BMRB Entry 25681
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25681
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Title: FBP28 WW E454Y PubMed: 26483482
Deposition date: 2015-07-01 Original release date: 2015-10-19
Authors: Medina, Jordi; Macias, Maria J; Martin-Malpartida, Pau; Scheraga, Harold
Citation: Maisuradze, Gia; Medina, Jordi; Kachlishvili, Khatuna; Krupa, Pawel; Mozolewska, Magdalena; Martin-Malpartida, Pau; Maisuradze, Luka; Macias, Maria J; Scheraga, Harold. "Preventing fibril formation of a protein by selective mutation" Proc. Natl. Acad. Sci. U.S.A. 112, 13549-13554 (2015).
Assembly members:
entity, polymer, 37 residues, 4398.818 Da.
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GATAVSEWTEYKTADGKTYY
YNNRTLYSTWEKPQELK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 25 |
| 15N chemical shifts | 4 |
| 1H chemical shifts | 199 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 37 residues - 4398.818 Da.
| 1 | GLY | ALA | THR | ALA | VAL | SER | GLU | TRP | THR | GLU | ||||
| 2 | TYR | LYS | THR | ALA | ASP | GLY | LYS | THR | TYR | TYR | ||||
| 3 | TYR | ASN | ASN | ARG | THR | LEU | TYR | SER | THR | TRP | ||||
| 4 | GLU | LYS | PRO | GLN | GLU | LEU | LYS |
Samples:
sample_1: entity500 – 1000 uM; sodium phosphate 25 mM; sodium chloride 100 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 5.8; pressure: 1 atm; temperature: 285 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O'Donoghue and Nilges - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone
or all simulated shifts