BMRB Entry 11302

Title:
Solution structure of the N-terminal C2H2 type zinc-binding domain of the Zinc finger protein 64, isoforms 1 and 2
Deposition date:
2010-08-09
Original release date:
2011-08-19
Authors:
Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the N-terminal C2H2 type zinc-binding domain of the Zinc finger protein 64, isoforms 1 and 2"  .

Assembly members:

Assembly members:
C2H2-type zinc-binding domain, polymer, 96 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P050815-12

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts373
15N chemical shifts75
1H chemical shifts561

Additional metadata:

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

Assembly:

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

Entities:

Entity 1, C2H2-type zinc-binding domain 96 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPROHISLYS
2   CYSGLUVALCYSGLYLYSCYSPHESERARG
3   LYSASPLYSLEULYSTHRHISMETARGCYS
4   HISTHRGLYVALLYSPROTYRLYSCYSLYS
5   THRCYSASPTYRALAALAALAASPSERSER
6   SERLEUASNLYSHISLEUARGILEHISSER
7   ASPGLUARGPROPHELYSCYSGLNILECYS
8   PROTYRALASERARGASNSERSERGLNLEU
9   THRVALHISLEUARGSERHISTHRGLYASP
10   SERGLYPROSERSERGLY

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

1   ZN

Samples:

sample_1: C2H2 type zinc-binding domain, [U-13C; U-15N], 1.28 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 50 uM; IDA 1 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 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-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 v0.9736, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
GB EDL06563
REF XP_012374462

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