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. 2020 Dec;26(12):2031–2043. doi: 10.1261/rna.077354.120

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© 2020 Immer et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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FIGURE 2. — NMR solution structure and electrostatic surface features of Lpp1663. (A) Lpp1663 has a ProQ/FinO fold with five central helices that are connected by four structurally well-defined loops. Shown is an overlay of the 10 final structures with an rmsd of 0.4 Å (ordered residues) that were deposited in the PDB under accession number 6S10. (B) The {¹H}, ¹⁵N heteronuclear NOE of ¹⁵N-labeled Lpp1663 indicates the flexible amino- and carboxyl termini of the protein. Secondary structure elements are depicted by blue boxes. (C) The electrostatic surface potential of the lowest energy structure reveals two positively charged patches on either side of the protein, the concave and the convex site. Positive and negative charges are colored in blue and red. Amino- and carboxyl termini are indicated as N and C, respectively.