BMRB Entry 16477

Name: Solution structure of the transmembrane proximal region of the hepatis C virus E1 glycoprotein.
Published: 2009-12-11

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PDB ID: 2knu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16477
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the transmembrane proximal region of the hepatis C virus E1 glycoprotein.

Deposition date:

2009-09-04

Original release date:

2009-12-11

Authors:

Spadaccini, Roberta; D'Errico, Gerardino; D'Alessio, Viviana; Notomista, Eugenio; Bianchi, Alessia; Merola, Marcello; Picone, Delia

Citation:

Citation: Spadaccini, Roberta; Notomista, Gerardino; Bianchi, Viviana; Merola, Eugenio; Picone, Alessia. "Structural characterization of the transmembrane proximal region of the hepatitis C virus E1 glycoprotein." Biochim. Biophys. Acta 1798, 344-353 (2010).
PubMed: 19891955

Assembly members:

Assembly members:
e1_peptide, polymer, 29 residues, 3328.988 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
e1_peptide: TGHRMAWDMMMNWSPTAALV VAQLLRIPQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	205

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	e1	1

Entities:

Entity 1, e1 29 residues - 3328.988 Da.

1

THR

GLY

HIS

ARG

MET

ALA

TRP

ASP

MET

2

MET

ASN

TRP

SER

PRO

THR

ALA

LEU

VAL

3

VAL

ALA

GLN

LEU

ARG

ILE

PRO

GLN

Samples:

sample_1: e1 1 mM; D2O 20%; hexafluoroisopropanol 80%

sample_2: e1 1 mM; H2O 20%; hexafluoroisopropanol 80%

sample_conditions: pH: 4.5; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions
2D 1H-1H COSY	sample_2	isotropic	sample_conditions
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions
2D 1H-1H COSY	sample_1	isotropic	sample_conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

Bruker DRX 600 MHz

PDB	2KNU
DBJ	BAC41283 BAC41284 BAN91312
EMBL	CAA37292 CAD53863 CAD53864 CAD53866 CAD53867
GB	AAA45563 AAB02127 AAB02128 AAB66324 AAB67036
REF	NP_671491 NP_751920