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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
0.0002
GLU 155
LEU 156
0.0574
LEU 156
ASP 157
-0.0001
ASP 157
ALA 158
-0.0699
ALA 158
ALA 159
0.0001
ALA 159
PRO 160
0.0263
PRO 160
GLY 161
0.0000
GLY 161
ALA 162
-0.0124
ALA 162
SER 163
0.0001
SER 163
LYS 164
0.1180
LYS 164
LEU 165
-0.0000
LEU 165
ARG 166
-0.0107
ARG 166
ALA 167
-0.0002
ALA 167
VAL 168
0.0200
VAL 168
LEU 169
0.0003
LEU 169
GLU 170
-0.0339
GLU 170
LYS 171
0.0001
LYS 171
LEU 172
-0.0028
LEU 172
LYS 173
0.0001
LYS 173
LEU 174
-0.0305
LEU 174
SER 175
-0.0000
SER 175
ARG 176
-0.0060
ARG 176
ASP 177
0.0000
ASP 177
ASP 178
0.0303
ASP 178
ILE 179
0.0002
ILE 179
SER 180
-0.0037
SER 180
THR 181
-0.0002
THR 181
ALA 182
-0.0229
ALA 182
ALA 183
0.0000
ALA 183
GLY 184
-0.0054
GLY 184
MET 185
-0.0002
MET 185
VAL 186
-0.0023
VAL 186
LYS 187
0.0002
LYS 187
GLY 188
0.0010
GLY 188
VAL 189
0.0002
VAL 189
VAL 190
0.0033
VAL 190
ASP 191
0.0000
ASP 191
HIS 192
0.0050
HIS 192
LEU 193
-0.0004
LEU 193
LEU 194
0.0032
LEU 194
LEU 195
-0.0002
LEU 195
ARG 196
-0.0026
ARG 196
LEU 197
0.0001
LEU 197
LYS 198
0.0020
LYS 198
CYS 199
0.0000
CYS 199
ASP 200
-0.0070
ASP 200
SER 201
-0.0001
SER 201
ALA 202
-0.0007
ALA 202
PHE 203
-0.0003
PHE 203
ARG 204
-0.0024
ARG 204
GLY 205
-0.0001
GLY 205
VAL 206
-0.0037
VAL 206
GLY 207
-0.0002
GLY 207
LEU 208
-0.0060
LEU 208
LEU 209
0.0002
LEU 209
ASN 210
0.0044
ASN 210
THR 211
-0.0000
THR 211
GLY 212
0.0013
GLY 212
SER 213
0.0004
SER 213
TYR 214
0.0070
TYR 214
TYR 215
-0.0001
TYR 215
GLU 216
0.0011
GLU 216
HIS 217
-0.0001
HIS 217
VAL 218
-0.0302
VAL 218
LYS 219
-0.0001
LYS 219
ILE 220
0.0272
ILE 220
SER 221
0.0001
SER 221
ALA 222
0.0112
ALA 222
PRO 223
-0.0002
PRO 223
ASN 224
0.0371
ASN 224
GLU 225
-0.0000
GLU 225
PHE 226
-0.0037
PHE 226
ASP 227
-0.0002
ASP 227
VAL 228
-0.0017
VAL 228
MET 229
-0.0001
MET 229
PHE 230
0.0033
PHE 230
LYS 231
0.0001
LYS 231
LEU 232
-0.0004
LEU 232
GLU 233
-0.0003
GLU 233
VAL 234
0.0002
VAL 234
PRO 235
-0.0000
PRO 235
ARG 236
0.0006
ARG 236
ILE 237
0.0005
ILE 237
GLN 238
0.0038
GLN 238
LEU 239
0.0001
LEU 239
GLU 240
0.0048
GLU 240
GLU 241
-0.0002
GLU 241
TYR 242
0.0014
TYR 242
SER 243
-0.0003
SER 243
ASN 244
-0.0094
ASN 244
THR 245
-0.0003
THR 245
ARG 246
-0.0062
ARG 246
ALA 247
-0.0001
ALA 247
TYR 248
-0.0095
TYR 248
TYR 249
-0.0000
TYR 249
PHE 250
-0.0071
PHE 250
VAL 251
-0.0001
VAL 251
LYS 252
0.0023
LYS 252
PHE 253
-0.0004
PHE 253
LYS 254
0.0028
LYS 254
ARG 255
0.0001
ARG 255
ASN 256
-0.0031
ASN 256
PRO 257
-0.0002
PRO 257
LYS 258
-0.0015
LYS 258
GLU 259
0.0000
GLU 259
ASN 260
-0.0041
ASN 260
PRO 261
0.0003
PRO 261
LEU 262
-0.0040
LEU 262
SER 263
-0.0001
SER 263
GLN 264
0.0062
GLN 264
PHE 265
0.0003
PHE 265
LEU 266
0.0012
LEU 266
GLU 267
-0.0006
GLU 267
GLY 268
0.0037
GLY 268
GLU 269
0.0001
GLU 269
ILE 270
0.0010
ILE 270
LEU 271
-0.0001
LEU 271
SER 272
0.0014
SER 272
ALA 273
-0.0002
ALA 273
SER 274
0.0023
SER 274
LYS 275
-0.0004
LYS 275
MET 276
0.0007
MET 276
LEU 277
-0.0001
LEU 277
SER 278
-0.0076
SER 278
LYS 279
-0.0003
LYS 279
PHE 280
0.0072
PHE 280
ARG 281
0.0003
ARG 281
LYS 282
0.0025
LYS 282
ILE 283
-0.0001
ILE 283
ILE 284
0.0072
ILE 284
LYS 285
0.0003
LYS 285
GLU 286
0.0021
GLU 286
GLU 287
0.0002
GLU 287
ILE 288
0.0031
ILE 288
ASN 289
-0.0001
ASN 289
ASP 290
0.0015
ASP 290
ILE 291
-0.0001
ILE 291
LYS 292
0.0086
LYS 292
ASP 293
-0.0001
ASP 293
THR 294
0.0042
THR 294
ASP 295
0.0003
ASP 295
VAL 296
-0.0051
VAL 296
ILE 297
0.0003
ILE 297
MET 298
-0.0098
MET 298
LYS 299
0.0002
LYS 299
ARG 300
0.0046
ARG 300
LYS 301
0.0001
LYS 301
ARG 302
0.0011
ARG 302
GLY 303
0.0001
GLY 303
GLY 304
-0.0059
GLY 304
SER 305
-0.0003
SER 305
PRO 306
0.0016
PRO 306
ALA 307
-0.0001
ALA 307
VAL 308
-0.0109
VAL 308
THR 309
0.0003
THR 309
LEU 310
-0.0087
LEU 310
LEU 311
-0.0000
LEU 311
ILE 312
-0.0019
ILE 312
SER 313
-0.0002
SER 313
GLU 314
0.0119
GLU 314
LYS 315
0.0004
LYS 315
ILE 316
-0.0085
ILE 316
SER 317
0.0002
SER 317
VAL 318
-0.0045
VAL 318
ASP 319
0.0001
ASP 319
ILE 320
0.0086
ILE 320
THR 321
0.0004
THR 321
LEU 322
0.0115
LEU 322
ALA 323
-0.0000
ALA 323
LEU 324
0.0009
LEU 324
GLU 325
0.0002
GLU 325
SER 326
-0.0025
SER 326
LYS 327
-0.0004
LYS 327
SER 328
0.0052
SER 328
SER 329
0.0000
SER 329
TRP 330
-0.0002
TRP 330
PRO 331
-0.0001
PRO 331
ALA 332
0.0020
ALA 332
SER 333
0.0001
SER 333
THR 334
-0.0080
THR 334
GLN 335
0.0001
GLN 335
GLU 336
-0.0090
GLU 336
GLY 337
-0.0001
GLY 337
LEU 338
0.0000
LEU 338
ARG 339
0.0000
ARG 339
ILE 340
-0.0084
ILE 340
GLN 341
-0.0002
GLN 341
ASN 342
-0.0251
ASN 342
TRP 343
-0.0001
TRP 343
LEU 344
0.0006
LEU 344
SER 345
0.0000
SER 345
ALA 346
-0.0116
ALA 346
LYS 347
0.0002
LYS 347
VAL 348
0.0018
VAL 348
ARG 349
-0.0001
ARG 349
LYS 350
0.0036
LYS 350
GLN 351
0.0000
GLN 351
LEU 352
0.0001
LEU 352
ARG 353
0.0002
ARG 353
LEU 354
0.0072
LEU 354
LYS 355
-0.0001
LYS 355
PRO 356
0.0015
PRO 356
PHE 357
-0.0002
PHE 357
TYR 358
-0.0016
TYR 358
LEU 359
0.0003
LEU 359
VAL 360
-0.0066
VAL 360
PRO 361
0.0000
PRO 361
LYS 362
-0.0020
LYS 362
HIS 363
-0.0001
HIS 363
ALA 364
-0.0065
ALA 364
LYS 365
-0.0003
LYS 365
GLU 366
-0.0132
GLU 366
GLY 367
0.0001
GLY 367
ASN 368
-0.0045
ASN 368
GLY 369
0.0003
GLY 369
PHE 370
-0.0086
PHE 370
GLN 371
0.0000
GLN 371
GLU 372
-0.0144
GLU 372
GLU 373
0.0002
GLU 373
THR 374
-0.0058
THR 374
TRP 375
-0.0001
TRP 375
ARG 376
-0.0013
ARG 376
LEU 377
-0.0002
LEU 377
SER 378
0.0238
SER 378
PHE 379
0.0003
PHE 379
SER 380
0.0095
SER 380
HIS 381
0.0002
HIS 381
ILE 382
0.0103
ILE 382
GLU 383
0.0003
GLU 383
LYS 384
0.0054
LYS 384
GLU 385
0.0004
GLU 385
ILE 386
0.0169
ILE 386
LEU 387
-0.0000
LEU 387
ASN 388
-0.0157
ASN 388
ASN 389
-0.0003
ASN 389
HIS 390
-0.0028
HIS 390
GLY 391
-0.0003
GLY 391
LYS 392
0.0053
LYS 392
SER 393
-0.0005
SER 393
LYS 394
0.0049
LYS 394
THR 395
-0.0001
THR 395
CYS 396
-0.0067
CYS 396
CYS 397
0.0001
CYS 397
GLU 398
-0.0045
GLU 398
ASN 399
0.0000
ASN 399
LYS 400
0.0090
LYS 400
GLU 401
-0.0001
GLU 401
GLU 402
-0.0047
GLU 402
LYS 403
-0.0001
LYS 403
CYS 404
-0.0042
CYS 404
CYS 405
-0.0000
CYS 405
ARG 406
0.0106
ARG 406
LYS 407
0.0004
LYS 407
ASP 408
-0.0114
ASP 408
CYS 409
0.0001
CYS 409
LEU 410
0.0020
LEU 410
LYS 411
-0.0001
LYS 411
LEU 412
-0.0008
LEU 412
MET 413
0.0002
MET 413
LYS 414
-0.0081
LYS 414
TYR 415
-0.0002
TYR 415
LEU 416
-0.0065
LEU 416
LEU 417
-0.0000
LEU 417
GLU 418
-0.0189
GLU 418
GLN 419
-0.0001
GLN 419
LEU 420
-0.0135
LEU 420
LYS 421
-0.0003
LYS 421
GLU 422
0.0120
GLU 422
ARG 423
-0.0002
ARG 423
PHE 424
0.0101
PHE 424
LYS 425
-0.0000
LYS 425
ASP 426
-0.0004
ASP 426
LYS 427
-0.0002
LYS 427
LYS 428
-0.0005
LYS 428
HIS 429
0.0002
HIS 429
LEU 430
-0.0039
LEU 430
ASP 431
-0.0002
ASP 431
LYS 432
0.0214
LYS 432
PHE 433
-0.0002
PHE 433
SER 434
-0.0254
SER 434
SER 435
-0.0000
SER 435
TYR 436
0.0145
TYR 436
HIS 437
0.0005
HIS 437
VAL 438
0.0153
VAL 438
LYS 439
-0.0001
LYS 439
THR 440
0.0040
THR 440
ALA 441
0.0002
ALA 441
PHE 442
0.0044
PHE 442
PHE 443
-0.0001
PHE 443
HIS 444
0.0065
HIS 444
VAL 445
-0.0004
VAL 445
CYS 446
0.0118
CYS 446
THR 447
0.0002
THR 447
GLN 448
-0.0003
GLN 448
ASN 449
-0.0000
ASN 449
PRO 450
0.0150
PRO 450
GLN 451
-0.0002
GLN 451
ASP 452
-0.0142
ASP 452
SER 453
0.0002
SER 453
GLN 454
-0.0062
GLN 454
TRP 455
-0.0003
TRP 455
ASP 456
-0.0429
ASP 456
ARG 457
0.0006
ARG 457
LYS 458
-0.0514
LYS 458
ASP 459
0.0001
ASP 459
LEU 460
-0.0042
LEU 460
GLY 461
-0.0003
GLY 461
LEU 462
0.0458
LEU 462
CYS 463
-0.0002
CYS 463
PHE 464
-0.0094
PHE 464
ASP 465
0.0001
ASP 465
ASN 466
0.0252
ASN 466
CYS 467
-0.0002
CYS 467
VAL 468
0.0047
VAL 468
THR 469
0.0002
THR 469
TYR 470
0.0031
TYR 470
PHE 471
-0.0001
PHE 471
LEU 472
0.0114
LEU 472
GLN 473
0.0000
GLN 473
CYS 474
-0.0027
CYS 474
LEU 475
-0.0001
LEU 475
ARG 476
0.0039
ARG 476
THR 477
-0.0001
THR 477
GLU 478
-0.0093
GLU 478
LYS 479
-0.0000
LYS 479
LEU 480
0.0139
LEU 480
GLU 481
0.0002
GLU 481
ASN 482
0.0051
ASN 482
TYR 483
-0.0001
TYR 483
PHE 484
-0.0143
PHE 484
ILE 485
0.0002
ILE 485
PRO 486
-0.0060
PRO 486
GLU 487
-0.0001
GLU 487
PHE 488
0.0143
PHE 488
ASN 489
-0.0000
ASN 489
LEU 490
0.0270
LEU 490
PHE 491
0.0001
PHE 491
SER 492
-0.0168
SER 492
SER 493
0.0002
SER 493
ASN 494
-0.0345
ASN 494
LEU 495
0.0001
LEU 495
ILE 496
0.0213
ILE 496
ASP 497
0.0001
ASP 497
LYS 498
-0.0060
LYS 498
ARG 499
0.0000
ARG 499
SER 500
-0.0078
SER 500
LYS 501
0.0000
LYS 501
GLU 502
0.0023
GLU 502
PHE 503
-0.0001
PHE 503
LEU 504
-0.0037
LEU 504
THR 505
-0.0001
THR 505
LYS 506
0.0033
LYS 506
GLN 507
0.0003
GLN 507
ILE 508
-0.0030
ILE 508
GLU 509
-0.0002
GLU 509
TYR 510
0.0021
TYR 510
GLU 511
-0.0000
GLU 511
ARG 512
-0.0043
ARG 512
ASN 513
0.0001
ASN 513
ASN 514
0.0027
ASN 514
GLU 515
-0.0000
GLU 515
PHE 516
-0.0007
PHE 516
PRO 517
0.0001
PRO 517
VAL 518
0.0006
VAL 518
PHE 519
0.0001
PHE 519
ASP 520
-0.0054
ASP 520
GLU 521
-0.0000
GLU 521
PHE 522
-0.0022
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.