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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
-0.0004
ILE 2
GLU 3
-0.0075
GLU 3
GLU 4
-0.0000
GLU 4
GLY 5
-0.0104
GLY 5
LYS 6
-0.0000
LYS 6
LEU 7
0.0046
LEU 7
VAL 8
-0.0001
VAL 8
ILE 9
-0.0001
ILE 9
TRP 10
0.0003
TRP 10
ILE 11
-0.0428
ILE 11
ASN 12
0.0000
ASN 12
GLY 13
-0.0031
GLY 13
ASP 14
0.0001
ASP 14
LYS 15
-0.0121
LYS 15
GLY 16
0.0001
GLY 16
TYR 17
0.0052
TYR 17
ASN 18
-0.0002
ASN 18
GLY 19
-0.0121
GLY 19
LEU 20
0.0001
LEU 20
ALA 21
0.0102
ALA 21
GLU 22
-0.0000
GLU 22
VAL 23
-0.0010
VAL 23
GLY 24
0.0002
GLY 24
LYS 25
-0.0083
LYS 25
LYS 26
-0.0001
LYS 26
PHE 27
-0.0016
PHE 27
GLU 28
0.0002
GLU 28
LYS 29
-0.0169
LYS 29
ASP 30
0.0003
ASP 30
THR 31
-0.0094
THR 31
GLY 32
0.0001
GLY 32
ILE 33
-0.0042
ILE 33
LYS 34
0.0001
LYS 34
VAL 35
0.0140
VAL 35
THR 36
-0.0000
THR 36
VAL 37
0.0184
VAL 37
GLU 38
0.0000
GLU 38
HIS 39
0.0148
HIS 39
PRO 40
-0.0001
PRO 40
ASP 41
0.0213
ASP 41
LYS 42
0.0004
LYS 42
LEU 43
-0.0060
LEU 43
GLU 44
0.0000
GLU 44
GLU 45
-0.0042
GLU 45
LYS 46
0.0002
LYS 46
PHE 47
0.0189
PHE 47
PRO 48
0.0001
PRO 48
GLN 49
0.0152
GLN 49
VAL 50
0.0001
VAL 50
ALA 51
0.0096
ALA 51
ALA 52
-0.0004
ALA 52
THR 53
0.0033
THR 53
GLY 54
-0.0004
GLY 54
ASP 55
-0.0092
ASP 55
GLY 56
-0.0002
GLY 56
PRO 57
-0.0104
PRO 57
ASP 58
-0.0001
ASP 58
ILE 59
-0.0122
ILE 59
ILE 60
0.0003
ILE 60
PHE 61
-0.0267
PHE 61
TRP 62
0.0003
TRP 62
ALA 63
0.0042
ALA 63
HIS 64
0.0001
HIS 64
ASP 65
0.0263
ASP 65
ARG 66
0.0002
ARG 66
PHE 67
-0.0007
PHE 67
GLY 68
0.0001
GLY 68
GLY 69
0.0195
GLY 69
TYR 70
-0.0002
TYR 70
ALA 71
0.0291
ALA 71
GLN 72
0.0001
GLN 72
SER 73
0.0339
SER 73
GLY 74
0.0005
GLY 74
LEU 75
-0.0018
LEU 75
LEU 76
-0.0001
LEU 76
ALA 77
0.0238
ALA 77
GLU 78
0.0001
GLU 78
ILE 79
0.0154
ILE 79
THR 80
0.0004
THR 80
PRO 81
0.0142
PRO 81
ASP 82
-0.0000
ASP 82
LYS 83
0.0382
LYS 83
ALA 84
0.0006
ALA 84
PHE 85
0.0110
PHE 85
GLN 86
0.0000
GLN 86
ASP 87
0.0329
ASP 87
LYS 88
-0.0004
LYS 88
LEU 89
-0.0043
LEU 89
TYR 90
0.0003
TYR 90
PRO 91
0.0169
PRO 91
PHE 92
-0.0001
PHE 92
THR 93
-0.0041
THR 93
TRP 94
-0.0001
TRP 94
ASP 95
-0.0008
ASP 95
ALA 96
0.0004
ALA 96
VAL 97
-0.0191
VAL 97
ARG 98
0.0003
ARG 98
TYR 99
0.0311
TYR 99
ASN 100
-0.0002
ASN 100
GLY 101
0.0129
GLY 101
LYS 102
-0.0002
LYS 102
LEU 103
-0.0007
LEU 103
ILE 104
-0.0000
ILE 104
ALA 105
-0.0047
ALA 105
TYR 106
0.0002
TYR 106
PRO 107
-0.0315
PRO 107
ILE 108
0.0001
ILE 108
ALA 109
-0.0402
ALA 109
VAL 110
0.0001
VAL 110
GLU 111
-0.0509
GLU 111
ALA 112
-0.0002
ALA 112
LEU 113
-0.0655
LEU 113
SER 114
0.0003
SER 114
LEU 115
-0.0501
LEU 115
ILE 116
0.0003
ILE 116
TYR 117
-0.0358
TYR 117
ASN 118
-0.0000
ASN 118
LYS 119
0.0272
LYS 119
ASP 120
0.0001
ASP 120
LEU 121
-0.0218
LEU 121
LEU 122
0.0003
LEU 122
PRO 123
0.0262
PRO 123
ASN 124
0.0002
ASN 124
PRO 125
-0.0160
PRO 125
PRO 126
0.0001
PRO 126
LYS 127
0.0088
LYS 127
THR 128
0.0002
THR 128
TRP 129
0.0031
TRP 129
GLU 130
-0.0001
GLU 130
GLU 131
0.0015
GLU 131
ILE 132
0.0002
ILE 132
PRO 133
-0.0145
PRO 133
ALA 134
0.0000
ALA 134
LEU 135
-0.0070
LEU 135
ASP 136
0.0003
ASP 136
LYS 137
-0.0205
LYS 137
GLU 138
0.0003
GLU 138
LEU 139
-0.0132
LEU 139
LYS 140
0.0001
LYS 140
ALA 141
0.0184
ALA 141
LYS 142
0.0002
LYS 142
GLY 143
0.0030
GLY 143
LYS 144
0.0004
LYS 144
SER 145
0.0319
SER 145
ALA 146
0.0001
ALA 146
LEU 147
-0.0097
LEU 147
MET 148
0.0001
MET 148
PHE 149
-0.0127
PHE 149
ASN 150
0.0001
ASN 150
LEU 151
0.0361
LEU 151
GLN 152
0.0001
GLN 152
GLU 153
-0.0317
GLU 153
PRO 154
0.0000
PRO 154
TYR 155
0.0555
TYR 155
PHE 156
0.0001
PHE 156
THR 157
0.0222
THR 157
TRP 158
-0.0004
TRP 158
PRO 159
-0.0058
PRO 159
LEU 160
-0.0001
LEU 160
ILE 161
0.0048
ILE 161
ALA 162
-0.0001
ALA 162
ALA 163
-0.0096
ALA 163
ASP 164
0.0002
ASP 164
GLY 165
-0.0082
GLY 165
GLY 166
0.0001
GLY 166
TYR 167
-0.0120
TYR 167
ALA 168
-0.0001
ALA 168
PHE 169
-0.0067
PHE 169
LYS 170
0.0001
LYS 170
TYR 171
-0.0003
TYR 171
GLU 172
-0.0000
GLU 172
ASN 173
0.0044
ASN 173
GLY 174
0.0004
GLY 174
LYS 175
0.0076
LYS 175
TYR 176
0.0002
TYR 176
ASP 177
-0.0029
ASP 177
ILE 178
-0.0002
ILE 178
LYS 179
0.0101
LYS 179
ASP 180
-0.0001
ASP 180
VAL 181
0.0138
VAL 181
GLY 182
0.0002
GLY 182
VAL 183
0.0107
VAL 183
ASP 184
-0.0000
ASP 184
ASN 185
-0.0136
ASN 185
ALA 186
-0.0002
ALA 186
GLY 187
-0.0087
GLY 187
ALA 188
0.0007
ALA 188
LYS 189
0.0001
LYS 189
ALA 190
0.0002
ALA 190
GLY 191
-0.0058
GLY 191
LEU 192
-0.0001
LEU 192
THR 193
-0.0088
THR 193
PHE 194
0.0001
PHE 194
LEU 195
0.0014
LEU 195
VAL 196
-0.0001
VAL 196
ASP 197
-0.0097
ASP 197
LEU 198
0.0002
LEU 198
ILE 199
0.0023
ILE 199
LYS 200
0.0003
LYS 200
ASN 201
0.0234
ASN 201
LYS 202
0.0001
LYS 202
HIS 203
-0.0305
HIS 203
MET 204
0.0000
MET 204
ASN 205
0.0169
ASN 205
ALA 206
0.0000
ALA 206
ASP 207
0.0147
ASP 207
THR 208
0.0001
THR 208
ASP 209
-0.0172
ASP 209
TYR 210
0.0001
TYR 210
SER 211
-0.0100
SER 211
ILE 212
-0.0001
ILE 212
ALA 213
-0.0078
ALA 213
GLU 214
-0.0001
GLU 214
ALA 215
-0.0332
ALA 215
ALA 216
0.0001
ALA 216
PHE 217
0.0015
PHE 217
ASN 218
0.0002
ASN 218
LYS 219
-0.0494
LYS 219
GLY 220
0.0000
GLY 220
GLU 221
-0.0033
GLU 221
THR 222
-0.0003
THR 222
ALA 223
0.0106
ALA 223
MET 224
-0.0004
MET 224
THR 225
-0.0201
THR 225
ILE 226
0.0004
ILE 226
ASN 227
-0.0191
ASN 227
GLY 228
-0.0004
GLY 228
PRO 229
0.0047
PRO 229
TRP 230
0.0001
TRP 230
ALA 231
-0.0447
ALA 231
TRP 232
0.0003
TRP 232
SER 233
0.0208
SER 233
ASN 234
0.0001
ASN 234
ILE 235
-0.0194
ILE 235
ASP 236
-0.0002
ASP 236
THR 237
-0.0058
THR 237
SER 238
-0.0002
SER 238
LYS 239
0.0132
LYS 239
VAL 240
0.0003
VAL 240
ASN 241
0.0173
ASN 241
TYR 242
0.0002
TYR 242
GLY 243
-0.0193
GLY 243
VAL 244
0.0001
VAL 244
THR 245
0.0204
THR 245
VAL 246
-0.0001
VAL 246
LEU 247
0.0012
LEU 247
PRO 248
0.0001
PRO 248
THR 249
0.0083
THR 249
PHE 250
0.0005
PHE 250
LYS 251
0.0003
LYS 251
GLY 252
-0.0000
GLY 252
GLN 253
-0.0019
GLN 253
PRO 254
-0.0004
PRO 254
SER 255
-0.0001
SER 255
LYS 256
-0.0001
LYS 256
PRO 257
-0.0117
PRO 257
PHE 258
-0.0002
PHE 258
VAL 259
0.0236
VAL 259
GLY 260
0.0005
GLY 260
VAL 261
-0.0167
VAL 261
LEU 262
-0.0001
LEU 262
SER 263
-0.0488
SER 263
ALA 264
-0.0001
ALA 264
GLY 265
-0.0238
GLY 265
ILE 266
-0.0000
ILE 266
ASN 267
0.0163
ASN 267
ALA 268
0.0000
ALA 268
ALA 269
-0.0039
ALA 269
SER 270
-0.0002
SER 270
PRO 271
-0.0087
PRO 271
ASN 272
-0.0003
ASN 272
LYS 273
-0.0138
LYS 273
GLU 274
-0.0001
GLU 274
LEU 275
-0.0162
LEU 275
ALA 276
0.0003
ALA 276
LYS 277
0.0093
LYS 277
GLU 278
-0.0001
GLU 278
PHE 279
0.0011
PHE 279
LEU 280
0.0002
LEU 280
GLU 281
0.0119
GLU 281
ASN 282
0.0002
ASN 282
TYR 283
-0.0117
TYR 283
LEU 284
-0.0001
LEU 284
LEU 285
-0.0051
LEU 285
THR 286
-0.0004
THR 286
ASP 287
0.0093
ASP 287
GLU 288
0.0002
GLU 288
GLY 289
-0.0026
GLY 289
LEU 290
0.0002
LEU 290
GLU 291
0.0081
GLU 291
ALA 292
0.0002
ALA 292
VAL 293
0.0079
VAL 293
ASN 294
-0.0000
ASN 294
LYS 295
0.0062
LYS 295
ASP 296
-0.0001
ASP 296
LYS 297
0.0338
LYS 297
PRO 298
0.0000
PRO 298
LEU 299
-0.0632
LEU 299
GLY 300
-0.0005
GLY 300
ALA 301
-0.0516
ALA 301
VAL 302
0.0002
VAL 302
ALA 303
-0.0501
ALA 303
LEU 304
0.0002
LEU 304
LYS 305
0.0132
LYS 305
SER 306
-0.0003
SER 306
TYR 307
-0.0078
TYR 307
GLU 308
-0.0003
GLU 308
GLU 309
0.0232
GLU 309
GLU 310
-0.0001
GLU 310
LEU 311
-0.0080
LEU 311
ALA 312
0.0002
ALA 312
LYS 313
0.0139
LYS 313
ASP 314
-0.0001
ASP 314
PRO 315
-0.0410
PRO 315
ARG 316
0.0004
ARG 316
ILE 317
-0.0661
ILE 317
ALA 318
-0.0001
ALA 318
ALA 319
-0.0044
ALA 319
THR 320
0.0001
THR 320
MET 321
-0.0233
MET 321
GLU 322
-0.0001
GLU 322
ASN 323
0.0144
ASN 323
ALA 324
0.0003
ALA 324
GLN 325
-0.0012
GLN 325
LYS 326
-0.0001
LYS 326
GLY 327
-0.0314
GLY 327
GLU 328
0.0000
GLU 328
ILE 329
-0.0387
ILE 329
MET 330
0.0004
MET 330
PRO 331
-0.0411
PRO 331
ASN 332
-0.0000
ASN 332
ILE 333
0.0074
ILE 333
PRO 334
-0.0001
PRO 334
GLN 335
-0.0017
GLN 335
MET 336
0.0001
MET 336
SER 337
0.0127
SER 337
ALA 338
-0.0000
ALA 338
PHE 339
0.0078
PHE 339
TRP 340
0.0002
TRP 340
TYR 341
0.0128
TYR 341
ALA 342
-0.0001
ALA 342
VAL 343
0.0014
VAL 343
ARG 344
-0.0002
ARG 344
THR 345
0.0082
THR 345
ALA 346
0.0002
ALA 346
VAL 347
0.0238
VAL 347
ILE 348
-0.0004
ILE 348
ASN 349
0.0275
ASN 349
ALA 350
-0.0002
ALA 350
ALA 351
0.0355
ALA 351
SER 352
-0.0002
SER 352
GLY 353
0.0361
GLY 353
ARG 354
-0.0000
ARG 354
GLN 355
-0.0101
GLN 355
THR 356
0.0001
THR 356
VAL 357
-0.0170
VAL 357
ASP 358
-0.0001
ASP 358
GLU 359
-0.0063
GLU 359
ALA 360
0.0003
ALA 360
LEU 361
0.0010
LEU 361
LYS 362
-0.0004
LYS 362
ASP 363
-0.0097
ASP 363
ALA 364
-0.0000
ALA 364
GLN 365
0.0156
GLN 365
THR 366
0.0002
THR 366
ARG 367
0.0128
ARG 367
ILE 368
0.0002
ILE 368
THR 369
0.0078
THR 369
LYS 370
-0.0001
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.