BMRB Entry 19566
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR19566
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Title: chemical shift assignments and 3Jcgn & 3Jcgc' scalar couplings for human dihdyrofolate reductase bound to NADPH PubMed: 24498949
Deposition date: 2013-10-18 Original release date: 2016-04-04
Authors: Wright, Peter; Bhabha, Gira; Tuttle, Lisa; Kroon, Gerard
Citation: Tuttle, Lisa; Dyson, H. Jane; Wright, Peter. "Side Chain Conformational Averaging in Human Dihydrofolate Reductase" Biochemistry 53, 1134-1145 (2014).
Assembly members:
DHFR, polymer, 187 residues, Formula weight is not available
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, non-polymer, 745.421 Da.
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
DHFR: MVGSLNCIVAVSQNMGIGKN
GDLPWPPLRNEFRYFQRMTT
TSSVEGKQNLVIMGKKTWFS
IPEKNRPLKGRINLVLSREL
KEPPQGAHFLSRSLDDALKL
TEQPELANKVDMVWIVGGSS
VYKEAMNHPGHLKLFVTRIM
QDFESDTFFPEIDLEKYKLL
PEYPGVLSDVQEEKGIKYKF
EVYEKND
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 13C chemical shifts | 275 |
| 15N chemical shifts | 167 |
| 1H chemical shifts | 452 |
| coupling constants | 119 |