› 1aab

Solution NMR

NMR STRUCTURE OF RAT HMG1 HMGA FRAGMENT

Released:
DOI: 10.2210/pdb1aab/pdb
PDB entry 1aab coloured by chain, ensemble of 33 models, front view.
PDB entry 1aab coloured by chain, ensemble of 33 models, side view.
PDB entry 1aab coloured by chain, ensemble of 33 models, top view.
Source organism: Rattus norvegicus
Primary publication:
Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy.
Hardman CH, Broadhurst RW, Raine AR, Grasser KD, Thomas JO, Laue ED
Biochemistry 34 16596-607 (1995)
PMID: 8527432

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159002 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
High mobility group protein B1 Chain: A
Molecule details ›
Chain: A
Length: 83 amino acids
Theoretical weight: 9.69 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P63159 (Residues: 2-84; Coverage: 39%)
Gene names: Hmg-1, Hmg1, Hmgb1
Sequence domains: HMG-box domain
Structure domains: High mobility group box domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

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Citations

23 review citations

Using chemical shift perturbation to characterise ligand binding.
Williamson MP. (2013)
22 more

13 mentions without citation

Bacteriophage T4 gene 41 helicase and gene 59 helicase-loading protein: a versatile couple with roles in replication and recombination.
Jones et al. (2001)
12 more