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 51104

Title: 1H, 13C and 15N chemical shift assignments of the ZnR and GYF cytoplasmic domains of the GltJ protein from Myxococcus xanthus   PubMed: 35445965

Deposition date: 2021-09-27 Original release date: 2022-04-20

Authors: Attia, Bouchra; Serrano, Bastien; Bornet, Olivier; Guerlesquin, Francoise; Elantak, Latifa

Citation: Attia, Bouchra; Serrano, Bastien; Bornet, Olivier; Guerlesquin, Francoise; My, Laetitia; Castaing, Jean-Philippe; Mignot, Tam; Elantak, Latifa. "1H, 13C and 15N chemical shift assignments of the ZnR and GYF cytoplasmic domains of the GltJ protein from Myxococcus xanthus"  Biomol. NMR Assignments 16, 219-223 (2022).

Assembly members:
entity_1, polymer, 45 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: Myxococcus xanthus   Taxonomy ID: 34   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Myxococcus xanthus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):
entity_1: MARFVCDSCRAQYMISDDKI GPKGVKVRCKKCGHTITVRP AGALE

Data sets:
Data typeCount
13C chemical shifts181
15N chemical shifts42
1H chemical shifts291

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GltJ-ZnR-chain1
2Zinc ion2

Entities:

Entity 1, GltJ-ZnR-chain 45 residues - Formula weight is not available

1   METALAARGPHEVALCYSASPSERCYSARG
2   ALAGLNTYRMETILESERASPASPLYSILE
3   GLYPROLYSGLYVALLYSVALARGCYSLYS
4   LYSCYSGLYHISTHRILETHRVALARGPRO
5   ALAGLYALALEUGLU

Entity 2, Zinc ion - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: GltJ-ZnR, [U-100% 13C; U-100% 15N], 0.45 mM; D2O, [U-100% 2H], 5%; sodium phosphate 10 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D CBCACONHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection, processing

CcpNMR - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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