Project name: SH3_G106A

Status: done

submitted: 2019-03-14 19:05:46, status changed: 2019-03-14 20:35:57
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues GA106A
Energy difference between WT (input) and mutated protein (by FoldX) 3.0519 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
1.8491
Average score
-0.9167
Total score value
-52.2529

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 0.5173
86 L A 0.7932
87 F A 0.9869
88 V A 0.6138
89 A A 0.0000
90 L A 0.0170
91 Y A -0.4257
92 D A -2.4366
93 Y A -1.9125
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 -2.5342
105 K A -2.0369
106 A A -0.8786 mutated: GA106A
107 E A -1.0185
108 K A -0.4920
109 F A 0.0000
110 Q A -0.5091
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 0.0594
126 T A -0.4184
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 -1.1508
137 Y A -0.1102
138 V A 0.0000
139 A A 0.4677
140 P A 0.7757
141 V A 1.8491

 

Laboratory of Theory of Biopolymers 2015