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
LYS 1
ILE 2
-0.0002
ILE 2
GLU 3
-0.1202
GLU 3
VAL 4
0.0002
VAL 4
VAL 5
-0.0876
VAL 5
CYS 6
-0.0003
CYS 6
ASP 7
0.0707
ASP 7
SER 8
-0.0003
SER 8
LEU 9
-0.0207
LEU 9
GLY 10
-0.0000
GLY 10
SER 11
0.0428
SER 11
ARG 12
-0.0000
ARG 12
LEU 13
-0.0697
LEU 13
THR 14
-0.0000
THR 14
ILE 15
-0.0590
ILE 15
ASP 16
-0.0001
ASP 16
GLY 17
-0.0691
GLY 17
LYS 18
0.0000
LYS 18
PRO 19
0.0589
PRO 19
PHE 20
-0.0002
PHE 20
PHE 21
0.0652
PHE 21
LEU 22
0.0002
LEU 22
LYS 23
-0.0469
LYS 23
GLY 24
-0.0001
GLY 24
MET 25
-0.0098
MET 25
ASN 26
0.0002
ASN 26
TRP 27
0.0028
TRP 27
ASP 28
0.0003
ASP 28
TYR 29
-0.0381
TYR 29
TYR 30
0.0002
TYR 30
PRO 31
-0.0613
PRO 31
ILE 32
-0.0001
ILE 32
GLY 33
0.0539
GLY 33
THR 34
0.0000
THR 34
ASN 35
-0.0303
ASN 35
TYR 36
0.0002
TYR 36
THR 37
-0.0724
THR 37
TYR 38
-0.0004
TYR 38
SER 39
0.0280
SER 39
LEU 40
0.0001
LEU 40
TRP 41
0.0222
TRP 41
GLU 42
0.0003
GLU 42
LYS 43
-0.0316
LYS 43
PRO 44
-0.0000
PRO 44
ASP 45
-0.0250
ASP 45
ASP 46
-0.0000
ASP 46
ILE 47
-0.0687
ILE 47
ILE 48
-0.0001
ILE 48
LYS 49
0.0138
LYS 49
ALA 50
-0.0000
ALA 50
ALA 51
-0.1050
ALA 51
LEU 52
-0.0002
LEU 52
ASN 53
-0.0481
ASN 53
SER 54
0.0000
SER 54
GLU 55
-0.0557
GLU 55
MET 56
-0.0002
MET 56
THR 57
-0.0554
THR 57
LEU 58
-0.0001
LEU 58
LEU 59
-0.0586
LEU 59
LYS 60
-0.0001
LYS 60
LYS 61
0.0822
LYS 61
MET 62
-0.0003
MET 62
GLY 63
-0.1187
GLY 63
VAL 64
0.0005
VAL 64
ASN 65
-0.0602
ASN 65
VAL 66
-0.0004
VAL 66
ILE 67
-0.0401
ILE 67
ARG 68
-0.0000
ARG 68
GLN 69
-0.0040
GLN 69
TYR 70
0.0000
TYR 70
ASN 71
0.0553
ASN 71
THR 72
-0.0003
THR 72
ILE 73
-0.0210
ILE 73
PRO 74
0.0000
PRO 74
PRO 75
0.0069
PRO 75
ARG 76
0.0000
ARG 76
TRP 77
-0.0003
TRP 77
ILE 78
-0.0002
ILE 78
GLN 79
-0.0155
GLN 79
TYR 80
-0.0002
TYR 80
ILE 81
0.0423
ILE 81
TYR 82
-0.0006
TYR 82
GLU 83
-0.0184
GLU 83
THR 84
-0.0001
THR 84
TYR 85
0.0442
TYR 85
GLY 86
0.0001
GLY 86
ILE 87
-0.0206
ILE 87
TYR 88
-0.0002
TYR 88
THR 89
-0.0348
THR 89
MET 90
-0.0000
MET 90
ILE 91
0.0008
ILE 91
ASN 92
0.0001
ASN 92
HIS 93
-0.0313
HIS 93
SER 94
0.0003
SER 94
PHE 95
-0.0828
PHE 95
GLY 96
0.0001
GLY 96
ARG 97
0.0479
ARG 97
TYR 98
-0.0003
TYR 98
GLY 99
-0.1387
GLY 99
MET 100
-0.0001
MET 100
THR 101
-0.0821
THR 101
ILE 102
-0.0001
ILE 102
HIS 103
-0.0181
HIS 103
GLY 104
0.0001
GLY 104
THR 105
0.0640
THR 105
TRP 106
-0.0001
TRP 106
TYR 107
0.0653
TYR 107
GLY 108
-0.0002
GLY 108
ASN 109
0.0991
ASN 109
THR 110
0.0003
THR 110
ASP 111
-0.0037
ASP 111
TYR 112
0.0002
TYR 112
CYS 113
-0.0218
CYS 113
LYS 114
-0.0002
LYS 114
GLU 115
-0.0278
GLU 115
ASP 116
-0.0000
ASP 116
VAL 117
-0.0404
VAL 117
LYS 118
-0.0004
LYS 118
GLU 119
-0.0297
GLU 119
GLN 120
0.0000
GLN 120
LEU 121
-0.0554
LEU 121
LEU 122
-0.0003
LEU 122
GLN 123
-0.0373
GLN 123
GLU 124
-0.0001
GLU 124
VAL 125
-0.0549
VAL 125
ASP 126
-0.0003
ASP 126
ASN 127
-0.0262
ASN 127
PHE 128
-0.0002
PHE 128
VAL 129
-0.0197
VAL 129
LYS 130
0.0000
LYS 130
THR 131
0.0068
THR 131
TYR 132
0.0001
TYR 132
GLN 133
-0.0360
GLN 133
GLY 134
0.0002
GLY 134
THR 135
0.0092
THR 135
PRO 136
0.0004
PRO 136
GLY 137
0.0390
GLY 137
VAL 138
0.0002
VAL 138
LEU 139
-0.0290
LEU 139
MET 140
-0.0001
MET 140
TYR 141
0.0159
TYR 141
LEU 142
-0.0003
LEU 142
LEU 143
0.0235
LEU 143
GLY 144
0.0001
GLY 144
ASN 145
0.0613
ASN 145
GLU 146
0.0000
GLU 146
ASN 147
-0.1153
ASN 147
ASN 148
-0.0002
ASN 148
TYR 149
0.0516
TYR 149
GLY 150
-0.0004
GLY 150
LEU 151
0.0241
LEU 151
PHE 152
0.0003
PHE 152
TRP 153
0.0100
TRP 153
SER 154
0.0001
SER 154
GLY 155
0.0390
GLY 155
ALA 156
-0.0000
ALA 156
GLU 157
0.0153
GLU 157
SER 158
0.0001
SER 158
GLU 159
-0.0607
GLU 159
ASP 160
0.0002
ASP 160
LEU 161
0.1239
LEU 161
PRO 162
0.0003
PRO 162
ILE 163
-0.2136
ILE 163
GLY 164
-0.0000
GLY 164
GLU 165
0.3102
GLU 165
ASN 166
-0.0001
ASN 166
ILE 167
0.0883
ILE 167
HIS 168
0.0002
HIS 168
ASP 169
-0.0091
ASP 169
ARG 170
0.0001
ARG 170
ARG 171
-0.0085
ARG 171
ALA 172
0.0001
ALA 172
ARG 173
0.0130
ARG 173
CYS 174
0.0001
CYS 174
LEU 175
-0.0389
LEU 175
TYR 176
0.0000
TYR 176
GLU 177
-0.0187
GLU 177
LEU 178
-0.0002
LEU 178
LEU 179
0.0087
LEU 179
ASN 180
0.0002
ASN 180
GLU 181
-0.0823
GLU 181
ALA 182
-0.0000
ALA 182
THR 183
-0.0253
THR 183
LEU 184
0.0002
LEU 184
ARG 185
-0.0996
ARG 185
ILE 186
-0.0001
ILE 186
LYS 187
-0.0118
LYS 187
ALA 188
0.0001
ALA 188
VAL 189
-0.0465
VAL 189
ASP 190
-0.0001
ASP 190
THR 191
0.0030
THR 191
SER 192
-0.0002
SER 192
ILE 193
0.0038
ILE 193
PRO 194
0.0000
PRO 194
VAL 195
0.1213
VAL 195
ALA 196
0.0002
ALA 196
ILE 197
0.0876
ILE 197
CYS 198
0.0000
CYS 198
ASN 199
-0.0021
ASN 199
GLY 200
-0.0002
GLY 200
ASP 201
-0.0039
ASP 201
LEU 202
0.0002
LEU 202
GLN 203
-0.1418
GLN 203
PHE 204
-0.0001
PHE 204
ILE 205
0.1379
ILE 205
ASP 206
0.0000
ASP 206
ILE 207
-0.1231
ILE 207
ILE 208
0.0002
ILE 208
ALA 209
0.0034
ALA 209
ASP 210
-0.0000
ASP 210
VAL 211
-0.0871
VAL 211
CYS 212
0.0004
CYS 212
LYS 213
0.0423
LYS 213
ASP 214
0.0004
ASP 214
ILE 215
0.0302
ILE 215
ASP 216
0.0000
ASP 216
VAL 217
0.0221
VAL 217
LEU 218
-0.0002
LEU 218
GLY 219
0.0547
GLY 219
VAL 220
-0.0000
VAL 220
ASN 221
0.1222
ASN 221
SER 222
0.0003
SER 222
TYR 223
0.1582
TYR 223
ARG 224
-0.0001
ARG 224
GLY 225
-0.1707
GLY 225
ASP 226
0.0000
ASP 226
SER 227
0.0862
SER 227
PHE 228
-0.0002
PHE 228
ASP 229
-0.0153
ASP 229
ILE 230
-0.0001
ILE 230
LEU 231
-0.0872
LEU 231
PHE 232
-0.0002
PHE 232
ASN 233
0.0249
ASN 233
ASP 234
-0.0001
ASP 234
VAL 235
-0.0106
VAL 235
LYS 236
0.0001
LYS 236
GLU 237
-0.0390
GLU 237
LYS 238
-0.0002
LYS 238
LEU 239
-0.0205
LEU 239
LYS 240
0.0004
LYS 240
LYS 241
-0.0358
LYS 241
PRO 242
-0.0001
PRO 242
VAL 243
0.1503
VAL 243
LEU 244
0.0004
LEU 244
LEU 245
0.1038
LEU 245
THR 246
0.0002
THR 246
GLU 247
0.0784
GLU 247
PHE 248
0.0004
PHE 248
GLY 249
0.0199
GLY 249
ALA 250
0.0001
ALA 250
ASP 251
0.1134
ASP 251
ALA 252
-0.0002
ALA 252
TYR 253
0.0079
TYR 253
ASN 254
0.0001
ASN 254
ALA 255
-0.0751
ALA 255
VAL 256
-0.0001
VAL 256
THR 257
-0.0137
THR 257
LEU 258
0.0001
LEU 258
GLN 259
-0.0879
GLN 259
GLU 260
0.0001
GLU 260
ALA 261
0.0586
ALA 261
GLN 262
-0.0002
GLN 262
GLN 263
0.0526
GLN 263
GLU 264
0.0005
GLU 264
GLN 265
-0.0188
GLN 265
ALA 266
0.0002
ALA 266
GLU 267
0.0939
GLU 267
ILE 268
0.0003
ILE 268
LEU 269
0.0439
LEU 269
LEU 270
-0.0001
LEU 270
ASN 271
-0.0296
ASN 271
ASN 272
0.0003
ASN 272
TRP 273
0.0633
TRP 273
GLN 274
0.0002
GLN 274
GLU 275
-0.2418
GLU 275
ILE 276
-0.0000
ILE 276
TYR 277
0.0158
TYR 277
LEU 278
0.0001
LEU 278
ASN 279
-0.1898
ASN 279
ALA 280
-0.0001
ALA 280
SER 281
0.0164
SER 281
GLY 282
0.0001
GLY 282
MET 283
-0.0129
MET 283
GLY 284
-0.0002
GLY 284
GLU 285
-0.0568
GLU 285
ASN 286
-0.0003
ASN 286
ASP 287
0.0425
ASP 287
ASN 288
-0.0001
ASN 288
CYS 289
0.0170
CYS 289
ILE 290
0.0004
ILE 290
GLY 291
0.0514
GLY 291
GLY 292
-0.0001
GLY 292
PHE 293
0.0423
PHE 293
THR 294
0.0002
THR 294
PHE 295
0.0639
PHE 295
GLN 296
0.0001
GLN 296
PHE 297
0.0343
PHE 297
SER 298
-0.0003
SER 298
ASP 299
-0.0970
ASP 299
GLY 300
-0.0002
GLY 300
TRP 301
0.0539
TRP 301
TRP 302
-0.0000
TRP 302
LYS 303
-0.1039
LYS 303
TYR 304
-0.0003
TYR 304
GLY 305
-0.0353
GLY 305
GLN 306
0.0002
GLN 306
THR 307
0.0047
THR 307
THR 308
0.0000
THR 308
HIS 309
0.0064
HIS 309
LEU 310
-0.0001
LEU 310
ASP 311
0.0093
ASP 311
ILE 312
-0.0001
ILE 312
HIS 313
0.0601
HIS 313
ASP 314
0.0001
ASP 314
ASN 315
-0.0760
ASN 315
HIS 316
-0.0002
HIS 316
ALA 317
-0.0277
ALA 317
SER 318
0.0001
SER 318
TRP 319
-0.1316
TRP 319
LYS 320
-0.0004
LYS 320
ASN 321
0.0644
ASN 321
GLY 322
-0.0002
GLY 322
GLY 323
0.0551
GLY 323
TYR 324
-0.0002
TYR 324
LYS 325
-0.0412
LYS 325
PHE 326
0.0001
PHE 326
ASP 327
-0.0609
ASP 327
TYR 328
0.0003
TYR 328
VAL 329
0.0562
VAL 329
PRO 330
-0.0004
PRO 330
ASN 331
-0.0172
ASN 331
GLU 332
0.0001
GLU 332
ASN 333
-0.1524
ASN 333
ASN 334
0.0001
ASN 334
MET 335
-0.0845
MET 335
ASN 336
0.0002
ASN 336
GLU 337
-0.0577
GLU 337
GLU 338
0.0001
GLU 338
TRP 339
0.0232
TRP 339
PHE 340
0.0000
PHE 340
GLY 341
-0.0419
GLY 341
ILE 342
-0.0002
ILE 342
CYS 343
0.0701
CYS 343
ALA 344
0.0001
ALA 344
LYS 345
0.1623
LYS 345
GLY 346
-0.0002
GLY 346
GLN 347
0.1296
GLN 347
PRO 348
0.0002
PRO 348
ASP 349
-0.1006
ASP 349
ASP 350
0.0001
ASP 350
LYS 351
-0.1500
LYS 351
GLY 352
-0.0001
GLY 352
LEU 353
0.0266
LEU 353
TYR 354
-0.0001
TYR 354
GLU 355
0.3477
GLU 355
LEU 356
-0.0001
LEU 356
ILE 357
0.1631
ILE 357
PRO 358
-0.0000
PRO 358
ARG 359
0.1740
ARG 359
LYS 360
-0.0001
LYS 360
ALA 361
-0.0657
ALA 361
TYR 362
-0.0000
TYR 362
GLU 363
0.1717
GLU 363
ALA 364
0.0002
ALA 364
LEU 365
0.0480
LEU 365
HIS 366
-0.0004
HIS 366
SER 367
0.3610
SER 367
ILE 368
-0.0001
ILE 368
HIS 369
0.0836
HIS 369
GLY 370
0.0002
GLY 370
ILE 371
-0.0063
ILE 371
ASP 372
0.0003
ASP 372
PRO 373
-0.0817
PRO 373
TYR 374
-0.0001
TYR 374
GLN 375
0.0512
GLN 375
SER 376
-0.0001
SER 376
THR 377
0.0045
THR 377
PRO 378
0.0001
PRO 378
THR 379
-0.1157
THR 379
ALA 380
-0.0001
ALA 380
ILE 381
0.0108
ILE 381
VAL 382
-0.0001
VAL 382
GLN 383
-0.0619
GLN 383
TYR 384
-0.0004
TYR 384
PHE 385
-0.0638
PHE 385
ASP 386
0.0002
ASP 386
ILE 387
-0.0455
ILE 387
VAL 388
0.0001
VAL 388
ARG 389
0.0476
ARG 389
ASP 390
-0.0001
ASP 390
GLN 391
0.0801
GLN 391
ILE 392
0.0001
ILE 392
LYS 393
0.1947
LYS 393
GLU 394
0.0001
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.