BMRB Entry 15295
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15295
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Title: Solution structure At3g28950.1 from Arabidopsis thaliana PubMed: 18214976
Deposition date: 2007-06-07 Original release date: 2007-08-15
Authors: Volkman, B.; de la Cruz, N.; Peterson, F.
Citation: de la Cruz, N.; Peterson, F.; Volkman, B.. "Solution structure of At3g28950 from Arabidopsis thaliana" Proteins 71, 546-551 (2008).
Assembly members:
At3g28950.1, polymer, 165 residues, 18603.959 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
Entity Sequences (FASTA):
At3g28950.1: STSSDPQSHNVFVYGSILEP
AVAAVILDRTADTVPAVLHG
YHRYKLKGLPYPCIVSSDSG
KVNGKVITGVSDAELNNFDV
IEGNDYERVTVEVVRMDNSE
KVKVETYVWVNKDDPRMYGE
WDFEEWRVVHAEKFVETFRK
MLEWNKNPNGKSMEEAVGSL
LSSGD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 612 |
| 15N chemical shifts | 149 |
| 1H chemical shifts | 929 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | At3g28950.1 | 1 |
Entities:
Entity 1, At3g28950.1 165 residues - 18603.959 Da.
| 1 | SER | THR | SER | SER | ASP | PRO | GLN | SER | HIS | ASN | ||||
| 2 | VAL | PHE | VAL | TYR | GLY | SER | ILE | LEU | GLU | PRO | ||||
| 3 | ALA | VAL | ALA | ALA | VAL | ILE | LEU | ASP | ARG | THR | ||||
| 4 | ALA | ASP | THR | VAL | PRO | ALA | VAL | LEU | HIS | GLY | ||||
| 5 | TYR | HIS | ARG | TYR | LYS | LEU | LYS | GLY | LEU | PRO | ||||
| 6 | TYR | PRO | CYS | ILE | VAL | SER | SER | ASP | SER | GLY | ||||
| 7 | LYS | VAL | ASN | GLY | LYS | VAL | ILE | THR | GLY | VAL | ||||
| 8 | SER | ASP | ALA | GLU | LEU | ASN | ASN | PHE | ASP | VAL | ||||
| 9 | ILE | GLU | GLY | ASN | ASP | TYR | GLU | ARG | VAL | THR | ||||
| 10 | VAL | GLU | VAL | VAL | ARG | MET | ASP | ASN | SER | GLU | ||||
| 11 | LYS | VAL | LYS | VAL | GLU | THR | TYR | VAL | TRP | VAL | ||||
| 12 | ASN | LYS | ASP | ASP | PRO | ARG | MET | TYR | GLY | GLU | ||||
| 13 | TRP | ASP | PHE | GLU | GLU | TRP | ARG | VAL | VAL | HIS | ||||
| 14 | ALA | GLU | LYS | PHE | VAL | GLU | THR | PHE | ARG | LYS | ||||
| 15 | MET | LEU | GLU | TRP | ASN | LYS | ASN | PRO | ASN | GLY | ||||
| 16 | LYS | SER | MET | GLU | GLU | ALA | VAL | GLY | SER | LEU | ||||
| 17 | LEU | SER | SER | GLY | ASP |
Samples:
sample: At3g28950.1, [U-100% 13C; U-100% 15N], 0.75 mM; MOPS 10 mM; sodium chloride 100 mM; DTT 5 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D_15N-separated_NOESY | sample | isotropic | sample_conditions_1 |
| 3D_13C-separated_NOESY | sample | isotropic | sample_conditions_1 |
| 3D_13C-separated_NOESY (AROMATIC) | sample | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement
xwinnmr v3.5, Bruker - collection
NMRPipe v2004, Delagio,F. et al. - processing
XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis
SPSCAN v1.1.0, R.W. Glaser - data analysis
GARANT v2.1, C. Bartels - data analysis
CYANA v2.1, Guntert, P. - structural calculation
NMR spectrometers:
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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or all simulated shifts