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. 2014 Apr 22;15(4):6797–6814. doi: 10.3390/ijms15046797

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© 2014 by the authors; licensee MDPI, Basel, Switzerland

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Figure 3. — ERRAT plots for (A) NBD; (B) K71L and (C) T204V mutants. Black bars identify the misfolded region located distantly from the active site, gray bars demonstrate the error region between 95% and 99%, and white bars indicate the region with a lower error rate for protein folding. * On the error axis, two lines are drawn to indicate the confidence with which it is possible to reject regions that exceed that error value. ** Expressed as the percentage of the protein for which the calculated error value falls below the 95% rejection limit. Good high resolution structures generally produce values around 95% or higher. For lower resolutions (2.5 to 3 A) the average overall quality factor is around 91%.

Figure 3. — ERRAT plots for (A) NBD; (B) K71L and (C) T204V mutants. Black bars identify the misfolded region located distantly from the active site, gray bars demonstrate the error region between 95% and 99%, and white bars indicate the region with a lower error rate for protein folding. * On the error axis, two lines are drawn to indicate the confidence with which it is possible to reject regions that exceed that error value. ** Expressed as the percentage of the protein for which the calculated error value falls below the 95% rejection limit. Good high resolution structures generally produce values around 95% or higher. For lower resolutions (2.5 to 3 A) the average overall quality factor is around 91%.