› 2mu2

Solution NMR

NMR structure of the cap domain of NP_346487.1, a putative phosphoglycolate phosphatase from Streptococcus pneumoniae TIGR4

Released:
DOI: 10.2210/pdb2mu2/pdb
PDB entry 2mu2 coloured by chain, ensemble of 20 models, front view.
PDB entry 2mu2 coloured by chain, ensemble of 20 models, side view.
PDB entry 2mu2 coloured by chain, ensemble of 20 models, top view.
Source organism: Streptococcus pneumoniae TIGR4
Primary publication:
J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4.
Jaudzems K, Pedrini B, Geralt M, Serrano P, Wüthrich K
J Biomol NMR 61 65-72 (2015)
PMID: 25428766

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101484 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydrolase, haloacid dehalogenase-like family Chain: A
Molecule details ›
Chain: A
Length: 208 amino acids
Theoretical weight: 23.71 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H2URV7 (Residues: 1-206; Coverage: 100%)
Gene name: SP_2064
Sequence domains: Haloacid dehalogenase-like hydrolase
Structure domains: Putative phosphatase; domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 76%
Refinement method: torsion angle dynamics, simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

CASD-NMR 2: robust and accurate unsupervised analysis of raw NOESY spectra and protein structure determination with UNIO.
Guerry et al. (2015)

1 mention without citation

J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4.
Jaudzems et al. (2015)