› 1ilf

Solution NMR

NMR STRUCTURE OF APO CBFB

Released:
DOI: 10.2210/pdb1ilf/pdb
PDB entry 1ilf coloured by chain, ensemble of 25 models, front view.
PDB entry 1ilf coloured by chain, ensemble of 25 models, side view.
PDB entry 1ilf coloured by chain, ensemble of 25 models, top view.
Source organism: Mus musculus
Primary publication:
Structure and backbone dynamics of Apo-CBFbeta in solution.
Wolf-Watz M, Grundström T, Härd T
Biochemistry 40 11423-32 (2001)
PMID: 11560490

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170588 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Core-binding factor subunit beta Chain: A
Molecule details ›
Chain: A
Length: 141 amino acids
Theoretical weight: 16.61 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q08024 (Residues: 1-141; Coverage: 75%)
Gene names: Cbfb, Pebp2b, Pebpb2
Sequence domains: Core binding factor beta subunit
Structure domains: Core binding factor, beta subunit

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing and torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 citation in other articles

Application of the random coil index to studying protein flexibility.
Berjanskii et al. (2008)
4 more

6 mentions without citation

Protein-protein docking benchmark version 4.0.
Hwang et al. (2010)
5 more