BMRB Entry 17320
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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/BMR17320
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Title: NMR structure of the protein YP_926445.1 from Shewanella Amazonensis
Deposition date: 2010-11-23 Original release date: 2012-07-25
Authors: Serrano, Pedro; Geralt, Michael; Mohanty, Biswaranjan; Horst, Reto; Wuthrich, Kurt
Citation: Serrano, Pedro; Geralt, Michael; Mohanty, Biswaranjan; Horst, Reto; Wuthrich, Kurt. "NMR structure of the protein YP_926445.1 from Shewanella Amazonensis" Not known ., .-..
Assembly members:
YP_926445.1, polymer, 114 residues, 12793.651 Da.
Natural source: Common Name: Shewanella amazonensis Taxonomy ID: 60478 Superkingdom: Bacteria Kingdom: not available Genus/species: Shewanella amazonensis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
YP_926445.1: MGAGQTPHPQLIWPALLKQQ
GCNELLPLRTNDDWQRFCAD
SKHLLQYGDKLVDSNFHCFV
LEEDAHWHPAAPLPPEGLND
LIRAHCATLGHCCTSKMHLH
SVMDAIDFLNALEG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 385 |
| 15N chemical shifts | 119 |
| 1H chemical shifts | 785 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YP_926445.1 | 1 |
Entities:
Entity 1, YP_926445.1 114 residues - 12793.651 Da.
| 1 | MET | GLY | ALA | GLY | GLN | THR | PRO | HIS | PRO | GLN | ||||
| 2 | LEU | ILE | TRP | PRO | ALA | LEU | LEU | LYS | GLN | GLN | ||||
| 3 | GLY | CYS | ASN | GLU | LEU | LEU | PRO | LEU | ARG | THR | ||||
| 4 | ASN | ASP | ASP | TRP | GLN | ARG | PHE | CYS | ALA | ASP | ||||
| 5 | SER | LYS | HIS | LEU | LEU | GLN | TYR | GLY | ASP | LYS | ||||
| 6 | LEU | VAL | ASP | SER | ASN | PHE | HIS | CYS | PHE | VAL | ||||
| 7 | LEU | GLU | GLU | ASP | ALA | HIS | TRP | HIS | PRO | ALA | ||||
| 8 | ALA | PRO | LEU | PRO | PRO | GLU | GLY | LEU | ASN | ASP | ||||
| 9 | LEU | ILE | ARG | ALA | HIS | CYS | ALA | THR | LEU | GLY | ||||
| 10 | HIS | CYS | CYS | THR | SER | LYS | MET | HIS | LEU | HIS | ||||
| 11 | SER | VAL | MET | ASP | ALA | ILE | ASP | PHE | LEU | ASN | ||||
| 12 | ALA | LEU | GLU | GLY |
Samples:
sample_1: sodium phosphate 20 mM; sodium chloride 50 mM; DTT 8 mM; sodium azide 4.5 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.113 M; pH: 6.5; 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (ali) | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY (Aro) | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY-HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
OPALp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
TOPSPIN v2.1, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
UNIO, Herrmann and Wuthrich - chemical shift assignment, peak picking, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts