Project name: SH3_G106R

Status: done

submitted: 2019-03-14 19:06:13, status changed: 2019-03-14 20:42:29
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues GA106R
Energy difference between WT (input) and mutated protein (by FoldX) 3.06516 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
1.6191
Average score
-1.012
Total score value
-57.6822

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 0.5034
86 L A 0.7618
87 F A 0.6900
88 V A 0.0061
89 A A 0.0000
90 L A -0.2880
91 Y A -0.5414
92 D A -2.4876
93 Y A -1.8063
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 -2.7539
105 K A -2.3841
106 R A -2.5213 mutated: GA106R
107 E A -1.7901
108 K A -0.9551
109 F A 0.0000
110 Q A -0.5267
111 I A -0.0568
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 -1.7155
124 S A 0.0000
125 L A 0.0445
126 T A -0.6153
127 T A -0.8205
128 G A -1.3572
129 E A -2.2401
130 T A -1.6927
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 -1.1511
137 Y A -0.0499
138 V A 0.0000
139 A A 0.2331
140 P A 0.7401
141 V A 1.6191

 

Laboratory of Theory of Biopolymers 2015