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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
-0.0000
ILE 2
GLU 3
-0.0006
GLU 3
GLU 4
0.0001
GLU 4
GLY 5
-0.0059
GLY 5
LYS 6
-0.0003
LYS 6
LEU 7
0.0004
LEU 7
VAL 8
0.0000
VAL 8
ILE 9
-0.0042
ILE 9
TRP 10
0.0001
TRP 10
ILE 11
-0.0145
ILE 11
ASN 12
-0.0002
ASN 12
GLY 13
0.0003
GLY 13
ASP 14
-0.0002
ASP 14
LYS 15
-0.0064
LYS 15
GLY 16
-0.0005
GLY 16
TYR 17
0.0031
TYR 17
ASN 18
0.0000
ASN 18
GLY 19
-0.0103
GLY 19
LEU 20
0.0001
LEU 20
ALA 21
0.0014
ALA 21
GLU 22
0.0003
GLU 22
VAL 23
-0.0081
VAL 23
GLY 24
0.0003
GLY 24
LYS 25
-0.0027
LYS 25
LYS 26
-0.0001
LYS 26
PHE 27
-0.0050
PHE 27
GLU 28
-0.0001
GLU 28
LYS 29
-0.0181
LYS 29
ASP 30
-0.0001
ASP 30
THR 31
-0.0125
THR 31
GLY 32
-0.0003
GLY 32
ILE 33
-0.0102
ILE 33
LYS 34
-0.0003
LYS 34
VAL 35
-0.0017
VAL 35
THR 36
-0.0001
THR 36
VAL 37
-0.0045
VAL 37
GLU 38
-0.0002
GLU 38
HIS 39
-0.0106
HIS 39
PRO 40
0.0002
PRO 40
ASP 41
-0.0021
ASP 41
LYS 42
-0.0005
LYS 42
LEU 43
0.0155
LEU 43
GLU 44
-0.0000
GLU 44
GLU 45
0.0063
GLU 45
LYS 46
0.0002
LYS 46
PHE 47
0.0051
PHE 47
PRO 48
-0.0002
PRO 48
GLN 49
-0.0039
GLN 49
VAL 50
-0.0002
VAL 50
ALA 51
0.0002
ALA 51
ALA 52
0.0001
ALA 52
THR 53
-0.0101
THR 53
GLY 54
-0.0000
GLY 54
ASP 55
0.0026
ASP 55
GLY 56
-0.0003
GLY 56
PRO 57
0.0019
PRO 57
ASP 58
-0.0004
ASP 58
ILE 59
-0.0013
ILE 59
ILE 60
0.0002
ILE 60
PHE 61
-0.0090
PHE 61
TRP 62
-0.0000
TRP 62
ALA 63
0.0119
ALA 63
HIS 64
0.0001
HIS 64
ASP 65
0.0033
ASP 65
ARG 66
-0.0001
ARG 66
PHE 67
-0.0053
PHE 67
GLY 68
-0.0001
GLY 68
GLY 69
0.0119
GLY 69
TYR 70
-0.0000
TYR 70
ALA 71
0.0257
ALA 71
GLN 72
-0.0002
GLN 72
SER 73
-0.0001
SER 73
GLY 74
-0.0001
GLY 74
LEU 75
-0.0001
LEU 75
LEU 76
0.0001
LEU 76
ALA 77
0.0104
ALA 77
GLU 78
0.0000
GLU 78
ILE 79
0.0036
ILE 79
THR 80
-0.0000
THR 80
PRO 81
0.0069
PRO 81
ASP 82
-0.0002
ASP 82
LYS 83
0.0080
LYS 83
ALA 84
-0.0002
ALA 84
PHE 85
-0.0126
PHE 85
GLN 86
0.0003
GLN 86
ASP 87
0.0092
ASP 87
LYS 88
-0.0001
LYS 88
LEU 89
0.0035
LEU 89
TYR 90
0.0003
TYR 90
PRO 91
0.0051
PRO 91
PHE 92
0.0000
PHE 92
THR 93
-0.0048
THR 93
TRP 94
-0.0002
TRP 94
ASP 95
0.0109
ASP 95
ALA 96
-0.0000
ALA 96
VAL 97
-0.0030
VAL 97
ARG 98
-0.0001
ARG 98
TYR 99
0.0303
TYR 99
ASN 100
0.0000
ASN 100
GLY 101
0.0213
GLY 101
LYS 102
-0.0000
LYS 102
LEU 103
0.0014
LEU 103
ILE 104
0.0000
ILE 104
ALA 105
-0.0065
ALA 105
TYR 106
0.0001
TYR 106
PRO 107
0.0028
PRO 107
ILE 108
-0.0004
ILE 108
ALA 109
0.0083
ALA 109
VAL 110
0.0001
VAL 110
GLU 111
-0.0086
GLU 111
ALA 112
-0.0004
ALA 112
LEU 113
-0.0036
LEU 113
SER 114
-0.0001
SER 114
LEU 115
0.0068
LEU 115
ILE 116
0.0001
ILE 116
TYR 117
0.0008
TYR 117
ASN 118
0.0004
ASN 118
LYS 119
-0.0102
LYS 119
ASP 120
-0.0005
ASP 120
LEU 121
-0.0016
LEU 121
LEU 122
0.0003
LEU 122
PRO 123
-0.0114
PRO 123
ASN 124
0.0000
ASN 124
PRO 125
0.0052
PRO 125
PRO 126
0.0001
PRO 126
LYS 127
0.0067
LYS 127
THR 128
0.0001
THR 128
TRP 129
-0.0121
TRP 129
GLU 130
-0.0004
GLU 130
GLU 131
0.0142
GLU 131
ILE 132
0.0004
ILE 132
PRO 133
-0.0035
PRO 133
ALA 134
-0.0001
ALA 134
LEU 135
-0.0192
LEU 135
ASP 136
-0.0002
ASP 136
LYS 137
0.0015
LYS 137
GLU 138
-0.0001
GLU 138
LEU 139
-0.0054
LEU 139
LYS 140
-0.0000
LYS 140
ALA 141
-0.0266
ALA 141
LYS 142
-0.0003
LYS 142
GLY 143
-0.0071
GLY 143
LYS 144
0.0003
LYS 144
SER 145
-0.0137
SER 145
ALA 146
0.0002
ALA 146
LEU 147
-0.0125
LEU 147
MET 148
-0.0002
MET 148
PHE 149
-0.0283
PHE 149
ASN 150
0.0002
ASN 150
LEU 151
-0.0013
LEU 151
GLN 152
0.0002
GLN 152
GLU 153
-0.0102
GLU 153
PRO 154
0.0002
PRO 154
TYR 155
0.0203
TYR 155
PHE 156
0.0002
PHE 156
THR 157
0.0065
THR 157
TRP 158
0.0005
TRP 158
PRO 159
0.0065
PRO 159
LEU 160
-0.0001
LEU 160
ILE 161
0.0146
ILE 161
ALA 162
-0.0001
ALA 162
ALA 163
0.0094
ALA 163
ASP 164
0.0003
ASP 164
GLY 165
0.0424
GLY 165
GLY 166
-0.0001
GLY 166
TYR 167
0.0087
TYR 167
ALA 168
0.0001
ALA 168
PHE 169
0.0295
PHE 169
LYS 170
0.0005
LYS 170
TYR 171
0.0123
TYR 171
GLU 172
-0.0000
GLU 172
ASN 173
0.0531
ASN 173
GLY 174
0.0001
GLY 174
LYS 175
-0.0362
LYS 175
TYR 176
-0.0000
TYR 176
ASP 177
0.0482
ASP 177
ILE 178
0.0005
ILE 178
LYS 179
-0.0086
LYS 179
ASP 180
-0.0001
ASP 180
VAL 181
-0.0040
VAL 181
GLY 182
0.0001
GLY 182
VAL 183
-0.0007
VAL 183
ASP 184
-0.0003
ASP 184
ASN 185
0.0083
ASN 185
ALA 186
-0.0000
ALA 186
GLY 187
0.0043
GLY 187
ALA 188
-0.0002
ALA 188
LYS 189
0.0002
LYS 189
ALA 190
-0.0002
ALA 190
GLY 191
-0.0008
GLY 191
LEU 192
-0.0002
LEU 192
THR 193
-0.0054
THR 193
PHE 194
-0.0000
PHE 194
LEU 195
-0.0040
LEU 195
VAL 196
0.0001
VAL 196
ASP 197
-0.0117
ASP 197
LEU 198
-0.0003
LEU 198
ILE 199
-0.0073
ILE 199
LYS 200
0.0001
LYS 200
ASN 201
-0.0437
ASN 201
LYS 202
0.0005
LYS 202
HIS 203
0.0175
HIS 203
MET 204
-0.0002
MET 204
ASN 205
-0.0208
ASN 205
ALA 206
-0.0001
ALA 206
ASP 207
0.0062
ASP 207
THR 208
0.0000
THR 208
ASP 209
0.0196
ASP 209
TYR 210
-0.0001
TYR 210
SER 211
-0.0146
SER 211
ILE 212
0.0002
ILE 212
ALA 213
0.0097
ALA 213
GLU 214
-0.0002
GLU 214
ALA 215
-0.0015
ALA 215
ALA 216
0.0000
ALA 216
PHE 217
-0.0005
PHE 217
ASN 218
-0.0003
ASN 218
LYS 219
0.0063
LYS 219
GLY 220
0.0001
GLY 220
GLU 221
-0.0014
GLU 221
THR 222
0.0002
THR 222
ALA 223
0.0050
ALA 223
MET 224
0.0002
MET 224
THR 225
-0.0120
THR 225
ILE 226
0.0001
ILE 226
ASN 227
0.0004
ASN 227
GLY 228
-0.0000
GLY 228
PRO 229
0.0131
PRO 229
TRP 230
0.0002
TRP 230
ALA 231
0.0033
ALA 231
TRP 232
0.0000
TRP 232
SER 233
0.0081
SER 233
ASN 234
-0.0003
ASN 234
ILE 235
-0.0062
ILE 235
ASP 236
-0.0000
ASP 236
THR 237
0.0047
THR 237
SER 238
0.0003
SER 238
LYS 239
-0.0059
LYS 239
VAL 240
-0.0002
VAL 240
ASN 241
-0.0031
ASN 241
TYR 242
-0.0003
TYR 242
GLY 243
0.0193
GLY 243
VAL 244
0.0001
VAL 244
THR 245
0.0045
THR 245
VAL 246
-0.0001
VAL 246
LEU 247
0.0046
LEU 247
PRO 248
-0.0002
PRO 248
THR 249
0.0045
THR 249
PHE 250
0.0002
PHE 250
LYS 251
-0.0034
LYS 251
GLY 252
0.0000
GLY 252
GLN 253
-0.0014
GLN 253
PRO 254
0.0002
PRO 254
SER 255
-0.0108
SER 255
LYS 256
-0.0000
LYS 256
PRO 257
-0.0179
PRO 257
PHE 258
-0.0000
PHE 258
VAL 259
0.0025
VAL 259
GLY 260
0.0002
GLY 260
VAL 261
-0.0151
VAL 261
LEU 262
0.0001
LEU 262
SER 263
-0.0075
SER 263
ALA 264
-0.0004
ALA 264
GLY 265
-0.0015
GLY 265
ILE 266
0.0002
ILE 266
ASN 267
0.0202
ASN 267
ALA 268
-0.0001
ALA 268
ALA 269
-0.0026
ALA 269
SER 270
-0.0000
SER 270
PRO 271
-0.0098
PRO 271
ASN 272
-0.0002
ASN 272
LYS 273
0.0018
LYS 273
GLU 274
0.0001
GLU 274
LEU 275
-0.0131
LEU 275
ALA 276
0.0004
ALA 276
LYS 277
0.0057
LYS 277
GLU 278
0.0002
GLU 278
PHE 279
-0.0033
PHE 279
LEU 280
0.0000
LEU 280
GLU 281
-0.0015
GLU 281
ASN 282
-0.0003
ASN 282
TYR 283
-0.0108
TYR 283
LEU 284
-0.0002
LEU 284
LEU 285
0.0005
LEU 285
THR 286
-0.0001
THR 286
ASP 287
0.0152
ASP 287
GLU 288
0.0002
GLU 288
GLY 289
-0.0038
GLY 289
LEU 290
-0.0001
LEU 290
GLU 291
0.0028
GLU 291
ALA 292
-0.0000
ALA 292
VAL 293
-0.0051
VAL 293
ASN 294
-0.0003
ASN 294
LYS 295
-0.0000
LYS 295
ASP 296
0.0000
ASP 296
LYS 297
0.0117
LYS 297
PRO 298
0.0002
PRO 298
LEU 299
0.0100
LEU 299
GLY 300
-0.0001
GLY 300
ALA 301
-0.0027
ALA 301
VAL 302
-0.0002
VAL 302
ALA 303
-0.0004
ALA 303
LEU 304
0.0003
LEU 304
LYS 305
0.0002
LYS 305
SER 306
0.0001
SER 306
TYR 307
-0.0122
TYR 307
GLU 308
0.0002
GLU 308
GLU 309
-0.0035
GLU 309
GLU 310
-0.0002
GLU 310
LEU 311
0.0029
LEU 311
ALA 312
0.0000
ALA 312
LYS 313
-0.0035
LYS 313
ASP 314
0.0003
ASP 314
PRO 315
0.0348
PRO 315
ARG 316
-0.0003
ARG 316
ILE 317
0.0177
ILE 317
ALA 318
-0.0002
ALA 318
ALA 319
0.0108
ALA 319
THR 320
0.0001
THR 320
MET 321
-0.0065
MET 321
GLU 322
0.0001
GLU 322
ASN 323
0.0047
ASN 323
ALA 324
0.0002
ALA 324
GLN 325
-0.0135
GLN 325
LYS 326
0.0002
LYS 326
GLY 327
0.0345
GLY 327
GLU 328
0.0002
GLU 328
ILE 329
-0.0390
ILE 329
MET 330
0.0002
MET 330
PRO 331
-0.0015
PRO 331
ASN 332
0.0003
ASN 332
ILE 333
0.0177
ILE 333
PRO 334
0.0001
PRO 334
GLN 335
-0.0160
GLN 335
MET 336
0.0001
MET 336
SER 337
-0.0064
SER 337
ALA 338
0.0004
ALA 338
PHE 339
0.0153
PHE 339
TRP 340
0.0003
TRP 340
TYR 341
0.0148
TYR 341
ALA 342
0.0003
ALA 342
VAL 343
0.0092
VAL 343
ARG 344
0.0000
ARG 344
THR 345
0.0085
THR 345
ALA 346
-0.0000
ALA 346
VAL 347
-0.0184
VAL 347
ILE 348
0.0004
ILE 348
ASN 349
0.0048
ASN 349
ALA 350
0.0000
ALA 350
ALA 351
-0.0136
ALA 351
SER 352
0.0000
SER 352
GLY 353
0.0005
GLY 353
ARG 354
-0.0001
ARG 354
GLN 355
-0.0018
GLN 355
THR 356
0.0006
THR 356
VAL 357
0.0085
VAL 357
ASP 358
0.0001
ASP 358
GLU 359
0.0008
GLU 359
ALA 360
-0.0001
ALA 360
LEU 361
0.0022
LEU 361
LYS 362
0.0001
LYS 362
ASP 363
0.0158
ASP 363
ALA 364
-0.0004
ALA 364
GLN 365
-0.0275
GLN 365
THR 366
-0.0002
THR 366
ARG 367
0.0163
ARG 367
ILE 368
0.0004
ILE 368
THR 369
-0.0306
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.