Crystal structures of myoglobin-ligand complexes at near-atomic resolution.
VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGY
NO GEOMETRIC RESTRAINTS APPLIED TO IRON AND THE PLANAR ATOMS OF THE HEME. AQUOMET CONTAMINATION CORRECTED BY 30% OCCUPIED MODEL OF AQUOMET MYOGLOBIN. BAYESIAN DIFFERENCE REFINEMENT WAS USED AT THE FINAL STEP. SEE TERWILLIGER AND BERENDZEN, ACTA CRYST. D52:1004-1011 (1996). THE SOLVENT MOLECULES 81, 129, 139 AND 151 CAN BE MODELED ONLY FOR ONE ALTERNATIVE PROTEIN CONFORMATION.
HEME PROTEIN, MODEL COMPOUNDS, OXYGEN STORAGE, LIGAND BINDING GEOMETRY, CONFORMATIONAL SUBSTATES, OXYGEN TRANSPORT
VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGYQG