Pre-computed interfaces

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Pre-computed interfaces from JET2

PDB Structure: 1GNL chain A auto

 

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 Residue 
 Chain 
 Type 
 Evolutionary conservation
TJET 
 Physico-chemical properties
PC 
 Circular variance
CV 
 #detections 
5
A
PHE
0.80
1.00
0.63
3
6
A
CYS
0.92
0.64
0.52
3
20
A
GLN
0.30
0.43
0.74
1
21
A
VAL
0.38
0.56
0.67
4
22
A
GLY
0.88
0.41
0.60
1
24
A
CYS
0.96
0.64
0.49
4
25
A
GLY
0.94
0.41
0.58
3
26
A
LYS
0.96
0.25
0.53
4
75
A
THR
0.94
0.33
0.25
4
79
A
PHE
0.92
1.00
0.50
4
214
A
THR
0.81
0.33
0.57
1
218
A
GLY
0.96
0.41
0.62
6
222
A
ILE
0.87
0.64
0.68
6
231
A
SER
0.58
0.36
0.83
6
232
A
ASN
0.88
0.39
0.81
6
233
A
PRO
0.84
0.47
0.79
6
251
A
GLN
0.89
0.43
0.73
5
253
A
GLU
0.54
0.33
0.80
6
254
A
GLY
0.73
0.41
0.83
6
255
A
THR
0.63
0.33
0.81
6
256
A
GLY
0.88
0.41
0.82
6
272
A
PRO
0.98
0.47
0.68
6
273
A
ALA
0.58
0.38
0.68
1
275
A
LYS
0.75
0.25
0.70
6
276
A
LYS
0.82
0.25
0.77
6
277
A
TYR
0.74
0.80
0.72
6
278
A
ALA
0.47
0.38
0.78
5
279
A
HIS
0.83
0.60
0.74
3
280
A
PHE
0.86
1.00
0.63
4
289
A
TRP
0.80
0.99
0.49
2
296
A
GLU
0.70
0.33
0.72
5
299
A
ASN
0.85
0.39
0.75
6
308
A
CYS
0.99
0.64
0.25
4
318
A
ASP
0.77
0.32
0.75
1
319
A
ARG
0.85
0.51
0.69
1
328
A
PHE
0.70
1.00
0.59
4
341
A
HIS
0.09
0.60
0.72
3
343
A
ASP
0.85
0.32
0.73
3
345
A
SER
0.56
0.36
0.77
2
346
A
ALA
0.65
0.38
0.76
1
348
A
ILE
0.93
0.64
0.75
6
350
A
HIS
0.54
0.60
0.77
3
352
A
LYS
0.74
0.25
0.83
6
353
A
THR
0.45
0.33
0.83
4
354
A
CYS
0.68
0.64
0.80
6
355
A
PRO
0.60
0.47
0.81
6
356
A
ALA
0.79
0.38
0.79
6
357
A
PRO
0.76
0.47
0.75
5
359
A
GLU
0.60
0.33
0.77
1
360
A
ILE
0.59
0.64
0.71
1
377
A
LEU
0.72
0.70
0.74
2
386
A
LYS
0.76
0.25
0.85
6
387
A
SER
0.34
0.36
0.86
6
388
A
GLY
0.86
0.41
0.84
6
389
A
ALA
0.69
0.38
0.82
5
398
A
GLY
0.99
0.41
0.21
4
399
A
CYS
0.99
0.64
0.19
4
402
A
ARG
0.81
0.51
0.52
1
417
A
PRO
0.96
0.47
0.78
6
419
A
ASP
0.85
0.32
0.80
6
427
A
CYS
0.99
0.64
0.24
4
430
A
TYR
0.76
0.80
0.42
1
431
A
ARG
0.85
0.51
0.53
2
435
A
LEU
0.70
0.70
0.68
7
436
A
ASN
0.59
0.39
0.75
3
437
A
LEU
0.78
0.70
0.71
6
438
A
GLY
0.98
0.41
0.75
6
439
A
ASP
0.51
0.32
0.79
6
440
A
ILE
0.78
0.64
0.78
6
441
A
GLY
0.54
0.41
0.82
6
442
A
GLY
0.92
0.41
0.79
6
443
A
ILE
0.72
0.64
0.74
1
444
A
PRO
0.98
0.47
0.69
6
454
A
ASP
0.94
0.32
0.30
1
455
A
SER
0.79
0.36
0.29
1
467
A
GLU
0.54
0.33
0.77
6
468
A
VAL
0.71
0.56
0.80
6
469
A
PHE
0.77
1.00
0.80
6
470
A
GLY
0.48
0.41
0.82
6
471
A
LEU
0.64
0.70
0.79
6
472
A
GLU
0.12
0.33
0.81
6
475
A
ASN
0.95
0.39
0.70
4
477
A
LEU
0.96
0.70
0.71
3
490
A
ALA
0.96
0.38
0.14
4
493
A
VAL
0.80
0.56
0.23
4
494
A
LEU
0.93
0.70
0.35
4
497
A
LEU
0.93
0.70
0.43
3
500
A
LEU
0.94
0.70
0.56
3
501
A
GLY
0.93
0.41
0.62
3
532
A
ILE
0.71
0.64
0.63
6
536
A
GLN
0.55
0.43
0.79
6
537
A
ASP
0.32
0.32
0.79
6
539
A
LEU
0.59
0.70
0.75
6
540
A
LYS
0.35
0.25
0.82
6
541
A
ALA
0.31
0.38
0.78
6
542
A
PHE
0.54
1.00
0.70
6
543
A
PHE
0.71
1.00
0.75
6