Journal of Biomolecular NMR

, Volume 30, Issue 1, pp 11–23

Mars - robust automatic backbone assignment of proteins

  • Young-Sang Jung
  • Markus Zweckstetter
Article

DOI: 10.1023/B:JNMR.0000042954.99056.ad

Cite this article as:
Jung, YS. & Zweckstetter, M. J Biomol NMR (2004) 30: 11. doi:10.1023/B:JNMR.0000042954.99056.ad

Abstract

MARS a program for robust automatic backbone assignment of 13C/15N labeled proteins is presented. MARS does not require tight thresholds for establishing sequential connectivity or detailed adjustment of these thresholds and it can work with a wide variety of NMR experiments. Using only 13Cα/13Cβ connectivity information, MARS allows automatic, error-free assignment of 96% of the 370-residue maltose-binding protein. MARS can successfully be used when data are missing for a substantial portion of residues or for proteins with very high chemical shift degeneracy such as partially or fully unfolded proteins. Other sources of information, such as residue specific information or known assignments from a homologues protein, can be included into the assignment process. MARS exports its result in SPARKY format. This allows visual validation and integration of automated and manual assignment.

automated assignmentNMRsoftwarestructural genomicstriple resonanceunfolded protein

Copyright information

© Kluwer Academic Publishers 2004

Authors and Affiliations

  • Young-Sang Jung
    • 1
  • Markus Zweckstetter
    • 1
    • 1
  1. 1.Max Planck Institute for Biophysical ChemistryGöttingenGermany