Binding mode of the activity-modulating C-terminal segment of NS2B to NS3 in the dengue virus NS2B–NS3 protease
Version of Record online: 12 FEB 2014
© 2014 FEBS
The FEBS Journal
Volume 281, Issue 6, pages 1517–1533, March 2014
How to Cite
de la Cruz, L., Chen, W.-N., Graham, B. and Otting, G. (2014), Binding mode of the activity-modulating C-terminal segment of NS2B to NS3 in the dengue virus NS2B–NS3 protease. The FEBS Journal, 281: 1517–1533. doi: 10.1111/febs.12729
- Issue online: 18 MAR 2014
- Version of Record online: 12 FEB 2014
- Accepted manuscript online: 29 JAN 2014 02:47AM EST
- Manuscript Accepted: 24 JAN 2014
- Manuscript Revised: 21 JAN 2014
- Manuscript Received: 27 NOV 2013
- Australian Research Council
Fig. S1. Sequence alignment of the NS2B–NS3pro in the dengue virus serotypes 1–4.
Fig. S2. Chemical structures of inhibitor 1 and C1 lanthanide tag.
Fig. S3. DENp is enzymatically active.
Fig. S4. 15N-HSQC spectrum of DENp selectively labelled with 15N-serine and 15N-isoleucine.
Fig. S5. 15N-HSQC spectra of DENp selectively labelled with 15N-isoleucine at different ionic strengths.
Fig. S6. PCSs observed for NS2B of DENp at 50 mm and 300 mm NaCl.
Fig. S7. Correlations between back-calculated and experimental PCSs of DENp at low and high salt.
Table S1. PCSs of backbone amide protons of 15N-labelled DENp mutant B with C2 tag loaded with Tb3+ at 50 mm and 300 mm NaCl concentrations.
Table S2. Δχ tensor parameters of DENp mutant B with C2–Tb3+ tag.
Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.