Receptor
PDB id Resolution Class Description Source Keywords
4X3H 2.4 Å NON-ENZYME: OTHER CRYSTAL STRUCTURE OF ARC N-LOBE COMPLEXED WITH STARGAZIN PEP RATTUS NORVEGICUS ENDOCYTOSIS MEDIATOR SIGNALING PROTEIN
Ref.: STRUCTURAL BASIS OF ARC BINDING TO SYNAPTIC PROTEIN IMPLICATIONS FOR COGNITIVE DISEASE. NEURON V. 86 490 2015
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
ARG ILE PRO SER TYR ARG TYR ARG TYR B:225;
Valid;
Atoms found LESS than expected: % Diff = 0.011;
Kd = 59.4 uM
1261.5 n/a O=C(N...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
4X3H 2.4 Å NON-ENZYME: OTHER CRYSTAL STRUCTURE OF ARC N-LOBE COMPLEXED WITH STARGAZIN PEP RATTUS NORVEGICUS ENDOCYTOSIS MEDIATOR SIGNALING PROTEIN
Ref.: STRUCTURAL BASIS OF ARC BINDING TO SYNAPTIC PROTEIN IMPLICATIONS FOR COGNITIVE DISEASE. NEURON V. 86 490 2015
Members (2)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1610 families.
1 4X3H Kd = 59.4 uM ARG ILE PRO SER TYR ARG TYR ARG TYR n/a n/a
2 4X3I - ALA THR ARG ASN PHE SER GLY n/a n/a
70% Homology Family (2)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1331 families.
1 4X3H Kd = 59.4 uM ARG ILE PRO SER TYR ARG TYR ARG TYR n/a n/a
2 4X3I - ALA THR ARG ASN PHE SER GLY n/a n/a
50% Homology Family (2)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1144 families.
1 4X3H Kd = 59.4 uM ARG ILE PRO SER TYR ARG TYR ARG TYR n/a n/a
2 4X3I - ALA THR ARG ASN PHE SER GLY n/a n/a
Polypharmacology
Similar Ligands (2D)
Ligand no: 1; Ligand: ARG ILE PRO SER TYR ARG TYR ARG TYR; Similar ligands found: 238
No: Ligand ECFP6 Tc MDL keys Tc
1 ARG ILE PRO SER TYR ARG TYR ARG TYR 1 1
2 SER SER TYR ARG ARG PRO VAL GLY ILE 0.666667 0.945205
3 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.614286 0.902778
4 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.594406 0.890411
5 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.585526 0.945946
6 ALA PHE ARG ILE PRO LEU THR ARG 0.576389 0.890411
7 TYR PRO LYS ARG ILE ALA 0.57554 0.888889
8 PRO PRO ARG PRO ILE TYR ASN ARG ASN 0.568493 0.917808
9 GLU ARG THR ILE PRO ILE THR ARG GLU 0.568182 0.887324
10 ARG THR PHE SER PRO THR TYR GLY LEU 0.556291 0.932432
11 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.554054 0.918919
12 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.553191 0.813333
13 ARG SEP PRO VAL PHE SER 0.541096 0.782051
14 PHE TYR ARG TYR GLY PHE VAL ALA ASN PHE 0.540984 0.690141
15 DTY ILE ARG LEU LPD 0.540741 0.875
16 ALA ARG SER HIS SEP TYR PRO ALA 0.538462 0.860759
17 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.53125 0.864865
18 ALA GLN ASP ILE TYR ARG ALA SER TYR 0.530612 0.794521
19 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.524096 0.881579
20 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.522876 0.789474
21 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.519231 0.824324
22 ARG VAL SER PRO SER THR SER TYR THR PRO 0.518797 0.819444
23 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.516779 0.835616
24 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.516779 0.701149
25 TYR TYR SER ILE ILE PRO HIS SER ILE 0.513514 0.891892
26 DPN PRO DAR ILE NH2 0.51145 0.802817
27 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.511111 0.706667
28 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.509317 0.85
29 ARG PRO MET THR TYR LYS GLY ALA LEU 0.509091 0.835443
30 ARG LEU TYR HIS SEP LEU PRO ALA 0.50625 0.85
31 TYR PRO SER LYS PRO ASP ASN PRO GLY GLU 0.5 0.816901
32 ARG TYR PRO LEU THR PHE GLY TRP CYS PHE 0.497207 0.907895
33 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.49697 0.945946
34 THR PRO ARG ARG SER MLZ SER ALA 0.496296 0.84
35 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.493421 0.783784
36 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.490909 0.8125
37 TYR TYR SER ILE ALA PRO HIS SER ILE 0.490196 0.891892
38 ACE GLY PHE GLY VAL VAL PRO SER PHE TYR 0.489362 0.767123
39 ARG PRO LYS ARG ILE ALA 0.489209 0.805556
40 DPN PRO DAR DTH NH2 0.488722 0.84507
41 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.487342 0.878378
42 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.486486 0.837838
43 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.484277 0.891892
44 SER ARG ASP HIS SER ARG THR PRO MET 0.481481 0.822785
45 ILE GLY PRO GLY ARG ALA PHE TYR ALA 0.481013 0.890411
46 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.478788 0.918919
47 LEU PRO PHE ASP ARG THR THR ILE MET 0.478261 0.833333
48 ILE GLY PRO GLY ARG ALA PHE TYR THR 0.478261 0.90411
49 ILE GLY PRO GLY ARG ALA PHE TYR VAL 0.478261 0.878378
50 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.478261 0.853333
51 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.477707 0.835616
52 DPN PRO DAR CYS NH2 0.477273 0.75
53 LYS TYR TYR SER ILE ILE PRO HIS SER ILE 0.477124 0.891892
54 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.476744 0.858974
55 ARG ILE PHE SER 0.476562 0.690141
56 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.47619 0.863014
57 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.475 0.876712
58 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.475 0.864865
59 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.472973 0.72973
60 LYS ARG ARG ARG HIS PRO SER 0.472603 0.808219
61 TYR PRO TYR ASP VAL PRO ASP TYR ALA 0.471831 0.797297
62 VAL PRO LEU ARG PRO MET THR TYR 0.471338 0.87013
63 LYS ARG ARG ARG HIS PRO SER GLY 0.469799 0.824324
64 ALA ARG THR GLU LEU TYR ARG SER LEU 0.468966 0.756757
65 ARG PRO PRO GLY PHE SER PRO PHE ALA 0.467949 0.888889
66 SER PRO LYS ARG ILE ALA 0.467153 0.833333
67 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.467066 0.931507
68 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.467066 0.931507
69 ALA TYR ARG 0.466667 0.676056
70 N7P THR SEP PRO SER TYR SET 0.465753 0.78481
71 ASN ARG PRO VAL TYR ILE PRO PRO PRO PRO 0.464789 0.819444
72 HIS HIS ALA SER PRO ARG LYS 0.464516 0.835616
73 ASP ARG VAL TYR ILE HIS PRO PHE 0.463576 0.763158
74 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.462963 0.810811
75 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.462963 0.824324
76 TRP GLU TYR ILE PRO ASN VAL 0.462963 0.792208
77 ARG THR TYR SEP GLY PRO MET ASN LYS VAL 0.460674 0.8
78 ALA ASN SER ARG ALA PRO THR SER ILE ILE 0.460526 0.84
79 LYS VAL ALA PRO PRO ILE PRO HIS ARG 0.460123 0.786667
80 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.460123 0.78481
81 ARG SER HIS SEP SER PRO ALA SER LEU GLN 0.458824 0.790123
82 LEU PRO PHE GLU ARG ALA THR ILE MET 0.458333 0.820513
83 ARG SER ALA SEP GLU PRO SER LEU 0.458065 0.775
84 ASP ILE ASN TYR TYR ALA SER GLU PRO 0.457516 0.864865
85 ARG TYR PRO LEU THR PHE GLY TRP 0.457143 0.894737
86 PHQ LEU VAL ARG TYR 0.457143 0.72
87 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.456044 0.92
88 DMG PRO ARG ARG ARG SER ARG LYS PRO 0.455224 0.826667
89 SER PRO ILE VAL PRO SER PHE ASP MET 0.455128 0.769231
90 ACE GLU LEU LEU MET VAL PRO ASP MET TYR 0.453947 0.717949
91 5JP PRO LYS ARG ILE ALA 0.453901 0.810811
92 GLU THR VAL ARG PHE GLN SER ASP 0.452703 0.675676
93 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.451613 0.810811
94 LEU PRO PRO LEU ASP ILE THR PRO TYR 0.451613 0.810811
95 VAL MET ALA PRO ARG THR LEU PHE LEU 0.450617 0.807692
96 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.450617 0.866667
97 GLN ALA SER TPO PRO ARG NIT 0.450617 0.755814
98 ARG ARG ALA SEP ALA PRO LEU PRO 0.450331 0.772152
99 LEU PRO SER PHE GLU THR ALA LEU 0.450331 0.783784
100 ARG PRO MET THR PHE LYS GLY ALA LEU 0.450292 0.797468
101 1IP CYS PHE SER LYS PRO ARG 0.449367 0.815789
102 ARG GLY PRO GLY ARG ALA PHE VAL THR ILE 0.449102 0.890411
103 ARG THR PRO SEP LEU PRO THR 49F 0.44898 0.807692
104 ALA ASN SER ARG VAL PRO THR SER ILE ILE 0.44898 0.863014
105 ARG THR PRO SEP LEU PRO THR 0.44898 0.807692
106 ASN ARG PRO ILE LEU SER LEU 0.448276 0.826667
107 ACE ARG TYR ALA VAL VAL PRO ASP GLU 0.448276 0.847222
108 ALA ALA ARG KCR SER ALA PRO ALA 0.447368 0.810811
109 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.447205 0.76
110 VAL PRO TYR SER SER ALA GLN NAG 0.446667 0.78481
111 LEU PRO PHE GLU ARG ALA THR VAL MET 0.446429 0.807692
112 ARG ARG ARG GLU ARG SER PRO THR ARG 0.445946 0.835616
113 SER LEU ARG PHE LEU TYR GLU GLY 0.445205 0.77027
114 GLN ILE MET TYR ASN TYR PRO ALA MET 0.44375 0.782051
115 SER HIS PRO ARG PRO ILE ARG VAL 0.442308 0.866667
116 TYR PRO PHE PHE NH2 0.44186 0.760563
117 ASP ILE ASN TYR TYR THR SER GLU PRO 0.441558 0.864865
118 ASP ASP LEU ASP VAL PRO SER PHE LEU GLN 0.440789 0.783784
119 ALA VAL ALA PHE TYR ILE PRO ASP GLN ALA 0.440559 0.805556
120 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.43871 0.77027
121 ALA ASN SER ARG ALY PRO THR SER ILE ILE 0.438272 0.842105
122 THR PRO TYR ASP ILE ASN GLN MET LEU 0.438272 0.759494
123 GLY ASP CYS PHE SER LYS PRO ARG 0.4375 0.824324
124 PRO SER TYR SEP PRO THR SEP PRO SER 0.437086 0.782051
125 LYS PRO VAL LEU ARG THR ALA 0.436242 0.835616
126 GLN ASN TYR PRO ILE VAL GLN 0.436242 0.773333
127 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.435484 0.896104
128 PHE ARG TYR LEU GLY 0.434783 0.716216
129 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.434783 0.786667
130 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.434783 0.837838
131 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.434211 0.689189
132 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.433735 0.84
133 GLU LEU ARG SER ARG TYR TRP ALA ILE 0.433735 0.828947
134 ALA ILE ALA TYR PHE ILE PRO ASP GLN ALA 0.433566 0.816901
135 ALA ARG MLZ SER ALA PRO ALA THR 0.433333 0.828947
136 HIS SER ILE THR TYR LEU LEU PRO VAL 0.432927 0.866667
137 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.432624 0.739726
138 ILE SER PRO ARG THR LEU ASP ALA TRP 0.432584 0.894737
139 ALA ASN SER ARG TRP PRO ALY SER ILE ILE 0.432584 0.858974
140 LEU SER SER PRO VAL THR LYS SER PHE 0.432258 0.819444
141 PRO SER ILE ASP ARG SER THR LYS PRO 0.43125 0.890411
142 PHE PRO ARG 0.430769 0.732394
143 DPN PRO ARG 0.430769 0.736111
144 SER ASP TYR GLN ARG LEU 0.42963 0.689189
145 ARG VAL ALA SER PRO THR SER GLY VAL 0.42953 0.824324
146 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.429379 0.818182
147 VAL ALA PHE ARG SER 0.428571 0.652778
148 SER ARG ILE ARG ILE ARG GLY TYR VAL ARG 0.428571 0.783784
149 ARG LYS LYS ARG TYR THR VAL VAL GLY ASN 0.428571 0.756757
150 PHE ASN ARG PRO VAL 0.427586 0.773333
151 SER SER ARG LYS GLU TYR TYR ALA 0.427536 0.726027
152 ARG ARG GLU VAL HIS THR TYR TYR 0.426752 0.789474
153 PHE ALA PRO GLY PHE PHE PRO TYR LEU 0.426752 0.810811
154 ARG SER LEU SEP ALA PRO GLY ASN 0.426667 0.7625
155 ACE TYR PRO ILE GLN GLU THR 0.426667 0.77027
156 ASP ILE ALA TYR TYR THR SER GLU PRO 0.426667 0.876712
157 ARG GLN ALA SEP ILE GLU LEU PRO SER MET 0.426136 0.75
158 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.425926 0.824324
159 PHE LEU PRO HIS ALY TYR ASP VAL LYS LEU 0.425287 0.789474
160 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.42515 0.849315
161 ARG PRO ARG PRO ASP ASP LEU GLU ILE 0.424837 0.810811
162 PRO LYS ARG PRO THR THR LEU ASN LEU PHE 0.424419 0.878378
163 MET TRP ARG PRO TRP 0.424051 0.766234
164 PRO GLN PTR GLU PTR ILE PRO ALA 0.424051 0.772152
165 ARG GLY TYR VAL TYR GLN GLY LEU 0.422819 0.716216
166 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.421384 0.824324
167 LYS ARG LYS SER ARG TRP ASP GLU THR PRO 0.421348 0.88
168 ARG GLU ARG SER PRO THR ARG 0.421053 0.794521
169 ACE GLN GLU ARG GLU VAL PRO CYS 0.42069 0.723684
170 ACE GLN PM3 GLU GLU ILE PRO 0.42069 0.692308
171 GLU LEU LYS ARG LYS MET ILE TYR MET 0.420382 0.679487
172 SER ALA PRO ASP THR ARG PRO ALA 0.42 0.851351
173 LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL 0.418605 0.789474
174 VAL LYS VAL VAL ALA LYS LYS TYR ARG ASN 0.41844 0.706667
175 ARG GLY TYR LEU TYR GLN GLY LEU 0.417808 0.716216
176 PRO GLN PTR GLU GLU ILE PRO ILE 0.417722 0.746835
177 ARG PHE PRO LEU THR PHE GLY TRP 0.417143 0.868421
178 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.416667 0.871795
179 GLU LEU ARG ARG LYS MET MET TYR MET 0.416107 0.679487
180 GLY GLY LYS LYS ARG TYR LYS LEU 0.415493 0.716216
181 GLY GLY ARG LYS LYS TYR LYS LEU 0.415493 0.716216
182 GLY GLY LYS LYS LYS TYR ARG LEU 0.415493 0.716216
183 SER THR GLY GLY VAL M3L LYS PRO HIS ARG 0.415301 0.802469
184 ALA ILE ARG SER 0.414634 0.647887
185 SER GLU LEU GLU ILE LYS ARG TYR 0.414474 0.77027
186 ARG LEU PRO ALA LYS ALA PRO LEU LEU 0.414474 0.783784
187 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.414474 0.824324
188 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.414201 0.824324
189 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.41358 0.786667
190 3BY PRO LYS ARG ILE ALA 0.413333 0.776316
191 PRO PRO LYS ARG ILE ALA 0.413333 0.805556
192 LEU PHE GLY TYR PRO VAL TYR VAL 0.412903 0.783784
193 TYR HIS SEP VAL VAL ARG TYR ALA 0.4125 0.7625
194 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.412121 0.824324
195 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.411765 0.789474
196 ARG GLN PHE GLY PRO ASP TRP ILE VAL ALA 0.411765 0.828947
197 ASN ASP TRP LEU LEU PRO SER TYR 0.411765 0.831169
198 GLY ALA ALA ARG ALA GLU VAL TYR LEU ARG 0.411392 0.693333
199 ASP TYR ASN PRO TYR LEU LEU PHE LEU LYS 0.411392 0.826667
200 ALA THR PRO PHE GLN GLU 0.410959 0.726027
201 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.410714 0.87013
202 ARG GLN PRO ALA LYS ALA PRO LEU LEU 0.410256 0.773333
203 TYR SEP PRO THR SEP PRO SER 0.409722 0.782051
204 ASN ASP LYS TYR GLU PRO PHE TRP GLU 0.40884 0.776316
205 ARG VAL ALA SEP PRO THR SER GLY VAL 0.408805 0.7625
206 ACE ALA ALA ARG LBZ SER ALA PRO ALA 0.408805 0.849315
207 LEU ASP PRO ARG 0.408759 0.756757
208 ARG PRO LYS PRO LEU VAL ASP PRO 0.408451 0.791667
209 GLY LEU LEU GLY SER PRO VAL ARG ALA 0.407895 0.797297
210 ALA TRP ARG HIS PRO GLN PHE GLY GLY 0.407821 0.776316
211 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.407609 0.85
212 ILE THR ASP GLN VAL PRO PHE SER VAL 0.407407 0.797297
213 LEU PRO PRO GLU GLU ARG LEU ILE 0.406667 0.783784
214 TYR PRO TYR 0.406504 0.736111
215 LYS ILE LEU HIS ARG LEU LEU GLN ASP 0.40625 0.697368
216 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.40625 0.783784
217 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.40625 0.783784
218 GLU LEU ASN ARG LYS MET ILE TYR MET 0.406061 0.696203
219 ILE MET ASP GLN VAL PRO PHE SER VAL 0.406061 0.74359
220 PRO PRO LYS LYS LYS ARG LYS VAL 0.405594 0.763889
221 ALA MET ALA PRO ARG THR LEU LEU LEU 0.405229 0.782051
222 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.404255 0.8625
223 GLU TYR GLY PRO LYS TRP ASN LYS 0.40411 0.739726
224 PRO ARG ARG PRO VAL ILE MET ARG ARG 0.403846 0.763158
225 MET CYS PRO ARG MET THR ALA VAL MET 0.403727 0.805195
226 LEU PRO PHE ASP LYS SER THR ILE MET 0.403509 0.769231
227 ARG PHE PRO LEU THR PHE GLY TRP CYS PHE 0.403226 0.87013
228 TRP ASP ILE PRO PHE 0.402985 0.712329
229 ARG PRO PRO GLY PHE 0.402778 0.777778
230 ARG PRO PRO GLY PHE SER PRO PHE ARG 0.402778 0.777778
231 SER SER ILE GLU PHE ALA ARG LEU 0.402597 0.702703
232 ALA PRO SER PTR VAL ASN VAL GLN ASN 0.402516 0.743902
233 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.402439 0.7625
234 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.402367 0.704545
235 GLY GLN VAL PRO PHE SER LYS GLU GLU CYS 0.401235 0.75
236 MET SER LEU PRO GLY ARG TRP LYS PRO LYS 0.40107 0.825
237 THR PRO ARG VAL THR GLY GLY GLY ALA MET 0.4 0.78481
238 ALA THR ARG ASN PHE SER GLY 0.4 0.712329
Similar Ligands (3D)
Ligand no: 1; Ligand: ARG ILE PRO SER TYR ARG TYR ARG TYR; Similar ligands found: 0
No: Ligand Similarity coefficient
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 4X3H; Ligand: ARG ILE PRO SER TYR ARG TYR ARG TYR; Similar sites found with APoc: No similar binding sites found, or similarity not calculated due to duplicate pocket.
This union binding pocket(no: 1) in the query (biounit: 4x3h.bio1) has 22 residues
No: Leader PDB Ligand Sequence Similarity
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