GPCompReports

EDNRB

Gene EDNRB Endothelin receptors Peptide receptors UniProt P24530
802
Total Contact Pairs
79
Significant Changes
6.31
Max Increase
-19.11
Max Decrease

Interactive snake plot

GPCRdb-style topology. Click the view buttons to recolor residues by different data layers. Toggle contact links to draw significant residue-residue contacts as arcs. Click loop labels (ICL/ECL) to expand or collapse loop regions.

Color convention: blue = active-favoring, red = inactive-favoring.

ICL1 K130 12.48x48 K130 12.48x48 K C131 12.49x49 C131 12.49x49 C M132 12.50x50 M132 12.50x50 M R133 12.51x51 R133 12.51x51 R N134 12.52x52 N134 12.52x52 N ICL1ECL1 E165 E165 E D166 23.49x49 D166 23.49x49 D W167 23.50x50 W167 23.50x50 W P168 23.51x51 P168 23.51x51 P F169 23.52x52 F169 23.52x52 F ECL1ICL2 W206 34.50x50 W206 34.50x50 W S207 34.51x51 S207 34.51x51 S R208 34.52x52 R208 34.52x52 R I209 34.53x53 I209 34.53x53 I K210 34.54x54 K210 34.54x54 K G211 34.55x55 G211 34.55x55 G I212 34.56x56 I212 34.56x56 I G213 34.57x57 G213 34.57x57 G ICL2ECL2 D241 D241 D I242 I242 I I243 I243 I T244 T244 T M245 M245 M D246 D246 D Y247 Y247 Y K248 K248 K G249 G249 G S250 S250 S Y251 Y251 Y L252 L252 L R253 R253 R I254 I254 I C255 45.50x50 C255 45.50x50 C L256 45.51x51 L256 45.51x51 L L257 45.52x52 L257 45.52x52 L H258 H258 H P259 P259 P V260 V260 V Q261 Q261 Q K262 K262 K ECL2ICL3 Q308 Q308 Q I309 I309 I A310 A310 A L311 L311 L ICL3ECL3 N351 N351 N Q352 Q352 Q N353 N353 N D354 D354 D P355 P355 P N356 N356 N ECL3N-term M1 M1 M Q2 Q2 Q P3 P3 P P4 P4 P P5 P5 P S6 S6 S L7 L7 L C8 C8 C G9 G9 G R10 R10 R A11 A11 A L12 L12 L V13 V13 V A14 A14 A L15 L15 L V16 V16 V L17 L17 L A18 A18 A C19 C19 C G20 G20 G L21 L21 L S22 S22 S R23 R23 R I24 I24 I W25 W25 W G26 G26 G E27 E27 E E28 E28 E R29 R29 R G30 G30 G F31 F31 F P32 P32 P P33 P33 P D34 D34 D R35 R35 R A36 A36 A T37 T37 T P38 P38 P L39 L39 L L40 L40 L Q41 Q41 Q T42 T42 T A43 A43 A E44 E44 E I45 I45 I M46 M46 M T47 T47 T P48 P48 P P49 P49 P T50 T50 T K51 K51 K T52 T52 T L53 L53 L W54 W54 W P55 P55 P K56 K56 K G57 G57 G S58 S58 S N59 N59 N A60 A60 A S61 S61 S L62 L62 L A63 A63 A R64 R64 R S65 S65 S L66 L66 L A67 A67 A P68 P68 P A69 A69 A E70 E70 E V71 V71 V P72 P72 P K73 K73 K G74 G74 G D75 D75 D R76 R76 R T77 T77 T A78 A78 A G79 G79 G S80 S80 S P81 P81 P P82 P82 P R83 R83 R T84 T84 T I85 I85 I S86 S86 S P87 P87 P P88 P88 P P89 P89 P C90 C90 C N-termC-term W404 W404 W C405 C405 C Q406 Q406 Q S407 S407 S F408 F408 F E409 E409 E E410 E410 E K411 K411 K Q412 Q412 Q S413 S413 S L414 L414 L E415 E415 E E416 E416 E K417 K417 K Q418 Q418 Q S419 S419 S C420 C420 C L421 L421 L K422 K422 K F423 F423 F K424 K424 K A425 A425 A N426 N426 N D427 D427 D H428 H428 H G429 G429 G Y430 Y430 Y D431 D431 D N432 N432 N F433 F433 F R434 R434 R S435 S435 S S436 S436 S N437 N437 N K438 K438 K Y439 Y439 Y S440 S440 S S441 S441 S S442 S442 S C-term Q91 1.22x22 Q91 1.22x22 Q G92 1.23x23 G92 1.23x23 G P93 1.24x24 P93 1.24x24 P I94 1.25x25 I94 1.25x25 I E95 1.26x26 E95 1.26x26 E I96 1.27x27 I96 1.27x27 I K97 1.28x28 K97 1.28x28 K E98 1.29x29 E98 1.29x29 E T99 1.30x30 T99 1.30x30 T F100 1.31x31 F100 1.31x31 F K101 1.32x32 K101 1.32x32 K Y102 1.33x33 Y102 1.33x33 Y I103 1.34x34 I103 1.34x34 I N104 1.35x35 N104 1.35x35 N T105 1.36x36 T105 1.36x36 T V106 1.37x37 V106 1.37x37 V V107 1.38x38 V107 1.38x38 V S108 1.39x39 S108 1.39x39 S C109 1.40x40 C109 1.40x40 C L110 1.41x41 L110 1.41x41 L V111 1.42x42 V111 1.42x42 V F112 1.43x43 F112 1.43x43 F V113 1.44x44 V113 1.44x44 V L114 1.45x45 L114 1.45x45 L G115 1.46x46 G115 1.46x46 G I116 1.47x47 I116 1.47x47 I I117 1.48x48 I117 1.48x48 I G118 1.49x49 G118 1.49x49 G N119 1.50x50 N119 1.50x50 N S120 1.51x51 S120 1.51x51 S T121 1.52x52 T121 1.52x52 T L122 1.53x53 L122 1.53x53 L L123 1.54x54 L123 1.54x54 L R124 1.55x55 R124 1.55x55 R I125 1.56x56 I125 1.56x56 I I126 1.57x57 I126 1.57x57 I Y127 1.58x58 Y127 1.58x58 Y K128 1.59x59 K128 1.59x59 K N129 1.60x60 N129 1.60x60 N G135 2.38x38 G135 2.38x38 G P136 2.39x39 P136 2.39x39 P N137 2.40x40 N137 2.40x40 N I138 2.41x41 I138 2.41x41 I L139 2.42x42 L139 2.42x42 L I140 2.43x43 I140 2.43x43 I A141 2.44x44 A141 2.44x44 A S142 2.45x45 S142 2.45x45 S L143 2.46x46 L143 2.46x46 L A144 2.47x47 A144 2.47x47 A L145 2.48x48 L145 2.48x48 L G146 2.49x49 G146 2.49x49 G D147 2.50x50 D147 2.50x50 D L148 2.51x51 L148 2.51x51 L L149 2.52x52 L149 2.52x52 L H150 2.53x53 H150 2.53x53 H I151 2.54x54 I151 2.54x54 I V152 2.55x55 V152 2.55x55 V I153 2.56x551 I153 2.56x551 I D154 2.57x56 D154 2.57x56 D I155 2.58x57 I155 2.58x57 I P156 2.59x58 P156 2.59x58 P I157 2.60x59 I157 2.60x59 I N158 2.61x60 N158 2.61x60 N V159 2.62x61 V159 2.62x61 V Y160 2.63x62 Y160 2.63x62 Y K161 2.64x63 K161 2.64x63 K L162 2.65x64 L162 2.65x64 L L163 2.66x65 L163 2.66x65 L A164 2.67x66 A164 2.67x66 A G170 3.21x21 G170 3.21x21 G A171 3.22x22 A171 3.22x22 A E172 3.23x23 E172 3.23x23 E M173 3.24x24 M173 3.24x24 M C174 3.25x25 C174 3.25x25 C K175 3.26x26 K175 3.26x26 K L176 3.27x27 L176 3.27x27 L V177 3.28x28 V177 3.28x28 V P178 3.29x29 P178 3.29x29 P F179 3.30x30 F179 3.30x30 F I180 3.31x31 I180 3.31x31 I Q181 3.32x32 Q181 3.32x32 Q K182 3.33x33 K182 3.33x33 K A183 3.34x34 A183 3.34x34 A S184 3.35x35 S184 3.35x35 S V185 3.36x36 V185 3.36x36 V G186 3.37x37 G186 3.37x37 G I187 3.38x38 I187 3.38x38 I T188 3.39x39 T188 3.39x39 T V189 3.40x40 V189 3.40x40 V L190 3.41x41 L190 3.41x41 L S191 3.42x42 S191 3.42x42 S L192 3.43x43 L192 3.43x43 L C193 3.44x44 C193 3.44x44 C A194 3.45x45 A194 3.45x45 A L195 3.46x46 L195 3.46x46 L S196 3.47x47 S196 3.47x47 S I197 3.48x48 I197 3.48x48 I D198 3.49x49 D198 3.49x49 D R199 3.50x50 R199 3.50x50 R Y200 3.51x51 Y200 3.51x51 Y R201 3.52x52 R201 3.52x52 R A202 3.53x53 A202 3.53x53 A V203 3.54x54 V203 3.54x54 V A204 3.55x55 A204 3.55x55 A S205 3.56x56 S205 3.56x56 S V214 4.38x38 V214 4.38x38 V P215 4.39x39 P215 4.39x39 P K216 4.40x40 K216 4.40x40 K W217 4.41x41 W217 4.41x41 W T218 4.42x42 T218 4.42x42 T A219 4.43x43 A219 4.43x43 A V220 4.44x44 V220 4.44x44 V E221 4.45x45 E221 4.45x45 E I222 4.46x46 I222 4.46x46 I V223 4.47x47 V223 4.47x47 V L224 4.48x48 L224 4.48x48 L I225 4.49x49 I225 4.49x49 I W226 4.50x50 W226 4.50x50 W V227 4.51x51 V227 4.51x51 V V228 4.52x52 V228 4.52x52 V S229 4.53x53 S229 4.53x53 S V230 4.54x54 V230 4.54x54 V V231 4.55x55 V231 4.55x55 V L232 4.56x56 L232 4.56x56 L A233 4.57x57 A233 4.57x57 A V234 4.58x59 V234 4.58x59 V P235 4.59x60 P235 4.59x60 P E236 4.60x61 E236 4.60x61 E A237 4.61x62 A237 4.61x62 A I238 4.62x63 I238 4.62x63 I G239 4.63x64 G239 4.63x64 G F240 4.64x65 F240 4.64x65 F T263 5.28x29 T263 5.28x29 T A264 5.29x30 A264 5.29x30 A F265 5.30x31 F265 5.30x31 F M266 5.31x32 M266 5.31x32 M Q267 5.32x33 Q267 5.32x33 Q F268 5.33x34 F268 5.33x34 F Y269 5.34x35 Y269 5.34x35 Y K270 5.35x36 K270 5.35x36 K T271 5.36x37 T271 5.36x37 T A272 5.37x38 A272 5.37x38 A K273 5.38x39 K273 5.38x39 K D274 5.39x40 D274 5.39x40 D W275 5.40x41 W275 5.40x41 W W276 5.41x42 W276 5.41x42 W L277 5.42x43 L277 5.42x43 L F278 5.43x44 F278 5.43x44 F S279 5.44x45 S279 5.44x45 S F280 5.45x46 F280 5.45x46 F Y281 5.46x461 Y281 5.46x461 Y F282 5.47x47 F282 5.47x47 F C283 5.48x48 C283 5.48x48 C L284 5.49x49 L284 5.49x49 L P285 5.50x50 P285 5.50x50 P L286 5.51x51 L286 5.51x51 L A287 5.52x52 A287 5.52x52 A I288 5.53x53 I288 5.53x53 I T289 5.54x54 T289 5.54x54 T A290 5.55x55 A290 5.55x55 A F291 5.56x56 F291 5.56x56 F F292 5.57x57 F292 5.57x57 F Y293 5.58x58 Y293 5.58x58 Y T294 5.59x59 T294 5.59x59 T L295 5.60x60 L295 5.60x60 L M296 5.61x61 M296 5.61x61 M T297 5.62x62 T297 5.62x62 T C298 5.63x63 C298 5.63x63 C E299 5.64x64 E299 5.64x64 E M300 5.65x65 M300 5.65x65 M L301 5.66x66 L301 5.66x66 L R302 5.67x67 R302 5.67x67 R K303 5.68x68 K303 5.68x68 K K304 5.69x69 K304 5.69x69 K S305 5.70x70 S305 5.70x70 S G306 5.71x71 G306 5.71x71 G M307 5.72x72 M307 5.72x72 M N312 6.24x24 N312 6.24x24 N D313 6.25x25 D313 6.25x25 D H314 6.26x26 H314 6.26x26 H L315 6.27x27 L315 6.27x27 L K316 6.28x28 K316 6.28x28 K Q317 6.29x29 Q317 6.29x29 Q R318 6.30x30 R318 6.30x30 R R319 6.31x31 R319 6.31x31 R E320 6.32x32 E320 6.32x32 E V321 6.33x33 V321 6.33x33 V A322 6.34x34 A322 6.34x34 A K323 6.35x35 K323 6.35x35 K T324 6.36x36 T324 6.36x36 T V325 6.37x37 V325 6.37x37 V F326 6.38x38 F326 6.38x38 F C327 6.39x39 C327 6.39x39 C L328 6.40x40 L328 6.40x40 L V329 6.41x41 V329 6.41x41 V L330 6.42x42 L330 6.42x42 L V331 6.43x43 V331 6.43x43 V F332 6.44x44 F332 6.44x44 F A333 6.45x45 A333 6.45x45 A L334 6.46x46 L334 6.46x46 L C335 6.47x47 C335 6.47x47 C W336 6.48x48 W336 6.48x48 W L337 6.49x49 L337 6.49x49 L P338 6.50x50 P338 6.50x50 P L339 6.51x51 L339 6.51x51 L H340 6.52x52 H340 6.52x52 H L341 6.53x53 L341 6.53x53 L S342 6.54x54 S342 6.54x54 S R343 6.55x55 R343 6.55x55 R I344 6.56x56 I344 6.56x56 I L345 6.57x57 L345 6.57x57 L K346 6.58x58 K346 6.58x58 K L347 6.59x59 L347 6.59x59 L T348 6.60x60 T348 6.60x60 T L349 6.61x61 L349 6.61x61 L Y350 6.62x62 Y350 6.62x62 Y R357 7.24x23 R357 7.24x23 R C358 7.25x24 C358 7.25x24 C E359 7.26x25 E359 7.26x25 E L360 7.27x26 L360 7.27x26 L L361 7.28x27 L361 7.28x27 L S362 7.29x28 S362 7.29x28 S F363 7.30x29 F363 7.30x29 F L364 7.31x30 L364 7.31x30 L L365 7.32x31 L365 7.32x31 L V366 7.33x32 V366 7.33x32 V L367 7.34x33 L367 7.34x33 L D368 7.35x34 D368 7.35x34 D Y369 7.36x35 Y369 7.36x35 Y I370 7.37x36 I370 7.37x36 I G371 7.38x37 G371 7.38x37 G I372 7.39x38 I372 7.39x38 I N373 7.40x39 N373 7.40x39 N M374 7.41x40 M374 7.41x40 M A375 7.42x41 A375 7.42x41 A S376 7.43x42 S376 7.43x42 S L377 7.44x43 L377 7.44x43 L N378 7.45x45 N378 7.45x45 N S379 7.46x46 S379 7.46x46 S C380 7.47x47 C380 7.47x47 C I381 7.48x48 I381 7.48x48 I N382 7.49x49 N382 7.49x49 N P383 7.50x50 P383 7.50x50 P I384 7.51x51 I384 7.51x51 I A385 7.52x52 A385 7.52x52 A L386 7.53x53 L386 7.53x53 L Y387 7.54x54 Y387 7.54x54 Y L388 7.55x55 L388 7.55x55 L V389 7.56x56 V389 7.56x56 V S390 8.47x47 S390 8.47x47 S K391 8.48x48 K391 8.48x48 K R392 8.49x49 R392 8.49x49 R F397 8.54x54 F397 8.54x54 F K398 8.55x55 K398 8.55x55 K S399 8.56x56 S399 8.56x56 S F393 8.50x50 F393 8.50x50 F K394 8.51x51 K394 8.51x51 K N395 8.52x52 N395 8.52x52 N C396 8.53x53 C396 8.53x53 C C400 8.57x57 C400 8.57x57 C L401 8.58x58 L401 8.58x58 L C402 8.59x59 C402 8.59x59 C C403 8.60x60 C403 8.60x60 C

Top 100 conformational changes

Residue pairs with the largest RRCS changes between active and inactive states. GPCRdb numbering in parentheses. Highlighted rows exceed the significance threshold.

Rank Residue 1 Residue 2 Active RRCS Inactive RRCS ΔRRCS Magnitude
1 GLN41 ILE94 (1.25x25) 0.000 19.115 -19.115 HIGH
2 ARG343 (6.55x55) ASP368 (7.35x34) 0.109 9.910 -9.801 HIGH
3 SER399 (8.56x56) GLN406 0.000 9.393 -9.393 HIGH
4 PRO38 GLU165 0.000 8.706 -8.706 HIGH
5 PRO3 TYR102 (1.33x33) 0.000 8.620 -8.620 HIGH
6 TYR293 (5.58x58) PHE326 (6.38x38) 0.760 8.484 -7.724 HIGH
7 ARG201 (3.52x52) ARG208 (34.52x52) 0.000 6.633 -6.633 HIGH
8 TYR430 ASP431 6.314 0.000 +6.314 HIGH
9 ALA43 LEU256 (45.51x51) 0.000 6.104 -6.104 HIGH
10 TYR293 (5.58x58) VAL325 (6.37x37) 6.003 0.000 +6.003 HIGH
11 GLN261 GLN267 (5.32x33) 5.067 10.908 -5.841 HIGH
12 TYR127 (1.58x58) ARG133 (12.51x51) 0.111 5.942 -5.831 HIGH
13 TRP404 PHE408 5.757 0.000 +5.757 HIGH
14 MET300 (5.65x65) ARG318 (6.30x30) 5.691 0.120 +5.572 HIGH
15 ARG199 (3.50x50) TYR293 (5.58x58) 5.441 0.000 +5.441 HIGH
16 LEU39 TYR247 0.000 5.058 -5.058 HIGH
17 CYS8 CYS109 (1.40x40) 0.000 5.026 -5.026 HIGH
18 GLU299 (5.64x64) LYS303 (5.68x68) 0.000 4.881 -4.881 MED
19 SER196 (3.47x47) TYR293 (5.58x58) 4.631 0.000 +4.631 MED
20 LYS175 (3.26x26) ASP241 0.037 4.629 -4.592 MED
21 PRO4 TYR102 (1.33x33) 0.000 4.590 -4.590 MED
22 SER342 (6.54x54) LEU367 (7.34x33) 2.246 6.654 -4.408 MED
23 TRP167 (23.50x50) CYS255 (45.50x50) 2.367 6.761 -4.394 MED
24 ASP166 (23.49x49) ARG253 7.370 3.025 +4.345 MED
25 PHE326 (6.38x38) LEU330 (6.42x42) 0.000 4.294 -4.294 MED
26 THR47 LYS270 (5.35x36) 0.000 4.269 -4.269 MED
27 ASP147 (2.50x50) THR188 (3.39x39) 4.570 0.542 +4.028 MED
28 TRP206 (34.50x50) LYS303 (5.68x68) 0.000 3.782 -3.782 MED
29 LYS398 (8.55x55) GLU409 0.000 3.582 -3.582 MED
30 LEU12 PHE112 (1.43x43) 0.000 3.569 -3.569 MED
31 ASP198 (3.49x49) ARG199 (3.50x50) 0.000 3.531 -3.531 MED
32 GLU27 ARG29 0.000 3.520 -3.520 MED
33 PRO136 (2.39x39) ARG199 (3.50x50) 0.000 3.485 -3.485 MED
34 ILE94 (1.25x25) SER362 (7.29x28) 1.601 5.048 -3.447 MED
35 PHE240 (4.64x65) LEU257 (45.52x52) 5.054 8.458 -3.404 MED
36 ALA43 ILE254 0.000 3.379 -3.379 MED
37 TRP206 (34.50x50) LEU311 0.000 3.362 -3.362 MED
38 ARG199 (3.50x50) VAL321 (6.33x33) 0.000 3.337 -3.337 MED
39 LEU39 GLU165 0.000 3.249 -3.249 MED
40 GLN352 ARG357 (7.24x23) 1.685 4.889 -3.204 MED
41 GLU44 VAL260 3.121 0.000 +3.121 MED
42 ARG124 (1.55x55) LYS128 (1.59x59) 0.000 3.055 -3.055 MED
43 TRP25 LYS97 (1.28x28) 3.048 0.000 +3.048 MED
44 LEU40 GLN41 3.044 0.000 +3.044 MED
45 ILE94 (1.25x25) LEU361 (7.28x27) 0.779 3.818 -3.039 MED
46 PHE332 (6.44x44) TRP336 (6.48x48) 4.334 7.365 -3.031 MED
47 LEU149 (2.52x52) SER184 (3.35x35) 4.266 1.247 +3.019 MED
48 CYS90 ARG357 (7.24x23) 6.543 3.587 +2.956 MED
49 PHE112 (1.43x43) ILE116 3.706 0.793 +2.914 MED
50 TYR350 ARG357 (7.24x23) 0.348 3.219 -2.871 MED
51 TYR269 LYS273 0.133 3.001 -2.868 MED
52 ARG201 (3.52x52) ILE209 2.867 0.000 +2.867 MED
53 SER58 ASN59 2.806 0.000 +2.806 MED
54 ILE94 (1.25x25) CYS358 2.882 5.686 -2.804 MED
55 PHE240 (4.64x65) LEU256 (45.51x51) 6.018 8.815 -2.797 MED
56 GLN91 PRO355 0.838 3.593 -2.755 MED
57 TYR247 LYS248 5.208 7.960 -2.752 MED
58 THR297 PHE326 (6.38x38) 2.723 0.000 +2.723 MED
59 LEU12 PRO156 0.000 2.668 -2.668 MED
60 ASN104 ASN373 4.523 7.172 -2.649 MED
61 ALA202 ILE209 2.639 0.000 +2.639 MED
62 VAL71 PRO72 1.239 3.861 -2.622 MED
63 MET296 ALA322 0.000 2.612 -2.612 MED
64 VAL16 PRO156 0.000 2.605 -2.605 MED
65 GLU44 LYS346 0.000 2.564 -2.564 MED
66 THR324 VAL389 2.511 5.038 -2.527 MED
67 SER436 ASN437 2.516 0.000 +2.516 MED
68 TRP276 PHE280 5.282 7.762 -2.480 MED
69 TRP167 (23.50x50) PHE169 2.592 5.061 -2.469 MED
70 VAL185 TRP336 (6.48x48) 2.906 5.350 -2.444 MED
71 ALA202 ARG318 (6.30x30) 0.000 2.436 -2.436 MED
72 THR294 PHE326 (6.38x38) 2.340 0.000 +2.340 MED
73 GLU44 PRO259 2.336 0.000 +2.336 MED
74 LEU339 ARG343 (6.55x55) 2.734 0.406 +2.328 MED
75 ASP198 (3.49x49) LYS210 0.000 2.315 -2.315 MED
76 LEU339 GLY371 2.192 4.496 -2.304 MED
77 TYR293 (5.58x58) THR297 0.000 2.286 -2.286 MED
78 PRO5 TYR102 (1.33x33) 0.000 2.282 -2.282 MED
79 ILE243 HIS258 1.255 3.538 -2.282 MED
80 LEU252 ILE254 0.189 2.387 -2.198 LOW
81 LEU232 TYR281 0.000 2.197 -2.197 LOW
82 CYS8 LEU388 2.189 0.000 +2.189 LOW
83 PRO5 ARG10 2.343 0.167 +2.175 LOW
84 ILE157 PHE169 0.000 2.171 -2.171 LOW
85 THR289 VAL329 1.317 3.477 -2.161 LOW
86 PHE282 LEU286 0.843 2.991 -2.147 LOW
87 SER342 (6.54x54) ASP368 (7.35x34) 4.369 6.514 -2.144 LOW
88 CYS131 ARG392 4.898 7.022 -2.123 LOW
89 PRO235 TYR269 4.504 6.617 -2.113 LOW
90 ARG124 (1.55x55) CYS400 0.011 2.094 -2.083 LOW
91 TRP54 PRO55 2.431 0.352 +2.080 LOW
92 SER196 (3.47x47) VAL325 (6.37x37) 0.000 2.021 -2.021 LOW
93 VAL203 ARG318 (6.30x30) 0.000 2.000 -2.000 LOW
94 VAL203 MET300 (5.65x65) 2.945 0.957 +1.987 LOW
95 ILE238 MET266 0.000 1.982 -1.982 LOW
96 TYR387 LYS394 6.462 8.410 -1.948 LOW
97 PRO168 PHE169 1.796 3.738 -1.942 LOW
98 PRO48 GLN352 0.000 1.930 -1.930 LOW
99 THR42 TYR247 0.000 1.927 -1.927 LOW
100 PRO136 (2.39x39) LEU195 0.000 1.887 -1.887 LOW

Transmembrane domain analysis

Active-favoring residues form stronger contacts in the active state (positive ΔRRCS). Inactive-favoring residues form stronger contacts in the inactive state (negative ΔRRCS). Only residues with |ΔRRCS| ≥ 2.26 are shown (per-receptor significance threshold = max(mean(|Δ|) + σ, 0.2)).

Per-segment summary
Segment Range Active-favoring residues Count Inactive-favoring residues Count
TM1 94-128 97 (3.0) 1 94 (-19.1), 102 (-8.6), 127 (-5.8), 109 (-5.0), 112 (-3.6), 124 (-3.1), 128 (-3.1) 7
TM2 136-149 147 (4.0), 149 (3.0) 2 136 (-3.5) 1
TM3 175-201 199 (5.4), 196 (4.6), 188 (4.0), 184 (3.0) 4 201 (-6.6), 175 (-4.6), 198 (-3.5) 3
TM4 240-240 - 0 240 (-3.4) 1
TM5 267-303 300 (5.6) 1 293 (-7.7), 267 (-5.8), 299 (-4.9), 303 (-4.9), 270 (-4.3) 5
TM6 318-343 325 (6.0), 318 (5.6) 2 343 (-9.8), 326 (-7.7), 342 (-4.4), 330 (-4.3), 321 (-3.3), 332 (-3.0), 336 (-3.0) 7
TM7 357-368 - 0 368 (-9.8), 367 (-4.4), 362 (-3.4), 357 (-3.2), 361 (-3.0) 5
Intracellular / Extracellular loops & H8
ICL1 133-133 - 0 133 (-5.8) 1
ICL2 206-208 - 0 208 (-6.6), 206 (-3.8) 2
ICL3 311-311 - 0 311 (-3.4) 1
ECL1 165-167 166 (4.3) 1 165 (-8.7), 167 (-4.4) 2
ECL2 241-261 253 (4.3), 260 (3.1) 2 256 (-6.1), 261 (-5.8), 247 (-5.1), 241 (-4.6), 255 (-4.4), 257 (-3.4), 254 (-3.4) 7
ECL3 352-352 - 0 352 (-3.2) 1
H8 398-399 - 0 399 (-9.4), 398 (-3.6) 2

Interactive visualizations

ΔRRCS distribution

Active vs inactive comparison

Residue-wise changes

TM domain breakdown

Variants of interest

111 variants mapped to contact positions, sorted by |ΔRRCS| impact.

Position Protein change DNA change Allele freq Het / Hom ΔRRCS AM score Pathogenicity Conservation dbSNP
41 p.Cys41Phe c.122G>T 6.85e-07 1 / 0 19.11 0.277 BENIGN 0.49
94 p.Ile94Met c.282C>G 6.84e-07 1 / 0 19.11 0.084 BENIGN 0.57
94 p.Ile94Ser c.281T>G 6.88e-07 1 / 0 19.11 - nan - rs1235006032
94 p.Ile94Val c.280A>G 6.85e-07 1 / 0 19.11 - nan - rs772055405
41 p.Cys41Ser c.121T>A 1.37e-06 2 / 0 19.11 - nan -
41 p.Cys41Arg c.121T>C 6.85e-07 1 / 0 19.11 - nan - rs1211498023
343 p.Arg343Gly c.1027A>G 6.85e-07 1 / 0 9.80 0.925 PATHOGENIC 0.91
399 p.Ala399Gly c.1196C>G 7.13e-07 1 / 0 9.39 0.238 BENIGN 0.73
406 p.Lys406Arg c.1217A>G 7.06e-07 1 / 0 9.39 0.082 BENIGN 0.46 rs199973193
406 p.Lys406Met c.1217A>T 6.57e-06 1 / 0 9.39 - nan - rs199973193
399 p.Ala399Val c.1196C>T 7.13e-07 1 / 0 9.39 - nan - rs1439193162
406 p.Gln406Leu c.1217A>T 1.37e-06 2 / 0 9.39 - nan -
399 p.Ser399Pro c.1195T>C 6.58e-06 1 / 0 9.39 - nan - rs750260325
399 p.Ser399Thr c.1195T>A 8.91e-06 9 / 2 9.39 - nan - rs750260325
165 p.Glu165Asp c.495G>C 6.85e-07 1 / 0 8.71 0.250 BENIGN 0.44
38 p.Pro38Arg c.113C>G 7.10e-07 1 / 0 8.71 0.086 BENIGN 0.66
38 p.Pro38Leu c.113C>T 2.13e-06 3 / 0 8.71 - nan - rs779495524
102 p.Tyr102Cys c.305A>G 6.84e-07 1 / 0 8.62 0.264 BENIGN 0.96
3 p.Pro3Leu c.8C>T 4.43e-05 64 / 0 8.62 0.084 BENIGN 0.85 rs200047993
3 p.Pro3Gln c.8C>A 6.92e-07 1 / 0 8.62 - nan -
3 p.Lys3Arg c.8A>G 6.88e-07 1 / 0 8.62 - nan - rs1880008161
293 p.Tyr293His c.877T>C 6.85e-07 1 / 0 7.72 0.992 PATHOGENIC 0.92 rs1352720092
208 p.Arg208Lys c.623G>A 1.37e-06 2 / 0 6.63 0.412 AMBIGUOUS 0.86 rs1361744218
201 p.Arg201Gln c.602G>A 1.64e-05 24 / 0 6.63 0.365 AMBIGUOUS 0.85 rs780841273
201 p.Arg201Leu c.602G>T 6.85e-07 1 / 0 6.63 - nan -
431 p.Arg431Ile c.1292G>T 7.04e-07 1 / 0 6.31 0.559 AMBIGUOUS 0.78
430 p.Glu430Lys c.1288G>A 7.03e-07 1 / 0 6.31 0.456 AMBIGUOUS 0.52
431 p.Arg431Gly c.1291A>G 7.04e-07 1 / 0 6.31 - nan - rs200248884
430 p.Tyr430Cys c.1289A>G 6.85e-07 1 / 0 6.31 - nan -
430 p.Tyr430Phe c.1289A>T 6.58e-06 1 / 0 6.31 - nan - rs1878736000
430 p.Tyr430His c.1288T>C 1.31e-05 2 / 0 6.31 - nan - rs568662694
43 p.Ala43Thr c.127G>A 7.09e-07 1 / 0 6.10 0.066 BENIGN 0.45 rs200304077
43 p.Ala43Ser c.127G>T 3.54e-06 5 / 0 6.10 - nan - rs200304077
43 p.Ser43Cys c.128C>G 8.90e-06 13 / 0 6.10 - nan - rs578207213
43 p.Ser43Pro c.127T>C 6.85e-07 1 / 0 6.10 - nan - rs1451648041
325 p.Val325Ile c.973G>A 2.05e-05 28 / 1 6.00 0.530 AMBIGUOUS 0.95 rs201437745
261 p.Gln261Arg c.782A>G 6.85e-07 1 / 0 5.84 0.560 AMBIGUOUS 0.37
267 p.Gln267Glu c.799C>G 6.85e-07 1 / 0 5.84 0.075 BENIGN 0.41
404 p.Lys404Arg c.1211A>G 1.11e-05 16 / 0 5.76 0.764 PATHOGENIC 0.63 rs749769388
408 p.Val408Leu c.1222G>C 7.04e-07 1 / 0 5.76 0.331 BENIGN 0.31
408 p.Phe408Cys c.1223T>G 1.37e-06 2 / 0 5.76 - nan -
408 p.Phe408Leu c.1222T>C 2.05e-06 3 / 0 5.76 - nan - rs1297352198
408 p.Ser408Thr c.1222T>A 7.16e-07 1 / 0 5.76 - nan -
404 p.Lys404Glu c.1210A>G 6.95e-07 1 / 0 5.76 - nan -
300 p.Met300Leu c.898A>T 6.85e-07 1 / 0 5.57 0.637 PATHOGENIC 0.85 rs1878952382
300 p.Met300Val c.898A>G 6.85e-07 1 / 0 5.57 - nan -
199 p.Arg199Ser c.597A>T 6.85e-07 1 / 0 5.44 1.000 PATHOGENIC 0.92
247 p.Tyr247Cys c.740A>G 9.58e-06 14 / 0 5.06 0.430 AMBIGUOUS 0.73 rs200272603
39 p.Glu39Gly c.116A>G 6.85e-07 1 / 0 5.06 0.135 BENIGN 0.67 rs1274241424
109 p.Cys109Ser c.325T>A 6.84e-07 1 / 0 5.03 0.221 BENIGN 0.73
8 p.Cys8Gly c.22T>G 6.57e-06 1 / 0 5.03 0.046 BENIGN 0.74 rs765870134
8 p.Met8Ile c.24G>A 6.86e-07 1 / 0 5.03 - nan - rs765515093
303 p.Lys303Arg c.908A>G 3.43e-06 5 / 0 4.88 0.093 BENIGN 0.56 rs1336420198
241 p.Asp241Ala c.722A>C 5.48e-06 8 / 0 4.59 0.433 AMBIGUOUS 0.64 rs201625400
241 p.Asp241Asn c.721G>A 6.84e-07 1 / 0 4.59 - nan - rs762204581
4 p.Pro4Ala c.10C>G 1.38e-06 2 / 0 4.59 0.054 BENIGN 0.71 rs777992864
4 p.Ser4Arg c.12T>G 6.88e-07 1 / 0 4.59 - nan -
4 p.Ser4Asn c.11G>A 3.44e-06 5 / 0 4.59 - nan -
4 p.Ser4Thr c.11G>C 8.87e-05 129 / 0 4.59 - nan - rs201115708
255 p.Cys255Phe c.764G>T 6.85e-07 1 / 0 4.39 0.988 PATHOGENIC 0.87
167 p.Trp167Ser c.500G>C 1.37e-06 2 / 0 4.39 0.956 PATHOGENIC 0.69
166 p.Asp166Val c.497A>T 6.85e-07 1 / 0 4.35 0.360 AMBIGUOUS 0.60 rs998395399
253 p.Arg253Gln c.758G>A 2.74e-05 40 / 0 4.35 0.085 BENIGN 0.50 rs140514830
330 p.Leu330Pro c.989T>C 6.85e-07 1 / 0 4.29 0.982 PATHOGENIC 0.70
330 p.Leu330Phe c.988C>T 2.05e-06 3 / 0 4.29 - nan -
270 p.Lys270Gln c.808A>C 2.74e-06 4 / 0 4.27 0.183 BENIGN 0.52 rs771549175
47 p.Thr47Lys c.140C>A 7.05e-07 1 / 0 4.27 0.093 BENIGN 0.55 rs1316261633
47 p.Thr47Met c.140C>T 4.23e-06 6 / 0 4.27 - nan -
47 p.Gly47Val c.140G>T 3.42e-06 5 / 0 4.27 - nan - rs1183332009
47 p.Gly47Asp c.140G>A 2.05e-06 3 / 0 4.27 - nan -
147 p.Asp147Tyr c.439G>T 6.84e-07 1 / 0 4.03 0.995 PATHOGENIC 0.96
188 p.Thr188Ile c.563C>T 1.37e-06 2 / 0 4.03 0.995 PATHOGENIC 0.90
188 p.Thr188Ser c.563C>G 6.85e-07 1 / 0 4.03 - nan -
206 p.Trp206Arg c.616T>A 6.58e-06 1 / 0 3.78 0.987 PATHOGENIC 0.92 rs1410186437
409 p.Met409Ile c.1227G>A 7.03e-07 1 / 0 3.58 0.305 BENIGN 0.43 rs941247743
409 p.Met409Ile c.1227G>T 7.03e-07 1 / 0 3.58 - nan -
409 p.Glu409Gly c.1226A>G 1.37e-06 2 / 0 3.58 - nan -
409 p.Glu409Lys c.1225G>A 6.85e-07 1 / 0 3.58 - nan - rs200670733
409 p.Leu409Ser c.1226T>C 7.20e-07 1 / 0 3.58 - nan - rs770101988
112 p.Phe112Leu c.336C>A 6.58e-06 1 / 0 3.57 0.966 PATHOGENIC 0.99 rs1879914204
12 p.Thr12Ile c.35C>T 6.85e-07 1 / 0 3.57 0.091 BENIGN 0.81 rs201841569
12 p.Thr12Asn c.35C>A 3.43e-06 5 / 0 3.57 - nan - rs201841569
198 p.Asp198Ala c.593A>C 1.37e-06 2 / 0 3.53 0.997 PATHOGENIC 0.93
29 p.Val29Ile c.85G>A 1.37e-06 2 / 0 3.52 0.128 BENIGN 0.62 rs773347747
27 p.Glu27Gly c.80A>G 7.06e-07 1 / 0 3.52 0.065 BENIGN 0.67
27 p.Arg27Leu c.80G>T 3.42e-06 5 / 0 3.52 - nan - rs760706605
27 p.Arg27Pro c.80G>C 6.85e-07 1 / 0 3.52 - nan - rs760706605
27 p.Arg27Cys c.79C>T 2.74e-06 4 / 0 3.52 - nan -
27 p.Arg27Ser c.79C>A 6.85e-07 1 / 0 3.52 - nan -
136 p.Pro136Ser c.406C>T 1.37e-06 2 / 0 3.49 0.992 PATHOGENIC 0.98
136 p.Pro136Ala c.406C>G 6.84e-07 1 / 0 3.49 - nan -
362 p.Ser362Arg c.1084A>C 1.32e-05 2 / 0 3.45 0.809 PATHOGENIC 0.72 rs369090616
254 p.Ile254Thr c.761T>C 2.74e-06 4 / 0 3.38 0.294 BENIGN 0.56 rs371057149
254 p.Ile254Asn c.761T>A 2.74e-06 4 / 0 3.38 - nan - rs371057149
254 p.Ile254Leu c.760A>C 1.37e-06 2 / 0 3.38 - nan - rs750477425
352 p.Gln352Arg c.1055A>G 3.42e-06 5 / 0 3.20 0.089 BENIGN 0.49 rs1397373759
260 p.Val260Gly c.779T>G 3.56e-05 52 / 0 3.12 0.134 BENIGN 0.20 rs1220991715
44 p.Glu44Asp c.132G>T 1.41e-06 2 / 0 3.12 0.077 BENIGN 0.63 rs1401360436
260 p.Val260Phe c.778G>T 1.56e-03 2269 / 2 3.12 - nan - rs77132068
260 p.Val260Ile c.778G>A 2.12e-04 307 / 1 3.12 - nan - rs77132068
44 p.Glu44Val c.131A>T 4.25e-06 6 / 0 3.12 - nan - rs755457512
44 p.Pro44Leu c.131C>T 3.42e-05 50 / 0 3.12 - nan - rs201601278
44 p.Pro44Ser c.130C>T 6.57e-06 1 / 0 3.12 - nan - rs1447007979
124 p.Arg124Lys c.371G>A 4.10e-06 6 / 0 3.05 0.204 BENIGN 0.91 rs541269180
97 p.Lys97Glu c.289A>G 1.37e-06 2 / 0 3.05 0.149 BENIGN 0.59 rs1280780830
97 p.Lys97Gln c.289A>C 6.84e-07 1 / 0 3.05 - nan -
40 p.Ala40Glu c.119C>A 1.37e-06 2 / 0 3.04 0.121 BENIGN 0.74 rs749692138
40 p.Ala40Val c.119C>T 6.85e-07 1 / 0 3.04 - nan -
40 p.Ala40Thr c.118G>A 6.85e-07 1 / 0 3.04 - nan -
40 p.Ala40Ser c.118G>T 4.79e-06 7 / 0 3.04 - nan -
40 p.Ala40Pro c.118G>C 6.85e-07 1 / 0 3.04 - nan -

