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

* 01-JUN-22 *

CA strain for 23010311011276112

--- normal mode 10 ---

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 ASN 3 -0.0015

ASN 3 THR 4 0.0002

THR 4 THR 5 -0.0327

THR 5 THR 6 0.0001

THR 6 PRO 7 0.0261

PRO 7 GLN 8 -0.0001

GLN 8 PRO 9 -0.0154

PRO 9 SER 10 0.0002

SER 10 ASP 11 -0.0020

ASP 11 LEU 12 -0.0000

LEU 12 PRO 13 0.0305

PRO 13 SER 14 -0.0001

SER 14 THR 15 -0.0259

THR 15 ARG 16 0.0001

ARG 16 GLU 17 -0.0053

GLU 17 LYS 18 0.0000

LYS 18 ILE 19 0.0518

ILE 19 HIS 20 -0.0000

HIS 20 GLN 21 -0.0000

GLN 21 ARG 22 -0.0001

ARG 22 PHE 23 0.0059

PHE 23 MET 24 -0.0000

MET 24 ARG 25 -0.0107

ARG 25 LEU 26 -0.0002

LEU 26 ALA 27 0.0019

ALA 27 LEU 28 0.0001

LEU 28 ALA 29 0.0009

ALA 29 GLN 30 -0.0002

GLN 30 ALA 31 -0.0018

ALA 31 ARG 32 -0.0002

ARG 32 LEU 33 0.0012

LEU 33 SER 34 -0.0001

SER 34 PRO 35 -0.0050

PRO 35 PRO 36 0.0001

PRO 36 MET 37 -0.0191

MET 37 SER 38 -0.0000

SER 38 THR 39 -0.0217

THR 39 LYS 40 -0.0001

LYS 40 TYR 41 0.0112

TYR 41 SER 42 0.0003

SER 42 VAL 43 0.0028

VAL 43 GLY 44 0.0001

GLY 44 ALA 45 -0.0004

ALA 45 LEU 46 -0.0000

LEU 46 LEU 47 0.0007

LEU 47 VAL 48 -0.0003

VAL 48 ASP 49 -0.0010

ASP 49 SER 50 -0.0002

SER 50 ASP 51 -0.0016

ASP 51 GLY 52 -0.0002

GLY 52 ASN 53 0.0001

ASN 53 GLU 54 -0.0001

GLU 54 ILE 55 -0.0025

ILE 55 LEU 56 -0.0002

LEU 56 SER 57 -0.0019

SER 57 THR 58 0.0004

THR 58 GLY 59 -0.0013

GLY 59 TYR 60 0.0000

TYR 60 SER 61 0.0054

SER 61 LEU 62 0.0002

LEU 62 GLU 63 0.0045

GLU 63 LEU 64 -0.0000

LEU 64 PRO 65 0.0026

PRO 65 ALA 66 -0.0001

ALA 66 MET 67 0.0003

MET 67 HIS 68 0.0001

HIS 68 ALA 69 0.0015

ALA 69 GLU 70 -0.0001

GLU 70 GLN 71 -0.0017

GLN 71 CYS 72 0.0001

CYS 72 CYS 73 0.0019

CYS 73 LEU 74 -0.0004

LEU 74 ALA 75 -0.0002

ALA 75 LYS 76 0.0000

LYS 76 ILE 77 0.0006

ILE 77 ALA 78 0.0004

ALA 78 ALA 79 -0.0013

ALA 79 ALA 80 -0.0001

ALA 80 HIS 81 0.0001

HIS 81 ASP 82 0.0003

ASP 82 VAL 83 -0.0013

VAL 83 PRO 84 0.0003

PRO 84 GLU 85 -0.0000

GLU 85 GLU 86 0.0001

GLU 86 ARG 87 0.0013

ARG 87 VAL 88 0.0005

VAL 88 ALA 89 -0.0014

ALA 89 GLU 90 -0.0001

GLU 90 VAL 91 0.0007

VAL 91 LEU 92 -0.0002

LEU 92 PRO 93 0.0010

PRO 93 PRO 94 -0.0002

PRO 94 ARG 95 -0.0014

ARG 95 THR 96 0.0003

THR 96 VAL 97 -0.0048

VAL 97 LEU 98 -0.0003

LEU 98 TYR 99 -0.0008

TYR 99 THR 100 0.0002

THR 100 THR 101 -0.0005

THR 101 MET 102 0.0001

