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

* *

CA strain for 22022415224472301

--- normal mode 10 ---

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
ASP 82 LEU 83 0.0001

LEU 83 GLY 84 0.1231

GLY 84 THR 85 -0.0002

THR 85 GLY 86 0.0613

GLY 86 LEU 87 -0.0000

LEU 87 LEU 88 0.0578

LEU 88 GLU 89 0.0002

GLU 89 ALA 90 0.0569

ALA 90 LEU 91 -0.0001

LEU 91 LEU 92 0.0345

LEU 92 ARG 93 -0.0001

ARG 93 GLY 94 -0.0209

GLY 94 ASP 95 0.0000

ASP 95 LEU 96 0.0345

LEU 96 ALA 97 -0.0004

ALA 97 GLY 98 0.0296

GLY 98 ALA 99 -0.0001

ALA 99 GLU 100 0.1011

GLU 100 ALA 101 -0.0003

ALA 101 LEU 102 0.0798

LEU 102 PHE 103 0.0003

PHE 103 ARG 104 0.0608

ARG 104 ARG 105 -0.0002

ARG 105 GLY 106 0.0105

GLY 106 LEU 107 0.0002

LEU 107 ARG 108 -0.0658

ARG 108 PHE 109 0.0001

PHE 109 TRP 110 -0.0139

TRP 110 GLY 111 0.0003

GLY 111 PRO 112 -0.0534

PRO 112 GLU 113 0.0001

GLU 113 GLY 114 -0.0081

GLY 114 VAL 115 0.0001

VAL 115 LEU 116 -0.0015

LEU 116 GLU 117 -0.0001

GLU 117 HIS 118 0.0279

HIS 118 LEU 119 0.0002

LEU 119 LEU 120 0.0187

LEU 120 LEU 121 0.0001

LEU 121 PRO 122 0.0012

PRO 122 VAL 123 -0.0001

VAL 123 LEU 124 0.0668

LEU 124 ARG 125 -0.0005

ARG 125 GLU 126 0.0234

GLU 126 VAL 127 -0.0003

VAL 127 GLY 128 0.0413

GLY 128 GLU 129 -0.0001

GLU 129 ALA 130 -0.0007

ALA 130 TRP 131 0.0001

TRP 131 HIS 132 -0.0095

HIS 132 ARG 133 -0.0001

ARG 133 GLY 134 -0.0143

GLY 134 GLU 135 0.0002

GLU 135 ILE 136 -0.0099

ILE 136 GLY 137 0.0002

GLY 137 VAL 138 -0.0044

VAL 138 ALA 139 0.0004

ALA 139 GLU 140 0.0038

GLU 140 GLU 141 0.0000

GLU 141 HIS 142 -0.0018

HIS 142 LEU 143 0.0001

LEU 143 ALA 144 0.0148

ALA 144 SER 145 -0.0001

SER 145 THR 146 -0.0120

THR 146 PHE 147 0.0001

PHE 147 LEU 148 0.0420

LEU 148 ARG 149 0.0003

ARG 149 ALA 150 -0.2108

ALA 150 ARG 151 -0.0002

ARG 151 LEU 152 -0.0276

LEU 152 GLN 153 0.0001

GLN 153 GLU 154 -0.4590

GLU 154 LEU 155 -0.0003

LEU 155 LEU 156 -0.1909

LEU 156 ASP 157 -0.0001

ASP 157 LEU 158 -0.0860

LEU 158 ALA 159 0.0002

ALA 159 GLY 160 -0.2760

GLY 160 PHE 161 -0.0001

PHE 161 PRO 162 -0.0399

PRO 162 PRO 163 -0.0004

PRO 163 GLY 164 -0.0423

GLY 164 PRO 165 -0.0001

PRO 165 PRO 166 0.1279

PRO 166 VAL 167 0.0003

VAL 167 LEU 168 0.0469

LEU 168 VAL 169 -0.0001

VAL 169 THR 170 0.0388

THR 170 THR 171 -0.0000

THR 171 PRO 172 -0.1085

PRO 172 PRO 173 0.0002

PRO 173 GLY 174 0.0790

GLY 174 GLU 175 -0.0002

GLU 175 ARG 176 -0.0818

ARG 176 HIS 177 -0.0003

HIS 177 GLU 178 -0.0368

GLU 178 ILE 179 0.0003

ILE 179 GLY 180 -0.0026

GLY 180 ALA 181 0.0002

ALA 181 MET 182 -0.2268

MET 182 LEU 183 -0.0003

LEU 183 ALA 184 0.0268

ALA 184 ALA 185 -0.0001

ALA 185 TYR 186 -0.1545

TYR 186 HIS 187 -0.0000

HIS 187 LEU 188 0.0207

LEU 188 ARG 189 0.0000

ARG 189 ARG 190 -0.0180

ARG 190 LYS 191 0.0002

LYS 191 GLY 192 -0.0147

GLY 192 VAL 193 -0.0005

VAL 193 PRO 194 0.0143

PRO 194 ALA 195 -0.0005

ALA 195 LEU 196 0.0674

LEU 196 TYR 197 -0.0002

TYR 197 LEU 198 -0.0953

LEU 198 GLY 199 -0.0001

GLY 199 PRO 200 -0.0046

PRO 200 ASP 201 -0.0001

ASP 201 THR 202 0.0268

THR 202 PRO 203 -0.0001

PRO 203 LEU 204 -0.0220

LEU 204 PRO 205 -0.0002

PRO 205 ASP 206 0.0215

ASP 206 LEU 207 -0.0002

LEU 207 ARG 208 -0.0159

ARG 208 ALA 209 0.0000

ALA 209 LEU 210 -0.0479

LEU 210 ALA 211 -0.0000

ALA 211 ARG 212 0.0069

ARG 212 ARG 213 0.0002

ARG 213 LEU 214 -0.0794

LEU 214 GLY 215 0.0003

GLY 215 ALA 216 0.0316

ALA 216 GLY 217 0.0001

GLY 217 ALA 218 0.0590

ALA 218 VAL 219 -0.0004

VAL 219 VAL 220 0.0401

VAL 220 LEU 221 -0.0002

LEU 221 SER 222 0.0377

SER 222 ALA 223 0.0004

ALA 223 VAL 224 0.0497

VAL 224 LEU 225 0.0003

LEU 225 SER 226 0.0127

SER 226 GLU 227 -0.0001

GLU 227 PRO 228 0.0120

PRO 228 LEU 229 -0.0004

LEU 229 ARG 230 -0.0430

ARG 230 ALA 231 0.0001

ALA 231 LEU 232 0.0227

LEU 232 PRO 233 0.0003

PRO 233 ASP 234 0.0021

ASP 234 GLY 235 0.0001

GLY 235 ALA 236 -0.0185

ALA 236 LEU 237 -0.0002

LEU 237 LYS 238 0.0068

LYS 238 ASP 239 0.0001

ASP 239 LEU 240 -0.0569

LEU 240 ALA 241 0.0004

ALA 241 PRO 242 0.0794

PRO 242 ARG 243 -0.0001

ARG 243 VAL 244 0.0191

VAL 244 PHE 245 0.0002

PHE 245 LEU 246 0.0455

LEU 246 GLY 247 0.0001

GLY 247 GLY 248 0.0292

GLY 248 GLN 249 -0.0003

GLN 249 GLY 250 0.0610

GLY 250 ALA 251 -0.0003

ALA 251 GLY 252 -0.0195

GLY 252 PRO 253 0.0004

PRO 253 GLU 254 -0.0028

GLU 254 GLU 255 -0.0002

GLU 255 ALA 256 -0.0210

ALA 256 ARG 257 -0.0002

ARG 257 ARG 258 0.0025

ARG 258 LEU 259 0.0001

LEU 259 GLY 260 0.0048

GLY 260 ALA 261 0.0000

ALA 261 GLU 262 0.0374

GLU 262 TYR 263 -0.0002

TYR 263 MET 264 0.0187

MET 264 GLU 265 0.0002

GLU 265 ASP 266 0.0532

ASP 266 LEU 267 -0.0000

LEU 267 LYS 268 -0.0259

LYS 268 GLY 269 -0.0003

GLY 269 LEU 270 0.0340

LEU 270 ALA 271 0.0004

ALA 271 GLU 272 -0.0401

GLU 272 ALA 273 -0.0000

ALA 273 LEU 274 0.0358

LEU 274 TRP 275 -0.0001

TRP 275 LEU 276 -0.0223

LEU 276 PRO 277 0.0001

