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

* 2V7Y *

CA strain for 240228055913921343

--- 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
MET 1 SER 2 0.0003

SER 2 LYS 3 0.0001

LYS 3 ILE 4 -0.0040

ILE 4 ILE 5 0.0004

ILE 5 GLY 6 0.0000

GLY 6 ILE 7 -0.0000

ILE 7 ASP 8 -0.0003

ASP 8 LEU 9 -0.0001

LEU 9 GLY 10 -0.0006

GLY 10 THR 11 -0.0001

THR 11 THR 12 -0.0001

THR 12 ASN 13 -0.0001

ASN 13 SER 14 0.0003

SER 14 CYS 15 -0.0000

CYS 15 VAL 16 -0.0001

VAL 16 ALA 17 -0.0000

ALA 17 VAL 18 -0.0001

VAL 18 LEU 19 -0.0020

LEU 19 GLU 20 -0.0003

GLU 20 GLY 21 0.0002

GLY 21 GLY 22 -0.0021

GLY 22 GLU 23 -0.0004

GLU 23 VAL 24 0.0003

VAL 24 LYS 25 -0.0107

LYS 25 VAL 26 -0.0001

VAL 26 ILE 27 -0.0000

ILE 27 PRO 28 -0.0064

PRO 28 ASN 29 0.0001

ASN 29 PRO 30 -0.0002

PRO 30 GLU 31 0.0070

GLU 31 GLY 32 0.0003

GLY 32 ASN 33 0.0001

ASN 33 ARG 34 -0.0016

ARG 34 THR 35 0.0001

THR 35 THR 36 -0.0001

THR 36 PRO 37 -0.0011

PRO 37 SER 38 -0.0004

SER 38 VAL 39 -0.0001

VAL 39 VAL 40 -0.0084

VAL 40 ALA 41 -0.0002

ALA 41 PHE 42 -0.0003

PHE 42 LYS 43 -0.0017

LYS 43 ASN 44 0.0002

ASN 44 GLY 45 -0.0001

GLY 45 GLU 46 -0.0013

GLU 46 ARG 47 0.0004

ARG 47 LEU 48 0.0001

LEU 48 VAL 49 -0.0005

VAL 49 GLY 50 0.0000

GLY 50 GLU 51 -0.0003

GLU 51 VAL 52 -0.0061

VAL 52 ALA 53 -0.0000

ALA 53 LYS 54 0.0000

LYS 54 ARG 55 0.0001

ARG 55 GLN 56 -0.0000

GLN 56 ALA 57 -0.0000

ALA 57 ILE 58 0.0060

ILE 58 THR 59 0.0000

THR 59 ASN 60 -0.0002

ASN 60 PRO 61 0.0044

PRO 61 ASN 62 -0.0003

ASN 62 THR 63 0.0000

THR 63 ILE 64 0.0005

ILE 64 ILE 65 -0.0004

ILE 65 SER 66 -0.0002

SER 66 ILE 67 0.0040

ILE 67 LYS 68 0.0001

LYS 68 ARG 69 0.0003

ARG 69 HIS 70 0.0025

HIS 70 MET 71 0.0003

MET 71 GLY 72 -0.0002

GLY 72 THR 73 -0.0026

THR 73 ASP 74 -0.0004

ASP 74 TYR 75 0.0002

TYR 75 LYS 76 -0.0048

LYS 76 VAL 77 -0.0003

VAL 77 GLU 78 -0.0001

GLU 78 ILE 79 -0.0046

ILE 79 GLU 80 0.0003

GLU 80 GLY 81 -0.0003

GLY 81 LYS 82 0.0016

LYS 82 GLN 83 -0.0000

GLN 83 TYR 84 -0.0001

TYR 84 THR 85 0.0061

THR 85 PRO 86 0.0004

PRO 86 GLN 87 -0.0001

GLN 87 GLU 88 0.0038

GLU 88 ILE 89 -0.0002

ILE 89 SER 90 0.0003

SER 90 ALA 91 0.0034

ALA 91 ILE 92 -0.0000

ILE 92 ILE 93 0.0002

ILE 93 LEU 94 0.0143

LEU 94 GLN 95 0.0000

GLN 95 TYR 96 -0.0004

TYR 96 LEU 97 0.0070

LEU 97 LYS 98 0.0004

LYS 98 SER 99 0.0002

SER 99 TYR 100 -0.0044

TYR 100 ALA 101 -0.0001

ALA 101 GLU 102 -0.0002

GLU 102 ASP 103 0.0003

ASP 103 TYR 104 0.0000

TYR 104 LEU 105 -0.0001

LEU 105 GLY 106 -0.0075

GLY 106 GLU 107 -0.0001

GLU 107 PRO 108 -0.0002

PRO 108 VAL 109 -0.0134

VAL 109 THR 110 0.0000

THR 110 ARG 111 -0.0000

ARG 111 ALA 112 -0.0208

ALA 112 VAL 113 -0.0001

VAL 113 ILE 114 0.0004

ILE 114 THR 115 -0.0065

THR 115 VAL 116 -0.0002

VAL 116 PRO 117 0.0003

PRO 117 ALA 118 0.0050

ALA 118 TYR 119 -0.0000

TYR 119 PHE 120 -0.0004

PHE 120 ASN 121 0.0012

ASN 121 ASP 122 -0.0003

ASP 122 ALA 123 0.0003

ALA 123 GLN 124 0.0009

GLN 124 ARG 125 0.0003

ARG 125 GLN 126 -0.0001

GLN 126 ALA 127 -0.0024

ALA 127 THR 128 0.0002

THR 128 LYS 129 0.0001

LYS 129 ASP 130 0.0034

ASP 130 ALA 131 -0.0000

ALA 131 GLY 132 0.0000

GLY 132 ARG 133 -0.0012

ARG 133 ILE 134 0.0003

ILE 134 ALA 135 0.0003

ALA 135 GLY 136 0.0257

GLY 136 LEU 137 0.0001

LEU 137 GLU 138 -0.0003

GLU 138 VAL 139 -0.0120

VAL 139 GLU 140 0.0001

GLU 140 ARG 141 0.0003

ARG 141 ILE 142 -0.0102

ILE 142 ILE 143 0.0001

ILE 143 ASN 144 0.0001

ASN 144 GLU 145 -0.0065

GLU 145 PRO 146 -0.0000

PRO 146 THR 147 0.0005

THR 147 ALA 148 -0.0060

ALA 148 ALA 149 0.0003

ALA 149 ALA 150 -0.0001

ALA 150 LEU 151 -0.0189

LEU 151 ALA 152 0.0004

ALA 152 TYR 153 -0.0001

TYR 153 GLY 154 0.0006

GLY 154 LEU 155 -0.0000

LEU 155 ASP 156 0.0002

ASP 156 LYS 157 0.0028

LYS 157 GLU 158 0.0002

GLU 158 GLU 159 -0.0003

GLU 159 ASP 160 -0.0003

ASP 160 GLN 161 0.0004

GLN 161 THR 162 -0.0002

THR 162 ILE 163 0.0007

ILE 163 LEU 164 -0.0002

LEU 164 VAL 165 -0.0001

VAL 165 TYR 166 -0.0077

TYR 166 ASP 167 -0.0000

ASP 167 LEU 168 0.0004

LEU 168 GLY 169 0.0049

GLY 169 GLY 170 -0.0002

GLY 170 GLY 171 -0.0001

GLY 171 THR 172 0.0009

THR 172 PHE 173 0.0001

PHE 173 ASP 174 0.0000

ASP 174 VAL 175 0.0039

VAL 175 SER 176 -0.0000

SER 176 ILE 177 0.0000

ILE 177 LEU 178 -0.0009

LEU 178 GLU 179 -0.0001

GLU 179 LEU 180 -0.0000

LEU 180 GLY 181 0.0027

GLY 181 ASP 182 0.0001

ASP 182 GLY 183 -0.0002

GLY 183 VAL 184 0.0028

VAL 184 PHE 185 0.0001

PHE 185 GLU 186 0.0001

GLU 186 VAL 187 0.0004

VAL 187 LYS 188 0.0000

LYS 188 ALA 189 0.0004

ALA 189 THR 190 0.0034

THR 190 ALA 191 0.0003

ALA 191 GLY 192 0.0004

GLY 192 ASP 193 0.0056

ASP 193 ASN 194 0.0003

ASN 194 HIS 195 0.0001

HIS 195 LEU 196 -0.0008

LEU 196 GLY 197 0.0001

GLY 197 GLY 198 0.0000

GLY 198 ASP 199 -0.0068

ASP 199 ASP 200 -0.0002

ASP 200 PHE 201 0.0001

PHE 201 ASP 202 -0.0031

ASP 202 GLN 203 0.0002

GLN 203 VAL 204 0.0000

VAL 204 ILE 205 -0.0018

ILE 205 ILE 206 -0.0001

ILE 206 ASP 207 0.0003

ASP 207 TYR 208 0.0050

TYR 208 LEU 209 -0.0002

LEU 209 VAL 210 -0.0003

VAL 210 ASN 211 0.0063

ASN 211 GLN 212 0.0001

GLN 212 PHE 213 0.0000

PHE 213 LYS 214 0.0003

LYS 214 GLN 215 0.0003

GLN 215 GLU 216 -0.0001

GLU 216 HIS 217 -0.0059

HIS 217 GLY 218 -0.0001

GLY 218 ILE 219 0.0002

ILE 219 ASP 220 0.0043

ASP 220 LEU 221 0.0002

LEU 221 SER 222 -0.0001

SER 222 LYS 223 -0.0052

LYS 223 ASP 224 -0.0000

ASP 224 LYS 225 0.0003

LYS 225 MET 226 0.0007

MET 226 ALA 227 -0.0000

ALA 227 LEU 228 -0.0001

LEU 228 GLN 229 0.0066

GLN 229 ARG 230 0.0004

ARG 230 LEU 231 -0.0001

LEU 231 LYS 232 -0.0008

LYS 232 ASP 233 -0.0000

ASP 233 ALA 234 -0.0003

ALA 234 ALA 235 0.0032

ALA 235 GLU 236 0.0004

GLU 236 LYS 237 0.0001

LYS 237 ALA 238 0.0044

ALA 238 LYS 239 -0.0003

LYS 239 LYS 240 0.0003

LYS 240 GLU 241 0.0012

GLU 241 LEU 242 -0.0002

LEU 242 SER 243 0.0000

SER 243 GLY 244 -0.0011

GLY 244 VAL 245 0.0001

VAL 245 THR 246 -0.0001

THR 246 GLN 247 -0.0017

GLN 247 THR 248 0.0002

THR 248 GLN 249 -0.0004

GLN 249 ILE 250 0.0035

ILE 250 SER 251 0.0003

SER 251 LEU 252 -0.0002

LEU 252 PRO 253 -0.0006

PRO 253 PHE 254 0.0000

PHE 254 ILE 255 0.0001

ILE 255 SER 256 0.0147

SER 256 ALA 257 0.0001

ALA 257 ASN 258 -0.0004

ASN 258 GLU 259 0.0115

GLU 259 ASN 260 0.0001

ASN 260 GLY 261 0.0002

GLY 261 PRO 262 0.0025

PRO 262 LEU 263 0.0001

LEU 263 HIS 264 0.0001

HIS 264 LEU 265 -0.0146

LEU 265 GLU 266 0.0003

GLU 266 MET 267 -0.0000

MET 267 THR 268 -0.0071

THR 268 LEU 269 0.0002

LEU 269 THR 270 0.0001

THR 270 ARG 271 -0.0060

ARG 271 ALA 272 -0.0001

ALA 272 LYS 273 0.0000

LYS 273 PHE 274 -0.0001

PHE 274 GLU 275 0.0001

GLU 275 GLU 276 0.0002

GLU 276 LEU 277 0.0006

LEU 277 SER 278 -0.0000

SER 278 ALA 279 0.0001

ALA 279 HIS 280 0.0019

HIS 280 LEU 281 -0.0000

LEU 281 VAL 282 -0.0000

VAL 282 GLU 283 0.0018

GLU 283 ARG 284 0.0000

ARG 284 THR 285 -0.0001

THR 285 MET 286 0.0015

MET 286 GLY 287 -0.0003

GLY 287 PRO 288 0.0002

PRO 288 VAL 289 0.0021

VAL 289 ARG 290 -0.0001

ARG 290 GLN 291 -0.0002

GLN 291 ALA 292 -0.0008

ALA 292 LEU 293 0.0000

LEU 293 GLN 294 0.0001

GLN 294 ASP 295 -0.0008

ASP 295 ALA 296 0.0003

ALA 296 GLY 297 0.0000

GLY 297 LEU 298 -0.0001

LEU 298 THR 299 -0.0001

THR 299 PRO 300 0.0004

PRO 300 ALA 301 0.0014

ALA 301 ASP 302 0.0003

ASP 302 ILE 303 0.0002

ILE 303 ASP 304 -0.0010

ASP 304 LYS 305 0.0002

LYS 305 VAL 306 -0.0001

VAL 306 ILE 307 -0.0020

ILE 307 LEU 308 -0.0004

LEU 308 VAL 309 -0.0000

VAL 309 GLY 310 -0.0011

GLY 310 GLY 311 -0.0002

GLY 311 SER 312 0.0003

SER 312 THR 313 -0.0000

THR 313 ARG 314 -0.0002

ARG 314 ILE 315 -0.0002

ILE 315 PRO 316 -0.0016

PRO 316 ALA 317 -0.0003

ALA 317 VAL 318 -0.0003

VAL 318 GLN 319 -0.0059

GLN 319 GLU 320 -0.0001

GLU 320 ALA 321 -0.0001

ALA 321 ILE 322 -0.0027

ILE 322 LYS 323 -0.0005

LYS 323 ARG 324 0.0001

ARG 324 GLU 325 -0.0004

GLU 325 LEU 326 0.0003

LEU 326 GLY 327 0.0001

GLY 327 LYS 328 -0.0002

LYS 328 GLU 329 0.0004

GLU 329 PRO 330 -0.0003

PRO 330 HIS 331 -0.0043

HIS 331 LYS 332 0.0001

LYS 332 GLY 333 0.0003

GLY 333 VAL 334 0.0082

VAL 334 ASN 335 -0.0004

ASN 335 PRO 336 0.0001

PRO 336 ASP 337 0.0112

ASP 337 GLU 338 -0.0000

GLU 338 VAL 339 0.0001

VAL 339 VAL 340 0.0024

VAL 340 ALA 341 -0.0001

ALA 341 ILE 342 -0.0001

ILE 342 GLY 343 -0.0042

GLY 343 ALA 344 -0.0000

ALA 344 ALA 345 -0.0003

ALA 345 ILE 346 -0.0070

ILE 346 GLN 347 0.0001

GLN 347 GLY 348 0.0001

GLY 348 GLY 349 -0.0223

GLY 349 VAL 350 0.0000

VAL 350 ILE 351 0.0004

ILE 351 ALA 352 -0.0772

ALA 352 GLY 353 0.0002

GLY 353 GLU 354 -0.0002

GLU 354 VAL 355 -0.1120

VAL 355 LYS 356 0.0002

LYS 356 ASP 357 -0.0001

ASP 357 VAL 358 -0.1520

VAL 358 VAL 359 0.0000

VAL 359 LEU 360 0.0002

LEU 360 LEU 361 -0.3026

LEU 361 ASP 362 -0.0000

ASP 362 VAL 363 -0.0003

VAL 363 THR 364 -0.1544

THR 364 PRO 365 -0.0000

PRO 365 LEU 366 -0.0003

LEU 366 SER 367 0.0059

SER 367 LEU 368 0.0003

LEU 368 GLY 369 0.0004

GLY 369 ILE 370 -0.1750

ILE 370 GLU 371 -0.0003

GLU 371 THR 372 0.0002

THR 372 MET 373 -0.0614

MET 373 GLY 374 -0.0000

GLY 374 GLY 375 -0.0001

GLY 375 VAL 376 -0.0661

VAL 376 PHE 377 -0.0000

PHE 377 THR 378 -0.0000

THR 378 LYS 379 0.0413

LYS 379 LEU 380 0.0001

LEU 380 ILE 381 -0.0001

ILE 381 GLU 382 -0.0795

GLU 382 ARG 383 -0.0004

ARG 383 ASN 384 -0.0000

ASN 384 THR 385 0.1379

THR 385 THR 386 0.0000

THR 386 ILE 387 0.0003

ILE 387 PRO 388 0.0834

PRO 388 THR 389 0.0000

THR 389 SER 390 -0.0000

SER 390 LYS 391 0.0131

LYS 391 SER 392 0.0001

SER 392 GLN 393 0.0001

GLN 393 VAL 394 -0.0889

VAL 394 PHE 395 -0.0000

PHE 395 THR 396 -0.0000

THR 396 THR 397 -0.1390

THR 397 ALA 398 0.0001

ALA 398 ALA 399 -0.0001

ALA 399 ASP 400 0.1429

ASP 400 ASN 401 0.0001

ASN 401 GLN 402 0.0002

GLN 402 THR 403 0.0503

THR 403 THR 404 -0.0002

THR 404 VAL 405 -0.0000

VAL 405 ASP 406 0.0234

ASP 406 ILE 407 -0.0000

ILE 407 HIS 408 -0.0001

HIS 408 VAL 409 -0.1906

VAL 409 LEU 410 0.0000

LEU 410 GLN 411 0.0004

GLN 411 GLY 412 -0.1494

GLY 412 GLU 413 0.0003

GLU 413 ARG 414 0.0001

ARG 414 PRO 415 0.0643

PRO 415 MET 416 -0.0001

MET 416 ALA 417 0.0001

ALA 417 ALA 418 -0.0096

ALA 418 ASP 419 0.0002

ASP 419 ASN 420 0.0000

ASN 420 LYS 421 -0.0652

LYS 421 SER 422 -0.0002

SER 422 LEU 423 -0.0001

LEU 423 GLY 424 -0.1959

GLY 424 ARG 425 0.0000

ARG 425 PHE 426 0.0001

PHE 426 GLN 427 -0.0526

GLN 427 LEU 428 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: April 25th, 2023.

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

*** 2V7Y ***

CA strain for 240228055913921343

--- normal mode 15 ---

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

* 2V7Y *