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

* DMD *

CA strain for 2609111750043690248

--- normal mode 11 ---

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 ARG 2 0.0001

ARG 2 GLU 3 0.0363

GLU 3 GLN 4 -0.0002

GLN 4 LEU 5 -0.0115

LEU 5 LYS 6 -0.0001

LYS 6 GLY 7 -0.0432

GLY 7 HIS 8 0.0002

HIS 8 GLU 9 0.0091

GLU 9 THR 10 0.0003

THR 10 GLN 11 0.0209

GLN 11 THR 12 -0.0000

THR 12 THR 13 0.0678

THR 13 CYS 14 0.0003

CYS 14 TRP 15 0.0086

TRP 15 ASP 16 0.0001

ASP 16 HIS 17 0.0060

HIS 17 PRO 18 -0.0002

PRO 18 LYS 19 -0.0231

LYS 19 MET 20 -0.0001

MET 20 THR 21 0.0102

THR 21 GLU 22 -0.0002

GLU 22 LEU 23 -0.0344

LEU 23 TYR 24 -0.0001

TYR 24 GLN 25 -0.0079

GLN 25 SER 26 -0.0003

SER 26 LEU 27 0.0107

LEU 27 ALA 28 0.0000

ALA 28 ASP 29 -0.0060

ASP 29 LEU 30 -0.0001

LEU 30 ASN 31 0.0345

ASN 31 ASN 32 0.0003

ASN 32 VAL 33 0.0451

VAL 33 ARG 34 0.0000

ARG 34 PHE 35 -0.0189

PHE 35 SER 36 0.0002

SER 36 ALA 37 -0.0115

ALA 37 TYR 38 -0.0004

TYR 38 ARG 39 0.0100

ARG 39 THR 40 -0.0002

THR 40 ALA 41 0.0093

ALA 41 MET 42 0.0005

MET 42 LYS 43 -0.0687

LYS 43 LEU 44 0.0001

LEU 44 ARG 45 -0.0415

ARG 45 ARG 46 -0.0001

ARG 46 LEU 47 -0.0423

LEU 47 GLN 48 -0.0000

GLN 48 LYS 49 0.0162

LYS 49 ALA 50 0.0001

ALA 50 LEU 51 -0.0501

LEU 51 CYS 52 0.0001

CYS 52 LEU 53 -0.0022

LEU 53 ASP 54 0.0000

ASP 54 LEU 55 -0.0045

LEU 55 LEU 56 -0.0002

LEU 56 SER 57 -0.0045

SER 57 LEU 58 -0.0001

LEU 58 SER 59 -0.0064

SER 59 ALA 60 0.0004

ALA 60 ALA 61 -0.0010

ALA 61 CYS 62 0.0000

CYS 62 ASP 63 -0.0087

ASP 63 ALA 64 -0.0001

ALA 64 LEU 65 -0.0011

LEU 65 ASP 66 -0.0000

ASP 66 GLN 67 -0.0007

GLN 67 HIS 68 -0.0000

HIS 68 ASN 69 -0.0056

ASN 69 LEU 70 -0.0004

LEU 70 LYS 71 -0.0027

LYS 71 GLN 72 0.0002

GLN 72 ASN 73 -0.0002

ASN 73 ASP 74 0.0002

ASP 74 GLN 75 0.0027

GLN 75 PRO 76 -0.0001

PRO 76 MET 77 -0.0009

MET 77 ASP 78 -0.0000

ASP 78 ILE 79 -0.0024

ILE 79 LEU 80 0.0002

LEU 80 GLN 81 -0.0005

GLN 81 ILE 82 0.0000

ILE 82 ILE 83 0.0016

ILE 83 ASN 84 0.0000

ASN 84 CYS 85 -0.0026

CYS 85 LEU 86 0.0003

LEU 86 THR 87 0.0064

THR 87 THR 88 0.0001

THR 88 ILE 89 -0.0002

ILE 89 TYR 90 0.0001

TYR 90 ASP 91 -0.0014

ASP 91 ARG 92 -0.0004

ARG 92 LEU 93 0.0036

LEU 93 GLU 94 -0.0001

GLU 94 GLN 95 -0.0016

GLN 95 GLU 96 -0.0002

GLU 96 HIS 97 0.0010

HIS 97 ASN 98 -0.0002

ASN 98 ASN 99 -0.0007

ASN 99 LEU 100 -0.0001

LEU 100 VAL 101 0.0019

VAL 101 ASN 102 -0.0002

ASN 102 VAL 103 0.0011

VAL 103 PRO 104 -0.0001

PRO 104 LEU 105 -0.0009

LEU 105 CYS 106 -0.0003

CYS 106 VAL 107 -0.0147

VAL 107 ASP 108 0.0002

ASP 108 MET 109 -0.0110

MET 109 CYS 110 -0.0001

CYS 110 LEU 111 -0.0185

LEU 111 ASN 112 0.0000

ASN 112 TRP 113 0.0089

TRP 113 LEU 114 0.0002

LEU 114 LEU 115 -0.0083

LEU 115 ASN 116 0.0000

ASN 116 VAL 117 0.0248

VAL 117 TYR 118 -0.0003

TYR 118 ASP 119 0.0415

ASP 119 THR 120 0.0003

THR 120 GLY 121 0.0177

GLY 121 ARG 122 -0.0000

ARG 122 THR 123 0.0018

THR 123 GLY 124 0.0003

GLY 124 ARG 125 0.0162

ARG 125 ILE 126 0.0001

ILE 126 ARG 127 0.0102

ARG 127 VAL 128 0.0001

VAL 128 LEU 129 0.0037

LEU 129 SER 130 -0.0001

SER 130 PHE 131 0.0057

PHE 131 LYS 132 -0.0002

LYS 132 THR 133 0.0009

THR 133 GLY 134 -0.0001

GLY 134 ILE 135 0.0030

ILE 135 ILE 136 -0.0002

ILE 136 SER 137 0.0082

SER 137 LEU 138 0.0001

LEU 138 CYS 139 -0.0024

CYS 139 LYS 140 0.0000

LYS 140 ALA 141 -0.0024

ALA 141 HIS 142 0.0003

HIS 142 LEU 143 -0.0267

LEU 143 GLU 144 0.0001

GLU 144 ASP 145 -0.0057

ASP 145 LYS 146 -0.0001

LYS 146 TYR 147 -0.0166

TYR 147 ARG 148 -0.0003

ARG 148 TYR 149 -0.0202

TYR 149 LEU 150 -0.0003

LEU 150 PHE 151 -0.0080

PHE 151 LYS 152 0.0002

LYS 152 GLN 153 -0.0080

GLN 153 VAL 154 0.0002

VAL 154 ALA 155 -0.0121

ALA 155 SER 156 -0.0002

SER 156 SER 157 -0.0045

SER 157 THR 158 0.0001

THR 158 GLY 159 0.0134

GLY 159 PHE 160 -0.0001

PHE 160 CYS 161 -0.0036

CYS 161 ASP 162 -0.0001

ASP 162 GLN 163 -0.0036

GLN 163 ARG 164 0.0000

ARG 164 ARG 165 0.0009

ARG 165 LEU 166 -0.0001

LEU 166 GLY 167 -0.0061

GLY 167 LEU 168 0.0000

LEU 168 LEU 169 0.0078

LEU 169 LEU 170 0.0002

LEU 170 HIS 171 0.0095

HIS 171 ASP 172 -0.0000

ASP 172 SER 173 0.0234

SER 173 ILE 174 0.0000

ILE 174 GLN 175 0.0385

GLN 175 ILE 176 -0.0003

ILE 176 PRO 177 0.0087

PRO 177 ARG 178 -0.0000

ARG 178 GLN 179 0.0384

GLN 179 LEU 180 -0.0002

LEU 180 GLY 181 0.0328

GLY 181 GLU 182 0.0001

GLU 182 VAL 183 -0.0801

VAL 183 ALA 184 0.0001

ALA 184 SER 185 0.0259

SER 185 PHE 186 0.0001

PHE 186 GLY 187 -0.0064

GLY 187 GLY 188 0.0003

GLY 188 SER 189 0.0403

SER 189 ASN 190 0.0002

ASN 190 ILE 191 -0.0024

ILE 191 GLU 192 0.0001

GLU 192 PRO 193 -0.0017

PRO 193 SER 194 -0.0003

SER 194 VAL 195 0.0058

VAL 195 ARG 196 -0.0001

ARG 196 SER 197 0.0073

SER 197 CYS 198 0.0003

CYS 198 PHE 199 0.0127

PHE 199 GLN 200 0.0002

GLN 200 PHE 201 0.0014

PHE 201 ALA 202 -0.0003

ALA 202 ASN 203 0.0092

ASN 203 ASN 204 -0.0001

ASN 204 LYS 205 -0.0028

LYS 205 PRO 206 0.0001

PRO 206 GLU 207 0.0031

GLU 207 ILE 208 0.0003

ILE 208 GLU 209 -0.0005

GLU 209 ALA 210 0.0000

ALA 210 ALA 211 -0.0034

ALA 211 LEU 212 -0.0001

LEU 212 PHE 213 -0.0034

PHE 213 LEU 214 -0.0002

LEU 214 ASP 215 -0.0043

ASP 215 TRP 216 0.0003

TRP 216 MET 217 0.0194

MET 217 ARG 218 0.0003

ARG 218 LEU 219 -0.0354

LEU 219 GLU 220 0.0001

GLU 220 PRO 221 0.0329

PRO 221 GLN 222 -0.0000

GLN 222 SER 223 0.0467

SER 223 MET 224 0.0001

MET 224 VAL 225 0.0573

VAL 225 TRP 226 0.0001

TRP 226 LEU 227 -0.0314

LEU 227 PRO 228 -0.0003

PRO 228 VAL 229 0.0182

VAL 229 LEU 230 -0.0001

LEU 230 HIS 231 0.0108

HIS 231 ARG 232 -0.0002

ARG 232 VAL 233 0.0279

VAL 233 ALA 234 -0.0000

ALA 234 ALA 235 -0.0700

ALA 235 ALA 236 0.0002

ALA 236 GLU 237 -0.0334

GLU 237 THR 238 -0.0001

THR 238 ALA 239 -0.1180

ALA 239 LYS 240 -0.0002

LYS 240 HIS 241 -0.0397

HIS 241 GLN 242 0.0002

GLN 242 ALA 243 -0.0132

ALA 243 LYS 244 0.0003

LYS 244 CYS 245 -0.0122

CYS 245 ASN 246 -0.0003

ASN 246 ILE 247 -0.0220

ILE 247 CYS 248 -0.0001

CYS 248 LYS 249 -0.0186

LYS 249 GLU 250 0.0001

GLU 250 CYS 251 -0.0146

CYS 251 PRO 252 0.0000

PRO 252 ILE 253 -0.0020

ILE 253 ILE 254 0.0002

ILE 254 GLY 255 0.0222

GLY 255 PHE 256 0.0001

PHE 256 ARG 257 -0.0366

ARG 257 TYR 258 -0.0002

TYR 258 ARG 259 -0.0176

ARG 259 SER 260 -0.0002

SER 260 LEU 261 -0.0239

LEU 261 LYS 262 -0.0001

LYS 262 HIS 263 0.0071

HIS 263 PHE 264 -0.0001

PHE 264 ASN 265 -0.0170

ASN 265 TYR 266 0.0004

TYR 266 ASP 267 -0.0188

ASP 267 ILE 268 0.0000

ILE 268 CYS 269 -0.0426

CYS 269 GLN 270 0.0002

GLN 270 SER 271 0.0285

SER 271 CYS 272 -0.0002

CYS 272 PHE 273 0.0285

PHE 273 PHE 274 -0.0001

PHE 274 SER 275 0.0455

SER 275 GLY 276 0.0003

GLY 276 ARG 277 -0.0305

ARG 277 VAL 278 -0.0001

VAL 278 ALA 279 -0.0368

ALA 279 LYS 280 -0.0001

LYS 280 GLY 281 0.0235

GLY 281 HIS 282 -0.0005

HIS 282 LYS 283 0.0090

LYS 283 MET 284 -0.0003

MET 284 HIS 285 0.0263

HIS 285 TYR 286 0.0002

TYR 286 PRO 287 -0.0247

PRO 287 MET 288 -0.0001

MET 288 VAL 289 -0.0217

VAL 289 GLU 290 0.0000

GLU 290 TYR 291 0.0093

TYR 291 CYS 292 -0.0003

CYS 292 THR 293 0.0470

THR 293 PRO 294 0.0001

PRO 294 THR 295 -0.0564

THR 295 THR 296 -0.0002

THR 296 SER 297 -0.0063

SER 297 GLY 298 0.0002

GLY 298 GLU 299 0.0204

GLU 299 ASP 300 -0.0006

ASP 300 VAL 301 -0.0162

VAL 301 ARG 302 -0.0001

ARG 302 ASP 303 0.0197

ASP 303 PHE 304 -0.0005

PHE 304 ALA 305 -0.0104

ALA 305 LYS 306 0.0001

LYS 306 VAL 307 -0.0067

VAL 307 LEU 308 0.0002

LEU 308 LYS 309 0.0107

LYS 309 ASN 310 -0.0002

ASN 310 LYS 311 0.0066

LYS 311 PHE 312 -0.0002

PHE 312 ARG 313 0.0069

ARG 313 THR 314 0.0004

THR 314 LYS 315 0.0006

LYS 315 ARG 316 -0.0004

ARG 316 TYR 317 0.0032

TYR 317 PHE 318 0.0001

PHE 318 ALA 319 0.0127

ALA 319 LYS 320 -0.0000

LYS 320 HIS 321 0.0014

HIS 321 PRO 322 -0.0001

PRO 322 ARG 323 -0.0096

ARG 323 MET 324 -0.0000

MET 324 GLY 325 0.1740

GLY 325 TYR 326 -0.0002

TYR 326 LEU 327 -0.0582

LEU 327 PRO 328 0.0001

PRO 328 VAL 329 -0.0819

VAL 329 GLN 330 0.0002

GLN 330 THR 331 0.0640

THR 331 VAL 332 0.0000

VAL 332 LEU 333 -0.0527

LEU 333 GLU 334 0.0001

GLU 334 GLY 335 -0.1262

GLY 335 ASP 336 -0.0002

ASP 336 ASN 337 0.0076

ASN 337 MET 338 0.0000

MET 338 GLU 339 0.0431

GLU 339 THR 340 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.

*** DMD ***

CA strain for 2609111750043690248

--- normal mode 11 ---

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

* DMD *