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Solution NMR

Solution NMR Structure of asl3597 from Nostoc sp. PCC7120. Northeast Structural Genomics Consortium Target ID Nsr244.

Released:
DOI: 10.2210/pdb2krx/pdb
PDB entry 2krx coloured by chain, ensemble of 20 models, front view.
PDB entry 2krx coloured by chain, ensemble of 20 models, side view.
PDB entry 2krx coloured by chain, ensemble of 20 models, top view.
Source organism: Nostoc sp. PCC 7120 = FACHB-418
Primary publication:
Solution NMR structure of Asl3597 from Nostoc sp. PCC7120, the first structure from protein domain family PF12095, reveals a novel fold.
Feldmann EA, Ramelot TA, Yang Y, Xiao R, Acton TB, Everett JK, Montelione GT, Kennedy MA
Proteins 80 671-5 (2012)
PMID: 22113821

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-187101 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Asl3597 protein Chain: A
Molecule details ›
Chain: A
Length: 94 amino acids
Theoretical weight: 10.99 KDa
Source organism: Nostoc sp. PCC 7120 = FACHB-418
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8YR53 (Residues: 1-86; Coverage: 100%)
Gene name: asl3597
Sequence domains: Protein CHLORORESPIRATORY REDUCTION 7
Structure domains: Protein CHLORORESPIRATORY REDUCTION 7

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Applications of NMR-based PRE and EPR-based DEER spectroscopy to homodimer chain exchange characterization and structure determination.
Yang et al. (2014)

1 mention without citation

Solution NMR structure of Asl3597 from Nostoc sp. PCC7120, the first structure from protein domain family PF12095, reveals a novel fold.
Feldmann et al. (2012)