   1.6.2.4 | modeling of a complex of the FMN domain with cytochrome P450 monooxygenase Tri11. The complex shows significant interface contacts and structural changes on interaction, the hydrogen bonding interactions are observed between Tri11 protein residues R91, R97, K127, P131,K136, Q139, E275, K375, R411, W412, E415, A416, K417, T418, N419, S421, S422, P423, W424, Y425, N426, D427, R428, R429, N436, V437, G438, R440, N441, R445 and CPR FMN domain residues D132, E102, E78, Y70, S82, R83, E202, E208, T96, N169, Y172, T171, G203, A204, T74, Q73, Y125, E127, E173, G128, E129, T131, S177, T76, A77, G75, A123, D100, N133, S72 |
| 1.6.2.4 | purified mutant CYPOR with an engineered disulfide bond between the FAD and FMN domains, with or without complexed NADP+, hanging drop vapour diffusion method, mixing of 0.002 ml of 15 mg/ml protein solution with 0.002 ml of reservoir solution containing 100 mM HEPES, pH 7.2, 150 mM MgCl2, and 17% PEG 335, purified protein is treated with 2 and 20 times molar excess of FMN and NADP+, respectively, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement |
