BMRB Entry 11368
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11368
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Takahashi, M.; Kuwasako, K.; Tsuda, K.; Tanabe, W.; Harada, T.; Watanabe, S.; Tochio, N.; Muto, Y.; Kigawa, T.; Yokoyama, S.. "Solution structure of the C2H2 type zinc finger (region 656-688) of human Zinc
finger protein 95 homolog" .
Assembly members:
ZF-C2H2, 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 Host organism: E. coli - cell free Vector: P061225-40
Entity Sequences (FASTA):
ZF-C2H2: GSSGSSGSREKSHQCRECGE
IFFQYVSLIEHQVLHMGQKN
SGPSSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 170 |
| 15N chemical shifts | 38 |
| 1H chemical shifts | 245 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ZF-C2H2 | 1 |
| 2 | ZINC ION | 2 |
Entities:
Entity 1, ZF-C2H2 46 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | SER | ARG | GLU | ||||
| 2 | LYS | SER | HIS | GLN | CYS | ARG | GLU | CYS | GLY | GLU | ||||
| 3 | ILE | PHE | PHE | GLN | TYR | VAL | SER | LEU | ILE | GLU | ||||
| 4 | HIS | GLN | VAL | LEU | HIS | MET | GLY | GLN | LYS | ASN | ||||
| 5 | SER | GLY | PRO | SER | SER | GLY |
Entity 2, ZINC ION - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: ZF-C2H2, [U-13C; U-15N], 1.0 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
| 3D 15N-separated NOESY | sample_1 | isotropic | condition_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 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks