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. 2019 Feb 17;8(1):262–271. doi: 10.1080/22221751.2019.1575700

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© 2019 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group

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 use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — Position of polymerase complex substitutions that show large effects on polymerase activity in human cells. (A) Location of all substitutions showing an increase in polymerase activity of over 5 fold are shown of the molecular structure of the influenza A polymerase complex (PDB 4WSB). The substitutions that resulted in substantial activity increases can be divided into two groups: (1) sites on the complex surface (PB2-L183S, G74R, PB2-Q507R, PB2-F323 V, PB1-P596S, PB1-L598P, PB2-K526R, PA-L336M) and (2) sites at subunit interfaces: PB1 C-terminus and PA endonuclease domains (PB1-720, PB1-724, PA-94, PA-86) and the PB1 C-terminus and PB2 N-terminus domains (PB2-73, PB1-696, PB2-100, PB2-112, PB1-674) as shown in panel (B).