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

* CfusW145A_RX *

CA strain for 22020815032149861

--- normal mode 7 ---

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 -0.0000

LYS 3 ARG 4 -0.0217

ARG 4 PRO 5 0.0003

PRO 5 ILE 6 0.0121

ILE 6 ARG 7 -0.0001

ARG 7 ILE 8 -0.0298

ILE 8 ILE 9 -0.0001

ILE 9 GLN 10 -0.0001

GLN 10 TRP 11 0.0004

TRP 11 GLY 12 -0.0144

GLY 12 CYS 13 0.0003

CYS 13 GLY 14 0.2207

GLY 14 LEU 15 0.0001

LEU 15 MET 16 0.0129

MET 16 GLY 17 -0.0001

GLY 17 GLN 18 -0.0406

GLN 18 THR 19 0.0001

THR 19 LEU 20 -0.0108

LEU 20 ILE 21 -0.0004

ILE 21 ARG 22 0.0048

ARG 22 THR 23 0.0003

THR 23 LEU 24 -0.0046

LEU 24 ARG 25 0.0000

ARG 25 GLU 26 0.0597

GLU 26 LYS 27 -0.0000

LYS 27 GLY 28 -0.0154

GLY 28 ALA 29 -0.0000

ALA 29 GLU 30 0.0360

GLU 30 LEU 31 0.0000

LEU 31 VAL 32 -0.0150

VAL 32 GLY 33 0.0000

GLY 33 ALA 34 0.0201

ALA 34 ILE 35 -0.0003

ILE 35 ASP 36 0.0085

ASP 36 HIS 37 -0.0001

HIS 37 ASN 38 -0.0146

ASN 38 ALA 39 0.0000

ALA 39 ALA 40 0.0022

ALA 40 ARG 41 -0.0002

ARG 41 ARG 42 0.0297

ARG 42 ASP 43 -0.0003

ASP 43 ARG 44 -0.0071

ARG 44 ASP 45 0.0002

ASP 45 ALA 46 0.0133

ALA 46 GLY 47 -0.0001

GLY 47 GLU 48 0.0240

GLU 48 VAL 49 0.0000

VAL 49 ALA 50 0.0535

ALA 50 GLY 51 -0.0000

GLY 51 LEU 52 -0.0237

LEU 52 GLY 53 0.0000

GLY 53 GLN 54 -0.0120

GLN 54 SER 55 -0.0002

SER 55 LEU 56 0.0122

LEU 56 GLY 57 0.0004

GLY 57 VAL 58 -0.0373

VAL 58 ARG 59 0.0000

ARG 59 ILE 60 -0.0133

ILE 60 HIS 61 -0.0002

HIS 61 PRO 62 -0.0123

PRO 62 PRO 63 0.0003

PRO 63 ASP 64 0.0017

ASP 64 GLN 65 -0.0002

GLN 65 ALA 66 -0.0267

ALA 66 ASP 67 0.0001

ASP 67 ASP 67 0.0049

ASP 67 ALA 68 -0.0197

ALA 68 VAL 69 0.0002

VAL 69 PHE 70 0.0069

PHE 70 ARG 71 0.0000

ARG 71 GLU 72 0.0043

GLU 72 ALA 73 -0.0000

ALA 73 ARG 74 0.0077

ARG 74 ALA 75 0.0000

ALA 75 ASP 76 0.0057

ASP 76 VAL 77 -0.0001

VAL 77 CYS 78 -0.0072

CYS 78 ILE 79 -0.0002

ILE 79 LEU 80 -0.0118

LEU 80 CYS 81 -0.0004

CYS 81 THR 82 -0.1086

THR 82 ARG 83 -0.0002

ARG 83 SER 84 -0.1656

SER 84 ILE 85 -0.0001

ILE 85 MET 86 0.1551

MET 86 SER 87 -0.0002

SER 87 GLU 88 0.0111

GLU 88 LEU 89 -0.0004

LEU 89 ALA 90 0.0878

ALA 90 GLY 91 0.0000

GLY 91 ALA 92 -0.0460

ALA 92 LEU 93 0.0000

LEU 93 ARG 94 0.0139

ARG 94 VAL 95 -0.0002

VAL 95 ALA 96 -0.0268

ALA 96 ALA 97 -0.0003

ALA 97 ARG 98 -0.0335

ARG 98 HIS 99 0.0002

HIS 99 GLY 100 -0.0150

GLY 100 VAL 101 -0.0000

VAL 101 ASN 102 -0.0250

ASN 102 ALA 103 0.0000

ALA 103 ILE 104 0.0159

ILE 104 THR 105 -0.0001

THR 105 ILE 106 0.0395

ILE 106 GLY 107 0.0002

GLY 107 GLU 108 -0.0835

GLU 108 GLU 109 -0.0000

GLU 109 ALA 110 0.0509

ALA 110 PHE 111 0.0001

PHE 111 TYR 112 -0.0486

TYR 112 PRO 113 -0.0001

PRO 113 TRP 114 0.0180

TRP 114 THR 115 0.0002

THR 115 THR 116 0.0344

THR 116 SER 117 0.0001

SER 117 GLN 118 0.0771

GLN 118 ALA 119 -0.0000

ALA 119 LEU 120 -0.0161

LEU 120 THR 121 -0.0000

THR 121 GLU 122 0.0292

GLU 122 GLU 123 -0.0002

GLU 123 LEU 124 0.0024

LEU 124 ASP 125 -0.0001

ASP 125 GLN 126 -0.0217

GLN 126 LEU 127 0.0003

LEU 127 ALA 128 0.0055

ALA 128 ARG 129 -0.0001

ARG 129 ALA 130 -0.0119

ALA 130 ASN 131 0.0004

ASN 131 ASP 132 -0.0245

ASP 132 CYS 133 -0.0002

CYS 133 THR 134 -0.0239

THR 134 LEU 135 -0.0004

LEU 135 THR 136 -0.0147

THR 136 GLY 137 -0.0001

GLY 137 SER 138 -0.0003

SER 138 GLY 139 -0.0000

GLY 139 PHE 140 0.0039

PHE 140 GLN 141 -0.0001

GLN 141 ASP 142 -0.0413

ASP 142 VAL 143 -0.0002

VAL 143 PHE 144 -0.1012

PHE 144 ALA 145 0.0002

ALA 145 GLY 146 -0.0018

GLY 146 ASN 147 0.0004

ASN 147 LEU 148 -0.1394

LEU 148 ILE 149 0.0001

ILE 149 THR 150 -0.0233

THR 150 VAL 151 -0.0003

VAL 151 VAL 151 -0.0031

VAL 151 LEU 152 -0.0123

LEU 152 ALA 153 0.0000

ALA 153 GLY 154 -0.0182

GLY 154 ALA 155 -0.0001

ALA 155 THR 156 0.0034

THR 156 HIS 157 0.0000

HIS 157 ARG 158 -0.0243

ARG 158 ILE 159 0.0001

ILE 159 ASP 160 0.0007

ASP 160 ARG 161 -0.0000

ARG 161 ILE 162 0.0348

ILE 162 VAL 163 0.0000

VAL 163 GLY 164 0.0213

GLY 164 LEU 165 -0.0004

LEU 165 THR 166 0.0174

THR 166 GLN 167 -0.0002

GLN 167 TYR 168 0.0222

TYR 168 ASN 169 -0.0002

ASN 169 ALA 170 0.0382

ALA 170 ASP 171 -0.0003

ASP 171 ASP 172 -0.1570

ASP 172 TYR 173 -0.0001

TYR 173 GLY 174 0.0104

GLY 174 SER 175 -0.0001

SER 175 ALA 176 0.0777

ALA 176 LEU 177 0.0000

LEU 177 ALA 178 0.0937

ALA 178 GLN 179 0.0001

GLN 179 LYS 180 0.0062

LYS 180 HIS 181 0.0002

HIS 181 GLY 182 0.0440

GLY 182 VAL 183 -0.0004

VAL 183 GLY 184 0.0121

GLY 184 LEU 185 -0.0001

LEU 185 ASP 186 -0.0094

ASP 186 PRO 187 0.0001

PRO 187 GLU 188 -0.0153

GLU 188 THR 189 0.0000

THR 189 PHE 190 -0.0111

PHE 190 ALA 191 -0.0000

ALA 191 ALA 192 -0.0571

ALA 192 ARG 193 -0.0002

ARG 193 ILE 194 0.0014

ILE 194 GLY 195 0.0001

GLY 195 ALA 196 -0.0319

ALA 196 SER 197 0.0001

SER 197 ASN 198 0.0239

ASN 198 SER 199 -0.0001

SER 199 PRO 200 0.1531

PRO 200 SER 201 0.0002

SER 201 TYR 202 -0.0135

TYR 202 VAL 203 0.0002

VAL 203 TRP 204 -0.0205

TRP 204 ASN 205 0.0002

ASN 205 SER 206 0.0316

SER 206 ASN 207 0.0001

ASN 207 GLU 208 -0.0736

GLU 208 TRP 209 0.0003

TRP 209 LEU 210 -0.0657

LEU 210 CYS 211 -0.0001

CYS 211 ALA 212 0.0201

ALA 212 GLN 213 -0.0002

GLN 213 LEU 214 0.0107

LEU 214 GLY 215 0.0001

GLY 215 TRP 216 0.0435

TRP 216 ARG 217 0.0002

ARG 217 VAL 218 0.0037

VAL 218 ARG 219 0.0001

ARG 219 ASP 220 0.0088

ASP 220 ILE 221 0.0005

ILE 221 ARG 222 0.0310

ARG 222 GLN 223 -0.0002

GLN 223 GLN 224 0.0635

GLN 224 LEU 225 -0.0007

LEU 225 LEU 226 0.0712

LEU 226 PRO 227 0.0002

PRO 227 THR 228 0.0097

THR 228 THR 229 -0.0002

THR 229 HIS 230 0.0492

HIS 230 THR 231 0.0000

THR 231 GLY 232 0.0298

GLY 232 THR 233 0.0000

THR 233 LEU 234 -0.0054

LEU 234 ARG 235 0.0002

ARG 235 SER 236 0.0400

SER 236 ALA 237 -0.0001

ALA 237 SER 238 0.0480

SER 238 LEU 239 -0.0002

LEU 239 GLY 240 0.0762

GLY 240 ARG 241 0.0002

ARG 241 GLU 242 0.0101

GLU 242 VAL 243 0.0001

VAL 243 PRO 244 -0.0099

PRO 244 ALA 245 -0.0002

ALA 245 GLY 246 0.0057

GLY 246 HIS 247 -0.0001

HIS 247 ALA 248 0.0037

ALA 248 THR 249 0.0001

THR 249 GLY 250 0.0283

GLY 250 MET 251 -0.0004

MET 251 LYS 252 -0.0201

LYS 252 ALA 253 -0.0001

ALA 253 VAL 254 -0.0029

VAL 254 VAL 255 -0.0001

VAL 255 VAL 256 -0.0019

VAL 256 THR 257 0.0001

THR 257 GLU 258 0.0060

GLU 258 THR 259 -0.0001

THR 259 HIS 260 -0.0020

HIS 260 GLU 261 0.0001

GLU 261 GLY 262 0.0160

GLY 262 PRO 263 0.0000

PRO 263 VAL 264 0.0051

VAL 264 ILE 265 0.0000

ILE 265 GLU 266 0.0039

GLU 266 THR 267 0.0005

THR 267 HIS 268 -0.0130

HIS 268 CYS 269 0.0000

CYS 269 VAL 270 0.0111

VAL 270 GLY 271 0.0001

GLY 271 LYS 272 0.0266

LYS 272 LEU 273 -0.0000

LEU 273 TYR 274 0.0422

TYR 274 ALA 275 -0.0000

ALA 275 PRO 276 0.0117

PRO 276 GLY 277 0.0001

GLY 277 GLU 278 -0.0221

GLU 278 VAL 279 -0.0000

VAL 279 ASP 280 -0.0539

ASP 280 LEU 281 0.0000

LEU 281 ASN 282 -0.0587

ASN 282 GLU 283 -0.0003

GLU 283 TRP 284 0.0240

TRP 284 THR 285 0.0001

THR 285 LEU 286 0.0212

LEU 286 ARG 287 -0.0002

ARG 287 GLY 288 0.0072

GLY 288 GLU 289 -0.0000

GLU 289 PRO 290 0.0143

PRO 290 ASP 291 -0.0002

ASP 291 THR 292 0.0344

THR 292 THR 293 -0.0000

THR 293 VAL 294 0.0601

VAL 294 THR 295 -0.0003

THR 295 ILE 296 0.0898

ILE 296 ARG 297 0.0000

ARG 297 GLN 298 0.0112

GLN 298 PRO 299 0.0003

PRO 299 ALA 300 0.1327

ALA 300 THR 301 0.0002

THR 301 PRO 302 0.0977

PRO 302 ALA 303 -0.0002

ALA 303 LEU 304 0.1267

LEU 304 THR 305 -0.0000

THR 305 CYS 306 0.0571

CYS 306 ALA 307 0.0001

ALA 307 THR 308 0.1267

THR 308 VAL 309 0.0001

VAL 309 LEU 310 0.0137

LEU 310 ASN 311 0.0000

ASN 311 ARG 312 0.0541

ARG 312 LEU 313 -0.0002

LEU 313 PRO 314 -0.0077

PRO 314 GLN 315 -0.0001

GLN 315 LEU 316 -0.0162

LEU 316 LEU 317 0.0000

LEU 317 ALA 318 0.0065

ALA 318 ALA 319 0.0002

ALA 319 PRO 320 -0.0112

PRO 320 PRO 321 0.0000

PRO 321 GLY 322 0.0455

GLY 322 PHE 323 0.0001

PHE 323 VAL 324 -0.0833

VAL 324 THR 325 0.0000

THR 325 THR 326 -0.0273

THR 326 ASP 327 0.0002

ASP 327 ARG 328 -0.0070

ARG 328 PHE 329 0.0001

PHE 329 THR 330 -0.0435

THR 330 PRO 331 -0.0003

PRO 331 ALA 332 0.1279

ALA 332 THR 333 -0.0001

THR 333 TYR 334 0.1324

TYR 334 VAL 335 0.0002

VAL 335 SER 336 0.0477

SER 336 ARG 337 -0.0002

ARG 337 LEU 338 -0.0043

LEU 338 GLU 339 0.0001

GLU 339 THR 340 -0.0381

THR 340 GLU 341 -0.0000

GLU 341 ALA 342 0.0137

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 7 ---

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

* CfusW145A_RX *