Should you encounter any unexpected behaviour,
please let us know. elNémo has been relocated.
**Some cleaning from time to time**
Sorry for the inconvenience.
***  PERIPLASMIC BINDING PROTEIN 25-JUN-97 1ANF  ***
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
LYS 1
ILE 2
-0.0001
ILE 2
GLU 3
-0.0065
GLU 3
GLU 4
0.0001
GLU 4
GLY 5
0.0339
GLY 5
LYS 6
-0.0001
LYS 6
LEU 7
0.0028
LEU 7
VAL 8
-0.0001
VAL 8
ILE 9
-0.0108
ILE 9
TRP 10
-0.0001
TRP 10
ILE 11
-0.0352
ILE 11
ASN 12
-0.0001
ASN 12
GLY 13
0.0236
GLY 13
ASP 14
-0.0002
ASP 14
LYS 15
0.0406
LYS 15
GLY 16
0.0002
GLY 16
TYR 17
-0.0119
TYR 17
ASN 18
-0.0002
ASN 18
GLY 19
-0.0073
GLY 19
LEU 20
0.0002
LEU 20
ALA 21
0.0003
ALA 21
GLU 22
-0.0003
GLU 22
VAL 23
-0.0110
VAL 23
GLY 24
-0.0003
GLY 24
LYS 25
0.0024
LYS 25
LYS 26
-0.0003
LYS 26
PHE 27
-0.0068
PHE 27
GLU 28
-0.0002
GLU 28
LYS 29
0.0007
LYS 29
ASP 30
0.0001
ASP 30
THR 31
-0.0136
THR 31
GLY 32
-0.0003
GLY 32
ILE 33
0.0007
ILE 33
LYS 34
0.0004
LYS 34
VAL 35
-0.0005
VAL 35
THR 36
0.0001
THR 36
VAL 37
-0.0140
VAL 37
GLU 38
-0.0001
GLU 38
HIS 39
-0.0010
HIS 39
PRO 40
-0.0002
PRO 40
ASP 41
0.0135
ASP 41
LYS 42
-0.0001
LYS 42
LEU 43
0.0022
LEU 43
GLU 44
-0.0002
GLU 44
GLU 45
-0.0076
GLU 45
LYS 46
-0.0000
LYS 46
PHE 47
0.0028
PHE 47
PRO 48
0.0003
PRO 48
GLN 49
-0.0084
GLN 49
VAL 50
-0.0000
VAL 50
ALA 51
0.0033
ALA 51
ALA 52
-0.0003
ALA 52
THR 53
0.0116
THR 53
GLY 54
-0.0001
GLY 54
ASP 55
-0.0125
ASP 55
GLY 56
-0.0002
GLY 56
PRO 57
-0.0012
PRO 57
ASP 58
-0.0001
ASP 58
ILE 59
0.0012
ILE 59
ILE 60
0.0004
ILE 60
PHE 61
-0.0107
PHE 61
TRP 62
0.0001
TRP 62
ALA 63
0.0043
ALA 63
HIS 64
0.0001
HIS 64
ASP 65
0.0171
ASP 65
ARG 66
-0.0001
ARG 66
PHE 67
0.0155
PHE 67
GLY 68
-0.0001
GLY 68
GLY 69
-0.0028
GLY 69
TYR 70
-0.0002
TYR 70
ALA 71
-0.0080
ALA 71
GLN 72
0.0003
GLN 72
SER 73
0.0098
SER 73
GLY 74
0.0002
GLY 74
LEU 75
-0.0041
LEU 75
LEU 76
0.0003
LEU 76
ALA 77
0.0033
ALA 77
GLU 78
0.0002
GLU 78
ILE 79
0.0008
ILE 79
THR 80
0.0000
THR 80
PRO 81
0.0101
PRO 81
ASP 82
-0.0002
ASP 82
LYS 83
-0.0115
LYS 83
ALA 84
0.0002
ALA 84
PHE 85
-0.1091
PHE 85
GLN 86
-0.0002
GLN 86
ASP 87
-0.0179
ASP 87
LYS 88
0.0004
LYS 88
LEU 89
0.0154
LEU 89
TYR 90
0.0001
TYR 90
PRO 91
-0.0292
PRO 91
PHE 92
0.0001
PHE 92
THR 93
0.0009
THR 93
TRP 94
-0.0001
TRP 94
ASP 95
0.0046
ASP 95
ALA 96
-0.0004
ALA 96
VAL 97
0.0124
VAL 97
ARG 98
0.0002
ARG 98
TYR 99
-0.0090
TYR 99
ASN 100
-0.0001
ASN 100
GLY 101
0.0121
GLY 101
LYS 102
-0.0001
LYS 102
LEU 103
-0.0065
LEU 103
ILE 104
-0.0001
ILE 104
ALA 105
-0.0099
ALA 105
TYR 106
0.0001
TYR 106
PRO 107
0.0056
PRO 107
ILE 108
-0.0002
ILE 108
ALA 109
0.0269
ALA 109
VAL 110
0.0002
VAL 110
GLU 111
0.0571
GLU 111
ALA 112
0.0004
ALA 112
LEU 113
0.0236
LEU 113
SER 114
-0.0002
SER 114
LEU 115
-0.0040
LEU 115
ILE 116
-0.0001
ILE 116
TYR 117
-0.0057
TYR 117
ASN 118
0.0001
ASN 118
LYS 119
0.0176
LYS 119
ASP 120
0.0000
ASP 120
LEU 121
-0.0137
LEU 121
LEU 122
-0.0001
LEU 122
PRO 123
0.0116
PRO 123
ASN 124
-0.0002
ASN 124
PRO 125
-0.0026
PRO 125
PRO 126
0.0002
PRO 126
LYS 127
-0.0240
LYS 127
THR 128
0.0000
THR 128
TRP 129
0.0237
TRP 129
GLU 130
0.0003
GLU 130
GLU 131
-0.0433
GLU 131
ILE 132
-0.0002
ILE 132
PRO 133
0.0231
PRO 133
ALA 134
0.0000
ALA 134
LEU 135
0.0845
LEU 135
ASP 136
0.0002
ASP 136
LYS 137
0.0062
LYS 137
GLU 138
-0.0005
GLU 138
LEU 139
0.0350
LEU 139
LYS 140
-0.0003
LYS 140
ALA 141
0.1044
ALA 141
LYS 142
-0.0001
LYS 142
GLY 143
0.0530
GLY 143
LYS 144
0.0004
LYS 144
SER 145
0.0295
SER 145
ALA 146
-0.0003
ALA 146
LEU 147
0.0413
LEU 147
MET 148
0.0001
MET 148
PHE 149
0.0759
PHE 149
ASN 150
0.0000
ASN 150
LEU 151
-0.0148
LEU 151
GLN 152
-0.0002
GLN 152
GLU 153
0.0217
GLU 153
PRO 154
0.0002
PRO 154
TYR 155
-0.0098
TYR 155
PHE 156
0.0001
PHE 156
THR 157
0.0033
THR 157
TRP 158
0.0002
TRP 158
PRO 159
-0.0291
PRO 159
LEU 160
-0.0002
LEU 160
ILE 161
-0.0153
ILE 161
ALA 162
-0.0003
ALA 162
ALA 163
-0.0142
ALA 163
ASP 164
-0.0001
ASP 164
GLY 165
-0.0212
GLY 165
GLY 166
-0.0001
GLY 166
TYR 167
0.0347
TYR 167
ALA 168
-0.0001
ALA 168
PHE 169
0.0352
PHE 169
LYS 170
-0.0003
LYS 170
TYR 171
0.0706
TYR 171
GLU 172
0.0000
GLU 172
ASN 173
0.1198
ASN 173
GLY 174
0.0002
GLY 174
LYS 175
-0.0738
LYS 175
TYR 176
-0.0000
TYR 176
ASP 177
0.0045
ASP 177
ILE 178
-0.0000
ILE 178
LYS 179
0.0331
LYS 179
ASP 180
0.0002
ASP 180
VAL 181
0.0148
VAL 181
GLY 182
0.0000
GLY 182
VAL 183
0.0514
VAL 183
ASP 184
0.0004
ASP 184
ASN 185
-0.0330
ASN 185
ALA 186
-0.0001
ALA 186
GLY 187
-0.0181
GLY 187
ALA 188
-0.0000
ALA 188
LYS 189
0.0215
LYS 189
ALA 190
-0.0000
ALA 190
GLY 191
-0.0170
GLY 191
LEU 192
-0.0001
LEU 192
THR 193
0.0071
THR 193
PHE 194
-0.0003
PHE 194
LEU 195
-0.0146
LEU 195
VAL 196
-0.0000
VAL 196
ASP 197
0.0067
ASP 197
LEU 198
-0.0000
LEU 198
ILE 199
0.0159
ILE 199
LYS 200
-0.0000
LYS 200
ASN 201
0.0860
ASN 201
LYS 202
-0.0001
LYS 202
HIS 203
-0.0409
HIS 203
MET 204
0.0001
MET 204
ASN 205
0.0558
ASN 205
ALA 206
0.0001
ALA 206
ASP 207
-0.0338
ASP 207
THR 208
0.0000
THR 208
ASP 209
-0.0155
ASP 209
TYR 210
-0.0001
TYR 210
SER 211
0.0337
SER 211
ILE 212
-0.0000
ILE 212
ALA 213
-0.0062
ALA 213
GLU 214
0.0000
GLU 214
ALA 215
0.0435
ALA 215
ALA 216
-0.0000
ALA 216
PHE 217
0.0054
PHE 217
ASN 218
-0.0004
ASN 218
LYS 219
0.0442
LYS 219
GLY 220
-0.0001
GLY 220
GLU 221
-0.0021
GLU 221
THR 222
-0.0003
THR 222
ALA 223
-0.0196
ALA 223
MET 224
-0.0002
MET 224
THR 225
0.0290
THR 225
ILE 226
-0.0002
ILE 226
ASN 227
0.0228
ASN 227
GLY 228
0.0001
GLY 228
PRO 229
0.0382
PRO 229
TRP 230
0.0003
TRP 230
ALA 231
0.0265
ALA 231
TRP 232
0.0000
TRP 232
SER 233
0.0080
SER 233
ASN 234
-0.0002
ASN 234
ILE 235
-0.0048
ILE 235
ASP 236
-0.0002
ASP 236
THR 237
0.0403
THR 237
SER 238
-0.0001
SER 238
LYS 239
0.0056
LYS 239
VAL 240
-0.0001
VAL 240
ASN 241
0.0131
ASN 241
TYR 242
-0.0000
TYR 242
GLY 243
-0.0023
GLY 243
VAL 244
-0.0001
VAL 244
THR 245
0.0185
THR 245
VAL 246
-0.0004
VAL 246
LEU 247
-0.0012
LEU 247
PRO 248
-0.0002
PRO 248
THR 249
0.0066
THR 249
PHE 250
-0.0002
PHE 250
LYS 251
0.0119
LYS 251
GLY 252
0.0000
GLY 252
GLN 253
0.0004
GLN 253
PRO 254
-0.0002
PRO 254
SER 255
0.0042
SER 255
LYS 256
-0.0002
LYS 256
PRO 257
0.0105
PRO 257
PHE 258
0.0000
PHE 258
VAL 259
0.0311
VAL 259
GLY 260
-0.0000
GLY 260
VAL 261
0.0351
VAL 261
LEU 262
0.0001
LEU 262
SER 263
0.0089
SER 263
ALA 264
-0.0003
ALA 264
GLY 265
0.0028
GLY 265
ILE 266
0.0000
ILE 266
ASN 267
0.0041
ASN 267
ALA 268
0.0003
ALA 268
ALA 269
0.0131
ALA 269
SER 270
0.0002
SER 270
PRO 271
-0.0067
PRO 271
ASN 272
-0.0002
ASN 272
LYS 273
0.0127
LYS 273
GLU 274
-0.0001
GLU 274
LEU 275
-0.0195
LEU 275
ALA 276
-0.0001
ALA 276
LYS 277
-0.0018
LYS 277
GLU 278
0.0001
GLU 278
PHE 279
-0.0011
PHE 279
LEU 280
-0.0001
LEU 280
GLU 281
-0.0160
GLU 281
ASN 282
-0.0002
ASN 282
TYR 283
-0.0283
TYR 283
LEU 284
0.0001
LEU 284
LEU 285
-0.0173
LEU 285
THR 286
-0.0003
THR 286
ASP 287
0.0207
ASP 287
GLU 288
0.0002
GLU 288
GLY 289
-0.0053
GLY 289
LEU 290
0.0001
LEU 290
GLU 291
-0.0007
GLU 291
ALA 292
-0.0002
ALA 292
VAL 293
-0.0018
VAL 293
ASN 294
0.0003
ASN 294
LYS 295
-0.0050
LYS 295
ASP 296
-0.0000
ASP 296
LYS 297
0.0051
LYS 297
PRO 298
0.0003
PRO 298
LEU 299
0.0195
LEU 299
GLY 300
0.0000
GLY 300
ALA 301
0.0348
ALA 301
VAL 302
-0.0000
VAL 302
ALA 303
0.0155
ALA 303
LEU 304
0.0002
LEU 304
LYS 305
-0.0039
LYS 305
SER 306
-0.0001
SER 306
TYR 307
-0.0087
TYR 307
GLU 308
-0.0000
GLU 308
GLU 309
-0.0105
GLU 309
GLU 310
-0.0000
GLU 310
LEU 311
0.0017
LEU 311
ALA 312
0.0000
ALA 312
LYS 313
-0.0088
LYS 313
ASP 314
-0.0001
ASP 314
PRO 315
-0.0273
PRO 315
ARG 316
-0.0002
ARG 316
ILE 317
0.0076
ILE 317
ALA 318
0.0002
ALA 318
ALA 319
-0.0049
ALA 319
THR 320
0.0003
THR 320
MET 321
0.0086
MET 321
GLU 322
0.0001
GLU 322
ASN 323
0.0005
ASN 323
ALA 324
0.0000
ALA 324
GLN 325
-0.0011
GLN 325
LYS 326
0.0001
LYS 326
GLY 327
-0.0053
GLY 327
GLU 328
0.0001
GLU 328
ILE 329
0.0412
ILE 329
MET 330
-0.0003
MET 330
PRO 331
0.0060
PRO 331
ASN 332
0.0000
ASN 332
ILE 333
-0.0011
ILE 333
PRO 334
-0.0001
PRO 334
GLN 335
0.0472
GLN 335
MET 336
0.0004
MET 336
SER 337
-0.0165
SER 337
ALA 338
-0.0001
ALA 338
PHE 339
-0.0095
PHE 339
TRP 340
0.0000
TRP 340
TYR 341
0.0010
TYR 341
ALA 342
-0.0001
ALA 342
VAL 343
-0.0220
VAL 343
ARG 344
0.0002
ARG 344
THR 345
-0.0121
THR 345
ALA 346
-0.0002
ALA 346
VAL 347
0.0146
VAL 347
ILE 348
-0.0004
ILE 348
ASN 349
-0.0135
ASN 349
ALA 350
0.0001
ALA 350
ALA 351
0.0089
ALA 351
SER 352
0.0003
SER 352
GLY 353
-0.0308
GLY 353
ARG 354
-0.0002
ARG 354
GLN 355
0.0186
GLN 355
THR 356
-0.0003
THR 356
VAL 357
0.0188
VAL 357
ASP 358
-0.0000
ASP 358
GLU 359
0.0025
GLU 359
ALA 360
0.0004
ALA 360
LEU 361
0.0132
LEU 361
LYS 362
-0.0001
LYS 362
ASP 363
-0.0123
ASP 363
ALA 364
0.0001
ALA 364
GLN 365
0.0262
GLN 365
THR 366
0.0002
THR 366
ARG 367
0.0258
ARG 367
ILE 368
-0.0004
ILE 368
THR 369
0.0329
THR 369
LYS 370
0.0004
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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.