PRO 277 ARG 278 0.0110

ARG 278 ARG 79 -0.2026

ARG 79 PRO 80 -0.0002

PRO 80 GLU 81 -0.0208

GLU 81 ASP 82 0.0001

ASP 82 LEU 83 -0.0034

LEU 83 GLY 84 -0.0001

GLY 84 THR 85 0.0178

THR 85 GLY 86 0.0002

GLY 86 LEU 87 0.0328

LEU 87 LEU 88 0.0002

LEU 88 GLU 89 0.0064

GLU 89 ALA 90 -0.0004

ALA 90 LEU 91 0.0350

LEU 91 LEU 92 -0.0001

LEU 92 ARG 93 0.0390

ARG 93 GLY 94 -0.0004

GLY 94 ASP 95 0.0208

ASP 95 LEU 96 -0.0005

LEU 96 ALA 97 0.0615

ALA 97 GLY 98 0.0000

GLY 98 ALA 99 -0.0026

ALA 99 GLU 100 0.0001

GLU 100 ALA 101 0.0099

ALA 101 LEU 102 -0.0001

LEU 102 PHE 103 0.0205

PHE 103 ARG 104 0.0000

ARG 104 ARG 105 0.1611

ARG 105 GLY 106 0.0001

GLY 106 LEU 107 -0.1549

LEU 107 ARG 108 0.0002

ARG 108 PHE 109 0.1846

PHE 109 TRP 110 0.0000

TRP 110 GLY 111 0.1570

GLY 111 PRO 112 0.0002

PRO 112 GLU 113 -0.2837

GLU 113 GLY 114 -0.0001

GLY 114 VAL 115 0.0701

VAL 115 LEU 116 -0.0003

LEU 116 GLU 117 -0.0465

GLU 117 HIS 118 -0.0005

HIS 118 LEU 119 0.1429

LEU 119 LEU 120 0.0002

LEU 120 LEU 121 -0.1841

LEU 121 PRO 122 -0.0000

PRO 122 VAL 123 0.0596

VAL 123 LEU 124 0.0001

LEU 124 ARG 125 0.0542

ARG 125 GLU 126 -0.0000

GLU 126 VAL 127 0.0223

VAL 127 GLY 128 -0.0003

GLY 128 GLU 129 0.0452

GLU 129 ALA 130 -0.0004

ALA 130 TRP 131 -0.0096

TRP 131 HIS 132 -0.0000

HIS 132 ARG 133 0.0217

ARG 133 GLY 134 0.0003

GLY 134 GLU 135 0.0121

GLU 135 ILE 136 0.0002

ILE 136 GLY 137 -0.0549

GLY 137 VAL 138 0.0002

VAL 138 ALA 139 0.0530

ALA 139 GLU 140 0.0002

GLU 140 GLU 141 0.0652

GLU 141 HIS 142 0.0000

HIS 142 LEU 143 0.2142

LEU 143 ALA 144 -0.0001

ALA 144 SER 145 0.0706

SER 145 THR 146 0.0001

THR 146 PHE 147 0.1444

PHE 147 LEU 148 0.0000

LEU 148 ARG 149 -0.0019

ARG 149 ALA 150 0.0004

ALA 150 ARG 151 0.1469

ARG 151 LEU 152 0.0004

LEU 152 GLN 153 -0.0130

GLN 153 GLU 154 0.0003

GLU 154 LEU 155 -0.0002

LEU 155 LEU 156 0.0002

LEU 156 ASP 157 0.0822

ASP 157 LEU 158 -0.0003

LEU 158 ALA 159 -0.0520

ALA 159 GLY 160 -0.0002

GLY 160 PHE 161 0.1011

PHE 161 PRO 162 -0.0003

PRO 162 PRO 163 0.0718

PRO 163 GLY 164 -0.0001

GLY 164 PRO 165 0.0102

PRO 165 PRO 166 -0.0003

PRO 166 VAL 167 0.0071

VAL 167 LEU 168 0.0002

LEU 168 VAL 169 -0.0354

VAL 169 THR 170 0.0002

THR 170 THR 171 -0.0039

THR 171 PRO 172 0.0001

PRO 172 PRO 173 -0.0370

PRO 173 GLY 174 -0.0002

GLY 174 GLU 175 -0.0125

GLU 175 ARG 176 -0.0000

ARG 176 HIS 177 -0.0222

HIS 177 GLU 178 0.0003

GLU 178 ILE 179 -0.0256

ILE 179 GLY 180 -0.0001

