BMRB Entry 27400

Title:
Assignment of 1H, 13C and 15N resonances of the extrecclular domain of human Death Receptor DR5
Deposition date:
2018-02-09
Original release date:
2018-06-20
Authors:
Odaert, Benoit; Baudin, Antoine; Berbon, Melanie; Mackereth, Cameron; Guichard, Gilles
Citation:

Citation: Baudin, Antoine; Guichard, Anne; Collie, Gavin; Rousseau, Sabrina; Chaignepain, Stephane; Hocquellet, Agnes; Berbon, Melanie; Loquet, Antoine; Mackereth, Cameron; Guichard, Gilles; Odaert, Benoit. "1H, 13C, 15N NMR resonance assignments and secondary structure determination of the extra-cellular domain from the human proapoptotic TRAIL-R2 death receptor 5 (DR5-ECD)"  Biomol. NMR Assignments 12, 309-314 (2018).
PubMed: 29869749

Assembly members:

Assembly members:
DR5, polymer, 135 residues, 14998 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: pETNus_1a

Data sets:
Data typeCount
13C chemical shifts447
15N chemical shifts114
1H chemical shifts653

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DR5 monomer1

Entities:

Entity 1, DR5 monomer 135 residues - 14998 Da.

Residus 1-4 represent a non-native cleavage site for the TeV protease

1   GLYALAMETGLUSERALALEUILETHRGLN
2   GLNASPLEUALAPROGLNGLNARGALAALA
3   PROGLNGLNLYSARGSERSERPROSERGLU
4   GLYLEUCYSPROPROGLYHISHISILESER
5   GLUASPGLYARGASPCYSILESERCYSLYS
6   TYRGLYGLNASPTYRSERTHRHISTRPASN
7   ASPLEULEUPHECYSLEUARGCYSTHRARG
8   CYSASPSERGLYGLUVALGLULEUSERPRO
9   CYSTHRTHRTHRARGASNTHRVALCYSGLN
10   CYSGLUGLUGLYTHRPHEARGGLUGLUASP
11   SERPROGLUMETCYSARGLYSCYSARGTHR
12   GLYCYSPROARGGLYMETVALLYSVALGLY
13   ASPCYSTHRPROTRPSERASPILEGLUCYS
14   VALHISLYSGLUSER

Samples:

sample_1: DR5, [U-13C; U-15N], 300 uM; Na2HPO4 20 mM; NaCl 50 mM

sample_2: DR5, [U-15N], 90 uM; Na2HPO4 20 mM; NaCl 50 mM

sample_3: DR5, [U-13C; U-15N], 300 uM; Na2HPO4 20 mM; NaCl 50 mM

sample_4: DR5 300 uM; Na2HPO4 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 70 mM; pH: 6.3; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1
2D DQF-COSYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D CBHDsample_3isotropicsample_conditions_1
2D CBHEsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

Related Database Links:

GB AAC01565.1

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