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
0.0003
ILE 2
GLU 3
0.0029
GLU 3
GLU 4
-0.0001
GLU 4
GLY 5
0.0162
GLY 5
LYS 6
-0.0000
LYS 6
LEU 7
-0.0134
LEU 7
VAL 8
-0.0005
VAL 8
ILE 9
-0.0388
ILE 9
TRP 10
0.0003
TRP 10
ILE 11
-0.0785
ILE 11
ASN 12
0.0001
ASN 12
GLY 13
0.0573
GLY 13
ASP 14
-0.0001
ASP 14
LYS 15
-0.1124
LYS 15
GLY 16
0.0000
GLY 16
TYR 17
-0.0194
TYR 17
ASN 18
0.0001
ASN 18
GLY 19
0.0399
GLY 19
LEU 20
-0.0003
LEU 20
ALA 21
0.0071
ALA 21
GLU 22
-0.0001
GLU 22
VAL 23
-0.0284
VAL 23
GLY 24
0.0000
GLY 24
LYS 25
0.0276
LYS 25
LYS 26
-0.0002
LYS 26
PHE 27
0.0019
PHE 27
GLU 28
-0.0001
GLU 28
LYS 29
0.0058
LYS 29
ASP 30
-0.0001
ASP 30
THR 31
-0.0003
THR 31
GLY 32
-0.0001
GLY 32
ILE 33
-0.0131
ILE 33
LYS 34
0.0000
LYS 34
VAL 35
-0.0325
VAL 35
THR 36
0.0003
THR 36
VAL 37
-0.0861
VAL 37
GLU 38
0.0001
GLU 38
HIS 39
-0.0730
HIS 39
PRO 40
0.0001
PRO 40
ASP 41
-0.0291
ASP 41
LYS 42
-0.0002
LYS 42
LEU 43
0.0861
LEU 43
GLU 44
0.0004
GLU 44
GLU 45
0.0122
GLU 45
LYS 46
0.0001
LYS 46
PHE 47
-0.0113
PHE 47
PRO 48
-0.0003
PRO 48
GLN 49
0.0036
GLN 49
VAL 50
0.0002
VAL 50
ALA 51
0.0021
ALA 51
ALA 52
0.0003
ALA 52
THR 53
0.0099
THR 53
GLY 54
-0.0003
GLY 54
ASP 55
0.0069
ASP 55
GLY 56
0.0001
GLY 56
PRO 57
0.0149
PRO 57
ASP 58
-0.0002
ASP 58
ILE 59
-0.0029
ILE 59
ILE 60
-0.0003
ILE 60
PHE 61
-0.0226
PHE 61
TRP 62
-0.0002
TRP 62
ALA 63
0.0150
ALA 63
HIS 64
0.0001
HIS 64
ASP 65
-0.0308
ASP 65
ARG 66
-0.0002
ARG 66
PHE 67
-0.1683
PHE 67
GLY 68
-0.0001
GLY 68
GLY 69
0.0046
GLY 69
TYR 70
-0.0001
TYR 70
ALA 71
-0.0113
ALA 71
GLN 72
-0.0002
GLN 72
SER 73
0.0151
SER 73
GLY 74
0.0002
GLY 74
LEU 75
0.0049
LEU 75
LEU 76
-0.0004
LEU 76
ALA 77
-0.0279
ALA 77
GLU 78
0.0002
GLU 78
ILE 79
-0.0128
ILE 79
THR 80
0.0002
THR 80
PRO 81
-0.0009
PRO 81
ASP 82
0.0001
ASP 82
LYS 83
-0.0148
LYS 83
ALA 84
0.0004
ALA 84
PHE 85
-0.0347
PHE 85
GLN 86
-0.0003
GLN 86
ASP 87
-0.0146
ASP 87
LYS 88
0.0000
LYS 88
LEU 89
0.0217
LEU 89
TYR 90
-0.0001
TYR 90
PRO 91
-0.0715
PRO 91
PHE 92
0.0003
PHE 92
THR 93
0.0089
THR 93
TRP 94
-0.0002
TRP 94
ASP 95
0.0268
ASP 95
ALA 96
0.0000
ALA 96
VAL 97
0.0780
VAL 97
ARG 98
-0.0000
ARG 98
TYR 99
-0.0606
TYR 99
ASN 100
0.0002
ASN 100
GLY 101
-0.0040
GLY 101
LYS 102
-0.0000
LYS 102
LEU 103
-0.0208
LEU 103
ILE 104
-0.0001
ILE 104
ALA 105
-0.0026
ALA 105
TYR 106
0.0003
TYR 106
PRO 107
0.0291
PRO 107
ILE 108
0.0002
ILE 108
ALA 109
0.0799
ALA 109
VAL 110
-0.0002
VAL 110
GLU 111
0.0772
GLU 111
ALA 112
0.0000
ALA 112
LEU 113
0.0839
LEU 113
SER 114
-0.0003
SER 114
LEU 115
0.0292
LEU 115
ILE 116
-0.0000
ILE 116
TYR 117
-0.0262
TYR 117
ASN 118
-0.0002
ASN 118
LYS 119
0.0011
LYS 119
ASP 120
-0.0001
ASP 120
LEU 121
0.0062
LEU 121
LEU 122
0.0001
LEU 122
PRO 123
0.0181
PRO 123
ASN 124
0.0001
ASN 124
PRO 125
-0.0155
PRO 125
PRO 126
-0.0000
PRO 126
LYS 127
-0.0279
LYS 127
THR 128
0.0002
THR 128
TRP 129
-0.0224
TRP 129
GLU 130
0.0000
GLU 130
GLU 131
-0.0113
GLU 131
ILE 132
-0.0003
ILE 132
PRO 133
0.0201
PRO 133
ALA 134
0.0002
ALA 134
LEU 135
-0.0058
LEU 135
ASP 136
0.0001
ASP 136
LYS 137
-0.0040
LYS 137
GLU 138
-0.0003
GLU 138
LEU 139
-0.0140
LEU 139
LYS 140
-0.0002
LYS 140
ALA 141
-0.0004
ALA 141
LYS 142
0.0000
LYS 142
GLY 143
-0.0172
GLY 143
LYS 144
-0.0001
LYS 144
SER 145
0.0204
SER 145
ALA 146
-0.0003
ALA 146
LEU 147
-0.0194
LEU 147
MET 148
-0.0005
MET 148
PHE 149
-0.0204
PHE 149
ASN 150
-0.0002
ASN 150
LEU 151
0.0038
LEU 151
GLN 152
0.0000
GLN 152
GLU 153
-0.0702
GLU 153
PRO 154
-0.0001
PRO 154
TYR 155
-0.0103
TYR 155
PHE 156
0.0006
PHE 156
THR 157
-0.0584
THR 157
TRP 158
-0.0001
TRP 158
PRO 159
-0.0044
PRO 159
LEU 160
0.0001
LEU 160
ILE 161
-0.0077
ILE 161
ALA 162
-0.0001
ALA 162
ALA 163
-0.0202
ALA 163
ASP 164
-0.0002
ASP 164
GLY 165
-0.0559
GLY 165
GLY 166
-0.0000
GLY 166
TYR 167
-0.0112
TYR 167
ALA 168
-0.0006
ALA 168
PHE 169
-0.0422
PHE 169
LYS 170
0.0001
LYS 170
TYR 171
-0.0238
TYR 171
GLU 172
-0.0003
GLU 172
ASN 173
-0.0239
ASN 173
GLY 174
0.0002
GLY 174
LYS 175
0.0341
LYS 175
TYR 176
-0.0003
TYR 176
ASP 177
-0.0080
ASP 177
ILE 178
-0.0004
ILE 178
LYS 179
0.0077
LYS 179
ASP 180
0.0000
ASP 180
VAL 181
-0.0094
VAL 181
GLY 182
0.0002
GLY 182
VAL 183
0.0005
VAL 183
ASP 184
0.0000
ASP 184
ASN 185
-0.0199
ASN 185
ALA 186
0.0001
ALA 186
GLY 187
-0.0013
GLY 187
ALA 188
-0.0001
ALA 188
LYS 189
0.0201
LYS 189
ALA 190
-0.0001
ALA 190
GLY 191
0.0026
GLY 191
LEU 192
0.0000
LEU 192
THR 193
-0.0067
THR 193
PHE 194
-0.0001
PHE 194
LEU 195
-0.0195
LEU 195
VAL 196
-0.0004
VAL 196
ASP 197
-0.0173
ASP 197
LEU 198
-0.0002
LEU 198
ILE 199
0.0133
ILE 199
LYS 200
0.0000
LYS 200
ASN 201
-0.0099
ASN 201
LYS 202
0.0001
LYS 202
HIS 203
0.0031
HIS 203
MET 204
0.0003
MET 204
ASN 205
0.0183
ASN 205
ALA 206
0.0002
ALA 206
ASP 207
-0.0135
ASP 207
THR 208
0.0000
THR 208
ASP 209
-0.1170
ASP 209
TYR 210
0.0000
TYR 210
SER 211
-0.0067
SER 211
ILE 212
-0.0002
ILE 212
ALA 213
0.0170
ALA 213
GLU 214
-0.0002
GLU 214
ALA 215
-0.0459
ALA 215
ALA 216
-0.0003
ALA 216
PHE 217
0.0317
PHE 217
ASN 218
-0.0000
ASN 218
LYS 219
-0.0701
LYS 219
GLY 220
-0.0002
GLY 220
GLU 221
-0.0076
GLU 221
THR 222
0.0001
THR 222
ALA 223
0.0141
ALA 223
MET 224
0.0003
MET 224
THR 225
-0.0487
THR 225
ILE 226
0.0001
ILE 226
ASN 227
-0.1153
ASN 227
GLY 228
0.0002
GLY 228
PRO 229
-0.0076
PRO 229
TRP 230
0.0000
TRP 230
ALA 231
-0.0073
ALA 231
TRP 232
0.0001
TRP 232
SER 233
-0.0378
SER 233
ASN 234
0.0003
ASN 234
ILE 235
-0.0552
ILE 235
ASP 236
-0.0000
ASP 236
THR 237
-0.0150
THR 237
SER 238
0.0000
SER 238
LYS 239
-0.0113
LYS 239
VAL 240
-0.0002
VAL 240
ASN 241
0.0000
ASN 241
TYR 242
0.0003
TYR 242
GLY 243
0.0026
GLY 243
VAL 244
0.0001
VAL 244
THR 245
-0.0343
THR 245
VAL 246
-0.0001
VAL 246
LEU 247
0.0846
LEU 247
PRO 248
-0.0002
PRO 248
THR 249
-0.0363
THR 249
PHE 250
0.0004
PHE 250
LYS 251
-0.0103
LYS 251
GLY 252
0.0003
GLY 252
GLN 253
0.0247
GLN 253
PRO 254
-0.0001
PRO 254
SER 255
-0.0180
SER 255
LYS 256
-0.0001
LYS 256
PRO 257
0.0095
PRO 257
PHE 258
-0.0000
PHE 258
VAL 259
0.0928
VAL 259
GLY 260
0.0000
GLY 260
VAL 261
0.0270
VAL 261
LEU 262
-0.0000
LEU 262
SER 263
0.0060
SER 263
ALA 264
-0.0002
ALA 264
GLY 265
0.0171
GLY 265
ILE 266
0.0002
ILE 266
ASN 267
0.0171
ASN 267
ALA 268
-0.0004
ALA 268
ALA 269
0.0144
ALA 269
SER 270
-0.0003
SER 270
PRO 271
-0.0087
PRO 271
ASN 272
-0.0002
ASN 272
LYS 273
0.0250
LYS 273
GLU 274
0.0001
GLU 274
LEU 275
-0.0088
LEU 275
ALA 276
-0.0001
ALA 276
LYS 277
0.0029
LYS 277
GLU 278
-0.0001
GLU 278
PHE 279
-0.0372
PHE 279
LEU 280
-0.0000
LEU 280
GLU 281
-0.0141
GLU 281
ASN 282
0.0002
ASN 282
TYR 283
-0.0280
TYR 283
LEU 284
0.0002
LEU 284
LEU 285
0.0350
LEU 285
THR 286
0.0000
THR 286
ASP 287
0.0644
ASP 287
GLU 288
0.0000
GLU 288
GLY 289
0.0233
GLY 289
LEU 290
-0.0001
LEU 290
GLU 291
-0.0154
GLU 291
ALA 292
-0.0005
ALA 292
VAL 293
0.0085
VAL 293
ASN 294
-0.0003
ASN 294
LYS 295
0.0204
LYS 295
ASP 296
-0.0003
ASP 296
LYS 297
-0.0300
LYS 297
PRO 298
-0.0002
PRO 298
LEU 299
-0.0349
LEU 299
GLY 300
-0.0001
GLY 300
ALA 301
0.0168
ALA 301
VAL 302
-0.0004
VAL 302
ALA 303
0.0002
ALA 303
LEU 304
-0.0001
LEU 304
LYS 305
0.0154
LYS 305
SER 306
-0.0000
SER 306
TYR 307
-0.0537
TYR 307
GLU 308
-0.0002
GLU 308
GLU 309
-0.0085
GLU 309
GLU 310
-0.0003
GLU 310
LEU 311
0.0137
LEU 311
ALA 312
0.0002
ALA 312
LYS 313
0.0098
LYS 313
ASP 314
-0.0000
ASP 314
PRO 315
0.0903
PRO 315
ARG 316
-0.0001
ARG 316
ILE 317
0.0618
ILE 317
ALA 318
0.0003
ALA 318
ALA 319
0.1684
ALA 319
THR 320
-0.0000
THR 320
MET 321
-0.0392
MET 321
GLU 322
0.0005
GLU 322
ASN 323
0.0151
ASN 323
ALA 324
0.0003
ALA 324
GLN 325
-0.0089
GLN 325
LYS 326
-0.0002
LYS 326
GLY 327
-0.0032
GLY 327
GLU 328
-0.0001
GLU 328
ILE 329
0.2397
ILE 329
MET 330
0.0003
MET 330
PRO 331
0.0427
PRO 331
ASN 332
-0.0002
ASN 332
ILE 333
0.0105
ILE 333
PRO 334
0.0002
PRO 334
GLN 335
-0.0550
GLN 335
MET 336
0.0004
MET 336
SER 337
0.0138
SER 337
ALA 338
-0.0004
ALA 338
PHE 339
-0.0083
PHE 339
TRP 340
-0.0000
TRP 340
TYR 341
0.0097
TYR 341
ALA 342
-0.0001
ALA 342
VAL 343
0.0186
VAL 343
ARG 344
0.0001
ARG 344
THR 345
-0.0256
THR 345
ALA 346
-0.0001
ALA 346
VAL 347
0.0336
VAL 347
ILE 348
-0.0004
ILE 348
ASN 349
0.0003
ASN 349
ALA 350
0.0005
ALA 350
ALA 351
0.0205
ALA 351
SER 352
0.0001
SER 352
GLY 353
0.0023
GLY 353
ARG 354
-0.0004
ARG 354
GLN 355
0.0280
GLN 355
THR 356
0.0001
THR 356
VAL 357
0.0302
VAL 357
ASP 358
-0.0004
ASP 358
GLU 359
0.0072
GLU 359
ALA 360
-0.0002
ALA 360
LEU 361
0.0195
LEU 361
LYS 362
-0.0004
LYS 362
ASP 363
-0.0143
ASP 363
ALA 364
0.0002
ALA 364
GLN 365
0.0118
GLN 365
THR 366
0.0004
THR 366
ARG 367
-0.0146
ARG 367
ILE 368
-0.0003
ILE 368
THR 369
0.0058
THR 369
LYS 370
-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: April 8th, 2025.