Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex
Journal, issue, pages	To be Published
Publish date	Jan 7, 2008 (structure data deposition date)
Authors	Cho, S. / Swaminathan, C.P. / Kerzic, M.C. / Guan, R. / Yang, J. / Kieke, M.C. / Andersen, P.S. / Krantz, D.M. / Mariuzza, R.A. / Eric, S.J.
External links	Search PubMed
Methods	X-ray diffraction
Resolution	2 - 2.3 Å
Structure data	PDB-3bvm: Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex Method: X-RAY DIFFRACTION / Resolution: 2 Å PDB-3bvz: Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex Method: X-RAY DIFFRACTION / Resolution: 2.3 Å PDB-3byt: A complex between a variant of staphylococcal enterotoxin C3 and the variable domain of the murine T cell receptor beta chain 8.2 Method: X-RAY DIFFRACTION / Resolution: 2.3 Å PDB-3byy: Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex Method: X-RAY DIFFRACTION / Resolution: 2.2 Å PDB-3bzd: Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex Method: X-RAY DIFFRACTION / Resolution: 2.3 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-HOH: WATER ChemComp-SO4: SULFATE ION
Source	staphylococcus aureus (bacteria) mus musculus (house mouse)
Keywords	TOXIN / N-terminal Oligosaccharide/oligonucleotide fold / Enterotoxin / Secreted / Superantigen / N-terminal oligosaccharide/oligonucleotide fold (OB fold)