Danish

Uniprot ID: P29474

Protein: Nitric oxide synthase 3
Organism: Human (Homo sapiens)
Length: 1203
Sequence:

MGNLKSVAQEPGPPCGLGLGLGLGLCGKQGPATPAPEPSRAPASLLPPAPEHSPPSSPLTQPPEGPKFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQGRPSPGPPAPEQLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDDPPELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPWKGSAAKGTGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGRLFRKAFDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSSPRPEQHKSYKIRFNSISCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHFCAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAARDIFSPKRSWKRQRYRLSAQAEGLQLLPGLIHVHRRKMFQATIRSVENLQSSKSTRATILVRLDTGGQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPAPTEPVAVEQLEKGSPGGPPPGWVRDPRLPPCTLRQALTFFLDITSPPSPQLLRLLSTLAEEPREQQELEALSQDPRRYEEWKWFRCPTLLEVLEQFPSVALPAPLLLTQLPLLQPRYYSVSSAPSTHPGEIHLTVAVLAYRTQDGLGPLHYGVCSTWLSQLKPGDPVPCFIRGAPSFRLPPDPSLPCILVGPGTGIAPFRGFWQERLHDIESKGLQPTPMTLVFGCRCSQLDHLYRDEVQNAQQRGVFGRVLTAFSREPDNPKTYVQDILRTELAAEVHRVLCLERGHMFVCGDVTMATNVLQTVQRILATEGDMELDEAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWAFDPPGSDTNSP

Number of chains: 374

PDB ID: pdb_00009cwi , Chain A
Resolution	1.73 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cwi , Chain B
Resolution	1.73 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cwi , Chain C
Resolution	1.73 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	BA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cwi , Chain D
Resolution	1.73 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	MA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00004d1p , Chain A
Resolution	1.73 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	C
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00004d1p , Chain B
Resolution	1.73 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	N
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwu , Chain A
Resolution	1.74 Å
Residue indices (Uniprot), coverage	67-480 (41-481), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, G482-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	C
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwu , Chain B
Resolution	1.74 Å
Residue indices (Uniprot), coverage	67-481 (41-481), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, G482-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006pp1 , Chain A
Resolution	1.76 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pp1 , Chain B
Resolution	1.76 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006pp1 , Chain C
Resolution	1.76 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006pp1 , Chain D
Resolution	1.76 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	HA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwo , Chain A
Resolution	1.76 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwo , Chain B
Resolution	1.76 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwo , Chain C
Resolution	1.76 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwo , Chain D
Resolution	1.76 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	KA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008uft , Chain A
Resolution	1.78 Å
Residue indices (Uniprot), coverage	66-480 (41-480), 0.37
Difference from Uniprot sequence	engineered mutation:variant
Mutations (UniProt numbering)	D298E, P370N
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9955
auth_asym_id	A
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008uft , Chain B
Resolution	1.78 Å
Residue indices (Uniprot), coverage	66-480 (41-480), 0.37
Difference from Uniprot sequence	engineered mutation:variant
Mutations (UniProt numbering)	D298E, P370N
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9955
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00008uft , Chain C
Resolution	1.78 Å
Residue indices (Uniprot), coverage	66-480 (41-480), 0.37
Difference from Uniprot sequence	engineered mutation:variant
Mutations (UniProt numbering)	D298E, P370N
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9955
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	AA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008uft , Chain D
Resolution	1.78 Å
Residue indices (Uniprot), coverage	66-480 (41-480), 0.37
Difference from Uniprot sequence	engineered mutation:variant
Mutations (UniProt numbering)	D298E, P370N
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9955
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	OA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008fgo , Chain A
Resolution	1.80 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00008fgo , Chain B
Resolution	1.80 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00008fgo , Chain C
Resolution	1.80 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	AA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008fgo , Chain D
Resolution	1.80 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	KA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nh8 , Chain A
Resolution	1.80 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nh8 , Chain B
Resolution	1.80 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nh8 , Chain C
Resolution	1.80 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	W
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nh8 , Chain D
Resolution	1.80 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	GA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mww , Chain A
Resolution	1.80 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mww , Chain B
Resolution	1.80 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mww , Chain C
Resolution	1.80 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	BA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009mww , Chain D
Resolution	1.80 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	OA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q51 , Chain A
Resolution	1.80 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q51 , Chain B
Resolution	1.80 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009q51 , Chain C
Resolution	1.80 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q51 , Chain D
Resolution	1.80 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	IA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00004d1o , Chain A
Resolution	1.82 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	D
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00004d1o , Chain B
Resolution	1.82 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	N
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nhf , Chain A
Resolution	1.83 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006nhf , Chain B
Resolution	1.83 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nhf , Chain C
Resolution	1.83 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	W
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006nhf , Chain D
Resolution	1.83 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	GA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cw7 , Chain A
Resolution	1.83 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cw7 , Chain B
Resolution	1.83 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cw7 , Chain C
Resolution	1.83 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	BA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cw7 , Chain D
Resolution	1.83 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	LA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwx , Chain A
Resolution	1.84 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mwx , Chain B
Resolution	1.84 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwx , Chain C
Resolution	1.84 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mwx , Chain D
Resolution	1.84 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	JA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008fgs , Chain A
Resolution	1.84 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00008fgs , Chain B
Resolution	1.84 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008fgs , Chain C
Resolution	1.84 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	BA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008fgs , Chain D
Resolution	1.84 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	NA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007tsg , Chain A
Resolution	1.85 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00007tsg , Chain B
Resolution	1.85 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007tsg , Chain C
Resolution	1.85 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00007tsg , Chain D
Resolution	1.85 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	JA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007tsm , Chain A
Resolution	1.85 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007tsm , Chain B
Resolution	1.85 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007tsm , Chain C
Resolution	1.85 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007tsm , Chain D
Resolution	1.85 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	IA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwp , Chain A
Resolution	1.86 Å
Residue indices (Uniprot), coverage	67-480 (41-481), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, G482-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	112ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	C
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mwp , Chain B
Resolution	1.86 Å
Residue indices (Uniprot), coverage	68-481 (41-481), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, G482-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008ufr , Chain A
Resolution	1.87 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008ufr , Chain B
Resolution	1.87 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008ufr , Chain C
Resolution	1.87 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	W
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008ufr , Chain D
Resolution	1.87 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	GA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgp , Chain A
Resolution	1.88 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgp , Chain B
Resolution	1.88 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008fgp , Chain C
Resolution	1.88 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgp , Chain D
Resolution	1.88 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	GA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cw5 , Chain A
Resolution	1.88 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00009cw5 , Chain B
Resolution	1.88 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cw5 , Chain C
Resolution	1.88 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	AA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cw5 , Chain D
Resolution	1.88 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	KA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009q53 , Chain A
Resolution	1.88 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q53 , Chain B
Resolution	1.88 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009q53 , Chain C
Resolution	1.88 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009q53 , Chain D
Resolution	1.88 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	JA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mwv , Chain A
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mwv , Chain B
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	S
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwv , Chain C
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	DA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.07 Å

PDB ID: pdb_00009mwv , Chain D
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	NA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mws , Chain A
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mws , Chain B
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mws , Chain C
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	109LEU-119ALA
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mws , Chain D
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	110GLN-117PRO
Structural gaps	Exists
label_asym_ids of heme	JA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nh7 , Chain A
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	C
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nh7 , Chain B
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	M
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007tsl , Chain A
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00007tsl , Chain B
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007tsl , Chain C
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	X
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007tsl , Chain D
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	IA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007uao , Chain A
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00007uao , Chain B
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	R
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007uao , Chain C
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	AA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007uao , Chain D
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	LA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008fgt , Chain A
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgt , Chain B
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgt , Chain C
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgt , Chain D
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	LA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cwj , Chain A
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00009cwj , Chain B
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	R
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cwj , Chain C
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	CA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cwj , Chain D
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	MA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cwk , Chain A
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cwk , Chain B
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cwk , Chain C
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cwk , Chain D
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	JA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwt , Chain A
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.07 Å

PDB ID: pdb_00009mwt , Chain B
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwt , Chain C
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwt , Chain D
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	IA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009q4z , Chain A
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009q4z , Chain B
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009q4z , Chain C
Resolution	1.90 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q4z , Chain D
Resolution	1.90 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	JA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006av7 , Chain A
Resolution	1.92 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.14 Å

PDB ID: pdb_00006av7 , Chain B
Resolution	1.92 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	N
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006av7 , Chain C
Resolution	1.92 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	U
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006av7 , Chain D
Resolution	1.92 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	EA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cw8 , Chain A
Resolution	1.92 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009cw8 , Chain B
Resolution	1.92 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.08 Å

PDB ID: pdb_00009cw8 , Chain C
Resolution	1.92 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cw8 , Chain D
Resolution	1.92 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	JA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cwd , Chain A
Resolution	1.92 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cwd , Chain B
Resolution	1.92 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cwd , Chain C
Resolution	1.92 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	AA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cwd , Chain D
Resolution	1.92 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	LA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwq , Chain A
Resolution	1.94 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	109LEU-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mwq , Chain B
Resolution	1.94 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	R
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwq , Chain C
Resolution	1.94 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	108LYS-120PRO
Structural gaps	Exists
label_asym_ids of heme	AA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwq , Chain D
Resolution	1.94 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	KA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mz4 , Chain A
Resolution	1.94 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.15 Å

PDB ID: pdb_00009mz4 , Chain B
Resolution	1.94 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mz4 , Chain C
Resolution	1.94 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009mz4 , Chain D
Resolution	1.94 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	JA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00006cie , Chain A
Resolution	1.95 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00006cie , Chain B
Resolution	1.95 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006cie , Chain C
Resolution	1.95 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	W
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006cie , Chain D
Resolution	1.95 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	GA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pp3 , Chain A
Resolution	1.95 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006pp3 , Chain B
Resolution	1.95 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pp3 , Chain C
Resolution	1.95 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006pp3 , Chain D
Resolution	1.95 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	GA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mz3 , Chain A
Resolution	1.95 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00009mz3 , Chain B
Resolution	1.95 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	T
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mz3 , Chain C
Resolution	1.95 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	EA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00009mz3 , Chain D
Resolution	1.95 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	QA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007m56 , Chain A
Resolution	1.96 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	88ALA-88ALA:107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	C
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007m56 , Chain B
Resolution	1.96 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	M
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nh5 , Chain A
Resolution	1.96 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00006nh5 , Chain B
Resolution	1.96 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nh5 , Chain C
Resolution	1.96 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nh5 , Chain D
Resolution	1.96 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	IA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00001m9m , Chain A
Resolution	1.96 Å
Residue indices (Uniprot), coverage	67-480 (67-481), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-P66, G482-P1203
Sequence identity to UniProt	0.9976
auth_asym_id	A
Missing residues	106PRO-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00001m9m , Chain B
Resolution	1.96 Å
Residue indices (Uniprot), coverage	67-480 (67-481), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-P66, G482-P1203
Sequence identity to UniProt	0.9976
auth_asym_id	B
Missing residues	106PRO-119ALA
Structural gaps	Exists
label_asym_ids of heme	K
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006pp0 , Chain A
Resolution	1.97 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006pp0 , Chain B
Resolution	1.97 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00006pp0 , Chain C
Resolution	1.97 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	W
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pp0 , Chain D
Resolution	1.97 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	GA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mwr , Chain A
Resolution	1.97 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009mwr , Chain B
Resolution	1.97 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	R
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mwr , Chain C
Resolution	1.97 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	BA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mwr , Chain D
Resolution	1.97 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	MA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008fgr , Chain A
Resolution	1.98 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00008fgr , Chain B
Resolution	1.98 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	R
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.22 Å

PDB ID: pdb_00008fgr , Chain C
Resolution	1.98 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00008fgr , Chain D
Resolution	1.98 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	LA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mz2 , Chain A
Resolution	1.99 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mz2 , Chain B
Resolution	1.99 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mz2 , Chain C
Resolution	1.99 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	AA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mz2 , Chain D
Resolution	1.99 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	KA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00007tso , Chain A
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007tso , Chain B
Resolution	2.00 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007tso , Chain C
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007tso , Chain D
Resolution	2.00 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	KA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007tsp , Chain A
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007tsp , Chain B
Resolution	2.00 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007tsp , Chain C
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00007tsp , Chain D
Resolution	2.00 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	KA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgu , Chain A
Resolution	2.00 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgu , Chain B
Resolution	2.00 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008fgu , Chain C
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	X
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgu , Chain D
Resolution	2.00 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	HA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009c1z , Chain A
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009c1z , Chain B
Resolution	2.00 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009c1z , Chain C
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	X
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009c1z , Chain D
Resolution	2.00 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	FA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cw4 , Chain A
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009cw4 , Chain B
Resolution	2.00 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cw4 , Chain C
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cw4 , Chain D
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	JA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mwn , Chain A
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-480 (41-481), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, G482-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mwn , Chain B
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-481 (41-481), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, G482-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mwn , Chain C
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-480 (41-481), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, G482-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	W
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mwn , Chain D
Resolution	2.00 Å
Residue indices (Uniprot), coverage	67-480 (41-481), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, G482-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	FA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00001m9k , Chain A
Resolution	2.01 Å
Residue indices (Uniprot), coverage	67-480 (67-481), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-P66, G482-P1203
Sequence identity to UniProt	0.9976
auth_asym_id	A
Missing residues	106PRO-119ALA
Structural gaps	Exists
label_asym_ids of heme	D
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00001m9k , Chain B
Resolution	2.01 Å
Residue indices (Uniprot), coverage	67-481 (67-481), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-P66, G482-P1203
Sequence identity to UniProt	0.9976
auth_asym_id	B
Missing residues	106PRO-119ALA
Structural gaps	Exists
label_asym_ids of heme	F
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00001m9q , Chain A
Resolution	2.01 Å
Residue indices (Uniprot), coverage	67-480 (67-481), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-P66, G482-P1203
Sequence identity to UniProt	0.9976
auth_asym_id	A
Missing residues	106PRO-119ALA
Structural gaps	Exists
label_asym_ids of heme	D
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00001m9q , Chain B
Resolution	2.01 Å
Residue indices (Uniprot), coverage	67-480 (67-481), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-P66, G482-P1203
Sequence identity to UniProt	0.9976
auth_asym_id	B
Missing residues	106PRO-119ALA
Structural gaps	Exists
label_asym_ids of heme	K
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nh3 , Chain A
Resolution	2.01 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006nh3 , Chain B
Resolution	2.01 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006nh3 , Chain C
Resolution	2.01 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	X
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006nh3 , Chain D
Resolution	2.01 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	JA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pp2 , Chain A
Resolution	2.02 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pp2 , Chain B
Resolution	2.02 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	M
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006pp2 , Chain C
Resolution	2.02 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	U
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pp2 , Chain D
Resolution	2.02 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	DA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.08 Å

PDB ID: pdb_00009q58 , Chain A
Resolution	2.03 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q58 , Chain B
Resolution	2.03 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q58 , Chain C
Resolution	2.03 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	W
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00009q58 , Chain D
Resolution	2.03 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	GA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pov , Chain A
Resolution	2.05 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pov , Chain B
Resolution	2.05 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pov , Chain C
Resolution	2.05 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006pov , Chain D
Resolution	2.05 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	HA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00007tsk , Chain A
Resolution	2.05 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007tsk , Chain B
Resolution	2.05 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007tsk , Chain C
Resolution	2.05 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007tsk , Chain D
Resolution	2.05 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	IA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008ufs , Chain A
Resolution	2.05 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict:engineered mutation
Mutations (UniProt numbering)	D298E, E361Q
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9955
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00008ufs , Chain B
Resolution	2.05 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	conflict:engineered mutation
Mutations (UniProt numbering)	D298E, E361Q
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9955
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008ufs , Chain C
Resolution	2.05 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict:engineered mutation
Mutations (UniProt numbering)	D298E, E361Q
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9955
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008ufs , Chain D
Resolution	2.05 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	conflict:engineered mutation
Mutations (UniProt numbering)	D298E, E361Q
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9955
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	IA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008ufu , Chain A
Resolution	2.05 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00008ufu , Chain B
Resolution	2.05 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00008ufu , Chain C
Resolution	2.05 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	W
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008ufu , Chain D
Resolution	2.05 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	IA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mz1 , Chain A
Resolution	2.05 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00009mz1 , Chain B
Resolution	2.05 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009mz1 , Chain C
Resolution	2.05 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009mz1 , Chain D
Resolution	2.05 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	LA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006av6 , Chain A
Resolution	2.08 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006av6 , Chain B
Resolution	2.08 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	N
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006av6 , Chain C
Resolution	2.08 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	W
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006av6 , Chain D
Resolution	2.08 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	EA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007tsn , Chain A
Resolution	2.08 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00007tsn , Chain B
Resolution	2.08 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007tsn , Chain C
Resolution	2.08 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	X
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00007tsn , Chain D
Resolution	2.08 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	KA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007tsi , Chain A
Resolution	2.10 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00007tsi , Chain B
Resolution	2.10 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00007tsi , Chain C
Resolution	2.10 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00007tsi , Chain D
Resolution	2.10 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	MA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009cw2 , Chain A
Resolution	2.10 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00009cw2 , Chain B
Resolution	2.10 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cw2 , Chain C
Resolution	2.10 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009cw2 , Chain D
Resolution	2.10 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	MA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009q4y , Chain A
Resolution	2.10 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-120PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009q4y , Chain B
Resolution	2.10 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q4y , Chain C
Resolution	2.10 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	X
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009q4y , Chain D
Resolution	2.10 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	GA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q55 , Chain A
Resolution	2.10 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q55 , Chain B
Resolution	2.10 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q55 , Chain C
Resolution	2.10 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	W
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009q55 , Chain D
Resolution	2.10 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	EA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009cw9 , Chain A
Resolution	2.12 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cw9 , Chain B
Resolution	2.12 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.08 Å

PDB ID: pdb_00009cw9 , Chain C
Resolution	2.12 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cw9 , Chain D
Resolution	2.12 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	KA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009q54 , Chain A
Resolution	2.13 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00009q54 , Chain B
Resolution	2.13 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009q54 , Chain C
Resolution	2.13 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	W
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00009q54 , Chain D
Resolution	2.13 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	GA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00007tsh , Chain A
Resolution	2.15 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00007tsh , Chain B
Resolution	2.15 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00007tsh , Chain C
Resolution	2.15 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00007tsh , Chain D
Resolution	2.15 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	JA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00005vvb , Chain A
Resolution	2.15 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00005vvb , Chain B
Resolution	2.15 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	N
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00005vvb , Chain C
Resolution	2.15 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	V
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00005vvb , Chain D
Resolution	2.15 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	EA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006pow , Chain A
Resolution	2.15 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006pow , Chain B
Resolution	2.15 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	M
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006pow , Chain C
Resolution	2.15 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	V
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pow , Chain D
Resolution	2.15 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	EA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00009q4x , Chain A
Resolution	2.15 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009q4x , Chain B
Resolution	2.15 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q4x , Chain C
Resolution	2.15 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-120PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q4x , Chain D
Resolution	2.15 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	IA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cw6 , Chain A
Resolution	2.15 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009cw6 , Chain B
Resolution	2.15 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009cw6 , Chain C
Resolution	2.15 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009cw6 , Chain D
Resolution	2.15 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	KA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00005uo8 , Chain A
Resolution	2.18 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.15 Å

