BMRB Entry 16213

Title:
A Complete NMR Spectral Assignment of the MESD Protein
Deposition date:
2009-03-12
Original release date:
2010-06-28
Authors:
Chen, Jianglei; Wang, Jianjun
Citation:

Citation: Chen, Jianglei; Li, Qianqian; Liu, Chia-Chen; Zhou, Bei; Bu, Guojun; Wang, Jianjun. "NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6."  J. Biomol. NMR 47, 283-288 (2010).
PubMed: 20506034

Assembly members:

Assembly members:
MESD, polymer, 195 residues, 22037.7 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTWIN1

Data sets:
Data typeCount
13C chemical shifts599
15N chemical shifts190
1H chemical shifts1277

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MESD1

Entities:

Entity 1, MESD 195 residues - 22037.7 Da.

1   ALAASPTHRPROGLYGLUALATHRPROPRO
2   PROARGLYSLYSLYSASPILEARGASPTYR
3   ASNASPALAASPMETALAARGLEULEUGLU
4   GLNTRPGLULYSASPASPASPILEGLUGLU
5   GLYASPLEUPROGLUHISLYSARGPROSER
6   ALAPROILEASPPHESERLYSLEUASPPRO
7   GLYLYSPROGLUSERILELEULYSMETTHR
8   LYSLYSGLYLYSTHRLEUMETMETPHEVAL
9   THRVALSERGLYASNPROTHRGLULYSGLU
10   THRGLUGLUILETHRSERLEUTRPGLNGLY
11   SERLEUPHEASNALAASNTYRASPVALGLN
12   ARGPHEILEVALGLYSERASPARGALAILE
13   PHEMETLEUARGASPGLYSERTYRALATRP
14   GLUILELYSASPPHELEUVALSERGLNASP
15   ARGCYSALAGLUVALTHRLEUGLUGLYGLN
16   METTYRPROGLYLYSGLYGLYGLYSERLYS
17   GLULYSASNLYSTHRLYSPROGLULYSALA
18   LYSLYSLYSGLUGLYASPPROLYSPROARG
19   ALASERLYSGLUASPASNARGALAGLYSER
20   ARGARGGLUASPLEU

Samples:

sample_1: MESD, [U-13C; U-15N], 0.8 – 1.0 mM; sodium chloride 25 mM; EDTA 10 mM; DTT 10 mM; sodium azide 0.1 mM; sodium phosphate 25 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCTOCSYsample_1isotropicsample_conditions_1
3D CCCTOCSYsample_1isotropicsample_conditions_1
4D 13C/15N-edited NOESYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 11076
PDB
DBJ BAB25865 BAC27617 BAC36471 BAC36476
GB AAG33621 AAH14742 AAH85892 EDL06865 EDL06866
REF NP_001008346 NP_075892
SP Q5U2R7 Q9ERE7
AlphaFold Q5U2R7 Q9ERE7

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