This graph displays the distance variation between successive pairs of CA atoms
in the two extreme conformations that were computed for this mode (DQMIN/DQMAX).
Large distance variations can be an indicator for residue pairs that support the
important strain in that particular normal mode movement.
Note that residue pairs between chain breaks or at flexible ends of the protein
may also exhibit large CA-CA distance variations.
If more than one residues ae grouped together into a rigid block (NRBL>1), CA-CA distance variations
between CA atoms in the same block will be very low.
This feature is still experimental and will be further developped in the future.
CA i
CA i+1
vari
SER 3
GLY 4
0.0001
GLY 4
ASN 5
-0.0130
ASN 5
ALA 6
-0.0002
ALA 6
LYS 7
0.0104
LYS 7
ILE 8
-0.0001
ILE 8
GLY 9
0.0041
GLY 9
HIS 10
0.0001
HIS 10
PRO 11
-0.0770
PRO 11
ALA 12
-0.0000
ALA 12
PRO 13
-0.0477
PRO 13
SER 14
-0.0004
SER 14
PHE 15
-0.1189
PHE 15
LYS 16
-0.0001
LYS 16
ALA 17
-0.0678
ALA 17
THR 18
-0.0000
THR 18
ALA 19
0.0218
ALA 19
VAL 20
0.0002
VAL 20
MET 21
-0.0285
MET 21
PRO 22
0.0000
PRO 22
ASP 23
0.0386
ASP 23
GLY 24
-0.0002
GLY 24
GLN 25
-0.0124
GLN 25
PHE 26
0.0001
PHE 26
LYS 27
-0.1078
LYS 27
ASP 28
-0.0001
ASP 28
ILE 29
-0.0421
ILE 29
SER 30
0.0003
SER 30
LEU 31
-0.0773
LEU 31
SER 32
-0.0003
SER 32
ASP 33
0.0108
ASP 33
TYR 34
-0.0001
TYR 34
LYS 35
-0.0625
LYS 35
GLY 36
-0.0000
GLY 36
LYS 37
0.0125
LYS 37
TYR 38
0.0003
TYR 38
VAL 39
-0.0009
VAL 39
VAL 40
0.0003
VAL 40
PHE 41
0.0184
PHE 41
PHE 42
-0.0001
PHE 42
PHE 43
0.0039
PHE 43
TYR 44
0.0002
TYR 44
PRO 45
-0.0292
PRO 45
LEU 46
-0.0001
LEU 46
ASP 47
0.0100
ASP 47
PHE 48
0.0003
PHE 48
THR 49
-0.2239
THR 49
PHE 50
-0.0003
PHE 50
VAL 51
-0.1180
VAL 51
CYS 52
-0.0000
CYS 52
PRO 53
0.2543
PRO 53
THR 54
-0.0004
THR 54
GLU 55
0.1758
GLU 55
ILE 56
-0.0001
ILE 56
ILE 57
-0.0456
ILE 57
ALA 58
-0.0001
ALA 58
PHE 59
0.0698
PHE 59
SER 60
0.0001
SER 60
ASP 61
0.0004
ASP 61
ARG 62
-0.0000
ARG 62
ALA 63
-0.0317
ALA 63
GLU 64
0.0003
GLU 64
GLU 65
0.0219
GLU 65
PHE 66
-0.0001
PHE 66
LYS 67
0.0199
LYS 67
LYS 68
0.0000
LYS 68
LEU 69
0.0434
LEU 69
ASN 70
0.0003
ASN 70
CYS 71
-0.0085
CYS 71
GLN 72
0.0001
GLN 72
VAL 73
0.0243
VAL 73
ILE 74
-0.0002
ILE 74
GLY 75
-0.0118
GLY 75
ALA 76
-0.0003
ALA 76
SER 77
-0.0235
SER 77
VAL 78
-0.0000
VAL 78
ASP 79
0.0036
ASP 79
SER 80
0.0002
SER 80
HIS 81
0.0095
HIS 81
PHE 82
-0.0000
PHE 82
SER 83
-0.0398
SER 83
HIS 84
-0.0002
HIS 84
LEU 85
0.0172
LEU 85
ALA 86
-0.0001
ALA 86
TRP 87
-0.0240
TRP 87
ILE 88
0.0000
ILE 88
ASN 89
-0.0252
ASN 89
THR 90
0.0000
THR 90
PRO 91
-0.0174
PRO 91
LYS 92
-0.0000
LYS 92
LYS 93
0.0697
LYS 93
GLN 94
0.0000
GLN 94
GLY 95
0.0705
GLY 95
GLY 96
-0.0003
GLY 96
LEU 97
0.0428
LEU 97
GLY 98
0.0004
GLY 98
PRO 99
-0.0018
PRO 99
MET 100
-0.0001
MET 100
ASN 101
-0.0125
ASN 101
ILE 102
-0.0002
ILE 102
PRO 103
0.0337
PRO 103
LEU 104
-0.0001
LEU 104
VAL 105
0.0139
VAL 105
SER 106
0.0001
SER 106
ASP 107
0.0209
ASP 107
PRO 108
0.0000
PRO 108
LYS 109
-0.0091
LYS 109
ARG 110
0.0005
ARG 110
THR 111
0.0027
THR 111
ILE 112
-0.0000
ILE 112
ALA 113
-0.0216
ALA 113
GLN 114
-0.0001
GLN 114
ASP 115
0.0174
ASP 115
TYR 116
-0.0000
TYR 116
GLY 117
-0.0562
GLY 117
VAL 118
-0.0001
VAL 118
LEU 119
0.0810
LEU 119
LYS 120
0.0001
LYS 120
ALA 121
-0.0073
ALA 121
ASP 122
-0.0001
ASP 122
GLU 123
-0.0249
GLU 123
GLY 124
0.0000
GLY 124
ILE 125
-0.0310
ILE 125
SER 126
0.0001
SER 126
PHE 127
-0.0452
PHE 127
ARG 128
-0.0002
ARG 128
GLY 129
-0.0643
GLY 129
LEU 130
-0.0003
LEU 130
PHE 131
0.0006
PHE 131
ILE 132
0.0002
ILE 132
ILE 133
0.0199
ILE 133
ASP 134
0.0001
ASP 134
ASP 135
-0.0037
ASP 135
LYS 136
-0.0002
LYS 136
GLY 137
-0.0689
GLY 137
ILE 138
0.0001
ILE 138
LEU 139
0.0707
LEU 139
ARG 140
0.0002
ARG 140
GLN 141
-0.0439
GLN 141
ILE 142
-0.0003
ILE 142
THR 143
-0.0290
THR 143
ILE 144
-0.0002
ILE 144
ASN 145
-0.0791
ASN 145
ASP 146
0.0000
ASP 146
LEU 147
-0.2037
LEU 147
PRO 148
-0.0001
PRO 148
VAL 149
-0.0121
VAL 149
GLY 150
-0.0002
GLY 150
ARG 151
0.0265
ARG 151
SER 152
0.0002
SER 152
VAL 153
0.0763
VAL 153
ASP 154
-0.0001
ASP 154
GLU 155
0.0390
GLU 155
ILE 156
-0.0004
ILE 156
LEU 157
0.0079
LEU 157
ARG 158
-0.0001
ARG 158
LEU 159
-0.0638
LEU 159
VAL 160
0.0002
VAL 160
GLN 161
0.0331
GLN 161
ALA 162
-0.0003
ALA 162
PHE 163
0.0739
PHE 163
GLN 164
-0.0001
GLN 164
PHE 165
0.0800
PHE 165
