BMRB Entry 17868

Title:
Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat
Deposition date:
2011-08-18
Original release date:
2012-03-27
Authors:
Borgert, Andrew; Heimburg-Molinaro, Jamie; Lasanajak, Yi; Ju, Tongzhong; Liu, Mian; Thompson, Pamela; Ragupathi, Govind; Barany, George; Cummings, Richard; Smith, David; Live, David
Citation:

Citation: Borgert, Andrew; Heimburg-Molinaro, Jamie; Song, Xuezheng; Lasanajak, Yi; Ju, Tongzhong; Liu, Mian; Thompson, Pamela; Ragupathi, Govind; Barany, George; Smith, David; Cummings, Richard; Live, David. "Deciphering structural elements of mucin glycoprotein recognition."  ACS Chem. Biol. 7, 1031-1039 (2012).
PubMed: 22444368

Assembly members:

Assembly members:
MUC2_Mucin_Domain_Peptide, polymer, 9 residues, 781.948 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MUC2_Mucin_Domain_Peptide: XPTTTPLKX

Data sets:
Data typeCount
13C chemical shifts27
15N chemical shifts5
1H chemical shifts53

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1MUC2_Mucin_Domain_Peptide1

Entities:

Entity 1, MUC2_Mucin_Domain_Peptide 9 residues - 781.948 Da.

Non-glycosylated peptide

1   XPROTHRTHRTHRPROLEULYSX

Samples:

sample_1: MUC2_Mucin_Domain_Peptide2 – 10 mM; H2O 90%; D2O 10%

sample_2: MUC2_Mucin_Domain_Peptide2 – 10 mM; D2O 100%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_2isotropicsample_conditions_all
3D TOCSY-NOESYsample_1isotropicsample_conditions_all
2D 1H-15N HSQCsample_1isotropicsample_conditions_all
2D 1H-13C HSQCsample_1isotropicsample_conditions_all
2D 1H-1H TOCSYsample_1isotropicsample_conditions_all
2D 1H-1H COSYsample_2isotropicsample_conditions_all
2D 1H-13C HMBCsample_1isotropicsample_conditions_all

Software:

CNS, Brunger A. T. et.al. - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 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