BMRB Entry 15767

Name: Backbone Resonance Assignments of the N-terminal half of hepatitis core protein
Published: 2008-11-03

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15767

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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 Resonance Assignments of the N-terminal half of hepatitis core protein

Deposition date:

2008-05-12

Original release date:

2008-11-03

Authors:

DUVIGNAUD, Jean-Baptiste; SAVARD, Christian; FROMENTIN, Remi; MAJEAU, Nathalie; LECLERC, Denis; GAGNE, Stephane

Citation:

Citation: DUVIGNAUD, Jean-Baptiste; SAVARD, Christian; FROMENTIN, Remi; MAJEAU, Nathalie; LECLERC, Denis; GAGNE, Stephane. "Structure and dynamics of the N-terminal half of hepatitis C virus core protein: an intrinsically unstructured protein" Biochem. Biophys. Res. Commun. 378, 27-31 (2009).
PubMed: 18992225

Assembly members:

Assembly members:
HCV_core_protein, polymer, 88 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: pet3D

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HCV_core_protein: MSTNPKPQRKTKRNTNRRPQ DVKFPGGGQIVGGVYLLPRR GPRLGVRATRKTSERSQPRG RRQPIPKARRPEGRTWAQPG YPHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	157
15N chemical shifts	48
1H chemical shifts	48

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-terminal half	1

Entities:

Entity 1, N-terminal half 88 residues - Formula weight is not available

1

MET

SER

THR

ASN

PRO

LYS

PRO

GLN

ARG

LYS

2

THR

LYS

ARG

ASN

THR

ASN

ARG

PRO

GLN

3

ASP

VAL

LYS

PHE

PRO

GLY

GLN

ILE

4

VAL

GLY

VAL

TYR

LEU

PRO

ARG

5

GLY

PRO

ARG

LEU

GLY

VAL

ARG

ALA

THR

ARG

6

LYS

THR

SER

GLU

ARG

SER

GLN

PRO

ARG

GLY

7

ARG

GLN

PRO

ILE

PRO

LYS

ALA

ARG

8

PRO

GLU

GLY

ARG

THR

TRP

ALA

GLN

PRO

GLY

9

TYR

PRO

HIS

Samples:

sample_1: HCV core protein, [U-100% 13C; U-100% 15N], 0.4 mM; Phosphate 25 mM; NaCl 50 mM; DSS 0.2 mM; NaN3 0.1%

sample_conditions_1: ionic strength: 75 mM; pH: 6.6; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

NMRView v5.2.2.01, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	15768 4669
PDB	1CWX 1XCQ 1XCT 1XF5
DBJ	BAA00452 BAA00705 BAA00706 BAA00968 BAA01529
EMBL	CAA03854 CAA43788 CAA43790 CAA43793 CAA46717
GB	AAA16300 AAA16311 AAA20153 AAA20154 AAA21040
PIR	JQ1926
REF	NP_671491 YP_001469632
SP	O39929 O92972 P26662 P26663 P26664
AlphaFold	O39929 O92972 P26662 P26663 P26664