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Updated: Mar 31, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3
Beat Vögeli1, Simon Olsson2, Roland Riek1
1Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, Vladimir-Prelog-Weg 2, ETH-Hönggerberg, CH-8093 Zürich, Switzerland.
Abstract:
We compiled an NMR data set consisting of exact nuclear Overhauser enhancement (eNOE) distance limits, residual dipolar couplings (RDCs) and scalar (J) couplings for GB3, which forms one of the largest and most diverse data set for structural characterization of a protein to date. All data have small experimental errors, which are carefully estimated. We use the data in the research article Vogeli et al., 2015, Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics, J. Struct. Biol., 191, 3, 306-317, doi:10.1016/j.jsb.2015.07.008 [1] for cross-validation in multiple-state structural ensemble calculation. We advocate this set to be an ideal test case for molecular dynamics simulations and structure calculations.
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