BMRB Entry 53376

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53376

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Title:
HBX 1-120 isoform
Deposition date:
2025-09-29
Original release date:
2025-11-10
Authors:
Clavier, Alexis; Shida, Toshinobu; Droemer, Maxim; Holzinger, Julian; Schutz, Anne
Citation:

Citation: Clavier, Alexis; Shida, Toshinobu; Droemer, Maxim; Holzinger, Julian; Schutz, Anne. "Sequential backbone chemical shift assignments of a cancer-associated isoform of the HBx protein from human hepatitis B virus"  Biomol. NMR Assignments 20, 4-4 (2025).
PubMed: 41204047

Assembly members:

Assembly members:
entity_1, polymer, 120 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet28a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAARLCCQLDPARDVLCLRP VGAESCGRPFSGSLGTLSSP SPSAVPTDHGAHLSLRGLPV CAFSSAGPCALRFTSARRME TTVNAHQILPKVLHKRTLGL SAMSTTDLEAYFKDCLFKDW

Data sets:
Data typeCount
13C chemical shifts332
15N chemical shifts224
1H chemical shifts230

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HBx 1-1201

Entities:

Entity 1, HBx 1-120 120 residues - Formula weight is not available

HBx genotype D : strain: Switzerland/Strubin/1999 (UniProt) (truncated 1-120)

1   METALAALAARGLEUCYSCYSGLNLEUASP
2   PROALAARGASPVALLEUCYSLEUARGPRO
3   VALGLYALAGLUSERCYSGLYARGPROPHE
4   SERGLYSERLEUGLYTHRLEUSERSERPRO
5   SERPROSERALAVALPROTHRASPHISGLY
6   ALAHISLEUSERLEUARGGLYLEUPROVAL
7   CYSALAPHESERSERALAGLYPROCYSALA
8   LEUARGPHETHRSERALAARGARGMETGLU
9   THRTHRVALASNALAHISGLNILELEUPRO
10   LYSVALLEUHISLYSARGTHRLEUGLYLEU
11   SERALAMETSERTHRTHRASPLEUGLUALA
12   TYRPHELYSASPCYSLEUPHELYSASPTRP

Samples:

sample_1: HBx 1-120, [U-99% 13C; U-98% 15N], 280 uM; urea 1 M; HEPES 50 mM; D2O 5.55 M; L-arginine 125 mM; sodium chloride 150 mM; DTT 5 mM

sample_2: HBx 1-120, [U-99% 13C; U-98% 15N], 50 uM; urea 190 mM; HEPES 50 mM; D2O 5.55 M; L-arginine 125 mM; sodium chloride 150 mM; DTT 0.62 mM

sample_conditions_1: pH: 7.4; temperature: 277 K

sample_conditions_2: pH: 7.4; temperature: 277 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HMQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HMQCsample_2isotropicsample_conditions_2

Software:

CcpNMR v3.2.2 - chemical shift assignment, peak picking

TOPSPIN v3.7 - collection, processing

NMRPipe - processing

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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