Iron in PDB 2at0: 1.00 A Crystal Structure of L133V Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6

The structure of 1.00 A Crystal Structure of L133V Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6, PDB code: 2at0 was solved by A.M.Amoia, W.R.Montfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.47 / 1.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	70.286, 42.699, 52.970, 90.00, 94.27, 90.00
R / Rfree (%)	13.9 / 15.4

The binding sites of Iron atom in the 1.00 A Crystal Structure of L133V Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6 (pdb code 2at0). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the 1.00 A Crystal Structure of L133V Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6, PDB code: 2at0:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the 1.00 A Crystal Structure of L133V Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 1.00 A Crystal Structure of L133V Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6 within 5.0Å range: probe atom residue distance (Å) B Occ X:Fe185 b:5.7 occ:0.50 FE X:HEM185 0.0 5.7 0.5 FE X:HEM185 0.0 5.7 0.5 FE X:HEM185 0.0 5.7 0.0 FE X:HEM185 0.0 5.7 0.0 N X:NO186 1.7 7.4 1.0 ND X:HEM185 2.0 6.0 0.5 NA X:HEM185 2.0 6.0 0.0 NA X:HEM185 2.0 6.0 0.5 NA X:HEM185 2.0 6.0 0.0 NB X:HEM185 2.0 6.1 0.0 NB X:HEM185 2.0 6.1 0.5 NB X:HEM185 2.0 6.1 0.0 NC X:HEM185 2.0 6.1 0.5 ND X:HEM185 2.0 6.4 0.0 ND X:HEM185 2.0 6.4 0.0 ND X:HEM185 2.0 6.4 0.5 NA X:HEM185 2.0 6.4 0.5 NB X:HEM185 2.0 6.3 0.5 NC X:HEM185 2.0 6.3 0.0 NC X:HEM185 2.0 6.3 0.5 NC X:HEM185 2.0 6.3 0.0 NE2 X:HIS59 2.1 5.2 1.0 O X:NO186 2.8 12.3 1.0 C4D X:HEM185 3.0 5.8 0.5 C1A X:HEM185 3.0 5.8 0.5 C1A X:HEM185 3.0 5.8 0.0 C1A X:HEM185 3.0 5.8 0.0 C4A X:HEM185 3.0 6.0 0.0 C4A X:HEM185 3.0 6.0 0.5 C4A X:HEM185 3.0 6.0 0.0 C1D X:HEM185 3.0 6.0 0.5 C1B X:HEM185 3.0 6.3 0.0 C1B X:HEM185 3.0 6.3 0.5 C1B X:HEM185 3.0 6.3 0.0 C4C X:HEM185 3.0 6.3 0.5 C4A X:HEM185 3.0 7.2 0.5 C1D X:HEM185 3.0 7.2 0.0 C1D X:HEM185 3.0 7.2 0.0 C1D X:HEM185 3.0 7.2 0.5 C4B X:HEM185 3.0 7.7 0.5 C1C X:HEM185 3.0 7.7 0.0 C1C X:HEM185 3.0 7.7 0.0 C1C X:HEM185 3.0 7.7 0.5 C4B X:HEM185 3.0 7.0 0.0 C4B X:HEM185 3.0 7.0 0.5 C4B X:HEM185 3.0 7.0 0.0 C1C X:HEM185 3.0 7.0 0.5 C1B X:HEM185 3.0 7.0 0.5 C4C X:HEM185 3.0 7.0 0.0 C4C X:HEM185 3.0 7.0 0.0 C4C X:HEM185 3.0 7.0 0.5 C4D X:HEM185 3.0 6.6 0.0 C4D X:HEM185 3.0 6.6 0.0 C4D X:HEM185 3.0 6.6 0.5 C1A X:HEM185 3.0 6.6 0.5 CE1 X:HIS59 3.1 5.0 1.0 CD2 X:HIS59 3.1 5.2 1.0 CHD X:HEM185 3.4 6.5 0.5 CHB X:HEM185 3.4 6.5 0.0 CHB X:HEM185 3.4 6.5 0.5 CHB X:HEM185 3.4 6.5 0.0 CHD X:HEM185 3.4 8.0 0.5 CHD X:HEM185 3.4 8.0 0.0 CHD X:HEM185 3.4 8.0 0.0 CHB X:HEM185 3.4 8.0 0.5 CHC X:HEM185 3.4 8.3 0.0 CHC X:HEM185 3.4 8.3 0.0 CHC X:HEM185 3.4 8.3 0.5 CHC X:HEM185 3.4 8.3 0.5 CHA X:HEM185 3.4 6.5 0.0 CHA X:HEM185 3.4 6.5 0.0 CHA X:HEM185 3.4 6.5 0.5 CHA X:HEM185 3.4 6.5 0.5 ND1 X:HIS59 4.2 4.9 1.0 CG X:HIS59 4.2 5.1 1.0 C2D X:HEM185 4.2 6.8 0.5 C3A X:HEM185 4.2 6.8 0.0 C3A X:HEM185 4.2 6.8 0.5 C3A X:HEM185 4.2 6.8 0.0 C3D X:HEM185 4.2 6.2 0.5 C2A X:HEM185 4.2 6.2 0.0 C2A X:HEM185 4.2 6.2 0.5 C2A X:HEM185 4.2 6.2 0.0 C2C X:HEM185 4.2 8.9 0.0 C2C X:HEM185 4.2 8.9 0.5 C2C X:HEM185 4.2 8.9 0.0 C3B X:HEM185 4.2 8.9 0.5 C3C X:HEM185 4.3 8.0 0.0 C3C X:HEM185 4.3 8.0 0.5 C3C X:HEM185 4.3 8.0 0.0 C2B X:HEM185 4.3 8.0 0.5 C3C X:HEM185 4.3 7.0 0.5 C2B X:HEM185 4.3 7.0 0.0 C2B X:HEM185 4.3 7.0 0.5 C2B X:HEM185 4.3 7.0 0.0 C2C X:HEM185 4.3 7.4 0.5 C3B X:HEM185 4.3 7.4 0.0 C3B X:HEM185 4.3 7.4 0.5 C3B X:HEM185 4.3 7.4 0.0 C2D X:HEM185 4.3 8.3 0.0 C2D X:HEM185 4.3 8.3 0.5 C2D X:HEM185 4.3 8.3 0.0 C3A X:HEM185 4.3 8.3 0.5 C3D X:HEM185 4.3 7.8 0.5 C3D X:HEM185 4.3 7.8 0.0 C3D X:HEM185 4.3 7.8 0.0 C2A X:HEM185 4.3 7.8 0.5 CD2 X:LEU130 4.7 14.6 0.7 CD2 X:LEU123 5.0 9.9 1.0

Iron binding site 2 out of 4 in the 1.00 A Crystal Structure of L133V Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 1.00 A Crystal Structure of L133V Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6 within 5.0Å range: probe atom residue distance (Å) B Occ X:Fe185 b:5.7 occ:0.00 FE X:HEM185 0.0 5.7 0.5 FE X:HEM185 0.0 5.7 0.5 FE X:HEM185 0.0 5.7 0.0 FE X:HEM185 0.0 5.7 0.0 N X:NO186 1.7 7.4 1.0 ND X:HEM185 2.0 6.0 0.5 NA X:HEM185 2.0 6.0 0.0 NA X:HEM185 2.0 6.0 0.5 NA X:HEM185 2.0 6.0 0.0 NB X:HEM185 2.0 6.1 0.0 NB X:HEM185 2.0 6.1 0.5 NB X:HEM185 2.0 6.1 0.0 NC X:HEM185 2.0 6.1 0.5 ND X:HEM185 2.0 6.4 0.0 ND X:HEM185 2.0 6.4 0.0 ND X:HEM185 2.0 6.4 0.5 NA X:HEM185 2.0 6.4 0.5 NB X:HEM185 2.0 6.3 0.5 NC X:HEM185 2.0 6.3 0.0 NC X:HEM185 2.0 6.3 0.5 NC X:HEM185 2.0 6.3 0.0 NE2 X:HIS59 2.1 5.2 1.0 O X:NO186 2.8 12.3 1.0 C4D X:HEM185 3.0 5.8 0.5 C1A X:HEM185 3.0 5.8 0.5 C1A X:HEM185 3.0 5.8 0.0 C1A X:HEM185 3.0 5.8 0.0 C4A X:HEM185 3.0 6.0 0.0 C4A X:HEM185 3.0 6.0 0.5 C4A X:HEM185 3.0 6.0 0.0 C1D X:HEM185 3.0 6.0 0.5 C1B X:HEM185 3.0 6.3 0.0 C1B X:HEM185 3.0 6.3 0.5 C1B X:HEM185 3.0 6.3 0.0 C4C X:HEM185 3.0 6.3 0.5 C4A X:HEM185 3.0 7.2 0.5 C1D X:HEM185 3.0 7.2 0.0 C1D X:HEM185 3.0 7.2 0.0 C1D X:HEM185 3.0 7.2 0.5 C4B X:HEM185 3.0 7.7 0.5 C1C X:HEM185 3.0 7.7 0.0 C1C X:HEM185 3.0 7.7 0.0 C1C X:HEM185 3.0 7.7 0.5 C4B X:HEM185 3.0 7.0 0.0 C4B X:HEM185 3.0 7.0 0.5 C4B X:HEM185 3.0 7.0 0.0 C1C X:HEM185 3.0 7.0 0.5 C1B X:HEM185 3.0 7.0 0.5 C4C X:HEM185 3.0 7.0 0.0 C4C X:HEM185 3.0 7.0 0.0 C4C X:HEM185 3.0 7.0 0.5 C4D X:HEM185 3.0 6.6 0.0 C4D X:HEM185 3.0 6.6 0.0 C4D X:HEM185 3.0 6.6 0.5 C1A X:HEM185 3.0 6.6 0.5 CE1 X:HIS59 3.1 5.0 1.0 CD2 X:HIS59 3.1 5.2 1.0 CHD X:HEM185 3.4 6.5 0.5 CHB X:HEM185 3.4 6.5 0.0 CHB X:HEM185 3.4 6.5 0.5 CHB X:HEM185 3.4 6.5 0.0 CHD X:HEM185 3.4 8.0 0.5 CHD X:HEM185 3.4 8.0 0.0 CHD X:HEM185 3.4 8.0 0.0 CHB X:HEM185 3.4 8.0 0.5 CHC X:HEM185 3.4 8.3 0.0 CHC X:HEM185 3.4 8.3 0.0 CHC X:HEM185 3.4 8.3 0.5 CHC X:HEM185 3.4 8.3 0.5 CHA X:HEM185 3.4 6.5 0.0 CHA X:HEM185 3.4 6.5 0.0 CHA X:HEM185 3.4 6.5 0.5 CHA X:HEM185 3.4 6.5 0.5 ND1 X:HIS59 4.2 4.9 1.0 CG X:HIS59 4.2 5.1 1.0 C2D X:HEM185 4.2 6.8 0.5 C3A X:HEM185 4.2 6.8 0.0 C3A X:HEM185 4.2 6.8 0.5 C3A X:HEM185 4.2 6.8 0.0 C3D X:HEM185 4.2 6.2 0.5 C2A X:HEM185 4.2 6.2 0.0 C2A X:HEM185 4.2 6.2 0.5 C2A X:HEM185 4.2 6.2 0.0 C2C X:HEM185 4.2 8.9 0.0 C2C X:HEM185 4.2 8.9 0.5 C2C X:HEM185 4.2 8.9 0.0 C3B X:HEM185 4.2 8.9 0.5 C3C X:HEM185 4.3 8.0 0.0 C3C X:HEM185 4.3 8.0 0.5 C3C X:HEM185 4.3 8.0 0.0 C2B X:HEM185 4.3 8.0 0.5 C3C X:HEM185 4.3 7.0 0.5 C2B X:HEM185 4.3 7.0 0.0 C2B X:HEM185 4.3 7.0 0.5 C2B X:HEM185 4.3 7.0 0.0 C2C X:HEM185 4.3 7.4 0.5 C3B X:HEM185 4.3 7.4 0.0 C3B X:HEM185 4.3 7.4 0.5 C3B X:HEM185 4.3 7.4 0.0 C2D X:HEM185 4.3 8.3 0.0 C2D X:HEM185 4.3 8.3 0.5 C2D X:HEM185 4.3 8.3 0.0 C3A X:HEM185 4.3 8.3 0.5 C3D X:HEM185 4.3 7.8 0.5 C3D X:HEM185 4.3 7.8 0.0 C3D X:HEM185 4.3 7.8 0.0 C2A X:HEM185 4.3 7.8 0.5 CD2 X:LEU130 4.7 14.6 0.7 CD2 X:LEU123 5.0 9.9 1.0

Iron binding site 3 out of 4 in the 1.00 A Crystal Structure of L133V Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of 1.00 A Crystal Structure of L133V Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6 within 5.0Å range: probe atom residue distance (Å) B Occ X:Fe185 b:5.7 occ:0.00 FE X:HEM185 0.0 5.7 0.5 FE X:HEM185 0.0 5.7 0.5 FE X:HEM185 0.0 5.7 0.0 FE X:HEM185 0.0 5.7 0.0 N X:NO186 1.7 7.4 1.0 ND X:HEM185 2.0 6.0 0.5 NA X:HEM185 2.0 6.0 0.0 NA X:HEM185 2.0 6.0 0.5 NA X:HEM185 2.0 6.0 0.0 NB X:HEM185 2.0 6.1 0.0 NB X:HEM185 2.0 6.1 0.5 NB X:HEM185 2.0 6.1 0.0 NC X:HEM185 2.0 6.1 0.5 ND X:HEM185 2.0 6.4 0.0 ND X:HEM185 2.0 6.4 0.0 ND X:HEM185 2.0 6.4 0.5 NA X:HEM185 2.0 6.4 0.5 NB X:HEM185 2.0 6.3 0.5 NC X:HEM185 2.0 6.3 0.0 NC X:HEM185 2.0 6.3 0.5 NC X:HEM185 2.0 6.3 0.0 NE2 X:HIS59 2.1 5.2 1.0 O X:NO186 2.8 12.3 1.0 C4D X:HEM185 3.0 5.8 0.5 C1A X:HEM185 3.0 5.8 0.5 C1A X:HEM185 3.0 5.8 0.0 C1A X:HEM185 3.0 5.8 0.0 C4A X:HEM185 3.0 6.0 0.0 C4A X:HEM185 3.0 6.0 0.5 C4A X:HEM185 3.0 6.0 0.0 C1D X:HEM185 3.0 6.0 0.5 C1B X:HEM185 3.0 6.3 0.0 C1B X:HEM185 3.0 6.3 0.5 C1B X:HEM185 3.0 6.3 0.0 C4C X:HEM185 3.0 6.3 0.5 C4A X:HEM185 3.0 7.2 0.5 C1D X:HEM185 3.0 7.2 0.0 C1D X:HEM185 3.0 7.2 0.0 C1D X:HEM185 3.0 7.2 0.5 C4B X:HEM185 3.0 7.7 0.5 C1C X:HEM185 3.0 7.7 0.0 C1C X:HEM185 3.0 7.7 0.0 C1C X:HEM185 3.0 7.7 0.5 C4B X:HEM185 3.0 7.0 0.0 C4B X:HEM185 3.0 7.0 0.5 C4B X:HEM185 3.0 7.0 0.0 C1C X:HEM185 3.0 7.0 0.5 C1B X:HEM185 3.0 7.0 0.5 C4C X:HEM185 3.0 7.0 0.0 C4C X:HEM185 3.0 7.0 0.0 C4C X:HEM185 3.0 7.0 0.5 C4D X:HEM185 3.0 6.6 0.0 C4D X:HEM185 3.0 6.6 0.0 C4D X:HEM185 3.0 6.6 0.5 C1A X:HEM185 3.0 6.6 0.5 CE1 X:HIS59 3.1 5.0 1.0 CD2 X:HIS59 3.1 5.2 1.0 CHD X:HEM185 3.4 6.5 0.5 CHB X:HEM185 3.4 6.5 0.0 CHB X:HEM185 3.4 6.5 0.5 CHB X:HEM185 3.4 6.5 0.0 CHD X:HEM185 3.4 8.0 0.5 CHD X:HEM185 3.4 8.0 0.0 CHD X:HEM185 3.4 8.0 0.0 CHB X:HEM185 3.4 8.0 0.5 CHC X:HEM185 3.4 8.3 0.0 CHC X:HEM185 3.4 8.3 0.0 CHC X:HEM185 3.4 8.3 0.5 CHC X:HEM185 3.4 8.3 0.5 CHA X:HEM185 3.4 6.5 0.0 CHA X:HEM185 3.4 6.5 0.0 CHA X:HEM185 3.4 6.5 0.5 CHA X:HEM185 3.4 6.5 0.5 ND1 X:HIS59 4.2 4.9 1.0 CG X:HIS59 4.2 5.1 1.0 C2D X:HEM185 4.2 6.8 0.5 C3A X:HEM185 4.2 6.8 0.0 C3A X:HEM185 4.2 6.8 0.5 C3A X:HEM185 4.2 6.8 0.0 C3D X:HEM185 4.2 6.2 0.5 C2A X:HEM185 4.2 6.2 0.0 C2A X:HEM185 4.2 6.2 0.5 C2A X:HEM185 4.2 6.2 0.0 C2C X:HEM185 4.2 8.9 0.0 C2C X:HEM185 4.2 8.9 0.5 C2C X:HEM185 4.2 8.9 0.0 C3B X:HEM185 4.2 8.9 0.5 C3C X:HEM185 4.3 8.0 0.0 C3C X:HEM185 4.3 8.0 0.5 C3C X:HEM185 4.3 8.0 0.0 C2B X:HEM185 4.3 8.0 0.5 C3C X:HEM185 4.3 7.0 0.5 C2B X:HEM185 4.3 7.0 0.0 C2B X:HEM185 4.3 7.0 0.5 C2B X:HEM185 4.3 7.0 0.0 C2C X:HEM185 4.3 7.4 0.5 C3B X:HEM185 4.3 7.4 0.0 C3B X:HEM185 4.3 7.4 0.5 C3B X:HEM185 4.3 7.4 0.0 C2D X:HEM185 4.3 8.3 0.0 C2D X:HEM185 4.3 8.3 0.5 C2D X:HEM185 4.3 8.3 0.0 C3A X:HEM185 4.3 8.3 0.5 C3D X:HEM185 4.3 7.8 0.5 C3D X:HEM185 4.3 7.8 0.0 C3D X:HEM185 4.3 7.8 0.0 C2A X:HEM185 4.3 7.8 0.5 CD2 X:LEU130 4.7 14.6 0.7 CD2 X:LEU123 5.0 9.9 1.0

Iron binding site 4 out of 4 in the 1.00 A Crystal Structure of L133V Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of 1.00 A Crystal Structure of L133V Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6 within 5.0Å range: probe atom residue distance (Å) B Occ X:Fe185 b:5.7 occ:0.50 FE X:HEM185 0.0 5.7 0.5 FE X:HEM185 0.0 5.7 0.5 FE X:HEM185 0.0 5.7 0.0 FE X:HEM185 0.0 5.7 0.0 N X:NO186 1.7 7.4 1.0 ND X:HEM185 2.0 6.0 0.5 NA X:HEM185 2.0 6.0 0.0 NA X:HEM185 2.0 6.0 0.5 NA X:HEM185 2.0 6.0 0.0 NB X:HEM185 2.0 6.1 0.0 NB X:HEM185 2.0 6.1 0.5 NB X:HEM185 2.0 6.1 0.0 NC X:HEM185 2.0 6.1 0.5 ND X:HEM185 2.0 6.4 0.0 ND X:HEM185 2.0 6.4 0.0 ND X:HEM185 2.0 6.4 0.5 NA X:HEM185 2.0 6.4 0.5 NB X:HEM185 2.0 6.3 0.5 NC X:HEM185 2.0 6.3 0.0 NC X:HEM185 2.0 6.3 0.5 NC X:HEM185 2.0 6.3 0.0 NE2 X:HIS59 2.1 5.2 1.0 O X:NO186 2.8 12.3 1.0 C4D X:HEM185 3.0 5.8 0.5 C1A X:HEM185 3.0 5.8 0.5 C1A X:HEM185 3.0 5.8 0.0 C1A X:HEM185 3.0 5.8 0.0 C4A X:HEM185 3.0 6.0 0.0 C4A X:HEM185 3.0 6.0 0.5 C4A X:HEM185 3.0 6.0 0.0 C1D X:HEM185 3.0 6.0 0.5 C1B X:HEM185 3.0 6.3 0.0 C1B X:HEM185 3.0 6.3 0.5 C1B X:HEM185 3.0 6.3 0.0 C4C X:HEM185 3.0 6.3 0.5 C4A X:HEM185 3.0 7.2 0.5 C1D X:HEM185 3.0 7.2 0.0 C1D X:HEM185 3.0 7.2 0.0 C1D X:HEM185 3.0 7.2 0.5 C4B X:HEM185 3.0 7.7 0.5 C1C X:HEM185 3.0 7.7 0.0 C1C X:HEM185 3.0 7.7 0.0 C1C X:HEM185 3.0 7.7 0.5 C4B X:HEM185 3.0 7.0 0.0 C4B X:HEM185 3.0 7.0 0.5 C4B X:HEM185 3.0 7.0 0.0 C1C X:HEM185 3.0 7.0 0.5 C1B X:HEM185 3.0 7.0 0.5 C4C X:HEM185 3.0 7.0 0.0 C4C X:HEM185 3.0 7.0 0.0 C4C X:HEM185 3.0 7.0 0.5 C4D X:HEM185 3.0 6.6 0.0 C4D X:HEM185 3.0 6.6 0.0 C4D X:HEM185 3.0 6.6 0.5 C1A X:HEM185 3.0 6.6 0.5 CE1 X:HIS59 3.1 5.0 1.0 CD2 X:HIS59 3.1 5.2 1.0 CHD X:HEM185 3.4 6.5 0.5 CHB X:HEM185 3.4 6.5 0.0 CHB X:HEM185 3.4 6.5 0.5 CHB X:HEM185 3.4 6.5 0.0 CHD X:HEM185 3.4 8.0 0.5 CHD X:HEM185 3.4 8.0 0.0 CHD X:HEM185 3.4 8.0 0.0 CHB X:HEM185 3.4 8.0 0.5 CHC X:HEM185 3.4 8.3 0.0 CHC X:HEM185 3.4 8.3 0.0 CHC X:HEM185 3.4 8.3 0.5 CHC X:HEM185 3.4 8.3 0.5 CHA X:HEM185 3.4 6.5 0.0 CHA X:HEM185 3.4 6.5 0.0 CHA X:HEM185 3.4 6.5 0.5 CHA X:HEM185 3.4 6.5 0.5 ND1 X:HIS59 4.2 4.9 1.0 CG X:HIS59 4.2 5.1 1.0 C2D X:HEM185 4.2 6.8 0.5 C3A X:HEM185 4.2 6.8 0.0 C3A X:HEM185 4.2 6.8 0.5 C3A X:HEM185 4.2 6.8 0.0 C3D X:HEM185 4.2 6.2 0.5 C2A X:HEM185 4.2 6.2 0.0 C2A X:HEM185 4.2 6.2 0.5 C2A X:HEM185 4.2 6.2 0.0 C2C X:HEM185 4.2 8.9 0.0 C2C X:HEM185 4.2 8.9 0.5 C2C X:HEM185 4.2 8.9 0.0 C3B X:HEM185 4.2 8.9 0.5 C3C X:HEM185 4.3 8.0 0.0 C3C X:HEM185 4.3 8.0 0.5 C3C X:HEM185 4.3 8.0 0.0 C2B X:HEM185 4.3 8.0 0.5 C3C X:HEM185 4.3 7.0 0.5 C2B X:HEM185 4.3 7.0 0.0 C2B X:HEM185 4.3 7.0 0.5 C2B X:HEM185 4.3 7.0 0.0 C2C X:HEM185 4.3 7.4 0.5 C3B X:HEM185 4.3 7.4 0.0 C3B X:HEM185 4.3 7.4 0.5 C3B X:HEM185 4.3 7.4 0.0 C2D X:HEM185 4.3 8.3 0.0 C2D X:HEM185 4.3 8.3 0.5 C2D X:HEM185 4.3 8.3 0.0 C3A X:HEM185 4.3 8.3 0.5 C3D X:HEM185 4.3 7.8 0.5 C3D X:HEM185 4.3 7.8 0.0 C3D X:HEM185 4.3 7.8 0.0 C2A X:HEM185 4.3 7.8 0.5 CD2 X:LEU130 4.7 14.6 0.7 CD2 X:LEU123 5.0 9.9 1.0

A.M.Amoia, W.R.Montfort. Heme Distortion in Nitrophorin 4: High Resolution Structures of Mutated Positions L123V and L133V and Heme Altered Proteins To Be Published.