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

* *

CA strain for 2404232236172138714

--- 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
SER 19 VAL 20 -0.0002

VAL 20 ASP 21 0.0175

ASP 21 GLN 22 -0.0002

GLN 22 ALA 23 -0.0051

ALA 23 THR 24 -0.0001

THR 24 LEU 25 0.0036

LEU 25 ASP 26 0.0003

ASP 26 LYS 27 0.0007

LYS 27 LEU 28 0.0001

LEU 28 GLU 29 0.0163

GLU 29 ALA 30 -0.0000

ALA 30 GLY 31 0.0060

GLY 31 PHE 32 -0.0001

PHE 32 LYS 33 -0.0029

LYS 33 LYS 34 -0.0004

LYS 34 LEU 35 -0.0528

LEU 35 GLN 36 0.0000

GLN 36 ASP 37 -0.0324

ASP 37 ALA 38 -0.0002

ALA 38 LYS 39 0.1173

LYS 39 ASP 40 0.0000

ASP 40 CYS 41 -0.0391

CYS 41 LYS 42 0.0001

LYS 42 SER 43 -0.0965

SER 43 LEU 44 -0.0001

LEU 44 LEU 45 -0.0242

LEU 45 LYS 46 -0.0003

LYS 46 LYS 47 -0.1158

LYS 47 TYR 48 -0.0004

TYR 48 LEU 49 -0.0241

LEU 49 THR 50 0.0000

THR 50 LYS 51 -0.0006

LYS 51 GLU 52 -0.0000

GLU 52 ILE 53 -0.0217

ILE 53 PHE 54 0.0002

PHE 54 ASP 55 0.0165

ASP 55 ARG 56 -0.0001

ARG 56 LEU 57 -0.0136

LEU 57 LYS 58 -0.0002

LYS 58 THR 59 0.0049

THR 59 ARG 60 -0.0001

ARG 60 LYS 61 -0.0687

LYS 61 THR 62 0.0002

THR 62 ALA 63 -0.0610

ALA 63 MET 64 0.0001

MET 64 GLY 65 -0.0134

GLY 65 ALA 66 -0.0003

ALA 66 THR 67 -0.0090

THR 67 LEU 68 -0.0004

LEU 68 LEU 69 0.0006

LEU 69 ASP 70 -0.0001

ASP 70 VAL 71 -0.0001

VAL 71 ILE 72 0.0000

ILE 72 GLN 73 0.0337

GLN 73 SER 74 0.0001

SER 74 GLY 75 0.0536

GLY 75 VAL 76 -0.0000

VAL 76 GLU 77 0.0385

GLU 77 ASN 78 -0.0000

ASN 78 LEU 79 0.1618

LEU 79 ASP 80 -0.0002

ASP 80 SER 81 -0.0471

SER 81 GLY 82 0.0001

GLY 82 VAL 83 0.0003

VAL 83 GLY 84 -0.0001

GLY 84 VAL 85 0.0110

VAL 85 TYR 86 0.0000

TYR 86 ALA 87 -0.0273

ALA 87 PRO 88 0.0003

PRO 88 ASP 89 0.0258

ASP 89 ALA 90 -0.0004

ALA 90 GLU 91 -0.0599

GLU 91 SER 92 0.0002

SER 92 TYR 93 0.0501

TYR 93 THR 94 -0.0002

THR 94 VAL 95 0.0226

VAL 95 PHE 96 -0.0003

PHE 96 ALA 97 0.0690

ALA 97 ASP 98 0.0002

ASP 98 LEU 99 0.0365

LEU 99 PHE 100 -0.0002

PHE 100 ASN 101 0.0041

ASN 101 PRO 102 0.0002

PRO 102 VAL 103 0.0252

VAL 103 ILE 104 0.0003

ILE 104 GLU 105 -0.0124

GLU 105 ASP 106 0.0003

ASP 106 TYR 107 0.0786

TYR 107 HIS 108 -0.0000

HIS 108 GLY 109 0.0086

GLY 109 GLY 110 0.0001

GLY 110 PHE 111 0.0232

PHE 111 LYS 112 0.0004

LYS 112 PRO 113 0.0520

PRO 113 THR 114 0.0001

THR 114 ASP 115 -0.0310

ASP 115 LYS 116 0.0001

LYS 116 HIS 117 -0.0380

HIS 117 PRO 118 0.0004

PRO 118 PRO 119 -0.0739

PRO 119 THR 120 0.0002

THR 120 ASP 121 -0.0052

ASP 121 PHE 122 0.0000

PHE 122 GLY 123 0.0301

GLY 123 ASP 124 -0.0000

ASP 124 MET 125 0.0023

MET 125 ASN 126 -0.0003

ASN 126 THR 127 0.0383

THR 127 ILE 128 -0.0002

ILE 128 VAL 129 -0.0095

VAL 129 ASN 130 0.0000

ASN 130 VAL 131 0.0168

VAL 131 ASP 132 0.0002

ASP 132 PRO 133 0.0017

PRO 133 GLU 134 -0.0000

GLU 134 ASN 135 0.0007

ASN 135 LYS 136 -0.0002

LYS 136 TYR 137 0.0135

TYR 137 VAL 138 0.0000

VAL 138 VAL 139 -0.0332

VAL 139 SER 140 0.0002

SER 140 THR 141 -0.0142

THR 141 ARG 142 -0.0002

ARG 142 VAL 143 -0.0098

VAL 143 ARG 144 -0.0001

ARG 144 CYS 145 -0.0157

CYS 145 GLY 146 -0.0003

GLY 146 ARG 147 -0.0066

ARG 147 SER 148 -0.0000

SER 148 LEU 149 -0.0113

LEU 149 GLN 150 0.0003

GLN 150 GLY 151 0.0157

GLY 151 TYR 152 0.0002

TYR 152 PRO 153 -0.0882

PRO 153 PHE 154 -0.0004

PHE 154 ASN 155 0.0124

ASN 155 PRO 156 0.0002

PRO 156 CYS 157 -0.0087

CYS 157 LEU 158 0.0000

LEU 158 THR 159 -0.0082

THR 159 GLU 160 0.0000

GLU 160 ALA 161 0.0113

ALA 161 GLN 162 0.0002

GLN 162 TYR 163 -0.0245

TYR 163 LYS 164 0.0002

LYS 164 GLU 165 0.0230

GLU 165 MET 166 -0.0003

MET 166 GLU 167 -0.0551

GLU 167 ASP 168 0.0000

ASP 168 LYS 169 0.0118

LYS 169 VAL 170 0.0001

VAL 170 SER 171 -0.0347

SER 171 SER 172 -0.0002

SER 172 GLN 173 0.0100

GLN 173 LEU 174 -0.0000

LEU 174 LYS 175 -0.0167

LYS 175 GLY 176 0.0000

GLY 176 MET 177 0.0200

MET 177 THR 178 0.0003

THR 178 GLY 179 0.0088

GLY 179 ASP 180 0.0000

ASP 180 LEU 181 -0.0057

LEU 181 LYS 182 -0.0001

LYS 182 GLY 183 0.0181

GLY 183 THR 184 0.0003

THR 184 TYR 185 0.0363

TYR 185 TYR 186 0.0003

TYR 186 PRO 187 0.0555

PRO 187 LEU 188 0.0003

LEU 188 THR 189 -0.0142

THR 189 GLY 190 -0.0001

GLY 190 MET 191 -0.0129

MET 191 ASP 192 -0.0004

ASP 192 LYS 193 0.0062

LYS 193 LYS 194 -0.0002

LYS 194 THR 195 -0.0506

THR 195 GLN 196 -0.0001

GLN 196 GLN 197 -0.0610

GLN 197 GLN 198 0.0000

GLN 198 LEU 199 0.0010

LEU 199 ILE 200 0.0003

ILE 200 ASP 201 -0.0098

ASP 201 ASP 202 -0.0003

ASP 202 HIS 203 -0.0043

HIS 203 PHE 204 -0.0002

PHE 204 LEU 205 -0.0406

LEU 205 PHE 206 0.0001

PHE 206 LYS 207 0.0752

LYS 207 GLU 208 -0.0002

GLU 208 GLY 209 0.3923

GLY 209 ASP 210 -0.0000

ASP 210 ARG 211 0.2784

ARG 211 PHE 212 0.0000

PHE 212 LEU 213 0.0588

LEU 213 GLN 214 0.0002

GLN 214 ALA 215 0.1213

ALA 215 ALA 216 0.0002

ALA 216 ASN 217 0.0598

ASN 217 ALA 218 -0.0003

ALA 218 CYS 219 0.0454

CYS 219 ARG 220 0.0002

ARG 220 TYR 221 0.1029

TYR 221 TRP 222 -0.0002

TRP 222 PRO 223 0.0808

PRO 223 THR 224 0.0001

THR 224 GLY 225 0.0103

GLY 225 ARG 226 0.0001

ARG 226 GLY 227 0.0083

GLY 227 ILE 228 0.0001

ILE 228 TYR 229 0.0436

TYR 229 HIS 230 -0.0002

HIS 230 ASN 231 0.0118

ASN 231 ASP 232 0.0002

ASP 232 ALA 233 -0.0031

ALA 233 LYS 234 0.0001

LYS 234 THR 235 -0.0095

THR 235 PHE 236 0.0005

PHE 236 LEU 237 0.0149

LEU 237 VAL 238 0.0000

VAL 238 TRP 239 0.0381

TRP 239 VAL 240 0.0002

VAL 240 ASN 241 0.0211

ASN 241 GLU 242 -0.0002

GLU 242 GLU 243 0.0535

GLU 243 ASP 244 -0.0001

ASP 244 HIS 245 0.0298

HIS 245 LEU 246 0.0001

LEU 246 ARG 247 -0.0231

ARG 247 ILE 248 -0.0001

ILE 248 ILE 249 -0.0232

ILE 249 SER 250 0.0002

SER 250 MET 251 -0.0199

MET 251 GLN 252 0.0003

GLN 252 GLN 253 -0.0370

GLN 253 GLY 254 -0.0001

GLY 254 GLY 255 -0.0143

GLY 255 ASP 256 0.0003

ASP 256 LEU 257 -0.0045

LEU 257 LYS 258 0.0003

LYS 258 GLN 259 0.0227

GLN 259 VAL 260 0.0001

VAL 260 TYR 261 -0.0421

TYR 261 SER 262 -0.0000

SER 262 ARG 263 0.0246

ARG 263 MET 264 0.0006

MET 264 VAL 265 -0.0217

VAL 265 SER 266 -0.0004

SER 266 GLY 267 0.0250

GLY 267 VAL 268 0.0000

VAL 268 LYS 269 -0.0123

LYS 269 GLU 270 0.0003

GLU 270 ILE 271 0.0196

ILE 271 GLU 272 -0.0001

GLU 272 LYS 273 -0.0512

LYS 273 LYS 274 0.0002

LYS 274 LEU 275 -0.0269

LEU 275 PRO 276 0.0003

PRO 276 PHE 277 -0.0687

PHE 277 SER 278 0.0003

SER 278 ARG 279 -0.0281

ARG 279 ASP 280 0.0001

ASP 280 ASP 281 -0.0125

ASP 281 ARG 282 -0.0004

ARG 282 LEU 283 0.0227

LEU 283 GLY 284 0.0001

GLY 284 PHE 285 -0.0622

PHE 285 LEU 286 -0.0000

LEU 286 THR 287 0.0479

THR 287 PHE 288 -0.0001

PHE 288 CYS 289 -0.0255

CYS 289 PRO 290 -0.0002

PRO 290 THR 291 0.0249

THR 291 ASN 292 -0.0002

ASN 292 LEU 293 0.0254

LEU 293 GLY 294 0.0001

GLY 294 THR 295 -0.0412

THR 295 THR 296 0.0000

THR 296 ILE 297 0.0079

ILE 297 ARG 298 0.0001

ARG 298 ALA 299 0.0042

ALA 299 SER 300 0.0002

SER 300 VAL 301 0.0095

VAL 301 HIS 302 0.0001

HIS 302 ILE 303 -0.0620

ILE 303 LYS 304 -0.0001

LYS 304 LEU 305 -0.0518

LEU 305 PRO 306 -0.0000

PRO 306 LYS 307 -0.0462

LYS 307 LEU 308 -0.0002

LEU 308 ALA 309 -0.0500

ALA 309 ALA 310 -0.0001

ALA 310 ASP 311 -0.0093

ASP 311 LYS 312 -0.0001

LYS 312 ALA 313 -0.0519

ALA 313 LYS 314 0.0000

LYS 314 LEU 315 0.0030

LEU 315 ASP 316 -0.0000

ASP 316 SER 317 -0.0581

SER 317 ILE 318 0.0003

ILE 318 ALA 319 0.0080

ALA 319 ALA 320 -0.0001

ALA 320 LYS 321 -0.0343

LYS 321 TYR 322 0.0000

TYR 322 ASN 323 0.0308

ASN 323 LEU 324 -0.0004

LEU 324 GLN 325 -0.0688

GLN 325 VAL 326 0.0003

VAL 326 ARG 327 -0.0886

ARG 327 GLY 328 -0.0001

GLY 328 THR 329 -0.0422

THR 329 ARG 330 -0.0003

ARG 330 GLY 331 0.1122

GLY 331 GLU 332 -0.0002

GLU 332 HIS 333 0.0410

HIS 333 THR 334 0.0001

THR 334 GLU 335 -0.0687

GLU 335 SER 336 0.0005

SER 336 GLU 337 -0.0057

GLU 337 GLY 338 0.0003

GLY 338 GLY 339 -0.0262

GLY 339 VAL 340 -0.0000

VAL 340 TYR 341 0.0492

TYR 341 ASP 342 0.0001

ASP 342 ILE 343 -0.0091

ILE 343 SER 344 0.0001

SER 344 ASN 345 0.0558

ASN 345 LYS 346 -0.0001

LYS 346 ARG 347 0.0196

ARG 347 ARG 348 -0.0003

ARG 348 MET 349 0.0883

MET 349 GLY 350 0.0001

GLY 350 LEU 351 -0.0983

LEU 351 THR 352 -0.0001

THR 352 GLU 353 -0.0177

GLU 353 TYR 354 -0.0003

TYR 354 GLN 355 -0.0181

GLN 355 ALA 356 -0.0001

ALA 356 VAL 357 -0.0077

VAL 357 ARG 358 -0.0000

ARG 358 GLU 359 -0.0064

GLU 359 MET 360 -0.0001

MET 360 GLN 361 -0.0175

GLN 361 ASP 362 0.0000

ASP 362 GLY 363 0.0160

GLY 363 ILE 364 0.0004

ILE 364 GLN 365 -0.0186

GLN 365 GLU 366 0.0000

GLU 366 LEU 367 -0.0087

LEU 367 ILE 368 0.0002

ILE 368 LYS 369 -0.0236

LYS 369 LEU 370 -0.0001

LEU 370 GLU 371 -0.0072

GLU 371 GLN 372 -0.0000

GLN 372 ALA 373 -0.0229

ALA 373 ALA 374 -0.0002

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 8 ---

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

* *