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 19849

Title: Solution structure of reduced BolA2 from Arabidopsis thaliana   PubMed: 25012657

Deposition date: 2014-03-13 Original release date: 2014-07-21

Authors: RORET, THOMAS; TSAN, PASCALE; COUTURIER, JEREMY; ROUHIER, NICOLAS; DIDIERJEAN, CLAUDE

Citation: Roret, Thomas; Tsan, Pascale; Couturier, Jeremy; Zhang, Bo; Johnson, Michael; Rouhier, Nicolas; Didierjean, Claude. "Structural and Spectroscopic Insights into BolA-Glutaredoxin Complexes."  J. Biol. Chem. 289, 24588-24598 (2014).

Assembly members:
BolA2, polymer, 93 residues, 10389.931 Da.

Natural source:   Common Name: Thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

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

Entity Sequences (FASTA):
BolA2: MVTKEQVEASLTSKLKPIHL EVIDISGGCGSSFEVEVVSE QFEGKRLLERHRMVNAALEE EMKEIHALSIKKAQTPQQWK PPSQDSATLTKDA

Data sets:
Data typeCount
1H chemical shifts445
13C chemical shifts244
15N chemical shifts95

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1reduced BolA2 from Arabidopsis thaliana1

Entities:

Entity 1, reduced BolA2 from Arabidopsis thaliana 93 residues - 10389.931 Da.

1   METVALTHRLYSGLUGLNVALGLUALASER
2   LEUTHRSERLYSLEULYSPROILEHISLEU
3   GLUVALILEASPILESERGLYGLYCYSGLY
4   SERSERPHEGLUVALGLUVALVALSERGLU
5   GLNPHEGLUGLYLYSARGLEULEUGLUARG
6   HISARGMETVALASNALAALALEUGLUGLU
7   GLUMETLYSGLUILEHISALALEUSERILE
8   LYSLYSALAGLNTHRPROGLNGLNTRPLYS
9   PROPROSERGLNASPSERALATHRLEUTHR
10   LYSASPALA

Samples:

sample_1: BolA2, [U-100% 13C; U-100% 15N], 0.9 mM; phosphate buffer 50 mM; azide 0.02%; H2O 90%; D2O 10%

sample_2: BolA2, [U-100% 15N], 0.9 mM; phosphate buffer 50 mM; azide 0.02%; 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
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

ARIA v2.3, Linge, O, . - chemical shift assignment, refinement, structure solution

CcpNmr, CCPN - data analysis, peak picking

NMRView, Johnson, One Moon Scientific - peak picking

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAB09404 BAF00125
GB AAM65194 AAO24583 AED91453 EFH49685
REF NP_568217 XP_002873426
SP Q9FIC3

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