GPCompReports

OPRM

Gene OPRM1 Opioid receptors Peptide receptors UniProt P35372
819
Total Contact Pairs
94
Significant Changes
13.90
Max Increase
-9.02
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 T99 12.48x48 T99 12.48x48 T K100 12.49x49 K100 12.49x49 K M101 12.50x50 M101 12.50x50 M K102 12.51x51 K102 12.51x51 K ICL1ECL1 T134 23.49x49 T134 23.49x49 T W135 23.50x50 W135 23.50x50 W P136 23.51x51 P136 23.51x51 P F137 23.52x52 F137 23.52x52 F ECL1ICL2 P174 34.50x50 P174 34.50x50 P V175 34.51x51 V175 34.51x51 V K176 34.52x52 K176 34.52x52 K A177 34.53x53 A177 34.53x53 A L178 34.54x54 L178 34.54x54 L D179 34.55x55 D179 34.55x55 D F180 34.56x56 F180 34.56x56 F R181 34.57x57 R181 34.57x57 R ICL2ECL2 T209 T209 T T210 T210 T K211 K211 K Y212 Y212 Y R213 R213 R Q214 Q214 Q G215 G215 G S216 S216 S I217 I217 I D218 D218 D C219 45.50x50 C219 45.50x50 C T220 45.51x51 T220 45.51x51 T L221 45.52x52 L221 45.52x52 L T222 T222 T F223 F223 F S224 S224 S H225 H225 H ECL2ICL3 R265 R265 R M266 M266 M L267 L267 L S268 S268 S G269 G269 G ICL3ECL3 T309 T309 T I310 I310 I P311 P311 P E312 E312 E ECL3N-term M1 M1 M D2 D2 D S3 S3 S S4 S4 S A5 A5 A A6 A6 A P7 P7 P T8 T8 T N9 N9 N A10 A10 A S11 S11 S N12 N12 N C13 C13 C T14 T14 T D15 D15 D A16 A16 A L17 L17 L A18 A18 A Y19 Y19 Y S20 S20 S S21 S21 S C22 C22 C S23 S23 S P24 P24 P A25 A25 A P26 P26 P S27 S27 S P28 P28 P G29 G29 G S30 S30 S W31 W31 W V32 V32 V N33 N33 N L34 L34 L S35 S35 S H36 H36 H L37 L37 L D38 D38 D G39 G39 G N40 N40 N L41 L41 L S42 S42 S D43 D43 D P44 P44 P C45 C45 C G46 G46 G P47 P47 P N48 N48 N R49 R49 R T50 T50 T D51 D51 D L52 L52 L G53 G53 G G54 G54 G R55 R55 R D56 D56 D S57 S57 S L58 L58 L C59 C59 C P60 P60 P P61 P61 P T62 T62 T G63 G63 G S64 S64 S P65 P65 P S66 S66 S N-termC-term P355 P355 P T356 T356 T S357 S357 S S358 S358 S N359 N359 N I360 I360 I E361 E361 E Q362 Q362 Q Q363 Q363 Q N364 N364 N S365 S365 S T366 T366 T R367 R367 R I368 I368 I R369 R369 R Q370 Q370 Q N371 N371 N T372 T372 T R373 R373 R D374 D374 D H375 H375 H P376 P376 P S377 S377 S T378 T378 T A379 A379 A N380 N380 N T381 T381 T V382 V382 V D383 D383 D R384 R384 R T385 T385 T N386 N386 N H387 H387 H Q388 Q388 Q L389 L389 L E390 E390 E N391 N391 N L392 L392 L E393 E393 E A394 A394 A E395 E395 E T396 T396 T A397 A397 A P398 P398 P L399 L399 L P400 P400 P C-term M67 1.29x29 M67 1.29x29 M I68 1.30x30 I68 1.30x30 I T69 1.31x31 T69 1.31x31 T A70 1.32x32 A70 1.32x32 A I71 1.33x33 I71 1.33x33 I T72 1.34x34 T72 1.34x34 T I73 1.35x35 I73 1.35x35 I M74 1.36x36 M74 1.36x36 M A75 1.37x37 A75 1.37x37 A L76 1.38x38 L76 1.38x38 L Y77 1.39x39 Y77 1.39x39 Y S78 1.40x40 S78 1.40x40 S I79 1.41x41 I79 1.41x41 I V80 1.42x42 V80 1.42x42 V C81 1.43x43 C81 1.43x43 C V82 1.44x44 V82 1.44x44 V V83 1.45x45 V83 1.45x45 V G84 1.46x46 G84 1.46x46 G L85 1.47x47 L85 1.47x47 L F86 1.48x48 F86 1.48x48 F G87 1.49x49 G87 1.49x49 G N88 1.50x50 N88 1.50x50 N F89 1.51x51 F89 1.51x51 F L90 1.52x52 L90 1.52x52 L V91 1.53x53 V91 1.53x53 V M92 1.54x54 M92 1.54x54 M Y93 1.55x55 Y93 1.55x55 Y V94 1.56x56 V94 1.56x56 V I95 1.57x57 I95 1.57x57 I V96 1.58x58 V96 1.58x58 V R97 1.59x59 R97 1.59x59 R Y98 1.60x60 Y98 1.60x60 Y T103 2.37x37 T103 2.37x37 T A104 2.38x38 A104 2.38x38 A T105 2.39x39 T105 2.39x39 T N106 2.40x40 N106 2.40x40 N I107 2.41x41 I107 2.41x41 I Y108 2.42x42 Y108 2.42x42 Y I109 2.43x43 I109 2.43x43 I F110 2.44x44 F110 2.44x44 F N111 2.45x45 N111 2.45x45 N L112 2.46x46 L112 2.46x46 L A113 2.47x47 A113 2.47x47 A L114 2.48x48 L114 2.48x48 L A115 2.49x49 A115 2.49x49 A D116 2.50x50 D116 2.50x50 D A117 2.51x51 A117 2.51x51 A L118 2.52x52 L118 2.52x52 L A119 2.53x53 A119 2.53x53 A T120 2.54x54 T120 2.54x54 T S121 2.55x55 S121 2.55x55 S T122 2.56x56 T122 2.56x56 T L123 2.57x57 L123 2.57x57 L P124 2.58x58 P124 2.58x58 P F125 2.59x59 F125 2.59x59 F Q126 2.60x60 Q126 2.60x60 Q S127 2.61x61 S127 2.61x61 S V128 2.62x62 V128 2.62x62 V N129 2.63x63 N129 2.63x63 N Y130 2.64x64 Y130 2.64x64 Y L131 2.65x65 L131 2.65x65 L M132 2.66x66 M132 2.66x66 M G133 2.67x67 G133 2.67x67 G G138 3.21x21 G138 3.21x21 G T139 3.22x22 T139 3.22x22 T I140 3.23x23 I140 3.23x23 I L141 3.24x24 L141 3.24x24 L C142 3.25x25 C142 3.25x25 C K143 3.26x26 K143 3.26x26 K I144 3.27x27 I144 3.27x27 I V145 3.28x28 V145 3.28x28 V I146 3.29x29 I146 3.29x29 I S147 3.30x30 S147 3.30x30 S I148 3.31x31 I148 3.31x31 I D149 3.32x32 D149 3.32x32 D Y150 3.33x33 Y150 3.33x33 Y Y151 3.34x34 Y151 3.34x34 Y N152 3.35x35 N152 3.35x35 N M153 3.36x36 M153 3.36x36 M F154 3.37x37 F154 3.37x37 F T155 3.38x38 T155 3.38x38 T S156 3.39x39 S156 3.39x39 S I157 3.40x40 I157 3.40x40 I F158 3.41x41 F158 3.41x41 F T159 3.42x42 T159 3.42x42 T L160 3.43x43 L160 3.43x43 L C161 3.44x44 C161 3.44x44 C T162 3.45x45 T162 3.45x45 T M163 3.46x46 M163 3.46x46 M S164 3.47x47 S164 3.47x47 S V165 3.48x48 V165 3.48x48 V D166 3.49x49 D166 3.49x49 D R167 3.50x50 R167 3.50x50 R Y168 3.51x51 Y168 3.51x51 Y I169 3.52x52 I169 3.52x52 I A170 3.53x53 A170 3.53x53 A V171 3.54x54 V171 3.54x54 V C172 3.55x55 C172 3.55x55 C H173 3.56x56 H173 3.56x56 H T182 4.38x38 T182 4.38x38 T P183 4.39x39 P183 4.39x39 P R184 4.40x40 R184 4.40x40 R N185 4.41x41 N185 4.41x41 N A186 4.42x42 A186 4.42x42 A K187 4.43x43 K187 4.43x43 K I188 4.44x44 I188 4.44x44 I I189 4.45x45 I189 4.45x45 I N190 4.46x46 N190 4.46x46 N V191 4.47x47 V191 4.47x47 V C192 4.48x48 C192 4.48x48 C N193 4.49x49 N193 4.49x49 N W194 4.50x50 W194 4.50x50 W I195 4.51x51 I195 4.51x51 I L196 4.52x52 L196 4.52x52 L S197 4.53x53 S197 4.53x53 S S198 4.54x54 S198 4.54x54 S A199 4.55x55 A199 4.55x55 A I200 4.56x56 I200 4.56x56 I G201 4.57x57 G201 4.57x57 G L202 4.58x58 L202 4.58x58 L P203 4.59x59 P203 4.59x59 P V204 4.60x60 V204 4.60x60 V M205 4.61x61 M205 4.61x61 M F206 4.62x62 F206 4.62x62 F M207 4.63x63 M207 4.63x63 M A208 4.64x64 A208 4.64x64 A P226 5.30x31 P226 5.30x31 P T227 5.31x32 T227 5.31x32 T W228 5.32x33 W228 5.32x33 W Y229 5.33x34 Y229 5.33x34 Y W230 5.34x35 W230 5.34x35 W E231 5.35x36 E231 5.35x36 E N232 5.36x37 N232 5.36x37 N L233 5.37x38 L233 5.37x38 L L234 5.38x39 L234 5.38x39 L K235 5.39x40 K235 5.39x40 K I236 5.40x41 I236 5.40x41 I C237 5.41x42 C237 5.41x42 C V238 5.42x43 V238 5.42x43 V F239 5.43x44 F239 5.43x44 F I240 5.44x45 I240 5.44x45 I F241 5.45x46 F241 5.45x46 F A242 5.46x461 A242 5.46x461 A F243 5.47x47 F243 5.47x47 F I244 5.48x48 I244 5.48x48 I M245 5.49x49 M245 5.49x49 M P246 5.50x50 P246 5.50x50 P V247 5.51x51 V247 5.51x51 V L248 5.52x52 L248 5.52x52 L I249 5.53x53 I249 5.53x53 I I250 5.54x54 I250 5.54x54 I T251 5.55x55 T251 5.55x55 T V252 5.56x56 V252 5.56x56 V C253 5.57x57 C253 5.57x57 C Y254 5.58x58 Y254 5.58x58 Y G255 5.59x59 G255 5.59x59 G L256 5.60x60 L256 5.60x60 L M257 5.61x61 M257 5.61x61 M I258 5.62x62 I258 5.62x62 I L259 5.63x63 L259 5.63x63 L R260 5.64x64 R260 5.64x64 R L261 5.65x65 L261 5.65x65 L K262 5.66x66 K262 5.66x66 K S263 5.67x67 S263 5.67x67 S V264 5.68x68 V264 5.68x68 V S270 6.23x23 S270 6.23x23 S K271 6.24x24 K271 6.24x24 K E272 6.25x25 E272 6.25x25 E K273 6.26x26 K273 6.26x26 K D274 6.27x27 D274 6.27x27 D R275 6.28x28 R275 6.28x28 R N276 6.29x29 N276 6.29x29 N L277 6.30x30 L277 6.30x30 L R278 6.31x31 R278 6.31x31 R R279 6.32x32 R279 6.32x32 R I280 6.33x33 I280 6.33x33 I T281 6.34x34 T281 6.34x34 T R282 6.35x35 R282 6.35x35 R M283 6.36x36 M283 6.36x36 M V284 6.37x37 V284 6.37x37 V L285 6.38x38 L285 6.38x38 L V286 6.39x39 V286 6.39x39 V V287 6.40x40 V287 6.40x40 V V288 6.41x41 V288 6.41x41 V A289 6.42x42 A289 6.42x42 A V290 6.43x43 V290 6.43x43 V F291 6.44x44 F291 6.44x44 F I292 6.45x45 I292 6.45x45 I V293 6.46x46 V293 6.46x46 V C294 6.47x47 C294 6.47x47 C W295 6.48x48 W295 6.48x48 W T296 6.49x49 T296 6.49x49 T P297 6.50x50 P297 6.50x50 P I298 6.51x51 I298 6.51x51 I H299 6.52x52 H299 6.52x52 H I300 6.53x53 I300 6.53x53 I Y301 6.54x54 Y301 6.54x54 Y V302 6.55x55 V302 6.55x55 V I303 6.56x56 I303 6.56x56 I I304 6.57x57 I304 6.57x57 I K305 6.58x58 K305 6.58x58 K A306 6.59x59 A306 6.59x59 A L307 6.60x60 L307 6.60x60 L V308 6.61x61 V308 6.61x61 V T313 7.28x27 T313 7.28x27 T T314 7.29x28 T314 7.29x28 T F315 7.30x29 F315 7.30x29 F Q316 7.31x30 Q316 7.31x30 Q T317 7.32x31 T317 7.32x31 T V318 7.33x32 V318 7.33x32 V S319 7.34x33 S319 7.34x33 S W320 7.35x34 W320 7.35x34 W H321 7.36x35 H321 7.36x35 H F322 7.37x36 F322 7.37x36 F C323 7.38x37 C323 7.38x37 C I324 7.39x38 I324 7.39x38 I A325 7.40x39 A325 7.40x39 A L326 7.41x40 L326 7.41x40 L G327 7.42x41 G327 7.42x41 G Y328 7.43x42 Y328 7.43x42 Y T329 7.44x43 T329 7.44x43 T N330 7.45x45 N330 7.45x45 N S331 7.46x46 S331 7.46x46 S C332 7.47x47 C332 7.47x47 C L333 7.48x48 L333 7.48x48 L N334 7.49x49 N334 7.49x49 N P335 7.50x50 P335 7.50x50 P V336 7.51x51 V336 7.51x51 V L337 7.52x52 L337 7.52x52 L Y338 7.53x53 Y338 7.53x53 Y A339 7.54x54 A339 7.54x54 A F340 7.55x55 F340 7.55x55 F L341 7.56x56 L341 7.56x56 L D342 8.47x47 D342 8.47x47 D E343 8.48x48 E343 8.48x48 E N344 8.49x49 N344 8.49x49 N F349 8.54x54 F349 8.54x54 F R350 8.55x55 R350 8.55x55 R E351 8.56x56 E351 8.56x56 E F345 8.50x50 F345 8.50x50 F K346 8.51x51 K346 8.51x51 K R347 8.52x52 R347 8.52x52 R C348 8.53x53 C348 8.53x53 C F352 8.57x57 F352 8.57x57 F C353 8.58x58 C353 8.58x58 C I354 8.59x59 I354 8.59x59 I

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 TYR98 (1.60x60) PHE352 (8.57x57) 13.902 0.000 +13.902 HIGH
2 LEU34 GLU312 9.811 0.000 +9.811 HIGH
3 HIS36 THR62 0.000 9.025 -9.025 HIGH
4 ARG167 (3.50x50) THR281 (6.34x34) 0.000 8.873 -8.873 HIGH
5 TYR254 (5.58x58) LEU285 (6.38x38) 0.000 8.863 -8.863 HIGH
6 SER27 GLU231 (5.35x36) 8.536 0.000 +8.536 HIGH
7 TYR77 (1.39x39) HIS321 (7.36x35) 8.227 0.000 +8.227 HIGH
8 TYR151 (3.34x34) TRP194 (4.50x50) 9.929 2.441 +7.488 HIGH
9 ARG167 (3.50x50) LEU277 (6.30x30) 0.000 7.255 -7.255 HIGH
10 HIS387 GLN388 0.000 6.633 -6.633 HIGH
11 MET101 (12.50x50) ASN106 (2.40x40) 0.160 6.295 -6.135 HIGH
12 HIS36 GLN214 6.033 0.000 +6.033 HIGH
13 GLU390 ASN391 0.000 5.935 -5.935 HIGH
14 LEU118 (2.52x52) ASN152 (3.35x35) 5.736 0.000 +5.736 HIGH
15 ARG167 (3.50x50) ILE280 (6.33x33) 0.000 5.543 -5.543 HIGH
16 SER27 THR227 (5.31x32) 0.023 5.534 -5.510 HIGH
17 TRP31 VAL302 (6.55x55) 0.000 5.491 -5.491 HIGH
18 ASP274 (6.27x27) ARG278 (6.31x31) 1.415 6.884 -5.468 HIGH
19 ARG167 (3.50x50) TYR254 (5.58x58) 5.468 0.000 +5.468 HIGH
20 ALA339 (7.54x54) PHE345 (8.50x50) 5.426 0.069 +5.356 HIGH
21 LEU37 GLN214 5.266 0.000 +5.266 HIGH
22 PRO28 LYS235 (5.39x40) 5.062 0.000 +5.062 HIGH
23 LEU341 (7.56x56) LYS346 (8.51x51) 4.935 0.000 +4.935 MED
24 VAL32 ASP218 4.914 0.000 +4.914 MED
25 SER164 (3.47x47) TYR254 (5.58x58) 6.540 1.647 +4.893 MED
26 GLY29 LEU221 (45.52x52) 0.416 5.201 -4.785 MED
27 PRO28 LEU34 0.000 4.630 -4.630 MED
28 GLU395 THR396 0.000 4.572 -4.572 MED
29 PRO28 GLU231 (5.35x36) 7.315 2.765 +4.550 MED
30 ARG347 (8.52x52) GLU351 (8.56x56) 0.000 4.465 -4.465 MED
31 LEU123 (2.57x57) TYR328 (7.43x42) 7.643 3.230 +4.413 MED
32 THR385 ASN386 0.044 4.456 -4.411 MED
33 MET101 (12.50x50) PHE345 (8.50x50) 0.000 4.322 -4.322 MED
34 MET266 LYS273 (6.26x26) 4.219 0.000 +4.219 MED
35 TYR108 (2.42x42) ASN190 (4.46x46) 6.913 2.711 +4.202 MED
36 PRO335 (7.50x50) PHE340 (7.55x55) 4.193 0.000 +4.193 MED
37 ILE73 (1.35x35) TYR130 (2.64x64) 4.644 0.555 +4.089 MED
38 ILE169 (3.52x52) PHE180 (34.56x56) 4.074 0.000 +4.074 MED
39 MET92 (1.54x54) PHE110 (2.44x44) 2.850 6.788 -3.939 MED
40 LEU267 ASP274 (6.27x27) 1.691 5.623 -3.932 MED
41 TRP31 TYR150 (3.33x33) 0.000 3.927 -3.927 MED
42 TRP31 ASN129 (2.63x63) 3.920 0.000 +3.920 MED
43 LEU90 (1.52x52) PHE349 (8.54x54) 0.000 3.897 -3.897 MED
44 VAL32 TYR130 (2.64x64) 0.000 3.882 -3.882 MED
45 THR155 (3.38x38) ASN193 (4.49x49) 0.000 3.874 -3.874 MED
46 PHE125 (2.59x59) PHE137 (23.52x52) 2.916 6.764 -3.848 MED
47 VAL336 (7.51x51) LEU341 (7.56x56) 3.750 0.000 +3.750 MED
48 PHE158 (3.41x41) ASN193 (4.49x49) 2.251 5.953 -3.702 MED
49 PHE223 GLU231 (5.35x36) 8.093 4.405 +3.689 MED
50 TYR301 (6.54x54) TRP320 (7.35x34) 4.223 7.870 -3.647 MED
51 TYR151 (3.34x34) SER197 (4.53x53) 7.159 3.554 +3.606 MED
52 THR162 (3.45x45) ASN193 (4.49x49) 3.593 0.000 +3.593 MED
53 TYR151 (3.34x34) SER198 (4.54x54) 3.712 7.268 -3.556 MED
54 ASP116 (2.50x50) SER156 (3.39x39) 3.633 0.105 +3.528 MED
55 LEU267 LYS273 (6.26x26) 3.516 0.000 +3.516 MED
56 HIS36 GLY63 0.000 3.464 -3.464 MED
57 TYR168 (3.51x51) MET257 (5.61x61) 0.148 3.572 -3.424 MED
58 TYR77 (1.39x39) LEU123 (2.57x57) 1.042 4.460 -3.419 MED
59 ILE109 (2.43x43) TYR338 (7.53x53) 1.223 4.585 -3.362 MED
60 ASP166 (3.49x49) ARG181 (34.57x57) 7.733 11.093 -3.360 MED
61 ASP383 ARG384 0.000 3.345 -3.345 MED
62 LEU90 (1.52x52) PHE352 (8.57x57) 0.000 3.318 -3.318 MED
63 ALA339 (7.54x54) LYS346 (8.51x51) 0.000 3.316 -3.316 MED
64 THR99 (12.48x48) ASN106 (2.40x40) 3.263 0.000 +3.263 MED
65 TYR150 (3.33x33) VAL204 (4.60x60) 1.285 4.524 -3.239 MED
66 PHE340 (7.55x55) LYS346 (8.51x51) 3.203 0.000 +3.203 MED
67 LYS211 THR222 3.144 0.000 +3.144 MED
68 TYR168 (3.51x51) CYS253 (5.57x57) 4.409 1.268 +3.141 MED
69 ARG167 (3.50x50) TYR338 (7.53x53) 3.121 0.000 +3.121 MED
70 LEU34 LYS305 (6.58x58) 0.000 3.102 -3.102 MED
71 THR50 ASP51 3.833 0.817 +3.016 MED
72 TYR151 (3.34x34) GLY201 0.604 3.602 -2.998 MED
73 LEU160 TYR338 (7.53x53) 2.991 0.000 +2.991 MED
74 SER35 GLY63 1.661 4.646 -2.984 MED
75 PHE154 ILE200 2.461 5.428 -2.967 MED
76 GLU272 ASN276 0.556 3.512 -2.956 MED
77 SER224 TRP230 4.762 7.710 -2.948 MED
78 PHE322 LEU326 2.933 0.000 +2.933 MED
79 PHE180 (34.56x56) ASN185 6.926 4.008 +2.917 MED
80 PHE291 ASN330 1.382 4.189 -2.807 MED
81 ILE298 CYS323 4.584 1.782 +2.802 MED
82 ILE157 TRP295 2.798 0.000 +2.798 MED
83 TYR77 (1.39x39) ILE324 3.817 1.070 +2.747 MED
84 THR159 ASN193 (4.49x49) 0.519 3.244 -2.725 MED
85 TYR254 (5.58x58) MET257 (5.61x61) 1.043 3.757 -2.715 MED
86 TRP295 GLY327 1.904 4.611 -2.706 MED
87 ASN185 ILE189 2.694 0.000 +2.694 MED
88 THR182 ASN185 1.145 3.833 -2.688 MED
89 ILE250 PHE291 2.662 0.000 +2.662 MED
90 VAL96 LYS102 0.000 2.649 -2.649 MED
91 TYR98 (1.60x60) GLU351 (8.56x56) 0.000 2.647 -2.647 MED
92 THR122 ASP149 3.310 0.730 +2.580 MED
93 ASN111 THR159 0.242 2.818 -2.575 MED
94 GLU343 LYS346 (8.51x51) 3.890 1.367 +2.523 MED
95 ASN33 SER35 2.486 0.000 +2.486 LOW
96 GLU272 ARG275 6.393 3.940 +2.452 LOW
97 ILE95 LYS100 2.412 0.000 +2.412 LOW
98 THR155 (3.38x38) TRP194 (4.50x50) 6.366 3.966 +2.400 LOW
99 SER30 ARG213 2.397 0.000 +2.397 LOW
100 TRP135 CYS219 6.068 3.671 +2.397 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| ≥ 2.52 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 73-98 98 (13.9), 77 (8.2), 73 (4.1) 3 92 (-3.9), 90 (-3.9) 2
TM2 106-130 118 (5.7), 123 (4.4), 108 (4.2), 130 (4.1), 129 (3.9), 116 (3.5) 6 106 (-6.1), 110 (-3.9), 125 (-3.8), 109 (-3.4) 4
TM3 150-169 151 (7.5), 152 (5.7), 164 (4.9), 169 (4.1), 162 (3.6), 156 (3.5) 6 167 (-8.9), 150 (-3.9), 155 (-3.9), 158 (-3.7), 168 (-3.4), 166 (-3.4) 6
TM4 190-204 194 (7.5), 190 (4.2), 197 (3.6) 3 193 (-3.9), 198 (-3.6), 204 (-3.2) 3
TM5 227-257 231 (8.5), 235 (5.1), 253 (3.1) 3 254 (-8.9), 227 (-5.5), 257 (-3.4) 3
TM6 273-305 273 (4.2) 1 281 (-8.9), 285 (-8.9), 277 (-7.3), 280 (-5.5), 302 (-5.5), 274 (-5.5), 278 (-5.5), 301 (-3.6), 305 (-3.1) 9
TM7 320-341 321 (8.2), 339 (5.4), 341 (4.9), 328 (4.4), 335 (4.2), 340 (4.2), 336 (3.8) 7 320 (-3.6), 338 (-3.4) 2
Intracellular / Extracellular loops & H8
ICL1 99-101 99 (3.3) 1 101 (-6.1) 1
ICL2 180-181 180 (4.1) 1 181 (-3.4) 1
ICL3 266-267 266 (4.2) 1 267 (-3.9) 1
ECL1 137-137 - 0 137 (-3.8) 1
ECL2 211-223 214 (6.0), 218 (4.9), 223 (3.7), 211 (3.1), 222 (3.1) 5 221 (-4.8) 1
ECL3 312-312 312 (9.8) 1 - 0
H8 345-352 352 (13.9), 345 (5.4), 346 (4.9) 3 347 (-4.5), 351 (-4.5), 349 (-3.9) 3

Interactive visualizations

ΔRRCS distribution

Active vs inactive comparison

Residue-wise changes

TM domain breakdown

Variants of interest

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

Position Protein change DNA change Allele freq Het / Hom ΔRRCS AM score Pathogenicity Conservation dbSNP
352 p.Phe352Leu c.1054T>C 6.84e-07 1 / 0 13.90 0.973 PATHOGENIC 0.94
98 p.Tyr98Cys c.293A>G 3.09e-05 45 / 0 13.90 0.858 PATHOGENIC 1.00 rs373741336
34 p.Glu34Lys c.100G>A 7.15e-07 1 / 0 9.81 0.169 BENIGN 0.34
34 p.Glu34Val c.101A>T 7.15e-07 1 / 0 9.81 - nan -
34 p.Glu34Asp c.102A>C 1.36e-05 19 / 0 9.81 - nan -
34 p.Glu34Asp c.102A>T 7.15e-07 1 / 0 9.81 - nan -
34 p.Lys34Arg c.101A>G 7.14e-07 1 / 0 9.81 - nan - rs1251854747
34 p.Lys34Asn c.102G>C 7.14e-07 1 / 0 9.81 - nan - rs1484361892
36 p.Arg36Cys c.106C>T 1.36e-05 19 / 0 9.02 0.205 BENIGN 0.36 rs200293056
62 p.Thr62Ala c.184A>G 1.37e-06 2 / 0 9.02 0.058 BENIGN 0.38 rs201013311
36 p.Arg36Gly c.106C>G 1.29e-05 18 / 0 9.02 - nan - rs200293056
36 p.Arg36Leu c.107G>T 2.86e-06 4 / 0 9.02 - nan - rs577434238
36 p.Arg36His c.107G>A 1.43e-06 2 / 0 9.02 - nan - rs577434238
36 p.Ala36Val c.107C>T 7.14e-07 1 / 0 9.02 - nan - rs1779567081
36 p.Ala36Glu c.107C>A 7.14e-07 1 / 0 9.02 - nan -
62 p.Thr62Pro c.184A>C 3.57e-05 52 / 0 9.02 - nan - rs201013311
62 p.Thr62Asn c.185C>A 2.06e-06 3 / 0 9.02 - nan - rs1297476429
36 p.His36Tyr c.106C>T 4.38e-05 62 / 1 9.02 - nan - rs199953844
36 p.His36Asn c.106C>A 1.37e-06 2 / 0 9.02 - nan - rs199953844
62 p.Thr62Ser c.185C>G 2.06e-06 3 / 0 9.02 - nan - rs771201043
167 p.Arg167Pro c.500G>C 6.58e-06 1 / 0 8.87 1.000 PATHOGENIC 1.00 rs766402253
167 p.Arg167Gln c.500G>A 6.84e-06 10 / 0 8.87 - nan - rs766402253
254 p.Tyr254His c.760T>C 1.37e-06 2 / 0 8.86 0.994 PATHOGENIC 1.00 rs1290858635
254 p.Tyr254Asp c.760T>G 6.84e-07 1 / 0 8.86 - nan -
254 p.Tyr254Cys c.761A>G 3.42e-06 5 / 0 8.86 - nan - rs758020420
27 p.Pro27Ala c.79C>G 7.15e-07 1 / 0 8.54 0.072 BENIGN 0.53
27 p.Pro27Ser c.79C>T 1.43e-06 2 / 0 8.54 - nan -
27 p.Pro27Thr c.79C>A 3.57e-06 5 / 0 8.54 - nan - rs755233900
27 p.Gln27Lys c.79C>A 4.29e-06 6 / 0 8.54 - nan - rs1328682380
27 p.Gln27Arg c.80A>G 1.43e-06 2 / 0 8.54 - nan - rs1033909721
27 p.Ser27Ile c.80G>T 2.74e-06 4 / 0 8.54 - nan - rs780726314
27 p.Ser27Arg c.81C>A 6.84e-07 1 / 0 8.54 - nan -
77 p.Tyr77Cys c.230A>G 1.38e-06 2 / 0 8.23 0.976 PATHOGENIC 0.99 rs937906502
321 p.His321Tyr c.961C>T 6.84e-07 1 / 0 8.23 0.510 AMBIGUOUS 0.75
77 p.Tyr77Ser c.230A>C 2.55e-05 37 / 0 8.23 - nan - rs937906502
321 p.His321Asn c.961C>A 6.84e-07 1 / 0 8.23 - nan -
321 p.His321Pro c.962A>C 6.84e-07 1 / 0 8.23 - nan -
321 p.His321Gln c.963C>A 6.84e-07 1 / 0 8.23 - nan -
194 p.Trp194Cys c.582G>T 2.05e-06 3 / 0 7.49 0.998 PATHOGENIC 1.00 rs201858274
151 p.Tyr151Cys c.452A>G 1.37e-06 2 / 0 7.49 0.865 PATHOGENIC 1.00
277 p.Leu277Pro c.830T>C 6.16e-06 9 / 0 7.26 0.998 PATHOGENIC 0.94 rs763655185
277 p.Leu277Arg c.830T>G 6.84e-07 1 / 0 7.26 - nan -
388 p.Gln388His c.1164G>C 1.37e-06 2 / 0 6.63 0.120 BENIGN 0.81
387 p.His387Tyr c.1159C>T 6.86e-07 1 / 0 6.63 0.089 BENIGN 0.61
214 p.Gln214Arg c.641A>G 6.89e-07 1 / 0 6.03 0.073 BENIGN 0.42
390 p.Arg390Cys c.1168C>T 3.41e-04 492 / 2 5.94 0.497 AMBIGUOUS 0.57 rs79668187
391 p.Ser391Gly c.1171A>G 2.06e-06 3 / 0 5.94 0.140 BENIGN 0.49 rs1792197377
391 p.Ser391Thr c.1172G>C 6.88e-07 1 / 0 5.94 - nan - rs762824513
390 p.Leu390Pro c.1169T>C 6.85e-07 1 / 0 5.94 - nan -
391 p.Pro391Leu c.1172C>T 6.85e-07 1 / 0 5.94 - nan -
390 p.Glu390Lys c.1168G>A 1.77e-06 1 / 0 5.94 - nan - rs1326523267
390 p.Glu390Gly c.1169A>G 2.65e-05 15 / 0 5.94 - nan - rs758348717
391 p.Leu391Val c.1171T>G 1.77e-06 1 / 0 5.94 - nan -
391 p.Leu391Phe c.1173G>C 1.77e-06 1 / 0 5.94 - nan - rs1193804794
390 p.Pro390Ser c.1168C>T 1.77e-06 1 / 0 5.94 - nan -
390 p.Ile390Thr c.1169T>C 1.80e-05 23 / 0 5.94 - nan - rs780125425
391 p.Asn391Asp c.1171A>G 6.57e-06 1 / 0 5.94 - nan - rs1797127592
390 p.Pro390Leu c.1169C>T 6.84e-07 1 / 0 5.94 - nan - rs373281207
390 p.Pro390Arg c.1169C>G 9.58e-06 14 / 0 5.94 - nan - rs373281207
152 p.Asn152Asp c.454A>G 3.14e-04 453 / 3 5.74 0.991 PATHOGENIC 1.00 rs17174801
280 p.Ile280Val c.838A>G 6.84e-07 1 / 0 5.54 0.816 PATHOGENIC 1.00
227 p.Thr227Ala c.679A>G 1.71e-05 25 / 0 5.51 0.054 BENIGN 0.41 rs201874618
302 p.Val302Ile c.904G>A 3.15e-05 46 / 0 5.49 0.154 BENIGN 0.81 rs187512719
31 p.Pro31Leu c.92C>T 1.43e-06 2 / 0 5.49 0.117 BENIGN 0.53
31 p.Gln31Glu c.91C>G 2.86e-06 4 / 0 5.49 - nan -
31 p.Trp31Arg c.91T>A 1.37e-06 2 / 0 5.49 - nan - rs1423291779
302 p.Val302Ala c.905T>C 6.84e-07 1 / 0 5.49 - nan - rs202213165
274 p.Asp274Asn c.820G>A 2.83e-04 414 / 0 5.47 0.952 PATHOGENIC 0.99 rs17174829
278 p.Arg278Gln c.833G>A 1.09e-05 16 / 0 5.47 0.488 AMBIGUOUS 1.00 rs201847839
274 p.Asp274Gly c.821A>G 6.84e-07 1 / 0 5.47 - nan -
274 p.Asp274Glu c.822C>G 6.84e-07 1 / 0 5.47 - nan -
278 p.Arg278Leu c.833G>T 6.84e-07 1 / 0 5.47 - nan - rs201847839
339 p.Ala339Glu c.1016C>A 6.84e-07 1 / 0 5.36 0.999 PATHOGENIC 0.85
37 p.Met37Val c.109A>G 2.14e-06 3 / 0 5.27 0.067 BENIGN 0.42 rs1779528860
37 p.Met37Leu c.109A>T 7.15e-07 1 / 0 5.27 - nan -
37 p.Met37Leu c.109A>C 6.58e-06 1 / 0 5.27 - nan - rs1779528860
37 p.Met37Lys c.110T>A 7.15e-07 1 / 0 5.27 - nan - rs201734461
37 p.Met37Thr c.110T>C 4.14e-05 58 / 0 5.27 - nan - rs201734461
37 p.Met37Arg c.110T>G 1.43e-06 2 / 0 5.27 - nan -
37 p.Met37Ile c.111G>A 7.15e-07 1 / 0 5.27 - nan -
37 p.Met37Ile c.111G>C 2.86e-06 4 / 0 5.27 - nan - rs758842824
37 p.Ala37Thr c.109G>A 6.56e-06 1 / 0 5.27 - nan - rs571366137
37 p.Ala37Ser c.109G>T 1.43e-06 2 / 0 5.27 - nan - rs571366137
37 p.Ala37Val c.110C>T 1.43e-06 2 / 0 5.27 - nan -
37 p.Leu37Ser c.110T>C 6.84e-07 1 / 0 5.27 - nan -
37 p.Leu37Phe c.111A>C 6.57e-06 1 / 0 5.27 - nan - rs1779622178
235 p.Lys235Met c.704A>T 2.05e-06 3 / 0 5.06 0.931 PATHOGENIC 0.99 rs767947264
28 p.Pro28Ser c.82C>T 2.14e-06 3 / 0 5.06 0.069 BENIGN 0.47 rs1779523625
28 p.Pro28Ala c.82C>G 7.15e-07 1 / 0 5.06 - nan -
28 p.Pro28Leu c.83C>T 6.57e-06 1 / 0 5.06 - nan - rs929536552
28 p.Pro28Ala c.82C>G 1.37e-06 2 / 0 5.06 - nan - rs1207812281
235 p.Lys235Arg c.704A>G 2.05e-06 3 / 0 5.06 - nan - rs767947264
235 p.Lys235Asn c.705G>T 6.84e-07 1 / 0 5.06 - nan - rs750834795
341 p.Leu341Pro c.1022T>C 6.84e-07 1 / 0 4.94 0.998 PATHOGENIC 0.97
346 p.Lys346Glu c.1036A>G 4.10e-06 6 / 0 4.94 0.985 PATHOGENIC 1.00 rs771106503
32 p.Ala32Gly c.95C>G 6.57e-06 1 / 0 4.91 0.067 BENIGN 0.41 rs1049355494
32 p.Arg32Trp c.94C>T 7.14e-07 1 / 0 4.91 - nan -
32 p.Arg32Gln c.95G>A 7.14e-07 1 / 0 4.91 - nan -
32 p.Val32Leu c.94G>C 4.79e-06 7 / 0 4.91 - nan - rs1160067850
32 p.Val32Ala c.95T>C 1.37e-06 2 / 0 4.91 - nan -
164 p.Ser164Arg c.492T>G 6.84e-07 1 / 0 4.89 1.000 PATHOGENIC 1.00
29 p.Leu29Val c.85C>G 7.15e-07 1 / 0 4.78 0.098 BENIGN 0.58
29 p.Gly29Cys c.85G>T 1.37e-06 2 / 0 4.78 - nan - rs775097209
395 p.Leu395Pro c.1184T>C 6.84e-07 1 / 0 4.57 0.183 BENIGN 0.57
396 p.Ser396Tyr c.1187C>A 6.84e-07 1 / 0 4.57 0.145 BENIGN 0.58
395 p.Cys395Arg c.1183T>C 1.77e-06 1 / 0 4.57 - nan -
395 p.Cys395Tyr c.1184G>A 1.77e-06 1 / 0 4.57 - nan - rs1431508236
396 p.His396Asn c.1186C>A 3.36e-05 19 / 0 4.57 - nan - rs1373802399
395 p.Val395Ile c.1183G>A 1.97e-05 3 / 0 4.57 - nan - rs1414361004
395 p.Val395Ala c.1184T>C 6.57e-06 1 / 0 4.57 - nan - rs1795813900
396 p.Ala396Thr c.1186G>A 6.58e-06 1 / 0 4.57 - nan - rs1355692530
396 p.Ala396Val c.1187C>T 6.57e-06 1 / 0 4.57 - nan - rs1357614491
396 p.Asp396Tyr c.1186G>T 7.85e-06 4 / 0 4.57 - nan -
396 p.Ser396Leu c.1187C>T 7.47e-07 1 / 0 4.57 - nan -
395 p.Glu395Val c.1184A>T 6.84e-07 1 / 0 4.57 - nan -
396 p.Thr396Ala c.1186A>G 2.05e-06 3 / 0 4.57 - nan - rs201921259
396 p.Thr396Ser c.1187C>G 6.84e-07 1 / 0 4.57 - nan - rs200398791
396 p.Thr396Ile c.1187C>T 6.84e-06 10 / 0 4.57 - nan - rs200398791
395 p.Met395Thr c.1184T>C 1.37e-06 2 / 0 4.57 - nan -
395 p.Met395Ile c.1185G>T 6.84e-07 1 / 0 4.57 - nan -
396 p.Ala396Pro c.1186G>C 1.37e-06 2 / 0 4.57 - nan -
396 p.Ala396Thr c.1186G>A 6.84e-07 1 / 0 4.57 - nan -
351 p.Glu351Lys c.1051G>A 6.84e-07 1 / 0 4.46 0.710 PATHOGENIC 0.77 rs1259264846
347 p.Arg347Gly c.1039C>G 6.57e-06 1 / 0 4.46 0.592 PATHOGENIC 0.98 rs200512398
347 p.Arg347Gln c.1040G>A 1.04e-04 152 / 0 4.46 - nan - rs77013544
386 p.Asn386Asp c.1156A>G 1.37e-06 2 / 0 4.41 0.123 BENIGN 0.80 rs2128487104
385 p.Thr385Asn c.1154C>A 6.85e-07 1 / 0 4.41 0.087 BENIGN 0.62 rs1347406881
386 p.Asn386Lys c.1158T>G 6.86e-07 1 / 0 4.41 - nan - rs776230437
266 p.Met266Val c.796A>G 1.37e-06 2 / 0 4.22 0.258 BENIGN 0.77 rs1792047615
266 p.Met266Thr c.797T>C 6.84e-07 1 / 0 4.22 - nan -
190 p.Asn190Ser c.569A>G 1.37e-06 2 / 0 4.20 0.157 BENIGN 1.00
190 p.Asn190Lys c.570T>G 6.84e-07 1 / 0 4.20 - nan -
190 p.Asn190Lys c.570T>A 8.21e-05 120 / 0 4.20 - nan - rs34074916
335 p.Pro335Arg c.1004C>G 6.57e-06 1 / 0 4.19 1.000 PATHOGENIC 1.00 rs1412224107
340 p.Phe340Leu c.1020T>G 6.16e-06 9 / 0 4.19 0.981 PATHOGENIC 0.88 rs1792129299
73 p.Ile73Val c.217A>G 2.06e-06 3 / 0 4.09 0.172 BENIGN 0.98
73 p.Ile73Thr c.218T>C 6.88e-07 1 / 0 4.09 - nan - rs1779658672
180 p.Phe180Ser c.539T>C 1.85e-05 27 / 0 4.07 0.950 PATHOGENIC 0.98 rs769509205
169 p.Ile169Leu c.505A>C 6.84e-07 1 / 0 4.07 0.259 BENIGN 0.81
169 p.Ile169Val c.505A>G 6.57e-06 1 / 0 4.07 - nan - rs1791691188
169 p.Ile169Thr c.506T>C 2.05e-06 3 / 0 4.07 - nan -
169 p.Ile169Met c.507T>G 6.57e-06 1 / 0 4.07 - nan - rs1791692517
92 p.Met92Arg c.275T>G 1.40e-06 2 / 0 3.94 0.997 PATHOGENIC 0.99 rs747290680
92 p.Met92Lys c.275T>A 6.98e-07 1 / 0 3.94 - nan -
267 p.Leu267Pro c.800T>C 1.37e-06 2 / 0 3.93 0.947 PATHOGENIC 0.99 rs761129137
267 p.Leu267His c.800T>A 1.37e-06 0 / 1 3.93 - nan - rs761129137
150 p.Tyr150Asp c.448T>G 6.84e-07 1 / 0 3.93 0.988 PATHOGENIC 1.00
129 p.Asn129Tyr c.385A>T 6.84e-07 1 / 0 3.92 0.597 PATHOGENIC 0.57
349 p.Phe349Cys c.1046T>G 6.84e-07 1 / 0 3.90 0.964 PATHOGENIC 0.99
155 p.Thr155Ile c.464C>T 1.55e-04 226 / 0 3.87 0.946 PATHOGENIC 0.95 rs202022370
193 p.Asn193Asp c.577A>G 6.84e-07 1 / 0 3.87 0.730 PATHOGENIC 0.59 rs755039601
193 p.Asn193Ser c.578A>G 5.47e-06 8 / 0 3.87 - nan -
193 p.Asn193Lys c.579C>A 6.84e-07 1 / 0 3.87 - nan - rs1185829859
137 p.Phe137Leu c.409T>C 6.84e-07 1 / 0 3.85 0.996 PATHOGENIC 1.00 rs1210840287
125 p.Phe125Leu c.375C>G 5.47e-05 80 / 0 3.85 0.992 PATHOGENIC 1.00 rs77806090
137 p.Phe137Ser c.410T>C 2.05e-06 3 / 0 3.85 - nan - rs1276028790
137 p.Phe137Cys c.410T>G 6.84e-07 1 / 0 3.85 - nan -
158 p.Phe158Ser c.473T>C 6.84e-07 1 / 0 3.70 0.975 PATHOGENIC 0.99
223 p.Phe223Ser c.668T>C 3.42e-06 5 / 0 3.69 0.987 PATHOGENIC 0.97 rs770684457
320 p.Trp320Leu c.959G>T 6.84e-07 1 / 0 3.65 0.728 PATHOGENIC 0.67
301 p.Tyr301Cys c.902A>G 6.84e-07 1 / 0 3.65 0.555 AMBIGUOUS 0.86
197 p.Ser197Phe c.590C>T 4.10e-06 6 / 0 3.61 0.998 PATHOGENIC 0.95
197 p.Ser197Tyr c.590C>A 6.84e-07 1 / 0 3.61 - nan -
162 p.Thr162Pro c.484A>C 6.84e-07 1 / 0 3.59 0.953 PATHOGENIC 0.67
162 p.Thr162Ser c.485C>G 6.84e-07 1 / 0 3.59 - nan - rs1345025227
198 p.Ser198Leu c.593C>T 6.84e-07 1 / 0 3.56 0.812 PATHOGENIC 1.00
156 p.Ser156Asn c.467G>A 1.37e-06 2 / 0 3.53 0.994 PATHOGENIC 1.00
63 p.Gly63Ser c.187G>A 1.31e-05 2 / 0 3.46 0.076 BENIGN 0.54 rs777180052
63 p.Gly63Val c.188G>T 3.98e-05 58 / 0 3.46 - nan - rs9282817
63 p.Gly63Asp c.188G>A 5.49e-06 8 / 0 3.46 - nan - rs9282817
257 p.Met257Lys c.770T>A 6.57e-06 1 / 0 3.42 0.999 PATHOGENIC 1.00 rs1792035857
168 p.Tyr168His c.502T>C 6.84e-07 1 / 0 3.42 0.995 PATHOGENIC 1.00
168 p.Tyr168Cys c.503A>G 1.16e-05 17 / 0 3.42 - nan - rs199749405
257 p.Met257Ile c.771G>C 1.09e-05 16 / 0 3.42 - nan - rs201750403
257 p.Met257Ile c.771G>T 5.20e-05 76 / 0 3.42 - nan - rs201750403
257 p.Met257Ile c.771G>A 1.37e-06 2 / 0 3.42 - nan - rs201750403
338 p.Tyr338Cys c.1013A>G 1.37e-05 20 / 0 3.36 0.995 PATHOGENIC 1.00 rs201429844
109 p.Ile109Phe c.325A>T 2.05e-06 3 / 0 3.36 0.992 PATHOGENIC 1.00
181 p.Arg181Cys c.541C>T 1.83e-03 2659 / 6 3.36 0.987 PATHOGENIC 0.99 rs79910351
181 p.Arg181His c.542G>A 2.80e-05 41 / 0 3.36 - nan - rs748807412
384 p.Arg384Gly c.1150A>G 2.74e-06 4 / 0 3.35 0.176 BENIGN 0.69 rs1210793358
383 p.Asp383Asn c.1147G>A 1.37e-06 2 / 0 3.35 0.111 BENIGN 0.73 rs746718852
383 p.Asp383Gly c.1148A>G 6.85e-07 1 / 0 3.35 - nan -
99 p.Thr99Ala c.295A>G 4.12e-06 6 / 0 3.26 0.564 AMBIGUOUS 1.00 rs774733136
99 p.Thr99Asn c.296C>A 2.06e-06 3 / 0 3.26 - nan -
204 p.Val204Ile c.610G>A 2.74e-06 4 / 0 3.24 0.218 BENIGN 0.66
222 p.Thr222Ile c.665C>T 6.84e-07 1 / 0 3.14 0.159 BENIGN 0.44 rs777753483
253 p.Cys253Ser c.757T>A 6.84e-07 1 / 0 3.14 0.922 PATHOGENIC 1.00
253 p.Cys253Ser c.758G>C 1.37e-06 2 / 0 3.14 - nan - rs752365239
253 p.Cys253Tyr c.758G>A 1.37e-06 2 / 0 3.14 - nan - rs752365239
305 p.Lys305Arg c.914A>G 1.37e-06 2 / 0 3.10 0.111 BENIGN 0.59 rs200318741
50 p.Ala50Pro c.148G>C 1.40e-06 2 / 0 3.02 0.114 BENIGN 0.43
51 p.Thr51Ala c.151A>G 6.57e-06 1 / 0 3.02 0.085 BENIGN 0.36 rs535843430
50 p.Ala50Val c.149C>T 1.40e-06 2 / 0 3.02 - nan - rs9282815
50 p.Ala50Asp c.149C>A 7.67e-04 1051 / 23 3.02 - nan - rs9282815
51 p.Thr51Ile c.152C>T 2.09e-06 3 / 0 3.02 - nan - rs370868117
50 p.Thr50Ala c.148A>G 6.84e-07 1 / 0 3.02 - nan -
51 p.Asp51Tyr c.151G>T 6.84e-07 1 / 0 3.02 - nan -
51 p.Asp51Asn c.151G>A 7.53e-06 11 / 0 3.02 - nan - rs1042753

Complete RRCS results

Top 1000 contact pairs by |ΔRRCS|. Significance threshold: |ΔRRCS| ≥ 2.52, computed as max(mean(|Δ|) + σ, 0.2). Highlighted rows indicate significant changes.

Res1 AA1 Res2 AA2 Active RRCS Inactive RRCS ΔRRCS |ΔRRCS|
98 TYR 352 PHE 13.902 0.000 13.902 13.902
34 LEU 312 GLU 9.811 0.000 9.811 9.811
36 HIS 62 THR 0.000 9.025 -9.025 9.025
167 ARG 281 THR 0.000 8.873 -8.873 8.873
254 TYR 285 LEU 0.000 8.863 -8.863 8.863
27 SER 231 GLU 8.536 0.000 8.536 8.536
77 TYR 321 HIS 8.227 0.000 8.227 8.227
151 TYR 194 TRP 9.929 2.441 7.488 7.488
167 ARG 277 LEU 0.000 7.255 -7.255 7.255
387 HIS 388 GLN 0.000 6.633 -6.633 6.633
101 MET 106 ASN 0.160 6.295 -6.135 6.135
36 HIS 214 GLN 6.033 0.000 6.033 6.033
390 GLU 391 ASN 0.000 5.935 -5.935 5.935
118 LEU 152 ASN 5.736 0.000 5.736 5.736
167 ARG 280 ILE 0.000 5.543 -5.543 5.543
27 SER 227 THR 0.023 5.534 -5.510 5.510
31 TRP 302 VAL 0.000 5.491 -5.491 5.491
274 ASP 278 ARG 1.415 6.884 -5.468 5.468
167 ARG 254 TYR 5.468 0.000 5.468 5.468
339 ALA 345 PHE 5.426 0.069 5.356 5.356
37 LEU 214 GLN 5.266 0.000 5.266 5.266
28 PRO 235 LYS 5.062 0.000 5.062 5.062
341 LEU 346 LYS 4.935 0.000 4.935 4.935
32 VAL 218 ASP 4.914 0.000 4.914 4.914
164 SER 254 TYR 6.540 1.647 4.893 4.893
29 GLY 221 LEU 0.416 5.201 -4.785 4.785
28 PRO 34 LEU 0.000 4.630 -4.630 4.630
395 GLU 396 THR 0.000 4.572 -4.572 4.572
28 PRO 231 GLU 7.315 2.765 4.550 4.550
347 ARG 351 GLU 0.000 4.465 -4.465 4.465
123 LEU 328 TYR 7.643 3.230 4.413 4.413
385 THR 386 ASN 0.044 4.456 -4.411 4.411
101 MET 345 PHE 0.000 4.322 -4.322 4.322
266 MET 273 LYS 4.219 0.000 4.219 4.219
108 TYR 190 ASN 6.913 2.711 4.202 4.202
335 PRO 340 PHE 4.193 0.000 4.193 4.193
73 ILE 130 TYR 4.644 0.555 4.089 4.089
169 ILE 180 PHE 4.074 0.000 4.074 4.074
92 MET 110 PHE 2.850 6.788 -3.939 3.939
267 LEU 274 ASP 1.691 5.623 -3.932 3.932
31 TRP 150 TYR 0.000 3.927 -3.927 3.927
31 TRP 129 ASN 3.920 0.000 3.920 3.920
90 LEU 349 PHE 0.000 3.897 -3.897 3.897
32 VAL 130 TYR 0.000 3.882 -3.882 3.882
155 THR 193 ASN 0.000 3.874 -3.874 3.874
125 PHE 137 PHE 2.916 6.764 -3.848 3.848
336 VAL 341 LEU 3.750 0.000 3.750 3.750
158 PHE 193 ASN 2.251 5.953 -3.702 3.702
223 PHE 231 GLU 8.093 4.405 3.689 3.689
301 TYR 320 TRP 4.223 7.870 -3.647 3.647
151 TYR 197 SER 7.159 3.554 3.606 3.606
162 THR 193 ASN 3.593 0.000 3.593 3.593
151 TYR 198 SER 3.712 7.268 -3.556 3.556
116 ASP 156 SER 3.633 0.105 3.528 3.528
267 LEU 273 LYS 3.516 0.000 3.516 3.516
36 HIS 63 GLY 0.000 3.464 -3.464 3.464
168 TYR 257 MET 0.148 3.572 -3.424 3.424
77 TYR 123 LEU 1.042 4.460 -3.419 3.419
109 ILE 338 TYR 1.223 4.585 -3.362 3.362
166 ASP 181 ARG 7.733 11.093 -3.360 3.360
383 ASP 384 ARG 0.000 3.345 -3.345 3.345
90 LEU 352 PHE 0.000 3.318 -3.318 3.318
339 ALA 346 LYS 0.000 3.316 -3.316 3.316
99 THR 106 ASN 3.263 0.000 3.263 3.263
150 TYR 204 VAL 1.285 4.524 -3.239 3.239
340 PHE 346 LYS 3.203 0.000 3.203 3.203
211 LYS 222 THR 3.144 0.000 3.144 3.144
168 TYR 253 CYS 4.409 1.268 3.141 3.141
167 ARG 338 TYR 3.121 0.000 3.121 3.121
34 LEU 305 LYS 0.000 3.102 -3.102 3.102
50 THR 51 ASP 3.833 0.817 3.016 3.016
151 TYR 201 GLY 0.604 3.602 -2.998 2.998
160 LEU 338 TYR 2.991 0.000 2.991 2.991
35 SER 63 GLY 1.661 4.646 -2.984 2.984
154 PHE 200 ILE 2.461 5.428 -2.967 2.967
272 GLU 276 ASN 0.556 3.512 -2.956 2.956
224 SER 230 TRP 4.762 7.710 -2.948 2.948
322 PHE 326 LEU 2.933 0.000 2.933 2.933
180 PHE 185 ASN 6.926 4.008 2.917 2.917
291 PHE 330 ASN 1.382 4.189 -2.807 2.807
298 ILE 323 CYS 4.584 1.782 2.802 2.802
157 ILE 295 TRP 2.798 0.000 2.798 2.798
77 TYR 324 ILE 3.817 1.070 2.747 2.747
159 THR 193 ASN 0.519 3.244 -2.725 2.725
254 TYR 257 MET 1.043 3.757 -2.715 2.715
295 TRP 327 GLY 1.904 4.611 -2.706 2.706
185 ASN 189 ILE 2.694 0.000 2.694 2.694
182 THR 185 ASN 1.145 3.833 -2.688 2.688
250 ILE 291 PHE 2.662 0.000 2.662 2.662
96 VAL 102 LYS 0.000 2.649 -2.649 2.649
98 TYR 351 GLU 0.000 2.647 -2.647 2.647
122 THR 149 ASP 3.310 0.730 2.580 2.580
111 ASN 159 THR 0.242 2.818 -2.575 2.575
343 GLU 346 LYS 3.890 1.367 2.523 2.523
33 ASN 35 SER 2.486 0.000 2.486 2.486
272 GLU 275 ARG 6.393 3.940 2.452 2.452
95 ILE 100 LYS 2.412 0.000 2.412 2.412
155 THR 194 TRP 6.366 3.966 2.400 2.400
30 SER 213 ARG 2.397 0.000 2.397 2.397
135 TRP 219 CYS 6.068 3.671 2.397 2.397
171 VAL 260 ARG 2.673 0.286 2.388 2.388
74 MET 127 SER 3.940 1.553 2.386 2.386
268 SER 273 LYS 0.207 2.581 -2.373 2.373
160 LEU 291 PHE 1.069 3.442 -2.373 2.373
107 ILE 186 ALA 0.199 2.556 -2.358 2.358
295 TRP 299 HIS 3.143 0.786 2.356 2.356
209 THR 222 THR 4.529 2.174 2.355 2.355
153 MET 295 TRP 2.512 0.160 2.352 2.352
93 TYR 97 ARG 0.479 2.808 -2.328 2.328
301 TYR 319 SER 1.770 4.088 -2.318 2.318
339 ALA 349 PHE 0.000 2.303 -2.303 2.303
338 TYR 345 PHE 0.000 2.285 -2.285 2.285
97 ARG 98 TYR 3.078 0.807 2.271 2.271
129 ASN 134 THR 3.616 5.886 -2.270 2.270
147 SER 151 TYR 0.000 2.269 -2.269 2.269
166 ASP 180 PHE 2.264 0.000 2.264 2.264
291 PHE 295 TRP 4.224 6.474 -2.250 2.250
151 TYR 202 LEU 0.000 2.241 -2.241 2.241
154 PHE 242 ALA 1.562 3.769 -2.207 2.207
155 THR 197 SER 5.535 3.335 2.201 2.201
88 ASN 117 ALA 3.679 1.489 2.190 2.190
243 PHE 296 THR 5.866 3.683 2.183 2.183
207 MET 222 THR 9.666 7.483 2.183 2.183
295 TRP 330 ASN 3.989 1.816 2.173 2.173
94 VAL 348 CYS 0.000 2.168 -2.168 2.168
150 TYR 234 LEU 0.000 2.151 -2.151 2.151
31 TRP 219 CYS 2.140 0.000 2.140 2.140
108 TYR 189 ILE 1.030 3.154 -2.124 2.124
168 TYR 173 HIS 4.145 2.025 2.120 2.120
163 MET 338 TYR 2.104 0.000 2.104 2.104
136 PRO 137 PHE 2.431 4.525 -2.095 2.095
135 TRP 137 PHE 7.530 5.442 2.088 2.088
170 ALA 181 ARG 2.479 4.543 -2.064 2.064
30 SER 219 CYS 0.000 2.053 -2.053 2.053
125 PHE 145 VAL 2.021 0.000 2.021 2.021
163 MET 284 VAL 0.000 1.998 -1.998 1.998
26 PRO 37 LEU 0.000 1.982 -1.982 1.982
116 ASP 334 ASN 5.085 3.118 1.967 1.967
212 TYR 217 ILE 0.150 2.115 -1.965 1.965
160 LEU 334 ASN 1.960 0.000 1.960 1.960
77 TYR 325 ALA 0.192 2.151 -1.959 1.959
380 ASN 381 THR 2.323 0.365 1.958 1.958
340 PHE 349 PHE 1.938 0.000 1.938 1.938
107 ILE 190 ASN 1.536 3.456 -1.919 1.919
391 ASN 392 LEU 0.000 1.916 -1.916 1.916
330 ASN 334 ASN 2.390 0.476 1.914 1.914
239 PHE 303 ILE 1.680 3.546 -1.867 1.867
279 ARG 343 GLU 3.258 1.392 1.866 1.866
88 ASN 116 ASP 5.734 3.892 1.842 1.842
153 MET 299 HIS 0.000 1.831 -1.831 1.831
384 ARG 385 THR 0.000 1.819 -1.819 1.819
33 ASN 218 ASP 0.000 1.811 -1.811 1.811
151 TYR 152 ASN 1.804 0.000 1.804 1.804
2 ASP 3 SER 0.223 2.026 -1.802 1.802
119 ALA 328 TYR 1.895 0.105 1.790 1.790
95 ILE 99 THR 1.790 0.000 1.790 1.790
161 CYS 246 PRO 2.162 0.376 1.786 1.786
356 THR 358 SER 1.756 0.000 1.756 1.756
287 VAL 338 TYR 2.599 0.871 1.728 1.728
180 PHE 189 ILE 1.725 0.000 1.725 1.725
157 ILE 291 PHE 0.777 2.471 -1.694 1.694
170 ALA 277 LEU 0.000 1.685 -1.685 1.685
101 MET 107 ILE 1.675 0.000 1.675 1.675
158 PHE 196 LEU 0.698 2.369 -1.671 1.671
242 ALA 299 HIS 1.913 0.244 1.668 1.668
167 ARG 284 VAL 0.000 1.658 -1.658 1.658
94 VAL 101 MET 0.000 1.640 -1.640 1.640
239 PHE 299 HIS 2.840 1.204 1.636 1.636
95 ILE 102 LYS 0.000 1.615 -1.615 1.615
77 TYR 328 TYR 0.000 1.613 -1.613 1.613
107 ILE 187 LYS 0.771 2.382 -1.611 1.611
247 VAL 291 PHE 1.583 0.000 1.583 1.583
225 HIS 226 PRO 1.568 0.000 1.568 1.568
31 TRP 320 TRP 0.000 1.552 -1.552 1.552
112 LEU 160 LEU 1.978 0.429 1.549 1.549
152 ASN 156 SER 0.000 1.546 -1.546 1.546
65 PRO 130 TYR 1.655 0.119 1.536 1.536
101 MET 344 ASN 0.000 1.523 -1.523 1.523
101 MET 110 PHE 1.523 0.000 1.523 1.523
111 ASN 190 ASN 5.724 7.247 -1.522 1.522
153 MET 238 VAL 0.621 2.125 -1.503 1.503
152 ASN 194 TRP 1.501 0.000 1.501 1.501
156 SER 291 PHE 0.000 1.496 -1.496 1.496
91 VAL 339 ALA 1.488 0.000 1.488 1.488
286 VAL 341 LEU 0.000 1.482 -1.482 1.482
112 LEU 116 ASP 2.137 0.662 1.474 1.474
342 ASP 345 PHE 0.919 2.373 -1.453 1.453
243 PHE 295 TRP 1.453 0.000 1.453 1.453
246 PRO 291 PHE 1.448 0.000 1.448 1.448
73 ILE 77 TYR 1.280 2.727 -1.446 1.446
258 ILE 284 VAL 1.439 0.000 1.439 1.439
69 THR 314 THR 1.434 0.000 1.434 1.434
160 LEU 288 VAL 0.000 1.398 -1.398 1.398
108 TYR 163 MET 1.787 3.183 -1.397 1.397
125 PHE 141 LEU 1.273 2.664 -1.392 1.392
77 TYR 127 SER 1.968 0.577 1.391 1.391
129 ASN 135 TRP 3.571 4.950 -1.378 1.378
108 TYR 159 THR 0.901 2.275 -1.374 1.374
98 TYR 348 CYS 0.000 1.365 -1.365 1.365
254 TYR 288 VAL 1.350 0.000 1.350 1.350
87 GLY 335 PRO 2.905 4.254 -1.349 1.349
261 LEU 277 LEU 1.347 0.000 1.347 1.347
