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
PRO 1
ILE 2
-0.0002
ILE 2
THR 3
-0.0001
THR 3
ILE 4
0.0134
ILE 4
ASN 5
-0.0001
ASN 5
ASN 6
-0.0002
ASN 6
PHE 7
0.0037
PHE 7
ARG 8
0.0003
ARG 8
TYR 9
-0.0003
TYR 9
SER 10
-0.0004
SER 10
ASP 11
-0.0001
ASP 11
PRO 12
-0.0001
PRO 12
VAL 13
0.0000
VAL 13
ASN 14
0.0001
ASN 14
ASN 15
-0.0002
ASN 15
ASP 16
-0.0712
ASP 16
THR 17
-0.0001
THR 17
ILE 18
0.0001
ILE 18
ILE 19
-0.0215
ILE 19
MET 20
0.0002
MET 20
MET 21
0.0004
MET 21
GLU 22
-0.0217
GLU 22
PRO 23
-0.0001
PRO 23
PRO 24
-0.0001
PRO 24
TYR 25
-0.0087
TYR 25
CYS 26
0.0003
CYS 26
LYS 27
-0.0001
LYS 27
GLY 28
-0.0110
GLY 28
LEU 29
0.0003
LEU 29
ASP 30
-0.0000
ASP 30
ILE 31
-0.0152
ILE 31
TYR 32
0.0001
TYR 32
TYR 33
-0.0003
TYR 33
LYS 34
-0.0690
LYS 34
ALA 35
0.0001
ALA 35
PHE 36
-0.0003
PHE 36
LYS 37
0.0168
LYS 37
ILE 38
-0.0002
ILE 38
THR 39
0.0002
THR 39
ASP 40
0.0945
ASP 40
ARG 41
0.0001
ARG 41
ILE 42
-0.0000
ILE 42
TRP 43
0.0193
TRP 43
ILE 44
-0.0003
ILE 44
VAL 45
0.0001
VAL 45
PRO 46
0.0253
PRO 46
GLU 47
0.0001
GLU 47
ARG 48
-0.0001
ARG 48
TYR 49
-0.0891
TYR 49
GLU 50
0.0001
GLU 50
PHE 51
-0.0000
PHE 51
GLY 52
-0.0739
GLY 52
THR 53
0.0001
THR 53
LYS 54
-0.0003
LYS 54
PRO 55
-0.0128
PRO 55
GLU 56
-0.0001
GLU 56
ASP 57
-0.0002
ASP 57
PHE 58
-0.0694
PHE 58
ASN 59
0.0003
ASN 59
PRO 60
-0.0002
PRO 60
PRO 61
0.0661
PRO 61
SER 62
0.0001
SER 62
SER 63
0.0005
SER 63
LEU 64
-0.0007
LEU 64
ILE 65
0.0002
ILE 65
GLU 66
0.0008
GLU 66
GLY 67
-0.1341
GLY 67
ALA 68
0.0001
ALA 68
SER 69
-0.0002
SER 69
GLU 70
0.0248
GLU 70
TYR 71
-0.0000
TYR 71
TYR 72
-0.0002
TYR 72
ASP 73
0.0445
ASP 73
PRO 74
-0.0002
PRO 74
ASN 75
0.0001
ASN 75
TYR 76
0.0274
TYR 76
LEU 77
-0.0001
LEU 77
ARG 78
-0.0000
ARG 78
THR 79
0.0062
THR 79
ASP 80
0.0004
ASP 80
SER 81
-0.0003
SER 81
ASP 82
0.0013
ASP 82
LYS 83
-0.0000
LYS 83
ASP 84
0.0002
ASP 84
ARG 85
-0.0125
ARG 85
PHE 86
-0.0000
PHE 86
LEU 87
-0.0001
LEU 87
GLN 88
-0.0146
GLN 88
THR 89
0.0000
THR 89
MET 90
0.0002
MET 90
VAL 91
0.0064
VAL 91
LYS 92
0.0003
LYS 92
LEU 93
-0.0003
LEU 93
PHE 94
0.0288
PHE 94
ASN 95
-0.0004
ASN 95
ARG 96
0.0002
ARG 96
ILE 97
0.0381
ILE 97
LYS 98
-0.0003
LYS 98
ASN 99
0.0001
ASN 99
ASN 100
-0.0325
ASN 100
VAL 101
0.0005
VAL 101
ALA 102
0.0000
ALA 102
GLY 103
-0.0062
GLY 103
GLU 104
0.0004
GLU 104
ALA 105
-0.0002
ALA 105
LEU 106
-0.0234
LEU 106
LEU 107
0.0000
LEU 107
ASP 108
0.0000
ASP 108
LYS 109
0.0728
LYS 109
ILE 110
-0.0001
ILE 110
ILE 111
-0.0001
ILE 111
ASN 112
0.0964
ASN 112
ALA 113
0.0000
ALA 113
ILE 114
0.0001
ILE 114
PRO 115
0.0335
PRO 115
TYR 116
-0.0000
TYR 116
LEU 117
-0.0001
LEU 117
GLY 118
0.0544
GLY 118
ASN 119
0.0001
ASN 119
SER 120
0.0002
SER 120
TYR 121
0.0222
TYR 121
SER 122
0.0001
SER 122
LEU 123
0.0001
LEU 123
LEU 124
-0.0001
LEU 124
ASP 125
0.0002
ASP 125
LYS 126
0.0003
LYS 126
PHE 127
0.0043
PHE 127
ASP 128
0.0000
ASP 128
THR 129
0.0000
THR 129
ASN 130
-0.0399
ASN 130
SER 131
0.0002
SER 131
ASN 132
0.0000
ASN 132
SER 133
-0.0165
SER 133
VAL 134
0.0002
VAL 134
SER 135
0.0001
SER 135
PHE 136
-0.0069
PHE 136
ASN 137
0.0000
ASN 137
LEU 138
0.0003
LEU 138
LEU 139
0.0240
LEU 139
GLU 140
0.0003
GLU 140
GLN 141
-0.0002
GLN 141
ASP 142
0.0204
ASP 142
PRO 143
-0.0002
PRO 143
SER 144
0.0001
SER 144
GLY 145
0.0126
GLY 145
ALA 146
0.0002
ALA 146
THR 147
-0.0002
THR 147
THR 148
0.0010
THR 148
LYS 149
-0.0002
LYS 149
SER 150
-0.0004
SER 150
ALA 151
-0.0117
ALA 151
MET 152
0.0000
MET 152
LEU 153
0.0001
LEU 153
THR 154
0.0098
THR 154
ASN 155
0.0002
ASN 155
LEU 156
0.0000
LEU 156
ILE 157
0.0092
ILE 157
ILE 158
-0.0000
ILE 158
PHE 159
0.0002
PHE 159
GLY 160
-0.0085
GLY 160
PRO 161
-0.0001
PRO 161
GLY 162
0.0002
GLY 162
PRO 163
-0.0994
PRO 163
VAL 164
-0.0004
VAL 164
LEU 165
-0.0003
LEU 165
ASN 166
0.0141
ASN 166
LYS 167
0.0002
LYS 167
ASN 168
0.0002
ASN 168
GLU 169
-0.1393
GLU 169
VAL 170
-0.0003
VAL 170
ARG 171
0.0002
ARG 171
GLY 172
-0.1597
GLY 172
ILE 173
0.0002
ILE 173
VAL 174
-0.0001
VAL 174
LEU 175
-0.0885
LEU 175
ARG 176
-0.0001
ARG 176
VAL 177
-0.0002
VAL 177
ASP 178
0.0070
ASP 178
ASN 179
0.0001
ASN 179
LYS 180
0.0000
LYS 180
ASN 181
-0.0329
ASN 181
TYR 182
0.0004
TYR 182
PHE 183
-0.0003
PHE 183
PRO 184
0.0135
PRO 184
CYS 185
0.0001
CYS 185
ARG 186
0.0003
ARG 186
ASP 187
-0.0578
ASP 187
GLY 188
-0.0003
GLY 188
PHE 189
-0.0005
PHE 189
GLY 190
-0.0407
GLY 190
SER 191
0.0003
SER 191
ILE 192
0.0000
ILE 192
MET 193
-0.0236
MET 193
GLN 194
0.0000
GLN 194
MET 195
0.0003
MET 195
ALA 196
-0.0935
ALA 196
PHE 197
0.0003
PHE 197
CYS 198
0.0001
CYS 198
PRO 199
-0.0276
PRO 199
GLU 200
0.0002
GLU 200
TYR 201
0.0004
TYR 201
VAL 202
-0.0019
VAL 202
PRO 203
0.0002
PRO 203
THR 204
-0.0003
THR 204
PHE 205
-0.0007
PHE 205
