BMRB Entry 30457

Name: HSP40 co-chaperone Sis1 J-domain
Published: 2019-04-24

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PDB ID: 6d6x
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30457
MolProbity Validation Chart

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3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

HSP40 co-chaperone Sis1 J-domain

Deposition date:

2018-04-23

Original release date:

2019-04-24

Authors:

Pinheiro, G.; Amorim, G.; Iqbal, A.; Ramos, C.; Almeida, F.

Citation:

Citation: Pinheiro, Glaucia; Amorim, Gisele; Iqbal, Anwar; Almeida, Fabio; Ramos, C. "Solution NMR investigation on the structure and function of the isolated J-domain from Sis1: Evidence of transient inter-domain interactions in the full-length protein" Arch. Biochem. Biophys. 669, 71-79 (2019).
PubMed: 31141701

Assembly members:

Assembly members:
entity_1, polymer, 81 residues, 9091.122 Da.

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 BL21(DE3) Vector: pEt32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SVKETKLYDLLGVSPSANEQ ELKKGYRKAALKYHPDKPTG DTEKFKEISEAFEILNDPQK REIYDQYGLEAARSGGPSFG P

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	323
15N chemical shifts	73
1H chemical shifts	467

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 81 residues - 9091.122 Da.

1

SER

VAL

LYS

GLU

THR

LYS

LEU

TYR

ASP

LEU

2

LEU

GLY

VAL

SER

PRO

SER

ALA

ASN

GLU

GLN

3

GLU

LEU

LYS

GLY

TYR

ARG

LYS

ALA

4

LEU

LYS

TYR

HIS

PRO

ASP

LYS

PRO

THR

GLY

5

ASP

THR

GLU

LYS

PHE

LYS

GLU

ILE

SER

GLU

6

ALA

PHE

GLU

ILE

LEU

ASN

ASP

PRO

GLN

LYS

7

ARG

GLU

ILE

TYR

ASP

GLN

TYR

GLY

LEU

GLU

8

ALA

ARG

SER

GLY

PRO

SER

PHE

GLY

9

PRO

Samples:

sample_1: Sis1 1-81, [U-13C; U-15N], 220 uM

sample_2: Sis1 1-81, [U-15N], 200 uM

sample_conditions_1: ionic strength: 200 mM; pH: 7.5; pressure: 1 atm; temperature: 303 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

Analysis, CCPN - chemical shift assignment, data analysis, peak picking

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

CS-Rosetta, Shen, Vernon, Baker and Bax - refinement, structure calculation

NMR spectrometers:

Bruker DRX 600 MHz
Bruker AvanceIII 800 MHz

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