Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide -- Data Supplement - Supporting Figure -- Proceedings of the National Academy of Sciences

Supporting information for Donaldson et al. (2002) Proc. Natl. Acad. Sci. USA, 10.1073/pnas.212518799

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Fig. 5.
Dynamics of the Crk SH2 domain within the ternary complex. (Top) Amide ¹⁵N-T₁ values. (Middle) Amide ¹⁵N-T₂ values. (Bottom) Heteronuclear ¹H{¹⁵N}-NOE enhancements. The average errors in the ¹⁵N-T₁, ¹⁵N-T₂, and heteronuclear NOE measurements are 1.73 ± 0.8%, 2.09 ± 0.93%, and 1.41 ± 0.55%, respectively. Secondary structure elements are labeled at the top following the standard nomenclature for SH2 domains.