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ID of heme	Distortion Sort by saddling ruffling doming breathing	Axial ligands on heme		Function & structure
3ic2-A-143	`sad. +0.12 ruf. -0.21 dom. -0.25 bre. -0.28`	HIS	chainID: A, resSeq: 87, molecule: Hemoglobin subunit alpha	oxygen carrier oligomeric count: 4 pocket vol.: 512.0 Å³ d(Fe-oop): 0.102 Å
3ic2-A-143	`sad. +0.12 ruf. -0.21 dom. -0.25 bre. -0.28`	OXY	chainID: A, resSeq: 142, molecule: OXYGEN MOLECULE
3ic2-B-148	`sad. +0.29 ruf. -0.22 dom. -0.19 bre. -0.23`	HIS	chainID: B, resSeq: 92, molecule: Hemoglobin subunit beta	oxygen carrier oligomeric count: 4 pocket vol.: 534.0 Å³ d(Fe-oop): 0.087 Å
3ic2-B-148	`sad. +0.29 ruf. -0.22 dom. -0.19 bre. -0.23`	OXY	chainID: B, resSeq: 147, molecule: OXYGEN MOLECULE
3ic2-C-143	`sad. +0.32 ruf. -0.09 dom. -0.22 bre. -0.17`	HIS	chainID: C, resSeq: 87, molecule: Hemoglobin subunit alpha	oxygen carrier oligomeric count: 4 pocket vol.: 552.0 Å³ d(Fe-oop): 0.067 Å
3ic2-C-143	`sad. +0.32 ruf. -0.09 dom. -0.22 bre. -0.17`	OXY	chainID: C, resSeq: 142, molecule: OXYGEN MOLECULE
3ic2-D-148	`sad. +0.38 ruf. -0.31 dom. -0.14 bre. -0.16`	HIS	chainID: D, resSeq: 92, molecule: Hemoglobin subunit beta	oxygen carrier oligomeric count: 4 pocket vol.: 546.0 Å³ d(Fe-oop): 0.022 Å
3ic2-D-148	`sad. +0.38 ruf. -0.31 dom. -0.14 bre. -0.16`	OXY	chainID: D, resSeq: 147, molecule: OXYGEN MOLECULE