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

* VVWT DHQ *

CA strain for 2610090010133421365

--- normal mode 7 ---

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
GLU 6 THR 7 -0.0003

THR 7 VAL 8 0.0198

VAL 8 CYS 9 0.0001

CYS 9 VAL 10 -0.0016

VAL 10 THR 11 0.0001

THR 11 GLY 12 0.0237

GLY 12 ALA 13 -0.0003

ALA 13 SER 14 0.0148

SER 14 GLY 15 -0.0002

GLY 15 PHE 16 -0.1698

PHE 16 ILE 17 0.0000

ILE 17 GLY 18 -0.0667

GLY 18 SER 19 0.0003

SER 19 TRP 20 0.0154

TRP 20 LEU 21 0.0002

LEU 21 VAL 22 0.0295

VAL 22 MET 23 0.0002

MET 23 ARG 24 -0.0328

ARG 24 LEU 25 -0.0003

LEU 25 LEU 26 -0.0013

LEU 26 GLU 27 0.0002

GLU 27 ARG 28 -0.0707

ARG 28 GLY 29 0.0000

GLY 29 TYR 30 0.0066

TYR 30 THR 31 -0.0003

THR 31 VAL 32 0.0074

VAL 32 ARG 33 -0.0001

ARG 33 ALA 34 -0.0500

ALA 34 THR 35 0.0003

THR 35 VAL 36 -0.0246

VAL 36 ARG 37 -0.0001

ARG 37 ASP 38 0.1222

ASP 38 PRO 39 0.0000

PRO 39 THR 40 -0.0160

THR 40 ASN 41 0.0004

ASN 41 VAL 42 0.0284

VAL 42 LYS 43 0.0001

LYS 43 LYS 44 0.0623

LYS 44 VAL 45 0.0002

VAL 45 LYS 46 0.0414

LYS 46 HIS 47 0.0002

HIS 47 LEU 48 -0.0364

LEU 48 LEU 49 -0.0001

LEU 49 ASP 50 0.0175

ASP 50 LEU 51 0.0001

LEU 51 PRO 52 0.0216

PRO 52 LYS 53 0.0005

LYS 53 ALA 54 -0.0067

ALA 54 GLU 55 0.0001

GLU 55 THR 56 -0.0209

THR 56 HIS 57 -0.0001

HIS 57 LEU 58 0.0165

LEU 58 THR 59 0.0003

THR 59 LEU 60 0.0254

LEU 60 TRP 61 0.0004

TRP 61 LYS 62 0.1073

LYS 62 ALA 63 0.0002

ALA 63 ASP 64 0.0859

ASP 64 LEU 65 -0.0003

LEU 65 ALA 66 -0.0285

ALA 66 ASP 67 -0.0002

ASP 67 GLU 68 -0.0157

GLU 68 GLY 69 -0.0001

GLY 69 SER 70 -0.0033

SER 70 PHE 71 -0.0004

PHE 71 ASP 72 0.0060

ASP 72 GLU 73 -0.0004

GLU 73 ALA 74 0.0027

ALA 74 ILE 75 -0.0001

ILE 75 LYS 76 -0.0077

LYS 76 GLY 77 -0.0001

GLY 77 CYS 78 0.0400

CYS 78 THR 79 -0.0000

THR 79 GLY 80 0.0073

GLY 80 VAL 81 -0.0003

VAL 81 PHE 82 0.0090

PHE 82 HIS 83 0.0001

HIS 83 VAL 84 0.0615

VAL 84 ALA 85 -0.0001

ALA 85 THR 86 0.1307

THR 86 PRO 87 0.0003

PRO 87 MET 88 -0.1082

MET 88 ASP 89 0.0000

ASP 89 PHE 90 -0.0466

PHE 90 GLU 91 0.0001

GLU 91 SER 92 -0.0532

SER 92 LYS 93 -0.0000

LYS 93 ASP 94 0.0029

ASP 94 PRO 95 -0.0002

PRO 95 GLU 96 0.0181

GLU 96 ASN 97 0.0000

ASN 97 GLU 98 -0.0194

GLU 98 VAL 99 -0.0004

VAL 99 ILE 100 0.0110

ILE 100 LYS 101 -0.0000

LYS 101 PRO 102 0.0050

PRO 102 THR 103 0.0003

THR 103 ILE 104 0.0057

ILE 104 GLU 105 0.0001

GLU 105 GLY 106 0.0047

GLY 106 MET 107 -0.0001

MET 107 LEU 108 0.0192

LEU 108 GLY 109 0.0004

GLY 109 ILE 110 0.0063

ILE 110 MET 111 -0.0000

MET 111 LYS 112 0.0346

LYS 112 SER 113 -0.0002

SER 113 CYS 114 0.0210

CYS 114 ALA 115 -0.0001

ALA 115 ALA 116 0.0025

ALA 116 ALA 117 0.0000

ALA 117 LYS 118 -0.0051

LYS 118 THR 119 -0.0002

THR 119 VAL 120 0.0014

VAL 120 ARG 121 -0.0001

ARG 121 ARG 122 0.0123

ARG 122 LEU 123 -0.0001

LEU 123 VAL 124 0.0121

VAL 124 PHE 125 -0.0002

PHE 125 THR 126 0.0071

THR 126 SER 127 0.0001

SER 127 SER 128 -0.0142

SER 128 ALA 129 0.0001

ALA 129 GLY 130 -0.0110

GLY 130 THR 131 0.0001

THR 131 VAL 132 -0.0027

VAL 132 ASN 133 -0.0000

ASN 133 ILE 134 -0.0676

ILE 134 GLN 135 0.0002

GLN 135 GLU 136 0.0255

GLU 136 HIS 137 -0.0003

HIS 137 GLN 138 -0.0378

GLN 138 LEU 139 -0.0002

LEU 139 PRO 140 0.0066

PRO 140 VAL 141 0.0002

VAL 141 TYR 142 0.0169

TYR 142 ASP 143 0.0001

ASP 143 GLU 144 0.0334

GLU 144 SER 145 -0.0002

SER 145 CYS 146 -0.0649

CYS 146 TRP 147 0.0001

TRP 147 SER 148 -0.0655

SER 148 ASP 149 -0.0000

ASP 149 MET 150 -0.0150

MET 150 GLU 151 0.0001

GLU 151 PHE 152 0.0071

PHE 152 CYS 153 0.0001

CYS 153 ARG 154 -0.0174

ARG 154 ALA 155 0.0002

ALA 155 LYS 156 0.0334

LYS 156 LYS 157 0.0001

LYS 157 MET 158 -0.0359

MET 158 THR 159 -0.0001

THR 159 ALA 160 -0.2232

ALA 160 TRP 161 -0.0002

TRP 161 MET 162 -0.0926

MET 162 TYR 163 -0.0000

TYR 163 PHE 164 -0.0160

PHE 164 VAL 165 0.0002

VAL 165 SER 166 0.0520

SER 166 LYS 167 -0.0002

LYS 167 THR 168 0.0218

THR 168 LEU 169 0.0003

LEU 169 ALA 170 0.0176

ALA 170 GLU 171 0.0001

GLU 171 GLN 172 0.0234

GLN 172 ALA 173 0.0002

ALA 173 ALA 174 0.0073

ALA 174 TRP 175 0.0001

TRP 175 LYS 176 0.0453

LYS 176 TYR 177 0.0001

TYR 177 ALA 178 -0.0126

ALA 178 LYS 179 0.0004

LYS 179 GLU 180 0.0165

GLU 180 ASN 181 0.0000

ASN 181 ASN 182 0.0093

ASN 182 ILE 183 -0.0001

ILE 183 ASP 184 0.1021

ASP 184 PHE 185 0.0002

PHE 185 ILE 186 0.0367

ILE 186 THR 187 0.0002

THR 187 ILE 188 0.0070

ILE 188 ILE 189 -0.0002

ILE 189 PRO 190 -0.0025

PRO 190 THR 191 -0.0000

THR 191 LEU 192 0.1216

LEU 192 VAL 193 0.0002

VAL 193 VAL 194 0.0424

VAL 194 GLY 195 0.0001

GLY 195 PRO 196 0.0315

PRO 196 PHE 197 -0.0001

PHE 197 ILE 198 0.0624

ILE 198 MET 199 -0.0002

MET 199 SER 200 -0.0060

SER 200 SER 201 -0.0003

SER 201 MET 202 -0.1370

MET 202 PRO 203 -0.0001

PRO 203 PRO 204 0.0540

PRO 204 SER 205 -0.0003

SER 205 LEU 206 0.0474

LEU 206 ILE 207 0.0001

ILE 207 THR 208 0.0156

THR 208 ALA 209 -0.0000

ALA 209 LEU 210 0.0405

LEU 210 SER 211 0.0001

SER 211 PRO 212 -0.0576

PRO 212 ILE 213 0.0003

ILE 213 THR 214 0.0267

THR 214 GLY 215 -0.0000

GLY 215 ASN 216 0.0277

ASN 216 GLU 217 -0.0001

GLU 217 ALA 218 -0.0777

ALA 218 HIS 219 -0.0002

HIS 219 TYR 220 -0.1297

TYR 220 SER 221 0.0001

SER 221 ILE 222 0.0743

ILE 222 ILE 223 -0.0001

ILE 223 ARG 224 -0.1311

ARG 224 GLN 225 -0.0003

GLN 225 GLY 226 -0.0849

GLY 226 GLN 227 -0.0001

GLN 227 PHE 228 0.0339

PHE 228 VAL 229 0.0002

VAL 229 HIS 230 0.0304

HIS 230 LEU 231 -0.0004

LEU 231 ASP 232 0.0143

ASP 232 ASP 233 -0.0001

ASP 233 LEU 234 0.0124

LEU 234 CYS 235 0.0000

CYS 235 ASN 236 -0.0552

ASN 236 ALA 237 -0.0001

ALA 237 HIS 238 0.0284

HIS 238 ILE 239 -0.0001

ILE 239 TYR 240 -0.0706

TYR 240 LEU 241 -0.0000

LEU 241 PHE 242 0.0420

PHE 242 GLU 243 -0.0003

GLU 243 ASN 244 -0.0397

ASN 244 PRO 245 -0.0001

PRO 245 LYS 246 -0.0047

LYS 246 ALA 247 0.0001

ALA 247 GLU 248 -0.0340

GLU 248 GLY 249 -0.0000

GLY 249 ARG 250 -0.0595

ARG 250 TYR 251 -0.0000

TYR 251 ILE 252 0.0641

ILE 252 CYS 253 -0.0003

CYS 253 SER 254 0.0616

SER 254 SER 255 0.0001

SER 255 HIS 256 0.1556

HIS 256 ASP 257 0.0003

ASP 257 CYS 258 0.1768

CYS 258 ILE 259 0.0001

ILE 259 ILE 260 0.0396

ILE 260 LEU 261 -0.0002

LEU 261 ASP 262 0.0474

ASP 262 LEU 263 0.0001

LEU 263 ALA 264 0.0189

ALA 264 LYS 265 -0.0001

LYS 265 MET 266 0.1238

MET 266 LEU 267 0.0004

LEU 267 ARG 268 0.0195

ARG 268 GLU 269 0.0002

GLU 269 LYS 270 0.0605

LYS 270 TYR 271 -0.0001

TYR 271 PRO 272 0.0286

PRO 272 GLU 273 -0.0003

GLU 273 TYR 274 0.0085

TYR 274 ASN 275 -0.0001

ASN 275 ILE 276 0.0027

ILE 276 PRO 277 -0.0003

PRO 277 THR 278 -0.0398

THR 278 GLU 279 -0.0002

GLU 279 PHE 280 -0.0203

PHE 280 LYS 281 -0.0003

LYS 281 GLY 282 0.0231

GLY 282 VAL 283 -0.0004

VAL 283 ASP 284 -0.0407

ASP 284 GLU 285 0.0000

GLU 285 ASN 286 0.0528

ASN 286 LEU 287 0.0002

LEU 287 LYS 288 0.1130

LYS 288 SER 289 -0.0003

SER 289 VAL 290 -0.0423

VAL 290 CYS 291 -0.0003

CYS 291 PHE 292 0.1226

PHE 292 SER 293 0.0003

SER 293 SER 294 -0.0295

SER 294 LYS 295 0.0000

LYS 295 LYS 296 0.0459

LYS 296 LEU 297 -0.0001

LEU 297 THR 298 -0.0217

THR 298 ASP 299 -0.0001

ASP 299 LEU 300 0.0216

LEU 300 GLY 301 -0.0003

GLY 301 PHE 302 0.0010

PHE 302 GLU 303 0.0002

GLU 303 PHE 304 0.1032

PHE 304 LYS 305 -0.0000

LYS 305 TYR 306 0.0932

TYR 306 SER 307 0.0000

SER 307 LEU 308 0.1458

LEU 308 GLU 309 -0.0002

GLU 309 ASP 310 0.0395

ASP 310 MET 311 0.0001

MET 311 PHE 312 0.0339

PHE 312 THR 313 0.0002

THR 313 GLY 314 0.0473

GLY 314 ALA 315 -0.0002

ALA 315 VAL 316 0.0047

VAL 316 ASP 317 -0.0000

ASP 317 THR 318 0.0320

THR 318 CYS 319 -0.0001

CYS 319 ARG 320 0.0151

ARG 320 ALA 321 0.0003

ALA 321 LYS 322 0.0095

LYS 322 GLY 323 0.0003

GLY 323 LEU 324 0.0609

LEU 324 LEU 325 -0.0002

LEU 325 PRO 326 -0.0532

PRO 326 PRO 327 0.0001

PRO 327 SER 328 0.0070

SER 328 HIS 329 -0.0004

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.

*** VVWT DHQ ***

CA strain for 2610090010133421365

--- normal mode 7 ---

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

* VVWT DHQ *