GPCompReports

OPN5

Gene OPN5 Opsins Sensory receptors UniProt Q6U736
847
Total Contact Pairs
91
Significant Changes
14.08
Max Increase
-14.77
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 K63 12.48x48 K63 12.48x48 K K62 K62 K K64 12.49x49 K64 12.49x49 K L65 12.50x50 L65 12.50x50 L R66 12.51x51 R66 12.51x51 R ICL1ECL1 R98 23.49x49 R98 23.49x49 R W99 23.50x50 W99 23.50x50 W V100 23.51x51 V100 23.51x51 V F101 23.52x52 F101 23.52x52 F ECL1ICL2 L138 34.50x50 L138 34.50x50 L S139 34.51x51 S139 34.51x51 S Y140 34.52x52 Y140 34.52x52 Y G141 34.53x53 G141 34.53x53 G V142 34.54x54 V142 34.54x54 V W143 34.55x55 W143 34.55x55 W L144 34.56x56 L144 34.56x56 L ICL2ECL2 L171 L171 L G172 G172 G D173 D173 D Y174 Y174 Y V175 V175 V P176 P176 P E177 E177 E P178 P178 P F179 F179 F G180 G180 G T181 T181 T S182 S182 S C183 45.50x50 C183 45.50x50 C T184 45.51x51 T184 45.51x51 T L185 45.52x52 L185 45.52x52 L D186 D186 D W187 W187 W W188 W188 W L189 L189 L A190 A190 A Q191 Q191 Q A192 A192 A S193 S193 S V194 V194 V ECL2ICL3 H235 H235 H F236 F236 F D237 D237 D S238 S238 S ICL3ECL3 R279 R279 R P280 P280 P D281 D281 D S282 S282 S I283 I283 I ECL3N-term M1 M1 M A2 A2 A L3 L3 L N4 N4 N H5 H5 H T6 T6 T A7 A7 A L8 L8 L P9 P9 P Q10 Q10 Q D11 D11 D E12 E12 E R13 R13 R L14 L14 L P15 P15 P H16 H16 H Y17 Y17 Y L18 L18 L R19 R19 R D20 D20 D G21 G21 G D22 D22 D P23 P23 P F24 F24 F A25 A25 A S26 S26 S K27 K27 K L28 L28 L N-termC-term A323 A323 A T324 T324 T K325 K325 K K326 K326 K K327 K327 K S328 S328 S L329 L329 L E330 E330 E G331 G331 G F332 F332 F R333 R333 R L334 L334 L H335 H335 H T336 T336 T V337 V337 V T338 T338 T T339 T339 T V340 V340 V R341 R341 R K342 K342 K S343 S343 S S344 S344 S A345 A345 A V346 V346 V L347 L347 L E348 E348 E I349 I349 I H350 H350 H E351 E351 E E352 E352 E W353 W353 W E354 E354 E C-term S29 1.28x28 S29 1.28x28 S W30 1.29x29 W30 1.29x29 W E31 1.30x30 E31 1.30x30 E A32 1.31x31 A32 1.31x31 A D33 1.32x32 D33 1.32x32 D L34 1.33x33 L34 1.33x33 L V35 1.34x34 V35 1.34x34 V A36 1.35x35 A36 1.35x35 A G37 1.36x36 G37 1.36x36 G F38 1.37x37 F38 1.37x37 F Y39 1.38x38 Y39 1.38x38 Y L40 1.39x39 L40 1.39x39 L T41 1.40x40 T41 1.40x40 T I42 1.41x41 I42 1.41x41 I I43 1.42x42 I43 1.42x42 I G44 1.43x43 G44 1.43x43 G I45 1.44x44 I45 1.44x44 I L46 1.45x45 L46 1.45x45 L S47 1.46x46 S47 1.46x46 S T48 1.47x47 T48 1.47x47 T F49 1.48x48 F49 1.48x48 F G50 1.49x49 G50 1.49x49 G N51 1.50x50 N51 1.50x50 N G52 1.51x51 G52 1.51x51 G Y53 1.52x52 Y53 1.52x52 Y V54 1.53x53 V54 1.53x53 V L55 1.54x54 L55 1.54x54 L Y56 1.55x55 Y56 1.55x55 Y M57 1.56x56 M57 1.56x56 M S58 1.57x57 S58 1.57x57 S S59 1.58x58 S59 1.58x58 S R60 1.59x59 R60 1.59x59 R R61 1.60x60 R61 1.60x60 R P67 2.38x38 P67 2.38x38 P A68 2.39x39 A68 2.39x39 A E69 2.40x40 E69 2.40x40 E I70 2.41x41 I70 2.41x41 I M71 2.42x42 M71 2.42x42 M T72 2.43x43 T72 2.43x43 T I73 2.44x44 I73 2.44x44 I N74 2.45x45 N74 2.45x45 N L75 2.46x46 L75 2.46x46 L A76 2.47x47 A76 2.47x47 A V77 2.48x48 V77 2.48x48 V C78 2.49x49 C78 2.49x49 C D79 2.50x50 D79 2.50x50 D L80 2.51x51 L80 2.51x51 L G81 2.52x52 G81 2.52x52 G I82 2.53x53 I82 2.53x53 I S83 2.54x54 S83 2.54x54 S V84 2.55x55 V84 2.55x55 V V85 2.56x551 V85 2.56x551 V G86 2.57x56 G86 2.57x56 G K87 2.58x57 K87 2.58x57 K P88 2.59x58 P88 2.59x58 P F89 2.60x59 F89 2.60x59 F T90 2.61x60 T90 2.61x60 T I91 2.62x61 I91 2.62x61 I I92 2.63x62 I92 2.63x62 I S93 2.64x63 S93 2.64x63 S C94 2.65x64 C94 2.65x64 C F95 2.66x65 F95 2.66x65 F C96 2.67x66 C96 2.67x66 C H97 2.68x67 H97 2.68x67 H G102 3.21x21 G102 3.21x21 G W103 3.22x22 W103 3.22x22 W I104 3.23x23 I104 3.23x23 I G105 3.24x24 G105 3.24x24 G C106 3.25x25 C106 3.25x25 C R107 3.26x26 R107 3.26x26 R W108 3.27x27 W108 3.27x27 W Y109 3.28x28 Y109 3.28x28 Y G110 3.29x29 G110 3.29x29 G W111 3.30x30 W111 3.30x30 W A112 3.31x31 A112 3.31x31 A G113 3.32x32 G113 3.32x32 G F114 3.33x33 F114 3.33x33 F F115 3.34x34 F115 3.34x34 F F116 3.35x35 F116 3.35x35 F G117 3.36x36 G117 3.36x36 G C118 3.37x37 C118 3.37x37 C G119 3.38x38 G119 3.38x38 G S120 3.39x39 S120 3.39x39 S L121 3.40x40 L121 3.40x40 L I122 3.41x41 I122 3.41x41 I T123 3.42x42 T123 3.42x42 T M124 3.43x43 M124 3.43x43 M T125 3.44x44 T125 3.44x44 T A126 3.45x45 A126 3.45x45 A V127 3.46x46 V127 3.46x46 V S128 3.47x47 S128 3.47x47 S L129 3.48x48 L129 3.48x48 L D130 3.49x49 D130 3.49x49 D R131 3.50x50 R131 3.50x50 R Y132 3.51x51 Y132 3.51x51 Y L133 3.52x52 L133 3.52x52 L K134 3.53x53 K134 3.53x53 K I135 3.54x54 I135 3.54x54 I C136 3.55x55 C136 3.55x55 C Y137 3.56x56 Y137 3.56x56 Y K145 4.38x38 K145 4.38x38 K R146 4.39x39 R146 4.39x39 R K147 4.40x40 K147 4.40x40 K H148 4.41x41 H148 4.41x41 H A149 4.42x42 A149 4.42x42 A Y150 4.43x43 Y150 4.43x43 Y I151 4.44x44 I151 4.44x44 I C152 4.45x45 C152 4.45x45 C L153 4.46x46 L153 4.46x46 L A154 4.47x47 A154 4.47x47 A A155 4.48x48 A155 4.48x48 A I156 4.49x49 I156 4.49x49 I W157 4.50x50 W157 4.50x50 W A158 4.51x51 A158 4.51x51 A Y159 4.52x52 Y159 4.52x52 Y A160 4.53x53 A160 4.53x53 A S161 4.54x54 S161 4.54x54 S F162 4.55x55 F162 4.55x55 F W163 4.56x56 W163 4.56x56 W T164 4.57x57 T164 4.57x57 T T165 4.58x58 T165 4.58x58 T M166 4.59x59 M166 4.59x59 M P167 4.60x60 P167 4.60x60 P L168 4.61x61 L168 4.61x61 L V169 4.62x62 V169 4.62x62 V G170 4.63x63 G170 4.63x63 G G195 5.34x35 G195 5.34x35 G G196 5.35x36 G196 5.35x36 G Q197 5.36x37 Q197 5.36x37 Q V198 5.37x38 V198 5.37x38 V F199 5.38x39 F199 5.38x39 F I200 5.39x40 I200 5.39x40 I L201 5.40x41 L201 5.40x41 L N202 5.41x42 N202 5.41x42 N I203 5.42x43 I203 5.42x43 I L204 5.43x44 L204 5.43x44 L F205 5.44x45 F205 5.44x45 F F206 5.45x46 F206 5.45x46 F C207 5.46x461 C207 5.46x461 C L208 5.47x47 L208 5.47x47 L L209 5.48x48 L209 5.48x48 L L210 5.49x49 L210 5.49x49 L P211 5.50x50 P211 5.50x50 P T212 5.51x51 T212 5.51x51 T A213 5.52x52 A213 5.52x52 A V214 5.53x53 V214 5.53x53 V I215 5.54x54 I215 5.54x54 I V216 5.55x55 V216 5.55x55 V F217 5.56x56 F217 5.56x56 F S218 5.57x57 S218 5.57x57 S Y219 5.58x58 Y219 5.58x58 Y V220 5.59x59 V220 5.59x59 V K221 5.60x60 K221 5.60x60 K I222 5.61x61 I222 5.61x61 I I223 5.62x62 I223 5.62x62 I A224 5.63x63 A224 5.63x63 A K225 5.64x64 K225 5.64x64 K V226 5.65x65 V226 5.65x65 V K227 5.66x66 K227 5.66x66 K S228 5.67x67 S228 5.67x67 S S229 5.68x68 S229 5.68x68 S S230 5.69x69 S230 5.69x69 S K231 5.70x70 K231 5.70x70 K E232 5.71x71 E232 5.71x71 E V233 5.72x72 V233 5.72x72 V A234 5.73x73 A234 5.73x73 A R239 6.22x22 R239 6.22x22 R I240 6.23x23 I240 6.23x23 I H241 6.24x24 H241 6.24x24 H S242 6.25x25 S242 6.25x25 S S243 6.26x26 S243 6.26x26 S H244 6.27x27 H244 6.27x27 H V245 6.28x28 V245 6.28x28 V L246 6.29x29 L246 6.29x29 L E247 6.30x30 E247 6.30x30 E M248 6.31x31 M248 6.31x31 M K249 6.32x32 K249 6.32x32 K L250 6.33x33 L250 6.33x33 L T251 6.34x34 T251 6.34x34 T K252 6.35x35 K252 6.35x35 K V253 6.36x36 V253 6.36x36 V A254 6.37x37 A254 6.37x37 A M255 6.38x38 M255 6.38x38 M L256 6.39x39 L256 6.39x39 L I257 6.40x40 I257 6.40x40 I C258 6.41x41 C258 6.41x41 C A259 6.42x42 A259 6.42x42 A G260 6.43x43 G260 6.43x43 G F261 6.44x44 F261 6.44x44 F L262 6.45x45 L262 6.45x45 L I263 6.46x46 I263 6.46x46 I A264 6.47x47 A264 6.47x47 A W265 6.48x48 W265 6.48x48 W I266 6.49x49 I266 6.49x49 I P267 6.50x50 P267 6.50x50 P Y268 6.51x51 Y268 6.51x51 Y A269 6.52x52 A269 6.52x52 A V270 6.53x53 V270 6.53x53 V V271 6.54x54 V271 6.54x54 V S272 6.55x55 S272 6.55x55 S V273 6.56x56 V273 6.56x56 V W274 6.57x57 W274 6.57x57 W S275 6.58x58 S275 6.58x58 S A276 6.59x59 A276 6.59x59 A F277 6.60x60 F277 6.60x60 F G278 6.61x61 G278 6.61x61 G P284 7.31x30 P284 7.31x30 P I285 7.32x31 I285 7.32x31 I Q286 7.33x32 Q286 7.33x32 Q L287 7.34x33 L287 7.34x33 L S288 7.35x34 S288 7.35x34 S V289 7.36x35 V289 7.36x35 V V290 7.37x36 V290 7.37x36 V P291 7.38x37 P291 7.38x37 P T292 7.39x38 T292 7.39x38 T L293 7.40x39 L293 7.40x39 L L294 7.41x40 L294 7.41x40 L A295 7.42x41 A295 7.42x41 A K296 7.43x42 K296 7.43x42 K S297 7.44x43 S297 7.44x43 S A298 7.45x45 A298 7.45x45 A A299 7.46x46 A299 7.46x46 A M300 7.47x47 M300 7.47x47 M Y301 7.48x48 Y301 7.48x48 Y N302 7.49x49 N302 7.49x49 N P303 7.50x50 P303 7.50x50 P I304 7.51x51 I304 7.51x51 I I305 7.52x52 I305 7.52x52 I Y306 7.53x53 Y306 7.53x53 Y Q307 7.54x54 Q307 7.54x54 Q V308 7.55x55 V308 7.55x55 V I309 7.56x56 I309 7.56x56 I D310 8.47x47 D310 8.47x47 D Y311 8.48x48 Y311 8.48x48 Y K312 8.49x49 K312 8.49x49 K Q317 8.54x54 Q317 8.54x54 Q T318 8.55x55 T318 8.55x55 T G319 8.56x56 G319 8.56x56 G F313 8.50x50 F313 8.50x50 F A314 8.51x51 A314 8.51x51 A C315 8.52x52 C315 8.52x52 C C316 8.53x53 C316 8.53x53 C G320 8.57x57 G320 8.57x57 G L321 8.58x58 L321 8.58x58 L K322 8.59x59 K322 8.59x59 K

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 TRP143 (34.55x55) HIS148 (4.41x41) 0.000 14.771 -14.771 HIGH
2 ARG131 (3.50x50) ASP310 (8.47x47) 14.082 0.000 +14.082 HIGH
3 ARG61 (1.60x60) TYR311 (8.48x48) 13.139 0.000 +13.139 HIGH
4 PHE89 (2.60x59) PHE101 (23.52x52) 0.000 12.520 -12.520 HIGH
5 TRP187 SER272 (6.55x55) 0.000 12.102 -12.102 HIGH
6 PHE24 TRP99 (23.50x50) 0.000 11.004 -11.004 HIGH
7 TYR219 (5.58x58) MET255 (6.38x38) 0.000 10.574 -10.574 HIGH
8 TRP111 (3.30x30) TYR174 0.000 10.358 -10.358 HIGH
9 ARG107 (3.26x26) LEU171 9.673 0.000 +9.673 HIGH
10 ARG61 (1.60x60) HIS335 0.000 9.314 -9.314 HIGH
11 VAL54 (1.53x53) GLN307 (7.54x54) 9.048 0.000 +9.048 HIGH
12 TRP103 (3.22x22) ASP173 8.915 0.000 +8.915 HIGH
13 SER26 HIS97 (2.68x67) 0.000 8.862 -8.862 HIGH
14 ARG107 (3.26x26) ASP173 0.000 8.747 -8.747 HIGH
15 SER93 (2.64x63) ARG98 (23.49x49) 0.000 8.493 -8.493 HIGH
16 PHE24 TRP103 (3.22x22) 0.000 8.405 -8.405 HIGH
17 LEU171 PHE199 (5.38x39) 0.000 7.682 -7.682 HIGH
18 TRP30 (1.29x29) GLU31 (1.30x30) 8.005 0.480 +7.525 HIGH
19 ARG131 (3.50x50) GLU247 (6.30x30) 0.000 7.418 -7.418 HIGH
20 ARG19 ASP281 0.000 7.225 -7.225 HIGH
21 GLY110 (3.29x29) TYR174 0.000 7.131 -7.131 HIGH
22 PRO167 (4.60x60) GLY172 0.000 7.119 -7.119 HIGH
23 TRP111 (3.30x30) LEU168 (4.61x61) 9.548 2.631 +6.917 HIGH
24 HIS16 TRP188 0.000 6.777 -6.777 HIGH
25 VAL175 THR184 (45.51x51) 0.000 6.775 -6.775 HIGH
26 TYR219 (5.58x58) ILE257 (6.40x40) 6.656 0.000 +6.656 HIGH
27 GLY172 ASP186 6.558 0.000 +6.558 HIGH
28 TRP103 (3.22x22) ILE104 (3.23x23) 6.396 0.000 +6.396 HIGH
29 LEU185 (45.52x52) TRP187 8.853 2.507 +6.345 HIGH
30 TYR109 (3.28x28) CYS183 (45.50x50) 0.000 6.177 -6.177 HIGH
31 LYS249 (6.32x32) PHE313 (8.50x50) 3.546 9.614 -6.068 HIGH
32 GLU177 PHE179 0.000 6.049 -6.049 HIGH
33 GLU177 SER182 0.000 6.025 -6.025 HIGH
34 ASP33 (1.32x32) CYS94 (2.65x64) 0.000 6.020 -6.020 HIGH
35 PHE261 (6.44x44) TRP265 (6.48x48) 4.539 10.537 -5.997 HIGH
36 ASP310 (8.47x47) LEU334 0.000 5.886 -5.886 HIGH
37 TRP30 (1.29x29) HIS97 (2.68x67) 0.000 5.845 -5.845 HIGH
38 PRO88 (2.59x58) TYR109 (3.28x28) 5.840 0.000 +5.840 HIGH
39 ALA190 GLN197 (5.36x37) 0.544 6.138 -5.594 HIGH
40 ARG131 (3.50x50) THR251 (6.34x34) 0.000 5.555 -5.555 HIGH
41 THR212 (5.51x51) PHE261 (6.44x44) 5.513 0.000 +5.513 HIGH
42 TYR174 SER182 5.420 0.000 +5.420 HIGH
43 PHE114 (3.33x33) THR164 (4.57x57) 2.214 7.623 -5.409 HIGH
44 TRP187 PHE199 (5.38x39) 5.409 0.000 +5.409 HIGH
45 ARG19 ASP20 0.000 5.394 -5.394 HIGH
46 SER230 (5.69x69) GLU247 (6.30x30) 5.363 0.000 +5.363 HIGH
47 SER93 (2.64x63) TRP99 (23.50x50) 0.000 5.135 -5.135 HIGH
48 LYS63 (12.48x48) THR338 0.000 5.072 -5.072 HIGH
49 ILE92 (2.63x62) HIS97 (2.68x67) 5.011 0.000 +5.011 HIGH
50 LYS147 (4.40x40) HIS148 (4.41x41) 0.000 4.927 -4.927 MED
51 TRP103 (3.22x22) ARG107 (3.26x26) 4.891 0.000 +4.891 MED
52 THR164 (4.57x57) TYR174 0.000 4.846 -4.846 MED
53 TYR56 (1.55x55) ARG60 (1.59x59) 7.978 3.207 +4.772 MED
54 ILE304 (7.51x51) ILE309 (7.56x56) 4.502 0.000 +4.502 MED
55 LEU189 GLY196 (5.35x36) 0.000 4.498 -4.498 MED
56 LEU204 (5.43x44) SER272 (6.55x55) 4.443 0.000 +4.443 MED
57 THR90 (2.61x60) TYR109 (3.28x28) 0.000 4.442 -4.442 MED
58 ASP130 (3.49x49) ARG131 (3.50x50) 0.000 4.404 -4.404 MED
59 LEU28 GLN286 (7.33x32) 4.387 0.000 +4.387 MED
60 TYR17 VAL175 0.000 4.366 -4.366 MED
61 PRO178 PHE179 4.316 0.000 +4.316 MED
62 VAL175 CYS183 (45.50x50) 0.000 4.304 -4.304 MED
63 MET166 (4.59x59) LEU171 0.000 4.287 -4.287 MED
64 GLU177 THR184 (45.51x51) 0.000 4.248 -4.248 MED
65 MET124 (3.43x43) PHE261 (6.44x44) 1.253 5.474 -4.222 MED
66 ASP33 (1.32x32) SER93 (2.64x63) 4.206 0.000 +4.206 MED
67 ARG131 (3.50x50) TYR219 (5.58x58) 4.207 0.007 +4.199 MED
68 GLY102 (3.21x21) ASP173 4.084 0.000 +4.084 MED
69 TRP30 (1.29x29) LEU34 (1.33x33) 0.000 4.046 -4.046 MED
70 SER26 ASP33 (1.32x32) 0.000 4.012 -4.012 MED
71 HIS16 PRO178 0.000 4.008 -4.008 MED
72 TRP188 SER275 (6.58x58) 0.000 3.992 -3.992 MED
73 TRP111 (3.30x30) THR165 (4.58x58) 0.000 3.972 -3.972 MED
74 ILE257 (6.40x40) ASN302 (7.49x49) 0.000 3.951 -3.951 MED
75 THR72 (2.43x43) TYR306 (7.53x53) 0.300 4.194 -3.894 MED
76 SER93 (2.64x63) THR181 0.000 3.840 -3.840 MED
77 THR41 (1.40x40) ILE91 (2.62x61) 0.000 3.835 -3.835 MED
78 ILE92 (2.63x62) TRP99 (23.50x50) 3.827 0.000 +3.827 MED
79 GLN191 ALA276 (6.59x59) 0.000 3.807 -3.807 MED
80 GLY86 (2.57x56) TYR109 (3.28x28) 0.000 3.753 -3.753 MED
81 TRP99 (23.50x50) CYS183 (45.50x50) 5.496 1.744 +3.752 MED
82 TYR17 ASP186 0.000 3.710 -3.710 MED
83 PHE179 VAL289 (7.36x35) 0.000 3.699 -3.699 MED
84 GLU348 ILE349 0.000 3.691 -3.691 MED
85 VAL175 ASP186 0.000 3.663 -3.663 MED
86 GLY170 (4.63x63) ASP186 3.652 0.000 +3.652 MED
87 PHE24 ARG98 (23.49x49) 0.000 3.561 -3.561 MED
88 TYR109 (3.28x28) LYS296 (7.43x42) 0.000 3.495 -3.495 MED
89 PRO167 (4.60x60) TYR174 0.000 3.485 -3.485 MED
90 TRP187 ALA276 (6.59x59) 0.000 3.461 -3.461 MED
91 SER229 (5.68x68) GLU232 (5.71x71) 0.132 3.566 -3.434 MED
92 ASP237 ARG239 (6.22x22) 3.396 0.000 +3.396 LOW
93 SER29 (1.28x28) GLU31 (1.30x30) 0.000 3.394 -3.394 LOW
94 LEU8 GLU12 0.368 3.755 -3.387 LOW
95 GLN191 GLN197 (5.36x37) 3.377 0.000 +3.377 LOW
96 ARG131 (3.50x50) LYS134 (3.53x53) 0.000 3.375 -3.375 LOW
97 SER230 (5.69x69) HIS244 (6.27x27) 3.368 0.000 +3.368 LOW
98 ARG131 (3.50x50) TYR306 (7.53x53) 3.362 0.000 +3.362 LOW
99 GLY170 (4.63x63) TRP187 3.345 0.000 +3.345 LOW
100 LYS134 (3.53x53) GLY141 (34.53x53) 0.000 3.337 -3.337 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| ≥ 3.41 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 29-61 61 (13.1), 54 (9.0), 30 (7.5), 31 (7.5), 56 (4.8), 60 (4.8) 6 33 (-6.0), 34 (-4.0), 41 (-3.8) 3
TM2 69-97 88 (5.8), 92 (5.0) 2 89 (-12.5), 97 (-8.9), 93 (-8.5), 94 (-6.0), 90 (-4.4), 72 (-3.9), 91 (-3.8), 86 (-3.8) 8
TM3 102-134 131 (14.1), 107 (9.7), 103 (8.9), 104 (6.4), 102 (4.1) 5 111 (-10.4), 110 (-7.1), 109 (-6.2), 114 (-5.4), 130 (-4.4), 124 (-4.2) 6
TM4 147-170 168 (6.9), 170 (3.7) 2 148 (-14.8), 167 (-7.1), 164 (-5.4), 147 (-4.9), 166 (-4.3), 165 (-4.0) 6
TM5 196-232 212 (5.5), 230 (5.4), 204 (4.4) 3 219 (-10.6), 199 (-7.7), 197 (-5.6), 196 (-4.5), 229 (-3.4), 232 (-3.4) 6
TM6 239-276 257 (6.7) 1 272 (-12.1), 255 (-10.6), 247 (-7.4), 249 (-6.1), 261 (-6.0), 265 (-6.0), 251 (-5.6), 275 (-4.0), 276 (-3.8) 9
TM7 286-309 307 (9.0), 304 (4.5), 309 (4.5), 286 (4.4) 4 302 (-4.0), 306 (-3.9), 289 (-3.7), 296 (-3.5) 4
Intracellular / Extracellular loops & H8
ICL1 63-66 - 0 63 (-5.1) 1
ICL2 141-143 - 0 143 (-14.8) 1
ICL3 237-237 - 0 - 0
ECL1 98-101 - 0 101 (-12.5), 99 (-11.0), 98 (-8.5) 3
ECL2 171-191 171 (9.7), 173 (8.9), 186 (6.6), 185 (6.3), 178 (4.3) 5 187 (-12.1), 174 (-10.4), 172 (-7.1), 188 (-6.8), 175 (-6.8), 184 (-6.8), 183 (-6.2), 177 (-6.0), 179 (-6.0), 182 (-6.0), 190 (-5.6), 189 (-4.5), 181 (-3.8), 191 (-3.8) 14
ECL3 281-281 - 0 281 (-7.2) 1
H8 310-313 310 (14.1), 311 (13.1) 2 313 (-6.1) 1

Interactive visualizations

ΔRRCS distribution

Active vs inactive comparison

Residue-wise changes

TM domain breakdown

Variants of interest

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

Position Protein change DNA change Allele freq Het / Hom ΔRRCS AM score Pathogenicity Conservation dbSNP
148 p.His148Asn c.442C>A 2.07e-06 3 / 0 14.77 0.290 BENIGN 0.87
131 p.Arg131Gln c.392G>A 2.74e-06 4 / 0 14.08 0.927 PATHOGENIC 0.88 rs1349834900
61 p.Arg61Gln c.182G>A 1.31e-05 19 / 0 13.14 0.151 BENIGN 0.76 rs201533729
101 p.Phe101Ser c.302T>C 6.84e-07 1 / 0 12.52 0.938 PATHOGENIC 0.89 rs755177267
272 p.Ser272Tyr c.815C>A 6.84e-07 1 / 0 12.10 0.985 PATHOGENIC 0.91
255 p.Met255Lys c.764T>A 6.84e-07 1 / 0 10.57 0.976 PATHOGENIC 0.68
219 p.Tyr219His c.655T>C 6.84e-07 1 / 0 10.57 0.957 PATHOGENIC 0.99
255 p.Met255Ile c.765G>A 1.37e-06 2 / 0 10.57 - nan - rs763362808
107 p.Arg107Cys c.319C>T 7.53e-06 11 / 0 9.67 0.431 AMBIGUOUS 0.53 rs1219866609
171 p.Leu171Met c.511C>A 6.84e-07 1 / 0 9.67 0.169 BENIGN 0.48
107 p.Arg107His c.320G>A 8.89e-06 13 / 0 9.67 - nan - rs1303441120
335 p.His335Pro c.1004A>C 6.85e-07 1 / 0 9.31 0.072 BENIGN 0.74
54 p.Val54Gly c.161T>G 6.86e-07 1 / 0 9.05 0.877 PATHOGENIC 0.98
54 p.Val54Ala c.161T>C 6.86e-07 1 / 0 9.05 - nan - rs1561888730
173 p.Asp173His c.517G>C 6.84e-07 1 / 0 8.91 0.199 BENIGN 0.51
173 p.Asp173Gly c.518A>G 6.84e-07 1 / 0 8.91 - nan -
98 p.Arg98Ser c.292C>A 6.84e-07 1 / 0 8.49 0.669 PATHOGENIC 0.71
98 p.Arg98Cys c.292C>T 4.79e-06 7 / 0 8.49 - nan - rs145617365
98 p.Arg98His c.293G>A 3.42e-06 5 / 0 8.49 - nan - rs1773384350
30 p.Trp30Arg c.88T>C 6.84e-07 1 / 0 7.52 0.160 BENIGN 0.44
30 p.Trp30Gly c.88T>G 6.84e-07 1 / 0 7.52 - nan -
19 p.Arg19Gly c.55C>G 6.16e-06 9 / 0 7.23 0.132 BENIGN 0.47
19 p.Arg19Pro c.56G>C 6.57e-06 1 / 0 7.23 - nan - rs1240730978
19 p.Arg19Gln c.56G>A 2.74e-06 4 / 0 7.23 - nan - rs1240730978
172 p.Gly172Val c.515G>T 6.57e-06 1 / 0 7.12 0.938 PATHOGENIC 0.89 rs1413712031
168 p.Leu168Trp c.503T>G 6.84e-07 1 / 0 6.92 0.467 AMBIGUOUS 0.65
188 p.Trp188Arg c.562T>C 6.84e-07 1 / 0 6.78 0.594 PATHOGENIC 0.80 rs1773513992
16 p.His16Tyr c.46C>T 1.37e-06 2 / 0 6.78 0.100 BENIGN 0.84
16 p.His16Arg c.47A>G 2.53e-05 37 / 0 6.78 - nan - rs377432555
184 p.Thr184Ala c.550A>G 6.84e-07 1 / 0 6.77 0.725 PATHOGENIC 0.92 rs1773513415
175 p.Val175Ile c.523G>A 1.23e-05 18 / 0 6.77 0.139 BENIGN 0.64 rs780695747
104 p.Ile104Met c.312C>G 6.84e-07 1 / 0 6.40 0.076 BENIGN 0.37
185 p.Leu185Val c.553C>G 6.84e-07 1 / 0 6.35 0.307 BENIGN 0.77
109 p.Tyr109Cys c.326A>G 2.74e-06 4 / 0 6.18 0.885 PATHOGENIC 0.89 rs748559697
313 p.Phe313Ser c.938T>C 5.47e-06 8 / 0 6.07 0.323 BENIGN 0.48 rs1320473532
249 p.Lys249Gln c.745A>C 6.85e-07 1 / 0 6.07 0.268 BENIGN 0.82
177 p.Glu177Ala c.530A>C 6.84e-07 1 / 0 6.05 0.944 PATHOGENIC 0.95
33 p.Asp33Ala c.98A>C 6.84e-07 1 / 0 6.02 0.988 PATHOGENIC 0.98
94 p.Cys94Gly c.280T>G 6.84e-07 1 / 0 6.02 0.472 AMBIGUOUS 0.53
261 p.Phe261Leu c.781T>C 6.84e-07 1 / 0 6.00 0.999 PATHOGENIC 1.00
334 p.Leu334Gln c.1001T>A 7.54e-06 11 / 0 5.89 0.068 BENIGN 0.52 rs774001394
88 p.Pro88Ser c.262C>T 6.84e-07 1 / 0 5.84 0.896 PATHOGENIC 0.93 rs1189336023
88 p.Pro88Thr c.262C>A 6.84e-07 1 / 0 5.84 - nan -
88 p.Pro88Leu c.263C>T 1.37e-06 2 / 0 5.84 - nan - rs758572074
190 p.Ala190Pro c.568G>C 1.37e-06 2 / 0 5.59 0.496 AMBIGUOUS 0.64 rs1172262178
190 p.Ala190Ser c.568G>T 6.57e-06 1 / 0 5.59 - nan - rs1172262178
190 p.Ala190Val c.569C>T 6.84e-07 1 / 0 5.59 - nan - rs1581735042
251 p.Thr251Ala c.751A>G 6.86e-07 1 / 0 5.55 0.576 PATHOGENIC 0.88
212 p.Thr212Lys c.635C>A 6.57e-06 1 / 0 5.51 0.978 PATHOGENIC 0.71 rs773340997
212 p.Thr212Met c.635C>T 1.18e-04 172 / 0 5.51 - nan - rs773340997
114 p.Phe114Val c.340T>G 6.84e-07 1 / 0 5.41 0.928 PATHOGENIC 0.92 rs778478489
164 p.Thr164Ala c.490A>G 6.84e-07 1 / 0 5.41 0.106 BENIGN 0.80
114 p.Phe114Leu c.340T>C 6.84e-07 1 / 0 5.41 - nan - rs778478489
20 p.Asp20His c.58G>C 1.10e-05 16 / 0 5.39 0.136 BENIGN 0.51 rs775797817
20 p.Asp20Val c.59A>T 9.58e-06 14 / 0 5.39 - nan - rs1773107467
230 p.Ser230Thr c.688T>A 3.42e-06 5 / 0 5.36 0.091 BENIGN 0.51 rs1471692820
230 p.Ser230Phe c.689C>T 5.47e-06 8 / 0 5.36 - nan - rs778780427
230 p.Ser230Tyr c.689C>A 6.84e-07 1 / 0 5.36 - nan -
338 p.Thr338Ala c.1012A>G 6.85e-07 1 / 0 5.07 0.070 BENIGN 0.67 rs756067884
338 p.Thr338Ile c.1013C>T 6.85e-07 1 / 0 5.07 - nan - rs1224100656
92 p.Ile92Thr c.275T>C 6.84e-07 1 / 0 5.01 0.363 AMBIGUOUS 0.61
92 p.Ile92Met c.276C>G 6.84e-07 1 / 0 5.01 - nan - rs1289920922
147 p.Lys147Arg c.440A>G 3.46e-06 5 / 0 4.93 0.073 BENIGN 0.61 rs774464271
60 p.Arg60Gly c.178A>G 2.75e-05 40 / 0 4.77 0.309 BENIGN 0.75 rs140514652
309 p.Ile309Thr c.926T>C 6.57e-06 1 / 0 4.50 0.195 BENIGN 0.71 rs1295284200
304 p.Ile304Leu c.910A>C 6.84e-07 1 / 0 4.50 0.150 BENIGN 0.90 rs748306671
196 p.Gly196Val c.587G>T 6.84e-07 1 / 0 4.50 0.764 PATHOGENIC 0.78
130 p.Asp130Asn c.388G>A 6.84e-07 1 / 0 4.40 0.891 PATHOGENIC 0.71 rs1322203175
28 p.Leu28Pro c.83T>C 1.37e-06 2 / 0 4.39 0.975 PATHOGENIC 0.98
286 p.Gln286His c.858G>C 3.42e-06 5 / 0 4.39 0.209 BENIGN 0.48 rs1239178606
17 p.Tyr17Cys c.50A>G 1.37e-06 2 / 0 4.37 0.277 BENIGN 0.88
178 p.Pro178Ser c.532C>T 1.37e-06 2 / 0 4.32 0.842 PATHOGENIC 0.95 rs1773512297
166 p.Met166Leu c.496A>C 6.84e-07 1 / 0 4.29 0.158 BENIGN 0.66
166 p.Met166Val c.496A>G 2.05e-06 3 / 0 4.29 - nan - rs754199132
166 p.Met166Arg c.497T>G 6.84e-07 1 / 0 4.29 - nan -
166 p.Met166Ile c.498G>A 6.84e-07 1 / 0 4.29 - nan - rs143358523
166 p.Met166Ile c.498G>C 2.05e-06 3 / 0 4.29 - nan - rs143358523
302 p.Asn302Ser c.905A>G 6.84e-07 1 / 0 3.95 0.751 PATHOGENIC 0.98
306 p.Tyr306Cys c.917A>G 1.37e-06 2 / 0 3.89 0.784 PATHOGENIC 0.97 rs1774054650
72 p.Thr72Ala c.214A>G 6.85e-07 1 / 0 3.89 0.419 AMBIGUOUS 0.84
72 p.Thr72Ile c.215C>T 3.42e-06 5 / 0 3.89 - nan - rs757212050
181 p.Thr181Asn c.542C>A 6.84e-07 1 / 0 3.84 0.770 PATHOGENIC 0.83
91 p.Ile91Val c.271A>G 2.74e-06 4 / 0 3.83 0.127 BENIGN 0.71 rs985983285
86 p.Gly86Ser c.256G>A 6.84e-07 1 / 0 3.75 0.693 PATHOGENIC 0.89
289 p.Val289Leu c.865G>C 2.05e-06 3 / 0 3.70 0.481 AMBIGUOUS 0.78
348 p.Glu348Lys c.1042G>A 2.06e-06 3 / 0 3.69 0.109 BENIGN 0.87 rs1044176414
170 p.Gly170Asp c.509G>A 6.84e-07 1 / 0 3.65 0.658 PATHOGENIC 0.97
232 p.Glu232Asp c.696A>T 2.74e-06 4 / 0 3.43 0.142 BENIGN 0.68 rs772178094
232 p.Glu232Asp c.696A>C 1.37e-06 2 / 0 3.43 - nan -
237 p.Asp237Tyr c.709G>T 6.57e-06 1 / 0 3.40 0.609 PATHOGENIC 0.71 rs1287318511
239 p.Arg239Trp c.715C>T 1.37e-06 2 / 0 3.40 0.369 AMBIGUOUS 0.70 rs1773523930
239 p.Arg239Gln c.716G>A 2.74e-06 4 / 0 3.40 - nan - rs975328159
29 p.Ser29Cys c.86C>G 6.84e-07 1 / 0 3.39 0.492 AMBIGUOUS 0.84
12 p.Glu12Gln c.34G>C 2.05e-06 3 / 0 3.39 0.091 BENIGN 0.55
8 p.Leu8Pro c.23T>C 6.84e-07 1 / 0 3.39 0.070 BENIGN 0.41 rs1773106198
12 p.Glu12Gly c.35A>G 8.90e-06 13 / 0 3.39 - nan - rs779233023
244 p.His244Tyr c.730C>T 1.37e-06 2 / 0 3.37 0.170 BENIGN 0.69 rs972216916
141 p.Gly141Trp c.421G>T 6.85e-07 1 / 0 3.34 0.893 PATHOGENIC 0.91
248 p.Met248Arg c.743T>G 1.37e-06 2 / 0 3.19 0.356 AMBIGUOUS 0.64
248 p.Met248Thr c.743T>C 6.85e-07 1 / 0 3.19 - nan -
69 p.Glu69Lys c.205G>A 6.85e-07 1 / 0 3.18 0.945 PATHOGENIC 0.98
347 p.Leu347Pro c.1040T>C 6.85e-07 1 / 0 3.18 0.065 BENIGN 0.41
292 p.Thr292Ile c.875C>T 6.84e-07 1 / 0 3.16 0.856 PATHOGENIC 0.84
42 p.Ile42Thr c.125T>C 3.42e-06 5 / 0 3.15 0.283 BENIGN 0.65 rs1464761466
42 p.Ile42Met c.126A>G 6.85e-07 1 / 0 3.15 - nan - rs1773108778
66 p.Arg66Ile c.197G>T 6.85e-07 1 / 0 3.09 0.683 PATHOGENIC 0.82
246 p.Leu246Arg c.737T>G 1.37e-06 2 / 0 3.09 0.222 BENIGN 0.71
66 p.Arg66Lys c.197G>A 2.06e-06 3 / 0 3.09 - nan -
27 p.Lys27Glu c.79A>G 6.84e-07 1 / 0 3.06 0.369 AMBIGUOUS 0.74
27 p.Lys27Gln c.79A>C 2.05e-06 3 / 0 3.06 - nan - rs916898311
27 p.Lys27Arg c.80A>G 4.78e-04 697 / 1 3.06 - nan - rs149802356

Complete RRCS results

Top 1000 contact pairs by |ΔRRCS|. Significance threshold: |ΔRRCS| ≥ 3.41, computed as max(mean(|Δ|) + σ, 0.2). Highlighted rows indicate significant changes.

Res1 AA1 Res2 AA2 Active RRCS Inactive RRCS ΔRRCS |ΔRRCS|
143 TRP 148 HIS 0.000 14.771 -14.771 14.771
131 ARG 310 ASP 14.082 0.000 14.082 14.082
61 ARG 311 TYR 13.139 0.000 13.139 13.139
89 PHE 101 PHE 0.000 12.520 -12.520 12.520
187 TRP 272 SER 0.000 12.102 -12.102 12.102
24 PHE 99 TRP 0.000 11.004 -11.004 11.004
219 TYR 255 MET 0.000 10.574 -10.574 10.574
111 TRP 174 TYR 0.000 10.358 -10.358 10.358
107 ARG 171 LEU 9.673 0.000 9.673 9.673
61 ARG 335 HIS 0.000 9.314 -9.314 9.314
54 VAL 307 GLN 9.048 0.000 9.048 9.048
103 TRP 173 ASP 8.915 0.000 8.915 8.915
26 SER 97 HIS 0.000 8.862 -8.862 8.862
107 ARG 173 ASP 0.000 8.747 -8.747 8.747
93 SER 98 ARG 0.000 8.493 -8.493 8.493
24 PHE 103 TRP 0.000 8.405 -8.405 8.405
171 LEU 199 PHE 0.000 7.682 -7.682 7.682
30 TRP 31 GLU 8.005 0.480 7.525 7.525
131 ARG 247 GLU 0.000 7.418 -7.418 7.418
19 ARG 281 ASP 0.000 7.225 -7.225 7.225
110 GLY 174 TYR 0.000 7.131 -7.131 7.131
167 PRO 172 GLY 0.000 7.119 -7.119 7.119
111 TRP 168 LEU 9.548 2.631 6.917 6.917
16 HIS 188 TRP 0.000 6.777 -6.777 6.777
175 VAL 184 THR 0.000 6.775 -6.775 6.775
219 TYR 257 ILE 6.656 0.000 6.656 6.656
172 GLY 186 ASP 6.558 0.000 6.558 6.558
103 TRP 104 ILE 6.396 0.000 6.396 6.396
185 LEU 187 TRP 8.853 2.507 6.345 6.345
109 TYR 183 CYS 0.000 6.177 -6.177 6.177
249 LYS 313 PHE 3.546 9.614 -6.068 6.068
177 GLU 179 PHE 0.000 6.049 -6.049 6.049
177 GLU 182 SER 0.000 6.025 -6.025 6.025
33 ASP 94 CYS 0.000 6.020 -6.020 6.020
261 PHE 265 TRP 4.539 10.537 -5.997 5.997
310 ASP 334 LEU 0.000 5.886 -5.886 5.886
30 TRP 97 HIS 0.000 5.845 -5.845 5.845
88 PRO 109 TYR 5.840 0.000 5.840 5.840
190 ALA 197 GLN 0.544 6.138 -5.594 5.594
131 ARG 251 THR 0.000 5.555 -5.555 5.555
212 THR 261 PHE 5.513 0.000 5.513 5.513
174 TYR 182 SER 5.420 0.000 5.420 5.420
114 PHE 164 THR 2.214 7.623 -5.409 5.409
187 TRP 199 PHE 5.409 0.000 5.409 5.409
19 ARG 20 ASP 0.000 5.394 -5.394 5.394
230 SER 247 GLU 5.363 0.000 5.363 5.363
93 SER 99 TRP 0.000 5.135 -5.135 5.135
63 LYS 338 THR 0.000 5.072 -5.072 5.072
92 ILE 97 HIS 5.011 0.000 5.011 5.011
147 LYS 148 HIS 0.000 4.927 -4.927 4.927
103 TRP 107 ARG 4.891 0.000 4.891 4.891
164 THR 174 TYR 0.000 4.846 -4.846 4.846
56 TYR 60 ARG 7.978 3.207 4.772 4.772
304 ILE 309 ILE 4.502 0.000 4.502 4.502
189 LEU 196 GLY 0.000 4.498 -4.498 4.498
204 LEU 272 SER 4.443 0.000 4.443 4.443
90 THR 109 TYR 0.000 4.442 -4.442 4.442
130 ASP 131 ARG 0.000 4.404 -4.404 4.404
28 LEU 286 GLN 4.387 0.000 4.387 4.387
17 TYR 175 VAL 0.000 4.366 -4.366 4.366
178 PRO 179 PHE 4.316 0.000 4.316 4.316
175 VAL 183 CYS 0.000 4.304 -4.304 4.304
166 MET 171 LEU 0.000 4.287 -4.287 4.287
177 GLU 184 THR 0.000 4.248 -4.248 4.248
124 MET 261 PHE 1.253 5.474 -4.222 4.222
33 ASP 93 SER 4.206 0.000 4.206 4.206
131 ARG 219 TYR 4.207 0.007 4.199 4.199
102 GLY 173 ASP 4.084 0.000 4.084 4.084
30 TRP 34 LEU 0.000 4.046 -4.046 4.046
26 SER 33 ASP 0.000 4.012 -4.012 4.012
16 HIS 178 PRO 0.000 4.008 -4.008 4.008
188 TRP 275 SER 0.000 3.992 -3.992 3.992
111 TRP 165 THR 0.000 3.972 -3.972 3.972
257 ILE 302 ASN 0.000 3.951 -3.951 3.951
72 THR 306 TYR 0.300 4.194 -3.894 3.894
93 SER 181 THR 0.000 3.840 -3.840 3.840
41 THR 91 ILE 0.000 3.835 -3.835 3.835
92 ILE 99 TRP 3.827 0.000 3.827 3.827
191 GLN 276 ALA 0.000 3.807 -3.807 3.807
86 GLY 109 TYR 0.000 3.753 -3.753 3.753
99 TRP 183 CYS 5.496 1.744 3.752 3.752
17 TYR 186 ASP 0.000 3.710 -3.710 3.710
179 PHE 289 VAL 0.000 3.699 -3.699 3.699
348 GLU 349 ILE 0.000 3.691 -3.691 3.691
175 VAL 186 ASP 0.000 3.663 -3.663 3.663
170 GLY 186 ASP 3.652 0.000 3.652 3.652
24 PHE 98 ARG 0.000 3.561 -3.561 3.561
109 TYR 296 LYS 0.000 3.495 -3.495 3.495
167 PRO 174 TYR 0.000 3.485 -3.485 3.485
187 TRP 276 ALA 0.000 3.461 -3.461 3.461
229 SER 232 GLU 0.132 3.566 -3.434 3.434
237 ASP 239 ARG 3.396 0.000 3.396 3.396
29 SER 31 GLU 0.000 3.394 -3.394 3.394
8 LEU 12 GLU 0.368 3.755 -3.387 3.387
191 GLN 197 GLN 3.377 0.000 3.377 3.377
131 ARG 134 LYS 0.000 3.375 -3.375 3.375
230 SER 244 HIS 3.368 0.000 3.368 3.368
131 ARG 306 TYR 3.362 0.000 3.362 3.362
170 GLY 187 TRP 3.345 0.000 3.345 3.345
134 LYS 141 GLY 0.000 3.337 -3.337 3.337
114 PHE 174 TYR 0.000 3.335 -3.335 3.335
90 THR 181 THR 0.000 3.299 -3.299 3.299
174 TYR 184 THR 2.024 5.320 -3.296 3.296
173 ASP 186 ASP 0.287 3.561 -3.275 3.275
107 ARG 174 TYR 0.000 3.236 -3.236 3.236
40 LEU 91 ILE 0.000 3.224 -3.224 3.224
244 HIS 248 MET 0.000 3.187 -3.187 3.187
24 PHE 102 GLY 0.000 3.182 -3.182 3.182
61 ARG 69 GLU 3.429 0.248 3.181 3.181
347 LEU 348 GLU 0.000 3.178 -3.178 3.178
109 TYR 182 SER 0.000 3.159 -3.159 3.159
177 GLU 292 THR 0.000 3.159 -3.159 3.159
38 PHE 42 ILE 3.149 0.000 3.149 3.149
187 TRP 196 GLY 3.093 0.000 3.093 3.093
66 ARG 246 LEU 0.000 3.091 -3.091 3.091
124 MET 306 TYR 3.091 0.000 3.091 3.091
26 SER 179 PHE 0.000 3.068 -3.068 3.068
85 VAL 109 TYR 3.063 0.000 3.063 3.063
27 LYS 179 PHE 0.000 3.056 -3.056 3.056
311 TYR 315 CYS 2.984 0.000 2.984 2.984
208 LEU 265 TRP 2.970 0.000 2.970 2.970
184 THR 268 TYR 0.000 2.970 -2.970 2.970
326 LYS 330 GLU 2.943 0.000 2.943 2.943
72 THR 307 GLN 2.935 0.000 2.935 2.935
179 PHE 182 SER 0.000 2.919 -2.919 2.919
65 LEU 146 ARG 7.311 4.399 2.912 2.912
124 MET 258 CYS 0.000 2.901 -2.901 2.901
99 TRP 181 THR 5.420 2.541 2.879 2.879
124 MET 302 ASN 2.838 0.000 2.838 2.838
236 PHE 240 ILE 0.000 2.835 -2.835 2.835
99 TRP 180 GLY 0.000 2.829 -2.829 2.829
61 ARG 334 LEU 0.000 2.800 -2.800 2.800
225 LYS 229 SER 0.441 3.222 -2.780 2.780
190 ALA 276 ALA 0.000 2.777 -2.777 2.777
37 GLY 95 PHE 0.000 2.777 -2.777 2.777
135 ILE 248 MET 0.000 2.773 -2.773 2.773
274 TRP 282 SER 0.239 3.009 -2.770 2.770
162 PHE 163 TRP 3.790 6.559 -2.769 2.769
85 VAL 108 TRP 0.000 2.762 -2.762 2.762
33 ASP 181 THR 0.000 2.751 -2.751 2.751
226 VAL 247 GLU 2.736 0.000 2.736 2.736
22 ASP 98 ARG 0.000 2.676 -2.676 2.676
197 GLN 276 ALA 2.651 0.000 2.651 2.651
297 SER 301 TYR 0.912 3.560 -2.647 2.647
303 PRO 308 VAL 2.633 0.000 2.633 2.633
174 TYR 176 PRO 2.610 0.000 2.610 2.610
167 PRO 173 ASP 0.000 2.566 -2.566 2.566
17 TYR 23 PRO 0.000 2.566 -2.566 2.566
87 LYS 296 LYS 0.000 2.564 -2.564 2.564
176 PRO 183 CYS 0.000 2.541 -2.541 2.541
191 GLN 278 GLY 0.000 2.534 -2.534 2.534
264 ALA 294 LEU 4.368 6.890 -2.521 2.521
130 ASP 144 LEU 0.370 2.889 -2.518 2.518
215 ILE 261 PHE 2.500 0.000 2.500 2.500
187 TRP 268 TYR 0.000 2.498 -2.498 2.498
82 ILE 87 LYS 0.000 2.463 -2.463 2.463
16 HIS 17 TYR 0.000 2.449 -2.449 2.449
249 LYS 310 ASP 0.000 2.430 -2.430 2.430
179 PHE 181 THR 0.000 2.404 -2.404 2.404
28 LEU 33 ASP 0.000 2.399 -2.399 2.399
187 TRP 190 ALA 2.350 0.000 2.350 2.350
106 CYS 176 PRO 0.000 2.343 -2.343 2.343
28 LEU 97 HIS 0.000 2.341 -2.341 2.341
24 PHE 180 GLY 0.000 2.329 -2.329 2.329
97 HIS 182 SER 2.271 0.000 2.271 2.271
