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
ALA 3
THR 4
-0.0001
THR 4
VAL 5
-0.0943
VAL 5
LEU 6
0.0001
LEU 6
LEU 7
0.0406
LEU 7
GLU 8
-0.0002
GLU 8
VAL 9
0.0224
VAL 9
PRO 10
-0.0002
PRO 10
PHE 11
0.0108
PHE 11
SER 12
-0.0002
SER 12
ALA 13
0.0506
ALA 13
ARG 14
0.0002
ARG 14
GLY 15
-0.0181
GLY 15
ASP 16
-0.0003
ASP 16
ARG 17
0.0164
ARG 17
ILE 18
0.0001
ILE 18
PRO 19
-0.0402
PRO 19
ASP 20
0.0002
ASP 20
ALA 21
-0.0146
ALA 21
VAL 22
0.0001
VAL 22
ALA 23
0.0038
ALA 23
GLU 24
-0.0003
GLU 24
LEU 25
0.0200
LEU 25
ARG 26
-0.0002
ARG 26
THR 27
-0.0169
THR 27
ARG 28
-0.0003
ARG 28
GLU 29
0.0127
GLU 29
PRO 30
-0.0002
PRO 30
ILE 31
0.0200
ILE 31
ARG 32
-0.0002
ARG 32
LYS 33
0.0390
LYS 33
VAL 34
0.0001
VAL 34
ARG 35
0.0578
ARG 35
THR 36
0.0001
THR 36
ILE 37
0.0436
ILE 37
THR 38
-0.0001
THR 38
GLY 39
0.0505
GLY 39
ALA 40
0.0003
ALA 40
GLU 41
0.0104
GLU 41
ALA 42
-0.0004
ALA 42
TRP 43
0.0194
TRP 43
LEU 44
-0.0001
LEU 44
VAL 45
0.0202
VAL 45
SER 46
0.0001
SER 46
SER 47
0.0171
SER 47
TYR 48
0.0004
TYR 48
ALA 49
0.0382
ALA 49
LEU 50
-0.0002
LEU 50
CYS 51
-0.0214
CYS 51
THR 52
-0.0002
THR 52
GLN 53
0.0774
GLN 53
VAL 54
0.0001
VAL 54
LEU 55
-0.0101
LEU 55
GLU 56
0.0001
GLU 56
ASP 57
0.0864
ASP 57
ARG 58
0.0001
ARG 58
ARG 59
0.0452
ARG 59
PHE 60
-0.0001
PHE 60
SER 61
0.0274
SER 61
MET 62
-0.0003
MET 62
LYS 63
-0.0036
LYS 63
GLU 64
0.0002
GLU 64
THR 65
-0.0166
THR 65
ALA 66
-0.0001
ALA 66
ALA 67
0.0106
ALA 67
ALA 68
-0.0000
ALA 68
GLY 69
0.0473
GLY 69
ALA 70
0.0001
ALA 70
PRO 71
0.0051
PRO 71
ARG 72
-0.0000
ARG 72
LEU 73
-0.0954
LEU 73
ASN 74
0.0000
ASN 74
ALA 75
0.1239
ALA 75
LEU 76
-0.0001
LEU 76
THR 77
0.0032
THR 77
VAL 78
-0.0000
VAL 78
PRO 79
-0.0970
PRO 79
PRO 80
0.0003
PRO 80
GLU 81
0.0733
GLU 81
VAL 82
-0.0001
VAL 82
VAL 83
0.1216
VAL 83
ASN 84
0.0002
ASN 84
ASN 85
0.0672
ASN 85
MET 86
0.0005
MET 86
GLY 87
0.0151
GLY 87
ASN 88
0.0004
ASN 88
ILE 89
0.0525
ILE 89
ALA 90
0.0003
ALA 90
ASP 91
0.0377
ASP 91
ALA 92
0.0002
ALA 92
GLY 93
0.0433
GLY 93
LEU 94
0.0001
LEU 94
ARG 95
0.0453
ARG 95
LYS 96
0.0001
LYS 96
ALA 97
-0.0159
ALA 97
VAL 98
-0.0004
VAL 98
MET 99
0.0121
MET 99
LYS 100
-0.0000
LYS 100
ALA 101
0.0356
ALA 101
ILE 102
-0.0003
ILE 102
THR 103
0.0089
THR 103
PRO 104
0.0001
PRO 104
LYS 105
-0.0428
LYS 105
ALA 106
-0.0002
ALA 106
PRO 107
0.0069
PRO 107
GLY 108
-0.0001
GLY 108
LEU 109
-0.0085
LEU 109
GLU 110
0.0000
GLU 110
GLN 111
0.0217
GLN 111
PHE 112
0.0001
PHE 112
LEU 113
-0.0432
LEU 113
ARG 114
-0.0001
ARG 114
ASP 115
0.0089
ASP 115
THR 116
0.0002
THR 116
ALA 117
-0.1021
ALA 117
ASN 118
0.0001
ASN 118
SER 119
0.0250
SER 119
LEU 120
0.0001
LEU 120
LEU 121
-0.0720
LEU 121
ASP 122
-0.0001
ASP 122
ASN 123
0.0371
ASN 123
LEU 124
-0.0001
LEU 124
ILE 125
-0.0607
ILE 125
THR 126
-0.0000
THR 126
GLU 127
0.0216
GLU 127
GLY 128
-0.0000
GLY 128
ALA 129
0.0243
ALA 129
PRO 130
0.0000
PRO 130
ALA 131
-0.0552
ALA 131
ASP 132
0.0002
ASP 132
LEU 133
0.0034
LEU 133
ARG 134
-0.0003
ARG 134
ASN 135
-0.0205
ASN 135
ASP 136
-0.0003
ASP 136
PHE 137
0.0397
PHE 137
ALA 138
0.0002
ALA 138
ASP 139
-0.1114
ASP 139
PRO 140
-0.0001
PRO 140
LEU 141
0.0002
LEU 141
ALA 142
-0.0003
ALA 142
THR 143
-0.0617
THR 143
ALA 144
0.0001
ALA 144
LEU 145
-0.0290
LEU 145
HIS 146
0.0001
HIS 146
CYS 147
-0.0044
CYS 147
LYS 148
0.0000
LYS 148
VAL 149
0.0231
VAL 149
LEU 150
-0.0001
LEU 150
GLY 151
0.0118
GLY 151
ILE 152
-0.0002
ILE 152
PRO 153
0.0452
PRO 153
GLN 154
-0.0000
GLN 154
GLU 155
-0.0239
GLU 155
ASP 156
0.0001
ASP 156
GLY 157
-0.0425
GLY 157
PRO 158
0.0004
PRO 158
LYS 159
-0.0356
LYS 159
LEU 160
-0.0003
LEU 160
PHE 161
-0.0989
PHE 161
ARG 162
-0.0000
ARG 162
SER 163
-0.0516
SER 163
LEU 164
0.0001
LEU 164
SER 165
0.0164
SER 165
ILE 166
-0.0004
ILE 166
ALA 167
-0.0244
ALA 167
PHE 168
0.0002
PHE 168
MET 169
0.0478
MET 169
SER 170
0.0002
SER 170
SER 171
-0.0113
SER 171
ALA 172
-0.0002
ALA 172
ASP 173
0.0598
ASP 173
PRO 174
0.0001
PRO 174
ILE 175
-0.0154
ILE 175
PRO 176
-0.0002
PRO 176
ALA 177
0.0212
ALA 177
ALA 178
0.0004
ALA 178
LYS 179
0.0051
LYS 179
ILE 180
0.0001
ILE 180
ASN 181
-0.0422
ASN 181
TRP 182
-0.0000
TRP 182
ASP 183
0.0214
ASP 183
ARG 184
-0.0004
ARG 184
ASP 185
-0.0004
ASP 185
ILE 186
-0.0003
ILE 186
GLU 187
0.0043
GLU 187
TYR 188
0.0001
TYR 188
MET 189
-0.0298
MET 189
ALA 190
-0.0002
ALA 190
GLY 191
0.0161
GLY 191
ILE 192
-0.0004
ILE 192
LEU 193
-0.0795
LEU 193
GLU 194
0.0001
GLU 194
ASN 195
-0.0327
ASN 195
PRO 196
-0.0001
PRO 196
ASN 197
-0.0178
ASN 197
ILE 198
0.0001
ILE 198
THR 199
0.0236
THR 199
THR 200
-0.0001
THR 200
GLY 201
-0.0341
GLY 201
LEU 202
0.0002
LEU 202
MET 203
0.0013
MET 203
GLY 204
0.0003
GLY 204
GLU 205
0.0315
GLU 205
LEU 206
-0.0002
LEU 206
SER 207
0.0170
SER 207
ARG 208
-0.0002
ARG 208
LEU 209
-0.0185
LEU 209
ARG 210
0.0003
ARG 210
LYS 211
0.0563
LYS 211
ASP 212
-0.0002
ASP 212
PRO 213
-0.0845
PRO 213
ALA 214
0.0000
ALA 214
TYR 215
0.0296
TYR 215
SER 216
-0.0002
SER 216
HIS 217
-0.0123
HIS 217
VAL 218
-0.0002
VAL 218
SER 219
-0.0479
SER 219
ASP 220
0.0002
ASP 220
GLU 221
0.1116
GLU 221
LEU 222
0.0003
LEU 222
PHE 223
0.0749
PHE 223
ALA 224
-0.0003
ALA 224
THR 225
0.1020
THR 225
ILE 226
0.0001
ILE 226
GLY 227
0.0040
GLY 227
VAL 228
-0.0001
VAL 228
THR 229
0.0022
THR 229
PHE 230
0.0003
PHE 230
PHE 231
-0.0378
PHE 231
GLY 232
0.0001
GLY 232
ALA 233
0.0215
ALA 233
GLY 234
0.0000
GLY 234
VAL 235
-0.0163
VAL 235
ILE 236
0.0004
ILE 236
SER 237
-0.0275
SER 237
THR 238
0.0001
THR 238
GLY 239
-0.0046
GLY 239
SER 240
-0.0000
SER 240
PHE 241
-0.0217
PHE 241
LEU 242
-0.0005
LEU 242
THR 243
0.0119
THR 243
THR 244
0.0001
THR 244
ALA 245
-0.0230
ALA 245
LEU 246
0.0000
LEU 246
ILE 247
-0.0191
ILE 247
SER 248
0.0001
SER 248
LEU 249
-0.0260
LEU 249
ILE 250
-0.0001
ILE 250
GLN 251
0.0162
GLN 251
ARG 252
0.0001
ARG 252
PRO 253
0.0178
PRO 253
GLN 254
0.0003
GLN 254
LEU 255
0.0442
LEU 255
ARG 256
-0.0001
ARG 256
ASN 257
-0.0046
ASN 257
LEU 258
-0.0002
LEU 258
LEU 259
-0.0069
LEU 259
HIS 260
-0.0002
HIS 260
GLU 261
-0.0299
GLU 261
LYS 262
-0.0002
LYS 262
PRO 263
-0.0072
PRO 263
GLU 264
-0.0002
GLU 264
LEU 265
-0.0033
LEU 265
ILE 266
-0.0002
ILE 266
PRO 267
0.0370
PRO 267
ALA 268
0.0000
ALA 268
GLY 269
-0.0006
GLY 269
VAL 270
-0.0000
VAL 270
GLU 271
-0.0138
GLU 271
GLU 272
0.0001
GLU 272
LEU 273
0.0007
LEU 273
LEU 274
0.0000
LEU 274
ARG 275
-0.0736
ARG 275
ILE 276
0.0001
ILE 276
ASN 277
0.0009
ASN 277
LEU 278
-0.0002
LEU 278
SER 279
0.0105
SER 279
PHE 280
0.0001
PHE 280
ALA 281
-0.0087
ALA 281
ASP 282
0.0001
ASP 282
GLY 283
-0.0151
GLY 283
LEU 284
0.0002
LEU 284
PRO 285
-0.0186
PRO 285
ARG 286
-0.0001
ARG 286
LEU 287
-0.0107
LEU 287
ALA 288
0.0000
ALA 288
THR 289
-0.0229
THR 289
ALA 290
0.0003
ALA 290
ASP 291
0.0014
ASP 291
ILE 292
0.0001
ILE 292
GLN 293
-0.0000
GLN 293
VAL 294
-0.0002
VAL 294
GLY 295
-0.0074
GLY 295
ASP 296
-0.0001
ASP 296
VAL 297
0.0173
VAL 297
LEU 298
0.0001
LEU 298
VAL 299
0.0147
VAL 299
ARG 300
0.0002
ARG 300
LYS 301
0.0266
LYS 301
GLY 302
0.0002
GLY 302
GLU 303
-0.0616
GLU 303
LEU 304
0.0002
LEU 304
VAL 305
0.0076
VAL 305
LEU 306
-0.0000
LEU 306
VAL 307
0.0228
VAL 307
LEU 308
0.0003
LEU 308
LEU 309
-0.0090
LEU 309
GLU 310
0.0003
GLU 310
GLY 311
-0.0058
GLY 311
ALA 312
0.0002
ALA 312
ASN 313
0.0348
ASN 313
PHE 314
-0.0001
PHE 314
ASP 315
0.0350
ASP 315
PRO 316
0.0002
PRO 316
GLU 317
-0.0068
GLU 317
HIS 318
0.0004
HIS 318
PHE 319
0.0643
PHE 319
PRO 320
0.0000
PRO 320
ASN 321
0.0222
ASN 321
PRO 322
-0.0000
PRO 322
GLY 323
0.0496
GLY 323
SER 324
-0.0002
SER 324
ILE 325
-0.0203
ILE 325
GLU 326
-0.0001
GLU 326
LEU 327
-0.0591
LEU 327
ASP 328
-0.0004
ASP 328
ARG 329
0.0431
ARG 329
PRO 330
0.0001
PRO 330
ASN 331
0.0457
ASN 331
PRO 332
0.0003
PRO 332
THR 333
0.0205
THR 333
SER 334
0.0003
SER 334
HIS 335
0.0373
HIS 335
LEU 336
-0.0001
LEU 336
ALA 337
-0.0456
ALA 337
PHE 338
-0.0006
PHE 338
GLY 339
0.0363
GLY 339
ARG 340
-0.0001
ARG 340
GLY 341
0.0917
GLY 341
GLN 342
-0.0001
GLN 342
HIS 343
-0.0047
HIS 343
PHE 344
0.0001
PHE 344
CYS 345
-0.0650
CYS 345
PRO 346
-0.0002
PRO 346
GLY 347
0.0514
GLY 347
SER 348
0.0002
SER 348
ALA 349
-0.0269
ALA 349
LEU 350
0.0001
LEU 350
GLY 351
-0.0157
GLY 351
ARG 352
0.0001
ARG 352
ARG 353
-0.0756
ARG 353
HIS 354
-0.0002
HIS 354
ALA 355
-0.0491
ALA 355
GLN 356
0.0000
GLN 356
ILE 357
-0.0648
ILE 357
GLY 358
0.0002
GLY 358
ILE 359
-0.0547
ILE 359
GLU 360
0.0001
GLU 360
ALA 361
-0.0049
ALA 361
LEU 362
-0.0002
LEU 362
LEU 363
-0.0598
LEU 363
LYS 364
-0.0001
LYS 364
LYS 365
0.0339
LYS 365
MET 366
-0.0002
MET 366
PRO 367
0.0048
PRO 367
GLY 368
-0.0001
GLY 368
VAL 369
-0.0535
VAL 369
ASP 370
0.0003
ASP 370
LEU 371
-0.0605
LEU 371
ALA 372
0.0002
ALA 372
VAL 373
-0.0146
VAL 373
PRO 374
0.0001
PRO 374
ILE 375
0.0194
ILE 375
ASP 376
0.0001
ASP 376
GLN 377
0.0104
GLN 377
LEU 378
0.0001
LEU 378
VAL 379
-0.0958
VAL 379
TRP 380
-0.0001
TRP 380
ARG 381
-0.1074
ARG 381
THR 382
-0.0001
THR 382
ARG 383
-0.1711
ARG 383
PHE 384
-0.0001
PHE 384
GLN 385
0.0175
GLN 385
ARG 386
-0.0001
ARG 386
ARG 387
0.0116
ARG 387
ILE 388
-0.0002
ILE 388
PRO 389
-0.0307
PRO 389
GLU 390
-0.0002
GLU 390
ARG 391
-0.1003
ARG 391
LEU 392
-0.0003
LEU 392
PRO 393
-0.0550
PRO 393
VAL 394
0.0000
VAL 394
LEU 395
-0.0466
LEU 395
TRP 396
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.