BMRB Entry 51237

Name: Resonance assignments of a phsophomimetic of the C-terminal domain of the P protein of the Nishigahara strain of rabies virus
Published: 2022-03-29

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51237

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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 of a phsophomimetic of the C-terminal domain of the P protein of the Nishigahara strain of rabies virus

Deposition date:

2021-12-19

Original release date:

2022-03-29

Authors:

Zhan, Jingyu; Gooley, Paul

Citation:

Citation: Zhan, Jingyu; Watts, Ericka; Brice, Aaron; Metcalfe, Riley; Sethi, Ashish; Yan, Fei; Rozario, Ashley; Bell, Toby; Griffin, Michael; Moseley, Gregory; Gooley, Paul. "Molecular basis of functional effects of protein kinase C phosphorylation of rabies virus P protein" J. Virol. 96, e0011122-e0011122 (2022).
PubMed: 35404083

Assembly members:

Assembly members:
entity_1, polymer, 115 residues, 13042.86 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMWSATNEEDDLSVEAEIA HQIAESFEKKYKFPSRSSGI FLYNFEQLKMNLDDIVKEAK NVPGVTRLAHDGSKLPLRCV LGWVALANSKKFQLLVEANK LNKIMQDDLNRYASS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	417
15N chemical shifts	122
1H chemical shifts	134

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C-terminal domain	1

Entities:

Entity 1, C-terminal domain 115 residues - 13042.86 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

GLU

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

LEU

PRO

LEU

ARG

CYS

VAL

9

LEU

GLY

TRP

VAL

ALA

LEU

ALA

ASN

SER

LYS

10

LYS

PHE

GLN

LEU

VAL

GLU

ALA

ASN

LYS

11

LEU

ASN

LYS

ILE

MET

GLN

ASP

LEU

ASN

12

ARG

TYR

ALA

SER

Samples:

sample_1: Phosphomimetic of P protein C-terminal domain, [U-98% 15N], 0.45 mM; phosphate buffer 50 mM; sodium chloride 100 mM

sample_2: Phosphomimetic of P protein C-terminal domain, [U-98% 13C; U-98% 15N], 0.4-0.5 mM; phosphate buffer 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.2 M; pH: 6.8; 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_2	isotropic	sample_conditions_2
3D HN(CO)CA	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D HN(CO)CACB	sample_2	isotropic	sample_conditions_2
3D C(CO)NH	sample_2	isotropic	sample_conditions_2

Software:

TOPSPIN v3 - collection

NMRPipe v10.9 - processing

SMILE - processing

NMRFAM-SPARKY v1.470 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 700 MHz

UniProt	Q9IPJ8
AlphaFold	Q75T11