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

* *

CA strain for 2606181404432809667

--- 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
ALA 4 ALA 5 0.0001

ALA 5 ALA 6 0.0040

ALA 6 ILE 7 -0.0003

ILE 7 GLY 8 -0.0011

GLY 8 ILE 9 -0.0003

ILE 9 ASP 10 0.0024

ASP 10 LEU 11 -0.0002

LEU 11 GLY 12 0.0025

GLY 12 THR 13 -0.0001

THR 13 THR 14 0.0114

THR 14 TYR 15 -0.0003

TYR 15 SER 16 0.0341

SER 16 CYS 17 0.0002

CYS 17 VAL 18 0.0064

VAL 18 GLY 19 -0.0001

GLY 19 VAL 20 -0.0005

VAL 20 PHE 21 -0.0000

PHE 21 GLN 22 -0.0088

GLN 22 HIS 23 0.0002

HIS 23 GLY 24 0.0003

GLY 24 LYS 25 -0.0000

LYS 25 VAL 26 0.0146

VAL 26 GLU 27 -0.0000

GLU 27 ILE 28 0.0087

ILE 28 ILE 29 0.0004

ILE 29 ALA 30 -0.0016

ALA 30 ASN 31 0.0001

ASN 31 ASP 32 -0.0086

ASP 32 GLN 33 -0.0001

GLN 33 GLY 34 -0.0247

GLY 34 ASN 35 -0.0001

ASN 35 ARG 36 -0.0151

ARG 36 THR 37 0.0000

THR 37 THR 38 -0.0225

THR 38 PRO 39 0.0003

PRO 39 SER 40 0.0079

SER 40 TYR 41 0.0002

TYR 41 VAL 42 -0.0021

VAL 42 ALA 43 0.0003

ALA 43 PHE 44 -0.0011

PHE 44 THR 45 -0.0002

THR 45 ASP 46 0.0042

ASP 46 THR 47 0.0000

THR 47 GLU 48 -0.0275

GLU 48 ARG 49 0.0002

ARG 49 LEU 50 -0.0113

LEU 50 ILE 51 -0.0002

ILE 51 GLY 52 -0.0063

GLY 52 ASP 53 0.0001

ASP 53 ALA 54 -0.0153

ALA 54 ALA 55 0.0000

ALA 55 LYS 56 -0.0057

LYS 56 ASN 57 -0.0004

ASN 57 GLN 58 -0.0190

GLN 58 VAL 59 -0.0002

VAL 59 ALA 60 0.0281

ALA 60 LEU 61 -0.0002

LEU 61 ASN 62 0.0534

ASN 62 PRO 63 0.0001

PRO 63 GLN 64 -0.0497

GLN 64 ASN 65 -0.0003

ASN 65 THR 66 0.0052

THR 66 VAL 67 -0.0001

VAL 67 PHE 68 0.0257

PHE 68 ASP 69 -0.0001

ASP 69 ALA 70 -0.0186

ALA 70 LYS 71 0.0001

LYS 71 ARG 72 0.0022

ARG 72 LEU 73 -0.0002

LEU 73 ILE 74 -0.0212

ILE 74 GLY 75 -0.0002

GLY 75 ARG 76 -0.0011

ARG 76 LYS 77 0.0002

LYS 77 PHE 78 0.0119

PHE 78 GLY 79 0.0001

GLY 79 ASP 80 0.0041

ASP 80 PRO 81 -0.0002

PRO 81 VAL 82 -0.0092

VAL 82 VAL 83 0.0003

VAL 83 GLN 84 0.0042

GLN 84 SER 85 0.0002

SER 85 ASP 86 -0.0023

ASP 86 MET 87 0.0001

MET 87 LYS 88 0.0148

LYS 88 HIS 89 0.0002

HIS 89 TRP 90 0.0170

TRP 90 PRO 91 0.0001

PRO 91 PHE 92 -0.0799

PHE 92 GLN 93 0.0002

GLN 93 VAL 94 -0.0401

VAL 94 ILE 95 -0.0000

ILE 95 ASN 96 -0.0159

ASN 96 ASP 97 -0.0003

ASP 97 GLY 98 -0.0076

GLY 98 ASP 99 -0.0002

ASP 99 LYS 100 -0.0027

LYS 100 PRO 101 0.0003

PRO 101 LYS 102 0.0113

LYS 102 VAL 103 0.0000

VAL 103 GLN 104 0.0180

GLN 104 VAL 105 -0.0002

VAL 105 SER 106 0.0271

SER 106 TYR 107 0.0001

TYR 107 LYS 108 0.0031

LYS 108 GLY 109 0.0003

GLY 109 GLU 110 0.0064

GLU 110 THR 111 0.0001

THR 111 LYS 112 -0.0054

LYS 112 ALA 113 -0.0001

ALA 113 PHE 114 0.0028

PHE 114 TYR 115 -0.0005

TYR 115 PRO 116 0.0102

PRO 116 GLU 117 0.0001

GLU 117 GLU 118 0.0066

GLU 118 ILE 119 -0.0002

ILE 119 SER 120 -0.0008

SER 120 SER 121 0.0000

SER 121 MET 122 0.0150

MET 122 VAL 123 0.0000

VAL 123 LEU 124 0.0089

LEU 124 THR 125 0.0001

THR 125 LYS 126 0.0239

LYS 126 MET 127 -0.0002

MET 127 LYS 128 0.0149

LYS 128 GLU 129 -0.0000

GLU 129 ILE 130 -0.0003

ILE 130 ALA 131 0.0004

ALA 131 GLU 132 0.0075

GLU 132 ALA 133 -0.0000

ALA 133 TYR 134 -0.0077

TYR 134 LEU 135 0.0000

LEU 135 GLY 136 0.0133

GLY 136 TYR 137 -0.0001

TYR 137 PRO 138 0.0010

PRO 138 VAL 139 -0.0001

VAL 139 THR 140 0.0031

THR 140 ASN 141 0.0001

ASN 141 ALA 142 0.0002

ALA 142 VAL 143 0.0001

VAL 143 ILE 144 0.0123

ILE 144 THR 145 0.0001

THR 145 VAL 146 -0.0009

VAL 146 PRO 147 0.0001

PRO 147 ALA 148 0.0290

ALA 148 TYR 149 0.0002

TYR 149 PHE 150 0.0266

PHE 150 ASN 151 -0.0005

ASN 151 ASP 152 -0.0107

ASP 152 SER 153 0.0001

SER 153 GLN 154 0.0014

GLN 154 ARG 155 -0.0001

ARG 155 GLN 156 -0.0028

GLN 156 ALA 157 -0.0001

ALA 157 THR 158 0.0030

THR 158 LYS 159 -0.0001

LYS 159 ASP 160 0.0059

ASP 160 ALA 161 -0.0003

ALA 161 GLY 162 -0.0084

GLY 162 VAL 163 -0.0000

VAL 163 ILE 164 -0.0012

ILE 164 ALA 165 0.0001

ALA 165 GLY 166 -0.0073

GLY 166 LEU 167 -0.0001

LEU 167 ASN 168 0.0118

ASN 168 VAL 169 -0.0004

VAL 169 LEU 170 0.0300

LEU 170 ARG 171 0.0001

ARG 171 ILE 172 0.0345

ILE 172 ILE 173 0.0000

ILE 173 ASN 174 0.0076

ASN 174 GLU 175 -0.0001

GLU 175 PRO 176 0.0019

PRO 176 THR 177 0.0004

THR 177 ALA 178 -0.0037

ALA 178 ALA 179 0.0002

ALA 179 ALA 180 0.0046

ALA 180 ILE 181 0.0001

ILE 181 ALA 182 0.0064

ALA 182 TYR 183 -0.0003

TYR 183 GLY 184 0.0360

GLY 184 LEU 185 -0.0001

LEU 185 ASP 186 0.0044

ASP 186 ARG 187 -0.0002

ARG 187 THR 188 -0.0111

THR 188 GLY 189 0.0002

GLY 189 LYS 190 0.0049

LYS 190 GLY 191 0.0001

GLY 191 GLU 192 -0.0079

GLU 192 ARG 193 0.0001

ARG 193 ASN 194 -0.0139

ASN 194 VAL 195 -0.0001

VAL 195 LEU 196 -0.0146

LEU 196 ILE 197 -0.0000

ILE 197 PHE 198 -0.0059

PHE 198 ASP 199 0.0000

ASP 199 LEU 200 -0.0156

LEU 200 GLY 201 0.0000

GLY 201 GLY 202 -0.0112

GLY 202 GLY 203 -0.0000

GLY 203 THR 204 -0.0172

THR 204 PHE 205 0.0002

PHE 205 ASP 206 -0.0223

ASP 206 VAL 207 0.0004

VAL 207 SER 208 -0.0320

SER 208 ILE 209 0.0002

ILE 209 LEU 210 -0.0317

LEU 210 THR 211 -0.0000

THR 211 ILE 212 -0.0178

ILE 212 ASP 213 0.0001

ASP 213 ASP 214 -0.0039

ASP 214 GLY 215 0.0004

GLY 215 ILE 216 -0.0042

ILE 216 PHE 217 -0.0002

PHE 217 GLU 218 -0.0132

GLU 218 VAL 219 -0.0002

VAL 219 LYS 220 0.0094

LYS 220 ALA 221 0.0001

ALA 221 THR 222 0.0008

THR 222 ALA 223 -0.0002

ALA 223 GLY 224 -0.0430

GLY 224 ASP 225 -0.0002

ASP 225 THR 226 0.1009

THR 226 HIS 227 -0.0002

HIS 227 LEU 228 0.0316

LEU 228 GLY 229 -0.0002

GLY 229 GLY 230 0.0096

GLY 230 GLU 231 0.0001

GLU 231 ASP 232 0.0469

ASP 232 PHE 233 -0.0003

PHE 233 ASP 234 -0.0046

ASP 234 ASN 235 -0.0004

ASN 235 ARG 236 0.0602

ARG 236 LEU 237 0.0001

LEU 237 VAL 238 -0.0185

VAL 238 ASN 239 -0.0001

ASN 239 HIS 240 0.0552

HIS 240 PHE 241 -0.0003

PHE 241 VAL 242 0.0324

VAL 242 GLU 243 -0.0003

GLU 243 GLU 244 0.0218

GLU 244 PHE 245 0.0001

PHE 245 LYS 246 0.0416

LYS 246 ARG 247 -0.0001

ARG 247 LYS 248 -0.0016

LYS 248 HIS 249 0.0002

HIS 249 LYS 250 0.0231

LYS 250 LYS 251 0.0002

LYS 251 ASP 252 -0.0048

ASP 252 ILE 253 0.0001

ILE 253 SER 254 -0.0019

SER 254 GLN 255 -0.0002

GLN 255 ASN 256 0.0208

ASN 256 LYS 257 0.0002

LYS 257 ARG 258 0.0067

ARG 258 ALA 259 -0.0000

ALA 259 VAL 260 -0.0225

VAL 260 ARG 261 0.0002

ARG 261 ARG 262 -0.0390

ARG 262 LEU 263 0.0000

LEU 263 ARG 264 0.0139

ARG 264 THR 265 -0.0003

THR 265 ALA 266 -0.0090

ALA 266 CYS 267 -0.0000

CYS 267 GLU 268 0.0562

GLU 268 ARG 269 0.0004

ARG 269 ALA 270 -0.0139

ALA 270 LYS 271 0.0000

LYS 271 ARG 272 0.0435

ARG 272 THR 273 -0.0002

THR 273 LEU 274 -0.0388

LEU 274 SER 275 0.0001

SER 275 SER 276 -0.0153

SER 276 SER 277 0.0000

SER 277 THR 278 -0.0097

THR 278 GLN 279 0.0002

GLN 279 ALA 280 0.0249

ALA 280 SER 281 -0.0000

SER 281 LEU 282 -0.0140

LEU 282 GLU 283 -0.0002

GLU 283 ILE 284 -0.0310

ILE 284 ASP 285 -0.0001

ASP 285 SER 286 -0.0033

SER 286 LEU 287 0.0003

LEU 287 PHE 288 0.0187

PHE 288 GLU 289 -0.0000

GLU 289 GLY 290 0.0071

GLY 290 ILE 291 0.0003

ILE 291 ASP 292 0.0364

ASP 292 PHE 293 0.0005

PHE 293 TYR 294 0.0596

TYR 294 THR 295 -0.0001

THR 295 SER 296 0.0395

SER 296 ILE 297 -0.0003

ILE 297 THR 298 0.0491

THR 298 ARG 299 -0.0002

ARG 299 ALA 300 -0.0052

ALA 300 ARG 301 -0.0003

ARG 301 PHE 302 0.0116

PHE 302 GLU 303 -0.0002

GLU 303 GLU 304 0.0175

GLU 304 LEU 305 -0.0001

LEU 305 CYS 306 -0.0564

CYS 306 SER 307 -0.0001

SER 307 ASP 308 -0.0058

ASP 308 LEU 309 0.0000

LEU 309 PHE 310 -0.0117

PHE 310 ARG 311 0.0005

ARG 311 SER 312 0.0405

SER 312 THR 313 -0.0002

THR 313 LEU 314 -0.0154

LEU 314 GLU 315 0.0003

GLU 315 PRO 316 0.0059

PRO 316 VAL 317 -0.0001

VAL 317 GLU 318 0.0139

GLU 318 LYS 319 -0.0002

LYS 319 ALA 320 -0.0025

ALA 320 LEU 321 -0.0004

LEU 321 ARG 322 0.0151

ARG 322 ASP 323 -0.0000

ASP 323 ALA 324 -0.0009

ALA 324 LYS 325 0.0002

LYS 325 LEU 326 -0.0020

LEU 326 ASP 327 0.0004

ASP 327 LYS 328 0.0039

LYS 328 ALA 329 0.0001

ALA 329 GLN 330 -0.0044

GLN 330 ILE 331 0.0002

ILE 331 HIS 332 -0.0112

HIS 332 ASP 333 -0.0002

ASP 333 LEU 334 0.0087

LEU 334 VAL 335 -0.0002

VAL 335 LEU 336 0.0325

LEU 336 VAL 337 0.0002

VAL 337 GLY 338 0.0316

GLY 338 GLY 339 0.0001

GLY 339 SER 340 0.0121

SER 340 THR 341 -0.0001

THR 341 ARG 342 0.0397

ARG 342 ILE 343 0.0001

ILE 343 PRO 344 -0.0195

PRO 344 LYS 345 0.0000

LYS 345 VAL 346 -0.0050

VAL 346 GLN 347 0.0002

GLN 347 LYS 348 -0.0131

LYS 348 LEU 349 0.0002

LEU 349 LEU 350 -0.0168

LEU 350 GLN 351 -0.0003

GLN 351 ASP 352 -0.0014

ASP 352 PHE 353 0.0001

PHE 353 PHE 354 -0.0070

PHE 354 ASN 355 0.0003

ASN 355 GLY 356 -0.0031

GLY 356 ARG 357 0.0002

ARG 357 ASP 358 -0.0207

ASP 358 LEU 359 -0.0001

LEU 359 ASN 360 -0.0232

ASN 360 LYS 361 0.0001

LYS 361 SER 362 0.0215

SER 362 ILE 363 0.0002

ILE 363 ASN 364 0.0385

ASN 364 PRO 365 0.0001

PRO 365 ASP 366 -0.0264

ASP 366 GLU 367 0.0003

GLU 367 ALA 368 -0.0039

ALA 368 VAL 369 -0.0001

VAL 369 ALA 370 -0.0058

ALA 370 TYR 371 0.0001

TYR 371 GLY 372 0.0084

GLY 372 ALA 373 -0.0001

ALA 373 ALA 374 -0.0105

ALA 374 VAL 375 0.0001

VAL 375 GLN 376 -0.0010

GLN 376 ALA 377 0.0002

ALA 377 ALA 378 -0.0642

ALA 378 ILE 379 -0.0001

ILE 379 LEU 380 -0.0239

LEU 380 ILE 381 -0.0002

ILE 381 LYS 382 -0.0889

LYS 382 SER 383 0.0000

SER 383 THR 384 0.0167

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.

*** ***

CA strain for 2606181404432809667

--- 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.

* *