Should you encounter any unexpected behaviour,
please let us know.

* zxy *

CA strain for 2404230438531985751

--- 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 ASP 2 -0.0002

ASP 2 PRO 3 0.0291

PRO 3 LEU 4 0.0004

LEU 4 GLY 5 0.0170

GLY 5 LEU 6 0.0001

LEU 6 GLN 7 0.0601

GLN 7 ASP 8 0.0001

ASP 8 PHE 9 -0.0295

PHE 9 ASP 10 0.0001

ASP 10 LEU 11 0.0513

LEU 11 LEU 12 0.0004

LEU 12 ARG 13 0.0850

ARG 13 VAL 14 0.0004

VAL 14 ILE 15 -0.0783

ILE 15 GLY 16 -0.0003

GLY 16 ARG 17 -0.1082

ARG 17 GLY 18 -0.0002

GLY 18 SER 19 -0.1255

SER 19 TYR 20 0.0001

TYR 20 ALA 21 0.0285

ALA 21 LYS 22 0.0001

LYS 22 VAL 23 -0.0720

VAL 23 LEU 24 0.0002

LEU 24 LEU 25 -0.0553

LEU 25 VAL 26 -0.0003

VAL 26 ARG 27 0.0314

ARG 27 LEU 28 -0.0000

LEU 28 LYS 29 -0.0388

LYS 29 LYS 30 0.0002

LYS 30 THR 31 0.0128

THR 31 ASP 32 -0.0003

ASP 32 ARG 33 -0.0268

ARG 33 ILE 34 0.0000

ILE 34 TYR 35 0.0102

TYR 35 ALA 36 -0.0001

ALA 36 MET 37 -0.0821

MET 37 LYS 38 -0.0003

LYS 38 VAL 39 -0.0995

VAL 39 VAL 40 0.0004

VAL 40 LYS 41 -0.1505

LYS 41 LYS 42 0.0001

LYS 42 GLU 43 -0.0085

GLU 43 LEU 44 0.0000

LEU 44 VAL 45 -0.0001

VAL 45 ASN 46 -0.0005

ASN 46 ASP 47 -0.0022

ASP 47 ASP 48 -0.0001

ASP 48 GLU 49 -0.0644

GLU 49 ASP 50 0.0006

ASP 50 ILE 51 0.0100

ILE 51 ASP 52 -0.0004

ASP 52 TRP 53 0.0698

TRP 53 VAL 54 -0.0001

VAL 54 GLN 55 0.0422

GLN 55 THR 56 -0.0000

THR 56 GLU 57 0.0442

GLU 57 LYS 58 -0.0002

LYS 58 HIS 59 0.0952

HIS 59 VAL 60 -0.0002

VAL 60 PHE 61 0.0142

PHE 61 GLU 62 0.0001

GLU 62 GLN 63 0.0821

GLN 63 ALA 64 0.0001

ALA 64 SER 65 -0.0126

SER 65 ASN 66 0.0001

ASN 66 HIS 67 0.0464

HIS 67 PRO 68 -0.0001

PRO 68 PHE 69 0.0036

PHE 69 LEU 70 0.0001

LEU 70 VAL 71 -0.0322

VAL 71 GLY 72 -0.0001

GLY 72 LEU 73 0.0565

LEU 73 HIS 74 -0.0000

HIS 74 SER 75 0.0896

SER 75 CYS 76 -0.0000

CYS 76 PHE 77 0.1627

PHE 77 GLN 78 0.0001

GLN 78 THR 79 0.2322

THR 79 GLU 80 -0.0004

GLU 80 SER 81 -0.1336

SER 81 ARG 82 -0.0000

ARG 82 LEU 83 0.0661

LEU 83 PHE 84 0.0000

PHE 84 PHE 85 0.0563

PHE 85 VAL 86 -0.0002

VAL 86 ILE 87 0.0011

ILE 87 GLU 88 0.0001

GLU 88 TYR 89 0.1362

TYR 89 VAL 90 -0.0002

VAL 90 ASN 91 0.1219

ASN 91 GLY 92 0.0001

GLY 92 GLY 93 0.0001

GLY 93 ASP 94 -0.0003

ASP 94 LEU 95 -0.0186

LEU 95 MET 96 0.0001

MET 96 PHE 97 -0.0794

PHE 97 HIS 98 0.0002

HIS 98 MET 99 -0.0186

MET 99 GLN 100 0.0000

GLN 100 ARG 101 -0.0281

ARG 101 GLN 102 0.0001

GLN 102 ARG 103 -0.0730

ARG 103 LYS 104 -0.0001

LYS 104 LEU 105 -0.0484

LEU 105 PRO 106 0.0000

PRO 106 GLU 107 0.1383

GLU 107 GLU 108 -0.0003

GLU 108 HIS 109 0.0174

HIS 109 ALA 110 0.0002

ALA 110 ARG 111 -0.0511

ARG 111 PHE 112 0.0000

PHE 112 TYR 113 -0.0094

TYR 113 SER 114 0.0001

SER 114 ALA 115 -0.0580

ALA 115 GLU 116 0.0001

GLU 116 ILE 117 -0.0157

ILE 117 SER 118 0.0002

SER 118 LEU 119 -0.0053

LEU 119 ALA 120 0.0001

ALA 120 LEU 121 0.0187

LEU 121 ASN 122 0.0002

ASN 122 TYR 123 0.0034

TYR 123 LEU 124 -0.0000

LEU 124 HIS 125 0.0102

HIS 125 GLU 126 0.0001

GLU 126 ARG 127 0.0259

ARG 127 GLY 128 -0.0001

GLY 128 ILE 129 -0.0095

ILE 129 ILE 130 -0.0000

ILE 130 TYR 131 -0.0542

TYR 131 ARG 132 -0.0003

ARG 132 ASP 133 -0.0775

ASP 133 LEU 134 -0.0003

LEU 134 LYS 135 -0.0617

LYS 135 LEU 136 -0.0001

LEU 136 ASP 137 0.0817

ASP 137 ASN 138 -0.0003

ASN 138 VAL 139 -0.0212

VAL 139 LEU 140 -0.0000

LEU 140 LEU 141 -0.0105

LEU 141 ASP 142 -0.0002

ASP 142 SER 143 0.0423

SER 143 GLU 144 0.0003

GLU 144 GLY 145 0.0003

GLY 145 HIS 146 -0.0001

HIS 146 ILE 147 -0.0010

ILE 147 LYS 148 -0.0000

LYS 148 LEU 149 0.0008

LEU 149 THR 150 0.0001

THR 150 ASP 151 -0.0430

ASP 151 TYR 152 -0.0002

TYR 152 GLY 153 -0.0222

GLY 153 MET 154 -0.0001

MET 154 CYS 155 -0.0285

CYS 155 LYS 156 0.0002

LYS 156 GLU 157 0.0289

GLU 157 GLY 158 0.0004

GLY 158 LEU 159 0.1704

LEU 159 ARG 160 0.0000

ARG 160 PRO 161 0.0046

PRO 161 GLY 162 -0.0002

GLY 162 ASP 163 0.0403

ASP 163 THR 164 -0.0000

THR 164 THR 165 0.0418

THR 165 SER 166 0.0003

SER 166 GLU 167 0.0267

GLU 167 PHE 168 -0.0001

PHE 168 CYS 169 -0.1027

CYS 169 GLY 170 0.0002

GLY 170 THR 171 -0.0403

THR 171 PRO 172 0.0000

PRO 172 ASN 173 -0.0279

ASN 173 TYR 174 -0.0001

TYR 174 ILE 175 -0.0909

ILE 175 ALA 176 -0.0001

ALA 176 PRO 177 -0.0063

PRO 177 GLU 178 0.0001

GLU 178 ILE 179 -0.0219

ILE 179 LEU 180 0.0002

LEU 180 ARG 181 0.0706

ARG 181 GLY 182 0.0002

GLY 182 GLU 183 0.0730

GLU 183 ASP 184 -0.0001

ASP 184 TYR 185 0.0112

TYR 185 GLY 186 0.0000

GLY 186 PHE 187 0.0574

PHE 187 SER 188 -0.0000

SER 188 VAL 189 0.0242

VAL 189 ASP 190 0.0002

ASP 190 TRP 191 0.0250

TRP 191 TRP 192 0.0004

TRP 192 ALA 193 -0.0369

ALA 193 LEU 194 0.0002

LEU 194 GLY 195 -0.0073

GLY 195 VAL 196 -0.0003

VAL 196 LEU 197 -0.0538

LEU 197 MET 198 0.0002

MET 198 PHE 199 -0.0906

PHE 199 GLU 200 0.0001

GLU 200 MET 201 -0.1921

MET 201 MET 202 0.0002

MET 202 ALA 203 -0.1706

ALA 203 GLY 204 0.0004

GLY 204 ARG 205 -0.4212

ARG 205 SER 206 -0.0001

SER 206 PRO 207 0.0531

PRO 207 PHE 208 -0.0004

PHE 208 ASP 209 -0.0919

ASP 209 ILE 210 0.0001

ILE 210 VAL 211 -0.1284

VAL 211 GLY 212 0.0001

GLY 212 SER 213 -0.1953

SER 213 SER 214 -0.0002

SER 214 ASP 215 0.0560

ASP 215 ASN 216 -0.0002

ASN 216 PRO 217 -0.0451

PRO 217 ASP 218 -0.0000

ASP 218 GLN 219 0.1222

GLN 219 ASN 220 0.0001

ASN 220 THR 221 0.0645

THR 221 GLU 222 0.0002

GLU 222 ASP 223 -0.1179

ASP 223 TYR 224 -0.0000

TYR 224 LEU 225 -0.1015

LEU 225 PHE 226 -0.0001

PHE 226 GLN 227 -0.1326

GLN 227 VAL 228 0.0000

VAL 228 ILE 229 0.0563

ILE 229 LEU 230 0.0001

LEU 230 GLU 231 -0.0474

GLU 231 LYS 232 0.0001

LYS 232 GLN 233 0.0640

GLN 233 ILE 234 -0.0001

ILE 234 ARG 235 0.0423

ARG 235 ILE 236 -0.0001

ILE 236 PRO 237 -0.0274

PRO 237 ARG 238 0.0000

ARG 238 SER 239 0.0504

SER 239 LEU 240 -0.0002

LEU 240 SER 241 -0.0654

SER 241 VAL 242 -0.0002

VAL 242 LYS 243 -0.0238

LYS 243 ALA 244 -0.0003

ALA 244 ALA 245 -0.0325

ALA 245 SER 246 -0.0001

SER 246 VAL 247 -0.0088

VAL 247 LEU 248 -0.0000

LEU 248 LYS 249 0.0388

LYS 249 SER 250 0.0002

SER 250 PHE 251 0.0077

PHE 251 LEU 252 0.0001

LEU 252 ASN 253 -0.0299

ASN 253 LYS 254 -0.0001

LYS 254 ASP 255 0.0179

ASP 255 PRO 256 -0.0003

PRO 256 LYS 257 0.0185

LYS 257 GLU 258 0.0004

GLU 258 ARG 259 0.0071

ARG 259 LEU 260 -0.0002

LEU 260 GLY 261 -0.0082

GLY 261 CYS 262 -0.0003

CYS 262 HIS 263 0.0073

HIS 263 PRO 264 -0.0001

PRO 264 GLN 265 0.0265

GLN 265 THR 266 -0.0003

THR 266 GLY 267 0.0015

GLY 267 PHE 268 -0.0000

PHE 268 ALA 269 0.0102

ALA 269 ASP 270 0.0002

ASP 270 ILE 271 -0.0459

ILE 271 GLN 272 0.0002

GLN 272 GLY 273 -0.0089

GLY 273 HIS 274 -0.0001

HIS 274 PRO 275 0.0234

PRO 275 PHE 276 -0.0002

PHE 276 PHE 277 -0.0340

PHE 277 ARG 278 -0.0000

ARG 278 ASN 279 0.0198

ASN 279 VAL 280 -0.0001

VAL 280 ASP 281 -0.0600

ASP 281 TRP 282 -0.0002

TRP 282 ASP 283 -0.0049

ASP 283 MET 284 0.0004

MET 284 MET 285 -0.0212

MET 285 GLU 286 0.0001

GLU 286 GLN 287 0.0233

GLN 287 LYS 288 0.0002

LYS 288 GLN 289 0.0295

GLN 289 VAL 290 -0.0003

VAL 290 VAL 291 -0.0324

VAL 291 PRO 292 0.0001

PRO 292 PRO 293 -0.0090

PRO 293 PHE 294 -0.0000

PHE 294 LYS 295 -0.1623

LYS 295 PRO 296 -0.0000

PRO 296 ASN 297 -0.0474

ASN 297 ILE 298 0.0002

ILE 298 SER 299 -0.0504

SER 299 GLY 300 -0.0000

GLY 300 GLU 301 0.0285

GLU 301 PHE 302 -0.0003

PHE 302 GLY 303 -0.0157

GLY 303 LEU 304 0.0001

LEU 304 ASP 305 -0.0090

ASP 305 ASN 306 0.0003

ASN 306 PHE 307 -0.1372

PHE 307 ASP 308 -0.0004

ASP 308 SER 309 -0.0053

SER 309 GLN 310 -0.0003

GLN 310 PHE 311 0.0086

PHE 311 THR 312 -0.0002

THR 312 ASN 313 -0.0442

ASN 313 GLU 314 0.0002

GLU 314 PRO 315 0.0151

PRO 315 VAL 316 -0.0000

VAL 316 GLN 317 -0.1519

GLN 317 LEU 318 0.0002

LEU 318 GLU 319 0.0220

GLU 319 PRO 320 -0.0004

PRO 320 ASP 321 -0.0762

ASP 321 ASP 322 -0.0000

ASP 322 ASP 323 -0.1251

ASP 323 ASP 324 -0.0000

ASP 324 ILE 325 -0.1023

ILE 325 VAL 326 0.0001

VAL 326 ARG 327 -0.0332

ARG 327 LYS 328 -0.0001

LYS 328 ILE 329 0.0401

ILE 329 ASP 330 -0.0002

ASP 330 GLN 331 0.0050

GLN 331 SER 332 -0.0003

SER 332 GLU 333 0.0194

GLU 333 PHE 334 -0.0000

PHE 334 GLU 335 -0.0577

GLU 335 GLY 336 0.0001

GLY 336 PHE 337 0.0279

PHE 337 GLU 338 -0.0001

GLU 338 TYR 339 0.1687

TYR 339 ILE 340 -0.0000

ILE 340 ASN 341 0.0479

ASN 341 PRO 342 0.0002

PRO 342 LEU 343 -0.0122

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).
Last modification: April 25th, 2023.

Should you encounter any unexpected behaviour, please let us know.

*** zxy ***

CA strain for 2404230438531985751

--- normal mode 11 ---

Should you encounter any unexpected behaviour,
please let us know.

* zxy *