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. 2005 May;79(10):6134–6141. doi: 10.1128/JVI.79.10.6134-6141.2005

FIG. 5.

FIG. 5.

Structural model of wild-type gH tail peptide at 10°C. The nine lowest-energy structures are superimposed. Residues 1 to 3 and residues 11 to 14 are highly disordered and were omitted for clarity. The backbone is colored blue, and the side chains are colored red, with the exception of those of Val7, Pro8, and Phe10, which are highlighted in green.