BMRB Entry 15863
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15863
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Title: Solution structure of EAS D15 truncation mutant PubMed: 18674544
Deposition date: 2008-07-07 Original release date: 2008-09-24
Authors: Kwan, Ann
Citation: Kwan, Ann; Macindoe, Ingrid; Paul, Vukasin; Morris, Vanessa; Kass, Itamar; Gupte, Rima; Mark, Alan; Templeton, Matthew; Mackay, Joel; Sunde, Margaret. "The Cys3-Cys4 loop of the hydrophobin EAS is not required for rodlet formation and surface activity" J. Mol. Biol. 382, 708-720 (2008).
Assembly members:
EAS_D15, polymer, 68 residues, 6818.720 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):
EAS_D15: SATTIGPNTCSIDDYKPYCC
QSMSGSASLGCVVGVIGSQC
GASVKCCKDDVTNTGNSFLI
INAANCVA
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 15N chemical shifts | 72 |
| 1H chemical shifts | 417 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | EAS_D15 | 1 |
Entities:
Entity 1, EAS_D15 68 residues - 6818.720 Da.
Residue 1 (Ser) represents a non-native residue from cloning.
| 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 | PHE | LEU | ILE | ||||
| 7 | ILE | ASN | ALA | ALA | ASN | CYS | VAL | ALA |
Samples:
sample_1: EAS_D15 0.3-0.5 ± 0.05 mM; sodium phosphate 20 ± 2 mM
sample_2: EAS_D15, [U-99% 15N], 0.1-0.3 ± 0.05 mM; sodium acetate 20 ± 2 mM
sample_conditions_1: ionic strength: 20 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v1.3, Bruker Biospin - collection, processing
XWINNMR, Bruker Biospin - collection
SPARKY v3.113, Goddard - chemical shift assignment, chemical shift calculation, data analysis, peak picking
CNS, Linge, O'Donoghue and Nilges - structure solution
ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution
NMR spectrometers:
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts