Module 2

Residual dipolar coupling and residual chemical shift analysis software
Patrice Dosset and Martin Blackledge

This development was funded by the European Union under the EUNMR project as part of the Joint Research Activity ORIENTING NMR, project number : RII3-026145

Presentation

Version 2 of the program MODULE designed to analyze residual dipolar couplings and residual chemical shifts measured in partially aligned proteins and nucleic acids.
Analysis of residual anisotropic interactions measured in proteins and nucleic acids aligned in dilute liquid crystalline media.
Version 2

  • Allows for the analysis of residual chemical shifts due to non-averaged chemical shift anisotropy.
  • Allows for the analysis and comparison of multiple data sets measured for the same molecule.
  • Allows for output of fitted data into external files (bug-fix).
  • Allows for cursor selection of RDC/RCS between peptide units aswell as within peptide units.

The executable is currently working for Linux machines.

The license is free for academic sites and non commercial use

References

If any results obtained with the MODULE program are published, whatever the means of publication, particularly in the scientific literature, the program should be referenced in the following way:

Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data. Dosset, P.; Hus, J-C; Blackledge, M.; Marion, D. J.Biomol.NMR. 2000, 16: 23-28.

Documentation

Downloaded with the executable

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