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. 2003 Nov;12(11):2453–2475. doi: 10.1110/ps.03233703

Table 5.

Summary of distance proximity constraints on rhodopsin conformations based upon epitope mappings of selected mAbs

Constraint
Antibody name No. occurrences From To Avg. block sub. score Map type
Intradiskal
    B1gN 1 N 2 V 11 75% I
    B1gN 1 T 4 F 9 75% I
    B1gN 1 F 9 V 11 100% I
    B1gN 1 V 11 F 24 86% F
    B1gN 1 V 11 F 37 88% F
    B1gN 1 P 12 V 204 88% F
    B1gN 1 F 13 D 190 100% F
    B1gN 2 F 13 D 282 100% V
    B1gN 1 N 15 T 17 75% I
    B1gN 1 N 15 Q 28 100% F
    B1gN 2 N 15 Q 36 100% F
    B1gN 1 N 15 Q 184 100% F
    B1gN 1 N 15 Q 279 100% F
    B1gN 13 K 16 G 18 100% V
    B1gN 1 T 17 Y 29 42% I
    B1gN 1 V 19 Q 28 58% I
    B1gN 1 V 19 Y 30 75% I
    B1gN 1 S 22 F 24 100% F
    B1gN 1 Q 28 Y 191 88% F
    B1gN 5 Y 30 A 32 100% V
    B1gN 4 Y 30 I 189 88% F
    B1gN 2 Q 36 Y 191 88% F
    B1gN 1 Y 43 I 189 88% F
    B1gN 1 Q 184 Y 191 88% F
    B1gN 1 D 190 V 204 100% F
    B1gN 1 Y 191 Q 279 88% F
    B1gN 1 V 204 D 282 100% F
    B1gN 1 S 281 F 283 67% I
    B1gN 1 D 282 G 284 50% I
Cyloplasmic group I
    K42-41L 2 R 69 E 239 90% F
    K42-41L 1 R 69 S 338 100% F
    K42-41L 1 R 147 E 239 100% F
    K42-41L 1 R 147 S 338 100% F
    K42-41L 1 G 149 E 332 75% F
    K42-41L 1 E 150 A 235 75% F
    K42-41L 1 E 150 Q 237 81% F
    K42-41L 1 E 150 A 333 75% F
    K42-41L 1 K 231 A 234 67% I
    K42-41L 1 K 231 Q 238 81% F
    K42-41L 1 E 232 A 234 67% F
    K42-41L 1 A 233 Q 236 72% F
    K42-41L 1 A 233 Q 237 70% I
    K42-41L 1 Q 237 E 239 57% F
    K42-41L 1 Q 237 E 332 75% F
    K42-41L 4 Q 238 S 240 69% F
    K42-41L 4 Q 238 L 328 90% F
    K42-41L 4 E 239 K 245 77% V
    K42-41L 1 E 239 R 314 80% F
    K42-41L 3 S 240 K 248 58% F
    K42-41L 1 K 245 E 247 67% F
    K42-41L 1 K 245 E 249 67% F
    K42-41L 1 K 245 S 343 67% I
    K42041L 1 A 246 K 248 67% I
    K42-41L 3 G 324 N 326 75% F
    K42-41L 1 P 327 G 329 83% I
    K42-41L 1 G 329 T 342 100% I
Cytoplasmic group II
    K16-111c
    K16-111c 1 N 145 G 324 90% I
    K16-111c 1 N 145 P 347 100% I
    K16-111c 3 F 148 A 346 81% V
    K16-111c 1 N 151 G 324 90% H
    K16-111c 1 N 151 P 347 100% H
    K16-111c 3 E 232 V 318 75% F
    K16-111c 1 E 249 P 347 67% H
    K16-111c 1 T 251 G 329 75% H
    K16-111c 1 N 310 G 324 90% I
    K16-111c 1 N 310 P 347 100% I
    K16-111c 1 N 315 M 317 83% F
    K16-111c 1 N 315 P 327 83% F
    K16-111c 2 M 317 G 329 100% V
    K16-111c 1 V 318 N 326 75% I
    K16-111c 2 K 325 P 327 73% F
    K16-111c 1 N 326 M 317 90% F
    K16-111c 2 N 326 P 347 58% I
    K16-111c 3 P 327 G 329 100% I

Additional distance proximity constraints on rhodopsin confirmations, based on the other mAbs mapped are presented in Supplementary Material to this paper.

Epitope maps that contain rhodopsin sequence gaps were used to infer structural proximities in the folded protein, as explained in the text. Average block substitution scores were calculated using the amino acid similarity matrix (based on Table 3) between the phage display consensus epitope and all linearly continuous residues of rhodopsin that are mapped to on either side of a gap. "Map type" describes how the mapping was obtained: F = mapped with FINDMAP, I = mapped by manual Inspection, H = Hybrid of both methods (some residues held constant then mapped by FINDMAP), or V = aVeraged, in cases where the gap is present in multiple mappings from different source types.