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
-0.0001
ALA 2
PRO 3
0.0001
PRO 3
PRO 4
-0.4310
PRO 4
ALA 5
-0.0001
ALA 5
SER 6
0.0002
SER 6
PRO 7
-0.0953
PRO 7
PRO 8
0.0002
PRO 8
ALA 9
-0.0000
ALA 9
SER 10
0.0817
SER 10
PRO 11
-0.0001
PRO 11
LYS 12
0.0003
LYS 12
THR 13
0.0077
THR 13
PRO 14
0.0002
PRO 14
ILE 15
-0.0004
ILE 15
GLU 16
0.0243
GLU 16
LYS 17
-0.0003
LYS 17
LYS 18
0.0001
LYS 18
HIS 19
0.0012
HIS 19
ALA 20
-0.0003
ALA 20
ASP 21
-0.0001
ASP 21
GLU 22
-0.0169
GLU 22
ILE 23
-0.0002
ILE 23
ASP 24
0.0001
ASP 24
LYS 25
0.0403
LYS 25
TYR 26
-0.0003
TYR 26
ILE 27
0.0001
ILE 27
GLN 28
0.0242
GLN 28
GLY 29
-0.0001
GLY 29
LEU 30
0.0001
LEU 30
ASP 31
-0.1056
ASP 31
TYR 32
-0.0004
TYR 32
ASN 33
0.0001
ASN 33
LYS 34
0.0064
LYS 34
ASN 35
0.0001
ASN 35
ASN 36
0.0001
ASN 36
VAL 37
0.0236
VAL 37
LEU 38
0.0002
LEU 38
VAL 39
-0.0003
VAL 39
TYR 40
-0.0677
TYR 40
HIS 41
0.0002
HIS 41
GLY 42
-0.0002
GLY 42
ASP 43
0.0941
ASP 43
ALA 44
0.0003
ALA 44
VAL 45
0.0002
VAL 45
THR 46
-0.0174
THR 46
ASN 47
0.0001
ASN 47
VAL 48
0.0001
VAL 48
PRO 49
-0.0072
PRO 49
PRO 50
0.0004
PRO 50
ARG 51
-0.0003
ARG 51
LYS 52
0.0767
LYS 52
GLY 53
-0.0003
GLY 53
TYR 54
-0.0004
TYR 54
LYS 55
0.1138
LYS 55
ASP 56
-0.0001
ASP 56
GLY 57
-0.0002
GLY 57
ASN 58
0.0307
ASN 58
GLU 59
-0.0000
GLU 59
TYR 60
-0.0002
TYR 60
ILE 61
0.0569
ILE 61
VAL 62
0.0000
VAL 62
VAL 63
0.0001
VAL 63
GLU 64
0.1255
GLU 64
LYS 65
-0.0004
LYS 65
LYS 66
0.0003
LYS 66
LYS 67
0.1043
LYS 67
LYS 68
-0.0003
LYS 68
SER 69
0.0002
SER 69
ILE 70
-0.0122
ILE 70
ASN 71
-0.0001
ASN 71
GLN 72
-0.0002
GLN 72
ASN 73
0.0302
ASN 73
ASN 74
-0.0001
ASN 74
ALA 75
-0.0002
ALA 75
ASP 76
-0.0306
ASP 76
ILE 77
-0.0001
ILE 77
GLN 78
-0.0005
GLN 78
VAL 79
0.0123
VAL 79
VAL 80
0.0002
VAL 80
ASN 81
-0.0005
ASN 81
ALA 82
-0.0094
ALA 82
ILE 83
0.0000
ILE 83
SER 84
0.0000
SER 84
SER 85
0.0195
SER 85
LEU 86
0.0000
LEU 86
THR 87
0.0003
THR 87
TYR 88
-0.0225
TYR 88
PRO 89
-0.0001
PRO 89
GLY 90
-0.0002
GLY 90
ALA 91
-0.0228
ALA 91
LEU 92
-0.0001
LEU 92
VAL 93
-0.0001
VAL 93
LYS 94
-0.0224
LYS 94
ALA 95
0.0001
ALA 95
ASN 96
-0.0002
ASN 96
SER 97
-0.0282
SER 97
GLU 98
0.0002
GLU 98
LEU 99
0.0001
LEU 99
VAL 100
0.0255
VAL 100
GLU 101
0.0000
GLU 101
ASN 102
0.0000
ASN 102
GLN 103
0.0198
GLN 103
PRO 104
0.0000
PRO 104
ASP 105
-0.0001
ASP 105
VAL 106
0.0246
VAL 106
LEU 107
0.0004
LEU 107
PRO 108
-0.0002
PRO 108
VAL 109
0.0870
VAL 109
LYS 110
-0.0000
LYS 110
ARG 111
-0.0004
ARG 111
ASP 112
-0.0426
ASP 112
SER 113
-0.0001
SER 113
LEU 114
0.0000
LEU 114
THR 115
0.0341
THR 115
LEU 116
0.0001
LEU 116
SER 117
-0.0002
SER 117
ILE 118
-0.0090
ILE 118
ASP 119
-0.0001
ASP 119
LEU 120
0.0001
LEU 120
PRO 121
0.0299
PRO 121
GLY 122
0.0002
GLY 122
MET 123
-0.0000
MET 123
THR 124
0.0688
THR 124
ASN 125
0.0000
ASN 125
GLN 126
-0.0002
GLN 126
ASP 127
-0.1011
ASP 127
ASN 128
-0.0002
ASN 128
LYS 129
-0.0000
LYS 129
ILE 130
-0.1673
ILE 130
VAL 131
-0.0001
VAL 131
VAL 132
-0.0002
VAL 132
LYS 133
0.0292
LYS 133
ASN 134
-0.0003
ASN 134
ALA 135
0.0001
ALA 135
THR 136
0.0023
THR 136
LYS 137
0.0003
LYS 137
SER 138
-0.0001
SER 138
ASN 139
-0.0034
ASN 139
VAL 140
-0.0001
VAL 140
ASN 141
-0.0002
ASN 141
ASN 142
-0.1067
ASN 142
ALA 143
0.0003
ALA 143
VAL 144
0.0004
VAL 144
ASN 145
0.0104
ASN 145
THR 146
-0.0000
THR 146
LEU 147
-0.0002
LEU 147
VAL 148
0.0231
VAL 148
GLU 149
-0.0002
GLU 149
ARG 150
0.0004
ARG 150
TRP 151
0.0276
TRP 151
ASN 152
0.0001
ASN 152
GLU 153
0.0002
GLU 153
LYS 154
-0.0417
LYS 154
TYR 155
0.0000
TYR 155
ALA 156
0.0002
ALA 156
GLN 157
-0.0179
GLN 157
ALA 158
-0.0004
ALA 158
TYR 159
0.0001
TYR 159
PRO 160
-0.0747
PRO 160
ASN 161
-0.0003
ASN 161
VAL 162
-0.0001
VAL 162
SER 163
0.1120
SER 163
ALA 164
-0.0002
ALA 164
LYS 165
0.0001
LYS 165
ILE 166
0.2779
ILE 166
ASP 167
-0.0003
ASP 167
TYR 168
0.0002
TYR 168
ASP 169
0.0541
ASP 169
ASP 170
0.0003
ASP 170
GLU 171
-0.0002
GLU 171
MET 172
0.0283
MET 172
ALA 173
-0.0002
ALA 173
TYR 174
-0.0003
TYR 174
SER 175
0.0089
SER 175
GLU 176
-0.0003
GLU 176
SER 177
0.0001
SER 177
GLN 178
-0.0176
GLN 178
LEU 179
-0.0000
LEU 179
ILE 180
0.0003
ILE 180
ALA 181
-0.0184
ALA 181
LYS 182
-0.0000
LYS 182
PHE 183
0.0001
PHE 183
GLY 184
0.0200
GLY 184
THR 185
0.0000
THR 185
ALA 186
-0.0001
ALA 186
PHE 187
0.0052
PHE 187
LYS 188
-0.0001
LYS 188
ALA 189
0.0002
ALA 189
VAL 190
-0.0157
VAL 190
ASN 191
-0.0004
ASN 191
ASN 192
-0.0000
ASN 192
SER 193
-0.0078
SER 193
LEU 194
0.0004
LEU 194
ASN 195
0.0002
ASN 195
VAL 196
0.0209
VAL 196
ASN 197
0.0001
ASN 197
PHE 198
-0.0000
PHE 198
GLY 199
0.0670
GLY 199
ALA 200
0.0001
ALA 200
ILE 201
0.0001
