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 27667

Title: Backbone resonance assignment of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime

Deposition date: 2018-10-30 Original release date: 2018-10-30

Authors: Zhou, Yuan

Citation: Zhou, Yuan. "Backbone resonance assignment of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime"  Biomol. NMR Assignments ., .-..

Assembly members:
catalytic_and_ATP-binding_domain_of_HK853, polymer, 171 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: 2336   Superkingdom: not available   Kingdom: Thermotoga   Genus/species: maritima not available

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
catalytic_and_ATP-binding_domain_of_HK853: SLQINREKVDLCDLVESAVN AIKEFASSHNVNVLFESNVP CPVEAYIDPTRIRQVLLNLL NNGVKYSKKDAPDKYVKVIL DEKDGGVLIIVEDNGIGIPD HAKDRIFEQFYRVDSSLTYE VPGTGLGLAITKEIVELHGG RIWVESEVGKGSRFFVWIPK DRAGEDNRQDN

Data sets:
Data typeCount
13C chemical shifts330
1381H chemical shifts

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1catalytic and ATP-binding domain of HK8531

Entities:

Entity 1, catalytic and ATP-binding domain of HK853 171 residues - Formula weight is not available

1   SER.276675.GLU.2766711.
2   ASP.2766717.VAL.2766723.
3   PHE.2766729.VAL.2766735.
4   SER.2766741.VAL.2766747.
5   PRO.2766753.VAL.2766759.
6   ASN.2766765.SER.2766771.
7   ASP.2766777.ILE.2766783.
8   GLY.2766789.VAL.2766795.
9   GLY.27667101.LYS.27667107.
10   GLN.27667113.SER.27667119.
11   VAL.27667125.GLY.27667131.
12   GLU.27667137.GLY.27667143.
13   GLU.27667149.GLY.27667155.
14   TRP.27667161.ALA.27667167.
15   GLN.27667

Samples:

sample_1: catalytic and ATP-binding domain of HK853' '[U-99% 13C; U-99% 15N]; .; . mM

sample_conditions_1: ionic strength: 0.14 M; 8.0: . 27667; .: atm temperature; K: 27667

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
nosotropicnot availablenot available
not availablenot availablenot availablenot available
not availablenot available1not available
not availablenot available$sample_conditions_1not available
not availablesample_conditions_1not availablespectrometer_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, . - chemical shift assignment, 27667

NMR spectrometers:

  • Bruker Avance 700 MHz

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