Pre-computed interfaces

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Pre-computed interfaces from JET2

PDB Structure: 1A6C chain A auto

 

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 Residue 
 Chain 
 Type 
 Evolutionary conservation
TJET 
 Physico-chemical properties
PC 
 Circular variance
CV 
 #detections 
16
A
PHE
0.47
1.00
0.62
7
19
A
PRO
0.79
0.47
0.70
6
20
A
LYS
0.81
0.25
0.77
7
21
A
ASP
0.90
0.32
0.75
7
23
A
LYS
0.71
0.25
0.65
1
28
A
LEU
0.98
0.70
0.56
2
65
A
PRO
0.81
0.47
0.74
5
67
A
ASN
0.78
0.39
0.76
3
68
A
ALA
0.71
0.38
0.76
1
69
A
PHE
0.95
1.00
0.80
8
81
A
TYR
0.71
0.80
0.24
2
83
A
ARG
0.89
0.51
0.29
2
84
A
ILE
0.84
0.64
0.43
2
86
A
LEU
0.49
0.70
0.56
2
89
A
LEU
0.64
0.70
0.58
2
101
A
LEU
0.42
0.70
0.20
1
102
A
PRO
0.90
0.47
0.31
1
116
A
TRP
0.73
0.99
0.37
1
118
A
PHE
0.37
1.00
0.40
1
123
A
LEU
0.76
0.70
0.26
1
148
A
ASN
0.88
0.39
0.65
1
150
A
VAL
0.71
0.56
0.75
7
151
A
THR
0.59
0.33
0.78
6
152
A
MET
0.70
0.66
0.77
7
153
A
ALA
0.77
0.38
0.83
7
154
A
ALA
0.64
0.38
0.81
6
155
A
ASP
0.83
0.32
0.78
7
156
A
TRP
0.90
0.99
0.71
7
170
A
ILE
0.26
0.64
0.65
1
171
A
ASP
0.20
0.32
0.71
1
172
A
ARG
0.36
0.51
0.63
1
173
A
PHE
0.84
1.00
0.54
2
175
A
LEU
0.71
0.70
0.53
1
177
A
PRO
0.97
0.47
0.47
1
185
A
LEU
0.24
0.70
0.49
1
189
A
PHE
0.47
1.00
0.35
2
194
A
TYR
0.71
0.80
0.27
1
195
A
TYR
0.58
0.80
0.30
1
201
A
LYS
0.66
0.25
0.76
5
202
A
LEU
0.85
0.70
0.81
8
203
A
ASP
0.63
0.32
0.81
6
204
A
GLY
0.56
0.41
0.78
6
254
A
LEU
0.45
0.70
0.78
8
255
A
PHE
0.72
1.00
0.82
8
271
A
PRO
0.59
0.47
0.81
2
273
A
LEU
0.61
0.70
0.82
7
274
A
ARG
0.39
0.51
0.86
7
275
A
GLN
0.24
0.43
0.81
6
277
A
LEU
0.58
0.70
0.82
7
278
A
TRP
0.67
0.99
0.85
7
279
A
GLY
0.65
0.41
0.79
6
280
A
PRO
0.90
0.47
0.75
4
281
A
HIS
0.69
0.60
0.76
7
283
A
ILE
0.71
0.64
0.76
7
314
A
LEU
0.41
0.70
0.72
6
316
A
LEU
0.67
0.70
0.79
7
318
A
GLY
0.90
0.41
0.80
7
319
A
PRO
0.92
0.47
0.78
7
320
A
ILE
0.39
0.64
0.83
8
321
A
ALA
0.84
0.38
0.83
7
322
A
PRO
0.95
0.47
0.86
7
323
A
ASP
0.54
0.32
0.88
7
324
A
ALA
0.71
0.38
0.86
7
325
A
HIS
0.70
0.60
0.80
6
326
A
VAL
0.59
0.56
0.79
6
338
A
TRP
0.69
0.99
0.46
1
357
A
TRP
1.00
0.99
0.44
1
379
A
TYR
0.59
0.80
0.44
2
380
A
ILE
0.71
0.64
0.34
2
381
A
HIS
0.67
0.60
0.39
2
382
A
ASP
0.89
0.32
0.38
1
392
A
LEU
0.50
0.70
0.47
2
405
A
GLY
1.00
0.41
0.21
2
406
A
TRP
0.71
0.99
0.35
2
408
A
TYR
0.28
0.80
0.52
2
428
A
GLY
0.48
0.41
0.87
6
436
A
TYR
0.43
0.80
0.71
6
437
A
ARG
0.43
0.51
0.76
6
439
A
TRP
0.33
0.99
0.78
6
440
A
GLY
0.37
0.41
0.81
6
441
A
ALA
0.17
0.38
0.83
6
442
A
TYR
0.40
0.80
0.80
6
443
A
TRP
0.31
0.99
0.80
6
449
A
ILE
0.21
0.64
0.86
6
450
A
TYR
0.21
0.80
0.87
6
452
A
LEU
0.18
0.70
0.79
6
462
A
PHE
0.59
1.00
0.61
3
463
A
LEU
0.47
0.70
0.55
2
465
A
SER
0.71
0.36
0.40
1
466
A
TYR
0.56
0.80
0.28
2
467
A
ALA
0.77
0.38
0.41
1
468
A
GLY
1.00
0.41
0.50
3
470
A
THR
0.67
0.33
0.55
1
471
A
PRO
0.70
0.47
0.62
1
472
A
SER
0.68
0.36
0.68
1
481
A
VAL
0.38
0.56
0.78
6
483
A
ILE
0.66
0.64
0.84
6
485
A
ILE
0.27
0.64
0.86
6
506
A
TRP
0.73
0.99
0.38
2
508
A
ARG
0.84
0.51
0.13
2