174 TYR 185 LEU 0.000 2.248 -2.248 2.248
99 TRP 106 CYS 7.796 5.557 2.239 2.239
153 LEU 157 TRP 2.265 0.041 2.224 2.224
63 LYS 336 THR 0.000 2.207 -2.207 2.207
132 TYR 217 PHE 0.000 2.190 -2.190 2.190
44 GLY 87 LYS 0.000 2.168 -2.168 2.168
298 ALA 301 TYR 2.162 0.000 2.162 2.162
172 GLY 184 THR 2.158 0.000 2.158 2.158
131 ARG 250 LEU 0.000 2.150 -2.150 2.150
43 ILE 87 LYS 0.000 2.146 -2.146 2.146
233 VAL 244 HIS 0.209 2.351 -2.143 2.143
38 PHE 95 PHE 0.000 2.130 -2.130 2.130
162 PHE 166 MET 0.000 2.128 -2.128 2.128
173 ASP 185 LEU 0.000 2.120 -2.120 2.120
168 LEU 174 TYR 0.000 2.113 -2.113 2.113
27 LYS 178 PRO 0.000 2.107 -2.107 2.107
89 PHE 99 TRP 0.015 2.106 -2.091 2.091
265 TRP 295 ALA 1.960 4.043 -2.082 2.082
94 CYS 181 THR 0.000 2.080 -2.080 2.080
103 TRP 176 PRO 0.000 2.072 -2.072 2.072
179 PHE 292 THR 0.000 2.055 -2.055 2.055
166 MET 199 PHE 3.210 1.167 2.042 2.042
305 ILE 310 ASP 2.037 0.000 2.037 2.037
99 TRP 109 TYR 1.995 4.017 -2.022 2.022
190 ALA 196 GLY 3.718 1.703 2.015 2.015
22 ASP 27 LYS 0.000 2.011 -2.011 2.011
69 GLU 311 TYR 2.011 0.000 2.011 2.011
92 ILE 101 PHE 0.000 2.004 -2.004 2.004
128 SER 219 TYR 3.706 5.699 -1.993 1.993
115 PHE 164 THR 4.537 6.511 -1.974 1.974
131 ARG 257 ILE 1.965 0.000 1.965 1.965
88 PRO 99 TRP 1.959 0.000 1.959 1.959
177 GLU 178 PRO 0.000 1.943 -1.943 1.943
66 ARG 311 TYR 1.939 0.000 1.939 1.939
76 ALA 307 GLN 1.935 0.000 1.935 1.935
51 ASN 76 ALA 6.045 4.121 1.924 1.924
134 LYS 247 GLU 0.000 1.913 -1.913 1.913
178 PRO 188 TRP 0.000 1.913 -1.913 1.913
115 PHE 116 PHE 1.005 2.916 -1.912 1.912
16 HIS 176 PRO 0.000 1.910 -1.910 1.910
99 TRP 182 SER 0.576 2.478 -1.902 1.902
50 GLY 303 PRO 2.262 4.163 -1.901 1.901
83 SER 87 LYS 0.000 1.888 -1.888 1.888
88 PRO 101 PHE 1.862 0.000 1.862 1.862
37 GLY 94 CYS 0.000 1.858 -1.858 1.858
98 ARG 181 THR 2.590 0.733 1.857 1.857
262 LEU 266 ILE 2.198 0.347 1.852 1.852
159 TYR 163 TRP 11.201 9.359 1.841 1.841
182 SER 184 THR 1.834 0.000 1.834 1.834
85 VAL 113 GLY 1.825 0.000 1.825 1.825
171 LEU 185 LEU 1.822 0.000 1.822 1.822
167 PRO 199 PHE 0.387 2.204 -1.817 1.817
186 ASP 189 LEU 0.000 1.817 -1.817 1.817
41 THR 90 THR 1.815 0.000 1.815 1.815
349 ILE 350 HIS 1.796 0.000 1.796 1.796
115 PHE 157 TRP 5.727 3.952 1.774 1.774
208 LEU 269 ALA 2.639 0.867 1.773 1.773
29 SER 97 HIS 0.000 1.769 -1.769 1.769
12 GLU 280 PRO 0.000 1.765 -1.765 1.765
67 PRO 144 LEU 2.614 0.855 1.758 1.758
24 PHE 176 PRO 0.000 1.747 -1.747 1.747
66 ARG 250 LEU 0.000 1.734 -1.734 1.734
37 GLY 90 THR 1.733 0.000 1.733 1.733
276 ALA 277 PHE 0.000 1.719 -1.719 1.719
145 LYS 148 HIS 2.455 0.740 1.715 1.715
191 GLN 280 PRO 0.000 1.713 -1.713 1.713
236 PHE 241 HIS 0.000 1.694 -1.694 1.694
190 ALA 200 ILE 0.000 1.691 -1.691 1.691
66 ARG 318 THR 1.685 0.000 1.685 1.685
66 ARG 315 CYS 1.679 0.000 1.679 1.679
256 LEU 305 ILE 0.319 1.994 -1.675 1.675
106 CYS 175 VAL 0.000 1.670 -1.670 1.670
30 TRP 95 PHE 0.000 1.653 -1.653 1.653
177 GLU 268 TYR 0.000 1.648 -1.648 1.648
182 SER 296 LYS 0.000 1.648 -1.648 1.648
303 PRO 307 GLN 2.072 0.427 1.645 1.645
301 TYR 305 ILE 1.893 0.251 1.642 1.642
212 THR 262 LEU 0.402 2.023 -1.621 1.621
75 LEU 302 ASN 1.046 2.666 -1.621 1.621
124 MET 257 ILE 0.000 1.616 -1.616 1.616
135 ILE 222 ILE 2.017 0.401 1.616 1.616
233 VAL 236 PHE 0.000 1.611 -1.611 1.611
28 LEU 289 VAL 0.000 1.604 -1.604 1.604
184 THR 187 TRP 0.000 1.600 -1.600 1.600
39 TYR 297 SER 1.111 2.709 -1.597 1.597
22 ASP 24 PHE 1.014 2.609 -1.595 1.595
199 PHE 203 ILE 4.090 2.497 1.592 1.592
114 PHE 207 CYS 0.000 1.590 -1.590 1.590
110 GLY 171 LEU 1.590 0.000 1.590 1.590
186 ASP 188 TRP 0.000 1.588 -1.588 1.588
11 ASP 19 ARG 2.420 0.849 1.571 1.571
236 PHE 244 HIS 0.000 1.545 -1.545 1.545
188 TRP 280 PRO 1.535 0.000 1.535 1.535
128 SER 218 SER 2.098 3.608 -1.510 1.510
39 TYR 43 ILE 4.216 2.720 1.496 1.496
135 ILE 225 LYS 0.122 1.616 -1.494 1.494
85 VAL 112 ALA 1.962 0.479 1.483 1.483
111 TRP 164 THR 6.869 5.389 1.480 1.480
305 ILE 306 TYR 1.469 0.000 1.469 1.469
163 TRP 206 PHE 7.042 8.509 -1.467 1.467
27 LYS 30 TRP 1.465 0.000 1.465 1.465
75 LEU 123 THR 2.196 0.742 1.453 1.453
226 VAL 248 MET 0.000 1.447 -1.447 1.447
114 PHE 203 ILE 0.000 1.444 -1.444 1.444
99 TRP 173 ASP 1.443 0.000 1.443 1.443
245 VAL 249 LYS 1.442 0.000 1.442 1.442
176 PRO 182 SER 3.268 1.831 1.437 1.437
186 ASP 200 ILE 0.000 1.424 -1.424 1.424
8 LEU 13 ARG 0.000 1.409 -1.409 1.409
26 SER 181 THR 0.000 1.407 -1.407 1.407
89 PHE 109 TYR 2.392 0.997 1.395 1.395
83 SER 88 PRO 0.000 1.395 -1.395 1.395
174 TYR 181 THR 1.391 0.000 1.391 1.391
167 PRO 185 LEU 0.000 1.382 -1.382 1.382
253 VAL 313 PHE 1.374 0.000 1.374 1.374
37 GLY 93 SER 1.370 0.000 1.370 1.370
23 PRO 176 PRO 0.000 1.367 -1.367 1.367
107 ARG 168 LEU 1.997 0.637 1.360 1.360
63 LYS 337 VAL 0.000 1.358 -1.358 1.358
89 PHE 92 ILE 1.353 0.000 1.353 1.353
179 PHE 285 ILE 0.000 1.352 -1.352 1.352
132 TYR 137 TYR 2.881 4.215 -1.334 1.334
61 ARG 336 THR 0.000 1.333 -1.333 1.333
27 LYS 285 ILE 0.000 1.330 -1.330 1.330
61 ARG 65 LEU 0.000 1.318 -1.318 1.318
104 ILE 108 TRP 1.306 0.000 1.306 1.306
78 CYS 116 PHE 3.677 4.982 -1.305 1.305
47 SER 299 ALA 5.506 4.205 1.301 1.301
93 SER 101 PHE 0.000 1.298 -1.298 1.298
137 TYR 140 TYR 1.955 0.658 1.298 1.298
127 VAL 306 TYR 1.294 0.000 1.294 1.294
121 LEU 207 CYS 2.884 1.593 1.291 1.291
257 ILE 306 TYR 1.834 3.121 -1.287 1.287
26 SER 98 ARG 0.000 1.279 -1.279 1.279
336 THR 338 THR 0.000 1.276 -1.276 1.276
205 PHE 206 PHE 3.865 5.130 -1.265 1.265
79 ASP 302 ASN 4.666 3.407 1.260 1.260
26 SER 28 LEU 0.000 1.258 -1.258 1.258
240 ILE 243 SER 1.256 0.000 1.256 1.256
171 LEU 189 LEU 0.000 1.246 -1.246 1.246
110 GLY 183 CYS 0.000 1.233 -1.233 1.233
253 VAL 306 TYR 0.000 1.233 -1.233 1.233
177 GLU 183 CYS 0.000 1.223 -1.223 1.223
294 LEU 301 TYR 0.000 1.223 -1.223 1.223
292 THR 296 LYS 0.470 1.691 -1.221 1.221
241 HIS 245 VAL 0.396 1.601 -1.204 1.204
28 LEU 179 PHE 0.000 1.199 -1.199 1.199
96 CYS 100 VAL 0.000 1.181 -1.181 1.181
222 ILE 251 THR 0.000 1.179 -1.179 1.179
70 ILE 150 TYR 2.616 1.437 1.179 1.179
122 ILE 211 PRO 0.000 1.164 -1.164 1.164
123 THR 156 ILE 1.596 2.754 -1.158 1.158
219 TYR 251 THR 0.000 1.151 -1.151 1.151
264 ALA 301 TYR 2.028 0.878 1.150 1.150
188 TRP 191 GLN 0.013 1.161 -1.149 1.149
144 LEU 149 ALA 1.148 0.000 1.148 1.148
139 SER 140 TYR 0.029 1.176 -1.147 1.147
74 ASN 157 TRP 5.784 4.641 1.143 1.143
106 CYS 173 ASP 1.142 0.000 1.142 1.142
34 LEU 95 PHE 0.000 1.140 -1.140 1.140
91 ILE 101 PHE 1.126 0.000 1.126 1.126
172 GLY 189 LEU 0.000 1.101 -1.101 1.101
163 TRP 202 ASN 0.563 1.661 -1.097 1.097
271 VAL 283 ILE 0.193 1.287 -1.094 1.094
51 ASN 303 PRO 4.348 5.438 -1.090 1.090
121 LEU 208 LEU 1.378 0.291 1.087 1.087
253 VAL 309 ILE 2.120 3.202 -1.082 1.082
99 TRP 101 PHE 4.306 3.225 1.081 1.081
66 ARG 335 HIS 0.000 1.072 -1.072 1.072
300 MET 304 ILE 0.000 1.060 -1.060 1.060
301 TYR 302 ASN 1.170 0.116 1.054 1.054
90 THR 182 SER 0.000 1.050 -1.050 1.050
111 TRP 171 LEU 1.049 0.000 1.049 1.049
89 PHE 108 TRP 0.000 1.044 -1.044 1.044
25 ALA 180 GLY 0.000 1.044 -1.044 1.044
92 ILE 98 ARG 1.038 0.000 1.038 1.038
17 TYR 281 ASP 1.037 0.000 1.037 1.037
29 SER 286 GLN 1.037 0.000 1.037 1.037
260 GLY 301 TYR 3.720 2.686 1.034 1.034
80 LEU 84 VAL 0.001 1.035 -1.034 1.034
106 CYS 183 CYS 6.552 7.573 -1.021 1.021
233 VAL 241 HIS 0.000 1.019 -1.019 1.019
219 TYR 254 ALA 3.792 4.805 -1.013 1.013
121 LEU 265 TRP 1.006 0.000 1.006 1.006
226 VAL 251 THR 0.998 0.000 0.998 0.998
127 VAL 131 ARG 1.324 0.328 0.996 0.996
250 LEU 335 HIS 0.000 0.988 -0.988 0.988
33 ASP 97 HIS 4.190 5.178 -0.988 0.988
275 SER 283 ILE 1.742 2.729 -0.986 0.986
43 ILE 300 MET 0.383 1.368 -0.984 0.984
44 GLY 83 SER 1.193 0.210 0.983 0.983
163 TRP 207 CYS 1.968 2.951 -0.983 0.983
171 LEU 186 ASP 0.982 0.000 0.982 0.982
16 HIS 177 GLU 0.000 0.981 -0.981 0.981
201 LEU 276 ALA 0.979 0.000 0.979 0.979
268 TYR 272 SER 3.067 4.043 -0.977 0.977
179 PHE 288 SER 0.000 0.968 -0.968 0.968
300 MET 301 TYR 0.000 0.965 -0.965 0.965
172 GLY 199 PHE 0.000 0.963 -0.963 0.963
204 LEU 277 PHE 0.000 0.957 -0.957 0.957
93 SER 100 VAL 0.000 0.954 -0.954 0.954
9 PRO 12 GLU 0.000 0.954 -0.954 0.954
99 TRP 105 GLY 3.874 2.926 0.948 0.948
106 CYS 171 LEU 0.947 0.000 0.947 0.947
136 CYS 222 ILE 0.238 1.181 -0.943 0.943
70 ILE 146 ARG 0.544 1.484 -0.940 0.940
89 PHE 110 GLY 0.937 0.000 0.937 0.937
206 PHE 211 PRO 1.997 2.922 -0.925 0.925
133 LEU 141 GLY 0.000 0.921 -0.921 0.921
187 TRP 200 ILE 2.321 1.409 0.912 0.912
216 VAL 262 LEU 0.919 0.007 0.911 0.911
175 VAL 176 PRO 0.107 1.017 -0.910 0.910
185 LEU 203 ILE 0.000 0.906 -0.906 0.906
56 TYR 57 MET 0.259 1.163 -0.904 0.904
74 ASN 153 LEU 3.811 2.914 0.897 0.897
71 MET 153 LEU 0.406 1.297 -0.891 0.891
135 ILE 251 THR 0.000 0.889 -0.889 0.889
100 VAL 101 PHE 1.762 2.640 -0.878 0.878
305 ILE 309 ILE 0.000 0.874 -0.874 0.874
75 LEU 306 TYR 1.418 0.548 0.870 0.870
54 VAL 306 TYR 0.000 0.869 -0.869 0.869
79 ASP 120 SER 2.990 2.124 0.866 0.866
54 VAL 76 ALA 0.000 0.863 -0.863 0.863
163 TRP 203 ILE 1.076 1.932 -0.856 0.856
121 LEU 211 PRO 1.076 1.930 -0.854 0.854
185 LEU 200 ILE 0.000 0.847 -0.847 0.847
106 CYS 172 GLY 0.843 0.000 0.843 0.843
202 ASN 206 PHE 1.079 1.922 -0.843 0.843
174 TYR 186 ASP 0.958 0.115 0.843 0.843
243 SER 247 GLU 0.910 0.071 0.839 0.839
131 ARG 222 ILE 0.972 1.810 -0.838 0.838
70 ILE 153 LEU 0.278 1.113 -0.834 0.834
98 ARG 100 VAL 0.000 0.820 -0.820 0.820
51 ASN 307 GLN 0.819 0.000 0.819 0.819
215 ILE 258 CYS 0.000 0.818 -0.818 0.818
279 ARG 282 SER 0.067 0.880 -0.813 0.813
352 GLU 353 TRP 0.813 0.000 0.813 0.813
199 PHE 200 ILE 0.000 0.812 -0.812 0.812
41 THR 95 PHE 0.000 0.811 -0.811 0.811
244 HIS 247 GLU 0.807 0.000 0.807 0.807
106 CYS 174 TYR 0.000 0.805 -0.805 0.805
126 ALA 152 CYS 0.000 0.802 -0.802 0.802
97 HIS 181 THR 0.924 0.123 0.801 0.801
118 CYS 207 CYS 1.056 0.257 0.799 0.799
246 LEU 337 VAL 0.000 0.795 -0.795 0.795
334 LEU 335 HIS 0.792 0.000 0.792 0.792
268 TYR 292 THR 2.988 3.776 -0.788 0.788
187 TRP 275 SER 0.000 0.784 -0.784 0.784
29 SER 32 ALA 0.000 0.777 -0.777 0.777
191 GLN 200 ILE 0.768 0.000 0.768 0.768
48 THR 83 SER 1.490 2.256 -0.766 0.766
187 TRP 204 LEU 0.000 0.766 -0.766 0.766
152 CYS 156 ILE 0.000 0.765 -0.765 0.765
55 LEU 73 ILE 1.059 1.821 -0.763 0.763
265 TRP 268 TYR 0.279 1.041 -0.762 0.762
68 ALA 130 ASP 0.748 0.000 0.748 0.748
40 LEU 43 ILE 0.000 0.747 -0.747 0.747
128 SER 258 CYS 0.000 0.733 -0.733 0.733
178 PRO 288 SER 0.000 0.733 -0.733 0.733
117 GLY 261 PHE 0.000 0.726 -0.726 0.726
66 ARG 314 ALA 0.725 0.000 0.725 0.725
197 GLN 277 PHE 0.000 0.718 -0.718 0.718
127 VAL 254 ALA 0.000 0.716 -0.716 0.716
166 MET 169 VAL 0.000 0.715 -0.715 0.715
208 LEU 268 TYR 0.715 0.000 0.715 0.715
22 ASP 25 ALA 0.424 1.127 -0.703 0.703
66 ARG 69 GLU 8.794 9.495 -0.701 0.701
68 ALA 134 LYS 0.701 0.000 0.701 0.701
223 ILE 254 ALA 0.700 0.000 0.700 0.700
121 LEU 215 ILE 0.166 0.864 -0.698 0.698
223 ILE 227 LYS 0.000 0.694 -0.694 0.694
264 ALA 298 ALA 0.191 0.880 -0.689 0.689
262 LEU 267 PRO 0.685 0.003 0.682 0.682
114 PHE 163 TRP 0.000 0.682 -0.682 0.682
284 PRO 286 GLN 0.091 0.773 -0.682 0.682
78 CYS 120 SER 2.864 3.545 -0.681 0.681
82 ILE 116 PHE 4.245 4.913 -0.668 0.668
125 THR 211 PRO 3.544 4.211 -0.667 0.667
306 TYR 311 TYR 0.666 0.000 0.666 0.666
75 LEU 257 ILE 0.000 0.664 -0.664 0.664
23 PRO 103 TRP 0.000 0.664 -0.664 0.664
302 ASN 306 TYR 1.136 0.473 0.663 0.663
28 LEU 285 ILE 0.000 0.662 -0.662 0.662
132 TYR 221 LYS 2.030 2.691 -0.661 0.661
246 LEU 313 PHE 0.660 0.000 0.660 0.660
189 LEU 197 GLN 0.000 0.660 -0.660 0.660
132 TYR 218 SER 3.582 2.923 0.659 0.659
25 ALA 98 ARG 0.000 0.655 -0.655 0.655
223 ILE 251 THR 0.653 0.000 0.653 0.653
234 ALA 244 HIS 0.647 0.000 0.647 0.647
273 VAL 277 PHE 1.272 0.626 0.646 0.646
226 VAL 250 LEU 0.644 0.000 0.644 0.644
302 ASN 307 GLN 0.641 0.000 0.641 0.641
121 LEU 261 PHE 1.823 2.456 -0.634 0.634
219 TYR 306 TYR 0.632 0.000 0.632 0.632
173 ASP 182 SER 0.629 0.000 0.629 0.629
340 VAL 342 LYS 0.000 0.627 -0.627 0.627
135 ILE 250 LEU 0.625 0.000 0.625 0.625
135 ILE 247 GLU 0.000 0.624 -0.624 0.624
343 SER 344 SER 0.616 0.000 0.616 0.616
118 CYS 122 ILE 1.052 0.439 0.613 0.613
136 CYS 225 LYS 1.110 1.716 -0.605 0.605
136 CYS 221 LYS 0.650 1.250 -0.600 0.600
159 TYR 206 PHE 4.905 5.503 -0.598 0.598
36 ALA 94 CYS 0.000 0.594 -0.594 0.594
47 SER 300 MET 2.029 2.612 -0.583 0.583
247 GLU 250 LEU 0.000 0.582 -0.582 0.582
74 ASN 78 CYS 1.122 0.546 0.577 0.577
81 GLY 86 GLY 0.000 0.575 -0.575 0.575
223 ILE 255 MET 0.649 1.224 -0.574 0.574
43 ILE 297 SER 2.195 1.623 0.572 0.572
43 ILE 293 LEU 0.572 0.000 0.572 0.572
92 ILE 100 VAL 0.000 0.566 -0.566 0.566
140 TYR 142 VAL 0.566 0.000 0.566 0.566
51 ASN 299 ALA 1.604 2.168 -0.564 0.564
225 LYS 232 GLU 0.000 0.564 -0.564 0.564
32 ALA 286 GLN 0.564 0.000 0.564 0.564
191 GLN 277 PHE 0.000 0.561 -0.561 0.561
48 THR 80 LEU 1.690 2.251 -0.561 0.561
118 CYS 159 TYR 0.159 0.719 -0.560 0.560
178 PRO 285 ILE 0.000 0.560 -0.560 0.560
114 PHE 185 LEU 0.596 0.037 0.559 0.559
120 SER 302 ASN 0.557 0.000 0.557 0.557
253 VAL 305 ILE 0.000 0.556 -0.556 0.556
23 PRO 180 GLY 0.000 0.553 -0.553 0.553
201 LEU 277 PHE 2.691 2.139 0.552 0.552
47 SER 79 ASP 1.088 0.538 0.550 0.550
82 ILE 117 GLY 1.852 1.303 0.549 0.549
204 LEU 273 VAL 1.805 1.260 0.545 0.545
191 GLN 275 SER 2.367 2.908 -0.541 0.541
55 LEU 77 VAL 0.641 1.181 -0.540 0.540
133 LEU 137 TYR 0.548 0.011 0.537 0.537
85 VAL 89 PHE 0.535 0.000 0.535 0.535
170 GLY 185 LEU 0.531 0.000 0.531 0.531
54 VAL 72 THR 0.000 0.531 -0.531 0.531
249 LYS 309 ILE 0.000 0.523 -0.523 0.523
233 VAL 240 ILE 0.523 0.000 0.523 0.523
251 THR 255 MET 0.516 0.000 0.516 0.516
228 SER 229 SER 0.290 0.802 -0.513 0.513
133 LEU 144 LEU 0.000 0.512 -0.512 0.512
91 ILE 100 VAL 0.508 0.000 0.508 0.508
37 GLY 91 ILE 0.000 0.506 -0.506 0.506
187 TRP 188 TRP 0.000 0.505 -0.505 0.505
114 PHE 118 CYS 0.000 0.501 -0.501 0.501
59 SER 60 ARG 0.060 0.561 -0.501 0.501
24 PHE 106 CYS 0.000 0.493 -0.493 0.493
55 LEU 76 ALA 0.954 1.444 -0.489 0.489
36 ALA 293 LEU 1.255 0.768 0.487 0.487
51 ASN 80 LEU 0.916 0.432 0.485 0.485
271 VAL 288 SER 1.009 0.529 0.480 0.480
65 LEU 70 ILE 0.565 1.042 -0.477 0.477
81 GLY 116 PHE 6.110 6.586 -0.476 0.476
217 PHE 221 LYS 4.002 3.527 0.475 0.475
205 PHE 210 LEU 3.184 3.655 -0.472 0.472
22 ASP 23 PRO 1.501 1.972 -0.470 0.470
261 PHE 301 TYR 0.463 0.000 0.463 0.463
69 GLU 335 HIS 0.000 0.462 -0.462 0.462
257 ILE 305 ILE 1.939 2.399 -0.461 0.461
347 LEU 349 ILE 0.460 0.000 0.460 0.460
74 ASN 123 THR 3.138 2.680 0.458 0.458
36 ALA 289 VAL 0.455 0.000 0.455 0.455
128 SER 306 TYR 0.455 0.000 0.455 0.455
82 ILE 120 SER 0.453 0.000 0.453 0.453
107 ARG 172 GLY 0.452 0.000 0.452 0.452
40 LEU 296 LYS 1.249 0.797 0.452 0.452
283 ILE 287 LEU 1.019 0.570 0.449 0.449
75 LEU 124 MET 1.254 0.806 0.448 0.448
265 TRP 298 ALA 0.878 1.326 -0.448 0.448
85 VAL 116 PHE 0.812 0.365 0.446 0.446
79 ASP 82 ILE 0.466 0.021 0.445 0.445
39 TYR 40 LEU 0.000 0.440 -0.440 0.440
165 THR 166 MET 0.438 0.000 0.438 0.438
77 VAL 157 TRP 0.302 0.739 -0.437 0.437
175 VAL 181 THR 0.433 0.000 0.433 0.433
28 LEU 32 ALA 0.000 0.430 -0.430 0.430
87 LYS 91 ILE 0.000 0.428 -0.428 0.428
308 VAL 312 LYS 0.000 0.425 -0.425 0.425
304 ILE 308 VAL 0.000 0.423 -0.423 0.423
40 LEU 94 CYS 0.000 0.416 -0.416 0.416
48 THR 84 VAL 0.000 0.415 -0.415 0.415
98 ARG 180 GLY 0.000 0.413 -0.413 0.413
145 LYS 147 LYS 0.000 0.413 -0.413 0.413
261 PHE 298 ALA 0.000 0.409 -0.409 0.409
12 GLU 19 ARG 0.408 0.000 0.408 0.408
47 SER 51 ASN 1.707 1.300 0.407 0.407
118 CYS 164 THR 0.000 0.402 -0.402 0.402
67 PRO 145 LYS 0.245 0.638 -0.393 0.393
25 ALA 97 HIS 0.000 0.392 -0.392 0.392
271 VAL 287 LEU 1.120 0.729 0.391 0.391
111 TRP 115 PHE 3.112 2.724 0.387 0.387
25 ALA 179 PHE 0.000 0.386 -0.386 0.386
17 TYR 103 TRP 0.000 0.384 -0.384 0.384
3 LEU 5 HIS 0.000 0.384 -0.384 0.384
95 PHE 98 ARG 0.384 0.000 0.384 0.384
92 ILE 96 CYS 0.000 0.382 -0.382 0.382
189 LEU 199 PHE 0.000 0.381 -0.381 0.381
51 ASN 79 ASP 4.078 4.458 -0.379 0.379
120 SER 261 PHE 0.000 0.379 -0.379 0.379
119 GLY 156 ILE 0.684 1.063 -0.379 0.379
90 THR 99 TRP 0.000 0.377 -0.377 0.377
115 PHE 160 ALA 3.507 3.135 0.372 0.372
112 ALA 116 PHE 0.499 0.128 0.371 0.371
122 ILE 156 ILE 1.667 2.037 -0.371 0.371
294 LEU 297 SER 0.000 0.370 -0.370 0.370
250 LEU 317 GLN 0.366 0.000 0.366 0.366
68 ALA 250 LEU 0.000 0.365 -0.365 0.365
53 TYR 54 VAL 0.355 0.000 0.355 0.355
58 SER 73 ILE 2.412 2.766 -0.354 0.354
10 GLN 13 ARG 0.000 0.345 -0.345 0.345
237 ASP 238 SER 0.340 0.000 0.340 0.340
164 THR 165 THR 0.000 0.339 -0.339 0.339
15 PRO 188 TRP 0.000 0.332 -0.332 0.332
190 ALA 277 PHE 0.000 0.331 -0.331 0.331
252 LYS 256 LEU 0.000 0.330 -0.330 0.330
79 ASP 299 ALA 5.709 5.381 0.328 0.328
204 LEU 209 LEU 3.977 4.303 -0.326 0.326
132 TYR 222 ILE 2.771 3.097 -0.326 0.326
256 LEU 309 ILE 0.547 0.872 -0.325 0.325
215 ILE 262 LEU 0.000 0.320 -0.320 0.320
120 SER 124 MET 0.212 0.531 -0.319 0.319
136 CYS 137 TYR 1.038 1.353 -0.315 0.315
65 LEU 73 ILE 1.404 1.089 0.315 0.315
134 LYS 144 LEU 0.000 0.313 -0.313 0.313
266 ILE 270 VAL 0.505 0.194 0.311 0.311
27 LYS 180 GLY 0.000 0.311 -0.311 0.311
159 TYR 207 CYS 0.058 0.367 -0.309 0.309
337 VAL 339 THR 0.309 0.000 0.309 0.309
50 GLY 307 GLN 0.308 0.000 0.308 0.308
252 LYS 255 MET 0.306 0.000 0.306 0.306
153 LEU 156 ILE 0.000 0.306 -0.306 0.306
16 HIS 20 ASP 0.000 0.306 -0.306 0.306
39 TYR 293 LEU 3.902 4.206 -0.304 0.304
146 ARG 150 TYR 2.466 2.769 -0.303 0.303
78 CYS 157 TRP 1.170 0.870 0.300 0.300
83 SER 299 ALA 0.000 0.300 -0.300 0.300
284 PRO 287 LEU 0.480 0.780 -0.299 0.299
71 MET 127 VAL 1.148 1.447 -0.298 0.298
166 MET 172 GLY 0.000 0.295 -0.295 0.295
309 ILE 313 PHE 1.044 1.338 -0.294 0.294
173 ASP 184 THR 0.000 0.294 -0.294 0.294
40 LEU 93 SER 0.290 0.000 0.290 0.290
67 PRO 149 ALA 1.338 1.049 0.289 0.289
144 LEU 148 HIS 0.734 0.446 0.288 0.288
340 VAL 341 ARG 0.288 0.000 0.288 0.288
107 ARG 169 VAL 0.283 0.000 0.283 0.283
89 PHE 296 LYS 0.283 0.000 0.283 0.283
167 PRO 203 ILE 0.281 0.000 0.281 0.281
40 LEU 89 PHE 0.279 0.000 0.279 0.279
14 LEU 18 LEU 0.978 0.700 0.278 0.278
283 ILE 284 PRO 0.896 0.622 0.274 0.274
68 ALA 131 ARG 0.000 0.263 -0.263 0.263
124 MET 215 ILE 1.286 1.549 -0.263 0.263
103 TRP 175 VAL 0.000 0.262 -0.262 0.262
78 CYS 119 GLY 1.934 1.674 0.260 0.260
273 VAL 278 GLY 0.000 0.260 -0.260 0.260
283 ILE 288 SER 0.000 0.259 -0.259 0.259
42 ILE 46 LEU 0.929 0.671 0.258 0.258
285 ILE 289 VAL 0.000 0.256 -0.256 0.256
106 CYS 184 THR 0.255 0.000 0.255 0.255
264 ALA 265 TRP 0.473 0.220 0.253 0.253
288 SER 289 VAL 0.176 0.426 -0.250 0.250
205 PHE 209 LEU 0.244 0.000 0.244 0.244
182 SER 292 THR 0.000 0.244 -0.244 0.244
129 LEU 218 SER 1.734 1.977 -0.243 0.243
185 LEU 199 PHE 0.000 0.242 -0.242 0.242
74 ASN 156 ILE 0.250 0.491 -0.241 0.241
23 PRO 24 PHE 0.058 0.297 -0.239 0.239
197 GLN 201 LEU 0.000 0.239 -0.239 0.239
39 TYR 294 LEU 0.000 0.236 -0.236 0.236
54 VAL 58 SER 0.400 0.164 0.236 0.236
96 CYS 98 ARG 0.000 0.231 -0.231 0.231
173 ASP 175 VAL 0.000 0.228 -0.228 0.228
125 THR 129 LEU 0.226 0.000 0.226 0.226
121 LEU 125 THR 0.000 0.226 -0.226 0.226
209 LEU 269 ALA 0.224 0.000 0.224 0.224
263 ILE 294 LEU 0.348 0.569 -0.221 0.221
129 LEU 214 VAL 1.865 2.085 -0.221 0.221
290 VAL 294 LEU 0.220 0.000 0.220 0.220
267 PRO 291 PRO 3.064 3.284 -0.220 0.220
92 ILE 183 CYS 0.219 0.000 0.219 0.219
33 ASP 96 CYS 0.219 0.000 0.219 0.219
71 MET 152 CYS 1.187 1.404 -0.218 0.218
163 TRP 199 PHE 0.216 0.000 0.216 0.216
135 ILE 226 VAL 0.154 0.368 -0.214 0.214
40 LEU 87 LYS 0.000 0.214 -0.214 0.214
110 GLY 184 THR 0.000 0.211 -0.211 0.211
306 TYR 307 GLN 0.206 0.000 0.206 0.206
40 LEU 293 LEU 1.827 1.624 0.204 0.204
208 LEU 212 THR 0.268 0.472 -0.204 0.204
47 SER 87 LYS 0.000 0.202 -0.202 0.202
321 LEU 324 THR 0.202 0.000 0.202 0.202
128 SER 222 ILE 0.068 0.266 -0.198 0.198
114 PHE 167 PRO 0.198 0.000 0.198 0.198
271 VAL 275 SER 0.000 0.197 -0.197 0.197
165 THR 169 VAL 0.000 0.197 -0.197 0.197
333 ARG 336 THR 0.000 0.197 -0.197 0.197
87 LYS 88 PRO 0.949 0.753 0.196 0.196
67 PRO 146 ARG 0.371 0.567 -0.196 0.196
65 LEU 69 GLU 1.478 1.674 -0.196 0.196
191 GLN 279 ARG 0.000 0.191 -0.191 0.191
266 ILE 267 PRO 1.151 1.342 -0.191 0.191
64 LYS 146 ARG 6.453 6.643 -0.190 0.190
271 VAL 291 PRO 0.870 0.681 0.189 0.189
175 VAL 185 LEU 0.000 0.187 -0.187 0.187
245 VAL 248 MET 0.186 0.000 0.186 0.186
66 ARG 247 GLU 0.000 0.186 -0.186 0.186
229 SER 247 GLU 0.181 0.000 0.181 0.181
82 ILE 299 ALA 0.181 0.000 0.181 0.181
131 ARG 254 ALA 0.000 0.179 -0.179 0.179
219 TYR 258 CYS 2.579 2.402 0.177 0.177
58 SER 65 LEU 0.000 0.176 -0.176 0.176
16 HIS 281 ASP 0.000 0.175 -0.175 0.175
126 ALA 156 ILE 0.451 0.275 0.175 0.175
70 ILE 149 ALA 0.309 0.484 -0.175 0.175
132 TYR 133 LEU 0.325 0.150 0.175 0.175
78 CYS 123 THR 0.174 0.000 0.174 0.174
97 HIS 183 CYS 0.172 0.000 0.172 0.172
135 ILE 136 CYS 0.033 0.206 -0.172 0.172
323 ALA 324 THR 0.000 0.172 -0.172 0.172
132 TYR 136 CYS 2.853 2.687 0.165 0.165
206 PHE 210 LEU 0.267 0.432 -0.164 0.164
335 HIS 337 VAL 0.164 0.000 0.164 0.164
25 ALA 27 LYS 0.000 0.162 -0.162 0.162
171 LEU 184 THR 0.161 0.000 0.161 0.161
194 VAL 198 VAL 0.243 0.083 0.160 0.160
125 THR 215 ILE 3.832 3.673 0.160 0.160
274 TRP 283 ILE 5.404 5.563 -0.158 0.158
101 PHE 106 CYS 0.000 0.157 -0.157 0.157
184 THR 185 LEU 0.000 0.155 -0.155 0.155
114 PHE 268 TYR 0.154 0.000 0.154 0.154
249 LYS 335 HIS 0.000 0.152 -0.152 0.152
200 ILE 204 LEU 0.793 0.641 0.152 0.152
246 LEU 317 GLN 0.149 0.000 0.149 0.149
66 ARG 67 PRO 0.949 0.801 0.148 0.148
235 HIS 236 PHE 0.146 0.000 0.146 0.146
17 TYR 18 LEU 2.552 2.407 0.145 0.145
150 TYR 153 LEU 0.139 0.281 -0.141 0.141
285 ILE 286 GLN 0.000 0.141 -0.141 0.141
190 ALA 193 SER 0.137 0.000 0.137 0.137
52 GLY 80 LEU 0.000 0.135 -0.135 0.135
116 PHE 157 TRP 1.574 1.439 0.135 0.135
267 PRO 294 LEU 0.454 0.589 -0.135 0.135
71 MET 123 THR 1.567 1.700 -0.133 0.133
172 GLY 182 SER 0.132 0.000 0.132 0.132
122 ILE 160 ALA 0.131 0.000 0.131 0.131
173 ASP 174 TYR 0.000 0.131 -0.131 0.131
36 ALA 93 SER 0.131 0.000 0.131 0.131
280 PRO 281 ASP 0.320 0.192 0.129 0.129
202 ASN 207 CYS 0.082 0.210 -0.128 0.128
55 LEU 80 LEU 0.481 0.608 -0.127 0.127
122 ILE 159 TYR 2.826 2.951 -0.126 0.126
174 TYR 180 GLY 0.126 0.000 0.126 0.126
203 ILE 207 CYS 0.460 0.334 0.126 0.126
51 ASN 302 ASN 0.000 0.124 -0.124 0.124
238 SER 239 ARG 0.122 0.000 0.122 0.122
346 VAL 347 LEU 1.827 1.949 -0.122 0.122
285 ILE 288 SER 0.030 0.151 -0.121 0.121
131 ARG 253 VAL 0.121 0.000 0.121 0.121
268 TYR 291 PRO 3.780 3.661 0.119 0.119
345 ALA 346 VAL 0.336 0.219 0.117 0.117
167 PRO 171 LEU 0.117 0.000 0.117 0.117
200 ILE 272 SER 0.116 0.000 0.116 0.116
289 VAL 293 LEU 0.771 0.886 -0.115 0.115
143 TRP 144 LEU 0.000 0.115 -0.115 0.115
90 THR 94 CYS 0.134 0.248 -0.114 0.114
261 PHE 266 ILE 0.114 0.000 0.114 0.114
298 ALA 302 ASN 0.111 0.000 0.111 0.111
82 ILE 113 GLY 0.000 0.109 -0.109 0.109
215 ILE 219 TYR 0.986 1.094 -0.108 0.108
268 TYR 295 ALA 0.983 0.879 0.104 0.104
217 PHE 218 SER 0.000 0.103 -0.103 0.103
41 THR 45 ILE 0.588 0.486 0.102 0.102
175 VAL 182 SER 0.000 0.101 -0.101 0.101
253 VAL 257 ILE 0.644 0.544 0.101 0.101
105 GLY 110 GLY 0.101 0.000 0.101 0.101
175 VAL 177 GLU 0.100 0.000 0.100 0.100
133 LEU 138 LEU 0.476 0.574 -0.098 0.098
80 LEU 85 VAL 0.000 0.097 -0.097 0.097
79 ASP 298 ALA 0.096 0.000 0.096 0.096
103 TRP 174 TYR 0.000 0.095 -0.095 0.095
94 CYS 95 PHE 0.095 0.000 0.095 0.095
67 PRO 134 LYS 0.000 0.095 -0.095 0.095
133 LEU 140 TYR 0.000 0.094 -0.094 0.094
111 TRP 112 ALA 0.569 0.477 0.092 0.092
14 LEU 15 PRO 0.678 0.770 -0.092 0.092
282 SER 283 ILE 0.373 0.282 0.091 0.091
125 THR 214 VAL 1.385 1.476 -0.090 0.090
46 LEU 300 MET 2.444 2.534 -0.090 0.090
200 ILE 277 PHE 0.000 0.089 -0.089 0.089
187 TRP 203 ILE 0.000 0.087 -0.087 0.087
115 PHE 161 SER 4.518 4.432 0.085 0.085
8 LEU 9 PRO 1.179 1.094 0.085 0.085
205 PHE 211 PRO 0.370 0.454 -0.085 0.085
279 ARG 280 PRO 0.686 0.602 0.084 0.084
108 TRP 112 ALA 0.000 0.082 -0.082 0.082
249 LYS 253 VAL 0.000 0.078 -0.078 0.078
290 VAL 291 PRO 1.198 1.274 -0.076 0.076
306 TYR 334 LEU 0.000 0.076 -0.076 0.076
91 ILE 95 PHE 1.457 1.382 0.075 0.075
74 ASN 119 GLY 0.043 0.117 -0.075 0.075
101 PHE 109 TYR 0.075 0.000 0.075 0.075
71 MET 156 ILE 0.452 0.381 0.072 0.072
108 TRP 111 TRP 1.657 1.728 -0.071 0.071
264 ALA 295 ALA 3.637 3.567 0.071 0.071
198 VAL 202 ASN 0.825 0.756 0.068 0.068
30 TRP 96 CYS 0.000 0.068 -0.068 0.068
302 ASN 303 PRO 0.882 0.949 -0.068 0.068
128 SER 215 ILE 2.580 2.645 -0.065 0.065
240 ILE 242 SER 0.064 0.000 0.064 0.064
64 LYS 69 GLU 0.125 0.061 0.064 0.064
47 SER 52 GLY 0.187 0.123 0.064 0.064
84 VAL 85 VAL 0.000 0.063 -0.063 0.063
43 ILE 48 THR 0.062 0.000 0.062 0.062
119 GLY 160 ALA 0.847 0.791 0.057 0.057
75 LEU 120 SER 3.018 3.074 -0.057 0.057
26 SER 180 GLY 0.000 0.056 -0.056 0.056
166 MET 167 PRO 0.877 0.822 0.055 0.055
47 SER 303 PRO 0.000 0.054 -0.054 0.054
45 ILE 49 PHE 1.278 1.332 -0.054 0.054
189 LEU 200 ILE 0.000 0.054 -0.054 0.054
261 PHE 262 LEU 0.079 0.132 -0.053 0.053
15 PRO 18 LEU 0.626 0.573 0.053 0.053
225 LYS 228 SER 0.481 0.429 0.052 0.052
259 ALA 263 ILE 0.083 0.033 0.050 0.050
130 ASP 134 LYS 7.018 6.968 0.050 0.050
71 MET 149 ALA 2.051 2.003 0.049 0.049
53 TYR 57 MET 5.767 5.815 -0.049 0.049
219 TYR 222 ILE 0.975 1.023 -0.048 0.048
328 SER 329 LEU 0.048 0.000 0.048 0.048
77 VAL 116 PHE 0.112 0.064 0.048 0.048
75 LEU 79 ASP 1.663 1.711 -0.048 0.048
237 ASP 240 ILE 0.265 0.218 0.047 0.047
212 THR 216 VAL 0.179 0.225 -0.045 0.045
264 ALA 291 PRO 0.349 0.304 0.045 0.045
121 LEU 212 THR 0.000 0.045 -0.045 0.045
216 VAL 220 VAL 0.375 0.330 0.045 0.045
72 THR 127 VAL 0.044 0.000 0.044 0.044
325 LYS 329 LEU 0.043 0.000 0.043 0.043
40 LEU 90 THR 1.676 1.719 -0.043 0.043
165 THR 168 LEU 0.000 0.040 -0.040 0.040
204 LEU 208 LEU 0.323 0.284 0.039 0.039
274 TRP 287 LEU 0.000 0.037 -0.037 0.037
222 ILE 226 VAL 0.231 0.195 0.036 0.036
43 ILE 296 LYS 1.249 1.285 -0.036 0.036
26 SER 27 LYS 0.033 0.000 0.033 0.033
214 VAL 218 SER 0.335 0.305 0.030 0.030
15 PRO 17 TYR 5.328 5.299 0.029 0.029
203 ILE 208 LEU 0.556 0.586 -0.029 0.029
118 CYS 160 ALA 1.350 1.379 -0.028 0.028
11 ASP 14 LEU 0.000 0.028 -0.028 0.028
210 LEU 211 PRO 1.319 1.291 0.027 0.027
45 ILE 50 GLY 0.000 0.025 -0.025 0.025
106 CYS 111 TRP 0.025 0.000 0.025 0.025
246 LEU 250 LEU 0.000 0.025 -0.025 0.025
47 SER 83 SER 3.167 3.191 -0.024 0.024
51 ASN 75 LEU 0.023 0.000 0.023 0.023
56 TYR 59 SER 0.077 0.099 -0.022 0.022
160 ALA 165 THR 0.000 0.021 -0.021 0.021
61 ARG 66 ARG 0.019 0.000 0.019 0.019
29 SER 30 TRP 0.018 0.000 0.018 0.018
210 LEU 214 VAL 0.157 0.173 -0.017 0.017
246 LEU 335 HIS 0.000 0.017 -0.017 0.017
117 GLY 265 TRP 0.062 0.078 -0.016 0.016
78 CYS 79 ASP 0.016 0.000 0.016 0.016
302 ASN 305 ILE 0.000 0.015 -0.015 0.015
129 LEU 132 TYR 0.000 0.015 -0.015 0.015
134 LYS 135 ILE 0.000 0.014 -0.014 0.014
79 ASP 303 PRO 0.012 0.000 0.012 0.012
17 TYR 176 PRO 0.000 0.012 -0.012 0.012
53 TYR 56 TYR 0.000 0.011 -0.011 0.011
34 LEU 93 SER 0.010 0.000 0.010 0.010
71 MET 126 ALA 0.010 0.000 0.010 0.010
73 ILE 77 VAL 0.113 0.122 -0.009 0.009
206 PHE 207 CYS 0.000 0.009 -0.009 0.009
89 PHE 105 GLY 0.000 0.007 -0.007 0.007
200 ILE 276 ALA 0.418 0.413 0.005 0.005
88 PRO 89 PHE 0.000 0.003 -0.003 0.003
17 TYR 188 TRP 0.002 0.000 0.002 0.002
34 LEU 38 PHE 0.000 0.001 -0.001 0.001
148 HIS 151 ILE 0.000 0.001 -0.001 0.001
103 TRP 106 CYS 0.000 0.001 -0.001 0.001
123 THR 127 VAL 0.100 0.101 -0.000 0.000

RRCS change distribution

-0.42
Mean ΔRRCS
2.40
Std Dev
-0.18
Median

Magnitude classification

49
High (|Δ| ≥ 5.0)
42
Medium (3.4 ≤ |Δ| < 5.0)
756
Low (|Δ| < 3.4)

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| ≥ 3.41, 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