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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

Protein crystallography data

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

Iron Binding Sites:

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 2at0

Go back to Iron Binding Sites List in 2at0
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 0.0
FE X:HEM185 0.0 5.7 0.5
FE X:HEM185 0.0 5.7 0.0
N X:NO186 1.7 7.4 1.0
NA X:HEM185 2.0 6.0 0.0
NA X:HEM185 2.0 6.0 0.0
NA X:HEM185 2.0 6.0 0.5
ND X:HEM185 2.0 6.0 0.5
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
NA X:HEM185 2.0 6.4 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
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 0.0
C1A X:HEM185 3.0 5.8 0.5
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 0.0
C4A X:HEM185 3.0 6.0 0.5
C1D X:HEM185 3.0 6.0 0.5
C4C X:HEM185 3.0 6.3 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
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 0.5
C1D X:HEM185 3.0 7.2 0.0
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 0.5
C1C X:HEM185 3.0 7.7 0.0
C4B X:HEM185 3.0 7.0 0.0
C4B X:HEM185 3.0 7.0 0.0
C4B X:HEM185 3.0 7.0 0.5
C1C X:HEM185 3.0 7.0 0.5
C4C 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
C1B X:HEM185 3.0 7.0 0.5
C4D X:HEM185 3.0 6.6 0.0
C4D X:HEM185 3.0 6.6 0.5
C4D X:HEM185 3.0 6.6 0.0
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 0.5
CHC X:HEM185 3.4 8.3 0.5
CHC X:HEM185 3.4 8.3 0.0
CHC X:HEM185 3.4 8.3 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 0.0
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 0.0
C3A X:HEM185 4.2 6.8 0.5
C2A X:HEM185 4.2 6.2 0.5
C2A X:HEM185 4.2 6.2 0.0
C2A X:HEM185 4.2 6.2 0.0
C3D X:HEM185 4.2 6.2 0.5
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
C2B X:HEM185 4.3 8.0 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 7.0 0.5
C2B X:HEM185 4.3 7.0 0.0
C2B X:HEM185 4.3 7.0 0.0
C3C X:HEM185 4.3 7.0 0.5
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
C2A X:HEM185 4.3 7.8 0.5
C3D X:HEM185 4.3 7.8 0.0
C3D X:HEM185 4.3 7.8 0.5
C3D X:HEM185 4.3 7.8 0.0
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 2at0

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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 0.0
FE X:HEM185 0.0 5.7 0.5
FE X:HEM185 0.0 5.7 0.0
N X:NO186 1.7 7.4 1.0
NA X:HEM185 2.0 6.0 0.0
NA X:HEM185 2.0 6.0 0.0
NA X:HEM185 2.0 6.0 0.5
ND X:HEM185 2.0 6.0 0.5
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
NA X:HEM185 2.0 6.4 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
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 0.0
C1A X:HEM185 3.0 5.8 0.5
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 0.0
C4A X:HEM185 3.0 6.0 0.5
C1D X:HEM185 3.0 6.0 0.5
C4C X:HEM185 3.0 6.3 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
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 0.5
C1D X:HEM185 3.0 7.2 0.0
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 0.5
C1C X:HEM185 3.0 7.7 0.0
C4B X:HEM185 3.0 7.0 0.0
C4B X:HEM185 3.0 7.0 0.0
C4B X:HEM185 3.0 7.0 0.5
C1C X:HEM185 3.0 7.0 0.5
C4C 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
C1B X:HEM185 3.0 7.0 0.5
C4D X:HEM185 3.0 6.6 0.0
C4D X:HEM185 3.0 6.6 0.5
C4D X:HEM185 3.0 6.6 0.0
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 0.5
CHC X:HEM185 3.4 8.3 0.5
CHC X:HEM185 3.4 8.3 0.0
CHC X:HEM185 3.4 8.3 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 0.0
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 0.0
C3A X:HEM185 4.2 6.8 0.5
C2A X:HEM185 4.2 6.2 0.5
C2A X:HEM185 4.2 6.2 0.0
C2A X:HEM185 4.2 6.2 0.0
C3D X:HEM185 4.2 6.2 0.5
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
C2B X:HEM185 4.3 8.0 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 7.0 0.5
C2B X:HEM185 4.3 7.0 0.0
C2B X:HEM185 4.3 7.0 0.0
C3C X:HEM185 4.3 7.0 0.5
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
C2A X:HEM185 4.3 7.8 0.5
C3D X:HEM185 4.3 7.8 0.0
C3D X:HEM185 4.3 7.8 0.5
C3D X:HEM185 4.3 7.8 0.0
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 2at0

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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 0.0
FE X:HEM185 0.0 5.7 0.5
FE X:HEM185 0.0 5.7 0.0
N X:NO186 1.7 7.4 1.0
NA X:HEM185 2.0 6.0 0.0
NA X:HEM185 2.0 6.0 0.0
NA X:HEM185 2.0 6.0 0.5
ND X:HEM185 2.0 6.0 0.5
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
NA X:HEM185 2.0 6.4 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
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 0.0
C1A X:HEM185 3.0 5.8 0.5
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 0.0
C4A X:HEM185 3.0 6.0 0.5
C1D X:HEM185 3.0 6.0 0.5
C4C X:HEM185 3.0 6.3 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
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 0.5
C1D X:HEM185 3.0 7.2 0.0
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 0.5
C1C X:HEM185 3.0 7.7 0.0
C4B X:HEM185 3.0 7.0 0.0
C4B X:HEM185 3.0 7.0 0.0
C4B X:HEM185 3.0 7.0 0.5
C1C X:HEM185 3.0 7.0 0.5
C4C 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
C1B X:HEM185 3.0 7.0 0.5
C4D X:HEM185 3.0 6.6 0.0
C4D X:HEM185 3.0 6.6 0.5
C4D X:HEM185 3.0 6.6 0.0
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 0.5
CHC X:HEM185 3.4 8.3 0.5
CHC X:HEM185 3.4 8.3 0.0
CHC X:HEM185 3.4 8.3 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 0.0
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 0.0
C3A X:HEM185 4.2 6.8 0.5
C2A X:HEM185 4.2 6.2 0.5
C2A X:HEM185 4.2 6.2 0.0
C2A X:HEM185 4.2 6.2 0.0
C3D X:HEM185 4.2 6.2 0.5
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
C2B X:HEM185 4.3 8.0 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 7.0 0.5
C2B X:HEM185 4.3 7.0 0.0
C2B X:HEM185 4.3 7.0 0.0
C3C X:HEM185 4.3 7.0 0.5
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
C2A X:HEM185 4.3 7.8 0.5
C3D X:HEM185 4.3 7.8 0.0
C3D X:HEM185 4.3 7.8 0.5
C3D X:HEM185 4.3 7.8 0.0
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 2at0

Go back to Iron Binding Sites List in 2at0
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 0.0
FE X:HEM185 0.0 5.7 0.5
FE X:HEM185 0.0 5.7 0.0
N X:NO186 1.7 7.4 1.0
NA X:HEM185 2.0 6.0 0.0
NA X:HEM185 2.0 6.0 0.0
NA X:HEM185 2.0 6.0 0.5
ND X:HEM185 2.0 6.0 0.5
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
NA X:HEM185 2.0 6.4 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
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 0.0
C1A X:HEM185 3.0 5.8 0.5
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 0.0
C4A X:HEM185 3.0 6.0 0.5
C1D X:HEM185 3.0 6.0 0.5
C4C X:HEM185 3.0 6.3 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
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 0.5
C1D X:HEM185 3.0 7.2 0.0
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 0.5
C1C X:HEM185 3.0 7.7 0.0
C4B X:HEM185 3.0 7.0 0.0
C4B X:HEM185 3.0 7.0 0.0
C4B X:HEM185 3.0 7.0 0.5
C1C X:HEM185 3.0 7.0 0.5
C4C 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
C1B X:HEM185 3.0 7.0 0.5
C4D X:HEM185 3.0 6.6 0.0
C4D X:HEM185 3.0 6.6 0.5
C4D X:HEM185 3.0 6.6 0.0
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 0.5
CHC X:HEM185 3.4 8.3 0.5
CHC X:HEM185 3.4 8.3 0.0
CHC X:HEM185 3.4 8.3 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 0.0
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 0.0
C3A X:HEM185 4.2 6.8 0.5
C2A X:HEM185 4.2 6.2 0.5
C2A X:HEM185 4.2 6.2 0.0
C2A X:HEM185 4.2 6.2 0.0
C3D X:HEM185 4.2 6.2 0.5
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
C2B X:HEM185 4.3 8.0 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 7.0 0.5
C2B X:HEM185 4.3 7.0 0.0
C2B X:HEM185 4.3 7.0 0.0
C3C X:HEM185 4.3 7.0 0.5
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
C2A X:HEM185 4.3 7.8 0.5
C3D X:HEM185 4.3 7.8 0.0
C3D X:HEM185 4.3 7.8 0.5
C3D X:HEM185 4.3 7.8 0.0
CD2 X:LEU130 4.7 14.6 0.7
CD2 X:LEU123 5.0 9.9 1.0

Reference:

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.
Page generated: Sat Aug 3 19:22:28 2024

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