Should you encounter any unexpected behaviour,
please let us know. elNémo has been hacked on november 27th.
It has been moved away and runs again.
**Still some additional cleaning from time to time**
Sorry for the inconvenience.
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
ASN 8
ALA 9
0.0001
ALA 9
ALA 10
0.0001
ALA 10
GLY 11
-0.0001
GLY 11
THR 12
-0.0327
THR 12
ILE 13
-0.0004
ILE 13
SER 14
0.0005
SER 14
ASN 15
-0.0001
ASN 15
ASP 16
-0.0982
ASP 16
ILE 17
-0.0002
ILE 17
LEU 18
-0.0000
LEU 18
ALA 19
0.0001
ALA 19
GLN 20
0.0363
GLN 20
VAL 21
0.0002
VAL 21
THR 22
-0.0002
THR 22
PHE 23
-0.0003
PHE 23
ALA 24
0.0266
ALA 24
ASN 25
0.0001
ASN 25
GLU 26
-0.0000
GLU 26
ALA 27
0.0001
ALA 27
ILE 28
-0.0475
ILE 28
TYR 29
-0.0000
TYR 29
PRO 30
0.0000
PRO 30
LEU 31
-0.0003
LEU 31
LEU 32
0.0168
LEU 32
GLU 33
0.0000
GLU 33
LYS 34
-0.0002
LYS 34
ARG 35
-0.0002
ARG 35
ARG 36
0.0092
ARG 36
ALA 37
0.0001
ALA 37
GLU 38
0.0005
GLU 38
ILE 39
0.0001
ILE 39
GLU 40
-0.0485
GLU 40
ASN 41
0.0003
ASN 41
VAL 42
0.0002
VAL 42
THR 43
-0.0001
THR 43
ARG 44
-0.0212
ARG 44
LYS 45
0.0003
LYS 45
THR 46
-0.0004
THR 46
PHE 47
0.0000
PHE 47
ARG 48
0.0365
ARG 48
TYR 49
0.0002
TYR 49
GLY 50
-0.0001
GLY 50
ALA 51
-0.0002
ALA 51
LEU 52
0.0805
LEU 52
PRO 53
0.0001
PRO 53
GLY 54
-0.0002
GLY 54
SER 55
0.0001
SER 55
GLU 56
0.0102
GLU 56
MET 57
0.0002
MET 57
ASP 58
0.0001
ASP 58
VAL 59
0.0000
VAL 59
TYR 60
0.0283
TYR 60
TYR 61
0.0001
TYR 61
PRO 62
0.0002
PRO 62
SER 63
-0.0003
SER 63
SER 64
0.0755
SER 64
THR 65
-0.0002
THR 65
PRO 66
0.0001
PRO 66
SER 67
0.0000
SER 67
GLY 68
0.1262
GLY 68
LYS 69
0.0001
LYS 69
ALA 70
-0.0002
ALA 70
PRO 71
0.0003
PRO 71
VAL 72
0.0491
VAL 72
LEU 73
0.0002
LEU 73
ALA 74
-0.0002
ALA 74
PHE 75
0.0001
PHE 75
VAL 76
0.1075
VAL 76
HIS 77
0.0001
HIS 77
GLY 78
0.0003
GLY 78
GLY 79
-0.0001
GLY 79
ALA 80
0.1374
ALA 80
TYR 81
-0.0001
TYR 81
VAL 82
-0.0002
VAL 82
HIS 83
0.0002
HIS 83
GLY 84
0.2479
GLY 84
SER 85
0.0000
SER 85
LYS 86
-0.0001
LYS 86
THR 87
-0.0001
THR 87
HIS 88
0.3534
HIS 88
PRO 89
-0.0002
PRO 89
PRO 90
0.0001
PRO 90
PRO 91
0.0003
PRO 91
GLY 92
-0.1297
GLY 92
ASP 93
-0.0001
ASP 93
LEU 94
-0.0003
LEU 94
ILE 95
-0.0001
ILE 95
TYR 96
0.0328
TYR 96
LYS 97
0.0001
LYS 97
ASN 98
0.0003
ASN 98
VAL 99
-0.0004
VAL 99
GLY 100
-0.0223
GLY 100
ALA 101
-0.0001
ALA 101
PHE 102
0.0002
PHE 102
TYR 103
0.0000
TYR 103
ALA 104
-0.0724
ALA 104
SER 105
-0.0000
SER 105
GLN 106
0.0004
GLN 106
GLY 107
0.0002
GLY 107
PHE 108
-0.0004
PHE 108
VAL 109
-0.0000
VAL 109
THR 110
0.0000
THR 110
VAL 111
-0.0004
VAL 111
ILE 112
0.1924
ILE 112
PRO 113
-0.0001
PRO 113
ASP 114
0.0004
ASP 114
TYR 115
-0.0001
TYR 115
ARG 116
0.2719
ARG 116
LYS 117
-0.0002
LYS 117
LEU 118
-0.0002
LEU 118
PRO 119
0.0005
PRO 119
GLY 120
-0.1031
GLY 120
MET 121
0.0003
MET 121
LYS 122
0.0003
LYS 122
TRP 123
-0.0002
TRP 123
PRO 124
0.1188
PRO 124
ASP 125
0.0001
ASP 125
ALA 126
-0.0001
ALA 126
PRO 127
0.0002
PRO 127
SER 128
-0.0486
SER 128
ASP 129
0.0001
ASP 129
ILE 130
-0.0002
ILE 130
ALA 131
-0.0002
ALA 131
SER 132
-0.1480
SER 132
ALA 133
0.0001
ALA 133
LEU 134
0.0003
LEU 134
THR 135
-0.0002
THR 135
PHE 136
-0.0803
PHE 136
LEU 137
-0.0001
LEU 137
VAL 138
0.0004
VAL 138
ALA 139
-0.0001
ALA 139
HIS 140
-0.0283
HIS 140
SER 141
-0.0001
SER 141
SER 142
-0.0001
SER 142
ASP 143
0.0001
ASP 143
VAL 144
-0.0139
VAL 144
ASN 145
0.0000
ASN 145
ALA 146
-0.0002
ALA 146
SER 147
-0.0002
SER 147
ALA 148
-0.0257
ALA 148
PRO 149
0.0000
PRO 149
THR 150
-0.0005
THR 150
ALA 151
0.0000
ALA 151
ALA 152
-0.0235
ALA 152
ASP 153
0.0000
ASP 153
VAL 154
0.0000
VAL 154
GLN 155
0.0000
GLN 155
ASN 156
-0.0239
ASN 156
ILE 157
0.0000
ILE 157
PHE 158
0.0002
PHE 158
LEU 159
-0.0003
LEU 159
VAL 160
0.0077
VAL 160
GLY 161
-0.0001
GLY 161
HIS 162
0.0001
HIS 162
SER 163
-0.0002
SER 163
ALA 164
-0.0024
ALA 164
GLY 165
-0.0001
GLY 165
GLY 166
0.0000
GLY 166
ALA 167
0.0001
ALA 167
ILE 168
-0.0149
ILE 168
ALA 169
-0.0005
ALA 169
SER 170
-0.0001
SER 170
ASP 171
0.0002
ASP 171
VAL 172
0.0175
VAL 172
LEU 173
0.0003
LEU 173
LEU 174
-0.0002
LEU 174
ALA 175
-0.0002
ALA 175
PRO 176
-0.0121
PRO 176
GLY 177
0.0000
GLY 177
LEU 178
-0.0000
LEU 178
LEU 179
-0.0003
LEU 179
PRO 180
0.0559
PRO 180
ALA 181
0.0001
ALA 181
ASN 182
0.0003
ASN 182
VAL 183
0.0002
VAL 183
ARG 184
-0.1056
ARG 184
ARG 185
0.0001
ARG 185
SER 186
-0.0003
SER 186
VAL 187
0.0001
VAL 187
ARG 188
0.0495
ARG 188
GLY 189
0.0000
GLY 189
LEU 190
-0.0001
LEU 190
ILE 191
0.0002
ILE 191
VAL 192
-0.0412
VAL 192
PHE 193
-0.0000
PHE 193
GLY 194
0.0001
GLY 194
GLY 195
0.0000
GLY 195
MET 196
0.0267
MET 196
MET 197
-0.0002
MET 197
HIS 198
0.0002
HIS 198
TYR 199
0.0002
TYR 199
ARG 200
-0.0078
ARG 200
GLY 201
-0.0002
GLY 201
LEU 202
0.0002
LEU 202
GLU 203
0.0003
GLU 203
TYR 204
-0.0357
TYR 204
PRO 205
0.0000
PRO 205
ILE 206
-0.0003
ILE 206
PRO 207
-0.0000
PRO 207
PRO 208
0.0906
PRO 208
PHE 209
-0.0001
PHE 209
VAL 210
0.0000
VAL 210
LEU 211
0.0004
LEU 211
PRO 212
-0.1439
PRO 212
GLY 213
-0.0001
GLY 213
TYR 214
0.0001
TYR 214
TYR 215
-0.0001
TYR 215
GLY 216
-0.0446
GLY 216
THR 217
-0.0002
THR 217
ASP 218
-0.0002
ASP 218
GLU 219
-0.0000
GLU 219
ASP 220
-0.0438
ASP 220
VAL 221
-0.0000
VAL 221
ARG 222
-0.0001
ARG 222
ALA 223
0.0003
ALA 223
HIS 224
-0.0350
HIS 224
GLU 225
-0.0001
GLU 225
PRO 226
-0.0002
PRO 226
LEU 227
-0.0001
LEU 227
GLY 228
0.0165
GLY 228
LEU 229
0.0002
LEU 229
LEU 230
-0.0001
LEU 230
GLU 231
0.0001
GLU 231
SER 232
0.0114
SER 232
ALA 233
-0.0001
ALA 233
SER 234
-0.0002
SER 234
ASP 235
0.0002
ASP 235
GLU 236
-0.0089
GLU 236
ILE 237
-0.0000
ILE 237
VAL 238
-0.0003
VAL 238
ARG 239
0.0003
ARG 239
GLY 240
-0.0775
GLY 240
LEU 241
-0.0002
LEU 241
PRO 242
0.0002
PRO 242
ASP 243
-0.0002
ASP 243
VAL 244
-0.0519
VAL 244
LEU 245
0.0001
LEU 245
MET 246
-0.0002
MET 246
VAL 247
0.0003
VAL 247
LEU 248
-0.0890
LEU 248
SER 249
0.0003
SER 249
GLU 250
-0.0003
GLU 250
HIS 251
-0.0002
HIS 251
ASP 252
0.0293
ASP 252
VAL 253
0.0000
VAL 253
ALA 254
0.0003
ALA 254
ALA 255
0.0002
ALA 255
MET 256
-0.0175
MET 256
ARG 257
0.0000
ARG 257
ALA 258
-0.0002
ALA 258
ALA 259
-0.0001
ALA 259
VAL 260
-0.0111
VAL 260
THR 261
-0.0002
THR 261
ASP 262
-0.0001
ASP 262
PHE 263
-0.0000
PHE 263
ARG 264
-0.0225
ARG 264
SER 265
0.0001
SER 265
ALA 266
0.0001
ALA 266
LEU 267
-0.0003
LEU 267
ALA 268
-0.0001
ALA 268
GLU 269
-0.0001
GLU 269
ARG 270
0.0002
ARG 270
THR 271
-0.0002
THR 271
GLY 272
0.0126
GLY 272
LYS 273
0.0004
LYS 273
ASP 274
-0.0002
ASP 274
VAL 275
0.0003
VAL 275
PRO 276
0.0258
PRO 276
LEU 277
0.0002
LEU 277
LEU 278
-0.0001
LEU 278
VAL 279
-0.0001
VAL 279
ALA 280
0.0311
ALA 280
GLN 281
0.0001
GLN 281
GLY 282
-0.0003
GLY 282
HIS 283
0.0005
HIS 283
ASN 284
-0.0540
ASN 284
HIS 285
0.0002
HIS 285
ILE 286
0.0002
ILE 286
SER 287
0.0001
SER 287
PRO 288
0.0025
PRO 288
HIS 289
0.0001
HIS 289
TYR 290
-0.0002
TYR 290
ALA 291
0.0002
ALA 291
LEU 292
-0.0088
LEU 292
SER 293
-0.0004
SER 293
SER 294
0.0001
SER 294
GLY 295
-0.0005
GLY 295
GLU 296
0.0222
GLU 296
GLY 297
0.0003
GLY 297
GLU 298
0.0000
GLU 298
GLU 299
0.0002
GLU 299
TRP 300
0.0392
TRP 300
GLY 301
0.0001
GLY 301
HIS 302
0.0003
HIS 302
ASP 303
0.0001
ASP 303
VAL 304
0.0069
VAL 304
ILE 305
0.0003
ILE 305
ARG 306
-0.0000
ARG 306
TRP 307
-0.0001
TRP 307
MET 308
-0.0487
MET 308
ARG 309
-0.0000
ARG 309
ALA 310
-0.0001
ALA 310
LYS 311
0.0002
LYS 311
LEU 312
-0.0623
