BMRB Entry 25860
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25860
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Title: Backbone resonance assignments for S. aureus DHFR complexed with NADPH and Trimethoprim
Deposition date: 2015-10-26 Original release date: 2015-12-01
Authors: Sahasrabudhe, Parag
Citation: Sahasrabudhe, Parag. "Driving Drug Discovery with Biophysical Information Application to Staphylococcus aureus Dihydrofolate Reductase (DHFR)" Not known ., .-..
Assembly members:
DHFR, polymer, 158 residues, Formula weight is not available
entity_NDP, non-polymer, 745.421 Da.
entity_TOP, non-polymer, 290.318 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
DHFR: TLSILVAHDLQRVIGFENQL
PWHLPNDLKHVKKLSTGHTL
VMGRKTFESIGKPLPNRRNV
VLTSDTSFNVEGVDVIHSIE
DIYQLPGHVFIFGGQTLFEE
MIDKVDDMYITVIEGKFRGD
TFFPPYTFEDWEVASSVEGK
LDEKNTIPHTFLHLIRKK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 435 |
| 15N chemical shifts | 144 |
| 1H chemical shifts | 144 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DHFR | 1 |
| 2 | NADPH | 2 |
| 3 | TRIMETHOPRIM | 3 |
Entities:
Entity 1, DHFR 158 residues - Formula weight is not available
| 1 | THR | LEU | SER | ILE | LEU | VAL | ALA | HIS | ASP | LEU | ||||
| 2 | GLN | ARG | VAL | ILE | GLY | PHE | GLU | ASN | GLN | LEU | ||||
| 3 | PRO | TRP | HIS | LEU | PRO | ASN | ASP | LEU | LYS | HIS | ||||
| 4 | VAL | LYS | LYS | LEU | SER | THR | GLY | HIS | THR | LEU | ||||
| 5 | VAL | MET | GLY | ARG | LYS | THR | PHE | GLU | SER | ILE | ||||
| 6 | GLY | LYS | PRO | LEU | PRO | ASN | ARG | ARG | ASN | VAL | ||||
| 7 | VAL | LEU | THR | SER | ASP | THR | SER | PHE | ASN | VAL | ||||
| 8 | GLU | GLY | VAL | ASP | VAL | ILE | HIS | SER | ILE | GLU | ||||
| 9 | ASP | ILE | TYR | GLN | LEU | PRO | GLY | HIS | VAL | PHE | ||||
| 10 | ILE | PHE | GLY | GLY | GLN | THR | LEU | PHE | GLU | GLU | ||||
| 11 | MET | ILE | ASP | LYS | VAL | ASP | ASP | MET | TYR | ILE | ||||
| 12 | THR | VAL | ILE | GLU | GLY | LYS | PHE | ARG | GLY | ASP | ||||
| 13 | THR | PHE | PHE | PRO | PRO | TYR | THR | PHE | GLU | ASP | ||||
| 14 | TRP | GLU | VAL | ALA | SER | SER | VAL | GLU | GLY | LYS | ||||
| 15 | LEU | ASP | GLU | LYS | ASN | THR | ILE | PRO | HIS | THR | ||||
| 16 | PHE | LEU | HIS | LEU | ILE | ARG | LYS | LYS |
Entity 2, NADPH - C21 H30 N7 O17 P3 - 745.421 Da.
| 1 | NDP |
Entity 3, TRIMETHOPRIM - C14 H18 N4 O3 - 290.318 Da.
| 1 | TOP |
Samples:
sample_1: DHFR, [U-99% 13C; U-99% 15N], 0.250 mM; NADPH 1 mM; Trimethoprim 0.5 mM; HEPES, [U-2H], 10 mM; sodium chloride 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 8.0; 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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts