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
MET 1
GLU 2
0.0003
GLU 2
GLU 3
0.0000
GLU 3
LEU 4
0.1180
LEU 4
LYS 5
0.0001
LYS 5
SER 6
-0.0000
SER 6
TYR 7
0.1429
TYR 7
TYR 8
0.0000
TYR 8
LYS 9
0.0004
LYS 9
ARG 10
0.0029
ARG 10
VAL 11
0.0002
VAL 11
ALA 12
-0.0002
ALA 12
LYS 13
0.0663
LYS 13
TYR 14
-0.0000
TYR 14
TYR 15
-0.0004
TYR 15
SER 16
0.0772
SER 16
ALA 17
-0.0001
ALA 17
ALA 18
0.0004
ALA 18
ALA 19
0.0076
ALA 19
LEU 20
-0.0001
LEU 20
LEU 21
0.0004
LEU 21
TYR 22
0.0045
TYR 22
TRP 23
-0.0005
TRP 23
ASP 24
0.0003
ASP 24
MET 25
0.0168
MET 25
GLN 26
-0.0002
GLN 26
THR 27
0.0002
THR 27
TYR 28
0.0229
TYR 28
MET 29
-0.0000
MET 29
PRO 30
0.0001
PRO 30
LYS 31
0.2847
LYS 31
ASP 32
0.0000
ASP 32
ALA 33
-0.0001
ALA 33
GLY 34
0.0169
GLY 34
PRO 35
-0.0001
PRO 35
TYR 36
0.0001
TYR 36
ARG 37
0.0895
ARG 37
ALA 38
-0.0003
ALA 38
GLU 39
-0.0002
GLU 39
VAL 40
0.1118
VAL 40
LEU 41
-0.0001
LEU 41
SER 42
0.0001
SER 42
GLU 43
0.0871
GLU 43
ILE 44
-0.0000
ILE 44
GLY 45
-0.0002
GLY 45
THR 46
0.0240
THR 46
TYR 47
0.0002
TYR 47
ALA 48
-0.0000
ALA 48
PHE 49
0.0038
PHE 49
LYS 50
0.0001
LYS 50
GLN 51
0.0002
GLN 51
ILE 52
0.0230
ILE 52
THR 53
0.0000
THR 53
ASP 54
-0.0001
ASP 54
ASP 55
-0.1947
ASP 55
ALA 56
0.0001
ALA 56
LEU 57
0.0002
LEU 57
GLY 58
-0.1417
GLY 58
LYS 59
-0.0003
LYS 59
LEU 60
-0.0001
LEU 60
LEU 61
0.1071
LEU 61
GLU 62
0.0003
GLU 62
THR 63
-0.0001
THR 63
ALA 64
0.0196
ALA 64
GLN 65
-0.0003
GLN 65
PRO 66
0.0000
PRO 66
GLN 67
0.0373
GLN 67
SER 68
-0.0002
SER 68
GLU 69
0.0003
GLU 69
ILE 70
-0.0351
ILE 70
ASP 71
0.0003
ASP 71
GLU 72
0.0001
GLU 72
LYS 73
0.1834
LYS 73
LEU 74
-0.0002
LEU 74
VAL 75
-0.0001
VAL 75
TYR 76
0.1929
TYR 76
VAL 77
-0.0001
VAL 77
GLY 78
-0.0001
GLY 78
LYS 79
-0.0997
LYS 79
LYS 80
-0.0004
LYS 80
GLU 81
-0.0002
GLU 81
TYR 82
0.0896
TYR 82
TYR 83
0.0004
TYR 83
LYS 84
0.0000
LYS 84
TYR 85
0.0134
TYR 85
LYS 86
-0.0001
LYS 86
LYS 87
0.0002
LYS 87
VAL 88
-0.0253
VAL 88
PRO 89
0.0002
PRO 89
PRO 90
0.0003
PRO 90
GLU 91
-0.0568
GLU 91
LEU 92
-0.0000
LEU 92
PHE 93
0.0005
PHE 93
GLN 94
0.0195
GLN 94
GLU 95
-0.0002
GLU 95
ILE 96
0.0000
ILE 96
MET 97
-0.1171
MET 97
ILE 98
0.0001
ILE 98
THR 99
0.0001
THR 99
SER 100
0.0166
SER 100
THR 101
-0.0000
THR 101
MET 102
-0.0004
MET 102
LEU 103
-0.0347
LEU 103
GLU 104
0.0003
GLU 104
GLN 105
0.0001
GLN 105
LYS 106
-0.0058
LYS 106
TRP 107
0.0002
TRP 107
GLU 108
-0.0001
GLU 108
ILE 109
0.0142
ILE 109
ALA 110
0.0002
ALA 110
LYS 111
-0.0002
LYS 111
PRO 112
0.0132
PRO 112
ARG 113
-0.0002
ARG 113
GLY 114
-0.0003
GLY 114
ASP 115
0.0119
ASP 115
PHE 116
-0.0001
PHE 116
GLU 117
0.0001
GLU 117
GLU 118
0.0016
GLU 118
VAL 119
0.0002
VAL 119
ARG 120
0.0000
ARG 120
PRO 121
-0.0398
PRO 121
LEU 122
-0.0002
LEU 122
LEU 123
0.0000
LEU 123
GLU 124
0.0777
GLU 124
LYS 125
-0.0004
LYS 125
ILE 126
-0.0001
ILE 126
VAL 127
0.0296
VAL 127
ASP 128
0.0002
ASP 128
LEU 129
0.0002
LEU 129
SER 130
0.0065
SER 130
ARG 131
-0.0001
ARG 131
LYS 132
0.0000
LYS 132
TYR 133
-0.1493
TYR 133
ALA 134
0.0001
ALA 134
ASP 135
-0.0001
ASP 135
ILE 136
-0.0253
ILE 136
LEU 137
0.0002
LEU 137
GLY 138
-0.0004
GLY 138
TYR 139
0.1655
TYR 139
GLU 140
-0.0000
GLU 140
GLY 141
-0.0000
GLY 141
GLU 142
-0.0123
GLU 142
PRO 143
-0.0000
PRO 143
TYR 144
0.0001
TYR 144
ASN 145
-0.0562
ASN 145
ALA 146
-0.0003
ALA 146
LEU 147
-0.0003
LEU 147
LEU 148
-0.0315
LEU 148
ASP 149
0.0001
ASP 149
LEU 150
-0.0000
LEU 150
TYR 151
0.1257
TYR 151
GLU 152
-0.0001
GLU 152
PRO 153
0.0002
PRO 153
GLY 154
-0.0445
GLY 154
MET 155
-0.0001
MET 155
LYS 156
0.0002
LYS 156
ALA 157
-0.1113
ALA 157
GLU 158
0.0001
GLU 158
GLU 159
0.0000
GLU 159
VAL 160
-0.0049
VAL 160
ASP 161
0.0003
ASP 161
GLN 162
0.0004
GLN 162
ILE 163
0.0523
ILE 163
PHE 164
0.0002
PHE 164
SER 165
0.0001
SER 165
LYS 166
0.0198
LYS 166
VAL 167
0.0003
VAL 167
ARG 168
-0.0000
ARG 168
ASP 169
0.0425
ASP 169
PHE 170
-0.0001
PHE 170
ILE 171
0.0001
ILE 171
VAL 172
0.0445
VAL 172
GLU 173
0.0004
GLU 173
VAL 174
-0.0000
VAL 174
LEU 175
0.0432
LEU 175
GLU 176
-0.0001
GLU 176
LYS 177
0.0001
LYS 177
ILE 178
-0.0029
ILE 178
GLU 179
-0.0000
GLU 179
ARG 180
-0.0002
ARG 180
LEU 181
0.0526
LEU 181
PRO 182
-0.0001
PRO 182
LYS 183
0.0003
LYS 183
SER 184
-0.2056
SER 184
GLU 185
0.0001
GLU 185
ASP 186
-0.0001
ASP 186
PRO 187
-0.0304
PRO 187
PHE 188
-0.0002
PHE 188
ASN 189
-0.0004
ASN 189
ARG 190
0.0421
ARG 190
GLU 191
-0.0003
GLU 191
ILE 192
0.0002
ILE 192
GLY 193
-0.0136
GLY 193
VAL 194
0.0001
VAL 194
ASP 195
-0.0000
ASP 195
LYS 196
-0.0908
LYS 196
GLN 197
-0.0002
GLN 197
LYS 198
0.0000
LYS 198
GLU 199
-0.0451
GLU 199
PHE 200
0.0003
PHE 200
SER 201
-0.0000
SER 201
ASN 202
0.0359
ASN 202
TRP 203
0.0000
TRP 203
LEU 204
-0.0000
LEU 204
LEU 205
0.1824
LEU 205
HIS 206
-0.0002
HIS 206
TYR 207
-0.0002
TYR 207
LEU 208
0.0602
LEU 208
LYS 209
0.0001
LYS 209
TYR 210
0.0001
TYR 210
ASP 211
-0.0515
ASP 211
PHE 212
-0.0002
PHE 212
THR 213
-0.0002
THR 213
LYS 214
0.0393
LYS 214
GLY 215
0.0000
GLY 215
ARG 216
-0.0002
ARG 216
LEU 217
0.0452
LEU 217
ASP 218
0.0001
ASP 218
VAL 219
0.0002
VAL 219
SER 220
0.1240
SER 220
ALA 221
0.0001
ALA 221
HIS 222
0.0002
HIS 222
PRO 223
-0.0142
PRO 223
PHE 224
-0.0001
PHE 224
THR 225
0.0001
THR 225
ASN 226
-0.1974
ASN 226
PRO 227
0.0003
PRO 227
ILE 228
-0.0002
ILE 228
GLY 229
0.0509
GLY 229
LEU 230
0.0000
LEU 230
ASN 231
0.0001
ASN 231
ASP 232
0.0482
ASP 232
VAL 233
-0.0003
VAL 233
ARG 234
0.0001
ARG 234
ILE 235
-0.0860
ILE 235
THR 236
-0.0003
THR 236
THR 237
0.0004
THR 237
ARG 238
-0.0655
ARG 238
TYR 239
-0.0002
TYR 239
ILE 240
-0.0002
ILE 240
VAL 241
-0.1796
VAL 241
ASN 242
0.0001
ASN 242
ASP 243
0.0000
ASP 243
ILE 244
-0.0420
ILE 244
ARG 245
-0.0001
ARG 245
ASN 246
-0.0001
ASN 246
SER 247
0.0871
SER 247
ILE 248
0.0002
ILE 248
TYR 249
-0.0003
TYR 249
SER 250
0.0061
SER 250
THR 251
0.0004
THR 251
ILE 252
0.0002
ILE 252
HIS 253
0.0179
HIS 253
GLU 254
-0.0005
GLU 254
PHE 255
-0.0001
PHE 255
GLY 256
0.1003
GLY 256
HIS 257
0.0004
HIS 257
ALA 258
-0.0004
ALA 258
LEU 259
-0.0727
LEU 259
TYR 260
0.0002
TYR 260
ALA 261
-0.0003
ALA 261
LEU 262
0.0065
LEU 262
SER 263
-0.0003
SER 263
ILE 264
0.0003
ILE 264
PRO 265
-0.0294
PRO 265
THR 266
0.0001
THR 266
GLU 267
-0.0000
GLU 267
PHE 268
0.0470
PHE 268
TYR 269
0.0000
TYR 269
GLY 270
-0.0002
GLY 270
LEU 271
-0.1676
LEU 271
PRO 272
0.0003
PRO 272
ILE 273
-0.0000
ILE 273
GLY 274
-0.0456
GLY 274
SER 275
0.0001
SER 275
SER 276
-0.0001
SER 276
ALA 277
-0.1389
ALA 277
SER 278
-0.0002
SER 278
TYR 279
-0.0000
TYR 279
GLY 280
-0.0164
GLY 280
PHE 281
-0.0002
PHE 281
ASP 282
0.0001
ASP 282
GLU 283
-0.0057
GLU 283
SER 284
0.0001
SER 284
GLN 285
-0.0001
GLN 285
SER 286
0.0577
SER 286
ARG 287
0.0001
ARG 287
PHE 288
0.0002
PHE 288
TRP 289
-0.0391
TRP 289
GLU 290
0.0000
GLU 290
ASN 291
-0.0000
ASN 291
VAL 292
0.0519
VAL 292
VAL 293
-0.0002
VAL 293
GLY 294
0.0002
GLY 294
ARG 295
0.0563
ARG 295
SER 296
0.0001
SER 296
LEU 297
0.0002
LEU 297
ALA 298
0.2121
ALA 298
PHE 299
0.0001
PHE 299
TRP 300
0.0002
TRP 300
LYS 301
0.0275
LYS 301
GLY 302
0.0003
GLY 302
ILE 303
0.0002
ILE 303
TYR 304
0.1430
TYR 304
SER 305
-0.0000
SER 305
LYS 306
-0.0001
LYS 306
PHE 307
0.0114
PHE 307
ILE 308
-0.0001
ILE 308
GLU 309
-0.0001
GLU 309
ILE 310
0.0002
ILE 310
VAL 311
0.0002
VAL 311
PRO 312
-0.0004
PRO 312
GLU 313
0.0236
GLU 313
MET 314
-0.0004
MET 314
ARG 315
0.0001
ARG 315
GLY 316
-0.0185
GLY 316
TYR 317
-0.0001
TYR 317
SER 318
0.0001
SER 318
VAL 319
-0.0293
VAL 319
GLU 320
0.0002
GLU 320
GLU 321
0.0001
GLU 321
LEU 322
0.0491
LEU 322
TRP 323
-0.0003
TRP 323
ARG 324
0.0001
ARG 324
ALA 325
0.1579
ALA 325
VAL 326
-0.0003
VAL 326
ASN 327
0.0005
ASN 327
ARG 328
0.3384
ARG 328
VAL 329
-0.0002
VAL 329
GLN 330
0.0002
GLN 330
ARG 331
0.2274
ARG 331
SER 332
0.0003
SER 332
PHE 333
-0.0001
PHE 333
ILE 334
0.0673
ILE 334
ARG 335
-0.0001
ARG 335
THR 336
-0.0001
THR 336
GLU 337
-0.1169
GLU 337
ALA 338
0.0001
ALA 338
ASP 339
0.0000
ASP 339
GLU 340
0.1329
GLU 340
VAL 341
-0.0000
VAL 341
THR 342
-0.0000
THR 342
TYR 343
-0.1040
TYR 343
ASN 344
-0.0003
ASN 344
LEU 345
0.0002
LEU 345
HIS 346
-0.0658
HIS 346
ILE 347
0.0001
ILE 347
ILE 348
-0.0002
ILE 348
ILE 349
0.1265
ILE 349
ARG 350
0.0002
ARG 350
PHE 351
-0.0000
PHE 351
GLU 352
0.0278
GLU 352
ILE 353
0.0002
ILE 353
GLU 354
-0.0001
GLU 354
ARG 355
-0.0188
ARG 355
GLU 356
-0.0000
GLU 356
LEU 357
0.0003
LEU 357
ILE 358
-0.0642
ILE 358
ASN 359
-0.0001
ASN 359
GLY 360
0.0001
GLY 360
GLU 361
-0.0921
GLU 361
LEU 362
0.0001
LEU 362
SER 363
0.0002
SER 363
VAL 364
0.0620
VAL 364
LYS 365
0.0000
LYS 365
ASP 366
0.0002
ASP 366
VAL 367
0.1057
VAL 367
PRO 368
0.0000
PRO 368
ASP 369
-0.0001
ASP 369
LYS 370
0.0412
LYS 370
TRP 371
-0.0002
TRP 371
ASN 372
-0.0001
ASN 372
GLU 373
0.0137
GLU 373
LEU 374
0.0003
LEU 374
TYR 375
0.0001
TYR 375
LYS 376
-0.0484
LYS 376
LYS 377
0.0001
LYS 377
TYR 378
-0.0002
TYR 378
LEU 379
-0.0786
LEU 379
GLY 380
-0.0001
GLY 380
LEU 381
0.0004
LEU 381
ASP 382
0.2180
ASP 382
VAL 383
0.0001
VAL 383
PRO 384
-0.0003
PRO 384
ASN 385
0.1696
ASN 385
ASN 386
-0.0000
ASN 386
THR 387
-0.0001
THR 387
LEU 388
0.1416
LEU 388
GLY 389
0.0003
GLY 389
CYS 390
-0.0002
CYS 390
MET 391
0.0096
MET 391
GLN 392
-0.0001
GLN 392
ASP 393
0.0002
ASP 393
PRO 394
-0.0107
PRO 394
HIS 395
0.0001
HIS 395
TRP 396
-0.0001
TRP 396
PHE 397
-0.0396
PHE 397
GLY 398
-0.0000
GLY 398
GLY 399
-0.0004
GLY 399
ASN 400
0.0000
ASN 400
PHE 401
-0.0000
PHE 401
GLY 402
-0.0001
GLY 402
TYR 403
0.0295
TYR 403
PHE 404
0.0001
PHE 404
PRO 405
-0.0003
PRO 405
THR 406
0.0412
THR 406
TYR 407
0.0003
TYR 407
ALA 408
-0.0000
ALA 408
LEU 409
0.0655
LEU 409
GLY 410
-0.0004
GLY 410
ASN 411
-0.0001
ASN 411
LEU 412
0.0317
LEU 412
TYR 413
0.0001
TYR 413
ALA 414
-0.0002
ALA 414
ALA 415
-0.0451
ALA 415
GLN 416
0.0002
GLN 416
ILE 417
0.0001
ILE 417
PHE 418
0.0337
PHE 418
GLU 419
0.0001
GLU 419
LYS 420
0.0003
LYS 420
LEU 421
0.0986
LEU 421
LYS 422
0.0002
LYS 422
GLU 423
-0.0001
GLU 423
GLU 424
0.0849
GLU 424
ILE 425
0.0001
ILE 425
ASN 426
-0.0001
ASN 426
PHE 427
0.0493
PHE 427
GLU 428
0.0001
GLU 428
GLU 429
0.0003
GLU 429
VAL 430
-0.0810
VAL 430
VAL 431
-0.0005
VAL 431
SER 432
0.0001
SER 432
ALA 433
0.2110
ALA 433
GLY 434
0.0001
GLY 434
ASN 435
0.0002
ASN 435
PHE 436
0.0420
PHE 436
GLU 437
-0.0002
GLU 437
ILE 438
0.0002
ILE 438
ILE 439
0.0787
ILE 439
LYS 440
0.0001
LYS 440
ASN 441
-0.0004
ASN 441
PHE 442
0.1341
PHE 442
LEU 443
-0.0001
LEU 443
LYS 444
-0.0001
LYS 444
GLU 445
-0.0156
GLU 445
LYS 446
-0.0001
LYS 446
ILE 447
-0.0002
ILE 447
HIS 448
-0.0730
HIS 448
SER 449
0.0001
SER 449
LYS 450
0.0001
LYS 450
GLY 451
-0.1235
GLY 451
LYS 452
0.0002
LYS 452
MET 453
0.0000
MET 453
TYR 454
-0.1214
TYR 454
GLU 455
-0.0000
GLU 455
PRO 456
-0.0002
PRO 456
SER 457
0.0022
SER 457
ASP 458
0.0003
ASP 458
LEU 459
-0.0003
LEU 459
ILE 460
-0.0226
ILE 460
LYS 461
-0.0001
LYS 461
ILE 462
0.0002
ILE 462
VAL 463
0.0634
VAL 463
THR 464
-0.0002
THR 464
GLY 465
0.0000
GLY 465
LYS 466
0.0249
LYS 466
PRO 467
-0.0001
PRO 467
LEU 468
0.0002
LEU 468
SER 469
-0.2368
SER 469
TYR 470
-0.0001
TYR 470
GLU 471
-0.0003
GLU 471
SER 472
0.1166
SER 472
PHE 473
0.0003
PHE 473
VAL 474
0.0003
VAL 474
ARG 475
0.0424
ARG 475
TYR 476
-0.0001
TYR 476
ILE 477
-0.0001
ILE 477
LYS 478
0.0666
LYS 478
ASP 479
0.0002
ASP 479
LYS 480
0.0001
LYS 480
TYR 481
0.0660
TYR 481
SER 482
-0.0000
SER 482
LYS 483
0.0003
LYS 483
VAL 484
0.0079
VAL 484
TYR 485
-0.0000
TYR 485
GLU 486
0.0002
GLU 486
ILE 487
0.0212
ILE 487
GLU 488
0.0002
GLU 488
LEU 489
0.0000
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.