BMRB Entry 50160

Name: Point mutant of Oligosaccharyltransferase subunit, Ost4V23D
Published: 2020-05-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50160

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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:

Point mutant of Oligosaccharyltransferase subunit, Ost4V23D

Deposition date:

2020-01-16

Original release date:

2020-05-30

Authors:

Chaudhary, Bharat; Zoetewey, David; Mohanty, Smita

Citation:

Citation: Chaudhary, Bharat; Zoetewey, David; Mohanty, Smita. "1H, 13C, 15N Resonance Assignments and Secondary Structure of Yeast Oligosaccharyltransferase Subunit Ost4 and Its Functionally Important Mutant Ost4V23D" Biomelecular NMR Assignments 14, 205-209 (2020).
PubMed: 32328881

Assembly members:

Assembly members:
Ost4V23D, polymer, 45 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: Pet23a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ost4V23D: MISDEQLNSLAITFGIVMMT LIDIYHAVDSTMSPKNRLEH HHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	82
15N chemical shifts	39
1H chemical shifts	245

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Point mutant Ost4V23D	1

Entities:

Entity 1, Point mutant Ost4V23D 45 residues - Formula weight is not available

1

MET

ILE

SER

ASP

GLU

GLN

LEU

ASN

SER

LEU

2

ALA

ILE

THR

PHE

GLY

ILE

VAL

MET

THR

3

LEU

ILE

ASP

ILE

TYR

HIS

ALA

VAL

ASP

SER

4

THR

MET

SER

PRO

LYS

ASN

ARG

LEU

GLU

HIS

5

HIS

Samples:

sample_1_Ost4V23D: Ost4V23D, [U-2H], 300 uM; DPC, [U-2H], 100 mM

sample_conditions_1_Solution: ionic strength: 0.35 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
1 H- 15 N HSQC	sample_1_Ost4V23D	isotropic	sample_conditions_1_Solution
1 H- 13 C HSQC	sample_1_Ost4V23D	isotropic	sample_conditions_1_Solution
3D HNCACB	sample_1_Ost4V23D	isotropic	sample_conditions_1_Solution
3D CBCACONH	sample_1_Ost4V23D	isotropic	sample_conditions_1_Solution
3D HNCA	sample_1_Ost4V23D	isotropic	sample_conditions_1_Solution
3D HN(CO)CA	sample_1_Ost4V23D	isotropic	sample_conditions_1_Solution
3D HNHAHB	sample_1_Ost4V23D	isotropic	sample_conditions_1_Solution
3D HBHA(CO)NH	sample_1_Ost4V23D	isotropic	sample_conditions_1_Solution
3D 13 C-edited HCCH-TOCSY	sample_1_Ost4V23D	isotropic	sample_conditions_1_Solution
3D H(CCO)NH-TOCSY	sample_1_Ost4V23D	isotropic	sample_conditions_1_Solution
3D 15 N-edited HSQC-TOCSY	sample_1_Ost4V23D	isotropic	sample_conditions_1_Solution

Software:

SPARKY, Bruker Biospin, Cornilescu, Delaglio and Bax, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment, collection, data analysis, geometry optimization, processing

NMR spectrometers:

Bruker, Varian Avance 800 MHz
Bruker, Varian Avance 900 MHz
Bruker, Varian 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