Iron in PDB 8r8h: Ensemble-Refined Carboxymyoglobin Photolysis Power Titration, 31 Mj/CM2

The structure of Ensemble-Refined Carboxymyoglobin Photolysis Power Titration, 31 Mj/CM2, PDB code: 8r8h was solved by T.Barends, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	9.96 / 1.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	64.1, 28.8, 35.8, 90, 106.9, 90
R / Rfree (%)	17.6 / 21.3

The binding sites of Iron atom in the Ensemble-Refined Carboxymyoglobin Photolysis Power Titration, 31 Mj/CM2 (pdb code 8r8h). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Ensemble-Refined Carboxymyoglobin Photolysis Power Titration, 31 Mj/CM2, PDB code: 8r8h:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Ensemble-Refined Carboxymyoglobin Photolysis Power Titration, 31 Mj/CM2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ensemble-Refined Carboxymyoglobin Photolysis Power Titration, 31 Mj/CM2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:10.2 occ:0.63 FE A:HEM201 0.0 10.2 0.6 FE A:HEM201 0.2 10.1 0.4 C A:CMO204 1.7 11.9 0.6 ND A:HEM201 1.8 12.0 0.4 NB A:HEM201 2.0 9.6 0.6 NC A:HEM201 2.0 9.9 0.4 ND A:HEM201 2.0 12.5 0.6 NC A:HEM201 2.0 10.2 0.6 NA A:HEM201 2.0 10.2 0.6 NA A:HEM201 2.1 10.7 0.4 NE2 A:HIS93 2.1 9.8 0.6 NB A:HEM201 2.2 10.3 0.4 NE2 A:HIS93 2.3 9.6 0.4 C1D A:HEM201 2.8 11.7 0.4 C4D A:HEM201 2.9 11.7 0.4 O A:CMO204 2.9 17.6 0.6 C4C A:HEM201 3.0 10.6 0.4 C4C A:HEM201 3.0 10.5 0.6 C1D A:HEM201 3.0 10.9 0.6 C4D A:HEM201 3.0 12.0 0.6 C4B A:HEM201 3.0 9.3 0.6 C1A A:HEM201 3.0 11.0 0.4 C1B A:HEM201 3.0 10.2 0.6 C1C A:HEM201 3.1 10.1 0.6 C1A A:HEM201 3.1 10.6 0.6 C4A A:HEM201 3.1 11.5 0.6 CE1 A:HIS93 3.1 11.9 0.6 C1C A:HEM201 3.1 10.4 0.4 C4B A:HEM201 3.1 10.1 0.4 CD2 A:HIS93 3.1 9.4 0.6 C1B A:HEM201 3.2 10.4 0.4 C4A A:HEM201 3.2 11.3 0.4 CE1 A:HIS93 3.2 11.7 0.4 CHD A:HEM201 3.3 12.3 0.4 CD2 A:HIS93 3.3 10.0 0.4 CHA A:HEM201 3.4 10.8 0.4 CHD A:HEM201 3.4 12.0 0.6 CHB A:HEM201 3.4 10.1 0.6 CHA A:HEM201 3.4 10.9 0.6 CHC A:HEM201 3.4 10.1 0.6 CHC A:HEM201 3.5 10.4 0.4 CHB A:HEM201 3.5 10.6 0.4 C A:CMO204 3.7 11.7 0.4 C2D A:HEM201 4.1 11.8 0.4 C3D A:HEM201 4.1 12.8 0.4 ND1 A:HIS93 4.2 12.4 0.6 C3C A:HEM201 4.2 11.2 0.4 C2C A:HEM201 4.2 11.2 0.4 C3C A:HEM201 4.2 10.9 0.6 C2D A:HEM201 4.2 11.4 0.6 C3D A:HEM201 4.2 12.4 0.6 C2C A:HEM201 4.3 11.1 0.6 CG A:HIS93 4.3 10.7 0.6 C3B A:HEM201 4.3 10.6 0.6 C2B A:HEM201 4.3 10.2 0.6 C2A A:HEM201 4.3 10.4 0.6 C3A A:HEM201 4.3 11.2 0.6 C2A A:HEM201 4.3 10.8 0.4 C3A A:HEM201 4.3 11.5 0.4 C2B A:HEM201 4.4 10.3 0.4 C3B A:HEM201 4.4 10.8 0.4 ND1 A:HIS93 4.4 11.9 0.4 NE2 A:HIS64 4.4 16.7 0.4 CG A:HIS93 4.5 10.8 0.4 O A:CMO204 4.6 17.3 0.4 CG2 A:VAL68 4.6 13.2 0.4 NE2 A:HIS64 4.6 17.5 0.6 CG2 A:VAL68 4.7 14.0 0.6 CE1 A:HIS64 5.0 18.8 0.4

Iron binding site 2 out of 2 in the Ensemble-Refined Carboxymyoglobin Photolysis Power Titration, 31 Mj/CM2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Ensemble-Refined Carboxymyoglobin Photolysis Power Titration, 31 Mj/CM2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:10.1 occ:0.37 FE A:HEM201 0.0 10.1 0.4 FE A:HEM201 0.2 10.2 0.6 C A:CMO204 1.9 11.9 0.6 ND A:HEM201 1.9 12.0 0.4 NB A:HEM201 1.9 9.6 0.6 NE2 A:HIS93 1.9 9.8 0.6 NA A:HEM201 2.0 10.2 0.6 NA A:HEM201 2.0 10.7 0.4 NB A:HEM201 2.1 10.3 0.4 NC A:HEM201 2.1 9.9 0.4 NC A:HEM201 2.1 10.2 0.6 ND A:HEM201 2.1 12.5 0.6 NE2 A:HIS93 2.2 9.6 0.4 CE1 A:HIS93 2.9 11.9 0.6 C1B A:HEM201 2.9 10.2 0.6 C1D A:HEM201 3.0 11.7 0.4 C4A A:HEM201 3.0 11.5 0.6 C4D A:HEM201 3.0 11.7 0.4 C4B A:HEM201 3.0 9.3 0.6 CD2 A:HIS93 3.0 9.4 0.6 C1A A:HEM201 3.0 11.0 0.4 C1A A:HEM201 3.0 10.6 0.6 C1B A:HEM201 3.1 10.4 0.4 C4B A:HEM201 3.1 10.1 0.4 CE1 A:HIS93 3.1 11.7 0.4 C4C A:HEM201 3.1 10.6 0.4 C4A A:HEM201 3.1 11.3 0.4 C1C A:HEM201 3.1 10.1 0.6 O A:CMO204 3.1 17.6 0.6 C1C A:HEM201 3.1 10.4 0.4 C4D A:HEM201 3.1 12.0 0.6 C4C A:HEM201 3.1 10.5 0.6 C1D A:HEM201 3.1 10.9 0.6 CD2 A:HIS93 3.2 10.0 0.4 CHB A:HEM201 3.3 10.1 0.6 CHD A:HEM201 3.4 12.3 0.4 CHA A:HEM201 3.4 10.8 0.4 CHC A:HEM201 3.4 10.1 0.6 CHB A:HEM201 3.4 10.6 0.4 CHA A:HEM201 3.4 10.9 0.6 CHC A:HEM201 3.5 10.4 0.4 CHD A:HEM201 3.5 12.0 0.6 C A:CMO204 3.9 11.7 0.4 ND1 A:HIS93 4.0 12.4 0.6 CG A:HIS93 4.1 10.7 0.6 C2B A:HEM201 4.2 10.2 0.6 C3B A:HEM201 4.2 10.6 0.6 C3A A:HEM201 4.2 11.2 0.6 ND1 A:HIS93 4.2 11.9 0.4 C2A A:HEM201 4.2 10.4 0.6 C2A A:HEM201 4.2 10.8 0.4 C2D A:HEM201 4.2 11.8 0.4 C3D A:HEM201 4.2 12.8 0.4 C3A A:HEM201 4.3 11.5 0.4 C2B A:HEM201 4.3 10.3 0.4 C3C A:HEM201 4.3 11.2 0.4 C2C A:HEM201 4.3 11.2 0.4 C3B A:HEM201 4.3 10.8 0.4 CG A:HIS93 4.3 10.8 0.4 C2C A:HEM201 4.3 11.1 0.6 C3C A:HEM201 4.3 10.9 0.6 C3D A:HEM201 4.3 12.4 0.6 C2D A:HEM201 4.3 11.4 0.6 NE2 A:HIS64 4.5 16.7 0.4 CG2 A:VAL68 4.7 13.2 0.4 O A:CMO204 4.7 17.3 0.4 NE2 A:HIS64 4.8 17.5 0.6 CG2 A:VAL68 4.8 14.0 0.6

T.Barends, I.Schlichting. Influence of Pump Laser Fluence on Ultrafast Dynamics in Myoglobin To Be Published.