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 11414

Title: Solution structure of C2H2 type Zinc finger domain 345 in Zinc finger protein 278

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 345 in Zinc finger protein 278"  .

Assembly members:
C2H2 domain, polymer, 95 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: P060718-20

Entity Sequences (FASTA):
C2H2 domain: GSSGSSGVACEICGKIFRDV YHLNRHKLSHSGEKPYSCPV CGLRFKRKDRMSYHVRSHDG SVGKPYICQSCGKGFSRPDH LNGHIKQVHSGPSSG

Data sets:
Data typeCount
13C chemical shifts376
15N chemical shifts83
1H chemical shifts579

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C2H2 domain1
2ZINC ION no.12
3ZINC ION no.22
4ZINC ION no.32

Entities:

Entity 1, C2H2 domain 95 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYVALALACYS
2   GLUILECYSGLYLYSILEPHEARGASPVAL
3   TYRHISLEUASNARGHISLYSLEUSERHIS
4   SERGLYGLULYSPROTYRSERCYSPROVAL
5   CYSGLYLEUARGPHELYSARGLYSASPARG
6   METSERTYRHISVALARGSERHISASPGLY
7   SERVALGLYLYSPROTYRILECYSGLNSER
8   CYSGLYLYSGLYPHESERARGPROASPHIS
9   LEUASNGLYHISILELYSGLNVALHISSER
10   GLYPROSERSERGLY

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

1   ZN

Samples:

sample_1: C2H2 domain 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
DBJ BAE38619 BAF84492
GB AAF32518 AAF99602 AAG09031 AAG09035 AAH21091
REF NP_001240620 NP_001264144 NP_114440 XP_001927041 XP_003317256

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