GPCompReports

DRD3

Gene DRD3 Dopamine receptors Aminergic receptors UniProt P35462
742
Total Contact Pairs
70
Significant Changes
14.20
Max Increase
-8.46
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 R58 12.48x48 R58 12.48x48 R A59 12.49x49 A59 12.49x49 A L60 12.50x50 L60 12.50x50 L Q61 12.51x51 Q61 12.51x51 Q ICL1ECL1 G94 G94 G V95 23.49x49 V95 23.49x49 V W96 23.50x50 W96 23.50x50 W N97 23.51x51 N97 23.51x51 N F98 23.52x52 F98 23.52x52 F ECL1ICL2 P135 34.50x50 P135 34.50x50 P V136 34.51x51 V136 34.51x51 V H137 34.52x52 H137 34.52x52 H Y138 34.53x53 Y138 34.53x53 Y Q139 34.54x54 Q139 34.54x54 Q H140 34.55x55 H140 34.55x55 H G141 34.56x56 G141 34.56x56 G T142 34.57x57 T142 34.57x57 T G143 34.58x58 G143 34.58x58 G Q144 Q144 Q S145 S145 S ICL2ECL2 F172 F172 F N173 N173 N T174 T174 T T175 T175 T G176 G176 G D177 D177 D P178 P178 P T179 T179 T V180 V180 V C181 45.50x50 C181 45.50x50 C S182 45.51x51 S182 45.51x51 S I183 45.52x52 I183 45.52x52 I S184 S184 S ECL2ICL3 Q227 Q227 Q N228 N228 N S229 S229 S Q230 Q230 Q C231 C231 C N232 N232 N S233 S233 S V234 V234 V R235 R235 R P236 P236 P G237 G237 G F238 F238 F P239 P239 P Q240 Q240 Q Q241 Q241 Q T242 T242 T L243 L243 L S244 S244 S P245 P245 P D246 D246 D P247 P247 P A248 A248 A H249 H249 H L250 L250 L E251 E251 E L252 L252 L K253 K253 K R254 R254 R Y255 Y255 Y Y256 Y256 Y S257 S257 S I258 I258 I C259 C259 C Q260 Q260 Q D261 D261 D T262 T262 T A263 A263 A L264 L264 L G265 G265 G G266 G266 G P267 P267 P G268 G268 G F269 F269 F Q270 Q270 Q E271 E271 E R272 R272 R G273 G273 G G274 G274 G E275 E275 E L276 L276 L K277 K277 K R278 R278 R E279 E279 E E280 E280 E K281 K281 K T282 T282 T R283 R283 R N284 N284 N S285 S285 S L286 L286 L S287 S287 S P288 P288 P T289 T289 T I290 I290 I A291 A291 A P292 P292 P K293 K293 K L294 L294 L S295 S295 S L296 L296 L E297 E297 E V298 V298 V R299 R299 R K300 K300 K L301 L301 L S302 S302 S N303 N303 N G304 G304 G R305 R305 R L306 L306 L S307 S307 S T308 T308 T S309 S309 S L310 L310 L K311 K311 K L312 L312 L G313 G313 G P314 P314 P L315 L315 L Q316 Q316 Q P317 P317 P ICL3ECL3 Q356 Q356 Q T357 T357 T C358 C358 C H359 H359 H V360 V360 V ECL3N-term M1 M1 M A2 A2 A S3 S3 S L4 L4 L S5 S5 S Q6 Q6 Q L7 L7 L S8 S8 S G9 G9 G H10 H10 H L11 L11 L N12 N12 N Y13 Y13 Y T14 T14 T C15 C15 C G16 G16 G A17 A17 A E18 E18 E N19 N19 N S20 S20 S T21 T21 T G22 G22 G A23 A23 A S24 S24 S Q25 Q25 Q N-termC-term C400 C400 C C-term A26 1.29x29 A26 1.29x29 A R27 1.30x30 R27 1.30x30 R P28 1.31x31 P28 1.31x31 P H29 1.32x32 H29 1.32x32 H A30 1.33x33 A30 1.33x33 A Y31 1.34x34 Y31 1.34x34 Y Y32 1.35x35 Y32 1.35x35 Y A33 1.36x36 A33 1.36x36 A L34 1.37x37 L34 1.37x37 L S35 1.38x38 S35 1.38x38 S Y36 1.39x39 Y36 1.39x39 Y C37 1.40x40 C37 1.40x40 C A38 1.41x41 A38 1.41x41 A L39 1.42x42 L39 1.42x42 L I40 1.43x43 I40 1.43x43 I L41 1.44x44 L41 1.44x44 L A42 1.45x45 A42 1.45x45 A I43 1.46x46 I43 1.46x46 I V44 1.47x47 V44 1.47x47 V F45 1.48x48 F45 1.48x48 F G46 1.49x49 G46 1.49x49 G N47 1.50x50 N47 1.50x50 N G48 1.51x51 G48 1.51x51 G L49 1.52x52 L49 1.52x52 L V50 1.53x53 V50 1.53x53 V C51 1.54x54 C51 1.54x54 C M52 1.55x55 M52 1.55x55 M A53 1.56x56 A53 1.56x56 A V54 1.57x57 V54 1.57x57 V L55 1.58x58 L55 1.58x58 L K56 1.59x59 K56 1.59x59 K E57 1.60x60 E57 1.60x60 E T62 2.37x37 T62 2.37x37 T T63 2.38x38 T63 2.38x38 T T64 2.39x39 T64 2.39x39 T N65 2.40x40 N65 2.40x40 N Y66 2.41x41 Y66 2.41x41 Y L67 2.42x42 L67 2.42x42 L V68 2.43x43 V68 2.43x43 V V69 2.44x44 V69 2.44x44 V S70 2.45x45 S70 2.45x45 S L71 2.46x46 L71 2.46x46 L A72 2.47x47 A72 2.47x47 A V73 2.48x48 V73 2.48x48 V A74 2.49x49 A74 2.49x49 A D75 2.50x50 D75 2.50x50 D L76 2.51x51 L76 2.51x51 L L77 2.52x52 L77 2.52x52 L V78 2.53x53 V78 2.53x53 V A79 2.54x54 A79 2.54x54 A T80 2.55x55 T80 2.55x55 T L81 2.56x551 L81 2.56x551 L V82 2.57x56 V82 2.57x56 V M83 2.58x57 M83 2.58x57 M P84 2.59x58 P84 2.59x58 P W85 2.60x59 W85 2.60x59 W V86 2.61x60 V86 2.61x60 V V87 2.62x61 V87 2.62x61 V Y88 2.63x62 Y88 2.63x62 Y L89 2.64x63 L89 2.64x63 L E90 2.65x64 E90 2.65x64 E V91 2.66x65 V91 2.66x65 V T92 2.67x66 T92 2.67x66 T G93 2.68x67 G93 2.68x67 G S99 3.21x21 S99 3.21x21 S R100 3.22x22 R100 3.22x22 R I101 3.23x23 I101 3.23x23 I C102 3.24x24 C102 3.24x24 C C103 3.25x25 C103 3.25x25 C D104 3.26x26 D104 3.26x26 D V105 3.27x27 V105 3.27x27 V F106 3.28x28 F106 3.28x28 F V107 3.29x29 V107 3.29x29 V T108 3.30x30 T108 3.30x30 T L109 3.31x31 L109 3.31x31 L D110 3.32x32 D110 3.32x32 D V111 3.33x33 V111 3.33x33 V M112 3.34x34 M112 3.34x34 M M113 3.35x35 M113 3.35x35 M C114 3.36x36 C114 3.36x36 C T115 3.37x37 T115 3.37x37 T A116 3.38x38 A116 3.38x38 A S117 3.39x39 S117 3.39x39 S I118 3.40x40 I118 3.40x40 I L119 3.41x41 L119 3.41x41 L N120 3.42x42 N120 3.42x42 N L121 3.43x43 L121 3.43x43 L C122 3.44x44 C122 3.44x44 C A123 3.45x45 A123 3.45x45 A I124 3.46x46 I124 3.46x46 I S125 3.47x47 S125 3.47x47 S I126 3.48x48 I126 3.48x48 I D127 3.49x49 D127 3.49x49 D R128 3.50x50 R128 3.50x50 R Y129 3.51x51 Y129 3.51x51 Y T130 3.52x52 T130 3.52x52 T A131 3.53x53 A131 3.53x53 A V132 3.54x54 V132 3.54x54 V V133 3.55x55 V133 3.55x55 V M134 3.56x56 M134 3.56x56 M S146 4.38x38 S146 4.38x38 S C147 4.39x39 C147 4.39x39 C R148 4.40x40 R148 4.40x40 R R149 4.41x41 R149 4.41x41 R V150 4.42x42 V150 4.42x42 V A151 4.43x43 A151 4.43x43 A L152 4.44x44 L152 4.44x44 L M153 4.45x45 M153 4.45x45 M I154 4.46x46 I154 4.46x46 I T155 4.47x47 T155 4.47x47 T A156 4.48x48 A156 4.48x48 A V157 4.49x49 V157 4.49x49 V W158 4.50x50 W158 4.50x50 W V159 4.51x51 V159 4.51x51 V L160 4.52x52 L160 4.52x52 L A161 4.53x53 A161 4.53x53 A F162 4.54x54 F162 4.54x54 F A163 4.55x55 A163 4.55x55 A V164 4.56x56 V164 4.56x56 V S165 4.57x57 S165 4.57x57 S C166 4.58x59 C166 4.58x59 C P167 4.59x60 P167 4.59x60 P L168 4.60x61 L168 4.60x61 L L169 4.61x62 L169 4.61x62 L F170 4.62x63 F170 4.62x63 F G171 4.63x64 G171 4.63x64 G N185 5.35x36 N185 5.35x36 N P186 5.36x37 P186 5.36x37 P D187 5.37x38 D187 5.37x38 D F188 5.38x39 F188 5.38x39 F V189 5.39x40 V189 5.39x40 V I190 5.40x41 I190 5.40x41 I Y191 5.41x42 Y191 5.41x42 Y S192 5.42x43 S192 5.42x43 S S193 5.43x44 S193 5.43x44 S V194 5.44x45 V194 5.44x45 V V195 5.45x46 V195 5.45x46 V S196 5.46x461 S196 5.46x461 S F197 5.47x47 F197 5.47x47 F Y198 5.48x48 Y198 5.48x48 Y L199 5.49x49 L199 5.49x49 L P200 5.50x50 P200 5.50x50 P F201 5.51x51 F201 5.51x51 F G202 5.52x52 G202 5.52x52 G V203 5.53x53 V203 5.53x53 V T204 5.54x54 T204 5.54x54 T V205 5.55x55 V205 5.55x55 V L206 5.56x56 L206 5.56x56 L V207 5.57x57 V207 5.57x57 V Y208 5.58x58 Y208 5.58x58 Y A209 5.59x59 A209 5.59x59 A R210 5.60x60 R210 5.60x60 R I211 5.61x61 I211 5.61x61 I Y212 5.62x62 Y212 5.62x62 Y V213 5.63x63 V213 5.63x63 V V214 5.64x64 V214 5.64x64 V L215 5.65x65 L215 5.65x65 L K216 5.66x66 K216 5.66x66 K Q217 5.67x67 Q217 5.67x67 Q R218 5.68x68 R218 5.68x68 R R219 5.69x69 R219 5.69x69 R R220 5.70x70 R220 5.70x70 R K221 5.71x71 K221 5.71x71 K R222 5.72x72 R222 5.72x72 R I223 5.73x73 I223 5.73x73 I L224 5.74x74 L224 5.74x74 L T225 5.75x75 T225 5.75x75 T R226 5.76x76 R226 5.76x76 R R318 6.24x24 R318 6.24x24 R G319 6.25x25 G319 6.25x25 G V320 6.26x26 V320 6.26x26 V P321 6.27x27 P321 6.27x27 P L322 6.28x28 L322 6.28x28 L R323 6.29x29 R323 6.29x29 R E324 6.30x30 E324 6.30x30 E K325 6.31x31 K325 6.31x31 K K326 6.32x32 K326 6.32x32 K A327 6.33x33 A327 6.33x33 A T328 6.34x34 T328 6.34x34 T Q329 6.35x35 Q329 6.35x35 Q M330 6.36x36 M330 6.36x36 M V331 6.37x37 V331 6.37x37 V A332 6.38x38 A332 6.38x38 A I333 6.39x39 I333 6.39x39 I V334 6.40x40 V334 6.40x40 V L335 6.41x41 L335 6.41x41 L G336 6.42x42 G336 6.42x42 G A337 6.43x43 A337 6.43x43 A F338 6.44x44 F338 6.44x44 F I339 6.45x45 I339 6.45x45 I V340 6.46x46 V340 6.46x46 V C341 6.47x47 C341 6.47x47 C W342 6.48x48 W342 6.48x48 W L343 6.49x49 L343 6.49x49 L P344 6.50x50 P344 6.50x50 P F345 6.51x51 F345 6.51x51 F F346 6.52x52 F346 6.52x52 F L347 6.53x53 L347 6.53x53 L T348 6.54x54 T348 6.54x54 T H349 6.55x55 H349 6.55x55 H V350 6.56x56 V350 6.56x56 V L351 6.57x57 L351 6.57x57 L N352 6.58x58 N352 6.58x58 N T353 6.59x59 T353 6.59x59 T H354 6.60x60 H354 6.60x60 H C355 6.61x61 C355 6.61x61 C S361 7.31x30 S361 7.31x30 S P362 7.32x31 P362 7.32x31 P E363 7.33x32 E363 7.33x32 E L364 7.34x33 L364 7.34x33 L Y365 7.35x34 Y365 7.35x34 Y S366 7.36x35 S366 7.36x35 S A367 7.37x36 A367 7.37x36 A T368 7.38x37 T368 7.38x37 T T369 7.39x38 T369 7.39x38 T W370 7.40x39 W370 7.40x39 W L371 7.41x40 L371 7.41x40 L G372 7.42x41 G372 7.42x41 G Y373 7.43x42 Y373 7.43x42 Y V374 7.44x43 V374 7.44x43 V N375 7.45x45 N375 7.45x45 N S376 7.46x46 S376 7.46x46 S A377 7.47x47 A377 7.47x47 A L378 7.48x48 L378 7.48x48 L N379 7.49x49 N379 7.49x49 N P380 7.50x50 P380 7.50x50 P V381 7.51x51 V381 7.51x51 V I382 7.52x52 I382 7.52x52 I Y383 7.53x53 Y383 7.53x53 Y T384 7.54x54 T384 7.54x54 T T385 7.55x55 T385 7.55x55 T F386 7.56x56 F386 7.56x56 F N387 8.47x47 N387 8.47x47 N I388 8.48x48 I388 8.48x48 I E389 8.49x49 E389 8.49x49 E F394 8.54x54 F394 8.54x54 F L395 8.55x55 L395 8.55x55 L K396 8.56x56 K396 8.56x56 K F390 8.50x50 F390 8.50x50 F R391 8.51x51 R391 8.51x51 R K392 8.52x52 K392 8.52x52 K A393 8.53x53 A393 8.53x53 A I397 8.57x57 I397 8.57x57 I L398 8.58x58 L398 8.58x58 L S399 8.59x59 S399 8.59x59 S

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 GLN260 ARG323 (6.29x29) 14.196 0.000 +14.196 HIGH
2 THR262 ILE388 (8.48x48) 13.738 0.000 +13.738 HIGH
3 ARG219 (5.69x69) VAL320 (6.26x26) 10.253 0.000 +10.253 HIGH
4 THR384 (7.54x54) PHE390 (8.50x50) 9.595 0.002 +9.592 HIGH
5 GLU297 SER309 0.000 8.462 -8.462 HIGH
6 ARG323 (6.29x29) GLU389 (8.49x49) 0.000 8.282 -8.282 HIGH
7 THR64 (2.39x39) ARG128 (3.50x50) 0.000 8.247 -8.247 HIGH
8 THR262 GLU389 (8.49x49) 8.204 0.000 +8.204 HIGH
9 SER295 LYS311 0.000 7.814 -7.814 HIGH
10 PHE338 (6.44x44) TRP342 (6.48x48) 2.140 9.882 -7.743 HIGH
11 ARG299 SER307 0.000 7.387 -7.387 HIGH
12 THR63 (2.38x38) GLY141 (34.56x56) 7.384 0.000 +7.384 HIGH
13 GLU297 ARG299 0.013 6.591 -6.578 HIGH
14 ILE388 (8.48x48) ARG391 (8.51x51) 6.507 0.444 +6.063 HIGH
15 ARG222 (5.72x72) VAL320 (6.26x26) 0.000 5.812 -5.812 HIGH
16 PHE338 (6.44x44) ASN375 (7.45x45) 0.000 5.798 -5.798 HIGH
17 PHE269 GLN270 0.000 5.420 -5.420 HIGH
18 ARG218 (5.68x68) TYR255 5.214 0.000 +5.214 HIGH
19 ARG222 (5.72x72) GLY319 (6.25x25) 0.000 5.121 -5.121 HIGH
20 GLU297 LYS311 0.000 5.107 -5.107 HIGH
21 ILE118 (3.40x40) TRP342 (6.48x48) 5.010 0.000 +5.010 HIGH
22 ARG222 (5.72x72) LEU252 4.896 0.000 +4.896 MED
23 ASP127 (3.49x49) ARG128 (3.50x50) 0.000 4.895 -4.895 MED
24 ASN375 (7.45x45) ASN379 (7.49x49) 5.026 0.246 +4.781 MED
25 ARG128 (3.50x50) TYR208 (5.58x58) 4.699 0.000 +4.699 MED
26 HIS29 (1.32x32) GLU90 (2.65x64) 6.597 2.030 +4.567 MED
27 MET330 (6.36x36) PHE386 (7.56x56) 5.599 1.062 +4.537 MED
28 LYS293 ARG318 (6.24x24) 0.000 4.490 -4.490 MED
29 TRP342 (6.48x48) ASN375 (7.45x45) 7.253 2.847 +4.405 MED
30 ASP127 (3.49x49) ARG149 (4.41x41) 5.416 1.094 +4.322 MED
31 PHE197 (5.47x47) PHE201 (5.51x51) 4.264 0.000 +4.264 MED
32 VAL320 (6.26x26) LYS325 (6.31x31) 4.631 0.375 +4.256 MED
33 THR64 (2.39x39) TYR138 (34.53x53) 4.530 0.515 +4.015 MED
34 ILE333 (6.39x39) PHE386 (7.56x56) 0.160 4.126 -3.966 MED
35 PHE201 (5.51x51) PHE338 (6.44x44) 3.896 0.000 +3.896 MED
36 THR385 (7.55x55) ARG391 (8.51x51) 3.890 0.000 +3.890 MED
37 LEU121 (3.43x43) TYR383 (7.53x53) 3.868 0.000 +3.868 MED
38 TYR208 (5.58x58) ALA332 (6.38x38) 0.000 3.866 -3.866 MED
39 THR130 (3.52x52) ARG149 (4.41x41) 3.859 0.000 +3.859 MED
40 LEU294 LEU310 0.000 3.795 -3.795 MED
41 LEU49 (1.52x52) PHE394 (8.54x54) 2.641 6.428 -3.787 MED
42 PRO135 (34.50x50) TYR255 3.759 0.000 +3.759 MED
43 MET330 (6.36x36) TYR383 (7.53x53) 0.000 3.715 -3.715 MED
44 TRP342 (6.48x48) GLY372 (7.42x41) 2.852 6.527 -3.675 MED
45 TYR256 GLU324 (6.30x30) 3.656 0.000 +3.656 MED
46 GLY141 (34.56x56) SER146 (4.38x38) 0.000 3.544 -3.544 MED
47 ALA263 ARG323 (6.29x29) 3.502 0.000 +3.502 MED
48 TYR208 (5.58x58) VAL331 (6.37x37) 2.576 6.019 -3.443 MED
49 TYR212 (5.62x62) THR328 (6.34x34) 3.362 0.000 +3.362 MED
50 THR174 ASN185 (5.35x36) 3.728 0.391 +3.337 MED
51 ARG222 (5.72x72) TYR256 3.283 0.000 +3.283 MED
52 ARG219 (5.69x69) GLU324 (6.30x30) 3.208 0.000 +3.208 MED
53 VAL132 (3.54x54) TYR255 3.187 0.000 +3.187 MED
54 VAL68 (2.43x43) TYR383 (7.53x53) 0.337 3.508 -3.171 MED
55 PRO321 (6.27x27) GLU324 (6.30x30) 1.407 4.564 -3.157 MED
56 VAL133 (3.55x55) ARG218 (5.68x68) 0.381 3.403 -3.021 MED
57 ILE118 (3.40x40) PHE338 (6.44x44) 1.145 4.130 -2.985 MED
58 LEU301 ASN303 0.000 2.935 -2.935 MED
59 ARG128 (3.50x50) TYR383 (7.53x53) 2.865 0.000 +2.865 MED
60 ASP261 GLU389 (8.49x49) 2.840 0.000 +2.840 MED
61 PRO186 HIS354 7.100 4.310 +2.790 MED
62 TYR32 ALA367 2.826 0.038 +2.788 MED
63 THR384 (7.54x54) ARG391 (8.51x51) 0.055 2.750 -2.696 MED
64 CYS114 TRP342 (6.48x48) 1.935 4.602 -2.667 MED
65 GLU389 (8.49x49) LYS392 2.647 0.000 +2.647 MED
66 VAL381 PHE386 (7.56x56) 2.617 0.000 +2.617 MED
67 ARG128 (3.50x50) TYR138 (34.53x53) 0.000 2.604 -2.604 MED
68 THR63 (2.38x38) TYR138 (34.53x53) 0.000 2.590 -2.590 MED
69 SER295 LEU310 0.000 2.588 -2.588 MED
70 GLU57 LYS396 4.368 1.789 +2.579 MED
71 GLU275 LEU276 2.500 0.000 +2.500 LOW
72 ARG222 (5.72x72) GLU324 (6.30x30) 2.498 0.000 +2.498 LOW
73 TYR138 (34.53x53) ARG149 (4.41x41) 1.509 3.990 -2.481 LOW
74 CYS341 LEU371 5.081 7.472 -2.390 LOW
75 LEU296 THR308 0.000 2.386 -2.386 LOW
76 PHE345 PHE346 2.981 0.620 +2.361 LOW
77 TYR256 GLN260 2.344 0.000 +2.344 LOW
78 ALA123 MET153 0.344 2.653 -2.309 LOW
79 ILE124 TYR383 (7.53x53) 2.288 0.000 +2.288 LOW
80 SER257 ASP261 2.650 0.372 +2.278 LOW
81 THR204 PHE338 (6.44x44) 2.252 0.000 +2.252 LOW
82 PRO186 THR353 2.245 0.000 +2.245 LOW
83 ASN47 ALA72 6.682 4.465 +2.217 LOW
84 TRP85 PHE98 0.000 2.214 -2.214 LOW
85 THR385 (7.55x55) PHE386 (7.56x56) 1.155 3.368 -2.213 LOW
86 VAL320 (6.26x26) GLU324 (6.30x30) 0.718 2.910 -2.192 LOW
87 TYR208 (5.58x58) VAL334 2.181 0.000 +2.181 LOW
88 ASN387 PHE390 (8.50x50) 1.939 4.116 -2.176 LOW
89 VAL298 SER307 0.000 2.146 -2.146 LOW
90 GLU297 THR308 0.000 2.141 -2.141 LOW
91 ASP75 ASN379 (7.49x49) 5.140 3.010 +2.130 LOW
92 ALA74 SER117 3.147 1.019 +2.128 LOW
93 PHE197 (5.47x47) TRP342 (6.48x48) 3.957 1.845 +2.111 LOW
94 THR63 (2.38x38) CYS147 2.102 0.000 +2.102 LOW
95 TYR198 PHE346 3.977 1.883 +2.094 LOW
96 THR353 HIS354 1.822 3.903 -2.082 LOW
97 GLN144 ARG148 2.079 0.000 +2.079 LOW
98 LEU11 ASN12 2.053 0.000 +2.053 LOW
99 VAL50 THR384 (7.54x54) 2.052 0.000 +2.052 LOW
100 ARG149 (4.41x41) MET153 2.263 0.245 +2.017 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| ≥ 2.54 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 29-49 29 (4.6) 1 49 (-3.8) 1
TM2 63-90 63 (7.4), 90 (4.6) 2 64 (-8.2), 68 (-3.2) 2
TM3 118-133 118 (5.0), 121 (3.9), 130 (3.9), 132 (3.2) 4 128 (-8.2), 127 (-4.9), 133 (-3.0) 3
TM4 146-149 149 (4.3) 1 146 (-3.5) 1
TM5 185-222 219 (10.3), 218 (5.2), 208 (4.7), 197 (4.3), 201 (4.3), 212 (3.4), 185 (3.3) 7 222 (-5.8) 1
TM6 318-342 323 (14.2), 320 (10.3), 330 (4.5), 325 (4.3), 324 (3.7), 328 (3.4) 6 338 (-7.7), 342 (-7.7), 319 (-5.1), 318 (-4.5), 333 (-4.0), 332 (-3.9), 331 (-3.4), 321 (-3.2) 8
TM7 372-386 384 (9.6), 379 (4.8), 386 (4.5), 385 (3.9), 383 (3.9) 5 375 (-5.8), 372 (-3.7) 2
Intracellular / Extracellular loops & H8
ICL1 - - 0 - 0
ICL2 135-141 141 (7.4), 138 (4.0), 135 (3.8) 3 - 0
ICL3 252-311 260 (14.2), 262 (13.7), 255 (5.2), 252 (4.9), 256 (3.7), 263 (3.5) 6 297 (-8.5), 309 (-8.5), 295 (-7.8), 311 (-7.8), 299 (-7.4), 307 (-7.4), 269 (-5.4), 270 (-5.4), 293 (-4.5), 294 (-3.8), 310 (-3.8) 11
ECL1 - - 0 - 0
ECL2 174-174 174 (3.3) 1 - 0
ECL3 - - 0 - 0
H8 388-394 388 (13.7), 390 (9.6), 391 (6.1) 3 389 (-8.3), 394 (-3.8) 2

Interactive visualizations

ΔRRCS distribution

Active vs inactive comparison

Residue-wise changes

TM domain breakdown

Variants of interest

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

Position Protein change DNA change Allele freq Het / Hom ΔRRCS AM score Pathogenicity Conservation dbSNP
323 p.Arg323Gln c.968G>A 1.16e-05 15 / 1 14.20 0.277 BENIGN 0.82 rs370774588
323 p.Arg323Pro c.968G>C 6.84e-07 1 / 0 14.20 - nan - rs370774588
323 p.Arg323Trp c.967C>T 1.03e-05 15 / 0 14.20 - nan - rs1258445480
388 p.Ile388Thr c.1163T>C 1.37e-06 2 / 0 13.74 0.069 BENIGN 0.65 rs371591312
262 p.Thr262Ala c.784A>G 1.37e-06 2 / 0 13.74 0.061 BENIGN 0.47 rs147915170
388 p.Ile388Asn c.1163T>A 1.37e-06 2 / 0 13.74 - nan - rs371591312
388 p.Ile388Phe c.1162A>T 6.85e-07 1 / 0 13.74 - nan -
219 p.Arg219Ser c.657A>T 6.84e-07 1 / 0 10.25 0.471 AMBIGUOUS 0.71
219 p.Arg219Lys c.656G>A 1.37e-06 0 / 1 10.25 - nan -
390 p.Phe390Leu c.1170C>G 2.06e-06 3 / 0 9.59 0.999 PATHOGENIC 1.00 rs2077399377
384 p.Thr384Asn c.1151C>A 6.84e-07 1 / 0 9.59 0.975 PATHOGENIC 1.00 rs886057788
384 p.Thr384Ala c.1150A>G 2.05e-06 3 / 0 9.59 - nan - rs1196216612
297 p.Glu297Lys c.889G>A 6.84e-07 1 / 0 8.46 0.435 AMBIGUOUS 0.69
309 p.Ser309Phe c.926C>T 6.84e-07 1 / 0 8.46 0.278 BENIGN 0.64
389 p.Glu389Lys c.1165G>A 2.74e-06 4 / 0 8.28 0.913 PATHOGENIC 0.94 rs1235033455
389 p.Glu389Gln c.1165G>C 6.86e-07 1 / 0 8.28 - nan - rs1235033455
311 p.Lys311Met c.932A>T 1.37e-06 2 / 0 7.81 0.328 BENIGN 0.55 rs1472202736
295 p.Ser295Gly c.883A>G 6.84e-07 1 / 0 7.81 0.085 BENIGN 0.48 rs2077427506
311 p.Lys311Arg c.932A>G 6.84e-07 1 / 0 7.81 - nan - rs1472202736
307 p.Ser307Leu c.920C>T 9.58e-06 14 / 0 7.39 0.116 BENIGN 0.40 rs2077427003
299 p.Arg299Gln c.896G>A 1.09e-05 16 / 0 7.39 0.082 BENIGN 0.62 rs200082316
307 p.Ser307Ala c.919T>G 4.10e-06 6 / 0 7.39 - nan - rs958347845
299 p.Arg299Gly c.895C>G 1.37e-06 2 / 0 7.39 - nan -
141 p.Gly141Asp c.422G>A 6.84e-07 1 / 0 7.38 0.211 BENIGN 0.42 rs1322253778
63 p.Thr63Ala c.187A>G 6.84e-07 1 / 0 7.38 0.132 BENIGN 0.88 rs1437485782
391 p.Arg391Leu c.1172G>T 6.87e-07 1 / 0 6.06 0.990 PATHOGENIC 0.99
391 p.Arg391Gln c.1172G>A 2.06e-05 30 / 0 6.06 - nan - rs746592271
391 p.Arg391Trp c.1171C>T 4.81e-06 7 / 0 6.06 - nan - rs200007633
222 p.Arg222Thr c.665G>C 6.84e-07 1 / 0 5.81 0.367 AMBIGUOUS 0.79
375 p.Asn375Asp c.1123A>G 6.84e-07 1 / 0 5.80 0.993 PATHOGENIC 1.00 rs148428613
270 p.Gln270Arg c.809A>G 6.84e-07 1 / 0 5.42 0.065 BENIGN 0.47 rs1559979434
218 p.Arg218Met c.653G>T 6.84e-07 1 / 0 5.21 0.856 PATHOGENIC 0.76
319 p.Gly319Val c.956G>T 6.84e-07 1 / 0 5.12 0.095 BENIGN 0.41
118 p.Ile118Thr c.353T>C 6.84e-07 1 / 0 5.01 0.991 PATHOGENIC 0.96
118 p.Ile118Asn c.353T>A 2.05e-06 3 / 0 5.01 - nan - rs1396583854
252 p.Leu252Met c.754C>A 6.84e-07 1 / 0 4.90 0.096 BENIGN 0.52
252 p.Leu252Val c.754C>G 6.84e-07 1 / 0 4.90 - nan - rs1181229994
379 p.Asn379Lys c.1137C>A 6.84e-07 1 / 0 4.78 0.999 PATHOGENIC 1.00
379 p.Asn379Ser c.1136A>G 1.37e-06 2 / 0 4.78 - nan -
90 p.Glu90Gly c.269A>G 6.92e-07 1 / 0 4.57 0.915 PATHOGENIC 0.97
29 p.His29Arg c.86A>G 6.86e-07 1 / 0 4.57 0.065 BENIGN 0.70
29 p.His29Leu c.86A>T 5.49e-06 8 / 0 4.57 - nan - rs761362051
29 p.His29Asp c.85C>G 6.86e-07 1 / 0 4.57 - nan -
29 p.His29Tyr c.85C>T 1.37e-06 2 / 0 4.57 - nan -
330 p.Met330Ile c.990G>A 1.37e-06 2 / 0 4.54 0.956 PATHOGENIC 0.90
330 p.Met330Val c.988A>G 1.37e-06 2 / 0 4.54 - nan -
293 p.Lys293Asn c.879G>C 6.84e-07 1 / 0 4.49 0.364 AMBIGUOUS 0.56
318 p.Arg318Gln c.953G>A 1.37e-06 2 / 0 4.49 0.112 BENIGN 0.72 rs201759000
318 p.Arg318Trp c.952C>T 5.47e-06 8 / 0 4.49 - nan - rs1303294486
293 p.Lys293Thr c.878A>C 6.84e-07 1 / 0 4.49 - nan -
149 p.Arg149His c.446G>A 3.49e-05 51 / 0 4.32 0.361 AMBIGUOUS 0.93 rs368221644
149 p.Arg149Cys c.445C>T 1.37e-06 2 / 0 4.32 - nan - rs200010990
149 p.Arg149Ser c.445C>A 6.84e-07 1 / 0 4.32 - nan -
201 p.Phe201Tyr c.602T>A 1.37e-06 2 / 0 4.26 0.835 PATHOGENIC 0.87 rs2077506625
325 p.Lys325Asn c.975G>T 6.84e-07 1 / 0 4.26 0.879 PATHOGENIC 0.82 rs2077425767
138 p.Tyr138Cys c.413A>G 1.37e-06 2 / 0 4.02 0.814 PATHOGENIC 0.99 rs969758632
138 p.Tyr138His c.412T>C 6.57e-06 1 / 0 4.02 - nan - rs2077579778
333 p.Ile333Thr c.998T>C 5.48e-06 8 / 0 3.97 0.543 AMBIGUOUS 0.92
385 p.Thr385Ser c.1154C>G 5.48e-06 8 / 0 3.89 0.255 BENIGN 0.86
385 p.Thr385Ile c.1154C>T 6.57e-06 1 / 0 3.89 - nan - rs2077399711
383 p.Tyr383Cys c.1148A>G 6.84e-07 1 / 0 3.87 0.984 PATHOGENIC 1.00
121 p.Leu121Ile c.361C>A 6.57e-06 1 / 0 3.87 0.739 PATHOGENIC 0.95 rs201447792
383 p.Tyr383Ser c.1148A>C 6.84e-07 1 / 0 3.87 - nan - rs1274871399
332 p.Ala332Asp c.995C>A 6.58e-06 1 / 0 3.87 0.979 PATHOGENIC 0.80 rs2077425498
310 p.Leu310Trp c.929T>G 6.84e-07 1 / 0 3.80 0.395 AMBIGUOUS 0.67 rs1165623250
294 p.Leu294His c.881T>A 6.84e-07 1 / 0 3.80 0.212 BENIGN 0.45
294 p.Leu294Arg c.881T>G 4.79e-06 7 / 0 3.80 - nan -
394 p.Phe394Cys c.1181T>G 6.88e-07 1 / 0 3.79 0.973 PATHOGENIC 1.00
135 p.Pro135His c.404C>A 4.79e-06 7 / 0 3.76 0.976 PATHOGENIC 1.00 rs199862630
372 p.Gly372Asp c.1115G>A 6.16e-06 9 / 0 3.67 0.998 PATHOGENIC 1.00 rs754391076
372 p.Gly372Arg c.1114G>C 6.58e-06 1 / 0 3.67 - nan - rs2077400375
146 p.Ser146Pro c.436T>C 6.58e-06 1 / 0 3.54 0.150 BENIGN 0.89 rs1166704705
146 p.Ser146Ala c.436T>G 6.84e-07 1 / 0 3.54 - nan -
263 p.Ala263Thr c.787G>A 6.84e-07 1 / 0 3.50 0.070 BENIGN 0.47
331 p.Val331Ala c.992T>C 6.84e-07 1 / 0 3.44 0.733 PATHOGENIC 0.85 rs1300210592
331 p.Val331Leu c.991G>T 6.84e-07 1 / 0 3.44 - nan -
212 p.Tyr212His c.634T>C 6.84e-07 1 / 0 3.36 0.414 AMBIGUOUS 0.81
185 p.Asn185Lys c.555C>G 6.84e-07 1 / 0 3.34 0.854 PATHOGENIC 0.82 rs2077507183
132 p.Val132Ala c.395T>C 6.86e-07 1 / 0 3.19 0.907 PATHOGENIC 0.99
132 p.Val132Gly c.395T>G 2.74e-06 4 / 0 3.19 - nan -
68 p.Val68Ala c.203T>C 6.84e-07 1 / 0 3.17 0.952 PATHOGENIC 0.80
68 p.Val68Leu c.202G>C 6.84e-07 1 / 0 3.17 - nan -
68 p.Val68Leu c.202G>T 6.84e-07 1 / 0 3.17 - nan -
68 p.Val68Ile c.202G>A 8.89e-06 13 / 0 3.17 - nan - rs371939561
321 p.Pro321Ser c.961C>T 6.84e-07 1 / 0 3.16 0.121 BENIGN 0.55

Complete RRCS results

Top 1000 contact pairs by |ΔRRCS|. Significance threshold: |ΔRRCS| ≥ 2.54, computed as max(mean(|Δ|) + σ, 0.2). Highlighted rows indicate significant changes.

Res1 AA1 Res2 AA2 Active RRCS Inactive RRCS ΔRRCS |ΔRRCS|
260 GLN 323 ARG 14.196 0.000 14.196 14.196
262 THR 388 ILE 13.738 0.000 13.738 13.738
219 ARG 320 VAL 10.253 0.000 10.253 10.253
384 THR 390 PHE 9.595 0.002 9.592 9.592
297 GLU 309 SER 0.000 8.462 -8.462 8.462
323 ARG 389 GLU 0.000 8.282 -8.282 8.282
64 THR 128 ARG 0.000 8.247 -8.247 8.247
262 THR 389 GLU 8.204 0.000 8.204 8.204
295 SER 311 LYS 0.000 7.814 -7.814 7.814
338 PHE 342 TRP 2.140 9.882 -7.743 7.743
299 ARG 307 SER 0.000 7.387 -7.387 7.387
63 THR 141 GLY 7.384 0.000 7.384 7.384
297 GLU 299 ARG 0.013 6.591 -6.578 6.578
388 ILE 391 ARG 6.507 0.444 6.063 6.063
222 ARG 320 VAL 0.000 5.812 -5.812 5.812
338 PHE 375 ASN 0.000 5.798 -5.798 5.798
269 PHE 270 GLN 0.000 5.420 -5.420 5.420
218 ARG 255 TYR 5.214 0.000 5.214 5.214
222 ARG 319 GLY 0.000 5.121 -5.121 5.121
297 GLU 311 LYS 0.000 5.107 -5.107 5.107
118 ILE 342 TRP 5.010 0.000 5.010 5.010
222 ARG 252 LEU 4.896 0.000 4.896 4.896
127 ASP 128 ARG 0.000 4.895 -4.895 4.895
375 ASN 379 ASN 5.026 0.246 4.781 4.781
128 ARG 208 TYR 4.699 0.000 4.699 4.699
29 HIS 90 GLU 6.597 2.030 4.567 4.567
330 MET 386 PHE 5.599 1.062 4.537 4.537
293 LYS 318 ARG 0.000 4.490 -4.490 4.490
342 TRP 375 ASN 7.253 2.847 4.405 4.405
127 ASP 149 ARG 5.416 1.094 4.322 4.322
197 PHE 201 PHE 4.264 0.000 4.264 4.264
320 VAL 325 LYS 4.631 0.375 4.256 4.256
64 THR 138 TYR 4.530 0.515 4.015 4.015
333 ILE 386 PHE 0.160 4.126 -3.966 3.966
201 PHE 338 PHE 3.896 0.000 3.896 3.896
385 THR 391 ARG 3.890 0.000 3.890 3.890
121 LEU 383 TYR 3.868 0.000 3.868 3.868
208 TYR 332 ALA 0.000 3.866 -3.866 3.866
130 THR 149 ARG 3.859 0.000 3.859 3.859
294 LEU 310 LEU 0.000 3.795 -3.795 3.795
49 LEU 394 PHE 2.641 6.428 -3.787 3.787
135 PRO 255 TYR 3.759 0.000 3.759 3.759
330 MET 383 TYR 0.000 3.715 -3.715 3.715
342 TRP 372 GLY 2.852 6.527 -3.675 3.675
256 TYR 324 GLU 3.656 0.000 3.656 3.656
141 GLY 146 SER 0.000 3.544 -3.544 3.544
263 ALA 323 ARG 3.502 0.000 3.502 3.502
208 TYR 331 VAL 2.576 6.019 -3.443 3.443
212 TYR 328 THR 3.362 0.000 3.362 3.362
174 THR 185 ASN 3.728 0.391 3.337 3.337
222 ARG 256 TYR 3.283 0.000 3.283 3.283
219 ARG 324 GLU 3.208 0.000 3.208 3.208
132 VAL 255 TYR 3.187 0.000 3.187 3.187
68 VAL 383 TYR 0.337 3.508 -3.171 3.171
321 PRO 324 GLU 1.407 4.564 -3.157 3.157
133 VAL 218 ARG 0.381 3.403 -3.021 3.021
118 ILE 338 PHE 1.145 4.130 -2.985 2.985
301 LEU 303 ASN 0.000 2.935 -2.935 2.935
128 ARG 383 TYR 2.865 0.000 2.865 2.865
261 ASP 389 GLU 2.840 0.000 2.840 2.840
186 PRO 354 HIS 7.100 4.310 2.790 2.790
32 TYR 367 ALA 2.826 0.038 2.788 2.788
384 THR 391 ARG 0.055 2.750 -2.696 2.696
114 CYS 342 TRP 1.935 4.602 -2.667 2.667
389 GLU 392 LYS 2.647 0.000 2.647 2.647
381 VAL 386 PHE 2.617 0.000 2.617 2.617
128 ARG 138 TYR 0.000 2.604 -2.604 2.604
63 THR 138 TYR 0.000 2.590 -2.590 2.590
295 SER 310 LEU 0.000 2.588 -2.588 2.588
57 GLU 396 LYS 4.368 1.789 2.579 2.579
275 GLU 276 LEU 2.500 0.000 2.500 2.500
222 ARG 324 GLU 2.498 0.000 2.498 2.498
138 TYR 149 ARG 1.509 3.990 -2.481 2.481
341 CYS 371 LEU 5.081 7.472 -2.390 2.390
296 LEU 308 THR 0.000 2.386 -2.386 2.386
345 PHE 346 PHE 2.981 0.620 2.361 2.361
256 TYR 260 GLN 2.344 0.000 2.344 2.344
123 ALA 153 MET 0.344 2.653 -2.309 2.309
124 ILE 383 TYR 2.288 0.000 2.288 2.288
257 SER 261 ASP 2.650 0.372 2.278 2.278
204 THR 338 PHE 2.252 0.000 2.252 2.252
186 PRO 353 THR 2.245 0.000 2.245 2.245
47 ASN 72 ALA 6.682 4.465 2.217 2.217
85 TRP 98 PHE 0.000 2.214 -2.214 2.214
385 THR 386 PHE 1.155 3.368 -2.213 2.213
320 VAL 324 GLU 0.718 2.910 -2.192 2.192
208 TYR 334 VAL 2.181 0.000 2.181 2.181
387 ASN 390 PHE 1.939 4.116 -2.176 2.176
298 VAL 307 SER 0.000 2.146 -2.146 2.146
297 GLU 308 THR 0.000 2.141 -2.141 2.141
75 ASP 379 ASN 5.140 3.010 2.130 2.130
74 ALA 117 SER 3.147 1.019 2.128 2.128
197 PHE 342 TRP 3.957 1.845 2.111 2.111
63 THR 147 CYS 2.102 0.000 2.102 2.102
198 TYR 346 PHE 3.977 1.883 2.094 2.094
353 THR 354 HIS 1.822 3.903 -2.082 2.082
144 GLN 148 ARG 2.079 0.000 2.079 2.079
11 LEU 12 ASN 2.053 0.000 2.053 2.053
50 VAL 384 THR 2.052 0.000 2.052 2.052
149 ARG 153 MET 2.263 0.245 2.017 2.017
222 ARG 318 ARG 0.000 2.016 -2.016 2.016
62 THR 141 GLY 1.990 0.000 1.990 1.990
32 TYR 370 TRP 1.977 0.000 1.977 1.977
299 ARG 306 LEU 0.000 1.972 -1.972 1.972
135 PRO 218 ARG 0.208 2.178 -1.969 1.969
382 ILE 383 TYR 2.071 0.113 1.958 1.958
111 VAL 165 SER 1.649 3.584 -1.935 1.935
108 THR 165 SER 5.224 3.307 1.916 1.916
361 SER 363 GLU 3.665 1.754 1.911 1.911
390 PHE 394 PHE 2.545 0.645 1.900 1.900
236 PRO 238 PHE 0.000 1.875 -1.875 1.875
296 LEU 310 LEU 0.000 1.872 -1.872 1.872
99 SER 102 CYS 0.000 1.861 -1.861 1.861
125 SER 207 VAL 3.654 1.815 1.839 1.839
300 LYS 305 ARG 0.000 1.830 -1.830 1.830
246 ASP 247 PRO 1.966 0.139 1.827 1.827
71 LEU 120 ASN 5.546 3.744 1.802 1.802
343 LEU 347 LEU 0.000 1.752 -1.752 1.752
75 ASP 117 SER 2.262 0.519 1.743 1.743
188 PHE 192 SER 3.752 2.009 1.742 1.742
71 LEU 379 ASN 3.151 1.410 1.741 1.741
167 PRO 172 PHE 6.866 5.128 1.738 1.738
115 THR 196 SER 5.332 3.598 1.734 1.734
125 SER 204 THR 2.781 1.056 1.725 1.725
226 ARG 288 PRO 0.000 1.714 -1.714 1.714
262 THR 392 LYS 1.693 0.000 1.693 1.693
131 ALA 255 TYR 1.673 0.000 1.673 1.673
286 LEU 287 SER 1.665 0.000 1.665 1.665
64 THR 127 ASP 1.942 3.607 -1.665 1.665
352 ASN 365 TYR 1.662 0.000 1.662 1.662
204 THR 335 LEU 0.737 2.384 -1.647 1.647
124 ILE 128 ARG 1.900 0.286 1.614 1.614
383 TYR 390 PHE 0.000 1.613 -1.613 1.613
190 ILE 354 HIS 6.766 5.168 1.598 1.598
52 MET 56 LYS 0.000 1.595 -1.595 1.595
54 VAL 65 ASN 0.061 1.635 -1.574 1.574
302 SER 303 ASN 1.567 0.000 1.567 1.567
50 VAL 394 PHE 1.674 3.233 -1.559 1.559
100 ARG 178 PRO 9.505 11.059 -1.554 1.554
175 THR 182 SER 3.142 1.587 1.554 1.554
88 TYR 97 ASN 3.316 4.869 -1.553 1.553
88 TYR 98 PHE 4.657 6.202 -1.545 1.545
88 TYR 96 TRP 0.000 1.541 -1.541 1.541
168 LEU 173 ASN 1.665 0.141 1.524 1.524
124 ILE 331 VAL 0.000 1.516 -1.516 1.516
60 LEU 390 PHE 4.587 3.076 1.511 1.511
134 MET 137 HIS 2.000 0.495 1.505 1.505
50 VAL 383 TYR 0.000 1.501 -1.501 1.501
107 VAL 173 ASN 1.496 0.000 1.496 1.496
75 ASP 376 SER 10.977 9.487 1.491 1.491
104 ASP 168 LEU 2.294 0.814 1.480 1.480
67 LEU 127 ASP 2.100 0.643 1.457 1.457
210 ARG 214 VAL 1.445 0.000 1.445 1.445
201 PHE 339 ILE 1.707 3.151 -1.444 1.444
29 HIS 93 GLY 1.441 0.000 1.441 1.441
290 ILE 315 LEU 0.000 1.432 -1.432 1.432
305 ARG 306 LEU 1.425 0.000 1.425 1.425
136 VAL 140 HIS 0.000 1.420 -1.420 1.420
121 LEU 379 ASN 1.420 0.000 1.420 1.420
285 SER 286 LEU 1.415 0.000 1.415 1.415
121 LEU 338 PHE 1.480 2.887 -1.407 1.407
340 VAL 371 LEU 2.285 0.883 1.403 1.403
204 THR 208 TYR 1.390 0.000 1.390 1.390
45 PHE 49 LEU 3.634 2.256 1.378 1.378
289 THR 290 ILE 1.354 0.000 1.354 1.354
47 ASN 380 PRO 5.692 4.340 1.353 1.353
46 GLY 380 PRO 3.157 4.497 -1.341 1.341
100 ARG 175 THR 8.222 6.896 1.326 1.326
70 SER 120 ASN 8.134 6.834 1.300 1.300
110 ASP 114 CYS 1.288 0.000 1.288 1.288
43 ILE 376 SER 4.006 2.722 1.284 1.284
205 VAL 335 LEU 1.243 0.000 1.243 1.243
381 VAL 385 THR 1.460 0.223 1.237 1.237
49 LEU 398 LEU 0.000 1.223 -1.223 1.223
166 CYS 170 PHE 0.224 1.446 -1.221 1.221
330 MET 387 ASN 0.000 1.212 -1.212 1.212
125 SER 208 TYR 4.492 3.285 1.207 1.207
36 TYR 370 TRP 8.510 7.307 1.203 1.203
296 LEU 309 SER 0.000 1.185 -1.185 1.185
282 THR 284 ASN 0.000 1.177 -1.177 1.177
85 TRP 106 PHE 3.871 5.040 -1.169 1.169
119 LEU 160 LEU 2.263 1.096 1.167 1.167
189 VAL 349 HIS 4.042 2.879 1.164 1.164
292 PRO 312 LEU 0.000 1.163 -1.163 1.163
78 VAL 113 MET 2.678 1.524 1.155 1.155
189 VAL 353 THR 3.762 2.615 1.148 1.148
88 TYR 95 VAL 0.393 1.540 -1.147 1.147
118 ILE 346 PHE 1.226 0.084 1.141 1.141
192 SER 196 SER 0.000 1.140 -1.140 1.140
299 ARG 311 LYS 0.000 1.138 -1.138 1.138
380 PRO 385 THR 1.135 0.000 1.135 1.135
45 PHE 398 LEU 0.000 1.129 -1.129 1.129
40 ILE 83 MET 4.704 3.577 1.127 1.127
137 HIS 146 SER 1.126 0.000 1.126 1.126
107 VAL 168 LEU 2.664 1.539 1.125 1.125
339 ILE 344 PRO 1.566 0.443 1.123 1.123
342 TRP 345 PHE 0.691 1.811 -1.120 1.120
164 VAL 192 SER 1.117 0.000 1.117 1.117
193 SER 346 PHE 3.534 2.420 1.115 1.115
35 SER 370 TRP 3.867 2.772 1.095 1.095
112 MET 113 MET 2.363 1.269 1.094 1.094
54 VAL 60 LEU 2.594 1.504 1.090 1.090
256 TYR 323 ARG 1.085 0.000 1.085 1.085
184 SER 353 THR 1.081 0.000 1.081 1.081
63 THR 146 SER 2.862 1.788 1.074 1.074
198 TYR 350 VAL 1.284 0.210 1.074 1.074
138 TYR 258 ILE 1.069 0.000 1.069 1.069
337 ALA 375 ASN 0.113 1.171 -1.057 1.057
301 LEU 307 SER 0.000 1.051 -1.051 1.051
218 ARG 320 VAL 0.000 1.046 -1.046 1.046
349 HIS 365 TYR 4.881 3.838 1.043 1.043
130 THR 138 TYR 0.316 1.358 -1.042 1.042
65 ASN 390 PHE 3.048 2.016 1.031 1.031
348 THR 365 TYR 1.202 0.175 1.027 1.027
347 LEU 351 LEU 1.025 0.000 1.025 1.025
168 LEU 188 PHE 5.584 6.603 -1.020 1.020
341 CYS 375 ASN 3.567 2.552 1.015 1.015
298 VAL 306 LEU 0.000 1.012 -1.012 1.012
132 VAL 215 LEU 0.169 1.179 -1.010 1.010
355 CYS 357 THR 0.000 1.003 -1.003 1.003
303 ASN 305 ARG 0.000 0.985 -0.985 0.985
334 VAL 382 ILE 1.057 2.039 -0.981 0.981
387 ASN 389 GLU 0.995 1.967 -0.972 0.972
310 LEU 312 LEU 0.961 0.000 0.961 0.961
83 MET 373 TYR 0.319 1.275 -0.956 0.956
164 VAL 188 PHE 1.703 0.746 0.956 0.956
32 TYR 36 TYR 1.170 0.218 0.952 0.952
122 CYS 203 VAL 0.952 0.000 0.952 0.952
297 GLU 307 SER 0.000 0.945 -0.945 0.945
128 ARG 211 ILE 1.443 0.503 0.940 0.940
82 VAL 106 PHE 1.899 2.839 -0.940 0.940
326 LYS 386 PHE 0.936 0.000 0.936 0.936
164 VAL 191 TYR 0.000 0.930 -0.930 0.930
71 LEU 117 SER 1.939 2.838 -0.899 0.899
166 CYS 167 PRO 1.623 0.730 0.892 0.892
121 LEU 334 VAL 0.000 0.892 -0.892 0.892
160 LEU 195 VAL 0.890 0.000 0.890 0.890
333 ILE 382 ILE 0.247 1.130 -0.883 0.883
293 LYS 313 GLY 0.000 0.881 -0.881 0.881
36 TYR 86 VAL 2.748 1.868 0.880 0.880
37 CYS 87 VAL 1.385 0.512 0.873 0.873
128 ARG 131 ALA 0.000 0.858 -0.858 0.858
193 SER 349 HIS 0.856 0.000 0.856 0.856
191 TYR 195 VAL 2.115 1.260 0.855 0.855
238 PHE 239 PRO 1.379 0.529 0.850 0.850
185 ASN 188 PHE 0.723 1.571 -0.848 0.848
99 SER 101 ILE 1.517 0.671 0.846 0.846
129 TYR 210 ARG 1.577 0.739 0.838 0.838
195 VAL 200 PRO 2.085 2.921 -0.836 0.836
175 THR 184 SER 0.617 1.451 -0.834 0.834
49 LEU 52 MET 0.833 0.000 0.833 0.833
57 GLU 393 ALA 1.113 0.288 0.826 0.826
63 THR 127 ASP 0.000 0.823 -0.823 0.823
111 VAL 192 SER 0.000 0.821 -0.821 0.821
110 ASP 373 TYR 4.937 4.118 0.820 0.820
345 PHE 365 TYR 0.705 1.516 -0.811 0.811
112 MET 165 SER 4.026 4.835 -0.810 0.810
63 THR 142 THR 0.810 0.000 0.810 0.810
261 ASP 387 ASN 0.807 0.000 0.807 0.807
71 LEU 121 LEU 1.571 0.770 0.800 0.800
150 VAL 153 MET 0.793 0.000 0.793 0.793
57 GLU 59 ALA 0.000 0.790 -0.790 0.790
40 ILE 84 PRO 1.033 0.247 0.786 0.786
294 LEU 311 LYS 0.000 0.785 -0.785 0.785
348 THR 364 LEU 1.289 0.513 0.776 0.776
197 PHE 346 PHE 13.976 13.201 0.775 0.775
39 LEU 83 MET 2.121 1.348 0.773 0.773
104 ASP 173 ASN 2.837 3.609 -0.772 0.772
121 LEU 375 ASN 0.769 0.000 0.769 0.769
113 MET 158 TRP 1.071 1.837 -0.766 0.766
320 VAL 321 PRO 1.232 0.473 0.759 0.759
208 TYR 328 THR 0.000 0.759 -0.759 0.759
334 VAL 379 ASN 0.000 0.755 -0.755 0.755
138 TYR 142 THR 0.000 0.748 -0.748 0.748
5 SER 6 GLN 0.748 0.000 0.748 0.748
71 LEU 75 ASP 1.352 0.610 0.743 0.743
118 ILE 196 SER 3.021 3.763 -0.742 0.742
96 TRP 98 PHE 4.108 3.368 0.740 0.740
67 LEU 124 ILE 2.143 2.883 -0.740 0.740
382 ILE 386 PHE 0.000 0.736 -0.736 0.736
115 THR 164 VAL 0.000 0.731 -0.731 0.731
90 GLU 366 SER 1.513 2.238 -0.725 0.725
67 LEU 150 VAL 1.196 0.472 0.724 0.724
335 LEU 339 ILE 0.000 0.723 -0.723 0.723
129 TYR 133 VAL 4.665 3.950 0.715 0.715
96 TRP 103 CYS 5.549 6.260 -0.711 0.711
211 ILE 328 THR 0.000 0.709 -0.709 0.709
384 THR 394 PHE 3.449 2.740 0.708 0.708
199 LEU 200 PRO 1.408 2.114 -0.706 0.706
388 ILE 392 LYS 0.122 0.821 -0.699 0.699
174 THR 184 SER 0.898 0.200 0.698 0.698
295 SER 313 GLY 0.000 0.697 -0.697 0.697
47 ASN 75 ASP 4.835 4.142 0.693 0.693
140 HIS 142 THR 0.686 0.000 0.686 0.686
243 LEU 244 SER 0.000 0.686 -0.686 0.686
100 ARG 176 GLY 0.694 0.010 0.683 0.683
66 TYR 154 ILE 1.492 0.810 0.682 0.682
74 ALA 113 MET 0.628 1.304 -0.676 0.676
68 VAL 384 THR 0.670 0.000 0.670 0.670
33 ALA 87 VAL 0.915 0.248 0.666 0.666
112 MET 162 PHE 1.641 2.299 -0.658 0.658
295 SER 309 SER 0.000 0.658 -0.658 0.658
201 PHE 205 VAL 1.896 2.552 -0.656 0.656
365 TYR 369 THR 1.864 1.213 0.651 0.651
96 TRP 106 PHE 0.833 0.183 0.650 0.650
128 ARG 334 VAL 0.645 0.000 0.645 0.645
114 CYS 373 TYR 0.645 0.000 0.645 0.645
298 VAL 308 THR 0.000 0.643 -0.643 0.643
172 PHE 185 ASN 3.465 2.824 0.641 0.641
183 ILE 189 VAL 1.071 1.702 -0.631 0.631
112 MET 161 ALA 3.113 2.483 0.630 0.630
292 PRO 293 LYS 0.623 0.000 0.623 0.623
116 ALA 158 TRP 1.747 1.134 0.613 0.613
119 LEU 200 PRO 0.964 0.359 0.605 0.605
118 ILE 200 PRO 0.751 1.354 -0.603 0.603
51 CYS 69 VAL 0.098 0.691 -0.593 0.593
47 ASN 376 SER 1.889 2.473 -0.584 0.584
133 VAL 214 VAL 0.078 0.659 -0.581 0.581
59 ALA 323 ARG 0.000 0.578 -0.578 0.578
62 THR 64 THR 0.862 0.286 0.576 0.576
129 TYR 211 ILE 3.199 3.765 -0.566 0.566
162 PHE 166 CYS 0.594 1.158 -0.564 0.564
96 TRP 180 VAL 0.639 0.075 0.564 0.564
345 PHE 369 THR 3.910 3.347 0.563 0.563
139 GLN 140 HIS 0.552 0.000 0.552 0.552
197 PHE 343 LEU 4.338 3.790 0.547 0.547
98 PHE 102 CYS 0.835 0.288 0.546 0.546
351 LEU 360 VAL 0.639 0.096 0.544 0.544
370 TRP 374 VAL 3.286 3.828 -0.542 0.542
108 THR 168 LEU 2.809 3.351 -0.542 0.542
33 ALA 90 GLU 0.538 0.000 0.538 0.538
71 LEU 124 ILE 0.716 0.179 0.537 0.537
188 PHE 191 TYR 0.000 0.535 -0.535 0.535
212 TYR 216 LYS 0.602 1.126 -0.525 0.525
127 ASP 150 VAL 0.524 0.000 0.524 0.524
149 ARG 150 VAL 0.523 0.000 0.523 0.523
214 VAL 218 ARG 1.216 1.734 -0.518 0.518
299 ARG 305 ARG 0.000 0.517 -0.517 0.517
132 VAL 214 VAL 0.923 0.406 0.517 0.517
70 SER 154 ILE 1.807 2.320 -0.513 0.513
96 TRP 181 CYS 4.009 4.520 -0.511 0.511
100 ARG 180 VAL 2.505 1.995 0.510 0.510
112 MET 158 TRP 0.759 1.269 -0.509 0.509
118 ILE 197 PHE 0.665 1.172 -0.507 0.507
215 LEU 320 VAL 0.000 0.503 -0.503 0.503
331 VAL 335 LEU 0.501 0.000 0.501 0.501
46 GLY 394 PHE 0.000 0.495 -0.495 0.495
67 LEU 154 ILE 1.345 0.850 0.495 0.495
74 ALA 116 ALA 0.736 0.247 0.489 0.489
132 VAL 328 THR 0.000 0.486 -0.486 0.486
122 CYS 126 ILE 0.475 0.000 0.475 0.475
9 SER 10 HIS 0.676 0.202 0.474 0.474
131 ALA 258 ILE 0.474 0.000 0.474 0.474
89 LEU 106 PHE 1.245 0.774 0.471 0.471
50 VAL 380 PRO 0.814 1.283 -0.469 0.469
361 SER 362 PRO 1.102 0.634 0.468 0.468
358 CYS 360 VAL 0.468 0.000 0.468 0.468
40 ILE 79 ALA 2.389 1.923 0.466 0.466
180 VAL 182 SER 0.820 0.357 0.462 0.462
215 LEU 328 THR 0.000 0.462 -0.462 0.462
197 PHE 198 TYR 2.677 3.138 -0.461 0.461
78 VAL 114 CYS 0.461 0.000 0.461 0.461
334 VAL 383 TYR 1.191 0.733 0.457 0.457
362 PRO 363 GLU 1.100 1.555 -0.455 0.455
379 ASN 383 TYR 0.863 1.313 -0.450 0.450
294 LEU 312 LEU 0.000 0.448 -0.448 0.448
78 VAL 376 SER 0.448 0.000 0.448 0.448
352 ASN 360 VAL 2.131 1.684 0.447 0.447
127 ASP 153 MET 0.834 0.390 0.444 0.444
43 ILE 377 ALA 2.282 1.840 0.442 0.442
94 GLY 180 VAL 0.456 0.016 0.439 0.439
2 ALA 3 SER 1.051 1.488 -0.437 0.437
119 LEU 161 ALA 0.673 1.110 -0.436 0.436
114 CYS 118 ILE 0.000 0.435 -0.435 0.435
133 VAL 134 MET 0.224 0.658 -0.435 0.435
351 LEU 355 CYS 0.534 0.100 0.433 0.433
350 VAL 354 HIS 0.000 0.432 -0.432 0.432
31 TYR 32 TYR 0.426 0.000 0.426 0.426
361 SER 364 LEU 0.511 0.936 -0.425 0.425
111 VAL 164 VAL 0.422 0.000 0.422 0.422
120 ASN 157 VAL 3.514 3.932 -0.419 0.419
130 THR 134 MET 0.225 0.640 -0.415 0.415
139 GLN 254 ARG 0.414 0.000 0.414 0.414
89 LEU 96 TRP 1.977 1.563 0.414 0.414
63 THR 64 THR 0.241 0.654 -0.413 0.413
47 ASN 76 LEU 2.381 1.974 0.408 0.408
359 HIS 361 SER 0.000 0.407 -0.407 0.407
59 ALA 389 GLU 0.000 0.404 -0.404 0.404
175 THR 180 VAL 1.495 1.897 -0.402 0.402
208 TYR 335 LEU 2.588 2.187 0.402 0.402
128 ARG 331 VAL 0.000 0.401 -0.401 0.401
64 THR 124 ILE 0.000 0.400 -0.400 0.400
281 LYS 282 THR 0.398 0.000 0.398 0.398
316 GLN 317 PRO 0.786 0.388 0.397 0.397
114 CYS 346 PHE 0.000 0.395 -0.395 0.395
296 LEU 298 VAL 0.647 0.254 0.393 0.393
185 ASN 353 THR 0.390 0.000 0.390 0.390
264 LEU 323 ARG 0.390 0.000 0.390 0.390
62 THR 65 ASN 3.726 4.113 -0.387 0.387
125 SER 126 ILE 0.387 0.000 0.387 0.387
74 ALA 120 ASN 0.450 0.064 0.386 0.386
337 ALA 382 ILE 0.908 0.526 0.382 0.382
54 VAL 61 GLN 2.601 2.221 0.380 0.380
291 ALA 292 PRO 0.083 0.463 -0.380 0.380
300 LYS 306 LEU 0.000 0.379 -0.379 0.379
132 VAL 218 ARG 4.983 5.362 -0.379 0.379
148 ARG 152 LEU 0.000 0.378 -0.378 0.378
32 TYR 35 SER 0.000 0.377 -0.377 0.377
68 VAL 124 ILE 0.567 0.937 -0.370 0.370
216 LYS 220 ARG 2.345 1.975 0.370 0.370
124 ILE 208 TYR 0.368 0.000 0.368 0.368
164 VAL 196 SER 1.273 0.908 0.365 0.365
131 ALA 138 TYR 7.133 7.497 -0.363 0.363
138 TYR 146 SER 0.361 0.000 0.361 0.361
223 ILE 227 GLN 0.567 0.208 0.360 0.360
71 LEU 383 TYR 1.220 0.867 0.353 0.353
173 ASN 182 SER 1.660 2.012 -0.352 0.352
82 VAL 110 ASP 4.508 4.161 0.347 0.347
111 VAL 183 ILE 0.923 0.579 0.344 0.344
277 LYS 278 ARG 0.343 0.000 0.343 0.343
126 ILE 153 MET 0.340 0.000 0.340 0.340
142 THR 146 SER 0.000 0.337 -0.337 0.337
81 LEU 109 LEU 0.707 0.373 0.334 0.334
74 ALA 158 TRP 2.440 2.110 0.329 0.329
36 TYR 90 GLU 1.867 2.195 -0.327 0.327
385 THR 394 PHE 0.324 0.000 0.324 0.324
96 TRP 102 CYS 3.377 3.055 0.323 0.323
32 TYR 90 GLU 0.891 0.570 0.321 0.321
85 TRP 96 TRP 1.486 1.806 -0.321 0.321
57 GLU 60 LEU 1.048 1.368 -0.320 0.320
63 THR 149 ARG 0.000 0.316 -0.316 0.316
105 VAL 169 LEU 0.346 0.660 -0.313 0.313
380 PRO 394 PHE 0.000 0.309 -0.309 0.309
276 LEU 277 LYS 0.309 0.000 0.309 0.309
95 VAL 179 THR 2.088 1.783 0.305 0.305
111 VAL 168 LEU 1.233 0.929 0.304 0.304
78 VAL 117 SER 0.304 0.000 0.304 0.304
360 VAL 365 TYR 0.000 0.302 -0.302 0.302
177 ASP 179 THR 5.865 5.564 0.301 0.301
351 LEU 358 CYS 0.626 0.325 0.301 0.301
88 TYR 89 LEU 0.000 0.300 -0.300 0.300
66 TYR 150 VAL 0.326 0.620 -0.294 0.294
160 LEU 164 VAL 0.293 0.000 0.293 0.293
293 LYS 312 LEU 0.000 0.290 -0.290 0.290
63 THR 150 VAL 3.551 3.262 0.289 0.289
70 SER 158 TRP 2.768 2.481 0.288 0.288
