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

* 2V7Y *

CA strain for 240228055913921343

--- normal mode 11 ---

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 -0.0001

SER 2 LYS 3 -0.0001

LYS 3 ILE 4 -0.0003

ILE 4 ILE 5 -0.0002

ILE 5 GLY 6 0.0003

GLY 6 ILE 7 0.0026

ILE 7 ASP 8 0.0002

ASP 8 LEU 9 0.0002

LEU 9 GLY 10 -0.0002

GLY 10 THR 11 -0.0001

THR 11 THR 12 0.0000

THR 12 ASN 13 0.0026

ASN 13 SER 14 0.0000

SER 14 CYS 15 -0.0002

CYS 15 VAL 16 0.0032

VAL 16 ALA 17 0.0001

ALA 17 VAL 18 -0.0003

VAL 18 LEU 19 0.0028

LEU 19 GLU 20 -0.0002

GLU 20 GLY 21 0.0000

GLY 21 GLY 22 0.0001

GLY 22 GLU 23 0.0005

GLU 23 VAL 24 -0.0003

VAL 24 LYS 25 0.0016

LYS 25 VAL 26 0.0001

VAL 26 ILE 27 -0.0001

ILE 27 PRO 28 0.0021

PRO 28 ASN 29 0.0002

ASN 29 PRO 30 -0.0002

PRO 30 GLU 31 0.0014

GLU 31 GLY 32 0.0001

GLY 32 ASN 33 -0.0001

ASN 33 ARG 34 -0.0007

ARG 34 THR 35 -0.0002

THR 35 THR 36 0.0001

THR 36 PRO 37 0.0027

PRO 37 SER 38 0.0003

SER 38 VAL 39 -0.0001

VAL 39 VAL 40 0.0011

VAL 40 ALA 41 -0.0002

ALA 41 PHE 42 0.0002

PHE 42 LYS 43 0.0005

LYS 43 ASN 44 0.0003

ASN 44 GLY 45 -0.0002

GLY 45 GLU 46 -0.0005

GLU 46 ARG 47 -0.0003

ARG 47 LEU 48 -0.0003

LEU 48 VAL 49 -0.0003

VAL 49 GLY 50 0.0001

GLY 50 GLU 51 0.0001

GLU 51 VAL 52 0.0006

VAL 52 ALA 53 0.0003

ALA 53 LYS 54 0.0002

LYS 54 ARG 55 -0.0018

ARG 55 GLN 56 0.0002

GLN 56 ALA 57 -0.0003

ALA 57 ILE 58 -0.0010

ILE 58 THR 59 -0.0001

THR 59 ASN 60 -0.0004

ASN 60 PRO 61 -0.0019

PRO 61 ASN 62 0.0000

ASN 62 THR 63 0.0001

THR 63 ILE 64 0.0002

ILE 64 ILE 65 -0.0000

ILE 65 SER 66 -0.0001

SER 66 ILE 67 -0.0013

ILE 67 LYS 68 -0.0004

LYS 68 ARG 69 -0.0000

ARG 69 HIS 70 -0.0015

HIS 70 MET 71 0.0000

MET 71 GLY 72 -0.0002

GLY 72 THR 73 0.0005

THR 73 ASP 74 -0.0002

ASP 74 TYR 75 -0.0003

TYR 75 LYS 76 0.0005

LYS 76 VAL 77 -0.0003

VAL 77 GLU 78 0.0002

GLU 78 ILE 79 0.0001

ILE 79 GLU 80 -0.0001

GLU 80 GLY 81 0.0003

GLY 81 LYS 82 -0.0003

LYS 82 GLN 83 -0.0003

GLN 83 TYR 84 0.0003

TYR 84 THR 85 -0.0007

THR 85 PRO 86 -0.0001

PRO 86 GLN 87 0.0001

GLN 87 GLU 88 0.0004

GLU 88 ILE 89 0.0000

ILE 89 SER 90 -0.0003

SER 90 ALA 91 0.0004

ALA 91 ILE 92 -0.0001

ILE 92 ILE 93 -0.0001

ILE 93 LEU 94 -0.0001

LEU 94 GLN 95 -0.0001

GLN 95 TYR 96 0.0001

TYR 96 LEU 97 0.0008

LEU 97 LYS 98 -0.0001

LYS 98 SER 99 0.0001

SER 99 TYR 100 -0.0010

TYR 100 ALA 101 -0.0003

ALA 101 GLU 102 -0.0004

GLU 102 ASP 103 -0.0008

ASP 103 TYR 104 0.0001

TYR 104 LEU 105 0.0001

LEU 105 GLY 106 -0.0022

GLY 106 GLU 107 -0.0001

GLU 107 PRO 108 0.0000

PRO 108 VAL 109 -0.0004

VAL 109 THR 110 -0.0003

THR 110 ARG 111 0.0002

ARG 111 ALA 112 -0.0015

ALA 112 VAL 113 0.0001

VAL 113 ILE 114 0.0000

ILE 114 THR 115 -0.0009

THR 115 VAL 116 -0.0001

VAL 116 PRO 117 -0.0001

PRO 117 ALA 118 0.0011

ALA 118 TYR 119 0.0000

TYR 119 PHE 120 -0.0001

PHE 120 ASN 121 -0.0003

ASN 121 ASP 122 0.0001

ASP 122 ALA 123 -0.0000

ALA 123 GLN 124 -0.0001

GLN 124 ARG 125 0.0001

ARG 125 GLN 126 0.0001

GLN 126 ALA 127 0.0014

ALA 127 THR 128 -0.0001

THR 128 LYS 129 0.0002

LYS 129 ASP 130 0.0001

ASP 130 ALA 131 0.0000

ALA 131 GLY 132 -0.0001

GLY 132 ARG 133 -0.0004

ARG 133 ILE 134 -0.0002

ILE 134 ALA 135 -0.0000

ALA 135 GLY 136 0.0001

GLY 136 LEU 137 -0.0000

LEU 137 GLU 138 0.0001

GLU 138 VAL 139 -0.0008

VAL 139 GLU 140 0.0002

GLU 140 ARG 141 0.0001

ARG 141 ILE 142 -0.0146

ILE 142 ILE 143 0.0005

ILE 143 ASN 144 -0.0002

ASN 144 GLU 145 -0.0026

GLU 145 PRO 146 0.0001

PRO 146 THR 147 0.0001

THR 147 ALA 148 -0.0015

ALA 148 ALA 149 -0.0002

ALA 149 ALA 150 -0.0001

ALA 150 LEU 151 -0.0005

LEU 151 ALA 152 -0.0000

ALA 152 TYR 153 -0.0001

TYR 153 GLY 154 -0.0014

GLY 154 LEU 155 0.0001

LEU 155 ASP 156 -0.0002

ASP 156 LYS 157 -0.0003

LYS 157 GLU 158 -0.0001

GLU 158 GLU 159 -0.0000

GLU 159 ASP 160 -0.0004

ASP 160 GLN 161 -0.0001

GLN 161 THR 162 0.0001

THR 162 ILE 163 -0.0000

ILE 163 LEU 164 0.0000

LEU 164 VAL 165 0.0000

VAL 165 TYR 166 0.0000

TYR 166 ASP 167 0.0001

ASP 167 LEU 168 -0.0003

LEU 168 GLY 169 -0.0003

GLY 169 GLY 170 -0.0001

GLY 170 GLY 171 0.0002

GLY 171 THR 172 -0.0003

THR 172 PHE 173 0.0002

PHE 173 ASP 174 -0.0002

ASP 174 VAL 175 0.0009

VAL 175 SER 176 0.0000

SER 176 ILE 177 -0.0004

ILE 177 LEU 178 0.0000

LEU 178 GLU 179 0.0001

GLU 179 LEU 180 -0.0001

LEU 180 GLY 181 -0.0000

GLY 181 ASP 182 0.0001

ASP 182 GLY 183 0.0002

GLY 183 VAL 184 0.0003

VAL 184 PHE 185 -0.0000

PHE 185 GLU 186 -0.0002

GLU 186 VAL 187 0.0000

VAL 187 LYS 188 -0.0002

LYS 188 ALA 189 0.0000

ALA 189 THR 190 0.0006

THR 190 ALA 191 0.0003

ALA 191 GLY 192 -0.0003

GLY 192 ASP 193 0.0001

ASP 193 ASN 194 -0.0001

ASN 194 HIS 195 -0.0003

HIS 195 LEU 196 -0.0006

LEU 196 GLY 197 0.0003

GLY 197 GLY 198 -0.0001

GLY 198 ASP 199 0.0005

ASP 199 ASP 200 0.0003

ASP 200 PHE 201 0.0001

PHE 201 ASP 202 0.0004

ASP 202 GLN 203 -0.0003

GLN 203 VAL 204 -0.0000

VAL 204 ILE 205 -0.0013

ILE 205 ILE 206 0.0001

ILE 206 ASP 207 0.0001

ASP 207 TYR 208 0.0008

TYR 208 LEU 209 -0.0003

LEU 209 VAL 210 -0.0001

VAL 210 ASN 211 0.0010

ASN 211 GLN 212 -0.0004

GLN 212 PHE 213 -0.0004

PHE 213 LYS 214 0.0008

LYS 214 GLN 215 -0.0003

GLN 215 GLU 216 0.0003

GLU 216 HIS 217 -0.0004

HIS 217 GLY 218 -0.0003

GLY 218 ILE 219 -0.0002

ILE 219 ASP 220 -0.0002

ASP 220 LEU 221 0.0004

LEU 221 SER 222 -0.0004

SER 222 LYS 223 0.0004

LYS 223 ASP 224 -0.0002

ASP 224 LYS 225 -0.0000

LYS 225 MET 226 -0.0014

MET 226 ALA 227 0.0001

ALA 227 LEU 228 -0.0003

LEU 228 GLN 229 0.0022

GLN 229 ARG 230 0.0000

ARG 230 LEU 231 0.0004

LEU 231 LYS 232 0.0003

LYS 232 ASP 233 -0.0004

ASP 233 ALA 234 0.0002

ALA 234 ALA 235 0.0004

ALA 235 GLU 236 0.0000

GLU 236 LYS 237 0.0002

LYS 237 ALA 238 -0.0014

ALA 238 LYS 239 0.0001

LYS 239 LYS 240 -0.0001

LYS 240 GLU 241 -0.0003

GLU 241 LEU 242 0.0000

LEU 242 SER 243 -0.0001

SER 243 GLY 244 0.0005

GLY 244 VAL 245 0.0001

VAL 245 THR 246 0.0003

THR 246 GLN 247 0.0005

GLN 247 THR 248 0.0002

THR 248 GLN 249 0.0001

GLN 249 ILE 250 -0.0010

ILE 250 SER 251 0.0001

SER 251 LEU 252 -0.0000

LEU 252 PRO 253 0.0006

PRO 253 PHE 254 0.0001

PHE 254 ILE 255 0.0001

ILE 255 SER 256 0.0002

SER 256 ALA 257 0.0001

ALA 257 ASN 258 -0.0001

ASN 258 GLU 259 -0.0006

GLU 259 ASN 260 0.0001

ASN 260 GLY 261 0.0000

GLY 261 PRO 262 0.0007

PRO 262 LEU 263 0.0003

LEU 263 HIS 264 0.0001

HIS 264 LEU 265 0.0002

LEU 265 GLU 266 0.0000

GLU 266 MET 267 -0.0004

MET 267 THR 268 0.0009

THR 268 LEU 269 0.0002

LEU 269 THR 270 -0.0003

THR 270 ARG 271 0.0005

ARG 271 ALA 272 -0.0001

ALA 272 LYS 273 -0.0002

LYS 273 PHE 274 0.0001

PHE 274 GLU 275 0.0001

GLU 275 GLU 276 -0.0001

GLU 276 LEU 277 0.0006

LEU 277 SER 278 0.0001

SER 278 ALA 279 0.0003

ALA 279 HIS 280 -0.0011

HIS 280 LEU 281 -0.0001

LEU 281 VAL 282 0.0002

VAL 282 GLU 283 0.0002

GLU 283 ARG 284 0.0001

ARG 284 THR 285 0.0001

THR 285 MET 286 -0.0000

MET 286 GLY 287 -0.0001

GLY 287 PRO 288 0.0001

PRO 288 VAL 289 0.0003

VAL 289 ARG 290 -0.0002

ARG 290 GLN 291 0.0003

GLN 291 ALA 292 -0.0006

ALA 292 LEU 293 0.0001

LEU 293 GLN 294 -0.0004

GLN 294 ASP 295 -0.0004

ASP 295 ALA 296 0.0001

ALA 296 GLY 297 -0.0003

GLY 297 LEU 298 0.0001

LEU 298 THR 299 0.0002

THR 299 PRO 300 -0.0001

PRO 300 ALA 301 0.0001

ALA 301 ASP 302 0.0001

ASP 302 ILE 303 0.0002

ILE 303 ASP 304 -0.0002

ASP 304 LYS 305 0.0004

LYS 305 VAL 306 -0.0003

VAL 306 ILE 307 0.0000

ILE 307 LEU 308 -0.0002

LEU 308 VAL 309 -0.0000

VAL 309 GLY 310 0.0002

GLY 310 GLY 311 0.0003

GLY 311 SER 312 -0.0001

SER 312 THR 313 0.0001

THR 313 ARG 314 -0.0003

ARG 314 ILE 315 0.0000

ILE 315 PRO 316 0.0007

PRO 316 ALA 317 0.0000

ALA 317 VAL 318 -0.0001

VAL 318 GLN 319 0.0002

GLN 319 GLU 320 0.0003

GLU 320 ALA 321 -0.0002

ALA 321 ILE 322 0.0003

ILE 322 LYS 323 -0.0001

LYS 323 ARG 324 0.0001

ARG 324 GLU 325 0.0000

GLU 325 LEU 326 0.0000

LEU 326 GLY 327 -0.0002

GLY 327 LYS 328 -0.0003

LYS 328 GLU 329 -0.0004

GLU 329 PRO 330 -0.0002

PRO 330 HIS 331 0.0006

HIS 331 LYS 332 -0.0006

LYS 332 GLY 333 -0.0002

GLY 333 VAL 334 0.0001

VAL 334 ASN 335 -0.0003

ASN 335 PRO 336 0.0000

PRO 336 ASP 337 -0.0018

ASP 337 GLU 338 -0.0001

GLU 338 VAL 339 -0.0001

VAL 339 VAL 340 -0.0001

VAL 340 ALA 341 0.0001

ALA 341 ILE 342 -0.0002

ILE 342 GLY 343 -0.0011

GLY 343 ALA 344 0.0003

ALA 344 ALA 345 0.0003

ALA 345 ILE 346 -0.0001

ILE 346 GLN 347 -0.0002

GLN 347 GLY 348 -0.0004

GLY 348 GLY 349 0.0212

GLY 349 VAL 350 -0.0002

VAL 350 ILE 351 -0.0003

ILE 351 ALA 352 -0.0279

ALA 352 GLY 353 -0.0001

GLY 353 GLU 354 -0.0002

GLU 354 VAL 355 0.0216

VAL 355 LYS 356 -0.0000

LYS 356 ASP 357 -0.0000

ASP 357 VAL 358 -0.0025

VAL 358 VAL 359 0.0004

VAL 359 LEU 360 0.0000

LEU 360 LEU 361 -0.1878

LEU 361 ASP 362 0.0003

ASP 362 VAL 363 -0.0001

VAL 363 THR 364 0.0078

THR 364 PRO 365 -0.0003

PRO 365 LEU 366 0.0001

LEU 366 SER 367 0.0017

SER 367 LEU 368 -0.0001

LEU 368 GLY 369 -0.0002

GLY 369 ILE 370 -0.0025

ILE 370 GLU 371 0.0002

GLU 371 THR 372 -0.0004

THR 372 MET 373 -0.0024

MET 373 GLY 374 0.0001

GLY 374 GLY 375 -0.0002

GLY 375 VAL 376 -0.0018

VAL 376 PHE 377 -0.0004

PHE 377 THR 378 -0.0001

THR 378 LYS 379 0.0003

LYS 379 LEU 380 0.0000

LEU 380 ILE 381 -0.0001

ILE 381 GLU 382 -0.0019

GLU 382 ARG 383 0.0002

ARG 383 ASN 384 0.0002

ASN 384 THR 385 0.0125

THR 385 THR 386 -0.0002

THR 386 ILE 387 0.0004

ILE 387 PRO 388 0.0055

PRO 388 THR 389 0.0002

THR 389 SER 390 -0.0003

SER 390 LYS 391 -0.0087

LYS 391 SER 392 0.0000

SER 392 GLN 393 0.0000

GLN 393 VAL 394 -0.0100

VAL 394 PHE 395 -0.0002

PHE 395 THR 396 -0.0002

THR 396 THR 397 -0.0081

THR 397 ALA 398 0.0000

ALA 398 ALA 399 0.0000

ALA 399 ASP 400 0.0084

ASP 400 ASN 401 -0.0000

ASN 401 GLN 402 -0.0001

GLN 402 THR 403 -0.0014

THR 403 THR 404 0.0002

THR 404 VAL 405 0.0001

VAL 405 ASP 406 0.0027

ASP 406 ILE 407 -0.0001

ILE 407 HIS 408 -0.0000

HIS 408 VAL 409 -0.0031

VAL 409 LEU 410 -0.0001

LEU 410 GLN 411 0.0000

GLN 411 GLY 412 -0.0039

GLY 412 GLU 413 -0.0003

GLU 413 ARG 414 -0.0000

ARG 414 PRO 415 0.0034

PRO 415 MET 416 0.0000

MET 416 ALA 417 -0.0002

ALA 417 ALA 418 -0.0014

ALA 418 ASP 419 -0.0002

ASP 419 ASN 420 0.0000

ASN 420 LYS 421 -0.0019

LYS 421 SER 422 -0.0002

SER 422 LEU 423 0.0000

LEU 423 GLY 424 -0.0032

GLY 424 ARG 425 -0.0001

ARG 425 PHE 426 0.0001

PHE 426 GLN 427 -0.0017

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 11 ---

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

* 2V7Y *