BMRB Entry 27408

Title:
Axin RGS domain
Deposition date:
2018-02-21
Original release date:
2018-03-02
Authors:
Lee, Weontae; Yun, Jihye
Citation:

Citation: Cha, Pu-Hyeon; Cho, Yong-Hee; Lee, Sang-Kyu; Lee, JaeHeon; Jeong, Woo-Jeong; Moon, Byoung-San; Yun, Jihye; Yang, Jee Sun; Choi, Sooho; Soon, Juyong; Kim, Hyun-Yi; Kim, Mi-Yeon; Kaduwal, Saluja; Lee, Weontae; Min, Do Sik; Kim, Hoguen; Han, Gyoonhee; Choi, Kang-Yell. "Small-molecule binding of the axin RGS domain promotes beta-catenin and Ras degradation."  Nat. Chem. Biol. 12, 593-600 (2016).
PubMed: 27294323

Assembly members:

Assembly members:
Axin_RGS_domain, polymer, 147 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32a

Data sets:
Data typeCount
13C chemical shifts216
15N chemical shifts108
1H chemical shifts108

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Axin RGS domain1

Entities:

Entity 1, Axin RGS domain 147 residues - Formula weight is not available

1   GLYSERALASERPROTHRPROPROTYRLEU
2   LYSTRPALAGLUSERLEUHISSERLEULEU
3   ASPASPGLNASPGLYILESERLEUPHEARG
4   THRPHELEULYSGLNGLUGLYCYSALAASP
5   LEULEUASPPHETRPPHEALACYSTHRGLY
6   PHEARGLYSLEUGLUPROCYSASPSERASN
7   GLUGLULYSARGLEULYSLEUALAARGALA
8   ILETYRARGLYSTYRILELEUASPASNASN
9   GLYILEVALSERARGGLNTHRLYSPROALA
10   THRLYSSERPHEILELYSGLYCYSILEMET
11   LYSGLNLEUILEASPPROALAMETPHEASP
12   GLNALAGLNTHRGLUILEGLNALATHRMET
13   GLUGLUASNTHRTYRPROSERPHELEULYS
14   SERASPILETYRLEUGLUTYRTHRARGTHR
15   GLYSERGLUSERPROLYSVAL

Samples:

sample_1: Axin RGS domain, [U-99% 13C; U-99% 15N], 0.5 mM; Axin RGS domain, [U-99% 15N], 0.5 mM

Axin_RGS_domain_conditions: ionic strength: 0.3 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicAxin_RGS_domain_conditions
3D CBCA(CO)NHsample_1isotropicAxin_RGS_domain_conditions
3D HNCACBsample_1isotropicAxin_RGS_domain_conditions
3D HNCAsample_1isotropicAxin_RGS_domain_conditions

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz

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