ILE 201
SER 202
0.0222
SER 202
GLU 203
-0.0002
GLU 203
GLY 204
-0.0001
GLY 204
LYS 205
-0.0202
LYS 205
MET 206
-0.0005
MET 206
GLN 207
0.0003
GLN 207
GLU 208
0.0254
GLU 208
GLU 209
0.0003
GLU 209
VAL 210
-0.0001
VAL 210
ILE 211
0.1070
ILE 211
SER 212
-0.0003
SER 212
PHE 213
0.0001
PHE 213
LYS 214
0.1280
LYS 214
GLN 215
-0.0000
GLN 215
ILE 216
0.0003
ILE 216
TYR 217
0.1504
TYR 217
TYR 218
0.0004
TYR 218
ASN 219
-0.0001
ASN 219
VAL 220
0.0380
VAL 220
ASN 221
-0.0000
ASN 221
VAL 222
-0.0001
VAL 222
ASN 223
0.0082
ASN 223
GLU 224
0.0004
GLU 224
PRO 225
0.0000
PRO 225
THR 226
0.0849
THR 226
ARG 227
0.0000
ARG 227
PRO 228
-0.0003
PRO 228
SER 229
-0.0390
SER 229
ARG 230
0.0002
ARG 230
PHE 231
-0.0001
PHE 231
PHE 232
0.0023
PHE 232
GLY 233
-0.0000
GLY 233
LYS 234
0.0000
LYS 234
ALA 235
-0.0261
ALA 235
VAL 236
-0.0000
VAL 236
THR 237
0.0003
THR 237
LYS 238
-0.0187
LYS 238
GLU 239
0.0004
GLU 239
GLN 240
-0.0004
GLN 240
LEU 241
-0.0015
LEU 241
GLN 242
0.0002
GLN 242
ALA 243
-0.0004
ALA 243
LEU 244
-0.0036
LEU 244
GLY 245
0.0000
GLY 245
VAL 246
-0.0001
VAL 246
ASN 247
0.0014
ASN 247
ALA 248
0.0002
ALA 248
GLU 249
0.0005
GLU 249
ASN 250
0.0115
ASN 250
PRO 251
0.0001
PRO 251
PRO 252
-0.0004
PRO 252
ALA 253
0.0099
ALA 253
TYR 254
-0.0001
TYR 254
ILE 255
-0.0003
ILE 255
SER 256
-0.0062
SER 256
SER 257
-0.0000
SER 257
VAL 258
0.0002
VAL 258
ALA 259
0.0062
ALA 259
TYR 260
-0.0000
TYR 260
GLY 261
0.0002
GLY 261
ARG 262
0.1128
ARG 262
GLN 263
-0.0000
GLN 263
VAL 264
-0.0001
VAL 264
TYR 265
0.0646
TYR 265
LEU 266
-0.0003
LEU 266
LYS 267
-0.0001
LYS 267
LEU 268
-0.0098
LEU 268
SER 269
0.0004
SER 269
THR 270
-0.0003
THR 270
ASN 271
0.0302
ASN 271
SER 272
-0.0002
SER 272
HIS 273
0.0004
HIS 273
SER 274
-0.0943
SER 274
THR 275
-0.0002
THR 275
LYS 276
-0.0001
LYS 276
VAL 277
0.0577
VAL 277
LYS 278
-0.0000
LYS 278
ALA 279
0.0001
ALA 279
ALA 280
0.0011
ALA 280
PHE 281
0.0003
PHE 281
ASP 282
0.0000
ASP 282
ALA 283
0.0496
ALA 283
ALA 284
-0.0003
ALA 284
VAL 285
-0.0004
VAL 285
SER 286
0.0497
SER 286
GLY 287
0.0001
GLY 287
LYS 288
-0.0000
LYS 288
SER 289
0.0513
SER 289
VAL 290
-0.0000
VAL 290
SER 291
-0.0003
SER 291
GLY 292
0.0402
GLY 292
ASP 293
0.0001
ASP 293
VAL 294
0.0001
VAL 294
GLU 295
-0.0456
GLU 295
LEU 296
0.0001
LEU 296
THR 297
0.0002
THR 297
ASN 298
-0.0655
ASN 298
ILE 299
0.0001
ILE 299
ILE 300
-0.0000
ILE 300
LYS 301
0.0312
LYS 301
ASN 302
-0.0002
ASN 302
SER 303
0.0003
SER 303
SER 304
-0.0946
SER 304
PHE 305
-0.0001
PHE 305
LYS 306
-0.0000
LYS 306
ALA 307
0.0054
ALA 307
VAL 308
-0.0001
VAL 308
ILE 309
0.0001
ILE 309
TYR 310
0.0014
TYR 310
GLY 311
0.0002
GLY 311
GLY 312
-0.0002
GLY 312
SER 313
0.0103
SER 313
ALA 314
-0.0002
ALA 314
LYS 315
0.0000
LYS 315
ASP 316
-0.0088
ASP 316
GLU 317
-0.0002
GLU 317
VAL 318
-0.0003
VAL 318
GLN 319
-0.0367
GLN 319
ILE 320
-0.0006
ILE 320
ILE 321
0.0002
ILE 321
ASP 322
-0.0662
ASP 322
GLY 323
-0.0002
GLY 323
ASN 324
0.0001
ASN 324
LEU 325
-0.0287
LEU 325
GLY 326
-0.0001
GLY 326
ASP 327
-0.0002
ASP 327
LEU 328
0.0002
LEU 328
ARG 329
-0.0001
ARG 329
ASP 330
0.0006
ASP 330
ILE 331
-0.0160
ILE 331
LEU 332
0.0002
LEU 332
LYS 333
0.0001
LYS 333
LYS 334
-0.0321
LYS 334
GLY 335
-0.0001
GLY 335
ALA 336
0.0001
ALA 336
THR 337
0.1322
THR 337
PHE 338
-0.0000
PHE 338
ASN 339
-0.0001
ASN 339
ARG 340
0.1092
ARG 340
GLU 341
-0.0002
GLU 341
THR 342
0.0001
THR 342
PRO 343
0.0785
PRO 343
GLY 344
0.0004
GLY 344
VAL 345
-0.0003
VAL 345
PRO 346
0.0117
PRO 346
ILE 347
-0.0003
ILE 347
ALA 348
-0.0001
ALA 348
TYR 349
-0.0171
TYR 349
THR 350
-0.0001
THR 350
THR 351
0.0002
THR 351
ASN 352
-0.0241
ASN 352
PHE 353
0.0001
PHE 353
LEU 354
-0.0003
LEU 354
LYS 355
-0.0077
LYS 355
ASP 356
0.0003
ASP 356
ASN 357
0.0003
ASN 357
GLU 358
0.0163
GLU 358
LEU 359
0.0003
LEU 359
ALA 360
0.0002
ALA 360
VAL 361
0.0201
VAL 361
ILE 362
0.0001
ILE 362
LYS 363
0.0000
LYS 363
ASN 364
-0.0197
ASN 364
ASN 365
-0.0001
ASN 365
SER 366
-0.0000
SER 366
GLU 367
0.0736
GLU 367
TYR 368
0.0002
TYR 368
ILE 369
0.0001
ILE 369
GLU 370
-0.0202
GLU 370
THR 371
0.0003
THR 371
THR 372
-0.0003
THR 372
SER 373
0.1181
SER 373
LYS 374
-0.0002
LYS 374
ALA 375
-0.0002
ALA 375
TYR 376
0.0766
TYR 376
THR 377
-0.0001
THR 377
ASP 378
-0.0002
ASP 378
GLY 379
0.2580
GLY 379
LYS 380
0.0004
LYS 380
ILE 381
0.0001
ILE 381
ASN 382
0.1162
ASN 382
ILE 383
0.0001
ILE 383
ASP 384
-0.0003
ASP 384
HIS 385
0.1065
HIS 385
SER 386
-0.0000
SER 386
GLY 387
-0.0002
GLY 387
GLY 388
0.0602
GLY 388
TYR 389
-0.0003
TYR 389
VAL 390
-0.0001
VAL 390
ALA 391
-0.0200
ALA 391
GLN 392
-0.0003
GLN 392
PHE 393
-0.0001
PHE 393
ASN 394
-0.1146
ASN 394
ILE 395
-0.0004
ILE 395
SER 396
0.0001
SER 396
TRP 397
-0.1491
TRP 397
ASP 398
-0.0001
ASP 398
GLU 399
0.0002
GLU 399
VAL 400
0.0294
VAL 400
ASN 401
0.0004
ASN 401
TYR 402
-0.0000
TYR 402
ASP 403
0.0457
ASP 403
PRO 404
0.0002
PRO 404
GLU 405
0.0001
GLU 405
GLY 406
0.0028
GLY 406
ASN 407
0.0001
ASN 407
GLU 408
-0.0002
GLU 408
ILE 409
0.0764
ILE 409
VAL 410
0.0001
VAL 410
GLN 411
0.0001
GLN 411
HIS 412
-0.1251
HIS 412
LYS 413
0.0001
LYS 413
ASN 414
-0.0004
ASN 414
TRP 415
0.0711
TRP 415
SER 416
0.0000
SER 416
GLU 417
0.0001
GLU 417
ASN 418
-0.0089
ASN 418
ASN 419
0.0002
ASN 419
LYS 420
-0.0000
LYS 420
SER 421
-0.0152
SER 421
LYS 422
-0.0001
LYS 422
LEU 423
0.0000
LEU 423
ALA 424
-0.0021
ALA 424
HIS 425
-0.0002
HIS 425
PHE 426
0.0003
PHE 426
THR 427
0.0768
THR 427
SER 428
0.0000
SER 428
SER 429
-0.0001
SER 429
ILE 430
0.1417
ILE 430
TYR 431
0.0000
TYR 431
LEU 432
0.0001
LEU 432
PRO 433
0.1281
PRO 433
GLY 434
-0.0003
GLY 434
ASN 435
-0.0000
ASN 435
ALA 436
-0.0470
ALA 436
ARG 437
-0.0005
ARG 437
ASN 438
0.0002
ASN 438
ILE 439
-0.0462
ILE 439
ASN 440
0.0001
ASN 440
VAL 441
-0.0004
VAL 441
TYR 442
-0.0971
TYR 442
ALA 443
-0.0003
ALA 443
LYS 444
0.0001
LYS 444
GLU 445
-0.0259
GLU 445
CYS 446
0.0002
CYS 446
THR 447
-0.0001
THR 447
GLY 448
0.0287
GLY 448
LEU 449
-0.0003
LEU 449
ALA 450
-0.0001
ALA 450
TRP 451
0.0139
TRP 451
GLU 452
-0.0002
GLU 452
TRP 453
0.0001
TRP 453
TRP 454
-0.0813
TRP 454
ARG 455
-0.0000
ARG 455
THR 456
0.0005
THR 456
VAL 457
0.0342
VAL 457
ILE 458
0.0002
ILE 458
ASP 459
0.0003
ASP 459
ASP 460
-0.0290
ASP 460
ARG 461
0.0003
ARG 461
ASN 462
-0.0002
ASN 462
LEU 463
-0.0256
LEU 463
PRO 464
0.0005
PRO 464
LEU 465
-0.0004
LEU 465
VAL 466
-0.0065
VAL 466
LYS 467
0.0002
LYS 467
ASN 468
0.0000
ASN 468
ARG 469
0.0964
ARG 469
ASN 470
0.0002
ASN 470
ILE 471
0.0000
ILE 471
SER 472
0.1146
SER 472
ILE 473
0.0002
ILE 473
TRP 474
0.0002
TRP 474
GLY 475
0.0793
GLY 475
THR 476
0.0002
THR 476
THR 477
-0.0002
THR 477
LEU 478
0.0048
LEU 478
TYR 479
0.0002
TYR 479
PRO 480
0.0002
PRO 480
LYS 481
0.0751
LYS 481
TYR 482
0.0002
TYR 482
SER 483
0.0002
SER 483
ASN 484
0.1159
ASN 484
LYS 485
-0.0000
LYS 485
VAL 486
0.0000
VAL 486
ASP 487
0.0255
ASP 487
ASN 488
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.