Supplemental Data Ubiquitin Recognition by the Human TSG101 Protein

Comparison of the crystal structure with previously published NMR chemical shift perturbation data strongly supports the relevance of the crystallographic interface. The fi gure shows the same surface representations as Figure 2A, B, and C, of the manuscript. Residues that show change in their solvent accessible surface area are colored blue. Residues that show signifi cant perturbation in chemical shift are colored yellow. (Residues that show changes in both surface area and chemical shift are colored green.) As shown, all 16 of the ubiquitin residues that show signifi cant chemical shift perturbation also lie at the interface. Of the 13 UEV residues that show signifi cant chemical shift perturbation, only two (Leu39 and Asp40; yellow) do not loose solvent accessible surface upon complex formation. There are two possible explanations for the relatively large chemical shift changes shown by Leu39 and Asp40. First, they are close to Tyr42 and Trp75, both of which likel