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
-0.0005
PRO 3
PRO 4
-0.0012
PRO 4
ALA 5
-0.0000
ALA 5
SER 6
-0.0001
SER 6
PRO 7
-0.0045
PRO 7
PRO 8
0.0001
PRO 8
ALA 9
0.0001
ALA 9
SER 10
-0.0001
SER 10
PRO 11
-0.0003
PRO 11
LYS 12
0.0005
LYS 12
THR 13
-0.0008
THR 13
PRO 14
0.0001
PRO 14
ILE 15
-0.0001
ILE 15
GLU 16
-0.0001
GLU 16
LYS 17
0.0000
LYS 17
LYS 18
0.0001
LYS 18
HIS 19
0.0003
HIS 19
ALA 20
-0.0001
ALA 20
ASP 21
-0.0003
ASP 21
GLU 22
-0.0005
GLU 22
ILE 23
-0.0002
ILE 23
ASP 24
-0.0004
ASP 24
LYS 25
0.0005
LYS 25
TYR 26
-0.0002
TYR 26
ILE 27
-0.0002
ILE 27
GLN 28
0.0005
GLN 28
GLY 29
0.0000
GLY 29
LEU 30
-0.0003
LEU 30
ASP 31
-0.0038
ASP 31
TYR 32
-0.0001
TYR 32
ASN 33
0.0000
ASN 33
LYS 34
0.0003
LYS 34
ASN 35
0.0005
ASN 35
ASN 36
0.0002
ASN 36
VAL 37
0.0003
VAL 37
LEU 38
-0.0001
LEU 38
VAL 39
-0.0000
VAL 39
TYR 40
0.0065
TYR 40
HIS 41
0.0000
HIS 41
GLY 42
0.0000
GLY 42
ASP 43
0.0061
ASP 43
ALA 44
0.0003
ALA 44
VAL 45
0.0001
VAL 45
THR 46
-0.0047
THR 46
ASN 47
-0.0000
ASN 47
VAL 48
0.0001
VAL 48
PRO 49
0.0249
PRO 49
PRO 50
-0.0001
PRO 50
ARG 51
-0.0000
ARG 51
LYS 52
0.0049
LYS 52
GLY 53
-0.0003
GLY 53
TYR 54
0.0002
TYR 54
LYS 55
0.0103
LYS 55
ASP 56
-0.0003
ASP 56
GLY 57
0.0005
GLY 57
ASN 58
0.0130
ASN 58
GLU 59
0.0003
GLU 59
TYR 60
0.0001
TYR 60
ILE 61
0.0117
ILE 61
VAL 62
-0.0003
VAL 62
VAL 63
0.0003
VAL 63
GLU 64
-0.0128
GLU 64
LYS 65
0.0002
LYS 65
LYS 66
-0.0005
LYS 66
LYS 67
-0.0360
LYS 67
LYS 68
-0.0000
LYS 68
SER 69
-0.0003
SER 69
ILE 70
-0.0103
ILE 70
ASN 71
0.0004
ASN 71
GLN 72
-0.0001
GLN 72
ASN 73
-0.0149
ASN 73
ASN 74
-0.0003
ASN 74
ALA 75
0.0002
ALA 75
ASP 76
-0.0010
ASP 76
ILE 77
-0.0001
ILE 77
GLN 78
-0.0000
GLN 78
VAL 79
-0.0036
VAL 79
VAL 80
0.0001
VAL 80
ASN 81
-0.0004
ASN 81
ALA 82
0.0007
ALA 82
ILE 83
0.0000
ILE 83
SER 84
-0.0001
SER 84
SER 85
0.0032
SER 85
LEU 86
0.0005
LEU 86
THR 87
0.0000
THR 87
TYR 88
0.0024
TYR 88
PRO 89
-0.0002
PRO 89
GLY 90
0.0002
GLY 90
ALA 91
-0.0020
ALA 91
LEU 92
-0.0001
LEU 92
VAL 93
0.0002
VAL 93
LYS 94
-0.0012
LYS 94
ALA 95
-0.0003
ALA 95
ASN 96
0.0002
ASN 96
SER 97
0.0022
SER 97
GLU 98
-0.0004
GLU 98
LEU 99
-0.0003
LEU 99
VAL 100
0.0014
VAL 100
GLU 101
-0.0001
GLU 101
ASN 102
0.0002
ASN 102
GLN 103
0.0051
GLN 103
PRO 104
-0.0001
PRO 104
ASP 105
0.0001
ASP 105
VAL 106
0.0029
VAL 106
LEU 107
-0.0001
LEU 107
PRO 108
-0.0003
PRO 108
VAL 109
0.0051
VAL 109
LYS 110
-0.0001
LYS 110
ARG 111
-0.0000
ARG 111
ASP 112
-0.0009
ASP 112
SER 113
-0.0002
SER 113
LEU 114
0.0001
LEU 114
THR 115
-0.0031
THR 115
LEU 116
-0.0005
LEU 116
SER 117
0.0003
SER 117
ILE 118
-0.0035
ILE 118
ASP 119
0.0002
ASP 119
LEU 120
-0.0001
LEU 120
PRO 121
0.0017
PRO 121
GLY 122
0.0000
GLY 122
MET 123
0.0002
MET 123
THR 124
-0.0018
THR 124
ASN 125
-0.0001
ASN 125
GLN 126
-0.0000
GLN 126
ASP 127
0.0012
ASP 127
ASN 128
0.0001
ASN 128
LYS 129
0.0003
LYS 129
ILE 130
-0.0029
ILE 130
VAL 131
0.0001
VAL 131
VAL 132
-0.0003
VAL 132
LYS 133
-0.0027
LYS 133
ASN 134
0.0004
ASN 134
ALA 135
-0.0003
ALA 135
THR 136
0.0018
THR 136
LYS 137
0.0004
LYS 137
SER 138
0.0001
SER 138
ASN 139
0.0017
ASN 139
VAL 140
0.0002
VAL 140
ASN 141
-0.0001
ASN 141
ASN 142
0.0009
ASN 142
ALA 143
-0.0004
ALA 143
VAL 144
-0.0003
VAL 144
ASN 145
-0.0002
ASN 145
THR 146
-0.0001
THR 146
LEU 147
-0.0000
LEU 147
VAL 148
0.0005
VAL 148
GLU 149
-0.0000
GLU 149
ARG 150
0.0002
ARG 150
TRP 151
-0.0013
TRP 151
ASN 152
0.0002
ASN 152
GLU 153
-0.0002
GLU 153
LYS 154
0.0015
LYS 154
TYR 155
0.0003
TYR 155
ALA 156
0.0002
ALA 156
GLN 157
0.0008
GLN 157
ALA 158
0.0002
ALA 158
TYR 159
0.0001
TYR 159
PRO 160
0.0001
PRO 160
ASN 161
-0.0002
ASN 161
VAL 162
-0.0001
VAL 162
SER 163
-0.0033
SER 163
ALA 164
0.0001
ALA 164
LYS 165
-0.0000
LYS 165
ILE 166
-0.0219
ILE 166
ASP 167
-0.0000
ASP 167
TYR 168
0.0002
TYR 168
ASP 169
0.0029
ASP 169
ASP 170
-0.0000
ASP 170
GLU 171
0.0002
GLU 171
MET 172
-0.0119
MET 172
ALA 173
-0.0000
ALA 173
TYR 174
0.0000
TYR 174
SER 175
0.0134
SER 175
GLU 176
0.0003
GLU 176
SER 177
0.0000
SER 177
GLN 178
0.0001
GLN 178
LEU 179
0.0005
LEU 179
ILE 180
0.0002
ILE 180
ALA 181
0.0004
ALA 181
LYS 182
0.0002
LYS 182
PHE 183
-0.0000
PHE 183
GLY 184
-0.0035
GLY 184
THR 185
-0.0001
THR 185
ALA 186
-0.0001
ALA 186
PHE 187
0.0128
PHE 187
LYS 188
-0.0003
LYS 188
ALA 189
0.0000
ALA 189
VAL 190
-0.0020
VAL 190
ASN 191
0.0000
ASN 191
ASN 192
0.0000
ASN 192
SER 193
-0.0079
SER 193
LEU 194
-0.0000
LEU 194
ASN 195
-0.0001
ASN 195
VAL 196
0.0027
VAL 196
ASN 197
-0.0001
ASN 197
PHE 198
0.0002
PHE 198
GLY 199
0.0347
GLY 199
ALA 200
-0.0002
ALA 200
ILE 201
-0.0002
ILE 201
SER 202
-0.0073
SER 202
GLU 203
0.0000
GLU 203
GLY 204
-0.0001
GLY 204
LYS 205
-0.0000
LYS 205
MET 206
-0.0001
MET 206
GLN 207
0.0001
GLN 207
GLU 208
-0.0035
GLU 208
GLU 209
-0.0003
GLU 209
VAL 210
-0.0001
VAL 210
ILE 211
0.0009
ILE 211
SER 212
0.0001
SER 212
PHE 213
0.0002
PHE 213
LYS 214
-0.0088
LYS 214
GLN 215
0.0001
GLN 215
ILE 216
0.0002
ILE 216
TYR 217
-0.0070
TYR 217
TYR 218
-0.0002
TYR 218
ASN 219
0.0002
ASN 219
VAL 220
-0.0081
VAL 220
ASN 221
-0.0001
ASN 221
VAL 222
0.0002
VAL 222
ASN 223
-0.0004
ASN 223
GLU 224
0.0002
GLU 224
PRO 225
-0.0000
PRO 225
THR 226
0.0003
THR 226
ARG 227
0.0002
ARG 227
PRO 228
-0.0001
PRO 228
SER 229
-0.0020
SER 229
ARG 230
-0.0005
ARG 230
PHE 231
-0.0000
PHE 231
PHE 232
-0.0008
PHE 232
GLY 233
-0.0003
GLY 233
LYS 234
0.0002
LYS 234
ALA 235
-0.0004
ALA 235
VAL 236
0.0000
VAL 236
THR 237
0.0001
THR 237
LYS 238
-0.0011
LYS 238
GLU 239
-0.0001
GLU 239
GLN 240
0.0002
GLN 240
LEU 241
-0.0007
LEU 241
GLN 242
0.0001
GLN 242
ALA 243
-0.0001
ALA 243
LEU 244
0.0011
LEU 244
GLY 245
-0.0001
GLY 245
VAL 246
-0.0002
VAL 246
ASN 247
-0.0016
ASN 247
ALA 248
-0.0002
ALA 248
GLU 249
-0.0001
GLU 249
ASN 250
0.0008
ASN 250
PRO 251
0.0003
PRO 251
PRO 252
-0.0001
PRO 252
ALA 253
-0.0009
ALA 253
TYR 254
-0.0000
TYR 254
ILE 255
0.0003
ILE 255
SER 256
-0.0001
SER 256
SER 257
-0.0002
SER 257
VAL 258
0.0000
VAL 258
ALA 259
-0.0035
ALA 259
TYR 260
-0.0002
TYR 260
GLY 261
0.0001
GLY 261
ARG 262
0.0004
ARG 262
GLN 263
-0.0002
GLN 263
VAL 264
0.0000
VAL 264
TYR 265
0.0021
TYR 265
LEU 266
-0.0002
LEU 266
LYS 267
0.0002
LYS 267
LEU 268
0.0026
LEU 268
SER 269
-0.0002
SER 269
THR 270
0.0003
THR 270
ASN 271
0.0242
ASN 271
SER 272
-0.0002
SER 272
HIS 273
-0.0005
HIS 273
SER 274
-0.0226
SER 274
THR 275
0.0003
THR 275
LYS 276
0.0001
LYS 276
VAL 277
0.0065
VAL 277
LYS 278
0.0002
LYS 278
ALA 279
-0.0004
ALA 279
ALA 280
0.0105
ALA 280
PHE 281
0.0000
PHE 281
ASP 282
0.0001
ASP 282
ALA 283
0.0084
ALA 283
ALA 284
-0.0001
ALA 284
VAL 285
-0.0004
VAL 285
SER 286
0.0037
SER 286
GLY 287
-0.0000
GLY 287
LYS 288
-0.0001
LYS 288
SER 289
0.0028
SER 289
VAL 290
-0.0001
VAL 290
SER 291
-0.0002
SER 291
GLY 292
0.0037
GLY 292
ASP 293
0.0000
ASP 293
VAL 294
0.0002
VAL 294
GLU 295
-0.0003
GLU 295
LEU 296
0.0001
LEU 296
THR 297
-0.0001
THR 297
ASN 298
-0.0038
ASN 298
ILE 299
0.0003
ILE 299
ILE 300
-0.0003
ILE 300
LYS 301
-0.0012
LYS 301
ASN 302
0.0003
ASN 302
SER 303
-0.0002
SER 303
SER 304
0.0118
SER 304
PHE 305
0.0002
PHE 305
LYS 306
0.0001
LYS 306
ALA 307
0.0058
ALA 307
VAL 308
-0.0001
VAL 308
ILE 309
-0.0002
ILE 309
TYR 310
0.0073
TYR 310
GLY 311
-0.0002
GLY 311
GLY 312
-0.0001
GLY 312
SER 313
-0.0045
SER 313
ALA 314
-0.0001
ALA 314
LYS 315
0.0002
LYS 315
ASP 316
0.0014
ASP 316
GLU 317
0.0001
GLU 317
VAL 318
0.0001
VAL 318
GLN 319
0.0079
GLN 319
ILE 320
0.0005
ILE 320
ILE 321
-0.0004
ILE 321
ASP 322
0.0098
ASP 322
GLY 323
0.0000
GLY 323
ASN 324
0.0001
ASN 324
LEU 325
0.0018
LEU 325
GLY 326
-0.0001
GLY 326
ASP 327
0.0003
ASP 327
LEU 328
0.0006
LEU 328
ARG 329
0.0001
ARG 329
ASP 330
0.0000
ASP 330
ILE 331
-0.0000
ILE 331
LEU 332
0.0001
LEU 332
LYS 333
-0.0004
LYS 333
LYS 334
-0.0028
LYS 334
GLY 335
-0.0001
GLY 335
ALA 336
-0.0001
ALA 336
THR 337
-0.0071
THR 337
PHE 338
0.0002
PHE 338
ASN 339
0.0004
ASN 339
ARG 340
-0.0034
ARG 340
GLU 341
-0.0002
GLU 341
THR 342
-0.0001
THR 342
PRO 343
-0.0018
PRO 343
GLY 344
0.0004
GLY 344
VAL 345
0.0002
VAL 345
PRO 346
-0.0008
PRO 346
ILE 347
-0.0001
ILE 347
ALA 348
0.0001
ALA 348
TYR 349
-0.0024
TYR 349
THR 350
0.0002
THR 350
THR 351
0.0000
THR 351
ASN 352
0.0005
ASN 352
PHE 353
0.0001
PHE 353
LEU 354
0.0001
LEU 354
LYS 355
0.0004
LYS 355
ASP 356
-0.0003
ASP 356
ASN 357
0.0002
ASN 357
GLU 358
-0.0032
GLU 358
LEU 359
0.0002
LEU 359
ALA 360
-0.0002
ALA 360
VAL 361
-0.0084
VAL 361
ILE 362
0.0000
ILE 362
LYS 363
0.0001
LYS 363
ASN 364
-0.0080
ASN 364
ASN 365
0.0004
ASN 365
SER 366
-0.0004
SER 366
GLU 367
-0.0024
GLU 367
TYR 368
-0.0002
TYR 368
ILE 369
-0.0000
ILE 369
GLU 370
-0.0101
GLU 370
THR 371
0.0000
THR 371
THR 372
0.0004
THR 372
SER 373
-0.0448
SER 373
LYS 374
0.0003
LYS 374
ALA 375
-0.0004
ALA 375
TYR 376
-0.0482
TYR 376
THR 377
0.0001
THR 377
ASP 378
0.0003
ASP 378
GLY 379
0.0260
GLY 379
LYS 380
0.0001
LYS 380
ILE 381
-0.0001
ILE 381
ASN 382
0.0020
ASN 382
ILE 383
0.0001
ILE 383
ASP 384
-0.0000
ASP 384
HIS 385
0.0021
HIS 385
SER 386
0.0004
SER 386
GLY 387
-0.0002
GLY 387
GLY 388
0.0024
GLY 388
TYR 389
0.0000
TYR 389
VAL 390
0.0003
VAL 390
ALA 391
0.0006
ALA 391
GLN 392
-0.0001
GLN 392
PHE 393
-0.0001
PHE 393
ASN 394
-0.0006
ASN 394
ILE 395
-0.0003
ILE 395
SER 396
0.0001
SER 396
TRP 397
-0.0131
TRP 397
ASP 398
0.0001
ASP 398
GLU 399
0.0002
GLU 399
VAL 400
-0.0146
VAL 400
ASN 401
-0.0002
ASN 401
TYR 402
0.0001
TYR 402
ASP 403
-0.0168
ASP 403
PRO 404
0.0001
PRO 404
GLU 405
0.0003
GLU 405
GLY 406
-0.0193
GLY 406
ASN 407
0.0001
ASN 407
GLU 408
-0.0001
GLU 408
ILE 409
-0.0056
ILE 409
VAL 410
-0.0002
VAL 410
GLN 411
0.0002
GLN 411
HIS 412
0.0358
HIS 412
LYS 413
0.0001
LYS 413
ASN 414
-0.0001
ASN 414
TRP 415
-0.0016
TRP 415
SER 416
-0.0000
SER 416
GLU 417
-0.0003
GLU 417
ASN 418
-0.0014
ASN 418
ASN 419
0.0002
ASN 419
LYS 420
0.0003
LYS 420
SER 421
0.0007
SER 421
LYS 422
0.0003
LYS 422
LEU 423
-0.0004
LEU 423
ALA 424
-0.0010
ALA 424
HIS 425
0.0000
HIS 425
PHE 426
0.0000
PHE 426
THR 427
0.0042
THR 427
SER 428
-0.0000
SER 428
SER 429
0.0003
SER 429
ILE 430
0.0081
ILE 430
TYR 431
0.0002
TYR 431
LEU 432
0.0000
LEU 432
PRO 433
0.0381
PRO 433
GLY 434
-0.0000
GLY 434
ASN 435
-0.0003
ASN 435
ALA 436
0.0160
ALA 436
ARG 437
0.0001
ARG 437
ASN 438
0.0002
ASN 438
ILE 439
-0.0236
ILE 439
ASN 440
-0.0002
ASN 440
VAL 441
-0.0000
VAL 441
TYR 442
-0.0141
TYR 442
ALA 443
0.0001
ALA 443
LYS 444
-0.0000
LYS 444
GLU 445
-0.0013
GLU 445
CYS 446
0.0000
CYS 446
THR 447
0.0001
THR 447
GLY 448
-0.0009
GLY 448
LEU 449
0.0006
LEU 449
ALA 450
-0.0003
ALA 450
TRP 451
0.0005
TRP 451
GLU 452
0.0003
GLU 452
TRP 453
0.0002
TRP 453
TRP 454
-0.0031
TRP 454
ARG 455
-0.0002
ARG 455
THR 456
0.0002
THR 456
VAL 457
-0.0005
VAL 457
ILE 458
0.0001
ILE 458
ASP 459
0.0002
ASP 459
ASP 460
-0.0107
ASP 460
ARG 461
0.0001
ARG 461
ASN 462
-0.0003
ASN 462
LEU 463
0.0022
LEU 463
PRO 464
-0.0000
PRO 464
LEU 465
0.0001
LEU 465
VAL 466
-0.0027
VAL 466
LYS 467
-0.0001
LYS 467
ASN 468
-0.0000
ASN 468
ARG 469
0.0005
ARG 469
ASN 470
-0.0004
ASN 470
ILE 471
-0.0001
ILE 471
SER 472
-0.0041
SER 472
ILE 473
0.0001
ILE 473
TRP 474
-0.0000
TRP 474
GLY 475
-0.0003
GLY 475
THR 476
0.0002
THR 476
THR 477
0.0000
THR 477
LEU 478
0.0021
LEU 478
TYR 479
-0.0001
TYR 479
PRO 480
0.0001
PRO 480
LYS 481
-0.0027
LYS 481
TYR 482
0.0003
TYR 482
SER 483
-0.0003
SER 483
ASN 484
-0.0056
ASN 484
LYS 485
0.0000
LYS 485
VAL 486
-0.0003
VAL 486
ASP 487
0.0003
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.