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 27503

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27503

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Title: Backbone and side chain NMR assignments for the ribosome Elongation Factor P (EfP) from Staphylococcus aureus   PubMed: 30099718

Deposition date: 2018-06-04 Original release date: 2018-10-03

Authors: Golubev, Alexander; Validov, Shamil; Klochkov, Vladimir; Aganov, Albert; Khusainov, Iskander; Yusupov, Marat

Citation: Usachev, Konstantin; Golubev, Alexander; Validov, Shamil; Klochkov, Vladimir; Aganov, Albert; Khusainov, Iskander; Yusupov, Marat. "Backbone and side chain NMR assignments for the ribosome Elongation Factor P (EF-P) from Staphylococcus aureus"  Biomol. NMR Assignments 12, 351-355 (2018).

Assembly members:
Ef-P, polymer, 185 residues, 20545.9478 Da.

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

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

Entity Sequences (FASTA):
Ef-P: MISVNDFKTGLTISVDNAIW KVIDFQHVKPGKGSAFVRSK LRNLRTGAIQEKTFRAGEKV EPAMIENRRMQYLYADGDNH VFMDNESFEQTELSSDYLKE ELNYLKEGMEVQIQTYEGET IGVELPKTVELTVTETEPGI KGDTATGATKSATVETGYTL NVPLFVNEGDVLIINTGDGS YISRG

Data sets:
Data typeCount
13C chemical shifts556
15N chemical shifts152
1H chemical shifts674

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ef-P1

Entities:

Entity 1, Ef-P 185 residues - 20545.9478 Da.

1   METILESERVALASNASPPHELYSTHRGLY
2   LEUTHRILESERVALASPASNALAILETRP
3   LYSVALILEASPPHEGLNHISVALLYSPRO
4   GLYLYSGLYSERALAPHEVALARGSERLYS
5   LEUARGASNLEUARGTHRGLYALAILEGLN
6   GLULYSTHRPHEARGALAGLYGLULYSVAL
7   GLUPROALAMETILEGLUASNARGARGMET
8   GLNTYRLEUTYRALAASPGLYASPASNHIS
9   VALPHEMETASPASNGLUSERPHEGLUGLN
10   THRGLULEUSERSERASPTYRLEULYSGLU
11   GLULEUASNTYRLEULYSGLUGLYMETGLU
12   VALGLNILEGLNTHRTYRGLUGLYGLUTHR
13   ILEGLYVALGLULEUPROLYSTHRVALGLU
14   LEUTHRVALTHRGLUTHRGLUPROGLYILE
15   LYSGLYASPTHRALATHRGLYALATHRLYS
16   SERALATHRVALGLUTHRGLYTYRTHRLEU
17   ASNVALPROLEUPHEVALASNGLUGLYASP
18   VALLEUILEILEASNTHRGLYASPGLYSER
19   TYRILESERARGGLY

Samples:

sample_1: Ef-P, [U-100% 13C; U-100% 15N], 1.3 mM

sample_conditions_1: pH: 7.6; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

CcpNmr_Analysis v2.4, CCPN - chemical shift assignment

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