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. 2019 Feb 5;14(2):e0211432. doi: 10.1371/journal.pone.0211432

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© 2019 Salazar et al

This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig 6 — Surface rendering of R1 and R2-NTF structures with solvent accessible R-subtype polymorphism (SARP) associated residues highlighted. SARP residue patches in regions of negative curvature reveal putative receptor binding interaction sites (green arrows). (A) R2-NTF structure with surface residues different between all R-subtype pyocin tail fibers (red) and residues different only between R1 and R2-subtype pyocin tail fibers (orange) are highlighted; (top) Lateral view rotated 60^o, (bottom) Distal view along central axis. (B) R1-NTF structure with surface residues different between all R pyocin tail fiber subtypes (red) and residues different only between R1 and R2-subtype pyocin tail fibers (orange) are highlighted; (top) Lateral view rotated 60^o, (bottom) Distal view along central axis.