Skip to main content
. Author manuscript; available in PMC: 2017 Jan 12.
Published in final edited form as: J Chem Inf Model. 2016 May 17;56(6):1063–1077. doi: 10.1021/acs.jcim.5b00523

Figure 1.

Figure 1

Examples are given for TrmD, SYK, and FXa, showing the near-native poses (thick sticks with green carbons) among each set of 199 decoys (black lines). Protein surfaces are shown in white and are partially transparent. Ligands are labeled with a short-hand notation above; the complexes are TrmD-gtc000451, SYK-gtc000233, and FXa-gtc000101. These three ligands have the most favorable binding affinity, out of the ligands that have an available crystal structure.