› 2l56

Solution NMR

NMR structure of the GCN4 trigger peptide refined using biased molecular dynamics simulations

Released:
DOI: 10.2210/pdb2l56/pdb
PDB entry 2l56 coloured by chain, ensemble of 10 models, front view.
PDB entry 2l56 coloured by chain, ensemble of 10 models, side view.
PDB entry 2l56 coloured by chain, ensemble of 10 models, top view.
Source organism: Synthetic construct
Primary publication:
Exploring the trigger sequence of the GCN4 coiled-coil: biased molecular dynamics resolves apparent inconsistencies in NMR measurements.
Missimer JH, Dolenc J, Steinmetz MO, van Gunsteren WF
Protein Sci 19 2462-74 (2010)
PMID: 20954244

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-162864 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
General control protein GCN4 Chain: A
Molecule details ›
Chain: A
Length: 18 amino acids
Theoretical weight: 1.91 KDa
Source organism: Synthetic construct
Expression system: Not provided

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: molecular dynamics
Expression system: Not provided

Quick links

Citations

3 review citations

Understanding biomolecular motion, recognition, and allostery by use of conformational ensembles.
Fenwick et al. (2011)
2 more

1 mention without citation

Exploring the trigger sequence of the GCN4 coiled-coil: biased molecular dynamics resolves apparent inconsistencies in NMR measurements.
Missimer et al. (2010)