BMRB Entry 26333

Title:
Chemical shift assignments of the fusion protein consisting of the C-terminal deleted hepatitis B virus X protein BH3-like motif peptide and Bcl-xL
Deposition date:
2022-07-12
Original release date:
2023-07-19
Authors:
Kusunoki, Hideki; Hamaguchi, Isao; Kobayashi, Naohiro; Nagata, Takashi
Citation:

Citation: Kusunoki, Hideki; Hamaguchi, Isao; Kobayashi, Naohiro; Nagata, Takashi. "Chemical shift assignments of a fusion protein comprising the C-terminal-deleted hepatitis B virus X protein BH3-like motif peptide and Bcl-xL"  Biomol. NMR Assign. 16, 357-361 (2022).
PubMed: 36044106

Assembly members:

Assembly members:
HBx(101-120) and Bcl-xL fusion protein, polymer, 190 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 10407   Superkingdom: Viruses   Kingdom: not available   Genus/species: Orthohepadnavirus not available

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts763
15N chemical shifts184
1H chemical shifts1175

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HBx(101-120) and Bcl-xL fusion protein1

Entities:

Entity 1, HBx(101-120) and Bcl-xL fusion protein 190 residues - Formula weight is not available

1   GLYSERHISMETSERALAMETSERTHRTHR
2   ASPLEUGLUALATYRPHELYSASPCYSVAL
3   PHELYSASPTRPGLYSERGLYSERGLYSER
4   GLYSERGLYSERMETSERGLNSERASNARG
5   GLULEUVALVALASPPHELEUSERTYRLYS
6   LEUSERGLNLYSGLYTYRSERTRPSERGLN
7   PHESERASPVALGLUGLUASNARGTHRGLU
8   ALAPROGLUGLYTHRGLUSERGLUALAVAL
9   LYSGLNALALEUARGGLUALAGLYASPGLU
10   PHEGLULEUARGTYRARGARGALAPHESER
11   ASPLEUTHRSERGLNLEUHISILETHRPRO
12   GLYTHRALATYRGLNSERPHEGLUGLNVAL
13   VALASNGLULEUPHEARGASPGLYVALASN
14   TRPGLYARGILEVALALAPHEPHESERPHE
15   GLYGLYALALEUCYSVALGLUSERVALASP
16   LYSGLUMETGLNVALLEUVALSERARGILE
17   ALAALATRPMETALATHRTYRLEUASNASP
18   HISLEUGLUPROTRPILEGLNGLUASNGLY
19   GLYTRPASPTHRPHEVALGLULEUTYRGLY

Samples:

sample_1: HBx(101-120)-linker-Bcl-xL, [U-99% 13C; U-99% 15N], 0.5 mM; potassium phosphate20 – 50 mM; sodium chloride 50 mM; H2O 95%; D2O, U-2H, 5%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRDraw - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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