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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
-0.0001
PRO 4
ILE 5
-0.0106
ILE 5
ILE 6
-0.0001
ILE 6
HIS 7
-0.0001
HIS 7
ASP 8
0.0353
ASP 8
LEU 9
-0.0005
LEU 9
GLU 10
-0.0000
GLU 10
ASN 11
0.1790
ASN 11
ARG 12
-0.0000
ARG 12
TYR 13
-0.0000
TYR 13
THR 14
0.0559
THR 14
SER 15
-0.0001
SER 15
LYS 16
-0.0002
LYS 16
LYS 17
0.0409
LYS 17
TYR 18
-0.0002
TYR 18
ASP 19
0.0003
ASP 19
PRO 20
-0.0014
PRO 20
SER 21
-0.0002
SER 21
LYS 22
-0.0002
LYS 22
LYS 23
-0.0179
LYS 23
VAL 24
-0.0001
VAL 24
SER 25
-0.0003
SER 25
GLN 26
-0.0121
GLN 26
GLU 27
-0.0002
GLU 27
ASP 28
-0.0004
ASP 28
LEU 29
0.0385
LEU 29
ALA 30
0.0002
ALA 30
VAL 31
-0.0003
VAL 31
LEU 32
-0.0087
LEU 32
LEU 33
0.0001
LEU 33
GLU 34
0.0002
GLU 34
ALA 35
-0.0285
ALA 35
LEU 36
0.0004
LEU 36
ARG 37
0.0000
ARG 37
LEU 38
-0.0578
LEU 38
SER 39
0.0000
SER 39
ALA 40
-0.0002
ALA 40
SER 41
0.0782
SER 41
SER 42
-0.0001
SER 42
ILE 43
-0.0002
ILE 43
ASN 44
-0.0702
ASN 44
SER 45
0.0003
SER 45
GLN 46
-0.0001
GLN 46
PRO 47
-0.1138
PRO 47
TRP 48
0.0000
TRP 48
LYS 49
0.0001
LYS 49
PHE 50
-0.0375
PHE 50
ILE 51
0.0002
ILE 51
VAL 52
0.0002
VAL 52
ILE 53
-0.1056
ILE 53
GLU 54
-0.0001
GLU 54
SER 55
0.0002
SER 55
ASP 56
-0.0359
ASP 56
ALA 57
-0.0003
ALA 57
ALA 58
-0.0003
ALA 58
LYS 59
-0.0087
LYS 59
GLN 60
-0.0002
GLN 60
ARG 61
0.0000
ARG 61
MET 62
0.0369
MET 62
HIS 63
0.0000
HIS 63
ASP 64
-0.0001
ASP 64
SER 65
0.0156
SER 65
PHE 66
-0.0002
PHE 66
ALA 67
-0.0002
ALA 67
ASN 68
0.0553
ASN 68
MET 69
-0.0002
MET 69
HIS 70
0.0001
HIS 70
GLN 71
0.0045
GLN 71
PHE 72
0.0002
PHE 72
ASN 73
0.0001
ASN 73
GLN 74
0.0002
GLN 74
PRO 75
-0.0000
PRO 75
HIS 76
0.0001
HIS 76
ILE 77
0.0240
ILE 77
LYS 78
-0.0003
LYS 78
ALA 79
0.0003
ALA 79
CYS 80
-0.0140
CYS 80
SER 81
0.0000
SER 81
HIS 82
-0.0001
HIS 82
VAL 83
-0.0204
VAL 83
ILE 84
0.0002
ILE 84
LEU 85
-0.0001
LEU 85
PHE 86
-0.0463
PHE 86
ALA 87
0.0001
ALA 87
ASN 88
0.0001
ASN 88
LYS 89
-0.0906
LYS 89
LEU 90
0.0002
LEU 90
SER 91
0.0005
SER 91
TYR 92
-0.0724
TYR 92
THR 93
0.0001
THR 93
ARG 94
-0.0001
ARG 94
ASP 95
-0.0142
ASP 95
ASP 96
-0.0002
ASP 96
TYR 97
-0.0001
TYR 97
ASP 98
-0.0359
ASP 98
VAL 99
0.0002
VAL 99
VAL 100
0.0001
VAL 100
LEU 101
-0.0749
LEU 101
SER 102
0.0001
SER 102
LYS 103
0.0002
LYS 103
ALA 104
-0.0590
ALA 104
VAL 105
0.0001
VAL 105
ALA 106
-0.0000
ALA 106
ASP 107
-0.0616
ASP 107
LYS 108
-0.0005
LYS 108
ARG 109
-0.0002
ARG 109
ILE 110
0.1644
ILE 110
THR 111
0.0001
THR 111
GLU 112
0.0001
GLU 112
GLU 113
0.0132
GLU 113
GLN 114
0.0002
GLN 114
LYS 115
-0.0001
LYS 115
GLU 116
0.0011
GLU 116
ALA 117
0.0002
ALA 117
ALA 118
0.0001
ALA 118
PHE 119
-0.0341
PHE 119
ALA 120
0.0001
ALA 120
SER 121
0.0000
SER 121
PHE 122
-0.0047
PHE 122
LYS 123
0.0002
LYS 123
PHE 124
-0.0001
PHE 124
VAL 125
-0.0738
VAL 125
GLU 126
-0.0002
GLU 126
LEU 127
0.0000
LEU 127
ASN 128
0.0180
ASN 128
CYS 129
-0.0004
CYS 129
ASP 130
0.0002
ASP 130
GLU 131
-0.1102
GLU 131
ASN 132
0.0001
ASN 132
GLY 133
-0.0004
GLY 133
GLU 134
-0.0788
GLU 134
HIS 135
-0.0002
HIS 135
LYS 136
-0.0003
LYS 136
ALA 137
-0.0018
ALA 137
TRP 138
0.0000
TRP 138
THR 139
0.0003
THR 139
LYS 140
-0.0463
LYS 140
PRO 141
0.0000
PRO 141
GLN 142
0.0001
GLN 142
ALA 143
-0.0071
ALA 143
TYR 144
0.0002
TYR 144
LEU 145
-0.0001
LEU 145
ALA 146
-0.0184
ALA 146
LEU 147
-0.0000
LEU 147
GLY 148
0.0000
GLY 148
ASN 149
0.0141
ASN 149
ALA 150
0.0001
ALA 150
LEU 151
-0.0001
LEU 151
HIS 152
0.0165
HIS 152
THR 153
-0.0002
THR 153
LEU 154
0.0001
LEU 154
ALA 155
0.0101
ALA 155
ARG 156
-0.0001
ARG 156
LEU 157
-0.0003
LEU 157
ASN 158
-0.0046
ASN 158
ILE 159
-0.0004
ILE 159
ASP 160
0.0002
ASP 160
SER 161
0.0081
SER 161
THR 162
-0.0002
THR 162
THR 163
0.0000
THR 163
MET 164
0.0459
MET 164
GLU 165
0.0004
GLU 165
GLY 166
-0.0000
GLY 166
ILE 167
0.1300
ILE 167
ASP 168
0.0000
ASP 168
PRO 169
-0.0005
PRO 169
GLU 170
0.0428
GLU 170
LEU 171
0.0000
LEU 171
LEU 172
-0.0002
LEU 172
SER 173
-0.0288
SER 173
GLU 174
0.0002
GLU 174
ILE 175
0.0001
ILE 175
PHE 176
-0.0415
PHE 176
ALA 177
0.0001
ALA 177
ASP 178
0.0002
ASP 178
GLU 179
-0.0172
GLU 179
LEU 180
-0.0001
LEU 180
LYS 181
0.0001
LYS 181
GLY 182
-0.1488
GLY 182
TYR 183
0.0001
TYR 183
GLU 184
0.0003
GLU 184
CYS 185
-0.1853
CYS 185
HIS 186
-0.0002
HIS 186
VAL 187
-0.0002
VAL 187
ALA 188
-0.0515
ALA 188
LEU 189
-0.0002
LEU 189
ALA 190
-0.0001
ALA 190
ILE 191
-0.0279
ILE 191
GLY 192
-0.0002
GLY 192
TYR 193
0.0005
TYR 193
HIS 194
-0.0655
HIS 194
HIS 195
0.0001
HIS 195
PRO 196
0.0000
PRO 196
SER 197
-0.0184
SER 197
GLU 198
-0.0000
GLU 198
ASP 199
0.0002
ASP 199
TYR 200
-0.0403
TYR 200
ASN 201
-0.0005
ASN 201
ALA 202
-0.0001
ALA 202
SER 203
-0.1435
SER 203
LEU 204
0.0001
LEU 204
PRO 205
0.0001
PRO 205
LYS 206
0.0796
LYS 206
SER 207
-0.0002
SER 207
ARG 208
0.0001
ARG 208
LYS 209
0.2229
LYS 209
ALA 210
-0.0003
ALA 210
PHE 211
-0.0001
PHE 211
GLU 212
0.0652
GLU 212
ASP 213
-0.0000
ASP 213
VAL 214
0.0003
VAL 214
ILE 215
0.1839
ILE 215
THR 216
-0.0003
THR 216
ILE 217
-0.0001
ILE 217
LEU 218
0.1889
LEU 218
THR 2
-0.0462
THR 2
HIS 3
0.0001
HIS 3
PRO 4
-0.0003
PRO 4
ILE 5
0.0122
ILE 5
ILE 6
0.0000
ILE 6
HIS 7
0.0001
HIS 7
ASP 8
-0.0387
ASP 8
LEU 9
0.0000
LEU 9
GLU 10
0.0003
GLU 10
ASN 11
-0.1800
ASN 11
ARG 12
0.0002
ARG 12
TYR 13
-0.0003
TYR 13
THR 14
-0.0382
THR 14
SER 15
-0.0003
SER 15
LYS 16
-0.0003
LYS 16
LYS 17
-0.0538
LYS 17
TYR 18
0.0000
TYR 18
ASP 19
-0.0004
ASP 19
PRO 20
-0.0152
PRO 20
SER 21
-0.0002
SER 21
LYS 22
0.0002
LYS 22
LYS 23
0.0143
LYS 23
VAL 24
-0.0001
VAL 24
SER 25
-0.0001
SER 25
GLN 26
0.0119
GLN 26
GLU 27
0.0003
GLU 27
ASP 28
0.0001
ASP 28
LEU 29
-0.0490
LEU 29
ALA 30
0.0004
ALA 30
VAL 31
-0.0002
VAL 31
LEU 32
0.0086
LEU 32
LEU 33
0.0003
LEU 33
GLU 34
0.0002
GLU 34
ALA 35
0.0236
ALA 35
LEU 36
-0.0002
LEU 36
ARG 37
-0.0001
ARG 37
LEU 38
0.0369
LEU 38
SER 39
0.0003
SER 39
ALA 40
0.0000
ALA 40
SER 41
-0.0614
SER 41
SER 42
-0.0001
SER 42
ILE 43
0.0002
ILE 43
ASN 44
0.1360
ASN 44
SER 45
0.0001
SER 45
GLN 46
-0.0005
GLN 46
PRO 47
0.1136
PRO 47
TRP 48
0.0005
TRP 48
LYS 49
-0.0004
LYS 49
PHE 50
0.0404
PHE 50
ILE 51
0.0004
ILE 51
VAL 52
0.0001
VAL 52
ILE 53
0.1254
ILE 53
GLU 54
0.0003
GLU 54
SER 55
0.0000
SER 55
ASP 56
0.0465
ASP 56
ALA 57
-0.0003
ALA 57
ALA 58
-0.0002
ALA 58
LYS 59
0.0039
LYS 59
GLN 60
0.0001
GLN 60
ARG 61
-0.0003
ARG 61
MET 62
-0.0300
MET 62
HIS 63
0.0001
HIS 63
ASP 64
0.0004
ASP 64
SER 65
-0.0192
SER 65
PHE 66
-0.0001
PHE 66
ALA 67
-0.0005
ALA 67
ASN 68
-0.0495
ASN 68
MET 69
0.0001
MET 69
HIS 70
-0.0001
HIS 70
GLN 71
0.0053
GLN 71
PHE 72
-0.0005
PHE 72
ASN 73
-0.0001
ASN 73
GLN 74
-0.0049
GLN 74
PRO 75
0.0001
PRO 75
HIS 76
-0.0001
HIS 76
ILE 77
-0.0171
ILE 77
LYS 78
0.0003
LYS 78
ALA 79
-0.0001
ALA 79
CYS 80
0.0128
CYS 80
SER 81
-0.0001
SER 81
HIS 82
0.0001
HIS 82
VAL 83
0.0172
VAL 83
ILE 84
-0.0004
ILE 84
LEU 85
0.0001
LEU 85
PHE 86
0.0500
PHE 86
ALA 87
0.0003
ALA 87
ASN 88
-0.0001
ASN 88
LYS 89
0.0941
LYS 89
LEU 90
0.0004
LEU 90
SER 91
-0.0001
SER 91
TYR 92
0.0601
TYR 92
THR 93
0.0002
THR 93
ARG 94
-0.0002
ARG 94
ASP 95
0.0087
ASP 95
ASP 96
0.0002
ASP 96
TYR 97
0.0004
TYR 97
ASP 98
0.0299
ASP 98
VAL 99
-0.0004
VAL 99
VAL 100
-0.0001
VAL 100
LEU 101
0.0915
LEU 101
SER 102
0.0002
SER 102
LYS 103
0.0000
LYS 103
ALA 104
0.0396
ALA 104
VAL 105
0.0001
VAL 105
ALA 106
-0.0000
ALA 106
ASP 107
0.0499
ASP 107
LYS 108
0.0001
LYS 108
ARG 109
0.0003
ARG 109
ILE 110
-0.2127
ILE 110
THR 111
-0.0001
THR 111
GLU 112
0.0002
GLU 112
GLU 113
-0.0139
GLU 113
GLN 114
0.0001
GLN 114
LYS 115
