UNIO
Multi-purpose Software Suite For Protein NMR Structure Determination and more.

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Academic Download (Password protected)

Non-Academic Download (Password protected)

Release Information:

UNIO’10

Version 2.0.2, Jan 1, 2012

Copyright © 2002-2012 Torsten Herrmann

Look at the Release notes.

(Previous release: UNIO Version 2.0.1, Sept 30, 2010.)

(Previous release: UNIO Version 2.0.0, May 10, 2010.)

(Previous release: UNIO Version 1.0.4, April 15, 2009.)

(Previous release: UNIO Version 1.0.3, April 9, 2009.)

(Previous release: UNIO Version 1.0.2, February 6, 2009.)

(Previous release: UNIO Version 1.0.1, January 13, 2009.)

(First release: UNIO Version 1.0.0, December 11, 2008.)


Contact

Dr. Torsten Herrmann

Centre de RMN à Très Hauts Champs

Université de Lyon/UMR 5280 CNRS / ENS Lyon

5 rue de la Doua

69100 Villeurbanne, France

Email: torsten.herrmann@ens-lyon.fr

UNIO User’s Guide

Download the latest version of the User’s Guide for UNIO in PDF format: Unio-UserGuide.pdf [13.5MB]. (Using Acrobat Reader or Mac Preview)


UNIO License

Unio is free-of-charge for academic users. Please request a license via email and provide information about your institution and PI.

 

UNIO

UNIO enables you to perform automated NMR data analysis for protein 3D structure determination. UNIO represents the result of more than a 15 years of meticulous research performed in order to enable accurate, objective and highly automated protein structure determination by NMR.


UNIO NMR data analysis assembles the MATCH algorithm for backbone assignment (1), the ASCAN algorithm for side-chain assignment (2), the CANDID algorithm for NOE assignment (3) and the ATNOS algorithm for NMR signal identification (4) forming the core of UNIO and are accessed via a user-friendly and flexible graphical user interface. Crucial key elements in order to seamlessly integrate the principal data analysis components are numerous auxiliary algorithms, such as automated chemical shift referencing and chemical shift adaptation between the different NMR spectra etc. The standard UNIO data analysis protocol requires only a minimal set of six NMR spectra, namely 3 APSY and 3 NOESY, and features high computational efficiency. Triple-resonance NMR experiments can alternatively be used instead of APSY data for obtaining the backbone resonance assignments. Powerful interactive graphic and text tools facilitate and enhance expert intervention at the structure refinement stage in form of validation, correction and completion of intermediate and final results.


The underlying NMR data analysis models in UNIO were designed for real-world applications in ”standard” NMR laboratories (requiring magnetic field strengths of 500MHz equipped with cryoprobe or 600MHz or above).


The experience gained so far (> 70 de novo structure determinations performed with the entire protocol ranging from backbone resonance assignment to 3D structure calculation) shows that the UNIO approach leads to accurate and objective NMR data interpretation.


(1) Volk, J.; Herrmann, T.; Wüthrich, K. J. Biomol.NMR. 2008, 41, 127-138.

(2) Fiorito, F.; Damberger, F.F.; Herrmann, T.; Wüthrich, K. J. Biomol. NMR 2008, 42, 23-33.

(3) Herrmann, T.; Güntert, P.; Wüthrich, K. J. Mol. Biol. 2002, 319, 209-227.

(4) Herrmann, T.; Güntert, P.; Wüthrich, K. J. Biomol. NMR 2002, 24, 171-189.

News

  1. UNIO Release infos.

  2. Top-ranked UNIO performance in the NMR community-wide blind target initiative CASD-NMR, both in round 1 (CASD-NMR 1) and round 2 (CASD-NMR 2).

  3. More than 1000 UNIO licenses distributed world-wide.

  4. UNIO enables protein structure determination within one week including the collection of NMR experiments (see J-UNIO).

  5. UNIO includes data analysis algorithms for all parts of an NMR structure determination process, namely NMR signal identification, backbone and side-chain resonance assignment, and NOE assignment.

  6. UNIO comes with a rich suite of utility programs for format conversion, post analysis of the NMR structure, molecule visualization, restraint inspection and more.

  7. Comprehensive documentation with more than 120 pages and over 90 figures.

Recent key publications


  1. CASD-NMR 2: Robust and accurate unsupervised analysis of raw NOESY spectra and protein structure determination with UNIO. Guerry, P., Duong, V.D., Herrmann, T. J. Biomol. NMR 2015 April (ahead of print)

  2. APSY-NMR for protein backbone assignment in high-throughput structural biology. Dutta, S.K., , Serrano, P., Proudfoot, A. , Geralt, M. , Pedrini, B., Herrmann, T., Wüthrich, K. J. Biomol. NMR 2015 Jan., 61(1): 47–53.

  3. Rapid Proton-Detected NMR Assignment for Proteins with Fast Magic Angle Spinning. Barbet-Massin, E., Pell, A.J., Retel, J.S., Andreas, L.B., Jaudzems, K., Franks, W.T., Nieuwkoop, A.J., Hiller, M., Higman, V., Guerry, P., Bertarello, A., Knight, M.J., Felletti, M., Le Marchand,T., Kotelovica,S.,  Akopjana, I., Tars, K., Stoppini, M., Bellotti, V., Bolognesi, M., Ricagno, S., Chou, J.J., Griffin, R.G.,  Oschkinat, H., Lesage, A., Emsley, L., Herrmann, T., Pintacuda, G. J. Am. Chem. Soc. 2014, 136(35): 2489-12497.

  4. The J-UNIO protocol for automated protein structure determination by NMR in solution. Serrano, P., Pedrini, B., Mohanty, B., Geralt, M., Herrmann, T., Wüthrich, K.  J. Biomol. NMR 2012 Aug., 53(4): 341-354.