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

* *

CA strain for 22022413193125998

--- 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
ARG 79 PRO 80 -0.0000

PRO 80 GLU 81 -0.1341

GLU 81 ASP 82 0.0000

ASP 82 LEU 83 -0.0377

LEU 83 GLY 84 0.0000

GLY 84 THR 85 -0.2506

THR 85 GLY 86 0.0001

GLY 86 LEU 87 -0.2001

LEU 87 LEU 88 -0.0001

LEU 88 GLU 89 0.1139

GLU 89 ALA 90 -0.0000

ALA 90 LEU 91 -0.0282

LEU 91 LEU 92 0.0001

LEU 92 ARG 93 0.1053

ARG 93 GLY 94 0.0002

GLY 94 ASP 95 -0.1734

ASP 95 LEU 96 -0.0001

LEU 96 ALA 97 0.0225

ALA 97 GLY 98 -0.0002

GLY 98 ALA 99 0.1156

ALA 99 GLU 100 0.0002

GLU 100 ALA 101 -0.2645

ALA 101 LEU 102 0.0000

LEU 102 PHE 103 -0.1054

PHE 103 ARG 104 0.0001

ARG 104 ARG 105 -0.7525

ARG 105 GLY 106 -0.0000

GLY 106 LEU 107 0.1673

LEU 107 ARG 108 -0.0004

ARG 108 PHE 109 -0.0035

PHE 109 TRP 110 -0.0001

TRP 110 GLY 111 -0.1525

GLY 111 PRO 112 0.0001

PRO 112 GLU 113 -0.0654

GLU 113 GLY 114 -0.0001

GLY 114 VAL 115 -0.0094

VAL 115 LEU 116 -0.0003

LEU 116 GLU 117 0.1058

GLU 117 HIS 118 0.0003

HIS 118 LEU 119 -0.2319

LEU 119 LEU 120 -0.0000

LEU 120 LEU 121 0.2962

LEU 121 PRO 122 0.0000

PRO 122 VAL 123 -0.1397

VAL 123 LEU 124 0.0001

LEU 124 ARG 125 -0.0386

ARG 125 GLU 126 0.0001

GLU 126 VAL 127 -0.1755

VAL 127 GLY 128 0.0002

GLY 128 GLU 129 -0.0316

GLU 129 ALA 130 -0.0001

ALA 130 TRP 131 -0.0227

TRP 131 HIS 132 -0.0000

HIS 132 ARG 133 -0.0502

ARG 133 GLY 134 0.0001

GLY 134 GLU 135 0.0990

GLU 135 ILE 136 0.0002

ILE 136 GLY 137 -0.2473

GLY 137 VAL 138 0.0001

VAL 138 ALA 139 0.0197

ALA 139 GLU 140 0.0002

GLU 140 GLU 141 0.1444

GLU 141 HIS 142 0.0005

HIS 142 LEU 143 0.0400

LEU 143 ALA 144 0.0004

ALA 144 SER 145 0.1197

SER 145 THR 146 0.0002

THR 146 PHE 147 -0.1511

PHE 147 LEU 148 0.0000

LEU 148 ARG 149 0.0122

ARG 149 ALA 150 -0.0001

ALA 150 ARG 151 -0.1557

ARG 151 LEU 152 -0.0001

LEU 152 GLN 153 0.0823

GLN 153 GLU 154 -0.0005

GLU 154 LEU 155 0.1098

LEU 155 LEU 156 -0.0002

LEU 156 ASP 157 0.1461

ASP 157 LEU 158 -0.0002

LEU 158 ALA 159 0.0251

ALA 159 GLY 160 0.0000

GLY 160 PHE 161 0.0252

PHE 161 PRO 162 0.0002

PRO 162 PRO 163 -0.2401

PRO 163 GLY 164 -0.0001

GLY 164 PRO 165 -0.0165

PRO 165 PRO 166 -0.0001

PRO 166 VAL 167 0.1160

VAL 167 LEU 168 0.0002

LEU 168 VAL 169 0.0285

VAL 169 THR 170 0.0002

THR 170 THR 171 -0.0416

THR 171 PRO 172 -0.0001

PRO 172 PRO 173 0.0486

PRO 173 GLY 174 0.0002

GLY 174 GLU 175 0.0292

GLU 175 ARG 176 0.0001

ARG 176 HIS 177 -0.0167

HIS 177 GLU 178 -0.0003

GLU 178 ILE 179 0.0804

ILE 179 GLY 180 -0.0002

GLY 180 ALA 181 0.0489

ALA 181 MET 182 0.0002

MET 182 LEU 183 0.0998

LEU 183 ALA 184 0.0001

ALA 184 ALA 185 -0.0342

ALA 185 TYR 186 -0.0000

TYR 186 HIS 187 0.0869

HIS 187 LEU 188 -0.0001

LEU 188 ARG 189 0.0088

ARG 189 ARG 190 -0.0000

ARG 190 LYS 191 -0.0568

LYS 191 GLY 192 0.0000

GLY 192 VAL 193 -0.0406

VAL 193 PRO 194 -0.0001

PRO 194 ALA 195 0.0460

ALA 195 LEU 196 -0.0002

LEU 196 TYR 197 0.0123

TYR 197 LEU 198 -0.0001

LEU 198 GLY 199 0.0122

GLY 199 PRO 200 0.0001

PRO 200 ASP 201 0.0044

ASP 201 THR 202 -0.0003

THR 202 PRO 203 0.0794

PRO 203 LEU 204 0.0000

LEU 204 PRO 205 -0.0223

PRO 205 ASP 206 -0.0000

ASP 206 LEU 207 0.0144

LEU 207 ARG 208 -0.0001

ARG 208 ALA 209 -0.1894

ALA 209 LEU 210 0.0003

LEU 210 ALA 211 0.0719

ALA 211 ARG 212 -0.0001

ARG 212 ARG 213 -0.1734

ARG 213 LEU 214 0.0004

LEU 214 GLY 215 0.0855

GLY 215 ALA 216 0.0001

ALA 216 GLY 217 0.1662

GLY 217 ALA 218 0.0001

ALA 218 VAL 219 0.0983

VAL 219 VAL 220 0.0002

VAL 220 LEU 221 0.0277

LEU 221 SER 222 0.0002

SER 222 ALA 223 0.0245

ALA 223 VAL 224 0.0003

VAL 224 LEU 225 0.1370

LEU 225 SER 226 0.0001

SER 226 GLU 227 -0.1576

GLU 227 PRO 228 0.0003

PRO 228 LEU 229 0.0179

LEU 229 ARG 230 -0.0001

ARG 230 ALA 231 -0.0486

ALA 231 LEU 232 -0.0002

LEU 232 PRO 233 0.0266

PRO 233 ASP 234 0.0003

ASP 234 GLY 235 -0.0915

GLY 235 ALA 236 -0.0001

ALA 236 LEU 237 0.0263

LEU 237 LYS 238 0.0001

LYS 238 ASP 239 -0.0190

ASP 239 LEU 240 -0.0001

LEU 240 ALA 241 -0.0075

ALA 241 PRO 242 -0.0001

PRO 242 ARG 243 0.0250

ARG 243 VAL 244 0.0001

VAL 244 PHE 245 0.0542

PHE 245 LEU 246 0.0003

LEU 246 GLY 247 0.1034

GLY 247 GLY 248 0.0000

GLY 248 GLN 249 -0.0846

GLN 249 GLY 250 -0.0002

GLY 250 ALA 251 0.0995

ALA 251 GLY 252 -0.0004

GLY 252 PRO 253 0.0984

PRO 253 GLU 254 -0.0002

GLU 254 GLU 255 -0.0614

GLU 255 ALA 256 0.0001

ALA 256 ARG 257 0.0943

ARG 257 ARG 258 -0.0001

ARG 258 LEU 259 -0.0957

LEU 259 GLY 260 0.0003

GLY 260 ALA 261 0.1070

ALA 261 GLU 262 -0.0002

GLU 262 TYR 263 0.0063

TYR 263 MET 264 -0.0001

MET 264 GLU 265 -0.0677

GLU 265 ASP 266 0.0000

ASP 266 LEU 267 0.1858

LEU 267 LYS 268 0.0002

LYS 268 GLY 269 0.0798

GLY 269 LEU 270 0.0001

LEU 270 ALA 271 -0.0041

ALA 271 GLU 272 0.0003

GLU 272 ALA 273 -0.0148

