The current version of DIBS contains 1,576 complex structures in 772 entries.
Representative structures of each entry were determined by either X-ray (572 out of 772, accounting for 74.1%) or NMR (200 out of 772, accounting for 25.9%).
The X-ray structure with the highest resolution is DI1000328 (0.90 Å).
The X-ray structure with the lowest resolution is DI1200013 (4.08 Å).
For each entry DIBS provides a set of closely related structures if available. These related structures present interactions where the contributing protein chains are very close homologues of the ones in the entry (they belong to the same UniRef90 cluster and cover approximately the same regions in the corresponding proteins), and the disordered chains feature the same post-translational modifications. The number of these closely related structures can vary widely with some interactions being unique (no solved related structures) and others having a large number of available similar structures (with the maximum number of related structures being 162 for "Human estrogen receptor alpha ligand-binding domain in complex with NCOA2 peptide", accession DI2000015):
Each entry in DIBS incorporates indication that exactly one chain in the interaction is disordered in isolation. This evidence can be structure-based ("Confirmed" or "Inferred from homolgy") or sequence based ("Inferred from motif"); furthermore, many entries have both types of evidence. In addition, many complexes feature Kd values of the interaction between the disordered and the ordered partners. The distribution of entries in evidence categories and availability of Kd values has the following distribution:
The disordered protein region described in each entry in DIBS was assessed for inclusion in DisProt, IDEAL (both describing disordered protein sequences), DisBind (containing interacting regions of disordered proteins) and ELM (containing known linear motifs). For each database only a partial overlap was interpreted as a positive hit:
Entries in DIBS cover a wide range of taxonomic groups. The distribution of interactions in various source organism groups are shown here (taxonomic groups are mutually exclusive, i.e. for example “Mammal” refers to the group of interactions formed by non-human and non-rodent mammalian proteins):
Condensing the above taxonomic groups reveals the distribution of DIBS interactions across the three domains of life (plus viruses). Interactions formed by proteins from different taxonomic domains are classified as “Cross-domain” interactions:
