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Structure paper

TitleArginine residues at internal positions in a protein are always charged.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 108, Page 18954-18959, Year 2011
Publish dateMay 15, 2008 (structure data deposition date)
AuthorsHarms, M.J. / Schlessman, J.L. / Sue, G.R. / Garcia-Moreno E, B.
External linksProc. Natl. Acad. Sci. USA / PubMed:22080604
MethodsX-ray diffraction
Resolution1.9 - 2.15 Å
Structure data

PDB-3d4w:
Crystal structure of Staphylococcal nuclease variant Delta+PHS A109R at cryogenic temperature
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3d8g:
Crystal structure of Staphylococcal nuclease variant Delta+PHS I72R at cryogenic temperature
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

PDB-3dhq:
Crystal structure of Staphylococcal nuclease variant Delta+PHS A90R at cryogenic temperature
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-CA:
Unknown entry

ChemComp-THP:
THYMIDINE-3',5'-DIPHOSPHATE

Source
  • staphylococcus aureus (bacteria)
  • staphylococcus aureus subsp. aureus mw2 (bacteria)
KeywordsHYDROLASE / Staphylococcal nuclease / hyperstable variant / internal arg / Endonuclease / Metal-binding / Secreted / Zymogen / Nuclease / Membrane

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