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

* *

CA strain for 22122720180123252

--- 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 -0.0001

GLU 2 LEU 3 0.0072

LEU 3 ARG 4 0.0003

ARG 4 HIS 5 -0.0127

HIS 5 THR 6 0.0003

THR 6 PRO 7 -0.0100

PRO 7 ALA 8 -0.0000

ALA 8 ARG 9 0.0001

ARG 9 ASP 10 -0.0000

ASP 10 LEU 11 0.0023

LEU 11 ASP 12 0.0003

ASP 12 LYS 13 -0.0097

LYS 13 PHE 14 -0.0004

PHE 14 ILE 15 0.0149

ILE 15 GLU 16 -0.0003

GLU 16 ASP 17 0.0158

ASP 17 HIS 18 0.0001

HIS 18 LEU 19 0.0000

LEU 19 LEU 20 0.0001

LEU 20 PRO 21 -0.0259

PRO 21 ASN 22 0.0004

ASN 22 THR 23 0.0158

THR 23 CYS 24 -0.0004

CYS 24 PHE 25 0.0118

PHE 25 ARG 26 -0.0003

ARG 26 THR 27 -0.0170

THR 27 GLN 28 -0.0005

GLN 28 VAL 29 0.0086

VAL 29 LYS 30 0.0000

LYS 30 GLU 31 -0.0047

GLU 31 ALA 32 -0.0001

ALA 32 ILE 33 0.0036

ILE 33 ASP 34 0.0001

ASP 34 ILE 35 -0.0000

ILE 35 VAL 36 0.0000

VAL 36 CYS 37 0.0157

CYS 37 ARG 38 0.0001

ARG 38 PHE 39 -0.0189

PHE 39 LEU 40 0.0005

LEU 40 LYS 41 0.0101

LYS 41 GLU 42 -0.0003

GLU 42 ARG 43 -0.0162

ARG 43 CYS 44 -0.0001

CYS 44 PHE 45 0.0168

PHE 45 GLN 46 -0.0003

GLN 46 GLY 47 -0.0226

GLY 47 THR 48 -0.0003

THR 48 ALA 49 -0.0542

ALA 49 ASP 50 0.0000

ASP 50 PRO 51 0.0105

PRO 51 VAL 52 -0.0001

VAL 52 ARG 53 -0.0011

ARG 53 VAL 54 0.0001

VAL 54 SER 55 -0.0313

SER 55 LYS 56 0.0000

LYS 56 VAL 57 -0.0082

VAL 57 VAL 58 0.0001

VAL 58 LYS 59 -0.0375

LYS 59 GLY 60 -0.0003

GLY 60 GLY 61 -0.0575

GLY 61 SER 62 -0.0003

SER 62 SER 63 -0.0332

SER 63 GLY 64 -0.0000

GLY 64 LYS 65 0.0144

LYS 65 GLY 66 0.0003

GLY 66 THR 67 -0.0186

THR 67 THR 68 -0.0001

THR 68 LEU 69 -0.0065

LEU 69 ARG 70 0.0003

ARG 70 GLY 71 -0.0427

GLY 71 ARG 72 0.0002

ARG 72 SER 73 -0.0629

SER 73 ASP 74 -0.0000

ASP 74 ALA 75 -0.0807

ALA 75 ASP 76 0.0002

ASP 76 LEU 77 -0.0521

LEU 77 VAL 78 0.0000

VAL 78 VAL 79 0.0021

VAL 79 PHE 80 0.0001

PHE 80 LEU 81 0.0022

LEU 81 THR 82 -0.0001

THR 82 LYS 83 -0.0032

LYS 83 LEU 84 -0.0007

LEU 84 THR 85 -0.0079

THR 85 SER 86 -0.0001

SER 86 PHE 87 -0.0036

PHE 87 GLU 88 0.0004

GLU 88 ASP 89 0.0138

ASP 89 GLN 90 -0.0002

GLN 90 LEU 91 -0.0172

LEU 91 ARG 92 -0.0000

ARG 92 ARG 93 0.0300

ARG 93 ARG 94 0.0001

ARG 94 GLY 95 -0.0372

GLY 95 GLU 96 -0.0000

GLU 96 PHE 97 -0.0403

PHE 97 ILE 98 0.0002

ILE 98 GLN 99 0.0579

GLN 99 GLU 100 0.0001

GLU 100 ILE 101 0.0136

ILE 101 ARG 102 -0.0000

ARG 102 ARG 103 -0.0854

ARG 103 GLN 104 0.0000

GLN 104 LEU 105 0.0239

LEU 105 GLU 106 0.0003

GLU 106 ALA 107 -0.0256

ALA 107 CYS 108 0.0002

CYS 108 GLN 109 0.0224

GLN 109 ARG 110 0.0003

ARG 110 GLU 111 0.0028

GLU 111 GLN 112 -0.0001

GLN 112 LYS 113 -0.0071

LYS 113 PHE 114 -0.0001

PHE 114 LYS 115 0.0295

LYS 115 VAL 116 0.0004

VAL 116 THR 117 0.0600

THR 117 PHE 118 0.0003

PHE 118 GLY 119 0.3240

GLY 119 VAL 120 0.0001

VAL 120 GLN 121 -0.1355

GLN 121 SER 122 -0.0001

SER 122 PRO 123 0.3238

PRO 123 ARG 124 -0.0002

ARG 124 ARG 125 0.0727

ARG 125 GLU 126 0.0001

GLU 126 GLY 127 -0.1869

GLY 127 PRO 128 -0.0002

PRO 128 ARG 129 0.1240

ARG 129 ALA 130 0.0002

ALA 130 LEU 131 0.0193

LEU 131 SER 132 0.0000

SER 132 PHE 133 -0.0253

PHE 133 VAL 134 0.0001

VAL 134 LEU 135 0.0641

LEU 135 SER 136 0.0003

SER 136 SER 137 0.0289

SER 137 PRO 138 0.0002

PRO 138 GLN 139 -0.0001

GLN 139 LEU 140 -0.0001

LEU 140 GLN 141 -0.0027

GLN 141 GLN 142 0.0002

GLN 142 GLU 143 0.0485

GLU 143 VAL 144 0.0001

VAL 144 GLU 145 0.0304

GLU 145 PHE 146 0.0002

PHE 146 ASP 147 -0.0240

ASP 147 VAL 148 0.0002

VAL 148 LEU 149 -0.0275

LEU 149 PRO 150 -0.0001

PRO 150 ALA 151 0.0070

ALA 151 PHE 152 -0.0003

PHE 152 ASP 153 -0.0012

ASP 153 ALA 154 0.0000

ALA 154 LEU 155 0.0189

LEU 155 GLY 156 -0.0001

GLY 156 GLN 157 -0.0039

GLN 157 TRP 158 -0.0002

TRP 158 THR 159 -0.0018

THR 159 PRO 160 -0.0003

PRO 160 GLY 161 -0.0048

GLY 161 TYR 162 0.0003

TYR 162 LYS 163 -0.0108

LYS 163 PRO 164 -0.0003

PRO 164 ASN 165 -0.0018

ASN 165 PRO 166 -0.0003

PRO 166 GLU 167 0.0156

GLU 167 ILE 168 0.0003

ILE 168 TYR 169 -0.0127

TYR 169 VAL 170 -0.0001

VAL 170 GLN 171 0.0088

GLN 171 LEU 172 0.0002

LEU 172 ILE 173 0.0125

ILE 173 LYS 174 -0.0000

LYS 174 GLU 175 0.0213

GLU 175 CYS 176 0.0002

CYS 176 LYS 177 -0.0096

LYS 177 SER 178 -0.0002

SER 178 ARG 179 0.0118

ARG 179 GLY 180 -0.0002

GLY 180 LYS 181 0.0007

LYS 181 GLU 182 0.0001

GLU 182 GLY 183 0.0006

GLY 183 GLU 184 -0.0001

GLU 184 PHE 185 0.0087

PHE 185 SER 186 -0.0002

SER 186 THR 187 0.0146

THR 187 CYS 188 -0.0000

CYS 188 PHE 189 0.0169

PHE 189 THR 190 0.0002

THR 190 GLU 191 0.0081

GLU 191 LEU 192 0.0000

LEU 192 GLN 193 -0.0290

GLN 193 ARG 194 0.0004

ARG 194 ARG 194 0.0000

ARG 194 ASP 195 -0.0006

ASP 195 PHE 196 -0.0001

PHE 196 LEU 197 0.0240

LEU 197 ARG 198 -0.0000

ARG 198 ASN 199 0.0054

ASN 199 ARG 200 0.0001

ARG 200 PRO 201 0.0653

PRO 201 THR 202 0.0002

THR 202 LYS 203 0.0446

LYS 203 LEU 204 0.0001

LEU 204 LYS 205 -0.0151

LYS 205 SER 206 0.0004

SER 206 LEU 207 -0.0047

LEU 207 ILE 208 -0.0002

ILE 208 ARG 209 -0.0049

ARG 209 LEU 210 -0.0001

LEU 210 VAL 211 0.0080

VAL 211 LYS 212 -0.0000

LYS 212 HIS 213 -0.0188

HIS 213 TRP 214 0.0000

TRP 214 TYR 215 0.0140

TYR 215 GLN 216 -0.0002

GLN 216 THR 217 -0.0402

THR 217 CYS 218 0.0003

CYS 218 LYS 219 0.0452

LYS 219 LYS 220 -0.0003

LYS 220 THR 221 -0.0165

THR 221 HIS 222 0.0004

HIS 222 GLY 223 0.0509

GLY 223 ASN 224 -0.0002

ASN 224 LYS 225 -0.0064

LYS 225 LEU 226 -0.0000

LEU 226 PRO 227 -0.0903

PRO 227 PRO 228 -0.0000

PRO 228 GLN 229 0.0573

GLN 229 TYR 230 -0.0000

TYR 230 ALA 231 0.0045

ALA 231 LEU 232 0.0004

LEU 232 GLU 233 -0.0128

GLU 233 LEU 234 0.0003

LEU 234 LEU 235 -0.0082

LEU 235 THR 236 -0.0002

THR 236 VAL 237 0.0277

VAL 237 TYR 238 -0.0002

TYR 238 ALA 239 0.0433

ALA 239 TRP 240 -0.0001

TRP 240 GLU 241 0.0089

GLU 241 GLN 242 0.0004

GLN 242 GLY 243 0.0274

GLY 243 SER 244 0.0000

SER 244 ARG 245 0.0169

ARG 245 LYS 246 0.0000

LYS 246 THR 247 -0.0124

THR 247 ASP 248 0.0001

ASP 248 PHE 249 0.0336

PHE 249 SER 250 -0.0002

SER 250 THR 251 -0.0249

THR 251 ALA 252 0.0001

ALA 252 GLN 253 -0.0082

GLN 253 GLY 254 -0.0003

GLY 254 PHE 255 0.0162

PHE 255 GLN 256 0.0004

GLN 256 THR 257 0.0208

THR 257 VAL 258 -0.0002

VAL 258 LEU 259 0.0190

LEU 259 GLU 260 -0.0002

GLU 260 LEU 261 0.0028

LEU 261 VAL 262 0.0001

VAL 262 LEU 263 -0.0012

LEU 263 LYS 264 0.0002

LYS 264 HIS 265 -0.0155

HIS 265 GLN 266 -0.0000

GLN 266 LYS 267 0.0386

LYS 267 LEU 268 -0.0001

LEU 268 CYS 269 0.0638

CYS 269 ILE 270 0.0001

ILE 270 PHE 271 0.0555

PHE 271 TRP 272 0.0003

TRP 272 GLU 273 0.0551

GLU 273 ALA 274 -0.0000

ALA 274 TYR 275 0.0255

TYR 275 TYR 276 -0.0004

TYR 276 ASP 277 -0.0191

ASP 277 PHE 278 0.0002

PHE 278 THR 279 0.0204

THR 279 ASN 280 -0.0002

ASN 280 PRO 281 -0.0194

PRO 281 VAL 282 -0.0003

VAL 282 VAL 283 0.0040

VAL 283 GLY 284 -0.0003

GLY 284 ARG 285 -0.0056

ARG 285 CYS 286 -0.0002

CYS 286 MET 287 0.0169

MET 287 LEU 288 0.0001

LEU 288 GLN 289 0.0034

GLN 289 GLN 290 0.0001

GLN 290 LEU 291 0.0229

LEU 291 LYS 292 0.0003

LYS 292 LYS 293 0.0072

LYS 293 PRO 294 0.0000

PRO 294 ARG 295 -0.0259

ARG 295 PRO 296 -0.0004

PRO 296 VAL 297 -0.0266

VAL 297 ILE 298 0.0000

ILE 298 LEU 299 -0.0194

LEU 299 ASP 300 0.0001

ASP 300 PRO 301 -0.0204

PRO 301 ALA 302 0.0002

ALA 302 ASP 303 0.0293

ASP 303 PRO 304 -0.0002

PRO 304 THR 305 0.0316

THR 305 GLY 306 -0.0001

GLY 306 ASN 307 -0.1245

ASN 307 VAL 308 -0.0006

VAL 308 GLY 309 -0.0637

GLY 309 GLY 310 0.0002

GLY 310 GLY 311 0.0537

GLY 311 ASP 312 0.0002

ASP 312 THR 313 -0.0066

THR 313 HIS 314 0.0001

HIS 314 SER 315 0.0039

SER 315 TRP 316 0.0001

TRP 316 GLN 317 -0.0077

GLN 317 ARG 318 0.0005

ARG 318 LEU 319 0.0030

LEU 319 ALA 320 0.0001

ALA 320 GLN 321 0.0193

GLN 321 GLU 322 0.0002

GLU 322 ALA 323 0.0263

ALA 323 ARG 324 -0.0001

ARG 324 VAL 325 0.0005

VAL 325 TRP 326 0.0004

TRP 326 LEU 327 0.0014

LEU 327 GLY 328 -0.0000

GLY 328 TYR 329 -0.0031

TYR 329 PRO 330 0.0001

PRO 330 CYS 331 0.0062

CYS 331 CYS 332 0.0001

CYS 332 LYS 333 0.0061

LYS 333 ASN 334 -0.0003

ASN 334 LEU 335 0.0303

LEU 335 ASP 336 -0.0002

ASP 336 GLY 337 -0.0410

GLY 337 SER 338 0.0002

SER 338 LEU 339 0.0010

LEU 339 VAL 340 0.0001

VAL 340 GLY 341 0.0246

GLY 341 ALA 342 0.0004

ALA 342 TRP 343 0.0440

TRP 343 THR 344 0.0002

THR 344 MET 345 0.0184

MET 345 LEU 346 0.0003

LEU 346 GLN 347 -0.0001

GLN 347 LYS 348 0.0004

LYS 348 ILE 349 -0.0012

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 22122720180123252

--- normal mode 9 ---

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

* *