Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* *

CA strain for 2607070804273120202

--- 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
LYS 3 ALA 4 0.0002

ALA 4 ALA 5 -0.0106

ALA 5 ALA 6 0.0003

ALA 6 ILE 7 0.0657

ILE 7 GLY 8 0.0001

GLY 8 ILE 9 -0.0004

ILE 9 ASP 10 -0.0000

ASP 10 LEU 11 -0.0026

LEU 11 GLY 12 -0.0001

GLY 12 THR 13 -0.0034

THR 13 THR 14 0.0003

THR 14 TYR 15 0.0025

TYR 15 SER 16 -0.0002

SER 16 CYS 17 -0.0014

CYS 17 VAL 18 0.0001

VAL 18 GLY 19 -0.0082

GLY 19 VAL 20 0.0001

VAL 20 PHE 21 -0.0031

PHE 21 GLN 22 -0.0001

GLN 22 HIS 23 -0.0017

HIS 23 GLY 24 0.0001

GLY 24 LYS 25 -0.0018

LYS 25 VAL 26 0.0003

VAL 26 GLU 27 -0.0089

GLU 27 ILE 28 0.0001

ILE 28 ILE 29 -0.0032

ILE 29 ALA 30 0.0005

ALA 30 ASN 31 -0.0003

ASN 31 ASP 32 -0.0000

ASP 32 GLN 33 0.0012

GLN 33 GLY 34 0.0001

GLY 34 ASN 35 0.0029

ASN 35 ARG 36 0.0000

ARG 36 THR 37 -0.0040

THR 37 THR 38 0.0001

THR 38 PRO 39 0.0030

PRO 39 SER 40 0.0001

SER 40 TYR 41 -0.0051

TYR 41 VAL 42 -0.0003

VAL 42 ALA 43 0.0027

ALA 43 PHE 44 0.0002

PHE 44 THR 45 -0.0007

THR 45 ASP 46 -0.0000

ASP 46 THR 47 -0.0004

THR 47 GLU 48 -0.0004

GLU 48 ARG 49 0.0071

ARG 49 LEU 50 -0.0004

LEU 50 ILE 51 0.0067

ILE 51 GLY 52 -0.0001

GLY 52 ASP 53 0.0011

ASP 53 ALA 54 -0.0002

ALA 54 ALA 55 -0.0053

ALA 55 LYS 56 0.0002

LYS 56 ASN 57 -0.0052

ASN 57 GLN 58 -0.0001

GLN 58 VAL 59 0.0013

VAL 59 ALA 60 0.0001

ALA 60 LEU 61 0.0094

LEU 61 ASN 62 -0.0002

ASN 62 PRO 63 -0.0039

PRO 63 GLN 64 0.0000

GLN 64 ASN 65 0.0009

ASN 65 THR 66 -0.0001

THR 66 VAL 67 0.0002

VAL 67 PHE 68 0.0001

PHE 68 ASP 69 -0.0036

ASP 69 ALA 70 0.0001

ALA 70 LYS 71 -0.0030

LYS 71 ARG 72 -0.0001

ARG 72 LEU 73 0.0053

LEU 73 ILE 74 0.0001

ILE 74 GLY 75 0.0002

GLY 75 ARG 76 -0.0001

ARG 76 LYS 77 0.0004

LYS 77 PHE 78 0.0003

PHE 78 GLY 79 -0.0008

GLY 79 ASP 80 0.0001

ASP 80 PRO 81 -0.0009

PRO 81 VAL 82 -0.0005

VAL 82 VAL 83 0.0007

VAL 83 GLN 84 0.0003

GLN 84 SER 85 0.0004

SER 85 ASP 86 -0.0003

ASP 86 MET 87 -0.0010

MET 87 LYS 88 -0.0004

LYS 88 HIS 89 0.0018

HIS 89 TRP 90 0.0001

TRP 90 PRO 91 -0.0047

PRO 91 PHE 92 -0.0004

PHE 92 GLN 93 0.0012

GLN 93 VAL 94 0.0003

VAL 94 ILE 95 0.0007

ILE 95 ASN 96 -0.0001

ASN 96 ASP 97 -0.0002

ASP 97 GLY 98 0.0002

GLY 98 ASP 99 0.0003

ASP 99 LYS 100 -0.0002

LYS 100 PRO 101 -0.0001

PRO 101 LYS 102 -0.0001

LYS 102 VAL 103 -0.0010

VAL 103 GLN 104 0.0004

GLN 104 VAL 105 -0.0037

VAL 105 SER 106 -0.0003

SER 106 TYR 107 -0.0018

TYR 107 LYS 108 0.0000

LYS 108 GLY 109 0.0037

GLY 109 GLU 110 0.0001

GLU 110 THR 111 -0.0019

THR 111 LYS 112 0.0001

LYS 112 ALA 113 0.0019

ALA 113 PHE 114 0.0000

PHE 114 TYR 115 0.0003

TYR 115 PRO 116 -0.0000

PRO 116 GLU 117 0.0106

GLU 117 GLU 118 0.0002

GLU 118 ILE 119 0.0067

ILE 119 SER 120 0.0001

SER 120 SER 121 0.0099

SER 121 MET 122 0.0002

MET 122 VAL 123 -0.0024

VAL 123 LEU 124 -0.0002

LEU 124 THR 125 -0.0009

THR 125 LYS 126 -0.0000

LYS 126 MET 127 0.0046

MET 127 LYS 128 -0.0002

LYS 128 GLU 129 0.0044

GLU 129 ILE 130 -0.0004

ILE 130 ALA 131 0.0104

ALA 131 GLU 132 0.0002

GLU 132 ALA 133 -0.0017

ALA 133 TYR 134 -0.0000

TYR 134 LEU 135 0.0074

LEU 135 GLY 136 0.0003

GLY 136 TYR 137 -0.0022

TYR 137 PRO 138 0.0002

PRO 138 VAL 139 -0.0060

VAL 139 THR 140 -0.0002

THR 140 ASN 141 0.0300

ASN 141 ALA 142 -0.0001

ALA 142 VAL 143 -0.0098

VAL 143 ILE 144 0.0000

ILE 144 THR 145 0.0029

THR 145 VAL 146 -0.0001

VAL 146 PRO 147 -0.0011

PRO 147 ALA 148 -0.0000

ALA 148 TYR 149 0.0005

TYR 149 PHE 150 0.0002

PHE 150 ASN 151 0.0010

ASN 151 ASP 152 -0.0002

ASP 152 SER 153 0.0009

SER 153 GLN 154 0.0003

GLN 154 ARG 155 -0.0002

ARG 155 GLN 156 0.0000

GLN 156 ALA 157 0.0031

ALA 157 THR 158 -0.0001

THR 158 LYS 159 0.0038

LYS 159 ASP 160 0.0002

ASP 160 ALA 161 0.0008

ALA 161 GLY 162 -0.0002

GLY 162 VAL 163 0.0001

VAL 163 ILE 164 0.0003

ILE 164 ALA 165 -0.0055

ALA 165 GLY 166 0.0001

GLY 166 LEU 167 0.0041

LEU 167 ASN 168 -0.0002

ASN 168 VAL 169 -0.0174

VAL 169 LEU 170 0.0002

LEU 170 ARG 171 -0.0004

ARG 171 ILE 172 0.0002

ILE 172 ILE 173 -0.0096

ILE 173 ASN 174 0.0002

ASN 174 GLU 175 -0.0013

GLU 175 PRO 176 0.0000

PRO 176 THR 177 -0.0122

THR 177 ALA 178 -0.0000

ALA 178 ALA 179 -0.0166

ALA 179 ALA 180 -0.0000

ALA 180 ILE 181 -0.0422

ILE 181 ALA 182 -0.0003

ALA 182 TYR 183 -0.0135

TYR 183 GLY 184 -0.0000

GLY 184 LEU 185 -0.0014

LEU 185 ASP 186 0.0000

ASP 186 ARG 187 0.0030

ARG 187 THR 188 0.0004

THR 188 GLY 189 0.0023

GLY 189 LYS 190 0.0000

LYS 190 GLY 191 0.0030

GLY 191 GLU 192 0.0002

GLU 192 ARG 193 0.0017

ARG 193 ASN 194 -0.0001

ASN 194 VAL 195 0.0011

VAL 195 LEU 196 0.0001

LEU 196 ILE 197 -0.0019

ILE 197 PHE 198 -0.0003

PHE 198 ASP 199 0.0044

ASP 199 LEU 200 0.0001

LEU 200 GLY 201 0.0060

GLY 201 GLY 202 0.0001

GLY 202 GLY 203 0.0012

GLY 203 THR 204 -0.0001

THR 204 PHE 205 0.0059

PHE 205 ASP 206 -0.0000

ASP 206 VAL 207 0.0038

VAL 207 SER 208 0.0000

SER 208 ILE 209 0.0015

ILE 209 LEU 210 0.0000

LEU 210 THR 211 0.0027

THR 211 ILE 212 0.0002

ILE 212 ASP 213 0.0010

ASP 213 ASP 214 0.0004

ASP 214 GLY 215 -0.0032

GLY 215 ILE 216 0.0000

ILE 216 PHE 217 0.0016

PHE 217 GLU 218 0.0003

GLU 218 VAL 219 0.0001

VAL 219 LYS 220 -0.0002

LYS 220 ALA 221 0.0051

ALA 221 THR 222 -0.0002

THR 222 ALA 223 0.0017

ALA 223 GLY 224 -0.0002

GLY 224 ASP 225 0.0043

ASP 225 THR 226 -0.0000

THR 226 HIS 227 0.0011

HIS 227 LEU 228 -0.0004

LEU 228 GLY 229 0.0022

GLY 229 GLY 230 -0.0001

GLY 230 GLU 231 -0.0023

GLU 231 ASP 232 0.0000

ASP 232 PHE 233 0.0048

PHE 233 ASP 234 -0.0001

ASP 234 ASN 235 -0.0062

ASN 235 ARG 236 0.0003

ARG 236 LEU 237 0.0011

LEU 237 VAL 238 -0.0002

VAL 238 ASN 239 0.0055

ASN 239 HIS 240 0.0001

HIS 240 PHE 241 -0.0083

PHE 241 VAL 242 -0.0000

VAL 242 GLU 243 0.0074

GLU 243 GLU 244 0.0001

GLU 244 PHE 245 -0.0060

PHE 245 LYS 246 -0.0003

LYS 246 ARG 247 0.0063

ARG 247 LYS 248 0.0001

LYS 248 HIS 249 -0.0014

HIS 249 LYS 250 0.0000

LYS 250 LYS 251 0.0060

LYS 251 ASP 252 -0.0003

ASP 252 ILE 253 0.0090

ILE 253 SER 254 -0.0004

SER 254 GLN 255 -0.0008

GLN 255 ASN 256 0.0001

ASN 256 LYS 257 -0.0038

LYS 257 ARG 258 0.0001

ARG 258 ALA 259 0.0280

ALA 259 VAL 260 0.0000

VAL 260 ARG 261 0.0219

ARG 261 ARG 262 -0.0001

ARG 262 LEU 263 0.0180

LEU 263 ARG 264 -0.0002

ARG 264 THR 265 0.0080

THR 265 ALA 266 -0.0002

ALA 266 CYS 267 0.0064

CYS 267 GLU 268 -0.0003

GLU 268 ARG 269 0.0030

ARG 269 ALA 270 -0.0001

ALA 270 LYS 271 0.0076

LYS 271 ARG 272 -0.0001

ARG 272 THR 273 0.0054

THR 273 LEU 274 -0.0002

LEU 274 SER 275 -0.0102

SER 275 SER 276 -0.0003

SER 276 SER 277 -0.0049

SER 277 THR 278 -0.0001

THR 278 GLN 279 -0.0057

GLN 279 ALA 280 -0.0002

ALA 280 SER 281 -0.0040

SER 281 LEU 282 0.0004

LEU 282 GLU 283 0.0055

GLU 283 ILE 284 0.0001

ILE 284 ASP 285 -0.0001

ASP 285 SER 286 0.0001

SER 286 LEU 287 0.0007

LEU 287 PHE 288 -0.0002

PHE 288 GLU 289 0.0063

GLU 289 GLY 290 -0.0001

GLY 290 ILE 291 -0.0004

ILE 291 ASP 292 -0.0001

ASP 292 PHE 293 -0.0052

PHE 293 TYR 294 0.0004

TYR 294 THR 295 -0.0108

THR 295 SER 296 0.0000

SER 296 ILE 297 -0.0088

ILE 297 THR 298 -0.0002

THR 298 ARG 299 -0.0123

ARG 299 ALA 300 0.0003

ALA 300 ARG 301 -0.0037

ARG 301 PHE 302 -0.0003

PHE 302 GLU 303 -0.0068

GLU 303 GLU 304 -0.0002

GLU 304 LEU 305 0.0010

LEU 305 CYS 306 0.0001

CYS 306 SER 307 -0.0014

SER 307 ASP 308 -0.0001

ASP 308 LEU 309 0.0011

LEU 309 PHE 310 -0.0002

PHE 310 ARG 311 0.0030

ARG 311 SER 312 0.0003

SER 312 THR 313 -0.0020

THR 313 LEU 314 -0.0004

LEU 314 GLU 315 0.0004

GLU 315 PRO 316 -0.0001

PRO 316 VAL 317 0.0012

VAL 317 GLU 318 -0.0004

GLU 318 LYS 319 0.0003

LYS 319 ALA 320 -0.0002

ALA 320 LEU 321 -0.0002

LEU 321 ARG 322 0.0003

ARG 322 ASP 323 -0.0006

ASP 323 ALA 324 0.0001

ALA 324 LYS 325 -0.0030

LYS 325 LEU 326 0.0002

LEU 326 ASP 327 -0.0013

ASP 327 LYS 328 0.0001

LYS 328 ALA 329 0.0004

ALA 329 GLN 330 -0.0002

GLN 330 ILE 331 0.0011

ILE 331 HIS 332 -0.0001

HIS 332 ASP 333 0.0021

ASP 333 LEU 334 0.0001

LEU 334 VAL 335 -0.0013

VAL 335 LEU 336 0.0001

LEU 336 VAL 337 0.0040

VAL 337 GLY 338 0.0001

GLY 338 GLY 339 -0.0025

GLY 339 SER 340 -0.0002

SER 340 THR 341 -0.0020

THR 341 ARG 342 0.0000

ARG 342 ILE 343 -0.0133

ILE 343 PRO 344 -0.0001

PRO 344 LYS 345 0.0056

LYS 345 VAL 346 -0.0001

VAL 346 GLN 347 -0.0062

GLN 347 LYS 348 -0.0001

LYS 348 LEU 349 0.0004

LEU 349 LEU 350 0.0003

LEU 350 GLN 351 0.0017

GLN 351 ASP 352 -0.0005

ASP 352 PHE 353 -0.0005

PHE 353 PHE 354 0.0003

PHE 354 ASN 355 -0.0011

ASN 355 GLY 356 0.0003

GLY 356 ARG 357 -0.0014

ARG 357 ASP 358 -0.0001

ASP 358 LEU 359 -0.0008

LEU 359 ASN 360 0.0003

ASN 360 LYS 361 0.0079

LYS 361 SER 362 0.0001

SER 362 ILE 363 -0.0014

ILE 363 ASN 364 -0.0003

ASN 364 PRO 365 0.0068

PRO 365 ASP 366 -0.0004

ASP 366 GLU 367 -0.0078

GLU 367 ALA 368 0.0002

ALA 368 VAL 369 0.0062

VAL 369 ALA 370 0.0003

ALA 370 TYR 371 0.0014

TYR 371 GLY 372 0.0002

GLY 372 ALA 373 0.0039

ALA 373 ALA 374 0.0001

ALA 374 VAL 375 -0.0147

VAL 375 GLN 376 0.0003

GLN 376 ALA 377 0.0107

ALA 377 ALA 378 -0.0003

ALA 378 ILE 379 0.0800

ILE 379 LEU 380 -0.0004

LEU 380 ILE 381 0.0383

ILE 381 LYS 382 0.0000

LYS 382 SER 383 -0.0293

SER 383 THR 384 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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** ***

CA strain for 2607070804273120202

--- normal mode 9 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* *