The 1H-15N resonances that appeared have been completely assigned. Resonances
for all side chain have been assigned except for several nuclei in residues
E422 to E428. In conclusion, the extent of CbpA-R2 assignment is: 100% of the
amide resonances, 94% of alpha C, 94% of alpha H, 93% of CB and 94% of 1H and
13C side-chain resonances.

NMR assignment of the R2 domain of pneumococcal choline binding protein A (CbpA).

Zhang, J. R., Mostov, K. E., Lamm, M. E., Nanno, M., Shimida, S., Ohwaki, M. and Tuomanen, E. (2000) Cell, 102, 827-837.

essential for pneumococcal virulence and pathogenesis in humans

mediates invasion of human cells by S. pneumoniae

Solution Structure Of Choline Binding Protein A, Domain R2, The Major Adhesin Of Streptococcus Pneumoniae

choline-binding protein A CbpA [Streptococcus pneumoniae]

cell wall binding repeat family protein [Streptococcus pneumoniae GA41301]

cell wall binding repeat family protein [Streptococcus pneumoniae GA43265]

pneumococcal surface protein A [Streptococcus pneumoniae GA16531]

choline-binding protein A [Streptococcus pneumoniae]

cDNA for CbpA-R2 (residues 329-445) was amplified using PCR with genomic DNA
from the TIGR4 strain of S. pneumoniae as the template and subcloned into
pET-28a (Novagen). The expression vector with a N-terminal His tag was
introduced into E. coli strain BL21(DE3).

1H, 15N and 13C Assignments for the R2 Domain of Choline Binding Protein A (CbpA)

10 mM sodium phosphate buffer with 10% D2O and 0.02% sodium azide (pH 5.0) and the concentration is ~1.8 mM

10 mM sodium phosphate buffer with 10% D2O and 0.02% sodium azide (pH 5.0) and then concentrated to ~1.8 mM

Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. and Bax, A. (1995)
J. Biomol. NMR, 6, 277-293.