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. 2008 Jul 24;105(30):10366–10371. doi: 10.1073/pnas.0800405105

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© 2008 by The National Academy of Sciences of the USA

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Fig. 6. — ¹³C¹H_x recoupled dipolar spectra for residues Arg-44 and Lys-45. Arg-44 (¹³C¹H)α experimental data (Top Left) were simulated (Top, Right) best with 〈S〉 = 0.99 ± 0.04. Arg-44 (¹³C¹H₂)β experimental data (Second from Top, Left) were simulated (Second from Top, Right) best with 〈S〉 = 0.65 ± 0.04. Lys-45 (¹³C¹H)α experimental data (Third from Top, Left) were simulated (Third from Top, Right) best with 〈S〉 = 1.02 ± 0.04. Lys-45 (¹³C¹H₂)β experimental data (Fourth from Top, Left) were simulated (Fourth from Top, Right) best with 〈S〉 = 0.63 ± 0.04. Lys-45 (¹³C¹H₂)γ experimental data (Bottom Left) were simulated (Bottom Right) best with 〈S〉 = 0.28 ± 0.04. The simulated spectra were fit against the experimental spectra in the 2.3- to 10.8-kHz frequency range, and the zero frequency region was not plotted. Both Arg-44 and Lys-45 C-terminal residues have essentially staic protein backbones, but they have highly mobile side chains.