BMRB Entry 28000

Name: Structural basis for client recognition and activity of Hsp40 chaperones
Published: 2019-11-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28000

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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 PubMed: 31604242

Deposition date: 2019-08-16 Original release date: 2019-11-07

Authors: jiang, yajun; rossi, paolo; kalodimos, charalampos

Citation: Jiang, Yajun; Rossi, Paolo; Kalodimos, Charalampos. "Structural basis for client recognition and activity of Hsp40 chaperones" Science 365, 1313-1319 (2019).

Assembly members:
Ydj1-SBD, polymer, 240 residues, Formula weight is not available

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet16b

Entity Sequences (FASTA):
Ydj1-SBD: RGKDIKHEISASLEELYKGR TAKLALNKQILCKECEGRGG KKGAVKKCTSCNGQGIKFVT RQMGPMIQRFQTECDVCHGT GDIIDPKDRCKSCNGKKVEN ERKILEVHVEPGMKDGQRIV FKGEADQAPDVIPGDVVFIV SERPHKSFKRDGDDLVYEAE IDLLTAIAGGEFALEHVSGD WLKVGIVPGEVIAPGMRKVI EGKGMPIPKYGGYGNLIIKF TIKDPENHFTSEENLKKLEE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	217
1H chemical shifts	217

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ydj1_SBD	1

Entities:

Entity 1, Ydj1_SBD 240 residues - Formula weight is not available

1	ARG	GLY	LYS	ASP	ILE	LYS	HIS	GLU	ILE	SER
2	ALA	SER	LEU	GLU	GLU	LEU	TYR	LYS	GLY	ARG
3	THR	ALA	LYS	LEU	ALA	LEU	ASN	LYS	GLN	ILE
4	LEU	CYS	LYS	GLU	CYS	GLU	GLY	ARG	GLY	GLY
5	LYS	LYS	GLY	ALA	VAL	LYS	LYS	CYS	THR	SER
6	CYS	ASN	GLY	GLN	GLY	ILE	LYS	PHE	VAL	THR
7	ARG	GLN	MET	GLY	PRO	MET	ILE	GLN	ARG	PHE
8	GLN	THR	GLU	CYS	ASP	VAL	CYS	HIS	GLY	THR
9	GLY	ASP	ILE	ILE	ASP	PRO	LYS	ASP	ARG	CYS
10	LYS	SER	CYS	ASN	GLY	LYS	LYS	VAL	GLU	ASN
11	GLU	ARG	LYS	ILE	LEU	GLU	VAL	HIS	VAL	GLU
12	PRO	GLY	MET	LYS	ASP	GLY	GLN	ARG	ILE	VAL
13	PHE	LYS	GLY	GLU	ALA	ASP	GLN	ALA	PRO	ASP
14	VAL	ILE	PRO	GLY	ASP	VAL	VAL	PHE	ILE	VAL
15	SER	GLU	ARG	PRO	HIS	LYS	SER	PHE	LYS	ARG
16	ASP	GLY	ASP	ASP	LEU	VAL	TYR	GLU	ALA	GLU
17	ILE	ASP	LEU	LEU	THR	ALA	ILE	ALA	GLY	GLY
18	GLU	PHE	ALA	LEU	GLU	HIS	VAL	SER	GLY	ASP
19	TRP	LEU	LYS	VAL	GLY	ILE	VAL	PRO	GLY	GLU
20	VAL	ILE	ALA	PRO	GLY	MET	ARG	LYS	VAL	ILE
21	GLU	GLY	LYS	GLY	MET	PRO	ILE	PRO	LYS	TYR
22	GLY	GLY	TYR	GLY	ASN	LEU	ILE	ILE	LYS	PHE
23	THR	ILE	LYS	ASP	PRO	GLU	ASN	HIS	PHE	THR
24	SER	GLU	GLU	ASN	LEU	LYS	LYS	LEU	GLU	GLU

Samples:

sample_1: Ydj1-SBD, [U-13C; U-15N; U-2H], 400 uM; TRIS 20 mM; potassium chloride 75 mM

sample_conditions_1: ionic strength: 0.1 M; 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
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCOCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - data analysis

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

NMR spectrometers:

Bruker Avance 700 MHz

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

1	ARG	GLY	LYS	ASP	ILE	LYS	HIS	GLU	ILE	SER
2	ALA	SER	LEU	GLU	GLU	LEU	TYR	LYS	GLY	ARG
3	THR	ALA	LYS	LEU	ALA	LEU	ASN	LYS	GLN	ILE
4	LEU	CYS	LYS	GLU	CYS	GLU	GLY	ARG	GLY	GLY
5	LYS	LYS	GLY	ALA	VAL	LYS	LYS	CYS	THR	SER
6	CYS	ASN	GLY	GLN	GLY	ILE	LYS	PHE	VAL	THR
7	ARG	GLN	MET	GLY	PRO	MET	ILE	GLN	ARG	PHE
8	GLN	THR	GLU	CYS	ASP	VAL	CYS	HIS	GLY	THR
9	GLY	ASP	ILE	ILE	ASP	PRO	LYS	ASP	ARG	CYS
10	LYS	SER	CYS	ASN	GLY	LYS	LYS	VAL	GLU	ASN
11	GLU	ARG	LYS	ILE	LEU	GLU	VAL	HIS	VAL	GLU
12	PRO	GLY	MET	LYS	ASP	GLY	GLN	ARG	ILE	VAL
13	PHE	LYS	GLY	GLU	ALA	ASP	GLN	ALA	PRO	ASP
14	VAL	ILE	PRO	GLY	ASP	VAL	VAL	PHE	ILE	VAL
15	SER	GLU	ARG	PRO	HIS	LYS	SER	PHE	LYS	ARG
16	ASP	GLY	ASP	ASP	LEU	VAL	TYR	GLU	ALA	GLU
17	ILE	ASP	LEU	LEU	THR	ALA	ILE	ALA	GLY	GLY
18	GLU	PHE	ALA	LEU	GLU	HIS	VAL	SER	GLY	ASP
19	TRP	LEU	LYS	VAL	GLY	ILE	VAL	PRO	GLY	GLU
20	VAL	ILE	ALA	PRO	GLY	MET	ARG	LYS	VAL	ILE
21	GLU	GLY	LYS	GLY	MET	PRO	ILE	PRO	LYS	TYR
22	GLY	GLY	TYR	GLY	ASN	LEU	ILE	ILE	LYS	PHE
23	THR	ILE	LYS	ASP	PRO	GLU	ASN	HIS	PHE	THR
24	SER	GLU	GLU	ASN	LEU	LYS	LYS	LEU	GLU	GLU

