announcing normal mode analysis web server ElNemo

Karsten karsten_suhre at yahoo.fr
Tue Oct 5 11:28:36 EST 2004

I am pleased to announce our new protein normal mode 
analysis web-server ElNemo:


A paper describing its functions has just been published in the NAR web-server 
issue (see abstract below):

http://nar.oupjournals.org/cgi/content/full/32/suppl_2/W610 (This paper is 
open access)

I hope that you will find this web server useful and would begrateful for any 
comments or suggestions,

Kind regards,



Karsten Suhre and Yves-Henri Sanejouand

ElNémo: a normal mode web server for protein movement analysis and the 
generation of templates for molecular replacement

Nucleic Acids Research, 32, W610-W614, 2004.

Normal mode analysis (NMA) is a powerful tool for predicting the possible 
movements of a given macromolecule. It has been shown recently that half of 
the known protein movements can be modelled by using at most two 
low-frequency normal modes. Applications of NMA cover wide areas of 
structural biology, such as the study of protein conformational changes upon 
ligand binding, membrane channel opening and closure, potential movements of 
the ribosome, and viral capsid maturation. Another, newly emerging field of 
NMA is related to protein structure determination by X-ray crystallography, 
where normal mode perturbed models are used as templates for diffraction data 
phasing through molecular replacement (MR). Here we present ElNémo, a web 
interface to the Elastic Network Model that provides a fast and simple tool 
to compute, visualize and analyse low-frequency normal modes of large 
macro-molecules and to generate a large number of different starting models 
for use in MR. Due to the ‘rotation-translation-block' (RTB) approximation 
implemented in ElNémo, there is virtually no upper limit to the size of the 
proteins that can be treated. Upon input of a protein structure in Protein 
Data Bank (PDB) format, ElNémo computes its 100 lowest-frequency modes and 
produces a comprehensive set of descriptive parameters and visualizations, 
such as the degree of collectivity of movement, residue mean square 
displacements, distance fluctuation maps, and the correlation between 
observed and normal-mode-derived atomic displacement parameters (B-factors). 
Any number of normal mode perturbed models for MR can be generated for 
download. If two conformations of the same (or a homologous) protein are 
available, ElNémo identifies the normal modes that contribute most to the 
corresponding protein movement. The web server can be freely accessed at 

More information about the Bio-soft mailing list

Send comments to us at biosci-help [At] net.bio.net