› 2n48

Solution NMR

EC-NMR Structure of Escherichia coli YiaD Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target ER553

Released:
DOI: 10.2210/pdb2n48/pdb
PDB entry 2n48 coloured by chain, ensemble of 20 models, front view.
PDB entry 2n48 coloured by chain, ensemble of 20 models, side view.
PDB entry 2n48 coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli K-12
Primary publication:
Protein structure determination by combining sparse NMR data with evolutionary couplings.
Tang Y, Huang YJ, Hopf TA, Sander C, Marks DS, Montelione GT
Nat Methods 12 751-4 (2015)
PMID: 26121406

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153462 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable lipoprotein YiaD Chain: A
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 16.06 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P37665 (Residues: 79-219; Coverage: 71%)
Gene names: JW5657, b3552, yiaD
Sequence domains: OmpA family
Structure domains: OmpA-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 94%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

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Citations

11 review citations

Principles for Integrative Structural Biology Studies.
Rout et al. (2019)
10 more

1 mention without citation

Pangenome and immuno-proteomics analysis of Acinetobacter baumannii strains revealed the core peptide vaccine targets.
Hassan et al. (2016)