BMRB Entry 36162

Name: Solution structure of the SBDalpha domain of yeast Ssa1
Published: 2018-10-12

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PDB ID: 5z8q
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36162
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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:

Solution structure of the SBDalpha domain of yeast Ssa1

Deposition date:

2018-02-01

Original release date:

2018-10-12

Authors:

Gong, W.; Hu, W.; Perrett, S.

Citation:

Citation: Gong, W.; Hu, W.; Xu, L.; Wu, H.; Wu, S.; Zhang, H.; Wang, J.; Jones, G.; Perrett, S.. "The C-terminal GGAP motif of Hsp70 mediates substrate recognition and stress response in yeast" J. Biol. Chem. 293, 17663-17675 (2018).
PubMed: 30228181

Assembly members:

Assembly members:
entity_1, polymer, 101 residues, 10788.742 Da.

Natural source:

Natural source: Common Name: Baker's yeast Taxonomy ID: 559292 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces Saccharomyces cerevisiae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SKEEDEKESQRIASKNQLES IAYSLKNTISEAGDKLEQAD KDTVTKKAEETISWLDSNTT ASKEEFDDKLKELQDIANPI MSKLYQAGGAPGGAAGGAPG G

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	405
15N chemical shifts	107
1H chemical shifts	616

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_1 101 residues - 10788.742 Da.

1

SER

LYS

GLU

ASP

GLU

LYS

GLU

SER

GLN

2

ARG

ILE

ALA

SER

LYS

ASN

GLN

LEU

GLU

SER

3

ILE

ALA

TYR

SER

LEU

LYS

ASN

THR

ILE

SER

4

GLU

ALA

GLY

ASP

LYS

LEU

GLU

GLN

ALA

ASP

5

LYS

ASP

THR

VAL

THR

LYS

ALA

GLU

6

THR

ILE

SER

TRP

LEU

ASP

SER

ASN

THR

7

ALA

SER

LYS

GLU

PHE

ASP

LYS

LEU

8

LYS

GLU

LEU

GLN

ASP

ILE

ALA

ASN

PRO

ILE

9

MET

SER

LYS

LEU

TYR

GLN

ALA

GLY

ALA

10

PRO

GLY

ALA

GLY

ALA

PRO

GLY

11

GLY

Samples:

sample_1: Ssa1 SBDalpha, [U-13C; U-15N], 1.0 mM; H2O 90%; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 90 mM; pH: 6.5; 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

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