Table 3.

Tertiary and quaternary structure differences of selected hemoglobins

	CO bovine (R)	Met horse (R)	CO human (R)	Oxy human (R)	Met pig (R)	CO human (Y)	CO human (R2)	Dxy human (T)
CO bovine (R)	—	0.44	0.61	0.65	0.63	0.64	0.67	0.80
	—	1.56	1.93	1.90	2.49	2.73	3.27	5.78
	—	2.4	4.5	4.9	5.6	7.9	9.2	13.2
Met horse (R)	0.44	—	0.54	0.57	0.57	0.56	0.62	0.78
	1.56	—	0.99	0.79	1.16	3.62	4.35	5.41
	2.4	—	2.1	2.7	3.6	8.8	10.5	13.0
CO human (R)	0.61	0.54	—	0.34	0.64	0.39	0.49	0.83
	1.93	0.99	—	0.57	1.26	3.82	4.55	5.19
	4.5	2.1	—	1.6	3.0	9.7	11.7	13.6
Oxy human (R)	0.65	0.57	0.34	—	0.65	0.23	0.45	0.82
	1.90	0.79	0.57	—	1.03	3.89	4.62	5.06
	4.9	2.7	1.6	—	1.4	11.1	13.0	12.2
Met pig (R)	0.63	0.57	0.64	0.65	—	0.66	0.76	0.78
	2.49	1.16	1.26	1.03	—	4.61	5.36	4.88
	5.6	3.6	3.0	1.4	—	12.3	14.1	10.8
CO human (Y)	0.64	0.56	0.39	0.23	0.66	—	0.40	0.85
	2.73	3.62	3.82	3.89	4.61	—	0.98	8.19
	7.9	8.8	9.7	11.1	12.3	—	2.3	21.1
CO human (R2)	0.67	0.62	0.49	0.45	0.76	0.40	—	0.92
	3.27	4.35	4.55	4.62	5.36	0.98	—	8.60
	9.2	10.5	11.7	13.0	14.1	2.3	—	22.1
Dxy human (T)	0.80	0.78	0.83	0.82	0.78	0.85	0.92	—
	5.78	5.41	5.19	5.06	4.88	8.19	8.60	—
	13.2	13.0	13.6	12.2	10.8	21.1	22.1	—

The Ca atoms (minus three residues at the terminal ends) were used for the superposition with the program LSQMAN (Kleywegt and Jones 1996). For each pair of hemoglobin tetramers compared, the top entry corresponds to the rmsd of the superimposed α1β1 dimers. The middle entry corresponds to the rmsd between the nonsuperimposed α2β2. The bottom entry corresponds to the rigid body rotation relating the nonsuperimposed α2β2 dimers. The rmsds and rigid body rotation differences are in Å and degrees, respectively.