› 1n0c

Solution NMR

Stability of cyclic beta-hairpins: Asymmetric contibutions from side chains of hydrogen bonded cross-strand residue pair

Released:
DOI: 10.2210/pdb1n0c/pdb
PDB entry 1n0c coloured by chain, ensemble of 20 models, front view.
PDB entry 1n0c coloured by chain, ensemble of 20 models, side view.
PDB entry 1n0c coloured by chain, ensemble of 20 models, top view.
Source organism: Synthetic construct
Primary publication:
Stability of cyclic beta-hairpins: asymmetric contributions from side chains of a hydrogen-bonded cross-strand residue pair.
Russell SJ, Blandl T, Skelton NJ, Cochran AG
J Am Chem Soc 125 388-95 (2003)
PMID: 12517150

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-162332 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
bhp_HWLV, disulfide cyclized beta-hairpin peptide Chain: A
Molecule details ›
Chain: A
Length: 12 amino acids
Theoretical weight: 1.21 KDa
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Distance geometry and restrained molecular dynamics with chemical shift refinement
Expression system: Not provided

Quick links

Citations

5 review citations

Design of beta-sheet systems for understanding the thermodynamics and kinetics of protein folding.
Searle et al. (2004)
4 more

3 mentions without citation

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