BMRB Entry 51544

Name: 1H and 15N assignments for [R238A]-NS1B-CTD bound to 16-bp dsRNA
Published: 2024-08-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51544

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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 and 15N assignments for [R238A]-NS1B-CTD bound to 16-bp dsRNA

Deposition date:

2022-08-02

Original release date:

2024-08-10

Authors:

Woltz, Ryan; Montelione, Gaetano; Gurla, Swapna; Ma, Li-Chung; John, Rachel

Citation:

Citation: Woltz, Ryan; Schweibenz, Brandon; Tsutakawa, Susan; Zhao, Chen; Ma, LiChung; Shurina, Ben; Hura, Gregory; John, Rachael; Vorobiev, Sergey; Swapna, Gvt; Solotchi, Mihai; Tainer, John; Krug, Robert; Patel, Smita; Montelione, Gaetano. "The NS1 protein of influenza B virus binds 5'-triphosphorylated dsRNA to suppress RIG-I activation and the host antiviral response" .
PubMed: 38328244

Assembly members:

Assembly members:
entity_1, polymer, 139 residues, 15.69 Da.
entity_2, polymer, 32 residues, 10.25 Da.

Natural source:

Natural source: Common Name: Influenza B virus Taxonomy ID: 11520 Superkingdom: Viruses Kingdom: not available Genus/species: Betainfluenzavirus Influenza B virus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: IEVVLRDMNNKDARQKIKDE VNTQKEGKFRLTIKRDIRNV PSLRVLVNGTFLKHPNGDKS LSTLHRLNAYDQNGGLVAKL VATDDLTVEDEKDGHRILNS LFERFDEGHSKPIRAAETAV GVLSQFGQEHRLSPEEGDN
entity_2: CCAUCCUCUACAGGCGCGCC UGUAGAGGAUGG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	129
1H chemical shifts	129

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein	1
2	RNA	2

Entities:

Entity 1, protein 139 residues - 15.69 Da.

1

ILE

GLU

VAL

LEU

ARG

ASP

MET

ASN

2

LYS

ASP

ALA

ARG

GLN

LYS

ILE

LYS

ASP

GLU

3

VAL

ASN

THR

GLN

LYS

GLU

GLY

LYS

PHE

ARG

4

LEU

THR

ILE

LYS

ARG

ASP

ILE

ARG

ASN

VAL

5

PRO

SER

LEU

ARG

VAL

LEU

VAL

ASN

GLY

THR

6

PHE

LEU

LYS

HIS

PRO

ASN

GLY

ASP

LYS

SER

7

LEU

SER

THR

LEU

HIS

ARG

LEU

ASN

ALA

TYR

8

ASP

GLN

ASN

GLY

LEU

VAL

ALA

LYS

LEU

9

VAL

ALA

THR

ASP

LEU

THR

VAL

GLU

ASP

10

GLU

LYS

ASP

GLY

HIS

ARG

ILE

LEU

ASN

SER

11

LEU

PHE

GLU

ARG

PHE

ASP

GLU

GLY

HIS

SER

12

LYS

PRO

ILE

ARG

ALA

GLU

THR

ALA

VAL

13

GLY

VAL

LEU

SER

GLN

PHE

GLY

GLN

GLU

HIS

14

ARG

LEU

SER

PRO

GLU

GLY

ASP

ASN

Entity 2, RNA 32 residues - 10.25 Da.

1

C

A

U

C

U

C

U

A

2

C

A

G

C

G

C

G

C

3

U

G

U

A

G

A

G

A

U

4

G

Samples:

sample_1: R238A-NS1B-CTD(143-281), [U-100% 13C; U-100% 15N], 100 uM; sodium chloride 225 ± 1.0 mM; sodium azide 0.02%; Arginine 25 ± 1.0 mM; Calcium Chloride 5 ± 1.0 mM; D2O, [U-99% 2H], 10%; 16bp-dsRNA 100 uM

sample_conditions_1: ionic strength: 0.235 M; pH: 5.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1b - collection

NMRPipe v2.1 - processing

SPARKY v3.0 - peak picking

AutoAssign v2.4.0 - chemical shift assignment

PINE v1.0 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker Avance 800 MHz
Bruker Avance 600 MHz