Aggrescan3D: Trp871 [mutate: GX871W]

Project name: Trp871 [mutate: GX871W]

Status: done

submitted: 2019-01-30 09:18:30, status changed: 2019-01-30 11:35:52

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Chain sequence(s)	X: EVTIKVNLIFADGKIQTAEFKGTFEEATAEAYRYADLLAKVNGEYTADLEDGGNHMNIKFA
Distance of aggregation	10 Å
Dynamic mode	Yes
Mutated residues	GX871W
Energy difference between WT (input) and mutated protein (by FoldX)	1.67226 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: -2.4848
Maximal score value: 1.4397
Average score: -0.6835
Total score value: -41.0088

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	-1.5402
821	V	X	-0.6820
822	T	X	-1.3640
823	I	X	0.0000
824	K	X	-1.9756
825	V	X	0.0000
826	N	X	-0.6821
827	L	X	0.0000
828	I	X	1.4397
829	F	X	0.4066
830	A	X	-0.5410
831	D	X	-1.8325
832	G	X	-1.1400
833	K	X	-0.9543
834	I	X	1.0300
835	Q	X	-0.0860
836	T	X	-0.4245
837	A	X	-1.5415
838	E	X	-2.4437
839	F	X	-1.6915
840	K	X	-2.4404
841	G	X	-1.6826
842	T	X	-0.9910
843	F	X	0.0753
844	E	X	-1.8199
845	E	X	-2.4848
846	A	X	0.0000
847	T	X	-0.9616
848	A	X	-1.1206
849	E	X	-1.9702
850	A	X	0.0000
851	Y	X	0.2140
852	R	X	-1.3265
853	Y	X	0.0000
854	A	X	0.0149
855	D	X	-0.8077
856	L	X	0.5815
857	L	X	0.0000
858	A	X	-0.8144
859	K	X	-0.8936
860	V	X	0.4315
861	N	X	-1.1995
862	G	X	-1.1743
863	E	X	-1.4367
864	Y	X	-0.0125
865	T	X	-0.0595
866	A	X	-0.1522
867	D	X	-0.4410
868	L	X	0.4180
869	E	X	-0.9054
870	D	X	-1.5886
871	W	X	-0.0674	mutated: GX871W
872	G	X	-0.7463
873	N	X	-1.0120
874	H	X	-1.2506
875	M	X	-0.7476
876	N	X	-0.4891
877	I	X	0.0000
878	K	X	-0.2177
879	F	X	0.0923

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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, -0.6835 in this case) is selected and presented in A3D results.