BMRB Entry 16833
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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/BMR16833
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Title: Minimal Constraint Solution NMR Structure of Translationally-controlled tumor protein (TCTP) from C.elegans, Northeast Structural Genomics Consortium Target Target WR73
Deposition date: 2010-04-02 Original release date: 2010-04-29
Authors: Aramini, James; Rossi, Paolo; Cort, John; Cooper, Bonnie; Maglaqui, Melissa; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano
Citation: Aramini, James; Rossi, Paolo; Cort, John; Cooper, Bonnie; Maglaqui, Melissa; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano. "Minimal Constraint Solution NMR Structure of Translationally-controlled tumor protein (TCTP) from C.elegans, Northeast Structural Genomics Consortium Target Target WR73" To be published ., .-..
Assembly members:
WR73, polymer, 183 residues, 20813.826 Da.
Natural source: Common Name: Caenorhabditis elegans Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
WR73: MLIYKDIFTDDELSSDSFPM
KLVDDLVYEFKGKHVVRKEG
EIVLAGSNPSAEEGAEDDGS
DEHVERGIDIVLNHKLVEMN
CYEDASMFKAYIKKFMKNVI
DHMEKNNRDKADVDAFKKKI
QGWVVSLLAKDRFKNLAFFI
GERAAEGAENGQVAIIEYRD
VDGTEVPTLMLVKEAIIEEK
CLE
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 602 |
| 15N chemical shifts | 189 |
| 1H chemical shifts | 484 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | WR73 | 1 |
Entities:
Entity 1, WR73 183 residues - 20813.826 Da.
| 1 | MET | LEU | ILE | TYR | LYS | ASP | ILE | PHE | THR | ASP | ||||
| 2 | ASP | GLU | LEU | SER | SER | ASP | SER | PHE | PRO | MET | ||||
| 3 | LYS | LEU | VAL | ASP | ASP | LEU | VAL | TYR | GLU | PHE | ||||
| 4 | LYS | GLY | LYS | HIS | VAL | VAL | ARG | LYS | GLU | GLY | ||||
| 5 | GLU | ILE | VAL | LEU | ALA | GLY | SER | ASN | PRO | SER | ||||
| 6 | ALA | GLU | GLU | GLY | ALA | GLU | ASP | ASP | GLY | SER | ||||
| 7 | ASP | GLU | HIS | VAL | GLU | ARG | GLY | ILE | ASP | ILE | ||||
| 8 | VAL | LEU | ASN | HIS | LYS | LEU | VAL | GLU | MET | ASN | ||||
| 9 | CYS | TYR | GLU | ASP | ALA | SER | MET | PHE | LYS | ALA | ||||
| 10 | TYR | ILE | LYS | LYS | PHE | MET | LYS | ASN | VAL | ILE | ||||
| 11 | ASP | HIS | MET | GLU | LYS | ASN | ASN | ARG | ASP | LYS | ||||
| 12 | ALA | ASP | VAL | ASP | ALA | PHE | LYS | LYS | LYS | ILE | ||||
| 13 | GLN | GLY | TRP | VAL | VAL | SER | LEU | LEU | ALA | LYS | ||||
| 14 | ASP | ARG | PHE | LYS | ASN | LEU | ALA | PHE | PHE | ILE | ||||
| 15 | GLY | GLU | ARG | ALA | ALA | GLU | GLY | ALA | GLU | ASN | ||||
| 16 | GLY | GLN | VAL | ALA | ILE | ILE | GLU | TYR | ARG | ASP | ||||
| 17 | VAL | ASP | GLY | THR | GLU | VAL | PRO | THR | LEU | MET | ||||
| 18 | LEU | VAL | LYS | GLU | ALA | ILE | ILE | GLU | GLU | LYS | ||||
| 19 | CYS | LEU | GLU |
Samples:
sample_1: WR73, [U-13C; U-15N; U-2H; ILVFY-1H], 0.82 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_2: WR73, [U-5% 13C; U-100% 15N], 0.85 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_conditions_1: 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-15N TROSY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-15N-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-13C-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-13C-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-15N-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC high resolution | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3, Goddard - chemical shift assignment, data analysis, peak picking
TOPSPIN v2.1, Bruker Biospin - collection
VNMRJ, Varian - collection
PSVS v1.4, Bhattacharya and Montelione - structure validation
TALOS vplus, Cornilescu, Delaglio and Bax - dihedral angle constraints
PDBStat v5.1, Tejero and Montelione - PDB coordinate analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts