GPCompaRe

PAR2

Gene F2RL1 Family Proteinase-activated receptors Ligand type Peptide receptors UniProt P55085
776
Total Contact Pairs
77
Above-threshold changes
12.88
Max Increase
-11.21
Max Decrease

Interactive snake plot

GPCRdb-style topology. Use the view buttons to recolor residues by data layer. Toggle contact links to overlay above-threshold residue-residue contacts. Click ICL or ECL labels to expand or collapse loop regions.

Red: stronger in active. Blue: stronger in inactive.

ICL1 T104 T104 T K105 K105 K K106 K106 K K107 K107 K ICL1ECL1 G138 G138 G N139 N139 N N140 23.49x49 N140 23.49x49 N W141 23.50x50 W141 23.50x50 W I142 23.51x51 I142 23.51x51 I Y143 23.52x52 Y143 23.52x52 Y ECL1ICL2 P180 34.50x50 P180 34.50x50 P M181 34.51x51 M181 34.51x51 M G182 34.52x52 G182 34.52x52 G H183 34.53x53 H183 34.53x53 H S184 34.54x54 S184 34.54x54 S R185 34.55x55 R185 34.55x55 R K186 34.56x56 K186 34.56x56 K ICL2ECL2 V212 V212 V K213 K213 K Q214 Q214 Q T215 T215 T I216 I216 I F217 F217 F I218 I218 I P219 P219 P A220 A220 A L221 L221 L N222 N222 N I223 I223 I T224 T224 T T225 T225 T C226 45.50x50 C226 45.50x50 C H227 45.51x51 H227 45.51x51 H D228 45.52x52 D228 45.52x52 D V229 V229 V L230 L230 L P231 P231 P E232 E232 E Q233 Q233 Q L234 L234 L ECL2ICL3 A273 A273 A M274 M274 M D275 D275 D ICL3ECL3 G318 G318 G Q319 Q319 Q S320 S320 S H321 H321 H ECL3N-term M1 M1 M R2 R2 R S3 S3 S P4 P4 P S5 S5 S A6 A6 A A7 A7 A W8 W8 W L9 L9 L L10 L10 L G11 G11 G A12 A12 A A13 A13 A I14 I14 I L15 L15 L L16 L16 L A17 A17 A A18 A18 A S19 S19 S L20 L20 L S21 S21 S C22 C22 C S23 S23 S G24 G24 G T25 T25 T I26 I26 I Q27 Q27 Q G28 G28 G T29 T29 T N30 N30 N R31 R31 R S32 S32 S S33 S33 S K34 K34 K G35 G35 G R36 R36 R S37 S37 S L38 L38 L I39 I39 I G40 G40 G K41 K41 K V42 V42 V D43 D43 D G44 G44 G T45 T45 T S46 S46 S H47 H47 H V48 V48 V T49 T49 T G50 G50 G K51 K51 K G52 G52 G V53 V53 V T54 T54 T V55 V55 V E56 E56 E T57 T57 T V58 V58 V F59 F59 F S60 S60 S V61 V61 V D62 D62 D E63 E63 E F64 F64 F S65 S65 S A66 A66 A S67 S67 S V68 V68 V L69 L69 L T70 T70 T N-termC-term S363 S363 S V364 V364 V R365 R365 R T366 T366 T V367 V367 V K368 K368 K Q369 Q369 Q M370 M370 M Q371 Q371 Q V372 V372 V S373 S373 S L374 L374 L T375 T375 T S376 S376 S K377 K377 K K378 K378 K H379 H379 H S380 S380 S R381 R381 R K382 K382 K S383 S383 S S384 S384 S S385 S385 S Y386 Y386 Y S387 S387 S S388 S388 S S389 S389 S S390 S390 S T391 T391 T T392 T392 T V393 V393 V K394 K394 K T395 T395 T S396 S396 S Y397 Y397 Y C-term G71 1.28x28 G71 1.28x28 G K72 1.29x29 K72 1.29x29 K L73 1.30x30 L73 1.30x30 L T74 1.31x31 T74 1.31x31 T T75 1.32x32 T75 1.32x32 T V76 1.33x33 V76 1.33x33 V F77 1.34x34 F77 1.34x34 F L78 1.35x35 L78 1.35x35 L P79 1.36x36 P79 1.36x36 P I80 1.37x37 I80 1.37x37 I V81 1.38x38 V81 1.38x38 V Y82 1.39x39 Y82 1.39x39 Y T83 1.40x40 T83 1.40x40 T I84 1.41x41 I84 1.41x41 I V85 1.42x42 V85 1.42x42 V F86 1.43x43 F86 1.43x43 F V87 1.44x44 V87 1.44x44 V V88 1.45x45 V88 1.45x45 V G89 1.46x46 G89 1.46x46 G L90 1.47x47 L90 1.47x47 L P91 1.48x48 P91 1.48x48 P S92 1.49x49 S92 1.49x49 S N93 1.50x50 N93 1.50x50 N G94 1.51x51 G94 1.51x51 G M95 1.52x52 M95 1.52x52 M A96 1.53x53 A96 1.53x53 A L97 1.54x54 L97 1.54x54 L W98 1.55x55 W98 1.55x55 W V99 1.56x56 V99 1.56x56 V F100 1.57x57 F100 1.57x57 F L101 1.58x58 L101 1.58x58 L F102 1.59x59 F102 1.59x59 F R103 1.60x60 R103 1.60x60 R H108 2.37x37 H108 2.37x37 H P109 2.38x38 P109 2.38x38 P A110 2.39x39 A110 2.39x39 A V111 2.40x40 V111 2.40x40 V I112 2.41x41 I112 2.41x41 I Y113 2.42x42 Y113 2.42x42 Y M114 2.43x43 M114 2.43x43 M A115 2.44x44 A115 2.44x44 A N116 2.45x45 N116 2.45x45 N L117 2.46x46 L117 2.46x46 L A118 2.47x47 A118 2.47x47 A L119 2.48x48 L119 2.48x48 L A120 2.49x49 A120 2.49x49 A D121 2.50x50 D121 2.50x50 D L122 2.51x51 L122 2.51x51 L L123 2.52x52 L123 2.52x52 L S124 2.53x53 S124 2.53x53 S V125 2.54x54 V125 2.54x54 V I126 2.55x55 I126 2.55x55 I W127 2.56x56 W127 2.56x56 W F128 2.57x57 F128 2.57x57 F P129 2.58x58 P129 2.58x58 P L130 2.59x59 L130 2.59x59 L K131 2.60x60 K131 2.60x60 K I132 2.61x61 I132 2.61x61 I A133 2.62x62 A133 2.62x62 A Y134 2.63x63 Y134 2.63x63 Y H135 2.64x64 H135 2.64x64 H I136 2.65x65 I136 2.65x65 I H137 2.66x66 H137 2.66x66 H G144 3.21x21 G144 3.21x21 G E145 3.22x22 E145 3.22x22 E A146 3.23x23 A146 3.23x23 A L147 3.24x24 L147 3.24x24 L C148 3.25x25 C148 3.25x25 C N149 3.26x26 N149 3.26x26 N V150 3.27x27 V150 3.27x27 V L151 3.28x28 L151 3.28x28 L I152 3.29x29 I152 3.29x29 I G153 3.30x30 G153 3.30x30 G F154 3.31x31 F154 3.31x31 F F155 3.32x32 F155 3.32x32 F Y156 3.33x33 Y156 3.33x33 Y G157 3.34x34 G157 3.34x34 G N158 3.35x35 N158 3.35x35 N M159 3.36x36 M159 3.36x36 M Y160 3.37x37 Y160 3.37x37 Y C161 3.38x38 C161 3.38x38 C S162 3.39x39 S162 3.39x39 S I163 3.40x40 I163 3.40x40 I L164 3.41x41 L164 3.41x41 L F165 3.42x42 F165 3.42x42 F M166 3.43x43 M166 3.43x43 M T167 3.44x44 T167 3.44x44 T C168 3.45x45 C168 3.45x45 C L169 3.46x46 L169 3.46x46 L S170 3.47x47 S170 3.47x47 S V171 3.48x48 V171 3.48x48 V Q172 3.49x49 Q172 3.49x49 Q R173 3.50x50 R173 3.50x50 R Y174 3.51x51 Y174 3.51x51 Y W175 3.52x52 W175 3.52x52 W V176 3.53x53 V176 3.53x53 V I177 3.54x54 I177 3.54x54 I V178 3.55x55 V178 3.55x55 V N179 3.56x56 N179 3.56x56 N K187 4.38x38 K187 4.38x38 K A188 4.39x39 A188 4.39x39 A N189 4.40x40 N189 4.40x40 N I190 4.41x41 I190 4.41x41 I A191 4.42x42 A191 4.42x42 A I192 4.43x43 I192 4.43x43 I G193 4.44x44 G193 4.44x44 G I194 4.45x45 I194 4.45x45 I S195 4.46x46 S195 4.46x46 S L196 4.47x47 L196 4.47x47 L A197 4.48x48 A197 4.48x48 A I198 4.49x49 I198 4.49x49 I W199 4.50x50 W199 4.50x50 W L200 4.51x51 L200 4.51x51 L L201 4.52x52 L201 4.52x52 L I202 4.53x53 I202 4.53x53 I L203 4.54x54 L203 4.54x54 L L204 4.55x55 L204 4.55x55 L V205 4.56x56 V205 4.56x56 V T206 4.57x57 T206 4.57x57 T I207 4.58x59 I207 4.58x59 I P208 4.59x60 P208 4.59x60 P L209 4.60x61 L209 4.60x61 L Y210 4.61x62 Y210 4.61x62 Y V211 4.62x63 V211 4.62x63 V L235 5.31x32 L235 5.31x32 L V236 5.32x33 V236 5.32x33 V G237 5.33x34 G237 5.33x34 G D238 5.34x35 D238 5.34x35 D M239 5.35x36 M239 5.35x36 M F240 5.36x37 F240 5.36x37 F N241 5.37x38 N241 5.37x38 N Y242 5.38x39 Y242 5.38x39 Y F243 5.39x40 F243 5.39x40 F L244 5.40x41 L244 5.40x41 L S245 5.41x42 S245 5.41x42 S L246 5.42x43 L246 5.42x43 L A247 5.43x44 A247 5.43x44 A I248 5.44x45 I248 5.44x45 I G249 5.45x46 G249 5.45x46 G V250 5.46x461 V250 5.46x461 V F251 5.47x47 F251 5.47x47 F L252 5.48x48 L252 5.48x48 L F253 5.49x49 F253 5.49x49 F P254 5.50x50 P254 5.50x50 P A255 5.51x51 A255 5.51x51 A F256 5.52x52 F256 5.52x52 F L257 5.53x53 L257 5.53x53 L T258 5.54x54 T258 5.54x54 T A259 5.55x55 A259 5.55x55 A S260 5.56x56 S260 5.56x56 S A261 5.57x57 A261 5.57x57 A Y262 5.58x58 Y262 5.58x58 Y V263 5.59x59 V263 5.59x59 V L264 5.60x60 L264 5.60x60 L M265 5.61x61 M265 5.61x61 M I266 5.62x62 I266 5.62x62 I R267 5.63x63 R267 5.63x63 R M268 5.64x64 M268 5.64x64 M L269 5.65x65 L269 5.65x65 L R270 5.66x66 R270 5.66x66 R S271 5.67x67 S271 5.67x67 S S272 5.68x68 S272 5.68x68 S E276 6.24x25 E276 6.24x25 E N277 6.25x26 N277 6.25x26 N S278 6.26x27 S278 6.26x27 S E279 6.27x28 E279 6.27x28 E K280 6.28x29 K280 6.28x29 K K281 6.29x30 K281 6.29x30 K R282 6.30x31 R282 6.30x31 R K283 6.31x32 K283 6.31x32 K R284 6.32x33 R284 6.32x33 R A285 6.33x34 A285 6.33x34 A I286 6.34x35 I286 6.34x35 I K287 6.35x36 K287 6.35x36 K L288 6.36x37 L288 6.36x37 L I289 6.37x38 I289 6.37x38 I V290 6.38x39 V290 6.38x39 V T291 6.39x40 T291 6.39x40 T V292 6.40x41 V292 6.40x41 V L293 6.41x42 L293 6.41x42 L A294 6.42x43 A294 6.42x43 A M295 6.43x44 M295 6.43x44 M Y296 6.44x45 Y296 6.44x45 Y L297 6.45x46 L297 6.45x46 L I298 6.46x461 I298 6.46x461 I C299 6.47x47 C299 6.47x47 C F300 6.48x48 F300 6.48x48 F T301 6.49x49 T301 6.49x49 T P302 6.50x50 P302 6.50x50 P S303 6.51x51 S303 6.51x51 S N304 6.52x52 N304 6.52x52 N L305 6.53x53 L305 6.53x53 L L306 6.54x54 L306 6.54x54 L L307 6.55x55 L307 6.55x55 L V308 6.56x56 V308 6.56x56 V V309 6.57x57 V309 6.57x57 V H310 6.58x58 H310 6.58x58 H Y311 6.59x59 Y311 6.59x59 Y F312 6.60x60 F312 6.60x60 F L313 6.61x61 L313 6.61x61 L I314 6.62x62 I314 6.62x62 I K315 6.63x63 K315 6.63x63 K S316 6.64x64 S316 6.64x64 S Q317 6.65x65 Q317 6.65x65 Q V322 7.31x30 V322 7.31x30 V Y323 7.32x31 Y323 7.32x31 Y A324 7.33x32 A324 7.33x32 A L325 7.34x33 L325 7.34x33 L Y326 7.35x34 Y326 7.35x34 Y I327 7.36x35 I327 7.36x35 I V328 7.37x36 V328 7.37x36 V A329 7.38x37 A329 7.38x37 A L330 7.39x38 L330 7.39x38 L C331 7.40x39 C331 7.40x39 C L332 7.41x40 L332 7.41x40 L S333 7.42x41 S333 7.42x41 S T334 7.43x42 T334 7.43x42 T L335 7.44x43 L335 7.44x43 L N336 7.45x45 N336 7.45x45 N S337 7.46x46 S337 7.46x46 S C338 7.47x47 C338 7.47x47 C I339 7.48x48 I339 7.48x48 I D340 7.49x49 D340 7.49x49 D P341 7.50x50 P341 7.50x50 P F342 7.51x51 F342 7.51x51 F V343 7.52x52 V343 7.52x52 V Y344 7.53x53 Y344 7.53x53 Y Y345 7.54x54 Y345 7.54x54 Y F346 7.55x55 F346 7.55x55 F V347 7.56x56 V347 7.56x56 V S348 8.47x47 S348 8.47x47 S H349 8.48x48 H349 8.48x48 H D350 8.49x49 D350 8.49x49 D A355 8.54x54 A355 8.54x54 A K356 8.55x55 K356 8.55x55 K N357 8.56x56 N357 8.56x56 N R362 8.61x61 R362 8.61x61 R F351 8.50x50 F351 8.50x50 F R352 8.51x51 R352 8.51x51 R D353 8.52x52 D353 8.52x52 D H354 8.53x53 H354 8.53x53 H A358 8.57x57 A358 8.57x57 A L359 8.58x58 L359 8.58x58 L L360 8.59x59 L360 8.59x59 L C361 8.60x60 C361 8.60x60 C

Largest active-inactive contact-score changes

Residue pairs ranked by |ΔRRCS| between the active and inactive models. GPCRdb generic numbers are shown in parentheses when available. Highlighted rows exceed the receptor-specific ΔRRCS threshold.

Rank Residue 1 Residue 2 Active RRCS Inactive RRCS ΔRRCS Magnitude
1 ARG36 GLN319 12.881 0.000 +12.881 HIGH
2 VAL236 (5.32x33) TYR311 (6.59x59) 0.065 11.274 -11.209 HIGH
3 PHE243 (5.39x40) TYR311 (6.59x59) 11.159 0.027 +11.132 HIGH
4 TYR345 (7.54x54) ARG352 (8.51x51) 0.000 9.822 -9.822 HIGH
5 TYR296 (6.44x45) PHE300 (6.48x48) 0.727 10.000 -9.274 HIGH
6 PHE128 (2.57x57) THR334 (7.43x42) 2.793 11.273 -8.480 HIGH
7 ARG36 ASP62 7.200 0.000 +7.200 HIGH
8 LEU307 (6.55x55) TYR326 (7.35x34) 7.097 0.000 +7.097 HIGH
9 HIS310 (6.58x58) SER320 7.080 0.000 +7.080 HIGH
10 TYR82 (1.39x39) PRO129 (2.58x58) 0.000 7.058 -7.058 HIGH
11 MET114 (2.43x43) TYR345 (7.54x54) 6.792 0.000 +6.792 HIGH
12 PHE300 (6.48x48) SER333 (7.42x41) 2.526 9.139 -6.613 HIGH
13 ARG103 (1.60x60) ALA358 (8.57x57) 6.604 0.000 +6.604 HIGH
14 LYS41 SER60 0.903 7.127 -6.224 HIGH
15 SER37 GLN319 6.178 0.000 +6.178 HIGH
16 ILE163 (3.40x40) PHE300 (6.48x48) 5.786 0.000 +5.786 HIGH
17 LEU130 (2.59x59) TYR143 (23.52x52) 5.994 0.209 +5.785 HIGH
18 ALA255 (5.51x51) TYR296 (6.44x45) 5.780 0.000 +5.780 HIGH
19 PRO341 (7.50x50) PHE346 (7.55x55) 5.775 0.000 +5.775 HIGH
20 TYR344 (7.53x53) PHE351 (8.50x50) 0.000 5.672 -5.672 HIGH
21 HIS135 (2.64x64) TYR323 (7.32x31) 0.000 5.575 -5.575 HIGH
22 PHE100 (1.57x57) MET114 (2.43x43) 0.000 5.539 -5.539 HIGH
23 ARG103 (1.60x60) ASN357 (8.56x56) 5.425 0.000 +5.425 HIGH
24 TRP98 (1.55x55) ARG103 (1.60x60) 2.420 7.792 -5.373 HIGH
25 LEU313 (6.61x61) GLN319 5.347 0.000 +5.347 HIGH
26 TYR296 (6.44x45) ASN336 (7.45x45) 0.000 5.031 -5.031 HIGH
27 MET159 (3.36x36) PHE300 (6.48x48) 0.665 5.658 -4.993 MED
28 LEU69 ASN139 4.987 0.000 +4.987 MED
29 TYR134 (2.63x63) ASN139 16.835 11.930 +4.905 MED
30 MET159 (3.36x36) TYR296 (6.44x45) 0.000 4.882 -4.882 MED
31 PHE128 (2.57x57) ILE132 (2.61x61) 0.161 4.885 -4.724 MED
32 TYR345 (7.54x54) PHE351 (8.50x50) 7.188 2.624 +4.564 MED
33 TYR82 (1.39x39) PHE128 (2.57x57) 5.007 0.491 +4.516 MED
34 GLY40 PHE59 4.453 0.000 +4.453 MED
35 ASN336 (7.45x45) ASP340 (7.49x49) 4.746 0.377 +4.369 MED
36 LYS131 (2.60x60) PHE155 (3.32x32) 6.118 1.809 +4.309 MED
37 ILE163 (3.40x40) TYR296 (6.44x45) 2.174 6.464 -4.290 MED
38 PHE251 (5.47x47) TYR296 (6.44x45) 6.020 1.755 +4.264 MED
39 HIS310 (6.58x58) TYR323 (7.32x31) 4.190 0.000 +4.190 MED
40 THR225 HIS227 (45.51x51) 0.378 4.495 -4.118 MED
41 TYR156 (3.33x33) LEU307 (6.55x55) 0.000 4.002 -4.002 MED
42 MET166 (3.43x43) TYR344 (7.53x53) 4.491 0.505 +3.986 MED
43 PHE86 (1.43x43) PRO129 (2.58x58) 3.954 0.018 +3.936 MED
44 TRP127 (2.56x56) PHE154 (3.31x31) 6.240 10.154 -3.914 MED
45 THR258 (5.54x54) LEU293 (6.41x42) 0.000 3.873 -3.873 MED
46 SER37 GLY318 3.798 0.000 +3.798 MED
47 TRP175 (3.52x52) LYS187 (4.38x38) 8.736 4.963 +3.773 MED
48 MET114 (2.43x43) TYR344 (7.53x53) 0.791 4.544 -3.754 MED
49 LYS131 (2.60x60) LEU330 (7.39x38) 0.000 3.738 -3.738 MED
50 VAL68 THR74 (1.31x31) 3.731 0.000 +3.731 MED
51 ARG173 (3.50x50) TYR344 (7.53x53) 3.728 0.000 +3.728 MED
52 CYS361 (8.60x60) ARG365 0.000 3.631 -3.631 MED
53 TYR262 (5.58x58) VAL292 (6.40x41) 3.615 0.000 +3.615 MED
54 THR83 (1.40x40) ILE132 (2.61x61) 3.521 0.000 +3.521 MED
55 ALA96 (1.53x53) TYR345 (7.54x54) 3.505 0.000 +3.505 MED
56 ASP43 SER60 0.935 4.307 -3.372 MED
57 ASN149 (3.26x26) TYR210 (4.61x62) 4.621 7.898 -3.276 MED
58 ALA118 (2.47x47) TYR345 (7.54x54) 3.216 0.000 +3.216 MED
59 LEU288 (6.36x37) VAL347 (7.56x56) 0.896 4.093 -3.196 MED
60 MET274 ARG282 (6.30x31) 0.799 3.978 -3.178 MED
61 LYS131 (2.60x60) LEU151 (3.28x28) 0.931 4.101 -3.170 MED
62 LYS213 ASP228 (45.52x52) 6.415 9.574 -3.159 MED
63 HIS183 (34.53x53) LYS187 (4.38x38) 0.000 3.126 -3.126 MED
64 LEU269 (5.65x65) ARG282 (6.30x31) 4.627 1.516 +3.111 MED
65 ASP121 (2.50x50) SER162 (3.39x39) 3.881 0.771 +3.110 MED
66 GLU276 (6.24x25) LYS280 (6.28x29) 2.251 5.293 -3.041 MED
67 VAL99 PHE351 (8.50x50) 5.084 2.098 +2.985 MED
68 HIS135 (2.64x64) ASN139 3.083 0.136 +2.947 MED
69 ARG173 (3.50x50) LEU288 (6.36x37) 2.904 0.000 +2.904 MED
70 LEU78 HIS135 (2.64x64) 2.939 0.042 +2.897 MED
71 TYR156 (3.33x33) TYR326 (7.35x34) 3.456 0.631 +2.825 MED
72 PHE100 (1.57x57) ALA115 5.116 2.293 +2.823 MED
73 TYR82 (1.39x39) ILE132 (2.61x61) 3.107 0.356 +2.752 MED
74 VAL292 (6.40x41) ASP340 (7.49x49) 0.000 2.721 -2.721 MED
75 MET274 GLU279 0.162 2.802 -2.640 MED
76 TYR134 (2.63x63) ASN140 4.405 1.773 +2.632 MED
77 GLU279 ARG282 (6.30x31) 2.619 0.000 +2.619 MED
78 THR395 SER396 0.000 2.562 -2.562 LOW
79 PHE100 (1.57x57) THR104 2.594 0.034 +2.561 LOW
80 LEU78 TYR82 (1.39x39) 2.554 0.000 +2.554 LOW
81 MET159 (3.36x36) ASN304 0.000 2.547 -2.547 LOW
82 TYR134 (2.63x63) HIS135 (2.64x64) 3.331 0.794 +2.537 LOW
83 ILE314 GLN319 2.503 0.000 +2.503 LOW
84 TYR156 (3.33x33) LEU330 (7.39x38) 2.560 0.063 +2.497 LOW
85 SER3 SER5 0.000 2.485 -2.485 LOW
86 LEU288 (6.36x37) TYR344 (7.53x53) 0.000 2.459 -2.459 LOW
87 VAL85 PHE128 (2.57x57) 2.842 0.389 +2.453 LOW
88 TYR134 (2.63x63) THR225 2.448 0.000 +2.448 LOW
89 TYR160 LEU246 0.932 3.379 -2.447 LOW
90 VAL61 ILE218 2.425 0.000 +2.425 LOW
91 SER32 SER33 0.000 2.413 -2.413 LOW
92 PHE86 (1.43x43) VAL125 3.245 0.834 +2.411 LOW
93 TYR82 (1.39x39) PHE86 (1.43x43) 0.000 2.399 -2.399 LOW
94 TRP127 (2.56x56) LEU151 (3.28x28) 2.718 0.344 +2.374 LOW
95 CYS299 LEU332 5.738 3.366 +2.372 LOW
96 TYR160 VAL250 3.664 6.032 -2.368 LOW
97 ILE152 LYS213 4.192 1.841 +2.351 LOW
98 THR74 (1.31x31) ILE136 0.000 2.331 -2.331 LOW
99 HIS108 HIS183 (34.53x53) 4.133 1.834 +2.299 LOW
100 MET95 PHE346 (7.55x55) 2.290 0.000 +2.290 LOW

Transmembrane domain analysis

Residues are grouped by segment according to whether their contact pairs are stronger in the active model (positive ΔRRCS) or the inactive model (negative ΔRRCS). Only residues linked to contact-pair changes above the receptor-specific ΔRRCS threshold (|ΔRRCS| ≥ 2.60, computed as max(mean(|Δ|) + σ, 0.2)) are shown.

Per-segment summary
Segment Range Active-favoring residues Count Inactive-favoring residues Count
TM1 74-103 103 (+8.7), 74 (+8.7), 86 (+5.2), 82 (+5.2), 83 (+2.8), 96 (+1.2) 6 98 (-3.1), 100 (-2.1) 2
TM2 114-135 134 (+11.5), 135 (+9.2), 121 (+6.8), 130 (+6.0), 118 (+3.9), 132 (+0.9) 6 128 (-3.7), 129 (-3.4), 127 (-3.4), 131 (-1.9), 114 (-1.5) 5
TM3 149-175 173 (+5.0), 155 (+4.6), 166 (+4.5), 175 (+3.2), 162 (+3.2), 156 (+2.7) 6 159 (-13.0), 154 (-4.2), 149 (-3.5), 151 (-2.8), 163 (-0.5) 5
TM4 187-210 187 (+2.8) 1 210 (-9.4) 1
TM5 236-269 243 (+14.0), 251 (+7.2), 255 (+3.8), 262 (+1.8), 269 (+0.4) 5 258 (-7.2), 236 (-5.5) 2
TM6 276-313 310 (+12.4), 313 (+8.1), 307 (+4.6), 282 (+3.9), 292 (+1.6), 311 (+0.4) 6 296 (-11.2), 300 (-9.9), 293 (-5.4), 288 (-4.1), 280 (-3.2), 276 (-3.2) 6
TM7 323-347 326 (+13.5), 345 (+10.0), 346 (+9.6), 340 (+8.7), 341 (+2.9), 336 (+2.4) 6 334 (-5.5), 333 (-4.7), 347 (-2.8), 323 (-2.2), 330 (-2.1), 344 (-1.3) 6

Interactive visualizations

ΔRRCS distribution

Active vs inactive comparison

Residue-wise changes

TM domain breakdown

Contact-site missense variants

105 gnomAD missense variants located at contact-forming residues, sorted by the ΔRRCS magnitude of the corresponding position.

Position Protein change DNA change Allele freq Het count ΔRRCS AM score Pathogenicity Conservation dbSNP
319 p.Gln319His c.957G>C 9.58e-06 14 12.88 0.129 BENIGN 0.37 rs1186516213
236 p.Val236Leu c.706G>C 6.22e-05 91 11.21 0.169 BENIGN 0.41 rs375707707
236 p.Val236Met c.706G>A 2.74e-06 4 11.21 - - - rs375707707
236 p.Val236Ala c.707T>C 6.84e-07 1 11.21 - - - -
243 p.Phe243Ser c.728T>C 6.84e-07 1 11.13 0.895 PATHOGENIC 0.84 -
345 p.Tyr345Asn c.1033T>A 6.84e-07 1 9.82 0.748 PATHOGENIC 0.97 -
352 p.Arg352Lys c.1055G>A 1.03e-05 15 9.82 0.186 BENIGN 0.87 rs765152103
345 p.Tyr345His c.1033T>C 4.45e-05 65 9.82 - - - rs766276267
352 p.Arg352Ser c.1056G>C 6.84e-07 1 9.82 - - - rs1378304707
300 p.Phe300Leu c.898T>C 2.74e-06 4 9.27 0.995 PATHOGENIC 0.93 rs1233110593
296 p.Tyr296His c.886T>C 6.84e-07 1 9.27 0.830 PATHOGENIC 0.81 rs1750394394
128 p.Phe128Ile c.382T>A 1.37e-06 2 8.48 0.253 BENIGN 0.62 -
334 p.Thr334Ala c.1000A>G 6.84e-07 1 8.48 0.113 BENIGN 0.61 rs1278446886
334 p.Thr334Ile c.1001C>T 2.05e-06 3 8.48 - - - -
326 p.Tyr326His c.976T>C 6.84e-07 1 7.10 0.849 PATHOGENIC 0.99 rs1359132042
326 p.Tyr326Cys c.977A>G 6.84e-07 1 7.10 - - - -
310 p.His310Pro c.929A>C 1.37e-06 2 7.08 0.904 PATHOGENIC 0.92 rs754875227
320 p.Ser320Asn c.959G>A 1.37e-06 2 7.08 0.340 AMBIGUOUS 0.55 rs1486445755
310 p.His310Arg c.929A>G 8.89e-06 13 7.08 - - - rs754875227
129 p.Pro129Arg c.386C>G 6.84e-07 1 7.06 0.964 PATHOGENIC 0.98 -
82 p.Tyr82Cys c.245A>G 2.74e-06 4 7.06 0.308 BENIGN 1.00 rs1402378873
114 p.Met114Val c.340A>G 1.37e-06 2 6.79 0.436 AMBIGUOUS 0.86 rs1393875630
114 p.Met114Leu c.340A>T 6.84e-07 1 6.79 - - - -
333 p.Ser333Cys c.998C>G 6.58e-06 1 6.61 0.334 BENIGN 0.68 rs1750398347
333 p.Ser333Phe c.998C>T 6.84e-07 1 6.61 - - - -
358 p.Ala358Ser c.1072G>T 6.84e-07 1 6.60 0.123 BENIGN 0.56 -
103 p.Arg103Gln c.308G>A 3.97e-05 58 6.60 0.118 BENIGN 0.84 rs185549069
103 p.Arg103Pro c.308G>C 1.37e-06 2 6.60 - - - rs185549069
358 p.Ala358Thr c.1072G>A 2.67e-05 39 6.60 - - - rs563654389
60 p.Ser60Tyr c.179C>A 6.84e-07 1 6.22 0.098 BENIGN 0.41 -
60 p.Ser60Phe c.179C>T 6.84e-07 1 6.22 - - - -
37 p.Ser37Asn c.110G>A 2.05e-06 3 6.18 0.490 AMBIGUOUS 0.77 -
130 p.Leu130Trp c.389T>G 1.37e-06 2 5.79 0.426 AMBIGUOUS 0.74 rs910420444
341 p.Pro341Arg c.1022C>G 1.64e-05 24 5.78 0.959 PATHOGENIC 0.99 rs764534865
346 p.Phe346Ile c.1036T>A 6.84e-07 1 5.78 0.452 AMBIGUOUS 0.82 rs767669676
135 p.His135Arg c.404A>G 6.84e-06 10 5.58 0.820 PATHOGENIC 0.90 rs148584357
323 p.Tyr323Asn c.967T>A 6.84e-07 1 5.58 0.747 PATHOGENIC 0.99 rs771965396
323 p.Tyr323Cys c.968A>G 6.84e-07 1 5.58 - - - rs1220668965
357 p.Asn357Asp c.1069A>G 2.74e-06 4 5.42 0.188 BENIGN 0.68 rs1750400755
98 p.Trp98Arg c.292T>C 1.03e-05 15 5.37 0.894 PATHOGENIC 0.75 rs1003568019
98 p.Trp98Gly c.292T>G 2.05e-06 3 5.37 - - - rs1003568019
313 p.Leu313Val c.937C>G 1.32e-05 2 5.35 0.140 BENIGN 0.53 rs905528105
313 p.Leu313Gln c.938T>A 6.84e-07 1 5.35 - - - -
313 p.Leu313Pro c.938T>C 6.84e-07 1 5.35 - - - -
159 p.Met159Val c.475A>G 4.79e-06 7 4.99 0.498 AMBIGUOUS 0.96 rs762545643
159 p.Met159Thr c.476T>C 6.84e-07 1 4.99 - - - -
159 p.Met159Ile c.477G>T 1.18e-04 170 4.99 - - - rs115885685
159 p.Met159Ile c.477G>A 1.06e-03 1551 4.99 - - - rs115885685
69 p.Leu69Ile c.205C>A 1.37e-06 2 4.99 0.284 BENIGN 0.95 rs147135859
69 p.Leu69Arg c.206T>G 6.57e-06 1 4.99 - - - rs1471895947
69 p.Leu69Pro c.206T>C 6.84e-07 1 4.99 - - - -
134 p.Tyr134Cys c.401A>G 9.58e-06 14 4.91 0.861 PATHOGENIC 0.99 rs762020675
134 p.Tyr134Phe c.401A>T 6.84e-07 1 4.91 - - - -
40 p.Gly40Asp c.119G>A 8.90e-06 13 4.45 0.720 PATHOGENIC 0.71 rs143373085
340 p.Asp340Asn c.1018G>A 2.74e-06 4 4.37 0.849 PATHOGENIC 0.99 rs1176513304
340 p.Asp340Glu c.1020C>A 6.84e-07 1 4.37 - - - rs763346141
155 p.Phe155Val c.463T>G 6.84e-07 1 4.31 0.672 PATHOGENIC 0.96 -
155 p.Phe155Leu c.465C>G 6.84e-07 1 4.31 - - - rs1186871864
227 p.His227Arg c.680A>G 2.05e-06 3 4.12 0.801 PATHOGENIC 0.84 -
225 p.Thr225Ile c.674C>T 6.59e-06 1 4.12 0.764 PATHOGENIC 0.94 rs371819764
156 p.Tyr156Cys c.467A>G 6.84e-07 1 4.00 0.650 PATHOGENIC 0.93 rs1475152609
156 p.Tyr156Phe c.467A>T 1.37e-06 2 4.00 - - - -
166 p.Met166Leu c.496A>T 6.84e-07 1 3.99 0.199 BENIGN 0.68 -
166 p.Met166Val c.496A>G 6.84e-07 1 3.99 - - - rs1750381162
166 p.Met166Ile c.498G>T 6.84e-07 1 3.99 - - - rs1052875957
166 p.Met166Ile c.498G>A 6.84e-07 1 3.99 - - - rs1052875957
154 p.Phe154Val c.460T>G 2.05e-06 3 3.91 0.368 AMBIGUOUS 0.63 rs1226839415
293 p.Leu293Pro c.878T>C 1.37e-06 2 3.87 0.890 PATHOGENIC 0.95 rs1454241071
258 p.Thr258Ala c.772A>G 3.42e-06 5 3.87 0.271 BENIGN 0.58 -
258 p.Thr258Ile c.773C>T 6.84e-07 1 3.87 - - - rs1750389066
318 p.Gly318Ser c.952G>A 6.60e-06 1 3.80 0.090 BENIGN 0.36 rs1360640710
318 p.Gly318Asp c.953G>A 6.84e-07 1 3.80 - - - rs755911067
175 p.Trp175Arg c.523T>C 2.05e-06 3 3.77 0.355 AMBIGUOUS 0.57 rs1159550519
187 p.Lys187Asn c.561G>C 5.47e-06 8 3.77 0.140 BENIGN 0.47 rs1011311806
330 p.Leu330Phe c.988C>T 6.84e-07 1 3.74 0.678 PATHOGENIC 0.92 rs1750397962
74 p.Thr74Ala c.220A>G 6.84e-07 1 3.73 0.263 BENIGN 0.74 rs781567981
68 p.Val68Ile c.202G>A 5.47e-06 8 3.73 0.059 BENIGN 0.49 rs757902001
74 p.Thr74Asn c.221C>A 2.05e-06 3 3.73 - - - rs746271767
74 p.Thr74Ile c.221C>T 6.84e-07 1 3.73 - - - -
173 p.Arg173Lys c.518G>A 6.84e-07 1 3.73 0.590 PATHOGENIC 0.97 -
365 p.Arg365Cys c.1093C>T 1.03e-05 15 3.63 0.187 BENIGN 0.70 rs1416971894
365 p.Arg365Leu c.1094G>T 3.42e-06 5 3.63 - - - rs149001132
365 p.Arg365His c.1094G>A 1.92e-05 28 3.63 - - - rs149001132
262 p.Tyr262Cys c.785A>G 2.05e-06 3 3.62 0.333 BENIGN 0.97 rs181651370
292 p.Val292Ile c.874G>A 6.84e-07 1 3.62 0.140 BENIGN 0.96 rs1340682362
292 p.Val292Gly c.875T>G 6.84e-07 1 3.62 - - - -
96 p.Ala96Ser c.286G>T 6.84e-07 1 3.50 0.291 BENIGN 0.85 -
96 p.Ala96Val c.287C>T 6.84e-07 1 3.50 - - - -
43 p.Asp43Val c.128A>T 1.37e-06 2 3.37 0.089 BENIGN 0.39 -
118 p.Ala118Thr c.352G>A 6.84e-07 1 3.22 0.523 AMBIGUOUS 0.86 rs1449513991
288 p.Leu288Phe c.862C>T 9.58e-06 14 3.20 0.447 AMBIGUOUS 0.78 rs765886275
282 p.Arg282Met c.845G>T 4.10e-06 6 3.18 0.319 BENIGN 0.65 rs187106934
274 p.Met274Val c.820A>G 1.37e-06 2 3.18 0.054 BENIGN 0.33 rs1215678275
274 p.Met274Thr c.821T>C 1.37e-06 2 3.18 - - - rs1489493022
274 p.Met274Ile c.822G>A 6.84e-07 1 3.18 - - - rs747974393
282 p.Arg282Lys c.845G>A 7.52e-06 11 3.18 - - - rs187106934
151 p.Leu151Arg c.452T>G 3.28e-05 5 3.17 0.769 PATHOGENIC 0.70 rs1442301178
228 p.Asp228His c.682G>C 6.84e-07 1 3.16 0.975 PATHOGENIC 0.95 -
213 p.Lys213Glu c.637A>G 1.37e-06 2 3.16 0.115 BENIGN 0.52 -
183 p.His183Pro c.548A>C 1.37e-06 2 3.13 0.087 BENIGN 0.47 -
269 p.Leu269Pro c.806T>C 6.58e-06 1 3.11 0.874 PATHOGENIC 0.99 rs1750390588
162 p.Ser162Tyr c.485C>A 6.84e-07 1 3.11 0.978 PATHOGENIC 0.97 -
121 p.Asp121Asn c.361G>A 2.05e-06 3 3.11 0.903 PATHOGENIC 1.00 rs770126870
162 p.Ser162Phe c.485C>T 6.84e-07 1 3.11 - - - rs1750380999
280 p.Lys280Arg c.839A>G 6.84e-07 1 3.04 0.077 BENIGN 0.64 rs1750392428

RRCS results

Top 1000 contact pairs ranked by |ΔRRCS|. Rows above the receptor-specific ΔRRCS threshold (|ΔRRCS| ≥ 2.60, computed as max(mean(|Δ|) + σ, 0.2)) are highlighted.

Res1 AA1 Res2 AA2 Active RRCS Inactive RRCS ΔRRCS |ΔRRCS|
36 ARG 319 GLN 12.881 0.000 12.881 12.881
236 VAL 311 TYR 0.065 11.274 -11.209 11.209
243 PHE 311 TYR 11.159 0.027 11.132 11.132
345 TYR 352 ARG 0.000 9.822 -9.822 9.822
296 TYR 300 PHE 0.727 10.000 -9.274 9.274
128 PHE 334 THR 2.793 11.273 -8.480 8.480
36 ARG 62 ASP 7.200 0.000 7.200 7.200
307 LEU 326 TYR 7.097 0.000 7.097 7.097
310 HIS 320 SER 7.080 0.000 7.080 7.080
82 TYR 129 PRO 0.000 7.058 -7.058 7.058
114 MET 345 TYR 6.792 0.000 6.792 6.792
300 PHE 333 SER 2.526 9.139 -6.613 6.613
103 ARG 358 ALA 6.604 0.000 6.604 6.604
41 LYS 60 SER 0.903 7.127 -6.224 6.224
37 SER 319 GLN 6.178 0.000 6.178 6.178
163 ILE 300 PHE 5.786 0.000 5.786 5.786
130 LEU 143 TYR 5.994 0.209 5.785 5.785
255 ALA 296 TYR 5.780 0.000 5.780 5.780
341 PRO 346 PHE 5.775 0.000 5.775 5.775
344 TYR 351 PHE 0.000 5.672 -5.672 5.672
135 HIS 323 TYR 0.000 5.575 -5.575 5.575
100 PHE 114 MET 0.000 5.539 -5.539 5.539
103 ARG 357 ASN 5.425 0.000 5.425 5.425
98 TRP 103 ARG 2.420 7.792 -5.373 5.373
313 LEU 319 GLN 5.347 0.000 5.347 5.347
296 TYR 336 ASN 0.000 5.031 -5.031 5.031
159 MET 300 PHE 0.665 5.658 -4.993 4.993
69 LEU 139 ASN 4.987 0.000 4.987 4.987
134 TYR 139 ASN 16.835 11.930 4.905 4.905
159 MET 296 TYR 0.000 4.882 -4.882 4.882
128 PHE 132 ILE 0.161 4.885 -4.724 4.724
345 TYR 351 PHE 7.188 2.624 4.564 4.564
82 TYR 128 PHE 5.007 0.491 4.516 4.516
40 GLY 59 PHE 4.453 0.000 4.453 4.453
336 ASN 340 ASP 4.746 0.377 4.369 4.369
131 LYS 155 PHE 6.118 1.809 4.309 4.309
163 ILE 296 TYR 2.174 6.464 -4.290 4.290
251 PHE 296 TYR 6.020 1.755 4.264 4.264
310 HIS 323 TYR 4.190 0.000 4.190 4.190
225 THR 227 HIS 0.378 4.495 -4.118 4.118
156 TYR 307 LEU 0.000 4.002 -4.002 4.002
166 MET 344 TYR 4.491 0.505 3.986 3.986
86 PHE 129 PRO 3.954 0.018 3.936 3.936
127 TRP 154 PHE 6.240 10.154 -3.914 3.914
258 THR 293 LEU 0.000 3.873 -3.873 3.873
37 SER 318 GLY 3.798 0.000 3.798 3.798
175 TRP 187 LYS 8.736 4.963 3.773 3.773
114 MET 344 TYR 0.791 4.544 -3.754 3.754
131 LYS 330 LEU 0.000 3.738 -3.738 3.738
68 VAL 74 THR 3.731 0.000 3.731 3.731
173 ARG 344 TYR 3.728 0.000 3.728 3.728
361 CYS 365 ARG 0.000 3.631 -3.631 3.631
262 TYR 292 VAL 3.615 0.000 3.615 3.615
83 THR 132 ILE 3.521 0.000 3.521 3.521
96 ALA 345 TYR 3.505 0.000 3.505 3.505
43 ASP 60 SER 0.935 4.307 -3.372 3.372
149 ASN 210 TYR 4.621 7.898 -3.276 3.276
118 ALA 345 TYR 3.216 0.000 3.216 3.216
288 LEU 347 VAL 0.896 4.093 -3.196 3.196
274 MET 282 ARG 0.799 3.978 -3.178 3.178
131 LYS 151 LEU 0.931 4.101 -3.170 3.170
213 LYS 228 ASP 6.415 9.574 -3.159 3.159
183 HIS 187 LYS 0.000 3.126 -3.126 3.126
269 LEU 282 ARG 4.627 1.516 3.111 3.111
121 ASP 162 SER 3.881 0.771 3.110 3.110
276 GLU 280 LYS 2.251 5.293 -3.041 3.041
99 VAL 351 PHE 5.084 2.098 2.985 2.985
135 HIS 139 ASN 3.083 0.136 2.947 2.947
173 ARG 288 LEU 2.904 0.000 2.904 2.904
78 LEU 135 HIS 2.939 0.042 2.897 2.897
156 TYR 326 TYR 3.456 0.631 2.825 2.825
100 PHE 115 ALA 5.116 2.293 2.823 2.823
82 TYR 132 ILE 3.107 0.356 2.752 2.752
292 VAL 340 ASP 0.000 2.721 -2.721 2.721
274 MET 279 GLU 0.162 2.802 -2.640 2.640
134 TYR 140 ASN 4.405 1.773 2.632 2.632
279 GLU 282 ARG 2.619 0.000 2.619 2.619
395 THR 396 SER 0.000 2.562 -2.562 2.562
100 PHE 104 THR 2.594 0.034 2.561 2.561
78 LEU 82 TYR 2.554 0.000 2.554 2.554
159 MET 304 ASN 0.000 2.547 -2.547 2.547
134 TYR 135 HIS 3.331 0.794 2.537 2.537
314 ILE 319 GLN 2.503 0.000 2.503 2.503
156 TYR 330 LEU 2.560 0.063 2.497 2.497
3 SER 5 SER 0.000 2.485 -2.485 2.485
288 LEU 344 TYR 0.000 2.459 -2.459 2.459
85 VAL 128 PHE 2.842 0.389 2.453 2.453
134 TYR 225 THR 2.448 0.000 2.448 2.448
160 TYR 246 LEU 0.932 3.379 -2.447 2.447
61 VAL 218 ILE 2.425 0.000 2.425 2.425
32 SER 33 SER 0.000 2.413 -2.413 2.413
86 PHE 125 VAL 3.245 0.834 2.411 2.411
82 TYR 86 PHE 0.000 2.399 -2.399 2.399
127 TRP 151 LEU 2.718 0.344 2.374 2.374
299 CYS 332 LEU 5.738 3.366 2.372 2.372
160 TYR 250 VAL 3.664 6.032 -2.368 2.368
152 ILE 213 LYS 4.192 1.841 2.351 2.351
74 THR 136 ILE 0.000 2.331 -2.331 2.331
108 HIS 183 HIS 4.133 1.834 2.299 2.299
95 MET 346 PHE 2.290 0.000 2.290 2.290
300 PHE 336 ASN 5.550 3.265 2.286 2.286
169 LEU 344 TYR 2.277 0.000 2.277 2.277
38 LEU 65 SER 3.383 1.160 2.223 2.223
182 GLY 187 LYS 6.833 4.630 2.202 2.202
169 LEU 289 ILE 0.000 2.195 -2.195 2.195
242 TYR 243 PHE 2.610 0.420 2.190 2.190
262 TYR 290 VAL 0.000 2.183 -2.183 2.183
266 ILE 270 ARG 2.174 0.000 2.174 2.174
166 MET 340 ASP 2.550 0.381 2.168 2.168
303 SER 326 TYR 2.167 0.000 2.167 2.167
174 TYR 264 LEU 3.688 1.574 2.114 2.114
95 MET 355 ALA 0.281 2.391 -2.110 2.110
82 TYR 135 HIS 2.107 0.000 2.107 2.107
213 LYS 226 CYS 4.272 2.168 2.104 2.104
113 TYR 168 CYS 3.533 5.608 -2.075 2.075
92 SER 341 PRO 3.968 6.028 -2.060 2.060
213 LYS 227 HIS 6.555 4.497 2.058 2.058
74 THR 139 ASN 2.055 0.000 2.055 2.055
75 THR 135 HIS 2.042 0.000 2.042 2.042
240 PHE 315 LYS 2.025 0.000 2.025 2.025
254 PRO 296 TYR 2.022 0.000 2.022 2.022
206 THR 210 TYR 1.962 3.965 -2.003 2.003
123 LEU 154 PHE 3.941 1.948 1.993 1.993
230 LEU 236 VAL 1.989 0.001 1.988 1.988
251 PHE 301 THR 5.059 3.105 1.954 1.954
240 PHE 311 TYR 2.803 4.751 -1.948 1.948
69 LEU 74 THR 1.944 0.000 1.944 1.944
306 LEU 325 LEU 3.457 1.527 1.930 1.930
139 ASN 323 TYR 0.000 1.929 -1.929 1.929
98 TRP 102 PHE 4.822 2.929 1.893 1.893
121 ASP 340 ASP 3.669 1.778 1.891 1.891
154 PHE 210 TYR 3.296 5.185 -1.889 1.889
236 VAL 314 ILE 1.886 0.000 1.886 1.886
346 PHE 351 PHE 1.884 0.000 1.884 1.884
392 THR 393 VAL 2.184 0.303 1.882 1.882
93 ASN 122 LEU 1.626 3.500 -1.874 1.874
161 CYS 202 ILE 3.022 1.162 1.859 1.859
161 CYS 199 TRP 3.232 5.083 -1.850 1.850
251 PHE 300 PHE 4.108 2.259 1.849 1.849
74 THR 135 HIS 3.261 1.420 1.841 1.841
212 VAL 239 MET 2.413 0.580 1.833 1.833
390 SER 391 THR 0.424 2.246 -1.821 1.821
342 PHE 346 PHE 2.474 0.662 1.812 1.812
236 VAL 315 LYS 1.798 0.000 1.798 1.798
159 MET 160 TYR 1.860 3.643 -1.783 1.783
100 PHE 351 PHE 0.000 1.773 -1.773 1.773
342 PHE 347 VAL 1.771 0.000 1.771 1.771
292 VAL 344 TYR 2.614 0.852 1.761 1.761
299 CYS 333 SER 5.577 3.826 1.751 1.751
295 MET 340 ASP 1.749 0.000 1.749 1.749
99 VAL 354 HIS 0.245 1.985 -1.740 1.740
166 MET 336 ASN 1.733 0.000 1.733 1.733
130 LEU 151 LEU 0.591 2.306 -1.715 1.715
48 VAL 49 THR 0.000 1.688 -1.688 1.688
346 PHE 352 ARG 2.224 3.896 -1.672 1.672
340 ASP 345 TYR 1.668 0.000 1.668 1.668
125 VAL 128 PHE 1.664 0.000 1.664 1.664
216 ILE 229 VAL 1.835 0.173 1.663 1.663
262 TYR 289 ILE 7.993 6.333 1.660 1.660
174 TYR 261 ALA 2.004 0.349 1.655 1.655
117 LEU 166 MET 0.943 2.595 -1.652 1.652
82 TYR 131 LYS 1.648 0.000 1.648 1.648
141 TRP 226 CYS 2.893 1.248 1.645 1.645
113 TYR 169 LEU 2.344 0.725 1.619 1.619
306 LEU 322 VAL 1.615 0.000 1.615 1.615
93 ASN 118 ALA 2.925 1.320 1.605 1.605
141 TRP 148 CYS 6.231 7.826 -1.595 1.595
150 VAL 210 TYR 2.673 4.261 -1.588 1.588
340 ASP 344 TYR 2.158 3.737 -1.579 1.579
59 PHE 219 PRO 1.576 0.000 1.576 1.576
307 LEU 311 TYR 1.572 0.000 1.572 1.572
313 LEU 318 GLY 1.567 0.000 1.567 1.567
113 TYR 165 PHE 1.694 3.248 -1.553 1.553
134 TYR 226 CYS 1.444 2.997 -1.553 1.553
251 PHE 304 ASN 7.028 5.479 1.549 1.549
79 PRO 135 HIS 1.501 0.000 1.501 1.501
78 LEU 132 ILE 0.000 1.488 -1.488 1.488
214 GLN 229 VAL 3.846 5.331 -1.485 1.485
288 LEU 343 VAL 1.328 2.800 -1.472 1.472
167 THR 254 PRO 4.801 3.335 1.466 1.466
103 ARG 354 HIS 4.854 3.391 1.463 1.463
96 ALA 351 PHE 1.455 2.910 -1.454 1.454
295 MET 339 ILE 1.907 0.465 1.442 1.442
161 CYS 165 PHE 0.498 1.920 -1.422 1.422
97 LEU 115 ALA 0.532 1.948 -1.416 1.416
230 LEU 234 LEU 0.000 1.391 -1.391 1.391
79 PRO 132 ILE 1.368 0.000 1.368 1.368
166 MET 292 VAL 0.210 1.570 -1.360 1.360
73 LEU 78 LEU 3.025 4.374 -1.349 1.349
88 VAL 342 PHE 0.425 1.768 -1.343 1.343
141 TRP 147 LEU 3.108 4.430 -1.322 1.322
41 LYS 58 VAL 1.575 0.262 1.314 1.314
166 MET 258 THR 0.139 1.438 -1.299 1.299
170 SER 265 MET 0.841 2.124 -1.284 1.284
35 GLY 319 GLN 1.284 0.000 1.284 1.284
141 TRP 224 THR 4.856 6.113 -1.257 1.257
117 LEU 340 ASP 2.638 1.385 1.253 1.253
152 ILE 156 TYR 2.599 1.355 1.244 1.244
274 MET 278 SER 2.579 1.338 1.241 1.241
166 MET 295 MET 1.230 0.000 1.230 1.230
88 VAL 338 CYS 1.340 0.112 1.228 1.228
393 VAL 394 LYS 1.225 0.000 1.225 1.225
116 ASN 165 PHE 7.651 8.867 -1.216 1.216
140 ASN 223 ILE 3.644 4.846 -1.202 1.202
100 PHE 344 TYR 0.000 1.198 -1.198 1.198
212 VAL 228 ASP 3.266 4.435 -1.169 1.169
320 SER 322 VAL 1.164 0.000 1.164 1.164
100 PHE 101 LEU 1.163 0.000 1.163 1.163
85 VAL 334 THR 2.414 1.251 1.163 1.163
127 TRP 150 VAL 0.056 1.218 -1.162 1.162
349 HIS 353 ASP 4.653 5.814 -1.161 1.161
319 GLN 322 VAL 0.000 1.142 -1.142 1.142
176 VAL 183 HIS 1.920 3.057 -1.138 1.138
145 GLU 214 GLN 1.169 0.034 1.136 1.136
173 ARG 265 MET 1.392 2.516 -1.124 1.124
156 TYR 209 LEU 1.568 0.457 1.111 1.111
297 LEU 301 THR 1.211 0.103 1.108 1.108
217 PHE 223 ILE 3.711 2.619 1.092 1.092
113 TYR 172 GLN 1.347 0.256 1.090 1.090
69 LEU 321 HIS 0.000 1.089 -1.089 1.089
326 TYR 330 LEU 6.820 5.740 1.080 1.080
208 PRO 242 TYR 4.772 5.851 -1.078 1.078
148 CYS 213 LYS 1.014 2.068 -1.054 1.054
85 VAL 125 VAL 0.647 1.693 -1.046 1.046
130 LEU 141 TRP 1.579 0.541 1.038 1.038
43 ASP 58 VAL 1.695 0.658 1.036 1.036
138 GLY 223 ILE 1.036 0.000 1.036 1.036
90 LEU 122 LEU 1.307 2.342 -1.034 1.034
104 THR 111 VAL 1.135 2.169 -1.033 1.033
344 TYR 345 TYR 1.031 0.000 1.031 1.031
117 LEU 165 PHE 2.543 1.517 1.025 1.025
159 MET 333 SER 1.016 0.000 1.016 1.016
170 SER 258 THR 1.910 2.919 -1.009 1.009
269 LEU 286 ILE 0.405 1.406 -1.001 1.001
313 LEU 320 SER 0.996 0.000 0.996 0.996
240 PHE 312 PHE 4.727 3.736 0.991 0.991
230 LEU 239 MET 1.875 2.862 -0.988 0.988
269 LEU 274 MET 0.000 0.980 -0.980 0.980
163 ILE 255 ALA 0.000 0.977 -0.977 0.977
128 PHE 155 PHE 0.977 0.000 0.977 0.977
306 LEU 326 TYR 2.302 1.331 0.971 0.971
167 THR 258 THR 2.875 3.844 -0.969 0.969
97 LEU 101 LEU 0.938 1.900 -0.961 0.961
110 ALA 172 GLN 1.129 0.169 0.961 0.961
282 ARG 286 ILE 0.955 0.000 0.955 0.955
216 ILE 225 THR 7.219 8.171 -0.952 0.952
265 MET 289 ILE 0.943 0.000 0.943 0.943
352 ARG 356 LYS 0.820 1.752 -0.932 0.932
131 LYS 326 TYR 0.000 0.923 -0.923 0.923
165 PHE 195 SER 2.752 3.672 -0.919 0.919
78 LEU 331 CYS 1.018 0.104 0.913 0.913
303 SER 304 ASN 0.907 0.000 0.907 0.907
14 ILE 77 PHE 0.907 0.000 0.907 0.907
90 LEU 126 ILE 0.241 1.147 -0.906 0.906
255 ALA 297 LEU 0.000 0.905 -0.905 0.905
206 THR 242 TYR 0.472 1.376 -0.905 0.905
114 MET 169 LEU 2.237 1.336 0.901 0.901
251 PHE 297 LEU 0.000 0.900 -0.900 0.900
149 ASN 213 LYS 4.757 5.654 -0.898 0.898
153 GLY 209 LEU 0.638 1.532 -0.894 0.894
391 THR 392 THR 1.853 2.747 -0.894 0.894
117 LEU 121 ASP 1.629 0.739 0.891 0.891
70 THR 75 THR 0.889 0.000 0.889 0.889
61 VAL 321 HIS 0.000 0.887 -0.887 0.887
303 SER 329 ALA 3.660 4.540 -0.881 0.881
82 TYR 334 THR 0.875 0.000 0.875 0.875
243 PHE 246 LEU 1.116 0.245 0.871 0.871
155 PHE 334 THR 1.651 0.788 0.862 0.862
345 TYR 355 ALA 0.000 0.861 -0.861 0.861
152 ILE 209 LEU 1.049 0.193 0.856 0.856
310 HIS 311 TYR 0.854 0.000 0.854 0.854
150 VAL 154 PHE 0.036 0.885 -0.848 0.848
90 LEU 125 VAL 1.774 0.934 0.840 0.840
130 LEU 147 LEU 2.139 1.300 0.840 0.840
265 MET 286 ILE 0.000 0.835 -0.835 0.835
284 ARG 347 VAL 0.000 0.834 -0.834 0.834
107 LYS 188 ALA 1.827 0.992 0.834 0.834
313 LEU 317 GLN 0.830 0.000 0.830 0.830
348 SER 351 PHE 0.542 1.365 -0.823 0.823
275 ASP 277 ASN 0.000 0.822 -0.822 0.822
72 LYS 77 PHE 1.582 0.762 0.819 0.819
155 PHE 156 TYR 0.518 1.331 -0.813 0.813
42 VAL 59 PHE 2.131 1.319 0.812 0.812
123 LEU 158 ASN 3.958 3.157 0.800 0.800
320 SER 321 HIS 0.000 0.786 -0.786 0.786
121 ASP 337 SER 10.201 9.417 0.784 0.784
316 SER 317 GLN 0.784 0.000 0.784 0.784
42 VAL 58 VAL 1.021 0.238 0.783 0.783
66 ALA 221 LEU 0.783 0.000 0.783 0.783
237 GLY 315 LYS 0.769 0.000 0.769 0.769
319 GLN 321 HIS 0.765 0.000 0.765 0.765
343 VAL 344 TYR 0.749 0.000 0.749 0.749
345 TYR 356 LYS 0.000 0.749 -0.749 0.749
139 ASN 223 ILE 1.473 0.724 0.749 0.749
41 LYS 59 PHE 2.077 1.340 0.737 0.737
297 LEU 302 PRO 0.781 0.046 0.735 0.735
140 ASN 224 THR 6.317 5.584 0.733 0.733
5 SER 8 TRP 0.724 0.000 0.724 0.724
299 CYS 336 ASN 2.706 3.426 -0.720 0.720
97 LEU 118 ALA 0.230 0.948 -0.718 0.718
124 SER 158 ASN 4.192 3.480 0.712 0.712
175 TRP 179 ASN 1.972 2.682 -0.709 0.709
62 ASP 64 PHE 0.468 1.177 -0.709 0.709
113 TYR 191 ALA 5.262 4.556 0.707 0.707
161 CYS 198 ILE 0.074 0.772 -0.697 0.697
74 THR 78 LEU 1.047 0.350 0.697 0.697
228 ASP 311 TYR 0.695 0.000 0.695 0.695
239 MET 311 TYR 1.297 1.989 -0.692 0.692
82 TYR 331 CYS 0.691 0.000 0.691 0.691
298 ILE 332 LEU 0.689 0.000 0.689 0.689
217 PHE 224 THR 2.263 1.582 0.681 0.681
57 THR 59 PHE 1.263 0.584 0.679 0.679
314 ILE 320 SER 0.678 0.000 0.678 0.678
341 PRO 351 PHE 0.000 0.678 -0.678 0.678
115 ALA 345 TYR 0.676 0.000 0.676 0.676
86 PHE 128 PHE 0.675 0.000 0.675 0.675
244 LEU 248 ILE 1.057 1.732 -0.675 0.675
296 TYR 301 THR 0.669 0.008 0.661 0.661
234 LEU 239 MET 1.844 1.184 0.661 0.661
323 TYR 326 TYR 0.648 0.000 0.648 0.648
212 VAL 229 VAL 5.867 6.512 -0.645 0.645
234 LEU 238 ASP 0.907 1.548 -0.640 0.640
244 LEU 308 VAL 0.853 0.213 0.640 0.640
266 ILE 286 ILE 0.000 0.638 -0.638 0.638
153 GLY 206 THR 1.691 2.327 -0.636 0.636
85 VAL 338 CYS 3.816 3.180 0.636 0.636
108 HIS 111 VAL 0.886 0.252 0.634 0.634
145 GLU 149 ASN 1.250 0.617 0.634 0.634
110 ALA 169 LEU 1.451 2.084 -0.633 0.633
163 ILE 254 PRO 0.365 0.998 -0.633 0.633
40 GLY 60 SER 0.371 1.003 -0.632 0.632
178 VAL 268 MET 2.521 1.889 0.632 0.632
116 ASN 195 SER 2.658 3.287 -0.629 0.629
166 MET 300 PHE 0.629 0.000 0.629 0.629
173 ARG 289 ILE 0.000 0.626 -0.626 0.626
124 SER 337 SER 0.440 1.061 -0.621 0.621
162 SER 296 TYR 0.000 0.620 -0.620 0.620
212 VAL 230 LEU 0.057 0.676 -0.619 0.619
117 LEU 169 LEU 0.618 0.000 0.618 0.618
246 LEU 251 PHE 0.723 1.339 -0.616 0.616
303 SER 330 LEU 1.009 1.622 -0.612 0.612
295 MET 298 ILE 0.000 0.611 -0.611 0.611
109 PRO 188 ALA 0.971 0.362 0.609 0.609
42 VAL 57 THR 0.627 0.020 0.607 0.607
160 TYR 251 PHE 0.000 0.603 -0.603 0.603
86 PHE 90 LEU 1.706 1.105 0.602 0.602
73 LEU 328 VAL 0.743 0.142 0.601 0.601
163 ILE 293 LEU 0.000 0.600 -0.600 0.600
8 TRP 298 ILE 0.600 0.000 0.600 0.600
141 TRP 143 TYR 2.621 2.022 0.598 0.598
275 ASP 278 SER 0.224 0.818 -0.594 0.594
295 MET 343 VAL 0.593 0.000 0.593 0.593
149 ASN 209 LEU 0.097 0.685 -0.588 0.588
231 PRO 234 LEU 1.112 0.525 0.587 0.587
59 PHE 216 ILE 0.586 0.000 0.586 0.586
387 SER 388 SER 1.687 1.101 0.585 0.585
214 GLN 226 CYS 1.135 1.720 -0.585 0.585
73 LEU 77 PHE 1.201 1.777 -0.576 0.576
134 TYR 141 TRP 5.471 4.896 0.575 0.575
305 LEU 309 VAL 0.107 0.681 -0.574 0.574
272 SER 282 ARG 0.571 0.000 0.571 0.571
97 LEU 119 LEU 0.228 0.795 -0.567 0.567
170 SER 261 ALA 0.559 1.125 -0.566 0.566
128 PHE 330 LEU 0.000 0.563 -0.563 0.563
173 ARG 292 VAL 0.556 0.000 0.556 0.556
302 PRO 329 ALA 1.902 1.347 0.555 0.555
166 MET 289 ILE 0.000 0.555 -0.555 0.555
184 SER 186 LYS 1.638 2.193 -0.554 0.554
93 ASN 337 SER 2.783 3.338 -0.554 0.554
132 ILE 136 ILE 1.036 1.589 -0.553 0.553
69 LEU 138 GLY 0.550 0.000 0.550 0.550
240 PHE 308 VAL 1.308 0.777 0.531 0.531
223 ILE 225 THR 0.055 0.583 -0.527 0.527
126 ILE 127 TRP 0.000 0.527 -0.527 0.527
69 LEU 221 LEU 0.526 0.000 0.526 0.526
120 ALA 158 ASN 3.515 2.996 0.519 0.519
64 PHE 67 SER 0.624 0.108 0.516 0.516
148 CYS 215 THR 1.072 1.584 -0.512 0.512
82 TYR 83 THR 0.000 0.512 -0.512 0.512
139 ASN 224 THR 0.884 1.392 -0.508 0.508
110 ALA 173 ARG 0.000 0.508 -0.508 0.508
66 ALA 320 SER 0.000 0.505 -0.505 0.505
218 ILE 221 LEU 1.038 0.536 0.502 0.502
345 TYR 346 PHE 0.000 0.499 -0.499 0.499
360 LEU 364 VAL 0.000 0.495 -0.495 0.495
73 LEU 324 ALA 0.170 0.664 -0.494 0.494
364 VAL 368 LYS 0.172 0.665 -0.494 0.494
389 SER 390 SER 1.056 1.549 -0.493 0.493
212 VAL 227 HIS 0.406 0.896 -0.490 0.490
174 TYR 178 VAL 3.958 3.471 0.487 0.487
217 PHE 222 ASN 2.708 2.222 0.486 0.486
216 ILE 227 HIS 1.141 1.624 -0.483 0.483
120 ALA 162 SER 1.750 1.273 0.477 0.477
148 CYS 226 CYS 6.581 6.104 0.477 0.477
170 SER 171 VAL 0.000 0.473 -0.473 0.473
388 SER 389 SER 1.179 0.706 0.473 0.473
154 PHE 158 ASN 5.515 5.043 0.472 0.472
221 LEU 223 ILE 0.878 1.350 -0.472 0.472
357 ASN 360 LEU 0.470 0.000 0.470 0.470
269 LEU 279 GLU 0.000 0.467 -0.467 0.467
160 TYR 304 ASN 0.983 1.449 -0.466 0.466
218 ILE 225 THR 1.545 2.010 -0.465 0.465
245 SER 250 VAL 0.085 0.549 -0.464 0.464
155 PHE 330 LEU 0.059 0.521 -0.462 0.462
38 LEU 227 HIS 0.460 0.000 0.460 0.460
103 ARG 361 CYS 0.453 0.000 0.453 0.453
165 PHE 199 TRP 2.918 2.467 0.451 0.451
81 VAL 335 LEU 0.000 0.450 -0.450 0.450
117 LEU 344 TYR 1.193 1.642 -0.448 0.448
292 VAL 343 VAL 0.826 1.273 -0.448 0.448
165 PHE 198 ILE 2.997 2.551 0.446 0.446
323 TYR 327 ILE 3.348 2.904 0.444 0.444
120 ALA 161 CYS 0.717 0.275 0.443 0.443
363 SER 364 VAL 0.226 0.668 -0.443 0.443
230 LEU 231 PRO 0.410 0.851 -0.441 0.441
153 GLY 210 TYR 7.645 8.082 -0.437 0.437
93 ASN 125 VAL 0.042 0.477 -0.435 0.435
170 SER 262 TYR 4.679 5.111 -0.433 0.433
291 THR 343 VAL 0.171 0.603 -0.431 0.431
177 ILE 268 MET 1.438 1.861 -0.423 0.423
101 LEU 115 ALA 0.000 0.420 -0.420 0.420
149 ASN 214 GLN 1.004 0.585 0.419 0.419
240 PHE 241 ASN 1.344 0.926 0.418 0.418
172 GLN 176 VAL 0.858 0.440 0.418 0.418
8 TRP 295 MET 0.000 0.416 -0.416 0.416
152 ILE 228 ASP 0.414 0.000 0.414 0.414
205 VAL 242 TYR 2.810 3.223 -0.413 0.413
135 HIS 326 TYR 0.000 0.412 -0.412 0.412
309 VAL 313 LEU 0.878 1.289 -0.411 0.411
96 ALA 100 PHE 0.000 0.411 -0.411 0.411
74 THR 75 THR 0.408 0.000 0.408 0.408
214 GLN 227 HIS 5.318 5.721 -0.404 0.404
77 PHE 81 VAL 2.046 2.441 -0.394 0.394
309 VAL 322 VAL 0.392 0.000 0.392 0.392
125 VAL 337 SER 0.315 0.707 -0.392 0.392
142 ILE 143 TYR 4.326 3.937 0.389 0.389
112 ILE 191 ALA 0.880 1.263 -0.383 0.383
143 TYR 147 LEU 1.700 1.317 0.383 0.383
299 CYS 300 PHE 0.515 0.133 0.383 0.383
353 ASP 356 LYS 0.428 0.050 0.377 0.377
109 PRO 172 GLN 2.299 2.674 -0.375 0.375
303 SER 333 SER 2.512 2.883 -0.370 0.370
302 PRO 332 LEU 0.370 0.000 0.370 0.370
174 TYR 265 MET 5.259 4.891 0.368 0.368
166 MET 262 TYR 0.000 0.367 -0.367 0.367
155 PHE 333 SER 0.000 0.364 -0.364 0.364
37 SER 38 LEU 0.363 0.000 0.363 0.363
266 ILE 289 ILE 0.362 0.000 0.362 0.362
92 SER 342 PHE 0.360 0.000 0.360 0.360
253 PHE 257 LEU 3.167 3.527 -0.360 0.360
75 THR 76 VAL 0.504 0.863 -0.359 0.359
163 ILE 250 VAL 1.548 1.189 0.359 0.359
95 MET 351 PHE 0.847 0.492 0.355 0.355
106 LYS 111 VAL 0.000 0.351 -0.351 0.351
61 VAL 65 SER 1.064 0.714 0.350 0.350
172 GLN 175 TRP 0.350 0.000 0.350 0.350
141 TRP 225 THR 0.504 0.158 0.346 0.346
259 ALA 293 LEU 0.470 0.815 -0.345 0.345
128 PHE 131 LYS 0.342 0.000 0.342 0.342
141 TRP 215 THR 1.447 1.108 0.339 0.339
117 LEU 345 TYR 0.335 0.000 0.335 0.335
207 ILE 211 VAL 0.000 0.335 -0.335 0.335
89 GLY 125 VAL 0.830 1.162 -0.332 0.332
262 TYR 286 ILE 0.000 0.330 -0.330 0.330
124 SER 159 MET 0.517 0.187 0.329 0.329
269 LEU 283 LYS 0.000 0.329 -0.329 0.329
101 LEU 102 PHE 1.028 1.356 -0.328 0.328
160 TYR 163 ILE 0.326 0.000 0.326 0.326
218 ILE 223 ILE 5.342 5.668 -0.326 0.326
99 VAL 104 THR 1.994 2.319 -0.325 0.325
96 ALA 341 PRO 0.000 0.324 -0.324 0.324
98 TRP 358 ALA 1.518 1.194 0.324 0.324
157 GLY 206 THR 1.512 1.190 0.322 0.322
243 PHE 307 LEU 3.062 3.384 -0.321 0.321
74 THR 79 PRO 1.644 1.323 0.321 0.321
310 HIS 314 ILE 3.277 2.958 0.319 0.319
135 HIS 330 LEU 0.000 0.319 -0.319 0.319
47 HIS 48 VAL 0.000 0.318 -0.318 0.318
75 THR 138 GLY 0.315 0.000 0.315 0.315
286 ILE 290 VAL 0.181 0.489 -0.308 0.308
313 LEU 322 VAL 0.809 1.116 -0.307 0.307
360 LEU 363 SER 0.426 0.727 -0.301 0.301
248 ILE 253 PHE 2.978 3.278 -0.300 0.300
217 PHE 219 PRO 1.606 1.903 -0.298 0.298
351 PHE 355 ALA 0.106 0.402 -0.296 0.296
108 HIS 109 PRO 3.402 3.697 -0.295 0.295
59 PHE 217 PHE 0.295 0.000 0.295 0.295
69 LEU 75 THR 0.294 0.000 0.294 0.294
70 THR 221 LEU 0.289 0.000 0.289 0.289
272 SER 274 MET 2.161 1.873 0.288 0.288
295 MET 299 CYS 0.287 0.000 0.287 0.287
293 LEU 297 LEU 0.376 0.662 -0.286 0.286
128 PHE 129 PRO 0.699 0.983 -0.284 0.284
39 ILE 60 SER 0.281 0.000 0.281 0.281
89 GLY 338 CYS 2.070 1.789 0.280 0.280
67 SER 72 LYS 0.000 0.277 -0.277 0.277
128 PHE 331 CYS 0.000 0.276 -0.276 0.276
37 SER 320 SER 0.275 0.000 0.275 0.275
247 ALA 308 VAL 0.799 0.524 0.275 0.275
295 MET 344 TYR 0.272 0.000 0.272 0.272
347 VAL 352 ARG 0.000 0.272 -0.272 0.272
243 PHE 308 VAL 0.573 0.304 0.269 0.269
360 LEU 365 ARG 0.000 0.263 -0.263 0.263
167 THR 257 LEU 0.729 0.467 0.263 0.263
174 TYR 268 MET 1.476 1.214 0.262 0.262
227 HIS 228 ASP 0.261 0.000 0.261 0.261
209 LEU 242 TYR 3.761 3.500 0.261 0.261
141 TRP 151 LEU 1.470 1.726 -0.256 0.256
173 ARG 262 TYR 0.256 0.000 0.256 0.256
98 TRP 99 VAL 0.998 0.743 0.255 0.255
163 ILE 251 PHE 0.027 0.280 -0.253 0.253
332 LEU 335 LEU 0.253 0.000 0.253 0.253
202 ILE 250 VAL 0.257 0.509 -0.252 0.252
39 ILE 318 GLY 0.251 0.000 0.251 0.251
160 TYR 296 TYR 0.000 0.251 -0.251 0.251
131 LYS 135 HIS 0.006 0.253 -0.247 0.247
69 LEU 218 ILE 0.247 0.000 0.247 0.247
127 TRP 147 LEU 1.164 1.410 -0.245 0.245
84 ILE 89 GLY 0.099 0.344 -0.245 0.245
348 SER 350 ASP 0.571 0.328 0.243 0.243
68 VAL 324 ALA 0.240 0.000 0.240 0.240
98 TRP 354 HIS 0.000 0.234 -0.234 0.234
94 GLY 122 LEU 0.497 0.729 -0.232 0.232
184 SER 187 LYS 0.232 0.000 0.232 0.232
140 ASN 142 ILE 0.625 0.854 -0.228 0.228
263 VAL 267 ARG 0.607 0.833 -0.226 0.226
203 LEU 210 TYR 0.000 0.224 -0.224 0.224
79 PRO 136 ILE 1.082 0.858 0.224 0.224
343 VAL 347 VAL 0.000 0.223 -0.223 0.223
117 LEU 162 SER 3.309 3.088 0.221 0.221
157 GLY 202 ILE 2.803 3.024 -0.221 0.221
327 ILE 331 CYS 0.000 0.219 -0.219 0.219
177 ILE 269 LEU 0.000 0.219 -0.219 0.219
216 ILE 224 THR 2.890 2.672 0.219 0.219
160 TYR 307 LEU 0.237 0.019 0.218 0.218
209 LEU 246 LEU 0.000 0.217 -0.217 0.217
133 ALA 143 TYR 1.550 1.766 -0.215 0.215
269 LEU 289 ILE 0.215 0.000 0.215 0.215
99 VAL 355 ALA 0.000 0.215 -0.215 0.215
120 ALA 199 TRP 1.745 1.535 0.210 0.210
177 ILE 282 ARG 0.000 0.209 -0.209 0.209
386 TYR 387 SER 3.847 3.638 0.208 0.208
81 VAL 331 CYS 0.665 0.458 0.207 0.207
137 HIS 142 ILE 0.644 0.438 0.206 0.206
38 LEU 320 SER 0.203 0.000 0.203 0.203
100 PHE 111 VAL 3.179 2.977 0.202 0.202
367 VAL 371 GLN 0.201 0.000 0.201 0.201
169 LEU 262 TYR 0.000 0.201 -0.201 0.201
328 VAL 332 LEU 0.000 0.200 -0.200 0.200
116 ASN 199 TRP 2.840 2.641 0.199 0.199
113 TYR 195 SER 1.372 1.177 0.196 0.196
262 TYR 293 LEU 0.673 0.869 -0.196 0.196
43 ASP 45 THR 0.193 0.000 0.193 0.193
312 PHE 316 SER 0.193 0.000 0.193 0.193
172 GLN 187 LYS 0.000 0.188 -0.188 0.188
83 THR 87 VAL 0.279 0.466 -0.187 0.187
77 PHE 78 LEU 0.000 0.186 -0.186 0.186
177 ILE 286 ILE 0.000 0.186 -0.186 0.186
331 CYS 334 THR 0.181 0.000 0.181 0.181
240 PHE 244 LEU 0.966 1.145 -0.179 0.179
167 THR 296 TYR 0.179 0.000 0.179 0.179
100 PHE 118 ALA 0.000 0.176 -0.176 0.176
204 LEU 207 ILE 0.343 0.518 -0.175 0.175
202 ILE 206 THR 0.370 0.196 0.174 0.174
216 ILE 223 ILE 0.620 0.446 0.173 0.173
230 LEU 235 LEU 0.444 0.271 0.173 0.173
84 ILE 88 VAL 0.114 0.287 -0.173 0.173
64 PHE 68 VAL 2.304 2.475 -0.171 0.171
164 LEU 201 LEU 0.170 0.000 0.170 0.170
241 ASN 315 LYS 0.169 0.000 0.169 0.169
148 CYS 149 ASN 0.860 0.691 0.169 0.169
206 THR 209 LEU 0.493 0.326 0.167 0.167
175 TRP 182 GLY 0.000 0.166 -0.166 0.166
108 HIS 172 GLN 0.123 0.289 -0.166 0.166
86 PHE 91 PRO 0.475 0.641 -0.166 0.166
280 LYS 284 ARG 0.000 0.165 -0.165 0.165
85 VAL 90 LEU 0.312 0.477 -0.165 0.165
295 MET 336 ASN 2.908 3.071 -0.163 0.163
366 THR 370 MET 1.022 0.859 0.163 0.163
350 ASP 354 HIS 0.163 0.000 0.163 0.163
37 SER 39 ILE 0.160 0.000 0.160 0.160
169 LEU 173 ARG 0.000 0.159 -0.159 0.159
123 LEU 199 TRP 0.544 0.701 -0.158 0.158
62 ASP 63 GLU 0.186 0.029 0.157 0.157
312 PHE 313 LEU 0.157 0.000 0.157 0.157
166 MET 296 TYR 0.154 0.000 0.154 0.154
167 THR 170 SER 0.000 0.154 -0.154 0.154
85 VAL 335 LEU 1.589 1.435 0.154 0.154
205 VAL 250 VAL 0.144 0.298 -0.154 0.154
97 LEU 100 PHE 0.153 0.000 0.153 0.153
177 ILE 265 MET 1.393 1.543 -0.150 0.150
107 LYS 112 ILE 0.000 0.149 -0.149 0.149
247 ALA 304 ASN 0.080 0.228 -0.147 0.147
61 VAL 66 ALA 0.478 0.331 0.147 0.147
275 ASP 276 GLU 0.000 0.147 -0.147 0.147
168 CYS 194 ILE 0.393 0.538 -0.145 0.145
343 VAL 348 SER 0.000 0.145 -0.145 0.145
218 ILE 220 ALA 0.291 0.147 0.144 0.144
135 HIS 327 ILE 0.000 0.144 -0.144 0.144
253 PHE 254 PRO 1.882 1.742 0.140 0.140
113 TYR 194 ILE 3.678 3.538 0.140 0.140
170 SER 257 LEU 0.000 0.139 -0.139 0.139
192 ILE 196 LEU 0.352 0.213 0.139 0.139
97 LEU 122 LEU 0.416 0.279 0.138 0.138
148 CYS 214 GLN 1.580 1.444 0.137 0.137
287 LYS 291 THR 0.165 0.298 -0.133 0.133
156 TYR 159 MET 1.017 1.149 -0.132 0.132
311 TYR 314 ILE 0.252 0.121 0.131 0.131
137 HIS 140 ASN 0.261 0.391 -0.130 0.130
131 LYS 156 TYR 0.000 0.128 -0.128 0.128
248 ILE 252 LEU 0.285 0.157 0.128 0.128
250 VAL 296 TYR 0.128 0.000 0.128 0.128
100 PHE 112 ILE 0.127 0.000 0.127 0.127
78 LEU 327 ILE 1.773 1.900 -0.127 0.127
127 TRP 130 LEU 1.012 0.887 0.124 0.124
163 ILE 166 MET 0.000 0.124 -0.124 0.124
89 GLY 337 SER 0.122 0.000 0.122 0.122
119 LEU 123 LEU 0.874 0.754 0.121 0.121
110 ALA 114 MET 0.121 0.000 0.121 0.121
16 LEU 19 SER 0.398 0.519 -0.121 0.121
109 PRO 113 TYR 0.043 0.162 -0.119 0.119
86 PHE 87 VAL 0.119 0.000 0.119 0.119
201 LEU 205 VAL 0.536 0.418 0.118 0.118
237 GLY 311 TYR 0.000 0.116 -0.116 0.116
89 GLY 122 LEU 0.000 0.116 -0.116 0.116
123 LEU 126 ILE 0.115 0.000 0.115 0.115
72 LYS 76 VAL 0.114 0.000 0.114 0.114
93 ASN 121 ASP 3.489 3.375 0.114 0.114
133 ALA 137 HIS 0.157 0.271 -0.114 0.114
341 PRO 345 TYR 0.112 0.000 0.112 0.112
164 LEU 202 ILE 1.348 1.236 0.111 0.111
214 GLN 225 THR 0.678 0.789 -0.111 0.111
109 PRO 187 LYS 2.355 2.459 -0.104 0.104
256 PHE 260 SER 0.104 0.000 0.104 0.104
294 ALA 298 ILE 0.103 0.000 0.103 0.103
239 MET 243 PHE 1.208 1.310 -0.102 0.102
109 PRO 191 ALA 1.697 1.595 0.102 0.102
288 LEU 292 VAL 0.099 0.000 0.099 0.099
261 ALA 265 MET 0.285 0.187 0.098 0.098
170 SER 292 VAL 0.097 0.000 0.097 0.097
341 PRO 342 PHE 0.097 0.000 0.097 0.097
145 GLU 215 THR 4.631 4.727 -0.096 0.096
156 TYR 206 THR 0.155 0.062 0.092 0.092
242 TYR 245 SER 0.092 0.000 0.092 0.092
336 ASN 339 ILE 0.000 0.091 -0.091 0.091
3 SER 4 PRO 0.763 0.672 0.091 0.091
269 LEU 285 ALA 0.090 0.000 0.090 0.090
215 THR 224 THR 0.492 0.580 -0.088 0.088
372 VAL 375 THR 0.094 0.006 0.088 0.088
322 VAL 325 LEU 0.087 0.000 0.087 0.087
102 PHE 103 ARG 0.086 0.000 0.086 0.086
90 LEU 91 PRO 1.121 1.036 0.085 0.085
68 VAL 72 LYS 0.000 0.085 -0.085 0.085
93 ASN 341 PRO 4.466 4.381 0.085 0.085
235 LEU 238 ASP 0.841 0.926 -0.085 0.085
67 SER 68 VAL 0.084 0.000 0.084 0.084
310 HIS 322 VAL 0.000 0.083 -0.083 0.083
151 LEU 152 ILE 0.000 0.082 -0.082 0.082
340 ASP 341 PRO 0.914 0.995 -0.081 0.081
170 SER 344 TYR 0.081 0.000 0.081 0.081
156 TYR 303 SER 0.000 0.080 -0.080 0.080
189 ASN 192 ILE 0.103 0.022 0.080 0.080
64 PHE 321 HIS 0.079 0.000 0.079 0.079
96 ALA 344 TYR 0.000 0.079 -0.079 0.079
171 VAL 261 ALA 0.078 0.000 0.078 0.078
339 ILE 343 VAL 0.605 0.682 -0.077 0.077
207 ILE 208 PRO 1.277 1.200 0.077 0.077
160 TYR 202 ILE 1.734 1.810 -0.076 0.076
164 LEU 250 VAL 0.076 0.000 0.076 0.076
333 SER 334 THR 0.000 0.076 -0.076 0.076
356 LYS 360 LEU 0.000 0.075 -0.075 0.075
160 TYR 247 ALA 0.000 0.075 -0.075 0.075
148 CYS 227 HIS 0.074 0.000 0.074 0.074
119 LEU 199 TRP 0.327 0.253 0.074 0.074
216 ILE 218 ILE 0.000 0.074 -0.074 0.074
112 ILE 188 ALA 1.501 1.574 -0.073 0.073
173 ARG 343 VAL 0.072 0.000 0.072 0.072
370 MET 374 LEU 0.071 0.000 0.071 0.071
92 SER 93 ASN 0.532 0.461 0.070 0.070
178 VAL 179 ASN 1.928 1.859 0.069 0.069
294 ALA 295 MET 0.000 0.068 -0.068 0.068
156 TYR 160 TYR 2.135 2.067 0.068 0.068
247 ALA 252 LEU 4.326 4.259 0.068 0.068
163 ILE 258 THR 0.000 0.067 -0.067 0.067
215 THR 225 THR 2.499 2.565 -0.066 0.066
139 ASN 225 THR 2.100 2.034 0.066 0.066
19 SER 20 LEU 0.124 0.059 0.066 0.066
242 TYR 246 LEU 4.810 4.875 -0.064 0.064
246 LEU 250 VAL 0.321 0.383 -0.063 0.063
258 THR 262 TYR 0.496 0.435 0.061 0.061
173 ARG 285 ALA 0.000 0.061 -0.061 0.061
95 MET 99 VAL 0.062 0.122 -0.061 0.061
313 LEU 316 SER 0.000 0.060 -0.060 0.060
163 ILE 167 THR 0.000 0.059 -0.059 0.059
80 ILE 84 ILE 0.551 0.493 0.059 0.059
158 ASN 199 TRP 1.571 1.629 -0.058 0.058
255 ALA 258 THR 0.012 0.070 -0.058 0.058
301 THR 302 PRO 1.084 1.026 0.058 0.058
92 SER 338 CYS 0.283 0.340 -0.057 0.057
255 ALA 293 LEU 0.000 0.056 -0.056 0.056
38 LEU 323 TYR 0.055 0.000 0.055 0.055
209 LEU 243 PHE 1.182 1.237 -0.054 0.054
316 SER 319 GLN 0.000 0.053 -0.053 0.053
216 ILE 228 ASP 0.053 0.000 0.053 0.053
160 TYR 206 THR 0.000 0.052 -0.052 0.052
238 ASP 241 ASN 0.077 0.026 0.052 0.052
83 THR 88 VAL 0.000 0.051 -0.051 0.051
163 ILE 304 ASN 0.050 0.000 0.050 0.050
76 VAL 80 ILE 0.523 0.572 -0.049 0.049
95 MET 358 ALA 0.000 0.048 -0.048 0.048
198 ILE 202 ILE 0.071 0.119 -0.048 0.048
213 LYS 229 VAL 0.048 0.000 0.048 0.048
124 SER 155 PHE 0.048 0.000 0.048 0.048
78 LEU 79 PRO 0.964 0.917 0.048 0.048
66 ALA 71 GLY 0.063 0.108 -0.046 0.046
262 TYR 265 MET 2.417 2.462 -0.045 0.045
84 ILE 338 CYS 0.044 0.000 0.044 0.044
190 ILE 194 ILE 0.831 0.788 0.043 0.043
231 PRO 233 GLN 0.042 0.000 0.042 0.042
69 LEU 225 THR 0.042 0.000 0.042 0.042
124 SER 334 THR 0.000 0.041 -0.041 0.041
302 PRO 306 LEU 0.040 0.000 0.040 0.040
248 ILE 254 PRO 0.127 0.166 -0.039 0.039
167 THR 171 VAL 0.052 0.091 -0.039 0.039
194 ILE 198 ILE 0.666 0.705 -0.039 0.039
215 THR 226 CYS 0.054 0.091 -0.038 0.038
299 CYS 329 ALA 0.260 0.296 -0.036 0.036
122 LEU 126 ILE 0.372 0.337 0.034 0.034
249 GLY 254 PRO 2.077 2.112 -0.034 0.034
295 MET 300 PHE 0.034 0.000 0.034 0.034
99 VAL 103 ARG 0.150 0.117 0.033 0.033
144 GLY 215 THR 0.488 0.456 0.033 0.033
168 CYS 198 ILE 0.838 0.805 0.033 0.033
279 GLU 283 LYS 5.371 5.339 0.032 0.032
362 ARG 366 THR 0.031 0.000 0.031 0.031
129 PRO 130 LEU 0.000 0.028 -0.028 0.028
62 ASP 65 SER 0.483 0.455 0.028 0.028
61 VAL 69 LEU 0.027 0.000 0.027 0.027
218 ILE 219 PRO 0.420 0.393 0.027 0.027
125 VAL 338 CYS 0.000 0.025 -0.025 0.025
335 LEU 339 ILE 0.025 0.000 0.025 0.025
41 LYS 43 ASP 0.024 0.000 0.024 0.024
108 HIS 110 ALA 1.569 1.545 0.024 0.024
96 ALA 118 ALA 0.406 0.430 -0.023 0.023
88 VAL 92 SER 0.000 0.022 -0.022 0.022
306 LEU 329 ALA 0.805 0.825 -0.020 0.020
251 PHE 252 LEU 1.529 1.549 -0.020 0.020
265 MET 268 MET 0.020 0.000 0.020 0.020
268 MET 271 SER 0.006 0.026 -0.019 0.019
370 MET 373 SER 0.039 0.058 -0.019 0.019
299 CYS 339 ILE 0.207 0.189 0.018 0.018
114 MET 117 LEU 0.000 0.018 -0.018 0.018
235 LEU 311 TYR 0.000 0.018 -0.018 0.018
244 LEU 249 GLY 0.000 0.018 -0.018 0.018
152 ILE 157 GLY 0.017 0.000 0.017 0.017
373 SER 376 SER 0.013 0.000 0.013 0.013
112 ILE 192 ILE 0.888 0.876 0.012 0.012
205 VAL 246 LEU 1.287 1.298 -0.011 0.011
179 ASN 180 PRO 0.126 0.138 -0.011 0.011
376 SER 377 LYS 0.019 0.008 0.011 0.011
291 THR 295 MET 0.000 0.010 -0.010 0.010
81 VAL 85 VAL 0.241 0.231 0.010 0.010
188 ALA 189 ASN 0.000 0.008 -0.008 0.008
300 PHE 304 ASN 0.465 0.457 0.008 0.008
89 GLY 94 GLY 0.100 0.093 0.008 0.008
164 LEU 198 ILE 1.446 1.454 -0.007 0.007
68 VAL 73 LEU 0.000 0.007 -0.007 0.007
68 VAL 139 ASN 0.007 0.000 0.007 0.007
5 SER 7 ALA 0.007 0.000 0.007 0.007
385 SER 386 TYR 0.000 0.005 -0.005 0.005
112 ILE 195 SER 0.637 0.641 -0.004 0.004
112 ILE 116 ASN 0.626 0.630 -0.003 0.003
164 LEU 254 PRO 0.801 0.804 -0.003 0.003
58 VAL 219 PRO 0.003 0.000 0.003 0.003
262 TYR 344 TYR 0.001 0.000 0.001 0.001
257 LEU 260 SER 0.000 0.000 -0.000 0.000

RRCS change distribution

0.14
Mean ΔRRCS
1.87
Std Dev
0.03
Median

Magnitude classification

26
High (|Δ| ≥ 5.0)
51
Medium (2.6 ≤ |Δ| < 5.0)
699
Low (|Δ| < 2.6)

Methods

RRCS analysis. Residue-Residue Contact Scores (RRCS) quantify pairwise residue contact strength from inter-atomic distances; comparing active and inactive structures predicted by AlphaFold multistate (del Alamo et al., 2022) gives a per-pair ΔRRCS.

Receptor-specific ΔRRCS threshold. |ΔRRCS| ≥ 2.60, 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. The Het count column shows heterozygote allele counts; homozygote counts are uniformly zero across these rare missense variants in the current gnomAD v4 snapshot and are omitted.

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|. Notable contact-score difference between the active and inactive models.

Residues with large ΔRRCS values mark positions whose contact environment differs between the active and inactive models. These positions may be useful candidates for structural interpretation or follow-up variant analysis, but they should not be interpreted as functional proof on their own.

Pathogenicity predictions

AlphaMissense scores estimate the likelihood that a missense substitution disrupts function, based on structural and evolutionary features. The published score thresholds bin each variant as:

  • Pathogenic (score ≥ 0.564): consistent with disruptive substitutions in known disease genes.
  • Ambiguous (0.34–0.563): score does not clearly favor either class.
  • Benign (< 0.34): consistent with tolerated substitutions.

Conservation & population data

Conservation score. How well-preserved a position is across species (0 = variable, 1 = conserved). Highly conserved positions are often functionally important, but conservation alone is not proof of function.

Allele frequency. Population frequency of the variant in gnomAD v4. Rare variants are common across the genome and many are undersampled; rarity alone is not evidence of pathogenicity.

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