BMRB Entry 15533
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15533
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Stoll, Raphael; Lee, Brian; Debler, Erik; Laity, John; Wilson, Ian; Dyson, Helen; Wright, Peter. "Structure of the Wilms Tumor Suppressor Protein Zinc Finger Domain Bound to DNA" J. Mol. Biol. 372, 1227-1245 (2007).
PubMed: 17716689
Assembly members:
wt1-zf14, polymer, 119 residues, 14494.849 Da.
ZN, non-polymer, 65.409 Da.
wt1-14mer_1, polymer, 14 residues, Formula weight is not available
wt1-14mer_2, polymer, 14 residues, Formula weight is not available
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 Vector: pET21d
Entity Sequences (FASTA):
wt1-zf14: ASEKRPFMCAYPGCNKRYFK
LSHLQMHSRKHTGEKPYQCD
FKDCERRFSRSDQLKRHQRR
HTGVKPFQCKTCQRKFSRSD
HLKTHTRTHTGEKPFSCRWP
SCQKKFARSDELVRHHNMH
wt1-14mer_1: CGCGGGGGCGTCTG
wt1-14mer_2: CAGACGCCCCCGCG
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 115 |
| 1H chemical shifts | 121 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | wt1-zf14 | 1 |
| 2 | zinc1 | 2 |
| 3 | zinc2 | 2 |
| 4 | zinc3 | 2 |
| 5 | zinc4 | 2 |
| 6 | strand1 | 3 |
| 7 | strand2 | 4 |
Entities:
Entity 1, wt1-zf14 119 residues - 14494.849 Da.
| 1 | ALA | SER | GLU | LYS | ARG | PRO | PHE | MET | CYS | ALA | ||||
| 2 | TYR | PRO | GLY | CYS | ASN | LYS | ARG | TYR | PHE | LYS | ||||
| 3 | LEU | SER | HIS | LEU | GLN | MET | HIS | SER | ARG | LYS | ||||
| 4 | HIS | THR | GLY | GLU | LYS | PRO | TYR | GLN | CYS | ASP | ||||
| 5 | PHE | LYS | ASP | CYS | GLU | ARG | ARG | PHE | SER | ARG | ||||
| 6 | SER | ASP | GLN | LEU | LYS | ARG | HIS | GLN | ARG | ARG | ||||
| 7 | HIS | THR | GLY | VAL | LYS | PRO | PHE | GLN | CYS | LYS | ||||
| 8 | THR | CYS | GLN | ARG | LYS | PHE | SER | ARG | SER | ASP | ||||
| 9 | HIS | LEU | LYS | THR | HIS | THR | ARG | THR | HIS | THR | ||||
| 10 | GLY | GLU | LYS | PRO | PHE | SER | CYS | ARG | TRP | PRO | ||||
| 11 | SER | CYS | GLN | LYS | LYS | PHE | ALA | ARG | SER | ASP | ||||
| 12 | GLU | LEU | VAL | ARG | HIS | HIS | ASN | MET | HIS |
Entity 2, zinc1 - Zn - 65.409 Da.
| 1 | ZN |
Entity 3, strand1 14 residues - Formula weight is not available
| 1 | DC | DG | DC | DG | DG | DG | DG | DG | DC | DG | ||||
| 2 | DT | DC | DT | DG |
Entity 4, strand2 14 residues - Formula weight is not available
| 1 | DC | DA | DG | DA | DC | DG | DC | DC | DC | DC | ||||
| 2 | DC | DG | DC | DG |
Samples:
sample_1: wt1-14mer, [U-100% 13C; U-100% 15N], 0.6 mM; Tris/HCl 10 mM; KCl 20 mM; ZnSO4 5 uM; NaN3 2 mM
sample_conditions_1: ionic strength: 20 mM; pH: 6.7; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| IPAP | sample_1 | anisotropic | sample_conditions_1 |
Software:
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - structure solution
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 800 MHz
- Bruker Avance 900 MHz
Related Database Links:
| BMRB | 15532 4707 4708 4709 4710 |
| PDB | |
| DBJ | BAA11522 BAA28147 BAA94793 BAF84425 |
| EMBL | CAA35956 CAA43819 CDG23662 |
| GB | AAA36810 AAA61299 AAB33443 AAB53152 AAH32861 |
| PRF | 1604420A |
| REF | NP_000369 NP_001001264 NP_001079057 NP_001079336 NP_001135625 |
| SP | B5DE03 O62651 P19544 P79958 |
| TPG | DAA21902 |
| AlphaFold | B5DE03 O62651 P19544 P79958 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks