BMRB Entry 52635

Name: Assembly and functional mechanisms of the Hsp70-Hsp40 chaperone machinery
Published: 2025-10-20

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PDB ID: 9dyv
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52635
MolProbity Validation Chart

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NMR-STAR v3 text file.
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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:

Assembly and functional mechanisms of the Hsp70-Hsp40 chaperone machinery

Deposition date:

2024-10-09

Original release date:

2025-10-20

Authors:

Jiang, Yajun; Ibrahim, Ziad; Clay, Mary; Xia, Youlin

Citation:

Citation: Jiang, Yajun; Ibrahim, Ziad; Xia, Youlin; Clay, Mary; Myasnikov, Alexander; Immadisetty, Kalyan; Xia, Zhilian; Tang, Liang; Rossi, Paolo; Ganguly, Pritha; Liu, Jiangshu; Miller, Darcie; Che, Meixia; Palacios, Santiago; Kramer, Gunter; Bukau, Bernd; Kalodimos, Charalampos. "Mechanisms of assembly and function of the Hsp70-Hsp40 chaperone machinery" Mol. Cell 85, 4032-4046 (2025).
PubMed: 41092901

Assembly members:

Assembly members:
entity_1, polymer, 116 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thermus thermophilus HB8 Taxonomy ID: 300852 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAAKKDYYAILGVPRNATQE EIKRAYKRLARQYHPDVNKS PEAEEKFKEINEAYAVLSDP EKRRIYDTYGTTEAPPPPPP GGYDFSGFDVEDFSEFFQEL FGPGLFGGFGRRSRKG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
homonucl_NOEs
- homonucl_NOEs_1
- homonucl_NOEs_2

Data type	Count
13C chemical shifts	502
15N chemical shifts	121
1H chemical shifts	759

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DnaJ	1

Entities:

Entity 1, DnaJ 116 residues - Formula weight is not available

1

MET

ALA

LYS

ASP

TYR

ALA

ILE

2

LEU

GLY

VAL

PRO

ARG

ASN

ALA

THR

GLN

GLU

3

GLU

ILE

LYS

ARG

ALA

TYR

LYS

ARG

LEU

ALA

4

ARG

GLN

TYR

HIS

PRO

ASP

VAL

ASN

LYS

SER

5

PRO

GLU

ALA

GLU

LYS

PHE

LYS

GLU

ILE

6

ASN

GLU

ALA

TYR

ALA

VAL

LEU

SER

ASP

PRO

7

GLU

LYS

ARG

ILE

TYR

ASP

THR

TYR

GLY

8

THR

GLU

ALA

PRO

9

GLY

TYR

ASP

PHE

SER

GLY

PHE

ASP

VAL

10

GLU

ASP

PHE

SER

GLU

PHE

GLN

GLU

LEU

11

PHE

GLY

PRO

GLY

LEU

PHE

GLY

PHE

GLY

12

ARG

SER

ARG

LYS

GLY

Samples:

sample_1: DnaJ1-116, [U-100% 13C; U-100% 15N], 500 uM; sodium chloride 100 mM; potassium phosphate 50 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-separated NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN vv4.1.4 - collection

NMR spectrometers:

Bruker AVANCE NEO 700 MHz

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