Assignment of 1H, 13C and 15N resonances of N-terminal domain of DnaA protein

DnaA protein is a key protein in the initiation of chromosomal replication in Escherichia coli. We reported the assignments of ¹H, ¹³C, and ¹⁵N resonances of N-terminal domain of Dna A (1–108) which contains the activities of self-oligomerization and DnaB helicase loading.     

Assignment of 1H, 13C, and 15N chemical shift resonances of P2 C-repressor protein

This note presents the ¹H, ¹³C, and ¹⁵N resonances assignment of the 22 kDa, dimeric, C-repressor protein from the P2 bacteriophage. The C-repressor controls the genetic switch that determines if the temperate P2 phage should exist in the lytic or lysogenic lifemode.     

Assignment of 1H, 13C and 15N resonances of the reduced human IgG1 CH3 domain

Here we report the NMR resonance assignments for the reduced form of human IgG1 C_H3 domain, a 26 kDa dimer in solution (residues 341–447). The assignments have been deposited in the BioMagResBank with a BMRB accession number of 15204.     

1H, 13C, and 15N resonance assignment of the ubiquitin-like domain from Dsk2p

The ubiquitin-like domain (UBL) of yeast protein Dsk2p is widely believed to recognize and bind to ubiquitin receptors on the proteasome and, as part of Dsk2p, to bridge polyubiquitinated substrates and proteasomal degradation machinery. Here we report NMR resonance assignment for ¹H, ¹⁵N, and ¹³C nuclei in the backbone and side chains of the UBL domain of Dsk2p. This assignment will aid in NMR studies focused on understanding of Dsk2’s interactions with proteasomal receptors and its role as a polyubiquitin shuttle in the ubiquitin-dependent proteasomal degradation as well as other cellular pathways.     

1H, 13C, and 15N resonance assignments of a general stress protein GSP13 from Bacillus subtilis

GSP13 encoded by gene yugI is a general stress protein in Bacillus subtilis. The NMR assignments of the protein are essential for its structure determination.     

1H, 13C and 15N resonance assignment of the first N-terminal RNA recognition motif (RRM) of the human heterogeneous nuclear ribonucleoprotein H (hnRNP H)

Human heterogeneous nuclear ribonucleoprotein H (hnRNP H) regulates alternative splicing of HIV-1 Tat pre-mRNA. The structure of the first N-terminal domain (residues 1–104) of hnRNP H was solved and its binding to an exonic splicing silencer (pESS2) studied. For this, all backbone and 85% of side-chain resonance frequencies were assigned.