BMRB Entry 25801
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25801
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Title: UBL domain of the human DNA damage-inducible protein homolog 2 PubMed: 27461074
Deposition date: 2015-09-08 Original release date: 2016-07-13
Authors: Siva, Monika; Grantz Saskova, Klara; Veverka, Vaclav
Citation: Siva, Monika; Svoboda, Michal; Veverka, Vaclav; Trempe, Jean-Francois; Hofmann, Kay; Kozisek, Milan; Hexnerova, Rozalie; Sedlak, Frantisek; Belza, Jan; Brynda, Jiri; Sacha, Pavel; Hubalek, Martin; Starkova, Jana; Flaisigova, Iva; Konvalinka, Jan; Saskova, Klara Grantz. "Human DNA-Damage-Inducible 2 Protein Is Structurally and Functionally Distinct from Its Yeast Ortholog" Sci. Rep. 6, 30443-30443 (2016).
Assembly members:
entity, polymer, 97 residues, 11142.557 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: MGHHHHHHHHHHSSGHIEGR
HMLLTVYCVRRDLSEVTFSL
QVDADFELHNFRALCELESG
IPAAESQIVYAERPLTDNHR
SLASYGLKDGDVVILRQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 332 |
| 15N chemical shifts | 83 |
| 1H chemical shifts | 579 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 97 residues - 11142.557 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | HIS | HIS | SER | SER | GLY | HIS | ILE | GLU | GLY | ARG | ||||
| 3 | HIS | MET | LEU | LEU | THR | VAL | TYR | CYS | VAL | ARG | ||||
| 4 | ARG | ASP | LEU | SER | GLU | VAL | THR | PHE | SER | LEU | ||||
| 5 | GLN | VAL | ASP | ALA | ASP | PHE | GLU | LEU | HIS | ASN | ||||
| 6 | PHE | ARG | ALA | LEU | CYS | GLU | LEU | GLU | SER | GLY | ||||
| 7 | ILE | PRO | ALA | ALA | GLU | SER | GLN | ILE | VAL | TYR | ||||
| 8 | ALA | GLU | ARG | PRO | LEU | THR | ASP | ASN | HIS | ARG | ||||
| 9 | SER | LEU | ALA | SER | TYR | GLY | LEU | LYS | ASP | GLY | ||||
| 10 | ASP | VAL | VAL | ILE | LEU | ARG | GLN |
Samples:
sample_1: sodium phosphate 25 mM; sodium chloride 100 mM; entity, [U-13C; U-15N], 0.4 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; 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 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
YASARA, YASARA - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - refinement
NMR spectrometers:
- Bruker Avance 850 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts