Project name: ZEDIII Tol2 [mutate: LG307A, TG309A, KG394A, EG393A, VG391A]

Status: done

submitted: 2018-06-20 23:21:52, status changed: 2018-06-20 23:29:06
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Chain sequence(s) G: YSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSG
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues LG307A, TG309A, KG394A, EG393A, VG391A
Energy difference between WT (input) and mutated protein (by FoldX) 3.20261 kcal/mol

CAUTION: Your mutation/s can destabilize the protein structure

Changes in protein stability upon mutation are calculated using the FoldX forcefield. Computational prediction of protein stability is used with the intention of preventing the experimental characterization of proteins bearing mutations that significantly destabilize their structure. Mutations resulting in a predicted reduction in protein stability ≥ 1 kcal/mol are considered disruptive.

Show buried residues

Minimal score value
-3.0836
Maximal score value
1.1783
Average score
-0.4824
Total score value
-48.2388

The table below lists A3D score for protein residues. Residues with A3D score > 0.0000 are marked by yellow rows.

residue index residue name chain Aggrescan3D score mutation
residue index residue name chain Aggrescan3D score
mutation
305 Y G 1.0773
306 S G 0.1558
307 A G -0.1237 mutated: LG307A
308 C G 0.0000
309 A G -0.3560 mutated: TG309A
310 A G -0.4149
311 A G -0.1078
312 F G 0.0000
313 T G -0.5721
314 F G 0.0465
315 T G -0.5420
316 K G -0.6625
317 I G 1.0295
318 P G 0.0000
319 A G -0.6619
320 E G -1.7282
321 T G -0.5267
322 L G 0.6462
323 H G -0.7699
324 G G -0.8355
325 T G -0.7624
326 V G 0.0000
327 T G -0.4002
328 V G 0.0000
329 E G -0.3534
330 V G 0.0000
331 Q G -1.6608
332 Y G 0.0000
333 A G -1.4745
334 G G 0.0000
335 T G -1.6264
336 D G -1.5717
337 G G -1.4922
338 P G -0.8185
339 C G 0.0000
340 K G -0.5486
341 V G 0.0000
342 P G -0.2520
343 A G -0.5446
344 Q G -0.3814
345 M G 0.0000
346 A G 0.0000
347 V G 1.1783
348 D G 0.2185
349 M G 0.1446
350 Q G -0.9099
351 T G -0.3531
352 L G 0.2409
353 T G 0.0437
354 P G -0.2801
355 V G -0.0387
356 G G -0.4915
357 R G -1.6414
358 L G -0.3623
359 I G 0.3522
360 T G 0.0262
361 A G -0.1925
362 N G -1.0643
363 P G 0.0000
364 V G -0.1916
365 I G 0.0000
366 T G -0.9467
367 E G -2.1748
368 S G -1.7514
369 T G -1.9761
370 E G -3.0836
371 N G -2.8660
372 S G -2.3757
373 K G -2.2789
374 M G -0.3961
375 M G 0.2147
376 L G 0.0000
377 E G -0.4423
378 L G 0.0000
379 D G -0.7808
380 P G 0.0000
381 P G 0.0797
382 F G 0.8733
383 G G -0.6075
384 D G -1.5715
385 S G 0.0000
386 Y G 0.1388
387 I G 0.0000
388 V G 0.0000
389 I G 0.0000
390 G G 0.0000
391 A G -0.2415 mutated: VG391A
392 G G -0.5093
393 A G -0.2528 mutated: EG393A
394 A G -0.2357 mutated: KG394A
395 K G -0.4345
396 I G 0.0758
397 T G -0.1148
398 H G -0.1593
399 H G -1.1433
400 W G -1.3320
401 H G -1.8300
402 R G -1.2670
403 S G -0.7103
404 G G -0.5856

 

Laboratory of Theory of Biopolymers 2015