1H, 15N and 13C Backbone resonance assignments of the 40 kDa LicT-CAT-PRD1 protein

CAT-PRD1 domain of the transcriptional antiterminator LicT protein from Bacillus subtilis

TROSY effects were corrected based on a JHN of 93Hz and 800 MHz 1H frequency. All chemical shifts were obtained from the 2H/13C/15N labeled sample and no correction was applied on the reported values for correction of 2H isotope effect.

Letter to the Editor: 1H, 15N and 13C Backbone resonance assignments of the 40 kDa LicT-CAT-PRD1 protein

Prd Of Lict Antiterminator From Bacillus Subtilis

Structure Of The Native And Inactive Lict Prd From B. Subtilis

BglG family transcriptional antiterminator [Bacillus subtilis subsp. natto BEST195]

transcriptional antiterminator BglG family [Bacillus subtilis BEST7613]

transcriptional antiterminator BglG family [Bacillus subtilis BEST7003]

transcriptional antiterminator [Bacillus subtilis Miyagi-4]

transcriptional antiterminator (BglG family) [Bacillus subtilis subsp. subtilis str. 168]

Transcription antiterminator licT [Bacillus amyloliquefaciens subsp. plantarum CAU B946]

Beta-glucoside bgl operon antiterminator, BglG family [Bacillus subtilis E1]

transcription antiterminator LicT [Bacillus subtilis]

transcriptional antiterminator (BglG family) protein [Bacillus subtilis subsp. spizizenii str. W23]

transcriptional antiterminator (BglG family) protein [Bacillus subtilis BSn5]

transcription antiterminator LicT [Bacillus subtilis subsp. spizizenii TU-B-10]

transcription antiterminator LicT [Bacillus subtilis subsp. subtilis str. RO-NN-1]

transcriptional antiterminator BglG family [Bacillus sp. JS]

transcription antiterminator LicT [Bacillus subtilis subsp. subtilis str. 168]

MULTISPECIES: transcription antiterminator LicT [Bacillales]

RecName: Full=Transcription antiterminator LicT [Bacillus subtilis subsp. subtilis str. 168]

The 167 N-terminal residues of LicT protein were cloned into a pET15 derivative allowing expression of the LicT-CAT-PRD1 domain fused to a C-terminal His Tag (Leu-Glu-6xHis). The fusion protein was produced in E. coli BL21(DE3)

Pons, J.L., Malliavin, T.E., Delsuc, M.A. (1996) J. Biomol. NMR, 8, 445-452

Johnson, B.A, and Blevins, R.A (1994), J. Biomol. NMR, 4, 603-614