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The current paradigm for protein structure determination by NMR spectroscopyhas thus far been based on collecting distance restrains between pairs ofnuclei in the form of nuclear Overhauser enhancements (NOE). These, have insome circumstances been supplemented with other information sources such asparamagnetic relaxation enhancements or residual dipolar couplings. Here, wereport for the first time a protein structure determination by NMR without theuse of NOEs. The protein PioC from Rhodopseu-domonas palustris TIE-1 is anHIPIP where the 4Fe4S cluster is paramagnetic and provides the source ofParamagnetic Relaxation Enhancements (PRE) used as alternative distanceconstraints. Comparison of the family of structures obtained by NOE structuralrestraints, with that obtained by PRE and with the family of structuresobtained by combining NOEs and PREs reveals that the pairwise RMSD between themare similar and comparable with the precision within each family. This worksets the stage for the structural characterization of small and dynamicparamagnetic metalloproteins opening a new paradigm in the use of NMR instructural biology.

NOE-less protein structures-an alternative paradigm in Highly Paramagnetic Systems