BMRB Entry 19850

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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/BMR19850
MolProbity Validation Chart

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Title:
NMR-based docking model of GrxS14-BolA2 apo-heterodimer from Arabidopsis thaliana
Deposition date:
2014-03-13
Original release date:
2014-07-21
Authors:
RORET, THOMAS; TSAN, PASCALE; COUTURIER, JEREMY; ROUHIER, NICOLAS; DIDIERJEAN, CLAUDE
Citation:

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).
PubMed: 25012657

Assembly members:

Assembly members:
GrxS14, polymer, 109 residues, 12196.089 Da.
BolA2, polymer, 80 residues, 9042.453 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GrxS14: SALTPQLKDTLEKLVNSEKV VLFMKGTRDFPMCGFSNTVV QILKNLNVPFEDVNILENEM LRQGLKEYSNWPTFPQLYIG GEFFGGCDITLEAFKTGELQ EEVEKAMCS
BolA2: VTKEQVEASLTSKLKPIHLE VIDISGGCGSSFEVEVVSEQ FEGKRLLERHRMVNAALEEE MKEIHALSIKKAQTPQQWKP

Data typeCount
1H chemical shifts356
15N chemical shifts356

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1GrxS141
2BolA22

Entities:

Entity 1, GrxS14 109 residues - 12196.089 Da.

1   SERALALEUTHRPROGLNLEULYSASPTHR
2   LEUGLULYSLEUVALASNSERGLULYSVAL
3   VALLEUPHEMETLYSGLYTHRARGASPPHE
4   PROMETCYSGLYPHESERASNTHRVALVAL
5   GLNILELEULYSASNLEUASNVALPROPHE
6   GLUASPVALASNILELEUGLUASNGLUMET
7   LEUARGGLNGLYLEULYSGLUTYRSERASN
8   TRPPROTHRPHEPROGLNLEUTYRILEGLY
9   GLYGLUPHEPHEGLYGLYCYSASPILETHR
10   LEUGLUALAPHELYSTHRGLYGLULEUGLN
11   GLUGLUVALGLULYSALAMETCYSSER

Entity 2, BolA2 80 residues - 9042.453 Da.

1   VALTHRLYSGLUGLNVALGLUALASERLEU
2   THRSERLYSLEULYSPROILEHISLEUGLU
3   VALILEASPILESERGLYGLYCYSGLYSER
4   SERPHEGLUVALGLUVALVALSERGLUGLN
5   PHEGLUGLYLYSARGLEULEUGLUARGHIS
6   ARGMETVALASNALAALALEUGLUGLUGLU
7   METLYSGLUILEHISALALEUSERILELYS
8   LYSALAGLNTHRPROGLNGLNTRPLYSPRO

Samples:

sample_1: BolA2, [U-100% 15N], 0.12 mM; GrxS140.012 – 0.24 mM; phosphate buffer 50 mM; azide 0.02%; H2O 90%; D2O 10%

sample_2: GrxS14, [U-100% 15N], 0.12 mM; BolA20.012 – 0.24 mM; phosphate buffer 50 mM; azide 0.02%; H2O 90%; D2O 10%

sample_3: GrxS14, [U-100% 15N], 0.12 mM; phosphate buffer 50 mM; azide 0.02%; H2O 90%; D2O 10%

sample_4: BolA2, [U-100% 15N], 0.12 mM; phosphate buffer 50 mM; azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

GRAMM-X_Protein-Protein_Docking_Web_Server v1.2.0, Tovchigrechko A - structure solution

YASARA_Energy_Minimization_Server, KRIEGER - geometry optimization, refinement

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

UNP Q84Y95 Q9FIC3
PDB
EMBL CAB41094 CDX69884 CDY21608
GB AAK60300 AAL77721 AAO19647 AEE79309 EFH54264 AAM65194 AAO24583 AED91453 EFH49685 KFK25275
REF NP_191050 XP_002878005 XP_002883576 XP_002893837 NP_568217 XP_002873426 XP_009122117 XP_010491626
SP Q84Y95
BMRB 19849
DBJ BAB09404 BAF00125
AlphaFold Q9SV38 Q84Y95 Q9FIC3

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