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

* *

CA strain for 2401041731083859837

--- 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
MET 1 GLU 2 0.0001

GLU 2 PHE 3 0.0000

PHE 3 PRO 4 -0.0003

PRO 4 GLY 5 0.0003

GLY 5 LEU 6 -0.0001

LEU 6 GLY 7 -0.0017

GLY 7 SER 8 0.0001

SER 8 LEU 9 0.0000

LEU 9 GLY 10 -0.0024

GLY 10 THR 11 -0.0004

THR 11 SER 12 0.0004

SER 12 GLU 13 0.0002

GLU 13 PRO 14 -0.0001

PRO 14 LEU 15 -0.0003

LEU 15 PRO 16 -0.0016

PRO 16 GLN 17 0.0003

GLN 17 PHE 18 -0.0000

PHE 18 VAL 19 0.0002

VAL 19 ASP 20 0.0003

ASP 20 PRO 21 0.0000

PRO 21 ALA 22 0.0002

ALA 22 LEU 23 -0.0003

LEU 23 VAL 24 0.0003

VAL 24 SER 25 0.0005

SER 25 SER 26 -0.0004

SER 26 THR 27 -0.0000

THR 27 PRO 28 0.0005

PRO 28 GLU 29 -0.0000

GLU 29 SER 30 -0.0001

SER 30 GLY 31 0.0001

GLY 31 VAL 32 0.0001

VAL 32 PHE 33 0.0003

PHE 33 PHE 34 0.0002

PHE 34 PRO 35 -0.0001

PRO 35 SER 36 -0.0000

SER 36 GLY 37 0.0002

GLY 37 PRO 38 -0.0000

PRO 38 GLU 39 -0.0001

GLU 39 GLY 40 0.0000

GLY 40 LEU 41 -0.0000

LEU 41 ASP 42 0.0002

ASP 42 ALA 43 -0.0004

ALA 43 ALA 44 -0.0001

ALA 44 ALA 45 0.0005

ALA 45 SER 46 0.0015

SER 46 SER 47 0.0003

SER 47 THR 48 0.0002

THR 48 ALA 49 -0.0002

ALA 49 PRO 50 -0.0002

PRO 50 SER 51 -0.0001

SER 51 THR 52 0.0001

THR 52 ALA 53 0.0000

ALA 53 THR 54 -0.0001

THR 54 ALA 55 0.0005

ALA 55 ALA 56 0.0003

ALA 56 ALA 57 0.0002

ALA 57 ALA 58 -0.0004

ALA 58 ALA 59 0.0001

ALA 59 LEU 60 0.0000

LEU 60 ALA 61 0.0003

ALA 61 TYR 62 0.0001

TYR 62 TYR 63 -0.0001

TYR 63 ARG 64 -0.0000

ARG 64 ASP 65 -0.0000

ASP 65 ALA 66 -0.0002

ALA 66 GLU 67 0.0001

GLU 67 ALA 68 -0.0000

ALA 68 TYR 69 -0.0002

TYR 69 ARG 70 0.0004

ARG 70 HIS 71 0.0004

HIS 71 SER 72 -0.0002

SER 72 PRO 73 0.0003

PRO 73 VAL 74 -0.0000

VAL 74 PHE 75 0.0002

PHE 75 GLN 76 -0.0003

GLN 76 VAL 77 -0.0000

VAL 77 TYR 78 -0.0001

TYR 78 PRO 79 0.0002

PRO 79 LEU 80 -0.0000

LEU 80 LEU 81 -0.0001

LEU 81 ASN 82 -0.0001

ASN 82 CYS 83 0.0000

CYS 83 MET 84 0.0002

MET 84 GLU 85 -0.0003

GLU 85 GLY 86 -0.0001

GLY 86 ILE 87 0.0003

ILE 87 PRO 88 -0.0002

PRO 88 GLY 89 0.0002

GLY 89 GLY 90 -0.0002

GLY 90 SER 91 0.0004

SER 91 PRO 92 -0.0000

PRO 92 TYR 93 -0.0001

TYR 93 ALA 94 0.0004

ALA 94 GLY 95 0.0002

GLY 95 TRP 96 0.0001

TRP 96 ALA 97 -0.0002

ALA 97 TYR 98 -0.0004

TYR 98 GLY 99 0.0000

GLY 99 LYS 100 0.0000

LYS 100 THR 101 -0.0000

THR 101 GLY 102 0.0002

GLY 102 LEU 103 -0.0001

LEU 103 TYR 104 -0.0003

TYR 104 PRO 105 0.0003

PRO 105 ALA 106 -0.0003

ALA 106 SER 107 -0.0000

SER 107 THR 108 0.0003

THR 108 VAL 109 0.0006

VAL 109 CYS 110 -0.0001

CYS 110 PRO 111 0.0002

PRO 111 THR 112 0.0000

THR 112 ARG 113 0.0001

ARG 113 GLU 114 0.0001

GLU 114 ASP 115 0.0001

ASP 115 SER 116 0.0004

SER 116 PRO 117 -0.0001

PRO 117 PRO 118 -0.0006

PRO 118 GLN 119 -0.0001

GLN 119 ALA 120 0.0003

ALA 120 VAL 121 0.0000

VAL 121 GLU 122 0.0000

GLU 122 ASP 123 0.0002

ASP 123 LEU 124 0.0006

LEU 124 ASP 125 -0.0000

ASP 125 GLY 126 0.0003

GLY 126 LYS 127 -0.0000

LYS 127 GLY 128 -0.0002

GLY 128 SER 129 0.0002

SER 129 THR 130 -0.0002

THR 130 SER 131 -0.0004

SER 131 PHE 132 0.0000

PHE 132 LEU 133 0.0001

LEU 133 GLU 134 0.0000

GLU 134 THR 135 0.0001

THR 135 LEU 136 0.0002

LEU 136 LYS 137 0.0001

LYS 137 THR 138 -0.0002

THR 138 GLU 139 0.0000

GLU 139 ARG 140 0.0000

ARG 140 LEU 141 -0.0001

LEU 141 SER 142 -0.0001

SER 142 PRO 143 -0.0001

PRO 143 ASP 144 -0.0000

ASP 144 LEU 145 -0.0000

LEU 145 LEU 146 0.0002

LEU 146 THR 147 -0.0004

THR 147 LEU 148 0.0000

LEU 148 GLY 149 -0.0002

GLY 149 PRO 150 -0.0002

PRO 150 ALA 151 0.0003

ALA 151 LEU 152 0.0002

LEU 152 PRO 153 -0.0001

PRO 153 SER 154 -0.0000

SER 154 SER 155 0.0002

SER 155 LEU 156 -0.0000

LEU 156 PRO 157 -0.0001

PRO 157 VAL 158 0.0002

VAL 158 PRO 159 -0.0002

PRO 159 ASN 160 -0.0001

ASN 160 SER 161 -0.0000

SER 161 ALA 162 -0.0003

ALA 162 TYR 163 -0.0001

TYR 163 GLY 164 -0.0001

GLY 164 GLY 165 -0.0002

GLY 165 PRO 166 0.0000

PRO 166 ASP 167 0.0002

ASP 167 PHE 168 0.0001

PHE 168 SER 169 0.0001

SER 169 SER 170 0.0000

SER 170 THR 171 0.0001

THR 171 PHE 172 -0.0002

PHE 172 PHE 173 -0.0001

PHE 173 SER 174 0.0004

SER 174 PRO 175 0.0004

PRO 175 THR 176 -0.0002

THR 176 GLY 177 -0.0002

GLY 177 SER 178 -0.0000

SER 178 PRO 179 -0.0004

PRO 179 LEU 180 -0.0000

LEU 180 ASN 181 -0.0003

ASN 181 SER 182 -0.0001

SER 182 ALA 183 -0.0000

ALA 183 ALA 184 -0.0001

ALA 184 TYR 185 0.0001

TYR 185 SER 186 -0.0002

SER 186 SER 187 -0.0001

SER 187 PRO 188 -0.0006

PRO 188 LYS 189 0.0001

LYS 189 LEU 190 0.0003

LEU 190 ARG 191 -0.0001

ARG 191 GLY 192 -0.0001

GLY 192 THR 193 0.0001

THR 193 LEU 194 -0.0003

LEU 194 PRO 195 0.0001

PRO 195 LEU 196 0.0000

LEU 196 PRO 197 -0.0001

PRO 197 PRO 198 0.0001

PRO 198 CYS 199 -0.0001

CYS 199 GLU 200 -0.0001

GLU 200 ALA 201 -0.0004

ALA 201 ARG 202 0.0002

ARG 202 GLU 203 0.0001

GLU 203 CYS 204 -0.0003

CYS 204 VAL 205 0.0001

VAL 205 ASN 206 -0.0001

ASN 206 CYS 207 -0.0000

CYS 207 GLY 208 0.0003

GLY 208 ALA 209 -0.0002

ALA 209 THR 210 -0.0001

THR 210 ALA 211 -0.0001

ALA 211 THR 212 -0.0001

THR 212 PRO 213 0.0001

PRO 213 LEU 214 -0.0003

LEU 214 TRP 215 0.0002

TRP 215 ARG 216 -0.0001

ARG 216 ARG 217 0.0002

ARG 217 ASP 218 -0.0004

ASP 218 ARG 219 0.0000

ARG 219 THR 220 0.0000

THR 220 GLY 221 0.0003

GLY 221 HIS 222 -0.0001

HIS 222 TYR 223 0.0002

TYR 223 LEU 224 -0.0001

LEU 224 CYS 225 0.0001

CYS 225 ASN 226 0.0000

ASN 226 ALA 227 -0.0003

ALA 227 CYS 228 -0.0002

CYS 228 GLY 229 -0.0000

GLY 229 LEU 230 0.0001

LEU 230 TYR 231 -0.0000

TYR 231 HIS 232 0.0001

HIS 232 LYS 233 0.0003

LYS 233 MET 234 0.0002

MET 234 ASN 235 -0.0004

ASN 235 GLY 236 -0.0002

GLY 236 GLN 237 -0.0002

GLN 237 ASN 238 -0.0001

ASN 238 ARG 239 -0.0002

ARG 239 PRO 240 0.0001

PRO 240 LEU 241 0.0004

LEU 241 ILE 242 0.0003

ILE 242 ARG 243 -0.0002

ARG 243 PRO 244 0.0004

PRO 244 LYS 245 -0.0001

LYS 245 LYS 246 0.0002

LYS 246 ARG 247 -0.0014

ARG 247 LEU 248 -0.0004

LEU 248 ILE 249 0.0003

ILE 249 VAL 250 -0.0016

VAL 250 SER 251 -0.0001

SER 251 LYS 252 0.0000

LYS 252 ARG 253 0.0001

ARG 253 ALA 254 0.0001

ALA 254 GLY 255 -0.0005

GLY 255 THR 256 0.0007

THR 256 GLN 257 0.0000

GLN 257 CYS 258 -0.0002

CYS 258 THR 259 0.0003

THR 259 ASN 260 -0.0000

ASN 260 CYS 261 -0.0001

CYS 261 GLN 262 -0.0006

GLN 262 THR 263 0.0001

THR 263 THR 264 0.0003

THR 264 THR 265 -0.0001

THR 265 THR 266 0.0001

THR 266 THR 267 -0.0001

THR 267 LEU 268 -0.0003

LEU 268 TRP 269 -0.0001

TRP 269 ARG 270 -0.0000

ARG 270 ARG 271 0.0001

ARG 271 ASN 272 0.0002

ASN 272 ALA 273 -0.0002

ALA 273 SER 274 -0.0002

SER 274 GLY 275 -0.0001

GLY 275 ASP 276 0.0001

ASP 276 PRO 277 0.0000

PRO 277 VAL 278 -0.0004

VAL 278 CYS 279 -0.0000

CYS 279 ASN 280 0.0001

ASN 280 ALA 281 0.0001

ALA 281 CYS 282 -0.0002

CYS 282 GLY 283 0.0004

GLY 283 LEU 284 -0.0003

LEU 284 TYR 285 0.0000

TYR 285 TYR 286 -0.0006

TYR 286 LYS 287 0.0000

LYS 287 LEU 288 0.0000

LEU 288 HIS 289 0.0005

HIS 289 GLN 290 -0.0001

GLN 290 VAL 291 -0.0000

VAL 291 ASN 292 0.0002

ASN 292 ARG 293 -0.0003

ARG 293 PRO 294 -0.0004

PRO 294 LEU 295 -0.0000

LEU 295 THR 296 0.0001

THR 296 MET 297 0.0001

MET 297 ARG 298 0.0002

ARG 298 LYS 299 0.0003

LYS 299 ASP 300 0.0002

ASP 300 GLY 301 -0.0007

GLY 301 ILE 302 -0.0003

ILE 302 GLN 303 0.0003

GLN 303 THR 304 -0.0007

THR 304 ARG 305 -0.0003

ARG 305 ASN 306 0.0000

ASN 306 ARG 307 0.0007

ARG 307 LYS 308 -0.0002

LYS 308 ALA 309 0.0002

ALA 309 SER 310 -0.0002

SER 310 GLY 311 -0.0004

GLY 311 LYS 312 -0.0001

LYS 312 GLY 313 0.0002

GLY 313 LYS 314 0.0000

LYS 314 LYS 315 0.0003

LYS 315 LYS 316 0.0001

LYS 316 ARG 317 -0.0004

ARG 317 GLY 318 -0.0000

GLY 318 SER 319 0.0003

