BMRB Entry 51404

Name: Backbone chemical shifts of PR8 NS1 W187A effector domain
Published: 2023-02-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51404

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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 PR8 NS1 W187A 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, 127 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: TMASVPASRYLTDMTLEEMS RDWSMLIPKQKVAGPLCIRM DQAIMDKNIILKANFSVIFD RLETLILLRAFTEEGAIVGE ISPLPSLPGHTAEDVKNAVG VLIGGLEANDNTVRVSETLQ RFAWRSS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	373
15N chemical shifts	119
1H chemical shifts	473

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 127 residues - Formula weight is not available

1

THR

MET

ALA

SER

VAL

PRO

ALA

SER

ARG

TYR

2

LEU

THR

ASP

MET

THR

LEU

GLU

MET

SER

3

ARG

ASP

TRP

SER

MET

LEU

ILE

PRO

LYS

GLN

4

LYS

VAL

ALA

GLY

PRO

LEU

CYS

ILE

ARG

MET

5

ASP

GLN

ALA

ILE

MET

ASP

LYS

ASN

ILE

6

LEU

LYS

ALA

ASN

PHE

SER

VAL

ILE

PHE

ASP

7

ARG

LEU

GLU

THR

LEU

ILE

LEU

ARG

ALA

8

PHE

THR

GLU

GLY

ALA

ILE

VAL

GLY

GLU

9

ILE

SER

PRO

LEU

PRO

SER

LEU

PRO

GLY

HIS

10

THR

ALA

GLU

ASP

VAL

LYS

ASN

ALA

VAL

GLY

11

VAL

LEU

ILE

GLY

LEU

GLU

ALA

ASN

ASP

12

ASN

THR

VAL

ARG

VAL

SER

GLU

THR

LEU

GLN

13

ARG

PHE

ALA

TRP

ARG

SER

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 HNCACO	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