BMRB Entry 15232
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15232
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Title: proline-free mutant of SNase V8 PubMed: 17887731
Deposition date: 2007-05-02 Original release date: 2007-10-29
Authors: Shan, Lu
Citation: Shan, Lu; Tong, Yufeng; Xie, Tao; Wang, Min; Wang, Jinfeng. "Restricted backbone conformational and motional flexibilities of loops containing peptidyl-proline bonds dominate the enzyme activity of staphylococcal nuclease(,)." Biochemistry 46, 11504-11513 (2007).
Assembly members:
v8pf, polymer, 149 residues, 16678.268 Da.
Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
v8pf: ATSTKKLHKEAATLIKAIDG
DTVKLMYKGQAMTFRLLLVD
TAETKHTKKGVEKYGAEASA
FTKKMVENAKKIEVEFDKGQ
RTDKYGRGLAYIYADGKMVN
EALVRQGLAKVAYVYKGNNT
HEQLLRKSEAQAKKEKLNIW
SEDNADSGQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 371 |
| 15N chemical shifts | 127 |
| 1H chemical shifts | 666 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | v8pf | 1 |
Entities:
Entity 1, v8pf 149 residues - 16678.268 Da.
| 1 | ALA | THR | SER | THR | LYS | LYS | LEU | HIS | LYS | GLU | ||||
| 2 | ALA | ALA | THR | LEU | ILE | LYS | ALA | ILE | ASP | GLY | ||||
| 3 | ASP | THR | VAL | LYS | LEU | MET | TYR | LYS | GLY | GLN | ||||
| 4 | ALA | MET | THR | PHE | ARG | LEU | LEU | LEU | VAL | ASP | ||||
| 5 | THR | ALA | GLU | THR | LYS | HIS | THR | LYS | LYS | GLY | ||||
| 6 | VAL | GLU | LYS | TYR | GLY | ALA | GLU | ALA | SER | ALA | ||||
| 7 | PHE | THR | LYS | LYS | MET | VAL | GLU | ASN | ALA | LYS | ||||
| 8 | LYS | ILE | GLU | VAL | GLU | PHE | ASP | LYS | GLY | GLN | ||||
| 9 | ARG | THR | ASP | LYS | TYR | GLY | ARG | GLY | LEU | ALA | ||||
| 10 | TYR | ILE | TYR | ALA | ASP | GLY | LYS | MET | VAL | ASN | ||||
| 11 | GLU | ALA | LEU | VAL | ARG | GLN | GLY | LEU | ALA | LYS | ||||
| 12 | VAL | ALA | TYR | VAL | TYR | LYS | GLY | ASN | ASN | THR | ||||
| 13 | HIS | GLU | GLN | LEU | LEU | ARG | LYS | SER | GLU | ALA | ||||
| 14 | GLN | ALA | LYS | LYS | GLU | LYS | LEU | ASN | ILE | TRP | ||||
| 15 | SER | GLU | ASP | ASN | ALA | ASP | SER | GLY | GLN |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 1 mM; KCL 100 mM; D2O 10%; H2O 90%; acetate 59 mM
sample_conditions_1: ionic strength: 100 mM; pH: 5.0; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
FELIX v98, Accelrys Software Inc. - data analysis
NMR spectrometers:
- Bruker DMX 600 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
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