PDB-REPRDB: a database of representative protein chains from the Protein Data Bank (PDB)
By Tamotsu Noguchi, H. Matsuda, Y. Akiyama. 2001
87 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Materials Chemistry
- Roland L. Dunbrack
- Guoli Wang
- Katsuhisa Horimoto
- Akira R. Kinjo
- Ken Nishikawa
- Jinbo Xu
- David Baker
- Yang Zhang
In Molecular Biology
- Guoli Wang
- Roland L. Dunbrack
- Katsuhisa Horimoto
- Akira R. Kinjo
- Ken Nishikawa
- David Baker
- Jinbo Xu
- Yang Zhang
Citations in the corpus
- PISCES: a protein sequence culling server (2003, unknown): “The PDB-REPRDB server (Noguchi et al., 2001) provides a number of features, including an ability for the user to set parameters to generate customized lists.”
- PISCES: recent improvements to a PDB sequence culling server (2005, methodology): “In Table 1, we show the lengths of lists under various sequence identity cut-offs as determined by using BLAST, PSIBLAST and the REPRDB server (5), which use CLUSTALW and structure alignments.”
- PDB-REPRDB: a database of representative protein chains from the Protein Data Bank (PDB) in 2003 (2003, unknown): “PDB-REPRDB (2,3) is a database of representative protein chains from the PDB, whose criteria used to select the representatives are: (a) quality of atomic coordinate data, (b) sequence uniqueness, and (c) conformation uniqueness that is particularly local.”
- Predicting absolute contact numbers of native protein structure from amino acid sequence (2004, methodology): “We first selected nonredundant protein chains with known 3D structures in the Protein Data Bank 20 (PDB) using PDB-REPRDB, 21 with conditions such as sequence identity less than 30%, sequence length (cid:5) 50, no membrane proteins, no nonstandard residues, no chain breaks, resolution better than 2…”