BMRB Entry 11384

Title:
Solution structure of the 24th C2H2 type zinc finger domain of Zinc finger protein 268
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 24th C2H2 type zinc finger domain of Zinc finger protein 268"  .

Assembly members:

Assembly members:
zinc finger domain, UNP residues 915-947, polymer, 46 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: P061225-05

Entity Sequences (FASTA):

Entity Sequences (FASTA):
zinc finger domain, UNP residues 915-947: GSSGSSGTGEKPCKCTECGK AFCWKSQLIMHQRTHVDDKH SGPSSG

Data sets:
Data typeCount
13C chemical shifts154
15N chemical shifts34
1H chemical shifts221

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zinc finger domain, UNP residues 915-9471
2ZINC ION2

Entities:

Entity 1, zinc finger domain, UNP residues 915-947 46 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTHRGLYGLU
2   LYSPROCYSLYSCYSTHRGLUCYSGLYLYS
3   ALAPHECYSTRPLYSSERGLNLEUILEMET
4   HISGLNARGTHRHISVALASPASPLYSHIS
5   SERGLYPROSERSERGLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: zinc finger domain, UNP residues 915-947, [U-13C; U-15N], 1.15 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 700 MHz

Related Database Links:

PDB

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