Project name: ZEDIII EKSA [mutate: LE307A, TE309A, VE391A, EE393S, KE394A]

Chain sequence(s)	E: MRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGS
Distance of aggregation	10 Å
Dynamic mode	No
Mutated residues	LE307A, TE309A, VE391A, EE393S, KE394A
Energy difference between WT (input) and mutated protein (by FoldX)	4.1057 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: 1.6407
• Average score: -0.4385
• Total score value: -47.3601

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	0.8518
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	-0.4370	mutated: TE309A
310	A	E	-0.3432
311	A	E	-0.2834
312	F	E	0.0000
313	T	E	-0.5186
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	-1.4994
332	Y	E	0.0000
333	A	E	-1.4803
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	-2.8420
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	-0.4030
391	A	E	-0.3954	mutated: VE391A
392	G	E	-0.6782
393	S	E	-0.5560	mutated: EE393S
394	A	E	-0.4387	mutated: KE394A
395	K	E	-0.6670
396	I	E	0.0125
397	T	E	-0.0363
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