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
-0.0388
SER 95
SER 96
-0.0202
SER 96
VAL 97
0.0241
VAL 97
PRO 98
0.0062
PRO 98
SER 99
-0.0059
SER 99
GLN 100
0.0049
GLN 100
LYS 101
0.0305
LYS 101
THR 102
-0.1005
THR 102
TYR 103
-0.0917
TYR 103
GLN 104
-0.0980
GLN 104
GLY 105
-0.0041
GLY 105
SER 106
0.1071
SER 106
TYR 107
-0.0075
TYR 107
GLY 108
-0.1804
GLY 108
PHE 109
-0.0011
PHE 109
ARG 110
-0.1086
ARG 110
LEU 111
-0.1064
LEU 111
GLY 112
0.0294
GLY 112
PHE 113
0.0217
PHE 113
LEU 114
-0.0039
LEU 114
HIS 115
0.0136
HIS 115
SER 116
-0.0337
SER 116
GLY 117
-0.0534
GLY 117
THR 118
-0.0149
THR 118
ALA 119
-0.0301
ALA 119
LYS 120
0.0025
LYS 120
SER 121
0.0016
SER 121
VAL 122
0.0300
VAL 122
VAL 122
0.5799
VAL 122
THR 123
-0.1697
THR 123
CYS 124
0.0148
CYS 124
THR 125
-0.0392
THR 125
TYR 126
0.0385
TYR 126
SER 127
-0.1303
SER 127
PRO 128
-0.1625
PRO 128
ALA 129
0.0438
ALA 129
LEU 130
0.0559
LEU 130
ASN 131
-0.0451
ASN 131
LYS 132
0.1181
LYS 132
MET 133
0.0283
MET 133
MET 133
0.1898
MET 133
PHE 134
-0.1245
PHE 134
CYS 135
-0.1835
CYS 135
GLN 136
0.0519
GLN 136
LEU 137
-0.0956
LEU 137
ALA 138
-0.0299
ALA 138
LYS 139
-0.0740
LYS 139
THR 140
-0.1146
THR 140
CYS 141
-0.0338
CYS 141
PRO 142
0.0489
PRO 142
VAL 143
0.0180
VAL 143
GLN 144
-0.1210
GLN 144
LEU 145
-0.0369
LEU 145
TRP 146
-0.1192
TRP 146
VAL 147
0.2452
VAL 147
ASP 148
0.1628
ASP 148
SER 149
-0.1115
SER 149
THR 150
0.0188
THR 150
PRO 151
0.0050
PRO 151
PRO 152
-0.0422
PRO 152
PRO 153
0.0010
PRO 153
GLY 154
-0.0090
GLY 154
THR 155
0.0686
THR 155
ARG 156
-0.0674
ARG 156
VAL 157
0.0202
VAL 157
ARG 158
0.0851
ARG 158
ALA 159
-0.1205
ALA 159
MET 160
-0.1146
MET 160
ALA 161
0.0920
ALA 161
ILE 162
-0.0626
ILE 162
TYR 163
-0.2244
TYR 163
LYS 164
0.1268
LYS 164
GLN 165
-0.2747
GLN 165
SER 166
-0.1186
SER 166
GLN 167
0.0009
GLN 167
HIS 168
0.0272
HIS 168
MET 169
0.0060
MET 169
THR 170
0.0825
THR 170
GLU 171
-0.0522
GLU 171
VAL 172
-0.0403
VAL 172
VAL 173
0.1202
VAL 173
ARG 174
0.2251
ARG 174
ARG 175
-0.0743
ARG 175
CYS 176
0.0067
CYS 176
PRO 177
0.0152
PRO 177
HIS 178
0.0014
HIS 178
HIS 179
-0.0243
HIS 179
GLU 180
-0.0079
GLU 180
ARG 181
0.0022
ARG 181
CYS 182
0.0095
CYS 182
SER 183
0.0408
SER 183
ASP 184
-0.0298
ASP 184
SER 185
0.0066
SER 185
ASP 186
0.0157
ASP 186
GLY 187
-0.0003
GLY 187
LEU 188
0.1751
LEU 188
ALA 189
0.1241
ALA 189
PRO 190
0.2613
PRO 190
PRO 191
-0.0034
PRO 191
GLN 192
0.0263
GLN 192
HIS 193
-0.0077
HIS 193
LEU 194
-0.0184
LEU 194
ILE 195
0.0675
ILE 195
ARG 196
-0.0642
ARG 196
VAL 197
0.0248
VAL 197
GLU 198
0.0307
GLU 198
GLY 199
0.0267
GLY 199
ASN 200
0.0226
ASN 200
LEU 201
0.0029
LEU 201
ARG 202
-0.0023
ARG 202
VAL 203
-0.0507
VAL 203
GLU 204
0.1096
GLU 204
CYS 205
-0.2410
CYS 205
LEU 206
-0.1469
LEU 206
ASP 207
0.1256
ASP 207
ASP 208
-0.0445
ASP 208
ARG 209
0.0316
ARG 209
ASN 210
-0.0742
ASN 210
THR 211
0.0552
THR 211
PHE 212
-0.0219
PHE 212
ARG 213
0.0474
ARG 213
HIS 214
0.0788
HIS 214
SER 215
-0.0464
SER 215
VAL 216
0.0088
VAL 216
VAL 217
0.0251
VAL 217
VAL 218
0.0634
VAL 218
PRO 219
-0.0680
PRO 219
TYR 220
-0.1072
TYR 220
GLU 221
0.0198
GLU 221
PRO 222
-0.0389
PRO 222
PRO 223
0.1606
PRO 223
GLU 224
0.0006
GLU 224
VAL 225
0.0095
VAL 225
GLY 226
0.0103
GLY 226
SER 227
0.0738
SER 227
ASP 228
0.1257
ASP 228
CYS 229
-0.0572
CYS 229
THR 230
-0.0056
THR 230
THR 231
-0.0681
THR 231
ILE 232
-0.0037
ILE 232
HIS 233
-0.0774
HIS 233
TYR 234
0.0173
TYR 234
ASN 235
0.0634
ASN 235
TYR 236
-0.0799
TYR 236
MET 237
0.0068
MET 237
CYS 238
-0.1867
CYS 238
ASN 239
-0.0573
ASN 239
SER 240
-0.0153
SER 240
SER 241
-0.1137
SER 241
CYS 242
-0.1589
CYS 242
MET 243
-0.0311
MET 243
GLY 244
-0.0079
GLY 244
GLY 245
-0.0497
GLY 245
MET 246
-0.0257
MET 246
ARG 248
0.0005
ARG 248
ARG 249
0.0021
ARG 249
PRO 250
0.2207
PRO 250
ILE 251
0.0911
ILE 251
LEU 252
-0.1259
LEU 252
THR 253
-0.1420
THR 253
ILE 254
0.1568
ILE 254
ILE 255
-0.0013
ILE 255
THR 256
-0.1244
THR 256
LEU 257
-0.0045
LEU 257
GLU 258
0.0278
GLU 258
ASP 259
-0.0007
ASP 259
SER 260
0.0062
SER 260
SER 261
-0.0600
SER 261
GLY 262
-0.0245
GLY 262
ASN 263
0.0342
ASN 263
LEU 264
-0.0669
LEU 264
LEU 265
0.0041
LEU 265
GLY 266
0.0923
GLY 266
ARG 267
0.1065
ARG 267
ASN 268
0.0023
ASN 268
SER 269
0.1092
SER 269
PHE 270
-0.1270
PHE 270
GLU 271
0.0769
GLU 271
VAL 272
-0.1196
VAL 272
ARG 273
-0.0448
ARG 273
VAL 274
0.0085
VAL 274
CYS 275
0.0746
CYS 275
ALA 276
0.0566
ALA 276
CYS 277
0.0393
CYS 277
CYS 277
-0.0847
CYS 277
PRO 278
0.0269
PRO 278
GLY 279
0.1818
GLY 279
ARG 280
0.0062
ARG 280
ASP 281
0.0015
ASP 281
ARG 282
-0.0288
ARG 282
ARG 283
0.0015
ARG 283
THR 284
-0.0316
THR 284
GLU 285
0.0007
GLU 285
GLU 286
0.0257
GLU 286
GLU 287
-0.0031
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.