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. 2016 Feb 29;12(2):e1005885. doi: 10.1371/journal.pgen.1005885

Fig 4. Computational and experimental stability analysis of EphA3 WT and extended R-spine mutants.

Fig 4

A) Local stability analysis of EphA3 WT and mutants shown by fluctuations in side-chain conformation of R-spine-Asp. Each point corresponds to a snapshot taken at an interval of 20ps from a 200ns MD simulation trajectory. B) Global stability analysis of R-spine and ATP binding pocket in EphA3 WT and the extended R-spine network mutants. In each of the panels, the ATP binding site is shown in cyan, the R-spine residues are shown in orange, and the PTK-conserved residues are shown in green. For each panel, the number of clusters obtained at a clustering cutoff of 0.9 Angstroms is shown. Shown in the figure is a structural alignment of cluster centers obtained at the clustering cutoff. C) Thermal stability change of EphA3 and mutants are shown as histograms. Changes in Tm were calculated by subtracting Tm value of WT from Tm value of mutant. The mutants are grouped by single and double mutants, and single and double mutants with the addition of STK-histidine are shown as +S738H). The Tm values were calculated from triplicates, with standard deviations indicated above the histogram.