BMRB Entry 27159
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27159
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Title: LRT2 Cyclophilin of rice PubMed: 29353448
Deposition date: 2017-06-22 Original release date: 2018-02-02
Authors: Acevedo, Lucila; Nicholson, Linda
Citation: Acevedo, Lucila; Nicholson, Linda. "1H, 13C and 15N NMR assignments of cyclophilin LRT2 (OsCYP2) from rice" Biomol. NMR Assignments 12, 171-174 (2018).
Assembly members:
LRT2, polymer, 175 residues, 18686.36 Da.
Natural source: Common Name: rice Taxonomy ID: 4530 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Oryza sativa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: Pet28
Entity Sequences (FASTA):
LRT2: GHMMSNTRVFFDMTVGGAPA
GRIVMELYAKDVPRTAENFR
ALCTGEKGVGKSGKPLHYKG
STFHRVIPEFMCQGGDFTRG
NGTGGESIYGEKFADEVFKF
KHDSPGILSMANAGPNTNGS
QFFICTVPCSWLDGKHVVFG
RVVEGMDVVKAIEKVGSRGG
STAKPVVIADCGQLS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 638 |
| 15N chemical shifts | 164 |
| 1H chemical shifts | 983 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | LRT2 | 1 |
Entities:
Entity 1, LRT2 175 residues - 18686.36 Da.
residue 1 is left after TEV cleavage and residues 2 and 3 represent cloning artifacts
| 1 | GLY | HIS | MET | MET | SER | ASN | THR | ARG | VAL | PHE | ||||
| 2 | PHE | ASP | MET | THR | VAL | GLY | GLY | ALA | PRO | ALA | ||||
| 3 | GLY | ARG | ILE | VAL | MET | GLU | LEU | TYR | ALA | LYS | ||||
| 4 | ASP | VAL | PRO | ARG | THR | ALA | GLU | ASN | PHE | ARG | ||||
| 5 | ALA | LEU | CYS | THR | GLY | GLU | LYS | GLY | VAL | GLY | ||||
| 6 | LYS | SER | GLY | LYS | PRO | LEU | HIS | TYR | LYS | GLY | ||||
| 7 | SER | THR | PHE | HIS | ARG | VAL | ILE | PRO | GLU | PHE | ||||
| 8 | MET | CYS | GLN | GLY | GLY | ASP | PHE | THR | ARG | GLY | ||||
| 9 | ASN | GLY | THR | GLY | GLY | GLU | SER | ILE | TYR | GLY | ||||
| 10 | GLU | LYS | PHE | ALA | ASP | GLU | VAL | PHE | LYS | PHE | ||||
| 11 | LYS | HIS | ASP | SER | PRO | GLY | ILE | LEU | SER | MET | ||||
| 12 | ALA | ASN | ALA | GLY | PRO | ASN | THR | ASN | GLY | SER | ||||
| 13 | GLN | PHE | PHE | ILE | CYS | THR | VAL | PRO | CYS | SER | ||||
| 14 | TRP | LEU | ASP | GLY | LYS | HIS | VAL | VAL | PHE | GLY | ||||
| 15 | ARG | VAL | VAL | GLU | GLY | MET | ASP | VAL | VAL | LYS | ||||
| 16 | ALA | ILE | GLU | LYS | VAL | GLY | SER | ARG | GLY | GLY | ||||
| 17 | SER | THR | ALA | LYS | PRO | VAL | VAL | ILE | ALA | ASP | ||||
| 18 | CYS | GLY | GLN | LEU | SER |
Samples:
sample_1: LRT2, [U-99% 13C; U-99% 15N], 1.16 mM; potassium chloride 50 mM; potassium phosphate 20 mM; TCEP 1 mM; sodium azide 5 mM
sample_conditions_1: ionic strength: 94.76 mM; pH: 6.7; 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 C(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 H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| NCBI | BAS76709 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts