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

* ddd *

CA strain for 2502111056123569753

--- 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
MET 1 ARG 2 -0.0001

ARG 2 VAL 3 -0.0001

VAL 3 TRP 4 0.0002

TRP 4 VAL 5 0.0003

VAL 5 GLY 6 0.0000

GLY 6 ILE 7 -0.0002

ILE 7 ASP 8 -0.0003

ASP 8 ASP 9 0.0001

ASP 9 THR 10 0.0025

THR 10 ASP 11 0.0001

ASP 11 SER 12 -0.0002

SER 12 SER 13 -0.0017

SER 13 ARG 14 0.0001

ARG 14 GLY 15 -0.0000

GLY 15 MET 16 0.0013

MET 16 CYS 17 -0.0003

CYS 17 THR 19 -0.0009

THR 19 TYR 20 0.0003

TYR 20 LEU 21 -0.0000

LEU 21 ALA 22 -0.0007

ALA 22 VAL 23 -0.0004

VAL 23 LEU 24 -0.0003

LEU 24 ALA 25 -0.0011

ALA 25 MET 26 -0.0001

MET 26 GLU 27 -0.0003

GLU 27 ARG 28 -0.0014

ARG 28 VAL 29 0.0001

VAL 29 GLU 30 -0.0000

GLU 30 ARG 31 -0.0001

ARG 31 GLU 32 -0.0003

GLU 32 LEU 33 -0.0001

LEU 33 GLY 34 0.0002

GLY 34 LYS 35 0.0003

LYS 35 VAL 36 -0.0002

VAL 36 ILE 37 -0.0004

ILE 37 GLY 38 -0.0003

GLY 38 PHE 39 -0.0003

PHE 39 PRO 40 0.0017

PRO 40 ARG 41 0.0001

ARG 41 LEU 42 0.0002

LEU 42 ILE 43 0.0047

ILE 43 ARG 44 -0.0001

ARG 44 LEU 45 -0.0001

LEU 45 ASN 46 0.0083

ASN 46 PRO 47 -0.0002

PRO 47 THR 48 0.0001

THR 48 ILE 49 -0.0021

ILE 49 PRO 50 -0.0001

PRO 50 ARG 54 0.0057

ARG 54 GLY 55 0.0001

GLY 55 ASN 56 -0.0002

ASN 56 GLY 57 0.0087

GLY 57 ALA 58 0.0004

ALA 58 VAL 59 -0.0002

VAL 59 SER 60 0.0024

SER 60 PHE 61 0.0002

PHE 61 LEU 62 0.0001

LEU 62 VAL 63 0.0002

VAL 63 GLU 64 0.0003

GLU 64 VAL 65 -0.0000

VAL 65 ASP 66 0.0001

ASP 66 ASP 67 -0.0000

ASP 67 VAL 68 0.0000

VAL 68 GLY 69 -0.0001

GLY 69 GLU 70 -0.0000

GLU 70 LEU 71 -0.0001

LEU 71 VAL 72 0.0007

VAL 72 ASP 73 0.0001

ASP 73 VAL 74 0.0004

VAL 74 VAL 75 0.0006

VAL 75 ASN 76 -0.0002

ASN 76 GLU 77 0.0000

GLU 77 VAL 78 -0.0011

VAL 78 ILE 79 0.0002

ILE 79 ILE 80 -0.0000

ILE 80 GLU 81 0.0002

GLU 81 HIS 82 0.0002

HIS 82 ALA 83 -0.0003

ALA 83 MET 84 0.0004

MET 84 LEU 85 0.0002

LEU 85 ASP 86 0.0003

ASP 86 ASP 87 -0.0001

ASP 87 GLU 88 -0.0000

GLU 88 LYS 89 -0.0004

LYS 89 THR 90 0.0003

THR 90 ASN 91 -0.0000

ASN 91 PRO 92 0.0001

PRO 92 GLY 93 -0.0001

GLY 93 ALA 94 0.0002

ALA 94 VAL 95 0.0002

VAL 95 PHE 96 0.0006

PHE 96 VAL 97 0.0002

VAL 97 ASP 98 -0.0003

ASP 98 GLU 99 0.0005

GLU 99 GLU 100 0.0002

GLU 100 LEU 101 -0.0002

LEU 101 ALA 102 0.0004

ALA 102 VAL 103 0.0002

VAL 103 LYS 104 -0.0002

LYS 104 LEU 105 -0.0012

LEU 105 LYS 106 -0.0002

LYS 106 PRO 107 0.0002

PRO 107 PHE 108 0.0019

PHE 108 ALA 109 -0.0001

ALA 109 ASP 110 0.0003

ASP 110 LYS 111 -0.0016

LYS 111 ALA 112 -0.0000

ALA 112 ILE 113 0.0001

ILE 113 LYS 114 0.0051

LYS 114 ASP 115 0.0005

ASP 115 VAL 116 -0.0004

VAL 116 LEU 117 0.0070

LEU 117 GLN 118 0.0003

GLN 118 ILE 119 -0.0002

ILE 119 ASP 120 0.0008

ASP 120 GLU 121 0.0004

GLU 121 ALA 122 0.0000

ALA 122 LEU 123 0.0006

LEU 123 PHE 124 -0.0001

PHE 124 VAL 125 0.0000

VAL 125 ILE 126 -0.0001

ILE 126 GLY 127 0.0001

GLY 127 LYS 128 -0.0005

LYS 128 TYR 129 0.0000

TYR 129 PHE 130 -0.0002

PHE 130 ILE 131 0.0001

ILE 131 PRO 132 -0.0016

PRO 132 HIS 133 0.0003

HIS 133 LEU 134 0.0000

LEU 134 ARG 135 -0.0001

ARG 135 HIS 136 0.0002

HIS 136 LYS 137 0.0003

LYS 137 LYS 138 0.0017

LYS 138 GLY 139 -0.0002

GLY 139 ARG 140 0.0002

ARG 140 GLY 141 -0.0017

GLY 141 LEU 142 -0.0002

LEU 142 ILE 143 0.0001

ILE 143 GLY 144 -0.0021

GLY 144 ALA 145 0.0001

ALA 145 LEU 146 -0.0003

LEU 146 ALA 147 0.0005

ALA 147 ALA 148 -0.0003

ALA 148 VAL 149 0.0000

VAL 149 GLY 150 -0.0004

GLY 150 ALA 151 0.0003

ALA 151 GLU 152 -0.0004

GLU 152 LEU 153 0.0025

LEU 153 GLU 154 -0.0002

GLU 154 ASP 155 0.0002

ASP 155 PHE 156 0.0010

PHE 156 THR 157 0.0000

THR 157 LEU 158 -0.0001

LEU 158 GLU 159 0.0003

GLU 159 LEU 160 0.0001

LEU 160 ILE 161 0.0001

ILE 161 ALA 162 0.0019

ALA 162 TYR 163 0.0002

TYR 163 ARG 164 0.0002

ARG 164 TYR 165 -0.0002

TYR 165 PRO 166 -0.0002

PRO 166 GLU 167 -0.0001

GLU 167 ARG 168 -0.0004

ARG 168 PHE 169 -0.0003

PHE 169 GLY 170 -0.0000

GLY 170 THR 171 -0.0006

THR 171 GLU 172 -0.0002

GLU 172 ARG 173 -0.0003

ARG 173 GLU 174 -0.0036

GLU 174 TYR 175 0.0003

TYR 175 ASP 176 0.0003

ASP 176 GLU 177 0.0004

GLU 177 GLU 178 0.0001

GLU 178 SER 179 0.0002

SER 179 PHE 180 0.0008

PHE 180 PHE 181 -0.0002

PHE 181 ASP 182 0.0003

ASP 182 MET 183 0.0031

MET 183 ASP 184 -0.0001

ASP 184 TYR 185 -0.0000

TYR 185 GLU 186 0.0055

GLU 186 LEU 187 -0.0000

LEU 187 TYR 188 -0.0000

TYR 188 PRO 189 -0.0008

PRO 189 GLN 190 0.0002

GLN 190 THR 191 -0.0000

THR 191 PHE 192 0.0015

PHE 192 ASP 193 -0.0004

ASP 193 ASN 194 -0.0002

ASN 194 VAL 195 -0.0033

VAL 195 ASP 196 0.0003

ASP 196 TRP 197 -0.0003

TRP 197 CYS 198 0.0063

CYS 198 ASN 199 0.0003

ASN 199 ASP 200 -0.0004

ASP 200 VAL 201 -0.0051

VAL 201 VAL 202 -0.0004

VAL 202 VAL 203 -0.0002

VAL 203 CYS 204 -0.0040

CYS 204 ILE 205 -0.0003

ILE 205 PRO 206 -0.0001

PRO 206 ASN 207 0.0009

ASN 207 THR 208 -0.0001

THR 208 PRO 209 0.0002

PRO 209 CYS 210 0.0009

CYS 210 PRO 211 0.0003

PRO 211 VAL 212 -0.0000

VAL 212 LEU 213 -0.0015

LEU 213 TYR 214 -0.0000

TYR 214 GLY 215 -0.0004

GLY 215 ILE 216 -0.0001

ILE 216 ARG 217 -0.0003

ARG 217 GLY 218 0.0001

GLY 218 GLU 219 0.0001

GLU 219 SER 220 0.0002

SER 220 VAL 221 0.0002

VAL 221 GLU 222 0.0002

GLU 222 ALA 223 -0.0004

ALA 223 LEU 224 0.0003

LEU 224 TYR 225 -0.0013

TYR 225 LYS 226 -0.0002

LYS 226 ALA 227 -0.0003

ALA 227 MET 228 -0.0024

MET 228 GLU 229 -0.0003

GLU 229 SER 230 -0.0000

SER 230 VAL 231 -0.0023

VAL 231 LYS 232 0.0000

LYS 232 THR 233 0.0001

THR 233 GLU 234 -0.0022

GLU 234 PRO 235 -0.0001

PRO 235 VAL 236 0.0002

VAL 236 ASP 237 0.0004

ASP 237 ARG 238 -0.0001

ARG 238 ARG 239 0.0001

ARG 239 MET 240 -0.0000

MET 240 ILE 241 -0.0001

ILE 241 PHE 242 0.0000

PHE 242 VAL 243 -0.0017

VAL 243 THR 244 -0.0001

THR 244 ASN 245 -0.0001

ASN 245 HIS 246 -0.0004

HIS 246 ALA 247 -0.0001

ALA 247 THR 248 0.0001

THR 248 ASP 249 -0.0032

ASP 249 MET 250 0.0004

MET 250 HIS 251 -0.0002

HIS 251 LEU 252 0.0022

LEU 252 ILE 253 -0.0002

ILE 253 GLY 254 0.0003

GLY 254 GLU 255 -0.0009

GLU 255 GLU 256 0.0000

GLU 256 GLU 257 -0.0002

GLU 257 VAL 258 -0.0002

VAL 258 HIS 259 -0.0001

HIS 259 ARG 260 -0.0000

ARG 260 LEU 261 -0.0023

LEU 261 GLU 262 -0.0003

GLU 262 ASN 263 0.0001

ASN 263 TYR 264 0.0066

TYR 264 ARG 265 -0.0002

ARG 265 SER 266 0.0001

SER 266 TYR 267 0.0041

TYR 267 ARG 268 0.0002

ARG 268 LEU 269 -0.0002

LEU 269 ARG 270 0.0143

ARG 270 GLY 271 0.0001

GLY 271 ARG 272 0.0000

ARG 272 VAL 273 -0.0032

VAL 273 THR 274 0.0002

THR 274 LEU 275 0.0001

LEU 275 GLU 276 -0.0089

GLU 276 PRO 277 0.0003

PRO 277 TYR 278 -0.0003

TYR 278 ASP 279 0.0076

ASP 279 ILE 280 0.0000

ILE 280 GLU 281 -0.0000

GLU 281 GLY 282 0.0053

GLY 282 GLY 283 -0.0005

GLY 283 HIS 284 0.0001

HIS 284 VAL 285 0.0021

VAL 285 PHE 286 -0.0000

PHE 286 PHE 287 0.0002

PHE 287 GLU 288 -0.0054

GLU 288 ILE 289 0.0002

ILE 289 ASP 290 0.0002

ASP 290 THR 291 0.0041

THR 291 LYS 292 -0.0002

LYS 292 PHE 293 -0.0001

PHE 293 GLY 294 0.0005

GLY 294 SER 295 -0.0002

SER 295 VAL 296 0.0001

VAL 296 LYS 297 -0.0088

LYS 297 CYS 298 -0.0002

CYS 298 ALA 299 0.0003

ALA 299 ALA 300 0.0001

ALA 300 PHE 301 -0.0001

PHE 301 GLU 302 0.0001

GLU 302 PRO 303 0.0104

PRO 303 THR 304 0.0001

THR 304 LYS 305 0.0003

LYS 305 GLN 306 -0.0009

GLN 306 PHE 307 -0.0000

PHE 307 ARG 308 0.0002

ARG 308 ASN 309 -0.0099

ASN 309 VAL 310 0.0003

VAL 310 ILE 311 -0.0001

ILE 311 ARG 312 0.0016

ARG 312 LEU 313 0.0001

LEU 313 LEU 314 -0.0003

LEU 314 ARG 315 0.0177

ARG 315 LYS 316 -0.0002

LYS 316 GLY 317 0.0000

GLY 317 ASP 318 -0.0143

ASP 318 VAL 319 0.0000

VAL 319 VAL 320 0.0004

VAL 320 GLU 321 0.0222

GLU 321 VAL 322 -0.0004

VAL 322 TYR 323 0.0002

TYR 323 GLY 324 0.0016

GLY 324 SER 325 -0.0001

SER 325 MET 326 0.0002

MET 326 LYS 327 -0.0026

LYS 327 LYS 328 -0.0002

LYS 328 ASP 329 -0.0001

ASP 329 THR 330 -0.0039

THR 330 ILE 331 -0.0005

ILE 331 ASN 332 -0.0001

ASN 332 LEU 333 -0.0026

LEU 333 GLU 334 0.0002

GLU 334 LYS 335 -0.0002

LYS 335 ILE 336 -0.0062

ILE 336 GLN 337 0.0004

GLN 337 ILE 338 -0.0001

ILE 338 VAL 339 -0.0126

VAL 339 GLU 340 -0.0000

GLU 340 LEU 341 0.0002

LEU 341 ALA 342 0.0060

ALA 342 GLU 343 -0.0002

GLU 343 ILE 344 0.0001

ILE 344 TRP 345 0.1213

TRP 345 VAL 346 0.0004

VAL 346 GLU 347 0.0001

GLU 347 LYS 348 -0.1263

LYS 348 ASN 349 -0.0002

ASN 349 PRO 350 -0.0001

PRO 350 ILE 351 0.0132

ILE 351 CYS 352 -0.0000

CYS 352 PRO 353 -0.0001

PRO 353 SER 354 0.0014

SER 354 CYS 355 0.0003

CYS 355 GLY 356 -0.0001

GLY 356 ARG 357 -0.0111

ARG 357 ARG 358 -0.0000

ARG 358 MET 359 0.0001

MET 359 ASP 360 0.0087

ASP 360 SER 361 -0.0001

SER 361 ALA 362 -0.0002

ALA 362 GLY 363 0.0172

GLY 363 ARG 364 -0.0002

ARG 364 GLY 365 -0.0001

GLY 365 GLN 366 -0.0183

GLN 366 GLY 367 -0.0001

GLY 367 PHE 368 -0.0001

PHE 368 ARG 369 -0.0078

ARG 369 CYS 370 -0.0001

CYS 370 LYS 371 0.0001

LYS 371 LYS 372 -0.0036

LYS 372 CYS 373 -0.0001

CYS 373 ARG 374 0.0002

ARG 374 THR 375 0.0124

THR 375 LYS 376 -0.0002

LYS 376 ALA 377 0.0001

ALA 377 ASP 378 0.0299

ASP 378 GLU 379 0.0003

GLU 379 LYS 380 -0.0002

LYS 380 LEU 381 -0.0920

LEU 381 ARG 382 0.0002

ARG 382 GLU 383 -0.0000

GLU 383 LYS 384 0.0114

LYS 384 VAL 385 0.0002

VAL 385 GLU 386 0.0003

GLU 386 ARG 387 -0.1572

ARG 387 GLU 388 0.0001

GLU 388 LEU 389 0.0001

LEU 389 GLN 390 0.0135

GLN 390 PRO 391 -0.0001

PRO 391 GLY 392 -0.0003

GLY 392 PHE 393 0.0013

PHE 393 TYR 394 0.0001

TYR 394 GLU 395 0.0001

GLU 395 VAL 396 0.0019

VAL 396 PRO 397 -0.0001

PRO 397 PRO 398 -0.0003

PRO 398 SER 399 -0.0011

SER 399 ALA 400 -0.0003

ALA 400 ARG 401 0.0000

ARG 401 ARG 402 -0.0090

ARG 402 HIS 403 0.0001

HIS 403 LEU 404 0.0003

LEU 404 SER 405 -0.0014

SER 405 LYS 406 0.0003

LYS 406 PRO 407 0.0001

PRO 407 LEU 408 -0.0024

LEU 408 ILE 409 0.0002

ILE 409 ARG 410 -0.0000

ARG 410 MET 411 -0.0081

MET 411 ASN 412 -0.0001

ASN 412 VAL 413 -0.0001

VAL 413 GLU 414 0.0022

GLU 414 GLY 415 -0.0002

GLY 415 ARG 416 0.0001

ARG 416 HIS 417 0.0008

HIS 417 ILE 418 -0.0001

ILE 418 PHE 419 0.0004

PHE 419 ARG 420 -0.0152

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 8th, 2025.

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

*** ddd ***

CA strain for 2502111056123569753

--- normal mode 9 ---

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

* ddd *