Project name: 1SHG Q16+T24 [mutate: QA16D, TA24D]

Status: done

submitted: 2019-12-02 08:56:30, status changed: 2019-12-24 14:49:32
Settings
Chain sequence(s) A: KELVLALYDYQEKSPREVTMKKGDILTLLNSTNKDWWKVEVNDRQGFVPAAYVKKLD
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues QA16D, TA24D
Energy difference between WT (input) and mutated protein (by FoldX) 4.57316 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.

Show buried residues

Minimal score value
-3.9982
Maximal score value
0.9157
Average score
-1.4161
Total score value
-80.7196

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
residue index residue name chain Aggrescan3D score
mutation
6 K A -2.1785
7 E A -2.0628
8 L A -0.4266
9 V A 0.0000
10 L A 0.1439
11 A A 0.0000
12 L A -0.2080
13 Y A -0.6164
14 D A -2.7033
15 Y A 0.0000
16 D A -3.8476 mutated: QA16D
17 E A -3.7388
18 K A -3.1944
19 S A -1.8783
20 P A -1.4028
21 R A -1.9254
22 E A 0.0000
23 V A 0.0000
24 D A -3.9693 mutated: TA24D
25 M A 0.0000
26 K A -3.3098
27 K A -2.3973
28 G A -1.3143
29 D A -0.9361
30 I A 0.9157
31 L A 0.0000
32 T A -0.7391
33 L A 0.0000
34 L A -0.8183
35 N A -1.0908
36 S A -1.4295
37 T A -1.5864
38 N A -2.8393
39 K A -3.1620
40 D A -2.8141
41 W A -1.5161
42 W A -1.0414
43 K A -1.1164
44 V A 0.0000
45 E A -2.2609
46 V A -2.5995
47 N A -2.7374
48 D A -3.6644
49 R A -3.9982
50 Q A -3.2117
51 G A 0.0000
52 F A -1.1053
53 V A 0.0000
54 P A -0.5874
55 A A -1.2611
56 A A -0.3168
57 Y A 0.1871
58 V A 0.0000
59 K A -1.3142
60 K A -1.6058
61 L A -0.8134
62 D A -2.2271

 

Laboratory of Theory of Biopolymers 2015