BMRB Entry 11287

Title:
Solution structure of the C2H2 type zinc-binding domain of human zinc finger protein 292
Deposition date:
2010-08-09
Original release date:
2011-08-18
Authors:
Yoneyama, M.; Tomizawa, T.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Yoneyama, M.; Tomizawa, T.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the C2H2 type zinc-binding domain of human zinc finger protein 292"  .

Assembly members:

Assembly members:
C2H2 type zinc-binding domain, polymer, 73 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: P041018-02

Entity Sequences (FASTA):

Entity Sequences (FASTA):
C2H2 type zinc-binding domain: GSSGSSGRKKPVSQSLEFPT RYSPYRPYRCVHQGCFAAFT IQQNLILHYQAVHKSDLPAF SAEVEEESGPSSG

Data sets:
Data typeCount
13C chemical shifts297
15N chemical shifts62
1H chemical shifts450

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C2H2 type zinc-binding domain1
2ZINC ION2

Entities:

Entity 1, C2H2 type zinc-binding domain 73 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYARGLYSLYS
2   PROVALSERGLNSERLEUGLUPHEPROTHR
3   ARGTYRSERPROTYRARGPROTYRARGCYS
4   VALHISGLNGLYCYSPHEALAALAPHETHR
5   ILEGLNGLNASNLEUILELEUHISTYRGLN
6   ALAVALHISLYSSERASPLEUPROALAPHE
7   SERALAGLUVALGLUGLUGLUSERGLYPRO
8   SERSERGLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: C2H2 type zinc-binding domain, [U-13C; U-15N], 1.90 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 0.05 mM; NTA 0.1 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 v2.6, 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 800 MHz

Related Database Links:

PDB
DBJ BAA25456 BAB14654 BAI45414
EMBL CAD97823
GB AAB06954 AAH63594 AAI72360 AAV86070 AEB61065
REF NP_001179779 NP_055836 XP_001088554 XP_002806763 XP_002817165
SP O60281
TPG DAA26182
AlphaFold O60281

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