BMRB Entry 25976
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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/BMR25976
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Title: Solution structure of the HYD1 hydrophobin from Schizophyllum commune
Deposition date: 2016-02-21 Original release date: 2016-03-30
Authors: Langelaan, David; Smith, Steven; Grondin, Julie
Citation: Langelaan, David; Smith, Steven; Master, Emma; Gandier, Julie-Anne; Grondin, Julie. "Structure of a fungal hydrophobin" Not known ., .-..
Assembly members:
Hydrophobin, polymer, 107 residues, 10873.522 Da.
Natural source: Common Name: Schizophyllum commune Taxonomy ID: 5334 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Schizophyllum commune
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Hydrophobin: KAMADIGSTAVPRDVNGGTP
PKSCSSGPVYCCNKTEDSKH
LDKGTTALLGLLNIKIGDLK
DLVGLNCSPLSVIGVGGNSC
SAQTVCCTNTYQHGLVNVGC
TPINIGL
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 379 |
15N chemical shifts | 91 |
1H chemical shifts | 574 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Hydrophobin | 1 |
Entities:
Entity 1, Hydrophobin 107 residues - 10873.522 Da.
1 | LYS | ALA | MET | ALA | ASP | ILE | GLY | SER | THR | ALA | ||||
2 | VAL | PRO | ARG | ASP | VAL | ASN | GLY | GLY | THR | PRO | ||||
3 | PRO | LYS | SER | CYS | SER | SER | GLY | PRO | VAL | TYR | ||||
4 | CYS | CYS | ASN | LYS | THR | GLU | ASP | SER | LYS | HIS | ||||
5 | LEU | ASP | LYS | GLY | THR | THR | ALA | LEU | LEU | GLY | ||||
6 | LEU | LEU | ASN | ILE | LYS | ILE | GLY | ASP | LEU | LYS | ||||
7 | ASP | LEU | VAL | GLY | LEU | ASN | CYS | SER | PRO | LEU | ||||
8 | SER | VAL | ILE | GLY | VAL | GLY | GLY | ASN | SER | CYS | ||||
9 | SER | ALA | GLN | THR | VAL | CYS | CYS | THR | ASN | THR | ||||
10 | TYR | GLN | HIS | GLY | LEU | VAL | ASN | VAL | GLY | CYS | ||||
11 | THR | PRO | ILE | ASN | ILE | GLY | LEU |
Samples:
sample_1: Hydrophobin, [U-13C; U-15N], 1 mM; TRIS 25 mM; sodium chloride 150 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 0.15 M; pH: 8; pressure: 1 atm; temperature: 303 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
1H-15N Heteronuclear NOE | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMRJ, Varian - collection
CcpNmr_Analysis, Wim F. Vranken, Wayne Boucher, Tim J. Stevens, Rasmus H. Fogh, - chemical shift assignment
ARIA v1.3, Linge, O'Donoghue and Nilges - structure solution
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