Figure 1.

Ribbon diagrams indicating flexible segments of the Ves v 5 crystal structure[53]. Colored portions indicate regions of above-average flexibility as measured by crystallographic B-factors (A), solvent-accessible surface (B), COREX residue stability (C), and sequence entropy (D). Space-filled atoms correspond to disulfide-bonded cysteine residues. Numbers indicate the positions of residues near the centers of flexible sites.

Melton and Landry Clinical and Molecular Allergy 2008 6:9   doi:10.1186/1476-7961-6-9
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