BMRB Entry 26701

Title:
T-STAR KH domain
Deposition date:
2015-11-04
Original release date:
2016-01-06
Authors:
Feracci, Mikael; Dominguez, Cyril
Citation:

Citation: Feracci, Mikael; Foot, Jaelle; Grellscheid, Sushma; Danilenko, Marina; Stehle, Ralf; Gonchar, Oksana; Kang, Hyun-Seo; Dalgliesh, Caroline; Meyer, Helge; Liu, Yilei; Lahat, Albert; Sattler, Michael; Eperon, Ian; Elliott, David; Dominguez, Cyril. "Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68"  Nat. Commun. 7, 10355-10355 (2016).
PubMed: 26758068

Assembly members:

Assembly members:
T_STAR, polymer, 113 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: pLEICS-03

Data sets:
Data typeCount
15N chemical shifts101
1H chemical shifts101

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KH domain1

Entities:

Entity 1, KH domain 113 residues - Formula weight is not available

residues 1 and 2 are non-native amino acids from the tag after Tev cleavage

1   GLYALAILEASNLYSASNMETLYSLEUGLY
2   GLNLYSVALLEUILEPROVALLYSGLNPHE
3   PROLYSPHEASNPHEVALGLYLYSLEULEU
4   GLYPROARGGLYASNSERLEULYSARGLEU
5   GLNGLUGLUTHRLEUTHRLYSMETSERILE
6   LEUGLYLYSGLYSERMETARGASPLYSALA
7   LYSGLUGLUGLULEUARGLYSSERGLYGLU
8   ALALYSTYRPHEHISLEUASNASPASPLEU
9   HISVALLEUILEGLUVALPHEALAPROPRO
10   ALAGLUALATYRALAARGMETGLYHISALA
11   LEUGLUGLUILELYSLYSPHELEUILEPRO
12   ASPTYRASN

Samples:

sample_1: T_STAR, [U-15N], 0.5 ± 0.1 mM; T_STAR, [U-13C; U-15N], 1 ± 0.1 mM; H2O 93%; D2O 7%; sodium phosphate 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.2; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY v3.110, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP O75525
AlphaFold Q9UPA8

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