BMRB Entry 27405

Name: The 15N, 13C and 1H Chemical Shift Assignment of Sis1 J domain from S. cerevisiae
Published: 2019-04-24

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27405

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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:

The 15N, 13C and 1H Chemical Shift Assignment of Sis1 J domain from S. cerevisiae

Deposition date:

2018-02-15

Original release date:

2019-04-24

Authors:

Pinheiro, Glaucia; Amorim, Gisele; Iqbal, Anwar; Ramos, Carlos; Almeida, Fabio

Citation:

Citation: Pinheiro, Glaucia; Amorim, Gisele; Iqbal, Anwar; Ramos, Carlos; Almeida, Fabio. "1H, 15N and 13C resonance assignments of the J-domain of co-chaperone Sis1 from Saccharomyces cerevisiae" Biomol. NMR Assignments 12, 279-281 (2018).
PubMed: 29713947

Assembly members:

Assembly members:
Sis1_J-domain, polymer, 84 residues, 9366.455 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 Vector: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Sis1_J-domain: GMTSVKETKLYDLLGVSPSA NEQELKKGYRKAALKYHPDK PTGDTEKFKEISEAFEILND PQKREIYDQYGLEAARSGGP SFGP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

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	Sis1J	1

Entities:

Entity 1, Sis1J 84 residues - 9366.455 Da.

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

Samples:

sample_1: Sis1 J-domain 250 uM; TRIS HCl 25 mM; sodium chloride 200 mM

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/HMQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC/HMQC	sample_1	isotropic	sample_conditions_1
cbcaconh (H[N[co[{CA\|ca[C]}]]])	sample_1	isotropic	sample_conditions_1
hbhaconh (H{ca\|cca}[co[N]]HA)	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
hncaco (H[N[ca[CO]]])	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
hbcbcgcdcehe (hbCBcgcdceHE)	sample_1	isotropic	sample_conditions_1
hbcbcgcdhd (hbCBcgcdHD)	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
CCn-HCCHTOCSY (H[C_[C]].Jmultibond)	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CcpNmr_Analysis v2.3, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance III 600 MHz

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