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ID of heme	Distortion Sort by saddling ruffling doming breathing	Axial ligands on heme		Function & structure
2qss-A-142	`sad. +0.22 ruf. -0.35 dom. -0.27 bre. -0.27`	HIS	chainID: A, resSeq: 87, molecule: Hemoglobin subunit alpha	oxygen carrier oligomeric count: 4 pocket vol.: 566.0 Å³ d(Fe-oop): 0.048 Å
2qss-A-142	`sad. +0.22 ruf. -0.35 dom. -0.27 bre. -0.27`	CMO	chainID: A, resSeq: 143, molecule: CARBON MONOXIDE
2qss-B-146	`sad. +0.24 ruf. -0.57 dom. -0.23 bre. -0.26`	HIS	chainID: B, resSeq: 91, molecule: Hemoglobin subunit beta	oxygen carrier oligomeric count: 4 pocket vol.: 551.0 Å³ d(Fe-oop): 0.028 Å
2qss-B-146	`sad. +0.24 ruf. -0.57 dom. -0.23 bre. -0.26`	CMO	chainID: B, resSeq: 147, molecule: CARBON MONOXIDE
2qss-C-142	`sad. +0.28 ruf. -0.37 dom. -0.31 bre. -0.23`	HIS	chainID: C, resSeq: 87, molecule: Hemoglobin subunit alpha	oxygen carrier oligomeric count: 4 pocket vol.: 526.0 Å³ d(Fe-oop): 0.068 Å
2qss-C-142	`sad. +0.28 ruf. -0.37 dom. -0.31 bre. -0.23`	CMO	chainID: C, resSeq: 143, molecule: CARBON MONOXIDE
2qss-D-146	`sad. +0.17 ruf. -0.00 dom. -0.25 bre. -0.29`	HIS	chainID: D, resSeq: 91, molecule: Hemoglobin subunit beta	oxygen carrier oligomeric count: 4 pocket vol.: 586.0 Å³ d(Fe-oop): 0.023 Å
2qss-D-146	`sad. +0.17 ruf. -0.00 dom. -0.25 bre. -0.29`	CMO	chainID: D, resSeq: 147, molecule: CARBON MONOXIDE