› 2mjb

Solution NMR

Solution nmr structure of ubiquitin refined against dipolar couplings in 4 media

Released:
DOI: 10.2210/pdb2mjb/pdb
PDB entry 2mjb coloured by chain, ensemble of 20 models, front view.
PDB entry 2mjb coloured by chain, ensemble of 20 models, side view.
PDB entry 2mjb coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Improved cross validation of a static ubiquitin structure derived from high precision residual dipolar couplings measured in a drug-based liquid crystalline phase.
Maltsev AS, Grishaev A, Roche J, Zasloff M, Bax A
J Am Chem Soc 136 3752-5 (2014)
PMID: 24568736

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158832 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin Chain: A
Molecule details ›
Chain: A
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P62987 (Residues: 1-76; Coverage: 59%)
Gene names: UBA52, UBCEP2
Sequence domains: Ubiquitin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 87%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Hybrid Approaches to Structural Characterization of Conformational Ensembles of Complex Macromolecular Systems Combining NMR Residual Dipolar Couplings and Solution X-ray Scattering.
Venditti et al. (2016)
1 more

12 mentions without citation

NMR studies of dynamic biomolecular conformational ensembles.
Torchia DA. (2015)
11 more