BMRB Entry 26933

Name: Backbone assignment of unlinked NS2B-NS3 Protease of Zika Virus in complex with acetyl-lysine-arginine aldehyde
Published: 2017-07-17

Click here to enlarge.

PDB ID: 5h6v
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26933
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

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

Deposition date:

2016-11-04

Original release date:

2017-07-17

Authors:

Li, Yan; Zhang, Zhenzhen; Phoo, Wint Wint; Loh, Ying Ru; Wang, Wei Ling; Chen, Ming Wei; Liu, Shuang; Hung, Alvin; Keller, Thomas H; Luo, Dahai; Kang, CongBao

Citation:

Citation: Li, Yan; Zhang, Zhenzhen; Phoo, Wint Wint; Loh, Ying Ru; Wang, Weiling; Liu, Shuang; Chen, Ming Wei; Hung, Alvin; Keller, Thomas; Luo, Dahai; Kang, CongBao. "Structural Dynamics of Zika Virus NS2B-NS3 Protease Binding to Dipeptide Inhibitors" Structure 2126, 30186-30187 (2017).
PubMed: 28689970

Assembly members:

Assembly members:
NS2B_fragment, polymer, 73 residues, Formula weight is not available
NS3_fragment, polymer, 178 residues, Formula weight is not available
entity_7HS, non-polymer, 328.411 Da.

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: GSGALWDVPAPKEVKKGETT DGVYRVMTRKLLGSTQVGVG VMQEGVFHTMWHVTKGAALR SGEGRLDPYWGDVKQDLVSY CGPWKLDAAWDGLSEVQLLA VPPGERAKNIQTLPGIFKTK DGDIGAVALDYPAGTSGSPI LDKCGRVIGLYGNGVVIKNG SYVSAITQGKREEETPVE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	592
15N chemical shifts	191
1H chemical shifts	191

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 aldehyde	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) 178 residues - Formula weight is not available

1

GLY

SER

GLY

ALA

LEU

TRP

ASP

VAL

PRO

ALA

2

PRO

LYS

GLU

VAL

LYS

GLY

GLU

THR

3

ASP

GLY

VAL

TYR

ARG

VAL

MET

THR

ARG

LYS

4

LEU

GLY

SER

THR

GLN

VAL

GLY

VAL

GLY

5

VAL

MET

GLN

GLU

GLY

VAL

PHE

HIS

THR

MET

6

TRP

HIS

VAL

THR

LYS

GLY

ALA

LEU

ARG

7

SER

GLY

GLU

GLY

ARG

LEU

ASP

PRO

TYR

TRP

8

GLY

ASP

VAL

LYS

GLN

ASP

LEU

VAL

SER

TYR

9

CYS

GLY

PRO

TRP

LYS

LEU

ASP

ALA

TRP

10

ASP

GLY

LEU

SER

GLU

VAL

GLN

LEU

ALA

11

VAL

PRO

GLY

GLU

ARG

ALA

LYS

ASN

ILE

12

GLN

THR

LEU

PRO

GLY

ILE

PHE

LYS

THR

LYS

13

ASP

GLY

ASP

ILE

GLY

ALA

VAL

ALA

LEU

ASP

14

TYR

PRO

ALA

GLY

THR

SER

GLY

SER

PRO

ILE

15

LEU

ASP

LYS

CYS

GLY

ARG

VAL

ILE

GLY

LEU

16

TYR

GLY

ASN

GLY

VAL

ILE

LYS

ASN

GLY

17

SER

TYR

VAL

SER

ALA

ILE

THR

GLN

GLY

LYS

18

ARG

GLU

THR

PRO

VAL

GLU

Entity 3, acetyl-lysine-arginine aldehyde - C14 H28 N6 O3 - 328.411 Da.

1

7HS

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