BMRB Entry 16352
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16352
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Title: Solution NMR structure of protein AF2094 from Archaeoglobus fulgidus. Northeast Structural Genomics Consotium (NESG) target GT2
Deposition date: 2009-06-15 Original release date: 2009-07-07
Authors: Lemak, Alexander; Yee, Adelinda; Wu, Bin; Karra, Murthy; Ramelot, Theresa; Fares, Christophe; Semesi, Antony; Kennedy, Michael; Montelione, Gaetano; Arrowsmith, Cheryl
Citation: Lemak, Alexander; Yee, Adelinda; Wu, Bin; Karra, Murthy; Ramelot, Theresa; Fares, Christophe; Semesi, Antony; Kennedy, Michael; Montelione, Gaetano; Arrowsmith, Cheryl. "Solution NMR structure of proterin AF2094 from Archaeoglobus fulgidus." Not known ., .-..
Assembly members:
AF2094, polymer, 95 residues, 10726.126 Da.
Natural source: Common Name: Archaeoglobus fulgidus Taxonomy ID: 2234 Superkingdom: Archaea Kingdom: not available Genus/species: Archaeoglobus fulgidus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
AF2094: QGHMDLICMYVFKGEESFGE
SIDVYGDYLIVKVGTEFLAV
PKKSIKSVEDGRIVIGEFDE
EEARELGRKWLEEKSKPVTL
EELKSYGFGEEGEGS
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 391 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 640 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AF2094 | 1 |
Entities:
Entity 1, AF2094 95 residues - 10726.126 Da.
| 1 | GLN | GLY | HIS | MET | ASP | LEU | ILE | CYS | MET | TYR | ||||
| 2 | VAL | PHE | LYS | GLY | GLU | GLU | SER | PHE | GLY | GLU | ||||
| 3 | SER | ILE | ASP | VAL | TYR | GLY | ASP | TYR | LEU | ILE | ||||
| 4 | VAL | LYS | VAL | GLY | THR | GLU | PHE | LEU | ALA | VAL | ||||
| 5 | PRO | LYS | LYS | SER | ILE | LYS | SER | VAL | GLU | ASP | ||||
| 6 | GLY | ARG | ILE | VAL | ILE | GLY | GLU | PHE | ASP | GLU | ||||
| 7 | GLU | GLU | ALA | ARG | GLU | LEU | GLY | ARG | LYS | TRP | ||||
| 8 | LEU | GLU | GLU | LYS | SER | LYS | PRO | VAL | THR | LEU | ||||
| 9 | GLU | GLU | LEU | LYS | SER | TYR | GLY | PHE | GLY | GLU | ||||
| 10 | GLU | GLY | GLU | GLY | SER |
Samples:
sample_1: af2094 0.5 mM; TRIS 10 mM; sodium chloride 300 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C_aromatic NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - peak picking
FMC, Lemak, Steren, Llinas, Arrowsmith - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
PSVS, Bhattacharya and Montelione - structure validation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
- 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