BMRB Entry 30565
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30565
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Title: Solution structure of the Arabidopsis thaliana RALF8 peptide PubMed: 31004454
Deposition date: 2019-01-30 Original release date: 2019-05-02
Authors: Lee, W.; Markley, J.; Frederick, R.; Miyoshi, H.; Tonelli, M.; Cornilescu, G.; Cornilescu, C.; Sussman, M.
Citation: Frederick, R.; Miyoshi, H.; Tonelli, M.; Lee, W.; Cornilescu, G.; Cornilescu, C.; Sussman, M.; Markley, J.. "NMR Assignments and solution structure of the Arabidopsis thaliana RALF8 peptide" Protein Sci. 28, 1115-1126 (2019).
Assembly members:
entity_1, polymer, 56 residues, 6248.083 Da.
Natural source: Common Name: Mouse-ear cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: EASVRYITYPAIDRGDHAVH
CDKAHPNTCKKKQANPYRRG
CGVLEGCHRETGPKPT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 221 |
| 15N chemical shifts | 50 |
| 1H chemical shifts | 307 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 56 residues - 6248.083 Da.
| 1 | GLU | ALA | SER | VAL | ARG | TYR | ILE | THR | TYR | PRO | ||||
| 2 | ALA | ILE | ASP | ARG | GLY | ASP | HIS | ALA | VAL | HIS | ||||
| 3 | CYS | ASP | LYS | ALA | HIS | PRO | ASN | THR | CYS | LYS | ||||
| 4 | LYS | LYS | GLN | ALA | ASN | PRO | TYR | ARG | ARG | GLY | ||||
| 5 | CYS | GLY | VAL | LEU | GLU | GLY | CYS | HIS | ARG | GLU | ||||
| 6 | THR | GLY | PRO | LYS | PRO | THR |
Samples:
sample_1: Rapid ALkalinization Factor-8 (RALF8), [U-13C; U-15N], 1.0 mM
sample_conditions_1: ionic strength: 200 mM; pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMR, Varian - collection
AUDANA, W. Lee, C.M. Petit, G. Cornilescu, J.L. Stark, J.L. Markley - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SMILE, J. Ying, F. Delaglio, D.A. Torchia, and A. Bax - processing
NMRFAM-SPARKY, W. Lee, M. Tonelli, J.L. Markley - chemical shift assignment, peak picking
I-PINE, W. Lee, A. Bahrami, H. Dashti, H.R. Eghbalnia, M. Tonelli, W.M. Westler, J.L. Markley - chemical shift assignment
TALOS-N, Y. Shen, A. Bax - structure calculation
PECAN, Eghbalnia, Wang, Bahrami, Assadi, and Markley - structure calculation
PONDEROSA-C/S, W. Lee, J.L. Stark, J.L. Markley - refinement, structure calculation
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
NMR spectrometers:
- Varian VNMRS 600 MHz
- Varian VNMRS 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts