Published in

Springer (part of Springer Nature), Journal of Biomolecular NMR, 3(50), p. 263-266

DOI: 10.1007/s10858-011-9514-4

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Protein–protein HADDocking using exclusively pseudocontact shifts

Journal article published in 2011 by Christophe Schmitz, Alexandre M. J. J. Bonvin ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

In order to enhance the structure determination process of macromolecular assemblies by NMR, we have implemented long-range pseudocontact shift (PCS) restraints into the data-driven protein docking package HADDOCK. We demonstrate the efficiency of the method on a synthetic, yet realistic case based on the lanthanide-labeled N-terminal ε domain of the E. coli DNA polymerase III (ε186) in complex with the HOT domain. Docking from the bound form of the two partners is swiftly executed (interface RMSDs