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Additional Supporting Information may be found in the online version of this article.

FilenameFormatSizeDescription
PROT_23191_sm_suppinfofig1.tif1910KSupporting Information Figure S1: Backbone dynamics of gp17. (A) 15N longitudinal relaxation rates R1, (B) 15N transverse relaxation rates R2 and (C) 1H[RIGHTWARDS ARROW]15N NOEs are plotted as a function of the sequence.
PROT_23191_sm_suppinfofig2.tif5427KSupporting Information Figure S2: Amino acid sequence conservation within the gp17 (top) and gpU (bottom) protein families. Sequence alignments of gp17 and gpU with 10 homolog representatives (identified by their GI numbers) are shown. Conserved buried residues are boxed in green and conserved solvent exposed residues are boxed in orange. Secondary structure representations of gp17 NMR solution structure and gpU NMR and X-ray structures are plotted. Secondary structures elements are labeled; α-helices are colored in red and β-sheets in blue.

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