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

Chain sequence(s)	E: MRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGS
Distance of aggregation	10 Å
Dynamic mode	No
Mutated residues	EE393S, KE394S, LE307A, TE309A
Energy difference between WT (input) and mutated protein (by FoldX)	3.1805 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.

• Minimal score value: -3.2015
• Maximal score value: 1.631
• Average score: -0.3963
• Total score value: -42.7952

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
298	M	E	0.8467
299	R	E	-0.4713
300	L	E	1.0916
301	K	E	-0.2258
302	G	E	0.0000
303	V	E	1.6310
304	S	E	0.5762
305	Y	E	0.3363
306	S	E	0.0478
307	A	E	0.1953	mutated: LE307A
308	C	E	0.0000
309	A	E	-0.1665	mutated: TE309A
310	A	E	-0.1831
311	A	E	-0.1409
312	F	E	0.0000
313	T	E	-0.5321
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	-0.9119
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	-2.0543
337	G	E	0.0000
338	P	E	-1.1596
339	C	E	0.0000
340	K	E	-0.2291
341	V	E	0.0000
342	P	E	0.1350
343	A	E	-0.1575
344	Q	E	-0.4618
345	M	E	0.0000
346	A	E	0.0000
347	V	E	0.9070
348	D	E	-0.3298
349	M	E	-0.0070
350	Q	E	-1.0424
351	T	E	-0.5233
352	L	E	0.0697
353	T	E	-0.0281
354	P	E	-0.3925
355	V	E	-0.0534
356	G	E	-0.7778
357	R	E	-1.7682
358	L	E	-0.2272
359	I	E	0.5781
360	T	E	0.3180
361	A	E	-0.0146
362	N	E	-0.2561
363	P	E	0.0000
364	V	E	0.0000
365	I	E	0.0000
366	T	E	-1.1972
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	-0.5223
378	L	E	0.0000
379	D	E	-0.9275
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	0.1734
387	I	E	0.0000
388	V	E	0.0000
389	I	E	0.0000
390	G	E	0.0000
391	V	E	0.9760
392	G	E	-0.0349
393	S	E	-0.3102	mutated: EE393S
394	S	E	-0.2542	mutated: KE394S
395	K	E	-0.2424
396	I	E	0.1832
397	T	E	-0.0468
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