BMRB Entry 27845

Name: Solid-state NMR backbone assignment of HBV core protein at 100 kHz
Published: 2019-08-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27845

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

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Title:

Solid-state NMR backbone assignment of HBV core protein at 100 kHz

Deposition date:

2019-03-20

Original release date:

2019-08-14

Authors:

Lecoq, Lauriane; Schledorn, Maarten; Wang, Shishan; Smith-Penzel, Susanne; Malar, Alexander; Callon, Morgane; Nassal, Michael; Meier, Beat; Bockmann, Anja

Citation:

Citation: Lecoq, Lauriane; Schledorn, Maarten; Wang, Shishan; Smith-Penzel, Susanne; Malar, Alexander; Callon, Morgane; Nassal, Michael; Meier, Beat; Bockmann, Anja. "100 kHz MAS Proton-Detected NMR Spectroscopy of Hepatitis B Virus Capsids" Front. Mol. Biosci. 6, .-. (2019).
PubMed: 31396521

Assembly members:

Assembly members:
Cp149, polymer, 149 residues, 17777 Da.

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):
Cp149: MDIDPYKEFGATVELLSFLP SDFFPSVRDLLDTASALYRE ALESPEHCSPHHTALRQAIL CWGELMTLATWVGVNLEDPA SRDLVVSYVNTNMGLKFRQL LWFHISCLTFGRETVIEYLV SFGVWIRTPPAYRPPNAPIL STLPETTVV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	276
15N chemical shifts	131
1H chemical shifts	134

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Cp149	1

Entities:

Entity 1, Cp149 149 residues - 17777 Da.

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:

protonated_Cp149: Cp149, [U-100% 13C; U-100% 15N], 30 mg/mL; TRIS 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 295 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D hNH	protonated_Cp149	isotropic	sample_conditions_1
3D hCANH	protonated_Cp149	isotropic	sample_conditions_1
3D hCONH	protonated_Cp149	isotropic	sample_conditions_1
3D HNcoCA	protonated_Cp149	isotropic	sample_conditions_1
3D hncaCBCANH	protonated_Cp149	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CcpNmr v2.4.2, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 850 MHz

UNP	P03146
BMRB	27317
AlphaFold	P03146