4. Model quality ?

For models with atomic structures, MolProbity analysis is performed. For models with coarse-grained or multi-scale structures, excluded volume analysis is performed.

4.1b. MolProbity Analysis ?

Excluded volume satisfaction for the models in the entry are listed below. The Analysed column shows the number of particle-partice or particle-atom pairs for which excluded volume was analysed.
Standard geometry: bond outliers ?

There are 5994 bond length outliers in this entry (2.90% of 206365 assessed bonds). A summary is provided below. The output is limited to 100 rows.

Chain Res Type Atoms |Z| Observed (Å) Ideal (Å) Model ID (Worst) Models (Total)
D1
88
SER
N-CA
597.49
12.81
1.46
1
1
D2
88
SER
N-CA
597.41
12.81
1.46
1
1
A3
56
LEU
CA-C
534.50
12.75
1.52
1
1
A2
56
LEU
CA-C
534.46
12.75
1.52
1
1
A4
56
LEU
CA-C
475.10
11.50
1.52
1
1
A1
56
LEU
CA-C
475.05
11.50
1.52
1
1
W1
522
GLU
N-CA
460.47
10.21
1.46
1
1
d1
98
SER
N-CA
446.89
9.95
1.46
1
1
d2
98
SER
N-CA
446.88
9.95
1.46
1
1
A1
405
ASP
N-CA
426.20
9.56
1.46
1
1
A4
405
ASP
N-CA
426.16
9.56
1.46
1
1
A1
205
ASN
N-CA
395.33
8.97
1.46
1
1
A4
205
ASN
N-CA
395.30
8.97
1.46
1
1
B2
74
THR
CA-C
391.90
9.75
1.52
1
1
B1
74
THR
CA-C
391.85
9.75
1.52
1
1
B2
75
ILE
N-CA
385.14
8.78
1.46
1
1
B1
75
ILE
N-CA
385.10
8.77
1.46
1
1
C1
1651
ASP
N-CA
382.37
8.72
1.46
1
1
C2
1651
ASP
N-CA
382.35
8.72
1.46
1
1
J5
727
SER
CA-C
380.85
9.52
1.52
1
1
J3
727
SER
CA-C
380.81
9.52
1.52
1
1
J6
727
SER
CA-C
380.75
9.52
1.52
1
1
J4
727
SER
CA-C
380.75
9.52
1.52
1
1
B1
508
PRO
N-CD
380.46
6.80
1.47
1
1
B2
508
PRO
N-CD
380.43
6.80
1.47
1
1
D2
309
LEU
CA-C
377.26
9.45
1.52
1
1
D1
309
LEU
CA-C
377.23
9.45
1.52
1
1
B2
407
ALA
N-CA
376.77
8.62
1.46
1
1
B1
407
ALA
N-CA
376.66
8.61
1.46
1
1
V1
1126
LEU
CA-C
362.47
9.14
1.52
1
1
D1
481
GLY
N-CA
358.86
7.19
1.45
1
1
D2
481
GLY
N-CA
358.73
7.19
1.45
1
1
W2
452
SER
CA-C
350.15
8.88
1.52
1
1
I1
270
PRO
N-CD
347.67
6.34
1.47
1
1
I4
270
PRO
N-CD
347.58
6.34
1.47
1
1
I1
270
PRO
N-CA
342.88
6.61
1.47
1
1
I4
270
PRO
N-CA
342.77
6.61
1.47
1
1
D2
339
GLU
N-CA
337.74
7.88
1.46
1
1
D1
339
GLU
N-CA
337.69
7.87
1.46
1
1
V2
1126
LEU
CA-C
334.06
8.54
1.52
1
1
A2
405
ASP
N-CA
329.74
7.72
1.46
1
1
A3
405
ASP
N-CA
329.72
7.72
1.46
1
1
V1
1429
LYS
N-CA
328.63
7.70
1.46
1
1
B2
1567
GLN
CA-C
324.92
8.35
1.52
1
1
B1
1567
GLN
CA-C
324.85
8.35
1.52
1
1
W1
452
SER
CA-C
323.04
8.31
1.52
1
1
C1
814
ASN
N-CA
321.81
7.57
1.46
1
1
C2
814
ASN
N-CA
321.81
7.57
1.46
1
1
J1
637
LEU
N-CA
314.69
7.44
1.46
1
1
C1
1644
ASP
CA-C
313.81
8.12
1.52
1
1
C2
1644
ASP
CA-C
313.78
8.11
1.52
1
1
d1
992
CYS
CA-C
312.75
8.09
1.52
1
1
d2
992
CYS
CA-C
312.72
8.09
1.52
1
1
A4
374
TYR
CA-C
308.26
8.00
1.52
1
1
A1
374
TYR
CA-C
308.24
8.00
1.52
1
1
I1
359
THR
CA-C
306.54
7.96
1.52
1
1
I3
359
THR
CA-C
306.53
7.96
1.52
1
1
I2
359
THR
CA-C
306.52
7.96
1.52
1
1
I4
359
THR
CA-C
306.45
7.96
1.52
1
1
B1
341
PHE
CA-C
303.51
7.90
1.52
1
1
B2
341
PHE
CA-C
303.42
7.90
1.52
1
1
A2
205
ASN
N-CA
301.80
7.19
1.46
1
1
A3
205
ASN
N-CA
301.74
7.19
1.46
1
1
J2
637
LEU
N-CA
300.30
7.16
1.46
1
1
H2
476
GLN
CA-C
298.52
7.79
1.52
1
1
H4
476
GLN
CA-C
298.52
7.79
1.52
1
1
H3
476
GLN
CA-C
298.52
7.79
1.52
1
1
H1
476
GLN
CA-C
298.44
7.79
1.52
1
1
I2
433
LYS
N-CA
297.94
7.12
1.46
1
1
I1
433
LYS
N-CA
297.92
7.12
1.46
1
1
I4
433
LYS
N-CA
297.89
7.12
1.46
1
1
I3
433
LYS
N-CA
297.89
7.12
1.46
1
1
B1
1056
LYS
N-CA
295.77
7.08
1.46
1
1
B2
1056
LYS
N-CA
295.71
7.08
1.46
1
1
B1
1593
HIS
N-CA
295.05
7.06
1.46
1
1
B2
1593
HIS
N-CA
294.99
7.06
1.46
1
1
C1
798
ASN
CA-C
292.80
7.67
1.52
1
1
C2
798
ASN
CA-C
292.79
7.67
1.52
1
1
V1
1117
TYR
N-CA
289.75
6.96
1.46
1
1
I4
271
PRO
N-CD
287.72
5.50
1.47
1
1
I1
271
PRO
N-CD
287.63
5.50
1.47
1
1
V2
1382
VAL
N-CA
287.48
6.92
1.46
1
1
W2
522
GLU
N-CA
284.38
6.86
1.46
1
1
d1
992
CYS
N-CA
284.36
6.86
1.46
1
1
d2
992
CYS
N-CA
284.35
6.86
1.46
1
1
H4
287
GLN
N-CA
283.05
6.84
1.46
1
1
H1
287
GLN
N-CA
282.97
6.83
1.46
1
1
I4
369
LEU
N-CA
280.41
6.79
1.46
1
1
I2
369
LEU
N-CA
280.38
6.79
1.46
1
1
I1
369
LEU
N-CA
280.32
6.78
1.46
1
1
I3
369
LEU
N-CA
280.22
6.78
1.46
1
1
B2
649
LYS
N-CA
278.65
6.75
1.46
1
1
B1
649
LYS
N-CA
278.64
6.75
1.46
1
1
V2
1332
LYS
N-CA
276.68
6.71
1.46
1
1
B2
74
THR
N-CA
274.01
6.66
1.46
1
1
B1
74
THR
N-CA
273.90
6.66
1.46
1
1
B1
342
ASP
N-CA
272.73
6.64
1.46
1
1
B2
342
ASP
N-CA
272.64
6.64
1.46
1
1
B2
1383
GLN
N-CA
271.21
6.61
1.46
1
1
B1
1383
GLN
N-CA
271.20
6.61
1.46
1
1

Standard geometry: angle outliers ?

There are 17381 bond angle outliers in this entry (6.23% of 279179 assessed bonds). A summary is provided below. The output is limited to 100 rows.

Chain Res Type Atoms |Z| Observed (Å) Ideal (Å) Model ID (Worst) Models (Total)
A1
746
PRO
N-CA-CB
79.70
15.33
103.00
1
1
A4
746
PRO
N-CA-CB
79.66
15.38
103.00
1
1
B1
508
PRO
CA-N-CD
76.15
5.39
112.00
1
1
B2
508
PRO
CA-N-CD
76.14
5.40
112.00
1
1
D2
482
PRO
CA-N-CD
73.95
8.46
112.00
1
1
D1
482
PRO
CA-N-CD
73.94
8.48
112.00
1
1
C1
293
PRO
CA-N-CD
72.37
10.68
112.00
1
1
C2
293
PRO
CA-N-CD
72.33
10.74
112.00
1
1
W2
123
PRO
CA-N-CD
67.20
17.93
112.00
1
1
B1
1566
TYR
C-N-CA
66.63
1.77
121.70
1
1
B2
1566
TYR
C-N-CA
66.61
1.81
121.70
1
1
C2
1584
ASN
CA-C-N
65.87
18.10
116.90
1
1
C1
1584
ASN
CA-C-N
65.86
18.12
116.90
1
1
D1
481
GLY
CA-C-N
65.14
19.20
116.90
1
1
D2
481
GLY
CA-C-N
65.13
19.20
116.90
1
1
B1
407
ALA
CA-C-N
64.77
19.75
116.90
1
1
B2
407
ALA
CA-C-N
64.74
19.79
116.90
1
1
I1
270
PRO
CA-N-CD
64.61
21.54
112.00
1
1
I4
270
PRO
CA-N-CD
64.60
21.55
112.00
1
1
C2
1126
PRO
CA-N-CD
64.25
22.05
112.00
1
1
C1
1126
PRO
CA-N-CD
64.20
22.11
112.00
1
1
A2
746
PRO
N-CA-CB
63.50
172.85
103.00
1
1
A3
746
PRO
N-CA-CB
63.41
172.76
103.00
1
1
A1
405
ASP
CA-C-N
62.83
22.65
116.90
1
1
A4
405
ASP
CA-C-N
62.81
22.69
116.90
1
1
A4
55
GLN
C-N-CA
62.46
9.26
121.70
1
1
A1
55
GLN
C-N-CA
62.45
9.29
121.70
1
1
I4
271
PRO
CA-N-CD
62.22
24.89
112.00
1
1
I1
271
PRO
CA-N-CD
62.21
24.90
112.00
1
1
J6
726
VAL
C-N-CA
62.19
9.75
121.70
1
1
J5
726
VAL
C-N-CA
62.18
9.78
121.70
1
1
J4
726
VAL
C-N-CA
62.18
9.78
121.70
1
1
J3
726
VAL
C-N-CA
62.16
9.81
121.70
1
1
A2
405
ASP
CA-C-N
61.13
25.21
116.90
1
1
A3
405
ASP
CA-C-N
61.12
25.22
116.90
1
1
d1
1015
GLU
C-N-CA
60.88
12.11
121.70
1
1
C2
797
LEU
C-N-CA
60.87
12.14
121.70
1
1
d2
1015
GLU
C-N-CA
60.86
12.16
121.70
1
1
C1
797
LEU
C-N-CA
60.82
12.22
121.70
1
1
I2
271
PRO
CA-N-CD
60.61
27.14
112.00
1
1
I3
271
PRO
CA-N-CD
60.60
27.16
112.00
1
1
d2
831
LYS
CA-C-O
60.36
18.19
120.80
1
1
d1
831
LYS
CA-C-O
60.35
18.20
120.80
1
1
B1
1400
PRO
CA-N-CD
60.15
27.79
112.00
1
1
A3
359
ASN
C-N-CA
60.14
13.45
121.70
1
1
B2
1400
PRO
CA-N-CD
60.13
27.82
112.00
1
1
A2
359
ASN
C-N-CA
60.09
13.54
121.70
1
1
B2
90
ALA
C-N-CA
59.56
14.49
121.70
1
1
B1
90
ALA
C-N-CA
59.52
14.56
121.70
1
1
I3
270
PRO
CA-N-CD
59.41
28.82
112.00
1
1
I2
270
PRO
CA-N-CD
59.41
28.83
112.00
1
1
J2
777
ASN
C-N-CA
59.09
15.33
121.70
1
1
B2
405
SER
C-N-CA
59.03
15.44
121.70
1
1
B1
405
SER
C-N-CA
59.00
15.50
121.70
1
1
D1
932
ILE
C-N-CA
58.66
16.12
121.70
1
1
D2
932
ILE
C-N-CA
58.62
16.19
121.70
1
1
B2
408
PRO
CA-N-CD
58.53
30.06
112.00
1
1
B1
408
PRO
CA-N-CD
58.51
30.09
112.00
1
1
A1
746
PRO
C-N-CA
58.25
16.85
121.70
1
1
A4
746
PRO
C-N-CA
58.24
16.87
121.70
1
1
A2
20
LYS
CA-C-O
58.14
21.96
120.80
1
1
A3
20
LYS
CA-C-O
58.13
21.98
120.80
1
1
A1
515
LEU
N-CA-CB
58.04
11.83
110.50
1
1
A4
515
LEU
N-CA-CB
58.04
11.83
110.50
1
1
B1
1099
PHE
C-N-CA
58.00
17.29
121.70
1
1
B2
1099
PHE
C-N-CA
58.00
17.30
121.70
1
1
B2
165
ASN
C-N-CA
57.70
17.83
121.70
1
1
B1
165
ASN
C-N-CA
57.70
17.83
121.70
1
1
D2
961
PRO
CA-N-CD
57.51
31.48
112.00
1
1
D1
961
PRO
CA-N-CD
57.49
31.51
112.00
1
1
d1
1061
PRO
CA-N-CD
57.49
31.52
112.00
1
1
d2
1061
PRO
CA-N-CD
57.46
31.56
112.00
1
1
C2
1072
PRO
N-CA-CB
57.22
165.95
103.00
1
1
C1
1072
PRO
N-CA-CB
57.10
165.81
103.00
1
1
A1
359
ASN
C-N-CA
57.10
18.92
121.70
1
1
A4
359
ASN
C-N-CA
57.09
18.94
121.70
1
1
D2
514
ARG
C-N-CA
56.53
19.95
121.70
1
1
D1
514
ARG
C-N-CA
56.51
19.98
121.70
1
1
V2
1238
PHE
C-N-CA
56.06
20.78
121.70
1
1
B1
1009
PRO
CA-N-CD
55.74
33.97
112.00
1
1
B2
1009
PRO
CA-N-CD
55.73
33.97
112.00
1
1
I3
358
LEU
C-N-CA
55.69
21.45
121.70
1
1
I2
358
LEU
C-N-CA
55.68
21.47
121.70
1
1
I1
358
LEU
C-N-CA
55.62
21.58
121.70
1
1
I4
358
LEU
C-N-CA
55.62
21.58
121.70
1
1
A4
373
ALA
C-N-CA
55.43
21.92
121.70
1
1
A1
373
ALA
C-N-CA
55.39
21.99
121.70
1
1
I1
406
PHE
C-N-CA
55.34
22.09
121.70
1
1
W1
625
HIS
CA-C-O
55.32
26.75
120.80
1
1
I3
406
PHE
C-N-CA
55.32
22.13
121.70
1
1
I4
406
PHE
C-N-CA
55.30
22.15
121.70
1
1
I2
406
PHE
C-N-CA
55.28
22.20
121.70
1
1
D1
729
PHE
C-N-CA
55.25
22.25
121.70
1
1
C2
1272
LEU
CA-C-O
55.23
26.92
120.80
1
1
D2
729
PHE
C-N-CA
55.22
22.31
121.70
1
1
C1
1272
LEU
CA-C-O
55.20
26.96
120.80
1
1
V2
1125
ASP
C-N-CA
55.06
22.58
121.70
1
1
D2
829
LEU
C-N-CA
54.90
22.89
121.70
1
1
D1
829
LEU
C-N-CA
54.88
22.92
121.70
1
1
D1
339
GLU
CA-C-N
54.53
7.14
116.20
1
1

Too-close contacts ?

The following all-atom clashscore is based on a MolProbity analysis. All-atom clashscore is defined as the number of clashes found per 1000 atoms (including hydrogen atoms). The table below contains clashscores for all atomic models in this entry.

Model ID Clash score Number of clashes
1
0.00
0

There are no too-close contacts.
Torsion angles: Protein backbone ?

In the following table, Ramachandran outliers are listed. The Analysed column shows the number of residues for which the backbone conformation was analysed.

Model ID Analysed Favored Allowed Outliers
1
24713
21896
1749
1068

There are 1068 unique backbone outliers. Detailed list of outliers are tabulated below. The output is limited to 100 rows.

Chain Res Type Models (Total)
91
65
PHE
1
91
77
VAL
1
91
82
GLY
1
91
83
PRO
1
92
37
LEU
1
92
54
GLY
1
92
55
ASN
1
92
65
PHE
1
92
77
VAL
1
92
82
GLY
1
92
83
PRO
1
A1
21
LYS
1
A1
35
ALA
1
A1
37
SER
1
A1
46
ILE
1
A1
47
ASN
1
A1
55
GLN
1
A1
264
LYS
1
A1
268
ILE
1
A1
269
ASN
1
A1
297
GLY
1
A1
316
ALA
1
A1
317
ASP
1
A1
328
ILE
1
A1
346
ILE
1
A1
359
ASN
1
A1
406
PRO
1
A1
423
LYS
1
A1
470
GLY
1
A1
474
PHE
1
A1
475
SER
1
A1
476
ASN
1
A1
613
VAL
1
A1
675
VAL
1
A1
697
PHE
1
A1
732
TRP
1
A1
744
LEU
1
A1
746
PRO
1
A1
764
ASP
1
A1
765
ASP
1
A1
795
GLN
1
A1
834
ASN
1
A2
35
ALA
1
A2
37
SER
1
A2
46
ILE
1
A2
47
ASN
1
A2
55
GLN
1
A2
264
LYS
1
A2
268
ILE
1
A2
269
ASN
1
A2
297
GLY
1
A2
316
ALA
1
A2
317
ASP
1
A2
328
ILE
1
A2
346
ILE
1
A2
359
ASN
1
A2
373
ALA
1
A2
406
PRO
1
A2
423
LYS
1
A2
470
GLY
1
A2
474
PHE
1
A2
475
SER
1
A2
476
ASN
1
A2
613
VAL
1
A2
675
VAL
1
A2
697
PHE
1
A2
732
TRP
1
A2
744
LEU
1
A2
746
PRO
1
A2
764
ASP
1
A2
765
ASP
1
A2
795
GLN
1
A3
35
ALA
1
A3
37
SER
1
A3
46
ILE
1
A3
47
ASN
1
A3
55
GLN
1
A3
264
LYS
1
A3
268
ILE
1
A3
269
ASN
1
A3
297
GLY
1
A3
316
ALA
1
A3
317
ASP
1
A3
328
ILE
1
A3
346
ILE
1
A3
359
ASN
1
A3
373
ALA
1
A3
406
PRO
1
A3
423
LYS
1
A3
470
GLY
1
A3
474
PHE
1
A3
475
SER
1
A3
476
ASN
1
A3
613
VAL
1
A3
675
VAL
1
A3
697
PHE
1
A3
732
TRP
1
A3
744
LEU
1
A3
746
PRO
1
A3
764
ASP
1

