BMRB Entry 16864
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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/BMR16864
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Title: Sequence Specific 1H, 13C and 15N backbone resonance assignments of uvi31+ from Chlamydomonas reinhardtii PubMed: 20526700
Deposition date: 2010-04-14 Original release date: 2010-06-15
Authors: Rout, Ashok; Minda, Renu; Peri, Dinakar; Bhattacharya, S; Rao, Basuthkar; Chary, Kandala
Citation: Rout, Ashok; Minda, R.; Peri, D.; Ramakrishnan, V.; Bhattacharjee, S.; Rao, B.; Chary, K.. "Sequence specific 1H, 13C and 15N backbone resonance assignments of UVI31+ from Chlamydomonas reinhardtii." Biomol. NMR Assignments 4, 171-174 (2010).
Assembly members:
uvi31+, polymer, 120 residues, Formula weight is not available
Natural source: Common Name: green algae Taxonomy ID: 3055 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Chlamydomonas reinhardtii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
uvi31+: MRGSHHHHHHGSHVISSIAS
MAEHQLGPIAGAIKSKVEAA
LSPTHFKLINDSHKHAGHYA
RDGSTASDAGETHFRLEVTS
DAFKGLTLVKRHQLIYGLLS
DEFKAGLHALSMTTKTPAEQ
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 401 |
15N chemical shifts | 111 |
1H chemical shifts | 494 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | uvi31+ | 1 |
Entities:
Entity 1, uvi31+ 120 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 | MET | ALA | GLU | HIS | GLN | LEU | GLY | PRO | ILE | ALA | |
4 | GLY | ALA | ILE | LYS | SER | LYS | VAL | GLU | ALA | ALA | |
5 | LEU | SER | PRO | THR | HIS | PHE | LYS | LEU | ILE | ASN | |
6 | ASP | SER | HIS | LYS | HIS | ALA | GLY | HIS | TYR | ALA | |
7 | ARG | ASP | GLY | SER | THR | ALA | SER | ASP | ALA | GLY | |
8 | GLU | THR | HIS | PHE | ARG | LEU | GLU | VAL | THR | SER | |
9 | ASP | ALA | PHE | LYS | GLY | LEU | THR | LEU | VAL | LYS | |
10 | ARG | HIS | GLN | LEU | ILE | TYR | GLY | LEU | LEU | SER | |
11 | ASP | GLU | PHE | LYS | ALA | GLY | LEU | HIS | ALA | LEU | |
12 | SER | MET | THR | THR | LYS | THR | PRO | ALA | GLU | GLN |
Samples:
sample_1: uvi31+, [U-100% 15N], 0.8 mM; H2O 90%; D2O 10%; sodium phosphate 50 mM; NaCl 50 mM
sample_2: uvi31+, [U-100% 13C; U-100% 15N], 0.7 mM; H2O 90%; D2O 10%; sodium phosphate 50 mM; NaCl 50 mM
sample_conditions_1: ionic strength: 0.05 M; 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 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - processing
FELIX, Accelrys Software Inc. - processing
CARA, Keller and Wuthrich - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts