Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* BMan WT *

CA strain for 261030074727917150

--- normal mode 8 ---

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
HIS 1 THR 2 -0.0001

THR 2 VAL 3 -0.0384

VAL 3 SER 4 -0.0000

SER 4 PRO 5 0.1370

PRO 5 VAL 6 -0.0000

VAL 6 ASN 7 -0.0383

ASN 7 PRO 8 -0.0000

PRO 8 ASN 9 -0.0102

ASN 9 ALA 10 -0.0001

ALA 10 GLN 11 -0.1014

GLN 11 GLN 12 0.0003

GLN 12 THR 13 -0.0515

THR 13 THR 14 0.0004

THR 14 LYS 15 0.0538

LYS 15 THR 16 -0.0000

THR 16 VAL 17 -0.0124

VAL 17 MET 18 -0.0003

MET 18 ASN 19 0.0694

ASN 19 TRP 20 -0.0001

TRP 20 LEU 21 -0.0403

LEU 21 ALA 22 -0.0002

ALA 22 HIS 23 -0.0459

HIS 23 LEU 24 -0.0004

LEU 24 PRO 25 -0.0989

PRO 25 ASN 26 -0.0002

ASN 26 ARG 27 0.0193

ARG 27 THR 28 0.0002

THR 28 GLU 29 -0.0101

GLU 29 ASN 30 -0.0002

ASN 30 ARG 31 -0.0497

ARG 31 VAL 32 -0.0002

VAL 32 LEU 33 -0.0342

LEU 33 SER 34 -0.0001

SER 34 GLY 35 -0.0847

GLY 35 ALA 36 -0.0001

ALA 36 PHE 37 -0.1503

PHE 37 GLY 38 -0.0000

GLY 38 GLY 39 -0.1088

GLY 39 TYR 40 -0.0001

TYR 40 SER 41 -0.0766

SER 41 HIS 42 0.0002

HIS 42 ASP 43 0.0067

ASP 43 THR 44 0.0001

THR 44 PHE 45 -0.0025

PHE 45 SER 46 0.0004

SER 46 MET 47 -0.0141

MET 47 ALA 48 0.0002

ALA 48 GLU 49 0.0391

GLU 49 ALA 50 -0.0001

ALA 50 ASP 51 0.0177

ASP 51 ARG 52 -0.0001

ARG 52 ILE 53 -0.0014

ILE 53 ARG 54 -0.0000

ARG 54 SER 55 0.0111

SER 55 ALA 56 0.0002

ALA 56 THR 57 0.0142

THR 57 GLY 58 0.0000

GLY 58 GLN 59 0.0198

GLN 59 SER 60 -0.0004

SER 60 PRO 61 -0.0031

PRO 61 ALA 62 -0.0000

ALA 62 ILE 63 -0.0006

ILE 63 TYR 64 0.0001

TYR 64 GLY 65 -0.0212

GLY 65 CYS 66 0.0000

CYS 66 ASP 67 0.0173

ASP 67 TYR 68 -0.0003

TYR 68 ALA 69 0.1163

ALA 69 ARG 70 -0.0003

ARG 70 GLY 71 0.0757

GLY 71 TRP 72 0.0003

TRP 72 LEU 73 -0.0112

LEU 73 GLU 74 -0.0003

GLU 74 THR 75 0.0254

THR 75 ALA 76 0.0001

ALA 76 ASN 77 0.0261

ASN 77 ILE 78 0.0001

ILE 78 GLU 79 0.0667

GLU 79 ASP 80 0.0003

ASP 80 SER 81 -0.0695

SER 81 ILE 82 -0.0001

ILE 82 ASP 83 0.0536

ASP 83 VAL 84 -0.0002

VAL 84 SER 85 -0.0159

SER 85 CYS 86 -0.0002

CYS 86 ASN 87 -0.0363

ASN 87 GLY 88 0.0000

GLY 88 ASP 89 -0.0767

ASP 89 LEU 90 0.0002

LEU 90 MET 91 -0.0334

MET 91 SER 92 0.0001

SER 92 TYR 93 -0.0287

TYR 93 TRP 94 -0.0000

TRP 94 LYS 95 -0.0701

LYS 95 ASN 96 0.0001

ASN 96 GLY 97 0.0245

GLY 97 GLY 98 0.0001

GLY 98 ILE 99 0.0083

ILE 99 PRO 100 0.0002

PRO 100 GLN 101 0.0469

GLN 101 ILE 102 -0.0000

ILE 102 SER 103 0.0322

SER 103 LEU 104 -0.0001

LEU 104 HIS 105 0.0498

HIS 105 LEU 106 0.0001

LEU 106 ALA 107 -0.0312

ALA 107 ASN 108 -0.0001

ASN 108 PRO 109 -0.0538

PRO 109 ALA 110 -0.0000

ALA 110 PHE 111 0.0309

PHE 111 GLN 112 -0.0004

GLN 112 SER 113 -0.0304

SER 113 GLY 114 0.0002

GLY 114 HIS 115 -0.0189

HIS 115 PHE 116 -0.0001

PHE 116 LYS 117 0.0224

LYS 117 THR 118 -0.0004

THR 118 PRO 119 0.0708

