BMRB Entry 26927

Name: Backbone assignment of unlinked NS2B-NS3 Protease of Zika Virus in complex with acetyl-lysine-arginine
Published: 2016-12-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26927

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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 assignment of unlinked NS2B-NS3 Protease of Zika Virus in complex with acetyl-lysine-arginine

Deposition date:

2016-10-28

Original release date:

2016-12-15

Authors:

Li, Yan; Zhang, Zhenzhen; Loh, Ying Ru; Phoo, Wint Wint; Kang, CongBao; Luo, Dahai

Citation:

Citation: Zhang, Zhenzhen; Li, Yan; Loh, Ying Ru; Phoo, Wint Wint; Hung, Alvin; Kang, CongBao; Luo, Dahai. "Crystal structure of unlinked NS2B-NS3 protease from Zika virus" Science 354, 1597-1600 (2016).
PubMed: 27940580

Assembly members:

Assembly members:
NS2B_fragment, polymer, 73 residues, Formula weight is not available
NS3_fragment, polymer, 177 residues, Formula weight is not available
acetyl-lysine-arginine, polymer, 3 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Zika virus Taxonomy ID: 64320 Superkingdom: Viruses Kingdom: not available Genus/species: Zika virus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NS2B_fragment: MGSSHHHHHHSSGLVPRGSH MTGKSVDMYIERAGDITWEK DAEVTGNSPRLDVALDESGD FSLVEEDGPPMRE
NS3_fragment: SGALWDVPAPKEVKKGETTD GVYRVMTRRLLGSTQVGVGV MQEGVFHTMWHVTKGAALRS GEGRLDPYWGDVKQDLVSYC GPWKLDAAWDGLSEVQLLAV PPGERAKNIQTLPGIFKTKD GDIGAVALDYPAGTSGSPIL DKCGRVIGLYGNGVVIKNGS YVSAITQGKREEETPVE
acetyl-lysine-arginine: XKR

Data sets:

assigned_chemical_shifts

Data type	Count
13C chemical shifts	663
15N chemical shifts	221
1H chemical shifts	221

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NS2B fragment (45-96)	1
2	NS3 fragment (1-177)	2
3	acetyl-lysine-arginine	3

Entities:

Entity 1, NS2B fragment (45-96) 73 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

THR

GLY

LYS

SER

VAL

ASP

MET

TYR

ILE

4

GLU

ARG

ALA

GLY

ASP

ILE

THR

TRP

GLU

LYS

5

ASP

ALA

GLU

VAL

THR

GLY

ASN

SER

PRO

ARG

6

LEU

ASP

VAL

ALA

LEU

ASP

GLU

SER

GLY

ASP

7

PHE

SER

LEU

VAL

GLU

ASP

GLY

PRO

8

MET

ARG

GLU

Entity 2, NS3 fragment (1-177) 177 residues - Formula weight is not available

1

SER

GLY

ALA

LEU

TRP

ASP

VAL

PRO

ALA

PRO

2

LYS

GLU

VAL

LYS

GLY

GLU

THR

ASP

3

GLY

VAL

TYR

ARG

VAL

MET

THR

ARG

LEU

4

LEU

GLY

SER

THR

GLN

VAL

GLY

VAL

GLY

VAL

5

MET

GLN

GLU

GLY

VAL

PHE

HIS

THR

MET

TRP

6

HIS

VAL

THR

LYS

GLY

ALA

LEU

ARG

SER

7

GLY

GLU

GLY

ARG

LEU

ASP

PRO

TYR

TRP

GLY

8

ASP

VAL

LYS

GLN

ASP

LEU

VAL

SER

TYR

CYS

9

GLY

PRO

TRP

LYS

LEU

ASP

ALA

TRP

ASP

10

GLY

LEU

SER

GLU

VAL

GLN

LEU

ALA

VAL

11

PRO

GLY

GLU

ARG

ALA

LYS

ASN

ILE

GLN

12

THR

LEU

PRO

GLY

ILE

PHE

LYS

THR

LYS

ASP

13

GLY

ASP

ILE

GLY

ALA

VAL

ALA

LEU

ASP

TYR

14

PRO

ALA

GLY

THR

SER

GLY

SER

PRO

ILE

LEU

15

ASP

LYS

CYS

GLY

ARG

VAL

ILE

GLY

LEU

TYR

16

GLY

ASN

GLY

VAL

ILE

LYS

ASN

GLY

SER

17

TYR

VAL

SER

ALA

ILE

THR

GLN

GLY

LYS

ARG

18

GLU

THR

PRO

VAL

GLU

Entity 3, acetyl-lysine-arginine 3 residues - Formula weight is not available

1

ACE

LYS

ARG

Samples:

sample_1: NS2B fragment, [U-13C; U-15N; U-2H], 0.8 mM; NS3 fragment, [U-13C; U-15N; U-2H], 0.8 mM; HEPES 20 mM; sodium chloride 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 170 mM; pH: 7.3; 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_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific, Keller and Wuthrich - chemical shift assignment, processing

NMR spectrometers:

Bruker Avance 700 MHz

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