Project name: SH3_F87R

Status: done

submitted: 2019-03-14 18:55:33, status changed: 2019-03-14 19:15:34
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues FA87R
Energy difference between WT (input) and mutated protein (by FoldX) 3.25603 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
1.5861
Average score
-1.0133
Total score value
-57.758

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 0.3744
86 L A 0.4990
87 R A 0.3186 mutated: FA87R
88 V A 0.1304
89 A A 0.0000
90 L A -0.2238
91 Y A -0.5748
92 D A -2.5599
93 Y A -1.9315
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 -2.7282
105 K A -2.4059
106 G A -1.5315
107 E A -1.4009
108 K A -0.8323
109 F A 0.0000
110 Q A -0.6514
111 I A -0.1611
112 L A 0.1465
113 N A -0.8934
114 S A -1.1889
115 S A -1.6029
116 E A -2.5674
117 G A -2.1418
118 D A -2.4548
119 W A -1.1213
120 W A -1.0877
121 E A -1.1654
122 A A 0.0000
123 R A -1.7140
124 S A 0.0000
125 L A -0.0044
126 T A -0.4730
127 T A -0.8207
128 G A -1.3572
129 E A -2.2401
130 T A -1.6901
131 G A -1.5031
132 Y A -0.8774
133 I A 0.0000
134 P A 0.0000
135 S A -1.0041
136 N A -1.1544
137 Y A -0.1951
138 V A 0.0000
139 A A 0.2054
140 P A 0.5093
141 V A 1.5861

 

Laboratory of Theory of Biopolymers 2015