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 260522121915448221

--- 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 1 SER 2 0.0003

SER 2 SER 3 -0.0003

SER 3 THR 4 0.0076

THR 4 ASN 5 -0.0049

ASN 5 LEU 6 -0.0222

LEU 6 LYS 7 0.0275

LYS 7 ASP 8 0.0117

ASP 8 VAL 9 -0.0268

VAL 9 LEU 10 0.0094

LEU 10 ALA 11 -0.0223

ALA 11 ALA 12 0.0259

ALA 12 LEU 13 0.0055

LEU 13 ILE 14 -0.0758

ILE 14 PRO 15 0.0418

PRO 15 LYS 16 0.0372

LYS 16 GLU 17 -0.0399

GLU 17 GLN 18 -0.0162

GLN 18 ALA 19 0.0298

ALA 19 ARG 20 -0.0468

ARG 20 ILE 21 -0.0747

ILE 21 LYS 22 0.0912

LYS 22 THR 23 -0.0249

THR 23 PHE 24 -0.0312

PHE 24 ARG 25 0.0156

ARG 25 GLN 26 -0.0021

GLN 26 GLN 27 -0.0133

GLN 27 HIS 28 -0.0076

HIS 28 GLY 29 0.0035

GLY 29 GLY 30 -0.0857

GLY 30 THR 31 -0.0598

THR 31 ALA 32 0.0679

ALA 32 LEU 33 0.0061

LEU 33 GLY 34 -0.0248

GLY 34 GLN 35 -0.0083

GLN 35 ILE 36 -0.0069

ILE 36 THR 37 -0.0327

THR 37 VAL 38 0.1299

VAL 38 ASP 39 0.0949

ASP 39 MET 40 0.0334

MET 40 SER 41 -0.0150

SER 41 TYR 42 -0.0769

TYR 42 GLY 43 0.0851

GLY 43 GLY 44 0.0273

GLY 44 MET 45 0.0485

MET 45 ARG 46 0.0625

ARG 46 GLY 47 -0.0268

GLY 47 MET 48 -0.0119

MET 48 LYS 49 -0.0407

LYS 49 GLY 50 0.0505

GLY 50 LEU 51 0.1473

LEU 51 VAL 52 0.0065

VAL 52 TYR 53 -0.0563

TYR 53 GLU 54 0.0102

GLU 54 THR 55 0.0023

THR 55 SER 56 -0.0123

SER 56 VAL 57 0.0037

VAL 57 LEU 58 -0.0335

LEU 58 ASP 59 0.0033

ASP 59 PRO 60 0.0016

PRO 60 ASP 61 -0.0038

ASP 61 GLU 62 0.0153

GLU 62 GLY 63 -0.0175

GLY 63 ILE 64 -0.0030

ILE 64 ARG 65 0.0022

ARG 65 PHE 66 0.0100

PHE 66 ARG 67 0.0001

ARG 67 GLY 68 0.0045

GLY 68 PHE 69 -0.0056

PHE 69 SER 70 0.0079

SER 70 ILE 71 0.0061

ILE 71 PRO 72 -0.0092

PRO 72 GLU 73 0.0090

GLU 73 CYS 74 0.0089

CYS 74 GLN 75 -0.0004

GLN 75 LYS 76 0.0013

LYS 76 LEU 77 0.0002

LEU 77 LEU 78 0.0002

LEU 78 PRO 79 0.0036

PRO 79 LYS 80 0.0017

LYS 80 GLY 81 -0.0032

GLY 81 GLY 82 0.0005

GLY 82 GLY 84 0.0017

GLY 84 GLY 85 -0.0006

GLY 85 GLU 86 0.0016

GLU 86 PRO 87 0.0090

PRO 87 LEU 88 -0.0004

LEU 88 PRO 89 -0.0053

PRO 89 GLU 90 -0.0027

GLU 90 GLY 91 -0.0001

GLY 91 LEU 92 -0.0086

LEU 92 PHE 93 0.0099

PHE 93 TRP 94 -0.0114

TRP 94 LEU 95 -0.0108

LEU 95 LEU 96 -0.0011

LEU 96 VAL 97 -0.0167

VAL 97 THR 98 0.0135

THR 98 GLY 99 -0.0091

GLY 99 GLN 100 -0.0005

GLN 100 ILE 101 0.0052

ILE 101 PRO 102 -0.0050

PRO 102 THR 103 0.0018

THR 103 GLY 104 0.0003

GLY 104 ALA 105 0.0031

ALA 105 GLN 106 -0.0014

GLN 106 VAL 107 0.0018

VAL 107 SER 108 -0.0071

SER 108 TRP 109 0.0068

TRP 109 LEU 110 -0.0023

LEU 110 SER 111 0.0007

SER 111 LYS 112 0.0010

LYS 112 GLU 113 0.0034

GLU 113 TRP 114 -0.0024

TRP 114 ALA 115 0.0010

ALA 115 LYS 116 0.0031

LYS 116 ARG 117 0.0098

ARG 117 ALA 118 0.0078

ALA 118 ALA 119 -0.0017

ALA 119 LEU 120 0.0001

LEU 120 PRO 121 -0.0001

PRO 121 SER 122 0.0052

SER 122 HIS 123 -0.0011

HIS 123 VAL 124 -0.0006

VAL 124 VAL 125 0.0033

VAL 125 THR 126 -0.0008

THR 126 MET 127 0.0003

MET 127 LEU 128 0.0010

LEU 128 ASP 129 -0.0023

ASP 129 ASN 130 0.0008

ASN 130 PHE 131 0.0012

PHE 131 PRO 132 -0.0001

PRO 132 THR 133 -0.0011

THR 133 ASN 134 0.0003

ASN 134 LEU 135 -0.0001

LEU 135 HIS 136 0.0020

HIS 136 PRO 137 0.0001

PRO 137 MET 138 -0.0055

MET 138 SER 139 -0.0017

SER 139 GLN 140 0.0008

GLN 140 LEU 141 0.0010

LEU 141 SER 142 -0.0032

SER 142 ALA 143 0.0019

ALA 143 ALA 144 0.0029

ALA 144 ILE 145 0.0000

ILE 145 THR 146 0.0024

THR 146 ALA 147 0.0036

ALA 147 LEU 148 0.0034

LEU 148 ASN 149 0.0151

ASN 149 SER 150 0.0006

SER 150 GLU 151 0.0005

GLU 151 SER 152 0.0007

SER 152 ASN 153 -0.0025

ASN 153 PHE 154 0.0057

PHE 154 ALA 155 -0.0075

ALA 155 ARG 156 0.0065

ARG 156 ALA 157 -0.0086

ALA 157 TYR 158 0.0154

TYR 158 ALA 159 0.0034

ALA 159 GLU 160 -0.0017

GLU 160 GLY 161 -0.0078

GLY 161 ILE 162 0.0057

ILE 162 LEU 163 0.0034

LEU 163 ARG 164 0.0028

ARG 164 THR 165 -0.0084

THR 165 LYS 166 -0.0036

LYS 166 TYR 167 -0.0019

TYR 167 TRP 168 0.0058

TRP 168 GLU 169 -0.0053

GLU 169 MET 170 0.0047

MET 170 VAL 171 0.0039

VAL 171 TYR 172 -0.0000

TYR 172 GLU 173 0.0027

GLU 173 SER 174 -0.0019

SER 174 ALA 175 -0.0039

ALA 175 MET 176 0.0064

MET 176 ASP 177 -0.0022

ASP 177 LEU 178 0.0025

LEU 178 ILE 179 0.0015

ILE 179 ALA 180 -0.0108

ALA 180 LYS 181 0.0017

LYS 181 LEU 182 -0.0075

LEU 182 PRO 183 0.0036

PRO 183 CYS 184 -0.0007

CYS 184 VAL 185 0.0025

VAL 185 ALA 186 0.0023

ALA 186 ALA 187 -0.0021

ALA 187 LYS 188 0.0003

LYS 188 ILE 189 0.0009

ILE 189 TYR 190 -0.0020

TYR 190 ARG 191 -0.0015

ARG 191 ASN 192 0.0003

ASN 192 LEU 193 0.0024

LEU 193 TYR 194 -0.0022

TYR 194 ARG 195 -0.0025

ARG 195 ALA 196 0.0017

ALA 196 GLY 197 0.0017

GLY 197 SER 198 -0.0008

SER 198 SER 199 -0.0009

SER 199 ILE 200 0.0015

ILE 200 GLY 201 -0.0017

GLY 201 ALA 202 -0.0021

ALA 202 ILE 203 0.0031

ILE 203 ASP 204 0.0007

ASP 204 SER 205 0.0022

SER 205 LYS 206 0.0012

LYS 206 LEU 207 0.0029

LEU 207 ASP 208 -0.0045

ASP 208 TRP 209 0.0027

TRP 209 SER 210 0.0124

SER 210 HIS 211 -0.0023

HIS 211 ASN 212 0.0020

ASN 212 PHE 213 0.0028

PHE 213 THR 214 0.0047

THR 214 ASN 215 0.0039

ASN 215 MET 216 0.0021

MET 216 LEU 217 -0.0034

LEU 217 GLY 218 0.0005

GLY 218 TYR 219 0.0123

TYR 219 THR 220 0.0081

THR 220 ASP 221 -0.0032

ASP 221 ALA 222 -0.0045

ALA 222 GLN 223 0.0182

GLN 223 PHE 224 0.0160

PHE 224 THR 225 0.0101

THR 225 GLU 226 -0.0010

GLU 226 LEU 227 0.0194

LEU 227 MET 228 0.0135

MET 228 ARG 229 0.0023

ARG 229 LEU 230 0.0102

LEU 230 TYR 231 0.0060

TYR 231 LEU 232 0.0035

LEU 232 THR 233 0.0079

THR 233 ILE 234 -0.0055

ILE 234 HIS 235 0.0114

HIS 235 SER 236 0.0054

SER 236 ASP 237 -0.0161

ASP 237 HIS 238 -0.0351

HIS 238 GLU 239 -0.0059

GLU 239 GLY 240 -0.0116

GLY 240 GLY 241 -0.1915

GLY 241 ASN 242 -0.0956

ASN 242 VAL 243 0.0137

VAL 243 SER 244 0.0120

SER 244 ALA 245 0.0054

ALA 245 HIS 246 0.0020

HIS 246 THR 247 0.0024

THR 247 SER 248 0.0071

SER 248 HIS 249 -0.0018

HIS 249 LEU 250 0.0208

LEU 250 VAL 251 -0.0202

VAL 251 GLY 252 -0.0052

GLY 252 SER 253 0.0060

SER 253 ALA 254 -0.0504

ALA 254 LEU 255 0.0319

LEU 255 SER 256 0.0044

SER 256 ASP 257 -0.0041

ASP 257 PRO 258 0.0019

PRO 258 TYR 259 0.0013

TYR 259 LEU 260 0.0027

LEU 260 SER 261 0.0038

SER 261 PHE 262 -0.0012

PHE 262 ALA 263 0.0030

ALA 263 ALA 264 -0.0052

ALA 264 ALA 265 0.0132

ALA 265 MET 266 -0.0180

MET 266 ASN 267 0.0111

ASN 267 GLY 268 0.0071

GLY 268 LEU 269 0.0076

LEU 269 ALA 270 0.0011

ALA 270 GLY 271 0.0004

GLY 271 PRO 272 -0.0072

PRO 272 LEU 273 -0.0012

LEU 273 HIS 274 -0.0025

HIS 274 GLY 275 0.0125

GLY 275 LEU 276 -0.0105

LEU 276 ALA 277 0.0030

ALA 277 ASN 278 -0.0067

ASN 278 GLN 279 0.0080

GLN 279 GLU 280 0.0161

GLU 280 VAL 281 -0.0002

VAL 281 LEU 282 -0.0047

LEU 282 GLY 283 0.0086

GLY 283 TRP 284 0.0119

TRP 284 LEU 285 -0.0068

LEU 285 ALA 286 0.0096

ALA 286 GLN 287 0.0029

GLN 287 LEU 288 -0.0069

LEU 288 GLN 289 -0.0055

GLN 289 LYS 290 0.0040

LYS 290 ALA 291 0.0034

ALA 291 ALA 295 -0.0009

ALA 295 GLY 296 0.0029

GLY 296 ALA 297 0.0063

ALA 297 ASP 298 -0.0035

ASP 298 ALA 299 0.0023

ALA 299 SER 300 0.0061

SER 300 LEU 301 -0.0059

LEU 301 ARG 302 -0.0128

ARG 302 ASP 303 0.0028

ASP 303 TYR 304 -0.0033

TYR 304 ILE 305 -0.0023

ILE 305 TRP 306 0.0031

TRP 306 ASN 307 0.0002

ASN 307 THR 308 -0.0048

THR 308 LEU 309 0.0015

LEU 309 ASN 310 0.0002

ASN 310 SER 311 -0.0014

SER 311 GLY 312 0.0020

GLY 312 ARG 313 -0.0026

ARG 313 VAL 314 0.0013

VAL 314 VAL 315 0.0169

VAL 315 PRO 316 -0.0577

PRO 316 GLY 317 0.0021

GLY 317 TYR 318 -0.0085

TYR 318 GLY 319 -0.0015

GLY 319 HIS 320 0.0012

HIS 320 ALA 321 0.0005

ALA 321 VAL 322 -0.0035

VAL 322 LEU 323 0.0072

LEU 323 ARG 324 -0.0043

ARG 324 LYS 325 0.0002

LYS 325 THR 326 0.0015

THR 326 ASP 327 0.0013

ASP 327 PRO 328 -0.0004

PRO 328 ARG 329 0.0065

ARG 329 TYR 330 0.0044

TYR 330 THR 331 -0.0017

THR 331 CYS 332 0.0132

CYS 332 GLN 333 0.0005

GLN 333 ARG 334 0.0127

ARG 334 GLU 335 0.0077

GLU 335 PHE 336 0.0082

PHE 336 ALA 337 0.0194

ALA 337 LEU 338 -0.0151

LEU 338 LYS 339 0.0067

LYS 339 HIS 340 0.0078

HIS 340 LEU 341 0.0028

LEU 341 PRO 342 -0.0011

PRO 342 GLY 343 -0.0005

GLY 343 ASP 344 0.0029

ASP 344 PRO 345 0.0045

PRO 345 MET 346 0.0022

MET 346 PHE 347 -0.0007

PHE 347 LYS 348 -0.0017

LYS 348 LEU 349 0.0091

LEU 349 VAL 350 0.0050

VAL 350 ALA 351 0.0009

ALA 351 GLN 352 0.0335

GLN 352 LEU 353 -0.0088

LEU 353 TYR 354 -0.0041

TYR 354 LYS 355 -0.0017

LYS 355 ILE 356 0.0003

ILE 356 VAL 357 -0.0085

VAL 357 PRO 358 -0.0042

PRO 358 ASN 359 -0.0010

ASN 359 VAL 360 -0.0005

VAL 360 LEU 361 -0.0032

LEU 361 LEU 362 -0.0041

LEU 362 GLU 363 -0.0012

GLU 363 GLN 364 -0.0020

GLN 364 GLY 365 -0.0002

GLY 365 ALA 366 -0.0020

ALA 366 ALA 367 0.0002

ALA 367 ALA 368 -0.0025

ALA 368 ASN 369 0.0036

ASN 369 PRO 370 -0.0067

PRO 370 TRP 371 0.0052

TRP 371 PRO 372 -0.0006

PRO 372 ASN 373 0.0027

ASN 373 VAL 374 -0.0036

VAL 374 ASP 375 0.0081

ASP 375 ALA 376 -0.0036

ALA 376 HIS 377 -0.0002

HIS 377 SER 378 0.0043

SER 378 GLY 379 0.0077

GLY 379 VAL 380 -0.0052

VAL 380 LEU 381 0.0061

LEU 381 LEU 382 -0.0002

LEU 382 GLN 383 0.0103

GLN 383 TYR 384 0.0004

TYR 384 TYR 385 0.0215

TYR 385 GLY 386 0.0026

GLY 386 MET 387 -0.0017

MET 387 THR 388 -0.0082

THR 388 GLU 389 0.0149

GLU 389 MET 390 0.0171

MET 390 ASN 391 -0.0038

ASN 391 TYR 392 0.0019

TYR 392 TYR 393 -0.0007

TYR 393 THR 394 -0.0069

THR 394 VAL 395 -0.0038

VAL 395 LEU 396 0.0009

LEU 396 PHE 397 0.0023

PHE 397 GLY 398 -0.0082

GLY 398 VAL 399 -0.0012

VAL 399 SER 400 -0.0009

SER 400 ARG 401 -0.0121

ARG 401 ALA 402 -0.0020

ALA 402 LEU 403 -0.0039

LEU 403 GLY 404 -0.0160

GLY 404 VAL 405 0.0011

VAL 405 LEU 406 -0.0113

LEU 406 ALA 407 0.0028

ALA 407 GLN 408 -0.0009

GLN 408 LEU 409 -0.0016

LEU 409 ILE 410 0.0016

ILE 410 TRP 411 0.0202

TRP 411 SER 412 0.0016

SER 412 ARG 413 -0.0156

ARG 413 ALA 414 0.0025

ALA 414 LEU 415 -0.0141

LEU 415 GLY 416 0.0293

GLY 416 PHE 417 -0.0298

PHE 417 PRO 418 -0.0632

PRO 418 LEU 419 0.0332

LEU 419 GLU 420 0.0206

GLU 420 ARG 421 0.1208

ARG 421 PRO 422 0.0235

PRO 422 LYS 423 0.0051

LYS 423 SER 424 0.0035

SER 424 MET 425 0.1275

MET 425 SER 426 0.1940

SER 426 THR 427 0.0909

THR 427 ASP 428 -0.0058

ASP 428 GLY 429 0.0379

GLY 429 LEU 430 -0.0865

LEU 430 ILE 431 -0.0150

ILE 431 ALA 432 0.0089

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 260522121915448221

--- 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.

* *