2lkm

Solution NMR

Structural Basis for Molecular Interactions Involving MRG Domains: Implications in Chromatin Biology

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
PHD finger protein 12 Chain: A
Molecule details ›
Chain: A
Length: 42 amino acids
Theoretical weight: 4.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q96QT6 (Residues: 200-241; Coverage: 4%)
Gene names: KIAA1523, PHF12
Sequence domains: PHD finger protein 12 MRG binding domain
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Mortality factor 4-like protein 1 Chain: B
Molecule details ›
Chain: B
Length: 172 amino acids
Theoretical weight: 19.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9UBU8 (Residues: 194-362; Coverage: 47%)
Gene names: FWP006, HSPC008, HSPC061, MORF4L1, MRG15, PP368
Structure domains: MRG domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 85%
Refinement method: simulated annealing
Chemical shifts: BMR18000  
Expression system: Escherichia coli BL21