BMRB Entry 26906

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

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26906

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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 C-terminal domain of Respiratory Syncytial Virus phosphoprotein

Deposition date:

2016-09-22

Original release date:

2017-02-15

Authors:

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

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:
P-CTD, polymer, 83 residues, 9323.1498 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):
P-CTD: GSSARDGIRDAMVGLREEMI EKIRTEALMTNDRLEAMARL RNEESEKMAKDTSDEVSLNP TSEKLNNLLEGNDSDNDLSL EDF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	238
15N chemical shifts	81
1H chemical shifts	159

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	P-CTD	1

Entities:

Entity 1, P-CTD 83 residues - 9323.1498 Da.

P-CTD is a phosphoprotein fragment corresponding to the C-terminal domains of hRSV (residues S161-DF241). The two N-terminal residues (GS) are left over from a cleaved GST-tag.

1

GLY

SER

ALA

ARG

ASP

GLY

ILE

ARG

ASP

2

ALA

MET

VAL

GLY

LEU

ARG

GLU

MET

ILE

3

GLU

LYS

ILE

ARG

THR

GLU

ALA

LEU

MET

THR

4

ASN

ASP

ARG

LEU

GLU

ALA

MET

ALA

ARG

LEU

5

ARG

ASN

GLU

SER

GLU

LYS

MET

ALA

LYS

6

ASP

THR

SER

ASP

GLU

VAL

SER

LEU

ASN

PRO

7

THR

SER

GLU

LYS

LEU

ASN

LEU

GLU

8

GLY

ASN

ASP

SER

ASP

ASN

ASP

LEU

SER

LEU

9

GLU

ASP

PHE

Samples:

P-CTD_15N13C: P-CTD, [U-13C; U-15N; U-2H], 0.15 ± 2e-06 mM; sodium phosphate 20.00 ± 0.002 mM; soudim 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	P-CTD_15N13C	isotropic	CondSet1
3D HNCA	P-CTD_15N13C	isotropic	CondSet1
3D HN(CO)CA	P-CTD_15N13C	isotropic	CondSet1
3D HNHA	P-CTD_15N13C	isotropic	CondSet1
3D HNCO	P-CTD_15N13C	isotropic	CondSet1
3D HNCACB	P-CTD_15N13C	isotropic	CondSet1
3D CBCA(CO)NH	P-CTD_15N13C	isotropic	CondSet1

Software:

CcpNmr_Analysis v2.2, CCPN - chemical shift assignment, data analysis, peak picking

Topspin v3.1, Bruker - collection, processing

NMR spectrometers:

Bruker Avance 600 MHz

UniProt	P12579
AlphaFold	P12579