BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25681

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

Data sets:
Data typeCount
13C chemical shifts25
15N chemical shifts4
1H chemical shifts199

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 37 residues - 4398.818 Da.

1   GLYALATHRALAVALSERGLUTRPTHRGLU
2   TYRLYSTHRALAASPGLYLYSTHRTYRTYR
3   TYRASNASNARGTHRLEUTYRSERTHRTRP
4   GLULYSPROGLNGLULEULYS

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:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_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:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts