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

* zxy *

CA strain for 2404230453311989143

--- normal mode 10 ---

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 0.0243

PRO 3 LEU 4 0.0001

LEU 4 GLY 5 -0.0639

GLY 5 LEU 6 0.0001

LEU 6 GLN 7 0.0193

GLN 7 ASP 8 0.0004

ASP 8 PHE 9 0.0006

PHE 9 ASP 10 0.0001

ASP 10 LEU 11 -0.0204

LEU 11 LEU 12 0.0002

LEU 12 ARG 13 -0.0563

ARG 13 VAL 14 0.0001

VAL 14 ILE 15 0.0515

ILE 15 GLY 16 -0.0002

GLY 16 ARG 17 -0.1120

ARG 17 GLY 18 -0.0005

GLY 18 SER 19 -0.2160

SER 19 TYR 20 0.0003

TYR 20 ALA 21 -0.0229

ALA 21 LYS 22 0.0001

LYS 22 VAL 23 -0.0404

VAL 23 LEU 24 0.0003

LEU 24 LEU 25 -0.0236

LEU 25 VAL 26 -0.0003

VAL 26 ARG 27 -0.0076

ARG 27 LEU 28 -0.0003

LEU 28 LYS 29 -0.0320

LYS 29 LYS 30 0.0001

LYS 30 THR 31 0.0080

THR 31 ASP 32 -0.0004

ASP 32 ARG 33 0.0133

ARG 33 ILE 34 -0.0001

ILE 34 TYR 35 -0.0503

TYR 35 ALA 36 0.0001

ALA 36 MET 37 0.0207

MET 37 LYS 38 0.0001

LYS 38 VAL 39 0.0339

VAL 39 VAL 40 -0.0002

VAL 40 LYS 41 0.0076

LYS 41 LYS 42 0.0001

LYS 42 GLU 43 0.0070

GLU 43 LEU 44 -0.0001

LEU 44 VAL 45 -0.0009

VAL 45 ASN 46 -0.0001

ASN 46 ASP 47 0.0158

ASP 47 ASP 48 0.0001

ASP 48 GLU 49 0.0011

GLU 49 ASP 50 0.0001

ASP 50 ILE 51 0.0099

ILE 51 ASP 52 -0.0000

ASP 52 TRP 53 -0.0424

TRP 53 VAL 54 -0.0002

VAL 54 GLN 55 -0.0003

GLN 55 THR 56 -0.0001

THR 56 GLU 57 -0.0098

GLU 57 LYS 58 0.0003

LYS 58 HSD 59 -0.1138

HSD 59 VAL 60 -0.0004

VAL 60 PHE 61 -0.0656

PHE 61 GLU 62 -0.0000

GLU 62 GLN 63 -0.1899

GLN 63 ALA 64 -0.0002

ALA 64 SER 65 -0.0644

SER 65 ASN 66 -0.0001

ASN 66 HSD 67 -0.0922

HSD 67 PRO 68 0.0002

PRO 68 PHE 69 -0.0190

PHE 69 LEU 70 0.0001

LEU 70 VAL 71 -0.0320

VAL 71 GLY 72 0.0002

GLY 72 LEU 73 0.0020

LEU 73 HSD 74 0.0000

HSD 74 SER 75 0.0055

SER 75 CYS 76 0.0000

CYS 76 PHE 77 -0.0500

PHE 77 GLN 78 -0.0001

GLN 78 THR 79 -0.0361

THR 79 GLU 80 -0.0003

GLU 80 SER 81 -0.0122

SER 81 ARG 82 0.0002

ARG 82 LEU 83 -0.0306

LEU 83 PHE 84 -0.0000

PHE 84 PHE 85 -0.0091

PHE 85 VAL 86 0.0004

VAL 86 ILE 87 0.0354

ILE 87 GLU 88 0.0003

GLU 88 TYR 89 -0.0191

TYR 89 VAL 90 -0.0000

VAL 90 ASN 91 -0.0041

ASN 91 GLY 92 -0.0001

GLY 92 GLY 93 0.0122

GLY 93 ASP 94 -0.0002

ASP 94 LEU 95 0.1582

LEU 95 MET 96 0.0004

MET 96 PHE 97 0.0041

PHE 97 HSD 98 -0.0001

HSD 98 MET 99 0.0401

MET 99 GLN 100 -0.0002

GLN 100 ARG 101 -0.0619

ARG 101 GLN 102 -0.0001

GLN 102 ARG 103 -0.0159

ARG 103 LYS 104 -0.0002

LYS 104 LEU 105 -0.0599

LEU 105 PRO 106 -0.0002

PRO 106 GLU 107 0.0494

GLU 107 GLU 108 0.0002

GLU 108 HSD 109 0.0479

HSD 109 ALA 110 -0.0001

ALA 110 ARG 111 -0.0211

ARG 111 PHE 112 0.0003

PHE 112 TYR 113 0.0019

TYR 113 SER 114 -0.0002

SER 114 ALA 115 -0.0151

ALA 115 GLU 116 -0.0002

GLU 116 ILE 117 -0.0121

ILE 117 SER 118 -0.0001

SER 118 LEU 119 -0.0077

LEU 119 ALA 120 0.0003

ALA 120 LEU 121 0.0090

LEU 121 ASN 122 0.0001

ASN 122 TYR 123 -0.1000

TYR 123 LEU 124 0.0001

LEU 124 HSD 125 -0.0086

HSD 125 GLU 126 -0.0001

GLU 126 ARG 127 -0.0674

ARG 127 GLY 128 -0.0001

GLY 128 ILE 129 0.0212

ILE 129 ILE 130 0.0002

ILE 130 TYR 131 0.0459

TYR 131 ARG 132 -0.0000

ARG 132 ASP 133 0.0169

ASP 133 LEU 134 -0.0001

LEU 134 LYS 135 -0.0028

LYS 135 LEU 136 -0.0003

LEU 136 ASP 137 0.0333

ASP 137 ASN 138 0.0002

ASN 138 VAL 139 -0.0602

VAL 139 LEU 140 0.0002

LEU 140 LEU 141 -0.0662

LEU 141 ASP 142 -0.0003

ASP 142 SER 143 -0.0470

SER 143 GLU 144 -0.0005

GLU 144 GLY 145 -0.0143

GLY 145 HSD 146 0.0001

HSD 146 ILE 147 -0.0420

ILE 147 LYS 148 -0.0000

LYS 148 LEU 149 -0.0313

LEU 149 THR 150 -0.0002

THR 150 ASP 151 -0.0297

ASP 151 TYR 152 -0.0000

TYR 152 GLY 153 -0.0546

GLY 153 MET 154 -0.0001

MET 154 CYS 155 0.0507

CYS 155 LYS 156 -0.0001

LYS 156 GLU 157 -0.0193

GLU 157 GLY 158 0.0001

GLY 158 LEU 159 -0.1456

LEU 159 ARG 160 -0.0002

ARG 160 PRO 161 -0.0357

PRO 161 GLY 162 -0.0000

GLY 162 ASP 163 -0.0371

ASP 163 THR 164 -0.0002

THR 164 THR 165 -0.0147

THR 165 SER 166 -0.0002

SER 166 GLU 167 -0.0039

GLU 167 PHE 168 -0.0003

PHE 168 CYS 169 -0.0132

CYS 169 GLY 170 -0.0000

GLY 170 THR 171 -0.0288

THR 171 PRO 172 -0.0001

PRO 172 ASN 173 0.0383

ASN 173 TYR 174 0.0000

TYR 174 ILE 175 0.0124

ILE 175 ALA 176 -0.0001

ALA 176 PRO 177 -0.0041

PRO 177 GLU 178 0.0001

GLU 178 ILE 179 -0.0284

ILE 179 LEU 180 -0.0000

LEU 180 ARG 181 -0.0084

ARG 181 GLY 182 0.0002

GLY 182 GLU 183 0.0338

GLU 183 ASP 184 -0.0001

ASP 184 TYR 185 0.0073

TYR 185 GLY 186 -0.0001

GLY 186 PHE 187 0.0408

PHE 187 SER 188 -0.0005

SER 188 VAL 189 -0.0133

VAL 189 ASP 190 -0.0002

ASP 190 TRP 191 -0.0457

TRP 191 TRP 192 0.0001

TRP 192 ALA 193 -0.0324

ALA 193 LEU 194 0.0004

LEU 194 GLY 195 -0.0047

GLY 195 VAL 196 0.0003

VAL 196 LEU 197 -0.0131

LEU 197 MET 198 0.0002

MET 198 PHE 199 -0.0325

PHE 199 GLU 200 -0.0002

GLU 200 MET 201 -0.0971

MET 201 MET 202 0.0002

MET 202 ALA 203 -0.0473

ALA 203 GLY 204 -0.0001

GLY 204 ARG 205 -0.1813

ARG 205 SER 206 0.0002

SER 206 PRO 207 -0.0637

PRO 207 PHE 208 -0.0005

PHE 208 ASP 209 0.0721

ASP 209 ILE 210 0.0001

ILE 210 VAL 211 0.0357

VAL 211 GLY 212 0.0000

GLY 212 SER 213 -0.0986

SER 213 SER 214 -0.0001

SER 214 ASP 215 0.0802

ASP 215 ASN 216 -0.0000

ASN 216 PRO 217 0.0001

PRO 217 ASP 218 -0.0002

ASP 218 GLN 219 -0.0040

GLN 219 ASN 220 0.0000

ASN 220 THR 221 0.0379

THR 221 GLU 222 0.0000

GLU 222 ASP 223 -0.0142

ASP 223 TYR 224 0.0000

TYR 224 LEU 225 -0.0978

LEU 225 PHE 226 0.0003

PHE 226 GLN 227 -0.0679

GLN 227 VAL 228 -0.0004

VAL 228 ILE 229 0.1287

ILE 229 LEU 230 -0.0002

LEU 230 GLU 231 0.0124

GLU 231 LYS 232 0.0005

LYS 232 GLN 233 0.0486

GLN 233 ILE 234 -0.0002

ILE 234 ARG 235 -0.0470

ARG 235 ILE 236 0.0001

ILE 236 PRO 237 -0.0536

PRO 237 ARG 238 0.0003

ARG 238 SER 239 0.0377

SER 239 LEU 240 -0.0001

LEU 240 SER 241 -0.0031

SER 241 VAL 242 -0.0002

VAL 242 LYS 243 -0.0256

LYS 243 ALA 244 0.0001

ALA 244 ALA 245 0.0467

ALA 245 SER 246 0.0002

SER 246 VAL 247 -0.0138

VAL 247 LEU 248 -0.0003

LEU 248 LYS 249 0.0160

LYS 249 SER 250 -0.0000

SER 250 PHE 251 -0.0052

PHE 251 LEU 252 -0.0002

LEU 252 ASN 253 -0.0059

ASN 253 LYS 254 -0.0001

LYS 254 ASP 255 0.0627

ASP 255 PRO 256 -0.0002

PRO 256 LYS 257 0.0117

LYS 257 GLU 258 0.0003

GLU 258 ARG 259 -0.0018

ARG 259 LEU 260 0.0002

LEU 260 GLY 261 -0.0222

GLY 261 CYS 262 0.0002

CYS 262 HSD 263 -0.0020

HSD 263 PRO 264 0.0001

PRO 264 GLN 265 -0.0063

GLN 265 THR 266 -0.0001

THR 266 GLY 267 -0.0374

GLY 267 PHE 268 -0.0003

PHE 268 ALA 269 -0.0334

ALA 269 ASP 270 -0.0002

ASP 270 ILE 271 0.0109

ILE 271 GLN 272 0.0001

GLN 272 GLY 273 -0.0193

GLY 273 HSD 274 -0.0002

HSD 274 PRO 275 -0.0252

PRO 275 PHE 276 -0.0002

PHE 276 PHE 277 -0.0230

PHE 277 ARG 278 0.0003

ARG 278 ASN 279 0.0202

ASN 279 VAL 280 0.0001

VAL 280 ASP 281 -0.0457

ASP 281 TRP 282 -0.0001

TRP 282 ASP 283 0.0121

ASP 283 MET 284 -0.0000

MET 284 MET 285 -0.0265

MET 285 GLU 286 0.0001

GLU 286 GLN 287 0.0185

GLN 287 LYS 288 -0.0001

LYS 288 GLN 289 0.0156

GLN 289 VAL 290 0.0001

VAL 290 VAL 291 0.0335

VAL 291 PRO 292 0.0001

PRO 292 PRO 293 -0.0363

PRO 293 PHE 294 0.0002

PHE 294 LYS 295 0.0885

LYS 295 PRO 296 0.0001

PRO 296 ASN 297 0.0616

ASN 297 ILE 298 0.0004

ILE 298 SER 299 -0.0105

SER 299 GLY 300 -0.0002

GLY 300 GLU 301 0.1019

GLU 301 PHE 302 -0.0000

PHE 302 GLY 303 0.0921

GLY 303 LEU 304 0.0000

LEU 304 ASP 305 0.0708

ASP 305 ASN 306 0.0002

ASN 306 PHE 307 0.0089

PHE 307 ASP 308 0.0002

ASP 308 SER 309 0.1052

SER 309 GLN 310 -0.0002

GLN 310 PHE 311 -0.0177

PHE 311 THR 312 -0.0002

THR 312 ASN 313 0.0419

ASN 313 GLU 314 -0.0001

GLU 314 PRO 315 -0.0238

PRO 315 VAL 316 -0.0002

VAL 316 GLN 317 0.0812

GLN 317 LEU 318 -0.0001

LEU 318 GLU 319 0.0038

GLU 319 PRO 320 0.0003

PRO 320 ASP 321 0.0589

ASP 321 ASP 322 0.0005

ASP 322 ASP 323 0.0452

ASP 323 ASP 324 -0.0001

ASP 324 ILE 325 -0.0202

ILE 325 VAL 326 0.0001

VAL 326 ARG 327 0.0475

ARG 327 LYS 328 0.0001

LYS 328 ILE 329 -0.0421

ILE 329 ASP 330 -0.0003

ASP 330 GLN 331 0.0221

GLN 331 SER 332 0.0004

SER 332 GLU 333 -0.0540

GLU 333 PHE 334 0.0001

PHE 334 GLU 335 0.0099

GLU 335 GLY 336 0.0002

GLY 336 PHE 337 -0.0031

PHE 337 GLU 338 0.0002

GLU 338 TYR 339 0.0108

TYR 339 ILE 340 -0.0002

ILE 340 ASN 341 -0.0253

ASN 341 PRO 342 -0.0002

PRO 342 LEU 343 -0.0086

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 10 ---

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

* zxy *