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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
LYS 3
ALA 4
0.0002
ALA 4
ALA 5
-0.0157
ALA 5
ALA 6
-0.0000
ALA 6
ILE 7
0.0128
ILE 7
GLY 8
0.0002
GLY 8
ILE 9
0.0230
ILE 9
ASP 10
0.0001
ASP 10
LEU 11
0.0156
LEU 11
GLY 12
-0.0001
GLY 12
THR 13
0.0565
THR 13
THR 14
0.0003
THR 14
TYR 15
0.0295
TYR 15
SER 16
0.0001
SER 16
CYS 17
0.0513
CYS 17
VAL 18
0.0001
VAL 18
GLY 19
0.0417
GLY 19
VAL 20
-0.0000
VAL 20
PHE 21
0.0337
PHE 21
GLN 22
-0.0000
GLN 22
HIS 23
0.0071
HIS 23
GLY 24
-0.0001
GLY 24
LYS 25
0.0084
LYS 25
VAL 26
-0.0001
VAL 26
GLU 27
0.0426
GLU 27
ILE 28
-0.0006
ILE 28
ILE 29
0.0100
ILE 29
ALA 30
-0.0001
ALA 30
ASN 31
0.0535
ASN 31
ASP 32
0.0002
ASP 32
GLN 33
0.0091
GLN 33
GLY 34
-0.0001
GLY 34
ASN 35
-0.0236
ASN 35
ARG 36
-0.0003
ARG 36
THR 37
0.0327
THR 37
THR 38
-0.0002
THR 38
PRO 39
0.0569
PRO 39
SER 40
0.0001
SER 40
TYR 41
-0.0020
TYR 41
VAL 42
-0.0001
VAL 42
ALA 43
0.0169
ALA 43
PHE 44
-0.0003
PHE 44
THR 45
-0.0051
THR 45
ASP 46
-0.0000
ASP 46
THR 47
-0.0018
THR 47
GLU 48
-0.0004
GLU 48
ARG 49
0.0086
ARG 49
LEU 50
0.0001
LEU 50
ILE 51
0.0177
ILE 51
GLY 52
0.0001
GLY 52
ASP 53
-0.0331
ASP 53
ALA 54
-0.0003
ALA 54
ALA 55
0.0163
ALA 55
LYS 56
0.0002
LYS 56
ASN 57
-0.0368
ASN 57
GLN 58
0.0002
GLN 58
VAL 59
0.0259
VAL 59
ALA 60
0.0003
ALA 60
LEU 61
0.1162
LEU 61
ASN 62
-0.0000
ASN 62
PRO 63
-0.0588
PRO 63
GLN 64
0.0000
GLN 64
ASN 65
-0.0016
ASN 65
THR 66
0.0003
THR 66
VAL 67
-0.0182
VAL 67
PHE 68
-0.0001
PHE 68
ASP 69
-0.0231
ASP 69
ALA 70
-0.0001
ALA 70
LYS 71
-0.0200
LYS 71
ARG 72
0.0001
ARG 72
LEU 73
0.1769
LEU 73
ILE 74
-0.0001
ILE 74
GLY 75
-0.0267
GLY 75
ARG 76
0.0002
ARG 76
LYS 77
-0.0083
LYS 77
PHE 78
-0.0002
PHE 78
GLY 79
-0.0118
GLY 79
ASP 80
0.0001
ASP 80
PRO 81
-0.0349
PRO 81
VAL 82
-0.0004
VAL 82
VAL 83
0.0393
VAL 83
GLN 84
-0.0001
GLN 84
SER 85
0.0147
SER 85
ASP 86
0.0003
ASP 86
MET 87
0.0252
MET 87
LYS 88
-0.0002
LYS 88
HIS 89
0.0366
HIS 89
TRP 90
0.0001
TRP 90
PRO 91
-0.0433
PRO 91
PHE 92
-0.0001
PHE 92
GLN 93
0.0251
GLN 93
VAL 94
0.0003
VAL 94
ILE 95
0.0447
ILE 95
ASN 96
-0.0003
ASN 96
ASP 97
0.0075
ASP 97
GLY 98
-0.0003
GLY 98
ASP 99
0.0024
ASP 99
LYS 100
-0.0000
LYS 100
PRO 101
0.0175
PRO 101
LYS 102
-0.0001
LYS 102
VAL 103
0.0088
VAL 103
GLN 104
0.0003
GLN 104
VAL 105
-0.0050
VAL 105
SER 106
-0.0002
SER 106
TYR 107
-0.0005
TYR 107
LYS 108
0.0001
LYS 108
GLY 109
-0.0172
GLY 109
GLU 110
0.0002
GLU 110
THR 111
-0.0052
THR 111
LYS 112
-0.0002
LYS 112
ALA 113
-0.0030
ALA 113
PHE 114
-0.0000
PHE 114
TYR 115
0.0140
TYR 115
PRO 116
0.0000
PRO 116
GLU 117
-0.0281
GLU 117
GLU 118
0.0003
GLU 118
ILE 119
-0.0024
ILE 119
SER 120
0.0003
SER 120
SER 121
0.0305
SER 121
MET 122
0.0000
MET 122
VAL 123
-0.0235
VAL 123
LEU 124
0.0002
LEU 124
THR 125
0.0113
THR 125
LYS 126
0.0000
LYS 126
MET 127
0.0162
MET 127
LYS 128
-0.0000
LYS 128
GLU 129
0.0062
GLU 129
ILE 130
-0.0002
ILE 130
ALA 131
0.0341
ALA 131
GLU 132
-0.0001
GLU 132
ALA 133
0.0078
ALA 133
TYR 134
0.0001
TYR 134
LEU 135
-0.0054
LEU 135
GLY 136
0.0001
GLY 136
TYR 137
-0.0017
TYR 137
PRO 138
0.0000
PRO 138
VAL 139
-0.0002
VAL 139
THR 140
-0.0000
THR 140
ASN 141
0.0100
ASN 141
ALA 142
-0.0000
ALA 142
VAL 143
0.0223
VAL 143
ILE 144
0.0000
ILE 144
THR 145
0.0264
THR 145
VAL 146
-0.0001
VAL 146
PRO 147
0.0641
PRO 147
ALA 148
0.0000
ALA 148
TYR 149
-0.0417
TYR 149
PHE 150
0.0002
PHE 150
ASN 151
0.0622
ASN 151
ASP 152
0.0001
ASP 152
SER 153
-0.0213
SER 153
GLN 154
-0.0000
GLN 154
ARG 155
-0.0675
ARG 155
GLN 156
0.0000
GLN 156
ALA 157
-0.0134
ALA 157
THR 158
-0.0003
THR 158
LYS 159
0.0095
LYS 159
ASP 160
-0.0001
ASP 160
ALA 161
0.0223
ALA 161
GLY 162
-0.0002
GLY 162
VAL 163
0.0055
VAL 163
ILE 164
0.0000
ILE 164
ALA 165
-0.0053
ALA 165
GLY 166
0.0002
GLY 166
LEU 167
-0.0093
LEU 167
ASN 168
-0.0001
ASN 168
VAL 169
0.0199
VAL 169
LEU 170
-0.0002
LEU 170
ARG 171
0.0510
ARG 171
ILE 172
-0.0004
ILE 172
ILE 173
-0.0374
ILE 173
ASN 174
-0.0002
ASN 174
GLU 175
-0.0180
GLU 175
PRO 176
-0.0002
PRO 176
THR 177
-0.0078
THR 177
ALA 178
-0.0002
ALA 178
ALA 179
-0.0348
ALA 179
ALA 180
-0.0000
ALA 180
ILE 181
0.0260
ILE 181
ALA 182
-0.0000
ALA 182
TYR 183
-0.0554
TYR 183
GLY 184
0.0001
GLY 184
LEU 185
0.0206
LEU 185
ASP 186
-0.0001
ASP 186
ARG 187
-0.0176
ARG 187
THR 188
-0.0003
THR 188
GLY 189
0.0142
GLY 189
LYS 190
-0.0002
LYS 190
GLY 191
-0.0001
GLY 191
GLU 192
0.0002
GLU 192
ARG 193
0.0143
ARG 193
ASN 194
0.0004
ASN 194
VAL 195
0.0076
VAL 195
LEU 196
0.0002
LEU 196
ILE 197
0.0012
ILE 197
PHE 198
0.0002
PHE 198
ASP 199
0.0245
ASP 199
LEU 200
-0.0002
LEU 200
GLY 201
0.0223
GLY 201
GLY 202
-0.0004
GLY 202
GLY 203
0.0528
GLY 203
THR 204
0.0002
THR 204
PHE 205
-0.0056
PHE 205
ASP 206
0.0002
ASP 206
VAL 207
-0.0327
VAL 207
SER 208
0.0002
SER 208
ILE 209
-0.0416
ILE 209
LEU 210
0.0000
LEU 210
THR 211
-0.0438
THR 211
ILE 212
0.0001
ILE 212
ASP 213
-0.0224
ASP 213
ASP 214
0.0002
ASP 214
GLY 215
0.0157
GLY 215
ILE 216
0.0002
ILE 216
PHE 217
-0.0420
PHE 217
GLU 218
-0.0001
GLU 218
VAL 219
-0.0665
VAL 219
LYS 220
0.0003
LYS 220
ALA 221
-0.0479
ALA 221
THR 222
0.0001
THR 222
ALA 223
-0.0628
ALA 223
GLY 224
-0.0001
GLY 224
ASP 225
-0.1233
ASP 225
THR 226
0.0001
THR 226
HIS 227
0.0430
HIS 227
LEU 228
-0.0000
LEU 228
GLY 229
-0.0192
GLY 229
GLY 230
-0.0000
GLY 230
GLU 231
0.0276
GLU 231
ASP 232
-0.0001
ASP 232
PHE 233
0.0806
PHE 233
ASP 234
-0.0001
ASP 234
ASN 235
-0.0448
ASN 235
ARG 236
-0.0001
ARG 236
LEU 237
-0.0614
LEU 237
VAL 238
-0.0001
VAL 238
ASN 239
0.1030
ASN 239
HIS 240
0.0001
HIS 240
PHE 241
-0.1604
PHE 241
VAL 242
0.0002
VAL 242
GLU 243
0.0941
GLU 243
GLU 244
-0.0001
GLU 244
PHE 245
-0.0344
PHE 245
LYS 246
0.0001
LYS 246
ARG 247
0.0732
ARG 247
LYS 248
-0.0003
LYS 248
HIS 249
-0.0277
HIS 249
LYS 250
-0.0002
LYS 250
LYS 251
0.0513
LYS 251
ASP 252
0.0000
ASP 252
ILE 253
0.1002
ILE 253
SER 254
-0.0001
SER 254
GLN 255
-0.0634
GLN 255
ASN 256
-0.0000
ASN 256
LYS 257
-0.0060
LYS 257
ARG 258
0.0001
ARG 258
ALA 259
0.2431
ALA 259
VAL 260
-0.0001
VAL 260
ARG 261
0.2371
ARG 261
ARG 262
0.0001
ARG 262
LEU 263
0.0329
LEU 263
ARG 264
0.0000
ARG 264
THR 265
-0.0192
THR 265
ALA 266
0.0003
ALA 266
CYS 267
-0.0074
CYS 267
GLU 268
0.0000
GLU 268
ARG 269
-0.0515
ARG 269
ALA 270
-0.0001
ALA 270
LYS 271
0.0262
LYS 271
ARG 272
0.0004
ARG 272
THR 273
-0.0416
THR 273
LEU 274
-0.0002
LEU 274
SER 275
0.0271
SER 275
SER 276
0.0002
SER 276
SER 277
0.0233
SER 277
THR 278
-0.0002
THR 278
GLN 279
0.0854
GLN 279
ALA 280
-0.0000
ALA 280
SER 281
0.2390
SER 281
LEU 282
0.0003
LEU 282
GLU 283
0.0179
GLU 283
ILE 284
0.0002
ILE 284
ASP 285
0.0655
ASP 285
SER 286
0.0002
SER 286
LEU 287
-0.0587
LEU 287
PHE 288
-0.0001
PHE 288
GLU 289
0.0583
GLU 289
GLY 290
-0.0002
GLY 290
ILE 291
0.0024
ILE 291
ASP 292
0.0001
ASP 292
PHE 293
-0.0416
PHE 293
TYR 294
0.0001
TYR 294
THR 295
-0.0115
THR 295
SER 296
-0.0003
SER 296
ILE 297
0.0199
ILE 297
THR 298
0.0001
THR 298
ARG 299
0.0189
ARG 299
ALA 300
0.0001
ALA 300
ARG 301
-0.1157
ARG 301
PHE 302
0.0002
PHE 302
GLU 303
-0.0673
GLU 303
GLU 304
0.0002
GLU 304
LEU 305
-0.0053
LEU 305
CYS 306
-0.0002
CYS 306
SER 307
-0.0695
SER 307
ASP 308
0.0003
ASP 308
LEU 309
0.1051
LEU 309
PHE 310
0.0001
PHE 310
ARG 311
0.0219
ARG 311
SER 312
0.0002
SER 312
THR 313
-0.0150
THR 313
LEU 314
-0.0000
LEU 314
GLU 315
0.0331
GLU 315
PRO 316
-0.0001
PRO 316
VAL 317
0.0044
VAL 317
GLU 318
0.0001
GLU 318
LYS 319
0.0355
LYS 319
ALA 320
-0.0001
ALA 320
LEU 321
-0.0058
LEU 321
ARG 322
-0.0000
ARG 322
ASP 323
0.0156
ASP 323
ALA 324
0.0001
ALA 324
LYS 325
0.0182
LYS 325
LEU 326
-0.0001
LEU 326
ASP 327
0.0297
ASP 327
LYS 328
0.0002
LYS 328
ALA 329
-0.0117
ALA 329
GLN 330
-0.0001
GLN 330
ILE 331
0.0041
ILE 331
HIS 332
0.0001
HIS 332
ASP 333
0.0239
ASP 333
LEU 334
-0.0001
LEU 334
VAL 335
0.0018
VAL 335
LEU 336
0.0004
LEU 336
VAL 337
0.0179
VAL 337
GLY 338
-0.0002
GLY 338
GLY 339
0.0393
GLY 339
SER 340
-0.0003
SER 340
THR 341
0.0528
THR 341
ARG 342
-0.0002
ARG 342
ILE 343
-0.1741
ILE 343
PRO 344
-0.0002
PRO 344
LYS 345
0.0356
LYS 345
VAL 346
-0.0001
VAL 346
GLN 347
-0.0650
GLN 347
LYS 348
-0.0000
LYS 348
LEU 349
-0.0023
LEU 349
LEU 350
-0.0001
LEU 350
GLN 351
-0.0111
GLN 351
ASP 352
-0.0002
ASP 352
PHE 353
0.0245
PHE 353
PHE 354
0.0000
PHE 354
ASN 355
0.0014
ASN 355
GLY 356
-0.0000
GLY 356
ARG 357
-0.0008
ARG 357
ASP 358
0.0000
ASP 358
LEU 359
-0.0048
LEU 359
ASN 360
0.0004
ASN 360
LYS 361
0.0350
LYS 361
SER 362
0.0000
SER 362
ILE 363
-0.0805
ILE 363
ASN 364
-0.0003
ASN 364
PRO 365
-0.0483
PRO 365
ASP 366
0.0003
ASP 366
GLU 367
-0.0826
GLU 367
ALA 368
0.0001
ALA 368
VAL 369
-0.0187
VAL 369
ALA 370
0.0002
ALA 370
TYR 371
0.0286
TYR 371
GLY 372
-0.0000
GLY 372
ALA 373
-0.0465
ALA 373
ALA 374
-0.0001
ALA 374
VAL 375
0.0422
VAL 375
GLN 376
-0.0001
GLN 376
ALA 377
-0.0031
ALA 377
ALA 378
0.0001
ALA 378
ILE 379
0.0125
ILE 379
LEU 380
-0.0001
LEU 380
ILE 381
0.0164
ILE 381
LYS 382
0.0001
LYS 382
SER 383
-0.0199
SER 383
THR 384
0.0002
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.