Complete RRCS results

Top 1000 contact pairs by |ΔRRCS|. Significance threshold: |ΔRRCS| ≥ 2.26, computed as max(mean(|Δ|) + σ, 0.2). Highlighted rows indicate significant changes.

Res1 AA1 Res2 AA2 Active RRCS Inactive RRCS ΔRRCS |ΔRRCS|
41 GLN 94 ILE 0.000 19.115 -19.115 19.115
343 ARG 368 ASP 0.109 9.910 -9.801 9.801
399 SER 406 GLN 0.000 9.393 -9.393 9.393
38 PRO 165 GLU 0.000 8.706 -8.706 8.706
3 PRO 102 TYR 0.000 8.620 -8.620 8.620
293 TYR 326 PHE 0.760 8.484 -7.724 7.724
201 ARG 208 ARG 0.000 6.633 -6.633 6.633
430 TYR 431 ASP 6.314 0.000 6.314 6.314
43 ALA 256 LEU 0.000 6.104 -6.104 6.104
293 TYR 325 VAL 6.003 0.000 6.003 6.003
261 GLN 267 GLN 5.067 10.908 -5.841 5.841
127 TYR 133 ARG 0.111 5.942 -5.831 5.831
404 TRP 408 PHE 5.757 0.000 5.757 5.757
300 MET 318 ARG 5.691 0.120 5.572 5.572
199 ARG 293 TYR 5.441 0.000 5.441 5.441
39 LEU 247 TYR 0.000 5.058 -5.058 5.058
8 CYS 109 CYS 0.000 5.026 -5.026 5.026
299 GLU 303 LYS 0.000 4.881 -4.881 4.881
196 SER 293 TYR 4.631 0.000 4.631 4.631
175 LYS 241 ASP 0.037 4.629 -4.592 4.592
4 PRO 102 TYR 0.000 4.590 -4.590 4.590
342 SER 367 LEU 2.246 6.654 -4.408 4.408
167 TRP 255 CYS 2.367 6.761 -4.394 4.394
166 ASP 253 ARG 7.370 3.025 4.345 4.345
326 PHE 330 LEU 0.000 4.294 -4.294 4.294
47 THR 270 LYS 0.000 4.269 -4.269 4.269
147 ASP 188 THR 4.570 0.542 4.028 4.028
206 TRP 303 LYS 0.000 3.782 -3.782 3.782
398 LYS 409 GLU 0.000 3.582 -3.582 3.582
12 LEU 112 PHE 0.000 3.569 -3.569 3.569
198 ASP 199 ARG 0.000 3.531 -3.531 3.531
27 GLU 29 ARG 0.000 3.520 -3.520 3.520
136 PRO 199 ARG 0.000 3.485 -3.485 3.485
94 ILE 362 SER 1.601 5.048 -3.447 3.447
240 PHE 257 LEU 5.054 8.458 -3.404 3.404
43 ALA 254 ILE 0.000 3.379 -3.379 3.379
206 TRP 311 LEU 0.000 3.362 -3.362 3.362
199 ARG 321 VAL 0.000 3.337 -3.337 3.337
39 LEU 165 GLU 0.000 3.249 -3.249 3.249
352 GLN 357 ARG 1.685 4.889 -3.204 3.204
44 GLU 260 VAL 3.121 0.000 3.121 3.121
124 ARG 128 LYS 0.000 3.055 -3.055 3.055
25 TRP 97 LYS 3.048 0.000 3.048 3.048
40 LEU 41 GLN 3.044 0.000 3.044 3.044
94 ILE 361 LEU 0.779 3.818 -3.039 3.039
332 PHE 336 TRP 4.334 7.365 -3.031 3.031
149 LEU 184 SER 4.266 1.247 3.019 3.019
90 CYS 357 ARG 6.543 3.587 2.956 2.956
112 PHE 116 ILE 3.706 0.793 2.914 2.914
350 TYR 357 ARG 0.348 3.219 -2.871 2.871
269 TYR 273 LYS 0.133 3.001 -2.868 2.868
201 ARG 209 ILE 2.867 0.000 2.867 2.867
58 SER 59 ASN 2.806 0.000 2.806 2.806
94 ILE 358 CYS 2.882 5.686 -2.804 2.804
240 PHE 256 LEU 6.018 8.815 -2.797 2.797
91 GLN 355 PRO 0.838 3.593 -2.755 2.755
247 TYR 248 LYS 5.208 7.960 -2.752 2.752
297 THR 326 PHE 2.723 0.000 2.723 2.723
12 LEU 156 PRO 0.000 2.668 -2.668 2.668
104 ASN 373 ASN 4.523 7.172 -2.649 2.649
202 ALA 209 ILE 2.639 0.000 2.639 2.639
71 VAL 72 PRO 1.239 3.861 -2.622 2.622
296 MET 322 ALA 0.000 2.612 -2.612 2.612
16 VAL 156 PRO 0.000 2.605 -2.605 2.605
44 GLU 346 LYS 0.000 2.564 -2.564 2.564
324 THR 389 VAL 2.511 5.038 -2.527 2.527
436 SER 437 ASN 2.516 0.000 2.516 2.516
276 TRP 280 PHE 5.282 7.762 -2.480 2.480
167 TRP 169 PHE 2.592 5.061 -2.469 2.469
185 VAL 336 TRP 2.906 5.350 -2.444 2.444
202 ALA 318 ARG 0.000 2.436 -2.436 2.436
294 THR 326 PHE 2.340 0.000 2.340 2.340
44 GLU 259 PRO 2.336 0.000 2.336 2.336
339 LEU 343 ARG 2.734 0.406 2.328 2.328
198 ASP 210 LYS 0.000 2.315 -2.315 2.315
339 LEU 371 GLY 2.192 4.496 -2.304 2.304
293 TYR 297 THR 0.000 2.286 -2.286 2.286
5 PRO 102 TYR 0.000 2.282 -2.282 2.282
243 ILE 258 HIS 1.255 3.538 -2.282 2.282
252 LEU 254 ILE 0.189 2.387 -2.198 2.198
232 LEU 281 TYR 0.000 2.197 -2.197 2.197
8 CYS 388 LEU 2.189 0.000 2.189 2.189
5 PRO 10 ARG 2.343 0.167 2.175 2.175
157 ILE 169 PHE 0.000 2.171 -2.171 2.171
289 THR 329 VAL 1.317 3.477 -2.161 2.161
282 PHE 286 LEU 0.843 2.991 -2.147 2.147
342 SER 368 ASP 4.369 6.514 -2.144 2.144
131 CYS 392 ARG 4.898 7.022 -2.123 2.123
235 PRO 269 TYR 4.504 6.617 -2.113 2.113
124 ARG 400 CYS 0.011 2.094 -2.083 2.083
54 TRP 55 PRO 2.431 0.352 2.080 2.080
196 SER 325 VAL 0.000 2.021 -2.021 2.021
203 VAL 318 ARG 0.000 2.000 -2.000 2.000
203 VAL 300 MET 2.945 0.957 1.987 1.987
238 ILE 266 MET 0.000 1.982 -1.982 1.982
387 TYR 394 LYS 6.462 8.410 -1.948 1.948
168 PRO 169 PHE 1.796 3.738 -1.942 1.942
48 PRO 352 GLN 0.000 1.930 -1.930 1.930
42 THR 247 TYR 0.000 1.927 -1.927 1.927
136 PRO 195 LEU 0.000 1.887 -1.887 1.887
319 ARG 323 LYS 0.000 1.881 -1.881 1.881
311 LEU 314 HIS 1.859 0.000 1.859 1.859
197 ILE 201 ARG 2.521 0.714 1.808 1.808
434 ARG 435 SER 1.805 0.000 1.805 1.805
177 VAL 181 GLN 1.796 0.000 1.796 1.796
277 LEU 343 ARG 1.778 0.000 1.778 1.778
146 GLY 188 THR 1.730 0.000 1.730 1.730
126 ILE 133 ARG 0.688 2.416 -1.728 1.728
282 PHE 337 LEU 1.552 3.279 -1.727 1.727
328 LEU 382 ASN 0.000 1.726 -1.726 1.726
307 MET 311 LEU 1.737 0.011 1.726 1.726
182 LYS 236 GLU 2.185 3.911 -1.725 1.725
203 VAL 303 LYS 0.000 1.711 -1.711 1.711
12 LEU 331 VAL 1.709 0.000 1.709 1.709
204 ALA 303 LYS 0.000 1.703 -1.703 1.703
196 SER 292 PHE 2.677 0.989 1.688 1.688
433 PHE 434 ARG 1.629 0.000 1.629 1.629
205 SER 209 ILE 1.628 0.000 1.628 1.628
300 MET 319 ARG 0.000 1.624 -1.624 1.624
150 HIS 181 GLN 0.109 1.730 -1.621 1.621
91 GLN 356 ASN 0.244 1.865 -1.620 1.620
111 VAL 380 CYS 1.914 3.534 -1.619 1.619
285 PRO 332 PHE 1.649 0.050 1.599 1.599
239 GLY 261 GLN 2.840 4.426 -1.586 1.586
352 GLN 353 ASN 0.116 1.682 -1.566 1.566
175 LYS 237 ALA 4.517 6.073 -1.556 1.556
377 LEU 381 ILE 0.197 1.748 -1.552 1.552
278 PHE 282 PHE 4.051 2.500 1.551 1.551
266 MET 269 TYR 2.436 0.899 1.537 1.537
331 VAL 381 ILE 1.799 3.332 -1.533 1.533
137 ASN 393 PHE 1.144 2.661 -1.517 1.517
153 ILE 180 ILE 0.872 2.385 -1.513 1.513
168 PRO 253 ARG 3.316 1.805 1.511 1.511
150 HIS 154 ASP 2.314 3.823 -1.509 1.509
132 MET 137 ASN 8.136 6.654 1.482 1.482
350 TYR 361 LEU 1.480 0.000 1.480 1.480
435 SER 436 SER 1.480 0.000 1.480 1.480
182 LYS 277 LEU 0.515 1.985 -1.470 1.470
175 LYS 240 PHE 3.221 4.653 -1.432 1.432
330 LEU 334 LEU 1.427 0.000 1.427 1.427
293 TYR 329 VAL 1.424 0.000 1.424 1.424
112 PHE 151 ILE 2.754 4.177 -1.423 1.423
143 LEU 192 LEU 1.453 0.034 1.419 1.419
181 GLN 182 LYS 1.323 2.742 -1.419 1.419
162 LEU 369 TYR 7.612 9.029 -1.417 1.417
143 LEU 191 SER 2.255 0.863 1.392 1.392
297 THR 322 ALA 1.389 0.000 1.389 1.389
95 GLU 362 SER 0.689 2.053 -1.363 1.363
41 GLN 93 PRO 0.000 1.357 -1.357 1.357
111 VAL 155 ILE 0.000 1.355 -1.355 1.355
100 PHE 104 ASN 1.804 3.141 -1.337 1.337
282 PHE 340 HIS 2.720 4.055 -1.335 1.335
65 SER 66 LEU 0.101 1.435 -1.334 1.334
274 ASP 343 ARG 4.144 2.828 1.316 1.316
112 PHE 155 ILE 1.422 2.734 -1.312 1.312
265 PHE 266 MET 0.000 1.312 -1.312 1.312
439 TYR 440 SER 1.298 0.000 1.298 1.298
307 MET 308 GLN 0.000 1.293 -1.293 1.293
136 PRO 198 ASP 3.500 2.208 1.293 1.293
160 TYR 164 ALA 2.359 3.652 -1.292 1.292
121 THR 401 LEU 0.211 1.503 -1.292 1.292
150 HIS 376 SER 1.468 2.747 -1.279 1.279
440 SER 441 SER 1.272 0.000 1.272 1.272
160 TYR 168 PRO 3.723 4.989 -1.266 1.266
182 LYS 281 TYR 3.546 2.298 1.247 1.247
150 HIS 185 VAL 1.241 0.000 1.241 1.241
13 VAL 160 TYR 0.000 1.220 -1.220 1.220
276 TRP 281 TYR 0.165 1.384 -1.219 1.219
189 VAL 332 PHE 0.548 1.748 -1.201 1.201
167 TRP 174 CYS 4.612 5.812 -1.200 1.200
146 GLY 184 SER 0.685 1.883 -1.197 1.197
275 TRP 344 ILE 1.064 2.258 -1.193 1.193
296 MET 325 VAL 1.191 0.000 1.191 1.191
119 ASN 383 PRO 3.772 4.958 -1.185 1.185
47 THR 259 PRO 0.000 1.182 -1.182 1.182
134 ASN 137 ASN 5.858 7.039 -1.181 1.181
40 LEU 165 GLU 0.000 1.178 -1.178 1.178
243 ILE 245 MET 0.000 1.175 -1.175 1.175
93 PRO 95 GLU 3.100 4.275 -1.175 1.175
402 CYS 405 CYS 0.000 1.170 -1.170 1.170
153 ILE 181 GLN 1.151 0.000 1.151 1.151
161 LYS 167 TRP 0.000 1.151 -1.151 1.151
243 ILE 254 ILE 6.490 5.349 1.141 1.141
39 LEU 41 GLN 0.000 1.134 -1.134 1.134
160 TYR 166 ASP 0.793 1.916 -1.123 1.123
281 TYR 332 PHE 0.678 1.795 -1.116 1.116
336 TRP 375 ALA 2.583 3.692 -1.109 1.109
335 CYS 378 ASN 2.338 3.446 -1.108 1.108
149 LEU 226 TRP 0.000 1.102 -1.102 1.102
45 ILE 361 LEU 0.000 1.100 -1.100 1.100
38 PRO 101 LYS 0.000 1.099 -1.099 1.099
208 ARG 210 LYS 0.000 1.096 -1.096 1.096
199 ARG 325 VAL 0.249 1.315 -1.066 1.066
196 SER 288 ILE 1.063 0.000 1.063 1.063
320 GLU 389 VAL 0.000 1.063 -1.063 1.063
143 LEU 382 ASN 2.998 1.936 1.063 1.063
