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
0.0000
THR 4
VAL 5
-0.1231
VAL 5
LEU 6
0.0002
LEU 6
LEU 7
0.2020
LEU 7
GLU 8
0.0001
GLU 8
VAL 9
-0.0857
VAL 9
PRO 10
-0.0005
PRO 10
PHE 11
0.0489
PHE 11
SER 12
0.0002
SER 12
ALA 13
-0.0771
ALA 13
ARG 14
-0.0002
ARG 14
GLY 15
0.0123
GLY 15
ASP 16
0.0000
ASP 16
ARG 17
-0.0529
ARG 17
ILE 18
-0.0003
ILE 18
PRO 19
0.0005
PRO 19
ASP 20
-0.0000
ASP 20
ALA 21
0.0339
ALA 21
VAL 22
-0.0003
VAL 22
ALA 23
0.0210
ALA 23
GLU 24
-0.0000
GLU 24
LEU 25
0.0067
LEU 25
ARG 26
0.0000
ARG 26
THR 27
0.0155
THR 27
ARG 28
0.0003
ARG 28
GLU 29
-0.0076
GLU 29
PRO 30
0.0004
PRO 30
ILE 31
-0.0171
ILE 31
ARG 32
-0.0001
ARG 32
LYS 33
0.0044
LYS 33
VAL 34
-0.0000
VAL 34
ARG 35
0.0366
ARG 35
THR 36
0.0002
THR 36
ILE 37
-0.0602
ILE 37
THR 38
0.0000
THR 38
GLY 39
-0.0931
GLY 39
ALA 40
0.0003
ALA 40
GLU 41
-0.0054
GLU 41
ALA 42
0.0003
ALA 42
TRP 43
-0.0402
TRP 43
LEU 44
-0.0000
LEU 44
VAL 45
0.0171
VAL 45
SER 46
0.0001
SER 46
SER 47
0.0155
SER 47
TYR 48
0.0004
TYR 48
ALA 49
-0.0021
ALA 49
LEU 50
0.0001
LEU 50
CYS 51
0.0176
CYS 51
THR 52
-0.0001
THR 52
GLN 53
-0.0018
GLN 53
VAL 54
-0.0004
VAL 54
LEU 55
0.0474
LEU 55
GLU 56
0.0002
GLU 56
ASP 57
-0.0211
ASP 57
ARG 58
-0.0002
ARG 58
ARG 59
0.0430
ARG 59
PHE 60
-0.0000
PHE 60
SER 61
0.0002
SER 61
MET 62
-0.0004
MET 62
LYS 63
-0.0316
LYS 63
GLU 64
-0.0002
GLU 64
THR 65
0.0252
THR 65
ALA 66
-0.0001
ALA 66
ALA 67
0.0023
ALA 67
ALA 68
0.0001
ALA 68
GLY 69
-0.0112
GLY 69
ALA 70
0.0001
ALA 70
PRO 71
0.0088
PRO 71
ARG 72
-0.0001
ARG 72
LEU 73
0.0294
LEU 73
ASN 74
-0.0001
ASN 74
ALA 75
-0.0389
ALA 75
LEU 76
0.0000
LEU 76
THR 77
-0.0497
THR 77
VAL 78
-0.0005
VAL 78
PRO 79
0.0526
PRO 79
PRO 80
0.0002
PRO 80
GLU 81
0.0194
GLU 81
VAL 82
-0.0004
VAL 82
VAL 83
-0.0165
VAL 83
ASN 84
0.0002
ASN 84
ASN 85
0.0357
ASN 85
MET 86
0.0001
MET 86
GLY 87
0.0043
GLY 87
ASN 88
0.0000
ASN 88
ILE 89
0.0310
ILE 89
ALA 90
0.0001
ALA 90
ASP 91
-0.0296
ASP 91
ALA 92
-0.0001
ALA 92
GLY 93
-0.0231
GLY 93
LEU 94
0.0002
LEU 94
ARG 95
-0.0351
ARG 95
LYS 96
-0.0001
LYS 96
ALA 97
0.0633
ALA 97
VAL 98
0.0000
VAL 98
MET 99
-0.0386
MET 99
LYS 100
-0.0002
LYS 100
ALA 101
0.0485
ALA 101
ILE 102
0.0001
ILE 102
THR 103
-0.0453
THR 103
PRO 104
-0.0002
PRO 104
LYS 105
0.0246
LYS 105
ALA 106
-0.0003
ALA 106
PRO 107
-0.0045
PRO 107
GLY 108
-0.0004
GLY 108
LEU 109
0.0059
LEU 109
GLU 110
0.0002
GLU 110
GLN 111
0.0069
GLN 111
PHE 112
0.0002
PHE 112
LEU 113
0.0093
LEU 113
ARG 114
0.0002
ARG 114
ASP 115
0.0136
ASP 115
THR 116
0.0003
THR 116
ALA 117
0.0199
ALA 117
ASN 118
-0.0001
ASN 118
SER 119
-0.0041
SER 119
LEU 120
-0.0001
LEU 120
LEU 121
0.0307
LEU 121
ASP 122
-0.0001
ASP 122
ASN 123
-0.0110
ASN 123
LEU 124
-0.0001
LEU 124
ILE 125
0.0128
ILE 125
THR 126
-0.0000
THR 126
GLU 127
-0.0109
GLU 127
GLY 128
-0.0001
GLY 128
ALA 129
-0.0232
ALA 129
PRO 130
-0.0002
PRO 130
ALA 131
0.0336
ALA 131
ASP 132
0.0000
ASP 132
LEU 133
0.0022
LEU 133
ARG 134
0.0002
ARG 134
ASN 135
0.0023
ASN 135
ASP 136
-0.0001
ASP 136
PHE 137
-0.0174
PHE 137
ALA 138
0.0002
ALA 138
ASP 139
0.0564
ASP 139
PRO 140
-0.0001
PRO 140
LEU 141
0.0088
LEU 141
ALA 142
-0.0001
ALA 142
THR 143
0.0159
THR 143
ALA 144
0.0001
ALA 144
LEU 145
0.0241
LEU 145
HIS 146
0.0001
HIS 146
CYS 147
-0.0138
CYS 147
LYS 148
0.0001
LYS 148
VAL 149
0.0324
VAL 149
LEU 150
-0.0001
LEU 150
GLY 151
0.0057
GLY 151
ILE 152
-0.0002
ILE 152
PRO 153
-0.0036
PRO 153
GLN 154
0.0002
GLN 154
GLU 155
0.0106
GLU 155
ASP 156
-0.0002
ASP 156
GLY 157
0.0185
GLY 157
PRO 158
-0.0001
PRO 158
LYS 159
0.0167
LYS 159
LEU 160
-0.0001
LEU 160
PHE 161
0.0794
PHE 161
ARG 162
-0.0001
ARG 162
SER 163
0.0066
SER 163
LEU 164
-0.0004
LEU 164
SER 165
0.0324
SER 165
ILE 166
0.0003
ILE 166
ALA 167
0.0100
ALA 167
PHE 168
0.0003
PHE 168
MET 169
-0.0279
MET 169
SER 170
0.0000
SER 170
SER 171
0.0051
SER 171
ALA 172
-0.0000
ALA 172
ASP 173
-0.0351
ASP 173
PRO 174
0.0004
PRO 174
ILE 175
-0.0186
ILE 175
PRO 176
0.0003
PRO 176
ALA 177
-0.0215
ALA 177
ALA 178
0.0001
ALA 178
LYS 179
0.0197
LYS 179
ILE 180
0.0002
ILE 180
ASN 181
0.0201
ASN 181
TRP 182
-0.0001
TRP 182
ASP 183
-0.0010
ASP 183
ARG 184
-0.0001
ARG 184
ASP 185
-0.0016
ASP 185
ILE 186
-0.0001
ILE 186
GLU 187
-0.0135
GLU 187
TYR 188
-0.0001
TYR 188
MET 189
0.0160
MET 189
ALA 190
0.0001
ALA 190
GLY 191
-0.0100
GLY 191
ILE 192
-0.0005
ILE 192
LEU 193
0.0204
LEU 193
GLU 194
0.0004
GLU 194
ASN 195
0.0055
ASN 195
PRO 196
-0.0001
PRO 196
ASN 197
-0.0030
ASN 197
ILE 198
0.0001
ILE 198
THR 199
-0.0039
THR 199
THR 200
-0.0001
THR 200
GLY 201
0.0365
GLY 201
LEU 202
0.0000
LEU 202
MET 203
-0.0141
MET 203
GLY 204
0.0001
GLY 204
GLU 205
0.0167
GLU 205
LEU 206
-0.0001
LEU 206
SER 207
-0.0029
SER 207
ARG 208
-0.0003
ARG 208
LEU 209
0.0081
LEU 209
ARG 210
0.0002
ARG 210
LYS 211
0.0020
LYS 211
ASP 212
-0.0000
ASP 212
PRO 213
-0.0255
PRO 213
ALA 214
-0.0000
ALA 214
TYR 215
0.0161
TYR 215
SER 216
-0.0002
SER 216
HIS 217
0.0031
HIS 217
VAL 218
-0.0001
VAL 218
SER 219
0.0441
SER 219
ASP 220
0.0001
ASP 220
GLU 221
0.0104
GLU 221
LEU 222
-0.0003
LEU 222
PHE 223
0.0031
PHE 223
ALA 224
0.0000
ALA 224
THR 225
-0.0115
THR 225
ILE 226
0.0001
ILE 226
GLY 227
0.0061
GLY 227
VAL 228
0.0000
VAL 228
THR 229
-0.0042
THR 229
PHE 230
-0.0001
PHE 230
PHE 231
0.0423
PHE 231
GLY 232
0.0001
GLY 232
ALA 233
-0.0224
ALA 233
GLY 234
-0.0002
GLY 234
VAL 235
0.0160
VAL 235
ILE 236
0.0000
ILE 236
SER 237
0.0111
SER 237
THR 238
-0.0000
THR 238
GLY 239
0.0075
GLY 239
SER 240
0.0003
SER 240
PHE 241
0.0135
PHE 241
LEU 242
0.0002
LEU 242
THR 243
-0.0155
THR 243
THR 244
0.0001
THR 244
ALA 245
0.0214
ALA 245
LEU 246
-0.0002
LEU 246
ILE 247
-0.0127
ILE 247
SER 248
-0.0002
SER 248
LEU 249
0.0161
LEU 249
ILE 250
-0.0002
ILE 250
GLN 251
-0.0193
GLN 251
ARG 252
-0.0001
ARG 252
PRO 253
-0.0062
PRO 253
GLN 254
0.0004
GLN 254
LEU 255
-0.0332
LEU 255
ARG 256
-0.0001
ARG 256
ASN 257
0.0131
ASN 257
LEU 258
-0.0003
LEU 258
LEU 259
-0.0198
LEU 259
HIS 260
0.0002
HIS 260
GLU 261
0.0060
GLU 261
LYS 262
0.0001
LYS 262
PRO 263
-0.0303
PRO 263
GLU 264
-0.0002
GLU 264
LEU 265
0.0238
LEU 265
ILE 266
-0.0001
ILE 266
PRO 267
0.0057
PRO 267
ALA 268
0.0001
ALA 268
GLY 269
0.0050
GLY 269
VAL 270
0.0003
VAL 270
GLU 271
0.0515
GLU 271
GLU 272
0.0001
GLU 272
LEU 273
0.0081
LEU 273
LEU 274
0.0003
LEU 274
ARG 275
0.0355
ARG 275
ILE 276
-0.0000
ILE 276
ASN 277
0.0105
ASN 277
LEU 278
0.0000
LEU 278
SER 279
0.0079
SER 279
PHE 280
0.0000
PHE 280
ALA 281
0.0031
ALA 281
ASP 282
0.0004
ASP 282
GLY 283
-0.0066
GLY 283
LEU 284
-0.0003
LEU 284
PRO 285
-0.0083
PRO 285
ARG 286
-0.0001
ARG 286
LEU 287
0.0058
LEU 287
ALA 288
0.0003
ALA 288
THR 289
-0.0040
THR 289
ALA 290
-0.0000
ALA 290
ASP 291
0.0095
ASP 291
ILE 292
-0.0003
ILE 292
GLN 293
-0.0028
GLN 293
VAL 294
0.0002
VAL 294
GLY 295
-0.0028
GLY 295
ASP 296
-0.0001
ASP 296
VAL 297
-0.0047
VAL 297
LEU 298
0.0001
LEU 298
VAL 299
-0.0007
VAL 299
ARG 300
-0.0004
ARG 300
LYS 301
0.0030
LYS 301
GLY 302
-0.0000
GLY 302
GLU 303
0.0012
GLU 303
LEU 304
-0.0003
LEU 304
VAL 305
-0.0129
VAL 305
LEU 306
0.0001
LEU 306
VAL 307
-0.0165
VAL 307
LEU 308
-0.0000
LEU 308
LEU 309
0.0292
LEU 309
GLU 310
0.0001
GLU 310
GLY 311
-0.0081
GLY 311
ALA 312
0.0002
ALA 312
ASN 313
0.0015
ASN 313
PHE 314
0.0004
PHE 314
ASP 315
-0.0391
ASP 315
PRO 316
0.0001
PRO 316
GLU 317
-0.0087
GLU 317
HIS 318
-0.0002
HIS 318
PHE 319
-0.0374
PHE 319
PRO 320
-0.0000
PRO 320
ASN 321
-0.0307
ASN 321
PRO 322
0.0003
PRO 322
GLY 323
-0.0329
GLY 323
SER 324
-0.0000
SER 324
ILE 325
0.0067
ILE 325
GLU 326
-0.0003
GLU 326
LEU 327
0.0396
LEU 327
ASP 328
0.0005
ASP 328
ARG 329
0.0342
ARG 329
PRO 330
0.0001
PRO 330
ASN 331
-0.0117
ASN 331
PRO 332
0.0001
PRO 332
THR 333
-0.0328
THR 333
SER 334
-0.0003
SER 334
HIS 335
-0.0199
HIS 335
LEU 336
0.0003
LEU 336
ALA 337
0.0395
ALA 337
PHE 338
-0.0000
PHE 338
GLY 339
0.0481
GLY 339
ARG 340
-0.0002
ARG 340
GLY 341
-0.0725
GLY 341
GLN 342
0.0002
GLN 342
HIS 343
0.0219
HIS 343
PHE 344
-0.0001
PHE 344
CYS 345
0.0686
CYS 345
PRO 346
0.0001
PRO 346
GLY 347
0.0021
GLY 347
SER 348
-0.0002
SER 348
ALA 349
0.0721
ALA 349
LEU 350
-0.0004
LEU 350
GLY 351
-0.0239
GLY 351
ARG 352
-0.0001
ARG 352
ARG 353
0.1072
ARG 353
HIS 354
-0.0004
HIS 354
ALA 355
-0.0172
ALA 355
GLN 356
0.0001
GLN 356
ILE 357
0.0543
ILE 357
GLY 358
-0.0002
GLY 358
ILE 359
0.0034
ILE 359
GLU 360
0.0001
GLU 360
ALA 361
0.0241
ALA 361
LEU 362
0.0002
LEU 362
LEU 363
0.0153
LEU 363
LYS 364
-0.0002
LYS 364
LYS 365
0.0068
LYS 365
MET 366
-0.0002
MET 366
PRO 367
0.0109
PRO 367
GLY 368
0.0002
GLY 368
VAL 369
0.0171
VAL 369
ASP 370
-0.0001
ASP 370
LEU 371
0.0227
LEU 371
ALA 372
-0.0001
ALA 372
VAL 373
-0.0152
VAL 373
PRO 374
0.0001
PRO 374
ILE 375
-0.0245
ILE 375
ASP 376
-0.0002
ASP 376
GLN 377
-0.0136
GLN 377
LEU 378
0.0003
LEU 378
VAL 379
0.0548
VAL 379
TRP 380
0.0003
TRP 380
ARG 381
0.1260
ARG 381
THR 382
0.0001
THR 382
ARG 383
0.0547
ARG 383
PHE 384
0.0001
PHE 384
GLN 385
0.0164
GLN 385
ARG 386
0.0001
ARG 386
ARG 387
0.0242
ARG 387
ILE 388
0.0002
ILE 388
PRO 389
-0.0056
PRO 389
GLU 390
0.0003
GLU 390
ARG 391
0.0251
ARG 391
LEU 392
0.0004
LEU 392
PRO 393
0.0155
PRO 393
VAL 394
0.0001
VAL 394
LEU 395
0.0142
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.