BMRB Entry 19054

Title:
NMR structures of human apoptotic protein tBid in LPPG micelle
Deposition date:
2013-02-25
Original release date:
2013-11-11
Authors:
Wang, Yu; Suzuki, Motoshi; Tjandra, Nico
Citation:

Citation: Wang, Yu; Tjandra, Nico. "Structural insights of tBid, the caspase-8-activated Bid, and its BH3 domain."  J. Biol. Chem. 288, 35840-35851 (2013).
PubMed: 24158446

Assembly members:

Assembly members:
entity, polymer, 135 residues, 15243.369 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Data sets:
Data typeCount
13C chemical shifts564
15N chemical shifts125
1H chemical shifts908

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human apoptotic protein tBid1

Entities:

Entity 1, human apoptotic protein tBid 135 residues - 15243.369 Da.

1   GLYASNARGSERSERHISSERARGLEUGLY
2   ARGILEGLUALAASPSERGLUSERGLNGLU
3   ASPILEILEARGASNILEALAARGHISLEU
4   ALAGLNVALGLYASPSERMETASPARGSER
5   ILEPROPROGLYLEUVALASNGLYLEUALA
6   LEUGLNLEUARGASNTHRSERARGSERGLU
7   GLUASPARGASNARGASPLEUALATHRALA
8   LEUGLUGLNLEULEUGLNALATYRPROARG
9   ASPMETGLULYSGLULYSTHRMETLEUVAL
10   LEUALALEULEULEUALALYSLYSVALALA
11   SERHISTHRPROSERLEULEUARGASPVAL
12   PHEHISTHRTHRVALASNPHEILEASNGLN
13   ASNLEUARGTHRTYRVALARGSERLEUALA
14   ARGASNGLYMETASP

Samples:

sample_1: tBid in LPPG micelle, [U-15N], 0.5 ± 0.1 mM; tBid in LPPG micelle, [U-13C; U-15N], 0.8 ± 0.2 mM; tBid in LPPG micelle, [U-100% 15N; U-80% 2H], 0.8 ± 0.2 mM; D2O 10%; H2O 90%; Potassium Phosphate 50 mM

sample_2: tBid in LPPG micelle, [U-100% 13C; U-100% 15N], 1.0 ± 0.2 mM; D2O 100%; Potassium Phosphate 50 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.6; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
4D HCHC-NOESYsample_2isotropicsample_conditions_1
T1sample_1isotropicsample_conditions_1
T2sample_1isotropicsample_conditions_1

Software:

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

PIPP, Garrett - data analysis

NMRView, Johnson, One Moon Scientific - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

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

Related Database Links:

PDB
DBJ BAF79673 BAG10922 BAG36471 BAG52933
EMBL CAG28531 CAG30275 CAH92211 CAK54378 CAK54677
GB AAC34365 AAH09197 AAH22072 AAH33634 AAH36364
REF NP_001126293 NP_001187 NP_001231496 NP_001231498 NP_001231499
SP P55957
AlphaFold P55957

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