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. 2012 Feb 8;287(17):14099–14108. doi: 10.1074/jbc.M111.334904

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© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 3. — Structure of KlenTaq_F-T (yellow). A, stabilization network of ddTTP. The amino acid side chains Arg-587, Phe-667, and Tyr-671 are labeled. Gray and black dashed lines indicate hydrogen-bonding interactions and distance (Å), respectively. B, the O helices from the superimposition of KlenTaq_F-T (yellow), KlenTaq_F-A (purple), KlenTaq_A-T (magenta), and KlenTaq_binary (gold) are highlighted. C, the incoming ddNTPs of KlenTaq_F-T (yellow), KlenTaq_F-A (purple), and KlenTaq_A-T (berry) and the respective 3′-primer terminus are shown. The arrow indicates the displacement of the α-phosphate regarding the 3′-primer terminus.