BMRB Entry 15791
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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/BMR15791
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Title: Solution NMR Structure of UPF0339 Protein SO3888 from Shewanella Oneidensis. Northeast Structural Genomics Consortium Target SoR190 PubMed: TBA
Deposition date: 2008-05-31 Original release date: 2008-08-08
Authors: Tang, Yuefeng; Wang, Dongyan; Nwosu, Chioma; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation: Tang, Yuefeng; Wang, Dongyan; Nwosu, Chioma; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "Solution NMR Structure of UPF0339 Protein SO3888 from Shewanella Oneidensis." Not known ., .-..
Assembly members:
SoR190, polymer, 118 residues, 13103.730 Da.
Natural source: Common Name: Shewanella Oneidensis Taxonomy ID: 70863 Superkingdom: Bacteria Kingdom: not available Genus/species: Shewanella Oneidensis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SoR190: MSGWYELSKSSNDQFKFVLK
AGNGEVILTSELYTGKSGAM
NGIESVQTNSPIEARYAKEV
AKNDKPYFNLKAANHQIIGT
SQMYSSTAARDNGIKSVMEN
GKTTTIKDLTLEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 471 |
| 15N chemical shifts | 124 |
| 1H chemical shifts | 758 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SoR190 | 1 |
Entities:
Entity 1, SoR190 118 residues - 13103.730 Da.
Residue 111-118 represent a non-native affinity purification tag (LEHHHHHH)
| 1 | MET | SER | GLY | TRP | TYR | GLU | LEU | SER | LYS | SER | ||||
| 2 | SER | ASN | ASP | GLN | PHE | LYS | PHE | VAL | LEU | LYS | ||||
| 3 | ALA | GLY | ASN | GLY | GLU | VAL | ILE | LEU | THR | SER | ||||
| 4 | GLU | LEU | TYR | THR | GLY | LYS | SER | GLY | ALA | MET | ||||
| 5 | ASN | GLY | ILE | GLU | SER | VAL | GLN | THR | ASN | SER | ||||
| 6 | PRO | ILE | GLU | ALA | ARG | TYR | ALA | LYS | GLU | VAL | ||||
| 7 | ALA | LYS | ASN | ASP | LYS | PRO | TYR | PHE | ASN | LEU | ||||
| 8 | LYS | ALA | ALA | ASN | HIS | GLN | ILE | ILE | GLY | THR | ||||
| 9 | SER | GLN | MET | TYR | SER | SER | THR | ALA | ALA | ARG | ||||
| 10 | ASP | ASN | GLY | ILE | LYS | SER | VAL | MET | GLU | ASN | ||||
| 11 | GLY | LYS | THR | THR | THR | ILE | LYS | ASP | LEU | THR | ||||
| 12 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: SoR190, [U-100% 13C; U-100% 15N], 1.3 mM; CaCl2 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; NaN3 0.02%
sample_2: SoR190, [U-5% 13C; U-100% 15N], 1.3 mM; CaCl2 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; NaN3 0.02%
sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 293 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D simutaneous NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY_aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 HCCH-COSY | 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 |
| 2D 1H-13C HSQC_high resolution | sample_2 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection
AutoAssign v2.2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
SPARKY v3.110, Goddard - data analysis, peak picking
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PSVS v1.3, Bhattacharya and Montelione - data analysis
PDBStat v5.0, Tejero and Montelione - PDBanalysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| GB | AAN56863 ABI40290 ABK46978 ABN63039 ADV53245 |
| REF | NP_719419 WP_011073636 WP_011847750 WP_025007863 |
| SP | Q8EAL4 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts