PROCHECK-NMR Operating Manual

Sample plots

NOTE: The examples come from an early stage of refinement and deliberately show more restraint violations than in the final published coordinates.

The model-selection option has been used to give only the first 5 of the 25 models in the file.

Each example contains a brief Description of the plot and the main Options that can be selected via the parameter file, procheck_nmr.prm. By clicking on the plot example you will get a full-size version of the illustration.

Note that the asterisked plots below are switched off in the default parameter file, procheck_nmr.prm, and so will not normally be produced unless you edit the file and switch those plots back on (see Which plots to produce).

• a. Geometry plots
  • 1. Ramachandran plot
  • 2. Gly & Pro Ramachandran plots
  • 3. Chi1-Chi2 plots*
  • 4. Residue Phi torsion angle plots*
  • 5. Residue Psi torsion angle plots*
  • 6. Residue Chi-1 plots
  • 7. Residue Chi-2 plots
  • 8. Residue Ramachandran plots
  • 9. Residue chi1-chi2 plots*
  • 10. Ensemble geometry
  • 11. Equivalent resolution
  • 12. Model-by-model secondary structures

• b. Restraint analyses
  • 13. Distance restraints plot
  • 14. Restraint differences plot
  • 15. Numbers of distance restraints
  • 16. Actual distance - restraint summary
  • 17. Violation frequency summary
  • 18. Restraint statistics
  • 19. Restraint spans*
  • 20. Residue-by-residue restraint violations
  • 21. Model-by-model violations

Reference

Vis H, Mariani M, Vorgias C E, Wilson K S, Kaptein R & Boelens R (1995). Solution structure of the HU protein from Bacillus stearothermophilus. J. Mol. Biol., 254, 692-703.

PROCHECK-NMR Operating Manual