BMRB Entry 51811

Name: 1H, 13C, 15N backbone chemical shift assignments of the extended ARID domain from human AT-rich interactive domain protein 5a (Arid5a)
Published: 2023-02-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51811

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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, 13C, 15N backbone chemical shift assignments of the extended ARID domain from human AT-rich interactive domain protein 5a (Arid5a)

Deposition date:

2023-01-30

Original release date:

2023-02-03

Authors:

von Ehr, Julian; Korn, Sophie; Schlundt, Andreas

Citation:

Citation: von Ehr, Julian; Korn, Sophie Marianne; Weiss, Lena; Schlundt, Andreas. "1H, 13C, 15N backbone chemical shift assignments of the extended ARID domain in human AT-rich interactive domain protein 5a (Arid5a)" Biomol. NMR Assign. 17, 121-127 (2023).
PubMed: 37129704

Assembly members:

Assembly members:
entity_1, polymer, 108 residues, 12680 Da.

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-Trx1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMAREEEQEREEEQAFLVS LYKFMKERHTPIERVPHLGF KQINLWKIYKAVEKLGAYEL VTGRRLWKNVYDELGGSPGS TSAATCTRRHYERLVLPYVR HLKGEDDK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	315
15N chemical shifts	107
1H chemical shifts	343

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Arid5a 49-152	1

Entities:

Entity 1, Arid5a 49-152 108 residues - 12680 Da.

The first four residues (GAMA) in the protein construct used are cloning artifacts.

1

GLY

ALA

MET

ALA

ARG

GLU

GLN

GLU

2

ARG

GLU

GLN

ALA

PHE

LEU

VAL

SER

3

LEU

TYR

LYS

PHE

MET

LYS

GLU

ARG

HIS

THR

4

PRO

ILE

GLU

ARG

VAL

PRO

HIS

LEU

GLY

PHE

5

LYS

GLN

ILE

ASN

LEU

TRP

LYS

ILE

TYR

LYS

6

ALA

VAL

GLU

LYS

LEU

GLY

ALA

TYR

GLU

LEU

7

VAL

THR

GLY

ARG

LEU

TRP

LYS

ASN

VAL

8

TYR

ASP

GLU

LEU

GLY

SER

PRO

GLY

SER

9

THR

SER

ALA

THR

CYS

THR

ARG

HIS

10

TYR

GLU

ARG

LEU

VAL

LEU

PRO

TYR

VAL

ARG

11

HIS

LEU

LYS

GLY

GLU

ASP

LYS

Samples:

sample_1: Arid5a, [U-100% 13C; U-100% 15N], 127 uM; sodium chloride 150 uM; D2O, [U-99% 2H], 5%; Bis-Tris pH 6.5 20 mM; TCEP 2 mM

sample_2: Arid5a, [U-100% 13C; U-100% 15N], 471 uM; sodium chloride 150 uM; D2O, [U-99% 2H], 5%; Bis-Tris pH 6.5 20 mM; TCEP 2 mM

sample_3: Arid5a, [U-100% 13C; U-100% 15N], 225 uM; sodium chloride 150 uM; D2O, [U-99% 2H], 5%; Bis-Tris pH 6.5 20 mM; TCEP 2 mM

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
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HBHANH	sample_3	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_3	isotropic	sample_conditions_1

Software:

TOPSPIN v3 + 4 - collection

ANALYSIS v2.5.1 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 600 MHz
Bruker AVANCE III 600 MHz
Bruker AVANCE III 700 MHz
Bruker AVANCE III 800 MHz
Bruker AVANCE III 950 MHz

UNP	Q03989-1
AlphaFold	Q03989-1