MobiDB

Curated data for MobiDB is obtained from DisProt[4] database giving information and disorder annotation manually extracted from literature. In order to complement disorder annotation, MobiDB features additional annotations from external sources:

• UniProt: Annotations from the UniProt database include organism, subcellular location, tissue specificity, function, relevant sites, relevant regions, post-translational modifications, and linear motifs.
• Pfam: protein domain annotations are displayed in graphical form and are link-enabled, allowing the user to visit the corresponding Pfam page for further information.
• PDB: Secondary structure is extracted from the PDB whenever available, and displayed in graphical form and in 3D.
• STRING: Known interactors with evidence in "database" and "experimental" are displayed in a sortable table.

• PDB X-ray: When a crystallographic experiment is done to try and resolve a protein's structure, there are cases where the position of certain residues can not be accurately determined. One of the possible causes of this is that the residue is part of a flexible/disordered region. For this reason missing residues in PDB experiments are considered an indication of intrinsic disorder.
• PDB NMR: Deposited files of NMR experiments for protein structure resolution often contain multiple models, representing different conformations of the same protein. By calculating the differences between the positions of each model's residues, one can measure the degree in which this positions change. This change can be interpreted as a measure of how flexible or disordered a protein is. The MOBI web server (from which the name of this database was derived) automates this calculations taking as input a PDB formatted file.

A great variety of intrinsic protein disorder predictors have been trained in the last decade. The bulk of them are trained to mimic the nature of the annotations previously described. Since MobiDB currently covers the full set of UniProt sequences, the included predictors need to be extremely fast. Ten predictors currently included (ESpritz in its three flavours, IUPred in its two flavours, DisEMBL in two of its flavours, GlobPlot, VSL2b and JRONN) enable MobiDB to provide disorder annotations for every protein, even when no curated or indirect data is available.