BMRB Entry 15208
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                PDB ID: 
                
                
                Entry in NMR Restraints Grid
                Validation report in NRG-CING
            Chem Shift validation:  AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15208
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Title: Embryonic Neural Inducing Factor Churchill is not a DNA-Binding Zinc Finger Protein: Solution Structure Reveals a Solvent-Exposed Beta-Sheet and Zinc Binuclear Cluster PubMed: 17610897
Deposition date: 2007-04-07 Original release date: 2008-05-06
Authors: Lee, Brian; Buck-Koehntop, Bethany; Martinez-Yamout, Maria; Gottesfeld, Joel; Dyson, H. Jane; Wright, Peter
Citation: Lee, Brian; Buck-Koehntop, Bethany; Martinez-Yamout, Maria; Dyson, H. Jane; Wright, Peter. "Embryonic Neural Inducing Factor Churchill is not a DNA-Binding Zinc Finger Protein: Solution Structure Reveals a Solvent-Exposed Beta-Sheet and Zinc Binuclear Cluster" J. Mol. Biol. 371, 1274-1289 (2007).
Assembly members:
Churchill, polymer, 106 residues,   12166.857 Da.
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: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Churchill: CGDCVEKEYPNRGNTCLENG
SFLLNFTGCAVCSKRDFMLI
TNKSLKEEDGEEIVTYDHLC
KNCHHVIARHEYTFSIMDEF
QEYTMLCLLCGKAEDTISIL
PDDPRQ
- assigned_chemical_shifts
 
| Data type | Count | 
| 13C chemical shifts | 454 | 
| 15N chemical shifts | 113 | 
| 1H chemical shifts | 734 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | protein | 1 | 
| 2 | zinc ion, 1 | 2 | 
| 3 | zinc ion, 2 | 2 | 
| 4 | zinc ion, 3 | 2 | 
Entities:
Entity 1, protein 106 residues - 12166.857 Da.
| 1 | CYS | GLY | ASP | CYS | VAL | GLU | LYS | GLU | TYR | PRO | ||||
| 2 | ASN | ARG | GLY | ASN | THR | CYS | LEU | GLU | ASN | GLY | ||||
| 3 | SER | PHE | LEU | LEU | ASN | PHE | THR | GLY | CYS | ALA | ||||
| 4 | VAL | CYS | SER | LYS | ARG | ASP | PHE | MET | LEU | ILE | ||||
| 5 | THR | ASN | LYS | SER | LEU | LYS | GLU | GLU | ASP | GLY | ||||
| 6 | GLU | GLU | ILE | VAL | THR | TYR | ASP | HIS | LEU | CYS | ||||
| 7 | LYS | ASN | CYS | HIS | HIS | VAL | ILE | ALA | ARG | HIS | ||||
| 8 | GLU | TYR | THR | PHE | SER | ILE | MET | ASP | GLU | PHE | ||||
| 9 | GLN | GLU | TYR | THR | MET | LEU | CYS | LEU | LEU | CYS | ||||
| 10 | GLY | LYS | ALA | GLU | ASP | THR | ILE | SER | ILE | LEU | ||||
| 11 | PRO | ASP | ASP | PRO | ARG | GLN | 
Entity 2, zinc ion, 1 - Zn - 65.409 Da.
| 1 | ZN | 
Samples:
sample_1: Churchill, [U-13C; U-15N], 1 mM; Tris 25 mM; NaCl 100 mM; DTT 2 mM
sample_conditions_1: ionic strength: 40 mM; pH: 6.8; 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 HNCO | sample_1 | isotropic | sample_conditions_1 | 
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 | 
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 | 
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 | 
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 | 
| 3D (HCA)CO(CA)NH | sample_1 | isotropic | sample_conditions_1 | 
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 | 
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 | 
| 3D CBCGCD | sample_1 | isotropic | sample_conditions_1 | 
| 3D CBCGCE | sample_1 | isotropic | sample_conditions_1 | 
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 | 
| 3D HACAHB-COSY | sample_1 | isotropic | sample_conditions_1 | 
| 2D 1H-1H NOESY | 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 | 
Software:
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - peak picking, refinement
NMRView, Johnson, One Moon Scientific - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation
NMR spectrometers:
- Bruker DMX 500 MHz
 - Bruker DMX 600 MHz
 - Bruker DMX 800 MHz
 - Bruker DMX 900 MHz
 - Bruker DRX 750 MHz
 
Related Database Links:
| PDB | |
| DBJ | BAG51943 BAG59416 BAH12268 | 
| EMBL | CAH92555 | 
| GB | AAH20550 AAI68770 AIC61091 EAW80884 EAW80885 | 
| REF | NP_001100211 NP_001126496 NP_001189488 NP_001190992 NP_660148 | 
| SP | Q5R6Q5 Q8WUH1 | 
Download simulated HSQC data in one of the following formats:
            
CSV: Backbone
            or all simulated shifts
            
SPARKY: Backbone
            or all simulated shifts