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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
0.0001
HIS 3
PRO 4
0.0000
PRO 4
ILE 5
-0.0008
ILE 5
ILE 6
0.0001
ILE 6
HIS 7
-0.0005
HIS 7
ASP 8
-0.0077
ASP 8
LEU 9
-0.0001
LEU 9
GLU 10
0.0001
GLU 10
ASN 11
-0.0009
ASN 11
ARG 12
0.0002
ARG 12
TYR 13
0.0003
TYR 13
THR 14
-0.0333
THR 14
SER 15
-0.0004
SER 15
LYS 16
0.0003
LYS 16
LYS 17
0.0719
LYS 17
TYR 18
0.0001
TYR 18
ASP 19
0.0000
ASP 19
PRO 20
0.0522
PRO 20
SER 21
0.0002
SER 21
LYS 22
-0.0004
LYS 22
LYS 23
0.0079
LYS 23
VAL 24
-0.0001
VAL 24
SER 25
0.0002
SER 25
GLN 26
0.0075
GLN 26
GLU 27
-0.0003
GLU 27
ASP 28
0.0002
ASP 28
LEU 29
0.0305
LEU 29
ALA 30
0.0001
ALA 30
VAL 31
-0.0001
VAL 31
LEU 32
0.0072
LEU 32
LEU 33
0.0001
LEU 33
GLU 34
-0.0000
GLU 34
ALA 35
0.0180
ALA 35
LEU 36
0.0000
LEU 36
ARG 37
0.0001
ARG 37
LEU 38
0.0662
LEU 38
SER 39
-0.0002
SER 39
ALA 40
0.0000
ALA 40
SER 41
-0.0874
SER 41
SER 42
-0.0001
SER 42
ILE 43
0.0001
ILE 43
ASN 44
-0.2269
ASN 44
SER 45
0.0002
SER 45
GLN 46
-0.0003
GLN 46
PRO 47
-0.0294
PRO 47
TRP 48
-0.0001
TRP 48
LYS 49
0.0001
LYS 49
PHE 50
-0.0237
PHE 50
ILE 51
0.0004
ILE 51
VAL 52
0.0001
VAL 52
ILE 53
-0.1113
ILE 53
GLU 54
-0.0000
GLU 54
SER 55
-0.0004
SER 55
ASP 56
-0.0622
ASP 56
ALA 57
0.0000
ALA 57
ALA 58
0.0001
ALA 58
LYS 59
0.0023
LYS 59
GLN 60
0.0001
GLN 60
ARG 61
-0.0002
ARG 61
MET 62
-0.0008
MET 62
HIS 63
0.0001
HIS 63
ASP 64
-0.0002
ASP 64
SER 65
0.0312
SER 65
PHE 66
0.0003
PHE 66
ALA 67
0.0003
ALA 67
ASN 68
0.0189
ASN 68
MET 69
-0.0001
MET 69
HIS 70
-0.0000
HIS 70
GLN 71
-0.0103
GLN 71
PHE 72
0.0002
PHE 72
ASN 73
0.0004
ASN 73
GLN 74
0.0677
GLN 74
PRO 75
0.0002
PRO 75
HIS 76
-0.0001
HIS 76
ILE 77
-0.0195
ILE 77
LYS 78
-0.0000
LYS 78
ALA 79
-0.0001
ALA 79
CYS 80
-0.0076
CYS 80
SER 81
-0.0003
SER 81
HIS 82
-0.0000
HIS 82
VAL 83
0.0188
VAL 83
ILE 84
-0.0001
ILE 84
LEU 85
0.0002
LEU 85
PHE 86
-0.0052
PHE 86
ALA 87
0.0001
ALA 87
ASN 88
-0.0002
ASN 88
LYS 89
-0.0603
LYS 89
LEU 90
-0.0001
LEU 90
SER 91
0.0002
SER 91
TYR 92
0.0023
TYR 92
THR 93
0.0003
THR 93
ARG 94
-0.0002
ARG 94
ASP 95
-0.0242
ASP 95
ASP 96
-0.0002
ASP 96
TYR 97
-0.0004
TYR 97
ASP 98
-0.0232
ASP 98
VAL 99
0.0001
VAL 99
VAL 100
0.0003
VAL 100
LEU 101
-0.0543
LEU 101
SER 102
-0.0003
SER 102
LYS 103
0.0000
LYS 103
ALA 104
0.0422
ALA 104
VAL 105
-0.0001
VAL 105
ALA 106
-0.0001
ALA 106
ASP 107
-0.0605
ASP 107
LYS 108
0.0002
LYS 108
ARG 109
0.0002
ARG 109
ILE 110
0.2137
ILE 110
THR 111
-0.0000
THR 111
GLU 112
-0.0000
GLU 112
GLU 113
0.0420
GLU 113
GLN 114
-0.0001
GLN 114
LYS 115
0.0002
LYS 115
GLU 116
-0.1516
GLU 116
ALA 117
0.0003
ALA 117
ALA 118
0.0001
ALA 118
PHE 119
-0.1940
PHE 119
ALA 120
0.0000
ALA 120
SER 121
0.0003
SER 121
PHE 122
-0.0867
PHE 122
LYS 123
0.0001
LYS 123
PHE 124
0.0000
PHE 124
VAL 125
0.0184
VAL 125
GLU 126
0.0002
GLU 126
LEU 127
-0.0003
LEU 127
ASN 128
0.0540
ASN 128
CYS 129
-0.0000
CYS 129
ASP 130
0.0001
ASP 130
GLU 131
-0.0156
GLU 131
ASN 132
0.0003
ASN 132
GLY 133
-0.0001
GLY 133
GLU 134
-0.0553
GLU 134
HIS 135
-0.0002
HIS 135
LYS 136
-0.0003
LYS 136
ALA 137
-0.1304
ALA 137
TRP 138
0.0001
TRP 138
THR 139
0.0001
THR 139
LYS 140
0.0254
LYS 140
PRO 141
0.0004
PRO 141
GLN 142
0.0001
GLN 142
ALA 143
0.0523
ALA 143
TYR 144
0.0001
TYR 144
LEU 145
0.0000
LEU 145
ALA 146
-0.0495
ALA 146
LEU 147
-0.0000
LEU 147
GLY 148
0.0000
GLY 148
ASN 149
-0.0210
ASN 149
ALA 150
0.0002
ALA 150
LEU 151
0.0002
LEU 151
HIS 152
-0.0222
HIS 152
THR 153
0.0003
THR 153
LEU 154
-0.0002
LEU 154
ALA 155
0.0109
ALA 155
ARG 156
0.0003
ARG 156
LEU 157
-0.0000
LEU 157
ASN 158
-0.0078
ASN 158
ILE 159
-0.0002
ILE 159
ASP 160
0.0002
ASP 160
SER 161
-0.0771
SER 161
THR 162
-0.0003
THR 162
THR 163
0.0001
THR 163
MET 164
-0.0641
MET 164
GLU 165
0.0001
GLU 165
GLY 166
-0.0001
GLY 166
ILE 167
0.0582
ILE 167
ASP 168
-0.0002
ASP 168
PRO 169
-0.0002
PRO 169
GLU 170
-0.0185
GLU 170
LEU 171
0.0003
LEU 171
LEU 172
-0.0001
LEU 172
SER 173
-0.0180
SER 173
GLU 174
-0.0004
GLU 174
ILE 175
-0.0003
ILE 175
PHE 176
-0.0300
PHE 176
ALA 177
-0.0002
ALA 177
ASP 178
0.0004
ASP 178
GLU 179
0.0052
GLU 179
LEU 180
-0.0002
LEU 180
LYS 181
-0.0006
LYS 181
GLY 182
-0.0697
GLY 182
TYR 183
0.0003
TYR 183
GLU 184
-0.0001
GLU 184
CYS 185
-0.0100
CYS 185
HIS 186
0.0000
HIS 186
VAL 187
-0.0003
VAL 187
ALA 188
-0.0034
ALA 188
LEU 189
-0.0002
LEU 189
ALA 190
0.0002
ALA 190
ILE 191
-0.0391
ILE 191
GLY 192
-0.0002
GLY 192
TYR 193
0.0001
TYR 193
HIS 194
0.0717
HIS 194
HIS 195
0.0002
HIS 195
PRO 196
0.0001
PRO 196
SER 197
0.0292
SER 197
GLU 198
0.0002
GLU 198
ASP 199
-0.0002
ASP 199
TYR 200
0.1236
TYR 200
ASN 201
0.0003
ASN 201
ALA 202
0.0001
ALA 202
SER 203
0.0391
SER 203
LEU 204
-0.0001
LEU 204
PRO 205
0.0001
PRO 205
LYS 206
-0.0160
LYS 206
SER 207
-0.0002
SER 207
ARG 208
-0.0001
ARG 208
LYS 209
0.0976
LYS 209
ALA 210
0.0005
ALA 210
PHE 211
0.0000
PHE 211
GLU 212
0.0179
GLU 212
ASP 213
0.0001
ASP 213
VAL 214
0.0001
VAL 214
ILE 215
-0.1243
ILE 215
THR 216
0.0000
THR 216
ILE 217
-0.0001
ILE 217
LEU 218
-0.0930
LEU 218
THR 2
0.0091
THR 2
HIS 3
-0.0000
HIS 3
PRO 4
0.0001
PRO 4
ILE 5
0.0006
ILE 5
ILE 6
-0.0001
ILE 6
HIS 7
0.0003
HIS 7
ASP 8
-0.0194
ASP 8
LEU 9
0.0003
LEU 9
GLU 10
0.0002
GLU 10
ASN 11
-0.0543
ASN 11
ARG 12
0.0001
ARG 12
TYR 13
0.0005
TYR 13
THR 14
-0.0517
THR 14
SER 15
0.0006
SER 15
LYS 16
-0.0001
LYS 16
LYS 17
0.0644
LYS 17
TYR 18
-0.0000
TYR 18
ASP 19
-0.0000
ASP 19
PRO 20
0.0563
PRO 20
SER 21
-0.0002
SER 21
LYS 22
0.0001
LYS 22
LYS 23
0.0175
LYS 23
VAL 24
-0.0002
VAL 24
SER 25
-0.0003
SER 25
GLN 26
0.0151
GLN 26
GLU 27
0.0004
GLU 27
ASP 28
0.0005
ASP 28
LEU 29
0.0213
LEU 29
ALA 30
-0.0002
ALA 30
VAL 31
0.0001
VAL 31
LEU 32
0.0041
LEU 32
LEU 33
0.0001
LEU 33
GLU 34
-0.0002
GLU 34
ALA 35
0.0229
ALA 35
LEU 36
0.0000
LEU 36
ARG 37
0.0001
ARG 37
LEU 38
0.0711
LEU 38
SER 39
0.0002
SER 39
ALA 40
-0.0005
ALA 40
SER 41
-0.0847
SER 41
SER 42
0.0001
SER 42
ILE 43
-0.0002
ILE 43
ASN 44
-0.1908
ASN 44
SER 45
0.0002
SER 45
GLN 46
-0.0000
GLN 46
PRO 47
0.0095
PRO 47
TRP 48
-0.0003
TRP 48
LYS 49
0.0004
LYS 49
PHE 50
-0.0131
PHE 50
ILE 51
0.0001
ILE 51
VAL 52
0.0004
VAL 52
ILE 53
-0.0746
ILE 53
GLU 54
0.0003
GLU 54
SER 55
0.0000
SER 55
ASP 56
-0.0498
ASP 56
ALA 57
-0.0002
ALA 57
ALA 58
-0.0000
ALA 58
LYS 59
0.0099
LYS 59
GLN 60
-0.0000
GLN 60
ARG 61
0.0005
ARG 61
MET 62
-0.0092
MET 62
HIS 63
-0.0001
HIS 63
ASP 64
0.0001
ASP 64
SER 65
0.0276
SER 65
PHE 66
-0.0001
PHE 66
ALA 67
-0.0000
ALA 67
ASN 68
0.0011
ASN 68
MET 69
0.0001
MET 69
HIS 70
-0.0001
HIS 70
GLN 71
-0.0180
GLN 71
PHE 72
0.0004
PHE 72
ASN 73
-0.0004
ASN 73
GLN 74
0.0671
GLN 74
PRO 75
0.0001
PRO 75
HIS 76
0.0004
HIS 76
ILE 77
-0.0242
ILE 77
LYS 78
0.0002
LYS 78
ALA 79
0.0002
ALA 79
CYS 80
-0.0013
CYS 80
SER 81
0.0001
SER 81
HIS 82
0.0000
HIS 82
VAL 83
0.0195
VAL 83
ILE 84
0.0004
ILE 84
LEU 85
-0.0004
LEU 85
PHE 86
0.0018
PHE 86
ALA 87
-0.0001
ALA 87
ASN 88
-0.0002
ASN 88
LYS 89
-0.0269
LYS 89
LEU 90
-0.0002
LEU 90
SER 91
0.0001
SER 91
TYR 92
0.0299
TYR 92
THR 93
0.0001
THR 93
ARG 94
-0.0000
ARG 94
ASP 95
-0.0055
ASP 95
ASP 96
0.0000
ASP 96
TYR 97
-0.0001
TYR 97
ASP 98
0.0042
ASP 98
VAL 99
0.0001
VAL 99
VAL 100
-0.0001
VAL 100
LEU 101
-0.0343
LEU 101
SER 102
0.0005
SER 102
LYS 103
0.0001
LYS 103
ALA 104
0.0731
ALA 104
VAL 105
-0.0004
VAL 105
ALA 106
-0.0001
ALA 106
ASP 107
-0.0320
ASP 107
LYS 108
-0.0003
LYS 108
ARG 109
-0.0001
ARG 109
ILE 110
0.1389
ILE 110
THR 111
-0.0000
THR 111
GLU 112
-0.0003
GLU 112
GLU 113
0.0348
GLU 113
GLN 114
-0.0002
GLN 114
LYS 115
0.0000
