Should you encounter any unexpected behaviour,
please let us know.

* *

CA strain for 2503311029361266404

--- normal mode 10 ---

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
MET 1 SER 2 0.0001

SER 2 GLU 3 -0.0001

GLU 3 TYR 4 0.0006

TYR 4 ILE 5 -0.0003

ILE 5 ARG 6 0.0002

ARG 6 VAL 7 0.0009

VAL 7 THR 8 0.0001

THR 8 GLU 9 -0.0001

GLU 9 ASP 10 0.0015

ASP 10 GLU 11 0.0001

GLU 11 ASN 12 0.0000

ASN 12 ASP 13 -0.0008

ASP 13 GLU 14 0.0005

GLU 14 PRO 15 -0.0005

PRO 15 ILE 16 0.0000

ILE 16 GLU 17 0.0002

GLU 17 ILE 18 -0.0002

ILE 18 PRO 19 0.0003

PRO 19 SER 20 -0.0000

SER 20 GLU 21 0.0001

GLU 21 ASP 22 0.0002

ASP 22 ASP 23 0.0002

ASP 23 GLY 24 0.0001

GLY 24 THR 25 -0.0004

THR 25 VAL 26 0.0001

VAL 26 LEU 27 0.0004

LEU 27 LEU 28 -0.0018

LEU 28 SER 29 0.0001

SER 29 THR 30 0.0002

THR 30 VAL 31 -0.0001

VAL 31 THR 32 0.0003

THR 32 ALA 33 -0.0002

ALA 33 GLN 34 -0.0002

GLN 34 PHE 35 -0.0002

PHE 35 PRO 36 -0.0002

PRO 36 GLY 37 0.0007

GLY 37 ALA 38 0.0001

ALA 38 CYS 39 -0.0000

CYS 39 GLY 40 -0.0038

GLY 40 LEU 41 -0.0003

LEU 41 ARG 42 -0.0000

ARG 42 TYR 43 -0.0030

TYR 43 ARG 44 -0.0004

ARG 44 ASN 45 0.0001

ASN 45 PRO 46 -0.0007

PRO 46 VAL 47 0.0003

VAL 47 SER 48 0.0001

SER 48 GLN 49 0.0003

GLN 49 CYS 50 0.0003

CYS 50 MET 51 -0.0001

MET 51 ARG 52 0.0001

ARG 52 GLY 53 0.0000

GLY 53 VAL 54 0.0000

VAL 54 ARG 55 0.0011

ARG 55 LEU 56 -0.0001

LEU 56 VAL 57 0.0002

VAL 57 GLU 58 0.0002

GLU 58 GLY 59 0.0002

GLY 59 ILE 60 -0.0001

ILE 60 LEU 61 0.0002

LEU 61 HIS 62 -0.0004

HIS 62 ALA 63 0.0001

ALA 63 PRO 64 -0.0002

PRO 64 ASP 65 -0.0000

ASP 65 ALA 66 -0.0002

ALA 66 GLY 67 0.0006

GLY 67 TRP 68 0.0002

TRP 68 GLY 69 -0.0002

GLY 69 ASN 70 0.0001

ASN 70 LEU 71 0.0000

LEU 71 VAL 72 -0.0002

VAL 72 TYR 73 0.0003

TYR 73 VAL 74 -0.0002

VAL 74 VAL 75 -0.0001

VAL 75 ASN 76 0.0030

ASN 76 TYR 77 0.0003

TYR 77 PRO 78 0.0003

PRO 78 LYS 79 -0.0209

LYS 79 ASP 80 -0.0003

ASP 80 ASN 81 0.0001

ASN 81 LYS 82 -0.0043

LYS 82 ARG 83 -0.0001

ARG 83 LYS 84 -0.0002

LYS 84 MET 85 -0.0091

MET 85 ASP 86 -0.0000

ASP 86 GLU 87 0.0003

GLU 87 THR 88 -0.0102

THR 88 ASP 89 0.0000

ASP 89 ALA 90 -0.0001

ALA 90 SER 91 -0.0005

SER 91 SER 92 -0.0001

SER 92 ALA 93 -0.0002

ALA 93 VAL 94 -0.0099

VAL 94 LYS 95 0.0003

LYS 95 VAL 96 -0.0003

VAL 96 LYS 97 -0.0183

LYS 97 ARG 98 -0.0001

ARG 98 ALA 99 -0.0003

ALA 99 VAL 100 0.0014

VAL 100 GLN 101 -0.0003

GLN 101 LYS 102 0.0002

LYS 102 THR 103 -0.0004

THR 103 SER 104 0.0001

SER 104 ASP 105 0.0003

ASP 105 LEU 106 -0.0002

LEU 106 ILE 107 0.0002

ILE 107 VAL 108 0.0005

VAL 108 LEU 109 -0.0007

LEU 109 GLY 110 -0.0002

GLY 110 LEU 111 0.0001

LEU 111 PRO 112 0.0002

PRO 112 TRP 113 -0.0002

TRP 113 LYS 114 0.0003

LYS 114 THR 115 -0.0006

THR 115 THR 116 0.0001

THR 116 GLU 117 -0.0001

GLU 117 GLN 118 0.0004

GLN 118 ASP 119 0.0001

ASP 119 LEU 120 -0.0002

LEU 120 LYS 121 -0.0003

LYS 121 GLU 122 -0.0001

GLU 122 TYR 123 -0.0004

TYR 123 PHE 124 0.0001

PHE 124 SER 125 0.0002

SER 125 THR 126 0.0000

THR 126 PHE 127 -0.0012

PHE 127 GLY 128 -0.0004

GLY 128 GLU 129 0.0002

GLU 129 VAL 130 -0.0003

VAL 130 LEU 131 -0.0001

LEU 131 MET 132 0.0000

MET 132 VAL 133 -0.0006

VAL 133 GLN 134 0.0002

GLN 134 VAL 135 0.0001

VAL 135 LYS 136 -0.0009

LYS 136 LYS 137 -0.0002

LYS 137 ASP 138 0.0003

ASP 138 LEU 139 0.0006

LEU 139 LYS 140 0.0001

LYS 140 THR 141 0.0000

THR 141 GLY 142 -0.0000

GLY 142 HIS 143 0.0003

HIS 143 SER 144 0.0002

SER 144 LYS 145 0.0005

LYS 145 GLY 146 -0.0000

GLY 146 PHE 147 0.0001

PHE 147 GLY 148 -0.0005

GLY 148 PHE 149 0.0002

PHE 149 VAL 150 -0.0001

VAL 150 ARG 151 -0.0002

ARG 151 PHE 152 -0.0002

PHE 152 THR 153 -0.0001

THR 153 GLU 154 -0.0018

GLU 154 TYR 155 0.0000

TYR 155 GLU 156 -0.0001

GLU 156 THR 157 -0.0037

THR 157 GLN 158 0.0002

GLN 158 VAL 159 0.0000

VAL 159 LYS 160 -0.0011

LYS 160 VAL 161 0.0000

VAL 161 MET 162 0.0000

MET 162 SER 163 0.0008

SER 163 GLN 164 -0.0000

GLN 164 ARG 165 0.0000

ARG 165 HIS 166 0.0004

HIS 166 MET 167 -0.0001

MET 167 ILE 168 -0.0002

ILE 168 ASP 169 0.0001

ASP 169 GLY 170 0.0000

GLY 170 ARG 171 -0.0003

ARG 171 TRP 172 -0.0001

TRP 172 CYS 173 -0.0002

CYS 173 ASP 174 -0.0001

ASP 174 CYS 175 0.0002

CYS 175 LYS 176 -0.0000

LYS 176 LEU 177 -0.0001

LEU 177 PRO 178 0.0045

PRO 178 ASN 179 0.0002

ASN 179 SER 180 -0.0001

SER 180 LYS 181 0.0213

LYS 181 GLN 182 0.0006

GLN 182 SER 183 -0.0004

SER 183 GLN 184 -0.0014

GLN 184 ASP 185 -0.0001

ASP 185 GLU 186 -0.0003

GLU 186 PRO 187 0.0024

PRO 187 LEU 188 0.0004

LEU 188 ARG 189 0.0003

ARG 189 SER 190 0.0216

SER 190 ARG 191 0.0002

ARG 191 LYS 192 -0.0003

LYS 192 VAL 193 -0.0040

VAL 193 PHE 194 0.0001

PHE 194 VAL 195 0.0001

VAL 195 GLY 196 -0.0000

GLY 196 ARG 197 -0.0003

ARG 197 CYS 198 0.0001

CYS 198 THR 199 0.0007

THR 199 GLU 200 -0.0000

GLU 200 ASP 201 -0.0003

ASP 201 MET 202 0.0002

MET 202 THR 203 0.0001

THR 203 GLU 204 0.0000

GLU 204 ASP 205 -0.0000

ASP 205 GLU 206 0.0001

GLU 206 LEU 207 0.0001

LEU 207 ARG 208 0.0003

ARG 208 GLU 209 0.0001

GLU 209 PHE 210 0.0003

PHE 210 PHE 211 0.0006

PHE 211 SER 212 -0.0001

SER 212 GLN 213 0.0001

GLN 213 TYR 214 -0.0008

TYR 214 GLY 215 -0.0003

GLY 215 ASP 216 0.0001

ASP 216 VAL 217 -0.0011

VAL 217 MET 218 -0.0001

MET 218 ASP 219 0.0000

ASP 219 VAL 220 -0.0000

VAL 220 PHE 221 0.0001

PHE 221 ILE 222 -0.0001

ILE 222 PRO 223 -0.0029

PRO 223 LYS 224 -0.0001

LYS 224 PRO 225 -0.0000

PRO 225 PHE 226 0.0036

PHE 226 ARG 227 -0.0000

ARG 227 ALA 228 -0.0002

ALA 228 PHE 229 0.0001

PHE 229 ALA 230 -0.0002

ALA 230 PHE 231 0.0001

PHE 231 VAL 232 0.0000

VAL 232 THR 233 0.0000

THR 233 PHE 234 -0.0000

PHE 234 ALA 235 0.0006

ALA 235 ASP 236 -0.0002

ASP 236 ASP 237 0.0002

ASP 237 GLN 238 0.0036

GLN 238 ILE 239 0.0005

ILE 239 ALA 240 -0.0004

ALA 240 GLN 241 -0.0033

GLN 241 SER 242 -0.0002

SER 242 LEU 243 -0.0001

LEU 243 CYS 244 0.0028

CYS 244 GLY 245 0.0001

GLY 245 GLU 246 0.0001

GLU 246 ASP 247 -0.0007

ASP 247 LEU 248 0.0001

LEU 248 ILE 249 -0.0004

ILE 249 ILE 250 -0.0006

ILE 250 LYS 251 0.0001

LYS 251 GLY 252 -0.0000

GLY 252 ILE 253 0.0001

ILE 253 SER 254 -0.0002

SER 254 VAL 255 0.0005

VAL 255 HIS 256 0.0002

HIS 256 ILE 257 0.0002

ILE 257 SER 258 0.0001

SER 258 ASN 259 0.0020

ASN 259 ALA 260 0.0003

ALA 260 GLU 261 0.0001

GLU 261 PRO 262 -0.0037

PRO 262 LYS 263 -0.0001

LYS 263 HIS 264 -0.0001

HIS 264 ASN 265 0.0018

ASN 265 SER 266 0.0001

SER 266 ASN 267 0.0000

ASN 267 ARG 268 -0.0026

ARG 268 GLN 269 -0.0001

GLN 269 LEU 270 -0.0001

LEU 270 GLU 271 -0.0011

GLU 271 ARG 272 -0.0000

ARG 272 SER 273 0.0003

SER 273 GLY 274 -0.0020

GLY 274 ARG 275 -0.0002

ARG 275 PHE 276 0.0000

PHE 276 GLY 277 0.0032

GLY 277 GLY 278 0.0002

GLY 278 ASN 279 0.0000

ASN 279 PRO 280 -0.0005

PRO 280 GLY 281 -0.0000

GLY 281 GLY 282 -0.0002

GLY 282 PHE 283 -0.0001

PHE 283 GLY 284 0.0000

GLY 284 ASN 285 0.0002

ASN 285 GLN 286 -0.0004

GLN 286 GLY 287 0.0003

GLY 287 GLY 288 -0.0000

GLY 288 PHE 289 0.0005

PHE 289 GLY 290 -0.0000

GLY 290 ASN 291 0.0000

ASN 291 SER 292 -0.0004

SER 292 ARG 293 -0.0002

ARG 293 GLY 294 -0.0000

GLY 294 GLY 295 -0.0023

GLY 295 GLY 296 0.0001

GLY 296 ALA 297 -0.0001

ALA 297 GLY 298 -0.0021

GLY 298 LEU 299 0.0003

LEU 299 GLY 300 0.0002

GLY 300 ASN 301 -0.0014

ASN 301 ASN 302 0.0000

ASN 302 GLN 303 -0.0004

GLN 303 GLY 304 -0.0012

GLY 304 SER 305 0.0002

SER 305 ASN 306 0.0003

ASN 306 MET 307 0.0011

MET 307 GLY 308 -0.0000

GLY 308 GLY 309 -0.0003

GLY 309 GLY 310 -0.0026

GLY 310 MET 311 0.0002

MET 311 ASN 312 -0.0000

ASN 312 PHE 313 0.0012

PHE 313 GLY 314 -0.0003

GLY 314 ALA 315 -0.0003

ALA 315 PHE 316 0.0006

PHE 316 SER 317 0.0002

SER 317 ILE 318 -0.0003

ILE 318 ASN 319 0.0007

ASN 319 PRO 320 -0.0002

PRO 320 ALA 321 -0.0003

ALA 321 MET 322 -0.0000

MET 322 MET 323 0.0001

MET 323 ALA 324 0.0000

ALA 324 ALA 325 0.0009

ALA 325 ALA 326 0.0003

ALA 326 GLN 327 0.0002

GLN 327 ALA 328 -0.0004

ALA 328 ALA 329 0.0001

ALA 329 LEU 330 0.0003

LEU 330 GLN 331 -0.0001

GLN 331 SER 332 0.0001

SER 332 SER 333 0.0002

SER 333 TRP 334 -0.0001

TRP 334 GLY 335 -0.0000

GLY 335 MET 336 0.0003

MET 336 MET 337 0.0015

MET 337 GLY 338 0.0002

GLY 338 MET 339 -0.0000

MET 339 LEU 340 0.0005

LEU 340 ALA 341 -0.0000

ALA 341 SER 342 -0.0001

SER 342 GLN 343 -0.0000

GLN 343 GLN 344 -0.0001

GLN 344 ASN 345 -0.0001

ASN 345 GLN 346 -0.0000

GLN 346 SER 347 0.0003

SER 347 GLY 348 0.0001

GLY 348 PRO 349 0.0001

PRO 349 SER 350 -0.0000

SER 350 GLY 351 0.0001

GLY 351 ASN 352 0.0001

ASN 352 ASN 353 -0.0001

ASN 353 GLN 354 -0.0001

GLN 354 ASN 355 0.0006

ASN 355 GLN 356 0.0003

GLN 356 GLY 357 -0.0002

GLY 357 ASN 358 -0.0010

ASN 358 MET 359 0.0001

MET 359 GLN 360 0.0002

GLN 360 ARG 361 0.0001

ARG 361 GLU 362 -0.0001

GLU 362 PRO 363 -0.0001

PRO 363 ASN 364 0.0002

ASN 364 GLN 365 0.0000

GLN 365 ALA 366 0.0002

ALA 366 PHE 367 0.0008

PHE 367 GLY 368 0.0002

GLY 368 SER 369 -0.0000

SER 369 GLY 370 0.0015

GLY 370 ASN 371 0.0004

ASN 371 ASN 372 0.0001

ASN 372 SER 373 0.0004

SER 373 TYR 374 0.0002

TYR 374 SER 375 0.0002

SER 375 GLY 376 -0.0003

GLY 376 SER 377 -0.0000

SER 377 ASN 378 -0.0001

ASN 378 SER 379 0.0007

SER 379 GLY 380 -0.0002

GLY 380 ALA 381 0.0000

ALA 381 ALA 382 0.0017

ALA 382 ILE 383 0.0003

ILE 383 GLY 384 -0.0001

GLY 384 TRP 385 0.0026

TRP 385 GLY 386 0.0001

GLY 386 SER 387 0.0001

SER 387 ALA 388 0.0006

ALA 388 SER 389 0.0001

SER 389 ASN 390 0.0005

ASN 390 ALA 391 0.0033

ALA 391 GLY 392 -0.0000

GLY 392 SER 393 0.0005

SER 393 GLY 394 -0.0001

GLY 394 SER 395 0.0002

SER 395 GLY 396 0.0000

GLY 396 PHE 397 0.0001

PHE 397 ASN 398 0.0001

ASN 398 GLY 399 0.0001

GLY 399 GLY 400 -0.0004

GLY 400 PHE 401 0.0005

PHE 401 GLY 402 -0.0004

GLY 402 SER 403 -0.0016

SER 403 SER 404 -0.0000

SER 404 MET 405 -0.0001

MET 405 ASP 406 -0.0031

ASP 406 SER 407 -0.0000

SER 407 LYS 408 -0.0000

LYS 408 SER 409 -0.0001

SER 409 SER 410 0.0001

SER 410 GLY 411 -0.0002

GLY 411 TRP 412 0.0003

TRP 412 GLY 413 -0.0002

GLY 413 MET 414 0.0003

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).
Last modification: April 8th, 2025.

Should you encounter any unexpected behaviour, please let us know.

*** ***

CA strain for 2503311029361266404

--- normal mode 10 ---

Should you encounter any unexpected behaviour,
please let us know.

* *