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. 2008 Jul 28;36(15):5074–5082. doi: 10.1093/nar/gkn489

Figure 1.

Figure 1.

Amino acid sequence of full-length ɛ. Residues 7–180 have a defined conformation in the crystal structure of ɛ186 (15). The 57 residues of the ɛCTS are highlighted in bold. Secondary structure prediction suggests an α-helical segment in the ɛCTS with high propensity; the corresponding residues are underlined. Alanine and threonine residues in the CTS of ɛ are highlighted in red and yellow, respectively.