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
-0.0185
VAL 5
LEU 6
-0.0002
LEU 6
LEU 7
0.0738
LEU 7
GLU 8
0.0001
GLU 8
VAL 9
-0.0170
VAL 9
PRO 10
-0.0000
PRO 10
PHE 11
-0.0227
PHE 11
SER 12
0.0002
SER 12
ALA 13
-0.0106
ALA 13
ARG 14
-0.0002
ARG 14
GLY 15
0.0003
GLY 15
ASP 16
0.0001
ASP 16
ARG 17
0.0549
ARG 17
ILE 18
-0.0003
ILE 18
PRO 19
0.0443
PRO 19
ASP 20
-0.0002
ASP 20
ALA 21
0.0304
ALA 21
VAL 22
-0.0001
VAL 22
ALA 23
-0.0156
ALA 23
GLU 24
-0.0002
GLU 24
LEU 25
-0.0068
LEU 25
ARG 26
0.0001
ARG 26
THR 27
0.0086
THR 27
ARG 28
-0.0000
ARG 28
GLU 29
0.0074
GLU 29
PRO 30
-0.0003
PRO 30
ILE 31
-0.0091
ILE 31
ARG 32
-0.0003
ARG 32
LYS 33
-0.0345
LYS 33
VAL 34
-0.0003
VAL 34
ARG 35
-0.0279
ARG 35
THR 36
0.0002
THR 36
ILE 37
-0.0280
ILE 37
THR 38
-0.0001
THR 38
GLY 39
-0.0489
GLY 39
ALA 40
0.0002
ALA 40
GLU 41
-0.0001
GLU 41
ALA 42
0.0004
ALA 42
TRP 43
-0.0236
TRP 43
LEU 44
-0.0001
LEU 44
VAL 45
-0.0163
VAL 45
SER 46
-0.0004
SER 46
SER 47
-0.0108
SER 47
TYR 48
0.0001
TYR 48
ALA 49
-0.0428
ALA 49
LEU 50
-0.0001
LEU 50
CYS 51
-0.0015
CYS 51
THR 52
0.0004
THR 52
GLN 53
-0.0836
GLN 53
VAL 54
-0.0002
VAL 54
LEU 55
0.0034
LEU 55
GLU 56
-0.0003
GLU 56
ASP 57
-0.0842
ASP 57
ARG 58
-0.0003
ARG 58
ARG 59
-0.0642
ARG 59
PHE 60
0.0002
PHE 60
SER 61
0.1007
SER 61
MET 62
0.0003
MET 62
LYS 63
0.0398
LYS 63
GLU 64
-0.0001
GLU 64
THR 65
-0.0141
THR 65
ALA 66
0.0003
ALA 66
ALA 67
0.0003
ALA 67
ALA 68
0.0000
ALA 68
GLY 69
-0.0246
GLY 69
ALA 70
-0.0001
ALA 70
PRO 71
-0.0183
PRO 71
ARG 72
0.0001
ARG 72
LEU 73
0.0342
LEU 73
ASN 74
-0.0001
ASN 74
ALA 75
-0.0655
ALA 75
LEU 76
0.0003
LEU 76
THR 77
0.0426
THR 77
VAL 78
-0.0002
VAL 78
PRO 79
-0.0130
PRO 79
PRO 80
0.0002
PRO 80
GLU 81
-0.0853
GLU 81
VAL 82
0.0000
VAL 82
VAL 83
0.0471
VAL 83
ASN 84
-0.0001
ASN 84
ASN 85
-0.0491
ASN 85
MET 86
-0.0000
MET 86
GLY 87
0.0016
GLY 87
ASN 88
-0.0001
ASN 88
ILE 89
-0.0873
ILE 89
ALA 90
0.0002
ALA 90
ASP 91
0.0314
ASP 91
ALA 92
-0.0001
ALA 92
GLY 93
0.0279
GLY 93
LEU 94
-0.0001
LEU 94
ARG 95
0.1457
ARG 95
LYS 96
-0.0000
LYS 96
ALA 97
-0.0065
ALA 97
VAL 98
0.0000
VAL 98
MET 99
0.0742
MET 99
LYS 100
-0.0002
LYS 100
ALA 101
-0.0680
ALA 101
ILE 102
-0.0004
ILE 102
THR 103
0.0572
THR 103
PRO 104
-0.0004
PRO 104
LYS 105
0.0016
LYS 105
ALA 106
-0.0000
ALA 106
PRO 107
-0.0470
PRO 107
GLY 108
0.0002
GLY 108
LEU 109
0.0019
LEU 109
GLU 110
-0.0003
GLU 110
GLN 111
-0.0345
GLN 111
PHE 112
-0.0001
PHE 112
LEU 113
-0.0020
LEU 113
ARG 114
0.0001
ARG 114
ASP 115
0.0010
ASP 115
THR 116
-0.0001
THR 116
ALA 117
-0.0385
ALA 117
ASN 118
0.0001
ASN 118
SER 119
0.0206
SER 119
LEU 120
0.0001
LEU 120
LEU 121
-0.0384
LEU 121
ASP 122
0.0001
ASP 122
ASN 123
0.0191
ASN 123
LEU 124
0.0000
LEU 124
ILE 125
0.0056
ILE 125
THR 126
0.0000
THR 126
GLU 127
0.0121
GLU 127
GLY 128
0.0004
GLY 128
ALA 129
0.0237
ALA 129
PRO 130
-0.0003
PRO 130
ALA 131
-0.0347
ALA 131
ASP 132
-0.0002
ASP 132
LEU 133
-0.0010
LEU 133
ARG 134
0.0005
ARG 134
ASN 135
0.0090
ASN 135
ASP 136
-0.0001
ASP 136
PHE 137
0.0274
PHE 137
ALA 138
0.0000
ALA 138
ASP 139
-0.0529
ASP 139
PRO 140
0.0001
PRO 140
LEU 141
-0.0069
LEU 141
ALA 142
-0.0003
ALA 142
THR 143
-0.0057
THR 143
ALA 144
-0.0001
ALA 144
LEU 145
-0.0017
LEU 145
HIS 146
0.0000
HIS 146
CYS 147
0.0608
CYS 147
LYS 148
-0.0001
LYS 148
VAL 149
-0.0636
VAL 149
LEU 150
0.0003
LEU 150
GLY 151
0.0249
GLY 151
ILE 152
0.0003
ILE 152
PRO 153
-0.0041
PRO 153
GLN 154
0.0000
GLN 154
GLU 155
0.0336
GLU 155
ASP 156
-0.0001
ASP 156
GLY 157
-0.0472
GLY 157
PRO 158
-0.0002
PRO 158
LYS 159
0.0165
LYS 159
LEU 160
0.0002
LEU 160
PHE 161
-0.1470
PHE 161
ARG 162
-0.0005
ARG 162
SER 163
0.0353
SER 163
LEU 164
0.0000
LEU 164
SER 165
-0.0695
SER 165
ILE 166
-0.0002
ILE 166
ALA 167
0.0166
ALA 167
PHE 168
0.0001
PHE 168
MET 169
-0.0115
MET 169
SER 170
0.0001
SER 170
SER 171
0.0157
SER 171
ALA 172
0.0001
ALA 172
ASP 173
-0.0344
ASP 173
PRO 174
-0.0001
PRO 174
ILE 175
0.0278
ILE 175
PRO 176
-0.0003
PRO 176
ALA 177
0.0140
ALA 177
ALA 178
-0.0000
ALA 178
LYS 179
-0.0273
LYS 179
ILE 180
-0.0003
ILE 180
ASN 181
0.0151
ASN 181
TRP 182
-0.0000
TRP 182
ASP 183
-0.0237
ASP 183
ARG 184
-0.0001
ARG 184
ASP 185
0.0058
ASP 185
ILE 186
-0.0002
ILE 186
GLU 187
0.0434
GLU 187
TYR 188
-0.0000
TYR 188
MET 189
-0.0218
MET 189
ALA 190
0.0003
ALA 190
GLY 191
0.0408
GLY 191
ILE 192
0.0001
ILE 192
LEU 193
-0.0521
LEU 193
GLU 194
-0.0002
GLU 194
ASN 195
0.0006
ASN 195
PRO 196
-0.0001
PRO 196
ASN 197
-0.0077
ASN 197
ILE 198
0.0001
ILE 198
THR 199
-0.0191
THR 199
THR 200
0.0004
THR 200
GLY 201
0.0456
GLY 201
LEU 202
0.0003
LEU 202
MET 203
0.0549
MET 203
GLY 204
0.0000
GLY 204
GLU 205
-0.0111
GLU 205
LEU 206
0.0001
LEU 206
SER 207
0.0458
SER 207
ARG 208
0.0002
ARG 208
LEU 209
-0.0119
LEU 209
ARG 210
0.0002
ARG 210
LYS 211
0.0133
LYS 211
ASP 212
0.0000
ASP 212
PRO 213
0.0005
PRO 213
ALA 214
0.0003
ALA 214
TYR 215
-0.0052
TYR 215
SER 216
0.0002
SER 216
HIS 217
-0.0108
HIS 217
VAL 218
-0.0002
VAL 218
SER 219
-0.0718
SER 219
ASP 220
-0.0001
ASP 220
GLU 221
-0.0258
GLU 221
LEU 222
0.0002
LEU 222
PHE 223
0.0196
PHE 223
ALA 224
0.0000
ALA 224
THR 225
0.0150
THR 225
ILE 226
-0.0001
ILE 226
GLY 227
0.0042
GLY 227
VAL 228
-0.0005
VAL 228
THR 229
0.0241
THR 229
PHE 230
-0.0001
PHE 230
PHE 231
-0.0075
PHE 231
GLY 232
0.0000
GLY 232
ALA 233
0.0366
ALA 233
GLY 234
0.0005
GLY 234
VAL 235
-0.0018
VAL 235
ILE 236
-0.0002
ILE 236
SER 237
-0.0021
SER 237
THR 238
0.0002
THR 238
GLY 239
-0.0066
GLY 239
SER 240
0.0002
SER 240
PHE 241
-0.0178
PHE 241
LEU 242
0.0001
LEU 242
THR 243
0.0234
THR 243
THR 244
0.0003
THR 244
ALA 245
-0.0084
ALA 245
LEU 246
0.0001
LEU 246
ILE 247
0.0242
ILE 247
SER 248
-0.0001
SER 248
LEU 249
0.0039
LEU 249
ILE 250
-0.0001
ILE 250
GLN 251
0.0104
GLN 251
ARG 252
-0.0002
ARG 252
PRO 253
0.0118
PRO 253
GLN 254
-0.0000
GLN 254
LEU 255
0.0169
LEU 255
ARG 256
-0.0000
ARG 256
ASN 257
-0.0064
ASN 257
LEU 258
0.0001
LEU 258
LEU 259
0.0172
LEU 259
HIS 260
0.0000
HIS 260
GLU 261
0.0002
GLU 261
LYS 262
0.0002
LYS 262
PRO 263
0.0247
PRO 263
GLU 264
0.0000
GLU 264
LEU 265
-0.0198
LEU 265
ILE 266
-0.0001
ILE 266
PRO 267
-0.0178
PRO 267
ALA 268
-0.0001
ALA 268
GLY 269
-0.0077
GLY 269
VAL 270
0.0005
VAL 270
GLU 271
-0.0495
GLU 271
GLU 272
-0.0003
GLU 272
LEU 273
-0.0242
LEU 273
LEU 274
0.0001
LEU 274
ARG 275
0.0161
ARG 275
ILE 276
-0.0002
ILE 276
ASN 277
-0.0429
ASN 277
LEU 278
-0.0003
LEU 278
SER 279
-0.0321
SER 279
PHE 280
-0.0003
PHE 280
ALA 281
0.0068
ALA 281
ASP 282
-0.0004
ASP 282
GLY 283
0.0001
GLY 283
LEU 284
-0.0002
LEU 284
PRO 285
-0.0160
PRO 285
ARG 286
0.0001
ARG 286
LEU 287
-0.0170
LEU 287
ALA 288
0.0001
ALA 288
THR 289
0.0001
THR 289
ALA 290
0.0003
ALA 290
ASP 291
0.0222
ASP 291
ILE 292
-0.0001
ILE 292
GLN 293
0.0239
GLN 293
VAL 294
0.0001
VAL 294
GLY 295
0.0204
GLY 295
ASP 296
0.0003
ASP 296
VAL 297
-0.0065
VAL 297
LEU 298
-0.0002
LEU 298
VAL 299
-0.0015
VAL 299
ARG 300
0.0002
ARG 300
LYS 301
-0.0087
LYS 301
GLY 302
0.0002
GLY 302
GLU 303
0.0269
GLU 303
LEU 304
0.0001
LEU 304
VAL 305
-0.0120
VAL 305
LEU 306
0.0003
LEU 306
VAL 307
-0.0266
VAL 307
LEU 308
-0.0003
LEU 308
LEU 309
-0.0048
LEU 309
GLU 310
0.0002
GLU 310
GLY 311
-0.0015
GLY 311
ALA 312
0.0001
ALA 312
ASN 313
-0.0269
ASN 313
PHE 314
-0.0004
PHE 314
ASP 315
-0.0128
ASP 315
PRO 316
-0.0002
PRO 316
GLU 317
0.0090
GLU 317
HIS 318
-0.0005
HIS 318
PHE 319
-0.0066
PHE 319
PRO 320
-0.0001
PRO 320
ASN 321
0.0122
ASN 321
PRO 322
0.0000
PRO 322
GLY 323
-0.0013
GLY 323
SER 324
-0.0001
SER 324
ILE 325
0.0163
ILE 325
GLU 326
-0.0002
GLU 326
LEU 327
0.0083
LEU 327
ASP 328
0.0002
ASP 328
ARG 329
-0.0416
ARG 329
PRO 330
-0.0000
PRO 330
ASN 331
-0.0022
ASN 331
PRO 332
-0.0000
PRO 332
THR 333
0.0401
THR 333
SER 334
0.0002
SER 334
HIS 335
-0.0131
HIS 335
LEU 336
0.0004
LEU 336
ALA 337
-0.0262
ALA 337
PHE 338
-0.0001
PHE 338
GLY 339
-0.1450
GLY 339
ARG 340
0.0001
ARG 340
GLY 341
0.0731
GLY 341
GLN 342
-0.0004
GLN 342
HIS 343
-0.0877
HIS 343
PHE 344
0.0002
PHE 344
CYS 345
-0.0545
CYS 345
PRO 346
-0.0001
PRO 346
GLY 347
-0.0494
GLY 347
SER 348
-0.0000
SER 348
ALA 349
-0.0921
ALA 349
LEU 350
0.0002
LEU 350
GLY 351
0.0505
GLY 351
ARG 352
0.0001
ARG 352
ARG 353
-0.0893
ARG 353
HIS 354
0.0002
HIS 354
ALA 355
0.0370
ALA 355
GLN 356
-0.0000
GLN 356
ILE 357
-0.0290
ILE 357
GLY 358
-0.0002
GLY 358
ILE 359
-0.0090
ILE 359
GLU 360
0.0002
GLU 360
ALA 361
-0.0172
ALA 361
LEU 362
0.0001
LEU 362
LEU 363
-0.0124
LEU 363
LYS 364
-0.0002
LYS 364
LYS 365
-0.0035
LYS 365
MET 366
0.0002
MET 366
PRO 367
-0.0252
PRO 367
GLY 368
0.0000
GLY 368
VAL 369
0.0071
VAL 369
ASP 370
0.0001
ASP 370
LEU 371
0.0136
LEU 371
ALA 372
-0.0001
ALA 372
VAL 373
0.0319
VAL 373
PRO 374
0.0000
PRO 374
ILE 375
0.0244
ILE 375
ASP 376
0.0002
ASP 376
GLN 377
0.0048
GLN 377
LEU 378
0.0002
LEU 378
VAL 379
0.0095
VAL 379
TRP 380
-0.0001
TRP 380
ARG 381
-0.0863
ARG 381
THR 382
-0.0003
THR 382
ARG 383
0.0790
ARG 383
PHE 384
-0.0004
PHE 384
GLN 385
-0.0259
GLN 385
ARG 386
0.0002
ARG 386
ARG 387
-0.0113
ARG 387
ILE 388
0.0005
ILE 388
PRO 389
0.0237
PRO 389
GLU 390
0.0001
GLU 390
ARG 391
0.0369
ARG 391
LEU 392
-0.0000
LEU 392
PRO 393
0.0101
PRO 393
VAL 394
-0.0000
VAL 394
LEU 395
0.0076
LEU 395
TRP 396
-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.