Project name: SH3_R123N

Status: done

submitted: 2019-03-14 19:16:51, status changed: 2019-03-14 22:01:17
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues RA123N
Energy difference between WT (input) and mutated protein (by FoldX) 2.26119 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
1.7942
Average score
-0.9042
Total score value
-51.5378

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 0.4536
86 L A 0.7594
87 F A 0.8327
88 V A 0.3740
89 A A 0.0000
90 L A -0.1516
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 -3.0455
100 D A 0.0000
101 L A 0.0000
102 S A -2.2076
103 F A 0.0000
104 H A -2.7287
105 K A -2.4065
106 G A -1.4592
107 E A -1.3381
108 K A -0.6141
109 F A 0.0000
110 Q A -0.4650
111 I A 0.1772
112 L A 0.5600
113 N A -0.7737
114 S A -1.1095
115 S A -1.5605
116 E A -2.5599
117 G A -2.1340
118 D A -2.4444
119 W A -1.1028
120 W A -0.9225
121 E A -0.9016
122 A A 0.0000
123 N A -0.8631 mutated: RA123N
124 S A 0.0000
125 L A 0.0752
126 T A -0.4243
127 T A -0.7418
128 G A -1.2065
129 E A -1.9977
130 T A -1.3139
131 G A -1.2624
132 Y A -0.7061
133 I A 0.0000
134 P A 0.0000
135 S A -0.9195
136 N A -1.1504
137 Y A -0.1243
138 V A 0.0000
139 A A 0.4146
140 P A 0.7426
141 V A 1.7942

 

Laboratory of Theory of Biopolymers 2015