Project name: SH3_E107C

Status: done

submitted: 2019-03-14 19:06:29, status changed: 2019-03-14 20:43:12
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues EA107C
Energy difference between WT (input) and mutated protein (by FoldX) 1.05655 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
-3.1049
Maximal score value
1.799
Average score
-0.9259
Total score value
-52.7757

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 0.5161
86 L A 0.7936
87 F A 0.9612
88 V A 0.5074
89 A A 0.0000
90 L A -0.1158
91 Y A -0.5465
92 D A -2.5326
93 Y A -1.9370
94 E A -2.6522
95 A A -2.6327
96 R A -2.9879
97 T A -2.6628
98 E A -3.1049
99 D A -3.0452
100 D A 0.0000
101 L A 0.0000
102 S A -2.2230
103 F A 0.0000
104 H A -2.6610
105 K A -2.3336
106 G A -1.3450
107 C A 0.0000 mutated: EA107C
108 K A -0.5205
109 F A 0.0000
110 Q A -0.5093
111 I A -0.0552
112 L A 0.1430
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 -1.1529
122 A A 0.0000
123 R A -1.7170
124 S A 0.0000
125 L A 0.0945
126 T A -0.4226
127 T A -0.7980
128 G A -1.3624
129 E A -2.2448
130 T A -1.6962
131 G A -1.5015
132 Y A -0.8695
133 I A 0.0000
134 P A 0.0000
135 S A -0.9206
136 N A -1.1504
137 Y A -0.1243
138 V A 0.0000
139 A A 0.4178
140 P A 0.7774
141 V A 1.7990

 

Laboratory of Theory of Biopolymers 2015