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

* zxy *

CA strain for 2404230438531985751

--- normal mode 9 ---

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 0.0003

ASP 2 PRO 3 -0.0228

PRO 3 LEU 4 0.0001

LEU 4 GLY 5 0.0509

GLY 5 LEU 6 0.0002

LEU 6 GLN 7 -0.0150

GLN 7 ASP 8 -0.0002

ASP 8 PHE 9 0.0063

PHE 9 ASP 10 0.0001

ASP 10 LEU 11 -0.0135

LEU 11 LEU 12 -0.0001

LEU 12 ARG 13 -0.0446

ARG 13 VAL 14 -0.0003

VAL 14 ILE 15 0.0027

ILE 15 GLY 16 0.0001

GLY 16 ARG 17 0.0430

ARG 17 GLY 18 0.0002

GLY 18 SER 19 0.1400

SER 19 TYR 20 0.0002

TYR 20 ALA 21 0.0197

ALA 21 LYS 22 0.0002

LYS 22 VAL 23 0.0179

VAL 23 LEU 24 -0.0001

LEU 24 LEU 25 0.0345

LEU 25 VAL 26 -0.0003

VAL 26 ARG 27 -0.0284

ARG 27 LEU 28 0.0003

LEU 28 LYS 29 0.0257

LYS 29 LYS 30 -0.0002

LYS 30 THR 31 -0.0031

THR 31 ASP 32 0.0000

ASP 32 ARG 33 0.0242

ARG 33 ILE 34 0.0001

ILE 34 TYR 35 -0.0215

TYR 35 ALA 36 -0.0000

ALA 36 MET 37 0.0852

MET 37 LYS 38 -0.0000

LYS 38 VAL 39 -0.0221

VAL 39 VAL 40 -0.0003

VAL 40 LYS 41 -0.0463

LYS 41 LYS 42 -0.0001

LYS 42 GLU 43 0.0180

GLU 43 LEU 44 -0.0000

LEU 44 VAL 45 -0.0458

VAL 45 ASN 46 0.0000

ASN 46 ASP 47 -0.0021

ASP 47 ASP 48 0.0004

ASP 48 GLU 49 -0.0654

GLU 49 ASP 50 -0.0002

ASP 50 ILE 51 -0.0050

ILE 51 ASP 52 -0.0001

ASP 52 TRP 53 0.0481

TRP 53 VAL 54 -0.0001

VAL 54 GLN 55 -0.0533

GLN 55 THR 56 0.0000

THR 56 GLU 57 -0.0555

GLU 57 LYS 58 -0.0002

LYS 58 HIS 59 -0.0127

HIS 59 VAL 60 0.0002

VAL 60 PHE 61 -0.0203

PHE 61 GLU 62 -0.0003

GLU 62 GLN 63 0.0336

GLN 63 ALA 64 0.0003

ALA 64 SER 65 0.0217

SER 65 ASN 66 -0.0004

ASN 66 HIS 67 0.1589

HIS 67 PRO 68 0.0001

PRO 68 PHE 69 0.0349

PHE 69 LEU 70 0.0001

LEU 70 VAL 71 0.0334

VAL 71 GLY 72 0.0002

GLY 72 LEU 73 0.1041

LEU 73 HIS 74 0.0002

HIS 74 SER 75 0.0497

SER 75 CYS 76 0.0001

CYS 76 PHE 77 0.0581

PHE 77 GLN 78 0.0001

GLN 78 THR 79 0.0840

THR 79 GLU 80 -0.0003

GLU 80 SER 81 -0.0336

SER 81 ARG 82 -0.0000

ARG 82 LEU 83 -0.0135

LEU 83 PHE 84 -0.0003

PHE 84 PHE 85 0.0194

PHE 85 VAL 86 -0.0002

VAL 86 ILE 87 0.0866

ILE 87 GLU 88 0.0002

GLU 88 TYR 89 -0.0753

TYR 89 VAL 90 -0.0005

VAL 90 ASN 91 -0.0587

ASN 91 GLY 92 -0.0003

GLY 92 GLY 93 0.0521

GLY 93 ASP 94 -0.0000

ASP 94 LEU 95 0.0052

LEU 95 MET 96 -0.0003

MET 96 PHE 97 0.0113

PHE 97 HIS 98 -0.0000

HIS 98 MET 99 0.0580

MET 99 GLN 100 -0.0000

GLN 100 ARG 101 -0.0091

ARG 101 GLN 102 0.0003

GLN 102 ARG 103 0.0521

ARG 103 LYS 104 -0.0001

LYS 104 LEU 105 0.0037

LEU 105 PRO 106 0.0001

PRO 106 GLU 107 0.0151

GLU 107 GLU 108 -0.0001

GLU 108 HIS 109 0.0163

HIS 109 ALA 110 -0.0002

ALA 110 ARG 111 0.0021

ARG 111 PHE 112 -0.0004

PHE 112 TYR 113 -0.0021

TYR 113 SER 114 0.0003

SER 114 ALA 115 0.0161

ALA 115 GLU 116 -0.0001

GLU 116 ILE 117 -0.0006

ILE 117 SER 118 -0.0001

SER 118 LEU 119 0.0170

LEU 119 ALA 120 -0.0002

ALA 120 LEU 121 0.0249

LEU 121 ASN 122 -0.0002

ASN 122 TYR 123 -0.0095

TYR 123 LEU 124 -0.0001

LEU 124 HIS 125 0.0222

HIS 125 GLU 126 0.0003

GLU 126 ARG 127 -0.0378

ARG 127 GLY 128 -0.0002

GLY 128 ILE 129 0.0368

ILE 129 ILE 130 -0.0001

ILE 130 TYR 131 0.0409

TYR 131 ARG 132 0.0000

ARG 132 ASP 133 -0.0066

ASP 133 LEU 134 0.0004

LEU 134 LYS 135 -0.0178

LYS 135 LEU 136 -0.0006

LEU 136 ASP 137 0.0246

ASP 137 ASN 138 0.0001

ASN 138 VAL 139 -0.0246

VAL 139 LEU 140 -0.0003

LEU 140 LEU 141 -0.0142

LEU 141 ASP 142 0.0004

ASP 142 SER 143 -0.0251

SER 143 GLU 144 0.0000

GLU 144 GLY 145 0.0073

GLY 145 HIS 146 0.0002

HIS 146 ILE 147 -0.0223

ILE 147 LYS 148 0.0000

LYS 148 LEU 149 -0.0312

LEU 149 THR 150 -0.0000

THR 150 ASP 151 -0.0838

ASP 151 TYR 152 0.0002

TYR 152 GLY 153 -0.0963

GLY 153 MET 154 0.0004

MET 154 CYS 155 0.0309

CYS 155 LYS 156 0.0003

LYS 156 GLU 157 0.0796

GLU 157 GLY 158 -0.0004

GLY 158 LEU 159 -0.1892

LEU 159 ARG 160 0.0002

ARG 160 PRO 161 -0.0136

PRO 161 GLY 162 -0.0002

GLY 162 ASP 163 -0.0006

ASP 163 THR 164 -0.0000

THR 164 THR 165 0.0452

THR 165 SER 166 -0.0002

SER 166 GLU 167 0.0275

GLU 167 PHE 168 0.0001

PHE 168 CYS 169 -0.0774

CYS 169 GLY 170 0.0002

GLY 170 THR 171 0.0515

THR 171 PRO 172 -0.0003

PRO 172 ASN 173 -0.0298

ASN 173 TYR 174 -0.0001

TYR 174 ILE 175 -0.0258

ILE 175 ALA 176 0.0002

ALA 176 PRO 177 -0.0000

PRO 177 GLU 178 0.0001

GLU 178 ILE 179 0.0069

ILE 179 LEU 180 -0.0004

LEU 180 ARG 181 0.0212

ARG 181 GLY 182 0.0003

GLY 182 GLU 183 0.0223

GLU 183 ASP 184 -0.0003

ASP 184 TYR 185 0.0578

TYR 185 GLY 186 -0.0003

GLY 186 PHE 187 0.0655

PHE 187 SER 188 0.0001

SER 188 VAL 189 -0.0099

VAL 189 ASP 190 0.0003

ASP 190 TRP 191 -0.0393

TRP 191 TRP 192 0.0002

TRP 192 ALA 193 0.0270

ALA 193 LEU 194 -0.0001

LEU 194 GLY 195 -0.0202

GLY 195 VAL 196 -0.0003

VAL 196 LEU 197 0.0298

LEU 197 MET 198 -0.0004

MET 198 PHE 199 -0.0038

PHE 199 GLU 200 0.0000

GLU 200 MET 201 0.0597

MET 201 MET 202 0.0000

MET 202 ALA 203 0.0012

ALA 203 GLY 204 0.0001

GLY 204 ARG 205 0.0934

ARG 205 SER 206 0.0000

SER 206 PRO 207 0.0864

PRO 207 PHE 208 0.0001

PHE 208 ASP 209 -0.1594

ASP 209 ILE 210 -0.0001

ILE 210 VAL 211 -0.0832

VAL 211 GLY 212 0.0000

GLY 212 SER 213 0.0485

SER 213 SER 214 -0.0002

SER 214 ASP 215 -0.0347

ASP 215 ASN 216 0.0000

ASN 216 PRO 217 0.0337

PRO 217 ASP 218 -0.0003

ASP 218 GLN 219 0.0183

GLN 219 ASN 220 0.0000

ASN 220 THR 221 -0.0243

THR 221 GLU 222 -0.0000

GLU 222 ASP 223 -0.0559

ASP 223 TYR 224 -0.0000

TYR 224 LEU 225 0.1401

LEU 225 PHE 226 0.0002

PHE 226 GLN 227 0.0166

GLN 227 VAL 228 0.0002

VAL 228 ILE 229 -0.1460

ILE 229 LEU 230 -0.0001

LEU 230 GLU 231 -0.1528

GLU 231 LYS 232 -0.0003

LYS 232 GLN 233 -0.0349

GLN 233 ILE 234 -0.0003

ILE 234 ARG 235 -0.0015

ARG 235 ILE 236 -0.0002

ILE 236 PRO 237 0.0009

PRO 237 ARG 238 0.0000

ARG 238 SER 239 0.0272

SER 239 LEU 240 -0.0001

LEU 240 SER 241 -0.0176

SER 241 VAL 242 -0.0001

VAL 242 LYS 243 -0.0091

LYS 243 ALA 244 -0.0003

ALA 244 ALA 245 -0.0192

ALA 245 SER 246 -0.0000

SER 246 VAL 247 0.0040

VAL 247 LEU 248 0.0002

LEU 248 LYS 249 0.0473

LYS 249 SER 250 -0.0002

SER 250 PHE 251 -0.0209

PHE 251 LEU 252 0.0002

LEU 252 ASN 253 0.0425

ASN 253 LYS 254 -0.0001

LYS 254 ASP 255 -0.0877

ASP 255 PRO 256 -0.0004

PRO 256 LYS 257 -0.0166

LYS 257 GLU 258 0.0001

GLU 258 ARG 259 0.0264

ARG 259 LEU 260 -0.0003

LEU 260 GLY 261 -0.0319

GLY 261 CYS 262 0.0000

CYS 262 HIS 263 -0.0026

HIS 263 PRO 264 0.0000

PRO 264 GLN 265 -0.0160

GLN 265 THR 266 -0.0004

THR 266 GLY 267 -0.0044

GLY 267 PHE 268 -0.0002

PHE 268 ALA 269 -0.0070

ALA 269 ASP 270 -0.0001

ASP 270 ILE 271 0.0177

ILE 271 GLN 272 0.0001

GLN 272 GLY 273 -0.0190

GLY 273 HIS 274 -0.0003

HIS 274 PRO 275 0.0043

PRO 275 PHE 276 0.0000

PHE 276 PHE 277 -0.0244

PHE 277 ARG 278 0.0000

ARG 278 ASN 279 0.0025

ASN 279 VAL 280 0.0000

VAL 280 ASP 281 -0.0156

ASP 281 TRP 282 -0.0004

TRP 282 ASP 283 -0.0102

ASP 283 MET 284 -0.0001

MET 284 MET 285 -0.0021

MET 285 GLU 286 -0.0003

GLU 286 GLN 287 -0.0052

GLN 287 LYS 288 -0.0000

LYS 288 GLN 289 0.0176

GLN 289 VAL 290 -0.0001

VAL 290 VAL 291 0.0132

VAL 291 PRO 292 0.0001

PRO 292 PRO 293 -0.0001

PRO 293 PHE 294 0.0001

PHE 294 LYS 295 0.0898

LYS 295 PRO 296 -0.0003

PRO 296 ASN 297 0.0619

ASN 297 ILE 298 -0.0001

ILE 298 SER 299 0.0300

SER 299 GLY 300 -0.0002

GLY 300 GLU 301 -0.0457

GLU 301 PHE 302 0.0001

PHE 302 GLY 303 0.0352

GLY 303 LEU 304 0.0002

LEU 304 ASP 305 -0.0151

ASP 305 ASN 306 -0.0002

ASN 306 PHE 307 -0.0408

PHE 307 ASP 308 -0.0003

ASP 308 SER 309 -0.0218

SER 309 GLN 310 0.0002

GLN 310 PHE 311 0.0106

PHE 311 THR 312 0.0001

THR 312 ASN 313 0.0077

ASN 313 GLU 314 -0.0002

GLU 314 PRO 315 -0.0170

PRO 315 VAL 316 0.0003

VAL 316 GLN 317 0.0874

GLN 317 LEU 318 0.0000

LEU 318 GLU 319 0.0591

GLU 319 PRO 320 -0.0001

PRO 320 ASP 321 0.0519

ASP 321 ASP 322 -0.0004

ASP 322 ASP 323 -0.0034

ASP 323 ASP 324 -0.0001

ASP 324 ILE 325 -0.0871

ILE 325 VAL 326 0.0002

VAL 326 ARG 327 0.0210

ARG 327 LYS 328 0.0002

LYS 328 ILE 329 -0.0224

ILE 329 ASP 330 -0.0000

ASP 330 GLN 331 0.0051

GLN 331 SER 332 -0.0000

SER 332 GLU 333 -0.0094

GLU 333 PHE 334 -0.0001

PHE 334 GLU 335 0.0015

GLU 335 GLY 336 0.0000

GLY 336 PHE 337 -0.0073

PHE 337 GLU 338 -0.0000

GLU 338 TYR 339 0.0953

TYR 339 ILE 340 -0.0003

ILE 340 ASN 341 0.0896

ASN 341 PRO 342 0.0000

PRO 342 LEU 343 0.0093

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 9 ---

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

* zxy *