Should you encounter any unexpected behaviour,
please let us know.
elNémo has been hacked on november 27th.
It has been moved away and runs again.
Still some additional cleaning from time to time
Sorry for the inconvenience.

* *

CA strain for 2604191527403651211

--- normal mode 9 ---

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
GLY 1 SER 2 0.0001

SER 2 CYS 3 -0.0001

CYS 3 PHE 4 -0.0004

PHE 4 SER 5 0.0001

SER 5 SER 6 -0.0001

SER 6 ARG 7 0.0003

ARG 7 VAL 8 -0.0001

VAL 8 LYS 9 0.0003

LYS 9 ALA 10 0.0002

ALA 10 ASP 11 -0.0023

ASP 11 ILE 12 -0.0002

ILE 12 PHE 13 -0.0003

PHE 13 HIS 14 -0.0001

HIS 14 ASN 15 0.0002

ASN 15 GLY 16 0.0002

GLY 16 LYS 17 0.0013

LYS 17 SER 18 -0.0000

SER 18 SER 19 0.0001

SER 19 ASP 20 0.0001

ASP 20 LEU 21 0.0002

LEU 21 TYR 22 -0.0001

TYR 22 GLY 23 -0.0008

GLY 23 LEU 24 -0.0003

LEU 24 SER 25 -0.0000

SER 25 LEU 26 0.0001

LEU 26 SER 27 0.0019

SER 27 SER 28 -0.0003

SER 28 ARG 29 -0.0010

ARG 29 LYS 30 -0.0001

LYS 30 SER 31 -0.0021

SER 31 SER 32 0.0001

SER 32 SER 33 0.0076

SER 33 THR 34 -0.0001

THR 34 VAL 35 -0.0011

VAL 35 ALA 36 0.0001

ALA 36 ALA 37 -0.0005

ALA 37 ALA 38 -0.0003

ALA 38 GLN 39 0.0005

GLN 39 LYS 40 0.0000

LYS 40 THR 41 -0.0001

THR 41 GLU 42 -0.0001

GLU 42 GLY 43 0.0000

GLY 43 GLU 44 0.0002

GLU 44 ILE 45 -0.0003

ILE 45 LEU 46 -0.0001

LEU 46 SER 47 -0.0000

SER 47 SER 48 -0.0004

SER 48 THR 49 -0.0002

THR 49 PRO 50 -0.0002

PRO 50 VAL 51 0.0003

VAL 51 LYS 52 0.0001

LYS 52 SER 53 -0.0001

SER 53 PHE 54 -0.0002

PHE 54 THR 55 0.0001

THR 55 PHE 56 -0.0002

PHE 56 ASN 57 0.0001

ASN 57 GLU 58 0.0004

GLU 58 LEU 59 -0.0000

LEU 59 LYS 60 0.0000

LYS 60 LEU 61 0.0000

LEU 61 ALA 62 0.0000

ALA 62 THR 63 -0.0001

THR 63 ARG 64 -0.0004

ARG 64 ASN 65 -0.0002

ASN 65 PHE 66 -0.0000

PHE 66 ARG 67 0.0004

ARG 67 PRO 68 -0.0001

PRO 68 ASP 69 -0.0004

ASP 69 SER 70 -0.0000

SER 70 VAL 71 -0.0002

VAL 71 ILE 72 0.0001

ILE 72 GLY 73 0.0001

GLY 73 GLU 74 0.0003

GLU 74 GLY 75 0.0001

GLY 75 GLY 76 -0.0002

GLY 76 PHE 77 0.0002

PHE 77 GLY 78 -0.0001

GLY 78 CYS 79 0.0003

CYS 79 VAL 80 -0.0001

VAL 80 PHE 81 -0.0000

PHE 81 LYS 82 -0.0004

LYS 82 GLY 83 0.0001

GLY 83 TRP 84 -0.0000

TRP 84 LEU 85 0.0001

LEU 85 ASP 86 -0.0002

ASP 86 GLU 87 -0.0000

GLU 87 SER 88 0.0001

SER 88 THR 89 0.0004

THR 89 LEU 90 0.0002

LEU 90 THR 91 0.0001

THR 91 PRO 92 0.0001

PRO 92 THR 93 0.0001

THR 93 LYS 94 -0.0006

LYS 94 PRO 95 0.0003

PRO 95 GLY 96 -0.0003

GLY 96 THR 97 -0.0003

THR 97 GLY 98 -0.0001

GLY 98 LEU 99 -0.0000

LEU 99 VAL 100 0.0003

VAL 100 ILE 101 -0.0000

ILE 101 ALA 102 0.0000

ALA 102 VAL 103 0.0000

VAL 103 LYS 104 -0.0000

LYS 104 LYS 105 -0.0001

LYS 105 LEU 106 0.0004

LEU 106 ASN 107 -0.0004

ASN 107 GLN 108 0.0000

GLN 108 GLU 109 -0.0004

GLU 109 GLY 110 0.0001

GLY 110 PHE 111 -0.0002

PHE 111 GLN 112 0.0001

GLN 112 GLY 113 -0.0001

GLY 113 HIS 114 -0.0001

HIS 114 ARG 115 -0.0002

ARG 115 GLU 116 -0.0004

GLU 116 TRP 117 0.0002

TRP 117 LEU 118 -0.0001

LEU 118 THR 119 0.0000

THR 119 GLU 120 0.0001

GLU 120 ILE 121 0.0000

ILE 121 ASN 122 -0.0002

ASN 122 TYR 123 -0.0001

TYR 123 LEU 124 -0.0002

LEU 124 GLY 125 -0.0002

GLY 125 GLN 126 -0.0001

GLN 126 LEU 127 -0.0001

LEU 127 SER 128 -0.0001

SER 128 HIS 129 -0.0001

HIS 129 PRO 130 -0.0001

PRO 130 ASN 131 -0.0000

ASN 131 LEU 132 -0.0002

LEU 132 VAL 133 -0.0004

VAL 133 LYS 134 0.0003

LYS 134 LEU 135 -0.0003

LEU 135 ILE 136 0.0001

ILE 136 GLY 137 -0.0002

GLY 137 TYR 138 0.0001

TYR 138 CYS 139 -0.0000

CYS 139 LEU 140 0.0002

LEU 140 GLU 141 -0.0001

GLU 141 ASP 142 0.0004

ASP 142 GLU 143 -0.0001

GLU 143 HIS 144 0.0002

HIS 144 ARG 145 0.0002

ARG 145 LEU 146 0.0002

LEU 146 LEU 147 -0.0001

LEU 147 VAL 148 -0.0002

VAL 148 TYR 149 -0.0000

TYR 149 GLU 150 0.0003

GLU 150 PHE 151 -0.0002

PHE 151 MET 152 -0.0001

MET 152 GLN 153 0.0000

GLN 153 LYS 154 -0.0001

LYS 154 GLY 155 0.0001

GLY 155 SER 156 -0.0001

SER 156 LEU 157 0.0001

LEU 157 GLU 158 0.0001

GLU 158 ASN 159 -0.0006

ASN 159 HIS 160 -0.0000

HIS 160 LEU 161 0.0001

LEU 161 PHE 162 -0.0003

PHE 162 ARG 163 -0.0002

ARG 163 ARG 164 -0.0002

ARG 164 GLY 165 0.0001

GLY 165 ALA 166 -0.0001

ALA 166 TYR 167 -0.0003

TYR 167 PHE 168 0.0001

PHE 168 LYS 169 0.0002

LYS 169 PRO 170 -0.0004

PRO 170 LEU 171 -0.0004

LEU 171 PRO 172 0.0002

PRO 172 TRP 173 0.0005

TRP 173 PHE 174 0.0002

PHE 174 LEU 175 0.0004

LEU 175 ARG 176 0.0002

ARG 176 VAL 177 -0.0001

VAL 177 ASN 178 -0.0001

ASN 178 VAL 179 -0.0002

VAL 179 ALA 180 -0.0002

ALA 180 LEU 181 0.0001

LEU 181 ASP 182 -0.0004

ASP 182 ALA 183 0.0001

ALA 183 ALA 184 -0.0000

ALA 184 LYS 185 -0.0003

LYS 185 GLY 186 0.0003

GLY 186 LEU 187 -0.0001

LEU 187 ALA 188 -0.0001

ALA 188 PHE 189 -0.0002

PHE 189 LEU 190 -0.0001

LEU 190 HIS 191 -0.0000

HIS 191 SER 192 0.0002

SER 192 ASP 193 -0.0002

ASP 193 PRO 194 0.0001

PRO 194 VAL 195 0.0000

VAL 195 LYS 196 -0.0002

LYS 196 VAL 197 -0.0000

VAL 197 ILE 198 0.0002

ILE 198 TYR 199 -0.0001

TYR 199 ARG 200 -0.0003

ARG 200 ASP 201 0.0000

ASP 201 ILE 202 0.0000

ILE 202 LYS 203 0.0003

LYS 203 ALA 204 -0.0004

ALA 204 SER 205 -0.0002

SER 205 ASN 206 -0.0002

ASN 206 ILE 207 -0.0004

ILE 207 LEU 208 0.0002

LEU 208 LEU 209 0.0002

LEU 209 ASP 210 -0.0002

ASP 210 ALA 211 -0.0004

ALA 211 ASP 212 0.0000

ASP 212 TYR 213 -0.0003

TYR 213 ASN 214 0.0003

ASN 214 ALA 215 0.0002

ALA 215 LYS 216 -0.0001

LYS 216 LEU 217 0.0000

LEU 217 SER 218 -0.0001

SER 218 ASP 219 0.0000

ASP 219 PHE 220 -0.0002

PHE 220 GLY 221 -0.0000

GLY 221 LEU 222 0.0001

LEU 222 ALA 223 0.0002

ALA 223 ARG 224 -0.0003

ARG 224 ASP 225 0.0005

ASP 225 GLY 226 -0.0000

GLY 226 PRO 227 0.0003

PRO 227 MET 228 0.0003

MET 228 GLY 229 0.0004

GLY 229 ASP 230 0.0001

ASP 230 LEU 231 -0.0002

LEU 231 SER 232 -0.0003

SER 232 TYR 233 -0.0002

TYR 233 VAL 234 -0.0002

VAL 234 SER 235 0.0006

SER 235 THR 236 -0.0003

THR 236 ARG 237 -0.0001

ARG 237 VAL 238 -0.0001

VAL 238 MET 239 -0.0004

MET 239 GLY 240 0.0003

GLY 240 THR 241 -0.0001

THR 241 TYR 242 -0.0002

TYR 242 GLY 243 -0.0001

GLY 243 TYR 244 0.0002

TYR 244 ALA 245 0.0003

ALA 245 ALA 246 0.0000

ALA 246 PRO 247 0.0001

PRO 247 GLU 248 -0.0002

GLU 248 TYR 249 -0.0002

TYR 249 MET 250 -0.0002

MET 250 SER 251 -0.0002

SER 251 SER 252 0.0003

SER 252 GLY 253 -0.0003

GLY 253 HIS 254 -0.0002

HIS 254 LEU 255 -0.0000

LEU 255 ASN 256 0.0003

ASN 256 ALA 257 -0.0003

ALA 257 ARG 258 -0.0003

ARG 258 SER 259 0.0004

SER 259 ASP 260 0.0001

ASP 260 VAL 261 -0.0004

VAL 261 TYR 262 0.0002

TYR 262 SER 263 0.0004

SER 263 PHE 264 -0.0002

PHE 264 GLY 265 -0.0000

GLY 265 VAL 266 -0.0001

VAL 266 LEU 267 0.0002

LEU 267 LEU 268 -0.0004

LEU 268 LEU 269 0.0002

LEU 269 GLU 270 -0.0004

GLU 270 ILE 271 -0.0003

ILE 271 LEU 272 0.0003

LEU 272 SER 273 -0.0001

SER 273 GLY 274 -0.0000

GLY 274 LYS 275 0.0001

LYS 275 ARG 276 0.0002

ARG 276 ALA 277 -0.0001

ALA 277 LEU 278 -0.0001

LEU 278 ASP 279 -0.0002

ASP 279 HIS 280 0.0004

HIS 280 ASN 281 -0.0000

ASN 281 ARG 282 -0.0002

ARG 282 PRO 283 0.0002

PRO 283 ALA 284 0.0001

ALA 284 LYS 285 -0.0002

LYS 285 GLU 286 -0.0000

GLU 286 GLU 287 0.0007

GLU 287 ASN 288 0.0002

ASN 288 LEU 289 -0.0003

LEU 289 VAL 290 0.0001

VAL 290 ASP 291 0.0003

ASP 291 TRP 292 -0.0005

TRP 292 ALA 293 -0.0003

ALA 293 ARG 294 -0.0001

ARG 294 PRO 295 0.0001

PRO 295 TYR 296 0.0004

TYR 296 LEU 297 0.0002

LEU 297 THR 298 0.0002

THR 298 SER 299 -0.0005

SER 299 LYS 300 0.0003

LYS 300 ARG 301 0.0001

ARG 301 LYS 302 -0.0002

LYS 302 VAL 303 0.0003

VAL 303 LEU 304 0.0003

LEU 304 LEU 305 -0.0000

LEU 305 ILE 306 -0.0002

ILE 306 VAL 307 0.0003

VAL 307 ASP 308 -0.0003

ASP 308 ASN 309 -0.0002

ASN 309 ARG 310 -0.0000

ARG 310 LEU 311 0.0005

LEU 311 ASP 312 0.0000

ASP 312 THR 313 -0.0002

THR 313 GLN 314 -0.0000

GLN 314 TYR 315 0.0005

TYR 315 LEU 316 -0.0001

LEU 316 PRO 317 -0.0014

PRO 317 GLU 318 0.0001

GLU 318 GLU 319 0.0007

GLU 319 ALA 320 0.0001

ALA 320 VAL 321 0.0000

VAL 321 ARG 322 0.0002

ARG 322 MET 323 -0.0022

MET 323 ALA 324 0.0003

ALA 324 SER 325 -0.0001

SER 325 VAL 326 -0.0002

VAL 326 ALA 327 0.0002

ALA 327 VAL 328 -0.0003

VAL 328 GLN 329 0.0000

GLN 329 CYS 330 -0.0002

CYS 330 LEU 331 -0.0001

LEU 331 SER 332 -0.0001

SER 332 PHE 333 -0.0001

PHE 333 GLU 334 0.0002

GLU 334 PRO 335 -0.0000

PRO 335 LYS 336 -0.0001

LYS 336 SER 337 -0.0003

SER 337 ARG 338 0.0000

ARG 338 PRO 339 0.0002

PRO 339 THR 340 -0.0001

THR 340 MET 341 -0.0002

MET 341 ASP 342 -0.0001

ASP 342 GLN 343 -0.0002

GLN 343 VAL 344 -0.0001

VAL 344 VAL 345 0.0007

VAL 345 ARG 346 0.0002

ARG 346 ALA 347 -0.0005

ALA 347 LEU 348 0.0004

LEU 348 GLN 349 0.0001

GLN 349 GLN 350 -0.0002

GLN 350 LEU 351 0.0008

LEU 351 GLN 352 0.0001

GLN 352 ASP 353 -0.0009

ASP 353 ASN 354 0.0002

ASN 354 LEU 355 -0.0007

LEU 355 GLY 356 -0.0000

GLY 356 LYS 357 0.0025

LYS 357 PRO 358 0.0004

PRO 358 SER 359 -0.0174

SER 359 GLN 360 0.0002

GLN 360 THR 361 -0.0192

THR 361 ASN 362 0.0002

ASN 362 PRO 363 0.0157

PRO 363 VAL 364 -0.0002

VAL 364 LYS 365 0.0053

LYS 365 ASP 366 -0.0002

ASP 366 THR 367 0.0072

THR 367 LYS 368 0.0000

LYS 368 LYS 369 -0.0034

LYS 369 LEU 370 0.0001

LEU 370 GLY 371 -0.0208

GLY 371 PHE 372 0.0002

PHE 372 LYS 373 -0.0150

LYS 373 THR 374 0.0002

THR 374 GLY 375 0.0404

GLY 375 THR 376 -0.0002

THR 376 THR 377 0.0190

THR 377 LYS 378 -0.0003

LYS 378 SER 379 0.0093

SER 379 SER 380 -0.0003

SER 380 GLU 381 -0.0079

GLU 381 LYS 382 -0.0001

LYS 382 ARG 383 -0.0049

ARG 383 PHE 384 -0.0004

PHE 384 THR 385 -0.0107

THR 385 GLN 386 0.0002

GLN 386 LYS 387 0.0024

LYS 387 PRO 388 0.0004

PRO 388 PHE 389 -0.0096

PHE 389 GLY 390 0.0004

GLY 390 ARG 391 0.0022

ARG 391 HIS 392 -0.0003

HIS 392 LEU 393 0.0002

LEU 393 VAL 394 0.0002

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: december 26th, 2025.

Should you encounter any unexpected behaviour, please let us know. elNémo has been hacked on november 27th. It has been moved away and runs again. **Still some additional cleaning from time to time** Sorry for the inconvenience.

*** ***

CA strain for 2604191527403651211

--- normal mode 9 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been hacked on november 27th.
It has been moved away and runs again.
Still some additional cleaning from time to time
Sorry for the inconvenience.

* *