SOLUTION STRUCTURE OF THE CHEMOKINE HMIP-1BETA(SLASH)ACT-2 BY MULTI-DIMENSIONAL NMR: A NOVEL CHEMOKINE DIMER
High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
HUMAN MACROPHAGE INFLAMMATORY PROTEIN 1 BETA
RESTRAINED MINIMIZED AVERAGE STRUCTURE OVER 35 FILES AVE.RMS DIFF. TO MEAN FOR BACKBONE (4-69)= 0.304637 ANGSTROMS AVE.RMS DIFF. TO MEAN FOR ALL ORDERED NON-H-ATOMS (4-69)= 0.45 ANGSTROMS AVE.RMS DIFF. TO MEAN FOR ALL NON-H-ATOMS (4-69)= 0.706906 ANGSTROMS THE 3D STRUCTURE OF THE HMIP-1BETA DIMER IN SOLUTION BY NMR IS BASED ON 3586 EXPERIMENTAL RESTRAINTS COMPRISING: 3132 STRUCTURE USEFUL INTERPROTON DISTANCE RESTRAINTS OF WHICH 228 ARE INTERSUBUNIT; 24 RESTRAINTS FOR 12 H-BONDS INVOLVING TIGHTLY BOUND WATER MOLECULES; 108 RESTRAINTS FOR 54 BACKBONE HYDROGEN BONDS INVOLVING SLOWLY EXCHANGING AMIDE PROTONS; 220 TORSION ANGLE RESTRAINTS (122 PHI, 10 PSI, 80 CHI1 AND 8 CHI2); AND 102 HN-HALPHA THREE-BOND COUPLING CONSTANTS. A COMPLETE LIST OF EXPERIMENTAL RESTRAINTS AND 1H, 13C AND 15N ASSIGNMENTS ARE AVAILABLE FROM THE PROTEIN DATA BANK AS A SEPARATE ENTRY. 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. THIS ENTRY CORRESPONDS TO THE RESTRAINED MINIMIZED AVERAGE STRUCTURE: (SA)R. THIS IS OBTAINED BY FIRST AVERAGING THE COORDINATES OF THE INDIVIDUAL 35 DYNAMICAL SIMULATED ANNEALING SA STRUCTURES BEST FITTED TO RESIDUES A 4 - A 69 (CHAIN A) AND B 4 - B 69 (CHAIN B), AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. THE FIELD THAT CONTAINS THE B VALUE IN X-RAY STRUCTURES (COLUMNS 61 - 66) GIVES THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SA STRUCTURES AND THE MEAN STRUCTURE.
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