BMRB Entry 26833

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for alpha-N Catenin C-terminal domain
Deposition date:
2016-06-23
Original release date:
2017-02-20
Authors:
Nishikawa, Tadateru; Ishiyama, Noboru; Ikura, Mitsuhiko
Citation:

Citation: Nishikawa, Tadateru; Ishiyama, Noboru; Wang, Feng; Ikura, Mitsuhiko. "Backbone resonance assignments of the F-actin binding domain of mouse alpha N-catenin"  Biomol NMR Assign 11, 21-24 (2017).
PubMed: 27804064

Assembly members:

Assembly members:
alpha_N-catenin, polymer, 252 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: house 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: pGEX4T1

Data sets:
Data typeCount
13C chemical shifts719
15N chemical shifts228
1H chemical shifts228

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1alpha-N Catenin C-terminal domain1

Entities:

Entity 1, alpha-N Catenin C-terminal domain 252 residues - Formula weight is not available

First two residues, Gly-Ser, are come from plasmid.

1   GLYSERGLNTHRGLUASPASPGLNLEUILE
2   ALAGLYGLNSERALAARGALAILEMETALA
3   GLNLEUPROGLNGLUGLULYSALALYSILE
4   ALAGLUGLNVALGLUILEPHEHISGLNGLU
5   LYSSERLYSLEUASPALAGLUVALALALYS
6   TRPASPASPSERGLYASNASPILEILEVAL
7   LEUALALYSGLNMETCYSMETILEMETMET
8   GLUMETTHRASPPHETHRARGGLYLYSGLY
9   PROLEULYSASNTHRSERASPVALILEASN
10   ALAALALYSLYSILEALAGLUALAGLYSER
11   ARGMETASPLYSLEUALAARGALAVALALA
12   ASPGLNCYSPROASPSERALACYSLYSGLN
13   ASPLEULEUALATYRLEUGLNARGILEALA
14   LEUTYRCYSHISGLNLEUASNILECYSSER
15   LYSVALLYSALAGLUVALGLNASNLEUGLY
16   GLYGLULEUILEVALSERGLYLEUASPSER
17   ALATHRSERLEUILEGLNALAALALYSASN
18   LEUMETASNALAVALVALLEUTHRVALLYS
19   ALASERTYRVALALASERTHRLYSTYRGLN
20   LYSVALTYRGLYTHRALAALAVALASNSER
21   PROVALVALSERTRPLYSMETLYSALAPRO
22   GLULYSLYSPROLEUVALLYSARGGLULYS
23   PROGLUGLUPHEGLNTHRARGVALARGARG
24   GLYSERGLNLYSLYSHISILESERPROVAL
25   GLNALALEUSERGLUPHELYSALAMETASP
26   SERPHE

Samples:

sample_1: alpha N-catenin, [U-100% 13C; U-100% 15N; U-80% 2H], 0.4 mM; potassium phosphate 20 mM; sodium chloride 150 mM; TCEP 1 mM; sodium azide 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.17 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

NCBI NP_663785.2

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