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 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 0.0002

THR 7 VAL 8 -0.0100

VAL 8 CYS 9 -0.0002

CYS 9 VAL 10 0.0003

VAL 10 THR 11 -0.0000

THR 11 GLY 12 0.1008

GLY 12 ALA 13 0.0001

ALA 13 SER 14 0.0228

SER 14 GLY 15 0.0001

GLY 15 PHE 16 -0.0064

PHE 16 ILE 17 0.0001

ILE 17 GLY 18 0.0013

GLY 18 SER 19 0.0002

SER 19 TRP 20 0.1073

TRP 20 LEU 21 0.0000

LEU 21 VAL 22 0.0279

VAL 22 MET 23 0.0001

MET 23 ARG 24 0.0834

ARG 24 LEU 25 0.0001

LEU 25 LEU 26 0.0845

LEU 26 GLU 27 -0.0002

GLU 27 ARG 28 0.0780

ARG 28 GLY 29 0.0002

GLY 29 TYR 30 0.0057

TYR 30 THR 31 -0.0000

THR 31 VAL 32 -0.0052

VAL 32 ARG 33 -0.0001

ARG 33 ALA 34 0.0433

ALA 34 THR 35 0.0002

THR 35 VAL 36 0.0312

VAL 36 ARG 37 -0.0002

ARG 37 ASP 38 -0.1649

ASP 38 PRO 39 0.0002

PRO 39 THR 40 0.0340

THR 40 ASN 41 0.0003

ASN 41 VAL 42 0.0127

VAL 42 LYS 43 0.0003

LYS 43 LYS 44 -0.0038

LYS 44 VAL 45 0.0001

VAL 45 LYS 46 -0.0290

LYS 46 HIS 47 -0.0001

HIS 47 LEU 48 -0.0324

LEU 48 LEU 49 -0.0006

LEU 49 ASP 50 0.0088

ASP 50 LEU 51 -0.0000

LEU 51 PRO 52 -0.0802

PRO 52 LYS 53 0.0004

LYS 53 ALA 54 -0.0080

ALA 54 GLU 55 -0.0000

GLU 55 THR 56 0.0186

THR 56 HIS 57 0.0002

HIS 57 LEU 58 -0.0279

LEU 58 THR 59 0.0002

THR 59 LEU 60 -0.0118

LEU 60 TRP 61 0.0003

TRP 61 LYS 62 -0.1043

LYS 62 ALA 63 -0.0001

ALA 63 ASP 64 -0.1398

ASP 64 LEU 65 0.0000

LEU 65 ALA 66 0.0591

ALA 66 ASP 67 0.0002

ASP 67 GLU 68 -0.0008

GLU 68 GLY 69 0.0000

GLY 69 SER 70 0.0596

SER 70 PHE 71 -0.0002

PHE 71 ASP 72 -0.0027

ASP 72 GLU 73 0.0002

GLU 73 ALA 74 0.0153

ALA 74 ILE 75 0.0001

ILE 75 LYS 76 0.0151

LYS 76 GLY 77 -0.0001

GLY 77 CYS 78 -0.0125

CYS 78 THR 79 -0.0002

THR 79 GLY 80 -0.0143

GLY 80 VAL 81 -0.0004

VAL 81 PHE 82 -0.0366

PHE 82 HIS 83 0.0002

HIS 83 VAL 84 0.0584

VAL 84 ALA 85 0.0000

ALA 85 THR 86 -0.2069

THR 86 PRO 87 -0.0001

PRO 87 MET 88 -0.0007

MET 88 ASP 89 -0.0001

ASP 89 PHE 90 -0.0997

PHE 90 GLU 91 0.0001

GLU 91 SER 92 0.0561

SER 92 LYS 93 -0.0001

LYS 93 ASP 94 0.0052

ASP 94 PRO 95 -0.0000

PRO 95 GLU 96 0.0050

GLU 96 ASN 97 0.0000

ASN 97 GLU 98 0.0313

GLU 98 VAL 99 -0.0004

VAL 99 ILE 100 -0.0068

ILE 100 LYS 101 0.0002

LYS 101 PRO 102 -0.0333

PRO 102 THR 103 -0.0001

THR 103 ILE 104 -0.0040

ILE 104 GLU 105 -0.0000

GLU 105 GLY 106 0.0062

GLY 106 MET 107 -0.0000

MET 107 LEU 108 0.0043

LEU 108 GLY 109 -0.0001

GLY 109 ILE 110 0.0025

ILE 110 MET 111 -0.0001

MET 111 LYS 112 -0.0121

LYS 112 SER 113 0.0001

SER 113 CYS 114 -0.0112

CYS 114 ALA 115 -0.0001

ALA 115 ALA 116 0.0240

ALA 116 ALA 117 0.0002

ALA 117 LYS 118 0.0150

LYS 118 THR 119 0.0002

THR 119 VAL 120 0.0188

VAL 120 ARG 121 0.0002

ARG 121 ARG 122 0.0147

ARG 122 LEU 123 -0.0001

LEU 123 VAL 124 -0.0105

VAL 124 PHE 125 -0.0003

PHE 125 THR 126 -0.0050

THR 126 SER 127 0.0001

SER 127 SER 128 -0.0302

SER 128 ALA 129 0.0002

ALA 129 GLY 130 -0.0309

GLY 130 THR 131 -0.0004

THR 131 VAL 132 -0.0514

VAL 132 ASN 133 0.0005

ASN 133 ILE 134 -0.0261

ILE 134 GLN 135 0.0003

GLN 135 GLU 136 0.0482

GLU 136 HIS 137 0.0002

HIS 137 GLN 138 -0.0403

GLN 138 LEU 139 -0.0001

LEU 139 PRO 140 -0.0183

PRO 140 VAL 141 -0.0001

VAL 141 TYR 142 -0.0024

TYR 142 ASP 143 0.0002

ASP 143 GLU 144 0.0384

GLU 144 SER 145 -0.0002

SER 145 CYS 146 0.0625

CYS 146 TRP 147 0.0000

TRP 147 SER 148 0.1156

SER 148 ASP 149 -0.0001

ASP 149 MET 150 -0.0755

MET 150 GLU 151 0.0002

GLU 151 PHE 152 -0.0022

PHE 152 CYS 153 0.0002

CYS 153 ARG 154 -0.0138

ARG 154 ALA 155 0.0004

ALA 155 LYS 156 0.0071

LYS 156 LYS 157 0.0001

LYS 157 MET 158 0.0237

MET 158 THR 159 0.0000

THR 159 ALA 160 0.0916

ALA 160 TRP 161 -0.0000

TRP 161 MET 162 0.0203

MET 162 TYR 163 -0.0000

TYR 163 PHE 164 0.0032

PHE 164 VAL 165 0.0002

VAL 165 SER 166 -0.0787

SER 166 LYS 167 -0.0001

LYS 167 THR 168 -0.0231

THR 168 LEU 169 0.0001

LEU 169 ALA 170 0.0063

ALA 170 GLU 171 -0.0002

GLU 171 GLN 172 -0.0090

GLN 172 ALA 173 0.0004

ALA 173 ALA 174 -0.0267

ALA 174 TRP 175 0.0002

TRP 175 LYS 176 -0.0717

LYS 176 TYR 177 -0.0000

TYR 177 ALA 178 -0.0048

ALA 178 LYS 179 0.0001

LYS 179 GLU 180 -0.0180

GLU 180 ASN 181 -0.0000

ASN 181 ASN 182 -0.0263

ASN 182 ILE 183 -0.0002

ILE 183 ASP 184 -0.1109

ASP 184 PHE 185 -0.0001

PHE 185 ILE 186 -0.0338

ILE 186 THR 187 -0.0002

THR 187 ILE 188 -0.0042

ILE 188 ILE 189 -0.0002

ILE 189 PRO 190 0.0357

PRO 190 THR 191 0.0000

THR 191 LEU 192 0.0926

LEU 192 VAL 193 -0.0001

VAL 193 VAL 194 0.0110

VAL 194 GLY 195 0.0000

GLY 195 PRO 196 0.0495

PRO 196 PHE 197 -0.0002

PHE 197 ILE 198 0.1191

ILE 198 MET 199 0.0001

MET 199 SER 200 0.0540

SER 200 SER 201 0.0003

SER 201 MET 202 -0.2664

MET 202 PRO 203 -0.0002

PRO 203 PRO 204 -0.1605

PRO 204 SER 205 0.0002

SER 205 LEU 206 0.1088

LEU 206 ILE 207 0.0003

ILE 207 THR 208 -0.1062

THR 208 ALA 209 -0.0002

ALA 209 LEU 210 0.0162

LEU 210 SER 211 0.0001

SER 211 PRO 212 0.0554

PRO 212 ILE 213 0.0003

ILE 213 THR 214 0.0503

THR 214 GLY 215 0.0004

GLY 215 ASN 216 0.1339

ASN 216 GLU 217 -0.0003

GLU 217 ALA 218 0.1070

ALA 218 HIS 219 -0.0000

HIS 219 TYR 220 -0.0396

TYR 220 SER 221 -0.0001

SER 221 ILE 222 0.0336

ILE 222 ILE 223 -0.0001

ILE 223 ARG 224 -0.1401

ARG 224 GLN 225 0.0001

GLN 225 GLY 226 -0.0464

GLY 226 GLN 227 -0.0001

GLN 227 PHE 228 0.0279

PHE 228 VAL 229 0.0002

VAL 229 HIS 230 0.0564

HIS 230 LEU 231 0.0002

LEU 231 ASP 232 -0.0192

ASP 232 ASP 233 -0.0002

ASP 233 LEU 234 -0.0010

LEU 234 CYS 235 0.0000

CYS 235 ASN 236 0.0480

ASN 236 ALA 237 0.0001

ALA 237 HIS 238 0.0084

HIS 238 ILE 239 0.0001

ILE 239 TYR 240 0.1310

TYR 240 LEU 241 -0.0003

LEU 241 PHE 242 0.0249

PHE 242 GLU 243 -0.0000

GLU 243 ASN 244 0.0845

ASN 244 PRO 245 -0.0002

PRO 245 LYS 246 0.0046

LYS 246 ALA 247 -0.0004

ALA 247 GLU 248 0.0044

GLU 248 GLY 249 -0.0006

GLY 249 ARG 250 0.1228

ARG 250 TYR 251 -0.0002

TYR 251 ILE 252 0.0137

ILE 252 CYS 253 -0.0001

CYS 253 SER 254 -0.0347

SER 254 SER 255 0.0001

SER 255 HIS 256 0.0361

HIS 256 ASP 257 0.0001

ASP 257 CYS 258 0.0199

CYS 258 ILE 259 -0.0003

ILE 259 ILE 260 -0.0202

ILE 260 LEU 261 -0.0001

LEU 261 ASP 262 0.0264

ASP 262 LEU 263 -0.0002

LEU 263 ALA 264 -0.0546

ALA 264 LYS 265 -0.0002

LYS 265 MET 266 0.0338

MET 266 LEU 267 0.0002

LEU 267 ARG 268 -0.0342

ARG 268 GLU 269 0.0001

GLU 269 LYS 270 0.0691

LYS 270 TYR 271 0.0000

TYR 271 PRO 272 -0.0695

PRO 272 GLU 273 -0.0001

GLU 273 TYR 274 0.0463

TYR 274 ASN 275 -0.0006

ASN 275 ILE 276 -0.0002

ILE 276 PRO 277 0.0001

PRO 277 THR 278 0.0019

THR 278 GLU 279 0.0000

GLU 279 PHE 280 0.0373

PHE 280 LYS 281 -0.0000

LYS 281 GLY 282 0.0789

GLY 282 VAL 283 -0.0004

VAL 283 ASP 284 -0.0334

ASP 284 GLU 285 -0.0003

GLU 285 ASN 286 0.0319

ASN 286 LEU 287 0.0000

LEU 287 LYS 288 0.0994

LYS 288 SER 289 0.0000

SER 289 VAL 290 -0.0712

VAL 290 CYS 291 0.0004

CYS 291 PHE 292 0.0836

PHE 292 SER 293 -0.0002

SER 293 SER 294 0.0698

SER 294 LYS 295 -0.0003

LYS 295 LYS 296 -0.0101

LYS 296 LEU 297 -0.0002

LEU 297 THR 298 -0.0370

THR 298 ASP 299 -0.0001

ASP 299 LEU 300 0.0391

LEU 300 GLY 301 -0.0001

GLY 301 PHE 302 -0.0388

PHE 302 GLU 303 -0.0003

GLU 303 PHE 304 -0.1004

PHE 304 LYS 305 0.0002

LYS 305 TYR 306 -0.2136

TYR 306 SER 307 -0.0000

SER 307 LEU 308 0.0498

LEU 308 GLU 309 -0.0000

GLU 309 ASP 310 0.0039

ASP 310 MET 311 -0.0003

MET 311 PHE 312 -0.0974

PHE 312 THR 313 0.0001

THR 313 GLY 314 0.0941

GLY 314 ALA 315 0.0001

ALA 315 VAL 316 -0.0324

VAL 316 ASP 317 0.0001

ASP 317 THR 318 0.0959

THR 318 CYS 319 0.0002

CYS 319 ARG 320 0.0097

ARG 320 ALA 321 -0.0000

ALA 321 LYS 322 0.1983

LYS 322 GLY 323 -0.0002

GLY 323 LEU 324 0.0472

LEU 324 LEU 325 0.0000

LEU 325 PRO 326 0.1135

PRO 326 PRO 327 -0.0001

PRO 327 SER 328 0.0073

SER 328 HIS 329 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.

*** VVWT DHQ ***

CA strain for 2610090010133421365

--- 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.

* VVWT DHQ *