PDBe 2jss

Solution NMR

NMR structure of chaperone Chz1 complexed with histone H2A.Z-H2B

Released:
Primary publication:
NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B.
OpenAccess logo Nat. Struct. Mol. Biol. 15 868-9 (2008)
PMID: 18641662

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone H2A.Z-specific chaperone CHZ1 Chain: B
Molecule details ›
Chain: B
Length: 62 amino acids
Theoretical weight: 6.96 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P40019 (Residues: 64-125; Coverage: 41%)
Gene names: CHZ1, YER030W
Sequence domains: Histone chaperone domain CHZ
Histone H2A.Z; Histone H2B.1 Chain: A
Molecule details ›
Chain: A
Length: 192 amino acids
Theoretical weight: 21.07 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12692 (Residues: 23-119; Coverage: 72%)
  • Canonical: P02293 (Residues: 37-131; Coverage: 73%)
  • nullnull
Gene names: H2AZ, H2B1, HTA3, HTB1, HTZ1, O2345, SPT12, YD9934.09C, YDR224C, YOL012C
Structure domains: Histone, subunit A

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 75%
Refinement method: torsion angle dynamics, simulated annealing, molecular dynamics
Chemical shifts: BMR15393  
Expression systems:
  • Not provided
  • Escherichia coli