BMRB Entry 51403

Name: Backbone chemical shifts of VN NS1 W182A effector domain
Published: 2023-02-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51403

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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:

Backbone chemical shifts of VN NS1 W182A effector domain

Deposition date:

2022-04-19

Original release date:

2023-02-20

Authors:

Kim, Iktae; Cho, Jae-Hyun

Citation:

Citation: Kim, Iktae; Dubrow, Alyssa; Zuniga, Bryan; Zhao, Baoyu; Sherer, Noah; Bastiray, Abhishek; Li, Pingwei; Cho, Jae-Hyun. "Energy landscape reshaped by strain-specific mutations underlies epistasis in NS1 evolution of influenza A virus" Nat. Commun. 13, 5775-5775 (2022).
PubMed: 36182933

Assembly members:

Assembly members:
entity_1, polymer, 128 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Influenza A Taxonomy ID: 11320 Superkingdom: Viruses Kingdom: not available Genus/species: Alphainfluenzavirus Influenza A

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MPASRYLTDMTLEEMSRDWF MLMPKQKVAGSLCIKMDQAI MDKTIILKANFSVIFDRLET LILLRAFTEEGAIVGEISPL PSLPGHTGEDVKNAIGVLIG GLEANDNTVRVTETIQRFAW RNSDEDGR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	360
15N chemical shifts	121
1H chemical shifts	470

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 128 residues - Formula weight is not available

1

MET

PRO

ALA

SER

ARG

TYR

LEU

THR

ASP

MET

2

THR

LEU

GLU

MET

SER

ARG

ASP

TRP

PHE

3

MET

LEU

MET

PRO

LYS

GLN

LYS

VAL

ALA

GLY

4

SER

LEU

CYS

ILE

LYS

MET

ASP

GLN

ALA

ILE

5

MET

ASP

LYS

THR

ILE

LEU

LYS

ALA

ASN

6

PHE

SER

VAL

ILE

PHE

ASP

ARG

LEU

GLU

THR

7

LEU

ILE

LEU

ARG

ALA

PHE

THR

GLU

8

GLY

ALA

ILE

VAL

GLY

GLU

ILE

SER

PRO

LEU

9

PRO

SER

LEU

PRO

GLY

HIS

THR

GLY

GLU

ASP

10

VAL

LYS

ASN

ALA

ILE

GLY

VAL

LEU

ILE

GLY

11

GLY

LEU

GLU

ALA

ASN

ASP

ASN

THR

VAL

ARG

12

VAL

THR

GLU

THR

ILE

GLN

ARG

PHE

ALA

TRP

13

ARG

ASN

SER

ASP

GLU

ASP

GLY

ARG

Samples:

sample_1: NS1 effector domain, [U-99% 13C; U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 80 mM; EDTA 1 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 80 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRFAM-SPARKY - chemical shift assignment, peak picking

NMRPipe - processing

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 800 MHz

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