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

* *

CA strain for 22022413193125998

--- 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
ARG 79 PRO 80 0.0003

PRO 80 GLU 81 -0.2214

GLU 81 ASP 82 0.0000

ASP 82 LEU 83 -0.0260

LEU 83 GLY 84 0.0001

GLY 84 THR 85 -0.0654

THR 85 GLY 86 0.0001

GLY 86 LEU 87 0.0055

LEU 87 LEU 88 -0.0001

LEU 88 GLU 89 -0.1198

GLU 89 ALA 90 -0.0001

ALA 90 LEU 91 0.0565

LEU 91 LEU 92 0.0001

LEU 92 ARG 93 -0.0894

ARG 93 GLY 94 -0.0000

GLY 94 ASP 95 -0.0553

ASP 95 LEU 96 -0.0001

LEU 96 ALA 97 0.1068

ALA 97 GLY 98 0.0001

GLY 98 ALA 99 0.0099

ALA 99 GLU 100 0.0004

GLU 100 ALA 101 0.0325

ALA 101 LEU 102 -0.0002

LEU 102 PHE 103 0.1282

PHE 103 ARG 104 0.0002

ARG 104 ARG 105 -0.2848

ARG 105 GLY 106 -0.0002

GLY 106 LEU 107 0.2145

LEU 107 ARG 108 0.0000

ARG 108 PHE 109 -0.0498

PHE 109 TRP 110 -0.0002

TRP 110 GLY 111 0.1941

GLY 111 PRO 112 0.0002

PRO 112 GLU 113 0.1109

GLU 113 GLY 114 -0.0001

GLY 114 VAL 115 0.0133

VAL 115 LEU 116 0.0003

LEU 116 GLU 117 0.0499

GLU 117 HIS 118 0.0001

HIS 118 LEU 119 -0.0620

LEU 119 LEU 120 -0.0004

LEU 120 LEU 121 0.0732

LEU 121 PRO 122 0.0002

PRO 122 VAL 123 -0.0166

VAL 123 LEU 124 0.0001

LEU 124 ARG 125 -0.0254

ARG 125 GLU 126 0.0000

GLU 126 VAL 127 0.1297

VAL 127 GLY 128 -0.0001

GLY 128 GLU 129 -0.0289

GLU 129 ALA 130 0.0006

ALA 130 TRP 131 0.0442

TRP 131 HIS 132 0.0001

HIS 132 ARG 133 0.0202

ARG 133 GLY 134 -0.0000

GLY 134 GLU 135 -0.1145

GLU 135 ILE 136 -0.0000

ILE 136 GLY 137 0.3971

GLY 137 VAL 138 -0.0003

VAL 138 ALA 139 -0.0642

ALA 139 GLU 140 0.0000

GLU 140 GLU 141 -0.3227

GLU 141 HIS 142 -0.0004

HIS 142 LEU 143 -0.2549

LEU 143 ALA 144 0.0003

ALA 144 SER 145 -0.2595

SER 145 THR 146 0.0000

THR 146 PHE 147 -0.0444

PHE 147 LEU 148 -0.0002

LEU 148 ARG 149 0.0530

ARG 149 ALA 150 -0.0003

ALA 150 ARG 151 -0.1034

ARG 151 LEU 152 0.0001

LEU 152 GLN 153 0.3862

GLN 153 GLU 154 -0.0002

GLU 154 LEU 155 0.0221

LEU 155 LEU 156 -0.0000

LEU 156 ASP 157 0.4766

ASP 157 LEU 158 -0.0001

LEU 158 ALA 159 0.1339

ALA 159 GLY 160 0.0002

GLY 160 PHE 161 0.2797

PHE 161 PRO 162 0.0005

PRO 162 PRO 163 0.0568

PRO 163 GLY 164 -0.0001

GLY 164 PRO 165 0.0878

PRO 165 PRO 166 0.0002

PRO 166 VAL 167 -0.0062

VAL 167 LEU 168 0.0001

LEU 168 VAL 169 0.0204

VAL 169 THR 170 0.0002

THR 170 THR 171 0.0427

THR 171 PRO 172 -0.0001

PRO 172 PRO 173 0.0982

PRO 173 GLY 174 -0.0001

GLY 174 GLU 175 0.1060

GLU 175 ARG 176 0.0002

ARG 176 HIS 177 0.0951

HIS 177 GLU 178 0.0006

GLU 178 ILE 179 0.0179

ILE 179 GLY 180 0.0001

GLY 180 ALA 181 0.0018

ALA 181 MET 182 0.0001

MET 182 LEU 183 0.0833

LEU 183 ALA 184 -0.0001

ALA 184 ALA 185 0.1153

ALA 185 TYR 186 -0.0004

TYR 186 HIS 187 0.1275

HIS 187 LEU 188 -0.0000

LEU 188 ARG 189 0.2069

ARG 189 ARG 190 -0.0001

ARG 190 LYS 191 0.1053

LYS 191 GLY 192 0.0000

GLY 192 VAL 193 0.0711

VAL 193 PRO 194 -0.0002

PRO 194 ALA 195 -0.1380

ALA 195 LEU 196 -0.0001

LEU 196 TYR 197 -0.0898

TYR 197 LEU 198 -0.0002

LEU 198 GLY 199 0.0180

GLY 199 PRO 200 -0.0001

PRO 200 ASP 201 -0.0477

ASP 201 THR 202 0.0005

THR 202 PRO 203 0.0932

PRO 203 LEU 204 0.0000

LEU 204 PRO 205 -0.0981

PRO 205 ASP 206 0.0000

ASP 206 LEU 207 -0.0500

LEU 207 ARG 208 0.0003

ARG 208 ALA 209 -0.2713

ALA 209 LEU 210 0.0003

LEU 210 ALA 211 -0.1884

ALA 211 ARG 212 0.0000

ARG 212 ARG 213 -0.1783

ARG 213 LEU 214 -0.0001

LEU 214 GLY 215 -0.0837

GLY 215 ALA 216 0.0005

ALA 216 GLY 217 -0.0896

GLY 217 ALA 218 0.0002

ALA 218 VAL 219 -0.1010

VAL 219 VAL 220 0.0000

VAL 220 LEU 221 -0.0103

LEU 221 SER 222 0.0002

SER 222 ALA 223 0.1057

ALA 223 VAL 224 -0.0002

VAL 224 LEU 225 0.1172

LEU 225 SER 226 0.0001

SER 226 GLU 227 0.1507

GLU 227 PRO 228 0.0000

PRO 228 LEU 229 -0.2389

LEU 229 ARG 230 -0.0001

ARG 230 ALA 231 0.0760

ALA 231 LEU 232 0.0001

LEU 232 PRO 233 -0.2630

PRO 233 ASP 234 -0.0002

ASP 234 GLY 235 -0.0384

GLY 235 ALA 236 -0.0000

ALA 236 LEU 237 0.1184

LEU 237 LYS 238 0.0001

LYS 238 ASP 239 -0.0392

ASP 239 LEU 240 0.0000

LEU 240 ALA 241 -0.0376

ALA 241 PRO 242 -0.0001

PRO 242 ARG 243 -0.0689

ARG 243 VAL 244 -0.0001

VAL 244 PHE 245 -0.0433

PHE 245 LEU 246 -0.0001

LEU 246 GLY 247 -0.0670

GLY 247 GLY 248 0.0002

GLY 248 GLN 249 -0.0191

GLN 249 GLY 250 0.0001

GLY 250 ALA 251 -0.1908

ALA 251 GLY 252 0.0000

GLY 252 PRO 253 -0.2713

PRO 253 GLU 254 -0.0003

GLU 254 GLU 255 -0.2523

GLU 255 ALA 256 0.0001

ALA 256 ARG 257 0.0532

ARG 257 ARG 258 -0.0001

ARG 258 LEU 259 -0.1020

LEU 259 GLY 260 -0.0002

GLY 260 ALA 261 0.1710

ALA 261 GLU 262 -0.0001

GLU 262 TYR 263 -0.1732

TYR 263 MET 264 -0.0001

MET 264 GLU 265 -0.1947

GLU 265 ASP 266 0.0001

ASP 266 LEU 267 0.2342

LEU 267 LYS 268 -0.0000

LYS 268 GLY 269 0.1004

GLY 269 LEU 270 0.0001

LEU 270 ALA 271 0.1239

ALA 271 GLU 272 -0.0001

GLU 272 ALA 273 0.1619

ALA 273 LEU 274 -0.0002

