Proteinâ??protein HADDocking using exclusively pseudocontact shifts
 

Proteinâ??protein HADDocking using exclusively pseudocontact shifts


<div class="Abstract" lang="en">Abstract <div class="normal">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