Project name: ZEDIII EKSS [mutate: LE307A, TE309A, VE391A, EE393S, KE394S]

Status: done

submitted: 2018-07-02 23:57:21, status changed: 2018-07-03 00:03:50
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Chain sequence(s) E: MRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGS
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues LE307A, TE309A, VE391A, EE393S, KE394S
Energy difference between WT (input) and mutated protein (by FoldX) 4.31994 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
-3.2015
Maximal score value
1.6407
Average score
-0.4442
Total score value
-47.9697

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
298 M E 0.8518
299 R E -0.4626
300 L E 1.0959
301 K E -0.2196
302 G E 0.0000
303 V E 1.6407
304 S E 0.5825
305 Y E 0.3458
306 S E 0.0603
307 A E -0.0087 mutated: LE307A
308 C E 0.0000
309 A E -0.4616 mutated: TE309A
310 A E -0.3779
311 A E -0.3394
312 F E 0.0000
313 T E -0.5361
314 F E 0.0374
315 T E -0.5627
316 K E -0.6531
317 I E 1.0062
318 P E 0.0000
319 A E -0.4973
320 E E -1.5447
321 T E -0.5952
322 L E 0.6094
323 H E -0.6391
324 G E -0.6601
325 T E -0.9111
326 V E 0.0000
327 T E -0.3211
328 V E 0.0000
329 E E -0.4694
330 V E 0.0000
331 Q E -1.5002
332 Y E 0.0000
333 A E -1.4819
334 G E 0.0000
335 T E -1.9052
336 D E -2.0527
337 G E 0.0000
338 P E -1.1533
339 C E 0.0000
340 K E -0.2093
341 V E 0.0000
342 P E -0.2388
343 A E -0.3665
344 Q E -0.4674
345 M E 0.0000
346 A E 0.0000
347 V E 0.9126
348 D E -0.3213
349 M E 0.0023
350 Q E -1.0343
351 T E -0.5102
352 L E 0.0964
353 T E -0.0152
354 P E -0.3852
355 V E -0.0494
356 G E -0.7769
357 R E -1.7654
358 L E -0.2218
359 I E 0.5812
360 T E 0.3199
361 A E -0.0117
362 N E -0.2508
363 P E 0.0000
364 V E 0.0000
365 I E 0.0000
366 T E -1.1941
367 E E -2.4092
368 S E -1.9751
369 T E -2.0300
370 E E -3.2015
371 N E -2.8425
372 S E -2.4114
373 K E -2.3308
374 M E -0.6940
375 M E -0.1056
376 L E 0.0000
377 E E -0.5209
378 L E 0.0000
379 D E -0.9260
380 P E 0.0000
381 P E -0.1005
382 F E 0.4088
383 G E -0.6354
384 D E -1.6240
385 S E 0.0000
386 Y E 0.1758
387 I E 0.0000
388 V E 0.0000
389 I E 0.0000
390 G E -0.4385
391 A E -0.4320 mutated: VE391A
392 G E -0.7254
393 S E -0.6301 mutated: EE393S
394 S E -0.5915 mutated: KE394S
395 K E -0.7417
396 I E -0.0253
397 T E -0.0515
398 H E -0.0045
399 H E -0.8225
400 W E -1.0051
401 H E -1.6658
402 R E -1.1577
403 S E -0.7380
404 G E -0.4890
405 S E -0.1999

 

Laboratory of Theory of Biopolymers 2015