| simulated annealing | THE 3D STRUCTURE OF THE IGAMMA SUBDOMAIN OF MU A
TRANSPOSASE WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR
NMR AND IS BASED ON 1293 EXPERIMENTAL NMR RESTRAINTS:
264 SEQUENTIAL (|I- J|=1), 282 MEDIUM RANGE (1 < |I-J| <=5)
AND 178 LONG RANGE (|I-J| >5) INTERRESIDUES AND 245
INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE RESTRAINTS;
40 DISTANCE RESTRAINTS FOR 20 BACKBONE H-BONDS;
108 TORSION ANGLE RESTRAINTS; 47 THREE-BOND HN-HA COUPLING
CONSTANT RESTRAINTS; AND 129 (66 CALPHA AND 63 CBETA) 13C
SHIFT RESTRAINTS.
THE STRUCTURES WERE CALCULATED USING THE SIMULATED
ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229,
129-136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED TO
INCORPORATE COUPLING CONSTANT (GARRETT ET AL. (1984) J.
MAGN. RESON. SERIES B 104, 99-103) AND CARBON CHEMICAL
SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B
106, 92-96) RESTRAINTS, AND A CONFORMATIONAL DATABASE
POTENTIAL (KUSZEWSKI ET AL. (1996) PROTEIN SCI. 5,
1067-1080; KUSZEWSKI ET AL. (1997) J. MAGN. RESON 125,
171-177).
THE RESTRAINED REGULARIZED MEAN STRUCTURE IS PRESENTED IN
ENTRY 2EZH AND 30 STRUCTURES ARE PRESENTED IN ENTRY 2EZI,
AND THE EXPERIMENTAL RESTRAINTS IN 2EZHMR. IN THE
RESTRAINED REGULARIZED MEAN COORDINATES (2EZH) THE LAST
COLUMN REPRESENTS THE AVERAGE RMS DIFFERENCE BETWEEN THE
INDIVIDUAL SIMULATED ANNEALING STRUCTURES AND THE MEAN
COORDINATE POSITIONS. THE LAST COLUMN IN THE INDIVIDUAL SA
STRUCTURES (2EZI) HAS NO MEANING. BEST FITTING TO GENERATE
THE AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 180 -
240. NOTE THAT THE OCCUPANCY FIELD HAS NO MEANING. | X-PLOR (SEE ABOVE) |