ASP 206
-0.0000
ASP 206
ASN 207
-0.0000
ASN 207
VAL 208
0.0518
VAL 208
ILE 209
-0.0000
ILE 209
GLU 210
-0.0002
GLU 210
ASN 211
-0.0510
ASN 211
ILE 212
-0.0001
ILE 212
THR 213
0.0000
THR 213
SER 214
-0.0080
SER 214
LEU 215
0.0004
LEU 215
THR 216
-0.0005
THR 216
ILE 217
0.0033
ILE 217
GLY 218
-0.0001
GLY 218
LYS 219
0.0000
LYS 219
SER 220
0.0996
SER 220
LYS 221
-0.0000
LYS 221
TYR 222
-0.0004
TYR 222
PHE 223
-0.0428
PHE 223
GLN 224
-0.0003
GLN 224
ASP 225
0.0001
ASP 225
PRO 226
-0.0173
PRO 226
ALA 227
0.0002
ALA 227
LEU 228
-0.0002
LEU 228
LEU 229
0.0044
LEU 229
LEU 230
0.0000
LEU 230
MET 231
0.0001
MET 231
HIS 232
-0.0126
HIS 232
GLU 233
0.0003
GLU 233
LEU 234
0.0004
LEU 234
ILE 235
-0.0039
ILE 235
HIS 236
0.0002
HIS 236
VAL 237
0.0001
VAL 237
LEU 238
-0.0078
LEU 238
HIS 239
-0.0000
HIS 239
GLY 240
0.0002
GLY 240
LEU 241
0.0178
LEU 241
TYR 242
0.0003
TYR 242
GLY 243
-0.0002
GLY 243
MET 244
0.0116
MET 244
GLN 245
-0.0004
GLN 245
VAL 246
0.0006
VAL 246
SER 247
-0.0135
SER 247
SER 248
0.0000
SER 248
HIS 249
-0.0001
HIS 249
GLU 250
0.0742
GLU 250
ILE 251
-0.0002
ILE 251
ILE 252
0.0003
ILE 252
PRO 253
0.0217
PRO 253
SER 254
0.0002
SER 254
LYS 255
-0.0001
LYS 255
GLN 256
0.0143
GLN 256
GLU 257
0.0004
GLU 257
ILE 258
0.0000
ILE 258
TYR 259
0.0456
TYR 259
MET 260
-0.0000
MET 260
GLN 261
0.0003
GLN 261
HIS 262
-0.1222
HIS 262
THR 263
0.0004
THR 263
TYR 264
0.0001
TYR 264
PRO 265
-0.0564
PRO 265
ILE 266
0.0000
ILE 266
SER 267
-0.0002
SER 267
ALA 268
-0.0193
ALA 268
GLU 269
0.0004
GLU 269
GLU 270
0.0001
GLU 270
LEU 271
0.0320
LEU 271
PHE 272
-0.0000
PHE 272
THR 273
0.0001
THR 273
PHE 274
0.0275
PHE 274
GLY 275
-0.0001
GLY 275
GLY 276
-0.0002
GLY 276
GLN 277
-0.0437
GLN 277
ASP 278
0.0002
ASP 278
ALA 279
0.0000
ALA 279
ASN 280
-0.0113
ASN 280
LEU 281
-0.0000
LEU 281
ILE 282
0.0001
ILE 282
SER 283
-0.0117
SER 283
ILE 284
-0.0001
ILE 284
ASP 285
-0.0000
ASP 285
ILE 286
0.0189
ILE 286
LYS 287
-0.0001
LYS 287
ASN 288
0.0001
ASN 288
ASP 289
0.0341
ASP 289
LEU 290
0.0001
LEU 290
TYR 291
-0.0004
TYR 291
GLU 292
-0.0054
GLU 292
LYS 293
-0.0000
LYS 293
THR 294
0.0000
THR 294
LEU 295
-0.0195
LEU 295
ASN 296
-0.0003
ASN 296
ASP 297
0.0001
ASP 297
TYR 298
-0.0088
TYR 298
LYS 299
0.0002
LYS 299
ALA 300
-0.0002
ALA 300
ILE 301
0.0034
ILE 301
ALA 302
-0.0001
ALA 302
ASN 303
-0.0003
ASN 303
LYS 304
-0.0047
LYS 304
LEU 305
0.0001
LEU 305
SER 306
-0.0001
SER 306
GLN 307
0.0059
GLN 307
VAL 308
0.0001
VAL 308
THR 309
0.0001
THR 309
SER 310
-0.0184
SER 310
CYS 311
0.0000
CYS 311
ASN 312
-0.0000
ASN 312
ASP 313
0.0002
ASP 313
PRO 314
-0.0003
PRO 314
ASN 315
0.0000
ASN 315
ILE 316
-0.0010
ILE 316
ASP 317
0.0004
ASP 317
ILE 318
-0.0001
ILE 318
ASP 319
-0.0319
ASP 319
SER 320
-0.0000
SER 320
TYR 321
-0.0002
TYR 321
LYS 322
-0.0060
LYS 322
GLN 323
-0.0001
GLN 323
ILE 324
0.0002
ILE 324
TYR 325
-0.0179
TYR 325
GLN 326
0.0001
GLN 326
GLN 327
-0.0001
GLN 327
LYS 328
0.0283
LYS 328
TYR 329
-0.0000
TYR 329
GLN 330
0.0001
GLN 330
PHE 331
0.0485
PHE 331
ASP 332
0.0004
ASP 332
LYS 333
-0.0002
LYS 333
ASP 334
0.0452
ASP 334
SER 335
0.0002
SER 335
ASN 336
-0.0002
ASN 336
GLY 337
0.0606
GLY 337
GLN 338
0.0001
GLN 338
TYR 339
-0.0001
TYR 339
ILE 340
-0.0103
ILE 340
VAL 341
-0.0000
VAL 341
ASN 342
-0.0001
ASN 342
GLU 343
-0.0149
GLU 343
ASP 344
-0.0001
ASP 344
LYS 345
0.0004
LYS 345
PHE 346
-0.0127
PHE 346
GLN 347
0.0001
GLN 347
ILE 348
-0.0003
ILE 348
LEU 349
-0.0080
LEU 349
TYR 350
-0.0001
TYR 350
ASN 351
-0.0001
ASN 351
SER 352
0.0107
SER 352
ILE 353
0.0002
ILE 353
MET 354
-0.0000
MET 354
TYR 355
0.0150
TYR 355
GLY 356
-0.0001
GLY 356
PHE 357
-0.0003
PHE 357
THR 358
0.0326
THR 358
GLU 359
-0.0003
GLU 359
VAL 360
-0.0002
VAL 360
GLU 361
-0.0169
GLU 361
LEU 362
0.0003
LEU 362
GLY 363
-0.0000
GLY 363
LYS 364
0.0092
LYS 364
LYS 365
0.0001
LYS 365
PHE 366
0.0001
PHE 366
ASN 367
0.0275
ASN 367
ILE 368
-0.0002
ILE 368
LYS 369
-0.0000
LYS 369
THR 370
-0.0480
THR 370
ARG 371
0.0002
ARG 371
LEU 372
0.0002
LEU 372
SER 373
0.0244
SER 373
TYR 374
-0.0004
TYR 374
PHE 375
0.0001
PHE 375
SER 376
-0.1134
SER 376
MET 377
0.0002
MET 377
ASN 378
-0.0001
ASN 378
HIS 379
0.0133
HIS 379
ASP 380
-0.0003
ASP 380
PRO 381
0.0001
PRO 381
VAL 382
0.0466
VAL 382
LYS 383
0.0002
LYS 383
ILE 384
-0.0002
ILE 384
PRO 385
-0.0213
PRO 385
ASN 386
-0.0002
ASN 386
LEU 387
0.0000
LEU 387
LEU 388
0.0064
LEU 388
ASP 389
-0.0001
ASP 389
ASP 390
-0.0002
ASP 390
THR 391
-0.0052
THR 391
ILE 392
-0.0000
ILE 392
TYR 393
0.0004
TYR 393
ASN 394
0.0416
ASN 394
ASP 395
-0.0000
ASP 395
THR 396
-0.0002
THR 396
GLU 397
0.0049
GLU 397
GLY 398
-0.0001
GLY 398
PHE 399
-0.0001
PHE 399
ASN 400
-0.0041
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.