Project name: ZEDIII LVTEK-AQASS [mutate: LE307A, TE309N, VE391A, EE393S, KE394S]

Chain sequence(s)	E: MRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGS
Distance of aggregation	10 Å
Dynamic mode	No
Mutated residues	LE307A, TE309N, VE391A, EE393S, KE394S
Energy difference between WT (input) and mutated protein (by FoldX)	4.4647 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: 1.6091
• Average score: -0.4942
• Total score value: -53.3747

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	0.8523
299	R	E	-0.4626
300	L	E	1.0959
301	K	E	-0.2373
302	G	E	0.0000
303	V	E	1.6091
304	S	E	0.5621
305	Y	E	0.3083
306	S	E	-0.1570
307	A	E	-0.4272	mutated: LE307A
308	C	E	0.0000
309	N	E	-1.8122	mutated: TE309N
310	A	E	-1.0278
311	A	E	-0.6366
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	-1.6348
334	G	E	0.0000
335	T	E	-2.0574
336	D	E	-2.2914
337	G	E	0.0000
338	P	E	-1.1799
339	C	E	0.0000
340	K	E	-0.5019
341	V	E	0.0000
342	P	E	-0.4323
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	-0.2687
363	P	E	0.0000
364	V	E	0.0000
365	I	E	0.0000
366	T	E	-1.2113
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	-0.5195
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	-0.7149
391	A	E	-0.7139	mutated: VE391A
392	G	E	-0.9435
393	S	E	-0.7726	mutated: EE393S
394	S	E	-0.7993	mutated: KE394S
395	K	E	-0.8999
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