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
GLY 1
LYS 2
-0.0004
LYS 2
LEU 3
-0.0963
LEU 3
THR 4
-0.0002
THR 4
ALA 5
0.0730
ALA 5
VAL 6
-0.0004
VAL 6
ASP 7
-0.0368
ASP 7
PRO 8
0.0000
PRO 8
GLU 9
-0.0115
GLU 9
THR 10
-0.0000
THR 10
ASN 11
0.0155
ASN 11
MET 12
0.0000
MET 12
ASN 13
0.2345
ASN 13
VAL 14
-0.0003
VAL 14
SER 15
-0.0562
SER 15
GLU 16
0.0002
GLU 16
ILE 17
0.0060
ILE 17
ILE 18
-0.0000
ILE 18
SER 19
0.0024
SER 19
TYR 20
0.0001
TYR 20
TRP 21
-0.0196
TRP 21
GLY 22
-0.0001
GLY 22
PHE 23
0.0333
PHE 23
PRO 24
0.0001
PRO 24
SER 25
-0.0922
SER 25
GLU 26
-0.0001
GLU 26
GLU 27
-0.1724
GLU 27
TYR 28
0.0003
TYR 28
LEU 29
-0.1736
LEU 29
VAL 30
0.0003
VAL 30
GLU 31
-0.0591
GLU 31
THR 32
0.0002
THR 32
GLU 33
0.0441
GLU 33
ASP 34
-0.0001
ASP 34
GLY 35
-0.0435
GLY 35
TYR 36
-0.0000
TYR 36
ILE 37
-0.0938
ILE 37
LEU 38
0.0002
LEU 38
CYS 39
-0.0548
CYS 39
LEU 40
0.0001
LEU 40
ASN 41
-0.0704
ASN 41
ARG 42
-0.0000
ARG 42
ILE 43
-0.0801
ILE 43
PRO 44
-0.0000
PRO 44
HIS 45
-0.0737
HIS 45
GLY 46
0.0001
GLY 46
ARG 47
0.0091
ARG 47
LYS 48
-0.0002
LYS 48
ASN 49
-0.0432
ASN 49
HIS 50
0.0004
HIS 50
SER 51
-0.0033
SER 51
ASP 52
-0.0003
ASP 52
LYS 53
-0.0108
LYS 53
GLY 54
0.0003
GLY 54
PRO 55
0.0591
PRO 55
LYS 56
0.0001
LYS 56
PRO 57
0.0644
PRO 57
VAL 58
-0.0005
VAL 58
VAL 59
-0.0111
VAL 59
PHE 60
-0.0002
PHE 60
LEU 61
0.0080
LEU 61
GLN 62
-0.0001
GLN 62
HIS 63
-0.0083
HIS 63
GLY 64
0.0003
GLY 64
LEU 65
-0.0310
LEU 65
LEU 66
-0.0002
LEU 66
ALA 67
-0.1888
ALA 67
ASP 68
-0.0001
ASP 68
SER 69
-0.0893
SER 69
SER 70
-0.0003
SER 70
ASN 71
0.0090
ASN 71
TRP 72
0.0003
TRP 72
VAL 73
-0.0120
VAL 73
THR 74
0.0001
THR 74
ASN 75
0.0043
ASN 75
LEU 76
-0.0001
LEU 76
ALA 77
-0.0628
ALA 77
ASN 78
-0.0002
ASN 78
SER 79
0.0498
SER 79
SER 80
-0.0003
SER 80
LEU 81
-0.0388
LEU 81
GLY 82
0.0001
GLY 82
PHE 83
0.0125
PHE 83
ILE 84
-0.0000
ILE 84
LEU 85
-0.0361
LEU 85
ALA 86
0.0004
ALA 86
ASP 87
-0.0112
ASP 87
ALA 88
-0.0002
ALA 88
GLY 89
-0.0405
GLY 89
PHE 90
0.0002
PHE 90
ASP 91
-0.0393
ASP 91
VAL 92
0.0003
VAL 92
TRP 93
-0.0687
TRP 93
MET 94
0.0002
MET 94
GLY 95
-0.1002
GLY 95
ASN 96
0.0000
ASN 96
SER 97
-0.1280
SER 97
ARG 98
0.0000
ARG 98
GLY 99
0.0574
GLY 99
ASN 100
0.0000
ASN 100
THR 101
-0.1899
THR 101
TRP 102
0.0003
TRP 102
SER 103
0.0894
SER 103
ARG 104
0.0002
ARG 104
LYS 105
0.1540
LYS 105
HIS 106
0.0003
HIS 106
LYS 107
0.1163
LYS 107
THR 108
0.0001
THR 108
LEU 109
0.0029
LEU 109
SER 110
0.0001
SER 110
VAL 111
0.1300
VAL 111
SER 112
0.0001
SER 112
GLN 113
-0.0675
GLN 113
ASP 114
-0.0000
ASP 114
GLU 115
0.0282
GLU 115
PHE 116
-0.0001
PHE 116
TRP 117
-0.0302
TRP 117
ALA 118
0.0004
ALA 118
PHE 119
0.0177
PHE 119
SER 120
0.0000
SER 120
TYR 121
0.0506
TYR 121
ASP 122
-0.0005
ASP 122
GLU 123
-0.0995
GLU 123
MET 124
-0.0001
MET 124
ALA 125
0.0498
ALA 125
LYS 126
0.0002
LYS 126
TYR 127
-0.0443
TYR 127
ASP 128
-0.0001
ASP 128
LEU 129
-0.0211
LEU 129
PRO 130
-0.0001
PRO 130
ALA 131
-0.0159
ALA 131
SER 132
-0.0000
SER 132
ILE 133
-0.0338
ILE 133
ASN 134
-0.0001
ASN 134
PHE 135
0.0649
PHE 135
ILE 136
0.0000
ILE 136
LEU 137
0.0157
LEU 137
ASN 138
0.0002
ASN 138
LYS 139
0.0801
LYS 139
THR 140
-0.0005
THR 140
GLY 141
0.0790
GLY 141
GLN 142
-0.0005
GLN 142
GLU 143
0.0575
GLU 143
GLN 144
0.0002
GLN 144
VAL 145
-0.0137
VAL 145
TYR 146
-0.0003
TYR 146
TYR 147
0.0105
TYR 147
VAL 148
0.0003
VAL 148
GLY 149
0.0093
GLY 149
HIS 150
-0.0002
HIS 150
SER 151
0.0179
SER 151
GLN 152
-0.0001
GLN 152
GLY 153
-0.0092
GLY 153
THR 154
-0.0002
THR 154
THR 155
0.0372
THR 155
ILE 156
0.0002
ILE 156
GLY 157
0.0170
GLY 157
PHE 158
-0.0001
PHE 158
ILE 159
0.0056
ILE 159
ALA 160
0.0002
ALA 160
PHE 161
0.0027
PHE 161
SER 162
-0.0001
SER 162
GLN 163
-0.0042
GLN 163
ILE 164
-0.0004
ILE 164
PRO 165
0.0504
PRO 165
GLU 166
0.0001
GLU 166
LEU 167
0.0083
LEU 167
ALA 168
-0.0002
ALA 168
LYS 169
0.0296
LYS 169
ARG 170
-0.0001
ARG 170
ILE 171
-0.0565
ILE 171
LYS 172
0.0002
LYS 172
MET 173
-0.0476
MET 173
PHE 174
0.0001
PHE 174
PHE 175
-0.0458
PHE 175
ALA 176
0.0003
ALA 176
LEU 177
-0.0490
LEU 177
GLY 178
-0.0001
GLY 178
PRO 179
-0.0117
PRO 179
VAL 180
-0.0000
VAL 180
ALA 181
0.0116
ALA 181
SER 182
0.0001
SER 182
VAL 183
0.0076
VAL 183
ALA 184
0.0002
ALA 184
PHE 185
-0.0339
PHE 185
CYS 186
-0.0001
CYS 186
THR 187
-0.0751
THR 187
SER 188
0.0000
SER 188
PRO 189
0.0110
PRO 189
MET 190
0.0000
MET 190
ALA 191
-0.0681
ALA 191
LYS 192
0.0000
LYS 192
LEU 193
-0.0006
LEU 193
GLY 194
-0.0003
GLY 194
ARG 195
-0.0512
ARG 195
LEU 196
-0.0003
LEU 196
PRO 197
-0.0145
PRO 197
ASP 198
-0.0003
ASP 198
HIS 199
0.0672
HIS 199
LEU 200
-0.0000
LEU 200
ILE 201
-0.0470
ILE 201
LYS 202
0.0000
LYS 202
ASP 203
0.0425
ASP 203
LEU 204
-0.0002
LEU 204
PHE 205
-0.1027
PHE 205
GLY 206
-0.0004
GLY 206
ASP 207
-0.0047
ASP 207
LYS 208
-0.0001
LYS 208
GLU 209
-0.0217
GLU 209
PHE 210
0.0001
PHE 210
LEU 211
0.1347
LEU 211
PRO 212
0.0001
PRO 212
GLN 213
-0.0630
GLN 213
SER 214
0.0004
SER 214
ALA 215
0.0206
ALA 215
PHE 216
-0.0002
PHE 216
LEU 217
-0.1253
LEU 217
LYS 218
-0.0000
LYS 218
TRP 219
-0.0949
TRP 219
LEU 220
-0.0001
LEU 220
GLY 221
-0.0526
GLY 221
THR 222
0.0002
THR 222
HIS 223
-0.0127
HIS 223
VAL 224
0.0000
VAL 224
CYS 225
0.0496
CYS 225
THR 226
-0.0001
THR 226
HIS 227
-0.0222
HIS 227
VAL 228
0.0001
VAL 228
ILE 229
-0.1664
ILE 229
LEU 230
-0.0002
LEU 230
LYS 231
0.0317
LYS 231
GLU 232
-0.0001
GLU 232
LEU 233
0.0092
LEU 233
CYS 234
0.0001
CYS 234
GLY 235
-0.0521
GLY 235
ASN 236
0.0001
ASN 236
LEU 237
0.0720
LEU 237
CYS 238
0.0002
CYS 238
PHE 239
0.0706
PHE 239
LEU 240
0.0002
LEU 240
LEU 241
0.0026
LEU 241
CYS 242
0.0002
CYS 242
GLY 243
0.0488
GLY 243
PHE 244
0.0002
PHE 244
ASN 245
0.1047
ASN 245
GLU 246
-0.0002
GLU 246
ARG 247
0.0245
ARG 247
ASN 248
-0.0003
ASN 248
LEU 249
-0.0686
LEU 249
ASN 250
-0.0002
ASN 250
MET 251
-0.1219
MET 251
SER 252
0.0000
SER 252
ARG 253
0.0243
ARG 253
VAL 254
-0.0002
VAL 254
ASP 255
-0.0589
ASP 255
VAL 256
0.0002
VAL 256
TYR 257
-0.0541
TYR 257
THR 258
-0.0000
THR 258
THR 259
-0.0559
THR 259
HIS 260
0.0001
HIS 260
SER 261
-0.1867
SER 261
PRO 262
0.0002
PRO 262
ALA 263
0.1773
ALA 263
GLY 264
-0.0000
GLY 264
THR 265
-0.0739
THR 265
SER 266
-0.0003
SER 266
VAL 267
-0.1145
VAL 267
GLN 268
0.0001
GLN 268
ASN 269
-0.0013
ASN 269
MET 270
0.0002
MET 270
LEU 271
-0.0345
LEU 271
HIS 272
0.0001
HIS 272
TRP 273
0.0037
TRP 273
SER 274
0.0001
SER 274
GLN 275
0.0061
GLN 275
ALA 276
-0.0003
ALA 276
VAL 277
-0.0123
VAL 277
LYS 278
-0.0001
LYS 278
PHE 279
0.0245
PHE 279
GLN 280
0.0001
GLN 280
LYS 281
-0.0244
LYS 281
PHE 282
0.0003
PHE 282
GLN 283
0.0812
GLN 283
ALA 284
0.0001
ALA 284
PHE 285
0.0937
PHE 285
ASP 286
-0.0005
ASP 286
TRP 287
0.0489
TRP 287
GLY 288
0.0000
GLY 288
SER 289
0.0310
SER 289
SER 290
-0.0003
SER 290
ALA 291
0.0377
ALA 291
LYS 292
-0.0001
LYS 292
ASN 293
0.0368
ASN 293
TYR 294
0.0000
TYR 294
PHE 295
-0.0030
PHE 295
HIS 296
-0.0000
HIS 296
TYR 297
-0.0051
TYR 297
ASN 298
-0.0002
ASN 298
GLN 299
0.0229
GLN 299
SER 300
-0.0001
SER 300
TYR 301
0.1078
TYR 301
PRO 302
0.0001
PRO 302
PRO 303
0.0931
PRO 303
THR 304
-0.0004
THR 304
TYR 305
0.1314
TYR 305
ASN 306
0.0003
ASN 306
VAL 307
0.0968
VAL 307
LYS 308
-0.0002
LYS 308
ASP 309
-0.0770
ASP 309
MET 310
0.0000
MET 310
LEU 311
0.0395
LEU 311
VAL 312
0.0001
VAL 312
PRO 313
-0.0430
PRO 313
THR 314
0.0002
THR 314
ALA 315
-0.0537
ALA 315
VAL 316
-0.0001
VAL 316
TRP 317
-0.1199
TRP 317
SER 318
0.0002
SER 318
GLY 319
-0.0855
GLY 319
GLY 320
-0.0002
GLY 320
HIS 321
-0.0339
HIS 321
ASP 322
0.0001
ASP 322
TRP 323
0.1096
TRP 323
LEU 324
-0.0000
LEU 324
ALA 325
-0.0523
ALA 325
ASP 326
-0.0004
ASP 326
VAL 327
0.0244
VAL 327
TYR 328
-0.0004
TYR 328
ASP 329
-0.0232
ASP 329
VAL 330
-0.0005
VAL 330
ASN 331
0.0093
ASN 331
ILE 332
-0.0001
ILE 332
LEU 333
0.0000
LEU 333
LEU 334
-0.0000
LEU 334
THR 335
-0.0137
THR 335
GLN 336
0.0000
GLN 336
ILE 337
0.0436
ILE 337
THR 338
0.0001
THR 338
ASN 339
0.0651
ASN 339
LEU 340
0.0001
LEU 340
VAL 341
0.1142
VAL 341
PHE 342
-0.0001
PHE 342
HIS 343
-0.0437
HIS 343
GLU 344
-0.0005
GLU 344
SER 345
-0.0909
SER 345
ILE 346
0.0000
ILE 346
PRO 347
-0.0845
PRO 347
GLU 348
-0.0000
GLU 348
TRP 349
0.0549
TRP 349
GLU 350
-0.0001
GLU 350
HIS 351
0.0586
HIS 351
LEU 352
0.0003
LEU 352
ASP 353
-0.0029
ASP 353
PHE 354
0.0000
PHE 354
ILE 355
0.0056
ILE 355
TRP 356
0.0000
TRP 356
GLY 357
0.0369
GLY 357
LEU 358
0.0001
LEU 358
ASP 359
-0.0616
ASP 359
ALA 360
-0.0000
ALA 360
PRO 361
0.0139
PRO 361
TRP 362
-0.0002
TRP 362
ARG 363
0.0964
ARG 363
LEU 364
0.0002
LEU 364
TYR 365
0.0378
TYR 365
ASN 366
0.0002
ASN 366
LYS 367
0.0356
LYS 367
ILE 368
-0.0001
ILE 368
ILE 369
0.0788
ILE 369
ASN 370
0.0001
ASN 370
LEU 371
0.0622
LEU 371
MET 372
0.0002
MET 372
ARG 373
0.0439
ARG 373
LYS 374
-0.0002
LYS 374
TYR 375
-0.0092
TYR 375
GLN 376
-0.0000
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: October 18th, 2018.