bi5b01138_si_004.zip (43.01 MB)
Using Pseudocontact Shifts and Residual Dipolar Couplings as Exact NMR Restraints for the Determination of Protein Structural Ensembles
dataset
posted on 2015-12-29, 00:00 authored by Carlo Camilloni, Michele VendruscoloNuclear
magnetic resonance (NMR) spectroscopy provides detailed
information about the structure and dynamics of proteins by exploiting
the conformational dependence of the magnetic properties of certain
atomic nuclei. The mapping between NMR measurements and molecular
structures, however, often requires approximated descriptions based
on the fitting of a number of parameters, thus reducing the quality
of the information available from the experiments. To improve on this
limitation, we show here that it is possible to use pseudocontact
shifts and residual dipolar couplings as “exact” NMR
restraints. We implement this strategy by using a replica-averaging
method and illustrate its application by calculating an ensemble of
structures representing the dynamics of the two-domain protein calmodulin.