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The WeNMR (http://www.wenmr.eu) project is an EU-funded international effort to streamline and automate structure determination from Nuclear Magnetic Resonance (NMR) data. Conventionally calculation of structure requires the use of various softwares, considerable user expertise and ample computational resources. To facilitate the use of NMR spectroscopy in life sciences the eNMR/WeNMR consortium has set out to provide protocolized services through easy-to-use web interfaces, while still retaining sufficient flexibility to handle more specific requests. Thus far, a number of programs often used in Structural Biology have been made available through portals, including HADDOCK, XPLOR-NIH, CYANA and CS-ROSETTA, MARS, MDDNMR. The implementation of these services, in particular the distribution of calculations to the Grid, involves a novel mechanism for submission and handling of jobs that is independent of the type of job being run. With over 280 registered users (April 2011), eNMR/WeNMR is currently one of the largest Virtual Organization (VO) in life sciences. With its large and worldwide user community, WeNMR has become the first Virtual Research Community officially recognized by the European Grid Infrastructure (EGI)

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

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 e domain of the E. coli DNA polymerase III (e186) in complex with the HOT domain. Docking from the bound form of the two partners is swiftly executed (interface RMSDs