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. 2016 Mar 8;23(2):135–143. doi: 10.1093/dnares/dsw003

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© The Author 2016. Published by Oxford University Press on behalf of Kazusa DNA Research Institute.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 3. — Amino acid residues under diversifying selection mapped on structural models. Residues under diversifying selection (dN/dS > 1) in H. pylori proteins are shown as red spheres, and those interacting with any ligand in homologous proteins are shown as yellow spheres. (A) WaaC (HP0279). Red sphere, Y229. (B) RecB (HP1553). Red spheres, L680 and R681. (C) HsdS (Type I S subunit) (HP0462). Red spheres, 153, 158, 159, 163, 166, 177, 180, 188, 190, 198, and 346. (D) HsdS (Type I S subunit) (HP0790). The 44 positions shown in red correspond to the codons under diversifying selection.