SER 319 SER 320 0.0001

SER 320 LEU 321 -0.0003

LEU 321 GLY 322 0.0003

GLY 322 GLY 323 -0.0000

GLY 323 THR 324 -0.0002

THR 324 GLY 325 0.0003

GLY 325 ALA 326 -0.0002

ALA 326 ALA 327 0.0000

ALA 327 GLU 328 -0.0004

GLU 328 GLY 329 0.0002

GLY 329 PRO 330 -0.0003

PRO 330 ALA 331 0.0001

ALA 331 GLY 332 0.0000

GLY 332 GLY 333 -0.0003

GLY 333 PHE 334 -0.0001

PHE 334 MET 335 0.0001

MET 335 VAL 336 0.0005

VAL 336 VAL 337 0.0000

VAL 337 ALA 338 0.0003

ALA 338 GLY 339 0.0002

GLY 339 GLY 340 -0.0004

GLY 340 SER 341 0.0000

SER 341 GLY 342 0.0000

GLY 342 SER 343 0.0003

SER 343 GLY 344 -0.0002

GLY 344 ASN 345 0.0001

ASN 345 CYS 346 -0.0000

CYS 346 GLY 347 0.0002

GLY 347 GLU 348 0.0003

GLU 348 VAL 349 -0.0000

VAL 349 ALA 350 -0.0001

ALA 350 SER 351 0.0000

SER 351 GLY 352 0.0005

GLY 352 LEU 353 -0.0001

LEU 353 THR 354 -0.0003

THR 354 LEU 355 0.0001

LEU 355 GLY 356 -0.0002

GLY 356 PRO 357 0.0000

PRO 357 PRO 358 0.0002

PRO 358 GLY 359 -0.0003

GLY 359 THR 360 0.0000

THR 360 ALA 361 0.0002

ALA 361 HIS 362 -0.0001

HIS 362 LEU 363 -0.0004

LEU 363 TYR 364 0.0000

TYR 364 GLN 365 0.0002

GLN 365 GLY 366 -0.0001

GLY 366 LEU 367 0.0003

LEU 367 GLY 368 -0.0001

GLY 368 PRO 369 0.0001

PRO 369 VAL 370 -0.0004

VAL 370 VAL 371 0.0003

VAL 371 LEU 372 0.0000

LEU 372 SER 373 -0.0004

SER 373 GLY 374 -0.0004

GLY 374 PRO 375 -0.0000

PRO 375 VAL 376 -0.0018

VAL 376 SER 377 -0.0001

SER 377 HIS 378 -0.0002

HIS 378 LEU 379 0.0007

LEU 379 MET 380 -0.0003

MET 380 PRO 381 0.0006

PRO 381 PHE 382 -0.0011

PHE 382 PRO 383 0.0002

PRO 383 GLY 384 -0.0000

GLY 384 PRO 385 0.0070

PRO 385 LEU 386 0.0001

LEU 386 LEU 387 -0.0003

LEU 387 GLY 388 -0.0183

GLY 388 SER 389 0.0000

SER 389 PRO 390 -0.0001

PRO 390 THR 391 -0.0043

THR 391 GLY 392 0.0000

GLY 392 SER 393 0.0000

SER 393 PHE 394 0.0062

PHE 394 PRO 395 0.0004

PRO 395 THR 396 -0.0001

THR 396 GLY 397 -0.0171

GLY 397 PRO 398 -0.0003

PRO 398 MET 399 0.0003

MET 399 PRO 400 -0.0004

PRO 400 PRO 401 -0.0001

PRO 401 THR 402 -0.0000

THR 402 THR 403 0.0024

THR 403 SER 404 -0.0001

SER 404 THR 405 -0.0000

THR 405 THR 406 -0.0015

THR 406 VAL 407 -0.0000

VAL 407 VAL 408 0.0001

VAL 408 ALA 409 -0.0015

ALA 409 PRO 410 0.0001

PRO 410 LEU 411 -0.0000

LEU 411 SER 412 -0.0000

SER 412 SER 413 -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).
Last modification: April 25th, 2023.

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

*** ***

CA strain for 2401041731083859837

--- normal mode 8 ---

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

* *