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
MET 1
LEU 2
-0.0002
LEU 2
SER 3
-0.2609
SER 3
GLN 4
-0.0001
GLN 4
LEU 5
-0.1519
LEU 5
LEU 6
-0.0000
LEU 6
SER 7
-0.0133
SER 7
CYS 8
-0.0004
CYS 8
LEU 9
-0.1798
LEU 9
MET 10
0.0001
MET 10
GLU 11
0.1055
GLU 11
LEU 12
-0.0001
LEU 12
TYR 13
-0.0204
TYR 13
ASN 14
-0.0001
ASN 14
THR 15
-0.0114
THR 15
PRO 16
-0.0003
PRO 16
SER 17
0.0521
SER 17
GLU 18
-0.0002
GLU 18
GLN 19
-0.0309
GLN 19
LEU 20
-0.0001
LEU 20
ASP 21
-0.0046
ASP 21
LYS 22
-0.0002
LYS 22
PHE 23
0.0107
PHE 23
ILE 24
0.0001
ILE 24
TYR 25
0.0077
TYR 25
GLU 26
0.0001
GLU 26
VAL 27
0.0511
VAL 27
LEU 28
0.0002
LEU 28
GLN 29
-0.0688
GLN 29
PRO 30
-0.0004
PRO 30
ASP 31
0.0166
ASP 31
ARG 32
0.0002
ARG 32
THR 33
-0.0184
THR 33
PHE 34
-0.0001
PHE 34
LEU 35
0.0204
LEU 35
GLU 36
-0.0005
GLU 36
GLN 37
0.0033
GLN 37
LEU 38
0.0001
LEU 38
ARG 39
-0.0015
ARG 39
CYS 40
-0.0001
CYS 40
ALA 41
0.0127
ALA 41
VAL 42
0.0000
VAL 42
HIS 43
-0.0221
HIS 43
THR 44
-0.0002
THR 44
ILE 45
0.0144
ILE 45
CYS 46
0.0000
CYS 46
GLU 47
0.0131
GLU 47
PHE 48
-0.0001
PHE 48
LEU 49
0.0153
LEU 49
ARG 50
-0.0000
ARG 50
ASP 51
0.0321
ASP 51
ASN 52
-0.0001
ASN 52
CYS 53
0.0029
CYS 53
PHE 54
-0.0001
PHE 54
ALA 55
0.0603
ALA 55
GLY 56
0.0003
GLY 56
ALA 57
-0.0479
ALA 57
PRO 58
0.0002
PRO 58
PRO 59
-0.0072
PRO 59
PRO 60
-0.0002
PRO 60
ARG 61
-0.0320
ARG 61
THR 62
-0.0001
THR 62
ARG 63
-0.0275
ARG 63
VAL 64
-0.0001
VAL 64
LEU 65
0.0821
LEU 65
LYS 66
-0.0002
LYS 66
VAL 67
-0.0357
VAL 67
VAL 68
-0.0002
VAL 68
LYS 69
-0.0740
LYS 69
GLY 70
-0.0004
GLY 70
GLY 71
-0.0444
GLY 71
SER 72
0.0002
SER 72
ALA 73
0.0287
ALA 73
GLY 74
-0.0004
GLY 74
LYS 75
0.0241
LYS 75
GLY 76
-0.0000
GLY 76
THR 77
-0.0139
THR 77
ALA 78
0.0003
ALA 78
LEU 79
-0.0669
LEU 79
LYS 80
-0.0003
LYS 80
LYS 81
-0.0019
LYS 81
SER 82
-0.0002
SER 82
SER 83
-0.1739
SER 83
ASP 84
-0.0002
ASP 84
ALA 85
-0.1081
ALA 85
ASP 86
0.0001
ASP 86
LEU 87
-0.0660
LEU 87
VAL 88
-0.0001
VAL 88
VAL 89
-0.0320
VAL 89
PHE 90
-0.0002
PHE 90
LEU 91
0.0055
LEU 91
SER 92
0.0001
SER 92
CYS 93
-0.0234
CYS 93
PHE 94
0.0000
PHE 94
GLU 95
0.0096
GLU 95
ASP 96
-0.0004
ASP 96
TYR 97
0.0164
TYR 97
LYS 98
0.0000
LYS 98
ASP 99
0.0144
ASP 99
GLN 100
-0.0002
GLN 100
GLU 101
0.0102
GLU 101
LYS 102
0.0000
LYS 102
ASN 103
-0.0178
ASN 103
ARG 104
-0.0002
ARG 104
ALA 105
0.0058
ALA 105
GLU 106
-0.0002
GLU 106
ILE 107
0.0103
ILE 107
ILE 108
0.0003
ILE 108
ARG 109
0.0010
ARG 109
GLU 110
0.0001
GLU 110
ILE 111
-0.0139
ILE 111
GLN 112
-0.0002
GLN 112
LYS 113
0.0031
LYS 113
ARG 114
0.0001
ARG 114
LEU 115
-0.0469
LEU 115
VAL 116
0.0002
VAL 116
GLU 117
0.0092
GLU 117
CYS 118
-0.0002
CYS 118
GLN 119
-0.0016
GLN 119
GLN 120
0.0000
GLN 120
GLN 121
0.0145
GLN 121
LYS 122
-0.0002
LYS 122
HIS 123
-0.0931
HIS 123
PHE 124
0.0003
PHE 124
GLU 125
-0.0644
GLU 125
VAL 126
-0.0001
VAL 126
GLU 127
0.0188
GLU 127
PHE 128
-0.0001
PHE 128
GLU 129
0.0281
GLU 129
VAL 130
0.0001
VAL 130
SER 131
0.0156
SER 131
ARG 132
0.0002
ARG 132
TRP 133
-0.0217
TRP 133
SER 134
0.0002
SER 134
ASN 135
-0.0244
ASN 135
PRO 136
0.0001
PRO 136
ARG 137
-0.0126
ARG 137
VAL 138
-0.0004
VAL 138
LEU 139
-0.0203
LEU 139
SER 140
-0.0005
SER 140
PHE 141
0.0063
PHE 141
GLN 142
0.0005
GLN 142
LEU 143
0.0100
LEU 143
SER 144
-0.0001
SER 144
SER 145
0.0228
SER 145
LYS 146
-0.0003
LYS 146
THR 147
-0.0441
THR 147
LEU 148
0.0002
LEU 148
HIS 149
0.0217
HIS 149
GLU 150
0.0001
GLU 150
SER 151
-0.1662
SER 151
ILE 152
0.0004
ILE 152
SER 153
-0.0604
SER 153
PHE 154
0.0003
PHE 154
ASP 155
-0.0181
ASP 155
VAL 156
-0.0001
VAL 156
LEU 157
-0.0185
LEU 157
PRO 158
0.0002
PRO 158
ALA 159
-0.0094
ALA 159
TYR 160
-0.0003
TYR 160
ASP 161
-0.0169
ASP 161
ALA 162
-0.0001
ALA 162
LEU 163
-0.0141
LEU 163
HIS 164
-0.0001
HIS 164
HIS 165
0.0328
HIS 165
LEU 166
0.0001
LEU 166
VAL 167
-0.0128
VAL 167
SER 168
0.0001
SER 168
GLY 169
-0.0095
GLY 169
TYR 170
0.0000
TYR 170
LYS 171
-0.0219
LYS 171
VAL 172
-0.0000
VAL 172
ASN 173
-0.0192
ASN 173
PRO 174
0.0003
PRO 174
THR 175
-0.0188
THR 175
VAL 176
0.0003
VAL 176
TYR 177
0.0280
TYR 177
ILE 178
-0.0001
ILE 178
GLN 179
0.0164
GLN 179
LEU 180
0.0003
LEU 180
PHE 181
0.0133
PHE 181
GLN 182
0.0002
GLN 182
GLN 183
-0.0069
GLN 183
CYS 184
0.0000
CYS 184
SER 185
-0.0167
SER 185
ARG 186
-0.0001
ARG 186
GLY 187
0.0407
GLY 187
GLY 188
0.0002
GLY 188
GLU 189
0.0453
GLU 189
PHE 190
0.0001
PHE 190
SER 191
0.0012
SER 191
THR 192
-0.0003
THR 192
CYS 193
-0.0097
CYS 193
PHE 194
0.0002
PHE 194
THR 195
-0.0354
THR 195
GLU 196
0.0003
GLU 196
LEU 197
0.0642
LEU 197
GLN 198
0.0000
GLN 198
ARG 199
0.0001
ARG 199
ASP 200
0.0005
ASP 200
PHE 201
0.0613
PHE 201
ILE 202
-0.0004
ILE 202
ILE 203
0.0028
ILE 203
SER 204
-0.0000
SER 204
ARG 205
0.0090
ARG 205
PRO 206
0.0002
PRO 206
THR 207
-0.0107
THR 207
LYS 208
0.0002
LYS 208
VAL 209
0.0114
VAL 209
LYS 210
0.0004
LYS 210
SER 211
-0.0405
SER 211
LEU 212
-0.0003
LEU 212
ILE 213
0.0027
ILE 213
ARG 214
0.0003
ARG 214
LEU 215
-0.0362
LEU 215
VAL 216
-0.0001
VAL 216
LYS 217
-0.0098
LYS 217
HIS 218
0.0001
HIS 218
TRP 219
-0.0221
TRP 219
TYR 220
-0.0000
TYR 220
LYS 221
-0.0280
LYS 221
THR 222
0.0001
THR 222
TYR 223
-0.0149
TYR 223
ILE 224
-0.0003
ILE 224
CYS 225
-0.0148
CYS 225
PRO 226
0.0003
PRO 226
HIS 227
0.0231
HIS 227
LYS 228
-0.0001
LYS 228
TRP 229
0.0116
TRP 229
ALA 230
-0.0003
ALA 230
LEU 231
-0.0156
LEU 231
ARG 232
0.0000
ARG 232
GLY 233
0.0038
GLY 233
GLY 234
-0.0002
GLY 234
GLU 235
-0.0316
GLU 235
THR 236
-0.0002
THR 236
LEU 237
0.0513
LEU 237
PRO 238
0.0001
PRO 238
PRO 239
0.0363
PRO 239
GLN 240
0.0004
GLN 240
TYR 241
-0.0459
TYR 241
ALA 242
-0.0001
ALA 242
LEU 243
0.0098
LEU 243
GLU 244
-0.0003
GLU 244
LEU 245
-0.0286
LEU 245
LEU 246
-0.0002
LEU 246
THR 247
-0.0049
THR 247
VAL 248
0.0002
VAL 248
TYR 249
-0.0248
TYR 249
ALA 250
0.0002
ALA 250
TRP 251
-0.0084
TRP 251
GLU 252
-0.0001
GLU 252
GLN 253
-0.0060
GLN 253
GLY 254
-0.0001
GLY 254
SER 255
0.0016
SER 255
GLY 256
0.0005
GLY 256
GLU 257
-0.0100
GLU 257
THR 258
0.0002
THR 258
ASN 259
-0.0006
ASN 259
PHE 260
-0.0002
PHE 260
SER 261
0.0202
SER 261
VAL 262
0.0000
VAL 262
ALA 263
-0.0237
ALA 263
LYS 264
-0.0003
LYS 264
ALA 265
0.0153
ALA 265
PHE 266
0.0001
PHE 266
ARG 267
-0.0245
ARG 267
THR 268
0.0000
THR 268
VAL 269
-0.0028
VAL 269
LEU 270
-0.0003
LEU 270
GLU 271
0.0126
GLU 271
LEU 272
0.0000
LEU 272
LEU 273
-0.0384
LEU 273
GLN 274
0.0001
GLN 274
HIS 275
0.0816
HIS 275
TYR 276
0.0000
TYR 276
GLN 277
0.0137
GLN 277
GLN 278
-0.0002
GLN 278
LEU 279
-0.0009
LEU 279
CYS 280
-0.0003
CYS 280
VAL 281
-0.0143
VAL 281
TYR 282
0.0000
TYR 282
TRP 283
-0.0038
TRP 283
THR 284
0.0000
THR 284
VAL 285
-0.0099
VAL 285
ASN 286
0.0000
ASN 286
TYR 287
-0.0080
TYR 287
ASP 288
0.0002
ASP 288
PHE 289
-0.0055
PHE 289
ARG 290
-0.0002
ARG 290
ASP 291
-0.0030
ASP 291
ALA 292
0.0001
ALA 292
THR 293
-0.0131
THR 293
LEU 294
0.0003
LEU 294
SER 295
0.0225
SER 295
CYS 296
-0.0000
CYS 296
HIS 297
-0.0187
HIS 297
LEU 298
0.0001
LEU 298
SER 299
0.0123
SER 299
SER 300
0.0000
SER 300
GLN 301
-0.0035
GLN 301
LEU 302
0.0001
LEU 302
SER 303
-0.0145
SER 303
LYS 304
-0.0000
LYS 304
SER 305
0.0370
SER 305
ARG 306
0.0002
ARG 306
PRO 307
-0.0214
PRO 307
VAL 308
-0.0004
VAL 308
ILE 309
-0.0088
ILE 309
LEU 310
0.0001
LEU 310
ASP 311
0.0074
ASP 311
PRO 312
0.0002
PRO 312
ALA 313
0.0306
ALA 313
ASP 314
0.0004
ASP 314
PRO 315
-0.0028
PRO 315
THR 316
-0.0003
THR 316
ASN 317
0.0081
ASN 317
ILE 318
-0.0004
ILE 318
VAL 319
-0.0570
VAL 319
GLY 320
-0.0001
GLY 320
LYS 321
-0.0057
LYS 321
GLY 322
0.0001
GLY 322
SER 323
-0.0216
SER 323
ARG 324
-0.0000
ARG 324
TRP 325
-0.0529
TRP 325
ASP 326
-0.0005
ASP 326
LEU 327
0.0139
LEU 327
VAL 328
-0.0004
VAL 328
ALA 329
-0.0097
ALA 329
LYS 330
0.0002
LYS 330
GLU 331
0.0295
GLU 331
ALA 332
-0.0000
ALA 332
GLU 333
-0.0150
GLU 333
LYS 334
0.0000
LYS 334
CYS 335
-0.0122
CYS 335
CYS 336
-0.0000
CYS 336
SER 337
0.0339
SER 337
GLN 338
-0.0002
GLN 338
ARG 339
-0.0061
ARG 339
CYS 340
0.0002
CYS 340
CYS 341
0.0227
CYS 341
MET 342
-0.0004
MET 342
TYR 343
-0.0117
TYR 343
SER 344
-0.0004
SER 344
ASN 345
-0.0315
ASN 345
GLY 346
-0.0000
GLY 346
VAL 347
0.0250
VAL 347
PRO 348
0.0002
PRO 348
VAL 349
0.0019
VAL 349
GLN 350
-0.0004
GLN 350
PRO 351
0.0801
PRO 351
TRP 352
-0.0002
TRP 352
ASP 353
0.0494
ASP 353
VAL 354
0.0004
VAL 354
SER 355
0.0630
SER 355
PRO 356
0.0002
PRO 356
GLU 357
0.0453
GLU 357
GLN 358
0.0001
GLN 358
THR 359
0.0196
THR 359
ARG 360
0.0003
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.