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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
-0.0003
HIS 3
PRO 4
0.0002
PRO 4
ILE 5
0.0203
ILE 5
ILE 6
0.0003
ILE 6
HIS 7
0.0003
HIS 7
ASP 8
0.0590
ASP 8
LEU 9
0.0002
LEU 9
GLU 10
-0.0002
GLU 10
ASN 11
0.0160
ASN 11
ARG 12
0.0001
ARG 12
TYR 13
0.0002
TYR 13
THR 14
-0.1037
THR 14
SER 15
0.0001
SER 15
LYS 16
0.0002
LYS 16
LYS 17
-0.0434
LYS 17
TYR 18
-0.0001
TYR 18
ASP 19
0.0003
ASP 19
PRO 20
0.0010
PRO 20
SER 21
0.0001
SER 21
LYS 22
0.0003
LYS 22
LYS 23
-0.1394
LYS 23
VAL 24
-0.0004
VAL 24
SER 25
-0.0002
SER 25
GLN 26
-0.0884
GLN 26
GLU 27
-0.0002
GLU 27
ASP 28
0.0000
ASP 28
LEU 29
0.0270
LEU 29
ALA 30
0.0004
ALA 30
VAL 31
-0.0001
VAL 31
LEU 32
0.0044
LEU 32
LEU 33
0.0002
LEU 33
GLU 34
0.0004
GLU 34
ALA 35
0.0267
ALA 35
LEU 36
-0.0005
LEU 36
ARG 37
-0.0002
ARG 37
LEU 38
0.0941
LEU 38
SER 39
-0.0000
SER 39
ALA 40
-0.0004
ALA 40
SER 41
-0.0140
SER 41
SER 42
-0.0001
SER 42
ILE 43
-0.0001
ILE 43
ASN 44
-0.0756
ASN 44
SER 45
-0.0003
SER 45
GLN 46
-0.0001
GLN 46
PRO 47
0.1063
PRO 47
TRP 48
0.0001
TRP 48
LYS 49
0.0002
LYS 49
PHE 50
-0.0123
PHE 50
ILE 51
0.0001
ILE 51
VAL 52
-0.0001
VAL 52
ILE 53
0.0059
ILE 53
GLU 54
-0.0002
GLU 54
SER 55
0.0002
SER 55
ASP 56
0.0036
ASP 56
ALA 57
0.0000
ALA 57
ALA 58
0.0002
ALA 58
LYS 59
0.0082
LYS 59
GLN 60
0.0001
GLN 60
ARG 61
-0.0003
ARG 61
MET 62
-0.0276
MET 62
HIS 63
0.0002
HIS 63
ASP 64
0.0002
ASP 64
SER 65
-0.0131
SER 65
PHE 66
-0.0003
PHE 66
ALA 67
-0.0002
ALA 67
ASN 68
-0.0609
ASN 68
MET 69
-0.0002
MET 69
HIS 70
0.0000
HIS 70
GLN 71
0.0044
GLN 71
PHE 72
0.0002
PHE 72
ASN 73
-0.0002
ASN 73
GLN 74
0.0106
GLN 74
PRO 75
-0.0002
PRO 75
HIS 76
-0.0001
HIS 76
ILE 77
0.0010
ILE 77
LYS 78
0.0001
LYS 78
ALA 79
0.0004
ALA 79
CYS 80
-0.0027
CYS 80
SER 81
-0.0002
SER 81
HIS 82
0.0000
HIS 82
VAL 83
0.0265
VAL 83
ILE 84
-0.0000
ILE 84
LEU 85
-0.0003
LEU 85
PHE 86
0.0372
PHE 86
ALA 87
-0.0000
ALA 87
ASN 88
-0.0004
ASN 88
LYS 89
0.0692
LYS 89
LEU 90
-0.0000
LEU 90
SER 91
-0.0002
SER 91
TYR 92
0.1054
TYR 92
THR 93
0.0002
THR 93
ARG 94
-0.0004
ARG 94
ASP 95
0.0168
ASP 95
ASP 96
-0.0000
ASP 96
TYR 97
0.0003
TYR 97
ASP 98
0.0400
ASP 98
VAL 99
-0.0001
VAL 99
VAL 100
-0.0001
VAL 100
LEU 101
0.0105
LEU 101
SER 102
-0.0003
SER 102
LYS 103
-0.0002
LYS 103
ALA 104
0.0856
ALA 104
VAL 105
-0.0002
VAL 105
ALA 106
-0.0000
ALA 106
ASP 107
-0.0419
ASP 107
LYS 108
0.0000
LYS 108
ARG 109
-0.0002
ARG 109
ILE 110
-0.0444
ILE 110
THR 111
-0.0002
THR 111
GLU 112
0.0001
GLU 112
