BMRB Entry 15357
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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/BMR15357
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Title: the solution structure of SNase complex PubMed: 19658434
Deposition date: 2007-07-01 Original release date: 2007-07-01
Authors: Geng, Yong; Shan, Lu; Feng, Yingang; Wang, Jinfeng
Citation: Geng, Yong; Feng, Yingang; Xie, Tao; Shan, Lu; Wang, Jinfeng. "The native-like interactions between SNase121 and SNase(111-143) fragments induce the recovery of their native-like structures and the ability to degrade DNA." Biochemistry 48, 8692-8703 (2009).
Assembly members:
SNase complex -subdomain, polymer, 156 residues, 17686.604 Da.
Natural source: Common Name: not available 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):
SNase complex -subdomain: ATSTKKLHKEPATLIKAIDG
DTVKLMYKGQPMTFRLLLVD
TPETKHPKKGVEKYGPEASA
FTKKMVENAKKIEVEFDKGQ
RTDKYGRGLAYIYADGKMVN
EALVRQGLAKVAYVYKPNNT
HGSVAYVYKPNNTHEQLLRK
SEAQAKKEKLNIWSED
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 580 |
| 15N chemical shifts | 141 |
| 1H chemical shifts | 903 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | -subdomain | 1 |
Entities:
Entity 1, -subdomain 156 residues - 17686.604 Da.
| 1 | ALA | THR | SER | THR | LYS | LYS | LEU | HIS | LYS | GLU | ||||
| 2 | PRO | ALA | THR | LEU | ILE | LYS | ALA | ILE | ASP | GLY | ||||
| 3 | ASP | THR | VAL | LYS | LEU | MET | TYR | LYS | GLY | GLN | ||||
| 4 | PRO | MET | THR | PHE | ARG | LEU | LEU | LEU | VAL | ASP | ||||
| 5 | THR | PRO | GLU | THR | LYS | HIS | PRO | LYS | LYS | GLY | ||||
| 6 | VAL | GLU | LYS | TYR | GLY | PRO | 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 | PRO | ASN | ASN | THR | ||||
| 13 | HIS | GLY | SER | VAL | ALA | TYR | VAL | TYR | LYS | PRO | ||||
| 14 | ASN | ASN | THR | HIS | GLU | GLN | LEU | LEU | ARG | LYS | ||||
| 15 | SER | GLU | ALA | GLN | ALA | LYS | LYS | GLU | LYS | LEU | ||||
| 16 | ASN | ILE | TRP | SER | GLU | ASP |
Samples:
sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; deuterated acetate buffer 50 mM; KCl 100 mM; NaN3 0.01 (%w/v); H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 150 mM; pH: 5.0; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 4010 |
| PDB | |
| DBJ | BAT21500 |
| GB | AFR11891 AFR11892 AFR11893 AHG12631 AKU89572 |
| REF | WP_049881958 |
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