BMRB Entry 18370
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18370
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Title: Backbone 1H and 15N Chemical Shift Assignments for Hen Egg White Lysozyme mutant W123G. PubMed: 22468860
Deposition date: 2012-03-29 Original release date: 2012-04-18
Authors: Sziegat, Friederike; Silvers, Robert; Haehnke, Martin; Jensen, Malene; Blackledge, Martin; Wirmer-Bartoschek, Julia; Schwalbe, Harald
Citation: Sziegat, Friederike; Silvers, Robert; Hahnke, Martin; Jensen, Malene Ringkjbing; Blackledge, Martin; Wirmer-Bartoschek, Julia; Schwalbe, Harald. "Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme." Biochemistry 51, 3361-3372 (2012).
Assembly members:
W123G, polymer, 129 residues, Formula weight is not available
Natural source: Common Name: Chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11a
Entity Sequences (FASTA):
W123G: KVFGRAELAAAMKRHGLDNY
RGYSLGNWVAAAKFESNFNT
QATNRNTDGSTDYGILQINS
RWWANDGRTPGSRNLANIPA
SALLSSDITASVNAAKKIVS
DGNGMNAWVAWRNRAKGTDV
QAGIRGARL
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 125 |
1H chemical shifts | 125 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | W123G | 1 |
Entities:
Entity 1, W123G 129 residues - Formula weight is not available
1 | LYS | VAL | PHE | GLY | ARG | ALA | GLU | LEU | ALA | ALA | ||||
2 | ALA | MET | LYS | ARG | HIS | GLY | LEU | ASP | ASN | TYR | ||||
3 | ARG | GLY | TYR | SER | LEU | GLY | ASN | TRP | VAL | ALA | ||||
4 | ALA | ALA | LYS | PHE | GLU | SER | ASN | PHE | ASN | THR | ||||
5 | GLN | ALA | THR | ASN | ARG | ASN | THR | ASP | GLY | SER | ||||
6 | THR | ASP | TYR | GLY | ILE | LEU | GLN | ILE | ASN | SER | ||||
7 | ARG | TRP | TRP | ALA | ASN | ASP | GLY | ARG | THR | PRO | ||||
8 | GLY | SER | ARG | ASN | LEU | ALA | ASN | ILE | PRO | ALA | ||||
9 | SER | ALA | LEU | LEU | SER | SER | ASP | ILE | THR | ALA | ||||
10 | SER | VAL | ASN | ALA | ALA | LYS | LYS | ILE | VAL | SER | ||||
11 | ASP | GLY | ASN | GLY | MET | ASN | ALA | TRP | VAL | ALA | ||||
12 | TRP | ARG | ASN | ARG | ALA | LYS | GLY | THR | ASP | VAL | ||||
13 | GLN | ALA | GLY | ILE | ARG | GLY | ALA | ARG | LEU |
Samples:
sample_1: W123G, [U-99% 15N], 300 uM; H2O 49.95 M; D2O, [U-2H], 5.55 M
sample_conditions_1: pH: 2.0; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker DRX 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts