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

* *

CA strain for 22122720180123252

--- normal mode 7 ---

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 0.0130

LEU 3 ARG 4 0.0001

ARG 4 HIS 5 -0.0072

HIS 5 THR 6 0.0001

THR 6 PRO 7 -0.0155

PRO 7 ALA 8 -0.0002

ALA 8 ARG 9 -0.0021

ARG 9 ASP 10 0.0003

ASP 10 LEU 11 -0.0020

LEU 11 ASP 12 0.0002

ASP 12 LYS 13 -0.0232

LYS 13 PHE 14 0.0001

PHE 14 ILE 15 0.0146

ILE 15 GLU 16 -0.0004

GLU 16 ASP 17 -0.0012

ASP 17 HIS 18 0.0005

HIS 18 LEU 19 0.0009

LEU 19 LEU 20 0.0001

LEU 20 PRO 21 0.0922

PRO 21 ASN 22 -0.0001

ASN 22 THR 23 0.0637

THR 23 CYS 24 -0.0001

CYS 24 PHE 25 -0.0344

PHE 25 ARG 26 0.0001

ARG 26 THR 27 0.0006

THR 27 GLN 28 0.0003

GLN 28 VAL 29 0.0089

VAL 29 LYS 30 0.0001

LYS 30 GLU 31 0.0376

GLU 31 ALA 32 0.0003

ALA 32 ILE 33 0.0200

ILE 33 ASP 34 0.0001

ASP 34 ILE 35 0.0363

ILE 35 VAL 36 0.0004

VAL 36 CYS 37 0.0116

CYS 37 ARG 38 -0.0001

ARG 38 PHE 39 0.0134

PHE 39 LEU 40 0.0001

LEU 40 LYS 41 -0.0089

LYS 41 GLU 42 0.0004

GLU 42 ARG 43 0.0420

ARG 43 CYS 44 -0.0001

CYS 44 PHE 45 -0.0052

PHE 45 GLN 46 -0.0005

GLN 46 GLY 47 0.0066

GLY 47 THR 48 -0.0002

THR 48 ALA 49 -0.0157

ALA 49 ASP 50 -0.0000

ASP 50 PRO 51 0.0369

PRO 51 VAL 52 0.0000

VAL 52 ARG 53 0.0142

ARG 53 VAL 54 -0.0000

VAL 54 SER 55 0.1604

SER 55 LYS 56 0.0000

LYS 56 VAL 57 -0.0110

VAL 57 VAL 58 -0.0000

VAL 58 LYS 59 -0.0473

LYS 59 GLY 60 0.0003

GLY 60 GLY 61 -0.0234

GLY 61 SER 62 -0.0003

SER 62 SER 63 -0.0408

SER 63 GLY 64 -0.0002

GLY 64 LYS 65 0.0389

LYS 65 GLY 66 -0.0002

GLY 66 THR 67 -0.0487

THR 67 THR 68 0.0004

THR 68 LEU 69 0.0063

LEU 69 ARG 70 0.0003

ARG 70 GLY 71 0.0046

GLY 71 ARG 72 -0.0001

ARG 72 SER 73 -0.0113

SER 73 ASP 74 -0.0002

ASP 74 ALA 75 -0.0775

ALA 75 ASP 76 -0.0001

ASP 76 LEU 77 -0.0348

LEU 77 VAL 78 -0.0004

VAL 78 VAL 79 -0.0309

VAL 79 PHE 80 -0.0002

PHE 80 LEU 81 0.0251

LEU 81 THR 82 -0.0000

THR 82 LYS 83 -0.0095

LYS 83 LEU 84 0.0003

LEU 84 THR 85 0.0212

THR 85 SER 86 -0.0001

SER 86 PHE 87 -0.0035

PHE 87 GLU 88 0.0000

GLU 88 ASP 89 -0.0292

ASP 89 GLN 90 0.0000

GLN 90 LEU 91 -0.0061

LEU 91 ARG 92 -0.0000

ARG 92 ARG 93 -0.0546

ARG 93 ARG 94 0.0002

ARG 94 GLY 95 -0.0082

GLY 95 GLU 96 0.0001

GLU 96 PHE 97 0.0075

PHE 97 ILE 98 -0.0001

ILE 98 GLN 99 -0.0190

GLN 99 GLU 100 -0.0002

GLU 100 ILE 101 0.0043

ILE 101 ARG 102 -0.0000

ARG 102 ARG 103 0.0206

ARG 103 GLN 104 0.0001

GLN 104 LEU 105 -0.0141

LEU 105 GLU 106 0.0002

GLU 106 ALA 107 -0.0025

ALA 107 CYS 108 -0.0005

CYS 108 GLN 109 0.0068

GLN 109 ARG 110 -0.0002

ARG 110 GLU 111 -0.0107

GLU 111 GLN 112 0.0001

GLN 112 LYS 113 0.0135

LYS 113 PHE 114 -0.0002

PHE 114 LYS 115 0.0003

LYS 115 VAL 116 0.0000

VAL 116 THR 117 0.0199

THR 117 PHE 118 -0.0000

PHE 118 GLY 119 -0.0009

GLY 119 VAL 120 -0.0002

VAL 120 GLN 121 0.0202

