Aggrescan3D: 36e0e114df0d357

Project name: 36e0e114df0d357

Status: done

submitted: 2019-01-29 14:30:45, status changed: 2019-01-29 16:44:40

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Chain sequence(s)	X: EVTIKVNLIFADGKIQTAEFKGTFEEATAEAYRYADLLAKVNGEYTADLEDGGNHMNIKFA
Distance of aggregation	10 Å
Dynamic mode	Yes

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Show buried residues

Minimal score value: -2.7408
Maximal score value: 1.5351
Average score: -0.7393
Total score value: -44.3594

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	-1.4959
821	V	X	-0.1015
822	T	X	-0.7569
823	I	X	0.0000
824	K	X	-1.4483
825	V	X	0.0000
826	N	X	-0.5115
827	L	X	0.0000
828	I	X	1.2537
829	F	X	0.7141
830	A	X	-0.2912
831	D	X	-1.5699
832	G	X	-1.3128
833	K	X	-0.7445
834	I	X	1.2860
835	Q	X	0.1581
836	T	X	-0.2572
837	A	X	-0.6807
838	E	X	-1.4579
839	F	X	-1.1351
840	K	X	-1.9870
841	G	X	-1.4488
842	T	X	-0.7743
843	F	X	-0.0161
844	E	X	-1.8876
845	E	X	-2.5231
846	A	X	0.0000
847	T	X	-0.8599
848	A	X	-0.9801
849	E	X	-1.4889
850	A	X	0.0000
851	Y	X	-0.1216
852	R	X	-1.8625
853	Y	X	-0.8013
854	A	X	-0.7493
855	D	X	-2.0426
856	L	X	-0.5405
857	L	X	0.0000
858	A	X	-1.6355
859	K	X	-1.6110
860	V	X	-0.3987
861	N	X	-1.6670
862	G	X	-0.7733
863	E	X	-1.0750
864	Y	X	0.1839
865	T	X	0.3420
866	A	X	0.0008
867	D	X	-0.4678
868	L	X	0.0515
869	E	X	-2.0220
870	D	X	-2.7408
871	G	X	-1.9801
872	G	X	-1.7246
873	N	X	-1.3620
874	H	X	-1.7650
875	M	X	-0.8909
876	N	X	-0.3521
877	I	X	0.0000
878	K	X	0.4282
879	F	X	1.5351

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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, -0.7393 in this case) is selected and presented in A3D results.