BMRB Entry 53374

Name: Backbone resonance assignment of the C-terminal domain of the P protein of the CVS-11 strain of rabies virus
Published: 2025-10-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53374

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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 resonance assignment of the C-terminal domain of the P protein of the CVS-11 strain of rabies virus

Deposition date:

2025-09-24

Original release date:

2025-10-02

Authors:

Gooley, Paul

Citation:

Citation: Gooley, Paul. "Conformational dynamics, RNA binding, and phase separation regulate the multifunctionality of rabies virus P protein" Nat. Commun. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 115 residues, 12867.66 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMWSATNEEDDLSVEAEIA HQIAESFSKKYKFPSRSSGI FLYNFEQLKMNLDDIVKEAK NVPGVTRLAHDGSKIPLRCV LGWVALANSKKFQLLVEADK LSKIMQDDLNRYTSS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	218
15N chemical shifts	109
1H chemical shifts	109

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CTD	1

Entities:

Entity 1, CTD 115 residues - 12867.66 Da.

The first 3 residues GHM represent a non-native part introduced from cloning

1

GLY

HIS

MET

TRP

SER

ALA

THR

ASN

GLU

2

ASP

LEU

SER

VAL

GLU

ALA

GLU

ILE

ALA

3

HIS

GLN

ILE

ALA

GLU

SER

PHE

SER

LYS

4

TYR

LYS

PHE

PRO

SER

ARG

SER

GLY

ILE

5

PHE

LEU

TYR

ASN

PHE

GLU

GLN

LEU

LYS

MET

6

ASN

LEU

ASP

ILE

VAL

LYS

GLU

ALA

LYS

7

ASN

VAL

PRO

GLY

VAL

THR

ARG

LEU

ALA

HIS

8

ASP

GLY

SER

LYS

ILE

PRO

LEU

ARG

CYS

VAL

9

LEU

GLY

TRP

VAL

ALA

LEU

ALA

ASN

SER

LYS

10

LYS

PHE

GLN

LEU

VAL

GLU

ALA

ASP

LYS

11

LEU

SER

LYS

ILE

MET

GLN

ASP

LEU

ASN

12

ARG

TYR

THR

SER

Samples:

sample_1: CVS_RABV_P-protein_CTD, [U-98% 13C; U-98% 15N], 500 uM; Na2 PO4 50 mM; TCEP 1 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2.7 - collection

NMRPipe v10.9 - processing

NMRFAM-SPARKY v1.47 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 700 MHz