› 1fcl

Solution NMR

DELTA1.5: A COMPUTATIONALLY DESIGNED CORE VARIANT OF THE B1 DOMAIN OF STREPTOCOCCAL PROTEIN G

Released:
DOI: 10.2210/pdb1fcl/pdb
PDB entry 1fcl coloured by chain, ensemble of 40 models, front view.
PDB entry 1fcl coloured by chain, ensemble of 40 models, side view.
PDB entry 1fcl coloured by chain, ensemble of 40 models, top view.
Source organism: Streptococcus sp.
Primary publication:
Designed protein G core variants fold to native-like structures: sequence selection by ORBIT tolerates variation in backbone specification.
Ross SA, Sarisky CA, Su A, Mayo SL
Protein Sci 10 450-4 (2001)
PMID: 11266631

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148791 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Immunoglobulin G-binding protein G Chain: A
Molecule details ›
Chain: A
Length: 56 amino acids
Theoretical weight: 6.22 KDa
Source organism: Streptococcus sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: P19909 (Residues: 302-357; Coverage: 10%)
Gene name: spg
Sequence domains: B domain
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Standard Distance Geometry/simulated Annealing Methods
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Computer-based design of novel protein structures.
Butterfoss et al. (2006)
8 more

3 mentions without citation

Protein Simulations in Fluids: Coupling the OPEP Coarse-Grained Force Field with Hydrodynamics.
Sterpone et al. (2015)
2 more