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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 4
ALA 5
-0.0001
ALA 5
ALA 6
0.0061
ALA 6
ILE 7
0.0001
ILE 7
GLY 8
-0.0077
GLY 8
ILE 9
-0.0002
ILE 9
ASP 10
0.0008
ASP 10
LEU 11
-0.0001
LEU 11
GLY 12
0.0363
GLY 12
THR 13
-0.0003
THR 13
THR 14
0.0431
THR 14
TYR 15
0.0002
TYR 15
SER 16
0.0330
SER 16
CYS 17
0.0000
CYS 17
VAL 18
0.0128
VAL 18
GLY 19
-0.0001
GLY 19
VAL 20
0.0158
VAL 20
PHE 21
-0.0003
PHE 21
GLN 22
-0.0200
GLN 22
HIS 23
0.0001
HIS 23
GLY 24
0.0006
GLY 24
LYS 25
-0.0001
LYS 25
VAL 26
0.0123
VAL 26
GLU 27
-0.0000
GLU 27
ILE 28
0.0488
ILE 28
ILE 29
-0.0002
ILE 29
ALA 30
0.0408
ALA 30
ASN 31
-0.0000
ASN 31
ASP 32
0.0051
ASP 32
GLN 33
-0.0002
GLN 33
GLY 34
-0.0305
GLY 34
ASN 35
-0.0002
ASN 35
ARG 36
-0.0722
ARG 36
THR 37
-0.0003
THR 37
THR 38
-0.0916
THR 38
PRO 39
-0.0001
PRO 39
SER 40
-0.0046
SER 40
TYR 41
-0.0001
TYR 41
VAL 42
-0.0531
VAL 42
ALA 43
-0.0001
ALA 43
PHE 44
-0.0921
PHE 44
THR 45
-0.0001
THR 45
ASP 46
-0.0905
ASP 46
THR 47
-0.0001
THR 47
GLU 48
0.0652
GLU 48
ARG 49
-0.0003
ARG 49
LEU 50
-0.1559
LEU 50
ILE 51
-0.0001
ILE 51
GLY 52
-0.1428
GLY 52
ASP 53
-0.0003
ASP 53
ALA 54
-0.0800
ALA 54
ALA 55
0.0000
ALA 55
LYS 56
-0.1411
LYS 56
ASN 57
-0.0001
ASN 57
GLN 58
-0.1188
GLN 58
VAL 59
-0.0004
VAL 59
ALA 60
0.1693
ALA 60
LEU 61
-0.0001
LEU 61
ASN 62
-0.0305
ASN 62
PRO 63
-0.0002
PRO 63
GLN 64
0.0676
GLN 64
ASN 65
0.0002
ASN 65
THR 66
-0.0394
THR 66
VAL 67
-0.0002
VAL 67
PHE 68
0.0154
PHE 68
ASP 69
0.0002
ASP 69
ALA 70
0.0232
ALA 70
LYS 71
-0.0001
LYS 71
ARG 72
-0.0223
ARG 72
LEU 73
0.0004
LEU 73
ILE 74
-0.0557
ILE 74
GLY 75
-0.0001
GLY 75
ARG 76
-0.1870
ARG 76
LYS 77
-0.0000
LYS 77
PHE 78
0.0014
PHE 78
GLY 79
0.0002
GLY 79
ASP 80
-0.0264
ASP 80
PRO 81
-0.0002
PRO 81
VAL 82
0.1179
VAL 82
VAL 83
-0.0001
VAL 83
GLN 84
-0.0457
GLN 84
SER 85
0.0002
SER 85
ASP 86
0.0001
ASP 86
MET 87
0.0001
MET 87
LYS 88
0.0074
LYS 88
HIS 89
-0.0001
HIS 89
TRP 90
-0.0188
TRP 90
PRO 91
-0.0005
PRO 91
PHE 92
0.0821
PHE 92
GLN 93
-0.0001
GLN 93
VAL 94
0.0127
VAL 94
ILE 95
-0.0001
ILE 95
ASN 96
0.0231
ASN 96
ASP 97
0.0002
ASP 97
GLY 98
0.0029
GLY 98
ASP 99
0.0001
ASP 99
LYS 100
-0.0713
LYS 100
PRO 101
-0.0001
PRO 101
LYS 102
0.0398
LYS 102
VAL 103
-0.0004
VAL 103
GLN 104
0.0357
GLN 104
VAL 105
-0.0003
VAL 105
SER 106
0.0122
SER 106
TYR 107
0.0002
TYR 107
LYS 108
0.0222
LYS 108
GLY 109
-0.0002
GLY 109
GLU 110
0.0404
GLU 110
THR 111
-0.0001
THR 111
LYS 112
0.0474
LYS 112
ALA 113
0.0001
ALA 113
PHE 114
0.0456
PHE 114
TYR 115
0.0001
TYR 115
PRO 116
0.1003
PRO 116
GLU 117
0.0001
GLU 117
GLU 118
0.1433
GLU 118
ILE 119
-0.0000
ILE 119
SER 120
0.0116
SER 120
SER 121
-0.0001
SER 121
MET 122
0.1225
MET 122
VAL 123
-0.0001
VAL 123
LEU 124
0.0598
LEU 124
THR 125
0.0000
THR 125
LYS 126
-0.0190
LYS 126
MET 127
0.0003
MET 127
LYS 128
0.0323
LYS 128
GLU 129
0.0001
GLU 129
ILE 130
-0.0434
ILE 130
ALA 131
-0.0005
ALA 131
GLU 132
0.0075
GLU 132
ALA 133
-0.0005
ALA 133
TYR 134
-0.0226
TYR 134
LEU 135
0.0002
LEU 135
GLY 136
-0.0074
GLY 136
TYR 137
-0.0000
TYR 137
PRO 138
-0.0140
PRO 138
VAL 139
-0.0000
VAL 139
THR 140
-0.0270
THR 140
ASN 141
0.0002
ASN 141
ALA 142
0.0204
ALA 142
VAL 143
0.0000
VAL 143
ILE 144
-0.0129
ILE 144
THR 145
-0.0001
THR 145
VAL 146
-0.0237
VAL 146
PRO 147
0.0006
PRO 147
ALA 148
0.0705
ALA 148
TYR 149
0.0001
TYR 149
PHE 150
0.2089
PHE 150
ASN 151
0.0003
ASN 151
ASP 152
0.0318
ASP 152
SER 153
0.0003
SER 153
GLN 154
0.0202
GLN 154
ARG 155
0.0001
ARG 155
GLN 156
0.0972
GLN 156
ALA 157
0.0001
ALA 157
THR 158
-0.0127
THR 158
LYS 159
0.0000
LYS 159
ASP 160
0.0266
ASP 160
ALA 161
-0.0000
ALA 161
GLY 162
-0.0440
GLY 162
VAL 163
-0.0001
VAL 163
ILE 164
-0.0035
ILE 164
ALA 165
-0.0003
ALA 165
GLY 166
-0.0089
GLY 166
LEU 167
-0.0002
LEU 167
ASN 168
0.0565
ASN 168
VAL 169
-0.0001
VAL 169
LEU 170
-0.0126
LEU 170
ARG 171
-0.0001
ARG 171
ILE 172
-0.0603
ILE 172
ILE 173
0.0001
ILE 173
ASN 174
0.0523
ASN 174
GLU 175
0.0004
GLU 175
PRO 176
0.0506
PRO 176
THR 177
0.0004
THR 177
ALA 178
0.0087
ALA 178
ALA 179
0.0001
ALA 179
ALA 180
-0.0238
ALA 180
ILE 181
-0.0001
ILE 181
ALA 182
0.0099
ALA 182
TYR 183
-0.0000
TYR 183
GLY 184
-0.1468
GLY 184
LEU 185
-0.0002
LEU 185
ASP 186
-0.0174
ASP 186
ARG 187
0.0000
ARG 187
THR 188
0.1079
THR 188
GLY 189
0.0000
GLY 189
LYS 190
-0.0265
LYS 190
GLY 191
0.0000
GLY 191
GLU 192
0.0474
GLU 192
ARG 193
0.0003
ARG 193
ASN 194
-0.0154
ASN 194
VAL 195
0.0001
VAL 195
LEU 196
-0.0451
LEU 196
ILE 197
-0.0003
ILE 197
PHE 198
-0.0267
PHE 198
ASP 199
-0.0001
ASP 199
LEU 200
0.0020
LEU 200
GLY 201
-0.0001
GLY 201
GLY 202
-0.0521
GLY 202
GLY 203
0.0001
GLY 203
THR 204
0.0634
THR 204
PHE 205
0.0001
PHE 205
ASP 206
0.0714
ASP 206
VAL 207
0.0001
VAL 207
SER 208
0.0376
SER 208
ILE 209
-0.0001
ILE 209
LEU 210
-0.0126
LEU 210
THR 211
-0.0002
THR 211
ILE 212
-0.0110
ILE 212
ASP 213
0.0002
ASP 213
ASP 214
-0.0334
ASP 214
GLY 215
-0.0002
GLY 215
ILE 216
-0.0036
ILE 216
PHE 217
-0.0003
PHE 217
GLU 218
-0.0453
GLU 218
VAL 219
-0.0001
VAL 219
LYS 220
0.0728
LYS 220
ALA 221
-0.0002
ALA 221
THR 222
0.1540
THR 222
ALA 223
-0.0002
ALA 223
GLY 224
0.1589
GLY 224
ASP 225
0.0001
ASP 225
THR 226
0.1662
THR 226
HIS 227
0.0005
HIS 227
LEU 228
0.2777
LEU 228
GLY 229
0.0005
GLY 229
GLY 230
0.0460
GLY 230
GLU 231
-0.0004
GLU 231
ASP 232
-0.0233
ASP 232
PHE 233
0.0002
PHE 233
ASP 234
-0.0868
ASP 234
ASN 235
0.0002
ASN 235
ARG 236
-0.0203
ARG 236
LEU 237
-0.0002
LEU 237
VAL 238
-0.1150
VAL 238
ASN 239
0.0001
ASN 239
HIS 240
0.0673
HIS 240
PHE 241
0.0001
PHE 241
VAL 242
-0.1372
VAL 242
GLU 243
0.0005
GLU 243
GLU 244
0.0203
GLU 244
PHE 245
-0.0001
PHE 245
LYS 246
-0.0297
LYS 246
ARG 247
-0.0001
ARG 247
LYS 248
0.0175
LYS 248
HIS 249
-0.0003
HIS 249
LYS 250
-0.0038
LYS 250
LYS 251
0.0001
LYS 251
ASP 252
0.0909
ASP 252
ILE 253
-0.0002
ILE 253
SER 254
-0.0092
SER 254
GLN 255
0.0004
GLN 255
ASN 256
0.0237
ASN 256
LYS 257
-0.0002
LYS 257
ARG 258
-0.0238
ARG 258
ALA 259
-0.0002
ALA 259
VAL 260
-0.0039
VAL 260
ARG 261
-0.0002
ARG 261
ARG 262
-0.0762
ARG 262
LEU 263
0.0001
LEU 263
ARG 264
0.0616
ARG 264
THR 265
-0.0003
THR 265
ALA 266
-0.0818
ALA 266
CYS 267
0.0000
CYS 267
GLU 268
0.0157
GLU 268
ARG 269
0.0001
ARG 269
ALA 270
-0.1366
ALA 270
LYS 271
-0.0002
LYS 271
ARG 272
-0.0229
ARG 272
THR 273
-0.0004
THR 273
LEU 274
-0.0611
LEU 274
SER 275
-0.0004
SER 275
SER 276
0.0300
SER 276
SER 277
-0.0005
SER 277
THR 278
0.0210
THR 278
GLN 279
0.0002
GLN 279
ALA 280
0.0306
ALA 280
SER 281
0.0004
SER 281
LEU 282
0.0304
LEU 282
GLU 283
0.0001
GLU 283
ILE 284
0.0066
ILE 284
ASP 285
0.0001
ASP 285
SER 286
0.0205
SER 286
LEU 287
-0.0003
LEU 287
PHE 288
-0.0043
PHE 288
GLU 289
0.0002
GLU 289
GLY 290
-0.0103
GLY 290
ILE 291
-0.0002
ILE 291
ASP 292
-0.0232
ASP 292
PHE 293
-0.0004
PHE 293
TYR 294
-0.0368
TYR 294
THR 295
0.0004
THR 295
SER 296
-0.0926
SER 296
ILE 297
0.0000
ILE 297
THR 298
-0.1522
THR 298
ARG 299
-0.0003
ARG 299
ALA 300
0.0035
ALA 300
ARG 301
0.0003
ARG 301
PHE 302
0.0289
PHE 302
GLU 303
0.0004
GLU 303
GLU 304
-0.0719
GLU 304
LEU 305
0.0001
LEU 305
CYS 306
-0.0329
CYS 306
SER 307
0.0000
SER 307
ASP 308
0.0038
ASP 308
LEU 309
-0.0000
LEU 309
PHE 310
-0.0180
PHE 310
ARG 311
0.0001
ARG 311
SER 312
0.0476
SER 312
THR 313
0.0003
THR 313
LEU 314
0.0009
LEU 314
GLU 315
0.0002
GLU 315
PRO 316
0.0201
PRO 316
VAL 317
-0.0000
VAL 317
GLU 318
0.0118
GLU 318
LYS 319
0.0002
LYS 319
ALA 320
-0.0076
ALA 320
LEU 321
-0.0002
LEU 321
ARG 322
0.0001
ARG 322
ASP 323
0.0001
ASP 323
ALA 324
-0.0042
ALA 324
LYS 325
0.0002
LYS 325
LEU 326
-0.0639
LEU 326
ASP 327
-0.0003
ASP 327
LYS 328
-0.1081
LYS 328
ALA 329
-0.0001
ALA 329
GLN 330
-0.0572
GLN 330
ILE 331
-0.0000
ILE 331
HIS 332
-0.0092
HIS 332
ASP 333
-0.0001
ASP 333
LEU 334
-0.0996
LEU 334
VAL 335
0.0002
VAL 335
LEU 336
-0.1228
LEU 336
VAL 337
-0.0000
VAL 337
GLY 338
0.0100
GLY 338
GLY 339
-0.0003
GLY 339
SER 340
-0.0066
SER 340
THR 341
-0.0002
THR 341
ARG 342
-0.0248
ARG 342
ILE 343
0.0001
ILE 343
PRO 344
0.0300
PRO 344
LYS 345
-0.0002
LYS 345
VAL 346
-0.0147
VAL 346
GLN 347
0.0000
GLN 347
LYS 348
0.0960
LYS 348
LEU 349
-0.0000
LEU 349
LEU 350
-0.0521
LEU 350
GLN 351
0.0003
GLN 351
ASP 352
0.0746
ASP 352
PHE 353
-0.0006
PHE 353
PHE 354
-0.0121
PHE 354
ASN 355
-0.0000
ASN 355
GLY 356
0.0154
GLY 356
ARG 357
-0.0003
ARG 357
ASP 358
0.0277
ASP 358
LEU 359
0.0004
LEU 359
ASN 360
-0.0000
ASN 360
LYS 361
0.0002
LYS 361
SER 362
-0.0039
SER 362
ILE 363
-0.0002
ILE 363
ASN 364
-0.0563
ASN 364
PRO 365
0.0001
PRO 365
ASP 366
-0.0887
ASP 366
GLU 367
0.0000
GLU 367
ALA 368
-0.0570
ALA 368
VAL 369
-0.0003
VAL 369
ALA 370
-0.0133
ALA 370
TYR 371
0.0000
TYR 371
GLY 372
0.0210
GLY 372
ALA 373
-0.0003
ALA 373
ALA 374
-0.0132
ALA 374
VAL 375
0.0003
VAL 375
GLN 376
-0.0476
GLN 376
ALA 377
-0.0001
ALA 377
ALA 378
0.0371
ALA 378
ILE 379
0.0001
ILE 379
LEU 380
0.0214
LEU 380
ILE 381
-0.0006
ILE 381
LYS 382
-0.3095
LYS 382
SER 383
0.0001
SER 383
THR 384
-0.1950
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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.