PDB ID: pdb_00005uo8 , Chain B
Resolution	2.18 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	M
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00005uo8 , Chain C
Resolution	2.18 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	S
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00005uo8 , Chain D
Resolution	2.18 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	AA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00006nh6 , Chain A
Resolution	2.19 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00006nh6 , Chain B
Resolution	2.19 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	N
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00006nh6 , Chain C
Resolution	2.19 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	V
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006nh6 , Chain D
Resolution	2.19 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	GA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00005uo9 , Chain A
Resolution	2.19 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00005uo9 , Chain B
Resolution	2.19 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00005uo9 , Chain C
Resolution	2.19 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00005uo9 , Chain D
Resolution	2.19 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	HA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pou , Chain A
Resolution	2.19 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	G
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00006pou , Chain B
Resolution	2.19 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Q
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pou , Chain C
Resolution	2.19 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	AA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pou , Chain D
Resolution	2.19 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	KA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pou , Chain E
Resolution	2.19 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	E
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	TA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006pou , Chain F
Resolution	2.19 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	F
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	CB
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006pox , Chain A
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006pox , Chain B
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006pox , Chain C
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006pox , Chain D
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	HA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00005uoa , Chain A
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	C
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00005uoa , Chain B
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	N
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00005uoc , Chain A
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00005uoc , Chain B
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00005uoc , Chain C
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	X
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00005uoc , Chain D
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	IA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006cif , Chain A
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006cif , Chain B
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	N
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006cif , Chain C
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	V
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006cif , Chain D
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	FA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006poz , Chain A
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006poz , Chain B
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006poz , Chain C
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	W
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006poz , Chain D
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	FA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pp4 , Chain A
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006pp4 , Chain B
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	M
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006pp4 , Chain C
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	V
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00006pp4 , Chain D
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	CA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgn , Chain A
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgn , Chain B
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgn , Chain C
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	V
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgn , Chain D
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	FA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00008fgq , Chain A
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00008fgq , Chain B
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	N
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008fgq , Chain C
Resolution	2.20 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	V
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008fgq , Chain D
Resolution	2.20 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	FA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nh1 , Chain A
Resolution	2.22 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00006nh1 , Chain B
Resolution	2.22 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006nh1 , Chain C
Resolution	2.22 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Z
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006nh1 , Chain D
Resolution	2.22 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	HA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00005vvd , Chain A
Resolution	2.25 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00005vvd , Chain B
Resolution	2.25 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00005vvd , Chain C
Resolution	2.25 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00005vvd , Chain D
Resolution	2.25 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	GA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009q52 , Chain A
Resolution	2.25 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	107ARG-119ALA
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00009q52 , Chain B
Resolution	2.25 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q52 , Chain C
Resolution	2.25 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	X
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00009q52 , Chain D
Resolution	2.25 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	conflict
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	108LYS-118PRO
Structural gaps	Exists
label_asym_ids of heme	KA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006nh4 , Chain A
Resolution	2.27 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006nh4 , Chain B
Resolution	2.27 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00006nh4 , Chain C
Resolution	2.27 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	Y
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006nh4 , Chain D
Resolution	2.27 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	KA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00006nh2 , Chain A
Resolution	2.29 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006nh2 , Chain B
Resolution	2.29 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00006nh2 , Chain C
Resolution	2.29 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	X
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006nh2 , Chain D
Resolution	2.29 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	IA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00005uob , Chain A
Resolution	2.29 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00005uob , Chain B
Resolution	2.29 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	P
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00005uob , Chain C
Resolution	2.29 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	X
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00005uob , Chain D
Resolution	2.29 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	IA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006poy , Chain A
Resolution	2.30 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006poy , Chain B
Resolution	2.30 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	N
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006poy , Chain C
Resolution	2.30 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	V
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006poy , Chain D
Resolution	2.30 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Difference from Uniprot sequence	variant
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	EA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00003nos , Chain A
Resolution	2.40 Å
Residue indices (Uniprot), coverage	67-480 (66-492), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-G65, K493-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	108LYS-121GLU
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00003nos , Chain B
Resolution	2.40 Å
Residue indices (Uniprot), coverage	67-480 (66-492), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-G65, K493-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	108LYS-121GLU
Structural gaps	Exists
label_asym_ids of heme	H
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00005vvc , Chain A
Resolution	2.40 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00005vvc , Chain B
Resolution	2.40 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	109LEU-118PRO
Structural gaps	Exists
label_asym_ids of heme	O
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00005vvc , Chain C
Resolution	2.40 Å
Residue indices (Uniprot), coverage	68-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	C
Missing residues	107ARG-118PRO
Structural gaps	Exists
label_asym_ids of heme	W
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00005vvc , Chain D
Resolution	2.40 Å
Residue indices (Uniprot), coverage	67-480 (41-480), 0.37
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-R40, K481-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	D
Missing residues	110GLN-118PRO
Structural gaps	Exists
label_asym_ids of heme	GA
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00001m9j , Chain A
Resolution	2.43 Å
Residue indices (Uniprot), coverage	67-480 (67-481), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-P66, G482-P1203
Sequence identity to UniProt	0.9976
auth_asym_id	A
Missing residues	106PRO-119ALA
Structural gaps	Exists
label_asym_ids of heme	D
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00001m9j , Chain B
Resolution	2.43 Å
Residue indices (Uniprot), coverage	67-481 (67-481), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-P66, G482-P1203
Sequence identity to UniProt	0.9976
auth_asym_id	B
Missing residues	106PRO-119ALA
Structural gaps	Exists
label_asym_ids of heme	F
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00003eah , Chain A
Resolution	2.44 Å
Residue indices (Uniprot), coverage	37-446 (66-492), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-G65, K493-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	A
Missing residues	75PRO-88ALA
Structural gaps	Exists
label_asym_ids of heme	C
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00003eah , Chain B
Resolution	2.44 Å
Residue indices (Uniprot), coverage	36-446 (66-492), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-G65, K493-P1203
Sequence identity to UniProt	0.9977
auth_asym_id	B
Missing residues	76ARG-88ALA
Structural gaps	Exists
label_asym_ids of heme	L
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00001m9r , Chain A
Resolution	2.56 Å
Residue indices (Uniprot), coverage	67-480 (67-481), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-P66, G482-P1203
Sequence identity to UniProt	0.9976
auth_asym_id	A
Missing residues	106PRO-119ALA
Structural gaps	Exists
label_asym_ids of heme	D
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.09 Å

PDB ID: pdb_00001m9r , Chain B
Resolution	2.56 Å
Residue indices (Uniprot), coverage	67-480 (67-481), 0.35
Mutations (UniProt numbering)	D298E
Insertions	None
Deletions	M1-P66, G482-P1203
Sequence identity to UniProt	0.9976
auth_asym_id	B
Missing residues	106PRO-119ALA
Structural gaps	Exists
label_asym_ids of heme	G
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å