vanddraabe provides a powerful way to identify and analyze conserved waters within crystallographic protein structures and molecular dynamics simulation trajectories. Statistical parameters for each water cluster, informative graphs, and a PyMOL session file to visually explore the conserved waters and protein are returned. Hydrophilicity is the propensity of waters to congregate near specific protein atoms and is related to conserved waters. An informatics derived set of hydrophilicity values are provided based on a large, high-quality X-ray protein structure dataset.
This package is a reimplementation and expansion of the WatCH1 and PyWATER2 applications and was created to provide the following abilities:
Paul C Sanschagrin and Leslie A Kuhn. Cluster analysis of consensus water sites in thrombin and trypsin shows conservation between serine proteases and contributions to ligand specificity. Protein Science, 1998, 7 (10), pp 2054-2064. DOI: 10.1002/pro.5560071002 PMID: 9792092 WatCH webpage
Hitesh Patel, Bjorn A. Gruning, Stefan Gunther, and Irmgard Merfort. PyWATER: a PyMOL plug-in to find conserved water molecules in proteins by clustering. Bioinformatics, 2014, 30 (20), pp 2978-2980. DOI: 10.1093/bioinformatics/btu424 PMID: 24990608 PyWATER on GitHub
vanddraabe is available on GitHub and on CRAN. To install it:
# The easiest way to get vanddraabe is: install.packages("vanddraabe") # Or get the development version from GitHub: # install.packages("devtools") devtools::install_github("exeResearch/vanddraabe")
The vignette provided here is a detailed example of using
vanddraabe to identify the conserved waters of ten Thrombin structures.
Please note that this project is released with a Contributor Code of Conduct. By participating in this project you agree to abide by its terms.