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Uniprot ID: P04252

Protein: Bacterial hemoglobin
Organism: Vitreoscilla stercoraria
Length: 146
Sequence:

MLDQQTINIIKATVPVLKEHGVTITTTFYKNLFAKHPEVRPLFDMGRQESLEQPKALAMTVLAAAQNIENLPAILPAVKKIAVKHCQAGVAAAHYPIVGQELLGAIKEVLGDAATDDILDAWGKAYGVIADVFIQVEADLYAQAVE

Number of chains: 14

PDB ID: pdb_00003tm9 , Chain A
Resolution	1.72 Å
Residue indices (Uniprot), coverage	1-146 (1-146), 1.00
Difference from Uniprot sequence	engineered mutation
Mutations (UniProt numbering)	Y29A
Insertions	None
Deletions	None
Sequence identity to UniProt	0.9932
auth_asym_id	A
label_asym_ids of heme	B
Available structure	PDB

PDB ID: pdb_00003tm9 , Chain A-1
Resolution	1.72 Å
Residue indices (Uniprot), coverage	1-146 (1-146), 1.00
Difference from Uniprot sequence	engineered mutation
Mutations (UniProt numbering)	Y29A
Insertions	None
Deletions	None
Sequence identity to UniProt	0.9932
auth_asym_id	A
label_asym_ids of heme	B-1
Available structure	PDB

PDB ID: pdb_00003tm3 , Chain A
Resolution	1.75 Å
Residue indices (Uniprot), coverage	1-146 (1-146), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	A
Missing residues	47ARG-48GLN
Structural gaps	Exists
label_asym_ids of heme	B
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.16 Å

PDB ID: pdb_00003tm3 , Chain A-1
Resolution	1.75 Å
Residue indices (Uniprot), coverage	1-146 (1-146), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	A
Missing residues	47ARG-48GLN
Structural gaps	Exists
label_asym_ids of heme	B-1
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.16 Å

PDB ID: pdb_00002vhb , Chain A
Resolution	1.76 Å
Residue indices (Uniprot), coverage	2-146 (1-146), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	A
Missing residues	44ASP-51LEU
Structural gaps	Exists
label_asym_ids of heme	D
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00002vhb , Chain B
Resolution	1.76 Å
Residue indices (Uniprot), coverage	2-145 (1-146), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	B
Missing residues	44ASP-50SER
Structural gaps	Exists
label_asym_ids of heme	F
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00004vhb , Chain A
Resolution	1.80 Å
Residue indices (Uniprot), coverage	1-146 (1-146), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	A
Missing residues	44ASP-51LEU
Structural gaps	Exists
label_asym_ids of heme	D
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.15 Å

PDB ID: pdb_00004vhb , Chain B
Resolution	1.80 Å
Residue indices (Uniprot), coverage	2-145 (1-146), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	B
Missing residues	44ASP-50SER
Structural gaps	Exists
label_asym_ids of heme	F
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00001vhb , Chain A
Resolution	1.83 Å
Residue indices (Uniprot), coverage	2-145 (1-146), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	A
Missing residues	44ASP-52GLU
Structural gaps	Exists
label_asym_ids of heme	C
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å

PDB ID: pdb_00001vhb , Chain B
Resolution	1.83 Å
Residue indices (Uniprot), coverage	2-145 (1-146), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	B
Missing residues	44ASP-52GLU
Structural gaps	Exists
label_asym_ids of heme	D
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00003tld , Chain A
Resolution	1.90 Å
Residue indices (Uniprot), coverage	1-146 (1-146), 1.00
Difference from Uniprot sequence	engineered mutation
Mutations (UniProt numbering)	Y29F
Insertions	None
Deletions	None
Sequence identity to UniProt	0.9932
auth_asym_id	A
Missing residues	47ARG-48GLN
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_00003tld , Chain B
Resolution	1.90 Å
Residue indices (Uniprot), coverage	1-146 (1-146), 1.00
Difference from Uniprot sequence	engineered mutation
Mutations (UniProt numbering)	Y29F
Insertions	None
Deletions	None
Sequence identity to UniProt	0.9932
auth_asym_id	B
Missing residues	47ARG-48GLN
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_00003vhb , Chain A
Resolution	2.10 Å
Residue indices (Uniprot), coverage	2-145 (1-146), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	A
Missing residues	44ASP-52GLU
Structural gaps	Exists
label_asym_ids of heme	C
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.18 Å

PDB ID: pdb_00003vhb , Chain B
Resolution	2.10 Å
Residue indices (Uniprot), coverage	2-145 (1-146), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	B
Missing residues	44ASP-52GLU
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.16 Å