BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16822

Title: Solution structure of Bacillus anthracis dihydrofolate reductase   PubMed: 19323450

Deposition date: 2010-04-01 Original release date: 2010-04-29

Authors: deshmukh, lalit; vinogradova, olga; beierlein, jennifer; frey, kathleen; anderson, amy

Citation: Beierlein, Jennifer; Deshmukh, Lalit; Frey, Kathleen; Vinogradova, Olga; Anderson, Amy. "The solution structure of Bacillus anthracis dihydrofolate reductase yields insight into the analysis of structure-activity relationships for novel inhibitors."  Biochemistry 48, 4100-4108 (2009).

Assembly members:
DHFR, polymer, 162 residues, 19149.008 Da.
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, non-polymer, 743.405 Da.
5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine, non-polymer, 312.366 Da.

Natural source:   Common Name: anthrax bacteria   Taxonomy ID: 1392   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus anthracis

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

Entity Sequences (FASTA):
DHFR: MIVSFMVAMDENRVIGKDNN LPWRLPSELQYVKKTTMGHP LIMGRKNYEAIGRPLPGRRN IIVTRNEGYHVEGCEVAHSV EEVFELCKNEEEIFIFGGAQ IYDLFLPYVDKLYITKIHHA FEGDTFFPEMDMTNWKEVFV EKGLTDEKNPYTYYYHVYEK QQ

Data sets:
Data typeCount
13C chemical shifts581
15N chemical shifts149
1H chemical shifts638

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DHFR1
2NAP2
3N223

Entities:

Entity 1, DHFR 162 residues - 19149.008 Da.

1   METILEVALSERPHEMETVALALAMETASP
2   GLUASNARGVALILEGLYLYSASPASNASN
3   LEUPROTRPARGLEUPROSERGLULEUGLN
4   TYRVALLYSLYSTHRTHRMETGLYHISPRO
5   LEUILEMETGLYARGLYSASNTYRGLUALA
6   ILEGLYARGPROLEUPROGLYARGARGASN
7   ILEILEVALTHRARGASNGLUGLYTYRHIS
8   VALGLUGLYCYSGLUVALALAHISSERVAL
9   GLUGLUVALPHEGLULEUCYSLYSASNGLU
10   GLUGLUILEPHEILEPHEGLYGLYALAGLN
11   ILETYRASPLEUPHELEUPROTYRVALASP
12   LYSLEUTYRILETHRLYSILEHISHISALA
13   PHEGLUGLYASPTHRPHEPHEPROGLUMET
14   ASPMETTHRASNTRPLYSGLUVALPHEVAL
15   GLULYSGLYLEUTHRASPGLULYSASNPRO
16   TYRTHRTYRTYRTYRHISVALTYRGLULYS
17   GLNGLN

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

1   NAP

Entity 3, N22 - C17 H20 N4 O2 - 312.366 Da.

1   N22

Samples:

sample_1: DHFR, [U-100% 13C; U-100% 15N], 1 mM; UCP120B 2 mM; NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE 2 mM; EDTA 0.5 mM; DTT 10 mM; potassium chloride 50 mM; TES 20 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAL17957 BAR77036 BAR84614 GAE38630 GAE97667
EMBL CCW07550 CDN35653 CGF82795 CGG65241 CIZ56348
GB AAP09158 AAP26114 AAS41186 AAT31357 AAT40581
REF NP_831957 NP_844628 WP_000637196 WP_000637197 WP_000637198

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts