BMRB Entry 17835
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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/BMR17835
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Title: NOT AVAILABLE PubMed: 22481467
Deposition date: 2011-08-06 Original release date: 2012-04-30
Authors: Cui, G.; Botuyan, M.V.; Mer, G.
Citation: Cui, Gaofeng; Botuyan, Maria Victoria; Mer, Georges. "(1)H, (15)N and (13)C resonance assignments for the three LOTUS RNA binding domains of Tudor domain-containing protein TDRD7." Biomol. NMR Assignments 7, 79-83 (2013).
Assembly members:
TDRD7, polymer, 78 residues, 8681.178 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
TDRD7: GHMLEADLVSKMLRAVLQSH
KNGIVLPRLQGEYRSLTGDW
IPFKQLGYPTLEAYLRSVPA
VVRIEASRSGEIVCYAVA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 357 |
15N chemical shifts | 84 |
1H chemical shifts | 577 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | TDRD7 | 1 |
Entities:
Entity 1, TDRD7 78 residues - 8681.178 Da.
1 | GLY | HIS | MET | LEU | GLU | ALA | ASP | LEU | VAL | SER | ||||
2 | LYS | MET | LEU | ARG | ALA | VAL | LEU | GLN | SER | HIS | ||||
3 | LYS | ASN | GLY | ILE | VAL | LEU | PRO | ARG | LEU | GLN | ||||
4 | GLY | GLU | TYR | ARG | SER | LEU | THR | GLY | ASP | TRP | ||||
5 | ILE | PRO | PHE | LYS | GLN | LEU | GLY | TYR | PRO | THR | ||||
6 | LEU | GLU | ALA | TYR | LEU | ARG | SER | VAL | PRO | ALA | ||||
7 | VAL | VAL | ARG | ILE | GLU | ALA | SER | ARG | SER | GLY | ||||
8 | GLU | ILE | VAL | CYS | TYR | ALA | VAL | ALA |
Samples:
sample_1: TDRD7, [U-100% 15N], 1.5 mM; sodium acetate 50 mM; H2O 90%; D2O 10%
sample_2: TDRD7, [U-100% 13C; U-100% 15N], 1.5 mM; sodium acetate 50 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0 mM; pH: 4.3; 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-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D CCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
SANE, Duggan, Legge, Dyson & Wright - chemical shift assignment
NMRView, Johnson, One Moon Scientific - processing
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
PDB | |
DBJ | BAA82968 BAE36321 |
GB | AAH29689 AAH90066 EDL02384 EDL98827 |
REF | NP_001277404 NP_620226 NP_666254 XP_004581240 XP_006238169 |
SP | Q8K1H1 Q9R1R4 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts