Project name: SH3_D99P

Status: done

submitted: 2019-03-14 19:03:18, status changed: 2019-03-14 20:15:16
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues DA99P
Energy difference between WT (input) and mutated protein (by FoldX) 2.98941 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
-2.7282
Maximal score value
1.7964
Average score
-0.8701
Total score value
-49.5968

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 0.5173
86 L A 0.7932
87 F A 0.9238
88 V A 0.4313
89 A A 0.0000
90 L A -0.1511
91 Y A -0.5748
92 D A -2.5599
93 Y A -1.9315
94 E A -2.6448
95 A A -2.3543
96 R A -2.7253
97 T A -2.1569
98 E A -2.3386
99 P A -1.4818 mutated: DA99P
100 D A 0.0000
101 L A 0.0000
102 S A -2.0300
103 F A 0.0000
104 H A -2.7282
105 K A -2.4059
106 G A -1.4581
107 E A -1.3078
108 K A -0.6426
109 F A 0.0000
110 Q A -0.5065
111 I A -0.0410
112 L A 0.1646
113 N A -0.8729
114 S A -1.1702
115 S A -1.5970
116 E A -2.5631
117 G A -2.1386
118 D A -2.4409
119 W A -1.0890
120 W A -1.0293
121 E A -0.9356
122 A A 0.0000
123 R A -1.7002
124 S A 0.0000
125 L A 0.0591
126 T A -0.4730
127 T A -0.8207
128 G A -1.3571
129 E A -2.2399
130 T A -1.4691
131 G A -0.9877
132 Y A -0.3595
133 I A 0.0000
134 P A 0.0000
135 S A -0.9125
136 N A -1.1527
137 Y A -0.1259
138 V A 0.0000
139 A A 0.4158
140 P A 0.7757
141 V A 1.7964

 

Laboratory of Theory of Biopolymers 2015