PDB/UniProt Mapping

------------------------------------------------
         PDB             ||      UniProt        
-------------------------||---------------------
PDB  Chn  SeqNo Res ResNo||Accession Res  Number
------------------------------------------------
2e5k A        1 SER 248    Q8TF42    S       248
2e5k A        2 ARG 249    Q8TF42    R       249
2e5k A        3 ASP 250    Q8TF42    D       250
2e5k A        4 ILE 251    Q8TF42    I       251
2e5k A        5 ARG 252    Q8TF42    R       252
2e5k A        6 PHE 253    Q8TF42    F       253
2e5k A        7 ALA 254    Q8TF42    A       254
2e5k A        8 ASN 255    Q8TF42    N       255
2e5k A        9 HIS 256    Q8TF42    H       256
2e5k A       10 GLU 257    Q8TF42    E       257
2e5k A       11 THR 258    Q8TF42    T       258
2e5k A       12 LEU 259    Q8TF42    L       259
2e5k A       13 GLN 260    Q8TF42    Q       260
2e5k A       14 VAL 261    Q8TF42    V       261
2e5k A       15 ILE 262    Q8TF42    I       262
2e5k A       16 TYR 263    Q8TF42    Y       263
2e5k A       17 PRO 264    Q8TF42    P       264
2e5k A       18 TYR 265    Q8TF42    Y       265
2e5k A       19 THR 266    Q8TF42    T       266
2e5k A       20 PRO 267    Q8TF42    P       267
2e5k A       21 GLN 268    Q8TF42    Q       268
2e5k A       22 ASN 269    Q8TF42    N       269
2e5k A       23 ASP 270    Q8TF42    D       270
2e5k A       24 ASP 271    Q8TF42    D       271
2e5k A       25 GLU 272    Q8TF42    E       272
2e5k A       26 LEU 273    Q8TF42    L       273
2e5k A       27 GLU 274    Q8TF42    E       274
2e5k A       28 LEU 275    Q8TF42    L       275
2e5k A       29 VAL 276    Q8TF42    V       276
2e5k A       30 PRO 277    Q8TF42    P       277
2e5k A       31 GLY 278    Q8TF42    G       278
2e5k A       32 ASP 279    Q8TF42    D       279
2e5k A       33 PHE 280    Q8TF42    F       280
2e5k A       34 ILE 281    Q8TF42    I       281
2e5k A       35 PHE 282    Q8TF42    F       282
2e5k A       36 MET 283    Q8TF42    M       283
2e5k A       37 SER 284    Q8TF42    S       284
2e5k A       38 PRO 285    Q8TF42    P       285
2e5k A       39 MET 286    Q8TF42    M       286
2e5k A       40 GLU 287    Q8TF42    E       287
2e5k A       41 GLN 288    Q8TF42    Q       288
2e5k A       42 THR 289    Q8TF42    T       289
2e5k A       43 SER 290    Q8TF42    S       290
2e5k A       44 THR 291    Q8TF42    T       291
2e5k A       45 SER 292    Q8TF42    S       292
2e5k A       46 GLU 293    Q8TF42    E       293
2e5k A       47 GLY 294    Q8TF42    G       294
2e5k A       48 TRP 295    Q8TF42    W       295
2e5k A       49 ILE 296    Q8TF42    I       296
2e5k A       50 TYR 297    Q8TF42    Y       297
2e5k A       51 GLY 298    Q8TF42    G       298
2e5k A       52 THR 299    Q8TF42    T       299
2e5k A       53 SER 300    Q8TF42    S       300
2e5k A       54 LEU 301    Q8TF42    L       301
2e5k A       55 THR 302    Q8TF42    T       302
2e5k A       56 THR 303    Q8TF42    T       303
2e5k A       57 GLY 304    Q8TF42    G       304
2e5k A       58 CYS 305    Q8TF42    C       305
2e5k A       59 SER 306    Q8TF42    S       306
2e5k A       60 GLY 307    Q8TF42    G       307
2e5k A       61 LEU 308    Q8TF42    L       308
2e5k A       62 LEU 309    Q8TF42    L       309
2e5k A       63 PRO 310    Q8TF42    P       310
2e5k A       64 GLU 311    Q8TF42    E       311
2e5k A       65 ASN 312    Q8TF42    N       312
2e5k A       66 TYR 313    Q8TF42    Y       313
2e5k A       67 ILE 314    Q8TF42    I       314
2e5k A       68 THR 315    Q8TF42    T       315
2e5k A       69 LYS 316    Q8TF42    K       316
2e5k A       70 ALA 317    Q8TF42    A       317
2e5k A       71 ASP 318    Q8TF42    D       318
2e5k A       72 GLU 319    Q8TF42    E       319
2e5k A       73 CYS 320    Q8TF42    C       320
2e5k A       74 SER 321    Q8TF42    S       321
2e5k A       75 THR 322    Q8TF42    T       322
2e5k A       76 TRP 323    Q8TF42    W       323
2e5k A       77 ILE 324    Q8TF42    I       324
2e5k A       78 PHE 325    Q8TF42    F       325
2e5k A       79 HIS 326    Q8TF42    H       326
2e5k A       80 GLY 327    Q8TF42    G       327
2e5k A       81 SER 328    Q8TF42    S       328
2e5k A       82 SER 329    Q8TF42    Y       329
2e5k A       83 GLY 330    Q8TF42    S       330
2e5k A       84 PRO 331    Q8TF42    I       331
2e5k A       85 SER 332    Q8TF42    L       332
2e5k A       86 SER 333    Q8TF42    N       333
2e5k A       87 GLY 334    Q8TF42    T       334

A total of 87 residues were displayed for 1 chains.

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