STING (Sequence To and withINGraphics) is a free Web-based suite of programmes for a comprehensive analysis of the relationship between protein sequence, structure, function, and stability. STING is freely accessible at .
is a Web-based suite of programmes that starts with the visualisation of a molecular structure (using or CHIME)and leads the user through a series of operations resulting in an extensive structural analysis of the molecule:
- amino acid sequence and structure positions, with emphasis on bi-directional coupling of sequence and 3-D information
- pattern search, neighbours identification
- H-bonds, angles, and distances between atoms are easy to obtain thanks to the intuitive graphic and menu interface
- sequence to structure relationships
- analysis of structure's quality
- nature and volume of atomic contacts of intra- and inter-chain type
- analysis of amino acid relative conservation at specified position among homologous proteins
- Accessible Surface Area
- relationship of relative conservation to the intra-chain contacts
- functional parameters deciphered
is a service for extracting information about an individual amino acid of a protein. This information is presented as a series of GIF images and a table, integrated in a single printer-friendly HTML page, containing values of up to 125 structure/function descriptors/parameters. Sting Report allows the visualisation of all the information about a specific residue, on platforms with the most elementary configurations (without Java, Chime, or additional plug-ins).
Java Protein Dossier
is an interactive presentation of important physical-chemical characteristics of the macromolecular structure described in PDB file. By using colour code scales for each residue of the sequence, JPD shows corresponding: temperature factor, solvent accessibility of the single chain (and additionally in complex with the additional present chains in given PDB file), hydrophobicity, sequence conservation in a multiple alignment (relative entropy), double occupancies, reliability, pockets, rotamers, and histograms representing the atomic contacts. JPD additionally shows the identification of Interface Forming Residue (IFR) and their internal contacts. JPD offers information about electrostatic potential and curvature on protein surface. In addition, comparison of the Secondary Structure annotated by PDB, by DSSP and by Stride is presented. The JPD_HELP below is presented in the separate organisational units, so that a user is capable to quickly understand what's available in STING_DB and how to access this information. JPD relays much on the image summaries, rather than using the words.
is a powerful tool for the bioinformatics researcher to analyse the PDB's collection of protein structure descriptions from a variety of perspectives, and recover specific files using a repertoire of alternate criteria. PDB-Metrics employs a database system to maintain several measures extracted from files deposited in the PDB, such as size, type, deposition date, number of chains, number of models (for proteins resolved using NMR—Nuclear Magnetic Resonance), resolution (for non-NMR files), number of atoms, and the frequency of each kind of residue in the protein, among additional characteristics. The PDB-Metrics database additionally includes keywords, taken from the headers of the PDB files, to support information search and recovery. This database is periodically updated (usually once a week). The time of the most recent update of the PDB-Metrics database appears in the top of the PDB-Metrics main page. This date and time refers to the moment PDB-Metrics started the updating process, using a local copy of the PDB, which must have been synchronised with the PDB central repository a few minutes earlier.
shows the atomic contacts between amino acids in a PDB entry received a special attention. The complete profile of the interactions can be analysed in the contacts window containing HTML table, which displays residue name and number, its pair in contact establishing, type of the contact, distance between contacting atoms, and accessibility and entropy of two contacting residues.
IFR Graphical Contacts
The atomic contacts between amino acids belonging to facing chains in a given PDB entry received a special attention. The complete profile of the interactions across the interface can be analysed in the contacts window containing HTML table, which displays residue chain name, residue name and number, its pair in contact establishing across the interface, type of the contact, distance between contacting atoms, and accessibility and entropy of two contacting residues.
Protein DNA Contacts
Java Table of Contacts
Intelligent graphical presentation of the Ramachandran Plot using all advantages of Java programming language. The use of the existing options allows an inter-connection of data in the dihedral angle plot with the 3-D structure of the molecule. A selected number of amino acids can be highlighted for a better correlation between its position in the structure and the position of the Psi/Phi angles marked in the diagram.
This service presents PDB file sequence and consensus sequence (as found in Homology-derived Secondary Structure of Proteins) coloured by conservation, color-coded graphic bars of relative entropy, information about residues present in additional homologous sequences, with their respective frequency. For fast visualization, this programme generates the sequence logo.
XY Graphics Java Plot
is the STING component which permits to a user to examine one of 150 different parameters in a simple yet intuitive plot showing the numerical values at the Y-axes and the sequence residue numbers at the X-axis.
Java Cα-Cα Distance Plot
module displays the level curves of the distances between the alpha carbon of each residue and alpha carbon atoms of every additional residue, within a single chain of the PDB file.
Java Cβ-Cβ Distance Plot
module displays the level curves of the distances between the beta carbon of each residue and beta carbon atoms of every additional residue, within a single chain of the PDB file.
Diamond Sting MSA
Diamond Sting Phylogenetic Tree
is the Web-based tool for analysis of the amino acid frequencies within protein chain(s) (of given pdb file or group of pdb files) as well as for analysis of 3-D contacts between the C-alpha and/or Last Heavy Atoms (LHA) in the amino acid side chain.
is a programme for the calculation of the residue frequency and atomic contacts from inter-facial areas between two or more protein chains, for a given (list of) PDB file(s).
is a visual aid to display multiple sequence alignments with the amino acids coloured by physico-chemical properties. STING paint now supports the following sequence and Multiple-Sequence Alignment (MSA) formats: Coloring sequence of any PDB entry, Coloring any sequence in FASTA format, Coloring MSA in CE and PRISM output format Coloring MSA in CLUSTAL-W, PSI-BLAST, and GCG output format.
produces the image of the amino acid sequence along with the secondary structure elements, rendered as cartoons .
provides a graphical report of several important structural characteristics of the PDB entry. It offers a plot from PDB cartoon annotated with color-coded scales representing for each amino acid the corresponding temperature factor, solvent accessibility of the chain in isolation and in complex with the additional present chains in PDB file, sequence conservation in a multiple alignment (relative sequence entropy), and histograms representing the atomic contacts (as in the Graphical contacts module), as well as IFR residue identification and IFR contacts. In addition, comparison of the Secondary Structure annotated by PDB and by DSSP is presented. Protein Dossier is an excellent tool to browse through valuable information about the protein chain. Collection of information is allowing the user to make quite knowledgeable decisions about the possible role of a specific amino acid (or a number of them) in defining the function. It additionally helps in deciphering what effect the specific mutation will have on the structure and function of the protein.