Project name: SH3_G106M

Status: done

submitted: 2019-03-14 19:06:05, status changed: 2019-03-14 20:36:53
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues GA106M
Energy difference between WT (input) and mutated protein (by FoldX) 2.33201 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
-3.1028
Maximal score value
1.9168
Average score
-0.8163
Total score value
-46.5287

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
85 T A 0.5054
86 L A 0.7690
87 F A 1.0469
88 V A 0.9153
89 A A 0.0000
90 L A 0.4134
91 Y A 0.0078
92 D A -2.0472
93 Y A -1.8085
94 E A -2.6452
95 A A -2.6259
96 R A -2.9852
97 T A -2.6608
98 E A -3.1028
99 D A -3.0434
100 D A 0.0000
101 L A 0.0000
102 S A -2.2059
103 F A 0.0000
104 H A -1.9797
105 K A -0.9527
106 M A 0.3816 mutated: GA106M
107 E A -0.3785
108 K A -0.1939
109 F A 0.0000
110 Q A -0.5213
111 I A -0.0560
112 L A 0.1429
113 N A -0.8879
114 S A -1.1794
115 S A -1.5962
116 E A -2.5599
117 G A -2.1340
118 D A -2.4444
119 W A -1.1028
120 W A -1.0557
121 E A -1.1530
122 A A 0.0000
123 R A -1.7128
124 S A 0.0000
125 L A 0.0550
126 T A -0.3108
127 T A -0.8180
128 G A -1.3554
129 E A -2.2392
130 T A -1.6920
131 G A -1.4992
132 Y A -0.8673
133 I A 0.0000
134 P A 0.0000
135 S A -0.9206
136 N A -1.1567
137 Y A -0.0574
138 V A 0.0000
139 A A 0.5209
140 P A 0.7460
141 V A 1.9168

 

Laboratory of Theory of Biopolymers 2015