Project name: SH3_I111G

Status: done

submitted: 2019-03-14 19:08:40, status changed: 2019-03-14 21:00:14
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues IA111G
Energy difference between WT (input) and mutated protein (by FoldX) 4.75721 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
1.8103
Average score
-1.0255
Total score value
-58.4514

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 0.3770
86 L A 0.6122
87 F A 0.7902
88 V A 0.4449
89 A A 0.0000
90 L A -0.1463
91 Y A -0.5748
92 D A -2.5599
93 Y A -1.9315
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 -2.7282
105 K A -2.4059
106 G A -1.4533
107 E A -1.3077
108 K A -0.7379
109 F A 0.0000
110 Q A -0.9372
111 G A -0.8979 mutated: IA111G
112 L A -0.2420
113 N A -1.1332
114 S A -1.4098
115 S A -1.6177
116 E A -2.5751
117 G A -2.1462
118 D A -2.4532
119 W A -1.1067
120 W A -1.2468
121 E A -1.3734
122 A A 0.0000
123 R A -1.9361
124 S A 0.0000
125 L A 0.0274
126 T A -0.4881
127 T A -0.8294
128 G A -1.3692
129 E A -2.2470
130 T A -1.7955
131 G A -1.5780
132 Y A -0.9572
133 I A 0.0000
134 P A 0.0000
135 S A -1.0113
136 N A -1.1484
137 Y A -0.1197
138 V A 0.0000
139 A A 0.4297
140 P A 0.7907
141 V A 1.8103

 

Laboratory of Theory of Biopolymers 2015