1H, 13C, and 15N backbone and side chain resonance assignments of thermophilic Geobacillus kaustophilus cyclophilin-A.

Solution Structure For Cyclophilin A From Geobacillus Kaustophilus

peptidyl-prolyl cis-trans isomerase (rotamase) [Geobacillus kaustophilus HTA426]

peptidyl-prolyl cis-trans isomerase [Geobacillus kaustophilus GBlys]

peptidyl-prolyl cis-trans isomerase rotamase [Geobacillus thermoleovorans B23]

Peptidyl-prolyl cis-trans isomerase B, PPIase B, rotamase B [Geobacillus thermodenitrificans NG80-2]

peptidyl-prolyl cis-trans isomerase cyclophilin type [Geobacillus sp. Y412MC61]

peptidyl-prolyl cis-trans isomerase cyclophilin type [Geobacillus sp. C56-T3]

peptidyl-prolyl cis-trans isomerase cyclophilin type [Geobacillus sp. Y412MC52]

Peptidyl-prolyl cis-trans isomerase [Geobacillus thermoleovorans CCB_US3_UF5]

MULTISPECIES: peptidylprolyl isomerase [Geobacillus]

MULTISPECIES: peptidylprolyl isomerase [Bacillaceae]

peptidylprolyl isomerase [Geobacillus sp. C56-T3]

Cleavage of a purification tag left a 'GS' prior to the first listed residue on the N-terminal end of the peptide

1H, 13C, and 15N Backbone and Sidechain Resonance Assignments for Cyclophilin A from Geobacillus Kaustophilus

Department of Biochemistry, School of Medicine, University of Colorado Denver

Department of Chemistry and Biochemistry, University of Colorado at Boulder

WR Wiley Environmental Molecular Sciences Laboratory, High Field NMR Facility

The CCPN NMR assignment and data analysis application
Department of Biochemistry, Cambridge CB2 1GA, UK