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
SER 94
SER 95
0.0153
SER 95
SER 96
-0.0068
SER 96
VAL 97
-0.1266
VAL 97
PRO 98
0.0102
PRO 98
SER 99
0.0058
SER 99
GLN 100
-0.0097
GLN 100
LYS 101
-0.0843
LYS 101
THR 102
-0.0389
THR 102
TYR 103
0.0154
TYR 103
GLN 104
-0.1378
GLN 104
GLY 105
-0.0667
GLY 105
SER 106
0.0374
SER 106
TYR 107
0.0208
TYR 107
GLY 108
-0.1216
GLY 108
PHE 109
-0.0427
PHE 109
ARG 110
-0.0066
ARG 110
LEU 111
-0.1854
LEU 111
GLY 112
-0.0399
GLY 112
PHE 113
0.0713
PHE 113
LEU 114
0.0006
LEU 114
HIS 115
0.0086
HIS 115
SER 116
-0.0252
SER 116
GLY 117
0.0017
GLY 117
THR 118
0.1567
THR 118
ALA 119
0.0568
ALA 119
LYS 120
-0.0051
LYS 120
SER 121
-0.0402
SER 121
VAL 122
-0.0424
VAL 122
VAL 122
-0.4653
VAL 122
THR 123
0.1222
THR 123
CYS 124
-0.0038
CYS 124
THR 125
-0.0643
THR 125
TYR 126
0.1426
TYR 126
SER 127
0.1349
SER 127
PRO 128
0.0463
PRO 128
ALA 129
-0.0220
ALA 129
LEU 130
-0.0368
LEU 130
ASN 131
0.0365
ASN 131
LYS 132
-0.1033
LYS 132
MET 133
0.0774
MET 133
MET 133
-0.1379
MET 133
PHE 134
-0.0448
PHE 134
CYS 135
-0.1783
CYS 135
GLN 136
0.0479
GLN 136
LEU 137
0.0940
LEU 137
ALA 138
-0.0396
ALA 138
LYS 139
0.2002
LYS 139
THR 140
-0.0330
THR 140
CYS 141
0.0193
CYS 141
PRO 142
-0.0123
PRO 142
VAL 143
-0.0560
VAL 143
GLN 144
-0.0236
GLN 144
LEU 145
-0.0081
LEU 145
TRP 146
0.0158
TRP 146
VAL 147
0.0356
VAL 147
ASP 148
-0.0707
ASP 148
SER 149
-0.0803
SER 149
THR 150
0.1288
THR 150
PRO 151
0.0142
PRO 151
PRO 152
-0.1060
PRO 152
PRO 153
-0.0146
PRO 153
GLY 154
-0.0116
GLY 154
THR 155
0.0048
THR 155
ARG 156
0.0378
ARG 156
VAL 157
-0.0140
VAL 157
ARG 158
0.0925
ARG 158
ALA 159
-0.0105
ALA 159
MET 160
0.1150
MET 160
ALA 161
0.0628
ALA 161
ILE 162
-0.1149
ILE 162
TYR 163
-0.0086
TYR 163
LYS 164
0.0621
LYS 164
GLN 165
0.1046
GLN 165
SER 166
0.0921
SER 166
GLN 167
0.0099
GLN 167
HIS 168
-0.0322
HIS 168
MET 169
-0.0841
MET 169
THR 170
-0.1891
THR 170
GLU 171
0.1074
GLU 171
VAL 172
-0.0435
VAL 172
VAL 173
0.0599
VAL 173
ARG 174
0.0329
ARG 174
ARG 175
-0.0260
ARG 175
CYS 176
0.1803
CYS 176
PRO 177
0.0162
PRO 177
HIS 178
0.0151
HIS 178
HIS 179
-0.0789
HIS 179
GLU 180
-0.0064
GLU 180
ARG 181
0.0379
ARG 181
CYS 182
0.0313
CYS 182
SER 183
-0.0003
SER 183
ASP 184
0.0218
ASP 184
SER 185
-0.0177
SER 185
ASP 186
0.0015
ASP 186
GLY 187
-0.0035
GLY 187
LEU 188
-0.0140
LEU 188
ALA 189
-0.0706
ALA 189
PRO 190
-0.0684
PRO 190
PRO 191
0.0150
PRO 191
GLN 192
0.0289
GLN 192
HIS 193
0.0499
HIS 193
LEU 194
0.2147
LEU 194
ILE 195
0.2686
ILE 195
ARG 196
-0.2647
ARG 196
VAL 197
-0.1435
VAL 197
GLU 198
0.0228
GLU 198
GLY 199
-0.0816
GLY 199
ASN 200
-0.0108
ASN 200
LEU 201
0.0044
LEU 201
ARG 202
0.0161
ARG 202
VAL 203
-0.0148
VAL 203
GLU 204
-0.0634
GLU 204
TYR 205
-0.0301
TYR 205
LEU 206
-0.0346
LEU 206
ASP 207
-0.0352
ASP 207
ASP 208
0.0359
ASP 208
ARG 209
-0.0075
ARG 209
ASN 210
-0.0111
ASN 210
THR 211
-0.0027
THR 211
PHE 212
-0.0333
PHE 212
ARG 213
0.0511
ARG 213
HIS 214
0.0616
HIS 214
SER 215
-0.1397
SER 215
VAL 216
0.0105
VAL 216
VAL 217
0.1903
VAL 217
VAL 218
-0.0026
VAL 218
PRO 219
-0.0342
PRO 219
TYR 220
0.1338
TYR 220
GLU 221
-0.0125
GLU 221
PRO 222
0.0450
PRO 222
PRO 223
-0.0145
PRO 223
GLU 224
-0.0991
GLU 224
VAL 225
-0.0424
VAL 225
GLY 226
-0.0277
GLY 226
SER 227
-0.1135
SER 227
ASP 228
-0.0269
ASP 228
CYS 229
0.0588
CYS 229
THR 230
0.2041
THR 230
THR 231
0.1871
THR 231
ILE 232
0.0039
ILE 232
HIS 233
0.0836
HIS 233
TYR 234
0.0499
TYR 234
ASN 235
-0.1190
ASN 235
TYR 236
-0.3619
TYR 236
MET 237
0.0612
MET 237
CYS 238
-0.0368
CYS 238
ASN 239
-0.1423
ASN 239
SER 240
0.1789
SER 240
SER 241
-0.0323
SER 241
CYS 242
-0.0251
CYS 242
MET 243
-0.1026
MET 243
GLY 244
0.0677
GLY 244
GLY 245
0.0184
GLY 245
MET 246
0.0358
MET 246
ARG 248
-0.1272
ARG 248
ARG 249
0.0522
ARG 249
PRO 250
-0.0601
PRO 250
ILE 251
-0.0530
ILE 251
LEU 252
0.0936
LEU 252
THR 253
-0.0305
THR 253
ILE 254
0.0581
ILE 254
ILE 255
0.0200
ILE 255
THR 256
0.0538
THR 256
LEU 257
0.0069
LEU 257
GLU 258
0.0495
GLU 258
ASP 259
0.0145
ASP 259
SER 260
0.0501
SER 260
SER 261
-0.0341
SER 261
GLY 262
0.0400
GLY 262
ASN 263
0.0085
ASN 263
LEU 264
-0.0310
LEU 264
LEU 265
0.0452
LEU 265
GLY 266
0.0544
GLY 266
ARG 267
-0.0054
ARG 267
ASN 268
0.0335
ASN 268
SER 269
0.1572
SER 269
PHE 270
-0.1665
PHE 270
GLU 271
-0.0712
GLU 271
VAL 272
0.0615
VAL 272
ARG 273
0.1609
ARG 273
VAL 274
-0.1872
VAL 274
CYS 275
-0.0114
CYS 275
ALA 276
-0.0421
ALA 276
CYS 277
-0.0144
CYS 277
CYS 277
0.0733
CYS 277
PRO 278
-0.0266
PRO 278
GLY 279
-0.2250
GLY 279
ARG 280
-0.0234
ARG 280
ASP 281
-0.0204
ASP 281
ARG 282
0.0004
ARG 282
ARG 283
-0.0551
ARG 283
THR 284
0.0440
THR 284
GLU 285
-0.0008
GLU 285
GLU 286
-0.0212
GLU 286
GLU 287
-0.0104
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.