JET2 Viewer

Pre-computed interfaces from JET2

PDB Structure: 1D9S chain A sc1

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Residue	Chain	Type	Evolutionary conservation TJET	Physico-chemical properties PC	Circular variance CV	#detections
6	A	SER	0.67	0.36	0.55	4
8	A	ALA	0.70	0.38	0.40	10
9	A	GLY	0.63	0.41	0.44	8
11	A	ALA	0.69	0.38	0.28	10
13	A	ALA	0.85	0.38	0.48	10
16	A	ARG	0.43	0.51	0.65	10
17	A	GLY	0.81	0.41	0.58	10
18	A	GLN	0.64	0.43	0.61	10
19	A	VAL	0.40	0.56	0.52	10
20	A	GLU	0.54	0.33	0.69	10
23	A	ARG	0.44	0.51	0.58	10
24	A	GLN	0.56	0.43	0.68	10
25	A	LEU	0.92	0.70	0.51	10
26	A	LEU	0.64	0.70	0.51	10
27	A	GLU	0.38	0.33	0.69	10
28	A	ALA	0.33	0.38	0.73	10
29	A	GLY	0.76	0.41	0.75	10
30	A	ALA	0.76	0.38	0.65	10
31	A	ASP	0.55	0.32	0.64	10
35	A	LEU	0.34	0.70	0.47	10
36	A	ASN	0.64	0.39	0.41	1
37	A	ARG	0.41	0.51	0.49	6
38	A	PHE	0.41	1.00	0.49	6
39	A	GLY	0.66	0.41	0.42	5
40	A	ARG	0.49	0.51	0.38	1
41	A	ARG	0.74	0.51	0.33	10
44	A	GLN	0.67	0.43	0.16	6
45	A	VAL	0.53	0.56	0.28	4
46	A	MET	0.77	0.66	0.18	10
47	A	MET	0.55	0.66	0.49	10
48	A	MET	0.42	0.66	0.23	5
49	A	GLY	0.56	0.41	0.48	1
50	A	SER	0.63	0.36	0.45	2
52	A	GLN	0.41	0.43	0.55	7
56	A	LEU	0.52	0.70	0.41	7
58	A	LEU	0.62	0.70	0.38	7
59	A	LEU	0.38	0.70	0.57	7
60	A	HIS	0.40	0.60	0.55	7
61	A	GLY	0.74	0.41	0.51	5
66	A	CYS	0.36	0.64	0.47	10
69	A	PRO	0.40	0.47	0.61	10
70	A	ALA	0.41	0.38	0.64	4
72	A	LEU	0.41	0.70	0.58	7
73	A	THR	0.72	0.33	0.40	3
77	A	HIS	0.71	0.60	0.22	5
83	A	GLY	0.82	0.41	0.46	7
84	A	PHE	0.54	1.00	0.41	10
85	A	LEU	0.35	0.70	0.48	7
89	A	VAL	0.48	0.56	0.50	5
90	A	VAL	0.55	0.56	0.38	1
92	A	HIS	0.65	0.60	0.53	5
93	A	ARG	0.44	0.51	0.63	5
94	A	ALA	0.45	0.38	0.55	5
95	A	GLY	0.72	0.41	0.59	5
96	A	ALA	0.75	0.38	0.45	2
97	A	ARG	0.43	0.51	0.55	4
98	A	LEU	0.52	0.70	0.39	5
101	A	CYS	0.30	0.64	0.53	7
104	A	TRP	0.42	0.99	0.71	5
105	A	GLY	0.78	0.41	0.56	5
106	A	ARG	0.54	0.51	0.66	5
107	A	LEU	0.79	0.70	0.50	6
109	A	VAL	0.81	0.56	0.43	2
111	A	LEU	0.47	0.70	0.45	6
115	A	GLN	0.48	0.43	0.67	6
116	A	GLY	0.78	0.41	0.68	6
117	A	HIS	0.57	0.60	0.55	7
118	A	ARG	0.42	0.51	0.71	4
119	A	ASP	0.49	0.32	0.65	4
122	A	ARG	0.46	0.51	0.69	4
123	A	TYR	0.51	0.80	0.53	5
125	A	HIS	0.60	0.60	0.59	3
126	A	ALA	0.38	0.38	0.65	5
127	A	ALA	0.22	0.38	0.56	5
128	A	THR	0.73	0.33	0.51	1
129	A	GLY	0.75	0.41	0.67	4
130	A	ASP	0.37	0.32	0.73	3
6	A	SER	0.67	0.36	0.42	5
9	A	GLY	0.63	0.41	0.31	10
13	A	ALA	0.85	0.38	0.44	10
16	A	ARG	0.43	0.51	0.60	10
17	A	GLY	0.81	0.41	0.56	10
18	A	GLN	0.64	0.43	0.61	10
19	A	VAL	0.40	0.56	0.53	10
20	A	GLU	0.54	0.33	0.70	10
21	A	THR	0.52	0.33	0.58	10
23	A	ARG	0.44	0.51	0.57	10
24	A	GLN	0.56	0.43	0.66	10
25	A	LEU	0.92	0.70	0.43	10
26	A	LEU	0.64	0.70	0.45	10
27	A	GLU	0.38	0.33	0.67	10
28	A	ALA	0.33	0.38	0.63	10
29	A	GLY	0.76	0.41	0.60	10
30	A	ALA	0.76	0.38	0.47	10
32	A	PRO	0.54	0.47	0.55	10
35	A	LEU	0.34	0.70	0.47	1
37	A	ARG	0.41	0.51	0.51	10
38	A	PHE	0.41	1.00	0.55	1
41	A	ARG	0.74	0.51	0.32	1
45	A	VAL	0.53	0.56	0.29	1
47	A	MET	0.55	0.66	0.48	10
49	A	GLY	0.56	0.41	0.45	2
50	A	SER	0.63	0.36	0.42	2
52	A	GLN	0.41	0.43	0.52	2
58	A	LEU	0.62	0.70	0.36	9
59	A	LEU	0.38	0.70	0.57	9
60	A	HIS	0.40	0.60	0.57	9
61	A	GLY	0.74	0.41	0.52	9
62	A	ALA	0.73	0.38	0.33	6
69	A	PRO	0.40	0.47	0.63	1
83	A	GLY	0.82	0.41	0.45	2
84	A	PHE	0.54	1.00	0.43	2
85	A	LEU	0.35	0.70	0.48	3
89	A	VAL	0.48	0.56	0.49	4
92	A	HIS	0.65	0.60	0.52	4
93	A	ARG	0.44	0.51	0.58	4
94	A	ALA	0.45	0.38	0.52	4
95	A	GLY	0.72	0.41	0.57	4
97	A	ARG	0.43	0.51	0.57	2
106	A	ARG	0.54	0.51	0.64	2
107	A	LEU	0.79	0.70	0.52	2
111	A	LEU	0.47	0.70	0.46	2
114	A	GLU	0.40	0.33	0.66	2
115	A	GLN	0.48	0.43	0.66	2
116	A	GLY	0.78	0.41	0.68	2
117	A	HIS	0.57	0.60	0.53	2
118	A	ARG	0.42	0.51	0.72	3
119	A	ASP	0.49	0.32	0.59	3
122	A	ARG	0.46	0.51	0.67	3
123	A	TYR	0.51	0.80	0.52	4
125	A	HIS	0.60	0.60	0.62	2
126	A	ALA	0.38	0.38	0.64	4
129	A	GLY	0.75	0.41	0.69	1
130	A	ASP	0.37	0.32	0.76	1
6	A	SER	0.67	0.36	0.51	8
8	A	ALA	0.70	0.38	0.45	9
9	A	GLY	0.63	0.41	0.47	9
11	A	ALA	0.69	0.38	0.28	9
13	A	ALA	0.85	0.38	0.45	9
16	A	ARG	0.43	0.51	0.65	9
17	A	GLY	0.81	0.41	0.55	9
18	A	GLN	0.64	0.43	0.61	9
19	A	VAL	0.40	0.56	0.53	9
20	A	GLU	0.54	0.33	0.69	9
23	A	ARG	0.44	0.51	0.56	9
24	A	GLN	0.56	0.43	0.68	9
25	A	LEU	0.92	0.70	0.53	9
27	A	GLU	0.38	0.33	0.69	9
28	A	ALA	0.33	0.38	0.68	9
29	A	GLY	0.76	0.41	0.58	9
35	A	LEU	0.34	0.70	0.41	9
37	A	ARG	0.41	0.51	0.60	1
38	A	PHE	0.41	1.00	0.54	1
39	A	GLY	0.66	0.41	0.48	1
41	A	ARG	0.74	0.51	0.31	3
47	A	MET	0.55	0.66	0.48	9
49	A	GLY	0.56	0.41	0.47	1
50	A	SER	0.63	0.36	0.46	1
52	A	GLN	0.41	0.43	0.53	1
69	A	PRO	0.40	0.47	0.60	3
84	A	PHE	0.54	1.00	0.41	1
4	A	GLY	0.34	0.41	0.55	10
6	A	SER	0.67	0.36	0.49	10
8	A	ALA	0.70	0.38	0.41	10
9	A	GLY	0.63	0.41	0.42	10
13	A	ALA	0.85	0.38	0.47	10
16	A	ARG	0.43	0.51	0.65	10
17	A	GLY	0.81	0.41	0.55	10
18	A	GLN	0.64	0.43	0.62	10
19	A	VAL	0.40	0.56	0.51	10
20	A	GLU	0.54	0.33	0.69	10
23	A	ARG	0.44	0.51	0.57	10
24	A	GLN	0.56	0.43	0.64	10
25	A	LEU	0.92	0.70	0.47	10
27	A	GLU	0.38	0.33	0.62	10
28	A	ALA	0.33	0.38	0.58	10
29	A	GLY	0.76	0.41	0.49	10
30	A	ALA	0.76	0.38	0.39	10
35	A	LEU	0.34	0.70	0.49	10
36	A	ASN	0.64	0.39	0.47	2
37	A	ARG	0.41	0.51	0.67	5
38	A	PHE	0.41	1.00	0.58	5
39	A	GLY	0.66	0.41	0.51	1
41	A	ARG	0.74	0.51	0.40	4
44	A	GLN	0.67	0.43	0.18	2
45	A	VAL	0.53	0.56	0.33	4
46	A	MET	0.77	0.66	0.19	10
47	A	MET	0.55	0.66	0.49	10
50	A	SER	0.63	0.36	0.46	4
52	A	GLN	0.41	0.43	0.54	8
58	A	LEU	0.62	0.70	0.34	3
60	A	HIS	0.40	0.60	0.50	10
69	A	PRO	0.40	0.47	0.61	4
81	A	ARG	0.40	0.51	0.46	5
83	A	GLY	0.82	0.41	0.47	5
84	A	PHE	0.54	1.00	0.41	10
85	A	LEU	0.35	0.70	0.47	6
89	A	VAL	0.48	0.56	0.50	4
92	A	HIS	0.65	0.60	0.51	4
93	A	ARG	0.44	0.51	0.64	4
94	A	ALA	0.45	0.38	0.53	3
95	A	GLY	0.72	0.41	0.58	3
96	A	ALA	0.75	0.38	0.44	1
97	A	ARG	0.43	0.51	0.52	1
106	A	ARG	0.54	0.51	0.64	1
107	A	LEU	0.79	0.70	0.51	1
111	A	LEU	0.47	0.70	0.46	2
113	A	GLU	0.51	0.33	0.62	2
114	A	GLU	0.40	0.33	0.66	2
115	A	GLN	0.48	0.43	0.63	2
116	A	GLY	0.78	0.41	0.69	2
117	A	HIS	0.57	0.60	0.56	5
118	A	ARG	0.42	0.51	0.72	4
119	A	ASP	0.49	0.32	0.60	4
122	A	ARG	0.46	0.51	0.68	4
123	A	TYR	0.51	0.80	0.51	4
125	A	HIS	0.60	0.60	0.64	4
126	A	ALA	0.38	0.38	0.64	4
129	A	GLY	0.75	0.41	0.68	4
6	A	SER	0.67	0.36	0.46	10
8	A	ALA	0.70	0.38	0.41	8
9	A	GLY	0.63	0.41	0.44	8
13	A	ALA	0.85	0.38	0.48	10
16	A	ARG	0.43	0.51	0.68	10
17	A	GLY	0.81	0.41	0.55	10
18	A	GLN	0.64	0.43	0.61	10
19	A	VAL	0.40	0.56	0.54	10
