CING (biomolecular NMR structure)
NMR spectroscopy provides diverse data on the solution structure of biomolecules. CING combines many external programs and internalized algorithms to direct an author of a new structure or a biochemist interested in an existing structure to regions of the molecule that might be problematic in relation to the experimental data.
- 9000+ validation reports for existing Protein Data Bank structures in NRG-CING.
- CING has been applied to automatic predictions in the CASD-NMR experiment with results available at CASD-NMR.
Validated NMR data
- Protein or Nucleic acid structure together called Biomolecular structure
- Chemical shift
- (Nuclear Overhauser effect) Distance restraint
- Dihedral angle restraint
- RDC or Residual dipolar coupling restraint
- NMR (cross-)peak
Following software is used internally or externally by CING:
- 3DNA 
- Collaborative Computing Project for NMR
- CYANA (Software)
- DSSP (protein)
- MOLMOL 
- PROCHECK/Aqua 
- ShiftX 
- TALOS+ 
- WHAT_CHECK 
- Wattos 
The NRG-CING project was supported by the European Community grants 213010 (eNMR) and 261572 (WeNMR).
- Doreleijers, J. F.; Vranken, W. F.; Schulte, C.; Markley, J. L.; Ulrich, E. L.; Vriend, G.; Vuister, G. W. (2011). "NRG-CING: Integrated validation reports of remediated experimental biomolecular NMR data and coordinates in wwPDB". Nucleic Acids Research. 40 (Database issue): D519–D524. doi:10.1093/nar/gkr1134. PMC 3245154. PMID 22139937.
- CING; an integrated residue-based structure validation program suite, Jurgen F. Doreleijers Alan W. Sousa da Silva, Elmar Krieger, Sander B. Nabuurs, Chris Spronk, Tim Stevens, Wim F. Vranken, Gert Vriend, Geerten W. Vuister (to be submitted).
- Lu and Olson. 3DNA: a versatile, integrated software system for the analysis, rebuilding and visualization of three-dimensional nucleic-acid structures. Nature Protocols (2008) vol. 3 (7) pp. 1213-27
- Koradi et al. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph (1996) vol. 14 pp. 51-55
- Laskowski et al. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J Biomol NMR (1996) vol. 8 (4) pp. 477-486
- Neal et al. Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts. J Biomol NMR (2003) vol. 26 (3) pp. 215-240
- Shen et al. TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR (2009) vol. 44 (4) pp. 213-23
- Hooft et al. Errors in protein structures. Nature (1996) vol. 381 (6580) pp. 272-272
- Doreleijers, J. F.; Nederveen, A. J.; Vranken, W.; Lin, J.; Bonvin, A. M. J. J.; Kaptein, R.; Markley, J. L.; Ulrich, E. L. (2005). "BioMagResBank databases DOCR and FRED containing converted and filtered sets of experimental NMR restraints and coordinates from over 500 protein PDB structures". Journal of Biomolecular NMR. 32 (1): 1–12. doi:10.1007/s10858-005-2195-0. PMID 16041478.
- Kumar and Nussinov. Relationship between Ion Pair Geometries and Electrostatic Strengths in Proteins. Biophys.J. (2002) vol. 83 pp. 1595–1612
- Dombkowski and Crippen. Disulfide recognition in an optimized threading potential. Protein Engineering Design and Selection (2000) vol. 13 (10) pp. 679-689
- Ross. Peirce's criterion for the elimination of suspect experimental data. Journal of Engineering Technology (2003)