BMRB Entry 18721

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18721

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Title:
(1)H, (13)C, and (15)N backbone chemical shift assignments of StAR-related lipid transfer domain protein 5 (STARD5) in complex with cholic acid
Deposition date:
2012-09-17
Original release date:
2012-10-10
Authors:
Letourneau, Danny; Lorin, Aurelien; Lavigne, Pierre; LeHoux, Jean-Guy; Lefebvre, Andree
Citation:

Citation: Letourneau, Danny; Lorin, Aurelien; Lefebvre, Andree; Cabana, Jerome; Lavigne, Pierre; LeHoux, Jean-Guy. "Thermodynamic and solution state NMR characterization of the binding of secondary and conjugated bile acids to STARD5."  Biochim. Biophys. Acta 1831, 1589-1599 (2013).
PubMed: 23872533

Assembly members:

Assembly members:
Molecule_1, polymer, 213 residues, 23797.1169 Da.
HisTag, polymer, 6 residues, 846.9074 Da.

Natural source:

Natural source:   Common Name: Escherichia coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET3A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Molecule_1: MDPALAAQMSEAVAEKMLQY RRDTAGWKICREGNGVSVSW RPSVEFPGNLYRGEGIVYGT LEEVWDCVKPAVGGLRVKWD ENVTGFEIIQSITDTLCVSR TSTPSAAMKLISPRDFVDLV LVKRYEDGTISSNATHVEHP LCPPKPGFVRGFNHPCGCFC EPLPGEPTKTNLVTFFHTDL SGYLPQNVVDSFFPRSMTRF YANLQKAVKQFHE
HisTag: HHHHHH

Data typeCount
13C chemical shifts557
15N chemical shifts186
1H chemical shifts186

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1StarD51
2HisTag2

Entities:

Entity 1, StarD5 213 residues - 23797.1169 Da.

1   METASPPROALALEUALAALAGLNMETSER
2   GLUALAVALALAGLULYSMETLEUGLNTYR
3   ARGARGASPTHRALAGLYTRPLYSILECYS
4   ARGGLUGLYASNGLYVALSERVALSERTRP
5   ARGPROSERVALGLUPHEPROGLYASNLEU
6   TYRARGGLYGLUGLYILEVALTYRGLYTHR
7   LEUGLUGLUVALTRPASPCYSVALLYSPRO
8   ALAVALGLYGLYLEUARGVALLYSTRPASP
9   GLUASNVALTHRGLYPHEGLUILEILEGLN
10   SERILETHRASPTHRLEUCYSVALSERARG
11   THRSERTHRPROSERALAALAMETLYSLEU
12   ILESERPROARGASPPHEVALASPLEUVAL
13   LEUVALLYSARGTYRGLUASPGLYTHRILE
14   SERSERASNALATHRHISVALGLUHISPRO
15   LEUCYSPROPROLYSPROGLYPHEVALARG
16   GLYPHEASNHISPROCYSGLYCYSPHECYS
17   GLUPROLEUPROGLYGLUPROTHRLYSTHR
18   ASNLEUVALTHRPHEPHEHISTHRASPLEU
19   SERGLYTYRLEUPROGLNASNVALVALASP
20   SERPHEPHEPROARGSERMETTHRARGPHE
21   TYRALAASNLEUGLNLYSALAVALLYSGLN
22   PHEHISGLU

Entity 2, HisTag 6 residues - 846.9074 Da.

1   HISHISHISHISHISHIS

Samples:

sample_StarD5: StarD5, [U-100% 13C; U-100% 15N; U-80% 2H], 1 ± 0.05 mM

CondSet1: ionic strength: 0.050 M; pH: 7.400; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_StarD5isotropicCondSet1
2D 1H-15N HSQC/HMQCsample_StarD5isotropicCondSet1
3D HNCOsample_StarD5isotropicCondSet1
3D HNCAsample_StarD5isotropicCondSet1
Expt_9 (H[N[co[{CA|ca[C]}]]])sample_StarD5isotropicCondSet1

Software:

ANALYSIS v2.1, CCPN - Spectrum analysis and Chemical shift assignment

NMRDraw vany, F. Delaglio, S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer and A. Bax - Spectrum analysis, Spectrum display

NMRPipe vany, F. Delaglio, S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer and A. Bax - Spectrum processing

NMR spectrometers:

  • Varian UnityInova 600 MHz

Related Database Links:

BMRB 17909
PDB
EMBL CAH91861
GB AAH04365 AAL89654 AIC52409 EAW99097 EHH27540
REF NP_001126078 NP_001247845 NP_871629 XP_003281060 XP_003810787
SP Q5R8P9 Q9NSY2
AlphaFold Q5R8P9 Q9NSY2

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