BMRB Entry 51156

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51156

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Title:
Backbone NMR resonance assignments of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the ADP-bound state
Deposition date:
2021-10-26
Original release date:
2022-01-07
Authors:
Perez Carrillo, Victor Hugo; Rose-Sperling, Dania; Tran, Mai Ahn; Wiedemann, Christoph; Hellmich, Ute
Citation:

Citation: Perez Carrillo, Victor Hugo; Rose-Sperling, Dania; Tran, Mai Ahn; Wiedemann, Christoph; Hellmich, Ute. "Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state"  Biomol. NMR Assignments 16, 81-86 (2022).
PubMed: 34988902

Assembly members:

Assembly members:
entity_1, polymer, 259 residues, Formula weight is not available
entity_ADP, non-polymer, 427.201 Da.

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GKQIENAHLPIQLDRVSFGY KPDQLILKEVSAVIEAGKVT AIVGPSGGGKTTLFKLLERF YSPTAGTIRLGDEPVDTYSL ESWREHIGYVSQESPLMSGT IRENICYGLERDVTDAEIEK AAEMAYALNFIKELPNQFDT EVGERGIMLSGGQRQRIAIA RALLRNPSILMLDEATSSLD SQSEKSVQQALEVLMEGRTT IVIAHRLSTVVDADQLLFVE KGEITGRGTHHELMASHGLY RDFAEQQLKMNADLENKAG

Data sets:
Data typeCount
13C chemical shifts711
15N chemical shifts244
1H chemical shifts244

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BmrA NBD1
2ADP2

Entities:

Entity 1, BmrA NBD 259 residues - Formula weight is not available

1   GLYLYSGLNILEGLUASNALAHISLEUPRO
2   ILEGLNLEUASPARGVALSERPHEGLYTYR
3   LYSPROASPGLNLEUILELEULYSGLUVAL
4   SERALAVALILEGLUALAGLYLYSVALTHR
5   ALAILEVALGLYPROSERGLYGLYGLYLYS
6   THRTHRLEUPHELYSLEULEUGLUARGPHE
7   TYRSERPROTHRALAGLYTHRILEARGLEU
8   GLYASPGLUPROVALASPTHRTYRSERLEU
9   GLUSERTRPARGGLUHISILEGLYTYRVAL
10   SERGLNGLUSERPROLEUMETSERGLYTHR
11   ILEARGGLUASNILECYSTYRGLYLEUGLU
12   ARGASPVALTHRASPALAGLUILEGLULYS
13   ALAALAGLUMETALATYRALALEUASNPHE
14   ILELYSGLULEUPROASNGLNPHEASPTHR
15   GLUVALGLYGLUARGGLYILEMETLEUSER
16   GLYGLYGLNARGGLNARGILEALAILEALA
17   ARGALALEULEUARGASNPROSERILELEU
18   METLEUASPGLUALATHRSERSERLEUASP
19   SERGLNSERGLULYSSERVALGLNGLNALA
20   LEUGLUVALLEUMETGLUGLYARGTHRTHR
21   ILEVALILEALAHISARGLEUSERTHRVAL
22   VALASPALAASPGLNLEULEUPHEVALGLU
23   LYSGLYGLUILETHRGLYARGGLYTHRHIS
24   HISGLULEUMETALASERHISGLYLEUTYR
25   ARGASPPHEALAGLUGLNGLNLEULYSMET
26   ASNALAASPLEUGLUASNLYSALAGLY

Entity 2, ADP - C10 H15 N5 O10 P2 - 427.201 Da.

1   ADP

Samples:

sample_1: BmrA NBD, [U-13C; U-15N; U-2H], 441 uM; DSS 0.15 mM; ADP 10 mM; BisTris 50 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1

Software:

CARA - chemical shift assignment

TOPSPIN - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

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