Project name: SH3_E116V

Status: done

submitted: 2019-03-14 19:12:36, status changed: 2019-03-14 21:31:37
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues EA116V
Energy difference between WT (input) and mutated protein (by FoldX) 0.452558 kcal/mol

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
-3.0796
Maximal score value
1.7964
Average score
-0.7434
Total score value
-42.3744

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 0.9238
88 V A 0.4313
89 A A 0.0000
90 L A -0.1511
91 Y A -0.5748
92 D A -2.5599
93 Y A -1.9315
94 E A -2.6452
95 A A -2.6011
96 R A -2.9852
97 T A -2.6608
98 E A -3.0796
99 D A -2.9881
100 D A 0.0000
101 L A 0.0000
102 S A -2.1814
103 F A 0.0000
104 H A -2.7282
105 K A -2.4059
106 G A -1.4581
107 E A -1.3078
108 K A -0.6426
109 F A 0.0000
110 Q A -0.5175
111 I A -0.0600
112 L A 0.1191
113 N A -0.1276
114 S A -0.1154
115 S A 0.1356
116 V A 1.0152 mutated: EA116V
117 G A -0.3643
118 D A -1.6436
119 W A -0.3365
120 W A -0.2716
121 E A -0.5852
122 A A 0.0000
123 R A -1.6818
124 S A 0.0000
125 L A 0.0592
126 T A -0.4730
127 T A -0.8207
128 G A -1.3573
129 E A -2.2402
130 T A -1.6454
131 G A -1.3911
132 Y A -0.6721
133 I A 0.0000
134 P A 0.0000
135 S A -0.8830
136 N A -1.1473
137 Y A -0.1221
138 V A 0.0000
139 A A 0.4158
140 P A 0.7757
141 V A 1.7964

 

Laboratory of Theory of Biopolymers 2015