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ID of heme	Distortion Sort by saddling ruffling doming breathing	Axial ligands on heme		Function & structure
5urc-A-202	`sad. +0.27 ruf. -0.13 dom. -0.16 bre. -0.23`	HIS	chainID: A, resSeq: 87, molecule: Hemoglobin subunit alpha	oxygen carrier oligomeric count: 4 pocket vol.: 535.0 Å³ d(Fe-oop): 0.048 Å
5urc-A-202	`sad. +0.27 ruf. -0.13 dom. -0.16 bre. -0.23`	CMO	chainID: A, resSeq: 201, molecule: CARBON MONOXIDE
5urc-B-202	`sad. +0.15 ruf. -0.30 dom. -0.19 bre. -0.23`	HIS	chainID: B, resSeq: 92, molecule: Hemoglobin subunit beta	oxygen carrier oligomeric count: 4 pocket vol.: 561.0 Å³ d(Fe-oop): 0.052 Å
5urc-B-202	`sad. +0.15 ruf. -0.30 dom. -0.19 bre. -0.23`	CMO	chainID: B, resSeq: 201, molecule: CARBON MONOXIDE
5urc-C-202	`sad. +0.32 ruf. -0.03 dom. -0.19 bre. -0.18`	HIS	chainID: C, resSeq: 87, molecule: Hemoglobin subunit alpha	oxygen carrier oligomeric count: 4 pocket vol.: 550.0 Å³ d(Fe-oop): 0.065 Å
5urc-C-202	`sad. +0.32 ruf. -0.03 dom. -0.19 bre. -0.18`	CMO	chainID: C, resSeq: 201, molecule: CARBON MONOXIDE
5urc-D-202	`sad. +0.32 ruf. -0.29 dom. -0.21 bre. -0.21`	HIS	chainID: D, resSeq: 92, molecule: Hemoglobin subunit beta	oxygen carrier oligomeric count: 4 pocket vol.: 550.0 Å³ d(Fe-oop): 0.002 Å
5urc-D-202	`sad. +0.32 ruf. -0.29 dom. -0.21 bre. -0.21`	CMO	chainID: D, resSeq: 201, molecule: CARBON MONOXIDE