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Table S1. Resolution and measured temperature of X-ray crystal structural analysis. (DOCX 29Â kb)

Figure S2. Superposition of some residues in ligand-free units. Eight ligand-free units are superimposed so that the RMSD targeting the main chain (the N, CÎą and C atoms) would be minimized based on a specific ligand-free unit. a Arg358, b Tyr547, c Ser630, d Ser209, e Val711 and f Asn710. (DOCX 124Â kb)

Figure S4. Superposition of two specific water O atoms in ligand-free units (yellow spheres). Six ligand-free units (1J2E_A, 1J2E_B, 1NU6_A, 1PFQ_A, 1TK3_A and 1TK3_B) that had one of the two specific water O atoms were superimposed so that CÎą atoms in DPP-4 (residue numbers 41â 764) would be minimized based on 1X70_A. The two specific water O atoms of the six ligand-free units (yellow spheres in the white broken circles) superimposed well onto those in 1X70_A with ligand (red spheres). (DOCX 329Â kb)

Figure S1. Structural formula and PDB ID of 68 types of DPP-4 inhibitors. The PDB ID is followed by the chain ID that we used in this study. (DOCX 711Â kb)

Figure S3. Superposition of two specific water O atoms in high temperature-measured units (yellow symbol “+”). The temperature-measured units were superimposed so that Cα atoms in DPP-4 (residue numbers 41–764) would be minimized based on 1X70_A (the two specific water O atoms of 1X70_A are marked by red symbol “+” in the white broken circles). The two specific water O atoms registered in the high temperature-measured units are superimposed well onto those in 1X70_A that was measured at low temperature (yellow symbol “+” in the white broken circles). (DOCX 273 kb)

Table S4. DPP-4 inhibitory activity. (DOCX 30Â kb)

Table S2. B-factor of the first specific water O atom in a unit. (DOCX 40Â kb)

Table S3. B-factor of the second specific water O atom in a unit. (DOCX 41Â kb)