Project name: SH3_F87S

Status: done

submitted: 2019-03-14 18:55:35, status changed: 2019-03-14 19:15:16
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues FA87S
Energy difference between WT (input) and mutated protein (by FoldX) 5.52613 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
1.7175
Average score
-0.9794
Total score value
-55.8261

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 0.4724
86 L A 0.6940
87 S A 0.0000 mutated: FA87S
88 V A 0.3183
89 A A 0.0000
90 L A -0.1783
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 -1.4857
107 E A -1.3428
108 K A -0.7083
109 F A 0.0000
110 Q A -0.5271
111 I A -0.0219
112 L A 0.1897
113 N A -0.8432
114 S A -1.1331
115 S A -1.5809
116 E A -2.5424
117 G A -2.1157
118 D A -2.4203
119 W A -1.0595
120 W A -0.9554
121 E A -1.0940
122 A A 0.0000
123 R A -1.6917
124 S A 0.0000
125 L A 0.0353
126 T A -0.4730
127 T A -0.8207
128 G A -1.3572
129 E A -2.2401
130 T A -1.6857
131 G A -1.4786
132 Y A -0.8315
133 I A 0.0000
134 P A 0.0000
135 S A -0.9178
136 N A -1.1410
137 Y A -0.1508
138 V A 0.0000
139 A A 0.3372
140 P A 0.6757
141 V A 1.7175

 

Laboratory of Theory of Biopolymers 2015