-0.0001
LYS 115
GLU 116
0.0215
GLU 116
ALA 117
0.0003
ALA 117
ALA 118
0.0004
ALA 118
PHE 119
0.0772
PHE 119
ALA 120
-0.0000
ALA 120
SER 121
0.0001
SER 121
PHE 122
0.0104
PHE 122
LYS 123
-0.0001
LYS 123
PHE 124
0.0001
PHE 124
VAL 125
0.0854
VAL 125
GLU 126
-0.0000
GLU 126
LEU 127
-0.0001
LEU 127
ASN 128
-0.0393
ASN 128
CYS 129
-0.0000
CYS 129
ASP 130
0.0003
ASP 130
GLU 131
0.1279
GLU 131
ASN 132
0.0000
ASN 132
GLY 133
-0.0001
GLY 133
GLU 134
0.0531
GLU 134
HIS 135
0.0002
HIS 135
LYS 136
0.0001
LYS 136
ALA 137
0.0399
ALA 137
TRP 138
0.0006
TRP 138
THR 139
0.0002
THR 139
LYS 140
0.0378
LYS 140
PRO 141
0.0003
PRO 141
GLN 142
-0.0001
GLN 142
ALA 143
-0.0044
ALA 143
TYR 144
0.0002
TYR 144
LEU 145
-0.0002
LEU 145
ALA 146
0.0333
ALA 146
LEU 147
0.0001
LEU 147
GLY 148
-0.0001
GLY 148
ASN 149
-0.0057
ASN 149
ALA 150
0.0001
ALA 150
LEU 151
0.0001
LEU 151
HIS 152
-0.0103
HIS 152
THR 153
-0.0000
THR 153
LEU 154
0.0002
LEU 154
ALA 155
-0.0180
ALA 155
ARG 156
0.0003
ARG 156
LEU 157
0.0003
LEU 157
ASN 158
0.0172
ASN 158
ILE 159
0.0001
ILE 159
ASP 160
-0.0003
ASP 160
SER 161
0.0200
SER 161
THR 162
-0.0001
THR 162
THR 163
0.0003
THR 163
MET 164
-0.0197
MET 164
GLU 165
-0.0003
GLU 165
GLY 166
0.0000
GLY 166
ILE 167
-0.1203
ILE 167
ASP 168
0.0000
ASP 168
PRO 169
0.0003
PRO 169
GLU 170
-0.0415
GLU 170
LEU 171
-0.0000
LEU 171
LEU 172
0.0001
LEU 172
SER 173
0.0379
SER 173
GLU 174
0.0000
GLU 174
ILE 175
0.0000
ILE 175
PHE 176
0.0387
PHE 176
ALA 177
0.0003
ALA 177
ASP 178
-0.0002
ASP 178
GLU 179
0.0246
GLU 179
LEU 180
0.0002
LEU 180
LYS 181
0.0001
LYS 181
GLY 182
0.1397
GLY 182
TYR 183
-0.0003
TYR 183
GLU 184
-0.0005
GLU 184
CYS 185
0.1755
CYS 185
HIS 186
0.0002
HIS 186
VAL 187
0.0001
VAL 187
ALA 188
0.0528
ALA 188
LEU 189
0.0001
LEU 189
ALA 190
-0.0003
ALA 190
ILE 191
0.0417
ILE 191
GLY 192
-0.0001
GLY 192
TYR 193
-0.0000
TYR 193
HIS 194
0.0438
HIS 194
HIS 195
-0.0000
HIS 195
PRO 196
-0.0002
PRO 196
SER 197
0.0155
SER 197
GLU 198
-0.0001
GLU 198
ASP 199
0.0002
ASP 199
TYR 200
0.0061
TYR 200
ASN 201
0.0003
ASN 201
ALA 202
-0.0001
ALA 202
SER 203
0.1213
SER 203
LEU 204
-0.0000
LEU 204
PRO 205
0.0000
PRO 205
LYS 206
-0.0788
LYS 206
SER 207
-0.0000
SER 207
ARG 208
0.0004
ARG 208
LYS 209
-0.2230
LYS 209
ALA 210
0.0001
ALA 210
PHE 211
-0.0004
PHE 211
GLU 212
-0.0734
GLU 212
ASP 213
0.0001
ASP 213
VAL 214
-0.0001
VAL 214
ILE 215
-0.1446
ILE 215
THR 216
0.0003
THR 216
ILE 217
0.0002
ILE 217
LEU 218
-0.1741
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.