› 1btb

Solution NMR

THREE-DIMENSIONAL SOLUTION STRUCTURE AND 13C ASSIGNMENTS OF BARSTAR USING NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

Released:
DOI: 10.2210/pdb1btb/pdb
PDB entry 1btb coloured by chain, ensemble of 30 models, front view.
PDB entry 1btb coloured by chain, ensemble of 30 models, side view.
PDB entry 1btb coloured by chain, ensemble of 30 models, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy.
Lubienski MJ, Bycroft M, Freund SM, Fersht AR
Biochemistry 33 8866-77 (1994)
PMID: 8043574

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145869 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Barstar Chain: A
Molecule details ›
Chain: A
Length: 89 amino acids
Theoretical weight: 10.22 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Not provided
UniProt:
  • Canonical: P11540 (Residues: 2-90; Coverage: 99%)
Sequence domains: Barstar (barnase inhibitor)
Structure domains: Barstar-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

2 review citations

Fast events in protein folding: the time evolution of primary processes.
Callender et al. (1998)
1 more

6 mentions without citation

Conformer selection and induced fit in flexible backbone protein-protein docking using computational and NMR ensembles.
Chaudhury et al. (2008)
5 more