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. 2018 Sep 20;46(20):10840–10854. doi: 10.1093/nar/gky848

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© The Author(s) 2018. 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 2. — The structure, folding topology and sequence analysis of the CSFV NS5B NTD. (A) Stereo-pair images of the NTD with 3500 K composite SA-omit electron density map (contoured at 1.2σ) overlaid. (B) Topology of the CSFV NS5B NTD. The α-helix and β-strand labeling in panels A and B is based on secondary structure assignment by DSSP (68). (C) The sequence alignment of the pestiviruses NS5B NTD, linker and the RdRP regions that interact with NTD. The symbols of NTD α-helices (cylinders) and β-strands (block arrows) are plotted based on the secondary structure assignment of the CSFV NS5B structure. Two key residues involved in the intra-molecular of NTD–RdRP interactions and chosen for mutagenesis are indicated by asterisks. UniProtKB accession numbers of the pestivirus NS5B sequences used: Q5U8X5 (CSFV), X2KMP2 (BDV), P19711 (BVDV-1) and A0A0M4S9G5 (BVDV-2).