File S1 - Biochemical and Structural Characterization of SplD Protease from Staphylococcus aureus

Figure S1 , Overall fold of SplD protease. Figure S2, Interpretation of the orientation of the sidechain of catalytic triad Ser156 in the crystal structure of SplD. Figure S3, Comparison of substrate specificities of SplD and HNE proteases. Figure S4, Disposition of the N-terminal glutamic acid residue in the structures of SplA, SplB and GS-SplD proteases. Note S1, Ambiguity of P(n) and P(n)’ subsite specificity determination in fluorescence quenched LSTS assay. Note S2, Conformation of the catalytic triad serine in the crystal structure of SplD protease. Table S1, synthetic substrates tested for hydrolysis by SplD protease. Table S2, SplD substrate specificity determined using CLIPS. Table S3, Average main chain angles of the residues forming the oxyanion hole. Table S4, Predictions of the in silico model of SplD interaction with consensus substrate. Table S5, Potential physiological substrates of SplD protease. (DOC)