BMRB Entry 15225

Name: 1H, 13C, and 15N resonance assignments of domain 2 of non-structural protein 5A (NS5A) of hepatitis C virus
Published: 2007-10-29

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15225

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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:

1H, 13C, and 15N resonance assignments of domain 2 of non-structural protein 5A (NS5A) of hepatitis C virus

Deposition date:

2007-04-26

Original release date:

2007-10-29

Authors:

Liang, Yu; Ye, Hong; Kang, Cong Bao; Yoon, Ho Sup

Citation:

Citation: Liang, Yu; Ye, Hong; Kang, Cong Bao; Yoon, Ho Sup. "Domain 2 of Non-structural Protein 5A (NS5A) of Hepatitis C Virus is Natively Unfolded" Biochemistry 46, 11550-11558 (2007).
PubMed: 17880107

Assembly members:

Assembly members:
Domain_2_of_Non-structural_Protein_5A_(NS5AD2), polymer, 102 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-Ub-NS5A-D2-His

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Domain_2_of_Non-structural_Protein_5A_(NS5AD2): KATCTANHDSPDAELIEANL LWRQEMGGNITRVESENKVV ILDSFDPLVAEEDEREVSVP AEILRKSRRFARALPVWARP DYNPPLVETWKKPDYEHHHH HH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	385
15N chemical shifts	93
1H chemical shifts	636

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Domain 2 of Non-structural Protein 5A (NS5AD2)	1

Entities:

Entity 1, Domain 2 of Non-structural Protein 5A (NS5AD2) 102 residues - Formula weight is not available

1

LYS

ALA

THR

CYS

THR

ALA

ASN

HIS

ASP

SER

2

PRO

ASP

ALA

GLU

LEU

ILE

GLU

ALA

ASN

LEU

3

LEU

TRP

ARG

GLN

GLU

MET

GLY

ASN

ILE

4

THR

ARG

VAL

GLU

SER

GLU

ASN

LYS

VAL

5

ILE

LEU

ASP

SER

PHE

ASP

PRO

LEU

VAL

ALA

6

GLU

ASP

GLU

ARG

GLU

VAL

SER

VAL

PRO

7

ALA

GLU

ILE

LEU

ARG

LYS

SER

ARG

PHE

8

ALA

ARG

ALA

LEU

PRO

VAL

TRP

ALA

ARG

PRO

9

ASP

TYR

ASN

PRO

LEU

VAL

GLU

THR

TRP

10

LYS

PRO

ASP

TYR

GLU

HIS

11

HIS

Samples:

sample_1: Domain 2 of Non-structural Protein 5A (NS5AD2), [U-15N], 0.6 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%

sample_2: Domain 2 of Non-structural Protein 5A (NS5AD2), [U-13C; U-15N], 0.6 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

FELIX v2004, Accelrys Software Inc. - data analysis

NMR spectrometers:

Bruker Avance 700 MHz

EMBL	CAJ20207 CAJ20220
GB	AAA45534 AAA45676 AAA45677 AAB66324 AAB67036
REF	NP_671491 NP_751927
SP	P26664 P27958
AlphaFold	P26664 P27958