Project name: SH3_E107L

Status: done

submitted: 2019-03-14 19:06:43, status changed: 2019-03-14 20:43:39
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues EA107L
Energy difference between WT (input) and mutated protein (by FoldX) 1.27593 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
-3.1037
Maximal score value
1.8005
Average score
-0.9302
Total score value
-53.0208

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 0.7949
87 F A 0.9936
88 V A 0.5727
89 A A 0.0000
90 L A -0.0846
91 Y A -0.5203
92 D A -2.5027
93 Y A -1.9339
94 E A -2.6483
95 A A -2.6289
96 R A -2.9864
97 T A -2.6617
98 E A -3.1037
99 D A -3.0442
100 D A 0.0000
101 L A 0.0000
102 S A -2.2133
103 F A 0.0000
104 H A -2.5953
105 K A -2.2684
106 G A -1.2438
107 L A -0.8731 mutated: EA107L
108 K A -0.4210
109 F A 0.0000
110 Q A -0.5112
111 I A -0.0542
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 -1.7205
124 S A 0.0000
125 L A 0.1221
126 T A -0.3795
127 T A -0.7787
128 G A -1.3676
129 E A -2.2465
130 T A -1.6972
131 G A -1.5002
132 Y A -0.8683
133 I A 0.0000
134 P A 0.0000
135 S A -0.9206
136 N A -1.1504
137 Y A -0.1243
138 V A 0.0000
139 A A 0.4187
140 P A 0.7786
141 V A 1.8005

 

Laboratory of Theory of Biopolymers 2015