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Figure 3.
Figure 3 NMR spectral perturbation study of various activation
states of EphB2 kinase. (A) Overlay of a representative region
of the ^1H,^15N-HSQC spectra of the auto-inhibited EphB2 JMS-KD
fragment (black) and the activated EphB2 KD fragment (blue). (B)
Residues experiencing spectral perturbations are mapped onto the
structure of the EphB2 JMS-KD as relative peak intensities with
a linear gradient from white (I/I[ref] than
or equal to 0.4) to blue (I/I[ref]=0). Spheres represent the
nitrogen atoms of affected residues. (C) As panel A, but for the
EphB2 JMS-KD fragment phosphorylated on residues Y604 and Y610
(red). (D) As panel B, but for the phospho-JMS-KD fragment using
a linear gradient from white to red. (E) As panel A, but for the
EphB2 Y750A JMS-KD mutant (green). (F) As panel B, but for the
EphB2 Y750A JMS-KD mutant using a linear gradient from white to
green. In all spectral overlays, residues exhibiting significant
spectral perturbations are labeled. JMS residues are underlined,
whereas residues in the activation segment are in italics.
Dotted lines indicate large chemical shift changes between the
phosphorylated and unphosphorylated EphB2 JMS-KD fragment,
whereas arrows highlight the positions of peaks appearing around
8.0 p.p.m. in the spectrum of the phosphorylated EphB2 JMS-KD.
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