NMR STRUCTURE OF VAT-N: THE N-TERMINAL DOMAIN OF VAT (VCP-LIKE ATPASE OF THERMOPLASMA)
The solution structure of VAT-N reveals a 'missing link' in the evolution of complex enzymes from a simple betaalphabetabeta element.
N-TERMINAL DOMAIN: M1 TO E183 FOLLOWED BY A DIGLYCINE SPACER
MESNNGIILRVAEANSTDPGMSRVRLDESSRRLLDAEIGDVVEIEKVRKTVGRVYRARPEDENKGIVRIDSVMRNNCGAS IGDKVKVRKVRTEIAKKVTLAPIIRKDQRLKFGEGIEEYVQRALIRRPMLEQDNISVPGLTLAGQTGLLFKVVKTLPSKV PVEIGEETKIEIREEPASEVLEEGG
CHEMICAL SHIFTS, 3JHNHA COUPLING-CONSTANTS AND HET. NOE VALUES
THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY. 3JHNHA COUPLING-CONSTANTS FROM AN HNHA SPECTRUM
STRUCTURES BASED ON 1923 DISTANCE RESTRAINTS; 1817 NOE BASED RESTRAINTS, 196 DIHEDRAL ANGLE RESTRAINTS, 56 J-COUPLING RESTRAINTS, 106 DISTANCE RESTRAINTS FOR H-BONDS, 158 CA AND 148 CB CHEMICAL SHIFT RESTRAINTS. REFINED WITH A CONFORMATIONAL DATABASE POTENTIAL
1.4 MM VAT-NU-15N,13C; 40 MM PHOSPHATE BUFFER NA; 90% H2O, 10% D2O
1.2 MM VAT-N U-15N; 40 MM PHOSPHATE BUFFER NA; 90% H2O, 10% D2O
DOUBLE-PSI BETA-BARREL, BETA-CLAM, SUBSTRATE RECOGNITION DOMAIN, HYDROLASE