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
0.0001
LYS 2
LEU 3
0.0739
LEU 3
THR 4
0.0003
THR 4
ALA 5
-0.0127
ALA 5
VAL 6
0.0001
VAL 6
ASP 7
0.0748
ASP 7
PRO 8
-0.0000
PRO 8
GLU 9
-0.0143
GLU 9
THR 10
0.0002
THR 10
ASN 11
0.0373
ASN 11
MET 12
0.0000
MET 12
ASN 13
-0.1789
ASN 13
VAL 14
0.0002
VAL 14
SER 15
0.0109
SER 15
GLU 16
-0.0001
GLU 16
ILE 17
0.0212
ILE 17
ILE 18
-0.0001
ILE 18
SER 19
-0.0006
SER 19
TYR 20
-0.0001
TYR 20
TRP 21
0.0239
TRP 21
GLY 22
-0.0002
GLY 22
PHE 23
0.0119
PHE 23
PRO 24
-0.0003
PRO 24
SER 25
-0.0448
SER 25
GLU 26
-0.0002
GLU 26
GLU 27
-0.0559
GLU 27
TYR 28
-0.0002
TYR 28
LEU 29
-0.0791
LEU 29
VAL 30
0.0002
VAL 30
GLU 31
-0.0346
GLU 31
THR 32
-0.0002
THR 32
GLU 33
-0.0604
GLU 33
ASP 34
-0.0001
ASP 34
GLY 35
-0.0400
GLY 35
TYR 36
0.0000
TYR 36
ILE 37
-0.0383
ILE 37
LEU 38
-0.0002
LEU 38
CYS 39
-0.1202
CYS 39
LEU 40
0.0000
LEU 40
ASN 41
-0.0936
ASN 41
ARG 42
-0.0002
ARG 42
ILE 43
-0.0317
ILE 43
PRO 44
-0.0001
PRO 44
HIS 45
-0.0213
HIS 45
GLY 46
0.0000
GLY 46
ARG 47
-0.0056
ARG 47
LYS 48
-0.0001
LYS 48
ASN 49
0.0135
ASN 49
HIS 50
-0.0001
HIS 50
SER 51
0.0081
SER 51
ASP 52
-0.0004
ASP 52
LYS 53
0.0039
LYS 53
GLY 54
0.0001
GLY 54
PRO 55
-0.0075
PRO 55
LYS 56
0.0000
LYS 56
PRO 57
-0.0112
PRO 57
VAL 58
-0.0000
VAL 58
VAL 59
-0.0027
VAL 59
PHE 60
0.0003
PHE 60
LEU 61
0.0052
LEU 61
GLN 62
-0.0003
GLN 62
HIS 63
0.0018
HIS 63
GLY 64
0.0001
GLY 64
LEU 65
0.0085
LEU 65
LEU 66
0.0000
LEU 66
ALA 67
0.0113
ALA 67
ASP 68
-0.0002
ASP 68
SER 69
0.0464
SER 69
SER 70
-0.0000
SER 70
ASN 71
0.0070
ASN 71
TRP 72
0.0004
TRP 72
VAL 73
0.0264
VAL 73
THR 74
-0.0001
THR 74
ASN 75
-0.0592
ASN 75
LEU 76
0.0000
LEU 76
ALA 77
0.0216
ALA 77
ASN 78
0.0005
ASN 78
SER 79
-0.0190
SER 79
SER 80
0.0000
SER 80
LEU 81
0.0258
LEU 81
GLY 82
-0.0005
GLY 82
PHE 83
-0.0017
PHE 83
ILE 84
0.0001
ILE 84
LEU 85
0.0122
LEU 85
ALA 86
-0.0001
ALA 86
ASP 87
-0.0096
ASP 87
ALA 88
0.0003
ALA 88
GLY 89
0.0040
GLY 89
PHE 90
-0.0004
PHE 90
ASP 91
-0.0039
ASP 91
VAL 92
-0.0002
VAL 92
TRP 93
-0.0054
TRP 93
MET 94
0.0001
MET 94
GLY 95
-0.0247
GLY 95
ASN 96
0.0001
ASN 96
SER 97
-0.0967
SER 97
ARG 98
0.0002
ARG 98
GLY 99
0.0377
GLY 99
ASN 100
0.0003
ASN 100
THR 101
-0.1091
THR 101
TRP 102
0.0000
TRP 102
SER 103
-0.2293
SER 103
ARG 104
-0.0002
ARG 104
LYS 105
-0.0064
LYS 105
HIS 106
-0.0000
HIS 106
LYS 107
-0.0378
LYS 107
THR 108
-0.0003
THR 108
LEU 109
0.0222
LEU 109
SER 110
-0.0000
SER 110
VAL 111
-0.0207
VAL 111
SER 112
-0.0003
SER 112
GLN 113
-0.0023
GLN 113
ASP 114
0.0000
ASP 114
GLU 115
-0.0213
GLU 115
PHE 116
0.0002
PHE 116
TRP 117
-0.0368
TRP 117
ALA 118
0.0003
ALA 118
PHE 119
0.0843
PHE 119
SER 120
-0.0004
SER 120
TYR 121
0.0441
TYR 121
ASP 122
-0.0001
ASP 122
GLU 123
-0.1089
GLU 123
MET 124
-0.0001
MET 124
ALA 125
0.1030
ALA 125
LYS 126
-0.0000
LYS 126
TYR 127
-0.0336
TYR 127
ASP 128
0.0004
ASP 128
LEU 129
0.0622
LEU 129
PRO 130
-0.0001
PRO 130
ALA 131
-0.0085
ALA 131
SER 132
-0.0003
SER 132
ILE 133
0.0739
ILE 133
ASN 134
0.0000
ASN 134
PHE 135
-0.0480
PHE 135
ILE 136
0.0002
ILE 136
LEU 137
0.0330
LEU 137
ASN 138
0.0000
ASN 138
LYS 139
-0.0244
LYS 139
THR 140
0.0004
THR 140
GLY 141
-0.0037
GLY 141
GLN 142
0.0001
GLN 142
GLU 143
-0.0323
GLU 143
GLN 144
-0.0000
GLN 144
VAL 145
0.0077
VAL 145
TYR 146
0.0001
TYR 146
TYR 147
-0.0009
TYR 147
VAL 148
-0.0000
VAL 148
GLY 149
-0.0025
GLY 149
HIS 150
-0.0003
HIS 150
SER 151
0.0084
SER 151
GLN 152
-0.0001
GLN 152
GLY 153
0.0051
GLY 153
THR 154
0.0000
THR 154
THR 155
0.0274
THR 155
ILE 156
-0.0001
ILE 156
GLY 157
0.0071
GLY 157
PHE 158
0.0001
PHE 158
ILE 159
0.0724
ILE 159
ALA 160
-0.0001
ALA 160
PHE 161
0.0364
PHE 161
SER 162
0.0001
SER 162
GLN 163
0.0638
GLN 163
ILE 164
0.0000
ILE 164
PRO 165
0.0311
PRO 165
GLU 166
0.0001
GLU 166
LEU 167
0.0323
LEU 167
ALA 168
0.0003
ALA 168
LYS 169
-0.0068
LYS 169
ARG 170
-0.0003
ARG 170
ILE 171
-0.0044
ILE 171
LYS 172
-0.0000
LYS 172
MET 173
-0.0258
MET 173
PHE 174
-0.0001
PHE 174
PHE 175
0.0063
PHE 175
ALA 176
0.0001
ALA 176
LEU 177
0.0056
LEU 177
GLY 178
-0.0002
GLY 178
PRO 179
0.0572
PRO 179
VAL 180
-0.0001
VAL 180
ALA 181
0.0888
ALA 181
SER 182
0.0001
SER 182
VAL 183
-0.0557
VAL 183
ALA 184
-0.0001
ALA 184
PHE 185
0.1687
PHE 185
CYS 186
-0.0001
CYS 186
THR 187
0.0825
THR 187
SER 188
0.0002
SER 188
PRO 189
-0.0666
PRO 189
MET 190
0.0002
MET 190
ALA 191
0.0421
ALA 191
LYS 192
-0.0003
LYS 192
LEU 193
0.0136
LEU 193
GLY 194
-0.0000
GLY 194
ARG 195
0.0086
ARG 195
LEU 196
0.0001
LEU 196
PRO 197
0.0123
PRO 197
ASP 198
0.0002
ASP 198
HIS 199
-0.0228
HIS 199
LEU 200
0.0003
LEU 200
ILE 201
0.0152
ILE 201
LYS 202
0.0001
LYS 202
ASP 203
-0.0152
ASP 203
LEU 204
-0.0001
LEU 204
PHE 205
0.0795
PHE 205
GLY 206
0.0001
GLY 206
ASP 207
0.0268
ASP 207
LYS 208
-0.0002
LYS 208
GLU 209
-0.0712
GLU 209
PHE 210
-0.0002
PHE 210
LEU 211
-0.0921
LEU 211
PRO 212
0.0002
PRO 212
GLN 213
-0.0557
GLN 213
SER 214
-0.0005
SER 214
ALA 215
-0.0139
ALA 215
PHE 216
-0.0001
PHE 216
LEU 217
0.0627
LEU 217
LYS 218
0.0002
LYS 218
TRP 219
0.0918
TRP 219
LEU 220
-0.0000
LEU 220
GLY 221
0.0095
GLY 221
THR 222
0.0003
THR 222
HIS 223
0.0229
HIS 223
VAL 224
0.0000
VAL 224
CYS 225
-0.0094
CYS 225
THR 226
-0.0000
THR 226
HIS 227
-0.0425
HIS 227
VAL 228
0.0001
VAL 228
ILE 229
0.0161
ILE 229
LEU 230
-0.0001
LEU 230
LYS 231
0.0135
LYS 231
GLU 232
0.0003
GLU 232
LEU 233
0.0297
LEU 233
CYS 234
-0.0001
CYS 234
GLY 235
0.0375
GLY 235
ASN 236
0.0003
ASN 236
LEU 237
-0.0266
LEU 237
CYS 238
-0.0003
CYS 238
PHE 239
-0.0643
PHE 239
LEU 240
-0.0001
LEU 240
LEU 241
0.0137
LEU 241
CYS 242
0.0000
CYS 242
GLY 243
0.0372
GLY 243
PHE 244
-0.0001
PHE 244
ASN 245
-0.0462
ASN 245
GLU 246
-0.0000
GLU 246
ARG 247
-0.0427
ARG 247
ASN 248
-0.0001
ASN 248
LEU 249
0.0576
LEU 249
ASN 250
0.0000
ASN 250
MET 251
0.0193
MET 251
SER 252
-0.0001
SER 252
ARG 253
-0.0343
ARG 253
VAL 254
0.0000
VAL 254
ASP 255
0.0520
ASP 255
VAL 256
-0.0002
VAL 256
TYR 257
0.0155
TYR 257
THR 258
0.0006
THR 258
THR 259
0.0917
THR 259
HIS 260
-0.0000
HIS 260
SER 261
-0.0154
SER 261
PRO 262
-0.0002
PRO 262
ALA 263
0.0289
ALA 263
GLY 264
-0.0003
GLY 264
THR 265
-0.1608
THR 265
SER 266
-0.0001
SER 266
VAL 267
0.0650
VAL 267
GLN 268
-0.0002
GLN 268
ASN 269
-0.0264
ASN 269
MET 270
0.0002
MET 270
LEU 271
-0.0160
LEU 271
HIS 272
-0.0000
HIS 272
TRP 273
0.0155
TRP 273
SER 274
0.0002
SER 274
GLN 275
0.0422
GLN 275
ALA 276
-0.0001
ALA 276
VAL 277
0.0286
VAL 277
LYS 278
-0.0003
LYS 278
PHE 279
0.0458
PHE 279
GLN 280
0.0002
GLN 280
LYS 281
-0.1001
LYS 281
PHE 282
-0.0003
PHE 282
GLN 283
0.2852
GLN 283
ALA 284
-0.0003
ALA 284
PHE 285
0.0369
PHE 285
ASP 286
-0.0000
ASP 286
TRP 287
0.0769
TRP 287
GLY 288
0.0001
GLY 288
SER 289
0.0459
SER 289
SER 290
-0.0000
SER 290
ALA 291
0.0296
ALA 291
LYS 292
-0.0004
LYS 292
ASN 293
0.0609
ASN 293
TYR 294
-0.0001
TYR 294
PHE 295
-0.0327
PHE 295
HIS 296
-0.0002
HIS 296
TYR 297
-0.0652
TYR 297
ASN 298
-0.0000
ASN 298
GLN 299
0.0560
GLN 299
SER 300
0.0001
SER 300
TYR 301
0.2179
TYR 301
PRO 302
0.0003
PRO 302
PRO 303
0.0692
PRO 303
THR 304
0.0001
THR 304
TYR 305
0.1160
TYR 305
ASN 306
-0.0001
ASN 306
VAL 307
0.1656
VAL 307
LYS 308
-0.0002
LYS 308
ASP 309
-0.0362
ASP 309
MET 310
-0.0001
MET 310
LEU 311
0.0199
LEU 311
VAL 312
-0.0005
VAL 312
PRO 313
0.0316
PRO 313
THR 314
-0.0000
THR 314
ALA 315
0.0267
ALA 315
VAL 316
0.0002
VAL 316
TRP 317
0.0265
TRP 317
SER 318
0.0001
SER 318
GLY 319
-0.0082
GLY 319
GLY 320
0.0001
GLY 320
HIS 321
-0.0221
HIS 321
ASP 322
0.0002
ASP 322
TRP 323
-0.0468
TRP 323
LEU 324
-0.0000
LEU 324
ALA 325
-0.0647
ALA 325
ASP 326
-0.0003
ASP 326
VAL 327
-0.0546
VAL 327
TYR 328
-0.0000
TYR 328
ASP 329
0.0395
ASP 329
VAL 330
-0.0000
VAL 330
ASN 331
0.0061
ASN 331
ILE 332
0.0002
ILE 332
LEU 333
-0.0259
LEU 333
LEU 334
0.0002
LEU 334
THR 335
0.0396
THR 335
GLN 336
-0.0001
GLN 336
ILE 337
-0.0462
ILE 337
THR 338
-0.0001
THR 338
ASN 339
0.0306
ASN 339
LEU 340
0.0003
LEU 340
VAL 341
0.0271
VAL 341
PHE 342
-0.0000
PHE 342
HIS 343
-0.0163
HIS 343
GLU 344
0.0001
GLU 344
SER 345
-0.0241
SER 345
ILE 346
-0.0001
ILE 346
PRO 347
-0.0039
PRO 347
GLU 348
0.0001
GLU 348
TRP 349
-0.0311
TRP 349
GLU 350
0.0006
GLU 350
HIS 351
-0.0111
HIS 351
LEU 352
-0.0000
LEU 352
ASP 353
-0.0138
ASP 353
PHE 354
-0.0000
PHE 354
ILE 355
0.0285
ILE 355
TRP 356
0.0005
TRP 356
GLY 357
-0.0276
GLY 357
LEU 358
0.0001
LEU 358
ASP 359
0.0449
ASP 359
ALA 360
-0.0000
ALA 360
PRO 361
-0.0104
PRO 361
TRP 362
0.0002
TRP 362
ARG 363
0.0439
ARG 363
LEU 364
0.0003
LEU 364
TYR 365
-0.0127
TYR 365
ASN 366
-0.0002
ASN 366
LYS 367
0.0439
LYS 367
ILE 368
0.0003
ILE 368
ILE 369
0.0024
ILE 369
ASN 370
-0.0001
ASN 370
LEU 371
0.0349
LEU 371
MET 372
-0.0001
MET 372
ARG 373
0.0070
ARG 373
LYS 374
0.0001
LYS 374
TYR 375
0.0381
TYR 375
GLN 376
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: October 18th, 2018.