Receptor
PDB id Resolution Class Description Source Keywords
1G37 2 Å EC: 3.4.21.5 CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN COMPLEXED WITH BCH EXOSITE-DIRECTED PEPTIDE HOMO SAPIENS PROTEASE THROMBIN INHIBITOR BLOOD CLOTTING HYDROLASE-HYDINHIBITOR COMPLEX
Ref.: POTENT AND SELECTIVE BICYCLIC LACTAM INHIBITORS OF PART 4: TRANSITION STATE INHIBITORS. BIOORG.MED.CHEM.LETT. V. 11 287 2001
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
110 A:900;
Invalid;
none;
submit data
574.689 C28 H38 N4 O7 S CCCCO...
PHE GLU ALA ILE PRO ALA GLU TYR LEU B:356;
Valid;
none;
submit data
1050.18 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
1D9I 2.3 Å EC: 3.4.21.5 STRUCTURE OF THROMBIN COMPLEXED WITH SELECTIVE NON-ELECTOPHI INHIBITORS HAVING CYCLOHEXYL MOIETIES AT P1 HOMO SAPIENS GLOBULAR HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Ref.: STRUCTURE OF THROMBIN COMPLEXED WITH SELECTIVE NON-ELECTROPHILIC INHIBITORS HAVING CYCLOHEXYL MOIE P1. ACTA CRYSTALLOGR.,SECT.D V. 56 294 2000
Members (9)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 26 families.
1 1D9I Ki = 0.78 nM 00P C22 H29 N5 O5 S c1ccc(cc1)....
2 1JWT Ki = 14 nM BLI C22 H32 N6 O5 S c1ccc(cc1)....
3 1XM1 - GAH C38 H61 N11 O6 [H]/N=C(N)....
4 1HAG - ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU n/a n/a
5 1ZGV ic50 ~ 1 uM 501 C17 H21 Cl N6 CCCCNc1cc(....
6 2BDY ic50 = 0.017 uM UNB C27 H26 N4 O4 S [H]/N=C(c1....
7 1G37 - PHE GLU ALA ILE PRO ALA GLU TYR LEU n/a n/a
8 1ZGI Ki = 4.6 uM 382 C22 H23 F2 N7 O c1ccc(c(c1....
9 1D6W Ki = 1100 nM 00R C24 H29 N7 O5 S c1ccc(cc1)....
70% Homology Family (9)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 18 families.
1 1D9I Ki = 0.78 nM 00P C22 H29 N5 O5 S c1ccc(cc1)....
2 1JWT Ki = 14 nM BLI C22 H32 N6 O5 S c1ccc(cc1)....
3 1XM1 - GAH C38 H61 N11 O6 [H]/N=C(N)....
4 1HAG - ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU n/a n/a
5 1ZGV ic50 ~ 1 uM 501 C17 H21 Cl N6 CCCCNc1cc(....
6 2BDY ic50 = 0.017 uM UNB C27 H26 N4 O4 S [H]/N=C(c1....
7 1G37 - PHE GLU ALA ILE PRO ALA GLU TYR LEU n/a n/a
8 1ZGI Ki = 4.6 uM 382 C22 H23 F2 N7 O c1ccc(c(c1....
9 1D6W Ki = 1100 nM 00R C24 H29 N7 O5 S c1ccc(cc1)....
50% Homology Family (9)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 16 families.
1 1D9I Ki = 0.78 nM 00P C22 H29 N5 O5 S c1ccc(cc1)....
2 1JWT Ki = 14 nM BLI C22 H32 N6 O5 S c1ccc(cc1)....
3 1XM1 - GAH C38 H61 N11 O6 [H]/N=C(N)....
4 1HAG - ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU n/a n/a
5 1ZGV ic50 ~ 1 uM 501 C17 H21 Cl N6 CCCCNc1cc(....
6 2BDY ic50 = 0.017 uM UNB C27 H26 N4 O4 S [H]/N=C(c1....
7 1G37 - PHE GLU ALA ILE PRO ALA GLU TYR LEU n/a n/a
8 1ZGI Ki = 4.6 uM 382 C22 H23 F2 N7 O c1ccc(c(c1....
9 1D6W Ki = 1100 nM 00R C24 H29 N7 O5 S c1ccc(cc1)....
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: PHE GLU ALA ILE PRO ALA GLU TYR LEU; Similar ligands found: 212
No: Ligand ECFP6 Tc MDL keys Tc
1 PHE GLU ALA ILE PRO ALA GLU TYR LEU 1 1
2 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.673611 0.9375
3 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.662162 0.968254
4 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.648649 0.884058
5 LEU PRO SER PHE GLU THR ALA LEU 0.605634 0.820895
6 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.582781 0.84507
7 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.576923 0.953125
8 PHE ALA PRO GLY ASN TYR PRO ALA LEU 0.576159 0.882353
9 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.566879 0.75
10 TRP GLU TYR ILE PRO ASN VAL 0.566879 0.910448
11 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.559748 0.923077
12 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.554878 0.824324
13 ILE PRO LEU THR GLU GLU ALA GLU LEU 0.539568 0.830769
14 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.535948 0.746835
15 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.534162 0.923077
16 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.532374 0.887097
17 LEU PRO PHE GLU ARG ALA THR ILE MET 0.53012 0.736842
18 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.527397 0.71875
19 TYR TYR SER ILE ILE PRO HIS SER ILE 0.522876 0.830986
20 LYS TYR TYR SER ILE ILE PRO HIS SER ILE 0.522876 0.830986
21 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.518987 0.880597
22 ALA PRO GLN PRO ALA PRO GLU ASN ALA TYR 0.516556 0.835821
23 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.514451 0.797297
24 TRP ASP ILE PRO PHE 0.51145 0.854839
25 TRP MET ASP PHE ASP ASP ASP ILE PRO PHE 0.51145 0.854839
26 PRO GLN PTR GLU PTR ILE PRO ALA 0.509677 0.830986
27 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.509677 0.907692
28 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.508982 0.769231
29 ASP ALA ASP GLU TYR LEU 0.507576 0.68254
30 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.503311 0.865672
31 THR PRO TYR ASP ILE ASN GLN MET LEU 0.503106 0.842857
32 PHE LEU PRO HIS ALY TYR ASP VAL LYS LEU 0.502924 0.852941
33 LEU PRO PHE GLU ARG ALA THR VAL MET 0.5 0.723684
34 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.49697 0.910448
35 PHE ALA PRO GLY ASN TYI PRO ALA LEU 0.496894 0.821918
36 ASP ILE ASN TYR TYR ALA SER GLU PRO 0.496774 0.882353
37 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.496774 0.833333
38 ALA ILE ALA TYR PHE ILE PRO ASP GLN ALA 0.496504 0.95082
39 ALA PHE ARG ILE PRO LEU THR ARG 0.493671 0.753425
40 PRO GLN PTR GLU GLU ILE PRO ILE 0.49359 0.802817
41 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.493421 0.783784
42 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.490566 0.72973
43 ASP ILE ALA TYR TYR THR SER GLU PRO 0.489933 0.895522
44 TYR PRO PHE PHE NH2 0.48855 0.885246
45 ARG THR PHE SER PRO THR TYR GLY LEU 0.487805 0.821918
46 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.487179 0.920635
47 ALA VAL ALA PHE TYR ILE PRO ASP GLN ALA 0.482759 0.967213
48 PHE LEU ALA TYR LYS 0.481752 0.774194
49 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.480519 0.690141
50 SER ALA GLU PRO VAL PRO LEU GLN LEU 0.47973 0.779412
51 ILE GLY PRO GLY ARG ALA PHE TYR VAL 0.479042 0.897059
52 ILE GLY PRO GLY ARG ALA PHE TYR THR 0.479042 0.869565
53 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.479042 0.819444
54 PHE PRO THR LYS ASP VAL ALA LEU 0.477987 0.820895
55 PHE ASN PHE PRO GLN ILE THR 0.476821 0.863636
56 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.476744 0.84507
57 PHE GLU ALA ASN GLY ASN LEU ILE 0.47619 0.651515
58 VAL PRO LEU THR GLU ASP ALA GLU LEU 0.47619 0.815385
59 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.473684 0.838235
60 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.473373 0.910448
61 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.473054 0.838235
62 ILE GLY PRO GLY ARG ALA PHE TYR ALA 0.472727 0.882353
63 ACE GLN PM3 GLU GLU ILE PRO 0.472603 0.768116
64 ACE LEU TYR ALA SER SER ASN PRO ALA PTR 0.47205 0.789474
65 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.471698 0.967742
66 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.471698 0.967742
67 ILE LEU ALA LYS PHE LEU HIS GLU LEU 0.470588 0.742424
68 LEU ALA ILE TYR SER 0.469697 0.671875
69 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.469136 0.968254
70 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.469136 0.828125
71 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.46875 0.771429
72 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.467532 0.676471
73 ACE TYR PRO ILE GLN GLU THR 0.467105 0.920635
74 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.467066 0.882353
75 PHE ALA PRO GLY PHE PHE PRO TYR LEU 0.465409 0.907692
76 SER GLU ASP GLU PHE TYR ASP ALA LEU SER 0.463576 0.712121
77 TYR TYR SER ILE ALA PRO HIS SER ILE 0.462963 0.805556
78 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.4625 0.865672
79 TYR LEU GLU PRO GLY PRO VAL THR ALA 0.4625 0.865672
80 LEU PHE GLY TYR PRO VAL TYR VAL 0.461538 0.967742
81 VAL MET ALA PRO ARG THR LEU PHE LEU 0.461078 0.701299
82 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.459119 0.710145
83 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.458333 0.716216
84 THR ASN GLU PHE TYR PHE 0.458015 0.640625
85 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.457831 0.75
86 PHE ALA PRO GLY ASN TYR PRO ALA TRP 0.457143 0.828571
87 PHE TYR ARG ALA LEU MET 0.456954 0.652778
88 SER PRO ILE VAL PRO SER PHE ASP MET 0.45679 0.777778
89 GLY GLN VAL PRO PHE SER LYS GLU GLU CYS 0.45679 0.757143
90 ACE ILE TYR GLU SER LEU 0.455882 0.666667
91 GLY ALA ASP ILE PHE TYR LEU ASP GLY ALA 0.455172 0.730159
92 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.453488 0.810811
93 PRO ALA ILE LEU TYR ALA LEU LEU SER SER 0.453333 0.776119
94 TYR PRO TYR ASP VAL PRO ASP TYR ALA 0.453333 0.921875
95 HIS SER ILE THR TYR LEU LEU PRO VAL 0.452381 0.830986
96 PHE LEU ARG GLY ARG ALA TYR GLY LEU 0.45098 0.710145
97 ASP GLU LEU GLU ILE LYS ALA TYR 0.450331 0.75
98 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.449102 0.838235
99 PTR VAL PRO MET LEU 0.446667 0.767123
100 GLU ILE ILE ASN PHE GLU LYS LEU 0.446667 0.651515
101 LEU PRO PHE GLU LYS SER THR VAL MET 0.446429 0.763889
102 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.446429 0.897059
103 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.445783 0.893939
104 THR PRO ASP TYR PHE LEU 0.442029 0.857143
105 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.44186 0.783784
106 ARG PRO MET THR TYR LYS GLY ALA LEU 0.441341 0.753247
107 DHI PRO PHE HIS LEU LEU VAL TYR 0.441176 0.907692
108 TYR LEU ALA PRO GLY PRO VAL THR ALA 0.43949 0.852941
109 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.439306 0.779412
110 GLN ASN TYR PRO ILE VAL GLN 0.43871 0.921875
111 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.438202 0.810811
112 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU 0.438202 0.759494
113 PHE ARG TYR LEU GLY 0.4375 0.720588
114 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.436782 0.893939
115 LYS PRO SEP GLN GLU LEU 0.43662 0.69863
116 ILE THR ASP GLN VAL PRO PHE SER VAL 0.436364 0.835821
117 PHE SER ALA PTR PRO SER GLU GLU ASP 0.435897 0.743243
118 SER ASP ILE LEU PHE PRO ALA ASP SER 0.435897 0.820895
119 ARG PRO MET THR PHE LYS GLY ALA LEU 0.435754 0.714286
120 GLN MET PRO THR GLU ASP GLU TYR 0.435583 0.814286
121 ILE MET ASP GLN VAL PRO PHE SER VAL 0.434524 0.774648
122 SER ILE ILE ASN PHE GLU LYS LEU 0.434211 0.647059
123 TYR PRO LYS ARG ILE ALA 0.433962 0.826087
124 GLU ASN LEU TYR PHE GLN 0.433566 0.71875
125 GLY ASN TYR SER PHE TYR ALA LEU 0.433566 0.676471
126 PRO PRO ALA TYR PRO PRO PRO PRO VAL PRO 0.433333 0.875
127 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.432927 0.760563
128 LEU PRO PHE ASP LYS THR THR ILE MET 0.431953 0.788732
129 ACE PRO ASP PTR GLU ASN LEU 0.431373 0.77027
130 PHE LEU SER TYR LYS 0.429577 0.727273
131 GLY ILE LEU GLU PHE VAL PHE THR LEU 0.42953 0.692308
132 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.429448 0.814286
133 ASP ASN ARG LEU GLY LEU VAL TYR GLN PHE 0.428571 0.737705
134 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.427673 0.661972
135 TYR ASP GLN ILE LEU 0.427536 0.709677
136 LEU PRO PRO LEU ASP ILE THR PRO TYR 0.426829 0.907692
137 ASP ILE ASN TYR TYR THR SER GLU PRO 0.425926 0.882353
138 THR ASN GLU PHE TYR ALA 0.425532 0.651515
139 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.425287 0.780822
140 TYR GLN PHE 0.425197 0.672131
141 ASP PHE GLU GLU ILE 0.424242 0.629032
142 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.423529 0.648649
143 PRO GLN PTR ILE PTR VAL PRO ALA 0.423313 0.84507
144 GLU VAL ALA PRO PRO GLU TYR HIS ARG LYS 0.42328 0.794521
145 TYR MET ASP PHE ASP ASP ASP ILE PRO PHE 0.423077 0.836066
146 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.422857 0.909091
147 LEU PRO PHE ASP LYS SER THR ILE MET 0.422857 0.777778
148 TYR SEP PRO THR SEP PRO SER 0.422819 0.72
149 ARG GLN PRO ALA LYS ALA PRO LEU LEU 0.42236 0.732394
150 THR ASN GLU TYR TYR VAL 0.421053 0.6875
151 ARG GLN ALA SEP ILE GLU LEU PRO SER MET 0.420765 0.630952
152 LYS THR PHE PRO PRO THR GLU PRO LYS 0.420732 0.80597
153 TYR GLY GLY PHE LEU 0.42029 0.774194
154 LEU ASP GLU GLU THR GLY GLU PHE LEU 0.42 0.666667
155 LEU PRO PHE ASP ARG THR THR ILE MET 0.41954 0.727273
156 GLU PHE SER PRO 0.419118 0.769231
157 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.418994 0.794521
158 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.41875 0.691176
159 LEU PRO PRO VAL VAL ALA LYS GLU ILE 0.41875 0.828125
160 SER GLN TYR TYR TYR ASN SER LEU 0.41844 0.676471
161 DTY ILE ARG LEU LPD 0.418301 0.838235
