BMRB Entry 4732
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4732
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Citation: Cerdan, Rachel; Payet, Dominique; Yang, Ji-Chun; Travers, Andrew; Neuhaus, David. "HMG-D complexed to a bulge DNA: an NMR study" Protein Sci. ., .-. (2000).
Assembly members:
High Mobility Protein of Drosophila, polymer, 112 residues, Formula weight is not available
Natural source: Common Name: fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
High Mobility Protein of Drosophila: MSDKPKRPLSAYMLWLNSAR
ESIKRENPGIKVTEVAKRGG
ELWRAMKDKSEWEAKAAKAK
DDYDRAVKEFEANGGSSAAN
GGGAKKRAKPAKKVAKKSKK
EESDEDDDDESE
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 453 |
| 13C chemical shifts | 149 |
| 15N chemical shifts | 89 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HMG-D protein free | 1 |
Entities:
Entity 1, HMG-D protein free 112 residues - Formula weight is not available
| 1 | MET | SER | ASP | LYS | PRO | LYS | ARG | PRO | LEU | SER | ||||
| 2 | ALA | TYR | MET | LEU | TRP | LEU | ASN | SER | ALA | ARG | ||||
| 3 | GLU | SER | ILE | LYS | ARG | GLU | ASN | PRO | GLY | ILE | ||||
| 4 | LYS | VAL | THR | GLU | VAL | ALA | LYS | ARG | GLY | GLY | ||||
| 5 | GLU | LEU | TRP | ARG | ALA | MET | LYS | ASP | LYS | SER | ||||
| 6 | GLU | TRP | GLU | ALA | LYS | ALA | ALA | LYS | ALA | LYS | ||||
| 7 | ASP | ASP | TYR | ASP | ARG | ALA | VAL | LYS | GLU | PHE | ||||
| 8 | GLU | ALA | ASN | GLY | GLY | SER | SER | ALA | ALA | ASN | ||||
| 9 | GLY | GLY | GLY | ALA | LYS | LYS | ARG | ALA | LYS | PRO | ||||
| 10 | ALA | LYS | LYS | VAL | ALA | LYS | LYS | SER | LYS | LYS | ||||
| 11 | GLU | GLU | SER | ASP | GLU | ASP | ASP | ASP | ASP | GLU | ||||
| 12 | SER | GLU |
Samples:
sample_1: High Mobility Protein of Drosophila, [U-95% 15N; U-95% 13C], 0.8 – 1 mM
cond_1: pH: 6.0; temperature: 303 K; ionic strength: 0.005 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | not available | not available | not available |
| 2D 1H-15N HSQC | not available | not available | not available |
| 3D HNCA | not available | not available | not available |
| 3D CBCA(CO)NH | not available | not available | not available |
Software:
Xwin-NMR -
Felix -
NMR spectrometers:
- Bruker DMX 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks