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

* *

CA strain for 220926155553133140

--- normal mode 10 ---

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 -0.0003

GLU 2 LEU 3 0.0227

LEU 3 ARG 4 -0.0002

ARG 4 HIS 5 -0.0275

HIS 5 THR 6 0.0001

THR 6 PRO 7 -0.0344

PRO 7 ALA 8 -0.0003

ALA 8 ARG 9 0.0489

ARG 9 ASP 10 -0.0002

ASP 10 LEU 11 -0.0132

LEU 11 ASP 12 -0.0000

ASP 12 LYS 13 0.0955

LYS 13 PHE 14 0.0004

PHE 14 ILE 15 0.0028

ILE 15 GLU 16 -0.0004

GLU 16 ASP 17 0.0949

ASP 17 HIS 18 -0.0003

HIS 18 LEU 19 0.0161

LEU 19 LEU 20 0.0000

LEU 20 PRO 21 -0.3181

PRO 21 ASN 22 0.0003

ASN 22 THR 23 -0.0577

THR 23 CYS 24 -0.0002

CYS 24 PHE 25 0.1142

PHE 25 ARG 26 -0.0003

ARG 26 THR 27 -0.0163

THR 27 GLN 28 -0.0002

GLN 28 VAL 29 0.0841

VAL 29 LYS 30 -0.0003

LYS 30 GLU 31 0.0899

GLU 31 ALA 32 0.0001

ALA 32 ILE 33 0.0991

ILE 33 ASP 34 -0.0002

ASP 34 ILE 35 0.0831

ILE 35 VAL 36 -0.0003

VAL 36 CYS 37 0.0852

CYS 37 ARG 38 0.0000

ARG 38 PHE 39 0.0140

PHE 39 LEU 40 -0.0003

LEU 40 LYS 41 -0.0022

LYS 41 GLU 42 0.0002

GLU 42 ARG 43 0.1188

ARG 43 CYS 44 0.0002

CYS 44 PHE 45 0.0277

PHE 45 GLN 46 -0.0002

GLN 46 GLY 47 -0.0455

GLY 47 THR 48 -0.0003

THR 48 ALA 49 0.0697

ALA 49 ASP 50 0.0002

ASP 50 PRO 51 -0.0747

PRO 51 VAL 52 0.0001

VAL 52 ARG 53 -0.0629

ARG 53 VAL 54 0.0000

VAL 54 SER 55 0.1926

SER 55 LYS 56 -0.0004

LYS 56 VAL 57 0.0301

VAL 57 VAL 58 0.0003

VAL 58 LYS 59 -0.1136

LYS 59 GLY 60 -0.0001

GLY 60 GLY 61 0.0067

GLY 61 SER 62 -0.0001

SER 62 SER 63 0.0583

SER 63 GLY 64 0.0001

GLY 64 LYS 65 -0.0183

LYS 65 GLY 66 0.0000

GLY 66 THR 67 0.0951

THR 67 THR 68 0.0001

THR 68 LEU 69 0.0859

LEU 69 ARG 70 -0.0002

ARG 70 GLY 71 -0.1782

GLY 71 ARG 72 0.0001

ARG 72 SER 73 -0.0690

SER 73 ASP 74 -0.0001

ASP 74 ALA 75 -0.1155

ALA 75 ASP 76 0.0005

ASP 76 LEU 77 -0.0919

LEU 77 VAL 78 -0.0005

VAL 78 VAL 79 -0.0797

VAL 79 PHE 80 0.0001

PHE 80 LEU 81 -0.0492

LEU 81 THR 82 -0.0001

THR 82 LYS 83 -0.0439

LYS 83 LEU 84 0.0001

LEU 84 THR 85 0.0228

THR 85 SER 86 0.0002

SER 86 PHE 87 0.0979

PHE 87 GLU 88 0.0003

GLU 88 ASP 89 0.0846

ASP 89 GLN 90 -0.0004

GLN 90 LEU 91 0.0086

LEU 91 ARG 92 0.0003

ARG 92 ARG 93 0.0156

ARG 93 ARG 94 0.0001

ARG 94 GLY 95 -0.0136

GLY 95 GLU 96 -0.0004

GLU 96 PHE 97 -0.0092

PHE 97 ILE 98 -0.0000

ILE 98 GLN 99 -0.0313

GLN 99 GLU 100 0.0005

GLU 100 ILE 101 -0.0262

ILE 101 ARG 102 -0.0002

ARG 102 ARG 103 0.0665

ARG 103 GLN 104 0.0004

GLN 104 LEU 105 -0.0257

LEU 105 GLU 106 0.0000

GLU 106 ALA 107 0.0054

ALA 107 CYS 108 0.0002

CYS 108 GLN 109 0.0436

GLN 109 ARG 110 0.0002

ARG 110 GLU 111 -0.0249

GLU 111 GLN 112 0.0002

GLN 112 LYS 113 0.0242

LYS 113 PHE 114 0.0001

PHE 114 LYS 115 0.0238

LYS 115 VAL 116 0.0001

VAL 116 THR 117 0.0458

THR 117 PHE 118 0.0002

PHE 118 GLU 119 0.1427

GLU 119 VAL 120 -0.0000

VAL 120 GLN 121 0.0368

GLN 121 SER 122 0.0002

SER 122 PRO 123 -0.1032

PRO 123 ARG 124 0.0001

ARG 124 ARG 125 -0.0736

ARG 125 GLU 126 -0.0000

GLU 126 ASN 127 0.1257

ASN 127 PRO 128 0.0002

PRO 128 ARG 129 -0.0141

ARG 129 GLY 130 0.0002

GLY 130 LEU 131 -0.2375

LEU 131 SER 132 -0.0001

SER 132 PHE 133 0.0153

PHE 133 VAL 134 -0.0000

VAL 134 LEU 135 -0.0148

LEU 135 SER 136 -0.0001

SER 136 SER 137 0.0192

SER 137 PRO 138 0.0001

PRO 138 GLN 139 0.0132

GLN 139 LEU 140 0.0002

LEU 140 GLN 141 0.0071

GLN 141 GLN 142 0.0002

GLN 142 GLU 143 0.0613

GLU 143 VAL 144 0.0001

VAL 144 GLU 145 0.0717

GLU 145 PHE 146 0.0002

PHE 146 ASP 147 0.0389

ASP 147 VAL 148 0.0001

VAL 148 LEU 149 -0.0232

LEU 149 PRO 150 0.0000

PRO 150 ALA 151 -0.0232

ALA 151 PHE 152 0.0003

PHE 152 ASP 153 -0.0506

ASP 153 ALA 154 -0.0000

ALA 154 LEU 155 -0.0791

LEU 155 GLY 156 0.0002

GLY 156 GLN 157 -0.0488

GLN 157 TRP 158 0.0001

TRP 158 THR 159 -0.0124

THR 159 PRO 160 0.0003

PRO 160 GLY 161 -0.0064

GLY 161 TYR 162 0.0003

TYR 162 LYS 163 -0.0463

LYS 163 PRO 164 0.0005

PRO 164 ASN 165 0.0289

ASN 165 PRO 166 0.0001

PRO 166 GLU 167 -0.0097

GLU 167 ILE 168 0.0001

ILE 168 TYR 169 0.0591

TYR 169 VAL 170 -0.0001

VAL 170 GLN 171 0.0463

GLN 171 LEU 172 -0.0001

LEU 172 ILE 173 0.0415

ILE 173 LYS 174 -0.0002

LYS 174 GLU 175 0.0137

GLU 175 CYS 176 -0.0001

CYS 176 LYS 177 -0.0047

LYS 177 SER 178 0.0000

SER 178 ARG 179 0.0007

ARG 179 GLY 180 0.0001

GLY 180 LYS 181 -0.0518

LYS 181 GLU 182 -0.0002

GLU 182 GLY 183 -0.0071

GLY 183 GLU 184 -0.0000

GLU 184 PHE 185 -0.0018

PHE 185 SER 186 0.0000

SER 186 THR 187 0.0457

THR 187 CYS 188 -0.0005

CYS 188 PHE 189 0.0075

PHE 189 THR 190 0.0000

THR 190 GLU 191 -0.0061

GLU 191 LEU 192 -0.0002

LEU 192 GLN 193 0.0081

GLN 193 ARG 194 -0.0001

ARG 194 ARG 194 0.0000

ARG 194 ASP 195 0.0188

ASP 195 PHE 196 -0.0002

PHE 196 LEU 197 0.0618

LEU 197 ARG 198 0.0001

ARG 198 ASN 199 -0.0782

ASN 199 ARG 200 -0.0001

ARG 200 PRO 201 0.0202

PRO 201 THR 202 -0.0002

THR 202 LYS 203 -0.0244

LYS 203 LEU 204 -0.0001

LEU 204 LYS 205 -0.1598

LYS 205 SER 206 0.0000

SER 206 LEU 207 -0.0575

LEU 207 ILE 208 -0.0002

ILE 208 ARG 209 -0.0387

ARG 209 LEU 210 0.0003

LEU 210 VAL 211 0.0388

VAL 211 LYS 212 -0.0002

LYS 212 HIS 213 -0.0298

HIS 213 TRP 214 0.0001

TRP 214 TYR 215 -0.0190

TYR 215 GLN 216 0.0001

GLN 216 THR 217 -0.0692

THR 217 CYS 218 -0.0002

CYS 218 LYS 219 -0.0381

LYS 219 LYS 220 0.0002

LYS 220 THR 221 0.0312

THR 221 HIS 222 -0.0000

HIS 222 GLY 223 -0.0022

GLY 223 ASN 224 0.0002

ASN 224 LYS 225 -0.0420

LYS 225 LEU 226 -0.0001

LEU 226 PRO 227 -0.0522

PRO 227 PRO 228 -0.0000

PRO 228 GLN 229 0.0136

GLN 229 TYR 230 -0.0002

TYR 230 ALA 231 0.0448

ALA 231 LEU 232 0.0001

LEU 232 GLU 233 0.0386

GLU 233 LEU 234 -0.0002

LEU 234 LEU 235 0.0486

LEU 235 THR 236 -0.0002

THR 236 VAL 237 0.0261

VAL 237 TYR 238 -0.0003

TYR 238 ALA 239 0.1175

ALA 239 TRP 240 0.0003

TRP 240 GLU 241 0.0480

GLU 241 GLN 242 -0.0003

GLN 242 GLY 243 0.0718

GLY 243 SER 244 0.0003

SER 244 ARG 245 -0.0329

ARG 245 LYS 246 -0.0000

LYS 246 THR 247 -0.0190

THR 247 ASP 248 0.0001

ASP 248 PHE 249 -0.0014

PHE 249 SER 250 -0.0000

SER 250 THR 251 -0.0303

THR 251 ALA 252 0.0000

ALA 252 GLN 253 0.0322

GLN 253 GLY 254 -0.0000

GLY 254 PHE 255 0.0077

PHE 255 GLN 256 0.0002

GLN 256 THR 257 0.0615

THR 257 VAL 258 -0.0003

VAL 258 LEU 259 -0.0336

LEU 259 GLU 260 -0.0001

GLU 260 LEU 261 0.0909

LEU 261 VAL 262 0.0001

VAL 262 LEU 263 -0.0265

LEU 263 LYS 264 0.0003

LYS 264 HIS 265 0.0476

HIS 265 GLN 266 0.0003

GLN 266 LYS 267 -0.0732

LYS 267 LEU 268 -0.0002

LEU 268 CYS 269 0.0447

CYS 269 ILE 270 -0.0000

ILE 270 PHE 271 -0.0833

PHE 271 TRP 272 0.0003

TRP 272 GLU 273 0.0110

GLU 273 ALA 274 -0.0000

ALA 274 TYR 275 0.0006

TYR 275 TYR 276 0.0001

TYR 276 ASP 277 0.0054

ASP 277 PHE 278 0.0003

PHE 278 THR 279 -0.0304

THR 279 ASN 280 0.0003

ASN 280 PRO 281 0.0111

PRO 281 VAL 282 -0.0001

VAL 282 VAL 283 0.0199

VAL 283 GLY 284 -0.0002

GLY 284 ARG 285 0.0124

ARG 285 CYS 286 -0.0003

CYS 286 MET 287 0.0944

MET 287 LEU 288 -0.0000

LEU 288 GLN 289 -0.0141

GLN 289 GLN 290 -0.0003

GLN 290 LEU 291 0.1402

LEU 291 LYS 292 0.0003

LYS 292 LYS 293 -0.1383

LYS 293 PRO 294 -0.0001

PRO 294 ARG 295 0.0378

ARG 295 PRO 296 0.0001

PRO 296 VAL 297 0.0016

VAL 297 ILE 298 0.0003

ILE 298 LEU 299 0.0491

LEU 299 ASP 300 0.0006

ASP 300 PRO 301 -0.0159

PRO 301 ALA 302 0.0001

ALA 302 ASP 303 0.0065

ASP 303 PRO 304 -0.0002

PRO 304 THR 305 -0.0183

THR 305 GLY 306 -0.0003

GLY 306 ASN 307 0.2019

ASN 307 VAL 308 0.0002

VAL 308 GLY 309 0.0996

GLY 309 GLY 310 -0.0002

GLY 310 GLY 311 -0.0546

GLY 311 ASP 312 0.0003

ASP 312 THR 313 0.0338

THR 313 HIS 314 0.0002

HIS 314 SER 315 0.0463

SER 315 TRP 316 -0.0001

TRP 316 GLN 317 0.0247

GLN 317 ARG 318 -0.0001

ARG 318 LEU 319 -0.0070

LEU 319 ALA 320 -0.0001

ALA 320 GLN 321 0.0200

GLN 321 GLU 322 0.0001

GLU 322 ALA 323 -0.0188

ALA 323 ARG 324 0.0001

ARG 324 VAL 325 0.0458

VAL 325 TRP 326 -0.0003

TRP 326 LEU 327 -0.0254

LEU 327 GLY 328 -0.0000

GLY 328 TYR 329 0.0093

TYR 329 PRO 330 -0.0004

PRO 330 CYS 331 0.0255

CYS 331 CYS 332 -0.0001

CYS 332 LYS 333 0.0248

LYS 333 ASN 334 -0.0000

ASN 334 LEU 335 0.1406

LEU 335 ASP 336 -0.0003

ASP 336 GLY 337 -0.0508

GLY 337 SER 338 -0.0005

SER 338 LEU 339 0.0496

LEU 339 VAL 340 0.0004

VAL 340 GLY 341 0.1588

GLY 341 ALA 342 0.0001

ALA 342 TRP 343 0.0584

TRP 343 THR 344 -0.0000

THR 344 MET 345 0.1043

MET 345 LEU 346 0.0000

LEU 346 GLN 347 0.0157

GLN 347 LYS 348 0.0001

LYS 348 ILE 349 0.0293

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: October 18th, 2018.

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

*** ***

CA strain for 220926155553133140

--- normal mode 10 ---

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

* *