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
LYS 1
ILE 2
0.0001
ILE 2
GLU 3
0.0339
GLU 3
GLU 4
0.0002
GLU 4
GLY 5
-0.0388
GLY 5
LYS 6
0.0001
LYS 6
LEU 7
-0.0056
LEU 7
VAL 8
0.0001
VAL 8
ILE 9
0.0111
ILE 9
TRP 10
-0.0001
TRP 10
ILE 11
0.1489
ILE 11
ASN 12
-0.0002
ASN 12
GLY 13
-0.0192
GLY 13
ASP 14
0.0002
ASP 14
LYS 15
-0.0402
LYS 15
GLY 16
-0.0000
GLY 16
TYR 17
0.0442
TYR 17
ASN 18
0.0001
ASN 18
GLY 19
-0.0060
GLY 19
LEU 20
0.0002
LEU 20
ALA 21
-0.0031
ALA 21
GLU 22
0.0000
GLU 22
VAL 23
-0.0044
VAL 23
GLY 24
-0.0000
GLY 24
LYS 25
-0.0176
LYS 25
LYS 26
-0.0003
LYS 26
PHE 27
0.0011
PHE 27
GLU 28
0.0003
GLU 28
LYS 29
-0.0148
LYS 29
ASP 30
0.0001
ASP 30
THR 31
-0.0010
THR 31
GLY 32
-0.0001
GLY 32
ILE 33
-0.0109
ILE 33
LYS 34
0.0002
LYS 34
VAL 35
0.0018
VAL 35
THR 36
-0.0000
THR 36
VAL 37
0.0415
VAL 37
GLU 38
0.0001
GLU 38
HIS 39
-0.0053
HIS 39
PRO 40
-0.0001
PRO 40
ASP 41
-0.0725
ASP 41
LYS 42
-0.0002
LYS 42
LEU 43
0.0393
LEU 43
GLU 44
-0.0001
GLU 44
GLU 45
0.0307
GLU 45
LYS 46
-0.0001
LYS 46
PHE 47
-0.0102
PHE 47
PRO 48
0.0001
PRO 48
GLN 49
-0.0322
GLN 49
VAL 50
-0.0002
VAL 50
ALA 51
-0.0041
ALA 51
ALA 52
-0.0002
ALA 52
THR 53
-0.0310
THR 53
GLY 54
0.0002
GLY 54
ASP 55
0.0285
ASP 55
GLY 56
0.0004
GLY 56
PRO 57
0.0233
PRO 57
ASP 58
-0.0001
ASP 58
ILE 59
0.0014
ILE 59
ILE 60
0.0003
ILE 60
PHE 61
0.0171
PHE 61
TRP 62
0.0001
TRP 62
ALA 63
0.0124
ALA 63
HIS 64
-0.0002
HIS 64
ASP 65
0.0189
ASP 65
ARG 66
0.0003
ARG 66
PHE 67
0.0249
PHE 67
GLY 68
-0.0000
GLY 68
GLY 69
-0.0057
GLY 69
TYR 70
-0.0001
TYR 70
ALA 71
0.0264
ALA 71
GLN 72
0.0001
GLN 72
SER 73
-0.0407
SER 73
GLY 74
-0.0000
GLY 74
LEU 75
0.0122
LEU 75
LEU 76
0.0000
LEU 76
ALA 77
-0.0114
ALA 77
GLU 78
-0.0001
GLU 78
ILE 79
-0.0274
ILE 79
THR 80
-0.0000
THR 80
PRO 81
-0.0275
PRO 81
ASP 82
-0.0001
ASP 82
LYS 83
0.0026
LYS 83
ALA 84
-0.0001
ALA 84
PHE 85
-0.0125
PHE 85
GLN 86
0.0003
GLN 86
ASP 87
-0.0086
ASP 87
LYS 88
-0.0002
LYS 88
LEU 89
0.0174
LEU 89
TYR 90
-0.0001
TYR 90
PRO 91
-0.0324
PRO 91
PHE 92
0.0002
PHE 92
THR 93
-0.0060
THR 93
TRP 94
-0.0002
TRP 94
ASP 95
0.0531
ASP 95
ALA 96
-0.0001
ALA 96
VAL 97
-0.0087
VAL 97
ARG 98
-0.0004
ARG 98
TYR 99
0.0049
TYR 99
ASN 100
-0.0000
ASN 100
GLY 101
0.0191
GLY 101
LYS 102
-0.0000
LYS 102
LEU 103
0.0028
LEU 103
ILE 104
-0.0000
ILE 104
ALA 105
0.0084
ALA 105
TYR 106
-0.0002
TYR 106
PRO 107
-0.0154
PRO 107
ILE 108
-0.0001
ILE 108
ALA 109
-0.0135
ALA 109
VAL 110
0.0003
VAL 110
GLU 111
-0.0326
GLU 111
ALA 112
0.0000
ALA 112
LEU 113
-0.0123
LEU 113
SER 114
0.0001
SER 114
LEU 115
-0.0226
LEU 115
ILE 116
0.0001
ILE 116
TYR 117
0.0168
TYR 117
ASN 118
-0.0001
ASN 118
LYS 119
0.0039
LYS 119
ASP 120
-0.0000
ASP 120
LEU 121
0.0112
LEU 121
LEU 122
0.0003
LEU 122
PRO 123
0.0116
PRO 123
ASN 124
0.0003
ASN 124
PRO 125
0.0030
PRO 125
PRO 126
0.0001
PRO 126
LYS 127
-0.0052
LYS 127
THR 128
0.0003
THR 128
TRP 129
0.0261
TRP 129
GLU 130
-0.0002
GLU 130
GLU 131
-0.0358
GLU 131
ILE 132
-0.0002
ILE 132
PRO 133
0.0121
PRO 133
ALA 134
-0.0002
ALA 134
LEU 135
0.0405
LEU 135
ASP 136
0.0002
ASP 136
LYS 137
0.0038
LYS 137
GLU 138
0.0001
GLU 138
LEU 139
0.0192
LEU 139
LYS 140
0.0003
LYS 140
ALA 141
0.0285
ALA 141
LYS 142
-0.0002
LYS 142
GLY 143
0.0087
GLY 143
LYS 144
0.0002
LYS 144
SER 145
0.0171
SER 145
ALA 146
0.0004
ALA 146
LEU 147
0.0389
LEU 147
MET 148
-0.0001
MET 148
PHE 149
0.0882
PHE 149
ASN 150
0.0002
ASN 150
LEU 151
-0.0802
LEU 151
GLN 152
-0.0000
GLN 152
GLU 153
0.0971
GLU 153
PRO 154
0.0001
PRO 154
TYR 155
-0.1103
TYR 155
PHE 156
-0.0003
PHE 156
THR 157
-0.0676
THR 157
TRP 158
0.0001
TRP 158
PRO 159
-0.0162
PRO 159
LEU 160
-0.0001
LEU 160
ILE 161
-0.0053
ILE 161
ALA 162
-0.0001
ALA 162
ALA 163
-0.0475
ALA 163
ASP 164
0.0002
ASP 164
GLY 165
-0.1247
GLY 165
GLY 166
-0.0004
GLY 166
TYR 167
-0.0779
TYR 167
ALA 168
-0.0001
ALA 168
PHE 169
-0.0270
PHE 169
LYS 170
-0.0001
LYS 170
TYR 171
-0.0359
TYR 171
GLU 172
-0.0005
GLU 172
ASN 173
-0.0234
ASN 173
GLY 174
0.0000
GLY 174
LYS 175
0.0129
LYS 175
TYR 176
-0.0004
TYR 176
ASP 177
0.0804
ASP 177
ILE 178
0.0002
ILE 178
LYS 179
-0.0144
LYS 179
ASP 180
-0.0000
ASP 180
VAL 181
-0.0290
VAL 181
GLY 182
0.0002
GLY 182
VAL 183
-0.0505
VAL 183
ASP 184
-0.0000
ASP 184
ASN 185
0.0224
ASN 185
ALA 186
0.0002
ALA 186
GLY 187
0.0334
GLY 187
ALA 188
-0.0003
ALA 188
LYS 189
0.0121
LYS 189
ALA 190
-0.0000
ALA 190
GLY 191
0.0153
GLY 191
LEU 192
-0.0001
LEU 192
THR 193
0.0136
THR 193
PHE 194
-0.0000
PHE 194
LEU 195
-0.0080
LEU 195
VAL 196
-0.0001
VAL 196
ASP 197
0.0381
ASP 197
LEU 198
-0.0002
LEU 198
ILE 199
-0.0025
ILE 199
LYS 200
-0.0000
LYS 200
ASN 201
0.0467
ASN 201
LYS 202
0.0002
LYS 202
HIS 203
-0.0047
HIS 203
MET 204
-0.0001
MET 204
ASN 205
0.0366
ASN 205
ALA 206
0.0000
ALA 206
ASP 207
-0.1021
ASP 207
THR 208
-0.0002
THR 208
ASP 209
-0.0925
ASP 209
TYR 210
-0.0001
TYR 210
SER 211
0.0277
SER 211
ILE 212
0.0000
ILE 212
ALA 213
0.0090
ALA 213
GLU 214
-0.0001
GLU 214
ALA 215
0.0374
ALA 215
ALA 216
0.0001
ALA 216
PHE 217
-0.0271
PHE 217
ASN 218
-0.0001
ASN 218
LYS 219
0.0001
LYS 219
GLY 220
-0.0000
GLY 220
GLU 221
-0.0052
GLU 221
THR 222
-0.0003
THR 222
ALA 223
-0.0105
ALA 223
MET 224
0.0001
MET 224
THR 225
0.0509
THR 225
ILE 226
-0.0002
ILE 226
ASN 227
0.0064
ASN 227
GLY 228
0.0001
GLY 228
PRO 229
-0.0344
PRO 229
TRP 230
0.0000
TRP 230
ALA 231
0.0614
ALA 231
TRP 232
0.0004
TRP 232
SER 233
0.0052
SER 233
ASN 234
-0.0004
ASN 234
ILE 235
0.0847
ILE 235
ASP 236
0.0006
ASP 236
THR 237
-0.0413
THR 237
SER 238
0.0001
SER 238
LYS 239
0.0227
LYS 239
VAL 240
0.0001
VAL 240
ASN 241
-0.0044
ASN 241
TYR 242
0.0002
TYR 242
GLY 243
-0.0636
GLY 243
VAL 244
-0.0001
VAL 244
THR 245
0.0586
THR 245
VAL 246
0.0003
VAL 246
LEU 247
0.0090
LEU 247
PRO 248
0.0003
PRO 248
THR 249
0.0598
THR 249
PHE 250
0.0001
PHE 250
LYS 251
0.0126
LYS 251
GLY 252
-0.0001
GLY 252
GLN 253
-0.0170
GLN 253
PRO 254
-0.0001
PRO 254
SER 255
-0.0016
SER 255
LYS 256
0.0001
LYS 256
PRO 257
-0.0160
PRO 257
PHE 258
-0.0003
PHE 258
VAL 259
0.0467
VAL 259
GLY 260
0.0001
GLY 260
VAL 261
0.0252
VAL 261
LEU 262
-0.0001
LEU 262
SER 263
0.0042
SER 263
ALA 264
-0.0001
ALA 264
GLY 265
-0.0040
GLY 265
ILE 266
0.0003
ILE 266
ASN 267
-0.0241
ASN 267
ALA 268
-0.0000
ALA 268
ALA 269
-0.0299
ALA 269
SER 270
-0.0000
SER 270
PRO 271
0.0053
PRO 271
ASN 272
0.0001
ASN 272
LYS 273
0.0003
LYS 273
GLU 274
-0.0003
GLU 274
LEU 275
0.0171
LEU 275
ALA 276
-0.0001
ALA 276
LYS 277
-0.0144
LYS 277
GLU 278
-0.0001
GLU 278
PHE 279
0.0068
PHE 279
LEU 280
-0.0002
LEU 280
GLU 281
-0.0089
GLU 281
ASN 282
-0.0003
ASN 282
TYR 283
0.0257
TYR 283
LEU 284
-0.0000
LEU 284
LEU 285
0.0139
LEU 285
THR 286
-0.0000
THR 286
ASP 287
-0.0250
ASP 287
GLU 288
0.0003
GLU 288
GLY 289
0.0072
GLY 289
LEU 290
0.0000
LEU 290
GLU 291
-0.0018
GLU 291
ALA 292
0.0003
ALA 292
VAL 293
0.0008
VAL 293
ASN 294
-0.0001
ASN 294
LYS 295
0.0464
LYS 295
ASP 296
-0.0002
ASP 296
LYS 297
-0.0036
LYS 297
PRO 298
0.0003
PRO 298
LEU 299
-0.0071
LEU 299
GLY 300
-0.0002
GLY 300
ALA 301
-0.0653
ALA 301
VAL 302
-0.0005
VAL 302
ALA 303
-0.0526
ALA 303
LEU 304
-0.0004
LEU 304
LYS 305
0.0123
LYS 305
SER 306
0.0000
SER 306
TYR 307
-0.0036
TYR 307
GLU 308
-0.0001
GLU 308
GLU 309
0.0645
GLU 309
GLU 310
-0.0001
GLU 310
LEU 311
-0.0003
LEU 311
ALA 312
-0.0002
ALA 312
LYS 313
0.0369
LYS 313
ASP 314
-0.0002
ASP 314
PRO 315
-0.0235
PRO 315
ARG 316
-0.0002
ARG 316
ILE 317
-0.1128
ILE 317
ALA 318
0.0001
ALA 318
ALA 319
0.0187
ALA 319
THR 320
0.0003
THR 320
MET 321
-0.0479
MET 321
GLU 322
-0.0001
GLU 322
ASN 323
0.0430
ASN 323
ALA 324
-0.0001
ALA 324
GLN 325
-0.0257
GLN 325
LYS 326
0.0000
LYS 326
GLY 327
-0.0804
GLY 327
GLU 328
-0.0003
GLU 328
ILE 329
-0.0714
ILE 329
MET 330
-0.0001
MET 330
PRO 331
-0.0677
PRO 331
ASN 332
0.0001
ASN 332
ILE 333
0.0530
ILE 333
PRO 334
-0.0003
PRO 334
GLN 335
0.0633
GLN 335
MET 336
0.0000
MET 336
SER 337
-0.0055
SER 337
ALA 338
-0.0002
ALA 338
PHE 339
-0.0553
PHE 339
TRP 340
0.0002
TRP 340
TYR 341
-0.0550
TYR 341
ALA 342
-0.0002
ALA 342
VAL 343
-0.0058
VAL 343
ARG 344
-0.0001
ARG 344
THR 345
-0.0383
THR 345
ALA 346
-0.0002
ALA 346
VAL 347
-0.0292
VAL 347
ILE 348
-0.0002
ILE 348
ASN 349
-0.0835
ASN 349
ALA 350
-0.0001
ALA 350
ALA 351
-0.0636
ALA 351
SER 352
0.0000
SER 352
GLY 353
-0.0523
GLY 353
ARG 354
0.0002
ARG 354
GLN 355
0.0062
GLN 355
THR 356
-0.0005
THR 356
VAL 357
0.0323
VAL 357
ASP 358
-0.0001
ASP 358
GLU 359
0.0246
GLU 359
ALA 360
-0.0003
ALA 360
LEU 361
-0.0001
LEU 361
LYS 362
0.0002
LYS 362
ASP 363
0.0040
ASP 363
ALA 364
-0.0001
ALA 364
GLN 365
-0.0191
GLN 365
THR 366
0.0001
THR 366
ARG 367
-0.0340
ARG 367
ILE 368
-0.0001
ILE 368
THR 369
-0.0284
THR 369
LYS 370
-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.