BMRB Entry 34120

Title:
Solution structure of the C-terminal domain of S. aureus Hibernating Promoting Factor (CTD-SaHPF)
Deposition date:
2017-03-31
Original release date:
2017-06-30
Authors:
Usachev, K.; Khusainov, I.; Ayupov, R.; Validov, S.; Kieffer, B.; Yusupov, M.
Citation:

Citation: Khusainov, Iskander; Vicens, Quentin; Ayupov, Rustam; Usachev, Konstantin; Myasnikov, Alexander; Simonetti, Angelita; Validov, Shamil; Kieffer, Bruno; Yusupova, Gulnara; Yusupov, Marat; Hashem, Yaser. "Structures and dynamics of hibernating ribosomes from Staphylococcus aureus mediated by intermolecular interactions of HPF"  EMBO J. 36, 2073-2087 (2017).
PubMed: 28645916

Assembly members:

Assembly members:
entity_1, polymer, 61 residues, 7124.070 Da.

Natural source:

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 93061   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pGS21A

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts516
15N chemical shifts120
1H chemical shifts760

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21

Entities:

Entity 1, entity_1, 1 61 residues - 7124.070 Da.

1   METILEGLUILEILEARGSERLYSGLUPHE
2   SERLEULYSPROMETASPSERGLUGLUALA
3   VALLEUGLNMETASNLEULEUGLYHISASP
4   PHEPHEVALPHETHRASPARGGLUTHRASP
5   GLYTHRSERILEVALTYRARGARGLYSASP
6   GLYLYSTYRGLYLEUILEGLNTHRSERGLU
7   GLN

Samples:

sample_1: C-terminal domain of SaHPF, [U-99% 13C; U-99% 15N], 2.0 mM; NH4Cl 250 mM; potassium phosphate 50 mM

sample_conditions_1: ionic strength: 250 mM; pH: 7.6; pressure: 1 bar; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - chemical shift assignment, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - data analysis

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

  • Bruker AvanceIII 700 MHz

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