BMRB Entry 10205

Title:
Solution structure of the C2H2 type zinc finger (region 668-70) of human Zinc finger protein 28 homolog
Deposition date:
2008-03-05
Original release date:
2009-03-05
Authors:
Tomizawa, T.; Tochio, N.; Abe, H.; Saito, K.; Li, H.; Sato, M.; Koshiba, S.; Kobayashi, N.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Tochio, N.; Tomizawa, T.; Abe, H.; Saito, K.; Li, H.; Sato, M.; Koshiba, S.; Kobayashi, N.; Kigawa, T.. "Solution structure of the C2H2 type zinc finger (region 668-70) of human Zinc finger protein 28 homolog"  .

Assembly members:

Assembly members:
zf-C2H2, UNP residues 668-700, 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   Vector: P061225-34

Entity Sequences (FASTA):

Entity Sequences (FASTA):
zf-C2H2, UNP residues 668-700: GSSGSSGTGEKPYECKECGK AFSQTTHLIQHQRVHTGEKP SGPSSG

Data sets:
Data typeCount
13C chemical shifts163
15N chemical shifts35
1H chemical shifts243

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zf-C2H2, UNP residues 668-7001
2ZINC ION2

Entities:

Entity 1, zf-C2H2, UNP residues 668-700 46 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTHRGLYGLU
2   LYSPROTYRGLUCYSLYSGLUCYSGLYLYS
3   ALAPHESERGLNTHRTHRHISLEUILEGLN
4   HISGLNARGVALHISTHRGLYGLULYSPRO
5   SERGLYPROSERSERGLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: zf-C2H2, UNP residues 668-700, [U-13C; U-15N], 1.0 ± 0.1 mM; d-Tris-HCl 20 mM; NaCl 100 mM; ZnCl2 0.05 mM; IDA 1 mM; d-DTT 1 mM; NaN3 0.02%; D2O 10%; H2O 90%

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 v20030801, Delaglio, F - processing

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

Kujira v0.9820, Kobayashi, N. - data analysis

CYANA v2.0.17, Guentert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 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