› 1yyj

Solution NMR

The NMR solution structure of a redesigned apocytochrome b562:Rd-apocyt b562

Released:
DOI: 10.2210/pdb1yyj/pdb
PDB entry 1yyj coloured by chain, ensemble of 10 models, front view.
PDB entry 1yyj coloured by chain, ensemble of 10 models, side view.
PDB entry 1yyj coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Specific non-native hydrophobic interactions in a hidden folding intermediate: implications for protein folding.
Feng H, Takei J, Lipsitz R, Tjandra N, Bai Y
Biochemistry 42 12461-5 (2003)
PMID: 14580191

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-162583 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
redesigned apocytochrome B562 Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 11.73 KDa
Source organism: Homo sapiens
Expression system: Not provided
Structure domains: Cytochrome c/b562

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Refinement method: distance geometry, simulated annealing, molecular dynamics, matrix relaxation, torsion angle dynamics
Expression system: Not provided

Quick links

Citations

6 review citations

Protein folding and misfolding: mechanism and principles.
Englander et al. (2007)
5 more

4 mentions without citation

The folding transition-state ensemble of a four-helix bundle protein: helix propensity as a determinant and macromolecular crowding as a probe.
Tjong et al. (2010)
3 more