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

* zxy *

CA strain for 2404230453311989143

--- 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 -0.0001

ASP 2 PRO 3 0.0094

PRO 3 LEU 4 0.0000

LEU 4 GLY 5 -0.0342

GLY 5 LEU 6 -0.0001

LEU 6 GLN 7 0.0151

GLN 7 ASP 8 0.0000

ASP 8 PHE 9 -0.0084

PHE 9 ASP 10 -0.0001

ASP 10 LEU 11 -0.0082

LEU 11 LEU 12 -0.0001

LEU 12 ARG 13 -0.0116

ARG 13 VAL 14 -0.0001

VAL 14 ILE 15 -0.0184

ILE 15 GLY 16 -0.0002

GLY 16 ARG 17 -0.0971

ARG 17 GLY 18 -0.0002

GLY 18 SER 19 -0.1458

SER 19 TYR 20 -0.0001

TYR 20 ALA 21 0.0017

ALA 21 LYS 22 -0.0000

LYS 22 VAL 23 -0.0542

VAL 23 LEU 24 -0.0004

LEU 24 LEU 25 -0.0250

LEU 25 VAL 26 -0.0000

VAL 26 ARG 27 0.0066

ARG 27 LEU 28 0.0002

LEU 28 LYS 29 -0.0150

LYS 29 LYS 30 0.0000

LYS 30 THR 31 0.0131

THR 31 ASP 32 -0.0000

ASP 32 ARG 33 0.0114

ARG 33 ILE 34 0.0000

ILE 34 TYR 35 -0.0233

TYR 35 ALA 36 0.0000

ALA 36 MET 37 -0.0246

MET 37 LYS 38 0.0001

LYS 38 VAL 39 -0.0202

VAL 39 VAL 40 0.0002

VAL 40 LYS 41 -0.0253

LYS 41 LYS 42 -0.0000

LYS 42 GLU 43 -0.0034

GLU 43 LEU 44 0.0001

LEU 44 VAL 45 0.0158

VAL 45 ASN 46 0.0001

ASN 46 ASP 47 0.0078

ASP 47 ASP 48 -0.0001

ASP 48 GLU 49 0.0135

GLU 49 ASP 50 0.0002

ASP 50 ILE 51 0.0033

ILE 51 ASP 52 -0.0002

ASP 52 TRP 53 -0.0354

TRP 53 VAL 54 -0.0002

VAL 54 GLN 55 0.0619

GLN 55 THR 56 -0.0001

THR 56 GLU 57 0.0482

GLU 57 LYS 58 -0.0001

LYS 58 HSD 59 -0.0180

HSD 59 VAL 60 0.0003

VAL 60 PHE 61 -0.0281

PHE 61 GLU 62 0.0002

GLU 62 GLN 63 -0.0663

GLN 63 ALA 64 0.0000

ALA 64 SER 65 -0.0696

SER 65 ASN 66 -0.0001

ASN 66 HSD 67 0.0246

HSD 67 PRO 68 0.0000

PRO 68 PHE 69 0.0237

PHE 69 LEU 70 0.0004

LEU 70 VAL 71 -0.0268

VAL 71 GLY 72 0.0000

GLY 72 LEU 73 0.0455

LEU 73 HSD 74 -0.0000

HSD 74 SER 75 0.0254

SER 75 CYS 76 -0.0002

CYS 76 PHE 77 0.0132

PHE 77 GLN 78 -0.0003

GLN 78 THR 79 0.0145

THR 79 GLU 80 -0.0001

GLU 80 SER 81 -0.0248

SER 81 ARG 82 -0.0000

ARG 82 LEU 83 0.0129

LEU 83 PHE 84 0.0001

PHE 84 PHE 85 0.0112

PHE 85 VAL 86 -0.0001

VAL 86 ILE 87 0.0159

ILE 87 GLU 88 0.0002

GLU 88 TYR 89 -0.0029

TYR 89 VAL 90 0.0001

VAL 90 ASN 91 0.0359

ASN 91 GLY 92 0.0000

GLY 92 GLY 93 0.1337

GLY 93 ASP 94 0.0004

ASP 94 LEU 95 0.0775

LEU 95 MET 96 0.0000

MET 96 PHE 97 0.0379

PHE 97 HSD 98 -0.0002

HSD 98 MET 99 0.0524

MET 99 GLN 100 -0.0000

GLN 100 ARG 101 -0.0169

ARG 101 GLN 102 -0.0001

GLN 102 ARG 103 0.0419

ARG 103 LYS 104 -0.0001

LYS 104 LEU 105 0.0120

LEU 105 PRO 106 0.0001

PRO 106 GLU 107 -0.0008

GLU 107 GLU 108 0.0000

GLU 108 HSD 109 -0.0164

HSD 109 ALA 110 0.0000

ALA 110 ARG 111 0.0109

ARG 111 PHE 112 0.0001

PHE 112 TYR 113 0.0024

TYR 113 SER 114 -0.0002

SER 114 ALA 115 0.0041

ALA 115 GLU 116 -0.0001

GLU 116 ILE 117 0.0040

ILE 117 SER 118 -0.0001

SER 118 LEU 119 -0.0017

LEU 119 ALA 120 -0.0001

ALA 120 LEU 121 -0.0094

LEU 121 ASN 122 -0.0001

ASN 122 TYR 123 0.0018

TYR 123 LEU 124 0.0000

LEU 124 HSD 125 -0.0363

HSD 125 GLU 126 -0.0000

GLU 126 ARG 127 0.0363

ARG 127 GLY 128 -0.0002

GLY 128 ILE 129 -0.0192

ILE 129 ILE 130 -0.0002

ILE 130 TYR 131 0.0083

TYR 131 ARG 132 -0.0001

ARG 132 ASP 133 0.0222

ASP 133 LEU 134 -0.0004

LEU 134 LYS 135 -0.0108

LYS 135 LEU 136 -0.0001

LEU 136 ASP 137 -0.0007

ASP 137 ASN 138 0.0001

ASN 138 VAL 139 0.0141

VAL 139 LEU 140 -0.0001

LEU 140 LEU 141 0.0098

LEU 141 ASP 142 -0.0002

ASP 142 SER 143 0.0158

SER 143 GLU 144 -0.0003

GLU 144 GLY 145 0.0139

GLY 145 HSD 146 -0.0000

HSD 146 ILE 147 0.0091

ILE 147 LYS 148 0.0001

LYS 148 LEU 149 0.0017

LEU 149 THR 150 0.0002

THR 150 ASP 151 -0.0207

ASP 151 TYR 152 0.0001

TYR 152 GLY 153 -0.0038

GLY 153 MET 154 0.0002

MET 154 CYS 155 0.0223

CYS 155 LYS 156 -0.0004

LYS 156 GLU 157 -0.0626

GLU 157 GLY 158 0.0002

GLY 158 LEU 159 0.0524

LEU 159 ARG 160 0.0004

ARG 160 PRO 161 0.0093

PRO 161 GLY 162 0.0000

GLY 162 ASP 163 0.0186

ASP 163 THR 164 -0.0001

THR 164 THR 165 0.0140

THR 165 SER 166 -0.0000

SER 166 GLU 167 0.0077

GLU 167 PHE 168 0.0002

PHE 168 CYS 169 0.0407

CYS 169 GLY 170 0.0004

GLY 170 THR 171 -0.0114

THR 171 PRO 172 0.0004

PRO 172 ASN 173 -0.0175

ASN 173 TYR 174 -0.0001

TYR 174 ILE 175 0.0317

ILE 175 ALA 176 0.0005

ALA 176 PRO 177 0.0090

PRO 177 GLU 178 0.0003

GLU 178 ILE 179 0.0132

ILE 179 LEU 180 0.0004

LEU 180 ARG 181 0.0073

ARG 181 GLY 182 -0.0002

GLY 182 GLU 183 -0.0160

GLU 183 ASP 184 0.0001

ASP 184 TYR 185 -0.0079

TYR 185 GLY 186 -0.0003

GLY 186 PHE 187 -0.0230

PHE 187 SER 188 -0.0001

SER 188 VAL 189 0.0082

VAL 189 ASP 190 -0.0001

ASP 190 TRP 191 0.0061

TRP 191 TRP 192 0.0001

TRP 192 ALA 193 0.0375

ALA 193 LEU 194 -0.0000

LEU 194 GLY 195 -0.0086

GLY 195 VAL 196 -0.0005

VAL 196 LEU 197 0.0430

LEU 197 MET 198 -0.0002

MET 198 PHE 199 0.0072

PHE 199 GLU 200 -0.0001

GLU 200 MET 201 0.0440

MET 201 MET 202 0.0000

MET 202 ALA 203 0.0248

ALA 203 GLY 204 -0.0000

GLY 204 ARG 205 0.0777

ARG 205 SER 206 0.0000

SER 206 PRO 207 0.0304

PRO 207 PHE 208 -0.0003

PHE 208 ASP 209 -0.0291

ASP 209 ILE 210 -0.0000

ILE 210 VAL 211 -0.0113

VAL 211 GLY 212 -0.0002

GLY 212 SER 213 0.0402

SER 213 SER 214 -0.0002

SER 214 ASP 215 -0.0183

ASP 215 ASN 216 0.0002

ASN 216 PRO 217 0.0043

PRO 217 ASP 218 0.0001

ASP 218 GLN 219 -0.0069

GLN 219 ASN 220 -0.0000

ASN 220 THR 221 -0.0116

THR 221 GLU 222 0.0003

GLU 222 ASP 223 0.0191

ASP 223 TYR 224 0.0001

TYR 224 LEU 225 0.0305

LEU 225 PHE 226 0.0001

PHE 226 GLN 227 0.0241

GLN 227 VAL 228 0.0000

VAL 228 ILE 229 -0.0349

ILE 229 LEU 230 0.0001

LEU 230 GLU 231 -0.0083

GLU 231 LYS 232 -0.0002

LYS 232 GLN 233 -0.0161

GLN 233 ILE 234 0.0004

ILE 234 ARG 235 -0.0054

ARG 235 ILE 236 0.0001

ILE 236 PRO 237 0.0072

PRO 237 ARG 238 0.0003

ARG 238 SER 239 -0.0011

SER 239 LEU 240 0.0003

LEU 240 SER 241 0.0083

SER 241 VAL 242 -0.0003

VAL 242 LYS 243 0.0068

LYS 243 ALA 244 0.0002

ALA 244 ALA 245 -0.0157

ALA 245 SER 246 -0.0000

SER 246 VAL 247 0.0037

VAL 247 LEU 248 -0.0003

LEU 248 LYS 249 0.0055

LYS 249 SER 250 -0.0002

SER 250 PHE 251 -0.0017

PHE 251 LEU 252 -0.0000

LEU 252 ASN 253 0.0217

ASN 253 LYS 254 -0.0004

LYS 254 ASP 255 -0.0047

ASP 255 PRO 256 0.0002

PRO 256 LYS 257 0.0031

LYS 257 GLU 258 0.0002

GLU 258 ARG 259 -0.0051

ARG 259 LEU 260 -0.0001

LEU 260 GLY 261 0.0066

GLY 261 CYS 262 -0.0002

CYS 262 HSD 263 0.0112

HSD 263 PRO 264 0.0001

PRO 264 GLN 265 0.0134

GLN 265 THR 266 0.0001

THR 266 GLY 267 0.0100

GLY 267 PHE 268 0.0002

PHE 268 ALA 269 0.0175

ALA 269 ASP 270 -0.0002

ASP 270 ILE 271 0.0043

ILE 271 GLN 272 0.0002

GLN 272 GLY 273 0.0059

GLY 273 HSD 274 -0.0001

HSD 274 PRO 275 0.0121

PRO 275 PHE 276 -0.0001

PHE 276 PHE 277 0.0039

PHE 277 ARG 278 0.0001

ARG 278 ASN 279 -0.0129

ASN 279 VAL 280 0.0000

VAL 280 ASP 281 0.0234

ASP 281 TRP 282 0.0002

TRP 282 ASP 283 -0.0149

ASP 283 MET 284 0.0000

MET 284 MET 285 0.0195

MET 285 GLU 286 -0.0000

GLU 286 GLN 287 -0.0031

GLN 287 LYS 288 -0.0003

LYS 288 GLN 289 0.0122

GLN 289 VAL 290 0.0001

VAL 290 VAL 291 -0.0525

VAL 291 PRO 292 -0.0004

PRO 292 PRO 293 0.0258

PRO 293 PHE 294 -0.0000

PHE 294 LYS 295 -0.0796

LYS 295 PRO 296 0.0001

PRO 296 ASN 297 -0.0137

ASN 297 ILE 298 0.0003

ILE 298 SER 299 -0.0700

SER 299 GLY 300 0.0001

GLY 300 GLU 301 0.0288

GLU 301 PHE 302 0.0002

PHE 302 GLY 303 0.0550

GLY 303 LEU 304 -0.0000

LEU 304 ASP 305 0.0282

ASP 305 ASN 306 -0.0002

ASN 306 PHE 307 -0.1285

PHE 307 ASP 308 -0.0002

ASP 308 SER 309 0.0224

SER 309 GLN 310 -0.0002

GLN 310 PHE 311 0.0082

PHE 311 THR 312 0.0004

THR 312 ASN 313 -0.0063

ASN 313 GLU 314 -0.0002

GLU 314 PRO 315 -0.0248

PRO 315 VAL 316 -0.0003

VAL 316 GLN 317 -0.0285

GLN 317 LEU 318 0.0000

LEU 318 GLU 319 -0.0024

GLU 319 PRO 320 0.0001

PRO 320 ASP 321 -0.0375

ASP 321 ASP 322 0.0000

ASP 322 ASP 323 -0.0280

ASP 323 ASP 324 -0.0001

ASP 324 ILE 325 -0.0001

ILE 325 VAL 326 -0.0001

VAL 326 ARG 327 -0.0009

ARG 327 LYS 328 -0.0004

LYS 328 ILE 329 0.0268

ILE 329 ASP 330 -0.0002

ASP 330 GLN 331 0.0180

GLN 331 SER 332 0.0000

SER 332 GLU 333 -0.0207

GLU 333 PHE 334 -0.0001

PHE 334 GLU 335 -0.0187

GLU 335 GLY 336 -0.0001

GLY 336 PHE 337 -0.0009

PHE 337 GLU 338 -0.0003

GLU 338 TYR 339 0.0614

TYR 339 ILE 340 0.0002

ILE 340 ASN 341 0.0162

ASN 341 PRO 342 -0.0001

PRO 342 LEU 343 -0.0219

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 2404230453311989143

--- normal mode 8 ---

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

* zxy *