BMRB Entry 18018
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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/BMR18018
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Title: NMR structure of the putative ATPase regulatory protein YP_916642.1 from Paracoccus denitrificans
Deposition date: 2011-10-24 Original release date: 2011-11-29
Authors: Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; Morales-Rios, Edga; Zarco-Zavala, Mariel; Garcia-Trejo, Jose; Dutta, Samit; JCSG, JCSG
Citation: Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; Dutta, Samit; Morales-Rios, Edga; Garcia-Trejo, Jose; Zarco-Zavala, Mariel. "NMR structure of the putative ATPase regulatory protein YP_916642.1 from Paracoccus denitrificans" Not known ., .-..
Assembly members:
entity, polymer, 104 residues, 11687.060 Da.
Natural source: Common Name: Paracoccus denitrificans Taxonomy ID: 266 Superkingdom: Bacteria Kingdom: not available Genus/species: Paracoccus denitrificans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MTTFDDRERAHEAKFAHDAE
LNFKAEARRNRLLGEWAAGL
LGKTGDDARAYALTVVTSDF
DEPGDEDVFRKLAADLEGKA
DEETIRAKMVELRATAREQI
ISEI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 360 |
| 15N chemical shifts | 98 |
| 1H chemical shifts | 593 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YP_916642.1 | 1 |
Entities:
Entity 1, YP_916642.1 104 residues - 11687.060 Da.
| 1 | MET | THR | THR | PHE | ASP | ASP | ARG | GLU | ARG | ALA | ||||
| 2 | HIS | GLU | ALA | LYS | PHE | ALA | HIS | ASP | ALA | GLU | ||||
| 3 | LEU | ASN | PHE | LYS | ALA | GLU | ALA | ARG | ARG | ASN | ||||
| 4 | ARG | LEU | LEU | GLY | GLU | TRP | ALA | ALA | GLY | LEU | ||||
| 5 | LEU | GLY | LYS | THR | GLY | ASP | ASP | ALA | ARG | ALA | ||||
| 6 | TYR | ALA | LEU | THR | VAL | VAL | THR | SER | ASP | PHE | ||||
| 7 | ASP | GLU | PRO | GLY | ASP | GLU | ASP | VAL | PHE | ARG | ||||
| 8 | LYS | LEU | ALA | ALA | ASP | LEU | GLU | GLY | LYS | ALA | ||||
| 9 | ASP | GLU | GLU | THR | ILE | ARG | ALA | LYS | MET | VAL | ||||
| 10 | GLU | LEU | ARG | ALA | THR | ALA | ARG | GLU | GLN | ILE | ||||
| 11 | ILE | SER | GLU | ILE |
Samples:
sample_1: YP_916642.1, [U-98% 13C; U-98% 15N], 1.5 mM; sodium chloride 50 mM; sodium phosphate 25 mM; sodium azide 5 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.083 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY HACACONH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, G ntert P. - refinement
UNIO, Unio Herrmann Wuthrich - chemical shift assignment, structure solution
TOPSPIN, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
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