BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

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
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1G51

Entities:

Entity 1, G5 111 residues - 12154.605 Da.

1   METGLYSERSERHISHISHISHISHISSER
2   SERGLYLEUVALPROARGGLYSERHISMET
3   SERLEUASPGLUASNGLUVALALAALAASN
4   VALGLUTHRARGPROGLULEUILETHRARG
5   THRGLUGLUILEPROPHEGLUVALILELYS
6   LYSGLUASNPROASNLEUPROALAGLYGLN
7   GLUASNILEILETHRALAGLYVALLYSGLY
8   GLUARGTHRHISTYRILESERVALLEUTHR
9   GLUASNGLYLYSTHRTHRGLUTHRVALLEU
10   ASPSERGLNVALTHRLYSGLUVALILEASN
11   GLNVALVALGLUVALGLYALAPROVALTHR
12   HIS

Samples:

G5_sample: G5, [U-100% 13C; U-100% 15N], 1 mM; TRIS 25 mM; sodium chloride 25 mM; DSS 0.5 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.025 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCG5_sampleisotropicsample_conditions_1
3D CBCA(CO)NHG5_sampleisotropicsample_conditions_1
2D 1H-1H NOESYG5_sampleisotropicsample_conditions_1
2D 1H-1H TOCSYG5_sampleisotropicsample_conditions_1
3D C(CO)NHG5_sampleisotropicsample_conditions_1
3D HNCACBG5_sampleisotropicsample_conditions_1
3D CBCA(CO)NHG5_sampleisotropicsample_conditions_1
3D H(CCO)NHG5_sampleisotropicsample_conditions_1
3D HCCH-TOCSYG5_sampleisotropicsample_conditions_1
3D 1H-15N NOESYG5_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticG5_sampleisotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

VNMRJ, Varian - collection

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts