BMRB Entry 25639
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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/BMR25639
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Title: Solution structure of LEDGF/p75 IBD in complex with POGZ peptide (1389-1404) PubMed: 26245978
Deposition date: 2015-05-26 Original release date: 2015-08-17
Authors: Tesina, Petr; Cermakova, Katerina; Horejsi, Magdalena; Prochazkova, Katerina; Fabry, Milan; Sharma, Subhalakshmi; Christ, Frauke; Demeulemeester, Jonas; Debyser, Zeger; De Rijck, Jan; Veverka, Vaclav; Rezacova, Pavlina
Citation: Tesina, P.; Cermakova, K.; Horejsi, M.; Prochazkova, K.; Fabry, M.; Sharma, S.; Christ, F.; Demeulemeester, J.; Debyser, Z.; Rijck, J.D.; Veverka, V.; Rezacova, P.. "Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif" Nat. Commun. 6, 7968-7968 (2015).
Assembly members:
entity_1, polymer, 16 residues, 1825.766 Da.
entity_2, polymer, 79 residues, 9355.110 Da.
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: EGESETESFYGFEEAD
entity_2: MDSRLQRIHAEIKNSLKIDN
LDVNRCIEALDELASLQVTM
QQAQKHTEMITTLKKIRRFK
VSQVIMEKSTMLYNKFKNM
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 345 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 610 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 16 residues - 1825.766 Da.
| 1 | GLU | GLY | GLU | SER | GLU | THR | GLU | SER | PHE | TYR | ||||
| 2 | GLY | PHE | GLU | GLU | ALA | ASP |
Entity 2, entity_2 79 residues - 9355.110 Da.
| 1 | MET | ASP | SER | ARG | LEU | GLN | ARG | ILE | HIS | ALA | ||||
| 2 | GLU | ILE | LYS | ASN | SER | LEU | LYS | ILE | ASP | ASN | ||||
| 3 | LEU | ASP | VAL | ASN | ARG | CYS | ILE | GLU | ALA | LEU | ||||
| 4 | ASP | GLU | LEU | ALA | SER | LEU | GLN | VAL | THR | MET | ||||
| 5 | GLN | GLN | ALA | GLN | LYS | HIS | THR | GLU | MET | ILE | ||||
| 6 | THR | THR | LEU | LYS | LYS | ILE | ARG | ARG | PHE | LYS | ||||
| 7 | VAL | SER | GLN | VAL | ILE | MET | GLU | LYS | SER | THR | ||||
| 8 | MET | LEU | TYR | ASN | LYS | PHE | LYS | ASN | MET |
Samples:
sample_1: entity_1 0.5 mM; entity_2, [U-13C; U-15N], 0.5 mM; HEPES 25 mM; NaCl 100 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 125 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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:
TOPSPIN, Bruker Biospin - collection
SPARKY, Goddard - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
YASARA, YASARA - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA32306 BAC27169 BAC29003 BAC65570 BAE36623 |
| EMBL | CAD97850 CAL37797 |
| GB | AAH32176 AAH85188 AAH96492 AAI39433 AAI39434 |
| REF | NP_001101163 NP_001156662 NP_001159420 NP_001162545 NP_001181866 |
| SP | Q7Z3K3 Q8BZH4 |
| TPG | DAA31680 |
Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone
or all simulated shifts