Backbone 1H, 13C, and 15N Chemical Shift Assignments and relaxation data for
Chorismate Mutase from Bacillus subtilis in complex with inhibitor

Investigation of ligand binding and protein dynamics in Bacillus subtilis chorismate mutase by transverse relaxation optimized spectroscopy-nuclear magnetic resonance.

chorismate mutase (isozymes 1 and 2) [Bacillus subtilis subsp. subtilis str. JH642]

RecName: Full=Chorismate mutase; Short=CM

chorismate mutase (isozymes 1 and 2) [Bacillus subtilis subsp. subtilis str. 168]

chorismate mutase (isozymes 1 and 2) [Bacillus subtilis subsp. subtilis str. NCIB 3610]

chorismate mutase [Bacillus subtilis subsp. subtilis str. 168]

chorismate mutase (aroH) [Bacillus subtilis]

chorismate mutase [Bacillus subtilis subsp. natto BEST195]

Crystal Structures Of The Monofunctional Chorismate Mutase From Bacillus Subtilis And Its Complex With A Transition State Analog

The Monofunctional Chorismate Mutase From Bacillus Subtilis: Structure Determination Of Chorismate Mutase And Its Complexes With A Transition State Analog And Prephenate, And Implications On The Mechanism Of Enzymatic Reaction

Chorismate Mutase From Bacillus Subtilis At 1.30 Angstrom

residue name for residue 112 corrected in relaxation save frames