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Note that elNémo will be down from Monday 26th, 6pm, to Tuesday 27th, 9am (french time).
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Welcome to elNémo !

elNémo is the Web-interface to the Elastic Network Model (ENM), a fast and simple way for computing the low frequency normal modes of a macromolecule (Tirion, 1996). Note that, thanks to the RTB approximation (Durand et al., 1994; Tama et al., 2000), this server can perform calculations for all-atom systems.


One major application of normal modes is the identification of potential conformational changes (Tama and Sanejouand, 2001; Delarue and Sanejouand, 2002), e.g. of enzymes upon ligand binding. It has for instance been used in the study of membrane channel opening (Valadie et al., 2003) and for the analysis of structural movements of systems as large as the ribosome (Tama et al., 2003).

It has been shown that in 50% of the cases where protein structures are available in two different conformations, the related movement can be described by using only one or two low frequency normal modes (Krebs et al., 2002). This prompts for an application in X-ray cristallography data phasing, that is to use normal mode perturbed models as templates in molecular replacement (Suhre and Sanejouand, 2004).

Some applications of normal mode analysis are presented in the example section. In the reference section you may find a number of papers that describe the concepts behind this approach. To access previous jobs, go to the job status page.

The present version of elNémo allows you to compute the low frequency normal modes for a given protein structure in PDB format. You will be able to analyse these modes at different levels of detail, i.e. compare the collectivity of the modes, view 3-D animations of the protein movement for each mode and identify those residues that have the largest distance fluctuations in a given mode. Comparision of B-factors derived from the normal mode decomposition and measured B-factors gives an indication on differences in protein flexibility of the free protein and the protein in a crystallographic environment. When you submit two conformations of the same protein, you may analyse the contribution of each mode to the conformational changes (overlap between a protein motion and a normal mode). When two homologous proteins are submitted, the root mean square distance (RMSD) between all residues and the number of residues that are closer than 3A as a function of mode and perturbation can be computed. Perturbed structures in PDB format can be downloaded for use as templates in molecular replacement.

The Elastic Network Model for the LAO binding protein
(figure from Tama and Sanejouand, 2001).

If you find results from this site helpful for your research, please cite one of our papers:

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: 28 March 2017.