Aggrescan3D: Trp865-Trp871 [mutate: TX865W, GX871W]

Project name: Trp865-Trp871 [mutate: TX865W, GX871W]

Status: done

submitted: 2019-01-30 09:32:44, status changed: 2019-01-30 11:50:21

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Chain sequence(s)	X: EVTIKVNLIFADGKIQTAEFKGTFEEATAEAYRYADLLAKVNGEYTADLEDGGNHMNIKFA
Distance of aggregation	10 Å
Dynamic mode	Yes
Mutated residues	TX865W, GX871W
Energy difference between WT (input) and mutated protein (by FoldX)	1.47073 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.

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Minimal score value: -2.6039
Maximal score value: 1.5054
Average score: -0.6117
Total score value: -36.7028

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
820	E	X	-1.6082
821	V	X	-0.7779
822	T	X	-1.3107
823	I	X	0.0000
824	K	X	-2.0680
825	V	X	0.0000
826	N	X	-0.4698
827	L	X	0.0000
828	I	X	1.1161
829	F	X	0.3748
830	A	X	-0.4854
831	D	X	-1.9214
832	G	X	-1.2659
833	K	X	-1.3453
834	I	X	0.7314
835	Q	X	-0.1576
836	T	X	-0.5674
837	A	X	-1.6367
838	E	X	-2.6039
839	F	X	-1.8239
840	K	X	-2.4921
841	G	X	-1.6064
842	T	X	-0.9165
843	F	X	0.1131
844	E	X	-1.8292
845	E	X	-2.1685
846	A	X	0.0000
847	T	X	-0.8433
848	A	X	-0.8510
849	E	X	-1.1907
850	A	X	0.0000
851	Y	X	0.3123
852	R	X	-0.9404
853	Y	X	-0.1026
854	A	X	0.1294
855	D	X	-0.8467
856	L	X	-0.0428
857	L	X	0.0000
858	A	X	-1.0682
859	K	X	-1.1341
860	V	X	0.3546
861	N	X	-1.3961
862	G	X	-1.1565
863	E	X	-1.1831
864	Y	X	1.0791
865	W	X	1.5054	mutated: TX865W
866	A	X	0.7442
867	D	X	-0.1074
868	L	X	0.2294
869	E	X	-1.5243
870	D	X	-1.7975
871	W	X	-0.3700	mutated: GX871W
872	G	X	-0.7748
873	N	X	-1.0940
874	H	X	-1.4119
875	M	X	-0.6194
876	N	X	-0.1349
877	I	X	0.0000
878	K	X	0.8332
879	F	X	1.4187

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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, -0.6117 in this case) is selected and presented in A3D results.