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

* *

CA strain for 220926155553133140

--- normal mode 11 ---

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 0.0001

GLU 2 LEU 3 0.0063

LEU 3 ARG 4 0.0000

ARG 4 HIS 5 0.0036

HIS 5 THR 6 -0.0000

THR 6 PRO 7 0.0129

PRO 7 ALA 8 0.0002

ALA 8 ARG 9 -0.0218

ARG 9 ASP 10 -0.0001

ASP 10 LEU 11 0.0153

LEU 11 ASP 12 0.0004

ASP 12 LYS 13 -0.0391

LYS 13 PHE 14 0.0000

PHE 14 ILE 15 0.0243

ILE 15 GLU 16 0.0000

GLU 16 ASP 17 -0.0261

ASP 17 HIS 18 0.0003

HIS 18 LEU 19 0.0208

LEU 19 LEU 20 0.0002

LEU 20 PRO 21 0.0298

PRO 21 ASN 22 -0.0001

ASN 22 THR 23 0.0089

THR 23 CYS 24 -0.0003

CYS 24 PHE 25 -0.0390

PHE 25 ARG 26 0.0001

ARG 26 THR 27 -0.0465

THR 27 GLN 28 0.0000

GLN 28 VAL 29 0.0148

VAL 29 LYS 30 0.0002

LYS 30 GLU 31 0.0133

GLU 31 ALA 32 -0.0002

ALA 32 ILE 33 0.0191

ILE 33 ASP 34 0.0002

ASP 34 ILE 35 0.0058

ILE 35 VAL 36 0.0005

VAL 36 CYS 37 0.0199

CYS 37 ARG 38 -0.0003

ARG 38 PHE 39 -0.0067

PHE 39 LEU 40 -0.0001

LEU 40 LYS 41 0.0007

LYS 41 GLU 42 0.0004

GLU 42 ARG 43 0.0201

ARG 43 CYS 44 0.0001

CYS 44 PHE 45 0.0110

PHE 45 GLN 46 0.0001

GLN 46 GLY 47 -0.0157

GLY 47 THR 48 -0.0002

THR 48 ALA 49 0.0703

ALA 49 ASP 50 0.0003

ASP 50 PRO 51 -0.0552

PRO 51 VAL 52 0.0002

VAL 52 ARG 53 -0.0385

ARG 53 VAL 54 0.0002

VAL 54 SER 55 -0.0398

SER 55 LYS 56 0.0001

LYS 56 VAL 57 0.0299

VAL 57 VAL 58 -0.0001

VAL 58 LYS 59 0.0060

LYS 59 GLY 60 0.0003

GLY 60 GLY 61 0.0192

GLY 61 SER 62 0.0001

SER 62 SER 63 -0.0492

SER 63 GLY 64 -0.0000

GLY 64 LYS 65 -0.0146

LYS 65 GLY 66 -0.0003

GLY 66 THR 67 0.0062

THR 67 THR 68 -0.0003

THR 68 LEU 69 0.0469

LEU 69 ARG 70 0.0003

ARG 70 GLY 71 0.0537

GLY 71 ARG 72 0.0001

ARG 72 SER 73 0.0595

SER 73 ASP 74 -0.0000

ASP 74 ALA 75 0.0257

ALA 75 ASP 76 -0.0001

ASP 76 LEU 77 0.0201

LEU 77 VAL 78 -0.0002

VAL 78 VAL 79 -0.0138

VAL 79 PHE 80 0.0002

PHE 80 LEU 81 -0.0417

LEU 81 THR 82 0.0000

THR 82 LYS 83 -0.0033

LYS 83 LEU 84 0.0002

LEU 84 THR 85 -0.0011

THR 85 SER 86 0.0001

SER 86 PHE 87 0.0100

PHE 87 GLU 88 0.0001

GLU 88 ASP 89 0.0180

ASP 89 GLN 90 0.0003

GLN 90 LEU 91 0.0119

LEU 91 ARG 92 -0.0000

ARG 92 ARG 93 0.0059

ARG 93 ARG 94 0.0004

ARG 94 GLY 95 -0.0154

GLY 95 GLU 96 0.0006

GLU 96 PHE 97 0.0067

PHE 97 ILE 98 0.0001

ILE 98 GLN 99 -0.0077

GLN 99 GLU 100 -0.0005

GLU 100 ILE 101 0.0000

ILE 101 ARG 102 -0.0001

ARG 102 ARG 103 0.0445

ARG 103 GLN 104 0.0001

GLN 104 LEU 105 0.0043

LEU 105 GLU 106 -0.0002

GLU 106 ALA 107 0.0200

ALA 107 CYS 108 0.0002

CYS 108 GLN 109 0.0122

GLN 109 ARG 110 0.0001

ARG 110 GLU 111 -0.0013

GLU 111 GLN 112 0.0001

GLN 112 LYS 113 0.0043

LYS 113 PHE 114 0.0003

PHE 114 LYS 115 0.0030

LYS 115 VAL 116 -0.0000

VAL 116 THR 117 0.0051

THR 117 PHE 118 0.0005

PHE 118 GLU 119 0.0557

GLU 119 VAL 120 -0.0002

VAL 120 GLN 121 0.0050

GLN 121 SER 122 -0.0001

SER 122 PRO 123 -0.0579

PRO 123 ARG 124 -0.0001

ARG 124 ARG 125 -0.0501

ARG 125 GLU 126 0.0002

GLU 126 ASN 127 0.0766

ASN 127 PRO 128 0.0005

PRO 128 ARG 129 0.0119

ARG 129 GLY 130 0.0000

GLY 130 LEU 131 -0.1401

LEU 131 SER 132 0.0004

SER 132 PHE 133 -0.0313

PHE 133 VAL 134 0.0001

VAL 134 LEU 135 -0.0290

LEU 135 SER 136 0.0002

SER 136 SER 137 -0.0197

SER 137 PRO 138 -0.0003

PRO 138 GLN 139 0.0014

GLN 139 LEU 140 -0.0001

LEU 140 GLN 141 0.0152

GLN 141 GLN 142 0.0002

GLN 142 GLU 143 -0.0124

GLU 143 VAL 144 -0.0001

VAL 144 GLU 145 -0.0206

GLU 145 PHE 146 0.0000

PHE 146 ASP 147 0.0070

ASP 147 VAL 148 -0.0003

VAL 148 LEU 149 0.0050

LEU 149 PRO 150 0.0001

PRO 150 ALA 151 -0.0256

ALA 151 PHE 152 0.0003

PHE 152 ASP 153 -0.0230

ASP 153 ALA 154 0.0002

ALA 154 LEU 155 -0.0261

LEU 155 GLY 156 -0.0003

GLY 156 GLN 157 -0.0300

GLN 157 TRP 158 -0.0001

TRP 158 THR 159 -0.0115

THR 159 PRO 160 0.0001

PRO 160 GLY 161 0.0088

GLY 161 TYR 162 0.0001

TYR 162 LYS 163 -0.0134

LYS 163 PRO 164 -0.0000

PRO 164 ASN 165 0.0459

ASN 165 PRO 166 0.0001

PRO 166 GLU 167 -0.0059

GLU 167 ILE 168 0.0000

ILE 168 TYR 169 -0.0068

TYR 169 VAL 170 0.0001

VAL 170 GLN 171 -0.0043

GLN 171 LEU 172 -0.0002

LEU 172 ILE 173 0.0127

ILE 173 LYS 174 0.0002

LYS 174 GLU 175 -0.0050

GLU 175 CYS 176 0.0000

CYS 176 LYS 177 0.0010

LYS 177 SER 178 -0.0001

SER 178 ARG 179 -0.0063

ARG 179 GLY 180 -0.0002

GLY 180 LYS 181 -0.0062

LYS 181 GLU 182 -0.0002

GLU 182 GLY 183 -0.0121

GLY 183 GLU 184 0.0003

GLU 184 PHE 185 -0.0058

PHE 185 SER 186 -0.0001

SER 186 THR 187 -0.0414

THR 187 CYS 188 0.0002

CYS 188 PHE 189 -0.0249

PHE 189 THR 190 -0.0003

THR 190 GLU 191 0.0296

GLU 191 LEU 192 -0.0003

LEU 192 GLN 193 -0.0028

GLN 193 ARG 194 -0.0002

ARG 194 ARG 194 0.0000

ARG 194 ASP 195 0.0254

ASP 195 PHE 196 -0.0001

PHE 196 LEU 197 0.0727

LEU 197 ARG 198 0.0000

ARG 198 ASN 199 -0.0196

ASN 199 ARG 200 0.0001

ARG 200 PRO 201 0.0690

PRO 201 THR 202 -0.0002

THR 202 LYS 203 0.0635

LYS 203 LEU 204 0.0002

LEU 204 LYS 205 -0.0513

LYS 205 SER 206 -0.0003

SER 206 LEU 207 0.0323

LEU 207 ILE 208 -0.0001

ILE 208 ARG 209 0.0175

ARG 209 LEU 210 -0.0005

LEU 210 VAL 211 -0.0031

VAL 211 LYS 212 0.0002

LYS 212 HIS 213 0.0524

HIS 213 TRP 214 0.0001

TRP 214 TYR 215 0.0007

TYR 215 GLN 216 -0.0002

GLN 216 THR 217 0.0290

THR 217 CYS 218 -0.0001

CYS 218 LYS 219 0.0161

LYS 219 LYS 220 -0.0000

LYS 220 THR 221 -0.0052

THR 221 HIS 222 -0.0000

HIS 222 GLY 223 0.0135

GLY 223 ASN 224 -0.0002

ASN 224 LYS 225 0.0226

LYS 225 LEU 226 -0.0004

LEU 226 PRO 227 0.0086

PRO 227 PRO 228 0.0002

PRO 228 GLN 229 -0.0156

GLN 229 TYR 230 -0.0002

TYR 230 ALA 231 -0.0184

ALA 231 LEU 232 0.0001

LEU 232 GLU 233 -0.0240

GLU 233 LEU 234 -0.0004

LEU 234 LEU 235 -0.0533

LEU 235 THR 236 -0.0002

THR 236 VAL 237 -0.0925

VAL 237 TYR 238 0.0000

TYR 238 ALA 239 -0.0067

ALA 239 TRP 240 0.0004

TRP 240 GLU 241 -0.1034

GLU 241 GLN 242 -0.0001

GLN 242 GLY 243 -0.0009

GLY 243 SER 244 -0.0002

SER 244 ARG 245 0.0605

ARG 245 LYS 246 0.0002

LYS 246 THR 247 -0.0434

THR 247 ASP 248 0.0002

ASP 248 PHE 249 0.0393

PHE 249 SER 250 -0.0003

SER 250 THR 251 -0.0149

THR 251 ALA 252 0.0001

ALA 252 GLN 253 0.0008

GLN 253 GLY 254 0.0002

GLY 254 PHE 255 -0.0006

PHE 255 GLN 256 0.0003

GLN 256 THR 257 0.0386

THR 257 VAL 258 0.0002

VAL 258 LEU 259 0.0550

LEU 259 GLU 260 -0.0002

GLU 260 LEU 261 -0.0292

LEU 261 VAL 262 0.0000

VAL 262 LEU 263 0.0332

LEU 263 LYS 264 0.0004

LYS 264 HIS 265 -0.0273

HIS 265 GLN 266 0.0002

GLN 266 LYS 267 0.0630

LYS 267 LEU 268 0.0001

LEU 268 CYS 269 -0.0681

CYS 269 ILE 270 0.0001

ILE 270 PHE 271 -0.0914

PHE 271 TRP 272 -0.0002

TRP 272 GLU 273 0.0430

GLU 273 ALA 274 0.0001

ALA 274 TYR 275 -0.0447

TYR 275 TYR 276 -0.0005

TYR 276 ASP 277 0.0345

ASP 277 PHE 278 -0.0000

PHE 278 THR 279 -0.0154

THR 279 ASN 280 0.0000

ASN 280 PRO 281 0.0083

PRO 281 VAL 282 0.0002

VAL 282 VAL 283 0.0198

VAL 283 GLY 284 -0.0001

GLY 284 ARG 285 0.0089

ARG 285 CYS 286 -0.0001

CYS 286 MET 287 0.0416

MET 287 LEU 288 0.0000

LEU 288 GLN 289 0.0344

GLN 289 GLN 290 -0.0004

GLN 290 LEU 291 0.0323

LEU 291 LYS 292 0.0003

LYS 292 LYS 293 0.0165

LYS 293 PRO 294 0.0000

PRO 294 ARG 295 -0.0369

ARG 295 PRO 296 0.0001

PRO 296 VAL 297 -0.0456

VAL 297 ILE 298 -0.0000

ILE 298 LEU 299 -0.0564

LEU 299 ASP 300 -0.0002

ASP 300 PRO 301 -0.0289

PRO 301 ALA 302 -0.0002

ALA 302 ASP 303 0.0124

ASP 303 PRO 304 -0.0002

PRO 304 THR 305 0.0082

THR 305 GLY 306 0.0001

GLY 306 ASN 307 -0.0650

ASN 307 VAL 308 -0.0001

VAL 308 GLY 309 -0.0520

GLY 309 GLY 310 0.0001

GLY 310 GLY 311 0.0209

GLY 311 ASP 312 0.0002

ASP 312 THR 313 -0.0020

THR 313 HIS 314 0.0001

HIS 314 SER 315 -0.0145

SER 315 TRP 316 -0.0002

TRP 316 GLN 317 -0.0100

GLN 317 ARG 318 0.0002

ARG 318 LEU 319 0.0155

LEU 319 ALA 320 -0.0002

ALA 320 GLN 321 0.0167

GLN 321 GLU 322 0.0002

GLU 322 ALA 323 0.0421

ALA 323 ARG 324 -0.0002

ARG 324 VAL 325 -0.0211

VAL 325 TRP 326 0.0001

TRP 326 LEU 327 0.0140

LEU 327 GLY 328 -0.0001

GLY 328 TYR 329 -0.0073

TYR 329 PRO 330 0.0001

PRO 330 CYS 331 0.0035

CYS 331 CYS 332 0.0005

CYS 332 LYS 333 -0.0128

LYS 333 ASN 334 0.0002

ASN 334 LEU 335 -0.0370

LEU 335 ASP 336 -0.0001

ASP 336 GLY 337 -0.0131

GLY 337 SER 338 -0.0001

SER 338 LEU 339 -0.0286

LEU 339 VAL 340 0.0004

VAL 340 GLY 341 -0.0196

GLY 341 ALA 342 0.0000

ALA 342 TRP 343 0.0176

TRP 343 THR 344 -0.0001

THR 344 MET 345 0.0082

MET 345 LEU 346 -0.0000

LEU 346 GLN 347 0.0046

GLN 347 LYS 348 0.0000

LYS 348 ILE 349 -0.0288

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 11 ---

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

* *