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ID of heme	Distortion Sort by saddling ruffling doming breathing	Axial ligands on heme		Function & structure
1m9p-A-142	`sad. +0.31 ruf. -0.14 dom. -0.18 bre. +0.20`	HIS	chainID: A, resSeq: 87, molecule: Hemoglobin alpha chain	oxygen carrier oligomeric count: 4 pocket vol.: 528.0 Å³ d(Fe-oop): 0.028 Å
1m9p-A-142	`sad. +0.31 ruf. -0.14 dom. -0.18 bre. +0.20`	CMO	chainID: A, resSeq: 543, molecule: CARBON MONOXIDE
1m9p-B-147	`sad. +0.30 ruf. -0.97 dom. -0.24 bre. +0.20`	HIS	chainID: B, resSeq: 92, molecule: Hemoglobin beta chain	oxygen carrier oligomeric count: 4 pocket vol.: 538.0 Å³ d(Fe-oop): 0.024 Å
1m9p-B-147	`sad. +0.30 ruf. -0.97 dom. -0.24 bre. +0.20`	CMO	chainID: B, resSeq: 544, molecule: CARBON MONOXIDE
1m9p-C-142	`sad. +0.14 ruf. -0.10 dom. -0.02 bre. +0.29`	HIS	chainID: C, resSeq: 87, molecule: Hemoglobin alpha chain	oxygen carrier oligomeric count: 4 pocket vol.: 495.0 Å³ d(Fe-oop): 0.004 Å
1m9p-C-142	`sad. +0.14 ruf. -0.10 dom. -0.02 bre. +0.29`	CMO	chainID: C, resSeq: 545, molecule: CARBON MONOXIDE
1m9p-D-147	`sad. +0.33 ruf. -0.41 dom. -0.14 bre. +0.06`	HIS	chainID: D, resSeq: 92, molecule: Hemoglobin beta chain	oxygen carrier oligomeric count: 4 pocket vol.: 526.0 Å³ d(Fe-oop): 0.052 Å
1m9p-D-147	`sad. +0.33 ruf. -0.41 dom. -0.14 bre. +0.06`	CMO	chainID: D, resSeq: 546, molecule: CARBON MONOXIDE