BMRB Entry 30629

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

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30629

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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: 2019-07-09 Original release date: 2019-09-11

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

Citation: Jiang, Y.; Rossi, P.; Kalodimos, C.. "Structural Basis for Client Recognition and Activity of Hsp40 Chaperones" . ., .-..

Assembly members:
entity_1, polymer, 89 residues, 9017.255 Da.

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

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

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	308
15N chemical shifts	65
1H chemical shifts	477

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 - 9017.255 Da.

1

MET

GLU

THR

ALA

THR

ALA

GLY

GLU

TRP

GLN

2

GLY

LYS

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: PhoA_235-245_DnaJ_191-256, [U-13C; U-15N], 1 mM; potassium phosphate 20 mM; potassium chloride 75 mM; sodium azide 0.04%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CCH-NOESY	sample_1	isotropic	sample_conditions_1
3D CCH_TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	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
2D 1H-15N HSQC	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

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

TopSpin v4.0, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

PSVS, Bhattacharya and Montelione - processing

NMR spectrometers:

Bruker AVANCE NEO 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts