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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
-0.0105
GLU 3
GLU 4
-0.0000
GLU 4
GLY 5
-0.0016
GLY 5
LYS 6
-0.0002
LYS 6
LEU 7
0.0046
LEU 7
VAL 8
-0.0001
VAL 8
ILE 9
0.0066
ILE 9
TRP 10
0.0001
TRP 10
ILE 11
0.0035
ILE 11
ASN 12
-0.0003
ASN 12
GLY 13
0.0086
GLY 13
ASP 14
0.0001
ASP 14
LYS 15
-0.0198
LYS 15
GLY 16
-0.0000
GLY 16
TYR 17
0.0049
TYR 17
ASN 18
-0.0002
ASN 18
GLY 19
-0.0004
GLY 19
LEU 20
-0.0002
LEU 20
ALA 21
0.0033
ALA 21
GLU 22
-0.0001
GLU 22
VAL 23
0.0213
VAL 23
GLY 24
0.0001
GLY 24
LYS 25
-0.0051
LYS 25
LYS 26
0.0001
LYS 26
PHE 27
0.0027
PHE 27
GLU 28
0.0000
GLU 28
LYS 29
0.0179
LYS 29
ASP 30
0.0001
ASP 30
THR 31
0.0107
THR 31
GLY 32
0.0002
GLY 32
ILE 33
0.0130
ILE 33
LYS 34
-0.0001
LYS 34
VAL 35
0.0146
VAL 35
THR 36
0.0001
THR 36
VAL 37
0.0231
VAL 37
GLU 38
0.0002
GLU 38
HIS 39
0.0234
HIS 39
PRO 40
0.0002
PRO 40
ASP 41
0.0129
ASP 41
LYS 42
-0.0002
LYS 42
LEU 43
-0.0184
LEU 43
GLU 44
0.0000
GLU 44
GLU 45
0.0025
GLU 45
LYS 46
-0.0000
LYS 46
PHE 47
-0.0059
PHE 47
PRO 48
0.0003
PRO 48
GLN 49
0.0157
GLN 49
VAL 50
0.0002
VAL 50
ALA 51
0.0049
ALA 51
ALA 52
0.0002
ALA 52
THR 53
0.0221
THR 53
GLY 54
-0.0001
GLY 54
ASP 55
-0.0110
ASP 55
GLY 56
0.0001
GLY 56
PRO 57
-0.0117
PRO 57
ASP 58
0.0000
ASP 58
ILE 59
-0.0029
ILE 59
ILE 60
0.0002
ILE 60
PHE 61
-0.0003
PHE 61
TRP 62
-0.0002
TRP 62
ALA 63
0.0137
ALA 63
HIS 64
0.0003
HIS 64
ASP 65
-0.0062
ASP 65
ARG 66
-0.0000
ARG 66
PHE 67
-0.0488
PHE 67
GLY 68
-0.0001
GLY 68
GLY 69
0.0052
GLY 69
TYR 70
-0.0001
TYR 70
ALA 71
-0.0159
ALA 71
GLN 72
0.0003
GLN 72
SER 73
0.0232
SER 73
GLY 74
-0.0001
GLY 74
LEU 75
-0.0002
LEU 75
LEU 76
-0.0001
LEU 76
ALA 77
-0.0088
ALA 77
GLU 78
-0.0001
GLU 78
ILE 79
0.0070
ILE 79
THR 80
-0.0001
THR 80
PRO 81
0.0024
PRO 81
ASP 82
-0.0005
ASP 82
LYS 83
0.0087
LYS 83
ALA 84
0.0002
ALA 84
PHE 85
0.0753
PHE 85
GLN 86
0.0002
GLN 86
ASP 87
0.0150
ASP 87
LYS 88
-0.0001
LYS 88
LEU 89
-0.0167
LEU 89
TYR 90
0.0000
TYR 90
PRO 91
0.0462
PRO 91
PHE 92
-0.0000
PHE 92
THR 93
-0.0078
THR 93
TRP 94
-0.0002
TRP 94
ASP 95
0.0008
ASP 95
ALA 96
-0.0000
ALA 96
VAL 97
-0.0066
VAL 97
ARG 98
0.0000
ARG 98
TYR 99
0.0193
TYR 99
ASN 100
0.0003
ASN 100
GLY 101
-0.0087
GLY 101
LYS 102
-0.0000
LYS 102
LEU 103
0.0044
LEU 103
ILE 104
-0.0002
ILE 104
ALA 105
0.0136
ALA 105
TYR 106
0.0003
TYR 106
PRO 107
-0.0034
PRO 107
ILE 108
0.0001
ILE 108
ALA 109
-0.0360
ALA 109
VAL 110
-0.0000
VAL 110
GLU 111
-0.0644
GLU 111
ALA 112
0.0002
ALA 112
LEU 113
-0.0366
LEU 113
SER 114
-0.0001
SER 114
LEU 115
0.0051
LEU 115
ILE 116
-0.0002
ILE 116
TYR 117
0.0179
TYR 117
ASN 118
0.0000
ASN 118
LYS 119
-0.0010
LYS 119
ASP 120
-0.0002
ASP 120
LEU 121
0.0045
LEU 121
LEU 122
-0.0002
LEU 122
PRO 123
0.0043
PRO 123
ASN 124
0.0000
ASN 124
PRO 125
-0.0122
PRO 125
PRO 126
0.0002
PRO 126
LYS 127
-0.0148
LYS 127
THR 128
0.0002
THR 128
TRP 129
0.0121
TRP 129
GLU 130
-0.0002
GLU 130
GLU 131
-0.0618
GLU 131
ILE 132
0.0000
ILE 132
PRO 133
0.0234
PRO 133
ALA 134
-0.0001
ALA 134
LEU 135
0.0253
LEU 135
ASP 136
0.0003
ASP 136
LYS 137
0.0124
LYS 137
GLU 138
-0.0003
GLU 138
LEU 139
0.0185
LEU 139
LYS 140
-0.0002
LYS 140
ALA 141
-0.0069
ALA 141
LYS 142
-0.0004
LYS 142
GLY 143
0.0041
GLY 143
LYS 144
-0.0001
LYS 144
SER 145
-0.0109
SER 145
ALA 146
-0.0000
ALA 146
LEU 147
0.0167
LEU 147
MET 148
0.0001
MET 148
PHE 149
0.0239
PHE 149
ASN 150
0.0001
ASN 150
LEU 151
-0.0013
LEU 151
GLN 152
0.0000
GLN 152
GLU 153
-0.0376
GLU 153
PRO 154
-0.0000
PRO 154
TYR 155
-0.0206
TYR 155
PHE 156
0.0002
PHE 156
THR 157
-0.0314
THR 157
TRP 158
-0.0001
TRP 158
PRO 159
0.0070
PRO 159
LEU 160
0.0000
LEU 160
ILE 161
-0.0174
ILE 161
ALA 162
0.0002
ALA 162
ALA 163
-0.0125
ALA 163
ASP 164
-0.0002
ASP 164
GLY 165
-0.0456
GLY 165
GLY 166
0.0003
GLY 166
TYR 167
-0.0054
TYR 167
ALA 168
-0.0003
ALA 168
PHE 169
-0.0189
PHE 169
LYS 170
-0.0002
LYS 170
TYR 171
-0.0038
TYR 171
GLU 172
0.0001
GLU 172
ASN 173
-0.0461
ASN 173
GLY 174
0.0002
GLY 174
LYS 175
-0.0112
LYS 175
TYR 176
-0.0003
TYR 176
ASP 177
0.0156
ASP 177
ILE 178
0.0003
ILE 178
LYS 179
0.0537
LYS 179
ASP 180
0.0004
ASP 180
VAL 181
-0.0236
VAL 181
GLY 182
0.0001
GLY 182
VAL 183
-0.0183
VAL 183
ASP 184
-0.0001
ASP 184
ASN 185
0.0027
ASN 185
ALA 186
0.0000
ALA 186
GLY 187
-0.0013
GLY 187
ALA 188
0.0001
ALA 188
LYS 189
0.0156
LYS 189
ALA 190
0.0004
ALA 190
GLY 191
-0.0025
GLY 191
LEU 192
0.0000
LEU 192
THR 193
0.0087
THR 193
PHE 194
0.0001
PHE 194
LEU 195
0.0233
LEU 195
VAL 196
0.0001
VAL 196
ASP 197
-0.0265
ASP 197
LEU 198
0.0002
LEU 198
ILE 199
0.0184
ILE 199
LYS 200
-0.0001
LYS 200
ASN 201
-0.0550
ASN 201
LYS 202
-0.0002
LYS 202
HIS 203
0.0081
HIS 203
MET 204
-0.0002
MET 204
ASN 205
0.0304
ASN 205
ALA 206
-0.0001
ALA 206
ASP 207
-0.0022
ASP 207
THR 208
-0.0001
THR 208
ASP 209
-0.0592
ASP 209
TYR 210
0.0001
TYR 210
SER 211
0.0138
SER 211
ILE 212
0.0002
ILE 212
ALA 213
-0.0065
ALA 213
GLU 214
-0.0001
GLU 214
ALA 215
0.0014
ALA 215
ALA 216
0.0001
ALA 216
PHE 217
-0.0007
PHE 217
ASN 218
-0.0000
ASN 218
LYS 219
0.0007
LYS 219
GLY 220
0.0000
GLY 220
GLU 221
-0.0028
GLU 221
THR 222
0.0000
THR 222
ALA 223
-0.0070
ALA 223
MET 224
0.0002
MET 224
THR 225
0.0195
THR 225
ILE 226
0.0003
ILE 226
ASN 227
-0.0216
ASN 227
GLY 228
0.0001
GLY 228
PRO 229
-0.0319
PRO 229
TRP 230
-0.0001
TRP 230
ALA 231
0.0199
ALA 231
TRP 232
0.0002
TRP 232
SER 233
-0.0069
SER 233
ASN 234
-0.0003
ASN 234
ILE 235
0.0349
ILE 235
ASP 236
-0.0002
ASP 236
THR 237
-0.0319
THR 237
SER 238
0.0001
SER 238
LYS 239
-0.0011
LYS 239
VAL 240
-0.0003
VAL 240
ASN 241
-0.0078
ASN 241
TYR 242
-0.0000
TYR 242
GLY 243
-0.0194
GLY 243
VAL 244
-0.0001
VAL 244
THR 245
-0.0140
THR 245
VAL 246
0.0002
VAL 246
LEU 247
-0.0019
LEU 247
PRO 248
-0.0002
PRO 248
THR 249
-0.0129
THR 249
PHE 250
0.0001
PHE 250
LYS 251
-0.0016
LYS 251
GLY 252
0.0002
GLY 252
GLN 253
-0.0134
GLN 253
PRO 254
-0.0001
PRO 254
SER 255
0.0024
SER 255
LYS 256
-0.0001
LYS 256
PRO 257
-0.0110
PRO 257
PHE 258
-0.0002
PHE 258
VAL 259
-0.0482
VAL 259
GLY 260
-0.0001
GLY 260
VAL 261
-0.0487
VAL 261
LEU 262
0.0001
LEU 262
SER 263
-0.0007
SER 263
ALA 264
-0.0003
ALA 264
GLY 265
-0.0039
GLY 265
ILE 266
-0.0003
ILE 266
ASN 267
-0.0097
ASN 267
ALA 268
0.0005
ALA 268
ALA 269
0.0064
ALA 269
SER 270
-0.0001
SER 270
PRO 271
0.0044
PRO 271
ASN 272
-0.0001
ASN 272
LYS 273
-0.0052
LYS 273
GLU 274
-0.0002
GLU 274
LEU 275
0.0057
LEU 275
ALA 276
0.0001
ALA 276
LYS 277
-0.0001
LYS 277
GLU 278
-0.0003
GLU 278
PHE 279
0.0111
PHE 279
LEU 280
-0.0000
LEU 280
GLU 281
0.0075
GLU 281
ASN 282
0.0002
ASN 282
TYR 283
0.0145
TYR 283
LEU 284
0.0001
LEU 284
LEU 285
-0.0101
LEU 285
THR 286
0.0000
THR 286
ASP 287
-0.0185
ASP 287
GLU 288
0.0001
GLU 288
GLY 289
-0.0014
GLY 289
LEU 290
0.0002
LEU 290
GLU 291
0.0197
GLU 291
ALA 292
-0.0001
ALA 292
VAL 293
-0.0014
VAL 293
ASN 294
-0.0002
ASN 294
LYS 295
0.0123
LYS 295
ASP 296
0.0001
ASP 296
LYS 297
-0.0093
LYS 297
PRO 298
0.0003
PRO 298
LEU 299
0.0450
LEU 299
GLY 300
0.0001
GLY 300
ALA 301
-0.0243
ALA 301
VAL 302
-0.0003
VAL 302
ALA 303
0.0046
ALA 303
LEU 304
0.0003
LEU 304
LYS 305
-0.0081
LYS 305
SER 306
0.0001
SER 306
TYR 307
0.0125
TYR 307
GLU 308
0.0003
GLU 308
GLU 309
-0.0029
GLU 309
GLU 310
-0.0002
GLU 310
LEU 311
-0.0043
LEU 311
ALA 312
-0.0002
ALA 312
LYS 313
0.0025
LYS 313
ASP 314
0.0002
ASP 314
PRO 315
0.0236
PRO 315
ARG 316
0.0002
ARG 316
ILE 317
-0.0033
ILE 317
ALA 318
0.0004
ALA 318
ALA 319
-0.0117
ALA 319
THR 320
-0.0002
THR 320
MET 321
-0.0055
MET 321
GLU 322
0.0002
GLU 322
ASN 323
-0.0006
ASN 323
ALA 324
0.0002
ALA 324
GLN 325
-0.0068
GLN 325
LYS 326
-0.0002
LYS 326
GLY 327
0.0174
GLY 327
GLU 328
-0.0000
GLU 328
ILE 329
-0.0535
ILE 329
MET 330
0.0000
MET 330
PRO 331
0.0260
PRO 331
ASN 332
-0.0003
ASN 332
ILE 333
0.0214
ILE 333
PRO 334
-0.0001
PRO 334
GLN 335
0.0360
GLN 335
MET 336
-0.0001
MET 336
SER 337
0.0270
SER 337
ALA 338
-0.0005
ALA 338
PHE 339
0.0213
PHE 339
TRP 340
-0.0004
TRP 340
TYR 341
0.0010
TYR 341
ALA 342
-0.0001
ALA 342
VAL 343
-0.0003
VAL 343
ARG 344
0.0001
ARG 344
THR 345
-0.0132
THR 345
ALA 346
-0.0003
ALA 346
VAL 347
0.0021
VAL 347
ILE 348
0.0005
ILE 348
ASN 349
0.0161
ASN 349
ALA 350
0.0001
ALA 350
ALA 351
-0.0171
ALA 351
SER 352
-0.0000
SER 352
GLY 353
-0.0292
GLY 353
ARG 354
0.0000
ARG 354
GLN 355
0.0236
GLN 355
THR 356
0.0000
THR 356
VAL 357
0.0313
VAL 357
ASP 358
-0.0002
ASP 358
GLU 359
-0.0108
GLU 359
ALA 360
-0.0002
ALA 360
LEU 361
0.0040
LEU 361
LYS 362
0.0000
LYS 362
ASP 363
0.0102
ASP 363
ALA 364
0.0002
ALA 364
GLN 365
-0.0065
GLN 365
THR 366
0.0003
THR 366
ARG 367
0.0365
ARG 367
ILE 368
0.0001
ILE 368
THR 369
0.0184
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.