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

* *

CA strain for 250216133155656269

--- 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
MET 1 GLU 2 0.0000

GLU 2 LEU 3 -0.0075

LEU 3 ARG 4 -0.0001

ARG 4 HIS 5 -0.0187

HIS 5 THR 6 0.0001

THR 6 PRO 7 0.0028

PRO 7 ALA 8 -0.0000

ALA 8 ARG 9 -0.0035

ARG 9 ASP 10 -0.0001

ASP 10 LEU 11 0.0053

LEU 11 ASP 12 0.0002

ASP 12 LYS 13 0.0095

LYS 13 PHE 14 0.0000

PHE 14 ILE 15 0.0328

ILE 15 GLU 16 0.0002

GLU 16 ASP 17 0.0388

ASP 17 HIS 18 0.0002

HIS 18 LEU 19 -0.0047

LEU 19 LEU 20 -0.0000

LEU 20 PRO 21 -0.0680

PRO 21 ASN 22 -0.0000

ASN 22 THR 23 0.0122

THR 23 CYS 24 -0.0000

CYS 24 PHE 25 0.0577

PHE 25 ARG 26 0.0002

ARG 26 THR 27 0.0383

THR 27 GLN 28 0.0001

GLN 28 VAL 29 -0.0171

VAL 29 LYS 30 0.0000

LYS 30 GLU 31 -0.0435

GLU 31 ALA 32 0.0001

ALA 32 ILE 33 -0.0473

ILE 33 ASP 34 -0.0000

ASP 34 ILE 35 -0.0330

ILE 35 VAL 36 0.0001

VAL 36 CYS 37 -0.0462

CYS 37 ARG 38 -0.0000

ARG 38 PHE 39 0.0300

PHE 39 LEU 40 -0.0001

LEU 40 LYS 41 -0.0027

LYS 41 GLU 42 -0.0003

GLU 42 ARG 43 -0.0538

ARG 43 CYS 44 0.0001

CYS 44 PHE 45 -0.0200

PHE 45 GLN 46 0.0002

GLN 46 GLY 47 0.0218

GLY 47 THR 48 0.0001

THR 48 ALA 49 -0.0467

ALA 49 ASP 50 -0.0003

ASP 50 PRO 51 0.0236

PRO 51 VAL 52 0.0002

VAL 52 ARG 53 0.0345

ARG 53 VAL 54 -0.0005

VAL 54 SER 55 -0.0937

SER 55 LYS 56 -0.0003

LYS 56 VAL 57 -0.0303

VAL 57 VAL 58 -0.0001

VAL 58 LYS 59 0.0646

LYS 59 GLY 60 0.0001

GLY 60 GLY 61 -0.0533

GLY 61 SER 62 -0.0001

SER 62 SER 63 0.0405

SER 63 GLY 64 -0.0003

GLY 64 LYS 65 -0.0034

LYS 65 GLY 66 0.0002

GLY 66 THR 67 0.0446

THR 67 THR 68 -0.0002

THR 68 LEU 69 0.0159

LEU 69 ARG 70 0.0002

ARG 70 GLY 71 -0.1504

GLY 71 ARG 72 -0.0002

ARG 72 SER 73 -0.1174

SER 73 ASP 74 0.0004

ASP 74 ALA 75 -0.0432

ALA 75 ASP 76 0.0002

ASP 76 LEU 77 -0.0480

LEU 77 VAL 78 -0.0005

VAL 78 VAL 79 0.0154

VAL 79 PHE 80 -0.0003

PHE 80 LEU 81 0.0310

LEU 81 THR 82 0.0003

THR 82 LYS 83 0.0276

LYS 83 LEU 84 -0.0001

LEU 84 THR 85 -0.0208

THR 85 SER 86 0.0001

SER 86 PHE 87 -0.0432

PHE 87 GLU 88 -0.0000

GLU 88 ASP 89 -0.0195

ASP 89 GLN 90 0.0001

GLN 90 LEU 91 -0.0037

LEU 91 ARG 92 -0.0001

ARG 92 ARG 93 0.0216

ARG 93 ARG 94 -0.0000

ARG 94 GLY 95 0.0329

GLY 95 GLU 96 -0.0002

GLU 96 PHE 97 0.0013

PHE 97 ILE 98 0.0003

ILE 98 GLN 99 0.0023

GLN 99 GLU 100 0.0006

GLU 100 ILE 101 -0.0233

ILE 101 ARG 102 0.0003

ARG 102 ARG 103 -0.0575

ARG 103 GLN 104 0.0001

GLN 104 LEU 105 -0.0193

LEU 105 GLU 106 -0.0004

GLU 106 ALA 107 -0.0136

ALA 107 CYS 108 -0.0001

CYS 108 GLN 109 -0.0277

GLN 109 ARG 110 -0.0002

ARG 110 GLU 111 0.0071

GLU 111 GLN 112 0.0001

GLN 112 LYS 113 -0.0209

LYS 113 PHE 114 0.0000

PHE 114 LYS 115 0.0215

LYS 115 VAL 116 -0.0000

VAL 116 THR 117 0.0147

THR 117 PHE 118 0.0001

PHE 118 GLU 119 -0.0075

GLU 119 VAL 120 -0.0005

VAL 120 GLN 121 0.0343

GLN 121 SER 122 -0.0000

SER 122 PRO 123 -0.0453

PRO 123 ARG 124 0.0003

ARG 124 ARG 125 -0.0114

ARG 125 GLU 126 -0.0001

GLU 126 ASN 127 0.0308

ASN 127 PRO 128 0.0001

PRO 128 ARG 129 -0.0044

ARG 129 ALA 130 -0.0000

ALA 130 PHE 131 0.2479

PHE 131 SER 132 -0.0000

SER 132 PHE 133 0.0643

PHE 133 VAL 134 -0.0001

VAL 134 LEU 135 0.0157

LEU 135 SER 136 0.0002

SER 136 SER 137 0.0340

SER 137 PRO 138 0.0000

PRO 138 GLN 139 -0.0087

GLN 139 LEU 140 -0.0001

LEU 140 GLN 141 -0.0067

GLN 141 GLN 142 -0.0004

GLN 142 GLU 143 -0.0247

GLU 143 VAL 144 -0.0000

VAL 144 GLU 145 0.0249

GLU 145 PHE 146 0.0003

PHE 146 ASP 147 0.0140

ASP 147 VAL 148 -0.0003

VAL 148 LEU 149 0.0054

LEU 149 PRO 150 -0.0003

PRO 150 ALA 151 0.0240

ALA 151 PHE 152 -0.0000

PHE 152 ASP 153 0.0328

ASP 153 ALA 154 -0.0001

ALA 154 LEU 155 0.0848

LEU 155 GLY 156 -0.0001

GLY 156 GLN 157 0.0188

GLN 157 TRP 158 0.0000

TRP 158 THR 159 0.0053

THR 159 PRO 160 0.0000

PRO 160 GLY 161 -0.0058

GLY 161 TYR 162 -0.0001

TYR 162 LYS 163 -0.0244

LYS 163 PRO 164 -0.0003

PRO 164 ASN 165 -0.0045

ASN 165 PRO 166 0.0001

PRO 166 GLU 167 0.0370

GLU 167 ILE 168 -0.0002

ILE 168 TYR 169 -0.0302

TYR 169 VAL 170 -0.0002

VAL 170 GLN 171 0.0067

GLN 171 LEU 172 0.0001

LEU 172 ILE 173 0.0073

ILE 173 LYS 174 0.0000

LYS 174 GLU 175 0.0400

GLU 175 CYS 176 0.0001

CYS 176 LYS 177 -0.0176

LYS 177 SER 178 0.0002

SER 178 ARG 179 0.0344

ARG 179 GLY 180 0.0003

GLY 180 LYS 181 0.0136

LYS 181 GLU 182 -0.0003

GLU 182 GLY 183 -0.0028

GLY 183 GLU 184 0.0001

GLU 184 PHE 185 -0.0281

PHE 185 SER 186 -0.0001

SER 186 THR 187 0.0919

THR 187 CYS 188 -0.0001

CYS 188 PHE 189 0.0189

PHE 189 THR 190 0.0004

THR 190 GLU 191 -0.0089

GLU 191 LEU 192 0.0003

LEU 192 GLN 193 0.0002

GLN 193 ARG 194 -0.0001

ARG 194 ARG 194 0.0377

ARG 194 ASP 195 -0.0098

ASP 195 PHE 196 -0.0002

PHE 196 LEU 197 0.0637

LEU 197 ARG 198 -0.0000

ARG 198 ASN 199 -0.0357

ASN 199 ARG 200 -0.0001

ARG 200 PRO 201 0.0831

PRO 201 THR 202 -0.0000

THR 202 LYS 203 0.0509

LYS 203 LEU 204 -0.0002

LEU 204 LYS 205 -0.0640

LYS 205 SER 206 0.0001

SER 206 LEU 207 -0.0194

LEU 207 ILE 208 -0.0001

ILE 208 ARG 209 -0.0116

ARG 209 LEU 210 -0.0003

LEU 210 VAL 211 -0.0060

VAL 211 LYS 212 -0.0002

LYS 212 HIS 213 -0.0510

HIS 213 TRP 214 -0.0001

TRP 214 TYR 215 -0.0338

TYR 215 GLN 216 -0.0002

GLN 216 THR 217 -0.0353

THR 217 CYS 218 -0.0004

CYS 218 LYS 219 -0.0302

LYS 219 LYS 220 0.0000

LYS 220 THR 221 0.0113

THR 221 HIS 222 -0.0000

HIS 222 GLY 223 -0.0294

GLY 223 ASN 224 -0.0003

ASN 224 LYS 225 0.0196

LYS 225 LEU 226 0.0003

LEU 226 PRO 227 -0.0817

PRO 227 PRO 228 0.0002

PRO 228 GLN 229 0.0669

GLN 229 TYR 230 0.0001

TYR 230 ALA 231 0.0237

ALA 231 LEU 232 -0.0004

LEU 232 GLU 233 0.0229

GLU 233 LEU 234 -0.0001

LEU 234 LEU 235 -0.0050

LEU 235 THR 236 0.0002

THR 236 VAL 237 0.0361

VAL 237 TYR 238 0.0001

TYR 238 ALA 239 0.0476

ALA 239 TRP 240 0.0002

TRP 240 GLU 241 0.0185

GLU 241 GLN 242 -0.0001

GLN 242 GLY 243 0.0335

GLY 243 SER 244 0.0002

SER 244 ARG 245 0.0082

ARG 245 LYS 246 -0.0005

LYS 246 THR 247 -0.0208

THR 247 ASP 248 0.0002

ASP 248 PHE 249 0.0275

PHE 249 SER 250 -0.0004

SER 250 THR 251 -0.0278

THR 251 ALA 252 0.0002

ALA 252 GLN 253 -0.0040

GLN 253 GLY 254 0.0000

GLY 254 PHE 255 0.0141

PHE 255 GLN 256 0.0002

GLN 256 THR 257 0.0242

THR 257 VAL 258 -0.0001

VAL 258 LEU 259 0.0122

LEU 259 GLU 260 -0.0005

GLU 260 LEU 261 -0.0052

LEU 261 VAL 262 -0.0003

VAL 262 LEU 263 0.0112

LEU 263 LYS 264 0.0005

LYS 264 HIS 265 -0.0210

HIS 265 GLN 266 -0.0001

GLN 266 LYS 267 0.0424

LYS 267 LEU 268 0.0004

LEU 268 CYS 269 0.0568

CYS 269 ILE 270 0.0000

ILE 270 PHE 271 0.0495

PHE 271 TRP 272 -0.0001

TRP 272 GLU 273 0.0821

GLU 273 ALA 274 0.0002

ALA 274 TYR 275 0.0313

TYR 275 TYR 276 -0.0000

TYR 276 ASP 277 -0.0391

ASP 277 PHE 278 0.0003

PHE 278 THR 279 0.0260

THR 279 ASN 280 -0.0003

ASN 280 PRO 281 -0.0385

PRO 281 VAL 282 -0.0002

VAL 282 VAL 283 0.0097

VAL 283 GLY 284 0.0000

GLY 284 ARG 285 -0.0014

ARG 285 CYS 286 -0.0005

CYS 286 MET 287 0.0253

MET 287 LEU 288 0.0000

LEU 288 GLN 289 0.0098

GLN 289 GLN 290 0.0001

GLN 290 LEU 291 0.0344

LEU 291 LYS 292 0.0003

LYS 292 LYS 293 -0.0099

LYS 293 PRO 294 -0.0002

PRO 294 ARG 295 -0.0314

ARG 295 PRO 296 -0.0003

PRO 296 VAL 297 -0.0438

VAL 297 ILE 298 -0.0001

ILE 298 LEU 299 -0.0262

LEU 299 ASP 300 0.0001

ASP 300 PRO 301 -0.0361

PRO 301 ALA 302 0.0001

ALA 302 ASP 303 0.0191

ASP 303 PRO 304 -0.0000

PRO 304 THR 305 0.0310

THR 305 GLY 306 -0.0003

GLY 306 ASN 307 -0.1524

ASN 307 VAL 308 0.0000

VAL 308 GLY 309 -0.0640

GLY 309 GLY 310 0.0002

GLY 310 GLY 311 0.0595

GLY 311 ASP 312 0.0003

ASP 312 THR 313 -0.0071

THR 313 HIS 314 0.0004

HIS 314 SER 315 0.0190

SER 315 TRP 316 0.0002

TRP 316 GLN 317 -0.0130

GLN 317 ARG 318 -0.0002

ARG 318 LEU 319 0.0184

LEU 319 ALA 320 0.0004

ALA 320 GLN 321 0.0138

GLN 321 GLU 322 -0.0002

GLU 322 ALA 323 0.0079

ALA 323 ARG 324 -0.0001

ARG 324 VAL 325 0.0075

VAL 325 TRP 326 -0.0004

TRP 326 LEU 327 -0.0025

LEU 327 GLY 328 0.0000

GLY 328 TYR 329 -0.0009

TYR 329 PRO 330 0.0000

PRO 330 CYS 331 0.0161

CYS 331 CYS 332 0.0003

CYS 332 LYS 333 0.0087

LYS 333 ASN 334 -0.0001

ASN 334 LEU 335 0.0344

LEU 335 ASP 336 -0.0002

ASP 336 GLY 337 -0.0467

GLY 337 SER 338 -0.0000

SER 338 LEU 339 -0.0061

LEU 339 VAL 340 0.0001

VAL 340 GLY 341 0.0247

GLY 341 ALA 342 0.0001

ALA 342 TRP 343 0.0402

TRP 343 THR 344 -0.0003

THR 344 MET 345 0.0258

MET 345 LEU 346 -0.0000

LEU 346 GLN 347 0.0001

GLN 347 LYS 348 -0.0001

LYS 348 ILE 349 -0.0004

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 8th, 2025.

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

*** ***

CA strain for 250216133155656269

--- normal mode 8 ---

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

* *