOM   1402 C  C   . ASN A  1 181 ? 88.255  18.183  28.164 1.00 23.70 ? 371 ASN A C   1 
ATOM   1403 O  O   . ASN A  1 181 ? 87.934  18.313  29.347 1.00 24.97 ? 371 ASN A O   1 
ATOM   1404 C  CB  . ASN A  1 181 ? 90.505  19.183  27.575 1.00 26.09 ? 371 ASN A CB  1 
ATOM   1405 C  CG  . ASN A  1 181 ? 90.022  20.002  26.395 1.00 30.13 ? 371 ASN A CG  1 
ATOM   1406 O  OD1 . ASN A  1 181 ? 89.667  19.458  25.341 1.00 29.89 ? 371 ASN A OD1 1 
ATOM   1407 N  ND2 . ASN A  1 181 ? 90.035  21.321  26.561 1.00 31.32 ? 371 ASN A ND2 1 
ATOM   1408 N  N   . CYS A  1 182 ? 87.379  18.262  27.165 1.00 23.62 ? 372 CYS A N   1 
ATOM   1409 C  CA  . CYS A  1 182 ? 85.959  18.508  27.403 1.00 25.76 ? 372 CYS A CA  1 
ATOM   1410 C  C   . CYS A  1 182 ? 85.360  17.328  28.171 1.00 26.86 ? 372 CYS A C   1 
ATOM   1411 O  O   . CYS A  1 182 ? 84.621  17.514  29.138 1.00 27.41 ? 372 CYS A O   1 
ATOM   1412 C  CB  . CYS A  1 182 ? 85.208  18.692  26.074 1.00 26.30 ? 372 CYS A CB  1 
ATOM   1413 S  SG  . CYS A  1 182 ? 85.659  20.189  25.132 1.00 30.79 ? 372 CYS A SG  1 
ATOM   1414 N  N   . SER A  1 183 ? 85.684  16.113  27.738 1.00 23.49 ? 373 SER A N   1 
ATOM   1415 C  CA  . SER A  1 183 ? 85.176  14.912  28.394 1.00 20.68 ? 373 SER A CA  1 
ATOM   1416 C  C   . SER A  1 183 ? 85.611  14.866  29.853 1.00 19.13 ? 373 SER A C   1 
ATOM   1417 O  O   . SER A  1 183 ? 84.883  14.379  30.711 1.00 18.59 ? 373 SER A O   1 
ATOM   1418 C  CB  . SER A  1 183 ? 85.677  13.657  27.673 1.00 21.36 ? 373 SER A CB  1 
ATOM   1419 O  OG  . SER A  1 183 ? 85.149  13.562  26.362 1.00 23.16 ? 373 SER A OG  1 
ATOM   1420 N  N   . TYR A  1 184 ? 86.805  15.376  30.129 1.00 21.06 ? 374 TYR A N   1 
ATOM   1421 C  CA  . TYR A  1 184 ? 87.331  15.389  31.486 1.00 23.26 ? 374 TYR A CA  1 
ATOM   1422 C  C   . TYR A  1 184 ? 86.482  16.281  32.384 1.00 23.90 ? 374 TYR A C   1 
ATOM   1423 O  O   . TYR A  1 184 ? 85.830  15.799  33.310 1.00 24.26 ? 374 TYR A O   1 
ATOM   1424 C  CB  . TYR A  1 184 ? 88.776  15.890  31.485 1.00 26.31 ? 374 TYR A CB  1 
ATOM   1425 C  CG  . TYR A  1 184 ? 89.421  15.926  32.852 1.00 30.18 ? 374 TYR A CG  1 
ATOM   1426 C  CD1 . TYR A  1 184 ? 90.055  14.801  33.378 1.00 34.50 ? 374 TYR A CD1 1 
ATOM   1427 C  CD2 . TYR A  1 184 ? 89.391  17.087  33.626 1.00 28.85 ? 374 TYR A CD2 1 
ATOM   1428 C  CE1 . TYR A  1 184 ? 90.645  14.832  34.643 1.00 30.50 ? 374 TYR A CE1 1 
ATOM   1429 C  CE2 . TYR A  1 184 ? 89.974  17.127  34.888 1.00 27.12 ? 374 TYR A CE2 1 
ATOM   1430 C  CZ  . TYR A  1 184 ? 90.599  15.998  35.390 1.00 27.27 ? 374 TYR A CZ  1 
ATOM   1431 O  OH  . TYR A  1 184 ? 91.173  16.038  36.638 1.00 27.54 ? 374 TYR A OH  1 
ATOM   1432 N  N   . PHE A  1 185 ? 86.491  17.582  32.103 1.00 26.02 ? 375 PHE A N   1 
ATOM   1433 C  CA  . PHE A  1 185 ? 85.730  18.550  32.892 1.00 27.53 ? 375 PHE A CA  1 
ATOM   1434 C  C   . PHE A  1 185 ? 84.262  18.157  32.999 1.00 26.74 ? 375 PHE A C   1 
ATOM   1435 O  O   . PHE A  1 185 ? 83.660  18.239  34.070 1.00 27.83 ? 375 PHE A O   1 
ATOM   1436 C  CB  . PHE A  1 185 ? 85.844  19.945  32.268 1.00 25.60 ? 375 PHE A CB  1 
ATOM   1437 C  CG  . PHE A  1 185 ? 87.253  20.463  32.195 1.00 26.39 ? 375 PHE A CG  1 
ATOM   1438 C  CD1 . PHE A  1 185 ? 87.784  20.904  30.985 1.00 27.65 ? 375 PHE A CD1 1 
ATOM   1439 C  CD2 . PHE A  1 185 ? 88.056  20.498  33.332 1.00 31.42 ? 375 PHE A CD2 1 
ATOM   1440 C  CE1 . PHE A  1 185 ? 89.093  21.371  30.906 1.00 27.13 ? 375 PHE A CE1 1 
ATOM   1441 C  CE2 . PHE A  1 185 ? 89.370  20.963  33.268 1.00 29.85 ? 375 PHE A CE2 1 
ATOM   1442 C  CZ  . PHE A  1 185 ? 89.889  21.400  32.052 1.00 34.05 ? 375 PHE A CZ  1 
ATOM   1443 N  N   . GLU A  1 186 ? 83.699  17.730  31.876 1.00 26.59 ? 376 GLU A N   1 
ATOM   1444 C  CA  . GLU A  1 186 ? 82.304  17.319  31.811 1.00 26.66 ? 376 GLU A CA  1 
ATOM   1445 C  C   . GLU A  1 186 ? 82.076  16.127  32.732 1.00 24.48 ? 376 GLU A C   1 
ATOM   1446 O  O   . GLU A  1 186 ? 81.109  16.089  33.493 1.00 23.70 ? 376 GLU A O   1 
ATOM   1447 C  CB  . GLU A  1 186 ? 81.954  16.958  30.366 1.00 29.33 ? 376 GLU A CB  1 
ATOM   1448 C  CG  . GLU A  1 186 ? 80.499  16.641  30.116 1.00 35.33 ? 376 GLU A CG  1 
ATOM   1449 C  CD  . GLU A  1 186 ? 80.162  16.643  28.636 1.00 42.86 ? 376 GLU A CD  1 
ATOM   1450 O  OE1 . GLU A  1 186 ? 79.008  16.321  28.289 1.00 50.78 ? 376 GLU A OE1 1 
ATOM   1451 O  OE2 . GLU A  1 186 ? 81.049  16.974  27.818 1.00 42.31 ? 376 GLU A OE2 1 
ATOM   1452 N  N   . CYS A  1 187 ? 82.985  15.160  32.658 1.00 21.53 ? 377 CYS A N   1 
ATOM   1453 C  CA  . CYS A  1 187 ? 82.919  13.962  33.483 1.00 20.79 ? 377 CYS A CA  1 
ATOM   1454 C  C   . CYS A  1 187 ? 82.926  14.307  34.969 1.00 23.14 ? 377 CYS A C   1 
ATOM   1455 O  O   . CYS A  1 187 ? 82.084  13.826  35.736 1.00 21.30 ? 377 CYS A O   1 
ATOM   1456 C  CB  . CYS A  1 187 ? 84.106  13.053  33.175 1.00 24.57 ? 377 CYS A CB  1 
ATOM   1457 S  SG  . CYS A  1 187 ? 84.258  11.637  34.272 1.00 20.19 ? 377 CYS A SG  1 
ATOM   1458 N  N   . TRP A  1 188 ? 83.880  15.139  35.380 1.00 19.40 ? 378 TRP A N   1 
ATOM   1459 C  CA  . TRP A  1 188 ? 83.964  15.521  36.779 1.00 22.88 ? 378 TRP A CA  1 
ATOM   1460 C  C   . TRP A  1 188 ? 82.874  16.489  37.206 1.00 25.11 ? 378 TRP A C   1 
ATOM   1461 O  O   . TRP A  1 188 ? 82.517  16.545  38.381 1.00 23.70 ? 378 TRP A O   1 
ATOM   1462 C  CB  . TRP A  1 188 ? 85.349  16.080  37.098 1.00 22.77 ? 378 TRP A CB  1 
ATOM   1463 C  CG  . TRP A  1 188 ? 86.342  14.978  37.219 1.00 24.52 ? 378 TRP A CG  1 
ATOM   1464 C  CD1 . TRP A  1 188 ? 87.275  14.602  36.293 1.00 27.62 ? 378 TRP A CD1 1 
ATOM   1465 C  CD2 . TRP A  1 188 ? 86.422  14.022  38.281 1.00 25.90 ? 378 TRP A CD2 1 
ATOM   1466 N  NE1 . TRP A  1 188 ? 87.926  13.467  36.712 1.00 25.79 ? 378 TRP A NE1 1 
ATOM   1467 C  CE2 . TRP A  1 188 ? 87.424  13.090  37.929 1.00 27.16 ? 378 TRP A CE2 1 
ATOM   1468 C  CE3 . TRP A  1 188 ? 85.743  13.862  39.497 1.00 24.58 ? 378 TRP A CE3 1 
ATOM   1469 C  CZ2 . TRP A  1 188 ? 87.762  12.006  38.750 1.00 26.36 ? 378 TRP A CZ2 1 
ATOM   1470 C  CZ3 . TRP A  1 188 ? 86.079  12.785  40.312 1.00 25.89 ? 378 TRP A CZ3 1 
ATOM   1471 C  CH2 . TRP A  1 188 ? 87.082  11.871  39.933 1.00 22.08 ? 378 TRP A CH2 1 
ATOM   1472 N  N   . ASP A  1 189 ? 82.333  17.244  36.259 1.00 28.34 ? 379 ASP A N   1 
ATOM   1473 C  CA  . ASP A  1 189 ? 81.259  18.160  36.598 1.00 32.50 ? 379 ASP A CA  1 
ATOM   1474 C  C   . ASP A  1 189 ? 80.104  17.286  37.080 1.00 30.00 ? 379 ASP A C   1 
ATOM   1475 O  O   . ASP A  1 189 ? 79.361  17.649  37.993 1.00 29.27 ? 379 ASP A O   1 
ATOM   1476 C  CB  . ASP A  1 189 ? 80.819  18.963  35.375 1.00 37.94 ? 379 ASP A CB  1 
ATOM   1477 C  CG  . ASP A  1 189 ? 79.831  20.060  35.728 1.00 44.27 ? 379 ASP A CG  1 
ATOM   1478 O  OD1 . ASP A  1 189 ? 80.243  21.038  36.388 1.00 51.40 ? 379 ASP A OD1 1 
ATOM   1479 O  OD2 . ASP A  1 189 ? 78.644  19.942  35.358 1.00 45.33 ? 379 ASP A OD2 1 
ATOM   1480 N  N   . PHE A  1 190 ? 79.972  16.121  36.456 1.00 26.56 ? 380 PHE A N   1 
ATOM   1481 C  CA  . PHE A  1 190 ? 78.923  15.174  36.806 1.00 28.07 ? 380 PHE A CA  1 
ATOM   1482 C  C   . PHE A  1 190 ? 79.131  14.622  38.212 1.00 30.35 ? 380 PHE A C   1 
ATOM   1483 O  O   . PHE A  1 190 ? 78.203  14.582  39.015 1.00 30.54 ? 380 PHE A O   1 
ATOM   1484 C  CB  . PHE A  1 190 ? 78.909  14.015  35.809 1.00 25.30 ? 380 PHE A CB  1 
ATOM   1485 C  CG  . PHE A  1 190 ? 77.905  12.950  36.136 1.00 22.82 ? 380 PHE A CG  1 
ATOM   1486 C  CD1 . PHE A  1 190 ? 76.540  13.223  36.083 1.00 24.04 ? 380 PHE A CD1 1 
ATOM   1487 C  CD2 . PHE A  1 190 ? 78.321  11.676  36.509 1.00 20.61 ? 380 PHE A CD2 1 
ATOM   1488 C  CE1 . PHE A  1 190 ? 75.601  12.241  36.398 1.00 23.73 ? 380 PHE A CE1 1 
ATOM   1489 C  CE2 . PHE A  1 190 ? 77.391  10.683  36.826 1.00 20.00 ? 380 PHE A CE2 1 
ATOM   1490 C  CZ  . PHE A  1 190 ? 76.028  10.967  36.771 1.00 23.71 ? 380 PHE A CZ  1 
ATOM   1491 N  N   . ILE A  1 191 ? 80.357  14.197  38.498 1.00 32.53 ? 381 ILE A N   1 
ATOM   1492 C  CA  . ILE A  1 191 ? 80.696  13.632  39.797 1.00 32.15 ? 381 ILE A CA  1 
ATOM   1493 C  C   . ILE A  1 191 ? 80.647  14.657  40.929 1.00 35.99 ? 381 ILE A C   1 
ATOM   1494 O  O   . ILE A  1 191 ? 80.442  14.300  42.088 1.00 40.30 ? 381 ILE A O   1 
ATOM   1495 C  CB  . ILE A  1 191 ? 82.091  12.974  39.745 1.00 30.16 ? 381 ILE A CB  1 
ATOM   1496 C  CG1 . ILE A  1 191 ? 82.078  11.848  38.705 1.00 28.91 ? 381 ILE A CG1 1 
ATOM   1497 C  CG2 . ILE A  1 191 ? 82.473  12.433  41.114 1.00 24.71 ? 381 ILE A CG2 1 
ATOM   1498 C  CD1 . ILE A  1 191 ? 83.402  11.129  38.534 1.00 26.20 ? 381 ILE A CD1 1 
ATOM   1499 N  N   . MET A  1 192 ? 80.827  15.930  40.598 1.00 39.58 ? 382 MET A N   1 
ATOM   1500 C  CA  . MET A  1 192 ? 80.784  16.980  41.608 1.00 38.69 ? 382 MET A CA  1 
ATOM   1501 C  C   . MET A  1 192 ? 79.336  17.312  41.962 1.00 37.96 ? 382 MET A C   1 
ATOM   1502 O  O   . MET A  1 192 ? 78.958  17.297  43.132 1.00 37.86 ? 382 MET A O   1 
ATOM   1503 C  CB  . MET A  1 192 ? 81.488  18.241  41.101 1.00 44.26 ? 382 MET A CB  1 
ATOM   1504 C  CG  . MET A  1 192 ? 82.957  18.054  40.755 1.00 51.78 ? 382 MET A CG  1 
ATOM   1505 S  SD  . MET A  1 192 ? 83.935  17.436  42.133 1.00 61.55 ? 382 MET A SD  1 
ATOM   1506 C  CE  . MET A  1 192 ? 84.138  18.944  43.102 1.00 62.16 ? 382 MET A CE  1 
ATOM   1507 N  N   . ASN A  1 193 ? 78.533  17.608  40.944 1.00 37.85 ? 383 ASN A N   1 
ATOM   1508 C  CA  . ASN A  1 193 ? 77.125  17.950  41.138 1.00 40.88 ? 383 ASN A CA  1 
ATOM   1509 C  C   . ASN A  1 193 ? 76.354  16.717  41.593 1.00 40.17 ? 383 ASN A C   1 
ATOM   1510 O  O   . ASN A  1 193 ? 75.969  16.622  42.756 1.00 39.90 ? 383 ASN A O   1 
ATOM   1511 C  CB  . ASN A  1 193 ? 76.546  18.505  39.838 1.00 44.83 ? 383 ASN A CB  1 
ATOM   1512 C  CG  . ASN A  1 193 ? 77.308  19.726  39.340 1.00 51.03 ? 383 ASN A CG  1 
ATOM   1513 O  OD1 . ASN A  1 193 ? 77.097  20.192  38.219 1.00 55.26 ? 383 ASN A OD1 1 
ATOM   1514 N  ND2 . ASN A  1 193 ? 78.199  20.252  40.177 1.00 48.73 ? 383 ASN A ND2 1 
ATOM   1515 N  N   . HIS A  1 194 ? 76.112  15.781  40.681 1.00 42.10 ? 384 HIS A N   1 
ATOM   1516 C  CA  . HIS A  1 194 ? 75.435  14.544  41.053 1.00 44.03 ? 384 HIS A CA  1 
ATOM   1517 C  C   . HIS A  1 194 ? 76.524  13.770  41.790 1.00 46.02 ? 384 HIS A C   1 
ATOM   1518 O  O   . HIS A  1 194 ? 77.709  13.979  41.525 1.00 49.35 ? 384 HIS A O   1 
ATOM   1519 C  CB  . HIS A  1 194 ? 75.002  13.755  39.814 1.00 46.12 ? 384 HIS A CB  1 
ATOM   1520 C  CG  . HIS A  1 194 ? 74.074  14.501  38.907 1.00 46.52 ? 384 HIS A CG  1 
ATOM   1521 N  ND1 . HIS A  1 194 ? 74.464  15.616  38.196 1.00 47.25 ? 384 HIS A ND1 1 
ATOM   1522 C  CD2 . HIS A  1 194 ? 72.779  14.280  38.580 1.00 47.14 ? 384 HIS A CD2 1 
ATOM   1523 C  CE1 . HIS A  1 194 ? 73.449  16.048  37.468 1.00 44.80 ? 384 HIS A CE1 1 
ATOM   1524 N  NE2 . HIS A  1 194 ? 72.415  15.255  37.683 1.00 48.54 ? 384 HIS A NE2 1 
ATOM   1525 N  N   . ASN A  1 195 ? 76.156  12.886  42.707 1.00 44.17 ? 385 ASN A N   1 
ATOM   1526 C  CA  . ASN A  1 195 ? 77.192  12.154  43.426 1.00 48.03 ? 385 ASN A CA  1 
ATOM   1527 C  C   . ASN A  1 195 ? 77.166  10.640  43.288 1.00 45.02 ? 385 ASN A C   1 
ATOM   1528 O  O   . ASN A  1 195 ? 76.572  9.946   44.111 1.00 44.68 ? 385 ASN A O   1 
ATOM   1529 C  CB  . ASN A  1 195 ? 77.177  12.530  44.912 1.00 56.08 ? 385 ASN A CB  1 
ATOM   1530 C  CG  . ASN A  1 195 ? 77.910  13.833  45.194 1.00 59.85 ? 385 ASN A CG  1 
ATOM   1531 O  OD1 . ASN A  1 195 ? 77.516  14.899  44.720 1.00 62.30 ? 385 ASN A OD1 1 
ATOM   1532 N  ND2 . ASN A  1 195 ? 78.989  13.749  45.968 1.00 57.68 ? 385 ASN A ND2 1 
ATOM   1533 N  N   . PRO A  1 196 ? 77.820  10.109  42.239 1.00 41.97 ? 386 PRO A N   1 
ATOM   1534 C  CA  . PRO A  1 196 ? 77.876  8.663   42.001 1.00 36.63 ? 386 PRO A CA  1 
ATOM   1535 C  C   . PRO A  1 196 ? 78.631  8.014   43.160 1.00 36.37 ? 386 PRO A C   1 
ATOM   1536 O  O   . PRO A  1 196 ? 79.816  7.702   43.047 1.00 43.24 ? 386 PRO A O   1 
ATOM   1537 C  CB  . PRO A  1 196 ? 78.649  8.558   40.686 1.00 30.52 ? 386 PRO A CB  1 
ATOM   1538 C  CG  . PRO A  1 196 ? 78.333  9.835   40.003 1.00 32.45 ? 386 PRO A CG  1 
ATOM   1539 C  CD  . PRO A  1 196 ? 78.440  10.838  41.121 1.00 37.89 ? 386 PRO A CD  1 
ATOM   1540 N  N   . GLU A  1 197 ? 77.940  7.824   44.275 1.00 33.97 ? 387 GLU A N   1 
ATOM   1541 C  CA  . GLU A  1 197 ? 78.541  7.235   45.464 1.00 36.47 ? 387 GLU A CA  1 
ATOM   1542 C  C   . GLU A  1 197 ? 79.055  5.814   45.244 1.00 32.55 ? 387 GLU A C   1 
ATOM   1543 O  O   . GLU A  1 197 ? 80.083  5.426   45.806 1.00 28.28 ? 387 GLU A O   1 
ATOM   1544 C  CB  . GLU A  1 197 ? 77.523  7.226   46.612 1.00 44.26 ? 387 GLU A CB  1 
ATOM   1545 C  CG  . GLU A  1 197 ? 76.439  6.157   46.478 1.00 51.38 ? 387 GLU A CG  1 
ATOM   1546 C  CD  . GLU A  1 197 ? 75.571  6.334   45.241 1.00 53.82 ? 387 GLU A CD  1 
ATOM   1547 O  OE1 . GLU A  1 197 ? 74.880  5.365   44.856 1.00 54.83 ? 387 GLU A OE1 1 
ATOM   1548 O  OE2 . GLU A  1 197 ? 75.566  7.440   44.659 1.00 51.44 ? 387 GLU A OE2 1 
ATOM   1549 N  N   . CYS A  1 198 ? 78.346  5.047   44.421 1.00 26.30 ? 388 CYS A N   1 
ATOM   1550 C  CA  . CYS A  1 198 ? 78.713  3.658   44.172 1.00 26.59 ? 388 CYS A CA  1 
ATOM   1551 C  C   . CYS A  1 198 ? 80.089  3.424   43.547 1.00 26.67 ? 388 CYS A C   1 
ATOM   1552 O  O   . CYS A  1 198 ? 80.585  2.298   43.565 1.00 21.72 ? 388 CYS A O   1 
ATOM   1553 C  CB  . CYS A  1 198 ? 77.634  2.973   43.325 1.00 29.26 ? 388 CYS A CB  1 
ATOM   1554 S  SG  . CYS A  1 198 ? 77.815  3.142   41.519 1.00 38.11 ? 388 CYS A SG  1 
ATOM   1555 N  N   . ILE A  1 199 ? 80.712  4.466   43.002 1.00 25.73 ? 389 ILE A N   1 
ATOM   1556 C  CA  . ILE A  1 199 ? 82.033  4.303   42.391 1.00 25.10 ? 389 ILE A CA  1 
ATOM   1557 C  C   . ILE A  1 199 ? 83.183  4.806   43.265 1.00 28.40 ? 389 ILE A C   1 
ATOM   1558 O  O   . ILE A  1 199 ? 84.308  4.960   42.785 1.00 31.40 ? 389 ILE A O   1 
ATOM   1559 C  CB  . ILE A  1 199 ? 82.134  5.029   41.032 1.00 24.69 ? 389 ILE A CB  1 
ATOM   1560 C  CG1 . ILE A  1 199 ? 81.822  6.514   41.218 1.00 22.64 ? 389 ILE A CG1 1 
ATOM   1561 C  CG2 . ILE A  1 199 ? 81.214  4.368   40.017 1.00 19.48 ? 389 ILE A CG2 1 
ATOM   1562 C  CD1 . ILE A  1 199 ? 82.122  7.362   40.011 1.00 17.89 ? 389 ILE A CD1 1 
ATOM   1563 N  N   . LEU A  1 200 ? 82.902  5.060   44.541 1.00 26.38 ? 390 LEU A N   1 
ATOM   1564 C  CA  . LEU A  1 200 ? 83.915  5.543   45.478 1.00 19.33 ? 390 LEU A CA  1 
ATOM   1565 C  C   . LEU A  1 200 ? 84.774  4.399   46.003 1.00 18.16 ? 390 LEU A C   1 
ATOM   1566 O  O   . LEU A  1 200 ? 86.002  4.482   46.016 1.00 15.57 ? 390 LEU A O   1 
ATOM   1567 C  CB  . LEU A  1 200 ? 83.246  6.229   46.664 1.00 19.87 ? 390 LEU A CB  1 
ATOM   1568 C  CG  . LEU A  1 200 ? 82.335  7.405   46.344 1.00 19.71 ? 390 LEU A CG  1 
ATOM   1569 C  CD1 . LEU A  1 200 ? 81.443  7.695   47.540 1.00 17.79 ? 390 LEU A CD1 1 
ATOM   1570 C  CD2 . LEU A  1 200 ? 83.184  8.605   45.965 1.00 13.21 ? 390 LEU A CD2 1 
ATOM   1571 N  N   . ASN A  1 201 ? 84.109  3.334   46.440 1.00 17.18 ? 391 ASN A N   1 
ATOM   1572 C  CA  . ASN A  1 201 ? 84.779  2.161   46.984 1.00 19.77 ? 391 ASN A CA  1 
ATOM   1573 C  C   . ASN A  1 201 ? 85.782  1.531   46.023 1.00 21.66 ? 391 ASN A C   1 
ATOM   1574 O  O   . ASN A  1 201 ? 85.499  1.348   44.839 1.00 24.54 ? 391 ASN A O   1 
ATOM   1575 C  CB  . ASN A  1 201 ? 83.738  1.116   47.364 1.00 17.41 ? 391 ASN A CB  1 
ATOM   1576 C  CG  . ASN A  1 201 ? 82.935  0.653   46.173 1.00 20.05 ? 391 ASN A CG  1 
ATOM   1577 O  OD1 . ASN A  1 201 ? 83.110  -0.462  45.686 1.00 21.10 ? 391 ASN A OD1 1 
ATOM   1578 N  ND2 . ASN A  1 201 ? 82.057  1.518   45.684 1.00 28.21 ? 391 ASN A ND2 1 
ATOM   1579 N  N   . GLU A  1 202 ? 86.957  1.202   46.547 1.00 22.83 ? 392 GLU A N   1 
ATOM   1580 C  CA  . GLU A  1 202 ? 88.001  0.560   45.760 1.00 24.37 ? 392 GLU A CA  1 
ATOM   1581 C  C   . GLU A  1 202 ? 87.697  -0.935  45.771 1.00 25.26 ? 392 GLU A C   1 
ATOM   1582 O  O   . GLU A  1 202 ? 87.599  -1.546  46.834 1.00 28.79 ? 392 GLU A O   1 
ATOM   1583 C  CB  . GLU A  1 202 ? 89.370  0.807   46.394 1.00 23.12 ? 392 GLU A CB  1 
ATOM   1584 C  CG  . GLU A  1 202 ? 90.519  0.111   45.685 1.00 32.70 ? 392 GLU A CG  1 
ATOM   1585 C  CD  . GLU A  1 202 ? 91.843  0.296   46.403 1.00 38.22 ? 392 GLU A CD  1 
ATOM   1586 O  OE1 . GLU A  1 202 ? 92.874  -0.191  45.890 1.00 39.64 ? 392 GLU A OE1 1 
ATOM   1587 O  OE2 . GLU A  1 202 ? 91.852  0.926   47.484 1.00 37.00 ? 392 GLU A OE2 1 
ATOM   1588 N  N   . PRO A  1 203 ? 87.537  -1.545  44.590 1.00 23.93 ? 393 PRO A N   1 
ATOM   1589 C  CA  . PRO A  1 203 ? 87.241  -2.978  44.567 1.00 23.17 ? 393 PRO A CA  1 
ATOM   1590 C  C   . PRO A  1 203 ? 88.321  -3.828  45.240 1.00 24.44 ? 393 PRO A C   1 
ATOM   1591 O  O   . PRO A  1 203 ? 89.501  -3.473  45.235 1.00 27.15 ? 393 PRO A O   1 
ATOM   1592 C  CB  . PRO A  1 203 ? 87.101  -3.269  43.074 1.00 21.06 ? 393 PRO A CB  1 
ATOM   1593 C  CG  . PRO A  1 203 ? 88.037  -2.279  42.451 1.00 14.23 ? 393 PRO A CG  1 
ATOM   1594 C  CD  . PRO A  1 203 ? 87.733  -1.026  43.225 1.00 18.90 ? 393 PRO A CD  1 
ATOM   1595 N  N   . LEU A  1 204 ? 87.905  -4.942  45.833 1.00 24.53 ? 394 LEU A N   1 
ATOM   1596 C  CA  . LEU A  1 204 ? 88.835  -5.850  46.495 1.00 26.15 ? 394 LEU A CA  1 
ATOM   1597 C  C   . LEU A  1 204 ? 89.336  -6.873  45.485 1.00 23.78 ? 394 LEU A C   1 
ATOM   1598 O  O   . LEU A  1 204 ? 88.579  -7.321  44.620 1.00 17.43 ? 394 LEU A O   1 
ATOM   1599 C  CB  . LEU A  1 204 ? 88.148  -6.569  47.660 1.00 31.49 ? 394 LEU A CB  1 
ATOM   1600 C  CG  . LEU A  1 204 ? 87.712  -5.692  48.839 1.00 37.56 ? 394 LEU A CG  1 
ATOM   1601 C  CD1 . LEU A  1 204 ? 86.942  -6.525  49.857 1.00 33.16 ? 394 LEU A CD1 1 
ATOM   1602 C  CD2 . LEU A  1 204 ? 88.937  -5.056  49.474 1.00 34.62 ? 394 LEU A CD2 1 
ATOM   1603 N  N   . GLY A  1 205 ? 90.611  -7.234  45.603 1.00 21.80 ? 395 GLY A N   1 
ATOM   1604 C  CA  . GLY A  1 205 ? 91.216  -8.196  44.698 1.00 23.24 ? 395 GLY A CA  1 
ATOM   1605 C  C   . GLY A  1 205 ? 90.320  -9.354  44.295 1.00 27.78 ? 395 GLY A C   1 
ATOM   1606 O  O   . GLY A  1 205 ? 90.188  -9.659  43.107 1.00 26.16 ? 395 GLY A O   1 
ATOM   1607 N  N   . THR A  1 206 ? 89.702  -9.997  45.281 1.00 26.36 ? 396 THR A N   1 
ATOM   1608 C  CA  . THR A  1 206 ? 88.823  -11.134 45.027 1.00 27.96 ? 396 THR A CA  1 
ATOM   1609 C  C   . THR A  1 206 ? 87.565  -10.789 44.227 1.00 28.66 ? 396 THR A C   1 
ATOM   1610 O  O   . THR A  1 206 ? 86.960  -11.668 43.614 1.00 28.78 ? 396 THR A O   1 
ATOM   1611 C  CB  . THR A  1 206 ? 88.391  -11.798 46.344 1.00 26.00 ? 396 THR A CB  1 
ATOM   1612 O  OG1 . THR A  1 206 ? 87.907  -10.793 47.241 1.00 27.47 ? 396 THR A OG1 1 
ATOM   1613 C  CG2 . THR A  1 206 ? 89.559  -12.529 46.982 1.00 32.10 ? 396 THR A CG2 1 
ATOM   1614 N  N   . ASP A  1 207 ? 87.167  -9.519  44.240 1.00 29.55 ? 397 ASP A N   1 
ATOM   1615 C  CA  . ASP A  1 207 ? 85.980  -9.086  43.504 1.00 28.89 ? 397 ASP A CA  1 
ATOM   1616 C  C   . ASP A  1 207 ? 86.232  -9.031  42.001 1.00 24.62 ? 397 ASP A C   1 
ATOM   1617 O  O   . ASP A  1 207 ? 85.296  -8.993  41.206 1.00 25.28 ? 397 ASP A O   1 
ATOM   1618 C  CB  . ASP A  1 207 ? 85.524  -7.705  43.978 1.00 34.88 ? 397 ASP A CB  1 
ATOM   1619 C  CG  . ASP A  1 207 ? 84.807  -7.752  45.310 1.00 44.00 ? 397 ASP A CG  1 
ATOM   1620 O  OD1 . ASP A  1 207 ? 83.835  -8.531  45.435 1.00 43.51 ? 397 ASP A OD1 1 
ATOM   1621 O  OD2 . ASP A  1 207 ? 85.209  -7.002  46.227 1.00 45.53 ? 397 ASP A OD2 1 
ATOM   1622 N  N   . ILE A  1 208 ? 87.504  -9.029  41.624 1.00 20.12 ? 398 ILE A N   1 
ATOM   1623 C  CA  . ILE A  1 208 ? 87.902  -8.965  40.226 1.00 16.25 ? 398 ILE A CA  1 
ATOM   1624 C  C   . ILE A  1 208 ? 88.010  -10.369 39.624 1.00 17.44 ? 398 ILE A C   1 
ATOM   1625 O  O   . ILE A  1 208 ? 88.844  -11.176 40.036 1.00 16.36 ? 398 ILE A O   1 
ATOM   1626 C  CB  . ILE A  1 208 ? 89.244  -8.222  40.105 1.00 16.63 ? 398 ILE A CB  1 
ATOM   1627 C  CG1 . ILE A  1 208 ? 89.105  -6.838  40.739 1.00 5.38  ? 398 ILE A CG1 1 
ATOM   1628 C  CG2 . ILE A  1 208 ? 89.667  -8.114  38.649 1.00 18.28 ? 398 ILE A CG2 1 
ATOM   1629 C  CD1 . ILE A  1 208 ? 90.410  -6.082  40.849 1.00 19.87 ? 398 ILE A CD1 1 
ATOM   1630 N  N   . ILE A  1 209 ? 87.157  -10.646 38.642 1.00 18.17 ? 399 ILE A N   1 
ATOM   1631 C  CA  . ILE A  1 209 ? 87.115  -11.948 37.984 1.00 20.77 ? 399 ILE A CA  1 
ATOM   1632 C  C   . ILE A  1 209 ? 88.183  -12.132 36.921 1.00 19.72 ? 399 ILE A C   1 
ATOM   1633 O  O   . ILE A  1 209 ? 88.513  -13.257 36.548 1.00 20.38 ? 399 ILE A O   1 
ATOM   1634 C  CB  . ILE A  1 209 ? 85.764  -12.173 37.307 1.00 23.07 ? 399 ILE A CB  1 
ATOM   1635 C  CG1 . ILE A  1 209 ? 85.555  -11.103 36.234 1.00 24.31 ? 399 ILE A CG1 1 
ATOM   1636 C  CG2 . ILE A  1 209 ? 84.650  -12.126 38.343 1.00 30.59 ? 399 ILE A CG2 1 
ATOM   1637 C  CD1 . ILE A  1 209 ? 84.395  -11.365 35.334 1.00 25.61 ? 399 ILE A CD1 1 
ATOM   1638 N  N   . SER A  1 210 ? 88.705  -11.023 36.417 1.00 19.10 ? 400 SER A N   1 
ATOM   1639 C  CA  . SER A  1 210 ? 89.725  -11.076 35.385 1.00 17.14 ? 400 SER A CA  1 
ATOM   1640 C  C   . SER A  1 210 ? 91.078  -11.436 35.972 1.00 19.62 ? 400 SER A C   1 
ATOM   1641 O  O   . SER A  1 210 ? 91.412  -11.030 37.085 1.00 21.59 ? 400 SER A O   1 
ATOM   1642 C  CB  . SER A  1 210 ? 89.824  -9.724  34.686 1.00 16.24 ? 400 SER A CB  1 
ATOM   1643 O  OG  . SER A  1 210 ? 90.181  -8.712  35.611 1.00 15.62 ? 400 SER A OG  1 
ATOM   1644 N  N   . PRO A  1 211 ? 91.871  -12.223 35.233 1.00 21.10 ? 401 PRO A N   1 
ATOM   1645 C  CA  . PRO A  1 211 ? 93.200  -12.623 35.699 1.00 19.66 ? 401 PRO A CA  1 
ATOM   1646 C  C   . PRO A  1 211 ? 93.963  -11.381 36.133 1.00 17.63 ? 401 PRO A C   1 
ATOM   1647 O  O   . PRO A  1 211 ? 93.948  -10.365 35.443 1.00 14.47 ? 401 PRO A O   1 
ATOM   1648 C  CB  . PRO A  1 211 ? 93.807  -13.276 34.463 1.00 12.76 ? 401 PRO A CB  1 
ATOM   1649 C  CG  . PRO A  1 211 ? 92.625  -13.945 33.852 1.00 15.74 ? 401 PRO A CG  1 
ATOM   1650 C  CD  . PRO A  1 211 ? 91.546  -12.880 33.956 1.00 22.75 ? 401 PRO A CD  1 
ATOM   1651 N  N   . PRO A  1 212 ? 94.630  -11.438 37.291 1.00 21.91 ? 402 PRO A N   1 
ATOM   1652 C  CA  . PRO A  1 212 ? 95.366  -10.249 37.721 1.00 22.04 ? 402 PRO A CA  1 
ATOM   1653 C  C   . PRO A  1 212 ? 96.411  -9.820  36.700 1.00 21.29 ? 402 PRO A C   1 
ATOM   1654 O  O   . PRO A  1 212 ? 97.033  -10.654 36.043 1.00 22.41 ? 402 PRO A O   1 
ATOM   1655 C  CB  . PRO A  1 212 ? 95.970  -10.680 39.057 1.00 20.62 ? 402 PRO A CB  1 
ATOM   1656 C  CG  . PRO A  1 212 ? 96.110  -12.159 38.908 1.00 26.30 ? 402 PRO A CG  1 
ATOM   1657 C  CD  . PRO A  1 212 ? 94.828  -12.552 38.233 1.00 17.52 ? 402 PRO A CD  1 
ATOM   1658 N  N   . VAL A  1 213 ? 96.572  -8.509  36.554 1.00 17.28 ? 403 VAL A N   1 
ATOM   1659 C  CA  . VAL A  1 213 ? 97.543  -7.947  35.628 1.00 13.12 ? 403 VAL A CA  1 
ATOM   1660 C  C   . VAL A  1 213 ? 98.444  -7.008  36.404 1.00 15.54 ? 403 VAL A C   1 
ATOM   1661 O  O   . VAL A  1 213 ? 97.966  -6.085  37.061 1.00 10.95 ? 403 VAL A O   1 
ATOM   1662 C  CB  . VAL A  1 213 ? 96.863  -7.135  34.500 1.00 19.33 ? 403 VAL A CB  1 
ATOM   1663 C  CG1 . VAL A  1 213 ? 97.901  -6.264  33.783 1.00 9.51  ? 403 VAL A CG1 1 
ATOM   1664 C  CG2 . VAL A  1 213 ? 96.189  -8.077  33.509 1.00 6.87  ? 403 VAL A CG2 1 
ATOM   1665 N  N   . CYS A  1 214 ? 99.749  -7.246  36.336 1.00 17.56 ? 404 CYS A N   1 
ATOM   1666 C  CA  . CYS A  1 214 ? 100.682 -6.386  37.040 1.00 16.30 ? 404 CYS A CA  1 
ATOM   1667 C  C   . CYS A  1 214 ? 101.008 -5.136  36.225 1.00 13.91 ? 404 CYS A C   1 
ATOM   1668 O  O   . CYS A  1 214 ? 101.630 -5.217  35.165 1.00 5.67  ? 404 CYS A O   1 
ATOM   1669 C  CB  . CYS A  1 214 ? 101.979 -7.129  37.374 1.00 18.19 ? 404 CYS A CB  1 
ATOM   1670 S  SG  . CYS A  1 214 ? 103.188 -5.957  38.061 1.00 32.80 ? 404 CYS A SG  1 
ATOM   1671 N  N   . GLY A  1 215 ? 100.584 -3.982  36.733 1.00 11.86 ? 405 GLY A N   1 
ATOM   1672 C  CA  . GLY A  1 215 ? 100.839 -2.726  36.050 1.00 10.84 ? 405 GLY A CA  1 
ATOM   1673 C  C   . GLY A  1 215 ? 99.576  -2.034  35.565 1.00 15.70 ? 405 GLY A C   1 
ATOM   1674 O  O   . GLY A  1 215 ? 99.646  -1.018  34.868 1.00 13.55 ? 405 GLY A O   1 
ATOM   1675 N  N   . ASN A  1 216 ? 98.417  -2.580  35.930 1.00 10.64 ? 406 ASN A N   1 
ATOM   1676 C  CA  . ASN A  1 216 ? 97.146  -2.001  35.524 1.00 8.24  ? 406 ASN A CA  1 
ATOM   1677 C  C   . ASN A  1 216 ? 96.645  -1.015  36.576 1.00 12.05 ? 406 ASN A C   1 
ATOM   1678 O  O   . ASN A  1 216 ? 95.550  -0.467  36.461 1.00 7.92  ? 406 ASN A O   1 
ATOM   1679 C  CB  . ASN A  1 216 ? 96.112  -3.105  35.303 1.00 15.55 ? 406 ASN A CB  1 
ATOM   1680 C  CG  . ASN A  1 216 ? 95.745  -3.827  36.582 1.00 20.80 ? 406 ASN A CG  1 
ATOM   1681 O  OD1 . ASN A  1 216 ? 96.296  -3.549  37.649 1.00 23.29 ? 406 ASN A OD1 1 
ATOM   1682 N  ND2 . ASN A  1 216 ? 94.808  -4.764  36.480 1.00 19.82 ? 406 ASN A ND2 1 
ATOM   1683 N  N   . GLU A  1 217 ? 97.462  -0.798  37.600 1.00 16.16 ? 407 GLU A N   1 
ATOM   1684 C  CA  . GLU A  1 217 ? 97.139  0.121   38.687 1.00 17.15 ? 407 GLU A CA  1 
ATOM   1685 C  C   . GLU A  1 217 ? 95.994  -0.367  39.561 1.00 16.86 ? 407 GLU A C   1 
ATOM   1686 O  O   . GLU A  1 217 ? 95.387  0.406   40.299 1.00 15.13 ? 407 GLU A O   1 
ATOM   1687 C  CB  . GLU A  1 217 ? 96.828  1.511   38.125 1.00 15.61 ? 407 GLU A CB  1 
ATOM   1688 C  CG  . GLU A  1 217 ? 97.992  2.095   37.339 1.00 22.13 ? 407 GLU A CG  1 
ATOM   1689 C  CD  . GLU A  1 217 ? 97.808  3.554   36.989 1.00 25.21 ? 407 GLU A CD  1 
ATOM   1690 O  OE1 . GLU A  1 217 ? 98.736  4.135   36.389 1.00 22.54 ? 407 GLU A OE1 1 
ATOM   1691 O  OE2 . GLU A  1 217 ? 96.741  4.120   37.312 1.00 30.69 ? 407 GLU A OE2 1 
ATOM   1692 N  N   . LEU A  1 218 ? 95.705  -1.660  39.475 1.00 18.32 ? 408 LEU A N   1 
ATOM   1693 C  CA  . LEU A  1 218 ? 94.652  -2.267  40.277 1.00 18.69 ? 408 LEU A CA  1 
ATOM   1694 C  C   . LEU A  1 218 ? 95.276  -3.317  41.182 1.00 20.20 ? 408 LEU A C   1 
ATOM   1695 O  O   . LEU A  1 218 ? 95.703  -4.372  40.712 1.00 22.17 ? 408 LEU A O   1 
ATOM   1696 C  CB  . LEU A  1 218 ? 93.605  -2.922  39.379 1.00 14.00 ? 408 LEU A CB  1 
ATOM   1697 C  CG  . LEU A  1 218 ? 92.713  -1.968  38.585 1.00 17.97 ? 408 LEU A CG  1 
ATOM   1698 C  CD1 . LEU A  1 218 ? 91.859  -2.769  37.614 1.00 5.39  ? 408 LEU A CD1 1 
ATOM   1699 C  CD2 . LEU A  1 218 ? 91.838  -1.155  39.546 1.00 8.45  ? 408 LEU A CD2 1 
ATOM   1700 N  N   . LEU A  1 219 ? 95.346  -3.028  42.478 1.00 20.94 ? 409 LEU A N   1 
ATOM   1701 C  CA  . LEU A  1 219 ? 95.927  -3.983  43.408 1.00 20.11 ? 409 LEU A CA  1 
ATOM   1702 C  C   . LEU A  1 219 ? 95.070  -5.238  43.347 1.00 20.86 ? 409 LEU A C   1 
ATOM   1703 O  O   . LEU A  1 219 ? 93.922  -5.252  43.797 1.00 20.37 ? 409 LEU A O   1 
ATOM   1704 C  CB  . LEU A  1 219 ? 95.953  -3.418  44.829 1.00 11.84 ? 409 LEU A CB  1 
ATOM   1705 C  CG  . LEU A  1 219 ? 96.710  -4.292  45.832 1.00 7.60  ? 409 LEU A CG  1 
ATOM   1706 C  CD1 . LEU A  1 219 ? 98.120  -4.548  45.332 1.00 8.64  ? 409 LEU A CD1 1 
ATOM   1707 C  CD2 . LEU A  1 219 ? 96.749  -3.609  47.184 1.00 7.01  ? 409 LEU A CD2 1 
ATOM   1708 N  N   . GLU A  1 220 ? 95.633  -6.292  42.774 1.00 18.72 ? 410 GLU A N   1 
ATOM   1709 C  CA  . GLU A  1 220 ? 94.903  -7.535  42.620 1.00 16.00 ? 410 GLU A CA  1 
ATOM   1710 C  C   . GLU A  1 220 ? 95.534  -8.691  43.380 1.00 13.24 ? 410 GLU A C   1 
ATOM   1711 O  O   . GLU A  1 220 ? 96.716  -8.659  43.722 1.00 9.66  ? 410 GLU A O   1 
ATOM   1712 C  CB  . GLU A  1 220 ? 94.792  -7.860  41.130 1.00 21.21 ? 410 GLU A CB  1 
ATOM   1713 C  CG  . GLU A  1 220 ? 94.126  -6.746  40.329 1.00 18.30 ? 410 GLU A CG  1 
ATOM   1714 C  CD  . GLU A  1 220 ? 94.361  -6.865  38.838 1.00 22.05 ? 410 GLU A CD  1 
ATOM   1715 O  OE1 . GLU A  1 220 ? 95.537  -6.931  38.419 1.00 24.20 ? 410 GLU A OE1 1 
ATOM   1716 O  OE2 . GLU A  1 220 ? 93.369  -6.883  38.082 1.00 24.43 ? 410 GLU A OE2 1 
ATOM   1717 N  N   . VAL A  1 221 ? 94.726  -9.712  43.645 1.00 13.35 ? 411 VAL A N   1 
ATOM   1718 C  CA  . VAL A  1 221 ? 95.174  -10.890 44.373 1.00 11.41 ? 411 VAL A CA  1 
ATOM   1719 C  C   . VAL A  1 221 ? 96.518  -11.421 43.886 1.00 11.37 ? 411 VAL A C   1 
ATOM   1720 O  O   . VAL A  1 221 ? 96.734  -11.601 42.686 1.00 13.90 ? 411 VAL A O   1 
ATOM   1721 C  CB  . VAL A  1 221 ? 94.109  -12.000 44.298 1.00 6.17  ? 411 VAL A CB  1 
ATOM   1722 C  CG1 . VAL A  1 221 ? 94.651  -13.298 44.870 1.00 8.00  ? 411 VAL A CG1 1 
ATOM   1723 C  CG2 . VAL A  1 221 ? 92.873  -11.561 45.077 1.00 1.00  ? 411 VAL A CG2 1 
ATOM   1724 N  N   . GLY A  1 222 ? 97.419  -11.657 44.836 1.00 9.61  ? 412 GLY A N   1 
ATOM   1725 C  CA  . GLY A  1 222 ? 98.739  -12.160 44.509 1.00 11.94 ? 412 GLY A CA  1 
ATOM   1726 C  C   . GLY A  1 222 ? 99.773  -11.057 44.380 1.00 15.82 ? 412 GLY A C   1 
ATOM   1727 O  O   . GLY A  1 222 ? 100.977 -11.319 44.401 1.00 22.84 ? 412 GLY A O   1 
ATOM   1728 N  N   . GLU A  1 223 ? 99.309  -9.818  44.243 1.00 16.62 ? 413 GLU A N   1 
ATOM   1729 C  CA  . GLU A  1 223 ? 100.213 -8.679  44.108 1.00 14.27 ? 413 GLU A CA  1 
ATOM   1730 C  C   . GLU A  1 223 ? 100.387 -7.942  45.432 1.00 14.54 ? 413 GLU A C   1 
ATOM   1731 O  O   . GLU A  1 223 ? 99.415  -7.713  46.157 1.00 11.31 ? 413 GLU A O   1 
ATOM   1732 C  CB  . GLU A  1 223 ? 99.673  -7.686  43.080 1.00 13.90 ? 413 GLU A CB  1 
ATOM   1733 C  CG  . GLU A  1 223 ? 99.127  -8.304  41.810 1.00 19.07 ? 413 GLU A CG  1 
ATOM   1734 C  CD  . GLU A  1 223 ? 98.676  -7.250  40.810 1.00 21.62 ? 413 GLU A CD  1 
ATOM   1735 O  OE1 . GLU A  1 223 ? 97.936  -6.321  41.211 1.00 12.55 ? 413 GLU A OE1 1 
ATOM   1736 O  OE2 . GLU A  1 223 ? 99.061  -7.357  39.624 1.00 17.81 ? 413 GLU A OE2 1 
ATOM   1737 N  N   . GLU A  1 224 ? 101.624 -7.571  45.743 1.00 12.23 ? 414 GLU A N   1 
ATOM   1738 C  CA  . GLU A  1 224 ? 101.904 -6.824  46.964 1.00 18.28 ? 414 GLU A CA  1 
ATOM   1739 C  C   . GLU A  1 224 ? 101.555 -5.368  46.692 1.00 19.91 ? 414 GLU A C   1 
ATOM   1740 O  O   . GLU A  1 224 ? 101.068 -4.656  47.567 1.00 21.91 ? 414 GLU A O   1 
ATOM   1741 C  CB  . GLU A  1 224 ? 103.384 -6.913  47.324 1.00 23.57 ? 414 GLU A CB  1 
ATOM   1742 C  CG  . GLU A  1 224 ? 103.843 -8.268  47.802 1.00 28.57 ? 414 GLU A CG  1 
ATOM   1743 C  CD  . GLU A  1 224 ? 105.348 -8.381  47.791 1.00 32.03 ? 414 GLU A CD  1 
ATOM   1744 O  OE1 . GLU A  1 224 ? 106.018 -7.367  48.082 1.00 29.93 ? 414 GLU A OE1 1 
ATOM   1745 O  OE2 . GLU A  1 224 ? 105.861 -9.482  47.498 1.00 36.66 ? 414 GLU A OE2 1 
ATOM   1746 N  N   . CYS A  1 225 ? 101.806 -4.935  45.462 1.00 20.25 ? 415 CYS A N   1 
ATOM   1747 C  CA  . CYS A  1 225 ? 101.528 -3.567  45.064 1.00 24.26 ? 415 CYS A CA  1 
ATOM   1748 C  C   . CYS A  1 225 ? 101.413 -3.452  43.550 1.00 25.59 ? 415 CYS A C   1 
ATOM   1749 O  O   . CYS A  1 225 ? 101.894 -4.312  42.816 1.00 28.59 ? 415 CYS A O   1 
ATOM   1750 C  CB  . CYS A  1 225 ? 102.646 -2.661  45.555 1.00 27.14 ? 415 CYS A CB  1 
ATOM   1751 S  SG  . CYS A  1 225 ? 104.288 -3.120  44.914 1.00 34.11 ? 415 CYS A SG  1 
ATOM   1752 N  N   . ASP A  1 226 ? 100.778 -2.381  43.087 1.00 25.96 ? 416 ASP A N   1 
ATOM   1753 C  CA  . ASP A  1 226 ? 100.622 -2.152  41.655 1.00 25.53 ? 416 ASP A CA  1 
ATOM   1754 C  C   . ASP A  1 226 ? 100.575 -0.655  41.375 1.00 23.13 ? 416 ASP A C   1 
ATOM   1755 O  O   . ASP A  1 226 ? 99.558  -0.006  41.609 1.00 19.72 ? 416 ASP A O   1 
ATOM   1756 C  CB  . ASP A  1 226 ? 99.340  -2.812  41.143 1.00 26.90 ? 416 ASP A CB  1 
ATOM   1757 C  CG  . ASP A  1 226 ? 99.301  -2.906  39.634 1.00 27.02 ? 416 ASP A CG  1 
ATOM   1758 O  OD1 . ASP A  1 226 ? 99.508  -1.870  38.968 1.00 26.46 ? 416 ASP A OD1 1 
ATOM   1759 O  OD2 . ASP A  1 226 ? 99.065  -4.016  39.114 1.00 31.26 ? 416 ASP A OD2 1 
ATOM   1760 N  N   . CYS A  1 227 ? 101.680 -0.110  40.877 1.00 25.18 ? 417 CYS A N   1 
ATOM   1761 C  CA  . CYS A  1 227 ? 101.753 1.317   40.579 1.00 29.29 ? 417 CYS A CA  1 
ATOM   1762 C  C   . CYS A  1 227 ? 101.803 1.590   39.081 1.00 29.31 ? 417 CYS A C   1 
ATOM   1763 O  O   . CYS A  1 227 ? 102.444 2.544   38.639 1.00 32.09 ? 417 CYS A O   1 
ATOM   1764 C  CB  . CYS A  1 227 ? 102.977 1.943   41.267 1.00 31.65 ? 417 CYS A CB  1 
ATOM   1765 S  SG  . CYS A  1 227 ? 104.601 1.226   40.832 1.00 38.90 ? 417 CYS A SG  1 
ATOM   1766 N  N   . GLY A  1 228 ? 101.120 0.756   38.304 1.00 26.10 ? 418 GLY A N   1 
ATOM   1767 C  CA  . GLY A  1 228 ? 101.109 0.935   36.864 1.00 25.65 ? 418 GLY A CA  1 
ATOM   1768 C  C   . GLY A  1 228 ? 102.396 0.477   36.205 1.00 25.91 ? 418 GLY A C   1 
ATOM   1769 O  O   . GLY A  1 228 ? 103.072 -0.426  36.698 1.00 30.42 ? 418 GLY A O   1 
ATOM   1770 N  N   . THR A  1 229 ? 102.738 1.093   35.081 1.00 23.25 ? 419 THR A N   1 
ATOM   1771 C  CA  . THR A  1 229 ? 103.953 0.726   34.369 1.00 26.18 ? 419 THR A CA  1 
ATOM   1772 C  C   . THR A  1 229 ? 105.144 1.427   35.008 1.00 23.98 ? 419 THR A C   1 
ATOM   1773 O  O   . THR A  1 229 ? 104.978 2.421   35.717 1.00 19.43 ? 419 THR A O   1 
ATOM   1774 C  CB  . THR A  1 229 ? 103.875 1.128   32.882 1.00 27.79 ? 419 THR A CB  1 
ATOM   1775 O  OG1 . THR A  1 229 ? 103.828 2.558   32.770 1.00 34.82 ? 419 THR A OG1 1 
ATOM   1776 C  CG2 . THR A  1 229 ? 102.633 0.533   32.239 1.00 25.30 ? 419 THR A CG2 1 
ATOM   1777 N  N   . PRO A  1 230 ? 106.361 0.909   34.776 1.00 23.55 ? 420 PRO A N   1 
ATOM   1778 C  CA  . PRO A  1 230 ? 107.577 1.503   35.338 1.00 25.38 ? 420 PRO A CA  1 
ATOM   1779 C  C   . PRO A  1 230 ? 107.660 2.993   35.025 1.00 30.62 ? 420 PRO A C   1 
ATOM   1780 O  O   . PRO A  1 230 ? 108.130 3.789   35.842 1.00 33.90 ? 420 PRO A O   1 
ATOM   1781 C  CB  . PRO A  1 230 ? 108.687 0.706   34.663 1.00 21.03 ? 420 PRO A CB  1 
ATOM   1782 C  CG  . PRO A  1 230 ? 108.069 -0.653  34.523 1.00 27.42 ? 420 PRO A CG  1 
ATOM   1783 C  CD  . PRO A  1 230 ? 106.680 -0.317  34.021 1.00 28.05 ? 420 PRO A CD  1 
ATOM   1784 N  N   . GLU A  1 231 ? 107.187 3.364   33.841 1.00 33.66 ? 421 GLU A N   1 
ATOM   1785 C  CA  . GLU A  1 231 ? 107.202 4.754   33.407 1.00 37.32 ? 421 GLU A CA  1 
ATOM   1786 C  C   . GLU A  1 231 ? 106.243 5.626   34.217 1.00 35.78 ? 421 GLU A C   1 
ATOM   1787 O  O   . GLU A  1 231 ? 106.592 6.737   34.613 1.00 38.09 ? 421 GLU A O   1 
ATOM   1788 C  CB  . GLU A  1 231 ? 106.832 4.839   31.926 1.00 44.78 ? 421 GLU A CB  1 
ATOM   1789 C  CG  . GLU A  1 231 ? 107.637 3.909   31.031 1.00 58.15 ? 421 GLU A CG  1 
ATOM   1790 C  CD  . GLU A  1 231 ? 107.239 4.014   29.569 1.00 64.31 ? 421 GLU A CD  1 
ATOM   1791 O  OE1 . GLU A  1 231 ? 107.479 5.078   28.957 1.00 64.89 ? 421 GLU A OE1 1 
ATOM   1792 O  OE2 . GLU A  1 231 ? 106.679 3.032   29.036 1.00 67.46 ? 421 GLU A OE2 1 
ATOM   1793 N  N   . ASN A  1 232 ? 105.040 5.116   34.464 1.00 29.29 ? 422 ASN A N   1 
ATOM   1794 C  CA  . ASN A  1 232 ? 104.025 5.860   35.202 1.00 26.55 ? 422 ASN A CA  1 
ATOM   1795 C  C   . ASN A  1 232 ? 104.088 5.729   36.717 1.00 28.69 ? 422 ASN A C   1 
ATOM   1796 O  O   . ASN A  1 232 ? 103.470 6.520   37.435 1.00 28.25 ? 422 ASN A O   1 
ATOM   1797 C  CB  . ASN A  1 232 ? 102.632 5.432   34.743 1.00 31.33 ? 422 ASN A CB  1 
ATOM   1798 C  CG  . ASN A  1 232 ? 102.293 5.934   33.361 1.00 32.37 ? 422 ASN A CG  1 
ATOM   1799 O  OD1 . ASN A  1 232 ? 101.273 5.552   32.786 1.00 35.54 ? 422 ASN A OD1 1 
ATOM   1800 N  ND2 . ASN A  1 232 ? 103.140 6.802   32.821 1.00 32.13 ? 422 ASN A ND2 1 
ATOM   1801 N  N   . CYS A  1 233 ? 104.825 4.737   37.203 1.00 29.67 ? 423 CYS A N   1 
ATOM   1802 C  CA  . CYS A  1 233 ? 104.920 4.502   38.639 1.00 28.11 ? 423 CYS A CA  1 
ATOM   1803 C  C   . CYS A  1 233 ? 105.422 5.692   39.436 1.00 29.56 ? 423 CYS A C   1 
ATOM   1804 O  O   . CYS A  1 233 ? 106.468 6.261   39.141 1.00 27.47 ? 423 CYS A O   1 
ATOM   1805 C  CB  . CYS A  1 233 ? 105.809 3.296   38.925 1.00 27.56 ? 423 CYS A CB  1 
ATOM   1806 S  SG  . CYS A  1 233 ? 105.856 2.827   40.684 1.00 32.74 ? 423 CYS A SG  1 
ATOM   1807 N  N   . GLN A  1 234 ? 104.657 6.057   40.458 1.00 34.21 ? 424 GLN A N   1 
ATOM   1808 C  CA  . GLN A  1 234 ? 105.001 7.171   41.330 1.00 36.12 ? 424 GLN A CA  1 
ATOM   1809 C  C   . GLN A  1 234 ? 105.084 6.655   42.761 1.00 34.59 ? 424 GLN A C   1 
ATOM   1810 O  O   . GLN A  1 234 ? 105.103 7.434   43.711 1.00 39.15 ? 424 GLN A O   1 
ATOM   1811 C  CB  . GLN A  1 234 ? 103.928 8.256   41.241 1.00 41.30 ? 424 GLN A CB  1 
ATOM   1812 C  CG  . GLN A  1 234 ? 103.693 8.785   39.836 1.00 48.08 ? 424 GLN A CG  1 
ATOM   1813 C  CD  . GLN A  1 234 ? 102.495 9.708   39.760 1.00 49.70 ? 424 GLN A CD  1 
ATOM   1814 O  OE1 . GLN A  1 234 ? 102.439 10.729  40.443 1.00 51.93 ? 424 GLN A OE1 1 
ATOM   1815 N  NE2 . GLN A  1 234 ? 101.525 9.350   38.928 1.00 55.76 ? 424 GLN A NE2 1 
ATOM   1816 N  N   . ASN A  1 235 ? 105.128 5.334   42.903 1.00 31.00 ? 425 ASN A N   1 
ATOM   1817 C  CA  . ASN A  1 235 ? 105.197 4.704   44.214 1.00 28.26 ? 425 ASN A CA  1 
ATOM   1818 C  C   . ASN A  1 235 ? 106.618 4.256   44.550 1.00 28.61 ? 425 ASN A C   1 
ATOM   1819 O  O   . ASN A  1 235 ? 107.136 3.300   43.972 1.00 25.23 ? 425 ASN A O   1 
ATOM   1820 C  CB  . ASN A  1 235 ? 104.265 3.496   44.258 1.00 26.21 ? 425 ASN A CB  1 
ATOM   1821 C  CG  . ASN A  1 235 ? 104.031 2.999   45.663 1.00 28.59 ? 425 ASN A CG  1 
ATOM   1822 O  OD1 . ASN A  1 235 ? 104.912 3.091   46.520 1.00 33.27 ? 425 ASN A OD1 1 
ATOM   1823 N  ND2 . ASN A  1 235 ? 102.844 2.456   45.910 1.00 27.23 ? 425 ASN A ND2 1 
ATOM   1824 N  N   . GLU A  1 236 ? 107.241 4.949   45.496 1.00 30.57 ? 426 GLU A N   1 
ATOM   1825 C  CA  . GLU A  1 236 ? 108.599 4.635   45.920 1.00 29.86 ? 426 GLU A CA  1 
ATOM   1826 C  C   . GLU A  1 236 ? 108.668 3.255   46.572 1.00 29.35 ? 426 GLU A C   1 
ATOM   1827 O  O   . GLU A  1 236 ? 109.734 2.639   46.649 1.00 24.65 ? 426 GLU A O   1 
ATOM   1828 C  CB  . GLU A  1 236 ? 109.088 5.688   46.917 1.00 36.19 ? 426 GLU A CB  1 
ATOM   1829 C  CG  . GLU A  1 236 ? 108.993 7.122   46.418 1.00 52.68 ? 426 GLU A CG  1 
ATOM   1830 C  CD  . GLU A  1 236 ? 109.774 7.349   45.137 1.00 60.84 ? 426 GLU A CD  1 
ATOM   1831 O  OE1 . GLU A  1 236 ? 110.975 7.009   45.108 1.00 66.28 ? 426 GLU A OE1 1 
ATOM   1832 O  OE2 . GLU A  1 236 ? 109.189 7.870   44.163 1.00 64.30 ? 426 GLU A OE2 1 
ATOM   1833 N  N   . CYS A  1 237 ? 107.521 2.770   47.033 1.00 29.25 ? 427 CYS A N   1 
ATOM   1834 C  CA  . CYS A  1 237 ? 107.450 1.480   47.706 1.00 30.74 ? 427 CYS A CA  1 
ATOM   1835 C  C   . CYS A  1 237 ? 107.313 0.293   46.768 1.00 31.77 ? 427 CYS A C   1 
ATOM   1836 O  O   . CYS A  1 237 ? 107.638 -0.836  47.137 1.00 32.16 ? 427 CYS A O   1 
ATOM   1837 C  CB  . CYS A  1 237 ? 106.263 1.464   48.664 1.00 27.50 ? 427 CYS A CB  1 
ATOM   1838 S  SG  . CYS A  1 237 ? 105.997 3.029   49.544 1.00 28.90 ? 427 CYS A SG  1 
ATOM   1839 N  N   . CYS A  1 238 ? 106.837 0.546   45.556 1.00 33.88 ? 428 CYS A N   1 
ATOM   1840 C  CA  . CYS A  1 238 ? 106.611 -0.533  44.608 1.00 36.54 ? 428 CYS A CA  1 
ATOM   1841 C  C   . CYS A  1 238 ? 107.616 -0.663  43.476 1.00 34.04 ? 428 CYS A C   1 
ATOM   1842 O  O   . CYS A  1 238 ? 108.158 0.324   42.981 1.00 34.13 ? 428 CYS A O   1 
ATOM   1843 C  CB  . CYS A  1 238 ? 105.206 -0.395  44.015 1.00 38.41 ? 428 CYS A CB  1 
ATOM   1844 S  SG  . CYS A  1 238 ? 104.518 -1.918  43.292 1.00 40.30 ? 428 CYS A SG  1 
ATOM   1845 N  N   . ASP A  1 239 ? 107.849 -1.907  43.076 1.00 33.51 ? 429 ASP A N   1 
ATOM   1846 C  CA  . ASP A  1 239 ? 108.742 -2.218  41.974 1.00 31.09 ? 429 ASP A CA  1 
ATOM   1847 C  C   . ASP A  1 239 ? 107.827 -2.505  40.786 1.00 29.70 ? 429 ASP A C   1 
ATOM   1848 O  O   . ASP A  1 239 ? 107.564 -3.660  40.451 1.00 30.74 ? 429 ASP A O   1 
ATOM   1849 C  CB  . ASP A  1 239 ? 109.578 -3.455  42.291 1.00 31.80 ? 429 ASP A CB  1 
ATOM   1850 C  CG  . ASP A  1 239 ? 110.515 -3.816  41.166 1.00 30.22 ? 429 ASP A CG  1 
ATOM   1851 O  OD1 . ASP A  1 239 ? 111.433 -3.020  40.886 1.00 33.49 ? 429 ASP A OD1 1 
ATOM   1852 O  OD2 . ASP A  1 239 ? 110.328 -4.889  40.556 1.00 30.10 ? 429 ASP A OD2 1 
ATOM   1853 N  N   . ALA A  1 240 ? 107.332 -1.434  40.177 1.00 25.89 ? 430 ALA A N   1 
ATOM   1854 C  CA  . ALA A  1 240 ? 106.423 -1.501  39.039 1.00 24.79 ? 430 ALA A CA  1 
ATOM   1855 C  C   . ALA A  1 240 ? 106.518 -2.766  38.190 1.00 25.02 ? 430 ALA A C   1 
ATOM   1856 O  O   . ALA A  1 240 ? 105.528 -3.470  37.987 1.00 25.78 ? 430 ALA A O   1 
ATOM   1857 C  CB  . ALA A  1 240 ? 106.630 -0.274  38.156 1.00 24.33 ? 430 ALA A CB  1 
ATOM   1858 N  N   . ALA A  1 241 ? 107.715 -3.049  37.694 1.00 24.04 ? 431 ALA A N   1 
ATOM   1859 C  CA  . ALA A  1 241 ? 107.939 -4.203  36.839 1.00 21.80 ? 431 ALA A CA  1 
ATOM   1860 C  C   . ALA A  1 241 ? 107.475 -5.545  37.390 1.00 24.20 ? 431 ALA A C   1 
ATOM   1861 O  O   . ALA A  1 241 ? 107.074 -6.418  36.625 1.00 28.93 ? 431 ALA A O   1 
ATOM   1862 C  CB  . ALA A  1 241 ? 109.413 -4.284  36.473 1.00 22.67 ? 431 ALA A CB  1 
ATOM   1863 N  N   . THR A  1 242 ? 107.511 -5.716  38.708 1.00 27.96 ? 432 THR A N   1 
ATOM   1864 C  CA  . THR A  1 242 ? 107.131 -6.996  39.303 1.00 23.49 ? 432 THR A CA  1 
ATOM   1865 C  C   . THR A  1 242 ? 105.952 -6.980  40.273 1.00 23.80 ? 432 THR A C   1 
ATOM   1866 O  O   . THR A  1 242 ? 105.472 -8.039  40.674 1.00 24.38 ? 432 THR A O   1 
ATOM   1867 C  CB  . THR A  1 242 ? 108.330 -7.623  40.044 1.00 24.10 ? 432 THR A CB  1 
ATOM   1868 O  OG1 . THR A  1 242 ? 108.616 -6.860  41.222 1.00 26.73 ? 432 THR A OG1 1 
ATOM   1869 C  CG2 . THR A  1 242 ? 109.565 -7.626  39.155 1.00 17.97 ? 432 THR A CG2 1 
ATOM   1870 N  N   . CYS A  1 243 ? 105.487 -5.793  40.649 1.00 22.56 ? 433 CYS A N   1 
ATOM   1871 C  CA  . CYS A  1 243 ? 104.381 -5.673  41.598 1.00 26.59 ? 433 CYS A CA  1 
ATOM   1872 C  C   . CYS A  1 243 ? 104.770 -6.215  42.971 1.00 28.94 ? 433 CYS A C   1 
ATOM   1873 O  O   . CYS A  1 243 ? 103.939 -6.731  43.718 1.00 31.16 ? 433 CYS A O   1 
ATOM   1874 C  CB  . CYS A  1 243 ? 103.130 -6.387  41.065 1.00 21.34 ? 433 CYS A CB  1 
ATOM   1875 S  SG  . CYS A  1 243 ? 102.313 -5.372  39.800 1.00 28.80 ? 433 CYS A SG  1 
ATOM   1876 N  N   . LYS A  1 244 ? 106.054 -6.088  43.287 1.00 30.42 ? 434 LYS A N   1 
ATOM   1877 C  CA  . LYS A  1 244 ? 106.599 -6.528  44.561 1.00 28.83 ? 434 LYS A CA  1 
ATOM   1878 C  C   . LYS A  1 244 ? 107.079 -5.280  45.286 1.00 29.23 ? 434 LYS A C   1 
ATOM   1879 O  O   . LYS A  1 244 ? 107.631 -4.377  44.660 1.00 32.58 ? 434 LYS A O   1 
ATOM   1880 C  CB  . LYS A  1 244 ? 107.778 -7.475  44.333 1.00 28.44 ? 434 LYS A CB  1 
ATOM   1881 C  CG  . LYS A  1 244 ? 107.406 -8.793  43.680 1.00 35.70 ? 434 LYS A CG  1 
ATOM   1882 C  CD  . LYS A  1 244 ? 106.462 -9.594  44.566 1.00 41.63 ? 434 LYS A CD  1 
ATOM   1883 C  CE  . LYS A  1 244 ? 106.066 -10.915 43.920 1.00 44.58 ? 434 LYS A CE  1 
ATOM   1884 N  NZ  . LYS A  1 244 ? 105.154 -11.709 44.793 1.00 45.70 ? 434 LYS A NZ  1 
ATOM   1885 N  N   . LEU A  1 245 ? 106.860 -5.216  46.596 1.00 27.20 ? 435 LEU A N   1 
ATOM   1886 C  CA  . LEU A  1 245 ? 107.298 -4.057  47.366 1.00 21.03 ? 435 LEU A CA  1 
ATOM   1887 C  C   . LEU A  1 245 ? 108.816 -4.059  47.444 1.00 20.57 ? 435 LEU A C   1 
ATOM   1888 O  O   . LEU A  1 245 ? 109.444 -5.120  47.389 1.00 21.60 ? 435 LEU A O   1 
ATOM   1889 C  CB  . LEU A  1 245 ? 106.715 -4.090  48.784 1.00 14.98 ? 435 LEU A CB  1 
ATOM   1890 C  CG  . LEU A  1 245 ? 105.195 -3.960  48.945 1.00 17.43 ? 435 LEU A CG  1 
ATOM   1891 C  CD1 . LEU A  1 245 ? 104.830 -4.014  50.425 1.00 14.56 ? 435 LEU A CD1 1 
ATOM   1892 C  CD2 . LEU A  1 245 ? 104.721 -2.651  48.335 1.00 14.40 ? 435 LEU A CD2 1 
ATOM   1893 N  N   . LYS A  1 246 ? 109.406 -2.872  47.555 1.00 19.76 ? 436 LYS A N   1 
ATOM   1894 C  CA  . LYS A  1 246 ? 110.854 -2.758  47.662 1.00 20.97 ? 436 LYS A CA  1 
ATOM   1895 C  C   . LYS A  1 246 ? 111.254 -3.462  48.949 1.00 23.57 ? 436 LYS A C   1 
ATOM   1896 O  O   . LYS A  1 246 ? 110.477 -3.499  49.903 1.00 22.00 ? 436 LYS A O   1 
ATOM   1897 C  CB  . LYS A  1 246 ? 111.278 -1.294  47.764 1.00 19.40 ? 436 LYS A CB  1 
ATOM   1898 C  CG  . LYS A  1 246 ? 110.903 -0.426  46.589 1.00 18.00 ? 436 LYS A CG  1 
ATOM   1899 C  CD  . LYS A  1 246 ? 111.708 -0.765  45.358 1.00 17.87 ? 436 LYS A CD  1 
ATOM   1900 C  CE  . LYS A  1 246 ? 111.487 0.287   44.275 1.00 28.40 ? 436 LYS A CE  1 
ATOM   1901 N  NZ  . LYS A  1 246 ? 111.778 1.668   44.771 1.00 18.30 ? 436 LYS A NZ  1 
ATOM   1902 N  N   . SER A  1 247 ? 112.458 -4.022  48.982 1.00 25.21 ? 437 SER A N   1 
ATOM   1903 C  CA  . SER A  1 247 ? 112.925 -4.692  50.187 1.00 27.72 ? 437 SER A CA  1 
ATOM   1904 C  C   . SER A  1 247 ? 112.917 -3.664  51.316 1.00 29.07 ? 437 SER A C   1 
ATOM   1905 O  O   . SER A  1 247 ? 113.354 -2.525  51.133 1.00 27.36 ? 437 SER A O   1 
ATOM   1906 C  CB  . SER A  1 247 ? 114.347 -5.232  49.988 1.00 31.30 ? 437 SER A CB  1 
ATOM   1907 O  OG  . SER A  1 247 ? 114.389 -6.230  48.981 1.00 36.03 ? 437 SER A OG  1 
ATOM   1908 N  N   . GLY A  1 248 ? 112.398 -4.059  52.472 1.00 29.29 ? 438 GLY A N   1 
ATOM   1909 C  CA  . GLY A  1 248 ? 112.356 -3.148  53.600 1.00 27.95 ? 438 GLY A CA  1 
ATOM   1910 C  C   . GLY A  1 248 ? 111.018 -2.464  53.794 1.00 25.54 ? 438 GLY A C   1 
ATOM   1911 O  O   . GLY A  1 248 ? 110.725 -1.964  54.881 1.00 24.17 ? 438 GLY A O   1 
ATOM   1912 N  N   . SER A  1 249 ? 110.202 -2.433  52.747 1.00 25.21 ? 439 SER A N   1 
ATOM   1913 C  CA  . SER A  1 249 ? 108.890 -1.801  52.835 1.00 25.91 ? 439 SER A CA  1 
ATOM   1914 C  C   . SER A  1 249 ? 107.904 -2.705  53.563 1.00 22.36 ? 439 SER A C   1 
ATOM   1915 O  O   . SER A  1 249 ? 107.948 -3.925  53.424 1.00 22.67 ? 439 SER A O   1 
ATOM   1916 C  CB  . SER A  1 249 ? 108.358 -1.484  51.438 1.00 26.08 ? 439 SER A CB  1 
ATOM   1917 O  OG  . SER A  1 249 ? 109.217 -0.581  50.763 1.00 39.96 ? 439 SER A OG  1 
ATOM   1918 N  N   . GLN A  1 250 ? 107.021 -2.104  54.350 1.00 19.43 ? 440 GLN A N   1 
ATOM   1919 C  CA  . GLN A  1 250 ? 106.026 -2.877  55.079 1.00 21.24 ? 440 GLN A CA  1 
ATOM   1920 C  C   . GLN A  1 250 ? 104.726 -2.872  54.287 1.00 20.47 ? 440 GLN A C   1 
ATOM   1921 O  O   . GLN A  1 250 ? 103.992 -3.860  54.262 1.00 19.15 ? 440 GLN A O   1 
ATOM   1922 C  CB  . GLN A  1 250 ? 105.783 -2.272  56.466 1.00 21.36 ? 440 GLN A CB  1 
ATOM   1923 C  CG  . GLN A  1 250 ? 106.987 -2.302  57.396 1.00 15.98 ? 440 GLN A CG  1 
ATOM   1924 C  CD  . GLN A  1 250 ? 106.687 -1.671  58.741 1.00 18.08 ? 440 GLN A CD  1 
ATOM   1925 O  OE1 . GLN A  1 250 ? 106.352 -0.490  58.823 1.00 17.54 ? 440 GLN A OE1 1 
ATOM   1926 N  NE2 . GLN A  1 250 ? 106.800 -2.457  59.805 1.00 16.43 ? 440 GLN A NE2 1 
ATOM   1927 N  N   . CYS A  1 251 ? 104.461 -1.749  53.632 1.00 18.72 ? 441 CYS A N   1 
ATOM   1928 C  CA  . CYS A  1 251 ? 103.256 -1.572  52.837 1.00 20.99 ? 441 CYS A CA  1 
ATOM   1929 C  C   . CYS A  1 251 ? 103.564 -0.720  51.608 1.00 24.26 ? 441 CYS A C   1 
ATOM   1930 O  O   . CYS A  1 251 ? 104.671 -0.195  51.463 1.00 24.92 ? 441 CYS A O   1 
ATOM   1931 C  CB  . CYS A  1 251 ? 102.180 -0.885  53.680 1.00 21.71 ? 441 CYS A CB  1 
ATOM   1932 S  SG  . CYS A  1 251 ? 102.743 0.683   54.422 1.00 28.16 ? 441 CYS A SG  1 
ATOM   1933 N  N   . GLY A  1 252 ? 102.575 -0.584  50.730 1.00 24.15 ? 442 GLY A N   1 
ATOM   1934 C  CA  . GLY A  1 252 ? 102.755 0.211   49.530 1.00 21.72 ? 442 GLY A CA  1 
ATOM   1935 C  C   . GLY A  1 252 ? 101.476 0.926   49.151 1.00 19.81 ? 442 GLY A C   1 
ATOM   1936 O  O   . GLY A  1 252 ? 101.392 1.562   48.103 1.00 17.71 ? 442 GLY A O   1 
ATOM   1937 N  N   . HIS A  1 253 ? 100.473 0.819   50.015 1.00 22.94 ? 443 HIS A N   1 
ATOM   1938 C  CA  . HIS A  1 253 ? 99.181  1.451   49.778 1.00 27.24 ? 443 HIS A CA  1 
ATOM   1939 C  C   . HIS A  1 253 ? 98.349  1.366   51.054 1.00 25.21 ? 443 HIS A C   1 
ATOM   1940 O  O   . HIS A  1 253 ? 98.664  0.586   51.954 1.00 26.86 ? 443 HIS A O   1 
ATOM   1941 C  CB  . HIS A  1 253 ? 98.438  0.728   48.656 1.00 34.20 ? 443 HIS A CB  1 
ATOM   1942 C  CG  . HIS A  1 253 ? 97.662  -0.459  49.127 1.00 38.58 ? 443 HIS A CG  1 
ATOM   1943 N  ND1 . HIS A  1 253 ? 98.253  -1.522  49.776 1.00 43.19 ? 443 HIS A ND1 1 
ATOM   1944 C  CD2 . HIS A  1 253 ? 96.336  -0.728  49.094 1.00 43.89 ? 443 HIS A CD2 1 
ATOM   1945 C  CE1 . HIS A  1 253 ? 97.324  -2.393  50.126 1.00 49.32 ? 443 HIS A CE1 1 
ATOM   1946 N  NE2 . HIS A  1 253 ? 96.151  -1.935  49.725 1.00 50.98 ? 443 HIS A NE2 1 
ATOM   1947 N  N   . GLY A  1 254 ? 97.283  2.158   51.124 1.00 21.45 ? 444 GLY A N   1 
ATOM   1948 C  CA  . GLY A  1 254 ? 96.428  2.133   52.298 1.00 18.07 ? 444 GLY A CA  1 
ATOM   1949 C  C   . GLY A  1 254 ? 96.470  3.409   53.114 1.00 17.31 ? 444 GLY A C   1 
ATOM   1950 O  O   . GLY A  1 254 ? 97.505  4.063   53.216 1.00 18.58 ? 444 GLY A O   1 
ATOM   1951 N  N   . ASP A  1 255 ? 95.336  3.760   53.705 1.00 17.45 ? 445 ASP A N   1 
ATOM   1952 C  CA  . ASP A  1 255 ? 95.235  4.963   54.516 1.00 21.87 ? 445 ASP A CA  1 
ATOM   1953 C  C   . ASP A  1 255 ? 96.200  4.935   55.689 1.00 23.69 ? 445 ASP A C   1 
ATOM   1954 O  O   . ASP A  1 255 ? 96.495  5.972   56.285 1.00 26.22 ? 445 ASP A O   1 
ATOM   1955 C  CB  . ASP A  1 255 ? 93.804  5.120   55.023 1.00 24.68 ? 445 ASP A CB  1 
ATOM   1956 C  CG  . ASP A  1 255 ? 92.823  5.418   53.905 1.00 28.76 ? 445 ASP A CG  1 
ATOM   1957 O  OD1 . ASP A  1 255 ? 91.618  5.142   54.080 1.00 30.87 ? 445 ASP A OD1 1 
ATOM   1958 O  OD2 . ASP A  1 255 ? 93.259  5.939   52.856 1.00 32.29 ? 445 ASP A OD2 1 
ATOM   1959 N  N   . CYS A  1 256 ? 96.688  3.744   56.020 1.00 22.81 ? 446 CYS A N   1 
ATOM   1960 C  CA  . CYS A  1 256 ? 97.622  3.594   57.126 1.00 25.76 ? 446 CYS A CA  1 
ATOM   1961 C  C   . CYS A  1 256 ? 99.021  3.225   56.655 1.00 29.78 ? 446 CYS A C   1 
ATOM   1962 O  O   . CYS A  1 256 ? 99.753  2.516   57.347 1.00 29.87 ? 446 CYS A O   1 
ATOM   1963 C  CB  . CYS A  1 256 ? 97.117  2.545   58.116 1.00 24.30 ? 446 CYS A CB  1 
ATOM   1964 S  SG  . CYS A  1 256 ? 95.658  3.076   59.064 1.00 23.62 ? 446 CYS A SG  1 
ATOM   1965 N  N   . CYS A  1 257 ? 99.384  3.705   55.470 1.00 30.97 ? 447 CYS A N   1 
ATOM   1966 C  CA  . CYS A  1 257 ? 100.705 3.451   54.918 1.00 29.99 ? 447 CYS A CA  1 
ATOM   1967 C  C   . CYS A  1 257 ? 101.386 4.789   54.662 1.00 29.51 ? 447 CYS A C   1 
ATOM   1968 O  O   . CYS A  1 257 ? 100.994 5.534   53.768 1.00 29.67 ? 447 CYS A O   1 
ATOM   1969 C  CB  . CYS A  1 257 ? 100.612 2.661   53.613 1.00 28.47 ? 447 CYS A CB  1 
ATOM   1970 S  SG  . CYS A  1 257 ? 102.247 2.098   53.046 1.00 27.50 ? 447 CYS A SG  1 
ATOM   1971 N  N   . GLU A  1 258 ? 102.400 5.095   55.461 1.00 30.32 ? 448 GLU A N   1 
ATOM   1972 C  CA  . GLU A  1 258 ? 103.120 6.351   55.324 1.00 32.03 ? 448 GLU A CA  1 
ATOM   1973 C  C   . GLU A  1 258 ? 104.562 6.106   54.913 1.00 33.99 ? 448 GLU A C   1 
ATOM   1974 O  O   . GLU A  1 258 ? 105.341 5.492   55.647 1.00 28.94 ? 448 GLU A O   1 
ATOM   1975 C  CB  . GLU A  1 258 ? 103.059 7.125   56.641 1.00 35.36 ? 448 GLU A CB  1 
ATOM   1976 C  CG  . GLU A  1 258 ? 101.644 7.537   57.020 1.00 47.81 ? 448 GLU A CG  1 
ATOM   1977 C  CD  . GLU A  1 258 ? 101.492 7.896   58.489 1.00 56.09 ? 448 GLU A CD  1 
ATOM   1978 O  OE1 . GLU A  1 258 ? 100.371 8.281   58.886 1.00 57.77 ? 448 GLU A OE1 1 
ATOM   1979 O  OE2 . GLU A  1 258 ? 102.482 7.789   59.246 1.00 58.75 ? 448 GLU A OE2 1 
ATOM   1980 N  N   . GLN A  1 259 ? 104.904 6.589   53.724 1.00 33.81 ? 449 GLN A N   1 
ATOM   1981 C  CA  . GLN A  1 259 ? 106.243 6.430   53.187 1.00 33.10 ? 449 GLN A CA  1 
ATOM   1982 C  C   . GLN A  1 259 ? 106.711 4.985   53.287 1.00 31.12 ? 449 GLN A C   1 
ATOM   1983 O  O   . GLN A  1 259 ? 107.749 4.694   53.878 1.00 32.35 ? 449 GLN A O   1 
ATOM   1984 C  CB  . GLN A  1 259 ? 107.212 7.361   53.916 1.00 37.51 ? 449 GLN A CB  1 
ATOM   1985 C  CG  . GLN A  1 259 ? 106.956 8.836   53.630 1.00 43.69 ? 449 GLN A CG  1 
ATOM   1986 C  CD  . GLN A  1 259 ? 107.857 9.756   54.430 1.00 52.27 ? 449 GLN A CD  1 
ATOM   1987 O  OE1 . GLN A  1 259 ? 109.085 9.657   54.364 1.00 57.05 ? 449 GLN A OE1 1 
ATOM   1988 N  NE2 . GLN A  1 259 ? 107.250 10.661  55.191 1.00 56.94 ? 449 GLN A NE2 1 
ATOM   1989 N  N   . CYS A  1 260 ? 105.916 4.085   52.715 1.00 28.23 ? 450 CYS A N   1 
ATOM   1990 C  CA  . CYS A  1 260 ? 106.229 2.661   52.687 1.00 22.20 ? 450 CYS A CA  1 
ATOM   1991 C  C   . CYS A  1 260 ? 106.199 1.951   54.033 1.00 18.73 ? 450 CYS A C   1 
ATOM   1992 O  O   . CYS A  1 260 ? 106.619 0.797   54.134 1.00 15.98 ? 450 CYS A O   1 
ATOM   1993 C  CB  . CYS A  1 260 ? 107.595 2.457   52.043 1.00 19.30 ? 450 CYS A CB  1 
ATOM   1994 S  SG  . CYS A  1 260 ? 107.774 3.354   50.472 1.00 21.47 ? 450 CYS A SG  1 
ATOM   1995 N  N   . LYS A  1 261 ? 105.699 2.627   55.063 1.00 18.72 ? 451 LYS A N   1 
ATOM   1996 C  CA  . LYS A  1 261 ? 105.641 2.026   56.391 1.00 17.18 ? 451 LYS A CA  1 
ATOM   1997 C  C   . LYS A  1 261 ? 104.259 2.117   57.013 1.00 13.56 ? 451 LYS A C   1 
ATOM   1998 O  O   . LYS A  1 261 ? 103.406 2.876   56.558 1.00 16.61 ? 451 LYS A O   1 
ATOM   1999 C  CB  . LYS A  1 261 ? 106.653 2.701   57.324 1.00 18.62 ? 451 LYS A CB  1 
ATOM   2000 C  CG  . LYS A  1 261 ? 108.081 2.714   56.794 1.00 23.44 ? 451 LYS A CG  1 
ATOM   2001 C  CD  . LYS A  1 261 ? 108.566 1.303   56.484 1.00 28.26 ? 451 LYS A CD  1 
ATOM   2002 C  CE  . LYS A  1 261 ? 109.969 1.310   55.901 1.00 24.42 ? 451 LYS A CE  1 
ATOM   2003 N  NZ  . LYS A  1 261 ? 110.946 1.880   56.861 1.00 34.64 ? 451 LYS A NZ  1 
ATOM   2004 N  N   . PHE A  1 262 ? 104.048 1.327   58.059 1.00 13.14 ? 452 PHE A N   1 
ATOM   2005 C  CA  . PHE A  1 262 ? 102.785 1.321   58.782 1.00 7.63  ? 452 PHE A CA  1 
ATOM   2006 C  C   . PHE A  1 262 ? 102.719 2.590   59.612 1.00 8.58  ? 452 PHE A C   1 
ATOM   2007 O  O   . PHE A  1 262 ? 103.683 2.939   60.291 1.00 11.77 ? 452 PHE A O   1 
ATOM   2008 C  CB  . PHE A  1 262 ? 102.713 0.115   59.720 1.00 6.78  ? 452 PHE A CB  1 
ATOM   2009 C  CG  . PHE A  1 262 ? 102.607 -1.204  59.013 1.00 10.61 ? 452 PHE A CG  1 
ATOM   2010 C  CD1 . PHE A  1 262 ? 103.117 -2.360  59.599 1.00 12.74 ? 452 PHE A CD1 1 
ATOM   2011 C  CD2 . PHE A  1 262 ? 101.975 -1.302  57.775 1.00 11.48 ? 452 PHE A CD2 1 
ATOM   2012 C  CE1 . PHE A  1 262 ? 103.000 -3.599  58.964 1.00 12.67 ? 452 PHE A CE1 1 
ATOM   2013 C  CE2 . PHE A  1 262 ? 101.850 -2.533  57.132 1.00 12.56 ? 452 PHE A CE2 1 
ATOM   2014 C  CZ  . PHE A  1 262 ? 102.365 -3.686  57.729 1.00 13.23 ? 452 PHE A CZ  1 
ATOM   2015 N  N   . SER A  1 263 ? 101.592 3.288   59.557 1.00 9.94  ? 453 SER A N   1 
ATOM   2016 C  CA  . SER A  1 263 ? 101.441 4.503   60.340 1.00 15.25 ? 453 SER A CA  1 
ATOM   2017 C  C   . SER A  1 263 ? 101.545 4.148   61.822 1.00 16.57 ? 453 SER A C   1 
ATOM   2018 O  O   . SER A  1 263 ? 101.271 3.014   62.220 1.00 16.55 ? 453 SER A O   1 
ATOM   2019 C  CB  . SER A  1 263 ? 100.090 5.147   60.048 1.00 15.87 ? 453 SER A CB  1 
ATOM   2020 O  OG  . SER A  1 263 ? 99.984  5.466   58.673 1.00 25.16 ? 453 SER A OG  1 
ATOM   2021 N  N   . LYS A  1 264 ? 101.948 5.114   62.638 1.00 18.96 ? 454 LYS A N   1 
ATOM   2022 C  CA  . LYS A  1 264 ? 102.085 4.874   64.066 1.00 23.43 ? 454 LYS A CA  1 
ATOM   2023 C  C   . LYS A  1 264 ? 100.740 4.521   64.687 1.00 24.74 ? 454 LYS A C   1 
ATOM   2024 O  O   . LYS A  1 264 ? 99.727  5.166   64.409 1.00 22.62 ? 454 LYS A O   1 
ATOM   2025 C  CB  . LYS A  1 264 ? 102.671 6.108   64.756 1.00 28.35 ? 454 LYS A CB  1 
ATOM   2026 C  CG  . LYS A  1 264 ? 104.077 6.450   64.291 1.00 44.84 ? 454 LYS A CG  1 
ATOM   2027 C  CD  . LYS A  1 264 ? 104.653 7.653   65.025 1.00 49.61 ? 454 LYS A CD  1 
ATOM   2028 C  CE  . LYS A  1 264 ? 106.096 7.904   64.596 1.00 50.40 ? 454 LYS A CE  1 
ATOM   2029 N  NZ  . LYS A  1 264 ? 106.722 9.040   65.328 1.00 52.66 ? 454 LYS A NZ  1 
ATOM   2030 N  N   . SER A  1 265 ? 100.740 3.484   65.520 1.00 24.07 ? 455 SER A N   1 
ATOM   2031 C  CA  . SER A  1 265 ? 99.532  3.037   66.203 1.00 20.77 ? 455 SER A CA  1 
ATOM   2032 C  C   . SER A  1 265 ? 98.805  4.240   66.786 1.00 21.47 ? 455 SER A C   1 
ATOM   2033 O  O   . SER A  1 265 ? 99.407  5.057   67.482 1.00 23.18 ? 455 SER A O   1 
ATOM   2034 C  CB  . SER A  1 265 ? 99.894  2.069   67.329 1.00 20.71 ? 455 SER A CB  1 
ATOM   2035 O  OG  . SER A  1 265 ? 98.761  1.735   68.110 1.00 22.34 ? 455 SER A OG  1 
ATOM   2036 N  N   . GLY A  1 266 ? 97.516  4.357   66.488 1.00 19.65 ? 456 GLY A N   1 
ATOM   2037 C  CA  . GLY A  1 266 ? 96.754  5.473   67.009 1.00 19.05 ? 456 GLY A CA  1 
ATOM   2038 C  C   . GLY A  1 266 ? 96.599  6.659   66.071 1.00 23.78 ? 456 GLY A C   1 
ATOM   2039 O  O   . GLY A  1 266 ? 95.899  7.613   66.412 1.00 27.21 ? 456 GLY A O   1 
ATOM   2040 N  N   . THR A  1 267 ? 97.239  6.632   64.905 1.00 22.17 ? 457 THR A N   1 
ATOM   2041 C  CA  . THR A  1 267 ? 97.088  7.754   63.981 1.00 28.93 ? 457 THR A CA  1 
ATOM   2042 C  C   . THR A  1 267 ? 95.726  7.660   63.300 1.00 31.56 ? 457 THR A C   1 
ATOM   2043 O  O   . THR A  1 267 ? 95.357  6.620   62.744 1.00 30.60 ? 457 THR A O   1 
ATOM   2044 C  CB  . THR A  1 267 ? 98.204  7.796   62.897 1.00 26.48 ? 457 THR A CB  1 
ATOM   2045 O  OG1 . THR A  1 267 ? 98.171  6.600   62.114 1.00 31.56 ? 457 THR A OG1 1 
ATOM   2046 C  CG2 . THR A  1 267 ? 99.573  7.944   63.546 1.00 28.52 ? 457 THR A CG2 1 
ATOM   2047 N  N   . GLU A  1 268 ? 94.979  8.756   63.364 1.00 30.39 ? 458 GLU A N   1 
ATOM   2048 C  CA  . GLU A  1 268 ? 93.647  8.828   62.782 1.00 27.55 ? 458 GLU A CA  1 
ATOM   2049 C  C   . GLU A  1 268 ? 93.654  8.573   61.281 1.00 25.05 ? 458 GLU A C   1 
ATOM   2050 O  O   . GLU A  1 268 ? 94.348  9.260   60.532 1.00 22.35 ? 458 GLU A O   1 
ATOM   2051 C  CB  . GLU A  1 268 ? 93.038  10.201  63.082 1.00 25.90 ? 458 GLU A CB  1 
ATOM   2052 C  CG  . GLU A  1 268 ? 91.653  10.422  62.509 1.00 31.04 ? 458 GLU A CG  1 
ATOM   2053 C  CD  . GLU A  1 268 ? 90.999  11.674  63.061 1.00 32.23 ? 458 GLU A CD  1 
ATOM   2054 O  OE1 . GLU A  1 268 ? 90.741  11.715  64.284 1.00 34.43 ? 458 GLU A OE1 1 
ATOM   2055 O  OE2 . GLU A  1 268 ? 90.748  12.614  62.278 1.00 28.42 ? 458 GLU A OE2 1 
ATOM   2056 N  N   . CYS A  1 269 ? 92.882  7.581   60.844 1.00 24.65 ? 459 CYS A N   1 
ATOM   2057 C  CA  . CYS A  1 269 ? 92.809  7.264   59.425 1.00 20.99 ? 459 CYS A CA  1 
ATOM   2058 C  C   . CYS A  1 269 ? 91.432  7.509   58.809 1.00 24.51 ? 459 CYS A C   1 
ATOM   2059 O  O   . CYS A  1 269 ? 91.288  7.528   57.584 1.00 27.39 ? 459 CYS A O   1 
ATOM   2060 C  CB  . CYS A  1 269 ? 93.276  5.831   59.169 1.00 17.73 ? 459 CYS A CB  1 
ATOM   2061 S  SG  . CYS A  1 269 ? 92.512  4.496   60.139 1.00 25.46 ? 459 CYS A SG  1 
ATOM   2062 N  N   . ARG A  1 270 ? 90.420  7.683   59.653 1.00 21.26 ? 460 ARG A N   1 
ATOM   2063 C  CA  . ARG A  1 270 ? 89.081  7.998   59.169 1.00 18.98 ? 460 ARG A CA  1 
ATOM   2064 C  C   . ARG A  1 270 ? 88.455  8.970   60.159 1.00 20.27 ? 460 ARG A C   1 
ATOM   2065 O  O   . ARG A  1 270 ? 88.018  8.582   61.244 1.00 15.20 ? 460 ARG A O   1 
ATOM   2066 C  CB  . ARG A  1 270 ? 88.200  6.753   59.023 1.00 20.33 ? 460 ARG A CB  1 
ATOM   2067 C  CG  . ARG A  1 270 ? 86.895  7.067   58.277 1.00 19.68 ? 460 ARG A CG  1 
ATOM   2068 C  CD  . ARG A  1 270 ? 85.929  5.886   58.167 1.00 23.15 ? 460 ARG A CD  1 
ATOM   2069 N  NE  . ARG A  1 270 ? 86.480  4.763   57.410 1.00 19.51 ? 460 ARG A NE  1 
ATOM   2070 C  CZ  . ARG A  1 270 ? 87.163  3.761   57.952 1.00 21.49 ? 460 ARG A CZ  1 
ATOM   2071 N  NH1 . ARG A  1 270 ? 87.376  3.739   59.260 1.00 27.38 ? 460 ARG A NH1 1 
ATOM   2072 N  NH2 . ARG A  1 270 ? 87.637  2.784   57.189 1.00 13.11 ? 460 ARG A NH2 1 
ATOM   2073 N  N   . ALA A  1 271 ? 88.433  10.241  59.773 1.00 19.65 ? 461 ALA A N   1 
ATOM   2074 C  CA  . ALA A  1 271 ? 87.893  11.308  60.601 1.00 21.71 ? 461 ALA A CA  1 
ATOM   2075 C  C   . ALA A  1 271 ? 86.457  11.078  61.064 1.00 25.76 ? 461 ALA A C   1 
ATOM   2076 O  O   . ALA A  1 271 ? 85.700  10.329  60.448 1.00 26.31 ? 461 ALA A O   1 
ATOM   2077 C  CB  . ALA A  1 271 ? 87.989  12.626  59.853 1.00 19.59 ? 461 ALA A CB  1 
ATOM   2078 N  N   . SER A  1 272 ? 86.099  11.745  62.158 1.00 27.22 ? 462 SER A N   1 
ATOM   2079 C  CA  . SER A  1 272 ? 84.768  11.653  62.748 1.00 29.68 ? 462 SER A CA  1 
ATOM   2080 C  C   . SER A  1 272 ? 83.795  12.673  62.147 1.00 31.87 ? 462 SER A C   1 
ATOM   2081 O  O   . SER A  1 272 ? 84.038  13.883  62.202 1.00 26.91 ? 462 SER A O   1 
ATOM   2082 C  CB  . SER A  1 272 ? 84.869  11.869  64.265 1.00 31.56 ? 462 SER A CB  1 
ATOM   2083 O  OG  . SER A  1 272 ? 83.599  12.094  64.857 1.00 30.01 ? 462 SER A OG  1 
ATOM   2084 N  N   . MET A  1 273 ? 82.697  12.184  61.574 1.00 31.53 ? 463 MET A N   1 
ATOM   2085 C  CA  . MET A  1 273 ? 81.692  13.067  60.988 1.00 34.67 ? 463 MET A CA  1 
ATOM   2086 C  C   . MET A  1 273 ? 81.068  13.922  62.096 1.00 33.45 ? 463 MET A C   1 
ATOM   2087 O  O   . MET A  1 273 ? 80.954  15.141  61.965 1.00 35.14 ? 463 MET A O   1 
ATOM   2088 C  CB  . MET A  1 273 ? 80.596  12.251  60.287 1.00 34.44 ? 463 MET A CB  1 
ATOM   2089 C  CG  . MET A  1 273 ? 81.047  11.491  59.044 1.00 36.56 ? 463 MET A CG  1 
ATOM   2090 S  SD  . MET A  1 273 ? 79.717  10.479  58.308 1.00 44.80 ? 463 MET A SD  1 
ATOM   2091 C  CE  . MET A  1 273 ? 78.937  11.673  57.204 1.00 37.66 ? 463 MET A CE  1 
ATOM   2092 N  N   . SER A  1 274 ? 80.672  13.267  63.183 1.00 30.19 ? 464 SER A N   1 
ATOM   2093 C  CA  . SER A  1 274 ? 80.062  13.933  64.332 1.00 26.28 ? 464 SER A CA  1 
ATOM   2094 C  C   . SER A  1 274 ? 80.272  13.052  65.556 1.00 25.04 ? 464 SER A C   1 
ATOM   2095 O  O   . SER A  1 274 ? 80.919  12.010  65.465 1.00 27.85 ? 464 SER A O   1 
ATOM   2096 C  CB  . SER A  1 274 ? 78.559  14.138  64.105 1.00 28.05 ? 464 SER A CB  1 
ATOM   2097 O  OG  . SER A  1 274 ? 77.862  12.902  64.083 1.00 18.04 ? 464 SER A OG  1 
ATOM   2098 N  N   . GLU A  1 275 ? 79.723  13.463  66.696 1.00 20.00 ? 465 GLU A N   1 
ATOM   2099 C  CA  . GLU A  1 275 ? 79.865  12.684  67.921 1.00 22.15 ? 465 GLU A CA  1 
ATOM   2100 C  C   . GLU A  1 275 ? 79.295  11.278  67.754 1.00 24.04 ? 465 GLU A C   1 
ATOM   2101 O  O   . GLU A  1 275 ? 79.692  10.353  68.456 1.00 32.06 ? 465 GLU A O   1 
ATOM   2102 C  CB  . GLU A  1 275 ? 79.165  13.385  69.084 1.00 22.01 ? 465 GLU A CB  1 
ATOM   2103 C  CG  . GLU A  1 275 ? 77.672  13.549  68.897 1.00 31.73 ? 465 GLU A CG  1 
ATOM   2104 C  CD  . GLU A  1 275 ? 77.041  14.383  69.993 1.00 37.81 ? 465 GLU A CD  1 
ATOM   2105 O  OE1 . GLU A  1 275 ? 76.902  13.881  71.130 1.00 35.52 ? 465 GLU A OE1 1 
ATOM   2106 O  OE2 . GLU A  1 275 ? 76.692  15.551  69.716 1.00 44.11 ? 465 GLU A OE2 1 
ATOM   2107 N  N   . CYS A  1 276 ? 78.364  11.120  66.821 1.00 24.36 ? 466 CYS A N   1 
ATOM   2108 C  CA  . CYS A  1 276 ? 77.750  9.822   66.567 1.00 18.41 ? 466 CYS A CA  1 
ATOM   2109 C  C   . CYS A  1 276 ? 78.640  8.945   65.699 1.00 16.28 ? 466 CYS A C   1 
ATOM   2110 O  O   . CYS A  1 276 ? 78.305  7.790   65.428 1.00 13.67 ? 466 CYS A O   1 
ATOM   2111 C  CB  . CYS A  1 276 ? 76.411  9.995   65.859 1.00 21.26 ? 466 CYS A CB  1 
ATOM   2112 S  SG  . CYS A  1 276 ? 75.102  10.833  66.802 1.00 29.17 ? 466 CYS A SG  1 
ATOM   2113 N  N   . ASP A  1 277 ? 79.766  9.498   65.256 1.00 15.28 ? 467 ASP A N   1 
ATOM   2114 C  CA  . ASP A  1 277 ? 80.701  8.760   64.407 1.00 17.59 ? 467 ASP A CA  1 
ATOM   2115 C  C   . ASP A  1 277 ? 82.109  8.667   64.993 1.00 14.95 ? 467 ASP A C   1 
ATOM   2116 O  O   . ASP A  1 277 ? 82.966  9.499   64.696 1.00 15.84 ? 467 ASP A O   1 
ATOM   2117 C  CB  . ASP A  1 277 ? 80.786  9.416   63.026 1.00 19.07 ? 467 ASP A CB  1 
ATOM   2118 C  CG  . ASP A  1 277 ? 81.763  8.711   62.102 1.00 18.74 ? 467 ASP A CG  1 
ATOM   2119 O  OD1 . ASP A  1 277 ? 82.165  9.317   61.086 1.00 23.85 ? 467 ASP A OD1 1 
ATOM   2120 O  OD2 . ASP A  1 277 ? 82.125  7.549   62.386 1.00 18.09 ? 467 ASP A OD2 1 
ATOM   2121 N  N   . PRO A  1 278 ? 82.372  7.652   65.830 1.00 13.50 ? 468 PRO A N   1 
ATOM   2122 C  CA  . PRO A  1 278 ? 83.717  7.537   66.402 1.00 11.86 ? 468 PRO A CA  1 
ATOM   2123 C  C   . PRO A  1 278 ? 84.748  7.298   65.307 1.00 10.40 ? 468 PRO A C   1 
ATOM   2124 O  O   . PRO A  1 278 ? 84.595  6.403   64.480 1.00 15.37 ? 468 PRO A O   1 
ATOM   2125 C  CB  . PRO A  1 278 ? 83.589  6.347   67.354 1.00 9.61  ? 468 PRO A CB  1 
ATOM   2126 C  CG  . PRO A  1 278 ? 82.540  5.498   66.698 1.00 7.99  ? 468 PRO A CG  1 
ATOM   2127 C  CD  . PRO A  1 278 ? 81.518  6.529   66.257 1.00 14.64 ? 468 PRO A CD  1 
ATOM   2128 N  N   . ALA A  1 279 ? 85.795  8.110   65.293 1.00 9.15  ? 469 ALA A N   1 
ATOM   2129 C  CA  . ALA A  1 279 ? 86.831  7.964   64.287 1.00 10.24 ? 469 ALA A CA  1 
ATOM   2130 C  C   . ALA A  1 279 ? 87.588  6.660   64.485 1.00 13.39 ? 469 ALA A C   1 
ATOM   2131 O  O   . ALA A  1 279 ? 87.553  6.064   65.559 1.00 16.40 ? 469 ALA A O   1 
ATOM   2132 C  CB  . ALA A  1 279 ? 87.795  9.135   64.360 1.00 11.54 ? 469 ALA A CB  1 
ATOM   2133 N  N   . GLU A  1 280 ? 88.257  6.210   63.432 1.00 15.79 ? 470 GLU A N   1 
ATOM   2134 C  CA  . GLU A  1 280 ? 89.053  4.999   63.508 1.00 19.63 ? 470 GLU A CA  1 
ATOM   2135 C  C   . GLU A  1 280 ? 90.521  5.404   63.479 1.00 23.83 ? 470 GLU A C   1 
ATOM   2136 O  O   . GLU A  1 280 ? 90.876  6.451   62.924 1.00 19.84 ? 470 GLU A O   1 
ATOM   2137 C  CB  . GLU A  1 280 ? 88.732  4.061   62.342 1.00 22.03 ? 470 GLU A CB  1 
ATOM   2138 C  CG  . GLU A  1 280 ? 87.383  3.368   62.476 1.00 28.72 ? 470 GLU A CG  1 
ATOM   2139 C  CD  . GLU A  1 280 ? 86.215  4.303   62.242 1.00 32.37 ? 470 GLU A CD  1 
ATOM   2140 O  OE1 . GLU A  1 280 ? 85.116  4.019   62.760 1.00 32.45 ? 470 GLU A OE1 1 
ATOM   2141 O  OE2 . GLU A  1 280 ? 86.391  5.312   61.528 1.00 33.72 ? 470 GLU A OE2 1 
ATOM   2142 N  N   . HIS A  1 281 ? 91.371  4.582   64.084 1.00 23.79 ? 471 HIS A N   1 
ATOM   2143 C  CA  . HIS A  1 281 ? 92.797  4.876   64.136 1.00 24.79 ? 471 HIS A CA  1 
ATOM   2144 C  C   . HIS A  1 281 ? 93.608  3.667   63.678 1.00 25.21 ? 471 HIS A C   1 
ATOM   2145 O  O   . HIS A  1 281 ? 93.169  2.523   63.831 1.00 23.35 ? 471 HIS A O   1 
ATOM   2146 C  CB  . HIS A  1 281 ? 93.176  5.273   65.564 1.00 26.62 ? 471 HIS A CB  1 
ATOM   2147 C  CG  . HIS A  1 281 ? 92.303  6.347   66.138 1.00 32.69 ? 471 HIS A CG  1 
ATOM   2148 N  ND1 . HIS A  1 281 ? 92.346  7.655   65.703 1.00 37.26 ? 471 HIS A ND1 1 
ATOM   2149 C  CD2 . HIS A  1 281 ? 91.337  6.299   67.087 1.00 34.88 ? 471 HIS A CD2 1 
ATOM   2150 C  CE1 . HIS A  1 281 ? 91.445  8.366   66.358 1.00 31.98 ? 471 HIS A CE1 1 
ATOM   2151 N  NE2 . HIS A  1 281 ? 90.819  7.567   67.204 1.00 33.94 ? 471 HIS A NE2 1 
ATOM   2152 N  N   . CYS A  1 282 ? 94.784  3.923   63.107 1.00 21.82 ? 472 CYS A N   1 
ATOM   2153 C  CA  . CYS A  1 282 ? 95.643  2.844   62.629 1.00 18.88 ? 472 CYS A CA  1 
ATOM   2154 C  C   . CYS A  1 282 ? 96.138  2.002   63.800 1.00 17.85 ? 472 CYS A C   1 
ATOM   2155 O  O   . CYS A  1 282 ? 96.305  2.505   64.914 1.00 14.50 ? 472 CYS A O   1 
ATOM   2156 C  CB  . CYS A  1 282 ? 96.837  3.410   61.855 1.00 20.07 ? 472 CYS A CB  1 
ATOM   2157 S  SG  . CYS A  1 282 ? 96.399  4.421   60.398 1.00 27.44 ? 472 CYS A SG  1 
ATOM   2158 N  N   . THR A  1 283 ? 96.367  0.718   63.546 1.00 15.45 ? 473 THR A N   1 
ATOM   2159 C  CA  . THR A  1 283 ? 96.841  -0.190  64.584 1.00 18.73 ? 473 THR A CA  1 
ATOM   2160 C  C   . THR A  1 283 ? 98.362  -0.128  64.727 1.00 21.12 ? 473 THR A C   1 
ATOM   2161 O  O   . THR A  1 283 ? 98.902  -0.291  65.820 1.00 19.68 ? 473 THR A O   1 
ATOM   2162 C  CB  . THR A  1 283 ? 96.449  -1.650  64.274 1.00 18.76 ? 473 THR A CB  1 
ATOM   2163 O  OG1 . THR A  1 283 ? 97.134  -2.092  63.094 1.00 22.73 ? 473 THR A OG1 1 
ATOM   2164 C  CG2 . THR A  1 283 ? 94.956  -1.765  64.052 1.00 11.73 ? 473 THR A CG2 1 
ATOM   2165 N  N   . GLY A  1 284 ? 99.046  0.114   63.615 1.00 20.70 ? 474 GLY A N   1 
ATOM   2166 C  CA  . GLY A  1 284 ? 100.494 0.170   63.639 1.00 21.64 ? 474 GLY A CA  1 
ATOM   2167 C  C   . GLY A  1 284 ? 101.034 -1.147  63.120 1.00 23.19 ? 474 GLY A C   1 
ATOM   2168 O  O   . GLY A  1 284 ? 102.238 -1.319  62.939 1.00 25.39 ? 474 GLY A O   1 
ATOM   2169 N  N   . GLN A  1 285 ? 100.122 -2.079  62.871 1.00 23.67 ? 475 GLN A N   1 
ATOM   2170 C  CA  . GLN A  1 285 ? 100.480 -3.397  62.371 1.00 26.52 ? 475 GLN A CA  1 
ATOM   2171 C  C   . GLN A  1 285 ? 99.984  -3.628  60.950 1.00 23.91 ? 475 GLN A C   1 
ATOM   2172 O  O   . GLN A  1 285 ? 100.378 -4.595  60.301 1.00 24.21 ? 475 GLN A O   1 
ATOM   2173 C  CB  . GLN A  1 285 ? 99.900  -4.474  63.284 1.00 30.52 ? 475 GLN A CB  1 
ATOM   2174 C  CG  . GLN A  1 285 ? 100.549 -4.546  64.645 1.00 39.84 ? 475 GLN A CG  1 
ATOM   2175 C  CD  . GLN A  1 285 ? 99.903  -5.592  65.530 1.00 49.69 ? 475 GLN A CD  1 
ATOM   2176 O  OE1 . GLN A  1 285 ? 98.777  -5.416  66.002 1.00 50.40 ? 475 GLN A OE1 1 
ATOM   2177 N  NE2 . GLN A  1 285 ? 100.609 -6.697  65.750 1.00 52.82 ? 475 GLN A NE2 1 
ATOM   2178 N  N   . SER A  1 286 ? 99.126  -2.740  60.466 1.00 23.03 ? 476 SER A N   1 
ATOM   2179 C  CA  . SER A  1 286 ? 98.579  -2.881  59.124 1.00 23.37 ? 476 SER A CA  1 
ATOM   2180 C  C   . SER A  1 286 ? 98.557  -1.570  58.347 1.00 23.41 ? 476 SER A C   1 
ATOM   2181 O  O   . SER A  1 286 ? 98.707  -0.489  58.916 1.00 24.46 ? 476 SER A O   1 
ATOM   2182 C  CB  . SER A  1 286 ? 97.158  -3.445  59.209 1.00 27.57 ? 476 SER A CB  1 
ATOM   2183 O  OG  . SER A  1 286 ? 96.553  -3.508  57.929 1.00 36.73 ? 476 SER A OG  1 
ATOM   2184 N  N   . SER A  1 287 ? 98.372  -1.673  57.038 1.00 21.15 ? 477 SER A N   1 
ATOM   2185 C  CA  . SER A  1 287 ? 98.311  -0.491  56.196 1.00 24.56 ? 477 SER A CA  1 
ATOM   2186 C  C   . SER A  1 287 ? 96.847  -0.138  55.956 1.00 25.95 ? 477 SER A C   1 
ATOM   2187 O  O   . SER A  1 287 ? 96.532  0.909   55.390 1.00 25.33 ? 477 SER A O   1 
ATOM   2188 C  CB  . SER A  1 287 ? 99.013  -0.755  54.865 1.00 24.31 ? 477 SER A CB  1 
ATOM   2189 O  OG  . SER A  1 287 ? 98.459  -1.883  54.215 1.00 29.68 ? 477 SER A OG  1 
ATOM   2190 N  N   . GLU A  1 288 ? 95.957  -1.021  56.398 1.00 27.84 ? 478 GLU A N   1 
ATOM   2191 C  CA  . GLU A  1 288 ? 94.522  -0.822  56.234 1.00 29.25 ? 478 GLU A CA  1 
ATOM   2192 C  C   . GLU A  1 288 ? 93.895  -0.176  57.455 1.00 28.06 ? 478 GLU A C   1 
ATOM   2193 O  O   . GLU A  1 288 ? 94.251  -0.479  58.592 1.00 32.12 ? 478 GLU A O   1 
ATOM   2194 C  CB  . GLU A  1 288 ? 93.821  -2.155  55.962 1.00 34.11 ? 478 GLU A CB  1 
ATOM   2195 C  CG  . GLU A  1 288 ? 94.138  -2.783  54.617 1.00 45.02 ? 478 GLU A CG  1 
ATOM   2196 C  CD  . GLU A  1 288 ? 93.783  -1.877  53.452 1.00 55.02 ? 478 GLU A CD  1 
ATOM   2197 O  OE1 . GLU A  1 288 ? 94.567  -0.951  53.149 1.00 56.24 ? 478 GLU A OE1 1 
ATOM   2198 O  OE2 . GLU A  1 288 ? 92.712  -2.088  52.843 1.00 62.41 ? 478 GLU A OE2 1 
ATOM   2199 N  N   . CYS A  1 289 ? 92.948  0.716   57.206 1.00 27.16 ? 479 CYS A N   1 
ATOM   2200 C  CA  . CYS A  1 289 ? 92.248  1.413   58.270 1.00 23.10 ? 479 CYS A CA  1 
ATOM   2201 C  C   . CYS A  1 289 ? 91.058  0.569   58.703 1.00 21.12 ? 479 CYS A C   1 
ATOM   2202 O  O   . CYS A  1 289 ? 90.281  0.103   57.868 1.00 18.42 ? 479 CYS A O   1 
ATOM   2203 C  CB  . CYS A  1 289 ? 91.771  2.767   57.752 1.00 23.63 ? 479 CYS A CB  1 
ATOM   2204 S  SG  . CYS A  1 289 ? 90.977  3.881   58.953 1.00 34.01 ? 479 CYS A SG  1 
ATOM   2205 N  N   . PRO A  1 290 ? 90.901  0.355   60.018 1.00 19.99 ? 480 PRO A N   1 
ATOM   2206 C  CA  . PRO A  1 290 ? 89.786  -0.443  60.538 1.00 15.37 ? 480 PRO A CA  1 
ATOM   2207 C  C   . PRO A  1 290 ? 88.413  -0.008  60.018 1.00 14.05 ? 480 PRO A C   1 
ATOM   2208 O  O   . PRO A  1 290 ? 88.206  1.154   59.659 1.00 11.92 ? 480 PRO A O   1 
ATOM   2209 C  CB  . PRO A  1 290 ? 89.924  -0.288  62.055 1.00 12.52 ? 480 PRO A CB  1 
ATOM   2210 C  CG  . PRO A  1 290 ? 90.660  1.007   62.212 1.00 19.96 ? 480 PRO A CG  1 
ATOM   2211 C  CD  . PRO A  1 290 ? 91.690  0.923   61.123 1.00 14.18 ? 480 PRO A CD  1 
ATOM   2212 N  N   . ALA A  1 291 ? 87.485  -0.960  59.979 1.00 11.80 ? 481 ALA A N   1 
ATOM   2213 C  CA  . ALA A  1 291 ? 86.129  -0.728  59.500 1.00 12.40 ? 481 ALA A CA  1 
ATOM   2214 C  C   . ALA A  1 291 ? 85.464  0.482   60.149 1.00 16.05 ? 481 ALA A C   1 
ATOM   2215 O  O   . ALA A  1 291 ? 85.727  0.812   61.306 1.00 16.66 ? 481 ALA A O   1 
ATOM   2216 C  CB  . ALA A  1 291 ? 85.287  -1.968  59.733 1.00 12.71 ? 481 ALA A CB  1 
ATOM   2217 N  N   . ASP A  1 292 ? 84.592  1.136   59.391 1.00 16.73 ? 482 ASP A N   1 
ATOM   2218 C  CA  . ASP A  1 292 ? 83.888  2.310   59.886 1.00 17.96 ? 482 ASP A CA  1 
ATOM   2219 C  C   . ASP A  1 292 ? 82.814  1.902   60.891 1.00 18.51 ? 482 ASP A C   1 
ATOM   2220 O  O   . ASP A  1 292 ? 81.914  1.121   60.582 1.00 20.44 ? 482 ASP A O   1 
ATOM   2221 C  CB  . ASP A  1 292 ? 83.257  3.076   58.716 1.00 13.82 ? 482 ASP A CB  1 
ATOM   2222 C  CG  . ASP A  1 292 ? 82.889  4.505   59.081 1.00 18.46 ? 482 ASP A CG  1 
ATOM   2223 O  OD1 . ASP A  1 292 ? 82.498  5.268   58.169 1.00 18.19 ? 482 ASP A OD1 1 
ATOM   2224 O  OD2 . ASP A  1 292 ? 82.988  4.867   60.274 1.00 10.02 ? 482 ASP A OD2 1 
ATOM   2225 N  N   . VAL A  1 293 ? 82.928  2.429   62.103 1.00 18.33 ? 483 VAL A N   1 
ATOM   2226 C  CA  . VAL A  1 293 ? 81.976  2.137   63.161 1.00 13.17 ? 483 VAL A CA  1 
ATOM   2227 C  C   . VAL A  1 293 ? 81.135  3.366   63.483 1.00 16.08 ? 483 VAL A C   1 
ATOM   2228 O  O   . VAL A  1 293 ? 81.642  4.490   63.547 1.00 12.02 ? 483 VAL A O   1 
ATOM   2229 C  CB  . VAL A  1 293 ? 82.697  1.673   64.455 1.00 14.41 ? 483 VAL A CB  1 
ATOM   2230 C  CG1 . VAL A  1 293 ? 81.699  1.592   65.615 1.00 11.25 ? 483 VAL A CG1 1 
ATOM   2231 C  CG2 . VAL A  1 293 ? 83.352  0.316   64.228 1.00 1.00  ? 483 VAL A CG2 1 
ATOM   2232 N  N   . PHE A  1 294 ? 79.843  3.136   63.685 1.00 15.41 ? 484 PHE A N   1 
ATOM   2233 C  CA  . PHE A  1 294 ? 78.906  4.198   64.015 1.00 15.39 ? 484 PHE A CA  1 
ATOM   2234 C  C   . PHE A  1 294 ? 78.301  3.887   65.371 1.00 14.10 ? 484 PHE A C   1 
ATOM   2235 O  O   . PHE A  1 294 ? 78.180  2.721   65.738 1.00 17.82 ? 484 PHE A O   1 
ATOM   2236 C  CB  . PHE A  1 294 ? 77.769  4.250   62.985 1.00 12.92 ? 484 PHE A CB  1 
ATOM   2237 C  CG  . PHE A  1 294 ? 78.155  4.851   61.661 1.00 16.75 ? 484 PHE A CG  1 
ATOM   2238 C  CD1 . PHE A  1 294 ? 77.279  4.777   60.580 1.00 14.48 ? 484 PHE A CD1 1 
ATOM   2239 C  CD2 . PHE A  1 294 ? 79.375  5.502   61.492 1.00 15.07 ? 484 PHE A CD2 1 
ATOM   2240 C  CE1 . PHE A  1 294 ? 77.613  5.341   59.350 1.00 9.74  ? 484 PHE A CE1 1 
ATOM   2241 C  CE2 . PHE A  1 294 ? 79.716  6.068   60.267 1.00 10.84 ? 484 PHE A CE2 1 
ATOM   2242 C  CZ  . PHE A  1 294 ? 78.831  5.987   59.194 1.00 6.93  ? 484 PHE A CZ  1 
ATOM   2243 N  N   . HIS A  1 295 ? 77.932  4.916   66.125 1.00 12.28 ? 485 HIS A N   1 
ATOM   2244 C  CA  . HIS A  1 295 ? 77.280  4.669   67.400 1.00 16.43 ? 485 HIS A CA  1 
ATOM   2245 C  C   . HIS A  1 295 ? 75.845  4.272   67.039 1.00 17.05 ? 485 HIS A C   1 
ATOM   2246 O  O   . HIS A  1 295 ? 75.398  4.500   65.913 1.00 20.56 ? 485 HIS A O   1 
ATOM   2247 C  CB  . HIS A  1 295 ? 77.290  5.922   68.282 1.00 16.73 ? 485 HIS A CB  1 
ATOM   2248 C  CG  . HIS A  1 295 ? 78.638  6.251   68.847 1.00 22.26 ? 485 HIS A CG  1 
ATOM   2249 N  ND1 . HIS A  1 295 ? 79.469  5.298   69.396 1.00 19.46 ? 485 HIS A ND1 1 
ATOM   2250 C  CD2 . HIS A  1 295 ? 79.293  7.431   68.966 1.00 24.79 ? 485 HIS A CD2 1 
ATOM   2251 C  CE1 . HIS A  1 295 ? 80.575  5.876   69.827 1.00 22.77 ? 485 HIS A CE1 1 
ATOM   2252 N  NE2 . HIS A  1 295 ? 80.494  7.170   69.578 1.00 19.75 ? 485 HIS A NE2 1 
ATOM   2253 N  N   . LYS A  1 296 ? 75.124  3.679   67.981 1.00 17.35 ? 486 LYS A N   1 
ATOM   2254 C  CA  . LYS A  1 296 ? 73.757  3.244   67.713 1.00 10.91 ? 486 LYS A CA  1 
ATOM   2255 C  C   . LYS A  1 296 ? 72.818  4.366   67.293 1.00 8.88  ? 486 LYS A C   1 
ATOM   2256 O  O   . LYS A  1 296 ? 72.885  5.475   67.815 1.00 14.32 ? 486 LYS A O   1 
ATOM   2257 C  CB  . LYS A  1 296 ? 73.181  2.536   68.941 1.00 6.72  ? 486 LYS A CB  1 
ATOM   2258 C  CG  . LYS A  1 296 ? 73.929  1.270   69.326 1.00 4.91  ? 486 LYS A CG  1 
ATOM   2259 C  CD  . LYS A  1 296 ? 73.365  0.665   70.596 1.00 1.00  ? 486 LYS A CD  1 
ATOM   2260 C  CE  . LYS A  1 296 ? 74.058  -0.629  70.934 1.00 1.00  ? 486 LYS A CE  1 
ATOM   2261 N  NZ  . LYS A  1 296 ? 73.454  -1.295  72.117 1.00 16.44 ? 486 LYS A NZ  1 
ATOM   2262 N  N   . ASN A  1 297 ? 71.946  4.067   66.337 1.00 9.72  ? 487 ASN A N   1 
ATOM   2263 C  CA  . ASN A  1 297 ? 70.962  5.033   65.867 1.00 8.51  ? 487 ASN A CA  1 
ATOM   2264 C  C   . ASN A  1 297 ? 69.957  5.215   66.995 1.00 6.48  ? 487 ASN A C   1 
ATOM   2265 O  O   . ASN A  1 297 ? 69.628  4.255   67.686 1.00 2.74  ? 487 ASN A O   1 
ATOM   2266 C  CB  . ASN A  1 297 ? 70.235  4.502   64.625 1.00 6.92  ? 487 ASN A CB  1 
ATOM   2267 C  CG  . ASN A  1 297 ? 71.108  4.509   63.383 1.00 10.91 ? 487 ASN A CG  1 
ATOM   2268 O  OD1 . ASN A  1 297 ? 70.728  3.971   62.343 1.00 11.93 ? 487 ASN A OD1 1 
ATOM   2269 N  ND2 . ASN A  1 297 ? 72.281  5.127   63.482 1.00 23.11 ? 487 ASN A ND2 1 
ATOM   2270 N  N   . GLY A  1 298 ? 69.475  6.440   67.182 1.00 10.72 ? 488 GLY A N   1 
ATOM   2271 C  CA  . GLY A  1 298 ? 68.509  6.698   68.235 1.00 9.81  ? 488 GLY A CA  1 
ATOM   2272 C  C   . GLY A  1 298 ? 69.156  7.173   69.520 1.00 13.79 ? 488 GLY A C   1 
ATOM   2273 O  O   . GLY A  1 298 ? 68.471  7.576   70.462 1.00 12.81 ? 488 GLY A O   1 
ATOM   2274 N  N   . GLN A  1 299 ? 70.482  7.116   69.567 1.00 16.06 ? 489 GLN A N   1 
ATOM   2275 C  CA  . GLN A  1 299 ? 71.211  7.559   70.742 1.00 17.64 ? 489 GLN A CA  1 
ATOM   2276 C  C   . GLN A  1 299 ? 71.197  9.080   70.788 1.00 18.76 ? 489 GLN A C   1 
ATOM   2277 O  O   . GLN A  1 299 ? 71.507  9.740   69.797 1.00 19.81 ? 489 GLN A O   1 
ATOM   2278 C  CB  . GLN A  1 299 ? 72.655  7.056   70.695 1.00 18.86 ? 489 GLN A CB  1 
ATOM   2279 C  CG  . GLN A  1 299 ? 73.538  7.657   71.777 1.00 29.67 ? 489 GLN A CG  1 
ATOM   2280 C  CD  . GLN A  1 299 ? 74.887  6.980   71.876 1.00 39.54 ? 489 GLN A CD  1 
ATOM   2281 O  OE1 . GLN A  1 299 ? 74.976  5.793   72.195 1.00 49.51 ? 489 GLN A OE1 1 
ATOM   2282 N  NE2 . GLN A  1 299 ? 75.948  7.729   71.601 1.00 47.53 ? 489 GLN A NE2 1 
ATOM   2283 N  N   . PRO A  1 300 ? 70.814  9.661   71.936 1.00 20.88 ? 490 PRO A N   1 
ATOM   2284 C  CA  . PRO A  1 300 ? 70.781  11.121  72.047 1.00 21.60 ? 490 PRO A CA  1 
ATOM   2285 C  C   . PRO A  1 300 ? 72.134  11.741  71.707 1.00 23.22 ? 490 PRO A C   1 
ATOM   2286 O  O   . PRO A  1 300 ? 73.182  11.209  72.082 1.00 23.23 ? 490 PRO A O   1 
ATOM   2287 C  CB  . PRO A  1 300 ? 70.378  11.339  73.500 1.00 18.44 ? 490 PRO A CB  1 
ATOM   2288 C  CG  . PRO A  1 300 ? 69.440  10.203  73.741 1.00 10.84 ? 490 PRO A CG  1 
ATOM   2289 C  CD  . PRO A  1 300 ? 70.189  9.036   73.116 1.00 21.97 ? 490 PRO A CD  1 
ATOM   2290 N  N   . CYS A  1 301 ? 72.101  12.861  70.991 1.00 20.15 ? 491 CYS A N   1 
ATOM   2291 C  CA  . CYS A  1 301 ? 73.319  13.551  70.585 1.00 18.79 ? 491 CYS A CA  1 
ATOM   2292 C  C   . CYS A  1 301 ? 73.151  15.074  70.587 1.00 17.77 ? 491 CYS A C   1 
ATOM   2293 O  O   . CYS A  1 301 ? 72.034  15.586  70.642 1.00 17.20 ? 491 CYS A O   1 
ATOM   2294 C  CB  . CYS A  1 301 ? 73.745  13.065  69.195 1.00 22.15 ? 491 CYS A CB  1 
ATOM   2295 S  SG  . CYS A  1 301 ? 72.445  13.151  67.915 1.00 27.24 ? 491 CYS A SG  1 
ATOM   2296 N  N   . LEU A  1 302 ? 74.272  15.786  70.525 1.00 15.95 ? 492 LEU A N   1 
ATOM   2297 C  CA  . LEU A  1 302 ? 74.278  17.244  70.535 1.00 20.49 ? 492 LEU A CA  1 
ATOM   2298 C  C   . LEU A  1 302 ? 73.457  17.813  71.689 1.00 25.43 ? 492 LEU A C   1 
ATOM   2299 O  O   . LEU A  1 302 ? 72.493  18.558  71.482 1.00 22.11 ? 492 LEU A O   1 
ATOM   2300 C  CB  . LEU A  1 302 ? 73.769  17.795  69.196 1.00 20.21 ? 492 LEU A CB  1 
ATOM   2301 C  CG  . LEU A  1 302 ? 74.707  17.620  67.993 1.00 19.41 ? 492 LEU A CG  1 
ATOM   2302 C  CD1 . LEU A  1 302 ? 74.053  18.172  66.724 1.00 11.69 ? 492 LEU A CD1 1 
ATOM   2303 C  CD2 . LEU A  1 302 ? 76.023  18.341  68.271 1.00 11.19 ? 492 LEU A CD2 1 
ATOM   2304 N  N   . ASP A  1 303 ? 73.857  17.455  72.908 1.00 31.31 ? 493 ASP A N   1 
ATOM   2305 C  CA  . ASP A  1 303 ? 73.189  17.912  74.124 1.00 39.90 ? 493 ASP A CA  1 
ATOM   2306 C  C   . ASP A  1 303 ? 71.678  17.709  74.081 1.00 40.91 ? 493 ASP A C   1 
ATOM   2307 O  O   . ASP A  1 303 ? 70.902  18.633  74.332 1.00 40.76 ? 493 ASP A O   1 
ATOM   2308 C  CB  . ASP A  1 303 ? 73.509  19.386  74.375 1.00 43.77 ? 493 ASP A CB  1 
ATOM   2309 C  CG  . ASP A  1 303 ? 74.976  19.615  74.670 1.00 46.50 ? 493 ASP A CG  1 
ATOM   2310 O  OD1 . ASP A  1 303 ? 75.448  19.149  75.730 1.00 48.93 ? 493 ASP A OD1 1 
ATOM   2311 O  OD2 . ASP A  1 303 ? 75.657  20.253  73.840 1.00 46.05 ? 493 ASP A OD2 1 
ATOM   2312 N  N   . ASN A  1 304 ? 71.276  16.484  73.764 1.00 40.44 ? 494 ASN A N   1 
ATOM   2313 C  CA  . ASN A  1 304 ? 69.871  16.115  73.685 1.00 40.10 ? 494 ASN A CA  1 
ATOM   2314 C  C   . ASN A  1 304 ? 69.032  16.959  72.738 1.00 36.34 ? 494 ASN A C   1 
ATOM   2315 O  O   . ASN A  1 304 ? 67.901  17.318  73.062 1.00 36.70 ? 494 ASN A O   1 
ATOM   2316 C  CB  . ASN A  1 304 ? 69.240  16.132  75.079 1.00 46.36 ? 494 ASN A CB  1 
ATOM   2317 C  CG  . ASN A  1 304 ? 69.628  14.922  75.903 1.00 53.34 ? 494 ASN A CG  1 
ATOM   2318 O  OD1 . ASN A  1 304 ? 70.791  14.753  76.273 1.00 58.46 ? 494 ASN A OD1 1 
ATOM   2319 N  ND2 . ASN A  1 304 ? 68.655  14.065  76.184 1.00 60.18 ? 494 ASN A ND2 1 
ATOM   2320 N  N   . TYR A  1 305 ? 69.585  17.274  71.569 1.00 29.46 ? 495 TYR A N   1 
ATOM   2321 C  CA  . TYR A  1 305 ? 68.854  18.045  70.571 1.00 25.57 ? 495 TYR A CA  1 
ATOM   2322 C  C   . TYR A  1 305 ? 68.530  17.162  69.377 1.00 21.40 ? 495 TYR A C   1 
ATOM   2323 O  O   . TYR A  1 305 ? 67.691  17.500  68.542 1.00 18.14 ? 495 TYR A O   1 
ATOM   2324 C  CB  . TYR A  1 305 ? 69.660  19.260  70.115 1.00 26.60 ? 495 TYR A CB  1 
ATOM   2325 C  CG  . TYR A  1 305 ? 69.363  20.506  70.913 1.00 30.11 ? 495 TYR A CG  1 
ATOM   2326 C  CD1 . TYR A  1 305 ? 69.727  20.602  72.254 1.00 31.71 ? 495 TYR A CD1 1 
ATOM   2327 C  CD2 . TYR A  1 305 ? 68.698  21.586  70.330 1.00 34.19 ? 495 TYR A CD2 1 
ATOM   2328 C  CE1 . TYR A  1 305 ? 69.435  21.742  72.997 1.00 32.40 ? 495 TYR A CE1 1 
ATOM   2329 C  CE2 . TYR A  1 305 ? 68.400  22.731  71.064 1.00 34.44 ? 495 TYR A CE2 1 
ATOM   2330 C  CZ  . TYR A  1 305 ? 68.773  22.801  72.397 1.00 34.45 ? 495 TYR A CZ  1 
ATOM   2331 O  OH  . TYR A  1 305 ? 68.488  23.929  73.128 1.00 37.41 ? 495 TYR A OH  1 
ATOM   2332 N  N   . GLY A  1 306 ? 69.202  16.022  69.304 1.00 19.09 ? 496 GLY A N   1 
ATOM   2333 C  CA  . GLY A  1 306 ? 68.961  15.099  68.215 1.00 19.93 ? 496 GLY A CA  1 
ATOM   2334 C  C   . GLY A  1 306 ? 69.229  13.669  68.633 1.00 18.25 ? 496 GLY A C   1 
ATOM   2335 O  O   . GLY A  1 306 ? 69.549  13.399  69.788 1.00 19.65 ? 496 GLY A O   1 
ATOM   2336 N  N   . TYR A  1 307 ? 69.076  12.750  67.689 1.00 21.06 ? 497 TYR A N   1 
ATOM   2337 C  CA  . TYR A  1 307 ? 69.332  11.339  67.935 1.00 18.93 ? 497 TYR A CA  1 
ATOM   2338 C  C   . TYR A  1 307 ? 70.217  10.850  66.805 1.00 18.62 ? 497 TYR A C   1 
ATOM   2339 O  O   . TYR A  1 307 ? 70.023  11.224  65.652 1.00 22.88 ? 497 TYR A O   1 
ATOM   2340 C  CB  . TYR A  1 307 ? 68.031  10.540  67.959 1.00 16.05 ? 497 TYR A CB  1 
ATOM   2341 C  CG  . TYR A  1 307 ? 67.085  10.954  69.056 1.00 13.61 ? 497 TYR A CG  1 
ATOM   2342 C  CD1 . TYR A  1 307 ? 66.128  11.947  68.842 1.00 18.33 ? 497 TYR A CD1 1 
ATOM   2343 C  CD2 . TYR A  1 307 ? 67.144  10.356  70.315 1.00 12.82 ? 497 TYR A CD2 1 
ATOM   2344 C  CE1 . TYR A  1 307 ? 65.244  12.331  69.858 1.00 14.35 ? 497 TYR A CE1 1 
ATOM   2345 C  CE2 . TYR A  1 307 ? 66.270  10.733  71.335 1.00 14.36 ? 497 TYR A CE2 1 
ATOM   2346 C  CZ  . TYR A  1 307 ? 65.322  11.719  71.098 1.00 11.29 ? 497 TYR A CZ  1 
ATOM   2347 O  OH  . TYR A  1 307 ? 64.449  12.084  72.096 1.00 15.91 ? 497 TYR A OH  1 
ATOM   2348 N  N   . CYS A  1 308 ? 71.193  10.018  67.136 1.00 20.65 ? 498 CYS A N   1 
ATOM   2349 C  CA  . CYS A  1 308 ? 72.113  9.510   66.131 1.00 16.65 ? 498 CYS A CA  1 
ATOM   2350 C  C   . CYS A  1 308 ? 71.413  8.802   64.993 1.00 13.04 ? 498 CYS A C   1 
ATOM   2351 O  O   . CYS A  1 308 ? 70.503  8.007   65.207 1.00 15.44 ? 498 CYS A O   1 
ATOM   2352 C  CB  . CYS A  1 308 ? 73.120  8.554   66.765 1.00 15.99 ? 498 CYS A CB  1 
ATOM   2353 S  SG  . CYS A  1 308 ? 74.307  9.331   67.908 1.00 28.90 ? 498 CYS A SG  1 
ATOM   2354 N  N   . TYR A  1 309 ? 71.841  9.106   63.775 1.00 15.51 ? 499 TYR A N   1 
ATOM   2355 C  CA  . TYR A  1 309 ? 71.291  8.474   62.587 1.00 13.91 ? 499 TYR A CA  1 
ATOM   2356 C  C   . TYR A  1 309 ? 72.418  8.246   61.587 1.00 14.12 ? 499 TYR A C   1 
ATOM   2357 O  O   . TYR A  1 309 ? 72.904  9.185   60.958 1.00 12.06 ? 499 TYR A O   1 
ATOM   2358 C  CB  . TYR A  1 309 ? 70.199  9.339   61.948 1.00 14.19 ? 499 TYR A CB  1 
ATOM   2359 C  CG  . TYR A  1 309 ? 69.645  8.729   60.679 1.00 13.80 ? 499 TYR A CG  1 
ATOM   2360 C  CD1 . TYR A  1 309 ? 69.007  7.489   60.700 1.00 16.16 ? 499 TYR A CD1 1 
ATOM   2361 C  CD2 . TYR A  1 309 ? 69.816  9.359   59.446 1.00 17.29 ? 499 TYR A CD2 1 
ATOM   2362 C  CE1 . TYR A  1 309 ? 68.561  6.887   59.525 1.00 19.01 ? 499 TYR A CE1 1 
ATOM   2363 C  CE2 . TYR A  1 309 ? 69.370  8.768   58.264 1.00 14.94 ? 499 TYR A CE2 1 
ATOM   2364 C  CZ  . TYR A  1 309 ? 68.747  7.532   58.310 1.00 20.21 ? 499 TYR A CZ  1 
ATOM   2365 O  OH  . TYR A  1 309 ? 68.330  6.933   57.143 1.00 20.08 ? 499 TYR A OH  1 
ATOM   2366 N  N   . ASN A  1 310 ? 72.830  6.989   61.460 1.00 11.61 ? 500 ASN A N   1 
ATOM   2367 C  CA  . ASN A  1 310 ? 73.897  6.595   60.547 1.00 11.83 ? 500 ASN A CA  1 
ATOM   2368 C  C   . ASN A  1 310 ? 75.182  7.406   60.660 1.00 12.40 ? 500 ASN A C   1 
ATOM   2369 O  O   . ASN A  1 310 ? 75.758  7.804   59.654 1.00 13.76 ? 500 ASN A O   1 
ATOM   2370 C  CB  . ASN A  1 310 ? 73.407  6.637   59.100 1.00 6.96  ? 500 ASN A CB  1 
ATOM   2371 C  CG  . ASN A  1 310 ? 72.285  5.659   58.842 1.00 15.61 ? 500 ASN A CG  1 
ATOM   2372 O  OD1 . ASN A  1 310 ? 72.304  4.529   59.332 1.00 15.09 ? 500 ASN A OD1 1 
ATOM   2373 N  ND2 . ASN A  1 310 ? 71.302  6.083   58.060 1.00 21.86 ? 500 ASN A ND2 1 
ATOM   2374 N  N   . GLY A  1 311 ? 75.627  7.647   61.888 1.00 14.07 ? 501 GLY A N   1 
ATOM   2375 C  CA  . GLY A  1 311 ? 76.864  8.374   62.094 1.00 9.82  ? 501 GLY A CA  1 
ATOM   2376 C  C   . GLY A  1 311 ? 76.756  9.879   62.163 1.00 11.12 ? 501 GLY A C   1 
ATOM   2377 O  O   . GLY A  1 311 ? 77.776  10.566  62.227 1.00 15.58 ? 501 GLY A O   1 
ATOM   2378 N  N   . ASN A  1 312 ? 75.535  10.402  62.152 1.00 15.64 ? 502 ASN A N   1 
ATOM   2379 C  CA  . ASN A  1 312 ? 75.342  11.847  62.222 1.00 17.91 ? 502 ASN A CA  1 
ATOM   2380 C  C   . ASN A  1 312 ? 74.275  12.253  63.225 1.00 18.10 ? 502 ASN A C   1 
ATOM   2381 O  O   . ASN A  1 312 ? 73.552  11.412  63.757 1.00 20.02 ? 502 ASN A O   1 
ATOM   2382 C  CB  . ASN A  1 312 ? 74.989  12.399  60.841 1.00 25.49 ? 502 ASN A CB  1 
ATOM   2383 C  CG  . ASN A  1 312 ? 76.176  12.399  59.901 1.00 34.27 ? 502 ASN A CG  1 
ATOM   2384 O  OD1 . ASN A  1 312 ? 77.183  13.062  60.158 1.00 37.89 ? 502 ASN A OD1 1 
ATOM   2385 N  ND2 . ASN A  1 312 ? 76.068  11.649  58.805 1.00 35.58 ? 502 ASN A ND2 1 
ATOM   2386 N  N   . CYS A  1 313 ? 74.183  13.551  63.484 1.00 20.65 ? 503 CYS A N   1 
ATOM   2387 C  CA  . CYS A  1 313 ? 73.203  14.060  64.429 1.00 21.21 ? 503 CYS A CA  1 
ATOM   2388 C  C   . CYS A  1 313 ? 72.392  15.188  63.804 1.00 23.70 ? 503 CYS A C   1 
ATOM   2389 O  O   . CYS A  1 313 ? 72.493  16.343  64.214 1.00 30.69 ? 503 CYS A O   1 
ATOM   2390 C  CB  . CYS A  1 313 ? 73.905  14.563  65.685 1.00 18.19 ? 503 CYS A CB  1 
ATOM   2391 S  SG  . CYS A  1 313 ? 72.747  14.950  67.025 1.00 26.60 ? 503 CYS A SG  1 
ATOM   2392 N  N   . PRO A  1 314 ? 71.561  14.860  62.803 1.00 19.85 ? 504 PRO A N   1 
ATOM   2393 C  CA  . PRO A  1 314 ? 70.734  15.856  62.122 1.00 14.80 ? 504 PRO A CA  1 
ATOM   2394 C  C   . PRO A  1 314 ? 69.738  16.585  63.017 1.00 16.51 ? 504 PRO A C   1 
ATOM   2395 O  O   . PRO A  1 314 ? 68.937  15.963  63.711 1.00 19.65 ? 504 PRO A O   1 
ATOM   2396 C  CB  . PRO A  1 314 ? 70.045  15.039  61.031 1.00 15.97 ? 504 PRO A CB  1 
ATOM   2397 C  CG  . PRO A  1 314 ? 69.906  13.686  61.665 1.00 18.50 ? 504 PRO A CG  1 
ATOM   2398 C  CD  . PRO A  1 314 ? 71.264  13.504  62.306 1.00 18.66 ? 504 PRO A CD  1 
ATOM   2399 N  N   . ILE A  1 315 ? 69.796  17.911  62.996 1.00 18.98 ? 505 ILE A N   1 
ATOM   2400 C  CA  . ILE A  1 315 ? 68.880  18.732  63.780 1.00 20.50 ? 505 ILE A CA  1 
ATOM   2401 C  C   . ILE A  1 315 ? 68.447  19.938  62.949 1.00 19.44 ? 505 ILE A C   1 
ATOM   2402 O  O   . ILE A  1 315 ? 69.195  20.410  62.089 1.00 23.82 ? 505 ILE A O   1 
ATOM   2403 C  CB  . ILE A  1 315 ? 69.527  19.234  65.101 1.00 22.93 ? 505 ILE A CB  1 
ATOM   2404 C  CG1 . ILE A  1 315 ? 70.702  20.165  64.801 1.00 21.55 ? 505 ILE A CG1 1 
ATOM   2405 C  CG2 . ILE A  1 315 ? 69.991  18.051  65.933 1.00 26.54 ? 505 ILE A CG2 1 
ATOM   2406 C  CD1 . ILE A  1 315 ? 71.284  20.817  66.030 1.00 13.48 ? 505 ILE A CD1 1 
ATOM   2407 N  N   . MET A  1 316 ? 67.240  20.429  63.208 1.00 12.83 ? 506 MET A N   1 
ATOM   2408 C  CA  . MET A  1 316 ? 66.703  21.575  62.485 1.00 14.09 ? 506 MET A CA  1 
ATOM   2409 C  C   . MET A  1 316 ? 67.715  22.720  62.365 1.00 17.52 ? 506 MET A C   1 
ATOM   2410 O  O   . MET A  1 316 ? 68.043  23.160  61.262 1.00 20.16 ? 506 MET A O   1 
ATOM   2411 C  CB  . MET A  1 316 ? 65.436  22.086  63.184 1.00 18.15 ? 506 MET A CB  1 
ATOM   2412 C  CG  . MET A  1 316 ? 64.322  21.048  63.318 1.00 19.92 ? 506 MET A CG  1 
ATOM   2413 S  SD  . MET A  1 316 ? 63.542  20.615  61.749 1.00 27.36 ? 506 MET A SD  1 
ATOM   2414 C  CE  . MET A  1 316 ? 61.896  20.189  62.280 1.00 25.12 ? 506 MET A CE  1 
ATOM   2415 N  N   . TYR A  1 317 ? 68.214  23.191  63.503 1.00 16.38 ? 507 TYR A N   1 
ATOM   2416 C  CA  . TYR A  1 317 ? 69.164  24.297  63.524 1.00 17.08 ? 507 TYR A CA  1 
ATOM   2417 C  C   . TYR A  1 317 ? 70.349  24.161  62.561 1.00 18.65 ? 507 TYR A C   1 
ATOM   2418 O  O   . TYR A  1 317 ? 70.602  25.062  61.762 1.00 14.90 ? 507 TYR A O   1 
ATOM   2419 C  CB  . TYR A  1 317 ? 69.676  24.522  64.949 1.00 17.21 ? 507 TYR A CB  1 
ATOM   2420 C  CG  . TYR A  1 317 ? 70.670  25.653  65.050 1.00 29.07 ? 507 TYR A CG  1 
ATOM   2421 C  CD1 . TYR A  1 317 ? 70.362  26.920  64.552 1.00 27.63 ? 507 TYR A CD1 1 
ATOM   2422 C  CD2 . TYR A  1 317 ? 71.921  25.462  65.640 1.00 28.79 ? 507 TYR A CD2 1 
ATOM   2423 C  CE1 . TYR A  1 317 ? 71.270  27.967  64.638 1.00 27.63 ? 507 TYR A CE1 1 
ATOM   2424 C  CE2 . TYR A  1 317 ? 72.837  26.505  65.730 1.00 25.99 ? 507 TYR A CE2 1 
ATOM   2425 C  CZ  . TYR A  1 317 ? 72.504  27.754  65.228 1.00 27.10 ? 507 TYR A CZ  1 
ATOM   2426 O  OH  . TYR A  1 317 ? 73.398  28.798  65.319 1.00 36.40 ? 507 TYR A OH  1 
ATOM   2427 N  N   . HIS A  1 318 ? 71.081  23.052  62.632 1.00 20.78 ? 508 HIS A N   1 
ATOM   2428 C  CA  . HIS A  1 318 ? 72.220  22.872  61.738 1.00 23.91 ? 508 HIS A CA  1 
ATOM   2429 C  C   . HIS A  1 318 ? 71.771  22.790  60.287 1.00 23.95 ? 508 HIS A C   1 
ATOM   2430 O  O   . HIS A  1 318 ? 72.437  23.327  59.397 1.00 18.32 ? 508 HIS A O   1 
ATOM   2431 C  CB  . HIS A  1 318 ? 73.021  21.614  62.095 1.00 23.81 ? 508 HIS A CB  1 
ATOM   2432 C  CG  . HIS A  1 318 ? 73.780  21.725  63.381 1.00 25.36 ? 508 HIS A CG  1 
ATOM   2433 N  ND1 . HIS A  1 318 ? 74.245  22.928  63.868 1.00 29.40 ? 508 HIS A ND1 1 
ATOM   2434 C  CD2 . HIS A  1 318 ? 74.177  20.782  64.268 1.00 25.92 ? 508 HIS A CD2 1 
ATOM   2435 C  CE1 . HIS A  1 318 ? 74.893  22.722  65.000 1.00 26.12 ? 508 HIS A CE1 1 
ATOM   2436 N  NE2 . HIS A  1 318 ? 74.867  21.428  65.265 1.00 24.68 ? 508 HIS A NE2 1 
ATOM   2437 N  N   . GLN A  1 319 ? 70.643  22.120  60.047 1.00 19.73 ? 509 GLN A N   1 
ATOM   2438 C  CA  . GLN A  1 319 ? 70.126  21.988  58.687 1.00 18.22 ? 509 GLN A CA  1 
ATOM   2439 C  C   . GLN A  1 319 ? 69.787  23.349  58.076 1.00 18.05 ? 509 GLN A C   1 
ATOM   2440 O  O   . GLN A  1 319 ? 69.956  23.540  56.870 1.00 17.20 ? 509 GLN A O   1 
ATOM   2441 C  CB  . GLN A  1 319 ? 68.906  21.065  58.656 1.00 13.96 ? 509 GLN A CB  1 
ATOM   2442 C  CG  . GLN A  1 319 ? 69.243  19.602  58.920 1.00 13.17 ? 509 GLN A CG  1 
ATOM   2443 C  CD  . GLN A  1 319 ? 68.022  18.702  58.897 1.00 12.44 ? 509 GLN A CD  1 
ATOM   2444 O  OE1 . GLN A  1 319 ? 67.414  18.479  57.847 1.00 12.38 ? 509 GLN A OE1 1 
ATOM   2445 N  NE2 . GLN A  1 319 ? 67.652  18.185  60.061 1.00 7.99  ? 509 GLN A NE2 1 
ATOM   2446 N  N   . CYS A  1 320 ? 69.316  24.290  58.897 1.00 13.43 ? 510 CYS A N   1 
ATOM   2447 C  CA  . CYS A  1 320 ? 69.006  25.634  58.404 1.00 16.19 ? 510 CYS A CA  1 
ATOM   2448 C  C   . CYS A  1 320 ? 70.310  26.352  58.060 1.00 20.62 ? 510 CYS A C   1 
ATOM   2449 O  O   . CYS A  1 320 ? 70.419  26.998  57.018 1.00 22.92 ? 510 CYS A O   1 
ATOM   2450 C  CB  . CYS A  1 320 ? 68.247  26.453  59.451 1.00 9.10  ? 510 CYS A CB  1 
ATOM   2451 S  SG  . CYS A  1 320 ? 66.477  26.057  59.613 1.00 18.82 ? 510 CYS A SG  1 
ATOM   2452 N  N   . TYR A  1 321 ? 71.298  26.236  58.942 1.00 22.55 ? 511 TYR A N   1 
ATOM   2453 C  CA  . TYR A  1 321 ? 72.595  26.863  58.719 1.00 20.90 ? 511 TYR A CA  1 
ATOM   2454 C  C   . TYR A  1 321 ? 73.220  26.381  57.413 1.00 21.25 ? 511 TYR A C   1 
ATOM   2455 O  O   . TYR A  1 321 ? 73.757  27.181  56.647 1.00 20.62 ? 511 TYR A O   1 
ATOM   2456 C  CB  . TYR A  1 321 ? 73.548  26.554  59.875 1.00 24.22 ? 511 TYR A CB  1 
ATOM   2457 C  CG  . TYR A  1 321 ? 75.001  26.830  59.549 1.00 27.88 ? 511 TYR A CG  1 
ATOM   2458 C  CD1 . TYR A  1 321 ? 75.459  28.133  59.359 1.00 28.98 ? 511 TYR A CD1 1 
ATOM   2459 C  CD2 . TYR A  1 321 ? 75.910  25.784  59.394 1.00 27.83 ? 511 TYR A CD2 1 
ATOM   2460 C  CE1 . TYR A  1 321 ? 76.784  28.389  59.021 1.00 27.91 ? 511 TYR A CE1 1 
ATOM   2461 C  CE2 . TYR A  1 321 ? 77.237  26.027  59.055 1.00 29.30 ? 511 TYR A CE2 1 
ATOM   2462 C  CZ  . TYR A  1 321 ? 77.668  27.331  58.869 1.00 30.70 ? 511 TYR A CZ  1 
ATOM   2463 O  OH  . TYR A  1 321 ? 78.979  27.574  58.526 1.00 33.80 ? 511 TYR A OH  1 
ATOM   2464 N  N   . ASP A  1 322 ? 73.157  25.075  57.167 1.00 21.10 ? 512 ASP A N   1 
ATOM   2465 C  CA  . ASP A  1 322 ? 73.729  24.510  55.949 1.00 26.82 ? 512 ASP A CA  1 
ATOM   2466 C  C   . ASP A  1 322 ? 73.089  25.083  54.688 1.00 27.36 ? 512 ASP A C   1 
ATOM   2467 O  O   . ASP A  1 322 ? 73.672  25.011  53.608 1.00 30.26 ? 512 ASP A O   1 
ATOM   2468 C  CB  . ASP A  1 322 ? 73.583  22.984  55.933 1.00 31.52 ? 512 ASP A CB  1 
ATOM   2469 C  CG  . ASP A  1 322 ? 74.397  22.304  57.020 1.00 41.83 ? 512 ASP A CG  1 
ATOM   2470 O  OD1 . ASP A  1 322 ? 75.608  22.599  57.131 1.00 40.72 ? 512 ASP A OD1 1 
ATOM   2471 O  OD2 . ASP A  1 322 ? 73.828  21.470  57.758 1.00 45.11 ? 512 ASP A OD2 1 
ATOM   2472 N  N   . LEU A  1 323 ? 71.894  25.654  54.827 1.00 23.09 ? 513 LEU A N   1 
ATOM   2473 C  CA  . LEU A  1 323 ? 71.181  26.221  53.686 1.00 18.09 ? 513 LEU A CA  1 
ATOM   2474 C  C   . LEU A  1 323 ? 71.293  27.729  53.530 1.00 17.93 ? 513 LEU A C   1 
ATOM   2475 O  O   . LEU A  1 323 ? 71.510  28.225  52.425 1.00 21.28 ? 513 LEU A O   1 
ATOM   2476 C  CB  . LEU A  1 323 ? 69.695  25.861  53.752 1.00 21.22 ? 513 LEU A CB  1 
ATOM   2477 C  CG  . LEU A  1 323 ? 69.262  24.466  53.305 1.00 20.00 ? 513 LEU A CG  1 
ATOM   2478 C  CD1 . LEU A  1 323 ? 67.768  24.316  53.515 1.00 20.26 ? 513 LEU A CD1 1 
ATOM   2479 C  CD2 . LEU A  1 323 ? 69.616  24.264  51.842 1.00 15.88 ? 513 LEU A CD2 1 
ATOM   2480 N  N   . PHE A  1 324 ? 71.140  28.460  54.629 1.00 16.53 ? 514 PHE A N   1 
ATOM   2481 C  CA  . PHE A  1 324 ? 71.180  29.917  54.578 1.00 14.34 ? 514 PHE A CA  1 
ATOM   2482 C  C   . PHE A  1 324 ? 72.329  30.564  55.342 1.00 10.22 ? 514 PHE A C   1 
ATOM   2483 O  O   . PHE A  1 324 ? 72.409  31.787  55.425 1.00 9.78  ? 514 PHE A O   1 
ATOM   2484 C  CB  . PHE A  1 324 ? 69.855  30.466  55.095 1.00 8.77  ? 514 PHE A CB  1 
ATOM   2485 C  CG  . PHE A  1 324 ? 68.659  29.786  54.511 1.00 14.93 ? 514 PHE A CG  1 
ATOM   2486 C  CD1 . PHE A  1 324 ? 67.619  29.348  55.335 1.00 19.42 ? 514 PHE A CD1 1 
ATOM   2487 C  CD2 . PHE A  1 324 ? 68.569  29.566  53.140 1.00 13.28 ? 514 PHE A CD2 1 
ATOM   2488 C  CE1 . PHE A  1 324 ? 66.503  28.696  54.803 1.00 16.21 ? 514 PHE A CE1 1 
ATOM   2489 C  CE2 . PHE A  1 324 ? 67.458  28.916  52.592 1.00 23.27 ? 514 PHE A CE2 1 
ATOM   2490 C  CZ  . PHE A  1 324 ? 66.421  28.479  53.429 1.00 20.13 ? 514 PHE A CZ  1 
ATOM   2491 N  N   . GLY A  1 325 ? 73.209  29.751  55.908 1.00 7.54  ? 515 GLY A N   1 
ATOM   2492 C  CA  . GLY A  1 325 ? 74.328  30.301  56.644 1.00 10.37 ? 515 GLY A CA  1 
ATOM   2493 C  C   . GLY A  1 325 ? 74.027  30.581  58.103 1.00 19.15 ? 515 GLY A C   1 
ATOM   2494 O  O   . GLY A  1 325 ? 72.998  30.162  58.637 1.00 11.98 ? 515 GLY A O   1 
ATOM   2495 N  N   . ALA A  1 326 ? 74.938  31.310  58.744 1.00 26.91 ? 516 ALA A N   1 
ATOM   2496 C  CA  . ALA A  1 326 ? 74.824  31.650  60.158 1.00 26.86 ? 516 ALA A CA  1 
ATOM   2497 C  C   . ALA A  1 326 ? 73.678  32.602  60.486 1.00 28.40 ? 516 ALA A C   1 
ATOM   2498 O  O   . ALA A  1 326 ? 73.072  33.198  59.598 1.00 26.24 ? 516 ALA A O   1 
ATOM   2499 C  CB  . ALA A  1 326 ? 76.144  32.234  60.652 1.00 18.30 ? 516 ALA A CB  1 
ATOM   2500 N  N   . ASP A  1 327 ? 73.401  32.727  61.782 1.00 32.56 ? 517 ASP A N   1 
ATOM   2501 C  CA  . ASP A  1 327 ? 72.347  33.588  62.305 1.00 37.80 ? 517 ASP A CA  1 
ATOM   2502 C  C   . ASP A  1 327 ? 70.953  33.260  61.769 1.00 41.08 ? 517 ASP A C   1 
ATOM   2503 O  O   . ASP A  1 327 ? 70.040  34.082  61.850 1.00 42.34 ? 517 ASP A O   1 
ATOM   2504 C  CB  . ASP A  1 327 ? 72.681  35.062  62.042 1.00 45.40 ? 517 ASP A CB  1 
ATOM   2505 C  CG  . ASP A  1 327 ? 73.921  35.531  62.801 1.00 51.25 ? 517 ASP A CG  1 
ATOM   2506 O  OD1 . ASP A  1 327 ? 74.026  35.255  64.018 1.00 52.84 ? 517 ASP A OD1 1 
ATOM   2507 O  OD2 . ASP A  1 327 ? 74.787  36.189  62.184 1.00 51.91 ? 517 ASP A OD2 1 
ATOM   2508 N  N   . VAL A  1 328 ? 70.796  32.058  61.223 1.00 42.68 ? 518 VAL A N   1 
ATOM   2509 C  CA  . VAL A  1 328 ? 69.508  31.605  60.698 1.00 43.51 ? 518 VAL A CA  1 
ATOM   2510 C  C   . VAL A  1 328 ? 69.033  30.440  61.568 1.00 43.73 ? 518 VAL A C   1 
ATOM   2511 O  O   . VAL A  1 328 ? 69.803  29.519  61.848 1.00 45.15 ? 518 VAL A O   1 
ATOM   2512 C  CB  . VAL A  1 328 ? 69.628  31.134  59.231 1.00 43.17 ? 518 VAL A CB  1 
ATOM   2513 C  CG1 . VAL A  1 328 ? 68.346  30.441  58.801 1.00 44.15 ? 518 VAL A CG1 1 
ATOM   2514 C  CG2 . VAL A  1 328 ? 69.907  32.324  58.325 1.00 37.56 ? 518 VAL A CG2 1 
ATOM   2515 N  N   . TYR A  1 329 ? 67.771  30.478  61.989 1.00 40.15 ? 519 TYR A N   1 
ATOM   2516 C  CA  . TYR A  1 329 ? 67.236  29.431  62.857 1.00 36.21 ? 519 TYR A CA  1 
ATOM   2517 C  C   . TYR A  1 329 ? 65.968  28.781  62.329 1.00 34.23 ? 519 TYR A C   1 
ATOM   2518 O  O   . TYR A  1 329 ? 65.430  29.183  61.301 1.00 33.15 ? 519 TYR A O   1 
ATOM   2519 C  CB  . TYR A  1 329 ? 66.968  30.005  64.250 1.00 31.49 ? 519 TYR A CB  1 
ATOM   2520 C  CG  . TYR A  1 329 ? 68.005  31.015  64.682 1.00 39.06 ? 519 TYR A CG  1 
ATOM   2521 C  CD1 . TYR A  1 329 ? 67.894  32.356  64.310 1.00 41.64 ? 519 TYR A CD1 1 
ATOM   2522 C  CD2 . TYR A  1 329 ? 69.125  30.625  65.416 1.00 34.57 ? 519 TYR A CD2 1 
ATOM   2523 C  CE1 . TYR A  1 329 ? 68.875  33.284  64.655 1.00 39.00 ? 519 TYR A CE1 1 
ATOM   2524 C  CE2 . TYR A  1 329 ? 70.111  31.545  65.766 1.00 35.94 ? 519 TYR A CE2 1 
ATOM   2525 C  CZ  . TYR A  1 329 ? 69.981  32.872  65.381 1.00 38.58 ? 519 TYR A CZ  1 
ATOM   2526 O  OH  . TYR A  1 329 ? 70.960  33.783  65.708 1.00 36.29 ? 519 TYR A OH  1 
ATOM   2527 N  N   . GLU A  1 330 ? 65.499  27.767  63.049 1.00 33.41 ? 520 GLU A N   1 
ATOM   2528 C  CA  . GLU A  1 330 ? 64.287  27.052  62.678 1.00 32.20 ? 520 GLU A CA  1 
ATOM   2529 C  C   . GLU A  1 330 ? 63.069  27.960  62.813 1.00 28.14 ? 520 GLU A C   1 
ATOM   2530 O  O   . GLU A  1 330 ? 62.959  28.731  63.766 1.00 25.64 ? 520 GLU A O   1 
ATOM   2531 C  CB  . GLU A  1 330 ? 64.119  25.812  63.563 1.00 36.76 ? 520 GLU A CB  1 
ATOM   2532 C  CG  . GLU A  1 330 ? 62.723  25.200  63.531 1.00 41.66 ? 520 GLU A CG  1 
ATOM   2533 C  CD  . GLU A  1 330 ? 62.660  23.839  64.206 1.00 46.05 ? 520 GLU A CD  1 
ATOM   2534 O  OE1 . GLU A  1 330 ? 63.213  23.693  65.320 1.00 41.54 ? 520 GLU A OE1 1 
ATOM   2535 O  OE2 . GLU A  1 330 ? 62.050  22.917  63.621 1.00 44.43 ? 520 GLU A OE2 1 
ATOM   2536 N  N   . ALA A  1 331 ? 62.158  27.860  61.851 1.00 24.39 ? 521 ALA A N   1 
ATOM   2537 C  CA  . ALA A  1 331 ? 60.949  28.669  61.845 1.00 24.40 ? 521 ALA A CA  1 
ATOM   2538 C  C   . ALA A  1 331 ? 59.912  28.155  62.838 1.00 28.48 ? 521 ALA A C   1 
ATOM   2539 O  O   . ALA A  1 331 ? 60.024  27.037  63.347 1.00 26.99 ? 521 ALA A O   1 
ATOM   2540 C  CB  . ALA A  1 331 ? 60.360  28.692  60.451 1.00 21.79 ? 521 ALA A CB  1 
ATOM   2541 N  N   . GLU A  1 332 ? 58.904  28.984  63.106 1.00 32.66 ? 522 GLU A N   1 
ATOM   2542 C  CA  . GLU A  1 332 ? 57.825  28.638  64.030 1.00 32.81 ? 522 GLU A CA  1 
ATOM   2543 C  C   . GLU A  1 332 ? 57.021  27.462  63.485 1.00 31.31 ? 522 GLU A C   1 
ATOM   2544 O  O   . GLU A  1 332 ? 56.988  27.230  62.276 1.00 30.37 ? 522 GLU A O   1 
ATOM   2545 C  CB  . GLU A  1 332 ? 56.893  29.839  64.231 1.00 35.04 ? 522 GLU A CB  1 
ATOM   2546 C  CG  . GLU A  1 332 ? 57.542  31.043  64.900 1.00 46.20 ? 522 GLU A CG  1 
ATOM   2547 C  CD  . GLU A  1 332 ? 57.837  30.815  66.374 1.00 54.26 ? 522 GLU A CD  1 
ATOM   2548 O  OE1 . GLU A  1 332 ? 56.878  30.632  67.157 1.00 55.59 ? 522 GLU A OE1 1 
ATOM   2549 O  OE2 . GLU A  1 332 ? 59.030  30.821  66.750 1.00 58.07 ? 522 GLU A OE2 1 
ATOM   2550 N  N   . ASP A  1 333 ? 56.371  26.724  64.380 1.00 31.11 ? 523 ASP A N   1 
ATOM   2551 C  CA  . ASP A  1 333 ? 55.567  25.573  63.985 1.00 29.51 ? 523 ASP A CA  1 
ATOM   2552 C  C   . ASP A  1 333 ? 54.610  25.903  62.843 1.00 31.09 ? 523 ASP A C   1 
ATOM   2553 O  O   . ASP A  1 333 ? 54.525  25.162  61.863 1.00 34.32 ? 523 ASP A O   1 
ATOM   2554 C  CB  . ASP A  1 333 ? 54.770  25.049  65.181 1.00 27.43 ? 523 ASP A CB  1 
ATOM   2555 C  CG  . ASP A  1 333 ? 55.642  24.360  66.207 1.00 35.27 ? 523 ASP A CG  1 
ATOM   2556 O  OD1 . ASP A  1 333 ? 55.110  23.949  67.260 1.00 38.64 ? 523 ASP A OD1 1 
ATOM   2557 O  OD2 . ASP A  1 333 ? 56.859  24.222  65.961 1.00 38.43 ? 523 ASP A OD2 1 
ATOM   2558 N  N   . SER A  1 334 ? 53.893  27.015  62.971 1.00 30.75 ? 524 SER A N   1 
ATOM   2559 C  CA  . SER A  1 334 ? 52.935  27.429  61.952 1.00 30.18 ? 524 SER A CA  1 
ATOM   2560 C  C   . SER A  1 334 ? 53.497  27.349  60.532 1.00 26.05 ? 524 SER A C   1 
ATOM   2561 O  O   . SER A  1 334 ? 52.803  26.930  59.609 1.00 27.26 ? 524 SER A O   1 
ATOM   2562 C  CB  . SER A  1 334 ? 52.448  28.850  62.238 1.00 31.89 ? 524 SER A CB  1 
ATOM   2563 O  OG  . SER A  1 334 ? 53.530  29.761  62.283 1.00 43.78 ? 524 SER A OG  1 
ATOM   2564 N  N   . CYS A  1 335 ? 54.751  27.748  60.355 1.00 25.41 ? 525 CYS A N   1 
ATOM   2565 C  CA  . CYS A  1 335 ? 55.373  27.705  59.036 1.00 24.77 ? 525 CYS A CA  1 
ATOM   2566 C  C   . CYS A  1 335 ? 55.362  26.299  58.437 1.00 22.62 ? 525 CYS A C   1 
ATOM   2567 O  O   . CYS A  1 335 ? 55.177  26.129  57.232 1.00 22.97 ? 525 CYS A O   1 
ATOM   2568 C  CB  . CYS A  1 335 ? 56.824  28.190  59.099 1.00 25.56 ? 525 CYS A CB  1 
ATOM   2569 S  SG  . CYS A  1 335 ? 57.110  29.990  59.175 1.00 26.57 ? 525 CYS A SG  1 
ATOM   2570 N  N   . PHE A  1 336 ? 55.562  25.294  59.281 1.00 19.55 ? 526 PHE A N   1 
ATOM   2571 C  CA  . PHE A  1 336 ? 55.606  23.912  58.819 1.00 20.62 ? 526 PHE A CA  1 
ATOM   2572 C  C   . PHE A  1 336 ? 54.277  23.350  58.316 1.00 23.16 ? 526 PHE A C   1 
ATOM   2573 O  O   . PHE A  1 336 ? 54.235  22.261  57.735 1.00 23.93 ? 526 PHE A O   1 
ATOM   2574 C  CB  . PHE A  1 336 ? 56.184  23.011  59.920 1.00 12.43 ? 526 PHE A CB  1 
ATOM   2575 C  CG  . PHE A  1 336 ? 57.672  23.142  60.087 1.00 13.07 ? 526 PHE A CG  1 
ATOM   2576 C  CD1 . PHE A  1 336 ? 58.223  24.254  60.721 1.00 12.83 ? 526 PHE A CD1 1 
ATOM   2577 C  CD2 . PHE A  1 336 ? 58.527  22.174  59.569 1.00 8.99  ? 526 PHE A CD2 1 
ATOM   2578 C  CE1 . PHE A  1 336 ? 59.607  24.399  60.833 1.00 16.19 ? 526 PHE A CE1 1 
ATOM   2579 C  CE2 . PHE A  1 336 ? 59.911  22.308  59.675 1.00 13.33 ? 526 PHE A CE2 1 
ATOM   2580 C  CZ  . PHE A  1 336 ? 60.452  23.421  60.307 1.00 17.33 ? 526 PHE A CZ  1 
ATOM   2581 N  N   . GLU A  1 337 ? 53.194  24.090  58.526 1.00 24.91 ? 527 GLU A N   1 
ATOM   2582 C  CA  . GLU A  1 337 ? 51.882  23.639  58.074 1.00 26.38 ? 527 GLU A CA  1 
ATOM   2583 C  C   . GLU A  1 337 ? 51.776  23.731  56.553 1.00 26.21 ? 527 GLU A C   1 
ATOM   2584 O  O   . GLU A  1 337 ? 50.864  23.161  55.950 1.00 22.82 ? 527 GLU A O   1 
ATOM   2585 C  CB  . GLU A  1 337 ? 50.785  24.470  58.742 1.00 27.68 ? 527 GLU A CB  1 
ATOM   2586 C  CG  . GLU A  1 337 ? 50.788  24.346  60.261 1.00 34.55 ? 527 GLU A CG  1 
ATOM   2587 C  CD  . GLU A  1 337 ? 49.715  25.185  60.929 1.00 37.94 ? 527 GLU A CD  1 
ATOM   2588 O  OE1 . GLU A  1 337 ? 49.656  25.180  62.177 1.00 40.10 ? 527 GLU A OE1 1 
ATOM   2589 O  OE2 . GLU A  1 337 ? 48.934  25.846  60.211 1.00 38.27 ? 527 GLU A OE2 1 
ATOM   2590 N  N   . ARG A  1 338 ? 52.719  24.447  55.940 1.00 24.37 ? 528 ARG A N   1 
ATOM   2591 C  CA  . ARG A  1 338 ? 52.759  24.603  54.488 1.00 21.54 ? 528 ARG A CA  1 
ATOM   2592 C  C   . ARG A  1 338 ? 52.973  23.250  53.816 1.00 21.04 ? 528 ARG A C   1 
ATOM   2593 O  O   . ARG A  1 338 ? 52.644  23.066  52.645 1.00 22.42 ? 528 ARG A O   1 
ATOM   2594 C  CB  . ARG A  1 338 ? 53.901  25.535  54.076 1.00 21.93 ? 528 ARG A CB  1 
ATOM   2595 C  CG  . ARG A  1 338 ? 53.633  27.027  54.225 1.00 30.91 ? 528 ARG A CG  1 
ATOM   2596 C  CD  . ARG A  1 338 ? 54.873  27.813  53.798 1.00 36.72 ? 528 ARG A CD  1 
ATOM   2597 N  NE  . ARG A  1 338 ? 54.678  29.262  53.733 1.00 37.36 ? 528 ARG A NE  1 
ATOM   2598 C  CZ  . ARG A  1 338 ? 54.277  30.021  54.750 1.00 37.95 ? 528 ARG A CZ  1 
ATOM   2599 N  NH1 . ARG A  1 338 ? 54.013  29.478  55.931 1.00 40.94 ? 528 ARG A NH1 1 
ATOM   2600 N  NH2 . ARG A  1 338 ? 54.165  31.331  54.591 1.00 28.71 ? 528 ARG A NH2 1 
ATOM   2601 N  N   . ASN A  1 339 ? 53.533  22.306  54.563 1.00 15.85 ? 529 ASN A N   1 
ATOM   2602 C  CA  . ASN A  1 339 ? 53.800  20.978  54.032 1.00 14.10 ? 529 ASN A CA  1 
ATOM   2603 C  C   . ASN A  1 339 ? 52.535  20.137  53.844 1.00 13.75 ? 529 ASN A C   1 
ATOM   2604 O  O   . ASN A  1 339 ? 52.594  19.018  53.340 1.00 13.82 ? 529 ASN A O   1 
ATOM   2605 C  CB  . ASN A  1 339 ? 54.806  20.256  54.937 1.00 13.86 ? 529 ASN A CB  1 
ATOM   2606 C  CG  . ASN A  1 339 ? 56.211  20.845  54.834 1.00 18.26 ? 529 ASN A CG  1 
ATOM   2607 O  OD1 . ASN A  1 339 ? 57.082  20.566  55.661 1.00 21.38 ? 529 ASN A OD1 1 
ATOM   2608 N  ND2 . ASN A  1 339 ? 56.436  21.658  53.809 1.00 10.49 ? 529 ASN A ND2 1 
ATOM   2609 N  N   . GLN A  1 340 ? 51.390  20.676  54.245 1.00 15.56 ? 530 GLN A N   1 
ATOM   2610 C  CA  . GLN A  1 340 ? 50.129  19.962  54.076 1.00 19.24 ? 530 GLN A CA  1 
ATOM   2611 C  C   . GLN A  1 340 ? 49.547  20.244  52.690 1.00 20.48 ? 530 GLN A C   1 
ATOM   2612 O  O   . GLN A  1 340 ? 48.733  19.474  52.186 1.00 24.44 ? 530 GLN A O   1 
ATOM   2613 C  CB  . GLN A  1 340 ? 49.119  20.384  55.144 1.00 14.45 ? 530 GLN A CB  1 
ATOM   2614 C  CG  . GLN A  1 340 ? 49.560  20.086  56.559 1.00 18.49 ? 530 GLN A CG  1 
ATOM   2615 C  CD  . GLN A  1 340 ? 48.477  20.368  57.580 1.00 24.34 ? 530 GLN A CD  1 
ATOM   2616 O  OE1 . GLN A  1 340 ? 47.412  19.748  57.561 1.00 25.83 ? 530 GLN A OE1 1 
ATOM   2617 N  NE2 . GLN A  1 340 ? 48.743  21.305  58.479 1.00 24.16 ? 530 GLN A NE2 1 
ATOM   2618 N  N   . LYS A  1 341 ? 49.973  21.351  52.083 1.00 22.34 ? 531 LYS A N   1 
ATOM   2619 C  CA  . LYS A  1 341 ? 49.500  21.750  50.757 1.00 22.81 ? 531 LYS A CA  1 
ATOM   2620 C  C   . LYS A  1 341 ? 49.692  20.639  49.729 1.00 25.47 ? 531 LYS A C   1 
ATOM   2621 O  O   . LYS A  1 341 ? 48.834  20.406  48.877 1.00 25.33 ? 531 LYS A O   1 
ATOM   2622 C  CB  . LYS A  1 341 ? 50.252  22.990  50.261 1.00 19.46 ? 531 LYS A CB  1 
ATOM   2623 C  CG  . LYS A  1 341 ? 50.134  24.236  51.119 1.00 18.29 ? 531 LYS A CG  1 
ATOM   2624 C  CD  . LYS A  1 341 ? 50.996  25.350  50.523 1.00 17.84 ? 531 LYS A CD  1 
ATOM   2625 C  CE  . LYS A  1 341 ? 50.946  26.621  51.346 1.00 18.67 ? 531 LYS A CE  1 
ATOM   2626 N  NZ  . LYS A  1 341 ? 49.569  27.184  51.399 1.00 24.59 ? 531 LYS A NZ  1 
ATOM   2627 N  N   . GLY A  1 342 ? 50.829  19.960  49.805 1.00 25.35 ? 532 GLY A N   1 
ATOM   2628 C  CA  . GLY A  1 342 ? 51.104  18.903  48.856 1.00 24.18 ? 532 GLY A CA  1 
ATOM   2629 C  C   . GLY A  1 342 ? 51.434  19.496  47.501 1.00 26.18 ? 532 GLY A C   1 
ATOM   2630 O  O   . GLY A  1 342 ? 51.271  18.833  46.476 1.00 26.71 ? 532 GLY A O   1 
ATOM   2631 N  N   . ASN A  1 343 ? 51.892  20.747  47.490 1.00 25.92 ? 533 ASN A N   1 
ATOM   2632 C  CA  . ASN A  1 343 ? 52.245  21.406  46.237 1.00 22.61 ? 533 ASN A CA  1 
ATOM   2633 C  C   . ASN A  1 343 ? 53.672  21.073  45.813 1.00 19.62 ? 533 ASN A C   1 
ATOM   2634 O  O   . ASN A  1 343 ? 54.229  20.056  46.224 1.00 20.08 ? 533 ASN A O   1 
ATOM   2635 C  CB  . ASN A  1 343 ? 52.076  22.927  46.337 1.00 18.96 ? 533 ASN A CB  1 
ATOM   2636 C  CG  . ASN A  1 343 ? 52.893  23.535  47.454 1.00 26.59 ? 533 ASN A CG  1 
ATOM   2637 O  OD1 . ASN A  1 343 ? 53.947  23.017  47.822 1.00 32.92 ? 533 ASN A OD1 1 
ATOM   2638 N  ND2 . ASN A  1 343 ? 52.419  24.654  47.989 1.00 23.91 ? 533 ASN A ND2 1 
ATOM   2639 N  N   . TYR A  1 344 ? 54.267  21.939  45.001 1.00 18.54 ? 534 TYR A N   1 
ATOM   2640 C  CA  . TYR A  1 344 ? 55.611  21.692  44.498 1.00 18.47 ? 534 TYR A CA  1 
ATOM   2641 C  C   . TYR A  1 344 ? 56.735  21.727  45.527 1.00 17.30 ? 534 TYR A C   1 
ATOM   2642 O  O   . TYR A  1 344 ? 57.827  21.230  45.254 1.00 16.53 ? 534 TYR A O   1 
ATOM   2643 C  CB  . TYR A  1 344 ? 55.925  22.658  43.343 1.00 15.29 ? 534 TYR A CB  1 
ATOM   2644 C  CG  . TYR A  1 344 ? 56.230  24.088  43.739 1.00 13.73 ? 534 TYR A CG  1 
ATOM   2645 C  CD1 . TYR A  1 344 ? 57.546  24.507  43.961 1.00 12.08 ? 534 TYR A CD1 1 
ATOM   2646 C  CD2 . TYR A  1 344 ? 55.210  25.033  43.856 1.00 13.62 ? 534 TYR A CD2 1 
ATOM   2647 C  CE1 . TYR A  1 344 ? 57.837  25.834  44.282 1.00 7.89  ? 534 TYR A CE1 1 
ATOM   2648 C  CE2 . TYR A  1 344 ? 55.487  26.364  44.178 1.00 10.33 ? 534 TYR A CE2 1 
ATOM   2649 C  CZ  . TYR A  1 344 ? 56.802  26.758  44.387 1.00 16.08 ? 534 TYR A CZ  1 
ATOM   2650 O  OH  . TYR A  1 344 ? 57.082  28.075  44.690 1.00 18.40 ? 534 TYR A OH  1 
ATOM   2651 N  N   . TYR A  1 345 ? 56.486  22.292  46.706 1.00 11.27 ? 535 TYR A N   1 
ATOM   2652 C  CA  . TYR A  1 345 ? 57.543  22.355  47.711 1.00 14.22 ? 535 TYR A CA  1 
ATOM   2653 C  C   . TYR A  1 345 ? 57.132  21.879  49.108 1.00 14.63 ? 535 TYR A C   1 
ATOM   2654 O  O   . TYR A  1 345 ? 57.967  21.396  49.878 1.00 12.41 ? 535 TYR A O   1 
ATOM   2655 C  CB  . TYR A  1 345 ? 58.106  23.782  47.785 1.00 12.38 ? 535 TYR A CB  1 
ATOM   2656 C  CG  . TYR A  1 345 ? 57.209  24.781  48.477 1.00 14.46 ? 535 TYR A CG  1 
ATOM   2657 C  CD1 . TYR A  1 345 ? 57.040  24.749  49.863 1.00 17.22 ? 535 TYR A CD1 1 
ATOM   2658 C  CD2 . TYR A  1 345 ? 56.517  25.753  47.751 1.00 13.35 ? 535 TYR A CD2 1 
ATOM   2659 C  CE1 . TYR A  1 345 ? 56.205  25.653  50.510 1.00 22.69 ? 535 TYR A CE1 1 
ATOM   2660 C  CE2 . TYR A  1 345 ? 55.676  26.667  48.392 1.00 13.17 ? 535 TYR A CE2 1 
ATOM   2661 C  CZ  . TYR A  1 345 ? 55.526  26.607  49.771 1.00 16.10 ? 535 TYR A CZ  1 
ATOM   2662 O  OH  . TYR A  1 345 ? 54.700  27.490  50.424 1.00 22.05 ? 535 TYR A OH  1 
ATOM   2663 N  N   . GLY A  1 346 ? 55.851  22.017  49.433 1.00 10.10 ? 536 GLY A N   1 
ATOM   2664 C  CA  . GLY A  1 346 ? 55.377  21.603  50.736 1.00 8.95  ? 536 GLY A CA  1 
ATOM   2665 C  C   . GLY A  1 346 ? 54.740  20.229  50.740 1.00 18.11 ? 536 GLY A C   1 
ATOM   2666 O  O   . GLY A  1 346 ? 53.515  20.102  50.711 1.00 23.20 ? 536 GLY A O   1 
ATOM   2667 N  N   . TYR A  1 347 ? 55.573  19.196  50.769 1.00 20.91 ? 537 TYR A N   1 
ATOM   2668 C  CA  . TYR A  1 347 ? 55.091  17.822  50.801 1.00 22.62 ? 537 TYR A CA  1 
ATOM   2669 C  C   . TYR A  1 347 ? 55.916  17.041  51.809 1.00 20.99 ? 537 TYR A C   1 
ATOM   2670 O  O   . TYR A  1 347 ? 56.846  17.586  52.395 1.00 26.44 ? 537 TYR A O   1 
ATOM   2671 C  CB  . TYR A  1 347 ? 55.186  17.188  49.410 1.00 24.17 ? 537 TYR A CB  1 
ATOM   2672 C  CG  . TYR A  1 347 ? 56.551  17.264  48.769 1.00 25.83 ? 537 TYR A CG  1 
ATOM   2673 C  CD1 . TYR A  1 347 ? 57.454  16.206  48.872 1.00 29.15 ? 537 TYR A CD1 1 
ATOM   2674 C  CD2 . TYR A  1 347 ? 56.935  18.390  48.041 1.00 26.00 ? 537 TYR A CD2 1 
ATOM   2675 C  CE1 . TYR A  1 347 ? 58.705  16.267  48.260 1.00 26.73 ? 537 TYR A CE1 1 
ATOM   2676 C  CE2 . TYR A  1 347 ? 58.182  18.461  47.430 1.00 25.53 ? 537 TYR A CE2 1 
ATOM   2677 C  CZ  . TYR A  1 347 ? 59.060  17.399  47.542 1.00 26.49 ? 537 TYR A CZ  1 
ATOM   2678 O  OH  . TYR A  1 347 ? 60.293  17.473  46.936 1.00 30.37 ? 537 TYR A OH  1 
ATOM   2679 N  N   . CYS A  1 348 ? 55.578  15.774  52.020 1.00 21.76 ? 538 CYS A N   1 
ATOM   2680 C  CA  . CYS A  1 348 ? 56.302  14.949  52.982 1.00 24.12 ? 538 CYS A CA  1 
ATOM   2681 C  C   . CYS A  1 348 ? 57.188  13.884  52.354 1.00 24.99 ? 538 CYS A C   1 
ATOM   2682 O  O   . CYS A  1 348 ? 58.250  13.560  52.881 1.00 26.14 ? 538 CYS A O   1 
ATOM   2683 C  CB  . CYS A  1 348 ? 55.318  14.283  53.952 1.00 26.04 ? 538 CYS A CB  1 
ATOM   2684 S  SG  . CYS A  1 348 ? 55.472  14.945  55.639 1.00 27.13 ? 538 CYS A SG  1 
ATOM   2685 N  N   . ARG A  1 349 ? 56.752  13.348  51.223 1.00 26.29 ? 539 ARG A N   1 
ATOM   2686 C  CA  . ARG A  1 349 ? 57.495  12.299  50.543 1.00 25.59 ? 539 ARG A CA  1 
ATOM   2687 C  C   . ARG A  1 349 ? 56.962  12.145  49.130 1.00 27.53 ? 539 ARG A C   1 
ATOM   2688 O  O   . ARG A  1 349 ? 55.979  12.791  48.759 1.00 25.88 ? 539 ARG A O   1 
ATOM   2689 C  CB  . ARG A  1 349 ? 57.327  10.984  51.306 1.00 26.67 ? 539 ARG A CB  1 
ATOM   2690 C  CG  . ARG A  1 349 ? 55.891  10.737  51.734 1.00 29.12 ? 539 ARG A CG  1 
ATOM   2691 C  CD  . ARG A  1 349 ? 55.726  9.451   52.518 1.00 36.27 ? 539 ARG A CD  1 
ATOM   2692 N  NE  . ARG A  1 349 ? 54.375  9.347   53.063 1.00 38.11 ? 539 ARG A NE  1 
ATOM   2693 C  CZ  . ARG A  1 349 ? 53.912  10.089  54.066 1.00 38.21 ? 539 ARG A CZ  1 
ATOM   2694 N  NH1 . ARG A  1 349 ? 54.695  10.990  54.646 1.00 29.18 ? 539 ARG A NH1 1 
ATOM   2695 N  NH2 . ARG A  1 349 ? 52.657  9.943   54.478 1.00 40.11 ? 539 ARG A NH2 1 
ATOM   2696 N  N   . LYS A  1 350 ? 57.610  11.287  48.347 1.00 25.80 ? 540 LYS A N   1 
ATOM   2697 C  CA  . LYS A  1 350 ? 57.186  11.055  46.976 1.00 30.80 ? 540 LYS A CA  1 
ATOM   2698 C  C   . LYS A  1 350 ? 56.827  9.597   46.684 1.00 36.92 ? 540 LYS A C   1 
ATOM   2699 O  O   . LYS A  1 350 ? 57.563  8.677   47.041 1.00 38.11 ? 540 LYS A O   1 
ATOM   2700 C  CB  . LYS A  1 350 ? 58.267  11.537  46.006 1.00 28.46 ? 540 LYS A CB  1 
ATOM   2701 C  CG  . LYS A  1 350 ? 58.401  13.053  45.953 1.00 28.23 ? 540 LYS A CG  1 
ATOM   2702 C  CD  . LYS A  1 350 ? 58.641  13.536  44.528 1.00 27.15 ? 540 LYS A CD  1 
ATOM   2703 C  CE  . LYS A  1 350 ? 60.115  13.541  44.157 1.00 23.47 ? 540 LYS A CE  1 
ATOM   2704 N  NZ  . LYS A  1 350 ? 60.823  14.690  44.787 1.00 22.97 ? 540 LYS A NZ  1 
ATOM   2705 N  N   . GLU A  1 351 ? 55.679  9.403   46.036 1.00 42.11 ? 541 GLU A N   1 
ATOM   2706 C  CA  . GLU A  1 351 ? 55.192  8.076   45.672 1.00 43.02 ? 541 GLU A CA  1 
ATOM   2707 C  C   . GLU A  1 351 ? 55.234  7.915   44.156 1.00 44.61 ? 541 GLU A C   1 
ATOM   2708 O  O   . GLU A  1 351 ? 54.442  8.526   43.436 1.00 40.96 ? 541 GLU A O   1 
ATOM   2709 C  CB  . GLU A  1 351 ? 53.748  7.881   46.146 1.00 47.82 ? 541 GLU A CB  1 
ATOM   2710 C  CG  . GLU A  1 351 ? 53.530  8.052   47.639 1.00 53.82 ? 541 GLU A CG  1 
ATOM   2711 C  CD  . GLU A  1 351 ? 54.182  6.964   48.462 1.00 56.27 ? 541 GLU A CD  1 
ATOM   2712 O  OE1 . GLU A  1 351 ? 55.412  6.787   48.349 1.00 62.54 ? 541 GLU A OE1 1 
ATOM   2713 O  OE2 . GLU A  1 351 ? 53.461  6.288   49.225 1.00 56.26 ? 541 GLU A OE2 1 
ATOM   2714 N  N   . ASN A  1 352 ? 56.160  7.089   43.680 1.00 45.76 ? 542 ASN A N   1 
ATOM   2715 C  CA  . ASN A  1 352 ? 56.311  6.836   42.251 1.00 44.86 ? 542 ASN A CA  1 
ATOM   2716 C  C   . ASN A  1 352 ? 56.370  8.114   41.423 1.00 42.71 ? 542 ASN A C   1 
ATOM   2717 O  O   . ASN A  1 352 ? 56.146  8.086   40.213 1.00 43.50 ? 542 ASN A O   1 
ATOM   2718 C  CB  . ASN A  1 352 ? 55.168  5.951   41.751 1.00 44.65 ? 542 ASN A CB  1 
ATOM   2719 C  CG  . ASN A  1 352 ? 55.205  4.561   42.352 1.00 49.83 ? 542 ASN A CG  1 
ATOM   2720 O  OD1 . ASN A  1 352 ? 56.144  3.798   42.121 1.00 47.70 ? 542 ASN A OD1 1 
ATOM   2721 N  ND2 . ASN A  1 352 ? 54.183  4.225   43.133 1.00 52.11 ? 542 ASN A ND2 1 
ATOM   2722 N  N   . GLY A  1 353 ? 56.670  9.233   42.075 1.00 40.26 ? 543 GLY A N   1 
ATOM   2723 C  CA  . GLY A  1 353 ? 56.763  10.492  41.361 1.00 38.26 ? 543 GLY A CA  1 
ATOM   2724 C  C   . GLY A  1 353 ? 55.778  11.548  41.814 1.00 35.49 ? 543 GLY A C   1 
ATOM   2725 O  O   . GLY A  1 353 ? 55.914  12.719  41.457 1.00 36.39 ? 543 GLY A O   1 
ATOM   2726 N  N   . ASN A  1 354 ? 54.784  11.140  42.595 1.00 32.90 ? 544 ASN A N   1 
ATOM   2727 C  CA  . ASN A  1 354 ? 53.777  12.072  43.095 1.00 28.86 ? 544 ASN A CA  1 
ATOM   2728 C  C   . ASN A  1 354 ? 54.201  12.600  44.461 1.00 24.92 ? 544 ASN A C   1 
ATOM   2729 O  O   . ASN A  1 354 ? 54.714  11.850  45.292 1.00 22.73 ? 544 ASN A O   1 
ATOM   2730 C  CB  . ASN A  1 354 ? 52.419  11.373  43.217 1.00 29.21 ? 544 ASN A CB  1 
ATOM   2731 C  CG  . ASN A  1 354 ? 52.013  10.659  41.942 1.00 32.85 ? 544 ASN A CG  1 
ATOM   2732 O  OD1 . ASN A  1 354 ? 51.829  11.283  40.896 1.00 32.01 ? 544 ASN A OD1 1 
ATOM   2733 N  ND2 . ASN A  1 354 ? 51.875  9.339   42.023 1.00 32.51 ? 544 ASN A ND2 1 
ATOM   2734 N  N   . LYS A  1 355 ? 53.998  13.892  44.688 1.00 21.14 ? 545 LYS A N   1 
ATOM   2735 C  CA  . LYS A  1 355 ? 54.354  14.493  45.966 1.00 21.34 ? 545 LYS A CA  1 
ATOM   2736 C  C   . LYS A  1 355 ? 53.194  14.295  46.931 1.00 21.63 ? 545 LYS A C   1 
ATOM   2737 O  O   . LYS A  1 355 ? 52.071  14.707  46.652 1.00 23.10 ? 545 LYS A O   1 
ATOM   2738 C  CB  . LYS A  1 355 ? 54.648  15.985  45.789 1.00 20.39 ? 545 LYS A CB  1 
ATOM   2739 C  CG  . LYS A  1 355 ? 55.830  16.254  44.878 1.00 24.19 ? 545 LYS A CG  1 
ATOM   2740 C  CD  . LYS A  1 355 ? 56.014  17.731  44.595 1.00 26.47 ? 545 LYS A CD  1 
ATOM   2741 C  CE  . LYS A  1 355 ? 57.236  17.959  43.707 1.00 25.45 ? 545 LYS A CE  1 
ATOM   2742 N  NZ  . LYS A  1 355 ? 57.439  19.403  43.390 1.00 26.37 ? 545 LYS A NZ  1 
ATOM   2743 N  N   . ILE A  1 356 ? 53.469  13.650  48.059 1.00 20.39 ? 546 ILE A N   1 
ATOM   2744 C  CA  . ILE A  1 356 ? 52.443  13.396  49.057 1.00 15.25 ? 546 ILE A CA  1 
ATOM   2745 C  C   . ILE A  1 356 ? 52.459  14.468  50.131 1.00 14.90 ? 546 ILE A C   1 
ATOM   2746 O  O   . ILE A  1 356 ? 53.505  14.789  50.683 1.00 21.34 ? 546 ILE A O   1 
ATOM   2747 C  CB  . ILE A  1 356 ? 52.655  12.036  49.733 1.00 19.90 ? 546 ILE A CB  1 
ATOM   2748 C  CG1 . ILE A  1 356 ? 52.761  10.943  48.670 1.00 22.47 ? 546 ILE A CG1 1 
ATOM   2749 C  CG2 . ILE A  1 356 ? 51.503  11.741  50.681 1.00 17.00 ? 546 ILE A CG2 1 
ATOM   2750 C  CD1 . ILE A  1 356 ? 51.568  10.869  47.738 1.00 21.83 ? 546 ILE A CD1 1 
ATOM   2751 N  N   . PRO A  1 357 ? 51.290  15.035  50.448 1.00 14.94 ? 547 PRO A N   1 
ATOM   2752 C  CA  . PRO A  1 357 ? 51.214  16.075  51.473 1.00 15.65 ? 547 PRO A CA  1 
ATOM   2753 C  C   . PRO A  1 357 ? 51.486  15.520  52.869 1.00 19.27 ? 547 PRO A C   1 
ATOM   2754 O  O   . PRO A  1 357 ? 51.276  14.334  53.127 1.00 22.77 ? 547 PRO A O   1 
ATOM   2755 C  CB  . PRO A  1 357 ? 49.786  16.586  51.326 1.00 14.65 ? 547 PRO A CB  1 
ATOM   2756 C  CG  . PRO A  1 357 ? 49.044  15.345  50.953 1.00 5.34  ? 547 PRO A CG  1 
ATOM   2757 C  CD  . PRO A  1 357 ? 49.951  14.736  49.910 1.00 11.60 ? 547 PRO A CD  1 
ATOM   2758 N  N   . CYS A  1 358 ? 51.962  16.379  53.764 1.00 19.73 ? 548 CYS A N   1 
ATOM   2759 C  CA  . CYS A  1 358 ? 52.232  15.968  55.134 1.00 19.80 ? 548 CYS A CA  1 
ATOM   2760 C  C   . CYS A  1 358 ? 50.940  15.965  55.934 1.00 18.80 ? 548 CYS A C   1 
ATOM   2761 O  O   . CYS A  1 358 ? 50.154  16.908  55.863 1.00 17.55 ? 548 CYS A O   1 
ATOM   2762 C  CB  . CYS A  1 358 ? 53.181  16.938  55.833 1.00 23.30 ? 548 CYS A CB  1 
ATOM   2763 S  SG  . CYS A  1 358 ? 54.940  16.889  55.398 1.00 24.32 ? 548 CYS A SG  1 
ATOM   2764 N  N   . ALA A  1 359 ? 50.721  14.907  56.701 1.00 20.29 ? 549 ALA A N   1 
ATOM   2765 C  CA  . ALA A  1 359 ? 49.542  14.846  57.543 1.00 18.39 ? 549 ALA A CA  1 
ATOM   2766 C  C   . ALA A  1 359 ? 49.875  15.785  58.692 1.00 17.67 ? 549 ALA A C   1 
ATOM   2767 O  O   . ALA A  1 359 ? 51.046  16.007  58.997 1.00 12.72 ? 549 ALA A O   1 
ATOM   2768 C  CB  . ALA A  1 359 ? 49.334  13.437  58.059 1.00 20.88 ? 549 ALA A CB  1 
ATOM   2769 N  N   . PRO A  1 360 ? 48.855  16.361  59.338 1.00 22.89 ? 550 PRO A N   1 
ATOM   2770 C  CA  . PRO A  1 360 ? 49.083  17.281  60.458 1.00 28.03 ? 550 PRO A CA  1 
ATOM   2771 C  C   . PRO A  1 360 ? 50.199  16.844  61.417 1.00 30.99 ? 550 PRO A C   1 
ATOM   2772 O  O   . PRO A  1 360 ? 50.975  17.669  61.896 1.00 34.59 ? 550 PRO A O   1 
ATOM   2773 C  CB  . PRO A  1 360 ? 47.717  17.325  61.132 1.00 28.14 ? 550 PRO A CB  1 
ATOM   2774 C  CG  . PRO A  1 360 ? 46.785  17.251  59.950 1.00 21.36 ? 550 PRO A CG  1 
ATOM   2775 C  CD  . PRO A  1 360 ? 47.412  16.169  59.095 1.00 20.59 ? 550 PRO A CD  1 
ATOM   2776 N  N   . GLU A  1 361 ? 50.284  15.543  61.677 1.00 32.14 ? 551 GLU A N   1 
ATOM   2777 C  CA  . GLU A  1 361 ? 51.289  15.000  62.585 1.00 28.71 ? 551 GLU A CA  1 
ATOM   2778 C  C   . GLU A  1 361 ? 52.718  15.027  62.039 1.00 27.80 ? 551 GLU A C   1 
ATOM   2779 O  O   . GLU A  1 361 ? 53.650  15.393  62.751 1.00 33.37 ? 551 GLU A O   1 
ATOM   2780 C  CB  . GLU A  1 361 ? 50.939  13.553  62.964 1.00 27.61 ? 551 GLU A CB  1 
ATOM   2781 C  CG  . GLU A  1 361 ? 49.490  13.316  63.395 1.00 38.87 ? 551 GLU A CG  1 
ATOM   2782 C  CD  . GLU A  1 361 ? 48.533  13.142  62.217 1.00 42.12 ? 551 GLU A CD  1 
ATOM   2783 O  OE1 . GLU A  1 361 ? 47.321  12.937  62.449 1.00 39.93 ? 551 GLU A OE1 1 
ATOM   2784 O  OE2 . GLU A  1 361 ? 48.990  13.203  61.057 1.00 48.41 ? 551 GLU A OE2 1 
ATOM   2785 N  N   . ASP A  1 362 ? 52.890  14.641  60.778 1.00 25.06 ? 552 ASP A N   1 
ATOM   2786 C  CA  . ASP A  1 362 ? 54.217  14.584  60.163 1.00 21.41 ? 552 ASP A CA  1 
ATOM   2787 C  C   . ASP A  1 362 ? 54.730  15.899  59.574 1.00 18.42 ? 552 ASP A C   1 
ATOM   2788 O  O   . ASP A  1 362 ? 55.751  15.930  58.885 1.00 12.98 ? 552 ASP A O   1 
ATOM   2789 C  CB  . ASP A  1 362 ? 54.219  13.510  59.081 1.00 22.66 ? 552 ASP A CB  1 
ATOM   2790 C  CG  . ASP A  1 362 ? 53.664  12.195  59.575 1.00 26.66 ? 552 ASP A CG  1 
ATOM   2791 O  OD1 . ASP A  1 362 ? 54.149  11.707  60.618 1.00 30.18 ? 552 ASP A OD1 1 
ATOM   2792 O  OD2 . ASP A  1 362 ? 52.745  11.651  58.925 1.00 26.91 ? 552 ASP A OD2 1 
ATOM   2793 N  N   . VAL A  1 363 ? 54.020  16.981  59.860 1.00 16.66 ? 553 VAL A N   1 
ATOM   2794 C  CA  . VAL A  1 363 ? 54.369  18.302  59.365 1.00 10.82 ? 553 VAL A CA  1 
ATOM   2795 C  C   . VAL A  1 363 ? 55.856  18.656  59.453 1.00 14.64 ? 553 VAL A C   1 
ATOM   2796 O  O   . VAL A  1 363 ? 56.430  19.173  58.495 1.00 19.71 ? 553 VAL A O   1 
ATOM   2797 C  CB  . VAL A  1 363 ? 53.524  19.364  60.099 1.00 7.33  ? 553 VAL A CB  1 
ATOM   2798 C  CG1 . VAL A  1 363 ? 54.318  20.619  60.318 1.00 3.45  ? 553 VAL A CG1 1 
ATOM   2799 C  CG2 . VAL A  1 363 ? 52.279  19.667  59.288 1.00 3.36  ? 553 VAL A CG2 1 
ATOM   2800 N  N   . LYS A  1 364 ? 56.479  18.374  60.593 1.00 16.51 ? 554 LYS A N   1 
ATOM   2801 C  CA  . LYS A  1 364 ? 57.894  18.684  60.798 1.00 14.81 ? 554 LYS A CA  1 
ATOM   2802 C  C   . LYS A  1 364 ? 58.880  17.799  60.033 1.00 17.78 ? 554 LYS A C   1 
ATOM   2803 O  O   . LYS A  1 364 ? 60.091  17.963  60.172 1.00 21.20 ? 554 LYS A O   1 
ATOM   2804 C  CB  . LYS A  1 364 ? 58.231  18.610  62.288 1.00 15.47 ? 554 LYS A CB  1 
ATOM   2805 C  CG  . LYS A  1 364 ? 57.601  19.693  63.141 1.00 17.51 ? 554 LYS A CG  1 
ATOM   2806 C  CD  . LYS A  1 364 ? 58.310  21.022  62.957 1.00 23.78 ? 554 LYS A CD  1 
ATOM   2807 C  CE  . LYS A  1 364 ? 57.769  22.062  63.924 1.00 30.49 ? 554 LYS A CE  1 
ATOM   2808 N  NZ  . LYS A  1 364 ? 57.939  21.644  65.345 1.00 32.16 ? 554 LYS A NZ  1 
ATOM   2809 N  N   . CYS A  1 365 ? 58.380  16.862  59.234 1.00 18.54 ? 555 CYS A N   1 
ATOM   2810 C  CA  . CYS A  1 365 ? 59.270  15.983  58.483 1.00 21.25 ? 555 CYS A CA  1 
ATOM   2811 C  C   . CYS A  1 365 ? 59.249  16.212  56.980 1.00 19.38 ? 555 CYS A C   1 
ATOM   2812 O  O   . CYS A  1 365 ? 59.823  15.428  56.226 1.00 15.94 ? 555 CYS A O   1 
ATOM   2813 C  CB  . CYS A  1 365 ? 58.949  14.514  58.773 1.00 24.89 ? 555 CYS A CB  1 
ATOM   2814 S  SG  . CYS A  1 365 ? 59.308  14.016  60.486 1.00 33.80 ? 555 CYS A SG  1 
ATOM   2815 N  N   . GLY A  1 366 ? 58.586  17.279  56.544 1.00 19.46 ? 556 GLY A N   1 
ATOM   2816 C  CA  . GLY A  1 366 ? 58.532  17.572  55.123 1.00 17.73 ? 556 GLY A CA  1 
ATOM   2817 C  C   . GLY A  1 366 ? 59.585  18.596  54.741 1.00 19.41 ? 556 GLY A C   1 
ATOM   2818 O  O   . GLY A  1 366 ? 60.776  18.413  55.010 1.00 15.31 ? 556 GLY A O   1 
ATOM   2819 N  N   . ARG A  1 367 ? 59.141  19.677  54.109 1.00 16.48 ? 557 ARG A N   1 
ATOM   2820 C  CA  . ARG A  1 367 ? 60.030  20.754  53.697 1.00 12.21 ? 557 ARG A CA  1 
ATOM   2821 C  C   . ARG A  1 367 ? 60.494  21.462  54.962 1.00 12.53 ? 557 ARG A C   1 
ATOM   2822 O  O   . ARG A  1 367 ? 59.732  21.592  55.915 1.00 13.09 ? 557 ARG A O   1 
ATOM   2823 C  CB  . ARG A  1 367 ? 59.270  21.735  52.792 1.00 12.51 ? 557 ARG A CB  1 
ATOM   2824 C  CG  . ARG A  1 367 ? 60.072  22.930  52.276 1.00 3.08  ? 557 ARG A CG  1 
ATOM   2825 C  CD  . ARG A  1 367 ? 61.173  22.516  51.308 1.00 8.44  ? 557 ARG A CD  1 
ATOM   2826 N  NE  . ARG A  1 367 ? 60.667  21.704  50.205 1.00 6.01  ? 557 ARG A NE  1 
ATOM   2827 C  CZ  . ARG A  1 367 ? 61.424  21.215  49.227 1.00 6.20  ? 557 ARG A CZ  1 
ATOM   2828 N  NH1 . ARG A  1 367 ? 62.728  21.459  49.208 1.00 4.76  ? 557 ARG A NH1 1 
ATOM   2829 N  NH2 . ARG A  1 367 ? 60.879  20.468  48.276 1.00 9.98  ? 557 ARG A NH2 1 
ATOM   2830 N  N   . LEU A  1 368 ? 61.748  21.899  54.977 1.00 15.21 ? 558 LEU A N   1 
ATOM   2831 C  CA  . LEU A  1 368 ? 62.298  22.607  56.127 1.00 12.91 ? 558 LEU A CA  1 
ATOM   2832 C  C   . LEU A  1 368 ? 62.085  24.112  55.984 1.00 13.08 ? 558 LEU A C   1 
ATOM   2833 O  O   . LEU A  1 368 ? 62.321  24.679  54.917 1.00 14.91 ? 558 LEU A O   1 
ATOM   2834 C  CB  . LEU A  1 368 ? 63.795  22.327  56.254 1.00 14.80 ? 558 LEU A CB  1 
ATOM   2835 C  CG  . LEU A  1 368 ? 64.582  23.289  57.155 1.00 14.68 ? 558 LEU A CG  1 
ATOM   2836 C  CD1 . LEU A  1 368 ? 64.117  23.159  58.600 1.00 12.67 ? 558 LEU A CD1 1 
ATOM   2837 C  CD2 . LEU A  1 368 ? 66.062  22.987  57.042 1.00 13.30 ? 558 LEU A CD2 1 
ATOM   2838 N  N   . TYR A  1 369 ? 61.640  24.753  57.059 1.00 12.60 ? 559 TYR A N   1 
ATOM   2839 C  CA  . TYR A  1 369 ? 61.418  26.196  57.055 1.00 9.38  ? 559 TYR A CA  1 
ATOM   2840 C  C   . TYR A  1 369 ? 62.311  26.834  58.111 1.00 13.98 ? 559 TYR A C   1 
ATOM   2841 O  O   . TYR A  1 369 ? 62.502  26.275  59.189 1.00 14.43 ? 559 TYR A O   1 
ATOM   2842 C  CB  . TYR A  1 369 ? 59.948  26.515  57.342 1.00 11.02 ? 559 TYR A CB  1 
ATOM   2843 C  CG  . TYR A  1 369 ? 59.000  25.907  56.338 1.00 18.29 ? 559 TYR A CG  1 
ATOM   2844 C  CD1 . TYR A  1 369 ? 58.530  24.604  56.494 1.00 19.74 ? 559 TYR A CD1 1 
ATOM   2845 C  CD2 . TYR A  1 369 ? 58.615  26.615  55.200 1.00 22.07 ? 559 TYR A CD2 1 
ATOM   2846 C  CE1 . TYR A  1 369 ? 57.701  24.019  55.539 1.00 24.87 ? 559 TYR A CE1 1 
ATOM   2847 C  CE2 . TYR A  1 369 ? 57.789  26.039  54.236 1.00 23.95 ? 559 TYR A CE2 1 
ATOM   2848 C  CZ  . TYR A  1 369 ? 57.337  24.741  54.411 1.00 27.07 ? 559 TYR A CZ  1 
ATOM   2849 O  OH  . TYR A  1 369 ? 56.528  24.164  53.455 1.00 24.45 ? 559 TYR A OH  1 
ATOM   2850 N  N   . CYS A  1 370 ? 62.860  28.003  57.802 1.00 15.80 ? 560 CYS A N   1 
ATOM   2851 C  CA  . CYS A  1 370 ? 63.749  28.681  58.734 1.00 23.58 ? 560 CYS A CA  1 
ATOM   2852 C  C   . CYS A  1 370 ? 63.416  30.170  58.872 1.00 28.15 ? 560 CYS A C   1 
ATOM   2853 O  O   . CYS A  1 370 ? 62.881  30.781  57.948 1.00 31.57 ? 560 CYS A O   1 
ATOM   2854 C  CB  . CYS A  1 370 ? 65.196  28.497  58.270 1.00 20.26 ? 560 CYS A CB  1 
ATOM   2855 S  SG  . CYS A  1 370 ? 65.645  26.765  57.896 1.00 24.54 ? 560 CYS A SG  1 
ATOM   2856 N  N   . LYS A  1 371 ? 63.730  30.747  60.030 1.00 32.61 ? 561 LYS A N   1 
ATOM   2857 C  CA  . LYS A  1 371 ? 63.450  32.159  60.286 1.00 37.27 ? 561 LYS A CA  1 
ATOM   2858 C  C   . LYS A  1 371 ? 64.706  33.024  60.195 1.00 37.70 ? 561 LYS A C   1 
ATOM   2859 O  O   . LYS A  1 371 ? 65.762  32.669  60.720 1.00 33.34 ? 561 LYS A O   1 
ATOM   2860 C  CB  . LYS A  1 371 ? 62.816  32.337  61.674 1.00 38.45 ? 561 LYS A CB  1 
ATOM   2861 C  CG  . LYS A  1 371 ? 63.782  32.101  62.827 1.00 44.57 ? 561 LYS A CG  1 
ATOM   2862 C  CD  . LYS A  1 371 ? 63.194  32.496  64.176 1.00 44.74 ? 561 LYS A CD  1 
ATOM   2863 C  CE  . LYS A  1 371 ? 62.097  31.546  64.620 1.00 49.43 ? 561 LYS A CE  1 
ATOM   2864 N  NZ  . LYS A  1 371 ? 61.612  31.875  65.991 1.00 50.73 ? 561 LYS A NZ  1 
ATOM   2865 N  N   . ASP A  1 372 ? 64.581  34.165  59.527 1.00 43.01 ? 562 ASP A N   1 
ATOM   2866 C  CA  . ASP A  1 372 ? 65.701  35.085  59.371 1.00 49.06 ? 562 ASP A CA  1 
ATOM   2867 C  C   . ASP A  1 372 ? 65.571  36.216  60.392 1.00 50.26 ? 562 ASP A C   1 
ATOM   2868 O  O   . ASP A  1 372 ? 64.622  37.006  60.350 1.00 47.53 ? 562 ASP A O   1 
ATOM   2869 C  CB  . ASP A  1 372 ? 65.718  35.651  57.950 1.00 53.98 ? 562 ASP A CB  1 
ATOM   2870 C  CG  . ASP A  1 372 ? 66.954  36.476  57.668 1.00 57.39 ? 562 ASP A CG  1 
ATOM   2871 O  OD1 . ASP A  1 372 ? 67.204  37.436  58.424 1.00 62.28 ? 562 ASP A OD1 1 
ATOM   2872 O  OD2 . ASP A  1 372 ? 67.672  36.169  56.692 1.00 56.59 ? 562 ASP A OD2 1 
ATOM   2873 N  N   . ASN A  1 373 ? 66.537  36.292  61.302 1.00 47.61 ? 563 ASN A N   1 
ATOM   2874 C  CA  . ASN A  1 373 ? 66.526  37.303  62.353 1.00 45.34 ? 563 ASN A CA  1 
ATOM   2875 C  C   . ASN A  1 373 ? 67.312  38.568  61.998 1.00 43.24 ? 563 ASN A C   1 
ATOM   2876 O  O   . ASN A  1 373 ? 67.880  39.215  62.877 1.00 44.45 ? 563 ASN A O   1 
ATOM   2877 C  CB  . ASN A  1 373 ? 67.086  36.699  63.643 1.00 46.62 ? 563 ASN A CB  1 
ATOM   2878 C  CG  . ASN A  1 373 ? 66.707  37.495  64.873 1.00 48.17 ? 563 ASN A CG  1 
ATOM   2879 O  OD1 . ASN A  1 373 ? 65.546  37.502  65.288 1.00 48.35 ? 563 ASN A OD1 1 
ATOM   2880 N  ND2 . ASN A  1 373 ? 67.684  38.176  65.463 1.00 49.19 ? 563 ASN A ND2 1 
ATOM   2881 N  N   . SER A  1 374 ? 67.343  38.922  60.717 1.00 38.68 ? 564 SER A N   1 
ATOM   2882 C  CA  . SER A  1 374 ? 68.062  40.115  60.284 1.00 34.12 ? 564 SER A CA  1 
ATOM   2883 C  C   . SER A  1 374 ? 67.113  41.309  60.259 1.00 33.66 ? 564 SER A C   1 
ATOM   2884 O  O   . SER A  1 374 ? 65.897  41.146  60.343 1.00 39.41 ? 564 SER A O   1 
ATOM   2885 C  CB  . SER A  1 374 ? 68.659  39.899  58.892 1.00 35.03 ? 564 SER A CB  1 
ATOM   2886 O  OG  . SER A  1 374 ? 67.643  39.797  57.909 1.00 38.56 ? 564 SER A OG  1 
ATOM   2887 N  N   . PRO A  1 375 ? 67.657  42.529  60.146 1.00 34.16 ? 565 PRO A N   1 
ATOM   2888 C  CA  . PRO A  1 375 ? 66.841  43.749  60.116 1.00 34.00 ? 565 PRO A CA  1 
ATOM   2889 C  C   . PRO A  1 375 ? 65.926  43.874  58.902 1.00 38.28 ? 565 PRO A C   1 
ATOM   2890 O  O   . PRO A  1 375 ? 66.361  43.680  57.767 1.00 43.52 ? 565 PRO A O   1 
ATOM   2891 C  CB  . PRO A  1 375 ? 67.885  44.862  60.155 1.00 30.58 ? 565 PRO A CB  1 
ATOM   2892 C  CG  . PRO A  1 375 ? 69.018  44.233  60.908 1.00 28.90 ? 565 PRO A CG  1 
ATOM   2893 C  CD  . PRO A  1 375 ? 69.084  42.867  60.282 1.00 29.37 ? 565 PRO A CD  1 
ATOM   2894 N  N   . GLY A  1 376 ? 64.661  44.200  59.157 1.00 42.55 ? 566 GLY A N   1 
ATOM   2895 C  CA  . GLY A  1 376 ? 63.683  44.373  58.095 1.00 48.07 ? 566 GLY A CA  1 
ATOM   2896 C  C   . GLY A  1 376 ? 63.374  43.187  57.195 1.00 54.76 ? 566 GLY A C   1 
ATOM   2897 O  O   . GLY A  1 376 ? 62.439  43.256  56.395 1.00 55.03 ? 566 GLY A O   1 
ATOM   2898 N  N   . GLN A  1 377 ? 64.145  42.106  57.322 1.00 61.39 ? 567 GLN A N   1 
ATOM   2899 C  CA  . GLN A  1 377 ? 63.971  40.898  56.505 1.00 61.15 ? 567 GLN A CA  1 
ATOM   2900 C  C   . GLN A  1 377 ? 62.499  40.613  56.196 1.00 61.71 ? 567 GLN A C   1 
ATOM   2901 O  O   . GLN A  1 377 ? 62.096  40.605  55.032 1.00 63.75 ? 567 GLN A O   1 
ATOM   2902 C  CB  . GLN A  1 377 ? 64.599  39.696  57.214 1.00 64.35 ? 567 GLN A CB  1 
ATOM   2903 C  CG  . GLN A  1 377 ? 65.061  38.588  56.274 1.00 69.31 ? 567 GLN A CG  1 
ATOM   2904 C  CD  . GLN A  1 377 ? 63.919  37.931  55.527 1.00 68.92 ? 567 GLN A CD  1 
ATOM   2905 O  OE1 . GLN A  1 377 ? 63.003  37.381  56.136 1.00 71.43 ? 567 GLN A OE1 1 
ATOM   2906 N  NE2 . GLN A  1 377 ? 63.969  37.981  54.199 1.00 68.85 ? 567 GLN A NE2 1 
ATOM   2907 N  N   . ASN A  1 378 ? 61.713  40.362  57.240 1.00 58.73 ? 568 ASN A N   1 
ATOM   2908 C  CA  . ASN A  1 378 ? 60.279  40.120  57.103 1.00 57.99 ? 568 ASN A CA  1 
ATOM   2909 C  C   . ASN A  1 378 ? 59.808  38.690  56.804 1.00 54.30 ? 568 ASN A C   1 
ATOM   2910 O  O   . ASN A  1 378 ? 58.734  38.300  57.265 1.00 57.51 ? 568 ASN A O   1 
ATOM   2911 C  CB  . ASN A  1 378 ? 59.691  41.083  56.058 1.00 63.12 ? 568 ASN A CB  1 
ATOM   2912 C  CG  . ASN A  1 378 ? 58.175  41.015  55.980 1.00 66.67 ? 568 ASN A CG  1 
ATOM   2913 O  OD1 . ASN A  1 378 ? 57.477  41.287  56.959 1.00 69.43 ? 568 ASN A OD1 1 
ATOM   2914 N  ND2 . ASN A  1 378 ? 57.657  40.655  54.808 1.00 64.15 ? 568 ASN A ND2 1 
ATOM   2915 N  N   . ASN A  1 379 ? 60.576  37.907  56.045 1.00 43.12 ? 569 ASN A N   1 
ATOM   2916 C  CA  . ASN A  1 379 ? 60.155  36.533  55.731 1.00 37.57 ? 569 ASN A CA  1 
ATOM   2917 C  C   . ASN A  1 379 ? 60.369  35.565  56.898 1.00 30.90 ? 569 ASN A C   1 
ATOM   2918 O  O   . ASN A  1 379 ? 61.502  35.214  57.228 1.00 27.73 ? 569 ASN A O   1 
ATOM   2919 C  CB  . ASN A  1 379 ? 60.895  35.996  54.501 1.00 38.03 ? 569 ASN A CB  1 
ATOM   2920 C  CG  . ASN A  1 379 ? 60.350  34.648  54.033 1.00 35.89 ? 569 ASN A CG  1 
ATOM   2921 O  OD1 . ASN A  1 379 ? 60.913  34.014  53.143 1.00 35.98 ? 569 ASN A OD1 1 
ATOM   2922 N  ND2 . ASN A  1 379 ? 59.244  34.215  54.628 1.00 31.57 ? 569 ASN A ND2 1 
ATOM   2923 N  N   . PRO A  1 380 ? 59.272  35.104  57.522 1.00 26.93 ? 570 PRO A N   1 
ATOM   2924 C  CA  . PRO A  1 380 ? 59.328  34.178  58.654 1.00 25.88 ? 570 PRO A CA  1 
ATOM   2925 C  C   . PRO A  1 380 ? 59.406  32.700  58.268 1.00 25.92 ? 570 PRO A C   1 
ATOM   2926 O  O   . PRO A  1 380 ? 59.814  31.864  59.075 1.00 25.87 ? 570 PRO A O   1 
ATOM   2927 C  CB  . PRO A  1 380 ? 58.048  34.502  59.405 1.00 24.82 ? 570 PRO A CB  1 
ATOM   2928 C  CG  . PRO A  1 380 ? 57.089  34.719  58.278 1.00 27.14 ? 570 PRO A CG  1 
ATOM   2929 C  CD  . PRO A  1 380 ? 57.887  35.558  57.292 1.00 26.07 ? 570 PRO A CD  1 
ATOM   2930 N  N   . CYS A  1 381 ? 59.013  32.376  57.043 1.00 23.44 ? 571 CYS A N   1 
ATOM   2931 C  CA  . CYS A  1 381 ? 59.045  30.988  56.602 1.00 25.68 ? 571 CYS A CA  1 
ATOM   2932 C  C   . CYS A  1 381 ? 59.997  30.760  55.432 1.00 23.35 ? 571 CYS A C   1 
ATOM   2933 O  O   . CYS A  1 381 ? 59.603  30.212  54.405 1.00 22.75 ? 571 CYS A O   1 
ATOM   2934 C  CB  . CYS A  1 381 ? 57.643  30.518  56.197 1.00 23.91 ? 571 CYS A CB  1 
ATOM   2935 S  SG  . CYS A  1 381 ? 56.317  30.693  57.440 1.00 30.89 ? 571 CYS A SG  1 
ATOM   2936 N  N   . LYS A  1 382 ? 61.248  31.174  55.578 1.00 23.77 ? 572 LYS A N   1 
ATOM   2937 C  CA  . LYS A  1 382 ? 62.206  30.974  54.501 1.00 25.65 ? 572 LYS A CA  1 
ATOM   2938 C  C   . LYS A  1 382 ? 62.356  29.478  54.248 1.00 21.52 ? 572 LYS A C   1 
ATOM   2939 O  O   . LYS A  1 382 ? 62.364  28.673  55.177 1.00 18.85 ? 572 LYS A O   1 
ATOM   2940 C  CB  . LYS A  1 382 ? 63.566  31.595  54.847 1.00 29.47 ? 572 LYS A CB  1 
ATOM   2941 C  CG  . LYS A  1 382 ? 64.610  31.441  53.743 1.00 40.91 ? 572 LYS A CG  1 
ATOM   2942 C  CD  . LYS A  1 382 ? 64.063  31.890  52.384 1.00 47.57 ? 572 LYS A CD  1 
ATOM   2943 C  CE  . LYS A  1 382 ? 65.057  31.623  51.256 1.00 51.54 ? 572 LYS A CE  1 
ATOM   2944 N  NZ  . LYS A  1 382 ? 64.496  31.958  49.911 1.00 45.62 ? 572 LYS A NZ  1 
ATOM   2945 N  N   . MET A  1 383 ? 62.471  29.114  52.979 1.00 19.43 ? 573 MET A N   1 
ATOM   2946 C  CA  . MET A  1 383 ? 62.599  27.722  52.593 1.00 19.37 ? 573 MET A CA  1 
ATOM   2947 C  C   . MET A  1 383 ? 63.419  27.638  51.311 1.00 22.13 ? 573 MET A C   1 
ATOM   2948 O  O   . MET A  1 383 ? 63.654  28.652  50.654 1.00 26.10 ? 573 MET A O   1 
ATOM   2949 C  CB  . MET A  1 383 ? 61.191  27.131  52.415 1.00 17.35 ? 573 MET A CB  1 
ATOM   2950 C  CG  . MET A  1 383 ? 61.041  26.015  51.392 1.00 20.84 ? 573 MET A CG  1 
ATOM   2951 S  SD  . MET A  1 383 ? 60.959  26.617  49.683 1.00 20.53 ? 573 MET A SD  1 
ATOM   2952 C  CE  . MET A  1 383 ? 59.294  27.241  49.617 1.00 19.44 ? 573 MET A CE  1 
ATOM   2953 N  N   . PHE A  1 384 ? 63.876  26.438  50.970 1.00 20.67 ? 574 PHE A N   1 
ATOM   2954 C  CA  . PHE A  1 384 ? 64.660  26.249  49.759 1.00 21.94 ? 574 PHE A CA  1 
ATOM   2955 C  C   . PHE A  1 384 ? 64.068  25.193  48.823 1.00 23.58 ? 574 PHE A C   1 
ATOM   2956 O  O   . PHE A  1 384 ? 63.765  24.075  49.245 1.00 24.62 ? 574 PHE A O   1 
ATOM   2957 C  CB  . PHE A  1 384 ? 66.101  25.868  50.116 1.00 20.49 ? 574 PHE A CB  1 
ATOM   2958 C  CG  . PHE A  1 384 ? 66.959  25.571  48.921 1.00 19.54 ? 574 PHE A CG  1 
ATOM   2959 C  CD1 . PHE A  1 384 ? 66.858  24.352  48.259 1.00 16.93 ? 574 PHE A CD1 1 
ATOM   2960 C  CD2 . PHE A  1 384 ? 67.833  26.533  48.425 1.00 22.38 ? 574 PHE A CD2 1 
ATOM   2961 C  CE1 . PHE A  1 384 ? 67.610  24.097  47.117 1.00 22.79 ? 574 PHE A CE1 1 
ATOM   2962 C  CE2 . PHE A  1 384 ? 68.592  26.288  47.283 1.00 23.31 ? 574 PHE A CE2 1 
ATOM   2963 C  CZ  . PHE A  1 384 ? 68.479  25.068  46.626 1.00 24.75 ? 574 PHE A CZ  1 
ATOM   2964 N  N   . TYR A  1 385 ? 63.907  25.563  47.554 1.00 22.26 ? 575 TYR A N   1 
ATOM   2965 C  CA  . TYR A  1 385 ? 63.387  24.657  46.532 1.00 20.91 ? 575 TYR A CA  1 
ATOM   2966 C  C   . TYR A  1 385 ? 64.055  24.912  45.186 1.00 19.57 ? 575 TYR A C   1 
ATOM   2967 O  O   . TYR A  1 385 ? 64.230  26.056  44.772 1.00 19.04 ? 575 TYR A O   1 
ATOM   2968 C  CB  . TYR A  1 385 ? 61.876  24.811  46.340 1.00 21.52 ? 575 TYR A CB  1 
ATOM   2969 C  CG  . TYR A  1 385 ? 61.368  23.962  45.190 1.00 20.81 ? 575 TYR A CG  1 
ATOM   2970 C  CD1 . TYR A  1 385 ? 61.164  22.593  45.347 1.00 24.70 ? 575 TYR A CD1 1 
ATOM   2971 C  CD2 . TYR A  1 385 ? 61.171  24.511  43.924 1.00 21.64 ? 575 TYR A CD2 1 
ATOM   2972 C  CE1 . TYR A  1 385 ? 60.780  21.788  44.272 1.00 21.33 ? 575 TYR A CE1 1 
ATOM   2973 C  CE2 . TYR A  1 385 ? 60.790  23.715  42.842 1.00 21.35 ? 575 TYR A CE2 1 
ATOM   2974 C  CZ  . TYR A  1 385 ? 60.596  22.354  43.023 1.00 20.94 ? 575 TYR A CZ  1 
ATOM   2975 O  OH  . TYR A  1 385 ? 60.220  21.557  41.959 1.00 13.18 ? 575 TYR A OH  1 
ATOM   2976 N  N   . SER A  1 386 ? 64.409  23.833  44.503 1.00 18.53 ? 576 SER A N   1 
ATOM   2977 C  CA  . SER A  1 386 ? 65.040  23.918  43.198 1.00 16.88 ? 576 SER A CA  1 
ATOM   2978 C  C   . SER A  1 386 ? 64.655  22.672  42.427 1.00 18.32 ? 576 SER A C   1 
ATOM   2979 O  O   . SER A  1 386 ? 65.001  21.564  42.824 1.00 26.35 ? 576 SER A O   1 
ATOM   2980 C  CB  . SER A  1 386 ? 66.556  23.983  43.349 1.00 23.11 ? 576 SER A CB  1 
ATOM   2981 O  OG  . SER A  1 386 ? 67.185  24.019  42.083 1.00 33.96 ? 576 SER A OG  1 
ATOM   2982 N  N   . ASN A  1 387 ? 63.932  22.844  41.328 1.00 19.70 ? 577 ASN A N   1 
ATOM   2983 C  CA  . ASN A  1 387 ? 63.506  21.700  40.533 1.00 19.36 ? 577 ASN A CA  1 
ATOM   2984 C  C   . ASN A  1 387 ? 64.710  20.936  39.997 1.00 19.97 ? 577 ASN A C   1 
ATOM   2985 O  O   . ASN A  1 387 ? 64.559  19.945  39.292 1.00 26.14 ? 577 ASN A O   1 
ATOM   2986 C  CB  . ASN A  1 387 ? 62.598  22.155  39.383 1.00 16.50 ? 577 ASN A CB  1 
ATOM   2987 C  CG  . ASN A  1 387 ? 63.363  22.784  38.239 1.00 12.57 ? 577 ASN A CG  1 
ATOM   2988 O  OD1 . ASN A  1 387 ? 64.339  23.502  38.446 1.00 24.05 ? 577 ASN A OD1 1 
ATOM   2989 N  ND2 . ASN A  1 387 ? 62.911  22.529  37.021 1.00 7.58  ? 577 ASN A ND2 1 
ATOM   2990 N  N   . GLU A  1 388 ? 65.904  21.407  40.343 1.00 22.39 ? 578 GLU A N   1 
ATOM   2991 C  CA  . GLU A  1 388 ? 67.149  20.770  39.921 1.00 24.06 ? 578 GLU A CA  1 
ATOM   2992 C  C   . GLU A  1 388 ? 67.398  19.543  40.802 1.00 24.27 ? 578 GLU A C   1 
ATOM   2993 O  O   . GLU A  1 388 ? 67.998  18.560  40.370 1.00 18.62 ? 578 GLU A O   1 
ATOM   2994 C  CB  . GLU A  1 388 ? 68.303  21.768  40.048 1.00 24.04 ? 578 GLU A CB  1 
ATOM   2995 C  CG  . GLU A  1 388 ? 69.673  21.229  39.677 1.00 29.03 ? 578 GLU A CG  1 
ATOM   2996 C  CD  . GLU A  1 388 ? 70.704  22.341  39.510 1.00 37.60 ? 578 GLU A CD  1 
ATOM   2997 O  OE1 . GLU A  1 388 ? 70.930  23.112  40.469 1.00 35.14 ? 578 GLU A OE1 1 
ATOM   2998 O  OE2 . GLU A  1 388 ? 71.286  22.446  38.410 1.00 42.87 ? 578 GLU A OE2 1 
ATOM   2999 N  N   . ASP A  1 389 ? 66.920  19.623  42.040 1.00 23.70 ? 579 ASP A N   1 
ATOM   3000 C  CA  . ASP A  1 389 ? 67.041  18.550  43.020 1.00 20.39 ? 579 ASP A CA  1 
ATOM   3001 C  C   . ASP A  1 389 ? 66.080  18.860  44.167 1.00 20.02 ? 579 ASP A C   1 
ATOM   3002 O  O   . ASP A  1 389 ? 66.455  19.468  45.171 1.00 18.28 ? 579 ASP A O   1 
ATOM   3003 C  CB  . ASP A  1 389 ? 68.477  18.455  43.533 1.00 23.13 ? 579 ASP A CB  1 
ATOM   3004 C  CG  . ASP A  1 389 ? 68.617  17.480  44.681 1.00 27.87 ? 579 ASP A CG  1 
ATOM   3005 O  OD1 . ASP A  1 389 ? 67.871  16.478  44.699 1.00 29.09 ? 579 ASP A OD1 1 
ATOM   3006 O  OD2 . ASP A  1 389 ? 69.473  17.711  45.559 1.00 31.00 ? 579 ASP A OD2 1 
ATOM   3007 N  N   . GLU A  1 390 ? 64.835  18.433  43.998 1.00 16.37 ? 580 GLU A N   1 
ATOM   3008 C  CA  . GLU A  1 390 ? 63.778  18.676  44.968 1.00 15.59 ? 580 GLU A CA  1 
ATOM   3009 C  C   . GLU A  1 390 ? 64.035  18.229  46.402 1.00 18.64 ? 580 GLU A C   1 
ATOM   3010 O  O   . GLU A  1 390 ? 63.458  18.792  47.339 1.00 17.37 ? 580 GLU A O   1 
ATOM   3011 C  CB  . GLU A  1 390 ? 62.483  18.049  44.466 1.00 13.48 ? 580 GLU A CB  1 
ATOM   3012 C  CG  . GLU A  1 390 ? 62.081  18.535  43.094 1.00 10.88 ? 580 GLU A CG  1 
ATOM   3013 C  CD  . GLU A  1 390 ? 60.710  18.052  42.692 1.00 12.35 ? 580 GLU A CD  1 
ATOM   3014 O  OE1 . GLU A  1 390 ? 60.499  16.819  42.659 1.00 10.69 ? 580 GLU A OE1 1 
ATOM   3015 O  OE2 . GLU A  1 390 ? 59.844  18.908  42.410 1.00 16.92 ? 580 GLU A OE2 1 
ATOM   3016 N  N   . HIS A  1 391 ? 64.890  17.227  46.583 1.00 17.81 ? 581 HIS A N   1 
ATOM   3017 C  CA  . HIS A  1 391 ? 65.182  16.732  47.924 1.00 15.24 ? 581 HIS A CA  1 
ATOM   3018 C  C   . HIS A  1 391 ? 65.952  17.758  48.745 1.00 13.06 ? 581 HIS A C   1 
ATOM   3019 O  O   . HIS A  1 391 ? 65.784  17.842  49.961 1.00 14.20 ? 581 HIS A O   1 
ATOM   3020 C  CB  . HIS A  1 391 ? 65.978  15.425  47.864 1.00 16.43 ? 581 HIS A CB  1 
ATOM   3021 C  CG  . HIS A  1 391 ? 66.235  14.824  49.210 1.00 25.65 ? 581 HIS A CG  1 
ATOM   3022 N  ND1 . HIS A  1 391 ? 65.218  14.405  50.042 1.00 29.17 ? 581 HIS A ND1 1 
ATOM   3023 C  CD2 . HIS A  1 391 ? 67.388  14.615  49.890 1.00 29.28 ? 581 HIS A CD2 1 
ATOM   3024 C  CE1 . HIS A  1 391 ? 65.733  13.966  51.177 1.00 31.23 ? 581 HIS A CE1 1 
ATOM   3025 N  NE2 . HIS A  1 391 ? 67.047  14.083  51.111 1.00 32.10 ? 581 HIS A NE2 1 
ATOM   3026 N  N   . LYS A  1 392 ? 66.804  18.531  48.081 1.00 9.42  ? 582 LYS A N   1 
ATOM   3027 C  CA  . LYS A  1 392 ? 67.577  19.558  48.763 1.00 10.13 ? 582 LYS A CA  1 
ATOM   3028 C  C   . LYS A  1 392 ? 66.595  20.518  49.435 1.00 13.79 ? 582 LYS A C   1 
ATOM   3029 O  O   . LYS A  1 392 ? 65.677  21.027  48.792 1.00 15.18 ? 582 LYS A O   1 
ATOM   3030 C  CB  . LYS A  1 392 ? 68.462  20.295  47.751 1.00 11.60 ? 582 LYS A CB  1 
ATOM   3031 C  CG  . LYS A  1 392 ? 69.281  21.444  48.322 1.00 17.29 ? 582 LYS A CG  1 
ATOM   3032 C  CD  . LYS A  1 392 ? 70.448  21.782  47.401 1.00 27.78 ? 582 LYS A CD  1 
ATOM   3033 C  CE  . LYS A  1 392 ? 70.954  23.207  47.605 1.00 34.74 ? 582 LYS A CE  1 
ATOM   3034 N  NZ  . LYS A  1 392 ? 71.261  23.521  49.025 1.00 44.61 ? 582 LYS A NZ  1 
ATOM   3035 N  N   . GLY A  1 393 ? 66.776  20.746  50.733 1.00 13.18 ? 583 GLY A N   1 
ATOM   3036 C  CA  . GLY A  1 393 ? 65.881  21.635  51.456 1.00 7.88  ? 583 GLY A CA  1 
ATOM   3037 C  C   . GLY A  1 393 ? 64.872  20.854  52.279 1.00 12.61 ? 583 GLY A C   1 
ATOM   3038 O  O   . GLY A  1 393 ? 64.200  21.402  53.160 1.00 7.95  ? 583 GLY A O   1 
ATOM   3039 N  N   . MET A  1 394 ? 64.758  19.564  51.981 1.00 13.02 ? 584 MET A N   1 
ATOM   3040 C  CA  . MET A  1 394 ? 63.846  18.691  52.706 1.00 13.02 ? 584 MET A CA  1 
ATOM   3041 C  C   . MET A  1 394 ? 64.519  18.306  54.015 1.00 14.42 ? 584 MET A C   1 
ATOM   3042 O  O   . MET A  1 394 ? 65.745  18.201  54.074 1.00 17.87 ? 584 MET A O   1 
ATOM   3043 C  CB  . MET A  1 394 ? 63.553  17.424  51.896 1.00 9.87  ? 584 MET A CB  1 
ATOM   3044 C  CG  . MET A  1 394 ? 62.681  17.633  50.669 1.00 12.49 ? 584 MET A CG  1 
ATOM   3045 S  SD  . MET A  1 394 ? 61.019  18.200  51.083 1.00 19.40 ? 584 MET A SD  1 
ATOM   3046 C  CE  . MET A  1 394 ? 60.241  16.678  51.558 1.00 7.10  ? 584 MET A CE  1 
ATOM   3047 N  N   . VAL A  1 395 ? 63.723  18.112  55.062 1.00 13.40 ? 585 VAL A N   1 
ATOM   3048 C  CA  . VAL A  1 395 ? 64.258  17.722  56.360 1.00 9.92  ? 585 VAL A CA  1 
ATOM   3049 C  C   . VAL A  1 395 ? 65.012  16.404  56.214 1.00 10.56 ? 585 VAL A C   1 
ATOM   3050 O  O   . VAL A  1 395 ? 64.523  15.462  55.593 1.00 15.26 ? 585 VAL A O   1 
ATOM   3051 C  CB  . VAL A  1 395 ? 63.126  17.542  57.397 1.00 12.95 ? 585 VAL A CB  1 
ATOM   3052 C  CG1 . VAL A  1 395 ? 63.632  16.764  58.602 1.00 13.92 ? 585 VAL A CG1 1 
ATOM   3053 C  CG2 . VAL A  1 395 ? 62.616  18.898  57.842 1.00 15.34 ? 585 VAL A CG2 1 
ATOM   3054 N  N   . LEU A  1 396 ? 66.208  16.336  56.779 1.00 6.08  ? 586 LEU A N   1 
ATOM   3055 C  CA  . LEU A  1 396 ? 66.992  15.116  56.689 1.00 11.80 ? 586 LEU A CA  1 
ATOM   3056 C  C   . LEU A  1 396 ? 66.355  13.998  57.510 1.00 14.11 ? 586 LEU A C   1 
ATOM   3057 O  O   . LEU A  1 396 ? 65.775  14.242  58.573 1.00 15.81 ? 586 LEU A O   1 
ATOM   3058 C  CB  . LEU A  1 396 ? 68.420  15.372  57.179 1.00 12.48 ? 586 LEU A CB  1 
ATOM   3059 C  CG  . LEU A  1 396 ? 69.263  16.265  56.263 1.00 17.07 ? 586 LEU A CG  1 
ATOM   3060 C  CD1 . LEU A  1 396 ? 70.541  16.687  56.969 1.00 12.90 ? 586 LEU A CD1 1 
ATOM   3061 C  CD2 . LEU A  1 396 ? 69.572  15.510  54.977 1.00 12.71 ? 586 LEU A CD2 1 
ATOM   3062 N  N   . PRO A  1 397 ? 66.429  12.755  57.017 1.00 8.38  ? 587 PRO A N   1 
ATOM   3063 C  CA  . PRO A  1 397 ? 65.832  11.666  57.792 1.00 11.07 ? 587 PRO A CA  1 
ATOM   3064 C  C   . PRO A  1 397 ? 66.562  11.496  59.124 1.00 12.10 ? 587 PRO A C   1 
ATOM   3065 O  O   . PRO A  1 397 ? 67.773  11.719  59.210 1.00 5.93  ? 587 PRO A O   1 
ATOM   3066 C  CB  . PRO A  1 397 ? 65.983  10.454  56.866 1.00 9.81  ? 587 PRO A CB  1 
ATOM   3067 C  CG  . PRO A  1 397 ? 67.148  10.804  56.012 1.00 5.95  ? 587 PRO A CG  1 
ATOM   3068 C  CD  . PRO A  1 397 ? 66.935  12.267  55.725 1.00 3.01  ? 587 PRO A CD  1 
ATOM   3069 N  N   . GLY A  1 398 ? 65.815  11.118  60.160 1.00 13.62 ? 588 GLY A N   1 
ATOM   3070 C  CA  . GLY A  1 398 ? 66.401  10.934  61.476 1.00 8.67  ? 588 GLY A CA  1 
ATOM   3071 C  C   . GLY A  1 398 ? 66.444  12.223  62.273 1.00 13.52 ? 588 GLY A C   1 
ATOM   3072 O  O   . GLY A  1 398 ? 66.942  12.258  63.398 1.00 17.07 ? 588 GLY A O   1 
ATOM   3073 N  N   . THR A  1 399 ? 65.925  13.298  61.692 1.00 16.72 ? 589 THR A N   1 
ATOM   3074 C  CA  . THR A  1 399 ? 65.912  14.583  62.377 1.00 15.77 ? 589 THR A CA  1 
ATOM   3075 C  C   . THR A  1 399 ? 64.877  14.576  63.494 1.00 15.15 ? 589 THR A C   1 
ATOM   3076 O  O   . THR A  1 399 ? 63.731  14.177  63.289 1.00 15.53 ? 589 THR A O   1 
ATOM   3077 C  CB  . THR A  1 399 ? 65.576  15.715  61.408 1.00 13.53 ? 589 THR A CB  1 
ATOM   3078 O  OG1 . THR A  1 399 ? 66.558  15.753  60.369 1.00 14.30 ? 589 THR A OG1 1 
ATOM   3079 C  CG2 . THR A  1 399 ? 65.547  17.048  62.138 1.00 11.03 ? 589 THR A CG2 1 
ATOM   3080 N  N   . LYS A  1 400 ? 65.287  15.015  64.676 1.00 13.82 ? 590 LYS A N   1 
ATOM   3081 C  CA  . LYS A  1 400 ? 64.388  15.061  65.819 1.00 14.73 ? 590 LYS A CA  1 
ATOM   3082 C  C   . LYS A  1 400 ? 63.246  16.032  65.516 1.00 15.49 ? 590 LYS A C   1 
ATOM   3083 O  O   . LYS A  1 400 ? 63.424  17.249  65.550 1.00 14.28 ? 590 LYS A O   1 
ATOM   3084 C  CB  . LYS A  1 400 ? 65.159  15.499  67.071 1.00 11.35 ? 590 LYS A CB  1 
ATOM   3085 C  CG  . LYS A  1 400 ? 64.354  15.407  68.350 1.00 14.43 ? 590 LYS A CG  1 
ATOM   3086 C  CD  . LYS A  1 400 ? 65.200  15.711  69.564 1.00 15.61 ? 590 LYS A CD  1 
ATOM   3087 C  CE  . LYS A  1 400 ? 64.377  15.596  70.837 1.00 18.44 ? 590 LYS A CE  1 
ATOM   3088 N  NZ  . LYS A  1 400 ? 65.204  15.805  72.055 1.00 19.65 ? 590 LYS A NZ  1 
ATOM   3089 N  N   . CYS A  1 401 ? 62.077  15.477  65.210 1.00 16.84 ? 591 CYS A N   1 
ATOM   3090 C  CA  . CYS A  1 401 ? 60.892  16.263  64.871 1.00 19.26 ? 591 CYS A CA  1 
ATOM   3091 C  C   . CYS A  1 401 ? 60.023  16.542  66.082 1.00 18.80 ? 591 CYS A C   1 
ATOM   3092 O  O   . CYS A  1 401 ? 59.036  17.264  65.990 1.00 17.74 ? 591 CYS A O   1 
ATOM   3093 C  CB  . CYS A  1 401 ? 60.062  15.518  63.826 1.00 19.52 ? 591 CYS A CB  1 
ATOM   3094 S  SG  . CYS A  1 401 ? 59.747  13.793  64.306 1.00 26.92 ? 591 CYS A SG  1 
ATOM   3095 N  N   . ALA A  1 402 ? 60.389  15.960  67.216 1.00 21.12 ? 592 ALA A N   1 
ATOM   3096 C  CA  . ALA A  1 402 ? 59.632  16.140  68.447 1.00 21.11 ? 592 ALA A CA  1 
ATOM   3097 C  C   . ALA A  1 402 ? 60.326  15.371  69.551 1.00 21.83 ? 592 ALA A C   1 
ATOM   3098 O  O   . ALA A  1 402 ? 61.101  14.452  69.283 1.00 24.16 ? 592 ALA A O   1 
ATOM   3099 C  CB  . ALA A  1 402 ? 58.205  15.619  68.272 1.00 14.70 ? 592 ALA A CB  1 
ATOM   3100 N  N   . ASP A  1 403 ? 60.044  15.748  70.792 1.00 20.16 ? 593 ASP A N   1 
ATOM   3101 C  CA  . ASP A  1 403 ? 60.637  15.078  71.936 1.00 19.11 ? 593 ASP A CA  1 
ATOM   3102 C  C   . ASP A  1 403 ? 60.308  13.588  71.844 1.00 17.04 ? 593 ASP A C   1 
ATOM   3103 O  O   . ASP A  1 403 ? 59.140  13.205  71.775 1.00 16.47 ? 593 ASP A O   1 
ATOM   3104 C  CB  . ASP A  1 403 ? 60.086  15.682  73.230 1.00 26.91 ? 593 ASP A CB  1 
ATOM   3105 C  CG  . ASP A  1 403 ? 60.755  15.124  74.473 1.00 39.98 ? 593 ASP A CG  1 
ATOM   3106 O  OD1 . ASP A  1 403 ? 60.515  15.672  75.571 1.00 46.76 ? 593 ASP A OD1 1 
ATOM   3107 O  OD2 . ASP A  1 403 ? 61.514  14.138  74.357 1.00 46.04 ? 593 ASP A OD2 1 
ATOM   3108 N  N   . GLY A  1 404 ? 61.347  12.759  71.811 1.00 15.73 ? 594 GLY A N   1 
ATOM   3109 C  CA  . GLY A  1 404 ? 61.160  11.321  71.726 1.00 13.17 ? 594 GLY A CA  1 
ATOM   3110 C  C   . GLY A  1 404 ? 60.801  10.809  70.343 1.00 15.49 ? 594 GLY A C   1 
ATOM   3111 O  O   . GLY A  1 404 ? 60.599  9.606   70.155 1.00 16.04 ? 594 GLY A O   1 
ATOM   3112 N  N   . LYS A  1 405 ? 60.729  11.710  69.367 1.00 17.53 ? 595 LYS A N   1 
ATOM   3113 C  CA  . LYS A  1 405 ? 60.369  11.319  68.006 1.00 19.12 ? 595 LYS A CA  1 
ATOM   3114 C  C   . LYS A  1 405 ? 61.394  11.771  66.970 1.00 17.70 ? 595 LYS A C   1 
ATOM   3115 O  O   . LYS A  1 405 ? 62.045  12.803  67.126 1.00 17.70 ? 595 LYS A O   1 
ATOM   3116 C  CB  . LYS A  1 405 ? 58.984  11.874  67.655 1.00 14.08 ? 595 LYS A CB  1 
ATOM   3117 C  CG  . LYS A  1 405 ? 57.960  11.656  68.764 1.00 9.71  ? 595 LYS A CG  1 
ATOM   3118 C  CD  . LYS A  1 405 ? 56.547  12.026  68.347 1.00 5.66  ? 595 LYS A CD  1 
ATOM   3119 C  CE  . LYS A  1 405 ? 55.958  10.976  67.430 1.00 10.93 ? 595 LYS A CE  1 
ATOM   3120 N  NZ  . LYS A  1 405 ? 54.527  11.232  67.136 1.00 14.58 ? 595 LYS A NZ  1 
ATOM   3121 N  N   . VAL A  1 406 ? 61.521  10.987  65.907 1.00 16.14 ? 596 VAL A N   1 
ATOM   3122 C  CA  . VAL A  1 406 ? 62.476  11.266  64.843 1.00 18.12 ? 596 VAL A CA  1 
ATOM   3123 C  C   . VAL A  1 406 ? 61.775  11.133  63.481 1.00 20.36 ? 596 VAL A C   1 
ATOM   3124 O  O   . VAL A  1 406 ? 60.708  10.525  63.390 1.00 24.93 ? 596 VAL A O   1 
ATOM   3125 C  CB  . VAL A  1 406 ? 63.674  10.271  64.953 1.00 15.00 ? 596 VAL A CB  1 
ATOM   3126 C  CG1 . VAL A  1 406 ? 63.563  9.163   63.912 1.00 10.32 ? 596 VAL A CG1 1 
ATOM   3127 C  CG2 . VAL A  1 406 ? 64.974  11.015  64.838 1.00 16.23 ? 596 VAL A CG2 1 
ATOM   3128 N  N   . CYS A  1 407 ? 62.358  11.701  62.428 1.00 19.91 ? 597 CYS A N   1 
ATOM   3129 C  CA  . CYS A  1 407 ? 61.740  11.606  61.105 1.00 22.33 ? 597 CYS A CA  1 
ATOM   3130 C  C   . CYS A  1 407 ? 62.131  10.336  60.370 1.00 20.92 ? 597 CYS A C   1 
ATOM   3131 O  O   . CYS A  1 407 ? 63.303  9.961   60.329 1.00 19.95 ? 597 CYS A O   1 
ATOM   3132 C  CB  . CYS A  1 407 ? 62.101  12.814  60.229 1.00 26.19 ? 597 CYS A CB  1 
ATOM   3133 S  SG  . CYS A  1 407 ? 61.298  14.379  60.705 1.00 32.86 ? 597 CYS A SG  1 
ATOM   3134 N  N   . SER A  1 408 ? 61.136  9.680   59.784 1.00 23.19 ? 598 SER A N   1 
ATOM   3135 C  CA  . SER A  1 408 ? 61.363  8.452   59.035 1.00 23.81 ? 598 SER A CA  1 
ATOM   3136 C  C   . SER A  1 408 ? 60.440  8.421   57.825 1.00 21.91 ? 598 SER A C   1 
ATOM   3137 O  O   . SER A  1 408 ? 59.229  8.274   57.963 1.00 27.58 ? 598 SER A O   1 
ATOM   3138 C  CB  . SER A  1 408 ? 61.098  7.237   59.922 1.00 26.09 ? 598 SER A CB  1 
ATOM   3139 O  OG  . SER A  1 408 ? 61.411  6.040   59.236 1.00 34.61 ? 598 SER A OG  1 
ATOM   3140 N  N   . ASN A  1 409 ? 61.022  8.572   56.640 1.00 23.32 ? 599 ASN A N   1 
ATOM   3141 C  CA  . ASN A  1 409 ? 60.263  8.572   55.394 1.00 23.84 ? 599 ASN A CA  1 
ATOM   3142 C  C   . ASN A  1 409 ? 59.083  9.542   55.448 1.00 22.50 ? 599 ASN A C   1 
ATOM   3143 O  O   . ASN A  1 409 ? 57.959  9.185   55.088 1.00 19.57 ? 599 ASN A O   1 
ATOM   3144 C  CB  . ASN A  1 409 ? 59.743  7.167   55.081 1.00 28.51 ? 599 ASN A CB  1 
ATOM   3145 C  CG  . ASN A  1 409 ? 59.113  7.073   53.700 1.00 34.78 ? 599 ASN A CG  1 
ATOM   3146 O  OD1 . ASN A  1 409 ? 58.228  6.251   53.463 1.00 31.64 ? 599 ASN A OD1 1 
ATOM   3147 N  ND2 . ASN A  1 409 ? 59.578  7.910   52.777 1.00 39.50 ? 599 ASN A ND2 1 
ATOM   3148 N  N   . GLY A  1 410 ? 59.345  10.764  55.903 1.00 22.27 ? 600 GLY A N   1 
ATOM   3149 C  CA  . GLY A  1 410 ? 58.299  11.770  55.987 1.00 21.64 ? 600 GLY A CA  1 
ATOM   3150 C  C   . GLY A  1 410 ? 57.281  11.530  57.088 1.00 20.55 ? 600 GLY A C   1 
ATOM   3151 O  O   . GLY A  1 410 ? 56.134  11.964  56.987 1.00 23.87 ? 600 GLY A O   1 
ATOM   3152 N  N   . HIS A  1 411 ? 57.698  10.836  58.139 1.00 18.71 ? 601 HIS A N   1 
ATOM   3153 C  CA  . HIS A  1 411 ? 56.818  10.540  59.263 1.00 16.31 ? 601 HIS A CA  1 
ATOM   3154 C  C   . HIS A  1 411 ? 57.525  10.822  60.584 1.00 17.49 ? 601 HIS A C   1 
ATOM   3155 O  O   . HIS A  1 411 ? 58.636  10.339  60.816 1.00 19.48 ? 601 HIS A O   1 
ATOM   3156 C  CB  . HIS A  1 411 ? 56.404  9.069   59.241 1.00 17.04 ? 601 HIS A CB  1 
ATOM   3157 C  CG  . HIS A  1 411 ? 55.438  8.717   58.155 1.00 17.77 ? 601 HIS A CG  1 
ATOM   3158 N  ND1 . HIS A  1 411 ? 54.088  8.988   58.242 1.00 22.52 ? 601 HIS A ND1 1 
ATOM   3159 C  CD2 . HIS A  1 411 ? 55.618  8.080   56.974 1.00 15.64 ? 601 HIS A CD2 1 
ATOM   3160 C  CE1 . HIS A  1 411 ? 53.478  8.529   57.165 1.00 16.38 ? 601 HIS A CE1 1 
ATOM   3161 N  NE2 . HIS A  1 411 ? 54.384  7.973   56.379 1.00 18.20 ? 601 HIS A NE2 1 
ATOM   3162 N  N   . CYS A  1 412 ? 56.891  11.608  61.445 1.00 15.07 ? 602 CYS A N   1 
ATOM   3163 C  CA  . CYS A  1 412 ? 57.476  11.898  62.747 1.00 19.66 ? 602 CYS A CA  1 
ATOM   3164 C  C   . CYS A  1 412 ? 57.066  10.741  63.650 1.00 21.63 ? 602 CYS A C   1 
ATOM   3165 O  O   . CYS A  1 412 ? 55.924  10.666  64.105 1.00 23.82 ? 602 CYS A O   1 
ATOM   3166 C  CB  . CYS A  1 412 ? 56.950  13.225  63.295 1.00 21.06 ? 602 CYS A CB  1 
ATOM   3167 S  SG  . CYS A  1 412 ? 57.781  13.735  64.829 1.00 26.28 ? 602 CYS A SG  1 
ATOM   3168 N  N   . VAL A  1 413 ? 58.007  9.836   63.898 1.00 23.93 ? 603 VAL A N   1 
ATOM   3169 C  CA  . VAL A  1 413 ? 57.743  8.648   64.701 1.00 21.63 ? 603 VAL A CA  1 
ATOM   3170 C  C   . VAL A  1 413 ? 58.623  8.508   65.942 1.00 27.54 ? 603 VAL A C   1 
ATOM   3171 O  O   . VAL A  1 413 ? 59.675  9.141   66.049 1.00 27.41 ? 603 VAL A O   1 
ATOM   3172 C  CB  . VAL A  1 413 ? 57.922  7.384   63.833 1.00 17.32 ? 603 VAL A CB  1 
ATOM   3173 C  CG1 . VAL A  1 413 ? 57.050  7.481   62.591 1.00 2.32  ? 603 VAL A CG1 1 
ATOM   3174 C  CG2 . VAL A  1 413 ? 59.380  7.234   63.433 1.00 12.97 ? 603 VAL A CG2 1 
ATOM   3175 N  N   . ASP A  1 414 ? 58.182  7.664   66.875 1.00 31.77 ? 604 ASP A N   1 
ATOM   3176 C  CA  . ASP A  1 414 ? 58.919  7.405   68.111 1.00 33.64 ? 604 ASP A CA  1 
ATOM   3177 C  C   . ASP A  1 414 ? 60.276  6.804   67.779 1.00 31.31 ? 604 ASP A C   1 
ATOM   3178 O  O   . ASP A  1 414 ? 60.377  5.913   66.931 1.00 22.65 ? 604 ASP A O   1 
ATOM   3179 C  CB  . ASP A  1 414 ? 58.160  6.417   69.001 1.00 38.15 ? 604 ASP A CB  1 
ATOM   3180 C  CG  . ASP A  1 414 ? 56.828  6.955   69.474 1.00 44.81 ? 604 ASP A CG  1 
ATOM   3181 O  OD1 . ASP A  1 414 ? 56.050  6.170   70.058 1.00 47.70 ? 604 ASP A OD1 1 
ATOM   3182 O  OD2 . ASP A  1 414 ? 56.559  8.157   69.268 1.00 48.97 ? 604 ASP A OD2 1 
ATOM   3183 N  N   . VAL A  1 415 ? 61.311  7.286   68.459 1.00 30.45 ? 605 VAL A N   1 
ATOM   3184 C  CA  . VAL A  1 415 ? 62.663  6.790   68.239 1.00 30.52 ? 605 VAL A CA  1 
ATOM   3185 C  C   . VAL A  1 415 ? 62.719  5.301   68.548 1.00 35.34 ? 605 VAL A C   1 
ATOM   3186 O  O   . VAL A  1 415 ? 63.254  4.514   67.766 1.00 38.03 ? 605 VAL A O   1 
ATOM   3187 C  CB  . VAL A  1 415 ? 63.677  7.498   69.150 1.00 26.42 ? 605 VAL A CB  1 
ATOM   3188 C  CG1 . VAL A  1 415 ? 65.087  7.158   68.706 1.00 31.94 ? 605 VAL A CG1 1 
ATOM   3189 C  CG2 . VAL A  1 415 ? 63.450  8.995   69.122 1.00 32.90 ? 605 VAL A CG2 1 
ATOM   3190 N  N   . ALA A  1 416 ? 62.155  4.928   69.695 1.00 39.40 ? 606 ALA A N   1 
ATOM   3191 C  CA  . ALA A  1 416 ? 62.128  3.543   70.155 1.00 42.49 ? 606 ALA A CA  1 
ATOM   3192 C  C   . ALA A  1 416 ? 61.598  2.558   69.115 1.00 44.29 ? 606 ALA A C   1 
ATOM   3193 O  O   . ALA A  1 416 ? 61.965  1.382   69.122 1.00 47.15 ? 606 ALA A O   1 
ATOM   3194 C  CB  . ALA A  1 416 ? 61.299  3.443   71.430 1.00 41.63 ? 606 ALA A CB  1 
ATOM   3195 N  N   . THR A  1 417 ? 60.739  3.035   68.221 1.00 44.67 ? 607 THR A N   1 
ATOM   3196 C  CA  . THR A  1 417 ? 60.172  2.178   67.185 1.00 46.56 ? 607 THR A CA  1 
ATOM   3197 C  C   . THR A  1 417 ? 60.707  2.559   65.807 1.00 46.20 ? 607 THR A C   1 
ATOM   3198 O  O   . THR A  1 417 ? 60.270  2.019   64.790 1.00 45.28 ? 607 THR A O   1 
ATOM   3199 C  CB  . THR A  1 417 ? 58.649  2.303   67.150 1.00 48.95 ? 607 THR A CB  1 
ATOM   3200 O  OG1 . THR A  1 417 ? 58.290  3.545   66.529 1.00 51.22 ? 607 THR A OG1 1 
ATOM   3201 C  CG2 . THR A  1 417 ? 58.087  2.270   68.567 1.00 47.28 ? 607 THR A CG2 1 
ATOM   3202 N  N   . ALA A  1 418 ? 61.654  3.494   65.785 1.00 44.16 ? 608 ALA A N   1 
ATOM   3203 C  CA  . ALA A  1 418 ? 62.252  3.973   64.544 1.00 37.63 ? 608 ALA A CA  1 
ATOM   3204 C  C   . ALA A  1 418 ? 63.341  3.050   64.009 1.00 33.75 ? 608 ALA A C   1 
ATOM   3205 O  O   . ALA A  1 418 ? 63.433  2.822   62.803 1.00 29.24 ? 608 ALA A O   1 
ATOM   3206 C  CB  . ALA A  1 418 ? 62.823  5.371   64.754 1.00 35.39 ? 608 ALA A CB  1 
ATOM   3207 N  N   . TYR A  1 419 ? 64.170  2.525   64.905 1.00 30.36 ? 609 TYR A N   1 
ATOM   3208 C  CA  . TYR A  1 419 ? 65.256  1.648   64.492 1.00 32.05 ? 609 TYR A CA  1 
ATOM   3209 C  C   . TYR A  1 419 ? 65.214  0.322   65.241 1.00 34.88 ? 609 TYR A C   1 
ATOM   3210 O  O   . TYR A  1 419 ? 64.343  0.179   66.125 1.00 40.71 ? 609 TYR A O   1 
ATOM   3211 C  CB  . TYR A  1 419 ? 66.607  2.333   64.735 1.00 26.93 ? 609 TYR A CB  1 
ATOM   3212 C  CG  . TYR A  1 419 ? 66.591  3.835   64.535 1.00 17.04 ? 609 TYR A CG  1 
ATOM   3213 C  CD1 . TYR A  1 419 ? 66.374  4.696   65.612 1.00 11.11 ? 609 TYR A CD1 1 
ATOM   3214 C  CD2 . TYR A  1 419 ? 66.777  4.396   63.265 1.00 10.97 ? 609 TYR A CD2 1 
ATOM   3215 C  CE1 . TYR A  1 419 ? 66.342  6.079   65.433 1.00 14.62 ? 609 TYR A CE1 1 
ATOM   3216 C  CE2 . TYR A  1 419 ? 66.748  5.775   63.073 1.00 4.14  ? 609 TYR A CE2 1 
ATOM   3217 C  CZ  . TYR A  1 419 ? 66.529  6.610   64.161 1.00 15.87 ? 609 TYR A CZ  1 
ATOM   3218 O  OH  . TYR A  1 419 ? 66.485  7.973   63.980 1.00 15.72 ? 609 TYR A OH  1 
ATOM   3219 O  OXT . TYR A  1 419 ? 66.057  -0.553  64.940 1.00 36.12 ? 609 TYR A OXT 1 
ATOM   3220 N  N   . ASN B  1 5   ? 93.339  41.839  38.236 1.00 55.62 ? 195 ASN B N   1 
ATOM   3221 C  CA  . ASN B  1 5   ? 93.069  42.398  39.592 1.00 56.69 ? 195 ASN B CA  1 
ATOM   3222 C  C   . ASN B  1 5   ? 91.860  41.725  40.244 1.00 54.34 ? 195 ASN B C   1 
ATOM   3223 O  O   . ASN B  1 5   ? 90.821  41.541  39.607 1.00 57.76 ? 195 ASN B O   1 
ATOM   3224 C  CB  . ASN B  1 5   ? 92.839  43.910  39.501 1.00 57.74 ? 195 ASN B CB  1 
ATOM   3225 C  CG  . ASN B  1 5   ? 92.387  44.509  40.816 1.00 58.76 ? 195 ASN B CG  1 
ATOM   3226 O  OD1 . ASN B  1 5   ? 92.981  44.253  41.864 1.00 56.61 ? 195 ASN B OD1 1 
ATOM   3227 N  ND2 . ASN B  1 5   ? 91.331  45.318  40.768 1.00 59.53 ? 195 ASN B ND2 1 
ATOM   3228 N  N   . PRO B  1 6   ? 91.989  41.341  41.524 1.00 49.41 ? 196 PRO B N   1 
ATOM   3229 C  CA  . PRO B  1 6   ? 90.916  40.681  42.277 1.00 46.32 ? 196 PRO B CA  1 
ATOM   3230 C  C   . PRO B  1 6   ? 90.067  41.617  43.147 1.00 43.50 ? 196 PRO B C   1 
ATOM   3231 O  O   . PRO B  1 6   ? 88.889  41.355  43.396 1.00 44.17 ? 196 PRO B O   1 
ATOM   3232 C  CB  . PRO B  1 6   ? 91.683  39.673  43.116 1.00 47.07 ? 196 PRO B CB  1 
ATOM   3233 C  CG  . PRO B  1 6   ? 92.892  40.476  43.512 1.00 45.46 ? 196 PRO B CG  1 
ATOM   3234 C  CD  . PRO B  1 6   ? 93.282  41.190  42.222 1.00 47.27 ? 196 PRO B CD  1 
ATOM   3235 N  N   . PHE B  1 7   ? 90.682  42.703  43.606 1.00 38.36 ? 197 PHE B N   1 
ATOM   3236 C  CA  . PHE B  1 7   ? 90.036  43.690  44.468 1.00 29.91 ? 197 PHE B CA  1 
ATOM   3237 C  C   . PHE B  1 7   ? 88.690  44.250  44.021 1.00 26.80 ? 197 PHE B C   1 
ATOM   3238 O  O   . PHE B  1 7   ? 88.478  44.540  42.846 1.00 26.44 ? 197 PHE B O   1 
ATOM   3239 C  CB  . PHE B  1 7   ? 90.989  44.862  44.700 1.00 24.02 ? 197 PHE B CB  1 
ATOM   3240 C  CG  . PHE B  1 7   ? 91.794  44.749  45.956 1.00 24.27 ? 197 PHE B CG  1 
ATOM   3241 C  CD1 . PHE B  1 7   ? 91.222  45.042  47.188 1.00 23.16 ? 197 PHE B CD1 1 
ATOM   3242 C  CD2 . PHE B  1 7   ? 93.128  44.351  45.911 1.00 22.21 ? 197 PHE B CD2 1 
ATOM   3243 C  CE1 . PHE B  1 7   ? 91.970  44.943  48.364 1.00 27.52 ? 197 PHE B CE1 1 
ATOM   3244 C  CE2 . PHE B  1 7   ? 93.883  44.247  47.079 1.00 22.99 ? 197 PHE B CE2 1 
ATOM   3245 C  CZ  . PHE B  1 7   ? 93.304  44.544  48.308 1.00 23.63 ? 197 PHE B CZ  1 
ATOM   3246 N  N   . ARG B  1 8   ? 87.791  44.403  44.989 1.00 25.15 ? 198 ARG B N   1 
ATOM   3247 C  CA  . ARG B  1 8   ? 86.466  44.972  44.765 1.00 24.96 ? 198 ARG B CA  1 
ATOM   3248 C  C   . ARG B  1 8   ? 86.499  46.320  45.469 1.00 23.39 ? 198 ARG B C   1 
ATOM   3249 O  O   . ARG B  1 8   ? 87.318  46.529  46.366 1.00 21.09 ? 198 ARG B O   1 
ATOM   3250 C  CB  . ARG B  1 8   ? 85.380  44.100  45.397 1.00 32.18 ? 198 ARG B CB  1 
ATOM   3251 C  CG  . ARG B  1 8   ? 85.096  42.804  44.663 1.00 42.49 ? 198 ARG B CG  1 
ATOM   3252 C  CD  . ARG B  1 8   ? 84.425  43.067  43.326 1.00 46.13 ? 198 ARG B CD  1 
ATOM   3253 N  NE  . ARG B  1 8   ? 84.086  41.827  42.631 1.00 50.66 ? 198 ARG B NE  1 
ATOM   3254 C  CZ  . ARG B  1 8   ? 84.978  40.941  42.197 1.00 50.18 ? 198 ARG B CZ  1 
ATOM   3255 N  NH1 . ARG B  1 8   ? 86.275  41.148  42.384 1.00 47.24 ? 198 ARG B NH1 1 
ATOM   3256 N  NH2 . ARG B  1 8   ? 84.570  39.844  41.573 1.00 51.45 ? 198 ARG B NH2 1 
ATOM   3257 N  N   . PHE B  1 9   ? 85.623  47.238  45.077 1.00 21.37 ? 199 PHE B N   1 
ATOM   3258 C  CA  . PHE B  1 9   ? 85.607  48.548  45.714 1.00 16.23 ? 199 PHE B CA  1 
ATOM   3259 C  C   . PHE B  1 9   ? 84.217  48.937  46.175 1.00 16.27 ? 199 PHE B C   1 
ATOM   3260 O  O   . PHE B  1 9   ? 83.225  48.624  45.520 1.00 23.92 ? 199 PHE B O   1 
ATOM   3261 C  CB  . PHE B  1 9   ? 86.130  49.621  44.758 1.00 14.96 ? 199 PHE B CB  1 
ATOM   3262 C  CG  . PHE B  1 9   ? 87.446  49.283  44.120 1.00 14.89 ? 199 PHE B CG  1 
ATOM   3263 C  CD1 . PHE B  1 9   ? 87.509  48.387  43.055 1.00 16.49 ? 199 PHE B CD1 1 
ATOM   3264 C  CD2 . PHE B  1 9   ? 88.624  49.870  44.573 1.00 17.49 ? 199 PHE B CD2 1 
ATOM   3265 C  CE1 . PHE B  1 9   ? 88.728  48.083  42.447 1.00 22.79 ? 199 PHE B CE1 1 
ATOM   3266 C  CE2 . PHE B  1 9   ? 89.851  49.573  43.973 1.00 20.28 ? 199 PHE B CE2 1 
ATOM   3267 C  CZ  . PHE B  1 9   ? 89.902  48.678  42.908 1.00 21.01 ? 199 PHE B CZ  1 
ATOM   3268 N  N   . VAL B  1 10  ? 84.152  49.618  47.312 1.00 18.21 ? 200 VAL B N   1 
ATOM   3269 C  CA  . VAL B  1 10  ? 82.882  50.080  47.860 1.00 17.45 ? 200 VAL B CA  1 
ATOM   3270 C  C   . VAL B  1 10  ? 82.935  51.596  47.963 1.00 17.67 ? 200 VAL B C   1 
ATOM   3271 O  O   . VAL B  1 10  ? 83.694  52.146  48.762 1.00 14.91 ? 200 VAL B O   1 
ATOM   3272 C  CB  . VAL B  1 10  ? 82.612  49.493  49.268 1.00 21.01 ? 200 VAL B CB  1 
ATOM   3273 C  CG1 . VAL B  1 10  ? 81.360  50.123  49.866 1.00 20.63 ? 200 VAL B CG1 1 
ATOM   3274 C  CG2 . VAL B  1 10  ? 82.438  47.985  49.180 1.00 24.14 ? 200 VAL B CG2 1 
ATOM   3275 N  N   . GLU B  1 11  ? 82.141  52.268  47.137 1.00 17.53 ? 201 GLU B N   1 
ATOM   3276 C  CA  . GLU B  1 11  ? 82.103  53.721  47.150 1.00 20.25 ? 201 GLU B CA  1 
ATOM   3277 C  C   . GLU B  1 11  ? 81.108  54.174  48.209 1.00 18.29 ? 201 GLU B C   1 
ATOM   3278 O  O   . GLU B  1 11  ? 79.896  54.195  47.991 1.00 14.79 ? 201 GLU B O   1 
ATOM   3279 C  CB  . GLU B  1 11  ? 81.746  54.241  45.757 1.00 19.19 ? 201 GLU B CB  1 
ATOM   3280 C  CG  . GLU B  1 11  ? 82.875  54.002  44.763 1.00 21.30 ? 201 GLU B CG  1 
ATOM   3281 C  CD  . GLU B  1 11  ? 82.501  54.321  43.333 1.00 27.42 ? 201 GLU B CD  1 
ATOM   3282 O  OE1 . GLU B  1 11  ? 81.594  53.649  42.792 1.00 26.17 ? 201 GLU B OE1 1 
ATOM   3283 O  OE2 . GLU B  1 11  ? 83.121  55.241  42.750 1.00 25.45 ? 201 GLU B OE2 1 
ATOM   3284 N  N   . LEU B  1 12  ? 81.657  54.529  49.366 1.00 18.20 ? 202 LEU B N   1 
ATOM   3285 C  CA  . LEU B  1 12  ? 80.884  54.947  50.527 1.00 18.89 ? 202 LEU B CA  1 
ATOM   3286 C  C   . LEU B  1 12  ? 80.513  56.424  50.613 1.00 18.32 ? 202 LEU B C   1 
ATOM   3287 O  O   . LEU B  1 12  ? 81.227  57.301  50.126 1.00 17.77 ? 202 LEU B O   1 
ATOM   3288 C  CB  . LEU B  1 12  ? 81.644  54.553  51.800 1.00 16.67 ? 202 LEU B CB  1 
ATOM   3289 C  CG  . LEU B  1 12  ? 81.102  55.006  53.157 1.00 18.57 ? 202 LEU B CG  1 
ATOM   3290 C  CD1 . LEU B  1 12  ? 79.737  54.381  53.412 1.00 19.82 ? 202 LEU B CD1 1 
ATOM   3291 C  CD2 . LEU B  1 12  ? 82.077  54.605  54.246 1.00 18.74 ? 202 LEU B CD2 1 
ATOM   3292 N  N   . VAL B  1 13  ? 79.373  56.672  51.248 1.00 19.39 ? 203 VAL B N   1 
ATOM   3293 C  CA  . VAL B  1 13  ? 78.866  58.013  51.484 1.00 18.47 ? 203 VAL B CA  1 
ATOM   3294 C  C   . VAL B  1 13  ? 78.541  58.042  52.968 1.00 19.53 ? 203 VAL B C   1 
ATOM   3295 O  O   . VAL B  1 13  ? 77.817  57.177  53.461 1.00 22.38 ? 203 VAL B O   1 
ATOM   3296 C  CB  . VAL B  1 13  ? 77.575  58.298  50.688 1.00 15.28 ? 203 VAL B CB  1 
ATOM   3297 C  CG1 . VAL B  1 13  ? 76.913  59.575  51.197 1.00 14.60 ? 203 VAL B CG1 1 
ATOM   3298 C  CG2 . VAL B  1 13  ? 77.902  58.454  49.226 1.00 22.72 ? 203 VAL B CG2 1 
ATOM   3299 N  N   . LEU B  1 14  ? 79.094  59.017  53.680 1.00 16.79 ? 204 LEU B N   1 
ATOM   3300 C  CA  . LEU B  1 14  ? 78.842  59.140  55.106 1.00 16.26 ? 204 LEU B CA  1 
ATOM   3301 C  C   . LEU B  1 14  ? 77.903  60.288  55.416 1.00 19.22 ? 204 LEU B C   1 
ATOM   3302 O  O   . LEU B  1 14  ? 78.055  61.395  54.897 1.00 18.49 ? 204 LEU B O   1 
ATOM   3303 C  CB  . LEU B  1 14  ? 80.149  59.338  55.874 1.00 16.93 ? 204 LEU B CB  1 
ATOM   3304 C  CG  . LEU B  1 14  ? 80.971  58.070  56.095 1.00 22.81 ? 204 LEU B CG  1 
ATOM   3305 C  CD1 . LEU B  1 14  ? 82.208  58.410  56.905 1.00 15.38 ? 204 LEU B CD1 1 
ATOM   3306 C  CD2 . LEU B  1 14  ? 80.120  57.025  56.821 1.00 19.08 ? 204 LEU B CD2 1 
ATOM   3307 N  N   . VAL B  1 15  ? 76.923  60.009  56.265 1.00 17.02 ? 205 VAL B N   1 
ATOM   3308 C  CA  . VAL B  1 15  ? 75.960  61.012  56.674 1.00 16.09 ? 205 VAL B CA  1 
ATOM   3309 C  C   . VAL B  1 15  ? 76.129  61.210  58.174 1.00 16.97 ? 205 VAL B C   1 
ATOM   3310 O  O   . VAL B  1 15  ? 76.082  60.251  58.946 1.00 20.07 ? 205 VAL B O   1 
ATOM   3311 C  CB  . VAL B  1 15  ? 74.520  60.559  56.365 1.00 16.73 ? 205 VAL B CB  1 
ATOM   3312 C  CG1 . VAL B  1 15  ? 73.528  61.637  56.779 1.00 20.61 ? 205 VAL B CG1 1 
ATOM   3313 C  CG2 . VAL B  1 15  ? 74.384  60.263  54.887 1.00 19.36 ? 205 VAL B CG2 1 
ATOM   3314 N  N   . VAL B  1 16  ? 76.350  62.456  58.575 1.00 13.22 ? 206 VAL B N   1 
ATOM   3315 C  CA  . VAL B  1 16  ? 76.533  62.806  59.979 1.00 8.93  ? 206 VAL B CA  1 
ATOM   3316 C  C   . VAL B  1 16  ? 75.319  63.623  60.401 1.00 8.19  ? 206 VAL B C   1 
ATOM   3317 O  O   . VAL B  1 16  ? 75.096  64.713  59.880 1.00 12.86 ? 206 VAL B O   1 
ATOM   3318 C  CB  . VAL B  1 16  ? 77.818  63.635  60.154 1.00 6.77  ? 206 VAL B CB  1 
ATOM   3319 C  CG1 . VAL B  1 16  ? 77.992  64.044  61.599 1.00 6.89  ? 206 VAL B CG1 1 
ATOM   3320 C  CG2 . VAL B  1 16  ? 79.010  62.827  59.681 1.00 1.00  ? 206 VAL B CG2 1 
ATOM   3321 N  N   . ASP B  1 17  ? 74.538  63.099  61.342 1.00 10.19 ? 207 ASP B N   1 
ATOM   3322 C  CA  . ASP B  1 17  ? 73.323  63.782  61.786 1.00 13.26 ? 207 ASP B CA  1 
ATOM   3323 C  C   . ASP B  1 17  ? 73.539  64.999  62.675 1.00 15.30 ? 207 ASP B C   1 
ATOM   3324 O  O   . ASP B  1 17  ? 74.663  65.312  63.082 1.00 9.81  ? 207 ASP B O   1 
ATOM   3325 C  CB  . ASP B  1 17  ? 72.373  62.792  62.479 1.00 14.05 ? 207 ASP B CB  1 
ATOM   3326 C  CG  . ASP B  1 17  ? 72.814  62.431  63.889 1.00 21.08 ? 207 ASP B CG  1 
ATOM   3327 O  OD1 . ASP B  1 17  ? 74.035  62.443  64.165 1.00 27.64 ? 207 ASP B OD1 1 
ATOM   3328 O  OD2 . ASP B  1 17  ? 71.934  62.117  64.720 1.00 13.35 ? 207 ASP B OD2 1 
ATOM   3329 N  N   . LYS B  1 18  ? 72.434  65.682  62.960 1.00 18.71 ? 208 LYS B N   1 
ATOM   3330 C  CA  . LYS B  1 18  ? 72.425  66.892  63.775 1.00 20.27 ? 208 LYS B CA  1 
ATOM   3331 C  C   . LYS B  1 18  ? 73.072  66.701  65.143 1.00 17.83 ? 208 LYS B C   1 
ATOM   3332 O  O   . LYS B  1 18  ? 73.813  67.568  65.612 1.00 17.61 ? 208 LYS B O   1 
ATOM   3333 C  CB  . LYS B  1 18  ? 70.982  67.380  63.942 1.00 16.86 ? 208 LYS B CB  1 
ATOM   3334 C  CG  . LYS B  1 18  ? 70.823  68.675  64.719 1.00 19.77 ? 208 LYS B CG  1 
ATOM   3335 C  CD  . LYS B  1 18  ? 71.500  69.849  64.024 1.00 23.15 ? 208 LYS B CD  1 
ATOM   3336 C  CE  . LYS B  1 18  ? 71.147  71.160  64.715 1.00 22.36 ? 208 LYS B CE  1 
ATOM   3337 N  NZ  . LYS B  1 18  ? 71.897  72.323  64.166 1.00 22.61 ? 208 LYS B NZ  1 
ATOM   3338 N  N   . ALA B  1 19  ? 72.789  65.568  65.779 1.00 12.74 ? 209 ALA B N   1 
ATOM   3339 C  CA  . ALA B  1 19  ? 73.343  65.283  67.096 1.00 14.75 ? 209 ALA B CA  1 
ATOM   3340 C  C   . ALA B  1 19  ? 74.865  65.306  67.055 1.00 12.18 ? 209 ALA B C   1 
ATOM   3341 O  O   . ALA B  1 19  ? 75.507  65.922  67.905 1.00 17.10 ? 209 ALA B O   1 
ATOM   3342 C  CB  . ALA B  1 19  ? 72.844  63.927  67.596 1.00 10.85 ? 209 ALA B CB  1 
ATOM   3343 N  N   . MET B  1 20  ? 75.440  64.629  66.069 1.00 11.85 ? 210 MET B N   1 
ATOM   3344 C  CA  . MET B  1 20  ? 76.889  64.591  65.923 1.00 15.35 ? 210 MET B CA  1 
ATOM   3345 C  C   . MET B  1 20  ? 77.459  66.000  65.813 1.00 15.39 ? 210 MET B C   1 
ATOM   3346 O  O   . MET B  1 20  ? 78.498  66.306  66.396 1.00 14.15 ? 210 MET B O   1 
ATOM   3347 C  CB  . MET B  1 20  ? 77.276  63.787  64.683 1.00 12.29 ? 210 MET B CB  1 
ATOM   3348 C  CG  . MET B  1 20  ? 77.487  62.314  64.943 1.00 16.89 ? 210 MET B CG  1 
ATOM   3349 S  SD  . MET B  1 20  ? 78.950  62.040  65.960 1.00 31.03 ? 210 MET B SD  1 
ATOM   3350 C  CE  . MET B  1 20  ? 80.228  61.989  64.699 1.00 19.30 ? 210 MET B CE  1 
ATOM   3351 N  N   . VAL B  1 21  ? 76.774  66.854  65.063 1.00 14.92 ? 211 VAL B N   1 
ATOM   3352 C  CA  . VAL B  1 21  ? 77.227  68.224  64.889 1.00 15.35 ? 211 VAL B CA  1 
ATOM   3353 C  C   . VAL B  1 21  ? 77.216  68.943  66.231 1.00 15.69 ? 211 VAL B C   1 
ATOM   3354 O  O   . VAL B  1 21  ? 78.157  69.664  66.569 1.00 18.45 ? 211 VAL B O   1 
ATOM   3355 C  CB  . VAL B  1 21  ? 76.327  68.989  63.896 1.00 16.16 ? 211 VAL B CB  1 
ATOM   3356 C  CG1 . VAL B  1 21  ? 76.837  70.410  63.726 1.00 16.01 ? 211 VAL B CG1 1 
ATOM   3357 C  CG2 . VAL B  1 21  ? 76.310  68.269  62.555 1.00 14.30 ? 211 VAL B CG2 1 
ATOM   3358 N  N   . THR B  1 22  ? 76.151  68.741  66.999 1.00 7.99  ? 212 THR B N   1 
ATOM   3359 C  CA  . THR B  1 22  ? 76.035  69.373  68.303 1.00 7.15  ? 212 THR B CA  1 
ATOM   3360 C  C   . THR B  1 22  ? 77.098  68.824  69.249 1.00 10.39 ? 212 THR B C   1 
ATOM   3361 O  O   . THR B  1 22  ? 77.692  69.572  70.028 1.00 12.96 ? 212 THR B O   1 
ATOM   3362 C  CB  . THR B  1 22  ? 74.642  69.134  68.904 1.00 6.49  ? 212 THR B CB  1 
ATOM   3363 O  OG1 . THR B  1 22  ? 73.649  69.615  67.989 1.00 9.47  ? 212 THR B OG1 1 
ATOM   3364 C  CG2 . THR B  1 22  ? 74.493  69.862  70.237 1.00 1.00  ? 212 THR B CG2 1 
ATOM   3365 N  N   . LYS B  1 23  ? 77.339  67.518  69.163 1.00 8.19  ? 213 LYS B N   1 
ATOM   3366 C  CA  . LYS B  1 23  ? 78.334  66.859  70.002 1.00 9.92  ? 213 LYS B CA  1 
ATOM   3367 C  C   . LYS B  1 23  ? 79.732  67.410  69.766 1.00 11.94 ? 213 LYS B C   1 
ATOM   3368 O  O   . LYS B  1 23  ? 80.609  67.271  70.615 1.00 13.30 ? 213 LYS B O   1 
ATOM   3369 C  CB  . LYS B  1 23  ? 78.347  65.354  69.735 1.00 7.06  ? 213 LYS B CB  1 
ATOM   3370 C  CG  . LYS B  1 23  ? 79.346  64.593  70.593 1.00 5.06  ? 213 LYS B CG  1 
ATOM   3371 C  CD  . LYS B  1 23  ? 79.267  63.102  70.324 1.00 7.39  ? 213 LYS B CD  1 
ATOM   3372 C  CE  . LYS B  1 23  ? 80.126  62.302  71.288 1.00 1.00  ? 213 LYS B CE  1 
ATOM   3373 N  NZ  . LYS B  1 23  ? 79.905  60.837  71.092 1.00 11.36 ? 213 LYS B NZ  1 
ATOM   3374 N  N   . ASN B  1 24  ? 79.934  68.024  68.605 1.00 15.72 ? 214 ASN B N   1 
ATOM   3375 C  CA  . ASN B  1 24  ? 81.228  68.593  68.252 1.00 14.49 ? 214 ASN B CA  1 
ATOM   3376 C  C   . ASN B  1 24  ? 81.203  70.116  68.216 1.00 18.20 ? 214 ASN B C   1 
ATOM   3377 O  O   . ASN B  1 24  ? 82.103  70.752  67.665 1.00 18.38 ? 214 ASN B O   1 
ATOM   3378 C  CB  . ASN B  1 24  ? 81.692  68.032  66.910 1.00 13.51 ? 214 ASN B CB  1 
ATOM   3379 C  CG  . ASN B  1 24  ? 82.225  66.620  67.032 1.00 17.16 ? 214 ASN B CG  1 
ATOM   3380 O  OD1 . ASN B  1 24  ? 83.428  66.411  67.181 1.00 17.32 ? 214 ASN B OD1 1 
ATOM   3381 N  ND2 . ASN B  1 24  ? 81.327  65.641  66.990 1.00 17.24 ? 214 ASN B ND2 1 
ATOM   3382 N  N   . ASN B  1 25  ? 80.158  70.695  68.796 1.00 13.38 ? 215 ASN B N   1 
ATOM   3383 C  CA  . ASN B  1 25  ? 80.037  72.141  68.876 1.00 14.96 ? 215 ASN B CA  1 
ATOM   3384 C  C   . ASN B  1 25  ? 80.092  72.855  67.527 1.00 14.54 ? 215 ASN B C   1 
ATOM   3385 O  O   . ASN B  1 25  ? 80.796  73.851  67.375 1.00 16.32 ? 215 ASN B O   1 
ATOM   3386 C  CB  . ASN B  1 25  ? 81.140  72.670  69.794 1.00 10.48 ? 215 ASN B CB  1 
ATOM   3387 C  CG  . ASN B  1 25  ? 81.179  71.944  71.130 1.00 9.39  ? 215 ASN B CG  1 
ATOM   3388 O  OD1 . ASN B  1 25  ? 82.248  71.680  71.672 1.00 11.67 ? 215 ASN B OD1 1 
ATOM   3389 N  ND2 . ASN B  1 25  ? 80.008  71.627  71.668 1.00 5.72  ? 215 ASN B ND2 1 
ATOM   3390 N  N   . GLY B  1 26  ? 79.346  72.342  66.556 1.00 15.78 ? 216 GLY B N   1 
ATOM   3391 C  CA  . GLY B  1 26  ? 79.300  72.951  65.236 1.00 13.73 ? 216 GLY B CA  1 
ATOM   3392 C  C   . GLY B  1 26  ? 80.612  73.041  64.481 1.00 15.42 ? 216 GLY B C   1 
ATOM   3393 O  O   . GLY B  1 26  ? 80.681  73.691  63.437 1.00 17.77 ? 216 GLY B O   1 
ATOM   3394 N  N   . ASP B  1 27  ? 81.648  72.385  64.995 1.00 16.97 ? 217 ASP B N   1 
ATOM   3395 C  CA  . ASP B  1 27  ? 82.965  72.406  64.366 1.00 18.99 ? 217 ASP B CA  1 
ATOM   3396 C  C   . ASP B  1 27  ? 83.015  71.399  63.214 1.00 21.32 ? 217 ASP B C   1 
ATOM   3397 O  O   . ASP B  1 27  ? 83.459  70.262  63.380 1.00 20.83 ? 217 ASP B O   1 
ATOM   3398 C  CB  . ASP B  1 27  ? 84.029  72.089  65.423 1.00 21.30 ? 217 ASP B CB  1 
ATOM   3399 C  CG  . ASP B  1 27  ? 85.448  72.338  64.934 1.00 27.72 ? 217 ASP B CG  1 
ATOM   3400 O  OD1 . ASP B  1 27  ? 86.351  72.435  65.794 1.00 31.08 ? 217 ASP B OD1 1 
ATOM   3401 O  OD2 . ASP B  1 27  ? 85.666  72.429  63.705 1.00 30.05 ? 217 ASP B OD2 1 
ATOM   3402 N  N   . LEU B  1 28  ? 82.559  71.838  62.045 1.00 19.44 ? 218 LEU B N   1 
ATOM   3403 C  CA  . LEU B  1 28  ? 82.512  70.997  60.853 1.00 19.17 ? 218 LEU B CA  1 
ATOM   3404 C  C   . LEU B  1 28  ? 83.849  70.485  60.327 1.00 19.39 ? 218 LEU B C   1 
ATOM   3405 O  O   . LEU B  1 28  ? 83.922  69.372  59.807 1.00 23.25 ? 218 LEU B O   1 
ATOM   3406 C  CB  . LEU B  1 28  ? 81.773  71.733  59.733 1.00 17.69 ? 218 LEU B CB  1 
ATOM   3407 C  CG  . LEU B  1 28  ? 80.246  71.625  59.712 1.00 10.75 ? 218 LEU B CG  1 
ATOM   3408 C  CD1 . LEU B  1 28  ? 79.671  71.896  61.083 1.00 8.40  ? 218 LEU B CD1 1 
ATOM   3409 C  CD2 . LEU B  1 28  ? 79.701  72.603  58.693 1.00 6.60  ? 218 LEU B CD2 1 
ATOM   3410 N  N   . ASP B  1 29  ? 84.901  71.287  60.442 1.00 22.99 ? 219 ASP B N   1 
ATOM   3411 C  CA  . ASP B  1 29  ? 86.209  70.854  59.966 1.00 25.73 ? 219 ASP B CA  1 
ATOM   3412 C  C   . ASP B  1 29  ? 86.713  69.700  60.817 1.00 24.72 ? 219 ASP B C   1 
ATOM   3413 O  O   . ASP B  1 29  ? 87.267  68.730  60.300 1.00 25.91 ? 219 ASP B O   1 
ATOM   3414 C  CB  . ASP B  1 29  ? 87.218  72.003  60.011 1.00 31.01 ? 219 ASP B CB  1 
ATOM   3415 C  CG  . ASP B  1 29  ? 87.014  73.000  58.890 1.00 43.26 ? 219 ASP B CG  1 
ATOM   3416 O  OD1 . ASP B  1 29  ? 86.993  72.576  57.712 1.00 42.23 ? 219 ASP B OD1 1 
ATOM   3417 O  OD2 . ASP B  1 29  ? 86.882  74.208  59.185 1.00 55.16 ? 219 ASP B OD2 1 
ATOM   3418 N  N   . LYS B  1 30  ? 86.518  69.809  62.127 1.00 23.16 ? 220 LYS B N   1 
ATOM   3419 C  CA  . LYS B  1 30  ? 86.952  68.764  63.040 1.00 22.59 ? 220 LYS B CA  1 
ATOM   3420 C  C   . LYS B  1 30  ? 86.264  67.455  62.665 1.00 21.72 ? 220 LYS B C   1 
ATOM   3421 O  O   . LYS B  1 30  ? 86.909  66.409  62.569 1.00 23.60 ? 220 LYS B O   1 
ATOM   3422 C  CB  . LYS B  1 30  ? 86.611  69.141  64.484 1.00 19.94 ? 220 LYS B CB  1 
ATOM   3423 C  CG  . LYS B  1 30  ? 87.094  68.126  65.503 1.00 23.03 ? 220 LYS B CG  1 
ATOM   3424 C  CD  . LYS B  1 30  ? 86.768  68.551  66.921 1.00 31.42 ? 220 LYS B CD  1 
ATOM   3425 C  CE  . LYS B  1 30  ? 87.300  67.541  67.927 1.00 38.31 ? 220 LYS B CE  1 
ATOM   3426 N  NZ  . LYS B  1 30  ? 86.933  67.889  69.330 1.00 43.56 ? 220 LYS B NZ  1 
ATOM   3427 N  N   . ILE B  1 31  ? 84.954  67.530  62.442 1.00 17.21 ? 221 ILE B N   1 
ATOM   3428 C  CA  . ILE B  1 31  ? 84.157  66.368  62.074 1.00 15.49 ? 221 ILE B CA  1 
ATOM   3429 C  C   . ILE B  1 31  ? 84.614  65.751  60.760 1.00 19.01 ? 221 ILE B C   1 
ATOM   3430 O  O   . ILE B  1 31  ? 84.778  64.533  60.666 1.00 14.65 ? 221 ILE B O   1 
ATOM   3431 C  CB  . ILE B  1 31  ? 82.655  66.733  61.940 1.00 19.16 ? 221 ILE B CB  1 
ATOM   3432 C  CG1 . ILE B  1 31  ? 82.090  67.136  63.307 1.00 13.51 ? 221 ILE B CG1 1 
ATOM   3433 C  CG2 . ILE B  1 31  ? 81.874  65.549  61.352 1.00 9.76  ? 221 ILE B CG2 1 
ATOM   3434 C  CD1 . ILE B  1 31  ? 80.642  67.573  63.268 1.00 6.50  ? 221 ILE B CD1 1 
ATOM   3435 N  N   . LYS B  1 32  ? 84.812  66.591  59.748 1.00 17.43 ? 222 LYS B N   1 
ATOM   3436 C  CA  . LYS B  1 32  ? 85.232  66.115  58.433 1.00 22.94 ? 222 LYS B CA  1 
ATOM   3437 C  C   . LYS B  1 32  ? 86.565  65.377  58.450 1.00 23.62 ? 222 LYS B C   1 
ATOM   3438 O  O   . LYS B  1 32  ? 86.680  64.276  57.910 1.00 23.96 ? 222 LYS B O   1 
ATOM   3439 C  CB  . LYS B  1 32  ? 85.316  67.278  57.446 1.00 20.92 ? 222 LYS B CB  1 
ATOM   3440 C  CG  . LYS B  1 32  ? 83.978  67.904  57.105 1.00 26.98 ? 222 LYS B CG  1 
ATOM   3441 C  CD  . LYS B  1 32  ? 84.156  69.085  56.160 1.00 26.18 ? 222 LYS B CD  1 
ATOM   3442 C  CE  . LYS B  1 32  ? 82.824  69.711  55.794 1.00 24.76 ? 222 LYS B CE  1 
ATOM   3443 N  NZ  . LYS B  1 32  ? 83.013  70.874  54.886 1.00 30.98 ? 222 LYS B NZ  1 
ATOM   3444 N  N   . THR B  1 33  ? 87.573  65.985  59.064 1.00 23.79 ? 223 THR B N   1 
ATOM   3445 C  CA  . THR B  1 33  ? 88.888  65.366  59.122 1.00 24.26 ? 223 THR B CA  1 
ATOM   3446 C  C   . THR B  1 33  ? 88.852  64.040  59.868 1.00 22.85 ? 223 THR B C   1 
ATOM   3447 O  O   . THR B  1 33  ? 89.589  63.113  59.524 1.00 25.55 ? 223 THR B O   1 
ATOM   3448 C  CB  . THR B  1 33  ? 89.915  66.292  59.794 1.00 22.99 ? 223 THR B CB  1 
ATOM   3449 O  OG1 . THR B  1 33  ? 89.422  66.699  61.075 1.00 31.91 ? 223 THR B OG1 1 
ATOM   3450 C  CG2 . THR B  1 33  ? 90.161  67.520  58.936 1.00 21.15 ? 223 THR B CG2 1 
ATOM   3451 N  N   . ARG B  1 34  ? 87.999  63.941  60.885 1.00 16.26 ? 224 ARG B N   1 
ATOM   3452 C  CA  . ARG B  1 34  ? 87.903  62.698  61.643 1.00 14.09 ? 224 ARG B CA  1 
ATOM   3453 C  C   . ARG B  1 34  ? 87.306  61.597  60.766 1.00 13.52 ? 224 ARG B C   1 
ATOM   3454 O  O   . ARG B  1 34  ? 87.814  60.477  60.739 1.00 12.33 ? 224 ARG B O   1 
ATOM   3455 C  CB  . ARG B  1 34  ? 87.042  62.876  62.896 1.00 15.94 ? 224 ARG B CB  1 
ATOM   3456 C  CG  . ARG B  1 34  ? 87.213  61.735  63.887 1.00 11.52 ? 224 ARG B CG  1 
ATOM   3457 C  CD  . ARG B  1 34  ? 86.130  61.719  64.944 1.00 19.58 ? 224 ARG B CD  1 
ATOM   3458 N  NE  . ARG B  1 34  ? 86.281  60.575  65.842 1.00 18.73 ? 224 ARG B NE  1 
ATOM   3459 C  CZ  . ARG B  1 34  ? 85.307  60.086  66.603 1.00 11.78 ? 224 ARG B CZ  1 
ATOM   3460 N  NH1 . ARG B  1 34  ? 84.101  60.637  66.580 1.00 12.27 ? 224 ARG B NH1 1 
ATOM   3461 N  NH2 . ARG B  1 34  ? 85.538  59.040  67.381 1.00 1.70  ? 224 ARG B NH2 1 
ATOM   3462 N  N   . MET B  1 35  ? 86.230  61.921  60.052 1.00 12.25 ? 225 MET B N   1 
ATOM   3463 C  CA  . MET B  1 35  ? 85.578  60.970  59.158 1.00 11.98 ? 225 MET B CA  1 
ATOM   3464 C  C   . MET B  1 35  ? 86.588  60.460  58.139 1.00 14.64 ? 225 MET B C   1 
ATOM   3465 O  O   . MET B  1 35  ? 86.509  59.321  57.688 1.00 19.61 ? 225 MET B O   1 
ATOM   3466 C  CB  . MET B  1 35  ? 84.414  61.633  58.424 1.00 13.96 ? 225 MET B CB  1 
ATOM   3467 C  CG  . MET B  1 35  ? 83.346  62.208  59.340 1.00 22.42 ? 225 MET B CG  1 
ATOM   3468 S  SD  . MET B  1 35  ? 82.639  60.977  60.446 1.00 20.10 ? 225 MET B SD  1 
ATOM   3469 C  CE  . MET B  1 35  ? 81.378  60.301  59.396 1.00 35.98 ? 225 MET B CE  1 
ATOM   3470 N  N   . TYR B  1 36  ? 87.534  61.315  57.768 1.00 11.52 ? 226 TYR B N   1 
ATOM   3471 C  CA  . TYR B  1 36  ? 88.568  60.927  56.820 1.00 14.83 ? 226 TYR B CA  1 
ATOM   3472 C  C   . TYR B  1 36  ? 89.426  59.838  57.456 1.00 10.87 ? 226 TYR B C   1 
ATOM   3473 O  O   . TYR B  1 36  ? 89.779  58.859  56.808 1.00 13.56 ? 226 TYR B O   1 
ATOM   3474 C  CB  . TYR B  1 36  ? 89.423  62.145  56.455 1.00 16.31 ? 226 TYR B CB  1 
ATOM   3475 C  CG  . TYR B  1 36  ? 88.660  63.208  55.700 1.00 17.72 ? 226 TYR B CG  1 
ATOM   3476 C  CD1 . TYR B  1 36  ? 89.108  64.527  55.664 1.00 15.86 ? 226 TYR B CD1 1 
ATOM   3477 C  CD2 . TYR B  1 36  ? 87.473  62.898  55.037 1.00 16.97 ? 226 TYR B CD2 1 
ATOM   3478 C  CE1 . TYR B  1 36  ? 88.387  65.511  54.990 1.00 11.93 ? 226 TYR B CE1 1 
ATOM   3479 C  CE2 . TYR B  1 36  ? 86.750  63.871  54.362 1.00 14.05 ? 226 TYR B CE2 1 
ATOM   3480 C  CZ  . TYR B  1 36  ? 87.209  65.172  54.344 1.00 16.58 ? 226 TYR B CZ  1 
ATOM   3481 O  OH  . TYR B  1 36  ? 86.475  66.133  53.685 1.00 31.31 ? 226 TYR B OH  1 
ATOM   3482 N  N   . GLU B  1 37  ? 89.750  60.021  58.732 1.00 15.15 ? 227 GLU B N   1 
ATOM   3483 C  CA  . GLU B  1 37  ? 90.543  59.060  59.494 1.00 20.78 ? 227 GLU B CA  1 
ATOM   3484 C  C   . GLU B  1 37  ? 89.826  57.711  59.553 1.00 21.65 ? 227 GLU B C   1 
ATOM   3485 O  O   . GLU B  1 37  ? 90.365  56.678  59.150 1.00 19.63 ? 227 GLU B O   1 
ATOM   3486 C  CB  . GLU B  1 37  ? 90.735  59.561  60.926 1.00 25.23 ? 227 GLU B CB  1 
ATOM   3487 C  CG  . GLU B  1 37  ? 91.615  60.775  61.068 1.00 39.72 ? 227 GLU B CG  1 
ATOM   3488 C  CD  . GLU B  1 37  ? 93.076  60.406  61.132 1.00 50.15 ? 227 GLU B CD  1 
ATOM   3489 O  OE1 . GLU B  1 37  ? 93.442  59.624  62.035 1.00 55.94 ? 227 GLU B OE1 1 
ATOM   3490 O  OE2 . GLU B  1 37  ? 93.856  60.896  60.285 1.00 58.06 ? 227 GLU B OE2 1 
ATOM   3491 N  N   . ILE B  1 38  ? 88.604  57.741  60.075 1.00 14.64 ? 228 ILE B N   1 
ATOM   3492 C  CA  . ILE B  1 38  ? 87.789  56.546  60.226 1.00 17.23 ? 228 ILE B CA  1 
ATOM   3493 C  C   . ILE B  1 38  ? 87.621  55.752  58.931 1.00 15.63 ? 228 ILE B C   1 
ATOM   3494 O  O   . ILE B  1 38  ? 87.905  54.556  58.894 1.00 13.80 ? 228 ILE B O   1 
ATOM   3495 C  CB  . ILE B  1 38  ? 86.396  56.918  60.791 1.00 14.61 ? 228 ILE B CB  1 
ATOM   3496 C  CG1 . ILE B  1 38  ? 86.561  57.538  62.181 1.00 13.10 ? 228 ILE B CG1 1 
ATOM   3497 C  CG2 . ILE B  1 38  ? 85.510  55.685  60.865 1.00 17.02 ? 228 ILE B CG2 1 
ATOM   3498 C  CD1 . ILE B  1 38  ? 85.272  58.021  62.805 1.00 12.44 ? 228 ILE B CD1 1 
ATOM   3499 N  N   . VAL B  1 39  ? 87.159  56.414  57.875 1.00 16.90 ? 229 VAL B N   1 
ATOM   3500 C  CA  . VAL B  1 39  ? 86.951  55.749  56.592 1.00 16.09 ? 229 VAL B CA  1 
ATOM   3501 C  C   . VAL B  1 39  ? 88.240  55.117  56.092 1.00 17.70 ? 229 VAL B C   1 
ATOM   3502 O  O   . VAL B  1 39  ? 88.227  54.017  55.537 1.00 15.18 ? 229 VAL B O   1 
ATOM   3503 C  CB  . VAL B  1 39  ? 86.444  56.734  55.518 1.00 19.22 ? 229 VAL B CB  1 
ATOM   3504 C  CG1 . VAL B  1 39  ? 86.241  56.007  54.197 1.00 17.61 ? 229 VAL B CG1 1 
ATOM   3505 C  CG2 . VAL B  1 39  ? 85.147  57.371  55.970 1.00 21.87 ? 229 VAL B CG2 1 
ATOM   3506 N  N   . ASN B  1 40  ? 89.358  55.809  56.292 1.00 18.07 ? 230 ASN B N   1 
ATOM   3507 C  CA  . ASN B  1 40  ? 90.635  55.278  55.844 1.00 21.20 ? 230 ASN B CA  1 
ATOM   3508 C  C   . ASN B  1 40  ? 91.084  54.071  56.666 1.00 23.43 ? 230 ASN B C   1 
ATOM   3509 O  O   . ASN B  1 40  ? 91.788  53.198  56.159 1.00 30.98 ? 230 ASN B O   1 
ATOM   3510 C  CB  . ASN B  1 40  ? 91.703  56.361  55.874 1.00 21.59 ? 230 ASN B CB  1 
ATOM   3511 C  CG  . ASN B  1 40  ? 92.875  56.026  54.983 1.00 36.01 ? 230 ASN B CG  1 
ATOM   3512 O  OD1 . ASN B  1 40  ? 93.877  55.461  55.434 1.00 40.04 ? 230 ASN B OD1 1 
ATOM   3513 N  ND2 . ASN B  1 40  ? 92.746  56.349  53.694 1.00 28.91 ? 230 ASN B ND2 1 
ATOM   3514 N  N   . THR B  1 41  ? 90.678  54.019  57.932 1.00 20.51 ? 231 THR B N   1 
ATOM   3515 C  CA  . THR B  1 41  ? 91.025  52.893  58.790 1.00 13.62 ? 231 THR B CA  1 
ATOM   3516 C  C   . THR B  1 41  ? 90.139  51.708  58.397 1.00 13.58 ? 231 THR B C   1 
ATOM   3517 O  O   . THR B  1 41  ? 90.565  50.549  58.447 1.00 13.12 ? 231 THR B O   1 
ATOM   3518 C  CB  . THR B  1 41  ? 90.801  53.233  60.268 1.00 15.00 ? 231 THR B CB  1 
ATOM   3519 O  OG1 . THR B  1 41  ? 91.636  54.338  60.629 1.00 19.30 ? 231 THR B OG1 1 
ATOM   3520 C  CG2 . THR B  1 41  ? 91.147  52.047  61.151 1.00 19.21 ? 231 THR B CG2 1 
ATOM   3521 N  N   . VAL B  1 42  ? 88.905  52.009  58.000 1.00 5.77  ? 232 VAL B N   1 
ATOM   3522 C  CA  . VAL B  1 42  ? 87.973  50.978  57.568 1.00 5.86  ? 232 VAL B CA  1 
ATOM   3523 C  C   . VAL B  1 42  ? 88.557  50.321  56.322 1.00 16.51 ? 232 VAL B C   1 
ATOM   3524 O  O   . VAL B  1 42  ? 88.476  49.104  56.145 1.00 22.73 ? 232 VAL B O   1 
ATOM   3525 C  CB  . VAL B  1 42  ? 86.601  51.577  57.216 1.00 5.88  ? 232 VAL B CB  1 
ATOM   3526 C  CG1 . VAL B  1 42  ? 85.731  50.523  56.545 1.00 1.00  ? 232 VAL B CG1 1 
ATOM   3527 C  CG2 . VAL B  1 42  ? 85.925  52.108  58.479 1.00 4.05  ? 232 VAL B CG2 1 
ATOM   3528 N  N   . ASN B  1 43  ? 89.151  51.142  55.460 1.00 19.76 ? 233 ASN B N   1 
ATOM   3529 C  CA  . ASN B  1 43  ? 89.759  50.653  54.233 1.00 16.13 ? 233 ASN B CA  1 
ATOM   3530 C  C   . ASN B  1 43  ? 90.902  49.697  54.567 1.00 20.09 ? 233 ASN B C   1 
ATOM   3531 O  O   . ASN B  1 43  ? 91.128  48.714  53.861 1.00 23.72 ? 233 ASN B O   1 
ATOM   3532 C  CB  . ASN B  1 43  ? 90.290  51.826  53.406 1.00 11.95 ? 233 ASN B CB  1 
ATOM   3533 C  CG  . ASN B  1 43  ? 90.844  51.388  52.064 1.00 10.42 ? 233 ASN B CG  1 
ATOM   3534 O  OD1 . ASN B  1 43  ? 90.136  50.796  51.251 1.00 13.95 ? 233 ASN B OD1 1 
ATOM   3535 N  ND2 . ASN B  1 43  ? 92.117  51.675  51.828 1.00 13.76 ? 233 ASN B ND2 1 
ATOM   3536 N  N   . GLU B  1 44  ? 91.626  49.992  55.641 1.00 16.80 ? 234 GLU B N   1 
ATOM   3537 C  CA  . GLU B  1 44  ? 92.735  49.143  56.055 1.00 19.71 ? 234 GLU B CA  1 
ATOM   3538 C  C   . GLU B  1 44  ? 92.187  47.805  56.533 1.00 16.80 ? 234 GLU B C   1 
ATOM   3539 O  O   . GLU B  1 44  ? 92.650  46.743  56.114 1.00 12.16 ? 234 GLU B O   1 
ATOM   3540 C  CB  . GLU B  1 44  ? 93.531  49.807  57.185 1.00 26.25 ? 234 GLU B CB  1 
ATOM   3541 C  CG  . GLU B  1 44  ? 94.128  51.155  56.814 1.00 37.87 ? 234 GLU B CG  1 
ATOM   3542 C  CD  . GLU B  1 44  ? 95.011  51.728  57.907 1.00 44.81 ? 234 GLU B CD  1 
ATOM   3543 O  OE1 . GLU B  1 44  ? 94.518  51.907  59.042 1.00 54.48 ? 234 GLU B OE1 1 
ATOM   3544 O  OE2 . GLU B  1 44  ? 96.199  52.004  57.632 1.00 45.94 ? 234 GLU B OE2 1 
ATOM   3545 N  N   . ILE B  1 45  ? 91.188  47.870  57.407 1.00 12.99 ? 235 ILE B N   1 
ATOM   3546 C  CA  . ILE B  1 45  ? 90.564  46.676  57.953 1.00 13.53 ? 235 ILE B CA  1 
ATOM   3547 C  C   . ILE B  1 45  ? 90.087  45.725  56.855 1.00 16.07 ? 235 ILE B C   1 
ATOM   3548 O  O   . ILE B  1 45  ? 90.170  44.505  57.002 1.00 18.69 ? 235 ILE B O   1 
ATOM   3549 C  CB  . ILE B  1 45  ? 89.361  47.046  58.851 1.00 14.81 ? 235 ILE B CB  1 
ATOM   3550 C  CG1 . ILE B  1 45  ? 89.844  47.867  60.050 1.00 10.74 ? 235 ILE B CG1 1 
ATOM   3551 C  CG2 . ILE B  1 45  ? 88.639  45.782  59.315 1.00 10.34 ? 235 ILE B CG2 1 
ATOM   3552 C  CD1 . ILE B  1 45  ? 88.722  48.377  60.938 1.00 11.03 ? 235 ILE B CD1 1 
ATOM   3553 N  N   . TYR B  1 46  ? 89.596  46.289  55.757 1.00 14.19 ? 236 TYR B N   1 
ATOM   3554 C  CA  . TYR B  1 46  ? 89.091  45.497  54.644 1.00 14.94 ? 236 TYR B CA  1 
ATOM   3555 C  C   . TYR B  1 46  ? 90.134  45.044  53.626 1.00 18.49 ? 236 TYR B C   1 
ATOM   3556 O  O   . TYR B  1 46  ? 89.790  44.398  52.634 1.00 22.44 ? 236 TYR B O   1 
ATOM   3557 C  CB  . TYR B  1 46  ? 87.987  46.272  53.926 1.00 11.40 ? 236 TYR B CB  1 
ATOM   3558 C  CG  . TYR B  1 46  ? 86.605  45.973  54.444 1.00 10.66 ? 236 TYR B CG  1 
ATOM   3559 C  CD1 . TYR B  1 46  ? 85.884  44.882  53.963 1.00 7.93  ? 236 TYR B CD1 1 
ATOM   3560 C  CD2 . TYR B  1 46  ? 86.022  46.770  55.430 1.00 10.24 ? 236 TYR B CD2 1 
ATOM   3561 C  CE1 . TYR B  1 46  ? 84.612  44.591  54.450 1.00 14.96 ? 236 TYR B CE1 1 
ATOM   3562 C  CE2 . TYR B  1 46  ? 84.750  46.489  55.928 1.00 10.09 ? 236 TYR B CE2 1 
ATOM   3563 C  CZ  . TYR B  1 46  ? 84.049  45.397  55.433 1.00 14.92 ? 236 TYR B CZ  1 
ATOM   3564 O  OH  . TYR B  1 46  ? 82.787  45.109  55.915 1.00 19.69 ? 236 TYR B OH  1 
ATOM   3565 N  N   . ARG B  1 47  ? 91.399  45.372  53.862 1.00 20.10 ? 237 ARG B N   1 
ATOM   3566 C  CA  . ARG B  1 47  ? 92.462  44.982  52.938 1.00 23.37 ? 237 ARG B CA  1 
ATOM   3567 C  C   . ARG B  1 47  ? 92.568  43.458  52.854 1.00 23.38 ? 237 ARG B C   1 
ATOM   3568 O  O   . ARG B  1 47  ? 92.627  42.882  51.767 1.00 23.42 ? 237 ARG B O   1 
ATOM   3569 C  CB  . ARG B  1 47  ? 93.794  45.583  53.396 1.00 24.60 ? 237 ARG B CB  1 
ATOM   3570 C  CG  . ARG B  1 47  ? 94.960  45.328  52.452 1.00 31.26 ? 237 ARG B CG  1 
ATOM   3571 C  CD  . ARG B  1 47  ? 96.177  46.151  52.859 1.00 34.29 ? 237 ARG B CD  1 
ATOM   3572 N  NE  . ARG B  1 47  ? 97.318  45.945  51.967 1.00 39.10 ? 237 ARG B NE  1 
ATOM   3573 C  CZ  . ARG B  1 47  ? 98.097  44.868  51.971 1.00 38.23 ? 237 ARG B CZ  1 
ATOM   3574 N  NH1 . ARG B  1 47  ? 97.871  43.880  52.825 1.00 31.59 ? 237 ARG B NH1 1 
ATOM   3575 N  NH2 . ARG B  1 47  ? 99.106  44.778  51.116 1.00 44.06 ? 237 ARG B NH2 1 
ATOM   3576 N  N   . TYR B  1 48  ? 92.588  42.817  54.018 1.00 23.06 ? 238 TYR B N   1 
ATOM   3577 C  CA  . TYR B  1 48  ? 92.676  41.365  54.132 1.00 22.11 ? 238 TYR B CA  1 
ATOM   3578 C  C   . TYR B  1 48  ? 91.523  40.701  53.388 1.00 24.78 ? 238 TYR B C   1 
ATOM   3579 O  O   . TYR B  1 48  ? 91.625  39.554  52.956 1.00 27.03 ? 238 TYR B O   1 
ATOM   3580 C  CB  . TYR B  1 48  ? 92.644  40.996  55.618 1.00 26.45 ? 238 TYR B CB  1 
ATOM   3581 C  CG  . TYR B  1 48  ? 92.197  39.590  55.958 1.00 27.67 ? 238 TYR B CG  1 
ATOM   3582 C  CD1 . TYR B  1 48  ? 93.071  38.509  55.855 1.00 22.44 ? 238 TYR B CD1 1 
ATOM   3583 C  CD2 . TYR B  1 48  ? 90.905  39.352  56.431 1.00 30.94 ? 238 TYR B CD2 1 
ATOM   3584 C  CE1 . TYR B  1 48  ? 92.673  37.225  56.222 1.00 23.93 ? 238 TYR B CE1 1 
ATOM   3585 C  CE2 . TYR B  1 48  ? 90.495  38.074  56.798 1.00 31.12 ? 238 TYR B CE2 1 
ATOM   3586 C  CZ  . TYR B  1 48  ? 91.384  37.016  56.695 1.00 30.68 ? 238 TYR B CZ  1 
ATOM   3587 O  OH  . TYR B  1 48  ? 90.987  35.760  57.088 1.00 33.06 ? 238 TYR B OH  1 
ATOM   3588 N  N   . MET B  1 49  ? 90.430  41.443  53.239 1.00 26.40 ? 239 MET B N   1 
ATOM   3589 C  CA  . MET B  1 49  ? 89.229  40.959  52.564 1.00 22.47 ? 239 MET B CA  1 
ATOM   3590 C  C   . MET B  1 49  ? 89.256  41.234  51.065 1.00 23.34 ? 239 MET B C   1 
ATOM   3591 O  O   . MET B  1 49  ? 88.286  40.967  50.358 1.00 18.97 ? 239 MET B O   1 
ATOM   3592 C  CB  . MET B  1 49  ? 88.004  41.637  53.172 1.00 21.23 ? 239 MET B CB  1 
ATOM   3593 C  CG  . MET B  1 49  ? 87.803  41.343  54.642 1.00 21.46 ? 239 MET B CG  1 
ATOM   3594 S  SD  . MET B  1 49  ? 87.032  39.746  54.892 1.00 16.84 ? 239 MET B SD  1 
ATOM   3595 C  CE  . MET B  1 49  ? 85.306  40.222  54.893 1.00 13.48 ? 239 MET B CE  1 
ATOM   3596 N  N   . TYR B  1 50  ? 90.370  41.767  50.580 1.00 26.09 ? 240 TYR B N   1 
ATOM   3597 C  CA  . TYR B  1 50  ? 90.494  42.092  49.168 1.00 26.35 ? 240 TYR B CA  1 
ATOM   3598 C  C   . TYR B  1 50  ? 89.415  43.064  48.718 1.00 25.89 ? 240 TYR B C   1 
ATOM   3599 O  O   . TYR B  1 50  ? 88.915  42.987  47.592 1.00 25.89 ? 240 TYR B O   1 
ATOM   3600 C  CB  . TYR B  1 50  ? 90.458  40.826  48.308 1.00 29.47 ? 240 TYR B CB  1 
ATOM   3601 C  CG  . TYR B  1 50  ? 91.827  40.222  48.130 1.00 33.63 ? 240 TYR B CG  1 
ATOM   3602 C  CD1 . TYR B  1 50  ? 92.391  39.414  49.117 1.00 33.01 ? 240 TYR B CD1 1 
ATOM   3603 C  CD2 . TYR B  1 50  ? 92.593  40.520  47.004 1.00 36.70 ? 240 TYR B CD2 1 
ATOM   3604 C  CE1 . TYR B  1 50  ? 93.687  38.921  48.987 1.00 37.84 ? 240 TYR B CE1 1 
ATOM   3605 C  CE2 . TYR B  1 50  ? 93.889  40.034  46.865 1.00 38.84 ? 240 TYR B CE2 1 
ATOM   3606 C  CZ  . TYR B  1 50  ? 94.431  39.237  47.858 1.00 38.68 ? 240 TYR B CZ  1 
ATOM   3607 O  OH  . TYR B  1 50  ? 95.717  38.764  47.720 1.00 42.22 ? 240 TYR B OH  1 
ATOM   3608 N  N   . ILE B  1 51  ? 89.063  43.979  49.615 1.00 21.93 ? 241 ILE B N   1 
ATOM   3609 C  CA  . ILE B  1 51  ? 88.072  45.007  49.328 1.00 19.53 ? 241 ILE B CA  1 
ATOM   3610 C  C   . ILE B  1 51  ? 88.674  46.348  49.715 1.00 19.52 ? 241 ILE B C   1 
ATOM   3611 O  O   . ILE B  1 51  ? 89.442  46.439  50.670 1.00 23.25 ? 241 ILE B O   1 
ATOM   3612 C  CB  . ILE B  1 51  ? 86.772  44.819  50.142 1.00 17.11 ? 241 ILE B CB  1 
ATOM   3613 C  CG1 . ILE B  1 51  ? 86.013  43.582  49.664 1.00 23.18 ? 241 ILE B CG1 1 
ATOM   3614 C  CG2 . ILE B  1 51  ? 85.879  46.041  49.982 1.00 19.10 ? 241 ILE B CG2 1 
ATOM   3615 C  CD1 . ILE B  1 51  ? 84.720  43.332  50.430 1.00 14.53 ? 241 ILE B CD1 1 
ATOM   3616 N  N   . HIS B  1 52  ? 88.339  47.383  48.959 1.00 16.49 ? 242 HIS B N   1 
ATOM   3617 C  CA  . HIS B  1 52  ? 88.825  48.720  49.252 1.00 17.84 ? 242 HIS B CA  1 
ATOM   3618 C  C   . HIS B  1 52  ? 87.621  49.611  49.509 1.00 17.78 ? 242 HIS B C   1 
ATOM   3619 O  O   . HIS B  1 52  ? 86.636  49.568  48.769 1.00 18.27 ? 242 HIS B O   1 
ATOM   3620 C  CB  . HIS B  1 52  ? 89.638  49.269  48.077 1.00 16.41 ? 242 HIS B CB  1 
ATOM   3621 C  CG  . HIS B  1 52  ? 91.045  48.761  48.025 1.00 19.05 ? 242 HIS B CG  1 
ATOM   3622 N  ND1 . HIS B  1 52  ? 91.799  48.774  46.871 1.00 22.31 ? 242 HIS B ND1 1 
ATOM   3623 C  CD2 . HIS B  1 52  ? 91.842  48.245  48.989 1.00 21.75 ? 242 HIS B CD2 1 
ATOM   3624 C  CE1 . HIS B  1 52  ? 93.000  48.286  47.126 1.00 21.23 ? 242 HIS B CE1 1 
ATOM   3625 N  NE2 . HIS B  1 52  ? 93.052  47.958  48.405 1.00 23.88 ? 242 HIS B NE2 1 
ATOM   3626 N  N   . VAL B  1 53  ? 87.688  50.402  50.571 1.00 16.80 ? 243 VAL B N   1 
ATOM   3627 C  CA  . VAL B  1 53  ? 86.596  51.306  50.887 1.00 20.14 ? 243 VAL B CA  1 
ATOM   3628 C  C   . VAL B  1 53  ? 87.058  52.737  50.647 1.00 16.74 ? 243 VAL B C   1 
ATOM   3629 O  O   . VAL B  1 53  ? 88.018  53.203  51.260 1.00 18.97 ? 243 VAL B O   1 
ATOM   3630 C  CB  . VAL B  1 53  ? 86.130  51.143  52.350 1.00 19.55 ? 243 VAL B CB  1 
ATOM   3631 C  CG1 . VAL B  1 53  ? 84.993  52.109  52.644 1.00 16.13 ? 243 VAL B CG1 1 
ATOM   3632 C  CG2 . VAL B  1 53  ? 85.670  49.711  52.587 1.00 17.54 ? 243 VAL B CG2 1 
ATOM   3633 N  N   . ALA B  1 54  ? 86.376  53.420  49.734 1.00 12.46 ? 244 ALA B N   1 
ATOM   3634 C  CA  . ALA B  1 54  ? 86.706  54.794  49.392 1.00 7.59  ? 244 ALA B CA  1 
ATOM   3635 C  C   . ALA B  1 54  ? 85.526  55.710  49.677 1.00 12.17 ? 244 ALA B C   1 
ATOM   3636 O  O   . ALA B  1 54  ? 84.372  55.354  49.417 1.00 11.13 ? 244 ALA B O   1 
ATOM   3637 C  CB  . ALA B  1 54  ? 87.086  54.878  47.926 1.00 10.85 ? 244 ALA B CB  1 
ATOM   3638 N  N   . LEU B  1 55  ? 85.819  56.892  50.210 1.00 16.69 ? 245 LEU B N   1 
ATOM   3639 C  CA  . LEU B  1 55  ? 84.781  57.864  50.533 1.00 18.58 ? 245 LEU B CA  1 
ATOM   3640 C  C   . LEU B  1 55  ? 84.541  58.776  49.333 1.00 23.15 ? 245 LEU B C   1 
ATOM   3641 O  O   . LEU B  1 55  ? 85.452  59.481  48.888 1.00 24.86 ? 245 LEU B O   1 
ATOM   3642 C  CB  . LEU B  1 55  ? 85.206  58.698  51.741 1.00 20.89 ? 245 LEU B CB  1 
ATOM   3643 C  CG  . LEU B  1 55  ? 84.096  59.464  52.463 1.00 26.18 ? 245 LEU B CG  1 
ATOM   3644 C  CD1 . LEU B  1 55  ? 83.181  58.479  53.176 1.00 25.74 ? 245 LEU B CD1 1 
ATOM   3645 C  CD2 . LEU B  1 55  ? 84.708  60.428  53.465 1.00 31.15 ? 245 LEU B CD2 1 
ATOM   3646 N  N   . VAL B  1 56  ? 83.317  58.757  48.810 1.00 22.42 ? 246 VAL B N   1 
ATOM   3647 C  CA  . VAL B  1 56  ? 82.967  59.583  47.658 1.00 23.89 ? 246 VAL B CA  1 
ATOM   3648 C  C   . VAL B  1 56  ? 81.860  60.586  47.977 1.00 26.00 ? 246 VAL B C   1 
ATOM   3649 O  O   . VAL B  1 56  ? 81.384  61.294  47.090 1.00 29.67 ? 246 VAL B O   1 
ATOM   3650 C  CB  . VAL B  1 56  ? 82.498  58.720  46.465 1.00 23.95 ? 246 VAL B CB  1 
ATOM   3651 C  CG1 . VAL B  1 56  ? 83.535  57.657  46.151 1.00 25.61 ? 246 VAL B CG1 1 
ATOM   3652 C  CG2 . VAL B  1 56  ? 81.146  58.090  46.773 1.00 18.72 ? 246 VAL B CG2 1 
ATOM   3653 N  N   . GLY B  1 57  ? 81.448  60.639  49.240 1.00 23.23 ? 247 GLY B N   1 
ATOM   3654 C  CA  . GLY B  1 57  ? 80.398  61.560  49.630 1.00 18.57 ? 247 GLY B CA  1 
ATOM   3655 C  C   . GLY B  1 57  ? 80.271  61.685  51.135 1.00 21.51 ? 247 GLY B C   1 
ATOM   3656 O  O   . GLY B  1 57  ? 80.277  60.682  51.847 1.00 20.78 ? 247 GLY B O   1 
ATOM   3657 N  N   . LEU B  1 58  ? 80.152  62.919  51.616 1.00 17.22 ? 248 LEU B N   1 
ATOM   3658 C  CA  . LEU B  1 58  ? 80.031  63.186  53.042 1.00 14.39 ? 248 LEU B CA  1 
ATOM   3659 C  C   . LEU B  1 58  ? 79.056  64.331  53.297 1.00 18.57 ? 248 LEU B C   1 
ATOM   3660 O  O   . LEU B  1 58  ? 79.391  65.502  53.125 1.00 26.19 ? 248 LEU B O   1 
ATOM   3661 C  CB  . LEU B  1 58  ? 81.405  63.528  53.623 1.00 13.24 ? 248 LEU B CB  1 
ATOM   3662 C  CG  . LEU B  1 58  ? 81.475  64.058  55.059 1.00 14.50 ? 248 LEU B CG  1 
ATOM   3663 C  CD1 . LEU B  1 58  ? 80.792  63.101  56.015 1.00 12.46 ? 248 LEU B CD1 1 
ATOM   3664 C  CD2 . LEU B  1 58  ? 82.932  64.251  55.446 1.00 15.20 ? 248 LEU B CD2 1 
ATOM   3665 N  N   . GLU B  1 59  ? 77.846  63.981  53.710 1.00 22.35 ? 249 GLU B N   1 
ATOM   3666 C  CA  . GLU B  1 59  ? 76.802  64.960  53.988 1.00 21.66 ? 249 GLU B CA  1 
ATOM   3667 C  C   . GLU B  1 59  ? 76.667  65.164  55.498 1.00 19.91 ? 249 GLU B C   1 
ATOM   3668 O  O   . GLU B  1 59  ? 76.719  64.205  56.268 1.00 21.14 ? 249 GLU B O   1 
ATOM   3669 C  CB  . GLU B  1 59  ? 75.487  64.472  53.376 1.00 20.66 ? 249 GLU B CB  1 
ATOM   3670 C  CG  . GLU B  1 59  ? 74.262  65.294  53.721 1.00 31.23 ? 249 GLU B CG  1 
ATOM   3671 C  CD  . GLU B  1 59  ? 73.074  64.953  52.831 1.00 35.78 ? 249 GLU B CD  1 
ATOM   3672 O  OE1 . GLU B  1 59  ? 71.927  65.243  53.228 1.00 31.98 ? 249 GLU B OE1 1 
ATOM   3673 O  OE2 . GLU B  1 59  ? 73.292  64.405  51.726 1.00 39.52 ? 249 GLU B OE2 1 
ATOM   3674 N  N   . ILE B  1 60  ? 76.495  66.412  55.920 1.00 15.67 ? 250 ILE B N   1 
ATOM   3675 C  CA  . ILE B  1 60  ? 76.390  66.711  57.342 1.00 15.05 ? 250 ILE B CA  1 
ATOM   3676 C  C   . ILE B  1 60  ? 75.186  67.583  57.663 1.00 14.80 ? 250 ILE B C   1 
ATOM   3677 O  O   . ILE B  1 60  ? 75.154  68.764  57.333 1.00 18.20 ? 250 ILE B O   1 
ATOM   3678 C  CB  . ILE B  1 60  ? 77.674  67.409  57.834 1.00 18.69 ? 250 ILE B CB  1 
ATOM   3679 C  CG1 . ILE B  1 60  ? 78.888  66.551  57.463 1.00 14.09 ? 250 ILE B CG1 1 
ATOM   3680 C  CG2 . ILE B  1 60  ? 77.612  67.632  59.345 1.00 20.85 ? 250 ILE B CG2 1 
ATOM   3681 C  CD1 . ILE B  1 60  ? 80.210  67.215  57.715 1.00 11.74 ? 250 ILE B CD1 1 
ATOM   3682 N  N   . TRP B  1 61  ? 74.200  66.992  58.325 1.00 15.75 ? 251 TRP B N   1 
ATOM   3683 C  CA  . TRP B  1 61  ? 72.982  67.704  58.685 1.00 15.42 ? 251 TRP B CA  1 
ATOM   3684 C  C   . TRP B  1 61  ? 73.191  68.719  59.805 1.00 13.07 ? 251 TRP B C   1 
ATOM   3685 O  O   . TRP B  1 61  ? 72.681  68.555  60.912 1.00 7.92  ? 251 TRP B O   1 
ATOM   3686 C  CB  . TRP B  1 61  ? 71.900  66.696  59.079 1.00 16.41 ? 251 TRP B CB  1 
ATOM   3687 C  CG  . TRP B  1 61  ? 71.581  65.722  57.983 1.00 15.78 ? 251 TRP B CG  1 
ATOM   3688 C  CD1 . TRP B  1 61  ? 71.834  65.880  56.651 1.00 18.11 ? 251 TRP B CD1 1 
ATOM   3689 C  CD2 . TRP B  1 61  ? 70.910  64.464  58.117 1.00 18.97 ? 251 TRP B CD2 1 
ATOM   3690 N  NE1 . TRP B  1 61  ? 71.364  64.801  55.946 1.00 21.03 ? 251 TRP B NE1 1 
ATOM   3691 C  CE2 . TRP B  1 61  ? 70.793  63.915  56.820 1.00 22.45 ? 251 TRP B CE2 1 
ATOM   3692 C  CE3 . TRP B  1 61  ? 70.397  63.746  59.204 1.00 17.14 ? 251 TRP B CE3 1 
ATOM   3693 C  CZ2 . TRP B  1 61  ? 70.178  62.679  56.580 1.00 19.98 ? 251 TRP B CZ2 1 
ATOM   3694 C  CZ3 . TRP B  1 61  ? 69.784  62.515  58.964 1.00 18.86 ? 251 TRP B CZ3 1 
ATOM   3695 C  CH2 . TRP B  1 61  ? 69.683  61.996  57.662 1.00 15.98 ? 251 TRP B CH2 1 
ATOM   3696 N  N   . SER B  1 62  ? 73.935  69.778  59.504 1.00 14.74 ? 252 SER B N   1 
ATOM   3697 C  CA  . SER B  1 62  ? 74.214  70.814  60.489 1.00 20.33 ? 252 SER B CA  1 
ATOM   3698 C  C   . SER B  1 62  ? 72.990  71.669  60.817 1.00 21.61 ? 252 SER B C   1 
ATOM   3699 O  O   . SER B  1 62  ? 72.927  72.282  61.883 1.00 22.86 ? 252 SER B O   1 
ATOM   3700 C  CB  . SER B  1 62  ? 75.365  71.703  60.010 1.00 17.44 ? 252 SER B CB  1 
ATOM   3701 O  OG  . SER B  1 62  ? 75.077  72.279  58.749 1.00 26.94 ? 252 SER B OG  1 
ATOM   3702 N  N   . ASN B  1 63  ? 72.018  71.712  59.912 1.00 21.03 ? 253 ASN B N   1 
ATOM   3703 C  CA  . ASN B  1 63  ? 70.811  72.493  60.159 1.00 24.75 ? 253 ASN B CA  1 
ATOM   3704 C  C   . ASN B  1 63  ? 69.752  71.636  60.833 1.00 25.15 ? 253 ASN B C   1 
ATOM   3705 O  O   . ASN B  1 63  ? 69.469  71.798  62.020 1.00 24.81 ? 253 ASN B O   1 
ATOM   3706 C  CB  . ASN B  1 63  ? 70.250  73.057  58.852 1.00 32.50 ? 253 ASN B CB  1 
ATOM   3707 C  CG  . ASN B  1 63  ? 71.193  74.040  58.189 1.00 44.42 ? 253 ASN B CG  1 
ATOM   3708 O  OD1 . ASN B  1 63  ? 71.635  75.010  58.811 1.00 49.36 ? 253 ASN B OD1 1 
ATOM   3709 N  ND2 . ASN B  1 63  ? 71.505  73.799  56.919 1.00 46.36 ? 253 ASN B ND2 1 
ATOM   3710 N  N   . GLU B  1 64  ? 69.171  70.720  60.067 1.00 26.65 ? 254 GLU B N   1 
ATOM   3711 C  CA  . GLU B  1 64  ? 68.138  69.836  60.584 1.00 29.12 ? 254 GLU B CA  1 
ATOM   3712 C  C   . GLU B  1 64  ? 68.329  68.441  59.997 1.00 27.12 ? 254 GLU B C   1 
ATOM   3713 O  O   . GLU B  1 64  ? 68.906  68.294  58.920 1.00 23.63 ? 254 GLU B O   1 
ATOM   3714 C  CB  . GLU B  1 64  ? 66.758  70.376  60.200 1.00 32.38 ? 254 GLU B CB  1 
ATOM   3715 C  CG  . GLU B  1 64  ? 65.712  70.271  61.304 1.00 50.07 ? 254 GLU B CG  1 
ATOM   3716 C  CD  . GLU B  1 64  ? 65.998  71.190  62.489 1.00 55.92 ? 254 GLU B CD  1 
ATOM   3717 O  OE1 . GLU B  1 64  ? 67.078  71.058  63.108 1.00 57.13 ? 254 GLU B OE1 1 
ATOM   3718 O  OE2 . GLU B  1 64  ? 65.139  72.044  62.803 1.00 56.33 ? 254 GLU B OE2 1 
ATOM   3719 N  N   . ASP B  1 65  ? 67.867  67.417  60.711 1.00 29.33 ? 255 ASP B N   1 
ATOM   3720 C  CA  . ASP B  1 65  ? 67.978  66.047  60.217 1.00 30.66 ? 255 ASP B CA  1 
ATOM   3721 C  C   . ASP B  1 65  ? 66.992  65.883  59.069 1.00 30.94 ? 255 ASP B C   1 
ATOM   3722 O  O   . ASP B  1 65  ? 65.866  66.377  59.134 1.00 29.17 ? 255 ASP B O   1 
ATOM   3723 C  CB  . ASP B  1 65  ? 67.624  65.024  61.302 1.00 34.43 ? 255 ASP B CB  1 
ATOM   3724 C  CG  . ASP B  1 65  ? 68.680  64.912  62.379 1.00 35.90 ? 255 ASP B CG  1 
ATOM   3725 O  OD1 . ASP B  1 65  ? 69.878  64.815  62.039 1.00 40.86 ? 255 ASP B OD1 1 
ATOM   3726 O  OD2 . ASP B  1 65  ? 68.307  64.901  63.570 1.00 38.03 ? 255 ASP B OD2 1 
ATOM   3727 N  N   . LYS B  1 66  ? 67.410  65.188  58.019 1.00 29.57 ? 256 LYS B N   1 
ATOM   3728 C  CA  . LYS B  1 66  ? 66.535  64.974  56.879 1.00 24.68 ? 256 LYS B CA  1 
ATOM   3729 C  C   . LYS B  1 66  ? 65.615  63.774  57.110 1.00 23.53 ? 256 LYS B C   1 
ATOM   3730 O  O   . LYS B  1 66  ? 64.759  63.466  56.281 1.00 22.65 ? 256 LYS B O   1 
ATOM   3731 C  CB  . LYS B  1 66  ? 67.369  64.805  55.612 1.00 21.24 ? 256 LYS B CB  1 
ATOM   3732 C  CG  . LYS B  1 66  ? 68.129  66.068  55.261 1.00 22.88 ? 256 LYS B CG  1 
ATOM   3733 C  CD  . LYS B  1 66  ? 68.922  65.926  53.976 1.00 30.22 ? 256 LYS B CD  1 
ATOM   3734 C  CE  . LYS B  1 66  ? 69.604  67.240  53.609 1.00 28.67 ? 256 LYS B CE  1 
ATOM   3735 N  NZ  . LYS B  1 66  ? 70.344  67.145  52.321 1.00 29.77 ? 256 LYS B NZ  1 
ATOM   3736 N  N   . ILE B  1 67  ? 65.801  63.102  58.244 1.00 21.05 ? 257 ILE B N   1 
ATOM   3737 C  CA  . ILE B  1 67  ? 64.961  61.968  58.621 1.00 20.17 ? 257 ILE B CA  1 
ATOM   3738 C  C   . ILE B  1 67  ? 64.762  62.039  60.132 1.00 22.87 ? 257 ILE B C   1 
ATOM   3739 O  O   . ILE B  1 67  ? 65.425  62.820  60.817 1.00 25.57 ? 257 ILE B O   1 
ATOM   3740 C  CB  . ILE B  1 67  ? 65.604  60.598  58.276 1.00 18.59 ? 257 ILE B CB  1 
ATOM   3741 C  CG1 . ILE B  1 67  ? 66.594  60.188  59.365 1.00 17.77 ? 257 ILE B CG1 1 
ATOM   3742 C  CG2 . ILE B  1 67  ? 66.303  60.671  56.924 1.00 21.90 ? 257 ILE B CG2 1 
ATOM   3743 C  CD1 . ILE B  1 67  ? 67.076  58.766  59.233 1.00 22.67 ? 257 ILE B CD1 1 
ATOM   3744 N  N   . THR B  1 68  ? 63.850  61.229  60.650 1.00 21.01 ? 258 THR B N   1 
ATOM   3745 C  CA  . THR B  1 68  ? 63.585  61.213  62.082 1.00 20.98 ? 258 THR B CA  1 
ATOM   3746 C  C   . THR B  1 68  ? 64.510  60.199  62.756 1.00 18.63 ? 258 THR B C   1 
ATOM   3747 O  O   . THR B  1 68  ? 64.223  59.002  62.763 1.00 19.27 ? 258 THR B O   1 
ATOM   3748 C  CB  . THR B  1 68  ? 62.105  60.834  62.368 1.00 20.17 ? 258 THR B CB  1 
ATOM   3749 O  OG1 . THR B  1 68  ? 61.236  61.789  61.745 1.00 23.94 ? 258 THR B OG1 1 
ATOM   3750 C  CG2 . THR B  1 68  ? 61.830  60.816  63.863 1.00 19.32 ? 258 THR B CG2 1 
ATOM   3751 N  N   . VAL B  1 69  ? 65.623  60.678  63.312 1.00 14.78 ? 259 VAL B N   1 
ATOM   3752 C  CA  . VAL B  1 69  ? 66.579  59.794  63.985 1.00 14.47 ? 259 VAL B CA  1 
ATOM   3753 C  C   . VAL B  1 69  ? 66.115  59.471  65.400 1.00 16.29 ? 259 VAL B C   1 
ATOM   3754 O  O   . VAL B  1 69  ? 66.099  60.343  66.267 1.00 18.84 ? 259 VAL B O   1 
ATOM   3755 C  CB  . VAL B  1 69  ? 67.981  60.428  64.076 1.00 7.43  ? 259 VAL B CB  1 
ATOM   3756 C  CG1 . VAL B  1 69  ? 68.935  59.461  64.749 1.00 10.53 ? 259 VAL B CG1 1 
ATOM   3757 C  CG2 . VAL B  1 69  ? 68.489  60.790  62.685 1.00 8.72  ? 259 VAL B CG2 1 
ATOM   3758 N  N   . LYS B  1 70  ? 65.744  58.216  65.632 1.00 13.46 ? 260 LYS B N   1 
ATOM   3759 C  CA  . LYS B  1 70  ? 65.264  57.799  66.946 1.00 12.12 ? 260 LYS B CA  1 
ATOM   3760 C  C   . LYS B  1 70  ? 66.234  56.802  67.562 1.00 9.56  ? 260 LYS B C   1 
ATOM   3761 O  O   . LYS B  1 70  ? 66.972  56.123  66.851 1.00 14.25 ? 260 LYS B O   1 
ATOM   3762 C  CB  . LYS B  1 70  ? 63.867  57.163  66.824 1.00 5.66  ? 260 LYS B CB  1 
ATOM   3763 C  CG  . LYS B  1 70  ? 62.898  57.961  65.953 1.00 7.56  ? 260 LYS B CG  1 
ATOM   3764 C  CD  . LYS B  1 70  ? 61.530  57.291  65.793 1.00 4.49  ? 260 LYS B CD  1 
ATOM   3765 C  CE  . LYS B  1 70  ? 60.650  57.542  66.994 1.00 16.28 ? 260 LYS B CE  1 
ATOM   3766 N  NZ  . LYS B  1 70  ? 60.490  59.008  67.238 1.00 21.79 ? 260 LYS B NZ  1 
ATOM   3767 N  N   . PRO B  1 71  ? 66.263  56.715  68.898 1.00 9.69  ? 261 PRO B N   1 
ATOM   3768 C  CA  . PRO B  1 71  ? 67.181  55.761  69.526 1.00 16.28 ? 261 PRO B CA  1 
ATOM   3769 C  C   . PRO B  1 71  ? 66.826  54.302  69.235 1.00 21.88 ? 261 PRO B C   1 
ATOM   3770 O  O   . PRO B  1 71  ? 67.513  53.389  69.694 1.00 23.21 ? 261 PRO B O   1 
ATOM   3771 C  CB  . PRO B  1 71  ? 67.100  56.119  71.013 1.00 11.04 ? 261 PRO B CB  1 
ATOM   3772 C  CG  . PRO B  1 71  ? 65.779  56.810  71.153 1.00 1.00  ? 261 PRO B CG  1 
ATOM   3773 C  CD  . PRO B  1 71  ? 65.682  57.623  69.900 1.00 6.95  ? 261 PRO B CD  1 
ATOM   3774 N  N   . GLU B  1 72  ? 65.754  54.092  68.471 1.00 24.44 ? 262 GLU B N   1 
ATOM   3775 C  CA  . GLU B  1 72  ? 65.320  52.746  68.092 1.00 23.62 ? 262 GLU B CA  1 
ATOM   3776 C  C   . GLU B  1 72  ? 65.990  52.433  66.749 1.00 21.62 ? 262 GLU B C   1 
ATOM   3777 O  O   . GLU B  1 72  ? 65.491  52.828  65.690 1.00 22.64 ? 262 GLU B O   1 
ATOM   3778 C  CB  . GLU B  1 72  ? 63.795  52.701  67.937 1.00 26.11 ? 262 GLU B CB  1 
ATOM   3779 C  CG  . GLU B  1 72  ? 63.207  51.294  67.909 1.00 34.35 ? 262 GLU B CG  1 
ATOM   3780 C  CD  . GLU B  1 72  ? 61.781  51.250  67.361 1.00 47.63 ? 262 GLU B CD  1 
ATOM   3781 O  OE1 . GLU B  1 72  ? 60.925  52.049  67.809 1.00 43.31 ? 262 GLU B OE1 1 
ATOM   3782 O  OE2 . GLU B  1 72  ? 61.515  50.403  66.478 1.00 53.11 ? 262 GLU B OE2 1 
ATOM   3783 N  N   . ALA B  1 73  ? 67.122  51.733  66.801 1.00 15.70 ? 263 ALA B N   1 
ATOM   3784 C  CA  . ALA B  1 73  ? 67.893  51.388  65.603 1.00 11.22 ? 263 ALA B CA  1 
ATOM   3785 C  C   . ALA B  1 73  ? 67.050  50.970  64.402 1.00 11.76 ? 263 ALA B C   1 
ATOM   3786 O  O   . ALA B  1 73  ? 67.152  51.562  63.324 1.00 10.11 ? 263 ALA B O   1 
ATOM   3787 C  CB  . ALA B  1 73  ? 68.906  50.292  65.932 1.00 6.06  ? 263 ALA B CB  1 
ATOM   3788 N  N   . GLY B  1 74  ? 66.224  49.946  64.593 1.00 17.96 ? 264 GLY B N   1 
ATOM   3789 C  CA  . GLY B  1 74  ? 65.375  49.457  63.521 1.00 13.03 ? 264 GLY B CA  1 
ATOM   3790 C  C   . GLY B  1 74  ? 64.565  50.549  62.853 1.00 11.35 ? 264 GLY B C   1 
ATOM   3791 O  O   . GLY B  1 74  ? 64.452  50.584  61.631 1.00 11.19 ? 264 GLY B O   1 
ATOM   3792 N  N   . TYR B  1 75  ? 63.990  51.443  63.646 1.00 12.37 ? 265 TYR B N   1 
ATOM   3793 C  CA  . TYR B  1 75  ? 63.203  52.524  63.077 1.00 16.62 ? 265 TYR B CA  1 
ATOM   3794 C  C   . TYR B  1 75  ? 64.100  53.407  62.211 1.00 19.81 ? 265 TYR B C   1 
ATOM   3795 O  O   . TYR B  1 75  ? 63.829  53.627  61.027 1.00 17.12 ? 265 TYR B O   1 
ATOM   3796 C  CB  . TYR B  1 75  ? 62.569  53.379  64.178 1.00 15.26 ? 265 TYR B CB  1 
ATOM   3797 C  CG  . TYR B  1 75  ? 61.727  54.508  63.627 1.00 15.35 ? 265 TYR B CG  1 
ATOM   3798 C  CD1 . TYR B  1 75  ? 60.336  54.417  63.604 1.00 18.57 ? 265 TYR B CD1 1 
ATOM   3799 C  CD2 . TYR B  1 75  ? 62.325  55.631  63.053 1.00 12.17 ? 265 TYR B CD2 1 
ATOM   3800 C  CE1 . TYR B  1 75  ? 59.559  55.412  63.016 1.00 18.42 ? 265 TYR B CE1 1 
ATOM   3801 C  CE2 . TYR B  1 75  ? 61.560  56.627  62.463 1.00 19.08 ? 265 TYR B CE2 1 
ATOM   3802 C  CZ  . TYR B  1 75  ? 60.178  56.512  62.444 1.00 21.06 ? 265 TYR B CZ  1 
ATOM   3803 O  OH  . TYR B  1 75  ? 59.419  57.483  61.828 1.00 27.32 ? 265 TYR B OH  1 
ATOM   3804 N  N   . THR B  1 76  ? 65.168  53.912  62.819 1.00 20.49 ? 266 THR B N   1 
ATOM   3805 C  CA  . THR B  1 76  ? 66.106  54.785  62.130 1.00 16.63 ? 266 THR B CA  1 
ATOM   3806 C  C   . THR B  1 76  ? 66.713  54.147  60.886 1.00 16.80 ? 266 THR B C   1 
ATOM   3807 O  O   . THR B  1 76  ? 66.809  54.794  59.843 1.00 21.67 ? 266 THR B O   1 
ATOM   3808 C  CB  . THR B  1 76  ? 67.241  55.223  63.074 1.00 14.40 ? 266 THR B CB  1 
ATOM   3809 O  OG1 . THR B  1 76  ? 66.685  55.946  64.181 1.00 7.09  ? 266 THR B OG1 1 
ATOM   3810 C  CG2 . THR B  1 76  ? 68.237  56.112  62.338 1.00 10.41 ? 266 THR B CG2 1 
ATOM   3811 N  N   . LEU B  1 77  ? 67.124  52.886  60.988 1.00 12.72 ? 267 LEU B N   1 
ATOM   3812 C  CA  . LEU B  1 77  ? 67.716  52.203  59.842 1.00 12.67 ? 267 LEU B CA  1 
ATOM   3813 C  C   . LEU B  1 77  ? 66.771  52.211  58.645 1.00 15.25 ? 267 LEU B C   1 
ATOM   3814 O  O   . LEU B  1 77  ? 67.168  52.545  57.528 1.00 15.42 ? 267 LEU B O   1 
ATOM   3815 C  CB  . LEU B  1 77  ? 68.069  50.760  60.199 1.00 14.49 ? 267 LEU B CB  1 
ATOM   3816 C  CG  . LEU B  1 77  ? 68.536  49.907  59.013 1.00 16.89 ? 267 LEU B CG  1 
ATOM   3817 C  CD1 . LEU B  1 77  ? 69.737  50.558  58.352 1.00 9.76  ? 267 LEU B CD1 1 
ATOM   3818 C  CD2 . LEU B  1 77  ? 68.873  48.503  59.490 1.00 17.82 ? 267 LEU B CD2 1 
ATOM   3819 N  N   . ASN B  1 78  ? 65.518  51.841  58.884 1.00 17.63 ? 268 ASN B N   1 
ATOM   3820 C  CA  . ASN B  1 78  ? 64.520  51.818  57.826 1.00 14.69 ? 268 ASN B CA  1 
ATOM   3821 C  C   . ASN B  1 78  ? 64.243  53.215  57.279 1.00 12.66 ? 268 ASN B C   1 
ATOM   3822 O  O   . ASN B  1 78  ? 64.155  53.396  56.068 1.00 14.94 ? 268 ASN B O   1 
ATOM   3823 C  CB  . ASN B  1 78  ? 63.224  51.186  58.335 1.00 14.72 ? 268 ASN B CB  1 
ATOM   3824 C  CG  . ASN B  1 78  ? 62.059  51.432  57.405 1.00 21.40 ? 268 ASN B CG  1 
ATOM   3825 O  OD1 . ASN B  1 78  ? 61.333  52.419  57.549 1.00 18.99 ? 268 ASN B OD1 1 
ATOM   3826 N  ND2 . ASN B  1 78  ? 61.883  50.545  56.427 1.00 19.50 ? 268 ASN B ND2 1 
ATOM   3827 N  N   . ALA B  1 79  ? 64.102  54.197  58.167 1.00 14.13 ? 269 ALA B N   1 
ATOM   3828 C  CA  . ALA B  1 79  ? 63.846  55.576  57.747 1.00 14.77 ? 269 ALA B CA  1 
ATOM   3829 C  C   . ALA B  1 79  ? 65.024  56.065  56.918 1.00 19.49 ? 269 ALA B C   1 
ATOM   3830 O  O   . ALA B  1 79  ? 64.846  56.637  55.843 1.00 24.19 ? 269 ALA B O   1 
ATOM   3831 C  CB  . ALA B  1 79  ? 63.653  56.481  58.963 1.00 8.37  ? 269 ALA B CB  1 
ATOM   3832 N  N   . PHE B  1 80  ? 66.230  55.832  57.426 1.00 20.92 ? 270 PHE B N   1 
ATOM   3833 C  CA  . PHE B  1 80  ? 67.445  56.234  56.732 1.00 19.71 ? 270 PHE B CA  1 
ATOM   3834 C  C   . PHE B  1 80  ? 67.515  55.546  55.374 1.00 21.57 ? 270 PHE B C   1 
ATOM   3835 O  O   . PHE B  1 80  ? 68.024  56.111  54.407 1.00 23.34 ? 270 PHE B O   1 
ATOM   3836 C  CB  . PHE B  1 80  ? 68.680  55.855  57.552 1.00 16.37 ? 270 PHE B CB  1 
ATOM   3837 C  CG  . PHE B  1 80  ? 69.976  56.197  56.879 1.00 9.29  ? 270 PHE B CG  1 
ATOM   3838 C  CD1 . PHE B  1 80  ? 70.322  57.522  56.641 1.00 8.39  ? 270 PHE B CD1 1 
ATOM   3839 C  CD2 . PHE B  1 80  ? 70.843  55.194  56.462 1.00 12.44 ? 270 PHE B CD2 1 
ATOM   3840 C  CE1 . PHE B  1 80  ? 71.512  57.843  55.996 1.00 5.91  ? 270 PHE B CE1 1 
ATOM   3841 C  CE2 . PHE B  1 80  ? 72.041  55.506  55.814 1.00 4.96  ? 270 PHE B CE2 1 
ATOM   3842 C  CZ  . PHE B  1 80  ? 72.373  56.830  55.582 1.00 1.23  ? 270 PHE B CZ  1 
ATOM   3843 N  N   . GLY B  1 81  ? 67.011  54.317  55.317 1.00 17.98 ? 271 GLY B N   1 
ATOM   3844 C  CA  . GLY B  1 81  ? 67.021  53.572  54.074 1.00 16.64 ? 271 GLY B CA  1 
ATOM   3845 C  C   . GLY B  1 81  ? 66.114  54.205  53.040 1.00 19.00 ? 271 GLY B C   1 
ATOM   3846 O  O   . GLY B  1 81  ? 66.511  54.386  51.889 1.00 17.23 ? 271 GLY B O   1 
ATOM   3847 N  N   . GLU B  1 82  ? 64.892  54.537  53.450 1.00 20.24 ? 272 GLU B N   1 
ATOM   3848 C  CA  . GLU B  1 82  ? 63.920  55.160  52.559 1.00 23.42 ? 272 GLU B CA  1 
ATOM   3849 C  C   . GLU B  1 82  ? 64.511  56.441  51.996 1.00 23.90 ? 272 GLU B C   1 
ATOM   3850 O  O   . GLU B  1 82  ? 64.501  56.669  50.784 1.00 23.43 ? 272 GLU B O   1 
ATOM   3851 C  CB  . GLU B  1 82  ? 62.634  55.501  53.319 1.00 28.18 ? 272 GLU B CB  1 
ATOM   3852 C  CG  . GLU B  1 82  ? 61.767  54.311  53.712 1.00 37.75 ? 272 GLU B CG  1 
ATOM   3853 C  CD  . GLU B  1 82  ? 61.054  53.680  52.526 1.00 41.88 ? 272 GLU B CD  1 
ATOM   3854 O  OE1 . GLU B  1 82  ? 61.675  52.867  51.810 1.00 41.12 ? 272 GLU B OE1 1 
ATOM   3855 O  OE2 . GLU B  1 82  ? 59.869  54.008  52.306 1.00 45.43 ? 272 GLU B OE2 1 
ATOM   3856 N  N   . TRP B  1 83  ? 65.028  57.275  52.891 1.00 22.40 ? 273 TRP B N   1 
ATOM   3857 C  CA  . TRP B  1 83  ? 65.625  58.543  52.500 1.00 21.45 ? 273 TRP B CA  1 
ATOM   3858 C  C   . TRP B  1 83  ? 66.772  58.365  51.510 1.00 22.42 ? 273 TRP B C   1 
ATOM   3859 O  O   . TRP B  1 83  ? 66.978  59.204  50.634 1.00 25.28 ? 273 TRP B O   1 
ATOM   3860 C  CB  . TRP B  1 83  ? 66.140  59.290  53.731 1.00 19.55 ? 273 TRP B CB  1 
ATOM   3861 C  CG  . TRP B  1 83  ? 66.876  60.537  53.377 1.00 20.36 ? 273 TRP B CG  1 
ATOM   3862 C  CD1 . TRP B  1 83  ? 66.335  61.720  52.967 1.00 18.39 ? 273 TRP B CD1 1 
ATOM   3863 C  CD2 . TRP B  1 83  ? 68.297  60.701  53.312 1.00 21.52 ? 273 TRP B CD2 1 
ATOM   3864 N  NE1 . TRP B  1 83  ? 67.331  62.610  52.644 1.00 18.95 ? 273 TRP B NE1 1 
ATOM   3865 C  CE2 . TRP B  1 83  ? 68.546  62.010  52.847 1.00 18.46 ? 273 TRP B CE2 1 
ATOM   3866 C  CE3 . TRP B  1 83  ? 69.386  59.865  53.596 1.00 18.97 ? 273 TRP B CE3 1 
ATOM   3867 C  CZ2 . TRP B  1 83  ? 69.837  62.504  52.662 1.00 12.70 ? 273 TRP B CZ2 1 
ATOM   3868 C  CZ3 . TRP B  1 83  ? 70.670  60.356  53.410 1.00 16.12 ? 273 TRP B CZ3 1 
ATOM   3869 C  CH2 . TRP B  1 83  ? 70.883  61.665  52.946 1.00 18.68 ? 273 TRP B CH2 1 
ATOM   3870 N  N   . ARG B  1 84  ? 67.515  57.272  51.648 1.00 23.22 ? 274 ARG B N   1 
ATOM   3871 C  CA  . ARG B  1 84  ? 68.650  57.017  50.770 1.00 24.87 ? 274 ARG B CA  1 
ATOM   3872 C  C   . ARG B  1 84  ? 68.244  56.769  49.323 1.00 28.72 ? 274 ARG B C   1 
ATOM   3873 O  O   . ARG B  1 84  ? 68.926  57.208  48.396 1.00 30.71 ? 274 ARG B O   1 
ATOM   3874 C  CB  . ARG B  1 84  ? 69.459  55.819  51.271 1.00 20.94 ? 274 ARG B CB  1 
ATOM   3875 C  CG  . ARG B  1 84  ? 70.843  55.744  50.657 1.00 24.30 ? 274 ARG B CG  1 
ATOM   3876 C  CD  . ARG B  1 84  ? 71.099  54.417  49.977 1.00 26.83 ? 274 ARG B CD  1 
ATOM   3877 N  NE  . ARG B  1 84  ? 72.357  54.433  49.236 1.00 25.02 ? 274 ARG B NE  1 
ATOM   3878 C  CZ  . ARG B  1 84  ? 72.757  53.458  48.428 1.00 27.17 ? 274 ARG B CZ  1 
ATOM   3879 N  NH1 . ARG B  1 84  ? 71.997  52.385  48.261 1.00 31.60 ? 274 ARG B NH1 1 
ATOM   3880 N  NH2 . ARG B  1 84  ? 73.904  53.561  47.771 1.00 30.24 ? 274 ARG B NH2 1 
ATOM   3881 N  N   . LYS B  1 85  ? 67.134  56.068  49.124 1.00 28.02 ? 275 LYS B N   1 
ATOM   3882 C  CA  . LYS B  1 85  ? 66.689  55.767  47.773 1.00 31.21 ? 275 LYS B CA  1 
ATOM   3883 C  C   . LYS B  1 85  ? 65.867  56.887  47.149 1.00 32.15 ? 275 LYS B C   1 
ATOM   3884 O  O   . LYS B  1 85  ? 66.029  57.197  45.970 1.00 34.03 ? 275 LYS B O   1 
ATOM   3885 C  CB  . LYS B  1 85  ? 65.889  54.462  47.761 1.00 31.01 ? 275 LYS B CB  1 
ATOM   3886 C  CG  . LYS B  1 85  ? 64.462  54.579  48.263 1.00 32.64 ? 275 LYS B CG  1 
ATOM   3887 C  CD  . LYS B  1 85  ? 63.797  53.210  48.348 1.00 37.39 ? 275 LYS B CD  1 
ATOM   3888 C  CE  . LYS B  1 85  ? 64.064  52.376  47.096 1.00 41.15 ? 275 LYS B CE  1 
ATOM   3889 N  NZ  . LYS B  1 85  ? 63.730  53.104  45.839 1.00 43.01 ? 275 LYS B NZ  1 
ATOM   3890 N  N   . THR B  1 86  ? 64.996  57.502  47.941 1.00 32.28 ? 276 THR B N   1 
ATOM   3891 C  CA  . THR B  1 86  ? 64.148  58.576  47.439 1.00 30.39 ? 276 THR B CA  1 
ATOM   3892 C  C   . THR B  1 86  ? 64.744  59.968  47.636 1.00 30.22 ? 276 THR B C   1 
ATOM   3893 O  O   . THR B  1 86  ? 64.007  60.951  47.704 1.00 35.66 ? 276 THR B O   1 
ATOM   3894 C  CB  . THR B  1 86  ? 62.758  58.546  48.112 1.00 28.94 ? 276 THR B CB  1 
ATOM   3895 O  OG1 . THR B  1 86  ? 62.868  59.000  49.466 1.00 29.95 ? 276 THR B OG1 1 
ATOM   3896 C  CG2 . THR B  1 86  ? 62.196  57.128  48.111 1.00 31.05 ? 276 THR B CG2 1 
ATOM   3897 N  N   . ASP B  1 87  ? 66.068  60.061  47.729 1.00 28.20 ? 277 ASP B N   1 
ATOM   3898 C  CA  . ASP B  1 87  ? 66.708  61.359  47.914 1.00 26.41 ? 277 ASP B CA  1 
ATOM   3899 C  C   . ASP B  1 87  ? 68.188  61.380  47.547 1.00 28.06 ? 277 ASP B C   1 
ATOM   3900 O  O   . ASP B  1 87  ? 68.548  61.829  46.462 1.00 34.44 ? 277 ASP B O   1 
ATOM   3901 C  CB  . ASP B  1 87  ? 66.539  61.838  49.358 1.00 26.81 ? 277 ASP B CB  1 
ATOM   3902 C  CG  . ASP B  1 87  ? 66.917  63.303  49.537 1.00 28.01 ? 277 ASP B CG  1 
ATOM   3903 O  OD1 . ASP B  1 87  ? 68.069  63.676  49.229 1.00 21.87 ? 277 ASP B OD1 1 
ATOM   3904 O  OD2 . ASP B  1 87  ? 66.055  64.086  49.990 1.00 34.49 ? 277 ASP B OD2 1 
ATOM   3905 N  N   . LEU B  1 88  ? 69.044  60.902  48.449 1.00 25.21 ? 278 LEU B N   1 
ATOM   3906 C  CA  . LEU B  1 88  ? 70.486  60.897  48.209 1.00 26.21 ? 278 LEU B CA  1 
ATOM   3907 C  C   . LEU B  1 88  ? 70.865  60.223  46.893 1.00 27.09 ? 278 LEU B C   1 
ATOM   3908 O  O   . LEU B  1 88  ? 71.415  60.859  45.991 1.00 25.76 ? 278 LEU B O   1 
ATOM   3909 C  CB  . LEU B  1 88  ? 71.217  60.195  49.358 1.00 26.65 ? 278 LEU B CB  1 
ATOM   3910 C  CG  . LEU B  1 88  ? 72.748  60.278  49.299 1.00 21.89 ? 278 LEU B CG  1 
ATOM   3911 C  CD1 . LEU B  1 88  ? 73.175  61.725  49.505 1.00 19.60 ? 278 LEU B CD1 1 
ATOM   3912 C  CD2 . LEU B  1 88  ? 73.371  59.392  50.362 1.00 18.05 ? 278 LEU B CD2 1 
ATOM   3913 N  N   . LEU B  1 89  ? 70.568  58.931  46.800 1.00 29.12 ? 279 LEU B N   1 
ATOM   3914 C  CA  . LEU B  1 89  ? 70.861  58.129  45.615 1.00 28.11 ? 279 LEU B CA  1 
ATOM   3915 C  C   . LEU B  1 89  ? 70.374  58.825  44.345 1.00 29.53 ? 279 LEU B C   1 
ATOM   3916 O  O   . LEU B  1 89  ? 70.880  58.572  43.248 1.00 28.89 ? 279 LEU B O   1 
ATOM   3917 C  CB  . LEU B  1 89  ? 70.190  56.762  45.753 1.00 25.96 ? 279 LEU B CB  1 
ATOM   3918 C  CG  . LEU B  1 89  ? 70.680  55.618  44.868 1.00 23.38 ? 279 LEU B CG  1 
ATOM   3919 C  CD1 . LEU B  1 89  ? 72.181  55.426  45.048 1.00 17.60 ? 279 LEU B CD1 1 
ATOM   3920 C  CD2 . LEU B  1 89  ? 69.927  54.345  45.243 1.00 22.52 ? 279 LEU B CD2 1 
ATOM   3921 N  N   . THR B  1 90  ? 69.388  59.701  44.508 1.00 31.24 ? 280 THR B N   1 
ATOM   3922 C  CA  . THR B  1 90  ? 68.813  60.462  43.402 1.00 32.26 ? 280 THR B CA  1 
ATOM   3923 C  C   . THR B  1 90  ? 69.780  61.523  42.881 1.00 32.10 ? 280 THR B C   1 
ATOM   3924 O  O   . THR B  1 90  ? 69.915  61.718  41.673 1.00 32.25 ? 280 THR B O   1 
ATOM   3925 C  CB  . THR B  1 90  ? 67.509  61.164  43.844 1.00 31.06 ? 280 THR B CB  1 
ATOM   3926 O  OG1 . THR B  1 90  ? 66.462  60.193  43.959 1.00 36.78 ? 280 THR B OG1 1 
ATOM   3927 C  CG2 . THR B  1 90  ? 67.106  62.245  42.850 1.00 26.02 ? 280 THR B CG2 1 
ATOM   3928 N  N   . ARG B  1 91  ? 70.452  62.204  43.798 1.00 30.54 ? 281 ARG B N   1 
ATOM   3929 C  CA  . ARG B  1 91  ? 71.383  63.251  43.420 1.00 32.98 ? 281 ARG B CA  1 
ATOM   3930 C  C   . ARG B  1 91  ? 72.846  62.849  43.543 1.00 31.02 ? 281 ARG B C   1 
ATOM   3931 O  O   . ARG B  1 91  ? 73.735  63.613  43.167 1.00 33.27 ? 281 ARG B O   1 
ATOM   3932 C  CB  . ARG B  1 91  ? 71.102  64.504  44.255 1.00 36.14 ? 281 ARG B CB  1 
ATOM   3933 C  CG  . ARG B  1 91  ? 70.902  64.235  45.733 1.00 39.39 ? 281 ARG B CG  1 
ATOM   3934 C  CD  . ARG B  1 91  ? 70.341  65.460  46.445 1.00 37.89 ? 281 ARG B CD  1 
ATOM   3935 N  NE  . ARG B  1 91  ? 70.264  65.260  47.889 1.00 38.97 ? 281 ARG B NE  1 
ATOM   3936 C  CZ  . ARG B  1 91  ? 71.316  65.003  48.663 1.00 38.75 ? 281 ARG B CZ  1 
ATOM   3937 N  NH1 . ARG B  1 91  ? 72.529  64.916  48.132 1.00 34.97 ? 281 ARG B NH1 1 
ATOM   3938 N  NH2 . ARG B  1 91  ? 71.156  64.833  49.968 1.00 38.73 ? 281 ARG B NH2 1 
ATOM   3939 N  N   . LYS B  1 92  ? 73.100  61.652  44.058 1.00 27.12 ? 282 LYS B N   1 
ATOM   3940 C  CA  . LYS B  1 92  ? 74.474  61.195  44.209 1.00 29.61 ? 282 LYS B CA  1 
ATOM   3941 C  C   . LYS B  1 92  ? 74.621  59.698  43.977 1.00 31.43 ? 282 LYS B C   1 
ATOM   3942 O  O   . LYS B  1 92  ? 73.947  58.885  44.610 1.00 32.20 ? 282 LYS B O   1 
ATOM   3943 C  CB  . LYS B  1 92  ? 75.003  61.541  45.602 1.00 28.28 ? 282 LYS B CB  1 
ATOM   3944 C  CG  . LYS B  1 92  ? 76.476  61.936  45.624 1.00 31.93 ? 282 LYS B CG  1 
ATOM   3945 C  CD  . LYS B  1 92  ? 77.357  60.945  44.875 1.00 21.48 ? 282 LYS B CD  1 
ATOM   3946 C  CE  . LYS B  1 92  ? 78.779  61.477  44.755 1.00 28.92 ? 282 LYS B CE  1 
ATOM   3947 N  NZ  . LYS B  1 92  ? 79.643  60.618  43.889 1.00 31.28 ? 282 LYS B NZ  1 
ATOM   3948 N  N   . LYS B  1 93  ? 75.519  59.342  43.069 1.00 32.48 ? 283 LYS B N   1 
ATOM   3949 C  CA  . LYS B  1 93  ? 75.767  57.948  42.751 1.00 31.03 ? 283 LYS B CA  1 
ATOM   3950 C  C   . LYS B  1 93  ? 76.821  57.393  43.707 1.00 28.71 ? 283 LYS B C   1 
ATOM   3951 O  O   . LYS B  1 93  ? 77.926  57.927  43.806 1.00 30.13 ? 283 LYS B O   1 
ATOM   3952 C  CB  . LYS B  1 93  ? 76.252  57.810  41.301 1.00 32.61 ? 283 LYS B CB  1 
ATOM   3953 C  CG  . LYS B  1 93  ? 75.380  58.521  40.261 1.00 37.79 ? 283 LYS B CG  1 
ATOM   3954 C  CD  . LYS B  1 93  ? 75.613  60.034  40.265 1.00 42.75 ? 283 LYS B CD  1 
ATOM   3955 C  CE  . LYS B  1 93  ? 74.760  60.754  39.222 1.00 44.84 ? 283 LYS B CE  1 
ATOM   3956 N  NZ  . LYS B  1 93  ? 73.296  60.699  39.521 1.00 46.81 ? 283 LYS B NZ  1 
ATOM   3957 N  N   . HIS B  1 94  ? 76.465  56.331  44.420 1.00 24.77 ? 284 HIS B N   1 
ATOM   3958 C  CA  . HIS B  1 94  ? 77.375  55.690  45.360 1.00 20.65 ? 284 HIS B CA  1 
ATOM   3959 C  C   . HIS B  1 94  ? 76.919  54.259  45.567 1.00 17.77 ? 284 HIS B C   1 
ATOM   3960 O  O   . HIS B  1 94  ? 75.806  53.900  45.191 1.00 17.84 ? 284 HIS B O   1 
ATOM   3961 C  CB  . HIS B  1 94  ? 77.390  56.434  46.697 1.00 21.99 ? 284 HIS B CB  1 
ATOM   3962 C  CG  . HIS B  1 94  ? 76.053  56.505  47.367 1.00 21.54 ? 284 HIS B CG  1 
ATOM   3963 N  ND1 . HIS B  1 94  ? 74.957  57.102  46.783 1.00 22.51 ? 284 HIS B ND1 1 
ATOM   3964 C  CD2 . HIS B  1 94  ? 75.636  56.052  48.573 1.00 23.98 ? 284 HIS B CD2 1 
ATOM   3965 C  CE1 . HIS B  1 94  ? 73.922  57.012  47.599 1.00 26.09 ? 284 HIS B CE1 1 
ATOM   3966 N  NE2 . HIS B  1 94  ? 74.307  56.380  48.692 1.00 22.61 ? 284 HIS B NE2 1 
ATOM   3967 N  N   . ASP B  1 95  ? 77.771  53.448  46.178 1.00 21.83 ? 285 ASP B N   1 
ATOM   3968 C  CA  . ASP B  1 95  ? 77.454  52.041  46.403 1.00 23.23 ? 285 ASP B CA  1 
ATOM   3969 C  C   . ASP B  1 95  ? 76.800  51.738  47.749 1.00 22.99 ? 285 ASP B C   1 
ATOM   3970 O  O   . ASP B  1 95  ? 75.810  51.011  47.815 1.00 23.87 ? 285 ASP B O   1 
ATOM   3971 C  CB  . ASP B  1 95  ? 78.731  51.208  46.268 1.00 20.77 ? 285 ASP B CB  1 
ATOM   3972 C  CG  . ASP B  1 95  ? 79.409  51.400  44.928 1.00 23.35 ? 285 ASP B CG  1 
ATOM   3973 O  OD1 . ASP B  1 95  ? 80.640  51.209  44.845 1.00 29.92 ? 285 ASP B OD1 1 
ATOM   3974 O  OD2 . ASP B  1 95  ? 78.710  51.735  43.952 1.00 27.61 ? 285 ASP B OD2 1 
ATOM   3975 N  N   . ASN B  1 96  ? 77.351  52.303  48.816 1.00 23.75 ? 286 ASN B N   1 
ATOM   3976 C  CA  . ASN B  1 96  ? 76.849  52.046  50.160 1.00 22.53 ? 286 ASN B CA  1 
ATOM   3977 C  C   . ASN B  1 96  ? 76.799  53.323  50.998 1.00 20.03 ? 286 ASN B C   1 
ATOM   3978 O  O   . ASN B  1 96  ? 77.634  54.213  50.835 1.00 16.91 ? 286 ASN B O   1 
ATOM   3979 C  CB  . ASN B  1 96  ? 77.757  50.993  50.813 1.00 24.73 ? 286 ASN B CB  1 
ATOM   3980 C  CG  . ASN B  1 96  ? 77.302  50.591  52.194 1.00 26.17 ? 286 ASN B CG  1 
ATOM   3981 O  OD1 . ASN B  1 96  ? 77.577  51.277  53.179 1.00 30.88 ? 286 ASN B OD1 1 
ATOM   3982 N  ND2 . ASN B  1 96  ? 76.598  49.471  52.276 1.00 24.92 ? 286 ASN B ND2 1 
ATOM   3983 N  N   . ALA B  1 97  ? 75.818  53.408  51.894 1.00 18.15 ? 287 ALA B N   1 
ATOM   3984 C  CA  . ALA B  1 97  ? 75.664  54.584  52.745 1.00 19.15 ? 287 ALA B CA  1 
ATOM   3985 C  C   . ALA B  1 97  ? 75.532  54.246  54.229 1.00 18.98 ? 287 ALA B C   1 
ATOM   3986 O  O   . ALA B  1 97  ? 74.736  53.387  54.618 1.00 14.78 ? 287 ALA B O   1 
ATOM   3987 C  CB  . ALA B  1 97  ? 74.460  55.394  52.290 1.00 24.99 ? 287 ALA B CB  1 
ATOM   3988 N  N   . GLN B  1 98  ? 76.312  54.946  55.049 1.00 16.47 ? 288 GLN B N   1 
ATOM   3989 C  CA  . GLN B  1 98  ? 76.317  54.746  56.493 1.00 15.61 ? 288 GLN B CA  1 
ATOM   3990 C  C   . GLN B  1 98  ? 76.015  56.051  57.229 1.00 18.29 ? 288 GLN B C   1 
ATOM   3991 O  O   . GLN B  1 98  ? 76.592  57.095  56.922 1.00 23.05 ? 288 GLN B O   1 
ATOM   3992 C  CB  . GLN B  1 98  ? 77.678  54.208  56.934 1.00 15.84 ? 288 GLN B CB  1 
ATOM   3993 C  CG  . GLN B  1 98  ? 78.045  52.875  56.304 1.00 26.08 ? 288 GLN B CG  1 
ATOM   3994 C  CD  . GLN B  1 98  ? 77.184  51.734  56.811 1.00 32.48 ? 288 GLN B CD  1 
ATOM   3995 O  OE1 . GLN B  1 98  ? 77.107  50.669  56.192 1.00 33.84 ? 288 GLN B OE1 1 
ATOM   3996 N  NE2 . GLN B  1 98  ? 76.537  51.948  57.948 1.00 31.77 ? 288 GLN B NE2 1 
ATOM   3997 N  N   . LEU B  1 99  ? 75.106  55.980  58.198 1.00 18.12 ? 289 LEU B N   1 
ATOM   3998 C  CA  . LEU B  1 99  ? 74.708  57.138  58.994 1.00 15.23 ? 289 LEU B CA  1 
ATOM   3999 C  C   . LEU B  1 99  ? 75.364  57.095  60.370 1.00 18.41 ? 289 LEU B C   1 
ATOM   4000 O  O   . LEU B  1 99  ? 75.155  56.153  61.136 1.00 13.99 ? 289 LEU B O   1 
ATOM   4001 C  CB  . LEU B  1 99  ? 73.189  57.160  59.174 1.00 14.58 ? 289 LEU B CB  1 
ATOM   4002 C  CG  . LEU B  1 99  ? 72.629  58.200  60.152 1.00 18.83 ? 289 LEU B CG  1 
ATOM   4003 C  CD1 . LEU B  1 99  ? 72.777  59.600  59.566 1.00 16.62 ? 289 LEU B CD1 1 
ATOM   4004 C  CD2 . LEU B  1 99  ? 71.167  57.897  60.435 1.00 19.30 ? 289 LEU B CD2 1 
ATOM   4005 N  N   . LEU B  1 100 ? 76.151  58.121  60.681 1.00 18.12 ? 290 LEU B N   1 
ATOM   4006 C  CA  . LEU B  1 100 ? 76.829  58.200  61.969 1.00 16.07 ? 290 LEU B CA  1 
ATOM   4007 C  C   . LEU B  1 100 ? 76.048  59.162  62.860 1.00 14.70 ? 290 LEU B C   1 
ATOM   4008 O  O   . LEU B  1 100 ? 75.981  60.358  62.582 1.00 16.17 ? 290 LEU B O   1 
ATOM   4009 C  CB  . LEU B  1 100 ? 78.267  58.700  61.776 1.00 16.34 ? 290 LEU B CB  1 
ATOM   4010 C  CG  . LEU B  1 100 ? 79.210  58.623  62.982 1.00 18.95 ? 290 LEU B CG  1 
ATOM   4011 C  CD1 . LEU B  1 100 ? 79.380  57.179  63.409 1.00 17.90 ? 290 LEU B CD1 1 
ATOM   4012 C  CD2 . LEU B  1 100 ? 80.559  59.217  62.622 1.00 18.15 ? 290 LEU B CD2 1 
ATOM   4013 N  N   . THR B  1 101 ? 75.450  58.636  63.924 1.00 13.14 ? 291 THR B N   1 
ATOM   4014 C  CA  . THR B  1 101 ? 74.667  59.457  64.842 1.00 14.40 ? 291 THR B CA  1 
ATOM   4015 C  C   . THR B  1 101 ? 75.246  59.484  66.254 1.00 13.34 ? 291 THR B C   1 
ATOM   4016 O  O   . THR B  1 101 ? 75.803  58.493  66.726 1.00 14.64 ? 291 THR B O   1 
ATOM   4017 C  CB  . THR B  1 101 ? 73.204  58.961  64.931 1.00 15.85 ? 291 THR B CB  1 
ATOM   4018 O  OG1 . THR B  1 101 ? 72.512  59.684  65.959 1.00 18.53 ? 291 THR B OG1 1 
ATOM   4019 C  CG2 . THR B  1 101 ? 73.163  57.478  65.251 1.00 10.10 ? 291 THR B CG2 1 
ATOM   4020 N  N   . ALA B  1 102 ? 75.099  60.622  66.927 1.00 10.41 ? 292 ALA B N   1 
ATOM   4021 C  CA  . ALA B  1 102 ? 75.608  60.774  68.285 1.00 10.10 ? 292 ALA B CA  1 
ATOM   4022 C  C   . ALA B  1 102 ? 74.568  60.350  69.316 1.00 14.05 ? 292 ALA B C   1 
ATOM   4023 O  O   . ALA B  1 102 ? 74.848  60.318  70.516 1.00 14.91 ? 292 ALA B O   1 
ATOM   4024 C  CB  . ALA B  1 102 ? 76.026  62.216  68.528 1.00 4.09  ? 292 ALA B CB  1 
ATOM   4025 N  N   . ILE B  1 103 ? 73.368  60.024  68.848 1.00 15.19 ? 293 ILE B N   1 
ATOM   4026 C  CA  . ILE B  1 103 ? 72.302  59.596  69.744 1.00 16.37 ? 293 ILE B CA  1 
ATOM   4027 C  C   . ILE B  1 103 ? 72.616  58.240  70.368 1.00 16.11 ? 293 ILE B C   1 
ATOM   4028 O  O   . ILE B  1 103 ? 73.108  57.332  69.700 1.00 18.63 ? 293 ILE B O   1 
ATOM   4029 C  CB  . ILE B  1 103 ? 70.950  59.507  69.005 1.00 17.28 ? 293 ILE B CB  1 
ATOM   4030 C  CG1 . ILE B  1 103 ? 70.508  60.906  68.571 1.00 21.28 ? 293 ILE B CG1 1 
ATOM   4031 C  CG2 . ILE B  1 103 ? 69.896  58.884  69.908 1.00 17.38 ? 293 ILE B CG2 1 
ATOM   4032 C  CD1 . ILE B  1 103 ? 69.191  60.934  67.837 1.00 24.77 ? 293 ILE B CD1 1 
ATOM   4033 N  N   . ASP B  1 104 ? 72.334  58.111  71.657 1.00 16.40 ? 294 ASP B N   1 
ATOM   4034 C  CA  . ASP B  1 104 ? 72.583  56.863  72.358 1.00 18.10 ? 294 ASP B CA  1 
ATOM   4035 C  C   . ASP B  1 104 ? 71.488  55.877  71.964 1.00 20.15 ? 294 ASP B C   1 
ATOM   4036 O  O   . ASP B  1 104 ? 70.416  55.849  72.572 1.00 21.55 ? 294 ASP B O   1 
ATOM   4037 C  CB  . ASP B  1 104 ? 72.580  57.112  73.869 1.00 20.58 ? 294 ASP B CB  1 
ATOM   4038 C  CG  . ASP B  1 104 ? 73.020  55.899  74.662 1.00 28.16 ? 294 ASP B CG  1 
ATOM   4039 O  OD1 . ASP B  1 104 ? 73.886  55.144  74.167 1.00 29.52 ? 294 ASP B OD1 1 
ATOM   4040 O  OD2 . ASP B  1 104 ? 72.511  55.711  75.788 1.00 31.71 ? 294 ASP B OD2 1 
ATOM   4041 N  N   . LEU B  1 105 ? 71.761  55.086  70.929 1.00 16.93 ? 295 LEU B N   1 
ATOM   4042 C  CA  . LEU B  1 105 ? 70.803  54.102  70.433 1.00 17.67 ? 295 LEU B CA  1 
ATOM   4043 C  C   . LEU B  1 105 ? 70.370  53.142  71.526 1.00 17.55 ? 295 LEU B C   1 
ATOM   4044 O  O   . LEU B  1 105 ? 71.082  52.937  72.506 1.00 21.94 ? 295 LEU B O   1 
ATOM   4045 C  CB  . LEU B  1 105 ? 71.405  53.304  69.273 1.00 13.72 ? 295 LEU B CB  1 
ATOM   4046 C  CG  . LEU B  1 105 ? 71.736  54.048  67.977 1.00 16.57 ? 295 LEU B CG  1 
ATOM   4047 C  CD1 . LEU B  1 105 ? 72.447  53.102  67.024 1.00 17.09 ? 295 LEU B CD1 1 
ATOM   4048 C  CD2 . LEU B  1 105 ? 70.465  54.588  67.339 1.00 14.46 ? 295 LEU B CD2 1 
ATOM   4049 N  N   . ASP B  1 106 ? 69.195  52.553  71.348 1.00 21.23 ? 296 ASP B N   1 
ATOM   4050 C  CA  . ASP B  1 106 ? 68.659  51.607  72.313 1.00 24.41 ? 296 ASP B CA  1 
ATOM   4051 C  C   . ASP B  1 106 ? 69.163  50.199  72.052 1.00 25.26 ? 296 ASP B C   1 
ATOM   4052 O  O   . ASP B  1 106 ? 69.124  49.713  70.921 1.00 28.57 ? 296 ASP B O   1 
ATOM   4053 C  CB  . ASP B  1 106 ? 67.128  51.604  72.266 1.00 29.91 ? 296 ASP B CB  1 
ATOM   4054 C  CG  . ASP B  1 106 ? 66.513  52.811  72.956 1.00 36.09 ? 296 ASP B CG  1 
ATOM   4055 O  OD1 . ASP B  1 106 ? 65.304  53.052  72.755 1.00 39.29 ? 296 ASP B OD1 1 
ATOM   4056 O  OD2 . ASP B  1 106 ? 67.227  53.511  73.704 1.00 39.63 ? 296 ASP B OD2 1 
ATOM   4057 N  N   . ARG B  1 107 ? 69.648  49.559  73.111 1.00 26.31 ? 297 ARG B N   1 
ATOM   4058 C  CA  . ARG B  1 107 ? 70.133  48.182  73.061 1.00 23.97 ? 297 ARG B CA  1 
ATOM   4059 C  C   . ARG B  1 107 ? 71.363  47.887  72.215 1.00 21.17 ? 297 ARG B C   1 
ATOM   4060 O  O   . ARG B  1 107 ? 72.166  47.036  72.585 1.00 25.53 ? 297 ARG B O   1 
ATOM   4061 C  CB  . ARG B  1 107 ? 68.994  47.250  72.631 1.00 21.83 ? 297 ARG B CB  1 
ATOM   4062 C  CG  . ARG B  1 107 ? 67.765  47.345  73.523 1.00 16.44 ? 297 ARG B CG  1 
ATOM   4063 C  CD  . ARG B  1 107 ? 66.752  46.268  73.197 1.00 18.15 ? 297 ARG B CD  1 
ATOM   4064 N  NE  . ARG B  1 107 ? 66.304  46.323  71.809 1.00 19.25 ? 297 ARG B NE  1 
ATOM   4065 C  CZ  . ARG B  1 107 ? 66.398  45.307  70.956 1.00 23.45 ? 297 ARG B CZ  1 
ATOM   4066 N  NH1 . ARG B  1 107 ? 66.929  44.152  71.347 1.00 24.70 ? 297 ARG B NH1 1 
ATOM   4067 N  NH2 . ARG B  1 107 ? 65.959  45.441  69.715 1.00 19.64 ? 297 ARG B NH2 1 
ATOM   4068 N  N   . VAL B  1 108 ? 71.516  48.570  71.086 1.00 22.50 ? 298 VAL B N   1 
ATOM   4069 C  CA  . VAL B  1 108 ? 72.664  48.328  70.213 1.00 17.84 ? 298 VAL B CA  1 
ATOM   4070 C  C   . VAL B  1 108 ? 73.501  49.581  69.962 1.00 16.10 ? 298 VAL B C   1 
ATOM   4071 O  O   . VAL B  1 108 ? 73.144  50.672  70.400 1.00 20.59 ? 298 VAL B O   1 
ATOM   4072 C  CB  . VAL B  1 108 ? 72.206  47.755  68.856 1.00 17.47 ? 298 VAL B CB  1 
ATOM   4073 C  CG1 . VAL B  1 108 ? 71.497  46.436  69.069 1.00 14.76 ? 298 VAL B CG1 1 
ATOM   4074 C  CG2 . VAL B  1 108 ? 71.283  48.735  68.160 1.00 16.30 ? 298 VAL B CG2 1 
ATOM   4075 N  N   . ILE B  1 109 ? 74.618  49.414  69.260 1.00 13.03 ? 299 ILE B N   1 
ATOM   4076 C  CA  . ILE B  1 109 ? 75.506  50.533  68.941 1.00 15.45 ? 299 ILE B CA  1 
ATOM   4077 C  C   . ILE B  1 109 ? 75.568  50.740  67.429 1.00 17.35 ? 299 ILE B C   1 
ATOM   4078 O  O   . ILE B  1 109 ? 76.212  51.669  66.936 1.00 11.44 ? 299 ILE B O   1 
ATOM   4079 C  CB  . ILE B  1 109 ? 76.936  50.278  69.447 1.00 14.02 ? 299 ILE B CB  1 
ATOM   4080 C  CG1 . ILE B  1 109 ? 77.476  48.990  68.825 1.00 15.71 ? 299 ILE B CG1 1 
ATOM   4081 C  CG2 . ILE B  1 109 ? 76.945  50.199  70.963 1.00 10.44 ? 299 ILE B CG2 1 
ATOM   4082 C  CD1 . ILE B  1 109 ? 78.901  48.678  69.205 1.00 20.98 ? 299 ILE B CD1 1 
ATOM   4083 N  N   . GLY B  1 110 ? 74.895  49.853  66.704 1.00 16.49 ? 300 GLY B N   1 
ATOM   4084 C  CA  . GLY B  1 110 ? 74.859  49.931  65.259 1.00 9.65  ? 300 GLY B CA  1 
ATOM   4085 C  C   . GLY B  1 110 ? 73.814  48.967  64.742 1.00 11.83 ? 300 GLY B C   1 
ATOM   4086 O  O   . GLY B  1 110 ? 73.274  48.169  65.508 1.00 12.74 ? 300 GLY B O   1 
ATOM   4087 N  N   . LEU B  1 111 ? 73.519  49.045  63.448 1.00 9.70  ? 301 LEU B N   1 
ATOM   4088 C  CA  . LEU B  1 111 ? 72.535  48.166  62.829 1.00 8.97  ? 301 LEU B CA  1 
ATOM   4089 C  C   . LEU B  1 111 ? 72.622  48.301  61.311 1.00 15.41 ? 301 LEU B C   1 
ATOM   4090 O  O   . LEU B  1 111 ? 72.942  49.375  60.789 1.00 19.19 ? 301 LEU B O   1 
ATOM   4091 C  CB  . LEU B  1 111 ? 71.122  48.529  63.296 1.00 9.97  ? 301 LEU B CB  1 
ATOM   4092 C  CG  . LEU B  1 111 ? 70.033  47.494  62.993 1.00 10.52 ? 301 LEU B CG  1 
ATOM   4093 C  CD1 . LEU B  1 111 ? 70.238  46.282  63.892 1.00 1.00  ? 301 LEU B CD1 1 
ATOM   4094 C  CD2 . LEU B  1 111 ? 68.653  48.094  63.226 1.00 5.28  ? 301 LEU B CD2 1 
ATOM   4095 N  N   . ALA B  1 112 ? 72.330  47.216  60.602 1.00 10.51 ? 302 ALA B N   1 
ATOM   4096 C  CA  . ALA B  1 112 ? 72.387  47.240  59.150 1.00 9.07  ? 302 ALA B CA  1 
ATOM   4097 C  C   . ALA B  1 112 ? 71.764  46.003  58.526 1.00 12.13 ? 302 ALA B C   1 
ATOM   4098 O  O   . ALA B  1 112 ? 71.741  44.932  59.131 1.00 19.15 ? 302 ALA B O   1 
ATOM   4099 C  CB  . ALA B  1 112 ? 73.833  47.365  58.699 1.00 7.71  ? 302 ALA B CB  1 
ATOM   4100 N  N   . TYR B  1 113 ? 71.262  46.158  57.307 1.00 13.37 ? 303 TYR B N   1 
ATOM   4101 C  CA  . TYR B  1 113 ? 70.668  45.047  56.577 1.00 15.73 ? 303 TYR B CA  1 
ATOM   4102 C  C   . TYR B  1 113 ? 71.774  44.040  56.265 1.00 19.42 ? 303 TYR B C   1 
ATOM   4103 O  O   . TYR B  1 113 ? 72.949  44.405  56.198 1.00 25.04 ? 303 TYR B O   1 
ATOM   4104 C  CB  . TYR B  1 113 ? 70.039  45.557  55.281 1.00 10.85 ? 303 TYR B CB  1 
ATOM   4105 C  CG  . TYR B  1 113 ? 68.916  46.545  55.516 1.00 18.98 ? 303 TYR B CG  1 
ATOM   4106 C  CD1 . TYR B  1 113 ? 67.714  46.133  56.095 1.00 12.04 ? 303 TYR B CD1 1 
ATOM   4107 C  CD2 . TYR B  1 113 ? 69.067  47.900  55.199 1.00 15.41 ? 303 TYR B CD2 1 
ATOM   4108 C  CE1 . TYR B  1 113 ? 66.694  47.038  56.356 1.00 12.00 ? 303 TYR B CE1 1 
ATOM   4109 C  CE2 . TYR B  1 113 ? 68.051  48.815  55.458 1.00 15.05 ? 303 TYR B CE2 1 
ATOM   4110 C  CZ  . TYR B  1 113 ? 66.866  48.374  56.041 1.00 16.03 ? 303 TYR B CZ  1 
ATOM   4111 O  OH  . TYR B  1 113 ? 65.860  49.269  56.337 1.00 21.12 ? 303 TYR B OH  1 
ATOM   4112 N  N   . VAL B  1 114 ? 71.403  42.777  56.084 1.00 17.80 ? 304 VAL B N   1 
ATOM   4113 C  CA  . VAL B  1 114 ? 72.376  41.733  55.784 1.00 15.19 ? 304 VAL B CA  1 
ATOM   4114 C  C   . VAL B  1 114 ? 72.384  41.372  54.297 1.00 18.09 ? 304 VAL B C   1 
ATOM   4115 O  O   . VAL B  1 114 ? 71.334  41.302  53.660 1.00 16.03 ? 304 VAL B O   1 
ATOM   4116 C  CB  . VAL B  1 114 ? 72.090  40.459  56.615 1.00 13.41 ? 304 VAL B CB  1 
ATOM   4117 C  CG1 . VAL B  1 114 ? 73.080  39.358  56.251 1.00 14.62 ? 304 VAL B CG1 1 
ATOM   4118 C  CG2 . VAL B  1 114 ? 72.189  40.781  58.098 1.00 7.64  ? 304 VAL B CG2 1 
ATOM   4119 N  N   . GLY B  1 115 ? 73.577  41.139  53.752 1.00 22.68 ? 305 GLY B N   1 
ATOM   4120 C  CA  . GLY B  1 115 ? 73.701  40.789  52.346 1.00 20.67 ? 305 GLY B CA  1 
ATOM   4121 C  C   . GLY B  1 115 ? 72.820  41.661  51.476 1.00 21.01 ? 305 GLY B C   1 
ATOM   4122 O  O   . GLY B  1 115 ? 71.943  41.170  50.773 1.00 19.47 ? 305 GLY B O   1 
ATOM   4123 N  N   . SER B  1 116 ? 73.056  42.966  51.518 1.00 22.17 ? 306 SER B N   1 
ATOM   4124 C  CA  . SER B  1 116 ? 72.251  43.895  50.745 1.00 21.09 ? 306 SER B CA  1 
ATOM   4125 C  C   . SER B  1 116 ? 73.088  44.938  50.020 1.00 23.14 ? 306 SER B C   1 
ATOM   4126 O  O   . SER B  1 116 ? 72.561  45.967  49.589 1.00 24.89 ? 306 SER B O   1 
ATOM   4127 C  CB  . SER B  1 116 ? 71.264  44.595  51.671 1.00 21.48 ? 306 SER B CB  1 
ATOM   4128 O  OG  . SER B  1 116 ? 71.958  45.269  52.705 1.00 22.92 ? 306 SER B OG  1 
ATOM   4129 N  N   . MET B  1 117 ? 74.384  44.676  49.884 1.00 20.79 ? 307 MET B N   1 
ATOM   4130 C  CA  . MET B  1 117 ? 75.277  45.610  49.210 1.00 19.41 ? 307 MET B CA  1 
ATOM   4131 C  C   . MET B  1 117 ? 74.749  45.947  47.820 1.00 19.59 ? 307 MET B C   1 
ATOM   4132 O  O   . MET B  1 117 ? 74.311  45.065  47.087 1.00 18.84 ? 307 MET B O   1 
ATOM   4133 C  CB  . MET B  1 117 ? 76.688  45.018  49.111 1.00 18.96 ? 307 MET B CB  1 
ATOM   4134 C  CG  . MET B  1 117 ? 77.718  45.939  48.461 1.00 17.14 ? 307 MET B CG  1 
ATOM   4135 S  SD  . MET B  1 117 ? 77.878  47.556  49.271 1.00 22.15 ? 307 MET B SD  1 
ATOM   4136 C  CE  . MET B  1 117 ? 78.830  47.089  50.729 1.00 12.58 ? 307 MET B CE  1 
ATOM   4137 N  N   . CYS B  1 118 ? 74.788  47.234  47.483 1.00 20.31 ? 308 CYS B N   1 
ATOM   4138 C  CA  . CYS B  1 118 ? 74.330  47.756  46.196 1.00 25.79 ? 308 CYS B CA  1 
ATOM   4139 C  C   . CYS B  1 118 ? 72.831  47.984  46.113 1.00 25.65 ? 308 CYS B C   1 
ATOM   4140 O  O   . CYS B  1 118 ? 72.351  48.612  45.175 1.00 29.50 ? 308 CYS B O   1 
ATOM   4141 C  CB  . CYS B  1 118 ? 74.760  46.850  45.041 1.00 27.62 ? 308 CYS B CB  1 
ATOM   4142 S  SG  . CYS B  1 118 ? 76.560  46.765  44.797 1.00 41.01 ? 308 CYS B SG  1 
ATOM   4143 N  N   . HIS B  1 119 ? 72.085  47.476  47.083 1.00 29.59 ? 309 HIS B N   1 
ATOM   4144 C  CA  . HIS B  1 119 ? 70.641  47.665  47.076 1.00 28.17 ? 309 HIS B CA  1 
ATOM   4145 C  C   . HIS B  1 119 ? 70.335  49.127  47.407 1.00 28.88 ? 309 HIS B C   1 
ATOM   4146 O  O   . HIS B  1 119 ? 70.883  49.690  48.356 1.00 23.84 ? 309 HIS B O   1 
ATOM   4147 C  CB  . HIS B  1 119 ? 69.980  46.735  48.094 1.00 24.23 ? 309 HIS B CB  1 
ATOM   4148 C  CG  . HIS B  1 119 ? 68.485  46.732  48.027 1.00 26.92 ? 309 HIS B CG  1 
ATOM   4149 N  ND1 . HIS B  1 119 ? 67.721  47.825  48.373 1.00 27.09 ? 309 HIS B ND1 1 
ATOM   4150 C  CD2 . HIS B  1 119 ? 67.611  45.764  47.660 1.00 29.35 ? 309 HIS B CD2 1 
ATOM   4151 C  CE1 . HIS B  1 119 ? 66.441  47.531  48.225 1.00 28.13 ? 309 HIS B CE1 1 
ATOM   4152 N  NE2 . HIS B  1 119 ? 66.348  46.286  47.793 1.00 27.20 ? 309 HIS B NE2 1 
ATOM   4153 N  N   . PRO B  1 120 ? 69.452  49.759  46.622 1.00 29.89 ? 310 PRO B N   1 
ATOM   4154 C  CA  . PRO B  1 120 ? 69.077  51.162  46.831 1.00 30.02 ? 310 PRO B CA  1 
ATOM   4155 C  C   . PRO B  1 120 ? 68.673  51.521  48.258 1.00 29.46 ? 310 PRO B C   1 
ATOM   4156 O  O   . PRO B  1 120 ? 69.165  52.499  48.820 1.00 29.18 ? 310 PRO B O   1 
ATOM   4157 C  CB  . PRO B  1 120 ? 67.940  51.370  45.828 1.00 30.44 ? 310 PRO B CB  1 
ATOM   4158 C  CG  . PRO B  1 120 ? 67.381  49.981  45.638 1.00 33.23 ? 310 PRO B CG  1 
ATOM   4159 C  CD  . PRO B  1 120 ? 68.624  49.148  45.569 1.00 27.05 ? 310 PRO B CD  1 
ATOM   4160 N  N   . LYS B  1 121 ? 67.783  50.730  48.845 1.00 28.06 ? 311 LYS B N   1 
ATOM   4161 C  CA  . LYS B  1 121 ? 67.323  50.995  50.202 1.00 28.38 ? 311 LYS B CA  1 
ATOM   4162 C  C   . LYS B  1 121 ? 68.123  50.271  51.280 1.00 27.60 ? 311 LYS B C   1 
ATOM   4163 O  O   . LYS B  1 121 ? 68.374  50.825  52.350 1.00 29.67 ? 311 LYS B O   1 
ATOM   4164 C  CB  . LYS B  1 121 ? 65.848  50.611  50.339 1.00 28.46 ? 311 LYS B CB  1 
ATOM   4165 C  CG  . LYS B  1 121 ? 65.272  50.821  51.737 1.00 29.52 ? 311 LYS B CG  1 
ATOM   4166 C  CD  . LYS B  1 121 ? 63.855  50.266  51.838 1.00 34.96 ? 311 LYS B CD  1 
ATOM   4167 C  CE  . LYS B  1 121 ? 63.180  50.655  53.148 1.00 35.86 ? 311 LYS B CE  1 
ATOM   4168 N  NZ  . LYS B  1 121 ? 63.939  50.187  54.338 1.00 38.72 ? 311 LYS B NZ  1 
ATOM   4169 N  N   . ARG B  1 122 ? 68.532  49.038  50.994 1.00 27.59 ? 312 ARG B N   1 
ATOM   4170 C  CA  . ARG B  1 122 ? 69.253  48.236  51.974 1.00 22.14 ? 312 ARG B CA  1 
ATOM   4171 C  C   . ARG B  1 122 ? 70.777  48.323  52.017 1.00 22.05 ? 312 ARG B C   1 
ATOM   4172 O  O   . ARG B  1 122 ? 71.394  47.807  52.950 1.00 15.48 ? 312 ARG B O   1 
ATOM   4173 C  CB  . ARG B  1 122 ? 68.821  46.773  51.851 1.00 20.28 ? 312 ARG B CB  1 
ATOM   4174 C  CG  . ARG B  1 122 ? 67.381  46.524  52.283 1.00 25.21 ? 312 ARG B CG  1 
ATOM   4175 C  CD  . ARG B  1 122 ? 67.143  45.049  52.573 1.00 31.09 ? 312 ARG B CD  1 
ATOM   4176 N  NE  . ARG B  1 122 ? 65.850  44.800  53.209 1.00 29.22 ? 312 ARG B NE  1 
ATOM   4177 C  CZ  . ARG B  1 122 ? 65.548  43.685  53.871 1.00 31.10 ? 312 ARG B CZ  1 
ATOM   4178 N  NH1 . ARG B  1 122 ? 66.446  42.715  53.985 1.00 30.83 ? 312 ARG B NH1 1 
ATOM   4179 N  NH2 . ARG B  1 122 ? 64.354  43.540  54.430 1.00 25.85 ? 312 ARG B NH2 1 
ATOM   4180 N  N   . SER B  1 123 ? 71.399  48.957  51.028 1.00 20.18 ? 313 SER B N   1 
ATOM   4181 C  CA  . SER B  1 123 ? 72.851  49.077  51.062 1.00 17.55 ? 313 SER B CA  1 
ATOM   4182 C  C   . SER B  1 123 ? 73.170  50.206  52.034 1.00 18.70 ? 313 SER B C   1 
ATOM   4183 O  O   . SER B  1 123 ? 73.761  51.224  51.663 1.00 15.76 ? 313 SER B O   1 
ATOM   4184 C  CB  . SER B  1 123 ? 73.408  49.404  49.678 1.00 15.28 ? 313 SER B CB  1 
ATOM   4185 O  OG  . SER B  1 123 ? 74.825  49.369  49.693 1.00 23.47 ? 313 SER B OG  1 
ATOM   4186 N  N   . THR B  1 124 ? 72.767  50.010  53.286 1.00 17.35 ? 314 THR B N   1 
ATOM   4187 C  CA  . THR B  1 124 ? 72.967  51.006  54.331 1.00 20.60 ? 314 THR B CA  1 
ATOM   4188 C  C   . THR B  1 124 ? 73.087  50.388  55.722 1.00 18.35 ? 314 THR B C   1 
ATOM   4189 O  O   . THR B  1 124 ? 72.887  49.186  55.910 1.00 15.19 ? 314 THR B O   1 
ATOM   4190 C  CB  . THR B  1 124 ? 71.789  52.004  54.367 1.00 21.54 ? 314 THR B CB  1 
ATOM   4191 O  OG1 . THR B  1 124 ? 70.556  51.274  54.413 1.00 22.99 ? 314 THR B OG1 1 
ATOM   4192 C  CG2 . THR B  1 124 ? 71.794  52.900  53.139 1.00 24.40 ? 314 THR B CG2 1 
ATOM   4193 N  N   . GLY B  1 125 ? 73.410  51.239  56.691 1.00 14.68 ? 315 GLY B N   1 
ATOM   4194 C  CA  . GLY B  1 125 ? 73.543  50.815  58.070 1.00 8.31  ? 315 GLY B CA  1 
ATOM   4195 C  C   . GLY B  1 125 ? 73.732  52.045  58.939 1.00 13.80 ? 315 GLY B C   1 
ATOM   4196 O  O   . GLY B  1 125 ? 74.088  53.113  58.436 1.00 12.80 ? 315 GLY B O   1 
ATOM   4197 N  N   . ILE B  1 126 ? 73.486  51.921  60.238 1.00 10.29 ? 316 ILE B N   1 
ATOM   4198 C  CA  . ILE B  1 126 ? 73.674  53.060  61.124 1.00 9.96  ? 316 ILE B CA  1 
ATOM   4199 C  C   . ILE B  1 126 ? 74.734  52.717  62.168 1.00 11.43 ? 316 ILE B C   1 
ATOM   4200 O  O   . ILE B  1 126 ? 74.833  51.572  62.614 1.00 12.01 ? 316 ILE B O   1 
ATOM   4201 C  CB  . ILE B  1 126 ? 72.347  53.472  61.826 1.00 9.65  ? 316 ILE B CB  1 
ATOM   4202 C  CG1 . ILE B  1 126 ? 71.957  52.448  62.892 1.00 11.63 ? 316 ILE B CG1 1 
ATOM   4203 C  CG2 . ILE B  1 126 ? 71.235  53.570  60.802 1.00 1.00  ? 316 ILE B CG2 1 
ATOM   4204 C  CD1 . ILE B  1 126 ? 70.767  52.879  63.737 1.00 11.33 ? 316 ILE B CD1 1 
ATOM   4205 N  N   . ILE B  1 127 ? 75.538  53.711  62.533 1.00 11.85 ? 317 ILE B N   1 
ATOM   4206 C  CA  . ILE B  1 127 ? 76.596  53.536  63.519 1.00 14.87 ? 317 ILE B CA  1 
ATOM   4207 C  C   . ILE B  1 127 ? 76.483  54.619  64.582 1.00 22.44 ? 317 ILE B C   1 
ATOM   4208 O  O   . ILE B  1 127 ? 76.176  55.770  64.270 1.00 25.14 ? 317 ILE B O   1 
ATOM   4209 C  CB  . ILE B  1 127 ? 78.011  53.658  62.884 1.00 16.70 ? 317 ILE B CB  1 
ATOM   4210 C  CG1 . ILE B  1 127 ? 78.321  52.444  62.004 1.00 18.67 ? 317 ILE B CG1 1 
ATOM   4211 C  CG2 . ILE B  1 127 ? 79.063  53.777  63.977 1.00 13.31 ? 317 ILE B CG2 1 
ATOM   4212 C  CD1 . ILE B  1 127 ? 77.572  52.419  60.700 1.00 23.07 ? 317 ILE B CD1 1 
ATOM   4213 N  N   . GLN B  1 128 ? 76.733  54.252  65.836 1.00 23.46 ? 318 GLN B N   1 
ATOM   4214 C  CA  . GLN B  1 128 ? 76.681  55.225  66.919 1.00 22.75 ? 318 GLN B CA  1 
ATOM   4215 C  C   . GLN B  1 128 ? 78.096  55.652  67.269 1.00 22.17 ? 318 GLN B C   1 
ATOM   4216 O  O   . GLN B  1 128 ? 78.980  54.807  67.412 1.00 20.35 ? 318 GLN B O   1 
ATOM   4217 C  CB  . GLN B  1 128 ? 76.024  54.632  68.166 1.00 22.44 ? 318 GLN B CB  1 
ATOM   4218 C  CG  . GLN B  1 128 ? 75.912  55.629  69.316 1.00 16.53 ? 318 GLN B CG  1 
ATOM   4219 C  CD  . GLN B  1 128 ? 75.302  55.032  70.565 1.00 18.24 ? 318 GLN B CD  1 
ATOM   4220 O  OE1 . GLN B  1 128 ? 74.304  54.318  70.501 1.00 23.80 ? 318 GLN B OE1 1 
ATOM   4221 N  NE2 . GLN B  1 128 ? 75.891  55.334  71.714 1.00 8.72  ? 318 GLN B NE2 1 
ATOM   4222 N  N   . ASP B  1 129 ? 78.306  56.963  67.392 1.00 21.75 ? 319 ASP B N   1 
ATOM   4223 C  CA  . ASP B  1 129 ? 79.611  57.508  67.754 1.00 19.71 ? 319 ASP B CA  1 
ATOM   4224 C  C   . ASP B  1 129 ? 79.831  57.160  69.226 1.00 18.23 ? 319 ASP B C   1 
ATOM   4225 O  O   . ASP B  1 129 ? 79.752  58.010  70.111 1.00 16.26 ? 319 ASP B O   1 
ATOM   4226 C  CB  . ASP B  1 129 ? 79.624  59.023  67.540 1.00 21.01 ? 319 ASP B CB  1 
ATOM   4227 C  CG  . ASP B  1 129 ? 80.973  59.640  67.833 1.00 26.39 ? 319 ASP B CG  1 
ATOM   4228 O  OD1 . ASP B  1 129 ? 81.991  59.073  67.382 1.00 22.12 ? 319 ASP B OD1 1 
ATOM   4229 O  OD2 . ASP B  1 129 ? 81.015  60.694  68.505 1.00 28.89 ? 319 ASP B OD2 1 
ATOM   4230 N  N   . TYR B  1 130 ? 80.110  55.881  69.448 1.00 21.91 ? 320 TYR B N   1 
ATOM   4231 C  CA  . TYR B  1 130 ? 80.315  55.270  70.759 1.00 24.04 ? 320 TYR B CA  1 
ATOM   4232 C  C   . TYR B  1 130 ? 81.535  55.727  71.562 1.00 24.00 ? 320 TYR B C   1 
ATOM   4233 O  O   . TYR B  1 130 ? 81.461  55.858  72.782 1.00 23.17 ? 320 TYR B O   1 
ATOM   4234 C  CB  . TYR B  1 130 ? 80.382  53.751  70.562 1.00 28.87 ? 320 TYR B CB  1 
ATOM   4235 C  CG  . TYR B  1 130 ? 80.038  52.924  71.771 1.00 28.92 ? 320 TYR B CG  1 
ATOM   4236 C  CD1 . TYR B  1 130 ? 78.819  53.091  72.424 1.00 36.15 ? 320 TYR B CD1 1 
ATOM   4237 C  CD2 . TYR B  1 130 ? 80.912  51.948  72.241 1.00 26.14 ? 320 TYR B CD2 1 
ATOM   4238 C  CE1 . TYR B  1 130 ? 78.475  52.302  73.519 1.00 41.71 ? 320 TYR B CE1 1 
ATOM   4239 C  CE2 . TYR B  1 130 ? 80.580  51.153  73.334 1.00 34.44 ? 320 TYR B CE2 1 
ATOM   4240 C  CZ  . TYR B  1 130 ? 79.359  51.334  73.968 1.00 40.56 ? 320 TYR B CZ  1 
ATOM   4241 O  OH  . TYR B  1 130 ? 79.013  50.546  75.044 1.00 48.19 ? 320 TYR B OH  1 
ATOM   4242 N  N   . SER B  1 131 ? 82.652  55.969  70.884 1.00 22.81 ? 321 SER B N   1 
ATOM   4243 C  CA  . SER B  1 131 ? 83.876  56.365  71.571 1.00 22.50 ? 321 SER B CA  1 
ATOM   4244 C  C   . SER B  1 131 ? 84.690  57.470  70.894 1.00 22.91 ? 321 SER B C   1 
ATOM   4245 O  O   . SER B  1 131 ? 84.503  57.772  69.717 1.00 22.04 ? 321 SER B O   1 
ATOM   4246 C  CB  . SER B  1 131 ? 84.762  55.124  71.753 1.00 22.71 ? 321 SER B CB  1 
ATOM   4247 O  OG  . SER B  1 131 ? 86.082  55.465  72.144 1.00 20.79 ? 321 SER B OG  1 
ATOM   4248 N  N   . GLU B  1 132 ? 85.594  58.070  71.663 1.00 23.28 ? 322 GLU B N   1 
ATOM   4249 C  CA  . GLU B  1 132 ? 86.479  59.112  71.157 1.00 25.11 ? 322 GLU B CA  1 
ATOM   4250 C  C   . GLU B  1 132 ? 87.546  58.446  70.299 1.00 24.03 ? 322 GLU B C   1 
ATOM   4251 O  O   . GLU B  1 132 ? 88.125  59.068  69.409 1.00 24.00 ? 322 GLU B O   1 
ATOM   4252 C  CB  . GLU B  1 132 ? 87.151  59.856  72.318 1.00 30.54 ? 322 GLU B CB  1 
ATOM   4253 C  CG  . GLU B  1 132 ? 86.470  61.159  72.695 1.00 40.79 ? 322 GLU B CG  1 
ATOM   4254 C  CD  . GLU B  1 132 ? 86.543  62.198  71.584 1.00 45.67 ? 322 GLU B CD  1 
ATOM   4255 O  OE1 . GLU B  1 132 ? 85.885  63.255  71.711 1.00 50.04 ? 322 GLU B OE1 1 
ATOM   4256 O  OE2 . GLU B  1 132 ? 87.263  61.961  70.586 1.00 48.19 ? 322 GLU B OE2 1 
ATOM   4257 N  N   . ILE B  1 133 ? 87.792  57.170  70.586 1.00 22.69 ? 323 ILE B N   1 
ATOM   4258 C  CA  . ILE B  1 133 ? 88.780  56.369  69.872 1.00 19.83 ? 323 ILE B CA  1 
ATOM   4259 C  C   . ILE B  1 133 ? 88.297  56.060  68.459 1.00 20.26 ? 323 ILE B C   1 
ATOM   4260 O  O   . ILE B  1 133 ? 87.299  55.361  68.275 1.00 24.70 ? 323 ILE B O   1 
ATOM   4261 C  CB  . ILE B  1 133 ? 89.028  55.041  70.604 1.00 20.27 ? 323 ILE B CB  1 
ATOM   4262 C  CG1 . ILE B  1 133 ? 89.311  55.311  72.080 1.00 11.91 ? 323 ILE B CG1 1 
ATOM   4263 C  CG2 . ILE B  1 133 ? 90.187  54.302  69.959 1.00 16.02 ? 323 ILE B CG2 1 
ATOM   4264 C  CD1 . ILE B  1 133 ? 89.508  54.060  72.898 1.00 13.35 ? 323 ILE B CD1 1 
ATOM   4265 N  N   . ASN B  1 134 ? 89.017  56.568  67.465 1.00 17.97 ? 324 ASN B N   1 
ATOM   4266 C  CA  . ASN B  1 134 ? 88.644  56.364  66.072 1.00 14.89 ? 324 ASN B CA  1 
ATOM   4267 C  C   . ASN B  1 134 ? 88.562  54.909  65.642 1.00 13.91 ? 324 ASN B C   1 
ATOM   4268 O  O   . ASN B  1 134 ? 87.659  54.531  64.898 1.00 17.69 ? 324 ASN B O   1 
ATOM   4269 C  CB  . ASN B  1 134 ? 89.596  57.146  65.168 1.00 7.80  ? 324 ASN B CB  1 
ATOM   4270 C  CG  . ASN B  1 134 ? 89.438  58.643  65.341 1.00 15.90 ? 324 ASN B CG  1 
ATOM   4271 O  OD1 . ASN B  1 134 ? 90.149  59.440  64.730 1.00 18.21 ? 324 ASN B OD1 1 
ATOM   4272 N  ND2 . ASN B  1 134 ? 88.492  59.034  66.187 1.00 19.38 ? 324 ASN B ND2 1 
ATOM   4273 N  N   . LEU B  1 135 ? 89.493  54.086  66.108 1.00 15.53 ? 325 LEU B N   1 
ATOM   4274 C  CA  . LEU B  1 135 ? 89.480  52.670  65.752 1.00 15.04 ? 325 LEU B CA  1 
ATOM   4275 C  C   . LEU B  1 135 ? 88.179  51.998  66.207 1.00 15.75 ? 325 LEU B C   1 
ATOM   4276 O  O   . LEU B  1 135 ? 87.613  51.171  65.488 1.00 16.78 ? 325 LEU B O   1 
ATOM   4277 C  CB  . LEU B  1 135 ? 90.682  51.960  66.379 1.00 8.41  ? 325 LEU B CB  1 
ATOM   4278 C  CG  . LEU B  1 135 ? 90.726  50.438  66.253 1.00 6.10  ? 325 LEU B CG  1 
ATOM   4279 C  CD1 . LEU B  1 135 ? 90.733  50.032  64.786 1.00 8.28  ? 325 LEU B CD1 1 
ATOM   4280 C  CD2 . LEU B  1 135 ? 91.961  49.910  66.967 1.00 4.49  ? 325 LEU B CD2 1 
ATOM   4281 N  N   . VAL B  1 136 ? 87.704  52.360  67.397 1.00 14.28 ? 326 VAL B N   1 
ATOM   4282 C  CA  . VAL B  1 136 ? 86.471  51.786  67.924 1.00 14.37 ? 326 VAL B CA  1 
ATOM   4283 C  C   . VAL B  1 136 ? 85.311  52.049  66.970 1.00 15.06 ? 326 VAL B C   1 
ATOM   4284 O  O   . VAL B  1 136 ? 84.557  51.134  66.633 1.00 22.36 ? 326 VAL B O   1 
ATOM   4285 C  CB  . VAL B  1 136 ? 86.124  52.366  69.326 1.00 17.28 ? 326 VAL B CB  1 
ATOM   4286 C  CG1 . VAL B  1 136 ? 84.741  51.908  69.765 1.00 1.00  ? 326 VAL B CG1 1 
ATOM   4287 C  CG2 . VAL B  1 136 ? 87.157  51.912  70.343 1.00 12.06 ? 326 VAL B CG2 1 
ATOM   4288 N  N   . VAL B  1 137 ? 85.170  53.297  66.535 1.00 10.93 ? 327 VAL B N   1 
ATOM   4289 C  CA  . VAL B  1 137 ? 84.095  53.661  65.614 1.00 11.32 ? 327 VAL B CA  1 
ATOM   4290 C  C   . VAL B  1 137 ? 84.329  53.058  64.223 1.00 11.94 ? 327 VAL B C   1 
ATOM   4291 O  O   . VAL B  1 137 ? 83.376  52.746  63.507 1.00 11.63 ? 327 VAL B O   1 
ATOM   4292 C  CB  . VAL B  1 137 ? 83.953  55.204  65.501 1.00 9.15  ? 327 VAL B CB  1 
ATOM   4293 C  CG1 . VAL B  1 137 ? 82.946  55.567  64.433 1.00 6.20  ? 327 VAL B CG1 1 
ATOM   4294 C  CG2 . VAL B  1 137 ? 83.502  55.777  66.832 1.00 3.92  ? 327 VAL B CG2 1 
ATOM   4295 N  N   . ALA B  1 138 ? 85.593  52.888  63.848 1.00 5.51  ? 328 ALA B N   1 
ATOM   4296 C  CA  . ALA B  1 138 ? 85.928  52.313  62.551 1.00 11.95 ? 328 ALA B CA  1 
ATOM   4297 C  C   . ALA B  1 138 ? 85.497  50.849  62.495 1.00 17.31 ? 328 ALA B C   1 
ATOM   4298 O  O   . ALA B  1 138 ? 84.929  50.396  61.496 1.00 16.43 ? 328 ALA B O   1 
ATOM   4299 C  CB  . ALA B  1 138 ? 87.425  52.427  62.295 1.00 15.63 ? 328 ALA B CB  1 
ATOM   4300 N  N   . VAL B  1 139 ? 85.768  50.112  63.569 1.00 15.89 ? 329 VAL B N   1 
ATOM   4301 C  CA  . VAL B  1 139 ? 85.399  48.704  63.626 1.00 14.60 ? 329 VAL B CA  1 
ATOM   4302 C  C   . VAL B  1 139 ? 83.884  48.540  63.518 1.00 12.40 ? 329 VAL B C   1 
ATOM   4303 O  O   . VAL B  1 139 ? 83.406  47.628  62.839 1.00 14.53 ? 329 VAL B O   1 
ATOM   4304 C  CB  . VAL B  1 139 ? 85.909  48.032  64.936 1.00 20.29 ? 329 VAL B CB  1 
ATOM   4305 C  CG1 . VAL B  1 139 ? 85.466  46.576  64.991 1.00 17.78 ? 329 VAL B CG1 1 
ATOM   4306 C  CG2 . VAL B  1 139 ? 87.428  48.095  64.997 1.00 15.48 ? 329 VAL B CG2 1 
ATOM   4307 N  N   . ILE B  1 140 ? 83.130  49.418  64.177 1.00 11.02 ? 330 ILE B N   1 
ATOM   4308 C  CA  . ILE B  1 140 ? 81.664  49.349  64.123 1.00 11.13 ? 330 ILE B CA  1 
ATOM   4309 C  C   . ILE B  1 140 ? 81.196  49.546  62.681 1.00 8.39  ? 330 ILE B C   1 
ATOM   4310 O  O   . ILE B  1 140 ? 80.368  48.788  62.169 1.00 2.97  ? 330 ILE B O   1 
ATOM   4311 C  CB  . ILE B  1 140 ? 80.984  50.451  64.987 1.00 12.05 ? 330 ILE B CB  1 
ATOM   4312 C  CG1 . ILE B  1 140 ? 81.474  50.387  66.433 1.00 11.83 ? 330 ILE B CG1 1 
ATOM   4313 C  CG2 . ILE B  1 140 ? 79.477  50.268  64.957 1.00 5.04  ? 330 ILE B CG2 1 
ATOM   4314 C  CD1 . ILE B  1 140 ? 80.789  51.383  67.347 1.00 3.72  ? 330 ILE B CD1 1 
ATOM   4315 N  N   . MET B  1 141 ? 81.734  50.578  62.039 1.00 10.42 ? 331 MET B N   1 
ATOM   4316 C  CA  . MET B  1 141 ? 81.391  50.896  60.661 1.00 14.97 ? 331 MET B CA  1 
ATOM   4317 C  C   . MET B  1 141 ? 81.708  49.690  59.774 1.00 15.57 ? 331 MET B C   1 
ATOM   4318 O  O   . MET B  1 141 ? 80.863  49.232  59.002 1.00 18.16 ? 331 MET B O   1 
ATOM   4319 C  CB  . MET B  1 141 ? 82.186  52.123  60.205 1.00 19.26 ? 331 MET B CB  1 
ATOM   4320 C  CG  . MET B  1 141 ? 81.629  52.820  58.969 1.00 29.77 ? 331 MET B CG  1 
ATOM   4321 S  SD  . MET B  1 141 ? 82.541  54.331  58.545 1.00 33.46 ? 331 MET B SD  1 
ATOM   4322 C  CE  . MET B  1 141 ? 82.110  55.378  59.950 1.00 16.02 ? 331 MET B CE  1 
ATOM   4323 N  N   . ALA B  1 142 ? 82.927  49.173  59.893 1.00 15.72 ? 332 ALA B N   1 
ATOM   4324 C  CA  . ALA B  1 142 ? 83.334  48.014  59.107 1.00 15.76 ? 332 ALA B CA  1 
ATOM   4325 C  C   . ALA B  1 142 ? 82.388  46.864  59.427 1.00 18.58 ? 332 ALA B C   1 
ATOM   4326 O  O   . ALA B  1 142 ? 81.976  46.111  58.537 1.00 15.83 ? 332 ALA B O   1 
ATOM   4327 C  CB  . ALA B  1 142 ? 84.763  47.625  59.445 1.00 16.19 ? 332 ALA B CB  1 
ATOM   4328 N  N   . HIS B  1 143 ? 82.048  46.740  60.707 1.00 17.45 ? 333 HIS B N   1 
ATOM   4329 C  CA  . HIS B  1 143 ? 81.146  45.693  61.163 1.00 14.32 ? 333 HIS B CA  1 
ATOM   4330 C  C   . HIS B  1 143 ? 79.828  45.794  60.406 1.00 14.16 ? 333 HIS B C   1 
ATOM   4331 O  O   . HIS B  1 143 ? 79.377  44.824  59.796 1.00 12.66 ? 333 HIS B O   1 
ATOM   4332 C  CB  . HIS B  1 143 ? 80.878  45.835  62.662 1.00 17.47 ? 333 HIS B CB  1 
ATOM   4333 C  CG  . HIS B  1 143 ? 80.000  44.759  63.224 1.00 18.30 ? 333 HIS B CG  1 
ATOM   4334 N  ND1 . HIS B  1 143 ? 80.503  43.603  63.785 1.00 9.36  ? 333 HIS B ND1 1 
ATOM   4335 C  CD2 . HIS B  1 143 ? 78.651  44.649  63.279 1.00 10.71 ? 333 HIS B CD2 1 
ATOM   4336 C  CE1 . HIS B  1 143 ? 79.500  42.829  64.161 1.00 13.84 ? 333 HIS B CE1 1 
ATOM   4337 N  NE2 . HIS B  1 143 ? 78.367  43.440  63.864 1.00 13.08 ? 333 HIS B NE2 1 
ATOM   4338 N  N   . GLU B  1 144 ? 79.216  46.977  60.447 1.00 15.44 ? 334 GLU B N   1 
ATOM   4339 C  CA  . GLU B  1 144 ? 77.945  47.197  59.771 1.00 16.23 ? 334 GLU B CA  1 
ATOM   4340 C  C   . GLU B  1 144 ? 78.030  46.930  58.271 1.00 17.32 ? 334 GLU B C   1 
ATOM   4341 O  O   . GLU B  1 144 ? 77.134  46.302  57.699 1.00 14.17 ? 334 GLU B O   1 
ATOM   4342 C  CB  . GLU B  1 144 ? 77.438  48.620  60.025 1.00 15.33 ? 334 GLU B CB  1 
ATOM   4343 C  CG  . GLU B  1 144 ? 77.012  48.884  61.467 1.00 17.32 ? 334 GLU B CG  1 
ATOM   4344 C  CD  . GLU B  1 144 ? 76.186  47.750  62.059 1.00 18.45 ? 334 GLU B CD  1 
ATOM   4345 O  OE1 . GLU B  1 144 ? 75.449  47.083  61.302 1.00 20.25 ? 334 GLU B OE1 1 
ATOM   4346 O  OE2 . GLU B  1 144 ? 76.265  47.531  63.286 1.00 15.65 ? 334 GLU B OE2 1 
ATOM   4347 N  N   . MET B  1 145 ? 79.094  47.406  57.630 1.00 16.35 ? 335 MET B N   1 
ATOM   4348 C  CA  . MET B  1 145 ? 79.256  47.163  56.203 1.00 18.57 ? 335 MET B CA  1 
ATOM   4349 C  C   . MET B  1 145 ? 79.409  45.662  55.991 1.00 19.78 ? 335 MET B C   1 
ATOM   4350 O  O   . MET B  1 145 ? 78.998  45.123  54.964 1.00 19.27 ? 335 MET B O   1 
ATOM   4351 C  CB  . MET B  1 145 ? 80.477  47.903  55.658 1.00 22.93 ? 335 MET B CB  1 
ATOM   4352 C  CG  . MET B  1 145 ? 80.159  49.285  55.111 1.00 32.40 ? 335 MET B CG  1 
ATOM   4353 S  SD  . MET B  1 145 ? 81.578  50.073  54.329 1.00 38.70 ? 335 MET B SD  1 
ATOM   4354 C  CE  . MET B  1 145 ? 81.913  48.899  52.990 1.00 26.75 ? 335 MET B CE  1 
ATOM   4355 N  N   . GLY B  1 146 ? 80.001  44.991  56.975 1.00 18.54 ? 336 GLY B N   1 
ATOM   4356 C  CA  . GLY B  1 146 ? 80.169  43.554  56.886 1.00 19.35 ? 336 GLY B CA  1 
ATOM   4357 C  C   . GLY B  1 146 ? 78.808  42.901  56.722 1.00 22.59 ? 336 GLY B C   1 
ATOM   4358 O  O   . GLY B  1 146 ? 78.616  42.029  55.871 1.00 27.16 ? 336 GLY B O   1 
ATOM   4359 N  N   . HIS B  1 147 ? 77.852  43.324  57.541 1.00 17.79 ? 337 HIS B N   1 
ATOM   4360 C  CA  . HIS B  1 147 ? 76.509  42.781  57.452 1.00 15.91 ? 337 HIS B CA  1 
ATOM   4361 C  C   . HIS B  1 147 ? 75.972  43.036  56.048 1.00 20.76 ? 337 HIS B C   1 
ATOM   4362 O  O   . HIS B  1 147 ? 75.254  42.207  55.493 1.00 26.33 ? 337 HIS B O   1 
ATOM   4363 C  CB  . HIS B  1 147 ? 75.594  43.437  58.487 1.00 15.71 ? 337 HIS B CB  1 
ATOM   4364 C  CG  . HIS B  1 147 ? 75.763  42.900  59.875 1.00 20.39 ? 337 HIS B CG  1 
ATOM   4365 N  ND1 . HIS B  1 147 ? 75.577  41.571  60.185 1.00 23.96 ? 337 HIS B ND1 1 
ATOM   4366 C  CD2 . HIS B  1 147 ? 76.075  43.517  61.040 1.00 20.65 ? 337 HIS B CD2 1 
ATOM   4367 C  CE1 . HIS B  1 147 ? 75.766  41.392  61.480 1.00 18.66 ? 337 HIS B CE1 1 
ATOM   4368 N  NE2 . HIS B  1 147 ? 76.069  42.557  62.022 1.00 8.14  ? 337 HIS B NE2 1 
ATOM   4369 N  N   . ASN B  1 148 ? 76.326  44.184  55.476 1.00 19.36 ? 338 ASN B N   1 
ATOM   4370 C  CA  . ASN B  1 148 ? 75.877  44.538  54.132 1.00 20.51 ? 338 ASN B CA  1 
ATOM   4371 C  C   . ASN B  1 148 ? 76.453  43.587  53.087 1.00 21.64 ? 338 ASN B C   1 
ATOM   4372 O  O   . ASN B  1 148 ? 75.829  43.326  52.059 1.00 20.57 ? 338 ASN B O   1 
ATOM   4373 C  CB  . ASN B  1 148 ? 76.291  45.975  53.787 1.00 18.91 ? 338 ASN B CB  1 
ATOM   4374 C  CG  . ASN B  1 148 ? 75.384  47.014  54.413 1.00 21.62 ? 338 ASN B CG  1 
ATOM   4375 O  OD1 . ASN B  1 148 ? 75.641  48.215  54.313 1.00 20.31 ? 338 ASN B OD1 1 
ATOM   4376 N  ND2 . ASN B  1 148 ? 74.311  46.560  55.056 1.00 21.67 ? 338 ASN B ND2 1 
ATOM   4377 N  N   . LEU B  1 149 ? 77.649  43.075  53.357 1.00 22.71 ? 339 LEU B N   1 
ATOM   4378 C  CA  . LEU B  1 149 ? 78.316  42.161  52.441 1.00 24.23 ? 339 LEU B CA  1 
ATOM   4379 C  C   . LEU B  1 149 ? 77.980  40.693  52.716 1.00 24.22 ? 339 LEU B C   1 
ATOM   4380 O  O   . LEU B  1 149 ? 78.767  39.795  52.401 1.00 24.98 ? 339 LEU B O   1 
ATOM   4381 C  CB  . LEU B  1 149 ? 79.830  42.377  52.515 1.00 23.89 ? 339 LEU B CB  1 
ATOM   4382 C  CG  . LEU B  1 149 ? 80.326  43.719  51.978 1.00 24.98 ? 339 LEU B CG  1 
ATOM   4383 C  CD1 . LEU B  1 149 ? 81.809  43.882  52.262 1.00 23.90 ? 339 LEU B CD1 1 
ATOM   4384 C  CD2 . LEU B  1 149 ? 80.057  43.790  50.484 1.00 29.05 ? 339 LEU B CD2 1 
ATOM   4385 N  N   . GLY B  1 150 ? 76.809  40.457  53.301 1.00 19.34 ? 340 GLY B N   1 
ATOM   4386 C  CA  . GLY B  1 150 ? 76.382  39.102  53.598 1.00 19.68 ? 340 GLY B CA  1 
ATOM   4387 C  C   . GLY B  1 150 ? 77.149  38.390  54.702 1.00 21.57 ? 340 GLY B C   1 
ATOM   4388 O  O   . GLY B  1 150 ? 77.005  37.178  54.874 1.00 20.96 ? 340 GLY B O   1 
ATOM   4389 N  N   . ILE B  1 151 ? 77.960  39.128  55.455 1.00 18.45 ? 341 ILE B N   1 
ATOM   4390 C  CA  . ILE B  1 151 ? 78.738  38.535  56.537 1.00 18.06 ? 341 ILE B CA  1 
ATOM   4391 C  C   . ILE B  1 151 ? 77.936  38.534  57.834 1.00 18.22 ? 341 ILE B C   1 
ATOM   4392 O  O   . ILE B  1 151 ? 77.171  39.460  58.101 1.00 17.04 ? 341 ILE B O   1 
ATOM   4393 C  CB  . ILE B  1 151 ? 80.055  39.308  56.781 1.00 16.07 ? 341 ILE B CB  1 
ATOM   4394 C  CG1 . ILE B  1 151 ? 80.826  39.455  55.467 1.00 15.72 ? 341 ILE B CG1 1 
ATOM   4395 C  CG2 . ILE B  1 151 ? 80.904  38.573  57.814 1.00 12.48 ? 341 ILE B CG2 1 
ATOM   4396 C  CD1 . ILE B  1 151 ? 82.093  40.281  55.579 1.00 1.00  ? 341 ILE B CD1 1 
ATOM   4397 N  N   . ASN B  1 152 ? 78.121  37.491  58.637 1.00 17.79 ? 342 ASN B N   1 
ATOM   4398 C  CA  . ASN B  1 152 ? 77.416  37.372  59.906 1.00 18.72 ? 342 ASN B CA  1 
ATOM   4399 C  C   . ASN B  1 152 ? 78.387  37.416  61.078 1.00 21.10 ? 342 ASN B C   1 
ATOM   4400 O  O   . ASN B  1 152 ? 79.583  37.645  60.892 1.00 22.99 ? 342 ASN B O   1 
ATOM   4401 C  CB  . ASN B  1 152 ? 76.601  36.079  59.930 1.00 24.56 ? 342 ASN B CB  1 
ATOM   4402 C  CG  . ASN B  1 152 ? 75.419  36.118  58.968 1.00 35.62 ? 342 ASN B CG  1 
ATOM   4403 O  OD1 . ASN B  1 152 ? 74.461  36.868  59.171 1.00 33.95 ? 342 ASN B OD1 1 
ATOM   4404 N  ND2 . ASN B  1 152 ? 75.488  35.313  57.911 1.00 38.91 ? 342 ASN B ND2 1 
ATOM   4405 N  N   . HIS B  1 153 ? 77.873  37.200  62.284 1.00 20.96 ? 343 HIS B N   1 
ATOM   4406 C  CA  . HIS B  1 153 ? 78.704  37.238  63.481 1.00 20.39 ? 343 HIS B CA  1 
ATOM   4407 C  C   . HIS B  1 153 ? 79.550  35.996  63.670 1.00 21.54 ? 343 HIS B C   1 
ATOM   4408 O  O   . HIS B  1 153 ? 79.190  34.910  63.224 1.00 22.90 ? 343 HIS B O   1 
ATOM   4409 C  CB  . HIS B  1 153 ? 77.833  37.459  64.717 1.00 18.74 ? 343 HIS B CB  1 
ATOM   4410 C  CG  . HIS B  1 153 ? 77.211  38.819  64.774 1.00 20.60 ? 343 HIS B CG  1 
ATOM   4411 N  ND1 . HIS B  1 153 ? 76.261  39.165  65.708 1.00 18.23 ? 343 HIS B ND1 1 
ATOM   4412 C  CD2 . HIS B  1 153 ? 77.410  39.921  64.013 1.00 20.48 ? 343 HIS B CD2 1 
ATOM   4413 C  CE1 . HIS B  1 153 ? 75.900  40.422  65.520 1.00 24.66 ? 343 HIS B CE1 1 
ATOM   4414 N  NE2 . HIS B  1 153 ? 76.583  40.903  64.498 1.00 23.75 ? 343 HIS B NE2 1 
ATOM   4415 N  N   . ASP B  1 154 ? 80.689  36.168  64.331 1.00 23.60 ? 344 ASP B N   1 
ATOM   4416 C  CA  . ASP B  1 154 ? 81.586  35.053  64.583 1.00 26.28 ? 344 ASP B CA  1 
ATOM   4417 C  C   . ASP B  1 154 ? 81.040  34.175  65.700 1.00 28.80 ? 344 ASP B C   1 
ATOM   4418 O  O   . ASP B  1 154 ? 80.477  34.664  66.682 1.00 31.29 ? 344 ASP B O   1 
ATOM   4419 C  CB  . ASP B  1 154 ? 82.984  35.559  64.957 1.00 26.89 ? 344 ASP B CB  1 
ATOM   4420 C  CG  . ASP B  1 154 ? 83.673  36.273  63.808 1.00 26.42 ? 344 ASP B CG  1 
ATOM   4421 O  OD1 . ASP B  1 154 ? 83.615  35.760  62.672 1.00 21.66 ? 344 ASP B OD1 1 
ATOM   4422 O  OD2 . ASP B  1 154 ? 84.281  37.339  64.039 1.00 30.50 ? 344 ASP B OD2 1 
ATOM   4423 N  N   . SER B  1 155 ? 81.204  32.870  65.537 1.00 30.64 ? 345 SER B N   1 
ATOM   4424 C  CA  . SER B  1 155 ? 80.740  31.914  66.528 1.00 30.49 ? 345 SER B CA  1 
ATOM   4425 C  C   . SER B  1 155 ? 81.706  30.750  66.544 1.00 32.02 ? 345 SER B C   1 
ATOM   4426 O  O   . SER B  1 155 ? 82.500  30.580  65.617 1.00 34.73 ? 345 SER B O   1 
ATOM   4427 C  CB  . SER B  1 155 ? 79.351  31.404  66.164 1.00 31.62 ? 345 SER B CB  1 
ATOM   4428 O  OG  . SER B  1 155 ? 79.386  30.728  64.920 1.00 42.26 ? 345 SER B OG  1 
ATOM   4429 N  N   . GLY B  1 156 ? 81.638  29.949  67.598 1.00 29.04 ? 346 GLY B N   1 
ATOM   4430 C  CA  . GLY B  1 156 ? 82.518  28.804  67.692 1.00 30.75 ? 346 GLY B CA  1 
ATOM   4431 C  C   . GLY B  1 156 ? 83.982  29.143  67.494 1.00 30.77 ? 346 GLY B C   1 
ATOM   4432 O  O   . GLY B  1 156 ? 84.476  30.150  68.002 1.00 31.00 ? 346 GLY B O   1 
ATOM   4433 N  N   . TYR B  1 157 ? 84.673  28.310  66.726 1.00 27.48 ? 347 TYR B N   1 
ATOM   4434 C  CA  . TYR B  1 157 ? 86.092  28.501  66.498 1.00 23.67 ? 347 TYR B CA  1 
ATOM   4435 C  C   . TYR B  1 157 ? 86.508  29.448  65.384 1.00 23.73 ? 347 TYR B C   1 
ATOM   4436 O  O   . TYR B  1 157 ? 87.579  29.282  64.803 1.00 24.02 ? 347 TYR B O   1 
ATOM   4437 C  CB  . TYR B  1 157 ? 86.764  27.139  66.304 1.00 25.41 ? 347 TYR B CB  1 
ATOM   4438 C  CG  . TYR B  1 157 ? 86.776  26.313  67.569 1.00 22.91 ? 347 TYR B CG  1 
ATOM   4439 C  CD1 . TYR B  1 157 ? 85.608  25.730  68.057 1.00 22.17 ? 347 TYR B CD1 1 
ATOM   4440 C  CD2 . TYR B  1 157 ? 87.943  26.175  68.318 1.00 21.44 ? 347 TYR B CD2 1 
ATOM   4441 C  CE1 . TYR B  1 157 ? 85.603  25.035  69.264 1.00 19.65 ? 347 TYR B CE1 1 
ATOM   4442 C  CE2 . TYR B  1 157 ? 87.947  25.484  69.522 1.00 18.14 ? 347 TYR B CE2 1 
ATOM   4443 C  CZ  . TYR B  1 157 ? 86.776  24.919  69.991 1.00 16.90 ? 347 TYR B CZ  1 
ATOM   4444 O  OH  . TYR B  1 157 ? 86.780  24.257  71.195 1.00 19.40 ? 347 TYR B OH  1 
ATOM   4445 N  N   . CYS B  1 158 ? 85.678  30.440  65.078 1.00 26.65 ? 348 CYS B N   1 
ATOM   4446 C  CA  . CYS B  1 158 ? 86.053  31.408  64.053 1.00 25.55 ? 348 CYS B CA  1 
ATOM   4447 C  C   . CYS B  1 158 ? 87.245  32.145  64.646 1.00 25.97 ? 348 CYS B C   1 
ATOM   4448 O  O   . CYS B  1 158 ? 87.222  32.531  65.815 1.00 25.72 ? 348 CYS B O   1 
ATOM   4449 C  CB  . CYS B  1 158 ? 84.906  32.378  63.759 1.00 25.67 ? 348 CYS B CB  1 
ATOM   4450 S  SG  . CYS B  1 158 ? 83.528  31.623  62.831 1.00 32.80 ? 348 CYS B SG  1 
ATOM   4451 N  N   . SER B  1 159 ? 88.292  32.332  63.852 1.00 26.88 ? 349 SER B N   1 
ATOM   4452 C  CA  . SER B  1 159 ? 89.495  32.977  64.356 1.00 26.05 ? 349 SER B CA  1 
ATOM   4453 C  C   . SER B  1 159 ? 90.103  33.999  63.406 1.00 26.73 ? 349 SER B C   1 
ATOM   4454 O  O   . SER B  1 159 ? 89.875  33.969  62.195 1.00 24.37 ? 349 SER B O   1 
ATOM   4455 C  CB  . SER B  1 159 ? 90.536  31.898  64.694 1.00 26.57 ? 349 SER B CB  1 
ATOM   4456 O  OG  . SER B  1 159 ? 91.682  32.437  65.330 1.00 29.85 ? 349 SER B OG  1 
ATOM   4457 N  N   . CYS B  1 160 ? 90.877  34.910  63.985 1.00 23.10 ? 350 CYS B N   1 
ATOM   4458 C  CA  . CYS B  1 160 ? 91.570  35.957  63.250 1.00 24.30 ? 350 CYS B CA  1 
ATOM   4459 C  C   . CYS B  1 160 ? 92.818  36.206  64.090 1.00 26.84 ? 350 CYS B C   1 
ATOM   4460 O  O   . CYS B  1 160 ? 93.334  37.322  64.161 1.00 29.12 ? 350 CYS B O   1 
ATOM   4461 C  CB  . CYS B  1 160 ? 90.709  37.228  63.178 1.00 24.10 ? 350 CYS B CB  1 
ATOM   4462 S  SG  . CYS B  1 160 ? 90.439  38.031  64.794 1.00 33.89 ? 350 CYS B SG  1 
ATOM   4463 N  N   . GLY B  1 161 ? 93.294  35.137  64.724 1.00 26.60 ? 351 GLY B N   1 
ATOM   4464 C  CA  . GLY B  1 161 ? 94.452  35.228  65.592 1.00 27.22 ? 351 GLY B CA  1 
ATOM   4465 C  C   . GLY B  1 161 ? 93.913  35.444  66.992 1.00 34.47 ? 351 GLY B C   1 
ATOM   4466 O  O   . GLY B  1 161 ? 92.702  35.344  67.204 1.00 36.95 ? 351 GLY B O   1 
ATOM   4467 N  N   . ASP B  1 162 ? 94.781  35.741  67.951 1.00 38.52 ? 352 ASP B N   1 
ATOM   4468 C  CA  . ASP B  1 162 ? 94.317  35.969  69.317 1.00 48.03 ? 352 ASP B CA  1 
ATOM   4469 C  C   . ASP B  1 162 ? 93.835  37.411  69.492 1.00 48.44 ? 352 ASP B C   1 
ATOM   4470 O  O   . ASP B  1 162 ? 94.151  38.066  70.488 1.00 51.12 ? 352 ASP B O   1 
ATOM   4471 C  CB  . ASP B  1 162 ? 95.439  35.670  70.319 1.00 54.93 ? 352 ASP B CB  1 
ATOM   4472 C  CG  . ASP B  1 162 ? 96.604  36.641  70.206 1.00 60.10 ? 352 ASP B CG  1 
ATOM   4473 O  OD1 . ASP B  1 162 ? 97.581  36.482  70.970 1.00 60.27 ? 352 ASP B OD1 1 
ATOM   4474 O  OD2 . ASP B  1 162 ? 96.543  37.561  69.359 1.00 61.36 ? 352 ASP B OD2 1 
ATOM   4475 N  N   . TYR B  1 163 ? 93.066  37.899  68.523 1.00 44.30 ? 353 TYR B N   1 
ATOM   4476 C  CA  . TYR B  1 163 ? 92.553  39.266  68.565 1.00 40.06 ? 353 TYR B CA  1 
ATOM   4477 C  C   . TYR B  1 163 ? 91.030  39.301  68.507 1.00 34.25 ? 353 TYR B C   1 
ATOM   4478 O  O   . TYR B  1 163 ? 90.400  38.395  67.965 1.00 34.41 ? 353 TYR B O   1 
ATOM   4479 C  CB  . TYR B  1 163 ? 93.085  40.064  67.376 1.00 42.52 ? 353 TYR B CB  1 
ATOM   4480 C  CG  . TYR B  1 163 ? 94.585  40.066  67.217 1.00 43.26 ? 353 TYR B CG  1 
ATOM   4481 C  CD1 . TYR B  1 163 ? 95.397  40.847  68.038 1.00 44.20 ? 353 TYR B CD1 1 
ATOM   4482 C  CD2 . TYR B  1 163 ? 95.193  39.311  66.215 1.00 45.56 ? 353 TYR B CD2 1 
ATOM   4483 C  CE1 . TYR B  1 163 ? 96.779  40.882  67.859 1.00 45.91 ? 353 TYR B CE1 1 
ATOM   4484 C  CE2 . TYR B  1 163 ? 96.571  39.336  66.027 1.00 44.39 ? 353 TYR B CE2 1 
ATOM   4485 C  CZ  . TYR B  1 163 ? 97.357  40.124  66.850 1.00 45.88 ? 353 TYR B CZ  1 
ATOM   4486 O  OH  . TYR B  1 163 ? 98.716  40.165  66.647 1.00 45.93 ? 353 TYR B OH  1 
ATOM   4487 N  N   . ALA B  1 164 ? 90.442  40.355  69.061 1.00 30.33 ? 354 ALA B N   1 
ATOM   4488 C  CA  . ALA B  1 164 ? 88.994  40.511  69.025 1.00 25.69 ? 354 ALA B CA  1 
ATOM   4489 C  C   . ALA B  1 164 ? 88.663  40.822  67.568 1.00 24.57 ? 354 ALA B C   1 
ATOM   4490 O  O   . ALA B  1 164 ? 88.948  41.916  67.080 1.00 18.77 ? 354 ALA B O   1 
ATOM   4491 C  CB  . ALA B  1 164 ? 88.569  41.657  69.922 1.00 17.79 ? 354 ALA B CB  1 
ATOM   4492 N  N   . CYS B  1 165 ? 88.068  39.855  66.877 1.00 24.13 ? 355 CYS B N   1 
ATOM   4493 C  CA  . CYS B  1 165 ? 87.745  40.020  65.467 1.00 26.79 ? 355 CYS B CA  1 
ATOM   4494 C  C   . CYS B  1 165 ? 86.596  40.985  65.207 1.00 27.61 ? 355 CYS B C   1 
ATOM   4495 O  O   . CYS B  1 165 ? 85.735  41.198  66.060 1.00 29.27 ? 355 CYS B O   1 
ATOM   4496 C  CB  . CYS B  1 165 ? 87.453  38.651  64.843 1.00 28.60 ? 355 CYS B CB  1 
ATOM   4497 S  SG  . CYS B  1 165 ? 88.618  37.367  65.407 1.00 37.00 ? 355 CYS B SG  1 
ATOM   4498 N  N   . ILE B  1 166 ? 86.599  41.563  64.011 1.00 24.70 ? 356 ILE B N   1 
ATOM   4499 C  CA  . ILE B  1 166 ? 85.592  42.531  63.601 1.00 23.55 ? 356 ILE B CA  1 
ATOM   4500 C  C   . ILE B  1 166 ? 84.147  42.063  63.768 1.00 26.06 ? 356 ILE B C   1 
ATOM   4501 O  O   . ILE B  1 166 ? 83.339  42.756  64.387 1.00 29.79 ? 356 ILE B O   1 
ATOM   4502 C  CB  . ILE B  1 166 ? 85.788  42.947  62.121 1.00 19.12 ? 356 ILE B CB  1 
ATOM   4503 C  CG1 . ILE B  1 166 ? 87.218  43.443  61.894 1.00 17.53 ? 356 ILE B CG1 1 
ATOM   4504 C  CG2 . ILE B  1 166 ? 84.795  44.040  61.752 1.00 18.14 ? 356 ILE B CG2 1 
ATOM   4505 C  CD1 . ILE B  1 166 ? 87.568  44.719  62.628 1.00 14.04 ? 356 ILE B CD1 1 
ATOM   4506 N  N   . MET B  1 167 ? 83.818  40.894  63.224 1.00 22.26 ? 357 MET B N   1 
ATOM   4507 C  CA  . MET B  1 167 ? 82.448  40.407  63.306 1.00 21.06 ? 357 MET B CA  1 
ATOM   4508 C  C   . MET B  1 167 ? 82.007  39.696  64.586 1.00 20.82 ? 357 MET B C   1 
ATOM   4509 O  O   . MET B  1 167 ? 81.083  38.884  64.555 1.00 20.09 ? 357 MET B O   1 
ATOM   4510 C  CB  . MET B  1 167 ? 82.124  39.530  62.093 1.00 18.71 ? 357 MET B CB  1 
ATOM   4511 C  CG  . MET B  1 167 ? 82.129  40.289  60.773 1.00 21.98 ? 357 MET B CG  1 
ATOM   4512 S  SD  . MET B  1 167 ? 81.326  41.923  60.854 1.00 20.14 ? 357 MET B SD  1 
ATOM   4513 C  CE  . MET B  1 167 ? 79.581  41.468  60.849 1.00 25.23 ? 357 MET B CE  1 
ATOM   4514 N  N   . ARG B  1 168 ? 82.657  39.990  65.708 1.00 20.69 ? 358 ARG B N   1 
ATOM   4515 C  CA  . ARG B  1 168 ? 82.237  39.392  66.971 1.00 17.14 ? 358 ARG B CA  1 
ATOM   4516 C  C   . ARG B  1 168 ? 80.879  40.031  67.264 1.00 16.32 ? 358 ARG B C   1 
ATOM   4517 O  O   . ARG B  1 168 ? 80.658  41.198  66.944 1.00 12.44 ? 358 ARG B O   1 
ATOM   4518 C  CB  . ARG B  1 168 ? 83.216  39.717  68.105 1.00 14.75 ? 358 ARG B CB  1 
ATOM   4519 C  CG  . ARG B  1 168 ? 84.525  38.935  68.083 1.00 20.32 ? 358 ARG B CG  1 
ATOM   4520 C  CD  . ARG B  1 168 ? 85.018  38.707  69.512 1.00 31.98 ? 358 ARG B CD  1 
ATOM   4521 N  NE  . ARG B  1 168 ? 86.394  38.215  69.610 1.00 38.50 ? 358 ARG B NE  1 
ATOM   4522 C  CZ  . ARG B  1 168 ? 86.847  37.095  69.051 1.00 43.24 ? 358 ARG B CZ  1 
ATOM   4523 N  NH1 . ARG B  1 168 ? 88.114  36.742  69.212 1.00 39.75 ? 358 ARG B NH1 1 
ATOM   4524 N  NH2 . ARG B  1 168 ? 86.044  36.332  68.321 1.00 50.75 ? 358 ARG B NH2 1 
ATOM   4525 N  N   . PRO B  1 169 ? 79.952  39.277  67.875 1.00 21.31 ? 359 PRO B N   1 
ATOM   4526 C  CA  . PRO B  1 169 ? 78.618  39.800  68.191 1.00 22.89 ? 359 PRO B CA  1 
ATOM   4527 C  C   . PRO B  1 169 ? 78.586  41.144  68.923 1.00 23.19 ? 359 PRO B C   1 
ATOM   4528 O  O   . PRO B  1 169 ? 77.579  41.847  68.886 1.00 29.35 ? 359 PRO B O   1 
ATOM   4529 C  CB  . PRO B  1 169 ? 77.984  38.666  68.997 1.00 18.24 ? 359 PRO B CB  1 
ATOM   4530 C  CG  . PRO B  1 169 ? 79.164  37.968  69.603 1.00 25.98 ? 359 PRO B CG  1 
ATOM   4531 C  CD  . PRO B  1 169 ? 80.139  37.939  68.461 1.00 23.74 ? 359 PRO B CD  1 
ATOM   4532 N  N   . GLU B  1 170 ? 79.678  41.502  69.586 1.00 21.13 ? 360 GLU B N   1 
ATOM   4533 C  CA  . GLU B  1 170 ? 79.739  42.779  70.291 1.00 22.25 ? 360 GLU B CA  1 
ATOM   4534 C  C   . GLU B  1 170 ? 81.147  43.366  70.323 1.00 22.66 ? 360 GLU B C   1 
ATOM   4535 O  O   . GLU B  1 170 ? 82.138  42.651  70.500 1.00 22.27 ? 360 GLU B O   1 
ATOM   4536 C  CB  . GLU B  1 170 ? 79.186  42.637  71.713 1.00 22.98 ? 360 GLU B CB  1 
ATOM   4537 C  CG  . GLU B  1 170 ? 79.531  41.339  72.409 1.00 35.59 ? 360 GLU B CG  1 
ATOM   4538 C  CD  . GLU B  1 170 ? 78.291  40.546  72.780 1.00 43.83 ? 360 GLU B CD  1 
ATOM   4539 O  OE1 . GLU B  1 170 ? 77.439  41.081  73.519 1.00 46.49 ? 360 GLU B OE1 1 
ATOM   4540 O  OE2 . GLU B  1 170 ? 78.166  39.388  72.331 1.00 50.30 ? 360 GLU B OE2 1 
ATOM   4541 N  N   . ILE B  1 171 ? 81.225  44.680  70.141 1.00 23.75 ? 361 ILE B N   1 
ATOM   4542 C  CA  . ILE B  1 171 ? 82.500  45.386  70.127 1.00 25.96 ? 361 ILE B CA  1 
ATOM   4543 C  C   . ILE B  1 171 ? 83.295  45.213  71.421 1.00 23.99 ? 361 ILE B C   1 
ATOM   4544 O  O   . ILE B  1 171 ? 82.769  45.405  72.515 1.00 25.45 ? 361 ILE B O   1 
ATOM   4545 C  CB  . ILE B  1 171 ? 82.280  46.888  69.872 1.00 26.01 ? 361 ILE B CB  1 
ATOM   4546 C  CG1 . ILE B  1 171 ? 83.626  47.592  69.710 1.00 25.59 ? 361 ILE B CG1 1 
ATOM   4547 C  CG2 . ILE B  1 171 ? 81.495  47.501  71.021 1.00 32.56 ? 361 ILE B CG2 1 
ATOM   4548 C  CD1 . ILE B  1 171 ? 83.505  49.046  69.358 1.00 27.97 ? 361 ILE B CD1 1 
ATOM   4549 N  N   . SER B  1 172 ? 84.566  44.853  71.292 1.00 24.15 ? 362 SER B N   1 
ATOM   4550 C  CA  . SER B  1 172 ? 85.417  44.663  72.462 1.00 31.47 ? 362 SER B CA  1 
ATOM   4551 C  C   . SER B  1 172 ? 86.092  45.964  72.867 1.00 34.91 ? 362 SER B C   1 
ATOM   4552 O  O   . SER B  1 172 ? 86.150  46.916  72.089 1.00 33.73 ? 362 SER B O   1 
ATOM   4553 C  CB  . SER B  1 172 ? 86.488  43.604  72.184 1.00 31.54 ? 362 SER B CB  1 
ATOM   4554 O  OG  . SER B  1 172 ? 87.363  44.022  71.153 1.00 29.86 ? 362 SER B OG  1 
ATOM   4555 N  N   . PRO B  1 173 ? 86.607  46.026  74.103 1.00 39.52 ? 363 PRO B N   1 
ATOM   4556 C  CA  . PRO B  1 173 ? 87.279  47.234  74.583 1.00 39.66 ? 363 PRO B CA  1 
ATOM   4557 C  C   . PRO B  1 173 ? 88.713  47.255  74.073 1.00 40.96 ? 363 PRO B C   1 
ATOM   4558 O  O   . PRO B  1 173 ? 89.429  48.242  74.232 1.00 44.25 ? 363 PRO B O   1 
ATOM   4559 C  CB  . PRO B  1 173 ? 87.204  47.078  76.095 1.00 40.18 ? 363 PRO B CB  1 
ATOM   4560 C  CG  . PRO B  1 173 ? 87.405  45.601  76.263 1.00 39.82 ? 363 PRO B CG  1 
ATOM   4561 C  CD  . PRO B  1 173 ? 86.513  45.017  75.176 1.00 41.32 ? 363 PRO B CD  1 
ATOM   4562 N  N   . GLU B  1 174 ? 89.114  46.150  73.453 1.00 41.00 ? 364 GLU B N   1 
ATOM   4563 C  CA  . GLU B  1 174 ? 90.459  45.991  72.912 1.00 38.58 ? 364 GLU B CA  1 
ATOM   4564 C  C   . GLU B  1 174 ? 90.327  45.598  71.438 1.00 33.02 ? 364 GLU B C   1 
ATOM   4565 O  O   . GLU B  1 174 ? 90.823  44.553  71.017 1.00 30.85 ? 364 GLU B O   1 
ATOM   4566 C  CB  . GLU B  1 174 ? 91.178  44.891  73.694 1.00 47.42 ? 364 GLU B CB  1 
ATOM   4567 C  CG  . GLU B  1 174 ? 92.669  44.776  73.442 1.00 63.26 ? 364 GLU B CG  1 
ATOM   4568 C  CD  . GLU B  1 174 ? 93.292  43.628  74.220 1.00 69.83 ? 364 GLU B CD  1 
ATOM   4569 O  OE1 . GLU B  1 174 ? 93.105  43.577  75.457 1.00 69.25 ? 364 GLU B OE1 1 
ATOM   4570 O  OE2 . GLU B  1 174 ? 93.969  42.779  73.595 1.00 74.02 ? 364 GLU B OE2 1 
ATOM   4571 N  N   . PRO B  1 175 ? 89.664  46.449  70.635 1.00 29.55 ? 365 PRO B N   1 
ATOM   4572 C  CA  . PRO B  1 175 ? 89.415  46.258  69.199 1.00 24.43 ? 365 PRO B CA  1 
ATOM   4573 C  C   . PRO B  1 175 ? 90.641  45.978  68.338 1.00 21.76 ? 365 PRO B C   1 
ATOM   4574 O  O   . PRO B  1 175 ? 91.722  46.522  68.571 1.00 19.13 ? 365 PRO B O   1 
ATOM   4575 C  CB  . PRO B  1 175 ? 88.740  47.568  68.783 1.00 21.49 ? 365 PRO B CB  1 
ATOM   4576 C  CG  . PRO B  1 175 ? 88.143  48.080  70.047 1.00 27.01 ? 365 PRO B CG  1 
ATOM   4577 C  CD  . PRO B  1 175 ? 89.219  47.790  71.051 1.00 26.67 ? 365 PRO B CD  1 
ATOM   4578 N  N   . SER B  1 176 ? 90.454  45.133  67.331 1.00 16.83 ? 366 SER B N   1 
ATOM   4579 C  CA  . SER B  1 176 ? 91.520  44.796  66.402 1.00 20.20 ? 366 SER B CA  1 
ATOM   4580 C  C   . SER B  1 176 ? 90.989  45.064  65.000 1.00 19.02 ? 366 SER B C   1 
ATOM   4581 O  O   . SER B  1 176 ? 89.783  45.125  64.791 1.00 23.86 ? 366 SER B O   1 
ATOM   4582 C  CB  . SER B  1 176 ? 91.920  43.325  66.525 1.00 17.79 ? 366 SER B CB  1 
ATOM   4583 O  OG  . SER B  1 176 ? 91.077  42.499  65.740 1.00 24.58 ? 366 SER B OG  1 
ATOM   4584 N  N   . THR B  1 177 ? 91.894  45.213  64.043 1.00 21.67 ? 367 THR B N   1 
ATOM   4585 C  CA  . THR B  1 177 ? 91.526  45.492  62.659 1.00 24.11 ? 367 THR B CA  1 
ATOM   4586 C  C   . THR B  1 177 ? 91.319  44.232  61.817 1.00 23.84 ? 367 THR B C   1 
ATOM   4587 O  O   . THR B  1 177 ? 91.090  44.321  60.610 1.00 18.68 ? 367 THR B O   1 
ATOM   4588 C  CB  . THR B  1 177 ? 92.621  46.324  61.982 1.00 24.74 ? 367 THR B CB  1 
ATOM   4589 O  OG1 . THR B  1 177 ? 93.877  45.643  62.125 1.00 27.04 ? 367 THR B OG1 1 
ATOM   4590 C  CG2 . THR B  1 177 ? 92.721  47.707  62.616 1.00 16.04 ? 367 THR B CG2 1 
ATOM   4591 N  N   . PHE B  1 178 ? 91.376  43.064  62.452 1.00 25.69 ? 368 PHE B N   1 
ATOM   4592 C  CA  . PHE B  1 178 ? 91.251  41.804  61.725 1.00 23.21 ? 368 PHE B CA  1 
ATOM   4593 C  C   . PHE B  1 178 ? 89.875  41.163  61.617 1.00 19.87 ? 368 PHE B C   1 
ATOM   4594 O  O   . PHE B  1 178 ? 89.112  41.126  62.577 1.00 20.05 ? 368 PHE B O   1 
ATOM   4595 C  CB  . PHE B  1 178 ? 92.214  40.777  62.319 1.00 26.29 ? 368 PHE B CB  1 
ATOM   4596 C  CG  . PHE B  1 178 ? 93.611  41.287  62.486 1.00 30.54 ? 368 PHE B CG  1 
ATOM   4597 C  CD1 . PHE B  1 178 ? 94.161  41.439  63.754 1.00 32.49 ? 368 PHE B CD1 1 
ATOM   4598 C  CD2 . PHE B  1 178 ? 94.379  41.626  61.375 1.00 36.65 ? 368 PHE B CD2 1 
ATOM   4599 C  CE1 . PHE B  1 178 ? 95.458  41.921  63.918 1.00 34.50 ? 368 PHE B CE1 1 
ATOM   4600 C  CE2 . PHE B  1 178 ? 95.678  42.111  61.525 1.00 36.33 ? 368 PHE B CE2 1 
ATOM   4601 C  CZ  . PHE B  1 178 ? 96.219  42.258  62.801 1.00 37.03 ? 368 PHE B CZ  1 
ATOM   4602 N  N   . PHE B  1 179 ? 89.591  40.648  60.423 1.00 21.34 ? 369 PHE B N   1 
ATOM   4603 C  CA  . PHE B  1 179 ? 88.349  39.943  60.114 1.00 19.49 ? 369 PHE B CA  1 
ATOM   4604 C  C   . PHE B  1 179 ? 88.669  38.464  60.291 1.00 19.93 ? 369 PHE B C   1 
ATOM   4605 O  O   . PHE B  1 179 ? 89.756  38.020  59.922 1.00 25.92 ? 369 PHE B O   1 
ATOM   4606 C  CB  . PHE B  1 179 ? 87.943  40.190  58.658 1.00 20.46 ? 369 PHE B CB  1 
ATOM   4607 C  CG  . PHE B  1 179 ? 86.914  41.268  58.484 1.00 20.38 ? 369 PHE B CG  1 
ATOM   4608 C  CD1 . PHE B  1 179 ? 85.610  41.084  58.941 1.00 15.15 ? 369 PHE B CD1 1 
ATOM   4609 C  CD2 . PHE B  1 179 ? 87.242  42.461  57.850 1.00 14.18 ? 369 PHE B CD2 1 
ATOM   4610 C  CE1 . PHE B  1 179 ? 84.649  42.070  58.768 1.00 17.67 ? 369 PHE B CE1 1 
ATOM   4611 C  CE2 . PHE B  1 179 ? 86.284  43.460  57.671 1.00 18.18 ? 369 PHE B CE2 1 
ATOM   4612 C  CZ  . PHE B  1 179 ? 84.986  43.263  58.131 1.00 18.71 ? 369 PHE B CZ  1 
ATOM   4613 N  N   . SER B  1 180 ? 87.737  37.698  60.848 1.00 20.59 ? 370 SER B N   1 
ATOM   4614 C  CA  . SER B  1 180 ? 87.970  36.269  61.059 1.00 18.86 ? 370 SER B CA  1 
ATOM   4615 C  C   . SER B  1 180 ? 88.030  35.539  59.725 1.00 19.93 ? 370 SER B C   1 
ATOM   4616 O  O   . SER B  1 180 ? 87.696  36.107  58.683 1.00 21.68 ? 370 SER B O   1 
ATOM   4617 C  CB  . SER B  1 180 ? 86.850  35.660  61.903 1.00 19.50 ? 370 SER B CB  1 
ATOM   4618 O  OG  . SER B  1 180 ? 85.679  35.473  61.127 1.00 13.47 ? 370 SER B OG  1 
ATOM   4619 N  N   . ASN B  1 181 ? 88.459  34.281  59.753 1.00 21.22 ? 371 ASN B N   1 
ATOM   4620 C  CA  . ASN B  1 181 ? 88.521  33.494  58.531 1.00 20.43 ? 371 ASN B CA  1 
ATOM   4621 C  C   . ASN B  1 181 ? 87.090  33.217  58.072 1.00 24.50 ? 371 ASN B C   1 
ATOM   4622 O  O   . ASN B  1 181 ? 86.817  33.134  56.873 1.00 25.54 ? 371 ASN B O   1 
ATOM   4623 C  CB  . ASN B  1 181 ? 89.302  32.194  58.766 1.00 22.45 ? 371 ASN B CB  1 
ATOM   4624 C  CG  . ASN B  1 181 ? 88.722  31.343  59.876 1.00 22.57 ? 371 ASN B CG  1 
ATOM   4625 O  OD1 . ASN B  1 181 ? 88.183  31.856  60.857 1.00 19.27 ? 371 ASN B OD1 1 
ATOM   4626 N  ND2 . ASN B  1 181 ? 88.864  30.029  59.735 1.00 31.02 ? 371 ASN B ND2 1 
ATOM   4627 N  N   . CYS B  1 182 ? 86.173  33.107  59.033 1.00 26.20 ? 372 CYS B N   1 
ATOM   4628 C  CA  . CYS B  1 182 ? 84.763  32.875  58.729 1.00 27.01 ? 372 CYS B CA  1 
ATOM   4629 C  C   . CYS B  1 182 ? 84.211  34.054  57.924 1.00 26.23 ? 372 CYS B C   1 
ATOM   4630 O  O   . CYS B  1 182 ? 83.649  33.868  56.844 1.00 28.45 ? 372 CYS B O   1 
ATOM   4631 C  CB  . CYS B  1 182 ? 83.946  32.718  60.018 1.00 26.82 ? 372 CYS B CB  1 
ATOM   4632 S  SG  . CYS B  1 182 ? 84.315  31.225  60.994 1.00 28.80 ? 372 CYS B SG  1 
ATOM   4633 N  N   . SER B  1 183 ? 84.375  35.262  58.462 1.00 19.16 ? 373 SER B N   1 
ATOM   4634 C  CA  . SER B  1 183 ? 83.907  36.475  57.799 1.00 17.70 ? 373 SER B CA  1 
ATOM   4635 C  C   . SER B  1 183 ? 84.351  36.516  56.340 1.00 18.51 ? 373 SER B C   1 
ATOM   4636 O  O   . SER B  1 183 ? 83.557  36.816  55.449 1.00 17.59 ? 373 SER B O   1 
ATOM   4637 C  CB  . SER B  1 183 ? 84.439  37.713  58.521 1.00 18.08 ? 373 SER B CB  1 
ATOM   4638 O  OG  . SER B  1 183 ? 83.974  37.772  59.857 1.00 21.80 ? 373 SER B OG  1 
ATOM   4639 N  N   . TYR B  1 184 ? 85.623  36.211  56.105 1.00 17.16 ? 374 TYR B N   1 
ATOM   4640 C  CA  . TYR B  1 184 ? 86.186  36.208  54.759 1.00 23.91 ? 374 TYR B CA  1 
ATOM   4641 C  C   . TYR B  1 184 ? 85.391  35.324  53.798 1.00 26.36 ? 374 TYR B C   1 
ATOM   4642 O  O   . TYR B  1 184 ? 84.863  35.796  52.788 1.00 26.41 ? 374 TYR B O   1 
ATOM   4643 C  CB  . TYR B  1 184 ? 87.631  35.714  54.804 1.00 26.28 ? 374 TYR B CB  1 
ATOM   4644 C  CG  . TYR B  1 184 ? 88.331  35.749  53.467 1.00 28.34 ? 374 TYR B CG  1 
ATOM   4645 C  CD1 . TYR B  1 184 ? 88.873  36.936  52.975 1.00 36.66 ? 374 TYR B CD1 1 
ATOM   4646 C  CD2 . TYR B  1 184 ? 88.449  34.598  52.689 1.00 29.41 ? 374 TYR B CD2 1 
ATOM   4647 C  CE1 . TYR B  1 184 ? 89.519  36.978  51.739 1.00 34.69 ? 374 TYR B CE1 1 
ATOM   4648 C  CE2 . TYR B  1 184 ? 89.092  34.629  51.450 1.00 31.84 ? 374 TYR B CE2 1 
ATOM   4649 C  CZ  . TYR B  1 184 ? 89.625  35.822  50.985 1.00 32.97 ? 374 TYR B CZ  1 
ATOM   4650 O  OH  . TYR B  1 184 ? 90.262  35.865  49.767 1.00 34.82 ? 374 TYR B OH  1 
ATOM   4651 N  N   . PHE B  1 185 ? 85.321  34.036  54.117 1.00 27.11 ? 375 PHE B N   1 
ATOM   4652 C  CA  . PHE B  1 185 ? 84.605  33.068  53.290 1.00 28.83 ? 375 PHE B CA  1 
ATOM   4653 C  C   . PHE B  1 185 ? 83.147  33.451  53.028 1.00 27.65 ? 375 PHE B C   1 
ATOM   4654 O  O   . PHE B  1 185 ? 82.669  33.351  51.895 1.00 27.40 ? 375 PHE B O   1 
ATOM   4655 C  CB  . PHE B  1 185 ? 84.685  31.683  53.942 1.00 28.89 ? 375 PHE B CB  1 
ATOM   4656 C  CG  . PHE B  1 185 ? 86.076  31.103  53.965 1.00 30.28 ? 375 PHE B CG  1 
ATOM   4657 C  CD1 . PHE B  1 185 ? 86.517  30.355  55.052 1.00 32.94 ? 375 PHE B CD1 1 
ATOM   4658 C  CD2 . PHE B  1 185 ? 86.943  31.293  52.890 1.00 30.45 ? 375 PHE B CD2 1 
ATOM   4659 C  CE1 . PHE B  1 185 ? 87.801  29.805  55.068 1.00 32.28 ? 375 PHE B CE1 1 
ATOM   4660 C  CE2 . PHE B  1 185 ? 88.226  30.746  52.897 1.00 28.53 ? 375 PHE B CE2 1 
ATOM   4661 C  CZ  . PHE B  1 185 ? 88.655  30.003  53.988 1.00 27.62 ? 375 PHE B CZ  1 
ATOM   4662 N  N   . GLU B  1 186 ? 82.438  33.881  54.067 1.00 25.47 ? 376 GLU B N   1 
ATOM   4663 C  CA  . GLU B  1 186 ? 81.047  34.282  53.905 1.00 27.33 ? 376 GLU B CA  1 
ATOM   4664 C  C   . GLU B  1 186 ? 80.967  35.510  53.017 1.00 25.55 ? 376 GLU B C   1 
ATOM   4665 O  O   . GLU B  1 186 ? 80.072  35.628  52.181 1.00 26.88 ? 376 GLU B O   1 
ATOM   4666 C  CB  . GLU B  1 186 ? 80.405  34.590  55.257 1.00 32.07 ? 376 GLU B CB  1 
ATOM   4667 C  CG  . GLU B  1 186 ? 79.913  33.364  55.992 1.00 43.92 ? 376 GLU B CG  1 
ATOM   4668 C  CD  . GLU B  1 186 ? 79.010  33.715  57.153 1.00 51.24 ? 376 GLU B CD  1 
ATOM   4669 O  OE1 . GLU B  1 186 ? 78.403  32.791  57.738 1.00 53.97 ? 376 GLU B OE1 1 
ATOM   4670 O  OE2 . GLU B  1 186 ? 78.913  34.917  57.479 1.00 53.21 ? 376 GLU B OE2 1 
ATOM   4671 N  N   . CYS B  1 187 ? 81.911  36.425  53.209 1.00 23.29 ? 377 CYS B N   1 
ATOM   4672 C  CA  . CYS B  1 187 ? 81.960  37.647  52.423 1.00 25.30 ? 377 CYS B CA  1 
ATOM   4673 C  C   . CYS B  1 187 ? 82.022  37.319  50.936 1.00 25.04 ? 377 CYS B C   1 
ATOM   4674 O  O   . CYS B  1 187 ? 81.273  37.878  50.131 1.00 22.40 ? 377 CYS B O   1 
ATOM   4675 C  CB  . CYS B  1 187 ? 83.184  38.474  52.815 1.00 28.27 ? 377 CYS B CB  1 
ATOM   4676 S  SG  . CYS B  1 187 ? 83.397  39.979  51.842 1.00 34.54 ? 377 CYS B SG  1 
ATOM   4677 N  N   . TRP B  1 188 ? 82.916  36.407  50.571 1.00 24.54 ? 378 TRP B N   1 
ATOM   4678 C  CA  . TRP B  1 188 ? 83.050  36.029  49.175 1.00 26.92 ? 378 TRP B CA  1 
ATOM   4679 C  C   . TRP B  1 188 ? 81.961  35.075  48.718 1.00 28.88 ? 378 TRP B C   1 
ATOM   4680 O  O   . TRP B  1 188 ? 81.656  34.998  47.529 1.00 28.88 ? 378 TRP B O   1 
ATOM   4681 C  CB  . TRP B  1 188 ? 84.436  35.444  48.917 1.00 25.17 ? 378 TRP B CB  1 
ATOM   4682 C  CG  . TRP B  1 188 ? 85.477  36.508  48.958 1.00 29.75 ? 378 TRP B CG  1 
ATOM   4683 C  CD1 . TRP B  1 188 ? 86.314  36.803  49.995 1.00 29.22 ? 378 TRP B CD1 1 
ATOM   4684 C  CD2 . TRP B  1 188 ? 85.725  37.493  47.949 1.00 31.09 ? 378 TRP B CD2 1 
ATOM   4685 N  NE1 . TRP B  1 188 ? 87.065  37.914  49.696 1.00 29.98 ? 378 TRP B NE1 1 
ATOM   4686 C  CE2 . TRP B  1 188 ? 86.723  38.358  48.445 1.00 30.86 ? 378 TRP B CE2 1 
ATOM   4687 C  CE3 . TRP B  1 188 ? 85.198  37.730  46.672 1.00 34.62 ? 378 TRP B CE3 1 
ATOM   4688 C  CZ2 . TRP B  1 188 ? 87.207  39.443  47.709 1.00 33.19 ? 378 TRP B CZ2 1 
ATOM   4689 C  CZ3 . TRP B  1 188 ? 85.679  38.810  45.940 1.00 33.27 ? 378 TRP B CZ3 1 
ATOM   4690 C  CH2 . TRP B  1 188 ? 86.674  39.652  46.462 1.00 32.73 ? 378 TRP B CH2 1 
ATOM   4691 N  N   . ASP B  1 189 ? 81.366  34.350  49.658 1.00 29.48 ? 379 ASP B N   1 
ATOM   4692 C  CA  . ASP B  1 189 ? 80.293  33.445  49.295 1.00 31.60 ? 379 ASP B CA  1 
ATOM   4693 C  C   . ASP B  1 189 ? 79.147  34.325  48.828 1.00 28.81 ? 379 ASP B C   1 
ATOM   4694 O  O   . ASP B  1 189 ? 78.362  33.946  47.960 1.00 31.20 ? 379 ASP B O   1 
ATOM   4695 C  CB  . ASP B  1 189 ? 79.851  32.610  50.494 1.00 38.97 ? 379 ASP B CB  1 
ATOM   4696 C  CG  . ASP B  1 189 ? 78.659  31.732  50.174 1.00 44.78 ? 379 ASP B CG  1 
ATOM   4697 O  OD1 . ASP B  1 189 ? 78.740  30.954  49.201 1.00 50.69 ? 379 ASP B OD1 1 
ATOM   4698 O  OD2 . ASP B  1 189 ? 77.640  31.821  50.892 1.00 50.42 ? 379 ASP B OD2 1 
ATOM   4699 N  N   . PHE B  1 190 ? 79.063  35.514  49.413 1.00 27.53 ? 380 PHE B N   1 
ATOM   4700 C  CA  . PHE B  1 190 ? 78.022  36.465  49.053 1.00 25.77 ? 380 PHE B CA  1 
ATOM   4701 C  C   . PHE B  1 190 ? 78.327  37.083  47.690 1.00 28.83 ? 380 PHE B C   1 
ATOM   4702 O  O   . PHE B  1 190 ? 77.459  37.157  46.820 1.00 25.31 ? 380 PHE B O   1 
ATOM   4703 C  CB  . PHE B  1 190 ? 77.929  37.571  50.100 1.00 20.38 ? 380 PHE B CB  1 
ATOM   4704 C  CG  . PHE B  1 190 ? 76.936  38.636  49.755 1.00 17.46 ? 380 PHE B CG  1 
ATOM   4705 C  CD1 . PHE B  1 190 ? 75.573  38.402  49.890 1.00 14.48 ? 380 PHE B CD1 1 
ATOM   4706 C  CD2 . PHE B  1 190 ? 77.363  39.864  49.254 1.00 15.72 ? 380 PHE B CD2 1 
ATOM   4707 C  CE1 . PHE B  1 190 ? 74.643  39.376  49.529 1.00 17.27 ? 380 PHE B CE1 1 
ATOM   4708 C  CE2 . PHE B  1 190 ? 76.444  40.845  48.890 1.00 14.15 ? 380 PHE B CE2 1 
ATOM   4709 C  CZ  . PHE B  1 190 ? 75.080  40.600  49.028 1.00 20.63 ? 380 PHE B CZ  1 
ATOM   4710 N  N   . ILE B  1 191 ? 79.569  37.525  47.516 1.00 30.62 ? 381 ILE B N   1 
ATOM   4711 C  CA  . ILE B  1 191 ? 80.003  38.140  46.270 1.00 33.24 ? 381 ILE B CA  1 
ATOM   4712 C  C   . ILE B  1 191 ? 79.875  37.206  45.069 1.00 34.70 ? 381 ILE B C   1 
ATOM   4713 O  O   . ILE B  1 191 ? 79.402  37.617  44.009 1.00 37.28 ? 381 ILE B O   1 
ATOM   4714 C  CB  . ILE B  1 191 ? 81.465  38.624  46.378 1.00 34.96 ? 381 ILE B CB  1 
ATOM   4715 C  CG1 . ILE B  1 191 ? 81.556  39.745  47.416 1.00 34.05 ? 381 ILE B CG1 1 
ATOM   4716 C  CG2 . ILE B  1 191 ? 81.965  39.105  45.024 1.00 36.81 ? 381 ILE B CG2 1 
ATOM   4717 C  CD1 . ILE B  1 191 ? 82.956  40.282  47.626 1.00 27.22 ? 381 ILE B CD1 1 
ATOM   4718 N  N   . MET B  1 192 ? 80.292  35.953  45.232 1.00 35.93 ? 382 MET B N   1 
ATOM   4719 C  CA  . MET B  1 192 ? 80.219  34.981  44.144 1.00 36.39 ? 382 MET B CA  1 
ATOM   4720 C  C   . MET B  1 192 ? 78.786  34.559  43.807 1.00 35.73 ? 382 MET B C   1 
ATOM   4721 O  O   . MET B  1 192 ? 78.370  34.662  42.653 1.00 32.52 ? 382 MET B O   1 
ATOM   4722 C  CB  . MET B  1 192 ? 81.057  33.744  44.480 1.00 42.62 ? 382 MET B CB  1 
ATOM   4723 C  CG  . MET B  1 192 ? 82.539  34.034  44.717 1.00 50.96 ? 382 MET B CG  1 
ATOM   4724 S  SD  . MET B  1 192 ? 83.383  34.769  43.291 1.00 58.20 ? 382 MET B SD  1 
ATOM   4725 C  CE  . MET B  1 192 ? 84.041  33.298  42.483 1.00 52.21 ? 382 MET B CE  1 
ATOM   4726 N  N   . ASN B  1 193 ? 78.036  34.085  44.800 1.00 34.27 ? 383 ASN B N   1 
ATOM   4727 C  CA  . ASN B  1 193 ? 76.652  33.661  44.572 1.00 37.01 ? 383 ASN B CA  1 
ATOM   4728 C  C   . ASN B  1 193 ? 75.803  34.838  44.119 1.00 36.98 ? 383 ASN B C   1 
ATOM   4729 O  O   . ASN B  1 193 ? 75.392  34.906  42.963 1.00 39.62 ? 383 ASN B O   1 
ATOM   4730 C  CB  . ASN B  1 193 ? 76.055  33.052  45.840 1.00 41.92 ? 383 ASN B CB  1 
ATOM   4731 C  CG  . ASN B  1 193 ? 76.553  31.645  46.097 1.00 48.03 ? 383 ASN B CG  1 
ATOM   4732 O  OD1 . ASN B  1 193 ? 77.756  31.409  46.215 1.00 50.28 ? 383 ASN B OD1 1 
ATOM   4733 N  ND2 . ASN B  1 193 ? 75.624  30.698  46.183 1.00 53.07 ? 383 ASN B ND2 1 
ATOM   4734 N  N   . HIS B  1 194 ? 75.522  35.760  45.032 1.00 40.82 ? 384 HIS B N   1 
ATOM   4735 C  CA  . HIS B  1 194 ? 74.755  36.944  44.670 1.00 43.07 ? 384 HIS B CA  1 
ATOM   4736 C  C   . HIS B  1 194 ? 75.746  37.769  43.861 1.00 43.15 ? 384 HIS B C   1 
ATOM   4737 O  O   . HIS B  1 194 ? 76.891  37.355  43.688 1.00 45.39 ? 384 HIS B O   1 
ATOM   4738 C  CB  . HIS B  1 194 ? 74.315  37.703  45.921 1.00 45.35 ? 384 HIS B CB  1 
ATOM   4739 C  CG  . HIS B  1 194 ? 73.453  36.896  46.840 1.00 49.97 ? 384 HIS B CG  1 
ATOM   4740 N  ND1 . HIS B  1 194 ? 73.887  35.729  47.432 1.00 50.83 ? 384 HIS B ND1 1 
ATOM   4741 C  CD2 . HIS B  1 194 ? 72.181  37.082  47.265 1.00 52.45 ? 384 HIS B CD2 1 
ATOM   4742 C  CE1 . HIS B  1 194 ? 72.919  35.231  48.182 1.00 51.00 ? 384 HIS B CE1 1 
ATOM   4743 N  NE2 . HIS B  1 194 ? 71.873  36.034  48.098 1.00 51.47 ? 384 HIS B NE2 1 
ATOM   4744 N  N   . ASN B  1 195 ? 75.342  38.927  43.362 1.00 41.44 ? 385 ASN B N   1 
ATOM   4745 C  CA  . ASN B  1 195 ? 76.290  39.697  42.578 1.00 44.20 ? 385 ASN B CA  1 
ATOM   4746 C  C   . ASN B  1 195 ? 76.279  41.185  42.894 1.00 46.53 ? 385 ASN B C   1 
ATOM   4747 O  O   . ASN B  1 195 ? 75.439  41.933  42.391 1.00 49.02 ? 385 ASN B O   1 
ATOM   4748 C  CB  . ASN B  1 195 ? 76.025  39.477  41.087 1.00 49.48 ? 385 ASN B CB  1 
ATOM   4749 C  CG  . ASN B  1 195 ? 77.272  39.657  40.237 1.00 51.20 ? 385 ASN B CG  1 
ATOM   4750 O  OD1 . ASN B  1 195 ? 77.202  39.646  39.006 1.00 52.87 ? 385 ASN B OD1 1 
ATOM   4751 N  ND2 . ASN B  1 195 ? 78.420  39.813  40.889 1.00 47.07 ? 385 ASN B ND2 1 
ATOM   4752 N  N   . PRO B  1 196 ? 77.207  41.631  43.756 1.00 45.62 ? 386 PRO B N   1 
ATOM   4753 C  CA  . PRO B  1 196 ? 77.301  43.044  44.134 1.00 43.46 ? 386 PRO B CA  1 
ATOM   4754 C  C   . PRO B  1 196 ? 77.856  43.853  42.959 1.00 41.07 ? 386 PRO B C   1 
ATOM   4755 O  O   . PRO B  1 196 ? 78.815  44.607  43.100 1.00 42.48 ? 386 PRO B O   1 
ATOM   4756 C  CB  . PRO B  1 196 ? 78.258  43.018  45.324 1.00 45.66 ? 386 PRO B CB  1 
ATOM   4757 C  CG  . PRO B  1 196 ? 78.061  41.646  45.897 1.00 44.39 ? 386 PRO B CG  1 
ATOM   4758 C  CD  . PRO B  1 196 ? 78.022  40.800  44.657 1.00 45.17 ? 386 PRO B CD  1 
ATOM   4759 N  N   . GLU B  1 197 ? 77.233  43.670  41.800 1.00 39.04 ? 387 GLU B N   1 
ATOM   4760 C  CA  . GLU B  1 197 ? 77.608  44.333  40.558 1.00 37.62 ? 387 GLU B CA  1 
ATOM   4761 C  C   . GLU B  1 197 ? 78.241  45.717  40.741 1.00 34.28 ? 387 GLU B C   1 
ATOM   4762 O  O   . GLU B  1 197 ? 79.305  46.001  40.191 1.00 31.61 ? 387 GLU B O   1 
ATOM   4763 C  CB  . GLU B  1 197 ? 76.366  44.454  39.667 1.00 43.55 ? 387 GLU B CB  1 
ATOM   4764 C  CG  . GLU B  1 197 ? 76.638  44.773  38.197 1.00 54.96 ? 387 GLU B CG  1 
ATOM   4765 C  CD  . GLU B  1 197 ? 76.972  43.538  37.368 1.00 59.48 ? 387 GLU B CD  1 
ATOM   4766 O  OE1 . GLU B  1 197 ? 76.129  42.616  37.295 1.00 54.64 ? 387 GLU B OE1 1 
ATOM   4767 O  OE2 . GLU B  1 197 ? 78.078  43.492  36.785 1.00 62.50 ? 387 GLU B OE2 1 
ATOM   4768 N  N   . CYS B  1 198 ? 77.588  46.564  41.530 1.00 29.68 ? 388 CYS B N   1 
ATOM   4769 C  CA  . CYS B  1 198 ? 78.045  47.932  41.755 1.00 23.71 ? 388 CYS B CA  1 
ATOM   4770 C  C   . CYS B  1 198 ? 79.373  48.125  42.486 1.00 23.63 ? 388 CYS B C   1 
ATOM   4771 O  O   . CYS B  1 198 ? 79.853  49.254  42.597 1.00 22.37 ? 388 CYS B O   1 
ATOM   4772 C  CB  . CYS B  1 198 ? 76.959  48.717  42.489 1.00 26.82 ? 388 CYS B CB  1 
ATOM   4773 S  SG  . CYS B  1 198 ? 77.088  48.664  44.304 1.00 40.04 ? 388 CYS B SG  1 
ATOM   4774 N  N   . ILE B  1 199 ? 79.978  47.050  42.980 1.00 25.16 ? 389 ILE B N   1 
ATOM   4775 C  CA  . ILE B  1 199 ? 81.248  47.192  43.690 1.00 22.69 ? 389 ILE B CA  1 
ATOM   4776 C  C   . ILE B  1 199 ? 82.464  46.745  42.880 1.00 24.56 ? 389 ILE B C   1 
ATOM   4777 O  O   . ILE B  1 199 ? 83.550  46.546  43.435 1.00 25.59 ? 389 ILE B O   1 
ATOM   4778 C  CB  . ILE B  1 199 ? 81.238  46.422  45.033 1.00 23.00 ? 389 ILE B CB  1 
ATOM   4779 C  CG1 . ILE B  1 199 ? 81.125  44.916  44.783 1.00 16.42 ? 389 ILE B CG1 1 
ATOM   4780 C  CG2 . ILE B  1 199 ? 80.081  46.913  45.897 1.00 25.08 ? 389 ILE B CG2 1 
ATOM   4781 C  CD1 . ILE B  1 199 ? 81.301  44.074  46.035 1.00 9.31  ? 389 ILE B CD1 1 
ATOM   4782 N  N   . LEU B  1 200 ? 82.288  46.604  41.569 1.00 22.45 ? 390 LEU B N   1 
ATOM   4783 C  CA  . LEU B  1 200 ? 83.382  46.181  40.700 1.00 18.90 ? 390 LEU B CA  1 
ATOM   4784 C  C   . LEU B  1 200 ? 84.302  47.320  40.270 1.00 17.52 ? 390 LEU B C   1 
ATOM   4785 O  O   . LEU B  1 200 ? 85.522  47.181  40.310 1.00 22.66 ? 390 LEU B O   1 
ATOM   4786 C  CB  . LEU B  1 200 ? 82.827  45.483  39.456 1.00 15.81 ? 390 LEU B CB  1 
ATOM   4787 C  CG  . LEU B  1 200 ? 82.156  44.129  39.699 1.00 21.39 ? 390 LEU B CG  1 
ATOM   4788 C  CD1 . LEU B  1 200 ? 81.435  43.653  38.444 1.00 17.40 ? 390 LEU B CD1 1 
ATOM   4789 C  CD2 . LEU B  1 200 ? 83.209  43.128  40.127 1.00 19.04 ? 390 LEU B CD2 1 
ATOM   4790 N  N   . ASN B  1 201 ? 83.717  48.445  39.869 1.00 14.37 ? 391 ASN B N   1 
ATOM   4791 C  CA  . ASN B  1 201 ? 84.488  49.594  39.399 1.00 16.65 ? 391 ASN B CA  1 
ATOM   4792 C  C   . ASN B  1 201 ? 85.451  50.229  40.398 1.00 18.71 ? 391 ASN B C   1 
ATOM   4793 O  O   . ASN B  1 201 ? 85.113  50.446  41.560 1.00 19.01 ? 391 ASN B O   1 
ATOM   4794 C  CB  . ASN B  1 201 ? 83.550  50.685  38.883 1.00 17.21 ? 391 ASN B CB  1 
ATOM   4795 C  CG  . ASN B  1 201 ? 82.655  51.246  39.971 1.00 24.96 ? 391 ASN B CG  1 
ATOM   4796 O  OD1 . ASN B  1 201 ? 82.065  52.314  39.812 1.00 27.27 ? 391 ASN B OD1 1 
ATOM   4797 N  ND2 . ASN B  1 201 ? 82.538  50.522  41.079 1.00 32.71 ? 391 ASN B ND2 1 
ATOM   4798 N  N   . GLU B  1 202 ? 86.655  50.529  39.922 1.00 23.05 ? 392 GLU B N   1 
ATOM   4799 C  CA  . GLU B  1 202 ? 87.677  51.178  40.730 1.00 26.02 ? 392 GLU B CA  1 
ATOM   4800 C  C   . GLU B  1 202 ? 87.336  52.662  40.699 1.00 26.25 ? 392 GLU B C   1 
ATOM   4801 O  O   . GLU B  1 202 ? 87.310  53.273  39.631 1.00 29.98 ? 392 GLU B O   1 
ATOM   4802 C  CB  . GLU B  1 202 ? 89.059  50.957  40.114 1.00 29.46 ? 392 GLU B CB  1 
ATOM   4803 C  CG  . GLU B  1 202 ? 90.189  51.685  40.823 1.00 37.47 ? 392 GLU B CG  1 
ATOM   4804 C  CD  . GLU B  1 202 ? 91.504  51.580  40.073 1.00 46.42 ? 392 GLU B CD  1 
ATOM   4805 O  OE1 . GLU B  1 202 ? 92.521  52.111  40.571 1.00 48.55 ? 392 GLU B OE1 1 
ATOM   4806 O  OE2 . GLU B  1 202 ? 91.520  50.966  38.983 1.00 47.99 ? 392 GLU B OE2 1 
ATOM   4807 N  N   . PRO B  1 203 ? 87.078  53.266  41.869 1.00 25.40 ? 393 PRO B N   1 
ATOM   4808 C  CA  . PRO B  1 203 ? 86.733  54.690  41.925 1.00 22.63 ? 393 PRO B CA  1 
ATOM   4809 C  C   . PRO B  1 203 ? 87.745  55.640  41.291 1.00 22.34 ? 393 PRO B C   1 
ATOM   4810 O  O   . PRO B  1 203 ? 88.952  55.511  41.490 1.00 23.06 ? 393 PRO B O   1 
ATOM   4811 C  CB  . PRO B  1 203 ? 86.553  54.943  43.421 1.00 19.40 ? 393 PRO B CB  1 
ATOM   4812 C  CG  . PRO B  1 203 ? 87.504  53.956  44.045 1.00 20.41 ? 393 PRO B CG  1 
ATOM   4813 C  CD  . PRO B  1 203 ? 87.257  52.714  43.225 1.00 22.58 ? 393 PRO B CD  1 
ATOM   4814 N  N   . LEU B  1 204 ? 87.238  56.591  40.513 1.00 26.32 ? 394 LEU B N   1 
ATOM   4815 C  CA  . LEU B  1 204 ? 88.089  57.585  39.872 1.00 26.94 ? 394 LEU B CA  1 
ATOM   4816 C  C   . LEU B  1 204 ? 88.701  58.452  40.963 1.00 24.45 ? 394 LEU B C   1 
ATOM   4817 O  O   . LEU B  1 204 ? 88.029  58.797  41.940 1.00 20.31 ? 394 LEU B O   1 
ATOM   4818 C  CB  . LEU B  1 204 ? 87.269  58.473  38.930 1.00 27.49 ? 394 LEU B CB  1 
ATOM   4819 C  CG  . LEU B  1 204 ? 86.731  57.864  37.635 1.00 28.19 ? 394 LEU B CG  1 
ATOM   4820 C  CD1 . LEU B  1 204 ? 85.768  58.844  36.975 1.00 23.01 ? 394 LEU B CD1 1 
ATOM   4821 C  CD2 . LEU B  1 204 ? 87.887  57.530  36.705 1.00 23.12 ? 394 LEU B CD2 1 
ATOM   4822 N  N   . GLY B  1 205 ? 89.970  58.806  40.791 1.00 25.85 ? 395 GLY B N   1 
ATOM   4823 C  CA  . GLY B  1 205 ? 90.646  59.636  41.772 1.00 24.34 ? 395 GLY B CA  1 
ATOM   4824 C  C   . GLY B  1 205 ? 89.823  60.851  42.152 1.00 25.17 ? 395 GLY B C   1 
ATOM   4825 O  O   . GLY B  1 205 ? 89.809  61.263  43.313 1.00 23.82 ? 395 GLY B O   1 
ATOM   4826 N  N   . THR B  1 206 ? 89.121  61.415  41.174 1.00 22.96 ? 396 THR B N   1 
ATOM   4827 C  CA  . THR B  1 206 ? 88.296  62.592  41.404 1.00 24.50 ? 396 THR B CA  1 
ATOM   4828 C  C   . THR B  1 206 ? 87.001  62.321  42.170 1.00 26.05 ? 396 THR B C   1 
ATOM   4829 O  O   . THR B  1 206 ? 86.382  63.251  42.691 1.00 25.32 ? 396 THR B O   1 
ATOM   4830 C  CB  . THR B  1 206 ? 87.944  63.287  40.074 1.00 25.55 ? 396 THR B CB  1 
ATOM   4831 O  OG1 . THR B  1 206 ? 87.469  62.314  39.138 1.00 28.78 ? 396 THR B OG1 1 
ATOM   4832 C  CG2 . THR B  1 206 ? 89.162  63.992  39.503 1.00 25.92 ? 396 THR B CG2 1 
ATOM   4833 N  N   . ASP B  1 207 ? 86.582  61.060  42.238 1.00 28.14 ? 397 ASP B N   1 
ATOM   4834 C  CA  . ASP B  1 207 ? 85.356  60.722  42.958 1.00 28.50 ? 397 ASP B CA  1 
ATOM   4835 C  C   . ASP B  1 207 ? 85.592  60.727  44.464 1.00 27.43 ? 397 ASP B C   1 
ATOM   4836 O  O   . ASP B  1 207 ? 84.691  61.054  45.244 1.00 27.13 ? 397 ASP B O   1 
ATOM   4837 C  CB  . ASP B  1 207 ? 84.830  59.345  42.535 1.00 39.00 ? 397 ASP B CB  1 
ATOM   4838 C  CG  . ASP B  1 207 ? 84.226  59.348  41.140 1.00 44.12 ? 397 ASP B CG  1 
ATOM   4839 O  OD1 . ASP B  1 207 ? 83.424  60.259  40.841 1.00 41.51 ? 397 ASP B OD1 1 
ATOM   4840 O  OD2 . ASP B  1 207 ? 84.541  58.430  40.350 1.00 44.15 ? 397 ASP B OD2 1 
ATOM   4841 N  N   . ILE B  1 208 ? 86.808  60.365  44.865 1.00 22.75 ? 398 ILE B N   1 
ATOM   4842 C  CA  . ILE B  1 208 ? 87.181  60.316  46.274 1.00 19.92 ? 398 ILE B CA  1 
ATOM   4843 C  C   . ILE B  1 208 ? 87.221  61.731  46.844 1.00 20.75 ? 398 ILE B C   1 
ATOM   4844 O  O   . ILE B  1 208 ? 88.030  62.555  46.417 1.00 17.12 ? 398 ILE B O   1 
ATOM   4845 C  CB  . ILE B  1 208 ? 88.554  59.648  46.442 1.00 19.94 ? 398 ILE B CB  1 
ATOM   4846 C  CG1 . ILE B  1 208 ? 88.556  58.303  45.710 1.00 18.65 ? 398 ILE B CG1 1 
ATOM   4847 C  CG2 . ILE B  1 208 ? 88.857  59.442  47.915 1.00 18.65 ? 398 ILE B CG2 1 
ATOM   4848 C  CD1 . ILE B  1 208 ? 89.907  57.637  45.640 1.00 20.70 ? 398 ILE B CD1 1 
ATOM   4849 N  N   . ILE B  1 209 ? 86.342  62.002  47.808 1.00 21.23 ? 399 ILE B N   1 
ATOM   4850 C  CA  . ILE B  1 209 ? 86.239  63.325  48.426 1.00 20.25 ? 399 ILE B CA  1 
ATOM   4851 C  C   . ILE B  1 209 ? 87.228  63.567  49.551 1.00 21.71 ? 399 ILE B C   1 
ATOM   4852 O  O   . ILE B  1 209 ? 87.426  64.706  49.978 1.00 24.00 ? 399 ILE B O   1 
ATOM   4853 C  CB  . ILE B  1 209 ? 84.833  63.566  49.006 1.00 19.58 ? 399 ILE B CB  1 
ATOM   4854 C  CG1 . ILE B  1 209 ? 84.593  62.618  50.185 1.00 20.03 ? 399 ILE B CG1 1 
ATOM   4855 C  CG2 . ILE B  1 209 ? 83.784  63.354  47.925 1.00 26.36 ? 399 ILE B CG2 1 
ATOM   4856 C  CD1 . ILE B  1 209 ? 83.339  62.907  50.966 1.00 14.45 ? 399 ILE B CD1 1 
ATOM   4857 N  N   . SER B  1 210 ? 87.839  62.498  50.045 1.00 20.41 ? 400 SER B N   1 
ATOM   4858 C  CA  . SER B  1 210 ? 88.793  62.622  51.135 1.00 16.02 ? 400 SER B CA  1 
ATOM   4859 C  C   . SER B  1 210 ? 90.155  63.034  50.607 1.00 18.46 ? 400 SER B C   1 
ATOM   4860 O  O   . SER B  1 210 ? 90.518  62.700  49.479 1.00 19.40 ? 400 SER B O   1 
ATOM   4861 C  CB  . SER B  1 210 ? 88.925  61.293  51.870 1.00 9.84  ? 400 SER B CB  1 
ATOM   4862 O  OG  . SER B  1 210 ? 89.581  60.338  51.054 1.00 7.00  ? 400 SER B OG  1 
ATOM   4863 N  N   . PRO B  1 211 ? 90.921  63.790  51.409 1.00 18.47 ? 401 PRO B N   1 
ATOM   4864 C  CA  . PRO B  1 211 ? 92.256  64.229  50.995 1.00 17.80 ? 401 PRO B CA  1 
ATOM   4865 C  C   . PRO B  1 211 ? 93.099  62.998  50.666 1.00 14.78 ? 401 PRO B C   1 
ATOM   4866 O  O   . PRO B  1 211 ? 93.113  62.030  51.420 1.00 15.42 ? 401 PRO B O   1 
ATOM   4867 C  CB  . PRO B  1 211 ? 92.766  64.976  52.228 1.00 13.52 ? 401 PRO B CB  1 
ATOM   4868 C  CG  . PRO B  1 211 ? 91.521  65.588  52.768 1.00 13.15 ? 401 PRO B CG  1 
ATOM   4869 C  CD  . PRO B  1 211 ? 90.525  64.445  52.668 1.00 20.94 ? 401 PRO B CD  1 
ATOM   4870 N  N   . PRO B  1 212 ? 93.812  63.022  49.536 1.00 16.39 ? 402 PRO B N   1 
ATOM   4871 C  CA  . PRO B  1 212 ? 94.634  61.867  49.167 1.00 19.61 ? 402 PRO B CA  1 
ATOM   4872 C  C   . PRO B  1 212 ? 95.567  61.382  50.273 1.00 18.47 ? 402 PRO B C   1 
ATOM   4873 O  O   . PRO B  1 212 ? 96.172  62.177  50.991 1.00 13.07 ? 402 PRO B O   1 
ATOM   4874 C  CB  . PRO B  1 212 ? 95.385  62.359  47.930 1.00 16.45 ? 402 PRO B CB  1 
ATOM   4875 C  CG  . PRO B  1 212 ? 95.485  63.833  48.165 1.00 26.42 ? 402 PRO B CG  1 
ATOM   4876 C  CD  . PRO B  1 212 ? 94.106  64.173  48.668 1.00 17.38 ? 402 PRO B CD  1 
ATOM   4877 N  N   . VAL B  1 213 ? 95.657  60.064  50.408 1.00 20.94 ? 403 VAL B N   1 
ATOM   4878 C  CA  . VAL B  1 213 ? 96.516  59.445  51.406 1.00 22.80 ? 403 VAL B CA  1 
ATOM   4879 C  C   . VAL B  1 213 ? 97.464  58.476  50.724 1.00 25.10 ? 403 VAL B C   1 
ATOM   4880 O  O   . VAL B  1 213 ? 97.039  57.463  50.171 1.00 24.64 ? 403 VAL B O   1 
ATOM   4881 C  CB  . VAL B  1 213 ? 95.697  58.678  52.458 1.00 22.54 ? 403 VAL B CB  1 
ATOM   4882 C  CG1 . VAL B  1 213 ? 96.610  57.780  53.279 1.00 15.22 ? 403 VAL B CG1 1 
ATOM   4883 C  CG2 . VAL B  1 213 ? 94.984  59.659  53.363 1.00 15.31 ? 403 VAL B CG2 1 
ATOM   4884 N  N   . CYS B  1 214 ? 98.753  58.792  50.761 1.00 26.33 ? 404 CYS B N   1 
ATOM   4885 C  CA  . CYS B  1 214 ? 99.741  57.932  50.139 1.00 24.97 ? 404 CYS B CA  1 
ATOM   4886 C  C   . CYS B  1 214 ? 100.006 56.687  50.978 1.00 24.02 ? 404 CYS B C   1 
ATOM   4887 O  O   . CYS B  1 214 ? 100.464 56.779  52.116 1.00 22.08 ? 404 CYS B O   1 
ATOM   4888 C  CB  . CYS B  1 214 ? 101.054 58.683  49.912 1.00 26.35 ? 404 CYS B CB  1 
ATOM   4889 S  SG  . CYS B  1 214 ? 102.313 57.544  49.267 1.00 31.16 ? 404 CYS B SG  1 
ATOM   4890 N  N   . GLY B  1 215 ? 99.716  55.525  50.401 1.00 26.09 ? 405 GLY B N   1 
ATOM   4891 C  CA  . GLY B  1 215 ? 99.926  54.267  51.095 1.00 23.60 ? 405 GLY B CA  1 
ATOM   4892 C  C   . GLY B  1 215 ? 98.627  53.588  51.490 1.00 24.71 ? 405 GLY B C   1 
ATOM   4893 O  O   . GLY B  1 215 ? 98.640  52.578  52.188 1.00 26.94 ? 405 GLY B O   1 
ATOM   4894 N  N   . ASN B  1 216 ? 97.501  54.134  51.041 1.00 25.03 ? 406 ASN B N   1 
ATOM   4895 C  CA  . ASN B  1 216 ? 96.197  53.570  51.370 1.00 25.27 ? 406 ASN B CA  1 
ATOM   4896 C  C   . ASN B  1 216 ? 95.716  52.622  50.282 1.00 23.29 ? 406 ASN B C   1 
ATOM   4897 O  O   . ASN B  1 216 ? 94.592  52.133  50.328 1.00 22.72 ? 406 ASN B O   1 
ATOM   4898 C  CB  . ASN B  1 216 ? 95.177  54.695  51.573 1.00 30.88 ? 406 ASN B CB  1 
ATOM   4899 C  CG  . ASN B  1 216 ? 94.749  55.338  50.270 1.00 32.38 ? 406 ASN B CG  1 
ATOM   4900 O  OD1 . ASN B  1 216 ? 95.519  55.398  49.311 1.00 34.70 ? 406 ASN B OD1 1 
ATOM   4901 N  ND2 . ASN B  1 216 ? 93.518  55.837  50.234 1.00 30.98 ? 406 ASN B ND2 1 
ATOM   4902 N  N   . GLU B  1 217 ? 96.582  52.367  49.306 1.00 23.97 ? 407 GLU B N   1 
ATOM   4903 C  CA  . GLU B  1 217 ? 96.279  51.475  48.191 1.00 22.93 ? 407 GLU B CA  1 
ATOM   4904 C  C   . GLU B  1 217 ? 95.125  51.951  47.322 1.00 22.90 ? 407 GLU B C   1 
ATOM   4905 O  O   . GLU B  1 217 ? 94.342  51.158  46.807 1.00 27.53 ? 407 GLU B O   1 
ATOM   4906 C  CB  . GLU B  1 217 ? 96.020  50.055  48.704 1.00 25.28 ? 407 GLU B CB  1 
ATOM   4907 C  CG  . GLU B  1 217 ? 97.301  49.247  48.845 1.00 28.09 ? 407 GLU B CG  1 
ATOM   4908 C  CD  . GLU B  1 217 ? 97.176  48.084  49.801 1.00 33.45 ? 407 GLU B CD  1 
ATOM   4909 O  OE1 . GLU B  1 217 ? 96.294  47.224  49.596 1.00 37.95 ? 407 GLU B OE1 1 
ATOM   4910 O  OE2 . GLU B  1 217 ? 97.973  48.030  50.762 1.00 37.62 ? 407 GLU B OE2 1 
ATOM   4911 N  N   . LEU B  1 218 ? 95.035  53.263  47.165 1.00 23.49 ? 408 LEU B N   1 
ATOM   4912 C  CA  . LEU B  1 218 ? 94.011  53.876  46.336 1.00 20.86 ? 408 LEU B CA  1 
ATOM   4913 C  C   . LEU B  1 218 ? 94.707  54.958  45.522 1.00 20.14 ? 408 LEU B C   1 
ATOM   4914 O  O   . LEU B  1 218 ? 95.276  55.893  46.084 1.00 21.80 ? 408 LEU B O   1 
ATOM   4915 C  CB  . LEU B  1 218 ? 92.912  54.486  47.209 1.00 19.76 ? 408 LEU B CB  1 
ATOM   4916 C  CG  . LEU B  1 218 ? 91.975  53.492  47.903 1.00 20.59 ? 408 LEU B CG  1 
ATOM   4917 C  CD1 . LEU B  1 218 ? 91.112  54.214  48.932 1.00 12.31 ? 408 LEU B CD1 1 
ATOM   4918 C  CD2 . LEU B  1 218 ? 91.104  52.800  46.855 1.00 10.31 ? 408 LEU B CD2 1 
ATOM   4919 N  N   . LEU B  1 219 ? 94.686  54.820  44.200 1.00 17.99 ? 409 LEU B N   1 
ATOM   4920 C  CA  . LEU B  1 219 ? 95.335  55.806  43.346 1.00 18.31 ? 409 LEU B CA  1 
ATOM   4921 C  C   . LEU B  1 219 ? 94.505  57.077  43.340 1.00 15.97 ? 409 LEU B C   1 
ATOM   4922 O  O   . LEU B  1 219 ? 93.426  57.132  42.749 1.00 16.59 ? 409 LEU B O   1 
ATOM   4923 C  CB  . LEU B  1 219 ? 95.493  55.273  41.920 1.00 18.36 ? 409 LEU B CB  1 
ATOM   4924 C  CG  . LEU B  1 219 ? 96.367  56.142  41.007 1.00 19.52 ? 409 LEU B CG  1 
ATOM   4925 C  CD1 . LEU B  1 219 ? 97.762  56.284  41.600 1.00 15.74 ? 409 LEU B CD1 1 
ATOM   4926 C  CD2 . LEU B  1 219 ? 96.441  55.516  39.632 1.00 19.65 ? 409 LEU B CD2 1 
ATOM   4927 N  N   . GLU B  1 220 ? 95.017  58.100  44.010 1.00 18.07 ? 410 GLU B N   1 
ATOM   4928 C  CA  . GLU B  1 220 ? 94.320  59.371  44.112 1.00 18.33 ? 410 GLU B CA  1 
ATOM   4929 C  C   . GLU B  1 220 ? 95.046  60.464  43.342 1.00 20.26 ? 410 GLU B C   1 
ATOM   4930 O  O   . GLU B  1 220 ? 96.209  60.303  42.953 1.00 15.95 ? 410 GLU B O   1 
ATOM   4931 C  CB  . GLU B  1 220 ? 94.184  59.751  45.586 1.00 20.79 ? 410 GLU B CB  1 
ATOM   4932 C  CG  . GLU B  1 220 ? 93.437  58.698  46.404 1.00 25.73 ? 410 GLU B CG  1 
ATOM   4933 C  CD  . GLU B  1 220 ? 93.667  58.836  47.895 1.00 26.44 ? 410 GLU B CD  1 
ATOM   4934 O  OE1 . GLU B  1 220 ? 94.820  58.654  48.342 1.00 28.14 ? 410 GLU B OE1 1 
ATOM   4935 O  OE2 . GLU B  1 220 ? 92.696  59.128  48.622 1.00 30.28 ? 410 GLU B OE2 1 
ATOM   4936 N  N   . VAL B  1 221 ? 94.354  61.578  43.121 1.00 17.17 ? 411 VAL B N   1 
ATOM   4937 C  CA  . VAL B  1 221 ? 94.937  62.692  42.386 1.00 15.24 ? 411 VAL B CA  1 
ATOM   4938 C  C   . VAL B  1 221 ? 96.244  63.168  43.015 1.00 15.05 ? 411 VAL B C   1 
ATOM   4939 O  O   . VAL B  1 221 ? 96.338  63.347  44.232 1.00 15.11 ? 411 VAL B O   1 
ATOM   4940 C  CB  . VAL B  1 221 ? 93.948  63.872  42.297 1.00 14.34 ? 411 VAL B CB  1 
ATOM   4941 C  CG1 . VAL B  1 221 ? 94.579  65.025  41.533 1.00 11.34 ? 411 VAL B CG1 1 
ATOM   4942 C  CG2 . VAL B  1 221 ? 92.668  63.418  41.607 1.00 6.65  ? 411 VAL B CG2 1 
ATOM   4943 N  N   . GLY B  1 222 ? 97.252  63.367  42.171 1.00 16.90 ? 412 GLY B N   1 
ATOM   4944 C  CA  . GLY B  1 222 ? 98.548  63.817  42.644 1.00 12.11 ? 412 GLY B CA  1 
ATOM   4945 C  C   . GLY B  1 222 ? 99.483  62.658  42.938 1.00 17.60 ? 412 GLY B C   1 
ATOM   4946 O  O   . GLY B  1 222 ? 100.660 62.864  43.240 1.00 18.92 ? 412 GLY B O   1 
ATOM   4947 N  N   . GLU B  1 223 ? 98.962  61.437  42.852 1.00 16.28 ? 413 GLU B N   1 
ATOM   4948 C  CA  . GLU B  1 223 ? 99.768  60.252  43.122 1.00 17.61 ? 413 GLU B CA  1 
ATOM   4949 C  C   . GLU B  1 223 ? 100.059 59.488  41.841 1.00 17.68 ? 413 GLU B C   1 
ATOM   4950 O  O   . GLU B  1 223 ? 99.146  59.176  41.077 1.00 18.46 ? 413 GLU B O   1 
ATOM   4951 C  CB  . GLU B  1 223 ? 99.044  59.319  44.093 1.00 23.63 ? 413 GLU B CB  1 
ATOM   4952 C  CG  . GLU B  1 223 ? 98.431  59.998  45.299 1.00 28.41 ? 413 GLU B CG  1 
ATOM   4953 C  CD  . GLU B  1 223 ? 97.908  58.997  46.310 1.00 31.82 ? 413 GLU B CD  1 
ATOM   4954 O  OE1 . GLU B  1 223 ? 97.234  58.030  45.893 1.00 25.60 ? 413 GLU B OE1 1 
ATOM   4955 O  OE2 . GLU B  1 223 ? 98.169  59.183  47.519 1.00 35.90 ? 413 GLU B OE2 1 
ATOM   4956 N  N   . GLU B  1 224 ? 101.332 59.180  41.613 1.00 15.73 ? 414 GLU B N   1 
ATOM   4957 C  CA  . GLU B  1 224 ? 101.725 58.441  40.424 1.00 15.90 ? 414 GLU B CA  1 
ATOM   4958 C  C   . GLU B  1 224 ? 101.357 56.983  40.616 1.00 16.56 ? 414 GLU B C   1 
ATOM   4959 O  O   . GLU B  1 224 ? 100.999 56.288  39.668 1.00 18.86 ? 414 GLU B O   1 
ATOM   4960 C  CB  . GLU B  1 224 ? 103.228 58.580  40.189 1.00 23.28 ? 414 GLU B CB  1 
ATOM   4961 C  CG  . GLU B  1 224 ? 103.663 60.006  39.895 1.00 29.74 ? 414 GLU B CG  1 
ATOM   4962 C  CD  . GLU B  1 224 ? 105.155 60.136  39.689 1.00 32.05 ? 414 GLU B CD  1 
ATOM   4963 O  OE1 . GLU B  1 224 ? 105.610 61.246  39.346 1.00 37.97 ? 414 GLU B OE1 1 
ATOM   4964 O  OE2 . GLU B  1 224 ? 105.876 59.134  39.873 1.00 38.54 ? 414 GLU B OE2 1 
ATOM   4965 N  N   . CYS B  1 225 ? 101.441 56.534  41.862 1.00 19.55 ? 415 CYS B N   1 
ATOM   4966 C  CA  . CYS B  1 225 ? 101.119 55.162  42.224 1.00 21.40 ? 415 CYS B CA  1 
ATOM   4967 C  C   . CYS B  1 225 ? 100.917 55.083  43.728 1.00 21.83 ? 415 CYS B C   1 
ATOM   4968 O  O   . CYS B  1 225 ? 101.338 55.972  44.470 1.00 18.90 ? 415 CYS B O   1 
ATOM   4969 C  CB  . CYS B  1 225 ? 102.254 54.227  41.815 1.00 23.42 ? 415 CYS B CB  1 
ATOM   4970 S  SG  . CYS B  1 225 ? 103.878 54.750  42.449 1.00 34.61 ? 415 CYS B SG  1 
ATOM   4971 N  N   . ASP B  1 226 ? 100.270 54.013  44.172 1.00 22.36 ? 416 ASP B N   1 
ATOM   4972 C  CA  . ASP B  1 226 ? 100.011 53.806  45.589 1.00 22.18 ? 416 ASP B CA  1 
ATOM   4973 C  C   . ASP B  1 226 ? 99.988  52.305  45.834 1.00 26.06 ? 416 ASP B C   1 
ATOM   4974 O  O   . ASP B  1 226 ? 99.024  51.630  45.471 1.00 24.84 ? 416 ASP B O   1 
ATOM   4975 C  CB  . ASP B  1 226 ? 98.662  54.419  45.971 1.00 18.09 ? 416 ASP B CB  1 
ATOM   4976 C  CG  . ASP B  1 226 ? 98.432  54.435  47.468 1.00 19.59 ? 416 ASP B CG  1 
ATOM   4977 O  OD1 . ASP B  1 226 ? 98.529  53.363  48.099 1.00 16.71 ? 416 ASP B OD1 1 
ATOM   4978 O  OD2 . ASP B  1 226 ? 98.149  55.522  48.016 1.00 19.58 ? 416 ASP B OD2 1 
ATOM   4979 N  N   . CYS B  1 227 ? 101.057 51.783  46.432 1.00 27.38 ? 417 CYS B N   1 
ATOM   4980 C  CA  . CYS B  1 227 ? 101.151 50.354  46.714 1.00 30.45 ? 417 CYS B CA  1 
ATOM   4981 C  C   . CYS B  1 227 ? 101.144 50.101  48.217 1.00 33.27 ? 417 CYS B C   1 
ATOM   4982 O  O   . CYS B  1 227 ? 101.844 49.220  48.717 1.00 33.56 ? 417 CYS B O   1 
ATOM   4983 C  CB  . CYS B  1 227 ? 102.423 49.765  46.077 1.00 32.26 ? 417 CYS B CB  1 
ATOM   4984 S  SG  . CYS B  1 227 ? 104.025 50.447  46.646 1.00 42.15 ? 417 CYS B SG  1 
ATOM   4985 N  N   . GLY B  1 228 ? 100.341 50.880  48.934 1.00 34.36 ? 418 GLY B N   1 
ATOM   4986 C  CA  . GLY B  1 228 ? 100.263 50.735  50.376 1.00 33.84 ? 418 GLY B CA  1 
ATOM   4987 C  C   . GLY B  1 228 ? 101.538 51.217  51.038 1.00 36.25 ? 418 GLY B C   1 
ATOM   4988 O  O   . GLY B  1 228 ? 102.302 51.982  50.445 1.00 39.36 ? 418 GLY B O   1 
ATOM   4989 N  N   . THR B  1 229 ? 101.772 50.773  52.268 1.00 34.10 ? 419 THR B N   1 
ATOM   4990 C  CA  . THR B  1 229 ? 102.968 51.161  53.005 1.00 32.33 ? 419 THR B CA  1 
ATOM   4991 C  C   . THR B  1 229 ? 104.163 50.399  52.449 1.00 31.15 ? 419 THR B C   1 
ATOM   4992 O  O   . THR B  1 229 ? 103.994 49.366  51.799 1.00 32.23 ? 419 THR B O   1 
ATOM   4993 C  CB  . THR B  1 229 ? 102.818 50.841  54.497 1.00 32.11 ? 419 THR B CB  1 
ATOM   4994 O  OG1 . THR B  1 229 ? 102.439 49.468  54.649 1.00 35.98 ? 419 THR B OG1 1 
ATOM   4995 C  CG2 . THR B  1 229 ? 101.754 51.730  55.128 1.00 25.54 ? 419 THR B CG2 1 
ATOM   4996 N  N   . PRO B  1 230 ? 105.388 50.897  52.686 1.00 31.85 ? 420 PRO B N   1 
ATOM   4997 C  CA  . PRO B  1 230 ? 106.564 50.192  52.166 1.00 32.61 ? 420 PRO B CA  1 
ATOM   4998 C  C   . PRO B  1 230 ? 106.663 48.741  52.626 1.00 33.13 ? 420 PRO B C   1 
ATOM   4999 O  O   . PRO B  1 230 ? 107.345 47.932  52.001 1.00 37.88 ? 420 PRO B O   1 
ATOM   5000 C  CB  . PRO B  1 230 ? 107.736 51.057  52.643 1.00 25.84 ? 420 PRO B CB  1 
ATOM   5001 C  CG  . PRO B  1 230 ? 107.192 51.764  53.848 1.00 31.60 ? 420 PRO B CG  1 
ATOM   5002 C  CD  . PRO B  1 230 ? 105.785 52.105  53.430 1.00 32.56 ? 420 PRO B CD  1 
ATOM   5003 N  N   . GLU B  1 231 ? 105.966 48.412  53.708 1.00 33.16 ? 421 GLU B N   1 
ATOM   5004 C  CA  . GLU B  1 231 ? 105.976 47.054  54.237 1.00 35.21 ? 421 GLU B CA  1 
ATOM   5005 C  C   . GLU B  1 231 ? 105.047 46.140  53.449 1.00 34.43 ? 421 GLU B C   1 
ATOM   5006 O  O   . GLU B  1 231 ? 105.386 44.991  53.171 1.00 32.96 ? 421 GLU B O   1 
ATOM   5007 C  CB  . GLU B  1 231 ? 105.564 47.048  55.713 1.00 41.53 ? 421 GLU B CB  1 
ATOM   5008 C  CG  . GLU B  1 231 ? 106.613 47.620  56.658 1.00 52.37 ? 421 GLU B CG  1 
ATOM   5009 C  CD  . GLU B  1 231 ? 106.845 49.106  56.460 1.00 56.39 ? 421 GLU B CD  1 
ATOM   5010 O  OE1 . GLU B  1 231 ? 107.828 49.635  57.023 1.00 59.77 ? 421 GLU B OE1 1 
ATOM   5011 O  OE2 . GLU B  1 231 ? 106.041 49.748  55.751 1.00 59.72 ? 421 GLU B OE2 1 
ATOM   5012 N  N   . ASN B  1 232 ? 103.876 46.650  53.086 1.00 33.36 ? 422 ASN B N   1 
ATOM   5013 C  CA  . ASN B  1 232 ? 102.909 45.857  52.336 1.00 33.17 ? 422 ASN B CA  1 
ATOM   5014 C  C   . ASN B  1 232 ? 103.081 45.957  50.826 1.00 32.45 ? 422 ASN B C   1 
ATOM   5015 O  O   . ASN B  1 232 ? 102.567 45.117  50.089 1.00 28.09 ? 422 ASN B O   1 
ATOM   5016 C  CB  . ASN B  1 232 ? 101.482 46.274  52.705 1.00 36.74 ? 422 ASN B CB  1 
ATOM   5017 C  CG  . ASN B  1 232 ? 101.111 45.895  54.122 1.00 39.48 ? 422 ASN B CG  1 
ATOM   5018 O  OD1 . ASN B  1 232 ? 101.117 44.720  54.480 1.00 44.60 ? 422 ASN B OD1 1 
ATOM   5019 N  ND2 . ASN B  1 232 ? 100.784 46.891  54.937 1.00 41.95 ? 422 ASN B ND2 1 
ATOM   5020 N  N   . CYS B  1 233 ? 103.802 46.979  50.369 1.00 36.72 ? 423 CYS B N   1 
ATOM   5021 C  CA  . CYS B  1 233 ? 104.007 47.190  48.937 1.00 40.29 ? 423 CYS B CA  1 
ATOM   5022 C  C   . CYS B  1 233 ? 104.527 45.957  48.211 1.00 42.81 ? 423 CYS B C   1 
ATOM   5023 O  O   . CYS B  1 233 ? 105.563 45.396  48.568 1.00 43.21 ? 423 CYS B O   1 
ATOM   5024 C  CB  . CYS B  1 233 ? 104.960 48.368  48.697 1.00 40.99 ? 423 CYS B CB  1 
ATOM   5025 S  SG  . CYS B  1 233 ? 105.207 48.812  46.940 1.00 42.24 ? 423 CYS B SG  1 
ATOM   5026 N  N   . GLN B  1 234 ? 103.787 45.539  47.190 1.00 45.56 ? 424 GLN B N   1 
ATOM   5027 C  CA  . GLN B  1 234 ? 104.157 44.382  46.387 1.00 48.32 ? 424 GLN B CA  1 
ATOM   5028 C  C   . GLN B  1 234 ? 104.428 44.849  44.963 1.00 48.63 ? 424 GLN B C   1 
ATOM   5029 O  O   . GLN B  1 234 ? 104.635 44.037  44.062 1.00 52.17 ? 424 GLN B O   1 
ATOM   5030 C  CB  . GLN B  1 234 ? 103.025 43.351  46.379 1.00 53.38 ? 424 GLN B CB  1 
ATOM   5031 C  CG  . GLN B  1 234 ? 102.631 42.824  47.752 1.00 59.30 ? 424 GLN B CG  1 
ATOM   5032 C  CD  . GLN B  1 234 ? 103.752 42.061  48.434 1.00 64.45 ? 424 GLN B CD  1 
ATOM   5033 O  OE1 . GLN B  1 234 ? 104.262 41.075  47.901 1.00 64.60 ? 424 GLN B OE1 1 
ATOM   5034 N  NE2 . GLN B  1 234 ? 104.139 42.513  49.623 1.00 68.04 ? 424 GLN B NE2 1 
ATOM   5035 N  N   . ASN B  1 235 ? 104.414 46.166  44.766 1.00 46.85 ? 425 ASN B N   1 
ATOM   5036 C  CA  . ASN B  1 235 ? 104.662 46.753  43.453 1.00 42.73 ? 425 ASN B CA  1 
ATOM   5037 C  C   . ASN B  1 235 ? 106.114 47.208  43.356 1.00 42.13 ? 425 ASN B C   1 
ATOM   5038 O  O   . ASN B  1 235 ? 106.601 47.954  44.207 1.00 42.06 ? 425 ASN B O   1 
ATOM   5039 C  CB  . ASN B  1 235 ? 103.730 47.943  43.220 1.00 36.49 ? 425 ASN B CB  1 
ATOM   5040 C  CG  . ASN B  1 235 ? 103.845 48.507  41.818 1.00 36.22 ? 425 ASN B CG  1 
ATOM   5041 O  OD1 . ASN B  1 235 ? 103.145 49.454  41.459 1.00 39.41 ? 425 ASN B OD1 1 
ATOM   5042 N  ND2 . ASN B  1 235 ? 104.732 47.928  41.015 1.00 36.74 ? 425 ASN B ND2 1 
ATOM   5043 N  N   . GLU B  1 236 ? 106.799 46.762  42.310 1.00 41.67 ? 426 GLU B N   1 
ATOM   5044 C  CA  . GLU B  1 236 ? 108.200 47.110  42.126 1.00 43.36 ? 426 GLU B CA  1 
ATOM   5045 C  C   . GLU B  1 236 ? 108.430 48.349  41.262 1.00 41.39 ? 426 GLU B C   1 
ATOM   5046 O  O   . GLU B  1 236 ? 109.570 48.679  40.928 1.00 37.31 ? 426 GLU B O   1 
ATOM   5047 C  CB  . GLU B  1 236 ? 108.950 45.907  41.550 1.00 43.76 ? 426 GLU B CB  1 
ATOM   5048 C  CG  . GLU B  1 236 ? 108.817 44.664  42.420 1.00 54.06 ? 426 GLU B CG  1 
ATOM   5049 C  CD  . GLU B  1 236 ? 109.815 43.575  42.070 1.00 58.23 ? 426 GLU B CD  1 
ATOM   5050 O  OE1 . GLU B  1 236 ? 111.034 43.840  42.154 1.00 56.11 ? 426 GLU B OE1 1 
ATOM   5051 O  OE2 . GLU B  1 236 ? 109.378 42.456  41.719 1.00 57.61 ? 426 GLU B OE2 1 
ATOM   5052 N  N   . CYS B  1 237 ? 107.350 49.044  40.917 1.00 35.31 ? 427 CYS B N   1 
ATOM   5053 C  CA  . CYS B  1 237 ? 107.461 50.244  40.098 1.00 33.37 ? 427 CYS B CA  1 
ATOM   5054 C  C   . CYS B  1 237 ? 107.225 51.484  40.938 1.00 32.86 ? 427 CYS B C   1 
ATOM   5055 O  O   . CYS B  1 237 ? 107.503 52.604  40.510 1.00 34.91 ? 427 CYS B O   1 
ATOM   5056 C  CB  . CYS B  1 237 ? 106.423 50.223  38.985 1.00 33.05 ? 427 CYS B CB  1 
ATOM   5057 S  SG  . CYS B  1 237 ? 106.228 48.625  38.149 1.00 40.67 ? 427 CYS B SG  1 
ATOM   5058 N  N   . CYS B  1 238 ? 106.716 51.277  42.143 1.00 34.54 ? 428 CYS B N   1 
ATOM   5059 C  CA  . CYS B  1 238 ? 106.391 52.381  43.026 1.00 33.90 ? 428 CYS B CA  1 
ATOM   5060 C  C   . CYS B  1 238 ? 107.350 52.546  44.195 1.00 34.68 ? 428 CYS B C   1 
ATOM   5061 O  O   . CYS B  1 238 ? 108.088 51.627  44.550 1.00 35.63 ? 428 CYS B O   1 
ATOM   5062 C  CB  . CYS B  1 238 ? 104.969 52.177  43.561 1.00 32.03 ? 428 CYS B CB  1 
ATOM   5063 S  SG  . CYS B  1 238 ? 104.135 53.679  44.155 1.00 30.67 ? 428 CYS B SG  1 
ATOM   5064 N  N   . ASP B  1 239 ? 107.336 53.741  44.771 1.00 33.81 ? 429 ASP B N   1 
ATOM   5065 C  CA  . ASP B  1 239 ? 108.136 54.056  45.944 1.00 33.35 ? 429 ASP B CA  1 
ATOM   5066 C  C   . ASP B  1 239 ? 107.086 54.229  47.030 1.00 33.69 ? 429 ASP B C   1 
ATOM   5067 O  O   . ASP B  1 239 ? 106.650 55.347  47.312 1.00 32.45 ? 429 ASP B O   1 
ATOM   5068 C  CB  . ASP B  1 239 ? 108.895 55.367  45.765 1.00 36.84 ? 429 ASP B CB  1 
ATOM   5069 C  CG  . ASP B  1 239 ? 109.643 55.777  47.018 1.00 37.29 ? 429 ASP B CG  1 
ATOM   5070 O  OD1 . ASP B  1 239 ? 110.155 56.916  47.066 1.00 40.92 ? 429 ASP B OD1 1 
ATOM   5071 O  OD2 . ASP B  1 239 ? 109.722 54.955  47.957 1.00 38.12 ? 429 ASP B OD2 1 
ATOM   5072 N  N   . ALA B  1 240 ? 106.669 53.110  47.614 1.00 30.17 ? 430 ALA B N   1 
ATOM   5073 C  CA  . ALA B  1 240 ? 105.644 53.090  48.650 1.00 26.75 ? 430 ALA B CA  1 
ATOM   5074 C  C   . ALA B  1 240 ? 105.632 54.303  49.579 1.00 26.98 ? 430 ALA B C   1 
ATOM   5075 O  O   . ALA B  1 240 ? 104.575 54.716  50.054 1.00 32.62 ? 430 ALA B O   1 
ATOM   5076 C  CB  . ALA B  1 240 ? 105.778 51.818  49.462 1.00 21.56 ? 430 ALA B CB  1 
ATOM   5077 N  N   . ALA B  1 241 ? 106.801 54.877  49.831 1.00 23.84 ? 431 ALA B N   1 
ATOM   5078 C  CA  . ALA B  1 241 ? 106.910 56.027  50.720 1.00 26.02 ? 431 ALA B CA  1 
ATOM   5079 C  C   . ALA B  1 241 ? 106.418 57.360  50.149 1.00 26.11 ? 431 ALA B C   1 
ATOM   5080 O  O   . ALA B  1 241 ? 105.742 58.117  50.842 1.00 29.34 ? 431 ALA B O   1 
ATOM   5081 C  CB  . ALA B  1 241 ? 108.356 56.171  51.191 1.00 28.69 ? 431 ALA B CB  1 
ATOM   5082 N  N   . THR B  1 242 ? 106.746 57.645  48.892 1.00 28.59 ? 432 THR B N   1 
ATOM   5083 C  CA  . THR B  1 242 ? 106.359 58.913  48.270 1.00 28.37 ? 432 THR B CA  1 
ATOM   5084 C  C   . THR B  1 242 ? 105.233 58.862  47.233 1.00 24.92 ? 432 THR B C   1 
ATOM   5085 O  O   . THR B  1 242 ? 104.740 59.903  46.801 1.00 28.45 ? 432 THR B O   1 
ATOM   5086 C  CB  . THR B  1 242 ? 107.579 59.574  47.599 1.00 28.15 ? 432 THR B CB  1 
ATOM   5087 O  OG1 . THR B  1 242 ? 108.100 58.701  46.589 1.00 28.83 ? 432 THR B OG1 1 
ATOM   5088 C  CG2 . THR B  1 242 ? 108.662 59.852  48.625 1.00 26.32 ? 432 THR B CG2 1 
ATOM   5089 N  N   . CYS B  1 243 ? 104.829 57.664  46.835 1.00 21.29 ? 433 CYS B N   1 
ATOM   5090 C  CA  . CYS B  1 243 ? 103.778 57.508  45.834 1.00 24.40 ? 433 CYS B CA  1 
ATOM   5091 C  C   . CYS B  1 243 ? 104.180 58.043  44.465 1.00 27.42 ? 433 CYS B C   1 
ATOM   5092 O  O   . CYS B  1 243 ? 103.352 58.552  43.709 1.00 31.76 ? 433 CYS B O   1 
ATOM   5093 C  CB  . CYS B  1 243 ? 102.480 58.168  46.310 1.00 22.24 ? 433 CYS B CB  1 
ATOM   5094 S  SG  . CYS B  1 243 ? 101.579 57.062  47.435 1.00 23.87 ? 433 CYS B SG  1 
ATOM   5095 N  N   . LYS B  1 244 ? 105.466 57.915  44.154 1.00 28.87 ? 434 LYS B N   1 
ATOM   5096 C  CA  . LYS B  1 244 ? 106.008 58.351  42.874 1.00 27.30 ? 434 LYS B CA  1 
ATOM   5097 C  C   . LYS B  1 244 ? 106.648 57.143  42.205 1.00 26.94 ? 434 LYS B C   1 
ATOM   5098 O  O   . LYS B  1 244 ? 107.383 56.393  42.852 1.00 26.83 ? 434 LYS B O   1 
ATOM   5099 C  CB  . LYS B  1 244 ? 107.075 59.436  43.076 1.00 24.10 ? 434 LYS B CB  1 
ATOM   5100 C  CG  . LYS B  1 244 ? 106.556 60.763  43.599 1.00 27.21 ? 434 LYS B CG  1 
ATOM   5101 C  CD  . LYS B  1 244 ? 105.586 61.394  42.614 1.00 40.07 ? 434 LYS B CD  1 
ATOM   5102 C  CE  . LYS B  1 244 ? 105.001 62.697  43.146 1.00 43.76 ? 434 LYS B CE  1 
ATOM   5103 N  NZ  . LYS B  1 244 ? 103.987 63.267  42.212 1.00 42.78 ? 434 LYS B NZ  1 
ATOM   5104 N  N   . LEU B  1 245 ? 106.360 56.937  40.923 1.00 24.92 ? 435 LEU B N   1 
ATOM   5105 C  CA  . LEU B  1 245 ? 106.958 55.822  40.196 1.00 24.52 ? 435 LEU B CA  1 
ATOM   5106 C  C   . LEU B  1 245 ? 108.470 55.993  40.288 1.00 25.05 ? 435 LEU B C   1 
ATOM   5107 O  O   . LEU B  1 245 ? 108.979 57.107  40.152 1.00 24.07 ? 435 LEU B O   1 
ATOM   5108 C  CB  . LEU B  1 245 ? 106.534 55.847  38.725 1.00 17.45 ? 435 LEU B CB  1 
ATOM   5109 C  CG  . LEU B  1 245 ? 105.077 55.515  38.391 1.00 22.47 ? 435 LEU B CG  1 
ATOM   5110 C  CD1 . LEU B  1 245 ? 104.845 55.697  36.893 1.00 15.17 ? 435 LEU B CD1 1 
ATOM   5111 C  CD2 . LEU B  1 245 ? 104.762 54.083  38.812 1.00 9.88  ? 435 LEU B CD2 1 
ATOM   5112 N  N   . LYS B  1 246 ? 109.195 54.910  40.535 1.00 23.28 ? 436 LYS B N   1 
ATOM   5113 C  CA  . LYS B  1 246 ? 110.638 55.041  40.624 1.00 29.67 ? 436 LYS B CA  1 
ATOM   5114 C  C   . LYS B  1 246 ? 111.220 55.313  39.243 1.00 29.96 ? 436 LYS B C   1 
ATOM   5115 O  O   . LYS B  1 246 ? 110.621 54.968  38.225 1.00 26.96 ? 436 LYS B O   1 
ATOM   5116 C  CB  . LYS B  1 246 ? 111.268 53.797  41.261 1.00 29.40 ? 436 LYS B CB  1 
ATOM   5117 C  CG  . LYS B  1 246 ? 110.707 52.472  40.805 1.00 33.86 ? 436 LYS B CG  1 
ATOM   5118 C  CD  . LYS B  1 246 ? 110.330 51.618  42.011 1.00 36.71 ? 436 LYS B CD  1 
ATOM   5119 C  CE  . LYS B  1 246 ? 111.492 51.465  42.984 1.00 35.16 ? 436 LYS B CE  1 
ATOM   5120 N  NZ  . LYS B  1 246 ? 111.118 50.665  44.186 1.00 35.77 ? 436 LYS B NZ  1 
ATOM   5121 N  N   . SER B  1 247 ? 112.380 55.960  39.220 1.00 30.69 ? 437 SER B N   1 
ATOM   5122 C  CA  . SER B  1 247 ? 113.041 56.313  37.972 1.00 31.79 ? 437 SER B CA  1 
ATOM   5123 C  C   . SER B  1 247 ? 113.168 55.144  37.008 1.00 29.30 ? 437 SER B C   1 
ATOM   5124 O  O   . SER B  1 247 ? 113.575 54.048  37.391 1.00 27.33 ? 437 SER B O   1 
ATOM   5125 C  CB  . SER B  1 247 ? 114.426 56.894  38.266 1.00 36.62 ? 437 SER B CB  1 
ATOM   5126 O  OG  . SER B  1 247 ? 114.319 58.049  39.083 1.00 42.83 ? 437 SER B OG  1 
ATOM   5127 N  N   . GLY B  1 248 ? 112.806 55.387  35.752 1.00 26.81 ? 438 GLY B N   1 
ATOM   5128 C  CA  . GLY B  1 248 ? 112.900 54.349  34.744 1.00 23.89 ? 438 GLY B CA  1 
ATOM   5129 C  C   . GLY B  1 248 ? 111.573 53.718  34.386 1.00 20.07 ? 438 GLY B C   1 
ATOM   5130 O  O   . GLY B  1 248 ? 111.368 53.293  33.250 1.00 17.23 ? 438 GLY B O   1 
ATOM   5131 N  N   . SER B  1 249 ? 110.667 53.653  35.352 1.00 23.22 ? 439 SER B N   1 
ATOM   5132 C  CA  . SER B  1 249 ? 109.361 53.055  35.110 1.00 32.98 ? 439 SER B CA  1 
ATOM   5133 C  C   . SER B  1 249 ? 108.404 54.021  34.416 1.00 31.91 ? 439 SER B C   1 
ATOM   5134 O  O   . SER B  1 249 ? 108.461 55.234  34.630 1.00 34.28 ? 439 SER B O   1 
ATOM   5135 C  CB  . SER B  1 249 ? 108.751 52.563  36.429 1.00 31.50 ? 439 SER B CB  1 
ATOM   5136 O  OG  . SER B  1 249 ? 108.656 53.612  37.373 1.00 39.77 ? 439 SER B OG  1 
ATOM   5137 N  N   . GLN B  1 250 ? 107.533 53.471  33.576 1.00 30.81 ? 440 GLN B N   1 
ATOM   5138 C  CA  . GLN B  1 250 ? 106.558 54.267  32.844 1.00 28.82 ? 440 GLN B CA  1 
ATOM   5139 C  C   . GLN B  1 250 ? 105.186 54.232  33.506 1.00 29.05 ? 440 GLN B C   1 
ATOM   5140 O  O   . GLN B  1 250 ? 104.393 55.158  33.354 1.00 26.89 ? 440 GLN B O   1 
ATOM   5141 C  CB  . GLN B  1 250 ? 106.443 53.763  31.404 1.00 25.30 ? 440 GLN B CB  1 
ATOM   5142 C  CG  . GLN B  1 250 ? 107.620 54.136  30.523 1.00 24.41 ? 440 GLN B CG  1 
ATOM   5143 C  CD  . GLN B  1 250 ? 107.481 53.619  29.101 1.00 27.51 ? 440 GLN B CD  1 
ATOM   5144 O  OE1 . GLN B  1 250 ? 108.077 54.167  28.174 1.00 23.83 ? 440 GLN B OE1 1 
ATOM   5145 N  NE2 . GLN B  1 250 ? 106.703 52.554  28.924 1.00 24.67 ? 440 GLN B NE2 1 
ATOM   5146 N  N   . CYS B  1 251 ? 104.916 53.164  34.247 1.00 29.89 ? 441 CYS B N   1 
ATOM   5147 C  CA  . CYS B  1 251 ? 103.633 53.006  34.920 1.00 31.15 ? 441 CYS B CA  1 
ATOM   5148 C  C   . CYS B  1 251 ? 103.765 52.082  36.125 1.00 33.01 ? 441 CYS B C   1 
ATOM   5149 O  O   . CYS B  1 251 ? 104.811 51.467  36.337 1.00 34.54 ? 441 CYS B O   1 
ATOM   5150 C  CB  . CYS B  1 251 ? 102.612 52.427  33.945 1.00 29.91 ? 441 CYS B CB  1 
ATOM   5151 S  SG  . CYS B  1 251 ? 103.233 50.933  33.112 1.00 27.56 ? 441 CYS B SG  1 
ATOM   5152 N  N   . GLY B  1 252 ? 102.696 51.987  36.908 1.00 32.79 ? 442 GLY B N   1 
ATOM   5153 C  CA  . GLY B  1 252 ? 102.713 51.137  38.084 1.00 31.63 ? 442 GLY B CA  1 
ATOM   5154 C  C   . GLY B  1 252 ? 101.362 50.495  38.310 1.00 30.93 ? 442 GLY B C   1 
ATOM   5155 O  O   . GLY B  1 252 ? 101.130 49.849  39.332 1.00 29.16 ? 442 GLY B O   1 
ATOM   5156 N  N   . HIS B  1 253 ? 100.470 50.679  37.342 1.00 32.19 ? 443 HIS B N   1 
ATOM   5157 C  CA  . HIS B  1 253 ? 99.123  50.127  37.401 1.00 33.00 ? 443 HIS B CA  1 
ATOM   5158 C  C   . HIS B  1 253 ? 98.514  50.145  36.002 1.00 32.35 ? 443 HIS B C   1 
ATOM   5159 O  O   . HIS B  1 253 ? 99.042  50.792  35.097 1.00 29.30 ? 443 HIS B O   1 
ATOM   5160 C  CB  . HIS B  1 253 ? 98.253  50.965  38.335 1.00 36.41 ? 443 HIS B CB  1 
ATOM   5161 C  CG  . HIS B  1 253 ? 97.945  52.327  37.799 1.00 41.93 ? 443 HIS B CG  1 
ATOM   5162 N  ND1 . HIS B  1 253 ? 98.923  53.265  37.548 1.00 47.33 ? 443 HIS B ND1 1 
ATOM   5163 C  CD2 . HIS B  1 253 ? 96.773  52.898  37.435 1.00 45.16 ? 443 HIS B CD2 1 
ATOM   5164 C  CE1 . HIS B  1 253 ? 98.366  54.355  37.051 1.00 48.24 ? 443 HIS B CE1 1 
ATOM   5165 N  NE2 . HIS B  1 253 ? 97.063  54.158  36.972 1.00 46.91 ? 443 HIS B NE2 1 
ATOM   5166 N  N   . GLY B  1 254 ? 97.400  49.437  35.832 1.00 33.01 ? 444 GLY B N   1 
ATOM   5167 C  CA  . GLY B  1 254 ? 96.734  49.403  34.542 1.00 30.18 ? 444 GLY B CA  1 
ATOM   5168 C  C   . GLY B  1 254 ? 96.879  48.093  33.796 1.00 31.02 ? 444 GLY B C   1 
ATOM   5169 O  O   . GLY B  1 254 ? 97.943  47.480  33.798 1.00 34.33 ? 444 GLY B O   1 
ATOM   5170 N  N   . ASP B  1 255 ? 95.803  47.663  33.146 1.00 34.10 ? 445 ASP B N   1 
ATOM   5171 C  CA  . ASP B  1 255 ? 95.821  46.418  32.388 1.00 34.21 ? 445 ASP B CA  1 
ATOM   5172 C  C   . ASP B  1 255 ? 96.808  46.499  31.230 1.00 33.02 ? 445 ASP B C   1 
ATOM   5173 O  O   . ASP B  1 255 ? 97.010  45.521  30.511 1.00 35.15 ? 445 ASP B O   1 
ATOM   5174 C  CB  . ASP B  1 255 ? 94.421  46.100  31.852 1.00 35.15 ? 445 ASP B CB  1 
ATOM   5175 C  CG  . ASP B  1 255 ? 93.418  45.828  32.959 1.00 31.99 ? 445 ASP B CG  1 
ATOM   5176 O  OD1 . ASP B  1 255 ? 93.640  44.884  33.750 1.00 33.34 ? 445 ASP B OD1 1 
ATOM   5177 O  OD2 . ASP B  1 255 ? 92.408  46.558  33.034 1.00 18.81 ? 445 ASP B OD2 1 
ATOM   5178 N  N   . CYS B  1 256 ? 97.411  47.669  31.044 1.00 30.85 ? 446 CYS B N   1 
ATOM   5179 C  CA  . CYS B  1 256 ? 98.388  47.852  29.978 1.00 33.43 ? 446 CYS B CA  1 
ATOM   5180 C  C   . CYS B  1 256 ? 99.762  48.210  30.524 1.00 35.06 ? 446 CYS B C   1 
ATOM   5181 O  O   . CYS B  1 256 ? 100.589 48.797  29.824 1.00 35.87 ? 446 CYS B O   1 
ATOM   5182 C  CB  . CYS B  1 256 ? 97.926  48.924  28.993 1.00 27.82 ? 446 CYS B CB  1 
ATOM   5183 S  SG  . CYS B  1 256 ? 96.607  48.352  27.882 1.00 34.48 ? 446 CYS B SG  1 
ATOM   5184 N  N   . CYS B  1 257 ? 99.995  47.857  31.785 1.00 35.19 ? 447 CYS B N   1 
ATOM   5185 C  CA  . CYS B  1 257 ? 101.277 48.110  32.422 1.00 31.26 ? 447 CYS B CA  1 
ATOM   5186 C  C   . CYS B  1 257 ? 101.950 46.781  32.730 1.00 31.86 ? 447 CYS B C   1 
ATOM   5187 O  O   . CYS B  1 257 ? 101.576 46.090  33.677 1.00 29.42 ? 447 CYS B O   1 
ATOM   5188 C  CB  . CYS B  1 257 ? 101.099 48.895  33.716 1.00 29.43 ? 447 CYS B CB  1 
ATOM   5189 S  SG  . CYS B  1 257 ? 102.708 49.428  34.372 1.00 29.21 ? 447 CYS B SG  1 
ATOM   5190 N  N   . GLU B  1 258 ? 102.943 46.422  31.925 1.00 35.29 ? 448 GLU B N   1 
ATOM   5191 C  CA  . GLU B  1 258 ? 103.645 45.163  32.121 1.00 39.74 ? 448 GLU B CA  1 
ATOM   5192 C  C   . GLU B  1 258 ? 105.107 45.381  32.511 1.00 37.60 ? 448 GLU B C   1 
ATOM   5193 O  O   . GLU B  1 258 ? 105.915 45.850  31.708 1.00 32.46 ? 448 GLU B O   1 
ATOM   5194 C  CB  . GLU B  1 258 ? 103.551 44.319  30.849 1.00 42.66 ? 448 GLU B CB  1 
ATOM   5195 C  CG  . GLU B  1 258 ? 103.639 42.824  31.094 1.00 56.52 ? 448 GLU B CG  1 
ATOM   5196 C  CD  . GLU B  1 258 ? 103.357 42.014  29.843 1.00 65.76 ? 448 GLU B CD  1 
ATOM   5197 O  OE1 . GLU B  1 258 ? 102.296 42.234  29.216 1.00 67.07 ? 448 GLU B OE1 1 
ATOM   5198 O  OE2 . GLU B  1 258 ? 104.193 41.155  29.489 1.00 72.02 ? 448 GLU B OE2 1 
ATOM   5199 N  N   . GLN B  1 259 ? 105.428 45.041  33.756 1.00 37.69 ? 449 GLN B N   1 
ATOM   5200 C  CA  . GLN B  1 259 ? 106.781 45.183  34.283 1.00 39.05 ? 449 GLN B CA  1 
ATOM   5201 C  C   . GLN B  1 259 ? 107.227 46.637  34.354 1.00 37.83 ? 449 GLN B C   1 
ATOM   5202 O  O   . GLN B  1 259 ? 108.362 46.963  34.007 1.00 38.52 ? 449 GLN B O   1 
ATOM   5203 C  CB  . GLN B  1 259 ? 107.765 44.382  33.428 1.00 43.04 ? 449 GLN B CB  1 
ATOM   5204 C  CG  . GLN B  1 259 ? 107.487 42.891  33.417 1.00 48.65 ? 449 GLN B CG  1 
ATOM   5205 C  CD  . GLN B  1 259 ? 107.427 42.316  34.816 1.00 51.61 ? 449 GLN B CD  1 
ATOM   5206 O  OE1 . GLN B  1 259 ? 108.375 42.441  35.591 1.00 55.24 ? 449 GLN B OE1 1 
ATOM   5207 N  NE2 . GLN B  1 259 ? 106.309 41.682  35.149 1.00 57.27 ? 449 GLN B NE2 1 
ATOM   5208 N  N   . CYS B  1 260 ? 106.328 47.504  34.808 1.00 34.60 ? 450 CYS B N   1 
ATOM   5209 C  CA  . CYS B  1 260 ? 106.614 48.930  34.936 1.00 31.10 ? 450 CYS B CA  1 
ATOM   5210 C  C   . CYS B  1 260 ? 106.700 49.639  33.590 1.00 29.07 ? 450 CYS B C   1 
ATOM   5211 O  O   . CYS B  1 260 ? 107.015 50.827  33.532 1.00 27.05 ? 450 CYS B O   1 
ATOM   5212 C  CB  . CYS B  1 260 ? 107.924 49.150  35.690 1.00 30.37 ? 450 CYS B CB  1 
ATOM   5213 S  SG  . CYS B  1 260 ? 108.040 48.299  37.292 1.00 35.95 ? 450 CYS B SG  1 
ATOM   5214 N  N   . LYS B  1 261 ? 106.423 48.914  32.511 1.00 24.14 ? 451 LYS B N   1 
ATOM   5215 C  CA  . LYS B  1 261 ? 106.479 49.501  31.177 1.00 23.90 ? 451 LYS B CA  1 
ATOM   5216 C  C   . LYS B  1 261 ? 105.154 49.403  30.427 1.00 20.97 ? 451 LYS B C   1 
ATOM   5217 O  O   . LYS B  1 261 ? 104.336 48.535  30.715 1.00 27.55 ? 451 LYS B O   1 
ATOM   5218 C  CB  . LYS B  1 261 ? 107.591 48.831  30.359 1.00 23.42 ? 451 LYS B CB  1 
ATOM   5219 C  CG  . LYS B  1 261 ? 108.991 49.382  30.630 1.00 23.92 ? 451 LYS B CG  1 
ATOM   5220 C  CD  . LYS B  1 261 ? 109.469 49.077  32.042 1.00 26.35 ? 451 LYS B CD  1 
ATOM   5221 C  CE  . LYS B  1 261 ? 110.527 50.079  32.517 1.00 24.33 ? 451 LYS B CE  1 
ATOM   5222 N  NZ  . LYS B  1 261 ? 111.725 50.151  31.640 1.00 20.34 ? 451 LYS B NZ  1 
ATOM   5223 N  N   . PHE B  1 262 ? 104.940 50.308  29.476 1.00 20.28 ? 452 PHE B N   1 
ATOM   5224 C  CA  . PHE B  1 262 ? 103.721 50.296  28.669 1.00 20.30 ? 452 PHE B CA  1 
ATOM   5225 C  C   . PHE B  1 262 ? 103.708 49.003  27.866 1.00 20.02 ? 452 PHE B C   1 
ATOM   5226 O  O   . PHE B  1 262 ? 104.737 48.592  27.331 1.00 22.48 ? 452 PHE B O   1 
ATOM   5227 C  CB  . PHE B  1 262 ? 103.698 51.488  27.704 1.00 18.01 ? 452 PHE B CB  1 
ATOM   5228 C  CG  . PHE B  1 262 ? 103.459 52.812  28.373 1.00 23.04 ? 452 PHE B CG  1 
ATOM   5229 C  CD1 . PHE B  1 262 ? 103.951 53.987  27.808 1.00 26.07 ? 452 PHE B CD1 1 
ATOM   5230 C  CD2 . PHE B  1 262 ? 102.734 52.892  29.565 1.00 25.96 ? 452 PHE B CD2 1 
ATOM   5231 C  CE1 . PHE B  1 262 ? 103.730 55.225  28.417 1.00 24.94 ? 452 PHE B CE1 1 
ATOM   5232 C  CE2 . PHE B  1 262 ? 102.505 54.120  30.183 1.00 23.99 ? 452 PHE B CE2 1 
ATOM   5233 C  CZ  . PHE B  1 262 ? 103.005 55.291  29.609 1.00 27.36 ? 452 PHE B CZ  1 
ATOM   5234 N  N   . SER B  1 263 ? 102.550 48.357  27.782 1.00 20.76 ? 453 SER B N   1 
ATOM   5235 C  CA  . SER B  1 263 ? 102.451 47.112  27.034 1.00 21.95 ? 453 SER B CA  1 
ATOM   5236 C  C   . SER B  1 263 ? 102.687 47.346  25.549 1.00 22.53 ? 453 SER B C   1 
ATOM   5237 O  O   . SER B  1 263 ? 102.343 48.396  25.009 1.00 21.70 ? 453 SER B O   1 
ATOM   5238 C  CB  . SER B  1 263 ? 101.082 46.470  27.240 1.00 18.66 ? 453 SER B CB  1 
ATOM   5239 O  OG  . SER B  1 263 ? 100.914 46.072  28.588 1.00 31.67 ? 453 SER B OG  1 
ATOM   5240 N  N   . LYS B  1 264 ? 103.287 46.357  24.899 1.00 24.66 ? 454 LYS B N   1 
ATOM   5241 C  CA  . LYS B  1 264 ? 103.575 46.435  23.476 1.00 27.71 ? 454 LYS B CA  1 
ATOM   5242 C  C   . LYS B  1 264 ? 102.301 46.861  22.751 1.00 30.18 ? 454 LYS B C   1 
ATOM   5243 O  O   . LYS B  1 264 ? 101.224 46.325  23.015 1.00 26.29 ? 454 LYS B O   1 
ATOM   5244 C  CB  . LYS B  1 264 ? 104.021 45.067  22.947 1.00 31.43 ? 454 LYS B CB  1 
ATOM   5245 C  CG  . LYS B  1 264 ? 105.212 44.423  23.669 1.00 36.07 ? 454 LYS B CG  1 
ATOM   5246 C  CD  . LYS B  1 264 ? 104.970 44.208  25.170 1.00 35.50 ? 454 LYS B CD  1 
ATOM   5247 C  CE  . LYS B  1 264 ? 103.696 43.426  25.461 1.00 26.21 ? 454 LYS B CE  1 
ATOM   5248 N  NZ  . LYS B  1 264 ? 103.723 42.058  24.881 1.00 29.12 ? 454 LYS B NZ  1 
ATOM   5249 N  N   . SER B  1 265 ? 102.420 47.830  21.850 1.00 29.67 ? 455 SER B N   1 
ATOM   5250 C  CA  . SER B  1 265 ? 101.266 48.289  21.089 1.00 26.63 ? 455 SER B CA  1 
ATOM   5251 C  C   . SER B  1 265 ? 100.548 47.080  20.499 1.00 27.90 ? 455 SER B C   1 
ATOM   5252 O  O   . SER B  1 265 ? 101.180 46.080  20.146 1.00 23.92 ? 455 SER B O   1 
ATOM   5253 C  CB  . SER B  1 265 ? 101.708 49.218  19.959 1.00 27.66 ? 455 SER B CB  1 
ATOM   5254 O  OG  . SER B  1 265 ? 100.624 49.528  19.100 1.00 28.25 ? 455 SER B OG  1 
ATOM   5255 N  N   . GLY B  1 266 ? 99.225  47.170  20.405 1.00 27.57 ? 456 GLY B N   1 
ATOM   5256 C  CA  . GLY B  1 266 ? 98.456  46.074  19.852 1.00 24.93 ? 456 GLY B CA  1 
ATOM   5257 C  C   . GLY B  1 266 ? 98.319  44.861  20.755 1.00 26.84 ? 456 GLY B C   1 
ATOM   5258 O  O   . GLY B  1 266 ? 97.907  43.799  20.294 1.00 28.42 ? 456 GLY B O   1 
ATOM   5259 N  N   . THR B  1 267 ? 98.664  44.992  22.031 1.00 27.97 ? 457 THR B N   1 
ATOM   5260 C  CA  . THR B  1 267 ? 98.522  43.859  22.939 1.00 33.82 ? 457 THR B CA  1 
ATOM   5261 C  C   . THR B  1 267 ? 97.162  43.910  23.626 1.00 34.97 ? 457 THR B C   1 
ATOM   5262 O  O   . THR B  1 267 ? 96.877  44.805  24.426 1.00 35.42 ? 457 THR B O   1 
ATOM   5263 C  CB  . THR B  1 267 ? 99.636  43.816  24.019 1.00 35.87 ? 457 THR B CB  1 
ATOM   5264 O  OG1 . THR B  1 267 ? 99.706  45.073  24.698 1.00 46.23 ? 457 THR B OG1 1 
ATOM   5265 C  CG2 . THR B  1 267 ? 100.979 43.501  23.386 1.00 37.16 ? 457 THR B CG2 1 
ATOM   5266 N  N   . GLU B  1 268 ? 96.323  42.940  23.283 1.00 31.66 ? 458 GLU B N   1 
ATOM   5267 C  CA  . GLU B  1 268 ? 94.982  42.822  23.833 1.00 29.51 ? 458 GLU B CA  1 
ATOM   5268 C  C   . GLU B  1 268 ? 94.962  43.041  25.343 1.00 27.06 ? 458 GLU B C   1 
ATOM   5269 O  O   . GLU B  1 268 ? 95.710  42.399  26.077 1.00 19.65 ? 458 GLU B O   1 
ATOM   5270 C  CB  . GLU B  1 268 ? 94.431  41.439  23.497 1.00 27.45 ? 458 GLU B CB  1 
ATOM   5271 C  CG  . GLU B  1 268 ? 93.080  41.129  24.091 1.00 34.22 ? 458 GLU B CG  1 
ATOM   5272 C  CD  . GLU B  1 268 ? 92.650  39.710  23.794 1.00 36.86 ? 458 GLU B CD  1 
ATOM   5273 O  OE1 . GLU B  1 268 ? 92.486  39.377  22.598 1.00 35.06 ? 458 GLU B OE1 1 
ATOM   5274 O  OE2 . GLU B  1 268 ? 92.484  38.930  24.756 1.00 37.64 ? 458 GLU B OE2 1 
ATOM   5275 N  N   . CYS B  1 269 ? 94.104  43.950  25.802 1.00 30.24 ? 459 CYS B N   1 
ATOM   5276 C  CA  . CYS B  1 269 ? 93.997  44.239  27.228 1.00 27.25 ? 459 CYS B CA  1 
ATOM   5277 C  C   . CYS B  1 269 ? 92.603  43.996  27.798 1.00 28.37 ? 459 CYS B C   1 
ATOM   5278 O  O   . CYS B  1 269 ? 92.361  44.223  28.983 1.00 32.74 ? 459 CYS B O   1 
ATOM   5279 C  CB  . CYS B  1 269 ? 94.435  45.672  27.517 1.00 22.01 ? 459 CYS B CB  1 
ATOM   5280 S  SG  . CYS B  1 269 ? 93.568  46.984  26.603 1.00 31.94 ? 459 CYS B SG  1 
ATOM   5281 N  N   . ARG B  1 270 ? 91.683  43.556  26.947 1.00 27.11 ? 460 ARG B N   1 
ATOM   5282 C  CA  . ARG B  1 270 ? 90.329  43.230  27.378 1.00 23.62 ? 460 ARG B CA  1 
ATOM   5283 C  C   . ARG B  1 270 ? 89.761  42.201  26.412 1.00 25.79 ? 460 ARG B C   1 
ATOM   5284 O  O   . ARG B  1 270 ? 89.367  42.529  25.288 1.00 19.35 ? 460 ARG B O   1 
ATOM   5285 C  CB  . ARG B  1 270 ? 89.423  44.460  27.419 1.00 23.78 ? 460 ARG B CB  1 
ATOM   5286 C  CG  . ARG B  1 270 ? 88.037  44.121  27.969 1.00 25.20 ? 460 ARG B CG  1 
ATOM   5287 C  CD  . ARG B  1 270 ? 87.091  45.307  28.013 1.00 24.95 ? 460 ARG B CD  1 
ATOM   5288 N  NE  . ARG B  1 270 ? 87.483  46.311  28.998 1.00 23.96 ? 460 ARG B NE  1 
ATOM   5289 C  CZ  . ARG B  1 270 ? 87.991  47.500  28.689 1.00 25.37 ? 460 ARG B CZ  1 
ATOM   5290 N  NH1 . ARG B  1 270 ? 88.172  47.835  27.420 1.00 24.66 ? 460 ARG B NH1 1 
ATOM   5291 N  NH2 . ARG B  1 270 ? 88.313  48.357  29.649 1.00 20.54 ? 460 ARG B NH2 1 
ATOM   5292 N  N   . ALA B  1 271 ? 89.738  40.952  26.867 1.00 26.29 ? 461 ALA B N   1 
ATOM   5293 C  CA  . ALA B  1 271 ? 89.254  39.827  26.078 1.00 25.63 ? 461 ALA B CA  1 
ATOM   5294 C  C   . ALA B  1 271 ? 87.851  40.013  25.509 1.00 28.30 ? 461 ALA B C   1 
ATOM   5295 O  O   . ALA B  1 271 ? 86.992  40.659  26.114 1.00 27.24 ? 461 ALA B O   1 
ATOM   5296 C  CB  . ALA B  1 271 ? 89.308  38.558  26.912 1.00 24.66 ? 461 ALA B CB  1 
ATOM   5297 N  N   . SER B  1 272 ? 87.636  39.423  24.337 1.00 27.21 ? 462 SER B N   1 
ATOM   5298 C  CA  . SER B  1 272 ? 86.359  39.494  23.644 1.00 25.25 ? 462 SER B CA  1 
ATOM   5299 C  C   . SER B  1 272 ? 85.396  38.407  24.115 1.00 27.83 ? 462 SER B C   1 
ATOM   5300 O  O   . SER B  1 272 ? 85.737  37.221  24.127 1.00 25.95 ? 462 SER B O   1 
ATOM   5301 C  CB  . SER B  1 272 ? 86.586  39.363  22.137 1.00 23.37 ? 462 SER B CB  1 
ATOM   5302 O  OG  . SER B  1 272 ? 85.362  39.200  21.443 1.00 27.16 ? 462 SER B OG  1 
ATOM   5303 N  N   . MET B  1 273 ? 84.191  38.823  24.500 1.00 31.79 ? 463 MET B N   1 
ATOM   5304 C  CA  . MET B  1 273 ? 83.163  37.898  24.969 1.00 32.34 ? 463 MET B CA  1 
ATOM   5305 C  C   . MET B  1 273 ? 82.654  37.076  23.788 1.00 30.80 ? 463 MET B C   1 
ATOM   5306 O  O   . MET B  1 273 ? 82.760  35.848  23.776 1.00 29.28 ? 463 MET B O   1 
ATOM   5307 C  CB  . MET B  1 273 ? 81.999  38.677  25.595 1.00 36.57 ? 463 MET B CB  1 
ATOM   5308 C  CG  . MET B  1 273 ? 82.411  39.695  26.657 1.00 38.52 ? 463 MET B CG  1 
ATOM   5309 S  SD  . MET B  1 273 ? 80.997  40.615  27.344 1.00 48.14 ? 463 MET B SD  1 
ATOM   5310 C  CE  . MET B  1 273 ? 80.953  39.988  29.022 1.00 44.04 ? 463 MET B CE  1 
ATOM   5311 N  N   . SER B  1 274 ? 82.103  37.775  22.800 1.00 27.72 ? 464 SER B N   1 
ATOM   5312 C  CA  . SER B  1 274 ? 81.568  37.161  21.588 1.00 24.31 ? 464 SER B CA  1 
ATOM   5313 C  C   . SER B  1 274 ? 81.829  38.102  20.414 1.00 27.38 ? 464 SER B C   1 
ATOM   5314 O  O   . SER B  1 274 ? 82.469  39.141  20.579 1.00 29.01 ? 464 SER B O   1 
ATOM   5315 C  CB  . SER B  1 274 ? 80.059  36.928  21.727 1.00 26.76 ? 464 SER B CB  1 
ATOM   5316 O  OG  . SER B  1 274 ? 79.346  38.152  21.837 1.00 7.69  ? 464 SER B OG  1 
ATOM   5317 N  N   . GLU B  1 275 ? 81.328  37.748  19.234 1.00 28.17 ? 465 GLU B N   1 
ATOM   5318 C  CA  . GLU B  1 275 ? 81.520  38.586  18.053 1.00 28.78 ? 465 GLU B CA  1 
ATOM   5319 C  C   . GLU B  1 275 ? 80.944  39.984  18.254 1.00 27.29 ? 465 GLU B C   1 
ATOM   5320 O  O   . GLU B  1 275 ? 81.343  40.929  17.576 1.00 30.83 ? 465 GLU B O   1 
ATOM   5321 C  CB  . GLU B  1 275 ? 80.881  37.933  16.826 1.00 26.91 ? 465 GLU B CB  1 
ATOM   5322 C  CG  . GLU B  1 275 ? 79.405  37.619  16.975 1.00 32.03 ? 465 GLU B CG  1 
ATOM   5323 C  CD  . GLU B  1 275 ? 78.871  36.798  15.814 1.00 33.70 ? 465 GLU B CD  1 
ATOM   5324 O  OE1 . GLU B  1 275 ? 78.703  37.357  14.707 1.00 30.84 ? 465 GLU B OE1 1 
ATOM   5325 O  OE2 . GLU B  1 275 ? 78.630  35.587  16.008 1.00 33.54 ? 465 GLU B OE2 1 
ATOM   5326 N  N   . CYS B  1 276 ? 80.017  40.111  19.198 1.00 28.14 ? 466 CYS B N   1 
ATOM   5327 C  CA  . CYS B  1 276 ? 79.382  41.394  19.496 1.00 25.21 ? 466 CYS B CA  1 
ATOM   5328 C  C   . CYS B  1 276 ? 80.248  42.276  20.383 1.00 20.75 ? 466 CYS B C   1 
ATOM   5329 O  O   . CYS B  1 276 ? 79.877  43.410  20.694 1.00 17.66 ? 466 CYS B O   1 
ATOM   5330 C  CB  . CYS B  1 276 ? 78.048  41.177  20.203 1.00 20.80 ? 466 CYS B CB  1 
ATOM   5331 S  SG  . CYS B  1 276 ? 76.798  40.269  19.252 1.00 27.53 ? 466 CYS B SG  1 
ATOM   5332 N  N   . ASP B  1 277 ? 81.392  41.751  20.802 1.00 15.98 ? 467 ASP B N   1 
ATOM   5333 C  CA  . ASP B  1 277 ? 82.290  42.502  21.666 1.00 16.19 ? 467 ASP B CA  1 
ATOM   5334 C  C   . ASP B  1 277 ? 83.708  42.547  21.100 1.00 18.22 ? 467 ASP B C   1 
ATOM   5335 O  O   . ASP B  1 277 ? 84.514  41.649  21.346 1.00 23.45 ? 467 ASP B O   1 
ATOM   5336 C  CB  . ASP B  1 277 ? 82.311  41.867  23.056 1.00 16.67 ? 467 ASP B CB  1 
ATOM   5337 C  CG  . ASP B  1 277 ? 83.103  42.677  24.056 1.00 19.39 ? 467 ASP B CG  1 
ATOM   5338 O  OD1 . ASP B  1 277 ? 83.337  42.172  25.176 1.00 22.28 ? 467 ASP B OD1 1 
ATOM   5339 O  OD2 . ASP B  1 277 ? 83.487  43.819  23.724 1.00 24.55 ? 467 ASP B OD2 1 
ATOM   5340 N  N   . PRO B  1 278 ? 84.029  43.590  20.323 1.00 13.15 ? 468 PRO B N   1 
ATOM   5341 C  CA  . PRO B  1 278 ? 85.378  43.671  19.766 1.00 11.38 ? 468 PRO B CA  1 
ATOM   5342 C  C   . PRO B  1 278 ? 86.353  43.938  20.904 1.00 14.93 ? 468 PRO B C   1 
ATOM   5343 O  O   . PRO B  1 278 ? 86.103  44.788  21.761 1.00 15.83 ? 468 PRO B O   1 
ATOM   5344 C  CB  . PRO B  1 278 ? 85.274  44.842  18.801 1.00 12.29 ? 468 PRO B CB  1 
ATOM   5345 C  CG  . PRO B  1 278 ? 84.326  45.758  19.524 1.00 16.12 ? 468 PRO B CG  1 
ATOM   5346 C  CD  . PRO B  1 278 ? 83.250  44.796  19.996 1.00 15.15 ? 468 PRO B CD  1 
ATOM   5347 N  N   . ALA B  1 279 ? 87.459  43.208  20.920 1.00 14.80 ? 469 ALA B N   1 
ATOM   5348 C  CA  . ALA B  1 279 ? 88.448  43.374  21.975 1.00 18.96 ? 469 ALA B CA  1 
ATOM   5349 C  C   . ALA B  1 279 ? 89.222  44.683  21.846 1.00 18.36 ? 469 ALA B C   1 
ATOM   5350 O  O   . ALA B  1 279 ? 89.356  45.233  20.755 1.00 21.65 ? 469 ALA B O   1 
ATOM   5351 C  CB  . ALA B  1 279 ? 89.413  42.192  21.967 1.00 13.40 ? 469 ALA B CB  1 
ATOM   5352 N  N   . GLU B  1 280 ? 89.715  45.184  22.974 1.00 21.14 ? 470 GLU B N   1 
ATOM   5353 C  CA  . GLU B  1 280 ? 90.507  46.407  22.992 1.00 21.88 ? 470 GLU B CA  1 
ATOM   5354 C  C   . GLU B  1 280 ? 91.973  46.004  23.113 1.00 24.08 ? 470 GLU B C   1 
ATOM   5355 O  O   . GLU B  1 280 ? 92.292  44.943  23.653 1.00 21.54 ? 470 GLU B O   1 
ATOM   5356 C  CB  . GLU B  1 280 ? 90.114  47.302  24.171 1.00 18.72 ? 470 GLU B CB  1 
ATOM   5357 C  CG  . GLU B  1 280 ? 88.737  47.940  24.040 1.00 21.50 ? 470 GLU B CG  1 
ATOM   5358 C  CD  . GLU B  1 280 ? 87.608  46.942  24.187 1.00 21.96 ? 470 GLU B CD  1 
ATOM   5359 O  OE1 . GLU B  1 280 ? 86.462  47.290  23.845 1.00 22.83 ? 470 GLU B OE1 1 
ATOM   5360 O  OE2 . GLU B  1 280 ? 87.860  45.812  24.652 1.00 29.42 ? 470 GLU B OE2 1 
ATOM   5361 N  N   . HIS B  1 281 ? 92.863  46.851  22.612 1.00 26.32 ? 471 HIS B N   1 
ATOM   5362 C  CA  . HIS B  1 281 ? 94.288  46.555  22.656 1.00 28.97 ? 471 HIS B CA  1 
ATOM   5363 C  C   . HIS B  1 281 ? 95.060  47.770  23.150 1.00 28.96 ? 471 HIS B C   1 
ATOM   5364 O  O   . HIS B  1 281 ? 94.659  48.909  22.903 1.00 26.70 ? 471 HIS B O   1 
ATOM   5365 C  CB  . HIS B  1 281 ? 94.762  46.165  21.257 1.00 30.98 ? 471 HIS B CB  1 
ATOM   5366 C  CG  . HIS B  1 281 ? 93.866  45.178  20.577 1.00 35.66 ? 471 HIS B CG  1 
ATOM   5367 N  ND1 . HIS B  1 281 ? 93.787  43.857  20.960 1.00 39.41 ? 471 HIS B ND1 1 
ATOM   5368 C  CD2 . HIS B  1 281 ? 92.980  45.331  19.565 1.00 38.52 ? 471 HIS B CD2 1 
ATOM   5369 C  CE1 . HIS B  1 281 ? 92.891  43.236  20.212 1.00 37.85 ? 471 HIS B CE1 1 
ATOM   5370 N  NE2 . HIS B  1 281 ? 92.387  44.109  19.358 1.00 40.74 ? 471 HIS B NE2 1 
ATOM   5371 N  N   . CYS B  1 282 ? 96.164  47.530  23.851 1.00 26.01 ? 472 CYS B N   1 
ATOM   5372 C  CA  . CYS B  1 282 ? 96.962  48.632  24.361 1.00 25.75 ? 472 CYS B CA  1 
ATOM   5373 C  C   . CYS B  1 282 ? 97.522  49.447  23.203 1.00 25.16 ? 472 CYS B C   1 
ATOM   5374 O  O   . CYS B  1 282 ? 97.901  48.895  22.168 1.00 24.36 ? 472 CYS B O   1 
ATOM   5375 C  CB  . CYS B  1 282 ? 98.100  48.111  25.234 1.00 22.35 ? 472 CYS B CB  1 
ATOM   5376 S  SG  . CYS B  1 282 ? 97.541  47.067  26.615 1.00 36.46 ? 472 CYS B SG  1 
ATOM   5377 N  N   . THR B  1 283 ? 97.558  50.763  23.381 1.00 22.34 ? 473 THR B N   1 
ATOM   5378 C  CA  . THR B  1 283 ? 98.070  51.665  22.358 1.00 25.35 ? 473 THR B CA  1 
ATOM   5379 C  C   . THR B  1 283 ? 99.583  51.546  22.219 1.00 25.39 ? 473 THR B C   1 
ATOM   5380 O  O   . THR B  1 283 ? 100.147 51.887  21.185 1.00 24.40 ? 473 THR B O   1 
ATOM   5381 C  CB  . THR B  1 283 ? 97.731  53.127  22.695 1.00 29.54 ? 473 THR B CB  1 
ATOM   5382 O  OG1 . THR B  1 283 ? 98.232  53.445  24.001 1.00 35.47 ? 473 THR B OG1 1 
ATOM   5383 C  CG2 . THR B  1 283 ? 96.228  53.345  22.666 1.00 33.57 ? 473 THR B CG2 1 
ATOM   5384 N  N   . GLY B  1 284 ? 100.235 51.058  23.268 1.00 30.23 ? 474 GLY B N   1 
ATOM   5385 C  CA  . GLY B  1 284 ? 101.678 50.915  23.237 1.00 32.29 ? 474 GLY B CA  1 
ATOM   5386 C  C   . GLY B  1 284 ? 102.335 52.146  23.824 1.00 35.14 ? 474 GLY B C   1 
ATOM   5387 O  O   . GLY B  1 284 ? 103.547 52.179  24.041 1.00 35.38 ? 474 GLY B O   1 
ATOM   5388 N  N   . GLN B  1 285 ? 101.521 53.164  24.084 1.00 36.47 ? 475 GLN B N   1 
ATOM   5389 C  CA  . GLN B  1 285 ? 102.002 54.415  24.650 1.00 40.80 ? 475 GLN B CA  1 
ATOM   5390 C  C   . GLN B  1 285 ? 101.149 54.835  25.847 1.00 39.56 ? 475 GLN B C   1 
ATOM   5391 O  O   . GLN B  1 285 ? 101.170 55.995  26.259 1.00 37.72 ? 475 GLN B O   1 
ATOM   5392 C  CB  . GLN B  1 285 ? 101.967 55.514  23.588 1.00 43.43 ? 475 GLN B CB  1 
ATOM   5393 C  CG  . GLN B  1 285 ? 100.579 55.768  23.031 1.00 52.30 ? 475 GLN B CG  1 
ATOM   5394 C  CD  . GLN B  1 285 ? 100.513 57.009  22.165 1.00 57.33 ? 475 GLN B CD  1 
ATOM   5395 O  OE1 . GLN B  1 285 ? 99.455  57.352  21.632 1.00 60.79 ? 475 GLN B OE1 1 
ATOM   5396 N  NE2 . GLN B  1 285 ? 101.643 57.692  22.021 1.00 58.55 ? 475 GLN B NE2 1 
ATOM   5397 N  N   . SER B  1 286 ? 100.398 53.889  26.401 1.00 38.61 ? 476 SER B N   1 
ATOM   5398 C  CA  . SER B  1 286 ? 99.541  54.166  27.548 1.00 34.88 ? 476 SER B CA  1 
ATOM   5399 C  C   . SER B  1 286 ? 99.455  52.950  28.463 1.00 32.80 ? 476 SER B C   1 
ATOM   5400 O  O   . SER B  1 286 ? 99.539  51.813  28.006 1.00 32.59 ? 476 SER B O   1 
ATOM   5401 C  CB  . SER B  1 286 ? 98.138  54.551  27.071 1.00 35.94 ? 476 SER B CB  1 
ATOM   5402 O  OG  . SER B  1 286 ? 97.266  54.777  28.167 1.00 41.46 ? 476 SER B OG  1 
ATOM   5403 N  N   . SER B  1 287 ? 99.283  53.191  29.757 1.00 31.33 ? 477 SER B N   1 
ATOM   5404 C  CA  . SER B  1 287 ? 99.189  52.098  30.714 1.00 32.69 ? 477 SER B CA  1 
ATOM   5405 C  C   . SER B  1 287 ? 97.737  51.697  30.946 1.00 33.84 ? 477 SER B C   1 
ATOM   5406 O  O   . SER B  1 287 ? 97.455  50.710  31.630 1.00 33.24 ? 477 SER B O   1 
ATOM   5407 C  CB  . SER B  1 287 ? 99.822  52.505  32.044 1.00 30.12 ? 477 SER B CB  1 
ATOM   5408 O  OG  . SER B  1 287 ? 99.132  53.600  32.617 1.00 32.14 ? 477 SER B OG  1 
ATOM   5409 N  N   . GLU B  1 288 ? 96.816  52.459  30.369 1.00 32.87 ? 478 GLU B N   1 
ATOM   5410 C  CA  . GLU B  1 288 ? 95.400  52.174  30.539 1.00 34.94 ? 478 GLU B CA  1 
ATOM   5411 C  C   . GLU B  1 288 ? 94.735  51.587  29.303 1.00 30.90 ? 478 GLU B C   1 
ATOM   5412 O  O   . GLU B  1 288 ? 94.937  52.056  28.183 1.00 28.43 ? 478 GLU B O   1 
ATOM   5413 C  CB  . GLU B  1 288 ? 94.661  53.443  30.970 1.00 43.75 ? 478 GLU B CB  1 
ATOM   5414 C  CG  . GLU B  1 288 ? 95.141  53.991  32.300 1.00 49.38 ? 478 GLU B CG  1 
ATOM   5415 C  CD  . GLU B  1 288 ? 94.946  53.004  33.433 1.00 52.70 ? 478 GLU B CD  1 
ATOM   5416 O  OE1 . GLU B  1 288 ? 95.555  53.203  34.505 1.00 56.16 ? 478 GLU B OE1 1 
ATOM   5417 O  OE2 . GLU B  1 288 ? 94.179  52.032  33.254 1.00 51.78 ? 478 GLU B OE2 1 
ATOM   5418 N  N   . CYS B  1 289 ? 93.938  50.550  29.529 1.00 28.29 ? 479 CYS B N   1 
ATOM   5419 C  CA  . CYS B  1 289 ? 93.212  49.872  28.467 1.00 25.41 ? 479 CYS B CA  1 
ATOM   5420 C  C   . CYS B  1 289 ? 92.095  50.798  27.991 1.00 23.51 ? 479 CYS B C   1 
ATOM   5421 O  O   . CYS B  1 289 ? 91.315  51.308  28.798 1.00 21.03 ? 479 CYS B O   1 
ATOM   5422 C  CB  . CYS B  1 289 ? 92.622  48.572  29.012 1.00 26.13 ? 479 CYS B CB  1 
ATOM   5423 S  SG  . CYS B  1 289 ? 91.962  47.406  27.778 1.00 35.61 ? 479 CYS B SG  1 
ATOM   5424 N  N   . PRO B  1 290 ? 92.009  51.036  26.673 1.00 20.86 ? 480 PRO B N   1 
ATOM   5425 C  CA  . PRO B  1 290 ? 90.964  51.917  26.141 1.00 18.25 ? 480 PRO B CA  1 
ATOM   5426 C  C   . PRO B  1 290 ? 89.549  51.445  26.473 1.00 17.70 ? 480 PRO B C   1 
ATOM   5427 O  O   . PRO B  1 290 ? 89.313  50.251  26.660 1.00 16.24 ? 480 PRO B O   1 
ATOM   5428 C  CB  . PRO B  1 290 ? 91.258  51.933  24.642 1.00 14.88 ? 480 PRO B CB  1 
ATOM   5429 C  CG  . PRO B  1 290 ? 91.906  50.605  24.407 1.00 22.36 ? 480 PRO B CG  1 
ATOM   5430 C  CD  . PRO B  1 290 ? 92.828  50.477  25.585 1.00 16.19 ? 480 PRO B CD  1 
ATOM   5431 N  N   . ALA B  1 291 ? 88.620  52.396  26.552 1.00 17.29 ? 481 ALA B N   1 
ATOM   5432 C  CA  . ALA B  1 291 ? 87.220  52.116  26.873 1.00 14.42 ? 481 ALA B CA  1 
ATOM   5433 C  C   . ALA B  1 291 ? 86.690  50.867  26.179 1.00 15.40 ? 481 ALA B C   1 
ATOM   5434 O  O   . ALA B  1 291 ? 87.145  50.508  25.091 1.00 14.49 ? 481 ALA B O   1 
ATOM   5435 C  CB  . ALA B  1 291 ? 86.359  53.310  26.506 1.00 12.42 ? 481 ALA B CB  1 
ATOM   5436 N  N   . ASP B  1 292 ? 85.723  50.209  26.815 1.00 14.04 ? 482 ASP B N   1 
ATOM   5437 C  CA  . ASP B  1 292 ? 85.142  48.996  26.250 1.00 16.17 ? 482 ASP B CA  1 
ATOM   5438 C  C   . ASP B  1 292 ? 84.093  49.305  25.187 1.00 16.39 ? 482 ASP B C   1 
ATOM   5439 O  O   . ASP B  1 292 ? 83.101  49.986  25.444 1.00 20.00 ? 482 ASP B O   1 
ATOM   5440 C  CB  . ASP B  1 292 ? 84.526  48.131  27.353 1.00 15.16 ? 482 ASP B CB  1 
ATOM   5441 C  CG  . ASP B  1 292 ? 84.176  46.731  26.870 1.00 22.18 ? 482 ASP B CG  1 
ATOM   5442 O  OD1 . ASP B  1 292 ? 84.647  46.340  25.780 1.00 18.46 ? 482 ASP B OD1 1 
ATOM   5443 O  OD2 . ASP B  1 292 ? 83.440  46.016  27.585 1.00 24.00 ? 482 ASP B OD2 1 
ATOM   5444 N  N   . VAL B  1 293 ? 84.333  48.796  23.986 1.00 15.67 ? 483 VAL B N   1 
ATOM   5445 C  CA  . VAL B  1 293 ? 83.432  48.994  22.864 1.00 12.36 ? 483 VAL B CA  1 
ATOM   5446 C  C   . VAL B  1 293 ? 82.659  47.711  22.565 1.00 16.24 ? 483 VAL B C   1 
ATOM   5447 O  O   . VAL B  1 293 ? 83.214  46.609  22.581 1.00 12.25 ? 483 VAL B O   1 
ATOM   5448 C  CB  . VAL B  1 293 ? 84.216  49.410  21.578 1.00 14.39 ? 483 VAL B CB  1 
ATOM   5449 C  CG1 . VAL B  1 293 ? 83.273  49.488  20.385 1.00 1.00  ? 483 VAL B CG1 1 
ATOM   5450 C  CG2 . VAL B  1 293 ? 84.905  50.751  21.789 1.00 8.01  ? 483 VAL B CG2 1 
ATOM   5451 N  N   . PHE B  1 294 ? 81.367  47.872  22.310 1.00 17.24 ? 484 PHE B N   1 
ATOM   5452 C  CA  . PHE B  1 294 ? 80.492  46.764  21.959 1.00 15.25 ? 484 PHE B CA  1 
ATOM   5453 C  C   . PHE B  1 294 ? 79.988  47.143  20.583 1.00 15.40 ? 484 PHE B C   1 
ATOM   5454 O  O   . PHE B  1 294 ? 79.998  48.319  20.230 1.00 15.76 ? 484 PHE B O   1 
ATOM   5455 C  CB  . PHE B  1 294 ? 79.276  46.697  22.888 1.00 16.69 ? 484 PHE B CB  1 
ATOM   5456 C  CG  . PHE B  1 294 ? 79.573  46.208  24.273 1.00 19.07 ? 484 PHE B CG  1 
ATOM   5457 C  CD1 . PHE B  1 294 ? 78.621  46.354  25.279 1.00 15.42 ? 484 PHE B CD1 1 
ATOM   5458 C  CD2 . PHE B  1 294 ? 80.779  45.587  24.577 1.00 25.43 ? 484 PHE B CD2 1 
ATOM   5459 C  CE1 . PHE B  1 294 ? 78.863  45.892  26.563 1.00 22.68 ? 484 PHE B CE1 1 
ATOM   5460 C  CE2 . PHE B  1 294 ? 81.033  45.119  25.865 1.00 27.33 ? 484 PHE B CE2 1 
ATOM   5461 C  CZ  . PHE B  1 294 ? 80.072  45.272  26.859 1.00 25.02 ? 484 PHE B CZ  1 
ATOM   5462 N  N   . HIS B  1 295 ? 79.562  46.167  19.795 1.00 14.15 ? 485 HIS B N   1 
ATOM   5463 C  CA  . HIS B  1 295 ? 78.996  46.503  18.502 1.00 15.76 ? 485 HIS B CA  1 
ATOM   5464 C  C   . HIS B  1 295 ? 77.577  46.958  18.827 1.00 14.66 ? 485 HIS B C   1 
ATOM   5465 O  O   . HIS B  1 295 ? 77.143  46.856  19.972 1.00 14.43 ? 485 HIS B O   1 
ATOM   5466 C  CB  . HIS B  1 295 ? 79.013  45.293  17.579 1.00 19.31 ? 485 HIS B CB  1 
ATOM   5467 C  CG  . HIS B  1 295 ? 80.363  45.023  16.992 1.00 28.77 ? 485 HIS B CG  1 
ATOM   5468 N  ND1 . HIS B  1 295 ? 80.685  43.838  16.366 1.00 34.83 ? 485 HIS B ND1 1 
ATOM   5469 C  CD2 . HIS B  1 295 ? 81.475  45.794  16.931 1.00 27.17 ? 485 HIS B CD2 1 
ATOM   5470 C  CE1 . HIS B  1 295 ? 81.937  43.891  15.946 1.00 33.69 ? 485 HIS B CE1 1 
ATOM   5471 N  NE2 . HIS B  1 295 ? 82.438  45.068  16.276 1.00 28.53 ? 485 HIS B NE2 1 
ATOM   5472 N  N   . LYS B  1 296 ? 76.855  47.472  17.844 1.00 14.45 ? 486 LYS B N   1 
ATOM   5473 C  CA  . LYS B  1 296 ? 75.507  47.964  18.103 1.00 13.50 ? 486 LYS B CA  1 
ATOM   5474 C  C   . LYS B  1 296 ? 74.492  46.883  18.451 1.00 10.63 ? 486 LYS B C   1 
ATOM   5475 O  O   . LYS B  1 296 ? 74.535  45.775  17.916 1.00 12.32 ? 486 LYS B O   1 
ATOM   5476 C  CB  . LYS B  1 296 ? 75.006  48.760  16.899 1.00 12.60 ? 486 LYS B CB  1 
ATOM   5477 C  CG  . LYS B  1 296 ? 75.875  49.942  16.532 1.00 13.22 ? 486 LYS B CG  1 
ATOM   5478 C  CD  . LYS B  1 296 ? 75.358  50.607  15.268 1.00 18.91 ? 486 LYS B CD  1 
ATOM   5479 C  CE  . LYS B  1 296 ? 76.180  51.827  14.911 1.00 19.30 ? 486 LYS B CE  1 
ATOM   5480 N  NZ  . LYS B  1 296 ? 75.608  52.532  13.738 1.00 24.89 ? 486 LYS B NZ  1 
ATOM   5481 N  N   . ASN B  1 297 ? 73.581  47.214  19.360 1.00 11.41 ? 487 ASN B N   1 
ATOM   5482 C  CA  . ASN B  1 297 ? 72.530  46.282  19.753 1.00 14.68 ? 487 ASN B CA  1 
ATOM   5483 C  C   . ASN B  1 297 ? 71.606  46.096  18.554 1.00 13.88 ? 487 ASN B C   1 
ATOM   5484 O  O   . ASN B  1 297 ? 71.254  47.066  17.879 1.00 14.63 ? 487 ASN B O   1 
ATOM   5485 C  CB  . ASN B  1 297 ? 71.745  46.830  20.947 1.00 10.69 ? 487 ASN B CB  1 
ATOM   5486 C  CG  . ASN B  1 297 ? 72.514  46.710  22.251 1.00 20.89 ? 487 ASN B CG  1 
ATOM   5487 O  OD1 . ASN B  1 297 ? 72.101  47.246  23.282 1.00 23.36 ? 487 ASN B OD1 1 
ATOM   5488 N  ND2 . ASN B  1 297 ? 73.637  45.993  22.214 1.00 16.33 ? 487 ASN B ND2 1 
ATOM   5489 N  N   . GLY B  1 298 ? 71.225  44.850  18.287 1.00 9.37  ? 488 GLY B N   1 
ATOM   5490 C  CA  . GLY B  1 298 ? 70.366  44.573  17.152 1.00 9.88  ? 488 GLY B CA  1 
ATOM   5491 C  C   . GLY B  1 298 ? 71.193  44.027  16.009 1.00 12.87 ? 488 GLY B C   1 
ATOM   5492 O  O   . GLY B  1 298 ? 70.670  43.415  15.078 1.00 16.46 ? 488 GLY B O   1 
ATOM   5493 N  N   . GLN B  1 299 ? 72.499  44.266  16.082 1.00 18.46 ? 489 GLN B N   1 
ATOM   5494 C  CA  . GLN B  1 299 ? 73.443  43.794  15.076 1.00 18.39 ? 489 GLN B CA  1 
ATOM   5495 C  C   . GLN B  1 299 ? 73.340  42.269  14.979 1.00 17.98 ? 489 GLN B C   1 
ATOM   5496 O  O   . GLN B  1 299 ? 73.788  41.554  15.873 1.00 20.35 ? 489 GLN B O   1 
ATOM   5497 C  CB  . GLN B  1 299 ? 74.860  44.208  15.486 1.00 18.13 ? 489 GLN B CB  1 
ATOM   5498 C  CG  . GLN B  1 299 ? 75.984  43.398  14.856 1.00 17.18 ? 489 GLN B CG  1 
ATOM   5499 C  CD  . GLN B  1 299 ? 76.274  43.803  13.435 1.00 19.29 ? 489 GLN B CD  1 
ATOM   5500 O  OE1 . GLN B  1 299 ? 76.706  44.928  13.176 1.00 20.11 ? 489 GLN B OE1 1 
ATOM   5501 N  NE2 . GLN B  1 299 ? 76.041  42.888  12.499 1.00 20.93 ? 489 GLN B NE2 1 
ATOM   5502 N  N   . PRO B  1 300 ? 72.746  41.754  13.893 1.00 17.84 ? 490 PRO B N   1 
ATOM   5503 C  CA  . PRO B  1 300 ? 72.610  40.303  13.733 1.00 20.52 ? 490 PRO B CA  1 
ATOM   5504 C  C   . PRO B  1 300 ? 73.939  39.585  13.937 1.00 20.75 ? 490 PRO B C   1 
ATOM   5505 O  O   . PRO B  1 300 ? 74.967  39.988  13.392 1.00 20.60 ? 490 PRO B O   1 
ATOM   5506 C  CB  . PRO B  1 300 ? 72.059  40.159  12.313 1.00 19.71 ? 490 PRO B CB  1 
ATOM   5507 C  CG  . PRO B  1 300 ? 72.574  41.373  11.622 1.00 21.11 ? 490 PRO B CG  1 
ATOM   5508 C  CD  . PRO B  1 300 ? 72.369  42.450  12.653 1.00 22.58 ? 490 PRO B CD  1 
ATOM   5509 N  N   . CYS B  1 301 ? 73.904  38.521  14.733 1.00 19.08 ? 491 CYS B N   1 
ATOM   5510 C  CA  . CYS B  1 301 ? 75.099  37.752  15.053 1.00 17.81 ? 491 CYS B CA  1 
ATOM   5511 C  C   . CYS B  1 301 ? 74.885  36.236  14.989 1.00 21.49 ? 491 CYS B C   1 
ATOM   5512 O  O   . CYS B  1 301 ? 73.813  35.763  14.614 1.00 26.52 ? 491 CYS B O   1 
ATOM   5513 C  CB  . CYS B  1 301 ? 75.584  38.156  16.444 1.00 13.16 ? 491 CYS B CB  1 
ATOM   5514 S  SG  . CYS B  1 301 ? 74.242  38.231  17.672 1.00 18.27 ? 491 CYS B SG  1 
ATOM   5515 N  N   . LEU B  1 302 ? 75.917  35.485  15.365 1.00 23.13 ? 492 LEU B N   1 
ATOM   5516 C  CA  . LEU B  1 302 ? 75.887  34.025  15.352 1.00 24.15 ? 492 LEU B CA  1 
ATOM   5517 C  C   . LEU B  1 302 ? 75.249  33.434  14.105 1.00 27.65 ? 492 LEU B C   1 
ATOM   5518 O  O   . LEU B  1 302 ? 74.334  32.615  14.187 1.00 28.39 ? 492 LEU B O   1 
ATOM   5519 C  CB  . LEU B  1 302 ? 75.179  33.485  16.597 1.00 24.52 ? 492 LEU B CB  1 
ATOM   5520 C  CG  . LEU B  1 302 ? 76.044  33.411  17.857 1.00 25.13 ? 492 LEU B CG  1 
ATOM   5521 C  CD1 . LEU B  1 302 ? 75.223  32.869  19.024 1.00 22.71 ? 492 LEU B CD1 1 
ATOM   5522 C  CD2 . LEU B  1 302 ? 77.250  32.518  17.586 1.00 13.25 ? 492 LEU B CD2 1 
ATOM   5523 N  N   . ASP B  1 303 ? 75.746  33.855  12.949 1.00 32.50 ? 493 ASP B N   1 
ATOM   5524 C  CA  . ASP B  1 303 ? 75.247  33.367  11.671 1.00 36.50 ? 493 ASP B CA  1 
ATOM   5525 C  C   . ASP B  1 303 ? 73.728  33.506  11.551 1.00 36.73 ? 493 ASP B C   1 
ATOM   5526 O  O   . ASP B  1 303 ? 73.048  32.599  11.073 1.00 38.36 ? 493 ASP B O   1 
ATOM   5527 C  CB  . ASP B  1 303 ? 75.659  31.905  11.479 1.00 39.53 ? 493 ASP B CB  1 
ATOM   5528 C  CG  . ASP B  1 303 ? 75.424  31.412  10.063 1.00 50.25 ? 493 ASP B CG  1 
ATOM   5529 O  OD1 . ASP B  1 303 ? 75.619  30.202  9.815  1.00 53.70 ? 493 ASP B OD1 1 
ATOM   5530 O  OD2 . ASP B  1 303 ? 75.048  32.233  9.196  1.00 52.18 ? 493 ASP B OD2 1 
ATOM   5531 N  N   . ASN B  1 304 ? 73.208  34.648  11.994 1.00 36.05 ? 494 ASN B N   1 
ATOM   5532 C  CA  . ASN B  1 304 ? 71.779  34.949  11.930 1.00 37.07 ? 494 ASN B CA  1 
ATOM   5533 C  C   . ASN B  1 304 ? 70.859  34.147  12.848 1.00 36.22 ? 494 ASN B C   1 
ATOM   5534 O  O   . ASN B  1 304 ? 69.696  33.907  12.517 1.00 36.59 ? 494 ASN B O   1 
ATOM   5535 C  CB  . ASN B  1 304 ? 71.291  34.839  10.483 1.00 42.91 ? 494 ASN B CB  1 
ATOM   5536 C  CG  . ASN B  1 304 ? 71.745  36.008  9.630  1.00 51.67 ? 494 ASN B CG  1 
ATOM   5537 O  OD1 . ASN B  1 304 ? 71.293  37.138  9.819  1.00 58.18 ? 494 ASN B OD1 1 
ATOM   5538 N  ND2 . ASN B  1 304 ? 72.652  35.746  8.695  1.00 51.87 ? 494 ASN B ND2 1 
ATOM   5539 N  N   . TYR B  1 305 ? 71.375  33.738  14.001 1.00 32.04 ? 495 TYR B N   1 
ATOM   5540 C  CA  . TYR B  1 305 ? 70.570  33.002  14.965 1.00 26.83 ? 495 TYR B CA  1 
ATOM   5541 C  C   . TYR B  1 305 ? 70.220  33.912  16.131 1.00 22.59 ? 495 TYR B C   1 
ATOM   5542 O  O   . TYR B  1 305 ? 69.400  33.564  16.975 1.00 23.31 ? 495 TYR B O   1 
ATOM   5543 C  CB  . TYR B  1 305 ? 71.317  31.768  15.478 1.00 31.30 ? 495 TYR B CB  1 
ATOM   5544 C  CG  . TYR B  1 305 ? 71.074  30.511  14.669 1.00 38.29 ? 495 TYR B CG  1 
ATOM   5545 C  CD1 . TYR B  1 305 ? 71.508  29.270  15.132 1.00 44.99 ? 495 TYR B CD1 1 
ATOM   5546 C  CD2 . TYR B  1 305 ? 70.396  30.557  13.450 1.00 44.77 ? 495 TYR B CD2 1 
ATOM   5547 C  CE1 . TYR B  1 305 ? 71.272  28.106  14.402 1.00 46.50 ? 495 TYR B CE1 1 
ATOM   5548 C  CE2 . TYR B  1 305 ? 70.156  29.400  12.715 1.00 44.18 ? 495 TYR B CE2 1 
ATOM   5549 C  CZ  . TYR B  1 305 ? 70.597  28.180  13.197 1.00 44.22 ? 495 TYR B CZ  1 
ATOM   5550 O  OH  . TYR B  1 305 ? 70.368  27.035  12.473 1.00 46.98 ? 495 TYR B OH  1 
ATOM   5551 N  N   . GLY B  1 306 ? 70.846  35.083  16.171 1.00 19.45 ? 496 GLY B N   1 
ATOM   5552 C  CA  . GLY B  1 306 ? 70.576  36.024  17.241 1.00 22.32 ? 496 GLY B CA  1 
ATOM   5553 C  C   . GLY B  1 306 ? 70.973  37.448  16.901 1.00 25.18 ? 496 GLY B C   1 
ATOM   5554 O  O   . GLY B  1 306 ? 71.563  37.707  15.853 1.00 30.25 ? 496 GLY B O   1 
ATOM   5555 N  N   . TYR B  1 307 ? 70.632  38.379  17.785 1.00 24.60 ? 497 TYR B N   1 
ATOM   5556 C  CA  . TYR B  1 307 ? 70.979  39.781  17.594 1.00 24.46 ? 497 TYR B CA  1 
ATOM   5557 C  C   . TYR B  1 307 ? 71.772  40.250  18.804 1.00 24.61 ? 497 TYR B C   1 
ATOM   5558 O  O   . TYR B  1 307 ? 71.417  39.945  19.943 1.00 32.99 ? 497 TYR B O   1 
ATOM   5559 C  CB  . TYR B  1 307 ? 69.728  40.647  17.449 1.00 19.43 ? 497 TYR B CB  1 
ATOM   5560 C  CG  . TYR B  1 307 ? 68.820  40.241  16.313 1.00 17.93 ? 497 TYR B CG  1 
ATOM   5561 C  CD1 . TYR B  1 307 ? 67.685  39.467  16.543 1.00 19.22 ? 497 TYR B CD1 1 
ATOM   5562 C  CD2 . TYR B  1 307 ? 69.092  40.640  15.005 1.00 16.15 ? 497 TYR B CD2 1 
ATOM   5563 C  CE1 . TYR B  1 307 ? 66.839  39.105  15.499 1.00 18.91 ? 497 TYR B CE1 1 
ATOM   5564 C  CE2 . TYR B  1 307 ? 68.257  40.282  13.957 1.00 10.53 ? 497 TYR B CE2 1 
ATOM   5565 C  CZ  . TYR B  1 307 ? 67.133  39.518  14.208 1.00 16.24 ? 497 TYR B CZ  1 
ATOM   5566 O  OH  . TYR B  1 307 ? 66.295  39.179  13.170 1.00 21.11 ? 497 TYR B OH  1 
ATOM   5567 N  N   . CYS B  1 308 ? 72.843  40.990  18.552 1.00 20.28 ? 498 CYS B N   1 
ATOM   5568 C  CA  . CYS B  1 308 ? 73.694  41.502  19.613 1.00 16.20 ? 498 CYS B CA  1 
ATOM   5569 C  C   . CYS B  1 308 ? 72.944  42.234  20.711 1.00 14.80 ? 498 CYS B C   1 
ATOM   5570 O  O   . CYS B  1 308 ? 71.943  42.909  20.466 1.00 11.06 ? 498 CYS B O   1 
ATOM   5571 C  CB  . CYS B  1 308 ? 74.740  42.458  19.041 1.00 20.46 ? 498 CYS B CB  1 
ATOM   5572 S  SG  . CYS B  1 308 ? 76.024  41.680  18.018 1.00 30.65 ? 498 CYS B SG  1 
ATOM   5573 N  N   . TYR B  1 309 ? 73.451  42.096  21.930 1.00 16.46 ? 499 TYR B N   1 
ATOM   5574 C  CA  . TYR B  1 309 ? 72.885  42.768  23.088 1.00 17.34 ? 499 TYR B CA  1 
ATOM   5575 C  C   . TYR B  1 309 ? 74.007  42.948  24.095 1.00 15.67 ? 499 TYR B C   1 
ATOM   5576 O  O   . TYR B  1 309 ? 74.583  41.973  24.573 1.00 15.59 ? 499 TYR B O   1 
ATOM   5577 C  CB  . TYR B  1 309 ? 71.756  41.955  23.719 1.00 19.91 ? 499 TYR B CB  1 
ATOM   5578 C  CG  . TYR B  1 309 ? 71.143  42.665  24.903 1.00 20.86 ? 499 TYR B CG  1 
ATOM   5579 C  CD1 . TYR B  1 309 ? 70.478  43.883  24.740 1.00 16.38 ? 499 TYR B CD1 1 
ATOM   5580 C  CD2 . TYR B  1 309 ? 71.271  42.150  26.192 1.00 22.24 ? 499 TYR B CD2 1 
ATOM   5581 C  CE1 . TYR B  1 309 ? 69.962  44.571  25.832 1.00 21.27 ? 499 TYR B CE1 1 
ATOM   5582 C  CE2 . TYR B  1 309 ? 70.756  42.830  27.293 1.00 26.42 ? 499 TYR B CE2 1 
ATOM   5583 C  CZ  . TYR B  1 309 ? 70.104  44.040  27.108 1.00 27.54 ? 499 TYR B CZ  1 
ATOM   5584 O  OH  . TYR B  1 309 ? 69.605  44.720  28.200 1.00 28.33 ? 499 TYR B OH  1 
ATOM   5585 N  N   . ASN B  1 310 ? 74.317  44.203  24.399 1.00 15.16 ? 500 ASN B N   1 
ATOM   5586 C  CA  . ASN B  1 310 ? 75.382  44.546  25.333 1.00 16.64 ? 500 ASN B CA  1 
ATOM   5587 C  C   . ASN B  1 310 ? 76.652  43.692  25.245 1.00 15.74 ? 500 ASN B C   1 
ATOM   5588 O  O   . ASN B  1 310 ? 77.195  43.255  26.259 1.00 18.16 ? 500 ASN B O   1 
ATOM   5589 C  CB  . ASN B  1 310 ? 74.845  44.532  26.757 1.00 17.60 ? 500 ASN B CB  1 
ATOM   5590 C  CG  . ASN B  1 310 ? 73.728  45.525  26.952 1.00 28.01 ? 500 ASN B CG  1 
ATOM   5591 O  OD1 . ASN B  1 310 ? 73.779  46.638  26.431 1.00 28.49 ? 500 ASN B OD1 1 
ATOM   5592 N  ND2 . ASN B  1 310 ? 72.711  45.135  27.711 1.00 34.75 ? 500 ASN B ND2 1 
ATOM   5593 N  N   . GLY B  1 311 ? 77.121  43.457  24.025 1.00 13.28 ? 501 GLY B N   1 
ATOM   5594 C  CA  . GLY B  1 311 ? 78.341  42.695  23.843 1.00 15.18 ? 501 GLY B CA  1 
ATOM   5595 C  C   . GLY B  1 311 ? 78.230  41.191  23.719 1.00 15.64 ? 501 GLY B C   1 
ATOM   5596 O  O   . GLY B  1 311 ? 79.250  40.500  23.721 1.00 19.58 ? 501 GLY B O   1 
ATOM   5597 N  N   . ASN B  1 312 ? 77.012  40.672  23.614 1.00 18.79 ? 502 ASN B N   1 
ATOM   5598 C  CA  . ASN B  1 312 ? 76.826  39.230  23.482 1.00 20.96 ? 502 ASN B CA  1 
ATOM   5599 C  C   . ASN B  1 312 ? 75.740  38.894  22.469 1.00 18.33 ? 502 ASN B C   1 
ATOM   5600 O  O   . ASN B  1 312 ? 74.979  39.761  22.045 1.00 13.83 ? 502 ASN B O   1 
ATOM   5601 C  CB  . ASN B  1 312 ? 76.467  38.602  24.834 1.00 30.28 ? 502 ASN B CB  1 
ATOM   5602 C  CG  . ASN B  1 312 ? 77.548  38.804  25.881 1.00 38.88 ? 502 ASN B CG  1 
ATOM   5603 O  OD1 . ASN B  1 312 ? 77.774  39.918  26.353 1.00 46.42 ? 502 ASN B OD1 1 
ATOM   5604 N  ND2 . ASN B  1 312 ? 78.226  37.723  26.245 1.00 45.77 ? 502 ASN B ND2 1 
ATOM   5605 N  N   . CYS B  1 313 ? 75.685  37.625  22.082 1.00 20.06 ? 503 CYS B N   1 
ATOM   5606 C  CA  . CYS B  1 313 ? 74.688  37.156  21.135 1.00 20.26 ? 503 CYS B CA  1 
ATOM   5607 C  C   . CYS B  1 313 ? 73.843  36.097  21.839 1.00 19.70 ? 503 CYS B C   1 
ATOM   5608 O  O   . CYS B  1 313 ? 74.026  34.896  21.627 1.00 24.39 ? 503 CYS B O   1 
ATOM   5609 C  CB  . CYS B  1 313 ? 75.364  36.553  19.904 1.00 19.59 ? 503 CYS B CB  1 
ATOM   5610 S  SG  . CYS B  1 313 ? 74.234  36.374  18.488 1.00 20.53 ? 503 CYS B SG  1 
ATOM   5611 N  N   . PRO B  1 314 ? 72.904  36.534  22.691 1.00 16.20 ? 504 PRO B N   1 
ATOM   5612 C  CA  . PRO B  1 314 ? 72.024  35.632  23.441 1.00 11.47 ? 504 PRO B CA  1 
ATOM   5613 C  C   . PRO B  1 314 ? 71.039  34.843  22.584 1.00 12.29 ? 504 PRO B C   1 
ATOM   5614 O  O   . PRO B  1 314 ? 70.144  35.411  21.961 1.00 14.40 ? 504 PRO B O   1 
ATOM   5615 C  CB  . PRO B  1 314 ? 71.322  36.575  24.415 1.00 13.81 ? 504 PRO B CB  1 
ATOM   5616 C  CG  . PRO B  1 314 ? 71.214  37.847  23.622 1.00 15.28 ? 504 PRO B CG  1 
ATOM   5617 C  CD  . PRO B  1 314 ? 72.585  37.945  22.985 1.00 14.88 ? 504 PRO B CD  1 
ATOM   5618 N  N   . ILE B  1 315 ? 71.204  33.528  22.550 1.00 11.91 ? 505 ILE B N   1 
ATOM   5619 C  CA  . ILE B  1 315 ? 70.300  32.696  21.775 1.00 14.94 ? 505 ILE B CA  1 
ATOM   5620 C  C   . ILE B  1 315 ? 69.776  31.512  22.582 1.00 18.37 ? 505 ILE B C   1 
ATOM   5621 O  O   . ILE B  1 315 ? 70.484  30.939  23.415 1.00 16.20 ? 505 ILE B O   1 
ATOM   5622 C  CB  . ILE B  1 315 ? 70.964  32.163  20.483 1.00 14.36 ? 505 ILE B CB  1 
ATOM   5623 C  CG1 . ILE B  1 315 ? 72.110  31.212  20.828 1.00 16.65 ? 505 ILE B CG1 1 
ATOM   5624 C  CG2 . ILE B  1 315 ? 71.463  33.323  19.645 1.00 16.79 ? 505 ILE B CG2 1 
ATOM   5625 C  CD1 . ILE B  1 315 ? 72.646  30.453  19.633 1.00 11.65 ? 505 ILE B CD1 1 
ATOM   5626 N  N   . MET B  1 316 ? 68.519  31.168  22.318 1.00 17.88 ? 506 MET B N   1 
ATOM   5627 C  CA  . MET B  1 316 ? 67.824  30.071  22.973 1.00 15.41 ? 506 MET B CA  1 
ATOM   5628 C  C   . MET B  1 316 ? 68.704  28.834  23.174 1.00 15.52 ? 506 MET B C   1 
ATOM   5629 O  O   . MET B  1 316 ? 68.771  28.284  24.271 1.00 17.47 ? 506 MET B O   1 
ATOM   5630 C  CB  . MET B  1 316 ? 66.591  29.692  22.145 1.00 20.39 ? 506 MET B CB  1 
ATOM   5631 C  CG  . MET B  1 316 ? 65.312  29.542  22.945 1.00 22.43 ? 506 MET B CG  1 
ATOM   5632 S  SD  . MET B  1 316 ? 64.719  31.116  23.537 1.00 20.65 ? 506 MET B SD  1 
ATOM   5633 C  CE  . MET B  1 316 ? 63.108  31.181  22.777 1.00 31.94 ? 506 MET B CE  1 
ATOM   5634 N  N   . TYR B  1 317 ? 69.384  28.405  22.116 1.00 18.06 ? 507 TYR B N   1 
ATOM   5635 C  CA  . TYR B  1 317 ? 70.242  27.221  22.175 1.00 19.59 ? 507 TYR B CA  1 
ATOM   5636 C  C   . TYR B  1 317 ? 71.368  27.285  23.213 1.00 20.30 ? 507 TYR B C   1 
ATOM   5637 O  O   . TYR B  1 317 ? 71.517  26.367  24.015 1.00 24.21 ? 507 TYR B O   1 
ATOM   5638 C  CB  . TYR B  1 317 ? 70.830  26.934  20.789 1.00 23.30 ? 507 TYR B CB  1 
ATOM   5639 C  CG  . TYR B  1 317 ? 71.791  25.766  20.753 1.00 29.61 ? 507 TYR B CG  1 
ATOM   5640 C  CD1 . TYR B  1 317 ? 71.362  24.473  21.046 1.00 27.45 ? 507 TYR B CD1 1 
ATOM   5641 C  CD2 . TYR B  1 317 ? 73.137  25.958  20.445 1.00 31.94 ? 507 TYR B CD2 1 
ATOM   5642 C  CE1 . TYR B  1 317 ? 72.250  23.402  21.033 1.00 23.53 ? 507 TYR B CE1 1 
ATOM   5643 C  CE2 . TYR B  1 317 ? 74.030  24.897  20.431 1.00 27.23 ? 507 TYR B CE2 1 
ATOM   5644 C  CZ  . TYR B  1 317 ? 73.583  23.622  20.725 1.00 29.41 ? 507 TYR B CZ  1 
ATOM   5645 O  OH  . TYR B  1 317 ? 74.475  22.569  20.713 1.00 34.48 ? 507 TYR B OH  1 
ATOM   5646 N  N   . HIS B  1 318 ? 72.162  28.352  23.203 1.00 18.34 ? 508 HIS B N   1 
ATOM   5647 C  CA  . HIS B  1 318 ? 73.257  28.466  24.164 1.00 20.36 ? 508 HIS B CA  1 
ATOM   5648 C  C   . HIS B  1 318 ? 72.754  28.558  25.598 1.00 20.98 ? 508 HIS B C   1 
ATOM   5649 O  O   . HIS B  1 318 ? 73.395  28.055  26.522 1.00 20.39 ? 508 HIS B O   1 
ATOM   5650 C  CB  . HIS B  1 318 ? 74.135  29.690  23.875 1.00 20.23 ? 508 HIS B CB  1 
ATOM   5651 C  CG  . HIS B  1 318 ? 74.973  29.560  22.643 1.00 21.79 ? 508 HIS B CG  1 
ATOM   5652 N  ND1 . HIS B  1 318 ? 75.534  28.366  22.246 1.00 23.39 ? 508 HIS B ND1 1 
ATOM   5653 C  CD2 . HIS B  1 318 ? 75.362  30.481  21.730 1.00 20.73 ? 508 HIS B CD2 1 
ATOM   5654 C  CE1 . HIS B  1 318 ? 76.229  28.555  21.139 1.00 23.25 ? 508 HIS B CE1 1 
ATOM   5655 N  NE2 . HIS B  1 318 ? 76.141  29.829  20.805 1.00 20.82 ? 508 HIS B NE2 1 
ATOM   5656 N  N   . GLN B  1 319 ? 71.611  29.208  25.785 1.00 20.98 ? 509 GLN B N   1 
ATOM   5657 C  CA  . GLN B  1 319 ? 71.050  29.357  27.119 1.00 20.53 ? 509 GLN B CA  1 
ATOM   5658 C  C   . GLN B  1 319 ? 70.616  28.006  27.682 1.00 20.58 ? 509 GLN B C   1 
ATOM   5659 O  O   . GLN B  1 319 ? 70.700  27.774  28.887 1.00 19.04 ? 509 GLN B O   1 
ATOM   5660 C  CB  . GLN B  1 319 ? 69.891  30.353  27.086 1.00 20.35 ? 509 GLN B CB  1 
ATOM   5661 C  CG  . GLN B  1 319 ? 70.356  31.777  26.823 1.00 20.68 ? 509 GLN B CG  1 
ATOM   5662 C  CD  . GLN B  1 319 ? 69.212  32.755  26.630 1.00 24.74 ? 509 GLN B CD  1 
ATOM   5663 O  OE1 . GLN B  1 319 ? 68.347  32.895  27.495 1.00 20.79 ? 509 GLN B OE1 1 
ATOM   5664 N  NE2 . GLN B  1 319 ? 69.207  33.442  25.491 1.00 17.96 ? 509 GLN B NE2 1 
ATOM   5665 N  N   . CYS B  1 320 ? 70.155  27.115  26.809 1.00 22.23 ? 510 CYS B N   1 
ATOM   5666 C  CA  . CYS B  1 320 ? 69.762  25.780  27.241 1.00 25.38 ? 510 CYS B CA  1 
ATOM   5667 C  C   . CYS B  1 320 ? 71.037  25.024  27.608 1.00 28.52 ? 510 CYS B C   1 
ATOM   5668 O  O   . CYS B  1 320 ? 71.068  24.267  28.577 1.00 32.63 ? 510 CYS B O   1 
ATOM   5669 C  CB  . CYS B  1 320 ? 69.030  25.032  26.123 1.00 23.52 ? 510 CYS B CB  1 
ATOM   5670 S  SG  . CYS B  1 320 ? 67.277  25.483  25.910 1.00 28.03 ? 510 CYS B SG  1 
ATOM   5671 N  N   . TYR B  1 321 ? 72.092  25.242  26.825 1.00 26.51 ? 511 TYR B N   1 
ATOM   5672 C  CA  . TYR B  1 321 ? 73.372  24.595  27.071 1.00 24.05 ? 511 TYR B CA  1 
ATOM   5673 C  C   . TYR B  1 321 ? 73.936  24.989  28.431 1.00 23.35 ? 511 TYR B C   1 
ATOM   5674 O  O   . TYR B  1 321 ? 74.342  24.127  29.210 1.00 24.49 ? 511 TYR B O   1 
ATOM   5675 C  CB  . TYR B  1 321 ? 74.369  24.949  25.961 1.00 28.69 ? 511 TYR B CB  1 
ATOM   5676 C  CG  . TYR B  1 321 ? 75.805  24.576  26.271 1.00 31.10 ? 511 TYR B CG  1 
ATOM   5677 C  CD1 . TYR B  1 321 ? 76.610  25.413  27.045 1.00 37.90 ? 511 TYR B CD1 1 
ATOM   5678 C  CD2 . TYR B  1 321 ? 76.348  23.374  25.817 1.00 30.30 ? 511 TYR B CD2 1 
ATOM   5679 C  CE1 . TYR B  1 321 ? 77.917  25.064  27.363 1.00 36.76 ? 511 TYR B CE1 1 
ATOM   5680 C  CE2 . TYR B  1 321 ? 77.654  23.014  26.130 1.00 32.38 ? 511 TYR B CE2 1 
ATOM   5681 C  CZ  . TYR B  1 321 ? 78.433  23.865  26.905 1.00 39.97 ? 511 TYR B CZ  1 
ATOM   5682 O  OH  . TYR B  1 321 ? 79.726  23.521  27.228 1.00 46.93 ? 511 TYR B OH  1 
ATOM   5683 N  N   . ASP B  1 322 ? 73.972  26.287  28.718 1.00 23.78 ? 512 ASP B N   1 
ATOM   5684 C  CA  . ASP B  1 322 ? 74.490  26.744  30.003 1.00 26.44 ? 512 ASP B CA  1 
ATOM   5685 C  C   . ASP B  1 322 ? 73.764  26.031  31.137 1.00 28.97 ? 512 ASP B C   1 
ATOM   5686 O  O   . ASP B  1 322 ? 74.384  25.606  32.115 1.00 31.44 ? 512 ASP B O   1 
ATOM   5687 C  CB  . ASP B  1 322 ? 74.313  28.259  30.172 1.00 26.54 ? 512 ASP B CB  1 
ATOM   5688 C  CG  . ASP B  1 322 ? 75.166  29.062  29.208 1.00 31.55 ? 512 ASP B CG  1 
ATOM   5689 O  OD1 . ASP B  1 322 ? 76.345  28.699  29.004 1.00 33.61 ? 512 ASP B OD1 1 
ATOM   5690 O  OD2 . ASP B  1 322 ? 74.661  30.069  28.666 1.00 34.52 ? 512 ASP B OD2 1 
ATOM   5691 N  N   . LEU B  1 323 ? 72.450  25.891  30.992 1.00 25.50 ? 513 LEU B N   1 
ATOM   5692 C  CA  . LEU B  1 323 ? 71.634  25.247  32.008 1.00 25.91 ? 513 LEU B CA  1 
ATOM   5693 C  C   . LEU B  1 323 ? 71.779  23.736  32.156 1.00 25.60 ? 513 LEU B C   1 
ATOM   5694 O  O   . LEU B  1 323 ? 72.163  23.259  33.220 1.00 29.21 ? 513 LEU B O   1 
ATOM   5695 C  CB  . LEU B  1 323 ? 70.159  25.579  31.787 1.00 25.66 ? 513 LEU B CB  1 
ATOM   5696 C  CG  . LEU B  1 323 ? 69.712  26.978  32.206 1.00 23.77 ? 513 LEU B CG  1 
ATOM   5697 C  CD1 . LEU B  1 323 ? 68.215  27.117  31.963 1.00 17.97 ? 513 LEU B CD1 1 
ATOM   5698 C  CD2 . LEU B  1 323 ? 70.045  27.207  33.675 1.00 13.25 ? 513 LEU B CD2 1 
ATOM   5699 N  N   . PHE B  1 324 ? 71.477  22.984  31.102 1.00 24.10 ? 514 PHE B N   1 
ATOM   5700 C  CA  . PHE B  1 324 ? 71.547  21.529  31.187 1.00 23.74 ? 514 PHE B CA  1 
ATOM   5701 C  C   . PHE B  1 324 ? 72.683  20.849  30.425 1.00 23.70 ? 514 PHE B C   1 
ATOM   5702 O  O   . PHE B  1 324 ? 72.602  19.656  30.126 1.00 24.22 ? 514 PHE B O   1 
ATOM   5703 C  CB  . PHE B  1 324 ? 70.213  20.927  30.742 1.00 22.37 ? 514 PHE B CB  1 
ATOM   5704 C  CG  . PHE B  1 324 ? 69.016  21.723  31.175 1.00 26.92 ? 514 PHE B CG  1 
ATOM   5705 C  CD1 . PHE B  1 324 ? 68.410  22.621  30.299 1.00 28.40 ? 514 PHE B CD1 1 
ATOM   5706 C  CD2 . PHE B  1 324 ? 68.505  21.593  32.461 1.00 27.86 ? 514 PHE B CD2 1 
ATOM   5707 C  CE1 . PHE B  1 324 ? 67.311  23.379  30.697 1.00 24.79 ? 514 PHE B CE1 1 
ATOM   5708 C  CE2 . PHE B  1 324 ? 67.405  22.347  32.872 1.00 27.19 ? 514 PHE B CE2 1 
ATOM   5709 C  CZ  . PHE B  1 324 ? 66.807  23.242  31.987 1.00 29.37 ? 514 PHE B CZ  1 
ATOM   5710 N  N   . GLY B  1 325 ? 73.738  21.593  30.113 1.00 23.41 ? 515 GLY B N   1 
ATOM   5711 C  CA  . GLY B  1 325 ? 74.858  21.002  29.401 1.00 23.49 ? 515 GLY B CA  1 
ATOM   5712 C  C   . GLY B  1 325 ? 74.668  20.870  27.901 1.00 29.74 ? 515 GLY B C   1 
ATOM   5713 O  O   . GLY B  1 325 ? 74.135  21.769  27.253 1.00 35.53 ? 515 GLY B O   1 
ATOM   5714 N  N   . ALA B  1 326 ? 75.096  19.740  27.345 1.00 34.44 ? 516 ALA B N   1 
ATOM   5715 C  CA  . ALA B  1 326 ? 74.992  19.506  25.906 1.00 35.83 ? 516 ALA B CA  1 
ATOM   5716 C  C   . ALA B  1 326 ? 73.863  18.561  25.511 1.00 37.14 ? 516 ALA B C   1 
ATOM   5717 O  O   . ALA B  1 326 ? 73.271  17.892  26.357 1.00 39.44 ? 516 ALA B O   1 
ATOM   5718 C  CB  . ALA B  1 326 ? 76.320  18.974  25.377 1.00 34.38 ? 516 ALA B CB  1 
ATOM   5719 N  N   . ASP B  1 327 ? 73.578  18.517  24.211 1.00 39.40 ? 517 ASP B N   1 
ATOM   5720 C  CA  . ASP B  1 327 ? 72.531  17.662  23.659 1.00 42.93 ? 517 ASP B CA  1 
ATOM   5721 C  C   . ASP B  1 327 ? 71.127  18.069  24.115 1.00 42.49 ? 517 ASP B C   1 
ATOM   5722 O  O   . ASP B  1 327 ? 70.180  17.287  24.017 1.00 40.48 ? 517 ASP B O   1 
ATOM   5723 C  CB  . ASP B  1 327 ? 72.796  16.198  24.028 1.00 51.12 ? 517 ASP B CB  1 
ATOM   5724 C  CG  . ASP B  1 327 ? 71.810  15.243  23.374 1.00 60.17 ? 517 ASP B CG  1 
ATOM   5725 O  OD1 . ASP B  1 327 ? 71.771  15.187  22.125 1.00 61.79 ? 517 ASP B OD1 1 
ATOM   5726 O  OD2 . ASP B  1 327 ? 71.074  14.549  24.110 1.00 63.11 ? 517 ASP B OD2 1 
ATOM   5727 N  N   . VAL B  1 328 ? 70.998  19.294  24.616 1.00 42.85 ? 518 VAL B N   1 
ATOM   5728 C  CA  . VAL B  1 328 ? 69.706  19.812  25.063 1.00 40.61 ? 518 VAL B CA  1 
ATOM   5729 C  C   . VAL B  1 328 ? 69.370  21.037  24.214 1.00 40.69 ? 518 VAL B C   1 
ATOM   5730 O  O   . VAL B  1 328 ? 69.996  22.087  24.357 1.00 44.37 ? 518 VAL B O   1 
ATOM   5731 C  CB  . VAL B  1 328 ? 69.746  20.224  26.549 1.00 37.12 ? 518 VAL B CB  1 
ATOM   5732 C  CG1 . VAL B  1 328 ? 68.388  20.758  26.974 1.00 41.35 ? 518 VAL B CG1 1 
ATOM   5733 C  CG2 . VAL B  1 328 ? 70.137  19.038  27.408 1.00 32.21 ? 518 VAL B CG2 1 
ATOM   5734 N  N   . TYR B  1 329 ? 68.382  20.903  23.335 1.00 38.00 ? 519 TYR B N   1 
ATOM   5735 C  CA  . TYR B  1 329 ? 68.003  21.998  22.448 1.00 38.16 ? 519 TYR B CA  1 
ATOM   5736 C  C   . TYR B  1 329 ? 66.731  22.720  22.870 1.00 39.14 ? 519 TYR B C   1 
ATOM   5737 O  O   . TYR B  1 329 ? 66.068  22.319  23.825 1.00 38.87 ? 519 TYR B O   1 
ATOM   5738 C  CB  . TYR B  1 329 ? 67.843  21.468  21.024 1.00 37.03 ? 519 TYR B CB  1 
ATOM   5739 C  CG  . TYR B  1 329 ? 68.915  20.475  20.646 1.00 40.72 ? 519 TYR B CG  1 
ATOM   5740 C  CD1 . TYR B  1 329 ? 68.727  19.107  20.843 1.00 39.16 ? 519 TYR B CD1 1 
ATOM   5741 C  CD2 . TYR B  1 329 ? 70.137  20.904  20.132 1.00 40.29 ? 519 TYR B CD2 1 
ATOM   5742 C  CE1 . TYR B  1 329 ? 69.732  18.192  20.537 1.00 37.88 ? 519 TYR B CE1 1 
ATOM   5743 C  CE2 . TYR B  1 329 ? 71.147  19.999  19.825 1.00 36.90 ? 519 TYR B CE2 1 
ATOM   5744 C  CZ  . TYR B  1 329 ? 70.939  18.648  20.028 1.00 38.06 ? 519 TYR B CZ  1 
ATOM   5745 O  OH  . TYR B  1 329 ? 71.939  17.755  19.720 1.00 44.63 ? 519 TYR B OH  1 
ATOM   5746 N  N   . GLU B  1 330 ? 66.403  23.792  22.153 1.00 38.70 ? 520 GLU B N   1 
ATOM   5747 C  CA  . GLU B  1 330 ? 65.204  24.573  22.444 1.00 35.66 ? 520 GLU B CA  1 
ATOM   5748 C  C   . GLU B  1 330 ? 63.989  23.664  22.348 1.00 34.10 ? 520 GLU B C   1 
ATOM   5749 O  O   . GLU B  1 330 ? 63.886  22.848  21.433 1.00 36.29 ? 520 GLU B O   1 
ATOM   5750 C  CB  . GLU B  1 330 ? 65.050  25.727  21.443 1.00 34.41 ? 520 GLU B CB  1 
ATOM   5751 C  CG  . GLU B  1 330 ? 63.899  26.683  21.770 1.00 36.03 ? 520 GLU B CG  1 
ATOM   5752 C  CD  . GLU B  1 330 ? 63.680  27.753  20.708 1.00 34.92 ? 520 GLU B CD  1 
ATOM   5753 O  OE1 . GLU B  1 330 ? 64.684  28.303  20.205 1.00 35.28 ? 520 GLU B OE1 1 
ATOM   5754 O  OE2 . GLU B  1 330 ? 62.505  28.053  20.387 1.00 28.87 ? 520 GLU B OE2 1 
ATOM   5755 N  N   . ALA B  1 331 ? 63.074  23.800  23.299 1.00 32.22 ? 521 ALA B N   1 
ATOM   5756 C  CA  . ALA B  1 331 ? 61.866  22.991  23.302 1.00 33.72 ? 521 ALA B CA  1 
ATOM   5757 C  C   . ALA B  1 331 ? 60.870  23.558  22.294 1.00 36.81 ? 521 ALA B C   1 
ATOM   5758 O  O   . ALA B  1 331 ? 60.953  24.729  21.916 1.00 32.61 ? 521 ALA B O   1 
ATOM   5759 C  CB  . ALA B  1 331 ? 61.256  22.976  24.696 1.00 33.26 ? 521 ALA B CB  1 
ATOM   5760 N  N   . GLU B  1 332 ? 59.929  22.725  21.860 1.00 40.49 ? 522 GLU B N   1 
ATOM   5761 C  CA  . GLU B  1 332 ? 58.921  23.151  20.898 1.00 40.95 ? 522 GLU B CA  1 
ATOM   5762 C  C   . GLU B  1 332 ? 58.070  24.310  21.411 1.00 38.89 ? 522 GLU B C   1 
ATOM   5763 O  O   . GLU B  1 332 ? 57.993  24.556  22.616 1.00 37.65 ? 522 GLU B O   1 
ATOM   5764 C  CB  . GLU B  1 332 ? 58.023  21.972  20.517 1.00 46.44 ? 522 GLU B CB  1 
ATOM   5765 C  CG  . GLU B  1 332 ? 58.706  20.957  19.617 1.00 55.60 ? 522 GLU B CG  1 
ATOM   5766 C  CD  . GLU B  1 332 ? 59.276  21.592  18.357 1.00 62.46 ? 522 GLU B CD  1 
ATOM   5767 O  OE1 . GLU B  1 332 ? 58.503  22.220  17.602 1.00 66.58 ? 522 GLU B OE1 1 
ATOM   5768 O  OE2 . GLU B  1 332 ? 60.498  21.465  18.122 1.00 66.15 ? 522 GLU B OE2 1 
ATOM   5769 N  N   . ASP B  1 333 ? 57.434  25.013  20.477 1.00 35.68 ? 523 ASP B N   1 
ATOM   5770 C  CA  . ASP B  1 333 ? 56.590  26.163  20.782 1.00 30.53 ? 523 ASP B CA  1 
ATOM   5771 C  C   . ASP B  1 333 ? 55.512  25.921  21.833 1.00 32.68 ? 523 ASP B C   1 
ATOM   5772 O  O   . ASP B  1 333 ? 55.209  26.811  22.626 1.00 38.63 ? 523 ASP B O   1 
ATOM   5773 C  CB  . ASP B  1 333 ? 55.922  26.667  19.501 1.00 32.38 ? 523 ASP B CB  1 
ATOM   5774 C  CG  . ASP B  1 333 ? 56.903  27.299  18.537 1.00 36.16 ? 523 ASP B CG  1 
ATOM   5775 O  OD1 . ASP B  1 333 ? 57.955  26.684  18.259 1.00 43.67 ? 523 ASP B OD1 1 
ATOM   5776 O  OD2 . ASP B  1 333 ? 56.616  28.411  18.048 1.00 34.30 ? 523 ASP B OD2 1 
ATOM   5777 N  N   . SER B  1 334 ? 54.927  24.728  21.844 1.00 31.81 ? 524 SER B N   1 
ATOM   5778 C  CA  . SER B  1 334 ? 53.867  24.425  22.804 1.00 34.55 ? 524 SER B CA  1 
ATOM   5779 C  C   . SER B  1 334 ? 54.319  24.520  24.263 1.00 32.53 ? 524 SER B C   1 
ATOM   5780 O  O   . SER B  1 334 ? 53.542  24.906  25.139 1.00 33.32 ? 524 SER B O   1 
ATOM   5781 C  CB  . SER B  1 334 ? 53.286  23.033  22.534 1.00 32.07 ? 524 SER B CB  1 
ATOM   5782 O  OG  . SER B  1 334 ? 54.256  22.024  22.744 1.00 36.06 ? 524 SER B OG  1 
ATOM   5783 N  N   . CYS B  1 335 ? 55.572  24.167  24.524 1.00 26.85 ? 525 CYS B N   1 
ATOM   5784 C  CA  . CYS B  1 335 ? 56.094  24.219  25.881 1.00 24.05 ? 525 CYS B CA  1 
ATOM   5785 C  C   . CYS B  1 335 ? 55.991  25.624  26.453 1.00 24.33 ? 525 CYS B C   1 
ATOM   5786 O  O   . CYS B  1 335 ? 55.529  25.820  27.578 1.00 25.42 ? 525 CYS B O   1 
ATOM   5787 C  CB  . CYS B  1 335 ? 57.560  23.788  25.914 1.00 28.71 ? 525 CYS B CB  1 
ATOM   5788 S  SG  . CYS B  1 335 ? 57.904  22.006  25.737 1.00 34.77 ? 525 CYS B SG  1 
ATOM   5789 N  N   . PHE B  1 336 ? 56.426  26.601  25.667 1.00 24.43 ? 526 PHE B N   1 
ATOM   5790 C  CA  . PHE B  1 336 ? 56.415  27.986  26.103 1.00 20.83 ? 526 PHE B CA  1 
ATOM   5791 C  C   . PHE B  1 336 ? 55.061  28.512  26.552 1.00 20.84 ? 526 PHE B C   1 
ATOM   5792 O  O   . PHE B  1 336 ? 54.997  29.483  27.304 1.00 13.20 ? 526 PHE B O   1 
ATOM   5793 C  CB  . PHE B  1 336 ? 57.001  28.880  25.009 1.00 21.06 ? 526 PHE B CB  1 
ATOM   5794 C  CG  . PHE B  1 336 ? 58.477  28.682  24.803 1.00 17.53 ? 526 PHE B CG  1 
ATOM   5795 C  CD1 . PHE B  1 336 ? 58.950  27.607  24.062 1.00 14.64 ? 526 PHE B CD1 1 
ATOM   5796 C  CD2 . PHE B  1 336 ? 59.394  29.545  25.393 1.00 12.49 ? 526 PHE B CD2 1 
ATOM   5797 C  CE1 . PHE B  1 336 ? 60.315  27.393  23.913 1.00 16.90 ? 526 PHE B CE1 1 
ATOM   5798 C  CE2 . PHE B  1 336 ? 60.761  29.339  25.251 1.00 15.63 ? 526 PHE B CE2 1 
ATOM   5799 C  CZ  . PHE B  1 336 ? 61.223  28.260  24.510 1.00 17.14 ? 526 PHE B CZ  1 
ATOM   5800 N  N   . GLU B  1 337 ? 53.983  27.871  26.105 1.00 25.14 ? 527 GLU B N   1 
ATOM   5801 C  CA  . GLU B  1 337 ? 52.638  28.289  26.491 1.00 27.49 ? 527 GLU B CA  1 
ATOM   5802 C  C   . GLU B  1 337 ? 52.504  28.308  28.011 1.00 25.94 ? 527 GLU B C   1 
ATOM   5803 O  O   . GLU B  1 337 ? 51.735  29.098  28.563 1.00 28.09 ? 527 GLU B O   1 
ATOM   5804 C  CB  . GLU B  1 337 ? 51.591  27.343  25.897 1.00 36.02 ? 527 GLU B CB  1 
ATOM   5805 C  CG  . GLU B  1 337 ? 51.537  27.347  24.378 1.00 49.50 ? 527 GLU B CG  1 
ATOM   5806 C  CD  . GLU B  1 337 ? 50.574  26.312  23.827 1.00 56.48 ? 527 GLU B CD  1 
ATOM   5807 O  OE1 . GLU B  1 337 ? 50.500  26.168  22.587 1.00 61.49 ? 527 GLU B OE1 1 
ATOM   5808 O  OE2 . GLU B  1 337 ? 49.892  25.641  24.632 1.00 56.68 ? 527 GLU B OE2 1 
ATOM   5809 N  N   . ARG B  1 338 ? 53.251  27.432  28.681 1.00 23.33 ? 528 ARG B N   1 
ATOM   5810 C  CA  . ARG B  1 338 ? 53.228  27.356  30.142 1.00 23.54 ? 528 ARG B CA  1 
ATOM   5811 C  C   . ARG B  1 338 ? 53.396  28.749  30.740 1.00 25.64 ? 528 ARG B C   1 
ATOM   5812 O  O   . ARG B  1 338 ? 52.763  29.091  31.739 1.00 24.11 ? 528 ARG B O   1 
ATOM   5813 C  CB  . ARG B  1 338 ? 54.367  26.469  30.658 1.00 24.47 ? 528 ARG B CB  1 
ATOM   5814 C  CG  . ARG B  1 338 ? 54.149  24.960  30.591 1.00 25.81 ? 528 ARG B CG  1 
ATOM   5815 C  CD  . ARG B  1 338 ? 55.394  24.258  31.131 1.00 34.45 ? 528 ARG B CD  1 
ATOM   5816 N  NE  . ARG B  1 338 ? 55.235  22.823  31.372 1.00 41.87 ? 528 ARG B NE  1 
ATOM   5817 C  CZ  . ARG B  1 338 ? 54.931  21.925  30.440 1.00 45.62 ? 528 ARG B CZ  1 
ATOM   5818 N  NH1 . ARG B  1 338 ? 54.740  22.301  29.183 1.00 50.01 ? 528 ARG B NH1 1 
ATOM   5819 N  NH2 . ARG B  1 338 ? 54.838  20.641  30.762 1.00 42.81 ? 528 ARG B NH2 1 
ATOM   5820 N  N   . ASN B  1 339 ? 54.256  29.548  30.114 1.00 24.43 ? 529 ASN B N   1 
ATOM   5821 C  CA  . ASN B  1 339 ? 54.545  30.900  30.576 1.00 22.78 ? 529 ASN B CA  1 
ATOM   5822 C  C   . ASN B  1 339 ? 53.328  31.811  30.712 1.00 21.96 ? 529 ASN B C   1 
ATOM   5823 O  O   . ASN B  1 339 ? 53.454  32.951  31.169 1.00 17.26 ? 529 ASN B O   1 
ATOM   5824 C  CB  . ASN B  1 339 ? 55.590  31.546  29.658 1.00 19.83 ? 529 ASN B CB  1 
ATOM   5825 C  CG  . ASN B  1 339 ? 56.992  30.999  29.895 1.00 25.30 ? 529 ASN B CG  1 
ATOM   5826 O  OD1 . ASN B  1 339 ? 57.908  31.225  29.100 1.00 24.63 ? 529 ASN B OD1 1 
ATOM   5827 N  ND2 . ASN B  1 339 ? 57.166  30.284  31.000 1.00 20.95 ? 529 ASN B ND2 1 
ATOM   5828 N  N   . GLN B  1 340 ? 52.153  31.315  30.329 1.00 19.63 ? 530 GLN B N   1 
ATOM   5829 C  CA  . GLN B  1 340 ? 50.931  32.115  30.433 1.00 22.62 ? 530 GLN B CA  1 
ATOM   5830 C  C   . GLN B  1 340 ? 50.211  31.886  31.753 1.00 21.42 ? 530 GLN B C   1 
ATOM   5831 O  O   . GLN B  1 340 ? 49.332  32.657  32.124 1.00 24.42 ? 530 GLN B O   1 
ATOM   5832 C  CB  . GLN B  1 340 ? 49.983  31.806  29.274 1.00 17.72 ? 530 GLN B CB  1 
ATOM   5833 C  CG  . GLN B  1 340 ? 50.556  32.166  27.917 1.00 26.45 ? 530 GLN B CG  1 
ATOM   5834 C  CD  . GLN B  1 340 ? 49.582  31.932  26.784 1.00 30.17 ? 530 GLN B CD  1 
ATOM   5835 O  OE1 . GLN B  1 340 ? 48.578  32.635  26.654 1.00 27.48 ? 530 GLN B OE1 1 
ATOM   5836 N  NE2 . GLN B  1 340 ? 49.871  30.936  25.954 1.00 33.79 ? 530 GLN B NE2 1 
ATOM   5837 N  N   . LYS B  1 341 ? 50.599  30.831  32.463 1.00 25.68 ? 531 LYS B N   1 
ATOM   5838 C  CA  . LYS B  1 341 ? 49.990  30.493  33.748 1.00 22.87 ? 531 LYS B CA  1 
ATOM   5839 C  C   . LYS B  1 341 ? 50.178  31.600  34.772 1.00 20.69 ? 531 LYS B C   1 
ATOM   5840 O  O   . LYS B  1 341 ? 49.301  31.855  35.592 1.00 23.66 ? 531 LYS B O   1 
ATOM   5841 C  CB  . LYS B  1 341 ? 50.600  29.205  34.308 1.00 23.41 ? 531 LYS B CB  1 
ATOM   5842 C  CG  . LYS B  1 341 ? 50.458  27.990  33.412 1.00 32.40 ? 531 LYS B CG  1 
ATOM   5843 C  CD  . LYS B  1 341 ? 51.152  26.783  34.027 1.00 40.12 ? 531 LYS B CD  1 
ATOM   5844 C  CE  . LYS B  1 341 ? 51.024  25.557  33.139 1.00 41.57 ? 531 LYS B CE  1 
ATOM   5845 N  NZ  . LYS B  1 341 ? 49.598  25.233  32.865 1.00 43.01 ? 531 LYS B NZ  1 
ATOM   5846 N  N   . GLY B  1 342 ? 51.329  32.259  34.726 1.00 21.99 ? 532 GLY B N   1 
ATOM   5847 C  CA  . GLY B  1 342 ? 51.593  33.309  35.687 1.00 21.96 ? 532 GLY B CA  1 
ATOM   5848 C  C   . GLY B  1 342 ? 51.741  32.679  37.059 1.00 25.42 ? 532 GLY B C   1 
ATOM   5849 O  O   . GLY B  1 342 ? 51.397  33.284  38.080 1.00 19.80 ? 532 GLY B O   1 
ATOM   5850 N  N   . ASN B  1 343 ? 52.240  31.444  37.081 1.00 26.27 ? 533 ASN B N   1 
ATOM   5851 C  CA  . ASN B  1 343 ? 52.439  30.738  38.335 1.00 23.81 ? 533 ASN B CA  1 
ATOM   5852 C  C   . ASN B  1 343 ? 53.839  31.024  38.851 1.00 23.78 ? 533 ASN B C   1 
ATOM   5853 O  O   . ASN B  1 343 ? 54.433  32.040  38.498 1.00 26.39 ? 533 ASN B O   1 
ATOM   5854 C  CB  . ASN B  1 343 ? 52.239  29.230  38.160 1.00 21.33 ? 533 ASN B CB  1 
ATOM   5855 C  CG  . ASN B  1 343 ? 53.230  28.620  37.203 1.00 22.33 ? 533 ASN B CG  1 
ATOM   5856 O  OD1 . ASN B  1 343 ? 54.367  29.074  37.102 1.00 28.31 ? 533 ASN B OD1 1 
ATOM   5857 N  ND2 . ASN B  1 343 ? 52.812  27.567  36.507 1.00 21.22 ? 533 ASN B ND2 1 
ATOM   5858 N  N   . TYR B  1 344 ? 54.373  30.125  39.672 1.00 24.08 ? 534 TYR B N   1 
ATOM   5859 C  CA  . TYR B  1 344 ? 55.693  30.326  40.250 1.00 20.02 ? 534 TYR B CA  1 
ATOM   5860 C  C   . TYR B  1 344 ? 56.851  30.249  39.262 1.00 20.35 ? 534 TYR B C   1 
ATOM   5861 O  O   . TYR B  1 344 ? 57.848  30.952  39.428 1.00 20.29 ? 534 TYR B O   1 
ATOM   5862 C  CB  . TYR B  1 344 ? 55.916  29.338  41.407 1.00 20.61 ? 534 TYR B CB  1 
ATOM   5863 C  CG  . TYR B  1 344 ? 56.209  27.899  41.012 1.00 20.68 ? 534 TYR B CG  1 
ATOM   5864 C  CD1 . TYR B  1 344 ? 57.522  27.459  40.808 1.00 13.39 ? 534 TYR B CD1 1 
ATOM   5865 C  CD2 . TYR B  1 344 ? 55.178  26.968  40.882 1.00 13.95 ? 534 TYR B CD2 1 
ATOM   5866 C  CE1 . TYR B  1 344 ? 57.796  26.130  40.494 1.00 4.89  ? 534 TYR B CE1 1 
ATOM   5867 C  CE2 . TYR B  1 344 ? 55.442  25.635  40.565 1.00 4.43  ? 534 TYR B CE2 1 
ATOM   5868 C  CZ  . TYR B  1 344 ? 56.747  25.220  40.376 1.00 14.90 ? 534 TYR B CZ  1 
ATOM   5869 O  OH  . TYR B  1 344 ? 57.000  23.891  40.087 1.00 15.04 ? 534 TYR B OH  1 
ATOM   5870 N  N   . TYR B  1 345 ? 56.724  29.421  38.228 1.00 17.76 ? 535 TYR B N   1 
ATOM   5871 C  CA  . TYR B  1 345 ? 57.807  29.284  37.258 1.00 22.31 ? 535 TYR B CA  1 
ATOM   5872 C  C   . TYR B  1 345 ? 57.546  29.915  35.890 1.00 23.81 ? 535 TYR B C   1 
ATOM   5873 O  O   . TYR B  1 345 ? 58.463  30.473  35.278 1.00 18.50 ? 535 TYR B O   1 
ATOM   5874 C  CB  . TYR B  1 345 ? 58.165  27.801  37.086 1.00 21.26 ? 535 TYR B CB  1 
ATOM   5875 C  CG  . TYR B  1 345 ? 57.178  26.990  36.275 1.00 23.22 ? 535 TYR B CG  1 
ATOM   5876 C  CD1 . TYR B  1 345 ? 57.205  27.013  34.877 1.00 22.53 ? 535 TYR B CD1 1 
ATOM   5877 C  CD2 . TYR B  1 345 ? 56.228  26.182  36.902 1.00 23.10 ? 535 TYR B CD2 1 
ATOM   5878 C  CE1 . TYR B  1 345 ? 56.312  26.248  34.126 1.00 24.19 ? 535 TYR B CE1 1 
ATOM   5879 C  CE2 . TYR B  1 345 ? 55.330  25.416  36.161 1.00 18.14 ? 535 TYR B CE2 1 
ATOM   5880 C  CZ  . TYR B  1 345 ? 55.378  25.451  34.777 1.00 21.51 ? 535 TYR B CZ  1 
ATOM   5881 O  OH  . TYR B  1 345 ? 54.499  24.687  34.046 1.00 25.96 ? 535 TYR B OH  1 
ATOM   5882 N  N   . GLY B  1 346 ? 56.303  29.821  35.419 1.00 24.88 ? 536 GLY B N   1 
ATOM   5883 C  CA  . GLY B  1 346 ? 55.942  30.370  34.123 1.00 19.25 ? 536 GLY B CA  1 
ATOM   5884 C  C   . GLY B  1 346 ? 55.362  31.770  34.184 1.00 22.31 ? 536 GLY B C   1 
ATOM   5885 O  O   . GLY B  1 346 ? 54.276  31.987  34.717 1.00 24.10 ? 536 GLY B O   1 
ATOM   5886 N  N   . TYR B  1 347 ? 56.096  32.729  33.634 1.00 22.79 ? 537 TYR B N   1 
ATOM   5887 C  CA  . TYR B  1 347 ? 55.656  34.117  33.613 1.00 23.22 ? 537 TYR B CA  1 
ATOM   5888 C  C   . TYR B  1 347 ? 56.608  34.934  32.743 1.00 21.75 ? 537 TYR B C   1 
ATOM   5889 O  O   . TYR B  1 347 ? 57.610  34.412  32.254 1.00 21.67 ? 537 TYR B O   1 
ATOM   5890 C  CB  . TYR B  1 347 ? 55.590  34.673  35.041 1.00 20.27 ? 537 TYR B CB  1 
ATOM   5891 C  CG  . TYR B  1 347 ? 56.905  34.657  35.786 1.00 25.54 ? 537 TYR B CG  1 
ATOM   5892 C  CD1 . TYR B  1 347 ? 57.806  35.714  35.672 1.00 24.31 ? 537 TYR B CD1 1 
ATOM   5893 C  CD2 . TYR B  1 347 ? 57.254  33.579  36.604 1.00 26.88 ? 537 TYR B CD2 1 
ATOM   5894 C  CE1 . TYR B  1 347 ? 59.019  35.702  36.351 1.00 23.01 ? 537 TYR B CE1 1 
ATOM   5895 C  CE2 . TYR B  1 347 ? 58.468  33.556  37.287 1.00 24.02 ? 537 TYR B CE2 1 
ATOM   5896 C  CZ  . TYR B  1 347 ? 59.346  34.621  37.155 1.00 25.28 ? 537 TYR B CZ  1 
ATOM   5897 O  OH  . TYR B  1 347 ? 60.555  34.607  37.816 1.00 23.23 ? 537 TYR B OH  1 
ATOM   5898 N  N   . CYS B  1 348 ? 56.302  36.210  32.551 1.00 20.41 ? 538 CYS B N   1 
ATOM   5899 C  CA  . CYS B  1 348 ? 57.136  37.055  31.709 1.00 22.81 ? 538 CYS B CA  1 
ATOM   5900 C  C   . CYS B  1 348 ? 58.038  38.057  32.417 1.00 24.83 ? 538 CYS B C   1 
ATOM   5901 O  O   . CYS B  1 348 ? 59.159  38.305  31.970 1.00 23.54 ? 538 CYS B O   1 
ATOM   5902 C  CB  . CYS B  1 348 ? 56.260  37.789  30.688 1.00 23.41 ? 538 CYS B CB  1 
ATOM   5903 S  SG  . CYS B  1 348 ? 56.517  37.160  29.002 1.00 24.58 ? 538 CYS B SG  1 
ATOM   5904 N  N   . ARG B  1 349 ? 57.563  38.634  33.515 1.00 23.83 ? 539 ARG B N   1 
ATOM   5905 C  CA  . ARG B  1 349 ? 58.362  39.619  34.226 1.00 22.53 ? 539 ARG B CA  1 
ATOM   5906 C  C   . ARG B  1 349 ? 57.838  39.879  35.630 1.00 26.62 ? 539 ARG B C   1 
ATOM   5907 O  O   . ARG B  1 349 ? 56.831  39.309  36.048 1.00 28.68 ? 539 ARG B O   1 
ATOM   5908 C  CB  . ARG B  1 349 ? 58.371  40.928  33.435 1.00 23.01 ? 539 ARG B CB  1 
ATOM   5909 C  CG  . ARG B  1 349 ? 57.059  41.701  33.494 1.00 17.81 ? 539 ARG B CG  1 
ATOM   5910 C  CD  . ARG B  1 349 ? 57.005  42.771  32.420 1.00 23.21 ? 539 ARG B CD  1 
ATOM   5911 N  NE  . ARG B  1 349 ? 56.742  42.189  31.108 1.00 29.98 ? 539 ARG B NE  1 
ATOM   5912 C  CZ  . ARG B  1 349 ? 55.547  41.763  30.710 1.00 33.40 ? 539 ARG B CZ  1 
ATOM   5913 N  NH1 . ARG B  1 349 ? 54.505  41.863  31.526 1.00 33.58 ? 539 ARG B NH1 1 
ATOM   5914 N  NH2 . ARG B  1 349 ? 55.398  41.217  29.508 1.00 25.89 ? 539 ARG B NH2 1 
ATOM   5915 N  N   . LYS B  1 350 ? 58.533  40.755  36.348 1.00 30.04 ? 540 LYS B N   1 
ATOM   5916 C  CA  . LYS B  1 350 ? 58.159  41.120  37.706 1.00 34.79 ? 540 LYS B CA  1 
ATOM   5917 C  C   . LYS B  1 350 ? 57.679  42.565  37.756 1.00 37.67 ? 540 LYS B C   1 
ATOM   5918 O  O   . LYS B  1 350 ? 58.141  43.411  36.993 1.00 35.31 ? 540 LYS B O   1 
ATOM   5919 C  CB  . LYS B  1 350 ? 59.358  40.971  38.644 1.00 37.00 ? 540 LYS B CB  1 
ATOM   5920 C  CG  . LYS B  1 350 ? 59.909  39.564  38.768 1.00 34.61 ? 540 LYS B CG  1 
ATOM   5921 C  CD  . LYS B  1 350 ? 58.906  38.633  39.413 1.00 32.65 ? 540 LYS B CD  1 
ATOM   5922 C  CE  . LYS B  1 350 ? 59.560  37.313  39.772 1.00 32.62 ? 540 LYS B CE  1 
ATOM   5923 N  NZ  . LYS B  1 350 ? 60.620  37.502  40.794 1.00 18.64 ? 540 LYS B NZ  1 
ATOM   5924 N  N   . GLU B  1 351 ? 56.748  42.834  38.664 1.00 44.23 ? 541 GLU B N   1 
ATOM   5925 C  CA  . GLU B  1 351 ? 56.200  44.173  38.859 1.00 48.73 ? 541 GLU B CA  1 
ATOM   5926 C  C   . GLU B  1 351 ? 55.733  44.288  40.303 1.00 52.21 ? 541 GLU B C   1 
ATOM   5927 O  O   . GLU B  1 351 ? 54.713  43.710  40.684 1.00 51.99 ? 541 GLU B O   1 
ATOM   5928 C  CB  . GLU B  1 351 ? 55.036  44.429  37.896 1.00 49.35 ? 541 GLU B CB  1 
ATOM   5929 C  CG  . GLU B  1 351 ? 55.482  44.762  36.476 1.00 58.83 ? 541 GLU B CG  1 
ATOM   5930 C  CD  . GLU B  1 351 ? 54.323  44.982  35.519 1.00 61.39 ? 541 GLU B CD  1 
ATOM   5931 O  OE1 . GLU B  1 351 ? 53.425  45.791  35.843 1.00 61.61 ? 541 GLU B OE1 1 
ATOM   5932 O  OE2 . GLU B  1 351 ? 54.315  44.352  34.437 1.00 62.35 ? 541 GLU B OE2 1 
ATOM   5933 N  N   . ASN B  1 352 ? 56.495  45.031  41.104 1.00 54.96 ? 542 ASN B N   1 
ATOM   5934 C  CA  . ASN B  1 352 ? 56.189  45.216  42.520 1.00 56.71 ? 542 ASN B CA  1 
ATOM   5935 C  C   . ASN B  1 352 ? 56.413  43.886  43.231 1.00 56.89 ? 542 ASN B C   1 
ATOM   5936 O  O   . ASN B  1 352 ? 55.905  43.660  44.331 1.00 59.44 ? 542 ASN B O   1 
ATOM   5937 C  CB  . ASN B  1 352 ? 54.735  45.663  42.706 1.00 60.41 ? 542 ASN B CB  1 
ATOM   5938 C  CG  . ASN B  1 352 ? 54.432  46.982  42.013 1.00 64.25 ? 542 ASN B CG  1 
ATOM   5939 O  OD1 . ASN B  1 352 ? 53.283  47.431  41.984 1.00 67.76 ? 542 ASN B OD1 1 
ATOM   5940 N  ND2 . ASN B  1 352 ? 55.463  47.611  41.453 1.00 58.73 ? 542 ASN B ND2 1 
ATOM   5941 N  N   . GLY B  1 353 ? 57.181  43.010  42.588 1.00 52.19 ? 543 GLY B N   1 
ATOM   5942 C  CA  . GLY B  1 353 ? 57.461  41.706  43.157 1.00 47.43 ? 543 GLY B CA  1 
ATOM   5943 C  C   . GLY B  1 353 ? 56.549  40.640  42.579 1.00 45.73 ? 543 GLY B C   1 
ATOM   5944 O  O   . GLY B  1 353 ? 56.898  39.457  42.546 1.00 42.18 ? 543 GLY B O   1 
ATOM   5945 N  N   . ASN B  1 354 ? 55.374  41.063  42.122 1.00 41.46 ? 544 ASN B N   1 
ATOM   5946 C  CA  . ASN B  1 354 ? 54.402  40.146  41.539 1.00 38.64 ? 544 ASN B CA  1 
ATOM   5947 C  C   . ASN B  1 354 ? 54.866  39.712  40.156 1.00 35.18 ? 544 ASN B C   1 
ATOM   5948 O  O   . ASN B  1 354 ? 55.401  40.518  39.389 1.00 32.39 ? 544 ASN B O   1 
ATOM   5949 C  CB  . ASN B  1 354 ? 53.038  40.829  41.435 1.00 42.98 ? 544 ASN B CB  1 
ATOM   5950 C  CG  . ASN B  1 354 ? 52.548  41.357  42.768 1.00 44.08 ? 544 ASN B CG  1 
ATOM   5951 O  OD1 . ASN B  1 354 ? 51.539  42.055  42.836 1.00 48.64 ? 544 ASN B OD1 1 
ATOM   5952 N  ND2 . ASN B  1 354 ? 53.260  41.023  43.839 1.00 49.14 ? 544 ASN B ND2 1 
ATOM   5953 N  N   . LYS B  1 355 ? 54.667  38.437  39.841 1.00 29.26 ? 545 LYS B N   1 
ATOM   5954 C  CA  . LYS B  1 355 ? 55.076  37.920  38.543 1.00 29.53 ? 545 LYS B CA  1 
ATOM   5955 C  C   . LYS B  1 355 ? 53.913  37.907  37.556 1.00 26.96 ? 545 LYS B C   1 
ATOM   5956 O  O   . LYS B  1 355 ? 52.889  37.260  37.783 1.00 23.25 ? 545 LYS B O   1 
ATOM   5957 C  CB  . LYS B  1 355 ? 55.689  36.524  38.699 1.00 27.67 ? 545 LYS B CB  1 
ATOM   5958 C  CG  . LYS B  1 355 ? 54.913  35.591  39.604 1.00 31.91 ? 545 LYS B CG  1 
ATOM   5959 C  CD  . LYS B  1 355 ? 55.694  34.313  39.885 1.00 32.20 ? 545 LYS B CD  1 
ATOM   5960 C  CE  . LYS B  1 355 ? 57.000  34.598  40.621 1.00 32.01 ? 545 LYS B CE  1 
ATOM   5961 N  NZ  . LYS B  1 355 ? 57.707  33.344  41.015 1.00 26.13 ? 545 LYS B NZ  1 
ATOM   5962 N  N   . ILE B  1 356 ? 54.092  38.642  36.461 1.00 23.20 ? 546 ILE B N   1 
ATOM   5963 C  CA  . ILE B  1 356 ? 53.085  38.772  35.416 1.00 19.32 ? 546 ILE B CA  1 
ATOM   5964 C  C   . ILE B  1 356 ? 53.199  37.675  34.366 1.00 18.49 ? 546 ILE B C   1 
ATOM   5965 O  O   . ILE B  1 356 ? 54.296  37.336  33.927 1.00 20.57 ? 546 ILE B O   1 
ATOM   5966 C  CB  . ILE B  1 356 ? 53.222  40.126  34.696 1.00 22.19 ? 546 ILE B CB  1 
ATOM   5967 C  CG1 . ILE B  1 356 ? 53.551  41.225  35.710 1.00 19.38 ? 546 ILE B CG1 1 
ATOM   5968 C  CG2 . ILE B  1 356 ? 51.934  40.455  33.957 1.00 21.40 ? 546 ILE B CG2 1 
ATOM   5969 C  CD1 . ILE B  1 356 ? 52.548  41.352  36.835 1.00 20.39 ? 546 ILE B CD1 1 
ATOM   5970 N  N   . PRO B  1 357 ? 52.059  37.112  33.937 1.00 18.89 ? 547 PRO B N   1 
ATOM   5971 C  CA  . PRO B  1 357 ? 52.067  36.051  32.927 1.00 17.28 ? 547 PRO B CA  1 
ATOM   5972 C  C   . PRO B  1 357 ? 52.389  36.602  31.541 1.00 19.46 ? 547 PRO B C   1 
ATOM   5973 O  O   . PRO B  1 357 ? 52.118  37.765  31.254 1.00 25.09 ? 547 PRO B O   1 
ATOM   5974 C  CB  . PRO B  1 357 ? 50.649  35.499  33.010 1.00 12.22 ? 547 PRO B CB  1 
ATOM   5975 C  CG  . PRO B  1 357 ? 49.852  36.726  33.296 1.00 11.99 ? 547 PRO B CG  1 
ATOM   5976 C  CD  . PRO B  1 357 ? 50.679  37.413  34.364 1.00 16.50 ? 547 PRO B CD  1 
ATOM   5977 N  N   . CYS B  1 358 ? 52.980  35.772  30.689 1.00 19.12 ? 548 CYS B N   1 
ATOM   5978 C  CA  . CYS B  1 358 ? 53.304  36.201  29.337 1.00 16.99 ? 548 CYS B CA  1 
ATOM   5979 C  C   . CYS B  1 358 ? 52.036  36.279  28.515 1.00 17.29 ? 548 CYS B C   1 
ATOM   5980 O  O   . CYS B  1 358 ? 51.096  35.512  28.731 1.00 14.30 ? 548 CYS B O   1 
ATOM   5981 C  CB  . CYS B  1 358 ? 54.229  35.209  28.639 1.00 19.10 ? 548 CYS B CB  1 
ATOM   5982 S  SG  . CYS B  1 358 ? 55.973  35.214  29.140 1.00 23.75 ? 548 CYS B SG  1 
ATOM   5983 N  N   . ALA B  1 359 ? 52.015  37.210  27.570 1.00 19.01 ? 549 ALA B N   1 
ATOM   5984 C  CA  . ALA B  1 359 ? 50.881  37.349  26.672 1.00 17.53 ? 549 ALA B CA  1 
ATOM   5985 C  C   . ALA B  1 359 ? 51.162  36.303  25.597 1.00 14.70 ? 549 ALA B C   1 
ATOM   5986 O  O   . ALA B  1 359 ? 52.314  35.929  25.378 1.00 10.63 ? 549 ALA B O   1 
ATOM   5987 C  CB  . ALA B  1 359 ? 50.848  38.749  26.066 1.00 12.03 ? 549 ALA B CB  1 
ATOM   5988 N  N   . PRO B  1 360 ? 50.119  35.812  24.915 1.00 19.68 ? 550 PRO B N   1 
ATOM   5989 C  CA  . PRO B  1 360 ? 50.308  34.801  23.869 1.00 22.13 ? 550 PRO B CA  1 
ATOM   5990 C  C   . PRO B  1 360 ? 51.483  35.052  22.917 1.00 22.16 ? 550 PRO B C   1 
ATOM   5991 O  O   . PRO B  1 360 ? 52.129  34.110  22.467 1.00 20.36 ? 550 PRO B O   1 
ATOM   5992 C  CB  . PRO B  1 360 ? 48.965  34.807  23.151 1.00 16.27 ? 550 PRO B CB  1 
ATOM   5993 C  CG  . PRO B  1 360 ? 48.013  35.056  24.276 1.00 18.60 ? 550 PRO B CG  1 
ATOM   5994 C  CD  . PRO B  1 360 ? 48.695  36.171  25.046 1.00 16.89 ? 550 PRO B CD  1 
ATOM   5995 N  N   . GLU B  1 361 ? 51.765  36.319  22.628 1.00 26.94 ? 551 GLU B N   1 
ATOM   5996 C  CA  . GLU B  1 361 ? 52.846  36.677  21.713 1.00 27.71 ? 551 GLU B CA  1 
ATOM   5997 C  C   . GLU B  1 361 ? 54.209  36.879  22.372 1.00 29.05 ? 551 GLU B C   1 
ATOM   5998 O  O   . GLU B  1 361 ? 55.223  36.952  21.680 1.00 32.80 ? 551 GLU B O   1 
ATOM   5999 C  CB  . GLU B  1 361 ? 52.490  37.954  20.947 1.00 29.77 ? 551 GLU B CB  1 
ATOM   6000 C  CG  . GLU B  1 361 ? 51.047  38.037  20.483 1.00 42.86 ? 551 GLU B CG  1 
ATOM   6001 C  CD  . GLU B  1 361 ? 50.106  38.471  21.592 1.00 48.89 ? 551 GLU B CD  1 
ATOM   6002 O  OE1 . GLU B  1 361 ? 48.874  38.463  21.373 1.00 52.77 ? 551 GLU B OE1 1 
ATOM   6003 O  OE2 . GLU B  1 361 ? 50.602  38.827  22.683 1.00 49.36 ? 551 GLU B OE2 1 
ATOM   6004 N  N   . ASP B  1 362 ? 54.241  36.976  23.697 1.00 28.28 ? 552 ASP B N   1 
ATOM   6005 C  CA  . ASP B  1 362 ? 55.501  37.188  24.409 1.00 27.23 ? 552 ASP B CA  1 
ATOM   6006 C  C   . ASP B  1 362 ? 55.956  35.921  25.117 1.00 24.27 ? 552 ASP B C   1 
ATOM   6007 O  O   . ASP B  1 362 ? 56.862  35.947  25.950 1.00 22.44 ? 552 ASP B O   1 
ATOM   6008 C  CB  . ASP B  1 362 ? 55.335  38.307  25.437 1.00 26.20 ? 552 ASP B CB  1 
ATOM   6009 C  CG  . ASP B  1 362 ? 54.852  39.601  24.816 1.00 32.63 ? 552 ASP B CG  1 
ATOM   6010 O  OD1 . ASP B  1 362 ? 55.522  40.097  23.883 1.00 35.15 ? 552 ASP B OD1 1 
ATOM   6011 O  OD2 . ASP B  1 362 ? 53.806  40.124  25.262 1.00 31.50 ? 552 ASP B OD2 1 
ATOM   6012 N  N   . VAL B  1 363 ? 55.323  34.812  24.760 1.00 23.32 ? 553 VAL B N   1 
ATOM   6013 C  CA  . VAL B  1 363 ? 55.598  33.515  25.361 1.00 22.10 ? 553 VAL B CA  1 
ATOM   6014 C  C   . VAL B  1 363 ? 57.054  33.028  25.293 1.00 22.20 ? 553 VAL B C   1 
ATOM   6015 O  O   . VAL B  1 363 ? 57.491  32.256  26.145 1.00 23.92 ? 553 VAL B O   1 
ATOM   6016 C  CB  . VAL B  1 363 ? 54.666  32.453  24.739 1.00 16.28 ? 553 VAL B CB  1 
ATOM   6017 C  CG1 . VAL B  1 363 ? 55.401  31.650  23.679 1.00 15.55 ? 553 VAL B CG1 1 
ATOM   6018 C  CG2 . VAL B  1 363 ? 54.105  31.574  25.820 1.00 18.90 ? 553 VAL B CG2 1 
ATOM   6019 N  N   . LYS B  1 364 ? 57.798  33.472  24.285 1.00 21.35 ? 554 LYS B N   1 
ATOM   6020 C  CA  . LYS B  1 364 ? 59.192  33.064  24.130 1.00 22.21 ? 554 LYS B CA  1 
ATOM   6021 C  C   . LYS B  1 364 ? 60.141  33.952  24.931 1.00 22.85 ? 554 LYS B C   1 
ATOM   6022 O  O   . LYS B  1 364 ? 61.360  33.836  24.804 1.00 26.78 ? 554 LYS B O   1 
ATOM   6023 C  CB  . LYS B  1 364 ? 59.608  33.117  22.656 1.00 24.80 ? 554 LYS B CB  1 
ATOM   6024 C  CG  . LYS B  1 364 ? 59.032  32.032  21.763 1.00 25.65 ? 554 LYS B CG  1 
ATOM   6025 C  CD  . LYS B  1 364 ? 59.600  30.673  22.109 1.00 32.54 ? 554 LYS B CD  1 
ATOM   6026 C  CE  . LYS B  1 364 ? 59.629  29.766  20.888 1.00 37.92 ? 554 LYS B CE  1 
ATOM   6027 N  NZ  . LYS B  1 364 ? 58.308  29.678  20.214 1.00 38.95 ? 554 LYS B NZ  1 
ATOM   6028 N  N   . CYS B  1 365 ? 59.590  34.836  25.754 1.00 21.42 ? 555 CYS B N   1 
ATOM   6029 C  CA  . CYS B  1 365 ? 60.423  35.735  26.539 1.00 20.61 ? 555 CYS B CA  1 
ATOM   6030 C  C   . CYS B  1 365 ? 60.277  35.564  28.038 1.00 20.80 ? 555 CYS B C   1 
ATOM   6031 O  O   . CYS B  1 365 ? 60.692  36.434  28.807 1.00 23.02 ? 555 CYS B O   1 
ATOM   6032 C  CB  . CYS B  1 365 ? 60.127  37.186  26.168 1.00 20.10 ? 555 CYS B CB  1 
ATOM   6033 S  SG  . CYS B  1 365 ? 60.601  37.611  24.465 1.00 29.77 ? 555 CYS B SG  1 
ATOM   6034 N  N   . GLY B  1 366 ? 59.683  34.451  28.454 1.00 17.57 ? 556 GLY B N   1 
ATOM   6035 C  CA  . GLY B  1 366 ? 59.517  34.196  29.872 1.00 17.78 ? 556 GLY B CA  1 
ATOM   6036 C  C   . GLY B  1 366 ? 60.461  33.090  30.307 1.00 22.32 ? 556 GLY B C   1 
ATOM   6037 O  O   . GLY B  1 366 ? 61.648  33.099  29.961 1.00 19.92 ? 556 GLY B O   1 
ATOM   6038 N  N   . ARG B  1 367 ? 59.941  32.134  31.069 1.00 18.59 ? 557 ARG B N   1 
ATOM   6039 C  CA  . ARG B  1 367 ? 60.758  31.019  31.518 1.00 15.78 ? 557 ARG B CA  1 
ATOM   6040 C  C   . ARG B  1 367 ? 61.209  30.274  30.276 1.00 13.75 ? 557 ARG B C   1 
ATOM   6041 O  O   . ARG B  1 367 ? 60.444  30.140  29.325 1.00 14.17 ? 557 ARG B O   1 
ATOM   6042 C  CB  . ARG B  1 367 ? 59.942  30.076  32.401 1.00 17.73 ? 557 ARG B CB  1 
ATOM   6043 C  CG  . ARG B  1 367 ? 60.738  28.921  32.987 1.00 7.46  ? 557 ARG B CG  1 
ATOM   6044 C  CD  . ARG B  1 367 ? 61.754  29.411  34.007 1.00 11.63 ? 557 ARG B CD  1 
ATOM   6045 N  NE  . ARG B  1 367 ? 61.131  30.280  35.002 1.00 6.48  ? 557 ARG B NE  1 
ATOM   6046 C  CZ  . ARG B  1 367 ? 61.764  30.796  36.049 1.00 3.19  ? 557 ARG B CZ  1 
ATOM   6047 N  NH1 . ARG B  1 367 ? 63.045  30.529  36.249 1.00 5.18  ? 557 ARG B NH1 1 
ATOM   6048 N  NH2 . ARG B  1 367 ? 61.116  31.586  36.894 1.00 9.50  ? 557 ARG B NH2 1 
ATOM   6049 N  N   . LEU B  1 368 ? 62.449  29.802  30.282 1.00 17.03 ? 558 LEU B N   1 
ATOM   6050 C  CA  . LEU B  1 368 ? 62.989  29.056  29.150 1.00 17.49 ? 558 LEU B CA  1 
ATOM   6051 C  C   . LEU B  1 368 ? 62.655  27.570  29.274 1.00 16.13 ? 558 LEU B C   1 
ATOM   6052 O  O   . LEU B  1 368 ? 62.551  27.038  30.378 1.00 18.44 ? 558 LEU B O   1 
ATOM   6053 C  CB  . LEU B  1 368 ? 64.508  29.240  29.078 1.00 10.28 ? 558 LEU B CB  1 
ATOM   6054 C  CG  . LEU B  1 368 ? 65.277  28.280  28.162 1.00 16.86 ? 558 LEU B CG  1 
ATOM   6055 C  CD1 . LEU B  1 368 ? 64.745  28.375  26.737 1.00 15.69 ? 558 LEU B CD1 1 
ATOM   6056 C  CD2 . LEU B  1 368 ? 66.769  28.613  28.208 1.00 12.08 ? 558 LEU B CD2 1 
ATOM   6057 N  N   . TYR B  1 369 ? 62.474  26.910  28.136 1.00 18.77 ? 559 TYR B N   1 
ATOM   6058 C  CA  . TYR B  1 369 ? 62.168  25.483  28.111 1.00 17.56 ? 559 TYR B CA  1 
ATOM   6059 C  C   . TYR B  1 369 ? 63.064  24.799  27.091 1.00 21.97 ? 559 TYR B C   1 
ATOM   6060 O  O   . TYR B  1 369 ? 63.300  25.331  26.005 1.00 21.62 ? 559 TYR B O   1 
ATOM   6061 C  CB  . TYR B  1 369 ? 60.702  25.251  27.750 1.00 14.07 ? 559 TYR B CB  1 
ATOM   6062 C  CG  . TYR B  1 369 ? 59.743  25.907  28.709 1.00 17.74 ? 559 TYR B CG  1 
ATOM   6063 C  CD1 . TYR B  1 369 ? 59.427  27.258  28.593 1.00 20.13 ? 559 TYR B CD1 1 
ATOM   6064 C  CD2 . TYR B  1 369 ? 59.189  25.192  29.767 1.00 13.25 ? 559 TYR B CD2 1 
ATOM   6065 C  CE1 . TYR B  1 369 ? 58.588  27.882  29.506 1.00 15.54 ? 559 TYR B CE1 1 
ATOM   6066 C  CE2 . TYR B  1 369 ? 58.351  25.806  30.684 1.00 17.21 ? 559 TYR B CE2 1 
ATOM   6067 C  CZ  . TYR B  1 369 ? 58.055  27.153  30.547 1.00 14.83 ? 559 TYR B CZ  1 
ATOM   6068 O  OH  . TYR B  1 369 ? 57.222  27.767  31.452 1.00 17.36 ? 559 TYR B OH  1 
ATOM   6069 N  N   . CYS B  1 370 ? 63.565  23.620  27.439 1.00 22.30 ? 560 CYS B N   1 
ATOM   6070 C  CA  . CYS B  1 370 ? 64.446  22.894  26.542 1.00 27.36 ? 560 CYS B CA  1 
ATOM   6071 C  C   . CYS B  1 370 ? 64.038  21.427  26.439 1.00 30.92 ? 560 CYS B C   1 
ATOM   6072 O  O   . CYS B  1 370 ? 63.337  20.911  27.306 1.00 31.13 ? 560 CYS B O   1 
ATOM   6073 C  CB  . CYS B  1 370 ? 65.886  23.009  27.044 1.00 25.82 ? 560 CYS B CB  1 
ATOM   6074 S  SG  . CYS B  1 370 ? 66.364  24.697  27.552 1.00 23.69 ? 560 CYS B SG  1 
ATOM   6075 N  N   . LYS B  1 371 ? 64.475  20.766  25.369 1.00 36.51 ? 561 LYS B N   1 
ATOM   6076 C  CA  . LYS B  1 371 ? 64.165  19.357  25.144 1.00 37.50 ? 561 LYS B CA  1 
ATOM   6077 C  C   . LYS B  1 371 ? 65.406  18.494  25.359 1.00 40.51 ? 561 LYS B C   1 
ATOM   6078 O  O   . LYS B  1 371 ? 66.497  18.828  24.890 1.00 36.99 ? 561 LYS B O   1 
ATOM   6079 C  CB  . LYS B  1 371 ? 63.643  19.142  23.720 1.00 40.46 ? 561 LYS B CB  1 
ATOM   6080 C  CG  . LYS B  1 371 ? 64.644  19.503  22.630 1.00 43.73 ? 561 LYS B CG  1 
ATOM   6081 C  CD  . LYS B  1 371 ? 64.379  18.729  21.341 1.00 45.86 ? 561 LYS B CD  1 
ATOM   6082 C  CE  . LYS B  1 371 ? 63.069  19.132  20.684 1.00 46.05 ? 561 LYS B CE  1 
ATOM   6083 N  NZ  . LYS B  1 371 ? 63.121  20.526  20.172 1.00 47.96 ? 561 LYS B NZ  1 
ATOM   6084 N  N   . ASP B  1 372 ? 65.234  17.380  26.061 1.00 44.06 ? 562 ASP B N   1 
ATOM   6085 C  CA  . ASP B  1 372 ? 66.344  16.477  26.339 1.00 49.34 ? 562 ASP B CA  1 
ATOM   6086 C  C   . ASP B  1 372 ? 66.268  15.234  25.454 1.00 49.81 ? 562 ASP B C   1 
ATOM   6087 O  O   . ASP B  1 372 ? 65.483  14.325  25.721 1.00 49.40 ? 562 ASP B O   1 
ATOM   6088 C  CB  . ASP B  1 372 ? 66.320  16.066  27.813 1.00 53.72 ? 562 ASP B CB  1 
ATOM   6089 C  CG  . ASP B  1 372 ? 67.625  15.444  28.266 1.00 57.61 ? 562 ASP B CG  1 
ATOM   6090 O  OD1 . ASP B  1 372 ? 67.690  14.975  29.423 1.00 60.41 ? 562 ASP B OD1 1 
ATOM   6091 O  OD2 . ASP B  1 372 ? 68.587  15.431  27.469 1.00 56.74 ? 562 ASP B OD2 1 
ATOM   6092 N  N   . ASN B  1 373 ? 67.086  15.196  24.406 1.00 49.39 ? 563 ASN B N   1 
ATOM   6093 C  CA  . ASN B  1 373 ? 67.094  14.059  23.488 1.00 53.00 ? 563 ASN B CA  1 
ATOM   6094 C  C   . ASN B  1 373 ? 67.994  12.923  23.962 1.00 52.41 ? 563 ASN B C   1 
ATOM   6095 O  O   . ASN B  1 373 ? 68.842  12.438  23.213 1.00 52.79 ? 563 ASN B O   1 
ATOM   6096 C  CB  . ASN B  1 373 ? 67.527  14.508  22.087 1.00 58.94 ? 563 ASN B CB  1 
ATOM   6097 C  CG  . ASN B  1 373 ? 66.483  15.374  21.399 1.00 64.10 ? 563 ASN B CG  1 
ATOM   6098 O  OD1 . ASN B  1 373 ? 66.670  15.807  20.261 1.00 61.37 ? 563 ASN B OD1 1 
ATOM   6099 N  ND2 . ASN B  1 373 ? 65.375  15.629  22.089 1.00 67.67 ? 563 ASN B ND2 1 
ATOM   6100 N  N   . SER B  1 374 ? 67.799  12.499  25.207 1.00 50.63 ? 564 SER B N   1 
ATOM   6101 C  CA  . SER B  1 374 ? 68.586  11.415  25.787 1.00 46.04 ? 564 SER B CA  1 
ATOM   6102 C  C   . SER B  1 374 ? 67.768  10.130  25.764 1.00 45.16 ? 564 SER B C   1 
ATOM   6103 O  O   . SER B  1 374 ? 66.570  10.146  26.049 1.00 48.62 ? 564 SER B O   1 
ATOM   6104 C  CB  . SER B  1 374 ? 68.948  11.740  27.236 1.00 44.44 ? 564 SER B CB  1 
ATOM   6105 O  OG  . SER B  1 374 ? 69.551  13.015  27.345 1.00 53.80 ? 564 SER B OG  1 
ATOM   6106 N  N   . PRO B  1 375 ? 68.402  8.997   25.427 1.00 40.42 ? 565 PRO B N   1 
ATOM   6107 C  CA  . PRO B  1 375 ? 67.666  7.732   25.394 1.00 39.51 ? 565 PRO B CA  1 
ATOM   6108 C  C   . PRO B  1 375 ? 66.995  7.465   26.739 1.00 42.23 ? 565 PRO B C   1 
ATOM   6109 O  O   . PRO B  1 375 ? 67.606  7.658   27.791 1.00 41.45 ? 565 PRO B O   1 
ATOM   6110 C  CB  . PRO B  1 375 ? 68.752  6.711   25.069 1.00 35.35 ? 565 PRO B CB  1 
ATOM   6111 C  CG  . PRO B  1 375 ? 69.985  7.333   25.646 1.00 37.24 ? 565 PRO B CG  1 
ATOM   6112 C  CD  . PRO B  1 375 ? 69.841  8.769   25.223 1.00 36.99 ? 565 PRO B CD  1 
ATOM   6113 N  N   . GLY B  1 376 ? 65.735  7.037   26.699 1.00 43.09 ? 566 GLY B N   1 
ATOM   6114 C  CA  . GLY B  1 376 ? 65.011  6.762   27.927 1.00 44.56 ? 566 GLY B CA  1 
ATOM   6115 C  C   . GLY B  1 376 ? 64.380  8.013   28.508 1.00 47.94 ? 566 GLY B C   1 
ATOM   6116 O  O   . GLY B  1 376 ? 63.171  8.212   28.390 1.00 49.51 ? 566 GLY B O   1 
ATOM   6117 N  N   . GLN B  1 377 ? 65.195  8.855   29.142 1.00 51.04 ? 567 GLN B N   1 
ATOM   6118 C  CA  . GLN B  1 377 ? 64.702  10.097  29.728 1.00 52.82 ? 567 GLN B CA  1 
ATOM   6119 C  C   . GLN B  1 377 ? 64.012  10.925  28.652 1.00 54.66 ? 567 GLN B C   1 
ATOM   6120 O  O   . GLN B  1 377 ? 64.657  11.405  27.719 1.00 50.78 ? 567 GLN B O   1 
ATOM   6121 C  CB  . GLN B  1 377 ? 65.849  10.916  30.336 1.00 55.13 ? 567 GLN B CB  1 
ATOM   6122 C  CG  . GLN B  1 377 ? 66.313  10.465  31.723 1.00 57.16 ? 567 GLN B CG  1 
ATOM   6123 C  CD  . GLN B  1 377 ? 67.113  9.175   31.699 1.00 57.54 ? 567 GLN B CD  1 
ATOM   6124 O  OE1 . GLN B  1 377 ? 66.611  8.122   31.301 1.00 55.09 ? 567 GLN B OE1 1 
ATOM   6125 N  NE2 . GLN B  1 377 ? 68.369  9.252   32.128 1.00 57.66 ? 567 GLN B NE2 1 
ATOM   6126 N  N   . ASN B  1 378 ? 62.699  11.087  28.790 1.00 56.94 ? 568 ASN B N   1 
ATOM   6127 C  CA  . ASN B  1 378 ? 61.917  11.851  27.828 1.00 57.14 ? 568 ASN B CA  1 
ATOM   6128 C  C   . ASN B  1 378 ? 61.114  12.987  28.456 1.00 53.40 ? 568 ASN B C   1 
ATOM   6129 O  O   . ASN B  1 378 ? 59.946  12.812  28.806 1.00 51.87 ? 568 ASN B O   1 
ATOM   6130 C  CB  . ASN B  1 378 ? 60.969  10.921  27.063 1.00 62.86 ? 568 ASN B CB  1 
ATOM   6131 C  CG  . ASN B  1 378 ? 59.869  11.678  26.329 1.00 66.50 ? 568 ASN B CG  1 
ATOM   6132 O  OD1 . ASN B  1 378 ? 60.136  12.629  25.594 1.00 67.74 ? 568 ASN B OD1 1 
ATOM   6133 N  ND2 . ASN B  1 378 ? 58.625  11.254  26.527 1.00 67.75 ? 568 ASN B ND2 1 
ATOM   6134 N  N   . ASN B  1 379 ? 61.748  14.147  28.605 1.00 49.41 ? 569 ASN B N   1 
ATOM   6135 C  CA  . ASN B  1 379 ? 61.074  15.321  29.151 1.00 46.38 ? 569 ASN B CA  1 
ATOM   6136 C  C   . ASN B  1 379 ? 61.087  16.375  28.049 1.00 42.79 ? 569 ASN B C   1 
ATOM   6137 O  O   . ASN B  1 379 ? 62.119  16.992  27.777 1.00 43.60 ? 569 ASN B O   1 
ATOM   6138 C  CB  . ASN B  1 379 ? 61.800  15.864  30.384 1.00 44.58 ? 569 ASN B CB  1 
ATOM   6139 C  CG  . ASN B  1 379 ? 60.988  16.923  31.117 1.00 43.33 ? 569 ASN B CG  1 
ATOM   6140 O  OD1 . ASN B  1 379 ? 60.405  17.815  30.497 1.00 37.63 ? 569 ASN B OD1 1 
ATOM   6141 N  ND2 . ASN B  1 379 ? 60.953  16.832  32.442 1.00 44.93 ? 569 ASN B ND2 1 
ATOM   6142 N  N   . PRO B  1 380 ? 59.936  16.590  27.398 1.00 38.21 ? 570 PRO B N   1 
ATOM   6143 C  CA  . PRO B  1 380 ? 59.804  17.566  26.314 1.00 38.31 ? 570 PRO B CA  1 
ATOM   6144 C  C   . PRO B  1 380 ? 59.964  19.038  26.714 1.00 37.69 ? 570 PRO B C   1 
ATOM   6145 O  O   . PRO B  1 380 ? 60.426  19.852  25.912 1.00 37.10 ? 570 PRO B O   1 
ATOM   6146 C  CB  . PRO B  1 380 ? 58.418  17.261  25.754 1.00 35.81 ? 570 PRO B CB  1 
ATOM   6147 C  CG  . PRO B  1 380 ? 57.663  16.840  26.976 1.00 37.62 ? 570 PRO B CG  1 
ATOM   6148 C  CD  . PRO B  1 380 ? 58.647  15.928  27.668 1.00 36.38 ? 570 PRO B CD  1 
ATOM   6149 N  N   . CYS B  1 381 ? 59.591  19.381  27.944 1.00 34.11 ? 571 CYS B N   1 
ATOM   6150 C  CA  . CYS B  1 381 ? 59.700  20.764  28.391 1.00 33.51 ? 571 CYS B CA  1 
ATOM   6151 C  C   . CYS B  1 381 ? 60.584  20.959  29.624 1.00 33.29 ? 571 CYS B C   1 
ATOM   6152 O  O   . CYS B  1 381 ? 60.095  21.385  30.673 1.00 33.36 ? 571 CYS B O   1 
ATOM   6153 C  CB  . CYS B  1 381 ? 58.315  21.338  28.695 1.00 30.53 ? 571 CYS B CB  1 
ATOM   6154 S  SG  . CYS B  1 381 ? 57.054  21.184  27.387 1.00 36.72 ? 571 CYS B SG  1 
ATOM   6155 N  N   . LYS B  1 382 ? 61.875  20.655  29.508 1.00 28.93 ? 572 LYS B N   1 
ATOM   6156 C  CA  . LYS B  1 382 ? 62.774  20.841  30.642 1.00 27.51 ? 572 LYS B CA  1 
ATOM   6157 C  C   . LYS B  1 382 ? 62.899  22.326  30.925 1.00 25.31 ? 572 LYS B C   1 
ATOM   6158 O  O   . LYS B  1 382 ? 63.097  23.134  30.016 1.00 26.11 ? 572 LYS B O   1 
ATOM   6159 C  CB  . LYS B  1 382 ? 64.167  20.264  30.368 1.00 30.83 ? 572 LYS B CB  1 
ATOM   6160 C  CG  . LYS B  1 382 ? 64.221  18.746  30.320 1.00 41.79 ? 572 LYS B CG  1 
ATOM   6161 C  CD  . LYS B  1 382 ? 65.641  18.236  30.517 1.00 45.24 ? 572 LYS B CD  1 
ATOM   6162 C  CE  . LYS B  1 382 ? 66.127  18.496  31.936 1.00 46.30 ? 572 LYS B CE  1 
ATOM   6163 N  NZ  . LYS B  1 382 ? 65.286  17.792  32.947 1.00 47.16 ? 572 LYS B NZ  1 
ATOM   6164 N  N   . MET B  1 383 ? 62.786  22.677  32.195 1.00 21.49 ? 573 MET B N   1 
ATOM   6165 C  CA  . MET B  1 383 ? 62.873  24.061  32.612 1.00 20.51 ? 573 MET B CA  1 
ATOM   6166 C  C   . MET B  1 383 ? 63.638  24.137  33.924 1.00 20.29 ? 573 MET B C   1 
ATOM   6167 O  O   . MET B  1 383 ? 63.724  23.154  34.652 1.00 21.82 ? 573 MET B O   1 
ATOM   6168 C  CB  . MET B  1 383 ? 61.455  24.622  32.756 1.00 19.20 ? 573 MET B CB  1 
ATOM   6169 C  CG  . MET B  1 383 ? 61.316  25.826  33.649 1.00 23.58 ? 573 MET B CG  1 
ATOM   6170 S  SD  . MET B  1 383 ? 61.256  25.375  35.387 1.00 28.63 ? 573 MET B SD  1 
ATOM   6171 C  CE  . MET B  1 383 ? 59.600  24.749  35.518 1.00 17.81 ? 573 MET B CE  1 
ATOM   6172 N  N   . PHE B  1 384 ? 64.207  25.298  34.220 1.00 18.26 ? 574 PHE B N   1 
ATOM   6173 C  CA  . PHE B  1 384 ? 64.950  25.458  35.457 1.00 19.09 ? 574 PHE B CA  1 
ATOM   6174 C  C   . PHE B  1 384 ? 64.342  26.521  36.362 1.00 21.28 ? 574 PHE B C   1 
ATOM   6175 O  O   . PHE B  1 384 ? 64.098  27.653  35.939 1.00 24.29 ? 574 PHE B O   1 
ATOM   6176 C  CB  . PHE B  1 384 ? 66.410  25.802  35.159 1.00 22.90 ? 574 PHE B CB  1 
ATOM   6177 C  CG  . PHE B  1 384 ? 67.260  25.947  36.389 1.00 26.66 ? 574 PHE B CG  1 
ATOM   6178 C  CD1 . PHE B  1 384 ? 67.243  27.125  37.131 1.00 29.78 ? 574 PHE B CD1 1 
ATOM   6179 C  CD2 . PHE B  1 384 ? 68.058  24.892  36.823 1.00 28.47 ? 574 PHE B CD2 1 
ATOM   6180 C  CE1 . PHE B  1 384 ? 68.007  27.251  38.288 1.00 29.93 ? 574 PHE B CE1 1 
ATOM   6181 C  CE2 . PHE B  1 384 ? 68.825  25.005  37.978 1.00 27.24 ? 574 PHE B CE2 1 
ATOM   6182 C  CZ  . PHE B  1 384 ? 68.799  26.189  38.713 1.00 33.00 ? 574 PHE B CZ  1 
ATOM   6183 N  N   . TYR B  1 385 ? 64.094  26.139  37.611 1.00 18.21 ? 575 TYR B N   1 
ATOM   6184 C  CA  . TYR B  1 385 ? 63.537  27.044  38.604 1.00 13.62 ? 575 TYR B CA  1 
ATOM   6185 C  C   . TYR B  1 385 ? 64.150  26.793  39.972 1.00 13.21 ? 575 TYR B C   1 
ATOM   6186 O  O   . TYR B  1 385 ? 64.284  25.651  40.403 1.00 9.98  ? 575 TYR B O   1 
ATOM   6187 C  CB  . TYR B  1 385 ? 62.018  26.885  38.729 1.00 15.94 ? 575 TYR B CB  1 
ATOM   6188 C  CG  . TYR B  1 385 ? 61.461  27.738  39.851 1.00 10.41 ? 575 TYR B CG  1 
ATOM   6189 C  CD1 . TYR B  1 385 ? 61.242  29.099  39.672 1.00 6.36  ? 575 TYR B CD1 1 
ATOM   6190 C  CD2 . TYR B  1 385 ? 61.260  27.205  41.122 1.00 12.51 ? 575 TYR B CD2 1 
ATOM   6191 C  CE1 . TYR B  1 385 ? 60.844  29.910  40.729 1.00 17.74 ? 575 TYR B CE1 1 
ATOM   6192 C  CE2 . TYR B  1 385 ? 60.865  28.004  42.185 1.00 13.64 ? 575 TYR B CE2 1 
ATOM   6193 C  CZ  . TYR B  1 385 ? 60.658  29.356  41.984 1.00 18.66 ? 575 TYR B CZ  1 
ATOM   6194 O  OH  . TYR B  1 385 ? 60.269  30.154  43.038 1.00 19.97 ? 575 TYR B OH  1 
ATOM   6195 N  N   . SER B  1 386 ? 64.498  27.877  40.656 1.00 16.85 ? 576 SER B N   1 
ATOM   6196 C  CA  . SER B  1 386 ? 65.082  27.813  41.988 1.00 18.51 ? 576 SER B CA  1 
ATOM   6197 C  C   . SER B  1 386 ? 64.742  29.117  42.692 1.00 22.24 ? 576 SER B C   1 
ATOM   6198 O  O   . SER B  1 386 ? 65.044  30.196  42.183 1.00 21.94 ? 576 SER B O   1 
ATOM   6199 C  CB  . SER B  1 386 ? 66.598  27.650  41.898 1.00 20.12 ? 576 SER B CB  1 
ATOM   6200 O  OG  . SER B  1 386 ? 67.182  27.661  43.186 1.00 21.66 ? 576 SER B OG  1 
ATOM   6201 N  N   . ASN B  1 387 ? 64.110  29.023  43.859 1.00 25.08 ? 577 ASN B N   1 
ATOM   6202 C  CA  . ASN B  1 387 ? 63.727  30.221  44.594 1.00 22.22 ? 577 ASN B CA  1 
ATOM   6203 C  C   . ASN B  1 387 ? 64.921  30.921  45.223 1.00 22.21 ? 577 ASN B C   1 
ATOM   6204 O  O   . ASN B  1 387 ? 64.759  31.834  46.029 1.00 25.10 ? 577 ASN B O   1 
ATOM   6205 C  CB  . ASN B  1 387 ? 62.681  29.886  45.660 1.00 19.61 ? 577 ASN B CB  1 
ATOM   6206 C  CG  . ASN B  1 387 ? 63.249  29.095  46.807 1.00 13.40 ? 577 ASN B CG  1 
ATOM   6207 O  OD1 . ASN B  1 387 ? 64.217  28.358  46.646 1.00 26.57 ? 577 ASN B OD1 1 
ATOM   6208 N  ND2 . ASN B  1 387 ? 62.637  29.228  47.975 1.00 11.94 ? 577 ASN B ND2 1 
ATOM   6209 N  N   . GLU B  1 388 ? 66.122  30.485  44.859 1.00 23.51 ? 578 GLU B N   1 
ATOM   6210 C  CA  . GLU B  1 388 ? 67.336  31.116  45.360 1.00 26.69 ? 578 GLU B CA  1 
ATOM   6211 C  C   . GLU B  1 388 ? 67.587  32.289  44.416 1.00 26.08 ? 578 GLU B C   1 
ATOM   6212 O  O   . GLU B  1 388 ? 68.097  33.336  44.814 1.00 25.92 ? 578 GLU B O   1 
ATOM   6213 C  CB  . GLU B  1 388 ? 68.517  30.137  45.318 1.00 29.05 ? 578 GLU B CB  1 
ATOM   6214 C  CG  . GLU B  1 388 ? 69.808  30.697  45.917 1.00 36.63 ? 578 GLU B CG  1 
ATOM   6215 C  CD  . GLU B  1 388 ? 70.925  29.663  46.032 1.00 39.58 ? 578 GLU B CD  1 
ATOM   6216 O  OE1 . GLU B  1 388 ? 72.047  30.050  46.418 1.00 40.79 ? 578 GLU B OE1 1 
ATOM   6217 O  OE2 . GLU B  1 388 ? 70.690  28.469  45.743 1.00 39.63 ? 578 GLU B OE2 1 
ATOM   6218 N  N   . ASP B  1 389 ? 67.199  32.090  43.159 1.00 23.43 ? 579 ASP B N   1 
ATOM   6219 C  CA  . ASP B  1 389 ? 67.333  33.089  42.109 1.00 21.95 ? 579 ASP B CA  1 
ATOM   6220 C  C   . ASP B  1 389 ? 66.308  32.755  41.025 1.00 23.46 ? 579 ASP B C   1 
ATOM   6221 O  O   . ASP B  1 389 ? 66.584  32.007  40.085 1.00 18.19 ? 579 ASP B O   1 
ATOM   6222 C  CB  . ASP B  1 389 ? 68.749  33.067  41.531 1.00 27.55 ? 579 ASP B CB  1 
ATOM   6223 C  CG  . ASP B  1 389 ? 68.979  34.170  40.517 1.00 36.26 ? 579 ASP B CG  1 
ATOM   6224 O  OD1 . ASP B  1 389 ? 68.618  35.329  40.812 1.00 40.74 ? 579 ASP B OD1 1 
ATOM   6225 O  OD2 . ASP B  1 389 ? 69.525  33.883  39.430 1.00 42.81 ? 579 ASP B OD2 1 
ATOM   6226 N  N   . GLU B  1 390 ? 65.113  33.312  41.173 1.00 24.66 ? 580 GLU B N   1 
ATOM   6227 C  CA  . GLU B  1 390 ? 64.032  33.060  40.234 1.00 20.88 ? 580 GLU B CA  1 
ATOM   6228 C  C   . GLU B  1 390 ? 64.345  33.525  38.820 1.00 23.21 ? 580 GLU B C   1 
ATOM   6229 O  O   . GLU B  1 390 ? 63.739  33.049  37.859 1.00 25.75 ? 580 GLU B O   1 
ATOM   6230 C  CB  . GLU B  1 390 ? 62.746  33.718  40.738 1.00 14.91 ? 580 GLU B CB  1 
ATOM   6231 C  CG  . GLU B  1 390 ? 62.366  33.293  42.152 1.00 21.30 ? 580 GLU B CG  1 
ATOM   6232 C  CD  . GLU B  1 390 ? 61.007  33.815  42.587 1.00 26.94 ? 580 GLU B CD  1 
ATOM   6233 O  OE1 . GLU B  1 390 ? 60.803  35.046  42.555 1.00 29.06 ? 580 GLU B OE1 1 
ATOM   6234 O  OE2 . GLU B  1 390 ? 60.141  32.994  42.965 1.00 30.25 ? 580 GLU B OE2 1 
ATOM   6235 N  N   . HIS B  1 391 ? 65.299  34.442  38.684 1.00 27.68 ? 581 HIS B N   1 
ATOM   6236 C  CA  . HIS B  1 391 ? 65.657  34.950  37.364 1.00 26.08 ? 581 HIS B CA  1 
ATOM   6237 C  C   . HIS B  1 391 ? 66.448  33.934  36.547 1.00 22.60 ? 581 HIS B C   1 
ATOM   6238 O  O   . HIS B  1 391 ? 66.374  33.921  35.318 1.00 21.53 ? 581 HIS B O   1 
ATOM   6239 C  CB  . HIS B  1 391 ? 66.455  36.249  37.474 1.00 27.27 ? 581 HIS B CB  1 
ATOM   6240 C  CG  . HIS B  1 391 ? 66.755  36.876  36.149 1.00 33.03 ? 581 HIS B CG  1 
ATOM   6241 N  ND1 . HIS B  1 391 ? 65.766  37.313  35.294 1.00 31.62 ? 581 HIS B ND1 1 
ATOM   6242 C  CD2 . HIS B  1 391 ? 67.929  37.102  35.512 1.00 30.64 ? 581 HIS B CD2 1 
ATOM   6243 C  CE1 . HIS B  1 391 ? 66.317  37.779  34.187 1.00 25.71 ? 581 HIS B CE1 1 
ATOM   6244 N  NE2 . HIS B  1 391 ? 67.628  37.662  34.294 1.00 29.13 ? 581 HIS B NE2 1 
ATOM   6245 N  N   . LYS B  1 392 ? 67.214  33.087  37.221 1.00 19.13 ? 582 LYS B N   1 
ATOM   6246 C  CA  . LYS B  1 392 ? 67.976  32.074  36.508 1.00 19.25 ? 582 LYS B CA  1 
ATOM   6247 C  C   . LYS B  1 392 ? 66.973  31.131  35.839 1.00 21.53 ? 582 LYS B C   1 
ATOM   6248 O  O   . LYS B  1 392 ? 66.020  30.675  36.474 1.00 22.77 ? 582 LYS B O   1 
ATOM   6249 C  CB  . LYS B  1 392 ? 68.877  31.301  37.478 1.00 13.88 ? 582 LYS B CB  1 
ATOM   6250 C  CG  . LYS B  1 392 ? 69.748  30.255  36.804 1.00 18.69 ? 582 LYS B CG  1 
ATOM   6251 C  CD  . LYS B  1 392 ? 70.685  29.564  37.786 1.00 21.62 ? 582 LYS B CD  1 
ATOM   6252 C  CE  . LYS B  1 392 ? 71.512  28.492  37.084 1.00 28.44 ? 582 LYS B CE  1 
ATOM   6253 N  NZ  . LYS B  1 392 ? 72.399  27.739  38.012 1.00 25.33 ? 582 LYS B NZ  1 
ATOM   6254 N  N   . GLY B  1 393 ? 67.178  30.850  34.556 1.00 23.15 ? 583 GLY B N   1 
ATOM   6255 C  CA  . GLY B  1 393 ? 66.267  29.971  33.840 1.00 20.17 ? 583 GLY B CA  1 
ATOM   6256 C  C   . GLY B  1 393 ? 65.342  30.768  32.937 1.00 19.92 ? 583 GLY B C   1 
ATOM   6257 O  O   . GLY B  1 393 ? 64.678  30.217  32.055 1.00 15.51 ? 583 GLY B O   1 
ATOM   6258 N  N   . MET B  1 394 ? 65.296  32.075  33.173 1.00 18.28 ? 584 MET B N   1 
ATOM   6259 C  CA  . MET B  1 394 ? 64.474  32.983  32.383 1.00 17.97 ? 584 MET B CA  1 
ATOM   6260 C  C   . MET B  1 394 ? 65.232  33.347  31.112 1.00 19.82 ? 584 MET B C   1 
ATOM   6261 O  O   . MET B  1 394 ? 66.444  33.557  31.148 1.00 21.05 ? 584 MET B O   1 
ATOM   6262 C  CB  . MET B  1 394 ? 64.180  34.264  33.172 1.00 16.01 ? 584 MET B CB  1 
ATOM   6263 C  CG  . MET B  1 394 ? 63.267  34.084  34.374 1.00 15.40 ? 584 MET B CG  1 
ATOM   6264 S  SD  . MET B  1 394 ? 61.639  33.462  33.913 1.00 24.93 ? 584 MET B SD  1 
ATOM   6265 C  CE  . MET B  1 394 ? 60.807  34.983  33.429 1.00 12.47 ? 584 MET B CE  1 
ATOM   6266 N  N   . VAL B  1 395 ? 64.520  33.414  29.992 1.00 20.99 ? 585 VAL B N   1 
ATOM   6267 C  CA  . VAL B  1 395 ? 65.140  33.769  28.722 1.00 18.78 ? 585 VAL B CA  1 
ATOM   6268 C  C   . VAL B  1 395 ? 65.834  35.119  28.875 1.00 18.68 ? 585 VAL B C   1 
ATOM   6269 O  O   . VAL B  1 395 ? 65.211  36.110  29.265 1.00 20.30 ? 585 VAL B O   1 
ATOM   6270 C  CB  . VAL B  1 395 ? 64.088  33.858  27.595 1.00 17.88 ? 585 VAL B CB  1 
ATOM   6271 C  CG1 . VAL B  1 395 ? 64.729  34.353  26.313 1.00 18.33 ? 585 VAL B CG1 1 
ATOM   6272 C  CG2 . VAL B  1 395 ? 63.472  32.497  27.369 1.00 19.87 ? 585 VAL B CG2 1 
ATOM   6273 N  N   . LEU B  1 396 ? 67.130  35.146  28.581 1.00 18.18 ? 586 LEU B N   1 
ATOM   6274 C  CA  . LEU B  1 396 ? 67.922  36.366  28.691 1.00 18.47 ? 586 LEU B CA  1 
ATOM   6275 C  C   . LEU B  1 396 ? 67.392  37.475  27.796 1.00 18.88 ? 586 LEU B C   1 
ATOM   6276 O  O   . LEU B  1 396 ? 66.855  37.217  26.718 1.00 18.05 ? 586 LEU B O   1 
ATOM   6277 C  CB  . LEU B  1 396 ? 69.381  36.093  28.313 1.00 12.66 ? 586 LEU B CB  1 
ATOM   6278 C  CG  . LEU B  1 396 ? 70.278  35.307  29.270 1.00 13.36 ? 586 LEU B CG  1 
ATOM   6279 C  CD1 . LEU B  1 396 ? 71.581  34.952  28.551 1.00 9.52  ? 586 LEU B CD1 1 
ATOM   6280 C  CD2 . LEU B  1 396 ? 70.559  36.135  30.526 1.00 3.41  ? 586 LEU B CD2 1 
ATOM   6281 N  N   . PRO B  1 397 ? 67.529  38.731  28.240 1.00 16.24 ? 587 PRO B N   1 
ATOM   6282 C  CA  . PRO B  1 397 ? 67.055  39.856  27.433 1.00 17.13 ? 587 PRO B CA  1 
ATOM   6283 C  C   . PRO B  1 397 ? 67.937  39.996  26.189 1.00 18.57 ? 587 PRO B C   1 
ATOM   6284 O  O   . PRO B  1 397 ? 69.146  39.756  26.247 1.00 18.54 ? 587 PRO B O   1 
ATOM   6285 C  CB  . PRO B  1 397 ? 67.186  41.040  28.388 1.00 16.84 ? 587 PRO B CB  1 
ATOM   6286 C  CG  . PRO B  1 397 ? 68.334  40.645  29.264 1.00 12.90 ? 587 PRO B CG  1 
ATOM   6287 C  CD  . PRO B  1 397 ? 68.043  39.193  29.541 1.00 12.71 ? 587 PRO B CD  1 
ATOM   6288 N  N   . GLY B  1 398 ? 67.326  40.368  25.068 1.00 16.45 ? 588 GLY B N   1 
ATOM   6289 C  CA  . GLY B  1 398 ? 68.069  40.515  23.829 1.00 15.21 ? 588 GLY B CA  1 
ATOM   6290 C  C   . GLY B  1 398 ? 68.021  39.239  23.010 1.00 19.74 ? 588 GLY B C   1 
ATOM   6291 O  O   . GLY B  1 398 ? 68.448  39.207  21.856 1.00 23.27 ? 588 GLY B O   1 
ATOM   6292 N  N   . THR B  1 399 ? 67.499  38.177  23.612 1.00 19.07 ? 589 THR B N   1 
ATOM   6293 C  CA  . THR B  1 399 ? 67.392  36.897  22.932 1.00 17.92 ? 589 THR B CA  1 
ATOM   6294 C  C   . THR B  1 399 ? 66.405  36.988  21.770 1.00 19.27 ? 589 THR B C   1 
ATOM   6295 O  O   . THR B  1 399 ? 65.333  37.581  21.892 1.00 17.89 ? 589 THR B O   1 
ATOM   6296 C  CB  . THR B  1 399 ? 66.924  35.794  23.903 1.00 18.37 ? 589 THR B CB  1 
ATOM   6297 O  OG1 . THR B  1 399 ? 67.882  35.652  24.961 1.00 19.27 ? 589 THR B OG1 1 
ATOM   6298 C  CG2 . THR B  1 399 ? 66.763  34.463  23.171 1.00 2.69  ? 589 THR B CG2 1 
ATOM   6299 N  N   . LYS B  1 400 ? 66.786  36.399  20.644 1.00 20.39 ? 590 LYS B N   1 
ATOM   6300 C  CA  . LYS B  1 400 ? 65.961  36.397  19.445 1.00 20.29 ? 590 LYS B CA  1 
ATOM   6301 C  C   . LYS B  1 400 ? 64.756  35.487  19.642 1.00 21.26 ? 590 LYS B C   1 
ATOM   6302 O  O   . LYS B  1 400 ? 64.856  34.271  19.496 1.00 25.70 ? 590 LYS B O   1 
ATOM   6303 C  CB  . LYS B  1 400 ? 66.791  35.917  18.247 1.00 16.71 ? 590 LYS B CB  1 
ATOM   6304 C  CG  . LYS B  1 400 ? 66.020  35.871  16.949 1.00 16.91 ? 590 LYS B CG  1 
ATOM   6305 C  CD  . LYS B  1 400 ? 66.903  35.458  15.799 1.00 14.31 ? 590 LYS B CD  1 
ATOM   6306 C  CE  . LYS B  1 400 ? 66.138  35.500  14.486 1.00 15.98 ? 590 LYS B CE  1 
ATOM   6307 N  NZ  . LYS B  1 400 ? 67.054  35.371  13.319 1.00 14.05 ? 590 LYS B NZ  1 
ATOM   6308 N  N   . CYS B  1 401 ? 63.616  36.082  19.971 1.00 24.65 ? 591 CYS B N   1 
ATOM   6309 C  CA  . CYS B  1 401 ? 62.390  35.322  20.204 1.00 24.20 ? 591 CYS B CA  1 
ATOM   6310 C  C   . CYS B  1 401 ? 61.654  34.992  18.912 1.00 20.77 ? 591 CYS B C   1 
ATOM   6311 O  O   . CYS B  1 401 ? 60.681  34.243  18.923 1.00 21.49 ? 591 CYS B O   1 
ATOM   6312 C  CB  . CYS B  1 401 ? 61.467  36.106  21.135 1.00 25.02 ? 591 CYS B CB  1 
ATOM   6313 S  SG  . CYS B  1 401 ? 61.191  37.807  20.565 1.00 29.99 ? 591 CYS B SG  1 
ATOM   6314 N  N   . ALA B  1 402 ? 62.123  35.552  17.802 1.00 19.15 ? 592 ALA B N   1 
ATOM   6315 C  CA  . ALA B  1 402 ? 61.506  35.318  16.499 1.00 18.06 ? 592 ALA B CA  1 
ATOM   6316 C  C   . ALA B  1 402 ? 62.254  36.076  15.414 1.00 19.83 ? 592 ALA B C   1 
ATOM   6317 O  O   . ALA B  1 402 ? 63.112  36.909  15.704 1.00 23.31 ? 592 ALA B O   1 
ATOM   6318 C  CB  . ALA B  1 402 ? 60.048  35.760  16.515 1.00 10.32 ? 592 ALA B CB  1 
ATOM   6319 N  N   . ASP B  1 403 ? 61.918  35.786  14.163 1.00 20.87 ? 593 ASP B N   1 
ATOM   6320 C  CA  . ASP B  1 403 ? 62.549  36.447  13.029 1.00 24.42 ? 593 ASP B CA  1 
ATOM   6321 C  C   . ASP B  1 403 ? 62.321  37.958  13.094 1.00 21.28 ? 593 ASP B C   1 
ATOM   6322 O  O   . ASP B  1 403 ? 61.192  38.435  12.980 1.00 17.33 ? 593 ASP B O   1 
ATOM   6323 C  CB  . ASP B  1 403 ? 61.985  35.890  11.718 1.00 28.43 ? 593 ASP B CB  1 
ATOM   6324 C  CG  . ASP B  1 403 ? 62.563  36.575  10.492 1.00 37.24 ? 593 ASP B CG  1 
ATOM   6325 O  OD1 . ASP B  1 403 ? 62.118  36.248  9.371  1.00 44.06 ? 593 ASP B OD1 1 
ATOM   6326 O  OD2 . ASP B  1 403 ? 63.460  37.436  10.643 1.00 38.15 ? 593 ASP B OD2 1 
ATOM   6327 N  N   . GLY B  1 404 ? 63.406  38.701  13.286 1.00 18.06 ? 594 GLY B N   1 
ATOM   6328 C  CA  . GLY B  1 404 ? 63.315  40.144  13.362 1.00 13.79 ? 594 GLY B CA  1 
ATOM   6329 C  C   . GLY B  1 404 ? 62.789  40.637  14.692 1.00 18.35 ? 594 GLY B C   1 
ATOM   6330 O  O   . GLY B  1 404 ? 62.410  41.804  14.815 1.00 18.96 ? 594 GLY B O   1 
ATOM   6331 N  N   . LYS B  1 405 ? 62.769  39.765  15.698 1.00 18.63 ? 595 LYS B N   1 
ATOM   6332 C  CA  . LYS B  1 405 ? 62.268  40.158  17.011 1.00 19.36 ? 595 LYS B CA  1 
ATOM   6333 C  C   . LYS B  1 405 ? 63.143  39.695  18.172 1.00 17.57 ? 595 LYS B C   1 
ATOM   6334 O  O   . LYS B  1 405 ? 63.737  38.620  18.122 1.00 24.12 ? 595 LYS B O   1 
ATOM   6335 C  CB  . LYS B  1 405 ? 60.840  39.637  17.189 1.00 17.96 ? 595 LYS B CB  1 
ATOM   6336 C  CG  . LYS B  1 405 ? 59.929  39.980  16.016 1.00 7.62  ? 595 LYS B CG  1 
ATOM   6337 C  CD  . LYS B  1 405 ? 58.474  39.664  16.299 1.00 2.21  ? 595 LYS B CD  1 
ATOM   6338 C  CE  . LYS B  1 405 ? 57.874  40.664  17.269 1.00 12.69 ? 595 LYS B CE  1 
ATOM   6339 N  NZ  . LYS B  1 405 ? 56.384  40.619  17.261 1.00 14.61 ? 595 LYS B NZ  1 
ATOM   6340 N  N   . VAL B  1 406 ? 63.224  40.521  19.213 1.00 16.19 ? 596 VAL B N   1 
ATOM   6341 C  CA  . VAL B  1 406 ? 64.016  40.202  20.401 1.00 16.97 ? 596 VAL B CA  1 
ATOM   6342 C  C   . VAL B  1 406 ? 63.226  40.464  21.686 1.00 19.27 ? 596 VAL B C   1 
ATOM   6343 O  O   . VAL B  1 406 ? 62.233  41.197  21.681 1.00 14.57 ? 596 VAL B O   1 
ATOM   6344 C  CB  . VAL B  1 406 ? 65.330  41.025  20.454 1.00 12.02 ? 596 VAL B CB  1 
ATOM   6345 C  CG1 . VAL B  1 406 ? 66.217  40.654  19.291 1.00 12.43 ? 596 VAL B CG1 1 
ATOM   6346 C  CG2 . VAL B  1 406 ? 65.024  42.508  20.424 1.00 7.60  ? 596 VAL B CG2 1 
ATOM   6347 N  N   . CYS B  1 407 ? 63.676  39.862  22.784 1.00 20.71 ? 597 CYS B N   1 
ATOM   6348 C  CA  . CYS B  1 407 ? 63.012  40.019  24.076 1.00 19.60 ? 597 CYS B CA  1 
ATOM   6349 C  C   . CYS B  1 407 ? 63.428  41.287  24.787 1.00 15.90 ? 597 CYS B C   1 
ATOM   6350 O  O   . CYS B  1 407 ? 64.599  41.479  25.096 1.00 16.58 ? 597 CYS B O   1 
ATOM   6351 C  CB  . CYS B  1 407 ? 63.311  38.829  24.989 1.00 21.47 ? 597 CYS B CB  1 
ATOM   6352 S  SG  . CYS B  1 407 ? 62.600  37.254  24.421 1.00 29.64 ? 597 CYS B SG  1 
ATOM   6353 N  N   . SER B  1 408 ? 62.456  42.153  25.047 1.00 18.66 ? 598 SER B N   1 
ATOM   6354 C  CA  . SER B  1 408 ? 62.719  43.402  25.739 1.00 16.48 ? 598 SER B CA  1 
ATOM   6355 C  C   . SER B  1 408 ? 61.717  43.528  26.871 1.00 18.28 ? 598 SER B C   1 
ATOM   6356 O  O   . SER B  1 408 ? 60.579  43.952  26.671 1.00 26.80 ? 598 SER B O   1 
ATOM   6357 C  CB  . SER B  1 408 ? 62.586  44.583  24.781 1.00 11.11 ? 598 SER B CB  1 
ATOM   6358 O  OG  . SER B  1 408 ? 63.069  45.769  25.385 1.00 6.99  ? 598 SER B OG  1 
ATOM   6359 N  N   . ASN B  1 409 ? 62.153  43.137  28.061 1.00 20.93 ? 599 ASN B N   1 
ATOM   6360 C  CA  . ASN B  1 409 ? 61.325  43.176  29.256 1.00 21.32 ? 599 ASN B CA  1 
ATOM   6361 C  C   . ASN B  1 409 ? 60.140  42.219  29.138 1.00 20.87 ? 599 ASN B C   1 
ATOM   6362 O  O   . ASN B  1 409 ? 58.982  42.625  29.230 1.00 23.15 ? 599 ASN B O   1 
ATOM   6363 C  CB  . ASN B  1 409 ? 60.826  44.599  29.518 1.00 19.17 ? 599 ASN B CB  1 
ATOM   6364 C  CG  . ASN B  1 409 ? 60.217  44.751  30.900 1.00 31.97 ? 599 ASN B CG  1 
ATOM   6365 O  OD1 . ASN B  1 409 ? 59.612  45.775  31.216 1.00 38.51 ? 599 ASN B OD1 1 
ATOM   6366 N  ND2 . ASN B  1 409 ? 60.382  43.730  31.736 1.00 35.25 ? 599 ASN B ND2 1 
ATOM   6367 N  N   . GLY B  1 410 ? 60.443  40.944  28.928 1.00 19.20 ? 600 GLY B N   1 
ATOM   6368 C  CA  . GLY B  1 410 ? 59.396  39.945  28.812 1.00 22.49 ? 600 GLY B CA  1 
ATOM   6369 C  C   . GLY B  1 410 ? 58.525  40.089  27.579 1.00 20.84 ? 600 GLY B C   1 
ATOM   6370 O  O   . GLY B  1 410 ? 57.519  39.401  27.447 1.00 22.22 ? 600 GLY B O   1 
ATOM   6371 N  N   . HIS B  1 411 ? 58.904  40.980  26.671 1.00 18.61 ? 601 HIS B N   1 
ATOM   6372 C  CA  . HIS B  1 411 ? 58.131  41.187  25.454 1.00 16.86 ? 601 HIS B CA  1 
ATOM   6373 C  C   . HIS B  1 411 ? 58.928  40.825  24.207 1.00 16.83 ? 601 HIS B C   1 
ATOM   6374 O  O   . HIS B  1 411 ? 60.114  41.147  24.105 1.00 16.79 ? 601 HIS B O   1 
ATOM   6375 C  CB  . HIS B  1 411 ? 57.693  42.648  25.356 1.00 17.87 ? 601 HIS B CB  1 
ATOM   6376 C  CG  . HIS B  1 411 ? 56.667  43.046  26.369 1.00 18.63 ? 601 HIS B CG  1 
ATOM   6377 N  ND1 . HIS B  1 411 ? 55.367  42.591  26.329 1.00 18.42 ? 601 HIS B ND1 1 
ATOM   6378 C  CD2 . HIS B  1 411 ? 56.744  43.875  27.437 1.00 18.00 ? 601 HIS B CD2 1 
ATOM   6379 C  CE1 . HIS B  1 411 ? 54.685  43.127  27.326 1.00 17.63 ? 601 HIS B CE1 1 
ATOM   6380 N  NE2 . HIS B  1 411 ? 55.497  43.910  28.013 1.00 17.87 ? 601 HIS B NE2 1 
ATOM   6381 N  N   . CYS B  1 412 ? 58.276  40.149  23.264 1.00 13.88 ? 602 CYS B N   1 
ATOM   6382 C  CA  . CYS B  1 412 ? 58.922  39.778  22.010 1.00 14.17 ? 602 CYS B CA  1 
ATOM   6383 C  C   . CYS B  1 412 ? 58.608  40.884  21.002 1.00 18.17 ? 602 CYS B C   1 
ATOM   6384 O  O   . CYS B  1 412 ? 57.582  40.854  20.324 1.00 22.46 ? 602 CYS B O   1 
ATOM   6385 C  CB  . CYS B  1 412 ? 58.391  38.435  21.510 1.00 13.69 ? 602 CYS B CB  1 
ATOM   6386 S  SG  . CYS B  1 412 ? 59.236  37.854  20.006 1.00 28.56 ? 602 CYS B SG  1 
ATOM   6387 N  N   . VAL B  1 413 ? 59.502  41.861  20.911 1.00 20.58 ? 603 VAL B N   1 
ATOM   6388 C  CA  . VAL B  1 413 ? 59.309  43.002  20.024 1.00 19.65 ? 603 VAL B CA  1 
ATOM   6389 C  C   . VAL B  1 413 ? 60.254  43.034  18.817 1.00 27.14 ? 603 VAL B C   1 
ATOM   6390 O  O   . VAL B  1 413 ? 61.281  42.355  18.796 1.00 30.42 ? 603 VAL B O   1 
ATOM   6391 C  CB  . VAL B  1 413 ? 59.469  44.316  20.820 1.00 10.85 ? 603 VAL B CB  1 
ATOM   6392 C  CG1 . VAL B  1 413 ? 58.592  44.272  22.050 1.00 1.00  ? 603 VAL B CG1 1 
ATOM   6393 C  CG2 . VAL B  1 413 ? 60.924  44.516  21.225 1.00 3.72  ? 603 VAL B CG2 1 
ATOM   6394 N  N   . ASP B  1 414 ? 59.893  43.831  17.814 1.00 29.51 ? 604 ASP B N   1 
ATOM   6395 C  CA  . ASP B  1 414 ? 60.703  43.972  16.608 1.00 34.07 ? 604 ASP B CA  1 
ATOM   6396 C  C   . ASP B  1 414 ? 62.079  44.534  16.949 1.00 30.64 ? 604 ASP B C   1 
ATOM   6397 O  O   . ASP B  1 414 ? 62.195  45.486  17.722 1.00 25.15 ? 604 ASP B O   1 
ATOM   6398 C  CB  . ASP B  1 414 ? 60.002  44.895  15.604 1.00 39.91 ? 604 ASP B CB  1 
ATOM   6399 C  CG  . ASP B  1 414 ? 60.899  45.286  14.437 1.00 47.46 ? 604 ASP B CG  1 
ATOM   6400 O  OD1 . ASP B  1 414 ? 61.450  44.385  13.769 1.00 50.73 ? 604 ASP B OD1 1 
ATOM   6401 O  OD2 . ASP B  1 414 ? 61.051  46.501  14.184 1.00 51.72 ? 604 ASP B OD2 1 
ATOM   6402 N  N   . VAL B  1 415 ? 63.115  43.939  16.363 1.00 27.31 ? 605 VAL B N   1 
ATOM   6403 C  CA  . VAL B  1 415 ? 64.489  44.364  16.600 1.00 26.64 ? 605 VAL B CA  1 
ATOM   6404 C  C   . VAL B  1 415 ? 64.693  45.835  16.253 1.00 30.05 ? 605 VAL B C   1 
ATOM   6405 O  O   . VAL B  1 415 ? 65.254  46.593  17.045 1.00 35.87 ? 605 VAL B O   1 
ATOM   6406 C  CB  . VAL B  1 415 ? 65.484  43.525  15.769 1.00 28.62 ? 605 VAL B CB  1 
ATOM   6407 C  CG1 . VAL B  1 415 ? 66.912  43.883  16.149 1.00 30.73 ? 605 VAL B CG1 1 
ATOM   6408 C  CG2 . VAL B  1 415 ? 65.243  42.049  16.004 1.00 36.94 ? 605 VAL B CG2 1 
ATOM   6409 N  N   . ALA B  1 416 ? 64.237  46.234  15.069 1.00 30.04 ? 606 ALA B N   1 
ATOM   6410 C  CA  . ALA B  1 416 ? 64.374  47.613  14.610 1.00 29.80 ? 606 ALA B CA  1 
ATOM   6411 C  C   . ALA B  1 416 ? 63.840  48.639  15.609 1.00 33.47 ? 606 ALA B C   1 
ATOM   6412 O  O   . ALA B  1 416 ? 64.359  49.751  15.705 1.00 38.08 ? 606 ALA B O   1 
ATOM   6413 C  CB  . ALA B  1 416 ? 63.670  47.783  13.275 1.00 25.59 ? 606 ALA B CB  1 
ATOM   6414 N  N   . THR B  1 417 ? 62.805  48.265  16.352 1.00 33.53 ? 607 THR B N   1 
ATOM   6415 C  CA  . THR B  1 417 ? 62.208  49.166  17.329 1.00 33.83 ? 607 THR B CA  1 
ATOM   6416 C  C   . THR B  1 417 ? 62.550  48.744  18.752 1.00 35.31 ? 607 THR B C   1 
ATOM   6417 O  O   . THR B  1 417 ? 61.943  49.223  19.709 1.00 39.69 ? 607 THR B O   1 
ATOM   6418 C  CB  . THR B  1 417 ? 60.673  49.192  17.195 1.00 35.27 ? 607 THR B CB  1 
ATOM   6419 O  OG1 . THR B  1 417 ? 60.119  48.007  17.782 1.00 33.71 ? 607 THR B OG1 1 
ATOM   6420 C  CG2 . THR B  1 417 ? 60.273  49.244  15.726 1.00 36.77 ? 607 THR B CG2 1 
ATOM   6421 N  N   . ALA B  1 418 ? 63.517  47.843  18.892 1.00 35.32 ? 608 ALA B N   1 
ATOM   6422 C  CA  . ALA B  1 418 ? 63.918  47.364  20.211 1.00 32.87 ? 608 ALA B CA  1 
ATOM   6423 C  C   . ALA B  1 418 ? 64.921  48.304  20.856 1.00 31.42 ? 608 ALA B C   1 
ATOM   6424 O  O   . ALA B  1 418 ? 64.971  48.424  22.081 1.00 25.62 ? 608 ALA B O   1 
ATOM   6425 C  CB  . ALA B  1 418 ? 64.513  45.968  20.105 1.00 33.08 ? 608 ALA B CB  1 
ATOM   6426 N  N   . TYR B  1 419 ? 65.718  48.967  20.023 1.00 33.28 ? 609 TYR B N   1 
ATOM   6427 C  CA  . TYR B  1 419 ? 66.728  49.895  20.515 1.00 35.84 ? 609 TYR B CA  1 
ATOM   6428 C  C   . TYR B  1 419 ? 66.710  51.200  19.723 1.00 41.70 ? 609 TYR B C   1 
ATOM   6429 O  O   . TYR B  1 419 ? 65.861  51.320  18.811 1.00 44.92 ? 609 TYR B O   1 
ATOM   6430 C  CB  . TYR B  1 419 ? 68.115  49.259  20.419 1.00 29.43 ? 609 TYR B CB  1 
ATOM   6431 C  CG  . TYR B  1 419 ? 68.136  47.784  20.744 1.00 23.89 ? 609 TYR B CG  1 
ATOM   6432 C  CD1 . TYR B  1 419 ? 68.009  46.826  19.734 1.00 14.86 ? 609 TYR B CD1 1 
ATOM   6433 C  CD2 . TYR B  1 419 ? 68.268  47.343  22.061 1.00 19.21 ? 609 TYR B CD2 1 
ATOM   6434 C  CE1 . TYR B  1 419 ? 68.017  45.466  20.029 1.00 13.54 ? 609 TYR B CE1 1 
ATOM   6435 C  CE2 . TYR B  1 419 ? 68.276  45.984  22.366 1.00 15.79 ? 609 TYR B CE2 1 
ATOM   6436 C  CZ  . TYR B  1 419 ? 68.152  45.054  21.348 1.00 16.55 ? 609 TYR B CZ  1 
ATOM   6437 O  OH  . TYR B  1 419 ? 68.169  43.715  21.653 1.00 25.66 ? 609 TYR B OH  1 
ATOM   6438 O  OXT . TYR B  1 419 ? 67.546  52.083  20.024 1.00 42.40 ? 609 TYR B OXT 1 
HETATM 6439 C  C1  . NAG C  2 .   ? 90.137  22.187  25.404 1.00 31.13 ? 801 NAG A C1  1 
HETATM 6440 C  C2  . NAG C  2 .   ? 89.375  23.480  25.625 1.00 26.35 ? 801 NAG A C2  1 
HETATM 6441 C  C3  . NAG C  2 .   ? 89.364  24.248  24.307 1.00 31.57 ? 801 NAG A C3  1 
HETATM 6442 C  C4  . NAG C  2 .   ? 90.803  24.463  23.794 1.00 31.75 ? 801 NAG A C4  1 
HETATM 6443 C  C5  . NAG C  2 .   ? 91.631  23.158  23.823 1.00 30.41 ? 801 NAG A C5  1 
HETATM 6444 C  C6  . NAG C  2 .   ? 93.112  23.424  23.638 1.00 32.38 ? 801 NAG A C6  1 
HETATM 6445 C  C7  . NAG C  2 .   ? 87.693  23.309  27.331 1.00 27.90 ? 801 NAG A C7  1 
HETATM 6446 C  C8  . NAG C  2 .   ? 86.539  24.241  27.655 1.00 29.45 ? 801 NAG A C8  1 
HETATM 6447 N  N2  . NAG C  2 .   ? 88.024  23.181  26.052 1.00 29.59 ? 801 NAG A N2  1 
HETATM 6448 O  O3  . NAG C  2 .   ? 88.727  25.504  24.501 1.00 26.56 ? 801 NAG A O3  1 
HETATM 6449 O  O4  . NAG C  2 .   ? 90.770  24.958  22.439 1.00 35.36 ? 801 NAG A O4  1 
HETATM 6450 O  O5  . NAG C  2 .   ? 91.496  22.483  25.090 1.00 32.80 ? 801 NAG A O5  1 
HETATM 6451 O  O6  . NAG C  2 .   ? 93.671  22.433  22.760 1.00 37.54 ? 801 NAG A O6  1 
HETATM 6452 O  O7  . NAG C  2 .   ? 88.280  22.718  28.237 1.00 32.59 ? 801 NAG A O7  1 
HETATM 6453 C  C1  . NAG D  2 .   ? 90.582  26.317  22.245 1.00 34.85 ? 802 NAG A C1  1 
HETATM 6454 C  C2  . NAG D  2 .   ? 91.260  26.713  20.925 1.00 31.66 ? 802 NAG A C2  1 
HETATM 6455 C  C3  . NAG D  2 .   ? 90.948  28.163  20.570 1.00 32.32 ? 802 NAG A C3  1 
HETATM 6456 C  C4  . NAG D  2 .   ? 89.435  28.328  20.529 1.00 34.96 ? 802 NAG A C4  1 
HETATM 6457 C  C5  . NAG D  2 .   ? 88.828  27.929  21.880 1.00 32.45 ? 802 NAG A C5  1 
HETATM 6458 C  C6  . NAG D  2 .   ? 87.311  28.015  21.873 1.00 28.60 ? 802 NAG A C6  1 
HETATM 6459 C  C7  . NAG D  2 .   ? 93.346  25.738  20.214 1.00 34.35 ? 802 NAG A C7  1 
HETATM 6460 C  C8  . NAG D  2 .   ? 94.848  25.641  20.411 1.00 29.34 ? 802 NAG A C8  1 
HETATM 6461 N  N2  . NAG D  2 .   ? 92.692  26.541  21.047 1.00 34.67 ? 802 NAG A N2  1 
HETATM 6462 O  O3  . NAG D  2 .   ? 91.503  28.478  19.300 1.00 24.26 ? 802 NAG A O3  1 
HETATM 6463 O  O4  . NAG D  2 .   ? 89.094  29.686  20.212 1.00 37.93 ? 802 NAG A O4  1 
HETATM 6464 O  O5  . NAG D  2 .   ? 89.164  26.557  22.185 1.00 34.92 ? 802 NAG A O5  1 
HETATM 6465 O  O6  . NAG D  2 .   ? 86.751  27.392  23.022 1.00 35.45 ? 802 NAG A O6  1 
HETATM 6466 O  O7  . NAG D  2 .   ? 92.796  25.092  19.318 1.00 30.61 ? 802 NAG A O7  1 
HETATM 6467 C  C1  . BMA E  3 .   ? 88.299  29.864  19.103 1.00 33.11 ? 803 BMA A C1  1 
HETATM 6468 C  C2  . BMA E  3 .   ? 87.741  31.277  19.128 1.00 35.97 ? 803 BMA A C2  1 
HETATM 6469 C  C3  . BMA E  3 .   ? 86.873  31.479  17.887 1.00 37.20 ? 803 BMA A C3  1 
HETATM 6470 C  C4  . BMA E  3 .   ? 87.693  31.206  16.625 1.00 37.45 ? 803 BMA A C4  1 
HETATM 6471 C  C5  . BMA E  3 .   ? 88.339  29.818  16.705 1.00 38.06 ? 803 BMA A C5  1 
HETATM 6472 C  C6  . BMA E  3 .   ? 89.301  29.650  15.556 1.00 31.46 ? 803 BMA A C6  1 
HETATM 6473 O  O2  . BMA E  3 .   ? 88.820  32.204  19.115 1.00 35.32 ? 803 BMA A O2  1 
HETATM 6474 O  O3  . BMA E  3 .   ? 86.376  32.832  17.853 1.00 37.23 ? 803 BMA A O3  1 
HETATM 6475 O  O4  . BMA E  3 .   ? 86.830  31.268  15.473 1.00 39.38 ? 803 BMA A O4  1 
HETATM 6476 O  O5  . BMA E  3 .   ? 89.108  29.684  17.931 1.00 38.19 ? 803 BMA A O5  1 
HETATM 6477 O  O6  . BMA E  3 .   ? 90.190  30.783  15.512 1.00 29.97 ? 803 BMA A O6  1 
HETATM 6478 C  C1  . NAG F  2 .   ? 87.230  32.101  14.442 1.00 37.75 ? 804 NAG A C1  1 
HETATM 6479 C  C2  . NAG F  2 .   ? 86.555  31.634  13.148 1.00 35.50 ? 804 NAG A C2  1 
HETATM 6480 C  C3  . NAG F  2 .   ? 86.764  32.634  12.009 1.00 33.96 ? 804 NAG A C3  1 
HETATM 6481 C  C4  . NAG F  2 .   ? 86.393  34.038  12.473 1.00 33.69 ? 804 NAG A C4  1 
HETATM 6482 C  C5  . NAG F  2 .   ? 87.189  34.379  13.725 1.00 32.93 ? 804 NAG A C5  1 
HETATM 6483 C  C6  . NAG F  2 .   ? 86.873  35.776  14.231 1.00 31.72 ? 804 NAG A C6  1 
HETATM 6484 C  C7  . NAG F  2 .   ? 86.324  29.274  12.763 1.00 40.66 ? 804 NAG A C7  1 
HETATM 6485 C  C8  . NAG F  2 .   ? 86.776  28.104  11.906 1.00 40.21 ? 804 NAG A C8  1 
HETATM 6486 N  N2  . NAG F  2 .   ? 87.104  30.347  12.775 1.00 38.04 ? 804 NAG A N2  1 
HETATM 6487 O  O3  . NAG F  2 .   ? 85.955  32.267  10.903 1.00 30.50 ? 804 NAG A O3  1 
HETATM 6488 O  O4  . NAG F  2 .   ? 86.668  34.984  11.454 1.00 35.03 ? 804 NAG A O4  1 
HETATM 6489 O  O5  . NAG F  2 .   ? 86.846  33.445  14.771 1.00 38.59 ? 804 NAG A O5  1 
HETATM 6490 O  O6  . NAG F  2 .   ? 87.404  35.989  15.529 1.00 31.39 ? 804 NAG A O6  1 
HETATM 6491 O  O7  . NAG F  2 .   ? 85.276  29.205  13.403 1.00 40.71 ? 804 NAG A O7  1 
HETATM 6492 C  C1  . MAN G  4 .   ? 85.052  32.971  17.423 1.00 34.33 ? 805 MAN A C1  1 
HETATM 6493 C  C2  . MAN G  4 .   ? 84.728  34.466  17.242 1.00 37.41 ? 805 MAN A C2  1 
HETATM 6494 C  C3  . MAN G  4 .   ? 84.214  35.212  18.506 1.00 39.74 ? 805 MAN A C3  1 
HETATM 6495 C  C4  . MAN G  4 .   ? 83.459  34.327  19.511 1.00 39.79 ? 805 MAN A C4  1 
HETATM 6496 C  C5  . MAN G  4 .   ? 84.103  32.949  19.614 1.00 38.94 ? 805 MAN A C5  1 
HETATM 6497 C  C6  . MAN G  4 .   ? 83.365  32.002  20.540 1.00 35.36 ? 805 MAN A C6  1 
HETATM 6498 O  O2  . MAN G  4 .   ? 83.893  34.710  16.081 1.00 37.48 ? 805 MAN A O2  1 
HETATM 6499 O  O3  . MAN G  4 .   ? 83.375  36.293  18.124 1.00 48.86 ? 805 MAN A O3  1 
HETATM 6500 O  O4  . MAN G  4 .   ? 83.491  34.946  20.788 1.00 35.68 ? 805 MAN A O4  1 
HETATM 6501 O  O5  . MAN G  4 .   ? 84.138  32.346  18.312 1.00 37.73 ? 805 MAN A O5  1 
HETATM 6502 O  O6  . MAN G  4 .   ? 84.267  31.335  21.412 1.00 36.82 ? 805 MAN A O6  1 
HETATM 6503 C  C1  . NAG H  2 .   ? 82.540  34.390  16.024 1.00 30.02 ? 806 NAG A C1  1 
HETATM 6504 C  C2  . NAG H  2 .   ? 82.054  34.653  14.583 1.00 30.90 ? 806 NAG A C2  1 
HETATM 6505 C  C3  . NAG H  2 .   ? 80.639  34.135  14.366 1.00 33.43 ? 806 NAG A C3  1 
HETATM 6506 C  C4  . NAG H  2 .   ? 80.543  32.675  14.793 1.00 32.59 ? 806 NAG A C4  1 
HETATM 6507 C  C5  . NAG H  2 .   ? 81.031  32.536  16.237 1.00 32.74 ? 806 NAG A C5  1 
HETATM 6508 C  C6  . NAG H  2 .   ? 80.998  31.099  16.727 1.00 25.11 ? 806 NAG A C6  1 
HETATM 6509 C  C7  . NAG H  2 .   ? 83.193  36.626  13.796 1.00 32.03 ? 806 NAG A C7  1 
HETATM 6510 C  C8  . NAG H  2 .   ? 84.110  37.351  14.780 1.00 17.04 ? 806 NAG A C8  1 
HETATM 6511 N  N2  . NAG H  2 .   ? 82.089  36.072  14.288 1.00 31.69 ? 806 NAG A N2  1 
HETATM 6512 O  O3  . NAG H  2 .   ? 80.297  34.262  12.993 1.00 33.13 ? 806 NAG A O3  1 
HETATM 6513 O  O4  . NAG H  2 .   ? 79.195  32.242  14.691 1.00 34.49 ? 806 NAG A O4  1 
HETATM 6514 O  O5  . NAG H  2 .   ? 82.397  32.999  16.339 1.00 32.96 ? 806 NAG A O5  1 
HETATM 6515 O  O6  . NAG H  2 .   ? 81.090  31.038  18.142 1.00 14.32 ? 806 NAG A O6  1 
HETATM 6516 O  O7  . NAG H  2 .   ? 83.487  36.578  12.600 1.00 30.82 ? 806 NAG A O7  1 
HETATM 6517 C  C1  . MAN I  4 .   ? 91.530  30.393  15.474 1.00 36.62 ? 807 MAN A C1  1 
HETATM 6518 C  C2  . MAN I  4 .   ? 92.417  31.626  15.733 1.00 37.35 ? 807 MAN A C2  1 
HETATM 6519 C  C3  . MAN I  4 .   ? 92.401  32.573  14.525 1.00 39.12 ? 807 MAN A C3  1 
HETATM 6520 C  C4  . MAN I  4 .   ? 92.680  31.828  13.205 1.00 42.78 ? 807 MAN A C4  1 
HETATM 6521 C  C5  . MAN I  4 .   ? 91.705  30.644  13.082 1.00 45.39 ? 807 MAN A C5  1 
HETATM 6522 C  C6  . MAN I  4 .   ? 91.854  29.799  11.811 1.00 42.17 ? 807 MAN A C6  1 
HETATM 6523 O  O2  . MAN I  4 .   ? 93.768  31.219  16.025 1.00 38.77 ? 807 MAN A O2  1 
HETATM 6524 O  O3  . MAN I  4 .   ? 93.380  33.579  14.705 1.00 32.83 ? 807 MAN A O3  1 
HETATM 6525 O  O4  . MAN I  4 .   ? 92.489  32.726  12.115 1.00 46.28 ? 807 MAN A O4  1 
HETATM 6526 O  O5  . MAN I  4 .   ? 91.867  29.774  14.227 1.00 42.72 ? 807 MAN A O5  1 
HETATM 6527 O  O6  . MAN I  4 .   ? 92.788  28.737  11.985 1.00 38.69 ? 807 MAN A O6  1 
HETATM 6528 C  C1  . NAG J  2 .   ? 94.025  30.873  17.346 1.00 42.71 ? 808 NAG A C1  1 
HETATM 6529 C  C2  . NAG J  2 .   ? 95.221  29.908  17.410 1.00 46.21 ? 808 NAG A C2  1 
HETATM 6530 C  C3  . NAG J  2 .   ? 95.634  29.639  18.861 1.00 47.57 ? 808 NAG A C3  1 
HETATM 6531 C  C4  . NAG J  2 .   ? 95.814  30.950  19.629 1.00 47.13 ? 808 NAG A C4  1 
HETATM 6532 C  C5  . NAG J  2 .   ? 94.560  31.816  19.484 1.00 46.51 ? 808 NAG A C5  1 
HETATM 6533 C  C6  . NAG J  2 .   ? 94.705  33.154  20.180 1.00 44.15 ? 808 NAG A C6  1 
HETATM 6534 C  C7  . NAG J  2 .   ? 95.127  28.462  15.481 1.00 46.07 ? 808 NAG A C7  1 
HETATM 6535 C  C8  . NAG J  2 .   ? 94.062  27.739  14.668 1.00 48.20 ? 808 NAG A C8  1 
HETATM 6536 N  N2  . NAG J  2 .   ? 94.882  28.648  16.774 1.00 44.93 ? 808 NAG A N2  1 
HETATM 6537 O  O3  . NAG J  2 .   ? 96.852  28.907  18.879 1.00 45.65 ? 808 NAG A O3  1 
HETATM 6538 O  O4  . NAG J  2 .   ? 96.045  30.669  21.001 1.00 43.52 ? 808 NAG A O4  1 
HETATM 6539 O  O5  . NAG J  2 .   ? 94.297  32.076  18.086 1.00 44.89 ? 808 NAG A O5  1 
HETATM 6540 O  O6  . NAG J  2 .   ? 94.862  32.978  21.579 1.00 49.04 ? 808 NAG A O6  1 
HETATM 6541 O  O7  . NAG J  2 .   ? 96.160  28.849  14.934 1.00 44.55 ? 808 NAG A O7  1 
HETATM 6542 C  C1  . FUC K  5 .   ? 94.953  22.783  22.316 1.00 31.01 ? 809 FUC A C1  1 
HETATM 6543 C  C2  . FUC K  5 .   ? 95.998  21.953  23.061 1.00 31.60 ? 809 FUC A C2  1 
HETATM 6544 C  C3  . FUC K  5 .   ? 95.837  20.473  22.703 1.00 29.64 ? 809 FUC A C3  1 
HETATM 6545 C  C4  . FUC K  5 .   ? 95.877  20.266  21.188 1.00 29.54 ? 809 FUC A C4  1 
HETATM 6546 C  C5  . FUC K  5 .   ? 94.902  21.222  20.469 1.00 33.16 ? 809 FUC A C5  1 
HETATM 6547 C  C6  . FUC K  5 .   ? 95.084  21.213  18.958 1.00 34.39 ? 809 FUC A C6  1 
HETATM 6548 O  O2  . FUC K  5 .   ? 95.822  22.118  24.462 1.00 39.42 ? 809 FUC A O2  1 
HETATM 6549 O  O3  . FUC K  5 .   ? 96.881  19.727  23.308 1.00 25.51 ? 809 FUC A O3  1 
HETATM 6550 O  O4  . FUC K  5 .   ? 97.197  20.480  20.715 1.00 23.18 ? 809 FUC A O4  1 
HETATM 6551 O  O5  . FUC K  5 .   ? 95.109  22.586  20.911 1.00 30.80 ? 809 FUC A O5  1 
HETATM 6552 ZN ZN  . ZN  L  6 .   ? 77.798  8.644   21.812 1.00 18.89 ? 700 ZN  A ZN  1 
HETATM 6553 CA CA  . CA  M  7 .   ? 81.503  0.403   43.618 1.00 21.01 ? 701 CA  A CA  1 
HETATM 6554 CA CA  . CA  N  7 .   ? 97.088  -5.343  39.059 1.00 20.93 ? 702 CA  A CA  1 
HETATM 6555 CA CA  . CA  O  7 .   ? 83.846  5.791   62.284 1.00 23.21 ? 703 CA  A CA  1 
HETATM 6556 C  C1  . NAG P  2 .   ? 88.910  29.184  60.910 1.00 33.74 ? 801 NAG B C1  1 
HETATM 6557 C  C2  . NAG P  2 .   ? 88.124  27.900  60.682 1.00 32.12 ? 801 NAG B C2  1 
HETATM 6558 C  C3  . NAG P  2 .   ? 88.054  27.157  62.015 1.00 34.72 ? 801 NAG B C3  1 
HETATM 6559 C  C4  . NAG P  2 .   ? 89.481  26.917  62.560 1.00 34.57 ? 801 NAG B C4  1 
HETATM 6560 C  C5  . NAG P  2 .   ? 90.330  28.198  62.561 1.00 32.79 ? 801 NAG B C5  1 
HETATM 6561 C  C6  . NAG P  2 .   ? 91.792  27.851  62.801 1.00 33.97 ? 801 NAG B C6  1 
HETATM 6562 C  C7  . NAG P  2 .   ? 86.330  27.615  59.090 1.00 41.01 ? 801 NAG B C7  1 
HETATM 6563 C  C8  . NAG P  2 .   ? 85.500  26.352  59.266 1.00 46.10 ? 801 NAG B C8  1 
HETATM 6564 N  N2  . NAG P  2 .   ? 86.792  28.203  60.192 1.00 37.97 ? 801 NAG B N2  1 
HETATM 6565 O  O3  . NAG P  2 .   ? 87.383  25.918  61.828 1.00 29.64 ? 801 NAG B O3  1 
HETATM 6566 O  O4  . NAG P  2 .   ? 89.435  26.413  63.909 1.00 38.84 ? 801 NAG B O4  1 
HETATM 6567 O  O5  . NAG P  2 .   ? 90.256  28.868  61.282 1.00 35.17 ? 801 NAG B O5  1 
HETATM 6568 O  O6  . NAG P  2 .   ? 92.492  28.976  63.361 1.00 39.21 ? 801 NAG B O6  1 
HETATM 6569 O  O7  . NAG P  2 .   ? 86.535  28.056  57.958 1.00 39.56 ? 801 NAG B O7  1 
HETATM 6570 C  C1  . NAG Q  2 .   ? 89.290  25.049  64.067 1.00 39.06 ? 802 NAG B C1  1 
HETATM 6571 C  C2  . NAG Q  2 .   ? 89.874  24.643  65.429 1.00 38.13 ? 802 NAG B C2  1 
HETATM 6572 C  C3  . NAG Q  2 .   ? 89.501  23.197  65.782 1.00 40.61 ? 802 NAG B C3  1 
HETATM 6573 C  C4  . NAG Q  2 .   ? 87.988  22.990  65.641 1.00 43.90 ? 802 NAG B C4  1 
HETATM 6574 C  C5  . NAG Q  2 .   ? 87.568  23.388  64.229 1.00 41.10 ? 802 NAG B C5  1 
HETATM 6575 C  C6  . NAG Q  2 .   ? 86.081  23.242  63.988 1.00 41.72 ? 802 NAG B C6  1 
HETATM 6576 C  C7  . NAG Q  2 .   ? 91.933  25.597  66.257 1.00 31.88 ? 802 NAG B C7  1 
HETATM 6577 C  C8  . NAG Q  2 .   ? 93.438  25.738  66.108 1.00 24.76 ? 802 NAG B C8  1 
HETATM 6578 N  N2  . NAG Q  2 .   ? 91.319  24.775  65.410 1.00 34.36 ? 802 NAG B N2  1 
HETATM 6579 O  O3  . NAG Q  2 .   ? 89.894  22.929  67.120 1.00 39.47 ? 802 NAG B O3  1 
HETATM 6580 O  O4  . NAG Q  2 .   ? 87.631  21.615  65.910 1.00 45.83 ? 802 NAG B O4  1 
HETATM 6581 O  O5  . NAG Q  2 .   ? 87.883  24.774  64.016 1.00 40.79 ? 802 NAG B O5  1 
HETATM 6582 O  O6  . NAG Q  2 .   ? 85.344  24.118  64.828 1.00 46.99 ? 802 NAG B O6  1 
HETATM 6583 O  O7  . NAG Q  2 .   ? 91.342  26.230  67.133 1.00 31.50 ? 802 NAG B O7  1 
HETATM 6584 C  C1  . BMA R  3 .   ? 86.774  21.409  66.988 1.00 40.99 ? 803 BMA B C1  1 
HETATM 6585 C  C2  . BMA R  3 .   ? 86.161  20.005  66.925 1.00 40.38 ? 803 BMA B C2  1 
HETATM 6586 C  C3  . BMA R  3 .   ? 85.239  19.807  68.127 1.00 41.86 ? 803 BMA B C3  1 
HETATM 6587 C  C4  . BMA R  3 .   ? 86.012  20.068  69.420 1.00 40.02 ? 803 BMA B C4  1 
HETATM 6588 C  C5  . BMA R  3 .   ? 86.693  21.440  69.385 1.00 39.34 ? 803 BMA B C5  1 
HETATM 6589 C  C6  . BMA R  3 .   ? 87.618  21.578  70.574 1.00 38.21 ? 803 BMA B C6  1 
HETATM 6590 O  O2  . BMA R  3 .   ? 87.188  19.024  66.969 1.00 42.25 ? 803 BMA B O2  1 
HETATM 6591 O  O3  . BMA R  3 .   ? 84.750  18.449  68.150 1.00 45.31 ? 803 BMA B O3  1 
HETATM 6592 O  O4  . BMA R  3 .   ? 85.103  20.015  70.534 1.00 40.74 ? 803 BMA B O4  1 
HETATM 6593 O  O5  . BMA R  3 .   ? 87.523  21.555  68.204 1.00 40.24 ? 803 BMA B O5  1 
HETATM 6594 O  O6  . BMA R  3 .   ? 88.563  20.488  70.556 1.00 34.14 ? 803 BMA B O6  1 
HETATM 6595 C  C1  . NAG S  2 .   ? 85.507  19.312  71.654 1.00 34.61 ? 804 NAG B C1  1 
HETATM 6596 C  C2  . NAG S  2 .   ? 84.688  19.808  72.841 1.00 30.87 ? 804 NAG B C2  1 
HETATM 6597 C  C3  . NAG S  2 .   ? 84.925  18.953  74.082 1.00 31.04 ? 804 NAG B C3  1 
HETATM 6598 C  C4  . NAG S  2 .   ? 84.696  17.482  73.739 1.00 32.41 ? 804 NAG B C4  1 
HETATM 6599 C  C5  . NAG S  2 .   ? 85.584  17.087  72.555 1.00 32.56 ? 804 NAG B C5  1 
HETATM 6600 C  C6  . NAG S  2 .   ? 85.361  15.639  72.140 1.00 31.22 ? 804 NAG B C6  1 
HETATM 6601 C  C7  . NAG S  2 .   ? 84.107  22.109  73.192 1.00 31.75 ? 804 NAG B C7  1 
HETATM 6602 C  C8  . NAG S  2 .   ? 84.404  23.316  74.067 1.00 29.58 ? 804 NAG B C8  1 
HETATM 6603 N  N2  . NAG S  2 .   ? 85.052  21.182  73.111 1.00 31.09 ? 804 NAG B N2  1 
HETATM 6604 O  O3  . NAG S  2 .   ? 84.024  19.353  75.104 1.00 24.40 ? 804 NAG B O3  1 
HETATM 6605 O  O4  . NAG S  2 .   ? 84.994  16.671  74.863 1.00 34.89 ? 804 NAG B O4  1 
HETATM 6606 O  O5  . NAG S  2 .   ? 85.268  17.915  71.413 1.00 36.37 ? 804 NAG B O5  1 
HETATM 6607 O  O6  . NAG S  2 .   ? 85.295  15.504  70.727 1.00 25.52 ? 804 NAG B O6  1 
HETATM 6608 O  O7  . NAG S  2 .   ? 83.031  22.023  72.597 1.00 28.86 ? 804 NAG B O7  1 
HETATM 6609 C  C1  . MAN T  4 .   ? 83.438  18.292  68.614 1.00 40.65 ? 805 MAN B C1  1 
HETATM 6610 C  C2  . MAN T  4 .   ? 83.189  16.795  68.897 1.00 43.34 ? 805 MAN B C2  1 
HETATM 6611 C  C3  . MAN T  4 .   ? 82.786  15.946  67.659 1.00 43.47 ? 805 MAN B C3  1 
HETATM 6612 C  C4  . MAN T  4 .   ? 81.986  16.718  66.591 1.00 42.73 ? 805 MAN B C4  1 
HETATM 6613 C  C5  . MAN T  4 .   ? 82.540  18.128  66.422 1.00 40.77 ? 805 MAN B C5  1 
HETATM 6614 C  C6  . MAN T  4 .   ? 81.806  18.984  65.419 1.00 39.68 ? 805 MAN B C6  1 
HETATM 6615 O  O2  . MAN T  4 .   ? 82.306  16.573  70.031 1.00 42.33 ? 805 MAN B O2  1 
HETATM 6616 O  O3  . MAN T  4 .   ? 82.039  14.810  68.076 1.00 45.50 ? 805 MAN B O3  1 
HETATM 6617 O  O4  . MAN T  4 .   ? 82.083  16.031  65.352 1.00 43.84 ? 805 MAN B O4  1 
HETATM 6618 O  O5  . MAN T  4 .   ? 82.496  18.803  67.685 1.00 38.57 ? 805 MAN B O5  1 
HETATM 6619 O  O6  . MAN T  4 .   ? 82.619  20.064  64.984 1.00 32.79 ? 805 MAN B O6  1 
HETATM 6620 C  C1  . NAG U  2 .   ? 80.931  16.789  69.983 1.00 34.33 ? 806 NAG B C1  1 
HETATM 6621 C  C2  . NAG U  2 .   ? 80.350  16.512  71.389 1.00 35.93 ? 806 NAG B C2  1 
HETATM 6622 C  C3  . NAG U  2 .   ? 78.878  16.905  71.454 1.00 35.58 ? 806 NAG B C3  1 
HETATM 6623 C  C4  . NAG U  2 .   ? 78.713  18.358  71.019 1.00 36.70 ? 806 NAG B C4  1 
HETATM 6624 C  C5  . NAG U  2 .   ? 79.321  18.546  69.619 1.00 38.79 ? 806 NAG B C5  1 
HETATM 6625 C  C6  . NAG U  2 .   ? 79.261  19.993  69.156 1.00 34.34 ? 806 NAG B C6  1 
HETATM 6626 C  C7  . NAG U  2 .   ? 81.567  14.681  72.383 1.00 38.65 ? 806 NAG B C7  1 
HETATM 6627 C  C8  . NAG U  2 .   ? 82.613  13.944  71.557 1.00 38.36 ? 806 NAG B C8  1 
HETATM 6628 N  N2  . NAG U  2 .   ? 80.486  15.110  71.738 1.00 39.49 ? 806 NAG B N2  1 
HETATM 6629 O  O3  . NAG U  2 .   ? 78.397  16.733  72.781 1.00 33.13 ? 806 NAG B O3  1 
HETATM 6630 O  O4  . NAG U  2 .   ? 77.333  18.694  71.005 1.00 28.81 ? 806 NAG B O4  1 
HETATM 6631 O  O5  . NAG U  2 .   ? 80.717  18.162  69.626 1.00 38.01 ? 806 NAG B O5  1 
HETATM 6632 O  O6  . NAG U  2 .   ? 79.334  20.083  67.741 1.00 30.08 ? 806 NAG B O6  1 
HETATM 6633 O  O7  . NAG U  2 .   ? 81.740  14.850  73.593 1.00 33.94 ? 806 NAG B O7  1 
HETATM 6634 C  C1  . MAN V  4 .   ? 89.884  20.929  70.663 1.00 36.50 ? 807 MAN B C1  1 
HETATM 6635 C  C2  . MAN V  4 .   ? 90.817  19.748  70.384 1.00 37.30 ? 807 MAN B C2  1 
HETATM 6636 C  C3  . MAN V  4 .   ? 90.797  18.749  71.541 1.00 35.24 ? 807 MAN B C3  1 
HETATM 6637 C  C4  . MAN V  4 .   ? 91.120  19.465  72.851 1.00 35.96 ? 807 MAN B C4  1 
HETATM 6638 C  C5  . MAN V  4 .   ? 90.102  20.586  73.060 1.00 38.06 ? 807 MAN B C5  1 
HETATM 6639 C  C6  . MAN V  4 .   ? 90.340  21.387  74.324 1.00 38.21 ? 807 MAN B C6  1 
HETATM 6640 O  O2  . MAN V  4 .   ? 92.158  20.218  70.184 1.00 38.65 ? 807 MAN B O2  1 
HETATM 6641 O  O3  . MAN V  4 .   ? 91.761  17.732  71.304 1.00 33.86 ? 807 MAN B O3  1 
HETATM 6642 O  O4  . MAN V  4 .   ? 91.066  18.538  73.926 1.00 36.15 ? 807 MAN B O4  1 
HETATM 6643 O  O5  . MAN V  4 .   ? 90.170  21.509  71.948 1.00 39.36 ? 807 MAN B O5  1 
HETATM 6644 O  O6  . MAN V  4 .   ? 91.527  22.161  74.222 1.00 40.26 ? 807 MAN B O6  1 
HETATM 6645 C  C1  . NAG W  2 .   ? 92.550  20.353  68.869 1.00 42.80 ? 808 NAG B C1  1 
HETATM 6646 C  C2  . NAG W  2 .   ? 93.717  21.336  68.789 1.00 45.44 ? 808 NAG B C2  1 
HETATM 6647 C  C3  . NAG W  2 .   ? 94.229  21.409  67.350 1.00 46.77 ? 808 NAG B C3  1 
HETATM 6648 C  C4  . NAG W  2 .   ? 94.580  20.008  66.840 1.00 46.96 ? 808 NAG B C4  1 
HETATM 6649 C  C5  . NAG W  2 .   ? 93.359  19.098  66.994 1.00 47.51 ? 808 NAG B C5  1 
HETATM 6650 C  C6  . NAG W  2 .   ? 93.613  17.673  66.546 1.00 48.69 ? 808 NAG B C6  1 
HETATM 6651 C  C7  . NAG W  2 .   ? 93.047  22.911  70.495 1.00 47.37 ? 808 NAG B C7  1 
HETATM 6652 C  C8  . NAG W  2 .   ? 91.779  23.691  70.817 1.00 44.46 ? 808 NAG B C8  1 
HETATM 6653 N  N2  . NAG W  2 .   ? 93.289  22.656  69.213 1.00 47.35 ? 808 NAG B N2  1 
HETATM 6654 O  O3  . NAG W  2 .   ? 95.375  22.244  67.298 1.00 47.62 ? 808 NAG B O3  1 
HETATM 6655 O  O4  . NAG W  2 .   ? 94.965  20.077  65.476 1.00 48.10 ? 808 NAG B O4  1 
HETATM 6656 O  O5  . NAG W  2 .   ? 92.950  19.059  68.383 1.00 47.05 ? 808 NAG B O5  1 
HETATM 6657 O  O6  . NAG W  2 .   ? 94.108  17.634  65.218 1.00 51.22 ? 808 NAG B O6  1 
HETATM 6658 O  O7  . NAG W  2 .   ? 93.791  22.539  71.403 1.00 42.67 ? 808 NAG B O7  1 
HETATM 6659 C  C1  . FUC X  5 .   ? 93.785  28.619  63.784 1.00 34.90 ? 809 FUC B C1  1 
HETATM 6660 C  C2  . FUC X  5 .   ? 94.800  29.649  63.274 1.00 32.54 ? 809 FUC B C2  1 
HETATM 6661 C  C3  . FUC X  5 .   ? 94.523  31.008  63.937 1.00 33.99 ? 809 FUC B C3  1 
HETATM 6662 C  C4  . FUC X  5 .   ? 94.544  30.877  65.472 1.00 28.78 ? 809 FUC B C4  1 
HETATM 6663 C  C5  . FUC X  5 .   ? 93.594  29.752  65.926 1.00 34.84 ? 809 FUC B C5  1 
HETATM 6664 C  C6  . FUC X  5 .   ? 93.702  29.440  67.412 1.00 30.37 ? 809 FUC B C6  1 
HETATM 6665 O  O2  . FUC X  5 .   ? 94.686  29.770  61.862 1.00 28.45 ? 809 FUC B O2  1 
HETATM 6666 O  O3  . FUC X  5 .   ? 95.498  31.956  63.522 1.00 30.08 ? 809 FUC B O3  1 
HETATM 6667 O  O4  . FUC X  5 .   ? 95.862  30.585  65.912 1.00 26.32 ? 809 FUC B O4  1 
HETATM 6668 O  O5  . FUC X  5 .   ? 93.888  28.520  65.210 1.00 36.52 ? 809 FUC B O5  1 
HETATM 6669 ZN ZN  . ZN  Y  6 .   ? 76.448  42.826  64.106 1.00 17.31 ? 700 ZN  B ZN  1 
HETATM 6670 CA CA  . CA  Z  7 .   ? 80.874  51.428  42.465 1.00 23.04 ? 711 CA  B CA  1 
HETATM 6671 CA CA  . CA  AA 7 .   ? 96.414  56.973  47.954 1.00 22.79 ? 712 CA  B CA  1 
HETATM 6672 CA CA  . CA  BA 7 .   ? 85.122  45.355  23.784 1.00 20.52 ? 713 CA  B CA  1 
HETATM 6673 O  O   . HOH CA 8 .   ? 92.505  3.614   35.146 1.00 20.61 ? 1   HOH A O   1 
HETATM 6674 O  O   . HOH CA 8 .   ? 87.312  -14.011 43.512 1.00 16.73 ? 2   HOH A O   1 
HETATM 6675 O  O   . HOH CA 8 .   ? 86.395  12.847  24.329 1.00 3.08  ? 3   HOH A O   1 
HETATM 6676 O  O   . HOH CA 8 .   ? 83.499  0.943   43.108 1.00 10.46 ? 4   HOH A O   1 
HETATM 6677 O  O   . HOH CA 8 .   ? 71.885  -12.940 20.732 1.00 1.00  ? 6   HOH A O   1 
HETATM 6678 O  O   . HOH CA 8 .   ? 68.116  9.730   64.505 1.00 11.00 ? 7   HOH A O   1 
HETATM 6679 O  O   . HOH CA 8 .   ? 88.898  -17.288 32.350 1.00 1.00  ? 8   HOH A O   1 
HETATM 6680 O  O   . HOH CA 8 .   ? 66.504  2.569   14.079 1.00 18.71 ? 10  HOH A O   1 
HETATM 6681 O  O   . HOH CA 8 .   ? 69.746  12.069  57.483 1.00 15.10 ? 13  HOH A O   1 
HETATM 6682 O  O   . HOH CA 8 .   ? 93.349  -7.028  18.610 1.00 10.69 ? 16  HOH A O   1 
HETATM 6683 O  O   . HOH CA 8 .   ? 87.519  11.122  14.113 1.00 15.76 ? 17  HOH A O   1 
HETATM 6684 O  O   . HOH CA 8 .   ? 103.105 -1.965  39.236 1.00 13.75 ? 19  HOH A O   1 
HETATM 6685 O  O   . HOH CA 8 .   ? 92.001  -3.270  43.771 1.00 10.80 ? 21  HOH A O   1 
HETATM 6686 O  O   . HOH CA 8 .   ? 78.859  -9.601  14.305 1.00 4.83  ? 22  HOH A O   1 
HETATM 6687 O  O   . HOH CA 8 .   ? 90.926  -14.261 22.655 1.00 17.23 ? 26  HOH A O   1 
HETATM 6688 O  O   . HOH CA 8 .   ? 89.584  10.122  12.863 1.00 5.76  ? 28  HOH A O   1 
HETATM 6689 O  O   . HOH CA 8 .   ? 72.240  -18.757 28.420 1.00 24.19 ? 31  HOH A O   1 
HETATM 6690 O  O   . HOH CA 8 .   ? 75.591  13.533  23.516 1.00 26.11 ? 33  HOH A O   1 
HETATM 6691 O  O   . HOH CA 8 .   ? 63.702  24.319  52.795 1.00 20.74 ? 35  HOH A O   1 
HETATM 6692 O  O   . HOH CA 8 .   ? 84.118  -11.767 18.553 1.00 28.78 ? 38  HOH A O   1 
HETATM 6693 O  O   . HOH CA 8 .   ? 92.451  -9.572  39.368 1.00 13.31 ? 39  HOH A O   1 
HETATM 6694 O  O   . HOH CA 8 .   ? 92.466  -10.338 42.009 1.00 17.13 ? 40  HOH A O   1 
HETATM 6695 O  O   . HOH CA 8 .   ? 72.780  -9.042  12.830 1.00 11.26 ? 43  HOH A O   1 
HETATM 6696 O  O   . HOH CA 8 .   ? 96.082  -2.517  26.126 1.00 43.22 ? 45  HOH A O   1 
HETATM 6697 O  O   . HOH CA 8 .   ? 74.357  3.362   60.848 1.00 29.84 ? 46  HOH A O   1 
HETATM 6698 O  O   . HOH CA 8 .   ? 78.121  -16.860 32.205 1.00 14.07 ? 47  HOH A O   1 
HETATM 6699 O  O   . HOH CA 8 .   ? 82.123  7.787   58.609 1.00 12.26 ? 49  HOH A O   1 
HETATM 6700 O  O   . HOH CA 8 .   ? 89.410  10.365  56.859 1.00 12.54 ? 50  HOH A O   1 
HETATM 6701 O  O   . HOH CA 8 .   ? 92.775  -7.902  35.848 1.00 30.46 ? 51  HOH A O   1 
HETATM 6702 O  O   . HOH CA 8 .   ? 90.508  -12.847 41.848 1.00 23.92 ? 54  HOH A O   1 
HETATM 6703 O  O   . HOH CA 8 .   ? 95.961  2.516   26.798 1.00 47.54 ? 55  HOH A O   1 
HETATM 6704 O  O   . HOH CA 8 .   ? 87.791  35.714  18.740 1.00 15.99 ? 56  HOH A O   1 
HETATM 6705 O  O   . HOH CA 8 .   ? 84.846  -4.777  44.881 1.00 32.87 ? 60  HOH A O   1 
HETATM 6706 O  O   . HOH CA 8 .   ? 67.946  -12.284 21.332 1.00 19.12 ? 63  HOH A O   1 
HETATM 6707 O  O   . HOH CA 8 .   ? 76.117  21.343  59.807 1.00 23.25 ? 64  HOH A O   1 
HETATM 6708 O  O   . HOH CA 8 .   ? 82.812  11.649  14.222 1.00 9.91  ? 67  HOH A O   1 
HETATM 6709 O  O   . HOH CA 8 .   ? 89.299  -5.795  35.026 1.00 18.62 ? 68  HOH A O   1 
HETATM 6710 O  O   . HOH CA 8 .   ? 64.521  -4.393  16.097 1.00 41.29 ? 69  HOH A O   1 
HETATM 6711 O  O   . HOH CA 8 .   ? 98.520  6.531   38.582 1.00 14.29 ? 72  HOH A O   1 
HETATM 6712 O  O   . HOH CA 8 .   ? 63.937  4.599   31.601 1.00 25.03 ? 74  HOH A O   1 
HETATM 6713 O  O   . HOH CA 8 .   ? 99.725  -9.798  38.611 1.00 20.04 ? 75  HOH A O   1 
HETATM 6714 O  O   . HOH CA 8 .   ? 73.459  -0.010  40.372 1.00 27.02 ? 76  HOH A O   1 
HETATM 6715 O  O   . HOH CA 8 .   ? 103.063 2.259   66.345 1.00 13.64 ? 79  HOH A O   1 