1	ARG	GLY	LYS	ASP	ILE	LYS	HIS	GLU	ILE	SER
2	ALA	SER	LEU	GLU	GLU	LEU	TYR	LYS	GLY	ARG
3	THR	ALA	LYS	LEU	ALA	LEU	ASN	LYS	GLN	ILE
4	LEU	CYS	LYS	GLU	CYS	GLU	GLY	ARG	GLY	GLY
5	LYS	LYS	GLY	ALA	VAL	LYS	LYS	CYS	THR	SER
6	CYS	ASN	GLY	GLN	GLY	ILE	LYS	PHE	VAL	THR
7	ARG	GLN	MET	GLY	PRO	MET	ILE	GLN	ARG	PHE
8	GLN	THR	GLU	CYS	ASP	VAL	CYS	HIS	GLY	THR
9	GLY	ASP	ILE	ILE	ASP	PRO	LYS	ASP	ARG	CYS
10	LYS	SER	CYS	ASN	GLY	LYS	LYS	VAL	GLU	ASN
11	GLU	ARG	LYS	ILE	LEU	GLU	VAL	HIS	VAL	GLU
12	PRO	GLY	MET	LYS	ASP	GLY	GLN	ARG	ILE	VAL
13	PHE	LYS	GLY	GLU	ALA	ASP	GLN	ALA	PRO	ASP
14	VAL	ILE	PRO	GLY	ASP	VAL	VAL	PHE	ILE	VAL
15	SER	GLU	ARG	PRO	HIS	LYS	SER	PHE	LYS	ARG
16	ASP	GLY	ASP	ASP	LEU	VAL	TYR	GLU	ALA	GLU
17	ILE	ASP	LEU	LEU	THR	ALA	ILE	ALA	GLY	GLY
18	GLU	PHE	ALA	LEU	GLU	HIS	VAL	SER	GLY	ASP
19	TRP	LEU	LYS	VAL	GLY	ILE	VAL	PRO	GLY	GLU
20	VAL	ILE	ALA	PRO	GLY	MET	ARG	LYS	VAL	ILE
21	GLU	GLY	LYS	GLY	MET	PRO	ILE	PRO	LYS	TYR
22	GLY	GLY	TYR	GLY	ASN	LEU	ILE	ILE	LYS	PHE
23	THR	ILE	LYS	ASP	PRO	GLU	ASN	HIS	PHE	THR
24	SER	GLU	GLU	ASN	LEU	LYS	LYS	LEU	GLU	GLU

1	ARG	GLY	LYS	ASP	ILE	LYS	HIS	GLU	ILE	SER
2	ALA	SER	LEU	GLU	GLU	LEU	TYR	LYS	GLY	ARG
3	THR	ALA	LYS	LEU	ALA	LEU	ASN	LYS	GLN	ILE
4	LEU	CYS	LYS	GLU	CYS	GLU	GLY	ARG	GLY	GLY
5	LYS	LYS	GLY	ALA	VAL	LYS	LYS	CYS	THR	SER
6	CYS	ASN	GLY	GLN	GLY	ILE	LYS	PHE	VAL	THR
7	ARG	GLN	MET	GLY	PRO	MET	ILE	GLN	ARG	PHE
8	GLN	THR	GLU	CYS	ASP	VAL	CYS	HIS	GLY	THR
9	GLY	ASP	ILE	ILE	ASP	PRO	LYS	ASP	ARG	CYS
10	LYS	SER	CYS	ASN	GLY	LYS	LYS	VAL	GLU	ASN
11	GLU	ARG	LYS	ILE	LEU	GLU	VAL	HIS	VAL	GLU
12	PRO	GLY	MET	LYS	ASP	GLY	GLN	ARG	ILE	VAL
13	PHE	LYS	GLY	GLU	ALA	ASP	GLN	ALA	PRO	ASP
14	VAL	ILE	PRO	GLY	ASP	VAL	VAL	PHE	ILE	VAL
15	SER	GLU	ARG	PRO	HIS	LYS	SER	PHE	LYS	ARG
16	ASP	GLY	ASP	ASP	LEU	VAL	TYR	GLU	ALA	GLU
17	ILE	ASP	LEU	LEU	THR	ALA	ILE	ALA	GLY	GLY
18	GLU	PHE	ALA	LEU	GLU	HIS	VAL	SER	GLY	ASP
19	TRP	LEU	LYS	VAL	GLY	ILE	VAL	PRO	GLY	GLU
20	VAL	ILE	ALA	PRO	GLY	MET	ARG	LYS	VAL	ILE
21	GLU	GLY	LYS	GLY	MET	PRO	ILE	PRO	LYS	TYR
22	GLY	GLY	TYR	GLY	ASN	LEU	ILE	ILE	LYS	PHE
23	THR	ILE	LYS	ASP	PRO	GLU	ASN	HIS	PHE	THR
24	SER	GLU	GLU	ASN	LEU	LYS	LYS	LEU	GLU	GLU