Project name: survivor [mutate: FC18R]

Status: done

submitted: 2019-10-11 03:25:57, status changed: 2019-10-11 05:54:56
Settings
Chain sequence(s) C: LKFNQLKFRKKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSSYMFRVDHDTIIDATKCGNFARFINHSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIEDVKIPCLCGSENCRGTLN
Distance of aggregation 10 Å
Dynamic mode Yes
Mutated residues FC18R
Energy difference between WT (input) and mutated protein (by FoldX) 1.43466 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
-3.9338
Maximal score value
2.3847
Average score
-0.7522
Total score value
-112.8288

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
4 L C 1.0640
5 K C 0.0875
6 F C 1.5872
7 N C 0.2909
8 Q C -0.3819
9 L C 0.3611
10 K C -0.8049
11 F C -1.5912
12 R C -2.5945
13 K C -3.0755
14 K C -2.9479
15 K C -2.0880
16 L C -1.8665
17 K C -2.2867
18 R C -2.0064 mutated: FC18R
19 C C -1.4435
20 K C -1.8203
21 S C -0.9745
22 H C -0.6263
23 I C 1.1814
24 H C 0.4404
25 D C 0.0000
26 W C -0.6017
27 G C -1.1882
28 L C 0.0000
29 F C -1.1385
30 A C 0.0000
31 M C 0.0000
32 E C -0.8327
33 P C 0.4901
34 I C 1.1974
35 A C -0.1697
36 A C -1.1037
37 D C -1.9702
38 E C 0.0000
39 M C -0.1227
40 V C 0.0000
41 I C 0.0000
42 E C -1.3229
43 Y C 0.0000
44 V C -0.7895
45 G C 0.0000
46 Q C -1.0897
47 N C -1.4774
48 I C -0.7773
49 R C -2.1486
50 Q C -0.2789
51 V C 2.0735
52 I C 2.3847
53 A C 0.0000
54 D C 0.1406
55 M C 0.7866
56 R C -0.9151
57 E C -1.8017
58 K C -3.4262
59 R C -3.1073
60 Y C -1.6773
61 E C -3.4465
62 D C -3.9338
63 E C -3.1032
64 G C -0.9940
65 I C 1.0216
66 G C 0.4780
67 S C 0.0398
68 S C 0.0000
69 Y C 0.0489
70 M C 0.0171
71 F C -0.4685
72 R C -1.9712
73 V C 0.0000
74 D C -3.3182
75 H C -2.7479
76 D C -2.9772
77 T C -2.5089
78 I C 0.0000
79 I C 0.0000
80 D C 0.0000
81 A C 0.0000
82 T C -1.0126
83 K C -1.9192
84 C C -1.3671
85 G C -1.3611
86 N C -1.9082
87 F C 0.0000
88 A C -1.3005
89 R C 0.0000
90 F C 0.0000
91 I C 0.0000
92 N C 0.0000
93 H C -0.4806
94 S C -0.3388
95 C C -1.2272
96 N C -1.7489
97 P C -1.4890
98 N C -1.6933
99 C C 0.0000
100 Y C -0.5082
101 A C 0.0000
102 K C -0.8939
103 V C 0.0000
104 I C 1.3950
105 T C 0.5354
106 V C 0.1675
107 E C -1.5704
108 S C -1.4019
109 Q C -0.7278
110 K C 0.0000
111 K C -0.2930
112 I C 0.0000
113 V C -0.1134
114 I C 0.0000
115 Y C -0.6932
116 S C 0.0000
117 K C -2.2459
118 Q C -1.7895
119 H C -0.2980
120 I C 1.5823
121 N C 0.8041
122 V C 1.2053
123 N C -0.2987
124 E C 0.0000
125 E C -1.7020
126 I C 0.0000
127 T C -0.8220
128 Y C 0.0000
129 D C -0.8886
130 Y C 0.0000
131 K C -1.5813
132 F C 0.0000
133 P C -0.9415
134 I C -0.3855
135 E C -2.1051
136 D C -2.9125
137 V C 0.0000
138 K C -2.9521
139 I C 0.0000
140 P C -0.5027
141 C C 0.0000
142 L C 0.9677
143 C C 0.1199
144 G C -1.2696
145 S C -1.6999
146 E C -2.7879
147 N C -2.6502
148 C C -2.1592
149 R C -2.2914
150 G C 0.0000
151 T C -0.5586
152 L C 0.0000
153 N C -2.4895

Above is the comparison between the input structure and the most aggregation prone model (predicted in the flexibility simulations, download both models in the PDB file format , download table with rmsd values ). The picture presents the most aggregation prone model (in blue) superimposed on the input structure (in red). The plot shows rmsd profile (distances between residues of the superimposed structures).

Dynamic mode uses CABS-flex simulations of protein structure fluctuations. The structure fluctuations may have impact on the size and extent of aggregation "hot-spots" on the protein surface. The dynamic mode uses the following pipeline: (1) based on the input structure, CABS-flex predicts a set of different models reflecting protein dynamics in solution; (2) for each of these models A3D score is calculated; (3) finally, the most aggregation prone model (the model with the highest A3D score, -0.7522 in this case) is selected and presented in A3D results.


 

Laboratory of Theory of Biopolymers 2015