162 GLU GLY GLN PTR GLN PRO GLN PRO ALA 0.418182 0.760563
163 ASP PHE GLU ASP TYR GLU PHE ASP 0.417266 0.661538
164 VAL ASN ASP ILE PHE GLU ALA ILE 0.417219 0.615385
165 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.416667 0.823529
166 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.416149 0.826087
167 ILE LEU ALA LYS PHE LEU HIS THR LEU 0.416149 0.724638
168 LEU ASN PHE PRO ILE SER PRO 0.414474 0.811594
169 GLU ASN GLN LYS GLU TYR PHE PHE 0.413793 0.681818
170 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.413408 0.783784
171 GLU LEU ASP LYS TYR ALA SER 0.413333 0.712121
172 ALA THR ALA ALA ALA THR GLU ALA TYR 0.413043 0.630769
173 SER ILE ILE GLY PHE GLU LYS LEU 0.412903 0.681818
174 GLU ALA ASP PRO THR GLY HIS SER TYR 0.412429 0.802817
175 ALA VAL PRO ILE ALA GLN 0.411348 0.852459
176 GLN LEU SER PRO PHE PRO PHE ASP LEU 0.411043 0.850746
177 SER GLU CYS THR THR PRO CYS 0.410959 0.75
178 ALA ALA SER LEU TYR GLU LYS LYS ALA ALA 0.410596 0.701493
179 ASN PRO ARG ALA MET GLN ALA LEU LEU 0.409938 0.671053
180 ASN ARG PRO VAL TYR ILE PRO PRO PRO PRO 0.409091 0.890625
181 PRO GLU ALA THR ALA PRO PRO GLU GLU 0.409091 0.764706
182 ARG LEU PRO ALA LYS ALA PRO LEU LEU 0.408805 0.71831
183 LYS ALA LEU TYR ASN PHE ALA THR MET 0.408537 0.690141
184 DPN PRO DAR ILE NH2 0.408163 0.735294
185 PHE GLN TRP MET GLY TYR GLU LEU TRP 0.408046 0.768116
186 GLU GLN TYR LYS PHE TYR SER VAL 0.407895 0.716418
187 SER LEU TYR ASN THR ILE ALA THR LEU 0.407895 0.647059
188 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.407186 0.658228
189 THR TYR LYS PHE PHE GLU GLN 0.406897 0.69697
190 GLU ASN PRO THR TYR LYS PHE PHE GLU GLN 0.406897 0.69697
191 SER LEU PHE HIS 22G THR PRO 0.40678 0.830986
192 PHE LEU TRP GLY PRO ARG ALA LEU VAL 0.406593 0.788732
193 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.406417 0.753247
194 PRO PRO THR LEU HIS GLU LEU TYR ASP LEU 0.405714 0.842857
195 GLU ASP GLU ASP PHE GLU ILE LEU SER LEU 0.405063 0.641791
196 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.404908 0.852941
197 ACE PRO ALA PRO TYR 0.404412 0.815385
198 ARG TYR PRO LEU THR PHE GLY TRP 0.404255 0.810811
199 ASN ASP LYS TYR GLU PRO PHE TRP GLU 0.404255 0.811594
200 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.403509 0.746479
201 LYS GLN TRP ASP ASN TYR GLU PHE ILE TRP 0.403509 0.720588
202 ILE SER TYR GLY ASN ASP ALA LEU MET PRO 0.403409 0.819444
203 LEU PRO GLU THR GLY 0.402878 0.815385
204 ACE VAL PHE PHE ALA GLU ASP NH2 0.402878 0.629032
205 ALA LEU TYR ASN THR ALA ALA ALA LEU 0.402778 0.621212
206 ASP ARG VAL TYR ILE HIS PRO PHE 0.402685 0.876923
207 PHE ASN ARG PRO VAL 0.402597 0.732394
208 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.402174 0.797297
209 SER LEU ARG PHE LEU TYR GLU GLY 0.401274 0.680556
210 DVA DPR GLY DSN DGN DHI DTY DAS DSN 0.401163 0.816901
211 GLY SER ASP PRO PHE LYS 0.4 0.735294
212 GLU VAL PTR GLU SER PRO 0.4 0.780822
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 1D9I; Ligand: 00P; Similar sites found with APoc: 3
This union binding pocket(no: 1) in the query (biounit: 1d9i.bio1) has 26 residues
No: Leader PDB Ligand Sequence Similarity
1 1FIW PBZ 44.0972
2 1OSS BEN 47.0852
3 1PQ7 ARG 49.5536
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