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
-0.0000
PRO 3
PRO 4
-0.0697
PRO 4
ALA 5
0.0000
ALA 5
SER 6
-0.0000
SER 6
PRO 7
-0.1415
PRO 7
PRO 8
0.0000
PRO 8
ALA 9
0.0003
ALA 9
SER 10
-0.0016
SER 10
PRO 11
0.0000
PRO 11
LYS 12
0.0001
LYS 12
THR 13
0.0016
THR 13
PRO 14
0.0003
PRO 14
ILE 15
0.0003
ILE 15
GLU 16
-0.0004
GLU 16
LYS 17
-0.0000
LYS 17
LYS 18
-0.0002
LYS 18
HIS 19
0.0008
HIS 19
ALA 20
-0.0002
ALA 20
ASP 21
-0.0001
ASP 21
GLU 22
-0.0003
GLU 22
ILE 23
0.0003
ILE 23
ASP 24
0.0003
ASP 24
LYS 25
-0.0019
LYS 25
TYR 26
0.0003
TYR 26
ILE 27
-0.0001
ILE 27
GLN 28
0.0024
GLN 28
GLY 29
0.0003
GLY 29
LEU 30
-0.0002
LEU 30
ASP 31
-0.0087
ASP 31
TYR 32
0.0000
TYR 32
ASN 33
-0.0001
ASN 33
LYS 34
0.0038
LYS 34
ASN 35
-0.0003
ASN 35
ASN 36
0.0004
ASN 36
VAL 37
-0.0053
VAL 37
LEU 38
-0.0003
LEU 38
VAL 39
-0.0000
VAL 39
TYR 40
0.0154
TYR 40
HIS 41
-0.0002
HIS 41
GLY 42
-0.0002
GLY 42
ASP 43
0.0625
ASP 43
ALA 44
-0.0002
ALA 44
VAL 45
0.0001
VAL 45
THR 46
-0.0064
THR 46
ASN 47
-0.0003
ASN 47
VAL 48
0.0000
VAL 48
PRO 49
-0.0175
PRO 49
PRO 50
-0.0001
PRO 50
ARG 51
-0.0000
ARG 51
LYS 52
0.0059
LYS 52
GLY 53
0.0001
GLY 53
TYR 54
0.0000
TYR 54
LYS 55
0.0199
LYS 55
ASP 56
0.0000
ASP 56
GLY 57
-0.0002
GLY 57
ASN 58
0.0260
ASN 58
GLU 59
0.0000
GLU 59
TYR 60
-0.0002
TYR 60
ILE 61
-0.0089
ILE 61
VAL 62
0.0001
VAL 62
VAL 63
-0.0001
VAL 63
GLU 64
-0.0120
GLU 64
LYS 65
0.0004
LYS 65
LYS 66
0.0001
LYS 66
LYS 67
-0.0114
LYS 67
LYS 68
-0.0002
LYS 68
SER 69
-0.0000
SER 69
ILE 70
-0.0672
ILE 70
ASN 71
-0.0001
ASN 71
GLN 72
0.0001
GLN 72
ASN 73
-0.0669
ASN 73
ASN 74
0.0001
ASN 74
ALA 75
-0.0004
ALA 75
ASP 76
0.0006
ASP 76
ILE 77
0.0000
ILE 77
GLN 78
-0.0000
GLN 78
VAL 79
-0.0073
VAL 79
VAL 80
0.0001
VAL 80
ASN 81
0.0005
ASN 81
ALA 82
-0.0237
ALA 82
ILE 83
-0.0000
ILE 83
SER 84
0.0000
SER 84
SER 85
0.0143
SER 85
LEU 86
0.0001
LEU 86
THR 87
-0.0002
THR 87
TYR 88
0.0273
TYR 88
PRO 89
0.0002
PRO 89
GLY 90
-0.0004
GLY 90
ALA 91
0.0019
ALA 91
LEU 92
0.0002
LEU 92
VAL 93
-0.0004
VAL 93
LYS 94
0.0023
LYS 94
ALA 95
-0.0005
ALA 95
ASN 96
-0.0001
ASN 96
SER 97
0.0100
SER 97
GLU 98
-0.0005
GLU 98
LEU 99
0.0002
LEU 99
VAL 100
0.0273
VAL 100
GLU 101
0.0001
GLU 101
ASN 102
-0.0000
ASN 102
GLN 103
0.0191
GLN 103
PRO 104
0.0001
PRO 104
ASP 105
-0.0002
ASP 105
VAL 106
0.0323
VAL 106
LEU 107
0.0003
LEU 107
PRO 108
-0.0001
PRO 108
VAL 109
0.0295
VAL 109
LYS 110
0.0000
LYS 110
ARG 111
-0.0002
ARG 111
ASP 112
0.0131
ASP 112
SER 113
0.0001
SER 113
LEU 114
-0.0004
LEU 114
THR 115
0.0163
THR 115
LEU 116
0.0001
LEU 116
SER 117
0.0004
SER 117
ILE 118
0.0056
ILE 118
ASP 119
-0.0003
ASP 119
LEU 120
0.0000
LEU 120
PRO 121
-0.0012
PRO 121
GLY 122
0.0003
GLY 122
MET 123
0.0000
MET 123
THR 124
-0.0495
THR 124
ASN 125
-0.0002
ASN 125
GLN 126
0.0001
GLN 126
ASP 127
0.0373
ASP 127
ASN 128
-0.0000
ASN 128
LYS 129
0.0002
LYS 129
ILE 130
0.0104
ILE 130
VAL 131
-0.0004
VAL 131
VAL 132
-0.0001
VAL 132
LYS 133
-0.0253
LYS 133
ASN 134
-0.0004
ASN 134
ALA 135
-0.0000
ALA 135
THR 136
0.0077
THR 136
LYS 137
-0.0002
LYS 137
SER 138
0.0000
SER 138
ASN 139
0.0354
ASN 139
VAL 140
0.0001
VAL 140
ASN 141
-0.0002
ASN 141
ASN 142
0.0288
ASN 142
ALA 143
0.0001
ALA 143
VAL 144
-0.0000
VAL 144
ASN 145
-0.0009
ASN 145
THR 146
-0.0002
THR 146
LEU 147
0.0002
LEU 147
VAL 148
-0.0283
VAL 148
GLU 149
0.0002
GLU 149
ARG 150
-0.0000
ARG 150
TRP 151
-0.0016
TRP 151
ASN 152
-0.0003
ASN 152
GLU 153
-0.0001
GLU 153
LYS 154
0.0362
LYS 154
TYR 155
0.0002
TYR 155
ALA 156
-0.0000
ALA 156
GLN 157
0.0089
GLN 157
ALA 158
-0.0001
ALA 158
TYR 159
-0.0003
TYR 159
PRO 160
0.0153
PRO 160
ASN 161
0.0001
ASN 161
VAL 162
-0.0002
VAL 162
SER 163
-0.0373
SER 163
ALA 164
0.0000
ALA 164
LYS 165
0.0001
LYS 165
ILE 166
-0.1337
ILE 166
ASP 167
-0.0001
ASP 167
TYR 168
-0.0001
TYR 168
ASP 169
-0.0259
ASP 169
ASP 170
0.0000
ASP 170
GLU 171
-0.0002
GLU 171
MET 172
-0.0451
MET 172
ALA 173
-0.0001
ALA 173
TYR 174
0.0005
TYR 174
SER 175
0.0448
SER 175
GLU 176
-0.0000
GLU 176
SER 177
0.0000
SER 177
GLN 178
-0.0146
GLN 178
LEU 179
-0.0002
LEU 179
ILE 180
0.0003
ILE 180
ALA 181
-0.0023
ALA 181
LYS 182
0.0000
LYS 182
PHE 183
-0.0001
PHE 183
GLY 184
0.0110
GLY 184
THR 185
-0.0002
THR 185
ALA 186
-0.0002
ALA 186
PHE 187
0.0380
PHE 187
LYS 188
-0.0001
LYS 188
ALA 189
0.0003
ALA 189
VAL 190
-0.0186
VAL 190
ASN 191
-0.0001
ASN 191
ASN 192
0.0004
ASN 192
SER 193
-0.0233
SER 193
LEU 194
0.0002
LEU 194
ASN 195
-0.0003
ASN 195
VAL 196
0.0160
VAL 196
ASN 197
0.0001
ASN 197
PHE 198
0.0004
PHE 198
GLY 199
0.0580
GLY 199
ALA 200
-0.0001
ALA 200
ILE 201
-0.0000
ILE 201
SER 202
-0.0152
SER 202
GLU 203
-0.0002
GLU 203
GLY 204
-0.0000
GLY 204
LYS 205
0.0077
LYS 205
MET 206
0.0002
MET 206
GLN 207
-0.0000
GLN 207
GLU 208
0.0114
GLU 208
GLU 209
0.0001
GLU 209
VAL 210
0.0004
VAL 210
ILE 211
-0.0233
ILE 211
SER 212
-0.0002
SER 212
PHE 213
0.0003
PHE 213
LYS 214
-0.0377
LYS 214
GLN 215
0.0001
GLN 215
ILE 216
-0.0000
ILE 216
TYR 217
-0.0563
TYR 217
TYR 218
0.0002
TYR 218
ASN 219
-0.0000
ASN 219
VAL 220
-0.0246
VAL 220
ASN 221
-0.0000
ASN 221
VAL 222
-0.0000
VAL 222
ASN 223
0.0103
ASN 223
GLU 224
-0.0002
GLU 224
PRO 225
0.0002
PRO 225
THR 226
0.0101
THR 226
ARG 227
0.0001
ARG 227
PRO 228
-0.0002
PRO 228
SER 229
-0.0115
SER 229
ARG 230
0.0000
ARG 230
PHE 231
0.0002
PHE 231
PHE 232
-0.0029
PHE 232
GLY 233
0.0001
GLY 233
LYS 234
-0.0001
LYS 234
ALA 235
0.0012
ALA 235
VAL 236
0.0002
VAL 236
THR 237
-0.0001
THR 237
LYS 238
-0.0010
LYS 238
GLU 239
-0.0002
GLU 239
GLN 240
-0.0003
GLN 240
LEU 241
0.0008
LEU 241
GLN 242
0.0002
GLN 242
ALA 243
0.0001
ALA 243
LEU 244
0.0013
LEU 244
GLY 245
0.0003
GLY 245
VAL 246
-0.0001
VAL 246
ASN 247
-0.0036
ASN 247
ALA 248
-0.0003
ALA 248
GLU 249
0.0002
GLU 249
ASN 250
-0.0059
ASN 250
PRO 251
0.0001
PRO 251
PRO 252
0.0001
PRO 252
ALA 253
-0.0031
ALA 253
TYR 254
0.0002
TYR 254
ILE 255
-0.0000
ILE 255
SER 256
0.0026
SER 256
SER 257
-0.0001
SER 257
VAL 258
-0.0002
VAL 258
ALA 259
-0.0062
ALA 259
TYR 260
0.0003
TYR 260
GLY 261
-0.0004
GLY 261
ARG 262
0.0026
ARG 262
GLN 263
-0.0004
GLN 263
VAL 264
-0.0001
VAL 264
TYR 265
0.0071
TYR 265
LEU 266
0.0001
LEU 266
LYS 267
0.0000
LYS 267
LEU 268
0.0139
LEU 268
SER 269
-0.0002
SER 269
THR 270
0.0004
THR 270
ASN 271
0.0334
ASN 271
SER 272
-0.0002
SER 272
HIS 273
-0.0001
HIS 273
SER 274
-0.0457
SER 274
THR 275
-0.0001
THR 275
LYS 276
0.0003
LYS 276
VAL 277
0.0211
VAL 277
LYS 278
0.0001
LYS 278
ALA 279
-0.0003
ALA 279
ALA 280
0.0265
ALA 280
PHE 281
-0.0003
PHE 281
ASP 282
-0.0002
ASP 282
ALA 283
0.0160
ALA 283
ALA 284
-0.0000
ALA 284
VAL 285
0.0001
VAL 285
SER 286
0.0078
SER 286
GLY 287
0.0001
GLY 287
LYS 288
0.0002
LYS 288
SER 289
0.0028
SER 289
VAL 290
-0.0000
VAL 290
SER 291
0.0001
SER 291
GLY 292
0.0099
GLY 292
ASP 293
-0.0000
ASP 293
VAL 294
0.0003
VAL 294
GLU 295
-0.0022
GLU 295
LEU 296
0.0001
LEU 296
THR 297
-0.0004
THR 297
ASN 298
-0.0035
ASN 298
ILE 299
-0.0001
ILE 299
ILE 300
-0.0004
ILE 300
LYS 301
0.0051
LYS 301
ASN 302
0.0002
ASN 302
SER 303
-0.0001
SER 303
SER 304
0.0346
SER 304
PHE 305
-0.0001
PHE 305
LYS 306
0.0002
LYS 306
ALA 307
0.0237
ALA 307
VAL 308
-0.0001
VAL 308
ILE 309
0.0003
ILE 309
TYR 310
0.0258
TYR 310
GLY 311
0.0000
GLY 311
GLY 312
0.0001
GLY 312
SER 313
-0.0301
SER 313
ALA 314
-0.0002
ALA 314
LYS 315
0.0003
LYS 315
ASP 316
0.0131
ASP 316
GLU 317
0.0001
GLU 317
VAL 318
0.0001
VAL 318
GLN 319
0.0129
GLN 319
ILE 320
0.0001
ILE 320
ILE 321
-0.0002
ILE 321
ASP 322
0.0336
ASP 322
GLY 323
-0.0001
GLY 323
ASN 324
0.0001
ASN 324
LEU 325
0.0089
LEU 325
GLY 326
0.0001
GLY 326
ASP 327
-0.0002
ASP 327
LEU 328
0.0022
LEU 328
ARG 329
0.0003
ARG 329
ASP 330
-0.0000
ASP 330
ILE 331
-0.0025
ILE 331
LEU 332
-0.0001
LEU 332
LYS 333
0.0005
LYS 333
LYS 334
-0.0148
LYS 334
GLY 335
0.0003
GLY 335
ALA 336
0.0003
ALA 336
THR 337
-0.0362
THR 337
PHE 338
0.0001
PHE 338
ASN 339
-0.0003
ASN 339
ARG 340
-0.0388
ARG 340
GLU 341
-0.0004
GLU 341
THR 342
0.0002
THR 342
PRO 343
-0.0250
PRO 343
GLY 344
0.0006
GLY 344
VAL 345
0.0002
VAL 345
PRO 346
-0.0187
PRO 346
ILE 347
0.0000
ILE 347
ALA 348
0.0003
ALA 348
TYR 349
0.0045
TYR 349
THR 350
0.0002
THR 350
THR 351
-0.0001
THR 351
ASN 352
0.0108
ASN 352
PHE 353
-0.0004
PHE 353
LEU 354
-0.0001
LEU 354
LYS 355
0.0007
LYS 355
ASP 356
-0.0001
ASP 356
ASN 357
0.0002
ASN 357
GLU 358
-0.0316
GLU 358
LEU 359
-0.0002
LEU 359
ALA 360
-0.0002
ALA 360
VAL 361
-0.0484
VAL 361
ILE 362
0.0002
ILE 362
LYS 363
-0.0001
LYS 363
ASN 364
-0.0329
ASN 364
ASN 365
0.0000
ASN 365
SER 366
-0.0004
SER 366
GLU 367
0.0188
GLU 367
TYR 368
0.0000
TYR 368
ILE 369
0.0002
ILE 369
GLU 370
0.0084
GLU 370
THR 371
0.0002
THR 371
THR 372
0.0000
THR 372
SER 373
0.0191
SER 373
LYS 374
-0.0001
LYS 374
ALA 375
0.0002
ALA 375
TYR 376
0.0657
TYR 376
THR 377
0.0004
THR 377
ASP 378
-0.0002
ASP 378
GLY 379
0.0065
GLY 379
LYS 380
-0.0003
LYS 380
ILE 381
0.0004
ILE 381
ASN 382
0.0014
ASN 382
ILE 383
0.0002
ILE 383
ASP 384
-0.0003
ASP 384
HIS 385
-0.0044
HIS 385
SER 386
0.0000
SER 386
GLY 387
0.0000
GLY 387
GLY 388
-0.0053
GLY 388
TYR 389
0.0000
TYR 389
VAL 390
0.0002
VAL 390
ALA 391
0.0004
ALA 391
GLN 392
-0.0006
GLN 392
PHE 393
0.0001
PHE 393
ASN 394
0.0044
ASN 394
ILE 395
-0.0003
ILE 395
SER 396
-0.0003
SER 396
TRP 397
0.0300
TRP 397
ASP 398
0.0002
ASP 398
GLU 399
-0.0000
GLU 399
VAL 400
0.0163
VAL 400
ASN 401
0.0003
ASN 401
TYR 402
-0.0004
TYR 402
ASP 403
0.0204
ASP 403
PRO 404
0.0004
PRO 404
GLU 405
-0.0001
GLU 405
GLY 406
0.0212
GLY 406
ASN 407
-0.0002
ASN 407
GLU 408
-0.0002
GLU 408
ILE 409
0.0102
ILE 409
VAL 410
-0.0002
VAL 410
GLN 411
-0.0002
GLN 411
HIS 412
-0.0523
HIS 412
LYS 413
0.0001
LYS 413
ASN 414
0.0004
ASN 414
TRP 415
0.0177
TRP 415
SER 416
-0.0002
SER 416
GLU 417
-0.0001
GLU 417
ASN 418
0.0018
ASN 418
ASN 419
-0.0002
ASN 419
LYS 420
-0.0001
LYS 420
SER 421
-0.0000
SER 421
LYS 422
-0.0001
LYS 422
LEU 423
0.0004
LEU 423
ALA 424
0.0046
ALA 424
HIS 425
0.0001
HIS 425
PHE 426
-0.0001
PHE 426
THR 427
-0.0150
THR 427
SER 428
-0.0004
SER 428
SER 429
0.0001
SER 429
ILE 430
-0.0171
ILE 430
TYR 431
0.0001
TYR 431
LEU 432
0.0002
LEU 432
PRO 433
-0.0461
PRO 433
GLY 434
-0.0001
GLY 434
ASN 435
-0.0002
ASN 435
ALA 436
-0.0042
ALA 436
ARG 437
0.0000
ARG 437
ASN 438
-0.0001
ASN 438
ILE 439
0.0389
ILE 439
ASN 440
-0.0002
ASN 440
VAL 441
0.0000
VAL 441
TYR 442
0.0406
TYR 442
ALA 443
-0.0002
ALA 443
LYS 444
0.0002
LYS 444
GLU 445
0.0033
GLU 445
CYS 446
0.0002
CYS 446
THR 447
-0.0000
THR 447
GLY 448
0.0066
GLY 448
LEU 449
-0.0001
LEU 449
ALA 450
0.0001
ALA 450
TRP 451
0.0028
TRP 451
GLU 452
0.0004
GLU 452
TRP 453
0.0000
TRP 453
TRP 454
0.0146
TRP 454
ARG 455
-0.0002
ARG 455
THR 456
-0.0002
THR 456
VAL 457
0.0077
VAL 457
ILE 458
-0.0004
ILE 458
ASP 459
0.0002
ASP 459
ASP 460
0.0383
ASP 460
ARG 461
0.0001
ARG 461
ASN 462
0.0001
ASN 462
LEU 463
-0.0049
LEU 463
PRO 464
-0.0001
PRO 464
LEU 465
-0.0000
LEU 465
VAL 466
-0.0182
VAL 466
LYS 467
0.0001
LYS 467
ASN 468
0.0001
ASN 468
ARG 469
0.0128
ARG 469
ASN 470
0.0000
ASN 470
ILE 471
-0.0000
ILE 471
SER 472
0.0188
SER 472
ILE 473
-0.0003
ILE 473
TRP 474
0.0003
TRP 474
GLY 475
0.0017
GLY 475
THR 476
0.0003
THR 476
THR 477
-0.0001
THR 477
LEU 478
-0.0050
LEU 478
TYR 479
0.0002
TYR 479
PRO 480
-0.0004
PRO 480
LYS 481
0.0174
LYS 481
TYR 482
-0.0002
TYR 482
SER 483
0.0003
SER 483
ASN 484
0.0312
ASN 484
LYS 485
0.0003
LYS 485
VAL 486
-0.0001
VAL 486
ASP 487
-0.0005
ASP 487
ASN 488
0.0003
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.