BMRB Entry 50839

Name: NMR backbone resonance assignment of Japanese encephalitis virus capsid protein
Published: 2021-04-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50839

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:

NMR backbone resonance assignment of Japanese encephalitis virus capsid protein

Deposition date:

2021-03-21

Original release date:

2021-04-05

Authors:

Guo, Yuting; Cheng, Kai; Wu, Qiong; Xu, Guohua; Jiang, Ling; Li, Conggang

Citation:

Citation: Guo, Yuting; Yao, Chendie; Cheng, Kai; Wu, Qiong; Xu, Guohua; Jiang, Ling; Li, Conggang. "NMR backbone resonance assignment of Japanese encephalitis virus capsid protein" Biomol. NMR Assign. 15, 403-407 (2021).
PubMed: 34170495

Assembly members:

Assembly members:
entity_1, polymer, 119 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Flavivirus Taxonomy ID: 11072 Superkingdom: Viruses Kingdom: not available Genus/species: Flavivirus Japanese encephalitis virus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HHHHHHMTKKPGGPGKNRAI NMLKRGLPRVFPLVGVKRVV MSLLDGRGPVRFVLALITFF KFTALAPTKALLGRWKAVEK SVAMKHLTSFKRELGTLIDA VNKRGRKQNKRGGNEGSIM

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	305
15N chemical shifts	103
1H chemical shifts	104

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Japanese encephalitis virus capsid protein	1

Entities:

Entity 1, Japanese encephalitis virus capsid protein 119 residues - Formula weight is not available

1

HIS

MET

THR

LYS

2

PRO

GLY

PRO

GLY

LYS

ASN

ARG

ALA

ILE

3

ASN

MET

LEU

LYS

ARG

GLY

LEU

PRO

ARG

VAL

4

PHE

PRO

LEU

VAL

GLY

VAL

LYS

ARG

VAL

5

MET

SER

LEU

ASP

GLY

ARG

GLY

PRO

VAL

6

ARG

PHE

VAL

LEU

ALA

LEU

ILE

THR

PHE

7

LYS

PHE

THR

ALA

LEU

ALA

PRO

THR

LYS

ALA

8

LEU

GLY

ARG

TRP

LYS

ALA

VAL

GLU

LYS

9

SER

VAL

ALA

MET

LYS

HIS

LEU

THR

SER

PHE

10

LYS

ARG

GLU

LEU

GLY

THR

LEU

ILE

ASP

ALA

11

VAL

ASN

LYS

ARG

GLY

ARG

LYS

GLN

ASN

LYS

12

ARG

GLY

ASN

GLU

GLY

SER

ILE

MET

Samples:

sample_1: entity_1, [U-2H; U-13C; U-15N], 0.42 mM; sodium phosphate 20 mM; sodium chloride 200 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - data analysis

SPARKY - chemical shift assignment

TOPSPIN - collection

NMR spectrometers:

Bruker Avance 800 MHz

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