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

* *

CA strain for 2404232236172138714

--- 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 19 VAL 20 0.0002

VAL 20 ASP 21 0.0210

ASP 21 GLN 22 0.0002

GLN 22 ALA 23 -0.0066

ALA 23 THR 24 0.0001

THR 24 LEU 25 0.0038

LEU 25 ASP 26 -0.0002

ASP 26 LYS 27 -0.0187

LYS 27 LEU 28 -0.0000

LEU 28 GLU 29 0.0427

GLU 29 ALA 30 -0.0002

ALA 30 GLY 31 -0.0167

GLY 31 PHE 32 0.0001

PHE 32 LYS 33 0.0193

LYS 33 LYS 34 0.0001

LYS 34 LEU 35 -0.0113

LEU 35 GLN 36 -0.0002

GLN 36 ASP 37 0.0132

ASP 37 ALA 38 -0.0001

ALA 38 LYS 39 0.0346

LYS 39 ASP 40 0.0001

ASP 40 CYS 41 -0.0424

CYS 41 LYS 42 0.0000

LYS 42 SER 43 -0.0681

SER 43 LEU 44 -0.0000

LEU 44 LEU 45 -0.0723

LEU 45 LYS 46 -0.0003

LYS 46 LYS 47 -0.0286

LYS 47 TYR 48 -0.0003

TYR 48 LEU 49 -0.0833

LEU 49 THR 50 -0.0001

THR 50 LYS 51 -0.0481

LYS 51 GLU 52 0.0004

GLU 52 ILE 53 -0.0001

ILE 53 PHE 54 0.0001

PHE 54 ASP 55 -0.0186

ASP 55 ARG 56 0.0001

ARG 56 LEU 57 0.0065

LEU 57 LYS 58 -0.0000

LYS 58 THR 59 -0.0064

THR 59 ARG 60 0.0002

ARG 60 LYS 61 0.0345

LYS 61 THR 62 -0.0003

THR 62 ALA 63 -0.0128

ALA 63 MET 64 -0.0003

MET 64 GLY 65 0.1023

GLY 65 ALA 66 -0.0002

ALA 66 THR 67 0.0947

THR 67 LEU 68 0.0000

LEU 68 LEU 69 -0.0220

LEU 69 ASP 70 0.0002

ASP 70 VAL 71 -0.0085

VAL 71 ILE 72 -0.0000

ILE 72 GLN 73 0.0234

GLN 73 SER 74 0.0003

SER 74 GLY 75 0.0267

GLY 75 VAL 76 -0.0003

VAL 76 GLU 77 -0.0459

GLU 77 ASN 78 0.0000

ASN 78 LEU 79 0.0422

LEU 79 ASP 80 -0.0001

ASP 80 SER 81 -0.0174

SER 81 GLY 82 0.0002

GLY 82 VAL 83 -0.0229

VAL 83 GLY 84 0.0002

GLY 84 VAL 85 0.0016

VAL 85 TYR 86 0.0005

TYR 86 ALA 87 -0.0054

ALA 87 PRO 88 0.0001

PRO 88 ASP 89 0.0165

ASP 89 ALA 90 -0.0002

ALA 90 GLU 91 0.1030

GLU 91 SER 92 0.0002

SER 92 TYR 93 0.0058

TYR 93 THR 94 0.0002

THR 94 VAL 95 0.0707

VAL 95 PHE 96 -0.0002

PHE 96 ALA 97 -0.0069

ALA 97 ASP 98 0.0001

ASP 98 LEU 99 0.0053

LEU 99 PHE 100 0.0001

PHE 100 ASN 101 0.0164

ASN 101 PRO 102 -0.0003

PRO 102 VAL 103 0.0140

VAL 103 ILE 104 0.0004

ILE 104 GLU 105 0.0215

GLU 105 ASP 106 -0.0001

ASP 106 TYR 107 -0.0398

TYR 107 HIS 108 -0.0001

HIS 108 GLY 109 0.0562

GLY 109 GLY 110 -0.0002

GLY 110 PHE 111 -0.0029

PHE 111 LYS 112 -0.0001

LYS 112 PRO 113 -0.0107

PRO 113 THR 114 -0.0004

THR 114 ASP 115 0.0292

ASP 115 LYS 116 -0.0004

LYS 116 HIS 117 0.0296

HIS 117 PRO 118 -0.0001

PRO 118 PRO 119 -0.0163

PRO 119 THR 120 -0.0002

THR 120 ASP 121 0.0798

ASP 121 PHE 122 0.0001

PHE 122 GLY 123 0.0216

GLY 123 ASP 124 0.0000

ASP 124 MET 125 -0.0078

MET 125 ASN 126 0.0001

ASN 126 THR 127 0.0200

THR 127 ILE 128 0.0002

ILE 128 VAL 129 0.0228

VAL 129 ASN 130 0.0004

ASN 130 VAL 131 0.0262

VAL 131 ASP 132 -0.0003

ASP 132 PRO 133 -0.0238

PRO 133 GLU 134 0.0003

GLU 134 ASN 135 -0.0120

ASN 135 LYS 136 0.0003

LYS 136 TYR 137 -0.0184

TYR 137 VAL 138 0.0001

VAL 138 VAL 139 0.0296

VAL 139 SER 140 0.0002

SER 140 THR 141 0.0043

THR 141 ARG 142 -0.0001

ARG 142 VAL 143 0.0275

VAL 143 ARG 144 0.0001

ARG 144 CYS 145 0.0291

CYS 145 GLY 146 -0.0002

GLY 146 ARG 147 -0.0242

ARG 147 SER 148 -0.0001

SER 148 LEU 149 -0.0025

LEU 149 GLN 150 0.0003

GLN 150 GLY 151 0.0070

GLY 151 TYR 152 -0.0002

TYR 152 PRO 153 0.0900

PRO 153 PHE 154 -0.0002

PHE 154 ASN 155 0.0144

ASN 155 PRO 156 -0.0002

PRO 156 CYS 157 -0.0102

CYS 157 LEU 158 -0.0003

LEU 158 THR 159 0.0083

THR 159 GLU 160 0.0004

GLU 160 ALA 161 0.0116

ALA 161 GLN 162 0.0000

GLN 162 TYR 163 0.0069

TYR 163 LYS 164 0.0001

LYS 164 GLU 165 -0.0204

GLU 165 MET 166 -0.0000

MET 166 GLU 167 0.0217

GLU 167 ASP 168 0.0005

ASP 168 LYS 169 -0.0235

LYS 169 VAL 170 -0.0000

VAL 170 SER 171 0.0011

SER 171 SER 172 0.0002

SER 172 GLN 173 -0.0147

GLN 173 LEU 174 -0.0004

LEU 174 LYS 175 -0.0043

LYS 175 GLY 176 -0.0004

GLY 176 MET 177 0.0063

MET 177 THR 178 0.0001

THR 178 GLY 179 0.0388

GLY 179 ASP 180 0.0003

ASP 180 LEU 181 0.0091

LEU 181 LYS 182 0.0002

LYS 182 GLY 183 -0.0200

GLY 183 THR 184 0.0001

THR 184 TYR 185 0.0165

TYR 185 TYR 186 0.0001

TYR 186 PRO 187 0.0098

PRO 187 LEU 188 0.0001

LEU 188 THR 189 -0.0002

THR 189 GLY 190 0.0001

GLY 190 MET 191 0.0207

MET 191 ASP 192 0.0001

ASP 192 LYS 193 0.0008

LYS 193 LYS 194 0.0005

LYS 194 THR 195 -0.0100

THR 195 GLN 196 0.0002

GLN 196 GLN 197 0.0042

GLN 197 GLN 198 0.0001

GLN 198 LEU 199 -0.0045

LEU 199 ILE 200 -0.0000

ILE 200 ASP 201 -0.0029

ASP 201 ASP 202 0.0002

ASP 202 HIS 203 0.0209

HIS 203 PHE 204 -0.0000

PHE 204 LEU 205 -0.0045

LEU 205 PHE 206 -0.0003

PHE 206 LYS 207 -0.0146

LYS 207 GLU 208 0.0001

GLU 208 GLY 209 -0.0146

GLY 209 ASP 210 -0.0003

ASP 210 ARG 211 -0.0201

ARG 211 PHE 212 -0.0001

PHE 212 LEU 213 -0.0076

LEU 213 GLN 214 0.0002

GLN 214 ALA 215 0.0134

ALA 215 ALA 216 -0.0000

ALA 216 ASN 217 0.0601

ASN 217 ALA 218 -0.0001

ALA 218 CYS 219 0.0156

CYS 219 ARG 220 0.0001

ARG 220 TYR 221 0.0374

TYR 221 TRP 222 0.0000

TRP 222 PRO 223 0.0229

PRO 223 THR 224 0.0000

THR 224 GLY 225 -0.0038

GLY 225 ARG 226 0.0001

ARG 226 GLY 227 0.0315

GLY 227 ILE 228 -0.0002

ILE 228 TYR 229 -0.0064

TYR 229 HIS 230 0.0003

HIS 230 ASN 231 -0.0009

ASN 231 ASP 232 -0.0000

ASP 232 ALA 233 0.0266

ALA 233 LYS 234 -0.0001

LYS 234 THR 235 -0.0087

THR 235 PHE 236 0.0003

PHE 236 LEU 237 0.0071

LEU 237 VAL 238 -0.0002

VAL 238 TRP 239 0.0050

TRP 239 VAL 240 -0.0005

VAL 240 ASN 241 0.0204

ASN 241 GLU 242 0.0001

GLU 242 GLU 243 0.0080

GLU 243 ASP 244 0.0002

ASP 244 HIS 245 -0.0329

HIS 245 LEU 246 0.0001

LEU 246 ARG 247 0.0012

ARG 247 ILE 248 -0.0002

ILE 248 ILE 249 0.0417

ILE 249 SER 250 -0.0001

SER 250 MET 251 0.0364

MET 251 GLN 252 -0.0000

GLN 252 GLN 253 0.0652

GLN 253 GLY 254 -0.0000

GLY 254 GLY 255 -0.0042

GLY 255 ASP 256 -0.0000

ASP 256 LEU 257 -0.0094

LEU 257 LYS 258 -0.0003

LYS 258 GLN 259 0.0034

GLN 259 VAL 260 0.0001

VAL 260 TYR 261 0.0051

TYR 261 SER 262 -0.0001

SER 262 ARG 263 -0.0177

ARG 263 MET 264 -0.0002

MET 264 VAL 265 -0.0098

VAL 265 SER 266 -0.0003

SER 266 GLY 267 -0.0013

GLY 267 VAL 268 -0.0002

VAL 268 LYS 269 -0.0073

LYS 269 GLU 270 -0.0001

GLU 270 ILE 271 0.0153

ILE 271 GLU 272 0.0003

GLU 272 LYS 273 -0.0126

LYS 273 LYS 274 0.0002

LYS 274 LEU 275 0.0312

LEU 275 PRO 276 -0.0002

PRO 276 PHE 277 -0.0198

PHE 277 SER 278 -0.0003

SER 278 ARG 279 -0.0420

ARG 279 ASP 280 0.0002

ASP 280 ASP 281 -0.0274

ASP 281 ARG 282 -0.0001

ARG 282 LEU 283 -0.0076

LEU 283 GLY 284 0.0001

GLY 284 PHE 285 -0.0169

PHE 285 LEU 286 0.0001

LEU 286 THR 287 -0.0023

THR 287 PHE 288 -0.0006

PHE 288 CYS 289 -0.0208

CYS 289 PRO 290 -0.0002

PRO 290 THR 291 -0.0605

THR 291 ASN 292 -0.0004

ASN 292 LEU 293 -0.0250

LEU 293 GLY 294 -0.0002

GLY 294 THR 295 0.0426

THR 295 THR 296 -0.0000

THR 296 ILE 297 0.0092

ILE 297 ARG 298 0.0000

ARG 298 ALA 299 -0.0019

ALA 299 SER 300 0.0002

SER 300 VAL 301 0.0045

VAL 301 HIS 302 0.0002

HIS 302 ILE 303 0.0189

ILE 303 LYS 304 -0.0001

LYS 304 LEU 305 0.0267

LEU 305 PRO 306 -0.0001

PRO 306 LYS 307 0.0032

LYS 307 LEU 308 0.0000

LEU 308 ALA 309 -0.0235

ALA 309 ALA 310 0.0003

ALA 310 ASP 311 0.0034

ASP 311 LYS 312 -0.0003

LYS 312 ALA 313 0.0165

ALA 313 LYS 314 -0.0004

LYS 314 LEU 315 0.0004

LEU 315 ASP 316 -0.0001

ASP 316 SER 317 0.0158

SER 317 ILE 318 -0.0002

ILE 318 ALA 319 -0.0357

ALA 319 ALA 320 0.0002

ALA 320 LYS 321 -0.0281

LYS 321 TYR 322 0.0001

TYR 322 ASN 323 -0.1354

ASN 323 LEU 324 -0.0002

LEU 324 GLN 325 0.0408

GLN 325 VAL 326 0.0001

VAL 326 ARG 327 0.0040

ARG 327 GLY 328 0.0002

GLY 328 THR 329 0.0212

THR 329 ARG 330 0.0000

ARG 330 GLY 331 0.0067

GLY 331 GLU 332 0.0002

GLU 332 HIS 333 -0.0662

HIS 333 THR 334 -0.0003

THR 334 GLU 335 -0.1719

GLU 335 SER 336 -0.0000

SER 336 GLU 337 0.0236

GLU 337 GLY 338 0.0000

GLY 338 GLY 339 0.0010

GLY 339 VAL 340 0.0001

VAL 340 TYR 341 0.0071

TYR 341 ASP 342 -0.0002

ASP 342 ILE 343 0.0284

ILE 343 SER 344 0.0002

SER 344 ASN 345 -0.0215

ASN 345 LYS 346 -0.0002

LYS 346 ARG 347 0.0141

ARG 347 ARG 348 0.0001

ARG 348 MET 349 0.0255

MET 349 GLY 350 0.0002

GLY 350 LEU 351 -0.0178

LEU 351 THR 352 0.0002

THR 352 GLU 353 -0.0018

GLU 353 TYR 354 0.0001

TYR 354 GLN 355 -0.0422

GLN 355 ALA 356 -0.0002

ALA 356 VAL 357 -0.0211

VAL 357 ARG 358 0.0001

ARG 358 GLU 359 -0.0239

GLU 359 MET 360 -0.0002

MET 360 GLN 361 -0.0602

GLN 361 ASP 362 0.0000

ASP 362 GLY 363 0.0412

GLY 363 ILE 364 -0.0001

ILE 364 GLN 365 -0.0315

GLN 365 GLU 366 -0.0003

GLU 366 LEU 367 0.0117

LEU 367 ILE 368 -0.0000

ILE 368 LYS 369 0.0017

LYS 369 LEU 370 -0.0004

LEU 370 GLU 371 -0.0064

GLU 371 GLN 372 0.0003

GLN 372 ALA 373 0.0265

ALA 373 ALA 374 0.0003

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.

*** ***

CA strain for 2404232236172138714

--- normal mode 7 ---

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

* *