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
GLU 2
0.0001
GLU 2
LEU 3
-0.0193
LEU 3
ARG 4
0.0001
ARG 4
HIS 5
0.0033
HIS 5
THR 6
0.0001
THR 6
PRO 7
-0.0127
PRO 7
ALA 8
-0.0002
ALA 8
ARG 9
0.0123
ARG 9
ASP 10
0.0002
ASP 10
LEU 11
-0.0053
LEU 11
ASP 12
0.0002
ASP 12
LYS 13
-0.0136
LYS 13
PHE 14
0.0002
PHE 14
ILE 15
-0.0175
ILE 15
GLU 16
0.0002
GLU 16
ASP 17
0.0257
ASP 17
HIS 18
0.0001
HIS 18
LEU 19
-0.0003
LEU 19
LEU 20
-0.0001
LEU 20
PRO 21
-0.0213
PRO 21
ASN 22
-0.0003
ASN 22
THR 23
-0.0047
THR 23
CYS 24
0.0003
CYS 24
PHE 25
-0.0048
PHE 25
ARG 26
0.0003
ARG 26
THR 27
0.0931
THR 27
GLN 28
0.0000
GLN 28
VAL 29
-0.0216
VAL 29
LYS 30
0.0001
LYS 30
GLU 31
0.0207
GLU 31
ALA 32
0.0003
ALA 32
ILE 33
-0.0257
ILE 33
ASP 34
0.0000
ASP 34
ILE 35
0.0734
ILE 35
VAL 36
-0.0002
VAL 36
CYS 37
-0.0280
CYS 37
ARG 38
0.0001
ARG 38
PHE 39
0.0561
PHE 39
LEU 40
-0.0002
LEU 40
LYS 41
-0.0061
LYS 41
GLU 42
0.0000
GLU 42
ARG 43
0.0666
ARG 43
CYS 44
0.0002
CYS 44
PHE 45
-0.0150
PHE 45
GLN 46
-0.0001
GLN 46
GLY 47
0.0171
GLY 47
THR 48
-0.0002
THR 48
ALA 49
0.0395
ALA 49
ASP 50
0.0001
ASP 50
PRO 51
-0.0265
PRO 51
VAL 52
-0.0002
VAL 52
ARG 53
-0.0064
ARG 53
VAL 54
0.0000
VAL 54
SER 55
0.0198
SER 55
LYS 56
-0.0000
LYS 56
VAL 57
0.0102
VAL 57
VAL 58
0.0001
VAL 58
LYS 59
0.0323
LYS 59
GLY 60
0.0004
GLY 60
GLY 61
0.0664
GLY 61
SER 62
-0.0000
SER 62
SER 63
0.0950
SER 63
GLY 64
-0.0001
GLY 64
LYS 65
0.0050
LYS 65
GLY 66
-0.0000
GLY 66
THR 67
0.0124
THR 67
THR 68
0.0002
THR 68
LEU 69
-0.0087
LEU 69
ARG 70
0.0001
ARG 70
GLY 71
-0.0296
GLY 71
ARG 72
-0.0001
ARG 72
SER 73
0.0091
SER 73
ASP 74
0.0001
ASP 74
ALA 75
0.0561
ALA 75
ASP 76
0.0002
ASP 76
LEU 77
0.0342
LEU 77
VAL 78
-0.0002
VAL 78
VAL 79
0.0067
VAL 79
PHE 80
-0.0001
PHE 80
LEU 81
0.0142
LEU 81
THR 82
0.0001
THR 82
LYS 83
-0.0255
LYS 83
LEU 84
-0.0002
LEU 84
THR 85
0.0117
THR 85
SER 86
-0.0002
SER 86
PHE 87
0.0168
PHE 87
GLU 88
-0.0001
GLU 88
ASP 89
0.0032
ASP 89
GLN 90
0.0002
GLN 90
LEU 91
0.0032
LEU 91
ARG 92
-0.0000
ARG 92
ARG 93
0.0060
ARG 93
ARG 94
-0.0002
ARG 94
GLY 95
0.0207
GLY 95
GLU 96
-0.0002
GLU 96
PHE 97
0.0211
PHE 97
ILE 98
0.0000
ILE 98
GLN 99
-0.0422
GLN 99
GLU 100
-0.0000
GLU 100
ILE 101
-0.0170
ILE 101
ARG 102
0.0002
ARG 102
ARG 103
0.0496
ARG 103
GLN 104
0.0001
GLN 104
LEU 105
-0.0262
LEU 105
GLU 106
0.0001
GLU 106
ALA 107
0.0196
ALA 107
CYS 108
-0.0001
CYS 108
GLN 109
-0.0170
GLN 109
ARG 110
0.0001
ARG 110
GLU 111
-0.0058
GLU 111
GLN 112
0.0001
GLN 112
LYS 113
0.0131
LYS 113
PHE 114
0.0003
PHE 114
LYS 115
-0.0045
LYS 115
VAL 116
-0.0002
VAL 116
THR 117
0.0232
THR 117
PHE 118
0.0001
PHE 118
GLU 119
0.1237
GLU 119
VAL 120
0.0000
VAL 120
GLN 121
0.0820
GLN 121
SER 122
-0.0001
SER 122
PRO 123
-0.2713
PRO 123
ARG 124
0.0000
ARG 124
ARG 125
-0.0887
ARG 125
GLU 126
-0.0000
GLU 126
ASN 127
0.1631
ASN 127
PRO 128
-0.0001
PRO 128
ARG 129
-0.1242
ARG 129
ALA 130
-0.0001
ALA 130
LEU 131
0.0640
LEU 131
SER 132
0.0002
SER 132
PHE 133
0.0731
PHE 133
VAL 134
0.0002
VAL 134
LEU 135
-0.0589
LEU 135
SER 136
-0.0004
SER 136
SER 137
-0.0183
SER 137
PRO 138
0.0003
PRO 138
GLN 139
0.0106
GLN 139
LEU 140
0.0001
LEU 140
GLN 141
-0.0050
GLN 141
GLN 142
0.0001
GLN 142
GLU 143
-0.0277
GLU 143
VAL 144
-0.0003
VAL 144
GLU 145
-0.0465
GLU 145
PHE 146
-0.0002
PHE 146
ASP 147
0.0555
ASP 147
VAL 148
-0.0000
VAL 148
LEU 149
0.0411
LEU 149
PRO 150
-0.0000
PRO 150
ALA 151
0.0113
ALA 151
PHE 152
0.0000
PHE 152
ASP 153
-0.0288
ASP 153
ALA 154
0.0001
ALA 154
LEU 155
-0.0584
LEU 155
GLY 156
0.0000
GLY 156
GLN 157
-0.1092
GLN 157
TRP 158
-0.0004
TRP 158
THR 159
0.0009
THR 159
PRO 160
-0.0000
PRO 160
GLY 161
-0.0327
GLY 161
TYR 162
0.0001
TYR 162
LYS 163
-0.0331
LYS 163
PRO 164
-0.0002
PRO 164
ASN 165
-0.0581
ASN 165
PRO 166
0.0001
PRO 166
GLU 167
-0.0124
GLU 167
ILE 168
-0.0001
ILE 168
TYR 169
0.0206
TYR 169
VAL 170
-0.0001
VAL 170
GLN 171
0.0290
GLN 171
LEU 172
-0.0001
LEU 172
ILE 173
-0.0046
ILE 173
LYS 174
-0.0003
LYS 174
GLU 175
0.0219
GLU 175
CYS 176
-0.0002
CYS 176
LYS 177
0.0047
LYS 177
SER 178
-0.0000
SER 178
ARG 179
0.0183
ARG 179
GLY 180
-0.0003
GLY 180
LYS 181
0.0026
LYS 181
GLU 182
-0.0002
GLU 182
GLY 183
-0.0116
GLY 183
GLU 184
0.0004
GLU 184
PHE 185
-0.0271
PHE 185
SER 186
0.0003
SER 186
THR 187
0.0514
THR 187
CYS 188
0.0004
CYS 188
PHE 189
0.0003
PHE 189
THR 190
0.0001
THR 190
GLU 191
-0.0247
GLU 191
LEU 192
0.0000
LEU 192
GLN 193
0.0554
GLN 193
ARG 194
-0.0000
ARG 194
ARG 194
0.1147
ARG 194
ASP 195
-0.0238
ASP 195
PHE 196
-0.0003
PHE 196
LEU 197
-0.1289
LEU 197
ARG 198
0.0001
ARG 198
ASN 199
0.0629
ASN 199
ARG 200
0.0002
ARG 200
PRO 201
-0.0764
PRO 201
THR 202
-0.0002
THR 202
LYS 203
-0.0107
LYS 203
LEU 204
0.0003
LEU 204
LYS 205
0.0131
LYS 205
SER 206
0.0001
SER 206
LEU 207
-0.0026
LEU 207
ILE 208
0.0001
ILE 208
ARG 209
-0.0154
ARG 209
LEU 210
-0.0002
LEU 210
VAL 211
0.0420
VAL 211
LYS 212
-0.0000
LYS 212
HIS 213
-0.0253
HIS 213
TRP 214
0.0001
TRP 214
TYR 215
0.0050
TYR 215
GLN 216
0.0000
GLN 216
THR 217
0.0001
THR 217
CYS 218
0.0003
CYS 218
LYS 219
-0.0633
LYS 219
LYS 220
0.0002
LYS 220
THR 221
0.0248
THR 221
HIS 222
-0.0001
HIS 222
GLY 223
-0.0662
GLY 223
ASN 224
0.0004
ASN 224
LYS 225
-0.0053
LYS 225
LEU 226
-0.0000
LEU 226
PRO 227
0.0627
PRO 227
PRO 228
0.0001
PRO 228
GLN 229
-0.0073
GLN 229
TYR 230
0.0002
TYR 230
ALA 231
0.0301
ALA 231
LEU 232
-0.0002
LEU 232
GLU 233
0.0037
GLU 233
LEU 234
0.0001
LEU 234
LEU 235
0.0559
LEU 235
THR 236
0.0002
THR 236
VAL 237
-0.0594
VAL 237
TYR 238
-0.0001
TYR 238
ALA 239
0.0145
ALA 239
TRP 240
0.0004
TRP 240
GLU 241
-0.0264
GLU 241
GLN 242
-0.0001
GLN 242
GLY 243
-0.0139
GLY 243
SER 244
-0.0000
SER 244
ARG 245
-0.0290
ARG 245
LYS 246
-0.0000
LYS 246
THR 247
-0.1011
THR 247
ASP 248
0.0000
ASP 248
PHE 249
-0.1221
PHE 249
SER 250
-0.0001
SER 250
THR 251
0.0085
THR 251
ALA 252
0.0002
ALA 252
GLN 253
0.0332
GLN 253
GLY 254
-0.0005
GLY 254
PHE 255
-0.0323
PHE 255
GLN 256
-0.0000
GLN 256
THR 257
0.0109
THR 257
VAL 258
-0.0001
VAL 258
LEU 259
-0.0582
LEU 259
GLU 260
0.0004
GLU 260
LEU 261
0.0476
LEU 261
VAL 262
0.0003
VAL 262
LEU 263
-0.0118
LEU 263
LYS 264
0.0002
LYS 264
HIS 265
0.0332
HIS 265
GLN 266
-0.0004
GLN 266
LYS 267
-0.0598
LYS 267
LEU 268
0.0001
LEU 268
CYS 269
0.0262
CYS 269
ILE 270
0.0002
ILE 270
PHE 271
-0.0357
PHE 271
TRP 272
-0.0000
TRP 272
GLU 273
-0.0250
GLU 273
ALA 274
-0.0003
ALA 274
TYR 275
0.0019
TYR 275
TYR 276
-0.0001
TYR 276
ASP 277
-0.0290
ASP 277
PHE 278
-0.0000
PHE 278
THR 279
-0.0040
THR 279
ASN 280
-0.0004
ASN 280
PRO 281
-0.0003
PRO 281
VAL 282
-0.0000
VAL 282
VAL 283
-0.0269
VAL 283
GLY 284
-0.0000
GLY 284
ARG 285
-0.0111
ARG 285
CYS 286
-0.0001
CYS 286
MET 287
-0.0087
MET 287
LEU 288
-0.0000
LEU 288
GLN 289
-0.0206
GLN 289
GLN 290
0.0000
GLN 290
LEU 291
0.0025
LEU 291
LYS 292
0.0003
LYS 292
LYS 293
-0.0132
LYS 293
PRO 294
0.0002
PRO 294
ARG 295
0.0437
ARG 295
PRO 296
0.0001
PRO 296
VAL 297
0.0533
VAL 297
ILE 298
0.0001
ILE 298
LEU 299
0.0599
LEU 299
ASP 300
-0.0001
ASP 300
PRO 301
0.0114
PRO 301
ALA 302
-0.0003
ALA 302
ASP 303
-0.0680
ASP 303
PRO 304
0.0001
PRO 304
THR 305
-0.0413
THR 305
GLY 306
0.0003
GLY 306
ASN 307
0.1811
ASN 307
VAL 308
-0.0001
VAL 308
GLY 309
0.0861
GLY 309
GLY 310
0.0001
GLY 310
GLY 311
-0.0570
GLY 311
ASP 312
-0.0002
ASP 312
THR 313
0.0012
THR 313
HIS 314
0.0002
HIS 314
SER 315
0.0142
SER 315
TRP 316
0.0002
TRP 316
GLN 317
0.0110
GLN 317
ARG 318
0.0001
ARG 318
LEU 319
-0.0125
LEU 319
ALA 320
-0.0000
ALA 320
GLN 321
-0.0187
GLN 321
GLU 322
0.0001
GLU 322
ALA 323
-0.0607
ALA 323
ARG 324
-0.0001
ARG 324
VAL 325
0.0421
VAL 325
TRP 326
-0.0001
TRP 326
LEU 327
-0.0206
LEU 327
GLY 328
-0.0000
GLY 328
TYR 329
0.0242
TYR 329
PRO 330
0.0002
PRO 330
CYS 331
-0.0035
CYS 331
CYS 332
0.0003
CYS 332
LYS 333
0.0043
LYS 333
ASN 334
-0.0002
ASN 334
LEU 335
0.0138
LEU 335
ASP 336
0.0002
ASP 336
GLY 337
0.0233
GLY 337
SER 338
0.0004
SER 338
LEU 339
0.0134
LEU 339
VAL 340
-0.0000
VAL 340
GLY 341
0.0361
GLY 341
ALA 342
0.0003
ALA 342
TRP 343
-0.0265
TRP 343
THR 344
0.0002
THR 344
MET 345
0.0308
MET 345
LEU 346
0.0004
LEU 346
GLN 347
0.0193
GLN 347
LYS 348
-0.0003
LYS 348
ILE 349
-0.0107
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.