Monte uses a monte-carlo method to obtain the NMR assignments of
proteins. The program was originally designed for the assignment of
large deuterated proteins. However, the current version has
considerable functionality for the assignment of protonated proteins
as well. Monte has been used to successfully assign small (~15 KDa)
protonated proteins as well as large (~55 KDa) deuterated proteins. A
detailed description of Monte has recently been published in the
Journal of Biomolecular NMR:
- Hitchens, T.K., McCallum, S.A., and Rule, G.S. (2003) Data
requirements for reliable chemical shift assignments in deuterated
proteins. J. Biomol. NMR, 25, 11-23.
Hitchens, T.K., Lukin, J.A., Zhan, Y., McCallum, S.A., and Rule, G.S. (2003)
MONTE: An automated Monte Carlo based approach to nuclear magnetic resonance assignment of proteins.
J. Biomol NMR, 25, 1-9.
The main features of the program are as follows:
NMRVIEW users: An interface program, NvAssign, has been written by Geoff Mueller. The website for this package is: http://dir.niehs.nih.gov/dirnmr/nvassign/
- A graphical Tk/tcl interface for parameter entry
- Several forms of output, including:
- A HTML document that summarizes chemical shift matching
- A postscript summary of the assignments, including information on the reliability of the assignments.
- A correlation plot that readily provides information on possible alternative assignments.
- The program can use a wide variety of input data:
- Inter-residue scalar connectivities, e.g. from HNCA/HN(CO)CA, HN(CA)HA, etc.
- Amide-amide NOEs, both 3D data and 4D NOESY data can be used in the
assignment process. This information can be used in conjunction with the
known tertiary structure of the protein or as sequential NOEs.
- Information from 15N specific labels.
- Information from 13C carbonyl edited HNCO experiment when
samples are specifically labeled at the carbonyl position.
- Existing chemical shifts of another form of the protein. This feature is
particularly useful in the assignment of protein-ligand complexes if the
assignments of the unliganded form of the protein are known.
Documentation A brief manual is available in PDF format. This
document explains the existing features of the program and provides guidelines for using Monte.
You can download this document:
MONTE operation manual, v2.02 (PDF)
Obtaining Monte Monte is freeware for the academic/non-profit
community. Please keep in mind that the program is under development
and not necessarily bug-free. We are constantly trying to improve
the program in terms of bug-fixes as well as the addition of new
features. If you have found a bug, or have a suggestion for a new
feature, or an improvement on existing features, please do not
hesitate to write.
Monte currently runs on IRIX systems as well as Red Hat Linux running
on a PC. Links to Tar files for each of the distributions are located
Distribution for SGI IRIX 6.5
Distribution for (Redhat) Linux
Users who wish to obtain the source code for MONTE for the purposes
of compiling on other platforms should contact Dr. Rule.
Monte requires a valid license key in order to run. To obtain a key,
please fill out the posted license agreement:
License file in word format
License file in PDF format
You will need to fill in items at the top of the first page (date and
place of operation), in section 1 (email address), section 5 (complete
mailing address), section 6 (signature and date).
A guide to the completion of the license agreement, in PDF form, can be found here
Two copies of the completed license file should be mailed to:
Dr. Gordon S. Rule
Department of Biological Sciences
Carnegie Mellon University
4400 Fifth Ave
Pittsburgh, PA 15213
Alternatively, you can FAX one copy to: 412-268-7129. Please mark the FAX to my attention.