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. 2020 Feb 4;48(6):3343–3355. doi: 10.1093/nar/gkaa071

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© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — The nucleotide hydrolysis and DNA-unwinding activities of NrS-1 polymerase. (A) Surface presentation of the helicase domain of NrS-1 polymerase. Residues with positive charge and negative charge are colored in blue and red, respectively. (B) Cartoon view of the helicase domain of NrS-1 polymerase. The phosphate ions bound at the Walker A motifs are shown as spheres. (C) Detailed interactions between the phosphate group and the Walker A motif of NrS-1 helicase domain. The 2F_o− F_c electron density maps are contoured at 1.5 sigma level. (D) Analysis of the nucleotide hydrolysis activity of WT NrS-1 polymerase. (E) Time-course analysis of the dCTPase activity of NrS-1 polymerase. (F) In vitro DNA-unwinding assays catalyzed by WT NrS-1 polymerase.