BMRB Entry 17765
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17765
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Title: Identification of the key regions that drive functional amyloid formation by the fungal hydrophobin EAS PubMed: 22308366
Deposition date: 2011-07-06 Original release date: 2012-01-24
Authors: Macindoe, Ingrid; Kwan, Ann; Morris, Vanessa; Mackay, Joel; Sunde, Margie
Citation: Macindoe, Ingrid; Kwan, Ann; Ren, Qin; Morris, Vanessa; Yang, Wenrong; Mackay, Joel; Sunde, Margaret. "Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS." Proc. Natl. Acad. Sci. U.S.A. 109, E804-E811 (2012).
Assembly members:
entity, polymer, 68 residues, 6728.595 Da.
Natural source: Common Name: Neurospora crassa Taxonomy ID: 5141 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Neurospora crassa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: SATTIGPNTCSIDDYKPYCC
QSMSGSASLGCVVGVIGSQC
GASVKCCKDDVTNTGNSGLI
INAANCVA
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 420 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | EAS | 1 |
Entities:
Entity 1, EAS 68 residues - 6728.595 Da.
Residue 1 represents a cloning artifact.
| 1 | SER | ALA | THR | THR | ILE | GLY | PRO | ASN | THR | CYS | ||||
| 2 | SER | ILE | ASP | ASP | TYR | LYS | PRO | TYR | CYS | CYS | ||||
| 3 | GLN | SER | MET | SER | GLY | SER | ALA | SER | LEU | GLY | ||||
| 4 | CYS | VAL | VAL | GLY | VAL | ILE | GLY | SER | GLN | CYS | ||||
| 5 | GLY | ALA | SER | VAL | LYS | CYS | CYS | LYS | ASP | ASP | ||||
| 6 | VAL | THR | ASN | THR | GLY | ASN | SER | GLY | LEU | ILE | ||||
| 7 | ILE | ASN | ALA | ALA | ASN | CYS | VAL | ALA |
Samples:
sample_1: EAS 890 uM; D2O 5%; H2O 95%; DSS20 – 34 uM; sodium phosphate 20 mM
sample_2: EAS, [U-98% 15N], 280 uM; D2O 5%; H2O 95%; DSS20 – 34 uM; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_2 |
Software:
TOPSPIN vv1.3, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
ARIA vv1.2, Linge, O, . - refinement, structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
ProcheckNMR, Laskowski and MacArthur - structure validation
Molmol, Koradi, Billeter and Wuthrich - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz