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 10207

Title: Solution structure of the C2H2 type zinc finger (region 368-400) of human Zinc finger protein 347

Deposition date: 2008-03-18 Original release date: 2009-03-18

Authors: Tochio, N.; Tomizawa, T.; Abe, H.; Saito, K.; Li, H.; Sato, M.; Koshiba, S.; Kobayashi, N.; Kigawa, T.; Yokoyama, S.

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 368-400) of human Zinc finger protein 347"  .

Assembly members:
zf-C2H2, UNP residues 368-400, 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   Vector: P070115-11

Entity Sequences (FASTA):
zf-C2H2, UNP residues 368-400: GSSGSSGTGEKPYKCNECGK AFRARSSLAIHQATHSGEKP SGPSSG

Data sets:
Data typeCount
13C chemical shifts146
15N chemical shifts32
1H chemical shifts225

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zf-C2H2, UNP residues 368-4001
2ZINC ION2

Entities:

Entity 1, zf-C2H2, UNP residues 368-400 46 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTHRGLYGLU
2   LYSPROTYRLYSCYSASNGLUCYSGLYLYS
3   ALAPHEARGALAARGSERSERLEUALAILE
4   HISGLNALATHRHISSERGLYGLULYSPRO
5   SERGLYPROSERSERGLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: zf-C2H2, UNP residues 368-400' '[U-13C; U-15N] 0.1; .; .; .; .; .; .; .; .

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, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 900 MHz

Related Database Links:

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