BMRB Entry 53239

Name: DNAJA1 J-domain
Published: 2025-11-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53239

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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:

DNAJA1 J-domain

Deposition date:

2025-06-24

Original release date:

2025-11-06

Authors:

Leder, Anna; Mas, Guillaume; Hiller, Sebastian

Citation:

Citation: Leder, Anna; Mas, Guillaume; Hiller, Sebastian. "A universal tyrosine-based regulatory switch controls J-domain protein activity" Nat. Commun. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 76 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: pCA528

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MVKETTYYDVLGVKPNATQE ELKKAYRKLALKYHPDKNPN EGEKFKQISQAYEVLSDAKK RELYDKGGEQAIKEGC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	68
1H chemical shifts	68

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DNAJA1 JD, WT	1

Entities:

Entity 1, DNAJA1 JD, WT 76 residues - Formula weight is not available

1

MET

VAL

LYS

GLU

THR

TYR

ASP

VAL

2

LEU

GLY

VAL

LYS

PRO

ASN

ALA

THR

GLN

GLU

3

GLU

LEU

LYS

ALA

TYR

ARG

LYS

LEU

ALA

4

LEU

LYS

TYR

HIS

PRO

ASP

LYS

ASN

PRO

ASN

5

GLU

GLY

GLU

LYS

PHE

LYS

GLN

ILE

SER

GLN

6

ALA

TYR

GLU

VAL

LEU

SER

ASP

ALA

LYS

7

ARG

GLU

LEU

TYR

ASP

LYS

GLY

GLU

GLN

8

ALA

ILE

LYS

GLU

GLY

CYS

Samples:

sample_1: DNAJA1 JD, [U-98% 15N], 0.75 mM; MES 25 mM; potassium chloride 150 mM; magnesium chloride 10 mM; DTT 5 mM; DSS 0.5 mM; D2O 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_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.5.2 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 700 MHz

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