BMRB Entry 12032

Name: Solution NMR structure of the W187R mutant of 1918 NS1 effector domain
Published: 2019-09-10

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PDB ID: 6nu0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR12032
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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 NMR structure of the W187R mutant of 1918 NS1 effector domain

Deposition date:

2019-01-31

Original release date:

2019-09-10

Authors:

Shen, Qingliang; Cho, Jae-Hyun

Citation:

Citation: Shen, Qingliang; Cho, Jae-Hyun. "The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus." Biochem. Biophys. Res. Commun. 518, 178-182 (2019).
PubMed: 31420169

Assembly members:

Assembly members:
NS1_effector_domain, polymer, 119 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NS1_effector_domain: SRYLTDMTLEEMSRDWFMLM PKQKVAGSLCIRMDQAIMDK NIILKANFSVIFDRLETLIL LRAFTEEGAIVGEISPLPSL PGHTDEDVKNAVGVLIGGLE RNDNTVRVSETLQRFAWRS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	482
15N chemical shifts	120
1H chemical shifts	750

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NS1 effector domain	1

Entities:

Entity 1, NS1 effector domain 119 residues - Formula weight is not available

1

SER

ARG

TYR

LEU

THR

ASP

MET

THR

LEU

GLU

2

GLU

MET

SER

ARG

ASP

TRP

PHE

MET

LEU

MET

3

PRO

LYS

GLN

LYS

VAL

ALA

GLY

SER

LEU

CYS

4

ILE

ARG

MET

ASP

GLN

ALA

ILE

MET

ASP

LYS

5

ASN

ILE

LEU

LYS

ALA

ASN

PHE

SER

VAL

6

ILE

PHE

ASP

ARG

LEU

GLU

THR

LEU

ILE

LEU

7

LEU

ARG

ALA

PHE

THR

GLU

GLY

ALA

ILE

8

VAL

GLY

GLU

ILE

SER

PRO

LEU

PRO

SER

LEU

9

PRO

GLY

HIS

THR

ASP

GLU

ASP

VAL

LYS

ASN

10

ALA

VAL

GLY

VAL

LEU

ILE

GLY

LEU

GLU

11

ARG

ASN

ASP

ASN

THR

VAL

ARG

VAL

SER

GLU

12

THR

LEU

GLN

ARG

PHE

ALA

TRP

ARG

SER

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	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-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

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

BMRB Entry 12032

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: