vanddraabe: Identification and Statistical Analysis of Conserved Waters Near Proteins

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.

Version: 1.1.1
Depends: R (≥ 3.6.0)
Imports: bio3d (≥ 2.3-4), cowplot (≥ 0.9.4), fastcluster (≥ 1.1.25), ggplot2 (≥ 3.1.1), openxlsx (≥ 4.1.0), reshape2 (≥ 1.4.3), scales (≥ 1.0.0)
Suggests: knitr, rmarkdown, testthat
Published: 2019-06-07
Author: Emilio Xavier Esposito [aut, cre]
Maintainer: Emilio Xavier Esposito <emilio at>
License: MIT + file LICENSE
NeedsCompilation: no
Materials: README NEWS
CRAN checks: vanddraabe results


Reference manual: vanddraabe.pdf
Vignettes: vanddraabe: Vignettes
Package source: vanddraabe_1.1.1.tar.gz
Windows binaries: r-devel:, r-release:, r-oldrel:
macOS binaries: r-release: vanddraabe_1.1.1.tgz, r-oldrel: vanddraabe_1.1.1.tgz
Old sources: vanddraabe archive


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