Project name: SH3_G106L

Status: done

submitted: 2019-03-14 19:06:03, status changed: 2019-03-14 20:36:50
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues GA106L
Energy difference between WT (input) and mutated protein (by FoldX) 2.94408 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
1.9795
Average score
-0.7848
Total score value
-44.7309

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 0.5100
86 L A 0.7795
87 F A 1.1341
88 V A 1.1021
89 A A 0.0000
90 L A 0.5513
91 Y A 0.0780
92 D A -2.0086
93 Y A -1.8236
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 -1.8938
105 K A -0.8030
106 L A 0.8434 mutated: GA106L
107 E A -0.1551
108 K A -0.0587
109 F A 0.0000
110 Q A -0.5154
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 0.0601
126 T A -0.2596
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 -1.1508
137 Y A -0.0526
138 V A 0.0000
139 A A 0.5944
140 P A 0.7580
141 V A 1.9795

 

Laboratory of Theory of Biopolymers 2015