Aggrescan3D: survivor [mutate: FC18N]

Project name: survivor [mutate: FC18N]

Status: done

submitted: 2019-10-11 03:27:31, status changed: 2019-10-11 05:55:35

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Chain sequence(s)	C: LKFNQLKFRKKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSSYMFRVDHDTIIDATKCGNFARFINHSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIEDVKIPCLCGSENCRGTLN
Distance of aggregation	10 Å
Dynamic mode	Yes
Mutated residues	FC18N
Energy difference between WT (input) and mutated protein (by FoldX)	0.119265 kcal/mol 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.

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Minimal score value: -4.0327
Maximal score value: 1.8552
Average score: -0.7862
Total score value: -117.923

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	-0.1140
5	K	C	-1.6164
6	F	C	-1.1705
7	N	C	-2.1722
8	Q	C	-1.9883
9	L	C	0.0000
10	K	C	-2.1584
11	F	C	-0.2080
12	R	C	-1.0697
13	K	C	-1.6295
14	K	C	-1.5227
15	K	C	-2.3981
16	L	C	-1.1238
17	K	C	-2.0684
18	N	C	-1.6304	mutated: FC18N
19	C	C	-1.3063
20	K	C	-2.1196
21	S	C	-1.3409
22	H	C	-0.9443
23	I	C	0.6953
24	H	C	-0.2249
25	D	C	-1.1625
26	W	C	0.0000
27	G	C	-1.1547
28	L	C	0.0000
29	F	C	-1.3656
30	A	C	0.0000
31	M	C	-1.4004
32	E	C	-1.2184
33	P	C	-0.0266
34	I	C	0.0000
35	A	C	0.1254
36	A	C	-0.8909
37	D	C	-1.9704
38	E	C	0.0000
39	M	C	-0.0945
40	V	C	0.0000
41	I	C	0.0000
42	E	C	0.0000
43	Y	C	-0.1693
44	V	C	0.0000
45	G	C	-0.7409
46	Q	C	-1.1060
47	N	C	-1.2838
48	I	C	-0.8233
49	R	C	-1.5364
50	Q	C	-0.5422
51	V	C	1.6522
52	I	C	1.8552
53	A	C	0.0000
54	D	C	-1.0518
55	M	C	0.2722
56	R	C	-0.9174
57	E	C	-2.5934
58	K	C	-3.6989
59	R	C	-3.3489
60	Y	C	-2.6448
61	E	C	-3.9024
62	D	C	-4.0327
63	E	C	-3.1416
64	G	C	-1.6265
65	I	C	0.2674
66	G	C	-0.6333
67	S	C	-0.0915
68	S	C	0.1736
69	Y	C	0.5178
70	M	C	0.6980
71	F	C	0.0592
72	R	C	-1.3054
73	V	C	-1.5571
74	D	C	-2.1517
75	H	C	-2.3630
76	D	C	-1.9774
77	T	C	-1.2878
78	I	C	0.0000
79	I	C	0.0000
80	D	C	0.0000
81	A	C	0.0000
82	T	C	-0.9135
83	K	C	-1.6531
84	C	C	0.0000
85	G	C	-1.2502
86	N	C	-1.8377
87	F	C	0.0000
88	A	C	0.0000
89	R	C	-0.8715
90	F	C	0.0000
91	I	C	0.2724
92	N	C	0.0000
93	H	C	-0.1158
94	S	C	-0.5026
95	C	C	-1.1414
96	N	C	-1.5631
97	P	C	-1.4276
98	N	C	-1.2610
99	C	C	0.0000
100	Y	C	-0.3807
101	A	C	0.0000
102	K	C	-0.7052
103	V	C	0.2249
104	I	C	0.7514
105	T	C	0.2352
106	V	C	0.1786
107	E	C	-1.4625
108	S	C	-1.1630
109	Q	C	-0.7208
110	K	C	0.0000
111	K	C	0.0587
112	I	C	0.0000
113	V	C	0.2335
114	I	C	0.0000
115	Y	C	-0.6310
116	S	C	0.0000
117	K	C	-2.5203
118	Q	C	-2.1941
119	H	C	-0.4503
120	I	C	1.2168
121	N	C	0.5097
122	V	C	0.8985
123	N	C	-0.9725
124	E	C	0.0000
125	E	C	-1.4347
126	I	C	0.0000
127	T	C	-0.4671
128	Y	C	0.0000
129	D	C	0.0000
130	Y	C	-0.2098
131	K	C	-0.6030
132	F	C	-0.1308
133	P	C	-0.0079
134	I	C	0.0460
135	E	C	-2.0822
136	D	C	-2.8329
137	V	C	-1.9744
138	K	C	-2.3452
139	I	C	-1.0550
140	P	C	-0.3009
141	C	C	0.5854
142	L	C	1.3884
143	C	C	0.4077
144	G	C	-1.1923
145	S	C	-1.6675
146	E	C	-3.2293
147	N	C	-2.5899
148	C	C	-2.3910
149	R	C	-2.6171
150	G	C	0.0000
151	T	C	0.0771
152	L	C	0.8140
153	N	C	-0.6508

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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, -0.7862 in this case) is selected and presented in A3D results.