95 VAL 97 ASN 1.053 1.340 -0.287 0.287
32 TYR 366 SER 0.285 0.000 0.285 0.285
49 LEU 397 ILE 0.709 0.989 -0.280 0.280
122 CYS 200 PRO 2.405 2.683 -0.279 0.279
177 ASP 180 VAL 0.250 0.527 -0.277 0.277
330 MET 333 ILE 0.276 0.000 0.276 0.276
53 ALA 60 LEU 2.429 2.158 0.271 0.271
210 ARG 213 VAL 0.267 0.000 0.267 0.267
35 SER 36 TYR 0.000 0.267 -0.267 0.267
233 SER 234 VAL 0.266 0.000 0.266 0.266
344 PRO 368 THR 2.722 2.988 -0.265 0.265
306 LEU 307 SER 0.265 0.000 0.265 0.265
44 VAL 76 LEU 1.810 2.074 -0.265 0.265
130 THR 135 PRO 0.429 0.166 0.263 0.263
219 ARG 223 ILE 0.869 0.607 0.262 0.262
326 LYS 388 ILE 0.000 0.260 -0.260 0.260
185 ASN 187 ASP 1.463 1.203 0.260 0.260
17 ALA 18 GLU 0.259 0.000 0.259 0.259
89 LEU 95 VAL 0.627 0.885 -0.258 0.258
80 THR 81 LEU 0.976 1.231 -0.255 0.255
213 VAL 217 GLN 1.429 1.683 -0.254 0.254
251 GLU 254 ARG 0.000 0.254 -0.254 0.254
116 ALA 157 VAL 1.480 1.228 0.253 0.253
86 VAL 373 TYR 1.682 1.930 -0.249 0.249
193 SER 350 VAL 1.098 1.345 -0.247 0.247
309 SER 311 LYS 0.000 0.241 -0.241 0.241
337 ALA 378 LEU 0.000 0.239 -0.239 0.239
104 ASP 169 LEU 0.814 0.576 0.238 0.238
338 PHE 343 LEU 0.377 0.143 0.234 0.234
103 CYS 181 CYS 6.688 6.455 0.233 0.233
54 VAL 390 PHE 1.471 1.238 0.232 0.232
293 LYS 311 LYS 0.000 0.231 -0.231 0.231
106 PHE 107 VAL 0.566 0.796 -0.230 0.230
173 ASN 175 THR 0.698 0.926 -0.228 0.228
82 VAL 113 MET 0.226 0.000 0.226 0.226
262 THR 387 ASN 0.226 0.000 0.226 0.226
192 SER 193 SER 0.226 0.000 0.226 0.226
88 TYR 92 THR 3.181 2.957 0.224 0.224
208 TYR 383 TYR 0.223 0.000 0.223 0.223
225 THR 229 SER 0.000 0.220 -0.220 0.220
60 LEU 389 GLU 2.088 2.300 -0.212 0.212
47 ASN 379 ASN 0.000 0.211 -0.211 0.211
85 TRP 102 CYS 0.209 0.000 0.209 0.209
43 ILE 79 ALA 1.478 1.272 0.206 0.206
89 LEU 94 GLY 3.724 3.926 -0.202 0.202
43 ILE 47 ASN 1.226 1.027 0.199 0.199
121 LEU 204 THR 0.213 0.411 -0.199 0.199
350 VAL 355 CYS 0.327 0.131 0.196 0.196
115 THR 119 LEU 1.113 0.920 0.193 0.193
53 ALA 397 ILE 1.957 1.765 0.192 0.192
218 ARG 222 ARG 0.000 0.191 -0.191 0.191
27 ARG 28 PRO 0.554 0.744 -0.190 0.190
341 CYS 372 GLY 2.280 2.092 0.188 0.188
61 GLN 66 TYR 2.897 2.709 0.188 0.188
103 CYS 173 ASN 0.606 0.792 -0.185 0.185
122 CYS 204 THR 2.865 2.680 0.185 0.185
329 GLN 333 ILE 0.744 0.559 0.185 0.185
43 ILE 75 ASP 1.946 1.761 0.185 0.185
51 CYS 73 VAL 0.072 0.256 -0.184 0.184
211 ILE 215 LEU 0.714 0.897 -0.183 0.183
168 LEU 183 ILE 0.240 0.058 0.182 0.182
64 THR 65 ASN 0.303 0.120 0.182 0.182
369 THR 373 TYR 1.376 1.194 0.182 0.182
360 VAL 364 LEU 0.000 0.181 -0.181 0.181
92 THR 97 ASN 0.376 0.195 0.181 0.181
341 CYS 368 THR 0.114 0.294 -0.180 0.180
118 ILE 122 CYS 0.000 0.180 -0.180 0.180
154 ILE 158 TRP 1.079 1.258 -0.179 0.179
189 VAL 354 HIS 0.309 0.132 0.177 0.177
196 SER 346 PHE 0.175 0.000 0.175 0.175
134 MET 218 ARG 0.000 0.175 -0.175 0.175
77 LEU 82 VAL 0.973 0.800 0.174 0.174
259 CYS 260 GLN 0.173 0.000 0.173 0.173
203 VAL 207 VAL 0.432 0.259 0.173 0.173
184 SER 189 VAL 0.173 0.000 0.173 0.173
86 VAL 106 PHE 1.155 1.327 -0.172 0.172
378 LEU 382 ILE 0.422 0.251 0.171 0.171
244 SER 245 PRO 0.805 0.974 -0.169 0.169
207 VAL 211 ILE 0.335 0.505 -0.169 0.169
111 VAL 196 SER 0.000 0.168 -0.168 0.168
183 ILE 349 HIS 1.016 0.850 0.166 0.166
36 TYR 87 VAL 1.332 1.167 0.166 0.166
167 PRO 188 PHE 1.217 1.053 0.164 0.164
197 PHE 338 PHE 1.528 1.365 0.163 0.163
391 ARG 395 LEU 0.000 0.163 -0.163 0.163
107 VAL 181 CYS 0.711 0.551 0.160 0.160
173 ASN 184 SER 0.000 0.160 -0.160 0.160
116 ALA 161 ALA 1.740 1.899 -0.159 0.159
201 PHE 204 THR 0.000 0.159 -0.159 0.159
81 LEU 85 TRP 0.157 0.000 0.157 0.157
150 VAL 154 ILE 0.980 0.824 0.156 0.156
263 ALA 388 ILE 0.156 0.000 0.156 0.156
115 THR 165 SER 0.000 0.155 -0.155 0.155
53 ALA 394 PHE 1.384 1.228 0.155 0.155
127 ASP 138 TYR 6.833 6.680 0.153 0.153
198 TYR 343 LEU 0.149 0.000 0.149 0.149
185 ASN 186 PRO 1.593 1.445 0.149 0.149
115 THR 161 ALA 2.243 2.094 0.148 0.148
136 VAL 137 HIS 0.148 0.000 0.148 0.148
192 SER 197 PHE 0.200 0.348 -0.147 0.147
342 TRP 346 PHE 2.112 2.259 -0.146 0.146
43 ILE 373 TYR 0.537 0.683 -0.146 0.146
50 VAL 68 VAL 0.557 0.703 -0.146 0.146
356 GLN 357 THR 0.145 0.000 0.145 0.145
48 GLY 76 LEU 0.915 1.059 -0.145 0.145
61 GLN 142 THR 0.144 0.000 0.144 0.144
345 PHE 349 HIS 0.160 0.303 -0.144 0.144
96 TRP 179 THR 6.330 6.472 -0.142 0.142
200 PRO 338 PHE 0.141 0.000 0.141 0.141
100 ARG 103 CYS 0.141 0.000 0.141 0.141
51 CYS 72 ALA 0.514 0.653 -0.140 0.140
329 GLN 386 PHE 0.000 0.139 -0.139 0.139
294 LEU 295 SER 0.139 0.000 0.139 0.139
219 ARG 321 PRO 0.138 0.000 0.138 0.138
368 THR 369 THR 0.037 0.174 -0.136 0.136
60 LEU 65 ASN 6.172 6.307 -0.135 0.135
54 VAL 69 VAL 1.908 2.041 -0.134 0.134
374 VAL 378 LEU 0.926 0.792 0.134 0.134
261 ASP 388 ILE 0.133 0.000 0.133 0.133
77 LEU 81 LEU 0.963 0.830 0.132 0.132
39 LEU 374 VAL 2.029 2.158 -0.129 0.129
321 PRO 323 ARG 0.000 0.128 -0.128 0.128
146 SER 149 ARG 0.317 0.443 -0.126 0.126
128 ARG 327 ALA 0.000 0.126 -0.126 0.126
155 THR 159 VAL 0.478 0.357 0.121 0.121
67 LEU 153 MET 0.818 0.937 -0.118 0.118
50 VAL 390 PHE 0.592 0.475 0.117 0.117
219 ARG 319 GLY 0.114 0.000 0.114 0.114
183 ILE 188 PHE 1.319 1.206 0.113 0.113
47 ASN 50 VAL 0.000 0.112 -0.112 0.112
78 VAL 373 TYR 1.200 1.312 -0.112 0.112
3 SER 5 SER 0.000 0.112 -0.112 0.112
382 ILE 387 ASN 0.000 0.110 -0.110 0.110
126 ILE 130 THR 0.096 0.206 -0.110 0.110
82 VAL 109 LEU 1.312 1.421 -0.109 0.109
53 ALA 390 PHE 0.424 0.532 -0.107 0.107
344 PRO 371 LEU 0.337 0.444 -0.106 0.106
122 CYS 125 SER 0.106 0.000 0.106 0.106
312 LEU 315 LEU 0.106 0.000 0.106 0.106
19 ASN 20 SER 0.000 0.105 -0.105 0.105
190 ILE 194 VAL 0.185 0.289 -0.104 0.104
67 LEU 120 ASN 0.601 0.705 -0.104 0.104
67 LEU 123 ALA 1.276 1.380 -0.103 0.103
119 LEU 195 VAL 0.101 0.000 0.101 0.101
36 TYR 366 SER 0.607 0.507 0.100 0.100
173 ASN 183 ILE 0.502 0.403 0.099 0.099
129 TYR 130 THR 0.000 0.097 -0.097 0.097
51 CYS 76 LEU 0.520 0.423 0.097 0.097
23 ALA 27 ARG 0.000 0.097 -0.097 0.097
73 VAL 158 TRP 0.358 0.262 0.096 0.096
108 THR 169 LEU 4.931 4.834 0.096 0.096
193 SER 198 TYR 5.638 5.733 -0.095 0.095
