The PyMOL Molecular Graphics System (2002) on World Wide Web ) was used to prepare these figures. Only a few substrate-binding residues are shown as markers. Balc424 is shown in semi-transparent surface (blue) representation with secondary elements at the active site pocket. Carbon atoms are shown in green (QRATKM) and gray (RRATKM). Superposed stick models of QRATKM and RRATKM are shown in green, and gray, respectively. Carbon, oxygen, nitrogen, sulfur and zinc atoms are shown in green, red, blue, yellow and magenta, respectively. Substrate peptide is shown in sphere (CPK) model. Balc424 is shown in solid blue-colored surface. (A) Figure shows the substrate peptide (QRATKM) binding in the active site of Balc424. Inhibition of Balc424 catalytic activity at increasing concentrations (µM) of QRATKML (E) and of RRATKML (F).īinding of the substrate peptide in the active site of Balc424. The PyMOL Molecular Graphics System (2002) on World Wide Web ) was used to prepare C and D figures. The peptide atoms are colored according to B factor with RGB (Red-Green-Blue) color ramp with blue and red corresponding to the lowest (17 Å 2) and highest (50 Å 2). Distribution of B factors for the QRATKM and RRATKM are shown in C and D, respectively. Figures were prepared using Molscript, Raster3D and Bobscript –. Carbon atoms are shown in green (QRATKM) and black (RRATKM). Zinc, oxygen and nitrogen atoms are shown as magenta, red and blue spheres, respectively. QRATKM (green) and RRATKM (gray) peptides are shown in ball and stick model. The electron density is from composite omit maps (2|F o|-|F c|) and contoured at 1σ level. Crystal data and refinement statistics of Balc424 with substrate peptide complexesĮlectron density maps (blue mesh) for bound substrate (QRATKM) and its variant (RRATKM) are shown in A and B, respectively.
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