MobiDB: a comprehensive database of intrinsic protein disorder annotations.
BACKGROUND
Disordered protein regions are key to the function of numerous processes within an organism and to the determination of a protein's biological role. The most common source for protein disorder annotations, DisProt, covers only a fraction of the available sequences. Alternatively, the Protein Data Bank (PDB) has been mined for missing residues in X-ray crystallographic structures. Herein, we provide a centralized source for data on different flavours of disorder in protein structures, MobiDB, building on and expanding the content provided by already existing sources. In addition to the DisProt and PDB X-ray structures, we have added experimental information from NMR structures and five different flavours of two disorder predictors (ESpritz and IUpred). These are combined into a weighted consensus disorder used to classify disordered regions into flexible and constrained disorder. Users are encouraged to submit manual annotations through a submission form. MobiDB features experimental annotations for 17 285 proteins, covering the entire PDB and predictions for the SwissProt database, with 565 200 annotated sequences. Depending on the disorder flavour, 6-20% of the residues are predicted as disordered.


BACKGROUND
The database is freely available at http://mobidb.bio.unipd.it/.


BACKGROUND
silvio.tosatto@unipd.it.
Department of Biology, University of Padova, Viale G. Colombo 3, 35131 Padova, Italy.
Tomás
T
Di Domenico
Ian
I
Walsh
Alberto J M
AJ
Martin
Silvio C E
SC
Tosatto
D018360:Crystallography, X-Ray; D030562:Databases, Protein; D009682:Magnetic Resonance Spectroscopy; D058977:Molecular Sequence Annotation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D020539:Sequence Analysis, Protein / Q000379:methods; D014584:User-Computer Interface
D011506:Proteins