BMRB Entry 16797
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16797
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Structure of the three-Cys2His2 domain of mouse testis zinc finger protein PubMed: 20544958
Deposition date: 2010-03-29 Original release date: 2010-07-27
Authors: Chou, Chun-Chi; Lou, Yuan-Chao; Chen, Chinpan
Citation: Chou, Chun-Chi; Lou, Yuan-Chao; Tang, Tang; Chen, Chinpan. "Structure and DNA binding characteristics of the three-Cys2His2 domain of mouse testis zinc finger protein." Proteins 78, 2202-2212 (2010).
Assembly members:
mTZD_finger2, polymer, 27 residues, 3120.5 Da.
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
mTZD_finger2: EKPFSCSLCPQRSRDFSAMT
KHLRTHG
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 106 |
15N chemical shifts | 26 |
1H chemical shifts | 175 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | mTZD finger2 | 1 |
2 | ZINC ION | 2 |
Entities:
Entity 1, mTZD finger2 27 residues - 3120.5 Da.
1 | GLU | LYS | PRO | PHE | SER | CYS | SER | LEU | CYS | PRO | ||||
2 | GLN | ARG | SER | ARG | ASP | PHE | SER | ALA | MET | THR | ||||
3 | LYS | HIS | LEU | ARG | THR | HIS | GLY |
Entity 2, ZINC ION - Zn - 65.409 Da.
1 | ZN |
Samples:
sample_1: mTZD finger2 mM; acetic acid, [U-99% 2H], 50 mM; sodium chloride 20 mM
sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.18, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMRView v5, Johnson, One Moon Scientific - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
PDB | |
DBJ | BAB30015 BAG73879 |
GB | AAD27708 AAD48448 AAF61244 AAI37688 AAK13198 |
REF | NP_001102987 NP_001129098 NP_001178153 NP_001303831 NP_001303832 |
SP | A1YGK1 A2T7E6 Q9JKD9 Q9Y2Y4 |
TPG | DAA19797 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts