Quick selection of representative protein chain sets based on customizable requirements

Bioinformatics

Volumn 16, Issue 6, 2000, Pages 520-526

  Noguchi, Tamotsu ^a   Onizuka, Kentaro ^a   Ando, Makoto ^a,c   Matsuda, Hideo ^b   Akiyama, Yutaka ^a  

^a Real World Computing Partnership   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c JFE STEEL CORPORATION   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; CLASSIFICATION; COMPUTER INTERFACE; COMPUTER PROGRAM; CONTROLLED STUDY; DATA BASE; INTERNET; MEDICAL RESEARCH; METHODOLOGY; PRIORITY JOURNAL; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

EID: 0033828958     PISSN: 13674803     EISSN: 13674811     Source Type: Journal    
DOI: 10.1093/bioinformatics/16.6.520     Document Type: Article

References (16)

1. Parallel Protein Information Analysis (PAPIA) system running on a 64-node PC cluster
2. The protein data bank: A computer-based archival file for macromolecular structures
3. DBGET/LinkDB: An integrated database retrieval system
4. LIGAND database for enzymes, compounds and reactions
5. Selection of representative protein data sets
6. Enlarged representative set of protein structures
7. The FSSP database of structurally aligned protein fold families
8. A discussion of the solution for the best rotation to relate two sets of vectors
9. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
10. HOMSTRAD: A database of protein structure alignments for homologous families
11. SCOP: A structural classification of proteins database for the investigation of sequences and structures
12. A general method applicable to the search for similarities in the amino acid sequence of two proteins
13. PDB-REPRDB: A database of representative protein chains in PDB (Protein Data Bank)
14. CATH-A hierarchic classification of protein domain structures
15. Database of homology derived protein structures and the structural meaning of sequence alignment
16. The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site