PRO 119 ILE 120 0.0002

ILE 120 THR 121 0.0522

THR 121 ASN 122 -0.0003

ASN 122 ASP 123 -0.0310

ASP 123 GLN 124 -0.0001

GLN 124 TYR 125 0.0158

TYR 125 LYS 126 -0.0003

LYS 126 LYS 127 0.0048

LYS 127 ILE 128 -0.0005

ILE 128 LEU 129 0.0300

LEU 129 ASP 130 0.0001

ASP 130 SER 131 -0.0317

SER 131 SER 132 -0.0002

SER 132 THR 133 -0.0246

THR 133 VAL 134 -0.0001

VAL 134 GLU 135 0.0021

GLU 135 GLY 136 -0.0002

GLY 136 LYS 137 -0.0062

LYS 137 ARG 138 0.0001

ARG 138 LEU 139 0.0526

LEU 139 ASN 140 0.0001

ASN 140 ALA 141 -0.0361

ALA 141 MET 142 -0.0000

MET 142 LEU 143 0.1187

LEU 143 SER 144 -0.0001

SER 144 LYS 145 -0.0717

LYS 145 ILE 146 -0.0002

ILE 146 ALA 147 0.0357

ALA 147 ASP 148 -0.0004

ASP 148 GLY 149 -0.0705

GLY 149 LEU 150 -0.0000

LEU 150 GLN 151 -0.0286

GLN 151 GLU 152 -0.0001

GLU 152 LEU 153 0.0374

LEU 153 GLU 154 0.0002

GLU 154 ASN 155 -0.0546

ASN 155 GLN 156 0.0000

GLN 156 GLY 157 0.0179

GLY 157 VAL 158 0.0002

VAL 158 PRO 159 0.0085

PRO 159 VAL 160 -0.0001

VAL 160 LEU 161 -0.0016

LEU 161 PHE 162 -0.0004

PHE 162 ARG 163 -0.0067

ARG 163 PRO 164 0.0002

PRO 164 LEU 165 0.0474

LEU 165 HIS 166 0.0001

HIS 166 GLU 167 0.0372

GLU 167 MET 168 0.0001

MET 168 ASN 169 0.0070

ASN 169 GLY 170 -0.0001

GLY 170 GLU 171 -0.0693

GLU 171 TRP 172 -0.0004

TRP 172 PHE 173 -0.0035

PHE 173 TRP 174 -0.0001

TRP 174 TRP 175 0.0267

TRP 175 GLY 176 0.0002

GLY 176 LEU 177 0.0895

LEU 177 THR 178 0.0005

THR 178 SER 179 -0.1113

SER 179 TYR 180 -0.0002

TYR 180 ASN 181 -0.0248

ASN 181 GLN 182 0.0001

GLN 182 LYS 183 0.0081

LYS 183 ASP 184 -0.0005

ASP 184 ASN 185 0.0173

ASN 185 GLU 186 -0.0004

GLU 186 ARG 187 0.0275

ARG 187 ILE 188 -0.0003

ILE 188 SER 189 0.0312

SER 189 LEU 190 0.0002

LEU 190 TYR 191 -0.0020

TYR 191 LYS 192 -0.0002

LYS 192 GLN 193 0.0957

GLN 193 LEU 194 -0.0003

LEU 194 TYR 195 0.0592

TYR 195 LYS 196 -0.0000

LYS 196 LYS 197 0.1538

LYS 197 ILE 198 0.0000

ILE 198 TYR 199 0.0956

TYR 199 HIS 200 0.0002

HIS 200 TYR 201 0.0501

TYR 201 MET 202 -0.0004

MET 202 THR 203 0.1249

THR 203 ASP 204 0.0001

ASP 204 THR 205 0.0336

THR 205 ARG 206 0.0001

ARG 206 GLY 207 0.1903

GLY 207 LEU 208 0.0001

LEU 208 ASP 209 0.1386

ASP 209 HIS 210 0.0002

HIS 210 LEU 211 -0.0238

LEU 211 ILE 212 -0.0002

ILE 212 TRP 213 -0.0272

TRP 213 VAL 214 -0.0000

VAL 214 TYR 215 -0.0571

TYR 215 SER 216 -0.0001

SER 216 PRO 217 -0.0058

PRO 217 ASP 218 -0.0001

ASP 218 ALA 219 -0.1477

ALA 219 ASN 220 0.0002

ASN 220 ARG 221 0.0694

ARG 221 ASP 222 -0.0001

ASP 222 PHE 223 -0.0328

PHE 223 LYS 224 -0.0001

LYS 224 THR 225 -0.0026

THR 225 ASP 226 0.0001

ASP 226 PHE 227 -0.0195

PHE 227 TYR 228 0.0000

TYR 228 PRO 229 0.0265

PRO 229 GLY 230 0.0000

GLY 230 ALA 231 0.0327

ALA 231 SER 232 -0.0003

SER 232 TYR 233 0.0255

TYR 233 VAL 234 0.0000

VAL 234 ASP 235 -0.0000

ASP 235 ILE 236 0.0001

ILE 236 VAL 237 -0.0370

VAL 237 GLY 238 -0.0000

GLY 238 LEU 239 -0.0093

LEU 239 ASP 240 0.0004

ASP 240 ALA 241 -0.1210

ALA 241 TYR 242 0.0000

TYR 242 PHE 243 -0.1349

PHE 243 GLN 244 -0.0000

GLN 244 ASP 245 0.0133

ASP 245 ALA 246 0.0000

ALA 246 TYR 247 0.0140

TYR 247 SER 248 0.0000

SER 248 ILE 249 -0.0570

ILE 249 ASN 250 -0.0002

ASN 250 GLY 251 0.1105

GLY 251 TYR 252 -0.0002

TYR 252 ASP 253 0.0145

ASP 253 GLN 254 -0.0002

GLN 254 LEU 255 -0.0163

LEU 255 THR 256 -0.0001

THR 256 ALA 257 -0.0033

ALA 257 LEU 258 -0.0004

LEU 258 ASN 259 -0.0615

ASN 259 LYS 260 -0.0001

LYS 260 PRO 261 0.0035

PRO 261 PHE 262 0.0002

PHE 262 ALA 263 -0.0116

ALA 263 PHE 264 -0.0001

PHE 264 THR 265 -0.0692

THR 265 GLU 266 -0.0002

GLU 266 VAL 267 -0.1047

VAL 267 GLY 268 0.0002

GLY 268 PRO 269 -0.0324

PRO 269 GLN 270 0.0000

GLN 270 THR 271 0.0185

THR 271 ALA 272 0.0005

ALA 272 ASN 273 -0.0336

ASN 273 GLY 274 -0.0002

GLY 274 SER 275 -0.0317

SER 275 PHE 276 0.0000

PHE 276 ASP 277 0.0486

ASP 277 TYR 278 0.0001

TYR 278 SER 279 -0.0536

SER 279 LEU 280 0.0002

LEU 280 PHE 281 -0.0135

PHE 281 ILE 282 0.0002

ILE 282 ASN 283 -0.0211

ASN 283 ALA 284 0.0001

ALA 284 ILE 285 0.0025

ILE 285 LYS 286 -0.0002

LYS 286 GLN 287 -0.0206

GLN 287 LYS 288 -0.0003

LYS 288 TYR 289 0.0069

TYR 289 PRO 290 0.0003

PRO 290 LYS 291 0.1171

LYS 291 THR 292 0.0003

THR 292 ILE 293 0.0694

ILE 293 TYR 294 -0.0003

TYR 294 PHE 295 -0.0608

PHE 295 LEU 296 -0.0001

LEU 296 ALA 297 -0.0020

ALA 297 TRP 298 0.0003

TRP 298 ASN 299 0.0593

ASN 299 ASP 300 0.0001

ASP 300 GLU 301 -0.1633

GLU 301 TRP 302 -0.0002

TRP 302 SER 303 0.0754

SER 303 ALA 304 0.0000

ALA 304 ALA 305 0.0053

ALA 305 VAL 306 0.0001

VAL 306 ASN 307 -0.0087

ASN 307 LYS 308 0.0001

LYS 308 GLY 309 0.0641

GLY 309 ALA 310 0.0002

ALA 310 SER 311 -0.0091

SER 311 ALA 312 -0.0001

ALA 312 LEU 313 -0.0236

LEU 313 TYR 314 0.0001

TYR 314 HIS 315 -0.0322

HIS 315 ASP 316 0.0002

ASP 316 SER 317 0.0163

SER 317 TRP 318 -0.0000

TRP 318 THR 319 -0.0276

THR 319 LEU 320 0.0000

LEU 320 ASN 321 -0.0220

ASN 321 LYS 322 -0.0002

LYS 322 GLY 323 0.0404

GLY 323 GLU 324 -0.0000

GLU 324 ILE 325 0.0531

ILE 325 TRP 326 -0.0004

TRP 326 ASN 327 0.0527

ASN 327 GLY 328 -0.0002

GLY 328 ASP 329 -0.0386

ASP 329 SER 330 0.0002

SER 330 LEU 331 -0.1296

LEU 331 THR 332 -0.0002

THR 332 PRO 333 0.1207

PRO 333 ILE 334 0.0004

ILE 334 VAL 335 0.2162

VAL 335 GLU 336 0.0003

GLU 336 LEU 337 0.2689

LEU 337 GLU 338 0.0000

If you find results from this site helpful for your research, please cite one of our papers:

K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.

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.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** BMan WT ***

CA strain for 261030074727917150

--- normal mode 8 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* BMan WT *