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

* CfusW145A_RX *

CA strain for 22020815032149861

--- 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
SER 2 LYS 3 0.0002

LYS 3 ARG 4 -0.0721

ARG 4 PRO 5 0.0002

PRO 5 ILE 6 -0.0048

ILE 6 ARG 7 -0.0001

ARG 7 ILE 8 0.0237

ILE 8 ILE 9 -0.0004

ILE 9 GLN 10 -0.0112

GLN 10 TRP 11 0.0003

TRP 11 GLY 12 0.0516

GLY 12 CYS 13 -0.0002

CYS 13 GLY 14 -0.3179

GLY 14 LEU 15 -0.0001

LEU 15 MET 16 -0.0048

MET 16 GLY 17 -0.0001

GLY 17 GLN 18 0.0838

GLN 18 THR 19 -0.0001

THR 19 LEU 20 0.0080

LEU 20 ILE 21 0.0001

ILE 21 ARG 22 -0.0223

ARG 22 THR 23 -0.0001

THR 23 LEU 24 -0.0111

LEU 24 ARG 25 0.0000

ARG 25 GLU 26 -0.0312

GLU 26 LYS 27 0.0003

LYS 27 GLY 28 0.0409

GLY 28 ALA 29 -0.0001

ALA 29 GLU 30 0.0259

GLU 30 LEU 31 0.0004

LEU 31 VAL 32 -0.0106

VAL 32 GLY 33 0.0003

GLY 33 ALA 34 -0.0300

ALA 34 ILE 35 -0.0000

ILE 35 ASP 36 0.0035

ASP 36 HIS 37 0.0002

HIS 37 ASN 38 0.0394

ASN 38 ALA 39 -0.0003

ALA 39 ALA 40 0.0007

ALA 40 ARG 41 0.0004

ARG 41 ARG 42 -0.0160

ARG 42 ASP 43 -0.0002

ASP 43 ARG 44 0.0171

ARG 44 ASP 45 -0.0003

ASP 45 ALA 46 0.0241

ALA 46 GLY 47 -0.0001

GLY 47 GLU 48 -0.0390

GLU 48 VAL 49 -0.0001

VAL 49 ALA 50 -0.0519

ALA 50 GLY 51 -0.0003

GLY 51 LEU 52 0.0138

LEU 52 GLY 53 -0.0001

GLY 53 GLN 54 0.0105

GLN 54 SER 55 -0.0003

SER 55 LEU 56 -0.0421

LEU 56 GLY 57 -0.0001

GLY 57 VAL 58 -0.0281

VAL 58 ARG 59 0.0002

ARG 59 ILE 60 0.0117

ILE 60 HIS 61 0.0002

HIS 61 PRO 62 0.0091

PRO 62 PRO 63 -0.0004

PRO 63 ASP 64 -0.0269

ASP 64 GLN 65 -0.0002

GLN 65 ALA 66 -0.0038

ALA 66 ASP 67 0.0003

ASP 67 ASP 67 0.0049

ASP 67 ALA 68 -0.0136

ALA 68 VAL 69 0.0003

VAL 69 PHE 70 -0.0393

PHE 70 ARG 71 0.0002

ARG 71 GLU 72 -0.0500

GLU 72 ALA 73 0.0001

ALA 73 ARG 74 0.0276

ARG 74 ALA 75 0.0001

ALA 75 ASP 76 0.0699

ASP 76 VAL 77 -0.0002

VAL 77 CYS 78 0.0017

CYS 78 ILE 79 -0.0001

ILE 79 LEU 80 0.0176

LEU 80 CYS 81 -0.0003

CYS 81 THR 82 0.1865

THR 82 ARG 83 -0.0001

ARG 83 SER 84 0.0828

SER 84 ILE 85 0.0003

ILE 85 MET 86 -0.0238

MET 86 SER 87 0.0001

SER 87 GLU 88 -0.0436

GLU 88 LEU 89 0.0001

LEU 89 ALA 90 0.0127

ALA 90 GLY 91 0.0000

GLY 91 ALA 92 0.0327

ALA 92 LEU 93 0.0001

LEU 93 ARG 94 0.0329

ARG 94 VAL 95 -0.0004

VAL 95 ALA 96 -0.0212

ALA 96 ALA 97 -0.0001

ALA 97 ARG 98 0.0256

ARG 98 HIS 99 0.0000

HIS 99 GLY 100 0.0709

GLY 100 VAL 101 0.0001

VAL 101 ASN 102 0.0818

ASN 102 ALA 103 0.0000

ALA 103 ILE 104 0.0152

ILE 104 THR 105 -0.0002

THR 105 ILE 106 -0.0176

ILE 106 GLY 107 0.0001

GLY 107 GLU 108 0.0415

GLU 108 GLU 109 0.0001

GLU 109 ALA 110 0.0296

ALA 110 PHE 111 0.0002

PHE 111 TYR 112 -0.0034

TYR 112 PRO 113 0.0001

PRO 113 TRP 114 0.0339

TRP 114 THR 115 -0.0003

THR 115 THR 116 0.0222

THR 116 SER 117 0.0003

SER 117 GLN 118 0.0462

GLN 118 ALA 119 -0.0001

ALA 119 LEU 120 0.0169

LEU 120 THR 121 -0.0004

THR 121 GLU 122 0.0089

GLU 122 GLU 123 0.0000

GLU 123 LEU 124 0.0093

LEU 124 ASP 125 -0.0005

ASP 125 GLN 126 0.0089

GLN 126 LEU 127 -0.0001

LEU 127 ALA 128 -0.0130

ALA 128 ARG 129 -0.0002

ARG 129 ALA 130 0.0089

ALA 130 ASN 131 0.0000

ASN 131 ASP 132 0.0407

ASP 132 CYS 133 0.0001

CYS 133 THR 134 0.0257

THR 134 LEU 135 -0.0000

LEU 135 THR 136 0.0086

THR 136 GLY 137 -0.0001

GLY 137 SER 138 -0.0112

SER 138 GLY 139 -0.0005

GLY 139 PHE 140 -0.0261

PHE 140 GLN 141 -0.0001

GLN 141 ASP 142 -0.0086

ASP 142 VAL 143 -0.0001

VAL 143 PHE 144 -0.0222

PHE 144 ALA 145 0.0001

ALA 145 GLY 146 0.0046

GLY 146 ASN 147 0.0003

ASN 147 LEU 148 -0.0630

LEU 148 ILE 149 -0.0003

ILE 149 THR 150 -0.0192

THR 150 VAL 151 0.0000

VAL 151 VAL 151 -0.0046

VAL 151 LEU 152 0.0506

LEU 152 ALA 153 0.0001

ALA 153 GLY 154 -0.0491

GLY 154 ALA 155 -0.0005

ALA 155 THR 156 -0.0210

THR 156 HIS 157 0.0000

HIS 157 ARG 158 -0.0641

ARG 158 ILE 159 0.0000

ILE 159 ASP 160 -0.0395

ASP 160 ARG 161 -0.0003

ARG 161 ILE 162 0.1200

ILE 162 VAL 163 0.0001

VAL 163 GLY 164 0.1855

GLY 164 LEU 165 0.0001

LEU 165 THR 166 0.0926

THR 166 GLN 167 0.0003

GLN 167 TYR 168 0.1325

TYR 168 ASN 169 -0.0000

ASN 169 ALA 170 0.0670

ALA 170 ASP 171 0.0001

ASP 171 ASP 172 0.0267

ASP 172 TYR 173 0.0002

TYR 173 GLY 174 0.1824

GLY 174 SER 175 -0.0001

SER 175 ALA 176 -0.2425

ALA 176 LEU 177 0.0002

LEU 177 ALA 178 -0.0791

ALA 178 GLN 179 -0.0003

GLN 179 LYS 180 -0.2951

LYS 180 HIS 181 -0.0001

HIS 181 GLY 182 0.0424

GLY 182 VAL 183 -0.0000

VAL 183 GLY 184 0.0381

GLY 184 LEU 185 0.0004

LEU 185 ASP 186 0.1429

ASP 186 PRO 187 -0.0002

PRO 187 GLU 188 -0.1087

GLU 188 THR 189 -0.0001

THR 189 PHE 190 -0.0672

PHE 190 ALA 191 -0.0001

ALA 191 ALA 192 0.0661

ALA 192 ARG 193 -0.0003

ARG 193 ILE 194 -0.0759

ILE 194 GLY 195 0.0002

GLY 195 ALA 196 -0.0642

ALA 196 SER 197 -0.0001

SER 197 ASN 198 -0.1593

ASN 198 SER 199 -0.0002

SER 199 PRO 200 0.1843

PRO 200 SER 201 0.0006

SER 201 TYR 202 0.0923

TYR 202 VAL 203 -0.0001

VAL 203 TRP 204 -0.0482

TRP 204 ASN 205 0.0001

ASN 205 SER 206 0.0449

SER 206 ASN 207 -0.0001

ASN 207 GLU 208 -0.0971

GLU 208 TRP 209 0.0000

TRP 209 LEU 210 -0.0645

LEU 210 CYS 211 0.0000

CYS 211 ALA 212 -0.0111

ALA 212 GLN 213 0.0004

GLN 213 LEU 214 0.0124

LEU 214 GLY 215 -0.0002

GLY 215 TRP 216 0.0390

TRP 216 ARG 217 0.0002

ARG 217 VAL 218 0.0330

VAL 218 ARG 219 -0.0001

ARG 219 ASP 220 0.0232

ASP 220 ILE 221 -0.0000

ILE 221 ARG 222 0.0663

ARG 222 GLN 223 0.0001

GLN 223 GLN 224 0.1674

GLN 224 LEU 225 -0.0002

LEU 225 LEU 226 0.2412

LEU 226 PRO 227 0.0003

PRO 227 THR 228 0.0443

THR 228 THR 229 0.0003

THR 229 HIS 230 0.2262

HIS 230 THR 231 -0.0003

THR 231 GLY 232 0.0031

GLY 232 THR 233 -0.0001

THR 233 LEU 234 -0.0500

LEU 234 ARG 235 0.0002

ARG 235 SER 236 -0.1608

SER 236 ALA 237 0.0000

ALA 237 SER 238 -0.2215

SER 238 LEU 239 -0.0001

LEU 239 GLY 240 -0.2259

GLY 240 ARG 241 0.0003

ARG 241 GLU 242 -0.0071

GLU 242 VAL 243 0.0000

VAL 243 PRO 244 0.0139

PRO 244 ALA 245 0.0002

ALA 245 GLY 246 0.0005

GLY 246 HIS 247 -0.0000

HIS 247 ALA 248 0.0263

ALA 248 THR 249 -0.0002

THR 249 GLY 250 -0.0362

GLY 250 MET 251 0.0000

MET 251 LYS 252 0.0307

LYS 252 ALA 253 -0.0004

ALA 253 VAL 254 0.0282

VAL 254 VAL 255 0.0002

VAL 255 VAL 256 0.0096

VAL 256 THR 257 0.0003

THR 257 GLU 258 0.0594

GLU 258 THR 259 0.0004

THR 259 HIS 260 0.0068

HIS 260 GLU 261 -0.0000

GLU 261 GLY 262 0.0603

GLY 262 PRO 263 0.0002

PRO 263 VAL 264 0.0290

VAL 264 ILE 265 -0.0002

ILE 265 GLU 266 0.0620

GLU 266 THR 267 -0.0004

THR 267 HIS 268 0.0422

HIS 268 CYS 269 -0.0000

CYS 269 VAL 270 0.1242

VAL 270 GLY 271 0.0003

GLY 271 LYS 272 -0.0045

LYS 272 LEU 273 0.0001

LEU 273 TYR 274 -0.0038

TYR 274 ALA 275 -0.0000

ALA 275 PRO 276 -0.0132

PRO 276 GLY 277 0.0002

GLY 277 GLU 278 0.1149

GLU 278 VAL 279 0.0001

VAL 279 ASP 280 -0.0835

ASP 280 LEU 281 -0.0002

LEU 281 ASN 282 0.1796

ASN 282 GLU 283 -0.0002

GLU 283 TRP 284 0.1631

TRP 284 THR 285 -0.0001

THR 285 LEU 286 0.1093

LEU 286 ARG 287 0.0002

ARG 287 GLY 288 -0.0176

GLY 288 GLU 289 0.0000

GLU 289 PRO 290 0.0431

PRO 290 ASP 291 -0.0000

ASP 291 THR 292 0.1319

THR 292 THR 293 0.0003

THR 293 VAL 294 0.1805

VAL 294 THR 295 -0.0001

THR 295 ILE 296 0.1839

ILE 296 ARG 297 -0.0001

ARG 297 GLN 298 0.0898

GLN 298 PRO 299 -0.0002

PRO 299 ALA 300 0.1985

ALA 300 THR 301 -0.0002

THR 301 PRO 302 0.0788

PRO 302 ALA 303 -0.0002

ALA 303 LEU 304 0.1366

LEU 304 THR 305 -0.0000

THR 305 CYS 306 0.1972

CYS 306 ALA 307 -0.0000

ALA 307 THR 308 0.1023

THR 308 VAL 309 0.0000

VAL 309 LEU 310 0.1127

LEU 310 ASN 311 0.0001

ASN 311 ARG 312 0.0207

ARG 312 LEU 313 -0.0000

LEU 313 PRO 314 0.0365

PRO 314 GLN 315 -0.0002

GLN 315 LEU 316 0.0274

LEU 316 LEU 317 0.0001

LEU 317 ALA 318 0.0138

ALA 318 ALA 319 -0.0001

ALA 319 PRO 320 -0.0369

PRO 320 PRO 321 -0.0003

PRO 321 GLY 322 -0.0050

GLY 322 PHE 323 0.0004

PHE 323 VAL 324 0.0025

VAL 324 THR 325 0.0001

THR 325 THR 326 0.0245

THR 326 ASP 327 0.0002

ASP 327 ARG 328 -0.0192

ARG 328 PHE 329 0.0001

PHE 329 THR 330 0.0462

THR 330 PRO 331 -0.0002

PRO 331 ALA 332 0.0930

ALA 332 THR 333 0.0003

THR 333 TYR 334 0.0811

TYR 334 VAL 335 -0.0001

VAL 335 SER 336 -0.0138

SER 336 ARG 337 0.0000

ARG 337 LEU 338 -0.0223

LEU 338 GLU 339 0.0001

GLU 339 THR 340 -0.0148

THR 340 GLU 341 0.0001

GLU 341 ALA 342 0.0127

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.

*** CfusW145A_RX ***

CA strain for 22020815032149861

--- normal mode 11 ---

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

* CfusW145A_RX *