BMRB Entry 16442
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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/BMR16442
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Title: Solution structure of At3g03773.1 protein from Arabidopsis thaliana
Deposition date: 2009-08-05 Original release date: 2010-09-03
Authors: Sahu, Sarata; Singh, Shanteri; Tonelli, Marco; Markley, John
Citation: Sahu, Sarata; Singh, Shanteri; Tonelli, Marco; Markley, John. "Solution structure of At3g03773.1 protein from Arabidopsis thaliana" Structure ., .-..
Assembly members:
At3g03773.1, polymer, 150 residues, 17342.326 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):
At3g03773.1: SSRNPEVLWAQRSDKVYLTV
ALPDAKDISVKCEPQGLFSF
SALGAQGERFEFSLELYGKI
MTEYRKNVGLRNIIFSIQKE
ERSWWTRLLKSEEKPAPYIK
VDWNKWCDEDEEVNSETASD
DESAFVNQDSESSDDDGLLY
LPDLEKARNK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 536 |
15N chemical shifts | 140 |
1H chemical shifts | 1052 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | At3g03773.1 | 1 |
Entities:
Entity 1, At3g03773.1 150 residues - 17342.326 Da.
1 | SER | SER | ARG | ASN | PRO | GLU | VAL | LEU | TRP | ALA | |
2 | GLN | ARG | SER | ASP | LYS | VAL | TYR | LEU | THR | VAL | |
3 | ALA | LEU | PRO | ASP | ALA | LYS | ASP | ILE | SER | VAL | |
4 | LYS | CYS | GLU | PRO | GLN | GLY | LEU | PHE | SER | PHE | |
5 | SER | ALA | LEU | GLY | ALA | GLN | GLY | GLU | ARG | PHE | |
6 | GLU | PHE | SER | LEU | GLU | LEU | TYR | GLY | LYS | ILE | |
7 | MET | THR | GLU | TYR | ARG | LYS | ASN | VAL | GLY | LEU | |
8 | ARG | ASN | ILE | ILE | PHE | SER | ILE | GLN | LYS | GLU | |
9 | GLU | ARG | SER | TRP | TRP | THR | ARG | LEU | LEU | LYS | |
10 | SER | GLU | GLU | LYS | PRO | ALA | PRO | TYR | ILE | LYS | |
11 | VAL | ASP | TRP | ASN | LYS | TRP | CYS | ASP | GLU | ASP | |
12 | GLU | GLU | VAL | ASN | SER | GLU | THR | ALA | SER | ASP | |
13 | ASP | GLU | SER | ALA | PHE | VAL | ASN | GLN | ASP | SER | |
14 | GLU | SER | SER | ASP | ASP | ASP | GLY | LEU | LEU | TYR | |
15 | LEU | PRO | ASP | LEU | GLU | LYS | ALA | ARG | ASN | LYS |
Samples:
sample_1: entity, [U-13C; U-15N], 1 ± 0.1 mM; H2O 93%; H2O 7%
sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 298 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
XEASY, Bartels et al. - chemical shift assignment
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
PDB | |
GB | AAT41786 AAT68743 AAT68744 AAT70471 AAX55169 |
REF | NP_001154589 NP_683525 |
SP | Q6ID70 |
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