BMRB Entry 10121
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10121
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Title: Solution structure of a putative peptidyl-tRNA hydrolase domain in a mouse hypothetical protein
Deposition date: 2007-04-02 Original release date: 2008-09-02
Authors: Nameki, N.; Kigawa, T.; Koshiba, S.; Kobayashi, N.; Tochio, N.; Inoue, M.; Yokoyama, S.
Citation: Nameki, N.; Kigawa, T.; Koshiba, S.; Kobayashi, N.; Tochio, N.; Inoue, M.; Yokoyama, S.. "Solution structure of a peptidyl-tRNA hydrolase domain of a hypothetical protein" Not known ., .-..
Assembly members:
peptidyl-tRNA hydrolase domain, polymer, 112 residues, Formula weight is not available
Natural source: Common Name: mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: cell free synthesis
Entity Sequences (FASTA):
peptidyl-tRNA hydrolase domain: GSSGSSGEHAKQASSYIPLD
RLSISYCRSSGPGGQNVNKV
NSKAEVRFHLASADWIEEPV
RQKIALTHKNKINKAGELVL
TSESSRYQFRNLAECLQKIR
DMIAEASGPSSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 455 |
| 15N chemical shifts | 117 |
| 1H chemical shifts | 740 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | immature colon carcinoma transcript 1 | 1 |
Entities:
Entity 1, immature colon carcinoma transcript 1 112 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | GLU | HIS | ALA | ||||
| 2 | LYS | GLN | ALA | SER | SER | TYR | ILE | PRO | LEU | ASP | ||||
| 3 | ARG | LEU | SER | ILE | SER | TYR | CYS | ARG | SER | SER | ||||
| 4 | GLY | PRO | GLY | GLY | GLN | ASN | VAL | ASN | LYS | VAL | ||||
| 5 | ASN | SER | LYS | ALA | GLU | VAL | ARG | PHE | HIS | LEU | ||||
| 6 | ALA | SER | ALA | ASP | TRP | ILE | GLU | GLU | PRO | VAL | ||||
| 7 | ARG | GLN | LYS | ILE | ALA | LEU | THR | HIS | LYS | ASN | ||||
| 8 | LYS | ILE | ASN | LYS | ALA | GLY | GLU | LEU | VAL | LEU | ||||
| 9 | THR | SER | GLU | SER | SER | ARG | TYR | GLN | PHE | ARG | ||||
| 10 | ASN | LEU | ALA | GLU | CYS | LEU | GLN | LYS | ILE | ARG | ||||
| 11 | ASP | MET | ILE | ALA | GLU | ALA | SER | GLY | PRO | SER | ||||
| 12 | SER | GLY |
Samples:
sample_1: peptidyl-tRNA hydrolase domain, [U-13C; U-15N], 1.7 mM; phosphate 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
| 3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
Software:
xwinnmr v2.6, Bruker - collection
NMRPipe v20020425, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.704, Kobayashi, N. - data analysis
CYANA v1.0.7, Guntert, P. - structure solution
OPALp, Guntert, P. - refinement
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAB22632 BAB22691 BAE35961 |
| GB | AAH28523 EDL34481 EDL34486 |
| REF | NP_081005 XP_006534127 XP_006997809 |
| SP | Q8R035 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts