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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
PHE 154
GLU 155
-0.0000
GLU 155
LEU 156
-0.0344
LEU 156
ASP 157
0.0001
ASP 157
ALA 158
-0.0374
ALA 158
ALA 159
0.0003
ALA 159
PRO 160
-0.0265
PRO 160
GLY 161
0.0002
GLY 161
ALA 162
-0.0270
ALA 162
SER 163
0.0002
SER 163
LYS 164
0.1606
LYS 164
LEU 165
0.0003
LEU 165
ARG 166
-0.0119
ARG 166
ALA 167
0.0002
ALA 167
VAL 168
0.0237
VAL 168
LEU 169
-0.0004
LEU 169
GLU 170
-0.0739
GLU 170
LYS 171
-0.0001
LYS 171
LEU 172
-0.0305
LEU 172
LYS 173
0.0001
LYS 173
LEU 174
-0.0536
LEU 174
SER 175
0.0002
SER 175
ARG 176
-0.0227
ARG 176
ASP 177
0.0001
ASP 177
ASP 178
0.0475
ASP 178
ILE 179
-0.0001
ILE 179
SER 180
0.0095
SER 180
THR 181
0.0000
THR 181
ALA 182
-0.0507
ALA 182
ALA 183
0.0002
ALA 183
GLY 184
-0.0464
GLY 184
MET 185
0.0004
MET 185
VAL 186
-0.0172
VAL 186
LYS 187
0.0001
LYS 187
GLY 188
0.0139
GLY 188
VAL 189
0.0000
VAL 189
VAL 190
-0.0307
VAL 190
ASP 191
-0.0004
ASP 191
HIS 192
-0.0069
HIS 192
LEU 193
0.0001
LEU 193
LEU 194
-0.0321
LEU 194
LEU 195
-0.0002
LEU 195
ARG 196
0.0013
ARG 196
LEU 197
-0.0002
LEU 197
LYS 198
-0.0248
LYS 198
CYS 199
0.0001
CYS 199
ASP 200
0.0242
ASP 200
SER 201
-0.0000
SER 201
ALA 202
-0.0006
ALA 202
PHE 203
0.0004
PHE 203
ARG 204
0.0000
ARG 204
GLY 205
0.0000
GLY 205
VAL 206
0.0523
VAL 206
GLY 207
0.0001
GLY 207
LEU 208
0.1129
LEU 208
LEU 209
0.0001
LEU 209
ASN 210
0.0520
ASN 210
THR 211
0.0003
THR 211
GLY 212
-0.0033
GLY 212
SER 213
0.0001
SER 213
TYR 214
-0.0060
TYR 214
TYR 215
-0.0003
TYR 215
GLU 216
0.0829
GLU 216
HIS 217
-0.0003
HIS 217
VAL 218
0.0183
VAL 218
LYS 219
-0.0000
LYS 219
ILE 220
0.0657
ILE 220
SER 221
0.0000
SER 221
ALA 222
0.1941
ALA 222
PRO 223
-0.0001
PRO 223
ASN 224
0.1777
ASN 224
GLU 225
0.0002
GLU 225
PHE 226
-0.0109
PHE 226
ASP 227
-0.0002
ASP 227
VAL 228
0.0418
VAL 228
MET 229
-0.0002
MET 229
PHE 230
0.0504
PHE 230
LYS 231
-0.0003
LYS 231
LEU 232
0.0565
LEU 232
GLU 233
0.0001
GLU 233
VAL 234
0.0234
VAL 234
PRO 235
-0.0001
PRO 235
ARG 236
0.0211
ARG 236
ILE 237
0.0002
ILE 237
GLN 238
-0.0094
GLN 238
LEU 239
-0.0001
LEU 239
GLU 240
0.0141
GLU 240
GLU 241
0.0002
GLU 241
TYR 242
0.0203
TYR 242
SER 243
-0.0005
SER 243
ASN 244
-0.0090
ASN 244
THR 245
-0.0001
THR 245
ARG 246
0.0766
ARG 246
ALA 247
0.0002
ALA 247
TYR 248
-0.0128
TYR 248
TYR 249
0.0001
TYR 249
PHE 250
-0.0570
PHE 250
VAL 251
-0.0002
VAL 251
LYS 252
-0.0214
LYS 252
PHE 253
-0.0001
PHE 253
LYS 254
0.0139
LYS 254
ARG 255
-0.0002
ARG 255
ASN 256
0.0055
ASN 256
PRO 257
-0.0001
PRO 257
LYS 258
-0.0009
LYS 258
GLU 259
-0.0003
GLU 259
ASN 260
0.0244
ASN 260
PRO 261
-0.0001
PRO 261
LEU 262
0.0051
LEU 262
SER 263
-0.0004
SER 263
GLN 264
-0.0147
GLN 264
PHE 265
-0.0001
PHE 265
LEU 266
0.0126
LEU 266
GLU 267
-0.0006
GLU 267
GLY 268
-0.0226
GLY 268
GLU 269
-0.0001
GLU 269
ILE 270
-0.0053
ILE 270
LEU 271
0.0003
LEU 271
SER 272
-0.0013
SER 272
ALA 273
-0.0003
ALA 273
SER 274
0.0037
SER 274
LYS 275
-0.0001
LYS 275
MET 276
0.0126
MET 276
LEU 277
0.0000
LEU 277
SER 278
0.0221
SER 278
LYS 279
-0.0003
LYS 279
PHE 280
0.0204
PHE 280
ARG 281
0.0000
ARG 281
LYS 282
0.0014
LYS 282
ILE 283
0.0001
ILE 283
ILE 284
0.0102
ILE 284
LYS 285
0.0000
LYS 285
GLU 286
0.0040
GLU 286
GLU 287
0.0002
GLU 287
ILE 288
0.0017
ILE 288
ASN 289
-0.0004
ASN 289
ASP 290
0.0023
ASP 290
ILE 291
0.0003
ILE 291
LYS 292
-0.0297
LYS 292
ASP 293
-0.0000
ASP 293
THR 294
0.0696
THR 294
ASP 295
0.0004
ASP 295
VAL 296
-0.0141
VAL 296
ILE 297
0.0000
ILE 297
MET 298
0.0130
MET 298
LYS 299
-0.0001
LYS 299
ARG 300
0.0107
ARG 300
LYS 301
-0.0001
LYS 301
ARG 302
-0.0142
ARG 302
GLY 303
-0.0001
GLY 303
GLY 304
0.0426
GLY 304
SER 305
0.0000
SER 305
PRO 306
-0.0249
PRO 306
ALA 307
-0.0002
ALA 307
VAL 308
0.0019
VAL 308
THR 309
-0.0002
THR 309
LEU 310
-0.0105
LEU 310
LEU 311
-0.0002
LEU 311
ILE 312
-0.0556
ILE 312
SER 313
0.0000
SER 313
GLU 314
-0.0091
GLU 314
LYS 315
0.0002
LYS 315
ILE 316
-0.0589
ILE 316
SER 317
0.0003
SER 317
VAL 318
-0.0251
VAL 318
ASP 319
0.0002
ASP 319
ILE 320
0.0161
ILE 320
THR 321
-0.0002
THR 321
LEU 322
-0.0123
LEU 322
ALA 323
0.0001
ALA 323
LEU 324
0.0004
LEU 324
GLU 325
0.0000
GLU 325
SER 326
-0.0363
SER 326
LYS 327
-0.0002
LYS 327
SER 328
-0.0604
SER 328
SER 329
0.0001
SER 329
TRP 330
0.0110
TRP 330
PRO 331
-0.0002
PRO 331
ALA 332
-0.0525
ALA 332
SER 333
0.0002
SER 333
THR 334
0.0260
THR 334
GLN 335
0.0004
GLN 335
GLU 336
-0.0366
GLU 336
GLY 337
0.0003
GLY 337
LEU 338
0.0003
LEU 338
ARG 339
0.0002
ARG 339
ILE 340
-0.0143
ILE 340
GLN 341
-0.0004
GLN 341
ASN 342
-0.0317
ASN 342
TRP 343
0.0001
TRP 343
LEU 344
0.0557
LEU 344
SER 345
-0.0003
SER 345
ALA 346
-0.0565
ALA 346
LYS 347
0.0001
LYS 347
VAL 348
-0.0374
VAL 348
ARG 349
0.0003
ARG 349
LYS 350
0.0269
LYS 350
GLN 351
-0.0000
GLN 351
LEU 352
-0.0396
LEU 352
ARG 353
-0.0002
ARG 353
LEU 354
-0.0073
LEU 354
LYS 355
0.0001
LYS 355
PRO 356
0.0405
PRO 356
PHE 357
-0.0001
PHE 357
TYR 358
-0.0041
TYR 358
LEU 359
-0.0005
LEU 359
VAL 360
0.0115
VAL 360
PRO 361
-0.0004
PRO 361
LYS 362
-0.0076
LYS 362
HIS 363
-0.0001
HIS 363
ALA 364
0.0272
ALA 364
LYS 365
-0.0001
LYS 365
GLU 366
0.0321
GLU 366
GLY 367
0.0001
GLY 367
ASN 368
-0.0223
ASN 368
GLY 369
0.0001
GLY 369
PHE 370
0.0467
PHE 370
GLN 371
-0.0000
GLN 371
GLU 372
-0.0111
GLU 372
GLU 373
0.0000
GLU 373
THR 374
0.0082
THR 374
TRP 375
-0.0001
TRP 375
ARG 376
0.0072
ARG 376
LEU 377
0.0000
LEU 377
SER 378
0.0232
SER 378
PHE 379
0.0001
PHE 379
SER 380
-0.0248
SER 380
HIS 381
0.0000
HIS 381
ILE 382
0.0049
ILE 382
GLU 383
-0.0001
GLU 383
LYS 384
-0.0056
LYS 384
GLU 385
-0.0001
GLU 385
ILE 386
0.0671
ILE 386
LEU 387
-0.0004
LEU 387
ASN 388
-0.0789
ASN 388
ASN 389
-0.0000
ASN 389
HIS 390
-0.0158
HIS 390
GLY 391
0.0001
GLY 391
LYS 392
0.0715
LYS 392
SER 393
-0.0000
SER 393
LYS 394
0.0104
LYS 394
THR 395
-0.0004
THR 395
CYS 396
-0.0224
CYS 396
CYS 397
0.0001
CYS 397
GLU 398
0.0229
GLU 398
ASN 399
-0.0001
ASN 399
LYS 400
0.1330
LYS 400
GLU 401
-0.0002
GLU 401
GLU 402
-0.1292
GLU 402
LYS 403
-0.0003
LYS 403
CYS 404
-0.0516
CYS 404
CYS 405
0.0002
CYS 405
ARG 406
0.0279
ARG 406
LYS 407
0.0000
LYS 407
ASP 408
-0.1041
ASP 408
CYS 409
0.0000
CYS 409
LEU 410
0.0359
LEU 410
LYS 411
-0.0001
LYS 411
LEU 412
-0.0054
LEU 412
MET 413
0.0003
MET 413
LYS 414
0.0887
LYS 414
TYR 415
0.0001
TYR 415
LEU 416
0.0653
LEU 416
LEU 417
0.0003
LEU 417
GLU 418
0.0273
GLU 418
GLN 419
0.0002
GLN 419
LEU 420
0.0334
LEU 420
LYS 421
-0.0001
LYS 421
GLU 422
-0.0092
GLU 422
ARG 423
0.0004
ARG 423
PHE 424
0.0144
PHE 424
LYS 425
0.0002
LYS 425
ASP 426
-0.0017
ASP 426
LYS 427
0.0000
LYS 427
LYS 428
-0.0021
LYS 428
HIS 429
0.0001
HIS 429
LEU 430
0.0033
LEU 430
ASP 431
-0.0002
ASP 431
LYS 432
-0.0263
LYS 432
PHE 433
0.0004
PHE 433
SER 434
0.0316
SER 434
SER 435
0.0004
SER 435
TYR 436
-0.0826
TYR 436
HIS 437
0.0000
HIS 437
VAL 438
-0.0210
VAL 438
LYS 439
-0.0001
LYS 439
THR 440
-0.0130
THR 440
ALA 441
-0.0000
ALA 441
PHE 442
-0.0140
PHE 442
PHE 443
-0.0001
PHE 443
HIS 444
0.0259
HIS 444
VAL 445
-0.0001
VAL 445
CYS 446
0.0050
CYS 446
THR 447
-0.0001
THR 447
GLN 448
0.0356
GLN 448
ASN 449
-0.0003
ASN 449
PRO 450
0.0184
PRO 450
GLN 451
-0.0001
GLN 451
ASP 452
-0.0986
ASP 452
SER 453
0.0002
SER 453
GLN 454
-0.0286
GLN 454
TRP 455
-0.0003
TRP 455
ASP 456
-0.1615
ASP 456
ARG 457
0.0000
ARG 457
LYS 458
0.0048
LYS 458
ASP 459
0.0002
ASP 459
LEU 460
0.0120
LEU 460
GLY 461
0.0001
GLY 461
LEU 462
0.0506
LEU 462
CYS 463
0.0002
CYS 463
PHE 464
-0.0114
PHE 464
ASP 465
-0.0002
ASP 465
ASN 466
0.0602
ASN 466
CYS 467
-0.0003
CYS 467
VAL 468
0.0029
VAL 468
THR 469
-0.0000
THR 469
TYR 470
0.0383
TYR 470
PHE 471
-0.0004
PHE 471
LEU 472
0.0326
LEU 472
GLN 473
0.0001
GLN 473
CYS 474
-0.0050
CYS 474
LEU 475
0.0001
LEU 475
ARG 476
0.0101
ARG 476
THR 477
-0.0002
THR 477
GLU 478
-0.0171
GLU 478
LYS 479
-0.0002
LYS 479
LEU 480
0.0424
LEU 480
GLU 481
-0.0004
GLU 481
ASN 482
0.0420
ASN 482
TYR 483
-0.0002
TYR 483
PHE 484
-0.0245
PHE 484
ILE 485
0.0001
ILE 485
PRO 486
0.0103
PRO 486
GLU 487
-0.0002
GLU 487
PHE 488
0.0599
PHE 488
ASN 489
0.0000
ASN 489
LEU 490
-0.0224
LEU 490
PHE 491
-0.0004
PHE 491
SER 492
0.0137
SER 492
SER 493
0.0000
SER 493
ASN 494
-0.0592
ASN 494
LEU 495
0.0001
LEU 495
ILE 496
-0.0886
ILE 496
ASP 497
-0.0000
ASP 497
LYS 498
-0.0191
LYS 498
ARG 499
-0.0001
ARG 499
SER 500
0.0137
SER 500
LYS 501
-0.0004
LYS 501
GLU 502
-0.0106
GLU 502
PHE 503
-0.0003
PHE 503
LEU 504
0.0025
LEU 504
THR 505
0.0001
THR 505
LYS 506
0.0072
LYS 506
GLN 507
0.0001
GLN 507
ILE 508
-0.0148
ILE 508
GLU 509
0.0002
GLU 509
TYR 510
0.0125
TYR 510
GLU 511
-0.0003
GLU 511
ARG 512
-0.0165
ARG 512
ASN 513
-0.0003
ASN 513
ASN 514
0.0074
ASN 514
GLU 515
0.0001
GLU 515
PHE 516
0.0038
PHE 516
PRO 517
-0.0002
PRO 517
VAL 518
0.0023
VAL 518
PHE 519
0.0002
PHE 519
ASP 520
-0.0167
ASP 520
GLU 521
-0.0003
GLU 521
PHE 522
-0.0020
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.