THR 166
-0.0002
THR 166
ASP 167
-0.0552
ASP 167
LYS 168
0.0001
LYS 168
HIS 169
-0.0142
HIS 169
GLY 170
-0.0000
GLY 170
GLU 171
-0.1183
GLU 171
VAL 172
-0.0000
VAL 172
CYS 173
0.0591
CYS 173
PRO 174
0.0001
PRO 174
ALA 175
-0.0444
ALA 175
SER 3
0.0036
SER 3
GLY 4
0.0002
GLY 4
ASN 5
-0.0069
ASN 5
ALA 6
-0.0002
ALA 6
LYS 7
0.0056
LYS 7
ILE 8
0.0002
ILE 8
GLY 9
0.0062
GLY 9
HIS 10
0.0001
HIS 10
PRO 11
-0.0776
PRO 11
ALA 12
0.0001
ALA 12
PRO 13
-0.0598
PRO 13
SER 14
0.0003
SER 14
PHE 15
-0.1288
PHE 15
LYS 16
-0.0002
LYS 16
ALA 17
-0.0695
ALA 17
THR 18
-0.0002
THR 18
ALA 19
0.0190
ALA 19
VAL 20
0.0002
VAL 20
MET 21
-0.0253
MET 21
PRO 22
-0.0000
PRO 22
ASP 23
0.0397
ASP 23
GLY 24
-0.0000
GLY 24
GLN 25
-0.0155
GLN 25
PHE 26
-0.0003
PHE 26
LYS 27
-0.1085
LYS 27
ASP 28
-0.0002
ASP 28
ILE 29
-0.0403
ILE 29
SER 30
0.0001
SER 30
LEU 31
-0.0864
LEU 31
SER 32
0.0000
SER 32
ASP 33
0.0103
ASP 33
TYR 34
-0.0000
TYR 34
LYS 35
-0.0658
LYS 35
GLY 36
0.0001
GLY 36
LYS 37
0.0093
LYS 37
TYR 38
0.0001
TYR 38
VAL 39
-0.0065
VAL 39
VAL 40
-0.0003
VAL 40
PHE 41
0.0176
PHE 41
PHE 42
0.0001
PHE 42
PHE 43
0.0060
PHE 43
TYR 44
-0.0001
TYR 44
PRO 45
-0.0281
PRO 45
LEU 46
0.0002
LEU 46
ASP 47
0.0095
ASP 47
PHE 48
0.0003
PHE 48
THR 49
-0.2025
THR 49
PHE 50
-0.0001
PHE 50
VAL 51
-0.0992
VAL 51
CYS 52
0.0002
CYS 52
PRO 53
0.2210
PRO 53
THR 54
0.0000
THR 54
GLU 55
0.1788
GLU 55
ILE 56
0.0000
ILE 56
ILE 57
-0.0419
ILE 57
ALA 58
0.0001
ALA 58
PHE 59
0.0694
PHE 59
SER 60
-0.0003
SER 60
ASP 61
0.0044
ASP 61
ARG 62
0.0003
ARG 62
ALA 63
-0.0347
ALA 63
GLU 64
0.0001
GLU 64
GLU 65
0.0224
GLU 65
PHE 66
0.0002
PHE 66
LYS 67
0.0176
LYS 67
LYS 68
-0.0004
LYS 68
LEU 69
0.0480
LEU 69
ASN 70
0.0000
ASN 70
CYS 71
-0.0093
CYS 71
GLN 72
-0.0002
GLN 72
VAL 73
0.0205
VAL 73
ILE 74
0.0003
ILE 74
GLY 75
-0.0103
GLY 75
ALA 76
0.0001
ALA 76
SER 77
-0.0183
SER 77
VAL 78
0.0002
VAL 78
ASP 79
-0.0039
ASP 79
SER 80
0.0002
SER 80
HIS 81
0.0100
HIS 81
PHE 82
0.0002
PHE 82
SER 83
-0.0323
SER 83
HIS 84
-0.0002
HIS 84
LEU 85
0.0155
LEU 85
ALA 86
-0.0003
ALA 86
TRP 87
-0.0136
TRP 87
ILE 88
-0.0004
ILE 88
ASN 89
-0.0313
ASN 89
THR 90
-0.0002
THR 90
PRO 91
-0.0180
PRO 91
LYS 92
-0.0001
LYS 92
LYS 93
0.0808
LYS 93
GLN 94
-0.0001
GLN 94
GLY 95
0.0843
GLY 95
GLY 96
-0.0005
GLY 96
LEU 97
0.0332
LEU 97
GLY 98
-0.0004
GLY 98
PRO 99
-0.0180
PRO 99
MET 100
-0.0001
MET 100
ASN 101
-0.0156
ASN 101
ILE 102
0.0002
ILE 102
PRO 103
0.0344
PRO 103
LEU 104
-0.0001
LEU 104
VAL 105
0.0135
VAL 105
SER 106
0.0001
SER 106
ASP 107
0.0143
ASP 107
PRO 108
0.0003
PRO 108
LYS 109
-0.0140
LYS 109
ARG 110
-0.0001
ARG 110
THR 111
0.0047
THR 111
ILE 112
0.0002
ILE 112
ALA 113
-0.0170
ALA 113
GLN 114
0.0002
GLN 114
ASP 115
0.0182
ASP 115
TYR 116
0.0001
TYR 116
GLY 117
-0.0581
GLY 117
VAL 118
-0.0006
VAL 118
LEU 119
0.0758
LEU 119
LYS 120
-0.0001
LYS 120
ALA 121
-0.0101
ALA 121
ASP 122
0.0000
ASP 122
GLU 123
-0.0292
GLU 123
GLY 124
-0.0002
GLY 124
ILE 125
-0.0328
ILE 125
SER 126
-0.0004
SER 126
PHE 127
-0.0415
PHE 127
ARG 128
0.0003
ARG 128
GLY 129
-0.0701
GLY 129
LEU 130
-0.0003
LEU 130
PHE 131
-0.0031
PHE 131
ILE 132
0.0004
ILE 132
ILE 133
0.0191
ILE 133
ASP 134
0.0002
ASP 134
ASP 135
-0.0096
ASP 135
LYS 136
0.0000
LYS 136
GLY 137
-0.0780
GLY 137
ILE 138
-0.0003
ILE 138
LEU 139
0.0902
LEU 139
ARG 140
0.0001
ARG 140
GLN 141
-0.0530
GLN 141
ILE 142
-0.0004
ILE 142
THR 143
-0.0269
THR 143
ILE 144
0.0000
ILE 144
ASN 145
-0.0761
ASN 145
ASP 146
0.0000
ASP 146
LEU 147
-0.1951
LEU 147
PRO 148
0.0001
PRO 148
VAL 149
-0.0069
VAL 149
GLY 150
0.0003
GLY 150
ARG 151
0.0081
ARG 151
SER 152
-0.0001
SER 152
VAL 153
0.0764
VAL 153
ASP 154
-0.0001
ASP 154
GLU 155
0.0400
GLU 155
ILE 156
0.0001
ILE 156
LEU 157
0.0155
LEU 157
ARG 158
-0.0003
ARG 158
LEU 159
-0.0659
LEU 159
VAL 160
-0.0002
VAL 160
GLN 161
0.0420
GLN 161
ALA 162
-0.0001
ALA 162
PHE 163
0.0700
PHE 163
GLN 164
-0.0002
GLN 164
PHE 165
0.0577
PHE 165
THR 166
-0.0001
THR 166
ASP 167
-0.0364
ASP 167
LYS 168
0.0000
LYS 168
HIS 169
0.0029
HIS 169
GLY 170
-0.0001
GLY 170
GLU 171
-0.1457
GLU 171
VAL 172
0.0000
VAL 172
CYS 173
0.0803
CYS 173
PRO 174
0.0000
PRO 174
ALA 175
-0.0457
If you find results from this site helpful for your research, please cite one of our papers:
elNémo
is maintained by Yves-Henri Sanejouand.
It was developed
by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.