BMRB Entry 30761

Name: NMR structure of Ost4 in DPC micelles
Published: 2021-02-04

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PDB ID: 6xcu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30761
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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:

NMR structure of Ost4 in DPC micelles

Deposition date:

2020-06-09

Original release date:

2021-02-04

Authors:

Chaudhary, B.

Citation:

Citation: Chaudhary, Bharat; Zoetewey, David; McCullagh, Martin; Mohanty, Smita. "NMR and MD simulations reveal the impact of the V23D mutation on the function of yeast oligosaccharyltransferase subunit Ost4" Glycobiology 31, 838-850 (2021).
PubMed: 33442744

Assembly members:

Assembly members:
entity_1, polymer, 45 residues, 5231.000 Da.

Natural source:

Natural source: Common Name: Baker's yeast Taxonomy ID: 307796 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: 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	unit_1	1

Entities:

Entity 1, unit_1 45 residues - 5231.000 Da.

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, [U-13C; U-15N], 400 uM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 308 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 H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRFAM-SPARKY, Lee, W., Tonelli, M., and Markley, J. L. - chemical shift assignment

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

NMR spectrometers:

Bruker AVANCE 600 MHz
Bruker AVANCE II 800 MHz
Varian INOVA 900 MHz

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