LEU 312
ALA 313
-0.0000
ALA 313
SER 314
-0.0003
SER 314
GLY 315
-0.0000
GLY 315
ASN 316
0.0381
ASN 316
ASN 8
0.0971
ASN 8
ALA 9
0.0002
ALA 9
ALA 10
-0.0002
ALA 10
GLY 11
0.0002
GLY 11
THR 12
0.0342
THR 12
ILE 13
-0.0002
ILE 13
SER 14
0.0000
SER 14
ASN 15
0.0001
ASN 15
ASP 16
0.0313
ASP 16
ILE 17
0.0002
ILE 17
LEU 18
0.0000
LEU 18
ALA 19
0.0004
ALA 19
GLN 20
0.0096
GLN 20
VAL 21
-0.0001
VAL 21
THR 22
0.0001
THR 22
PHE 23
0.0002
PHE 23
ALA 24
-0.0500
ALA 24
ASN 25
0.0002
ASN 25
GLU 26
0.0003
GLU 26
ALA 27
-0.0001
ALA 27
ILE 28
0.0061
ILE 28
TYR 29
-0.0002
TYR 29
PRO 30
0.0000
PRO 30
LEU 31
0.0000
LEU 31
LEU 32
-0.0610
LEU 32
GLU 33
-0.0000
GLU 33
LYS 34
0.0004
LYS 34
ARG 35
-0.0000
ARG 35
ARG 36
-0.0106
ARG 36
ALA 37
-0.0001
ALA 37
GLU 38
0.0003
GLU 38
ILE 39
-0.0004
ILE 39
GLU 40
-0.0176
GLU 40
ASN 41
0.0003
ASN 41
VAL 42
-0.0002
VAL 42
THR 43
0.0004
THR 43
ARG 44
0.0399
ARG 44
LYS 45
-0.0001
LYS 45
THR 46
-0.0000
THR 46
PHE 47
0.0001
PHE 47
ARG 48
0.0174
ARG 48
TYR 49
0.0000
TYR 49
GLY 50
-0.0001
GLY 50
ALA 51
0.0000
ALA 51
LEU 52
-0.0346
LEU 52
PRO 53
-0.0001
PRO 53
GLY 54
-0.0000
GLY 54
SER 55
-0.0003
SER 55
GLU 56
0.0332
GLU 56
MET 57
0.0003
MET 57
ASP 58
0.0003
ASP 58
VAL 59
0.0000
VAL 59
TYR 60
-0.0018
TYR 60
TYR 61
0.0001
TYR 61
PRO 62
0.0002
PRO 62
SER 63
0.0002
SER 63
SER 64
0.0335
SER 64
THR 65
0.0002
THR 65
PRO 66
-0.0002
PRO 66
SER 67
-0.0000
SER 67
GLY 68
-0.0748
GLY 68
LYS 69
-0.0001
LYS 69
ALA 70
-0.0001
ALA 70
PRO 71
0.0002
PRO 71
VAL 72
-0.0195
VAL 72
LEU 73
0.0002
LEU 73
ALA 74
0.0000
ALA 74
PHE 75
-0.0001
PHE 75
VAL 76
-0.0132
VAL 76
HIS 77
-0.0003
HIS 77
GLY 78
0.0001
GLY 78
GLY 79
-0.0003
GLY 79
ALA 80
-0.0535
ALA 80
TYR 81
-0.0002
TYR 81
VAL 82
-0.0001
VAL 82
HIS 83
-0.0001
HIS 83
GLY 84
-0.0488
GLY 84
SER 85
0.0001
SER 85
LYS 86
-0.0001
LYS 86
THR 87
0.0003
THR 87
HIS 88
-0.2484
HIS 88
PRO 89
0.0002
PRO 89
PRO 90
-0.0001
PRO 90
PRO 91
-0.0000
PRO 91
GLY 92
0.1693
GLY 92
ASP 93
0.0002
ASP 93
LEU 94
-0.0002
LEU 94
ILE 95
0.0001
ILE 95
TYR 96
-0.0031
TYR 96
LYS 97
-0.0003
LYS 97
ASN 98
-0.0003
ASN 98
VAL 99
0.0001
VAL 99
GLY 100
-0.0019
GLY 100
ALA 101
-0.0004
ALA 101
PHE 102
-0.0001
PHE 102
TYR 103
-0.0004
TYR 103
ALA 104
-0.0023
ALA 104
SER 105
0.0003
SER 105
GLN 106
0.0003
GLN 106
GLY 107
0.0004
GLY 107
PHE 108
-0.0027
PHE 108
VAL 109
-0.0001
VAL 109
THR 110
0.0000
THR 110
VAL 111
0.0004
VAL 111
ILE 112
-0.0445
ILE 112
PRO 113
0.0002
PRO 113
ASP 114
0.0003
ASP 114
TYR 115
-0.0001
TYR 115
ARG 116
-0.0850
ARG 116
LYS 117
-0.0001
LYS 117
LEU 118
0.0003
LEU 118
PRO 119
-0.0002
PRO 119
GLY 120
0.0107
GLY 120
MET 121
-0.0000
MET 121
LYS 122
-0.0002
LYS 122
TRP 123
0.0003
TRP 123
PRO 124
-0.0717
PRO 124
ASP 125
-0.0003
ASP 125
ALA 126
-0.0000
ALA 126
PRO 127
0.0001
PRO 127
SER 128
0.0634
SER 128
ASP 129
-0.0001
ASP 129
ILE 130
0.0001
ILE 130
ALA 131
-0.0001
ALA 131
SER 132
0.1278
SER 132
ALA 133
0.0000
ALA 133
LEU 134
0.0001
LEU 134
THR 135
0.0001
THR 135
PHE 136
0.0567
PHE 136
LEU 137
0.0004
LEU 137
VAL 138
0.0001
VAL 138
ALA 139
0.0004
ALA 139
HIS 140
0.0267
HIS 140
SER 141
0.0002
SER 141
SER 142
0.0000
SER 142
ASP 143
-0.0001
ASP 143
VAL 144
-0.0030
VAL 144
ASN 145
0.0001
ASN 145
ALA 146
0.0003
ALA 146
SER 147
0.0001
SER 147
ALA 148
0.0016
ALA 148
PRO 149
-0.0002
PRO 149
THR 150
-0.0001
THR 150
ALA 151
-0.0001
ALA 151
ALA 152
0.0115
ALA 152
ASP 153
0.0003
ASP 153
VAL 154
0.0001
VAL 154
GLN 155
0.0002
GLN 155
ASN 156
0.0190
ASN 156
ILE 157
0.0004
ILE 157
PHE 158
-0.0004
PHE 158
LEU 159
-0.0002
LEU 159
VAL 160
0.0015
VAL 160
GLY 161
-0.0003
GLY 161
HIS 162
0.0002
HIS 162
SER 163
-0.0001
SER 163
ALA 164
0.0137
ALA 164
GLY 165
-0.0003
GLY 165
GLY 166
0.0000
GLY 166
ALA 167
0.0003
ALA 167
ILE 168
-0.0078
ILE 168
ALA 169
-0.0002
ALA 169
SER 170
0.0001
SER 170
ASP 171
0.0001
ASP 171
VAL 172
-0.0007
VAL 172
LEU 173
0.0002
LEU 173
LEU 174
-0.0003
LEU 174
ALA 175
-0.0002
ALA 175
PRO 176
0.0169
PRO 176
GLY 177
0.0002
GLY 177
LEU 178
0.0002
LEU 178
LEU 179
-0.0001
LEU 179
PRO 180
-0.0419
PRO 180
ALA 181
0.0005
ALA 181
ASN 182
0.0000
ASN 182
VAL 183
0.0002
VAL 183
ARG 184
0.0827
ARG 184
ARG 185
-0.0001
ARG 185
SER 186
0.0002
SER 186
VAL 187
-0.0001
VAL 187
ARG 188
-0.0468
ARG 188
GLY 189
-0.0000
GLY 189
LEU 190
-0.0002
LEU 190
ILE 191
-0.0001
ILE 191
VAL 192
0.0500
VAL 192
PHE 193
0.0001
PHE 193
GLY 194
0.0002
GLY 194
GLY 195
-0.0001
GLY 195
MET 196
0.0346
MET 196
MET 197
-0.0001
MET 197
HIS 198
0.0000
HIS 198
TYR 199
0.0004
TYR 199
ARG 200
0.0081
ARG 200
GLY 201
-0.0005
GLY 201
LEU 202
-0.0003
LEU 202
GLU 203
0.0001
GLU 203
TYR 204
0.0087
TYR 204
PRO 205
-0.0000
PRO 205
ILE 206
0.0001
ILE 206
PRO 207
-0.0001
PRO 207
PRO 208
-0.0578
PRO 208
PHE 209
0.0001
PHE 209
VAL 210
0.0001
VAL 210
LEU 211
-0.0002
LEU 211
PRO 212
0.2018
PRO 212
GLY 213
-0.0002
GLY 213
TYR 214
-0.0004
TYR 214
TYR 215
-0.0002
TYR 215
GLY 216
0.0933
GLY 216
THR 217
0.0000
THR 217
ASP 218
0.0001
ASP 218
GLU 219
-0.0001
GLU 219
ASP 220
0.0293
ASP 220
VAL 221
-0.0001
VAL 221
ARG 222
-0.0001
ARG 222
ALA 223
-0.0004
ALA 223
HIS 224
0.0298
HIS 224
GLU 225
-0.0001
GLU 225
PRO 226
0.0000
PRO 226
LEU 227
0.0001
LEU 227
GLY 228
-0.0298
GLY 228
LEU 229
-0.0001
LEU 229
LEU 230
0.0003
LEU 230
GLU 231
-0.0001
GLU 231
SER 232
-0.0013
SER 232
ALA 233
0.0002
ALA 233
SER 234
0.0000
SER 234
ASP 235
0.0001
ASP 235
GLU 236
0.0083
GLU 236
ILE 237
-0.0002
ILE 237
VAL 238
-0.0001
VAL 238
ARG 239
-0.0000
ARG 239
GLY 240
0.0468
GLY 240
LEU 241
0.0002
LEU 241
PRO 242
-0.0002
PRO 242
ASP 243
-0.0000
ASP 243
VAL 244
0.0462
VAL 244
LEU 245
0.0000
LEU 245
MET 246
-0.0002
MET 246
VAL 247
0.0003
VAL 247
LEU 248
0.0672
LEU 248
SER 249
-0.0001
SER 249
GLU 250
-0.0002
GLU 250
HIS 251
0.0000
HIS 251
ASP 252
-0.0070
ASP 252
VAL 253
-0.0000
VAL 253
ALA 254
-0.0001
ALA 254
ALA 255
0.0003
ALA 255
MET 256
-0.0020
MET 256
ARG 257
0.0000
ARG 257
ALA 258
0.0003
ALA 258
ALA 259
0.0002
ALA 259
VAL 260
0.0303
VAL 260
THR 261
0.0005
THR 261
ASP 262
0.0000
ASP 262
PHE 263
0.0002
PHE 263
ARG 264
0.0445
ARG 264
SER 265
0.0001
SER 265
ALA 266
0.0001
ALA 266
LEU 267
-0.0002
LEU 267
ALA 268
0.0080
ALA 268
GLU 269
-0.0001
GLU 269
ARG 270
0.0003
ARG 270
THR 271
0.0001
THR 271
GLY 272
0.0045
GLY 272
LYS 273
-0.0002
LYS 273
ASP 274
0.0001
ASP 274
VAL 275
-0.0000
VAL 275
PRO 276
0.0064
PRO 276
LEU 277
0.0003
LEU 277
LEU 278
-0.0000
LEU 278
VAL 279
-0.0002
VAL 279
ALA 280
0.0138
ALA 280
GLN 281
-0.0001
GLN 281
GLY 282
0.0003
GLY 282
HIS 283
-0.0003
HIS 283
ASN 284
0.1182
ASN 284
HIS 285
0.0000
HIS 285
ILE 286
0.0001
ILE 286
SER 287
-0.0001
SER 287
PRO 288
0.0177
PRO 288
HIS 289
0.0003
HIS 289
TYR 290
-0.0001
TYR 290
ALA 291
-0.0002
ALA 291
LEU 292
0.0084
LEU 292
SER 293
0.0001
SER 293
SER 294
0.0003
SER 294
GLY 295
-0.0003
GLY 295
GLU 296
-0.0354
GLU 296
GLY 297
-0.0002
GLY 297
GLU 298
-0.0003
GLU 298
GLU 299
-0.0000
GLU 299
TRP 300
-0.0070
TRP 300
GLY 301
-0.0004
GLY 301
HIS 302
-0.0002
HIS 302
ASP 303
-0.0000
ASP 303
VAL 304
-0.0023
VAL 304
ILE 305
0.0000
ILE 305
ARG 306
0.0001
ARG 306
TRP 307
-0.0002
TRP 307
MET 308
0.0314
MET 308
ARG 309
-0.0001
ARG 309
ALA 310
0.0005
ALA 310
LYS 311
-0.0002
LYS 311
LEU 312
0.0184
LEU 312
ALA 313
0.0000
ALA 313
SER 314
0.0001
SER 314
GLY 315
0.0000
GLY 315
ASN 316
-0.0589
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: december 26th, 2025.