Title of article - Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3.
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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Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, Vladimir-Prelog-Weg 2, ETH-Hönggerberg, CH-8093 Zürich, Switzerland.
Details of Journal for Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3.
Journal Title - Data in brief
ISSN - 2352-3409
Volume - 5
Issue - 0
Publish date - 2015-Dec
Language - eng
Country - Netherlands
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