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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
-0.0003
ALA 5
ALA 6
-0.0174
ALA 6
ILE 7
0.0000
ILE 7
GLY 8
-0.0154
GLY 8
ILE 9
-0.0002
ILE 9
ASP 10
0.0077
ASP 10
LEU 11
0.0003
LEU 11
GLY 12
-0.0005
GLY 12
THR 13
-0.0001
THR 13
THR 14
0.0235
THR 14
TYR 15
-0.0002
TYR 15
SER 16
0.0223
SER 16
CYS 17
-0.0002
CYS 17
VAL 18
0.0164
VAL 18
GLY 19
-0.0004
GLY 19
VAL 20
-0.0024
VAL 20
PHE 21
-0.0001
PHE 21
GLN 22
0.0013
GLN 22
HIS 23
0.0002
HIS 23
GLY 24
-0.0005
GLY 24
LYS 25
-0.0002
LYS 25
VAL 26
0.0004
VAL 26
GLU 27
-0.0002
GLU 27
ILE 28
-0.0317
ILE 28
ILE 29
0.0002
ILE 29
ALA 30
-0.0216
ALA 30
ASN 31
-0.0003
ASN 31
ASP 32
0.0116
ASP 32
GLN 33
-0.0001
GLN 33
GLY 34
-0.0125
GLY 34
ASN 35
-0.0000
ASN 35
ARG 36
-0.0206
ARG 36
THR 37
-0.0002
THR 37
THR 38
-0.0361
THR 38
PRO 39
-0.0002
PRO 39
SER 40
0.0016
SER 40
TYR 41
0.0002
TYR 41
VAL 42
-0.0201
VAL 42
ALA 43
-0.0001
ALA 43
PHE 44
-0.0267
PHE 44
THR 45
-0.0001
THR 45
ASP 46
-0.0200
ASP 46
THR 47
-0.0000
THR 47
GLU 48
0.0523
GLU 48
ARG 49
0.0003
ARG 49
LEU 50
-0.0250
LEU 50
ILE 51
0.0001
ILE 51
GLY 52
-0.0439
GLY 52
ASP 53
0.0002
ASP 53
ALA 54
-0.0311
ALA 54
ALA 55
0.0000
ALA 55
LYS 56
0.0102
LYS 56
ASN 57
0.0000
ASN 57
GLN 58
-0.0350
GLN 58
VAL 59
0.0001
VAL 59
ALA 60
0.1404
ALA 60
LEU 61
-0.0003
LEU 61
ASN 62
0.1091
ASN 62
PRO 63
0.0002
PRO 63
GLN 64
0.0596
GLN 64
ASN 65
0.0003
ASN 65
THR 66
-0.0270
THR 66
VAL 67
-0.0003
VAL 67
PHE 68
-0.0202
PHE 68
ASP 69
0.0003
ASP 69
ALA 70
0.0288
ALA 70
LYS 71
-0.0003
LYS 71
ARG 72
-0.0057
ARG 72
LEU 73
0.0002
LEU 73
ILE 74
0.0134
ILE 74
GLY 75
-0.0003
GLY 75
ARG 76
-0.0325
ARG 76
LYS 77
-0.0002
LYS 77
PHE 78
0.0016
PHE 78
GLY 79
0.0001
GLY 79
ASP 80
-0.0099
ASP 80
PRO 81
0.0002
PRO 81
VAL 82
0.0268
VAL 82
VAL 83
0.0005
VAL 83
GLN 84
-0.0065
GLN 84
SER 85
-0.0000
SER 85
ASP 86
0.0029
ASP 86
MET 87
-0.0002
MET 87
LYS 88
-0.0057
LYS 88
HIS 89
0.0002
HIS 89
TRP 90
-0.0243
TRP 90
PRO 91
0.0000
PRO 91
PHE 92
0.0679
PHE 92
GLN 93
-0.0001
GLN 93
VAL 94
0.0327
VAL 94
ILE 95
-0.0001
ILE 95
ASN 96
0.0040
ASN 96
ASP 97
-0.0002
ASP 97
GLY 98
0.0048
GLY 98
ASP 99
0.0001
ASP 99
LYS 100
-0.0126
LYS 100
PRO 101
0.0002
PRO 101
LYS 102
-0.0075
LYS 102
VAL 103
0.0000
VAL 103
GLN 104
-0.0017
GLN 104
VAL 105
-0.0001
VAL 105
SER 106
-0.0299
SER 106
TYR 107
-0.0002
TYR 107
LYS 108
0.0013
LYS 108
GLY 109
-0.0001
GLY 109
GLU 110
0.0041
GLU 110
THR 111
-0.0002
THR 111
LYS 112
0.0366
LYS 112
ALA 113
-0.0000
ALA 113
PHE 114
0.0208
PHE 114
TYR 115
-0.0001
TYR 115
PRO 116
0.0092
PRO 116
GLU 117
-0.0001
GLU 117
GLU 118
0.0529
GLU 118
ILE 119
0.0002
ILE 119
SER 120
0.0106
SER 120
SER 121
0.0002
SER 121
MET 122
0.0750
MET 122
VAL 123
-0.0001
VAL 123
LEU 124
0.0805
LEU 124
THR 125
-0.0001
THR 125
LYS 126
-0.0216
LYS 126
MET 127
0.0003
MET 127
LYS 128
0.0461
LYS 128
GLU 129
-0.0000
GLU 129
ILE 130
-0.0115
ILE 130
ALA 131
0.0000
ALA 131
GLU 132
0.0061
GLU 132
ALA 133
0.0001
ALA 133
TYR 134
-0.0229
TYR 134
LEU 135
0.0003
LEU 135
GLY 136
-0.0191
GLY 136
TYR 137
-0.0002
TYR 137
PRO 138
-0.0421
PRO 138
VAL 139
0.0001
VAL 139
THR 140
-0.0353
THR 140
ASN 141
0.0001
ASN 141
ALA 142
-0.0371
ALA 142
VAL 143
-0.0000
VAL 143
ILE 144
0.0173
ILE 144
THR 145
-0.0002
THR 145
VAL 146
-0.0140
VAL 146
PRO 147
0.0002
PRO 147
ALA 148
0.0110
ALA 148
TYR 149
0.0003
TYR 149
PHE 150
0.0130
PHE 150
ASN 151
0.0004
ASN 151
ASP 152
-0.0035
ASP 152
SER 153
-0.0002
SER 153
GLN 154
0.0034
GLN 154
ARG 155
0.0005
ARG 155
GLN 156
0.0087
GLN 156
ALA 157
-0.0001
ALA 157
THR 158
0.0096
THR 158
LYS 159
0.0002
LYS 159
ASP 160
0.0471
ASP 160
ALA 161
0.0000
ALA 161
GLY 162
0.0525
GLY 162
VAL 163
-0.0001
VAL 163
ILE 164
0.0544
ILE 164
ALA 165
0.0001
ALA 165
GLY 166
0.0955
GLY 166
LEU 167
-0.0003
LEU 167
ASN 168
0.0794
ASN 168
VAL 169
0.0002
VAL 169
LEU 170
0.1856
LEU 170
ARG 171
-0.0001
ARG 171
ILE 172
0.0204
ILE 172
ILE 173
-0.0002
ILE 173
ASN 174
-0.0640
ASN 174
GLU 175
0.0000
GLU 175
PRO 176
0.0039
PRO 176
THR 177
-0.0000
THR 177
ALA 178
-0.0170
ALA 178
ALA 179
0.0003
ALA 179
ALA 180
0.0084
ALA 180
ILE 181
0.0004
ILE 181
ALA 182
-0.0278
ALA 182
TYR 183
-0.0001
TYR 183
GLY 184
-0.0782
GLY 184
LEU 185
-0.0000
LEU 185
ASP 186
-0.0587
ASP 186
ARG 187
-0.0001
ARG 187
THR 188
0.0136
THR 188
GLY 189
0.0000
GLY 189
LYS 190
-0.0134
LYS 190
GLY 191
-0.0002
GLY 191
GLU 192
0.0149
GLU 192
ARG 193
-0.0001
ARG 193
ASN 194
0.0005
ASN 194
VAL 195
0.0001
VAL 195
LEU 196
-0.0227
LEU 196
ILE 197
0.0000
ILE 197
PHE 198
-0.0521
PHE 198
ASP 199
-0.0002
ASP 199
LEU 200
-0.0295
LEU 200
GLY 201
0.0002
GLY 201
GLY 202
0.0160
GLY 202
GLY 203
0.0005
GLY 203
THR 204
0.0144
THR 204
PHE 205
-0.0002
PHE 205
ASP 206
0.0006
ASP 206
VAL 207
0.0004
VAL 207
SER 208
-0.0049
SER 208
ILE 209
-0.0003
ILE 209
LEU 210
-0.0046
LEU 210
THR 211
-0.0002
THR 211
ILE 212
0.0105
ILE 212
ASP 213
-0.0001
ASP 213
ASP 214
-0.0020
ASP 214
GLY 215
0.0001
GLY 215
ILE 216
0.0003
ILE 216
PHE 217
-0.0003
PHE 217
GLU 218
-0.0033
GLU 218
VAL 219
0.0002
VAL 219
LYS 220
-0.0159
LYS 220
ALA 221
0.0003
ALA 221
THR 222
0.0194
THR 222
ALA 223
0.0001
ALA 223
GLY 224
0.0312
GLY 224
ASP 225
0.0002
ASP 225
THR 226
-0.0240
THR 226
HIS 227
-0.0003
HIS 227
LEU 228
0.0294
LEU 228
GLY 229
-0.0003
GLY 229
GLY 230
0.0190
GLY 230
GLU 231
0.0001
GLU 231
ASP 232
-0.0012
ASP 232
PHE 233
-0.0001
PHE 233
ASP 234
-0.0289
ASP 234
ASN 235
0.0004
ASN 235
ARG 236
0.0070
ARG 236
LEU 237
-0.0001
LEU 237
VAL 238
-0.0666
VAL 238
ASN 239
-0.0001
ASN 239
HIS 240
0.0534
HIS 240
PHE 241
0.0001
PHE 241
VAL 242
-0.0729
VAL 242
GLU 243
-0.0002
GLU 243
GLU 244
0.0278
GLU 244
PHE 245
0.0000
PHE 245
LYS 246
0.0035
LYS 246
ARG 247
-0.0002
ARG 247
LYS 248
0.0179
LYS 248
HIS 249
-0.0003
HIS 249
LYS 250
0.0114
LYS 250
LYS 251
0.0000
LYS 251
ASP 252
0.0428
ASP 252
ILE 253
-0.0000
ILE 253
SER 254
-0.0061
SER 254
GLN 255
-0.0005
GLN 255
ASN 256
0.0239
ASN 256
LYS 257
0.0001
LYS 257
ARG 258
-0.0094
ARG 258
ALA 259
-0.0000
ALA 259
VAL 260
-0.0279
VAL 260
ARG 261
-0.0001
ARG 261
ARG 262
0.0368
ARG 262
LEU 263
-0.0001
LEU 263
ARG 264
0.0356
ARG 264
THR 265
0.0001
THR 265
ALA 266
0.0320
ALA 266
CYS 267
-0.0002
CYS 267
GLU 268
0.0328
GLU 268
ARG 269
0.0002
ARG 269
ALA 270
0.0434
ALA 270
LYS 271
0.0003
LYS 271
ARG 272
-0.0056
ARG 272
THR 273
0.0001
THR 273
LEU 274
0.0287
LEU 274
SER 275
-0.0003
SER 275
SER 276
0.0198
SER 276
SER 277
0.0000
SER 277
THR 278
-0.0046
THR 278
GLN 279
-0.0001
GLN 279
ALA 280
0.0273
ALA 280
SER 281
-0.0000
SER 281
LEU 282
-0.0150
LEU 282
GLU 283
0.0000
GLU 283
ILE 284
0.0005
ILE 284
ASP 285
-0.0001
ASP 285
SER 286
-0.0033
SER 286
LEU 287
0.0000
LEU 287
PHE 288
0.0041
PHE 288
GLU 289
0.0002
GLU 289
GLY 290
-0.0145
GLY 290
ILE 291
0.0000
ILE 291
ASP 292
-0.0243
ASP 292
PHE 293
0.0002
PHE 293
TYR 294
-0.0082
TYR 294
THR 295
0.0002
THR 295
SER 296
-0.0570
SER 296
ILE 297
0.0002
ILE 297
THR 298
-0.0789
THR 298
ARG 299
-0.0003
ARG 299
ALA 300
0.0029
ALA 300
ARG 301
-0.0001
ARG 301
PHE 302
0.0179
PHE 302
GLU 303
-0.0000
GLU 303
GLU 304
-0.0342
GLU 304
LEU 305
0.0000
LEU 305
CYS 306
-0.0410
CYS 306
SER 307
-0.0003
SER 307
ASP 308
0.0083
ASP 308
LEU 309
-0.0003
LEU 309
PHE 310
-0.0212
PHE 310
ARG 311
0.0002
ARG 311
SER 312
0.0166
SER 312
THR 313
-0.0000
THR 313
LEU 314
-0.0082
LEU 314
GLU 315
-0.0003
GLU 315
PRO 316
-0.0019
PRO 316
VAL 317
0.0001
VAL 317
GLU 318
0.0002
GLU 318
LYS 319
0.0003
LYS 319
ALA 320
-0.0005
ALA 320
LEU 321
-0.0001
LEU 321
ARG 322
-0.0010
ARG 322
ASP 323
0.0000
ASP 323
ALA 324
0.0045
ALA 324
LYS 325
-0.0003
LYS 325
LEU 326
0.0019
LEU 326
ASP 327
0.0001
ASP 327
LYS 328
-0.0100
LYS 328
ALA 329
-0.0000
ALA 329
GLN 330
-0.0139
GLN 330
ILE 331
0.0000
ILE 331
HIS 332
0.0004
HIS 332
ASP 333
-0.0001
ASP 333
LEU 334
-0.0465
LEU 334
VAL 335
0.0003
VAL 335
LEU 336
-0.0570
LEU 336
VAL 337
-0.0000
VAL 337
GLY 338
-0.0154
GLY 338
GLY 339
-0.0002
GLY 339
SER 340
-0.0172
SER 340
THR 341
-0.0003
THR 341
ARG 342
-0.0137
ARG 342
ILE 343
0.0000
ILE 343
PRO 344
0.0229
PRO 344
LYS 345
-0.0000
LYS 345
VAL 346
-0.0175
VAL 346
GLN 347
-0.0001
GLN 347
LYS 348
0.0403
LYS 348
LEU 349
-0.0003
LEU 349
LEU 350
-0.0409
LEU 350
GLN 351
-0.0002
GLN 351
ASP 352
0.0156
ASP 352
PHE 353
-0.0001
PHE 353
PHE 354
-0.0095
PHE 354
ASN 355
0.0005
ASN 355
GLY 356
0.0043
GLY 356
ARG 357
0.0000
ARG 357
ASP 358
0.0445
ASP 358
LEU 359
-0.0000
LEU 359
ASN 360
-0.0148
ASN 360
LYS 361
0.0003
LYS 361
SER 362
-0.0222
SER 362
ILE 363
0.0003
ILE 363
ASN 364
-0.0514
ASN 364
PRO 365
0.0001
PRO 365
ASP 366
0.0309
ASP 366
GLU 367
0.0001
GLU 367
ALA 368
0.0116
ALA 368
VAL 369
0.0000
VAL 369
ALA 370
0.0094
ALA 370
TYR 371
-0.0001
TYR 371
GLY 372
-0.0115
GLY 372
ALA 373
0.0003
ALA 373
ALA 374
0.0043
ALA 374
VAL 375
0.0002
VAL 375
GLN 376
0.0942
GLN 376
ALA 377
-0.0002
ALA 377
ALA 378
-0.0962
ALA 378
ILE 379
0.0000
ILE 379
LEU 380
-0.0382
LEU 380
ILE 381
-0.0003
ILE 381
LYS 382
0.5223
LYS 382
SER 383
-0.0001
SER 383
THR 384
0.0708
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.