Donald Lab Graphic
Other software:
OSPREY
DISCO
PIV
LibProtNMR
RDC-PANDA
NASCA
POOL
Q5
CRANS

Software previously released by the Donald Lab:
Exact-2NH
MTC
NVR/HD/GD
Rage/Enrage

Software Developed by the Donald Lab

DISCO

Download DISCO v1.0 | Download Source | License | Contact

Welcome to the website for the DISCO software. Here, you can download the newest version of DISCO, the source code of DISCO, read the license agreement, and e-mail us inquiries.

Instructions for installing and using DISCO, as well as citation instructions and the licensing agreement can be found in the README file included in the distribution.

About DISCO

DISCO is software to perform structure determination of protein homo-oligomers with cyclic symmetry, and was developed in the lab of Prof. Bruce Donald at Duke University. DISCO computes oligomeric protein structures using geometric constraints derived from RDCs and intermolecular distance restraints such as NOEs or disulfide bonds. When a reliable subunit structure can be calculated from intramolecular restraints, DISCO guarantees that all satisfying oligomer structures will be discovered, yet can run in minutes to hours on only a single desktop-class computer. For further description of DISCO, please refer to our primary publications:

We used DISCO recently in a project on the design and structure determination of a new antigenic membrane-bound MPER trimer for examining immunogenic responses to the HIV-1 viral coat protein gp41. This new design and structure, called gp41-M-MAT, provides important structural information that can further illuminate HIV vaccine development efforts. In particular, DISCO was used to help solve the structure. Our solution structure is also an important addition to the relatively small number of multimeric membrane-associated structures determined using solution state NMR.

This work is also of central interest to us, because gp41-M-MAT is an unusual and important designed protein, and our laboratory is very focused on protein design. In addition, there are implications more broadly for structural biology and also for NMR methodology. Specifically, as you may know, the majority of proteins in modern cells are complexes comprised of symmetric homo-oligomers. However, comparatively few of these have been structurally characterized (i.e., few have had their 3D structures determined from experimental measurements). Similarly, it is difficult to determine the structures of membrane-bound and membrane-associated proteins (even though such proteins are common and are very important). We have spent nearly 10 years developing a robust methodology for using NMR and novel computational algorithms to reliably determine the structure of these (relatively) large, symmetric, membrane-bound protein complexes, and our PNAS paper represents the culmination and application of those advanced computational techniques, (whose software we have released open-source). For background, see the DISCO paper in Protein Science, above, and also my textbook (MIT Press, 2011).

DISCO is free software and can be redistributed and/or modified under the terms of the GNU Lesser General Public License as published by the Free Software Foundation, either version 3 of the License, or (optionally) any later version. DISCO is distributed in the hope that they will be useful, but WITHOUT ANY WARRANTY; without even the implied warranty of MERCHANTABILITY or FITNESS FOR A PARTICULAR PURPOSE. See the GNU Lesser General Public License for more details. Full licensing details, including citation requirements for the various different modules of the software, are found in the README file within the DISCO distribution.

DISCO uses the arrangements package from CGAL generously provided by the computational geometry lab at Tel Aviv University.