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Software Developed by the Donald Lab

LibProtNMR - Library for Protein NMR

Download LibProtNMR | Documentation | License | Contact

Welcome to the website for the LibProtNMR software. Here, you can download LibProtNMR, download Documentation, read the license agreement, and e-mail us inquiries.

LibProtNMR is a software platform and library of algorithms in structural molecular biology, and was developed in the lab of Prof. Bruce Donald at Duke University.

LibProtNMR is a Java library of various modules and subroutines for implementing algorithms in structural molecular biology, and is available as a source distribution. This software is meant to aid developers implementing computational structural biology software in Java, but we feel it would not be of much use to end users directly.

LibProtNMR 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. LibProtNMR 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.

Additional License requirments:

There are additional restrictions imposed on the use and distribution of this open-source code, including:

1. The header in our source code (see license) must be included in any modication or extension of the code;
2. Any publications, grant applications, or patents that use LibProtNMR must state that LibProtNMR was used, with a sentence such as "We used the open-source LibProtNMR software [Ref] to analyze the NMR data and determine the solution structure/dynamics of...."
3. Any publications, grant applications, or patents that use LibProtNMR must cite (a) both our papers, listed below, and (b) this website. These papers constitute the first use of LibProtNMR:
   • A graphical method for analyzing distance restraints using residual dipolar couplings for structure determination of symmetric protein homo-oligomers. Martin JW, Yan AK, Bailey-Kellogg C, Zhou P, Donald BR. Protein Sci. 2011 Jun;20(6):970-85. doi: 10.1002/pro.620.
   • Structure of an HIV-1-neutralizing antibody target, the lipid-bound gp41 envelope membrane proximal region trimer. Reardon PN, Sage H, Dennison SM, Martin JW, Donald BR, Alam SM, Haynes BF, Spicer LD. Proc Natl Acad Sci U S A. (PNAS) 2014 Jan 28;111(4):1391-6. doi: 10.1073/pnas.1309842111.
4. By downloading and using LibProtNMR you consent and agree to these restrictions and requirements.