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Amino acid conservation mapping onto the structure of the FRP. (A) FRP dimer and tetramer structures shown in surface representation are colored according to conservation (red, high; white, medium; yellow, low). (B) Close-up view of the proposed active site with stick representation of side chains. Side chain oxygen and nitrogen atoms are colored red and blue, respectively. The location of the twofold symmetry axis is indicated with a black ellipse.