LYS 115
GLU 116
-0.1143
GLU 116
ALA 117
-0.0002
ALA 117
ALA 118
0.0000
ALA 118
PHE 119
-0.1786
PHE 119
ALA 120
-0.0000
ALA 120
SER 121
0.0002
SER 121
PHE 122
-0.0776
PHE 122
LYS 123
0.0004
LYS 123
PHE 124
0.0002
PHE 124
VAL 125
0.0132
VAL 125
GLU 126
0.0003
GLU 126
LEU 127
0.0001
LEU 127
ASN 128
0.0712
ASN 128
CYS 129
-0.0001
CYS 129
ASP 130
-0.0001
ASP 130
GLU 131
-0.1379
GLU 131
ASN 132
-0.0001
ASN 132
GLY 133
-0.0002
GLY 133
GLU 134
0.0042
GLU 134
HIS 135
0.0001
HIS 135
LYS 136
0.0002
LYS 136
ALA 137
-0.1026
ALA 137
TRP 138
-0.0002
TRP 138
THR 139
0.0001
THR 139
LYS 140
0.0427
LYS 140
PRO 141
-0.0001
PRO 141
GLN 142
0.0003
GLN 142
ALA 143
0.0544
ALA 143
TYR 144
-0.0000
TYR 144
LEU 145
0.0000
LEU 145
ALA 146
-0.0384
ALA 146
LEU 147
0.0002
LEU 147
GLY 148
0.0004
GLY 148
ASN 149
-0.0209
ASN 149
ALA 150
0.0002
ALA 150
LEU 151
-0.0000
LEU 151
HIS 152
-0.0296
HIS 152
THR 153
-0.0000
THR 153
LEU 154
-0.0000
LEU 154
ALA 155
0.0106
ALA 155
ARG 156
-0.0004
ARG 156
LEU 157
0.0001
LEU 157
ASN 158
-0.0117
ASN 158
ILE 159
0.0002
ILE 159
ASP 160
-0.0005
ASP 160
SER 161
-0.0857
SER 161
THR 162
0.0005
THR 162
THR 163
-0.0000
THR 163
MET 164
-0.0862
MET 164
GLU 165
0.0002
GLU 165
GLY 166
-0.0003
GLY 166
ILE 167
0.0367
ILE 167
ASP 168
0.0002
ASP 168
PRO 169
0.0003
PRO 169
GLU 170
-0.0321
GLU 170
LEU 171
0.0003
LEU 171
LEU 172
0.0001
LEU 172
SER 173
-0.0062
SER 173
GLU 174
0.0001
GLU 174
ILE 175
-0.0002
ILE 175
PHE 176
-0.0174
PHE 176
ALA 177
0.0004
ALA 177
ASP 178
-0.0001
ASP 178
GLU 179
0.0125
GLU 179
LEU 180
-0.0002
LEU 180
LYS 181
0.0001
LYS 181
GLY 182
-0.0268
GLY 182
TYR 183
-0.0003
TYR 183
GLU 184
0.0002
GLU 184
CYS 185
0.0314
CYS 185
HIS 186
0.0002
HIS 186
VAL 187
-0.0001
VAL 187
ALA 188
0.0009
ALA 188
LEU 189
0.0002
LEU 189
ALA 190
0.0000
ALA 190
ILE 191
-0.0362
ILE 191
GLY 192
-0.0002
GLY 192
TYR 193
-0.0001
TYR 193
HIS 194
0.1000
HIS 194
HIS 195
0.0000
HIS 195
PRO 196
0.0003
PRO 196
SER 197
0.0375
SER 197
GLU 198
0.0002
GLU 198
ASP 199
0.0001
ASP 199
TYR 200
0.1095
TYR 200
ASN 201
-0.0000
ASN 201
ALA 202
0.0000
ALA 202
SER 203
0.0705
SER 203
LEU 204
0.0000
LEU 204
PRO 205
-0.0001
PRO 205
LYS 206
-0.0258
LYS 206
SER 207
0.0002
SER 207
ARG 208
0.0002
ARG 208
LYS 209
0.0466
LYS 209
ALA 210
-0.0001
ALA 210
PHE 211
0.0002
PHE 211
GLU 212
-0.0153
GLU 212
ASP 213
0.0001
ASP 213
VAL 214
-0.0003
VAL 214
ILE 215
-0.1833
ILE 215
THR 216
-0.0002
THR 216
ILE 217
-0.0002
ILE 217
LEU 218
-0.1526
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.