BMRB Entry 18803

Name: SR-linker peptide
Published: 2013-01-29

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18803

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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:

SR-linker peptide

Deposition date:

2012-10-22

Original release date:

2013-01-29

Authors:

Keane, Sarah; Giedroc, David

Citation:

Citation: Keane, Sarah; Giedroc, David. "Solution Structure of Mouse Hepatitis Virus (MHV) nsp3a and Determinants of the Interaction with MHV Nucleocapsid (N) Protein." J. Virol. 87, 3502-3515 (2013).
PubMed: 23302895

Assembly members:

Assembly members:
SR-linker_peptide, polymer, 34 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Murine Hepatitis Virus Taxonomy ID: 11142 Superkingdom: Viruses Kingdom: not available Genus/species: Betacoronavirus Murine coronavirus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SR-linker_peptide: CAPASRSGSRSQSRGPNNRA RSSSNQRQPASTYK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	60
15N chemical shifts	27
1H chemical shifts	27

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MHV n-linker peptide	1

Entities:

Entity 1, MHV n-linker peptide 34 residues - Formula weight is not available

1

CYS

ALA

PRO

ALA

SER

ARG

SER

GLY

SER

ARG

2

SER

GLN

SER

ARG

GLY

PRO

ASN

ARG

ALA

3

ARG

SER

ASN

GLN

ARG

GLN

PRO

ALA

4

SER

THR

TYR

LYS

Samples:

sample_1: SR-linker peptide, [U-100% 13C; U-100% 15N], 1.8 mM; potassium phosphate 50 mM; potassium chloride 100 mM; TCEP 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
BEST 3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
BEST 3D HNCACB	sample_1	isotropic	sample_conditions_1
BEST 3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
BEST 3D HNCA	sample_1	isotropic	sample_conditions_1
BEST 3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

SPARKY, Goddard - data analysis, peak picking

NMR spectrometers:

Varian INOVA 600 MHz

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