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 27811

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Elongation factor P from E.coli   PubMed: 31178848

Deposition date: 2019-02-28 Original release date: 2019-06-26

Authors: Jagtap, Pravin Kumar Ankush; Macosek, Jakub; Hennig, Janosch

Citation: Volkwein, Wolfram; Krafczyk, Ralph; Jagtap, Pravin Kumar Ankush; Parr, Marina; Mankina, Elena; Macosek, Jakub; Guo, Zhenghuan; Furst, Maximilian Josef; Pfab, Miriam; Frishman, Dmitrij; Hennig, Janosch; Jung, Kirsten; Lassak, Jurgen. "Switching the Post-translational Modification of Translation Elongation Factor EF-P."  Front. Microbiol. 10, 1148-1148 (2019).

Assembly members:
EFP, polymer, 188 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
EFP: MATYYSNDFRAGLKIMLDGE PYAVEASEFVKPGKGQAFAR VKLRRLLTGTRVEKTFKSTD SAEGADVVDMNLTYLYNDGE FWHFMNNETFEQLSADAKAI GDNAKWLLDQAECIVTLWNG QPISVTPPNFVELEIVDTDP GLKGDTAGTGGKPATLSTGA VVKVPLFVQIGEVIKVDTRS GEYVSRVK

Data sets:
Data typeCount
13C chemical shifts299
15N chemical shifts168
1H chemical shifts168

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EFP1

Entities:

Entity 1, EFP 188 residues - Formula weight is not available

1   METALATHRTYRTYRSERASNASPPHEARG
2   ALAGLYLEULYSILEMETLEUASPGLYGLU
3   PROTYRALAVALGLUALASERGLUPHEVAL
4   LYSPROGLYLYSGLYGLNALAPHEALAARG
5   VALLYSLEUARGARGLEULEUTHRGLYTHR
6   ARGVALGLULYSTHRPHELYSSERTHRASP
7   SERALAGLUGLYALAASPVALVALASPMET
8   ASNLEUTHRTYRLEUTYRASNASPGLYGLU
9   PHETRPHISPHEMETASNASNGLUTHRPHE
10   GLUGLNLEUSERALAASPALALYSALAILE
11   GLYASPASNALALYSTRPLEULEUASPGLN
12   ALAGLUCYSILEVALTHRLEUTRPASNGLY
13   GLNPROILESERVALTHRPROPROASNPHE
14   VALGLULEUGLUILEVALASPTHRASPPRO
15   GLYLEULYSGLYASPTHRALAGLYTHRGLY
16   GLYLYSPROALATHRLEUSERTHRGLYALA
17   VALVALLYSVALPROLEUPHEVALGLNILE
18   GLYGLUVALILELYSVALASPTHRARGSER
19   GLYGLUTYRVALSERARGVALLYS

Samples:

sample_1: EFP, [U-100% 13C; U-100% 15N], 0.8 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

Cara, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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