BMRB Entry 28137

Name: Triple Resonance Assignments for the Rabies Phosphoprotein RavP (1-152)
Published: 2020-08-31

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28137

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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:

Triple Resonance Assignments for the Rabies Phosphoprotein RavP (1-152)

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, 158 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: GAHMMSKIFVNPSAIRAGLA DLEMAEETVDLINRNIEDNQ AHLQGEPIEVDNLPEDMGRL HLDGGKSPNPGEMAKVGEGK YREDFQMDEGEDPSLLFQSY LENVGVQIVRQIRSGERFLK IWSQTVEEIISYVAVNFPNP PGKSSEDKSTQTTGREGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	258
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	RavP	1

Entities:

Entity 1, RavP 158 residues - Formula weight is not available

GAHM sequence at the N-terminus is non-native, leftover from cleavage. C-terminus has a non-endogenous GS sequence.

1

GLY

ALA

HIS

MET

SER

LYS

ILE

PHE

VAL

2

ASN

PRO

SER

ALA

ILE

ARG

ALA

GLY

LEU

ALA

3

ASP

LEU

GLU

MET

ALA

GLU

THR

VAL

ASP

4

LEU

ILE

ASN

ARG

ASN

ILE

GLU

ASP

ASN

GLN

5

ALA

HIS

LEU

GLN

GLY

GLU

PRO

ILE

GLU

VAL

6

ASP

ASN

LEU

PRO

GLU

ASP

MET

GLY

ARG

LEU

7

HIS

LEU

ASP

GLY

LYS

SER

PRO

ASN

PRO

8

GLY

GLU

MET

ALA

LYS

VAL

GLY

GLU

GLY

LYS

9

TYR

ARG

GLU

ASP

PHE

GLN

MET

ASP

GLU

GLY

10

GLU

ASP

PRO

SER

LEU

PHE

GLN

SER

TYR

11

LEU

GLU

ASN

VAL

GLY

VAL

GLN

ILE

VAL

ARG

12

GLN

ILE

ARG

SER

GLY

GLU

ARG

PHE

LEU

LYS

13

ILE

TRP

SER

GLN

THR

VAL

GLU

ILE

14

SER

TYR

VAL

ALA

VAL

ASN

PHE

PRO

ASN

PRO

15

PRO

GLY

LYS

SER

GLU

ASP

LYS

SER

THR

16

GLN

THR

GLY

ARG

GLU

GLY

SER

Samples:

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

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

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