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 35
GLN 36
-0.0001
GLN 36
LEU 37
0.0191
LEU 37
PHE 38
-0.0000
PHE 38
PRO 39
0.0139
PRO 39
ALA 40
0.0000
ALA 40
PRO 41
-0.0000
PRO 41
LEU 42
-0.0002
LEU 42
LEU 43
0.0083
LEU 43
ALA 44
-0.0001
ALA 44
GLY 45
-0.0078
GLY 45
VAL 46
-0.0002
VAL 46
THR 47
0.0150
THR 47
ALA 48
-0.0002
ALA 48
THR 49
-0.0142
THR 49
CYS 50
-0.0004
CYS 50
VAL 51
0.0323
VAL 51
ALA 52
0.0001
ALA 52
LEU 53
0.0053
LEU 53
PHE 54
-0.0002
PHE 54
VAL 55
0.0169
VAL 55
VAL 56
0.0005
VAL 56
GLY 57
0.0116
GLY 57
ILE 58
-0.0003
ILE 58
ALA 59
-0.0073
ALA 59
GLY 60
-0.0000
GLY 60
ASN 61
-0.0139
ASN 61
LEU 62
0.0003
LEU 62
LEU 63
0.0191
LEU 63
THR 64
-0.0004
THR 64
MET 65
-0.0128
MET 65
LEU 66
0.0001
LEU 66
VAL 67
0.0500
VAL 67
VAL 68
-0.0000
VAL 68
SER 69
-0.0512
SER 69
ARG 70
0.0000
ARG 70
PHE 71
-0.0064
PHE 71
ARG 72
-0.0000
ARG 72
GLU 73
-0.0594
GLU 73
LEU 74
0.0000
LEU 74
ARG 75
0.1318
ARG 75
THR 76
0.0001
THR 76
THR 77
0.0752
THR 77
THR 78
-0.0000
THR 78
ASN 79
-0.0632
ASN 79
LEU 80
0.0002
LEU 80
TYR 81
0.0697
TYR 81
LEU 82
0.0001
LEU 82
SER 83
-0.0541
SER 83
SER 84
0.0005
SER 84
MET 85
-0.0179
MET 85
ALA 86
-0.0003
ALA 86
PHE 87
-0.0272
PHE 87
SER 88
-0.0001
SER 88
ASP 89
-0.0396
ASP 89
LEU 90
0.0003
LEU 90
LEU 91
0.0324
LEU 91
ILE 92
0.0003
ILE 92
PHE 93
-0.0277
PHE 93
LEU 94
0.0001
LEU 94
CYS 95
0.0183
CYS 95
MET 96
0.0001
MET 96
PRO 97
-0.0091
PRO 97
LEU 98
0.0002
LEU 98
ASP 99
0.0316
ASP 99
LEU 100
0.0004
LEU 100
VAL 101
-0.0444
VAL 101
ARG 102
0.0001
ARG 102
LEU 103
0.0177
LEU 103
TRP 104
-0.0000
TRP 104
GLN 105
-0.1144
GLN 105
TYR 106
-0.0000
TYR 106
ARG 107
-0.0704
ARG 107
PRO 108
-0.0004
PRO 108
TRP 109
-0.0061
TRP 109
ASN 110
-0.0001
ASN 110
PHE 111
0.0226
PHE 111
GLY 112
0.0000
GLY 112
ASP 113
-0.0295
ASP 113
LEU 114
-0.0002
LEU 114
LEU 115
-0.0113
LEU 115
CYS 116
0.0004
CYS 116
LYS 117
0.0088
LYS 117
LEU 118
0.0004
LEU 118
PHE 119
-0.0119
PHE 119
GLN 120
-0.0001
GLN 120
PHE 121
-0.0164
PHE 121
VAL 122
0.0000
VAL 122
SER 123
-0.0142
SER 123
GLU 124
0.0005
GLU 124
SER 125
-0.0489
SER 125
CYS 126
0.0001
CYS 126
THR 127
0.0033
THR 127
TYR 128
-0.0002
TYR 128
ALA 129
0.0160
ALA 129
THR 130
0.0002
THR 130
VAL 131
0.0328
VAL 131
LEU 132
-0.0003
LEU 132
THR 133
0.0262
THR 133
ILE 134
-0.0001
ILE 134
THR 135
-0.0086
THR 135
ALA 136
0.0001
ALA 136
LEU 137
0.0506
LEU 137
SER 138
-0.0002
SER 138
VAL 139
-0.0282
VAL 139
GLU 140
-0.0003
GLU 140
ARG 141
-0.0100
ARG 141
TYR 142
0.0001
TYR 142
PHE 143
0.1857
PHE 143
ALA 144
0.0001
ALA 144
ILE 145
-0.1911
ILE 145
CYS 146
0.0001
CYS 146
PHE 147
0.0219
PHE 147
PRO 148
-0.0003
PRO 148
LEU 149
0.1142
LEU 149
ARG 150
-0.0004
ARG 150
ALA 151
-0.0330
ALA 151
LYS 152
-0.0004
LYS 152
VAL 153
0.0827
VAL 153
VAL 154
0.0002
VAL 154
VAL 155
0.0058
VAL 155
THR 156
-0.0004
THR 156
LYS 157
-0.1225
LYS 157
GLY 158
0.0003
GLY 158
ARG 159
0.0984
ARG 159
VAL 160
-0.0002
VAL 160
LYS 161
-0.0672
LYS 161
LEU 162
-0.0002
LEU 162
VAL 163
0.1385
VAL 163
ILE 164
0.0001
ILE 164
PHE 165
0.0507
PHE 165
VAL 166
-0.0002
VAL 166
ILE 167
0.0464
ILE 167
TRP 168
0.0000
TRP 168
ALA 169
0.0143
ALA 169
VAL 170
-0.0001
VAL 170
ALA 171
-0.0207
ALA 171
PHE 172
-0.0002
PHE 172
CYS 173
-0.0132
CYS 173
SER 174
0.0000
SER 174
ALA 175
0.0161
ALA 175
GLY 176
0.0004
GLY 176
PRO 177
0.0050
PRO 177
ILE 178
0.0000
ILE 178
PHE 179
0.0113
PHE 179
VAL 180
-0.0000
VAL 180
LEU 181
-0.0191
LEU 181
VAL 182
0.0001
VAL 182
GLY 183
0.2233
GLY 183
VAL 184
-0.0002
VAL 184
GLU 185
0.1572
GLU 185
HIS 186
0.0002
HIS 186
GLU 187
0.0571
GLU 187
ASN 188
0.0002
ASN 188
GLY 189
0.0311
GLY 189
THR 190
0.0000
THR 190
ASP 191
0.0947
ASP 191
PRO 192
0.0000
PRO 192
TRP 193
0.0126
TRP 193
ASP 194
-0.0000
ASP 194
THR 195
0.0106
THR 195
ASN 196
-0.0001
ASN 196
GLU 197
-0.0196
GLU 197
CYS 198
0.0001
CYS 198
ARG 199
-0.0154
ARG 199
PRO 200
-0.0001
PRO 200
THR 201
0.0146
THR 201
GLU 202
-0.0001
GLU 202
PHE 203
0.0221
PHE 203
ALA 204
0.0001
ALA 204
VAL 205
-0.0405
VAL 205
ARG 206
0.0002
ARG 206
SER 207
-0.0034
SER 207
GLY 208
-0.0002
GLY 208
LEU 209
-0.0254
LEU 209
LEU 210
-0.0002
LEU 210
THR 211
0.0226
THR 211
VAL 212
-0.0003
VAL 212
MET 213
-0.0223
MET 213
VAL 214
0.0002
VAL 214
TRP 215
0.0017
TRP 215
VAL 216
-0.0002
VAL 216
SER 217
-0.0301
SER 217
SER 218
0.0005
SER 218
ILE 219
0.0123
ILE 219
PHE 220
-0.0001
PHE 220
PHE 221
-0.0009
PHE 221
PHE 222
-0.0001
PHE 222
LEU 223
-0.0666
LEU 223
PRO 224
-0.0000
PRO 224
VAL 225
-0.0085
VAL 225
PHE 226
0.0002
PHE 226
CYS 227
-0.0600
CYS 227
LEU 228
-0.0003
LEU 228
THR 229
-0.0397
THR 229
VAL 230
0.0001
VAL 230
LEU 231
-0.0821
LEU 231
TYR 232
-0.0003
TYR 232
SER 233
-0.1745
SER 233
LEU 234
-0.0001
LEU 234
ILE 235
0.0229
ILE 235
GLY 236
0.0003
GLY 236
ARG 237
-0.2948
ARG 237
LYS 238
0.0001
LYS 238
LEU 239
0.2051
LEU 239
TRP 240
-0.0001
TRP 240
ARG 241
-0.0792
ARG 241
ASN 257
-0.0324
ASN 257
HIS 258
0.0001
HIS 258
LYS 259
0.0912
LYS 259
GLN 260
0.0002
GLN 260
THR 261
0.2398
THR 261
VAL 262
-0.0001
VAL 262
LYS 263
-0.0645
LYS 263
MET 264
-0.0001
MET 264
LEU 265
0.0290
LEU 265
ALA 266
-0.0004
ALA 266
VAL 267
0.0442
VAL 267
VAL 268
-0.0001
VAL 268
VAL 269
-0.0952
VAL 269
PHE 270
-0.0002
PHE 270
ALA 271
0.0549
ALA 271
PHE 272
-0.0002
PHE 272
ILE 273
-0.0275
ILE 273
LEU 274
0.0001
LEU 274
CYS 275
0.0237
CYS 275
TRP 276
0.0001
TRP 276
LEU 277
0.0015
LEU 277
PRO 278
0.0002
PRO 278
PHE 279
-0.0111
PHE 279
HIS 280
0.0003
HIS 280
VAL 281
0.0071
VAL 281
GLY 282
0.0005
GLY 282
ARG 283
-0.0094
ARG 283
TYR 284
-0.0004
TYR 284
LEU 285
0.0204
LEU 285
PHE 286
0.0002
PHE 286
SER 287
0.0111
SER 287
LYS 288
0.0001
LYS 288
SER 289
-0.0131
SER 289
PHE 290
-0.0000
PHE 290
GLU 291
-0.0714
GLU 291
PRO 292
-0.0003
PRO 292
GLY 293
-0.0311
GLY 293
SER 294
0.0000
SER 294
LEU 295
0.0153
LEU 295
GLU 296
0.0001
GLU 296
ILE 297
0.0425
ILE 297
ALA 298
0.0002
ALA 298
GLN 299
0.0216
GLN 299
ILE 300
0.0002
ILE 300
SER 301
0.0007
SER 301
GLN 302
0.0001
GLN 302
TYR 303
-0.0163
TYR 303
CYS 304
-0.0000
CYS 304
ASN 305
0.0075
ASN 305
LEU 306
-0.0002
LEU 306
VAL 307
-0.0363
VAL 307
ALA 308
-0.0001
ALA 308
PHE 309
0.0491
PHE 309
VAL 310
0.0000
VAL 310
LEU 311
-0.0054
LEU 311
PHE 312
0.0000
PHE 312
TYR 313
0.0267
TYR 313
LEU 314
0.0004
LEU 314
SER 315
-0.0014
SER 315
ALA 316
-0.0001
ALA 316
ALA 317
0.0092
ALA 317
ILE 318
0.0001
ILE 318
ASN 319
-0.0226
ASN 319
PRO 320
-0.0001
PRO 320
ILE 321
-0.0021
ILE 321
LEU 322
0.0003
LEU 322
TYR 323
-0.0350
TYR 323
ASN 324
-0.0000
ASN 324
ILE 325
0.1153
ILE 325
MET 326
-0.0002
MET 326
SER 327
-0.2305
SER 327
LYS 328
0.0001
LYS 328
LYS 329
0.0602
LYS 329
TYR 330
0.0001
TYR 330
ARG 331
0.0717
ARG 331
VAL 332
-0.0002
VAL 332
ALA 333
-0.0502
ALA 333
VAL 334
0.0001
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.