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

* closed-open-cutoff10 *

CA strain for 2604270914072637783

--- normal mode 15 ---

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
SER 3 SER 4 0.0002

SER 4 TRP 5 -0.0002

TRP 5 TRP 6 0.1064

TRP 6 SER 7 -0.0002

SER 7 HIS 8 -0.0000

HIS 8 VAL 9 0.4191

VAL 9 GLU 10 -0.0005

GLU 10 MET 11 0.0002

MET 11 GLY 12 0.0362

GLY 12 PRO 13 0.0000

PRO 13 PRO 14 -0.0000

PRO 14 ASP 15 -0.1655

ASP 15 PRO 16 0.0000

PRO 16 ILE 17 0.0001

ILE 17 LEU 18 -0.1089

LEU 18 GLY 19 0.0002

GLY 19 VAL 20 -0.0002

VAL 20 THR 21 -0.0174

THR 21 GLU 22 -0.0000

GLU 22 ALA 23 0.0001

ALA 23 PHE 24 -0.0142

PHE 24 LYS 25 -0.0002

LYS 25 ARG 26 0.0003

ARG 26 ASP 27 -0.0056

ASP 27 THR 28 0.0001

THR 28 ASN 29 0.0001

ASN 29 SER 30 -0.0119

SER 30 LYS 31 -0.0001

LYS 31 LYS 32 -0.0001

LYS 32 MET 33 0.0195

MET 33 ASN 34 0.0001

ASN 34 LEU 35 0.0000

LEU 35 GLY 36 0.0042

GLY 36 VAL 37 0.0003

VAL 37 GLY 38 -0.0002

GLY 38 ALA 39 0.0281

ALA 39 TYR 40 0.0005

TYR 40 ARG 41 0.0001

ARG 41 ASP 42 -0.0258

ASP 42 ASP 43 0.0002

ASP 43 ASN 44 -0.0003

ASN 44 GLY 45 0.0486

GLY 45 LYS 46 -0.0003

LYS 46 PRO 47 0.0001

PRO 47 TYR 48 0.0379

TYR 48 VAL 49 0.0002

VAL 49 LEU 50 -0.0001

LEU 50 ASN 51 0.0113

ASN 51 CYS 52 0.0002

CYS 52 VAL 53 0.0002

VAL 53 ARG 54 0.0087

ARG 54 LYS 55 -0.0000

LYS 55 ALA 56 -0.0001

ALA 56 GLU 57 0.0284

GLU 57 ALA 58 -0.0002

ALA 58 MET 59 -0.0000

MET 59 ILE 60 -0.1171

ILE 60 ALA 61 -0.0001

ALA 61 ALA 62 -0.0001

ALA 62 LYS 63 -0.0877

LYS 63 LYS 64 -0.0001

LYS 64 MET 66 -0.0000

MET 66 ASP 67 0.0002

ASP 67 LYS 68 -0.0000

LYS 68 GLU 69 0.0741

GLU 69 TYR 70 -0.0001

TYR 70 LEU 71 -0.0004

LEU 71 PRO 72 0.0211

PRO 72 ILE 73 -0.0003

ILE 73 ALA 74 -0.0000

ALA 74 GLY 75 -0.0017

GLY 75 LEU 76 -0.0002

LEU 76 ALA 77 -0.0003

ALA 77 ASP 78 0.0089

ASP 78 PHE 79 0.0001

PHE 79 THR 80 -0.0001

THR 80 ARG 81 -0.0005

ARG 81 ALA 82 0.0000

ALA 82 SER 83 0.0003

SER 83 ALA 84 0.0143

ALA 84 GLU 85 -0.0000

GLU 85 LEU 86 0.0004

LEU 86 ALA 87 -0.0149

ALA 87 LEU 88 0.0001

LEU 88 GLY 89 0.0002

GLY 89 GLU 90 0.0107

GLU 90 ASN 91 0.0001

ASN 91 SER 92 -0.0000

SER 92 GLU 93 -0.0019

GLU 93 ALA 94 0.0005

ALA 94 PHE 95 0.0004

PHE 95 LYS 96 -0.0032

LYS 96 SER 97 -0.0002

SER 97 GLY 98 -0.0003

GLY 98 ARG 99 -0.0011

ARG 99 TYR 100 -0.0000

TYR 100 VAL 101 0.0002

VAL 101 THR 102 -0.0061

THR 102 VAL 103 0.0004

VAL 103 GLN 104 -0.0005

GLN 104 GLY 105 -0.0052

GLY 105 ILE 106 -0.0004

ILE 106 SER 107 -0.0001

SER 107 GLY 108 0.0033

GLY 108 THR 109 -0.0002

THR 109 GLY 110 -0.0003

GLY 110 SER 111 0.0032

SER 111 LEU 112 -0.0003

LEU 112 ARG 113 0.0001

ARG 113 VAL 114 0.0013

VAL 114 GLY 115 -0.0002

GLY 115 ALA 116 -0.0005

ALA 116 ASN 117 0.0125

ASN 117 PHE 118 0.0000

PHE 118 LEU 119 0.0001

LEU 119 GLN 120 0.0023

GLN 120 ARG 121 -0.0001

ARG 121 PHE 122 0.0000

PHE 122 PHE 123 0.0166

PHE 123 LYS 124 0.0001

LYS 124 PHE 125 0.0003

PHE 125 SER 126 -0.0048

SER 126 ARG 129 -0.0003

ARG 129 ASP 130 -0.0001

ASP 130 VAL 133 -0.0033

VAL 133 TYR 134 -0.0001

TYR 134 LEU 135 0.0000

LEU 135 PRO 136 0.0142

PRO 136 LYS 137 -0.0004

LYS 137 PRO 138 -0.0000

PRO 138 SER 139 0.0084

SER 139 TRP 140 -0.0004

TRP 140 GLY 141 0.0002

GLY 141 ASN 142 0.0534

ASN 142 HIS 143 -0.0001

HIS 143 THR 144 0.0002

THR 144 PRO 145 0.0170

PRO 145 ILE 146 0.0001

ILE 146 PHE 147 -0.0001

PHE 147 ARG 148 0.0035

ARG 148 ASP 149 -0.0004

ASP 149 ALA 150 -0.0002

ALA 150 GLY 151 0.0052

GLY 151 LEU 152 0.0001

LEU 152 GLN 154 -0.0002

GLN 154 LEU 155 0.0002

LEU 155 GLN 156 0.0001

GLN 156 ALA 157 0.0357

ALA 157 TYR 158 -0.0004

TYR 158 ARG 159 0.0001

ARG 159 TYR 160 0.0175

TYR 160 TYR 161 -0.0002

TYR 161 ASP 162 -0.0002

ASP 162 PRO 163 -0.0011

PRO 163 LYS 164 0.0000

LYS 164 THR 165 0.0002

THR 165 CYS 166 -0.0160

CYS 166 SER 167 -0.0002

SER 167 LEU 168 0.0001

LEU 168 ASP 169 0.0164

ASP 169 PHE 170 -0.0002

PHE 170 THR 171 0.0002

THR 171 GLY 172 -0.0038

GLY 172 ALA 173 -0.0001

ALA 173 MET 174 0.0001

MET 174 GLU 175 -0.0241

GLU 175 ASP 176 0.0004

ASP 176 ILE 177 0.0003

ILE 177 SER 178 -0.0109

SER 178 LYS 179 -0.0002

LYS 179 ILE 180 -0.0001

ILE 180 PRO 181 -0.0101

PRO 181 GLU 182 -0.0002

GLU 182 LYS 183 0.0002

LYS 183 SER 184 -0.0104

SER 184 ILE 185 0.0002

ILE 185 ILE 186 -0.0000

ILE 186 LEU 187 -0.0229

LEU 187 LEU 188 -0.0002

LEU 188 HIS 189 0.0001

HIS 189 ALA 190 -0.0239

ALA 190 CYS 191 0.0002

CYS 191 ALA 192 0.0001

ALA 192 HIS 193 -0.0226

HIS 193 ASN 194 -0.0003

ASN 194 PRO 195 0.0001

PRO 195 THR 196 0.0002

THR 196 GLY 197 -0.0000

GLY 197 VAL 198 -0.0002

VAL 198 ASP 199 0.0261

ASP 199 PRO 200 0.0001

PRO 200 ARG 201 -0.0001

ARG 201 GLN 202 -0.0038

GLN 202 GLU 203 0.0004

GLU 203 GLN 204 0.0000

GLN 204 TRP 205 -0.0097

TRP 205 LYS 206 0.0001

LYS 206 GLU 207 -0.0002

GLU 207 LEU 208 -0.0065

LEU 208 ALA 209 -0.0001

ALA 209 SER 210 -0.0004

SER 210 VAL 211 -0.0116

VAL 211 VAL 212 0.0002

VAL 212 LYS 213 -0.0000

LYS 213 LYS 214 -0.0017

LYS 214 ARG 215 -0.0002

ARG 215 ASN 216 0.0001

ASN 216 LEU 217 0.0001

LEU 217 LEU 218 0.0001

LEU 218 ALA 219 0.0000

ALA 219 TYR 220 -0.0019

TYR 220 PHE 221 -0.0003

PHE 221 ASP 222 0.0003

ASP 222 MET 223 -0.0149

MET 223 ALA 224 0.0003

ALA 224 TYR 225 0.0002

TYR 225 GLN 226 0.0058

GLN 226 GLY 227 0.0001

GLY 227 PHE 228 0.0000

PHE 228 ALA 229 -0.0122

ALA 229 SER 230 -0.0000

SER 230 GLY 231 0.0005

GLY 231 ASP 232 0.0408

ASP 232 ILE 233 0.0000

ILE 233 ASN 234 0.0003

ASN 234 ARG 235 0.0043

ARG 235 ASP 236 -0.0002

ASP 236 ALA 237 0.0002

ALA 237 TRP 238 -0.0117

TRP 238 ALA 239 -0.0002

ALA 239 LEU 240 -0.0002

LEU 240 ARG 241 -0.0210

ARG 241 HIS 242 0.0002

HIS 242 PHE 243 -0.0001

PHE 243 ILE 244 -0.0101

ILE 244 GLU 245 -0.0001

GLU 245 GLN 246 -0.0002

GLN 246 GLY 247 -0.0077

GLY 247 ILE 248 -0.0001

ILE 248 ASP 249 -0.0000

ASP 249 VAL 250 -0.0021

VAL 250 VAL 251 -0.0005

VAL 251 LEU 252 0.0002

LEU 252 SER 253 -0.0110

SER 253 GLN 254 -0.0002

GLN 254 SER 255 0.0003

SER 255 TYR 256 -0.0081

TYR 256 ALA 257 0.0004

ALA 257 LYS 258 0.0003

LYS 258 ASN 259 0.0373

ASN 259 MET 260 -0.0000

MET 260 GLY 261 0.0003

GLY 261 LEU 262 -0.0175

LEU 262 TYR 263 0.0001

TYR 263 GLY 264 -0.0000

GLY 264 GLU 265 -0.0194

GLU 265 ARG 266 -0.0000

ARG 266 ALA 267 0.0003

ALA 267 GLY 268 0.0004

GLY 268 ALA 269 -0.0003

ALA 269 PHE 270 -0.0003

PHE 270 THR 271 -0.0082

THR 271 VAL 272 0.0003

VAL 272 ILE 273 -0.0001

ILE 273 CYS 274 -0.0041

CYS 274 ARG 275 0.0002

ARG 275 ASP 276 -0.0001

ASP 276 ALA 277 -0.0049

ALA 277 GLU 278 0.0001

GLU 278 GLU 279 0.0004

GLU 279 ALA 280 -0.0017

ALA 280 LYS 281 -0.0001

LYS 281 ARG 282 0.0001

ARG 282 VAL 283 -0.0002

VAL 283 GLU 284 -0.0001

GLU 284 SER 285 -0.0002

SER 285 GLN 286 0.0020

GLN 286 LEU 287 0.0003

LEU 287 LYS 288 -0.0000

LYS 288 ILE 289 0.0052

ILE 289 LEU 290 -0.0002

LEU 290 ILE 291 -0.0003

ILE 291 ARG 292 0.0128

ARG 292 PRO 293 0.0003

PRO 293 MET 294 -0.0002

MET 294 TYR 295 -0.0084

TYR 295 SER 296 0.0001

SER 296 ASN 297 0.0003

ASN 297 PRO 298 -0.0135

PRO 298 PRO 299 -0.0002

PRO 299 MET 300 -0.0005

MET 300 ASN 301 -0.0255

ASN 301 GLY 302 -0.0003

GLY 302 ALA 303 0.0000

ALA 303 ARG 304 0.0255

ARG 304 ILE 305 0.0002

ILE 305 ALA 306 -0.0001

ALA 306 SER 307 0.0298

SER 307 LEU 308 -0.0002

LEU 308 ILE 309 0.0000

ILE 309 LEU 310 0.0236

LEU 310 ASN 311 0.0002

ASN 311 THR 312 -0.0001

THR 312 PRO 313 0.0042

PRO 313 GLU 314 0.0001

GLU 314 LEU 315 0.0003

LEU 315 ARG 316 0.0045

ARG 316 LYS 317 0.0001

LYS 317 GLU 318 0.0000

GLU 318 TRP 319 0.0052

TRP 319 LEU 320 0.0003

LEU 320 VAL 321 0.0000

VAL 321 GLU 322 -0.0174

GLU 322 VAL 323 -0.0002

VAL 323 LYS 324 -0.0001

LYS 324 GLY 325 0.0398

GLY 325 MET 326 0.0001

MET 326 ALA 327 -0.0000

ALA 327 ASP 328 0.0001

ASP 328 ARG 329 -0.0001

ARG 329 ILE 330 0.0002

ILE 330 ILE 331 0.0080

ILE 331 SER 332 -0.0001

SER 332 MET 333 0.0004

MET 333 ARG 334 0.0079

ARG 334 THR 335 -0.0000

THR 335 GLN 336 0.0000

GLN 336 LEU 337 0.0056

LEU 337 VAL 338 0.0003

VAL 338 SER 339 -0.0001

SER 339 ASN 340 0.0039

ASN 340 LEU 341 0.0004

LEU 341 LYS 342 0.0001

LYS 342 LYS 343 0.0024

LYS 343 GLU 344 -0.0002

GLU 344 GLY 345 0.0003

GLY 345 SER 346 0.0119

SER 346 SER 347 0.0003

SER 347 HIS 348 0.0003

HIS 348 ASN 349 0.0170

ASN 349 TRP 350 -0.0001

TRP 350 GLN 351 -0.0003

GLN 351 HIS 352 0.0013

HIS 352 ILE 353 -0.0001

ILE 353 THR 354 -0.0002

THR 354 ASP 355 0.0294

ASP 355 GLN 356 0.0001

GLN 356 ILE 357 0.0001

ILE 357 GLY 358 0.0137

GLY 358 MET 359 -0.0002

MET 359 PHE 360 -0.0004

PHE 360 CYS 361 0.0098

CYS 361 PHE 362 -0.0001

PHE 362 THR 363 -0.0000

THR 363 GLY 364 -0.0101

GLY 364 LEU 365 -0.0002

LEU 365 LYS 366 0.0001

LYS 366 PRO 367 -0.0030

PRO 367 GLU 368 0.0003

GLU 368 GLN 369 0.0003

GLN 369 VAL 370 0.0083

VAL 370 GLU 371 0.0002

GLU 371 ARG 372 -0.0002

ARG 372 LEU 373 0.0069

LEU 373 THR 374 0.0001

THR 374 LYS 375 -0.0002

LYS 375 GLU 376 0.0091

GLU 376 PHE 377 0.0001

PHE 377 SER 378 0.0000

SER 378 ILE 379 -0.0186

ILE 379 TYR 380 -0.0003

TYR 380 MET 381 0.0003

MET 381 THR 382 -0.0080

THR 382 LYS 383 0.0002

LYS 383 ASP 384 0.0003

ASP 384 GLY 385 -0.0047

GLY 385 ARG 386 -0.0000

ARG 386 ILE 387 -0.0002

ILE 387 SER 388 0.0236

SER 388 VAL 389 -0.0005

VAL 389 ALA 390 0.0000

ALA 390 GLY 391 0.0347

GLY 391 VAL 392 -0.0003

VAL 392 ALA 393 -0.0000

ALA 393 SER 394 -0.0104

SER 394 SER 395 -0.0003

SER 395 ASN 396 0.0000

ASN 396 VAL 397 0.0041

VAL 397 GLY 398 -0.0002

GLY 398 TYR 399 -0.0002

TYR 399 LEU 400 0.0003

LEU 400 ALA 401 0.0000

ALA 401 HIS 402 0.0000

HIS 402 ALA 403 -0.0053

ALA 403 ILE 404 0.0002

ILE 404 HIS 405 -0.0002

HIS 405 GLN 406 -0.0013

GLN 406 VAL 408 -0.0001

VAL 408 THR 409 0.0001

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.

*** closed-open-cutoff10 ***

CA strain for 2604270914072637783

--- normal mode 15 ---

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

* closed-open-cutoff10 *