BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18484

Title: Conformational analysis of StrH, the surface-attached exo- -D-N-acetylglucosaminidase from Streptococcus pneumoniae.   PubMed: 23154168

Deposition date: 2012-05-28 Original release date: 2012-11-27

Authors: Pluvinage, Benjamin; Chitayat, Seth; Ficko-Blean, Elizabeth; Abbott, D. Wade; Kunjachen, Jobby Maroor; Grondin, Julie; Spencer, Holly; Smith, Steven; Boraston, Alisdair

Citation: Pluvinage, Benjamin; Chitayat, Seth; Ficko-Blean, Elizabeth; Abbott, D. Wade; Kunjachen, Jobby Maroor; Grondin, Julie; Spencer, Holly; Smith, Steven; Boraston, Alisdair. "Conformational Analysis of StrH, the Surface-Attached exo--d-N-Acetylglucosaminidase from Streptococcus pneumoniae."  J. Mol. Biol. 425, 334-349 (2013).

Assembly members:
entity, polymer, 111 residues, 12154.605 Da.

Natural source:   Common Name: Streptococcus pneumoniae   Taxonomy ID: 1313   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus pneumoniae

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: MGSSHHHHHSSGLVPRGSHM SLDENEVAANVETRPELITR TEEIPFEVIKKENPNLPAGQ ENIITAGVKGERTHYISVLT ENGKTTETVLDSQVTKEVIN QVVEVGAPVTH

Data sets:
Data typeCount
13C chemical shifts309
15N chemical shifts101
1H chemical shifts679

Additional metadata:

  • Assembly
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Related Database Links:

PDB 2LTJ

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