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
GLN 2
-0.0002
GLN 2
LEU 3
-0.0000
LEU 3
ILE 4
0.0027
ILE 4
TRP 5
0.0000
TRP 5
LEU 6
0.0003
LEU 6
ARG 7
-0.0031
ARG 7
SER 8
0.0005
SER 8
ASP 9
-0.0002
ASP 9
LEU 10
-0.0018
LEU 10
ARG 11
-0.0000
ARG 11
VAL 12
0.0004
VAL 12
HIS 13
-0.0076
HIS 13
ASP 14
-0.0000
ASP 14
ASN 15
0.0000
ASN 15
THR 16
0.0132
THR 16
ALA 17
-0.0000
ALA 17
LEU 18
0.0001
LEU 18
SER 19
0.0017
SER 19
ALA 20
-0.0005
ALA 20
ALA 21
-0.0000
ALA 21
ALA 22
-0.0093
ALA 22
VAL 23
-0.0000
VAL 23
ARG 24
-0.0000
ARG 24
GLY 25
-0.0036
GLY 25
PRO 26
-0.0002
PRO 26
CYS 27
0.0004
CYS 27
VAL 28
0.0008
VAL 28
ALA 29
0.0002
ALA 29
VAL 30
0.0001
VAL 30
TYR 31
0.0013
TYR 31
LEU 32
-0.0003
LEU 32
LEU 33
0.0000
LEU 33
SER 34
0.0047
SER 34
PRO 35
-0.0003
PRO 35
ALA 36
0.0000
ALA 36
GLN 37
0.0057
GLN 37
TRP 38
0.0002
TRP 38
LEU 39
-0.0006
LEU 39
ALA 40
0.0285
ALA 40
HIS 41
-0.0003
HIS 41
ASP 42
-0.0002
ASP 42
ASP 43
0.0136
ASP 43
ALA 44
0.0001
ALA 44
PRO 45
-0.0003
PRO 45
CYS 46
-0.0059
CYS 46
LYS 47
-0.0001
LYS 47
VAL 48
-0.0003
VAL 48
ASP 49
0.0010
ASP 49
PHE 50
-0.0000
PHE 50
TRP 51
0.0002
TRP 51
LEU 52
0.0031
LEU 52
ARG 53
0.0000
ARG 53
ASN 54
-0.0001
ASN 54
LEU 55
0.0044
LEU 55
ARG 56
-0.0002
ARG 56
ASP 57
-0.0003
ASP 57
LEU 58
0.0058
LEU 58
SER 59
-0.0002
SER 59
GLN 60
-0.0001
GLN 60
THR 61
-0.0076
THR 61
LEU 62
-0.0002
LEU 62
ALA 63
-0.0000
ALA 63
ARG 64
0.0001
ARG 64
LEU 65
0.0002
LEU 65
ASN 66
-0.0001
ASN 66
ILE 67
-0.0013
ILE 67
PRO 68
-0.0001
PRO 68
LEU 69
0.0001
LEU 69
LEU 70
0.0007
LEU 70
ILE 71
-0.0003
ILE 71
ARG 72
0.0001
ARG 72
GLU 73
0.0046
GLU 73
ALA 74
-0.0003
ALA 74
SER 75
-0.0001
SER 75
HIS 76
0.0089
HIS 76
TRP 77
-0.0002
TRP 77
ASP 78
-0.0002
ASP 78
ASP 79
0.0029
ASP 79
ALA 80
-0.0002
ALA 80
PRO 81
0.0002
PRO 81
ARG 82
0.0034
ARG 82
VAL 83
0.0002
VAL 83
LEU 84
0.0003
LEU 84
ALA 85
-0.0011
ALA 85
GLY 86
-0.0003
GLY 86
LEU 87
-0.0000
LEU 87
CYS 88
-0.0003
CYS 88
ASP 89
0.0003
ASP 89
GLU 90
-0.0000
GLU 90
LEU 91
-0.0005
LEU 91
GLY 92
0.0002
GLY 92
VAL 93
0.0001
VAL 93
GLU 94
-0.0004
GLU 94
ALA 95
0.0002
ALA 95
VAL 96
0.0000
VAL 96
HIS 97
0.0042
HIS 97
ALA 98
-0.0000
ALA 98
ASN 99
0.0002
ASN 99
ASP 100
-0.0248
ASP 100
GLU 101
0.0001
GLU 101
TYR 102
-0.0004
TYR 102
GLY 103
-0.0047
GLY 103
VAL 104
0.0001
VAL 104
HIS 105
-0.0001
HIS 105
GLU 106
-0.0066
GLU 106
THR 107
-0.0004
THR 107
ARG 108
-0.0003
ARG 108
ARG 109
0.0077
ARG 109
ASP 110
0.0001
ASP 110
ALA 111
0.0001
ALA 111
ALA 112
0.0045
ALA 112
VAL 113
-0.0002
VAL 113
ARG 114
0.0000
ARG 114
GLN 115
0.0054
GLN 115
ALA 116
0.0001
ALA 116
LEU 117
-0.0002
LEU 117
GLU 118
-0.0032
GLU 118
THR 119
-0.0002
THR 119
ALA 120
-0.0002
ALA 120
GLY 121
0.0037
GLY 121
ILE 122
0.0001
ILE 122
ALA 123
-0.0002
ALA 123
TRP 124
-0.0003
TRP 124
HIS 125
-0.0001
HIS 125
ASN 126
-0.0001
ASN 126
TYR 127
0.0271
TYR 127
LEU 128
0.0000
LEU 128
ASP 129
-0.0000
ASP 129
GLN 130
-0.0079
GLN 130
LEU 131
0.0001
LEU 131
LEU 132
0.0003
LEU 132
PHE 133
-0.0047
PHE 133
GLN 134
-0.0001
GLN 134
PRO 135
0.0000
PRO 135
GLY 136
-0.0012
GLY 136
SER 137
-0.0001
SER 137
VAL 138
0.0001
VAL 138
LEU 139
0.0080
LEU 139
THR 140
-0.0002
THR 140
ARG 141
0.0002
ARG 141
THR 142
0.0039
THR 142
GLY 143
-0.0002
GLY 143
THR 144
-0.0003
THR 144
TYR 145
0.0034
TYR 145
PHE 146
-0.0002
PHE 146
GLN 147
0.0003
GLN 147
VAL 148
-0.0267
VAL 148
PHE 149
-0.0004
PHE 149
SER 150
-0.0001
SER 150
GLN 151
0.0117
GLN 151
PHE 152
0.0002
PHE 152
ARG 153
0.0002
ARG 153
LYS 154
0.0065
LYS 154
VAL 155
0.0001
VAL 155
CYS 156
0.0003
CYS 156
TYR 157
-0.0066
TYR 157
SER 158
0.0001
SER 158
ARG 159
-0.0003
ARG 159
LEU 160
-0.0040
LEU 160
HIS 161
-0.0001
HIS 161
GLY 162
0.0001
GLY 162
SER 163
-0.0031
SER 163
LEU 164
0.0001
LEU 164
PRO 165
-0.0005
PRO 165
GLN 166
-0.0261
GLN 166
LEU 167
0.0001
LEU 167
VAL 168
0.0002
VAL 168
ALA 169
-0.0267
ALA 169
PRO 170
-0.0001
PRO 170
PRO 171
0.0001
PRO 171
LYS 172
-0.0138
LYS 172
THR 173
-0.0002
THR 173
GLN 174
0.0004
GLN 174
ALA 175
-0.0072
ALA 175
PRO 176
-0.0001
PRO 176
THR 177
-0.0001
THR 177
GLY 178
-0.0022
GLY 178
ILE 179
-0.0002
ILE 179
ASP 180
0.0004
ASP 180
SER 181
0.0015
SER 181
ASP 182
-0.0002
ASP 182
SER 183
0.0000
SER 183
ILE 184
0.0019
ILE 184
PRO 185
-0.0001
PRO 185
GLU 186
0.0003
GLU 186
GLN 187
0.0056
GLN 187
LEU 188
-0.0000
LEU 188
ASP 189
0.0000
ASP 189
ASP 190
0.0058
ASP 190
PHE 191
0.0002
PHE 191
PRO 192
-0.0002
PRO 192
THR 193
-0.0085
THR 193
PRO 194
0.0003
PRO 194
SER 195
0.0001
SER 195
ALA 196
-0.0033
ALA 196
HIS 197
-0.0001
HIS 197
LEU 198
0.0003
LEU 198
ARG 199
0.0075
ARG 199
ALA 200
0.0004
ALA 200
LEU 201
-0.0001
LEU 201
TRP 202
0.0099
TRP 202
PRO 203
0.0001
PRO 203
ALA 204
0.0004
ALA 204
GLY 205
0.0164
GLY 205
GLU 206
0.0001
GLU 206
ALA 207
-0.0001
ALA 207
GLU 208
0.0125
GLU 208
ALA 209
-0.0001
ALA 209
GLN 210
0.0001
GLN 210
ARG 211
0.0030
ARG 211
ARG 212
0.0002
ARG 212
LEU 213
0.0002
LEU 213
ASN 214
-0.0000
ASN 214
GLU 215
0.0002
GLU 215
PHE 216
0.0001
PHE 216
THR 217
0.0008
THR 217
ASP 218
0.0003
ASP 218
ALA 219
-0.0002
ALA 219
GLN 220
0.0019
GLN 220
ILE 221
0.0000
ILE 221
ASP 222
0.0000
ASP 222
TYR 223
0.0037
TYR 223
TYR 224
-0.0002
TYR 224
LYS 225
0.0001
LYS 225
ASP 226
0.0133
ASP 226
GLU 227
-0.0000
GLU 227
ARG 228
0.0001
ARG 228
ASP 229
0.0137
ASP 229
LEU 230
0.0002
LEU 230
PRO 231
0.0003
PRO 231
ALA 232
-0.0026
ALA 232
LYS 233
0.0003
LYS 233
PRO 234
-0.0005
PRO 234
GLY 235
0.0144
GLY 235
THR 236
0.0000
THR 236
SER 237
0.0000
SER 237
GLN 238
-0.0014
GLN 238
LEU 239
0.0001
LEU 239
SER 240
-0.0002
SER 240
THR 241
-0.0052
THR 241
TYR 242
0.0001
TYR 242
LEU 243
0.0002
LEU 243
ALA 244
0.0018
ALA 244
ALA 245
-0.0000
ALA 245
GLY 246
0.0000
GLY 246
ILE 247
0.0006
ILE 247
LEU 248
0.0001
LEU 248
SER 249
-0.0001
SER 249
PRO 250
-0.0053
PRO 250
ARG 251
-0.0002
ARG 251
GLN 252
0.0004
GLN 252
CYS 253
0.0153
CYS 253
LEU 254
-0.0002
LEU 254
HIS 255
-0.0001
HIS 255
ALA 256
0.0056
ALA 256
ALA 257
0.0001
ALA 257
LEU 258
-0.0000
LEU 258
GLN 259
-0.0088
GLN 259
SER 260
0.0000
SER 260
ASN 261
0.0002
ASN 261
GLN 262
0.0007
GLN 262
GLY 263
-0.0001
GLY 263
GLU 264
-0.0003
GLU 264
PHE 265
-0.0079
PHE 265
GLU 266
-0.0002
GLU 266
SER 267
0.0000
SER 267
GLY 268
-0.0078
GLY 268
SER 269
0.0004
SER 269
VAL 270
-0.0001
VAL 270
GLY 271
-0.0038
GLY 271
VAL 272
0.0004
VAL 272
VAL 273
-0.0001
VAL 273
THR 274
0.0010
THR 274
TRP 275
-0.0001
TRP 275
ILE 276
-0.0001
ILE 276
ASN 277
-0.0221
ASN 277
GLU 278
-0.0002
GLU 278
LEU 279
-0.0001
LEU 279
LEU 280
-0.0109
LEU 280
TRP 281
0.0001
TRP 281
ARG 282
-0.0000
ARG 282
GLU 283
0.0104
GLU 283
PHE 284
-0.0001
PHE 284
TYR 285
-0.0002
TYR 285
LYS 286
0.0021
LYS 286
HIS 287
0.0002
HIS 287
ILE 288
0.0000
ILE 288
LEU 289
0.0049
LEU 289
VAL 290
-0.0003
VAL 290
GLY 291
-0.0001
GLY 291
TYR 292
-0.0226
TYR 292
PRO 293
0.0000
PRO 293
ARG 294
0.0000
ARG 294
VAL 295
0.0081
VAL 295
SER 296
-0.0003
SER 296
ARG 297
-0.0002
ARG 297
HIS 298
-0.0152
HIS 298
ARG 299
-0.0003
ARG 299
ALA 300
0.0002
ALA 300
PHE 301
0.0032
PHE 301
ARG 302
-0.0000
ARG 302
PRO 303
-0.0002
PRO 303
GLU 304
-0.1475
GLU 304
THR 305
0.0003
THR 305
GLU 306
0.0002
GLU 306
ALA 307
0.0422
ALA 307
LEU 308
0.0002
LEU 308
ALA 309
-0.0002
ALA 309
TRP 310
0.1146
TRP 310
ARG 311
0.0001
ARG 311
HIS 312
0.0001
HIS 312
ALA 313
0.0394
ALA 313
PRO 314
0.0000
PRO 314
GLU 315
-0.0001
GLU 315
ASP 316
-0.0009
ASP 316
LEU 317
0.0002
LEU 317
ALA 318
-0.0001
ALA 318
ALA 319
-0.0068
ALA 319
TRP 320
-0.0000
TRP 320
LYS 321
0.0003
LYS 321
GLU 322
-0.0210
GLU 322
ALA 323
-0.0003
ALA 323
ARG 324
0.0004
ARG 324
THR 325
0.0053
THR 325
GLY 326
-0.0002
GLY 326
LEU 327
0.0001
LEU 327
PRO 328
0.0171
PRO 328
ILE 329
0.0002
ILE 329
ILE 330
0.0002
ILE 330
ASP 331
-0.0038
ASP 331
ALA 332
0.0000
ALA 332
ALA 333
0.0001
ALA 333
MET 334
-0.0011
MET 334
ARG 335
-0.0000
ARG 335
GLN 336
-0.0001
GLN 336
LEU 337
-0.0208
LEU 337
LEU 338
0.0001
LEU 338
GLU 339
0.0004
GLU 339
THR 340
0.0113
THR 340
GLY 341
0.0001
GLY 341
TRP 342
-0.0003
TRP 342
MET 343
-0.0045
MET 343
HIS 344
-0.0002
HIS 344
ASN 345
-0.0001
ASN 345
ARG 346
0.0088
ARG 346
LEU 347
0.0000
LEU 347
ARG 348
-0.0000
ARG 348
MET 349
-0.0147
MET 349
VAL 350
0.0000
VAL 350
VAL 351
-0.0000
VAL 351
ALA 352
-0.0020
ALA 352
MET 353
0.0003
MET 353
PHE 354
-0.0002
PHE 354
LEU 355
-0.0044
LEU 355
THR 356
0.0003
THR 356
LYS 357
-0.0000
LYS 357
ASN 358
-0.0108
ASN 358
LEU 359
0.0000
LEU 359
LEU 360
0.0002
LEU 360
ILE 361
-0.0038
ILE 361
ASP 362
0.0004
ASP 362
TRP 363
-0.0001
TRP 363
ARG 364
-0.0136
ARG 364
GLU 365
-0.0002
GLU 365
GLY 366
-0.0001
GLY 366
GLU 367
-0.0086
GLU 367
ARG 368
-0.0000
ARG 368
PHE 369
-0.0000
PHE 369
PHE 370
0.0101
PHE 370
MET 371
0.0004
MET 371
ARG 372
0.0002
ARG 372
HIS 373
-0.0096
HIS 373
LEU 374
0.0003
LEU 374
ILE 375
0.0002
ILE 375
ASP 376
-0.0060
ASP 376
GLY 377
0.0003
GLY 377
ASP 378
0.0001
ASP 378
LEU 379
-0.0106
LEU 379
ALA 380
0.0001
ALA 380
ALA 381
-0.0001
ALA 381
ASN 382
0.0257
ASN 382
ASN 383
-0.0002
ASN 383
GLY 384
-0.0000
GLY 384
GLY 385
0.0253
GLY 385
TRP 386
0.0002
TRP 386
GLN 387
-0.0001
GLN 387
TRP 388
0.0175
TRP 388
SER 389
0.0002
SER 389
SER 390
0.0000
SER 390
SER 391
-0.0334
SER 391
THR 392
-0.0001
THR 392
GLY 393
0.0003
GLY 393
THR 394
-0.0207
THR 394
ASP 395
-0.0002
ASP 395
SER 396
-0.0001
SER 396
ALA 397
0.0147
ALA 397
PRO 398
0.0000
PRO 398
TYR 399
-0.0000
TYR 399
PHE 400
-0.0046
PHE 400
ARG 401
0.0002
ARG 401
ILE 402
0.0001
ILE 402
PHE 403
-0.0100
PHE 403
ASN 404
-0.0001
ASN 404
PRO 405
0.0000
PRO 405
LEU 406
0.0021
LEU 406
SER 407
0.0004
SER 407
GLN 408
-0.0002
GLN 408
SER 409
-0.0073
SER 409
GLU 410
0.0000
GLU 410
LYS 411
-0.0003
LYS 411
PHE 412
-0.0013
PHE 412
ASP 413
0.0003
ASP 413
SER 414
-0.0004
SER 414
GLU 415
0.0034
GLU 415
GLY 416
-0.0001
GLY 416
LEU 417
0.0002
LEU 417
PHE 418
-0.0126
PHE 418
ILE 419
-0.0002
ILE 419
LYS 420
0.0000
LYS 420
HIS 421
-0.0209
HIS 421
TRP 422
-0.0003
TRP 422
LEU 423
-0.0004
LEU 423
PRO 424
-0.0046
PRO 424
GLU 425
-0.0002
GLU 425
LEU 426
0.0005
LEU 426
ALA 427
0.0073
ALA 427
GLY 428
-0.0002
GLY 428
LEU 429
0.0001
LEU 429
ASN 430
0.0014
ASN 430
LYS 431
0.0001
LYS 431
LYS 432
0.0001
LYS 432
ASP 433
-0.0018
ASP 433
ILE 434
0.0005
ILE 434
HIS 435
0.0002
HIS 435
ASN 436
0.0070
ASN 436
PRO 437
0.0005
PRO 437
ALA 438
-0.0001
ALA 438
ASN 439
-0.0115
ASN 439
MET 440
-0.0003
MET 440
GLY 441
-0.0001
GLY 441
GLY 442
0.0098
GLY 442
LEU 443
0.0002
LEU 443
PHE 444
0.0002
PHE 444
GLY 445
-0.0079
GLY 445
VAL 446
0.0000
VAL 446
ALA 447
-0.0001
ALA 447
ASP 448
-0.0145
ASP 448
TYR 449
-0.0002
TYR 449
PRO 450
-0.0004
PRO 450
LEU 451
0.0203
LEU 451
PRO 452
0.0003
PRO 452
ILE 453
-0.0002
ILE 453
VAL 454
0.0407
VAL 454
ASN 455
0.0003
ASN 455
LEU 456
0.0003
LEU 456
GLY 457
0.0174
GLY 457
GLN 458
-0.0002
GLN 458
SER 459
-0.0002
SER 459
ARG 460
0.0011
ARG 460
GLU 461
-0.0001
GLU 461
ARG 462
0.0001
ARG 462
ALA 463
-0.0255
ALA 463
LEU 464
-0.0004
LEU 464
ALA 465
-0.0001
ALA 465
ALA 466
-0.0526
ALA 466
PHE 467
-0.0004
PHE 467
LYS 468
0.0001
LYS 468
ASN 469
-0.1124
ASN 469
LEU 470
-0.0003
LEU 470
PRO 471
0.0002
PRO 471
THR 472
0.0919
THR 472
ARG 473
-0.0000
ARG 473
MET 474
-0.0001
MET 474
ASP 475
0.0541
ASP 475
ALA 476
0.0006
ALA 476
ALA 477
0.0008
ALA 477
GLY 478
0.1409
GLY 478
VAL 479
0.0002
VAL 479
TYR 480
-0.0001
TYR 480
ASP 481
0.0243
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: October 18th, 2018.