BMRB Entry 34105

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34105
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Dehydroascorbate reductase 3A from Populus trichocarpa complexed with GSH.
Deposition date:
2017-02-27
Original release date:
2017-03-09
Authors:
Roret, T.; Tsan, P.
Citation:

Citation: Lallement, P.; Roret, T.; Tsan, P.; Gualberto, J.; Girardet, J.; Didierjean, C.; Rouhier, N.; Hecker, A.. "Insights into ascorbate regeneration in plants: investigating the redox and structural properties of dehydroascorbate reductases from Populus trichocarpa."  Biochem. J. 473, 717-731 (2016).
PubMed: 26699905

Assembly members:

Assembly members:
entity_1, polymer, 218 residues, 24364.195 Da.
entity_GSH, non-polymer, 307.323 Da.

Natural source:

Natural source:   Common Name: Western balsam poplar   Taxonomy ID: 3694   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Populus trichocarpa

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MALEICVKAAVGAPNILGDC PFCQRVLLSLEEKKIPYKSH LINLGDKPQWFLEISPEGKV PVVKIDDKWVADSDVIVGIL EEKNPEPPLATPPEFASVGS KIFPSFVKFLKSKDPNDGTE QALLEELKALDGHLKVHGPF IAGEKITAVDLSLAPKLYHL EVALGHFKNWPIPDNLTHVL NYIKLLFSRESFKKTRAAEE HVIAGWEPKVNAHHHHHH

Data sets:
Data typeCount
15N chemical shifts376
1H chemical shifts376

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 218 residues - 24364.195 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   ASNALAHISHISHISHISHISHIS

Entity 2, entity_2 - C10 H17 N3 O6 S - 307.323 Da.

1   GSH

Samples:

sample_1: Dehydroascorbate reductase, [U-100% 15N], 0.37 mM

sample_2: Dehydroascorbate reductase, [U-100% 15N], 0.37 mM; GLUTATHIONE 74.0 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

Software:

YASARA, YASARA - refinement

AutoDock, AutoDock - structure calculation

CcpNMR, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

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