BMRB Entry 51187

Name: Backbone and sidechain NMR assignments of the J-domain of co-chaperone Sis1 in complex with EEVD peptide of HSP70
Published: 2022-11-23

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PDB ID: 8eod
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51187
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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:

Backbone and sidechain NMR assignments of the J-domain of co-chaperone Sis1 in complex with EEVD peptide of HSP70

Deposition date:

2021-11-23

Original release date:

2022-11-23

Authors:

Matos, Carolina; Pinheiro, Glaucia; Ramos, Carlos; Almeida, Fabio

Citation:

Citation: Matos, Carolina; Pinheiro, Glaucia; Ramos, Carlos; Almeida, Fabio. "Backbone and sidechain NMR assignments of residues 1-81 from yeast Sis1 in complex with an Hsp70 C-terminal EEVD peptide" Biomol. NMR Assign. 17, 239-242 (2023).
PubMed: 37589820

Assembly members:

Assembly members:
entity_1, polymer, 84 residues, Formula weight is not available
entity_2, polymer, 8 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pEt32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GMTSVKETKLYDLLGVSPSA NEQELKKGYRKAALKYHPDK PTGDTEKFKEISEAFEILND PQKREIYDQYGLEAARSGGP SFGP
entity_2: GPTIEEVD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	355
15N chemical shifts	77
1H chemical shifts	548

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	J-domain of Sis1	1
2	HSP70 C-terminal tail octapeptide	2

Entities:

Entity 1, J-domain of Sis1 84 residues - Formula weight is not available

1

GLY

MET

THR

SER

VAL

LYS

GLU

THR

LYS

LEU

2

TYR

ASP

LEU

GLY

VAL

SER

PRO

SER

ALA

3

ASN

GLU

GLN

GLU

LEU

LYS

GLY

TYR

ARG

4

LYS

ALA

LEU

LYS

TYR

HIS

PRO

ASP

LYS

5

PRO

THR

GLY

ASP

THR

GLU

LYS

PHE

LYS

GLU

6

ILE

SER

GLU

ALA

PHE

GLU

ILE

LEU

ASN

ASP

7

PRO

GLN

LYS

ARG

GLU

ILE

TYR

ASP

GLN

TYR

8

GLY

LEU

GLU

ALA

ARG

SER

GLY

PRO

9

SER

PHE

GLY

PRO

Entity 2, HSP70 C-terminal tail octapeptide 8 residues - Formula weight is not available

1

GLY

PRO

THR

ILE

GLU

VAL

ASP

Samples:

sample_1: Sis1 J-domain, [U-95% 13C; U-95% 15N], 1 mM; GPTIEEVD 4 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.5; 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
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

ANALYSIS - chemical shift assignment, chemical shift calculation, data analysis

NMR spectrometers:

Bruker AVANCE III 900 MHz

UNIPROT	P11142 P11142
AlphaFold	Q9H3R6 Q9H3R6