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

* *

CA strain for 22122720105119216

--- 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 0.0003

GLU 2 LEU 3 0.0062

LEU 3 ARG 4 -0.0003

ARG 4 HIS 5 0.0032

HIS 5 THR 6 0.0000

THR 6 PRO 7 0.0132

PRO 7 ALA 8 0.0002

ALA 8 ARG 9 -0.0217

ARG 9 ASP 10 -0.0004

ASP 10 LEU 11 0.0150

LEU 11 ASP 12 0.0001

ASP 12 LYS 13 -0.0388

LYS 13 PHE 14 -0.0002

PHE 14 ILE 15 0.0239

ILE 15 GLU 16 -0.0001

GLU 16 ASP 17 -0.0255

ASP 17 HIS 18 -0.0003

HIS 18 LEU 19 0.0205

LEU 19 LEU 20 -0.0002

LEU 20 PRO 21 0.0281

PRO 21 ASN 22 -0.0002

ASN 22 THR 23 0.0085

THR 23 CYS 24 0.0000

CYS 24 PHE 25 -0.0383

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 -0.0004

LYS 30 GLU 31 0.0134

GLU 31 ALA 32 -0.0002

ALA 32 ILE 33 0.0193

ILE 33 ASP 34 -0.0002

ASP 34 ILE 35 0.0066

ILE 35 VAL 36 -0.0002

VAL 36 CYS 37 0.0204

CYS 37 ARG 38 -0.0003

ARG 38 PHE 39 -0.0065

PHE 39 LEU 40 0.0003

LEU 40 LYS 41 0.0014

LYS 41 GLU 42 0.0001

GLU 42 ARG 43 0.0206

ARG 43 CYS 44 0.0001

CYS 44 PHE 45 0.0108

PHE 45 GLN 46 0.0003

GLN 46 GLY 47 -0.0154

GLY 47 THR 48 -0.0002

THR 48 ALA 49 0.0707

ALA 49 ASP 50 -0.0001

ASP 50 PRO 51 -0.0551

PRO 51 VAL 52 0.0003

VAL 52 ARG 53 -0.0385

ARG 53 VAL 54 0.0002

VAL 54 SER 55 -0.0391

SER 55 LYS 56 0.0000

LYS 56 VAL 57 0.0293

VAL 57 VAL 58 -0.0000

VAL 58 LYS 59 0.0049

LYS 59 GLY 60 -0.0000

GLY 60 GLY 61 0.0195

GLY 61 SER 62 0.0001

SER 62 SER 63 -0.0488

SER 63 GLY 64 0.0003

GLY 64 LYS 65 -0.0150

LYS 65 GLY 66 0.0001

GLY 66 THR 67 0.0062

THR 67 THR 68 -0.0001

THR 68 LEU 69 0.0465

LEU 69 ARG 70 0.0001

ARG 70 GLY 71 0.0522

GLY 71 ARG 72 -0.0001

ARG 72 SER 73 0.0590

SER 73 ASP 74 -0.0000

ASP 74 ALA 75 0.0245

ALA 75 ASP 76 -0.0001

ASP 76 LEU 77 0.0192

LEU 77 VAL 78 0.0002

VAL 78 VAL 79 -0.0145

VAL 79 PHE 80 -0.0001

PHE 80 LEU 81 -0.0425

LEU 81 THR 82 0.0000

THR 82 LYS 83 -0.0037

LYS 83 LEU 84 -0.0002

LEU 84 THR 85 -0.0009

THR 85 SER 86 -0.0001

SER 86 PHE 87 0.0102

PHE 87 GLU 88 -0.0000

GLU 88 ASP 89 0.0185

ASP 89 GLN 90 0.0001

GLN 90 LEU 91 0.0115

LEU 91 ARG 92 0.0005

ARG 92 ARG 93 0.0065

ARG 93 ARG 94 -0.0002

ARG 94 GLY 95 -0.0150

GLY 95 GLU 96 0.0001

GLU 96 PHE 97 0.0060

PHE 97 ILE 98 0.0001

ILE 98 GLN 99 -0.0066

GLN 99 GLU 100 -0.0004

GLU 100 ILE 101 -0.0003

ILE 101 ARG 102 -0.0005

ARG 102 ARG 103 0.0437

ARG 103 GLN 104 -0.0003

GLN 104 LEU 105 0.0037

LEU 105 GLU 106 -0.0002

GLU 106 ALA 107 0.0199

ALA 107 CYS 108 -0.0002

CYS 108 GLN 109 0.0119

GLN 109 ARG 110 -0.0001

ARG 110 GLU 111 -0.0018

GLU 111 GLN 112 0.0002

GLN 112 LYS 113 0.0051

LYS 113 PHE 114 0.0003

PHE 114 LYS 115 0.0026

LYS 115 VAL 116 0.0000

VAL 116 THR 117 0.0055

THR 117 PHE 118 -0.0000

PHE 118 GLU 119 0.0563

GLU 119 VAL 120 -0.0002

VAL 120 GLN 121 0.0058

GLN 121 SER 122 0.0001

SER 122 PRO 123 -0.0578

PRO 123 ARG 124 0.0001

ARG 124 ARG 125 -0.0494

ARG 125 GLU 126 0.0003

GLU 126 ASN 127 0.0755

ASN 127 PRO 128 -0.0002

PRO 128 ARG 129 0.0102

ARG 129 ALA 130 -0.0004

ALA 130 LEU 131 -0.1197

LEU 131 SER 132 -0.0002

SER 132 PHE 133 -0.0327

PHE 133 VAL 134 -0.0001

VAL 134 LEU 135 -0.0290

LEU 135 SER 136 0.0001

SER 136 SER 137 -0.0193

SER 137 PRO 138 -0.0004

PRO 138 GLN 139 0.0015

GLN 139 LEU 140 0.0000

LEU 140 GLN 141 0.0150

GLN 141 GLN 142 0.0002

GLN 142 GLU 143 -0.0120

GLU 143 VAL 144 0.0001

VAL 144 GLU 145 -0.0199

GLU 145 PHE 146 0.0003

PHE 146 ASP 147 0.0078

ASP 147 VAL 148 -0.0004

VAL 148 LEU 149 0.0069

LEU 149 PRO 150 0.0000

PRO 150 ALA 151 -0.0246

ALA 151 PHE 152 -0.0004

PHE 152 ASP 153 -0.0228

ASP 153 ALA 154 0.0002

ALA 154 LEU 155 -0.0271

LEU 155 GLY 156 0.0004

GLY 156 GLN 157 -0.0300

GLN 157 TRP 158 0.0002

TRP 158 THR 159 -0.0120

THR 159 PRO 160 0.0002

PRO 160 GLY 161 0.0090

GLY 161 TYR 162 0.0000

TYR 162 LYS 163 -0.0135

LYS 163 PRO 164 0.0001

PRO 164 ASN 165 0.0453

ASN 165 PRO 166 -0.0001

PRO 166 GLU 167 -0.0065

GLU 167 ILE 168 0.0002

ILE 168 TYR 169 -0.0063

TYR 169 VAL 170 -0.0000

VAL 170 GLN 171 -0.0028

GLN 171 LEU 172 -0.0002

LEU 172 ILE 173 0.0130

ILE 173 LYS 174 0.0002

LYS 174 GLU 175 -0.0042

GLU 175 CYS 176 0.0001

CYS 176 LYS 177 0.0010

LYS 177 SER 178 0.0000

SER 178 ARG 179 -0.0056

ARG 179 GLY 180 0.0000

GLY 180 LYS 181 -0.0063

LYS 181 GLU 182 0.0000

GLU 182 GLY 183 -0.0118

GLY 183 GLU 184 -0.0001

GLU 184 PHE 185 -0.0058

PHE 185 SER 186 0.0003

SER 186 THR 187 -0.0417

THR 187 CYS 188 0.0001

CYS 188 PHE 189 -0.0252

PHE 189 THR 190 0.0000

THR 190 GLU 191 0.0296

GLU 191 LEU 192 0.0001

LEU 192 GLN 193 -0.0023

GLN 193 ARG 194 -0.0002

ARG 194 ARG 194 0.0000

ARG 194 ASP 195 0.0251

ASP 195 PHE 196 0.0002

PHE 196 LEU 197 0.0716

LEU 197 ARG 198 0.0004

ARG 198 ASN 199 -0.0203

ASN 199 ARG 200 -0.0001

ARG 200 PRO 201 0.0690

PRO 201 THR 202 -0.0002

THR 202 LYS 203 0.0632

LYS 203 LEU 204 0.0001

LEU 204 LYS 205 -0.0514

LYS 205 SER 206 -0.0002

SER 206 LEU 207 0.0316

LEU 207 ILE 208 0.0003

ILE 208 ARG 209 0.0174

ARG 209 LEU 210 -0.0003

LEU 210 VAL 211 -0.0028

VAL 211 LYS 212 -0.0000

LYS 212 HIS 213 0.0526

HIS 213 TRP 214 0.0002

TRP 214 TYR 215 0.0007

TYR 215 GLN 216 0.0000

GLN 216 THR 217 0.0293

THR 217 CYS 218 -0.0000

CYS 218 LYS 219 0.0165

LYS 219 LYS 220 -0.0006

LYS 220 THR 221 -0.0049

THR 221 HIS 222 0.0004

HIS 222 GLY 223 0.0126

GLY 223 ASN 224 0.0002

ASN 224 LYS 225 0.0226

LYS 225 LEU 226 0.0001

LEU 226 PRO 227 0.0091

PRO 227 PRO 228 0.0004

PRO 228 GLN 229 -0.0163

GLN 229 TYR 230 0.0001

TYR 230 ALA 231 -0.0181

ALA 231 LEU 232 -0.0000

LEU 232 GLU 233 -0.0245

GLU 233 LEU 234 -0.0004

LEU 234 LEU 235 -0.0531

LEU 235 THR 236 0.0001

THR 236 VAL 237 -0.0929

VAL 237 TYR 238 0.0000

TYR 238 ALA 239 -0.0068

ALA 239 TRP 240 -0.0003

TRP 240 GLU 241 -0.1036

GLU 241 GLN 242 -0.0003

GLN 242 GLY 243 -0.0010

GLY 243 SER 244 -0.0003

SER 244 ARG 245 0.0607

ARG 245 LYS 246 -0.0001

LYS 246 THR 247 -0.0433

THR 247 ASP 248 0.0000

ASP 248 PHE 249 0.0394

PHE 249 SER 250 0.0000

SER 250 THR 251 -0.0149

THR 251 ALA 252 -0.0001

ALA 252 GLN 253 0.0012

GLN 253 GLY 254 0.0001

GLY 254 PHE 255 -0.0006

PHE 255 GLN 256 0.0004

GLN 256 THR 257 0.0388

THR 257 VAL 258 0.0001

VAL 258 LEU 259 0.0549

LEU 259 GLU 260 0.0004

GLU 260 LEU 261 -0.0287

LEU 261 VAL 262 0.0002

VAL 262 LEU 263 0.0329

LEU 263 LYS 264 -0.0001

LYS 264 HIS 265 -0.0271

HIS 265 GLN 266 0.0002

GLN 266 LYS 267 0.0626

LYS 267 LEU 268 -0.0000

LEU 268 CYS 269 -0.0682

CYS 269 ILE 270 0.0001

ILE 270 PHE 271 -0.0918

PHE 271 TRP 272 -0.0001

TRP 272 GLU 273 0.0426

GLU 273 ALA 274 -0.0003

ALA 274 TYR 275 -0.0449

TYR 275 TYR 276 0.0002

TYR 276 ASP 277 0.0347

ASP 277 PHE 278 0.0002

PHE 278 THR 279 -0.0153

THR 279 ASN 280 -0.0002

ASN 280 PRO 281 0.0084

PRO 281 VAL 282 0.0001

VAL 282 VAL 283 0.0197

VAL 283 GLY 284 -0.0002

GLY 284 ARG 285 0.0084

ARG 285 CYS 286 0.0001

CYS 286 MET 287 0.0421

MET 287 LEU 288 0.0003

LEU 288 GLN 289 0.0340

GLN 289 GLN 290 -0.0001

GLN 290 LEU 291 0.0324

LEU 291 LYS 292 -0.0001

LYS 292 LYS 293 0.0162

LYS 293 PRO 294 0.0002

PRO 294 ARG 295 -0.0366

ARG 295 PRO 296 -0.0000

PRO 296 VAL 297 -0.0451

VAL 297 ILE 298 -0.0001

ILE 298 LEU 299 -0.0559

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 0.0003

PRO 304 THR 305 0.0080

THR 305 GLY 306 0.0002

GLY 306 ASN 307 -0.0630

ASN 307 VAL 308 0.0003

VAL 308 GLY 309 -0.0514

GLY 309 GLY 310 -0.0001

GLY 310 GLY 311 0.0201

GLY 311 ASP 312 -0.0003

ASP 312 THR 313 -0.0020

THR 313 HIS 314 -0.0004

HIS 314 SER 315 -0.0142

SER 315 TRP 316 0.0002

TRP 316 GLN 317 -0.0106

GLN 317 ARG 318 -0.0002

ARG 318 LEU 319 0.0156

LEU 319 ALA 320 0.0001

ALA 320 GLN 321 0.0162

GLN 321 GLU 322 0.0001

GLU 322 ALA 323 0.0415

ALA 323 ARG 324 0.0002

ARG 324 VAL 325 -0.0204

VAL 325 TRP 326 -0.0001

TRP 326 LEU 327 0.0140

LEU 327 GLY 328 -0.0003

GLY 328 TYR 329 -0.0075

TYR 329 PRO 330 -0.0000

PRO 330 CYS 331 0.0033

CYS 331 CYS 332 0.0000

CYS 332 LYS 333 -0.0123

LYS 333 ASN 334 -0.0002

ASN 334 LEU 335 -0.0373

LEU 335 ASP 336 0.0003

ASP 336 GLY 337 -0.0126

GLY 337 SER 338 -0.0001

SER 338 LEU 339 -0.0282

LEU 339 VAL 340 -0.0002

VAL 340 GLY 341 -0.0193

GLY 341 ALA 342 0.0001

ALA 342 TRP 343 0.0175

TRP 343 THR 344 0.0003

THR 344 MET 345 0.0090

MET 345 LEU 346 0.0000

LEU 346 GLN 347 0.0048

GLN 347 LYS 348 0.0003

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 22122720105119216

--- normal mode 11 ---

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

* *