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

* 2V7Y *

CA strain for 240228055913921343

--- normal mode 12 ---

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 0.0002

SER 2 LYS 3 -0.0003

LYS 3 ILE 4 0.0001

ILE 4 ILE 5 0.0003

ILE 5 GLY 6 0.0002

GLY 6 ILE 7 -0.0077

ILE 7 ASP 8 0.0001

ASP 8 LEU 9 0.0001

LEU 9 GLY 10 -0.0089

GLY 10 THR 11 0.0000

THR 11 THR 12 -0.0002

THR 12 ASN 13 0.0020

ASN 13 SER 14 -0.0002

SER 14 CYS 15 0.0003

CYS 15 VAL 16 -0.0006

VAL 16 ALA 17 -0.0001

ALA 17 VAL 18 -0.0001

VAL 18 LEU 19 0.0010

LEU 19 GLU 20 0.0005

GLU 20 GLY 21 -0.0004

GLY 21 GLY 22 -0.0013

GLY 22 GLU 23 -0.0002

GLU 23 VAL 24 0.0002

VAL 24 LYS 25 0.0000

LYS 25 VAL 26 0.0002

VAL 26 ILE 27 -0.0002

ILE 27 PRO 28 0.0005

PRO 28 ASN 29 -0.0002

ASN 29 PRO 30 0.0002

PRO 30 GLU 31 0.0018

GLU 31 GLY 32 -0.0001

GLY 32 ASN 33 -0.0002

ASN 33 ARG 34 -0.0012

ARG 34 THR 35 -0.0001

THR 35 THR 36 -0.0003

THR 36 PRO 37 0.0028

PRO 37 SER 38 0.0001

SER 38 VAL 39 0.0001

VAL 39 VAL 40 0.0012

VAL 40 ALA 41 0.0003

ALA 41 PHE 42 -0.0001

PHE 42 LYS 43 0.0002

LYS 43 ASN 44 0.0000

ASN 44 GLY 45 -0.0003

GLY 45 GLU 46 -0.0010

GLU 46 ARG 47 0.0004

ARG 47 LEU 48 -0.0003

LEU 48 VAL 49 -0.0013

VAL 49 GLY 50 -0.0001

GLY 50 GLU 51 -0.0002

GLU 51 VAL 52 -0.0008

VAL 52 ALA 53 0.0001

ALA 53 LYS 54 0.0002

LYS 54 ARG 55 -0.0029

ARG 55 GLN 56 0.0002

GLN 56 ALA 57 -0.0002

ALA 57 ILE 58 -0.0049

ILE 58 THR 59 0.0004

THR 59 ASN 60 0.0003

ASN 60 PRO 61 -0.0034

PRO 61 ASN 62 0.0001

ASN 62 THR 63 -0.0003

THR 63 ILE 64 -0.0008

ILE 64 ILE 65 -0.0002

ILE 65 SER 66 0.0006

SER 66 ILE 67 -0.0039

ILE 67 LYS 68 -0.0001

LYS 68 ARG 69 0.0001

ARG 69 HIS 70 -0.0006

HIS 70 MET 71 -0.0003

MET 71 GLY 72 0.0001

GLY 72 THR 73 0.0002

THR 73 ASP 74 -0.0000

ASP 74 TYR 75 0.0002

TYR 75 LYS 76 0.0017

LYS 76 VAL 77 0.0002

VAL 77 GLU 78 0.0001

GLU 78 ILE 79 0.0004

ILE 79 GLU 80 0.0002

GLU 80 GLY 81 0.0004

GLY 81 LYS 82 -0.0007

LYS 82 GLN 83 0.0001

GLN 83 TYR 84 -0.0000

TYR 84 THR 85 -0.0021

THR 85 PRO 86 0.0002

PRO 86 GLN 87 0.0002

GLN 87 GLU 88 -0.0002

GLU 88 ILE 89 0.0000

ILE 89 SER 90 0.0001

SER 90 ALA 91 0.0008

ALA 91 ILE 92 0.0003

ILE 92 ILE 93 0.0004

ILE 93 LEU 94 -0.0020

LEU 94 GLN 95 0.0001

GLN 95 TYR 96 0.0003

TYR 96 LEU 97 -0.0009

LEU 97 LYS 98 0.0003

LYS 98 SER 99 -0.0002

SER 99 TYR 100 -0.0010

TYR 100 ALA 101 0.0001

ALA 101 GLU 102 -0.0003

GLU 102 ASP 103 -0.0010

ASP 103 TYR 104 0.0001

TYR 104 LEU 105 0.0000

LEU 105 GLY 106 -0.0043

GLY 106 GLU 107 -0.0001

GLU 107 PRO 108 -0.0001

PRO 108 VAL 109 -0.0009

VAL 109 THR 110 0.0002

THR 110 ARG 111 0.0003

ARG 111 ALA 112 -0.0016

ALA 112 VAL 113 0.0000

VAL 113 ILE 114 0.0004

ILE 114 THR 115 -0.0026

THR 115 VAL 116 -0.0000

VAL 116 PRO 117 0.0003

PRO 117 ALA 118 0.0026

ALA 118 TYR 119 0.0002

TYR 119 PHE 120 -0.0001

PHE 120 ASN 121 -0.0009

ASN 121 ASP 122 0.0002

ASP 122 ALA 123 -0.0000

ALA 123 GLN 124 0.0002

GLN 124 ARG 125 0.0002

ARG 125 GLN 126 -0.0002

GLN 126 ALA 127 0.0027

ALA 127 THR 128 -0.0002

THR 128 LYS 129 0.0000

LYS 129 ASP 130 -0.0004

ASP 130 ALA 131 -0.0002

ALA 131 GLY 132 0.0002

GLY 132 ARG 133 -0.0010

ARG 133 ILE 134 0.0000

ILE 134 ALA 135 0.0002

ALA 135 GLY 136 0.0006

GLY 136 LEU 137 -0.0004

LEU 137 GLU 138 0.0003

GLU 138 VAL 139 -0.0006

VAL 139 GLU 140 0.0001

GLU 140 ARG 141 0.0001

ARG 141 ILE 142 -0.0291

ILE 142 ILE 143 -0.0000

ILE 143 ASN 144 0.0002

ASN 144 GLU 145 -0.0059

GLU 145 PRO 146 0.0000

PRO 146 THR 147 -0.0004

THR 147 ALA 148 -0.0042

ALA 148 ALA 149 0.0002

ALA 149 ALA 150 -0.0000

ALA 150 LEU 151 -0.0070

LEU 151 ALA 152 0.0001

ALA 152 TYR 153 0.0000

TYR 153 GLY 154 -0.0017

GLY 154 LEU 155 0.0000

LEU 155 ASP 156 -0.0002

ASP 156 LYS 157 0.0007

LYS 157 GLU 158 0.0001

GLU 158 GLU 159 -0.0002

GLU 159 ASP 160 0.0003

ASP 160 GLN 161 0.0004

GLN 161 THR 162 -0.0002

THR 162 ILE 163 0.0006

ILE 163 LEU 164 -0.0002

LEU 164 VAL 165 0.0003

VAL 165 TYR 166 -0.0016

TYR 166 ASP 167 0.0002

ASP 167 LEU 168 -0.0002

LEU 168 GLY 169 0.0018

GLY 169 GLY 170 0.0001

GLY 170 GLY 171 0.0002

GLY 171 THR 172 -0.0012

THR 172 PHE 173 0.0004

PHE 173 ASP 174 -0.0001

ASP 174 VAL 175 0.0017

VAL 175 SER 176 0.0002

SER 176 ILE 177 0.0000

ILE 177 LEU 178 -0.0015

LEU 178 GLU 179 -0.0004

GLU 179 LEU 180 -0.0000

LEU 180 GLY 181 0.0005

GLY 181 ASP 182 0.0004

ASP 182 GLY 183 0.0000

GLY 183 VAL 184 0.0006

VAL 184 PHE 185 0.0000

PHE 185 GLU 186 0.0000

GLU 186 VAL 187 0.0004

VAL 187 LYS 188 0.0005

LYS 188 ALA 189 -0.0000

ALA 189 THR 190 0.0023

THR 190 ALA 191 -0.0000

ALA 191 GLY 192 0.0003

GLY 192 ASP 193 0.0012

ASP 193 ASN 194 0.0003

ASN 194 HIS 195 -0.0003

HIS 195 LEU 196 -0.0014

LEU 196 GLY 197 0.0001

GLY 197 GLY 198 0.0001

GLY 198 ASP 199 -0.0008

ASP 199 ASP 200 -0.0001

ASP 200 PHE 201 -0.0003

PHE 201 ASP 202 0.0010

ASP 202 GLN 203 -0.0002

GLN 203 VAL 204 0.0000

VAL 204 ILE 205 -0.0013

ILE 205 ILE 206 -0.0002

ILE 206 ASP 207 -0.0002

ASP 207 TYR 208 0.0006

TYR 208 LEU 209 -0.0003

LEU 209 VAL 210 -0.0001

VAL 210 ASN 211 0.0013

ASN 211 GLN 212 -0.0000

GLN 212 PHE 213 0.0002

PHE 213 LYS 214 0.0016

LYS 214 GLN 215 -0.0000

GLN 215 GLU 216 -0.0004

GLU 216 HIS 217 -0.0002

HIS 217 GLY 218 -0.0001

GLY 218 ILE 219 0.0001

ILE 219 ASP 220 -0.0005

ASP 220 LEU 221 -0.0003

LEU 221 SER 222 -0.0000

SER 222 LYS 223 0.0015

LYS 223 ASP 224 -0.0001

ASP 224 LYS 225 -0.0000

LYS 225 MET 226 -0.0017

MET 226 ALA 227 -0.0000

ALA 227 LEU 228 -0.0001

LEU 228 GLN 229 0.0007

GLN 229 ARG 230 0.0002

ARG 230 LEU 231 -0.0003

LEU 231 LYS 232 -0.0006

LYS 232 ASP 233 0.0002

ASP 233 ALA 234 -0.0001

ALA 234 ALA 235 0.0006

ALA 235 GLU 236 0.0003

GLU 236 LYS 237 -0.0001

LYS 237 ALA 238 -0.0009

ALA 238 LYS 239 0.0003

LYS 239 LYS 240 0.0000

LYS 240 GLU 241 0.0001

GLU 241 LEU 242 -0.0001

LEU 242 SER 243 0.0001

SER 243 GLY 244 0.0011

GLY 244 VAL 245 0.0000

VAL 245 THR 246 -0.0002

THR 246 GLN 247 0.0008

GLN 247 THR 248 0.0001

THR 248 GLN 249 -0.0002

GLN 249 ILE 250 -0.0015

ILE 250 SER 251 0.0001

SER 251 LEU 252 -0.0001

LEU 252 PRO 253 0.0015

PRO 253 PHE 254 -0.0002

PHE 254 ILE 255 -0.0000

ILE 255 SER 256 -0.0016

SER 256 ALA 257 0.0001

ALA 257 ASN 258 -0.0003

ASN 258 GLU 259 -0.0010

GLU 259 ASN 260 -0.0001

ASN 260 GLY 261 -0.0001

GLY 261 PRO 262 0.0007

PRO 262 LEU 263 -0.0000

LEU 263 HIS 264 -0.0000

HIS 264 LEU 265 0.0005

LEU 265 GLU 266 0.0004

GLU 266 MET 267 -0.0006

MET 267 THR 268 0.0014

THR 268 LEU 269 -0.0003

LEU 269 THR 270 0.0002

THR 270 ARG 271 -0.0003

ARG 271 ALA 272 -0.0002

ALA 272 LYS 273 0.0003

LYS 273 PHE 274 -0.0002

PHE 274 GLU 275 -0.0004

GLU 275 GLU 276 -0.0002

GLU 276 LEU 277 0.0008

LEU 277 SER 278 -0.0001

SER 278 ALA 279 -0.0003

ALA 279 HIS 280 -0.0010

HIS 280 LEU 281 0.0003

LEU 281 VAL 282 -0.0001

VAL 282 GLU 283 0.0009

GLU 283 ARG 284 0.0003

ARG 284 THR 285 -0.0000

THR 285 MET 286 0.0004

MET 286 GLY 287 -0.0004

GLY 287 PRO 288 -0.0003

PRO 288 VAL 289 0.0008

VAL 289 ARG 290 0.0000

ARG 290 GLN 291 0.0002

GLN 291 ALA 292 -0.0008

ALA 292 LEU 293 0.0001

LEU 293 GLN 294 -0.0004

GLN 294 ASP 295 -0.0002

ASP 295 ALA 296 -0.0002

ALA 296 GLY 297 -0.0001

GLY 297 LEU 298 -0.0001

LEU 298 THR 299 0.0006

THR 299 PRO 300 -0.0001

PRO 300 ALA 301 0.0004

ALA 301 ASP 302 -0.0000

ASP 302 ILE 303 0.0000

ILE 303 ASP 304 -0.0005

ASP 304 LYS 305 -0.0001

LYS 305 VAL 306 0.0000

VAL 306 ILE 307 -0.0012

ILE 307 LEU 308 0.0000

LEU 308 VAL 309 0.0001

VAL 309 GLY 310 -0.0019

GLY 310 GLY 311 -0.0000

GLY 311 SER 312 -0.0002

SER 312 THR 313 -0.0002

THR 313 ARG 314 0.0003

ARG 314 ILE 315 0.0005

ILE 315 PRO 316 -0.0001

PRO 316 ALA 317 -0.0002

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 -0.0001

ILE 322 LYS 323 0.0000

LYS 323 ARG 324 -0.0001

ARG 324 GLU 325 -0.0002

GLU 325 LEU 326 0.0003

LEU 326 GLY 327 -0.0000

GLY 327 LYS 328 -0.0000

LYS 328 GLU 329 -0.0001

GLU 329 PRO 330 -0.0002

PRO 330 HIS 331 -0.0005

HIS 331 LYS 332 0.0001

LYS 332 GLY 333 -0.0003

GLY 333 VAL 334 0.0009

VAL 334 ASN 335 -0.0000

ASN 335 PRO 336 -0.0004

PRO 336 ASP 337 0.0010

ASP 337 GLU 338 0.0001

GLU 338 VAL 339 -0.0002

VAL 339 VAL 340 0.0017

VAL 340 ALA 341 -0.0001

ALA 341 ILE 342 0.0004

ILE 342 GLY 343 -0.0030

GLY 343 ALA 344 -0.0000

ALA 344 ALA 345 -0.0002

ALA 345 ILE 346 -0.0001

ILE 346 GLN 347 0.0002

GLN 347 GLY 348 0.0001

GLY 348 GLY 349 0.0206

GLY 349 VAL 350 -0.0001

VAL 350 ILE 351 -0.0004

ILE 351 ALA 352 -0.0506

ALA 352 GLY 353 -0.0000

GLY 353 GLU 354 0.0003

GLU 354 VAL 355 -0.1171

VAL 355 LYS 356 0.0000

LYS 356 ASP 357 0.0002

ASP 357 VAL 358 -0.0648

VAL 358 VAL 359 0.0001

VAL 359 LEU 360 -0.0002

LEU 360 LEU 361 0.1142

LEU 361 ASP 362 0.0000

ASP 362 VAL 363 -0.0003

VAL 363 THR 364 -0.1821

THR 364 PRO 365 0.0000

PRO 365 LEU 366 0.0001

LEU 366 SER 367 0.0055

SER 367 LEU 368 0.0001

LEU 368 GLY 369 -0.0000

GLY 369 ILE 370 -0.0274

ILE 370 GLU 371 -0.0000

GLU 371 THR 372 0.0001

THR 372 MET 373 -0.0086

MET 373 GLY 374 -0.0002

GLY 374 GLY 375 -0.0001

GLY 375 VAL 376 -0.0056

VAL 376 PHE 377 0.0002

PHE 377 THR 378 0.0001

THR 378 LYS 379 0.0329

LYS 379 LEU 380 -0.0002

LEU 380 ILE 381 0.0001

ILE 381 GLU 382 -0.0239

GLU 382 ARG 383 -0.0002

ARG 383 ASN 384 0.0002

ASN 384 THR 385 -0.0842

THR 385 THR 386 -0.0002

THR 386 ILE 387 0.0001

ILE 387 PRO 388 -0.0243

PRO 388 THR 389 -0.0000

THR 389 SER 390 0.0003

SER 390 LYS 391 -0.0474

LYS 391 SER 392 0.0000

SER 392 GLN 393 0.0000

GLN 393 VAL 394 0.0125

VAL 394 PHE 395 -0.0000

PHE 395 THR 396 0.0001

THR 396 THR 397 0.0192

THR 397 ALA 398 0.0000

ALA 398 ALA 399 0.0002

ALA 399 ASP 400 -0.0027

ASP 400 ASN 401 0.0003

ASN 401 GLN 402 -0.0002

GLN 402 THR 403 0.0266

THR 403 THR 404 0.0001

THR 404 VAL 405 -0.0000

VAL 405 ASP 406 -0.0264

ASP 406 ILE 407 -0.0000

ILE 407 HIS 408 0.0001

HIS 408 VAL 409 -0.0290

VAL 409 LEU 410 0.0000

LEU 410 GLN 411 -0.0003

GLN 411 GLY 412 -0.0166

GLY 412 GLU 413 0.0002

GLU 413 ARG 414 -0.0002

ARG 414 PRO 415 0.0085

PRO 415 MET 416 0.0001

MET 416 ALA 417 0.0001

ALA 417 ALA 418 0.0024

ALA 418 ASP 419 -0.0003

ASP 419 ASN 420 0.0005

ASN 420 LYS 421 -0.0058

LYS 421 SER 422 -0.0001

SER 422 LEU 423 -0.0006

LEU 423 GLY 424 -0.0529

GLY 424 ARG 425 0.0001

ARG 425 PHE 426 -0.0001

PHE 426 GLN 427 -0.0260

GLN 427 LEU 428 -0.0001

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 12 ---

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

* 2V7Y *