BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 5241

Title: 1H and 15N assignment and secondary structure of the double K18G/R82E mutant of Alicyclobacillus acidocaldarius thermostable thioredoxin   PubMed: 15147188

Deposition date: 2001-12-20 Original release date: 2004-09-10

Authors: Leone, Marilisa; Di Lello, Paola; Pedone, Emilia; Bartolucci, Simonetta; Rossi, Mose'; Di Blasio, Benedetto; Pedone, Carlo; Saviano, Michele; Isernia, Carla; Fattorusso, Roberto

Citation: Leone, Marilisa; Di Lello, Paola; Ohlenschlager, O.; Pedone, Emilia; Bartolucci, Simonetta; Rossi, Mose'; Di Blasio, Benedetto; Pedone, Carlo; Saviano, Michele; Isernia, Carla; Fattorusso, Roberto. "Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: a molecular analysis of its reduced thermal stability."  Biochemistry 43, 6043-6058 (2004).

Assembly members:
Alicyclobacillus acidocaldarius thioredoxin, polymer, 105 residues, 11475.0 Da.

Natural source:   Common Name: Alicyclobacillus acidocaldarius (Bacillus acidocaldarius)   Taxonomy ID: 1388   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Alicyclobacillus acidocaldarius

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Alicyclobacillus acidocaldarius thioredoxin: ATMTLTDANFQQAIQGDGPV LVDFWAAWCGPCRMMAPVLE EFAEAHADKVTVAKLNVDEN PETTSQFGIMSIPTLILFKG GEPVKQLIGYQPKEQLEAQL ADVLQ

Data sets:
Data typeCount
1H chemical shifts756
15N chemical shifts111

Additional metadata:

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Related Database Links:

BMRB 4446 5240
PDB 1NSW 1NW2 1QUW 1RQM
GB ACV57898 AEJ42820
REF WP_012810252 WP_014463721 YP_003184287 YP_005517339
SP P80579

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