GLU 113
-0.0386
GLU 113
GLN 114
0.0001
GLN 114
LYS 115
-0.0001
LYS 115
GLU 116
0.0263
GLU 116
ALA 117
0.0001
ALA 117
ALA 118
-0.0004
ALA 118
PHE 119
0.0891
PHE 119
ALA 120
-0.0002
ALA 120
SER 121
0.0001
SER 121
PHE 122
0.0843
PHE 122
LYS 123
0.0000
LYS 123
PHE 124
0.0002
PHE 124
VAL 125
0.0030
VAL 125
GLU 126
-0.0006
GLU 126
LEU 127
-0.0001
LEU 127
ASN 128
-0.0308
ASN 128
CYS 129
0.0001
CYS 129
ASP 130
-0.0000
ASP 130
GLU 131
0.0087
GLU 131
ASN 132
-0.0000
ASN 132
GLY 133
0.0001
GLY 133
GLU 134
0.0035
GLU 134
HIS 135
-0.0003
HIS 135
LYS 136
-0.0001
LYS 136
ALA 137
-0.0683
ALA 137
TRP 138
0.0001
TRP 138
THR 139
0.0000
THR 139
LYS 140
0.0315
LYS 140
PRO 141
-0.0001
PRO 141
GLN 142
0.0003
GLN 142
ALA 143
-0.0062
ALA 143
TYR 144
0.0000
TYR 144
LEU 145
-0.0003
LEU 145
ALA 146
-0.0397
ALA 146
LEU 147
-0.0001
LEU 147
GLY 148
-0.0000
GLY 148
ASN 149
-0.0112
ASN 149
ALA 150
0.0003
ALA 150
LEU 151
0.0003
LEU 151
HIS 152
-0.0367
HIS 152
THR 153
0.0001
THR 153
LEU 154
-0.0002
LEU 154
ALA 155
0.0090
ALA 155
ARG 156
0.0000
ARG 156
LEU 157
-0.0002
LEU 157
ASN 158
-0.2654
ASN 158
ILE 159
-0.0000
ILE 159
ASP 160
-0.0002
ASP 160
SER 161
-0.0414
SER 161
THR 162
0.0002
THR 162
THR 163
0.0003
THR 163
MET 164
-0.0942
MET 164
GLU 165
0.0002
GLU 165
GLY 166
-0.0001
GLY 166
ILE 167
-0.1492
ILE 167
ASP 168
-0.0000
ASP 168
PRO 169
0.0002
PRO 169
GLU 170
-0.0593
GLU 170
LEU 171
0.0001
LEU 171
LEU 172
-0.0000
LEU 172
SER 173
0.0157
SER 173
GLU 174
-0.0001
GLU 174
ILE 175
0.0001
ILE 175
PHE 176
0.0347
PHE 176
ALA 177
-0.0004
ALA 177
ASP 178
0.0002
ASP 178
GLU 179
0.0328
GLU 179
LEU 180
0.0001
LEU 180
LYS 181
-0.0001
LYS 181
GLY 182
0.0342
GLY 182
TYR 183
0.0002
TYR 183
GLU 184
0.0000
GLU 184
CYS 185
0.1296
CYS 185
HIS 186
-0.0005
HIS 186
VAL 187
0.0002
VAL 187
ALA 188
0.0883
ALA 188
LEU 189
0.0002
LEU 189
ALA 190
0.0001
ALA 190
ILE 191
0.0390
ILE 191
GLY 192
0.0001
GLY 192
TYR 193
0.0002
TYR 193
HIS 194
-0.0538
HIS 194
HIS 195
0.0003
HIS 195
PRO 196
0.0001
PRO 196
SER 197
-0.0535
SER 197
GLU 198
0.0001
GLU 198
ASP 199
0.0001
ASP 199
TYR 200
0.0602
TYR 200
ASN 201
-0.0001
ASN 201
ALA 202
0.0001
ALA 202
SER 203
0.0633
SER 203
LEU 204
-0.0001
LEU 204
PRO 205
0.0000
PRO 205
LYS 206
-0.0274
LYS 206
SER 207
-0.0000
SER 207
ARG 208
-0.0002
ARG 208
LYS 209
0.2412
LYS 209
ALA 210
0.0002
ALA 210
PHE 211
-0.0004
PHE 211
GLU 212
0.0762
GLU 212
ASP 213
0.0004
ASP 213
VAL 214
0.0001
VAL 214
ILE 215
-0.0223
ILE 215
THR 216
-0.0002
THR 216
ILE 217
0.0001
ILE 217
LEU 218
0.0726
LEU 218
THR 2
0.0487
THR 2
HIS 3
0.0001
HIS 3
PRO 4
-0.0004
PRO 4
ILE 5
0.0207
ILE 5
ILE 6
-0.0000
ILE 6
HIS 7
-0.0003
HIS 7
ASP 8
0.0544
ASP 8
LEU 9
-0.0003
LEU 9
GLU 10
-0.0001
GLU 10
ASN 11
0.0031
ASN 11
ARG 12
0.0004
ARG 12
TYR 13
0.0001
TYR 13
THR 14
-0.1075
THR 14
SER 15
-0.0001
SER 15
LYS 16
-0.0003
LYS 16
LYS 17
-0.0463
LYS 17
TYR 18
0.0000
TYR 18
ASP 19
-0.0002
ASP 19
PRO 20
-0.0037
PRO 20
SER 21
-0.0004
SER 21
LYS 22
0.0001
LYS 22
LYS 23
-0.1541
LYS 23
VAL 24
-0.0004
VAL 24
SER 25
0.0001
SER 25
GLN 26
-0.0986
GLN 26
GLU 27
0.0002
GLU 27
ASP 28
0.0001
ASP 28
LEU 29
0.0301
LEU 29
ALA 30
0.0001
ALA 30
VAL 31
0.0000
VAL 31
LEU 32
0.0100
LEU 32
LEU 33
-0.0003
LEU 33
GLU 34
0.0002
GLU 34
ALA 35
0.0378
ALA 35
LEU 36
-0.0004
LEU 36
ARG 37
0.0001
ARG 37
LEU 38
0.1101
LEU 38
SER 39
0.0002
SER 39
ALA 40
0.0001
ALA 40
SER 41
-0.0397
SER 41
SER 42
-0.0000
SER 42
ILE 43
-0.0002
ILE 43
ASN 44
-0.0757
ASN 44
SER 45
-0.0003
SER 45
GLN 46
0.0000
GLN 46
PRO 47
0.1137
PRO 47
TRP 48
0.0004
TRP 48
LYS 49
-0.0001
LYS 49
PHE 50
-0.0130
PHE 50
ILE 51
-0.0002
ILE 51
VAL 52
-0.0003
VAL 52
ILE 53
0.0028
ILE 53
GLU 54
0.0004
GLU 54
SER 55
0.0002
SER 55
ASP 56
0.0063
ASP 56
ALA 57
-0.0002
ALA 57
ALA 58
-0.0000
ALA 58
LYS 59
0.0047
LYS 59
GLN 60
0.0000
GLN 60
ARG 61
0.0001
ARG 61
MET 62
-0.0301
MET 62
HIS 63
-0.0000
HIS 63
ASP 64
-0.0001
ASP 64
SER 65
-0.0151
SER 65
PHE 66
-0.0000
PHE 66
ALA 67
-0.0002
ALA 67
ASN 68
-0.0618
ASN 68
MET 69
-0.0001
MET 69
HIS 70
0.0000
HIS 70
GLN 71
0.0171
GLN 71
PHE 72
-0.0003
PHE 72
ASN 73
0.0002
ASN 73
GLN 74
0.0262
GLN 74
PRO 75
0.0002
PRO 75
HIS 76
0.0002
HIS 76
ILE 77
-0.0000
ILE 77
LYS 78
0.0001
LYS 78
ALA 79
-0.0002
ALA 79
CYS 80
-0.0036
CYS 80
SER 81
0.0005
SER 81
HIS 82
-0.0001
HIS 82
VAL 83
0.0339
VAL 83
ILE 84
0.0000
ILE 84
LEU 85
-0.0003
LEU 85
PHE 86
0.0483
PHE 86
ALA 87
-0.0000
ALA 87
ASN 88
-0.0000
ASN 88
LYS 89
0.0727
LYS 89
LEU 90
0.0004
LEU 90
SER 91
-0.0000
SER 91
TYR 92
0.1241
TYR 92
THR 93
-0.0000
THR 93
ARG 94
0.0003
ARG 94
ASP 95
0.0157
ASP 95
ASP 96
0.0001
ASP 96
TYR 97
-0.0002
TYR 97
ASP 98
0.0542
ASP 98
VAL 99
0.0003
VAL 99
VAL 100
-0.0004
VAL 100
LEU 101
0.0090
LEU 101
SER 102
-0.0004
SER 102
LYS 103
-0.0004
LYS 103
ALA 104
0.0762
ALA 104
VAL 105
-0.0004
VAL 105
ALA 106
0.0004
ALA 106
ASP 107
-0.0346
ASP 107
LYS 108
-0.0002
LYS 108
ARG 109
-0.0002
ARG 109
ILE 110
-0.0224
ILE 110
THR 111
0.0001
THR 111
GLU 112
-0.0002
GLU 112
GLU 113
-0.0296
GLU 113
GLN 114
0.0003
GLN 114
LYS 115
-0.0000
LYS 115
GLU 116
0.0066
GLU 116
ALA 117
-0.0002
ALA 117
ALA 118
-0.0000
ALA 118
PHE 119
0.0792
PHE 119
ALA 120
0.0005
ALA 120
SER 121
-0.0001
SER 121
PHE 122
0.1114
PHE 122
LYS 123
0.0001
LYS 123
PHE 124
-0.0002
PHE 124
VAL 125
-0.0041
VAL 125
GLU 126
-0.0006
GLU 126
LEU 127
0.0001
LEU 127
ASN 128
-0.0273
ASN 128
CYS 129
0.0001
CYS 129
ASP 130
0.0003
ASP 130
GLU 131
-0.0323
GLU 131
ASN 132
0.0001
ASN 132
GLY 133
-0.0000
GLY 133
GLU 134
0.0190
GLU 134
HIS 135
-0.0000
HIS 135
LYS 136
0.0003
LYS 136
ALA 137
-0.0626
ALA 137
TRP 138
-0.0002
TRP 138
THR 139
0.0002
THR 139
LYS 140
0.0366
LYS 140
PRO 141
-0.0003
PRO 141
GLN 142
-0.0000
GLN 142
ALA 143
-0.0041
ALA 143
TYR 144
-0.0001
TYR 144
LEU 145
-0.0003
LEU 145
ALA 146
-0.0348
ALA 146
LEU 147
-0.0002
LEU 147
GLY 148
-0.0002
GLY 148
ASN 149
-0.0078
ASN 149
ALA 150
-0.0006
ALA 150
LEU 151
0.0001
LEU 151
HIS 152
-0.0352
HIS 152
THR 153
-0.0001
THR 153
LEU 154
-0.0000
LEU 154
ALA 155
0.0001
ALA 155
ARG 156
0.0001
ARG 156
LEU 157
-0.0001
LEU 157
ASN 158
-0.2817
ASN 158
ILE 159
0.0003
ILE 159
ASP 160
0.0001
ASP 160
SER 161
-0.0276
SER 161
THR 162
-0.0001
THR 162
THR 163
0.0000
THR 163
MET 164
-0.0865
MET 164
GLU 165
0.0003
GLU 165
GLY 166
0.0002
GLY 166
ILE 167
-0.1729
ILE 167
ASP 168
0.0000
ASP 168
PRO 169
-0.0002
PRO 169
GLU 170
-0.0764
GLU 170
LEU 171
-0.0001
LEU 171
LEU 172
0.0002
LEU 172
SER 173
0.0261
SER 173
GLU 174
0.0001
GLU 174
ILE 175
-0.0005
ILE 175
PHE 176
0.0320
PHE 176
ALA 177
-0.0003
ALA 177
ASP 178
-0.0003
ASP 178
GLU 179
0.0493
GLU 179
LEU 180
-0.0002
LEU 180
LYS 181
-0.0000
LYS 181
GLY 182
0.0256
GLY 182
TYR 183
0.0001
TYR 183
GLU 184
0.0001
GLU 184
CYS 185
0.1437
CYS 185
HIS 186
-0.0001
HIS 186
VAL 187
0.0000
VAL 187
ALA 188
0.1075
ALA 188
LEU 189
0.0001
LEU 189
ALA 190
-0.0003
ALA 190
ILE 191
0.0567
ILE 191
GLY 192
-0.0001
GLY 192
TYR 193
0.0001
TYR 193
HIS 194
-0.0602
HIS 194
HIS 195
0.0003
HIS 195
PRO 196
0.0000
PRO 196
SER 197
-0.0528
SER 197
GLU 198
-0.0000
GLU 198
ASP 199
0.0002
ASP 199
TYR 200
0.0607
TYR 200
ASN 201
-0.0002
ASN 201
ALA 202
-0.0002
ALA 202
SER 203
0.0860
SER 203
LEU 204
0.0001
LEU 204
PRO 205
-0.0004
PRO 205
LYS 206
-0.0306
LYS 206
SER 207
0.0001
SER 207
ARG 208
0.0002
ARG 208
LYS 209
0.2066
LYS 209
ALA 210
-0.0002
ALA 210
PHE 211
0.0002
PHE 211
GLU 212
0.0700
GLU 212
ASP 213
0.0001
ASP 213
VAL 214
0.0000
VAL 214
ILE 215
-0.0167
ILE 215
THR 216
0.0001
THR 216
ILE 217
-0.0001
ILE 217
LEU 218
0.0790
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.