Project name: SH3_L86P

Status: done

submitted: 2019-03-14 18:54:43, status changed: 2019-03-14 19:09:56
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues LA86P
Energy difference between WT (input) and mutated protein (by FoldX) 1.03243 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
1.6158
Average score
-1.0091
Total score value
-57.5202

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 0.1316
86 P A 0.0513 mutated: LA86P
87 F A 0.5185
88 V A 0.2292
89 A A 0.0000
90 L A -0.1137
91 Y A -0.5342
92 D A -2.5196
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 -3.0436
100 D A 0.0000
101 L A 0.0000
102 S A -2.2061
103 F A 0.0000
104 H A -2.6770
105 K A -2.3026
106 G A -1.2399
107 E A -1.1902
108 K A -0.8483
109 F A 0.0000
110 Q A -1.1858
111 I A -0.4007
112 L A 0.0874
113 N A -0.9142
114 S A -1.1623
115 S A -1.5884
116 E A -2.5599
117 G A -2.1340
118 D A -2.4444
119 W A -1.1028
120 W A -1.0909
121 E A -1.1948
122 A A 0.0000
123 R A -1.8499
124 S A 0.0000
125 L A 0.1072
126 T A -0.3315
127 T A -0.7516
128 G A -1.3336
129 E A -2.1920
130 T A -1.7069
131 G A -1.4850
132 Y A -0.8552
133 I A 0.0000
134 P A 0.0000
135 S A -0.9195
136 N A -1.1504
137 Y A -0.1371
138 V A 0.0000
139 A A 0.3242
140 P A 0.5321
141 V A 1.6158

 

Laboratory of Theory of Biopolymers 2015