BMRB Entry 18954

Name: NMR structure of the GUCT domain from human DEAD box polypeptide 21
Published: 2013-01-28

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PDB ID: 2m3d
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18954
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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:

NMR structure of the GUCT domain from human DEAD box polypeptide 21

Deposition date:

2013-01-16

Original release date:

2013-01-28

Authors:

Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation:

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the GUCT domain from human DEAD box polypeptide 21 (DDX21)" .

Assembly members:

Assembly members:
entity, polymer, 95 residues, 10640.232 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GHISGATSVDQRSLINSNVG FVTMILQCSIEMPNISYAWK ELKEQLGEEIDSKVKGMVFL KGKLGVCFDVPTASVTEIQE KWHDSRRWQLSVATE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	307
15N chemical shifts	101
1H chemical shifts	658

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GUCT	1

Entities:

Entity 1, GUCT 95 residues - 10640.232 Da.

1

GLY

HIS

ILE

SER

GLY

ALA

THR

SER

VAL

ASP

2

GLN

ARG

SER

LEU

ILE

ASN

SER

ASN

VAL

GLY

3

PHE

VAL

THR

MET

ILE

LEU

GLN

CYS

SER

ILE

4

GLU

MET

PRO

ASN

ILE

SER

TYR

ALA

TRP

LYS

5

GLU

LEU

LYS

GLU

GLN

LEU

GLY

GLU

ILE

6

ASP

SER

LYS

VAL

LYS

GLY

MET

VAL

PHE

LEU

7

LYS

GLY

LYS

LEU

GLY

VAL

CYS

PHE

ASP

VAL

8

PRO

THR

ALA

SER

VAL

THR

GLU

ILE

GLN

GLU

9

LYS

TRP

HIS

ASP

SER

ARG

TRP

GLN

LEU

10

SER

VAL

ALA

THR

GLU

Samples:

sample_1: GUCT, [U-99% 13C; U-99% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; D2O, [U-99% 2H], 95%; H2O 5%

sample_conditions_1: ionic strength: 0.798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
4D APSY HACANH	sample_1	isotropic	sample_conditions_1
5D APSY HACACONH	sample_1	isotropic	sample_conditions_1
5D APSY CBCACONH	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.0, G ntert P. - structure solution

TOPSPIN v3.1, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

j-UNIO, Herrmann, and Wuthrich - chemical shift assignment, peak picking, structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2M3D
DBJ	BAB93481 BAG37957 BAI45572
EMBL	CAH18395
GB	AAB02546 AAF78930 AAH08071 ABM84557 ABM87851
REF	NP_001243839 NP_004719 XP_001110939 XP_002820927 XP_003258243
SP	Q9NR30
AlphaFold	Q9NR30