BMRB Entry 51294

Name: Backbone assignment of Hepatitis B virus core protein Cp149 dimer by solution NMR at pH 7.5
Published: 2022-07-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51294

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone assignment of Hepatitis B virus core protein Cp149 dimer by solution NMR at pH 7.5

Deposition date:

2022-01-27

Original release date:

2022-07-13

Authors:

Lecoq, Lauriane; Briday, Mathilde; Bockmann, Anja

Citation:

Citation: Briday, Mathilde; Hallle, Francois; Lecoq, Lauriane; Radix, Sylvie; Martin, Juliette; Montserret, Roland; Dujardin, Marie; Fogeron, Marie-Laure; Nassal, Michael; Meier, Beat; Lomberget, Thierry; Bockmann, Anja. "Pharmacomodulation of a ligand targeting the HBV capsid hydrophobic pocket" Chem. Sci. 13, 8840-8847 (2022).
PubMed: 36042894

Assembly members:

Assembly members:
entity_1, polymer, 149 residues, Formula weight is not available

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: pET28a2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MDIDPYKEFGATVELLSFLP SDFFPSVRDLLDTASALYRE ALESPEHCSPHHTALRQAIL CWGELMTLATWVGVNLEDPA SRDLVVSYVNTNMGLKFRQL LWFHISCLTFGRETVIEYLV SFGVWIRTPPAYRPPNAPIL STLPETTVV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	182
15N chemical shifts	100
1H chemical shifts	100

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Cp149, chain 1	1
2	Cp149, chain 2	1

Entities:

Entity 1, Cp149, chain 1 149 residues - Formula weight is not available

1

MET

ASP

ILE

ASP

PRO

TYR

LYS

GLU

PHE

GLY

2

ALA

THR

VAL

GLU

LEU

SER

PHE

LEU

PRO

3

SER

ASP

PHE

PRO

SER

VAL

ARG

ASP

LEU

4

LEU

ASP

THR

ALA

SER

ALA

LEU

TYR

ARG

GLU

5

ALA

LEU

GLU

SER

PRO

GLU

HIS

CYS

SER

PRO

6

HIS

THR

ALA

LEU

ARG

GLN

ALA

ILE

LEU

7

CYS

TRP

GLY

GLU

LEU

MET

THR

LEU

ALA

THR

8

TRP

VAL

GLY

VAL

ASN

LEU

GLU

ASP

PRO

ALA

9

SER

ARG

ASP

LEU

VAL

SER

TYR

VAL

ASN

10

THR

ASN

MET

GLY

LEU

LYS

PHE

ARG

GLN

LEU

11

LEU

TRP

PHE

HIS

ILE

SER

CYS

LEU

THR

PHE

12

GLY

ARG

GLU

THR

VAL

ILE

GLU

TYR

LEU

VAL

13

SER

PHE

GLY

VAL

TRP

ILE

ARG

THR

PRO

14

ALA

TYR

ARG

PRO

ASN

ALA

PRO

ILE

LEU

15

SER

THR

LEU

PRO

GLU

THR

VAL

Samples:

sample_1: Cp149 dimer, [U-98% 13C; U-98% 15N; U-98% 2H], 100 uM; HEPES 50 mM; DTT 5 mM

sample_2: Cp149 dimer, [U-99% 13C; U-99% 15N], 100 uM; HEPES 50 mM; DTT 5 mM

sample_conditions_1: ionic strength: 0 M; pH: 7.5; pressure: 1 atm; temperature: 295 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v4 - collection, processing

CcpNMR v2.5 - chemical shift assignment, data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 950 MHz

UNP	P03146
AlphaFold	P03146