BMRB Entry 52640

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

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52640

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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:

2024-10-11

Original release date:

2025-10-20

Authors:

Jiang, Yajun; Ibrahin, Ziad; Xia, Youlin; Kalodimos, Babis

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 ., .-. (2025).
PubMed: 41092901

Assembly members:

Assembly members:
entity_1, polymer, 136 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: GPMDPGLFGGFGSGGSGGSG GSGVTPLSLGVETKGGVMTV LIPRNTTIPTRKCEIFTTAE HNQTAVEIHVLQGERPMAQD NKSLGRFRLEGIPPMPAGVP QIEVCFDIDANGILHVTAKE RSTGREASITIQNTTT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
homonucl_NOEs
- homonucl_NOEs_1
- homonucl_NOEs_2
spectral_peak_list

Data type	Count
13C chemical shifts	482
15N chemical shifts	118
1H chemical shifts	807

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DnaJ2	1

Entities:

Entity 1, DnaJ2 136 residues - Formula weight is not available

1

GLY

PRO

MET

ASP

PRO

GLY

LEU

PHE

GLY

2

PHE

GLY

SER

GLY

SER

GLY

SER

GLY

3

GLY

SER

GLY

VAL

THR

PRO

LEU

SER

LEU

GLY

4

VAL

GLU

THR

LYS

GLY

VAL

MET

THR

VAL

5

LEU

ILE

PRO

ARG

ASN

THR

ILE

PRO

THR

6

ARG

LYS

CYS

GLU

ILE

PHE

THR

ALA

GLU

7

HIS

ASN

GLN

THR

ALA

VAL

GLU

ILE

HIS

VAL

8

LEU

GLN

GLY

GLU

ARG

PRO

MET

ALA

GLN

ASP

9

ASN

LYS

SER

LEU

GLY

ARG

PHE

ARG

LEU

GLU

10

GLY

ILE

PRO

MET

PRO

ALA

GLY

VAL

PRO

11

GLN

ILE

GLU

VAL

CYS

PHE

ASP

ILE

ASP

ALA

12

ASN

GLY

ILE

LEU

HIS

VAL

THR

ALA

LYS

GLU

13

ARG

SER

THR

GLY

ARG

GLU

ALA

SER

ILE

THR

14

ILE

GLN

ASN

THR

Samples:

sample_1: DnaJ2 and DnaK fusion, [U-100% 13C; U-100% 15N], 500 uM; D2O, [U-100% 2H], 10%; sodium chloride 100 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.8; pressure: 1 atm; temperature: 303 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 CBCACONH	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 (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-separated NOESY	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.1.4 - 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