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ID of heme	Distortion Sort by saddling ruffling doming breathing default	Axial ligands on heme		Function & structure
3pi9-A-142	`sad. +0.15 ruf. -0.50 dom. -0.36 bre. +0.51`	HIS	chainID: A, resSeq: 87, molecule: Hemoglobin subunit alpha	oxygen carrier oligomeric count: 4 pocket vol.: 469.0 Å³ d(Fe-oop): 0.011 Å
3pi9-A-142	`sad. +0.15 ruf. -0.50 dom. -0.36 bre. +0.51`	CMO	chainID: A, resSeq: 143, molecule: CARBON MONOXIDE
3pi9-B-147	`sad. +0.22 ruf. -0.58 dom. -0.12 bre. +0.65`	HIS	chainID: B, resSeq: 92, molecule: Hemoglobin subunit beta	oxygen carrier oligomeric count: 4 pocket vol.: 571.0 Å³ d(Fe-oop): 0.165 Å
3pi9-B-147	`sad. +0.22 ruf. -0.58 dom. -0.12 bre. +0.65`	CMO	chainID: B, resSeq: 148, molecule: CARBON MONOXIDE
3pi9-C-142	`sad. +0.33 ruf. -0.01 dom. -0.32 bre. +0.56`	HIS	chainID: C, resSeq: 87, molecule: Hemoglobin subunit alpha	oxygen carrier oligomeric count: 4 pocket vol.: 497.0 Å³ d(Fe-oop): 0.001 Å
3pi9-C-142	`sad. +0.33 ruf. -0.01 dom. -0.32 bre. +0.56`	CMO	chainID: C, resSeq: 143, molecule: CARBON MONOXIDE
3pi9-D-147	`sad. +0.22 ruf. -0.10 dom. -0.33 bre. +0.48`	HIS	chainID: D, resSeq: 92, molecule: Hemoglobin subunit beta	oxygen carrier oligomeric count: 4 pocket vol.: 518.0 Å³ d(Fe-oop): 0.119 Å
3pi9-D-147	`sad. +0.22 ruf. -0.10 dom. -0.33 bre. +0.48`	CMO	chainID: D, resSeq: 148, molecule: CARBON MONOXIDE