BMRB Entry 19759

Name: Tetra-O-GalNAc glycosylated mucin sequence from alpha dystroglycan mucin domain
Published: 2015-02-02

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PDB ID: 2mk7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19759
MolProbity Validation Chart

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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: Tetra-O-GalNAc glycosylated mucin sequence from alpha dystroglycan mucin domain

Deposition date: 2014-02-02 Original release date: 2015-02-02

Authors: Live, David; Borgert, Andrew

Citation: Borgert, Andrew; Foley, Lachele; Live, David. "Differential Conformational Effects of O-GalNAc and O-Man Glycan Protein Modifications: Implications for the role of O-GalNAc glycans in the Mucin-Like Region of alpha-Dystroglycan" to be published ., .-..

Assembly members:
aDG_Mucin_Domain_Peptide, polymer, 11 residues, 936.116 Da.
SUGAR_(4-MER), polymer, 4 residues, Formula weight is not available

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):
aDG_Mucin_Domain_Peptide: XPPTTTTKKPX
SUGAR_(4-MER): XXXX

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	62
15N chemical shifts	10
1H chemical shifts	109

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	aDG_Mucin_Domain_Peptide	1
2	SUGAR (4-MER)	2

Entities:

Entity 1, aDG_Mucin_Domain_Peptide 11 residues - 936.116 Da.

All T residues in this molecule are modified with alpha-linked N-acetylgalactosamine

1

ACE

PRO

THR

LYS

PRO

2

NH2

Entity 2, SUGAR (4-MER) 4 residues - Formula weight is not available

1

A2G

Samples:

sample_d2o: aDG_Mucin_Domain_Peptide2 – 10 mM; D2O 100%

sample_h2o: aDG_Mucin_Domain_Peptide2 – 10 mM; D2O 5%; H2O 95%

sample_conditions_all: ionic strength: 0 M; pH: 4.5; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_d2o	isotropic	sample_conditions_all
3D TOCSY-NOESY	sample_h2o	isotropic	sample_conditions_all
2D 1H-15N HSQC	sample_h2o	isotropic	sample_conditions_all
2D 1H-13C HSQC	sample_h2o	isotropic	sample_conditions_all
2D 1H-1H TOCSY	sample_h2o	isotropic	sample_conditions_all
2D 1H-1H COSY	sample_d2o	isotropic	sample_conditions_all
2D 1H-13C HMBC	sample_h2o	isotropic	sample_conditions_all

Software:

No software information available

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 800 MHz
Varian INOVA 900 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts