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 25712

Title: Solution structure of the dehydroascorbate reductase 3A from Populus trichocarpa   PubMed: 26699905

Deposition date: 2015-07-15 Original release date: 2016-03-14

Authors: Roret, Thomas; Tsan, Pascale

Citation: Lallement, Pierre-Alexandre; Roret, Thomas; Tsan, Pascale; M. Gualberto, Jose; Girardet, Jean-Michel; Didierjean, Claude; Rouhier, Nicolas; Hecker, Arnaud. "Biochemical and structural characterization of dehydroascorbate reductases from poplar (Populus trichocarpa), enzymes contributing to the maintenance of the ascorbate pool in plants"  Biochem. J. 473, 717-731 (2016).

Assembly members:
Pt-DHAR3A, polymer, 217 residues, 23535.525 Da.

Natural source:   Common Name: black cottonwood   Taxonomy ID: 3694   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Populus trichocarpa

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

Entity Sequences (FASTA):
Pt-DHAR3A: MALEICVKAAVGAPNILGDC PFCQRVLLSLEEKKIPYKSH LINLGDKPQWFLEISPEGKV PVVKIDDKWVADSDVIVGIL EEKNPEPPLATPPEFASVGS KIFPSFVKFLKSKDPNDGTE QALLEELKALDGHLKVHGPF IAGEKITAVDLSLAPKLYHL EVALGHFKNWPIPDNLTHVL NYIKLLFSRESFKKTRAAEE HVIAGWEPKVNAHHHHH

Data sets:
Data typeCount
13C chemical shifts542
15N chemical shifts207
1H chemical shifts1107

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 217 residues - 23535.525 Da.

1   METALALEUGLUILECYSVALLYSALAALA
2   VALGLYALAPROASNILELEUGLYASPCYS
3   PROPHECYSGLNARGVALLEULEUSERLEU
4   GLUGLULYSLYSILEPROTYRLYSSERHIS
5   LEUILEASNLEUGLYASPLYSPROGLNTRP
6   PHELEUGLUILESERPROGLUGLYLYSVAL
7   PROVALVALLYSILEASPASPLYSTRPVAL
8   ALAASPSERASPVALILEVALGLYILELEU
9   GLUGLULYSASNPROGLUPROPROLEUALA
10   THRPROPROGLUPHEALASERVALGLYSER
11   LYSILEPHEPROSERPHEVALLYSPHELEU
12   LYSSERLYSASPPROASNASPGLYTHRGLU
13   GLNALALEULEUGLUGLULEULYSALALEU
14   ASPGLYHISLEULYSVALHISGLYPROPHE
15   ILEALAGLYGLULYSILETHRALAVALASP
16   LEUSERLEUALAPROLYSLEUTYRHISLEU
17   GLUVALALALEUGLYHISPHELYSASNTRP
18   PROILEPROASPASNLEUTHRHISVALLEU
19   ASNTYRILELYSLEULEUPHESERARGGLU
20   SERPHELYSLYSTHRARGALAALAGLUGLU
21   HISVALILEALAGLYTRPGLUPROLYSVAL
22   ASNALAHISHISHISHISHIS

Samples:

sample_1: Pt-DHAR3A, [U-100% 13C; U-100% 15N], 0.7 – 1.3 mM; sodium phosphate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

ARIA vv 2.3, Linge, O'Donoghue and Nilges - refinement, structure solution

CNS vv 1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMRView vv 2.4, Johnson, One Moon Scientific - data analysis

CcpNMR vv 2.4.1, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

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