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
LEU 1
TRP 2
-0.0001
TRP 2
VAL 3
-0.0867
VAL 3
THR 4
0.0000
THR 4
VAL 5
-0.0796
VAL 5
TYR 6
-0.0000
TYR 6
TYR 7
-0.1201
TYR 7
GLY 8
-0.0000
GLY 8
VAL 9
0.1540
VAL 9
PRO 10
0.0003
PRO 10
VAL 11
0.0448
VAL 11
TRP 12
0.0003
TRP 12
LYS 13
0.1299
LYS 13
GLU 14
-0.0005
GLU 14
ALA 15
-0.0250
ALA 15
THR 16
0.0003
THR 16
THR 17
-0.0329
THR 17
THR 18
0.0001
THR 18
LEU 19
-0.0547
LEU 19
PHE 20
0.0002
PHE 20
CYS 21
-0.0191
CYS 21
ALA 22
-0.0003
ALA 22
SER 23
-0.0494
SER 23
ASP 24
0.0005
ASP 24
ALA 25
-0.0905
ALA 25
LYS 26
-0.0001
LYS 26
ALA 27
0.0095
ALA 27
TYR 28
0.0001
TYR 28
ASP 29
0.0223
ASP 29
THR 30
-0.0003
THR 30
GLU 31
-0.0108
GLU 31
VAL 32
0.0002
VAL 32
HIS 33
-0.0086
HIS 33
ASN 34
-0.0001
ASN 34
VAL 35
-0.0116
VAL 35
TRP 36
-0.0002
TRP 36
ALA 37
-0.0158
ALA 37
THR 38
0.0002
THR 38
HIS 39
-0.0048
HIS 39
ALA 40
-0.0002
ALA 40
CYS 41
0.0263
CYS 41
VAL 42
0.0001
VAL 42
PRO 43
-0.0305
PRO 43
THR 44
0.0003
THR 44
ASP 45
-0.0617
ASP 45
PRO 46
0.0002
PRO 46
ASN 47
-0.0478
ASN 47
PRO 48
0.0000
PRO 48
GLN 49
-0.0626
GLN 49
GLU 50
-0.0001
GLU 50
VAL 51
-0.0324
VAL 51
VAL 52
-0.0002
VAL 52
LEU 53
0.0045
LEU 53
VAL 54
0.0003
VAL 54
ASN 55
-0.0011
ASN 55
VAL 56
0.0004
VAL 56
THR 57
0.0663
THR 57
GLU 58
0.0002
GLU 58
ASN 59
0.1314
ASN 59
PHE 60
-0.0004
PHE 60
ASN 61
0.1331
ASN 61
MET 62
0.0003
MET 62
TRP 63
-0.0061
TRP 63
LYS 64
0.0001
LYS 64
ASN 65
0.0270
ASN 65
ASP 66
-0.0004
ASP 66
MET 67
-0.0243
MET 67
VAL 68
-0.0000
VAL 68
GLU 69
-0.0272
GLU 69
GLN 70
0.0002
GLN 70
MET 71
-0.0187
MET 71
HIS 72
-0.0000
HIS 72
GLU 73
-0.0438
GLU 73
ASP 74
0.0001
ASP 74
ILE 75
0.0079
ILE 75
ILE 76
-0.0003
ILE 76
SER 77
-0.0488
SER 77
LEU 78
-0.0000
LEU 78
TRP 79
0.0001
TRP 79
ASP 80
0.0000
ASP 80
GLN 81
-0.0555
GLN 81
SER 82
-0.0002
SER 82
LEU 83
-0.0655
LEU 83
LYS 84
-0.0002
LYS 84
PRO 85
-0.0633
PRO 85
CYS 86
-0.0001
CYS 86
VAL 87
-0.0724
VAL 87
LYS 88
-0.0004
LYS 88
LEU 89
-0.0277
LEU 89
THR 90
0.0000
THR 90
GLY 91
-0.0098
GLY 91
GLY 92
-0.0003
GLY 92
SER 93
-0.0400
SER 93
VAL 94
-0.0000
VAL 94
ILE 95
-0.0065
ILE 95
THR 96
0.0001
THR 96
GLN 97
-0.0152
GLN 97
ALA 98
-0.0000
ALA 98
CYS 99
-0.0796
CYS 99
PRO 100
0.0002
PRO 100
LYS 101
-0.0845
LYS 101
VAL 102
0.0005
VAL 102
SER 103
-0.1641
SER 103
PHE 104
0.0000
PHE 104
GLU 105
-0.1159
GLU 105
PRO 106
-0.0002
PRO 106
ILE 107
-0.0886
ILE 107
PRO 108
0.0000
PRO 108
ILE 109
-0.0401
ILE 109
HIS 110
-0.0001
HIS 110
TYR 111
-0.0587
TYR 111
CYS 112
0.0003
CYS 112
ALA 113
-0.0849
ALA 113
PRO 114
-0.0003
PRO 114
ALA 115
0.0736
ALA 115
GLY 116
-0.0001
GLY 116
PHE 117
0.0758
PHE 117
ALA 118
-0.0003
ALA 118
ILE 119
0.0193
ILE 119
LEU 120
0.0002
LEU 120
LYS 121
-0.0278
LYS 121
CYS 122
-0.0004
CYS 122
ASN 123
-0.0074
ASN 123
ASN 124
0.0004
ASN 124
LYS 125
-0.0903
LYS 125
THR 126
-0.0002
THR 126
PHE 127
0.0355
PHE 127
ASN 128
0.0001
ASN 128
GLY 129
-0.0159
GLY 129
THR 130
-0.0003
THR 130
GLY 131
0.0725
GLY 131
PRO 132
0.0000
PRO 132
CYS 133
-0.0213
CYS 133
THR 134
0.0000
THR 134
ASN 135
0.0007
ASN 135
VAL 136
0.0000
VAL 136
SER 137
-0.0161
SER 137
THR 138
0.0003
THR 138
VAL 139
-0.0225
VAL 139
GLN 140
0.0001
GLN 140
CYS 141
-0.0790
CYS 141
THR 142
-0.0003
THR 142
HIS 143
-0.0608
HIS 143
GLY 144
-0.0001
GLY 144
ILE 145
-0.0156
ILE 145
ARG 146
0.0004
ARG 146
PRO 147
0.0127
PRO 147
VAL 148
-0.0001
VAL 148
VAL 149
-0.0029
VAL 149
SER 150
0.0002
SER 150
SER 151
-0.0357
SER 151
GLN 152
-0.0001
GLN 152
LEU 153
0.0119
LEU 153
LEU 154
-0.0003
LEU 154
LEU 155
0.0194
LEU 155
ASN 156
-0.0005
ASN 156
GLY 157
-0.0294
GLY 157
SER 158
-0.0001
SER 158
LEU 159
-0.0410
LEU 159
ALA 160
-0.0004
ALA 160
GLU 161
0.0590
GLU 161
GLU 162
-0.0000
GLU 162
GLU 163
-0.0682
GLU 163
VAL 164
-0.0002
VAL 164
VAL 165
0.0078
VAL 165
ILE 166
-0.0001
ILE 166
ARG 167
0.0426
ARG 167
SER 168
0.0004
SER 168
VAL 169
-0.0805
VAL 169
ASN 170
0.0002
ASN 170
PHE 171
0.1150
PHE 171
THR 172
-0.0002
THR 172
ASP 173
-0.0754
ASP 173
ASN 174
0.0001
ASN 174
ALA 175
0.0173
ALA 175
LYS 176
-0.0002
LYS 176
THR 177
0.0518
THR 177
ILE 178
-0.0001
ILE 178
ILE 179
-0.0004
ILE 179
VAL 180
0.0005
VAL 180
GLN 181
-0.0038
GLN 181
LEU 182
0.0001
LEU 182
ASN 183
0.0138
ASN 183
THR 184
-0.0000
THR 184
SER 185
-0.0859
SER 185
VAL 186
-0.0003
VAL 186
GLU 187
-0.1311
GLU 187
ILE 188
-0.0001
ILE 188
ASN 189
-0.0761
ASN 189
CYS 190
0.0001
CYS 190
THR 191
-0.0278
THR 191
GLY 192
0.0003
GLY 192
ALA 193
0.0002
ALA 193
GLY 194
0.0003
GLY 194
HIS 195
-0.0597
HIS 195
CYS 196
0.0004
CYS 196
ASN 197
-0.0747
ASN 197
ILE 198
0.0002
ILE 198
ALA 199
-0.0780
ALA 199
ARG 200
-0.0000
ARG 200
ALA 201
-0.0383
ALA 201
LYS 202
-0.0001
LYS 202
TRP 203
0.0550
TRP 203
ASN 204
0.0001
ASN 204
ASN 205
0.0191
ASN 205
THR 206
-0.0001
THR 206
LEU 207
-0.0223
LEU 207
LYS 208
0.0002
LYS 208
GLN 209
0.0022
GLN 209
ILE 210
0.0002
ILE 210
ALA 211
-0.0299
ALA 211
SER 212
-0.0004
SER 212
LYS 213
0.0104
LYS 213
LEU 214
0.0002
LEU 214
ARG 215
0.0361
ARG 215
GLU 216
-0.0002
GLU 216
GLN 217
-0.0157
GLN 217
PHE 218
-0.0001
PHE 218
GLY 219
0.0848
GLY 219
ASN 220
0.0003
ASN 220
ASN 221
-0.0329
ASN 221
LYS 222
-0.0002
LYS 222
THR 223
0.0008
THR 223
ILE 224
0.0003
ILE 224
ILE 225
0.0207
ILE 225
PHE 226
-0.0002
PHE 226
LYS 227
0.0368
LYS 227
GLN 228
0.0003
GLN 228
SER 229
0.0365
SER 229
SER 230
0.0004
SER 230
GLY 231
0.2249
GLY 231
GLY 232
-0.0000
GLY 232
ASP 233
0.2055
ASP 233
PRO 234
0.0002
PRO 234
GLU 235
0.0076
GLU 235
ILE 236
0.0001
ILE 236
VAL 237
0.0207
VAL 237
THR 238
-0.0001
THR 238
HIS 239
-0.0380
HIS 239
TRP 240
0.0000
TRP 240
PHE 241
-0.0141
PHE 241
ASN 242
0.0001
ASN 242
CYS 243
0.0563
CYS 243
GLY 244
-0.0002
GLY 244
GLY 245
-0.0481
GLY 245
GLU 246
-0.0003
GLU 246
PHE 247
0.0325
PHE 247
PHE 248
-0.0001
PHE 248
TYR 249
0.0182
TYR 249
CYS 250
0.0001
CYS 250
ASN 251
-0.0314
ASN 251
SER 252
-0.0002
SER 252
THR 253
-0.0289
THR 253
GLN 254
-0.0004
GLN 254
LEU 255
-0.0082
LEU 255
PHE 256
0.0001
PHE 256
ASN 257
0.0120
ASN 257
SER 258
-0.0001
SER 258
THR 259
-0.0538
THR 259
TRP 260
-0.0001
TRP 260
PHE 261
0.0293
PHE 261
ASN 262
0.0000
ASN 262
SER 263
-0.1074
SER 263
THR 264
-0.0000
THR 264
GLU 265
-0.0732
GLU 265
GLY 266
-0.0000
GLY 266
SER 267
-0.0904
SER 267
ASP 268
0.0001
ASP 268
THR 269
-0.0865
THR 269
ILE 270
0.0000
ILE 270
THR 271
-0.0724
THR 271
LEU 272
0.0003
LEU 272
PRO 273
-0.0608
PRO 273
CYS 274
0.0000
CYS 274
ARG 275
-0.1133
ARG 275
ILE 276
-0.0000
ILE 276
LYS 277
-0.1592
LYS 277
GLN 278
-0.0002
GLN 278
ILE 279
-0.0201
ILE 279
ILE 280
-0.0001
ILE 280
ASN 281
0.0131
ASN 281
MET 282
-0.0004
MET 282
TRP 283
0.2764
TRP 283
GLN 284
0.0001
GLN 284
LYS 285
0.1497
LYS 285
VAL 286
-0.0002
VAL 286
GLY 287
-0.1059
GLY 287
LYS 288
0.0002
LYS 288
ALA 289
-0.0265
ALA 289
MET 290
0.0000
MET 290
TYR 291
-0.0961
TYR 291
ALA 292
0.0000
ALA 292
PRO 293
-0.0318
PRO 293
PRO 294
-0.0001
PRO 294
ILE 295
0.0688
ILE 295
SER 296
0.0002
SER 296
GLY 297
-0.0267
GLY 297
GLN 298
-0.0001
GLN 298
ILE 299
0.0777
ILE 299
ARG 300
0.0001
ARG 300
CYS 301
-0.0491
CYS 301
SER 302
-0.0003
SER 302
SER 303
-0.0228
SER 303
ASN 304
-0.0005
ASN 304
ILE 305
-0.0013
ILE 305
THR 306
-0.0001
THR 306
GLY 307
-0.0107
GLY 307
LEU 308
-0.0000
LEU 308
LEU 309
0.0268
LEU 309
LEU 310
0.0002
LEU 310
THR 311
0.0151
THR 311
ARG 312
0.0001
ARG 312
ASP 313
0.0816
ASP 313
GLY 314
0.0000
GLY 314
GLY 315
0.1670
GLY 315
ASN 316
-0.0002
ASN 316
SER 317
0.0057
SER 317
ASN 318
0.0002
ASN 318
ASN 319
-0.0889
ASN 319
GLU 320
0.0000
GLU 320
SER 321
0.0547
SER 321
GLU 322
0.0001
GLU 322
ILE 323
0.0685
ILE 323
PHE 324
0.0000
PHE 324
ARG 325
0.0992
ARG 325
PRO 326
0.0003
PRO 326
GLY 327
0.0821
GLY 327
GLY 328
0.0004
GLY 328
GLY 329
0.1409
GLY 329
ASP 330
0.0004
ASP 330
MET 331
-0.0163
MET 331
ARG 332
0.0003
ARG 332
ASP 333
0.0882
ASP 333
ASN 334
-0.0002
ASN 334
TRP 335
0.0098
TRP 335
ARG 336
-0.0001
ARG 336
SER 337
-0.0084
SER 337
GLU 338
0.0002
GLU 338
LEU 339
-0.0415
LEU 339
TYR 340
-0.0001
TYR 340
LYS 341
0.0329
LYS 341
TYR 342
0.0002
TYR 342
LYS 343
-0.0590
LYS 343
VAL 344
-0.0000
VAL 344
VAL 345
0.0954
VAL 345
LYS 346
-0.0000
LYS 346
ILE 347
0.1079
ILE 347
GLU 348
0.0004
GLU 348
PRO 349
0.0826
PRO 349
LEU 350
0.0001
LEU 350
GLY 351
0.0273
GLY 351
VAL 352
-0.0003
VAL 352
ALA 353
0.0474
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.