Project name: SH3_L86N

Status: done

submitted: 2019-03-14 18:54:41, status changed: 2019-03-14 19:09:02
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues LA86N
Energy difference between WT (input) and mutated protein (by FoldX) 1.29752 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
1.5151
Average score
-1.0007
Total score value
-57.038

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 0.0797
86 N A -0.0810 mutated: LA86N
87 F A 0.4856
88 V A 0.2174
89 A A 0.0000
90 L A -0.1227
91 Y A -0.5375
92 D A -2.5214
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 -3.0434
100 D A 0.0000
101 L A 0.0000
102 S A -2.2059
103 F A 0.0000
104 H A -2.6825
105 K A -2.3107
106 G A -1.2536
107 E A -1.1869
108 K A -0.8260
109 F A 0.0000
110 Q A -0.8319
111 I A -0.2880
112 L A 0.1203
113 N A -0.8975
114 S A -1.1812
115 S A -1.5972
116 E A -2.5599
117 G A -2.1340
118 D A -2.4444
119 W A -1.1028
120 W A -1.0636
121 E A -1.1648
122 A A 0.0000
123 R A -1.7595
124 S A 0.0000
125 L A 0.2498
126 T A -0.2949
127 T A -0.7308
128 G A -1.2587
129 E A -2.1872
130 T A -1.6660
131 G A -1.5029
132 Y A -0.8699
133 I A 0.0000
134 P A 0.0000
135 S A -0.9206
136 N A -1.1511
137 Y A -0.1387
138 V A 0.0000
139 A A 0.2734
140 P A 0.4899
141 V A 1.5151

 

Laboratory of Theory of Biopolymers 2015