255 TYR 259 CYS 0.000 0.095 -0.095 0.095
208 TYR 211 ILE 0.697 0.604 0.093 0.093
28 PRO 32 TYR 0.092 0.000 0.092 0.092
101 ILE 105 VAL 0.000 0.092 -0.092 0.092
126 ILE 207 VAL 0.565 0.473 0.092 0.092
379 ASN 380 PRO 0.947 1.038 -0.092 0.092
339 ILE 343 LEU 0.584 0.493 0.091 0.091
132 VAL 133 VAL 0.090 0.000 0.090 0.090
341 CYS 374 VAL 0.090 0.000 0.090 0.090
384 THR 385 THR 0.357 0.268 0.089 0.089
164 VAL 195 VAL 1.320 1.408 -0.088 0.088
100 ARG 179 THR 0.000 0.088 -0.088 0.088
126 ILE 203 VAL 0.087 0.000 0.087 0.087
116 ALA 120 ASN 0.117 0.203 -0.086 0.086
169 LEU 170 PHE 0.086 0.000 0.086 0.086
254 ARG 258 ILE 0.000 0.085 -0.085 0.085
287 SER 288 PRO 0.625 0.708 -0.083 0.083
39 LEU 377 ALA 0.770 0.689 0.081 0.081
125 SER 211 ILE 0.450 0.530 -0.080 0.080
78 VAL 84 PRO 0.060 0.139 -0.079 0.079
357 THR 358 CYS 0.000 0.079 -0.079 0.079
364 LEU 368 THR 0.442 0.363 0.078 0.078
40 ILE 44 VAL 0.226 0.149 0.078 0.078
28 PRO 29 HIS 0.078 0.155 -0.077 0.077
109 LEU 113 MET 0.475 0.399 0.076 0.076
106 PHE 181 CYS 0.776 0.851 -0.075 0.075
78 VAL 82 VAL 0.018 0.090 -0.073 0.073
162 PHE 165 SER 0.072 0.000 0.072 0.072
77 LEU 113 MET 2.777 2.705 0.072 0.072
164 VAL 165 SER 0.000 0.072 -0.072 0.072
194 VAL 198 TYR 0.250 0.179 0.071 0.071
194 VAL 200 PRO 0.446 0.516 -0.070 0.070
215 LEU 327 ALA 0.070 0.000 0.070 0.070
43 ILE 76 LEU 0.228 0.297 -0.069 0.069
39 LEU 370 TRP 0.514 0.446 0.069 0.069
69 VAL 73 VAL 0.253 0.185 0.068 0.068
58 ARG 61 GLN 0.520 0.587 -0.067 0.067
222 ARG 226 ARG 0.065 0.000 0.065 0.065
343 LEU 344 PRO 0.880 0.946 -0.065 0.065
326 LYS 330 MET 0.065 0.000 0.065 0.065
103 CYS 182 SER 0.058 0.123 -0.065 0.065
96 TRP 178 PRO 0.866 0.930 -0.064 0.064
33 ALA 91 VAL 0.706 0.642 0.063 0.063
330 MET 390 PHE 0.000 0.063 -0.063 0.063
256 TYR 261 ASP 0.062 0.000 0.062 0.062
177 ASP 178 PRO 2.661 2.723 -0.062 0.062
129 TYR 134 MET 0.147 0.086 0.062 0.062
121 LEU 124 ILE 0.000 0.061 -0.061 0.061
194 VAL 199 LEU 3.204 3.265 -0.061 0.061
107 VAL 183 ILE 1.589 1.650 -0.061 0.061
79 ALA 83 MET 0.272 0.212 0.060 0.060
226 ARG 229 SER 0.059 0.000 0.059 0.059
78 VAL 83 MET 4.762 4.821 -0.059 0.059
60 LEU 393 ALA 0.710 0.652 0.059 0.059
32 TYR 363 GLU 0.118 0.175 -0.058 0.058
89 LEU 92 THR 0.075 0.132 -0.056 0.056
43 ILE 83 MET 1.238 1.182 0.056 0.056
50 VAL 72 ALA 0.770 0.826 -0.056 0.056
252 LEU 256 TYR 0.000 0.055 -0.055 0.055
77 LEU 158 TRP 0.744 0.800 -0.055 0.055
75 ASP 380 PRO 0.055 0.000 0.055 0.055
204 THR 205 VAL 0.000 0.055 -0.055 0.055
379 ASN 384 THR 0.055 0.000 0.055 0.055
68 VAL 390 PHE 0.087 0.142 -0.054 0.054
89 LEU 181 CYS 0.198 0.144 0.053 0.053
120 ASN 158 TRP 0.053 0.000 0.053 0.053
162 PHE 169 LEU 0.000 0.052 -0.052 0.052
100 ARG 104 ASP 0.000 0.052 -0.052 0.052
231 CYS 232 ASN 0.000 0.051 -0.051 0.051
345 PHE 368 THR 4.428 4.479 -0.051 0.051
36 TYR 83 MET 1.302 1.253 0.050 0.050
42 ALA 377 ALA 0.033 0.083 -0.049 0.049
87 VAL 91 VAL 0.210 0.162 0.048 0.048
65 ASN 68 VAL 0.000 0.045 -0.045 0.045
355 CYS 358 CYS 3.749 3.792 -0.044 0.044
322 LEU 326 LYS 0.000 0.043 -0.043 0.043
183 ILE 353 THR 0.018 0.061 -0.043 0.043
117 SER 376 SER 0.042 0.000 0.042 0.042
44 VAL 80 THR 0.198 0.158 0.040 0.040
39 LEU 43 ILE 1.352 1.313 0.039 0.039
383 TYR 384 THR 0.039 0.000 0.039 0.039
229 SER 230 GLN 0.039 0.000 0.039 0.039
121 LEU 342 TRP 0.038 0.000 0.038 0.038
212 TYR 213 VAL 0.038 0.000 0.038 0.038
139 GLN 258 ILE 0.038 0.000 0.038 0.038
132 VAL 211 ILE 0.478 0.441 0.038 0.038
370 TRP 371 LEU 0.115 0.078 0.037 0.037
82 VAL 373 TYR 1.185 1.222 -0.037 0.037
100 ARG 177 ASP 5.690 5.727 -0.037 0.037
348 THR 360 VAL 0.601 0.638 -0.037 0.037
182 SER 184 SER 0.075 0.039 0.036 0.036
348 THR 368 THR 3.397 3.363 0.034 0.034
280 GLU 281 LYS 0.000 0.034 -0.034 0.034
92 THR 95 VAL 0.524 0.490 0.034 0.034
341 CYS 342 TRP 0.329 0.295 0.034 0.034
36 TYR 39 LEU 0.085 0.052 0.033 0.033
86 VAL 90 GLU 0.000 0.032 -0.032 0.032
157 VAL 158 TRP 0.031 0.000 0.031 0.031
136 VAL 139 GLN 0.031 0.000 0.031 0.031
108 THR 166 CYS 0.030 0.000 0.030 0.030
73 VAL 77 LEU 0.550 0.521 0.030 0.030
44 VAL 79 ALA 0.660 0.689 -0.028 0.028
79 ALA 84 PRO 1.889 1.917 -0.028 0.028
178 PRO 179 THR 0.000 0.028 -0.028 0.028
189 VAL 350 VAL 0.192 0.220 -0.028 0.028
342 TRP 373 TYR 0.000 0.027 -0.027 0.027
36 TYR 369 THR 1.049 1.076 -0.027 0.027
103 CYS 107 VAL 0.368 0.395 -0.027 0.027
110 ASP 115 THR 0.027 0.000 0.027 0.027
111 VAL 115 THR 0.500 0.476 0.024 0.024
52 MET 397 ILE 1.368 1.344 0.023 0.023
270 GLN 271 GLU 0.000 0.021 -0.021 0.021
189 VAL 193 SER 0.345 0.366 -0.021 0.021
44 VAL 49 LEU 0.021 0.000 0.021 0.021
55 LEU 61 GLN 1.620 1.640 -0.020 0.020
376 SER 379 ASN 0.019 0.000 0.019 0.019
198 TYR 347 LEU 1.538 1.557 -0.019 0.019
129 TYR 207 VAL 1.538 1.520 0.018 0.018
94 GLY 179 THR 0.717 0.700 0.017 0.017
64 THR 141 GLY 0.017 0.000 0.017 0.017
119 LEU 157 VAL 4.421 4.438 -0.017 0.017
43 ILE 48 GLY 0.189 0.206 -0.016 0.016
83 MET 84 PRO 0.704 0.689 0.016 0.016
330 MET 382 ILE 0.660 0.644 0.016 0.016
53 ALA 393 ALA 0.689 0.704 -0.015 0.015
199 LEU 203 VAL 0.156 0.170 -0.014 0.014
36 TYR 373 TYR 0.909 0.924 -0.014 0.014
123 ALA 157 VAL 0.503 0.490 0.013 0.013
222 ARG 225 THR 0.013 0.000 0.013 0.013
188 PHE 193 SER 0.028 0.040 -0.011 0.011
111 VAL 188 PHE 0.010 0.000 0.010 0.010
105 VAL 109 LEU 0.762 0.753 0.010 0.010
40 ILE 87 VAL 0.497 0.506 -0.009 0.009
77 LEU 80 THR 0.166 0.174 -0.009 0.009
103 CYS 104 ASP 0.000 0.009 -0.009 0.009
341 CYS 378 LEU 0.531 0.540 -0.008 0.008
42 ALA 47 ASN 0.000 0.007 -0.007 0.007
235 ARG 236 PRO 0.294 0.287 0.007 0.007
63 THR 128 ARG 0.000 0.006 -0.006 0.006
39 LEU 373 TYR 1.510 1.515 -0.005 0.005
224 LEU 227 GLN 0.391 0.390 0.001 0.001
134 MET 135 PRO 0.098 0.099 -0.001 0.001
82 VAL 86 VAL 0.262 0.263 -0.001 0.001
179 THR 180 VAL 0.433 0.433 -0.000 0.000

RRCS change distribution

0.13
Mean ΔRRCS
1.83
Std Dev
0.04
Median

Magnitude classification

21
High (|Δ| ≥ 5.0)
49
Medium (2.5 ≤ |Δ| < 5.0)
672
Low (|Δ| < 2.5)

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| ≥ 2.54, 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