BMRB Entry 34180
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34180
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
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Title: Solution structure of the LEDGF/p75 IBD - POGZ (aa 1370-1404) complex PubMed: 29997176
Deposition date: 2017-10-03 Original release date: 2018-07-20
Authors: Veverka, V.
Citation: Sharma, S.; Cermakova, K.; De Rijck, J.; Demeulemeester, J.; Fabry, M.; El Ashkar, S.; Van Belle, S.; Lepsik, M.; Tesina, P.; Duchoslav, V.; Novak, P.; Hubalek, M.; Srb, P.; Christ, F.; Rezacova, P.; Hodges, H.; Debyser, Z.; Veverka, V.. "Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase-dependent phosphorylation." Proc. Natl. Acad. Sci. U.S.A. 115, E7053-E7062 (2018).
Assembly members:
entity_1, polymer, 139 residues, 16036.094 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: SNAASWETSMDSRLQRIHAE
IKNSLKIDNLDVNRCIEALD
ELASLQVTMQQAQKHTEMIT
TLKKIRRFKVSQVIMEKSTM
LYNKFKNMFLVGEGDSVITQ
VLNKRPRSSPEETIEPESLH
QLFEGESETESFYGFEEAD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 584 |
| 15N chemical shifts | 133 |
| 1H chemical shifts | 956 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 139 residues - 16036.094 Da.
| 1 | SER | ASN | ALA | ALA | SER | TRP | GLU | THR | SER | MET | ||||
| 2 | ASP | SER | ARG | LEU | GLN | ARG | ILE | HIS | ALA | GLU | ||||
| 3 | ILE | LYS | ASN | SER | LEU | LYS | ILE | ASP | ASN | LEU | ||||
| 4 | ASP | VAL | ASN | ARG | CYS | ILE | GLU | ALA | LEU | ASP | ||||
| 5 | GLU | LEU | ALA | SER | LEU | GLN | VAL | THR | MET | GLN | ||||
| 6 | GLN | ALA | GLN | LYS | HIS | THR | GLU | MET | ILE | THR | ||||
| 7 | THR | LEU | LYS | LYS | ILE | ARG | ARG | PHE | LYS | VAL | ||||
| 8 | SER | GLN | VAL | ILE | MET | GLU | LYS | SER | THR | MET | ||||
| 9 | LEU | TYR | ASN | LYS | PHE | LYS | ASN | MET | PHE | LEU | ||||
| 10 | VAL | GLY | GLU | GLY | ASP | SER | VAL | ILE | THR | GLN | ||||
| 11 | VAL | LEU | ASN | LYS | ARG | PRO | ARG | SER | SER | PRO | ||||
| 12 | GLU | GLU | THR | ILE | GLU | PRO | GLU | SER | LEU | HIS | ||||
| 13 | GLN | LEU | PHE | GLU | GLY | GLU | SER | GLU | THR | GLU | ||||
| 14 | SER | PHE | TYR | GLY | PHE | GLU | GLU | ALA | ASP |
Samples:
sample_1: LEDGF/p75 IBD-POGZ, [U-13C; U-15N], 0.5 mM; TRIS 50 mM; sodium chloride 150 mM
sample_conditions_1: ionic strength: 200 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
SPARKY, Goddard - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
YASARA, Krieger - refinement
NMR spectrometers:
- Bruker AvanceIII 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts