Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52109
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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:
entity_1, polymer, 133 residues, 14370.27 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 Vector: pET28a Novagen
Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH
NQTSLYKKAGCMMGSVELNL
RETELCLGLPGGDTVAPVTG
NKRGFSETVDLKLNLNNEPA
NKEGSTTHDVVTFDSKEKSA
CPKDPAKPPAKAQVVGWPPV
RSYRKNVMVSCQK
Data type | Count |
13C chemical shifts | 615 |
15N chemical shifts | 225 |
1H chemical shifts | 213 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | IAA17/AXR3 N-terminal half, chain A | 1 |
2 | IAA17/AXR3 N-terminal half, chain B | 1 |
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 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
3 | ASN | GLN | THR | SER | LEU | TYR | LYS | LYS | ALA | GLY | ||||
4 | CYS | MET | MET | GLY | SER | VAL | GLU | LEU | ASN | LEU | ||||
5 | ARG | GLU | THR | GLU | LEU | CYS | LEU | GLY | LEU | PRO | ||||
6 | GLY | GLY | ASP | THR | VAL | ALA | PRO | VAL | THR | GLY | ||||
7 | ASN | LYS | ARG | GLY | PHE | SER | GLU | THR | VAL | ASP | ||||
8 | LEU | LYS | LEU | ASN | LEU | ASN | ASN | GLU | PRO | ALA | ||||
9 | ASN | LYS | GLU | GLY | SER | THR | THR | HIS | ASP | VAL | ||||
10 | VAL | THR | PHE | ASP | SER | LYS | GLU | LYS | SER | ALA | ||||
11 | CYS | PRO | LYS | ASP | PRO | ALA | LYS | PRO | PRO | ALA | ||||
12 | LYS | ALA | GLN | VAL | VAL | GLY | TRP | PRO | PRO | VAL | ||||
13 | ARG | SER | TYR | ARG | LYS | ASN | VAL | MET | VAL | SER | ||||
14 | CYS | GLN | LYS |
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
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNcoCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCACONH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
2D CON | sample_1 | isotropic | sample_conditions_1 |
2D CACO | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D CAnCO | sample_1 | isotropic | sample_conditions_1 |
CCPN Assign v2.4 - chemical shift assignment
NMRPipe vunknown - chemical shift assignment
TAIR | AT1G04250 |
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