BMRB Entry 5396

Click here to enlarge.

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/BMR5396
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

Title:
NMR-based solution structure of the complex of Lactobacillus casei dihydrofolate reductase with trimethoprim and NADPH
Deposition date:
2002-06-14
Original release date:
2002-11-04
Authors:
Polshakov, Vladimir; Smirnov, Eugeni; Birdsall, Berry; Kelly, Geoff; Feeney, James
Citation:

Citation: Polshakov, Vladimir; Smirnov, Eugeni; Birdsall, Berry; Kelly, Geoff; Feeney, James. "Letters to the Editor: NMR-based solution structure of the complex of Lactobacillus casei dihydrofolate reductase with trimethoprim and NADPH "  J. Biomol. NMR 24, 67-70 (2002).

Assembly members:

Assembly members:
Dihydrofolate reductase, polymer, 162 residues, 18300 Da.
NAP, non-polymer, 743.405 Da.
TOP, non-polymer, 290.318 Da.

Natural source:

Natural source:   Common Name: L. casei   Taxonomy ID: 1582   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Lactobacillus casei

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PMT702

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Dihydrofolate reductase: TAFLWAQDRDGLIGKDGHLP WHLPDDLHYFRAQTVGKIMV VGRRTYESFPKRPLPERTNV VLTHQEDYQAQGAVVVHDVA AVFAYAKQHPDQELVIAGGA QIFTAFKDDVDTLLVTRLAG SFEGDTKMIPLNWDDFTKVS SRTVEDTNPALTHTYEVWQK KA

Data sets:
Data typeCount
1H chemical shifts1122
15N chemical shifts172

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1dihydrofolate reductase1
2trimethoprim3
3NADPH2

Entities:

Entity 1, dihydrofolate reductase 162 residues - 18300 Da.

1   THRALAPHELEUTRPALAGLNASPARGASP
2   GLYLEUILEGLYLYSASPGLYHISLEUPRO
3   TRPHISLEUPROASPASPLEUHISTYRPHE
4   ARGALAGLNTHRVALGLYLYSILEMETVAL
5   VALGLYARGARGTHRTYRGLUSERPHEPRO
6   LYSARGPROLEUPROGLUARGTHRASNVAL
7   VALLEUTHRHISGLNGLUASPTYRGLNALA
8   GLNGLYALAVALVALVALHISASPVALALA
9   ALAVALPHEALATYRALALYSGLNHISPRO
10   ASPGLNGLULEUVALILEALAGLYGLYALA
11   GLNILEPHETHRALAPHELYSASPASPVAL
12   ASPTHRLEULEUVALTHRARGLEUALAGLY
13   SERPHEGLUGLYASPTHRLYSMETILEPRO
14   LEUASNTRPASPASPPHETHRLYSVALSER
15   SERARGTHRVALGLUASPTHRASNPROALA
16   LEUTHRHISTHRTYRGLUVALTRPGLNLYS
17   LYSALA

Entity 3, trimethoprim - C14 H18 N4 O3 - 290.318 Da.

1   TOP

Entity 2, NADPH - C21 H28 N7 O17 P3 - 743.405 Da.

1   NAP

Samples:

sample_1: Dihydrofolate reductase, [U-95% 15N], 1.5 – 4.0 mM; TRIMETHOPRIM, [U-95% 15N], 1.5 – 4.0 mM; NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, [U-95% 15N], 1.5 – 4.0 mM; potassium phosphate 25 mM; KCl 50 mM

sample_2: Dihydrofolate reductase2.0 – 4.0 mM; TRIMETHOPRIM2.0 – 4.0 mM; NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE2.0 – 4.0 mM; potassium phosphate 25 mM; KCl 50 mM

sample_3: Dihydrofolate reductase, [U-95% 15N], 0.5 mM; TRIMETHOPRIM, [U-95% 15N], 0.5 mM; NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, [U-95% 15N], 0.5 mM; DMPC/DHPC (3/1) 5%; H2O/D2O (90/10) 95%

condition_1: pH: 6.5; temperature: 308 K; ionic strength: 0.125 M

Experiments:

NameSampleSample stateSample conditions
DQF-COSYnot availablenot availablecondition_1
TOCSYnot availablenot availablecondition_1
NOESYnot availablenot availablecondition_1
1H-15N HSQCnot availablenot availablecondition_1
1H-15N NOESY-HSQCnot availablenot availablecondition_1
1H-15N TOCSY-HSQCnot availablenot availablecondition_1
HNHAnot availablenot availablecondition_1
HNHBnot availablenot availablecondition_1
15N-rejected NOESYnot availablenot availablecondition_1
J-modulated 1H-15N HSQCnot availablenot availablecondition_1

Software:

VNMR v6.1 - spectra processing

NMRPipe v1998-2001 - spectra processing, spectra analysis

XEASY v1.3 - spectra analysis

NMRTABLE v2.0 - analysis of signal assignmnent

AngleSearch v2.10 - stereospecific assignmnents

NMR spectrometers:

  • Varian UNITY 600 MHz
  • Varian UNITYPlus 500 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 17125 17310 17311 3524 3525 4262 7196 7197 7198 7199 7200
PDB
DBJ BAI41869
EMBL CAR87293 CAR90253
GB AAA25237 AER64174 AGP71178 AGP74091 EDY98474
PRF 0309272A 1107232A
REF WP_005686414 WP_005689288 WP_014569635 WP_033573062 YP_003171144
SP P00381
AlphaFold P00381

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