ALA 273 LEU 274 -0.0001

LEU 274 ASP 82 0.0622

ASP 82 LEU 83 -0.0002

LEU 83 GLY 84 0.0812

GLY 84 THR 85 -0.0001

THR 85 GLY 86 0.0794

GLY 86 LEU 87 0.0001

LEU 87 LEU 88 -0.0467

LEU 88 GLU 89 0.0003

GLU 89 ALA 90 0.1637

ALA 90 LEU 91 0.0003

LEU 91 LEU 92 -0.1278

LEU 92 ARG 93 -0.0001

ARG 93 GLY 94 0.0441

GLY 94 ASP 95 -0.0005

ASP 95 LEU 96 -0.0672

LEU 96 ALA 97 -0.0002

ALA 97 GLY 98 0.1651

GLY 98 ALA 99 -0.0001

ALA 99 GLU 100 -0.0974

GLU 100 ALA 101 -0.0001

ALA 101 LEU 102 0.0836

LEU 102 PHE 103 -0.0000

PHE 103 ARG 104 -0.0281

ARG 104 ARG 105 -0.0002

ARG 105 GLY 106 0.0317

GLY 106 LEU 107 -0.0001

LEU 107 ARG 108 0.0138

ARG 108 PHE 109 -0.0000

PHE 109 TRP 110 -0.0183

TRP 110 GLY 111 0.0000

GLY 111 PRO 112 -0.0025

PRO 112 GLU 113 0.0000

GLU 113 GLY 114 -0.0202

GLY 114 VAL 115 -0.0000

VAL 115 LEU 116 0.0128

LEU 116 GLU 117 0.0002

GLU 117 HIS 118 0.0348

HIS 118 LEU 119 0.0002

LEU 119 LEU 120 0.0213

LEU 120 LEU 121 -0.0000

LEU 121 PRO 122 0.0218

PRO 122 VAL 123 0.0001

VAL 123 LEU 124 0.1033

LEU 124 ARG 125 0.0004

ARG 125 GLU 126 0.0597

GLU 126 VAL 127 -0.0004

VAL 127 GLY 128 0.1226

GLY 128 GLU 129 -0.0001

GLU 129 ALA 130 0.0132

ALA 130 TRP 131 0.0004

TRP 131 HIS 132 -0.0232

HIS 132 ARG 133 0.0001

ARG 133 GLY 134 0.0563

GLY 134 GLU 135 -0.0000

GLU 135 ILE 136 -0.1341

ILE 136 GLY 137 -0.0001

GLY 137 VAL 138 -0.2207

VAL 138 ALA 139 0.0002

ALA 139 GLU 140 -0.1754

GLU 140 GLU 141 0.0003

GLU 141 HIS 142 -0.0914

HIS 142 LEU 143 0.0001

LEU 143 ALA 144 0.0353

ALA 144 SER 145 0.0002

SER 145 THR 146 0.0342

THR 146 PHE 147 -0.0001

PHE 147 LEU 148 0.0624

LEU 148 ARG 149 0.0000

ARG 149 ALA 150 0.0709

ALA 150 ARG 151 -0.0002

ARG 151 LEU 152 0.0515

LEU 152 GLN 153 -0.0001

GLN 153 GLU 154 0.0240

GLU 154 LEU 155 0.0001

LEU 155 LEU 156 -0.0955

LEU 156 ASP 157 -0.0002

ASP 157 LEU 158 0.0716

LEU 158 ALA 159 0.0004

ALA 159 GLY 160 -0.1097

GLY 160 PHE 161 0.0000

PHE 161 PRO 162 -0.0673

PRO 162 PRO 163 0.0002

PRO 163 GLY 164 -0.1235

GLY 164 PRO 165 -0.0001

PRO 165 PRO 166 0.0439

PRO 166 VAL 167 -0.0002

VAL 167 LEU 168 0.0995

LEU 168 VAL 169 0.0000

VAL 169 THR 170 0.0545

THR 170 THR 171 -0.0002

THR 171 PRO 172 -0.0548

PRO 172 PRO 173 0.0001

PRO 173 GLY 174 0.2467

GLY 174 GLU 175 0.0003

GLU 175 ARG 176 0.1480

ARG 176 HIS 177 -0.0000

HIS 177 GLU 178 -0.0881

GLU 178 ILE 179 -0.0000

ILE 179 GLY 180 0.0630

GLY 180 ALA 181 -0.0001

