BMRB Entry 15607
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15607
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Takeda, Mitsuhiro; Sugimori, Nozomi; Torizawa, Takuya; Terauchi, Tsutomu; Ono, Akira; Yagi, Hirokazu; Yamaguchi, Yoshiki; Kato, Koichi; Ikeya, Teppei; Jee, Jungoo; Guntert, Peter; Aceti, David; Markley, John; Kainosho, Masatsune. "Structure of the putative 32 kDa myrosinase-binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR." FEBS J. 275, 5873-5884 (2008).
PubMed: 19021763
Assembly members:
At3g16450.1, polymer, 299 residues, 31936.729 Da.
Natural source: Common Name: not available Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free Vector: pIVEX2.3d
Entity Sequences (FASTA):
At3g16450.1: AQKVEAGGGAGGASWDDGVH
DGVRKVHVGQGQDGVSSINV
VYAKDSQDVEGGEHGKKTLL
GFETFEVDADDYIVAVQVTY
DNVFGQDSDIITSITFNTFK
GKTSPPYGLETQKKFVLKDK
NGGKLVGFHGRAGEALYALG
AYFATTTTPVTPAKKLSAIG
GDEGTAWDDGAYDGVKKVYV
GQGQDGISAVKFEYNKGAEN
IVGGEHGKPTLLGFEEFEID
YPSEYITAVEGTYDKIFGSD
GLIITMLRFKTNKQTSAPFG
LEAGTAFELKEEGHKIVGFH
GKASELLHQFGVHVMPLTN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 766 |
| 15N chemical shifts | 300 |
| 1H chemical shifts | 1397 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | At3g16450 | 1 |
Entities:
Entity 1, At3g16450 299 residues - 31936.729 Da.
| 1 | ALA | GLN | LYS | VAL | GLU | ALA | GLY | GLY | GLY | ALA | ||||
| 2 | GLY | GLY | ALA | SER | TRP | ASP | ASP | GLY | VAL | HIS | ||||
| 3 | ASP | GLY | VAL | ARG | LYS | VAL | HIS | VAL | GLY | GLN | ||||
| 4 | GLY | GLN | ASP | GLY | VAL | SER | SER | ILE | ASN | VAL | ||||
| 5 | VAL | TYR | ALA | LYS | ASP | SER | GLN | ASP | VAL | GLU | ||||
| 6 | GLY | GLY | GLU | HIS | GLY | LYS | LYS | THR | LEU | LEU | ||||
| 7 | GLY | PHE | GLU | THR | PHE | GLU | VAL | ASP | ALA | ASP | ||||
| 8 | ASP | TYR | ILE | VAL | ALA | VAL | GLN | VAL | THR | TYR | ||||
| 9 | ASP | ASN | VAL | PHE | GLY | GLN | ASP | SER | ASP | ILE | ||||
| 10 | ILE | THR | SER | ILE | THR | PHE | ASN | THR | PHE | LYS | ||||
| 11 | GLY | LYS | THR | SER | PRO | PRO | TYR | GLY | LEU | GLU | ||||
| 12 | THR | GLN | LYS | LYS | PHE | VAL | LEU | LYS | ASP | LYS | ||||
| 13 | ASN | GLY | GLY | LYS | LEU | VAL | GLY | PHE | HIS | GLY | ||||
| 14 | ARG | ALA | GLY | GLU | ALA | LEU | TYR | ALA | LEU | GLY | ||||
| 15 | ALA | TYR | PHE | ALA | THR | THR | THR | THR | PRO | VAL | ||||
| 16 | THR | PRO | ALA | LYS | LYS | LEU | SER | ALA | ILE | GLY | ||||
| 17 | GLY | ASP | GLU | GLY | THR | ALA | TRP | ASP | ASP | GLY | ||||
| 18 | ALA | TYR | ASP | GLY | VAL | LYS | LYS | VAL | TYR | VAL | ||||
| 19 | GLY | GLN | GLY | GLN | ASP | GLY | ILE | SER | ALA | VAL | ||||
| 20 | LYS | PHE | GLU | TYR | ASN | LYS | GLY | ALA | GLU | ASN | ||||
| 21 | ILE | VAL | GLY | GLY | GLU | HIS | GLY | LYS | PRO | THR | ||||
| 22 | LEU | LEU | GLY | PHE | GLU | GLU | PHE | GLU | ILE | ASP | ||||
| 23 | TYR | PRO | SER | GLU | TYR | ILE | THR | ALA | VAL | GLU | ||||
| 24 | GLY | THR | TYR | ASP | LYS | ILE | PHE | GLY | SER | ASP | ||||
| 25 | GLY | LEU | ILE | ILE | THR | MET | LEU | ARG | PHE | LYS | ||||
| 26 | THR | ASN | LYS | GLN | THR | SER | ALA | PRO | PHE | GLY | ||||
| 27 | LEU | GLU | ALA | GLY | THR | ALA | PHE | GLU | LEU | LYS | ||||
| 28 | GLU | GLU | GLY | HIS | LYS | ILE | VAL | GLY | PHE | HIS | ||||
| 29 | GLY | LYS | ALA | SER | GLU | LEU | LEU | HIS | GLN | PHE | ||||
| 30 | GLY | VAL | HIS | VAL | MET | PRO | LEU | THR | ASN |
Samples:
sample_1: At3g16450.1, stereo-array isotope labeling (SAIL), 0.2 mM; potassium chloride 100 mM; bis-TRIS-d19, [U-99% 2H], 20 mM; D2O, [U-100% 2H], 10%; H2O 90%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 bar; temperature: 300.65 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.2, Guntert, Mumenthaler and Wuthrich - structure solution
CYANA, Goddard - chemical shift assignment
OPALP v1.4, (OPALP) Koradi, Billeter, Guntert - refinement
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAB01144 BAH20032 |
| GB | AAB63632 AAK55736 AAM65267 AAM91376 AEE75817 |
| REF | NP_001030711 NP_188266 NP_850596 |
| SP | O04311 |
| AlphaFold | O04311 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks