Norine

NORINE is a platform that includes a database of nonribosomal peptides together with tools for their analysis. Norine currently contains more than 1000 peptides.
The name Norine stands for Nonribosomal peptides, with ine as a typical ending of peptide names.
For each peptide, the database stores its structure as well as various annotations such as the biological activity, producing organisms, bibliographical references among others. The database can be queried in order to search for peptides through their annotations as well as through their monomeric structures. In the latter case, the user can specify either the composition, the whole structure or a structural pattern (possibly including "undefined monomers") of the searched peptide.

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News

07/2013: Norine is still alive

  • Norine contains now 1164 peptides and others will come this automn
  • Some entries have been corrected
  • Norine code has moved under Model-view-controller architecture, but the functionalities are still effective
  • A new structure search form is available with improved features (see help for more details)
  • Structure search can be done by monomer fingerprint, as presented in our article :
    • A new fingerprint to predict nonribosomal peptides activity.
      Abdo A, Caboche S, Leclere V, Jacques P, Pupin M.
      J Comput Aided Mol Des. 2012 Oct;26(10):1187-94, doi: 10.1007/s10822-012-9608-4
  • Minor bugs fixed

04/2010: Norine features are upgraded:

  • Norine contains now 1122 peptides
  • A new version of the structure editor is available
  • Monomers and peptides are presented grouped to help their search
  • You can now have the list of peptides produced by an organism
  • Minor bugs were corrected

06/22/2009: Norine gets enriched by new features:

  • You can download Norine data as XML or text files
  • Similarity search is now available here

03/10/2009: New release of Norine:

  • The new release of Norine contains 1071 peptides
  • Fatty acids are encoded and all fatty acid variants of a peptide are available
  • Structural pattern matching allows a search for peptides containing the pattern substructure with a given minimal number of monomers. for more information see:
    • Structural pattern matching of nonribosomal peptides,
      Segolene Caboche, Maude Pupin, Valerie Leclere, Philippe Jacques and Gregory Kucherov,
      BMC Structural Biology 2009, 9:15, doi: 10.1186/1472-6807-9-15
  • A more detailled description of each monomer is available (e.g. molecular weight, SMILES, molecular formula)

08/08/2008: Norine gets enriched by new features:

  • You can submit a new peptide or modifications
  • For each peptide, you can add comments
  • Changes in search forms

Norine has been presented for the first time to the JOBIM 06 conference (poster and flash presentation).

In June 2007, a Norine poster has been presented to the 7th congress of the French Society for Microbiology in Nantes, where it has been awarded best poster over than more 300 posters presented.

Terms of use

Norine is freely available to everybody. If you use the database, please cite:
NORINE: a database of nonribosomal peptides
Segolene Caboche; Maude Pupin; Valerie Leclere; Arnaud Fontaine; Philippe Jacques; Gregory Kucherov
Nucleic Acids Research 2008; 36:D326-D331, January 11, 2008, doi: 10.1093/nar/gkm792

We make no warranties regarding the correctness of the data, and disclaim liability for damages resulting from its use. We cannot provide unrestricted permission regarding the use of the data, as some data may be covered by patents or other rights.

What are nonribosomal peptides

Bacteria or fungi feature peptides that are synthesized through a ribosome independent pathway rather than through the classical pathway from the DNA transcription to the translation of mRNA into peptides on the ribosome. This alternative pathway is called NonRibosomal Peptide Synthesis. It is performed by a huge protein complex called a NonRibosomal Peptide Synthetase (NRPS). This is a modularly organized multi-enzyme complex that bears template and biosynthetic machinery at the same time. The molecules synthesized by NRPS are short (two to about fifty monomers), include a high proportion of nonproteogenic amino acids and often contain amino acids connected by bonds other than peptide or disulfide bonds. The diversity of amino acids incorporated in NRPS peptides is large and it is why we prefer to speak of monomers rather than amino acids. Therefore the primary structure of nonribosomal peptides is not always linear. They can form cycles (partial or not) and branchings.
Nonribosomal peptides have a broad range of biological activities and pharmacological properties, for example immunomodulating, iron chelating or antibiotic activities. The latter is illustrated by the famous penicillin which is synthesized from ACV-tripeptide precursor produced by NRPS pathway.
For more details about the monomers stored in Norine, you can read our paper :
Diversity of monomers in nonribosomal peptides: towards the prediction of origin and biological activity. Caboche S, Leclere V, Pupin M, Kucherov G, Jacques P.
J Bacteriol. 2010 Oct;192(19):5143-50, doi: 10.1128/JB.00315-10

Contact informations

This project results from a tight collaboration between the Bonsai bioinformatics research group of LIFL (Laboratoire d'Informatique Fondamentale de Lille) and Inria (Institut National de Recherche en Informatique et en Automatique) and the NRPS team from the ProBioGem laboratory (Laboratoire des Procédés Biologiques Génie Enzymatique et Microbien).
The Norine Team is composed of contributors of these two labs.

All inquiries should be sent to Norine (norine_at_lifl.fr).

This project is supported by PPF Bioinformatique Lille.