ACM3

Gene CHRM3 Acetylcholine receptors (muscarinic) Aminergic receptors UniProt P20309

UniProt ↗ GPCRdb ↗ NCBI Gene ↗

832

Total Contact Pairs

Significant Changes

9.31

Max Increase

-10.29

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.

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	ASN103 (2.39x39)	ARG166 (3.50x50)	0.000	10.291	-10.291	HIGH
2	GLU276	ARG472	9.310	0.000	+9.310	HIGH
3	ASN338	ASN339	8.937	0.000	+8.937	HIGH
4	ASN340	ASP341	8.724	0.000	+8.724	HIGH
5	GLU347	ASN348	7.568	0.000	+7.568	HIGH
6	ILE521	TRP526 (7.35x34)	0.923	7.867	-6.944	HIGH
7	THR175 (34.52x52)	ASP341	0.000	6.864	-6.864	HIGH
8	ARG177 (34.54x54)	GLU486 (6.30x30)	0.000	6.815	-6.815	HIGH
9	MET327	ASP328	6.653	0.000	+6.653	HIGH
10	ASN339	ASN340	6.472	0.000	+6.472	HIGH
11	ASP564	ARG568	6.470	0.000	+6.470	HIGH
12	SER334	ASP335	6.404	0.000	+6.404	HIGH
13	GLN329	ASP330	6.374	0.000	+6.374	HIGH
14	GLU402	ARG403	6.325	0.000	+6.325	HIGH
15	ARG166 (3.50x50)	TYR544 (7.53x53)	6.237	0.000	+6.237	HIGH
16	SER292	TYR293	0.000	6.034	-6.034	HIGH
17	ALA545 (7.54x54)	ARG552 (8.51x51)	0.000	5.950	-5.950	HIGH
18	THR215	GLN224	2.257	8.062	-5.805	HIGH
19	GLU228 (5.35x36)	THR230 (5.37x38)	0.000	5.538	-5.538	HIGH
20	PHE313	PHE315	5.485	0.000	+5.485	HIGH
21	PHE93 (1.57x57)	TYR105 (2.41x41)	2.394	7.415	-5.021	HIGH
22	SER336	TRP337	4.553	0.000	+4.553	MED
23	HIS4	ASN5	4.428	0.000	+4.428	MED
24	TRP207 (4.64x64)	GLU228 (5.35x36)	4.364	0.000	+4.364	MED
25	ASP165 (3.49x49)	ARG180 (34.57x57)	5.799	10.016	-4.217	MED
26	SER349	ASP353	0.000	4.167	-4.167	MED
27	ASP330	HIS331	4.152	0.000	+4.152	MED
28	PHE233 (5.40x41)	ILE237 (5.44x45)	0.000	4.101	-4.101	MED
29	LEU159 (3.43x43)	TYR544 (7.53x53)	3.951	0.000	+3.951	MED
30	TYR573	GLN577	0.000	3.796	-3.796	MED
31	TRP200 (4.57x57)	THR235 (5.42x43)	3.791	0.017	+3.775	MED
32	TYR105 (2.41x41)	THR182 (4.39x39)	0.123	3.751	-3.628	MED
33	ALA545 (7.54x54)	PHE551 (8.50x50)	4.011	0.499	+3.512	MED
34	ARG166 (3.50x50)	ALA489 (6.33x33)	0.000	3.453	-3.453	MED
35	ARG166 (3.50x50)	TYR251 (5.58x58)	3.453	0.000	+3.453	MED
36	TYR241 (5.48x48)	ASN508 (6.52x52)	2.464	5.870	-3.406	MED
37	TYR251 (5.58x58)	SER494 (6.38x38)	0.000	3.405	-3.405	MED
38	PHE225	LEU226	0.000	3.396	-3.396	MED
39	LEU174 (34.51x51)	GLU347	0.000	3.342	-3.342	MED
40	LYS412	SER413	3.306	0.000	+3.306	MED
41	HIS374	SER375	0.815	4.119	-3.304	MED
42	LEU110 (2.46x46)	ASN158 (3.42x42)	3.349	0.059	+3.290	MED
43	ILE170 (3.54x54)	ARG261 (5.68x68)	4.286	7.562	-3.277	MED
44	GLN296	GLN297	0.000	3.179	-3.179	MED
45	MET122 (2.58x57)	TRP531 (7.40x39)	0.906	4.047	-3.141	MED
46	THR75 (1.39x39)	TRP531 (7.40x39)	4.003	7.144	-3.141	MED
47	LYS426	LEU427	3.127	0.000	+3.127	MED
48	ILE496 (6.40x40)	CYS543 (7.52x52)	3.341	0.217	+3.125	MED
49	SER17	SER18	3.121	0.000	+3.121	MED
50	PHE168 (3.52x52)	TYR176 (34.53x53)	10.852	7.806	+3.047	MED
51	VAL399	ASP400	3.162	0.154	+3.008	MED
52	TRP531 (7.40x39)	ILE535 (7.44x43)	3.005	0.000	+3.005	MED
53	ASN6	SER7	0.000	3.005	-3.005	MED
54	TRP504	ASN536	5.795	2.802	+2.994	MED
55	PHE125	TRP531 (7.40x39)	2.553	5.541	-2.989	MED
56	THR126	TRP531 (7.40x39)	0.064	3.021	-2.957	MED
57	GLU354	GLU355	2.953	0.000	+2.953	MED
58	TRP504	CYS533	6.177	9.117	-2.940	MED
59	LEU110 (2.46x46)	TYR544 (7.53x53)	0.255	3.071	-2.816	MED
60	GLN208	LYS213	1.961	4.772	-2.811	MED
61	SER25	ASP26	0.000	2.786	-2.786	MED
62	ASP328	GLN329	2.755	0.000	+2.755	MED
63	ASP114	SER155	3.173	0.447	+2.727	MED
64	TYR507	VAL511	3.952	1.230	+2.721	MED
65	PHE233 (5.40x41)	PHE516	2.684	0.000	+2.684	MED
66	LEU389	GLN390	2.618	0.000	+2.618	MED
67	TYR128	TRP134	1.374	3.985	-2.611	MED
68	LEU546	PHE555	2.610	0.000	+2.610	MED
69	TYR530	TYR534	3.193	0.593	+2.601	MED
70	SER323	SER324	0.544	3.107	-2.564	MED
71	LEU88	PHE555	7.437	4.875	+2.562	MED
72	THR492	CYS547	0.744	3.297	-2.553	MED
73	LEU12	PHE13	2.540	0.000	+2.540	MED
74	SER7	THR8	0.000	2.534	-2.534	MED
75	CYS561	LYS565	0.000	2.533	-2.533	MED
76	SER386	ASP387	4.756	2.238	+2.518	MED
77	PRO541	LEU546	2.500	0.000	+2.500	MED
78	LEU346	GLU347	2.480	0.000	+2.480	MED
79	PHE125	TYR530	6.141	3.733	+2.408	MED
80	ASN153	ALA239	2.550	0.157	+2.393	MED
81	ILE237 (5.44x45)	MET242	5.461	3.070	+2.392	MED
82	TYR251 (5.58x58)	TYR544 (7.53x53)	2.391	0.000	+2.391	MED
83	LYS213	GLN224	0.340	2.720	-2.380	MED
84	SER423	PHE424	4.340	1.970	+2.369	MED
85	PHE500	TRP504	4.864	7.222	-2.358	MED
86	LEU159 (3.43x43)	ASN540	2.355	0.000	+2.355	MED
87	ASP148	TYR530	2.353	0.000	+2.353	MED
88	LEU226	THR232	2.949	5.297	-2.347	MED
89	PRO229	ASN514	0.000	2.343	-2.343	MED
90	GLU360	THR361	2.342	0.000	+2.342	MED
91	MET157	ALA192	2.996	0.672	+2.324	MED
92	LEU78	TRP531 (7.40x39)	2.297	0.000	+2.297	MED
93	SER375	THR376	0.000	2.277	-2.277	LOW
94	GLU395	LEU396	2.276	0.000	+2.276	LOW
95	TRP337	ASN339	0.000	2.276	-2.276	LOW
96	THR248	LEU497	2.352	0.080	+2.272	LOW
97	LEU199	TRP200 (4.57x57)	2.942	0.685	+2.257	LOW
98	ILE162	ARG166 (3.50x50)	2.421	0.166	+2.255	LOW
99	GLN269	ARG480	0.049	2.276	-2.227	LOW
100	THR8	THR9	2.558	0.357	+2.201	LOW

Transmembrane domain analysis

Active-favoring residues form stronger contacts in the active state (positive ΔRRCS). Inactive-favoring residues form stronger contacts in the inactive state (negative ΔRRCS). Only residues with |ΔRRCS| ≥ 2.28 are shown (per-receptor significance threshold = max(mean(|Δ|) + σ, 0.2)).

Segment	Range	Active-favoring residues	Count	Inactive-favoring residues	Count
TM1	75-93	-	0	93 (-5.0), 75 (-3.1)	2
TM2	103-122	110 (3.3)	1	103 (-10.3), 105 (-5.0), 122 (-3.1)	3
TM3	158-170	159 (4.0), 158 (3.3), 168 (3.0)	3	166 (-10.3), 165 (-4.2), 170 (-3.3)	3
TM4	182-207	207 (4.4), 200 (3.8)	2	182 (-3.6)	1
TM5	228-261	235 (3.8), 251 (3.5)	2	228 (-5.5), 230 (-5.5), 233 (-4.1), 237 (-4.1), 241 (-3.4), 261 (-3.3)	6
TM6	486-508	496 (3.1)	1	486 (-6.8), 489 (-3.5), 508 (-3.4), 494 (-3.4)	4
TM7	526-545	544 (6.2), 543 (3.1), 535 (3.0)	3	526 (-6.9), 545 (-5.9), 531 (-3.1)	3
Intracellular / Extracellular loops & H8
ICL1	-	-	0	-	0
ICL2	174-180	176 (3.0)	1	175 (-6.9), 177 (-6.8), 180 (-4.2), 174 (-3.3)	4
ICL3	276-472	276 (9.3), 472 (9.3), 338 (8.9), 339 (8.9), 340 (8.7), 341 (8.7), 347 (7.6), 348 (7.6), 327 (6.7), 328 (6.7), 334 (6.4), 335 (6.4), 329 (6.4), 330 (6.4), 402 (6.3), 403 (6.3), 313 (5.5), 315 (5.5), 336 (4.6), 337 (4.6), 331 (4.2), 412 (3.3), 413 (3.3), 426 (3.1), 427 (3.1), 399 (3.0), 400 (3.0)	27	292 (-6.0), 293 (-6.0), 349 (-4.2), 353 (-4.2), 374 (-3.3), 375 (-3.3), 296 (-3.2), 297 (-3.2)	8
ECL1	-	-	0	-	0
ECL2	215-226	-	0	215 (-5.8), 224 (-5.8), 225 (-3.4), 226 (-3.4)	4
ECL3	521-521	-	0	521 (-6.9)	1
H8	551-552	551 (3.5)	1	552 (-5.9)	1

Interactive visualizations

ΔRRCS distribution

Active vs inactive comparison

Residue-wise changes

TM domain breakdown

Variants of interest

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

Position	Protein change	DNA change	Allele freq	Het / Hom	ΔRRCS	AM score	Pathogenicity	Conservation	dbSNP
103	p.Asn103Ser	c.308A>G	6.16e-06	9 / 0	10.29	0.229	BENIGN	0.69	rs777454212
472	p.Arg472Thr	c.1415G>C	6.84e-07	1 / 0	9.31	0.867	PATHOGENIC	0.69
276	p.Glu276Asp	c.828G>C	8.28e-05	121 / 0	9.31	0.095	BENIGN	0.45	rs200451506
472	p.Arg472Lys	c.1415G>A	1.37e-06	2 / 0	9.31	-	nan	-	rs760141928
338	p.Asn338Asp	c.1012A>G	5.48e-06	8 / 0	8.94	0.830	PATHOGENIC	0.47	rs767786650
339	p.Asn339Asp	c.1015A>G	1.37e-06	2 / 0	8.94	0.564	PATHOGENIC	0.45
339	p.Asn339Ser	c.1016A>G	2.74e-06	4 / 0	8.94	-	nan	-	rs202235271
339	p.Asn339Thr	c.1016A>C	2.63e-05	4 / 0	8.94	-	nan	-	rs202235271
339	p.Asn339Lys	c.1017C>A	2.19e-05	32 / 0	8.94	-	nan	-	rs149178518
340	p.Asn340Ser	c.1019A>G	6.85e-07	1 / 0	8.72	0.231	BENIGN	0.44
340	p.Asn340Lys	c.1020T>A	6.85e-07	1 / 0	8.72	-	nan	-
347	p.Glu347Gln	c.1039G>C	2.06e-06	3 / 0	7.57	0.329	BENIGN	0.41	rs1233638355
347	p.Glu347Asp	c.1041G>C	2.63e-05	4 / 0	7.57	-	nan	-	rs1382621395
521	p.Ile521Val	c.1561A>G	1.16e-05	17 / 0	6.94	0.093	BENIGN	0.79
175	p.Thr175Met	c.524C>T	1.16e-05	15 / 1	6.86	0.765	PATHOGENIC	0.73	rs760535785
177	p.Arg177Gly	c.529C>G	6.57e-06	1 / 0	6.82	0.996	PATHOGENIC	0.69	rs1680104037
177	p.Arg177Gln	c.530G>A	4.10e-06	6 / 0	6.82	-	nan	-	rs772370324
177	p.Arg177Leu	c.530G>T	6.84e-07	1 / 0	6.82	-	nan	-
177	p.Arg177Pro	c.530G>C	6.84e-07	1 / 0	6.82	-	nan	-	rs772370324
328	p.Asp328Asn	c.982G>A	6.57e-06	1 / 0	6.65	0.099	BENIGN	0.47	rs914082009
327	p.Met327Leu	c.979A>T	3.42e-06	5 / 0	6.65	0.079	BENIGN	0.29
327	p.Met327Ile	c.981G>A	6.84e-07	1 / 0	6.65	-	nan	-	rs1194552689
328	p.Asp328Gly	c.983A>G	1.37e-06	2 / 0	6.65	-	nan	-
328	p.Asp328Glu	c.984C>A	4.10e-06	6 / 0	6.65	-	nan	-
564	p.Asp564Val	c.1691A>T	6.84e-07	1 / 0	6.47	0.245	BENIGN	0.46
568	p.Arg568Lys	c.1703G>A	2.74e-06	4 / 0	6.47	0.082	BENIGN	0.61
564	p.Asp564Glu	c.1692C>A	6.85e-07	1 / 0	6.47	-	nan	-
335	p.Asp335Gly	c.1004A>G	6.84e-07	1 / 0	6.40	0.603	PATHOGENIC	0.40	rs2103051634
334	p.Ser334Gly	c.1000A>G	3.42e-06	5 / 0	6.40	0.172	BENIGN	0.43	rs1189025294
334	p.Ser334Asn	c.1001G>A	4.11e-06	6 / 0	6.40	-	nan	-	rs137992669
329	p.Gln329Arg	c.986A>G	4.79e-06	7 / 0	6.37	0.080	BENIGN	0.42	rs762974054
402	p.Glu402Asp	c.1206G>T	6.85e-07	1 / 0	6.33	0.086	BENIGN	0.46	rs892379527
403	p.Arg403Lys	c.1208G>A	3.08e-05	45 / 0	6.33	0.058	BENIGN	0.40	rs200350916
552	p.Arg552Lys	c.1655G>A	6.84e-07	1 / 0	5.95	0.309	BENIGN	0.80
228	p.Glu228Lys	c.682G>A	6.84e-07	1 / 0	5.54	0.406	AMBIGUOUS	0.60
230	p.Thr230Ala	c.688A>G	6.84e-07	1 / 0	5.54	0.067	BENIGN	0.41
230	p.Thr230Ile	c.689C>T	4.10e-06	6 / 0	5.54	-	nan	-
230	p.Thr230Ser	c.689C>G	1.37e-06	2 / 0	5.54	-	nan	-
313	p.Phe313Ile	c.937T>A	6.84e-07	1 / 0	5.49	0.100	BENIGN	0.43
315	p.Phe315Cys	c.944T>G	6.84e-07	1 / 0	5.49	0.090	BENIGN	0.36
313	p.Phe313Leu	c.939C>G	6.84e-07	1 / 0	5.49	-	nan	-	rs1458030491
105	p.Tyr105Asp	c.313T>G	6.84e-07	1 / 0	5.02	0.990	PATHOGENIC	0.99	rs1290736649
4	p.His4Arg	c.11A>G	2.05e-06	3 / 0	4.43	0.058	BENIGN	0.48
207	p.Trp207Arg	c.619T>C	6.84e-07	1 / 0	4.36	0.998	PATHOGENIC	0.98	rs1365414451
180	p.Arg180Gln	c.539G>A	6.84e-07	1 / 0	4.22	0.957	PATHOGENIC	0.98	rs1487020414
353	p.Asp353Tyr	c.1057G>T	6.91e-07	1 / 0	4.17	0.344	AMBIGUOUS	0.41	rs201087854
353	p.Asp353Asn	c.1057G>A	1.87e-05	27 / 0	4.17	-	nan	-	rs201087854
353	p.Asp353Glu	c.1059C>G	1.38e-06	2 / 0	4.17	-	nan	-	rs139009806
331	p.His331Tyr	c.991C>T	6.84e-07	1 / 0	4.15	0.102	BENIGN	0.39
237	p.Ile237Leu	c.709A>C	6.84e-07	1 / 0	4.10	0.165	BENIGN	0.73	rs1173536206
237	p.Ile237Val	c.709A>G	6.84e-07	1 / 0	4.10	-	nan	-	rs1173536206
577	p.Gln577Glu	c.1729C>G	6.84e-07	1 / 0	3.80	0.105	BENIGN	0.68	rs1383151839
573	p.Tyr573Phe	c.1718A>T	6.84e-07	1 / 0	3.80	0.092	BENIGN	0.71
577	p.Gln577His	c.1731G>C	6.84e-07	1 / 0	3.80	-	nan	-
182	p.Thr182Pro	c.544A>C	6.84e-07	1 / 0	3.63	0.075	BENIGN	0.63
182	p.Thr182Ala	c.544A>G	6.84e-07	1 / 0	3.63	-	nan	-
182	p.Thr182Lys	c.545C>A	6.84e-07	1 / 0	3.63	-	nan	-
551	p.Phe551Leu	c.1653C>G	6.84e-07	1 / 0	3.51	1.000	PATHOGENIC	0.97
489	p.Ala489Val	c.1466C>T	6.84e-07	1 / 0	3.45	0.919	PATHOGENIC	0.75
174	p.Leu174Phe	c.520C>T	6.84e-07	1 / 0	3.34	0.970	PATHOGENIC	0.92
412	p.Lys412Asn	c.1236G>T	1.37e-06	2 / 0	3.31	0.149	BENIGN	0.38	rs1007638498
413	p.Ser413Cys	c.1237A>T	6.85e-07	1 / 0	3.31	0.075	BENIGN	0.39
413	p.Ser413Gly	c.1237A>G	6.85e-07	1 / 0	3.31	-	nan	-
413	p.Ser413Arg	c.1239C>G	1.37e-06	2 / 0	3.31	-	nan	-	rs1426870767
375	p.Ser375Asn	c.1124G>A	6.93e-07	1 / 0	3.30	0.084	BENIGN	0.39	rs1334668008
375	p.Ser375Ile	c.1124G>T	6.93e-07	1 / 0	3.30	-	nan	-	rs1334668008
375	p.Ser375Arg	c.1125C>A	4.16e-06	6 / 0	3.30	-	nan	-	rs961905952
170	p.Ile170Thr	c.509T>C	6.84e-07	1 / 0	3.28	0.977	PATHOGENIC	0.81	rs1380703170
261	p.Arg261His	c.782G>A	4.79e-06	7 / 0	3.28	0.940	PATHOGENIC	0.92	rs753237593
297	p.Gln297His	c.891G>T	6.84e-07	1 / 0	3.18	0.120	BENIGN	0.40
75	p.Thr75Met	c.224C>T	2.74e-06	4 / 0	3.14	0.367	AMBIGUOUS	0.59	rs1221241600
426	p.Lys426Glu	c.1276A>G	2.74e-06	4 / 0	3.13	0.128	BENIGN	0.43	rs1680173991
496	p.Ile496Asn	c.1487T>A	6.57e-06	1 / 0	3.12	0.999	PATHOGENIC	0.98	rs144917572
543	p.Cys543Phe	c.1628G>T	1.37e-06	2 / 0	3.12	0.956	PATHOGENIC	0.91
496	p.Ile496Met	c.1488C>G	6.57e-06	1 / 0	3.12	-	nan	-	rs1680192976
17	p.Ser17Gly	c.49A>G	6.84e-07	1 / 0	3.12	0.084	BENIGN	0.66
18	p.Ser18Thr	c.52T>A	3.42e-06	5 / 0	3.12	0.069	BENIGN	0.52	rs1275601828
17	p.Ser17Thr	c.50G>C	1.37e-06	2 / 0	3.12	-	nan	-	rs1244235649
18	p.Ser18Tyr	c.53C>A	3.42e-06	5 / 0	3.12	-	nan	-	rs369433508
18	p.Ser18Cys	c.53C>G	1.37e-06	2 / 0	3.12	-	nan	-	rs369433508
168	p.Phe168Leu	c.502T>C	6.57e-06	1 / 0	3.05	0.875	PATHOGENIC	0.86	rs1680101823
176	p.Tyr176Phe	c.527A>T	6.84e-07	1 / 0	3.05	0.849	PATHOGENIC	1.00
168	p.Phe168Ser	c.503T>C	6.84e-07	1 / 0	3.05	-	nan	-
176	p.Tyr176Cys	c.527A>G	1.37e-06	2 / 0	3.05	-	nan	-
399	p.Val399Leu	c.1195G>T	2.05e-06	3 / 0	3.01	0.072	BENIGN	0.35	rs1368746636
535	p.Ile535Leu	c.1603A>C	3.42e-06	5 / 0	3.01	0.195	BENIGN	0.74	rs772511456

Complete RRCS results

Res1	AA1	Res2	AA2	Active RRCS	Inactive RRCS	ΔRRCS	\|ΔRRCS\|
103	ASN	166	ARG	0.000	10.291	-10.291	10.291
276	GLU	472	ARG	9.310	0.000	9.310	9.310
338	ASN	339	ASN	8.937	0.000	8.937	8.937
340	ASN	341	ASP	8.724	0.000	8.724	8.724
347	GLU	348	ASN	7.568	0.000	7.568	7.568
521	ILE	526	TRP	0.923	7.867	-6.944	6.944
175	THR	341	ASP	0.000	6.864	-6.864	6.864
177	ARG	486	GLU	0.000	6.815	-6.815	6.815
327	MET	328	ASP	6.653	0.000	6.653	6.653
339	ASN	340	ASN	6.472	0.000	6.472	6.472
564	ASP	568	ARG	6.470	0.000	6.470	6.470
334	SER	335	ASP	6.404	0.000	6.404	6.404
329	GLN	330	ASP	6.374	0.000	6.374	6.374
402	GLU	403	ARG	6.325	0.000	6.325	6.325
166	ARG	544	TYR	6.237	0.000	6.237	6.237
292	SER	293	TYR	0.000	6.034	-6.034	6.034
545	ALA	552	ARG	0.000	5.950	-5.950	5.950
215	THR	224	GLN	2.257	8.062	-5.805	5.805
228	GLU	230	THR	0.000	5.538	-5.538	5.538
313	PHE	315	PHE	5.485	0.000	5.485	5.485
93	PHE	105	TYR	2.394	7.415	-5.021	5.021
336	SER	337	TRP	4.553	0.000	4.553	4.553
4	HIS	5	ASN	4.428	0.000	4.428	4.428
207	TRP	228	GLU	4.364	0.000	4.364	4.364
165	ASP	180	ARG	5.799	10.016	-4.217	4.217
349	SER	353	ASP	0.000	4.167	-4.167	4.167
330	ASP	331	HIS	4.152	0.000	4.152	4.152
233	PHE	237	ILE	0.000	4.101	-4.101	4.101
159	LEU	544	TYR	3.951	0.000	3.951	3.951
573	TYR	577	GLN	0.000	3.796	-3.796	3.796
200	TRP	235	THR	3.791	0.017	3.775	3.775
105	TYR	182	THR	0.123	3.751	-3.628	3.628
545	ALA	551	PHE	4.011	0.499	3.512	3.512
166	ARG	489	ALA	0.000	3.453	-3.453	3.453
166	ARG	251	TYR	3.453	0.000	3.453	3.453
241	TYR	508	ASN	2.464	5.870	-3.406	3.406
251	TYR	494	SER	0.000	3.405	-3.405	3.405
225	PHE	226	LEU	0.000	3.396	-3.396	3.396
174	LEU	347	GLU	0.000	3.342	-3.342	3.342
412	LYS	413	SER	3.306	0.000	3.306	3.306
374	HIS	375	SER	0.815	4.119	-3.304	3.304
110	LEU	158	ASN	3.349	0.059	3.290	3.290
170	ILE	261	ARG	4.286	7.562	-3.277	3.277
296	GLN	297	GLN	0.000	3.179	-3.179	3.179
122	MET	531	TRP	0.906	4.047	-3.141	3.141
75	THR	531	TRP	4.003	7.144	-3.141	3.141
426	LYS	427	LEU	3.127	0.000	3.127	3.127
496	ILE	543	CYS	3.341	0.217	3.125	3.125
17	SER	18	SER	3.121	0.000	3.121	3.121
168	PHE	176	TYR	10.852	7.806	3.047	3.047
399	VAL	400	ASP	3.162	0.154	3.008	3.008
531	TRP	535	ILE	3.005	0.000	3.005	3.005
6	ASN	7	SER	0.000	3.005	-3.005	3.005
504	TRP	536	ASN	5.795	2.802	2.994	2.994
125	PHE	531	TRP	2.553	5.541	-2.989	2.989
126	THR	531	TRP	0.064	3.021	-2.957	2.957
354	GLU	355	GLU	2.953	0.000	2.953	2.953
504	TRP	533	CYS	6.177	9.117	-2.940	2.940
110	LEU	544	TYR	0.255	3.071	-2.816	2.816
208	GLN	213	LYS	1.961	4.772	-2.811	2.811
25	SER	26	ASP	0.000	2.786	-2.786	2.786
328	ASP	329	GLN	2.755	0.000	2.755	2.755
114	ASP	155	SER	3.173	0.447	2.727	2.727
507	TYR	511	VAL	3.952	1.230	2.721	2.721
233	PHE	516	PHE	2.684	0.000	2.684	2.684
389	LEU	390	GLN	2.618	0.000	2.618	2.618
128	TYR	134	TRP	1.374	3.985	-2.611	2.611
546	LEU	555	PHE	2.610	0.000	2.610	2.610
530	TYR	534	TYR	3.193	0.593	2.601	2.601
323	SER	324	SER	0.544	3.107	-2.564	2.564
88	LEU	555	PHE	7.437	4.875	2.562	2.562
492	THR	547	CYS	0.744	3.297	-2.553	2.553
12	LEU	13	PHE	2.540	0.000	2.540	2.540
7	SER	8	THR	0.000	2.534	-2.534	2.534
561	CYS	565	LYS	0.000	2.533	-2.533	2.533
386	SER	387	ASP	4.756	2.238	2.518	2.518
541	PRO	546	LEU	2.500	0.000	2.500	2.500
346	LEU	347	GLU	2.480	0.000	2.480	2.480
125	PHE	530	TYR	6.141	3.733	2.408	2.408
153	ASN	239	ALA	2.550	0.157	2.393	2.393
237	ILE	242	MET	5.461	3.070	2.392	2.392
251	TYR	544	TYR	2.391	0.000	2.391	2.391
213	LYS	224	GLN	0.340	2.720	-2.380	2.380
423	SER	424	PHE	4.340	1.970	2.369	2.369
500	PHE	504	TRP	4.864	7.222	-2.358	2.358
159	LEU	540	ASN	2.355	0.000	2.355	2.355
148	ASP	530	TYR	2.353	0.000	2.353	2.353
226	LEU	232	THR	2.949	5.297	-2.347	2.347
229	PRO	514	ASN	0.000	2.343	-2.343	2.343
360	GLU	361	THR	2.342	0.000	2.342	2.342
157	MET	192	ALA	2.996	0.672	2.324	2.324
78	LEU	531	TRP	2.297	0.000	2.297	2.297
375	SER	376	THR	0.000	2.277	-2.277	2.277
395	GLU	396	LEU	2.276	0.000	2.276	2.276
337	TRP	339	ASN	0.000	2.276	-2.276	2.276
248	THR	497	LEU	2.352	0.080	2.272	2.272
199	LEU	200	TRP	2.942	0.685	2.257	2.257
162	ILE	166	ARG	2.421	0.166	2.255	2.255
269	GLN	480	ARG	0.049	2.276	-2.227	2.227
8	THR	9	THR	2.558	0.357	2.201	2.201
175	THR	340	ASN	0.000	2.180	-2.180	2.180
544	TYR	551	PHE	0.000	2.148	-2.148	2.148
89	VAL	544	TYR	0.000	2.119	-2.119	2.119
149	TYR	507	TYR	2.427	0.316	2.111	2.111
13	PHE	14	PRO	2.584	0.488	2.096	2.096
247	MET	497	LEU	0.250	2.322	-2.072	2.072
425	SER	426	LYS	2.043	0.000	2.043	2.043
121	SER	534	TYR	5.668	3.630	2.038	2.038
86	ASN	541	PRO	3.591	5.619	-2.028	2.028
232	THR	515	THR	2.021	0.000	2.021	2.021
225	PHE	232	THR	2.021	0.000	2.021	2.021
171	THR	348	ASN	0.000	2.021	-2.021	2.021
272	GLY	472	ARG	2.011	0.000	2.011	2.011
107	LEU	544	TYR	1.349	3.359	-2.010	2.010
420	PHE	421	PRO	3.327	1.321	2.006	2.006
149	TYR	200	TRP	9.917	7.929	1.988	1.988
325	GLU	326	GLN	1.983	0.000	1.983	1.983
351	SER	352	SER	1.982	0.000	1.982	1.982
173	PRO	178	ALA	0.000	1.977	-1.977	1.977
262	THR	486	GLU	1.918	0.000	1.918	1.918
134	TRP	219	GLY	3.650	5.562	-1.912	1.912
179	LYS	184	ARG	3.986	5.890	-1.904	1.904
261	ARG	483	LEU	0.000	1.902	-1.902	1.902
93	PHE	104	ASN	2.119	4.016	-1.898	1.898
163	SER	251	TYR	1.897	0.000	1.897	1.897
153	ASN	200	TRP	4.296	6.176	-1.880	1.880
303	SER	304	ASN	1.877	0.000	1.877	1.877
160	LEU	243	PRO	1.375	3.250	-1.875	1.875
326	GLN	327	MET	1.874	0.000	1.874	1.874
376	THR	377	ILE	0.000	1.872	-1.872	1.872
102	VAL	181	THR	0.464	2.313	-1.849	1.849
165	ASP	176	TYR	4.919	6.760	-1.840	1.840
387	ASP	388	ASN	1.822	0.000	1.822	1.822
395	GLU	398	MET	0.000	1.816	-1.816	1.816
335	ASP	336	SER	1.795	0.000	1.795	1.795
251	TYR	493	LEU	1.795	0.000	1.795	1.795
21	ILE	22	HIS	0.000	1.795	-1.795	1.795
433	SER	434	ALA	1.794	0.000	1.794	1.794
167	TYR	168	PHE	3.123	1.330	1.793	1.793
208	GLN	224	GLN	5.446	3.663	1.783	1.783
331	HIS	332	SER	1.780	0.000	1.780	1.780
241	TYR	512	LEU	2.101	0.324	1.777	1.777
463	LEU	467	PHE	0.264	2.002	-1.737	1.737
10	SER	11	PRO	0.038	1.770	-1.732	1.732
242	MET	246	ILE	0.000	1.705	-1.705	1.705
223	ILE	225	PHE	4.964	3.264	1.700	1.700
162	ILE	544	TYR	1.686	0.000	1.686	1.686
167	TYR	250	LEU	3.953	2.287	1.667	1.667
165	ASP	166	ARG	0.000	1.658	-1.658	1.658
109	SER	193	TRP	3.427	1.780	1.647	1.647
265	LEU	480	ARG	0.000	1.628	-1.628	1.628
99	LEU	551	PHE	5.747	4.121	1.626	1.626
169	SER	177	ARG	5.638	4.013	1.625	1.625
172	ARG	177	ARG	0.242	1.862	-1.620	1.620
495	ALA	543	CYS	0.000	1.616	-1.616	1.616
109	SER	189	ILE	1.985	3.581	-1.596	1.596
93	PHE	108	LEU	1.748	3.341	-1.593	1.593
439	LYS	440	THR	1.590	0.000	1.590	1.590
223	ILE	226	LEU	1.358	2.949	-1.590	1.590
109	SER	158	ASN	6.606	5.025	1.581	1.581
122	MET	534	TYR	4.745	3.165	1.580	1.580
104	ASN	551	PHE	1.813	0.239	1.574	1.574
523	LYS	527	ASN	1.711	0.139	1.571	1.571
228	GLU	231	ILE	1.254	2.824	-1.569	1.569
129	ILE	531	TRP	0.000	1.564	-1.564	1.564
35	THR	36	HIS	0.000	1.541	-1.541	1.541
85	GLY	541	PRO	2.006	3.545	-1.539	1.539
286	SER	287	SER	1.523	0.000	1.523	1.523
18	SER	19	SER	0.000	1.522	-1.522	1.522
344	ALA	345	SER	1.522	0.000	1.522	1.522
424	PHE	425	SER	2.693	1.177	1.516	1.516
268	LEU	479	LYS	1.515	0.000	1.515	1.515
413	SER	414	VAL	2.178	0.673	1.504	1.504
233	PHE	511	VAL	0.000	1.503	-1.503	1.503
117	ILE	537	SER	2.686	1.187	1.499	1.499
139	LEU	143	LEU	0.000	1.492	-1.492	1.492
290	CYS	291	SER	1.517	0.028	1.489	1.489
255	TYR	259	GLU	3.051	1.565	1.486	1.486
499	ALA	536	ASN	0.071	1.552	-1.482	1.482
226	LEU	515	THR	1.475	0.000	1.475	1.475
225	PHE	231	ILE	2.873	1.400	1.474	1.474
431	LEU	432	GLU	1.461	0.000	1.461	1.461
208	GLN	209	TYR	2.268	3.718	-1.450	1.450
206	PHE	210	PHE	1.448	0.000	1.448	1.448
441	SER	442	ASP	1.785	0.338	1.447	1.447
233	PHE	515	THR	1.494	2.938	-1.444	1.444
174	LEU	344	ALA	0.000	1.436	-1.436	1.436
546	LEU	552	ARG	5.377	3.942	1.435	1.435
515	THR	516	PHE	1.882	0.450	1.432	1.432
536	ASN	540	ASN	3.626	2.205	1.421	1.421
153	ASN	199	LEU	1.487	0.071	1.416	1.416
391	VAL	392	PRO	2.216	0.801	1.415	1.415
240	PHE	508	ASN	10.254	11.665	-1.411	1.411
255	TYR	490	ALA	1.393	0.000	1.393	1.393
153	ASN	196	SER	8.300	6.908	1.392	1.392
434	ALA	435	VAL	1.391	0.000	1.391	1.391
502	ILE	532	LEU	1.371	0.000	1.371	1.371
128	TYR	133	ARG	2.387	3.751	-1.364	1.364
34	VAL	35	THR	0.000	1.336	-1.336	1.336
260	LYS	351	SER	0.000	1.328	-1.328	1.328
191	LEU	195	ILE	0.066	1.377	-1.311	1.311
160	LEU	164	PHE	1.598	0.292	1.306	1.306
232	THR	511	VAL	0.948	2.251	-1.302	1.302
427	LEU	428	PRO	2.154	0.860	1.293	1.293
326	GLN	328	ASP	0.000	1.283	-1.283	1.283
324	SER	325	GLU	2.824	1.542	1.282	1.282
390	GLN	391	VAL	1.276	0.000	1.276	1.276
500	PHE	536	ASN	3.417	4.692	-1.275	1.275
313	PHE	316	THR	0.000	1.269	-1.269	1.269
240	PHE	500	PHE	0.955	2.215	-1.260	1.260
314	TRP	316	THR	1.255	0.000	1.255	1.255
220	GLU	523	LYS	3.318	2.069	1.249	1.249
207	TRP	231	ILE	1.242	0.000	1.242	1.242
332	SER	333	SER	1.235	0.000	1.235	1.235
503	THR	532	LEU	7.733	6.498	1.235	1.235
214	ARG	224	GLN	4.620	3.387	1.233	1.233
220	GLU	222	PHE	2.302	1.093	1.209	1.209
143	LEU	147	ILE	1.207	0.000	1.207	1.207
159	LEU	247	MET	1.801	3.006	-1.205	1.205
307	LYS	308	TYR	1.191	0.000	1.191	1.191
496	ILE	540	ASN	0.000	1.190	-1.190	1.190
545	ALA	555	PHE	0.000	1.185	-1.185	1.185
383	LEU	384	PRO	1.575	0.392	1.183	1.183
110	LEU	114	ASP	2.346	1.163	1.183	1.183
380	SER	381	THR	0.000	1.148	-1.148	1.148
491	GLN	547	CYS	0.000	1.130	-1.130	1.130
86	ASN	115	LEU	1.553	2.680	-1.127	1.127
407	LYS	408	LEU	1.124	0.000	1.124	1.124
510	MET	526	TRP	5.000	6.117	-1.117	1.117
106	PHE	185	ALA	3.014	4.125	-1.111	1.111
507	TYR	533	CYS	2.169	1.063	1.106	1.106
233	PHE	512	LEU	5.054	3.951	1.103	1.103
134	TRP	220	GLU	0.602	1.705	-1.103	1.103
542	VAL	547	CYS	1.100	0.000	1.100	1.100
41	ASN	43	SER	0.000	1.097	-1.097	1.097
155	SER	540	ASN	1.090	0.000	1.090	1.090
262	THR	483	LEU	1.226	2.313	-1.087	1.087
166	ARG	496	ILE	1.083	0.000	1.083	1.083
102	VAL	182	THR	0.491	1.569	-1.078	1.078
240	PHE	241	TYR	3.275	2.201	1.074	1.074
261	ARG	264	GLU	0.394	1.467	-1.073	1.073
547	CYS	552	ARG	1.072	0.000	1.072	1.072
507	TYR	526	TRP	1.952	3.019	-1.067	1.067
517	CYS	520	CYS	3.099	2.043	1.056	1.056
240	PHE	244	VAL	3.360	2.307	1.052	1.052
158	ASN	189	ILE	0.000	1.046	-1.046	1.046
294	GLU	295	LEU	0.000	1.038	-1.038	1.038
445	SER	446	SER	2.038	1.009	1.029	1.029
23	SER	24	PRO	0.411	1.436	-1.025	1.025
200	TRP	239	ALA	1.391	0.368	1.023	1.023
421	PRO	422	LYS	1.018	0.000	1.018	1.018
114	ASP	537	SER	10.919	11.928	-1.009	1.009
159	LEU	500	PHE	1.286	2.285	-0.999	0.999
125	PHE	534	TYR	2.143	3.142	-0.999	0.999
236	ALA	508	ASN	0.155	1.153	-0.998	0.998
540	ASN	544	TYR	0.962	1.956	-0.994	0.994
167	TYR	254	ILE	3.247	2.261	0.986	0.986
260	LYS	264	GLU	4.610	5.592	-0.982	0.982
106	PHE	188	MET	1.381	0.404	0.978	0.978
543	CYS	544	TYR	0.971	0.000	0.971	0.971
401	LEU	402	GLU	0.960	0.000	0.960	0.960
145	LEU	223	ILE	1.334	2.292	-0.959	0.959
248	THR	252	TRP	0.000	0.956	-0.956	0.956
488	LYS	491	GLN	0.000	0.943	-0.943	0.943
411	GLN	412	LYS	0.942	0.000	0.942	0.942
557	MET	561	CYS	0.941	0.000	0.941	0.941
226	LEU	235	THR	0.000	0.939	-0.939	0.939
154	ALA	193	TRP	2.416	3.350	-0.934	0.934
564	ASP	567	LYS	0.948	0.021	0.927	0.927
244	VAL	501	ILE	0.000	0.924	-0.924	0.924
510	MET	529	GLY	1.170	0.248	0.922	0.922
117	ILE	122	MET	4.208	3.287	0.920	0.920
121	SER	144	TRP	2.187	3.105	-0.918	0.918
110	LEU	540	ASN	2.377	1.463	0.914	0.914
103	ASN	180	ARG	5.612	6.525	-0.913	0.913
151	ALA	193	TRP	0.000	0.913	-0.913	0.913
355	GLU	357	ILE	0.000	0.910	-0.910	0.910
159	LEU	496	ILE	0.000	0.905	-0.905	0.905
102	VAL	180	ARG	4.996	5.894	-0.898	0.898
254	ILE	493	LEU	0.969	0.078	0.891	0.891
82	THR	122	MET	1.709	2.583	-0.873	0.873
276	GLU	469	LEU	0.000	0.871	-0.871	0.871
377	ILE	378	LEU	0.731	1.588	-0.858	0.858
149	TYR	223	ILE	5.734	4.881	0.853	0.853
134	TRP	221	CYS	2.348	3.199	-0.851	0.851
134	TRP	144	TRP	6.030	5.180	0.850	0.850
170	ILE	257	GLU	0.673	1.518	-0.845	0.845
496	ILE	544	TYR	2.706	1.865	0.841	0.841
342	ALA	343	ALA	0.839	0.000	0.839	0.839
319	SER	320	TRP	0.000	0.839	-0.839	0.839
345	SER	346	LEU	0.836	0.000	0.836	0.836
142	ASP	224	GLN	0.835	0.000	0.835	0.835
83	ILE	119	VAL	1.913	2.747	-0.835	0.835
82	THR	537	SER	1.873	2.706	-0.833	0.833
242	MET	243	PRO	0.931	1.762	-0.830	0.830
74	LEU	78	LEU	0.882	0.055	0.827	0.827
163	SER	493	LEU	0.000	0.814	-0.814	0.814
208	GLN	214	ARG	5.094	5.900	-0.806	0.806
146	ALA	205	LEU	1.406	0.601	0.805	0.805
144	TRP	530	TYR	0.805	0.000	0.805	0.805
195	ILE	199	LEU	0.000	0.802	-0.802	0.802
29	LEU	30	PRO	1.397	2.196	-0.800	0.800
117	ILE	148	ASP	0.216	1.014	-0.798	0.798
520	CYS	521	ILE	0.000	0.796	-0.796	0.796
125	PHE	527	ASN	2.348	3.142	-0.794	0.794
128	TYR	221	CYS	0.167	0.961	-0.794	0.794
125	PHE	129	ILE	3.330	2.539	0.791	0.791
353	ASP	354	GLU	0.790	0.000	0.790	0.790
90	ILE	94	LYS	0.000	0.776	-0.776	0.776
495	ALA	547	CYS	0.000	0.774	-0.774	0.774
101	THR	104	ASN	3.143	3.915	-0.772	0.772
228	GLU	229	PRO	0.308	1.078	-0.771	0.771
503	THR	535	ILE	1.288	0.518	0.770	0.770
282	HIS	284	THR	0.000	0.763	-0.763	0.763
156	VAL	239	ALA	1.585	0.823	0.763	0.763
99	LEU	550	THR	2.656	1.901	0.756	0.756
14	PRO	15	ASN	0.753	0.000	0.753	0.753
393	GLU	394	GLU	0.752	0.000	0.752	0.752
199	LEU	239	ALA	0.749	0.000	0.749	0.749
484	VAL	488	LYS	0.208	0.954	-0.746	0.746
162	ILE	493	LEU	0.000	0.743	-0.743	0.743
160	LEU	247	MET	2.324	3.065	-0.741	0.741
114	ASP	540	ASN	5.618	4.881	0.737	0.737
587	GLU	588	GLN	0.730	0.000	0.730	0.730
128	TYR	523	LYS	1.628	2.358	-0.730	0.730
432	GLU	433	SER	1.251	0.523	0.729	0.729
141	CYS	214	ARG	1.217	0.489	0.728	0.728
164	PHE	168	PHE	1.251	1.975	-0.725	0.725
90	ILE	112	CYS	0.156	0.880	-0.724	0.724
419	SER	420	PHE	0.377	1.099	-0.722	0.722
230	THR	231	ILE	0.000	0.720	-0.720	0.720
503	THR	536	ASN	4.421	5.139	-0.718	0.718
134	TRP	136	LEU	3.039	2.322	0.717	0.717
410	ALA	411	GLN	0.717	0.000	0.717	0.717
113	ALA	154	ALA	0.717	0.000	0.717	0.717
507	TYR	530	TYR	6.507	7.221	-0.714	0.714
110	LEU	159	LEU	1.741	1.029	0.712	0.712
512	LEU	516	PHE	0.000	0.712	-0.712	0.712
226	LEU	231	ILE	0.000	0.706	-0.706	0.706
211	VAL	213	LYS	0.000	0.699	-0.699	0.699
429	ILE	430	GLN	0.698	0.000	0.698	0.698
142	ASP	208	GLN	3.512	2.819	0.693	0.693
247	MET	251	TYR	0.692	0.000	0.692	0.692
107	LEU	496	ILE	0.000	0.690	-0.690	0.690
106	PHE	162	ILE	1.870	2.560	-0.690	0.690
503	THR	533	CYS	2.374	1.686	0.688	0.688
337	TRP	338	ASN	0.682	0.000	0.682	0.682
51	SER	52	PRO	0.416	1.095	-0.679	0.679
458	PHE	462	THR	0.697	1.373	-0.677	0.677
187	VAL	191	LEU	0.676	0.000	0.676	0.676
476	THR	480	ARG	0.676	0.000	0.676	0.676
89	VAL	545	ALA	0.673	0.000	0.673	0.673
513	VAL	521	ILE	1.621	0.951	0.670	0.670
265	LEU	486	GLU	0.655	0.000	0.655	0.655
217	PRO	220	GLU	0.173	0.824	-0.652	0.652
526	TRP	527	ASN	0.650	0.000	0.650	0.650
282	HIS	283	PRO	1.289	0.647	0.641	0.641
169	SER	180	ARG	0.208	0.849	-0.641	0.641
352	SER	353	ASP	3.637	2.998	0.639	0.639
165	ASP	169	SER	0.638	0.000	0.638	0.638
521	ILE	525	PHE	0.041	0.679	-0.638	0.638
361	THR	365	TYR	0.000	0.637	-0.637	0.637
349	SER	350	ALA	0.633	0.000	0.633	0.633
167	TYR	253	ARG	3.762	4.391	-0.628	0.628
159	LEU	536	ASN	0.619	0.000	0.619	0.619
207	TRP	224	GLN	3.430	4.048	-0.618	0.618
124	LEU	144	TRP	3.727	3.109	0.617	0.617
585	ALA	586	PRO	0.000	0.617	-0.617	0.617
199	LEU	238	ALA	0.616	0.000	0.616	0.616
92	SER	551	PHE	1.242	0.626	0.616	0.616
321	LYS	322	PRO	1.039	0.425	0.613	0.613
204	ILE	223	ILE	1.751	2.364	-0.613	0.613
110	LEU	162	ILE	0.606	0.000	0.606	0.606
361	THR	362	ARG	0.604	0.000	0.604	0.604
214	ARG	216	VAL	0.432	1.036	-0.604	0.604
117	ILE	151	ALA	2.245	1.644	0.601	0.601
522	PRO	524	THR	0.554	1.155	-0.601	0.601
113	ALA	155	SER	1.041	0.448	0.593	0.593
333	SER	335	ASP	0.000	0.591	-0.591	0.591
111	ALA	544	TYR	0.000	0.590	-0.590	0.590
483	LEU	487	LYS	0.587	0.000	0.587	0.587
157	MET	238	ALA	0.583	0.000	0.583	0.583
414	VAL	415	ASP	3.752	4.332	-0.580	0.580
382	LYS	383	LEU	0.579	0.000	0.579	0.579
83	ILE	115	LEU	1.507	2.080	-0.573	0.573
511	VAL	526	TRP	2.938	2.369	0.569	0.569
265	LEU	483	LEU	0.000	0.567	-0.567	0.567
251	TYR	254	ILE	0.556	0.000	0.556	0.556
78	LEU	122	MET	1.355	1.909	-0.554	0.554
96	ASN	99	LEU	2.345	1.790	0.554	0.554
44	ARG	45	ALA	0.000	0.553	-0.553	0.553
548	ASN	551	PHE	1.868	2.419	-0.551	0.551
514	ASN	521	ILE	1.202	1.748	-0.546	0.546
146	ALA	204	ILE	2.181	2.726	-0.545	0.545
106	PHE	158	ASN	0.716	0.173	0.543	0.543
107	LEU	551	PHE	0.653	0.114	0.539	0.539
541	PRO	555	PHE	0.000	0.539	-0.539	0.539
86	ASN	111	ALA	5.875	6.406	-0.531	0.531
105	TYR	189	ILE	2.308	1.780	0.528	0.528
170	ILE	258	THR	0.000	0.528	-0.528	0.528
116	ILE	151	ALA	0.917	0.392	0.525	0.525
216	VAL	224	GLN	0.679	1.203	-0.524	0.524
176	TYR	180	ARG	1.865	1.345	0.520	0.520
85	GLY	555	PHE	0.748	0.231	0.517	0.517
86	ASN	114	ASP	4.532	5.048	-0.516	0.516
20	TRP	21	ILE	0.000	0.514	-0.514	0.514
322	PRO	323	SER	0.000	0.514	-0.514	0.514
357	ILE	361	THR	0.000	0.514	-0.514	0.514
341	ASP	342	ALA	0.512	0.000	0.512	0.512
91	VAL	558	LEU	1.081	1.588	-0.507	0.507
174	LEU	343	ALA	0.000	0.503	-0.503	0.503
96	ASN	98	GLN	2.550	3.053	-0.503	0.503
349	SER	354	GLU	0.000	0.502	-0.502	0.502
245	THR	249	ILE	0.499	0.000	0.499	0.499
197	PHE	201	ALA	1.557	2.053	-0.496	0.496
388	ASN	389	LEU	0.491	0.000	0.491	0.491
163	SER	254	ILE	0.269	0.757	-0.488	0.488
240	PHE	505	THR	3.028	3.513	-0.485	0.485
169	SER	176	TYR	2.051	2.532	-0.482	0.482
145	LEU	222	PHE	2.092	2.572	-0.480	0.480
287	SER	288	ARG	0.478	0.000	0.478	0.478
199	LEU	235	THR	0.477	0.000	0.477	0.477
106	PHE	161	VAL	1.804	2.278	-0.475	0.475
507	TYR	508	ASN	0.157	0.630	-0.473	0.473
157	MET	195	ILE	0.468	0.000	0.468	0.468
89	VAL	555	PHE	3.046	2.580	0.466	0.466
157	MET	160	LEU	0.324	0.787	-0.463	0.463
513	VAL	520	CYS	0.354	0.816	-0.462	0.462
157	MET	196	SER	1.202	0.742	0.460	0.460
226	LEU	511	VAL	0.453	0.000	0.453	0.453
110	LEU	496	ILE	0.000	0.450	-0.450	0.450
82	THR	114	ASP	0.693	1.140	-0.447	0.447
116	ILE	121	SER	0.928	0.482	0.446	0.446
101	THR	103	ASN	0.499	0.944	-0.446	0.446
24	PRO	25	SER	0.680	0.237	0.444	0.444
535	ILE	538	THR	0.442	0.000	0.442	0.442
131	MET	135	ALA	0.929	1.369	-0.440	0.440
127	THR	131	MET	1.078	0.645	0.433	0.433
160	LEU	163	SER	0.432	0.000	0.432	0.432
371	LEU	372	PRO	0.594	0.164	0.430	0.430
72	ALA	126	THR	0.070	0.498	-0.428	0.428
385	SER	386	SER	0.427	0.000	0.427	0.427
75	THR	126	THR	3.973	4.398	-0.425	0.425
181	THR	184	ARG	1.393	1.817	-0.424	0.424
216	VAL	220	GLU	0.421	0.000	0.421	0.421
79	ALA	123	ASN	0.731	1.147	-0.416	0.416
567	LYS	571	GLN	0.044	0.453	-0.409	0.409
145	LEU	530	TYR	0.409	0.000	0.409	0.409
166	ARG	254	ILE	1.144	1.553	-0.409	0.409
501	ILE	505	THR	1.165	0.757	0.408	0.408
99	LEU	554	THR	0.929	0.522	0.406	0.406
92	SER	554	THR	3.611	4.012	-0.401	0.401
128	TYR	220	GLU	1.387	0.987	0.400	0.400
379	ASN	380	SER	0.000	0.400	-0.400	0.400
90	ILE	111	ALA	0.911	0.511	0.399	0.399
148	ASP	534	TYR	6.485	6.086	0.399	0.399
134	TRP	140	ALA	2.653	3.049	-0.396	0.396
113	ALA	193	TRP	3.085	2.689	0.396	0.396
455	PRO	457	SER	0.000	0.395	-0.395	0.395
540	ASN	545	ALA	0.394	0.000	0.394	0.394
134	TRP	141	CYS	7.097	6.705	0.393	0.393
251	TYR	496	ILE	0.392	0.000	0.392	0.392
442	ASP	443	VAL	0.389	0.000	0.389	0.389
86	ASN	537	SER	1.625	2.013	-0.388	0.388
117	ILE	121	SER	0.944	1.331	-0.387	0.387
385	SER	388	ASN	0.000	0.385	-0.385	0.385
82	THR	538	THR	6.851	6.467	0.385	0.385
251	TYR	255	TYR	0.000	0.384	-0.384	0.384
200	TRP	225	PHE	1.316	0.938	0.378	0.378
216	VAL	222	PHE	5.095	4.717	0.377	0.377
120	ILE	147	ILE	0.523	0.897	-0.375	0.375
121	SER	148	ASP	7.229	6.854	0.374	0.374
164	PHE	250	LEU	4.421	4.794	-0.373	0.373
150	VAL	200	TRP	0.693	1.066	-0.373	0.373
21	ILE	23	SER	0.372	0.000	0.372	0.372
106	PHE	180	ARG	0.000	0.370	-0.370	0.370
236	ALA	512	LEU	0.370	0.000	0.370	0.370
163	SER	250	LEU	2.446	2.079	0.367	0.367
114	ASP	544	TYR	0.000	0.366	-0.366	0.366
336	SER	338	ASN	0.000	0.364	-0.364	0.364
122	MET	538	THR	0.003	0.367	-0.364	0.364
99	LEU	104	ASN	5.282	5.645	-0.363	0.363
106	PHE	165	ASP	2.951	3.313	-0.362	0.362
318	LYS	319	SER	0.000	0.361	-0.361	0.361
236	ALA	511	VAL	0.000	0.359	-0.359	0.359
197	PHE	202	PRO	1.670	2.028	-0.358	0.358
213	LYS	215	THR	0.000	0.356	-0.356	0.356
100	LYS	105	TYR	0.000	0.354	-0.354	0.354
82	THR	118	GLY	1.015	1.368	-0.353	0.353
158	ASN	193	TRP	1.084	0.732	0.352	0.352
217	PRO	222	PHE	0.654	1.006	-0.351	0.351
153	ASN	157	MET	2.199	1.848	0.350	0.350
149	TYR	226	LEU	0.000	0.350	-0.350	0.350
3	LEU	4	HIS	0.349	0.000	0.349	0.349
229	PRO	515	THR	2.503	2.154	0.349	0.349
92	SER	558	LEU	1.852	2.198	-0.347	0.347
117	ILE	534	TYR	1.868	1.525	0.343	0.343
164	PHE	246	ILE	1.457	1.115	0.342	0.342
241	TYR	509	ILE	1.237	1.573	-0.336	0.336
300	MET	303	SER	0.000	0.336	-0.336	0.336
539	VAL	543	CYS	0.994	0.661	0.333	0.333
79	ALA	118	GLY	0.587	0.919	-0.332	0.332
422	LYS	423	SER	0.021	0.352	-0.331	0.331
230	THR	515	THR	0.000	0.331	-0.331	0.331
118	GLY	123	ASN	2.014	1.683	0.330	0.330
148	ASP	152	SER	0.897	0.568	0.330	0.330
499	ALA	539	VAL	0.342	0.671	-0.329	0.329
72	ALA	130	ILE	1.523	1.852	-0.329	0.329
238	ALA	243	PRO	1.729	2.057	-0.329	0.329
364	ILE	366	SER	0.328	0.000	0.328	0.328
89	VAL	107	LEU	0.485	0.160	0.325	0.325
73	PHE	77	ILE	2.831	2.514	0.318	0.318
524	THR	525	PHE	0.404	0.720	-0.316	0.316
34	VAL	36	HIS	0.314	0.000	0.314	0.314
244	VAL	247	MET	0.000	0.313	-0.313	0.313
102	VAL	106	PHE	0.000	0.312	-0.312	0.312
138	ASN	214	ARG	13.408	13.720	-0.311	0.311
542	VAL	546	LEU	0.549	0.859	-0.310	0.310
210	PHE	211	VAL	0.003	0.312	-0.309	0.309
98	GLN	550	THR	1.053	1.357	-0.303	0.303
149	TYR	204	ILE	1.111	0.809	0.302	0.302
150	VAL	193	TRP	0.000	0.301	-0.301	0.301
158	ASN	192	ALA	0.340	0.040	0.300	0.300
203	ALA	225	PHE	3.328	3.621	-0.293	0.293
112	CYS	193	TRP	0.349	0.056	0.293	0.293
229	PRO	233	PHE	0.292	0.000	0.292	0.292
89	VAL	541	PRO	0.709	1.000	-0.291	0.291
129	ILE	527	ASN	2.707	2.418	0.288	0.288
87	ILE	115	LEU	0.808	1.093	-0.285	0.285
504	TRP	508	ASN	0.829	0.545	0.284	0.284
26	ASP	27	ALA	0.000	0.282	-0.282	0.282
405	ALA	406	ASP	0.000	0.282	-0.282	0.282
89	VAL	111	ALA	1.021	1.301	-0.279	0.279
79	ALA	122	MET	3.078	3.355	-0.277	0.277
492	THR	496	ILE	0.737	0.462	0.275	0.275
128	TYR	129	ILE	0.275	0.000	0.275	0.275
81	VAL	538	THR	0.990	1.261	-0.271	0.271
175	THR	344	ALA	0.000	0.267	-0.267	0.267
160	LEU	246	ILE	1.298	1.031	0.267	0.267
104	ASN	107	LEU	0.724	0.463	0.262	0.262
231	ILE	235	THR	0.378	0.118	0.259	0.259
153	ASN	195	ILE	0.259	0.000	0.259	0.259
343	ALA	344	ALA	0.258	0.000	0.258	0.258
155	SER	536	ASN	0.443	0.188	0.255	0.255
231	ILE	232	THR	0.254	0.000	0.254	0.254
202	PRO	206	PHE	0.245	0.499	-0.254	0.254
145	LEU	149	TYR	0.337	0.084	0.253	0.253
248	THR	501	ILE	0.000	0.250	-0.250	0.250
278	GLU	279	ASN	0.000	0.250	-0.250	0.250
333	SER	334	SER	0.249	0.000	0.249	0.249
548	ASN	550	THR	1.639	1.887	-0.248	0.248
225	PHE	235	THR	0.248	0.000	0.248	0.248
150	VAL	196	SER	4.215	3.968	0.248	0.248
444	ASN	445	SER	0.246	0.000	0.246	0.246
131	MET	133	ARG	0.067	0.312	-0.246	0.246
177	ARG	482	SER	0.000	0.245	-0.245	0.245
90	ILE	108	LEU	1.716	1.961	-0.244	0.244
114	ASP	117	ILE	0.243	0.000	0.243	0.243
157	MET	243	PRO	0.256	0.018	0.237	0.237
497	LEU	501	ILE	1.068	1.305	-0.237	0.237
103	ASN	177	ARG	0.237	0.000	0.237	0.237
522	PRO	525	PHE	1.373	1.609	-0.236	0.236
339	ASN	342	ALA	0.000	0.236	-0.236	0.236
155	SER	159	LEU	0.236	0.000	0.236	0.236
176	TYR	188	MET	0.402	0.637	-0.235	0.235
207	TRP	210	PHE	0.000	0.234	-0.234	0.234
247	MET	544	TYR	0.233	0.000	0.233	0.233
440	THR	441	SER	1.062	0.830	0.232	0.232
205	LEU	206	PHE	0.149	0.381	-0.231	0.231
240	PHE	504	TRP	3.931	4.162	-0.231	0.231
261	ARG	486	GLU	0.228	0.000	0.228	0.228
94	LYS	100	LYS	3.506	3.734	-0.228	0.228
65	VAL	69	VAL	0.241	0.013	0.228	0.228
141	CYS	222	PHE	0.252	0.479	-0.227	0.227
50	SER	51	SER	0.000	0.226	-0.226	0.226
88	LEU	559	LEU	0.442	0.667	-0.225	0.225
93	PHE	101	THR	0.353	0.128	0.224	0.224
144	TRP	148	ASP	1.214	0.991	0.224	0.224
144	TRP	534	TYR	0.634	0.855	-0.221	0.221
200	TRP	223	ILE	0.247	0.028	0.219	0.219
215	THR	216	VAL	0.218	0.000	0.218	0.218
265	LEU	482	SER	0.218	0.000	0.218	0.218
510	MET	525	PHE	2.607	2.824	-0.217	0.217
291	SER	292	SER	0.312	0.528	-0.216	0.216
288	ARG	289	SER	0.215	0.000	0.215	0.215
260	LYS	355	GLU	0.000	0.215	-0.215	0.215
156	VAL	504	TRP	0.215	0.000	0.215	0.215
356	ASP	359	SER	0.000	0.213	-0.213	0.213
107	LEU	492	THR	0.000	0.213	-0.213	0.213
150	VAL	197	PHE	2.877	3.084	-0.208	0.208
133	ARG	219	GLY	2.284	2.489	-0.205	0.205
128	TYR	219	GLY	0.090	0.294	-0.204	0.204
236	ALA	241	TYR	3.797	3.593	0.204	0.204
156	VAL	243	PRO	1.338	1.136	0.202	0.202
355	GLU	356	ASP	0.201	0.000	0.201	0.201
155	SER	537	SER	0.198	0.000	0.198	0.198
174	LEU	175	THR	0.005	0.203	-0.197	0.197
124	LEU	134	TRP	0.560	0.756	-0.197	0.197
454	LEU	455	PRO	0.648	0.844	-0.195	0.195
378	LEU	379	ASN	0.000	0.195	-0.195	0.195
226	LEU	526	TRP	0.192	0.000	0.192	0.192
90	ILE	115	LEU	0.570	0.762	-0.191	0.191
289	SER	290	CYS	0.292	0.481	-0.189	0.189
415	ASP	416	ASP	0.809	0.998	-0.189	0.189
163	SER	247	MET	1.719	1.905	-0.186	0.186
518	ASP	519	SER	0.356	0.170	0.185	0.185
169	SER	486	GLU	0.000	0.185	-0.185	0.185
252	TRP	253	ARG	0.184	0.000	0.184	0.184
449	LYS	450	SER	0.182	0.000	0.182	0.182
156	VAL	247	MET	0.004	0.186	-0.182	0.182
551	PHE	555	PHE	0.531	0.712	-0.181	0.181
173	PRO	347	GLU	0.000	0.179	-0.179	0.179
168	PHE	172	ARG	0.633	0.454	0.179	0.179
243	PRO	247	MET	0.000	0.179	-0.179	0.179
84	ILE	88	LEU	0.754	0.576	0.179	0.179
207	TRP	212	GLY	0.177	0.000	0.177	0.177
100	LYS	182	THR	0.000	0.176	-0.176	0.176
168	PHE	173	PRO	0.294	0.121	0.173	0.173
349	SER	352	SER	0.000	0.173	-0.173	0.173
265	LEU	479	LYS	0.057	0.229	-0.172	0.172
96	ASN	550	THR	1.295	1.125	0.170	0.170
82	THR	86	ASN	0.589	0.757	-0.168	0.168
91	VAL	95	VAL	0.504	0.338	0.165	0.165
161	VAL	192	ALA	0.161	0.000	0.161	0.161
78	LEU	538	THR	0.986	0.826	0.160	0.160
103	ASN	104	ASN	0.627	0.468	0.159	0.159
498	LEU	502	ILE	1.769	1.610	0.159	0.159
216	VAL	217	PRO	1.098	0.940	0.158	0.158
102	VAL	165	ASP	0.000	0.157	-0.157	0.157
251	TYR	490	ALA	0.000	0.156	-0.156	0.156
107	LEU	162	ILE	0.568	0.413	0.155	0.155
257	GLU	261	ARG	7.632	7.477	0.155	0.155
557	MET	562	GLN	0.154	0.000	0.154	0.154
152	SER	504	TRP	2.297	2.145	0.152	0.152
200	TRP	226	LEU	0.000	0.152	-0.152	0.152
142	ASP	204	ILE	1.067	1.219	-0.152	0.152
89	VAL	551	PHE	1.449	1.298	0.151	0.151
197	PHE	198	VAL	0.331	0.181	0.150	0.150
161	VAL	188	MET	0.854	0.707	0.148	0.148
438	ALA	439	LYS	0.000	0.146	-0.146	0.146
550	THR	554	THR	0.023	0.168	-0.146	0.146
78	LEU	535	ILE	0.247	0.102	0.144	0.144
521	ILE	522	PRO	0.668	0.524	0.144	0.144
119	VAL	120	ILE	0.383	0.527	-0.144	0.144
586	PRO	588	GLN	0.000	0.144	-0.144	0.144
105	TYR	185	ALA	0.000	0.143	-0.143	0.143
117	ILE	152	SER	1.739	1.596	0.143	0.143
474	GLN	478	ARG	0.268	0.410	-0.142	0.142
246	ILE	250	LEU	1.021	0.881	0.139	0.139
124	LEU	136	LEU	0.680	0.814	-0.135	0.135
141	CYS	145	LEU	0.776	0.906	-0.130	0.130
102	VAL	185	ALA	0.787	0.917	-0.130	0.130
166	ARG	493	LEU	0.155	0.283	-0.128	0.128
126	THR	130	ILE	0.844	0.972	-0.128	0.128
142	ASP	214	ARG	7.119	7.247	-0.127	0.127
457	SER	460	GLU	0.000	0.127	-0.127	0.127
83	ILE	87	ILE	0.846	0.720	0.127	0.127
70	PHE	74	LEU	0.195	0.068	0.127	0.127
578	SER	579	VAL	0.277	0.151	0.126	0.126
163	SER	164	PHE	0.124	0.000	0.124	0.124
125	PHE	144	TRP	2.123	2.247	-0.124	0.124
153	ASN	156	VAL	0.122	0.000	0.122	0.122
317	THR	318	LYS	0.000	0.122	-0.122	0.122
251	TYR	497	LEU	0.542	0.664	-0.122	0.122
116	ILE	193	TRP	0.549	0.671	-0.122	0.122
215	THR	222	PHE	0.000	0.122	-0.122	0.122
71	ILE	129	ILE	0.122	0.000	0.122	0.122
556	LYS	560	LEU	0.001	0.122	-0.121	0.121
207	TRP	225	PHE	7.207	7.327	-0.120	0.120
117	ILE	155	SER	0.117	0.000	0.117	0.117
110	LEU	155	SER	2.807	2.690	0.117	0.117
257	GLU	260	LYS	0.726	0.609	0.117	0.117
154	ALA	196	SER	4.288	4.172	0.116	0.116
487	LYS	491	GLN	0.000	0.116	-0.116	0.116
554	THR	558	LEU	0.457	0.344	0.113	0.113
146	ALA	201	ALA	0.342	0.455	-0.112	0.112
104	ASN	548	ASN	0.132	0.020	0.112	0.112
96	ASN	554	THR	3.038	2.927	0.111	0.111
526	TRP	530	TYR	0.110	0.000	0.110	0.110
475	ILE	479	LYS	0.306	0.196	0.110	0.110
232	THR	512	LEU	0.109	0.000	0.109	0.109
156	VAL	500	PHE	1.758	1.651	0.107	0.107
491	GLN	494	SER	0.000	0.107	-0.107	0.107
83	ILE	123	ASN	0.142	0.248	-0.107	0.107
142	ASP	205	LEU	1.882	1.987	-0.105	0.105
356	ASP	362	ARG	0.000	0.103	-0.103	0.103
462	THR	466	ARG	0.000	0.102	-0.102	0.102
482	SER	486	GLU	0.101	0.000	0.101	0.101
103	ASN	165	ASP	0.582	0.482	0.099	0.099
93	PHE	99	LEU	3.763	3.862	-0.099	0.099
144	TRP	221	CYS	1.854	1.756	0.098	0.098
68	VAL	130	ILE	1.170	1.268	-0.098	0.098
113	ALA	151	ALA	1.186	1.090	0.096	0.096
120	ILE	124	LEU	0.644	0.738	-0.094	0.094
71	ILE	75	THR	0.206	0.300	-0.094	0.094
359	SER	360	GLU	0.000	0.093	-0.093	0.093
93	PHE	551	PHE	0.092	0.000	0.092	0.092
259	GLU	263	LYS	3.904	3.997	-0.092	0.092
549	LYS	553	THR	0.000	0.091	-0.091	0.091
77	ILE	78	LEU	0.091	0.000	0.091	0.091
237	ILE	243	PRO	0.285	0.195	0.090	0.090
159	LEU	162	ILE	0.000	0.089	-0.089	0.089
254	ILE	490	ALA	0.000	0.088	-0.088	0.088
207	TRP	211	VAL	3.141	3.053	0.088	0.088
172	ARG	175	THR	1.122	1.209	-0.087	0.087
149	TYR	530	TYR	1.833	1.920	-0.087	0.087
170	ILE	254	ILE	1.164	1.248	-0.084	0.084
235	THR	240	PHE	0.003	0.087	-0.084	0.084
30	PRO	31	PRO	0.977	0.893	0.084	0.084
500	PHE	505	THR	0.014	0.095	-0.081	0.081
269	GLN	476	THR	0.080	0.000	0.080	0.080
310	ARG	312	HIS	0.079	0.000	0.079	0.079
501	ILE	506	PRO	0.314	0.235	0.079	0.079
108	LEU	112	CYS	0.000	0.079	-0.079	0.079
250	LEU	254	ILE	0.000	0.076	-0.076	0.076
106	PHE	189	ILE	3.001	3.077	-0.076	0.076
217	PRO	218	PRO	0.672	0.747	-0.075	0.075
505	THR	509	ILE	1.144	1.219	-0.075	0.075
478	ARG	481	MET	0.225	0.151	0.074	0.074
222	PHE	227	SER	0.000	0.074	-0.074	0.074
136	LEU	140	ALA	0.701	0.774	-0.073	0.073
216	VAL	221	CYS	0.479	0.407	0.072	0.072
141	CYS	142	ASP	0.803	0.731	0.072	0.072
249	ILE	253	ARG	1.351	1.280	0.071	0.071
510	MET	521	ILE	3.752	3.681	0.071	0.071
532	LEU	535	ILE	0.003	0.075	-0.071	0.071
500	PHE	501	ILE	0.000	0.071	-0.071	0.071
143	LEU	205	LEU	0.876	0.946	-0.070	0.070
472	ARG	476	THR	0.070	0.000	0.070	0.070
366	SER	367	ILE	0.000	0.068	-0.068	0.068
49	PHE	50	SER	0.067	0.000	0.067	0.067
154	ALA	158	ASN	0.150	0.217	-0.067	0.067
507	TYR	529	GLY	2.239	2.172	0.066	0.066
83	ILE	118	GLY	2.942	2.877	0.064	0.064
201	ALA	205	LEU	0.131	0.067	0.064	0.064
204	ILE	225	PHE	1.188	1.251	-0.064	0.064
93	PHE	100	LYS	4.522	4.458	0.063	0.063
80	LEU	84	ILE	1.663	1.600	0.063	0.063
556	LYS	561	CYS	0.075	0.013	0.061	0.061
535	ILE	539	VAL	0.412	0.474	-0.061	0.061
531	TRP	534	TYR	1.255	1.315	-0.061	0.061
144	TRP	145	LEU	0.916	0.855	0.060	0.060
364	ILE	367	ILE	0.059	0.000	0.059	0.059
59	PRO	60	LEU	0.358	0.300	0.058	0.058
254	ILE	258	THR	0.041	0.097	-0.055	0.055
114	ASP	536	ASN	0.000	0.054	-0.054	0.054
470	LYS	474	GLN	0.000	0.054	-0.054	0.054
363	ALA	367	ILE	0.000	0.052	-0.052	0.052
368	VAL	370	LYS	0.052	0.000	0.052	0.052
148	ASP	149	TYR	0.117	0.065	0.052	0.052
98	GLN	104	ASN	0.000	0.051	-0.051	0.051
168	PHE	171	THR	0.257	0.307	-0.050	0.050
145	LEU	204	ILE	2.064	2.015	0.050	0.050
75	THR	122	MET	0.049	0.000	0.049	0.049
202	PRO	207	TRP	0.208	0.257	-0.048	0.048
244	VAL	248	THR	0.359	0.310	0.048	0.048
251	TYR	252	TRP	0.000	0.047	-0.047	0.047
351	SER	355	GLU	0.000	0.047	-0.047	0.047
366	SER	368	VAL	0.047	0.000	0.047	0.047
189	ILE	193	TRP	0.659	0.705	-0.046	0.046
36	HIS	37	PHE	0.000	0.046	-0.046	0.046
181	THR	183	LYS	0.485	0.439	0.046	0.046
176	TYR	177	ARG	0.045	0.000	0.045	0.045
120	ILE	144	TRP	0.064	0.109	-0.045	0.045
570	LYS	574	GLN	0.000	0.044	-0.044	0.044
171	THR	172	ARG	0.736	0.693	0.043	0.043
483	LEU	486	GLU	0.043	0.000	0.043	0.043
233	PHE	241	TYR	0.000	0.042	-0.042	0.042
471	THR	475	ILE	0.568	0.527	0.041	0.041
369	LEU	371	LEU	0.040	0.000	0.040	0.040
58	ASP	59	PRO	0.632	0.593	0.039	0.039
154	ALA	192	ALA	0.038	0.000	0.038	0.038
509	ILE	513	VAL	0.131	0.169	-0.038	0.038
87	ILE	91	VAL	0.439	0.401	0.038	0.038
540	ASN	541	PRO	0.904	0.941	-0.037	0.037
503	THR	529	GLY	0.037	0.000	0.037	0.037
436	ASP	437	THR	2.145	2.109	0.036	0.036
229	PRO	230	THR	0.036	0.000	0.036	0.036
115	LEU	119	VAL	0.818	0.784	0.035	0.035
553	THR	554	THR	0.203	0.169	0.034	0.034
206	PHE	209	TYR	0.152	0.185	-0.033	0.033
82	THR	534	TYR	0.000	0.033	-0.033	0.033
273	THR	472	ARG	0.033	0.000	0.033	0.033
196	SER	201	ALA	0.000	0.032	-0.032	0.032
172	ARG	176	TYR	0.499	0.531	-0.032	0.032
477	LYS	481	MET	0.205	0.236	-0.032	0.032
88	LEU	558	LEU	0.831	0.799	0.032	0.032
201	ALA	206	PHE	0.041	0.011	0.029	0.029
43	SER	44	ARG	0.000	0.026	-0.026	0.026
505	THR	506	PRO	0.908	0.934	-0.026	0.026
541	PRO	544	TYR	0.000	0.025	-0.025	0.025
561	CYS	564	ASP	0.024	0.000	0.024	0.024
141	CYS	221	CYS	6.510	6.534	-0.024	0.024
200	TRP	204	ILE	0.588	0.565	0.023	0.023
145	LEU	221	CYS	1.293	1.271	0.022	0.022
172	ARG	173	PRO	0.088	0.110	-0.022	0.022
171	THR	261	ARG	0.132	0.111	0.021	0.021
125	PHE	128	TYR	0.264	0.285	-0.020	0.020
446	SER	447	VAL	1.082	1.102	-0.020	0.020
182	THR	183	LYS	0.020	0.000	0.020	0.020
244	VAL	500	PHE	0.897	0.878	0.020	0.020
229	PRO	516	PHE	0.018	0.000	0.018	0.018
174	LEU	340	ASN	0.000	0.018	-0.018	0.018
479	LYS	482	SER	0.000	0.017	-0.017	0.017
116	ILE	147	ILE	0.655	0.638	0.017	0.017
503	THR	504	TRP	1.785	1.768	0.017	0.017
64	THR	65	VAL	0.213	0.230	-0.016	0.016
105	TYR	108	LEU	0.000	0.014	-0.014	0.014
77	ILE	81	VAL	0.176	0.162	0.014	0.014
514	ASN	526	TRP	3.022	3.035	-0.013	0.013
92	SER	99	LEU	2.174	2.186	-0.012	0.012
506	PRO	532	LEU	0.814	0.826	-0.012	0.012
120	ILE	121	SER	0.000	0.011	-0.011	0.011
201	ALA	202	PRO	0.791	0.802	-0.011	0.011
297	GLN	300	MET	0.000	0.010	-0.010	0.010
268	LEU	271	SER	0.000	0.010	-0.010	0.010
99	LEU	548	ASN	0.214	0.206	0.009	0.009
237	ILE	241	TYR	0.119	0.127	-0.008	0.008
499	ALA	543	CYS	0.162	0.154	0.008	0.008
507	TYR	510	MET	0.050	0.043	0.007	0.007
166	ARG	543	CYS	0.007	0.000	0.007	0.007
116	ILE	120	ILE	0.206	0.212	-0.006	0.006
150	VAL	201	ALA	1.161	1.156	0.005	0.005
177	ARG	180	ARG	0.005	0.000	0.005	0.005
194	VAL	198	VAL	0.211	0.215	-0.004	0.004
247	MET	500	PHE	0.897	0.901	-0.004	0.004
141	CYS	220	GLU	0.004	0.000	0.004	0.004
92	SER	555	PHE	2.889	2.886	0.003	0.003
167	TYR	171	THR	2.547	2.549	-0.003	0.003
63	HIS	67	GLN	0.000	0.002	-0.002	0.002
255	TYR	258	THR	0.001	0.000	0.001	0.001
128	TYR	527	ASN	0.001	0.000	0.001	0.001

RRCS change distribution

0.07

Mean ΔRRCS

1.63

Std Dev

-0.00

Median

Magnitude classification

High (|Δ| ≥ 5.0)

Medium (2.3 ≤ |Δ| < 5.0)

740

Low (|Δ| < 2.3)

Methods

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

Significance threshold. |ΔRRCS| ≥ 2.28, 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