BMRB Entry 17660

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17660

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for LmrA-NBD
Deposition date:
2011-05-23
Original release date:
2012-07-11
Authors:
Woehnert, Jens; Hellmich, Ute; Duchardt-Ferner, Elke; Glaubitz, Clemens
Citation:

Citation: Hellmich, Ute; Duchardt-Ferner, Elke; Glaubitz, Clemens; Wohnert, Jens. "Backbone NMR resonance assignments of the nucleotide binding domain of the ABC multidrug transporter LmrA from Lactococcus lactis in its ADP-bound state."  Biomol. NMR Assignments 6, 69-73 (2012).
PubMed: 21786024

Assembly members:

Assembly members:
LmrA-NBD, polymer, 263 residues, 28879.2 Da.
ADP, non-polymer, 427.201 Da.

Natural source:

Natural source:   Common Name: Lactococcus lactis   Taxonomy ID: 1358   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Lactococcus lactis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LmrA-NBD: GSDEEQEVLHQGDSLDLEGK TLSAHHVDFAYDDSEQILHD ISFEAQPNSIIAFAGPSGGG KSTIFSLLERFYQPTAGEIT IGGQPIDSVSLENWRSQIGF VSQDSAIMAGTIRENLTYGL EGNFTDEDLWQVLDLAFARS FVENMPDQLNTEVGERGVKI SGGQRQRLAIARAFLRNPKI LMLDEATASLDSESESMVQR ALDSLMKGRTTLVIAHRLST IVDADKIYFIEKGEITGSGK HNELVATHPLYAKYVSEQLT VGQ

Data sets:
Data typeCount
13C chemical shifts724
15N chemical shifts247
1H chemical shifts247

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1nucleotide binding domain1
2adenosine 5'-phosphate2

Entities:

Entity 1, nucleotide binding domain 263 residues - 28879.2 Da.

1   GLYSERASPGLUGLUGLNGLUVALLEUHIS
2   GLNGLYASPSERLEUASPLEUGLUGLYLYS
3   THRLEUSERALAHISHISVALASPPHEALA
4   TYRASPASPSERGLUGLNILELEUHISASP
5   ILESERPHEGLUALAGLNPROASNSERILE
6   ILEALAPHEALAGLYPROSERGLYGLYGLY
7   LYSSERTHRILEPHESERLEULEUGLUARG
8   PHETYRGLNPROTHRALAGLYGLUILETHR
9   ILEGLYGLYGLNPROILEASPSERVALSER
10   LEUGLUASNTRPARGSERGLNILEGLYPHE
11   VALSERGLNASPSERALAILEMETALAGLY
12   THRILEARGGLUASNLEUTHRTYRGLYLEU
13   GLUGLYASNPHETHRASPGLUASPLEUTRP
14   GLNVALLEUASPLEUALAPHEALAARGSER
15   PHEVALGLUASNMETPROASPGLNLEUASN
16   THRGLUVALGLYGLUARGGLYVALLYSILE
17   SERGLYGLYGLNARGGLNARGLEUALAILE
18   ALAARGALAPHELEUARGASNPROLYSILE
19   LEUMETLEUASPGLUALATHRALASERLEU
20   ASPSERGLUSERGLUSERMETVALGLNARG
21   ALALEUASPSERLEUMETLYSGLYARGTHR
22   THRLEUVALILEALAHISARGLEUSERTHR
23   ILEVALASPALAASPLYSILETYRPHEILE
24   GLULYSGLYGLUILETHRGLYSERGLYLYS
25   HISASNGLULEUVALALATHRHISPROLEU
26   TYRALALYSTYRVALSERGLUGLNLEUTHR
27   VALGLYGLN

Entity 2, adenosine 5'-phosphate - C10 H15 N5 O10 P2 - 427.201 Da.

1   ADP

Samples:

sample_2: LmrA-NBD, [U-100% 15N; U-90% 2H], 300 uM; ADP 10 mM; H2O 90%; D2O 10%; NaCl 50 mM

sample_1: LmrA-NBD, [U-100% 13C; U-100% 15N; U-90% 2H], 300 uM; ADP 10 mM; H20 90%; D20 10%; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 950 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz

Related Database Links:

EMBL CAL98427
GB AAB49750 ABF67597 ADJ60835 AEU41048 AGV72614
REF WP_041168686 WP_041931331 WP_042748901 WP_043736657 WP_046125038
SP P97046
AlphaFold P97046

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