30 SER 218 ASP 1.345 0.000 1.345 1.345
148 ILE 152 ASN 1.340 0.000 1.340 1.340
95 ILE 106 ASN 0.740 2.065 -1.325 1.325
116 ASP 331 SER 11.299 12.616 -1.317 1.317
283 MET 342 ASP 0.000 1.303 -1.303 1.303
283 MET 341 LEU 0.689 1.964 -1.274 1.274
94 VAL 99 THR 1.271 0.000 1.271 1.271
122 THR 126 GLN 0.462 1.732 -1.270 1.270
279 ARG 341 LEU 0.000 1.265 -1.265 1.265
49 ARG 50 THR 0.000 1.255 -1.255 1.255
216 SER 218 ASP 1.904 0.650 1.254 1.254
276 ASN 279 ARG 0.000 1.249 -1.249 1.249
91 VAL 338 TYR 0.000 1.245 -1.245 1.245
398 PRO 399 LEU 0.000 1.240 -1.240 1.240
279 ARG 346 LYS 1.236 0.000 1.236 1.236
143 LYS 205 MET 5.031 6.265 -1.234 1.234
91 VAL 340 PHE 1.233 0.000 1.233 1.233
29 GLY 220 THR 4.201 2.973 1.229 1.229
112 LEU 159 THR 1.801 0.578 1.224 1.224
171 VAL 267 LEU 0.000 1.206 -1.206 1.206
243 PHE 247 VAL 1.598 0.393 1.204 1.204
126 GLN 328 TYR 4.796 6.000 -1.204 1.204
32 VAL 133 GLY 1.201 0.000 1.201 1.201
261 LEU 278 ARG 0.000 1.199 -1.199 1.199
254 TYR 281 THR 0.000 1.190 -1.190 1.190
161 CYS 250 ILE 0.644 1.832 -1.188 1.188
116 ASP 152 ASN 0.000 1.188 -1.188 1.188
135 TRP 217 ILE 6.990 5.805 1.185 1.185
229 TYR 230 TRP 3.936 5.104 -1.168 1.168
171 VAL 277 LEU 0.000 1.142 -1.142 1.142
198 SER 202 LEU 1.856 0.716 1.140 1.140
381 THR 382 VAL 1.367 0.228 1.138 1.138
240 ILE 245 MET 4.156 3.018 1.137 1.137
161 CYS 249 ILE 0.905 2.038 -1.134 1.134
154 PHE 241 PHE 1.615 0.487 1.129 1.129
382 VAL 383 ASP 2.116 0.992 1.125 1.125
164 SER 253 CYS 2.597 1.473 1.123 1.123
151 TYR 155 THR 1.244 0.125 1.119 1.119
134 THR 216 SER 2.985 1.881 1.104 1.104
132 MET 136 PRO 1.495 0.392 1.103 1.103
207 MET 223 PHE 1.309 0.215 1.095 1.095
301 TYR 316 GLN 5.753 6.820 -1.067 1.067
266 MET 271 LYS 0.000 1.066 -1.066 1.066
243 PHE 299 HIS 5.770 6.826 -1.056 1.056
91 VAL 349 PHE 0.000 1.054 -1.054 1.054
167 ARG 181 ARG 0.026 1.070 -1.044 1.044
150 TYR 221 LEU 0.589 1.630 -1.042 1.042
30 SER 220 THR 2.927 3.967 -1.040 1.040
119 ALA 148 ILE 0.000 1.040 -1.040 1.040
105 THR 280 ILE 0.000 1.040 -1.040 1.040
258 ILE 281 THR 1.038 0.000 1.038 1.038
375 HIS 376 PRO 1.227 0.192 1.035 1.035
171 VAL 261 LEU 1.453 0.423 1.030 1.030
122 THR 328 TYR 1.024 0.000 1.024 1.024
260 ARG 263 SER 1.348 0.330 1.018 1.018
267 LEU 278 ARG 0.000 1.010 -1.010 1.010
90 LEU 340 PHE 1.003 0.000 1.003 1.003
76 LEU 325 ALA 1.664 0.661 1.003 1.003
111 ASN 193 ASN 0.000 1.001 -1.001 1.001
160 LEU 250 ILE 0.324 1.317 -0.993 0.993
10 ALA 11 SER 0.000 0.980 -0.980 0.980
37 LEU 213 ARG 0.000 0.978 -0.978 0.978
356 THR 359 ASN 0.163 1.140 -0.977 0.977
337 LEU 338 TYR 0.968 0.000 0.968 0.968
95 ILE 110 PHE 3.262 2.302 0.960 0.960
171 VAL 257 MET 2.431 1.478 0.953 0.953
396 THR 397 ALA 0.000 0.953 -0.953 0.953
260 ARG 264 VAL 1.015 1.966 -0.951 0.951
135 TRP 141 LEU 1.003 1.947 -0.945 0.945
263 SER 264 VAL 0.000 0.931 -0.931 0.931
239 PHE 243 PHE 1.909 0.984 0.925 0.925
204 VAL 221 LEU 1.279 2.198 -0.920 0.920
126 GLN 145 VAL 0.000 0.913 -0.913 0.913
223 PHE 227 THR 0.592 1.479 -0.887 0.887
218 ASP 220 THR 0.047 0.933 -0.886 0.886
157 ILE 158 PHE 0.000 0.878 -0.878 0.878
139 THR 209 THR 0.316 1.187 -0.871 0.871
106 ASN 345 PHE 0.780 1.647 -0.867 0.867
152 ASN 295 TRP 0.000 0.866 -0.866 0.866
115 ALA 194 TRP 0.866 0.000 0.866 0.866
98 TYR 101 MET 0.000 0.863 -0.863 0.863
74 MET 131 LEU 1.263 0.404 0.859 0.859
317 THR 321 HIS 0.710 1.566 -0.856 0.856
235 LYS 302 VAL 0.320 1.175 -0.855 0.855
245 MET 249 ILE 0.000 0.855 -0.855 0.855
115 ALA 156 SER 1.385 0.532 0.853 0.853
88 ASN 113 ALA 5.406 6.257 -0.851 0.851
386 ASN 387 HIS 0.000 0.849 -0.849 0.849
115 ALA 152 ASN 4.267 3.422 0.846 0.846
157 ILE 246 PRO 1.612 2.456 -0.843 0.843
80 VAL 329 THR 1.058 1.897 -0.839 0.839
109 ILE 283 MET 0.000 0.838 -0.838 0.838
91 VAL 345 PHE 0.202 1.031 -0.830 0.830
83 VAL 332 CYS 0.000 0.816 -0.816 0.816
296 THR 300 ILE 1.220 0.411 0.808 0.808
85 LEU 120 THR 2.860 3.665 -0.804 0.804
94 VAL 349 PHE 1.599 0.796 0.804 0.804
193 ASN 197 SER 0.000 0.799 -0.799 0.799
37 LEU 38 ASP 0.000 0.795 -0.795 0.795
254 TYR 284 VAL 3.609 2.821 0.788 0.788
118 LEU 148 ILE 1.284 2.071 -0.788 0.788
345 PHE 349 PHE 0.442 1.226 -0.784 0.784
95 ILE 109 ILE 1.345 0.564 0.781 0.781
114 LEU 194 TRP 1.494 0.723 0.771 0.771
147 SER 204 VAL 0.935 0.165 0.770 0.770
36 HIS 213 ARG 0.000 0.763 -0.763 0.763
107 ILE 111 ASN 0.761 0.000 0.761 0.761
165 VAL 253 CYS 0.614 1.375 -0.760 0.760
125 PHE 135 TRP 2.626 1.867 0.759 0.759
105 THR 166 ASP 0.454 1.213 -0.758 0.758
40 ASN 41 LEU 0.522 1.277 -0.755 0.755
394 ALA 395 GLU 0.000 0.754 -0.754 0.754
310 ILE 311 PRO 0.597 1.350 -0.753 0.753
94 VAL 345 PHE 1.267 0.514 0.753 0.753
287 VAL 334 ASN 0.000 0.750 -0.750 0.750
213 ARG 218 ASP 5.878 5.129 0.749 0.749
36 HIS 312 GLU 0.000 0.747 -0.747 0.747
76 LEU 322 PHE 0.740 0.000 0.740 0.740
158 PHE 246 PRO 0.000 0.735 -0.735 0.735
342 ASP 344 ASN 3.908 3.173 0.735 0.735
350 ARG 354 ILE 0.491 1.225 -0.734 0.734
379 ALA 380 ASN 0.730 0.000 0.730 0.730
254 TYR 287 VAL 0.727 0.000 0.727 0.727
156 SER 334 ASN 0.722 0.000 0.722 0.722
112 LEU 156 SER 2.125 2.844 -0.718 0.718
102 LYS 183 PRO 1.005 1.722 -0.717 0.717
65 PRO 70 ALA 0.754 0.044 0.711 0.711
269 GLY 274 ASP 0.708 0.000 0.708 0.708
261 LEU 267 LEU 2.517 1.817 0.700 0.700
119 ALA 152 ASN 1.854 2.554 -0.700 0.700
138 GLY 210 THR 0.657 1.355 -0.698 0.698
176 LYS 180 PHE 0.000 0.694 -0.694 0.694
93 TYR 352 PHE 0.000 0.693 -0.693 0.693
211 LYS 218 ASP 6.741 6.050 0.691 0.691
158 PHE 241 PHE 0.934 1.621 -0.687 0.687
298 ILE 299 HIS 0.687 0.000 0.687 0.687
268 SER 274 ASP 1.348 0.663 0.686 0.686
160 LEU 287 VAL 0.000 0.682 -0.682 0.682
335 PRO 349 PHE 0.000 0.677 -0.677 0.677
301 TYR 310 ILE 1.115 0.439 0.676 0.676
236 ILE 240 ILE 0.882 0.208 0.674 0.674
154 PHE 238 VAL 1.511 0.841 0.670 0.670
105 THR 181 ARG 1.398 0.732 0.665 0.665
399 LEU 400 PRO 0.868 1.527 -0.659 0.659
254 TYR 338 TYR 0.655 0.000 0.655 0.655
226 PRO 228 TRP 1.718 2.372 -0.654 0.654
231 GLU 235 LYS 5.339 4.686 0.653 0.653
133 GLY 216 SER 1.734 1.081 0.652 0.652
111 ASN 194 TRP 3.674 4.320 -0.645 0.645
153 MET 242 ALA 0.310 0.944 -0.635 0.635
6 ALA 7 PRO 0.310 0.940 -0.630 0.630
130 TYR 317 THR 0.627 0.000 0.627 0.627
290 VAL 330 ASN 1.341 1.962 -0.621 0.621
158 PHE 197 SER 1.656 1.037 0.619 0.619
73 ILE 321 HIS 2.753 2.135 0.618 0.618
81 CYS 120 THR 2.780 2.164 0.616 0.616
329 THR 333 LEU 0.911 0.298 0.613 0.613
85 LEU 117 ALA 0.869 1.481 -0.612 0.612
88 ASN 331 SER 1.931 2.540 -0.608 0.608
264 VAL 266 MET 0.608 0.000 0.608 0.608
169 ILE 177 ALA 2.245 1.639 0.605 0.605
109 ILE 339 ALA 0.604 0.000 0.604 0.604
112 LEU 334 ASN 2.613 2.010 0.603 0.603
122 THR 145 VAL 1.413 2.012 -0.599 0.599
239 PHE 244 ILE 6.034 6.631 -0.597 0.597
174 PRO 267 LEU 0.000 0.594 -0.594 0.594
114 LEU 118 LEU 0.818 0.226 0.592 0.592
225 HIS 227 THR 0.000 0.591 -0.591 0.591
67 MET 71 ILE 0.591 0.000 0.591 0.591
80 VAL 325 ALA 0.584 0.000 0.584 0.584
160 LEU 330 ASN 0.582 0.000 0.582 0.582
238 VAL 299 HIS 0.845 0.266 0.580 0.580
170 ALA 177 ALA 1.136 0.562 0.574 0.574
153 MET 157 ILE 0.572 0.000 0.572 0.572
142 CYS 209 THR 1.192 1.763 -0.571 0.571
240 ILE 241 PHE 0.173 0.739 -0.566 0.566
277 LEU 281 THR 0.560 0.000 0.560 0.560
106 ASN 109 ILE 0.066 0.621 -0.556 0.556
257 MET 261 LEU 0.570 0.015 0.555 0.555
135 TRP 210 THR 0.664 1.217 -0.553 0.553
104 ALA 183 PRO 0.968 0.415 0.553 0.553
92 MET 114 LEU 1.836 2.389 -0.553 0.553
298 ILE 320 TRP 0.000 0.553 -0.553 0.553
122 THR 148 ILE 1.140 1.691 -0.551 0.551
261 LEU 280 ILE 0.546 0.000 0.546 0.546
95 ILE 101 MET 1.419 0.877 0.542 0.542
349 PHE 353 CYS 0.540 0.000 0.540 0.540
167 ARG 257 MET 1.502 2.040 -0.538 0.538
310 ILE 316 GLN 1.464 0.932 0.532 0.532
134 THR 217 ILE 6.207 6.729 -0.522 0.522
245 MET 248 LEU 0.521 0.000 0.521 0.521
120 THR 331 SER 0.139 0.658 -0.520 0.520
397 ALA 398 PRO 0.458 0.974 -0.516 0.516
213 ARG 214 GLN 0.516 0.000 0.516 0.516
33 ASN 63 GLY 0.512 0.000 0.512 0.512
315 PHE 319 SER 0.000 0.509 -0.509 0.509
239 PHE 300 ILE 0.000 0.508 -0.508 0.508
108 TYR 186 ALA 4.618 5.124 -0.506 0.506
142 CYS 219 CYS 6.652 7.157 -0.506 0.506
143 LYS 206 PHE 2.312 2.812 -0.500 0.500
270 SER 273 LYS 0.725 1.225 -0.500 0.500
88 ASN 120 THR 0.496 0.000 0.496 0.496
101 MET 348 CYS 0.000 0.495 -0.495 0.495
351 GLU 352 PHE 0.494 0.000 0.494 0.494
225 HIS 230 TRP 0.754 0.269 0.485 0.485
154 PHE 158 PHE 2.397 1.913 0.484 0.484
211 LYS 216 SER 0.886 0.404 0.482 0.482
