› 7tir

Solution NMR

Backbone-modified variant of the B domain of Staphylococcal protein A: beta3-residues in helix 3

Released:
DOI: 10.2210/pdb7tir/pdb
PDB entry 7tir coloured by chain, ensemble of 10 models, front view.
PDB entry 7tir coloured by chain, ensemble of 10 models, side view.
PDB entry 7tir coloured by chain, ensemble of 10 models, top view.
Source organism: Staphylococcus aureus
Primary publication:
Implications of the unfolded state in the folding energetics of heterogeneous-backbone protein mimetics.
Santhouse JR, Leung JMG, Chong LT, Horne WS
OpenAccess logo Chem Sci 13 11798-11806 (2022)
PMID: 36320921

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174081 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
LysM domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 59 amino acids
Theoretical weight: 6.67 KDa
Source organism: Staphylococcus aureus
Expression system: Not provided
UniProt:
  • Canonical: Q2UW47 (Residues: 185-242; Coverage: 13%)
Gene name: spa
Sequence domains: B domain

Ligands and Environments

No bound ligands
4 modified residues:
Ligand B3X 1 x B3X
Ligand B3E 1 x B3E
Ligand B3K 1 x B3K
Ligand B3A 1 x B3A

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 53%
Refinement method: simulated annealing
Expression system: Not provided

Quick links

Citations

1 citations in other articles

Chemical Shifts of Artificial Monomers Used to Construct Heterogeneous-Backbone Protein Mimetics in Random Coil and Folded States.
Rao et al. (2023)

2 mentions without citation

Implications of the unfolded state in the folding energetics of heterogeneous-backbone protein mimetics.
Santhouse et al. (2022)
1 more