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. 2017 Jan;23(1):98–107. doi: 10.1261/rna.058354.116

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© 2016 Yang 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 3. — Structural comparison of ScPcf11 538–608 with RING finger and LIM domain proteins. (A) Representative structure of ScPcf11 538–608 (upper) and topology representation (lower). The uncommon “petal” is colored in red. (B) Structure (upper) and topology diagram of a RING finger protein (pdb #1x4j). (C) Structure (upper) and topology diagram (lower) of a LIM protein (pdb #2o13). (D) Alignment of ScPcf11 538–608 (green) with 1x4j (wheat) and with 2o13 (salmon) based on their common structural elements, as described in the main text. (E) Backbone relaxation data of ScPcf11 538–608. Heteronuclear {¹H}–¹⁵N NOE values (top panel), ¹⁵N longitudinal relaxation rate constants R₁ (middle panel), and ¹⁵N transverse relaxation rate constants R₂ (bottom panel) plotted as a function of residue number. Corresponding secondary structures are presented on the top as a column for α helix and an arrow for β strand.