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

* *

CA strain for 220926155553133140

--- normal mode 9 ---

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 GLU 2 -0.0002

GLU 2 LEU 3 0.0187

LEU 3 ARG 4 0.0004

ARG 4 HIS 5 -0.0167

HIS 5 THR 6 -0.0003

THR 6 PRO 7 -0.0230

PRO 7 ALA 8 -0.0001

ALA 8 ARG 9 0.0062

ARG 9 ASP 10 0.0001

ASP 10 LEU 11 0.0010

LEU 11 ASP 12 -0.0000

ASP 12 LYS 13 -0.0045

LYS 13 PHE 14 0.0004

PHE 14 ILE 15 0.0076

ILE 15 GLU 16 0.0001

GLU 16 ASP 17 0.0201

ASP 17 HIS 18 0.0002

HIS 18 LEU 19 0.0051

LEU 19 LEU 20 -0.0001

LEU 20 PRO 21 -0.0798

PRO 21 ASN 22 -0.0002

ASN 22 THR 23 -0.0070

THR 23 CYS 24 0.0000

CYS 24 PHE 25 0.0173

PHE 25 ARG 26 0.0003

ARG 26 THR 27 -0.0542

THR 27 GLN 28 -0.0002

GLN 28 VAL 29 0.0373

VAL 29 LYS 30 0.0003

LYS 30 GLU 31 0.0104

GLU 31 ALA 32 0.0001

ALA 32 ILE 33 0.0356

ILE 33 ASP 34 0.0004

ASP 34 ILE 35 0.0075

ILE 35 VAL 36 0.0004

VAL 36 CYS 37 0.0432

CYS 37 ARG 38 0.0003

ARG 38 PHE 39 -0.0416

PHE 39 LEU 40 -0.0003

LEU 40 LYS 41 0.0131

LYS 41 GLU 42 0.0004

GLU 42 ARG 43 0.0010

ARG 43 CYS 44 -0.0003

CYS 44 PHE 45 0.0292

PHE 45 GLN 46 -0.0001

GLN 46 GLY 47 -0.0401

GLY 47 THR 48 0.0001

THR 48 ALA 49 -0.0346

ALA 49 ASP 50 0.0001

ASP 50 PRO 51 -0.0180

PRO 51 VAL 52 -0.0001

VAL 52 ARG 53 -0.0280

ARG 53 VAL 54 -0.0001

VAL 54 SER 55 -0.0164

SER 55 LYS 56 0.0003

LYS 56 VAL 57 0.0057

VAL 57 VAL 58 -0.0001

VAL 58 LYS 59 -0.0917

LYS 59 GLY 60 -0.0000

GLY 60 GLY 61 -0.0659

GLY 61 SER 62 0.0002

SER 62 SER 63 -0.0612

SER 63 GLY 64 0.0005

GLY 64 LYS 65 0.0127

LYS 65 GLY 66 0.0000

GLY 66 THR 67 -0.0299

THR 67 THR 68 0.0002

THR 68 LEU 69 -0.0090

LEU 69 ARG 70 0.0001

ARG 70 GLY 71 -0.0190

GLY 71 ARG 72 -0.0003

ARG 72 SER 73 -0.0655

SER 73 ASP 74 0.0001

ASP 74 ALA 75 -0.1088

ALA 75 ASP 76 0.0005

ASP 76 LEU 77 -0.0626

LEU 77 VAL 78 0.0003

VAL 78 VAL 79 -0.0084

VAL 79 PHE 80 -0.0003

PHE 80 LEU 81 -0.0252

LEU 81 THR 82 -0.0001

THR 82 LYS 83 -0.0247

LYS 83 LEU 84 0.0000

LEU 84 THR 85 0.0042

THR 85 SER 86 0.0000

SER 86 PHE 87 0.0239

PHE 87 GLU 88 0.0002

GLU 88 ASP 89 0.0522

ASP 89 GLN 90 0.0002

GLN 90 LEU 91 -0.0287

LEU 91 ARG 92 -0.0000

ARG 92 ARG 93 0.0467

ARG 93 ARG 94 0.0003

ARG 94 GLY 95 -0.0233

GLY 95 GLU 96 -0.0002

GLU 96 PHE 97 -0.0415

PHE 97 ILE 98 0.0001

ILE 98 GLN 99 0.0496

GLN 99 GLU 100 0.0003

GLU 100 ILE 101 0.0066

ILE 101 ARG 102 -0.0000

ARG 102 ARG 103 -0.0711

ARG 103 GLN 104 0.0001

GLN 104 LEU 105 0.0279

LEU 105 GLU 106 0.0002

GLU 106 ALA 107 -0.0291

ALA 107 CYS 108 -0.0002

CYS 108 GLN 109 0.0367

GLN 109 ARG 110 -0.0002

ARG 110 GLU 111 -0.0050

GLU 111 GLN 112 -0.0000

GLN 112 LYS 113 0.0004

LYS 113 PHE 114 0.0002

PHE 114 LYS 115 -0.0029

LYS 115 VAL 116 -0.0004

VAL 116 THR 117 -0.0279

THR 117 PHE 118 -0.0002

PHE 118 GLU 119 -0.1552

GLU 119 VAL 120 0.0001

VAL 120 GLN 121 -0.0815

GLN 121 SER 122 -0.0001

SER 122 PRO 123 0.3332

PRO 123 ARG 124 -0.0003

ARG 124 ARG 125 0.0839

ARG 125 GLU 126 0.0000

GLU 126 ASN 127 -0.1452

ASN 127 PRO 128 -0.0001

PRO 128 ARG 129 0.1559

ARG 129 GLY 130 0.0004

GLY 130 LEU 131 -0.0667

LEU 131 SER 132 -0.0001

SER 132 PHE 133 -0.0822

PHE 133 VAL 134 0.0002

VAL 134 LEU 135 0.0987

LEU 135 SER 136 -0.0003

SER 136 SER 137 0.0190

SER 137 PRO 138 -0.0000

PRO 138 GLN 139 0.0002

GLN 139 LEU 140 -0.0001

LEU 140 GLN 141 0.0069

GLN 141 GLN 142 0.0001

GLN 142 GLU 143 0.0651

GLU 143 VAL 144 -0.0002

VAL 144 GLU 145 0.0873

GLU 145 PHE 146 -0.0001

PHE 146 ASP 147 -0.0558

ASP 147 VAL 148 -0.0002

VAL 148 LEU 149 -0.0360

LEU 149 PRO 150 0.0000

PRO 150 ALA 151 -0.0050

ALA 151 PHE 152 0.0002

PHE 152 ASP 153 -0.0260

ASP 153 ALA 154 -0.0002

ALA 154 LEU 155 -0.0212

LEU 155 GLY 156 -0.0002

GLY 156 GLN 157 -0.0235

GLN 157 TRP 158 -0.0001

TRP 158 THR 159 -0.0144

THR 159 PRO 160 -0.0002

PRO 160 GLY 161 -0.0028

GLY 161 TYR 162 0.0000

TYR 162 LYS 163 -0.0139

LYS 163 PRO 164 -0.0001

PRO 164 ASN 165 0.0122

ASN 165 PRO 166 0.0001

PRO 166 GLU 167 0.0072

GLU 167 ILE 168 -0.0000

ILE 168 TYR 169 -0.0007

TYR 169 VAL 170 0.0003

VAL 170 GLN 171 0.0022

GLN 171 LEU 172 0.0005

LEU 172 ILE 173 0.0198

ILE 173 LYS 174 0.0004

LYS 174 GLU 175 0.0190

GLU 175 CYS 176 0.0000

CYS 176 LYS 177 -0.0166

LYS 177 SER 178 -0.0003

SER 178 ARG 179 0.0028

ARG 179 GLY 180 -0.0000

GLY 180 LYS 181 -0.0219

LYS 181 GLU 182 0.0003

GLU 182 GLY 183 -0.0080

GLY 183 GLU 184 0.0003

GLU 184 PHE 185 0.0094

PHE 185 SER 186 -0.0002

SER 186 THR 187 0.0089

THR 187 CYS 188 -0.0004

CYS 188 PHE 189 0.0172

PHE 189 THR 190 -0.0001

THR 190 GLU 191 0.0234

GLU 191 LEU 192 0.0001

LEU 192 GLN 193 -0.0396

GLN 193 ARG 194 -0.0002

ARG 194 ARG 194 0.0377

ARG 194 ASP 195 0.0120

ASP 195 PHE 196 0.0003

PHE 196 LEU 197 0.0304

LEU 197 ARG 198 0.0001

ARG 198 ASN 199 0.0045

ASN 199 ARG 200 -0.0001

ARG 200 PRO 201 0.0694

PRO 201 THR 202 -0.0003

THR 202 LYS 203 0.0419

LYS 203 LEU 204 -0.0001

LEU 204 LYS 205 -0.0187

LYS 205 SER 206 0.0003

SER 206 LEU 207 -0.0078

LEU 207 ILE 208 0.0001

ILE 208 ARG 209 -0.0071

ARG 209 LEU 210 0.0002

LEU 210 VAL 211 0.0132

VAL 211 LYS 212 0.0001

LYS 212 HIS 213 -0.0134

HIS 213 TRP 214 0.0002

TRP 214 TYR 215 0.0173

TYR 215 GLN 216 0.0003

GLN 216 THR 217 -0.0551

THR 217 CYS 218 -0.0002

CYS 218 LYS 219 0.0560

LYS 219 LYS 220 0.0002

LYS 220 THR 221 -0.0165

THR 221 HIS 222 0.0001

HIS 222 GLY 223 0.0656

GLY 223 ASN 224 -0.0002

ASN 224 LYS 225 -0.0120

LYS 225 LEU 226 0.0004

LEU 226 PRO 227 -0.1076

PRO 227 PRO 228 0.0001

PRO 228 GLN 229 0.0500

GLN 229 TYR 230 -0.0002

TYR 230 ALA 231 0.0037

ALA 231 LEU 232 -0.0002

LEU 232 GLU 233 -0.0233

GLU 233 LEU 234 -0.0000

LEU 234 LEU 235 -0.0028

LEU 235 THR 236 -0.0003

THR 236 VAL 237 0.0273

VAL 237 TYR 238 -0.0002

TYR 238 ALA 239 0.0662

ALA 239 TRP 240 0.0001

TRP 240 GLU 241 0.0131

GLU 241 GLN 242 -0.0000

GLN 242 GLY 243 0.0416

GLY 243 SER 244 -0.0000

SER 244 ARG 245 0.0168

ARG 245 LYS 246 -0.0002

LYS 246 THR 247 -0.0136

THR 247 ASP 248 -0.0002

ASP 248 PHE 249 0.0378

PHE 249 SER 250 0.0000

SER 250 THR 251 -0.0307

THR 251 ALA 252 0.0002

ALA 252 GLN 253 -0.0056

GLN 253 GLY 254 0.0004

GLY 254 PHE 255 0.0196

PHE 255 GLN 256 -0.0002

GLN 256 THR 257 0.0337

THR 257 VAL 258 0.0001

VAL 258 LEU 259 0.0188

LEU 259 GLU 260 -0.0002

GLU 260 LEU 261 0.0209

LEU 261 VAL 262 -0.0002

VAL 262 LEU 263 -0.0094

LEU 263 LYS 264 -0.0002

LYS 264 HIS 265 -0.0062

HIS 265 GLN 266 0.0000

GLN 266 LYS 267 0.0277

LYS 267 LEU 268 0.0001

LEU 268 CYS 269 0.0727

CYS 269 ILE 270 0.0002

ILE 270 PHE 271 0.0350

PHE 271 TRP 272 0.0001

TRP 272 GLU 273 0.0474

GLU 273 ALA 274 -0.0001

ALA 274 TYR 275 0.0204

TYR 275 TYR 276 0.0000

TYR 276 ASP 277 -0.0114

ASP 277 PHE 278 0.0002

PHE 278 THR 279 0.0105

THR 279 ASN 280 -0.0001

ASN 280 PRO 281 -0.0127

PRO 281 VAL 282 0.0003

VAL 282 VAL 283 0.0084

VAL 283 GLY 284 -0.0002

GLY 284 ARG 285 -0.0022

ARG 285 CYS 286 -0.0000

CYS 286 MET 287 0.0356

MET 287 LEU 288 -0.0000

LEU 288 GLN 289 0.0049

GLN 289 GLN 290 -0.0002

GLN 290 LEU 291 0.0604

LEU 291 LYS 292 -0.0001

LYS 292 LYS 293 -0.0144

LYS 293 PRO 294 0.0001

PRO 294 ARG 295 -0.0208

ARG 295 PRO 296 0.0003

PRO 296 VAL 297 -0.0281

VAL 297 ILE 298 -0.0002

ILE 298 LEU 299 -0.0151

LEU 299 ASP 300 -0.0004

ASP 300 PRO 301 -0.0221

PRO 301 ALA 302 -0.0001

ALA 302 ASP 303 0.0381

ASP 303 PRO 304 -0.0003

PRO 304 THR 305 0.0447

THR 305 GLY 306 -0.0004

GLY 306 ASN 307 -0.0830

ASN 307 VAL 308 -0.0002

VAL 308 GLY 309 -0.0520

GLY 309 GLY 310 0.0000

GLY 310 GLY 311 0.0448

GLY 311 ASP 312 0.0001

ASP 312 THR 313 0.0008

THR 313 HIS 314 -0.0002

HIS 314 SER 315 0.0056

SER 315 TRP 316 0.0004

TRP 316 GLN 317 -0.0047

GLN 317 ARG 318 -0.0002

ARG 318 LEU 319 -0.0006

LEU 319 ALA 320 -0.0002

ALA 320 GLN 321 0.0240

GLN 321 GLU 322 -0.0001

GLU 322 ALA 323 0.0311

ALA 323 ARG 324 0.0001

ARG 324 VAL 325 0.0062

VAL 325 TRP 326 0.0001

TRP 326 LEU 327 -0.0045

LEU 327 GLY 328 0.0001

GLY 328 TYR 329 -0.0013

TYR 329 PRO 330 -0.0001

PRO 330 CYS 331 0.0068

CYS 331 CYS 332 0.0000

CYS 332 LYS 333 0.0096

LYS 333 ASN 334 -0.0003

ASN 334 LEU 335 0.0566

LEU 335 ASP 336 -0.0000

ASP 336 GLY 337 -0.0583

GLY 337 SER 338 -0.0001

SER 338 LEU 339 0.0127

LEU 339 VAL 340 0.0002

VAL 340 GLY 341 0.0554

GLY 341 ALA 342 0.0002

ALA 342 TRP 343 0.0613

TRP 343 THR 344 -0.0001

THR 344 MET 345 0.0372

MET 345 LEU 346 -0.0001

LEU 346 GLN 347 0.0014

GLN 347 LYS 348 0.0000

LYS 348 ILE 349 -0.0014

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: October 18th, 2018.

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

*** ***

CA strain for 220926155553133140

--- normal mode 9 ---

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

* *