BMRB Entry 36004

Name: RRM-like domain of DEAD-box protein, CsdA
Published: 2025-10-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36004

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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:

RRM-like domain of DEAD-box protein, CsdA

Deposition date:

2016-07-05

Original release date:

2025-10-10

Authors:

Xu, L.; Peng, J.; Zhang, J.; Wu, J.; Tang, Y.; Shi, Y.

Citation:

Citation: Xu, Ling; Wang, Lijun; Peng, Junhui; Li, Fudong; Wu, Lijie; Zhang, Beibei; Lv, Mengqi; Zhang, Jiahai; Gong, Qingguo; Zhang, Rongguang; Zuo, Xiaobing; Zhang, Zhiyong; Wu, Jihui; Tang, Yajun; Shi, Yunyu. "Insights into the Structure of Dimeric RNA Helicase CsdA and Indispensable Role of Its C-Terminal Regions." Structure 25, 1795-1808 (2017).
PubMed: 29107486

Assembly members:

Assembly members:
ATP-dependent RNA helicase DeaD, polymer, 85 residues, 9448.825 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 83333 Superkingdom: Bacteria Kingdom: Pseudomonadati Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ATP-dependent RNA helicase DeaD: MADVGDMQLYRIEVGRDDGV EVRHIVGAIANEGDISSRYI GNIKLFASHSTIELPKGMPG EVLQHFTRTRILNKPMNMQL LGDAQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	244
15N chemical shifts	80
1H chemical shifts	390

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 85 residues - 9448.825 Da.

1

MET

ALA

ASP

VAL

GLY

ASP

MET

GLN

LEU

TYR

2

ARG

ILE

GLU

VAL

GLY

ARG

ASP

GLY

VAL

3

GLU

VAL

ARG

HIS

ILE

VAL

GLY

ALA

ILE

ALA

4

ASN

GLU

GLY

ASP

ILE

SER

ARG

TYR

ILE

5

GLY

ASN

ILE

LYS

LEU

PHE

ALA

SER

HIS

SER

6

THR

ILE

GLU

LEU

PRO

LYS

GLY

MET

PRO

GLY

7

GLU

VAL

LEU

GLN

HIS

PHE

THR

ARG

THR

ARG

8

ILE

LEU

ASN

LYS

PRO

MET

ASN

MET

GLN

LEU

9

LEU

GLY

ASP

ALA

GLN

Samples:

sample_1: RRM-like domain, [U-99% 13C; U-99% 15N], 1.0 mM; NaCl 150 mM; Na2HPO4 50 mM; D2O, [U-2H], 100%

sample_2: RRM-like domain, [U-99% 13C; U-99% 15N], 1 mM; NaCl 150 mM; Na2HPO4 50 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - peak picking

NMR spectrometers:

Bruker DMX 600 MHz

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