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
ARG 50
ARG 51
-0.0000
ARG 51
ALA 52
0.0029
ALA 52
VAL 53
-0.0000
VAL 53
TYR 54
0.0030
TYR 54
ILE 55
-0.0001
ILE 55
GLY 56
0.0021
GLY 56
ALA 57
-0.0002
ALA 57
LEU 58
0.0104
LEU 58
PHE 59
0.0003
PHE 59
PRO 60
0.0220
PRO 60
MET 61
0.0000
MET 61
SER 62
-0.0459
SER 62
GLY 63
0.0007
GLY 63
GLY 64
-0.0432
GLY 64
TRP 65
0.0001
TRP 65
PRO 66
-0.0818
PRO 66
GLY 67
-0.0003
GLY 67
GLY 68
-0.0151
GLY 68
GLN 69
-0.0003
GLN 69
ALA 70
-0.0088
ALA 70
CYS 71
0.0003
CYS 71
GLN 72
0.0187
GLN 72
PRO 73
0.0001
PRO 73
ALA 74
0.0034
ALA 74
VAL 75
0.0001
VAL 75
GLU 76
0.0021
GLU 76
MET 77
-0.0002
MET 77
ALA 78
-0.0014
ALA 78
LEU 79
0.0001
LEU 79
GLU 80
0.0017
GLU 80
ASP 81
0.0003
ASP 81
VAL 82
-0.0000
VAL 82
ASN 83
-0.0002
ASN 83
SER 84
0.0069
SER 84
TYR 92
-0.0004
TYR 92
GLU 93
-0.0004
GLU 93
LEU 94
-0.0033
LEU 94
LYS 95
0.0001
LYS 95
LEU 96
-0.0088
LEU 96
ILE 97
0.0000
ILE 97
HIS 98
0.0056
HIS 98
HIS 99
0.0002
HIS 99
ASP 100
0.0179
ASP 100
SER 101
-0.0001
SER 101
LYS 102
0.0240
LYS 102
CYS 103
-0.0002
CYS 103
ASP 104
0.0495
ASP 104
PRO 105
0.0001
PRO 105
GLY 106
-0.0068
GLY 106
GLN 107
0.0006
GLN 107
ALA 108
-0.0092
ALA 108
THR 109
0.0001
THR 109
LYS 110
-0.0244
LYS 110
TYR 111
0.0005
TYR 111
LEU 112
0.0017
LEU 112
TYR 113
0.0003
TYR 113
GLU 114
-0.0064
GLU 114
LEU 115
0.0001
LEU 115
LEU 116
0.0084
LEU 116
TYR 117
0.0002
TYR 117
ASN 118
-0.0117
ASN 118
ASP 119
-0.0003
ASP 119
PRO 120
-0.0008
PRO 120
ILE 121
0.0003
ILE 121
LYS 122
-0.0032
LYS 122
ILE 123
-0.0000
ILE 123
ILE 124
0.0023
ILE 124
LEU 125
-0.0002
LEU 125
MET 126
0.0106
MET 126
PRO 127
-0.0004
PRO 127
GLY 128
0.0229
GLY 128
CYS 129
0.0000
CYS 129
SER 130
-0.0575
SER 130
SER 131
-0.0001
SER 131
VAL 132
-0.0011
VAL 132
SER 133
-0.0002
SER 133
THR 134
-0.0169
THR 134
LEU 135
0.0001
LEU 135
VAL 136
0.0142
VAL 136
ALA 137
0.0003
ALA 137
GLU 138
-0.0018
GLU 138
ALA 139
-0.0003
ALA 139
ALA 140
0.0107
ALA 140
ARG 141
-0.0000
ARG 141
MET 142
-0.0151
MET 142
TRP 143
-0.0001
TRP 143
ASN 144
0.0026
ASN 144
LEU 145
-0.0002
LEU 145
ILE 146
-0.0211
ILE 146
VAL 147
-0.0001
VAL 147
LEU 148
-0.0068
LEU 148
SER 149
-0.0001
SER 149
TYR 150
-0.0002
TYR 150
GLY 151
0.0001
GLY 151
SER 152
-0.0223
SER 152
SER 153
-0.0000
SER 153
SER 154
0.0045
SER 154
PRO 155
0.0005
PRO 155
ALA 156
-0.0820
ALA 156
LEU 157
0.0001
LEU 157
SER 158
0.0172
SER 158
ASN 159
-0.0002
ASN 159
ARG 160
0.0371
ARG 160
GLN 161
-0.0003
GLN 161
ARG 162
0.0143
ARG 162
PHE 163
-0.0003
PHE 163
PRO 164
0.0555
PRO 164
THR 165
0.0003
THR 165
PHE 166
-0.0157
PHE 166
PHE 167
-0.0001
PHE 167
ARG 168
-0.0338
ARG 168
THR 169
-0.0002
THR 169
HIS 170
-0.0404
HIS 170
PRO 171
0.0004
PRO 171
SER 172
0.0476
SER 172
ALA 173
0.0002
ALA 173
THR 174
0.0159
THR 174
LEU 175
0.0003
LEU 175
HIS 176
-0.0289
HIS 176
ASN 177
0.0002
ASN 177
PRO 178
-0.0017
PRO 178
THR 179
-0.0003
THR 179
ARG 180
0.0188
ARG 180
VAL 181
-0.0002
VAL 181
LYS 182
-0.0020
LYS 182
LEU 183
0.0002
LEU 183
PHE 184
0.0192
PHE 184
GLU 185
-0.0002
GLU 185
LYS 186
-0.0094
LYS 186
TRP 187
-0.0002
TRP 187
GLY 188
0.0016
GLY 188
TRP 189
0.0001
TRP 189
LYS 190
-0.0059
LYS 190
LYS 191
-0.0002
LYS 191
ILE 192
-0.0052
ILE 192
ALA 193
0.0001
ALA 193
THR 194
-0.0035
THR 194
ILE 195
-0.0002
ILE 195
GLN 196
0.0182
GLN 196
GLN 197
0.0001
GLN 197
THR 198
0.0205
THR 198
THR 199
0.0002
THR 199
GLU 200
0.1877
GLU 200
VAL 201
0.0001
VAL 201
PHE 202
0.0351
PHE 202
THR 203
-0.0004
THR 203
SER 204
0.0778
SER 204
THR 205
-0.0002
THR 205
LEU 206
0.0189
LEU 206
ASP 207
-0.0002
ASP 207
ASP 208
0.0289
ASP 208
LEU 209
-0.0001
LEU 209
GLU 210
0.0176
GLU 210
GLU 211
-0.0002
GLU 211
ARG 212
0.0227
ARG 212
VAL 213
0.0001
VAL 213
LYS 214
0.0110
LYS 214
GLU 215
-0.0000
GLU 215
ALA 216
0.0013
ALA 216
GLY 217
-0.0002
GLY 217
ILE 218
-0.0014
ILE 218
GLU 219
-0.0000
GLU 219
ILE 220
-0.0065
ILE 220
THR 221
-0.0002
THR 221
PHE 222
-0.0049
PHE 222
ARG 223
-0.0000
ARG 223
GLN 224
-0.0129
GLN 224
SER 225
-0.0002
SER 225
PHE 226
-0.0197
PHE 226
PHE 227
-0.0000
PHE 227
SER 228
0.0195
SER 228
ASP 229
0.0001
ASP 229
PRO 230
-0.0023
PRO 230
ALA 231
-0.0000
ALA 231
VAL 232
-0.0099
VAL 232
PRO 233
-0.0002
PRO 233
VAL 234
0.0099
VAL 234
LYS 235
-0.0002
LYS 235
ASN 236
0.0080
ASN 236
LEU 237
-0.0001
LEU 237
LYS 238
0.0094
LYS 238
ARG 239
-0.0002
ARG 239
GLN 240
0.0085
GLN 240
ASP 241
0.0002
ASP 241
ALA 242
0.0023
ALA 242
ARG 243
-0.0001
ARG 243
ILE 244
-0.0011
ILE 244
ILE 245
0.0000
ILE 245
VAL 246
0.0053
VAL 246
GLY 247
0.0003
GLY 247
LEU 248
0.0139
LEU 248
PHE 249
-0.0001
PHE 249
TYR 250
-0.0559
TYR 250
GLU 251
-0.0002
GLU 251
THR 252
-0.0160
THR 252
GLU 253
0.0001
GLU 253
ALA 254
0.0031
ALA 254
ARG 255
-0.0001
ARG 255
LYS 256
-0.0147
LYS 256
VAL 257
-0.0001
VAL 257
PHE 258
0.0182
PHE 258
CYS 259
0.0002
CYS 259
GLU 260
-0.0017
GLU 260
VAL 261
-0.0003
VAL 261
TYR 262
0.0103
TYR 262
LYS 263
0.0000
LYS 263
GLU 264
0.0021
GLU 264
ARG 265
-0.0001
ARG 265
LEU 266
0.0006
LEU 266
PHE 267
-0.0004
PHE 267
GLY 268
0.0173
GLY 268
LYS 269
0.0003
LYS 269
LYS 270
-0.0077
LYS 270
TYR 271
0.0003
TYR 271
VAL 272
-0.0159
VAL 272
TRP 273
0.0000
TRP 273
PHE 274
-0.0118
PHE 274
LEU 275
0.0001
LEU 275
ILE 276
-0.0146
ILE 276
GLY 277
0.0000
GLY 277
TRP 278
0.0615
TRP 278
TYR 279
-0.0001
TYR 279
ALA 280
-0.0399
ALA 280
ASP 281
-0.0001
ASP 281
ASN 282
-0.0402
ASN 282
TRP 283
0.0001
TRP 283
PHE 284
-0.0040
PHE 284
LYS 285
-0.0002
LYS 285
ILE 286
-0.0101
ILE 286
TYR 287
-0.0000
TYR 287
ASP 288
-0.0011
ASP 288
PRO 289
-0.0002
PRO 289
SER 290
0.0177
SER 290
ILE 291
-0.0003
ILE 291
ASN 292
0.0152
ASN 292
CYS 293
-0.0001
CYS 293
THR 294
0.0015
THR 294
VAL 295
0.0001
VAL 295
ASP 296
0.0078
ASP 296
GLU 297
0.0003
GLU 297
MET 298
0.0003
MET 298
THR 299
0.0001
THR 299
GLU 300
0.0123
GLU 300
ALA 301
0.0003
ALA 301
VAL 302
-0.0189
VAL 302
GLU 303
-0.0001
GLU 303
GLY 304
-0.0155
GLY 304
HIS 305
-0.0000
HIS 305
ILE 306
-0.0260
ILE 306
THR 307
-0.0002
THR 307
THR 308
-0.0589
THR 308
GLU 309
-0.0001
GLU 309
ILE 310
-0.0846
ILE 310
VAL 311
-0.0001
VAL 311
MET 312
0.0168
MET 312
LEU 313
0.0000
LEU 313
ASN 314
0.0200
ASN 314
PRO 315
0.0001
PRO 315
ALA 316
-0.0478
ALA 316
ASN 317
0.0001
ASN 317
THR 318
0.0022
THR 318
ARG 319
0.0004
ARG 319
SER 320
0.0192
SER 320
ILE 321
-0.0003
ILE 321
SER 322
0.0089
SER 322
ASN 323
-0.0001
ASN 323
MET 324
-0.0057
MET 324
THR 325
-0.0001
THR 325
SER 326
-0.0026
SER 326
GLN 327
0.0001
GLN 327
GLU 328
0.0258
GLU 328
PHE 329
-0.0002
PHE 329
VAL 330
-0.0212
VAL 330
GLU 331
0.0003
GLU 331
LYS 332
0.0115
LYS 332
LEU 333
0.0002
LEU 333
THR 334
0.0071
THR 334
LYS 335
-0.0000
LYS 335
ARG 336
0.0008
ARG 336
LEU 337
-0.0002
LEU 337
THR 344
-0.0390
THR 344
GLY 345
-0.0002
GLY 345
GLY 346
0.0076
GLY 346
PHE 347
0.0000
PHE 347
GLN 348
0.1246
GLN 348
GLU 349
-0.0000
GLU 349
ALA 350
-0.0364
ALA 350
PRO 351
-0.0002
PRO 351
LEU 352
0.0132
LEU 352
ALA 353
-0.0002
ALA 353
TYR 354
-0.0090
TYR 354
ASP 355
-0.0001
ASP 355
ALA 356
0.0035
ALA 356
ILE 357
-0.0001
ILE 357
TRP 358
-0.0043
TRP 358
ALA 359
-0.0002
ALA 359
LEU 360
-0.0158
LEU 360
ALA 361
0.0002
ALA 361
LEU 362
0.0024
LEU 362
ALA 363
0.0002
ALA 363
LEU 364
-0.0120
LEU 364
ASN 365
0.0000
ASN 365
LYS 366
0.0064
LYS 366
THR 367
0.0002
THR 367
SER 368
0.0051
SER 368
ARG 377
-0.0152
ARG 377
LEU 378
0.0003
LEU 378
GLU 379
-0.0094
GLU 379
ASP 380
-0.0000
ASP 380
PHE 381
0.0116
PHE 381
ASN 382
0.0003
ASN 382
TYR 383
0.0088
TYR 383
ASN 384
-0.0001
ASN 384
ASN 385
-0.0044
ASN 385
GLN 386
-0.0004
GLN 386
THR 387
0.0066
THR 387
ILE 388
0.0000
ILE 388
THR 389
0.0145
THR 389
ASP 390
-0.0004
ASP 390
GLN 391
0.0034
GLN 391
ILE 392
-0.0002
ILE 392
TYR 393
0.0131
TYR 393
ARG 394
-0.0000
ARG 394
ALA 395
0.0104
ALA 395
MET 396
-0.0002
MET 396
ASN 397
0.0072
ASN 397
SER 398
0.0001
SER 398
SER 399
0.0021
SER 399
SER 400
0.0001
SER 400
PHE 401
0.0042
PHE 401
GLU 402
-0.0001
GLU 402
GLY 403
-0.0072
GLY 403
VAL 404
-0.0000
VAL 404
SER 405
0.0253
SER 405
GLY 406
0.0001
GLY 406
HIS 407
-0.0560
HIS 407
VAL 408
-0.0003
VAL 408
VAL 409
0.0218
VAL 409
PHE 410
0.0001
PHE 410
ASP 411
0.0484
ASP 411
ALA 412
0.0002
ALA 412
SER 413
-0.0496
SER 413
GLY 414
-0.0004
GLY 414
SER 415
-0.1024
SER 415
ARG 416
-0.0002
ARG 416
MET 417
-0.2088
MET 417
ALA 418
0.0001
ALA 418
TRP 419
-0.1066
TRP 419
THR 420
-0.0001
THR 420
LEU 421
-0.0834
LEU 421
ILE 422
0.0003
ILE 422
GLU 423
-0.0584
GLU 423
GLN 424
-0.0004
GLN 424
LEU 425
-0.0365
LEU 425
GLN 426
-0.0000
GLN 426
GLY 427
-0.0223
GLY 427
GLY 428
-0.0001
GLY 428
SER 429
-0.0424
SER 429
TYR 430
0.0002
TYR 430
LYS 431
0.0144
LYS 431
LYS 432
-0.0002
LYS 432
ILE 433
0.0235
ILE 433
GLY 434
0.0000
GLY 434
TYR 435
-0.0755
TYR 435
TYR 436
0.0004
TYR 436
ASP 437
-0.0302
ASP 437
SER 438
-0.0000
SER 438
THR 439
0.0003
THR 439
LYS 440
0.0001
LYS 440
ASP 441
0.0108
ASP 441
ASP 442
0.0001
ASP 442
LEU 443
-0.0219
LEU 443
SER 444
-0.0001
SER 444
TRP 445
-0.0385
TRP 445
SER 446
-0.0000
SER 446
LYS 447
-0.0194
LYS 447
THR 448
-0.0002
THR 448
ASP 449
-0.0081
ASP 449
LYS 450
-0.0002
LYS 450
TRP 451
-0.0414
TRP 451
ILE 452
-0.0000
ILE 452
GLY 453
0.0139
GLY 453
GLY 454
-0.0001
GLY 454
SER 455
-0.0104
SER 455
PRO 456
-0.0001
PRO 456
PRO 457
-0.0129
PRO 457
ALA 458
0.0001
ALA 458
ASP 459
-0.0055
ASP 459
ASP 460
-0.0001
ASP 460
TYR 461
0.0070
TYR 461
LYS 462
-0.0002
LYS 462
ASP 463
0.0426
ASP 463
ASP 464
-0.0001
ASP 464
ASP 465
-0.0229
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.