BMRB Entry 50105

Name: Nipah virus phosphoprotein residues 588-650
Published: 2020-01-10

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR50105

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:

Nipah virus phosphoprotein residues 588-650

Deposition date:

2019-11-29

Original release date:

2020-01-10

Authors:

Jensen, Malene; Blackledge, Martin

Citation:

Citation: Jensen, Malene Ringkjybing; Yabukarski, Filip; Communie, Guillaume; Condamine, Eric; Mas, Caroline; Volchkova, Valentina; Tarbouriech, Nicolas; Bourhis, Jean-Marie; Volchkov, Viktor; Blackledge, Martin; Jamin, Marc. "Structural Description of the Nipah Virus Phosphoprotein and Its Interaction With STAT1" Biophys. J. 118, 2470-2488 (2020).
PubMed: 32348724

Assembly members:

Assembly members:
entity_1, polymer, 72 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Nipah virus Taxonomy ID: 121791 Superkingdom: Virus Kingdom: not available Genus/species: henipavirus Nipah virus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGKNNPELKPVIGRDILEQQ SLFSFDNVKNFRDGSLTNEP YGAAVQLREDLILPELNFEE TNASLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	183
15N chemical shifts	58
1H chemical shifts	57

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Nipah virus phosphoprotein	1

Entities:

Entity 1, Nipah virus phosphoprotein 72 residues - Formula weight is not available

1

MET

GLY

LYS

ASN

PRO

GLU

LEU

LYS

PRO

2

VAL

ILE

GLY

ARG

ASP

ILE

LEU

GLU

GLN

3

SER

LEU

PHE

SER

PHE

ASP

ASN

VAL

LYS

ASN

4

PHE

ARG

ASP

GLY

SER

LEU

THR

ASN

GLU

PRO

5

TYR

GLY

ALA

VAL

GLN

LEU

ARG

GLU

ASP

6

LEU

ILE

LEU

PRO

GLU

LEU

ASN

PHE

GLU

7

THR

ASN

ALA

SER

LEU

GLU

HIS

8

HIS

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.5 mM; Bis-Tris ph 6.0 20 mM; NaCl 150 mM; Arginine 50 mM; glutamate 50 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 298 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 HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCOCA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCOCACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - peak picking

NMR spectrometers:

Agilent Unity 800 MHz

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