BMRB Entry 16269
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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/BMR16269
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Title: n-NafY. N-terminal domain of NafY
Deposition date: 2009-05-01 Original release date: 2012-08-06
Authors: Phillips, Aaron; Hernandez, Jose; Erbil, Kaya; Pelton, Jeff; Wemmer, David; Rubio, Luis
Citation: Phillips, Aaron; Hernandez, Jose; Erbil, Kaya; Pelton, Jeff; Wemmer, David; Rubio, Luis. "Biological activity and solution structure of the apo-dinitrogenase binding domain of NafY" Not known ., .-..
Assembly members:
n-NafY, polymer, 98 residues, 10284.854 Da.
Natural source: Common Name: Azotobacter Vinelandii Taxonomy ID: 354 Superkingdom: Bacteria Kingdom: not available Genus/species: Azotobacter Vinelandii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
n-NafY: GHMVTPVNMSRETALRIALA
ARALPGTTVGQLLEILHQRI
EGPLTEESLQGVSVTDLKIG
LAGSEEDVDMLDTPMSALKD
AVRILWGEAEVDSLPQPV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 233 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 514 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | n-NafY | 1 |
Entities:
Entity 1, n-NafY 98 residues - 10284.854 Da.
| 1 | GLY | HIS | MET | VAL | THR | PRO | VAL | ASN | MET | SER | ||||
| 2 | ARG | GLU | THR | ALA | LEU | ARG | ILE | ALA | LEU | ALA | ||||
| 3 | ALA | ARG | ALA | LEU | PRO | GLY | THR | THR | VAL | GLY | ||||
| 4 | GLN | LEU | LEU | GLU | ILE | LEU | HIS | GLN | ARG | ILE | ||||
| 5 | GLU | GLY | PRO | LEU | THR | GLU | GLU | SER | LEU | GLN | ||||
| 6 | GLY | VAL | SER | VAL | THR | ASP | LEU | LYS | ILE | GLY | ||||
| 7 | LEU | ALA | GLY | SER | GLU | GLU | ASP | VAL | ASP | MET | ||||
| 8 | LEU | ASP | THR | PRO | MET | SER | ALA | LEU | LYS | ASP | ||||
| 9 | ALA | VAL | ARG | ILE | LEU | TRP | GLY | GLU | ALA | GLU | ||||
| 10 | VAL | ASP | SER | LEU | PRO | GLN | PRO | VAL |
Samples:
sample_1: n-NafY, [U-100% 13C; U-100% 15N], 1 mM; NaCl 140 mM; KCl 2.7 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM; EDTA 2 mM; NaN3 0.02 % (w/v)
sample_2: n-NafY, [U-100% 13C; U-100% 15N], 1 mM; NaCl 140 mM; KCl 2.7 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM; EDTA 2 mM; NaN3 0.02 % (w/v)
sample_conditions_1: ionic strength: 150 mM; pH: 7.3; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR, Brunger A. T. et.al. - refinement
NMR spectrometers:
- Bruker AMX 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts