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 17233

Title: Solution structure of the PlyG cell wall binding domain

Deposition date: 2010-10-01 Original release date: 2012-07-25

Authors: Volkman, B.; Dias, J.; Peterson, F.

Citation: Dias, J.; Peterson, F.; Volkman, B.. "TBD"  To be published ., .-..

Assembly members:
PlyG, polymer, 85 residues, 9447.814 Da.

Natural source:   Common Name: Bacillus phage Gamma   Taxonomy ID: 347962   Superkingdom: viruses   Kingdom: not available   Genus/species: not available Bacillus phage Gamma

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE30

Entity Sequences (FASTA):
PlyG: GSIQKVKNGNVATTSPTKQN IIQSGAFSPYETPDVMGALT SLKMTADFILQSDGLTYFIS KPTSDAQLKAMKEYLDRKGW WYEVK

Data sets:
Data typeCount
13C chemical shifts376
15N chemical shifts96
1H chemical shifts634

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PlyG_11
2PlyG_21

Entities:

Entity 1, PlyG_1 85 residues - 9447.814 Da.

The GS dipeptide, residues 149 and 150, are a cloning artifact.

1   GLYSERILEGLNLYSVALLYSASNGLYASN
2   VALALATHRTHRSERPROTHRLYSGLNASN
3   ILEILEGLNSERGLYALAPHESERPROTYR
4   GLUTHRPROASPVALMETGLYALALEUTHR
5   SERLEULYSMETTHRALAASPPHEILELEU
6   GLNSERASPGLYLEUTHRTYRPHEILESER
7   LYSPROTHRSERASPALAGLNLEULYSALA
8   METLYSGLUTYRLEUASPARGLYSGLYTRP
9   TRPTYRGLUVALLYS

Samples:

sample_1: PlyG, [U-100% 13C; U-100% 15N], 1.25 mM; Bis-Tris, [U-99% 2H], 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 13 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESY (AROMATIC)sample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement

TOPSPIN v2.1, Bruker - collection

NMRPipe v2007, Delagio,F. et al. - processing

XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis

GARANT v2.1, C. Bartels - data analysis

CYANA v2.1, Guntert, P. - structural calculation

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
GB AAM97149 ABA42708 ABA46392 ABA46449 ABA46501
REF WP_001982889 YP_338149 YP_338200 YP_459981 YP_512326

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