BMRB Entry 19486
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19486
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Title: Solution NMR Structure of Zinc finger protein 423 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR7298F
Deposition date: 2013-09-10 Original release date: 2013-09-23
Authors: Pederson, Kari; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Everett, John; Acton, Thomas; Montelione, Gaetano; Prestegard, James
Citation: Pederson, Kari; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Everett, John; Acton, Thomas; Montelione, Gaetano; Prestegard, James. "Solution NMR Structure of Zinc finger protein 423 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR7298F" To be published ., .-..
Assembly members:
HR7298F, polymer, 55 residues, 6432.094 Da.
ZINC ION, 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):
HR7298F: MGSHKCNVCSRTFFSENGLR
EHLQTHRGPAKHYMCPICGE
RFPSLLTLTEHKVTH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 212 |
| 15N chemical shifts | 51 |
| 1H chemical shifts | 335 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR7298F | 1 |
| 2 | Zn ion 1 | 2 |
| 3 | Zn ion 2 | 2 |
Entities:
Entity 1, HR7298F 55 residues - 6432.094 Da.
M at N-terminal is part of His-Tag.
| 1 | MET | GLY | SER | HIS | LYS | CYS | ASN | VAL | CYS | SER | ||||
| 2 | ARG | THR | PHE | PHE | SER | GLU | ASN | GLY | LEU | ARG | ||||
| 3 | GLU | HIS | LEU | GLN | THR | HIS | ARG | GLY | PRO | ALA | ||||
| 4 | LYS | HIS | TYR | MET | CYS | PRO | ILE | CYS | GLY | GLU | ||||
| 5 | ARG | PHE | PRO | SER | LEU | LEU | THR | LEU | THR | GLU | ||||
| 6 | HIS | LYS | VAL | THR | HIS |
Entity 2, Zn ion 1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
NC: HR7298F.005, [U-100% 13C; U-100% 15N], 0.17 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O, [U-100% 2H], 10%; DSS 50 uM; ZnSO4 50 uM; H2O 90%
C12E5_NC5: HR7298F.0059, [U-5% 13C; U-100% 15N], 0.51 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O, [U-100% 2H], 5%; DSS 50 uM; C12E5 PEG/Hexanol 4.2%; ZnSO4 50 uM; H2O 95%
NC5: HR7298F.009, [U-5% 13C; U-100% 15N], 0.51 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O, [U-100% 2H], 5%; DSS 50 uM; ZnSO4 50 uM; H2O 95%
C12E5_NC: HR7298F.005, [U-100% 13C; U-100% 15N], 0.17 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O, [U-100% 2H], 10%; DSS 50 uM; ZnSO4 50 uM; C12E5 PEG?Hexanol 4.2%; H2O 90%
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HNCACB | NC | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | NC | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | NC5 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT HSQC | NC5 | isotropic | sample_conditions_1 |
| 2D 1H-15N J-modulation HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-15N J-modulation HSQC | C12E5_NC5 | anisotropic | sample_conditions_1 |
| 2D 1H-15N CO filtered TROSY | NC | isotropic | sample_conditions_1 |
| 2D 1H-15N CO-filtered TROSY | C12E5_NC | anisotropic | sample_conditions_1 |
Software:
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMRJ, Varian - collection
SPARKY v3.113, Goddard - chemical shift assignment
PALES, PALES (Zweckstetter, Bax) - structure validation
PSVS v1.5, Bhattacharya, Montelione - structure validation
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian Avance 900 MHz
- Varian Avance 600 MHz
Related Database Links:
| EMBL | ZN423_HUMAN |
| PDB | |
| DBJ | BAA34480 BAC65647 BAE21688 BAG51329 BAG72439 |
| GB | AAB58646 AAF28354 AAG17053 AAH59234 AAI12316 |
| REF | NP_001095363 NP_001258549 NP_001297449 NP_055884 NP_201584 |
| SP | O08961 Q2M1K9 Q80TS5 |
| TPG | DAA20039 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts