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ID of heme	Distortion Sort by saddling ruffling doming breathing default	Axial ligands on heme		Function & structure
28od-A-201	`sad. +0.11 ruf. -0.28 dom. -0.20 bre. -0.04`	HIS	chainID: A, resSeq: 87, molecule: Hemoglobin subunit alpha	oxygen carrier oligomeric count: 4 pocket vol.: 533.0 Å³ d(Fe-oop): 0.036 Å
28od-A-201	`sad. +0.11 ruf. -0.28 dom. -0.20 bre. -0.04`	CMO	chainID: A, resSeq: 206, molecule: CARBON MONOXIDE
28od-B-202	`sad. +0.15 ruf. -0.25 dom. -0.25 bre. -0.13`	HIS	chainID: B, resSeq: 92, molecule: Hemoglobin subunit beta	oxygen carrier oligomeric count: 4 pocket vol.: 517.0 Å³ d(Fe-oop): 0.025 Å
28od-B-202	`sad. +0.15 ruf. -0.25 dom. -0.25 bre. -0.13`	CMO	chainID: B, resSeq: 205, molecule: CARBON MONOXIDE
28od-C-204	`sad. +0.24 ruf. -0.27 dom. -0.23 bre. -0.08`	HIS	chainID: C, resSeq: 87, molecule: Hemoglobin subunit alpha	oxygen carrier oligomeric count: 4 pocket vol.: 528.0 Å³ d(Fe-oop): 0.021 Å
28od-C-204	`sad. +0.24 ruf. -0.27 dom. -0.23 bre. -0.08`	CMO	chainID: C, resSeq: 205, molecule: CARBON MONOXIDE
28od-D-201	`sad. +0.32 ruf. -0.31 dom. -0.18 bre. -0.01`	HIS	chainID: D, resSeq: 92, molecule: Hemoglobin subunit beta	oxygen carrier oligomeric count: 4 pocket vol.: 558.0 Å³ d(Fe-oop): 0.017 Å
28od-D-201	`sad. +0.32 ruf. -0.31 dom. -0.18 bre. -0.01`	CMO	chainID: D, resSeq: 202, molecule: CARBON MONOXIDE