Solution Structure of MSL2 CXC Domain Reveals an Unusual Zn3Cys9 Cluster and Similarity to Pre-SET Domains of Histone Lysine Methyltransferases
Figure 6
Amide proton exchange experiments.
(A–C) 1H-15N HSQC spectra collected immediately (A), 2 h (B) or 24 h (C) after dissolving the lyophilized CXC-3 protein in 2H2O. The peaks are labeled and the side chain amide proton Hδ of N563 is labeled as N563D. (C) Intensity of amide proton peak as a function of exchange time. (D) Distribution of slow exchange amide protons in the CXC domain structure. The protected amide protons are shown as spheres on a backbone trace and are colored pink if present in the first recorded spectrum but not after 2 h, orange if present at 2 h but not after 24 h, and red if present after 24 h. The side chain of N563 is also displayed.