BMRB Entry 50101

Name: Nipah virus phosphoprotein residues 223-319
Published: 2020-01-10

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR50101

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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:

Nipah virus phosphoprotein residues 223-319

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:
Nipah virus phosphoprotein residues 223-319, polymer, 106 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):
Nipah virus phosphoprotein residues 223-319: MGPQTSRNVNLDSIKLYTSD DEEADQLEFEDEFAGSSSEV IVGISPEDEEPSSVGGKPNE SIGRTIEGQSIRDNLQAKDN KSTDVPGAGPKDSAVKEELE HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	279
15N chemical shifts	90
1H chemical shifts	90

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

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

Entities:

Entity 1, Nipah virus phosphoprotein 106 residues - Formula weight is not available

1

MET

GLY

PRO

GLN

THR

SER

ARG

ASN

VAL

ASN

2

LEU

ASP

SER

ILE

LYS

LEU

TYR

THR

SER

ASP

3

ASP

GLU

ALA

ASP

GLN

LEU

GLU

PHE

GLU

4

ASP

GLU

PHE

ALA

GLY

SER

GLU

VAL

5

ILE

VAL

GLY

ILE

SER

PRO

GLU

ASP

GLU

6

PRO

SER

VAL

GLY

LYS

PRO

ASN

GLU

7

SER

ILE

GLY

ARG

THR

ILE

GLU

GLY

GLN

SER

8

ILE

ARG

ASP

ASN

LEU

GLN

ALA

LYS

ASP

ASN

9

LYS

SER

THR

ASP

VAL

PRO

GLY

ALA

GLY

PRO

10

LYS

ASP

SER

ALA

VAL

LYS

GLU

LEU

GLU

11

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