20	A	GLU	0.54	0.33	0.69	10
21	A	THR	0.52	0.33	0.60	1
23	A	ARG	0.44	0.51	0.57	10
24	A	GLN	0.56	0.43	0.69	10
25	A	LEU	0.92	0.70	0.53	10
26	A	LEU	0.64	0.70	0.46	10
27	A	GLU	0.38	0.33	0.69	10
28	A	ALA	0.33	0.38	0.71	10
29	A	GLY	0.76	0.41	0.62	10
30	A	ALA	0.76	0.38	0.49	10
35	A	LEU	0.34	0.70	0.47	6
37	A	ARG	0.41	0.51	0.56	8
38	A	PHE	0.41	1.00	0.54	8
39	A	GLY	0.66	0.41	0.50	1
41	A	ARG	0.74	0.51	0.32	1
45	A	VAL	0.53	0.56	0.33	2
47	A	MET	0.55	0.66	0.48	10
49	A	GLY	0.56	0.41	0.46	2
50	A	SER	0.63	0.36	0.44	3
52	A	GLN	0.41	0.43	0.52	3
58	A	LEU	0.62	0.70	0.38	6
59	A	LEU	0.38	0.70	0.56	9
60	A	HIS	0.40	0.60	0.54	9
61	A	GLY	0.74	0.41	0.51	6
62	A	ALA	0.73	0.38	0.31	4
66	A	CYS	0.36	0.64	0.47	1
69	A	PRO	0.40	0.47	0.62	2
81	A	ARG	0.40	0.51	0.48	1
83	A	GLY	0.82	0.41	0.43	1
84	A	PHE	0.54	1.00	0.40	3
85	A	LEU	0.35	0.70	0.47	1
86	A	ASP	0.45	0.32	0.47	1
89	A	VAL	0.48	0.56	0.49	1
92	A	HIS	0.65	0.60	0.51	1
93	A	ARG	0.44	0.51	0.59	4
95	A	GLY	0.72	0.41	0.57	4
97	A	ARG	0.43	0.51	0.57	1
117	A	HIS	0.57	0.60	0.55	1
2	A	LEU	0.37	0.70	0.49	5
6	A	SER	0.67	0.36	0.46	5
8	A	ALA	0.70	0.38	0.48	5
9	A	GLY	0.63	0.41	0.43	5
20	A	GLU	0.54	0.33	0.68	5
21	A	THR	0.52	0.33	0.60	5
23	A	ARG	0.44	0.51	0.58	5
24	A	GLN	0.56	0.43	0.58	5
25	A	LEU	0.92	0.70	0.43	5
27	A	GLU	0.38	0.33	0.63	5
28	A	ALA	0.33	0.38	0.55	5
29	A	GLY	0.76	0.41	0.52	5
30	A	ALA	0.76	0.38	0.41	5
35	A	LEU	0.34	0.70	0.49	2
36	A	ASN	0.64	0.39	0.44	2
37	A	ARG	0.41	0.51	0.70	2
38	A	PHE	0.41	1.00	0.58	2
39	A	GLY	0.66	0.41	0.52	2
60	A	HIS	0.40	0.60	0.49	5
6	A	SER	0.67	0.36	0.44	1
8	A	ALA	0.70	0.38	0.37	1
9	A	GLY	0.63	0.41	0.39	1
20	A	GLU	0.54	0.33	0.69	1
23	A	ARG	0.44	0.51	0.58	1
24	A	GLN	0.56	0.43	0.70	1
25	A	LEU	0.92	0.70	0.47	1
26	A	LEU	0.64	0.70	0.44	1
27	A	GLU	0.38	0.33	0.67	1
28	A	ALA	0.33	0.38	0.65	1
29	A	GLY	0.76	0.41	0.57	1
30	A	ALA	0.76	0.38	0.46	1
35	A	LEU	0.34	0.70	0.47	1
37	A	ARG	0.41	0.51	0.60	1
60	A	HIS	0.40	0.60	0.55	1

Pre-computed interfaces

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JET2 Viewer

Pre-computed interfaces from JET2

PDB Structure: 1D9S chain A sc1

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