Project name: SH3_G106W

Status: done

submitted: 2019-03-14 19:06:22, status changed: 2019-03-14 20:42:38
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues GA106W
Energy difference between WT (input) and mutated protein (by FoldX) 2.84831 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
1.9211
Average score
-0.7902
Total score value
-45.0403

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 0.5021
86 L A 0.7616
87 F A 1.0519
88 V A 0.9794
89 A A 0.0000
90 L A 0.5603
91 Y A 0.1532
92 D A -1.9255
93 Y A -1.7624
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 -1.8247
105 K A -0.6408
106 W A 0.6327 mutated: GA106W
107 E A -0.2436
108 K A -0.1361
109 F A 0.0000
110 Q A -0.5254
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 0.0516
126 T A -0.2970
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 -1.1511
137 Y A -0.0179
138 V A 0.0000
139 A A 0.5327
140 P A 0.7377
141 V A 1.9211

 

Laboratory of Theory of Biopolymers 2015