244 ILE 245 MET 0.477 0.000 0.477 0.477
213 ARG 216 SER 0.000 0.475 -0.475 0.475
164 SER 249 ILE 0.474 0.000 0.474 0.474
103 THR 106 ASN 4.443 3.969 0.474 0.474
226 PRO 230 TRP 0.473 0.000 0.473 0.473
104 ALA 182 THR 1.001 0.528 0.473 0.473
11 SER 12 ASN 0.000 0.472 -0.472 0.472
162 THR 189 ILE 0.980 1.451 -0.472 0.472
164 SER 288 VAL 0.000 0.464 -0.464 0.464
209 THR 220 THR 6.144 6.607 -0.462 0.462
95 ILE 345 PHE 2.151 1.690 0.461 0.461
227 THR 231 GLU 0.136 0.586 -0.451 0.451
202 LEU 205 MET 0.000 0.445 -0.445 0.445
112 LEU 287 VAL 0.000 0.442 -0.442 0.442
283 MET 338 TYR 0.000 0.441 -0.441 0.441
207 MET 221 LEU 2.330 2.771 -0.441 0.441
172 CYS 256 LEU 0.756 0.316 0.440 0.440
80 VAL 120 THR 0.273 0.706 -0.433 0.433
84 GLY 332 CYS 2.842 2.411 0.432 0.432
266 MET 274 ASP 0.000 0.430 -0.430 0.430
143 LYS 209 THR 0.423 0.000 0.423 0.423
262 LYS 277 LEU 0.422 0.000 0.422 0.422
112 LEU 163 MET 0.419 0.000 0.419 0.419
179 ASP 180 PHE 0.000 0.419 -0.419 0.419
86 PHE 90 LEU 0.898 0.483 0.416 0.416
177 ALA 181 ARG 0.539 0.953 -0.414 0.414
287 VAL 337 LEU 0.226 0.639 -0.413 0.413
189 ILE 193 ASN 0.412 0.000 0.412 0.412
334 ASN 338 TYR 1.705 2.117 -0.412 0.412
244 ILE 248 LEU 0.274 0.685 -0.411 0.411
251 THR 288 VAL 0.407 0.000 0.407 0.407
118 LEU 194 TRP 0.194 0.598 -0.404 0.404
334 ASN 337 LEU 0.000 0.402 -0.402 0.402
190 ASN 193 ASN 0.400 0.000 0.400 0.400
73 ILE 318 VAL 0.399 0.000 0.399 0.399
281 THR 285 LEU 0.395 0.000 0.395 0.395
77 TYR 126 GLN 0.443 0.835 -0.392 0.392
81 CYS 123 LEU 1.573 1.181 0.392 0.392
152 ASN 331 SER 0.000 0.391 -0.391 0.391
210 THR 217 ILE 1.212 0.821 0.391 0.391
146 ILE 204 VAL 1.751 1.362 0.389 0.389
171 VAL 281 THR 0.000 0.388 -0.388 0.388
164 SER 284 VAL 0.000 0.388 -0.388 0.388
126 GLN 324 ILE 0.387 0.000 0.387 0.387
141 LEU 145 VAL 0.687 0.302 0.385 0.385
19 TYR 20 SER 0.384 0.000 0.384 0.384
229 TYR 233 LEU 0.643 0.260 0.383 0.383
290 VAL 337 LEU 1.554 1.175 0.379 0.379
36 HIS 61 PRO 0.000 0.379 -0.379 0.379
128 VAL 137 PHE 2.225 1.847 0.378 0.378
85 LEU 121 SER 0.586 0.959 -0.373 0.373
294 CYS 327 GLY 1.272 1.642 -0.370 0.370
265 ARG 278 ARG 0.000 0.365 -0.365 0.365
120 THR 123 LEU 0.088 0.450 -0.362 0.362
150 TYR 153 MET 0.000 0.359 -0.359 0.359
313 THR 316 GLN 1.131 0.773 0.359 0.359
164 SER 250 ILE 3.090 2.732 0.358 0.358
334 ASN 339 ALA 0.357 0.000 0.357 0.357
242 ALA 291 PHE 0.357 0.000 0.357 0.357
304 ILE 310 ILE 0.000 0.355 -0.355 0.355
221 LEU 223 PHE 1.634 1.280 0.354 0.354
329 THR 332 CYS 0.000 0.354 -0.354 0.354
94 VAL 98 TYR 0.429 0.777 -0.348 0.348
35 SER 36 HIS 0.347 0.000 0.347 0.347
122 THR 123 LEU 0.347 0.000 0.347 0.347
147 SER 205 MET 4.427 4.091 0.336 0.336
293 VAL 326 LEU 0.000 0.336 -0.336 0.336
221 LEU 234 LEU 0.706 0.371 0.334 0.334
146 ILE 208 ALA 0.858 1.187 -0.329 0.329
349 PHE 354 ILE 0.326 0.000 0.326 0.326
232 ASN 235 LYS 1.550 1.224 0.326 0.326
145 VAL 149 ASP 0.000 0.322 -0.322 0.322
200 ILE 204 VAL 0.759 0.437 0.322 0.322
69 THR 318 VAL 0.771 0.450 0.321 0.321
247 VAL 292 ILE 0.257 0.575 -0.318 0.318
149 ASP 328 TYR 4.762 4.446 0.316 0.316
109 ILE 342 ASP 0.316 0.000 0.316 0.316
172 CYS 260 ARG 1.532 1.218 0.314 0.314
305 LYS 316 GLN 0.623 0.312 0.311 0.311
245 MET 246 PRO 0.877 1.187 -0.311 0.311
65 PRO 317 THR 0.000 0.309 -0.309 0.309
305 LYS 320 TRP 0.410 0.717 -0.307 0.307
211 LYS 220 THR 0.192 0.499 -0.307 0.307
105 THR 109 ILE 0.497 0.191 0.306 0.306
275 ARG 278 ARG 0.305 0.000 0.305 0.305
100 LYS 102 LYS 0.304 0.000 0.304 0.304
156 SER 331 SER 0.302 0.000 0.302 0.302
305 LYS 310 ILE 0.457 0.758 -0.301 0.301
294 CYS 295 TRP 0.024 0.325 -0.301 0.301
230 TRP 233 LEU 1.165 0.868 0.297 0.297
150 TYR 238 VAL 0.465 0.762 -0.296 0.296
163 MET 254 TYR 0.291 0.000 0.291 0.291
271 LYS 278 ARG 0.291 0.000 0.291 0.291
155 THR 159 THR 0.289 0.000 0.289 0.289
29 GLY 231 GLU 1.479 1.191 0.288 0.288
316 GLN 320 TRP 0.408 0.695 -0.288 0.288
182 THR 184 ARG 0.293 0.580 -0.288 0.288
30 SER 32 VAL 0.047 0.334 -0.287 0.287
165 VAL 169 ILE 0.959 0.673 0.286 0.286
108 TYR 180 PHE 0.284 0.000 0.284 0.284
107 ILE 183 PRO 1.393 1.110 0.283 0.283
32 VAL 33 ASN 0.278 0.000 0.278 0.278
139 THR 143 LYS 0.187 0.464 -0.277 0.277
290 VAL 294 CYS 0.539 0.264 0.275 0.275
223 PHE 234 LEU 1.436 1.162 0.274 0.274
33 ASN 65 PRO 0.272 0.000 0.272 0.272
154 PHE 193 ASN 0.000 0.272 -0.272 0.272
70 ALA 130 TYR 0.603 0.875 -0.272 0.272
104 ALA 166 ASP 0.000 0.272 -0.272 0.272
150 TYR 200 ILE 0.000 0.270 -0.270 0.270
198 SER 203 PRO 0.359 0.627 -0.268 0.268
31 TRP 235 LYS 0.000 0.267 -0.267 0.267
146 ILE 221 LEU 0.764 1.031 -0.266 0.266
159 THR 163 MET 0.324 0.590 -0.266 0.266
257 MET 281 THR 0.000 0.265 -0.265 0.265
235 LYS 303 ILE 0.082 0.346 -0.264 0.264
241 PHE 245 MET 0.040 0.304 -0.264 0.264
77 TYR 130 TYR 0.000 0.262 -0.262 0.262
333 LEU 337 LEU 0.262 0.000 0.262 0.262
119 ALA 331 SER 0.000 0.260 -0.260 0.260
294 CYS 333 LEU 0.000 0.259 -0.259 0.259
169 ILE 176 LYS 0.258 0.000 0.258 0.258
387 HIS 390 GLU 0.256 0.000 0.256 0.256
105 THR 167 ARG 0.000 0.253 -0.253 0.253
85 LEU 89 PHE 0.654 0.907 -0.252 0.252
165 VAL 249 ILE 0.421 0.170 0.251 0.251
74 MET 130 TYR 0.250 0.000 0.250 0.250
167 ARG 170 ALA 0.000 0.249 -0.249 0.249
264 VAL 267 LEU 0.000 0.249 -0.249 0.249
297 PRO 326 LEU 0.505 0.257 0.248 0.248
81 CYS 124 PRO 1.274 1.026 0.247 0.247
168 TYR 172 CYS 3.027 3.272 -0.244 0.244
241 PHE 246 PRO 3.004 2.760 0.244 0.244
67 MET 131 LEU 0.000 0.243 -0.243 0.243
280 ILE 400 PRO 0.242 0.000 0.242 0.242
139 THR 210 THR 6.373 6.132 0.241 0.241
32 VAL 216 SER 0.240 0.000 0.240 0.240
301 TYR 305 LYS 0.302 0.061 0.240 0.240
171 VAL 172 CYS 0.091 0.331 -0.240 0.240
68 ILE 72 THR 0.388 0.148 0.240 0.240
182 THR 183 PRO 0.648 0.888 -0.240 0.240
84 GLY 331 SER 0.000 0.239 -0.239 0.239
27 SER 28 PRO 0.286 0.523 -0.237 0.237
204 VAL 207 MET 0.237 0.000 0.237 0.237
108 TYR 162 THR 2.233 2.470 -0.237 0.237
105 THR 284 VAL 0.000 0.235 -0.235 0.235
126 GLN 149 ASP 2.335 2.570 -0.235 0.235
172 CYS 173 HIS 1.426 1.192 0.233 0.233
235 LYS 306 ALA 0.568 0.801 -0.233 0.233
146 ILE 150 TYR 0.857 0.629 0.228 0.228
258 ILE 285 LEU 0.225 0.000 0.225 0.225
69 THR 73 ILE 0.537 0.760 -0.223 0.223
247 VAL 251 THR 0.495 0.272 0.223 0.223
157 ILE 250 ILE 0.000 0.221 -0.221 0.221
65 PRO 321 HIS 0.000 0.219 -0.219 0.219
166 ASP 167 ARG 0.000 0.217 -0.217 0.217
164 SER 257 MET 0.000 0.217 -0.217 0.217
372 THR 373 ARG 0.213 0.000 0.213 0.213
209 THR 210 THR 0.000 0.213 -0.213 0.213
203 PRO 207 MET 0.431 0.221 0.210 0.210
135 TRP 145 VAL 0.802 0.592 0.210 0.210
153 MET 154 PHE 1.275 1.483 -0.209 0.209
354 ILE 355 PRO 0.420 0.215 0.206 0.206
103 THR 105 THR 0.114 0.318 -0.204 0.204
314 THR 318 VAL 0.000 0.199 -0.199 0.199
74 MET 78 SER 0.000 0.198 -0.198 0.198
180 PHE 181 ARG 0.197 0.000 0.197 0.197
147 SER 201 GLY 2.718 2.521 0.196 0.196
155 THR 156 SER 0.000 0.195 -0.195 0.195
91 VAL 95 ILE 0.822 0.628 0.195 0.195
73 ILE 317 THR 0.195 0.000 0.195 0.195
108 TYR 166 ASP 1.521 1.327 0.194 0.194
41 LEU 42 SER 0.193 0.000 0.193 0.193
239 PHE 240 ILE 0.081 0.272 -0.191 0.191
66 SER 69 THR 2.376 2.185 0.190 0.190
144 ILE 148 ILE 1.012 0.824 0.188 0.188
295 TRP 298 ILE 0.487 0.674 -0.188 0.188
157 ILE 242 ALA 3.043 3.227 -0.184 0.184
169 ILE 181 ARG 0.000 0.183 -0.183 0.183
267 LEU 277 LEU 0.881 0.699 0.182 0.182
297 PRO 323 CYS 1.340 1.160 0.181 0.181
111 ASN 155 THR 0.000 0.179 -0.179 0.179
159 THR 190 ASN 0.179 0.000 0.179 0.179
92 MET 113 ALA 1.330 1.508 -0.178 0.178
99 THR 100 LYS 0.000 0.178 -0.178 0.178
286 VAL 337 LEU 0.533 0.356 0.177 0.177
243 PHE 244 ILE 1.284 1.107 0.176 0.176
348 CYS 352 PHE 0.175 0.000 0.175 0.175
358 SER 359 ASN 0.174 0.000 0.174 0.174
337 LEU 341 LEU 0.168 0.342 -0.174 0.174
76 LEU 321 HIS 0.174 0.000 0.174 0.174
105 THR 283 MET 0.000 0.173 -0.173 0.173
27 SER 211 LYS 0.000 0.173 -0.173 0.173
302 VAL 320 TRP 1.117 1.289 -0.172 0.172
250 ILE 288 VAL 0.670 0.841 -0.172 0.172
292 ILE 297 PRO 0.218 0.047 0.171 0.171
105 THR 163 MET 0.000 0.170 -0.170 0.170
172 CYS 257 MET 0.628 0.458 0.170 0.170
280 ILE 283 MET 0.000 0.169 -0.169 0.169
70 ALA 131 LEU 0.000 0.169 -0.169 0.169
211 LYS 217 ILE 1.685 1.854 -0.169 0.169
34 LEU 37 LEU 0.168 0.000 0.168 0.168
251 THR 292 ILE 0.168 0.000 0.168 0.168
43 ASP 45 CYS 0.000 0.167 -0.167 0.167
294 CYS 330 ASN 3.086 2.921 0.165 0.165
65 PRO 69 THR 0.600 0.764 -0.164 0.164
31 TRP 32 VAL 0.000 0.161 -0.161 0.161
109 ILE 345 PHE 0.965 0.805 0.161 0.161
146 ILE 220 THR 1.523 1.684 -0.160 0.160
286 VAL 290 VAL 0.368 0.208 0.160 0.160
146 ILE 219 CYS 2.089 1.930 0.159 0.159
128 VAL 132 MET 1.092 1.250 -0.159 0.159
321 HIS 324 ILE 0.158 0.000 0.158 0.158
80 VAL 85 LEU 0.000 0.158 -0.158 0.158
30 SER 221 LEU 0.000 0.157 -0.157 0.157
80 VAL 123 LEU 1.073 1.229 -0.155 0.155
294 CYS 323 CYS 0.000 0.152 -0.152 0.152
169 ILE 174 PRO 0.553 0.401 0.152 0.152
375 HIS 377 SER 0.000 0.151 -0.151 0.151
87 GLY 340 PHE 0.150 0.000 0.150 0.150
135 TRP 218 ASP 0.021 0.171 -0.150 0.150
84 GLY 120 THR 0.955 0.806 0.149 0.149
160 LEU 163 MET 0.000 0.149 -0.149 0.149
29 GLY 223 PHE 0.000 0.149 -0.149 0.149
185 ASN 188 ILE 0.000 0.148 -0.148 0.148
284 VAL 288 VAL 0.060 0.208 -0.147 0.147
157 ILE 247 VAL 0.000 0.147 -0.147 0.147
169 ILE 173 HIS 0.145 0.000 0.145 0.145
233 LEU 237 CYS 0.555 0.699 -0.145 0.145
157 ILE 161 CYS 0.144 0.000 0.144 0.144
226 PRO 229 TYR 0.587 0.443 0.143 0.143
130 TYR 324 ILE 0.000 0.143 -0.143 0.143
208 ALA 221 LEU 1.885 1.743 0.142 0.142
240 ILE 244 ILE 0.000 0.142 -0.142 0.142
110 PHE 114 LEU 0.161 0.020 0.141 0.141
303 ILE 307 LEU 0.909 0.768 0.141 0.141
142 CYS 146 ILE 0.606 0.466 0.141 0.141
115 ALA 155 THR 1.180 1.040 0.140 0.140
223 PHE 230 TRP 3.211 3.070 0.140 0.140
324 ILE 328 TYR 1.228 1.365 -0.137 0.137
237 CYS 242 ALA 0.127 0.263 -0.136 0.136
153 MET 291 PHE 0.000 0.135 -0.135 0.135
16 ALA 17 LEU 0.134 0.000 0.134 0.134
290 VAL 333 LEU 0.640 0.507 0.134 0.134
69 THR 130 TYR 0.133 0.000 0.133 0.133
31 TRP 126 GLN 0.132 0.000 0.132 0.132
238 VAL 243 PHE 0.507 0.639 -0.132 0.132
232 ASN 306 ALA 0.376 0.507 -0.132 0.132
168 TYR 256 LEU 2.595 2.727 -0.131 0.131
89 PHE 92 MET 0.128 0.000 0.128 0.128
80 VAL 332 CYS 2.887 2.759 0.128 0.128
86 PHE 352 PHE 0.000 0.128 -0.128 0.128
294 CYS 329 THR 0.127 0.000 0.127 0.127
150 TYR 154 PHE 0.000 0.125 -0.125 0.125
270 SER 272 GLU 0.435 0.560 -0.125 0.125
137 PHE 141 LEU 2.350 2.473 -0.123 0.123
339 ALA 340 PHE 0.141 0.019 0.122 0.122
140 ILE 144 ILE 0.414 0.534 -0.120 0.120
151 TYR 156 SER 0.000 0.119 -0.119 0.119
127 SER 128 VAL 0.000 0.117 -0.117 0.117
163 MET 167 ARG 0.115 0.000 0.115 0.115
21 SER 22 CYS 0.115 0.000 0.115 0.115
331 SER 334 ASN 0.114 0.000 0.114 0.114
80 VAL 328 TYR 1.364 1.251 0.113 0.113
319 SER 323 CYS 0.112 0.000 0.112 0.112
159 THR 162 THR 0.000 0.109 -0.109 0.109
388 GLN 389 LEU 0.000 0.108 -0.108 0.108
311 PRO 313 THR 0.000 0.108 -0.108 0.108
186 ALA 190 ASN 0.108 0.000 0.108 0.108
143 LYS 208 ALA 6.435 6.539 -0.104 0.104
130 TYR 321 HIS 5.654 5.551 0.104 0.104
60 PRO 61 PRO 0.565 0.669 -0.104 0.104
184 ARG 188 ILE 0.313 0.210 0.103 0.103
29 GLY 219 CYS 0.102 0.000 0.102 0.102
31 TRP 221 LEU 0.000 0.101 -0.101 0.101
336 VAL 340 PHE 0.966 1.065 -0.100 0.100
132 MET 134 THR 0.523 0.623 -0.099 0.099
311 PRO 316 GLN 0.859 0.956 -0.097 0.097
283 MET 287 VAL 0.000 0.097 -0.097 0.097
96 VAL 110 PHE 0.785 0.881 -0.096 0.096
178 LEU 179 ASP 0.000 0.096 -0.096 0.096
152 ASN 155 THR 0.095 0.000 0.095 0.095
79 ILE 84 GLY 0.000 0.095 -0.095 0.095
103 THR 183 PRO 0.008 0.102 -0.094 0.094
91 VAL 335 PRO 1.204 1.110 0.093 0.093
208 ALA 220 THR 1.941 2.033 -0.092 0.092
209 THR 211 LYS 0.092 0.000 0.092 0.092
142 CYS 208 ALA 0.168 0.077 0.091 0.091
105 THR 342 ASP 0.089 0.000 0.089 0.089
143 LYS 207 MET 0.000 0.089 -0.089 0.089
123 LEU 126 GLN 0.004 0.093 -0.088 0.088
88 ASN 335 PRO 4.048 4.134 -0.086 0.086
320 TRP 321 HIS 1.445 1.359 0.085 0.085
228 TRP 229 TYR 2.179 2.094 0.085 0.085
121 SER 122 THR 0.164 0.249 -0.085 0.085
282 ARG 286 VAL 0.000 0.085 -0.085 0.085
151 TYR 205 MET 0.000 0.084 -0.084 0.084
258 ILE 262 LYS 0.876 0.960 -0.084 0.084
184 ARG 185 ASN 0.000 0.081 -0.081 0.081
228 TRP 232 ASN 0.113 0.192 -0.080 0.080
79 ILE 83 VAL 0.144 0.223 -0.079 0.079
104 ALA 186 ALA 1.869 1.944 -0.076 0.076
104 ALA 181 ARG 1.061 1.137 -0.076 0.076
210 THR 219 CYS 0.075 0.000 0.075 0.075
90 LEU 93 TYR 0.000 0.074 -0.074 0.074
256 LEU 259 LEU 0.225 0.152 0.073 0.073
43 ASP 44 PRO 0.753 0.682 0.072 0.072
279 ARG 282 ARG 0.222 0.293 -0.071 0.071
25 ALA 26 PRO 0.574 0.644 -0.070 0.070
210 THR 218 ASP 2.699 2.629 0.069 0.069
296 THR 297 PRO 1.093 1.025 0.068 0.068
301 TYR 323 CYS 0.481 0.549 -0.068 0.068
340 PHE 341 LEU 0.000 0.066 -0.066 0.066
109 ILE 163 MET 0.560 0.626 -0.066 0.066
342 ASP 343 GLU 0.065 0.000 0.065 0.065
188 ILE 192 CYS 0.200 0.265 -0.065 0.065
374 ASP 375 HIS 0.063 0.000 0.063 0.063
51 ASP 52 LEU 1.211 1.148 0.063 0.063
99 THR 348 CYS 0.063 0.000 0.063 0.063
173 HIS 176 LYS 0.267 0.329 -0.061 0.061
59 CYS 60 PRO 0.504 0.445 0.059 0.059
207 MET 220 THR 0.432 0.374 0.058 0.058
291 PHE 292 ILE 0.058 0.000 0.058 0.058
204 VAL 234 LEU 0.000 0.058 -0.058 0.058
89 PHE 117 ALA 0.057 0.000 0.057 0.057
135 TRP 142 CYS 5.433 5.378 0.055 0.055
23 SER 24 PRO 0.398 0.344 0.054 0.054
121 SER 148 ILE 0.052 0.000 0.052 0.052
81 CYS 85 LEU 1.025 0.973 0.052 0.052
191 VAL 195 ILE 0.774 0.723 0.051 0.051
264 VAL 278 ARG 0.000 0.050 -0.050 0.050
71 ILE 131 LEU 0.000 0.049 -0.049 0.049
237 CYS 241 PHE 0.427 0.379 0.049 0.049
35 SER 312 GLU 0.341 0.295 0.046 0.046
338 TYR 346 LYS 0.000 0.046 -0.046 0.046
123 LEU 124 PRO 0.837 0.791 0.046 0.046
238 VAL 242 ALA 0.218 0.173 0.045 0.045
105 THR 106 ASN 0.000 0.045 -0.045 0.045
313 THR 315 PHE 0.465 0.509 -0.044 0.044
91 VAL 109 ILE 0.659 0.618 0.041 0.041
35 SER 64 SER 0.000 0.041 -0.041 0.041
157 ILE 160 LEU 0.000 0.040 -0.040 0.040
209 THR 219 CYS 1.077 1.114 -0.037 0.037
92 MET 117 ALA 0.040 0.003 0.037 0.037
128 VAL 134 THR 0.104 0.067 0.037 0.037
31 TRP 149 ASP 0.037 0.000 0.037 0.037
142 CYS 220 THR 0.428 0.465 -0.037 0.037
76 LEU 80 VAL 0.103 0.140 -0.036 0.036
252 VAL 256 LEU 0.634 0.670 -0.036 0.036
129 ASN 217 ILE 0.000 0.035 -0.035 0.035
220 THR 222 THR 0.028 0.063 -0.034 0.034
104 ALA 108 TYR 0.033 0.000 0.033 0.033
90 LEU 94 VAL 0.170 0.203 -0.033 0.033
283 MET 284 VAL 0.000 0.031 -0.031 0.031
294 CYS 326 LEU 4.948 4.979 -0.031 0.031
234 LEU 238 VAL 0.465 0.434 0.031 0.031
72 THR 73 ILE 0.000 0.030 -0.030 0.030
93 TYR 98 TYR 0.030 0.000 0.030 0.030
307 LEU 308 VAL 0.271 0.301 -0.029 0.029
64 SER 65 PRO 0.581 0.609 -0.028 0.028
167 ARG 171 VAL 0.000 0.027 -0.027 0.027
337 LEU 342 ASP 0.000 0.027 -0.027 0.027
69 THR 72 THR 0.000 0.026 -0.026 0.026
320 TRP 324 ILE 3.090 3.064 0.026 0.026
250 ILE 255 GLY 0.025 0.000 0.025 0.025
116 ASP 330 ASN 0.000 0.025 -0.025 0.025
76 LEU 77 TYR 0.000 0.025 -0.025 0.025
156 SER 160 LEU 0.024 0.000 0.024 0.024
179 ASP 185 ASN 0.423 0.446 -0.024 0.024
246 PRO 250 ILE 0.023 0.000 0.023 0.023
61 PRO 64 SER 0.000 0.022 -0.022 0.022
200 ILE 234 LEU 0.784 0.763 0.021 0.021
298 ILE 302 VAL 0.378 0.400 -0.021 0.021
112 LEU 338 TYR 1.293 1.274 0.020 0.020
249 ILE 253 CYS 0.325 0.306 0.019 0.019
202 LEU 203 PRO 0.890 0.872 0.018 0.018
292 ILE 296 THR 1.036 1.018 0.018 0.018
165 VAL 180 PHE 0.017 0.000 0.017 0.017
316 GLN 317 THR 0.623 0.640 -0.017 0.017
91 VAL 113 ALA 0.686 0.703 -0.017 0.017
56 ASP 58 LEU 0.340 0.355 -0.015 0.015
288 VAL 292 ILE 0.664 0.649 0.015 0.015
128 VAL 133 GLY 0.059 0.044 0.014 0.014
334 ASN 335 PRO 0.914 0.901 0.013 0.013
298 ILE 324 ILE 1.486 1.474 0.012 0.012
32 VAL 129 ASN 0.225 0.237 -0.012 0.012
300 ILE 304 ILE 1.021 1.009 0.012 0.012
280 ILE 284 VAL 0.130 0.119 0.011 0.011
31 TRP 324 ILE 0.734 0.724 0.010 0.010
209 THR 218 ASP 0.951 0.960 -0.009 0.009
17 LEU 18 ALA 0.000 0.008 -0.008 0.008
135 TRP 136 PRO 0.298 0.291 0.008 0.008
173 HIS 174 PRO 0.103 0.096 0.007 0.007
119 ALA 149 ASP 0.006 0.000 0.006 0.006
37 LEU 312 GLU 0.000 0.006 -0.006 0.006
93 TYR 94 VAL 0.165 0.159 0.006 0.006
142 CYS 210 THR 0.898 0.893 0.005 0.005
248 LEU 253 CYS 0.003 0.000 0.003 0.003
246 PRO 251 THR 0.003 0.000 0.003 0.003
66 SER 68 ILE 0.338 0.335 0.003 0.003
154 PHE 197 SER 2.359 2.357 0.002 0.002
240 ILE 246 PRO 0.501 0.499 0.002 0.002
124 PRO 127 SER 0.000 0.002 -0.002 0.002
27 SER 213 ARG 0.002 0.000 0.002 0.002
168 TYR 169 ILE 0.295 0.297 -0.001 0.001
128 VAL 136 PRO 0.115 0.116 -0.001 0.001
141 LEU 144 ILE 0.090 0.088 0.001 0.001
126 GLN 135 TRP 0.000 0.001 -0.001 0.001
250 ILE 254 TYR 1.069 1.068 0.001 0.001
162 THR 163 MET 0.000 0.001 -0.001 0.001

RRCS change distribution

-0.03
Mean ΔRRCS
1.81
Std Dev
-0.02
Median

Magnitude classification

22
High (|Δ| ≥ 5.0)
72
Medium (2.5 ≤ |Δ| < 5.0)
725
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| ≥ 2.52, 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