BMRB Entry 7225
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7225
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution NMR structure of the UPF0291 protein ynzC from Bacillus subtilis. Northeast Structural Genomics target SR384. (CASP Target) PubMed: 18431750
Deposition date: 2006-07-14 Original release date: 2008-07-16
Authors: Aramini, J.; Swapna, G.; Ho, C.; Shetty, K.; Cunningham, K.; Ma, L.-C.; Xiao, R.; Liu, J.; Baran, M.; Acton, T.; Rost, B.; Montelione, G.
Citation: Aramini, J.; Sharma, S.; Huang, Y.; Swapna, G.; Ho, C.; Shetty, K.; Cunningham, K.; Ma, L.-C.; Zhao, L.; Owens, L.; Jiang, M.; Xiao, R.; Liu, J.; Baran, M.; Acton, T.; Rost, B.; Montelione, G.. "Solution NMR structure of the SOS response protein YnzC from Bacillus subtilis" Proteins 72, 526-530 (2008).
Assembly members:
UPF0291 protein ynzC, polymer, 85 residues, Formula weight is not available
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
UPF0291 protein ynzC: MISNAKIARINELAAKAKAG
VITEEEKAEQQKLRQEYLKG
FRSSMKNTLKSVKIIDPEGN
DVTPEKLKREQRNNKLHLEH
HHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 338 |
| 15N chemical shifts | 75 |
| 1H chemical shifts | 489 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | UPF0291 protein ynzC | 1 |
Entities:
Entity 1, UPF0291 protein ynzC 85 residues - Formula weight is not available
| 1 | MET | ILE | SER | ASN | ALA | LYS | ILE | ALA | ARG | ILE | ||||
| 2 | ASN | GLU | LEU | ALA | ALA | LYS | ALA | LYS | ALA | GLY | ||||
| 3 | VAL | ILE | THR | GLU | GLU | GLU | LYS | ALA | GLU | GLN | ||||
| 4 | GLN | LYS | LEU | ARG | GLN | GLU | TYR | LEU | LYS | GLY | ||||
| 5 | PHE | ARG | SER | SER | MET | LYS | ASN | THR | LEU | LYS | ||||
| 6 | SER | VAL | LYS | ILE | ILE | ASP | PRO | GLU | GLY | ASN | ||||
| 7 | ASP | VAL | THR | PRO | GLU | LYS | LEU | LYS | ARG | GLU | ||||
| 8 | GLN | ARG | ASN | ASN | LYS | LEU | HIS | LEU | GLU | HIS | ||||
| 9 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: UPF0291 protein ynzC, [U-13C; U-15N], 1.12 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; D2O 5%; H2O 95%
sample_2: UPF0291 protein ynzC, [U-5% 13C; U-15N], 1.12 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; D2O 5%; H2O 95%
sample_cond_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N-separated NOESY | not available | not available | not available |
| 3D 13C-separated NOESY | not available | not available | not available |
| HNHA | not available | not available | not available |
| 3D GFT-CBCACAcoNHN | not available | not available | not available |
| GFT-HNNCACBCA | not available | not available | not available |
| GFT-HABCABcoNHN | not available | not available | not available |
| 3D HCCH-TOCSY | not available | not available | not available |
| CCcoNH TOCSY | not available | not available | not available |
| HCCH-COSY | not available | not available | not available |
| high resolution 2D CH-HQSC (for stereospecific assignment of Val/Leu methyls) | not available | not available | not available |
| 3D HNCO | not available | not available | not available |
| HNcaCO | not available | not available | not available |
| 2D 15N1H-heteronuclear NOE | not available | not available | not available |
Software:
VNMR v6.1C - collection
xwinnmr v3.5pl6 - collection
AutoAssign v2.2.1 - data analysis
SPARKY v3.110 - data analysis
AutoStruct v2.1.1 - refinement
X-PLOR NIH v2.11.2 - refinement
AGNUS v2.0 - data analysis
PDBStat v4.01 - data analysis
PSVS v1.2 - data analysis
NMR spectrometers:
- Bruker AVANCE 600 MHz
Related Database Links:
| BMRB | 15476 |
| PDB | |
| DBJ | BAI85472 BAM52440 BAM58016 GAK81555 |
| EMBL | CAB13672 CCU58402 CEI56979 CEJ77403 |
| GB | ADV92690 AEP90959 AFI28488 AFQ57722 AGE63629 |
| REF | NP_389671 WP_003231595 WP_014664125 WP_019714523 WP_024573193 |
| SP | O31818 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts