BMRB Entry 16355
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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/BMR16355
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Title: NMR Solution Structure of a Putative Uncharacterized Protein obtained from Arabidopsis thaliana: Northeast Structural Genomics Consortium target AR3449A
Deposition date: 2009-06-16 Original release date: 2012-02-22
Authors: Mani, Rajeswari; Gurla, Swapna; Shastry, Ritu; Ciccosanti, Colleen; Foote, Erica; Jiang, Mei; Xiao, Rong; Nair, Rajesh; Everett, John; Huang, Yuanpeng; Acton, Tom; Rost, Burkhard; Montelione, Gaetano
Citation: Mani, Rajeswari; Gurla, Swapna; Shastry, Ritu; Ciccosanti, Colleen; Foote, Erica; Jiang, Mei; Xiao, Rong; Nair, Rajesh; Everett, John; Huang, Yuanpeng; Acton, Tom; Rost, Burkhard; Montelione, Gaetano. "NMR Solution Structure of a Putative Uncharacterized Protein obtained from Arabidopsis thaliana: Northeast Structural Genomics Consortium Target AR3449A" Not known ., .-..
Assembly members:
AR3449A, polymer, 84 residues, 9679.103 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):
AR3449A: MGHHHHHHSHMKFLVENLNG
SSFELEVDYRDTLLVVKQKI
ERSQHIPVSKQTLIVDGIVI
LREDLTVEQCQIVPTSDIQL
EVSS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 342 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 552 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AR3449A | 1 |
Entities:
Entity 1, AR3449A 84 residues - 9679.103 Da.
1-10 residues MGHHHHHHSH is a N-terminal tag
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | LYS | PHE | LEU | VAL | GLU | ASN | LEU | ASN | GLY | ||||
| 3 | SER | SER | PHE | GLU | LEU | GLU | VAL | ASP | TYR | ARG | ||||
| 4 | ASP | THR | LEU | LEU | VAL | VAL | LYS | GLN | LYS | ILE | ||||
| 5 | GLU | ARG | SER | GLN | HIS | ILE | PRO | VAL | SER | LYS | ||||
| 6 | GLN | THR | LEU | ILE | VAL | ASP | GLY | ILE | VAL | ILE | ||||
| 7 | LEU | ARG | GLU | ASP | LEU | THR | VAL | GLU | GLN | CYS | ||||
| 8 | GLN | ILE | VAL | PRO | THR | SER | ASP | ILE | GLN | LEU | ||||
| 9 | GLU | VAL | SER | SER |
Samples:
sample_1: AR3449A, [U-100% 13C; U-100% 15N], 1.11 mM; H2O 90%; D2O 10%; sodium azide 0.02%; calcium chloride 5 mM; sodium chloride 10 mM; MES 20 mM; DDT 10 mM
sample_2: AR3449A, [U-10% 13C; U-100% 15N], 1.22 mM; H2O 90%; D2O 10%; sodium azide 0.02%; calcium chloride 5 mM; sodium chloride 10 mM; MES 20 mM; DDT 10 mM
sample_conditions_1: ionic strength: . M; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C aliphatic NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C aromatic NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| (4,3)D GFT-HNNCABCA | sample_1 | isotropic | sample_conditions_1 |
| (4,3)D GFT-CABCA(CO)NHN | sample_1 | isotropic | sample_conditions_1 |
| 3D GFT-HNNCABCA | sample_1 | isotropic | sample_conditions_1 |
| 3D GFT-CABCA(CO)NHN | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
- Varian INOVA 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts