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
MET 1
LYS 2
0.0002
LYS 2
ASN 3
0.0003
ASN 3
GLY 4
0.0856
GLY 4
PHE 5
0.0003
PHE 5
TYR 6
-0.0002
TYR 6
ALA 7
0.0035
ALA 7
THR 8
0.0002
THR 8
TYR 9
-0.0001
TYR 9
ARG 10
0.0007
ARG 10
SER 11
-0.0001
SER 11
LYS 12
-0.0002
LYS 12
ASN 13
0.0106
ASN 13
LYS 14
0.0004
LYS 14
GLY 15
-0.0001
GLY 15
LYS 16
0.0226
LYS 16
ASP 17
-0.0003
ASP 17
LYS 18
0.0002
LYS 18
ARG 19
-0.0782
ARG 19
SER 20
-0.0002
SER 20
ILE 21
-0.0000
ILE 21
ASN 22
-0.0299
ASN 22
LEU 23
-0.0001
LEU 23
SER 24
-0.0003
SER 24
VAL 25
0.0903
VAL 25
PHE 26
-0.0004
PHE 26
LEU 27
0.0002
LEU 27
ASN 28
-0.0006
ASN 28
SER 29
-0.0001
SER 29
LEU 30
-0.0005
LEU 30
ASN 34
-0.0247
ASN 34
HIS 35
0.0001
HIS 35
HIS 36
0.0001
HIS 36
LEU 37
0.0242
LEU 37
GLN 38
-0.0000
GLN 38
VAL 39
0.0002
VAL 39
GLY 40
0.0432
GLY 40
SER 41
-0.0001
SER 41
ASN 42
-0.0000
ASN 42
TYR 43
0.0155
TYR 43
LEU 44
-0.0001
LEU 44
TYR 45
-0.0001
TYR 45
ILE 46
0.0565
ILE 46
HIS 47
0.0000
HIS 47
LYS 48
0.0002
LYS 48
ILE 49
0.0562
ILE 49
ASP 50
0.0000
ASP 50
GLY 51
0.0002
GLY 51
LYS 52
-0.1091
LYS 52
THR 53
0.0002
THR 53
PHE 54
-0.0003
PHE 54
LEU 55
-0.0245
LEU 55
PHE 56
-0.0000
PHE 56
THR 57
-0.0004
THR 57
LYS 58
-0.0133
LYS 58
THR 59
-0.0000
THR 59
ASN 60
0.0000
ASN 60
ASP 61
-0.0020
ASP 61
LYS 62
0.0002
LYS 62
SER 63
-0.0000
SER 63
LEU 64
-0.0203
LEU 64
VAL 65
0.0001
VAL 65
GLN 66
-0.0000
GLN 66
LYS 67
0.0056
LYS 67
ILE 68
0.0002
ILE 68
ASN 69
0.0000
ASN 69
ARG 70
-0.0076
ARG 70
SER 71
0.0002
SER 71
LYS 72
-0.0001
LYS 72
ALA 73
0.0324
ALA 73
SER 74
-0.0001
SER 74
VAL 75
-0.0000
VAL 75
GLU 76
-0.0165
GLU 76
ASP 77
-0.0005
ASP 77
ILE 78
0.0002
ILE 78
LYS 79
0.0218
LYS 79
ASN 80
-0.0003
ASN 80
SER 81
0.0003
SER 81
LEU 82
0.0264
LEU 82
ALA 83
0.0003
ALA 83
ASP 84
-0.0002
ASP 84
ASP 85
-0.0569
ASP 85
GLU 86
0.0000
GLU 86
SER 87
0.0002
SER 87
LEU 88
-0.0105
LEU 88
GLY 89
0.0003
GLY 89
PHE 90
-0.0001
PHE 90
PRO 91
-0.0489
PRO 91
SER 92
0.0002
SER 92
PHE 93
-0.0000
PHE 93
LEU 94
-0.0010
LEU 94
PHE 95
0.0004
PHE 95
VAL 96
-0.0002
VAL 96
GLU 97
-0.0294
GLU 97
GLY 98
0.0003
GLY 98
ASP 99
-0.0001
ASP 99
THR 100
0.1199
THR 100
ILE 101
0.0004
ILE 101
GLY 102
0.0003
GLY 102
PHE 103
0.0444
PHE 103
ALA 104
-0.0002
ALA 104
ARG 105
0.0001
ARG 105
THR 106
0.0502
THR 106
VAL 107
-0.0000
VAL 107
PHE 108
0.0001
PHE 108
GLY 109
0.0382
GLY 109
PRO 110
-0.0001
PRO 110
THR 111
0.0000
THR 111
THR 112
0.1212
THR 112
SER 113
0.0000
SER 113
ASP 114
-0.0002
ASP 114
LEU 115
0.0272
LEU 115
THR 116
-0.0001
THR 116
ASP 117
-0.0003
ASP 117
PHE 118
-0.0141
PHE 118
LEU 119
-0.0001
LEU 119
ILE 120
-0.0003
ILE 120
GLY 121
0.0351
GLY 121
LYS 122
-0.0002
LYS 122
GLY 123
0.0001
GLY 123
MET 124
-0.0014
MET 124
SER 125
0.0001
SER 125
LEU 126
-0.0003
LEU 126
SER 127
0.0576
SER 127
SER 128
-0.0003
SER 128
GLY 129
0.0001
GLY 129
GLU 130
-0.0249
GLU 130
ARG 131
-0.0003
ARG 131
VAL 132
0.0002
VAL 132
GLN 133
-0.1977
GLN 133
ILE 134
0.0000
ILE 134
GLU 135
-0.0002
GLU 135
PRO 136
-0.4456
PRO 136
LEU 137
-0.0001
LEU 137
MET 138
0.0005
MET 138
ARG 139
0.0662
ARG 139
GLY 140
0.0003
GLY 140
THR 141
0.0001
THR 141
THR 142
-0.3381
THR 142
LYS 143
0.0005
LYS 143
ASP 144
0.0000
ASP 144
ASP 145
0.0744
ASP 145
VAL 146
0.0001
VAL 146
MET 147
-0.0000
MET 147
HIS 148
0.0224
HIS 148
MET 149
-0.0001
MET 149
HIS 150
-0.0002
HIS 150
PHE 151
0.0666
PHE 151
ILE 152
-0.0004
ILE 152
GLY 153
-0.0000
GLY 153
ARG 154
0.0312
ARG 154
THR 155
-0.0001
THR 155
THR 156
-0.0001
THR 156
VAL 157
-0.0639
VAL 157
LYS 158
0.0004
LYS 158
VAL 159
-0.0001
VAL 159
GLU 160
-0.0269
GLU 160
ALA 161
0.0002
ALA 161
LYS 162
0.0003
LYS 162
LEU 163
0.0323
LEU 163
PRO 164
-0.0004
PRO 164
VAL 165
-0.0000
VAL 165
PHE 166
-0.0367
PHE 166
GLY 167
-0.0001
GLY 167
ASP 168
-0.0001
ASP 168
ILE 169
-0.0139
ILE 169
LEU 170
-0.0001
LEU 170
LYS 171
-0.0000
LYS 171
VAL 172
-0.0434
VAL 172
LEU 173
0.0001
LEU 173
GLY 174
-0.0002
GLY 174
ALA 175
-0.0441
ALA 175
THR 176
-0.0005
THR 176
ASP 177
-0.0001
ASP 177
ILE 178
0.0048
ILE 178
GLU 179
-0.0001
GLU 179
GLY 180
0.0000
GLY 180
GLU 181
-0.0348
GLU 181
LEU 182
-0.0001
LEU 182
PHE 183
-0.0000
PHE 183
ASP 184
0.0853
ASP 184
SER 185
0.0001
SER 185
LEU 186
0.0003
LEU 186
ASP 187
0.0302
ASP 187
ILE 188
-0.0000
ILE 188
VAL 189
-0.0004
VAL 189
ILE 190
0.0136
ILE 190
LYS 191
0.0000
LYS 191
PRO 192
0.0002
PRO 192
LYS 193
-0.0320
LYS 193
PHE 194
0.0001
PHE 194
LYS 195
0.0000
LYS 195
ARG 196
0.0026
ARG 196
ASP 197
-0.0003
ASP 197
ILE 198
0.0001
ILE 198
LYS 199
0.0574
LYS 199
LYS 200
0.0003
LYS 200
VAL 201
0.0003
VAL 201
ALA 202
-0.0054
ALA 202
LYS 203
-0.0002
LYS 203
ASP 204
-0.0003
ASP 204
ILE 205
0.0435
ILE 205
ILE 206
0.0000
ILE 206
PHE 207
-0.0002
PHE 207
ASN 208
-0.0636
ASN 208
PRO 209
0.0003
PRO 209
SER 210
0.0003
SER 210
PRO 211
0.0169
PRO 211
GLN 212
-0.0002
GLN 212
PHE 213
-0.0001
PHE 213
SER 214
0.1779
SER 214
ASP 215
0.0002
ASP 215
ILE 216
-0.0001
ILE 216
SER 217
-0.0732
SER 217
LEU 218
-0.0001
LEU 218
ARG 219
-0.0001
ARG 219
ALA 220
-0.0164
ALA 220
LYS 221
-0.0000
LYS 221
ASP 222
0.0001
ASP 222
GLU 223
-0.0457
GLU 223
ALA 224
0.0001
ALA 224
GLY 225
-0.0000
GLY 225
ASP 226
-0.0488
ASP 226
LEU 228
-0.0466
LEU 228
THR 229
-0.0003
THR 229
GLU 230
-0.0000
GLU 230
HIS 231
-0.0161
HIS 231
TYR 232
-0.0001
TYR 232
LEU 233
0.0001
LEU 233
SER 234
0.0764
SER 234
GLU 235
-0.0003
GLU 235
LYS 236
0.0002
LYS 236
GLY 237
-0.3619
GLY 237
HIS 238
-0.0004
HIS 238
LEU 239
0.0001
LEU 239
SER 240
0.2747
SER 240
ALA 241
0.0002
ALA 241
PRO 242
-0.0001
PRO 242
LEU 243
-0.0430
LEU 243
ASN 244
0.0002
ASN 244
LYS 245
-0.0006
LYS 245
VAL 246
-0.0949
VAL 246
THR 247
0.0003
THR 247
ASN 248
-0.0002
ASN 248
ALA 249
-0.0190
ALA 249
GLU 250
-0.0003
GLU 250
ILE 251
0.0002
ILE 251
ALA 252
-0.0858
ALA 252
GLU 253
0.0002
GLU 253
GLU 254
-0.0001
GLU 254
MET 255
-0.0373
MET 255
ALA 256
0.0001
ALA 256
TYR 257
-0.0001
TYR 257
CYS 258
-0.0148
CYS 258
TYR 259
0.0001
TYR 259
ALA 260
-0.0002
ALA 260
ARG 261
0.2103
ARG 261
MET 262
-0.0003
MET 262
LYS 263
-0.0003
LYS 263
SER 264
-0.0726
SER 264
ASP 265
-0.0002
ASP 265
ILE 266
-0.0002
ILE 266
LEU 267
-0.0444
LEU 267
GLU 268
0.0000
GLU 268
CYS 269
0.0001
CYS 269
PHE 270
0.0299
PHE 270
LYS 271
0.0003
LYS 271
ARG 272
0.0003
ARG 272
GLN 273
-0.0088
GLN 273
VAL 274
0.0003
VAL 274
GLY 275
0.0002
GLY 275
LYS 276
-0.0162
LYS 276
VAL 277
0.0001
VAL 277
LYS 278
0.0000
LYS 278
ASP 279
-0.1388
ASP 279
MET 1
0.1267
MET 1
LYS 2
-0.0003
LYS 2
ASN 3
-0.0000
ASN 3
GLY 4
-0.0126
GLY 4
PHE 5
-0.0004
PHE 5
TYR 6
0.0002
TYR 6
ALA 7
0.0557
ALA 7
THR 8
0.0000
THR 8
TYR 9
0.0001
TYR 9
ARG 10
-0.0050
ARG 10
SER 11
0.0003
SER 11
LYS 12
-0.0001
LYS 12
ASN 13
-0.0235
ASN 13
LYS 14
0.0001
LYS 14
GLY 15
-0.0001
GLY 15
LYS 16
0.0136
LYS 16
ASP 17
0.0001
ASP 17
LYS 18
0.0002
LYS 18
ARG 19
-0.0062
ARG 19
SER 20
-0.0003
SER 20
ILE 21
-0.0001
ILE 21
ASN 22
0.0258
ASN 22
LEU 23
0.0002
LEU 23
SER 24
-0.0002
SER 24
VAL 25
-0.0454
VAL 25
PHE 26
-0.0001
PHE 26
LEU 27
-0.0004
LEU 27
ASN 28
0.0237
ASN 28
SER 29
-0.0000
SER 29
LEU 30
0.0004
LEU 30
LEU 31
0.0365
LEU 31
ALA 32
-0.0002
ALA 32
ASP 33
-0.0003
ASP 33
ASN 34
0.0406
ASN 34
HIS 35
-0.0002
HIS 35
HIS 36
0.0003
HIS 36
LEU 37
-0.0073
LEU 37
GLN 38
-0.0003
GLN 38
VAL 39
0.0001
VAL 39
GLY 40
-0.0254
GLY 40
SER 41
-0.0003
SER 41
ASN 42
-0.0004
ASN 42
TYR 43
-0.0160
TYR 43
LEU 44
-0.0000
LEU 44
TYR 45
-0.0003
TYR 45
ILE 46
-0.0923
ILE 46
HIS 47
-0.0002
HIS 47
LYS 48
0.0000
LYS 48
ILE 49
-0.0575
ILE 49
ASP 50
-0.0002
ASP 50
GLY 51
0.0004
GLY 51
LYS 52
-0.0099
LYS 52
THR 53
-0.0003
THR 53
PHE 54
-0.0002
PHE 54
LEU 55
-0.0258
LEU 55
PHE 56
0.0000
PHE 56
THR 57
-0.0003
THR 57
LYS 58
-0.0275
LYS 58
THR 59
-0.0000
THR 59
ASN 60
0.0001
ASN 60
ASP 61
0.0166
ASP 61
LYS 62
-0.0002
LYS 62
SER 63
-0.0002
SER 63
LEU 64
-0.0072
LEU 64
VAL 65
-0.0000
VAL 65
GLN 66
-0.0003
GLN 66
LYS 67
0.0007
LYS 67
ILE 68
-0.0002
ILE 68
ASN 69
-0.0003
ASN 69
ARG 70
0.0056
ARG 70
SER 71
-0.0003
SER 71
LYS 72
0.0001
LYS 72
ALA 73
-0.0320
ALA 73
SER 74
0.0002
SER 74
VAL 75
-0.0001
VAL 75
GLU 76
0.0132
GLU 76
ASP 77
-0.0000
ASP 77
ILE 78
-0.0003
ILE 78
LYS 79
-0.0686
LYS 79
ASN 80
-0.0002
ASN 80
SER 81
-0.0000
SER 81
LEU 82
0.0116
LEU 82
ALA 83
-0.0002
ALA 83
ASP 84
0.0000
ASP 84
ASP 85
0.0452
ASP 85
GLU 86
0.0001
GLU 86
SER 87
0.0002
SER 87
LEU 88
0.0006
LEU 88
GLY 89
0.0002
GLY 89
PHE 90
0.0001
PHE 90
PRO 91
-0.0008
PRO 91
SER 92
-0.0001
SER 92
PHE 93
0.0000
PHE 93
LEU 94
-0.0221
LEU 94
PHE 95
-0.0002
PHE 95
VAL 96
-0.0002
VAL 96
GLU 97
-0.0376
GLU 97
GLY 98
0.0000
GLY 98
ASP 99
0.0003
ASP 99
THR 100
-0.0414
THR 100
ILE 101
-0.0000
ILE 101
GLY 102
0.0003
GLY 102
PHE 103
-0.0271
PHE 103
ALA 104
0.0004
ALA 104
ARG 105
-0.0000
ARG 105
THR 106
-0.0497
THR 106
VAL 107
-0.0002
VAL 107
PHE 108
-0.0002
PHE 108
GLY 109
-0.0473
GLY 109
PRO 110
-0.0004
PRO 110
THR 111
0.0001
THR 111
THR 112
-0.0499
THR 112
SER 113
0.0003
SER 113
ASP 114
-0.0004
ASP 114
LEU 115
-0.0348
LEU 115
THR 116
-0.0000
THR 116
ASP 117
-0.0001
ASP 117
PHE 118
0.0169
PHE 118
LEU 119
-0.0001
LEU 119
ILE 120
-0.0001
ILE 120
GLY 121
0.0020
GLY 121
LYS 122
0.0002
LYS 122
GLY 123
0.0001
GLY 123
MET 124
-0.0563
MET 124
SER 125
0.0002
SER 125
LEU 126
0.0002
LEU 126
SER 127
-0.0129
SER 127
SER 128
0.0003
SER 128
GLY 129
-0.0002
GLY 129
GLU 130
0.0013
GLU 130
ARG 131
-0.0000
ARG 131
VAL 132
-0.0002
VAL 132
GLN 133
0.1570
GLN 133
ILE 134
-0.0002
ILE 134
GLU 135
0.0000
GLU 135
PRO 136
0.3725
PRO 136
LEU 137
-0.0001
LEU 137
MET 138
-0.0001
MET 138
ARG 139
0.1150
ARG 139
GLY 140
-0.0002
GLY 140
THR 141
-0.0001
THR 141
THR 142
0.1753
THR 142
LYS 143
-0.0003
LYS 143
ASP 144
-0.0001
ASP 144
ASP 145
0.0048
ASP 145
VAL 146
0.0003
VAL 146
MET 147
0.0002
MET 147
HIS 148
-0.0274
HIS 148
MET 149
-0.0002
MET 149
HIS 150
-0.0002
HIS 150
PHE 151
-0.0642
PHE 151
ILE 152
-0.0001
ILE 152
GLY 153
-0.0003
GLY 153
ARG 154
-0.0146
ARG 154
THR 155
-0.0000
THR 155
THR 156
-0.0002
THR 156
VAL 157
0.0436
VAL 157
LYS 158
-0.0002
LYS 158
VAL 159
-0.0002
VAL 159
GLU 160
0.0068
GLU 160
ALA 161
0.0002
ALA 161
LYS 162
-0.0000
LYS 162
LEU 163
0.0223
LEU 163
PRO 164
-0.0000
PRO 164
VAL 165
-0.0000
VAL 165
PHE 166
0.0568
PHE 166
GLY 167
0.0001
GLY 167
ASP 168
-0.0000
ASP 168
ILE 169
0.0052
ILE 169
LEU 170
-0.0003
LEU 170
LYS 171
0.0002
LYS 171
VAL 172
0.0436
VAL 172
LEU 173
-0.0002
LEU 173
GLY 174
-0.0000
GLY 174
ALA 175
0.0524
ALA 175
THR 176
-0.0000
THR 176
ASP 177
0.0001
ASP 177
ILE 178
-0.0099
ILE 178
GLU 179
-0.0003
GLU 179
GLY 180
0.0002
GLY 180
GLU 181
0.0151
GLU 181
LEU 182
-0.0002
LEU 182
PHE 183
-0.0002
PHE 183
ASP 184
-0.0485
ASP 184
SER 185
0.0003
SER 185
LEU 186
-0.0001
LEU 186
ASP 187
-0.0148
ASP 187
ILE 188
0.0000
ILE 188
VAL 189
0.0002
VAL 189
ILE 190
0.0076
ILE 190
LYS 191
0.0002
LYS 191
