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Supported Applications

RASPnmr

  • Description

    (Protein NMR backbone resonance assignment) uses structure-based chemical shift predictions to solve the backbone resonance assignment problem in protein NMR spectroscopy. This enables rapid determination of highly accurate assignments on the basis of minimal experimental datasets, even for spectroscopically challenging proteins.

    RASP takes as input spin systems assembled on the basis of an arbitrary set of conventional triple-resonance NMR experiments. Uniquely, RASP is capable of extensive assignments even in the abscence of Cbeta chemical shift information: over a test set of 154 proteins RASP assigns 88 % of residues with an accuracy of 99.7 %, using only information available from HNCO and HNCA spectra.

  • Primary Citation*

    C. A. MacRaild and R. S. Norton. 2014. RASP: Rapid and robust backbone chemical shift assignments from protein structure. Journal of Biomolecular NMR. 58(3): 155-163.


    • *Full citation information available through

  • Categories

    NMR

  • Default Versions

    Linux 64:  0.1
    OS X INTEL:  RASP-0.1

  • Developers

    Christopher MacRaild, Raymond Norton.

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