BMRB Entry 20027

Name: Brome Mosaic Virus protein 1a Helix A bound to SDS micelle
Published: 2009-04-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR20027

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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:

Brome Mosaic Virus protein 1a Helix A bound to SDS micelle

Deposition date:

2008-06-27

Original release date:

2009-04-03

Authors:

Liu, Ling; Westler, William; Wang, Xiaofeng; Diaz, Arturo; Ahlquist, Paul

Citation:

Citation: Liu, Ling; Westler, William; den Boon, Johan; Wang, Xiaofeng; Diaz, Arturo; Steinberg, H.; Ahlquist, Paul. "An amphipathic alpha-helix controls multiple roles of brome mosaic virus protein 1a in RNA replication complex assembly and function" PLoS Pathog. 5, e1000351-e1000351 (2009).
PubMed: 19325881

Assembly members:

Assembly members:
1a, polymer, 18 residues, 2088.469 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 12302 Superkingdom: Virus Kingdom: not available Genus/species: Brome mosaic

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
1a: VAFALTLNLYQKYEKLTA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
conformer_family_coord_set
- ensemble_coordinates

Data type	Count
13C chemical shifts	57
15N chemical shifts	17
1H chemical shifts	112

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	1a	1

Entities:

Entity 1, 1a 18 residues - 2088.469 Da.

1

VAL

ALA

PHE

ALA

LEU

THR

LEU

ASN

LEU

TYR

2

GLN

LYS

TYR

GLU

LYS

LEU

THR

ALA

Samples:

sample_1: peptide, [U-100% 13C; U-100% 15N], 0.8 mM; SDS-d25 100 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 7; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	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
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

PISTACHIO, Eghbalnia, Bahrami, Wang, Assadi and Markley - chemical shift assignment

PECAN, Eghbalnia - Secondary structure

SPARKY, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

VNMRJ, Varian - collection

ATHNOS-CANDID, Herrmann - chemical shift assignment, peak picking, structure solution

PSVS, Bhattacharya and Montelione - refinement, validation

TALOS, Cornilescu, Delaglio and Bax - data analysis

HIFI, Eghbalnia et al - collection

NMR spectrometers:

Varian DirectDrive 600 MHz

DBJ	BAJ41520
EMBL	CAA26228 CAA41361
GB	ABF83485 ADW09019 AJY78069 AKA44627
REF	NP_041196
SP	P03588
AlphaFold	P03588