BMRB Entry 30635

Name: Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
Published: 2019-09-11

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PDB ID: 6prj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30635
MolProbity Validation Chart

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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:

Structural Basis for Client Recognition and Activity of Hsp40 Chaperones

Deposition date:

2019-07-10

Original release date:

2019-09-11

Authors:

Jiang, Y.; Rossi, P.; Kalodimos, C.

Citation:

Citation: Jiang, Y.; Rossi, P.; Kalodimos, C.. "Structural basis for client recognition and activity of Hsp40 chaperones" Science 365, 1313-1319 (2019).
PubMed: 31604242

Assembly members:

Assembly members:
entity_1, polymer, 89 residues, 9128.503 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 83333 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MQTDLFYTMKAAGSGGSGGS GGSQDLYATLDVPAPIAVVG GKVRAMTLEGPVEVAVPPRT QAGRKLRLKGKGFPGPAGRG DLYLEVRIT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	327
15N chemical shifts	76
1H chemical shifts	506

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 89 residues - 9128.503 Da.

1

MET

GLN

THR

ASP

LEU

PHE

TYR

THR

MET

LYS

2

ALA

GLY

SER

GLY

SER

GLY

SER

3

GLY

SER

GLN

ASP

LEU

TYR

ALA

THR

LEU

4

ASP

VAL

PRO

ALA

PRO

ILE

ALA

VAL

GLY

5

GLY

LYS

VAL

ARG

ALA

MET

THR

LEU

GLU

GLY

6

PRO

VAL

GLU

VAL

ALA

VAL

PRO

ARG

THR

7

GLN

ALA

GLY

ARG

LYS

LEU

ARG

LEU

LYS

GLY

8

LYS

GLY

PHE

PRO

GLY

PRO

ALA

GLY

ARG

GLY

9

ASP

LEU

TYR

LEU

GLU

VAL

ARG

ILE

THR

Samples:

sample_1: G-CBD2, [U-100% 13C; U-100% 15N], 1 mM; potassium chloride 75 mM; potassium phosphate 20 mM; sodium azide 0.04%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 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 HBHA(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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D CCH_NOESY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

Sparky, Goddard - peak picking

TopSpin v4.0, Bruker Biospin - collection

PSVS, Bhattacharya and Montelione - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

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