Project name: SH3_K105N

Status: done

submitted: 2019-03-14 19:05:29, status changed: 2019-03-14 20:35:17
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues KA105N
Energy difference between WT (input) and mutated protein (by FoldX) 1.71221 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
1.806
Average score
-0.9018
Total score value
-51.4041

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 0.5179
86 L A 0.7946
87 F A 0.9575
88 V A 0.6116
89 A A 0.0000
90 L A 0.2407
91 Y A -0.2277
92 D A -2.2932
93 Y A -1.8128
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 -2.4055
105 N A -1.7462 mutated: KA105N
106 G A -1.0585
107 E A -1.0674
108 K A -0.5237
109 F A 0.0000
110 Q A -0.5083
111 I A -0.0568
112 L A 0.1429
113 N A -0.8879
114 S A -1.1794
115 S A -1.5962
116 E A -2.5599
117 G A -2.1340
118 D A -2.4444
119 W A -1.1028
120 W A -1.0557
121 E A -1.1530
122 A A 0.0000
123 R A -1.7155
124 S A 0.0000
125 L A 0.0598
126 T A -0.4650
127 T A -0.8207
128 G A -1.3572
129 E A -2.2401
130 T A -1.6927
131 G A -1.4992
132 Y A -0.8673
133 I A 0.0000
134 P A 0.0000
135 S A -0.9206
136 N A -1.1250
137 Y A 0.0080
138 V A 0.0000
139 A A 0.4655
140 P A 0.7773
141 V A 1.8060

 

Laboratory of Theory of Biopolymers 2015