BMRB Entry 30246
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30246
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Title: Red abalone lysin F104A PubMed: 29348201
Deposition date: 2017-02-14 Original release date: 2018-01-25
Authors: Wilburn, D.; Tuttle, L.
Citation: Wilburn, D.; Tuttle, L.; Klevit, R.; Swanson, W.. "Solution structure of sperm lysin yields novel insights into molecular dynamics of rapid protein evolution" Proc. Natl. Acad. Sci. U. S. A. 115, 1310-1315 (2018).
Assembly members:
entity_1, polymer, 135 residues, 16089.939 Da.
Natural source: Common Name: California red abalone Taxonomy ID: 6454 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Haliotis rufescens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli K-12
Entity Sequences (FASTA):
entity_1: GRSWHYVEPKFLNKAFEVAL
KVQIIAGFDRGLVKWLRVHG
RTLSTVQKKALYFVNRRYMQ
THWANYMLWINKKIDALGRT
PVVGDYTRLGAEIGRRIDMA
YFYDALKDKNMIPKYLPYME
EINRMRPADVPVKYM
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 454 |
| 15N chemical shifts | 119 |
| 1H chemical shifts | 662 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 135 residues - 16089.939 Da.
| 1 | GLY | ARG | SER | TRP | HIS | TYR | VAL | GLU | PRO | LYS | ||||
| 2 | PHE | LEU | ASN | LYS | ALA | PHE | GLU | VAL | ALA | LEU | ||||
| 3 | LYS | VAL | GLN | ILE | ILE | ALA | GLY | PHE | ASP | ARG | ||||
| 4 | GLY | LEU | VAL | LYS | TRP | LEU | ARG | VAL | HIS | GLY | ||||
| 5 | ARG | THR | LEU | SER | THR | VAL | GLN | LYS | LYS | ALA | ||||
| 6 | LEU | TYR | PHE | VAL | ASN | ARG | ARG | TYR | MET | GLN | ||||
| 7 | THR | HIS | TRP | ALA | ASN | TYR | MET | LEU | TRP | ILE | ||||
| 8 | ASN | LYS | LYS | ILE | ASP | ALA | LEU | GLY | ARG | THR | ||||
| 9 | PRO | VAL | VAL | GLY | ASP | TYR | THR | ARG | LEU | GLY | ||||
| 10 | ALA | GLU | ILE | GLY | ARG | ARG | ILE | ASP | MET | ALA | ||||
| 11 | TYR | PHE | TYR | ASP | ALA | LEU | LYS | ASP | LYS | ASN | ||||
| 12 | MET | ILE | PRO | LYS | TYR | LEU | PRO | TYR | MET | GLU | ||||
| 13 | GLU | ILE | ASN | ARG | MET | ARG | PRO | ALA | ASP | VAL | ||||
| 14 | PRO | VAL | LYS | TYR | MET |
Samples:
sample_1: lysin, [U-15N], 300 uM; sodium chloride, natural abundunce, 200 mM; sodium phosphate 10 mM
sample_2: lysin, [U-13C; U-15N], 300 uM; sodium chloride 200 mM; sodium phosphate 10 mM
sample_3: c12e6/hexanol 5 w/v; lysin, [U-15N], 300 uM; sodium chloride 200 mM; sodium phosphate 10 mM
sample_4: Tris 10 mM; lysin, [U-13C; U-15N], 200 uM; sodium chloride 200 mM
sample_conditions_1: ionic strength: 200 mM; pH: 7.4; pressure: 1 atm; temperature: 298 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 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N hetNOE | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N T1 | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N T2 | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC-IPAP | sample_3 | anisotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, peak picking
TOPSPIN, Bruker Biospin - collection
X-PLOR NIH v2.43, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMR spectrometers:
- Bruker AVANCE 500 MHz
- Bruker AVANCE 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts