Project name: SH3_R123G

Status: done

submitted: 2019-03-14 19:16:36, status changed: 2019-03-14 22:01:08
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues RA123G
Energy difference between WT (input) and mutated protein (by FoldX) 2.26901 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
-3.1027
Maximal score value
1.7964
Average score
-0.8832
Total score value
-50.345

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 0.4072
86 L A 0.7198
87 F A 0.7924
88 V A 0.3620
89 A A 0.0000
90 L A -0.1511
91 Y A -0.5748
92 D A -2.5597
93 Y A -1.9312
94 E A -2.6448
95 A A -2.6254
96 R A -2.9850
97 T A -2.6607
98 E A -3.1027
99 D A -3.0494
100 D A 0.0000
101 L A 0.0000
102 S A -2.2071
103 F A 0.0000
104 H A -2.7280
105 K A -2.4059
106 G A -1.4581
107 E A -1.3078
108 K A -0.5822
109 F A 0.0000
110 Q A -0.5828
111 I A 0.1602
112 L A 0.6503
113 N A -0.7540
114 S A -1.0899
115 S A -1.5493
116 E A -2.5627
117 G A -2.1360
118 D A -2.4464
119 W A -1.1067
120 W A -0.9096
121 E A -0.8725
122 A A 0.0000
123 G A 0.0000 mutated: RA123G
124 S A 0.0000
125 L A 0.1905
126 T A -0.3489
127 T A -0.7128
128 G A -1.2178
129 E A -1.9510
130 T A -1.2542
131 G A -1.2213
132 Y A -0.6739
133 I A 0.0000
134 P A 0.0000
135 S A -0.9222
136 N A -1.1504
137 Y A -0.1243
138 V A 0.0000
139 A A 0.4158
140 P A 0.7210
141 V A 1.7964

 

Laboratory of Theory of Biopolymers 2015