Module

Module Version 1.0

Presentation

Module is a novel program developed to allow the determination of alignment tensor parameters for individual or multiple domains in macromolecules from residual dipolar couplings and to facilitate their manipulation to construct low-resolution models of macromolecular structure.
For multi-domain systems the program determines the relative orientation of individual structured domains, and provides graphical user-driven rigid-body modeling of the different modules relative to the common tensorial frame.
Translational freedom in the common frame, and equivalent rotations about the diagonalized (x,y,z) axes, are used to position the different modules in the common frame to find a model in best agreement with experimentally measured couplings alone or in combination with additional experimental or covalent information.

The program has been compiled for the following platforms :

• Mac OSX .
• PC Linux running Redhat 5.2 to 7 .
• PC Linux running Redhat 8 or 9 .
• Silicon Graphics running Irix 6.5 or higher.
• Sun Sparc running Solaris 2.6 or higher

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:

A Novel Interactive Tool for Rigid-Body Modeling of Multi-Domain Macromolecules using Residual Dipolar Couplings. Dosset, P.; Hus, J-C; Marion, D; Blackledge, M. J.Biomol.NMR. 20:223-231, July 2001.

Documentation

Downloaded with the executable

Download

Before downloading the software, you must read the license.
If you agree the license terms, you can download the software :

  version PC :

  version MAC :

Module 2

Residual dipolar coupling and residual chemical shift analysis software
Patrice Dosset and Martin Blackledge
Institut de Biologie Structurale
Grenoble

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

Download

Before downloading the software, you must read the license.
If you agree the license terms, you can download the software :

  version Linux :