PRO 192
-0.0000
PRO 192
LYS 193
0.0112
LYS 193
PHE 194
0.0000
PHE 194
LYS 195
-0.0002
LYS 195
ARG 196
-0.0302
ARG 196
ASP 197
0.0001
ASP 197
ILE 198
-0.0001
ILE 198
LYS 199
-0.0229
LYS 199
LYS 200
0.0002
LYS 200
VAL 201
0.0001
VAL 201
ALA 202
0.0110
ALA 202
LYS 203
0.0000
LYS 203
ASP 204
-0.0001
ASP 204
ILE 205
-0.0442
ILE 205
ILE 206
0.0002
ILE 206
PHE 207
-0.0002
PHE 207
ASN 208
0.0925
ASN 208
PRO 209
-0.0000
PRO 209
SER 210
-0.0004
SER 210
PRO 211
0.0019
PRO 211
GLN 212
-0.0002
GLN 212
PHE 213
0.0002
PHE 213
SER 214
-0.2325
SER 214
ASP 215
-0.0001
ASP 215
ILE 216
0.0002
ILE 216
SER 217
0.0615
SER 217
LEU 218
0.0001
LEU 218
ARG 219
-0.0005
ARG 219
ALA 220
-0.0621
ALA 220
LYS 221
-0.0000
LYS 221
ASP 222
-0.0000
ASP 222
GLU 223
0.0427
GLU 223
ALA 224
-0.0001
ALA 224
GLY 225
-0.0002
GLY 225
ASP 226
0.0441
ASP 226
ILE 227
0.0002
ILE 227
LEU 228
-0.0004
LEU 228
THR 229
0.1235
THR 229
GLU 230
-0.0001
GLU 230
HIS 231
0.0002
HIS 231
TYR 232
0.0212
TYR 232
LEU 233
0.0002
LEU 233
SER 234
0.0003
SER 234
GLU 235
0.0358
GLU 235
LYS 236
0.0002
LYS 236
GLY 237
0.0001
GLY 237
HIS 238
0.0039
HIS 238
LEU 239
-0.0000
LEU 239
SER 240
0.0001
SER 240
ALA 241
-0.0907
ALA 241
PRO 242
-0.0002
PRO 242
LEU 243
-0.0005
LEU 243
ASN 244
-0.0573
ASN 244
LYS 245
-0.0002
LYS 245
VAL 246
0.0000
VAL 246
THR 247
-0.0074
THR 247
ASN 248
-0.0001
ASN 248
ALA 249
-0.0004
ALA 249
GLU 250
-0.0514
GLU 250
ILE 251
0.0001
ILE 251
ALA 252
-0.0000
ALA 252
GLU 253
-0.0535
GLU 253
GLU 254
0.0001
GLU 254
MET 255
0.0004
MET 255
ALA 256
0.0580
ALA 256
TYR 257
0.0003
TYR 257
CYS 258
0.0001
CYS 258
TYR 259
0.1294
TYR 259
ALA 260
-0.0002
ALA 260
ARG 261
0.0000
ARG 261
MET 262
0.1845
MET 262
LYS 263
-0.0004
LYS 263
SER 264
-0.0002
SER 264
ASP 265
-0.0098
ASP 265
ILE 266
-0.0002
ILE 266
LEU 267
-0.0003
LEU 267
GLU 268
-0.0104
GLU 268
CYS 269
-0.0002
CYS 269
PHE 270
-0.0001
PHE 270
LYS 271
-0.0838
LYS 271
ARG 272
-0.0000
ARG 272
GLN 273
0.0001
GLN 273
VAL 274
0.0388
VAL 274
GLY 275
0.0000
GLY 275
LYS 276
0.0001
LYS 276
VAL 277
-0.1951
VAL 277
LYS 278
0.0005
LYS 278
ASP 279
0.0000
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.