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Table 1 AUC values for different combinations of features and environment definitions

From: Improving the prediction of protein binding sites by combining heterogeneous data and Voronoi diagrams

Features Voronoi Diagrams Sphere Sliding Window Single (no environment)
s 0.79 0.75 0.77 0.72
e 0.77 0.72 0.75 0.71
c 0.76 0.74 0.72 0.65
b 0.74 0.71 0.69 0.61
s+e 0.78 0.75 0.77 0.73
s+c 0.82 0.78 0.81 0.77
s+b 0.79 0.75 0.77 0.73
e+c 0.81 0.75 0.77 0.76
e+b 0.77 0.73 0.75 0.72
c+b 0.76 0.74 0.72 0.68
s+e+c 0.82 0.78 0.81 0.77
s+e+b 0.79 0.75 0.77 0.73
s+c+b 0.82 0.78 0.8 0.78
e+c+b 0.81 0.75 0.77 0.76
s+e+c+b 0.85 0.78 0.81 0.77
  1. The test consisted of a 5-fold cross validation using dataset B100 where interface residues were defined using DIMPLOT (Wallace, et al., 1995). The first column indicates the combination of features used: structural (s), energy (e), conservation (c), and B-factors (b). The second, third, fourth, fifth columns contain AUC values for Voronoi Diagram, sphere (15 Å cut-off), 9-residue sliding window, and single residue (no environment), respectively.