BMRB Entry 15123

Name: SeV Ntail(443-501)
Published: 2007-05-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15123

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

SeV Ntail(443-501)

Deposition date:

2007-02-01

Original release date:

2007-05-14

Authors:

Houben, Klaartje; Marion, Dominique; Tarbouriech, Nicolas; Ruigrok, Rob; Blanchard, Laurence

Citation:

Citation: Houben, Klaartje; Marion, Dominique; Tarbouriech, Nicolas; Ruigrok, Rob; Blanchard, Laurence. "Interaction of the C-terminal domains of sendai virus N and P proteins: comparison of polymerase-nucleocapsid interactions within the paramyxovirus family" J. Virol. 81, 6807-6816 (2007).
PubMed: 17459940

Assembly members:

Assembly members:
SeV_nucleoprotein_Ntail, polymer, 59 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Respirovirus Taxonomy ID: 186938 Superkingdom: Viruses Kingdom: not available Genus/species: Respirovirus not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-TEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SeV_nucleoprotein_Ntail: GESGERWARQVSGGHFVTLH GAERLEEETNDEDVSDIERR IAMRLAERRQEDSATHGDE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	162
15N chemical shifts	70
1H chemical shifts	357

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ntail	1

Entities:

Entity 1, Ntail 59 residues - Formula weight is not available

1

GLY

GLU

SER

GLY

GLU

ARG

TRP

ALA

ARG

GLN

2

VAL

SER

GLY

HIS

PHE

VAL

THR

LEU

HIS

3

GLY

ALA

GLU

ARG

LEU

GLU

THR

ASN

4

ASP

GLU

ASP

VAL

SER

ASP

ILE

GLU

ARG

5

ILE

ALA

MET

ARG

LEU

ALA

GLU

ARG

GLN

6

GLU

ASP

SER

ALA

THR

HIS

GLY

ASP

GLU

Samples:

13C_15N: SeV nucleoprotein Ntail, [U-100% 13C; U-100% 15N], 1 mM; sodium chloride 500 mM; potassium phosphate 50 mM

sample_condition_1: ionic strength: 0.5 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	13C_15N	isotropic	sample_condition_1
3D CBCA(CO)NH	13C_15N	isotropic	sample_condition_1
3D HCCH-TOCSY	13C_15N	isotropic	sample_condition_1
3D C(CO)NH	13C_15N	isotropic	sample_condition_1
3D HNCACB	13C_15N	isotropic	sample_condition_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Varian Avance 600 MHz
Varian Avance 800 MHz

DBJ	BAD74219 BAD74225 BAF73479 BAF73485 BAH59027
EMBL	CAA24945 CAA35092 CAA35715
GB	AAB06278 AAB06284 AAB06290
SP	P04857 P04858 Q07097
AlphaFold	P04857 P04858 Q07097