BMRB Entry 19517

Name: Micelle-solubilized transmembrane domain of the hepatitis C virus glycoprotein E1
Published: 2014-02-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19517

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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:

Micelle-solubilized transmembrane domain of the hepatitis C virus glycoprotein E1

Deposition date:

2013-09-21

Original release date:

2014-02-12

Authors:

Zazrin, Hadas; Shaked, Hadassa; Chill, Jordan

Citation:

Citation: Zazrin, Hadas; Shaked, Hadassa; Chill, Jordan. "Architecture of the hepatitis C virus E1 glycoprotein transmembrane domain studied by NMR." Biochim. Biophys. Acta 1838, 784-792 (2014).
PubMed: 24192053

Assembly members:

Assembly members:
E1TM, polymer, 54 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Hepatitis C virus Taxonomy ID: 11103 Superkingdom: Viruses Kingdom: not available Genus/species: Hepacivirus Hepatitis C virus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
E1TM: DPEREKAHWGVLAGIAYYSM VGNWAKVLIVLLLFAGVDAE REKDPHHHHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	171
15N chemical shifts	61
1H chemical shifts	61

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	E1TM	1

Entities:

Entity 1, E1TM 54 residues - Formula weight is not available

Residues 345-349 are an artificial extension for solubility Residues 350-383 are the E1 TM domain Residues 384-389 are an artificial extension for solubility Residues 390-397 are a his-tag

1

ASP

PRO

GLU

ARG

GLU

LYS

ALA

HIS

TRP

GLY

2

VAL

LEU

ALA

GLY

ILE

ALA

TYR

SER

MET

3

VAL

GLY

ASN

TRP

ALA

LYS

VAL

LEU

ILE

VAL

4

LEU

PHE

ALA

GLY

VAL

ASP

ALA

GLU

5

ARG

GLU

LYS

ASP

PRO

HIS

6

HIS

Samples:

sample_1: E1TM, [U-100% 13C; U-100% 15N; U-80% 2H], 0.3 – 0.6 mM; H2O 93 ± 1 %; D2O, [U-99% 2H], 7 ± 1 %; sodium chloride 20 ± 1 mM; sodium phosphate 20 ± 1 mM; SDS 300 ± 20 mM

sample_2: E1TM, [U-100% 13C; U-100% 15N; U-80% 2H], 0.3 – 0.6 mM; H2O 93 ± 1 %; D2O, [U-99% 2H], 7 ± 1 %; sodium chloride 20 ± 1 mM; sodium phosphate 20 ± 1 mM; LPPG 40 ± 4 mM

sample_conditions_1: ionic strength: 180 mM; pH: 6.7; pressure: 1 atm; temperature: 318 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - chemical shift assignment, collection

NMR spectrometers:

Bruker DRX 700 MHz

EMBL	CAD53672 CAD53673 CAD53674 CAD53675 CAD53676
GB	AAK27140 AAK27141 AAK59220 AAU93985 AAU93986