BMRB Entry 15969

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15969

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Title:
Heteronuclear NMR assignments for the dimeric human hepatitis B virus core protein under capsid dissociating conditions
Deposition date:
2008-10-01
Original release date:
2009-02-16
Authors:
Freund, Stefan; Johnson, Christopher; Jaulent, Agnes; Ferguson, Neil
Citation:

Citation: Freund, Stefan; Johnson, Christopher; Jaulent, Agnes; Ferguson, Neil. "Moving towards high resolution descriptions of the molecular interactions and structural rearrangements of the human hepatitis B core protein"  J. Mol. Biol. 384, 1301-1303 (2008).
PubMed: 18952101

Assembly members:

Assembly members:
Hepatitis_B_virus_coat_protein, polymer, 149 residues, 33540 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pT7-SC

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Hepatitis_B_virus_coat_protein: MDIDPYKEFGATVELLSFLP SDFFPSVRDLLDTAAALYRD ALESPEHCSPHHTALRQAIL CWGDLMTLATWVGTNLEDPA SRDLVVSYVNTNVGLKFRQL LWFHISCLTFGRETVLEYLV SFGVWIRTPPAYRPPNAPIL STLPETTVV

Data sets:
Data typeCount
13C chemical shifts327
15N chemical shifts97
1H chemical shifts100

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Hepatitis B virus coat protein monomer, chain 11
2Hepatitis B virus coat protein monomer, chain 21

Entities:

Entity 1, Hepatitis B virus coat protein monomer, chain 1 149 residues - 33540 Da.

The dimeric hepatitis core protein assignments deposited here correspond to residues 1-149 of the full length (183 residues) core protein. The C-terminal nucleic acid binding domain (residues 150-183) was truncated to simplify spectral assignment. Residues 1-149 of the core protein contain all structured regions reported to date and can form recombinant capsid like particles essentially identical to nucleocapsids isolated from patients infected with hepatitis B virus.

1   METASPILEASPPROTYRLYSGLUPHEGLY
2   ALATHRVALGLULEULEUSERPHELEUPRO
3   SERASPPHEPHEPROSERVALARGASPLEU
4   LEUASPTHRALAALAALALEUTYRARGASP
5   ALALEUGLUSERPROGLUHISCYSSERPRO
6   HISHISTHRALALEUARGGLNALAILELEU
7   CYSTRPGLYASPLEUMETTHRLEUALATHR
8   TRPVALGLYTHRASNLEUGLUASPPROALA
9   SERARGASPLEUVALVALSERTYRVALASN
10   THRASNVALGLYLEULYSPHEARGGLNLEU
11   LEUTRPPHEHISILESERCYSLEUTHRPHE
12   GLYARGGLUTHRVALLEUGLUTYRLEUVAL
13   SERPHEGLYVALTRPILEARGTHRPROPRO
14   ALATYRARGPROPROASNALAPROILELEU
15   SERTHRLEUPROGLUTHRTHRVALVAL

Samples:

sample_1: Hepatitis B virus coat protein monomer, chain 1, [U-13C; U-15N; U-2H], 150 ± 3 uM

sample_conditions_1: ionic strength: < 30 mM; pH: 9.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY_HNCOsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HN(CA)CBsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D TROSY-HN(COCA)CBsample_1isotropicsample_conditions_1
3D TROSY-HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HN(CACO)NHsample_1isotropicsample_conditions_1

Software:

FELIX v2004, Accelrys - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

Related Database Links:

UNP P03147
PDB
DBJ BAA85372 BAA85376
EMBL CAA59662 CAM58608 CAM58609 CAM58712 CAM58713
GB AAA02846 AAA02847 AAA45486 AAL31811 AAL31812
SP P03147 Q9QMI2
AlphaFold P03147 P03147 Q9QMI2

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