Project name: ZEDIII TQ [mutate: VE391A, EE393A, KE394A, LE307A, TE309Q]

Chain sequence(s)	E: MRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGS
Distance of aggregation	10 Å
Dynamic mode	No
Mutated residues	VE391A, EE393A, KE394A, LE307A, TE309Q
Energy difference between WT (input) and mutated protein (by FoldX)	3.59201 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: -3.0985
• Maximal score value: 1.6167
• Average score: -0.4531
• Total score value: -48.9375

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	0.8387
299	R	E	-0.4913
300	L	E	1.0701
301	K	E	-0.2662
302	G	E	0.0000
303	V	E	1.6167
304	S	E	0.5626
305	Y	E	0.4100
306	S	E	-0.0404
307	A	E	-0.2719	mutated: LE307A
308	C	E	0.0000
309	Q	E	-1.5361	mutated: TE309Q
310	A	E	-0.8028
311	A	E	-0.5275
312	F	E	0.0000
313	T	E	-0.5183
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	-1.5374
334	G	E	0.0000
335	T	E	-1.6832
336	D	E	-1.5237
337	G	E	0.0000
338	P	E	-0.9678
339	C	E	0.0000
340	K	E	-0.4102
341	V	E	0.0000
342	P	E	-0.4036
343	A	E	-0.3704
344	Q	E	-0.4672
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	-0.2217
359	I	E	0.5816
360	T	E	0.3207
361	A	E	-0.0143
362	N	E	-0.2648
363	P	E	0.0000
364	V	E	0.0000
365	I	E	0.0000
366	T	E	-1.1114
367	E	E	-2.2987
368	S	E	-1.7561
369	T	E	-1.9128
370	E	E	-3.0985
371	N	E	-2.8420
372	S	E	-2.4116
373	K	E	-2.3309
374	M	E	-0.6939
375	M	E	-0.1054
376	L	E	0.0000
377	E	E	-0.5208
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	-0.6165
391	A	E	-0.5980	mutated: VE391A
392	G	E	-0.7505
393	A	E	-0.4180	mutated: EE393A
394	A	E	-0.5005	mutated: KE394A
395	K	E	-0.7363
396	I	E	0.0494
397	T	E	-0.0360
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