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

* CfusW145A_RX *

CA strain for 22020815032149861

--- 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
SER 2 LYS 3 0.0002

LYS 3 ARG 4 -0.0592

ARG 4 PRO 5 0.0002

PRO 5 ILE 6 -0.0089

ILE 6 ARG 7 0.0003

ARG 7 ILE 8 -0.0705

ILE 8 ILE 9 -0.0002

ILE 9 GLN 10 -0.1135

GLN 10 TRP 11 0.0002

TRP 11 GLY 12 -0.0018

GLY 12 CYS 13 0.0003

CYS 13 GLY 14 -0.3032

GLY 14 LEU 15 -0.0002

LEU 15 MET 16 0.0120

MET 16 GLY 17 0.0001

GLY 17 GLN 18 0.0189

GLN 18 THR 19 -0.0002

THR 19 LEU 20 -0.0310

LEU 20 ILE 21 -0.0000

ILE 21 ARG 22 0.0291

ARG 22 THR 23 -0.0001

THR 23 LEU 24 0.0020

LEU 24 ARG 25 -0.0000

ARG 25 GLU 26 0.0149

GLU 26 LYS 27 -0.0002

LYS 27 GLY 28 0.0045

GLY 28 ALA 29 0.0003

ALA 29 GLU 30 0.0469

GLU 30 LEU 31 -0.0001

LEU 31 VAL 32 -0.0362

VAL 32 GLY 33 -0.0002

GLY 33 ALA 34 -0.0116

ALA 34 ILE 35 -0.0002

ILE 35 ASP 36 0.0501

ASP 36 HIS 37 0.0002

HIS 37 ASN 38 0.0425

ASN 38 ALA 39 0.0001

ALA 39 ALA 40 -0.0093

ALA 40 ARG 41 -0.0001

ARG 41 ARG 42 -0.0141

ARG 42 ASP 43 -0.0001

ASP 43 ARG 44 0.0086

ARG 44 ASP 45 0.0001

ASP 45 ALA 46 -0.0082

ALA 46 GLY 47 0.0000

GLY 47 GLU 48 0.0318

GLU 48 VAL 49 -0.0001

VAL 49 ALA 50 0.0238

ALA 50 GLY 51 0.0002

GLY 51 LEU 52 -0.0154

LEU 52 GLY 53 -0.0004

GLY 53 GLN 54 0.0010

GLN 54 SER 55 -0.0003

SER 55 LEU 56 0.0126

LEU 56 GLY 57 -0.0001

GLY 57 VAL 58 -0.0114

VAL 58 ARG 59 -0.0002

ARG 59 ILE 60 -0.0308

ILE 60 HIS 61 -0.0000

HIS 61 PRO 62 0.0005

PRO 62 PRO 63 -0.0004

PRO 63 ASP 64 -0.0205

ASP 64 GLN 65 -0.0005

GLN 65 ALA 66 0.0084

ALA 66 ASP 67 -0.0000

ASP 67 ASP 67 -0.0333

ASP 67 ALA 68 -0.0186

ALA 68 VAL 69 0.0001

VAL 69 PHE 70 0.0343

PHE 70 ARG 71 -0.0003

ARG 71 GLU 72 -0.0097

GLU 72 ALA 73 0.0003

ALA 73 ARG 74 0.0260

ARG 74 ALA 75 -0.0001

ALA 75 ASP 76 0.0880

ASP 76 VAL 77 -0.0001

VAL 77 CYS 78 -0.0846

CYS 78 ILE 79 -0.0001

ILE 79 LEU 80 -0.0752

LEU 80 CYS 81 0.0001

CYS 81 THR 82 0.0075

THR 82 ARG 83 0.0004

ARG 83 SER 84 -0.1543

SER 84 ILE 85 0.0002

ILE 85 MET 86 -0.0811

MET 86 SER 87 0.0001

SER 87 GLU 88 0.0149

GLU 88 LEU 89 0.0002

LEU 89 ALA 90 -0.0398

ALA 90 GLY 91 0.0003

GLY 91 ALA 92 0.0485

ALA 92 LEU 93 -0.0001

LEU 93 ARG 94 0.0297

ARG 94 VAL 95 0.0001

VAL 95 ALA 96 0.0132

ALA 96 ALA 97 0.0001

ALA 97 ARG 98 0.0689

ARG 98 HIS 99 -0.0000

HIS 99 GLY 100 0.1118

GLY 100 VAL 101 0.0003

VAL 101 ASN 102 0.0684

ASN 102 ALA 103 0.0001

ALA 103 ILE 104 -0.0126

ILE 104 THR 105 -0.0004

THR 105 ILE 106 -0.0425

ILE 106 GLY 107 0.0001

GLY 107 GLU 108 -0.1120

GLU 108 GLU 109 0.0001

GLU 109 ALA 110 -0.0526

ALA 110 PHE 111 0.0002

PHE 111 TYR 112 0.0053

TYR 112 PRO 113 -0.0001

PRO 113 TRP 114 -0.0078

TRP 114 THR 115 -0.0001

THR 115 THR 116 0.0112

THR 116 SER 117 0.0000

SER 117 GLN 118 0.0156

GLN 118 ALA 119 0.0001

ALA 119 LEU 120 0.0200

LEU 120 THR 121 0.0006

THR 121 GLU 122 -0.0132

GLU 122 GLU 123 0.0002

GLU 123 LEU 124 0.0112

LEU 124 ASP 125 -0.0003

ASP 125 GLN 126 0.0151

GLN 126 LEU 127 -0.0001

LEU 127 ALA 128 -0.0103

ALA 128 ARG 129 -0.0003

ARG 129 ALA 130 0.0221

ALA 130 ASN 131 0.0002

ASN 131 ASP 132 0.0331

ASP 132 CYS 133 0.0000

CYS 133 THR 134 0.0315

THR 134 LEU 135 0.0000

LEU 135 THR 136 0.0371

THR 136 GLY 137 0.0004

GLY 137 SER 138 0.0294

SER 138 GLY 139 -0.0001

GLY 139 PHE 140 0.0198

PHE 140 GLN 141 -0.0004

GLN 141 ASP 142 0.0107

ASP 142 VAL 143 0.0003

VAL 143 PHE 144 0.1039

PHE 144 ALA 145 -0.0005

ALA 145 GLY 146 0.0531

GLY 146 ASN 147 -0.0001

ASN 147 LEU 148 0.0865

LEU 148 ILE 149 0.0002

ILE 149 THR 150 0.0214

THR 150 VAL 151 -0.0000

VAL 151 VAL 151 -0.0134

VAL 151 LEU 152 0.0953

LEU 152 ALA 153 -0.0000

ALA 153 GLY 154 -0.0351

GLY 154 ALA 155 -0.0002

ALA 155 THR 156 -0.0037

THR 156 HIS 157 0.0002

HIS 157 ARG 158 -0.0038

ARG 158 ILE 159 -0.0003

ILE 159 ASP 160 0.0094

ASP 160 ARG 161 0.0000

ARG 161 ILE 162 0.0167

ILE 162 VAL 163 0.0000

VAL 163 GLY 164 -0.0350

GLY 164 LEU 165 -0.0001

LEU 165 THR 166 -0.0530

THR 166 GLN 167 -0.0001

GLN 167 TYR 168 -0.0848

TYR 168 ASN 169 -0.0002

ASN 169 ALA 170 0.0072

ALA 170 ASP 171 -0.0002

ASP 171 ASP 172 -0.1160

ASP 172 TYR 173 -0.0003

TYR 173 GLY 174 -0.0047

GLY 174 SER 175 -0.0002

SER 175 ALA 176 -0.1179

ALA 176 LEU 177 -0.0000

LEU 177 ALA 178 -0.1368

ALA 178 GLN 179 0.0003

GLN 179 LYS 180 0.0789

LYS 180 HIS 181 0.0000

HIS 181 GLY 182 -0.0423

GLY 182 VAL 183 -0.0002

VAL 183 GLY 184 -0.0685

GLY 184 LEU 185 0.0001

LEU 185 ASP 186 -0.0813

ASP 186 PRO 187 -0.0001

PRO 187 GLU 188 0.0500

GLU 188 THR 189 -0.0004

THR 189 PHE 190 0.0379

PHE 190 ALA 191 0.0000

ALA 191 ALA 192 -0.0301

ALA 192 ARG 193 -0.0001

ARG 193 ILE 194 0.0199

ILE 194 GLY 195 0.0001

GLY 195 ALA 196 -0.0026

ALA 196 SER 197 0.0001

SER 197 ASN 198 0.0376

ASN 198 SER 199 -0.0000

SER 199 PRO 200 -0.0271

PRO 200 SER 201 -0.0002

SER 201 TYR 202 -0.0041

TYR 202 VAL 203 -0.0002

VAL 203 TRP 204 -0.0105

TRP 204 ASN 205 -0.0000

ASN 205 SER 206 -0.0048

SER 206 ASN 207 -0.0000

ASN 207 GLU 208 0.0084

GLU 208 TRP 209 0.0000

TRP 209 LEU 210 0.0014

LEU 210 CYS 211 -0.0002

CYS 211 ALA 212 0.0522

ALA 212 GLN 213 -0.0005

GLN 213 LEU 214 0.1194

LEU 214 GLY 215 -0.0003

GLY 215 TRP 216 0.0315

TRP 216 ARG 217 -0.0002

ARG 217 VAL 218 0.0045

VAL 218 ARG 219 0.0002

ARG 219 ASP 220 0.0156

ASP 220 ILE 221 0.0001

ILE 221 ARG 222 0.0345

ARG 222 GLN 223 -0.0000

GLN 223 GLN 224 0.0901

GLN 224 LEU 225 0.0003

LEU 225 LEU 226 -0.0052

LEU 226 PRO 227 -0.0001

PRO 227 THR 228 0.0252

THR 228 THR 229 0.0002

THR 229 HIS 230 0.0173

HIS 230 THR 231 -0.0000

THR 231 GLY 232 -0.0507

GLY 232 THR 233 0.0000

THR 233 LEU 234 -0.0246

LEU 234 ARG 235 -0.0000

ARG 235 SER 236 -0.0552

SER 236 ALA 237 0.0004

ALA 237 SER 238 -0.0286

SER 238 LEU 239 0.0002

LEU 239 GLY 240 -0.0456

GLY 240 ARG 241 -0.0001

ARG 241 GLU 242 -0.0359

GLU 242 VAL 243 -0.0002

VAL 243 PRO 244 -0.0631

PRO 244 ALA 245 -0.0001

ALA 245 GLY 246 0.0089

GLY 246 HIS 247 -0.0003

HIS 247 ALA 248 -0.0074

ALA 248 THR 249 0.0001

THR 249 GLY 250 0.0106

GLY 250 MET 251 0.0000

MET 251 LYS 252 0.0863

LYS 252 ALA 253 0.0001

ALA 253 VAL 254 0.0455

VAL 254 VAL 255 -0.0002

VAL 255 VAL 256 0.0237

VAL 256 THR 257 0.0000

THR 257 GLU 258 0.0003

GLU 258 THR 259 -0.0001

THR 259 HIS 260 0.0029

HIS 260 GLU 261 0.0001

GLU 261 GLY 262 -0.0082

GLY 262 PRO 263 0.0003

PRO 263 VAL 264 0.0074

VAL 264 ILE 265 -0.0003

ILE 265 GLU 266 0.0486

GLU 266 THR 267 -0.0003

THR 267 HIS 268 0.0343

HIS 268 CYS 269 -0.0000

CYS 269 VAL 270 0.0336

VAL 270 GLY 271 0.0002

GLY 271 LYS 272 -0.0038

LYS 272 LEU 273 0.0003

LEU 273 TYR 274 -0.0087

TYR 274 ALA 275 0.0004

ALA 275 PRO 276 0.0083

PRO 276 GLY 277 0.0003

GLY 277 GLU 278 0.0181

GLU 278 VAL 279 0.0000

VAL 279 ASP 280 0.0293

ASP 280 LEU 281 -0.0001

LEU 281 ASN 282 0.0517

ASN 282 GLU 283 -0.0001

GLU 283 TRP 284 -0.0336

TRP 284 THR 285 -0.0002

THR 285 LEU 286 -0.0264

LEU 286 ARG 287 0.0001

ARG 287 GLY 288 -0.0205

GLY 288 GLU 289 -0.0001

GLU 289 PRO 290 -0.0104

PRO 290 ASP 291 -0.0002

ASP 291 THR 292 -0.0003

THR 292 THR 293 -0.0002

THR 293 VAL 294 -0.0188

VAL 294 THR 295 0.0001

THR 295 ILE 296 -0.0463

ILE 296 ARG 297 -0.0001

ARG 297 GLN 298 -0.0038

GLN 298 PRO 299 -0.0000

PRO 299 ALA 300 -0.0570

ALA 300 THR 301 0.0004

THR 301 PRO 302 -0.0360

PRO 302 ALA 303 0.0002

ALA 303 LEU 304 -0.0544

LEU 304 THR 305 0.0000

THR 305 CYS 306 0.0194

CYS 306 ALA 307 0.0001

ALA 307 THR 308 -0.0066

THR 308 VAL 309 0.0002

VAL 309 LEU 310 0.0416

LEU 310 ASN 311 0.0003

ASN 311 ARG 312 -0.0014

ARG 312 LEU 313 0.0001

LEU 313 PRO 314 0.0159

PRO 314 GLN 315 -0.0002

GLN 315 LEU 316 0.0115

LEU 316 LEU 317 -0.0001

LEU 317 ALA 318 0.0181

ALA 318 ALA 319 0.0000

ALA 319 PRO 320 -0.0193

PRO 320 PRO 321 0.0003

PRO 321 GLY 322 -0.0149

GLY 322 PHE 323 -0.0002

PHE 323 VAL 324 0.0780

VAL 324 THR 325 0.0000

THR 325 THR 326 0.0307

THR 326 ASP 327 0.0003

ASP 327 ARG 328 0.0251

ARG 328 PHE 329 -0.0001

PHE 329 THR 330 0.0175

THR 330 PRO 331 -0.0003

PRO 331 ALA 332 0.0510

ALA 332 THR 333 -0.0001

THR 333 TYR 334 0.0088

TYR 334 VAL 335 0.0001

VAL 335 SER 336 -0.0054

SER 336 ARG 337 -0.0002

ARG 337 LEU 338 -0.0314

LEU 338 GLU 339 -0.0005

GLU 339 THR 340 -0.0278

THR 340 GLU 341 -0.0001

GLU 341 ALA 342 0.0264

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 8 ---

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

* CfusW145A_RX *