Quality assessment for molecular models: Difference between revisions
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==NMR Models== | ==NMR Models== | ||
Models resulting from [[NMR Ensembles of Models|solution NMR experiments]] account for about 15% of those published in the [[Protein Data Bank]]. These are generally less reliable than crystallographic models because the method yields less detailed information. For NMR, there are no widely reported global error estimates equivalent to the crystallographic [[R value]] and [[Free R]]. Unlike with crystallographic results, it is not possible to distinguish reliable from unreliable NMR models from information included in the PDB files. NMR models are more likely to contain major errors <ref>Traditional biomolecular structure determination by NMR spectroscopy allows for major errors. Sander B. Nabuurs, Chris. A. E. M. Spronk, Geerten W. Vuister, and Gert Vriend. (2006). PLoS Computational Biology 2: [http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0020009 Open Access Full Text] [http://proteinexplorer.org/favlit/nmr.htm Precis]. DOI: 10.1371/journal.pcbi.0020009</ref> than are crystallographic models that have good [[Resolution]] and [[Free R]] values. At least one rapid approach | Models resulting from [[NMR Ensembles of Models|solution NMR experiments]] account for about 15% of those published in the [[Protein Data Bank]]. These are generally less reliable than crystallographic models because the method yields less detailed information. For NMR, there are no widely reported global error estimates equivalent to the crystallographic [[R value]] and [[Free R]]. Unlike with crystallographic results, it is not possible to distinguish reliable from unreliable NMR models from information included in the PDB files. NMR models are more likely to contain major errors <ref>Traditional biomolecular structure determination by NMR spectroscopy allows for major errors. Sander B. Nabuurs, Chris. A. E. M. Spronk, Geerten W. Vuister, and Gert Vriend. (2006). PLoS Computational Biology 2: [http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0020009 Open Access Full Text] [http://proteinexplorer.org/favlit/nmr.htm Precis]. DOI: 10.1371/journal.pcbi.0020009</ref> than are crystallographic models that have good [[Resolution]] and [[Free R]] values. At least one rapid approach <ref>PMID: 23779148</ref> has been introduced to avoid misassignments, as summarized [http://www.rsc.org/chemistryworld/2013/06/nmr-misassignments-spreadsheet-artificial-neural-networks here]. | ||
==Global vs. Local Quality== | ==Global vs. Local Quality== | ||