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
PRO 1
ILE 2
0.0002
ILE 2
THR 3
-0.0001
THR 3
ILE 4
-0.0042
ILE 4
ASN 5
0.0001
ASN 5
ASN 6
-0.0004
ASN 6
PHE 7
-0.0816
PHE 7
ARG 8
-0.0002
ARG 8
TYR 9
-0.0004
TYR 9
SER 10
-0.0024
SER 10
ASP 11
0.0001
ASP 11
PRO 12
0.0004
PRO 12
VAL 13
0.0473
VAL 13
ASN 14
-0.0001
ASN 14
ASN 15
-0.0000
ASN 15
ASP 16
-0.0550
ASP 16
THR 17
0.0004
THR 17
ILE 18
-0.0001
ILE 18
ILE 19
-0.0171
ILE 19
MET 20
0.0000
MET 20
MET 21
-0.0002
MET 21
GLU 22
-0.0565
GLU 22
PRO 23
-0.0003
PRO 23
PRO 24
0.0000
PRO 24
TYR 25
0.0045
TYR 25
CYS 26
0.0000
CYS 26
LYS 27
0.0006
LYS 27
GLY 28
0.0293
GLY 28
LEU 29
0.0002
LEU 29
ASP 30
0.0001
ASP 30
ILE 31
0.0284
ILE 31
TYR 32
-0.0000
TYR 32
TYR 33
-0.0004
TYR 33
LYS 34
-0.0751
LYS 34
ALA 35
-0.0001
ALA 35
PHE 36
0.0005
PHE 36
LYS 37
-0.0237
LYS 37
ILE 38
-0.0000
ILE 38
THR 39
-0.0004
THR 39
ASP 40
0.0497
ASP 40
ARG 41
-0.0004
ARG 41
ILE 42
0.0000
ILE 42
TRP 43
-0.0272
TRP 43
ILE 44
0.0003
ILE 44
VAL 45
0.0000
VAL 45
PRO 46
0.0381
PRO 46
GLU 47
-0.0002
GLU 47
ARG 48
0.0000
ARG 48
TYR 49
0.0057
TYR 49
GLU 50
0.0004
GLU 50
PHE 51
0.0002
PHE 51
GLY 52
0.0768
GLY 52
THR 53
-0.0001
THR 53
LYS 54
-0.0001
LYS 54
PRO 55
0.0074
PRO 55
GLU 56
-0.0001
GLU 56
ASP 57
-0.0001
ASP 57
PHE 58
0.0073
PHE 58
ASN 59
-0.0001
ASN 59
PRO 60
-0.0002
PRO 60
PRO 61
-0.0340
PRO 61
SER 62
-0.0003
SER 62
SER 63
0.0000
SER 63
LEU 64
-0.0267
LEU 64
ILE 65
-0.0000
ILE 65
GLU 66
0.0001
GLU 66
GLY 67
-0.0253
GLY 67
ALA 68
-0.0000
ALA 68
SER 69
0.0003
SER 69
GLU 70
0.2162
GLU 70
TYR 71
-0.0002
TYR 71
TYR 72
0.0001
TYR 72
ASP 73
0.0487
ASP 73
PRO 74
0.0003
PRO 74
ASN 75
-0.0001
ASN 75
TYR 76
-0.0412
TYR 76
LEU 77
0.0001
LEU 77
ARG 78
0.0000
ARG 78
THR 79
-0.0341
THR 79
ASP 80
-0.0002
ASP 80
SER 81
0.0000
SER 81
ASP 82
0.0310
ASP 82
LYS 83
-0.0001
LYS 83
ASP 84
-0.0000
ASP 84
ARG 85
0.0839
ARG 85
PHE 86
-0.0001
PHE 86
LEU 87
-0.0001
LEU 87
GLN 88
-0.0042
GLN 88
THR 89
-0.0004
THR 89
MET 90
-0.0001
MET 90
VAL 91
-0.0067
VAL 91
LYS 92
0.0003
LYS 92
LEU 93
-0.0001
LEU 93
PHE 94
-0.0106
PHE 94
ASN 95
-0.0000
ASN 95
ARG 96
0.0002
ARG 96
ILE 97
-0.0646
ILE 97
LYS 98
0.0000
LYS 98
ASN 99
-0.0003
ASN 99
ASN 100
-0.0331
ASN 100
VAL 101
-0.0000
VAL 101
ALA 102
0.0000
ALA 102
GLY 103
0.0316
GLY 103
GLU 104
-0.0000
GLU 104
ALA 105
-0.0002
ALA 105
LEU 106
0.0543
LEU 106
LEU 107
0.0001
LEU 107
ASP 108
0.0003
ASP 108
LYS 109
-0.0361
LYS 109
ILE 110
0.0000
ILE 110
ILE 111
-0.0002
ILE 111
ASN 112
-0.0283
ASN 112
ALA 113
0.0000
ALA 113
ILE 114
-0.0005
ILE 114
PRO 115
-0.0730
PRO 115
TYR 116
0.0000
TYR 116
LEU 117
0.0001
LEU 117
GLY 118
-0.0952
GLY 118
ASN 119
-0.0001
ASN 119
SER 120
-0.0000
SER 120
TYR 121
0.1584
TYR 121
SER 122
0.0001
SER 122
LEU 123
0.0000
LEU 123
LEU 124
0.0463
LEU 124
ASP 125
-0.0001
ASP 125
LYS 126
0.0000
LYS 126
PHE 127
0.1017
PHE 127
ASP 128
-0.0000
ASP 128
THR 129
-0.0002
THR 129
ASN 130
0.0436
ASN 130
SER 131
-0.0000
SER 131
ASN 132
-0.0001
ASN 132
SER 133
0.0893
SER 133
VAL 134
-0.0002
VAL 134
SER 135
0.0004
SER 135
PHE 136
0.2176
PHE 136
ASN 137
0.0004
ASN 137
LEU 138
-0.0003
LEU 138
LEU 139
0.0899
LEU 139
GLU 140
-0.0002
GLU 140
GLN 141
0.0003
GLN 141
ASP 142
0.0238
ASP 142
PRO 143
-0.0002
PRO 143
SER 144
-0.0002
SER 144
GLY 145
-0.0020
GLY 145
ALA 146
-0.0002
ALA 146
THR 147
0.0004
THR 147
THR 148
0.0108
THR 148
LYS 149
-0.0004
LYS 149
SER 150
0.0001
SER 150
ALA 151
0.1492
ALA 151
MET 152
0.0001
MET 152
LEU 153
-0.0002
LEU 153
THR 154
0.1338
THR 154
ASN 155
-0.0000
ASN 155
LEU 156
-0.0002
LEU 156
ILE 157
0.0084
ILE 157
ILE 158
0.0001
ILE 158
PHE 159
0.0000
PHE 159
GLY 160
0.0374
GLY 160
PRO 161
0.0003
PRO 161
GLY 162
0.0001
GLY 162
PRO 163
-0.0050
PRO 163
VAL 164
0.0000
VAL 164
LEU 165
0.0001
LEU 165
ASN 166
0.0685
ASN 166
LYS 167
0.0004
LYS 167
ASN 168
-0.0002
ASN 168
GLU 169
-0.0974
GLU 169
VAL 170
0.0000
VAL 170
ARG 171
0.0005
ARG 171
GLY 172
-0.0565
GLY 172
ILE 173
-0.0003
ILE 173
VAL 174
-0.0000
VAL 174
LEU 175
-0.1954
LEU 175
ARG 176
0.0001
ARG 176
VAL 177
0.0003
VAL 177
ASP 178
-0.1992
ASP 178
ASN 179
0.0001
ASN 179
LYS 180
0.0001
LYS 180
ASN 181
0.2286
ASN 181
TYR 182
-0.0002
TYR 182
PHE 183
0.0000
PHE 183
PRO 184
0.1365
PRO 184
CYS 185
-0.0002
CYS 185
ARG 186
0.0003
ARG 186
ASP 187
-0.0847
ASP 187
GLY 188
0.0002
GLY 188
PHE 189
0.0001
PHE 189
GLY 190
0.0809
GLY 190
SER 191
-0.0004
SER 191
ILE 192
0.0004
ILE 192
MET 193
0.0573
MET 193
GLN 194
-0.0000
GLN 194
MET 195
0.0001
MET 195
ALA 196
-0.0315
ALA 196
PHE 197
0.0002
PHE 197
CYS 198
-0.0003
CYS 198
PRO 199
-0.0056
PRO 199
GLU 200
-0.0002
GLU 200
TYR 201
-0.0001
TYR 201
VAL 202
0.1283
VAL 202
PRO 203
-0.0001
PRO 203
THR 204
-0.0003
THR 204
PHE 205
0.0496
PHE 205
ASP 206
0.0001
ASP 206
ASN 207
0.0002
ASN 207
VAL 208
0.0167
VAL 208
ILE 209
-0.0002
ILE 209
GLU 210
-0.0002
GLU 210
ASN 211
-0.1223
ASN 211
ILE 212
-0.0000
ILE 212
THR 213
-0.0001
THR 213
SER 214
0.0080
SER 214
LEU 215
-0.0002
LEU 215
THR 216
0.0002
THR 216
ILE 217
0.0387
ILE 217
GLY 218
-0.0001
GLY 218
LYS 219
0.0001
LYS 219
SER 220
-0.0369
SER 220
LYS 221
-0.0002
LYS 221
TYR 222
0.0001
TYR 222
PHE 223
-0.0160
PHE 223
GLN 224
0.0001
GLN 224
ASP 225
-0.0000
ASP 225
PRO 226
0.0324
PRO 226
ALA 227
-0.0003
ALA 227
LEU 228
0.0000
LEU 228
LEU 229
0.0482
LEU 229
LEU 230
0.0001
LEU 230
MET 231
0.0003
MET 231
HIS 232
0.0882
HIS 232
GLU 233
0.0001
GLU 233
LEU 234
-0.0002
LEU 234
ILE 235
-0.0188
ILE 235
HIS 236
-0.0000
HIS 236
VAL 237
0.0003
VAL 237
LEU 238
-0.0216
LEU 238
HIS 239
-0.0000
HIS 239
GLY 240
0.0002
GLY 240
LEU 241
0.0641
LEU 241
TYR 242
-0.0003
TYR 242
GLY 243
0.0001
GLY 243
MET 244
0.0341
MET 244
GLN 245
0.0000
GLN 245
VAL 246
-0.0002
VAL 246
SER 247
-0.1282
SER 247
SER 248
0.0001
SER 248
HIS 249
0.0005
HIS 249
GLU 250
-0.0921
GLU 250
ILE 251
0.0000
ILE 251
ILE 252
0.0001
ILE 252
PRO 253
0.0054
PRO 253
SER 254
0.0002
SER 254
LYS 255
0.0001
LYS 255
GLN 256
0.0933
GLN 256
GLU 257
-0.0003
GLU 257
ILE 258
0.0001
ILE 258
TYR 259
0.0837
TYR 259
MET 260
0.0001
MET 260
GLN 261
-0.0000
GLN 261
HIS 262
-0.0544
HIS 262
THR 263
0.0000
THR 263
TYR 264
0.0000
TYR 264
PRO 265
-0.0958
PRO 265
ILE 266
-0.0001
ILE 266
SER 267
-0.0001
SER 267
ALA 268
-0.1228
ALA 268
GLU 269
-0.0003
GLU 269
GLU 270
-0.0002
GLU 270
LEU 271
0.0937
LEU 271
PHE 272
-0.0000
PHE 272
THR 273
-0.0001
THR 273
PHE 274
-0.0462
PHE 274
GLY 275
0.0001
GLY 275
GLY 276
0.0003
GLY 276
GLN 277
-0.0661
GLN 277
ASP 278
0.0001
ASP 278
ALA 279
-0.0003
ALA 279
ASN 280
-0.0610
ASN 280
LEU 281
-0.0002
LEU 281
ILE 282
0.0002
ILE 282
SER 283
0.0013
SER 283
ILE 284
-0.0002
ILE 284
ASP 285
-0.0001
ASP 285
ILE 286
0.0528
ILE 286
LYS 287
-0.0002
LYS 287
ASN 288
-0.0002
ASN 288
ASP 289
0.0145
ASP 289
LEU 290
0.0000
LEU 290
TYR 291
0.0000
TYR 291
GLU 292
-0.0229
GLU 292
LYS 293
-0.0003
LYS 293
THR 294
0.0000
THR 294
LEU 295
-0.0249
LEU 295
ASN 296
-0.0002
ASN 296
ASP 297
0.0000
ASP 297
TYR 298
-0.0113
TYR 298
LYS 299
0.0002
LYS 299
ALA 300
0.0001
ALA 300
ILE 301
0.0169
ILE 301
ALA 302
-0.0000
ALA 302
ASN 303
-0.0001
ASN 303
LYS 304
0.0541
LYS 304
LEU 305
0.0004
LEU 305
SER 306
0.0003
SER 306
GLN 307
-0.0246
GLN 307
VAL 308
-0.0000
VAL 308
THR 309
0.0000
THR 309
SER 310
0.0118
SER 310
CYS 311
0.0000
CYS 311
ASN 312
-0.0001
ASN 312
ASP 313
-0.0093
ASP 313
PRO 314
0.0002
PRO 314
ASN 315
0.0001
ASN 315
ILE 316
0.0071
ILE 316
ASP 317
-0.0001
ASP 317
ILE 318
0.0003
ILE 318
ASP 319
-0.0340
ASP 319
SER 320
-0.0000
SER 320
TYR 321
-0.0004
TYR 321
LYS 322
0.0193
LYS 322
GLN 323
0.0002
GLN 323
ILE 324
-0.0002
ILE 324
TYR 325
-0.0143
TYR 325
GLN 326
0.0001
GLN 326
GLN 327
0.0001
GLN 327
LYS 328
-0.0019
LYS 328
TYR 329
0.0001
TYR 329
GLN 330
0.0001
GLN 330
PHE 331
-0.1117
PHE 331
ASP 332
-0.0001
ASP 332
LYS 333
0.0001
LYS 333
ASP 334
-0.0948
ASP 334
SER 335
-0.0002
SER 335
ASN 336
0.0003
ASN 336
GLY 337
0.1074
GLY 337
GLN 338
-0.0002
GLN 338
TYR 339
-0.0002
TYR 339
ILE 340
-0.1244
ILE 340
VAL 341
0.0000
VAL 341
ASN 342
-0.0002
ASN 342
GLU 343
-0.1593
GLU 343
ASP 344
0.0003
ASP 344
LYS 345
0.0004
LYS 345
PHE 346
0.0056
PHE 346
GLN 347
0.0000
GLN 347
ILE 348
-0.0005
ILE 348
LEU 349
0.0784
LEU 349
TYR 350
-0.0002
TYR 350
ASN 351
-0.0003
ASN 351
SER 352
0.0268
SER 352
ILE 353
-0.0001
ILE 353
MET 354
-0.0004
MET 354
TYR 355
0.0554
TYR 355
GLY 356
-0.0001
GLY 356
PHE 357
-0.0003
PHE 357
THR 358
-0.1551
THR 358
GLU 359
-0.0001
GLU 359
VAL 360
-0.0002
VAL 360
GLU 361
0.0531
GLU 361
LEU 362
0.0005
LEU 362
GLY 363
-0.0000
GLY 363
LYS 364
0.0429
LYS 364
LYS 365
-0.0001
LYS 365
PHE 366
0.0002
PHE 366
ASN 367
0.0263
ASN 367
ILE 368
-0.0002
ILE 368
LYS 369
0.0003
LYS 369
THR 370
-0.1079
THR 370
ARG 371
0.0002
ARG 371
LEU 372
-0.0002
LEU 372
SER 373
-0.0625
SER 373
TYR 374
-0.0005
TYR 374
PHE 375
-0.0002
PHE 375
SER 376
-0.0902
SER 376
MET 377
-0.0000
MET 377
ASN 378
0.0001
ASN 378
HIS 379
0.0004
HIS 379
ASP 380
0.0002
ASP 380
PRO 381
-0.0000
PRO 381
VAL 382
0.1147
VAL 382
LYS 383
-0.0002
LYS 383
ILE 384
0.0000
ILE 384
PRO 385
0.0329
PRO 385
ASN 386
0.0004
ASN 386
LEU 387
-0.0002
LEU 387
LEU 388
0.0342
LEU 388
ASP 389
0.0001
ASP 389
ASP 390
0.0004
ASP 390
THR 391
-0.0140
THR 391
ILE 392
-0.0001
ILE 392
TYR 393
0.0003
TYR 393
ASN 394
-0.0044
ASN 394
ASP 395
0.0001
ASP 395
THR 396
-0.0003
THR 396
GLU 397
-0.0014
GLU 397
GLY 398
0.0004
GLY 398
PHE 399
0.0000
PHE 399
ASN 400
0.0045
ASN 400
ILE 401
0.0005
ILE 401
GLU 402
0.0001
GLU 402
SER 403
-0.0084
SER 403
LYS 404
-0.0001
LYS 404
ASP 405
0.0002
ASP 405
LEU 406
0.0080
LEU 406
LYS 407
0.0003
LYS 407
SER 408
0.0000
SER 408
GLU 409
-0.0235
GLU 409
TYR 410
0.0003
TYR 410
LYS 411
0.0002
LYS 411
GLY 412
0.0076
GLY 412
GLN 413
-0.0002
GLN 413
ASN 414
-0.0000
ASN 414
MET 415
-0.0154
MET 415
ARG 416
-0.0001
ARG 416
VAL 417
0.0001
VAL 417
ASN 418
-0.0157
ASN 418
THR 419
-0.0001
THR 419
ASN 420
-0.0002
ASN 420
ALA 421
-0.0164
ALA 421
PHE 422
-0.0003
PHE 422
ARG 423
-0.0003
ARG 423
ASN 424
0.0453
ASN 424
VAL 425
0.0000
VAL 425
ASP 426
-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.