› 1c06

Solution NMR

SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN S4 DELTA 41, REFINED WITH DIPOLAR COUPLINGS (ENSEMBLE OF 16 STRUCTURES)

Released:
DOI: 10.2210/pdb1c06/pdb
PDB entry 1c06 coloured by chain, ensemble of 16 models, front view.
PDB entry 1c06 coloured by chain, ensemble of 16 models, side view.
PDB entry 1c06 coloured by chain, ensemble of 16 models, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Refining the overall structure and subdomain orientation of ribosomal protein S4 delta41 with dipolar couplings measured by NMR in uniaxial liquid crystalline phases.
Markus MA, Gerstner RB, Draper DE, Torchia DA
J Mol Biol 292 375-87 (1999)
PMID: 10493882

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160500 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Small ribosomal subunit protein uS4 Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 18.62 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P81288 (Residues: 43-200; Coverage: 79%)
Gene name: rpsD
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: HYBRID DGSA PROTOCOL WITHOUT THE DIPOLAR COUPLING RESTRAINTS FOLLOWED BY ADDITIONAL SA WITH THE DIPOLAR COUPLING RESTRAINTS ADDED
Expression system: Escherichia coli BL21(DE3)

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Citations

17 citation in other articles

Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin.
Skrynnikov et al. (2000)
16 more

7 mentions without citation

Structure and Dynamics Guiding Design of Antibody Therapeutics and Vaccines.
Fernández-Quintero et al. (2023)
6 more