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Backbone 1H, 15N, and 13C Resonances Assignment and Secondary Structure Prediction of SAV0506 from Staphylococcus aureus

  • Lee, In Gyun (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Lee, Ki-Young (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Kim, Ji-Hun (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Chae, Susanna (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Lee, Bong-Jin (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
  • 투고 : 2013.06.01
  • 심사 : 2013.06.10
  • 발행 : 2013.06.20

초록

SAV0506 is an 87 residue hypothetical protein from Staphylococcus aureus strain Mu50 and also predicted to have similar function to ribosome associated heat shock protein, Hsp 15. Hsp15 is thought to be involved in the repair mechanism of erroneously produced 50S ribosome subunit. In this report, we present the sequence specific backbone resonance assignment of SAV0506. About 82.5% of all resonances could be assigned unambiguously. By analyzing deviations of the $C{\alpha}$ and $C{\beta}$ chemical shift values, we could predict the secondary structure of SAV0506. This study is an essential step towards the structural characterization of SAV0506.

키워드

참고문헌

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피인용 문헌

  1. Dynamics of the mobile insert helix in the domain III-IV of Aux/IAA17 probed by site-directed spin labeling and paramagnetic NMR spectroscopy vol.19, pp.2, 2015, https://doi.org/10.6564/JKMRS.2015.19.2.061