BMRB Entry 30097
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30097
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: HDD domain from human Ddi2
Deposition date: 2016-05-23 Original release date: 2016-08-08
Authors: Veverka, V.
Citation: Veverka, V.. "HDD domain from human Ddi2" . ., .-..
Assembly members:
Protein DDI1 homolog 2, polymer, 98 residues, 11130.358 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):
Protein DDI1 homolog 2: SQQSHSSPGEITSSPQGLDN
PALLRDMLLANPHELSLLKE
RNPPLAEALLSGDLEKFSRV
LVEQQQDRARREQERIRLFS
ADPFDLEAQAKIEEDIRQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 405 |
| 15N chemical shifts | 103 |
| 1H chemical shifts | 682 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 98 residues - 11130.358 Da.
| 1 | SER | GLN | GLN | SER | HIS | SER | SER | PRO | GLY | GLU | ||||
| 2 | ILE | THR | SER | SER | PRO | GLN | GLY | LEU | ASP | ASN | ||||
| 3 | PRO | ALA | LEU | LEU | ARG | ASP | MET | LEU | LEU | ALA | ||||
| 4 | ASN | PRO | HIS | GLU | LEU | SER | LEU | LEU | LYS | GLU | ||||
| 5 | ARG | ASN | PRO | PRO | LEU | ALA | GLU | ALA | LEU | LEU | ||||
| 6 | SER | GLY | ASP | LEU | GLU | LYS | PHE | SER | ARG | VAL | ||||
| 7 | LEU | VAL | GLU | GLN | GLN | GLN | ASP | ARG | ALA | ARG | ||||
| 8 | ARG | GLU | GLN | GLU | ARG | ILE | ARG | LEU | PHE | SER | ||||
| 9 | ALA | ASP | PRO | PHE | ASP | LEU | GLU | ALA | GLN | ALA | ||||
| 10 | LYS | ILE | GLU | GLU | ASP | ILE | ARG | GLN |
Samples:
sample_1: hdd, [U-13C; U-15N], 280 uM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 200 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | 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 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
SPARKY, Goddard - chemical shift assignment
TOPSPIN, Bruker Biospin - collection, processing
YASARA, Hoegenauer, Koraimann, Kungl, Vriend - refinement
NMR spectrometers:
- Bruker AvanceIII 850 MHz
- Bruker AvanceIII 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts