Accuracy and precision of protein structures determined by magic angle spinning NMR spectroscopy: for some ‘with a little help from ... View Full Text


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Article Info

DATE

2019-03-07

AUTHORS

Ryan W. Russell, Matthew P. Fritz, Jodi Kraus, Caitlin M. Quinn, Tatyana Polenova, Angela M. Gronenborn

ABSTRACT

We present a systematic investigation into the attainable accuracy and precision of protein structures determined by heteronuclear magic angle spinning solid-state NMR for a set of four proteins of varied size and secondary structure content. Structures were calculated using synthetically generated random sets of C-C distances up to 7 Å at different degrees of completeness. For single-domain proteins, 9-15 restraints per residue are sufficient to derive an accurate model structure, while maximum accuracy and precision are reached with over 15 restraints per residue. For multi-domain proteins and protein assemblies, additional information on domain orientations, quaternary structure and/or protein shape is needed. As demonstrated for the HIV-1 capsid protein assembly, this can be accomplished by integrating MAS NMR with cryoEM data. In all cases, inclusion of TALOS-derived backbone torsion angles improves the accuracy for small number of restraints, while no further increases are noted for restraint completeness above 40%. In contrast, inclusion of TALOS-derived torsion angle restraints consistently increases the precision of the structural ensemble at all degrees of distance restraint completeness. More... »

PAGES

1-14

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s10858-019-00233-9

    DOI

    http://dx.doi.org/10.1007/s10858-019-00233-9

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1112607039

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/30847635


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