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
ASN 34
GLY 35
0.0003
GLY 35
LEU 36
-0.0000
LEU 36
THR 37
0.0043
THR 37
TYR 38
-0.0000
TYR 38
CYS 39
-0.0005
CYS 39
THR 40
-0.0369
THR 40
HIS 41
0.0001
HIS 41
ALA 42
0.0000
ALA 42
SER 43
0.0329
SER 43
GLY 44
0.0001
GLY 44
PHE 45
-0.0000
PHE 45
SER 46
0.0111
SER 46
PHE 47
-0.0004
PHE 47
ASN 48
0.0001
ASN 48
PRO 49
-0.0241
PRO 49
GLN 50
-0.0002
GLN 50
THR 51
0.0000
THR 51
ALA 52
-0.0032
ALA 52
ASP 53
-0.0001
ASP 53
ALA 54
0.0001
ALA 54
GLY 55
0.1480
GLY 55
THR 56
-0.0001
THR 56
SER 57
0.0001
SER 57
MET 58
-0.0236
MET 58
ASN 59
0.0002
ASN 59
VAL 60
-0.0001
VAL 60
VAL 61
-0.0112
VAL 61
THR 62
-0.0002
THR 62
GLU 63
0.0001
GLU 63
GLN 64
0.0077
GLN 64
ILE 65
0.0002
ILE 65
TYR 66
0.0000
TYR 66
ASN 67
0.0317
ASN 67
LYS 68
0.0001
LYS 68
LEU 69
0.0001
LEU 69
PHE 70
-0.0375
PHE 70
ASP 71
0.0001
ASP 71
ILE 72
0.0001
ILE 72
LYS 73
0.0166
LYS 73
ASN 74
0.0001
ASN 74
HIS 75
0.0001
HIS 75
SER 76
0.0010
SER 76
ALA 77
-0.0002
ALA 77
THR 78
0.0000
THR 78
LEU 79
0.0200
LEU 79
THR 80
0.0004
THR 80
PRO 81
0.0000
PRO 81
MET 82
-0.0024
MET 82
LEU 83
-0.0001
LEU 83
ALA 84
-0.0000
ALA 84
GLN 85
-0.0176
GLN 85
SER 86
0.0000
SER 86
TYR 87
-0.0000
TYR 87
SER 88
0.0495
SER 88
ILE 89
0.0004
ILE 89
SER 90
-0.0002
SER 90
ALA 91
0.0058
ALA 91
ASP 92
-0.0000
ASP 92
GLY 93
-0.0001
GLY 93
LYS 94
-0.0174
LYS 94
GLU 95
0.0003
GLU 95
ILE 96
-0.0001
ILE 96
LEU 97
0.0500
LEU 97
LEU 98
0.0001
LEU 98
ASN 99
0.0002
ASN 99
LEU 100
0.0428
LEU 100
ARG 101
0.0000
ARG 101
HIS 102
0.0001
HIS 102
GLY 103
0.0270
GLY 103
VAL 104
-0.0004
VAL 104
LYS 105
0.0003
LYS 105
PHE 106
0.0245
PHE 106
HIS 107
0.0002
HIS 107
GLN 108
-0.0003
GLN 108
THR 109
0.0131
THR 109
PRO 110
0.0002
PRO 110
TRP 111
-0.0002
TRP 111
PHE 112
0.0029
PHE 112
THR 113
0.0000
THR 113
PRO 114
-0.0001
PRO 114
THR 115
0.0035
THR 115
ARG 116
-0.0000
ARG 116
ASP 117
0.0001
ASP 117
PHE 118
-0.0044
PHE 118
ASN 119
-0.0002
ASN 119
ALA 120
-0.0003
ALA 120
GLU 121
-0.0099
GLU 121
ASP 122
0.0002
ASP 122
VAL 123
0.0004
VAL 123
VAL 124
-0.0040
VAL 124
PHE 125
-0.0001
PHE 125
SER 126
0.0001
SER 126
ILE 127
-0.0101
ILE 127
ASN 128
-0.0001
ASN 128
ARG 129
0.0000
ARG 129
VAL 130
0.0040
VAL 130
LEU 131
0.0001
LEU 131
GLY 132
-0.0003
GLY 132
HIS 133
0.0162
HIS 133
ASN 134
-0.0002
ASN 134
THR 135
0.0001
THR 135
TYR 136
-0.0689
TYR 136
LEU 137
0.0001
LEU 137
PRO 138
-0.0003
PRO 138
THR 139
-0.0021
THR 139
LEU 140
-0.0001
LEU 140
ALA 141
0.0000
ALA 141
GLU 142
0.0003
GLU 142
ALA 143
0.0002
ALA 143
ASN 144
-0.0004
ASN 144
VAL 145
-0.0298
VAL 145
THR 146
-0.0003
THR 146
TYR 147
0.0004
TYR 147
SER 148
-0.0014
SER 148
ASN 149
0.0003
ASN 149
PRO 150
0.0002
PRO 150
GLN 151
0.0345
GLN 151
TYR 152
0.0004
TYR 152
ARG 153
-0.0003
ARG 153
VAL 154
0.0393
VAL 154
PHE 155
0.0001
PHE 155
HIS 156
-0.0002
HIS 156
GLU 157
-0.0487
GLU 157
GLN 158
0.0001
GLN 158
ALA 159
-0.0004
ALA 159
ARG 160
-0.0094
ARG 160
LYS 161
-0.0002
LYS 161
VAL 162
0.0002
VAL 162
ARG 163
-0.0631
ARG 163
PHE 164
-0.0001
PHE 164
PRO 165
-0.0001
PRO 165
TYR 166
0.0475
TYR 166
PHE 167
0.0001
PHE 167
ASP 168
-0.0001
ASP 168
SER 169
-0.1200
SER 169
ILE 170
-0.0002
ILE 170
LYS 171
0.0001
LYS 171
LEU 172
0.1466
LEU 172
ASN 173
-0.0003
ASN 173
GLU 174
-0.0000
GLU 174
LYS 175
-0.0272
LYS 175
ILE 176
0.0003
ILE 176
LYS 177
0.0001
LYS 177
SER 178
0.0445
SER 178
VAL 179
0.0002
VAL 179
THR 180
-0.0004
THR 180
ALA 181
0.0285
ALA 181
LEU 182
0.0001
LEU 182
SER 183
0.0002
SER 183
PRO 184
0.0054
PRO 184
TYR 185
0.0001
TYR 185
GLN 186
0.0003
GLN 186
VAL 187
0.0248
VAL 187
LYS 188
-0.0003
LYS 188
ILE 189
0.0000
ILE 189
GLU 190
0.0251
GLU 190
LEU 191
-0.0001
LEU 191
PHE 192
-0.0002
PHE 192
ALA 193
-0.0917
ALA 193
PRO 194
0.0003
PRO 194
ASP 195
-0.0003
ASP 195
SER 196
-0.0858
SER 196
SER 197
0.0001
SER 197
ILE 198
-0.0002
ILE 198
LEU 199
0.0378
LEU 199
SER 200
0.0001
SER 200
HIS 201
-0.0000
HIS 201
LEU 202
0.0132
LEU 202
ALA 203
0.0001
ALA 203
SER 204
-0.0000
SER 204
GLN 205
-0.0059
GLN 205
TYR 206
0.0001
TYR 206
ALA 207
0.0002
ALA 207
ILE 208
0.0103
ILE 208
ILE 209
0.0001
ILE 209
PHE 210
-0.0001
PHE 210
SER 211
0.0132
SER 211
GLN 212
0.0002
GLN 212
GLU 213
-0.0002
GLU 213
TYR 214
-0.0022
TYR 214
ALA 215
-0.0002
ALA 215
TYR 216
-0.0001
TYR 216
GLN 217
-0.0222
GLN 217
LEU 218
-0.0002
LEU 218
SER 219
0.0002
SER 219
ALA 220
0.0001
ALA 220
ASP 221
-0.0003
ASP 221
ASP 222
0.0001
ASP 222
ASN 223
0.0080
ASN 223
LEU 224
-0.0000
LEU 224
ALA 225
0.0001
ALA 225
GLN 226
0.0023
GLN 226
LEU 227
-0.0001
LEU 227
ASP 228
0.0000
ASP 228
THR 229
-0.0242
THR 229
HIS 230
0.0003
HIS 230
PRO 231
0.0001
PRO 231
VAL 232
0.0128
VAL 232
GLY 233
0.0001
GLY 233
THR 234
-0.0005
THR 234
GLY 235
0.0055
GLY 235
PRO 236
0.0001
PRO 236
TYR 237
-0.0002
TYR 237
GLN 238
-0.0133
GLN 238
VAL 239
0.0002
VAL 239
LYS 240
-0.0003
LYS 240
ASP 241
0.0171
ASP 241
TYR 242
0.0001
TYR 242
VAL 243
0.0001
VAL 243
TYR 244
-0.0433
TYR 244
ASN 245
0.0003
ASN 245
GLN 246
-0.0001
GLN 246
TYR 247
-0.0231
TYR 247
VAL 248
-0.0001
VAL 248
ARG 249
0.0001
ARG 249
LEU 250
0.0124
LEU 250
VAL 251
-0.0003
VAL 251
ARG 252
-0.0000
ARG 252
ASN 253
0.0124
ASN 253
GLU 254
-0.0004
GLU 254
ASN 255
0.0000
ASN 255
TYR 256
0.0277
TYR 256
TRP 257
-0.0002
TRP 257
LYS 258
0.0002
LYS 258
LYS 259
0.0453
LYS 259
GLU 260
0.0000
GLU 260
ALA 261
0.0002
ALA 261
LYS 262
0.0370
LYS 262
ILE 263
0.0002
ILE 263
GLU 264
-0.0002
GLU 264
HIS 265
0.0021
HIS 265
ILE 266
-0.0002
ILE 266
ILE 267
0.0003
ILE 267
VAL 268
0.0049
VAL 268
ASP 269
-0.0004
ASP 269
LEU 270
-0.0002
LEU 270
SER 271
-0.0244
SER 271
THR 272
-0.0004
THR 272
ASP 273
-0.0001
ASP 273
ARG 274
0.0938
ARG 274
SER 275
0.0005
SER 275
GLY 276
0.0001
GLY 276
ARG 277
0.0540
ARG 277
LEU 278
-0.0001
LEU 278
VAL 279
-0.0004
VAL 279
LYS 280
0.0149
LYS 280
PHE 281
-0.0002
PHE 281
PHE 282
-0.0000
PHE 282
ASN 283
0.0122
ASN 283
ASN 284
0.0000
ASN 284
GLU 285
0.0001
GLU 285
CYS 286
0.0131
CYS 286
GLN 287
0.0004
GLN 287
ILE 288
-0.0001
ILE 288
ALA 289
-0.1328
ALA 289
SER 290
0.0002
SER 290
TYR 291
-0.0005
TYR 291
PRO 292
-0.0539
PRO 292
GLU 293
0.0003
GLU 293
VAL 294
-0.0001
VAL 294
SER 295
0.0764
SER 295
GLN 296
0.0000
GLN 296
ILE 297
-0.0001
ILE 297
GLY 298
0.0013
GLY 298
LEU 299
0.0003
LEU 299
LEU 300
-0.0000
LEU 300
LYS 301
0.0005
LYS 301
ASN 302
-0.0003
ASN 302
ASP 303
0.0003
ASP 303
ASP 304
-0.0223
ASP 304
LYS 305
0.0000
LYS 305
HIS 306
0.0001
HIS 306
TYR 307
0.0377
TYR 307
TYR 308
-0.0004
TYR 308
MET 309
-0.0000
MET 309
GLN 310
0.1490
GLN 310
SER 311
-0.0004
SER 311
THR 312
0.0002
THR 312
ASP 313
0.2151
ASP 313
GLY 314
-0.0001
GLY 314
MET 315
0.0002
MET 315
ASN 316
-0.0130
ASN 316
LEU 317
0.0003
LEU 317
ALA 318
-0.0002
ALA 318
TYR 319
-0.0713
TYR 319
LEU 320
-0.0003
LEU 320
ALA 321
0.0002
ALA 321
PHE 322
-0.0355
PHE 322
ASN 323
-0.0002
ASN 323
PHE 324
0.0000
PHE 324
ASP 325
0.0289
ASP 325
LYS 326
0.0005
LYS 326
PRO 327
-0.0002
PRO 327
LEU 328
0.0210
LEU 328
MET 329
-0.0003
MET 329
ARG 330
-0.0000
ARG 330
ASP 331
-0.0009
ASP 331
HIS 332
-0.0000
HIS 332
GLU 333
0.0001
GLU 333
ILE 334
-0.0011
ILE 334
ARG 335
-0.0003
ARG 335
ALA 336
0.0002
ALA 336
ALA 337
0.0027
ALA 337
ILE 338
0.0002
ILE 338
SER 339
-0.0002
SER 339
GLN 340
0.0080
GLN 340
SER 341
-0.0003
SER 341
LEU 342
-0.0000
LEU 342
ASN 343
0.0061
ASN 343
ARG 344
-0.0000
ARG 344
ALA 345
0.0002
ALA 345
ARG 346
0.0190
ARG 346
ILE 347
0.0002
ILE 347
ILE 348
-0.0001
ILE 348
HIS 349
-0.0090
HIS 349
SER 350
-0.0004
SER 350
ILE 351
0.0000
ILE 351
TYR 352
-0.1519
TYR 352
HIS 353
-0.0002
HIS 353
ASN 354
0.0001
ASN 354
THR 355
-0.0482
THR 355
ALA 356
-0.0003
ALA 356
THR 357
0.0005
THR 357
VAL 358
0.0743
VAL 358
ALA 359
-0.0000
ALA 359
ASN 360
0.0002
ASN 360
ASN 361
-0.0439
ASN 361
ILE 362
-0.0002
ILE 362
ILE 363
0.0001
ILE 363
PRO 364
0.0297
PRO 364
GLU 365
-0.0002
GLU 365
VAL 366
-0.0001
VAL 366
SER 367
0.0585
SER 367
TRP 368
-0.0002
TRP 368
ALA 369
0.0000
ALA 369
SER 370
-0.0586
SER 370
THR 371
-0.0002
THR 371
VAL 372
0.0000
VAL 372
ASN 373
-0.0763
ASN 373
THR 374
0.0003
THR 374
PRO 375
0.0002
PRO 375
GLU 376
-0.0665
GLU 376
PHE 377
0.0001
PHE 377
GLU 378
0.0000
GLU 378
PHE 379
-0.0277
PHE 379
ASP 380
-0.0004
ASP 380
TYR 381
0.0002
TYR 381
HIS 382
-0.0151
HIS 382
PRO 383
0.0002
PRO 383
LYS 384
-0.0000
LYS 384
ILE 385
0.0065
ILE 385
ALA 386
-0.0001
ALA 386
LYS 387
-0.0001
LYS 387
ASN 388
0.0034
ASN 388
LYS 389
-0.0003
LYS 389
LEU 390
0.0000
LEU 390
ALA 391
0.0012
ALA 391
ASP 392
0.0001
ASP 392
LYS 393
0.0001
LYS 393
ASN 394
-0.0024
ASN 394
LEU 395
0.0001
LEU 395
LEU 396
-0.0002
LEU 396
LEU 397
0.0248
LEU 397
ASN 398
-0.0003
ASN 398
LEU 399
0.0004
LEU 399
TRP 400
0.0409
TRP 400
VAL 401
-0.0001
VAL 401
ILE 402
0.0004
ILE 402
ASN 403
-0.0600
ASN 403
GLU 404
0.0000
GLU 404
GLU 405
-0.0001
GLU 405
GLN 406
-0.0698
GLN 406
VAL 407
0.0003
VAL 407
TYR 408
0.0003
TYR 408
ASN 409
-0.0174
ASN 409
PRO 410
0.0001
PRO 410
ALA 411
-0.0001
ALA 411
PRO 412
-0.1957
PRO 412
PHE 413
-0.0002
PHE 413
LYS 414
0.0002
LYS 414
MET 415
0.0475
MET 415
ALA 416
-0.0004
ALA 416
GLU 417
-0.0003
GLU 417
MET 418
0.0271
MET 418
ILE 419
0.0001
ILE 419
LYS 420
0.0003
LYS 420
TRP 421
0.0316
TRP 421
ASP 422
-0.0000
ASP 422
LEU 423
0.0001
LEU 423
ALA 424
-0.0003
ALA 424
GLN 425
0.0002
GLN 425
ALA 426
-0.0001
ALA 426
GLY 427
-0.0015
GLY 427
VAL 428
0.0001
VAL 428
LYS 429
-0.0001
LYS 429
VAL 430
0.0437
VAL 430
LYS 431
-0.0000
LYS 431
VAL 432
-0.0001
VAL 432
ARG 433
0.0897
ARG 433
ALA 434
0.0001
ALA 434
VAL 435
-0.0000
VAL 435
THR 436
0.2176
THR 436
ARG 437
0.0002
ARG 437
PRO 438
0.0001
PRO 438
PHE 439
0.0390
PHE 439
LEU 440
-0.0003
LEU 440
THR 441
-0.0000
THR 441
ALA 442
0.0833
ALA 442
GLN 443
0.0003
GLN 443
LEU 444
-0.0002
LEU 444
ARG 445
-0.0391
ARG 445
ASN 446
0.0001
ASN 446
GLN 447
-0.0001
GLN 447
SER 448
-0.0097
SER 448
GLU 449
-0.0003
GLU 449
ASN 450
-0.0000
ASN 450
TYR 451
-0.0120
TYR 451
ASP 452
0.0000
ASP 452
LEU 453
0.0000
LEU 453
ILE 454
-0.0324
ILE 454
LEU 455
-0.0001
LEU 455
SER 456
-0.0000
SER 456
GLY 457
-0.0142
GLY 457
TRP 458
-0.0002
TRP 458
LEU 459
-0.0001
LEU 459
ALA 460
-0.0144
ALA 460
GLY 461
-0.0002
GLY 461
ASN 462
-0.0002
ASN 462
LEU 463
-0.0038
LEU 463
ASP 464
-0.0004
ASP 464
PRO 465
0.0002
PRO 465
ASP 466
0.0275
ASP 466
GLY 467
0.0001
GLY 467
PHE 468
-0.0002
PHE 468
MET 469
0.0325
MET 469
ARG 470
-0.0001
ARG 470
PRO 471
0.0002
PRO 471
ILE 472
0.0348
ILE 472
LEU 473
0.0003
LEU 473
SER 474
-0.0005
SER 474
CYS 475
0.0130
CYS 475
GLY 476
-0.0002
GLY 476
THR 477
-0.0002
THR 477
LYS 478
0.0695
LYS 478
ASN 479
0.0003
ASN 479
GLU 480
-0.0001
GLU 480
LEU 481
0.0178
LEU 481
THR 482
-0.0001
THR 482
ASN 483
-0.0004
ASN 483
LEU 484
0.0724
LEU 484
SER 485
-0.0003
SER 485
ASN 486
0.0003
ASN 486
TRP 487
0.0400
TRP 487
CYS 488
0.0002
CYS 488
ASN 489
0.0002
ASN 489
GLU 490
0.0523
GLU 490
GLU 491
-0.0003
GLU 491
PHE 492
0.0002
PHE 492
ASP 493
-0.0047
ASP 493
GLN 494
0.0004
GLN 494
PHE 495
-0.0003
PHE 495
MET 496
-0.0167
MET 496
ASP 497
-0.0003
ASP 497
ARG 498
0.0000
ARG 498
ALA 499
0.0318
ALA 499
ILE 500
-0.0003
ILE 500
THR 501
0.0001
THR 501
THR 502
-0.0209
THR 502
SER 503
0.0001
SER 503
HIS 504
-0.0000
HIS 504
LEU 505
-0.0281
LEU 505
SER 506
0.0000
SER 506
SER 507
0.0002
SER 507
ARG 508
-0.0035
ARG 508
ALA 509
-0.0002
ALA 509
LYS 510
0.0001
LYS 510
ALA 511
0.0163
ALA 511
TYR 512
0.0001
TYR 512
ASN 513
0.0000
ASN 513
GLU 514
0.0314
GLU 514
ALA 515
0.0003
ALA 515
GLN 516
0.0000
GLN 516
GLU 517
0.0216
GLU 517
LEU 518
0.0002
LEU 518
VAL 519
-0.0002
VAL 519
LEU 520
-0.0081
LEU 520
ARG 521
-0.0002
ARG 521
GLU 522
0.0002
GLU 522
LEU 523
-0.0162
LEU 523
PRO 524
0.0002
PRO 524
ILE 525
0.0002
ILE 525
ILE 526
0.0249
ILE 526
PRO 527
-0.0001
PRO 527
ILE 528
0.0002
ILE 528
ALA 529
-0.0439
ALA 529
ASN 530
-0.0000
ASN 530
VAL 531
-0.0001
VAL 531
LYS 532
-0.0034
LYS 532
ARG 533
0.0001
ARG 533
ILE 534
0.0005
ILE 534
LEU 535
0.0082
LEU 535
VAL 536
0.0005
VAL 536
ALA 537
-0.0000
ALA 537
ASN 538
-0.0021
ASN 538
SER 539
0.0001
SER 539
ARG 540
0.0000
ARG 540
VAL 541
0.0324
VAL 541
LYS 542
-0.0000
LYS 542
GLY 543
0.0004
GLY 543
VAL 544
-0.0382
VAL 544
LYS 545
0.0003
LYS 545
MET 546
-0.0000
MET 546
THR 547
0.1589
THR 547
PRO 548
-0.0003
PRO 548
PHE 549
0.0001
PHE 549
GLY 550
-0.0238
GLY 550
SER 551
-0.0004
SER 551
LEU 552
0.0001
LEU 552
ASP 553
-0.0539
ASP 553
PHE 554
0.0005
PHE 554
SER 555
-0.0001
SER 555
THR 556
-0.0011
THR 556
LEU 557
0.0002
LEU 557
TYR 558
0.0000
TYR 558
PHE 559
0.0266
PHE 559
ILE 560
0.0001
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.