BMRB Entry 51826

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51826

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Title:
1H, 13C, 15N resonance assignment of the GltJ N-terminal cytoplasmic region (1-222) from Myxococcus xanthus
Deposition date:
2023-02-07
Original release date:
2024-09-28
Authors:
Attia, Bouchra; Elantak, Latifa
Citation:

Citation: Attia, Bouchra; My, Laetitia; Castaing, Jean-Philippe; Dinet, Celine; Le Guenno, Hugo; Schmidt, Victoria; Espinosa, Leon; Anantharaman, Vivek; Aravind, Lyer; Sebban-Kreuzer, Corinne; Nouailler, Matthieu; Bornet, Olivier; Viollier, Patrick; Elantak, Latifa; Mignot, Tam. "A molecular switch controls assembly of bacterial focal adhesions"  Sci. Adv. 10, eadn2789-eadn2789 (2024).
PubMed: 38809974

Assembly members:

Assembly members:
entity_1, polymer, 222 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: p304-nt1-222

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MRFVCDSCRAQYMISDDKIG PKGVKVRCKKCGHTITVRPA GATAAKDSASESSTSEASAS TDVGKGSDASAATMPATLGT PPEGGLFTDVEEDEIGAVFD QVLSSGTQKIPTEAANEAAA REASAENVRKLAEAEAEPDK EEAKANAAAHEWYVAIDEKQ VGPFNVEKVKDLWDRGEVGP DSLCWRSGFSDWIPLSETAE LASVLAPRPSKPVIVAPEPV SG

Data sets:
Data typeCount
13C chemical shifts552
15N chemical shifts184
1H chemical shifts183

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GltJ1
2Zn ion2

Entities:

Entity 1, GltJ 222 residues - Formula weight is not available

1   METARGPHEVALCYSASPSERCYSARGALA
2   GLNTYRMETILESERASPASPLYSILEGLY
3   PROLYSGLYVALLYSVALARGCYSLYSLYS
4   CYSGLYHISTHRILETHRVALARGPROALA
5   GLYALATHRALAALALYSASPSERALASER
6   GLUSERSERTHRSERGLUALASERALASER
7   THRASPVALGLYLYSGLYSERASPALASER
8   ALAALATHRMETPROALATHRLEUGLYTHR
9   PROPROGLUGLYGLYLEUPHETHRASPVAL
10   GLUGLUASPGLUILEGLYALAVALPHEASP
11   GLNVALLEUSERSERGLYTHRGLNLYSILE
12   PROTHRGLUALAALAASNGLUALAALAALA
13   ARGGLUALASERALAGLUASNVALARGLYS
14   LEUALAGLUALAGLUALAGLUPROASPLYS
15   GLUGLUALALYSALAASNALAALAALAHIS
16   GLUTRPTYRVALALAILEASPGLULYSGLN
17   VALGLYPROPHEASNVALGLULYSVALLYS
18   ASPLEUTRPASPARGGLYGLUVALGLYPRO
19   ASPSERLEUCYSTRPARGSERGLYPHESER
20   ASPTRPILEPROLEUSERGLUTHRALAGLU
21   LEUALASERVALLEUALAPROARGPROSER
22   LYSPROVALILEVALALAPROGLUPROVAL
23   SERGLY

Entity 2, Zn ion - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: GltJ-Nt1-222, [U-99% 13C; U-99% 15N], 0.75 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection, processing

CcpNMR - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker AVANCE III 950 MHz

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