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
ALA 2
0.0002
ALA 2
PRO 3
0.0002
PRO 3
PRO 4
-0.0051
PRO 4
ALA 5
0.0001
ALA 5
SER 6
-0.0001
SER 6
PRO 7
0.0015
PRO 7
PRO 8
0.0000
PRO 8
ALA 9
0.0000
ALA 9
SER 10
0.0382
SER 10
PRO 11
-0.0004
PRO 11
LYS 12
0.0000
LYS 12
THR 13
0.0108
THR 13
PRO 14
-0.0001
PRO 14
ILE 15
-0.0002
ILE 15
GLU 16
0.0054
GLU 16
LYS 17
0.0001
LYS 17
LYS 18
-0.0001
LYS 18
HIS 19
-0.0059
HIS 19
ALA 20
0.0002
ALA 20
ASP 21
0.0002
ASP 21
GLU 22
-0.0109
GLU 22
ILE 23
0.0001
ILE 23
ASP 24
-0.0003
ASP 24
LYS 25
0.0339
LYS 25
TYR 26
-0.0002
TYR 26
ILE 27
0.0003
ILE 27
GLN 28
0.0219
GLN 28
GLY 29
0.0000
GLY 29
LEU 30
-0.0002
LEU 30
ASP 31
-0.0871
ASP 31
TYR 32
0.0002
TYR 32
ASN 33
-0.0001
ASN 33
LYS 34
0.0073
LYS 34
ASN 35
0.0002
ASN 35
ASN 36
0.0004
ASN 36
VAL 37
0.0632
VAL 37
LEU 38
-0.0003
LEU 38
VAL 39
0.0003
VAL 39
TYR 40
-0.2136
TYR 40
HIS 41
0.0002
HIS 41
GLY 42
-0.0000
GLY 42
ASP 43
-0.1782
ASP 43
ALA 44
0.0001
ALA 44
VAL 45
-0.0002
VAL 45
THR 46
0.0197
THR 46
ASN 47
-0.0001
ASN 47
VAL 48
0.0001
VAL 48
PRO 49
-0.0992
PRO 49
PRO 50
0.0004
PRO 50
ARG 51
-0.0001
ARG 51
LYS 52
-0.0580
LYS 52
GLY 53
0.0004
GLY 53
TYR 54
-0.0000
TYR 54
LYS 55
-0.0589
LYS 55
ASP 56
-0.0002
ASP 56
GLY 57
0.0004
GLY 57
ASN 58
-0.0333
ASN 58
GLU 59
-0.0002
GLU 59
TYR 60
-0.0003
TYR 60
ILE 61
-0.1415
ILE 61
VAL 62
0.0003
VAL 62
VAL 63
0.0000
VAL 63
GLU 64
-0.1815
GLU 64
LYS 65
0.0001
LYS 65
LYS 66
-0.0003
LYS 66
LYS 67
-0.2105
LYS 67
LYS 68
-0.0003
LYS 68
SER 69
0.0004
SER 69
ILE 70
-0.1705
ILE 70
ASN 71
-0.0004
ASN 71
GLN 72
-0.0001
GLN 72
ASN 73
-0.1454
ASN 73
ASN 74
0.0002
ASN 74
ALA 75
-0.0002
ALA 75
ASP 76
-0.0339
ASP 76
ILE 77
-0.0001
ILE 77
GLN 78
0.0001
GLN 78
VAL 79
-0.0016
VAL 79
VAL 80
0.0001
VAL 80
ASN 81
0.0001
ASN 81
ALA 82
0.0183
ALA 82
ILE 83
0.0002
ILE 83
SER 84
0.0005
SER 84
SER 85
0.0139
SER 85
LEU 86
0.0000
LEU 86
THR 87
-0.0003
THR 87
TYR 88
-0.0309
TYR 88
PRO 89
0.0003
PRO 89
GLY 90
-0.0000
GLY 90
ALA 91
-0.0019
ALA 91
LEU 92
-0.0002
LEU 92
VAL 93
0.0002
VAL 93
LYS 94
-0.0202
LYS 94
ALA 95
0.0001
ALA 95
ASN 96
-0.0004
ASN 96
SER 97
-0.0513
SER 97
GLU 98
-0.0005
GLU 98
LEU 99
0.0001
LEU 99
VAL 100
-0.0752
VAL 100
GLU 101
-0.0002
GLU 101
ASN 102
0.0004
ASN 102
GLN 103
-0.0199
GLN 103
PRO 104
0.0002
PRO 104
ASP 105
0.0005
ASP 105
VAL 106
-0.0226
VAL 106
LEU 107
-0.0003
LEU 107
PRO 108
0.0003
PRO 108
VAL 109
0.0047
VAL 109
LYS 110
-0.0004
LYS 110
ARG 111
0.0003
ARG 111
ASP 112
-0.0110
ASP 112
SER 113
-0.0002
SER 113
LEU 114
0.0001
LEU 114
THR 115
0.0629
THR 115
LEU 116
0.0002
LEU 116
SER 117
-0.0001
SER 117
ILE 118
0.0520
ILE 118
ASP 119
0.0003
ASP 119
LEU 120
-0.0003
LEU 120
PRO 121
0.0068
PRO 121
GLY 122
-0.0002
GLY 122
MET 123
0.0001
MET 123
THR 124
0.0046
THR 124
ASN 125
-0.0003
ASN 125
GLN 126
-0.0001
GLN 126
ASP 127
0.0026
ASP 127
ASN 128
0.0003
ASN 128
LYS 129
-0.0002
LYS 129
ILE 130
0.0124
ILE 130
VAL 131
-0.0000
VAL 131
VAL 132
0.0002
VAL 132
LYS 133
0.0424
LYS 133
ASN 134
0.0002
ASN 134
ALA 135
-0.0001
ALA 135
THR 136
-0.0034
THR 136
LYS 137
-0.0002
LYS 137
SER 138
0.0001
SER 138
ASN 139
-0.0042
ASN 139
VAL 140
-0.0000
VAL 140
ASN 141
-0.0002
ASN 141
ASN 142
-0.0352
ASN 142
ALA 143
0.0000
ALA 143
VAL 144
-0.0002
VAL 144
ASN 145
-0.0053
ASN 145
THR 146
-0.0003
THR 146
LEU 147
0.0000
LEU 147
VAL 148
0.0368
VAL 148
GLU 149
0.0001
GLU 149
ARG 150
-0.0001
ARG 150
TRP 151
0.0021
TRP 151
ASN 152
0.0000
ASN 152
GLU 153
0.0002
GLU 153
LYS 154
0.0070
LYS 154
TYR 155
-0.0002
TYR 155
ALA 156
-0.0001
ALA 156
GLN 157
0.0020
GLN 157
ALA 158
0.0002
ALA 158
TYR 159
-0.0000
TYR 159
PRO 160
-0.0046
PRO 160
ASN 161
0.0003
ASN 161
VAL 162
-0.0000
VAL 162
SER 163
0.0156
SER 163
ALA 164
-0.0001
ALA 164
LYS 165
-0.0002
LYS 165
ILE 166
0.0297
ILE 166
ASP 167
0.0002
ASP 167
TYR 168
0.0000
TYR 168
ASP 169
-0.0113
ASP 169
ASP 170
-0.0002
ASP 170
GLU 171
-0.0003
GLU 171
MET 172
-0.0313
MET 172
ALA 173
0.0004
ALA 173
TYR 174
-0.0000
TYR 174
SER 175
-0.0635
SER 175
GLU 176
-0.0003
GLU 176
SER 177
0.0000
SER 177
GLN 178
0.0306
GLN 178
LEU 179
0.0002
LEU 179
ILE 180
0.0002
ILE 180
ALA 181
0.0179
ALA 181
LYS 182
0.0002
LYS 182
PHE 183
-0.0000
PHE 183
GLY 184
-0.0237
GLY 184
THR 185
-0.0001
THR 185
ALA 186
-0.0001
ALA 186
PHE 187
-0.0263
PHE 187
LYS 188
-0.0001
LYS 188
ALA 189
-0.0000
ALA 189
VAL 190
-0.0148
VAL 190
ASN 191
0.0002
ASN 191
ASN 192
-0.0002
ASN 192
SER 193
-0.0116
SER 193
LEU 194
0.0000
LEU 194
ASN 195
-0.0001
ASN 195
VAL 196
0.0257
VAL 196
ASN 197
0.0001
ASN 197
PHE 198
-0.0001
PHE 198
GLY 199
-0.0529
GLY 199
ALA 200
0.0002
ALA 200
ILE 201
0.0002
ILE 201
SER 202
0.0610
SER 202
GLU 203
-0.0001
GLU 203
GLY 204
-0.0003
GLY 204
LYS 205
0.0272
LYS 205
MET 206
-0.0001
MET 206
GLN 207
-0.0003
GLN 207
GLU 208
-0.0498
GLU 208
GLU 209
0.0003
GLU 209
VAL 210
-0.0001
VAL 210
ILE 211
0.0224
ILE 211
SER 212
0.0002
SER 212
PHE 213
-0.0001
PHE 213
LYS 214
0.0230
LYS 214
GLN 215
0.0003
GLN 215
ILE 216
0.0000
ILE 216
TYR 217
-0.0137
TYR 217
TYR 218
0.0001
TYR 218
ASN 219
-0.0002
ASN 219
VAL 220
0.0410
VAL 220
ASN 221
-0.0002
ASN 221
VAL 222
0.0001
VAL 222
ASN 223
0.0327
ASN 223
GLU 224
0.0001
GLU 224
PRO 225
-0.0003
PRO 225
THR 226
0.0518
THR 226
ARG 227
-0.0002
ARG 227
PRO 228
0.0001
PRO 228
SER 229
-0.0362
SER 229
ARG 230
0.0000
ARG 230
PHE 231
-0.0001
PHE 231
PHE 232
-0.0017
PHE 232
GLY 233
-0.0003
GLY 233
LYS 234
0.0001
LYS 234
ALA 235
-0.0054
ALA 235
VAL 236
-0.0000
VAL 236
THR 237
-0.0001
THR 237
LYS 238
-0.0064
LYS 238
GLU 239
0.0004
GLU 239
GLN 240
-0.0001
GLN 240
LEU 241
-0.0116
LEU 241
GLN 242
0.0003
GLN 242
ALA 243
0.0001
ALA 243
LEU 244
-0.0082
LEU 244
GLY 245
0.0000
GLY 245
VAL 246
0.0003
VAL 246
ASN 247
0.0127
ASN 247
ALA 248
-0.0002
ALA 248
GLU 249
-0.0002
GLU 249
ASN 250
0.0229
ASN 250
PRO 251
-0.0001
PRO 251
PRO 252
-0.0001
PRO 252
ALA 253
0.0091
ALA 253
TYR 254
-0.0004
TYR 254
ILE 255
0.0001
ILE 255
SER 256
-0.0029
SER 256
SER 257
-0.0003
SER 257
VAL 258
-0.0001
VAL 258
ALA 259
0.0421
ALA 259
TYR 260
-0.0004
TYR 260
GLY 261
0.0003
GLY 261
ARG 262
0.0811
ARG 262
GLN 263
0.0001
GLN 263
VAL 264
0.0001
VAL 264
TYR 265
0.0463
TYR 265
LEU 266
-0.0002
LEU 266
LYS 267
-0.0001
LYS 267
LEU 268
-0.0057
LEU 268
SER 269
0.0003
SER 269
THR 270
-0.0002
THR 270
ASN 271
0.0718
ASN 271
SER 272
-0.0002
SER 272
HIS 273
-0.0002
HIS 273
SER 274
-0.0298
SER 274
THR 275
0.0001
THR 275
LYS 276
0.0001
LYS 276
VAL 277
-0.0025
VAL 277
LYS 278
0.0001
LYS 278
ALA 279
0.0002
ALA 279
ALA 280
-0.0009
ALA 280
PHE 281
-0.0000
PHE 281
ASP 282
0.0002
ASP 282
ALA 283
0.0157
ALA 283
ALA 284
-0.0003
ALA 284
VAL 285
0.0001
VAL 285
SER 286
0.0166
SER 286
GLY 287
0.0003
GLY 287
LYS 288
0.0001
LYS 288
SER 289
0.0291
SER 289
VAL 290
0.0001
VAL 290
SER 291
-0.0002
SER 291
GLY 292
0.0184
GLY 292
ASP 293
0.0002
ASP 293
VAL 294
-0.0002
VAL 294
GLU 295
0.0033
GLU 295
LEU 296
0.0006
LEU 296
THR 297
-0.0001
THR 297
ASN 298
-0.0207
ASN 298
ILE 299
0.0002
ILE 299
ILE 300
0.0001
ILE 300
LYS 301
0.0110
LYS 301
ASN 302
-0.0000
ASN 302
SER 303
-0.0000
SER 303
SER 304
0.0000
SER 304
PHE 305
-0.0001
PHE 305
LYS 306
0.0000
LYS 306
ALA 307
0.0447
ALA 307
VAL 308
-0.0001
VAL 308
ILE 309
-0.0002
ILE 309
TYR 310
0.0467
TYR 310
GLY 311
0.0001
GLY 311
GLY 312
0.0001
GLY 312
SER 313
-0.0195
SER 313
ALA 314
0.0000
ALA 314
LYS 315
0.0004
LYS 315
ASP 316
0.0034
ASP 316
GLU 317
0.0001
GLU 317
VAL 318
0.0000
VAL 318
GLN 319
0.0145
GLN 319
ILE 320
-0.0001
ILE 320
ILE 321
0.0003
ILE 321
ASP 322
0.0430
ASP 322
GLY 323
-0.0002
GLY 323
ASN 324
0.0002
ASN 324
LEU 325
-0.0355
LEU 325
GLY 326
0.0004
GLY 326
ASP 327
-0.0001
ASP 327
LEU 328
-0.0271
LEU 328
ARG 329
0.0000
ARG 329
ASP 330
0.0002
ASP 330
ILE 331
-0.0267
ILE 331
LEU 332
0.0002
LEU 332
LYS 333
0.0003
LYS 333
LYS 334
-0.0260
LYS 334
GLY 335
-0.0001
GLY 335
ALA 336
0.0001
ALA 336
THR 337
0.0818
THR 337
PHE 338
-0.0003
PHE 338
ASN 339
0.0003
ASN 339
ARG 340
0.0219
ARG 340
GLU 341
0.0000
GLU 341
THR 342
0.0002
THR 342
PRO 343
0.0237
PRO 343
GLY 344
0.0002
GLY 344
VAL 345
-0.0001
VAL 345
PRO 346
0.0019
PRO 346
ILE 347
-0.0001
ILE 347
ALA 348
-0.0000
ALA 348
TYR 349
0.0380
TYR 349
THR 350
-0.0003
THR 350
THR 351
0.0002
THR 351
ASN 352
0.0225
ASN 352
PHE 353
-0.0000
PHE 353
LEU 354
0.0005
LEU 354
LYS 355
0.0166
LYS 355
ASP 356
0.0003
ASP 356
ASN 357
-0.0002
ASN 357
GLU 358
-0.0544
GLU 358
LEU 359
-0.0001
LEU 359
ALA 360
-0.0003
ALA 360
VAL 361
-0.1446
VAL 361
ILE 362
-0.0005
ILE 362
LYS 363
0.0001
LYS 363
ASN 364
-0.1948
ASN 364
ASN 365
-0.0003
ASN 365
SER 366
0.0001
SER 366
GLU 367
-0.2808
GLU 367
TYR 368
-0.0000
TYR 368
ILE 369
0.0001
ILE 369
GLU 370
-0.0706
GLU 370
THR 371
-0.0002
THR 371
THR 372
0.0003
THR 372
SER 373
-0.2554
SER 373
LYS 374
-0.0002
LYS 374
ALA 375
-0.0001
ALA 375
TYR 376
-0.3190
TYR 376
THR 377
-0.0004
THR 377
ASP 378
-0.0001
ASP 378
GLY 379
-0.2796
GLY 379
LYS 380
-0.0003
LYS 380
ILE 381
0.0000
ILE 381
ASN 382
-0.0926
ASN 382
ILE 383
-0.0004
ILE 383
ASP 384
0.0002
ASP 384
HIS 385
-0.0867
HIS 385
SER 386
-0.0003
SER 386
GLY 387
0.0002
GLY 387
GLY 388
-0.0385
GLY 388
TYR 389
-0.0001
TYR 389
VAL 390
-0.0003
VAL 390
ALA 391
-0.0057
ALA 391
GLN 392
-0.0002
GLN 392
PHE 393
0.0001
PHE 393
ASN 394
0.0314
ASN 394
ILE 395
0.0000
ILE 395
SER 396
0.0000
SER 396
TRP 397
0.0423
TRP 397
ASP 398
-0.0001
ASP 398
GLU 399
0.0002
GLU 399
VAL 400
-0.0570
VAL 400
ASN 401
0.0002
ASN 401
TYR 402
0.0002
TYR 402
ASP 403
0.0190
ASP 403
PRO 404
0.0003
PRO 404
GLU 405
-0.0001
GLU 405
GLY 406
0.0017
GLY 406
ASN 407
0.0001
ASN 407
GLU 408
-0.0003
GLU 408
ILE 409
0.0137
ILE 409
VAL 410
0.0002
VAL 410
GLN 411
-0.0002
GLN 411
HIS 412
0.0576
HIS 412
LYS 413
-0.0001
LYS 413
ASN 414
0.0001
ASN 414
TRP 415
0.0734
TRP 415
SER 416
0.0002
SER 416
GLU 417
0.0001
GLU 417
ASN 418
0.0081
ASN 418
ASN 419
-0.0002
ASN 419
LYS 420
0.0002
LYS 420
SER 421
0.0055
SER 421
LYS 422
0.0002
LYS 422
LEU 423
-0.0001
LEU 423
ALA 424
0.0151
ALA 424
HIS 425
0.0001
HIS 425
PHE 426
-0.0002
PHE 426
THR 427
-0.0935
THR 427
SER 428
-0.0000
SER 428
SER 429
0.0002
SER 429
ILE 430
-0.1156
ILE 430
TYR 431
-0.0001
TYR 431
LEU 432
-0.0000
LEU 432
PRO 433
-0.1922
PRO 433
GLY 434
0.0001
GLY 434
ASN 435
-0.0004
ASN 435
ALA 436
-0.0165
ALA 436
ARG 437
-0.0002
ARG 437
ASN 438
0.0000
ASN 438
ILE 439
0.0381
ILE 439
ASN 440
0.0000
ASN 440
VAL 441
-0.0001
VAL 441
TYR 442
0.0286
TYR 442
ALA 443
0.0004
ALA 443
LYS 444
-0.0002
LYS 444
GLU 445
-0.0040
GLU 445
CYS 446
0.0001
CYS 446
THR 447
0.0001
THR 447
GLY 448
0.0006
GLY 448
LEU 449
-0.0001
LEU 449
ALA 450
-0.0000
ALA 450
TRP 451
0.0013
TRP 451
GLU 452
0.0002
GLU 452
TRP 453
0.0002
TRP 453
TRP 454
0.0290
TRP 454
ARG 455
-0.0001
ARG 455
THR 456
-0.0001
THR 456
VAL 457
0.0073
VAL 457
ILE 458
0.0001
ILE 458
ASP 459
0.0000
ASP 459
ASP 460
0.0601
ASP 460
ARG 461
-0.0000
ARG 461
ASN 462
0.0001
ASN 462
LEU 463
0.0049
LEU 463
PRO 464
-0.0005
PRO 464
LEU 465
0.0001
LEU 465
VAL 466
-0.0331
VAL 466
LYS 467
0.0003
LYS 467
ASN 468
0.0001
ASN 468
ARG 469
-0.0477
ARG 469
ASN 470
0.0001
ASN 470
ILE 471
-0.0001
ILE 471
SER 472
-0.0522
SER 472
ILE 473
-0.0000
ILE 473
TRP 474
-0.0002
TRP 474
GLY 475
-0.0366
GLY 475
THR 476
-0.0001
THR 476
THR 477
0.0000
THR 477
LEU 478
-0.0084
LEU 478
TYR 479
0.0002
TYR 479
PRO 480
0.0000
PRO 480
LYS 481
0.0004
LYS 481
TYR 482
-0.0003
TYR 482
SER 483
0.0002
SER 483
ASN 484
0.0004
ASN 484
LYS 485
-0.0000
LYS 485
VAL 486
0.0001
VAL 486
ASP 487
-0.0098
ASP 487
ASN 488
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.