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

* zxy *

CA strain for 2404230438531985751

--- 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 ASP 2 0.0004

ASP 2 PRO 3 0.0038

PRO 3 LEU 4 0.0003

LEU 4 GLY 5 -0.0384

GLY 5 LEU 6 -0.0001

LEU 6 GLN 7 0.0209

GLN 7 ASP 8 0.0005

ASP 8 PHE 9 -0.0145

PHE 9 ASP 10 -0.0002

ASP 10 LEU 11 -0.0162

LEU 11 LEU 12 0.0001

LEU 12 ARG 13 -0.0142

ARG 13 VAL 14 -0.0002

VAL 14 ILE 15 -0.0404

ILE 15 GLY 16 -0.0001

GLY 16 ARG 17 -0.1292

ARG 17 GLY 18 0.0000

GLY 18 SER 19 -0.1739

SER 19 TYR 20 -0.0000

TYR 20 ALA 21 -0.0179

ALA 21 LYS 22 0.0003

LYS 22 VAL 23 -0.0638

VAL 23 LEU 24 0.0000

LEU 24 LEU 25 -0.0318

LEU 25 VAL 26 0.0000

VAL 26 ARG 27 0.0013

ARG 27 LEU 28 -0.0001

LEU 28 LYS 29 -0.0265

LYS 29 LYS 30 -0.0000

LYS 30 THR 31 0.0101

THR 31 ASP 32 0.0003

ASP 32 ARG 33 0.0140

ARG 33 ILE 34 0.0005

ILE 34 TYR 35 -0.0249

TYR 35 ALA 36 -0.0004

ALA 36 MET 37 -0.0447

MET 37 LYS 38 0.0001

LYS 38 VAL 39 -0.0259

VAL 39 VAL 40 0.0000

VAL 40 LYS 41 -0.0357

LYS 41 LYS 42 0.0001

LYS 42 GLU 43 -0.0074

GLU 43 LEU 44 -0.0000

LEU 44 VAL 45 0.0247

VAL 45 ASN 46 0.0001

ASN 46 ASP 47 0.0117

ASP 47 ASP 48 -0.0000

ASP 48 GLU 49 0.0056

GLU 49 ASP 50 -0.0001

ASP 50 ILE 51 -0.0021

ILE 51 ASP 52 -0.0001

ASP 52 TRP 53 -0.0494

TRP 53 VAL 54 0.0000

VAL 54 GLN 55 0.0729

GLN 55 THR 56 0.0001

THR 56 GLU 57 0.0562

GLU 57 LYS 58 0.0002

LYS 58 HIS 59 -0.0299

HIS 59 VAL 60 -0.0000

VAL 60 PHE 61 -0.0302

PHE 61 GLU 62 -0.0002

GLU 62 GLN 63 -0.0625

GLN 63 ALA 64 -0.0002

ALA 64 SER 65 -0.0533

SER 65 ASN 66 -0.0002

ASN 66 HIS 67 0.0541

HIS 67 PRO 68 -0.0003

PRO 68 PHE 69 0.0353

PHE 69 LEU 70 0.0001

LEU 70 VAL 71 -0.0059

VAL 71 GLY 72 -0.0002

GLY 72 LEU 73 0.0722

LEU 73 HIS 74 0.0001

HIS 74 SER 75 0.0338

SER 75 CYS 76 0.0005

CYS 76 PHE 77 0.0332

PHE 77 GLN 78 -0.0004

GLN 78 THR 79 0.0340

THR 79 GLU 80 -0.0003

GLU 80 SER 81 -0.0329

SER 81 ARG 82 -0.0005

ARG 82 LEU 83 0.0169

LEU 83 PHE 84 -0.0000

PHE 84 PHE 85 0.0154

PHE 85 VAL 86 -0.0001

VAL 86 ILE 87 0.0245

ILE 87 GLU 88 -0.0004

GLU 88 TYR 89 -0.0073

TYR 89 VAL 90 0.0005

VAL 90 ASN 91 0.0531

ASN 91 GLY 92 0.0003

GLY 92 GLY 93 0.1730

GLY 93 ASP 94 -0.0003

ASP 94 LEU 95 0.0954

LEU 95 MET 96 0.0001

MET 96 PHE 97 0.0471

PHE 97 HIS 98 0.0000

HIS 98 MET 99 0.0769

MET 99 GLN 100 -0.0004

GLN 100 ARG 101 -0.0232

ARG 101 GLN 102 -0.0000

GLN 102 ARG 103 0.0680

ARG 103 LYS 104 -0.0002

LYS 104 LEU 105 0.0168

LEU 105 PRO 106 -0.0004

PRO 106 GLU 107 -0.0043

GLU 107 GLU 108 0.0001

GLU 108 HIS 109 -0.0261

HIS 109 ALA 110 -0.0003

ALA 110 ARG 111 0.0124

ARG 111 PHE 112 -0.0001

PHE 112 TYR 113 -0.0030

TYR 113 SER 114 0.0001

SER 114 ALA 115 0.0065

ALA 115 GLU 116 0.0001

GLU 116 ILE 117 -0.0007

ILE 117 SER 118 -0.0003

SER 118 LEU 119 -0.0001

LEU 119 ALA 120 0.0001

ALA 120 LEU 121 -0.0087

LEU 121 ASN 122 -0.0000

ASN 122 TYR 123 0.0231

TYR 123 LEU 124 0.0002

LEU 124 HIS 125 -0.0472

HIS 125 GLU 126 -0.0004

GLU 126 ARG 127 0.0512

ARG 127 GLY 128 -0.0000

GLY 128 ILE 129 -0.0298

ILE 129 ILE 130 0.0004

ILE 130 TYR 131 0.0093

TYR 131 ARG 132 0.0002

ARG 132 ASP 133 0.0360

ASP 133 LEU 134 -0.0002

LEU 134 LYS 135 0.0029

LYS 135 LEU 136 -0.0004

LEU 136 ASP 137 -0.0138

ASP 137 ASN 138 -0.0002

ASN 138 VAL 139 -0.0083

VAL 139 LEU 140 -0.0000

LEU 140 LEU 141 0.0339

LEU 141 ASP 142 -0.0003

ASP 142 SER 143 -0.0007

SER 143 GLU 144 0.0001

GLU 144 GLY 145 0.0301

GLY 145 HIS 146 -0.0000

HIS 146 ILE 147 0.0051

ILE 147 LYS 148 -0.0003

LYS 148 LEU 149 0.0012

LEU 149 THR 150 -0.0001

THR 150 ASP 151 -0.0354

ASP 151 TYR 152 0.0003

TYR 152 GLY 153 0.0017

GLY 153 MET 154 -0.0001

MET 154 CYS 155 0.0105

CYS 155 LYS 156 0.0001

LYS 156 GLU 157 -0.0725

GLU 157 GLY 158 0.0001

GLY 158 LEU 159 0.0893

LEU 159 ARG 160 0.0003

ARG 160 PRO 161 0.0142

PRO 161 GLY 162 -0.0004

GLY 162 ASP 163 0.0204

ASP 163 THR 164 0.0001

THR 164 THR 165 0.0060

THR 165 SER 166 0.0002

SER 166 GLU 167 -0.0002

GLU 167 PHE 168 -0.0002

PHE 168 CYS 169 0.0472

CYS 169 GLY 170 -0.0002

GLY 170 THR 171 0.0052

THR 171 PRO 172 -0.0001

PRO 172 ASN 173 -0.0121

ASN 173 TYR 174 0.0001

TYR 174 ILE 175 0.0471

ILE 175 ALA 176 0.0001

ALA 176 PRO 177 0.0117

PRO 177 GLU 178 -0.0004

GLU 178 ILE 179 0.0139

ILE 179 LEU 180 -0.0000

LEU 180 ARG 181 0.0002

ARG 181 GLY 182 0.0001

GLY 182 GLU 183 -0.0168

GLU 183 ASP 184 0.0003

ASP 184 TYR 185 -0.0166

TYR 185 GLY 186 -0.0000

GLY 186 PHE 187 -0.0344

PHE 187 SER 188 -0.0001

SER 188 VAL 189 0.0080

VAL 189 ASP 190 0.0003

ASP 190 TRP 191 0.0002

TRP 191 TRP 192 -0.0002

TRP 192 ALA 193 0.0405

ALA 193 LEU 194 -0.0001

LEU 194 GLY 195 -0.0107

GLY 195 VAL 196 0.0001

VAL 196 LEU 197 0.0496

LEU 197 MET 198 0.0004

MET 198 PHE 199 0.0035

PHE 199 GLU 200 0.0000

GLU 200 MET 201 0.0551

MET 201 MET 202 0.0000

MET 202 ALA 203 0.0283

ALA 203 GLY 204 -0.0003

GLY 204 ARG 205 0.1032

ARG 205 SER 206 -0.0001

SER 206 PRO 207 0.0260

PRO 207 PHE 208 -0.0002

PHE 208 ASP 209 -0.0302

ASP 209 ILE 210 0.0001

ILE 210 VAL 211 -0.0054

VAL 211 GLY 212 0.0002

GLY 212 SER 213 0.0371

SER 213 SER 214 -0.0004

SER 214 ASP 215 -0.0166

ASP 215 ASN 216 0.0002

ASN 216 PRO 217 0.0131

PRO 217 ASP 218 0.0001

ASP 218 GLN 219 -0.0120

GLN 219 ASN 220 -0.0001

ASN 220 THR 221 -0.0141

THR 221 GLU 222 -0.0000

GLU 222 ASP 223 0.0168

ASP 223 TYR 224 0.0002

TYR 224 LEU 225 0.0456

LEU 225 PHE 226 0.0001

PHE 226 GLN 227 0.0277

GLN 227 VAL 228 0.0002

VAL 228 ILE 229 -0.0410

ILE 229 LEU 230 -0.0001

LEU 230 GLU 231 -0.0226

GLU 231 LYS 232 -0.0001

LYS 232 GLN 233 -0.0173

GLN 233 ILE 234 -0.0000

ILE 234 ARG 235 -0.0182

ARG 235 ILE 236 -0.0000

ILE 236 PRO 237 0.0064

PRO 237 ARG 238 0.0001

ARG 238 SER 239 -0.0011

SER 239 LEU 240 -0.0003

LEU 240 SER 241 0.0054

SER 241 VAL 242 -0.0002

VAL 242 LYS 243 0.0172

LYS 243 ALA 244 -0.0002

ALA 244 ALA 245 -0.0110

ALA 245 SER 246 0.0001

SER 246 VAL 247 0.0072

VAL 247 LEU 248 -0.0003

LEU 248 LYS 249 0.0043

LYS 249 SER 250 0.0004

SER 250 PHE 251 -0.0066

PHE 251 LEU 252 -0.0001

LEU 252 ASN 253 0.0253

ASN 253 LYS 254 0.0003

LYS 254 ASP 255 -0.0129

ASP 255 PRO 256 -0.0000

PRO 256 LYS 257 0.0022

LYS 257 GLU 258 0.0001

GLU 258 ARG 259 -0.0057

ARG 259 LEU 260 -0.0002

LEU 260 GLY 261 0.0150

GLY 261 CYS 262 -0.0000

CYS 262 HIS 263 0.0125

HIS 263 PRO 264 0.0000

PRO 264 GLN 265 0.0208

GLN 265 THR 266 0.0001

THR 266 GLY 267 0.0082

GLY 267 PHE 268 0.0001

PHE 268 ALA 269 0.0156

ALA 269 ASP 270 0.0002

ASP 270 ILE 271 0.0109

ILE 271 GLN 272 0.0002

GLN 272 GLY 273 0.0070

GLY 273 HIS 274 -0.0004

HIS 274 PRO 275 0.0084

PRO 275 PHE 276 -0.0001

PHE 276 PHE 277 0.0117

PHE 277 ARG 278 -0.0002

ARG 278 ASN 279 -0.0094

ASN 279 VAL 280 0.0003

VAL 280 ASP 281 0.0431

ASP 281 TRP 282 0.0003

TRP 282 ASP 283 -0.0151

ASP 283 MET 284 -0.0003

MET 284 MET 285 0.0287

MET 285 GLU 286 0.0003

GLU 286 GLN 287 -0.0003

GLN 287 LYS 288 -0.0001

LYS 288 GLN 289 0.0192

GLN 289 VAL 290 -0.0002

VAL 290 VAL 291 -0.0758

VAL 291 PRO 292 -0.0001

PRO 292 PRO 293 0.0310

PRO 293 PHE 294 0.0001

PHE 294 LYS 295 -0.0937

LYS 295 PRO 296 -0.0005

PRO 296 ASN 297 -0.0048

ASN 297 ILE 298 0.0000

ILE 298 SER 299 -0.0825

SER 299 GLY 300 0.0001

GLY 300 GLU 301 0.0100

GLU 301 PHE 302 -0.0004

PHE 302 GLY 303 0.0593

GLY 303 LEU 304 -0.0000

LEU 304 ASP 305 0.0204

ASP 305 ASN 306 -0.0000

ASN 306 PHE 307 -0.1213

PHE 307 ASP 308 -0.0003

ASP 308 SER 309 0.0237

SER 309 GLN 310 0.0000

GLN 310 PHE 311 0.0106

PHE 311 THR 312 -0.0002

THR 312 ASN 313 -0.0082

ASN 313 GLU 314 -0.0002

GLU 314 PRO 315 -0.0205

PRO 315 VAL 316 -0.0000

VAL 316 GLN 317 -0.0272

GLN 317 LEU 318 -0.0001

LEU 318 GLU 319 -0.0000

GLU 319 PRO 320 -0.0000

PRO 320 ASP 321 -0.0186

ASP 321 ASP 322 0.0001

ASP 322 ASP 323 -0.0283

ASP 323 ASP 324 0.0003

ASP 324 ILE 325 -0.0067

ILE 325 VAL 326 0.0001

VAL 326 ARG 327 -0.0014

ARG 327 LYS 328 0.0001

LYS 328 ILE 329 0.0118

ILE 329 ASP 330 -0.0001

ASP 330 GLN 331 0.0164

GLN 331 SER 332 0.0001

SER 332 GLU 333 -0.0273

GLU 333 PHE 334 -0.0002

PHE 334 GLU 335 -0.0250

GLU 335 GLY 336 -0.0002

GLY 336 PHE 337 -0.0090

PHE 337 GLU 338 0.0004

GLU 338 TYR 339 0.0868

TYR 339 ILE 340 0.0000

ILE 340 ASN 341 0.0356

ASN 341 PRO 342 0.0000

PRO 342 LEU 343 -0.0194

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 25th, 2023.

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

*** zxy ***

CA strain for 2404230438531985751

--- normal mode 8 ---

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

* zxy *