BMRB Entry 30020
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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/BMR30020
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Title: The C-terminal domain of rice beta-galactosidase 1 PubMed: 27451952
Deposition date: 2016-02-22 Original release date: 2016-08-08
Authors: Rimlumduan, T.; Hua, Y.-l.; Tanaka, T.; Ketudat-Cairns, J.R.
Citation: Rimlumduan, T.; Hua, Y.-l.; Tanaka, T.; Ketudat-Cairns, J.R.. "Structure of a plant beta-galactosidase C-terminal domain" Biochim. Biophys. Acta 1864, 1411-1418 (2016).
Assembly members:
entity_1, polymer, 122 residues,   13029.779 Da.
Natural source: Common Name: Rice Taxonomy ID: 39946 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Oryza sativa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GSHMRTVSGVCADVSEYHPN
IKNWQIESYGEPEFHTAKVH
LKCAPGQTISAIKFASFGTP
LGTCGTFQQGECHSINSNSV
LERKCIGLERCVVAISPSNF
GGDPCPEVMKRVAVEAVCST
AA
- assigned_chemical_shifts
 
| Data type | Count | 
| 13C chemical shifts | 444 | 
| 15N chemical shifts | 114 | 
| 1H chemical shifts | 775 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | entity_1 | 1 | 
Entities:
Entity 1, entity_1 122 residues - 13029.779 Da.
| 1 | GLY | SER | HIS | MET | ARG | THR | VAL | SER | GLY | VAL | ||||
| 2 | CYS | ALA | ASP | VAL | SER | GLU | TYR | HIS | PRO | ASN | ||||
| 3 | ILE | LYS | ASN | TRP | GLN | ILE | GLU | SER | TYR | GLY | ||||
| 4 | GLU | PRO | GLU | PHE | HIS | THR | ALA | LYS | VAL | HIS | ||||
| 5 | LEU | LYS | CYS | ALA | PRO | GLY | GLN | THR | ILE | SER | ||||
| 6 | ALA | ILE | LYS | PHE | ALA | SER | PHE | GLY | THR | PRO | ||||
| 7 | LEU | GLY | THR | CYS | GLY | THR | PHE | GLN | GLN | GLY | ||||
| 8 | GLU | CYS | HIS | SER | ILE | ASN | SER | ASN | SER | VAL | ||||
| 9 | LEU | GLU | ARG | LYS | CYS | ILE | GLY | LEU | GLU | ARG | ||||
| 10 | CYS | VAL | VAL | ALA | ILE | SER | PRO | SER | ASN | PHE | ||||
| 11 | GLY | GLY | ASP | PRO | CYS | PRO | GLU | VAL | MET | LYS | ||||
| 12 | ARG | VAL | ALA | VAL | GLU | ALA | VAL | CYS | SER | THR | ||||
| 13 | ALA | ALA | 
Samples:
sample_1: D2O, [U-2H], 5%; H2O 95%; OsBGal1 Cter 0.5 mM; sodium chloride 100 mM; sodium phosphate 20 mM
sample_2: D2O, [U-2H], 100%; OsBGal1 Cter 0.54 mM; sodium chloride 100 mM; sodium phosphate 20 mM
sample_3: D2O, [U-2H], 5%; H2O 95%; OsBGal1 Cter, [U-100% 15N], 0.79 mM; sodium chloride 100 mM; sodium phosphate 20 mM
sample_4: D2O, [U-2H], 5%; H2O 95%; OsBGal1 Cter, [U-100% 13C; U-100% 15N], 0.5 mM; sodium chloride 100 mM; sodium phosphate 20 mM
sample_5: D2O, [U-2H], 5%; H2O 95%; OsBGal1 Cter, [U-10% 13C], 0.18 mM; sodium chloride 100 mM; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 120 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions | 
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 | 
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 | 
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 | 
| 3D HNHA | sample_3 | isotropic | sample_conditions_1 | 
| 2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_1 | 
| 2D 1H-13C HSQC | sample_4 | isotropic | sample_conditions_1 | 
| 3D HNCO | sample_4 | isotropic | sample_conditions_1 | 
| 3D CBCA(CO)NH | sample_4 | isotropic | sample_conditions_1 | 
| 3D HNCACB | sample_4 | isotropic | sample_conditions_1 | 
| 3D HCCH-TOCSY | sample_4 | isotropic | sample_conditions_1 | 
| 3D C(CO)NH | sample_4 | isotropic | sample_conditions_1 | 
| 3D HBCBCACOCAHA | sample_4 | isotropic | sample_conditions_1 | 
| 3D 1H-13C NOESY | sample_4 | isotropic | sample_conditions_1 | 
| 2D 1H-13C HSQC | sample_5 | isotropic | sample_conditions_1 | 
Software:
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PIPP, Garrett - peak picking
ProcheckNMR, Laskowski and MacArthur - data analysis
X-PLOR vv3.1, Brunger - structure calculation
NMR spectrometers:
- Varian UNITY INOVA 500 MHz
 - Bruker AVANCE DRX 800 MHz
 - Bruker AVANCE III 800 MHz
 
Download simulated HSQC data in one of the following formats:
            
CSV: Backbone
            or all simulated shifts
            
SPARKY: Backbone
            or all simulated shifts