BMRB Entry 16123
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16123
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for d+PHS/V66K SNase
Deposition date: 2009-01-16 Original release date: 2012-08-07
Authors: Chimenti, Michael
Citation: Chimenti, Michael. "Increased fluctuations and local structural reorganization triggered by the ionization of an internal lysine" Protein Sci. ., .-..
Assembly members:
D+PHS-V66K_Nuclease, polymer, 143 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
D+PHS-V66K_Nuclease: ATSTKKLHKEPATLIKAIDG
DTVKLMYKGQPMTFRLLLVD
TPEFNEKYGPEASAFTKKMK
ENAKKIEVEFDKGQRTDKYG
RGLAYIYADGKMVNEALVRQ
GLAKVAYVYKGNNTHEQLLR
KAEAQAKKEKLNIWSEDNAD
SGQ
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 243 |
15N chemical shifts | 130 |
1H chemical shifts | 130 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | D+PHS/V66K | 1 |
Entities:
Entity 1, D+PHS/V66K 143 residues - Formula weight is not available
Residues 44-49 (an active site loop) were deleted from the protein; the original numbering scheme was kept.
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 | PHE | ASN | GLU | LYS | TYR | GLY | PRO | ||||
6 | GLU | ALA | SER | ALA | PHE | THR | LYS | LYS | MET | LYS | ||||
7 | GLU | ASN | ALA | LYS | LYS | ILE | GLU | VAL | GLU | PHE | ||||
8 | ASP | LYS | GLY | GLN | ARG | THR | ASP | LYS | TYR | GLY | ||||
9 | ARG | GLY | LEU | ALA | TYR | ILE | TYR | ALA | ASP | GLY | ||||
10 | LYS | MET | VAL | ASN | GLU | ALA | LEU | VAL | ARG | GLN | ||||
11 | GLY | LEU | ALA | LYS | VAL | ALA | TYR | VAL | TYR | LYS | ||||
12 | GLY | ASN | ASN | THR | HIS | GLU | GLN | LEU | LEU | ARG | ||||
13 | LYS | ALA | GLU | ALA | GLN | ALA | LYS | LYS | GLU | LYS | ||||
14 | LEU | ASN | ILE | TRP | SER | GLU | ASP | ASN | ALA | ASP | ||||
15 | SER | GLY | GLN |
Samples:
sample_1: D+PHS/V66K Nuclease, [U-99% 15N], 1 mM; D2O 10%; H2O 90%; sodium chloride 100 mM; sodium phosphate 25 mM
sample_conditions_1: ionic strength: 0.17 mM; pH: 6.7; pressure: 1 atm; temperature: 298 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 |
Software:
SPARKY v3.110, Goddard - chemical shift assignment
NMR spectrometers:
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts