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

* ddd *

CA strain for 2502111056123569753

--- 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 ARG 2 -0.0003

ARG 2 VAL 3 0.0003

VAL 3 TRP 4 -0.0005

TRP 4 VAL 5 0.0000

VAL 5 GLY 6 -0.0004

GLY 6 ILE 7 0.0002

ILE 7 ASP 8 -0.0002

ASP 8 ASP 9 0.0003

ASP 9 THR 10 -0.0011

THR 10 ASP 11 -0.0003

ASP 11 SER 12 -0.0000

SER 12 SER 13 -0.0003

SER 13 ARG 14 -0.0000

ARG 14 GLY 15 0.0004

GLY 15 MET 16 -0.0001

MET 16 CYS 17 -0.0000

CYS 17 THR 19 0.0003

THR 19 TYR 20 -0.0004

TYR 20 LEU 21 0.0002

LEU 21 ALA 22 0.0001

ALA 22 VAL 23 -0.0000

VAL 23 LEU 24 0.0001

LEU 24 ALA 25 0.0015

ALA 25 MET 26 -0.0001

MET 26 GLU 27 -0.0002

GLU 27 ARG 28 0.0015

ARG 28 VAL 29 -0.0001

VAL 29 GLU 30 0.0003

GLU 30 ARG 31 -0.0004

ARG 31 GLU 32 0.0001

GLU 32 LEU 33 0.0001

LEU 33 GLY 34 -0.0001

GLY 34 LYS 35 -0.0004

LYS 35 VAL 36 0.0000

VAL 36 ILE 37 -0.0004

ILE 37 GLY 38 -0.0000

GLY 38 PHE 39 -0.0000

PHE 39 PRO 40 0.0001

PRO 40 ARG 41 0.0002

ARG 41 LEU 42 0.0001

LEU 42 ILE 43 -0.0027

ILE 43 ARG 44 -0.0002

ARG 44 LEU 45 -0.0003

LEU 45 ASN 46 -0.0021

ASN 46 PRO 47 0.0002

PRO 47 THR 48 -0.0004

THR 48 ILE 49 0.0019

ILE 49 PRO 50 0.0001

PRO 50 ARG 54 -0.0010

ARG 54 GLY 55 -0.0000

GLY 55 ASN 56 -0.0003

ASN 56 GLY 57 0.0005

GLY 57 ALA 58 0.0001

ALA 58 VAL 59 0.0001

VAL 59 SER 60 -0.0002

SER 60 PHE 61 -0.0001

PHE 61 LEU 62 -0.0000

LEU 62 VAL 63 -0.0003

VAL 63 GLU 64 -0.0003

GLU 64 VAL 65 0.0000

VAL 65 ASP 66 0.0003

ASP 66 ASP 67 0.0001

ASP 67 VAL 68 -0.0001

VAL 68 GLY 69 -0.0003

GLY 69 GLU 70 0.0002

GLU 70 LEU 71 0.0000

LEU 71 VAL 72 -0.0002

VAL 72 ASP 73 0.0002

ASP 73 VAL 74 0.0002

VAL 74 VAL 75 -0.0005

VAL 75 ASN 76 0.0001

ASN 76 GLU 77 0.0003

GLU 77 VAL 78 0.0008

VAL 78 ILE 79 0.0001

ILE 79 ILE 80 0.0002

ILE 80 GLU 81 0.0000

GLU 81 HIS 82 -0.0000

HIS 82 ALA 83 0.0000

ALA 83 MET 84 0.0002

MET 84 LEU 85 -0.0002

LEU 85 ASP 86 -0.0000

ASP 86 ASP 87 -0.0002

ASP 87 GLU 88 -0.0003

GLU 88 LYS 89 0.0002

LYS 89 THR 90 0.0003

THR 90 ASN 91 -0.0000

ASN 91 PRO 92 0.0003

PRO 92 GLY 93 -0.0004

GLY 93 ALA 94 0.0002

ALA 94 VAL 95 -0.0002

VAL 95 PHE 96 -0.0004

PHE 96 VAL 97 0.0003

VAL 97 ASP 98 0.0000

ASP 98 GLU 99 0.0000

GLU 99 GLU 100 -0.0002

GLU 100 LEU 101 0.0003

LEU 101 ALA 102 -0.0002

ALA 102 VAL 103 -0.0001

VAL 103 LYS 104 -0.0000

LYS 104 LEU 105 0.0003

LEU 105 LYS 106 -0.0003

LYS 106 PRO 107 0.0001

PRO 107 PHE 108 0.0011

PHE 108 ALA 109 -0.0000

ALA 109 ASP 110 0.0002

ASP 110 LYS 111 0.0010

LYS 111 ALA 112 0.0003

ALA 112 ILE 113 0.0000

ILE 113 LYS 114 -0.0068

LYS 114 ASP 115 0.0001

ASP 115 VAL 116 0.0001

VAL 116 LEU 117 -0.0021

LEU 117 GLN 118 0.0001

GLN 118 ILE 119 -0.0001

ILE 119 ASP 120 -0.0004

ASP 120 GLU 121 0.0002

GLU 121 ALA 122 0.0002

ALA 122 LEU 123 -0.0006

LEU 123 PHE 124 0.0001

PHE 124 VAL 125 0.0000

VAL 125 ILE 126 -0.0000

ILE 126 GLY 127 -0.0003

GLY 127 LYS 128 -0.0002

LYS 128 TYR 129 0.0002

TYR 129 PHE 130 0.0001

PHE 130 ILE 131 0.0000

ILE 131 PRO 132 0.0005

PRO 132 HIS 133 -0.0003

HIS 133 LEU 134 -0.0001

LEU 134 ARG 135 -0.0001

ARG 135 HIS 136 -0.0001

HIS 136 LYS 137 -0.0000

LYS 137 LYS 138 -0.0003

LYS 138 GLY 139 0.0002

GLY 139 ARG 140 -0.0002

ARG 140 GLY 141 0.0008

GLY 141 LEU 142 0.0002

LEU 142 ILE 143 -0.0002

ILE 143 GLY 144 0.0008

GLY 144 ALA 145 0.0000

ALA 145 LEU 146 0.0001

LEU 146 ALA 147 -0.0001

ALA 147 ALA 148 0.0002

ALA 148 VAL 149 0.0002

VAL 149 GLY 150 -0.0007

GLY 150 ALA 151 0.0000

ALA 151 GLU 152 -0.0002

GLU 152 LEU 153 0.0016

LEU 153 GLU 154 0.0001

GLU 154 ASP 155 -0.0002

ASP 155 PHE 156 -0.0010

PHE 156 THR 157 0.0001

THR 157 LEU 158 -0.0002

LEU 158 GLU 159 -0.0016

GLU 159 LEU 160 0.0002

LEU 160 ILE 161 0.0002

ILE 161 ALA 162 -0.0023

ALA 162 TYR 163 -0.0002

TYR 163 ARG 164 0.0002

ARG 164 TYR 165 0.0004

TYR 165 PRO 166 0.0003

PRO 166 GLU 167 -0.0001

GLU 167 ARG 168 0.0007

ARG 168 PHE 169 -0.0000

PHE 169 GLY 170 -0.0000

GLY 170 THR 171 -0.0003

THR 171 GLU 172 0.0003

GLU 172 ARG 173 -0.0001

ARG 173 GLU 174 -0.0023

GLU 174 TYR 175 -0.0001

TYR 175 ASP 176 -0.0002

ASP 176 GLU 177 0.0033

GLU 177 GLU 178 -0.0001

GLU 178 SER 179 0.0000

SER 179 PHE 180 -0.0004

PHE 180 PHE 181 0.0002

PHE 181 ASP 182 0.0001

ASP 182 MET 183 0.0006

MET 183 ASP 184 -0.0001

ASP 184 TYR 185 -0.0001

TYR 185 GLU 186 0.0002

GLU 186 LEU 187 0.0000

LEU 187 TYR 188 -0.0000

TYR 188 PRO 189 -0.0007

PRO 189 GLN 190 -0.0002

GLN 190 THR 191 0.0004

THR 191 PHE 192 0.0001

PHE 192 ASP 193 -0.0001

ASP 193 ASN 194 0.0001

ASN 194 VAL 195 0.0021

VAL 195 ASP 196 0.0002

ASP 196 TRP 197 0.0002

TRP 197 CYS 198 0.0005

CYS 198 ASN 199 0.0000

ASN 199 ASP 200 0.0001

ASP 200 VAL 201 0.0025

VAL 201 VAL 202 -0.0001

VAL 202 VAL 203 -0.0001

VAL 203 CYS 204 0.0078

CYS 204 ILE 205 -0.0001

ILE 205 PRO 206 -0.0002

PRO 206 ASN 207 0.0004

ASN 207 THR 208 -0.0000

THR 208 PRO 209 0.0000

PRO 209 CYS 210 -0.0003

CYS 210 PRO 211 0.0002

PRO 211 VAL 212 -0.0003

VAL 212 LEU 213 -0.0002

LEU 213 TYR 214 -0.0004

TYR 214 GLY 215 0.0001

GLY 215 ILE 216 0.0002

ILE 216 ARG 217 -0.0003

ARG 217 GLY 218 -0.0001

GLY 218 GLU 219 0.0002

GLU 219 SER 220 -0.0000

SER 220 VAL 221 -0.0002

VAL 221 GLU 222 0.0004

GLU 222 ALA 223 -0.0003

ALA 223 LEU 224 -0.0000

LEU 224 TYR 225 -0.0006

TYR 225 LYS 226 0.0002

LYS 226 ALA 227 0.0003

ALA 227 MET 228 -0.0001

MET 228 GLU 229 -0.0001

GLU 229 SER 230 0.0001

SER 230 VAL 231 -0.0008

VAL 231 LYS 232 0.0003

LYS 232 THR 233 -0.0001

THR 233 GLU 234 0.0002

GLU 234 PRO 235 -0.0002

PRO 235 VAL 236 0.0002

VAL 236 ASP 237 0.0029

ASP 237 ARG 238 0.0002

ARG 238 ARG 239 -0.0004

ARG 239 MET 240 -0.0013

MET 240 ILE 241 0.0003

ILE 241 PHE 242 0.0001

PHE 242 VAL 243 -0.0012

VAL 243 THR 244 -0.0001

THR 244 ASN 245 0.0003

ASN 245 HIS 246 -0.0003

HIS 246 ALA 247 0.0002

ALA 247 THR 248 -0.0002

THR 248 ASP 249 -0.0041

ASP 249 MET 250 0.0005

MET 250 HIS 251 -0.0000

HIS 251 LEU 252 -0.0108

LEU 252 ILE 253 -0.0004

ILE 253 GLY 254 -0.0003

GLY 254 GLU 255 -0.0052

GLU 255 GLU 256 -0.0004

GLU 256 GLU 257 0.0003

GLU 257 VAL 258 0.0014

VAL 258 HIS 259 -0.0003

HIS 259 ARG 260 -0.0000

ARG 260 LEU 261 0.0016

LEU 261 GLU 262 -0.0001

GLU 262 ASN 263 -0.0002

ASN 263 TYR 264 -0.0000

TYR 264 ARG 265 0.0002

ARG 265 SER 266 0.0001

SER 266 TYR 267 -0.0048

TYR 267 ARG 268 -0.0003

ARG 268 LEU 269 -0.0000

LEU 269 ARG 270 -0.0187

ARG 270 GLY 271 -0.0001

GLY 271 ARG 272 0.0001

ARG 272 VAL 273 0.0006

VAL 273 THR 274 -0.0001

THR 274 LEU 275 -0.0002

LEU 275 GLU 276 -0.0054

GLU 276 PRO 277 0.0003

PRO 277 TYR 278 -0.0002

TYR 278 ASP 279 0.0040

ASP 279 ILE 280 -0.0000

ILE 280 GLU 281 0.0002

GLU 281 GLY 282 -0.0000

GLY 282 GLY 283 0.0001

GLY 283 HIS 284 -0.0002

HIS 284 VAL 285 0.0002

VAL 285 PHE 286 0.0002

PHE 286 PHE 287 -0.0001

PHE 287 GLU 288 0.0005

GLU 288 ILE 289 -0.0002

ILE 289 ASP 290 0.0000

ASP 290 THR 291 -0.0079

THR 291 LYS 292 -0.0002

LYS 292 PHE 293 0.0001

PHE 293 GLY 294 -0.0023

GLY 294 SER 295 -0.0001

SER 295 VAL 296 -0.0000

VAL 296 LYS 297 0.0021

LYS 297 CYS 298 -0.0004

CYS 298 ALA 299 0.0000

ALA 299 ALA 300 0.0006

ALA 300 PHE 301 -0.0001

PHE 301 GLU 302 0.0001

GLU 302 PRO 303 0.0017

PRO 303 THR 304 -0.0002

THR 304 LYS 305 0.0002

LYS 305 GLN 306 -0.0022

GLN 306 PHE 307 -0.0000

PHE 307 ARG 308 -0.0000

ARG 308 ASN 309 0.0029

ASN 309 VAL 310 0.0001

VAL 310 ILE 311 -0.0002

ILE 311 ARG 312 -0.0082

ARG 312 LEU 313 0.0000

LEU 313 LEU 314 0.0002

LEU 314 ARG 315 -0.0052

ARG 315 LYS 316 0.0002

LYS 316 GLY 317 -0.0004

GLY 317 ASP 318 -0.0027

ASP 318 VAL 319 -0.0001

VAL 319 VAL 320 0.0001

VAL 320 GLU 321 -0.0208

GLU 321 VAL 322 -0.0002

VAL 322 TYR 323 -0.0002

TYR 323 GLY 324 -0.0041

GLY 324 SER 325 -0.0001

SER 325 MET 326 0.0002

MET 326 LYS 327 -0.0005

LYS 327 LYS 328 0.0005

LYS 328 ASP 329 0.0004

ASP 329 THR 330 -0.0005

THR 330 ILE 331 -0.0001

ILE 331 ASN 332 -0.0001

ASN 332 LEU 333 -0.0010

LEU 333 GLU 334 -0.0000

GLU 334 LYS 335 -0.0002

LYS 335 ILE 336 -0.0074

ILE 336 GLN 337 -0.0000

GLN 337 ILE 338 0.0003

ILE 338 VAL 339 -0.0049

VAL 339 GLU 340 -0.0001

GLU 340 LEU 341 0.0002

LEU 341 ALA 342 -0.1094

ALA 342 GLU 343 0.0004

GLU 343 ILE 344 0.0000

ILE 344 TRP 345 -0.0702

TRP 345 VAL 346 -0.0000

VAL 346 GLU 347 0.0002

GLU 347 LYS 348 -0.0474

LYS 348 ASN 349 -0.0000

ASN 349 PRO 350 -0.0004

PRO 350 ILE 351 -0.0049

ILE 351 CYS 352 0.0001

CYS 352 PRO 353 -0.0001

PRO 353 SER 354 0.0004

SER 354 CYS 355 -0.0001

CYS 355 GLY 356 0.0001

GLY 356 ARG 357 -0.0017

ARG 357 ARG 358 0.0003

ARG 358 MET 359 0.0001

MET 359 ASP 360 0.0034

ASP 360 SER 361 -0.0001

SER 361 ALA 362 0.0002

ALA 362 GLY 363 0.0083

GLY 363 ARG 364 -0.0002

ARG 364 GLY 365 0.0000

GLY 365 GLN 366 -0.0013

GLN 366 GLY 367 0.0000

GLY 367 PHE 368 -0.0000

PHE 368 ARG 369 -0.0093

ARG 369 CYS 370 0.0001

CYS 370 LYS 371 -0.0000

LYS 371 LYS 372 -0.0010

LYS 372 CYS 373 -0.0002

CYS 373 ARG 374 -0.0000

ARG 374 THR 375 -0.0027

THR 375 LYS 376 0.0002

LYS 376 ALA 377 -0.0000

ALA 377 ASP 378 -0.0115

ASP 378 GLU 379 -0.0001

GLU 379 LYS 380 0.0003

LYS 380 LEU 381 0.0143

LEU 381 ARG 382 0.0002

ARG 382 GLU 383 -0.0002

GLU 383 LYS 384 0.0061

LYS 384 VAL 385 0.0005

VAL 385 GLU 386 -0.0004

GLU 386 ARG 387 0.0950

ARG 387 GLU 388 -0.0001

GLU 388 LEU 389 -0.0002

LEU 389 GLN 390 -0.0056

GLN 390 PRO 391 0.0000

PRO 391 GLY 392 0.0003

GLY 392 PHE 393 -0.0095

PHE 393 TYR 394 -0.0001

TYR 394 GLU 395 0.0001

GLU 395 VAL 396 0.0006

VAL 396 PRO 397 0.0001

PRO 397 PRO 398 0.0002

PRO 398 SER 399 0.0011

SER 399 ALA 400 0.0002

ALA 400 ARG 401 0.0001

ARG 401 ARG 402 0.0041

ARG 402 HIS 403 -0.0000

HIS 403 LEU 404 0.0002

LEU 404 SER 405 0.0027

SER 405 LYS 406 -0.0001

LYS 406 PRO 407 -0.0002

PRO 407 LEU 408 0.0039

LEU 408 ILE 409 0.0000

ILE 409 ARG 410 -0.0002

ARG 410 MET 411 -0.0061

MET 411 ASN 412 0.0000

ASN 412 VAL 413 -0.0001

VAL 413 GLU 414 0.0022

GLU 414 GLY 415 0.0001

GLY 415 ARG 416 0.0000

ARG 416 HIS 417 0.0018

HIS 417 ILE 418 0.0002

ILE 418 PHE 419 0.0001

PHE 419 ARG 420 0.0092

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.

*** ddd ***

CA strain for 2502111056123569753

--- normal mode 8 ---

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

* ddd *