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 51096

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

Deposition date: 2021-09-23 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, 88 residues, Formula weight is not available

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: GSHMDKEEAKANAAAHEWYV AIDEKQVGPFNVEKVKDLWD RGEVGPDSLCWRSGFSDWIP LSETAELASVLAPRPSKPVI VAPEPVSG

Data sets:
Data typeCount
13C chemical shifts341
15N chemical shifts85
1H chemical shifts521

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GltJ-GYF1

Entities:

Entity 1, GltJ-GYF 88 residues - Formula weight is not available

1   GLYSERHISMETASPLYSGLUGLUALALYS
2   ALAASNALAALAALAHISGLUTRPTYRVAL
3   ALAILEASPGLULYSGLNVALGLYPROPHE
4   ASNVALGLULYSVALLYSASPLEUTRPASP
5   ARGGLYGLUVALGLYPROASPSERLEUCYS
6   TRPARGSERGLYPHESERASPTRPILEPRO
7   LEUSERGLUTHRALAGLULEUALASERVAL
8   LEUALAPROARGPROSERLYSPROVALILE
9   VALALAPROGLUPROVALSERGLY

Samples:

sample_1: GltJ-GYF, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 10 mM

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

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_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 NOESYsample_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