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
GLY 26
THR 27
-0.0002
THR 27
HIS 28
0.0004
HIS 28
SER 29
-0.0373
SER 29
HIS 30
-0.0001
HIS 30
GLY 31
0.0002
GLY 31
LEU 32
-0.0500
LEU 32
PHE 33
-0.0001
PHE 33
LYS 34
0.0001
LYS 34
LYS 35
-0.0076
LYS 35
LEU 36
-0.0002
LEU 36
GLY 37
0.0001
GLY 37
ILE 38
-0.0056
ILE 38
PRO 39
0.0003
PRO 39
GLY 40
0.0000
GLY 40
PRO 41
0.0049
PRO 41
THR 42
0.0001
THR 42
PRO 43
0.0001
PRO 43
LEU 44
-0.0235
LEU 44
PRO 45
0.0001
PRO 45
PHE 46
-0.0002
PHE 46
LEU 47
0.0466
LEU 47
GLY 48
0.0003
GLY 48
ASN 49
-0.0000
ASN 49
ILE 50
0.0412
ILE 50
LEU 51
0.0002
LEU 51
SER 52
-0.0001
SER 52
TYR 53
0.0908
TYR 53
HIS 54
-0.0002
HIS 54
LYS 55
-0.0002
LYS 55
GLY 56
-0.0385
GLY 56
PHE 57
0.0002
PHE 57
CYS 58
-0.0000
CYS 58
MET 59
-0.0164
MET 59
PHE 60
0.0003
PHE 60
ASP 61
-0.0002
ASP 61
MET 62
-0.0308
MET 62
MET 62
0.0000
MET 62
GLU 63
-0.0004
GLU 63
CYS 64
0.0002
CYS 64
HIS 65
-0.0535
HIS 65
LYS 66
0.0001
LYS 66
LYS 67
-0.0001
LYS 67
TYR 68
0.0077
TYR 68
GLY 69
-0.0000
GLY 69
LYS 70
0.0004
LYS 70
VAL 71
-0.0175
VAL 71
TRP 72
-0.0001
TRP 72
GLY 73
0.0001
GLY 73
PHE 74
-0.0314
PHE 74
TYR 75
-0.0000
TYR 75
ASP 76
0.0005
ASP 76
GLY 77
0.0119
GLY 77
GLN 78
-0.0002
GLN 78
GLN 79
-0.0005
GLN 79
PRO 80
0.0090
PRO 80
VAL 81
-0.0001
VAL 81
LEU 82
-0.0000
LEU 82
ALA 83
-0.0314
ALA 83
ILE 84
0.0004
ILE 84
THR 85
0.0000
THR 85
ASP 86
0.0465
ASP 86
PRO 87
-0.0003
PRO 87
ASP 88
-0.0003
ASP 88
MET 89
-0.0212
MET 89
ILE 90
0.0000
ILE 90
LYS 91
0.0001
LYS 91
THR 92
-0.0064
THR 92
VAL 93
-0.0000
VAL 93
LEU 94
-0.0001
LEU 94
VAL 95
-0.0129
VAL 95
LYS 96
0.0002
LYS 96
GLU 97
0.0005
GLU 97
CYS 98
-0.0029
CYS 98
TYR 99
-0.0000
TYR 99
SER 100
0.0004
SER 100
VAL 101
-0.0290
VAL 101
PHE 102
-0.0001
PHE 102
THR 103
0.0001
THR 103
ASN 104
0.0389
ASN 104
ARG 105
0.0002
ARG 105
ARG 106
-0.0003
ARG 106
PRO 107
0.0922
PRO 107
PHE 108
-0.0000
PHE 108
GLY 109
0.0002
GLY 109
PRO 110
0.1716
PRO 110
VAL 111
0.0001
VAL 111
GLY 112
0.0002
GLY 112
PHE 113
-0.1035
PHE 113
MET 114
-0.0001
MET 114
LYS 115
-0.0002
LYS 115
SER 116
-0.0711
SER 116
ALA 117
0.0002
ALA 117
ILE 118
0.0001
ILE 118
SER 119
-0.0188
SER 119
ILE 120
-0.0002
ILE 120
ALA 121
-0.0003
ALA 121
GLU 122
0.1038
GLU 122
ASP 123
0.0003
ASP 123
GLU 124
0.0002
GLU 124
GLU 125
0.0085
GLU 125
TRP 126
0.0001
TRP 126
LYS 127
0.0001
LYS 127
ARG 128
-0.0300
ARG 128
LEU 129
-0.0003
LEU 129
ARG 130
-0.0000
ARG 130
SER 131
0.0765
SER 131
LEU 132
0.0002
LEU 132
LEU 133
0.0000
LEU 133
SER 134
0.0670
SER 134
PRO 135
0.0003
PRO 135
THR 136
0.0002
THR 136
PHE 137
0.0881
PHE 137
THR 138
-0.0004
THR 138
SER 139
0.0000
SER 139
GLY 140
-0.0110
GLY 140
LYS 141
-0.0001
LYS 141
LEU 142
0.0002
LEU 142
LYS 143
-0.0619
LYS 143
GLU 144
-0.0001
GLU 144
MET 145
-0.0001
MET 145
VAL 146
0.0240
VAL 146
PRO 147
-0.0002
PRO 147
ILE 148
-0.0001
ILE 148
ILE 149
-0.0083
ILE 149
ALA 150
-0.0002
ALA 150
GLN 151
0.0001
GLN 151
TYR 152
0.0066
TYR 152
GLY 153
0.0002
GLY 153
ASP 154
-0.0003
ASP 154
VAL 155
0.0424
VAL 155
LEU 156
-0.0001
LEU 156
VAL 157
-0.0001
VAL 157
ARG 158
0.0056
ARG 158
ASN 159
0.0001
ASN 159
LEU 160
0.0000
LEU 160
ARG 161
0.0245
ARG 161
ARG 162
-0.0000
ARG 162
GLU 163
0.0002
GLU 163
ALA 164
-0.0236
ALA 164
GLU 165
-0.0000
GLU 165
THR 166
-0.0004
THR 166
GLY 167
0.0242
GLY 167
LYS 168
-0.0000
LYS 168
PRO 169
0.0000
PRO 169
VAL 170
-0.0215
VAL 170
THR 171
0.0002
THR 171
LEU 172
-0.0004
LEU 172
LYS 173
-0.0245
LYS 173
ASP 174
-0.0002
ASP 174
VAL 175
0.0000
VAL 175
PHE 176
0.0114
PHE 176
GLY 177
0.0001
GLY 177
ALA 178
-0.0001
ALA 178
TYR 179
-0.0092
TYR 179
SER 180
-0.0004
SER 180
MET 181
0.0002
MET 181
ASP 182
0.0549
ASP 182
VAL 183
0.0000
VAL 183
ILE 184
-0.0001
ILE 184
THR 185
0.0118
THR 185
SER 186
0.0003
SER 186
THR 187
-0.0002
THR 187
SER 188
0.0399
SER 188
PHE 189
-0.0000
PHE 189
GLY 190
-0.0000
GLY 190
VAL 191
-0.1093
VAL 191
ASN 192
-0.0001
ASN 192
ILE 193
-0.0002
ILE 193
ASP 194
-0.1408
ASP 194
SER 195
0.0001
SER 195
LEU 196
-0.0000
LEU 196
ASN 197
-0.0065
ASN 197
ASN 198
-0.0003
ASN 198
PRO 199
-0.0000
PRO 199
GLN 200
-0.0114
GLN 200
ASP 201
0.0004
ASP 201
PRO 202
0.0000
PRO 202
PHE 203
-0.0087
PHE 203
VAL 204
-0.0002
VAL 204
GLU 205
-0.0001
GLU 205
ASN 206
0.0396
ASN 206
THR 207
0.0000
THR 207
LYS 208
0.0000
LYS 208
LYS 209
0.1290
LYS 209
LEU 210
-0.0001
LEU 210
LEU 211
-0.0002
LEU 211
ARG 212
0.0332
ARG 212
PHE 213
0.0004
PHE 213
ASP 214
0.0001
ASP 214
PHE 215
0.0976
PHE 215
LEU 216
-0.0000
LEU 216
ASP 217
0.0005
ASP 217
PRO 218
0.0091
PRO 218
PHE 219
0.0001
PHE 219
PHE 220
0.0001
PHE 220
LEU 221
-0.0009
LEU 221
SER 222
-0.0000
SER 222
ILE 223
0.0001
ILE 223
THR 224
0.0155
THR 224
VAL 225
-0.0001
VAL 225
PHE 226
0.0002
PHE 226
PRO 227
-0.0314
PRO 227
PHE 228
-0.0001
PHE 228
LEU 229
-0.0001
LEU 229
ILE 230
-0.0333
ILE 230
PRO 231
-0.0001
PRO 231
ILE 232
0.0002
ILE 232
LEU 233
0.0085
LEU 233
GLU 234
0.0001
GLU 234
VAL 235
0.0001
VAL 235
LEU 236
-0.0034
LEU 236
ASN 237
0.0003
ASN 237
ILE 238
0.0001
ILE 238
CYS 239
0.0008
CYS 239
VAL 240
0.0003
VAL 240
PHE 241
-0.0003
PHE 241
PRO 242
0.0351
PRO 242
ARG 243
0.0000
ARG 243
GLU 244
0.0001
GLU 244
VAL 245
-0.0228
VAL 245
THR 246
-0.0002
THR 246
ASN 247
-0.0001
ASN 247
PHE 248
0.0247
PHE 248
LEU 249
-0.0001
LEU 249
ARG 250
0.0002
ARG 250
LYS 251
0.0020
LYS 251
SER 252
-0.0001
SER 252
VAL 253
0.0002
VAL 253
LYS 254
0.0021
LYS 254
ARG 255
0.0002
ARG 255
MET 256
-0.0001
MET 256
LYS 257
-0.0505
LYS 257
GLU 258
0.0002
GLU 258
SER 259
-0.0003
SER 259
ARG 260
0.0133
ARG 260
LEU 261
-0.0003
LEU 261
GLU 262
-0.0004
GLU 262
ASP 263
0.0292
ASP 263
THR 269
0.1055
THR 269
ASP 270
0.0000
ASP 270
PHE 271
0.0003
PHE 271
LEU 272
0.0348
LEU 272
GLN 273
-0.0004
GLN 273
LEU 274
-0.0001
LEU 274
MET 275
0.0186
MET 275
ILE 276
0.0003
ILE 276
ASP 277
0.0002
ASP 277
SER 278
-0.0661
SER 278
GLN 279
-0.0003
GLN 279
ASN 280
-0.0000
ASN 280
SER 281
-0.0655
SER 281
SER 286
-0.0587
SER 286
HIS 287
0.0000
HIS 287
LYS 288
0.0000
LYS 288
ALA 289
-0.0110
ALA 289
LEU 290
-0.0003
LEU 290
SER 291
0.0002
SER 291
ASP 292
-0.0185
ASP 292
LEU 293
0.0001
LEU 293
GLU 294
-0.0000
GLU 294
LEU 295
-0.0062
LEU 295
VAL 296
-0.0001
VAL 296
ALA 297
0.0003
ALA 297
GLN 298
-0.0010
GLN 298
SER 299
-0.0001
SER 299
ILE 300
-0.0000
ILE 300
ILE 301
-0.0117
ILE 301
PHE 302
-0.0002
PHE 302
ILE 303
0.0000
ILE 303
PHE 304
0.0213
PHE 304
ALA 305
-0.0004
ALA 305
GLY 306
-0.0003
GLY 306
TYR 307
-0.0268
TYR 307
GLU 308
-0.0000
GLU 308
THR 309
-0.0004
THR 309
THR 310
0.0600
THR 310
SER 311
-0.0001
SER 311
SER 312
0.0003
SER 312
VAL 313
-0.0065
VAL 313
LEU 314
-0.0001
LEU 314
SER 315
-0.0001
SER 315
PHE 316
0.0224
PHE 316
ILE 317
-0.0003
ILE 317
MET 318
0.0000
MET 318
TYR 319
-0.0291
TYR 319
GLU 320
-0.0002
GLU 320
LEU 321
-0.0002
LEU 321
ALA 322
-0.0212
ALA 322
THR 323
-0.0001
THR 323
HIS 324
0.0002
HIS 324
PRO 325
0.0451
PRO 325
ASP 326
-0.0004
ASP 326
VAL 327
-0.0004
VAL 327
GLN 328
-0.0396
GLN 328
GLN 329
0.0001
GLN 329
LYS 330
-0.0002
LYS 330
LEU 331
0.0197
LEU 331
GLN 332
0.0005
GLN 332
GLU 333
0.0000
GLU 333
GLU 334
0.0324
GLU 334
ILE 335
0.0002
ILE 335
ASP 336
0.0002
ASP 336
ALA 337
0.0214
ALA 337
VAL 338
-0.0001
VAL 338
LEU 339
0.0003
LEU 339
PRO 340
-0.0306
PRO 340
ASN 341
-0.0001
ASN 341
LYS 342
-0.0002
LYS 342
ALA 343
-0.0182
ALA 343
PRO 344
0.0000
PRO 344
PRO 345
0.0000
PRO 345
THR 346
-0.0547
THR 346
TYR 347
0.0001
TYR 347
ASP 348
0.0004
ASP 348
THR 349
0.0392
THR 349
VAL 350
0.0002
VAL 350
LEU 351
0.0001
LEU 351
GLN 352
0.0777
GLN 352
MET 353
0.0001
MET 353
GLU 354
-0.0002
GLU 354
TYR 355
0.0505
TYR 355
LEU 356
0.0003
LEU 356
ASP 357
-0.0001
ASP 357
MET 358
0.0384
MET 358
VAL 359
-0.0001
VAL 359
VAL 360
0.0002
VAL 360
ASN 361
-0.0484
ASN 361
GLU 362
0.0000
GLU 362
THR 363
-0.0004
THR 363
LEU 364
0.0050
LEU 364
ARG 365
0.0001
ARG 365
LEU 366
0.0001
LEU 366
PHE 367
-0.0710
PHE 367
PRO 368
-0.0001
PRO 368
ILE 369
0.0000
ILE 369
ALA 370
0.0499
ALA 370
MET 371
-0.0000
MET 371
ARG 372
0.0001
ARG 372
LEU 373
0.0349
LEU 373
GLU 374
0.0000
GLU 374
ARG 375
-0.0000
ARG 375
VAL 376
0.0138
VAL 376
CYS 377
-0.0000
CYS 377
LYS 378
-0.0002
LYS 378
LYS 379
0.0347
LYS 379
ASP 380
0.0001
ASP 380
VAL 381
-0.0002
VAL 381
GLU 382
0.0042
GLU 382
ILE 383
0.0003
ILE 383
ASN 384
0.0002
ASN 384
GLY 385
-0.0337
GLY 385
MET 386
-0.0002
MET 386
PHE 387
0.0001
PHE 387
ILE 388
0.0193
ILE 388
PRO 389
0.0003
PRO 389
LYS 390
-0.0002
LYS 390
GLY 391
0.0306
GLY 391
VAL 392
0.0002
VAL 392
VAL 393
0.0004
VAL 393
VAL 394
-0.0115
VAL 394
MET 395
-0.0002
MET 395
ILE 396
-0.0001
ILE 396
PRO 397
0.0526
PRO 397
SER 398
0.0001
SER 398
TYR 399
0.0001
TYR 399
ALA 400
0.0183
ALA 400
LEU 401
0.0003
LEU 401
HIS 402
0.0005
HIS 402
ARG 403
0.0396
ARG 403
ASP 404
-0.0000
ASP 404
PRO 405
0.0002
PRO 405
LYS 406
0.0401
LYS 406
TYR 407
0.0001
TYR 407
TRP 408
-0.0001
TRP 408
THR 409
0.0884
THR 409
GLU 410
-0.0002
GLU 410
PRO 411
0.0001
PRO 411
GLU 412
0.0651
GLU 412
LYS 413
0.0002
LYS 413
PHE 414
-0.0003
PHE 414
LEU 415
-0.0486
LEU 415
PRO 416
0.0001
PRO 416
GLU 417
0.0001
GLU 417
ARG 418
-0.0207
ARG 418
PHE 419
-0.0001
PHE 419
SER 420
0.0000
SER 420
LYS 421
-0.0213
LYS 421
LYS 422
-0.0002
LYS 422
ASN 423
0.0001
ASN 423
LYS 424
0.0572
LYS 424
ASP 425
0.0002
ASP 425
ASN 426
0.0002
ASN 426
ASN 426
0.0235
ASN 426
ILE 427
0.0936
ILE 427
ASP 428
0.0001
ASP 428
PRO 429
0.0001
PRO 429
TYR 430
0.0173
TYR 430
ILE 431
0.0001
ILE 431
TYR 432
0.0001
TYR 432
THR 433
0.0345
THR 433
PRO 434
-0.0001
PRO 434
PHE 435
0.0002
PHE 435
GLY 436
-0.0701
GLY 436
SER 437
0.0001
SER 437
GLY 438
0.0002
GLY 438
PRO 439
0.1507
PRO 439
ARG 440
-0.0003
ARG 440
ASN 441
-0.0000
ASN 441
CYS 442
-0.0752
CYS 442
ILE 443
0.0002
ILE 443
GLY 444
-0.0003
GLY 444
MET 445
0.1280
MET 445
ARG 446
-0.0002
ARG 446
PHE 447
0.0002
PHE 447
ALA 448
0.0934
ALA 448
LEU 449
0.0001
LEU 449
MET 450
-0.0000
MET 450
ASN 451
-0.0268
ASN 451
MET 452
-0.0001
MET 452
LYS 453
-0.0001
LYS 453
LEU 454
0.0112
LEU 454
ALA 455
0.0003
ALA 455
LEU 456
0.0003
LEU 456
ILE 457
0.0198
ILE 457
ARG 458
-0.0001
ARG 458
VAL 459
-0.0002
VAL 459
LEU 460
-0.0086
LEU 460
GLN 461
-0.0000
GLN 461
ASN 462
-0.0002
ASN 462
PHE 463
0.0409
PHE 463
SER 464
0.0000
SER 464
PHE 465
0.0001
PHE 465
LYS 466
0.0222
LYS 466
PRO 467
-0.0001
PRO 467
CYS 468
-0.0003
CYS 468
LYS 469
-0.0027
LYS 469
GLU 470
-0.0003
GLU 470
THR 471
-0.0000
THR 471
GLN 472
0.1192
GLN 472
ILE 473
-0.0001
ILE 473
PRO 474
-0.0001
PRO 474
LEU 475
0.0621
LEU 475
LYS 476
-0.0001
LYS 476
LEU 477
0.0000
LEU 477
SER 478
-0.0322
SER 478
LEU 479
0.0002
LEU 479
GLY 480
0.0001
GLY 480
GLY 481
-0.0248
GLY 481
LEU 482
-0.0001
LEU 482
LEU 483
-0.0000
LEU 483
GLN 484
0.0529
GLN 484
PRO 485
0.0000
PRO 485
GLU 486
-0.0000
GLU 486
LYS 487
0.1907
LYS 487
PRO 488
0.0000
PRO 488
VAL 489
0.0005
VAL 489
VAL 490
0.1728
VAL 490
LEU 491
-0.0001
LEU 491
LYS 492
-0.0002
LYS 492
VAL 493
0.0435
VAL 493
GLU 494
0.0000
GLU 494
SER 495
0.0001
SER 495
SER 495
0.0000
SER 495
ARG 496
-0.0137
ARG 496
ASP 497
-0.0005
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: April 25th, 2023.