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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
-0.0060
GLU 3
GLU 4
0.0001
GLU 4
GLY 5
0.0201
GLY 5
LYS 6
0.0000
LYS 6
LEU 7
-0.0004
LEU 7
VAL 8
-0.0001
VAL 8
ILE 9
-0.0130
ILE 9
TRP 10
0.0004
TRP 10
ILE 11
-0.0477
ILE 11
ASN 12
0.0001
ASN 12
GLY 13
0.0063
GLY 13
ASP 14
0.0003
ASP 14
LYS 15
0.0207
LYS 15
GLY 16
0.0002
GLY 16
TYR 17
-0.0138
TYR 17
ASN 18
-0.0003
ASN 18
GLY 19
-0.0038
GLY 19
LEU 20
-0.0001
LEU 20
ALA 21
0.0045
ALA 21
GLU 22
0.0004
GLU 22
VAL 23
-0.0018
VAL 23
GLY 24
0.0000
GLY 24
LYS 25
0.0038
LYS 25
LYS 26
0.0000
LYS 26
PHE 27
-0.0017
PHE 27
GLU 28
-0.0002
GLU 28
LYS 29
0.0037
LYS 29
ASP 30
-0.0000
ASP 30
THR 31
-0.0045
THR 31
GLY 32
0.0000
GLY 32
ILE 33
0.0014
ILE 33
LYS 34
-0.0004
LYS 34
VAL 35
-0.0033
VAL 35
THR 36
-0.0001
THR 36
VAL 37
-0.0191
VAL 37
GLU 38
0.0002
GLU 38
HIS 39
-0.0096
HIS 39
PRO 40
0.0000
PRO 40
ASP 41
0.0066
ASP 41
LYS 42
-0.0000
LYS 42
LEU 43
0.0068
LEU 43
GLU 44
-0.0000
GLU 44
GLU 45
-0.0042
GLU 45
LYS 46
-0.0003
LYS 46
PHE 47
0.0051
PHE 47
PRO 48
0.0003
PRO 48
GLN 49
0.0039
GLN 49
VAL 50
-0.0002
VAL 50
ALA 51
0.0060
ALA 51
ALA 52
0.0000
ALA 52
THR 53
0.0129
THR 53
GLY 54
0.0001
GLY 54
ASP 55
-0.0109
ASP 55
GLY 56
-0.0002
GLY 56
PRO 57
-0.0043
PRO 57
ASP 58
0.0002
ASP 58
ILE 59
-0.0029
ILE 59
ILE 60
-0.0001
ILE 60
PHE 61
-0.0198
PHE 61
TRP 62
0.0003
TRP 62
ALA 63
0.0183
ALA 63
HIS 64
-0.0003
HIS 64
ASP 65
0.0221
ASP 65
ARG 66
0.0001
ARG 66
PHE 67
-0.0077
PHE 67
GLY 68
0.0002
GLY 68
GLY 69
0.0046
GLY 69
TYR 70
-0.0000
TYR 70
ALA 71
0.0050
ALA 71
GLN 72
-0.0005
GLN 72
SER 73
0.0307
SER 73
GLY 74
-0.0000
GLY 74
LEU 75
-0.0035
LEU 75
LEU 76
0.0002
LEU 76
ALA 77
-0.0011
ALA 77
GLU 78
-0.0003
GLU 78
ILE 79
0.0018
ILE 79
THR 80
0.0001
THR 80
PRO 81
0.0064
PRO 81
ASP 82
-0.0001
ASP 82
LYS 83
-0.0074
LYS 83
ALA 84
0.0001
ALA 84
PHE 85
-0.0386
PHE 85
GLN 86
-0.0001
GLN 86
ASP 87
-0.0071
ASP 87
LYS 88
-0.0000
LYS 88
LEU 89
0.0102
LEU 89
TYR 90
-0.0002
TYR 90
PRO 91
-0.0106
PRO 91
PHE 92
0.0002
PHE 92
THR 93
-0.0039
THR 93
TRP 94
-0.0004
TRP 94
ASP 95
0.0341
ASP 95
ALA 96
0.0002
ALA 96
VAL 97
0.0105
VAL 97
ARG 98
-0.0000
ARG 98
TYR 99
-0.0106
TYR 99
ASN 100
0.0000
ASN 100
GLY 101
0.0022
GLY 101
LYS 102
0.0001
LYS 102
LEU 103
-0.0009
LEU 103
ILE 104
-0.0001
ILE 104
ALA 105
0.0020
ALA 105
TYR 106
0.0001
TYR 106
PRO 107
-0.0034
PRO 107
ILE 108
0.0001
ILE 108
ALA 109
0.0047
ALA 109
VAL 110
0.0001
VAL 110
GLU 111
0.0207
GLU 111
ALA 112
-0.0001
ALA 112
LEU 113
-0.0014
LEU 113
SER 114
0.0002
SER 114
LEU 115
-0.0131
LEU 115
ILE 116
0.0002
ILE 116
TYR 117
-0.0141
TYR 117
ASN 118
0.0001
ASN 118
LYS 119
-0.0045
LYS 119
ASP 120
0.0003
ASP 120
LEU 121
-0.0182
LEU 121
LEU 122
-0.0001
LEU 122
PRO 123
-0.0068
PRO 123
ASN 124
-0.0001
ASN 124
PRO 125
0.0048
PRO 125
PRO 126
-0.0000
PRO 126
LYS 127
0.0088
LYS 127
THR 128
-0.0001
THR 128
TRP 129
0.0171
TRP 129
GLU 130
0.0000
GLU 130
GLU 131
-0.0044
GLU 131
ILE 132
0.0002
ILE 132
PRO 133
0.0031
PRO 133
ALA 134
0.0001
ALA 134
LEU 135
0.0107
LEU 135
ASP 136
-0.0002
ASP 136
LYS 137
0.0028
LYS 137
GLU 138
0.0001
GLU 138
LEU 139
0.0052
LEU 139
LYS 140
-0.0000
LYS 140
ALA 141
-0.0083
ALA 141
LYS 142
0.0003
LYS 142
GLY 143
0.0165
GLY 143
LYS 144
-0.0000
LYS 144
SER 145
-0.0242
SER 145
ALA 146
-0.0001
ALA 146
LEU 147
0.0010
LEU 147
MET 148
0.0000
MET 148
PHE 149
-0.0118
PHE 149
ASN 150
-0.0004
ASN 150
LEU 151
-0.0152
LEU 151
GLN 152
-0.0001
GLN 152
GLU 153
0.0242
GLU 153
PRO 154
0.0000
PRO 154
TYR 155
0.0302
TYR 155
PHE 156
-0.0003
PHE 156
THR 157
0.0121
THR 157
TRP 158
-0.0000
TRP 158
PRO 159
-0.0026
PRO 159
LEU 160
-0.0000
LEU 160
ILE 161
-0.0054
ILE 161
ALA 162
0.0002
ALA 162
ALA 163
-0.0133
ALA 163
ASP 164
-0.0001
ASP 164
GLY 165
-0.0421
GLY 165
GLY 166
0.0002
GLY 166
TYR 167
-0.0366
TYR 167
ALA 168
-0.0002
ALA 168
PHE 169
-0.0589
PHE 169
LYS 170
0.0002
LYS 170
TYR 171
-0.0646
TYR 171
GLU 172
0.0001
GLU 172
ASN 173
-0.1208
ASN 173
GLY 174
-0.0003
GLY 174
LYS 175
0.0539
LYS 175
TYR 176
0.0003
TYR 176
ASP 177
0.0167
ASP 177
ILE 178
0.0001
ILE 178
LYS 179
0.0088
LYS 179
ASP 180
-0.0002
ASP 180
VAL 181
-0.0305
VAL 181
GLY 182
0.0000
GLY 182
VAL 183
-0.0537
VAL 183
ASP 184
-0.0000
ASP 184
ASN 185
0.0198
ASN 185
ALA 186
0.0002
ALA 186
GLY 187
0.0261
GLY 187
ALA 188
-0.0001
ALA 188
LYS 189
-0.0027
LYS 189
ALA 190
-0.0003
ALA 190
GLY 191
0.0225
GLY 191
LEU 192
0.0001
LEU 192
THR 193
0.0097
THR 193
PHE 194
0.0001
PHE 194
LEU 195
-0.0033
LEU 195
VAL 196
-0.0005
VAL 196
ASP 197
0.0222
ASP 197
LEU 198
0.0000
LEU 198
ILE 199
0.0033
ILE 199
LYS 200
-0.0000
LYS 200
ASN 201
0.0115
ASN 201
LYS 202
-0.0005
LYS 202
HIS 203
0.0102
HIS 203
MET 204
0.0001
MET 204
ASN 205
0.0011
ASN 205
ALA 206
0.0002
ALA 206
ASP 207
-0.0187
ASP 207
THR 208
-0.0001
THR 208
ASP 209
0.0556
ASP 209
TYR 210
-0.0000
TYR 210
SER 211
-0.0114
SER 211
ILE 212
0.0001
ILE 212
ALA 213
0.0148
ALA 213
GLU 214
0.0000
GLU 214
ALA 215
0.0189
ALA 215
ALA 216
0.0001
ALA 216
PHE 217
-0.0011
PHE 217
ASN 218
0.0000
ASN 218
LYS 219
0.0345
LYS 219
GLY 220
0.0002
GLY 220
GLU 221
-0.0043
GLU 221
THR 222
-0.0001
THR 222
ALA 223
0.0010
ALA 223
MET 224
0.0003
MET 224
THR 225
-0.0079
THR 225
ILE 226
-0.0000
ILE 226
ASN 227
0.0127
ASN 227
GLY 228
0.0001
GLY 228
PRO 229
0.0288
PRO 229
TRP 230
-0.0004
TRP 230
ALA 231
0.0025
ALA 231
TRP 232
0.0000
TRP 232
SER 233
0.0110
SER 233
ASN 234
-0.0000
ASN 234
ILE 235
-0.0299
ILE 235
ASP 236
0.0002
ASP 236
THR 237
0.0457
THR 237
SER 238
-0.0001
SER 238
LYS 239
-0.0088
LYS 239
VAL 240
0.0002
VAL 240
ASN 241
0.0060
ASN 241
TYR 242
-0.0002
TYR 242
GLY 243
0.0363
GLY 243
VAL 244
-0.0002
VAL 244
THR 245
0.0222
THR 245
VAL 246
0.0001
VAL 246
LEU 247
0.0001
LEU 247
PRO 248
0.0002
PRO 248
THR 249
0.0254
THR 249
PHE 250
0.0001
PHE 250
LYS 251
0.0057
LYS 251
GLY 252
0.0001
GLY 252
GLN 253
-0.0116
GLN 253
PRO 254
0.0001
PRO 254
SER 255
-0.0044
SER 255
LYS 256
0.0000
LYS 256
PRO 257
-0.0129
PRO 257
PHE 258
0.0000
PHE 258
VAL 259
0.0429
VAL 259
GLY 260
-0.0001
GLY 260
VAL 261
0.0109
VAL 261
LEU 262
-0.0002
LEU 262
SER 263
-0.0117
SER 263
ALA 264
0.0002
ALA 264
GLY 265
-0.0080
GLY 265
ILE 266
-0.0003
ILE 266
ASN 267
-0.0007
ASN 267
ALA 268
-0.0001
ALA 268
ALA 269
0.0102
ALA 269
SER 270
0.0003
SER 270
PRO 271
-0.0037
PRO 271
ASN 272
-0.0000
ASN 272
LYS 273
0.0121
LYS 273
GLU 274
0.0001
GLU 274
LEU 275
-0.0042
LEU 275
ALA 276
-0.0005
ALA 276
LYS 277
-0.0007
LYS 277
GLU 278
-0.0002
GLU 278
PHE 279
-0.0035
PHE 279
LEU 280
-0.0004
LEU 280
GLU 281
-0.0083
GLU 281
ASN 282
0.0003
ASN 282
TYR 283
-0.0091
TYR 283
LEU 284
-0.0002
LEU 284
LEU 285
-0.0066
LEU 285
THR 286
0.0001
THR 286
ASP 287
0.0139
ASP 287
GLU 288
0.0002
GLU 288
GLY 289
-0.0047
GLY 289
LEU 290
0.0002
LEU 290
GLU 291
0.0048
GLU 291
ALA 292
-0.0000
ALA 292
VAL 293
0.0006
VAL 293
ASN 294
0.0004
ASN 294
LYS 295
-0.0104
LYS 295
ASP 296
-0.0001
ASP 296
LYS 297
0.0093
LYS 297
PRO 298
0.0003
PRO 298
LEU 299
0.0044
LEU 299
GLY 300
-0.0001
GLY 300
ALA 301
0.0130
ALA 301
VAL 302
-0.0001
VAL 302
ALA 303
0.0024
ALA 303
LEU 304
0.0001
LEU 304
LYS 305
-0.0036
LYS 305
SER 306
0.0000
SER 306
TYR 307
-0.0035
TYR 307
GLU 308
0.0004
GLU 308
GLU 309
-0.0085
GLU 309
GLU 310
0.0000
GLU 310
LEU 311
0.0108
LEU 311
ALA 312
-0.0002
ALA 312
LYS 313
-0.0167
LYS 313
ASP 314
0.0002
ASP 314
PRO 315
-0.0077
PRO 315
ARG 316
0.0001
ARG 316
ILE 317
0.0150
ILE 317
ALA 318
-0.0004
ALA 318
ALA 319
-0.0073
ALA 319
THR 320
-0.0004
THR 320
MET 321
0.0037
MET 321
GLU 322
-0.0002
GLU 322
ASN 323
0.0066
ASN 323
ALA 324
-0.0000
ALA 324
GLN 325
-0.0163
GLN 325
LYS 326
0.0000
LYS 326
GLY 327
-0.0115
GLY 327
GLU 328
0.0001
GLU 328
ILE 329
0.0075
ILE 329
MET 330
0.0003
MET 330
PRO 331
-0.0061
PRO 331
ASN 332
-0.0000
ASN 332
ILE 333
0.0029
ILE 333
PRO 334
0.0002
PRO 334
GLN 335
-0.0011
GLN 335
MET 336
0.0002
MET 336
SER 337
0.0110
SER 337
ALA 338
-0.0002
ALA 338
PHE 339
-0.0151
PHE 339
TRP 340
0.0003
TRP 340
TYR 341
-0.0044
TYR 341
ALA 342
-0.0004
ALA 342
VAL 343
0.0031
VAL 343
ARG 344
-0.0004
ARG 344
THR 345
0.0025
THR 345
ALA 346
-0.0003
ALA 346
VAL 347
-0.0155
VAL 347
ILE 348
-0.0002
ILE 348
ASN 349
-0.0296
ASN 349
ALA 350
-0.0003
ALA 350
ALA 351
-0.0303
ALA 351
SER 352
0.0002
SER 352
GLY 353
-0.0409
GLY 353
ARG 354
-0.0001
ARG 354
GLN 355
-0.0074
GLN 355
THR 356
0.0001
THR 356
VAL 357
0.0069
VAL 357
ASP 358
0.0002
ASP 358
GLU 359
0.0193
GLU 359
ALA 360
0.0004
ALA 360
LEU 361
-0.0055
LEU 361
LYS 362
-0.0001
LYS 362
ASP 363
0.0071
ASP 363
ALA 364
0.0002
ALA 364
GLN 365
-0.0255
GLN 365
THR 366
0.0002
THR 366
ARG 367
-0.0131
ARG 367
ILE 368
-0.0001
ILE 368
THR 369
-0.0221
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.