BMRB Entry 18732
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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/BMR18732
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Title: NMR structure of the protein NP_390345.1 from Bacilus subtilis
Deposition date: 2012-09-21 Original release date: 2012-10-22
Authors: Proudfoot, Andrew; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation: Proudfoot, Andrew; Wuthrich, Kurt. "NMR structure of the protein NP_390345.1 from Bacilus subtilis" Not known ., .-..
Assembly members:
NP_390345.1, polymer, 87 residues, 10333.016 Da.
Natural source: Common Name: Firmicutes Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NP_390345.1: GEETPLVTARHMSKWEEIAV
KEAKKRYPLAQVLFKQKVWD
RKRKDEAVKQYHLTLREGSK
EFGVFVTISFDPYSQKVNKI
AILEEYQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 324 |
| 15N chemical shifts | 90 |
| 1H chemical shifts | 615 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NP_390345.1 | 1 |
Entities:
Entity 1, NP_390345.1 87 residues - 10333.016 Da.
| 1 | GLY | GLU | GLU | THR | PRO | LEU | VAL | THR | ALA | ARG | ||||
| 2 | HIS | MET | SER | LYS | TRP | GLU | GLU | ILE | ALA | VAL | ||||
| 3 | LYS | GLU | ALA | LYS | LYS | ARG | TYR | PRO | LEU | ALA | ||||
| 4 | GLN | VAL | LEU | PHE | LYS | GLN | LYS | VAL | TRP | ASP | ||||
| 5 | ARG | LYS | ARG | LYS | ASP | GLU | ALA | VAL | LYS | GLN | ||||
| 6 | TYR | HIS | LEU | THR | LEU | ARG | GLU | GLY | SER | LYS | ||||
| 7 | GLU | PHE | GLY | VAL | PHE | VAL | THR | ILE | SER | PHE | ||||
| 8 | ASP | PRO | TYR | SER | GLN | LYS | VAL | ASN | LYS | ILE | ||||
| 9 | ALA | ILE | LEU | GLU | GLU | TYR | GLN |
Samples:
sample_1: NP_390345.1, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM; calcium chloride 20 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.220 M; pH: 6.5; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| APSY 4D-HACANH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-HACACONH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, G ntert P. - refinement
Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
TOPSPIN, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment
UNIO, Herrmann and Wuthrich - chemical shift assignment, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAI85984 BAM52951 BAM58525 GAK78312 |
| EMBL | CAB14396 CCU58980 CEI57685 CEJ78107 CJS87682 |
| GB | ADV93209 AEP91497 AFQ58416 AGA24194 AGE64116 |
| REF | NP_390345 WP_003246051 WP_015384086 WP_017696198 WP_021480018 |
| SP | O32019 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts