BMRB Entry 17260
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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/BMR17260
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Title: Backbone and side-chain 1H, 13C and 15N assignments of the UCHL1 S18Y variant PubMed: 21298373
Deposition date: 2010-10-20 Original release date: 2011-02-10
Authors: Tse, Ho Sum; Sze, Kong Hung
Citation: Tse, Ho-Sum; Hu, Hong-Yu; Sze, Kong-Hung. "Backbone and side-chain 1H, 15N and 13C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1." Biomol. NMR Assignments 5, 165-168 (2011).
Assembly members:
UCHL1_S18Y_variant, polymer, 231 residues, Formula weight is not available
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):
UCHL1_S18Y_variant: MQLKPMEINPEMLNKVLYRL
GVAGQWRFVDVLGLEEESLG
SVPAPACALLLLFPLTAQHE
NFRKKQIEELKGQEVSPKVY
FMKQTIGNSCGTIGLIHAVA
NNQDKLGFEDGSVLKQFLSE
TEKMSPEDRAKCFEKNEAIQ
AAHDAVAQEGQCRVDDKVNF
HFILFNNVDGHLYELDGRMP
FPVNHGASSEDTLLKDAAKV
CREFTEREQGEVRFSAVALC
KAALEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 842 |
| 15N chemical shifts | 236 |
| 1H chemical shifts | 1384 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | UCHL1 S18Y variant | 1 |
Entities:
Entity 1, UCHL1 S18Y variant 231 residues - Formula weight is not available
Residues 226-231 represent a non-native affinity His tag
| 1 | MET | GLN | LEU | LYS | PRO | MET | GLU | ILE | ASN | PRO | ||||
| 2 | GLU | MET | LEU | ASN | LYS | VAL | LEU | TYR | ARG | LEU | ||||
| 3 | GLY | VAL | ALA | GLY | GLN | TRP | ARG | PHE | VAL | ASP | ||||
| 4 | VAL | LEU | GLY | LEU | GLU | GLU | GLU | SER | LEU | GLY | ||||
| 5 | SER | VAL | PRO | ALA | PRO | ALA | CYS | ALA | LEU | LEU | ||||
| 6 | LEU | LEU | PHE | PRO | LEU | THR | ALA | GLN | HIS | GLU | ||||
| 7 | ASN | PHE | ARG | LYS | LYS | GLN | ILE | GLU | GLU | LEU | ||||
| 8 | LYS | GLY | GLN | GLU | VAL | SER | PRO | LYS | VAL | TYR | ||||
| 9 | PHE | MET | LYS | GLN | THR | ILE | GLY | ASN | SER | CYS | ||||
| 10 | GLY | THR | ILE | GLY | LEU | ILE | HIS | ALA | VAL | ALA | ||||
| 11 | ASN | ASN | GLN | ASP | LYS | LEU | GLY | PHE | GLU | ASP | ||||
| 12 | GLY | SER | VAL | LEU | LYS | GLN | PHE | LEU | SER | GLU | ||||
| 13 | THR | GLU | LYS | MET | SER | PRO | GLU | ASP | ARG | ALA | ||||
| 14 | LYS | CYS | PHE | GLU | LYS | ASN | GLU | ALA | ILE | GLN | ||||
| 15 | ALA | ALA | HIS | ASP | ALA | VAL | ALA | GLN | GLU | GLY | ||||
| 16 | GLN | CYS | ARG | VAL | ASP | ASP | LYS | VAL | ASN | PHE | ||||
| 17 | HIS | PHE | ILE | LEU | PHE | ASN | ASN | VAL | ASP | GLY | ||||
| 18 | HIS | LEU | TYR | GLU | LEU | ASP | GLY | ARG | MET | PRO | ||||
| 19 | PHE | PRO | VAL | ASN | HIS | GLY | ALA | SER | SER | GLU | ||||
| 20 | ASP | THR | LEU | LEU | LYS | ASP | ALA | ALA | LYS | VAL | ||||
| 21 | CYS | ARG | GLU | PHE | THR | GLU | ARG | GLU | GLN | GLY | ||||
| 22 | GLU | VAL | ARG | PHE | SER | ALA | VAL | ALA | LEU | CYS | ||||
| 23 | LYS | ALA | ALA | LEU | GLU | HIS | HIS | HIS | HIS | HIS | ||||
| 24 | HIS |
Samples:
sample_1: UCHL1 S18Y variant, [U-99% 13C; U-99% 15N], 0.7 – 0.8 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 3 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 16537 |
| PDB | |
| DBJ | BAA28214 BAB33087 BAD51987 BAE87282 BAG37761 |
| EMBL | CAA28443 |
| GB | AAD09172 AAH00332 AAH05117 AAH06305 AAY40923 |
| REF | NP_004172 XP_002745940 XP_002814743 XP_003258669 XP_003800742 |
| SP | P09936 Q60HC8 Q9GM50 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts