› 1f0e

Solution NMR

Cecropin A(1-8)-magainin 2(1-12) modified gig to P in dodecylphosphocholine micelles

Released:
DOI: 10.2210/pdb1f0e/pdb
PDB entry 1f0e coloured by chain, ensemble of 20 models, front view.
PDB entry 1f0e coloured by chain, ensemble of 20 models, side view.
PDB entry 1f0e coloured by chain, ensemble of 20 models, top view.
Source organisms:
Primary publication:
Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures.
Oh D, Shin SY, Lee S, Kang JH, Kim SD, Ryu PD, Hahm KS, Kim Y
Biochemistry 39 11855-64 (2000)
PMID: 11009597

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-134344 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cecropin-A; Magainin-2 Chain: A
Molecule details ›
Chain: A
Length: 19 amino acids
Theoretical weight: 2.28 KDa
Source organisms: Expression system: Not provided
UniProt:
  • Canonical: P01507 (Residues: 27-36; Coverage: 24%)
  • Canonical: P11006 (Residues: 271-278; Coverage: 3%)
Gene name: magainins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Distance Geometry-Dynamical Simulated Annealing Hybrid Method
Expression system: Not provided

Quick links

Citations

6 review citations

The relationship between peptide structure and antibacterial activity.
Powers et al. (2003)
5 more

1 mention without citation

Evaluating tilt angles of membrane-associated helices: comparison of computational and NMR techniques.
Ulmschneider et al. (2006)