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 exeResearch.com> |
BugReports: | https://github.com/exeResearch/vanddraabe/issues |
License: | MIT + file LICENSE |
URL: | http://vanddraabe.com, https://github.com/exeResearch/vanddraabe/ |
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: vanddraabe_1.1.1.zip, r-release: vanddraabe_1.1.1.zip, r-oldrel: vanddraabe_1.1.1.zip |
macOS binaries: | r-release: vanddraabe_1.1.1.tgz, r-oldrel: vanddraabe_1.1.1.tgz |
Old sources: | vanddraabe archive |
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