BMRB Entry 18954
Click here to enlarge.
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/BMR18954
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: NMR structure of the GUCT domain from human DEAD box polypeptide 21
Deposition date: 2013-01-16 Original release date: 2013-01-28
Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the GUCT domain from human DEAD box polypeptide 21 (DDX21)" Not known ., .-..
Assembly members:
entity, polymer, 95 residues, 10640.232 Da.
Natural source: Common Name: Humans 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: GHISGATSVDQRSLINSNVG
FVTMILQCSIEMPNISYAWK
ELKEQLGEEIDSKVKGMVFL
KGKLGVCFDVPTASVTEIQE
KWHDSRRWQLSVATE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 307 |
| 15N chemical shifts | 101 |
| 1H chemical shifts | 658 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | GUCT | 1 |
Entities:
Entity 1, GUCT 95 residues - 10640.232 Da.
| 1 | GLY | HIS | ILE | SER | GLY | ALA | THR | SER | VAL | ASP | ||||
| 2 | GLN | ARG | SER | LEU | ILE | ASN | SER | ASN | VAL | GLY | ||||
| 3 | PHE | VAL | THR | MET | ILE | LEU | GLN | CYS | SER | ILE | ||||
| 4 | GLU | MET | PRO | ASN | ILE | SER | TYR | ALA | TRP | LYS | ||||
| 5 | GLU | LEU | LYS | GLU | GLN | LEU | GLY | GLU | GLU | ILE | ||||
| 6 | ASP | SER | LYS | VAL | LYS | GLY | MET | VAL | PHE | LEU | ||||
| 7 | LYS | GLY | LYS | LEU | GLY | VAL | CYS | PHE | ASP | VAL | ||||
| 8 | PRO | THR | ALA | SER | VAL | THR | GLU | ILE | GLN | GLU | ||||
| 9 | LYS | TRP | HIS | ASP | SER | ARG | ARG | TRP | GLN | LEU | ||||
| 10 | SER | VAL | ALA | THR | GLU |
Samples:
sample_1: GUCT, [U-99% 13C; U-99% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; D2O, [U-99% 2H], 95%; H2O 5%
sample_conditions_1: ionic strength: 0.798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY HACACONH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY CBCACONH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, G ntert P. - structure solution
TOPSPIN v3.1, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
j-UNIO, Herrmann, and Wuthrich - chemical shift assignment, peak picking, structure solution
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAB93481 BAG37957 BAI45572 |
| EMBL | CAH18395 |
| GB | AAB02546 AAF78930 AAH08071 ABM84557 ABM87851 |
| REF | NP_001243839 NP_004719 XP_001110939 XP_002820927 XP_003258243 |
| SP | Q9NR30 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts