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 11416

Title: Solution structure of C2H2 type Zinc finger domain 5 in Zinc finger protein 32

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

Authors: Kasahara, N.; Tsuda, K.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.

Citation: Kasahara, N.; Tsuda, K.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.. "Solution structure of C2H2 type Zinc finger domain 5 in Zinc finger protein 32"  .

Assembly members:
zinc-finger motif, polymer, 42 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: P061204-06

Entity Sequences (FASTA):
zinc-finger motif: GSSGSSGGEKPYRCDQCGKA FSQKGSLIVHIRVHTGSGPS SG

Data sets:
Data typeCount
13C chemical shifts137
15N chemical shifts31
1H chemical shifts214

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1zinc-finger motif1
2ZINC ION2

Entities:

Entity 1, zinc-finger motif 42 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLYGLULYS
2   PROTYRARGCYSASPGLNCYSGLYLYSALA
3   PHESERGLNLYSGLYSERLEUILEVALHIS
4   ILEARGVALHISTHRGLYSERGLYPROSER
5   SERGLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: zinc-finger motif 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, Jonson B.A. - data analysis

Kujira v0.9820, Kobayashi N. - data analysis

CYANA v2.0.17, Gutert 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 shifts
SPARKY: Backbone or all simulated shifts