BMRB Entry 50099

Name: Nipah virus phosphoprotein residues 91-190
Published: 2020-01-10

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR50099

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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 91-190

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 91-190, polymer, 109 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 91-190: MRVSNTRDWAEGSDDIQLDP VVTDVVYHDHGGECTGYGFT SSPERGWSDYTSGANNGNVC LVSDAKMLSYAPEIAVSKED RETDLVHLENKLSTTGLNPT ALEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	283
15N chemical shifts	93
1H chemical shifts	93

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 109 residues - Formula weight is not available

1

MET

ARG

VAL

SER

ASN

THR

ARG

ASP

TRP

ALA

2

GLU

GLY

SER

ASP

ILE

GLN

LEU

ASP

PRO

3

VAL

THR

ASP

VAL

TYR

HIS

ASP

HIS

4

GLY

GLU

CYS

THR

GLY

TYR

GLY

PHE

THR

5

SER

PRO

GLU

ARG

GLY

TRP

SER

ASP

TYR

6

THR

SER

GLY

ALA

ASN

GLY

ASN

VAL

CYS

7

LEU

VAL

SER

ASP

ALA

LYS

MET

LEU

SER

TYR

8

ALA

PRO

GLU

ILE

ALA

VAL

SER

LYS

GLU

ASP

9

ARG

GLU

THR

ASP

LEU

VAL

HIS

LEU

GLU

ASN

10

LYS

LEU

SER

THR

GLY

LEU

ASN

PRO

THR

11

ALA

LEU

GLU

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