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ID of heme	Distortion Sort by saddling ruffling doming breathing	Axial ligands on heme		Function & structure
9hba-A-201	`sad. +0.13 ruf. -0.32 dom. -0.19 bre. -0.11`	HIS	chainID: A, resSeq: 87, molecule: Hemoglobin subunit alpha	oxygen carrier oligomeric count: 4 pocket vol.: 521.0 Å³ d(Fe-oop): 0.039 Å
9hba-A-201	`sad. +0.13 ruf. -0.32 dom. -0.19 bre. -0.11`	CMO	chainID: A, resSeq: 206, molecule: CARBON MONOXIDE
9hba-B-202	`sad. +0.17 ruf. -0.26 dom. -0.28 bre. -0.10`	HIS	chainID: B, resSeq: 92, molecule: Hemoglobin subunit beta	oxygen carrier oligomeric count: 4 pocket vol.: 516.0 Å³ d(Fe-oop): 0.043 Å
9hba-B-202	`sad. +0.17 ruf. -0.26 dom. -0.28 bre. -0.10`	CMO	chainID: B, resSeq: 206, molecule: CARBON MONOXIDE
9hba-C-203	`sad. +0.22 ruf. -0.27 dom. -0.24 bre. -0.04`	HIS	chainID: C, resSeq: 87, molecule: Hemoglobin subunit alpha	oxygen carrier oligomeric count: 4 pocket vol.: 535.0 Å³ d(Fe-oop): 0.016 Å
9hba-C-203	`sad. +0.22 ruf. -0.27 dom. -0.24 bre. -0.04`	CMO	chainID: C, resSeq: 204, molecule: CARBON MONOXIDE
9hba-D-201	`sad. +0.26 ruf. -0.31 dom. -0.20 bre. -0.04`	HIS	chainID: D, resSeq: 92, molecule: Hemoglobin subunit beta	oxygen carrier oligomeric count: 4 pocket vol.: 542.0 Å³ d(Fe-oop): 0.025 Å
9hba-D-201	`sad. +0.26 ruf. -0.31 dom. -0.20 bre. -0.04`	CMO	chainID: D, resSeq: 202, molecule: CARBON MONOXIDE