THE HIGH-RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURES OF THE OXIDIZED AND REDUCED STATES OF HUMAN THIOREDOXIN
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THE 3D STRUCTURE OF REDUCED HUMAN THIOREDOXIN IN SOLUTION BY NMR IS BASED ON 2933 EXPERIMENTAL RESTRAINTS COMPRISING: 2571 STRUCTURE USEFUL INTERPROTON DISTANCE RESTRAINTS; 28 RESTRAINTS FOR 14 H-BONDS INVOLVING 6 TIGHTLY BOUND WATER MOLECULES; 60 RESTRAINTS FOR 30 BACKBONE HYDROGEN BONDS INVOLVING SLOWLY EXCHANGING AMIDE PROTONS; 273 TORSION ANGLE RESTRAINTS (104 PHI, 71 PSI, 78 CHI1 AND 20 CHI2); AND 89 HN-HALPHA THREE-BOND COUPLING CONSTANTS. A COMPLETE LIST OF EXPERIMENTAL RESTRAINTS AND 1H, 13C AND 15N ASSIGNMENTS HAVE BEEN DEPOSITED WITH THE PROTEIN DATA BANK. THE STRUCTURES ARE CALCULATED USING THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD DESCRIBED BY: NILGES, M., CLORE, G.M. & GRONENBORN, A.M. (1988) FEBS LETT 229, 317 - 324. ALL STRUCTURAL STATISTICS ARE GIVEN IN THE REFERENCE. THE RESTRAINED MINIMIZED AVERAGE STRUCTURE (SA)R IS PRESENTED IN PROTEIN DATA BANK ENTRY 1TRW. THIS IS OBTAINED BY FIRST AVERAGING THE COORDINATES OF THE INDIVIDUAL 40 DYNAMICAL SIMULATED ANNEALING SA STRUCTURES BEST FITTED TO RESIDUES 1 - 105, AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. COLUMNS 61 - 65 OF THE COORDINATE RECORDS (THE B VALUE FIELD IN X-RAY STRUCTURES) IN THE MINIMIZED STRUCTURE (ENTRY 1TRW) GIVE THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SA STRUCTURES AND THE MEAN STRUCTURE. THE NUMBERS IN THIS FIELD OF THE INDIVIDUAL STRUCTURES (ENTRY 1TRV) HAVE NO MEANING.
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