› 2mnu

Solution NMR

Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for EDB and specific binding aptide

Released:
DOI: 10.2210/pdb2mnu/pdb
PDB entry 2mnu coloured by chain, ensemble of 20 models, front view.
PDB entry 2mnu coloured by chain, ensemble of 20 models, side view.
PDB entry 2mnu coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
An unusual protein-protein interaction through coupled unfolding and binding.
Yu TK, Shin SA, Kim EH, Kim S, Ryu KS, Cheong H, Ahn HC, Jon S, Suh JY
Angew Chem Int Ed Engl 53 9784-7 (2014)
PMID: 24985319

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-526881 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ugl-Y3 Chain: A
Molecule details ›
Chain: A
Length: 93 amino acids
Theoretical weight: 9.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02751 (Residues: 1266-1356; Coverage: 4%)
Gene names: FN, FN1
Sequence domains: Fibronectin type III domain
Structure domains: Immunoglobulins
APT Chain: B
Molecule details ›
Chain: B
Length: 26 amino acids
Theoretical weight: 3.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 75%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Modulating protein-protein interactions: the potential of peptides.
Nevola et al. (2015)
1 more

2 mentions without citation

Computed Protein-Protein Enthalpy Signatures as a Tool for Identifying Conformation Sampling Problems.
Çınaroğlu et al. (2023)
1 more