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

* MEMBRANE PROTEIN 28-DEC-19 6LN2 *

CA strain for 22033117492247294

--- 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
PRO 137 GLU 138 -0.0004

GLU 138 GLU 139 0.0053

GLU 139 GLN 140 0.0000

GLN 140 LEU 141 -0.0088

LEU 141 LEU 142 -0.0002

LEU 142 PHE 143 0.0060

PHE 143 LEU 144 0.0000

LEU 144 TYR 145 -0.0088

TYR 145 ILE 146 0.0004

ILE 146 ILE 147 0.0009

ILE 147 TYR 148 -0.0003

TYR 148 THR 149 0.0032

THR 149 VAL 150 0.0002

VAL 150 GLY 151 0.0161

GLY 151 TYR 152 -0.0000

TYR 152 ALA 153 0.0100

ALA 153 LEU 154 0.0001

LEU 154 SER 155 -0.0001

SER 155 PHE 156 -0.0002

PHE 156 SER 157 0.0224

SER 157 ALA 158 0.0002

ALA 158 LEU 159 -0.0139

LEU 159 VAL 160 -0.0002

VAL 160 ILE 161 0.0616

ILE 161 ALA 162 -0.0004

ALA 162 SER 163 -0.0415

SER 163 ALA 164 0.0001

ALA 164 ILE 165 0.0236

ILE 165 LEU 166 -0.0003

LEU 166 LEU 167 -0.0371

LEU 167 GLY 168 0.0002

GLY 168 PHE 169 0.0857

PHE 169 ARG 170 -0.0001

ARG 170 HIS 171 -0.0079

HIS 171 LEU 172 0.0002

LEU 172 HIS 173 -0.0206

HIS 173 CYS 174 -0.0004

CYS 174 THR 175 -0.0007

THR 175 ARG 176 0.0002

ARG 176 ASN 177 0.0180

ASN 177 TYR 178 0.0002

TYR 178 ILE 179 0.0066

ILE 179 HIS 180 0.0000

HIS 180 LEU 181 -0.0001

LEU 181 ASN 182 -0.0000

ASN 182 LEU 183 0.0013

LEU 183 PHE 184 0.0003

PHE 184 ALA 185 0.0115

ALA 185 SER 186 -0.0001

SER 186 PHE 187 -0.0117

PHE 187 ILE 188 0.0001

ILE 188 LEU 189 0.0386

LEU 189 ARG 190 -0.0001

ARG 190 ALA 191 0.0011

ALA 191 LEU 192 -0.0003

LEU 192 CYS 193 0.0639

CYS 193 VAL 194 -0.0001

VAL 194 PHE 195 -0.0804

PHE 195 PHE 196 0.0001

PHE 196 LYS 197 0.0394

LYS 197 ASP 198 0.0001

ASP 198 ALA 199 -0.0855

ALA 199 ALA 200 -0.0002

ALA 200 LEU 201 0.0288

LEU 201 LYS 202 0.0000

LYS 202 TRP 203 -0.0420

TRP 203 MET 204 0.0002

MET 204 TYR 205 -0.0037

TYR 205 SER 206 0.0000

SER 206 THR 207 0.0167

THR 207 ALA 208 0.0003

ALA 208 ALA 209 -0.0120

ALA 209 GLN 210 0.0002

GLN 210 GLN 211 -0.0026

GLN 211 HIS 212 0.0000

HIS 212 GLN 213 0.0050

GLN 213 TRP 214 -0.0001

TRP 214 ASP 215 -0.0136

ASP 215 GLY 216 -0.0001

GLY 216 LEU 217 0.0222

LEU 217 LEU 218 -0.0002

LEU 218 SER 219 0.0481

SER 219 TYR 220 -0.0001

TYR 220 GLN 221 0.0334

GLN 221 ASP 222 -0.0001

ASP 222 SER 223 0.0304

SER 223 LEU 224 -0.0003

LEU 224 ALA 225 0.0084

ALA 225 CYS 226 -0.0002

CYS 226 ARG 227 0.0222

ARG 227 LEU 228 0.0002

LEU 228 VAL 229 0.0232

VAL 229 PHE 230 -0.0002

PHE 230 LEU 231 0.0142

LEU 231 LEU 232 0.0001

LEU 232 CYS 233 0.0016

CYS 233 GLN 234 -0.0002

GLN 234 TYR 235 -0.0327

TYR 235 CYS 236 0.0001

CYS 236 VAL 237 0.0050

VAL 237 ALA 238 -0.0003

ALA 238 ALA 239 0.0048

ALA 239 ASN 240 0.0001

ASN 240 TYR 241 -0.0015

TYR 241 TYR 242 -0.0004

TYR 242 TRP 243 -0.0079

TRP 243 LEU 244 0.0004

LEU 244 LEU 245 0.0072

LEU 245 VAL 246 0.0000

VAL 246 GLU 247 -0.0172

GLU 247 GLY 248 -0.0003

GLY 248 VAL 249 0.0080

VAL 249 TYR 250 0.0005

TYR 250 LEU 251 -0.0015

LEU 251 TYR 252 0.0002

TYR 252 THR 253 0.0144

THR 253 LEU 254 0.0005

LEU 254 LEU 255 0.0073

LEU 255 ALA 256 -0.0002

ALA 256 PHE 257 -0.0115

PHE 257 MET 1001 0.0133

MET 1001 LYS 1002 -0.0003

LYS 1002 LYS 1003 0.0136

LYS 1003 TYR 1004 0.0000

TYR 1004 THR 1005 0.0068

THR 1005 CYS 1006 0.0000

CYS 1006 THR 1007 0.0058

THR 1007 VAL 1008 -0.0000

VAL 1008 CYS 1009 -0.0035

CYS 1009 GLY 1010 0.0001

GLY 1010 TYR 1011 -0.0078

TYR 1011 ILE 1012 -0.0001

ILE 1012 TYR 1013 -0.0137

TYR 1013 ASN 1014 0.0002

ASN 1014 PRO 1015 0.0028

PRO 1015 GLU 1016 -0.0001

GLU 1016 ASP 1017 0.0060

ASP 1017 GLY 1018 -0.0000

GLY 1018 ASP 1019 0.0017

ASP 1019 PRO 1020 -0.0003

PRO 1020 ASP 1021 0.0016

ASP 1021 ASN 1022 -0.0002

ASN 1022 GLY 1023 -0.0007

GLY 1023 VAL 1024 -0.0001

VAL 1024 ASN 1025 0.0035

ASN 1025 PRO 1026 -0.0001

PRO 1026 GLY 1027 0.0050

GLY 1027 THR 1028 0.0000

THR 1028 ASP 1029 0.0057

ASP 1029 PHE 1030 -0.0002

PHE 1030 LYS 1031 0.0119

LYS 1031 ASP 1032 0.0003

ASP 1032 ILE 1033 0.0051

ILE 1033 PRO 1034 0.0000

PRO 1034 ASP 1035 0.0116

ASP 1035 ASP 1036 -0.0002

ASP 1036 TRP 1037 -0.0112

TRP 1037 VAL 1038 -0.0001

VAL 1038 CYS 1039 -0.0067

CYS 1039 PRO 1040 0.0004

PRO 1040 LEU 1041 -0.0069

LEU 1041 CYS 1042 0.0001

CYS 1042 GLY 1043 0.0028

GLY 1043 VAL 1044 0.0001

VAL 1044 GLY 1045 -0.0104

GLY 1045 LYS 1046 -0.0001

LYS 1046 ASP 1047 0.0492

ASP 1047 GLN 1048 0.0001

GLN 1048 PHE 1049 -0.0376

PHE 1049 GLU 1050 0.0001

GLU 1050 GLU 1051 -0.0196

GLU 1051 VAL 1052 -0.0001

VAL 1052 GLU 1053 0.0229

GLU 1053 GLU 1054 -0.0002

GLU 1054 GLU 262 0.0083

GLU 262 GLN 263 0.0004

GLN 263 TRP 264 -0.0231

TRP 264 ILE 265 0.0000

ILE 265 PHE 266 0.0037

PHE 266 ARG 267 -0.0001

ARG 267 LEU 268 0.0111

LEU 268 TYR 269 0.0003

TYR 269 VAL 270 -0.0180

VAL 270 ALA 271 -0.0001

ALA 271 ILE 272 0.0305

ILE 272 GLY 273 -0.0000

GLY 273 TRP 274 0.0105

TRP 274 GLY 275 -0.0000

GLY 275 VAL 276 0.0327

VAL 276 PRO 277 0.0001

PRO 277 LEU 278 -0.0042

LEU 278 LEU 279 0.0003

LEU 279 PHE 280 -0.0066

PHE 280 VAL 281 -0.0001

VAL 281 VAL 282 0.0252

VAL 282 PRO 283 -0.0003

PRO 283 TRP 284 -0.0016

TRP 284 GLY 285 -0.0002

GLY 285 ILE 286 0.0295

ILE 286 VAL 287 -0.0002

VAL 287 LYS 288 0.0018

LYS 288 TYR 289 0.0000

TYR 289 LEU 290 0.0154

LEU 290 TYR 291 0.0003

TYR 291 GLU 292 -0.0084

GLU 292 ASP 293 -0.0000

ASP 293 GLU 294 -0.0203

GLU 294 GLY 295 -0.0001

GLY 295 CYS 296 0.0097

CYS 296 TRP 297 0.0001

TRP 297 THR 298 0.0210

THR 298 ARG 299 -0.0001

ARG 299 ASN 300 -0.0358

ASN 300 SER 301 -0.0001

SER 301 ASN 302 0.0023

ASN 302 MET 303 -0.0004

MET 303 ASN 304 0.0022

ASN 304 TYR 305 -0.0001

TYR 305 TRP 306 0.0197

TRP 306 LEU 307 -0.0000

LEU 307 ILE 308 0.0174

ILE 308 ILE 309 0.0002

ILE 309 ARG 310 -0.0007

ARG 310 LEU 311 0.0002

LEU 311 PRO 312 0.0135

PRO 312 ILE 313 -0.0001

ILE 313 LEU 314 0.0003

LEU 314 PHE 315 0.0003

PHE 315 ALA 316 0.0107

ALA 316 CYS 317 0.0001

CYS 317 ILE 318 0.0070

ILE 318 VAL 319 -0.0003

VAL 319 ASN 320 -0.0014

ASN 320 PHE 321 -0.0003

PHE 321 LEU 322 0.0086

LEU 322 ILE 323 -0.0003

ILE 323 PHE 324 -0.0012

PHE 324 VAL 325 0.0003

VAL 325 ARG 326 0.0150

ARG 326 VAL 327 -0.0001

VAL 327 ILE 328 -0.0069

ILE 328 CYS 329 -0.0001

CYS 329 ILE 330 0.0129

ILE 330 VAL 331 0.0000

VAL 331 VAL 332 0.0027

VAL 332 SER 333 -0.0002

SER 333 LYS 334 0.0036

LYS 334 LEU 335 -0.0002

LEU 335 LYS 336 -0.0037

LYS 336 ALA 337 0.0003

ALA 337 ASN 338 0.0029

ASN 338 LEU 339 -0.0003

LEU 339 MET 340 0.0051

MET 340 CYS 341 0.0002

CYS 341 LYS 342 0.0164

LYS 342 THR 343 0.0001

THR 343 ASP 344 0.0095

ASP 344 ILE 345 -0.0003

ILE 345 ALA 346 -0.0270

ALA 346 PHE 347 0.0002

PHE 347 ARG 348 -0.0115

ARG 348 LEU 349 -0.0002

LEU 349 ALA 350 -0.0260

ALA 350 LYS 351 0.0002

LYS 351 SER 352 0.0311

SER 352 THR 353 0.0003

THR 353 LEU 354 0.0020

LEU 354 THR 355 0.0001

THR 355 LEU 356 0.0093

LEU 356 ILE 357 0.0003

ILE 357 PRO 358 -0.0038

PRO 358 LEU 359 0.0000

LEU 359 LEU 360 0.0030

LEU 360 CYS 361 0.0001

CYS 361 THR 362 -0.0083

THR 362 HIS 363 0.0001

HIS 363 GLU 364 0.0085

GLU 364 VAL 365 -0.0001

VAL 365 ILE 366 0.0131

ILE 366 PHE 367 -0.0002

PHE 367 ALA 368 0.0030

ALA 368 PHE 369 0.0002

PHE 369 VAL 370 -0.0019

VAL 370 MET 371 -0.0000

MET 371 ASP 372 0.0071

ASP 372 GLU 373 -0.0001

GLU 373 HIS 374 -0.0007

HIS 374 ALA 375 -0.0000

ALA 375 ARG 376 0.0001

ARG 376 GLY 377 -0.0004

GLY 377 THR 378 0.0022

THR 378 LEU 379 0.0002

LEU 379 ARG 380 0.0080

ARG 380 PHE 381 -0.0001

PHE 381 ILE 382 0.0029

ILE 382 LYS 383 0.0004

LYS 383 LEU 384 0.0001

LEU 384 PHE 385 0.0001

PHE 385 THR 386 0.0148

THR 386 ASP 387 -0.0003

ASP 387 LEU 388 -0.0129

LEU 388 SER 389 -0.0000

SER 389 PHE 390 -0.0039

PHE 390 THR 391 0.0002

THR 391 SER 392 -0.0005

SER 392 PHE 393 -0.0000

PHE 393 GLN 394 0.0091

GLN 394 GLY 395 -0.0003

GLY 395 LEU 396 -0.0018

LEU 396 MET 397 -0.0002

MET 397 VAL 398 0.0025

VAL 398 ALA 399 0.0000

ALA 399 ILE 400 -0.0104

ILE 400 LEU 401 0.0001

LEU 401 TYR 402 -0.0007

TYR 402 CYS 403 0.0002

CYS 403 PHE 404 -0.0278

PHE 404 VAL 405 -0.0001

VAL 405 ASN 406 -0.0043

ASN 406 ASN 407 -0.0001

ASN 407 GLU 408 0.0268

GLU 408 VAL 409 -0.0002

VAL 409 GLN 410 -0.0390

GLN 410 LEU 411 0.0002

LEU 411 GLU 412 0.0354

GLU 412 PHE 413 -0.0003

PHE 413 ARG 414 0.0233

ARG 414 LYS 415 -0.0003

LYS 415 SER 416 -0.1070

SER 416 TRP 417 -0.0001

TRP 417 GLU 418 0.0693

GLU 418 ARG 419 0.0000

ARG 419 TRP 420 -0.0458

TRP 420 ARG 421 0.0006

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: October 18th, 2018.

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

*** MEMBRANE PROTEIN 28-DEC-19 6LN2 ***

CA strain for 22033117492247294

--- normal mode 8 ---

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

* MEMBRANE PROTEIN 28-DEC-19 6LN2 *