|
This database is a collection of protein-protein homo- and
hetero-complexes as well as domain-domain structures. This issue of
the database contains 17.024 entries (as of October 2007) of which
1350 are two-chain
protein hetero-complexes, 7773 homodimers and 1589 are one-chain
proteins parsed into two domains (domain structures). The rest of
entries are constructed from PDB files for multi-chain protein
complexes by leaving only two interacting chains, (in the database
nomenclature designators of those chains are appended to the name of
the original PDB file). The homo-complexes in this database
are the complexes with two monomers having more than 95 % sequence
identity.
Each entry consists of the X-ray structure taken from the PDB data
bank (in the PDB/ folder), sequence file (in the SEQ/ folder) and the data file (in the INF/ folder)
where all relevant information is stored. File names consist of PDB
ID and extensions .pdb (X-ray structures), .seq (sequence files or .inf (data files).
Current implementation of the database accommodates the following
information for each entry, separately for larger (denoted as chain
A*) and smaller (chain B) components:
- Full sequence;
- Number of residues;
- Number of residues on the
interface;
- List of interfacial residues;
- Number of helices and strands;
- Absolute (in
Å2) and relative
interface areas.
The
database is searchable with respect to majority of the above parameters.
Additional search is possible with respect to the PDB ID and protein
names. Downloads are possible for both individual entries (as plain
text files) and for
the whole content or search (checked) result list (as one gzipped
file). Supplementary search and download is available for the subset of the
database at 40% sequence identity level (the DPPC40 database). Good luck and feel free to sent suggestions or
comment by the clicking Send a
comment button. Yes, and do not forget to enable
Javascript in your browser, otherwise search engine will not work
properly!
If usage of the database results to
publication please quote the original paper**! |