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Volume Area Dihedral Angle Reporter information


Volume Area Dihedral Angle Reporter
Content
DescriptionStructure Validation Server
Contact
Research centerUniversity of Alberta and The Metabolomics Innovation Centre
LaboratoryDr. David Wishart
Primary citation[1]
Access
Data formatData Input: PDB coordinate file(s); Data Output: Text and graphical data on protein structure features and quality
Websitehttp://vadar.wishartlab.com/
Miscellaneous
Data release
frequency
Every 1-2 years with periodic corrections and updates
Curation policyManually curated

Volume, Area, Dihedral Angle Reporter (VADAR) is a freely available protein structure validation web server that was developed as a collaboration between Dr. Brian Sykes and Dr. David Wishart at the University of Alberta.[1] VADAR consists of over 15 different algorithms and programs for assessing and validating peptide and protein structures from their PDB coordinate data. VADAR is capable of determining secondary structure (using three different algorithms), identifying and classifying six different types of beta turns, determining and calculating the strength of C=O -- N-H hydrogen bonds, calculating residue-specific accessible surface areas (ASA), calculating residue volumes, determining backbone and side chain torsion angles (phi, psi, omega and chi angles), assessing local structure quality (through numerous quality indices), evaluating global structure quality, and identifying residue "outliers" (residues with unusual structural features). The results have been validated through extensive comparison to published data and careful visual inspection. VADAR produces both text and graphical output with most of the quantitative data presented in easily viewed tables. In particular, VADAR's output is presented in a vertical, tabular format with most of the sequence data, residue numbering and any other calculated property or feature presented from top to bottom, rather than from left to right.

  1. ^ a b Willard, L (July 2003). "VADAR: a web server for quantitative evaluation of protein structure quality". Nucleic Acids Res. 31 (13): 3316–9. doi:10.1093/nar/gkg565. PMC 168972. PMID 12824316.

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