| simulated annealing | THE 3D STRUCTURE OF THE IBETA SUBDOMAIN OF MU A TRANSPOSASE
WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR NMR AND
IS BASED ON 1446 EXPERIMENTAL NMR RESTRAINTS:
255 SEQUENTIAL (|I- J|=1), 220 MEDIUM RANGE (1 < |I-J| <=5)
AND 252 LONG RANGE (|I-J| >5) INTERRESIDUES AND 234
INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE RESTRAINTS;
52 DISTANCE RESTRAINTS FOR 26 BACKBONE H-BONDS;.
153 TORSION ANGLE RESTRAINTS
(94 PHI, 8 PSI, 36 CHI1 AND 15 CHI2);
58 THREE-BOND HN-HA COUPLING CONSTANT RESTRAINTS; AND 180
(92 CALPHA AND 88 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 2EZK AND 29 STRUCTURES ARE PRESENTED IN ENTRY 2EZL,
AND THE EXPERIMENTAL RESTRAINTS IN R2EZKMR. IN THE
RESTRAINED REGULARIZED MEAN COORDINATES (2EZK) 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
THE STRUCTURES (2EZI) HAS NO MEANING. BEST FITTING TO
GENERATE AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 89 -
166. RESIDUES 76 - 88 AND 167 - 174 AT THE N- AND
C-TERMINI ARE POORLY DEFINED BY THE EXPERIMENTAL DATA.
NOTE THE OCCUPANCY FIELD HAS NO MEANING.
RMSD IN BONDS,ANGLES,IMPROPERS,CDIH,NOE,COUP:
2808E-03,0.871524,1.02906,0.295155,2.337017E-02,0.902726
SHIFTS RMS A, B: 1.04343, 1.11143 | X-PLOR (SEE ABOVE) |
