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: 2018-11-05

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: Thermotoga maritima   Taxonomy ID: 2336   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermotoga maritima

Experimental source:   Production method: recombinant technology   Host organism: 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
15N chemical shifts138
1H chemical shifts490

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   SERLEUGLNILEASNARGGLULYSVALASP
2   LEUCYSASPLEUVALGLUSERALAVALASN
3   ALAILELYSGLUPHEALASERSERHISASN
4   VALASNVALLEUPHEGLUSERASNVALPRO
5   CYSPROVALGLUALATYRILEASPPROTHR
6   ARGILEARGGLNVALLEULEUASNLEULEU
7   ASNASNGLYVALLYSTYRSERLYSLYSASP
8   ALAPROASPLYSTYRVALLYSVALILELEU
9   ASPGLULYSASPGLYGLYVALLEUILEILE
10   VALGLUASPASNGLYILEGLYILEPROASP
11   HISALALYSASPARGILEPHEGLUGLNPHE
12   TYRARGVALASPSERSERLEUTHRTYRGLU
13   VALPROGLYTHRGLYLEUGLYLEUALAILE
14   THRLYSGLUILEVALGLULEUHISGLYGLY
15   ARGILETRPVALGLUSERGLUVALGLYLYS
16   GLYSERARGPHEPHEVALTRPILEPROLYS
17   ASPARGALAGLYGLUASPASNARGGLNASP
18   ASN

Samples:

sample_1: catalytic and ATP-binding domain of HK853, [U-99% 13C; U-99% 15N], 0.5 mM; HEPES 20 mM; KCl 50 mM

sample_conditions_1: ionic strength: 0.14 M; pH: 8.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Keller and Wuthrich - chemical shift assignment, collection

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