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
0.0000
ALA 2
PRO 3
0.0001
PRO 3
PRO 4
-0.0746
PRO 4
ALA 5
-0.0001
ALA 5
SER 6
0.0001
SER 6
PRO 7
0.1102
PRO 7
PRO 8
-0.0001
PRO 8
ALA 9
0.0001
ALA 9
SER 10
0.0797
SER 10
PRO 11
-0.0001
PRO 11
LYS 12
-0.0001
LYS 12
THR 13
0.0013
THR 13
PRO 14
0.0001
PRO 14
ILE 15
0.0000
ILE 15
GLU 16
0.0195
GLU 16
LYS 17
-0.0003
LYS 17
LYS 18
0.0001
LYS 18
HIS 19
0.0085
HIS 19
ALA 20
0.0000
ALA 20
ASP 21
0.0002
ASP 21
GLU 22
0.0188
GLU 22
ILE 23
0.0003
ILE 23
ASP 24
-0.0002
ASP 24
LYS 25
-0.0075
LYS 25
TYR 26
0.0002
TYR 26
ILE 27
-0.0003
ILE 27
GLN 28
-0.0128
GLN 28
GLY 29
0.0000
GLY 29
LEU 30
-0.0003
LEU 30
ASP 31
0.0315
ASP 31
TYR 32
0.0003
TYR 32
ASN 33
-0.0003
ASN 33
LYS 34
-0.0158
LYS 34
ASN 35
0.0000
ASN 35
ASN 36
0.0003
ASN 36
VAL 37
-0.0084
VAL 37
LEU 38
-0.0000
LEU 38
VAL 39
-0.0001
VAL 39
TYR 40
0.0899
TYR 40
HIS 41
0.0001
HIS 41
GLY 42
0.0001
GLY 42
ASP 43
0.0054
ASP 43
ALA 44
-0.0001
ALA 44
VAL 45
0.0002
VAL 45
THR 46
-0.0705
THR 46
ASN 47
0.0001
ASN 47
VAL 48
-0.0003
VAL 48
PRO 49
0.0719
PRO 49
PRO 50
-0.0004
PRO 50
ARG 51
0.0002
ARG 51
LYS 52
-0.0523
LYS 52
GLY 53
-0.0002
GLY 53
TYR 54
0.0003
TYR 54
LYS 55
-0.0625
LYS 55
ASP 56
0.0002
ASP 56
GLY 57
0.0003
GLY 57
ASN 58
0.0457
ASN 58
GLU 59
0.0003
GLU 59
TYR 60
-0.0004
TYR 60
ILE 61
0.0883
ILE 61
VAL 62
0.0003
VAL 62
VAL 63
-0.0001
VAL 63
GLU 64
-0.0391
GLU 64
LYS 65
-0.0001
LYS 65
LYS 66
0.0006
LYS 66
LYS 67
0.0122
LYS 67
LYS 68
-0.0005
LYS 68
SER 69
0.0000
SER 69
ILE 70
0.1450
ILE 70
ASN 71
0.0005
ASN 71
GLN 72
-0.0003
GLN 72
ASN 73
0.1345
ASN 73
ASN 74
-0.0000
ASN 74
ALA 75
0.0000
ALA 75
ASP 76
-0.0151
ASP 76
ILE 77
0.0002
ILE 77
GLN 78
0.0001
GLN 78
VAL 79
-0.0032
VAL 79
VAL 80
-0.0002
VAL 80
ASN 81
-0.0001
ASN 81
ALA 82
0.0256
ALA 82
ILE 83
-0.0001
ILE 83
SER 84
-0.0000
SER 84
SER 85
0.0052
SER 85
LEU 86
0.0002
LEU 86
THR 87
0.0002
THR 87
TYR 88
-0.0184
TYR 88
PRO 89
-0.0001
PRO 89
GLY 90
0.0004
GLY 90
ALA 91
-0.0089
ALA 91
LEU 92
0.0000
LEU 92
VAL 93
-0.0001
VAL 93
LYS 94
0.0046
LYS 94
ALA 95
-0.0003
ALA 95
ASN 96
0.0001
ASN 96
SER 97
0.0027
SER 97
GLU 98
-0.0001
GLU 98
LEU 99
0.0002
LEU 99
VAL 100
-0.0042
VAL 100
GLU 101
0.0003
GLU 101
ASN 102
0.0000
ASN 102
GLN 103
0.0020
GLN 103
PRO 104
0.0003
PRO 104
ASP 105
-0.0003
ASP 105
VAL 106
-0.0366
VAL 106
LEU 107
-0.0000
LEU 107
PRO 108
-0.0002
PRO 108
VAL 109
-0.0571
VAL 109
LYS 110
-0.0001
LYS 110
ARG 111
0.0000
ARG 111
ASP 112
-0.0165
ASP 112
SER 113
0.0002
SER 113
LEU 114
-0.0002
LEU 114
THR 115
-0.0028
THR 115
LEU 116
-0.0002
LEU 116
SER 117
0.0001
SER 117
ILE 118
-0.0054
ILE 118
ASP 119
-0.0003
ASP 119
LEU 120
0.0001
LEU 120
PRO 121
-0.0138
PRO 121
GLY 122
0.0001
GLY 122
MET 123
-0.0001
MET 123
THR 124
0.0360
THR 124
ASN 125
0.0001
ASN 125
GLN 126
0.0001
GLN 126
ASP 127
-0.0101
ASP 127
ASN 128
0.0000
ASN 128
LYS 129
-0.0003
LYS 129
ILE 130
0.0112
ILE 130
VAL 131
0.0002
VAL 131
VAL 132
-0.0000
VAL 132
LYS 133
0.0528
LYS 133
ASN 134
-0.0001
ASN 134
ALA 135
-0.0001
ALA 135
THR 136
-0.0149
THR 136
LYS 137
-0.0005
LYS 137
SER 138
-0.0002
SER 138
ASN 139
-0.0426
ASN 139
VAL 140
0.0003
VAL 140
ASN 141
-0.0000
ASN 141
ASN 142
-0.0279
ASN 142
ALA 143
0.0003
ALA 143
VAL 144
0.0003
VAL 144
ASN 145
-0.0084
ASN 145
THR 146
0.0002
THR 146
LEU 147
0.0002
LEU 147
VAL 148
-0.0060
VAL 148
GLU 149
0.0004
GLU 149
ARG 150
-0.0000
ARG 150
TRP 151
0.0208
TRP 151
ASN 152
0.0000
ASN 152
GLU 153
-0.0000
GLU 153
LYS 154
-0.0089
LYS 154
TYR 155
0.0002
TYR 155
ALA 156
0.0000
ALA 156
GLN 157
-0.0009
GLN 157
ALA 158
0.0000
ALA 158
TYR 159
-0.0001
TYR 159
PRO 160
-0.0211
PRO 160
ASN 161
-0.0003
ASN 161
VAL 162
0.0002
VAL 162
SER 163
0.0652
SER 163
ALA 164
0.0000
ALA 164
LYS 165
-0.0001
LYS 165
ILE 166
0.2270
ILE 166
ASP 167
-0.0001
ASP 167
TYR 168
0.0002
TYR 168
ASP 169
0.0577
ASP 169
ASP 170
0.0001
ASP 170
GLU 171
-0.0002
GLU 171
MET 172
0.0678
MET 172
ALA 173
-0.0002
ALA 173
TYR 174
-0.0003
TYR 174
SER 175
0.0563
SER 175
GLU 176
0.0001
GLU 176
SER 177
-0.0000
SER 177
GLN 178
-0.0053
GLN 178
LEU 179
-0.0000
LEU 179
ILE 180
0.0000
ILE 180
ALA 181
-0.0033
ALA 181
LYS 182
-0.0001
LYS 182
PHE 183
0.0001
PHE 183
GLY 184
-0.0030
GLY 184
THR 185
0.0001
THR 185
ALA 186
-0.0004
ALA 186
PHE 187
0.0362
PHE 187
LYS 188
-0.0001
LYS 188
ALA 189
-0.0001
ALA 189
VAL 190
0.0012
VAL 190
ASN 191
0.0001
ASN 191
ASN 192
0.0003
ASN 192
SER 193
-0.0148
SER 193
LEU 194
-0.0000
LEU 194
ASN 195
0.0003
ASN 195
VAL 196
0.0272
VAL 196
ASN 197
0.0002
ASN 197
PHE 198
0.0000
PHE 198
GLY 199
0.1532
GLY 199
ALA 200
-0.0000
ALA 200
ILE 201
-0.0002
ILE 201
SER 202
-0.0386
SER 202
GLU 203
-0.0001
GLU 203
GLY 204
-0.0001
GLY 204
LYS 205
0.0005
LYS 205
MET 206
0.0002
MET 206
GLN 207
-0.0004
GLN 207
GLU 208
0.1864
GLU 208
GLU 209
-0.0000
GLU 209
VAL 210
-0.0002
VAL 210
ILE 211
0.1363
ILE 211
SER 212
-0.0002
SER 212
PHE 213
0.0002
PHE 213
LYS 214
0.1222
LYS 214
GLN 215
-0.0002
GLN 215
ILE 216
0.0001
ILE 216
TYR 217
0.1255
TYR 217
TYR 218
0.0001
TYR 218
ASN 219
-0.0001
ASN 219
VAL 220
0.0530
VAL 220
ASN 221
0.0002
ASN 221
VAL 222
0.0002
VAL 222
ASN 223
-0.0023
ASN 223
GLU 224
0.0003
GLU 224
PRO 225
-0.0002
PRO 225
THR 226
-0.0397
THR 226
ARG 227
-0.0001
ARG 227
PRO 228
0.0000
PRO 228
SER 229
0.0486
SER 229
ARG 230
0.0001
ARG 230
PHE 231
-0.0005
PHE 231
PHE 232
0.0242
PHE 232
GLY 233
-0.0003
GLY 233
LYS 234
0.0001
LYS 234
ALA 235
-0.0312
ALA 235
VAL 236
-0.0003
VAL 236
THR 237
-0.0001
THR 237
LYS 238
-0.0042
LYS 238
GLU 239
-0.0004
GLU 239
GLN 240
0.0002
GLN 240
LEU 241
-0.0058
LEU 241
GLN 242
-0.0000
GLN 242
ALA 243
-0.0001
ALA 243
LEU 244
0.0052
LEU 244
GLY 245
-0.0003
GLY 245
VAL 246
0.0001
VAL 246
ASN 247
0.0023
ASN 247
ALA 248
-0.0004
ALA 248
GLU 249
0.0001
GLU 249
ASN 250
0.0141
ASN 250
PRO 251
0.0000
PRO 251
PRO 252
0.0001
PRO 252
ALA 253
-0.0199
ALA 253
TYR 254
0.0002
TYR 254
ILE 255
-0.0002
ILE 255
SER 256
-0.0272
SER 256
SER 257
0.0001
SER 257
VAL 258
-0.0001
VAL 258
ALA 259
-0.0066
ALA 259
TYR 260
0.0003
TYR 260
GLY 261
-0.0001
GLY 261
ARG 262
0.0835
ARG 262
GLN 263
-0.0003
GLN 263
VAL 264
0.0002
VAL 264
TYR 265
0.0817
TYR 265
LEU 266
0.0004
LEU 266
LYS 267
0.0001
LYS 267
LEU 268
0.0594
LEU 268
SER 269
0.0000
SER 269
THR 270
-0.0000
THR 270
ASN 271
0.2552
ASN 271
SER 272
-0.0001
SER 272
HIS 273
-0.0002
HIS 273
SER 274
-0.1116
SER 274
THR 275
-0.0004
THR 275
LYS 276
0.0000
LYS 276
VAL 277
0.0052
VAL 277
LYS 278
0.0001
LYS 278
ALA 279
-0.0001
ALA 279
ALA 280
-0.0125
ALA 280
PHE 281
-0.0003
PHE 281
ASP 282
0.0001
ASP 282
ALA 283
0.0145
ALA 283
ALA 284
0.0002
ALA 284
VAL 285
0.0001
VAL 285
SER 286
0.0213
SER 286
GLY 287
-0.0001
GLY 287
LYS 288
-0.0004
LYS 288
SER 289
0.0268
SER 289
VAL 290
-0.0001
VAL 290
SER 291
-0.0003
SER 291
GLY 292
0.0305
GLY 292
ASP 293
0.0002
ASP 293
VAL 294
-0.0000
VAL 294
GLU 295
-0.0167
GLU 295
LEU 296
-0.0001
LEU 296
THR 297
0.0002
THR 297
ASN 298
-0.0334
ASN 298
ILE 299
-0.0001
ILE 299
ILE 300
0.0005
ILE 300
LYS 301
0.0264
LYS 301
ASN 302
0.0001
ASN 302
SER 303
-0.0002
SER 303
SER 304
-0.0024
SER 304
PHE 305
0.0000
PHE 305
LYS 306
-0.0003
LYS 306
ALA 307
0.0449
ALA 307
VAL 308
0.0003
VAL 308
ILE 309
0.0000
ILE 309
TYR 310
0.0122
TYR 310
GLY 311
0.0003
GLY 311
GLY 312
-0.0001
GLY 312
SER 313
0.0067
SER 313
ALA 314
0.0001
ALA 314
LYS 315
-0.0003
LYS 315
ASP 316
0.0019
ASP 316
GLU 317
-0.0003
GLU 317
VAL 318
-0.0003
VAL 318
GLN 319
-0.0156
GLN 319
ILE 320
0.0003
ILE 320
ILE 321
0.0000
ILE 321
ASP 322
-0.0089
ASP 322
GLY 323
0.0000
GLY 323
ASN 324
0.0001
ASN 324
LEU 325
-0.0304
LEU 325
GLY 326
-0.0001
GLY 326
ASP 327
-0.0001
ASP 327
LEU 328
-0.0261
LEU 328
ARG 329
0.0002
ARG 329
ASP 330
0.0001
ASP 330
ILE 331
-0.0276
ILE 331
LEU 332
-0.0004
LEU 332
LYS 333
0.0000
LYS 333
LYS 334
-0.0282
LYS 334
GLY 335
0.0001
GLY 335
ALA 336
-0.0002
ALA 336
THR 337
0.1118
THR 337
PHE 338
-0.0004
PHE 338
ASN 339
-0.0001
ASN 339
ARG 340
0.0393
ARG 340
GLU 341
0.0001
GLU 341
THR 342
-0.0001
THR 342
PRO 343
0.0154
PRO 343
GLY 344
-0.0001
GLY 344
VAL 345
0.0003
VAL 345
PRO 346
0.0102
PRO 346
ILE 347
0.0003
ILE 347
ALA 348
-0.0002
ALA 348
TYR 349
-0.0230
TYR 349
THR 350
0.0000
THR 350
THR 351
0.0003
THR 351
ASN 352
-0.0057
ASN 352
PHE 353
0.0004
PHE 353
LEU 354
-0.0003
LEU 354
LYS 355
-0.0005
LYS 355
ASP 356
-0.0000
ASP 356
ASN 357
-0.0003
ASN 357
GLU 358
0.0951
GLU 358
LEU 359
0.0001
LEU 359
ALA 360
0.0001
ALA 360
VAL 361
0.1565
VAL 361
ILE 362
-0.0000
ILE 362
LYS 363
-0.0001
LYS 363
ASN 364
0.1235
ASN 364
ASN 365
-0.0003
ASN 365
SER 366
0.0002
SER 366
GLU 367
0.1051
GLU 367
TYR 368
0.0001
TYR 368
ILE 369
0.0002
ILE 369
GLU 370
-0.0019
GLU 370
THR 371
-0.0003
THR 371
THR 372
0.0001
THR 372
SER 373
0.0379
SER 373
LYS 374
-0.0001
LYS 374
ALA 375
0.0000
ALA 375
TYR 376
0.1737
TYR 376
THR 377
-0.0003
THR 377
ASP 378
-0.0000
ASP 378
GLY 379
-0.0509
GLY 379
LYS 380
-0.0001
LYS 380
ILE 381
-0.0002
ILE 381
ASN 382
-0.0765
ASN 382
ILE 383
-0.0002
ILE 383
ASP 384
0.0001
ASP 384
HIS 385
-0.0932
HIS 385
SER 386
0.0000
SER 386
GLY 387
0.0003
GLY 387
GLY 388
-0.0623
GLY 388
TYR 389
-0.0000
TYR 389
VAL 390
-0.0001
VAL 390
ALA 391
0.0646
ALA 391
GLN 392
0.0000
GLN 392
PHE 393
0.0002
PHE 393
ASN 394
0.2390
ASN 394
ILE 395
0.0000
ILE 395
SER 396
-0.0004
SER 396
TRP 397
0.3559
TRP 397
ASP 398
0.0000
ASP 398
GLU 399
-0.0000
GLU 399
VAL 400
0.2393
VAL 400
ASN 401
0.0003
ASN 401
TYR 402
0.0001
TYR 402
ASP 403
-0.0617
ASP 403
PRO 404
-0.0005
PRO 404
GLU 405
-0.0001
GLU 405
GLY 406
-0.0118
GLY 406
ASN 407
-0.0003
ASN 407
GLU 408
-0.0001
GLU 408
ILE 409
0.0340
ILE 409
VAL 410
0.0003
VAL 410
GLN 411
-0.0000
GLN 411
HIS 412
0.3077
HIS 412
LYS 413
0.0006
LYS 413
ASN 414
-0.0004
ASN 414
TRP 415
0.0368
TRP 415
SER 416
0.0002
SER 416
GLU 417
0.0001
GLU 417
ASN 418
-0.0183
ASN 418
ASN 419
0.0001
ASN 419
LYS 420
0.0002
LYS 420
SER 421
0.0573
SER 421
LYS 422
-0.0000
LYS 422
LEU 423
0.0001
LEU 423
ALA 424
0.0114
ALA 424
HIS 425
0.0000
HIS 425
PHE 426
0.0002
PHE 426
THR 427
-0.0758
THR 427
SER 428
0.0001
SER 428
SER 429
0.0000
SER 429
ILE 430
-0.0934
ILE 430
TYR 431
-0.0001
TYR 431
LEU 432
-0.0001
LEU 432
PRO 433
0.0166
PRO 433
GLY 434
-0.0000
GLY 434
ASN 435
0.0002
ASN 435
ALA 436
0.1611
ALA 436
ARG 437
-0.0002
ARG 437
ASN 438
-0.0002
ASN 438
ILE 439
0.0971
ILE 439
ASN 440
-0.0001
ASN 440
VAL 441
0.0000
VAL 441
TYR 442
0.2418
TYR 442
ALA 443
-0.0003
ALA 443
LYS 444
0.0002
LYS 444
GLU 445
0.0671
GLU 445
CYS 446
-0.0001
CYS 446
THR 447
0.0001
THR 447
GLY 448
-0.0234
GLY 448
LEU 449
0.0003
LEU 449
ALA 450
-0.0000
ALA 450
TRP 451
-0.0050
TRP 451
GLU 452
0.0002
GLU 452
TRP 453
-0.0002
TRP 453
TRP 454
0.1484
TRP 454
ARG 455
-0.0000
ARG 455
THR 456
-0.0002
THR 456
VAL 457
-0.0089
VAL 457
ILE 458
-0.0001
ILE 458
ASP 459
0.0000
ASP 459
ASP 460
0.1027
ASP 460
ARG 461
0.0000
ARG 461
ASN 462
0.0000
ASN 462
LEU 463
0.0323
LEU 463
PRO 464
0.0002
PRO 464
LEU 465
-0.0001
LEU 465
VAL 466
-0.0456
VAL 466
LYS 467
-0.0001
LYS 467
ASN 468
-0.0002
ASN 468
ARG 469
-0.0554
ARG 469
ASN 470
-0.0002
ASN 470
ILE 471
0.0002
ILE 471
SER 472
-0.0719
SER 472
ILE 473
0.0004
ILE 473
TRP 474
-0.0000
TRP 474
GLY 475
-0.0768
GLY 475
THR 476
0.0003
THR 476
THR 477
-0.0002
THR 477
LEU 478
-0.0044
LEU 478
TYR 479
-0.0000
TYR 479
PRO 480
-0.0003
PRO 480
LYS 481
-0.0489
LYS 481
TYR 482
0.0001
TYR 482
SER 483
-0.0001
SER 483
ASN 484
-0.0832
ASN 484
LYS 485
-0.0001
LYS 485
VAL 486
-0.0002
VAL 486
ASP 487
-0.0209
ASP 487
ASN 488
0.0002
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.