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

* 4FF6 *

CA strain for 201226195629118096

--- 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 7 THR 8 -0.0000

THR 8 THR 9 0.0002

THR 9 ALA 10 -0.0021

ALA 10 THR 11 -0.0000

THR 11 ARG 12 -0.0001

ARG 12 LEU 13 -0.0071

LEU 13 THR 14 -0.0002

THR 14 GLY 15 0.0004

GLY 15 TRP 16 -0.0040

TRP 16 GLY 17 0.0000

GLY 17 ARG 18 0.0001

ARG 18 THR 19 -0.0263

THR 19 ALA 20 0.0001

ALA 20 PRO 21 0.0002

PRO 21 SER 22 0.0053

SER 22 VAL 23 0.0002

VAL 23 ALA 24 -0.0003

ALA 24 ASN 25 0.0011

ASN 25 VAL 26 -0.0000

VAL 26 LEU 27 0.0001

LEU 27 ARG 28 -0.0022

ARG 28 THR 29 0.0001

THR 29 PRO 30 0.0003

PRO 30 ASP 31 -0.0036

ASP 31 ALA 32 0.0000

ALA 32 GLU 33 -0.0001

GLU 33 MET 34 0.0037

MET 34 ILE 35 -0.0003

ILE 35 VAL 36 -0.0002

VAL 36 LYS 37 0.0034

LYS 37 ALA 38 -0.0004

ALA 38 VAL 39 -0.0001

VAL 39 ALA 40 0.0009

ALA 40 ARG 41 0.0002

ARG 41 VAL 42 -0.0003

VAL 42 ALA 43 -0.0010

ALA 43 GLU 44 0.0001

GLU 44 SER 45 -0.0003

SER 45 GLY 48 -0.0099

GLY 48 ARG 49 -0.0000

ARG 49 GLY 50 -0.0003

GLY 50 ALA 51 -0.0039

ALA 51 ILE 52 -0.0000

ILE 52 ALA 53 0.0004

ALA 53 ARG 54 -0.0146

ARG 54 GLY 55 -0.0002

GLY 55 LEU 56 0.0002

LEU 56 GLY 57 0.0554

GLY 57 ARG 58 -0.0002

ARG 58 SER 59 -0.0002

SER 59 TYR 60 0.0364

TYR 60 GLY 61 0.0005

GLY 61 ASP 62 -0.0005

ASP 62 ASN 63 0.0073

ASN 63 ALA 64 0.0001

ALA 64 GLN 65 0.0000

GLN 65 ASN 66 -0.0103

ASN 66 GLY 67 -0.0001

GLY 67 GLY 68 -0.0002

GLY 68 GLY 69 -0.0029

GLY 69 LEU 70 0.0003

LEU 70 VAL 71 0.0001

VAL 71 ILE 72 0.0050

ILE 72 ASP 73 0.0002

ASP 73 MET 74 0.0001

MET 74 THR 75 -0.0134

THR 75 PRO 76 0.0000

PRO 76 LEU 77 -0.0001

LEU 77 ASN 78 -0.0185

ASN 78 THR 79 0.0001

THR 79 ILE 80 0.0003

ILE 80 HIS 81 -0.0011

HIS 81 SER 82 -0.0002

SER 82 ILE 83 -0.0003

ILE 83 ASP 84 0.0103

ASP 84 ALA 85 -0.0002

ALA 85 ASP 86 -0.0000

ASP 86 THR 87 -0.0065

THR 87 LYS 88 0.0000

LYS 88 LEU 89 -0.0001

LEU 89 VAL 90 0.0069

VAL 90 ASP 91 -0.0001

ASP 91 ILE 92 -0.0001

ILE 92 ASP 93 0.0148

ASP 93 ALA 94 0.0001

ALA 94 GLY 95 -0.0002

GLY 95 VAL 96 -0.0206

VAL 96 ASN 97 0.0001

ASN 97 LEU 98 -0.0001

LEU 98 ASP 99 -0.0085

ASP 99 GLN 100 0.0004

GLN 100 LEU 101 -0.0001

LEU 101 MET 102 -0.0155

MET 102 LYS 103 0.0001

LYS 103 ALA 104 0.0001

ALA 104 ALA 105 0.0029

ALA 105 LEU 106 -0.0001

LEU 106 PRO 107 0.0000

PRO 107 PHE 108 -0.0015

PHE 108 GLY 109 -0.0001

GLY 109 LEU 110 0.0001

LEU 110 TRP 111 -0.0013

TRP 111 VAL 112 0.0000

VAL 112 PRO 113 -0.0000

PRO 113 VAL 114 -0.0118

VAL 114 LEU 115 -0.0001

LEU 115 PRO 116 -0.0001

PRO 116 GLY 117 0.0159

GLY 117 THR 118 0.0001

THR 118 ARG 119 0.0001

ARG 119 GLN 120 -0.0397

GLN 120 VAL 121 0.0001

VAL 121 THR 122 -0.0002

THR 122 VAL 123 0.0027

VAL 123 GLY 124 -0.0002

GLY 124 GLY 125 0.0000

GLY 125 ALA 126 -0.0022

ALA 126 ILE 127 0.0000

ILE 127 ALA 128 0.0001

ALA 128 CYS 129 0.0051

CYS 129 ASP 130 -0.0003

ASP 130 ILE 131 0.0004

ILE 131 HIS 132 0.0053

HIS 132 GLY 133 -0.0000

GLY 133 LYS 134 -0.0001

LYS 134 ASN 135 0.0253

ASN 135 HIS 136 -0.0001

HIS 136 HIS 137 -0.0002

HIS 137 SER 138 -0.0172

SER 138 ALA 139 -0.0001

ALA 139 GLY 140 0.0003

GLY 140 SER 141 0.0283

SER 141 PHE 142 0.0003

PHE 142 GLY 143 0.0000

GLY 143 ASN 144 -0.0021

ASN 144 HIS 145 0.0003

HIS 145 VAL 146 -0.0001

VAL 146 ARG 147 0.0023

ARG 147 SER 148 0.0001

SER 148 MET 149 -0.0002

MET 149 ASP 150 0.0244

ASP 150 LEU 151 -0.0001

LEU 151 LEU 152 0.0001

LEU 152 THR 153 -0.0022

THR 153 ALA 154 -0.0002

ALA 154 ASP 155 0.0001

ASP 155 GLY 156 -0.0073

GLY 156 GLU 157 -0.0002

GLU 157 ILE 158 -0.0001

ILE 158 ARG 159 0.0025

ARG 159 HIS 160 0.0000

HIS 160 LEU 161 -0.0004

LEU 161 THR 162 0.0099

THR 162 PRO 163 -0.0000

PRO 163 THR 164 -0.0004

THR 164 GLY 165 0.0044

GLY 165 GLU 166 -0.0003

GLU 166 ASP 167 0.0000

ASP 167 ALA 168 -0.0034

ALA 168 GLU 169 -0.0001

GLU 169 LEU 170 0.0002

LEU 170 PHE 171 0.0130

PHE 171 TRP 172 0.0002

TRP 172 ALA 173 -0.0001

ALA 173 THR 174 -0.0047

THR 174 VAL 175 -0.0001

VAL 175 GLY 176 0.0002

GLY 176 GLY 177 0.0044

GLY 177 ASN 178 -0.0000

ASN 178 GLY 179 0.0000

GLY 179 LEU 180 -0.0002

LEU 180 THR 181 0.0003

THR 181 GLY 182 -0.0001

GLY 182 ILE 183 -0.0082

ILE 183 ILE 184 0.0005

ILE 184 MET 185 -0.0002

MET 185 ARG 186 0.0227

ARG 186 ALA 187 0.0003

ALA 187 THR 188 -0.0001

THR 188 ILE 189 0.0206

ILE 189 GLU 190 0.0001

GLU 190 MET 191 -0.0003

MET 191 THR 192 0.0376

THR 192 PRO 193 0.0001

PRO 193 THR 194 -0.0003

THR 194 SER 195 0.0262

SER 195 THR 196 -0.0002

THR 196 ALA 197 -0.0001

ALA 197 TYR 198 0.0164

TYR 198 PHE 199 0.0001

PHE 199 ILE 200 -0.0001

ILE 200 ALA 201 0.0354

ALA 201 ASP 202 0.0003

ASP 202 GLY 203 -0.0003

GLY 203 ASP 204 0.0821

ASP 204 VAL 205 0.0003

VAL 205 THR 206 -0.0002

THR 206 ALA 207 -0.0139

ALA 207 SER 208 0.0000

SER 208 LEU 209 0.0002

LEU 209 ASP 210 0.0069

ASP 210 GLU 211 0.0001

GLU 211 THR 212 -0.0000

THR 212 ILE 213 -0.0083

ILE 213 ALA 214 0.0000

ALA 214 LEU 215 0.0004

LEU 215 HIS 216 0.0012

HIS 216 SER 217 -0.0001

SER 217 ASP 218 0.0003

ASP 218 GLY 219 -0.0601

GLY 219 SER 220 0.0001

SER 220 GLU 221 0.0002

GLU 221 ALA 222 -0.0300

ALA 222 ARG 223 0.0002

ARG 223 TYR 224 -0.0002

TYR 224 THR 225 0.0198

THR 225 TYR 226 -0.0003

TYR 226 SER 227 0.0000

SER 227 SER 228 -0.0114

SER 228 ALA 229 0.0001

ALA 229 TRP 230 -0.0004

TRP 230 PHE 231 0.0939

PHE 231 ASP 232 -0.0003

ASP 232 ALA 233 0.0001

ALA 233 ILE 234 -0.0107

ILE 234 SER 235 -0.0002

SER 235 ALA 236 -0.0004

ALA 236 PRO 237 0.0513

PRO 237 PRO 238 0.0001

PRO 238 LYS 239 -0.0002

LYS 239 LEU 240 -0.0149

LEU 240 GLY 241 0.0001

GLY 241 ARG 242 -0.0001

ARG 242 ALA 243 0.0665

ALA 243 ALA 244 0.0001

ALA 244 VAL 245 -0.0004

VAL 245 SER 246 0.0784

SER 246 ARG 247 0.0001

ARG 247 GLY 248 0.0002

GLY 248 ARG 249 0.0071

ARG 249 LEU 250 -0.0002

LEU 250 ALA 251 -0.0001

ALA 251 THR 252 -0.0103

THR 252 VAL 253 -0.0001

VAL 253 GLU 254 0.0002

GLU 254 GLN 255 0.0093

GLN 255 LEU 256 0.0000

LEU 256 PRO 257 -0.0000

PRO 257 ALA 258 0.0135

ALA 258 LYS 259 -0.0001

LYS 259 LEU 260 -0.0004

LEU 260 ARG 261 0.0026

ARG 261 SER 262 0.0003

SER 262 GLU 263 -0.0002

GLU 263 PRO 264 0.0057

PRO 264 LEU 265 -0.0001

LEU 265 LYS 266 -0.0002

LYS 266 PHE 267 -0.0181

PHE 267 ASP 268 0.0001

ASP 268 ALA 284 0.5567

ALA 284 ASN 285 -0.0001

ASN 285 LYS 286 0.0000

LYS 286 TYR 287 -0.0100

TYR 287 THR 288 0.0001

THR 288 PHE 289 -0.0001

PHE 289 GLY 290 0.0449

GLY 290 PRO 291 0.0000

PRO 291 ILE 292 0.0001

ILE 292 GLY 293 -0.0335

GLY 293 GLU 294 -0.0004

GLU 294 LEU 295 -0.0001

LEU 295 TRP 296 -0.1590

TRP 296 TYR 297 0.0001

TYR 297 ARG 298 -0.0002

ARG 298 LYS 299 -0.0542

LYS 299 SER 300 0.0003

SER 300 GLY 301 0.0001

GLY 301 THR 302 0.0995

THR 302 TYR 303 0.0003

TYR 303 ARG 304 0.0001

ARG 304 GLY 305 0.0487

GLY 305 LYS 306 -0.0000

LYS 306 VAL 307 0.0000

VAL 307 GLN 308 -0.0418

GLN 308 ASN 309 0.0002

ASN 309 LEU 310 -0.0002

LEU 310 THR 311 0.0083

THR 311 GLN 312 0.0002

GLN 312 PHE 313 -0.0001

PHE 313 TYR 314 -0.0534

TYR 314 HIS 315 0.0002

HIS 315 GLY 331 -0.0389

GLY 331 PHE 332 -0.0003

PHE 332 LEU 333 0.0001

LEU 333 GLN 334 0.0140

GLN 334 TYR 335 0.0003

TYR 335 GLN 336 0.0001

GLN 336 PHE 337 0.0102

PHE 337 VAL 338 -0.0001

VAL 338 ILE 339 -0.0001

ILE 339 PRO 340 -0.0018

PRO 340 THR 341 -0.0001

THR 341 GLU 342 -0.0001

GLU 342 ALA 343 -0.0052

ALA 343 VAL 344 0.0001

VAL 344 ASP 345 0.0000

ASP 345 GLU 346 0.0154

GLU 346 PHE 347 0.0000

PHE 347 LYS 348 0.0000

LYS 348 LYS 349 0.0297

LYS 349 ILE 350 0.0001

ILE 350 ILE 351 -0.0003

ILE 351 GLY 352 0.0018

GLY 352 VAL 353 0.0000

VAL 353 ILE 354 -0.0005

ILE 354 GLN 355 -0.0176

GLN 355 ALA 356 0.0002

ALA 356 SER 357 0.0001

SER 357 GLY 358 0.0014

GLY 358 HIS 359 -0.0002

HIS 359 TYR 360 0.0001

TYR 360 SER 361 -0.0274

SER 361 PHE 362 -0.0004

PHE 362 LEU 363 0.0000

LEU 363 ASN 364 0.0100

ASN 364 VAL 365 -0.0002

VAL 365 PHE 366 -0.0001

PHE 366 LYS 367 0.0133

LYS 367 LEU 368 0.0000

LEU 368 PHE 369 -0.0002

PHE 369 GLY 370 0.0039

GLY 370 PRO 371 0.0002

PRO 371 ARG 372 0.0002

ARG 372 ASN 373 -0.0114

ASN 373 GLN 374 0.0000

GLN 374 ALA 375 -0.0002

ALA 375 PRO 376 -0.0012

PRO 376 LEU 377 0.0001

LEU 377 SER 378 0.0001

SER 378 PHE 379 -0.0054

PHE 379 PRO 380 0.0001

PRO 380 ILE 381 0.0004

ILE 381 PRO 382 -0.0032

PRO 382 GLY 383 0.0002

GLY 383 TRP 384 -0.0002

TRP 384 ASN 385 0.0016

ASN 385 ILE 386 -0.0002

ILE 386 CYS 387 0.0003

CYS 387 VAL 388 -0.0039

VAL 388 ASP 389 0.0000

ASP 389 PHE 390 -0.0001

PHE 390 PRO 391 -0.0139

PRO 391 ILE 392 -0.0003

ILE 392 LYS 393 -0.0001

LYS 393 ASP 394 -0.0018

ASP 394 GLY 395 -0.0001

GLY 395 LEU 396 -0.0001

LEU 396 GLY 397 -0.0101

GLY 397 LYS 398 -0.0002

LYS 398 PHE 399 -0.0000

PHE 399 VAL 400 -0.0059

VAL 400 SER 401 -0.0004

SER 401 GLU 402 -0.0000

GLU 402 LEU 403 -0.0006

LEU 403 ASP 404 0.0001

ASP 404 ARG 405 -0.0002

ARG 405 ARG 406 0.0114

ARG 406 VAL 407 -0.0000

VAL 407 LEU 408 0.0003

LEU 408 GLU 409 -0.0057

GLU 409 PHE 410 0.0002

PHE 410 GLY 411 -0.0003

GLY 411 GLY 412 0.0014

GLY 412 ARG 413 0.0003

ARG 413 LEU 414 -0.0003

LEU 414 TYR 415 0.0062

TYR 415 THR 416 0.0002

THR 416 ALA 417 0.0002

ALA 417 LYS 418 0.0157

LYS 418 ASP 419 -0.0000

ASP 419 SER 420 0.0001

SER 420 ARG 421 0.0171

ARG 421 THR 422 -0.0001

THR 422 THR 423 -0.0002

THR 423 ALA 424 -0.0219

ALA 424 GLU 425 -0.0001

GLU 425 THR 426 -0.0005

THR 426 PHE 427 -0.0115

PHE 427 HIS 428 0.0001

HIS 428 ALA 429 -0.0002

ALA 429 MET 430 0.0130

MET 430 TYR 431 0.0001

TYR 431 PRO 432 -0.0000

PRO 432 ARG 433 -0.0464

ARG 433 VAL 434 -0.0000

VAL 434 ASP 435 -0.0000

ASP 435 GLU 436 -0.0278

GLU 436 TRP 437 -0.0000

TRP 437 ILE 438 0.0002

ILE 438 SER 439 -0.0067

SER 439 VAL 440 0.0002

VAL 440 ARG 441 0.0002

ARG 441 ARG 442 0.0048

ARG 442 LYS 443 -0.0002

LYS 443 VAL 444 0.0001

VAL 444 ASP 445 0.0082

ASP 445 PRO 446 -0.0000

PRO 446 LEU 447 -0.0000

LEU 447 ARG 448 -0.0052

ARG 448 VAL 449 0.0000

VAL 449 PHE 450 0.0001

PHE 450 ALA 451 -0.0008

ALA 451 SER 452 -0.0001

SER 452 ASP 453 -0.0001

ASP 453 MET 454 0.0041

MET 454 ALA 455 0.0000

ALA 455 ARG 456 -0.0003

ARG 456 ARG 457 -0.0123

ARG 457 LEU 458 0.0001

LEU 458 GLU 459 0.0002

GLU 459 LEU 460 -0.0091

LEU 460 LEU 461 -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: October 18th, 2018.

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

*** 4FF6 ***

CA strain for 201226195629118096

--- normal mode 8 ---

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

* 4FF6 *