BMRB Entry 26902

Name: Backbone chemical shift assignment of the N-terminal domain of the phosphoprotein of Respiratory Syncytial Virus
Published: 2017-02-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26902

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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:

Backbone chemical shift assignment of the N-terminal domain of the phosphoprotein of Respiratory Syncytial Virus

Deposition date:

2016-09-22

Original release date:

2017-02-15

Authors:

Lassoued, Safa; Pereira, Nelson; Fix, Jenna; Galloux, Marie; Eleouet, Jean-Francois; Sizun, Christina

Citation:

Citation: Pereira, Nelson; Cardone, Christophe; Lassoued, Safa; Galloux, Marie; Fix, Jenna; Assrir, Nadine; Lescop, Ewen; Bontems, Francois; Eleouet, Jean-Francois; Sizun, Christina. "New Insights into Structural Disorder in Human Respiratory Syncytial Virus Phosphoprotein and Implications for Binding of Protein Partners" J. Biol. Chem. 292, 2120-2131 (2017).
PubMed: 28031463

Assembly members:

Assembly members:
P1-126, polymer, 128 residues, 14476.6662 Da.

Natural source:

Natural source: Common Name: human RSV Taxonomy ID: 11250 Superkingdom: Viruses Kingdom: not available Genus/species: Orthopneumovirus HRSV

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
P1-126: GSMEKFAPEFHGEDANNRAT KFLESIKGKFTSPKDPKKKD SIISVNSIDIEVTKESPITS NSTIINPTNETDDNAGNKPN YQRKPLVSFKEDPIPSDNPF SKLYKETIETFDNNEEESSY SYEEINDQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	311
15N chemical shifts	119
1H chemical shifts	234

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	P1-126	1

Entities:

Entity 1, P1-126 128 residues - 14476.6662 Da.

P1-126 is a phosphoprotein fragment that contains residues M1-Q126 and two N-terminal residues (GS) that are left over from a cleaved GST-tag.

1

GLY

SER

MET

GLU

LYS

PHE

ALA

PRO

GLU

PHE

2

HIS

GLY

GLU

ASP

ALA

ASN

ARG

ALA

THR

3

LYS

PHE

LEU

GLU

SER

ILE

LYS

GLY

LYS

PHE

4

THR

SER

PRO

LYS

ASP

PRO

LYS

ASP

5

SER

ILE

SER

VAL

ASN

SER

ILE

ASP

ILE

6

GLU

VAL

THR

LYS

GLU

SER

PRO

ILE

THR

SER

7

ASN

SER

THR

ILE

ASN

PRO

THR

ASN

GLU

8

THR

ASP

ASN

ALA

GLY

ASN

LYS

PRO

ASN

9

TYR

GLN

ARG

LYS

PRO

LEU

VAL

SER

PHE

LYS

10

GLU

ASP

PRO

ILE

PRO

SER

ASP

ASN

PRO

PHE

11

SER

LYS

LEU

TYR

LYS

GLU

THR

ILE

GLU

THR

12

PHE

ASP

ASN

GLU

SER

TYR

13

SER

TYR

GLU

ILE

ASN

ASP

GLN

Samples:

sample_P1-126: P1-126, [U-13C; U-15N], 0.05 ± 5e-06 mM; sodium phosphate 20.00 ± 0.002 mM; sodium chloride 100.00 ± 0.01 mM

CondSet1: ionic strength: 0.100 M; pH: 6.500; pressure: 1.000 atm; temperature: 288.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_P1-126	isotropic	CondSet1
3D HNCO	sample_P1-126	isotropic	CondSet1
3D HNCA	sample_P1-126	isotropic	CondSet1
3D HN(CO)CA	sample_P1-126	isotropic	CondSet1
3D HNCACB	sample_P1-126	isotropic	CondSet1
3D HNHA	sample_P1-126	isotropic	CondSet1

Software:

CcpNmr_Analysis v2.2, Bruker Biospin, CCPN - chemical shift assignment, collection, data analysis, peak picking, processing

NMR spectrometers:

Bruker Avance 600 MHz

UniProt	P12579
AlphaFold	P12579