Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53627

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Name: 1H, 15N, and 13C chemical shift assignments for the N-terminal region (residues 1-168) of the human DEAD-box RNA helicase DDX3X
Published: 2026-06-06

Title:

1H, 15N, and 13C chemical shift assignments for the N-terminal region (residues 1-168) of the human DEAD-box RNA helicase DDX3X

Deposition date:

2026-03-15

Original release date:

2026-06-06

Authors:

Toyama, Yuki; Takeuchi, Koh; Shimada, Ichio

Citation:

Citation: Toyama, Yuki; Inakami, Shinichiro; Takarada, Masaharu; Okabe, Kohki; Takeuchi, Koh; Shimada, Ichio. "Phase Separation Driven by Dynamic Interactions in the N-Terminal Intrinsically Disordered Region of the DEAD-Box RNA Helicase DDX3X" J. Am. Chem. Soc. 148, 21313-21331 (2026).
PubMed: 42159288

Assembly members:

Assembly members:
entity_1, polymer, 168 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 LNSSDNQSGGSTASKGRYIP PHLRNREATKGFYDKDSSGW SSSKDKDAYSSFGSRSDSRG KSSFFSDRGSGSRGRFDDRG RSDYDGIGSRGDRSGFGKFE RGGNSRWCDKSDEDDWSKPL PPSERLEQELFSGGNTGINF EKYDDIPV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	472
15N chemical shifts	159
1H chemical shifts	159

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 168 residues - Formula weight is not available

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

ARG

TYR

ILE

PRO

5

PRO

HIS

LEU

ARG

ASN

ARG

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

ARG

SER

ASP

SER

ARG

GLY

9

LYS

SER

PHE

SER

ASP

ARG

GLY

SER

10

GLY

SER

ARG

GLY

ARG

PHE

ASP

ARG

GLY

11

ARG

SER

ASP

TYR

ASP

GLY

ILE

GLY

SER

ARG

12

GLY

ASP

ARG

SER

GLY

PHE

GLY

LYS

PHE

GLU

13

ARG

GLY

ASN

SER

ARG

TRP

CYS

ASP

LYS

14

SER

ASP

GLU

ASP

TRP

SER

LYS

PRO

LEU

15

PRO

SER

GLU

ARG

LEU

GLU

GLN

GLU

LEU

16

PHE

SER

GLY

ASN

THR

GLY

ILE

ASN

PHE

17

GLU

LYS

TYR

ASP

ILE

PRO

VAL

Samples:

sample_1: N-IDR, [U-13C; U-15N], 270 uM; potassium phosphate 20 mM; potassium chloride 200 mM; DTT 5 mM; EDTA 1 mM

sample_conditions_1: pH: 6.0; 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 HNCACO	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY v1.470 - chemical shift assignment

NMRPipe v11.1 - processing

TOPSPIN v3.5pl7 - collection

NMR spectrometers:

Bruker AVANCE III HD 800 MHz

BMRB Entry 53627