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

* 6ACC *

CA strain for 240228060327926732

--- normal mode 15 ---

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
ARG 1 CYS 2 -0.0004

CYS 2 THR 3 0.0000

THR 3 THR 4 0.0004

THR 4 PHE 5 0.0002

PHE 5 ASP 6 -0.0000

ASP 6 ASP 7 0.0001

ASP 7 VAL 8 -0.0002

VAL 8 GLN 9 -0.0000

GLN 9 ALA 10 -0.0028

ALA 10 PRO 11 0.0002

PRO 11 ASN 12 0.0002

ASN 12 TYR 13 -0.0001

TYR 13 THR 14 0.0002

THR 14 GLN 15 -0.0003

GLN 15 HIS 16 -0.0037

HIS 16 THR 17 0.0002

THR 17 SER 18 0.0003

SER 18 SER 19 -0.0034

SER 19 MET 20 0.0003

MET 20 ARG 21 -0.0000

ARG 21 GLY 22 -0.0029

GLY 22 VAL 23 0.0004

VAL 23 TYR 24 -0.0001

TYR 24 TYR 25 -0.0028

TYR 25 PRO 26 0.0001

PRO 26 ASP 27 -0.0000

ASP 27 GLU 28 -0.0037

GLU 28 ILE 29 0.0003

ILE 29 PHE 30 -0.0005

PHE 30 ARG 31 0.0036

ARG 31 SER 32 0.0001

SER 32 ASP 33 0.0002

ASP 33 THR 34 0.0054

THR 34 LEU 35 -0.0000

LEU 35 TYR 36 0.0002

TYR 36 LEU 37 -0.0079

LEU 37 THR 38 0.0004

THR 38 GLN 39 0.0001

GLN 39 ASP 40 -0.0204

ASP 40 LEU 41 -0.0001

LEU 41 PHE 42 0.0001

PHE 42 LEU 43 0.0030

LEU 43 PRO 44 -0.0001

PRO 44 PHE 45 -0.0003

PHE 45 TYR 46 -0.0017

TYR 46 SER 47 0.0002

SER 47 ASN 48 -0.0001

ASN 48 VAL 49 -0.0020

VAL 49 THR 50 0.0000

THR 50 GLY 51 0.0001

GLY 51 PHE 52 -0.0016

PHE 52 HIS 53 -0.0004

HIS 53 THR 54 -0.0003

THR 54 ILE 55 -0.0003

ILE 55 ASN 56 0.0001

ASN 56 HIS 57 0.0002

HIS 57 THR 58 -0.0001

THR 58 PHE 59 0.0000

PHE 59 GLY 60 -0.0003

GLY 60 ASN 61 0.0017

ASN 61 PRO 62 0.0003

PRO 62 VAL 63 -0.0000

VAL 63 ILE 64 -0.0044

ILE 64 PRO 65 -0.0000

PRO 65 PHE 66 0.0000

PHE 66 LYS 67 -0.0054

LYS 67 ASP 68 -0.0005

ASP 68 GLY 69 -0.0001

GLY 69 ILE 70 0.0021

ILE 70 TYR 71 -0.0003

TYR 71 PHE 72 -0.0002

PHE 72 ALA 73 -0.0012

ALA 73 ALA 74 0.0003

ALA 74 THR 75 0.0001

THR 75 GLU 76 0.0012

GLU 76 LYS 77 0.0001

LYS 77 SER 78 0.0003

SER 78 ASN 79 -0.0013

ASN 79 VAL 80 -0.0001

VAL 80 VAL 81 -0.0000

VAL 81 ARG 82 -0.0003

ARG 82 GLY 83 0.0002

GLY 83 TRP 84 -0.0005

TRP 84 VAL 85 0.0029

VAL 85 PHE 86 0.0002

PHE 86 GLY 87 0.0003

GLY 87 SER 88 0.0025

SER 88 THR 89 0.0003

THR 89 MET 90 0.0001

MET 90 ASN 91 -0.0029

ASN 91 ASN 92 -0.0001

ASN 92 LYS 93 -0.0000

LYS 93 SER 94 -0.0012

SER 94 GLN 95 0.0004

GLN 95 SER 96 -0.0002

SER 96 VAL 97 0.0021

VAL 97 ILE 98 -0.0000

ILE 98 ILE 99 0.0003

ILE 99 ILE 100 -0.0018

ILE 100 ASN 101 0.0002

ASN 101 ASN 102 0.0003

ASN 102 SER 103 0.0004

SER 103 THR 104 -0.0003

THR 104 ASN 105 -0.0000

ASN 105 VAL 106 -0.0011

VAL 106 VAL 107 -0.0001

VAL 107 ILE 108 0.0000

ILE 108 ARG 109 0.0022

ARG 109 ALA 110 -0.0004

ALA 110 CYS 111 0.0001

CYS 111 ASN 112 0.0014

ASN 112 PHE 113 -0.0000

PHE 113 GLU 114 0.0000

GLU 114 LEU 115 -0.0003

LEU 115 CYS 116 0.0004

CYS 116 ASP 117 -0.0001

ASP 117 ASN 118 0.0011

ASN 118 PRO 119 -0.0003

PRO 119 PHE 120 0.0001

PHE 120 PHE 121 0.0009

PHE 121 ALA 122 -0.0003

ALA 122 VAL 123 -0.0002

VAL 123 SER 124 -0.0014

SER 124 LYS 125 0.0004

LYS 125 PRO 126 0.0001

PRO 126 MET 127 0.0001

MET 127 GLY 128 0.0001

GLY 128 THR 129 0.0003

THR 129 GLN 130 -0.0006

GLN 130 THR 131 0.0005

THR 131 HIS 132 0.0001

HIS 132 THR 133 -0.0010

THR 133 MET 134 0.0000

MET 134 ILE 135 0.0003

ILE 135 PHE 136 0.0007

PHE 136 ASP 137 0.0000

ASP 137 ASN 138 -0.0002

ASN 138 ALA 139 0.0004

ALA 139 PHE 140 -0.0001

PHE 140 ASN 141 0.0001

ASN 141 CYS 142 0.0005

CYS 142 THR 143 -0.0003

THR 143 PHE 144 -0.0003

PHE 144 GLU 145 0.0005

GLU 145 TYR 146 0.0000

TYR 146 ILE 147 -0.0001

ILE 147 SER 148 -0.0000

SER 148 ASP 149 0.0000

ASP 149 ALA 150 0.0003

ALA 150 PHE 151 -0.0007

PHE 151 SER 152 0.0000

SER 152 LEU 153 0.0003

LEU 153 ASP 154 -0.0005

ASP 154 VAL 155 -0.0003

VAL 155 SER 156 -0.0000

SER 156 GLU 157 -0.0005

GLU 157 LYS 158 0.0004

LYS 158 SER 159 -0.0002

SER 159 GLY 160 0.0038

GLY 160 ASN 161 0.0003

ASN 161 PHE 162 0.0002

PHE 162 LYS 163 -0.0005

LYS 163 HIS 164 0.0001

HIS 164 LEU 165 0.0003

LEU 165 ARG 166 -0.0026

ARG 166 GLU 167 0.0001

GLU 167 PHE 168 -0.0001

PHE 168 VAL 169 -0.0037

VAL 169 PHE 170 0.0001

PHE 170 LYS 171 0.0001

LYS 171 ASN 172 0.0010

ASN 172 LYS 173 0.0001

LYS 173 ASP 174 -0.0001

ASP 174 GLY 175 -0.0092

GLY 175 PHE 176 -0.0000

PHE 176 LEU 177 -0.0001

LEU 177 TYR 178 0.0016

TYR 178 VAL 179 -0.0001

VAL 179 TYR 180 0.0001

TYR 180 LYS 181 -0.0032

LYS 181 GLY 182 0.0003

GLY 182 TYR 183 -0.0002

TYR 183 GLN 184 -0.0025

GLN 184 PRO 185 0.0001

PRO 185 ILE 186 -0.0003

ILE 186 ASP 187 -0.0018

ASP 187 VAL 188 -0.0001

VAL 188 VAL 189 -0.0003

VAL 189 ARG 190 -0.0022

ARG 190 ASP 191 0.0003

ASP 191 LEU 192 0.0000

LEU 192 PRO 193 -0.0004

PRO 193 SER 194 0.0001

SER 194 GLY 195 0.0001

GLY 195 PHE 196 -0.0001

PHE 196 ASN 197 -0.0001

ASN 197 THR 198 -0.0000

THR 198 LEU 199 0.0048

LEU 199 LYS 200 -0.0002

LYS 200 PRO 201 -0.0001

PRO 201 ILE 202 0.0037

ILE 202 PHE 203 0.0001

PHE 203 LYS 204 0.0001

LYS 204 LEU 205 0.0079

LEU 205 PRO 206 -0.0004

PRO 206 LEU 207 -0.0000

LEU 207 GLY 208 0.0022

GLY 208 ILE 209 -0.0001

ILE 209 ASN 210 -0.0000

ASN 210 ILE 211 -0.0006

ILE 211 THR 212 0.0000

THR 212 ASN 213 0.0004

ASN 213 PHE 214 0.0015

PHE 214 ARG 215 -0.0001

ARG 215 ALA 216 -0.0001

ALA 216 ILE 217 -0.0041

ILE 217 LEU 218 -0.0001

LEU 218 THR 219 0.0003

THR 219 ALA 220 -0.0006

ALA 220 PHE 221 -0.0002

PHE 221 SER 222 -0.0001

SER 222 ILE 223 -0.0001

ILE 223 TRP 224 -0.0004

TRP 224 GLY 225 0.0004

GLY 225 THR 226 0.0022

THR 226 SER 227 0.0003

SER 227 ALA 228 -0.0004

ALA 228 ALA 229 -0.0008

ALA 229 ALA 230 0.0002

ALA 230 TYR 231 0.0005

TYR 231 PHE 232 -0.0024

PHE 232 VAL 233 0.0002

VAL 233 GLY 234 -0.0003

GLY 234 TYR 235 0.0009

TYR 235 LEU 236 -0.0004

LEU 236 LYS 237 0.0004

LYS 237 PRO 238 -0.0085

PRO 238 THR 239 0.0001

THR 239 THR 240 0.0001

THR 240 PHE 241 -0.0014

PHE 241 MET 242 -0.0001

MET 242 LEU 243 -0.0002

LEU 243 LYS 244 -0.0064

LYS 244 TYR 245 0.0002

TYR 245 ASP 246 0.0002

ASP 246 GLU 247 0.0005

GLU 247 ASN 248 0.0003

ASN 248 GLY 249 -0.0001

GLY 249 THR 250 -0.0048

THR 250 ILE 251 0.0004

ILE 251 THR 252 0.0000

THR 252 ASP 253 -0.0048

ASP 253 ALA 254 0.0001

ALA 254 VAL 255 0.0002

VAL 255 ASP 256 -0.0020

ASP 256 CYS 257 0.0002

CYS 257 SER 258 0.0001

SER 258 GLN 259 0.0027

GLN 259 ASN 260 0.0000

ASN 260 PRO 261 0.0001

PRO 261 LEU 262 -0.0107

LEU 262 ALA 263 0.0000

ALA 263 GLU 264 0.0001

GLU 264 LEU 265 -0.0153

LEU 265 LYS 266 -0.0001

LYS 266 CYS 267 0.0001

CYS 267 SER 268 -0.0058

SER 268 VAL 269 0.0002

VAL 269 LYS 270 -0.0001

LYS 270 SER 271 -0.0196

SER 271 PHE 272 -0.0002

PHE 272 GLU 273 0.0004

GLU 273 ILE 274 0.0303

ILE 274 ASP 275 -0.0003

ASP 275 LYS 276 0.0002

LYS 276 GLY 277 0.0005

GLY 277 ILE 278 -0.0003

ILE 278 TYR 279 0.0000

TYR 279 GLN 280 0.0535

GLN 280 THR 281 -0.0001

THR 281 SER 282 -0.0001

SER 282 ASN 283 0.0146

ASN 283 PHE 284 0.0002

PHE 284 ARG 285 -0.0000

ARG 285 VAL 286 -0.0159

VAL 286 VAL 287 0.0001

VAL 287 PRO 288 -0.0003

PRO 288 SER 289 -0.0207

SER 289 GLY 290 0.0007

GLY 290 ASP 291 0.0001

ASP 291 VAL 292 0.0911

VAL 292 VAL 293 -0.0002

VAL 293 ARG 294 0.0003

ARG 294 PHE 295 0.0480

PHE 295 PRO 296 0.0001

PRO 296 ASN 297 -0.0002

ASN 297 ILE 298 -0.0257

ILE 298 THR 299 0.0001

THR 299 ASN 300 -0.0000

ASN 300 LEU 301 -0.0025

LEU 301 CYS 302 0.0001

CYS 302 PRO 303 -0.0003

PRO 303 PHE 304 0.0099

PHE 304 GLY 305 0.0001

GLY 305 GLU 306 0.0000

GLU 306 VAL 307 -0.0019

VAL 307 PHE 308 0.0001

PHE 308 ASN 309 -0.0000

ASN 309 ALA 310 -0.0020

ALA 310 THR 311 -0.0003

THR 311 LYS 312 -0.0001

LYS 312 PHE 313 -0.0014

PHE 313 PRO 314 -0.0002

PRO 314 SER 315 0.0001

SER 315 VAL 316 -0.0061

VAL 316 TYR 317 -0.0002

TYR 317 ALA 318 -0.0001

ALA 318 TRP 319 0.0026

TRP 319 GLU 320 0.0001

GLU 320 ARG 321 -0.0001

ARG 321 LYS 322 0.0138

LYS 322 LYS 323 0.0002

LYS 323 ILE 324 0.0001

ILE 324 SER 325 0.0486

SER 325 ASN 326 -0.0003

ASN 326 CYS 327 -0.0002

CYS 327 VAL 328 -0.0246

VAL 328 ALA 329 -0.0001

ALA 329 ASP 330 -0.0003

ASP 330 TYR 331 0.0023

TYR 331 SER 332 -0.0001

SER 332 VAL 333 0.0001

VAL 333 LEU 334 -0.0041

LEU 334 TYR 335 0.0002

TYR 335 ASN 336 -0.0003

ASN 336 SER 337 -0.0093

SER 337 THR 338 -0.0001

THR 338 PHE 339 0.0003

PHE 339 PHE 340 0.0033

PHE 340 SER 341 -0.0000

SER 341 THR 342 0.0001

THR 342 PHE 343 -0.0123

PHE 343 LYS 344 -0.0000

LYS 344 CYS 345 0.0002

CYS 345 TYR 346 0.0066

TYR 346 GLY 347 -0.0000

GLY 347 VAL 348 -0.0003

VAL 348 SER 349 0.0160

SER 349 ALA 350 0.0003

ALA 350 THR 351 -0.0004

THR 351 LYS 352 -0.0130

LYS 352 LEU 353 0.0004

LEU 353 ASN 354 0.0001

ASN 354 ASP 355 -0.0064

ASP 355 LEU 356 0.0003

LEU 356 CYS 357 -0.0002

CYS 357 PHE 358 0.0449

PHE 358 SER 359 -0.0001

SER 359 ASN 360 -0.0001

ASN 360 VAL 361 0.0025

VAL 361 TYR 362 0.0000

TYR 362 ALA 363 -0.0000

ALA 363 ASP 364 0.0062

ASP 364 SER 365 -0.0003

SER 365 PHE 366 0.0001

PHE 366 VAL 367 0.0049

VAL 367 VAL 368 -0.0003

VAL 368 LYS 369 0.0002

LYS 369 GLY 370 0.0020

GLY 370 ASP 371 0.0003

ASP 371 ASP 372 0.0000

ASP 372 VAL 373 -0.0058

VAL 373 ARG 374 -0.0004

ARG 374 GLN 375 0.0000

GLN 375 ILE 376 -0.0013

ILE 376 ALA 377 0.0000

ALA 377 PRO 378 0.0000

PRO 378 GLY 379 -0.0005

GLY 379 GLN 380 -0.0000

GLN 380 THR 381 0.0001

THR 381 GLY 382 0.0006

GLY 382 VAL 383 -0.0002

VAL 383 ILE 384 0.0004

ILE 384 ALA 385 0.0001

ALA 385 ASP 386 -0.0000

ASP 386 TYR 387 0.0002

TYR 387 ASN 388 0.0022

ASN 388 TYR 389 -0.0001

TYR 389 LYS 390 0.0001

LYS 390 LEU 391 -0.0037

LEU 391 PRO 392 0.0003

PRO 392 ASP 393 -0.0002

ASP 393 ASP 394 0.0002

ASP 394 PHE 395 0.0003

PHE 395 MET 396 -0.0001

MET 396 GLY 397 -0.0041

GLY 397 CYS 398 -0.0003

CYS 398 VAL 399 0.0002

VAL 399 LEU 400 0.0042

LEU 400 ALA 401 0.0003

ALA 401 TRP 402 -0.0002

TRP 402 ASN 403 -0.0019

ASN 403 THR 404 0.0001

THR 404 ARG 405 0.0002

ARG 405 ASN 406 -0.0016

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.

*** 6ACC ***

CA strain for 240228060327926732

--- normal mode 15 ---

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

* 6ACC *