BMRB Entry 50102

Name: Nipah virus phosphoprotein residues 299-401
Published: 2020-01-10

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR50102

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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 299-401

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 299-401, polymer, 111 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 299-401: MDNKSTDVPGAGPKDSAVKE EPPQKRLPMLAEEFECSGSE DPIIRELLKENSLINCQQGK DAQPPYHWSIERSISPDKTE IVNGAVQTADRQRPGTPMPK SRGLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	292
15N chemical shifts	89
1H chemical shifts	89

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 111 residues - Formula weight is not available

1

MET

ASP

ASN

LYS

SER

THR

ASP

VAL

PRO

GLY

2

ALA

GLY

PRO

LYS

ASP

SER

ALA

VAL

LYS

GLU

3

GLU

PRO

GLN

LYS

ARG

LEU

PRO

MET

LEU

4

ALA

GLU

PHE

GLU

CYS

SER

GLY

SER

GLU

5

ASP

PRO

ILE

ARG

GLU

LEU

LYS

GLU

6

ASN

SER

LEU

ILE

ASN

CYS

GLN

GLY

LYS

7

ASP

ALA

GLN

PRO

TYR

HIS

TRP

SER

ILE

8

GLU

ARG

SER

ILE

SER

PRO

ASP

LYS

THR

GLU

9

ILE

VAL

ASN

GLY

ALA

VAL

GLN

THR

ALA

ASP

10

ARG

GLN

ARG

PRO

GLY

THR

PRO

MET

PRO

LYS

11

SER

ARG

GLY

LEU

GLU

HIS

12

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