BMRB Entry 30102
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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/BMR30102
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Trempe, J.; Saskova, K.; Siva, M.; Ratcliffe, C.; Veverka, V.; Hoegl, A.; Menade, M.; Feng, X.; Shenker, S.; Svoboda, M.; Kozisek, M.; Konvalinka, J.; Gehring, K.. "Structural studies of the yeast DNA damage-inducible protein Ddi1 reveal domain architecture of this eukaryotic protein family." Sci. Rep. 6, 33671-33671 (2016).
PubMed: 27646017
Assembly members:
entity_1, polymer, 116 residues, 13309.941 Da.
Natural source: Common Name: Baker's yeast Taxonomy ID: 559292 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli K-12 Vector: pGEX-6P1
Entity Sequences (FASTA):
entity_1: GPLGSATLSDEAFIEQFRQE
LLNNQMLRSQLILQIPGLND
LVNDPLLFRERLGPLILQRR
YGGYNTAMNPFGIPQDEYTR
LMANPDDPDNKKRIAELLDQ
QAIDEQLRNAIEYTPE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 507 |
| 15N chemical shifts | 126 |
| 1H chemical shifts | 857 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 116 residues - 13309.941 Da.
| 1 | GLY | PRO | LEU | GLY | SER | ALA | THR | LEU | SER | ASP | ||||
| 2 | GLU | ALA | PHE | ILE | GLU | GLN | PHE | ARG | GLN | GLU | ||||
| 3 | LEU | LEU | ASN | ASN | GLN | MET | LEU | ARG | SER | GLN | ||||
| 4 | LEU | ILE | LEU | GLN | ILE | PRO | GLY | LEU | ASN | ASP | ||||
| 5 | LEU | VAL | ASN | ASP | PRO | LEU | LEU | PHE | ARG | GLU | ||||
| 6 | ARG | LEU | GLY | PRO | LEU | ILE | LEU | GLN | ARG | ARG | ||||
| 7 | TYR | GLY | GLY | TYR | ASN | THR | ALA | MET | ASN | PRO | ||||
| 8 | PHE | GLY | ILE | PRO | GLN | ASP | GLU | TYR | THR | ARG | ||||
| 9 | LEU | MET | ALA | ASN | PRO | ASP | ASP | PRO | ASP | ASN | ||||
| 10 | LYS | LYS | ARG | ILE | ALA | GLU | LEU | LEU | ASP | GLN | ||||
| 11 | GLN | ALA | ILE | ASP | GLU | GLN | LEU | ARG | ASN | ALA | ||||
| 12 | ILE | GLU | TYR | THR | PRO | GLU |
Samples:
sample_1: Ddi1 86-196-1, [U-13C; U-15N], 0.5 ± 0.1 mM
sample_2: Ddi1 86-196-2, [U-15N], 0.5 ± 0.1 mM
sample_conditions_1: ionic strength: 110 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K
sample_conditions_2: ionic strength: 110 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N het NOE | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC-IPAP | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC-IPAP | sample_2 | anisotropic | sample_conditions_2 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N/1H NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C/1H HSQC-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment
MODULE, M. Blackledge - data analysis
SPARKY, Goddard - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - data analysis
XPLOR-NIH v2.40, C.D. Schwieters, J.J. Kuszewski, N. Tjandra, and G.M. Clore - refinement, structure calculation
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks