BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 11395

Title: Solution structure of the 11th C2H2 type zinc finger domain of Zinc finger protein 224

Deposition date: 2010-09-09 Original release date: 2011-09-08

Authors: Masuda, K.; Suzuki, S.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.

Citation: Masuda, K.; Suzuki, S.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.. "Solution structure of the 11th C2H2 type zinc finger domain of Zinc finger protein 224"  .

Assembly members:
zinc finger domain, polymer, 46 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: p061225-41

Entity Sequences (FASTA):
zinc finger domain: GSSGSSGTGEKLYNCKECGK SFSRAPCLLKHERLHSGEKP SGPSSG

Data sets:
Data typeCount
13C chemical shifts152
15N chemical shifts34
1H chemical shifts234

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zinc finger domain1
2ZINC ION2

Entities:

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

1   GLYSERSERGLYSERSERGLYTHRGLYGLU
2   LYSLEUTYRASNCYSLYSGLUCYSGLYLYS
3   SERPHESERARGALAPROCYSLEULEULYS
4   HISGLUARGLEUHISSERGLYGLULYSPRO
5   SERGLYPROSERSERGLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: zinc finger domain, [U-13C; U-15N], 1.11 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 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 700 MHz

Related Database Links:

PDB

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