› 1l1k

Solution NMR

NMR Identification and Characterization of the Flexible Regions in the 160 KD Molten Globule-like Aggregate of Barstar at Low pH

Released:
DOI: 10.2210/pdb1l1k/pdb
PDB entry 1l1k coloured by chain, ensemble of 10 models, front view.
PDB entry 1l1k coloured by chain, ensemble of 10 models, side view.
PDB entry 1l1k coloured by chain, ensemble of 10 models, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
NMR identification and characterization of the flexible regions in the 160 kDa molten globule-like aggregate of barstar at low pH.
Juneja J, Bhavesh NS, Udgaonkar JB, Hosur RV
Biochemistry 41 9885-99 (2002)
PMID: 12146954

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
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: 20 amino acids
Theoretical weight: 2.25 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11540 (Residues: 2-21; Coverage: 22%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Refinement method: simulated annealing
Expression system: Escherichia coli

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Citations

1 review citation

Intrinsically disordered proteins: modes of binding with emphasis on disordered domains.
Morris et al. (2021)
17 other articles