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 34
GLN 35
0.0002
GLN 35
ALA 36
0.0056
ALA 36
LEU 37
-0.0001
LEU 37
LYS 38
-0.0178
LYS 38
ILE 39
-0.0003
ILE 39
SER 40
0.0049
SER 40
LEU 41
0.0002
LEU 41
ALA 42
-0.0012
ALA 42
VAL 43
0.0001
VAL 43
VAL 44
-0.0026
VAL 44
LEU 45
0.0003
LEU 45
SER 46
0.0021
SER 46
VAL 47
0.0001
VAL 47
ILE 48
0.0005
ILE 48
THR 49
0.0001
THR 49
LEU 50
0.0019
LEU 50
ALA 51
0.0001
ALA 51
THR 52
-0.0027
THR 52
VAL 53
0.0003
VAL 53
LEU 54
0.0011
LEU 54
SER 55
-0.0000
SER 55
ASN 56
0.0020
ASN 56
ALA 57
-0.0001
ALA 57
PHE 58
-0.0098
PHE 58
VAL 59
0.0002
VAL 59
LEU 60
0.0051
LEU 60
THR 61
-0.0001
THR 61
THR 62
-0.0089
THR 62
ILE 63
-0.0002
ILE 63
LEU 64
0.0050
LEU 64
LEU 65
0.0001
LEU 65
THR 66
-0.0079
THR 66
ARG 67
-0.0002
ARG 67
LYS 68
-0.0139
LYS 68
LEU 69
-0.0002
LEU 69
HIS 70
-0.0117
HIS 70
THR 71
0.0000
THR 71
PRO 72
-0.0001
PRO 72
ALA 73
-0.0001
ALA 73
ASN 74
0.0250
ASN 74
TYR 75
0.0002
TYR 75
LEU 76
-0.0021
LEU 76
ILE 77
-0.0005
ILE 77
GLY 78
0.0042
GLY 78
SER 79
-0.0002
SER 79
LEU 80
0.0025
LEU 80
ALA 81
0.0002
ALA 81
THR 82
0.0033
THR 82
THR 83
-0.0003
THR 83
ASP 84
0.0007
ASP 84
LEU 85
-0.0001
LEU 85
LEU 86
0.0030
LEU 86
VAL 87
-0.0001
VAL 87
SER 88
-0.0049
SER 88
ILE 89
0.0002
ILE 89
LEU 90
0.0110
LEU 90
VAL 91
-0.0000
VAL 91
MET 92
0.0011
MET 92
PRO 93
-0.0000
PRO 93
ILE 94
0.0123
ILE 94
SER 95
-0.0004
SER 95
ILE 96
-0.0053
ILE 96
ALA 97
-0.0003
ALA 97
TYR 98
0.0027
TYR 98
THR 99
-0.0001
THR 99
ILE 100
-0.0005
ILE 100
THR 101
-0.0004
THR 101
HIS 102
-0.0046
HIS 102
THR 103
-0.0000
THR 103
TRP 104
-0.0037
TRP 104
ASN 105
-0.0002
ASN 105
PHE 106
-0.0014
PHE 106
GLY 107
-0.0001
GLY 107
GLN 108
-0.0017
GLN 108
ILE 109
-0.0001
ILE 109
LEU 110
0.0047
LEU 110
CYS 111
-0.0003
CYS 111
ASP 112
-0.0057
ASP 112
ILE 113
-0.0005
ILE 113
TRP 114
0.0071
TRP 114
LEU 115
0.0002
LEU 115
SER 116
-0.0113
SER 116
SER 117
-0.0001
SER 117
ASP 118
0.0097
ASP 118
ILE 119
0.0001
ILE 119
THR 120
-0.0040
THR 120
CYS 121
0.0002
CYS 121
CYS 122
0.0016
CYS 122
THR 123
-0.0003
THR 123
ALA 124
0.0006
ALA 124
SER 125
0.0003
SER 125
ILE 126
-0.0086
ILE 126
TRP 127
0.0001
TRP 127
HIS 128
0.0017
HIS 128
LEU 129
0.0001
LEU 129
CYS 130
-0.0017
CYS 130
VAL 131
0.0001
VAL 131
ILE 132
-0.0082
ILE 132
ALA 133
0.0001
ALA 133
LEU 134
0.0097
LEU 134
ASP 135
0.0003
ASP 135
ARG 136
-0.0049
ARG 136
TYR 137
0.0003
TYR 137
TRP 138
-0.0045
TRP 138
ALA 139
-0.0005
ALA 139
ILE 140
0.0327
ILE 140
THR 141
0.0000
THR 141
ASP 142
-0.0310
ASP 142
ALA 143
-0.0002
ALA 143
LEU 144
-0.0088
LEU 144
GLU 145
-0.0002
GLU 145
TYR 146
0.0057
TYR 146
SER 147
0.0005
SER 147
LYS 148
-0.0029
LYS 148
ARG 149
0.0002
ARG 149
ARG 150
-0.0081
ARG 150
THR 151
0.0002
THR 151
ALA 152
0.0046
ALA 152
GLY 153
-0.0003
GLY 153
HIS 154
-0.0196
HIS 154
ALA 155
0.0002
ALA 155
ALA 156
0.0002
ALA 156
THR 157
-0.0003
THR 157
MET 158
0.0008
MET 158
ILE 159
-0.0002
ILE 159
ALA 160
-0.0028
ALA 160
ILE 161
0.0000
ILE 161
VAL 162
0.0015
VAL 162
TRP 163
-0.0001
TRP 163
ALA 164
0.0056
ALA 164
ILE 165
-0.0000
ILE 165
SER 166
-0.0024
SER 166
ILE 167
-0.0002
ILE 167
CYS 168
0.0092
CYS 168
ILE 169
-0.0001
ILE 169
SER 170
-0.0101
SER 170
ILE 171
0.0001
ILE 171
PRO 172
0.0058
PRO 172
PRO 173
-0.0000
PRO 173
LEU 174
-0.0014
LEU 174
PHE 175
-0.0004
PHE 175
TRP 176
0.0024
TRP 176
ARG 177
-0.0005
ARG 177
ASP 187
-0.0061
ASP 187
CYS 188
0.0002
CYS 188
LEU 189
-0.0051
LEU 189
VAL 190
-0.0002
VAL 190
ASN 191
0.0069
ASN 191
THR 192
0.0001
THR 192
SER 193
0.0021
SER 193
GLN 194
0.0000
GLN 194
ILE 195
0.0026
ILE 195
SER 196
0.0003
SER 196
TYR 197
0.0030
TYR 197
THR 198
0.0004
THR 198
ILE 199
-0.0058
ILE 199
TYR 200
-0.0004
TYR 200
SER 201
0.0080
SER 201
THR 202
-0.0000
THR 202
CYS 203
-0.0071
CYS 203
GLY 204
0.0002
GLY 204
ALA 205
0.0141
ALA 205
PHE 206
-0.0000
PHE 206
TYR 207
-0.0017
TYR 207
ILE 208
0.0001
ILE 208
PRO 209
0.0082
PRO 209
SER 210
-0.0001
SER 210
VAL 211
0.0023
VAL 211
LEU 212
0.0000
LEU 212
LEU 213
0.0198
LEU 213
ILE 214
-0.0000
ILE 214
ILE 215
0.0175
ILE 215
LEU 216
-0.0003
LEU 216
TYR 217
0.0131
TYR 217
GLY 218
-0.0004
GLY 218
ARG 219
0.0676
ARG 219
ILE 220
-0.0001
ILE 220
TYR 221
-0.0421
TYR 221
ARG 222
0.0001
ARG 222
ALA 223
0.0259
ALA 223
ALA 224
0.0000
ALA 224
ARG 225
-0.0169
ARG 225
ASN 226
0.0001
ASN 226
ARG 227
-0.0682
ARG 227
ILE 228
0.0001
ILE 228
LEU 229
0.0129
LEU 229
ASN 230
-0.0003
ASN 230
PRO 231
0.0032
PRO 231
PRO 232
-0.0002
PRO 232
SER 233
-0.0245
SER 233
LEU 234
-0.0002
LEU 234
TYR 235
0.0172
TYR 235
GLY 236
0.0002
GLY 236
LYS 237
0.0314
LYS 237
ARG 238
0.0001
ARG 238
PHE 239
-0.0016
PHE 239
SER 284
0.0945
SER 284
ALA 285
0.0001
ALA 285
LEU 286
-0.0314
LEU 286
GLU 287
-0.0001
GLU 287
ARG 288
-0.0012
ARG 288
LYS 289
-0.0001
LYS 289
ARG 290
-0.0044
ARG 290
ILE 291
-0.0004
ILE 291
SER 292
-0.0461
SER 292
ALA 293
0.0001
ALA 293
ALA 294
-0.0495
ALA 294
ARG 295
0.0002
ARG 295
GLU 296
0.0217
GLU 296
ARG 297
0.0002
ARG 297
LYS 298
-0.1818
LYS 298
ALA 299
0.0002
ALA 299
THR 300
0.0029
THR 300
LYS 301
-0.0003
LYS 301
ILE 302
-0.0185
ILE 302
LEU 303
0.0001
LEU 303
GLY 304
-0.0535
GLY 304
ILE 305
-0.0001
ILE 305
ILE 306
0.0203
ILE 306
LEU 307
-0.0003
LEU 307
GLY 308
-0.0227
GLY 308
ALA 309
0.0002
ALA 309
PHE 310
0.0243
PHE 310
ILE 311
-0.0003
ILE 311
ILE 312
-0.0085
ILE 312
CYS 313
-0.0002
CYS 313
TRP 314
0.0042
TRP 314
LEU 315
-0.0001
LEU 315
PRO 316
0.0010
PRO 316
PHE 317
0.0004
PHE 317
PHE 318
-0.0102
PHE 318
VAL 319
-0.0001
VAL 319
VAL 320
-0.0047
VAL 320
SER 321
-0.0001
SER 321
LEU 322
-0.0043
LEU 322
VAL 323
0.0002
VAL 323
LEU 324
-0.0054
LEU 324
PRO 325
-0.0000
PRO 325
ILE 326
0.0035
ILE 326
CYS 327
-0.0001
CYS 327
ARG 328
0.0004
ARG 328
ASP 329
-0.0002
ASP 329
SER 330
-0.0014
SER 330
CYS 331
-0.0001
CYS 331
TRP 332
0.0015
TRP 332
ILE 333
0.0002
ILE 333
HIS 334
-0.0009
HIS 334
PRO 335
-0.0001
PRO 335
ALA 336
0.0020
ALA 336
LEU 337
0.0002
LEU 337
PHE 338
-0.0027
PHE 338
ASP 339
0.0003
ASP 339
PHE 340
0.0069
PHE 340
PHE 341
0.0001
PHE 341
THR 342
-0.0059
THR 342
TRP 343
-0.0002
TRP 343
LEU 344
0.0265
LEU 344
GLY 345
-0.0001
GLY 345
TYR 346
-0.0065
TYR 346
LEU 347
-0.0002
LEU 347
ASN 348
0.0147
ASN 348
SER 349
-0.0002
SER 349
LEU 350
-0.0042
LEU 350
ILE 351
0.0000
ILE 351
ASN 352
0.0080
ASN 352
PRO 353
-0.0002
PRO 353
ILE 354
-0.0050
ILE 354
ILE 355
0.0006
ILE 355
TYR 356
-0.0017
TYR 356
THR 357
0.0002
THR 357
VAL 358
0.0033
VAL 358
PHE 359
-0.0001
PHE 359
ASN 360
-0.0457
ASN 360
GLU 361
-0.0004
GLU 361
GLU 362
-0.0463
GLU 362
PHE 363
0.0000
PHE 363
ARG 364
-0.0034
ARG 364
GLN 365
0.0001
GLN 365
ALA 366
-0.0021
ALA 366
PHE 367
0.0001
PHE 367
GLN 368
-0.0023
GLN 368
LYS 369
0.0000
LYS 369
ILE 370
-0.0037
ILE 370
VAL 371
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: October 18th, 2018.