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

* 6DNP *

CA strain for 240228060517928664

--- 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
THR 1 ASP 2 -0.0001

ASP 2 ARG 3 -0.0003

ARG 3 VAL 4 0.0003

VAL 4 SER 5 -0.0001

SER 5 VAL 6 -0.0000

VAL 6 GLY 7 0.0014

GLY 7 ASN 8 -0.0000

ASN 8 LEU 9 0.0001

LEU 9 ARG 10 0.0010

ARG 10 ILE 11 -0.0001

ILE 11 ALA 12 0.0003

ALA 12 ARG 13 -0.0018

ARG 13 VAL 14 0.0000

VAL 14 LEU 15 0.0001

LEU 15 TYR 16 -0.0012

TYR 16 ASP 17 -0.0002

ASP 17 PHE 18 0.0003

PHE 18 VAL 19 0.0003

VAL 19 ASN 20 0.0004

ASN 20 ASN 21 -0.0004

ASN 21 GLU 22 0.0009

GLU 22 ALA 23 -0.0001

ALA 23 LEU 24 -0.0004

LEU 24 PRO 25 0.0009

PRO 25 GLY 26 -0.0001

GLY 26 THR 27 -0.0003

THR 27 ASP 28 -0.0011

ASP 28 ILE 29 -0.0003

ILE 29 ASP 30 0.0003

ASP 30 PRO 31 -0.0010

PRO 31 ASP 32 -0.0000

ASP 32 SER 33 0.0002

SER 33 PHE 34 -0.0020

PHE 34 TRP 35 0.0003

TRP 35 ALA 36 0.0001

ALA 36 GLY 37 -0.0003

GLY 37 VAL 38 0.0002

VAL 38 ASP 39 -0.0001

ASP 39 LYS 40 0.0018

LYS 40 VAL 41 0.0002

VAL 41 VAL 42 0.0003

VAL 42 ALA 43 -0.0049

ALA 43 ASP 44 -0.0004

ASP 44 LEU 45 0.0001

LEU 45 THR 46 -0.0056

THR 46 PRO 47 0.0001

PRO 47 GLN 48 -0.0003

GLN 48 GLN 48 -0.0061

GLN 48 ASN 49 -0.0020

ASN 49 GLN 50 0.0001

GLN 50 ALA 51 -0.0001

ALA 51 LEU 52 -0.0049

LEU 52 LEU 53 0.0003

LEU 53 ASN 54 0.0003

ASN 54 ALA 55 -0.0136

ALA 55 ARG 56 -0.0001

ARG 56 ASP 57 -0.0003

ASP 57 GLU 58 -0.0034

GLU 58 LEU 59 -0.0003

LEU 59 GLN 60 -0.0001

GLN 60 ALA 61 0.0288

ALA 61 GLN 62 0.0002

GLN 62 ILE 63 0.0002

ILE 63 ASP 64 0.0083

ASP 64 LYS 65 0.0003

LYS 65 TRP 66 -0.0002

TRP 66 HIS 67 0.0034

HIS 67 ARG 68 0.0003

ARG 68 ARG 69 0.0000

ARG 69 ARG 70 0.0077

ARG 70 VAL 71 0.0003

VAL 71 ILE 72 -0.0002

ILE 72 GLU 73 0.0055

GLU 73 PRO 74 0.0002

PRO 74 ILE 75 -0.0003

ILE 75 ASP 76 0.0026

ASP 76 MET 77 -0.0001

MET 77 ASP 78 -0.0001

ASP 78 ALA 79 0.0009

ALA 79 TYR 80 -0.0000

TYR 80 ARG 81 -0.0000

ARG 81 ARG 81 -0.0465

ARG 81 GLN 82 0.0049

GLN 82 PHE 83 -0.0001

PHE 83 LEU 84 0.0002

LEU 84 THR 85 0.0055

THR 85 GLU 86 0.0004

GLU 86 ILE 87 0.0001

ILE 87 GLY 88 0.0041

GLY 88 TYR 89 -0.0003

TYR 89 LEU 90 -0.0001

LEU 90 LEU 91 0.0103

LEU 91 PRO 92 -0.0006

PRO 92 GLU 93 0.0001

GLU 93 PRO 94 -0.0112

PRO 94 ASP 95 -0.0002

ASP 95 ASP 96 0.0002

ASP 96 PHE 97 0.0625

PHE 97 THR 98 0.0003

THR 98 ILE 99 -0.0003

ILE 99 THR 100 0.0616

THR 100 THR 101 0.0002

THR 101 SER 102 0.0001

SER 102 GLY 103 0.0874

GLY 103 VAL 104 0.0002

VAL 104 ASP 105 0.0000

ASP 105 ALA 106 -0.0126

ALA 106 GLU 107 0.0003

GLU 107 ILE 108 0.0004

ILE 108 THR 109 0.0188

THR 109 THR 110 0.0001

THR 110 THR 111 0.0003

THR 111 ALA 112 -0.0082

ALA 112 GLY 113 -0.0001

GLY 113 PRO 114 0.0002

PRO 114 GLN 115 -0.0007

GLN 115 LEU 116 -0.0001

LEU 116 VAL 117 -0.0004

VAL 117 VAL 118 0.0164

VAL 118 PRO 119 -0.0000

PRO 119 VAL 120 -0.0000

VAL 120 LEU 121 0.0063

LEU 121 ASN 122 0.0003

ASN 122 ALA 123 -0.0005

ALA 123 ARG 124 -0.0039

ARG 124 PHE 125 0.0002

PHE 125 ALA 126 0.0001

ALA 126 LEU 127 -0.0118

LEU 127 ASN 128 -0.0003

ASN 128 ALA 129 -0.0002

ALA 129 ALA 130 -0.0027

ALA 130 ASN 131 0.0003

ASN 131 ALA 132 -0.0002

ALA 132 ARG 133 0.0072

ARG 133 TRP 134 0.0001

TRP 134 GLY 135 0.0001

GLY 135 SER 136 -0.0189

SER 136 LEU 137 -0.0000

LEU 137 TYR 138 0.0002

TYR 138 ASP 139 -0.0001

ASP 139 ALA 140 0.0002

ALA 140 LEU 141 -0.0000

LEU 141 TYR 142 -0.0037

TYR 142 GLY 143 -0.0001

GLY 143 THR 144 -0.0003

THR 144 ASP 145 0.0013

ASP 145 VAL 146 -0.0004

VAL 146 ILE 147 -0.0002

ILE 147 PRO 148 -0.0033

PRO 148 GLU 149 -0.0001

GLU 149 THR 150 0.0002

THR 150 ASP 151 -0.0016

ASP 151 GLY 152 0.0001

GLY 152 ALA 153 -0.0000

ALA 153 GLU 154 -0.0022

GLU 154 LYS 155 0.0003

LYS 155 GLY 156 -0.0002

GLY 156 PRO 157 -0.0014

PRO 157 THR 158 -0.0000

THR 158 TYR 159 0.0000

TYR 159 ASN 160 0.0016

ASN 160 LYS 161 -0.0003

LYS 161 VAL 162 0.0002

VAL 162 ARG 163 0.0006

ARG 163 GLY 164 -0.0000

GLY 164 ASP 165 0.0002

ASP 165 LYS 166 0.0024

LYS 166 VAL 167 0.0001

VAL 167 ILE 168 -0.0000

ILE 168 ALA 169 0.0015

ALA 169 TYR 170 -0.0002

TYR 170 ALA 171 -0.0002

ALA 171 ARG 172 0.0025

ARG 172 LYS 173 -0.0001

LYS 173 PHE 174 0.0001

PHE 174 LEU 175 -0.0014

LEU 175 ASP 176 -0.0004

ASP 176 ASP 177 -0.0002

ASP 177 SER 178 -0.0113

SER 178 VAL 179 -0.0003

VAL 179 PRO 180 -0.0002

PRO 180 LEU 181 -0.0017

LEU 181 SER 182 0.0004

SER 182 SER 183 0.0002

SER 183 GLY 184 -0.0006

GLY 184 SER 185 0.0001

SER 185 PHE 186 -0.0003

PHE 186 GLY 187 -0.0005

GLY 187 ASP 188 0.0002

ASP 188 ALA 189 0.0001

ALA 189 THR 190 0.0006

THR 190 GLY 191 0.0001

GLY 191 PHE 192 -0.0002

PHE 192 THR 193 -0.0005

THR 193 VAL 194 -0.0003

VAL 194 GLN 195 0.0001

GLN 195 ASP 196 -0.0033

ASP 196 GLY 197 0.0001

GLY 197 GLN 198 0.0001

GLN 198 LEU 199 -0.0032

LEU 199 VAL 200 -0.0002

VAL 200 VAL 201 0.0001

VAL 201 ALA 202 -0.0017

ALA 202 LEU 203 -0.0000

LEU 203 PRO 204 0.0005

PRO 204 ASP 205 -0.0002

ASP 205 LYS 206 0.0002

LYS 206 SER 207 -0.0002

SER 207 THR 208 0.0003

THR 208 GLY 209 0.0001

GLY 209 LEU 210 0.0004

LEU 210 ALA 211 0.0029

ALA 211 ASN 212 -0.0005

ASN 212 PRO 213 0.0003

PRO 213 GLY 214 0.0036

GLY 214 GLN 215 0.0002

GLN 215 PHE 216 0.0002

PHE 216 ALA 217 -0.0159

