Project name: SH3_E129P

Status: done

submitted: 2019-03-14 19:20:26, status changed: 2019-03-14 22:29:24
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues EA129P
Energy difference between WT (input) and mutated protein (by FoldX) 2.588 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
-3.0687
Maximal score value
1.7964
Average score
-0.8763
Total score value
-49.9469

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 0.9234
88 V A 0.4306
89 A A 0.0000
90 L A -0.1515
91 Y A -0.5751
92 D A -2.5604
93 Y A -1.9045
94 E A -2.6126
95 A A -2.5708
96 R A -2.9594
97 T A -2.6340
98 E A -3.0687
99 D A -3.0035
100 D A 0.0000
101 L A -1.5088
102 S A -1.9181
103 F A 0.0000
104 H A -2.7291
105 K A -2.4066
106 G A -1.4592
107 E A -1.3102
108 K A -0.6438
109 F A 0.0000
110 Q A -0.5092
111 I A -0.0569
112 L A 0.1429
113 N A -0.8883
114 S A -1.1799
115 S A -1.5966
116 E A -2.5603
117 G A -2.1347
118 D A -2.4456
119 W A -1.1053
120 W A -1.0569
121 E A -1.1325
122 A A 0.0000
123 R A -1.1366
124 S A 0.0000
125 L A 0.3392
126 T A -0.1915
127 T A -0.2548
128 G A -0.5057
129 P A -0.4605 mutated: EA129P
130 T A -0.7954
131 G A -1.0404
132 Y A -0.8172
133 I A 0.0000
134 P A 0.0000
135 S A -0.9214
136 N A -1.1508
137 Y A -0.1246
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