BMRB Entry 6361
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6361
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Title: Resonance Assignments for the SAP domain of the human protein DEK
Deposition date: 2004-10-19 Original release date: 2005-02-10
Authors: Devany, Matthew; Kotharu, N.; Matsuo, Hiroshi
Citation: Devany, Matthew; Matsuo, Hiroshi. "Letter to the Editor: NMR resonance assignments for the DNA-supercoiling domain of the human protein DEK" J. Biomol. NMR 31, 65-65 (2005).
Assembly members:
DEK, polymer, 109 residues, 12688 Da.
Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
DEK: FTIAQGKGQKLCEIERIHFF
LSKKKTDELRNLHKLLYNRP
GTVSSLKKNVGQFSGFPFEK
GSVQYKKKEEMLKKFRNAML
KSICEVLDLERSGVNSELVK
RILNFLMHP
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 707 |
| 13C chemical shifts | 447 |
| 15N chemical shifts | 112 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DEK78-186 | 1 |
Entities:
Entity 1, DEK78-186 109 residues - 12688 Da.
| 1 | PHE | THR | ILE | ALA | GLN | GLY | LYS | GLY | GLN | LYS | ||||
| 2 | LEU | CYS | GLU | ILE | GLU | ARG | ILE | HIS | PHE | PHE | ||||
| 3 | LEU | SER | LYS | LYS | LYS | THR | ASP | GLU | LEU | ARG | ||||
| 4 | ASN | LEU | HIS | LYS | LEU | LEU | TYR | ASN | ARG | PRO | ||||
| 5 | GLY | THR | VAL | SER | SER | LEU | LYS | LYS | ASN | VAL | ||||
| 6 | GLY | GLN | PHE | SER | GLY | PHE | PRO | PHE | GLU | LYS | ||||
| 7 | GLY | SER | VAL | GLN | TYR | LYS | LYS | LYS | GLU | GLU | ||||
| 8 | MET | LEU | LYS | LYS | PHE | ARG | ASN | ALA | MET | LEU | ||||
| 9 | LYS | SER | ILE | CYS | GLU | VAL | LEU | ASP | LEU | GLU | ||||
| 10 | ARG | SER | GLY | VAL | ASN | SER | GLU | LEU | VAL | LYS | ||||
| 11 | ARG | ILE | LEU | ASN | PHE | LEU | MET | HIS | PRO |
Samples:
sample_1: DEK, [U-13C; U-15N], 0.7 mM; Na2HPO4 25 mM; NaH2PO4 25 mM; KCl 100 mM; DTT 20 mM; pefabloc 0.4 mM; NaN3 0.02%; DTT 20 mM
cond-1: pH: 6.8; temperature: 298 K; ionic strength: 0.15 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H-15N NOESY | not available | not available | not available |
| 1H-15N TOCSY | not available | not available | not available |
| HNCA | not available | not available | not available |
| HNCO | not available | not available | not available |
| CBCANH | not available | not available | not available |
| CBCACONH | not available | not available | not available |
| HCCHTOCSY | not available | not available | not available |
| 1H-13C NOESYHSQC | not available | not available | not available |
| 1H-15N NOESYHSQC | not available | not available | not available |
Software:
No software information available
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAB25100 BAG35503 BAG60099 BAG60375 BAG72522 |
| EMBL | CAA45536 |
| GB | AAH35259 AAH79344 AAI42199 ABZ92195 ADP20523 |
| REF | NP_001004255 NP_001093187 NP_001128181 NP_001244457 NP_001266767 |
| SP | P35659 Q6AXS3 |
| TPG | DAA16149 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts