-->
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;
Ki = 96 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 1443 families.
1 4X3H Ki = 96 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 1205 families.
1 4X3H Ki = 96 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 1039 families.
1 4X3H Ki = 96 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
Ligand no: 1; Ligand: ARG ILE PRO SER TYR ARG TYR ARG TYR; Similar ligands found: 234
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 0.647059 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 ASN SER ARG TYR PRO THR SER ILE ILE 0.578231 0.918919
7 ALA PHE ARG ILE PRO LEU THR ARG 0.576389 0.890411
8 TYR PRO LYS ARG ILE ALA 0.57554 0.888889
9 PRO PRO ARG PRO ILE TYR ASN ARG ASN 0.568493 0.917808
10 GLU ARG THR ILE PRO ILE THR ARG GLU 0.568182 0.887324
11 ARG THR PHE SER PRO THR TYR GLY LEU 0.556291 0.932432
12 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.553191 0.813333
13 GLU VAL ALA PRO PRO GLU TYR HIS ARG LYS 0.547619 0.831169
14 ARG SEP PRO VAL PHE SER 0.541096 0.782051
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 ARG VAL SER PRO SER THR SER TYR THR PRO 0.530303 0.833333
20 ARG ARG ARG GLU ARG SER PRO THR ARG 0.528571 0.835616
21 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.527607 0.906667
22 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.524096 0.881579
23 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.522876 0.789474
24 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.519231 0.824324
25 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.516779 0.701149
26 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.516779 0.835616
27 TYR TYR SER ILE ILE PRO HIS SER ILE 0.513514 0.891892
28 LYS TYR TYR SER ILE ILE PRO HIS SER ILE 0.513514 0.891892
29 DPN PRO DAR ILE NH2 0.51145 0.802817
30 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.511111 0.706667
31 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.509317 0.85
32 ARG PRO MET THR TYR LYS GLY ALA LEU 0.509091 0.835443
33 ARG LEU TYR HIS SEP LEU PRO ALA 0.50625 0.85
34 CYS THR PRO SER ARG 0.503817 0.821918
35 ARG TYR PRO LEU THR PHE GLY TRP CYS PHE 0.497207 0.907895
36 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.49697 0.945946
37 THR PRO ARG ARG SER MLZ SER ALA 0.496296 0.84
38 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.49375 0.891892
39 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.493421 0.783784
40 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.490909 0.8125
41 TYR TYR SER ILE ALA PRO HIS SER ILE 0.490196 0.891892
42 ARG PRO LYS ARG ILE ALA 0.489209 0.805556
43 DPN PRO DAR DTH NH2 0.488722 0.84507
44 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.487342 0.878378
45 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.486486 0.837838
46 SER ARG ASP HIS SER ARG THR PRO MET 0.481481 0.822785
47 ILE GLY PRO GLY ARG ALA PHE TYR ALA 0.481013 0.890411
48 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.478788 0.918919
49 LEU PRO PHE ASP ARG THR THR ILE MET 0.478261 0.833333
50 ILE GLY PRO GLY ARG ALA PHE TYR VAL 0.478261 0.878378
51 ILE GLY PRO GLY ARG ALA PHE TYR THR 0.478261 0.90411
52 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.477707 0.835616
53 TYR PRO SER LYS PRO ASP ASN PRO GLY GLU 0.477612 0.830986
54 DPN PRO DAR CYS NH2 0.477273 0.75
55 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.476744 0.858974
56 ARG ILE PHE SER 0.476562 0.690141
57 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.47619 0.863014
58 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.475 0.864865
59 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.475 0.876712
60 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.472973 0.72973
61 LYS ARG ARG ARG HIS PRO SER 0.472603 0.808219
62 TYR PRO TYR ASP VAL PRO ASP TYR ALA 0.471831 0.797297
63 VAL PRO LEU ARG PRO MET THR TYR 0.471338 0.87013
64 LYS ARG ARG ARG HIS PRO SER GLY 0.469799 0.824324
65 ALA ARG THR GLU LEU TYR ARG SER LEU 0.468966 0.756757
66 ARG PRO PRO GLY PHE SER PRO PHE ALA 0.467949 0.888889
67 SER PRO LYS ARG ILE ALA 0.467153 0.833333
68 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.467066 0.931507
69 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.467066 0.931507
70 N7P THR SEP PRO SER TYR SET 0.465753 0.78481
71 ALA ASN SER ARG VAL PRO THR SER ILE ILE 0.465753 0.863014
72 PRO THR SEP PRO SER TYR 0.465753 0.792208
73 DMG PRO ARG ARG ARG SER ARG LYS PRO 0.465116 0.8
74 ASN ARG PRO VAL TYR ILE PRO PRO PRO PRO 0.464789 0.819444
75 HIS HIS ALA SER PRO ARG LYS 0.464516 0.835616
76 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.462963 0.810811
77 TRP GLU TYR ILE PRO ASN VAL 0.462963 0.792208
78 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.462963 0.824324
79 GLN ARG SER THR SEP THR PRO ASN VAL HIS 0.461039 0.7625
80 ARG THR TYR SEP GLY PRO MET ASN LYS VAL 0.460674 0.8
81 ALA ASN SER ARG ALA PRO THR SER ILE ILE 0.460526 0.84
82 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.460123 0.78481
83 LEU PRO PHE GLU ARG ALA THR ILE MET 0.458333 0.820513
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 ALA ASN SER ARG LEU PRO THR SER ILE ILE 0.455172 0.863014
89 SER PRO ILE VAL PRO SER PHE ASP MET 0.455128 0.769231
90 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.45509 0.866667
91 5JP PRO LYS ARG ILE ALA 0.454545 0.797297
92 GLU THR VAL ARG PHE GLN SER ASP 0.452703 0.675676
93 SER ASP TYR GLN ARG LEU 0.451852 0.689189
94 SER LEU SER ARG THR PRO ALA ASP GLY ARG 0.451613 0.849315
95 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.451613 0.810811
96 LEU PRO PRO LEU ASP ILE THR PRO TYR 0.451613 0.810811
97 VAL MET ALA PRO ARG THR LEU PHE LEU 0.450617 0.807692
98 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.450617 0.866667
99 GLN ALA SER TPO PRO ARG NIT 0.450617 0.755814
100 LEU PRO SER PHE GLU THR ALA LEU 0.450331 0.783784
101 ARG ARG ALA SEP ALA PRO LEU PRO 0.450331 0.772152
102 ARG PRO MET THR PHE LYS GLY ALA LEU 0.450292 0.797468
103 1IP CYS PHE SER LYS PRO ARG 0.449367 0.815789
104 ARG GLY PRO GLY ARG ALA PHE VAL THR ILE 0.449102 0.890411
105 ASP ILE ALA TYR TYR THR SER GLU PRO 0.44898 0.876712
106 ARG THR PRO SEP LEU PRO THR 0.44898 0.807692
107 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.448718 0.7625
108 ASN ARG PRO ILE LEU SER LEU 0.448276 0.826667
109 ALA ALA ARG KCR SER ALA PRO ALA 0.447368 0.810811
110 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.447205 0.76
111 ALA THR VAL ARG THR TYR SER CYS 0.446809 0.72973
112 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.446809 0.739726
113 VAL PRO TYR SER SER ALA GLN NAG 0.446667 0.78481
114 LEU PRO PHE GLU ARG ALA THR VAL MET 0.446429 0.807692
115 SER LEU ARG PHE LEU TYR GLU GLY 0.445205 0.77027
116 SER HIS PRO ARG PRO ILE ARG VAL 0.442308 0.866667
117 SER TYR SEP PRO THR SEP PRO SEP TYR SER 0.442177 0.779221
118 TYR PRO PHE PHE NH2 0.44186 0.760563
119 ASP ILE ASN TYR TYR THR SER GLU PRO 0.441558 0.864865
120 ALA VAL ALA PHE TYR ILE PRO ASP GLN ALA 0.440559 0.805556
121 ACE GLN PM3 GLU GLU ILE PRO 0.440559 0.692308
122 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.43871 0.77027
123 ALA ASN SER ARG HIS PRO THR SER ILE ILE 0.43871 0.891892
124 ALA ASN SER ARG ALY PRO THR SER ILE ILE 0.438272 0.842105
125 THR PRO TYR ASP ILE ASN GLN MET LEU 0.438272 0.759494
126 SER SER ARG LYS GLU TYR TYR ALA 0.437956 0.726027
127 PRO SER TYR SEP PRO THR SEP PRO SER 0.437086 0.782051
128 LYS PRO VAL LEU ARG THR ALA 0.436242 0.835616
129 GLN ASN TYR PRO ILE VAL GLN 0.436242 0.773333
130 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.435484 0.896104
131 PHE ARG TYR LEU GLY 0.434783 0.716216
132 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.434783 0.786667
133 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.434783 0.837838
134 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.434524 0.87013
135 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.434211 0.689189
136 GLU LEU ARG SER ARG TYR TRP ALA ILE 0.433735 0.828947
137 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.433735 0.84
138 ALA ILE ALA TYR PHE ILE PRO ASP GLN ALA 0.433566 0.816901
139 ALA ARG MLZ SER ALA PRO ALA THR 0.433333 0.828947
140 HIS SER ILE THR TYR LEU LEU PRO VAL 0.432927 0.866667
141 SER PRO ARG LEU PRO LEU LEU GLU SER 0.432624 0.777778
142 ILE SER PRO ARG THR LEU ASP ALA TRP 0.432584 0.894737
143 ALA ASN SER ARG TRP PRO ALY SER ILE ILE 0.432584 0.858974
144 LEU SER SER PRO VAL THR LYS SER PHE 0.432258 0.819444
145 TRP MET ASP PHE ASP ASP ASP ILE PRO PHE 0.431818 0.712329
146 TRP ASP ILE PRO PHE 0.431818 0.712329
147 PRO SER ILE ASP ARG SER THR LYS PRO 0.43125 0.890411
148 DPN PRO ARG 0.430769 0.736111
149 PHE PRO ARG 0.430769 0.732394
150 ARG VAL ALA SER PRO THR SER GLY VAL 0.42953 0.824324
151 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.429379 0.818182
152 VAL ALA PHE ARG SER 0.428571 0.652778
153 SER ARG ILE ARG ILE ARG GLY TYR VAL ARG 0.428571 0.783784
154 PHE ASN ARG PRO VAL 0.427586 0.773333
155 PHE ALA PRO GLY PHE PHE PRO TYR LEU 0.426752 0.810811
156 ACE TYR PRO ILE GLN GLU THR 0.426667 0.77027
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 ALA PRO ASP THR ARG PRO 0.422535 0.837838
167 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.421384 0.824324
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 GLU LEU LYS ARG LYS MET ILE TYR MET 0.420382 0.679487
171 SER ALA PRO ASP THR ARG PRO ALA 0.42 0.851351
172 SER PRO THR SER PRO SEP TYR SER PRO PRO 0.419355 0.792208
173 PRO ARG PRO ILE LEU LEU PRO TRP ARG NH2 0.418182 0.824324
174 ARG GLY TYR LEU TYR GLN GLY LEU 0.417808 0.716216
175 PRO GLN PTR GLU GLU ILE PRO ILE 0.417722 0.746835
176 ARG PHE PRO LEU THR PHE GLY TRP 0.417143 0.868421
177 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.416667 0.871795
178 GLU LEU ARG ARG LYS MET MET TYR MET 0.416107 0.679487
179 GLY GLY LYS LYS LYS TYR ARG LEU 0.415493 0.716216
180 GLY GLY ARG LYS LYS TYR LYS LEU 0.415493 0.716216
181 VAL LYS VAL VAL ALA LYS LYS TYR ARG ASN 0.415493 0.706667
182 GLY GLY LYS LYS ARG TYR LYS 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 DVA DPR GLY DSN DGN DHI DTY DAS DSN 0.414634 0.828947
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 SER GLU LEU GLU ILE LYS ARG TYR 0.414474 0.77027
189 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.414201 0.824324
190 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.41358 0.786667
191 PRO PRO LYS ARG ILE ALA 0.413333 0.805556
192 3BY PRO LYS ARG ILE ALA 0.413333 0.776316
193 ARG ARG ARG ARG SER TRP TYR 0.413043 0.753425
194 LEU PHE GLY TYR PRO VAL TYR VAL 0.412903 0.783784
195 TYR HIS SEP VAL VAL ARG TYR ALA 0.4125 0.7625
196 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.412121 0.824324
197 ARG GLN PHE GLY PRO ASP TRP ILE VAL ALA 0.411765 0.828947
198 ASN ASP TRP LEU LEU PRO SER TYR 0.411765 0.831169
199 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.411765 0.789474
200 GLY ALA ALA ARG ALA GLU VAL TYR LEU ARG 0.411392 0.693333
201 ALA PRO ASP THR ARG PRO ALA PRO 0.410959 0.837838
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 LEU ASP PRO ARG 0.408759 0.756757
207 ARG PRO LYS PRO LEU VAL ASP PRO 0.408451 0.791667
208 GLY LEU LEU GLY SER PRO VAL ARG ALA 0.407895 0.797297
209 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.407609 0.85
210 ILE THR ASP GLN VAL PRO PHE SER VAL 0.407407 0.797297
211 LEU PRO PRO GLU GLU ARG LEU ILE 0.406667 0.783784
212 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.40625 0.783784
213 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.40625 0.783784
214 ILE MET ASP GLN VAL PRO PHE SER VAL 0.406061 0.74359
215 GLU LEU ASN ARG LYS MET ILE TYR MET 0.406061 0.696203
216 ALA MET ALA PRO ARG THR LEU LEU LEU 0.405229 0.782051
217 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.404255 0.8625
218 PRO ARG ARG PRO VAL ILE MET ARG ARG 0.403846 0.763158
219 MET CYS PRO ARG MET THR ALA VAL MET 0.403727 0.805195
220 LEU PRO PHE ASP LYS SER THR ILE MET 0.403509 0.769231
221 ARG PHE PRO LEU THR PHE GLY TRP CYS PHE 0.403226 0.87013
222 ARG PRO PRO GLY PHE 0.402778 0.777778
223 SER SER ILE GLU PHE ALA ARG LEU 0.402597 0.702703
224 ALA PRO SER PTR VAL ASN VAL GLN ASN 0.402516 0.743902
225 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.402439 0.7625
226 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.402367 0.704545
227 LYS ARG LYS SER ARG TRP ASP GLU THR PRO 0.402367 0.855263
228 ASN TRP SER HIS PRO GLN PHE GLU LYS 0.401361 0.77027
229 LYS ALA PRO ARG ALY GLN LEU ALA THR LYS 0.401361 0.733333
230 ASP ARG VAL GLU LEU ASN ALA PRO ARG GLN 0.401274 0.763158
231 GLY GLN VAL PRO PHE SER LYS GLU GLU CYS 0.401235 0.75
232 MET SER LEU PRO GLY ARG TRP LYS PRO LYS 0.40107 0.825
233 ALA THR ARG ASN PHE SER GLY 0.4 0.712329
234 THR PRO ARG VAL THR GLY GLY GLY ALA MET 0.4 0.78481
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: 91
This union binding pocket(no: 1) in the query (biounit: 4x3h.bio1) has 22 residues
No: Leader PDB Ligand Sequence Similarity
1 3SJK LYS PRO VAL LEU ARG THR ALA None
2 1KSK URA None
3 5CHR 4NC None
4 4TV1 36M None
5 2HZL PYR None
6 2ATJ BHO None
7 5BVE 4VG None
8 3BIB PSF None
9 6FX2 FUC C4W NAG BMA MAN NAG GAL None
10 1SBR VIB None
11 5WGQ EST None
12 5XJ7 87O None
13 5VGS 9A7 None
14 4MGA 27L None
15 4EUU BX7 None
16 3BPX SAL 1.26582
17 1JQY A32 3.79747
18 5AVF TAU 3.79747
19 3CV6 HXS 3.79747
20 3CV6 NAP 3.79747
21 3H9R TAK 3.79747
22 4WNP 3RJ 5.06329
23 2BVE PH5 5.06329
24 1HFU NAG NDG 5.06329
25 4O4Z N2O 5.06329
26 4G17 0VN 5.06329
27 3M2W L8I 6.32911
28 1RYD GLC 7.59494
29 5JBE MAL 7.59494
30 1PVC ILE SER GLU VAL 7.59494
31 3B6R CRN 7.59494
32 6AYU MLI 7.59494
33 5IH9 6BF 7.59494
34 1NXJ GLV 7.59494
35 5GG9 8GM 7.59494
36 2ZV2 609 7.59494
37 4C2C ALA ALA ALA 8.86076
38 1WLJ U5P 8.86076
39 1LTT GAL BGC 8.86076
40 4C2W ANP 8.86076
41 1LT3 GAL BGC 8.86076
42 1JGS SAL 10.1266
43 3KP6 SAL 10.1266
44 2F57 23D 10.1266
45 3BP1 GUN 11.3924
46 1N62 FAD 11.3924
47 5EI3 5O8 11.3924
48 5MJA 7O3 11.3924
49 3SBZ MLI 11.3924
50 3HMO STU 11.3924
51 5OCA 9QZ 12.6582
52 4BCN T9N 12.6582
53 3UEC ALA ARG TPO LYS 12.6582
54 4BCM T7Z 12.6582
55 3AB4 THR 12.6582
56 2BP1 FLC 12.6582
57 5LMK 6ZK 12.6582
58 5XJD 87L 12.6582
59 1FFU FAD 12.6582
60 2UUU FAD 12.6582
61 2UUU PL3 12.6582
62 4Y8D 49J 12.6582
63 1R89 CTP 13.9241
64 1VR0 3SL 13.9241
65 2VN9 GVD 15.1899
66 4UCI ADN 15.1899
67 2WEL K88 15.1899
68 4AP9 1PS 15.1899
69 2XYA 7L4 16.4557
70 5LX9 OLB 16.4557
71 3HRD FAD 17.7215
72 2VO4 4NM 18.9873
73 4F4P 0SB 18.9873
74 5VKM GAL SIA 20.2532
75 4B1X LAB 20.2532
76 5YEE LAB 20.2532
77 5ZZB LAB 20.2532
78 1UNH IXM 21.519
79 4AU8 Z3R 21.519
80 3PTG 932 24.0506
81 4OKE AMP 24.0506
82 6AC9 ANP 24.0506
83 4E28 9MZ 25.3165
84 4E28 0MZ 25.3165
85 5AWM ANP 25.3165
86 6BJO DUY 27.8481
87 1JPA ANP 29.1139
88 3ZRM ZRM 31.6456
89 2JLD ALA GLY GLY ALA ALA ALA ALA ALA 31.6456
90 2JLD AG1 31.6456
91 3F7Z 34O 31.6456
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