BMRB Entry 19565

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR19565

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Title:
chemical shift assignments and 3Jcgn & 3Jcgc' scalar couplings for human dihdyrofolate reductase bound to NADP+ and THF
Deposition date:
2013-10-18
Original release date:
2016-04-04
Authors:
Wright, Peter; Bhabha, Gira; Tuttle, Lisa; Kroon, Gerard
Citation:

Citation: Tuttle, Lisa; Dyson, H. Jane; Wright, Peter. "Side Chain Conformational Averaging in Human Dihydrofolate Reductase"  Biochemistry 53, 1134-1145 (2014).
PubMed: 24498949

Assembly members:

Assembly members:
DHFR, polymer, 187 residues, Formula weight is not available
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, non-polymer, 745.421 Da.
(6S)-5,6,7,8-TETRAHYDROFOLATE, non-polymer, 445.429 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DHFR: MVGSLNCIVAVSQNMGIGKN GDLPWPPLRNEFRYFQRMTT TSSVEGKQNLVIMGKKTWFS IPEKNRPLKGRINLVLSREL KEPPQGAHFLSRSLDDALKL TEQPELANKVDMVWIVGGSS VYKEAMNHPGHLKLFVTRIM QDFESDTFFPEIDLEKYKLL PEYPGVLSDVQEEKGIKYKF EVYEKND

Data sets:
Data typeCount
13C chemical shifts260
15N chemical shifts170
1H chemical shifts440
coupling constants122

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1DHFR1
2NADP+2
3Tetrahydrofolate3

Entities:

Entity 1, DHFR 187 residues - Formula weight is not available

1   METVALGLYSERLEUASNCYSILEVALALA
2   VALSERGLNASNMETGLYILEGLYLYSASN
3   GLYASPLEUPROTRPPROPROLEUARGASN
4   GLUPHEARGTYRPHEGLNARGMETTHRTHR
5   THRSERSERVALGLUGLYLYSGLNASNLEU
6   VALILEMETGLYLYSLYSTHRTRPPHESER
7   ILEPROGLULYSASNARGPROLEULYSGLY
8   ARGILEASNLEUVALLEUSERARGGLULEU
9   LYSGLUPROPROGLNGLYALAHISPHELEU
10   SERARGSERLEUASPASPALALEULYSLEU
11   THRGLUGLNPROGLULEUALAASNLYSVAL
12   ASPMETVALTRPILEVALGLYGLYSERSER
13   VALTYRLYSGLUALAMETASNHISPROGLY
14   HISLEULYSLEUPHEVALTHRARGILEMET
15   GLNASPPHEGLUSERASPTHRPHEPHEPRO
16   GLUILEASPLEUGLULYSTYRLYSLEULEU
17   PROGLUTYRPROGLYVALLEUSERASPVAL
18   GLNGLUGLULYSGLYILELYSTYRLYSPHE
19   GLUVALTYRGLULYSASNASP

Entity 2, NADP+ - 745.421 Da.

1   NDP

Entity 3, Tetrahydrofolate - 445.429 Da.

1   THG

Samples:

sample_1: DHFR, [U-99% 15N], 1000 uM; potassium phosphate 50 mM; potassium chloride 50 mM; EDTA 1 mM; DTT 1 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 750 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks