BMRB Entry 28138

Name: Resonance Assignments for the Rabies Phosphoprotein RavP C terminus (140-297)
Published: 2020-08-31

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28138

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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:

Resonance Assignments for the Rabies Phosphoprotein RavP C terminus (140-297)

Deposition date:

2020-07-30

Original release date:

2020-08-31

Authors:

Jespersen, Nathan; Leyrat, Cedric; Gerard, Francine; Bourhis, Jean-Marie; Blondel, Danielle; Jamin, Marc; Barbar, Elisar

Citation:

Citation: Jespersen, Nathan; Leyrat, Cedric; Gerard, Francine; Bourhis, Jean-Marie; Blondel, Danielle; Jamin, Marc; Barbar, Elisar. "The LC8-RavP ensemble Structure Evinces A Role for LC8 in Regulating Lyssavirus Polymerase Functionality" J. Mol. Biol. 431, 4959-4977 (2019).
PubMed: 31634467

Assembly members:

Assembly members:
Rabies_Phosphoprotein_RavP, polymer, 162 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Rabies lyssavirus Taxonomy ID: 11292 Superkingdom: Viruses Kingdom: not available Genus/species: Lyssavirus Rabies Virus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET24d+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rabies_Phosphoprotein_RavP: GAHMSSEDKSTQTTGRELKK ETTPTPSQRESQSSKARMAA QTASGPPALEWSATNEEDDL SVEAEIAHQIAESFSKKYKF PSRSSGILLYNFEQLKMNLD DIVKEAKNVPGVTRLARDGS KLPLRCVLGWVALANSKKFQ LLVESNKLSKIMQDDLNRYT SC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	450
15N chemical shifts	149
1H chemical shifts	511

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RavP	1

Entities:

Entity 1, RavP 162 residues - Formula weight is not available

GAHM sequence at the N-terminus is non-native

1

GLY

ALA

HIS

MET

SER

GLU

ASP

LYS

SER

2

THR

GLN

THR

GLY

ARG

GLU

LEU

LYS

3

GLU

THR

PRO

THR

PRO

SER

GLN

ARG

GLU

4

SER

GLN

SER

LYS

ALA

ARG

MET

ALA

5

GLN

THR

ALA

SER

GLY

PRO

ALA

LEU

GLU

6

TRP

SER

ALA

THR

ASN

GLU

ASP

LEU

7

SER

VAL

GLU

ALA

GLU

ILE

ALA

HIS

GLN

ILE

8

ALA

GLU

SER

PHE

SER

LYS

TYR

LYS

PHE

9

PRO

SER

ARG

SER

GLY

ILE

LEU

TYR

10

ASN

PHE

GLU

GLN

LEU

LYS

MET

ASN

LEU

ASP

11

ASP

ILE

VAL

LYS

GLU

ALA

LYS

ASN

VAL

PRO

12

GLY

VAL

THR

ARG

LEU

ALA

ARG

ASP

GLY

SER

13

LYS

LEU

PRO

LEU

ARG

CYS

VAL

LEU

GLY

TRP

14

VAL

ALA

LEU

ALA

ASN

SER

LYS

PHE

GLN

15

LEU

VAL

GLU

SER

ASN

LYS

LEU

SER

LYS

16

ILE

MET

GLN

ASP

LEU

ASN

ARG

TYR

THR

17

SER

CYS

Samples:

sample_1: Rabies Phosphoprotein (RavP), [U-99% 13C; U-99% 15N], 150 uM; DSS, [U-2H], 100 uM; sodium azide 1 mM; sodium chloride 100 mM; MES 25 mM; beta-mercaptoethanol 5 mM; EDTA 5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks