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***  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
0.0002
ILE 2
GLU 3
-0.0042
GLU 3
GLU 4
-0.0001
GLU 4
GLY 5
0.0188
GLY 5
LYS 6
0.0002
LYS 6
LEU 7
-0.0134
LEU 7
VAL 8
-0.0005
VAL 8
ILE 9
-0.0322
ILE 9
TRP 10
-0.0001
TRP 10
ILE 11
-0.0331
ILE 11
ASN 12
0.0004
ASN 12
GLY 13
0.0148
GLY 13
ASP 14
0.0001
ASP 14
LYS 15
-0.0065
LYS 15
GLY 16
0.0002
GLY 16
TYR 17
-0.0290
TYR 17
ASN 18
-0.0003
ASN 18
GLY 19
0.0357
GLY 19
LEU 20
0.0001
LEU 20
ALA 21
-0.0076
ALA 21
GLU 22
-0.0004
GLU 22
VAL 23
0.0205
VAL 23
GLY 24
-0.0000
GLY 24
LYS 25
0.0158
LYS 25
LYS 26
-0.0001
LYS 26
PHE 27
0.0044
PHE 27
GLU 28
0.0001
GLU 28
LYS 29
0.0193
LYS 29
ASP 30
0.0003
ASP 30
THR 31
0.0178
THR 31
GLY 32
0.0003
GLY 32
ILE 33
-0.0000
ILE 33
LYS 34
0.0002
LYS 34
VAL 35
-0.0263
VAL 35
THR 36
0.0000
THR 36
VAL 37
-0.0471
VAL 37
GLU 38
0.0000
GLU 38
HIS 39
-0.0161
HIS 39
PRO 40
-0.0002
PRO 40
ASP 41
0.0001
ASP 41
LYS 42
-0.0003
LYS 42
LEU 43
0.0232
LEU 43
GLU 44
-0.0000
GLU 44
GLU 45
0.0133
GLU 45
LYS 46
0.0000
LYS 46
PHE 47
-0.0015
PHE 47
PRO 48
-0.0004
PRO 48
GLN 49
-0.0068
GLN 49
VAL 50
0.0001
VAL 50
ALA 51
0.0001
ALA 51
ALA 52
-0.0001
ALA 52
THR 53
0.0023
THR 53
GLY 54
0.0003
GLY 54
ASP 55
-0.0041
ASP 55
GLY 56
0.0002
GLY 56
PRO 57
0.0102
PRO 57
ASP 58
-0.0001
ASP 58
ILE 59
-0.0189
ILE 59
ILE 60
-0.0002
ILE 60
PHE 61
-0.0204
PHE 61
TRP 62
-0.0002
TRP 62
ALA 63
-0.0338
ALA 63
HIS 64
0.0002
HIS 64
ASP 65
-0.0350
ASP 65
ARG 66
-0.0001
ARG 66
PHE 67
-0.0346
PHE 67
GLY 68
0.0000
GLY 68
GLY 69
0.0001
GLY 69
TYR 70
-0.0004
TYR 70
ALA 71
0.0137
ALA 71
GLN 72
0.0002
GLN 72
SER 73
0.0066
SER 73
GLY 74
0.0003
GLY 74
LEU 75
-0.0000
LEU 75
LEU 76
0.0002
LEU 76
ALA 77
-0.0015
ALA 77
GLU 78
0.0001
GLU 78
ILE 79
0.0044
ILE 79
THR 80
0.0002
THR 80
PRO 81
0.0028
PRO 81
ASP 82
-0.0002
ASP 82
LYS 83
0.0197
LYS 83
ALA 84
-0.0003
ALA 84
PHE 85
0.0889
PHE 85
GLN 86
-0.0000
GLN 86
ASP 87
0.0217
ASP 87
LYS 88
-0.0002
LYS 88
LEU 89
-0.0200
LEU 89
TYR 90
-0.0003
TYR 90
PRO 91
0.0373
PRO 91
PHE 92
0.0000
PHE 92
THR 93
-0.0031
THR 93
TRP 94
-0.0001
TRP 94
ASP 95
-0.0305
ASP 95
ALA 96
0.0001
ALA 96
VAL 97
-0.0076
VAL 97
ARG 98
-0.0002
ARG 98
TYR 99
0.0012
TYR 99
ASN 100
0.0002
ASN 100
GLY 101
-0.0052
GLY 101
LYS 102
0.0000
LYS 102
LEU 103
-0.0026
LEU 103
ILE 104
0.0002
ILE 104
ALA 105
-0.0020
ALA 105
TYR 106
0.0000
TYR 106
PRO 107
0.0012
PRO 107
ILE 108
0.0001
ILE 108
ALA 109
-0.0474
ALA 109
VAL 110
0.0004
VAL 110
GLU 111
-0.0354
GLU 111
ALA 112
-0.0002
ALA 112
LEU 113
-0.0295
LEU 113
SER 114
-0.0000
SER 114
LEU 115
-0.0236
LEU 115
ILE 116
-0.0001
ILE 116
TYR 117
-0.0161
TYR 117
ASN 118
-0.0001
ASN 118
LYS 119
0.0039
LYS 119
ASP 120
0.0002
ASP 120
LEU 121
-0.0014
LEU 121
LEU 122
-0.0003
LEU 122
PRO 123
-0.0010
PRO 123
ASN 124
-0.0003
ASN 124
PRO 125
0.0208
PRO 125
PRO 126
0.0003
PRO 126
LYS 127
0.0163
LYS 127
THR 128
0.0003
THR 128
TRP 129
0.0322
TRP 129
GLU 130
0.0000
GLU 130
GLU 131
0.0054
GLU 131
ILE 132
0.0003
ILE 132
PRO 133
-0.0119
PRO 133
ALA 134
0.0003
ALA 134
LEU 135
0.0260
LEU 135
ASP 136
0.0002
ASP 136
LYS 137
-0.0114
LYS 137
GLU 138
0.0000
GLU 138
LEU 139
0.0084
LEU 139
LYS 140
0.0003
LYS 140
ALA 141
0.0286
ALA 141
LYS 142
0.0001
LYS 142
GLY 143
0.0248
GLY 143
LYS 144
0.0001
LYS 144
SER 145
0.0006
SER 145
ALA 146
0.0004
ALA 146
LEU 147
0.0064
LEU 147
MET 148
-0.0000
MET 148
PHE 149
0.0224
PHE 149
ASN 150
-0.0004
ASN 150
LEU 151
-0.0284
LEU 151
GLN 152
0.0005
GLN 152
GLU 153
0.0020
GLU 153
PRO 154
0.0001
PRO 154
TYR 155
-0.0415
TYR 155
PHE 156
-0.0001
PHE 156
THR 157
-0.0443
THR 157
TRP 158
0.0002
TRP 158
PRO 159
0.0056
PRO 159
LEU 160
-0.0002
LEU 160
ILE 161
0.0257
ILE 161
ALA 162
-0.0000
ALA 162
ALA 163
-0.0044
ALA 163
ASP 164
-0.0002
ASP 164
GLY 165
-0.0056
GLY 165
GLY 166
-0.0002
GLY 166
TYR 167
-0.0182
TYR 167
ALA 168
0.0002
ALA 168
PHE 169
0.0123
PHE 169
LYS 170
-0.0003
LYS 170
TYR 171
0.0055
TYR 171
GLU 172
-0.0002
GLU 172
ASN 173
0.0190
ASN 173
GLY 174
-0.0003
GLY 174
LYS 175
0.0076
LYS 175
TYR 176
-0.0003
TYR 176
ASP 177
-0.0003
ASP 177
ILE 178
0.0001
ILE 178
LYS 179
-0.0211
LYS 179
ASP 180
-0.0001
ASP 180
VAL 181
0.0106
VAL 181
GLY 182
-0.0004
GLY 182
VAL 183
0.0104
VAL 183
ASP 184
0.0001
ASP 184
ASN 185
0.0020
ASN 185
ALA 186
0.0001
ALA 186
GLY 187
0.0101
GLY 187
ALA 188
-0.0001
ALA 188
LYS 189
-0.0144
