› 1fh1

Solution NMR

BACKBONE FOLD OF NODF

Released:
DOI: 10.2210/pdb1fh1/pdb
PDB entry 1fh1 coloured by chain, front view.
PDB entry 1fh1 coloured by chain, side view.
PDB entry 1fh1 coloured by chain, top view.
Source organism: Rhizobium leguminosarum
Primary publication:
Rapid determination of protein folds using residual dipolar couplings.
Fowler CA, Tian F, Al-Hashimi HM, Prestegard JH
J Mol Biol 304 447-60 (2000)
PMID: 11090286

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138143 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nodulation protein F Chain: A
Molecule details ›
Chain: A
Length: 92 amino acids
Theoretical weight: 9.95 KDa
Source organism: Rhizobium leguminosarum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04685 (Residues: 1-92; Coverage: 100%)
Gene names: hsnA, nodF
Sequence domains: Phosphopantetheine attachment site

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: other
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Residual dipolar couplings in NMR structure analysis.
Lipsitz et al. (2004)
12 more

1 mention without citation

Machine learning model for fast prediction of the natural frequencies of protein molecules.
Qin et al. (2020)