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. 2017 Feb 15;30(5):387–394. doi: 10.1093/protein/gzx011

Fig. 8.

Fig. 8

Comparison of the accuracy of combined rotations for core Met, Trp and Tyr residues in the Dunbrack 1.0 Å database using the hard-sphere model (red, left bar) and Rosetta (yellow, right bar). Each bar shows the fraction F(Δχ) of residues for which the model prediction was Δχ < 30° for each side chain dihedral angle separately.