BMRB Entry 10226

Title:
Solution structure of the C2H2 type zinc finger (region 273-303) of human Zinc finger protein 268
Deposition date:
2008-08-19
Original release date:
2009-08-19
Authors:
Tochio, N.; Tomizawa, T.; 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.; Yokoyama, S.. "Solution structure of the C2H2 type zinc finger (region 273-303) of human Zinc finger protein 268"  .

Assembly members:

Assembly members:
zf-C2H2, UNP residues 273-303, polymer, 44 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: P061218-01

Entity Sequences (FASTA):

Entity Sequences (FASTA):
zf-C2H2, UNP residues 273-303: GSSGSSGEKPFGCSCCEKAF SSKSYLLVHQQTHAEEKPSG PSSG

Data sets:
Data typeCount
13C chemical shifts152
15N chemical shifts34
1H chemical shifts229

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zf-C2H2, UNP residues 273-3031
2ZINC ION2

Entities:

Entity 1, zf-C2H2, UNP residues 273-303 44 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLULYSPRO
2   PHEGLYCYSSERCYSCYSGLULYSALAPHE
3   SERSERLYSSERTYRLEULEUVALHISGLN
4   GLNTHRHISALAGLUGLULYSPROSERGLY
5   PROSERSERGLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: zf-C2H2, UNP residues 273-303, [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%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 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