BMRB Entry 27176

Name: 1H, 13C, and 15N Chemical Shift Assignments for truncated forms of the coronavirus nsp1 protein and its solubility domain GB1
Published: 2017-08-10

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27176

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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:

1H, 13C, and 15N Chemical Shift Assignments for truncated forms of the coronavirus nsp1 protein and its solubility domain GB1

Deposition date:

2017-07-13

Original release date:

2017-08-10

Authors:

Vazquez, Leonardo; Almeida, Marcius

Citation:

Citation: Vazquez, Leonardo; Lima, Luis; Almeida, Marcius. "Comprehensive structural analysis of designed incomplete polypeptide chains of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus" PLoS ONE 12, e0182132-e0182132 (2017).
PubMed: 28750053

Assembly members:

Assembly members:
nsp1(13-25), polymer, 99 residues, Formula weight is not available

Natural source:

Natural source: Common Name: SARS coronavirus Taxonomy ID: 227859 Superkingdom: Viruses Kingdom: not available Genus/species: SARS coronavirus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-25(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
nsp1(13-25): MGHVQLSLPVLQVRDHGRAP IKVESQEHKLVPRGSFQYKL ILNGKTLKGETTTEAVDAAT AEKVFKQYANDNGVDGEWTY DDATKTFTVTESGHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	247
15N chemical shifts	86
1H chemical shifts	201

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Coronavirus nsp1 truncated proteins; nsp1(13-25)	1

Entities:

Entity 1, Coronavirus nsp1 truncated proteins; nsp1(13-25) 99 residues - Formula weight is not available

1

MET

GLY

HIS

VAL

GLN

LEU

SER

LEU

PRO

VAL

2

LEU

GLN

VAL

ARG

ASP

HIS

GLY

ARG

ALA

PRO

3

ILE

LYS

VAL

GLU

SER

GLN

GLU

HIS

LYS

LEU

4

VAL

PRO

ARG

GLY

SER

PHE

GLN

TYR

LYS

LEU

5

ILE

LEU

ASN

GLY

LYS

THR

LEU

LYS

GLY

GLU

6

THR

GLU

ALA

VAL

ASP

ALA

THR

7

ALA

GLU

LYS

VAL

PHE

LYS

GLN

TYR

ALA

ASN

8

ASP

ASN

GLY

VAL

ASP

GLY

GLU

TRP

THR

TYR

9

ASP

ALA

THR

LYS

THR

PHE

THR

VAL

THR

10

GLU

SER

GLY

HIS

Samples:

All_samples: potassium phosphate 2 mM; sodium chloride 250 mM; DTT 1 mM; sodium azide 3 mM; nsp1(13-25), [U-13C; U-15N], 2 mM

Condition_of_all_samples: ionic strength: 250 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	All_samples	isotropic	Condition_of_all_samples
2D 1H-13C HSQC aliphatic	All_samples	isotropic	Condition_of_all_samples
2D 1H-13C HSQC aromatic	All_samples	isotropic	Condition_of_all_samples
3D CBCA(CO)NH	All_samples	isotropic	Condition_of_all_samples
3D HNCACB	All_samples	isotropic	Condition_of_all_samples
3D HNCO	All_samples	isotropic	Condition_of_all_samples
3D HNCA	All_samples	isotropic	Condition_of_all_samples
3D HBHA(CO)NH	All_samples	isotropic	Condition_of_all_samples

Software:

XEASY, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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