BMRB Entry 52739

Name: 1H, 15N, and 13C chemical shift assignments for the N-terminal region (residues 1-132) of the human DEAD-box RNA helicase DDX3X RtoK variant
Published: 2025-08-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52739

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

1H, 15N, and 13C chemical shift assignments for the N-terminal region (residues 1-132) of the human DEAD-box RNA helicase DDX3X RtoK variant

Deposition date:

2024-12-04

Original release date:

2025-08-30

Authors:

Toyama, Yuki; Takeuchi, Koh; Shimada, Ichio

Citation:

Citation: Toyama, Yuki; Takeuchi, Koh; Shimada, Ichio. "Regulatory role of the N-terminal intrinsically disordered region of the DEAD-box RNA helicase DDX3X in selective RNA recognition" Nat. Commun. 16, 7762-7762 (2025).
PubMed: 40877262

Assembly members:

Assembly members:
entity_1, polymer, 132 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSHVAVENALGLDQQFAGLD LNSSDNQSGGSTASKGKYIP PHLKNKEATKGFYDKDSSGW SSSKDKDAYSSFGSKSDSKG KSSFFSDKGSGSKGKFDDKG KSDYDGIGSKGDKSGFGKFE KGGNSKWCDKSD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	370
15N chemical shifts	128
1H chemical shifts	128

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-IDR	1

Entities:

Entity 1, N-IDR 132 residues - Formula weight is not available

R37K, R44K, R46K, R75K, R79K, R88K, R93K, R95K, R99K, R101K, R110K, R113K, R121K, and R126K variant

1

MET

SER

HIS

VAL

ALA

VAL

GLU

ASN

ALA

LEU

2

GLY

LEU

ASP

GLN

PHE

ALA

GLY

LEU

ASP

3

LEU

ASN

SER

ASP

ASN

GLN

SER

GLY

4

SER

THR

ALA

SER

LYS

GLY

LYS

TYR

ILE

PRO

5

PRO

HIS

LEU

LYS

ASN

LYS

GLU

ALA

THR

LYS

6

GLY

PHE

TYR

ASP

LYS

ASP

SER

GLY

TRP

7

SER

LYS

ASP

LYS

ASP

ALA

TYR

SER

8

SER

PHE

GLY

SER

LYS

SER

ASP

SER

LYS

GLY

9

LYS

SER

PHE

SER

ASP

LYS

GLY

SER

10

GLY

SER

LYS

GLY

LYS

PHE

ASP

LYS

GLY

11

LYS

SER

ASP

TYR

ASP

GLY

ILE

GLY

SER

LYS

12

GLY

ASP

LYS

SER

GLY

PHE

GLY

LYS

PHE

GLU

13

LYS

GLY

ASN

SER

LYS

TRP

CYS

ASP

LYS

14

SER

ASP

Samples:

sample_1: N-IDR, [U-13C; U-15N], 90 uM; potassium phosphate 20 mM; potassium chloride 250 mM; DTT 5 mM

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 283.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNN	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY v1.470 - chemical shift assignment

NMRPipe v11.1 - processing

TOPSPIN v4.2.0 - collection

NMR spectrometers:

Bruker AVANCE NEO 600 MHz