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

* VvWTDHK *

CA strain for 2610090002023416476

--- 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
GLU 6 THR 7 0.0000

THR 7 VAL 8 0.0333

VAL 8 CYS 9 -0.0000

CYS 9 VAL 10 0.0009

VAL 10 THR 11 -0.0001

THR 11 GLY 12 0.0678

GLY 12 ALA 13 0.0001

ALA 13 SER 14 0.0150

SER 14 GLY 15 0.0001

GLY 15 PHE 16 -0.1491

PHE 16 ILE 17 -0.0005

ILE 17 GLY 18 -0.0916

GLY 18 SER 19 0.0000

SER 19 TRP 20 0.0500

TRP 20 LEU 21 0.0002

LEU 21 VAL 22 0.0134

VAL 22 MET 23 -0.0001

MET 23 ARG 24 0.0047

ARG 24 LEU 25 -0.0000

LEU 25 LEU 26 0.0307

LEU 26 GLU 27 0.0003

GLU 27 ARG 28 -0.0426

ARG 28 GLY 29 0.0000

GLY 29 TYR 30 0.0135

TYR 30 THR 31 0.0002

THR 31 VAL 32 0.0223

VAL 32 ARG 33 -0.0001

ARG 33 ALA 34 -0.0324

ALA 34 THR 35 -0.0002

THR 35 VAL 36 0.0452

VAL 36 ARG 37 0.0003

ARG 37 ASP 38 0.0791

ASP 38 PRO 39 0.0001

PRO 39 THR 40 -0.0085

THR 40 ASN 41 0.0001

ASN 41 VAL 42 0.0338

VAL 42 LYS 43 0.0002

LYS 43 LYS 44 0.0249

LYS 44 VAL 45 0.0001

VAL 45 LYS 46 0.0481

LYS 46 HIS 47 0.0002

HIS 47 LEU 48 -0.0660

LEU 48 LEU 49 0.0000

LEU 49 ASP 50 0.0246

ASP 50 LEU 51 -0.0003

LEU 51 PRO 52 -0.0213

PRO 52 LYS 53 0.0002

LYS 53 ALA 54 0.0099

ALA 54 GLU 55 0.0000

GLU 55 THR 56 -0.0191

THR 56 HIS 57 0.0003

HIS 57 LEU 58 0.0210

LEU 58 THR 59 -0.0002

THR 59 LEU 60 0.0533

LEU 60 TRP 61 -0.0003

TRP 61 LYS 62 0.0679

LYS 62 ALA 63 0.0000

ALA 63 ASP 64 0.0013

ASP 64 LEU 65 0.0000

LEU 65 ALA 66 0.0053

ALA 66 ASP 67 -0.0000

ASP 67 GLU 68 -0.0059

GLU 68 GLY 69 -0.0003

GLY 69 SER 70 -0.0138

SER 70 PHE 71 0.0001

PHE 71 ASP 72 0.0008

ASP 72 GLU 73 -0.0003

GLU 73 ALA 74 0.0063

ALA 74 ILE 75 0.0001

ILE 75 LYS 76 -0.0265

LYS 76 GLY 77 -0.0000

GLY 77 CYS 78 0.0355

CYS 78 THR 79 0.0000

THR 79 GLY 80 0.0106

GLY 80 VAL 81 -0.0001

VAL 81 PHE 82 0.0050

PHE 82 HIS 83 -0.0001

HIS 83 VAL 84 0.1120

VAL 84 ALA 85 -0.0003

ALA 85 THR 86 0.3448

THR 86 PRO 87 0.0001

PRO 87 MET 88 0.0352

MET 88 ASP 89 -0.0002

ASP 89 PHE 90 -0.0299

PHE 90 GLU 91 -0.0001

GLU 91 SER 92 -0.0306

SER 92 LYS 93 -0.0002

LYS 93 ASP 94 -0.0673

ASP 94 PRO 95 -0.0004

PRO 95 GLU 96 -0.0300

GLU 96 ASN 97 -0.0001

ASN 97 GLU 98 0.0286

GLU 98 VAL 99 0.0001

VAL 99 ILE 100 -0.0418

ILE 100 LYS 101 -0.0004

LYS 101 PRO 102 0.1065

PRO 102 THR 103 0.0000

THR 103 ILE 104 0.0221

ILE 104 GLU 105 -0.0001

GLU 105 GLY 106 0.0686

GLY 106 MET 107 0.0003

MET 107 LEU 108 0.0370

LEU 108 GLY 109 0.0001

GLY 109 ILE 110 0.0110

ILE 110 MET 111 -0.0004

MET 111 LYS 112 0.0415

LYS 112 SER 113 -0.0003

SER 113 CYS 114 0.0118

CYS 114 ALA 115 0.0003

ALA 115 ALA 116 0.0520

ALA 116 ALA 117 0.0004

ALA 117 LYS 118 0.0269

LYS 118 THR 119 0.0004

THR 119 VAL 120 0.0356

VAL 120 ARG 121 -0.0004

ARG 121 ARG 122 0.0408

ARG 122 LEU 123 0.0002

LEU 123 VAL 124 0.0034

VAL 124 PHE 125 0.0005

PHE 125 THR 126 0.0136

THR 126 SER 127 0.0000

SER 127 SER 128 -0.0407

SER 128 ALA 129 -0.0001

ALA 129 GLY 130 0.0237

GLY 130 THR 131 -0.0003

THR 131 VAL 132 -0.0204

VAL 132 ASN 133 -0.0001

ASN 133 ILE 134 0.0011

ILE 134 GLN 135 0.0000

GLN 135 GLU 136 0.0212

GLU 136 HIS 137 0.0001

HIS 137 GLN 138 0.0601

GLN 138 LEU 139 0.0001

LEU 139 PRO 140 -0.0278

PRO 140 VAL 141 0.0001

VAL 141 TYR 142 0.0973

TYR 142 ASP 143 0.0000

ASP 143 GLU 144 0.1258

GLU 144 SER 145 -0.0000

SER 145 CYS 146 -0.0817

CYS 146 TRP 147 -0.0001

TRP 147 SER 148 -0.1079

SER 148 ASP 149 0.0001

ASP 149 MET 150 -0.0458

MET 150 GLU 151 -0.0001

GLU 151 PHE 152 0.0035

PHE 152 CYS 153 -0.0003

CYS 153 ARG 154 -0.0434

ARG 154 ALA 155 0.0003

ALA 155 LYS 156 0.0808

LYS 156 LYS 157 -0.0001

LYS 157 MET 158 0.1338

MET 158 THR 159 -0.0000

THR 159 ALA 160 -0.1846

ALA 160 TRP 161 0.0005

TRP 161 MET 162 -0.0406

MET 162 TYR 163 -0.0003

TYR 163 PHE 164 -0.0867

PHE 164 VAL 165 0.0002

VAL 165 SER 166 0.0671

SER 166 LYS 167 -0.0001

LYS 167 THR 168 0.0101

THR 168 LEU 169 0.0002

LEU 169 ALA 170 0.0520

ALA 170 GLU 171 0.0004

GLU 171 GLN 172 0.0212

GLN 172 ALA 173 -0.0002

ALA 173 ALA 174 0.0039

ALA 174 TRP 175 0.0000

TRP 175 LYS 176 0.0103

LYS 176 TYR 177 0.0002

TYR 177 ALA 178 -0.0252

ALA 178 LYS 179 0.0002

LYS 179 GLU 180 0.0231

GLU 180 ASN 181 0.0004

ASN 181 ASN 182 -0.0235

ASN 182 ILE 183 0.0001

ILE 183 ASP 184 -0.0330

ASP 184 PHE 185 0.0003

PHE 185 ILE 186 0.0298

ILE 186 THR 187 -0.0001

THR 187 ILE 188 0.0026

ILE 188 ILE 189 -0.0000

ILE 189 PRO 190 0.0143

PRO 190 THR 191 -0.0002

THR 191 LEU 192 0.1186

LEU 192 VAL 193 0.0000

VAL 193 VAL 194 0.0606

VAL 194 GLY 195 -0.0000

GLY 195 PRO 196 0.0339

PRO 196 PHE 197 -0.0001

PHE 197 ILE 198 0.0461

ILE 198 MET 199 -0.0000

MET 199 SER 200 -0.0189

SER 200 SER 201 0.0001

SER 201 MET 202 -0.1766

MET 202 PRO 203 0.0000

PRO 203 PRO 204 -0.1026

PRO 204 SER 205 0.0004

SER 205 LEU 206 0.1138

LEU 206 ILE 207 0.0002

ILE 207 THR 208 0.0800

THR 208 ALA 209 0.0000

ALA 209 LEU 210 0.0912

LEU 210 SER 211 -0.0001

SER 211 PRO 212 0.0427

PRO 212 ILE 213 -0.0002

ILE 213 THR 214 0.1213

THR 214 GLY 215 0.0003

GLY 215 ASN 216 0.1609

ASN 216 GLU 217 0.0001

GLU 217 ALA 218 0.1108

ALA 218 HIS 219 0.0003

HIS 219 TYR 220 -0.0590

TYR 220 SER 221 0.0001

SER 221 ILE 222 -0.0327

ILE 222 ILE 223 0.0001

ILE 223 ARG 224 -0.0366

ARG 224 GLN 225 -0.0001

GLN 225 GLY 226 -0.0033

GLY 226 GLN 227 -0.0003

GLN 227 PHE 228 -0.0078

PHE 228 VAL 229 0.0001

VAL 229 HIS 230 0.0069

HIS 230 LEU 231 0.0001

LEU 231 ASP 232 0.0014

ASP 232 ASP 233 0.0002

ASP 233 LEU 234 0.0467

LEU 234 CYS 235 -0.0002

CYS 235 ASN 236 -0.0105

ASN 236 ALA 237 0.0004

ALA 237 HIS 238 0.0229

HIS 238 ILE 239 0.0001

ILE 239 TYR 240 0.0117

TYR 240 LEU 241 0.0003

LEU 241 PHE 242 0.0363

PHE 242 GLU 243 0.0001

GLU 243 ASN 244 0.0026

ASN 244 PRO 245 -0.0005

PRO 245 LYS 246 0.0064

LYS 246 ALA 247 0.0003

ALA 247 GLU 248 -0.0471

GLU 248 GLY 249 -0.0000

GLY 249 ARG 250 -0.0317

ARG 250 TYR 251 -0.0001

TYR 251 ILE 252 0.0630

ILE 252 CYS 253 -0.0001

CYS 253 SER 254 0.0071

SER 254 SER 255 -0.0000

SER 255 HIS 256 0.0834

HIS 256 ASP 257 0.0003

ASP 257 CYS 258 0.0825

CYS 258 ILE 259 0.0003

ILE 259 ILE 260 0.0186

ILE 260 LEU 261 -0.0001

LEU 261 ASP 262 0.0412

ASP 262 LEU 263 -0.0001

LEU 263 ALA 264 -0.0035

ALA 264 LYS 265 -0.0001

LYS 265 MET 266 0.0640

MET 266 LEU 267 -0.0000

LEU 267 ARG 268 -0.0014

ARG 268 GLU 269 0.0000

GLU 269 LYS 270 0.0196

LYS 270 TYR 271 0.0001

TYR 271 PRO 272 0.0033

PRO 272 GLU 273 -0.0003

GLU 273 TYR 274 0.0411

TYR 274 ASN 275 -0.0000

ASN 275 ILE 276 0.0011

ILE 276 PRO 277 0.0002

PRO 277 THR 278 -0.0373

THR 278 GLU 279 0.0001

GLU 279 PHE 280 -0.0163

PHE 280 LYS 281 0.0001

LYS 281 GLY 282 -0.0007

GLY 282 VAL 283 0.0000

VAL 283 ASP 284 -0.0034

ASP 284 GLU 285 -0.0000

GLU 285 ASN 286 -0.0240

ASN 286 LEU 287 -0.0002

LEU 287 LYS 288 -0.0749

LYS 288 SER 289 0.0002

SER 289 VAL 290 0.1141

VAL 290 CYS 291 0.0001

CYS 291 PHE 292 0.1000

PHE 292 SER 293 0.0001

SER 293 SER 294 0.0411

SER 294 LYS 295 0.0002

LYS 295 LYS 296 0.0442

LYS 296 LEU 297 0.0002

LEU 297 THR 298 -0.0315

THR 298 ASP 299 -0.0001

ASP 299 LEU 300 0.0402

LEU 300 GLY 301 0.0002

GLY 301 PHE 302 -0.0116

PHE 302 GLU 303 -0.0000

GLU 303 PHE 304 -0.0163

PHE 304 LYS 305 -0.0002

LYS 305 TYR 306 -0.0072

TYR 306 SER 307 0.0001

SER 307 LEU 308 0.1261

LEU 308 GLU 309 -0.0005

GLU 309 ASP 310 0.0576

ASP 310 MET 311 0.0004

MET 311 PHE 312 -0.0103

PHE 312 THR 313 0.0003

THR 313 GLY 314 0.0469

GLY 314 ALA 315 -0.0004

ALA 315 VAL 316 -0.0286

VAL 316 ASP 317 0.0000

ASP 317 THR 318 0.0274

THR 318 CYS 319 -0.0000

CYS 319 ARG 320 0.0031

ARG 320 ALA 321 0.0002

ALA 321 LYS 322 0.0331

LYS 322 GLY 323 -0.0003

GLY 323 LEU 324 0.0365

LEU 324 LEU 325 -0.0001

LEU 325 PRO 326 -0.0046

PRO 326 PRO 327 0.0002

PRO 327 SER 328 0.0030

SER 328 HIS 329 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).
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.

*** VvWTDHK ***

CA strain for 2610090002023416476

--- 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.

* VvWTDHK *