Journal of Biomolecular NMR

, Volume 62, Issue 1, pp 81–95 | Cite as

Systematic evaluation of combined automated NOE assignment and structure calculation with CYANA

  • Lena Buchner
  • Peter GüntertEmail author


The automated assignment of NOESY cross peaks has become a fundamental technique for NMR protein structure analysis. A widely used algorithm for this purpose is implemented in the program CYANA. It has been used for a large number of structure determinations of proteins in solution but a systematic evaluation of its performance has not yet been reported. In this paper we systematically analyze the reliability of combined automated NOESY assignment and structure calculation with CYANA under a variety of conditions on the basis of the experimental NMR data sets of ten proteins. To evaluate the robustness of the algorithm, the original high-quality experimental data sets were modified in different ways to simulate the effect of data imperfections, i.e. incomplete or erroneous chemical shift assignments, missing NOESY cross peaks, inaccurate peak positions, inaccurate peak intensities, lower dimensionality NOESY spectra, and higher tolerances for the matching of chemical shifts and peak positions. The results show that the algorithm is remarkably robust with regard to imperfections of the NOESY peak lists and the chemical shift tolerances but susceptible to lacking or erroneous resonance assignments, in particular for nuclei that are involved in many NOESY cross peaks.


Automated assignment NOESY Distance restraints Structure calculation CYANA 



We gratefully acknowledge financial support by the Lichtenberg program of the Volkswagen Foundation and a Grant-in-Aid for Scientific Research of the Japan Society for the Promotion of Science (JSPS).

Supplementary material

10858_2015_9921_MOESM1_ESM.docx (2.1 mb)
Supplementary material 1 (DOCX 2146 kb)


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Copyright information

© Springer Science+Business Media Dordrecht 2015

Authors and Affiliations

  1. 1.Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, and Frankfurt Institute of Advanced StudiesGoethe University Frankfurt am MainFrankfurt am MainGermany
  2. 2.Laboratory of Physical ChemistryETH ZürichZurichSwitzerland
  3. 3.Graduate School of ScienceTokyo Metropolitan UniversityHachiojiJapan

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