Download MendeleyAutomated NMR resonance assignments and structure determination using a minimal set of 4D spectra.
Evangelidis, T., Nerli, S., Novacek, J., Brereton, A.E., Karplus, P.A., Dotas, R.R., Venditti, V., Sgourakis, N.G., Tripsianes, K.(2018) Nat Commun 9: 384-384
- PubMed: 29374165
- DOI: https://doi.org/10.1038/s41467-017-02592-z
- Primary Citation of Related Structures:
5WOT, 5WOX, 5WOY, 5WOZ - PubMed Abstract:
Automated methods for NMR structure determination of proteins are continuously becoming more robust. However, current methods addressing larger, more complex targets rely on analyzing 6-10 complementary spectra, suggesting the need for alternative approaches. Here, we describe 4D-CHAINS/autoNOE-Rosetta, a complete pipeline for NOE-driven structure determination of medium- to larger-sized proteins. The 4D-CHAINS algorithm analyzes two 4D spectra recorded using a single, fully protonated protein sample in an iterative ansatz where common NOEs between different spin systems supplement conventional through-bond connectivities to establish assignments of sidechain and backbone resonances at high levels of completeness and with a minimum error rate. The 4D-CHAINS assignments are then used to guide automated assignment of long-range NOEs and structure refinement in autoNOE-Rosetta. Our results on four targets ranging in size from 15.5 to 27.3 kDa illustrate that the structures of proteins can be determined accurately and in an unsupervised manner in a matter of days.
Organizational Affiliation:
CEITEC-Central European Institute of Technology, Masaryk University, Kamenice 5, Brno, 62500, Czech Republic.