LEU 274 ASP 82 0.1544

ASP 82 LEU 83 -0.0001

LEU 83 GLY 84 -0.3043

GLY 84 THR 85 0.0002

THR 85 GLY 86 -0.0030

GLY 86 LEU 87 0.0000

LEU 87 LEU 88 -0.1515

LEU 88 GLU 89 -0.0002

GLU 89 ALA 90 0.0737

ALA 90 LEU 91 -0.0002

LEU 91 LEU 92 -0.0544

LEU 92 ARG 93 0.0004

ARG 93 GLY 94 0.1816

GLY 94 ASP 95 0.0000

ASP 95 LEU 96 -0.0565

LEU 96 ALA 97 0.0001

ALA 97 GLY 98 0.3927

GLY 98 ALA 99 0.0000

ALA 99 GLU 100 -0.0633

GLU 100 ALA 101 -0.0003

ALA 101 LEU 102 0.2164

LEU 102 PHE 103 0.0004

PHE 103 ARG 104 -0.1789

ARG 104 ARG 105 0.0001

ARG 105 GLY 106 -0.0504

GLY 106 LEU 107 0.0002

LEU 107 ARG 108 0.0586

ARG 108 PHE 109 -0.0003

PHE 109 TRP 110 -0.0637

TRP 110 GLY 111 -0.0000

GLY 111 PRO 112 0.1915

PRO 112 GLU 113 -0.0001

GLU 113 GLY 114 0.1146

GLY 114 VAL 115 0.0002

VAL 115 LEU 116 -0.2175

LEU 116 GLU 117 0.0001

GLU 117 HIS 118 0.0132

HIS 118 LEU 119 -0.0003

LEU 119 LEU 120 -0.1120

LEU 120 LEU 121 0.0000

LEU 121 PRO 122 0.1488

PRO 122 VAL 123 -0.0002

VAL 123 LEU 124 -0.3231

LEU 124 ARG 125 0.0000

ARG 125 GLU 126 0.0015

GLU 126 VAL 127 -0.0002

VAL 127 GLY 128 -0.0833

GLY 128 GLU 129 0.0000

GLU 129 ALA 130 -0.0137

ALA 130 TRP 131 -0.0003

TRP 131 HIS 132 -0.0104

HIS 132 ARG 133 -0.0003

ARG 133 GLY 134 0.1232

GLY 134 GLU 135 -0.0000

GLU 135 ILE 136 -0.0269

ILE 136 GLY 137 -0.0000

GLY 137 VAL 138 -0.0837

VAL 138 ALA 139 -0.0002

ALA 139 GLU 140 -0.1606

GLU 140 GLU 141 0.0002

GLU 141 HIS 142 0.0413

HIS 142 LEU 143 -0.0001

LEU 143 ALA 144 -0.0914

ALA 144 SER 145 0.0002

SER 145 THR 146 0.1124

THR 146 PHE 147 0.0000

PHE 147 LEU 148 -0.2170

LEU 148 ARG 149 0.0002

ARG 149 ALA 150 0.2653

ALA 150 ARG 151 0.0001

ARG 151 LEU 152 -0.1277

LEU 152 GLN 153 0.0001

GLN 153 GLU 154 0.3739

GLU 154 LEU 155 -0.0001

LEU 155 LEU 156 0.2715

LEU 156 ASP 157 -0.0001

ASP 157 LEU 158 0.1473

LEU 158 ALA 159 -0.0001

ALA 159 GLY 160 0.5191

GLY 160 PHE 161 -0.0000

PHE 161 PRO 162 -0.0368

PRO 162 PRO 163 -0.0002

PRO 163 GLY 164 0.1091

GLY 164 PRO 165 -0.0000

PRO 165 PRO 166 -0.2410

PRO 166 VAL 167 -0.0001

VAL 167 LEU 168 -0.0773

LEU 168 VAL 169 0.0000

VAL 169 THR 170 -0.0905

THR 170 THR 171 -0.0001

THR 171 PRO 172 0.1310

PRO 172 PRO 173 -0.0004

PRO 173 GLY 174 -0.3872

GLY 174 GLU 175 -0.0002

GLU 175 ARG 176 -0.0129

ARG 176 HIS 177 0.0004

HIS 177 GLU 178 0.0497

GLU 178 ILE 179 0.0002

ILE 179 GLY 180 -0.1894

GLY 180 ALA 181 -0.0000

ALA 181 MET 182 0.0700

MET 182 LEU 183 -0.0002

LEU 183 ALA 184 -0.0942

ALA 184 ALA 185 0.0004

ALA 185 TYR 186 0.2360

TYR 186 HIS 187 -0.0003

HIS 187 LEU 188 -0.0928

LEU 188 ARG 189 0.0001

ARG 189 ARG 190 0.2636

ARG 190 LYS 191 0.0000

LYS 191 GLY 192 -0.0763

GLY 192 VAL 193 0.0003

VAL 193 PRO 194 -0.1061

PRO 194 ALA 195 -0.0002

ALA 195 LEU 196 -0.1677

LEU 196 TYR 197 0.0003

TYR 197 LEU 198 0.0289

LEU 198 GLY 199 -0.0002

GLY 199 PRO 200 0.0327

PRO 200 ASP 201 0.0000

ASP 201 THR 202 -0.2602

THR 202 PRO 203 -0.0002

PRO 203 LEU 204 0.0967

LEU 204 PRO 205 -0.0000

PRO 205 ASP 206 0.1719

ASP 206 LEU 207 0.0003

LEU 207 ARG 208 -0.0759

ARG 208 ALA 209 -0.0000

ALA 209 LEU 210 0.1749

LEU 210 ALA 211 -0.0000

ALA 211 ARG 212 -0.0727

ARG 212 ARG 213 -0.0001

ARG 213 LEU 214 0.0725

LEU 214 GLY 215 -0.0002

GLY 215 ALA 216 -0.0260

ALA 216 GLY 217 -0.0001

GLY 217 ALA 218 -0.0700

ALA 218 VAL 219 0.0002

VAL 219 VAL 220 -0.0487

VAL 220 LEU 221 0.0002

LEU 221 SER 222 -0.1399

SER 222 ALA 223 -0.0000

ALA 223 VAL 224 -0.1952

VAL 224 LEU 225 -0.0001

LEU 225 SER 226 -0.2978

SER 226 GLU 227 -0.0001

GLU 227 PRO 228 0.0172

PRO 228 LEU 229 0.0001

LEU 229 ARG 230 0.1303

ARG 230 ALA 231 -0.0001

ALA 231 LEU 232 -0.1018

LEU 232 PRO 233 -0.0002

PRO 233 ASP 234 -0.0354

ASP 234 GLY 235 -0.0003

GLY 235 ALA 236 0.1611

ALA 236 LEU 237 0.0001

LEU 237 LYS 238 -0.1930

LYS 238 ASP 239 -0.0002

ASP 239 LEU 240 0.0260

LEU 240 ALA 241 0.0000

ALA 241 PRO 242 -0.0827

PRO 242 ARG 243 0.0002

ARG 243 VAL 244 -0.0366

VAL 244 PHE 245 0.0003

PHE 245 LEU 246 -0.0457

LEU 246 GLY 247 -0.0002

GLY 247 GLY 248 -0.0235

GLY 248 GLN 249 0.0003

GLN 249 GLY 250 -0.3410

GLY 250 ALA 251 -0.0001

ALA 251 GLY 252 -0.1137

GLY 252 PRO 253 -0.0000

PRO 253 GLU 254 -0.0566

GLU 254 GLU 255 0.0004

GLU 255 ALA 256 0.0466

ALA 256 ARG 257 -0.0004

ARG 257 ARG 258 -0.0392

ARG 258 LEU 259 -0.0001

LEU 259 GLY 260 -0.1134

GLY 260 ALA 261 -0.0002

ALA 261 GLU 262 -0.0639

GLU 262 TYR 263 -0.0001

TYR 263 MET 264 -0.1902

MET 264 GLU 265 0.0000

GLU 265 ASP 266 -0.3809

ASP 266 LEU 267 0.0000

LEU 267 LYS 268 0.1292

LYS 268 GLY 269 0.0001

GLY 269 LEU 270 0.0289

LEU 270 ALA 271 -0.0001

ALA 271 GLU 272 -0.2507

GLU 272 ALA 273 -0.0002

ALA 273 LEU 274 0.0076

LEU 274 ALA 275 0.0002

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 22022413193125998

--- normal mode 11 ---

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

* *