Project name: SH3_L86T

Status: done

submitted: 2019-03-14 18:54:54, status changed: 2019-03-14 19:09:38
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues LA86T
Energy difference between WT (input) and mutated protein (by FoldX) 3.19615 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
1.6495
Average score
-0.9745
Total score value
-55.5447

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 0.2147
86 T A 0.2410 mutated: LA86T
87 F A 0.6469
88 V A 0.3153
89 A A 0.0000
90 L A -0.1120
91 Y A -0.5397
92 D A -2.5217
93 Y A -1.9321
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 -2.6675
105 K A -2.2948
106 G A -1.2237
107 E A -1.1316
108 K A -0.6523
109 F A 0.0000
110 Q A -0.8661
111 I A -0.2449
112 L A 0.1527
113 N A -0.8845
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 -1.0641
121 E A -1.1587
122 A A 0.0000
123 R A -1.7207
124 S A 0.0000
125 L A 0.2652
126 T A -0.2772
127 T A -0.7220
128 G A -1.2853
129 E A -2.1808
130 T A -1.6671
131 G A -1.4836
132 Y A -0.8544
133 I A 0.0000
134 P A 0.0000
135 S A -0.9195
136 N A -1.1511
137 Y A -0.1408
138 V A 0.0000
139 A A 0.3406
140 P A 0.5870
141 V A 1.6495

 

Laboratory of Theory of Biopolymers 2015