BMRB Entry 4262
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR4262
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: POLSHAKOV, V.; BIRDSALL, B.; FRENKIEL, T.; GARGARO, A.; FEENEY, J.. "Structure and dynamics in solution of the complex of Lactobillus casei
dihydrofolate reductase with the new lipophilic antifolate drug trimetrexate"" Protein Sci. 8, 467-481 (1999).
Assembly members:
DIHYDROFOLATE REDUCTASE, polymer, 162 residues, 18300 Da.
TMQ, non-polymer, 370.426 Da.
Natural source: Common Name: Lactobacillus casei Taxonomy ID: 1582 Superkingdom: Bacteria Kingdom: not available Genus/species: Lactobacillus casei
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PLASMID
Entity Sequences (FASTA):
DIHYDROFOLATE REDUCTASE: TAFLWAQDRDGLIGKDGHLP
WHLPDDLHYFRAQTVGKIMV
VGRRTYESFPKRPLPERTNV
VLTHQEDYQAQGAVVVHDVA
AVFAYAKQHPDQELVIAGGA
QIFTAFKDDVDTLLVTRLAG
SFEGDTKMIPLNWDDFTKVS
SRTVEDTNPALTHTYEVWQK
KA
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 1082 |
| 15N chemical shifts | 168 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DIHYDROFOLATE REDUCTASE | 1 |
| 2 | TRIMETREXATE | 2 |
Entities:
Entity 1, DIHYDROFOLATE REDUCTASE 162 residues - 18300 Da.
| 1 | THR | ALA | PHE | LEU | TRP | ALA | GLN | ASP | ARG | ASP | ||||
| 2 | GLY | LEU | ILE | GLY | LYS | ASP | GLY | HIS | LEU | PRO | ||||
| 3 | TRP | HIS | LEU | PRO | ASP | ASP | LEU | HIS | TYR | PHE | ||||
| 4 | ARG | ALA | GLN | THR | VAL | GLY | LYS | ILE | MET | VAL | ||||
| 5 | VAL | GLY | ARG | ARG | THR | TYR | GLU | SER | PHE | PRO | ||||
| 6 | LYS | ARG | PRO | LEU | PRO | GLU | ARG | THR | ASN | VAL | ||||
| 7 | VAL | LEU | THR | HIS | GLN | GLU | ASP | TYR | GLN | ALA | ||||
| 8 | GLN | GLY | ALA | VAL | VAL | VAL | HIS | ASP | VAL | ALA | ||||
| 9 | ALA | VAL | PHE | ALA | TYR | ALA | LYS | GLN | HIS | PRO | ||||
| 10 | ASP | GLN | GLU | LEU | VAL | ILE | ALA | GLY | GLY | ALA | ||||
| 11 | GLN | ILE | PHE | THR | ALA | PHE | LYS | ASP | ASP | VAL | ||||
| 12 | ASP | THR | LEU | LEU | VAL | THR | ARG | LEU | ALA | GLY | ||||
| 13 | SER | PHE | GLU | GLY | ASP | THR | LYS | MET | ILE | PRO | ||||
| 14 | LEU | ASN | TRP | ASP | ASP | PHE | THR | LYS | VAL | SER | ||||
| 15 | SER | ARG | THR | VAL | GLU | ASP | THR | ASN | PRO | ALA | ||||
| 16 | LEU | THR | HIS | THR | TYR | GLU | VAL | TRP | GLN | LYS | ||||
| 17 | LYS | ALA |
Entity 2, TRIMETREXATE - C19 H24 N5 O3 - 370.426 Da.
| 1 | TMQ |
Samples:
sample_1: DIHYDROFOLATE REDUCTASE, [U-15N], 1.0 – 4.0 mM; potassium phosphate 50 mM; TRIMETREXATE1.0 – 4.0 mM
sample_2: DIHYDROFOLATE REDUCTASE1.0 – 4.0 mM; potassium phosphate 50 mM; TRIMETREXATE1.0 – 4.0 mM
sample_cond_1: pH: 6.5; temperature: 308 K; ionic strength: 550 mM; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| DQF-COSY | not available | not available | sample_cond_1 |
| NOESY | not available | not available | sample_cond_1 |
| ROESY | not available | not available | sample_cond_1 |
| HNHA | not available | not available | sample_cond_1 |
| HNHB | not available | not available | sample_cond_1 |
| HSQC | not available | not available | sample_cond_1 |
| 3D-1H/15N-TOCSY-HMQC | not available | not available | sample_cond_1 |
| 3D-1H/ 15N-ROESY-HMQC | not available | not available | sample_cond_1 |
| 3D-1H/15N-NOESY-HMQC | not available | not available | sample_cond_1 |
| 1D-NOE DIFFERENCE | not available | not available | sample_cond_1 |
Software:
No software information available
NMR spectrometers:
- VARIAN UNITY 600 MHz
Related Database Links:
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks