› 1ihq

Solution NMR

GLYTM1BZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF A RAT SHORT ALPHA TROPOMYOSIN WITH THE N-TERMINUS ENCODED BY EXON 1B

Released:
DOI: 10.2210/pdb1ihq/pdb
PDB entry 1ihq coloured by chain, ensemble of 10 models, front view.
PDB entry 1ihq coloured by chain, ensemble of 10 models, side view.
PDB entry 1ihq coloured by chain, ensemble of 10 models, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein.
Greenfield NJ, Huang YJ, Palm T, Swapna GV, Monleon D, Montelione GT, Hitchcock-DeGregori SE
J Mol Biol 312 833-47 (2001)
PMID: 11575936

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136527 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
General control transcription factor GCN4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 38 amino acids
Theoretical weight: 4.33 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P03069 (Residues: 250-281; Coverage: 11%)
Gene names: AAS101, AAS3, ARG9, GCN4, YEL009C
Sequence domains: Basic region leucine zipper

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: 1156 CONFORMATIONALLY-RESTRICTING NOE CONSTRAINTS (OUT OF A TOTAL OF 1746 NOE DERIVED DISTANCES) 112 LOOSE DIHEDRAL ANGLE CONSTRAINTS AND FORTY-EIGHT BACKBONE INTRA-HELICAL HYDROGEN BOND CONSTRAINTS WERE UTILILIZED.
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Toxicological evaluation of proteins introduced into food crops.
Hammond et al. (2013)
7 more

2 mentions without citation

Structural attributes for the recognition of weak and anomalous regions in coiled-coils of myosins and other motor proteins.
Sunitha et al. (2012)
1 more