Project name: ZEDIII LTVEK-ANASS [mutate: LE307A, TE309Q, VE391A, EE393S, KE394S]

Chain sequence(s)	E: MRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGS
Distance of aggregation	10 Å
Dynamic mode	No
Mutated residues	LE307A, TE309Q, VE391A, EE393S, KE394S
Energy difference between WT (input) and mutated protein (by FoldX)	3.78602 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: -3.098
• Maximal score value: 1.6141
• Average score: -0.4673
• Total score value: -50.4656

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	0.8537
299	R	E	-0.4593
300	L	E	1.1007
301	K	E	-0.2275
302	G	E	0.0000
303	V	E	1.6141
304	S	E	0.5666
305	Y	E	0.3997
306	S	E	-0.0606
307	A	E	-0.3105	mutated: LE307A
308	C	E	0.0000
309	Q	E	-1.6012	mutated: TE309Q
310	A	E	-0.8679
311	A	E	-0.6209
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	-0.9105
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	-1.5385
334	G	E	0.0000
335	T	E	-1.6813
336	D	E	-1.5201
337	G	E	0.0000
338	P	E	-0.9785
339	C	E	0.0000
340	K	E	-0.4865
341	V	E	0.0000
342	P	E	-0.4204
343	A	E	-0.3772
344	Q	E	-0.4646
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	-0.3846
355	V	E	-0.0487
356	G	E	-0.7758
357	R	E	-1.7628
358	L	E	-0.2157
359	I	E	0.5839
360	T	E	0.3215
361	A	E	-0.0109
362	N	E	-0.2669
363	P	E	0.0000
364	V	E	0.0000
365	I	E	0.0000
366	T	E	-1.1221
367	E	E	-2.2977
368	S	E	-1.7548
369	T	E	-1.9121
370	E	E	-3.0980
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	-0.5195
378	L	E	0.0000
379	D	E	-0.9246
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	-0.6989
391	A	E	-0.6968	mutated: VE391A
392	G	E	-0.9315
393	S	E	-0.7649	mutated: EE393S
394	S	E	-0.7881	mutated: KE394S
395	K	E	-0.8913
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