› 2nmq

Solution NMR

Simultaneous determination of protein structure and dynamics using rdcs

Released:
DOI: 10.2210/pdb2nmq/pdb
PDB entry 2nmq coloured by chain, front view.
PDB entry 2nmq coloured by chain, side view.
PDB entry 2nmq coloured by chain, top view.
Source organism: Streptococcus sp. 'group G'
Primary publication:
Simultaneous determination of protein backbone structure and dynamics from residual dipolar couplings.
Bouvignies G, Markwick P, Brüschweiler R, Blackledge M
J Am Chem Soc 128 15100-1 (2006)
PMID: 17117856

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-139123 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Immunoglobulin G-binding protein G Chain: A
Molecule details ›
Chain: A
Length: 55 amino acids
Theoretical weight: 6.06 KDa
Source organism: Streptococcus sp. 'group G'
Expression system: Escherichia coli
UniProt:
  • Canonical: P06654 (Residues: 298-352; Coverage: 13%)
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: dynamic meccano
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings.
Jensen et al. (2009)
5 more

1 mention without citation

An alternative approach to protein folding.
Kang et al. (2013)