Journal of Biomolecular NMR

, Volume 1, Issue 2, pp 111–130 | Cite as

Efficient analysis of protein 2D NMR spectra using the software packageEASY

  • Craig Eccles
  • Peter Güntert
  • Martin Billeter
  • Kurt Wüthrich
Research Papers


The programEASY supports the spectral analysis of biomacromolecular two-dimensional (2D) nuclear magnetic resonance (NMR) data. It provides a user-friendly, window-based environment in which to view spectra for interactive interpretation. In addition, it includes a number of automated routines for peakpicking, spin-system identification, sequential resonance assignment in polypeptide chains, and cross peak integration. In this uniform environment, all resulting parameter lists can be recorded on disk, so that the paper plots and handwritten notes which normally accompany manual assignment of spectra can be largely eliminated. For example, in a protein structure determination by 2D1H NMR,EASY accepts the frequency domain datasets as input, and after combined use of the automated and interactive routines it can yield a listing of conformational constraints in the format required as input for the calculation of the 3D structure. The program was extensively tested with current protein structure determinations in our laboratory. In this paper, its main features are illustrated with data on the protein basic pancreatic trypsin inhibitor.


Nuclear magnetic resonance Protein structure determination Automated spectral analysis Software packageEASY Sequence-specific assignments 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Billeter, M., Braun, W. and Wüthrich, K. (1982).J. Mol. Biol. 155, 321–346.CrossRefPubMedGoogle Scholar
  2. Billeter, M., Basus, V.J. and Kuntz, I.D. (1988)J. Magn. Reson.,76, 400–415.Google Scholar
  3. Braun, W. (1987)Q. Rev. Biophys.,19, 115–157.PubMedGoogle Scholar
  4. Cieslar, C., Clore, G.M. and Gronenborn, A.M. (1988).J. Magn. Reson.,80, 119–127.Google Scholar
  5. Clore, G.M. and Gronenborn, A.M. (1989)CRC Crit. Rev. Biochem. Mol. Biol. 24, 479–564.Google Scholar
  6. Denk, W., Baumann, R. and Wagner, G. (1986)J. Magn. Reson.,67, 386–390.Google Scholar
  7. Deisenhofer, J. and Steigemann, W. (1975)Acta Crystallogr. sect. B 31, 238–250.Google Scholar
  8. Eads, C.D. and Kuntz, I.D. (1989)J. Magn. Reson. 82, 467–482.Google Scholar
  9. Glaser, S. and Kalbitzer, H.R. (1987)J. Magn. Reson.,74, 450–463.Google Scholar
  10. Güntert, P., Braun, W., Billeter, M. and Wüthrich, K. (1989)J. Am. Chem. Soc.,111, 3997–4004.Google Scholar
  11. Güntert, P., Braun, W. and Wüthrich, K. (1991)J. Mol. Biol.,217, 517–530.PubMedGoogle Scholar
  12. Hoch, J.C., Hengyi, S., Kjær, M., Ludvigsen, S. and Poulsen, F.M. (1987)Calsberg Res. Commun.,52, 111–122.Google Scholar
  13. Holak, T.A., Scarsdale, J.N. and Prestegard, J.H. (1987).J. Magn. Reson.,74, 546–549.Google Scholar
  14. Kay, L.E., Clore, G.M., Bax, A. and Gronenborn, A.M. (1990).Science,249, 411–414.PubMedGoogle Scholar
  15. Kjær, M., Andersen, K.V., Ludvigsen, S., Hengyi, S., Madsen, J.C. and Poulsen, F.M. (1990)Abstracts XIV ICMRBS, Warwick, P3–21.Google Scholar
  16. Kleywegt, G.J., Lamerichs, R.M.J.N., Boelens, R. and Kaptein, R. (1989).J. Magn. Reson.,85, 186–197.Google Scholar
  17. Kraulis, P.J. (1989)J. Magn. Reson.,84, 627–633.Google Scholar
  18. Meier, B.U., Mádi, Z.L. and Ernst, R.R. (1987)J. Magn. Reson.,74, 565–673.Google Scholar
  19. Neidig, K.P., Bodenmüller, H. and Kalbitzer, H.R. (1984)Biochem. Biophys. Res. Comm.,125, 1143–1150.PubMedGoogle Scholar
  20. Oh, B.H., Westler, W.M., Darba, P. and Markley, J.L. (1988).Science,240, 908–911.PubMedGoogle Scholar
  21. Otting, G., Qian, Y.Q., Billeter, M., Müller, M., Affolter, M., Gehring, W.J. and Wüthrich, K. (1990)EMBO J.,9, 3085–3092.PubMedGoogle Scholar
  22. Pardi, A., Billeter, M. and Wüthrich, K. (1984).J. Mol. Biol.,180, 741–751.PubMedGoogle Scholar
  23. Pfändler, P., Bodenhausen, G., Meier, B.U. and Ernst, R.R. (1985)Anal. Chem. 57, 2510–2516.Google Scholar
  24. Press, W.H., Flannery, B.P., Teukolsky, S.A. and Vetterling, W.T. (1986).Numerical Recipes. The Art of Scientific Computing, Cambridge University Press, Cambridge, pp. 509–515.Google Scholar
  25. Stoven, V., Mikou, A., Piveteau, D., Guittet, E. and Lallemand, J.-Y. (1989)J. Magn. Reson.,86, 163–168.Google Scholar
  26. Van de Ven, F.J.M. (1990)J. Magn. Reson.,86, 633–644.Google Scholar
  27. Wagner, G. and Wüthrich, K. (1982).J. Mol. Biol.,155, 347–366.PubMedGoogle Scholar
  28. Wagner, G., Braun, W., Havel, T.F., Schaumann, T., Gö, N. and Wüthrich, K. (1987)J. Mol. Biol.,196, 611–639.PubMedGoogle Scholar
  29. Weber, P.L., Malikayil, J.A. and Müller, L. (1989)J. Magn. Reson.,82, 419–426.Google Scholar
  30. Wider, G., Lee, K.H. and Wüthrich, K. (1982).J. Mol. Biol.,155, 367–388.PubMedGoogle Scholar
  31. Wlodawer, A., Walter, J., Huber, R. and Sjölin, L. (1984)J. Mol. Biol.,180, 301–329.PubMedGoogle Scholar
  32. Wlodawer, A., Nachman, J., Gilliland, G.L., Gallagher, C. and Woodward, C. (1987)J. Mol. Biol.,198, 469–480.PubMedGoogle Scholar
  33. Wüthrich, K. (1986)Biopolymers,22, 131–138.Google Scholar
  34. Wüthrich, K. (1986)NMR of Proteins and Nucleic Acids, Wiley, New York.Google Scholar
  35. Wüthrich, K. (1989)Science,243, 45–50.PubMedGoogle Scholar
  36. Wüthrich, K., Billeter, M. and Braun, W. (1984)J. Mol. Biol.,180, 715–740.PubMedGoogle Scholar

Copyright information

© ESCOM Science Publishers B.V. 1991

Authors and Affiliations

  • Craig Eccles
    • 1
  • Peter Güntert
    • 1
  • Martin Billeter
    • 1
  • Kurt Wüthrich
    • 1
  1. 1.Institut für Molekularbiologie und BiophysikEtdgenössische Technische Hochschule-HönggerbergZürichSwitzerland

Personalised recommendations