134 ASN 213 GLY 2.079 1.019 1.060 1.060
132 MET 393 PHE 2.947 4.004 -1.056 1.056
39 LEU 252 LEU 0.000 1.056 -1.056 1.056
336 TRP 378 ASN 3.042 4.094 -1.052 1.052
93 PRO 358 CYS 0.000 1.051 -1.051 1.051
119 ASN 147 ASP 2.095 3.145 -1.050 1.050
120 SER 148 LEU 0.680 1.729 -1.048 1.048
88 PRO 353 ASN 0.424 1.463 -1.039 1.039
134 ASN 136 PRO 2.003 3.041 -1.037 1.037
259 PRO 270 LYS 6.217 5.179 1.037 1.037
236 GLU 240 PHE 3.724 2.691 1.033 1.033
142 SER 222 ILE 0.528 1.550 -1.022 1.022
200 TYR 204 ALA 2.132 1.115 1.017 1.017
96 ILE 365 LEU 0.019 1.033 -1.014 1.014
49 PRO 50 THR 1.014 0.000 1.014 1.014
260 VAL 267 GLN 0.000 1.006 -1.006 1.006
46 MET 259 PRO 0.000 1.006 -1.006 1.006
125 ILE 400 CYS 1.232 0.242 0.990 0.990
291 PHE 292 PHE 0.922 1.908 -0.987 0.987
116 ILE 151 ILE 0.000 0.976 -0.976 0.976
98 GLU 101 LYS 5.548 4.574 0.973 0.973
149 LEU 180 ILE 1.296 0.330 0.966 0.966
204 ALA 299 GLU 0.000 0.966 -0.966 0.966
101 LYS 162 LEU 3.657 4.622 -0.965 0.965
338 PRO 367 LEU 1.595 0.630 0.965 0.965
19 CYS 374 MET 0.964 0.000 0.964 0.964
45 ILE 350 TYR 0.000 0.963 -0.963 0.963
40 LEU 369 TYR 0.000 0.955 -0.955 0.955
284 LEU 288 ILE 0.625 1.574 -0.949 0.949
145 LEU 226 TRP 1.588 0.659 0.928 0.928
167 TRP 253 ARG 6.282 5.358 0.925 0.925
350 TYR 352 GLN 0.000 0.912 -0.912 0.912
200 TYR 295 LEU 3.221 4.111 -0.890 0.890
12 LEU 327 CYS 0.889 0.000 0.889 0.889
232 LEU 276 TRP 1.758 0.871 0.887 0.887
354 ASP 355 PRO 2.710 1.840 0.870 0.870
33 PRO 34 ASP 0.000 0.867 -0.867 0.867
125 ILE 132 MET 0.171 1.036 -0.865 0.865
280 PHE 281 TYR 3.366 2.511 0.855 0.855
351 ASN 357 ARG 0.847 1.697 -0.850 0.850
293 TYR 296 MET 0.845 0.000 0.845 0.845
167 TRP 173 MET 2.015 2.854 -0.839 0.839
88 PRO 357 ARG 4.279 5.114 -0.835 0.835
290 ALA 329 VAL 0.830 0.000 0.830 0.830
190 LEU 225 ILE 2.356 3.184 -0.829 0.829
147 ASP 382 ASN 2.799 3.627 -0.828 0.828
194 ALA 221 GLU 1.849 2.668 -0.818 0.818
100 PHE 369 TYR 0.986 1.803 -0.817 0.817
192 LEU 332 PHE 0.844 1.654 -0.809 0.809
346 LYS 364 LEU 1.724 2.531 -0.807 0.807
183 ALA 229 SER 3.082 3.888 -0.806 0.806
267 GLN 270 LYS 0.000 0.804 -0.804 0.804
139 LEU 218 THR 1.094 0.291 0.802 0.802
185 VAL 281 TYR 2.456 3.242 -0.787 0.787
119 ASN 148 LEU 1.012 1.792 -0.780 0.780
105 THR 163 LEU 1.063 1.840 -0.777 0.777
195 LEU 199 ARG 0.775 0.000 0.775 0.775
96 ILE 369 TYR 0.642 1.415 -0.772 0.772
300 MET 321 VAL 0.769 0.000 0.769 0.769
139 LEU 221 GLU 0.000 0.767 -0.767 0.767
50 THR 51 LYS 0.763 0.000 0.763 0.763
115 GLY 380 CYS 1.933 2.695 -0.762 0.762
179 PHE 237 ALA 2.174 1.413 0.761 0.761
339 LEU 368 ASP 1.213 0.455 0.758 0.758
143 LEU 195 LEU 0.751 0.000 0.751 0.751
257 LEU 266 MET 0.744 0.000 0.744 0.744
178 PRO 236 GLU 1.632 2.374 -0.742 0.742
354 ASP 356 ASN 2.579 1.856 0.723 0.723
31 PHE 32 PRO 2.309 1.590 0.719 0.719
158 ASN 369 TYR 1.725 1.006 0.719 0.719
122 LEU 383 PRO 1.114 0.398 0.716 0.716
155 ILE 376 SER 2.678 1.975 0.704 0.704
323 LYS 389 VAL 0.000 0.703 -0.703 0.703
153 ILE 177 VAL 0.672 1.373 -0.701 0.701
187 ILE 225 ILE 0.626 1.323 -0.697 0.697
87 PRO 352 GLN 1.195 1.891 -0.696 0.696
6 SER 105 THR 0.000 0.695 -0.695 0.695
135 GLY 214 VAL 0.766 0.077 0.690 0.690
279 SER 284 LEU 2.503 3.190 -0.687 0.687
108 SER 155 ILE 1.800 2.486 -0.686 0.686
263 THR 266 MET 1.133 1.819 -0.685 0.685
282 PHE 332 PHE 0.276 0.961 -0.685 0.685
40 LEU 365 LEU 0.000 0.682 -0.682 0.682
205 SER 208 ARG 0.492 1.174 -0.681 0.681
151 ILE 376 SER 0.772 0.091 0.681 0.681
170 GLY 242 ILE 2.409 3.087 -0.678 0.678
154 ASP 376 SER 0.429 1.106 -0.677 0.677
224 LEU 228 VAL 0.671 0.000 0.671 0.671
387 TYR 397 PHE 4.524 3.854 0.670 0.670
125 ILE 397 PHE 4.277 4.945 -0.667 0.667
293 TYR 322 ALA 0.000 0.664 -0.664 0.664
341 LEU 345 LEU 1.264 1.927 -0.663 0.663
324 THR 386 LEU 0.000 0.657 -0.657 0.657
165 GLU 252 LEU 0.000 0.657 -0.657 0.657
155 ILE 373 ASN 0.656 0.000 0.656 0.656
220 VAL 224 LEU 0.000 0.654 -0.654 0.654
331 VAL 378 ASN 1.033 1.685 -0.653 0.653
46 MET 245 MET 0.653 0.000 0.653 0.653
12 LEU 159 VAL 0.000 0.650 -0.650 0.650
133 ARG 213 GLY 0.857 1.505 -0.648 0.648
13 VAL 17 LEU 1.163 0.516 0.647 0.647
151 ILE 155 ILE 0.109 0.754 -0.645 0.645
116 ILE 148 LEU 1.083 1.726 -0.644 0.644
61 SER 62 LEU 0.805 1.446 -0.640 0.640
157 ILE 167 TRP 0.796 1.433 -0.637 0.637
44 GLU 270 LYS 0.631 0.000 0.631 0.631
432 ASN 433 PHE 0.630 0.000 0.630 0.630
200 TYR 296 MET 2.834 2.205 0.629 0.629
297 THR 301 LEU 1.006 0.383 0.623 0.623
167 TRP 242 ILE 1.229 1.851 -0.622 0.622
254 ILE 256 LEU 1.560 0.941 0.619 0.619
133 ARG 138 ILE 0.153 0.769 -0.616 0.616
45 ILE 352 GLN 0.614 0.000 0.614 0.614
188 THR 378 ASN 0.000 0.611 -0.611 0.611
197 ILE 292 PHE 3.991 4.599 -0.609 0.609
116 ILE 152 VAL 0.147 0.753 -0.606 0.606
269 TYR 276 TRP 0.864 0.259 0.604 0.604
115 GLY 151 ILE 1.128 1.731 -0.604 0.604
143 LEU 147 ASP 1.821 1.218 0.603 0.603
268 PHE 272 ALA 0.941 1.541 -0.600 0.600
441 SER 442 SER 0.600 0.000 0.600 0.600
192 LEU 328 LEU 0.000 0.597 -0.597 0.597
142 SER 187 ILE 0.566 1.162 -0.596 0.596
261 GLN 266 MET 7.168 6.576 0.592 0.592
296 MET 318 ARG 0.000 0.591 -0.591 0.591
289 THR 293 TYR 0.591 0.000 0.591 0.591
336 TRP 340 HIS 1.407 0.817 0.590 0.590
286 LEU 333 ALA 0.550 1.139 -0.589 0.589
135 GLY 213 GLY 1.085 0.501 0.584 0.584
133 ARG 214 VAL 0.686 1.268 -0.583 0.583
199 ARG 296 MET 1.976 1.397 0.580 0.580
157 ILE 177 VAL 0.549 1.126 -0.577 0.577
92 GLY 358 CYS 1.119 1.695 -0.576 0.576
90 CYS 355 PRO 1.912 2.489 -0.576 0.576
174 CYS 241 ASP 2.076 2.651 -0.575 0.575
123 LEU 145 LEU 1.304 1.875 -0.571 0.571
246 ASP 251 TYR 0.000 0.568 -0.568 0.568
6 SER 320 GLU 0.567 0.000 0.567 0.567
124 ARG 404 TRP 0.566 0.000 0.566 0.566
17 LEU 21 LEU 0.000 0.559 -0.559 0.559
100 PHE 366 VAL 4.689 4.132 0.557 0.557
277 LEU 282 PHE 0.511 1.067 -0.556 0.556
215 PRO 218 THR 2.826 2.273 0.553 0.553
259 PRO 267 GLN 0.000 0.551 -0.551 0.551
38 PRO 94 ILE 0.000 0.551 -0.551 0.551
150 HIS 184 SER 2.425 2.975 -0.550 0.550
205 SER 207 SER 0.000 0.550 -0.550 0.550
139 LEU 194 ALA 0.590 1.137 -0.547 0.547
191 SER 225 ILE 1.108 1.654 -0.546 0.546
59 ASN 60 ALA 0.009 0.541 -0.532 0.532
261 GLN 270 LYS 0.028 0.557 -0.529 0.529
278 PHE 283 CYS 6.016 6.542 -0.527 0.527
135 GLY 215 PRO 1.260 0.738 0.521 0.521
179 PHE 233 ALA 4.432 4.954 -0.521 0.521
245 MET 252 LEU 6.043 5.526 0.517 0.517
123 LEU 141 ALA 2.124 2.637 -0.513 0.513
192 LEU 289 THR 1.411 0.900 0.512 0.512
6 SER 102 TYR 0.000 0.509 -0.509 0.509
151 ILE 379 SER 1.723 2.228 -0.505 0.505
154 ASP 372 ILE 1.263 0.761 0.502 0.502
98 GLU 102 TYR 0.731 0.230 0.501 0.501
342 SER 343 ARG 0.498 0.000 0.498 0.498
67 ALA 68 PRO 1.630 2.128 -0.498 0.498
64 ARG 65 SER 0.899 0.407 0.492 0.492
166 ASP 252 LEU 0.000 0.492 -0.492 0.492
154 ASP 181 GLN 4.371 4.859 -0.487 0.487
174 CYS 255 CYS 7.297 7.783 -0.486 0.486
378 ASN 382 ASN 0.000 0.485 -0.485 0.485
258 HIS 259 PRO 2.803 3.287 -0.484 0.484
151 ILE 380 CYS 0.694 0.213 0.481 0.481
348 THR 349 LEU 1.227 0.747 0.481 0.481
199 ARG 328 LEU 0.478 0.000 0.478 0.478
245 MET 254 ILE 0.477 0.000 0.477 0.477
404 TRP 407 SER 0.473 0.000 0.473 0.473
44 GLU 256 LEU 0.000 0.472 -0.472 0.472
148 LEU 152 VAL 0.467 0.000 0.467 0.467
214 VAL 219 ALA 0.487 0.022 0.465 0.465
60 ALA 61 SER 0.789 1.253 -0.463 0.463
300 MET 315 LEU 0.000 0.456 -0.456 0.456
96 ILE 100 PHE 1.356 1.806 -0.450 0.450
119 ASN 144 ALA 4.257 3.808 0.449 0.449
275 TRP 278 PHE 0.000 0.447 -0.447 0.447
239 GLY 257 LEU 4.354 3.909 0.446 0.446
139 LEU 198 ASP 0.445 0.000 0.445 0.445
150 HIS 379 SER 1.197 0.753 0.445 0.445
139 LEU 225 ILE 0.012 0.455 -0.443 0.443
12 LEU 155 ILE 0.000 0.438 -0.438 0.438
247 TYR 252 LEU 0.437 0.000 0.437 0.437
173 MET 177 VAL 0.000 0.436 -0.436 0.436
88 PRO 352 GLN 0.000 0.436 -0.436 0.436
123 LEU 148 LEU 0.358 0.792 -0.434 0.434
308 GLN 309 ILE 0.430 0.000 0.430 0.430
138 ILE 214 VAL 0.587 1.016 -0.429 0.429
178 PRO 240 PHE 4.831 4.403 0.428 0.428
186 GLY 281 TYR 2.252 2.677 -0.425 0.425
277 LEU 281 TYR 1.970 1.546 0.424 0.424
296 MET 300 MET 1.227 0.806 0.421 0.421
166 ASP 168 PRO 0.264 0.681 -0.417 0.417
123 LEU 144 ALA 0.885 1.301 -0.417 0.417
192 LEU 382 ASN 0.414 0.000 0.414 0.414
398 LYS 403 CYS 0.000 0.414 -0.414 0.414
182 LYS 233 ALA 0.821 1.234 -0.413 0.413
338 PRO 374 MET 0.000 0.413 -0.413 0.413
63 ALA 64 ARG 0.000 0.412 -0.412 0.412
242 ILE 254 ILE 2.379 2.790 -0.411 0.411
173 MET 176 LEU 0.050 0.460 -0.410 0.410
275 TRP 347 LEU 1.517 1.107 0.410 0.410
320 GLU 323 LYS 4.295 3.886 0.409 0.409
258 HIS 270 LYS 0.707 0.298 0.409 0.409
44 GLU 343 ARG 0.000 0.406 -0.406 0.406
111 VAL 373 ASN 0.488 0.083 0.405 0.405
280 PHE 285 PRO 2.070 2.475 -0.404 0.404
158 ASN 372 ILE 3.212 2.809 0.403 0.403
218 THR 221 GLU 0.000 0.402 -0.402 0.402
119 ASN 379 SER 2.514 2.913 -0.399 0.399
274 ASP 344 ILE 0.060 0.458 -0.397 0.397
142 SER 191 SER 0.828 0.431 0.397 0.397
278 PHE 340 HIS 4.910 4.519 0.391 0.391
34 ASP 35 ARG 0.391 0.000 0.391 0.391
132 MET 396 CYS 0.000 0.387 -0.387 0.387
140 ILE 393 PHE 0.219 0.605 -0.386 0.386
149 LEU 153 ILE 0.385 0.000 0.385 0.385
335 CYS 381 ILE 0.194 0.576 -0.382 0.382
281 TYR 340 HIS 0.381 0.000 0.381 0.381
235 PRO 265 PHE 0.232 0.609 -0.377 0.377
186 GLY 229 SER 3.759 4.135 -0.376 0.376
42 THR 43 ALA 0.371 0.000 0.371 0.371
126 ILE 138 ILE 0.076 0.446 -0.371 0.371
334 LEU 374 MET 0.371 0.000 0.371 0.371
107 VAL 373 ASN 1.033 1.399 -0.367 0.367
175 LYS 238 ILE 0.000 0.366 -0.366 0.366
175 LYS 236 GLU 0.641 0.277 0.365 0.365
301 LEU 319 ARG 0.362 0.000 0.362 0.362
160 TYR 165 GLU 0.299 0.659 -0.360 0.360
122 LEU 140 ILE 0.935 1.292 -0.357 0.357
130 LYS 212 ILE 0.000 0.354 -0.354 0.354
268 PHE 271 THR 0.350 0.000 0.350 0.350
179 PHE 236 GLU 0.642 0.987 -0.346 0.346
108 SER 373 ASN 6.803 6.459 0.344 0.344
299 GLU 302 ARG 6.506 6.163 0.343 0.343
94 ILE 365 LEU 0.653 0.994 -0.341 0.341
243 ILE 252 LEU 0.905 1.246 -0.340 0.340
16 VAL 152 VAL 0.000 0.340 -0.340 0.340
179 PHE 234 VAL 1.118 1.454 -0.336 0.336
126 ILE 141 ALA 1.937 1.601 0.336 0.336
9 GLY 109 CYS 0.000 0.335 -0.335 0.335
140 ILE 386 LEU 0.943 1.278 -0.335 0.335
112 PHE 156 PRO 1.813 1.482 0.332 0.332
196 SER 197 ILE 0.329 0.000 0.329 0.329
172 GLU 175 LYS 0.326 0.000 0.326 0.326
93 PRO 362 SER 0.260 0.583 -0.323 0.323
363 PHE 367 LEU 0.620 0.297 0.323 0.323
394 LYS 395 ASN 0.000 0.323 -0.323 0.323
125 ILE 396 CYS 4.474 4.151 0.323 0.323
335 CYS 377 LEU 0.000 0.321 -0.321 0.321
332 PHE 378 ASN 3.705 3.387 0.318 0.318
126 ILE 393 PHE 0.175 0.492 -0.317 0.317
118 GLY 383 PRO 3.770 4.086 -0.316 0.316
187 ILE 226 TRP 5.948 5.632 0.316 0.316
89 PRO 355 PRO 0.000 0.315 -0.315 0.315
104 ASN 108 SER 1.057 0.742 0.315 0.315
138 ILE 222 ILE 1.663 1.978 -0.314 0.314
152 VAL 153 ILE 0.000 0.314 -0.314 0.314
189 VAL 285 PRO 1.611 1.924 -0.313 0.313
139 LEU 191 SER 0.000 0.313 -0.313 0.313
387 TYR 398 LYS 0.227 0.537 -0.310 0.310
190 LEU 280 PHE 0.309 0.000 0.309 0.309
345 LEU 367 LEU 0.203 0.510 -0.307 0.307
127 TYR 128 LYS 0.000 0.306 -0.306 0.306
87 PRO 357 ARG 0.065 0.370 -0.305 0.305
122 LEU 397 PHE 1.882 2.187 -0.305 0.305
328 LEU 381 ILE 0.297 0.000 0.297 0.297
245 MET 247 TYR 0.296 0.000 0.296 0.296
112 PHE 152 VAL 0.276 0.569 -0.293 0.293
210 LYS 215 PRO 0.000 0.290 -0.290 0.290
157 ILE 161 LYS 0.000 0.289 -0.289 0.289
401 LEU 402 CYS 0.000 0.287 -0.287 0.287
52 THR 54 TRP 0.000 0.282 -0.282 0.282
126 ILE 140 ILE 0.842 0.562 0.280 0.280
174 CYS 242 ILE 1.375 1.100 0.275 0.275
351 ASN 353 ASN 1.662 1.936 -0.274 0.274
424 LYS 428 HIS 0.000 0.273 -0.273 0.273
431 ASP 432 ASN 0.272 0.000 0.272 0.272
327 CYS 389 VAL 0.000 0.272 -0.272 0.272
49 PRO 84 THR 0.268 0.000 0.268 0.268
296 MET 297 THR 0.268 0.000 0.268 0.268
335 CYS 374 MET 7.960 8.227 -0.267 0.267
171 ALA 241 ASP 0.145 0.412 -0.267 0.267
121 THR 400 CYS 0.541 0.807 -0.265 0.265
160 TYR 169 PHE 4.440 4.178 0.261 0.261
3 PRO 316 LYS 0.261 0.000 0.261 0.261
403 CYS 406 GLN 0.261 0.000 0.261 0.261
40 LEU 161 LYS 0.000 0.260 -0.260 0.260
176 LEU 180 ILE 2.092 2.345 -0.254 0.254
130 LYS 133 ARG 0.000 0.252 -0.252 0.252
399 SER 403 CYS 0.251 0.000 0.251 0.251
199 ARG 202 ALA 0.000 0.251 -0.251 0.251
397 PHE 402 CYS 0.000 0.251 -0.251 0.251
258 HIS 260 VAL 1.231 1.481 -0.250 0.250
317 GLN 321 VAL 0.249 0.000 0.249 0.249
201 ARG 206 TRP 0.249 0.000 0.249 0.249
201 ARG 205 SER 0.249 0.000 0.249 0.249
139 LEU 222 ILE 1.382 1.630 -0.248 0.248
354 ASP 357 ARG 0.000 0.247 -0.247 0.247
135 GLY 218 THR 2.596 2.350 0.246 0.246
111 VAL 377 LEU 1.646 1.886 -0.240 0.240
203 VAL 296 MET 1.885 2.124 -0.240 0.240
132 MET 392 ARG 6.140 6.379 -0.239 0.239
273 LYS 277 LEU 1.532 1.293 0.239 0.239
339 LEU 375 ALA 0.103 0.342 -0.239 0.239
207 SER 208 ARG 0.238 0.000 0.238 0.238
129 ASN 132 MET 1.052 1.290 -0.238 0.238
45 ILE 94 ILE 0.000 0.238 -0.238 0.238
174 CYS 240 PHE 2.956 3.192 -0.236 0.236
195 LEU 293 TYR 0.236 0.000 0.236 0.236
140 ILE 195 LEU 1.048 0.813 0.235 0.235
134 ASN 214 VAL 0.234 0.000 0.234 0.234
190 LEU 228 VAL 0.631 0.864 -0.233 0.233
125 ILE 393 PHE 0.333 0.100 0.232 0.232
47 THR 48 PRO 0.412 0.179 0.232 0.232
345 LEU 364 LEU 0.990 0.760 0.230 0.230
41 GLN 358 CYS 0.000 0.230 -0.230 0.230
351 ASN 354 ASP 0.406 0.636 -0.230 0.230
147 ASP 379 SER 11.941 11.713 0.228 0.228
345 LEU 349 LEU 0.614 0.841 -0.226 0.226
236 GLU 273 LYS 5.944 6.169 -0.225 0.225
397 PHE 401 LEU 0.000 0.225 -0.225 0.225
115 GLY 148 LEU 0.091 0.315 -0.225 0.225
169 PHE 173 MET 1.014 1.237 -0.223 0.223
360 LEU 364 LEU 1.597 1.819 -0.222 0.222
233 ALA 281 TYR 0.000 0.220 -0.220 0.220
335 CYS 371 GLY 0.535 0.316 0.219 0.219
387 TYR 388 LEU 1.285 1.066 0.219 0.219
105 THR 162 LEU 0.204 0.422 -0.218 0.218
32 PRO 33 PRO 1.081 0.864 0.218 0.218
174 CYS 256 LEU 0.279 0.495 -0.216 0.216
243 ILE 253 ARG 1.264 1.481 -0.216 0.216
355 PRO 356 ASN 0.287 0.073 0.214 0.214
311 LEU 315 LEU 1.449 1.658 -0.209 0.209
336 TRP 339 LEU 0.323 0.531 -0.208 0.208
158 ASN 161 LYS 0.000 0.206 -0.206 0.206
116 ILE 120 SER 0.501 0.296 0.205 0.205
190 LEU 229 SER 0.882 1.084 -0.202 0.202
19 CYS 377 LEU 0.200 0.000 0.200 0.200
37 THR 38 PRO 1.074 0.877 0.198 0.198
187 ILE 229 SER 4.513 4.316 0.198 0.198
257 LEU 270 LYS 1.616 1.421 0.196 0.196
126 ILE 132 MET 0.697 0.892 -0.195 0.195
189 VAL 281 TYR 1.599 1.793 -0.194 0.194
9 GLY 105 THR 0.000 0.192 -0.192 0.192
191 SER 195 LEU 0.192 0.000 0.192 0.192
2 GLN 36 ALA 0.000 0.192 -0.192 0.192
89 PRO 357 ARG 1.373 1.187 0.185 0.185
161 LYS 255 CYS 0.000 0.185 -0.185 0.185
126 ILE 137 ASN 1.739 1.923 -0.184 0.184
381 ILE 385 ALA 0.035 0.217 -0.182 0.182
200 TYR 292 PHE 4.307 4.489 -0.182 0.182
122 LEU 144 ALA 0.791 0.609 0.182 0.182
122 LEU 386 LEU 1.153 1.335 -0.182 0.182
6 SER 8 CYS 0.124 0.304 -0.179 0.179
222 ILE 226 TRP 0.940 1.119 -0.179 0.179
229 SER 281 TYR 0.000 0.178 -0.178 0.178
232 LEU 280 PHE 2.302 2.480 -0.178 0.178
291 PHE 295 LEU 3.230 3.054 0.176 0.176
394 LYS 398 LYS 0.300 0.465 -0.165 0.165
241 ASP 255 CYS 1.371 1.207 0.165 0.165
363 PHE 364 LEU 0.428 0.264 0.164 0.164
38 PRO 95 GLU 0.000 0.162 -0.162 0.162
122 LEU 393 PHE 1.307 1.466 -0.159 0.159
205 SER 318 ARG 0.000 0.158 -0.158 0.158
292 PHE 295 LEU 0.025 0.182 -0.157 0.157
241 ASP 258 HIS 0.600 0.445 0.156 0.156
327 CYS 385 ALA 0.000 0.155 -0.155 0.155
277 LEU 340 HIS 2.758 2.913 -0.155 0.155
324 THR 328 LEU 0.000 0.155 -0.155 0.155
258 HIS 261 GLN 0.777 0.622 0.155 0.155
119 ASN 122 LEU 0.000 0.154 -0.154 0.154
105 THR 159 VAL 0.435 0.587 -0.152 0.152
196 SER 329 VAL 0.000 0.151 -0.151 0.151
121 THR 397 PHE 2.360 2.210 0.150 0.150
256 LEU 259 PRO 0.362 0.510 -0.148 0.148
338 PRO 371 GLY 0.961 0.813 0.148 0.148
194 ALA 225 ILE 0.665 0.518 0.148 0.148
150 HIS 375 ALA 0.463 0.316 0.147 0.147
107 VAL 111 VAL 0.148 0.295 -0.147 0.147
28 GLU 29 ARG 0.145 0.000 0.145 0.145
100 PHE 370 ILE 1.648 1.503 0.145 0.145
167 TRP 177 VAL 0.393 0.535 -0.142 0.142
103 ILE 107 VAL 0.184 0.045 0.139 0.139
335 CYS 336 TRP 0.124 0.261 -0.137 0.137
200 TYR 201 ARG 0.000 0.136 -0.136 0.136
104 ASN 370 ILE 0.247 0.383 -0.136 0.136
183 ALA 230 VAL 0.402 0.538 -0.136 0.136
240 PHE 273 LYS 1.699 1.565 0.134 0.134
377 LEU 380 CYS 0.080 0.213 -0.132 0.132
349 LEU 360 LEU 1.777 1.645 0.132 0.132
357 ARG 358 CYS 0.167 0.038 0.128 0.128
214 VAL 218 THR 0.422 0.550 -0.127 0.127
386 LEU 393 PHE 2.792 2.666 0.126 0.126
218 THR 222 ILE 0.471 0.345 0.126 0.126
313 ASP 316 LYS 0.000 0.125 -0.125 0.125
243 ILE 256 LEU 1.359 1.483 -0.124 0.124
413 SER 414 LEU 0.123 0.000 0.123 0.123
374 MET 377 LEU 0.179 0.301 -0.123 0.123
122 LEU 126 ILE 0.941 1.063 -0.121 0.121
177 VAL 178 PRO 1.273 1.394 -0.121 0.121
321 VAL 325 VAL 0.120 0.000 0.120 0.120
150 HIS 155 ILE 0.147 0.267 -0.120 0.120
393 PHE 397 PHE 1.027 0.907 0.120 0.120
101 LYS 165 GLU 2.449 2.567 -0.118 0.118
350 TYR 360 LEU 1.005 0.887 0.118 0.118
335 CYS 375 ALA 2.502 2.385 0.117 0.117
278 PHE 344 ILE 0.231 0.348 -0.117 0.117
413 SER 417 LYS 0.116 0.000 0.116 0.116
101 LYS 163 LEU 0.000 0.116 -0.116 0.116
300 MET 322 ALA 0.116 0.000 0.116 0.116
167 TRP 254 ILE 0.000 0.115 -0.115 0.115
183 ALA 233 ALA 1.630 1.745 -0.114 0.114
203 VAL 299 GLU 0.821 0.707 0.114 0.114
280 PHE 284 LEU 1.245 1.359 -0.113 0.113
345 LEU 348 THR 0.113 0.001 0.111 0.111
4 PRO 5 PRO 0.701 0.594 0.107 0.107
180 ILE 184 SER 0.531 0.637 -0.106 0.106
119 ASN 151 ILE 0.387 0.489 -0.103 0.103
301 LEU 318 ARG 0.102 0.000 0.102 0.102
383 PRO 397 PHE 1.677 1.779 -0.102 0.102
131 CYS 132 MET 0.243 0.345 -0.102 0.102
113 VAL 117 ILE 0.779 0.679 0.100 0.100
271 THR 272 ALA 0.100 0.000 0.100 0.100
171 ALA 242 ILE 2.957 3.055 -0.098 0.098
344 ILE 347 LEU 0.000 0.098 -0.098 0.098
136 PRO 137 ASN 0.000 0.098 -0.098 0.098
282 PHE 333 ALA 2.048 2.145 -0.097 0.097
244 THR 253 ARG 0.377 0.474 -0.097 0.097
188 THR 332 PHE 0.000 0.097 -0.097 0.097
361 LEU 365 LEU 0.000 0.097 -0.097 0.097
328 LEU 385 ALA 0.681 0.586 0.095 0.095
154 ASP 158 ASN 4.253 4.158 0.095 0.095
159 VAL 163 LEU 0.677 0.771 -0.095 0.095
257 LEU 273 LYS 0.759 0.665 0.095 0.095
206 TRP 318 ARG 0.000 0.094 -0.094 0.094
86 SER 87 PRO 0.566 0.660 -0.093 0.093
294 THR 298 CYS 0.213 0.305 -0.091 0.091
129 ASN 131 CYS 0.352 0.442 -0.090 0.090
38 PRO 96 ILE 0.000 0.089 -0.089 0.089
97 LYS 100 PHE 0.106 0.018 0.088 0.088
37 THR 165 GLU 0.000 0.088 -0.088 0.088
288 ILE 292 PHE 0.986 1.073 -0.087 0.087
345 LEU 350 TYR 0.509 0.423 0.086 0.086
250 SER 252 LEU 0.085 0.000 0.085 0.085
315 LEU 318 ARG 0.000 0.084 -0.084 0.084
372 ILE 376 SER 0.071 0.154 -0.083 0.083
24 ILE 25 TRP 0.082 0.000 0.082 0.082
221 GLU 225 ILE 0.416 0.336 0.081 0.081
108 SER 159 VAL 1.395 1.476 -0.081 0.081
234 VAL 238 ILE 0.885 0.965 -0.080 0.080
242 ILE 253 ARG 0.618 0.698 -0.080 0.080
286 LEU 332 PHE 0.934 1.014 -0.080 0.080
109 CYS 113 VAL 0.078 0.000 0.078 0.078
117 ILE 401 LEU 0.078 0.000 0.078 0.078
319 ARG 320 GLU 0.000 0.077 -0.077 0.077
114 LEU 380 CYS 0.212 0.135 0.077 0.077
388 LEU 389 VAL 0.108 0.031 0.077 0.077
193 CYS 289 THR 0.933 0.857 0.076 0.076
146 GLY 187 ILE 0.438 0.362 0.075 0.075
282 PHE 283 CYS 0.362 0.437 -0.075 0.075
225 ILE 229 SER 0.230 0.305 -0.075 0.075
15 LEU 377 LEU 0.075 0.000 0.075 0.075
96 ILE 101 LYS 2.784 2.710 0.074 0.074
279 SER 285 PRO 0.000 0.073 -0.073 0.073
337 LEU 338 PRO 0.974 1.047 -0.073 0.073
262 LYS 263 THR 0.042 0.115 -0.073 0.073
342 SER 364 LEU 2.670 2.597 0.073 0.073
325 VAL 329 VAL 0.000 0.072 -0.072 0.072
16 VAL 21 LEU 0.000 0.071 -0.071 0.071
23 ARG 24 ILE 0.000 0.071 -0.071 0.071
236 GLU 277 LEU 0.000 0.071 -0.071 0.071
104 ASN 162 LEU 2.074 2.003 0.070 0.070
274 ASP 347 LEU 2.425 2.355 0.070 0.070
128 LYS 129 ASN 0.000 0.069 -0.069 0.069
273 LYS 274 ASP 0.200 0.269 -0.069 0.069
243 ILE 259 PRO 1.206 1.137 0.068 0.068
412 GLN 415 GLU 0.000 0.068 -0.068 0.068
286 LEU 329 VAL 0.880 0.948 -0.068 0.068
142 SER 226 TRP 2.878 2.945 -0.067 0.067
137 ASN 140 ILE 0.529 0.463 0.066 0.066
90 CYS 358 CYS 5.255 5.190 0.065 0.065
195 LEU 325 VAL 0.000 0.065 -0.065 0.065
185 VAL 189 VAL 0.245 0.310 -0.064 0.064
344 ILE 348 THR 0.311 0.374 -0.064 0.064
265 PHE 269 TYR 0.000 0.064 -0.064 0.064
278 PHE 279 SER 0.064 0.000 0.064 0.064
189 VAL 190 LEU 0.184 0.247 -0.063 0.063
241 ASP 254 ILE 1.021 0.959 0.062 0.062
234 VAL 235 PRO 0.973 1.035 -0.062 0.062
118 GLY 397 PHE 0.449 0.510 -0.061 0.061
241 ASP 256 LEU 5.206 5.266 -0.060 0.060
182 LYS 229 SER 0.000 0.058 -0.058 0.058
173 MET 178 PRO 0.340 0.282 0.058 0.058
416 GLU 419 SER 0.139 0.082 0.057 0.057
382 ASN 383 PRO 0.962 1.017 -0.055 0.055
3 PRO 4 PRO 0.583 0.638 -0.055 0.055
282 PHE 336 TRP 1.198 1.253 -0.055 0.055
351 ASN 352 GLN 0.000 0.054 -0.054 0.054
146 GLY 226 TRP 0.000 0.054 -0.054 0.054
237 ALA 238 ILE 0.054 0.000 0.054 0.054
111 VAL 376 SER 2.270 2.216 0.054 0.054
223 VAL 227 VAL 0.302 0.250 0.052 0.052
116 ILE 121 THR 0.077 0.025 0.052 0.052
227 VAL 231 VAL 0.255 0.203 0.051 0.051
285 PRO 290 ALA 0.051 0.000 0.051 0.051
327 CYS 331 VAL 0.100 0.151 -0.051 0.051
214 VAL 215 PRO 0.721 0.671 0.050 0.050
324 THR 390 SER 0.000 0.049 -0.049 0.049
115 GLY 120 SER 0.060 0.011 0.049 0.049
139 LEU 195 LEU 1.713 1.762 -0.048 0.048
21 LEU 24 ILE 0.000 0.048 -0.048 0.048
41 GLN 247 TYR 0.000 0.047 -0.047 0.047
235 PRO 266 MET 2.687 2.734 -0.047 0.047
284 LEU 285 PRO 1.339 1.292 0.047 0.047
121 THR 125 ILE 0.598 0.644 -0.046 0.046
386 LEU 397 PHE 0.063 0.018 0.045 0.045
345 LEU 363 PHE 0.045 0.000 0.045 0.045
242 ILE 255 CYS 0.044 0.000 0.044 0.044
370 ILE 374 MET 0.314 0.357 -0.043 0.043
240 PHE 258 HIS 0.020 0.061 -0.042 0.042
240 PHE 255 CYS 0.677 0.636 0.041 0.041
200 TYR 299 GLU 0.040 0.000 0.040 0.040
238 ILE 261 GLN 0.000 0.039 -0.039 0.039
9 GLY 163 LEU 0.000 0.039 -0.039 0.039
387 TYR 393 PHE 0.015 0.054 -0.039 0.039
385 ALA 390 SER 0.079 0.118 -0.038 0.038
410 GLU 413 SER 0.043 0.081 -0.038 0.038
12 LEU 381 ILE 0.037 0.000 0.037 0.037
241 ASP 242 ILE 0.086 0.123 -0.037 0.037
188 THR 192 LEU 0.168 0.204 -0.036 0.036
176 LEU 179 PHE 0.380 0.344 0.035 0.035
244 THR 252 LEU 2.308 2.274 0.034 0.034
239 GLY 258 HIS 2.570 2.604 -0.034 0.034
407 SER 408 PHE 0.043 0.010 0.033 0.033
274 ASP 277 LEU 0.141 0.173 -0.032 0.032
360 LEU 363 PHE 0.000 0.032 -0.032 0.032
151 ILE 156 PRO 1.027 1.059 -0.032 0.032
257 LEU 261 GLN 0.883 0.915 -0.032 0.032
239 GLY 266 MET 1.587 1.555 0.031 0.031
87 PRO 88 PRO 0.621 0.590 0.031 0.031
366 VAL 370 ILE 0.580 0.609 -0.029 0.029
339 LEU 372 ILE 0.785 0.757 0.028 0.028
193 CYS 288 ILE 1.910 1.883 0.027 0.027
361 LEU 364 LEU 0.000 0.026 -0.026 0.026
41 GLN 42 THR 0.304 0.278 0.026 0.026
150 HIS 336 TRP 0.171 0.145 0.026 0.026
39 LEU 40 LEU 0.025 0.000 0.025 0.025
81 PRO 82 PRO 0.697 0.672 0.025 0.025
346 LYS 350 TYR 0.075 0.050 0.024 0.024
157 ILE 158 ASN 0.024 0.000 0.024 0.024
106 VAL 110 LEU 0.210 0.234 -0.024 0.024
197 ILE 288 ILE 0.024 0.000 0.024 0.024
236 GLU 269 TYR 4.740 4.761 -0.022 0.022
390 SER 393 PHE 3.141 3.162 -0.021 0.021
88 PRO 89 PRO 0.615 0.636 -0.021 0.021
119 ASN 380 CYS 0.000 0.021 -0.021 0.021
245 MET 250 SER 1.328 1.348 -0.020 0.020
96 ILE 162 LEU 0.733 0.753 -0.020 0.020
187 ILE 191 SER 0.428 0.408 0.020 0.020
129 ASN 396 CYS 0.350 0.369 -0.019 0.019
48 PRO 49 PRO 0.633 0.614 0.019 0.019
179 PHE 230 VAL 1.906 1.923 -0.017 0.017
155 ILE 156 PRO 1.199 1.216 -0.017 0.017
239 GLY 256 LEU 0.380 0.397 -0.017 0.017
276 TRP 277 LEU 0.679 0.663 0.016 0.016
43 ALA 44 GLU 0.016 0.000 0.016 0.016
105 THR 109 CYS 0.000 0.015 -0.015 0.015
179 PHE 180 ILE 0.700 0.715 -0.015 0.015
186 GLY 191 SER 0.035 0.020 0.015 0.015
386 LEU 394 LYS 0.087 0.101 -0.014 0.014
193 CYS 285 PRO 1.749 1.762 -0.013 0.013
167 TRP 168 PRO 0.177 0.164 0.013 0.013
390 SER 392 ARG 0.610 0.597 0.013 0.013
104 ASN 369 TYR 3.495 3.482 0.013 0.013
155 ILE 372 ILE 0.013 0.000 0.013 0.013
43 ALA 245 MET 0.000 0.012 -0.012 0.012
155 ILE 159 VAL 0.380 0.392 -0.012 0.012
80 SER 81 PRO 0.639 0.651 -0.012 0.012
161 LYS 369 TYR 1.944 1.932 0.012 0.012
215 PRO 217 TRP 0.000 0.012 -0.012 0.012
46 MET 270 LYS 0.000 0.011 -0.011 0.011
331 VAL 335 CYS 0.395 0.385 0.010 0.010
263 THR 265 PHE 0.308 0.317 -0.009 0.009
228 VAL 232 LEU 0.947 0.956 -0.008 0.008
225 ILE 226 TRP 0.119 0.127 -0.008 0.008
2 GLN 3 PRO 0.553 0.545 0.008 0.008
257 LEU 269 TYR 0.123 0.129 -0.007 0.007
35 ARG 37 THR 0.000 0.006 -0.006 0.006
286 LEU 291 PHE 0.006 0.000 0.006 0.006
196 SER 289 THR 2.951 2.956 -0.005 0.005
143 LEU 188 THR 3.150 3.155 -0.005 0.005
99 THR 103 ILE 0.394 0.390 0.004 0.004
154 ASP 155 ILE 0.000 0.003 -0.003 0.003
245 MET 251 TYR 1.353 1.351 0.002 0.002
339 LEU 342 SER 0.002 0.000 0.002 0.002
384 ILE 388 LEU 0.700 0.699 0.001 0.001
117 ILE 121 THR 0.307 0.306 0.001 0.001
9 GLY 159 VAL 0.000 0.001 -0.001 0.001
112 PHE 113 VAL 0.098 0.099 -0.001 0.001
125 ILE 129 ASN 0.777 0.777 0.000 0.000

RRCS change distribution

-0.33
Mean ΔRRCS
1.61
Std Dev
-0.09
Median

Magnitude classification

17
High (|Δ| ≥ 5.0)
62
Medium (2.3 ≤ |Δ| < 5.0)
723
Low (|Δ| < 2.3)

Methods

RRCS analysis. Residue-Residue Contact Scores (RRCS) were calculated for each conformational state based on inter-atomic distances. Changes (ΔRRCS) were computed by comparing active and inactive structures predicted by AlphaFold multistate (del Alamo et al., 2022).

Significance threshold. |ΔRRCS| ≥ 2.26, computed as max(mean(|Δ|) + σ, 0.2). The 0.2 floor ensures receptors with very small overall change still surface their largest contacts.

Variant data. Population frequencies from gnomAD v4; pathogenicity predictions from AlphaMissense; conservation from ProtVar / UniProt.

Structural annotation. TM domain boundaries and generic numbering from GPCRdb.

What is RRCS?

Residue-Residue Contact Score (RRCS) measures how strongly two amino acids interact in a protein structure. When a protein changes shape (from inactive to active), these contact strengths change.

ΔRRCS (Delta RRCS) shows the difference in contact strength between states:

  • Positive ΔRRCS. Contact is stronger in the active state.
  • Negative ΔRRCS. Contact is stronger in the inactive state.
  • Large |ΔRRCS|. Significant structural rearrangement.

Residues with large RRCS changes are critical for protein function. Mutations at these positions may disrupt the protein's ability to change shape properly.

Pathogenicity predictions

AlphaMissense predicts whether a mutation harms protein function:

  • Pathogenic (score ≥ 0.564): mutation likely damages function.
  • Ambiguous (0.34–0.563): effect uncertain.
  • Benign (< 0.34): mutation likely tolerated.

Conservation & population data

Conservation score. How well-preserved a position is across species (0 = variable, 1 = conserved). High conservation suggests the position is critical for function.

Allele frequency. How often a variant appears in the population. Rare variants (low frequency) may be more likely to be harmful.

Sources: AlphaFold multistate · RRCS · gnomAD v4 · AlphaMissense · GPCRdb · UniProt / ProtVar