1H, 15N, and 13C chemical shift assignments of the micelle immersed C-terminal
FATC domain of the human protein kinase ataxia-telangiectasia mutated (ATM)
fused to the B1 domain of streptococcal protein G (GB1)

The fusion protein consists of 100 amino acid residues

1H, 15N, and 13C chemical shift assignments of the micelle immersed FAT C-terminal (FATC) domains of the human protein kinases ataxia-telangiectasia mutated (ATM) and DNA-dependent protein kinase catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1).

NMR- and circular dichroism-monitored lipid binding studies suggest a general role for the FATC domain as membrane anchor of phosphatidylinositol 3-kinase-related kinases (PIKK).

FATC domain of human 'ataxia-telangiectasia mutated'

Residue 1-56 represent the GB1 tag and are followed by a thrombin (LVPRGS) and an enterokinase (DDDDK) site.
Residue 68-100 correspond to the FATC domain.

pGEV2 ref: Huth, J. R., C. A. Bewley, G. M. Clore, A. M. Gronenborn, B. M. Jackson and A. G. Hinnebusch (1997). "Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR." Protein Science 6(11): 2359-2364

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Publication title: 1H, 15N, and 13C chemical shift assignments of the micelle
immersed C-terminal FATC domains of the human protein kinases
ataxia-telangiectasia mutated (ATM) and DNA-dependent protein kinase catalytic
subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1).

1H, 15N, and 13C chemical shift assignments of the micelle immersed C-terminal FATC domain of the human DNA-dependent protein kinase catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1)

50 mM TRIS, 100 mM NaCl, 0.2 % NaN3, 150 mM deuterated dodecylphosphocholine

Schwieters, Kuszewski, Tjandra and Clore

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax