BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 28122

Title: 1H-13C-15N solid-state NMR assignment of a second conformation of HBV capsid   PubMed: 33879615

Deposition date: 2020-05-15 Original release date: 2021-04-27

Authors: Lecoq, Lauriane; Bockmann, Anja; Wang, Shishan; Dujardin, Marie; Fogeron, Marie-Laure; Schledorn, Maarten; Montserret, Roland; Bressanelli, Stephane; Meier, Beat; Nassal, Michael

Citation: Lecoq, Lauriane; Wang, Shishan; Dujardin, Marie; Zimmermann, Peter; Schuster, Leonard; Fogeron, Marie-Laure; Briday, Mathilde; Schledorn, Maarten; Wiegand, Thomas; Cole, Laura; Montserret, Roland; Bressanelli, Stephane; Meier, Beat; Nassal, Michael; Bockmann, Anja. "A pocket-factor-triggered conformational switch in the hepatitis B virus capsid"  Proc. Natl. Acad. Sci. U. S. A. 118, e2022464118-e2022464118 (2021).

Assembly members:
Cp183, polymer, 183 residues, 22244 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pRSF_T7

Entity Sequences (FASTA):
Cp183: MDIDPYKEFGATVELLSFLP SDFFPSVRDLLDTASALYRE ALESPEHCSPHHTALRQAIL CWGELMTLATWVGVNLEDPA SRDLVVSYVNTNMGLKFRQL LWFHISCLTFGRETVIEYLV SFGVWIRTPPAYRPPNAPIL STLPETTVVRRRGRSPRRRT PSPRRRRSQSPRRRRSQSRE SQC

Data sets:
Data typeCount
13C chemical shifts517
15N chemical shifts136
1H chemical shifts117

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Capsid1

Entities:

Entity 1, Capsid 183 residues - 22244 Da.

1   METASPILEASPPROTYRLYSGLUPHEGLY
2   ALATHRVALGLULEULEUSERPHELEUPRO
3   SERASPPHEPHEPROSERVALARGASPLEU
4   LEUASPTHRALASERALALEUTYRARGGLU
5   ALALEUGLUSERPROGLUHISCYSSERPRO
6   HISHISTHRALALEUARGGLNALAILELEU
7   CYSTRPGLYGLULEUMETTHRLEUALATHR
8   TRPVALGLYVALASNLEUGLUASPPROALA
9   SERARGASPLEUVALVALSERTYRVALASN
10   THRASNMETGLYLEULYSPHEARGGLNLEU
11   LEUTRPPHEHISILESERCYSLEUTHRPHE
12   GLYARGGLUTHRVALILEGLUTYRLEUVAL
13   SERPHEGLYVALTRPILEARGTHRPROPRO
14   ALATYRARGPROPROASNALAPROILELEU
15   SERTHRLEUPROGLUTHRTHRVALVALARG
16   ARGARGGLYARGSERPROARGARGARGTHR
17   PROSERPROARGARGARGARGSERGLNSER
18   PROARGARGARGARGSERGLNSERARGGLU
19   SERGLNCYS

Samples:

sample_1: Cp183, [U-99% 13C; U-99% 15N], 20 mg/mL

conditions_rotor_3.2mm: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 277 K

conditions_rotor_0.7mm: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D DARRsample_1isotropicconditions_rotor_3.2mm
2D NCAsample_1isotropicconditions_rotor_3.2mm
2D NCOsample_1isotropicconditions_rotor_3.2mm
3D NCACXsample_1isotropicconditions_rotor_3.2mm
3D CANCOsample_1isotropicconditions_rotor_3.2mm
3D NCOCXsample_1isotropicconditions_rotor_3.2mm
2D hNHsample_1isotropicconditions_rotor_0.7mm
3D hCANHsample_1isotropicconditions_rotor_0.7mm
3D hCONHsample_1isotropicconditions_rotor_0.7mm
3D hCAcoNHsample_1isotropicconditions_rotor_0.7mm

Software:

TOPSPIN, Bruker Biospin - collection, processing

CcpNmr, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 850 MHz

Related Database Links:

UNP P03146

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts