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Figure 1 | BMC Bioinformatics

Figure 1

From: Effective inter-residue contact definitions for accurate protein fold recognition

Figure 1

ROC curves of structure pair retrieval on the fold level dataset. To determine corresponding residues in protein pairs, TM-align (the left column), HHpred (the middle column), and SUPRB (the right column) were used. Three different bases for residue contact definitions are used, the Cα-Cα distance (the first row), the Cβ-Cβ distance (the second row), and the heavy atom distance (the third row). A, ROC curves using TM-align alignments and the Cα-Cα distance for contact definition. 15 different distance cutoffs were used, namely, 4.5, 5.0, 5.5, 6.0, 6.5, 7.0, 7.5, 8.0, 10.0, 12.0, 15.0, 20.0, 30.0, 50.0, and 100.0 Å to define contacts. B, HHpred alignments and the Cα-Cα distance were used. C, SUPRB alignments and the Cα-Cα distance were used. D, ROC curves using TM-align alignments and the Cβ-Cβ distance for contact definition. The same 15 different distance thresholds as used for the Cα-Cα distance cutoffs were used. E, HHpred alignments and the Cβ-Cβ distance were used. F, SUPRB alignments and the Cβ-Cβ distance were used. G, ROC curves using TM-align alignments and the heavy atom distance for contact definition. The same 15 different distance thresholds as used for the Cα-Cα distance cutoffs were used. H, HHpred alignments and the heavy atom distance were used. I, SUPRB alignments and the heavy atom distance were used

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