HETATM 6716 O  O   . HOH CA 8 .   ? 101.388 5.566   39.721 1.00 35.61 ? 80  HOH A O   1 
HETATM 6717 O  O   . HOH CA 8 .   ? 55.434  29.916  45.813 1.00 7.39  ? 82  HOH A O   1 
HETATM 6718 O  O   . HOH CA 8 .   ? 89.666  -17.967 29.451 1.00 17.16 ? 83  HOH A O   1 
HETATM 6719 O  O   . HOH CA 8 .   ? 86.254  3.417   65.911 1.00 11.76 ? 84  HOH A O   1 
HETATM 6720 O  O   . HOH CA 8 .   ? 79.787  -0.052  45.379 1.00 29.74 ? 86  HOH A O   1 
HETATM 6721 O  O   . HOH CA 8 .   ? 83.882  34.980  10.596 1.00 67.21 ? 89  HOH A O   1 
HETATM 6722 O  O   . HOH CA 8 .   ? 58.996  31.599  62.236 1.00 19.46 ? 90  HOH A O   1 
HETATM 6723 O  O   . HOH CA 8 .   ? 86.848  2.393   13.056 1.00 22.36 ? 91  HOH A O   1 
HETATM 6724 O  O   . HOH CA 8 .   ? 80.550  -13.611 36.440 1.00 23.71 ? 93  HOH A O   1 
HETATM 6725 O  O   . HOH CA 8 .   ? 73.864  18.097  63.061 1.00 22.31 ? 94  HOH A O   1 
HETATM 6726 O  O   . HOH CA 8 .   ? 64.964  21.256  46.081 1.00 23.40 ? 95  HOH A O   1 
HETATM 6727 O  O   . HOH CA 8 .   ? 62.805  -8.522  25.980 1.00 15.88 ? 96  HOH A O   1 
HETATM 6728 O  O   . HOH CA 8 .   ? 89.057  7.361   20.132 1.00 24.94 ? 97  HOH A O   1 
HETATM 6729 O  O   . HOH CA 8 .   ? 53.423  9.615   62.168 1.00 31.88 ? 98  HOH A O   1 
HETATM 6730 O  O   . HOH CA 8 .   ? 78.339  0.667   62.919 1.00 9.32  ? 100 HOH A O   1 
HETATM 6731 O  O   . HOH CA 8 .   ? 100.070 2.782   34.337 1.00 24.53 ? 101 HOH A O   1 
HETATM 6732 O  O   . HOH CA 8 .   ? 63.946  2.338   37.676 1.00 35.28 ? 102 HOH A O   1 
HETATM 6733 O  O   . HOH CA 8 .   ? 99.305  -1.134  27.317 1.00 28.89 ? 103 HOH A O   1 
HETATM 6734 O  O   . HOH CA 8 .   ? 94.091  3.087   16.482 1.00 11.98 ? 104 HOH A O   1 
HETATM 6735 O  O   . HOH CA 8 .   ? 78.455  16.012  67.395 1.00 47.79 ? 106 HOH A O   1 
HETATM 6736 O  O   . HOH CA 8 .   ? 67.699  14.204  71.983 1.00 26.76 ? 107 HOH A O   1 
HETATM 6737 O  O   . HOH CA 8 .   ? 93.605  17.321  26.908 1.00 28.09 ? 113 HOH A O   1 
HETATM 6738 O  O   . HOH CA 8 .   ? 76.034  15.060  61.757 1.00 25.60 ? 116 HOH A O   1 
HETATM 6739 O  O   . HOH CA 8 .   ? 64.746  7.738   61.232 1.00 21.39 ? 118 HOH A O   1 
HETATM 6740 O  O   . HOH CA 8 .   ? 109.669 -6.323  53.030 1.00 25.01 ? 119 HOH A O   1 
HETATM 6741 O  O   . HOH CA 8 .   ? 67.584  21.891  66.198 1.00 20.88 ? 120 HOH A O   1 
HETATM 6742 O  O   . HOH CA 8 .   ? 55.415  19.371  40.975 1.00 8.06  ? 122 HOH A O   1 
HETATM 6743 O  O   . HOH CA 8 .   ? 51.839  17.890  64.261 1.00 17.23 ? 128 HOH A O   1 
HETATM 6744 O  O   . HOH CA 8 .   ? 92.642  27.464  17.265 1.00 20.18 ? 131 HOH A O   1 
HETATM 6745 O  O   . HOH CA 8 .   ? 104.840 -6.178  55.180 1.00 20.78 ? 133 HOH A O   1 
HETATM 6746 O  O   . HOH CA 8 .   ? 92.232  8.872   54.845 1.00 31.12 ? 137 HOH A O   1 
HETATM 6747 O  O   . HOH CA 8 .   ? 76.673  -13.371 36.417 1.00 18.47 ? 139 HOH A O   1 
HETATM 6748 O  O   . HOH CA 8 .   ? 64.603  28.022  65.711 1.00 34.10 ? 140 HOH A O   1 
HETATM 6749 O  O   . HOH CA 8 .   ? 80.025  5.446   15.115 1.00 8.35  ? 142 HOH A O   1 
HETATM 6750 O  O   . HOH CA 8 .   ? 50.987  9.844   60.441 1.00 36.60 ? 145 HOH A O   1 
HETATM 6751 O  O   . HOH CA 8 .   ? 102.273 7.713   62.134 1.00 24.95 ? 146 HOH A O   1 
HETATM 6752 O  O   . HOH CA 8 .   ? 92.233  -14.966 29.354 1.00 40.85 ? 147 HOH A O   1 
HETATM 6753 O  O   . HOH CA 8 .   ? 56.988  6.258   50.266 1.00 29.47 ? 150 HOH A O   1 
HETATM 6754 O  O   . HOH CA 8 .   ? 52.276  12.299  56.473 1.00 16.21 ? 151 HOH A O   1 
HETATM 6755 O  O   . HOH CA 8 .   ? 93.093  -4.491  33.323 1.00 8.77  ? 152 HOH A O   1 
HETATM 6756 O  O   . HOH CA 8 .   ? 76.631  7.148   21.099 1.00 4.08  ? 153 HOH A O   1 
HETATM 6757 O  O   . HOH CA 8 .   ? 76.214  14.949  18.885 1.00 12.51 ? 154 HOH A O   1 
HETATM 6758 O  O   . HOH DA 8 .   ? 70.271  64.114  65.411 1.00 11.39 ? 5   HOH B O   1 
HETATM 6759 O  O   . HOH DA 8 .   ? 69.362  41.780  20.552 1.00 9.66  ? 9   HOH B O   1 
HETATM 6760 O  O   . HOH DA 8 .   ? 72.412  42.399  61.758 1.00 12.87 ? 11  HOH B O   1 
HETATM 6761 O  O   . HOH DA 8 .   ? 63.579  48.341  57.246 1.00 14.87 ? 12  HOH B O   1 
HETATM 6762 O  O   . HOH DA 8 .   ? 71.090  39.339  27.889 1.00 20.08 ? 14  HOH B O   1 
HETATM 6763 O  O   . HOH DA 8 .   ? 69.556  37.341  20.263 1.00 12.23 ? 15  HOH B O   1 
HETATM 6764 O  O   . HOH DA 8 .   ? 91.738  61.738  44.938 1.00 2.80  ? 18  HOH B O   1 
HETATM 6765 O  O   . HOH DA 8 .   ? 63.171  40.304  28.685 1.00 1.81  ? 20  HOH B O   1 
HETATM 6766 O  O   . HOH DA 8 .   ? 64.383  27.550  32.392 1.00 2.10  ? 23  HOH B O   1 
HETATM 6767 O  O   . HOH DA 8 .   ? 89.010  66.048  64.347 1.00 26.78 ? 24  HOH B O   1 
HETATM 6768 O  O   . HOH DA 8 .   ? 81.232  46.173  67.270 1.00 25.88 ? 27  HOH B O   1 
HETATM 6769 O  O   . HOH DA 8 .   ? 98.171  63.438  46.297 1.00 18.92 ? 29  HOH B O   1 
HETATM 6770 O  O   . HOH DA 8 .   ? 51.314  31.313  22.207 1.00 25.17 ? 30  HOH B O   1 
HETATM 6771 O  O   . HOH DA 8 .   ? 83.304  54.257  74.883 1.00 11.92 ? 34  HOH B O   1 
HETATM 6772 O  O   . HOH DA 8 .   ? 94.423  42.669  31.657 1.00 34.43 ? 36  HOH B O   1 
HETATM 6773 O  O   . HOH DA 8 .   ? 100.923 46.168  47.298 1.00 21.32 ? 37  HOH B O   1 
HETATM 6774 O  O   . HOH DA 8 .   ? 69.623  37.063  13.157 1.00 21.13 ? 41  HOH B O   1 
HETATM 6775 O  O   . HOH DA 8 .   ? 91.618  61.318  47.538 1.00 10.01 ? 42  HOH B O   1 
HETATM 6776 O  O   . HOH DA 8 .   ? 85.440  38.809  62.129 1.00 20.00 ? 44  HOH B O   1 
HETATM 6777 O  O   . HOH DA 8 .   ? 72.724  51.374  45.994 1.00 41.78 ? 48  HOH B O   1 
HETATM 6778 O  O   . HOH DA 8 .   ? 75.197  28.596  47.909 1.00 22.93 ? 52  HOH B O   1 
HETATM 6779 O  O   . HOH DA 8 .   ? 65.355  63.746  64.226 1.00 30.24 ? 53  HOH B O   1 
HETATM 6780 O  O   . HOH DA 8 .   ? 64.634  29.989  38.845 1.00 15.58 ? 57  HOH B O   1 
HETATM 6781 O  O   . HOH DA 8 .   ? 71.471  52.733  76.397 1.00 18.88 ? 58  HOH B O   1 
HETATM 6782 O  O   . HOH DA 8 .   ? 67.754  67.160  65.401 1.00 13.22 ? 59  HOH B O   1 
HETATM 6783 O  O   . HOH DA 8 .   ? 71.513  50.034  17.083 1.00 37.55 ? 61  HOH B O   1 
HETATM 6784 O  O   . HOH DA 8 .   ? 86.806  35.332  21.996 1.00 19.80 ? 62  HOH B O   1 
HETATM 6785 O  O   . HOH DA 8 .   ? 53.779  39.457  27.809 1.00 35.79 ? 65  HOH B O   1 
HETATM 6786 O  O   . HOH DA 8 .   ? 79.870  35.495  19.004 1.00 21.32 ? 66  HOH B O   1 
HETATM 6787 O  O   . HOH DA 8 .   ? 92.123  59.666  51.107 1.00 25.14 ? 70  HOH B O   1 
HETATM 6788 O  O   . HOH DA 8 .   ? 62.523  36.603  37.336 1.00 15.79 ? 71  HOH B O   1 
HETATM 6789 O  O   . HOH DA 8 .   ? 61.004  41.722  35.892 1.00 15.34 ? 73  HOH B O   1 
HETATM 6790 O  O   . HOH DA 8 .   ? 82.042  36.334  60.688 1.00 14.73 ? 77  HOH B O   1 
HETATM 6791 O  O   . HOH DA 8 .   ? 52.442  27.301  20.721 1.00 32.88 ? 78  HOH B O   1 
HETATM 6792 O  O   . HOH DA 8 .   ? 80.891  33.829  59.144 1.00 32.29 ? 81  HOH B O   1 
HETATM 6793 O  O   . HOH DA 8 .   ? 77.779  68.490  54.026 1.00 25.02 ? 85  HOH B O   1 
HETATM 6794 O  O   . HOH DA 8 .   ? 90.704  45.400  30.685 1.00 37.35 ? 87  HOH B O   1 
HETATM 6795 O  O   . HOH DA 8 .   ? 58.837  57.685  69.283 1.00 27.74 ? 88  HOH B O   1 
HETATM 6796 O  O   . HOH DA 8 .   ? 71.223  60.095  72.987 1.00 16.19 ? 92  HOH B O   1 
HETATM 6797 O  O   . HOH DA 8 .   ? 85.551  40.562  28.273 1.00 60.29 ? 99  HOH B O   1 
HETATM 6798 O  O   . HOH DA 8 .   ? 52.038  34.316  41.162 1.00 26.15 ? 105 HOH B O   1 
HETATM 6799 O  O   . HOH DA 8 .   ? 83.633  43.316  27.818 1.00 10.82 ? 108 HOH B O   1 
HETATM 6800 O  O   . HOH DA 8 .   ? 70.184  35.814  36.960 1.00 25.96 ? 110 HOH B O   1 
HETATM 6801 O  O   . HOH DA 8 .   ? 68.556  34.523  33.742 1.00 27.40 ? 111 HOH B O   1 
HETATM 6802 O  O   . HOH DA 8 .   ? 88.589  57.170  51.322 1.00 17.59 ? 112 HOH B O   1 
HETATM 6803 O  O   . HOH DA 8 .   ? 52.609  37.133  41.448 1.00 34.68 ? 114 HOH B O   1 
HETATM 6804 O  O   . HOH DA 8 .   ? 70.940  70.380  57.706 1.00 8.59  ? 115 HOH B O   1 
HETATM 6805 O  O   . HOH DA 8 .   ? 68.201  31.292  29.477 1.00 10.16 ? 117 HOH B O   1 
HETATM 6806 O  O   . HOH DA 8 .   ? 91.595  58.101  67.618 1.00 32.69 ? 121 HOH B O   1 
HETATM 6807 O  O   . HOH DA 8 .   ? 94.566  17.835  71.800 1.00 37.03 ? 123 HOH B O   1 
HETATM 6808 O  O   . HOH DA 8 .   ? 87.701  47.318  20.961 1.00 23.52 ? 124 HOH B O   1 
HETATM 6809 O  O   . HOH DA 8 .   ? 64.126  47.797  59.983 1.00 12.02 ? 125 HOH B O   1 
HETATM 6810 O  O   . HOH DA 8 .   ? 67.654  24.948  19.851 1.00 19.41 ? 126 HOH B O   1 
HETATM 6811 O  O   . HOH DA 8 .   ? 93.278  40.787  35.679 1.00 37.26 ? 127 HOH B O   1 
HETATM 6812 O  O   . HOH DA 8 .   ? 69.417  31.872  33.387 1.00 29.58 ? 129 HOH B O   1 
HETATM 6813 O  O   . HOH DA 8 .   ? 89.573  29.474  66.474 1.00 40.20 ? 130 HOH B O   1 
HETATM 6814 O  O   . HOH DA 8 .   ? 93.638  39.209  27.411 1.00 18.84 ? 132 HOH B O   1 
HETATM 6815 O  O   . HOH DA 8 .   ? 100.702 50.237  26.042 1.00 54.03 ? 134 HOH B O   1 
HETATM 6816 O  O   . HOH DA 8 .   ? 62.096  60.300  58.654 1.00 5.82  ? 135 HOH B O   1 
HETATM 6817 O  O   . HOH DA 8 .   ? 74.864  28.797  37.785 1.00 26.72 ? 136 HOH B O   1 
HETATM 6818 O  O   . HOH DA 8 .   ? 108.852 59.640  39.811 1.00 34.80 ? 141 HOH B O   1 
HETATM 6819 O  O   . HOH DA 8 .   ? 78.529  46.108  71.084 1.00 15.77 ? 143 HOH B O   1 
HETATM 6820 O  O   . HOH DA 8 .   ? 82.968  60.279  70.848 1.00 23.29 ? 144 HOH B O   1 
HETATM 6821 O  O   . HOH DA 8 .   ? 48.727  41.300  19.730 1.00 27.78 ? 148 HOH B O   1 
HETATM 6822 O  O   . HOH DA 8 .   ? 83.954  74.246  60.805 1.00 24.51 ? 149 HOH B O   1 
HETATM 6823 O  O   . HOH DA 8 .   ? 75.003  44.025  65.179 1.00 5.32  ? 155 HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   HIS 1   191 ?   ?   ?   A . n 
A 1 2   GLN 2   192 ?   ?   ?   A . n 
A 1 3   LYS 3   193 ?   ?   ?   A . n 
A 1 4   TYR 4   194 ?   ?   ?   A . n 
A 1 5   ASN 5   195 195 ASN ASN A . n 
A 1 6   PRO 6   196 196 PRO PRO A . n 
A 1 7   PHE 7   197 197 PHE PHE A . n 
A 1 8   ARG 8   198 198 ARG ARG A . n 
A 1 9   PHE 9   199 199 PHE PHE A . n 
A 1 10  VAL 10  200 200 VAL VAL A . n 
A 1 11  GLU 11  201 201 GLU GLU A . n 
A 1 12  LEU 12  202 202 LEU LEU A . n 
A 1 13  VAL 13  203 203 VAL VAL A . n 
A 1 14  LEU 14  204 204 LEU LEU A . n 
A 1 15  VAL 15  205 205 VAL VAL A . n 
A 1 16  VAL 16  206 206 VAL VAL A . n 
A 1 17  ASP 17  207 207 ASP ASP A . n 
A 1 18  LYS 18  208 208 LYS LYS A . n 
A 1 19  ALA 19  209 209 ALA ALA A . n 
A 1 20  MET 20  210 210 MET MET A . n 
A 1 21  VAL 21  211 211 VAL VAL A . n 
A 1 22  THR 22  212 212 THR THR A . n 
A 1 23  LYS 23  213 213 LYS LYS A . n 
A 1 24  ASN 24  214 214 ASN ASN A . n 
A 1 25  ASN 25  215 215 ASN ASN A . n 
A 1 26  GLY 26  216 216 GLY GLY A . n 
A 1 27  ASP 27  217 217 ASP ASP A . n 
A 1 28  LEU 28  218 218 LEU LEU A . n 
A 1 29  ASP 29  219 219 ASP ASP A . n 
A 1 30  LYS 30  220 220 LYS LYS A . n 
A 1 31  ILE 31  221 221 ILE ILE A . n 
A 1 32  LYS 32  222 222 LYS LYS A . n 
A 1 33  THR 33  223 223 THR THR A . n 
A 1 34  ARG 34  224 224 ARG ARG A . n 
A 1 35  MET 35  225 225 MET MET A . n 
A 1 36  TYR 36  226 226 TYR TYR A . n 
A 1 37  GLU 37  227 227 GLU GLU A . n 
A 1 38  ILE 38  228 228 ILE ILE A . n 
A 1 39  VAL 39  229 229 VAL VAL A . n 
A 1 40  ASN 40  230 230 ASN ASN A . n 
A 1 41  THR 41  231 231 THR THR A . n 
A 1 42  VAL 42  232 232 VAL VAL A . n 
A 1 43  ASN 43  233 233 ASN ASN A . n 
A 1 44  GLU 44  234 234 GLU GLU A . n 
A 1 45  ILE 45  235 235 ILE ILE A . n 
A 1 46  TYR 46  236 236 TYR TYR A . n 
A 1 47  ARG 47  237 237 ARG ARG A . n 
A 1 48  TYR 48  238 238 TYR TYR A . n 
A 1 49  MET 49  239 239 MET MET A . n 
A 1 50  TYR 50  240 240 TYR TYR A . n 
A 1 51  ILE 51  241 241 ILE ILE A . n 
A 1 52  HIS 52  242 242 HIS HIS A . n 
A 1 53  VAL 53  243 243 VAL VAL A . n 
A 1 54  ALA 54  244 244 ALA ALA A . n 
A 1 55  LEU 55  245 245 LEU LEU A . n 
A 1 56  VAL 56  246 246 VAL VAL A . n 
A 1 57  GLY 57  247 247 GLY GLY A . n 
A 1 58  LEU 58  248 248 LEU LEU A . n 
A 1 59  GLU 59  249 249 GLU GLU A . n 
A 1 60  ILE 60  250 250 ILE ILE A . n 
A 1 61  TRP 61  251 251 TRP TRP A . n 
A 1 62  SER 62  252 252 SER SER A . n 
A 1 63  ASN 63  253 253 ASN ASN A . n 
A 1 64  GLU 64  254 254 GLU GLU A . n 
A 1 65  ASP 65  255 255 ASP ASP A . n 
A 1 66  LYS 66  256 256 LYS LYS A . n 
A 1 67  ILE 67  257 257 ILE ILE A . n 
A 1 68  THR 68  258 258 THR THR A . n 
A 1 69  VAL 69  259 259 VAL VAL A . n 
A 1 70  LYS 70  260 260 LYS LYS A . n 
A 1 71  PRO 71  261 261 PRO PRO A . n 
A 1 72  GLU 72  262 262 GLU GLU A . n 
A 1 73  ALA 73  263 263 ALA ALA A . n 
A 1 74  GLY 74  264 264 GLY GLY A . n 
A 1 75  TYR 75  265 265 TYR TYR A . n 
A 1 76  THR 76  266 266 THR THR A . n 
A 1 77  LEU 77  267 267 LEU LEU A . n 
A 1 78  ASN 78  268 268 ASN ASN A . n 
A 1 79  ALA 79  269 269 ALA ALA A . n 
A 1 80  PHE 80  270 270 PHE PHE A . n 
A 1 81  GLY 81  271 271 GLY GLY A . n 
A 1 82  GLU 82  272 272 GLU GLU A . n 
A 1 83  TRP 83  273 273 TRP TRP A . n 
A 1 84  ARG 84  274 274 ARG ARG A . n 
A 1 85  LYS 85  275 275 LYS LYS A . n 
A 1 86  THR 86  276 276 THR THR A . n 
A 1 87  ASP 87  277 277 ASP ASP A . n 
A 1 88  LEU 88  278 278 LEU LEU A . n 
A 1 89  LEU 89  279 279 LEU LEU A . n 
A 1 90  THR 90  280 280 THR THR A . n 
A 1 91  ARG 91  281 281 ARG ARG A . n 
A 1 92  LYS 92  282 282 LYS LYS A . n 
A 1 93  LYS 93  283 283 LYS LYS A . n 
A 1 94  HIS 94  284 284 HIS HIS A . n 
A 1 95  ASP 95  285 285 ASP ASP A . n 
A 1 96  ASN 96  286 286 ASN ASN A . n 
A 1 97  ALA 97  287 287 ALA ALA A . n 
A 1 98  GLN 98  288 288 GLN GLN A . n 
A 1 99  LEU 99  289 289 LEU LEU A . n 
A 1 100 LEU 100 290 290 LEU LEU A . n 
A 1 101 THR 101 291 291 THR THR A . n 
A 1 102 ALA 102 292 292 ALA ALA A . n 
A 1 103 ILE 103 293 293 ILE ILE A . n 
A 1 104 ASP 104 294 294 ASP ASP A . n 
A 1 105 LEU 105 295 295 LEU LEU A . n 
A 1 106 ASP 106 296 296 ASP ASP A . n 
A 1 107 ARG 107 297 297 ARG ARG A . n 
A 1 108 VAL 108 298 298 VAL VAL A . n 
A 1 109 ILE 109 299 299 ILE ILE A . n 
A 1 110 GLY 110 300 300 GLY GLY A . n 
A 1 111 LEU 111 301 301 LEU LEU A . n 
A 1 112 ALA 112 302 302 ALA ALA A . n 
A 1 113 TYR 113 303 303 TYR TYR A . n 
A 1 114 VAL 114 304 304 VAL VAL A . n 
A 1 115 GLY 115 305 305 GLY GLY A . n 
A 1 116 SER 116 306 306 SER SER A . n 
A 1 117 MET 117 307 307 MET MET A . n 
A 1 118 CYS 118 308 308 CYS CYS A . n 
A 1 119 HIS 119 309 309 HIS HIS A . n 
A 1 120 PRO 120 310 310 PRO PRO A . n 
A 1 121 LYS 121 311 311 LYS LYS A . n 
A 1 122 ARG 122 312 312 ARG ARG A . n 
A 1 123 SER 123 313 313 SER SER A . n 
A 1 124 THR 124 314 314 THR THR A . n 
A 1 125 GLY 125 315 315 GLY GLY A . n 
A 1 126 ILE 126 316 316 ILE ILE A . n 
A 1 127 ILE 127 317 317 ILE ILE A . n 
A 1 128 GLN 128 318 318 GLN GLN A . n 
A 1 129 ASP 129 319 319 ASP ASP A . n 
A 1 130 TYR 130 320 320 TYR TYR A . n 
A 1 131 SER 131 321 321 SER SER A . n 
A 1 132 GLU 132 322 322 GLU GLU A . n 
A 1 133 ILE 133 323 323 ILE ILE A . n 
A 1 134 ASN 134 324 324 ASN ASN A . n 
A 1 135 LEU 135 325 325 LEU LEU A . n 
A 1 136 VAL 136 326 326 VAL VAL A . n 
A 1 137 VAL 137 327 327 VAL VAL A . n 
A 1 138 ALA 138 328 328 ALA ALA A . n 
A 1 139 VAL 139 329 329 VAL VAL A . n 
A 1 140 ILE 140 330 330 ILE ILE A . n 
A 1 141 MET 141 331 331 MET MET A . n 
A 1 142 ALA 142 332 332 ALA ALA A . n 
A 1 143 HIS 143 333 333 HIS HIS A . n 
A 1 144 GLU 144 334 334 GLU GLU A . n 
A 1 145 MET 145 335 335 MET MET A . n 
A 1 146 GLY 146 336 336 GLY GLY A . n 
A 1 147 HIS 147 337 337 HIS HIS A . n 
A 1 148 ASN 148 338 338 ASN ASN A . n 
A 1 149 LEU 149 339 339 LEU LEU A . n 
A 1 150 GLY 150 340 340 GLY GLY A . n 
A 1 151 ILE 151 341 341 ILE ILE A . n 
A 1 152 ASN 152 342 342 ASN ASN A . n 
A 1 153 HIS 153 343 343 HIS HIS A . n 
A 1 154 ASP 154 344 344 ASP ASP A . n 
A 1 155 SER 155 345 345 SER SER A . n 
A 1 156 GLY 156 346 346 GLY GLY A . n 
A 1 157 TYR 157 347 347 TYR TYR A . n 
A 1 158 CYS 158 348 348 CYS CYS A . n 
A 1 159 SER 159 349 349 SER SER A . n 
A 1 160 CYS 160 350 350 CYS CYS A . n 
A 1 161 GLY 161 351 351 GLY GLY A . n 
A 1 162 ASP 162 352 352 ASP ASP A . n 
A 1 163 TYR 163 353 353 TYR TYR A . n 
A 1 164 ALA 164 354 354 ALA ALA A . n 
A 1 165 CYS 165 355 355 CYS CYS A . n 
A 1 166 ILE 166 356 356 ILE ILE A . n 
A 1 167 MET 167 357 357 MET MET A . n 
A 1 168 ARG 168 358 358 ARG ARG A . n 
A 1 169 PRO 169 359 359 PRO PRO A . n 
A 1 170 GLU 170 360 360 GLU GLU A . n 
A 1 171 ILE 171 361 361 ILE ILE A . n 
A 1 172 SER 172 362 362 SER SER A . n 
A 1 173 PRO 173 363 363 PRO PRO A . n 
A 1 174 GLU 174 364 364 GLU GLU A . n 
A 1 175 PRO 175 365 365 PRO PRO A . n 
A 1 176 SER 176 366 366 SER SER A . n 
A 1 177 THR 177 367 367 THR THR A . n 
A 1 178 PHE 178 368 368 PHE PHE A . n 
A 1 179 PHE 179 369 369 PHE PHE A . n 
A 1 180 SER 180 370 370 SER SER A . n 
A 1 181 ASN 181 371 371 ASN ASN A . n 
A 1 182 CYS 182 372 372 CYS CYS A . n 
A 1 183 SER 183 373 373 SER SER A . n 
A 1 184 TYR 184 374 374 TYR TYR A . n 
A 1 185 PHE 185 375 375 PHE PHE A . n 
A 1 186 GLU 186 376 376 GLU GLU A . n 
A 1 187 CYS 187 377 377 CYS CYS A . n 
A 1 188 TRP 188 378 378 TRP TRP A . n 
A 1 189 ASP 189 379 379 ASP ASP A . n 
A 1 190 PHE 190 380 380 PHE PHE A . n 
A 1 191 ILE 191 381 381 ILE ILE A . n 
A 1 192 MET 192 382 382 MET MET A . n 
A 1 193 ASN 193 383 383 ASN ASN A . n 
A 1 194 HIS 194 384 384 HIS HIS A . n 
A 1 195 ASN 195 385 385 ASN ASN A . n 
A 1 196 PRO 196 386 386 PRO PRO A . n 
A 1 197 GLU 197 387 387 GLU GLU A . n 
A 1 198 CYS 198 388 388 CYS CYS A . n 
A 1 199 ILE 199 389 389 ILE ILE A . n 
A 1 200 LEU 200 390 390 LEU LEU A . n 
A 1 201 ASN 201 391 391 ASN ASN A . n 
A 1 202 GLU 202 392 392 GLU GLU A . n 
A 1 203 PRO 203 393 393 PRO PRO A . n 
A 1 204 LEU 204 394 394 LEU LEU A . n 
A 1 205 GLY 205 395 395 GLY GLY A . n 
A 1 206 THR 206 396 396 THR THR A . n 
A 1 207 ASP 207 397 397 ASP ASP A . n 
A 1 208 ILE 208 398 398 ILE ILE A . n 
A 1 209 ILE 209 399 399 ILE ILE A . n 
A 1 210 SER 210 400 400 SER SER A . n 
A 1 211 PRO 211 401 401 PRO PRO A . n 
A 1 212 PRO 212 402 402 PRO PRO A . n 
A 1 213 VAL 213 403 403 VAL VAL A . n 
A 1 214 CYS 214 404 404 CYS CYS A . n 
A 1 215 GLY 215 405 405 GLY GLY A . n 
A 1 216 ASN 216 406 406 ASN ASN A . n 
A 1 217 GLU 217 407 407 GLU GLU A . n 
A 1 218 LEU 218 408 408 LEU LEU A . n 
A 1 219 LEU 219 409 409 LEU LEU A . n 
A 1 220 GLU 220 410 410 GLU GLU A . n 
A 1 221 VAL 221 411 411 VAL VAL A . n 
A 1 222 GLY 222 412 412 GLY GLY A . n 
A 1 223 GLU 223 413 413 GLU GLU A . n 
A 1 224 GLU 224 414 414 GLU GLU A . n 
A 1 225 CYS 225 415 415 CYS CYS A . n 
A 1 226 ASP 226 416 416 ASP ASP A . n 
A 1 227 CYS 227 417 417 CYS CYS A . n 
A 1 228 GLY 228 418 418 GLY GLY A . n 
A 1 229 THR 229 419 419 THR THR A . n 
A 1 230 PRO 230 420 420 PRO PRO A . n 
A 1 231 GLU 231 421 421 GLU GLU A . n 
A 1 232 ASN 232 422 422 ASN ASN A . n 
A 1 233 CYS 233 423 423 CYS CYS A . n 
A 1 234 GLN 234 424 424 GLN GLN A . n 
A 1 235 ASN 235 425 425 ASN ASN A . n 
A 1 236 GLU 236 426 426 GLU GLU A . n 
A 1 237 CYS 237 427 427 CYS CYS A . n 
A 1 238 CYS 238 428 428 CYS CYS A . n 
A 1 239 ASP 239 429 429 ASP ASP A . n 
A 1 240 ALA 240 430 430 ALA ALA A . n 
A 1 241 ALA 241 431 431 ALA ALA A . n 
A 1 242 THR 242 432 432 THR THR A . n 
A 1 243 CYS 243 433 433 CYS CYS A . n 
A 1 244 LYS 244 434 434 LYS LYS A . n 
A 1 245 LEU 245 435 435 LEU LEU A . n 
A 1 246 LYS 246 436 436 LYS LYS A . n 
A 1 247 SER 247 437 437 SER SER A . n 
A 1 248 GLY 248 438 438 GLY GLY A . n 
A 1 249 SER 249 439 439 SER SER A . n 
A 1 250 GLN 250 440 440 GLN GLN A . n 
A 1 251 CYS 251 441 441 CYS CYS A . n 
A 1 252 GLY 252 442 442 GLY GLY A . n 
A 1 253 HIS 253 443 443 HIS HIS A . n 
A 1 254 GLY 254 444 444 GLY GLY A . n 
A 1 255 ASP 255 445 445 ASP ASP A . n 
A 1 256 CYS 256 446 446 CYS CYS A . n 
A 1 257 CYS 257 447 447 CYS CYS A . n 
A 1 258 GLU 258 448 448 GLU GLU A . n 
A 1 259 GLN 259 449 449 GLN GLN A . n 
A 1 260 CYS 260 450 450 CYS CYS A . n 
A 1 261 LYS 261 451 451 LYS LYS A . n 
A 1 262 PHE 262 452 452 PHE PHE A . n 
A 1 263 SER 263 453 453 SER SER A . n 
A 1 264 LYS 264 454 454 LYS LYS A . n 
A 1 265 SER 265 455 455 SER SER A . n 
A 1 266 GLY 266 456 456 GLY GLY A . n 
A 1 267 THR 267 457 457 THR THR A . n 
A 1 268 GLU 268 458 458 GLU GLU A . n 
A 1 269 CYS 269 459 459 CYS CYS A . n 
A 1 270 ARG 270 460 460 ARG ARG A . n 
A 1 271 ALA 271 461 461 ALA ALA A . n 
A 1 272 SER 272 462 462 SER SER A . n 
A 1 273 MET 273 463 463 MET MET A . n 
A 1 274 SER 274 464 464 SER SER A . n 
A 1 275 GLU 275 465 465 GLU GLU A . n 
A 1 276 CYS 276 466 466 CYS CYS A . n 
A 1 277 ASP 277 467 467 ASP ASP A . n 
A 1 278 PRO 278 468 468 PRO PRO A . n 
A 1 279 ALA 279 469 469 ALA ALA A . n 
A 1 280 GLU 280 470 470 GLU GLU A . n 
A 1 281 HIS 281 471 471 HIS HIS A . n 
A 1 282 CYS 282 472 472 CYS CYS A . n 
A 1 283 THR 283 473 473 THR THR A . n 
A 1 284 GLY 284 474 474 GLY GLY A . n 
A 1 285 GLN 285 475 475 GLN GLN A . n 
A 1 286 SER 286 476 476 SER SER A . n 
A 1 287 SER 287 477 477 SER SER A . n 
A 1 288 GLU 288 478 478 GLU GLU A . n 
A 1 289 CYS 289 479 479 CYS CYS A . n 
A 1 290 PRO 290 480 480 PRO PRO A . n 
A 1 291 ALA 291 481 481 ALA ALA A . n 
A 1 292 ASP 292 482 482 ASP ASP A . n 
A 1 293 VAL 293 483 483 VAL VAL A . n 
A 1 294 PHE 294 484 484 PHE PHE A . n 
A 1 295 HIS 295 485 485 HIS HIS A . n 
A 1 296 LYS 296 486 486 LYS LYS A . n 
A 1 297 ASN 297 487 487 ASN ASN A . n 
A 1 298 GLY 298 488 488 GLY GLY A . n 
A 1 299 GLN 299 489 489 GLN GLN A . n 
A 1 300 PRO 300 490 490 PRO PRO A . n 
A 1 301 CYS 301 491 491 CYS CYS A . n 
A 1 302 LEU 302 492 492 LEU LEU A . n 
A 1 303 ASP 303 493 493 ASP ASP A . n 
A 1 304 ASN 304 494 494 ASN ASN A . n 
A 1 305 TYR 305 495 495 TYR TYR A . n 
A 1 306 GLY 306 496 496 GLY GLY A . n 
A 1 307 TYR 307 497 497 TYR TYR A . n 
A 1 308 CYS 308 498 498 CYS CYS A . n 
A 1 309 TYR 309 499 499 TYR TYR A . n 
A 1 310 ASN 310 500 500 ASN ASN A . n 
A 1 311 GLY 311 501 501 GLY GLY A . n 
A 1 312 ASN 312 502 502 ASN ASN A . n 
A 1 313 CYS 313 503 503 CYS CYS A . n 
A 1 314 PRO 314 504 504 PRO PRO A . n 
A 1 315 ILE 315 505 505 ILE ILE A . n 
A 1 316 MET 316 506 506 MET MET A . n 
A 1 317 TYR 317 507 507 TYR TYR A . n 
A 1 318 HIS 318 508 508 HIS HIS A . n 
A 1 319 GLN 319 509 509 GLN GLN A . n 
A 1 320 CYS 320 510 510 CYS CYS A . n 
A 1 321 TYR 321 511 511 TYR TYR A . n 
A 1 322 ASP 322 512 512 ASP ASP A . n 
A 1 323 LEU 323 513 513 LEU LEU A . n 
A 1 324 PHE 324 514 514 PHE PHE A . n 
A 1 325 GLY 325 515 515 GLY GLY A . n 
A 1 326 ALA 326 516 516 ALA ALA A . n 
A 1 327 ASP 327 517 517 ASP ASP A . n 
A 1 328 VAL 328 518 518 VAL VAL A . n 
A 1 329 TYR 329 519 519 TYR TYR A . n 
A 1 330 GLU 330 520 520 GLU GLU A . n 
A 1 331 ALA 331 521 521 ALA ALA A . n 
A 1 332 GLU 332 522 522 GLU GLU A . n 
A 1 333 ASP 333 523 523 ASP ASP A . n 
A 1 334 SER 334 524 524 SER SER A . n 
A 1 335 CYS 335 525 525 CYS CYS A . n 
A 1 336 PHE 336 526 526 PHE PHE A . n 
A 1 337 GLU 337 527 527 GLU GLU A . n 
A 1 338 ARG 338 528 528 ARG ARG A . n 
A 1 339 ASN 339 529 529 ASN ASN A . n 
A 1 340 GLN 340 530 530 GLN GLN A . n 
A 1 341 LYS 341 531 531 LYS LYS A . n 
A 1 342 GLY 342 532 532 GLY GLY A . n 
A 1 343 ASN 343 533 533 ASN ASN A . n 
A 1 344 TYR 344 534 534 TYR TYR A . n 
A 1 345 TYR 345 535 535 TYR TYR A . n 
A 1 346 GLY 346 536 536 GLY GLY A . n 
A 1 347 TYR 347 537 537 TYR TYR A . n 
A 1 348 CYS 348 538 538 CYS CYS A . n 
A 1 349 ARG 349 539 539 ARG ARG A . n 
A 1 350 LYS 350 540 540 LYS LYS A . n 
A 1 351 GLU 351 541 541 GLU GLU A . n 
A 1 352 ASN 352 542 542 ASN ASN A . n 
A 1 353 GLY 353 543 543 GLY GLY A . n 
A 1 354 ASN 354 544 544 ASN ASN A . n 
A 1 355 LYS 355 545 545 LYS LYS A . n 
A 1 356 ILE 356 546 546 ILE ILE A . n 
A 1 357 PRO 357 547 547 PRO PRO A . n 
A 1 358 CYS 358 548 548 CYS CYS A . n 
A 1 359 ALA 359 549 549 ALA ALA A . n 
A 1 360 PRO 360 550 550 PRO PRO A . n 
A 1 361 GLU 361 551 551 GLU GLU A . n 
A 1 362 ASP 362 552 552 ASP ASP A . n 
A 1 363 VAL 363 553 553 VAL VAL A . n 
A 1 364 LYS 364 554 554 LYS LYS A . n 
A 1 365 CYS 365 555 555 CYS CYS A . n 
A 1 366 GLY 366 556 556 GLY GLY A . n 
A 1 367 ARG 367 557 557 ARG ARG A . n 
A 1 368 LEU 368 558 558 LEU LEU A . n 
A 1 369 TYR 369 559 559 TYR TYR A . n 
A 1 370 CYS 370 560 560 CYS CYS A . n 
A 1 371 LYS 371 561 561 LYS LYS A . n 
A 1 372 ASP 372 562 562 ASP ASP A . n 
A 1 373 ASN 373 563 563 ASN ASN A . n 
A 1 374 SER 374 564 564 SER SER A . n 
A 1 375 PRO 375 565 565 PRO PRO A . n 
A 1 376 GLY 376 566 566 GLY GLY A . n 
A 1 377 GLN 377 567 567 GLN GLN A . n 
A 1 378 ASN 378 568 568 ASN ASN A . n 
A 1 379 ASN 379 569 569 ASN ASN A . n 
A 1 380 PRO 380 570 570 PRO PRO A . n 
A 1 381 CYS 381 571 571 CYS CYS A . n 
A 1 382 LYS 382 572 572 LYS LYS A . n 
A 1 383 MET 383 573 573 MET MET A . n 
A 1 384 PHE 384 574 574 PHE PHE A . n 
A 1 385 TYR 385 575 575 TYR TYR A . n 
A 1 386 SER 386 576 576 SER SER A . n 
A 1 387 ASN 387 577 577 ASN ASN A . n 
A 1 388 GLU 388 578 578 GLU GLU A . n 
A 1 389 ASP 389 579 579 ASP ASP A . n 
A 1 390 GLU 390 580 580 GLU GLU A . n 
A 1 391 HIS 391 581 581 HIS HIS A . n 
A 1 392 LYS 392 582 582 LYS LYS A . n 
A 1 393 GLY 393 583 583 GLY GLY A . n 
A 1 394 MET 394 584 584 MET MET A . n 
A 1 395 VAL 395 585 585 VAL VAL A . n 
A 1 396 LEU 396 586 586 LEU LEU A . n 
A 1 397 PRO 397 587 587 PRO PRO A . n 
A 1 398 GLY 398 588 588 GLY GLY A . n 
A 1 399 THR 399 589 589 THR THR A . n 
A 1 400 LYS 400 590 590 LYS LYS A . n 
A 1 401 CYS 401 591 591 CYS CYS A . n 
A 1 402 ALA 402 592 592 ALA ALA A . n 
A 1 403 ASP 403 593 593 ASP ASP A . n 
A 1 404 GLY 404 594 594 GLY GLY A . n 
A 1 405 LYS 405 595 595 LYS LYS A . n 
A 1 406 VAL 406 596 596 VAL VAL A . n 
A 1 407 CYS 407 597 597 CYS CYS A . n 
A 1 408 SER 408 598 598 SER SER A . n 
A 1 409 ASN 409 599 599 ASN ASN A . n 
A 1 410 GLY 410 600 600 GLY GLY A . n 
A 1 411 HIS 411 601 601 HIS HIS A . n 
A 1 412 CYS 412 602 602 CYS CYS A . n 
A 1 413 VAL 413 603 603 VAL VAL A . n 
A 1 414 ASP 414 604 604 ASP ASP A . n 
A 1 415 VAL 415 605 605 VAL VAL A . n 
A 1 416 ALA 416 606 606 ALA ALA A . n 
A 1 417 THR 417 607 607 THR THR A . n 
A 1 418 ALA 418 608 608 ALA ALA A . n 
A 1 419 TYR 419 609 609 TYR TYR A . n 
B 1 1   HIS 1   191 ?   ?   ?   B . n 
B 1 2   GLN 2   192 ?   ?   ?   B . n 
B 1 3   LYS 3   193 ?   ?   ?   B . n 
B 1 4   TYR 4   194 ?   ?   ?   B . n 
B 1 5   ASN 5   195 195 ASN ASN B . n 
B 1 6   PRO 6   196 196 PRO PRO B . n 
B 1 7   PHE 7   197 197 PHE PHE B . n 
B 1 8   ARG 8   198 198 ARG ARG B . n 
B 1 9   PHE 9   199 199 PHE PHE B . n 
B 1 10  VAL 10  200 200 VAL VAL B . n 
B 1 11  GLU 11  201 201 GLU GLU B . n 
B 1 12  LEU 12  202 202 LEU LEU B . n 
B 1 13  VAL 13  203 203 VAL VAL B . n 
B 1 14  LEU 14  204 204 LEU LEU B . n 
B 1 15  VAL 15  205 205 VAL VAL B . n 
B 1 16  VAL 16  206 206 VAL VAL B . n 
B 1 17  ASP 17  207 207 ASP ASP B . n 
B 1 18  LYS 18  208 208 LYS LYS B . n 
B 1 19  ALA 19  209 209 ALA ALA B . n 
B 1 20  MET 20  210 210 MET MET B . n 
B 1 21  VAL 21  211 211 VAL VAL B . n 
B 1 22  THR 22  212 212 THR THR B . n 
B 1 23  LYS 23  213 213 LYS LYS B . n 
B 1 24  ASN 24  214 214 ASN ASN B . n 
B 1 25  ASN 25  215 215 ASN ASN B . n 
B 1 26  GLY 26  216 216 GLY GLY B . n 
B 1 27  ASP 27  217 217 ASP ASP B . n 
B 1 28  LEU 28  218 218 LEU LEU B . n 
B 1 29  ASP 29  219 219 ASP ASP B . n 
B 1 30  LYS 30  220 220 LYS LYS B . n 
B 1 31  ILE 31  221 221 ILE ILE B . n 
B 1 32  LYS 32  222 222 LYS LYS B . n 
B 1 33  THR 33  223 223 THR THR B . n 
B 1 34  ARG 34  224 224 ARG ARG B . n 
B 1 35  MET 35  225 225 MET MET B . n 
B 1 36  TYR 36  226 226 TYR TYR B . n 
B 1 37  GLU 37  227 227 GLU GLU B . n 
B 1 38  ILE 38  228 228 ILE ILE B . n 
B 1 39  VAL 39  229 229 VAL VAL B . n 
B 1 40  ASN 40  230 230 ASN ASN B . n 
B 1 41  THR 41  231 231 THR THR B . n 
B 1 42  VAL 42  232 232 VAL VAL B . n 
B 1 43  ASN 43  233 233 ASN ASN B . n 
B 1 44  GLU 44  234 234 GLU GLU B . n 
B 1 45  ILE 45  235 235 ILE ILE B . n 
B 1 46  TYR 46  236 236 TYR TYR B . n 
B 1 47  ARG 47  237 237 ARG ARG B . n 
B 1 48  TYR 48  238 238 TYR TYR B . n 
B 1 49  MET 49  239 239 MET MET B . n 
B 1 50  TYR 50  240 240 TYR TYR B . n 
B 1 51  ILE 51  241 241 ILE ILE B . n 
B 1 52  HIS 52  242 242 HIS HIS B . n 
B 1 53  VAL 53  243 243 VAL VAL B . n 
B 1 54  ALA 54  244 244 ALA ALA B . n 
B 1 55  LEU 55  245 245 LEU LEU B . n 
B 1 56  VAL 56  246 246 VAL VAL B . n 
B 1 57  GLY 57  247 247 GLY GLY B . n 
B 1 58  LEU 58  248 248 LEU LEU B . n 
B 1 59  GLU 59  249 249 GLU GLU B . n 
B 1 60  ILE 60  250 250 ILE ILE B . n 
B 1 61  TRP 61  251 251 TRP TRP B . n 
B 1 62  SER 62  252 252 SER SER B . n 
B 1 63  ASN 63  253 253 ASN ASN B . n 
B 1 64  GLU 64  254 254 GLU GLU B . n 
B 1 65  ASP 65  255 255 ASP ASP B . n 
B 1 66  LYS 66  256 256 LYS LYS B . n 
B 1 67  ILE 67  257 257 ILE ILE B . n 
B 1 68  THR 68  258 258 THR THR B . n 
B 1 69  VAL 69  259 259 VAL VAL B . n 
B 1 70  LYS 70  260 260 LYS LYS B . n 
B 1 71  PRO 71  261 261 PRO PRO B . n 
B 1 72  GLU 72  262 262 GLU GLU B . n 
B 1 73  ALA 73  263 263 ALA ALA B . n 
B 1 74  GLY 74  264 264 GLY GLY B . n 
B 1 75  TYR 75  265 265 TYR TYR B . n 
B 1 76  THR 76  266 266 THR THR B . n 
B 1 77  LEU 77  267 267 LEU LEU B . n 
B 1 78  ASN 78  268 268 ASN ASN B . n 
B 1 79  ALA 79  269 269 ALA ALA B . n 
B 1 80  PHE 80  270 270 PHE PHE B . n 
B 1 81  GLY 81  271 271 GLY GLY B . n 
B 1 82  GLU 82  272 272 GLU GLU B . n 
B 1 83  TRP 83  273 273 TRP TRP B . n 
B 1 84  ARG 84  274 274 ARG ARG B . n 
B 1 85  LYS 85  275 275 LYS LYS B . n 
B 1 86  THR 86  276 276 THR THR B . n 
B 1 87  ASP 87  277 277 ASP ASP B . n 
B 1 88  LEU 88  278 278 LEU LEU B . n 
B 1 89  LEU 89  279 279 LEU LEU B . n 
B 1 90  THR 90  280 280 THR THR B . n 
B 1 91  ARG 91  281 281 ARG ARG B . n 
B 1 92  LYS 92  282 282 LYS LYS B . n 
B 1 93  LYS 93  283 283 LYS LYS B . n 
B 1 94  HIS 94  284 284 HIS HIS B . n 
B 1 95  ASP 95  285 285 ASP ASP B . n 
B 1 96  ASN 96  286 286 ASN ASN B . n 
B 1 97  ALA 97  287 287 ALA ALA B . n 
B 1 98  GLN 98  288 288 GLN GLN B . n 
B 1 99  LEU 99  289 289 LEU LEU B . n 
B 1 100 LEU 100 290 290 LEU LEU B . n 
B 1 101 THR 101 291 291 THR THR B . n 
B 1 102 ALA 102 292 292 ALA ALA B . n 
B 1 103 ILE 103 293 293 ILE ILE B . n 
B 1 104 ASP 104 294 294 ASP ASP B . n 
B 1 105 LEU 105 295 295 LEU LEU B . n 
B 1 106 ASP 106 296 296 ASP ASP B . n 
B 1 107 ARG 107 297 297 ARG ARG B . n 
B 1 108 VAL 108 298 298 VAL VAL B . n 
B 1 109 ILE 109 299 299 ILE ILE B . n 
B 1 110 GLY 110 300 300 GLY GLY B . n 
B 1 111 LEU 111 301 301 LEU LEU B . n 
B 1 112 ALA 112 302 302 ALA ALA B . n 
B 1 113 TYR 113 303 303 TYR TYR B . n 
B 1 114 VAL 114 304 304 VAL VAL B . n 
B 1 115 GLY 115 305 305 GLY GLY B . n 
B 1 116 SER 116 306 306 SER SER B . n 
B 1 117 MET 117 307 307 MET MET B . n 
B 1 118 CYS 118 308 308 CYS CYS B . n 
B 1 119 HIS 119 309 309 HIS HIS B . n 
B 1 120 PRO 120 310 310 PRO PRO B . n 
B 1 121 LYS 121 311 311 LYS LYS B . n 
B 1 122 ARG 122 312 312 ARG ARG B . n 
B 1 123 SER 123 313 313 SER SER B . n 
B 1 124 THR 124 314 314 THR THR B . n 
B 1 125 GLY 125 315 315 GLY GLY B . n 
B 1 126 ILE 126 316 316 ILE ILE B . n 
B 1 127 ILE 127 317 317 ILE ILE B . n 
B 1 128 GLN 128 318 318 GLN GLN B . n 
B 1 129 ASP 129 319 319 ASP ASP B . n 
B 1 130 TYR 130 320 320 TYR TYR B . n 
B 1 131 SER 131 321 321 SER SER B . n 
B 1 132 GLU 132 322 322 GLU GLU B . n 
B 1 133 ILE 133 323 323 ILE ILE B . n 
B 1 134 ASN 134 324 324 ASN ASN B . n 
B 1 135 LEU 135 325 325 LEU LEU B . n 
B 1 136 VAL 136 326 326 VAL VAL B . n 
B 1 137 VAL 137 327 327 VAL VAL B . n 
B 1 138 ALA 138 328 328 ALA ALA B . n 
B 1 139 VAL 139 329 329 VAL VAL B . n 
B 1 140 ILE 140 330 330 ILE ILE B . n 
B 1 141 MET 141 331 331 MET MET B . n 
B 1 142 ALA 142 332 332 ALA ALA B . n 
B 1 143 HIS 143 333 333 HIS HIS B . n 
B 1 144 GLU 144 334 334 GLU GLU B . n 
B 1 145 MET 145 335 335 MET MET B . n 
B 1 146 GLY 146 336 336 GLY GLY B . n 
B 1 147 HIS 147 337 337 HIS HIS B . n 
B 1 148 ASN 148 338 338 ASN ASN B . n 
B 1 149 LEU 149 339 339 LEU LEU B . n 
B 1 150 GLY 150 340 340 GLY GLY B . n 
B 1 151 ILE 151 341 341 ILE ILE B . n 
B 1 152 ASN 152 342 342 ASN ASN B . n 
B 1 153 HIS 153 343 343 HIS HIS B . n 
B 1 154 ASP 154 344 344 ASP ASP B . n 
B 1 155 SER 155 345 345 SER SER B . n 
B 1 156 GLY 156 346 346 GLY GLY B . n 
B 1 157 TYR 157 347 347 TYR TYR B . n 
B 1 158 CYS 158 348 348 CYS CYS B . n 
B 1 159 SER 159 349 349 SER SER B . n 
B 1 160 CYS 160 350 350 CYS CYS B . n 
B 1 161 GLY 161 351 351 GLY GLY B . n 
B 1 162 ASP 162 352 352 ASP ASP B . n 
B 1 163 TYR 163 353 353 TYR TYR B . n 
B 1 164 ALA 164 354 354 ALA ALA B . n 
B 1 165 CYS 165 355 355 CYS CYS B . n 
B 1 166 ILE 166 356 356 ILE ILE B . n 
B 1 167 MET 167 357 357 MET MET B . n 
B 1 168 ARG 168 358 358 ARG ARG B . n 
B 1 169 PRO 169 359 359 PRO PRO B . n 
B 1 170 GLU 170 360 360 GLU GLU B . n 
B 1 171 ILE 171 361 361 ILE ILE B . n 
B 1 172 SER 172 362 362 SER SER B . n 
B 1 173 PRO 173 363 363 PRO PRO B . n 
B 1 174 GLU 174 364 364 GLU GLU B . n 
B 1 175 PRO 175 365 365 PRO PRO B . n 
B 1 176 SER 176 366 366 SER SER B . n 
B 1 177 THR 177 367 367 THR THR B . n 
B 1 178 PHE 178 368 368 PHE PHE B . n 
B 1 179 PHE 179 369 369 PHE PHE B . n 
B 1 180 SER 180 370 370 SER SER B . n 
B 1 181 ASN 181 371 371 ASN ASN B . n 
B 1 182 CYS 182 372 372 CYS CYS B . n 
B 1 183 SER 183 373 373 SER SER B . n 
B 1 184 TYR 184 374 374 TYR TYR B . n 
B 1 185 PHE 185 375 375 PHE PHE B . n 
B 1 186 GLU 186 376 376 GLU GLU B . n 
B 1 187 CYS 187 377 377 CYS CYS B . n 
B 1 188 TRP 188 378 378 TRP TRP B . n 
B 1 189 ASP 189 379 379 ASP ASP B . n 
B 1 190 PHE 190 380 380 PHE PHE B . n 
B 1 191 ILE 191 381 381 ILE ILE B . n 
B 1 192 MET 192 382 382 MET MET B . n 
B 1 193 ASN 193 383 383 ASN ASN B . n 
B 1 194 HIS 194 384 384 HIS HIS B . n 
B 1 195 ASN 195 385 385 ASN ASN B . n 
B 1 196 PRO 196 386 386 PRO PRO B . n 
B 1 197 GLU 197 387 387 GLU GLU B . n 
B 1 198 CYS 198 388 388 CYS CYS B . n 
B 1 199 ILE 199 389 389 ILE ILE B . n 
B 1 200 LEU 200 390 390 LEU LEU B . n 
B 1 201 ASN 201 391 391 ASN ASN B . n 
B 1 202 GLU 202 392 392 GLU GLU B . n 
B 1 203 PRO 203 393 393 PRO PRO B . n 
B 1 204 LEU 204 394 394 LEU LEU B . n 
B 1 205 GLY 205 395 395 GLY GLY B . n 
B 1 206 THR 206 396 396 THR THR B . n 
B 1 207 ASP 207 397 397 ASP ASP B . n 
B 1 208 ILE 208 398 398 ILE ILE B . n 
B 1 209 ILE 209 399 399 ILE ILE B . n 
B 1 210 SER 210 400 400 SER SER B . n 
B 1 211 PRO 211 401 401 PRO PRO B . n 
B 1 212 PRO 212 402 402 PRO PRO B . n 
B 1 213 VAL 213 403 403 VAL VAL B . n 
B 1 214 CYS 214 404 404 CYS CYS B . n 
B 1 215 GLY 215 405 405 GLY GLY B . n 
B 1 216 ASN 216 406 406 ASN ASN B . n 
B 1 217 GLU 217 407 407 GLU GLU B . n 
B 1 218 LEU 218 408 408 LEU LEU B . n 
B 1 219 LEU 219 409 409 LEU LEU B . n 
B 1 220 GLU 220 410 410 GLU GLU B . n 
B 1 221 VAL 221 411 411 VAL VAL B . n 
B 1 222 GLY 222 412 412 GLY GLY B . n 
B 1 223 GLU 223 413 413 GLU GLU B . n 
B 1 224 GLU 224 414 414 GLU GLU B . n 
B 1 225 CYS 225 415 415 CYS CYS B . n 
B 1 226 ASP 226 416 416 ASP ASP B . n 
B 1 227 CYS 227 417 417 CYS CYS B . n 
B 1 228 GLY 228 418 418 GLY GLY B . n 
B 1 229 THR 229 419 419 THR THR B . n 
B 1 230 PRO 230 420 420 PRO PRO B . n 
B 1 231 GLU 231 421 421 GLU GLU B . n 
B 1 232 ASN 232 422 422 ASN ASN B . n 
B 1 233 CYS 233 423 423 CYS CYS B . n 
B 1 234 GLN 234 424 424 GLN GLN B . n 
B 1 235 ASN 235 425 425 ASN ASN B . n 
B 1 236 GLU 236 426 426 GLU GLU B . n 
B 1 237 CYS 237 427 427 CYS CYS B . n 
B 1 238 CYS 238 428 428 CYS CYS B . n 
B 1 239 ASP 239 429 429 ASP ASP B . n 
B 1 240 ALA 240 430 430 ALA ALA B . n 
B 1 241 ALA 241 431 431 ALA ALA B . n 
B 1 242 THR 242 432 432 THR THR B . n 
B 1 243 CYS 243 433 433 CYS CYS B . n 
B 1 244 LYS 244 434 434 LYS LYS B . n 
B 1 245 LEU 245 435 435 LEU LEU B . n 
B 1 246 LYS 246 436 436 LYS LYS B . n 
B 1 247 SER 247 437 437 SER SER B . n 
B 1 248 GLY 248 438 438 GLY GLY B . n 
B 1 249 SER 249 439 439 SER SER B . n 
B 1 250 GLN 250 440 440 GLN GLN B . n 
B 1 251 CYS 251 441 441 CYS CYS B . n 
B 1 252 GLY 252 442 442 GLY GLY B . n 
B 1 253 HIS 253 443 443 HIS HIS B . n 
B 1 254 GLY 254 444 444 GLY GLY B . n 
B 1 255 ASP 255 445 445 ASP ASP B . n 
B 1 256 CYS 256 446 446 CYS CYS B . n 
B 1 257 CYS 257 447 447 CYS CYS B . n 
B 1 258 GLU 258 448 448 GLU GLU B . n 
B 1 259 GLN 259 449 449 GLN GLN B . n 
B 1 260 CYS 260 450 450 CYS CYS B . n 
B 1 261 LYS 261 451 451 LYS LYS B . n 
B 1 262 PHE 262 452 452 PHE PHE B . n 
B 1 263 SER 263 453 453 SER SER B . n 
B 1 264 LYS 264 454 454 LYS LYS B . n 
B 1 265 SER 265 455 455 SER SER B . n 
B 1 266 GLY 266 456 456 GLY GLY B . n 
B 1 267 THR 267 457 457 THR THR B . n 
B 1 268 GLU 268 458 458 GLU GLU B . n 
B 1 269 CYS 269 459 459 CYS CYS B . n 
B 1 270 ARG 270 460 460 ARG ARG B . n 
B 1 271 ALA 271 461 461 ALA ALA B . n 
B 1 272 SER 272 462 462 SER SER B . n 
B 1 273 MET 273 463 463 MET MET B . n 
B 1 274 SER 274 464 464 SER SER B . n 
B 1 275 GLU 275 465 465 GLU GLU B . n 
B 1 276 CYS 276 466 466 CYS CYS B . n 
B 1 277 ASP 277 467 467 ASP ASP B . n 
B 1 278 PRO 278 468 468 PRO PRO B . n 
B 1 279 ALA 279 469 469 ALA ALA B . n 
B 1 280 GLU 280 470 470 GLU GLU B . n 
B 1 281 HIS 281 471 471 HIS HIS B . n 
B 1 282 CYS 282 472 472 CYS CYS B . n 
B 1 283 THR 283 473 473 THR THR B . n 
B 1 284 GLY 284 474 474 GLY GLY B . n 
B 1 285 GLN 285 475 475 GLN GLN B . n 
B 1 286 SER 286 476 476 SER SER B . n 
B 1 287 SER 287 477 477 SER SER B . n 
B 1 288 GLU 288 478 478 GLU GLU B . n 
B 1 289 CYS 289 479 479 CYS CYS B . n 
B 1 290 PRO 290 480 480 PRO PRO B . n 
B 1 291 ALA 291 481 481 ALA ALA B . n 
B 1 292 ASP 292 482 482 ASP ASP B . n 
B 1 293 VAL 293 483 483 VAL VAL B . n 
B 1 294 PHE 294 484 484 PHE PHE B . n 
B 1 295 HIS 295 485 485 HIS HIS B . n 
B 1 296 LYS 296 486 486 LYS LYS B . n 
B 1 297 ASN 297 487 487 ASN ASN B . n 
B 1 298 GLY 298 488 488 GLY GLY B . n 
B 1 299 GLN 299 489 489 GLN GLN B . n 
B 1 300 PRO 300 490 490 PRO PRO B . n 
B 1 301 CYS 301 491 491 CYS CYS B . n 
B 1 302 LEU 302 492 492 LEU LEU B . n 
B 1 303 ASP 303 493 493 ASP ASP B . n 
B 1 304 ASN 304 494 494 ASN ASN B . n 
B 1 305 TYR 305 495 495 TYR TYR B . n 
B 1 306 GLY 306 496 496 GLY GLY B . n 
B 1 307 TYR 307 497 497 TYR TYR B . n 
B 1 308 CYS 308 498 498 CYS CYS B . n 
B 1 309 TYR 309 499 499 TYR TYR B . n 
B 1 310 ASN 310 500 500 ASN ASN B . n 
B 1 311 GLY 311 501 501 GLY GLY B . n 
B 1 312 ASN 312 502 502 ASN ASN B . n 
B 1 313 CYS 313 503 503 CYS CYS B . n 
B 1 314 PRO 314 504 504 PRO PRO B . n 
B 1 315 ILE 315 505 505 ILE ILE B . n 
B 1 316 MET 316 506 506 MET MET B . n 
B 1 317 TYR 317 507 507 TYR TYR B . n 
B 1 318 HIS 318 508 508 HIS HIS B . n 
B 1 319 GLN 319 509 509 GLN GLN B . n 
B 1 320 CYS 320 510 510 CYS CYS B . n 
B 1 321 TYR 321 511 511 TYR TYR B . n 
B 1 322 ASP 322 512 512 ASP ASP B . n 
B 1 323 LEU 323 513 513 LEU LEU B . n 
B 1 324 PHE 324 514 514 PHE PHE B . n 
B 1 325 GLY 325 515 515 GLY GLY B . n 
B 1 326 ALA 326 516 516 ALA ALA B . n 
B 1 327 ASP 327 517 517 ASP ASP B . n 
B 1 328 VAL 328 518 518 VAL VAL B . n 
B 1 329 TYR 329 519 519 TYR TYR B . n 
B 1 330 GLU 330 520 520 GLU GLU B . n 
B 1 331 ALA 331 521 521 ALA ALA B . n 
B 1 332 GLU 332 522 522 GLU GLU B . n 
B 1 333 ASP 333 523 523 ASP ASP B . n 
B 1 334 SER 334 524 524 SER SER B . n 
B 1 335 CYS 335 525 525 CYS CYS B . n 
B 1 336 PHE 336 526 526 PHE PHE B . n 
B 1 337 GLU 337 527 527 GLU GLU B . n 
B 1 338 ARG 338 528 528 ARG ARG B . n 
B 1 339 ASN 339 529 529 ASN ASN B . n 
B 1 340 GLN 340 530 530 GLN GLN B . n 
B 1 341 LYS 341 531 531 LYS LYS B . n 
B 1 342 GLY 342 532 532 GLY GLY B . n 
B 1 343 ASN 343 533 533 ASN ASN B . n 
B 1 344 TYR 344 534 534 TYR TYR B . n 
B 1 345 TYR 345 535 535 TYR TYR B . n 
B 1 346 GLY 346 536 536 GLY GLY B . n 
B 1 347 TYR 347 537 537 TYR TYR B . n 
B 1 348 CYS 348 538 538 CYS CYS B . n 
B 1 349 ARG 349 539 539 ARG ARG B . n 
B 1 350 LYS 350 540 540 LYS LYS B . n 
B 1 351 GLU 351 541 541 GLU GLU B . n 
B 1 352 ASN 352 542 542 ASN ASN B . n 
B 1 353 GLY 353 543 543 GLY GLY B . n 
B 1 354 ASN 354 544 544 ASN ASN B . n 
B 1 355 LYS 355 545 545 LYS LYS B . n 
B 1 356 ILE 356 546 546 ILE ILE B . n 
B 1 357 PRO 357 547 547 PRO PRO B . n 
B 1 358 CYS 358 548 548 CYS CYS B . n 
B 1 359 ALA 359 549 549 ALA ALA B . n 
B 1 360 PRO 360 550 550 PRO PRO B . n 
B 1 361 GLU 361 551 551 GLU GLU B . n 
B 1 362 ASP 362 552 552 ASP ASP B . n 
B 1 363 VAL 363 553 553 VAL VAL B . n 
B 1 364 LYS 364 554 554 LYS LYS B . n 
B 1 365 CYS 365 555 555 CYS CYS B . n 
B 1 366 GLY 366 556 556 GLY GLY B . n 
B 1 367 ARG 367 557 557 ARG ARG B . n 
B 1 368 LEU 368 558 558 LEU LEU B . n 
B 1 369 TYR 369 559 559 TYR TYR B . n 
B 1 370 CYS 370 560 560 CYS CYS B . n 
B 1 371 LYS 371 561 561 LYS LYS B . n 
B 1 372 ASP 372 562 562 ASP ASP B . n 
B 1 373 ASN 373 563 563 ASN ASN B . n 
B 1 374 SER 374 564 564 SER SER B . n 
B 1 375 PRO 375 565 565 PRO PRO B . n 
B 1 376 GLY 376 566 566 GLY GLY B . n 
B 1 377 GLN 377 567 567 GLN GLN B . n 
B 1 378 ASN 378 568 568 ASN ASN B . n 
B 1 379 ASN 379 569 569 ASN ASN B . n 
B 1 380 PRO 380 570 570 PRO PRO B . n 
B 1 381 CYS 381 571 571 CYS CYS B . n 
B 1 382 LYS 382 572 572 LYS LYS B . n 
B 1 383 MET 383 573 573 MET MET B . n 
B 1 384 PHE 384 574 574 PHE PHE B . n 
B 1 385 TYR 385 575 575 TYR TYR B . n 
B 1 386 SER 386 576 576 SER SER B . n 
B 1 387 ASN 387 577 577 ASN ASN B . n 
B 1 388 GLU 388 578 578 GLU GLU B . n 
B 1 389 ASP 389 579 579 ASP ASP B . n 
B 1 390 GLU 390 580 580 GLU GLU B . n 
B 1 391 HIS 391 581 581 HIS HIS B . n 
B 1 392 LYS 392 582 582 LYS LYS B . n 
B 1 393 GLY 393 583 583 GLY GLY B . n 
B 1 394 MET 394 584 584 MET MET B . n 
B 1 395 VAL 395 585 585 VAL VAL B . n 
B 1 396 LEU 396 586 586 LEU LEU B . n 
B 1 397 PRO 397 587 587 PRO PRO B . n 
B 1 398 GLY 398 588 588 GLY GLY B . n 
B 1 399 THR 399 589 589 THR THR B . n 
B 1 400 LYS 400 590 590 LYS LYS B . n 
B 1 401 CYS 401 591 591 CYS CYS B . n 
B 1 402 ALA 402 592 592 ALA ALA B . n 
B 1 403 ASP 403 593 593 ASP ASP B . n 
B 1 404 GLY 404 594 594 GLY GLY B . n 
B 1 405 LYS 405 595 595 LYS LYS B . n 
B 1 406 VAL 406 596 596 VAL VAL B . n 
B 1 407 CYS 407 597 597 CYS CYS B . n 
B 1 408 SER 408 598 598 SER SER B . n 
B 1 409 ASN 409 599 599 ASN ASN B . n 
B 1 410 GLY 410 600 600 GLY GLY B . n 
B 1 411 HIS 411 601 601 HIS HIS B . n 
B 1 412 CYS 412 602 602 CYS CYS B . n 
B 1 413 VAL 413 603 603 VAL VAL B . n 
B 1 414 ASP 414 604 604 ASP ASP B . n 
B 1 415 VAL 415 605 605 VAL VAL B . n 
B 1 416 ALA 416 606 606 ALA ALA B . n 
B 1 417 THR 417 607 607 THR THR B . n 
B 1 418 ALA 418 608 608 ALA ALA B . n 
B 1 419 TYR 419 609 609 TYR TYR B . 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 181 A ASN 371 ? ASN 'GLYCOSYLATION SITE' 
2 B ASN 181 B ASN 371 ? 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 ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,J,K,L,M,N,O,CA   
2 1 B,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,DA 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_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   NE2 ? A  HIS 143 ? A HIS 333 ? 1_555 ZN ? L  ZN . ? A ZN 700 ? 1_555 NE2 ? A  HIS 147 ? A HIS 337 ? 1_555 97.0  ? 
2   NE2 ? A  HIS 143 ? A HIS 333 ? 1_555 ZN ? L  ZN . ? A ZN 700 ? 1_555 NE2 ? A  HIS 153 ? A HIS 343 ? 1_555 100.5 ? 
3   NE2 ? A  HIS 147 ? A HIS 337 ? 1_555 ZN ? L  ZN . ? A ZN 700 ? 1_555 NE2 ? A  HIS 153 ? A HIS 343 ? 1_555 106.2 ? 
4   NE2 ? A  HIS 143 ? A HIS 333 ? 1_555 ZN ? L  ZN . ? A ZN 700 ? 1_555 O   ? CA HOH .   ? A HOH 153 ? 1_555 111.7 ? 
5   NE2 ? A  HIS 147 ? A HIS 337 ? 1_555 ZN ? L  ZN . ? A ZN 700 ? 1_555 O   ? CA HOH .   ? A HOH 153 ? 1_555 108.6 ? 
6   NE2 ? A  HIS 153 ? A HIS 343 ? 1_555 ZN ? L  ZN . ? A ZN 700 ? 1_555 O   ? CA HOH .   ? A HOH 153 ? 1_555 128.2 ? 
7   NE2 ? B  HIS 143 ? B HIS 333 ? 1_555 ZN ? Y  ZN . ? B ZN 700 ? 1_555 NE2 ? B  HIS 147 ? B HIS 337 ? 1_555 95.1  ? 
8   NE2 ? B  HIS 143 ? B HIS 333 ? 1_555 ZN ? Y  ZN . ? B ZN 700 ? 1_555 NE2 ? B  HIS 153 ? B HIS 343 ? 1_555 104.8 ? 
9   NE2 ? B  HIS 147 ? B HIS 337 ? 1_555 ZN ? Y  ZN . ? B ZN 700 ? 1_555 NE2 ? B  HIS 153 ? B HIS 343 ? 1_555 94.8  ? 
10  NE2 ? B  HIS 143 ? B HIS 333 ? 1_555 ZN ? Y  ZN . ? B ZN 700 ? 1_555 O   ? DA HOH .   ? B HOH 155 ? 1_555 121.6 ? 
11  NE2 ? B  HIS 147 ? B HIS 337 ? 1_555 ZN ? Y  ZN . ? B ZN 700 ? 1_555 O   ? DA HOH .   ? B HOH 155 ? 1_555 115.8 ? 
12  NE2 ? B  HIS 153 ? B HIS 343 ? 1_555 ZN ? Y  ZN . ? B ZN 700 ? 1_555 O   ? DA HOH .   ? B HOH 155 ? 1_555 119.3 ? 
13  OE1 ? A  GLU 11  ? A GLU 201 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 OD1 ? A  ASP 95  ? A ASP 285 ? 1_555 87.0  ? 
14  OE1 ? A  GLU 11  ? A GLU 201 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 OD2 ? A  ASP 95  ? A ASP 285 ? 1_555 79.9  ? 
15  OD1 ? A  ASP 95  ? A ASP 285 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 OD2 ? A  ASP 95  ? A ASP 285 ? 1_555 51.4  ? 
16  OE1 ? A  GLU 11  ? A GLU 201 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? A  CYS 198 ? A CYS 388 ? 1_555 158.9 ? 
17  OD1 ? A  ASP 95  ? A ASP 285 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? A  CYS 198 ? A CYS 388 ? 1_555 84.2  ? 
18  OD2 ? A  ASP 95  ? A ASP 285 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? A  CYS 198 ? A CYS 388 ? 1_555 79.6  ? 
19  OE1 ? A  GLU 11  ? A GLU 201 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 ND2 ? A  ASN 201 ? A ASN 391 ? 1_555 121.6 ? 
20  OD1 ? A  ASP 95  ? A ASP 285 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 ND2 ? A  ASN 201 ? A ASN 391 ? 1_555 148.3 ? 
21  OD2 ? A  ASP 95  ? A ASP 285 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 ND2 ? A  ASN 201 ? A ASN 391 ? 1_555 139.8 ? 
22  O   ? A  CYS 198 ? A CYS 388 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 ND2 ? A  ASN 201 ? A ASN 391 ? 1_555 72.9  ? 
23  OE1 ? A  GLU 11  ? A GLU 201 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? CA HOH .   ? A HOH 86  ? 1_555 88.1  ? 
24  OD1 ? A  ASP 95  ? A ASP 285 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? CA HOH .   ? A HOH 86  ? 1_555 130.8 ? 
25  OD2 ? A  ASP 95  ? A ASP 285 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? CA HOH .   ? A HOH 86  ? 1_555 79.5  ? 
26  O   ? A  CYS 198 ? A CYS 388 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? CA HOH .   ? A HOH 86  ? 1_555 83.2  ? 
27  ND2 ? A  ASN 201 ? A ASN 391 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? CA HOH .   ? A HOH 86  ? 1_555 68.8  ? 
28  OE1 ? A  GLU 11  ? A GLU 201 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? CA HOH .   ? A HOH 4   ? 1_555 97.3  ? 
29  OD1 ? A  ASP 95  ? A ASP 285 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? CA HOH .   ? A HOH 4   ? 1_555 80.1  ? 
30  OD2 ? A  ASP 95  ? A ASP 285 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? CA HOH .   ? A HOH 4   ? 1_555 131.4 ? 
31  O   ? A  CYS 198 ? A CYS 388 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? CA HOH .   ? A HOH 4   ? 1_555 100.0 ? 
32  ND2 ? A  ASN 201 ? A ASN 391 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? CA HOH .   ? A HOH 4   ? 1_555 82.7  ? 
33  O   ? CA HOH .   ? A HOH 86  ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 O   ? CA HOH .   ? A HOH 4   ? 1_555 149.1 ? 
34  OE1 ? A  GLU 11  ? A GLU 201 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 OD1 ? A  ASN 201 ? A ASN 391 ? 1_555 73.0  ? 
35  OD1 ? A  ASP 95  ? A ASP 285 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 OD1 ? A  ASN 201 ? A ASN 391 ? 1_555 144.0 ? 
36  OD2 ? A  ASP 95  ? A ASP 285 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 OD1 ? A  ASN 201 ? A ASN 391 ? 1_555 145.9 ? 
37  O   ? A  CYS 198 ? A CYS 388 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 OD1 ? A  ASN 201 ? A ASN 391 ? 1_555 123.7 ? 
38  ND2 ? A  ASN 201 ? A ASN 391 ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 OD1 ? A  ASN 201 ? A ASN 391 ? 1_555 50.9  ? 
39  O   ? CA HOH .   ? A HOH 86  ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 OD1 ? A  ASN 201 ? A ASN 391 ? 1_555 79.3  ? 
40  O   ? CA HOH .   ? A HOH 4   ? 1_555 CA ? M  CA . ? A CA 701 ? 1_555 OD1 ? A  ASN 201 ? A ASN 391 ? 1_555 73.3  ? 
41  O   ? A  VAL 213 ? A VAL 403 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OD1 ? A  ASN 216 ? A ASN 406 ? 1_555 81.8  ? 
42  O   ? A  VAL 213 ? A VAL 403 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OE1 ? A  GLU 220 ? A GLU 410 ? 1_555 78.1  ? 
43  OD1 ? A  ASN 216 ? A ASN 406 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OE1 ? A  GLU 220 ? A GLU 410 ? 1_555 97.4  ? 
44  O   ? A  VAL 213 ? A VAL 403 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 O   ? A  LEU 218 ? A LEU 408 ? 1_555 164.0 ? 
45  OD1 ? A  ASN 216 ? A ASN 406 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 O   ? A  LEU 218 ? A LEU 408 ? 1_555 84.9  ? 
46  OE1 ? A  GLU 220 ? A GLU 410 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 O   ? A  LEU 218 ? A LEU 408 ? 1_555 94.7  ? 
47  O   ? A  VAL 213 ? A VAL 403 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OE1 ? A  GLU 223 ? A GLU 413 ? 1_555 119.3 ? 
48  OD1 ? A  ASN 216 ? A ASN 406 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OE1 ? A  GLU 223 ? A GLU 413 ? 1_555 154.2 ? 
49  OE1 ? A  GLU 220 ? A GLU 410 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OE1 ? A  GLU 223 ? A GLU 413 ? 1_555 101.3 ? 
50  O   ? A  LEU 218 ? A LEU 408 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OE1 ? A  GLU 223 ? A GLU 413 ? 1_555 76.0  ? 
51  O   ? A  VAL 213 ? A VAL 403 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OE2 ? A  GLU 223 ? A GLU 413 ? 1_555 71.5  ? 
52  OD1 ? A  ASN 216 ? A ASN 406 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OE2 ? A  GLU 223 ? A GLU 413 ? 1_555 149.3 ? 
53  OE1 ? A  GLU 220 ? A GLU 410 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OE2 ? A  GLU 223 ? A GLU 413 ? 1_555 91.9  ? 
54  O   ? A  LEU 218 ? A LEU 408 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OE2 ? A  GLU 223 ? A GLU 413 ? 1_555 123.5 ? 
55  OE1 ? A  GLU 223 ? A GLU 413 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OE2 ? A  GLU 223 ? A GLU 413 ? 1_555 47.7  ? 
56  O   ? A  VAL 213 ? A VAL 403 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OD2 ? A  ASP 226 ? A ASP 416 ? 1_555 83.3  ? 
57  OD1 ? A  ASN 216 ? A ASN 406 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OD2 ? A  ASP 226 ? A ASP 416 ? 1_555 82.6  ? 
58  OE1 ? A  GLU 220 ? A GLU 410 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OD2 ? A  ASP 226 ? A ASP 416 ? 1_555 161.2 ? 
59  O   ? A  LEU 218 ? A LEU 408 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OD2 ? A  ASP 226 ? A ASP 416 ? 1_555 104.0 ? 
60  OE1 ? A  GLU 223 ? A GLU 413 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OD2 ? A  ASP 226 ? A ASP 416 ? 1_555 85.2  ? 
61  OE2 ? A  GLU 223 ? A GLU 413 ? 1_555 CA ? N  CA . ? A CA 702 ? 1_555 OD2 ? A  ASP 226 ? A ASP 416 ? 1_555 79.4  ? 
62  OE1 ? A  GLU 280 ? A GLU 470 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 O   ? A  PRO 278 ? A PRO 468 ? 1_555 80.2  ? 
63  OE1 ? A  GLU 280 ? A GLU 470 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 OD2 ? A  ASP 292 ? A ASP 482 ? 1_555 94.4  ? 
64  O   ? A  PRO 278 ? A PRO 468 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 OD2 ? A  ASP 292 ? A ASP 482 ? 1_555 170.9 ? 
65  OE1 ? A  GLU 280 ? A GLU 470 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 OE2 ? A  GLU 280 ? A GLU 470 ? 1_555 51.8  ? 
66  O   ? A  PRO 278 ? A PRO 468 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 OE2 ? A  GLU 280 ? A GLU 470 ? 1_555 90.4  ? 
67  OD2 ? A  ASP 292 ? A ASP 482 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 OE2 ? A  GLU 280 ? A GLU 470 ? 1_555 92.0  ? 
68  OE1 ? A  GLU 280 ? A GLU 470 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 O   ? A  VAL 293 ? A VAL 483 ? 1_555 89.0  ? 
69  O   ? A  PRO 278 ? A PRO 468 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 O   ? A  VAL 293 ? A VAL 483 ? 1_555 87.3  ? 
70  OD2 ? A  ASP 292 ? A ASP 482 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 O   ? A  VAL 293 ? A VAL 483 ? 1_555 85.3  ? 
71  OE2 ? A  GLU 280 ? A GLU 470 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 O   ? A  VAL 293 ? A VAL 483 ? 1_555 140.5 ? 
72  OE1 ? A  GLU 280 ? A GLU 470 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 OD2 ? A  ASP 277 ? A ASP 467 ? 1_555 162.9 ? 
73  O   ? A  PRO 278 ? A PRO 468 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 OD2 ? A  ASP 277 ? A ASP 467 ? 1_555 89.9  ? 
74  OD2 ? A  ASP 292 ? A ASP 482 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 OD2 ? A  ASP 277 ? A ASP 467 ? 1_555 93.5  ? 
75  OE2 ? A  GLU 280 ? A GLU 470 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 OD2 ? A  ASP 277 ? A ASP 467 ? 1_555 142.9 ? 
76  O   ? A  VAL 293 ? A VAL 483 ? 1_555 CA ? O  CA . ? A CA 703 ? 1_555 OD2 ? A  ASP 277 ? A ASP 467 ? 1_555 76.5  ? 
77  OD2 ? B  ASP 95  ? B ASP 285 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 OD1 ? B  ASN 201 ? B ASN 391 ? 1_555 141.1 ? 
78  OD2 ? B  ASP 95  ? B ASP 285 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 OD1 ? B  ASP 95  ? B ASP 285 ? 1_555 51.2  ? 
79  OD1 ? B  ASN 201 ? B ASN 391 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 OD1 ? B  ASP 95  ? B ASP 285 ? 1_555 158.4 ? 
80  OD2 ? B  ASP 95  ? B ASP 285 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 OE1 ? B  GLU 11  ? B GLU 201 ? 1_555 93.6  ? 
81  OD1 ? B  ASN 201 ? B ASN 391 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 OE1 ? B  GLU 11  ? B GLU 201 ? 1_555 74.1  ? 
82  OD1 ? B  ASP 95  ? B ASP 285 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 OE1 ? B  GLU 11  ? B GLU 201 ? 1_555 88.8  ? 
83  OD2 ? B  ASP 95  ? B ASP 285 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 O   ? B  CYS 198 ? B CYS 388 ? 1_555 74.1  ? 
84  OD1 ? B  ASN 201 ? B ASN 391 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 O   ? B  CYS 198 ? B CYS 388 ? 1_555 118.5 ? 
85  OD1 ? B  ASP 95  ? B ASP 285 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 O   ? B  CYS 198 ? B CYS 388 ? 1_555 79.7  ? 
86  OE1 ? B  GLU 11  ? B GLU 201 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 O   ? B  CYS 198 ? B CYS 388 ? 1_555 166.8 ? 
87  OD2 ? B  ASP 95  ? B ASP 285 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 ND2 ? B  ASN 201 ? B ASN 391 ? 1_555 163.2 ? 
88  OD1 ? B  ASN 201 ? B ASN 391 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 ND2 ? B  ASN 201 ? B ASN 391 ? 1_555 47.1  ? 
89  OD1 ? B  ASP 95  ? B ASP 285 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 ND2 ? B  ASN 201 ? B ASN 391 ? 1_555 128.2 ? 
90  OE1 ? B  GLU 11  ? B GLU 201 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 ND2 ? B  ASN 201 ? B ASN 391 ? 1_555 103.2 ? 
91  O   ? B  CYS 198 ? B CYS 388 ? 1_555 CA ? Z  CA . ? B CA 711 ? 1_555 ND2 ? B  ASN 201 ? B ASN 391 ? 1_555 89.1  ? 
92  O   ? B  LEU 218 ? B LEU 408 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OD2 ? B  ASP 226 ? B ASP 416 ? 1_555 95.4  ? 
93  O   ? B  LEU 218 ? B LEU 408 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OD1 ? B  ASN 216 ? B ASN 406 ? 1_555 88.1  ? 
94  OD2 ? B  ASP 226 ? B ASP 416 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OD1 ? B  ASN 216 ? B ASN 406 ? 1_555 80.8  ? 
95  O   ? B  LEU 218 ? B LEU 408 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 O   ? B  VAL 213 ? B VAL 403 ? 1_555 159.6 ? 
96  OD2 ? B  ASP 226 ? B ASP 416 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 O   ? B  VAL 213 ? B VAL 403 ? 1_555 84.5  ? 
97  OD1 ? B  ASN 216 ? B ASN 406 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 O   ? B  VAL 213 ? B VAL 403 ? 1_555 71.7  ? 
98  O   ? B  LEU 218 ? B LEU 408 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE1 ? B  GLU 220 ? B GLU 410 ? 1_555 97.3  ? 
99  OD2 ? B  ASP 226 ? B ASP 416 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE1 ? B  GLU 220 ? B GLU 410 ? 1_555 167.1 ? 
100 OD1 ? B  ASN 216 ? B ASN 406 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE1 ? B  GLU 220 ? B GLU 410 ? 1_555 97.5  ? 
101 O   ? B  VAL 213 ? B VAL 403 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE1 ? B  GLU 220 ? B GLU 410 ? 1_555 82.9  ? 
102 O   ? B  LEU 218 ? B LEU 408 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE1 ? B  GLU 223 ? B GLU 413 ? 1_555 72.7  ? 
103 OD2 ? B  ASP 226 ? B ASP 416 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE1 ? B  GLU 223 ? B GLU 413 ? 1_555 92.5  ? 
104 OD1 ? B  ASN 216 ? B ASN 406 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE1 ? B  GLU 223 ? B GLU 413 ? 1_555 159.1 ? 
105 O   ? B  VAL 213 ? B VAL 403 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE1 ? B  GLU 223 ? B GLU 413 ? 1_555 127.7 ? 
106 OE1 ? B  GLU 220 ? B GLU 410 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE1 ? B  GLU 223 ? B GLU 413 ? 1_555 93.3  ? 
107 O   ? B  LEU 218 ? B LEU 408 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE2 ? B  GLU 223 ? B GLU 413 ? 1_555 120.8 ? 
108 OD2 ? B  ASP 226 ? B ASP 416 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE2 ? B  GLU 223 ? B GLU 413 ? 1_555 91.7  ? 
109 OD1 ? B  ASN 216 ? B ASN 406 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE2 ? B  GLU 223 ? B GLU 413 ? 1_555 150.8 ? 
110 O   ? B  VAL 213 ? B VAL 403 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE2 ? B  GLU 223 ? B GLU 413 ? 1_555 79.6  ? 
111 OE1 ? B  GLU 220 ? B GLU 410 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE2 ? B  GLU 223 ? B GLU 413 ? 1_555 83.6  ? 
112 OE1 ? B  GLU 223 ? B GLU 413 ? 1_555 CA ? AA CA . ? B CA 712 ? 1_555 OE2 ? B  GLU 223 ? B GLU 413 ? 1_555 48.3  ? 
113 O   ? B  VAL 293 ? B VAL 483 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 OE2 ? B  GLU 280 ? B GLU 470 ? 1_555 139.4 ? 
114 O   ? B  VAL 293 ? B VAL 483 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 O   ? B  PRO 278 ? B PRO 468 ? 1_555 91.4  ? 
115 OE2 ? B  GLU 280 ? B GLU 470 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 O   ? B  PRO 278 ? B PRO 468 ? 1_555 84.3  ? 
116 O   ? B  VAL 293 ? B VAL 483 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 OD1 ? B  ASP 292 ? B ASP 482 ? 1_555 92.5  ? 
117 OE2 ? B  GLU 280 ? B GLU 470 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 OD1 ? B  ASP 292 ? B ASP 482 ? 1_555 82.3  ? 
118 O   ? B  PRO 278 ? B PRO 468 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 OD1 ? B  ASP 292 ? B ASP 482 ? 1_555 163.6 ? 
119 O   ? B  VAL 293 ? B VAL 483 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 OE1 ? B  GLU 280 ? B GLU 470 ? 1_555 91.9  ? 
120 OE2 ? B  GLU 280 ? B GLU 470 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 OE1 ? B  GLU 280 ? B GLU 470 ? 1_555 47.7  ? 
121 O   ? B  PRO 278 ? B PRO 468 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 OE1 ? B  GLU 280 ? B GLU 470 ? 1_555 89.0  ? 
122 OD1 ? B  ASP 292 ? B ASP 482 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 OE1 ? B  GLU 280 ? B GLU 470 ? 1_555 75.0  ? 
123 O   ? B  VAL 293 ? B VAL 483 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 OD2 ? B  ASP 277 ? B ASP 467 ? 1_555 77.4  ? 
124 OE2 ? B  GLU 280 ? B GLU 470 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 OD2 ? B  ASP 277 ? B ASP 467 ? 1_555 143.3 ? 
125 O   ? B  PRO 278 ? B PRO 468 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 OD2 ? B  ASP 277 ? B ASP 467 ? 1_555 96.8  ? 
126 OD1 ? B  ASP 292 ? B ASP 482 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 OD2 ? B  ASP 277 ? B ASP 467 ? 1_555 99.6  ? 
127 OE1 ? B  GLU 280 ? B GLU 470 ? 1_555 CA ? BA CA . ? B CA 713 ? 1_555 OD2 ? B  ASP 277 ? B ASP 467 ? 1_555 167.9 ? 
# 
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 2007-07-10 
2 'Structure model' 1 1 2008-04-30 
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 
ADSC     'data collection' Quantum   ? 1 
MOLREP   phasing           'in CCP4' ? 2 
CNS      refinement        1.0       ? 3 
HKL-2000 'data reduction'  .         ? 4 
HKL-2000 'data scaling'    .         ? 5 
# 
_pdbx_database_remark.id     999 
_pdbx_database_remark.text   
;SEQUENCE  
There is difference between the SEQRES and 
the sequence database.
The depositors believe it is a variant.
;
# 
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 ASP A 277 ? ? -132.13 -69.86  
2  1 ARG A 297 ? ? 65.55   -38.09  
3  1 CYS A 308 ? ? 88.41   -20.53  
4  1 SER A 313 ? ? -90.67  50.69   
5  1 LEU A 339 ? ? -84.94  32.17   
6  1 TYR A 347 ? ? -85.40  39.00   
7  1 CYS A 350 ? ? -152.11 31.97   
8  1 ASP A 352 ? ? -80.96  49.27   
9  1 MET A 357 ? ? -94.63  38.62   
10 1 ASN A 383 ? ? -69.22  -73.71  
11 1 PRO A 386 ? ? -64.01  79.59   
12 1 ASP A 429 ? ? -101.67 79.00   
13 1 ALA A 430 ? ? -25.70  -56.01  
14 1 ASP A 517 ? ? 58.47   18.19   
15 1 ASN A 533 ? ? -85.00  -156.67 
16 1 ASN A 542 ? ? 49.47   19.00   
17 1 ASN A 563 ? ? -93.66  31.78   
18 1 ASN A 568 ? ? 86.10   -33.66  
19 1 CYS A 571 ? ? -117.20 53.45   
20 1 ASN A 577 ? ? -61.40  0.87    
21 1 ASP A 579 ? ? -165.66 86.22   
22 1 ASN B 253 ? ? -90.85  -72.15  
23 1 ASP B 277 ? ? -160.80 -80.28  
24 1 ARG B 297 ? ? 64.98   -35.42  
25 1 CYS B 308 ? ? 82.44   -11.85  
26 1 CYS B 350 ? ? -149.91 32.27   
27 1 ASP B 352 ? ? -83.56  44.46   
28 1 ASN B 383 ? ? -62.90  -71.47  
29 1 GLU B 387 ? ? -29.63  -49.76  
30 1 ALA B 430 ? ? -33.70  -32.06  
31 1 ALA B 481 ? ? -41.21  150.92  
32 1 GLN B 489 ? ? -57.97  107.12  
33 1 ASN B 500 ? ? 39.72   45.33   
34 1 CYS B 503 ? ? -118.92 77.99   
35 1 ASN B 529 ? ? -56.14  -3.70   
36 1 ASN B 533 ? ? -90.50  -155.79 
37 1 ASP B 579 ? ? -157.06 89.66   
# 
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 HIS 191 ? A HIS 1 
2 1 Y 1 A GLN 192 ? A GLN 2 
3 1 Y 1 A LYS 193 ? A LYS 3 
4 1 Y 1 A TYR 194 ? A TYR 4 
5 1 Y 1 B HIS 191 ? B HIS 1 
6 1 Y 1 B GLN 192 ? B GLN 2 
7 1 Y 1 B LYS 193 ? B LYS 3 
8 1 Y 1 B TYR 194 ? B TYR 4 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 BETA-D-MANNOSE         BMA 
4 ALPHA-D-MANNOSE        MAN 
5 ALPHA-L-FUCOSE         FUC 
6 'ZINC ION'             ZN  
7 'CALCIUM ION'          CA  
8 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 
C  2 NAG 1  801 801 NAG NAG A . 
D  2 NAG 2  802 802 NAG NAG A . 
E  3 BMA 3  803 803 BMA BMA A . 
F  2 NAG 4  804 804 NAG NAG A . 
G  4 MAN 5  805 805 MAN MAN A . 
H  2 NAG 6  806 806 NAG NAG A . 
I  4 MAN 7  807 807 MAN MAN A . 
J  2 NAG 8  808 808 NAG NAG A . 
K  5 FUC 9  809 809 FUC FUC A . 
L  6 ZN  1  700 700 ZN  ZN  A . 
M  7 CA  1  701 701 CA  CA  A . 
N  7 CA  1  702 702 CA  CA  A . 
O  7 CA  1  703 703 CA  CA  A . 
P  2 NAG 1  801 801 NAG NAG B . 
Q  2 NAG 2  802 802 NAG NAG B . 
R  3 BMA 3  803 803 BMA BMA B . 
S  2 NAG 4  804 804 NAG NAG B . 
T  4 MAN 5  805 805 MAN MAN B . 
U  2 NAG 6  806 806 NAG NAG B . 
V  4 MAN 7  807 807 MAN MAN B . 
W  2 NAG 8  808 808 NAG NAG B . 
X  5 FUC 9  809 809 FUC FUC B . 
Y  6 ZN  1  700 700 ZN  ZN  B . 
Z  7 CA  1  711 711 CA  CA  B . 
AA 7 CA  1  712 712 CA  CA  B . 
BA 7 CA  1  713 713 CA  CA  B . 
CA 8 HOH 1  1   1   HOH TIP A . 
CA 8 HOH 2  2   2   HOH TIP A . 
CA 8 HOH 3  3   3   HOH TIP A . 
CA 8 HOH 4  4   4   HOH TIP A . 
CA 8 HOH 5  6   6   HOH TIP A . 
CA 8 HOH 6  7   7   HOH TIP A . 
CA 8 HOH 7  8   8   HOH TIP A . 
CA 8 HOH 8  10  10  HOH TIP A . 
CA 8 HOH 9  13  13  HOH TIP A . 
CA 8 HOH 10 16  16  HOH TIP A . 
CA 8 HOH 11 17  17  HOH TIP A . 
CA 8 HOH 12 19  19  HOH TIP A . 
CA 8 HOH 13 21  21  HOH TIP A . 
CA 8 HOH 14 22  22  HOH TIP A . 
CA 8 HOH 15 26  26  HOH TIP A . 
CA 8 HOH 16 28  28  HOH TIP A . 
CA 8 HOH 17 31  31  HOH TIP A . 
CA 8 HOH 18 33  33  HOH TIP A . 
CA 8 HOH 19 35  35  HOH TIP A . 
CA 8 HOH 20 38  38  HOH TIP A . 
CA 8 HOH 21 39  39  HOH TIP A . 
CA 8 HOH 22 40  40  HOH TIP A . 
CA 8 HOH 23 43  43  HOH TIP A . 
CA 8 HOH 24 45  45  HOH TIP A . 
CA 8 HOH 25 46  46  HOH TIP A . 
CA 8 HOH 26 47  47  HOH TIP A . 
CA 8 HOH 27 49  49  HOH TIP A . 
CA 8 HOH 28 50  50  HOH TIP A . 
CA 8 HOH 29 51  51  HOH TIP A . 
CA 8 HOH 30 54  54  HOH TIP A . 
CA 8 HOH 31 55  55  HOH TIP A . 
CA 8 HOH 32 56  56  HOH TIP A . 
CA 8 HOH 33 60  60  HOH TIP A . 
CA 8 HOH 34 63  63  HOH TIP A . 
CA 8 HOH 35 64  64  HOH TIP A . 
CA 8 HOH 36 67  67  HOH TIP A . 
CA 8 HOH 37 68  68  HOH TIP A . 
CA 8 HOH 38 69  69  HOH TIP A . 
CA 8 HOH 39 72  72  HOH TIP A . 
CA 8 HOH 40 74  74  HOH TIP A . 
CA 8 HOH 41 75  75  HOH TIP A . 
CA 8 HOH 42 76  76  HOH TIP A . 
CA 8 HOH 43 79  79  HOH TIP A . 
CA 8 HOH 44 80  80  HOH TIP A . 
CA 8 HOH 45 82  82  HOH TIP A . 
CA 8 HOH 46 83  83  HOH TIP A . 
CA 8 HOH 47 84  84  HOH TIP A . 
CA 8 HOH 48 86  86  HOH TIP A . 
CA 8 HOH 49 89  89  HOH TIP A . 
CA 8 HOH 50 90  90  HOH TIP A . 
CA 8 HOH 51 91  91  HOH TIP A . 
CA 8 HOH 52 93  93  HOH TIP A . 
CA 8 HOH 53 94  94  HOH TIP A . 
CA 8 HOH 54 95  95  HOH TIP A . 
CA 8 HOH 55 96  96  HOH TIP A . 
CA 8 HOH 56 97  97  HOH TIP A . 
CA 8 HOH 57 98  98  HOH TIP A . 
CA 8 HOH 58 100 100 HOH TIP A . 
CA 8 HOH 59 101 101 HOH TIP A . 
CA 8 HOH 60 102 102 HOH TIP A . 
CA 8 HOH 61 103 103 HOH TIP A . 
CA 8 HOH 62 104 104 HOH TIP A . 
CA 8 HOH 63 106 106 HOH TIP A . 
CA 8 HOH 64 107 107 HOH TIP A . 
CA 8 HOH 65 113 113 HOH TIP A . 
CA 8 HOH 66 116 116 HOH TIP A . 
CA 8 HOH 67 118 118 HOH TIP A . 
CA 8 HOH 68 119 119 HOH TIP A . 
CA 8 HOH 69 120 120 HOH TIP A . 
CA 8 HOH 70 122 122 HOH TIP A . 
CA 8 HOH 71 128 128 HOH TIP A . 
CA 8 HOH 72 131 131 HOH TIP A . 
CA 8 HOH 73 133 133 HOH TIP A . 
CA 8 HOH 74 137 137 HOH TIP A . 
CA 8 HOH 75 139 139 HOH TIP A . 
CA 8 HOH 76 140 140 HOH TIP A . 
CA 8 HOH 77 142 142 HOH TIP A . 
CA 8 HOH 78 145 145 HOH TIP A . 
CA 8 HOH 79 146 146 HOH TIP A . 
CA 8 HOH 80 147 147 HOH TIP A . 
CA 8 HOH 81 150 150 HOH TIP A . 
CA 8 HOH 82 151 151 HOH TIP A . 
CA 8 HOH 83 152 152 HOH TIP A . 
CA 8 HOH 84 153 153 HOH TIP A . 
CA 8 HOH 85 154 154 HOH TIP A . 
DA 8 HOH 1  5   5   HOH TIP B . 
DA 8 HOH 2  9   9   HOH TIP B . 
DA 8 HOH 3  11  11  HOH TIP B . 
DA 8 HOH 4  12  12  HOH TIP B . 
DA 8 HOH 5  14  14  HOH TIP B . 
DA 8 HOH 6  15  15  HOH TIP B . 
DA 8 HOH 7  18  18  HOH TIP B . 
DA 8 HOH 8  20  20  HOH TIP B . 
DA 8 HOH 9  23  23  HOH TIP B . 
DA 8 HOH 10 24  24  HOH TIP B . 
DA 8 HOH 11 27  27  HOH TIP B . 
DA 8 HOH 12 29  29  HOH TIP B . 
DA 8 HOH 13 30  30  HOH TIP B . 
DA 8 HOH 14 34  34  HOH TIP B . 
DA 8 HOH 15 36  36  HOH TIP B . 
DA 8 HOH 16 37  37  HOH TIP B . 
DA 8 HOH 17 41  41  HOH TIP B . 
DA 8 HOH 18 42  42  HOH TIP B . 
DA 8 HOH 19 44  44  HOH TIP B . 
DA 8 HOH 20 48  48  HOH TIP B . 
DA 8 HOH 21 52  52  HOH TIP B . 
DA 8 HOH 22 53  53  HOH TIP B . 
DA 8 HOH 23 57  57  HOH TIP B . 
DA 8 HOH 24 58  58  HOH TIP B . 
DA 8 HOH 25 59  59  HOH TIP B . 
DA 8 HOH 26 61  61  HOH TIP B . 
DA 8 HOH 27 62  62  HOH TIP B . 
DA 8 HOH 28 65  65  HOH TIP B . 
DA 8 HOH 29 66  66  HOH TIP B . 
DA 8 HOH 30 70  70  HOH TIP B . 
DA 8 HOH 31 71  71  HOH TIP B . 
DA 8 HOH 32 73  73  HOH TIP B . 
DA 8 HOH 33 77  77  HOH TIP B . 
DA 8 HOH 34 78  78  HOH TIP B . 
DA 8 HOH 35 81  81  HOH TIP B . 
DA 8 HOH 36 85  85  HOH TIP B . 
DA 8 HOH 37 87  87  HOH TIP B . 
DA 8 HOH 38 88  88  HOH TIP B . 
DA 8 HOH 39 92  92  HOH TIP B . 
DA 8 HOH 40 99  99  HOH TIP B . 
DA 8 HOH 41 105 105 HOH TIP B . 
DA 8 HOH 42 108 108 HOH TIP B . 
DA 8 HOH 43 110 110 HOH TIP B . 
DA 8 HOH 44 111 111 HOH TIP B . 
DA 8 HOH 45 112 112 HOH TIP B . 
DA 8 HOH 46 114 114 HOH TIP B . 
DA 8 HOH 47 115 115 HOH TIP B . 
DA 8 HOH 48 117 117 HOH TIP B . 
DA 8 HOH 49 121 121 HOH TIP B . 
DA 8 HOH 50 123 123 HOH TIP B . 
DA 8 HOH 51 124 124 HOH TIP B . 
DA 8 HOH 52 125 125 HOH TIP B . 
DA 8 HOH 53 126 126 HOH TIP B . 
DA 8 HOH 54 127 127 HOH TIP B . 
DA 8 HOH 55 129 129 HOH TIP B . 
DA 8 HOH 56 130 130 HOH TIP B . 
DA 8 HOH 57 132 132 HOH TIP B . 
DA 8 HOH 58 134 134 HOH TIP B . 
DA 8 HOH 59 135 135 HOH TIP B . 
DA 8 HOH 60 136 136 HOH TIP B . 
DA 8 HOH 61 141 141 HOH TIP B . 
DA 8 HOH 62 143 143 HOH TIP B . 
DA 8 HOH 63 144 144 HOH TIP B . 
DA 8 HOH 64 148 148 HOH TIP B . 
DA 8 HOH 65 149 149 HOH TIP B . 
DA 8 HOH 66 155 155 HOH TIP B . 
# 
