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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
THR 2
HIS 3
-0.0002
HIS 3
PRO 4
0.0000
PRO 4
ILE 5
0.0096
ILE 5
ILE 6
-0.0001
ILE 6
HIS 7
-0.0004
HIS 7
ASP 8
0.0035
ASP 8
LEU 9
0.0000
LEU 9
GLU 10
-0.0002
GLU 10
ASN 11
-0.0025
ASN 11
ARG 12
0.0002
ARG 12
TYR 13
-0.0001
TYR 13
THR 14
-0.0257
THR 14
SER 15
-0.0002
SER 15
LYS 16
-0.0002
LYS 16
LYS 17
-0.0774
LYS 17
TYR 18
0.0002
TYR 18
ASP 19
-0.0001
ASP 19
PRO 20
-0.0365
PRO 20
SER 21
0.0002
SER 21
LYS 22
0.0003
LYS 22
LYS 23
-0.1431
LYS 23
VAL 24
0.0001
VAL 24
SER 25
0.0000
SER 25
GLN 26
-0.0861
GLN 26
GLU 27
0.0002
GLU 27
ASP 28
0.0001
ASP 28
LEU 29
0.0156
LEU 29
ALA 30
0.0001
ALA 30
VAL 31
-0.0002
VAL 31
LEU 32
0.0477
LEU 32
LEU 33
0.0001
LEU 33
GLU 34
0.0001
GLU 34
ALA 35
0.0779
ALA 35
LEU 36
-0.0001
LEU 36
ARG 37
0.0000
ARG 37
LEU 38
0.0824
LEU 38
SER 39
0.0002
SER 39
ALA 40
0.0004
ALA 40
SER 41
-0.1004
SER 41
SER 42
0.0003
SER 42
ILE 43
-0.0001
ILE 43
ASN 44
-0.0675
ASN 44
SER 45
-0.0000
SER 45
GLN 46
0.0000
GLN 46
PRO 47
0.0181
PRO 47
TRP 48
0.0001
TRP 48
LYS 49
-0.0002
LYS 49
PHE 50
-0.0180
PHE 50
ILE 51
-0.0000
ILE 51
VAL 52
-0.0002
VAL 52
ILE 53
-0.0365
ILE 53
GLU 54
0.0002
GLU 54
SER 55
0.0000
SER 55
ASP 56
0.0081
ASP 56
ALA 57
-0.0002
ALA 57
ALA 58
0.0001
ALA 58
LYS 59
-0.0230
LYS 59
GLN 60
-0.0002
GLN 60
ARG 61
0.0000
ARG 61
MET 62
-0.0216
MET 62
HIS 63
0.0001
HIS 63
ASP 64
-0.0002
ASP 64
SER 65
-0.0133
SER 65
PHE 66
0.0001
PHE 66
ALA 67
-0.0000
ALA 67
ASN 68
-0.0670
ASN 68
MET 69
-0.0001
MET 69
HIS 70
0.0002
HIS 70
GLN 71
0.0076
GLN 71
PHE 72
0.0002
PHE 72
ASN 73
-0.0004
ASN 73
GLN 74
-0.0116
GLN 74
PRO 75
0.0001
PRO 75
HIS 76
0.0002
HIS 76
ILE 77
-0.0331
ILE 77
LYS 78
0.0001
LYS 78
ALA 79
-0.0000
ALA 79
CYS 80
-0.0116
CYS 80
SER 81
-0.0001
SER 81
HIS 82
0.0001
HIS 82
VAL 83
0.0454
VAL 83
ILE 84
-0.0000
ILE 84
LEU 85
-0.0001
LEU 85
PHE 86
0.0728
PHE 86
ALA 87
-0.0000
ALA 87
ASN 88
0.0000
ASN 88
LYS 89
-0.0247
LYS 89
LEU 90
-0.0000
LEU 90
SER 91
-0.0001
SER 91
TYR 92
0.0422
TYR 92
THR 93
0.0000
THR 93
ARG 94
0.0001
ARG 94
ASP 95
-0.0046
ASP 95
ASP 96
-0.0002
ASP 96
TYR 97
0.0004
TYR 97
ASP 98
0.0269
ASP 98
VAL 99
-0.0002
VAL 99
VAL 100
-0.0001
VAL 100
LEU 101
-0.0364
LEU 101
SER 102
0.0001
SER 102
LYS 103
0.0003
LYS 103
ALA 104
-0.0264
ALA 104
VAL 105
0.0002
VAL 105
ALA 106
-0.0002
ALA 106
ASP 107
0.0237
ASP 107
LYS 108
-0.0002
LYS 108
ARG 109
0.0001
ARG 109
ILE 110
0.0123
ILE 110
THR 111
-0.0002
THR 111
GLU 112
-0.0001
GLU 112
GLU 113
0.0317
GLU 113
GLN 114
-0.0002
GLN 114
LYS 115
0.0001
LYS 115
GLU 116
-0.1215
GLU 116
ALA 117
-0.0001
ALA 117
ALA 118
-0.0002
ALA 118
PHE 119
-0.0959
PHE 119
ALA 120
-0.0002
ALA 120
SER 121
0.0001
SER 121
PHE 122
-0.0694
PHE 122
LYS 123
0.0002
LYS 123
PHE 124
-0.0002
PHE 124
VAL 125
0.0174
VAL 125
GLU 126
0.0001
GLU 126
LEU 127
0.0001
LEU 127
ASN 128
0.0473
ASN 128
CYS 129
0.0001
CYS 129
ASP 130
0.0002
ASP 130
GLU 131
-0.0136
GLU 131
ASN 132
-0.0001
ASN 132
GLY 133
-0.0000
GLY 133
GLU 134
0.0308
GLU 134
HIS 135
-0.0001
HIS 135
LYS 136
0.0003
LYS 136
ALA 137
-0.0215
ALA 137
TRP 138
0.0002
TRP 138
THR 139
0.0001
THR 139
LYS 140
0.0161
LYS 140
PRO 141
-0.0000
PRO 141
GLN 142
0.0002
GLN 142
ALA 143
0.0244
ALA 143
TYR 144
-0.0002
TYR 144
LEU 145
-0.0004
LEU 145
ALA 146
0.0092
ALA 146
LEU 147
-0.0001
LEU 147
GLY 148
-0.0001
GLY 148
ASN 149
-0.0021
ASN 149
ALA 150
0.0001
ALA 150
LEU 151
0.0000
LEU 151
HIS 152
-0.0029
HIS 152
THR 153
-0.0002
THR 153
LEU 154
0.0001
LEU 154
ALA 155
-0.0422
ALA 155
ARG 156
0.0001
ARG 156
LEU 157
-0.0002
LEU 157
ASN 158
-0.0930
ASN 158
ILE 159
-0.0003
ILE 159
ASP 160
0.0001
ASP 160
SER 161
0.0471
SER 161
THR 162
-0.0000
THR 162
THR 163
-0.0003
THR 163
MET 164
0.0053
MET 164
GLU 165
-0.0002
GLU 165
GLY 166
-0.0000
GLY 166
ILE 167
-0.1685
ILE 167
ASP 168
-0.0003
ASP 168
PRO 169
-0.0001
PRO 169
GLU 170
-0.0431
GLU 170
LEU 171
-0.0005
LEU 171
LEU 172
0.0002
LEU 172
SER 173
-0.0084
SER 173
GLU 174
-0.0003
GLU 174
ILE 175
-0.0000
ILE 175
PHE 176
0.0051
PHE 176
ALA 177
0.0002
ALA 177
ASP 178
0.0001
ASP 178
GLU 179
0.0063
GLU 179
LEU 180
0.0002
LEU 180
LYS 181
-0.0002
LYS 181
GLY 182
0.0068
GLY 182
TYR 183
0.0001
TYR 183
GLU 184
0.0001
GLU 184
CYS 185
0.0330
CYS 185
HIS 186
-0.0001
HIS 186
VAL 187
0.0002
VAL 187
ALA 188
0.1324
ALA 188
LEU 189
0.0000
LEU 189
ALA 190
-0.0002
ALA 190
ILE 191
0.0675
ILE 191
GLY 192
-0.0001
GLY 192
TYR 193
0.0002
TYR 193
HIS 194
-0.0853
HIS 194
HIS 195
-0.0004
HIS 195
PRO 196
0.0001
PRO 196
SER 197
-0.0372
SER 197
GLU 198
-0.0003
GLU 198
ASP 199
0.0003
ASP 199
TYR 200
-0.0496
TYR 200
ASN 201
0.0002
ASN 201
ALA 202
-0.0001
ALA 202
SER 203
0.0716
SER 203
LEU 204
0.0001
LEU 204
PRO 205
-0.0003
PRO 205
LYS 206
0.0075
LYS 206
SER 207
-0.0005
SER 207
ARG 208
0.0001
ARG 208
LYS 209
-0.0371
LYS 209
ALA 210
-0.0003
ALA 210
PHE 211
0.0002
PHE 211
GLU 212
0.0011
GLU 212
ASP 213
-0.0002
ASP 213
VAL 214
0.0002
VAL 214
ILE 215
0.1126
ILE 215
THR 216
0.0005
THR 216
ILE 217
-0.0001
ILE 217
LEU 218
0.0657
LEU 218
THR 2
-0.0046
THR 2
HIS 3
0.0000
HIS 3
PRO 4
-0.0003
PRO 4
ILE 5
-0.0149
ILE 5
ILE 6
0.0002
ILE 6
HIS 7
0.0003
HIS 7
ASP 8
0.0048
ASP 8
LEU 9
-0.0005
LEU 9
GLU 10
0.0001
GLU 10
ASN 11
0.0247
ASN 11
ARG 12
0.0002
ARG 12
TYR 13
-0.0005
TYR 13
THR 14
0.0185
THR 14
SER 15
-0.0001
SER 15
LYS 16
0.0001
LYS 16
LYS 17
0.0622
LYS 17
TYR 18
0.0001
TYR 18
ASP 19
-0.0003
ASP 19
PRO 20
0.0330
PRO 20
SER 21
0.0004
SER 21
LYS 22
0.0003
LYS 22
LYS 23
0.1168
LYS 23
VAL 24
-0.0003
VAL 24
SER 25
0.0005
SER 25
GLN 26
0.0675
GLN 26
GLU 27
-0.0002
GLU 27
ASP 28
0.0003
ASP 28
LEU 29
-0.0181
LEU 29
ALA 30
-0.0001
ALA 30
VAL 31
0.0004
VAL 31
LEU 32
-0.0437
LEU 32
LEU 33
-0.0001
LEU 33
GLU 34
0.0002
GLU 34
ALA 35
-0.0658
ALA 35
LEU 36
-0.0001
LEU 36
ARG 37
0.0002
ARG 37
LEU 38
-0.0666
LEU 38
SER 39
0.0002
SER 39
ALA 40
-0.0000
ALA 40
SER 41
0.0855
SER 41
SER 42
0.0002
SER 42
ILE 43
0.0001
ILE 43
ASN 44
0.0800
ASN 44
SER 45
-0.0000
SER 45
GLN 46
0.0002
GLN 46
PRO 47
-0.0021
PRO 47
TRP 48
-0.0002
TRP 48
LYS 49
0.0000
LYS 49
PHE 50
0.0129
PHE 50
ILE 51
0.0000
ILE 51
VAL 52
0.0001
VAL 52
ILE 53
0.0382
ILE 53
GLU 54
0.0001
GLU 54
SER 55
0.0001
SER 55
ASP 56
-0.0025
ASP 56
ALA 57
-0.0001
ALA 57
ALA 58
-0.0001
ALA 58
LYS 59
0.0224
LYS 59
GLN 60
-0.0003
GLN 60
ARG 61
-0.0000
ARG 61
MET 62
0.0153
MET 62
HIS 63
-0.0001
HIS 63
ASP 64
-0.0000
ASP 64
SER 65
0.0104
SER 65
PHE 66
0.0002
PHE 66
ALA 67
0.0001
ALA 67
ASN 68
0.0471
ASN 68
MET 69
-0.0001
MET 69
HIS 70
0.0000
HIS 70
GLN 71
-0.0300
GLN 71
PHE 72
-0.0000
PHE 72
ASN 73
-0.0003
ASN 73
GLN 74
-0.0246
GLN 74
PRO 75
-0.0004
PRO 75
HIS 76
-0.0003
HIS 76
ILE 77
0.0321
ILE 77
LYS 78
-0.0003
LYS 78
ALA 79
0.0003
ALA 79
CYS 80
0.0117
CYS 80
SER 81
0.0001
SER 81
HIS 82
0.0000
HIS 82
VAL 83
-0.0460
VAL 83
ILE 84
0.0002
ILE 84
LEU 85
-0.0004
LEU 85
PHE 86
-0.0728
PHE 86
ALA 87
0.0005
ALA 87
ASN 88
-0.0003
ASN 88
LYS 89
0.0436
LYS 89
LEU 90
-0.0002
LEU 90
SER 91
-0.0001
SER 91
TYR 92
-0.0219
TYR 92
THR 93
-0.0003
THR 93
ARG 94
0.0002
ARG 94
ASP 95
0.0012
ASP 95
ASP 96
0.0000
ASP 96
TYR 97
0.0001
TYR 97
ASP 98
-0.0223
ASP 98
VAL 99
0.0000
VAL 99
VAL 100
0.0004
VAL 100
LEU 101
0.0518
LEU 101
SER 102
-0.0001
SER 102
LYS 103
-0.0001
LYS 103
ALA 104
0.0123
ALA 104
VAL 105
-0.0001
VAL 105
ALA 106
0.0003
ALA 106
ASP 107
-0.0301
ASP 107
LYS 108
0.0002
LYS 108
ARG 109
0.0001
ARG 109
ILE 110
0.0053
ILE 110
THR 111
-0.0001
THR 111
GLU 112
-0.0003
GLU 112
GLU 113
-0.0406
GLU 113
GLN 114
0.0003
GLN 114
LYS 115
-0.0002
LYS 115
GLU 116
0.1111
GLU 116
ALA 117
-0.0002
ALA 117
ALA 118
0.0000
ALA 118
PHE 119
0.1083
PHE 119
ALA 120
-0.0001
ALA 120
SER 121
-0.0002
SER 121
PHE 122
0.1279
PHE 122
LYS 123
-0.0002
LYS 123
PHE 124
-0.0001
PHE 124
VAL 125
-0.0185
VAL 125
GLU 126
-0.0001
GLU 126
LEU 127
-0.0002
LEU 127
ASN 128
-0.0872
ASN 128
CYS 129
-0.0001
CYS 129
ASP 130
0.0003
ASP 130
GLU 131
0.0350
GLU 131
ASN 132
-0.0001
ASN 132
GLY 133
0.0004
GLY 133
GLU 134
-0.0198
GLU 134
HIS 135
-0.0000
HIS 135
LYS 136
0.0001
LYS 136
ALA 137
0.0212
ALA 137
TRP 138
0.0004
TRP 138
THR 139
0.0003
THR 139
LYS 140
0.0009
LYS 140
PRO 141
-0.0001
PRO 141
GLN 142
0.0001
GLN 142
ALA 143
-0.0370
ALA 143
TYR 144
-0.0001
TYR 144
LEU 145
-0.0001
LEU 145
ALA 146
-0.0107
ALA 146
LEU 147
-0.0000
LEU 147
GLY 148
0.0001
GLY 148
ASN 149
-0.0001
ASN 149
ALA 150
-0.0001
ALA 150
LEU 151
-0.0001
LEU 151
HIS 152
0.0028
HIS 152
THR 153
-0.0003
THR 153
LEU 154
-0.0003
LEU 154
ALA 155
0.0382
ALA 155
ARG 156
0.0001
ARG 156
LEU 157
-0.0002
LEU 157
ASN 158
0.0687
ASN 158
ILE 159
0.0002
ILE 159
ASP 160
-0.0002
ASP 160
SER 161
-0.0532
SER 161
THR 162
-0.0002
THR 162
THR 163
0.0005
THR 163
MET 164
-0.0211
MET 164
GLU 165
-0.0001
GLU 165
GLY 166
-0.0001
GLY 166
ILE 167
0.1430
ILE 167
ASP 168
0.0000
ASP 168
PRO 169
0.0004
PRO 169
GLU 170
0.0358
GLU 170
LEU 171
-0.0005
LEU 171
LEU 172
0.0003
LEU 172
SER 173
0.0040
SER 173
GLU 174
0.0001
GLU 174
ILE 175
-0.0000
ILE 175
PHE 176
0.0056
PHE 176
ALA 177
-0.0001
ALA 177
ASP 178
0.0002
ASP 178
GLU 179
0.0030
GLU 179
LEU 180
-0.0000
LEU 180
LYS 181
-0.0001
LYS 181
GLY 182
-0.0110
GLY 182
TYR 183
0.0002
TYR 183
GLU 184
0.0001
GLU 184
CYS 185
-0.0028
CYS 185
HIS 186
0.0003
HIS 186
VAL 187
-0.0001
VAL 187
ALA 188
-0.1210
ALA 188
LEU 189
-0.0002
LEU 189
ALA 190
0.0002
ALA 190
ILE 191
-0.0700
ILE 191
GLY 192
-0.0001
GLY 192
TYR 193
0.0001
TYR 193
HIS 194
0.0675
HIS 194
HIS 195
0.0003
HIS 195
PRO 196
-0.0002
PRO 196
SER 197
0.0238
SER 197
GLU 198
-0.0001
GLU 198
ASP 199
0.0001
ASP 199
TYR 200
0.0221
TYR 200
ASN 201
0.0001
ASN 201
ALA 202
0.0001
ALA 202
SER 203
-0.0793
SER 203
LEU 204
0.0004
LEU 204
PRO 205
-0.0002
PRO 205
LYS 206
0.0107
LYS 206
SER 207
-0.0002
SER 207
ARG 208
0.0004
ARG 208
LYS 209
0.0713
LYS 209
ALA 210
0.0000
ALA 210
PHE 211
-0.0001
PHE 211
GLU 212
0.0007
GLU 212
ASP 213
-0.0000
ASP 213
VAL 214
-0.0001
VAL 214
ILE 215
-0.1145
ILE 215
THR 216
-0.0004
THR 216
ILE 217
0.0001
ILE 217
LEU 218
-0.0471
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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.