ArticleJournal of biomolecular NMR2015
Analysis of the performance of the CHESHIRE and YAPP methods at CASD-NMR round 3.
Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Enhancing coevolution-based contact prediction by imposing structural self-consistency of the contacts.Scientific reports · 2018Article
- A protocol for the refinement of NMR structures using simultaneously pseudocontact shift restraints from multiple lanthanide ions.Journal of biomolecular NMR · 2016Article
- Structure of the Bacterial Cytoskeleton Protein Bactofilin by NMR Chemical Shifts and Sequence Variation.Biophysical journal · 2016Article
- The second round of Critical Assessment of Automated Structure Determination of Proteins by NMR: CASD-NMR-2013.Journal of biomolecular NMR · 2015Article
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2 authors.
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Abstract
We present an analysis of the results obtained at CASD-NMR round 3 by the CHESHIRE and the YAPP methods. To determine protein structures, the CHESHIRE method uses solely information provided by NMR chemical shifts, while the YAPP method uses an automated assignment of NOESY spectra. Of the ten targets of CASD-NMR round 3, nine CHESHIRE predictions and eight YAPP ones were submitted. The eight YAPP predictions ranged from 0.7 to 1.9 Å Cα accuracy, with an average of 1.3 Å. The nine CHESHIRE predictions ranged from 0.8 to 2.6 Å Cα accuracy for the ordered regions of the proteins, with an average of 1.6 Å. Taken together, these results illustrate how the NOESY based YAPP method and the chemical shift based CHESHIRE method can provide structures of comparable quality.
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