› 2kbl

Solution NMR

NMR Structure of a Monomeric Folding Intermediate Reveals the Structural Basis for Rapid Assembly of an Evolutionary Optimized Trimerization Module

Released:
DOI: 10.2210/pdb2kbl/pdb
PDB entry 2kbl coloured by chain, ensemble of 10 models, front view.
PDB entry 2kbl coloured by chain, ensemble of 10 models, side view.
PDB entry 2kbl coloured by chain, ensemble of 10 models, top view.
Source organism: Escherichia virus T4
Primary publication:
NMR structure of a monomeric intermediate on the evolutionarily optimized assembly pathway of a small trimerization domain.
Habazettl J, Reiner A, Kiefhaber T
J Mol Biol 389 103-14 (2009)
PMID: 19361528

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-535873 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibritin Chain: A
Molecule details ›
Chain: A
Length: 29 amino acids
Theoretical weight: 3.26 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P10104 (Residues: 458-484; Coverage: 6%)
Gene name: wac

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 58%
Refinement method: simulated annealing, simulated annealing with explicit solvent
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Unusual biophysics of intrinsically disordered proteins.
Uversky VN. (2013)
1 more

2 mentions without citation

PEP-FOLD: an updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides.
Thévenet et al. (2012)
1 more