BMRB Entry 18567
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18567
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Title: Overexpression, purification and structural characterization of S114A mutant of UVI31+ from chlamydomonas reinhardtii PubMed: 23266947
Deposition date: 2012-07-05 Original release date: 2013-02-28
Authors: Singh, Himanshu; Chary, Kandala
Citation: Singh, Himanshu; Raghavan, Vandana; Shukla, Manish; Rao, Basuthkar; Chary, Kandala. "H, 13C and 15N resonance assignments of S114A mutant of UVI31+ from Chlamydomonas reinhardtii." Biomol. NMR Assignments 8, 71-74 (2014).
Assembly members:
S114A_mutant_of_UVI31+, polymer, 123 residues, Formula weight is not available
Natural source: Common Name: Green algae Taxonomy ID: 3055 Superkingdom: Eukaryota Kingdom: not available Genus/species: Chlamydomonas reinhardtii
Experimental source: Production method: cell free synthesis Host organism: chlamydomonas reinhardtii
Entity Sequences (FASTA):
S114A_mutant_of_UVI31+: MRGSHHHHHHGSHVISSIAS
RGSMAEHQLGPIAGAIKSKV
EAALSPTHFKLINDSHKHAG
HYARDGSTASDAGETHFRLE
VTSDAFKGLTLVKRHQLIYG
LLSDEFKAGLHALAMTTKTP
AEQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 314 |
| 15N chemical shifts | 107 |
| 1H chemical shifts | 107 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | S114A mutant of UVI31+ | 1 |
Entities:
Entity 1, S114A mutant of UVI31+ 123 residues - Formula weight is not available
| 1 | MET | ARG | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | GLY | SER | HIS | VAL | ILE | SER | SER | ILE | ALA | SER | ||||
| 3 | ARG | GLY | SER | MET | ALA | GLU | HIS | GLN | LEU | GLY | ||||
| 4 | PRO | ILE | ALA | GLY | ALA | ILE | LYS | SER | LYS | VAL | ||||
| 5 | GLU | ALA | ALA | LEU | SER | PRO | THR | HIS | PHE | LYS | ||||
| 6 | LEU | ILE | ASN | ASP | SER | HIS | LYS | HIS | ALA | GLY | ||||
| 7 | HIS | TYR | ALA | ARG | ASP | GLY | SER | THR | ALA | SER | ||||
| 8 | ASP | ALA | GLY | GLU | THR | HIS | PHE | ARG | LEU | GLU | ||||
| 9 | VAL | THR | SER | ASP | ALA | PHE | LYS | GLY | LEU | THR | ||||
| 10 | LEU | VAL | LYS | ARG | HIS | GLN | LEU | ILE | TYR | GLY | ||||
| 11 | LEU | LEU | SER | ASP | GLU | PHE | LYS | ALA | GLY | LEU | ||||
| 12 | HIS | ALA | LEU | ALA | MET | THR | THR | LYS | THR | PRO | ||||
| 13 | ALA | GLU | GLN |
Samples:
sample_1: S114A mutant of UVI31+, [U-100% 13C; U-100% 15N], 0.8 ± 0.03 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
FELIX v2002, accelrys Inc. - processing
NMR spectrometers:
- Bruker Avance 800 MHz
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