GLN 121 SER 122 -0.0001

SER 122 PRO 123 0.0209

PRO 123 ARG 124 -0.0002

ARG 124 ARG 125 -0.0309

ARG 125 GLU 126 0.0004

GLU 126 GLY 127 0.0519

GLY 127 PRO 128 0.0000

PRO 128 ARG 129 -0.0275

ARG 129 ALA 130 0.0000

ALA 130 LEU 131 -0.0491

LEU 131 SER 132 0.0003

SER 132 PHE 133 0.0480

PHE 133 VAL 134 -0.0000

VAL 134 LEU 135 0.0076

LEU 135 SER 136 -0.0002

SER 136 SER 137 0.0079

SER 137 PRO 138 0.0001

PRO 138 GLN 139 0.0099

GLN 139 LEU 140 0.0002

LEU 140 GLN 141 -0.0154

GLN 141 GLN 142 0.0003

GLN 142 GLU 143 0.0678

GLU 143 VAL 144 -0.0002

VAL 144 GLU 145 0.0844

GLU 145 PHE 146 -0.0001

PHE 146 ASP 147 0.0389

ASP 147 VAL 148 0.0002

VAL 148 LEU 149 -0.0019

LEU 149 PRO 150 0.0004

PRO 150 ALA 151 0.0136

ALA 151 PHE 152 -0.0003

PHE 152 ASP 153 0.0219

ASP 153 ALA 154 -0.0001

ALA 154 LEU 155 0.0161

LEU 155 GLY 156 -0.0003

GLY 156 GLN 157 0.0087

GLN 157 TRP 158 0.0005

TRP 158 THR 159 0.0213

THR 159 PRO 160 0.0002

PRO 160 GLY 161 -0.0133

GLY 161 TYR 162 -0.0002

TYR 162 LYS 163 0.0054

LYS 163 PRO 164 0.0000

PRO 164 ASN 165 -0.0262

ASN 165 PRO 166 0.0000

PRO 166 GLU 167 0.0036

GLU 167 ILE 168 -0.0001

ILE 168 TYR 169 0.0109

TYR 169 VAL 170 0.0001

VAL 170 GLN 171 0.0624

GLN 171 LEU 172 -0.0002

LEU 172 ILE 173 0.0146

ILE 173 LYS 174 0.0003

LYS 174 GLU 175 -0.0029

GLU 175 CYS 176 0.0001

CYS 176 LYS 177 0.0100

LYS 177 SER 178 0.0003

SER 178 ARG 179 -0.0057

ARG 179 GLY 180 -0.0002

GLY 180 LYS 181 0.0255

LYS 181 GLU 182 -0.0001

GLU 182 GLY 183 0.0249

GLY 183 GLU 184 -0.0000

GLU 184 PHE 185 0.0364

PHE 185 SER 186 -0.0004

SER 186 THR 187 -0.0755

THR 187 CYS 188 0.0002

CYS 188 PHE 189 0.0130

PHE 189 THR 190 0.0002

THR 190 GLU 191 -0.0385

GLU 191 LEU 192 0.0002

LEU 192 GLN 193 -0.0293

GLN 193 ARG 194 0.0003

ARG 194 ARG 194 -0.0000

ARG 194 ASP 195 -0.0167

ASP 195 PHE 196 0.0003

PHE 196 LEU 197 -0.0268

LEU 197 ARG 198 -0.0003

ARG 198 ASN 199 0.0467

ASN 199 ARG 200 0.0001

ARG 200 PRO 201 0.0371

PRO 201 THR 202 0.0000

THR 202 LYS 203 0.0392

LYS 203 LEU 204 0.0001

LEU 204 LYS 205 0.0171

LYS 205 SER 206 0.0001

SER 206 LEU 207 0.0138

LEU 207 ILE 208 0.0003

ILE 208 ARG 209 0.0025

ARG 209 LEU 210 -0.0001

LEU 210 VAL 211 0.0262

VAL 211 LYS 212 -0.0003

LYS 212 HIS 213 0.0133

HIS 213 TRP 214 -0.0001

TRP 214 TYR 215 0.0229

TYR 215 GLN 216 -0.0001

GLN 216 THR 217 -0.0156

THR 217 CYS 218 -0.0000

CYS 218 LYS 219 -0.0022

LYS 219 LYS 220 -0.0001

LYS 220 THR 221 -0.0002

THR 221 HIS 222 0.0004

HIS 222 GLY 223 -0.0243

GLY 223 ASN 224 0.0002

ASN 224 LYS 225 0.0287

LYS 225 LEU 226 -0.0001

LEU 226 PRO 227 -0.0093

PRO 227 PRO 228 -0.0002

PRO 228 GLN 229 0.0426

GLN 229 TYR 230 0.0001

TYR 230 ALA 231 -0.0175

ALA 231 LEU 232 -0.0003

LEU 232 GLU 233 -0.0249

GLU 233 LEU 234 0.0002

LEU 234 LEU 235 -0.0105

LEU 235 THR 236 -0.0000

THR 236 VAL 237 0.0265

VAL 237 TYR 238 0.0002

TYR 238 ALA 239 0.0184

ALA 239 TRP 240 0.0003

TRP 240 GLU 241 -0.0087

GLU 241 GLN 242 0.0001

GLN 242 GLY 243 0.0035

GLY 243 SER 244 -0.0002

SER 244 ARG 245 0.0235

ARG 245 LYS 246 0.0003

LYS 246 THR 247 -0.0062

THR 247 ASP 248 -0.0002

ASP 248 PHE 249 0.0314

PHE 249 SER 250 -0.0002

SER 250 THR 251 -0.0215

THR 251 ALA 252 -0.0002

ALA 252 GLN 253 -0.0137

GLN 253 GLY 254 0.0003

GLY 254 PHE 255 0.0073

PHE 255 GLN 256 0.0001

GLN 256 THR 257 0.0054

THR 257 VAL 258 -0.0001

VAL 258 LEU 259 0.0205

LEU 259 GLU 260 -0.0002

GLU 260 LEU 261 -0.0010

LEU 261 VAL 262 -0.0000

VAL 262 LEU 263 0.0005

LEU 263 LYS 264 -0.0001

LYS 264 HIS 265 -0.0158

HIS 265 GLN 266 0.0000

GLN 266 LYS 267 0.0370

LYS 267 LEU 268 -0.0001

LEU 268 CYS 269 0.0646

CYS 269 ILE 270 0.0000

ILE 270 PHE 271 0.1010

PHE 271 TRP 272 0.0004

TRP 272 GLU 273 0.0522

GLU 273 ALA 274 -0.0001

ALA 274 TYR 275 0.0341

TYR 275 TYR 276 0.0002

TYR 276 ASP 277 -0.0051

ASP 277 PHE 278 -0.0001

PHE 278 THR 279 0.0330

THR 279 ASN 280 0.0000

ASN 280 PRO 281 0.0011

PRO 281 VAL 282 0.0001

VAL 282 VAL 283 -0.0086

VAL 283 GLY 284 -0.0002

GLY 284 ARG 285 -0.0159

ARG 285 CYS 286 0.0001

CYS 286 MET 287 -0.0170

MET 287 LEU 288 -0.0002

LEU 288 GLN 289 -0.0167

GLN 289 GLN 290 0.0002

GLN 290 LEU 291 -0.0751

LEU 291 LYS 292 0.0002

LYS 292 LYS 293 0.0645

LYS 293 PRO 294 -0.0000

PRO 294 ARG 295 -0.0226

ARG 295 PRO 296 -0.0001

PRO 296 VAL 297 0.0091

VAL 297 ILE 298 -0.0001

ILE 298 LEU 299 -0.0032

LEU 299 ASP 300 0.0001

ASP 300 PRO 301 0.0021

PRO 301 ALA 302 -0.0002

ALA 302 ASP 303 0.0179

ASP 303 PRO 304 0.0003

PRO 304 THR 305 -0.0184

THR 305 GLY 306 -0.0000

GLY 306 ASN 307 -0.1364

ASN 307 VAL 308 0.0003

VAL 308 GLY 309 -0.0648

GLY 309 GLY 310 -0.0001

GLY 310 GLY 311 0.0490

GLY 311 ASP 312 0.0001

ASP 312 THR 313 -0.0177

THR 313 HIS 314 0.0001

HIS 314 SER 315 -0.0131

SER 315 TRP 316 0.0003

TRP 316 GLN 317 -0.0076

GLN 317 ARG 318 -0.0001

ARG 318 LEU 319 -0.0019

LEU 319 ALA 320 -0.0003

ALA 320 GLN 321 0.0016

GLN 321 GLU 322 -0.0002

GLU 322 ALA 323 0.0087

ALA 323 ARG 324 -0.0004

ARG 324 VAL 325 -0.0022

VAL 325 TRP 326 -0.0002

TRP 326 LEU 327 -0.0089

LEU 327 GLY 328 0.0000

GLY 328 TYR 329 0.0027

TYR 329 PRO 330 0.0001

PRO 330 CYS 331 -0.0015

CYS 331 CYS 332 -0.0001

CYS 332 LYS 333 -0.0012

LYS 333 ASN 334 0.0001

ASN 334 LEU 335 0.0067

LEU 335 ASP 336 0.0001

ASP 336 GLY 337 -0.0219

GLY 337 SER 338 0.0000

SER 338 LEU 339 -0.0002

LEU 339 VAL 340 -0.0001

VAL 340 GLY 341 0.0000

GLY 341 ALA 342 -0.0001

ALA 342 TRP 343 0.0234

TRP 343 THR 344 0.0005

THR 344 MET 345 -0.0089

MET 345 LEU 346 0.0002

LEU 346 GLN 347 0.0020

GLN 347 LYS 348 -0.0002

LYS 348 ILE 349 -0.0003

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 7 ---

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

* *