BMRB Entry 16101
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16101
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Title: NMR solution Structure of O64736 protein from Arabidopsis thaliana:Northeast Structural Genomics Consortium MEGA Target AR3445A
Deposition date: 2008-12-31 Original release date: 2009-02-19
Authors: G. V. T., Swapna; Shastry, Ritu; Foote, E. L.; Ciccosanti, Colleen; Jiang, Mei; Xiao, Rong; Nair, R; Everett, John; Huang, Yuanpeng; Acton, Thomas; Rost, B.; Montelione, Gaetano
Citation: G. V. T., Swapna; Montelione, Gaetano. "NMR solution structure of O64736 protein from Arabidopsis thaliana" Not known ., .-..
Assembly members:
AR3445A, polymer, 85 residues, 9196.865 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):
AR3445A: MGHHHHHHSHSTIKLTVKFG
GKSIPLSVSPDCTVKDLKSQ
LQPITNVLPRGQKLIFKGKV
LVETSTLKQSDVGSGAKLML
MASQG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 342 |
| 15N chemical shifts | 76 |
| 1H chemical shifts | 560 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AR3445A | 1 |
Entities:
Entity 1, AR3445A 85 residues - 9196.865 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | SER | THR | ILE | LYS | LEU | THR | VAL | LYS | PHE | GLY | ||||
| 3 | GLY | LYS | SER | ILE | PRO | LEU | SER | VAL | SER | PRO | ||||
| 4 | ASP | CYS | THR | VAL | LYS | ASP | LEU | LYS | SER | GLN | ||||
| 5 | LEU | GLN | PRO | ILE | THR | ASN | VAL | LEU | PRO | ARG | ||||
| 6 | GLY | GLN | LYS | LEU | ILE | PHE | LYS | GLY | LYS | VAL | ||||
| 7 | LEU | VAL | GLU | THR | SER | THR | LEU | LYS | GLN | SER | ||||
| 8 | ASP | VAL | GLY | SER | GLY | ALA | LYS | LEU | MET | LEU | ||||
| 9 | MET | ALA | SER | GLN | GLY |
Samples:
sample_1: sample_1, [U-100% 13C; U-100% 15N], 1.8 ± 0.1 mM; CaCL2 5.0 mM; NACL 200 mM
sample_2: sample_2, [U-10% 13C; U-100% 15N], 1.80 ± 0.1 mM; CaCL2 5.0 mM; NACL 200 mM
sample_conditions_1: ionic strength: 205 M; pH: 6.5; pressure: 1.0 atm; temperature: 293 K
sample_conditions_2: ionic strength: 205 M; pH: 6.5; pressure: 1.0 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHANH | 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis
AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
SPARKY v3.1, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts