BMRB Entry 51186

Name: Backbone chemical shifts of PreS domain from hepatitis B virus envelope protein
Published: 2022-02-23

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51186

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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:

Backbone chemical shifts of PreS domain from hepatitis B virus envelope protein

Deposition date:

2021-11-23

Original release date:

2022-02-23

Authors:

Lecoq, Lauriane; Fogeron, Marie-Laure; Cole, Laura; Montserret, Roland; David, Guillaume; Page, Adeline; Delolme, Frederic; Nassal, Michael; Bockmann, Anja

Citation:

Citation: Fogeron, Marie-Laure; Lecoq, Lauriane; Cole, Laura; Montserret, Roland; David, Guillaume; Page, Adeline; Delolme, Frederic; Nassal, Michael; Bockmann, Anja. "Phosphorylation of the Hepatitis B Virus Large Envelope Protein" Frontiers Mol. Bio. 8, 821755-821755 (2022).
PubMed: 35282608

Assembly members:

Assembly members:
entity_1, polymer, 172 residues, 18430 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: pRSF_T7-H6-GB1-ENLYFQG-preS-Strep-tag-II

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GQNLSTSNPLGFFPDHQLDP AFRANTANPDWDFNPNKDTW PDANKVGAGAFGLGFTPPHG GLLGWSPQAQGILQTLPANP PPASTNRQSGRQPTPLSPPL RNTHPQAMQWNSTTFHQTLQ DPRVRGLYFPAGGSSSGTVN PVLTTASPLSSIFSRIGDPA LNASWSHPQFEK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	465
15N chemical shifts	140
1H chemical shifts	143

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	preS	1

Entities:

Entity 1, preS 172 residues - 18430 Da.

StreptagII in Cter: ASWSHPQFEK

1

GLY

GLN

ASN

LEU

SER

THR

SER

ASN

PRO

LEU

2

GLY

PHE

PRO

ASP

HIS

GLN

LEU

ASP

PRO

3

ALA

PHE

ARG

ALA

ASN

THR

ALA

ASN

PRO

ASP

4

TRP

ASP

PHE

ASN

PRO

ASN

LYS

ASP

THR

TRP

5

PRO

ASP

ALA

ASN

LYS

VAL

GLY

ALA

GLY

ALA

6

PHE

GLY

LEU

GLY

PHE

THR

PRO

HIS

GLY

7

GLY

LEU

GLY

TRP

SER

PRO

GLN

ALA

GLN

8

GLY

ILE

LEU

GLN

THR

LEU

PRO

ALA

ASN

PRO

9

PRO

ALA

SER

THR

ASN

ARG

GLN

SER

GLY

10

ARG

GLN

PRO

THR

PRO

LEU

SER

PRO

LEU

11

ARG

ASN

THR

HIS

PRO

GLN

ALA

MET

GLN

TRP

12

ASN

SER

THR

PHE

HIS

GLN

THR

LEU

GLN

13

ASP

PRO

ARG

VAL

ARG

GLY

LEU

TYR

PHE

PRO

14

ALA

GLY

SER

GLY

THR

VAL

ASN

15

PRO

VAL

LEU

THR

ALA

SER

PRO

LEU

SER

16

SER

ILE

PHE

SER

ARG

ILE

GLY

ASP

PRO

ALA

17

LEU

ASN

ALA

SER

TRP

SER

HIS

PRO

GLN

PHE

18

GLU

LYS

Samples:

sample_1: preS, [U-99% 13C; U-99% 15N], 50 uM; PO4 buffer 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N BESTTROSY	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4 - collection, processing

CcpNMR v2.5 - chemical shift assignment, data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz

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