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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
-0.0003
ILE 2
GLU 3
0.0003
GLU 3
GLU 4
0.0001
GLU 4
GLY 5
-0.0038
GLY 5
LYS 6
0.0002
LYS 6
LEU 7
0.0047
LEU 7
VAL 8
-0.0003
VAL 8
ILE 9
0.0078
ILE 9
TRP 10
0.0002
TRP 10
ILE 11
0.0156
ILE 11
ASN 12
-0.0003
ASN 12
GLY 13
0.0117
GLY 13
ASP 14
-0.0000
ASP 14
LYS 15
0.0191
LYS 15
GLY 16
-0.0003
GLY 16
TYR 17
0.0188
TYR 17
ASN 18
-0.0001
ASN 18
GLY 19
-0.0242
GLY 19
LEU 20
0.0001
LEU 20
ALA 21
-0.0031
ALA 21
GLU 22
0.0002
GLU 22
VAL 23
-0.0081
VAL 23
GLY 24
0.0003
GLY 24
LYS 25
-0.0134
LYS 25
LYS 26
0.0001
LYS 26
PHE 27
-0.0057
PHE 27
GLU 28
-0.0001
GLU 28
LYS 29
-0.0217
LYS 29
ASP 30
-0.0005
ASP 30
THR 31
-0.0163
THR 31
GLY 32
-0.0001
GLY 32
ILE 33
-0.0086
ILE 33
LYS 34
0.0003
LYS 34
VAL 35
0.0109
VAL 35
THR 36
0.0001
THR 36
VAL 37
0.0224
VAL 37
GLU 38
-0.0003
GLU 38
HIS 39
0.0067
HIS 39
PRO 40
-0.0000
PRO 40
ASP 41
0.0006
ASP 41
LYS 42
-0.0006
LYS 42
LEU 43
0.0007
LEU 43
GLU 44
0.0002
GLU 44
GLU 45
0.0018
GLU 45
LYS 46
-0.0002
LYS 46
PHE 47
0.0041
PHE 47
PRO 48
-0.0002
PRO 48
GLN 49
0.0093
GLN 49
VAL 50
-0.0000
VAL 50
ALA 51
0.0011
ALA 51
ALA 52
-0.0004
ALA 52
THR 53
0.0011
THR 53
GLY 54
0.0000
GLY 54
ASP 55
0.0021
ASP 55
GLY 56
0.0000
GLY 56
PRO 57
0.0001
PRO 57
ASP 58
0.0000
ASP 58
ILE 59
0.0010
ILE 59
ILE 60
-0.0003
ILE 60
PHE 61
0.0010
PHE 61
TRP 62
-0.0000
TRP 62
ALA 63
-0.0097
ALA 63
HIS 64
-0.0002
HIS 64
ASP 65
-0.0138
ASP 65
ARG 66
0.0001
ARG 66
PHE 67
-0.0218
PHE 67
GLY 68
0.0001
GLY 68
GLY 69
0.0074
GLY 69
TYR 70
-0.0003
TYR 70
ALA 71
0.0204
ALA 71
GLN 72
0.0004
GLN 72
SER 73
0.0223
SER 73
GLY 74
0.0003
GLY 74
LEU 75
0.0031
LEU 75
LEU 76
0.0005
LEU 76
ALA 77
0.0057
ALA 77
GLU 78
0.0001
GLU 78
ILE 79
0.0073
ILE 79
THR 80
0.0000
THR 80
PRO 81
0.0089
PRO 81
ASP 82
-0.0000
ASP 82
LYS 83
0.0024
LYS 83
ALA 84
-0.0000
ALA 84
PHE 85
0.0135
PHE 85
GLN 86
0.0003
GLN 86
ASP 87
0.0057
ASP 87
LYS 88
-0.0001
LYS 88
LEU 89
-0.0042
LEU 89
TYR 90
-0.0004
TYR 90
PRO 91
0.0034
PRO 91
PHE 92
0.0001
PHE 92
THR 93
0.0039
THR 93
TRP 94
0.0002
TRP 94
ASP 95
-0.0317
ASP 95
ALA 96
-0.0002
ALA 96
VAL 97
-0.0076
VAL 97
ARG 98
0.0000
ARG 98
TYR 99
0.0082
TYR 99
ASN 100
-0.0001
ASN 100
GLY 101
-0.0046
GLY 101
LYS 102
0.0005
LYS 102
LEU 103
0.0051
LEU 103
ILE 104
0.0001
ILE 104
ALA 105
-0.0033
ALA 105
TYR 106
0.0002
TYR 106
PRO 107
0.0103
PRO 107
ILE 108
-0.0002
ILE 108
ALA 109
0.0165
ALA 109
VAL 110
-0.0000
VAL 110
GLU 111
0.0022
GLU 111
ALA 112
-0.0002
ALA 112
LEU 113
-0.0069
LEU 113
SER 114
0.0001
SER 114
LEU 115
-0.0071
LEU 115
ILE 116
0.0002
ILE 116
TYR 117
0.0055
TYR 117
ASN 118
0.0005
ASN 118
LYS 119
-0.0056
LYS 119
ASP 120
-0.0001
ASP 120
LEU 121
0.0123
LEU 121
LEU 122
-0.0001
LEU 122
PRO 123
-0.0023
PRO 123
ASN 124
0.0004
ASN 124
PRO 125
-0.0059
PRO 125
PRO 126
0.0001
PRO 126
LYS 127
-0.0109
LYS 127
THR 128
0.0002
THR 128
TRP 129
0.0045
TRP 129
GLU 130
-0.0002
GLU 130
GLU 131
-0.0226
GLU 131
ILE 132
-0.0001
ILE 132
PRO 133
0.0121
PRO 133
ALA 134
-0.0000
ALA 134
LEU 135
0.0239
LEU 135
ASP 136
-0.0002
ASP 136
LYS 137
0.0100
LYS 137
GLU 138
-0.0001
GLU 138
LEU 139
0.0127
LEU 139
LYS 140
-0.0002
LYS 140
ALA 141
0.0030
ALA 141
LYS 142
0.0001
LYS 142
GLY 143
0.0050
GLY 143
LYS 144
-0.0000
LYS 144
SER 145
-0.0089
SER 145
ALA 146
0.0002
ALA 146
LEU 147
-0.0031
LEU 147
MET 148
0.0003
MET 148
PHE 149
-0.0017
PHE 149
ASN 150
-0.0002
ASN 150
LEU 151
0.0134
LEU 151
GLN 152
0.0003
GLN 152
GLU 153
-0.0133
GLU 153
PRO 154
-0.0002
PRO 154
TYR 155
0.0058
TYR 155
PHE 156
0.0000
PHE 156
THR 157
0.0116
THR 157
TRP 158
0.0003
TRP 158
PRO 159
-0.0038
PRO 159
LEU 160
-0.0003
LEU 160
ILE 161
-0.0073
ILE 161
ALA 162
-0.0002
ALA 162
ALA 163
-0.0147
ALA 163
ASP 164
0.0002
ASP 164
GLY 165
-0.0410
GLY 165
GLY 166
0.0003
GLY 166
TYR 167
-0.0319
TYR 167
ALA 168
0.0002
ALA 168
PHE 169
-0.0157
PHE 169
LYS 170
-0.0002
LYS 170
TYR 171
-0.0026
TYR 171
GLU 172
-0.0001
GLU 172
ASN 173
-0.0101
ASN 173
GLY 174
0.0001
GLY 174
LYS 175
0.0183
LYS 175
TYR 176
-0.0001
TYR 176
ASP 177
-0.0154
ASP 177
ILE 178
0.0002
ILE 178
LYS 179
-0.0138
LYS 179
ASP 180
-0.0004
ASP 180
VAL 181
0.0030
VAL 181
GLY 182
0.0001
GLY 182
VAL 183
0.0026
VAL 183
ASP 184
0.0003
ASP 184
ASN 185
0.0003
ASN 185
ALA 186
-0.0001
ALA 186
GLY 187
0.0070
GLY 187
ALA 188
-0.0001
ALA 188
LYS 189
-0.0019
LYS 189
ALA 190
0.0003
ALA 190
GLY 191
0.0069
GLY 191
LEU 192
-0.0001
LEU 192
THR 193
-0.0035
THR 193
PHE 194
0.0001
PHE 194
LEU 195
0.0041
LEU 195
VAL 196
-0.0001
VAL 196
ASP 197
-0.0019
ASP 197
LEU 198
0.0002
LEU 198
ILE 199
0.0070
ILE 199
LYS 200
0.0002
LYS 200
ASN 201
0.0027
ASN 201
LYS 202
0.0002
LYS 202
HIS 203
0.0057
HIS 203
MET 204
-0.0003
MET 204
ASN 205
0.0040
ASN 205
ALA 206
0.0002
ALA 206
ASP 207
0.0005
ASP 207
THR 208
-0.0001
THR 208
ASP 209
-0.0016
ASP 209
TYR 210
0.0005
TYR 210
SER 211
0.0074
SER 211
ILE 212
-0.0001
ILE 212
ALA 213
-0.0047
ALA 213
GLU 214
-0.0002
GLU 214
ALA 215
0.0037
ALA 215
ALA 216
0.0002
ALA 216
PHE 217
-0.0017
PHE 217
ASN 218
0.0005
ASN 218
LYS 219
0.0141
LYS 219
GLY 220
-0.0001
GLY 220
GLU 221
0.0027
GLU 221
THR 222
-0.0001
THR 222
ALA 223
-0.0105
ALA 223
MET 224
-0.0002
MET 224
THR 225
0.0053
THR 225
ILE 226
0.0002
ILE 226
ASN 227
0.0291
ASN 227
GLY 228
0.0002
GLY 228
PRO 229
0.0228
PRO 229
TRP 230
-0.0002
TRP 230
ALA 231
0.0235
ALA 231
TRP 232
0.0003
TRP 232
SER 233
0.0099
SER 233
ASN 234
-0.0003
ASN 234
ILE 235
0.0419
ILE 235
ASP 236
-0.0003
ASP 236
THR 237
-0.0206
THR 237
SER 238
0.0002
SER 238
LYS 239
0.0034
LYS 239
VAL 240
-0.0002
VAL 240
ASN 241
-0.0079
ASN 241
TYR 242
-0.0003
TYR 242
GLY 243
-0.0255
GLY 243
VAL 244
0.0005
VAL 244
THR 245
0.0026
THR 245
VAL 246
0.0001
VAL 246
LEU 247
0.0184
LEU 247
PRO 248
0.0001
PRO 248
THR 249
0.0114
THR 249
PHE 250
0.0004
PHE 250
LYS 251
0.0062
LYS 251
GLY 252
-0.0002
GLY 252
GLN 253
-0.0035
GLN 253
PRO 254
-0.0003
PRO 254
SER 255
0.0001
SER 255
LYS 256
-0.0002
LYS 256
PRO 257
-0.0033
PRO 257
PHE 258
0.0001
PHE 258
VAL 259
0.0018
VAL 259
GLY 260
0.0002
GLY 260
VAL 261
-0.0053
VAL 261
LEU 262
-0.0000
LEU 262
SER 263
0.0118
SER 263
ALA 264
0.0001
ALA 264
GLY 265
0.0034
GLY 265
ILE 266
-0.0002
ILE 266
ASN 267
0.0183
ASN 267
ALA 268
-0.0000
ALA 268
ALA 269
-0.0025
ALA 269
SER 270
0.0002
SER 270
PRO 271
-0.0082
PRO 271
ASN 272
-0.0001
ASN 272
LYS 273
-0.0046
LYS 273
GLU 274
-0.0000
GLU 274
LEU 275
-0.0160
LEU 275
ALA 276
0.0001
ALA 276
LYS 277
0.0036
LYS 277
GLU 278
0.0000
GLU 278
PHE 279
0.0102
PHE 279
LEU 280
0.0001
LEU 280
GLU 281
-0.0004
GLU 281
ASN 282
-0.0001
ASN 282
TYR 283
-0.0092
TYR 283
LEU 284
0.0002
LEU 284
LEU 285
-0.0082
LEU 285
THR 286
0.0002
THR 286
ASP 287
0.0142
ASP 287
GLU 288
0.0000
GLU 288
GLY 289
-0.0086
GLY 289
LEU 290
0.0000
LEU 290
GLU 291
-0.0010
GLU 291
ALA 292
0.0002
ALA 292
VAL 293
-0.0163
VAL 293
ASN 294
-0.0000
ASN 294
LYS 295
-0.0016
LYS 295
ASP 296
0.0003
ASP 296
LYS 297
0.0108
LYS 297
PRO 298
-0.0003
PRO 298
LEU 299
0.0348
LEU 299
GLY 300
-0.0002
GLY 300
ALA 301
0.0117
ALA 301
VAL 302
0.0000
VAL 302
ALA 303
0.0127
ALA 303
LEU 304
-0.0001
LEU 304
LYS 305
-0.0051
LYS 305
SER 306
0.0002
SER 306
TYR 307
-0.0036
TYR 307
GLU 308
0.0002
GLU 308
GLU 309
-0.0068
GLU 309
GLU 310
-0.0003
GLU 310
LEU 311
0.0046
LEU 311
ALA 312
-0.0001
ALA 312
LYS 313
-0.0037
LYS 313
ASP 314
0.0002
ASP 314
PRO 315
0.0501
PRO 315
ARG 316
-0.0002
ARG 316
ILE 317
0.0179
ILE 317
ALA 318
-0.0002
ALA 318
ALA 319
0.0165
ALA 319
THR 320
0.0003
THR 320
MET 321
-0.0046
MET 321
GLU 322
-0.0004
GLU 322
ASN 323
0.0022
ASN 323
ALA 324
0.0002
ALA 324
GLN 325
0.0045
GLN 325
LYS 326
0.0001
LYS 326
GLY 327
-0.0247
GLY 327
GLU 328
0.0001
GLU 328
ILE 329
-0.0193
ILE 329
MET 330
-0.0001
MET 330
PRO 331
-0.0031
PRO 331
ASN 332
-0.0006
ASN 332
ILE 333
-0.0131
ILE 333
PRO 334
-0.0001
PRO 334
GLN 335
-0.0742
GLN 335
MET 336
0.0000
MET 336
SER 337
0.0252
SER 337
ALA 338
0.0002
ALA 338
PHE 339
-0.0052
PHE 339
TRP 340
0.0004
TRP 340
TYR 341
-0.0007
TYR 341
ALA 342
0.0001
ALA 342
VAL 343
0.0065
VAL 343
ARG 344
0.0003
ARG 344
THR 345
-0.0085
THR 345
ALA 346
-0.0001
ALA 346
VAL 347
0.0155
VAL 347
ILE 348
0.0003
ILE 348
ASN 349
0.0071
ASN 349
ALA 350
0.0001
ALA 350
ALA 351
0.0072
ALA 351
SER 352
0.0004
SER 352
GLY 353
0.0033
GLY 353
ARG 354
-0.0002
ARG 354
GLN 355
0.0074
GLN 355
THR 356
0.0003
THR 356
VAL 357
0.0063
VAL 357
ASP 358
-0.0002
ASP 358
GLU 359
0.0075
GLU 359
ALA 360
-0.0000
ALA 360
LEU 361
0.0022
LEU 361
LYS 362
-0.0002
LYS 362
ASP 363
-0.0016
ASP 363
ALA 364
0.0003
ALA 364
GLN 365
0.0132
GLN 365
THR 366
-0.0003
THR 366
ARG 367
-0.0113
ARG 367
ILE 368
0.0000
ILE 368
THR 369
0.0251
THR 369
LYS 370
-0.0000
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.