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. BAYESIAN DIFFERENCE REFINEMENT WAS USED AT THE FINAL STEP. SEE TERWILLIGER AND BERENDZEN, ACTA CRYST. D52:1004-1011. (1996). THE SOLVENT MOLECULES 81, 129, 130, 139 AND 151 CAN BE MODELED ONLY FOR ONE ALTERNATIVE PROTEIN CONFORMATION. SULFATE NEAR DISTAL HISTIDINE MODELED AS A DISORDERED MOLECULE.
HEME PROTEIN, MODEL COMPOUNDS, OXYGEN STORAGE, LIGAND BINDING GEOMETRY, CONFORMATIONAL SUBSTATES
VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGYQG