BMRB Entry 11379

Title:
Solution structure of the secound zinc finger domain of Zinc finger protein 278
Deposition date:
2010-09-08
Original release date:
2011-09-07
Authors:
Tanabe, W.; Suzuki, S.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.
Citation:

Citation: Tanabe, W.; Suzuki, S.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.. "Solution structure of the secound zinc finger domain of Zinc finger protein 278"  .

Assembly members:

Assembly members:
zinc finger domain, UNP residues 350-384, polymer, 48 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

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: P061204-08

Entity Sequences (FASTA):

Entity Sequences (FASTA):
zinc finger domain, UNP residues 350-384: GSSGSSGRTRKQVACEICGK IFRDVYHLNRHKLSHSGEKP YSSGPSSG

Data sets:
Data typeCount
13C chemical shifts157
15N chemical shifts29
1H chemical shifts219

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zinc finger domain, UNP residues 350-3841
2ZINC ION2

Entities:

Entity 1, zinc finger domain, UNP residues 350-384 48 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYARGTHRARG
2   LYSGLNVALALACYSGLUILECYSGLYLYS
3   ILEPHEARGASPVALTYRHISLEUASNARG
4   HISLYSLEUSERHISSERGLYGLULYSPRO
5   TYRSERSERGLYPROSERSERGLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: zinc finger domain, UNP residues 350-384, [U-13C; U-15N], 0.25 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 0.05 mM; IDA 1 mM; H2O 90%; D2O 10%

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

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-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 BAA90874 BAD92024 BAE38619 BAF84492 BAG10581
EMBL CAB51404 CAG30499 CAK54641 CAK54940
GB AAF01349 AAF32518 AAF99602 AAG09031 AAG09032
REF NP_001100701 NP_001164822 NP_001178126 NP_001240619 NP_001240620
SP Q9HBE1
TPG DAA20504 DAA20505
AlphaFold Q9HBE1

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