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
-0.0516
LEU 3
THR 4
0.0000
THR 4
ALA 5
0.1467
ALA 5
VAL 6
-0.0001
VAL 6
ASP 7
-0.0501
ASP 7
PRO 8
0.0004
PRO 8
GLU 9
-0.0254
GLU 9
THR 10
-0.0001
THR 10
ASN 11
0.0765
ASN 11
MET 12
0.0002
MET 12
ASN 13
-0.2061
ASN 13
VAL 14
0.0001
VAL 14
SER 15
0.0232
SER 15
GLU 16
0.0001
GLU 16
ILE 17
0.0422
ILE 17
ILE 18
0.0001
ILE 18
SER 19
0.0346
SER 19
TYR 20
0.0001
TYR 20
TRP 21
0.0812
TRP 21
GLY 22
0.0001
GLY 22
PHE 23
-0.0556
PHE 23
PRO 24
0.0003
PRO 24
SER 25
0.0175
SER 25
GLU 26
-0.0003
GLU 26
GLU 27
0.0159
GLU 27
TYR 28
-0.0001
TYR 28
LEU 29
0.0003
LEU 29
VAL 30
-0.0002
VAL 30
GLU 31
0.0301
GLU 31
THR 32
0.0001
THR 32
GLU 33
-0.0582
GLU 33
ASP 34
-0.0001
ASP 34
GLY 35
0.0172
GLY 35
TYR 36
0.0000
TYR 36
ILE 37
0.0250
ILE 37
LEU 38
-0.0000
LEU 38
CYS 39
-0.0906
CYS 39
LEU 40
-0.0002
LEU 40
ASN 41
-0.0668
ASN 41
ARG 42
0.0002
ARG 42
ILE 43
-0.0102
ILE 43
PRO 44
0.0000
PRO 44
HIS 45
0.0426
HIS 45
GLY 46
-0.0001
GLY 46
ARG 47
0.0017
ARG 47
LYS 48
-0.0002
LYS 48
ASN 49
-0.0539
ASN 49
HIS 50
-0.0001
HIS 50
SER 51
-0.0065
SER 51
ASP 52
0.0001
ASP 52
LYS 53
0.0261
LYS 53
GLY 54
-0.0001
GLY 54
PRO 55
-0.0386
PRO 55
LYS 56
0.0003
LYS 56
PRO 57
0.0177
PRO 57
VAL 58
0.0001
VAL 58
VAL 59
-0.0236
VAL 59
PHE 60
-0.0005
PHE 60
LEU 61
-0.0057
LEU 61
GLN 62
0.0003
GLN 62
HIS 63
0.0187
HIS 63
GLY 64
-0.0002
GLY 64
LEU 65
0.0256
LEU 65
LEU 66
-0.0001
LEU 66
ALA 67
-0.0304
ALA 67
ASP 68
0.0002
ASP 68
SER 69
0.0681
SER 69
SER 70
0.0000
SER 70
ASN 71
0.0432
ASN 71
TRP 72
-0.0004
TRP 72
VAL 73
0.0479
VAL 73
THR 74
-0.0001
THR 74
ASN 75
-0.0385
ASN 75
LEU 76
-0.0002
LEU 76
ALA 77
-0.3082
ALA 77
ASN 78
0.0001
ASN 78
SER 79
-0.1172
SER 79
SER 80
0.0001
SER 80
LEU 81
-0.0216
LEU 81
GLY 82
0.0004
GLY 82
PHE 83
0.0223
PHE 83
ILE 84
-0.0003
ILE 84
LEU 85
-0.0716
LEU 85
ALA 86
-0.0001
ALA 86
ASP 87
0.0449
ASP 87
ALA 88
0.0002
ALA 88
GLY 89
-0.0392
GLY 89
PHE 90
0.0000
PHE 90
ASP 91
0.0178
ASP 91
VAL 92
-0.0001
VAL 92
TRP 93
0.0284
TRP 93
MET 94
0.0006
MET 94
GLY 95
0.0235
GLY 95
ASN 96
0.0002
ASN 96
SER 97
-0.0105
SER 97
ARG 98
0.0005
ARG 98
GLY 99
0.0296
GLY 99
ASN 100
0.0003
ASN 100
THR 101
-0.1252
THR 101
TRP 102
-0.0002
TRP 102
SER 103
-0.2423
SER 103
ARG 104
-0.0003
ARG 104
LYS 105
0.0191
LYS 105
HIS 106
-0.0001
HIS 106
LYS 107
-0.0425
LYS 107
THR 108
-0.0001
THR 108
LEU 109
0.0442
LEU 109
SER 110
0.0001
SER 110
VAL 111
-0.0239
VAL 111
SER 112
0.0002
SER 112
GLN 113
-0.0259
GLN 113
ASP 114
0.0000
ASP 114
GLU 115
0.0104
GLU 115
PHE 116
0.0000
PHE 116
TRP 117
0.0614
TRP 117
ALA 118
0.0004
ALA 118
PHE 119
0.0513
PHE 119
SER 120
0.0000
SER 120
TYR 121
0.0135
TYR 121
ASP 122
-0.0001
ASP 122
GLU 123
0.0387
GLU 123
MET 124
0.0002
MET 124
ALA 125
-0.0098
ALA 125
LYS 126
-0.0001
LYS 126
TYR 127
-0.0196
TYR 127
ASP 128
0.0000
ASP 128
LEU 129
0.0538
LEU 129
PRO 130
0.0002
PRO 130
ALA 131
-0.0661
ALA 131
SER 132
-0.0001
SER 132
ILE 133
0.0678
ILE 133
ASN 134
-0.0002
ASN 134
PHE 135
-0.1291
PHE 135
ILE 136
0.0003
ILE 136
LEU 137
0.0118
LEU 137
ASN 138
-0.0001
ASN 138
LYS 139
-0.1011
LYS 139
THR 140
0.0001
THR 140
GLY 141
-0.0548
GLY 141
GLN 142
0.0002
GLN 142
GLU 143
-0.0068
GLU 143
GLN 144
0.0000
GLN 144
VAL 145
-0.0195
VAL 145
TYR 146
0.0004
TYR 146
TYR 147
0.0344
TYR 147
VAL 148
-0.0003
VAL 148
GLY 149
0.0229
GLY 149
HIS 150
0.0001
HIS 150
SER 151
-0.0034
SER 151
GLN 152
-0.0001
GLN 152
GLY 153
0.0311
GLY 153
THR 154
0.0001
THR 154
THR 155
-0.0051
THR 155
ILE 156
0.0001
ILE 156
GLY 157
0.0324
GLY 157
PHE 158
0.0002
PHE 158
ILE 159
-0.0026
ILE 159
ALA 160
-0.0001
ALA 160
PHE 161
0.0488
PHE 161
SER 162
-0.0004
SER 162
GLN 163
-0.0246
GLN 163
ILE 164
-0.0001
ILE 164
PRO 165
0.0494
PRO 165
GLU 166
-0.0000
GLU 166
LEU 167
-0.0212
LEU 167
ALA 168
-0.0001
ALA 168
LYS 169
0.0232
LYS 169
ARG 170
0.0001
ARG 170
ILE 171
-0.0393
ILE 171
LYS 172
0.0003
LYS 172
MET 173
-0.0758
MET 173
PHE 174
-0.0006
PHE 174
PHE 175
-0.0162
PHE 175
ALA 176
-0.0000
ALA 176
LEU 177
0.0066
LEU 177
GLY 178
-0.0001
GLY 178
PRO 179
0.0126
PRO 179
VAL 180
-0.0002
VAL 180
ALA 181
-0.0045
ALA 181
SER 182
0.0001
SER 182
VAL 183
0.0539
VAL 183
ALA 184
-0.0000
ALA 184
PHE 185
-0.0303
PHE 185
CYS 186
-0.0000
CYS 186
THR 187
0.0280
THR 187
SER 188
0.0002
SER 188
PRO 189
-0.0513
PRO 189
MET 190
0.0000
MET 190
ALA 191
0.0001
ALA 191
LYS 192
0.0002
LYS 192
LEU 193
-0.0427
LEU 193
GLY 194
0.0001
GLY 194
ARG 195
-0.0039
ARG 195
LEU 196
0.0000
LEU 196
PRO 197
0.0436
PRO 197
ASP 198
0.0000
ASP 198
HIS 199
0.0257
HIS 199
LEU 200
-0.0000
LEU 200
ILE 201
0.0052
ILE 201
LYS 202
0.0003
LYS 202
ASP 203
0.0224
ASP 203
LEU 204
-0.0002
LEU 204
PHE 205
-0.0562
PHE 205
GLY 206
-0.0001
GLY 206
ASP 207
-0.0225
ASP 207
LYS 208
0.0000
LYS 208
GLU 209
-0.0146
GLU 209
PHE 210
-0.0001
PHE 210
LEU 211
0.1195
LEU 211
PRO 212
0.0003
PRO 212
GLN 213
-0.1658
GLN 213
SER 214
0.0000
SER 214
ALA 215
0.0031
ALA 215
PHE 216
-0.0002
PHE 216
LEU 217
-0.0065
LEU 217
LYS 218
0.0003
LYS 218
TRP 219
0.0336
TRP 219
LEU 220
0.0000
LEU 220
GLY 221
-0.0148
GLY 221
THR 222
0.0000
THR 222
HIS 223
-0.0547
HIS 223
VAL 224
0.0002
VAL 224
CYS 225
0.0192
CYS 225
THR 226
-0.0002
THR 226
HIS 227
-0.1104
HIS 227
VAL 228
0.0000
VAL 228
ILE 229
-0.1047
ILE 229
LEU 230
0.0002
LEU 230
LYS 231
-0.0691
LYS 231
GLU 232
-0.0001
GLU 232
LEU 233
0.0234
LEU 233
CYS 234
-0.0000
CYS 234
GLY 235
0.0882
GLY 235
ASN 236
-0.0006
ASN 236
LEU 237
0.2155
LEU 237
CYS 238
0.0002
CYS 238
PHE 239
-0.0672
PHE 239
LEU 240
0.0000
LEU 240
LEU 241
0.2029
LEU 241
CYS 242
0.0002
CYS 242
GLY 243
0.1534
GLY 243
PHE 244
0.0002
PHE 244
ASN 245
-0.0795
ASN 245
GLU 246
-0.0001
GLU 246
ARG 247
-0.1489
ARG 247
ASN 248
-0.0001
ASN 248
LEU 249
0.1413
LEU 249
ASN 250
0.0005
ASN 250
MET 251
-0.2819
MET 251
SER 252
0.0002
SER 252
ARG 253
-0.2478
ARG 253
VAL 254
0.0004
VAL 254
ASP 255
0.1001
ASP 255
VAL 256
-0.0003
VAL 256
TYR 257
0.0395
TYR 257
THR 258
0.0000
THR 258
THR 259
0.0942
THR 259
HIS 260
-0.0003
HIS 260
SER 261
-0.0868
SER 261
PRO 262
0.0001
PRO 262
ALA 263
0.2105
ALA 263
GLY 264
0.0002
GLY 264
THR 265
-0.0537
THR 265
SER 266
-0.0001
SER 266
VAL 267
-0.0644
VAL 267
GLN 268
0.0001
GLN 268
ASN 269
0.0196
ASN 269
MET 270
0.0003
MET 270
LEU 271
0.0015
LEU 271
HIS 272
0.0000
HIS 272
TRP 273
0.0340
TRP 273
SER 274
-0.0002
SER 274
GLN 275
0.0001
GLN 275
ALA 276
-0.0000
ALA 276
VAL 277
0.0181
VAL 277
LYS 278
0.0003
LYS 278
PHE 279
-0.0308
PHE 279
GLN 280
0.0001
GLN 280
LYS 281
0.0539
LYS 281
PHE 282
-0.0000
PHE 282
GLN 283
-0.1270
GLN 283
ALA 284
0.0002
ALA 284
PHE 285
0.0231
PHE 285
ASP 286
-0.0000
ASP 286
TRP 287
-0.0358
TRP 287
GLY 288
0.0003
GLY 288
SER 289
-0.0627
SER 289
SER 290
-0.0000
SER 290
ALA 291
-0.0074
ALA 291
LYS 292
0.0001
LYS 292
ASN 293
-0.0370
ASN 293
TYR 294
-0.0001
TYR 294
PHE 295
0.0489
PHE 295
HIS 296
0.0001
HIS 296
TYR 297
0.0349
TYR 297
ASN 298
-0.0005
ASN 298
GLN 299
-0.0689
GLN 299
SER 300
-0.0003
SER 300
TYR 301
-0.1797
TYR 301
PRO 302
0.0001
PRO 302
PRO 303
0.0141
PRO 303
THR 304
-0.0001
THR 304
TYR 305
-0.0307
TYR 305
ASN 306
-0.0003
ASN 306
VAL 307
-0.0464
VAL 307
LYS 308
0.0002
LYS 308
ASP 309
-0.0042
ASP 309
MET 310
0.0002
MET 310
LEU 311
0.0149
LEU 311
VAL 312
0.0001
VAL 312
PRO 313
0.0110
PRO 313
THR 314
0.0003
THR 314
ALA 315
-0.0093
ALA 315
VAL 316
-0.0001
VAL 316
TRP 317
0.0075
TRP 317
SER 318
0.0001
SER 318
GLY 319
-0.0124
GLY 319
GLY 320
0.0001
GLY 320
HIS 321
-0.0335
HIS 321
ASP 322
0.0003
ASP 322
TRP 323
-0.0843
TRP 323
LEU 324
0.0003
LEU 324
ALA 325
-0.0326
ALA 325
ASP 326
0.0001
ASP 326
VAL 327
-0.0368
VAL 327
TYR 328
0.0000
TYR 328
ASP 329
-0.0177
ASP 329
VAL 330
-0.0001
VAL 330
ASN 331
0.0122
ASN 331
ILE 332
-0.0001
ILE 332
LEU 333
-0.0085
LEU 333
LEU 334
-0.0001
LEU 334
THR 335
0.0358
THR 335
GLN 336
0.0003
GLN 336
ILE 337
0.0079
ILE 337
THR 338
0.0001
THR 338
ASN 339
0.0104
ASN 339
LEU 340
-0.0001
LEU 340
VAL 341
0.0225
VAL 341
PHE 342
-0.0002
PHE 342
HIS 343
-0.0417
HIS 343
GLU 344
0.0002
GLU 344
SER 345
-0.0774
SER 345
ILE 346
0.0001
ILE 346
PRO 347
-0.0218
PRO 347
GLU 348
-0.0001
GLU 348
TRP 349
-0.0110
TRP 349
GLU 350
-0.0003
GLU 350
HIS 351
0.0465
HIS 351
LEU 352
-0.0004
LEU 352
ASP 353
-0.0612
ASP 353
PHE 354
0.0002
PHE 354
ILE 355
0.0701
ILE 355
TRP 356
0.0001
TRP 356
GLY 357
0.0832
GLY 357
LEU 358
-0.0005
LEU 358
ASP 359
0.0436
ASP 359
ALA 360
-0.0001
ALA 360
PRO 361
-0.0578
PRO 361
TRP 362
-0.0000
TRP 362
ARG 363
0.1185
ARG 363
LEU 364
-0.0002
LEU 364
TYR 365
-0.0581
TYR 365
ASN 366
-0.0003
ASN 366
LYS 367
0.0923
LYS 367
ILE 368
0.0003
ILE 368
ILE 369
-0.0026
ILE 369
ASN 370
0.0001
ASN 370
LEU 371
0.0741
LEU 371
MET 372
0.0000
MET 372
ARG 373
0.0548
ARG 373
LYS 374
-0.0000
LYS 374
TYR 375
0.0754
TYR 375
GLN 376
0.0002
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.