ALA 181 MET 182 -0.0159

MET 182 LEU 183 0.0003

LEU 183 ALA 184 0.0147

ALA 184 ALA 185 -0.0001

ALA 185 TYR 186 -0.0171

TYR 186 HIS 187 -0.0001

HIS 187 LEU 188 -0.0229

LEU 188 ARG 189 0.0001

ARG 189 ARG 190 -0.0084

ARG 190 LYS 191 -0.0001

LYS 191 GLY 192 -0.0124

GLY 192 VAL 193 0.0002

VAL 193 PRO 194 0.0179

PRO 194 ALA 195 0.0002

ALA 195 LEU 196 0.1123

LEU 196 TYR 197 0.0002

TYR 197 LEU 198 0.0759

LEU 198 GLY 199 0.0001

GLY 199 PRO 200 -0.0597

PRO 200 ASP 201 -0.0001

ASP 201 THR 202 0.2009

THR 202 PRO 203 -0.0000

PRO 203 LEU 204 -0.0067

LEU 204 PRO 205 0.0003

PRO 205 ASP 206 -0.1081

ASP 206 LEU 207 -0.0002

LEU 207 ARG 208 0.0768

ARG 208 ALA 209 -0.0002

ALA 209 LEU 210 -0.1361

LEU 210 ALA 211 -0.0004

ALA 211 ARG 212 0.0876

ARG 212 ARG 213 0.0003

ARG 213 LEU 214 0.0571

LEU 214 GLY 215 -0.0002

GLY 215 ALA 216 0.0462

ALA 216 GLY 217 -0.0001

GLY 217 ALA 218 0.0840

ALA 218 VAL 219 -0.0002

VAL 219 VAL 220 0.0900

VAL 220 LEU 221 0.0004

LEU 221 SER 222 0.1293

SER 222 ALA 223 -0.0001

ALA 223 VAL 224 0.1843

VAL 224 LEU 225 -0.0002

LEU 225 SER 226 0.2499

SER 226 GLU 227 0.0001

GLU 227 PRO 228 -0.0710

PRO 228 LEU 229 -0.0001

LEU 229 ARG 230 -0.1161

ARG 230 ALA 231 0.0002

ALA 231 LEU 232 -0.0010

LEU 232 PRO 233 0.0000

PRO 233 ASP 234 0.0453

ASP 234 GLY 235 0.0002

GLY 235 ALA 236 -0.0807

ALA 236 LEU 237 0.0000

LEU 237 LYS 238 0.1576

LYS 238 ASP 239 0.0001

ASP 239 LEU 240 -0.0514

LEU 240 ALA 241 0.0002

ALA 241 PRO 242 0.0687

PRO 242 ARG 243 -0.0001

ARG 243 VAL 244 0.0473

VAL 244 PHE 245 -0.0002

PHE 245 LEU 246 0.1029

LEU 246 GLY 247 -0.0000

GLY 247 GLY 248 0.0776

GLY 248 GLN 249 -0.0001

GLN 249 GLY 250 0.0824

GLY 250 ALA 251 -0.0003

ALA 251 GLY 252 0.1372

GLY 252 PRO 253 -0.0002

PRO 253 GLU 254 0.0055

GLU 254 GLU 255 -0.0003

GLU 255 ALA 256 -0.0588

ALA 256 ARG 257 -0.0000

ARG 257 ARG 258 0.0488

ARG 258 LEU 259 -0.0003

LEU 259 GLY 260 0.0834

GLY 260 ALA 261 -0.0000

ALA 261 GLU 262 -0.0069

GLU 262 TYR 263 -0.0003

TYR 263 MET 264 -0.0185

MET 264 GLU 265 -0.0002

GLU 265 ASP 266 0.0388

ASP 266 LEU 267 0.0003

LEU 267 LYS 268 -0.0324

LYS 268 GLY 269 0.0002

GLY 269 LEU 270 -0.0190

LEU 270 ALA 271 -0.0002

ALA 271 GLU 272 -0.0128

GLU 272 ALA 273 -0.0003

ALA 273 LEU 274 0.0020

LEU 274 ALA 275 0.0001

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 9 ---

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

* *