GLY 180 ALA 181 0.0064

ALA 181 MET 182 0.0002

MET 182 LEU 183 -0.0582

LEU 183 ALA 184 -0.0002

ALA 184 ALA 185 0.0958

ALA 185 TYR 186 -0.0002

TYR 186 HIS 187 -0.1118

HIS 187 LEU 188 0.0001

LEU 188 ARG 189 -0.0286

ARG 189 ARG 190 0.0002

ARG 190 LYS 191 -0.1098

LYS 191 GLY 192 -0.0001

GLY 192 VAL 193 0.0072

VAL 193 PRO 194 -0.0001

PRO 194 ALA 195 -0.0235

ALA 195 LEU 196 0.0002

LEU 196 TYR 197 -0.0805

TYR 197 LEU 198 0.0000

LEU 198 GLY 199 -0.0735

GLY 199 PRO 200 0.0001

PRO 200 ASP 201 0.0518

ASP 201 THR 202 0.0000

THR 202 PRO 203 0.0639

PRO 203 LEU 204 0.0001

LEU 204 PRO 205 -0.0272

PRO 205 ASP 206 -0.0003

ASP 206 LEU 207 0.0203

LEU 207 ARG 208 -0.0002

ARG 208 ALA 209 -0.0064

ALA 209 LEU 210 -0.0001

LEU 210 ALA 211 -0.0164

ALA 211 ARG 212 0.0002

ARG 212 ARG 213 0.0099

ARG 213 LEU 214 0.0003

LEU 214 GLY 215 0.0042

GLY 215 ALA 216 -0.0000

ALA 216 GLY 217 0.0107

GLY 217 ALA 218 0.0001

ALA 218 VAL 219 0.0047

VAL 219 VAL 220 -0.0003

VAL 220 LEU 221 0.0183

LEU 221 SER 222 0.0000

SER 222 ALA 223 0.0014

ALA 223 VAL 224 -0.0002

VAL 224 LEU 225 -0.0689

LEU 225 SER 226 0.0000

SER 226 GLU 227 -0.0175

GLU 227 PRO 228 0.0001

PRO 228 LEU 229 0.0580

LEU 229 ARG 230 -0.0001

ARG 230 ALA 231 -0.0167

ALA 231 LEU 232 0.0004

LEU 232 PRO 233 0.0274

PRO 233 ASP 234 -0.0000

ASP 234 GLY 235 0.0276

GLY 235 ALA 236 -0.0000

ALA 236 LEU 237 -0.0225

LEU 237 LYS 238 0.0001

LYS 238 ASP 239 0.0135

ASP 239 LEU 240 -0.0001

LEU 240 ALA 241 0.0084

ALA 241 PRO 242 -0.0004

PRO 242 ARG 243 -0.0082

ARG 243 VAL 244 -0.0003

VAL 244 PHE 245 -0.0609

PHE 245 LEU 246 0.0000

LEU 246 GLY 247 -0.0140

GLY 247 GLY 248 0.0001

GLY 248 GLN 249 0.0524

GLN 249 GLY 250 -0.0002

GLY 250 ALA 251 0.0307

ALA 251 GLY 252 -0.0001

GLY 252 PRO 253 0.0222

PRO 253 GLU 254 -0.0001

GLU 254 GLU 255 0.0536

GLU 255 ALA 256 0.0002

ALA 256 ARG 257 -0.0338

ARG 257 ARG 258 -0.0004

ARG 258 LEU 259 0.0258

LEU 259 GLY 260 -0.0004

GLY 260 ALA 261 -0.0876

ALA 261 GLU 262 0.0000

GLU 262 TYR 263 0.0157

TYR 263 MET 264 -0.0002

MET 264 GLU 265 0.0695

GLU 265 ASP 266 -0.0002

ASP 266 LEU 267 -0.0847

LEU 267 LYS 268 0.0001

LYS 268 GLY 269 -0.1442

GLY 269 LEU 270 0.0002

LEU 270 ALA 271 -0.0077

ALA 271 GLU 272 -0.0002

GLU 272 ALA 273 -0.0990

ALA 273 LEU 274 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 22022415224472301

--- normal mode 10 ---

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

* *