ALA 217 GLY 218 -0.0001

GLY 218 TYR 219 -0.0001

TYR 219 THR 220 -0.0037

THR 220 GLY 221 -0.0003

GLY 221 ALA 222 0.0002

ALA 222 ALA 223 -0.0026

ALA 223 GLU 224 0.0002

GLU 224 SER 225 0.0000

SER 225 PRO 226 -0.0041

PRO 226 THR 227 0.0002

THR 227 SER 228 -0.0000

SER 228 VAL 229 0.0039

VAL 229 LEU 230 0.0003

LEU 230 LEU 231 -0.0001

LEU 231 ILE 232 0.0079

ILE 232 ASN 233 0.0000

ASN 233 HIS 234 -0.0000

HIS 234 GLY 235 -0.0409

GLY 235 LEU 236 0.0002

LEU 236 HIS 237 -0.0002

HIS 237 ILE 238 -0.0206

ILE 238 GLU 239 0.0000

GLU 239 ILE 240 0.0002

ILE 240 LEU 241 -0.0020

LEU 241 ILE 242 0.0001

ILE 242 ASP 243 -0.0004

ASP 243 PRO 244 0.0065

PRO 244 GLU 245 0.0002

GLU 245 SER 246 -0.0000

SER 246 GLN 247 0.0101

GLN 247 VAL 248 0.0004

VAL 248 GLY 249 -0.0003

GLY 249 THR 250 -0.0018

THR 250 THR 251 -0.0001

THR 251 ASP 252 0.0005

ASP 252 ARG 253 0.0006

ARG 253 ALA 254 -0.0000

ALA 254 GLY 255 -0.0003

GLY 255 VAL 256 -0.0063

VAL 256 LYS 257 -0.0001

LYS 257 ASP 258 0.0001

ASP 258 VAL 259 -0.0151

VAL 259 ILE 260 -0.0001

ILE 260 LEU 261 0.0005

LEU 261 GLU 262 -0.0415

GLU 262 SER 263 0.0002

SER 263 ALA 264 0.0003

ALA 264 ILE 265 -0.0227

ILE 265 THR 266 -0.0002

THR 266 THR 267 0.0002

THR 267 ILE 268 -0.0050

ILE 268 MET 269 0.0002

MET 269 ASP 270 -0.0002

ASP 270 PHE 271 0.0034

PHE 271 GLU 272 0.0001

GLU 272 ASP 273 0.0005

ASP 273 SER 274 -0.0152

SER 274 VAL 275 -0.0002

VAL 275 ALA 276 0.0001

ALA 276 ALA 277 0.0017

ALA 277 VAL 278 0.0003

VAL 278 ASP 279 -0.0002

ASP 279 ALA 280 -0.0003

ALA 280 ALA 281 -0.0002

ALA 281 ASP 282 0.0002

ASP 282 LYS 283 0.0002

LYS 283 VAL 284 -0.0001

VAL 284 LEU 285 0.0000

LEU 285 GLY 286 0.0002

GLY 286 TYR 287 -0.0002

TYR 287 ARG 288 -0.0003

ARG 288 ASN 289 0.0055

ASN 289 TRP 290 0.0000

TRP 290 LEU 291 0.0004

LEU 291 GLY 292 0.0039

GLY 292 LEU 293 0.0000

LEU 293 ASN 294 -0.0002

ASN 294 LYS 295 -0.0027

LYS 295 GLY 296 -0.0002

GLY 296 ASP 297 0.0000

ASP 297 LEU 298 -0.0020

LEU 298 ALA 299 0.0002

ALA 299 ALA 300 -0.0001

ALA 300 ARG 301 -0.0032

ARG 301 VAL 302 0.0003

VAL 302 LEU 303 -0.0003

LEU 303 ASN 304 -0.0253

ASN 304 ARG 305 -0.0002

ARG 305 ASP 306 0.0000

ASP 306 ARG 307 0.0335

ARG 307 ASN 308 0.0002

ASN 308 TYR 309 0.0001

TYR 309 THR 310 -0.0142

THR 310 ALA 311 -0.0001

ALA 311 PRO 312 -0.0000

PRO 312 GLY 313 0.0029

GLY 313 GLY 314 -0.0003

GLY 314 GLY 315 0.0002

GLY 315 GLN 316 -0.0125

GLN 316 PHE 317 -0.0001

PHE 317 THR 318 0.0002

THR 318 THR 318 -0.0317

THR 318 LEU 319 0.0122

LEU 319 PRO 320 -0.0001

PRO 320 GLY 321 -0.0002

GLY 321 ARG 322 -0.0018

ARG 322 SER 323 0.0002

SER 323 LEU 324 -0.0004

LEU 324 MET 325 0.0019

MET 325 PHE 326 -0.0000

PHE 326 VAL 327 -0.0002

VAL 327 ARG 328 -0.0049

ARG 328 ASN 329 0.0000

ASN 329 VAL 330 0.0001

VAL 330 GLY 331 -0.0114

GLY 331 HIS 332 -0.0000

HIS 332 LEU 333 0.0004

LEU 333 MET 334 -0.0155

MET 334 THR 335 0.0003

THR 335 ASN 336 -0.0001

ASN 336 ASP 337 -0.0040

ASP 337 ALA 338 -0.0000

ALA 338 ILE 339 0.0001

ILE 339 VAL 340 0.0007

VAL 340 ASP 341 0.0003

ASP 341 THR 342 -0.0004

THR 342 ASP 343 0.0004

ASP 343 GLY 344 -0.0002

GLY 344 SER 345 0.0004

SER 345 GLU 346 0.0000

GLU 346 VAL 347 -0.0003

VAL 347 PHE 348 0.0002

PHE 348 GLU 349 -0.0022

GLU 349 GLY 350 0.0001

GLY 350 ILE 351 -0.0002

ILE 351 MET 352 0.0031

MET 352 ASP 353 -0.0003

ASP 353 ALA 354 0.0002

ALA 354 LEU 355 -0.0019

LEU 355 PHE 356 -0.0001

PHE 356 THR 357 -0.0000

THR 357 GLY 358 -0.0020

GLY 358 LEU 359 -0.0003

LEU 359 ILE 360 0.0000

ILE 360 ALA 361 -0.0001

ALA 361 ILE 362 -0.0000

ILE 362 HIS 363 -0.0000

HIS 363 GLY 364 0.0010

GLY 364 LEU 365 -0.0004

LEU 365 LYS 366 -0.0003

LYS 366 ALA 367 0.0113

ALA 367 SER 368 0.0000

SER 368 PRO 369 0.0000

PRO 369 LEU 370 -0.0008

LEU 370 ILE 371 0.0001

ILE 371 ASN 372 0.0000

ASN 372 SER 373 0.0079

SER 373 ARG 374 0.0001

ARG 374 THR 375 -0.0001

THR 375 GLY 376 0.0038

GLY 376 SER 377 0.0001

SER 377 ILE 378 -0.0003

ILE 378 TYR 379 -0.0042

TYR 379 ILE 380 0.0001

ILE 380 ILE 380 -0.0000

ILE 380 VAL 381 -0.0002

VAL 381 LYS 382 -0.0045

LYS 382 PRO 383 0.0002

PRO 383 LYS 384 -0.0002

LYS 384 MET 385 -0.0220

MET 385 HIS 386 -0.0002

HIS 386 GLY 387 0.0004

GLY 387 PRO 388 -0.0112

PRO 388 ALA 389 -0.0001

ALA 389 GLU 390 0.0002

GLU 390 VAL 391 0.0039

VAL 391 ALA 392 0.0002

ALA 392 PHE 393 0.0002

PHE 393 THR 394 0.0002

THR 394 CYS 395 -0.0002

CYS 395 GLU 396 -0.0000

GLU 396 LEU 397 0.0003

LEU 397 PHE 398 0.0002

PHE 398 SER 399 -0.0001

SER 399 ARG 400 -0.0015

ARG 400 VAL 401 -0.0003

VAL 401 GLU 402 0.0000

GLU 402 ASP 403 -0.0068

ASP 403 VAL 404 -0.0001

VAL 404 LEU 405 -0.0000

LEU 405 GLY 406 -0.0044

GLY 406 LEU 407 -0.0004

LEU 407 PRO 408 0.0003

PRO 408 GLN 409 0.0034

GLN 409 ASN 410 0.0004

ASN 410 THR 411 -0.0002

THR 411 MET 412 0.0026

MET 412 LYS 413 -0.0004

LYS 413 ILE 414 -0.0001

ILE 414 ILE 414 0.0000

ILE 414 GLY 415 -0.0168

GLY 415 ILE 416 -0.0002

ILE 416 MET 417 0.0002

MET 417 ASP 418 -0.0298

ASP 418 GLU 419 -0.0002

GLU 419 GLU 420 0.0001

GLU 420 ARG 421 -0.1170

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.

*** 6DNP ***

CA strain for 240228060517928664

--- normal mode 8 ---

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

* 6DNP *