unique NMR experiments. Often the pulse sequence used and the acquisition parameter ﬁles are available for the experiments. In some cases, processing parameters and peak lists have been provided along with the experimental parameters. Three of the entries, those corresponding to references [(36–38); BMRB accession codes 6128, 6176 and 6318] contain the full input and output data sets for the software used to derive the peaklists, automated peak assignments, NOE peak lists and restraints used to calculate the 3D structures of the proteins studied. Educational resources BMRB contains educational resources for NMR spectro- scopists and software programmers interested in probing the archive. A special section of the BMRB website highlights biomolecules that have been studied extensively by NMR spectroscopy. A brief description of each molecule is given, along with its historical signiﬁcance and links to associated BMRB and PDB entries and literature references. ACKNOWLEDGEMENTS We gratefully acknowledge our many fruitful interactions with members of the scientiﬁc community and, in particular, Wim Vranken in developing the NMR Restraints Grid, the PDB, the Protein Data Bank Japan (PDBj), the National Magnetic Resonance Facility at Madison (NMRFAM), the Collaborative Computational Program on NMR (CCPN), the European Bioinformatics Institute (EBI) and the Condor team. This work was funded by National Library of Medicine, National Institutes of Health (LM05799). Funding to pay the Open Access publication charges for this article was provided by the National Library of Medicine, National Institutes of Health (LM05799). Conﬂict of interest statement. None declared. REFERENCES 1. Pervushin,K.V., Riek,R., Wider,G. and Wu¨ thrich,K. (1998) Transverse relaxation-optimized spectroscopy (TROSY) for NMR studies of aromatic spin systems in 13C-labeled proteins. J. Am. Chem. Soc., 120, 6394–6400. 2. Pervushin,K.V., Wider,G. and Wu¨ thrich,K. 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