BMRB Entry 18490
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18490
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Title: TDRD3 complex PubMed: 23066109
Deposition date: 2012-05-30 Original release date: 2012-11-02
Authors: Sikorsky, Tomas
Citation: Sikorsky, Tomas; Hobor, Fruzsina; Krizanova, Eva; Pasulka, Josef; Kubicek, Karel; Stefl, Richard. "Recognition of asymmetrically dimethylated arginine by TDRD3." Nucleic Acids Res. 40, 11748-11755 (2012).
Assembly members:
entity_1, polymer, 58 residues, 6827.864 Da.
TDRD3_2, polymer, 13 residues, 1494.620 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_1: MKMWKPGDECFALYWEDNKF
YRAEVEALHSSGMTAVVKFI
DYGNYEEVLLSNIKPILE
TDRD3_2: YSPSSPXYTPQSP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 176 |
| 15N chemical shifts | 53 |
| 1H chemical shifts | 346 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TDRD3, chain 1 | 1 |
| 2 | TDRD3, chain 2 | 2 |
Entities:
Entity 1, TDRD3, chain 1 58 residues - 6827.864 Da.
| 1 | MET | LYS | MET | TRP | LYS | PRO | GLY | ASP | GLU | CYS | ||||
| 2 | PHE | ALA | LEU | TYR | TRP | GLU | ASP | ASN | LYS | PHE | ||||
| 3 | TYR | ARG | ALA | GLU | VAL | GLU | ALA | LEU | HIS | SER | ||||
| 4 | SER | GLY | MET | THR | ALA | VAL | VAL | LYS | PHE | ILE | ||||
| 5 | ASP | TYR | GLY | ASN | TYR | GLU | GLU | VAL | LEU | LEU | ||||
| 6 | SER | ASN | ILE | LYS | PRO | ILE | LEU | GLU |
Entity 2, TDRD3, chain 2 13 residues - 1494.620 Da.
| 1 | TYR | SER | PRO | SER | SER | PRO | DA2 | TYR | THR | PRO | ||||
| 2 | GLN | SER | PRO |
Samples:
sample_1: TDRD3_1, [U-99% 13C; U-99% 15N], 1.7 mM; sodium phosphate 50 mM; beta-mercaptoethanol 10 mM; sodium chloride 150 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 150 mM; pH: 8; pressure: 1 atm; temperature: 293.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | 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 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAB14950 BAJ17879 BAK63800 |
| EMBL | CAD97894 CAL37786 |
| GB | AAH30514 AAH60876 ACC94142 AIC52422 EAW52079 |
| REF | NP_001139542 NP_001139543 NP_110421 XP_003257452 XP_003257453 |
| SP | Q9H7E2 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts