BMRB Entry 50301
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50301
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Title: Urea Denatured Staphylococcal Nuclease PubMed: 32737158
Deposition date: 2020-05-29 Original release date: 2020-07-15
Authors: Mizukami, Takuya; Furuzawa, Shunta; Itoh, Satoru; Segawa, Saho; Ikura, Teikichi; Ihara, Kunio; Okumura, Hisashi; Roder, Heinrich; Maki, Kosuke
Citation: Mizukami, Takuya; Furuzawa, Shunta; Itoh, Satoru; Segawa, Saho; Ikura, Teikichi; Ihara, Kunio; Okumura, Hisashi; Roder, Heinrich; Maki, Kosuke. "Energetics and kinetics of substrate analog-coupled staphylococcal nuclease folding revealed by a statistical mechanical approach" Proc. Natl. Acad. Sci. U.S.A. 117, 19953-19962 (2020).
Assembly members:
entity_1, polymer, 149 residues, 16811 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 Vector: pMT7-SN
Entity Sequences (FASTA):
entity_1: ATSTKKLHKEPATLIKAIDG
DTVKLMYKGQPMTFRLLLVD
TPETKHPKKGVEKYGPEASA
FTKKMVENAKKIEVEFDKGQ
RTDKYGRGLAYIYADGKMVN
EALVRQGLAKVAYVYKPNNT
HEQHLRKSEAQAKKEKLNIW
SEDNADSGQ
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 227 |
15N chemical shifts | 95 |
1H chemical shifts | 95 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Staphylococcal nuclease | 1 |
Entities:
Entity 1, Staphylococcal nuclease 149 residues - 16811 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 | GLU | GLN | HIS | 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: Staphylococcal nuclease, [U-100% 13C; U-100% 15N], 650 uM; MOPS 10 mM; CaCl2 10 mM; urea 2.91 M
sample_conditions_1: ionic strength: 0.04 M; pH: 5.4; pressure: 1 atm; temperature: 295 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4.0 - collection, processing
NMR spectrometers:
- Bruker AVANCE NEO 600 MHz
Related Database Links:
PDB |
Download HSQC peak lists in one of the following formats:
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SPARKY: Backbone
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