BMRB Entry 52985

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/BMR52985

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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:

2025-03-29

Original release date:

2025-10-20

Authors:

Jiang, Yajun; Ibrahim, Ziad; Clay, Mary; 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, 131 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thermus thermophilus Taxonomy ID: 274 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Assembly and functional mechanisms of the Hsp70-Hsp40 chaperone machinery Vector: pCoofy

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PMLARSGEGGSGGSGGSDVT PLSLGVETKGGVMTVLIPRN TTIPTRKCEIFTTAEHNQTA VEIHVLQGERPMAQDNKSLG RFRLEGIPPMPAGVPQIEVC FDIDANGILHVTAKERSTGR EASITIQNTTT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	375
15N chemical shifts	113
1H chemical shifts	771

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DnaA-DnaK	1

Entities:

Entity 1, DnaA-DnaK 131 residues - Formula weight is not available

1

PRO

MET

LEU

ALA

ARG

SER

GLY

GLU

GLY

2

SER

GLY

SER

GLY

SER

ASP

VAL

THR

3

PRO

LEU

SER

LEU

GLY

VAL

GLU

THR

LYS

GLY

4

GLY

VAL

MET

THR

VAL

LEU

ILE

PRO

ARG

ASN

5

THR

ILE

PRO

THR

ARG

LYS

CYS

GLU

ILE

6

PHE

THR

ALA

GLU

HIS

ASN

GLN

THR

ALA

7

VAL

GLU

ILE

HIS

VAL

LEU

GLN

GLY

GLU

ARG

8

PRO

MET

ALA

GLN

ASP

ASN

LYS

SER

LEU

GLY

9

ARG

PHE

ARG

LEU

GLU

GLY

ILE

PRO

MET

10

PRO

ALA

GLY

VAL

PRO

GLN

ILE

GLU

VAL

CYS

11

PHE

ASP

ILE

ASP

ALA

ASN

GLY

ILE

LEU

HIS

12

VAL

THR

ALA

LYS

GLU

ARG

SER

THR

GLY

ARG

13

GLU

ALA

SER

ILE

THR

ILE

GLN

ASN

THR

14

THR

Samples:

sample_1: DafA-DnaK, [U-100% 13C; U-100% 15N], 600 uM; D2O 5%; H2O 95%; potassium phosphate 20 mM; potassium chloride 100 mM; DTT 5 mM

sample_conditions_1: ionic strength: 0.12 M; pH: 7.0; pressure: 1 atm; temperature: 320 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C 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 C(CO)NH	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 13C-separated NOESY	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - 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