BMRB Entry 11397

Title:
Solution structure of the BACK domain of Kelch repeat and BTB domain-containing protein 4
Deposition date:
2010-09-09
Original release date:
2011-09-08
Authors:
Imai, M.; Suzuki, S.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.
Citation:

Citation: Imai, M.; Suzuki, S.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.. "Solution structure of the BACK domain of Kelch repeat and BTB domain-containing protein 4"  .

Assembly members:

Assembly members:
BACK domain, polymer, 105 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: cell free synthesis   Host organism: E. coli - cell free   Vector: P060821-14

Data sets:
Data typeCount
13C chemical shifts435
15N chemical shifts107
1H chemical shifts695

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BACK domain1

Entities:

Entity 1, BACK domain 105 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYVALGLNVAL
2   GLYASNCYSLEUGLNVALMETTRPLEUALA
3   ASPARGHISSERASPPROGLULEUTYRTHR
4   ALAALALYSHISCYSALALYSTHRHISLEU
5   ALAGLNLEUGLNASNTHRGLUGLUPHELEU
6   HISLEUPROHISARGLEULEUTHRASPILE
7   ILESERASPGLYVALPROCYSSERGLNASN
8   PROTHRGLUALAILEGLUALATRPILEASN
9   PHEASNLYSGLUGLUARGGLUALAPHEALA
10   GLUSERLEUARGTHRSERLEULYSGLUILE
11   GLYGLUASNVALHIS

Samples:

sample_1: BACK domain, [U-13C; U-15N], 1.15 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20060702, Delaglio F. - processing

NMRView v5.0.4, Johnson B.A. - data analysis

Kujira v0.9820, Kobayashi N. - data analysis

CYANA v2.1, Guntert P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAA91616 BAA91880 BAB03555 BAB27317 BAB29305
EMBL CAD28521 CAG33551 CAH90011 CAH93240
GB AAH02736 AAH25103 ADZ15413 AIC51824 EAW67898
REF NP_001101216 NP_001126905 NP_001247465 NP_001267133 NP_001298045
SP Q5R4S6 Q8R179 Q9N010 Q9NVX7
AlphaFold Q5R4S6 Q9NVX7 Q9N010 Q8R179

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