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

* close cutoff 10 melek *

CA strain for 260522120726406031

--- 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 0.0130

SER 2 SER 3 -0.0036

SER 3 THR 4 0.0131

THR 4 ASN 5 0.0094

ASN 5 LEU 6 -0.0723

LEU 6 LYS 7 -0.0062

LYS 7 ASP 8 0.0379

ASP 8 VAL 9 -0.0486

VAL 9 LEU 10 0.0177

LEU 10 ALA 11 -0.0206

ALA 11 SER 12 0.0900

SER 12 LEU 13 0.0168

LEU 13 ILE 14 -0.1927

ILE 14 PRO 15 0.1192

PRO 15 LYS 16 0.1185

LYS 16 GLU 17 -0.0722

GLU 17 GLN 18 0.2200

GLN 18 ALA 19 0.0988

ALA 19 ARG 20 0.3484

ARG 20 ILE 21 -0.0633

ILE 21 LYS 22 0.6127

LYS 22 THR 23 0.4922

THR 23 PHE 24 0.1496

PHE 24 ARG 25 0.6829

ARG 25 GLN 26 0.3661

GLN 26 GLN 27 0.7111

GLN 27 HIS 28 -0.0638

HIS 28 GLY 29 0.7562

GLY 29 ASN 30 0.6935

ASN 30 THR 31 0.7152

THR 31 ALA 32 0.4182

ALA 32 VAL 33 1.0159

VAL 33 GLY 34 0.7580

GLY 34 GLN 35 0.7679

GLN 35 ILE 36 0.2805

ILE 36 THR 37 0.3523

THR 37 VAL 38 0.2959

VAL 38 ASP 39 0.2179

ASP 39 MET 40 0.2783

MET 40 SER 41 0.2588

SER 41 TYR 42 0.3009

TYR 42 GLY 43 0.3061

GLY 43 GLY 44 0.2792

GLY 44 MET 45 0.0500

MET 45 ARG 46 0.2300

ARG 46 GLY 47 0.1911

GLY 47 MET 48 0.3719

MET 48 LYS 49 -0.0063

LYS 49 GLY 50 0.4559

GLY 50 LEU 51 0.5608

LEU 51 ILE 52 -0.1115

ILE 52 TYR 53 0.0053

TYR 53 GLU 54 0.0260

GLU 54 THR 55 -0.0052

THR 55 SER 56 -0.0013

SER 56 VAL 57 -0.0036

VAL 57 LEU 58 -0.0036

LEU 58 ASP 59 0.0232

ASP 59 PRO 60 -0.0018

PRO 60 ASP 61 -0.0124

ASP 61 GLU 62 -0.0100

GLU 62 GLY 63 0.0167

GLY 63 ILE 64 -0.0008

ILE 64 ARG 65 0.0021

ARG 65 PHE 66 -0.0209

PHE 66 ARG 67 -0.0018

ARG 67 GLY 68 0.0010

GLY 68 PHE 69 0.0078

PHE 69 SER 70 -0.0178

SER 70 ILE 71 -0.0016

ILE 71 PRO 72 0.0122

PRO 72 GLU 73 0.0027

GLU 73 CYS 74 -0.0007

CYS 74 GLN 75 0.0088

GLN 75 LYS 76 0.0054

LYS 76 LEU 77 -0.0010

LEU 77 LEU 78 0.0081

LEU 78 PRO 79 0.0022

PRO 79 LYS 80 0.0059

LYS 80 ALA 81 -0.0054

ALA 81 GLY 82 0.0073

GLY 82 GLY 84 0.0021

GLY 84 GLU 85 0.0006

GLU 85 GLU 86 0.0050

GLU 86 PRO 87 0.0040

PRO 87 LEU 88 -0.0012

LEU 88 PRO 89 0.0038

PRO 89 GLU 90 0.0003

GLU 90 GLY 91 0.0031

GLY 91 LEU 92 -0.0017

LEU 92 PHE 93 0.0039

PHE 93 TRP 94 -0.0009

TRP 94 LEU 95 -0.0094

LEU 95 LEU 96 0.0052

LEU 96 VAL 97 -0.0156

VAL 97 THR 98 0.0278

THR 98 GLY 99 -0.0269

GLY 99 GLN 100 -0.0032

GLN 100 ILE 101 0.0034

ILE 101 PRO 102 -0.0063

PRO 102 THR 103 0.0062

THR 103 PRO 104 0.0092

PRO 104 GLU 105 0.0135

GLU 105 GLN 106 -0.0003

GLN 106 VAL 107 0.0097

VAL 107 SER 108 0.0007

SER 108 TRP 109 0.0359

TRP 109 VAL 110 -0.0209

VAL 110 SER 111 0.0231

SER 111 LYS 112 -0.0029

LYS 112 GLU 113 0.0101

GLU 113 TRP 114 0.0102

TRP 114 ALA 115 -0.0030

ALA 115 LYS 116 -0.0036

LYS 116 ARG 117 -0.0013

ARG 117 ALA 118 -0.0003

ALA 118 ALA 119 0.0053

ALA 119 LEU 120 0.0012

LEU 120 PRO 121 0.0010

PRO 121 SER 122 0.0010

SER 122 HIS 123 0.0028

HIS 123 VAL 124 0.0032

VAL 124 VAL 125 -0.0009

VAL 125 THR 126 0.0064

THR 126 MET 127 -0.0004

MET 127 LEU 128 0.0037

LEU 128 ASP 129 0.0021

ASP 129 ASN 130 0.0044

ASN 130 PHE 131 0.0005

PHE 131 PRO 132 0.0039

PRO 132 THR 133 0.0036

THR 133 ASN 134 0.0029

ASN 134 LEU 135 0.0019

LEU 135 HIS 136 0.0018

HIS 136 PRO 137 0.0061

PRO 137 MET 138 0.0049

MET 138 SER 139 0.0025

SER 139 GLN 140 0.0051

GLN 140 LEU 141 0.0038

LEU 141 SER 142 -0.0013

SER 142 ALA 143 0.0038

ALA 143 ALA 144 -0.0004

ALA 144 ILE 145 0.0023

ILE 145 THR 146 0.0056

THR 146 ALA 147 -0.0011

ALA 147 LEU 148 0.0054

LEU 148 ASN 149 0.0001

ASN 149 SER 150 0.0007

SER 150 GLU 151 0.0073

GLU 151 SER 152 0.0002

SER 152 ASN 153 0.0057

ASN 153 PHE 154 -0.0024

PHE 154 ALA 155 0.0071

ALA 155 ARG 156 0.0021

ARG 156 ALA 157 -0.0096

ALA 157 TYR 158 0.0194

TYR 158 ALA 159 -0.0052

ALA 159 GLU 160 0.0010

GLU 160 GLY 161 -0.0019

GLY 161 ILE 162 0.0074

ILE 162 ASN 163 0.0034

ASN 163 ARG 164 0.0002

ARG 164 THR 165 -0.0144

THR 165 LYS 166 -0.0118

LYS 166 TYR 167 -0.0042

TYR 167 TRP 168 0.0312

TRP 168 GLU 169 -0.0154

GLU 169 PHE 170 0.0339

PHE 170 VAL 171 0.0141

VAL 171 TYR 172 0.0124

TYR 172 GLU 173 0.0002

GLU 173 ASP 174 0.0221

ASP 174 ALA 175 0.0057

ALA 175 MET 176 -0.0060

MET 176 ASP 177 0.0029

ASP 177 LEU 178 -0.0029

LEU 178 ILE 179 0.0030

ILE 179 ALA 180 0.0066

ALA 180 LYS 181 0.0025

LYS 181 LEU 182 0.0031

LEU 182 PRO 183 0.0021

PRO 183 CYS 184 0.0035

CYS 184 VAL 185 0.0000

VAL 185 ALA 186 0.0026

ALA 186 ALA 187 0.0032

ALA 187 LYS 188 0.0033

LYS 188 ILE 189 0.0010

ILE 189 TYR 190 0.0029

TYR 190 ARG 191 0.0046

ARG 191 ASN 192 0.0054

ASN 192 LEU 193 -0.0018

LEU 193 TYR 194 0.0042

TYR 194 ARG 195 0.0058

ARG 195 ALA 196 0.0047

ALA 196 GLY 197 -0.0007

GLY 197 SER 198 -0.0001

SER 198 SER 199 0.0041

SER 199 ILE 200 0.0030

ILE 200 GLY 201 0.0024

GLY 201 ALA 202 0.0028

ALA 202 ILE 203 0.0075

ILE 203 ASP 204 0.0004

ASP 204 SER 205 0.0048

SER 205 LYS 206 0.0031

LYS 206 LEU 207 -0.0022

LEU 207 ASP 208 0.0019

ASP 208 TRP 209 -0.0056

TRP 209 SER 210 0.0030

SER 210 HIS 211 0.0053

HIS 211 ASN 212 0.0020

ASN 212 PHE 213 0.0001

PHE 213 THR 214 0.0021

THR 214 ASN 215 -0.0036

ASN 215 MET 216 0.0059

MET 216 LEU 217 0.0011

LEU 217 GLY 218 0.0026

GLY 218 TYR 219 -0.0026

TYR 219 THR 220 0.0079

THR 220 ASP 221 0.0039

ASP 221 PRO 222 0.0049

PRO 222 GLN 223 -0.0019

GLN 223 PHE 224 0.0081

PHE 224 THR 225 0.0081

THR 225 GLU 226 0.0006

GLU 226 LEU 227 0.0067

LEU 227 MET 228 0.0047

MET 228 ARG 229 0.0041

ARG 229 LEU 230 0.0003

LEU 230 TYR 231 0.0043

TYR 231 LEU 232 0.0033

LEU 232 THR 233 0.0017

THR 233 ILE 234 -0.0014

ILE 234 HIS 235 0.0042

HIS 235 SER 236 -0.0001

SER 236 ASP 237 0.0034

ASP 237 HIS 238 -0.0001

HIS 238 GLU 239 0.0244

GLU 239 GLY 240 0.0055

GLY 240 GLY 241 -0.0088

GLY 241 ASN 242 -0.0122

ASN 242 VAL 243 0.0119

VAL 243 SER 244 0.0022

SER 244 ALA 245 0.0010

ALA 245 HIS 246 -0.0129

HIS 246 THR 247 -0.0085

THR 247 SER 248 0.0037

SER 248 HIS 249 -0.0203

HIS 249 LEU 250 0.0136

LEU 250 VAL 251 0.0109

VAL 251 GLY 252 -0.0001

GLY 252 SER 253 0.0052

SER 253 ALA 254 0.0059

ALA 254 LEU 255 0.0613

LEU 255 SER 256 -0.0128

SER 256 ASP 257 -0.0022

ASP 257 PRO 258 0.0034

PRO 258 TYR 259 0.0030

TYR 259 LEU 260 0.0000

LEU 260 SER 261 -0.0016

SER 261 PHE 262 0.0001

PHE 262 ALA 263 0.0006

ALA 263 ALA 264 -0.0022

ALA 264 ALA 265 0.0059

ALA 265 MET 266 -0.0034

MET 266 ASN 267 0.0026

ASN 267 GLY 268 0.0016

GLY 268 LEU 269 0.0021

LEU 269 ALA 270 0.0060

ALA 270 GLY 271 0.0040

GLY 271 PRO 272 -0.0042

PRO 272 LEU 273 0.0098

LEU 273 HIS 274 -0.0082

HIS 274 GLY 275 0.0021

GLY 275 LEU 276 0.0035

LEU 276 ALA 277 0.0045

ALA 277 ASN 278 0.0041

ASN 278 GLN 279 0.0050

GLN 279 GLU 280 0.0029

GLU 280 VAL 281 0.0040

VAL 281 LEU 282 0.0081

LEU 282 LEU 283 0.0107

LEU 283 TRP 284 0.0045

TRP 284 LEU 285 0.0077

LEU 285 SER 286 0.0073

SER 286 GLN 287 0.0070

GLN 287 LEU 288 0.0024

LEU 288 GLN 289 0.0132

GLN 289 LYS 290 0.0125

LYS 290 ASP 291 0.0005

ASP 291 ASP 295 0.0095

ASP 295 ALA 296 0.0072

ALA 296 SER 297 -0.0039

SER 297 ASP 298 0.0069

ASP 298 GLU 299 0.0032

GLU 299 LYS 300 0.0074

LYS 300 LEU 301 0.0009

LEU 301 ARG 302 0.0040

ARG 302 ASP 303 0.0072

ASP 303 TYR 304 0.0015

TYR 304 ILE 305 0.0045

ILE 305 TRP 306 0.0048

TRP 306 ASN 307 0.0055

ASN 307 THR 308 -0.0031

THR 308 LEU 309 0.0055

LEU 309 ASN 310 0.0023

ASN 310 SER 311 0.0035

SER 311 GLY 312 0.0088

GLY 312 ARG 313 0.0061

ARG 313 VAL 314 0.0021

VAL 314 VAL 315 0.0070

VAL 315 PRO 316 -0.0030

PRO 316 GLY 317 0.0037

GLY 317 TYR 318 0.0069

TYR 318 GLY 319 0.0108

GLY 319 HIS 320 0.0046

HIS 320 ALA 321 -0.0295

ALA 321 VAL 322 -0.0693

VAL 322 LEU 323 0.0582

LEU 323 ARG 324 -0.0026

ARG 324 LYS 325 -0.0038

LYS 325 THR 326 0.0053

THR 326 ASP 327 0.0011

ASP 327 PRO 328 -0.0035

PRO 328 ARG 329 0.0021

ARG 329 TYR 330 0.0001

TYR 330 THR 331 0.0062

THR 331 CYS 332 -0.0003

CYS 332 GLN 333 0.0068

GLN 333 ARG 334 0.0065

ARG 334 GLU 335 0.0043

GLU 335 PHE 336 0.0013

PHE 336 ALA 337 0.0064

ALA 337 LEU 338 0.0001

LEU 338 LYS 339 0.0016

LYS 339 HIS 340 0.0027

HIS 340 LEU 341 0.0051

LEU 341 PRO 342 -0.0035

PRO 342 SER 343 0.0067

SER 343 ASP 344 0.0026

ASP 344 PRO 345 0.0056

PRO 345 MET 346 0.0017

MET 346 PHE 347 0.0092

PHE 347 LYS 348 0.0011

LYS 348 LEU 349 0.0062

LEU 349 VAL 350 0.0086

VAL 350 ALA 351 0.0016

ALA 351 GLN 352 0.0048

GLN 352 LEU 353 0.0069

LEU 353 TYR 354 0.0095

TYR 354 LYS 355 0.0045

LYS 355 ILE 356 0.0056

ILE 356 VAL 357 0.0066

VAL 357 PRO 358 0.0072

PRO 358 ASN 359 0.0020

ASN 359 VAL 360 0.0069

VAL 360 LEU 361 0.0053

LEU 361 LEU 362 0.0063

LEU 362 GLU 363 0.0005

GLU 363 GLN 364 0.0056

GLN 364 GLY 365 0.0056

GLY 365 LYS 366 0.0030

LYS 366 ALA 367 0.0063

ALA 367 LYS 368 0.0004

LYS 368 ASN 369 0.0074

ASN 369 PRO 370 0.0054

PRO 370 TRP 371 0.0022

TRP 371 PRO 372 0.0007

PRO 372 ASN 373 0.0023

ASN 373 VAL 374 0.0020

VAL 374 ASP 375 0.0055

ASP 375 ALA 376 0.0030

ALA 376 HIS 377 0.0031

HIS 377 SER 378 0.0023

SER 378 GLY 379 0.0074

GLY 379 VAL 380 -0.0007

VAL 380 LEU 381 0.0038

LEU 381 LEU 382 0.0017

LEU 382 GLN 383 0.0081

GLN 383 TYR 384 0.0002

TYR 384 TYR 385 0.0059

TYR 385 GLY 386 0.0072

GLY 386 MET 387 -0.0010

MET 387 THR 388 0.0117

THR 388 GLU 389 0.0014

GLU 389 MET 390 0.0040

MET 390 ASN 391 -0.0004

ASN 391 TYR 392 0.0080

TYR 392 TYR 393 0.0029

TYR 393 THR 394 -0.0013

THR 394 VAL 395 0.0019

VAL 395 LEU 396 0.0023

LEU 396 PHE 397 0.0013

PHE 397 GLY 398 0.0011

GLY 398 VAL 399 -0.0010

VAL 399 SER 400 0.0028

SER 400 ARG 401 0.0004

ARG 401 ALA 402 -0.0016

ALA 402 LEU 403 0.0008

LEU 403 GLY 404 -0.0003

GLY 404 VAL 405 0.0040

VAL 405 LEU 406 -0.0018

LEU 406 ALA 407 0.0070

ALA 407 GLN 408 -0.0004

GLN 408 LEU 409 0.0074

LEU 409 ILE 410 0.0014

ILE 410 TRP 411 0.0462

TRP 411 SER 412 0.0013

SER 412 ARG 413 0.0414

ARG 413 ALA 414 -0.0082

ALA 414 LEU 415 -0.1214

LEU 415 GLY 416 -0.0116

GLY 416 PHE 417 0.0277

PHE 417 PRO 418 0.0100

PRO 418 LEU 419 0.0145

LEU 419 GLU 420 -0.0209

GLU 420 ARG 421 -0.0284

ARG 421 PRO 422 0.5601

PRO 422 LYS 423 0.3793

LYS 423 SER 424 0.2210

SER 424 MET 425 -0.0911

MET 425 SER 426 0.9134

SER 426 THR 427 0.8421

THR 427 ALA 428 0.4723

ALA 428 GLY 429 0.8898

GLY 429 LEU 430 0.1991

LEU 430 GLU 431 0.8857

GLU 431 LYS 432 0.7190

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.

*** close cutoff 10 melek ***

CA strain for 260522120726406031

--- 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.

* close cutoff 10 melek *