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

* *

CA strain for 230101190352136506

--- normal mode 20 ---

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
PHE 1 ASP 2 -0.0001

ASP 2 MET 3 0.0433

MET 3 ILE 4 -0.0002

ILE 4 ARG 5 0.0126

ARG 5 LEU 6 0.0002

LEU 6 ALA 7 -0.0422

ALA 7 THR 8 -0.0002

THR 8 ASN 9 -0.0772

ASN 9 LYS 10 -0.0002

LYS 10 PHE 11 0.0251

PHE 11 SER 12 -0.0003

SER 12 GLU 13 0.0021

GLU 13 ASP 14 0.0002

ASP 14 ASN 15 -0.0645

ASN 15 LYS 16 0.0001

LYS 16 ILE 17 -0.0596

ILE 17 GLY 18 0.0003

GLY 18 GLU 19 0.3948

GLU 19 GLY 20 0.0003

GLY 20 GLY 21 0.0606

GLY 21 PHE 22 0.0004

PHE 22 GLY 23 0.2049

GLY 23 ASP 24 0.0003

ASP 24 VAL 25 0.1821

VAL 25 TYR 26 -0.0001

TYR 26 LYS 27 0.2275

LYS 27 GLY 28 -0.0000

GLY 28 MET 29 0.2333

MET 29 PHE 30 -0.0002

PHE 30 PRO 31 0.0000

PRO 31 ASN 32 0.0003

ASN 32 GLY 33 0.1545

GLY 33 TYR 34 -0.0003

TYR 34 GLU 35 0.1374

GLU 35 ILE 36 0.0001

ILE 36 ALA 37 0.1400

ALA 37 VAL 38 0.0004

VAL 38 LYS 39 0.0817

LYS 39 ARG 40 0.0002

ARG 40 LEU 41 0.2850

LEU 41 ILE 42 0.0001

ILE 42 ARG 43 -0.1474

ARG 43 ASN 44 -0.0001

ASN 44 SER 45 0.2851

SER 45 SER 46 0.0006

SER 46 GLN 47 -0.1656

GLN 47 GLY 48 -0.0004

GLY 48 ALA 49 -0.1988

ALA 49 VAL 50 -0.0003

VAL 50 GLU 51 0.0947

GLU 51 PHE 52 -0.0004

PHE 52 LYS 53 0.0429

LYS 53 ASN 54 0.0001

ASN 54 GLU 55 -0.0360

GLU 55 VAL 56 -0.0002

VAL 56 LEU 57 0.0591

LEU 57 LEU 58 0.0001

LEU 58 ILE 59 -0.1142

ILE 59 ALA 60 -0.0003

ALA 60 LYS 61 -0.0027

LYS 61 LEU 62 0.0005

LEU 62 GLN 63 -0.0338

GLN 63 HIS 64 -0.0001

HIS 64 ARG 65 0.0284

ARG 65 ASN 66 -0.0002

ASN 66 LEU 67 0.0209

LEU 67 VAL 68 0.0003

VAL 68 ARG 69 0.0856

ARG 69 LEU 70 -0.0005

LEU 70 LEU 71 -0.1755

LEU 71 GLY 72 0.0004

GLY 72 PHE 73 0.0287

PHE 73 CYS 74 0.0003

CYS 74 ILE 75 0.0063

ILE 75 GLN 76 0.0003

GLN 76 ARG 77 0.0347

ARG 77 ASN 78 -0.0002

ASN 78 GLU 79 0.0130

GLU 79 LYS 80 0.0000

LYS 80 ILE 81 -0.0421

ILE 81 LEU 82 -0.0003

LEU 82 ILE 83 -0.0277

ILE 83 TYR 84 -0.0001

TYR 84 GLU 85 0.0937

GLU 85 TYR 86 -0.0002

TYR 86 MET 87 0.0379

MET 87 HIS 88 -0.0003

HIS 88 ASN 89 0.1056

ASN 89 LYS 90 0.0001

LYS 90 SER 91 0.0095

SER 91 LEU 92 -0.0002

LEU 92 ASP 93 0.0344

ASP 93 TYR 94 0.0002

TYR 94 TYR 95 -0.0167

TYR 95 LEU 96 -0.0002

LEU 96 PHE 97 0.0081

PHE 97 SER 98 -0.0002

SER 98 PRO 99 0.0079

PRO 99 GLU 100 -0.0001

GLU 100 ASN 101 -0.0178

ASN 101 HIS 102 -0.0005

HIS 102 ARG 103 0.0170

ARG 103 LYS 104 0.0003

LYS 104 LEU 105 -0.0589

LEU 105 THR 106 -0.0002

THR 106 TRP 107 -0.0669

TRP 107 HIS 108 -0.0002

HIS 108 ALA 109 0.0282

ALA 109 ARG 110 0.0001

ARG 110 TYR 111 -0.0439

TYR 111 LYS 112 0.0001

LYS 112 ILE 113 0.0071

ILE 113 ILE 114 -0.0001

ILE 114 ARG 115 0.0164

ARG 115 GLY 116 0.0002

GLY 116 ILE 117 -0.0096

ILE 117 ALA 118 -0.0002

ALA 118 ARG 119 -0.0213

ARG 119 GLY 120 -0.0003

GLY 120 ILE 121 -0.0379

ILE 121 LEU 122 -0.0002

LEU 122 TYR 123 -0.0257

TYR 123 LEU 124 -0.0003

LEU 124 HIS 125 -0.0499

HIS 125 GLU 126 -0.0001

GLU 126 ASP 127 -0.0208

ASP 127 SER 128 0.0001

SER 128 HIS 129 0.0041

HIS 129 LEU 130 -0.0004

LEU 130 LYS 131 -0.0089

LYS 131 ILE 132 0.0001

ILE 132 ILE 133 -0.0295

ILE 133 HIS 134 0.0000

HIS 134 CYS 135 -0.0271

CYS 135 ASP 136 0.0003

ASP 136 LEU 137 -0.0037

LEU 137 LYS 138 0.0002

LYS 138 PRO 139 0.0130

PRO 139 SER 140 0.0001

SER 140 ASN 141 0.0222

ASN 141 ILE 142 0.0001

ILE 142 LEU 143 -0.0250

LEU 143 LEU 144 -0.0001

LEU 144 ASP 145 0.0370

ASP 145 ASP 146 -0.0004

ASP 146 LYS 147 -0.0064

LYS 147 MET 148 0.0001

MET 148 ASN 149 0.0292

ASN 149 ALA 150 0.0000

ALA 150 LYS 151 0.0442

LYS 151 ILE 152 0.0004

ILE 152 SER 153 0.0333

SER 153 ASP 154 0.0001

ASP 154 PHE 155 0.0749

PHE 155 GLY 156 -0.0000

GLY 156 LEU 157 -0.0491

LEU 157 ALA 158 0.0001

ALA 158 ARG 159 0.0014

ARG 159 ILE 160 0.0002

ILE 160 VAL 161 -0.0346

VAL 161 ALA 162 0.0002

ALA 162 ILE 163 0.0125

ILE 163 ASP 164 0.0003

ASP 164 GLN 165 -0.0207

GLN 165 MET 166 -0.0003

MET 166 GLN 167 -0.0658

GLN 167 GLY 168 -0.0001

GLY 168 ASN 169 -0.0812

ASN 169 THR 170 -0.0002

THR 170 SER 171 -0.1721

SER 171 ILE 172 -0.0002

ILE 172 ILE 173 -0.0041

ILE 173 ALA 174 -0.0003

ALA 174 GLY 175 -0.0198

GLY 175 THR 176 -0.0004

THR 176 TYR 177 0.0200

TYR 177 GLY 178 0.0001

GLY 178 TYR 179 0.0325

TYR 179 MET 180 -0.0001

MET 180 SER 181 0.0213

SER 181 PRO 182 0.0001

PRO 182 GLU 183 -0.0311

GLU 183 TYR 184 -0.0003

TYR 184 ALA 185 -0.0544

ALA 185 MET 186 0.0004

MET 186 LEU 187 -0.0681

LEU 187 GLY 188 -0.0001

GLY 188 GLN 189 -0.0278

GLN 189 PHE 190 0.0001

PHE 190 SER 191 -0.0312

SER 191 VAL 192 0.0002

VAL 192 LYS 193 -0.0572

LYS 193 SER 194 -0.0002

SER 194 ASP 195 -0.0261

ASP 195 VAL 196 0.0000

VAL 196 PHE 197 -0.0148

PHE 197 SER 198 0.0003

SER 198 PHE 199 -0.0039

PHE 199 GLY 200 0.0001

GLY 200 VAL 201 0.0036

VAL 201 ILE 202 -0.0004

ILE 202 MET 203 0.0035

MET 203 LEU 204 -0.0002

LEU 204 GLU 205 0.0179

GLU 205 ILE 206 0.0003

ILE 206 VAL 207 0.0050

VAL 207 SER 208 0.0002

SER 208 GLY 209 -0.0040

GLY 209 LYS 210 -0.0002

LYS 210 ARG 211 -0.0841

ARG 211 ASN 212 0.0000

ASN 212 VAL 213 0.0123

VAL 213 ASP 214 0.0001

ASP 214 TYR 215 0.0817

TYR 215 ASN 216 -0.0001

ASN 216 GLY 217 -0.1348

GLY 217 VAL 218 -0.0000

VAL 218 ASN 219 -0.0188

ASN 219 SER 220 -0.0003

SER 220 ILE 221 -0.0137

ILE 221 ASP 222 0.0001

ASP 222 ASP 223 0.0292

ASP 223 LEU 224 -0.0002

LEU 224 VAL 225 0.0022

VAL 225 SER 226 0.0000

SER 226 HIS 227 0.0083

HIS 227 ALA 228 -0.0002

ALA 228 TRP 229 0.0182

TRP 229 LYS 230 0.0000

LYS 230 LYS 231 -0.0022

LYS 231 TRP 232 -0.0001

TRP 232 THR 233 -0.0003

THR 233 GLU 234 -0.0001

GLU 234 ASN 235 -0.0009

ASN 235 LYS 236 0.0004

LYS 236 GLN 237 0.0060

GLN 237 MET 238 0.0000

MET 238 GLU 239 0.0035

GLU 239 LEU 240 -0.0000

LEU 240 LEU 241 0.0285

LEU 241 ASP 242 0.0003

ASP 242 PRO 243 -0.0047

PRO 243 ALA 244 0.0001

ALA 244 LEU 245 -0.0172

LEU 245 THR 246 0.0001

THR 246 TYR 247 -0.0207

TYR 247 SER 248 0.0002

SER 248 PHE 249 -0.0240

PHE 249 SER 250 -0.0001

SER 250 GLU 251 0.0037

GLU 251 THR 252 -0.0005

THR 252 GLU 253 0.0055

GLU 253 VAL 254 -0.0001

VAL 254 SER 255 -0.0064

SER 255 ARG 256 0.0000

ARG 256 CYS 257 0.0013

CYS 257 ILE 258 0.0001

ILE 258 GLN 259 0.0032

GLN 259 LEU 260 0.0004

LEU 260 GLY 261 0.0118

GLY 261 LEU 262 0.0000

LEU 262 LEU 263 -0.0077

LEU 263 CYS 264 0.0000

CYS 264 VAL 265 -0.0134

VAL 265 GLN 266 -0.0000

GLN 266 GLU 267 0.0183

GLU 267 ASN 268 0.0000

ASN 268 PRO 269 -0.0412

PRO 269 ASP 270 0.0000

ASP 270 GLN 271 0.0067

GLN 271 ARG 272 0.0003

ARG 272 PRO 273 -0.0413

PRO 273 THR 274 -0.0004

THR 274 MET 275 -0.0509

MET 275 ALA 276 -0.0002

ALA 276 THR 277 -0.0111

THR 277 ILE 278 -0.0004

ILE 278 ALA 279 -0.0071

ALA 279 LEU 280 0.0002

LEU 280 TYR 281 -0.0011

TYR 281 PHE 282 0.0002

PHE 282 ASN 283 -0.0048

ASN 283 ILE 284 -0.0003

ILE 284 ASP 285 0.0069

ASP 285 SER 286 -0.0000

SER 286 ILE 287 -0.0009

ILE 287 ASP 288 -0.0001

ASP 288 LEU 289 0.0077

LEU 289 PRO 290 -0.0001

PRO 290 LEU 291 -0.0133

LEU 291 PRO 292 -0.0002

PRO 292 GLN 293 -0.0080

GLN 293 GLN 294 -0.0002

GLN 294 PRO 295 0.0118

PRO 295 PRO 296 -0.0001

PRO 296 PHE 297 -0.0607

PHE 297 TYR 298 -0.0003

TYR 298 MET 299 -0.0104

MET 299 ARG 300 0.0002

ARG 300 GLY 301 0.0161

GLY 301 LYS 302 0.0000

LYS 302 ILE 303 0.0122

ILE 303 GLU 304 0.0002

GLU 304 SER 305 -0.0417

SER 305 LYS 306 0.0003

LYS 306 VAL 307 0.0344

VAL 307 ALA 308 0.0000

ALA 308 SER 309 -0.1761

SER 309 LYS 310 -0.0000

LYS 310 LYS 311 -0.1491

LYS 311 THR 312 0.0003

THR 312 MET 313 -0.1522

MET 313 SER 314 0.0000

SER 314 GLY 315 0.3408

GLY 315 ARG 316 -0.0000

ARG 316 PRO 317 -0.2449

PRO 317 ARG 318 -0.0001

ARG 318 SER 319 0.1859

SER 319 TYR 320 -0.0000

TYR 320 SER 321 0.2826

SER 321 VAL 322 -0.0000

VAL 322 THR 323 -0.0051

THR 323 ARG 324 -0.0001

ARG 324 PHE 325 -0.8087

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 230101190352136506

--- normal mode 20 ---

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

* *