Torsion angles : Protein sidechains ?
In the following table, sidechain rotameric outliers are listed. The Analysed column shows the number of residues for which the sidechain conformation was analysed.

Model ID Analysed Favored Allowed Outliers
1
22485
19359
1717
1409

There are 1409 unique sidechain outliers. Detailed list of outliers are tabulated below. The output is limited to 100 rows.

Chain Res Type Models (Total)
91
7
SER
1
91
8
THR
1
91
17
THR
1
91
44
THR
1
91
52
LYS
1
91
76
PHE
1
92
17
THR
1
92
52
LYS
1
92
55
ASN
1
92
76
PHE
1
A1
22
LEU
1
A1
37
SER
1
A1
47
ASN
1
A1
56
LEU
1
A1
205
ASN
1
A1
206
ASN
1
A1
232
PHE
1
A1
272
GLU
1
A1
312
LYS
1
A1
313
LEU
1
A1
318
LYS
1
A1
360
ILE
1
A1
374
TYR
1
A1
405
ASP
1
A1
406
PRO
1
A1
429
THR
1
A1
439
HIS
1
A1
444
LYS
1
A1
500
GLU
1
A1
515
LEU
1
A1
542
THR
1
A1
625
GLU
1
A1
668
SER
1
A1
672
GLN
1
A1
683
THR
1
A1
697
PHE
1
A1
746
PRO
1
A1
747
PHE
1
A1
754
ARG
1
A1
765
ASP
1
A1
795
GLN
1
A1
834
ASN
1
A1
835
ILE
1
A2
20
LYS
1
A2
22
LEU
1
A2
37
SER
1
A2
47
ASN
1
A2
56
LEU
1
A2
232
PHE
1
A2
272
GLU
1
A2
312
LYS
1
A2
313
LEU
1
A2
318
LYS
1
A2
360
ILE
1
A2
367
PHE
1
A2
374
TYR
1
A2
405
ASP
1
A2
429
THR
1
A2
439
HIS
1
A2
500
GLU
1
A2
515
LEU
1
A2
542
THR
1
A2
625
GLU
1
A2
668
SER
1
A2
672
GLN
1
A2
683
THR
1
A2
697
PHE
1
A2
746
PRO
1
A2
747
PHE
1
A2
754
ARG
1
A2
765
ASP
1
A2
795
GLN
1
A3
20
LYS
1
A3
22
LEU
1
A3
37
SER
1
A3
47
ASN
1
A3
56
LEU
1
A3
232
PHE
1
A3
272
GLU
1
A3
312
LYS
1
A3
313
LEU
1
A3
318
LYS
1
A3
360
ILE
1
A3
367
PHE
1
A3
374
TYR
1
A3
405
ASP
1
A3
429
THR
1
A3
439
HIS
1
A3
500
GLU
1
A3
515
LEU
1
A3
542
THR
1
A3
625
GLU
1
A3
668
SER
1
A3
672
GLN
1
A3
683
THR
1
A3
697
PHE
1
A3
746
PRO
1
A3
747
PHE
1
A3
754
ARG
1
A3
765
ASP
1