› 2lj5

Solution NMR

Description of the Structural fluctuations of proteins from structure-based calculations of Residual dipolar couplings

Released:
DOI: 10.2210/pdb2lj5/pdb
PDB entry 2lj5 coloured by chain, ensemble of 301 models, front view.
PDB entry 2lj5 coloured by chain, ensemble of 301 models, side view.
PDB entry 2lj5 coloured by chain, ensemble of 301 models, top view.
Source organism: Homo sapiens
Primary publication:
Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings.
Montalvao RW, De Simone A, Vendruscolo M
J. Biomol. NMR (2012)
PMID: 22729708

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
UniProt:
  • Canonical: P62987 (Residues: 1-76; Coverage: 59%)
Gene names: UBA52, UBCEP2
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 46%
Refinement method: molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and Dynamics.
Maximova et al. (2016)
4 more

4 mentions without citation

Enhancing NMR derived ensembles with kinetics on multiple timescales.
Smith et al. (2020)
3 more