› 1zn5

Solid-state NMR

Solid State NMR Structure of the low-temperature form of the Pf1 Major Coat Protein in Magnetically Aligned Bacteriophage

Released:
DOI: 10.2210/pdb1zn5/pdb
PDB entry 1zn5 coloured by chain, ensemble of 27 models, front view.
PDB entry 1zn5 coloured by chain, ensemble of 27 models, side view.
PDB entry 1zn5 coloured by chain, ensemble of 27 models, top view.
Source organism: Pseudomonas virus Pf1
Primary publication:
Structural basis of the temperature transition of Pf1 bacteriophage.
Thiriot DS, Nevzorov AA, Opella SJ
Protein Sci 14 1064-70 (2005)
PMID: 15741342

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-137182 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Capsid protein G8P Chain: A
Molecule details ›
Chain: A
Length: 46 amino acids
Theoretical weight: 4.61 KDa
Source organism: Pseudomonas virus Pf1
UniProt:
  • Canonical: P03621 (Residues: 37-82; Coverage: 85%)
Gene name: VIII
Sequence domains: Inovirus Coat protein B
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Determination of torsion angles between adjacent residues using solid-state NMR frequencies

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Citations

6 review citations

Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins.
Saitô et al. (2010)
5 more

1 mention without citation

Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Straus et al. (2011)