BMRB Entry 52109

Title:
Chemical shifts for IAA17/AXR3 N-terminal
Deposition date:
2023-09-01
Original release date:
2023-09-29
Authors:
Ramans-Harborough, Sigurd; Kalverda, Arnout; Manfield, Iain; Thompson, Gary; Kieffer, Martin; Uzunova, Veselina; Quareshy, Mussa; Prusinska, Justyna; Roychoudhry, Suruchi; Hayashi, Ken-ichiro; Napier, Richard; de Genio, Charo; Kepinski, Stephan
Citation:

Citation: Ramans-Harborough, Sigurd; Kalverda, Arnout; Manfield, Iain; Thompson, Gary; Kieffer, Martin; Uzunova, Veselina; Quareshy, Mussa; Prusinska, Justyna; Roychoudhry, Suruchi; Hayashi, Ken-ichiro; Napier, Richard; del Genio, Charo; Kepinski, Stefan. "Intrinsic disorder and conformational coexistence in auxin coreceptors"  Proc. Natl. Acad. Sci. U. S. A. 120, e2221286120-e2221286120 (2023).
PubMed: 37756337

Assembly members:

Assembly members:
entity_1, polymer, 133 residues, 14370.27 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: pET28a Novagen

Data sets:
Data typeCount
13C chemical shifts615
15N chemical shifts225
1H chemical shifts213

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IAA17/AXR3 N-terminal half, chain A1
2IAA17/AXR3 N-terminal half, chain B1

Entities:

Entity 1, IAA17/AXR3 N-terminal half, chain A 133 residues - 14370.27 Da.

The sequence in the deposition starts at -30 Two sets of chemical shifts are reported for around Residue 87 (PRO) chain A 87 trans chain B 87 cis

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   ASNGLNTHRSERLEUTYRLYSLYSALAGLY
4   CYSMETMETGLYSERVALGLULEUASNLEU
5   ARGGLUTHRGLULEUCYSLEUGLYLEUPRO
6   GLYGLYASPTHRVALALAPROVALTHRGLY
7   ASNLYSARGGLYPHESERGLUTHRVALASP
8   LEULYSLEUASNLEUASNASNGLUPROALA
9   ASNLYSGLUGLYSERTHRTHRHISASPVAL
10   VALTHRPHEASPSERLYSGLULYSSERALA
11   CYSPROLYSASPPROALALYSPROPROALA
12   LYSALAGLNVALVALGLYTRPPROPROVAL
13   ARGSERTYRARGLYSASNVALMETVALSER
14   CYSGLNLYS

Samples:

sample_1: IAA17/AXR3 N-terminal half, [U-99% 13C; U-99% 15N], 290 uM; D2O 5%; NaxPO3 20 mM; NaCl 150 mM; EDTA 3 mM; DTT 10 mM; protease inhibitor cocktail 2 % v/v

sample_conditions_1: ionic strength: 210 mM; pH: 6.0; pressure: 1 atm; temperature: 289.6 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNcoCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
2D CACOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D CAnCOsample_1isotropicsample_conditions_1

Software:

CCPN Assign v2.4 - chemical shift assignment

NMRPipe vunknown - chemical shift assignment

NMR spectrometers:

  • Agilent DDX3 600 MHz
  • Bruker AVIII HD 950 MHz

Related Database Links:

TAIR AT1G04250

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