BMRB Entry 36361

Name: Solution structure of 28 amino acid polypeptide (354-381) in Plantago asiatica mosaic virus replicase bound to SDS micelle
Published: 2025-10-13

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PDB ID: 7ck5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36361
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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:

Solution structure of 28 amino acid polypeptide (354-381) in Plantago asiatica mosaic virus replicase bound to SDS micelle

Deposition date:

2020-07-15

Original release date:

2025-10-13

Authors:

Komatsu, K.; Sasaki, N.; Yoshida, T.; Suzuki, K.; Masujima, Y.; Hashimoto, M.; Watanabe, S.; Tochio, N.; Kigawa, T.; Yamaji, Y.; Oshima, K.; Namba, S.; Nelson, R.; Arie, T.

Citation:

Citation: Komatsu, Ken; Sasaki, Nobumitsu; Yoshida, Tetsuya; Suzuki, Katsuhiro; Masujima, Yuki; Hashimoto, Masayoshi; Watanabe, Satoru; Tochio, Naoya; Kigawa, Takanori; Yamaji, Yasuyuki; Oshima, Kenro; Namba, Shigetou; Nelson, Richard; Arie, Tsutomu. "Identification of a Proline-Kinked Amphipathic a-Helix Downstream from the Methyltransferase Domain of a Potexvirus Replicase and Its Role in Virus Replication and Perinuclear Complex Formation." J. Virol. 95, e0190620-e0190620 (2021).
PubMed: 34346768

Assembly members:

Assembly members:
PlAMV replicase peptide from RNA-dependent RNA polymerase, polymer, 28 residues, 3296.862 Da.

Natural source:

Natural source: Common Name: P1AMV Taxonomy ID: 28354 Superkingdom: not available Kingdom: Orthornavirae Genus/species: Potexvirus marmorplantagonis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PlAMV replicase peptide from RNA-dependent RNA polymerase: FEDILSGNLLQRMLRPLRSG LTQLLDFF

Data sets:

assigned_chemical_shifts
- MET_peptide.str

Data type	Count
13C chemical shifts	134
15N chemical shifts	32
1H chemical shifts	219

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 28 residues - 3296.862 Da.

1

PHE

GLU

ASP

ILE

LEU

SER

GLY

ASN

LEU

2

GLN

ARG

MET

LEU

ARG

PRO

LEU

ARG

SER

GLY

3

LEU

THR

GLN

LEU

ASP

PHE

Samples:

sample_1: PlAMV replicase peptide, [U-13C; U-15N], 1 mM; sodium acetate 20 mM; D2O, [U-2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 120 mM; pH: 5.6; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

MagRO-NMRView, Kobayashi N. - chemical shift assignment

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

Bruker ava 600 MHz

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