Figure 21.3.5.2

Dym, O.; Eisenberg, D.; Yeates, T. O.

doi:10.1107/97809553602060000709

International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

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International Tables for Crystallography (2006). Vol. F. ch. 21.3, p. 523 | 1 | 2 |

Figure 21.3.5.2

O. Dym,^a D. Eisenberg^b ^* and T. O. Yeates^c

^aUCLA–DOE Laboratory of Structural Biology and Molecular Medicine, UCLA, Box 951570, Los Angeles, CA 90095-1570, USA, ^bUCLA–DOE Laboratory of Structural Biology and Molecular Medicine, Department of Chemistry & Biochemistry, Molecular Biology Institute and Department of Biological Chemistry, UCLA, Los Angeles, CA 90095-1570, USA, and ^cUCLA–DOE Laboratory of Structural Biology and Molecular Medicine, Department of Chemistry & Biochemistry and Molecular Biology Institute, UCLA, Los Angeles, CA 90095-1569, USA
Correspondence e-mail: david@mbi.ucla.edu

Figure 21.3.5.2

The detection of model errors due to refinement in an incorrect space group: an example (3xia.coor) from the archive of obsolete PDB entries. (a) ERRAT plot of the error function in a nine-residue sliding window. The solid bold line represents the revised structure and the dashed line represents the original structure. The thin solid lines indicate the 95% and 99% confidence limits for rejection. (b) VERIFY3D profile-window plots for the revised (bold) and original (dashed) models. The vertical axis gives the average 3D–1D score for residues within a 21-residue sliding window. (c) Ramachandran diagram of the original structure. All non-glycine residues outside the allowed regions are marked. (d) Ramachandran diagram for the revised structure.