Table 5.

Experimental distances used for modeling the rhodopsin helical bundle

Helix1	Helix2	Residue1	Residue2	Minimum distance	Maximum distance	Experimental method	Reference
C	F	139	248	6	20	Dipolar SDSL-EPRa	Farrens et al. 1996
C	F	139	249	9	26	Dipolar SDSL-EPRa	Farrens et al. 1996
C	F	139	250	9	26	Dipolar SDSL-EPRa	Farrens et al. 1996
C	F	139	251	6	20	Dipolar SDSL-EPRa	Farrens et al. 1996
C	F	139	252	9	26	Dipolar SDSL-EPRa	Farrens et al. 1996
A	G	65	316	4	19	Dipolar SDSL-EPRa	Yang et al. 1996
E	F	204	276	4	8	Disulfide mappingb	Yu et al. 1995
C	E	140	222	4	8	Disulfide mappingb	Yu et al. 1999
C	E	140	225	4	8	Disulfide mappingb	Yu et al. 1999
C	F	135	250	4	8	Disulfide mappingb	Yu et al. 1999
C	E	136	222	4	8	Disulfide mappingb	Cai et al. 1997
C	E	136	225	4	8	Disulfide mappingb	Cai et al. 1997
B	C	71	134	9	13	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
B	C	90	116	5	10	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
B	D	71	153	5	10	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
B	D	86	172	15	20	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
C	E	136	226	6	9	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
C	E	125	215	6	9	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
D	E	152	225	18	22	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
E	F	216	258	9	13	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
F	G	253	305	6	8	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
F	G	264	298	6	8	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
A	G	39	286	9	14	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
C	F	114	268	14	18	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
D	F	171	268	17	20	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
B	F	73	250	10	15	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
A	F	62	250	16	20	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001
A	F	47	264	16	19	Electron diffractionc	Unger and Schertler 1995; Yeagle et al. 2001

Helices A, B, C, D, E, F, G correspond to residues 33–65, 70–101, 105–140, 149–173, 199–226, 245–278, and 284–309, respectively.

^a Reported distance ranges were adjusted to account for the error involved in using spin–spin distances as Cα–Cα distances as described in the text.

^b Cα–Cα distances from disulfide mapping were set to 5.68 Å ± (reported error) as described in the text.

^c Cα–Cα distances correspond to distances measured from the top, middle, and bottom of consecutive helices as described by Yeagle et al. (2001).