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 18870

Title: Solution structure of the dimerization domain of Aux/IAA transcription factor Ps-IAA4 from pea (Pisum sativum)

Deposition date: 2012-12-03 Original release date: 2013-12-02

Authors: Kovermann, Michael; Dhurvas Chandrasekaran, Dinesh; Gopalswamy, Mohanraj; Abel, Steffen; Balbach, Jochen

Citation: Dhurvas Chandrasekaran, Dinesh; Kovermann, Michael; Gopalswamy, Mohanraj; Balbach, Jochen; Abel, Steffen. "Solution structure of the dimerization domain of Aux/IAA transcription factor Ps-IAA4 from pea (Pisum sativum)"  Not known ., .-..

Assembly members:
PsIAA4_DIII/IV, polymer, 107 residues, 11938.721 Da.

Natural source:   Common Name: garden pea   Taxonomy ID: 3888   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Pisum sativum

Experimental source:   Production method: recombinant technology   Host organism: Pisum sativum

Entity Sequences (FASTA):
PsIAA4_DIII/IV: HEADVGGIFVKVSMDGAPYL RKIDLRVYGGYSELLKALET MFKLTIGEYSEREGYKGSEY APTYEDKDGDWMLVGDVPWD MFVTSCKRLRIMKGTEAKGL GCGVGSH

Data sets:
Data typeCount
13C chemical shifts399
15N chemical shifts104
1H chemical shifts629

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PsIAA4_DIII/IV1

Entities:

Entity 1, PsIAA4_DIII/IV 107 residues - 11938.721 Da.

86-189 aa

1   HISGLUALAASPVALGLYGLYILEPHEVAL
2   LYSVALSERMETASPGLYALAPROTYRLEU
3   ARGLYSILEASPLEUARGVALTYRGLYGLY
4   TYRSERGLULEULEULYSALALEUGLUTHR
5   METPHELYSLEUTHRILEGLYGLUTYRSER
6   GLUARGGLUGLYTYRLYSGLYSERGLUTYR
7   ALAPROTHRTYRGLUASPLYSASPGLYASP
8   TRPMETLEUVALGLYASPVALPROTRPASP
9   METPHEVALTHRSERCYSLYSARGLEUARG
10   ILEMETLYSGLYTHRGLUALALYSGLYLEU
11   GLYCYSGLYVALGLYSERHIS

Samples:

sample_1: PsIAA4_DIII/IV, [U-98% 13C; U-98% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; magnesium chloride 2 mM; DTT 1 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.112 M; pH: 2.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.3, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - data analysis

ARIA, Linge, O, . - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UniProtKB P49679
PDB
EMBL CAA48297 CAA48298
SP P49679

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