LYS 189
ALA 190
0.0002
ALA 190
GLY 191
0.0033
GLY 191
LEU 192
-0.0002
LEU 192
THR 193
-0.0264
THR 193
PHE 194
-0.0002
PHE 194
LEU 195
-0.0107
LEU 195
VAL 196
0.0000
VAL 196
ASP 197
0.0155
ASP 197
LEU 198
-0.0001
LEU 198
ILE 199
0.0011
ILE 199
LYS 200
0.0004
LYS 200
ASN 201
0.0578
ASN 201
LYS 202
-0.0001
LYS 202
HIS 203
-0.0253
HIS 203
MET 204
0.0000
MET 204
ASN 205
0.0237
ASN 205
ALA 206
0.0001
ALA 206
ASP 207
-0.0224
ASP 207
THR 208
-0.0002
THR 208
ASP 209
-0.0143
ASP 209
TYR 210
0.0001
TYR 210
SER 211
0.0159
SER 211
ILE 212
-0.0002
ILE 212
ALA 213
0.0019
ALA 213
GLU 214
-0.0004
GLU 214
ALA 215
0.0300
ALA 215
ALA 216
-0.0003
ALA 216
PHE 217
-0.0027
PHE 217
ASN 218
-0.0001
ASN 218
LYS 219
0.0298
LYS 219
GLY 220
0.0001
GLY 220
GLU 221
0.0013
GLU 221
THR 222
-0.0004
THR 222
ALA 223
-0.0002
ALA 223
MET 224
0.0001
MET 224
THR 225
-0.0043
THR 225
ILE 226
0.0002
ILE 226
ASN 227
-0.0484
ASN 227
GLY 228
0.0003
GLY 228
PRO 229
-0.0300
PRO 229
TRP 230
0.0002
TRP 230
ALA 231
-0.0062
ALA 231
TRP 232
0.0003
TRP 232
SER 233
-0.0032
SER 233
ASN 234
0.0001
ASN 234
ILE 235
-0.0305
ILE 235
ASP 236
0.0001
ASP 236
THR 237
0.0421
THR 237
SER 238
-0.0001
SER 238
LYS 239
-0.0070
LYS 239
VAL 240
-0.0004
VAL 240
ASN 241
0.0071
ASN 241
TYR 242
-0.0000
TYR 242
GLY 243
0.0374
GLY 243
VAL 244
0.0004
VAL 244
THR 245
0.0297
THR 245
VAL 246
0.0002
VAL 246
LEU 247
-0.0132
LEU 247
PRO 248
-0.0003
PRO 248
THR 249
0.0279
THR 249
PHE 250
0.0004
PHE 250
LYS 251
0.0011
LYS 251
GLY 252
0.0004
GLY 252
GLN 253
-0.0185
GLN 253
PRO 254
0.0002
PRO 254
SER 255
0.0002
SER 255
LYS 256
0.0001
LYS 256
PRO 257
-0.0347
PRO 257
PHE 258
-0.0003
PHE 258
VAL 259
-0.0677
VAL 259
GLY 260
-0.0000
GLY 260
VAL 261
-0.0535
VAL 261
LEU 262
-0.0002
LEU 262
SER 263
-0.0124
SER 263
ALA 264
-0.0003
ALA 264
GLY 265
-0.0110
GLY 265
ILE 266
0.0005
ILE 266
ASN 267
0.0175
ASN 267
ALA 268
0.0002
ALA 268
ALA 269
0.0065
ALA 269
SER 270
-0.0001
SER 270
PRO 271
-0.0092
PRO 271
ASN 272
0.0002
ASN 272
LYS 273
0.0162
LYS 273
GLU 274
0.0001
GLU 274
LEU 275
0.0017
LEU 275
ALA 276
-0.0004
ALA 276
LYS 277
0.0207
LYS 277
GLU 278
0.0001
GLU 278
PHE 279
-0.0090
PHE 279
LEU 280
0.0002
LEU 280
GLU 281
0.0246
GLU 281
ASN 282
-0.0005
ASN 282
TYR 283
0.0106
TYR 283
LEU 284
-0.0000
LEU 284
LEU 285
0.0130
LEU 285
THR 286
0.0004
THR 286
ASP 287
-0.0145
ASP 287
GLU 288
-0.0001
GLU 288
GLY 289
0.0024
GLY 289
LEU 290
-0.0001
LEU 290
GLU 291
0.0027
GLU 291
ALA 292
0.0002
ALA 292
VAL 293
0.0061
VAL 293
ASN 294
-0.0002
ASN 294
LYS 295
-0.0072
LYS 295
ASP 296
-0.0002
ASP 296
LYS 297
-0.0286
LYS 297
PRO 298
-0.0005
PRO 298
LEU 299
0.0132
LEU 299
GLY 300
-0.0000
GLY 300
ALA 301
-0.0049
ALA 301
VAL 302
0.0002
VAL 302
ALA 303
0.0065
ALA 303
LEU 304
0.0000
LEU 304
LYS 305
0.0059
LYS 305
SER 306
0.0001
SER 306
TYR 307
0.0148
TYR 307
GLU 308
-0.0002
GLU 308
GLU 309
-0.0056
GLU 309
GLU 310
0.0004
GLU 310
LEU 311
-0.0054
LEU 311
ALA 312
-0.0001
ALA 312
LYS 313
-0.0078
LYS 313
ASP 314
-0.0003
ASP 314
PRO 315
-0.0409
PRO 315
ARG 316
-0.0001
ARG 316
ILE 317
-0.0108
ILE 317
ALA 318
0.0001
ALA 318
ALA 319
-0.0408
ALA 319
THR 320
0.0002
THR 320
MET 321
0.0144
MET 321
GLU 322
0.0004
GLU 322
ASN 323
-0.0049
ASN 323
ALA 324
0.0004
ALA 324
GLN 325
-0.0111
GLN 325
LYS 326
-0.0002
LYS 326
GLY 327
0.0073
GLY 327
GLU 328
0.0003
GLU 328
ILE 329
-0.0722
ILE 329
MET 330
0.0001
MET 330
PRO 331
0.0160
PRO 331
ASN 332
-0.0000
ASN 332
ILE 333
-0.0070
ILE 333
PRO 334
0.0002
PRO 334
GLN 335
-0.0531
GLN 335
MET 336
-0.0000
MET 336
SER 337
0.0090
SER 337
ALA 338
-0.0002
ALA 338
PHE 339
-0.0042
PHE 339
TRP 340
0.0001
TRP 340
TYR 341
-0.0057
TYR 341
ALA 342
-0.0002
ALA 342
VAL 343
0.0164
VAL 343
ARG 344
-0.0003
ARG 344
THR 345
-0.0269
THR 345
ALA 346
0.0004
ALA 346
VAL 347
0.0210
VAL 347
ILE 348
-0.0002
ILE 348
ASN 349
-0.0354
ASN 349
ALA 350
0.0002
ALA 350
ALA 351
-0.0046
ALA 351
SER 352
0.0002
SER 352
GLY 353
-0.0427
GLY 353
ARG 354
0.0001
ARG 354
GLN 355
0.0146
GLN 355
THR 356
0.0000
THR 356
VAL 357
0.0063
VAL 357
ASP 358
-0.0002
ASP 358
GLU 359
0.0231
GLU 359
ALA 360
0.0003
ALA 360
LEU 361
-0.0001
LEU 361
LYS 362
0.0003
LYS 362
ASP 363
0.0012
ASP 363
ALA 364
-0.0000
ALA 364
GLN 365
0.0078
GLN 365
THR 366
0.0004
THR 366
ARG 367
-0.0187
ARG 367
ILE 368
0.0005
ILE 368
THR 369
0.0142
THR 369
LYS 370
0.0002
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.