BMRB Entry 25026
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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/BMR25026
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Title: NMR structure of putative beta-lactamase (NP_372339.1) from Staphylococcus aureus Mu50
Deposition date: 2014-06-18 Original release date: 2014-09-02
Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of putative beta-lactamase (NP_372339.1) from Staphylococcus aureus Mu50" Not known ., .-..
Assembly members:
entity, polymer, 152 residues, 16609.299 Da.
Natural source: Common Name: firmicutes Taxonomy ID: 158878 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GEEKMTNGQLWKKVKDSLID
SNIISGNENEEITVTYVNKT
GYSSSVSAYGNNNDDFSSTP
SNFSKLKEIDLKKDNVPSDD
FNTTVSGEDSWKTLTSKLKE
KGLVTDGQTVTIHCNDKSDN
TKSSVSGKVGADLTSGNGTT
FKKRFIDKITID
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 1008 |
| 13C chemical shifts | 484 |
| 15N chemical shifts | 164 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 152 residues - 16609.299 Da.
| 1 | GLY | GLU | GLU | LYS | MET | THR | ASN | GLY | GLN | LEU | ||||
| 2 | TRP | LYS | LYS | VAL | LYS | ASP | SER | LEU | ILE | ASP | ||||
| 3 | SER | ASN | ILE | ILE | SER | GLY | ASN | GLU | ASN | GLU | ||||
| 4 | GLU | ILE | THR | VAL | THR | TYR | VAL | ASN | LYS | THR | ||||
| 5 | GLY | TYR | SER | SER | SER | VAL | SER | ALA | TYR | GLY | ||||
| 6 | ASN | ASN | ASN | ASP | ASP | PHE | SER | SER | THR | PRO | ||||
| 7 | SER | ASN | PHE | SER | LYS | LEU | LYS | GLU | ILE | ASP | ||||
| 8 | LEU | LYS | LYS | ASP | ASN | VAL | PRO | SER | ASP | ASP | ||||
| 9 | PHE | ASN | THR | THR | VAL | SER | GLY | GLU | ASP | SER | ||||
| 10 | TRP | LYS | THR | LEU | THR | SER | LYS | LEU | LYS | GLU | ||||
| 11 | LYS | GLY | LEU | VAL | THR | ASP | GLY | GLN | THR | VAL | ||||
| 12 | THR | ILE | HIS | CYS | ASN | ASP | LYS | SER | ASP | ASN | ||||
| 13 | THR | LYS | SER | SER | VAL | SER | GLY | LYS | VAL | GLY | ||||
| 14 | ALA | ASP | LEU | THR | SER | GLY | ASN | GLY | THR | THR | ||||
| 15 | PHE | LYS | LYS | ARG | PHE | ILE | ASP | LYS | ILE | THR | ||||
| 16 | ILE | ASP |
Samples:
sample_1: entity, [U-99% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; H2O 95%; D2O 5%
sample_conditions_1: temperature: 308 K; pH: 6.0; pressure: 1 atm; ionic strength: 0.0798 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| APSY 4D-HACANH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 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 |
Software:
CYANA, G??ntert P. - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAB42901 BAB57977 BAF78683 |
| EMBL | CBX35026 CCJ11292 CCJ13257 CCJ15221 CCJ19148 |
| GB | ABQ49653 ABR52738 ACY11710 ADC37981 AHM70591 |
| REF | WP_001092756 WP_001092778 WP_001092779 WP_001092780 WP_001092781 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts