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
VAL 8
GLU 9
0.0000
GLU 9
CYS 10
0.1247
CYS 10
PRO 11
-0.0001
PRO 11
PHE 12
-0.2089
PHE 12
CYS 13
0.0001
CYS 13
ASP 14
0.0344
ASP 14
GLU 15
-0.0003
GLU 15
VAL 16
0.0067
VAL 16
SER 17
-0.0002
SER 17
LYS 18
-0.0136
LYS 18
TYR 19
-0.0001
TYR 19
GLU 20
0.0431
GLU 20
LYS 21
-0.0001
LYS 21
LEU 22
-0.0043
LEU 22
ALA 23
-0.0000
ALA 23
LYS 24
0.0052
LYS 24
ILE 25
-0.0001
ILE 25
GLY 26
0.0263
GLY 26
GLN 27
-0.0002
GLN 27
GLY 28
0.0079
GLY 28
THR 29
0.0005
THR 29
PHE 30
0.0044
PHE 30
GLY 31
-0.0002
GLY 31
GLU 32
-0.0329
GLU 32
VAL 33
-0.0001
VAL 33
PHE 34
0.0130
PHE 34
LYS 35
-0.0003
LYS 35
ALA 36
-0.0128
ALA 36
ARG 37
0.0002
ARG 37
HIS 38
0.0056
HIS 38
ARG 39
0.0000
ARG 39
LYS 40
-0.0059
LYS 40
THR 41
0.0001
THR 41
GLY 42
-0.0273
GLY 42
GLN 43
-0.0000
GLN 43
LYS 44
-0.0217
LYS 44
VAL 45
0.0001
VAL 45
ALA 46
0.0072
ALA 46
LEU 47
-0.0001
LEU 47
LYS 48
-0.0095
LYS 48
LYS 49
0.0002
LYS 49
VAL 50
-0.0120
VAL 50
GLU 55
-0.4518
GLU 55
LYS 56
-0.0001
LYS 56
GLU 57
0.0491
GLU 57
GLY 58
0.0002
GLY 58
PHE 59
-0.2357
PHE 59
PRO 60
0.0001
PRO 60
ILE 61
-0.1025
ILE 61
THR 62
0.0004
THR 62
ALA 63
-0.0143
ALA 63
LEU 64
0.0001
LEU 64
ARG 65
-0.0044
ARG 65
GLU 66
0.0002
GLU 66
ILE 67
0.0237
ILE 67
LYS 68
-0.0002
LYS 68
ILE 69
-0.0099
ILE 69
LEU 70
-0.0003
LEU 70
GLN 71
-0.0126
GLN 71
LEU 72
-0.0003
LEU 72
LEU 73
-0.0212
LEU 73
LYS 74
0.0000
LYS 74
HIS 75
-0.0281
HIS 75
GLU 76
-0.0000
GLU 76
ASN 77
0.0046
ASN 77
VAL 78
-0.0003
VAL 78
VAL 79
0.0010
VAL 79
ASN 80
-0.0000
ASN 80
LEU 81
-0.0067
LEU 81
ILE 82
-0.0002
ILE 82
GLU 83
-0.0046
GLU 83
ILE 84
-0.0004
ILE 84
CYS 85
0.0646
CYS 85
ARG 86
0.0000
ARG 86
THR 87
-0.0345
THR 87
SER 98
0.0160
SER 98
ILE 99
0.0002
ILE 99
TYR 100
0.0029
TYR 100
LEU 101
0.0003
LEU 101
VAL 102
-0.0182
VAL 102
PHE 103
-0.0000
PHE 103
ASP 104
-0.0143
ASP 104
PHE 105
-0.0001
PHE 105
CYS 106
-0.0871
CYS 106
GLU 107
-0.0001
GLU 107
HIS 108
-0.1270
HIS 108
ASP 109
-0.0002
ASP 109
LEU 110
-0.0590
LEU 110
ALA 111
-0.0000
ALA 111
GLY 112
0.0097
GLY 112
LEU 113
-0.0002
LEU 113
LEU 114
-0.0654
LEU 114
SER 115
-0.0002
SER 115
ASN 116
0.0045
ASN 116
VAL 117
-0.0001
VAL 117
LEU 118
0.0021
LEU 118
VAL 119
-0.0002
VAL 119
LYS 120
-0.0058
LYS 120
PHE 121
-0.0003
PHE 121
THR 122
-0.0048
THR 122
LEU 123
-0.0001
LEU 123
SER 124
-0.0075
SER 124
GLU 125
0.0002
GLU 125
ILE 126
-0.0028
ILE 126
LYS 127
0.0000
LYS 127
ARG 128
-0.0136
ARG 128
VAL 129
-0.0001
VAL 129
MET 130
-0.0097
MET 130
GLN 131
0.0001
GLN 131
MET 132
-0.0085
MET 132
LEU 133
0.0002
LEU 133
LEU 134
-0.0140
LEU 134
ASN 135
0.0004
ASN 135
GLY 136
0.0043
GLY 136
LEU 137
-0.0000
LEU 137
TYR 138
-0.0111
TYR 138
TYR 139
0.0000
TYR 139
ILE 140
0.0066
ILE 140
HIS 141
0.0001
HIS 141
ARG 142
-0.0053
ARG 142
ASN 143
0.0002
ASN 143
LYS 144
-0.0055
LYS 144
ILE 145
0.0002
ILE 145
LEU 146
0.0032
LEU 146
HIS 147
0.0002
HIS 147
ARG 148
-0.0104
ARG 148
ASP 149
-0.0005
ASP 149
MET 150
0.0167
MET 150
LYS 151
0.0001
LYS 151
ALA 152
0.0107
ALA 152
ALA 153
-0.0000
ALA 153
ASN 154
-0.0062
ASN 154
VAL 155
0.0001
VAL 155
LEU 156
-0.0069
LEU 156
ILE 157
0.0004
ILE 157
THR 158
-0.0056
THR 158
ARG 159
-0.0000
ARG 159
ASP 160
-0.0367
ASP 160
GLY 161
-0.0001
GLY 161
VAL 162
-0.0078
VAL 162
LEU 163
-0.0001
LEU 163
LYS 164
-0.0051
LYS 164
LEU 165
-0.0000
LEU 165
ALA 166
0.0010
ALA 166
ASP 167
-0.0000
ASP 167
PHE 168
-0.0054
PHE 168
GLY 169
-0.0003
GLY 169
LEU 170
0.0256
LEU 170
ALA 171
-0.0001
ALA 171
ARG 172
-0.0128
ARG 172
ALA 173
-0.0001
ALA 173
PHE 174
0.0463
PHE 174
SER 175
0.0003
SER 175
LEU 176
0.0071
LEU 176
PRO 182
-0.0138
PRO 182
ASN 183
0.0000
ASN 183
ARG 184
-0.0099
ARG 184
TYR 185
0.0000
TYR 185
ASN 187
-0.0117
ASN 187
ARG 188
0.0000
ARG 188
VAL 189
0.0111
VAL 189
VAL 190
-0.0000
VAL 190
THR 191
-0.0095
THR 191
LEU 192
-0.0002
LEU 192
TRP 193
-0.0007
TRP 193
TYR 194
0.0001
TYR 194
ARG 195
0.0062
ARG 195
PRO 196
-0.0003
PRO 196
PRO 197
0.0050
PRO 197
GLU 198
-0.0002
GLU 198
LEU 199
0.0097
LEU 199
LEU 200
-0.0002
LEU 200
LEU 201
0.0097
LEU 201
GLY 202
-0.0000
GLY 202
GLU 203
0.0002
GLU 203
ARG 204
0.0000
ARG 204
ASP 205
-0.0039
ASP 205
TYR 206
-0.0002
TYR 206
GLY 207
-0.0306
GLY 207
PRO 208
-0.0002
PRO 208
PRO 209
0.0429
PRO 209
ILE 210
0.0001
ILE 210
ASP 211
-0.0006
ASP 211
LEU 212
0.0001
LEU 212
TRP 213
0.0057
TRP 213
GLY 214
0.0004
GLY 214
ALA 215
-0.0019
ALA 215
GLY 216
0.0000
GLY 216
CYS 217
0.0023
CYS 217
ILE 218
0.0002
ILE 218
MET 219
-0.0010
MET 219
ALA 220
0.0002
ALA 220
GLU 221
-0.0159
GLU 221
MET 222
-0.0001
MET 222
TRP 223
-0.0177
TRP 223
THR 224
-0.0003
THR 224
ARG 225
-0.0297
ARG 225
SER 226
-0.0000
SER 226
PRO 227
0.0063
PRO 227
ILE 228
-0.0002
ILE 228
MET 229
0.0016
MET 229
GLN 230
-0.0002
GLN 230
GLY 231
0.0112
GLY 231
ASN 232
-0.0003
ASN 232
THR 233
0.0054
THR 233
GLU 234
-0.0001
GLU 234
GLN 235
-0.0016
GLN 235
HIS 236
0.0003
HIS 236
GLN 237
-0.0002
GLN 237
LEU 238
0.0002
LEU 238
ALA 239
0.0052
ALA 239
LEU 240
-0.0004
LEU 240
ILE 241
0.0033
ILE 241
SER 242
-0.0004
SER 242
GLN 243
0.0006
GLN 243
LEU 244
-0.0003
LEU 244
CYS 245
-0.0011
CYS 245
GLY 246
-0.0000
GLY 246
SER 247
-0.0060
SER 247
ILE 248
-0.0003
ILE 248
THR 249
-0.0043
THR 249
PRO 250
0.0000
PRO 250
GLU 251
-0.0009
GLU 251
VAL 252
0.0004
VAL 252
TRP 253
0.0021
TRP 253
PRO 254
-0.0001
PRO 254
ASN 255
-0.0120
ASN 255
VAL 256
-0.0004
VAL 256
ASP 257
-0.0047
ASP 257
ASN 258
-0.0002
ASN 258
TYR 259
-0.0024
TYR 259
LEU 267
0.0047
LEU 267
VAL 268
0.0002
VAL 268
LYS 269
-0.0058
LYS 269
GLY 270
-0.0001
GLY 270
GLN 271
-0.0139
GLN 271
LYS 272
0.0001
LYS 272
ARG 273
-0.0010
ARG 273
LYS 274
0.0000
LYS 274
VAL 275
0.0026
VAL 275
LYS 276
-0.0000
LYS 276
ASP 277
0.0187
ASP 277
ARG 278
0.0002
ARG 278
LEU 279
-0.0073
LEU 279
LYS 280
-0.0000
LYS 280
ALA 281
-0.0039
ALA 281
TYR 282
0.0002
TYR 282
VAL 283
0.0127
VAL 283
ARG 284
-0.0002
ARG 284
ASP 285
0.0008
ASP 285
PRO 286
0.0001
PRO 286
TYR 287
0.0078
TYR 287
ALA 288
0.0001
ALA 288
LEU 289
-0.0069
LEU 289
ASP 290
0.0003
ASP 290
LEU 291
0.0084
LEU 291
ILE 292
-0.0002
ILE 292
ASP 293
-0.0178
ASP 293
LYS 294
0.0000
LYS 294
LEU 295
0.0014
LEU 295
LEU 296
-0.0000
LEU 296
VAL 297
-0.0165
VAL 297
LEU 298
-0.0002
LEU 298
ASP 299
0.0041
ASP 299
PRO 300
-0.0002
PRO 300
ALA 301
-0.0016
ALA 301
GLN 302
0.0001
GLN 302
ARG 303
-0.0093
ARG 303
ILE 304
-0.0004
ILE 304
ASP 305
0.0249
ASP 305
SER 306
-0.0002
SER 306
ASP 307
-0.0085
ASP 307
ASP 308
0.0000
ASP 308
ALA 309
0.0049
ALA 309
LEU 310
-0.0001
LEU 310
ASN 311
0.0051
ASN 311
HIS 312
0.0002
HIS 312
ASP 313
0.0030
ASP 313
PHE 314
0.0001
PHE 314
PHE 315
-0.0003
PHE 315
TRP 316
-0.0002
TRP 316
SER 317
0.0024
SER 317
ASP 318
0.0003
ASP 318
PRO 319
-0.0021
PRO 319
MET 320
-0.0003
MET 320
PRO 321
-0.0068
PRO 321
SER 322
-0.0002
SER 322
ASP 323
-0.0313
ASP 323
LEU 324
0.0000
LEU 324
LYS 325
0.0059
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.