BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 18647

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18647

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Title: 1H, 13C, and 15N backbone resonance assignments of the L124D mutant of StAR-related lipid transfer domain protein 4 (StARD4)   PubMed: 22918595

Deposition date: 2012-08-07 Original release date: 2012-10-18

Authors: Dikiy, Igor; Ramlall, Trudy; Eliezer, David

Citation: Dikiy, Igor; Ramlall, Trudy; Eliezer, David. "1H, 13C, and 15N backbone resonance assignments of the L124D mutant of StAR-related lipid transfer domain protein 4 (StARD4)."  Biomol. NMR Assignments 7, 245-248 (2013).

Assembly members:
mStARD4L124D, polymer, 224 residues, Formula weight is not available

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
mStARD4L124D: MADPESPWSQIGRKIKLEGL SDVASISTKLQNTLIQYHSI KEDEWRVAKKVKDVTVWRKP SEEFNGYLYKAQGVMDDVVN NVIDHIRPGPWRLDWDRLMT SLDVLEHFEENCCVMRYTTA GQLDNIISPREFVDFSYTVG YEEGLLSCGVSVEWSETRPE FVRGYNHPCGWFCVPLKDSP SQSLLTGYIQTDLRGMIPQS AVDTAMASTLANFYSDLRKG LRKA

Data sets:
Data typeCount
13C chemical shifts619
15N chemical shifts200
1H chemical shifts524

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1mStARD4L124D1

Entities:

Entity 1, mStARD4L124D 224 residues - Formula weight is not available

1   METALAASPPROGLUSERPROTRPSERGLN
2   ILEGLYARGLYSILELYSLEUGLUGLYLEU
3   SERASPVALALASERILESERTHRLYSLEU
4   GLNASNTHRLEUILEGLNTYRHISSERILE
5   LYSGLUASPGLUTRPARGVALALALYSLYS
6   VALLYSASPVALTHRVALTRPARGLYSPRO
7   SERGLUGLUPHEASNGLYTYRLEUTYRLYS
8   ALAGLNGLYVALMETASPASPVALVALASN
9   ASNVALILEASPHISILEARGPROGLYPRO
10   TRPARGLEUASPTRPASPARGLEUMETTHR
11   SERLEUASPVALLEUGLUHISPHEGLUGLU
12   ASNCYSCYSVALMETARGTYRTHRTHRALA
13   GLYGLNLEUASPASNILEILESERPROARG
14   GLUPHEVALASPPHESERTYRTHRVALGLY
15   TYRGLUGLUGLYLEULEUSERCYSGLYVAL
16   SERVALGLUTRPSERGLUTHRARGPROGLU
17   PHEVALARGGLYTYRASNHISPROCYSGLY
18   TRPPHECYSVALPROLEULYSASPSERPRO
19   SERGLNSERLEULEUTHRGLYTYRILEGLN
20   THRASPLEUARGGLYMETILEPROGLNSER
21   ALAVALASPTHRALAMETALASERTHRLEU
22   ALAASNPHETYRSERASPLEUARGLYSGLY
23   LEUARGLYSALA

Samples:

sample_1: mStARD4L124D, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.04 M; pH: 6.4; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

VNMR, Varian - collection

TOPSPIN, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAC31233 BAC31335 BAC35805 BAC37423 BAC39424
GB AAH05642 AAL87127 AAL87128 EDK97071
REF NP_598535
SP Q99JV5

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts