title: The RING 2.0 web server for high quality residue interaction networks.
abstract: Residue interaction networks (RINs) are an alternative way of representing protein structures where nodes are residues and arcs physico-chemical interactions. RINs have been extensively and successfully used for analysing mutation effects, protein folding, domain-domain communication and catalytic activity. Here we present RING 2.0, a new version of the RING software for the identification of covalent and non-covalent bonds in protein structures, including π-π stacking and π-cation interactions. RING 2.0 is extremely fast and generates both intra and inter-chain interactions including solvent and ligand atoms. The generated networks are very accurate and reliable thanks to a complex empirical re-parameterization of distance thresholds performed on the entire Protein Data Bank. By default, RING output is generated with optimal parameters but the web server provides an exhaustive interface to customize the calculation. The network can be visualized directly in the browser or in Cytoscape. Alternatively, the RING-Viz script for Pymol allows visualizing the interactions at atomic level in the structure. The web server and RING-Viz, together with an extensive help and tutorial, are available from URL: http://protein.bio.unipd.it/ring.
authors.affiliation: Department of Biomedical Sciences, University of Padua, Padua 35121, Italy.
authors.forename: Damiano
authors.initials: D
authors.lastname: Piovesan
authors.affiliation: Department of Biomedical Sciences, University of Padua, Padua 35121, Italy.
authors.forename: Giovanni
authors.initials: G
authors.lastname: Minervini
authors.affiliation: Department of Biomedical Sciences, University of Padua, Padua 35121, Italy CNR Institute of Neuroscience, Padua 35121, Italy silvio.tosatto@unipd.it.
authors.forename: Silvio C E
authors.identifier: 0000-0003-4525-7793
authors.initials: SC
authors.lastname: Tosatto
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D020134:Catalytic Domain; D003196:Computer Graphics; D019925:Cyclin A / Q000737:chemistry* / Q000235:genetics; D051357:Cyclin-Dependent Kinase 2 / Q000737:chemistry* / Q000235:genetics; D050760:Cyclin-Dependent Kinase Inhibitor p27 / Q000737:chemistry* / Q000235:genetics; D030541:Databases, Genetic; D006860:Hydrogen Bonding; D020407:Internet; D008024:Ligands; D000069550:Machine Learning; D008958:Models, Molecular; D011485:Protein Binding; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D020539:Sequence Analysis, Protein; D012984:Software; D055672:Static Electricity
chemical_list: C436291:CDKN1B protein, human; D019925:Cyclin A; D008024:Ligands; D050760:Cyclin-Dependent Kinase Inhibitor p27; C495894:CDK2 protein, human; D051357:Cyclin-Dependent Kinase 2