BMRB Entry 27177

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_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27177

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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(13-50), polymer, 124 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(13-50): MGHVQLSLPVLQVRDVLVRG FGDSVEEALSEAREHLKNGT HGRAPIKVESQEHKLVPRGS FQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTESGHH HHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	330
15N chemical shifts	112
1H chemical shifts	318

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(13-50)	1

Entities:

Entity 1, Coronavirus nsp1 truncated proteins; nsp1(13-50) 124 residues - Formula weight is not available

1

MET

GLY

HIS

VAL

GLN

LEU

SER

LEU

PRO

VAL

2

LEU

GLN

VAL

ARG

ASP

VAL

LEU

VAL

ARG

GLY

3

PHE

GLY

ASP

SER

VAL

GLU

ALA

LEU

SER

4

GLU

ALA

ARG

GLU

HIS

LEU

LYS

ASN

GLY

THR

5

HIS

GLY

ARG

ALA

PRO

ILE

LYS

VAL

GLU

SER

6

GLN

GLU

HIS

LYS

LEU

VAL

PRO

ARG

GLY

SER

7

PHE

GLN

TYR

LYS

LEU

ILE

LEU

ASN

GLY

LYS

8

THR

LEU

LYS

GLY

GLU

THR

GLU

ALA

9

VAL

ASP

ALA

THR

ALA

GLU

LYS

VAL

PHE

10

LYS

GLN

TYR

ALA

ASN

ASP

ASN

GLY

VAL

ASP

11

GLY

GLU

TRP

THR

TYR

ASP

ALA

THR

LYS

12

THR

PHE

THR

VAL

THR

GLU

SER

GLY

HIS

13

HIS

Samples:

All_samples: potassium phosphate 2 mM; sodium chloride 250 mM; DTT 1 mM; sodium azide 3 mM; nsp1(13-50), [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