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 27090

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Elongation factor P   PubMed: 28951478

Authors: Macosek, Jakub; Hennig, Janosch

Citation: Krafczyk, Ralph; Macosek, Jakub; Jagtap, Pravin Kumar Ankush; Gast, Daniel; Wunder, Swetlana; Mitra, Prithiba; Jha, Amit Kumar; Rohr, Jurgen; Hoffmann-Roder, Anja; Jung, Kirsten; Hennig, Janosch; Lassak, Jurgen. "Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P"  MBio 8, e01412-e01417 (2017).

Assembly members:
EF-P, polymer, 189 residues, 21303.1 Da.

Natural source:   Common Name: Pseudomonas putida   Taxonomy ID: 303   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas putida

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

Entity Sequences (FASTA):
EF-P: MKTGKELKPGTVLRIDNDPW LVQKAEFTKSGRNSAIMKTK LKNLLTGYKTETVYGADDKL DDVILDRKEATLSFINGDEY TFMDTTDYTMYELNAEDIEA VLPYIEEGMEDVCEAVFFEG RLVSVELPTTISRKVVYTEN AARGDTSGKVMKPAKLANGT EISVADFIQIDEWIDIDTRD NSFKGRSKK

Data sets:
Data typeCount
13C chemical shifts516
15N chemical shifts178
1H chemical shifts178

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Elongation factor P1

Entities:

Entity 1, Elongation factor P 189 residues - 21303.1 Da.

1   METLYSTHRGLYLYSGLULEULYSPROGLY
2   THRVALLEUARGILEASPASNASPPROTRP
3   LEUVALGLNLYSALAGLUPHETHRLYSSER
4   GLYARGASNSERALAILEMETLYSTHRLYS
5   LEULYSASNLEULEUTHRGLYTYRLYSTHR
6   GLUTHRVALTYRGLYALAASPASPLYSLEU
7   ASPASPVALILELEUASPARGLYSGLUALA
8   THRLEUSERPHEILEASNGLYASPGLUTYR
9   THRPHEMETASPTHRTHRASPTYRTHRMET
10   TYRGLULEUASNALAGLUASPILEGLUALA
11   VALLEUPROTYRILEGLUGLUGLYMETGLU
12   ASPVALCYSGLUALAVALPHEPHEGLUGLY
13   ARGLEUVALSERVALGLULEUPROTHRTHR
14   ILESERARGLYSVALVALTYRTHRGLUASN
15   ALAALAARGGLYASPTHRSERGLYLYSVAL
16   METLYSPROALALYSLEUALAASNGLYTHR
17   GLUILESERVALALAASPPHEILEGLNILE
18   ASPGLUTRPILEASPILEASPTHRARGASP
19   ASNSERPHELYSGLYARGSERLYSLYS

Samples:

sample_1: EF-P, [U-100% 13C; U-100% 15N], 0.45 mM; sodium phosphate 100 mM; sodium chloride 50 mM; DTT 5 mM; sodium azide 0.02%

sample_conditions_1: pH: 7.6; 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing

CcpNMR, CCPN - chemical shift assignment

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP A0A059UQW3