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Figure 5 | BMC Bioinformatics

Figure 5

From: Protein docking by Rotation-Based Uniform Sampling (RotBUS) with fast computing of intermolecular contact distance and residue desolvation

Figure 5

Analysis of the residue-based desolvation filtered subsets. A) Percentage of cases with concentration of near-native solutions (10 Å ligand RMSD with respect to a reference formed by the unbound molecules superimposed on the complex structure) above the value indicated in abscissas at 9 Å (green) and 12.5 Å/14 Å resolution (red), when only the top 1% and 10% docking poses with the best residue-based desolvation values are considered. B) Success rates (near-native solutions defined with respect to the complex structure) after scoring by pyDock (w vdw = 0.02) the top 1% docking poses with the best residue-based desolvation of the docking sets generated at 9 Å and 12.5 Å/14 Å resolution (in red and green, respectively), and the top 10% docking poses with the best residue-based desolvation of the docking sets generated at 9 Å resolution (blue). C) Same as in B but in logarithmic scale.

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