MET 102 GLU 103 0.0008

GLU 103 PRO 104 -0.0001

PRO 104 CYS 105 -0.0003

CYS 105 SER 106 -0.0001

SER 106 GLU 107 -0.0003

GLU 107 ARG 108 0.0002

ARG 108 LEU 109 -0.0024

LEU 109 SER 110 0.0000

SER 110 GLY 111 0.0025

GLY 111 ARG 112 0.0001

ARG 112 ARG 113 0.0021

ARG 113 ALA 114 -0.0002

ALA 114 CYS 115 -0.0007

CYS 115 ALA 116 0.0003

ALA 116 ASP 117 -0.0014

ASP 117 ARG 118 -0.0001

ARG 118 ILE 119 0.0001

ILE 119 LEU 120 -0.0004

LEU 120 ALA 121 -0.0021

ALA 121 LEU 122 -0.0003

LEU 122 LYS 123 0.0000

LYS 123 GLY 124 -0.0003

GLY 124 ALA 125 0.0004

ALA 125 VAL 126 -0.0001

VAL 126 GLY 127 -0.0065

GLY 127 ILE 128 0.0001

ILE 128 VAL 129 -0.0002

VAL 129 TYR 130 -0.0000

TYR 130 VAL 131 0.0020

VAL 131 GLY 132 -0.0002

GLY 132 ILE 133 -0.0040

ILE 133 ALA 134 -0.0001

ALA 134 GLU 135 0.0094

GLU 135 PRO 136 -0.0000

PRO 136 ASP 137 0.0334

ASP 137 VAL 138 0.0001

VAL 138 PHE 139 0.0014

PHE 139 VAL 140 -0.0001

VAL 140 ALA 141 -0.0003

ALA 141 ARG 142 0.0001

ARG 142 LEU 143 -0.0003

LEU 143 ASP 144 0.0003

ASP 144 GLY 145 0.0003

GLY 145 THR 146 0.0001

THR 146 ARG 147 0.0003

ARG 147 GLN 148 -0.0001

GLN 148 PRO 149 0.0011

PRO 149 PHE 150 0.0001

PHE 150 PHE 151 0.0050

PHE 151 MET 152 -0.0001

MET 152 LYS 153 0.0030

LYS 153 VAL 154 0.0001

VAL 154 ILE 155 0.0028

ILE 155 ASN 156 0.0002

ASN 156 HIS 157 0.0002

HIS 157 GLU 158 0.0001

GLU 158 ILE 159 -0.0014

ILE 159 GLY 160 -0.0000

GLY 160 ARG 161 0.0007

ARG 161 LYS 162 0.0002

LYS 162 MET 163 0.0001

MET 163 VAL 164 -0.0001

VAL 164 HIS 165 0.0012

HIS 165 GLY 166 -0.0003

GLY 166 GLU 167 0.0005

GLU 167 PHE 168 0.0001

PHE 168 GLU 169 -0.0010

GLU 169 SER 170 0.0002

SER 170 MET 171 -0.0000

MET 171 LYS 172 0.0005

LYS 172 ALA 173 -0.0016

ALA 173 ILE 174 0.0000

ILE 174 TYR 175 -0.0014

TYR 175 GLU 176 -0.0002

GLU 176 VAL 177 -0.0008

VAL 177 SER 178 -0.0000

SER 178 PRO 179 -0.0025

PRO 179 ALA 180 0.0001

ALA 180 PHE 181 0.0001

PHE 181 ALA 182 -0.0000

ALA 182 PRO 183 -0.0016

PRO 183 LYS 184 0.0002

LYS 184 PRO 185 -0.0006

PRO 185 VAL 186 -0.0001

VAL 186 ALA 187 0.0006

ALA 187 TRP 188 0.0002

TRP 188 GLY 189 0.0019

GLY 189 THR 190 -0.0000

THR 190 TYR 191 0.0003

TYR 191 GLN 192 0.0002

GLN 192 CYS 193 0.0006

CYS 193 LEU 194 0.0000

LEU 194 PRO 195 0.0002

PRO 195 ASP 196 0.0002

ASP 196 THR 197 -0.0002

THR 197 HIS 198 -0.0002

HIS 198 PHE 199 0.0007

PHE 199 PHE 200 -0.0003

PHE 200 LEU 201 0.0006

LEU 201 CYS 202 0.0004

CYS 202 GLU 203 0.0023

GLU 203 PHE 204 0.0001

PHE 204 ARG 205 -0.0009

ARG 205 ASN 206 -0.0000

ASN 206 MET 207 0.0007

MET 207 LYS 208 0.0002

LYS 208 GLU 209 -0.0262

GLU 209 GLU 210 0.0001

GLU 210 LYS 211 0.0105

LYS 211 PRO 212 -0.0005

PRO 212 ASP 213 0.0014

ASP 213 PRO 214 0.0000

PRO 214 GLY 215 0.0003

GLY 215 GLU 216 -0.0002

GLU 216 PHE 217 -0.0004

PHE 217 GLY 218 0.0001

GLY 218 SER 219 0.0007

SER 219 ARG 220 0.0002

ARG 220 LEU 221 -0.0005

LEU 221 ALA 222 -0.0002

ALA 222 ALA 223 0.0003

ALA 223 LEU 224 0.0002

LEU 224 HIS 225 -0.0005

HIS 225 GLN 226 0.0003

GLN 226 ASP 227 -0.0000

ASP 227 SER 228 0.0004

SER 228 GLN 229 -0.0009

GLN 229 SER 230 0.0004

SER 230 PRO 231 0.0001

PRO 231 ASN 232 -0.0000

ASN 232 GLY 233 0.0000

GLY 233 LYS 234 -0.0002

LYS 234 PHE 235 0.0005

PHE 235 GLY 236 0.0004

GLY 236 PHE 237 -0.0009

PHE 237 HIS 238 0.0001

HIS 238 VAL 239 0.0008

VAL 239 ALA 240 0.0004

ALA 240 THR 241 0.0002

THR 241 TYR 242 -0.0000

TYR 242 SER 243 -0.0005

SER 243 GLY 244 -0.0001

GLY 244 ASN 245 -0.0020

ASN 245 LEU 246 -0.0001

LEU 246 PRO 247 0.0004

PRO 247 GLN 248 -0.0002

GLN 248 VAL 249 0.0007

VAL 249 ASN 250 -0.0004

ASN 250 ASP 251 0.0004

ASP 251 TRP 252 0.0001

TRP 252 GLU 253 0.0000

GLU 253 ASP 254 0.0002

ASP 254 SER 255 0.0005

SER 255 TRP 256 -0.0003

TRP 256 GLU 257 -0.0010

GLU 257 VAL 258 -0.0000

VAL 258 PHE 259 0.0001

PHE 259 PHE 260 -0.0002

PHE 260 THR 261 -0.0004

THR 261 LYS 262 -0.0002

LYS 262 ASN 263 0.0004

ASN 263 LEU 264 0.0000

LEU 264 LYS 265 0.0002

LYS 265 LEU 266 0.0001

LEU 266 ALA 267 0.0002

ALA 267 LEU 268 0.0004

LEU 268 LYS 269 0.0001

LYS 269 PHE 270 -0.0000

PHE 270 GLU 271 0.0004

GLU 271 ILE 272 0.0002

ILE 272 GLU 273 0.0002

GLU 273 ALA 274 0.0001

ALA 274 LYS 275 0.0004

LYS 275 GLY 276 -0.0003

GLY 276 PRO 277 -0.0000

PRO 277 ASP 278 0.0002

ASP 278 ALA 279 0.0005

ALA 279 GLU 280 0.0001

GLU 280 LEU 281 0.0008

LEU 281 ASP 282 0.0000

ASP 282 THR 283 0.0005

THR 283 LEU 284 -0.0003

LEU 284 LEU 285 0.0001

LEU 285 PRO 286 -0.0001

PRO 286 VAL 287 0.0005

VAL 287 LEU 288 -0.0001

LEU 288 PHE 289 0.0003

PHE 289 ASP 290 -0.0001

ASP 290 LYS 291 0.0006

LYS 291 VAL 292 -0.0002

VAL 292 ILE 293 -0.0005

ILE 293 PRO 294 -0.0002

PRO 294 ARG 295 0.0002

ARG 295 LEU 296 0.0001

LEU 296 LEU 297 -0.0002

LEU 297 GLN 298 0.0000

GLN 298 PRO 299 -0.0002

