BMRB Entry 25860

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:

Citation: Sahasrabudhe, Parag. "Driving Drug Discovery with Biophysical Information Application to Staphylococcus aureus Dihydrofolate Reductase (DHFR)"  .

Assembly members:

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:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts435
15N chemical shifts144
1H chemical shifts144

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DHFR1
2NADPH2
3TRIMETHOPRIM3

Entities:

Entity 1, DHFR 158 residues - Formula weight is not available

1   THRLEUSERILELEUVALALAHISASPLEU
2   GLNARGVALILEGLYPHEGLUASNGLNLEU
3   PROTRPHISLEUPROASNASPLEULYSHIS
4   VALLYSLYSLEUSERTHRGLYHISTHRLEU
5   VALMETGLYARGLYSTHRPHEGLUSERILE
6   GLYLYSPROLEUPROASNARGARGASNVAL
7   VALLEUTHRSERASPTHRSERPHEASNVAL
8   GLUGLYVALASPVALILEHISSERILEGLU
9   ASPILETYRGLNLEUPROGLYHISVALPHE
10   ILEPHEGLYGLYGLNTHRLEUPHEGLUGLU
11   METILEASPLYSVALASPASPMETTYRILE
12   THRVALILEGLUGLYLYSPHEARGGLYASP
13   THRPHEPHEPROPROTYRTHRPHEGLUASP
14   TRPGLUVALALASERSERVALGLUGLYLYS
15   LEUASPGLULYSASNTHRILEPROHISTHR
16   PHELEUHISLEUILEARGLYSLYS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_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

Related Database Links:

UNP P0A017
AlphaFold P10167

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