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

* TRANSFERASE 31-MAR-06 2CJD *

CA strain for 220405004109145553

--- normal mode 9 ---

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 15 THR 16 0.0004

THR 16 PRO 17 0.0001

PRO 17 ASP 18 -0.1716

ASP 18 ARG 19 -0.0003

ARG 19 VAL 20 0.0000

VAL 20 HIS 21 0.0045

HIS 21 GLU 22 0.0004

GLU 22 VAL 23 -0.0001

VAL 23 LEU 24 0.0027

LEU 24 GLY 25 0.0000

GLY 25 ARG 26 -0.0001

ARG 26 SER 27 -0.0512

SER 27 MET 28 0.0001

MET 28 LEU 29 -0.0001

LEU 29 VAL 30 -0.0821

VAL 30 ASP 31 -0.0002

ASP 31 GLY 32 -0.0000

GLY 32 LEU 33 0.0722

LEU 33 ASP 34 -0.0003

ASP 34 ILE 35 0.0002

ILE 35 VAL 36 0.0039

VAL 36 LEU 37 -0.0002

LEU 37 ASP 38 0.0001

ASP 38 LEU 39 -0.0992

LEU 39 THR 40 0.0000

THR 40 ARG 41 0.0001

ARG 41 SER 42 0.0021

SER 42 GLY 43 0.0003

GLY 43 GLY 44 0.0001

GLY 44 SER 45 -0.0267

SER 45 TYR 46 -0.0000

TYR 46 LEU 47 -0.0001

LEU 47 VAL 48 -0.0649

VAL 48 ASP 49 0.0002

ASP 49 ALA 50 -0.0001

ALA 50 ILE 51 -0.1882

ILE 51 THR 52 0.0000

THR 52 GLY 53 -0.0002

GLY 53 ARG 54 0.0595

ARG 54 ARG 55 0.0002

ARG 55 TYR 56 0.0001

TYR 56 LEU 57 0.0572

LEU 57 ASP 58 -0.0003

ASP 58 MET 59 0.0003

MET 59 PHE 60 0.0018

PHE 60 THR 61 0.0000

THR 61 PHE 62 0.0003

PHE 62 VAL 63 0.0582

VAL 63 ALA 64 0.0000

ALA 64 SER 65 0.0001

SER 65 SER 66 0.0355

SER 66 ALA 67 -0.0002

ALA 67 LEU 68 -0.0002

LEU 68 GLY 69 -0.0910

GLY 69 MET 70 0.0003

MET 70 ASN 71 -0.0002

ASN 71 PRO 72 -0.0700

PRO 72 PRO 73 -0.0002

PRO 73 ALA 74 -0.0001

ALA 74 LEU 75 0.0232

LEU 75 VAL 76 -0.0004

VAL 76 ASP 77 0.0001

ASP 77 ASP 78 -0.0152

ASP 78 ARG 79 -0.0000

ARG 79 GLU 80 -0.0001

GLU 80 PHE 81 0.0077

PHE 81 HIS 82 -0.0001

HIS 82 ALA 83 -0.0001

ALA 83 GLU 84 -0.0009

GLU 84 LEU 85 -0.0001

LEU 85 MET 86 0.0000

MET 86 GLN 87 -0.0067

GLN 87 ALA 88 0.0002

ALA 88 ALA 89 -0.0005

ALA 89 LEU 90 -0.0202

LEU 90 ASN 91 -0.0001

ASN 91 LYS 92 0.0001

LYS 92 PRO 93 0.0023

PRO 93 SER 94 0.0004

SER 94 ASN 95 -0.0003

ASN 95 SER 96 0.0101

SER 96 ASP 97 -0.0002

ASP 97 VAL 98 -0.0001

VAL 98 TYR 99 0.0174

TYR 99 SER 100 0.0002

SER 100 VAL 101 0.0001

VAL 101 ALA 102 -0.0210

ALA 102 MET 103 -0.0002

MET 103 ALA 104 0.0001

ALA 104 ARG 105 0.0115

ARG 105 PHE 106 0.0001

PHE 106 VAL 107 0.0002

VAL 107 GLU 108 0.0042

GLU 108 THR 109 0.0000

THR 109 PHE 110 -0.0003

PHE 110 ALA 111 -0.0305

ALA 111 ARG 112 -0.0001

ARG 112 VAL 113 -0.0002

VAL 113 LEU 114 -0.0376

LEU 114 GLY 115 0.0000

GLY 115 ASP 116 -0.0003

ASP 116 PRO 117 -0.0060

PRO 117 ALA 118 0.0004

ALA 118 LEU 119 -0.0001

LEU 119 PRO 120 0.0087

PRO 120 HIS 121 0.0002

HIS 121 LEU 122 0.0002

LEU 122 PHE 123 0.0172

PHE 123 PHE 124 0.0001

PHE 124 VAL 125 -0.0002

VAL 125 GLU 126 0.0288

GLU 126 GLY 127 -0.0002

GLY 127 GLY 128 0.0001

GLY 128 ALA 129 0.0290

ALA 129 LEU 130 -0.0001

LEU 130 ALA 131 0.0001

ALA 131 VAL 132 0.0086

VAL 132 GLU 133 0.0004

GLU 133 ASN 134 -0.0000

ASN 134 ALA 135 0.0075

ALA 135 LEU 136 -0.0002

LEU 136 LYS 137 0.0004

LYS 137 ALA 138 -0.0059

ALA 138 ALA 139 -0.0001

ALA 139 PHE 140 0.0004

PHE 140 ASP 141 -0.0173

ASP 141 TRP 142 0.0000

TRP 142 LYS 143 -0.0004

LYS 143 SER 144 0.0068

SER 144 ARG 145 0.0004

ARG 145 HIS 146 0.0003

HIS 146 ASN 147 -0.0077

ASN 147 GLN 148 0.0001

GLN 148 ALA 149 -0.0000

ALA 149 HIS 150 0.0018

HIS 150 GLY 151 0.0003

GLY 151 ILE 152 0.0002

ILE 152 ASP 153 -0.0008

ASP 153 PRO 154 0.0000

PRO 154 ALA 155 0.0000

ALA 155 LEU 156 0.0017

LEU 156 GLY 157 0.0000

GLY 157 THR 158 -0.0002

THR 158 GLN 159 -0.0045

GLN 159 VAL 160 0.0001

VAL 160 LEU 161 0.0001

LEU 161 HIS 162 0.0113

HIS 162 LEU 163 -0.0003

LEU 163 ARG 164 0.0004

ARG 164 GLY 165 0.0255

GLY 165 ALA 166 -0.0001

ALA 166 PHE 167 0.0001

PHE 167 HIS 168 -0.0334

HIS 168 GLY 169 0.0003

GLY 169 ARG 170 -0.0002

ARG 170 SER 171 -0.0257

SER 171 GLY 172 0.0001

GLY 172 TYR 173 0.0000

TYR 173 THR 174 -0.0095

THR 174 LEU 175 0.0001

LEU 175 SER 176 -0.0002

SER 176 LEU 177 0.0018

LEU 177 THR 178 0.0000

THR 178 ASN 179 0.0001

ASN 179 THR 180 0.0174

THR 180 LYS 181 -0.0001

LYS 181 PRO 182 0.0001

PRO 182 THR 183 0.0195

THR 183 ILE 184 -0.0002

ILE 184 THR 185 0.0000

THR 185 ALA 186 -0.0006

ALA 186 ARG 187 0.0004

ARG 187 PHE 188 0.0001

PHE 188 PRO 189 -0.0253

PRO 189 LYS 190 0.0001

LYS 190 PHE 191 -0.0000

PHE 191 ASP 192 0.0064

ASP 192 TRP 193 0.0003

TRP 193 PRO 194 -0.0004

PRO 194 ARG 195 0.0033

ARG 195 ILE 196 -0.0004

ILE 196 ASP 197 0.0000

ASP 197 ALA 198 0.0033

ALA 198 PRO 199 -0.0001

PRO 199 TYR 200 0.0001

TYR 200 MET 201 0.0082

MET 201 ARG 202 0.0001

ARG 202 PRO 203 -0.0003

PRO 203 GLY 204 0.0123

GLY 204 LEU 205 -0.0000

LEU 205 ASP 206 0.0000

ASP 206 GLU 207 0.0095

GLU 207 PRO 208 -0.0005

PRO 208 ALA 209 -0.0000

ALA 209 MET 210 -0.0119

MET 210 ALA 211 -0.0001

ALA 211 ALA 212 0.0002

ALA 212 LEU 213 -0.0093

LEU 213 GLU 214 -0.0002

GLU 214 ALA 215 -0.0001

ALA 215 GLU 216 -0.0232

GLU 216 ALA 217 0.0000

ALA 217 LEU 218 0.0002

LEU 218 ARG 219 -0.0123

ARG 219 GLN 220 -0.0003

GLN 220 ALA 221 -0.0003

ALA 221 ARG 222 0.0089

ARG 222 ALA 223 -0.0002

ALA 223 ALA 224 0.0001

ALA 224 PHE 225 0.0035

PHE 225 GLU 226 0.0001

GLU 226 THR 227 0.0001

THR 227 ARG 228 0.0067

ARG 228 PRO 229 -0.0001

PRO 229 HIS 230 -0.0001

HIS 230 ASP 231 -0.0023

ASP 231 ILE 232 -0.0002

ILE 232 ALA 233 -0.0000

ALA 233 CYS 234 0.0060

CYS 234 PHE 235 0.0003

PHE 235 VAL 236 -0.0001

VAL 236 ALA 237 0.0055

ALA 237 GLU 238 0.0000

GLU 238 PRO 239 -0.0001

PRO 239 ILE 240 0.0227

ILE 240 GLN 241 0.0000

GLN 241 GLY 242 -0.0001

GLY 242 GLU 243 -0.0026

GLU 243 GLY 244 0.0003

GLY 244 GLY 245 0.0001

GLY 245 ASP 246 0.0052

ASP 246 ARG 247 -0.0000

ARG 247 HIS 248 0.0000

HIS 248 PHE 249 0.0621

PHE 249 ARG 250 0.0000

ARG 250 PRO 251 -0.0001

PRO 251 GLU 252 -0.0057

GLU 252 PHE 253 0.0003

PHE 253 PHE 254 0.0001

PHE 254 ALA 255 0.0175

ALA 255 ALA 256 -0.0003

ALA 256 MET 257 0.0004

MET 257 ARG 258 0.0219

ARG 258 GLU 259 0.0000

GLU 259 LEU 260 0.0001

LEU 260 CYS 261 0.0135

CYS 261 ASP 262 0.0000

ASP 262 GLU 263 0.0001

GLU 263 PHE 264 0.0018

PHE 264 ASP 265 -0.0001

ASP 265 ALA 266 0.0002

ALA 266 LEU 267 -0.0131

LEU 267 LEU 268 0.0002

LEU 268 ILE 269 0.0001

ILE 269 PHE 270 -0.0051

PHE 270 ASP 271 -0.0001

ASP 271 GLU 272 -0.0000

GLU 272 VAL 273 -0.0184

VAL 273 GLN 274 -0.0002

GLN 274 THR 275 0.0001

THR 275 GLY 276 0.0027

GLY 276 CYS 277 0.0003

CYS 277 GLY 278 -0.0001

GLY 278 LEU 279 0.0114

LEU 279 THR 280 0.0001

THR 280 GLY 281 -0.0004

GLY 281 THR 282 0.0340

THR 282 ALA 283 0.0003

ALA 283 TRP 284 0.0000

TRP 284 ALA 285 -0.0186

ALA 285 TYR 286 -0.0002

TYR 286 GLN 287 -0.0002

GLN 287 GLN 288 0.0321

GLN 288 LEU 289 0.0000

LEU 289 ASP 290 0.0002

ASP 290 VAL 291 0.0135

VAL 291 ALA 292 -0.0005

ALA 292 PRO 293 -0.0002

PRO 293 ASP 294 0.0203

ASP 294 ILE 295 0.0001

ILE 295 VAL 296 0.0001

VAL 296 ALA 297 -0.0036

ALA 297 PHE 298 0.0001

PHE 298 GLY 299 0.0001

GLY 299 LYS 300 -0.0498

LYS 300 LYS 301 -0.0001

LYS 301 THR 302 -0.0001

THR 302 GLN 303 -0.0121

GLN 303 VAL 304 -0.0001

VAL 304 CYS 305 -0.0000

CYS 305 GLY 306 0.0093

GLY 306 VAL 307 -0.0001

VAL 307 MET 308 -0.0002

MET 308 ALA 309 -0.0253

ALA 309 GLY 310 0.0003

GLY 310 ARG 311 0.0000

ARG 311 ARG 312 -0.0282

ARG 312 VAL 313 0.0001

VAL 313 ASP 314 -0.0003

ASP 314 GLU 315 -0.0306

GLU 315 VAL 316 0.0002

VAL 316 ALA 317 0.0002

ALA 317 ASP 318 0.0091

ASP 318 ASN 319 -0.0001

ASN 319 VAL 320 0.0003

VAL 320 PHE 321 -0.0086

PHE 321 ALA 322 0.0003

ALA 322 VAL 323 -0.0001

VAL 323 PRO 324 0.0282

PRO 324 SER 325 -0.0001

SER 325 ARG 326 0.0004

ARG 326 LEU 327 0.0174

LEU 327 ASN 328 -0.0001

ASN 328 SER 329 0.0002

SER 329 THR 330 0.0411

THR 330 TRP 331 -0.0001

TRP 331 GLY 332 -0.0001

GLY 332 GLY 333 0.0023

GLY 333 ASN 334 0.0002

ASN 334 LEU 335 -0.0002

LEU 335 THR 336 -0.0007

THR 336 ASP 337 -0.0004

ASP 337 MET 338 0.0000

MET 338 VAL 339 0.0078

VAL 339 ARG 340 -0.0002

ARG 340 ALA 341 0.0002

ALA 341 ARG 342 -0.0029

ARG 342 ARG 343 -0.0003

ARG 343 ILE 344 0.0002

ILE 344 LEU 345 -0.0345

LEU 345 GLU 346 -0.0001

GLU 346 VAL 347 0.0003

VAL 347 ILE 348 0.0139

ILE 348 GLU 349 0.0000

GLU 349 ALA 350 -0.0000

ALA 350 GLU 351 0.0225

GLU 351 GLY 352 0.0002

GLY 352 LEU 353 -0.0002

LEU 353 PHE 354 -0.0354

PHE 354 GLU 355 0.0006

GLU 355 ARG 356 -0.0002

ARG 356 ALA 357 -0.0064

ALA 357 VAL 358 0.0000

VAL 358 GLN 359 -0.0003

GLN 359 HIS 360 0.0078

HIS 360 GLY 361 -0.0000

GLY 361 LYS 362 -0.0001

LYS 362 TYR 363 0.0236

TYR 363 LEU 364 -0.0003

LEU 364 ARG 365 -0.0002

ARG 365 ALA 366 0.0022

ALA 366 ARG 367 0.0002

ARG 367 LEU 368 0.0000

LEU 368 ASP 369 -0.0155

ASP 369 GLU 370 0.0001

GLU 370 LEU 371 -0.0003

LEU 371 ALA 372 -0.0027

ALA 372 ALA 373 -0.0002

ALA 373 ASP 374 -0.0001

ASP 374 PHE 375 -0.0038

PHE 375 PRO 376 -0.0002

PRO 376 ALA 377 0.0001

ALA 377 VAL 378 0.0007

VAL 378 VAL 379 0.0003

VAL 379 LEU 380 -0.0002

LEU 380 ASP 381 0.0657

ASP 381 PRO 382 0.0001

PRO 382 ARG 383 -0.0000

ARG 383 GLY 384 0.0671

GLY 384 ARG 385 0.0002

ARG 385 GLY 386 -0.0004

GLY 386 LEU 387 -0.0495

LEU 387 MET 388 0.0001

MET 388 CYS 389 0.0002

CYS 389 ALA 390 0.0076

ALA 390 PHE 391 0.0002

PHE 391 SER 392 -0.0004

SER 392 LEU 393 0.0392

LEU 393 PRO 394 -0.0003

PRO 394 THR 395 -0.0001

THR 395 THR 396 0.0018

THR 396 ALA 397 -0.0004

ALA 397 ASP 398 0.0004

ASP 398 ARG 399 -0.0170

ARG 399 ASP 400 0.0002

ASP 400 GLU 401 0.0000

GLU 401 LEU 402 -0.0083

LEU 402 ILE 403 -0.0003

ILE 403 ARG 404 0.0001

ARG 404 GLN 405 0.0042

GLN 405 LEU 406 -0.0000

LEU 406 TRP 407 0.0001

TRP 407 GLN 408 -0.0383

GLN 408 ARG 409 -0.0000

ARG 409 ALA 410 -0.0002

ALA 410 VAL 411 0.0466

VAL 411 ILE 412 0.0004

ILE 412 VAL 413 0.0001

VAL 413 LEU 414 0.0451

LEU 414 PRO 415 0.0000

PRO 415 ALA 416 -0.0001

ALA 416 GLY 417 0.0314

GLY 417 ALA 418 -0.0001

ALA 418 ASP 419 0.0002

ASP 419 THR 420 -0.0075

THR 420 VAL 421 -0.0000

VAL 421 ARG 422 -0.0002

ARG 422 PHE 423 -0.0067

PHE 423 ARG 424 -0.0001

ARG 424 PRO 425 -0.0000

PRO 425 PRO 426 -0.0029

PRO 426 LEU 427 0.0003

LEU 427 THR 428 0.0001

THR 428 VAL 429 -0.0166

VAL 429 SER 430 -0.0001

SER 430 THR 431 -0.0003

THR 431 ALA 432 0.0015

ALA 432 GLU 433 -0.0003

GLU 433 ILE 434 0.0003

ILE 434 ASP 435 -0.0081

ASP 435 ALA 436 -0.0002

ALA 436 ALA 437 -0.0001

ALA 437 ILE 438 -0.0098

ILE 438 ALA 439 0.0002

ALA 439 ALA 440 0.0001

ALA 440 VAL 441 -0.0031

VAL 441 ARG 442 0.0001

ARG 442 SER 443 0.0005

SER 443 ALA 444 -0.0012

ALA 444 LEU 445 -0.0003

LEU 445 PRO 446 0.0004

PRO 446 VAL 447 0.0000

VAL 447 VAL 448 0.0001

VAL 448 THR 449 -0.0000

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.

*** TRANSFERASE 31-MAR-06 2CJD ***

CA strain for 220405004109145553

--- normal mode 9 ---

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

* TRANSFERASE 31-MAR-06 2CJD *