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 10243

Title: Solution structures of the C2H2 type zinc finger domain of human Zinc finger protein 24

Authors: Sato, M.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Sato, M.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structures of the C2H2 type zinc finger domain of human Zinc finger protein 24"  . ., .-..

Assembly members:
C2H2 type zinc finger domain, polymer, 72 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

Entity Sequences (FASTA):
C2H2 type zinc finger domain: GSSGSSGIHSGEKPYGCVEC GKAFSRSSILVQHQRVHTGE KPYKCLECGKAFSQNSGLIN HQRIHTSGPSSG

Data sets:
Data typeCount
13C chemical shifts268
15N chemical shifts62
1H chemical shifts411

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C2H2 type zinc finger domain1
2ZINC ION no.12
3ZINC ION no.22

Entities:

Entity 1, C2H2 type zinc finger domain 72 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYILEHISSER
2   GLYGLULYSPROTYRGLYCYSVALGLUCYS
3   GLYLYSALAPHESERARGSERSERILELEU
4   VALGLNHISGLNARGVALHISTHRGLYGLU
5   LYSPROTYRLYSCYSLEUGLUCYSGLYLYS
6   ALAPHESERGLNASNSERGLYLEUILEASN
7   HISGLNARGILEHISTHRSERGLYPROSER
8   SERGLY

Entity 2, ZINC ION no.1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: C2H2 type zinc finger domain, [U-13C; U-15N], 1 mM; d-Tris HCl 20 mM; NaCl 100 mM; d-DTT 5 mM; NaN3 0.02%; ZnCl2 0.01 mM; 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 v20031121, Delaglio, F. - processing

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

Kujira v0.9295, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 900 MHz

Related Database Links:

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