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. 2013 Jan 7;110(4):1327–1332. doi: 10.1073/pnas.1207518110

Fig. 4.

Fig. 4.

Representations of UBL domains with residues colored white to red in eight shaded increments of increasing normalized 1H/15N chemical shift perturbations observed in the presence of the equivalent SGT. Residues greater than 80% of maximum chemical shift are colored the darkest red. Between 0% and 80% are divided equally across the seven remaining shades. (A) Ribbon and (B) surface views of Get5_UBL binding interface with Sgt2_NT; (C) ribbon and (D) surface views of Ubl4a_UBL binding interface with Sgta_NT; (E) surface views of UBL domains from Get5 (Upper) and Ubl4a (Lower) colored by electrostatics; (F) structure-based sequence alignment of the UBL domains from Get5 (Upper) and Ubl4a (Lower). Red, α-helix; blue, β-strand; yellow, η-helix; green, residues perturbed upon binding to equivalent SGT protein.