BMRB Entry 34475
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34475
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Title: LEDGF/p75 dimer (residues 345-467)
Deposition date: 2020-01-10 Original release date: 2020-09-07
Authors: Lux, V.; Veverka, V.
Citation: Lux, V.; Veverka, V.. "Structural basis of the LEDGF/p75 dimerization" . ., .-..
Assembly members:
entity_1, polymer, 128 residues, 14644.854 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):
entity_1: SNAASETSMDSRLQRIHAEI
KNSLKIDNLDVNRCIEALDE
LASLQVTMQQAQKHTEMITT
LKKIRRFKVSQVIMEKSTML
YNKFKNMFLVGEGDSVITQV
LNKSLAEQRQHEEANKTKDQ
GKKGPNKK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 549 |
| 15N chemical shifts | 130 |
| 1H chemical shifts | 882 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
| 2 | unit_2 | 1 |
Entities:
Entity 1, unit_1 128 residues - 14644.854 Da.
| 1 | SER | ASN | ALA | ALA | SER | GLU | THR | SER | MET | ASP | ||||
| 2 | SER | ARG | LEU | GLN | ARG | ILE | HIS | ALA | GLU | ILE | ||||
| 3 | LYS | ASN | SER | LEU | LYS | ILE | ASP | ASN | LEU | ASP | ||||
| 4 | VAL | ASN | ARG | CYS | ILE | GLU | ALA | LEU | ASP | GLU | ||||
| 5 | LEU | ALA | SER | LEU | GLN | VAL | THR | MET | GLN | GLN | ||||
| 6 | ALA | GLN | LYS | HIS | THR | GLU | MET | ILE | THR | THR | ||||
| 7 | LEU | LYS | LYS | ILE | ARG | ARG | PHE | LYS | VAL | SER | ||||
| 8 | GLN | VAL | ILE | MET | GLU | LYS | SER | THR | MET | LEU | ||||
| 9 | TYR | ASN | LYS | PHE | LYS | ASN | MET | PHE | LEU | VAL | ||||
| 10 | GLY | GLU | GLY | ASP | SER | VAL | ILE | THR | GLN | VAL | ||||
| 11 | LEU | ASN | LYS | SER | LEU | ALA | GLU | GLN | ARG | GLN | ||||
| 12 | HIS | GLU | GLU | ALA | ASN | LYS | THR | LYS | ASP | GLN | ||||
| 13 | GLY | LYS | LYS | GLY | PRO | ASN | LYS | LYS |
Samples:
sample_1: LEDGF, [U-13C; U-15N], 0.5 mM; HEPES 20 mM; sodium chloride 100 mM; TCEP 1 mM
sample_conditions_1: ionic strength: 120 mM; pH: 7; 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | 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:
CYANA, Guntert, Mumenthaler and Wuthrich - refinement
Sparky, Goddard - data analysis
TopSpin, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker AVANCE 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts