› 2l15

Solution NMR

Solution Structure of Cold Shock Protein CspA Using Combined NMR and CS-Rosetta method

Released:
DOI: 10.2210/pdb2l15/pdb
PDB entry 2l15 coloured by chain, ensemble of 10 models, front view.
PDB entry 2l15 coloured by chain, ensemble of 10 models, side view.
PDB entry 2l15 coloured by chain, ensemble of 10 models, top view.
Source organism: Escherichia coli
Primary publication:
Fully automated high-quality NMR structure determination of small (2)H-enriched proteins.
Tang Y, Schneider WM, Shen Y, Raman S, Inouye M, Baker D, Roth MJ, Montelione GT
J Struct Funct Genomics 11 223-32 (2010)
PMID: 20734145

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-141939 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cold shock protein CspA Chain: A
Molecule details ›
Chain: A
Length: 70 amino acids
Theoretical weight: 7.41 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A9X9 (Residues: 1-70; Coverage: 100%)
Gene names: JW3525, b3556, cspA, cspS
Sequence domains: 'Cold-shock' DNA-binding domain
Structure domains: Nucleic acid-binding proteins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, molecular dynamics
Expression system: Escherichia coli

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Citations

1 review citation

Possibilities of Using De Novo Design for Generating Diverse Functional Food Enzymes.
Wang et al. (2023)
7 other articles

3 mentions without citation

Fully automated high-quality NMR structure determination of small (2)H-enriched proteins.
Tang et al. (2010)
2 more