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 8 ---

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 0.0003

ALA 4 ALA 5 0.0092

ALA 5 ALA 6 0.0002

ALA 6 ILE 7 0.0013

ILE 7 GLY 8 -0.0001

GLY 8 ILE 9 -0.0078

ILE 9 ASP 10 0.0001

ASP 10 LEU 11 -0.0173

LEU 11 GLY 12 -0.0001

GLY 12 THR 13 -0.0080

THR 13 THR 14 0.0000

THR 14 TYR 15 0.0032

TYR 15 SER 16 -0.0000

SER 16 CYS 17 -0.0018

CYS 17 VAL 18 0.0001

VAL 18 GLY 19 -0.0022

GLY 19 VAL 20 0.0000

VAL 20 PHE 21 -0.0038

PHE 21 GLN 22 0.0001

GLN 22 HIS 23 -0.0033

HIS 23 GLY 24 -0.0003

GLY 24 LYS 25 0.0064

LYS 25 VAL 26 0.0001

VAL 26 GLU 27 -0.0175

GLU 27 ILE 28 -0.0003

ILE 28 ILE 29 -0.0175

ILE 29 ALA 30 -0.0000

ALA 30 ASN 31 -0.0091

ASN 31 ASP 32 -0.0001

ASP 32 GLN 33 0.0030

GLN 33 GLY 34 0.0001

GLY 34 ASN 35 0.0048

ASN 35 ARG 36 0.0002

ARG 36 THR 37 0.0181

THR 37 THR 38 0.0003

THR 38 PRO 39 0.0113

PRO 39 SER 40 0.0001

SER 40 TYR 41 0.0010

TYR 41 VAL 42 -0.0001

VAL 42 ALA 43 0.0033

ALA 43 PHE 44 -0.0001

PHE 44 THR 45 0.0062

THR 45 ASP 46 0.0000

ASP 46 THR 47 0.0019

THR 47 GLU 48 0.0001

GLU 48 ARG 49 -0.0122

ARG 49 LEU 50 0.0003

LEU 50 ILE 51 -0.0213

ILE 51 GLY 52 -0.0000

GLY 52 ASP 53 0.0210

ASP 53 ALA 54 0.0001

ALA 54 ALA 55 -0.0412

ALA 55 LYS 56 -0.0002

LYS 56 ASN 57 -0.0006

ASN 57 GLN 58 0.0000

GLN 58 VAL 59 -0.0302

VAL 59 ALA 60 0.0002

ALA 60 LEU 61 0.0338

LEU 61 ASN 62 0.0000

ASN 62 PRO 63 -0.0140

PRO 63 GLN 64 -0.0000

GLN 64 ASN 65 -0.0027

ASN 65 THR 66 -0.0001

THR 66 VAL 67 0.0237

VAL 67 PHE 68 -0.0001

PHE 68 ASP 69 0.0335

ASP 69 ALA 70 0.0002

ALA 70 LYS 71 0.0060

LYS 71 ARG 72 -0.0002

ARG 72 LEU 73 -0.0443

LEU 73 ILE 74 0.0002

ILE 74 GLY 75 0.0072

GLY 75 ARG 76 -0.0000

ARG 76 LYS 77 0.0182

LYS 77 PHE 78 0.0003

PHE 78 GLY 79 0.0000

GLY 79 ASP 80 -0.0000

ASP 80 PRO 81 0.0053

PRO 81 VAL 82 0.0002

VAL 82 VAL 83 -0.0026

VAL 83 GLN 84 0.0002

GLN 84 SER 85 -0.0022

SER 85 ASP 86 0.0002

ASP 86 MET 87 0.0191

MET 87 LYS 88 -0.0001

LYS 88 HIS 89 -0.0257

HIS 89 TRP 90 -0.0001

TRP 90 PRO 91 0.0096

PRO 91 PHE 92 0.0002

PHE 92 GLN 93 -0.0398

GLN 93 VAL 94 0.0002

VAL 94 ILE 95 -0.0226

ILE 95 ASN 96 -0.0000

ASN 96 ASP 97 -0.0066

ASP 97 GLY 98 -0.0000

GLY 98 ASP 99 0.0013

ASP 99 LYS 100 -0.0000

LYS 100 PRO 101 -0.0069

PRO 101 LYS 102 -0.0000

LYS 102 VAL 103 -0.0111

VAL 103 GLN 104 -0.0002

GLN 104 VAL 105 0.0088

VAL 105 SER 106 0.0000

SER 106 TYR 107 0.0007

TYR 107 LYS 108 0.0002

LYS 108 GLY 109 -0.0038

GLY 109 GLU 110 -0.0003

GLU 110 THR 111 0.0156

THR 111 LYS 112 0.0002

LYS 112 ALA 113 0.0214

ALA 113 PHE 114 0.0004

PHE 114 TYR 115 0.0188

TYR 115 PRO 116 0.0002

PRO 116 GLU 117 -0.0109

GLU 117 GLU 118 -0.0001

GLU 118 ILE 119 -0.0056

ILE 119 SER 120 0.0003

SER 120 SER 121 -0.0049

SER 121 MET 122 0.0001

MET 122 VAL 123 -0.0009

VAL 123 LEU 124 -0.0001

LEU 124 THR 125 0.0059

THR 125 LYS 126 0.0000

LYS 126 MET 127 -0.0140

MET 127 LYS 128 -0.0002

LYS 128 GLU 129 0.0077

GLU 129 ILE 130 -0.0001

ILE 130 ALA 131 0.0052

ALA 131 GLU 132 -0.0006

GLU 132 ALA 133 -0.0047

ALA 133 TYR 134 -0.0003

TYR 134 LEU 135 0.0081

LEU 135 GLY 136 -0.0002

GLY 136 TYR 137 -0.0021

TYR 137 PRO 138 -0.0002

PRO 138 VAL 139 -0.0061

VAL 139 THR 140 0.0000

THR 140 ASN 141 -0.0021

ASN 141 ALA 142 0.0002

ALA 142 VAL 143 -0.0108

VAL 143 ILE 144 -0.0001

ILE 144 THR 145 -0.0096

THR 145 VAL 146 0.0001

VAL 146 PRO 147 -0.0258

PRO 147 ALA 148 -0.0000

ALA 148 TYR 149 0.0151

TYR 149 PHE 150 0.0001

PHE 150 ASN 151 -0.0350

ASN 151 ASP 152 -0.0004

ASP 152 SER 153 0.0012

SER 153 GLN 154 0.0000

GLN 154 ARG 155 0.0245

ARG 155 GLN 156 0.0000

GLN 156 ALA 157 0.0091

ALA 157 THR 158 0.0002

THR 158 LYS 159 -0.0041

LYS 159 ASP 160 0.0001

ASP 160 ALA 161 0.0004

ALA 161 GLY 162 -0.0000

GLY 162 VAL 163 0.0048

VAL 163 ILE 164 -0.0006

ILE 164 ALA 165 -0.0021

ALA 165 GLY 166 -0.0001

GLY 166 LEU 167 0.0067

LEU 167 ASN 168 -0.0001

ASN 168 VAL 169 -0.0066

VAL 169 LEU 170 -0.0002

LEU 170 ARG 171 -0.0202

ARG 171 ILE 172 -0.0002

ILE 172 ILE 173 0.0225

ILE 173 ASN 174 0.0004

ASN 174 GLU 175 0.0134

GLU 175 PRO 176 0.0002

PRO 176 THR 177 -0.0024

THR 177 ALA 178 0.0000

ALA 178 ALA 179 0.0197

ALA 179 ALA 180 0.0003

ALA 180 ILE 181 -0.0287

ILE 181 ALA 182 0.0001

ALA 182 TYR 183 -0.0045

TYR 183 GLY 184 -0.0000

GLY 184 LEU 185 -0.0308

LEU 185 ASP 186 0.0001

ASP 186 ARG 187 -0.0022

ARG 187 THR 188 0.0001

THR 188 GLY 189 0.0031

GLY 189 LYS 190 -0.0003

LYS 190 GLY 191 -0.0005

GLY 191 GLU 192 0.0001

GLU 192 ARG 193 0.0066

ARG 193 ASN 194 -0.0001

ASN 194 VAL 195 -0.0030

VAL 195 LEU 196 0.0002

LEU 196 ILE 197 0.0025

ILE 197 PHE 198 -0.0002

PHE 198 ASP 199 -0.0108

ASP 199 LEU 200 -0.0001

LEU 200 GLY 201 -0.0068

GLY 201 GLY 202 -0.0001

GLY 202 GLY 203 -0.0251

GLY 203 THR 204 0.0001

THR 204 PHE 205 0.0359

PHE 205 ASP 206 -0.0001

ASP 206 VAL 207 -0.0133

VAL 207 SER 208 -0.0000

SER 208 ILE 209 -0.0094

ILE 209 LEU 210 0.0000

LEU 210 THR 211 -0.0019

THR 211 ILE 212 0.0001

ILE 212 ASP 213 -0.0023

ASP 213 ASP 214 -0.0000

ASP 214 GLY 215 0.0014

GLY 215 ILE 216 -0.0003

ILE 216 PHE 217 -0.0016

PHE 217 GLU 218 0.0000

GLU 218 VAL 219 0.0019

VAL 219 LYS 220 -0.0003

LYS 220 ALA 221 -0.0217

ALA 221 THR 222 0.0000

THR 222 ALA 223 -0.0578

ALA 223 GLY 224 0.0003

GLY 224 ASP 225 -0.0337

ASP 225 THR 226 0.0003

THR 226 HIS 227 -0.1011

HIS 227 LEU 228 -0.0001

LEU 228 GLY 229 0.0293

GLY 229 GLY 230 -0.0002

GLY 230 GLU 231 -0.0333

GLU 231 ASP 232 -0.0001

ASP 232 PHE 233 -0.0576

PHE 233 ASP 234 0.0002

ASP 234 ASN 235 0.0331

ASN 235 ARG 236 -0.0001

ARG 236 LEU 237 -0.0589

LEU 237 VAL 238 -0.0002

VAL 238 ASN 239 0.1039

ASN 239 HIS 240 -0.0003

HIS 240 PHE 241 -0.0651

PHE 241 VAL 242 -0.0000

VAL 242 GLU 243 0.0611

GLU 243 GLU 244 -0.0000

GLU 244 PHE 245 -0.0114

PHE 245 LYS 246 0.0000

LYS 246 ARG 247 0.0232

ARG 247 LYS 248 -0.0002

LYS 248 HIS 249 -0.0339

HIS 249 LYS 250 -0.0000

LYS 250 LYS 251 -0.0198

LYS 251 ASP 252 -0.0002

ASP 252 ILE 253 0.0138

ILE 253 SER 254 0.0004

SER 254 GLN 255 -0.0026

GLN 255 ASN 256 0.0000

ASN 256 LYS 257 -0.0284

LYS 257 ARG 258 -0.0001

ARG 258 ALA 259 0.0184

ALA 259 VAL 260 0.0000

VAL 260 ARG 261 -0.0135

ARG 261 ARG 262 0.0003

ARG 262 LEU 263 -0.1075

LEU 263 ARG 264 -0.0001

ARG 264 THR 265 0.0709

THR 265 ALA 266 -0.0001

ALA 266 CYS 267 0.0008

CYS 267 GLU 268 -0.0001

GLU 268 ARG 269 -0.0126

ARG 269 ALA 270 -0.0002

ALA 270 LYS 271 0.0034

LYS 271 ARG 272 -0.0002

ARG 272 THR 273 0.0493

THR 273 LEU 274 -0.0002

LEU 274 SER 275 0.1530

SER 275 SER 276 -0.0001

SER 276 SER 277 0.0972

SER 277 THR 278 0.0002

THR 278 GLN 279 0.0790

GLN 279 ALA 280 0.0003

ALA 280 SER 281 0.1764

SER 281 LEU 282 -0.0002

LEU 282 GLU 283 0.0286

GLU 283 ILE 284 -0.0001

ILE 284 ASP 285 0.0332

ASP 285 SER 286 -0.0001

SER 286 LEU 287 -0.0342

LEU 287 PHE 288 0.0001

PHE 288 GLU 289 0.0113

GLU 289 GLY 290 0.0000

GLY 290 ILE 291 0.0051

ILE 291 ASP 292 -0.0001

ASP 292 PHE 293 -0.0240

PHE 293 TYR 294 0.0002

TYR 294 THR 295 -0.0143

THR 295 SER 296 0.0000

SER 296 ILE 297 -0.0083

ILE 297 THR 298 0.0002

THR 298 ARG 299 0.0638

ARG 299 ALA 300 -0.0001

ALA 300 ARG 301 0.0115

ARG 301 PHE 302 0.0002

PHE 302 GLU 303 -0.0147

GLU 303 GLU 304 0.0001

GLU 304 LEU 305 0.0379

LEU 305 CYS 306 -0.0001

CYS 306 SER 307 -0.0136

SER 307 ASP 308 0.0001

ASP 308 LEU 309 0.0205

LEU 309 PHE 310 -0.0001

PHE 310 ARG 311 -0.0060

ARG 311 SER 312 -0.0002

SER 312 THR 313 -0.0110

THR 313 LEU 314 -0.0001

LEU 314 GLU 315 0.0324

GLU 315 PRO 316 -0.0000

PRO 316 VAL 317 0.0032

VAL 317 GLU 318 -0.0001

GLU 318 LYS 319 0.0201

LYS 319 ALA 320 -0.0001

ALA 320 LEU 321 0.0150

LEU 321 ARG 322 -0.0000

ARG 322 ASP 323 -0.0002

ASP 323 ALA 324 0.0003

ALA 324 LYS 325 0.0091

LYS 325 LEU 326 -0.0001

LEU 326 ASP 327 0.0200

ASP 327 LYS 328 -0.0001

LYS 328 ALA 329 -0.0047

ALA 329 GLN 330 -0.0000

GLN 330 ILE 331 0.0033

ILE 331 HIS 332 0.0003

HIS 332 ASP 333 -0.0006

ASP 333 LEU 334 -0.0002

LEU 334 VAL 335 -0.0093

VAL 335 LEU 336 0.0002

LEU 336 VAL 337 -0.0234

VAL 337 GLY 338 -0.0001

GLY 338 GLY 339 0.0373

GLY 339 SER 340 -0.0003

SER 340 THR 341 -0.0172

THR 341 ARG 342 0.0002

ARG 342 ILE 343 0.0996

ILE 343 PRO 344 -0.0001

PRO 344 LYS 345 -0.0039

LYS 345 VAL 346 -0.0003

VAL 346 GLN 347 0.0005

GLN 347 LYS 348 -0.0003

LYS 348 LEU 349 0.0145

LEU 349 LEU 350 0.0001

LEU 350 GLN 351 -0.0127

GLN 351 ASP 352 -0.0001

ASP 352 PHE 353 0.0081

PHE 353 PHE 354 -0.0001

PHE 354 ASN 355 0.0035

ASN 355 GLY 356 -0.0001

GLY 356 ARG 357 -0.0013

ARG 357 ASP 358 0.0000

ASP 358 LEU 359 -0.0143

LEU 359 ASN 360 0.0000

ASN 360 LYS 361 -0.0013

LYS 361 SER 362 0.0000

SER 362 ILE 363 -0.0006

ILE 363 ASN 364 -0.0000

ASN 364 PRO 365 -0.0171

PRO 365 ASP 366 0.0004

ASP 366 GLU 367 0.0563

GLU 367 ALA 368 0.0002

ALA 368 VAL 369 0.0060

VAL 369 ALA 370 0.0002

ALA 370 TYR 371 -0.0203

TYR 371 GLY 372 0.0000

GLY 372 ALA 373 0.0101

ALA 373 ALA 374 -0.0001

ALA 374 VAL 375 -0.0272

VAL 375 GLN 376 -0.0001

GLN 376 ALA 377 -0.0123

ALA 377 ALA 378 0.0002

ALA 378 ILE 379 0.0010

ILE 379 LEU 380 -0.0001

LEU 380 ILE 381 0.0040

ILE 381 LYS 382 -0.0001

LYS 382 SER 383 -0.0794

SER 383 THR 384 0.0000

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 8 ---

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

* *