File:Ramachandran Gly Pro data and contours T8000 small.jpg
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Summary
Ramachandran plots (phi, psi backbone torsion angles) for glycine (left) and for trans proline (right). Datapoints from the "Top8000" crystal-structure chains with both resolution and MolProbity score <2.0, non-redundant at the PDB's 70% clusters, and each point with backbone B-factors ≤30. Inner contour encloses 98% of this high-quality data (favored region); outer contour encloses 99.9% (allowed) and excludes 0.1% (outlier or disallowed region). Methodology from [1] and [2].
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- ↑ Lovell SC, Davis IW, Arendall WB 3rd, de Bakker PI, Word JM, Prisant MG, Richardson JS, Richardson DC. Structure validation by Calpha geometry: phi,psi and Cbeta deviation. Proteins. 2003 Feb 15;50(3):437-50. PMID:12557186 doi:10.1002/prot.10286
- ↑ Read RJ, Adams PD, Arendall WB 3rd, Brunger AT, Emsley P, Joosten RP, Kleywegt GJ, Krissinel EB, Lutteke T, Otwinowski Z, Perrakis A, Richardson JS, Sheffler WH, Smith JL, Tickle IJ, Vriend G, Zwart PH. A new generation of crystallographic validation tools for the protein data bank. Structure. 2011 Oct 12;19(10):1395-412. PMID:22000512 doi:10.1016/j.str.2011.08.006
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 15:28, 8 June 2012 | 2,520 × 1,341 (1.34 MB) | Jane S. Richardson (talk | contribs) | Ramachandran plots (phi, psi backbone torsion angles) for glycine (left) and for trans proline (right). Datapoints from the "Top8000" crystal-structure chains with both resolution and MolProbity score <2.0, non-redundant at the PDB's 70% clusters, and ea |
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