PRO 299 LEU 300 0.0000

LEU 300 GLU 301 0.0009

GLU 301 SER 302 0.0001

SER 302 ASP 303 -0.0002

ASP 303 GLY 304 -0.0001

GLY 304 ARG 305 0.0002

ARG 305 SER 306 -0.0004

SER 306 VAL 307 -0.0002

VAL 307 LYS 308 -0.0001

LYS 308 PRO 309 0.0005

PRO 309 SER 310 -0.0002

SER 310 LEU 311 -0.0008

LEU 311 VAL 312 -0.0002

VAL 312 HIS 313 0.0003

HIS 313 GLY 314 -0.0000

GLY 314 ASP 315 0.0013

ASP 315 LEU 316 -0.0001

LEU 316 TRP 317 0.0054

TRP 317 TYR 318 -0.0000

TYR 318 GLY 319 -0.0041

GLY 319 ASN 320 0.0002

ASN 320 SER 321 0.0009

SER 321 GLY 322 0.0001

GLY 322 ILE 323 0.0015

ILE 323 ASP 324 0.0004

ASP 324 THR 325 0.0013

THR 325 THR 326 0.0002

THR 326 THR 327 -0.0007

THR 327 GLY 328 -0.0002

GLY 328 GLU 329 -0.0010

GLU 329 SER 330 -0.0000

SER 330 LEU 331 -0.0017

LEU 331 ILE 332 0.0001

ILE 332 PHE 333 -0.0017

PHE 333 ASP 334 0.0003

ASP 334 ALA 335 0.0003

ALA 335 CYS 336 -0.0002

CYS 336 CYS 337 -0.0001

CYS 337 PHE 338 0.0001

PHE 338 TYR 339 -0.0003

TYR 339 ALA 340 -0.0003

ALA 340 HIS 341 0.0001

HIS 341 ASN 342 0.0005

ASN 342 GLU 343 -0.0003

GLU 343 TYR 344 0.0000

TYR 344 GLU 345 0.0014

GLU 345 PHE 346 0.0001

PHE 346 GLY 347 -0.0000

GLY 347 GLN 348 -0.0000

GLN 348 TRP 349 -0.0009

TRP 349 MET 350 0.0002

MET 350 PRO 351 0.0001

PRO 351 ALA 352 -0.0002

ALA 352 CYS 353 0.0003

CYS 353 ASN 354 -0.0001

ASN 354 ARG 355 -0.0014

ARG 355 PHE 356 0.0004

PHE 356 GLY 357 0.0012

GLY 357 PRO 358 0.0002

PRO 358 GLU 359 -0.0002

GLU 359 TYR 360 0.0004

TYR 360 ARG 361 0.0020

ARG 361 GLU 362 -0.0002

GLU 362 ALA 363 -0.0014

ALA 363 TYR 364 0.0003

TYR 364 HIS 365 0.0002

HIS 365 SER 366 0.0001

SER 366 SER 367 0.0002

SER 367 VAL 368 0.0003

VAL 368 GLU 369 -0.0017

GLU 369 ILE 370 0.0004

ILE 370 SER 371 0.0001

SER 371 HIS 372 0.0005

HIS 372 PRO 373 -0.0001

PRO 373 LYS 374 0.0003

LYS 374 GLU 375 -0.0006

GLU 375 ASP 376 -0.0002

ASP 376 TYR 377 0.0009

TYR 377 LYS 378 -0.0001

LYS 378 GLY 379 -0.0004

GLY 379 ARG 380 0.0001

ARG 380 LEU 381 0.0017

LEU 381 ASP 382 -0.0000

ASP 382 LEU 383 0.0003

LEU 383 TYR 384 0.0002

TYR 384 LYS 385 0.0007

LYS 385 LEU 386 0.0003

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: October 18th, 2018.

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

*** 01-JUN-22 ***

CA strain for 23010311011276112

--- normal mode 10 ---

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

* 01-JUN-22 *