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

* *

CA strain for 220224165159117000

--- normal mode 8 ---

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 0.0002

LEU 83 GLY 84 -0.0683

GLY 84 THR 85 -0.0001

THR 85 GLY 86 -0.0292

GLY 86 LEU 87 0.0002

LEU 87 LEU 88 -0.0418

LEU 88 GLU 89 -0.0002

GLU 89 ALA 90 -0.0273

ALA 90 LEU 91 -0.0004

LEU 91 LEU 92 -0.0136

LEU 92 ARG 93 0.0000

ARG 93 GLY 94 0.0047

GLY 94 ASP 95 -0.0002

ASP 95 LEU 96 0.0140

LEU 96 ALA 97 0.0001

ALA 97 GLY 98 -0.0269

GLY 98 ALA 99 -0.0001

ALA 99 GLU 100 -0.0259

GLU 100 ALA 101 -0.0001

ALA 101 LEU 102 0.0084

LEU 102 PHE 103 0.0001

PHE 103 ARG 104 -0.0872

ARG 104 ARG 105 -0.0002

ARG 105 GLY 106 -0.0139

GLY 106 LEU 107 -0.0000

LEU 107 ARG 108 -0.0484

ARG 108 PHE 109 0.0004

PHE 109 TRP 110 -0.0899

TRP 110 GLY 111 0.0002

GLY 111 PRO 112 0.0320

PRO 112 GLU 113 -0.0002

GLU 113 GLY 114 0.0056

GLY 114 VAL 115 0.0002

VAL 115 LEU 116 -0.0661

LEU 116 GLU 117 0.0002

GLU 117 HIS 118 0.0065

HIS 118 LEU 119 -0.0002

LEU 119 LEU 120 -0.0162

LEU 120 LEU 121 0.0000

LEU 121 PRO 122 0.0199

PRO 122 VAL 123 -0.0002

VAL 123 LEU 124 -0.0479

LEU 124 ARG 125 0.0001

ARG 125 GLU 126 -0.0058

GLU 126 VAL 127 -0.0001

VAL 127 GLY 128 -0.0131

GLY 128 GLU 129 -0.0001

GLU 129 ALA 130 0.0069

ALA 130 TRP 131 0.0003

TRP 131 HIS 132 -0.0014

HIS 132 ARG 133 0.0001

ARG 133 GLY 134 0.0035

GLY 134 GLU 135 -0.0003

GLU 135 ILE 136 0.0053

ILE 136 GLY 137 -0.0002

GLY 137 VAL 138 0.0010

VAL 138 ALA 139 0.0000

ALA 139 GLU 140 -0.0074

GLU 140 GLU 141 0.0001

GLU 141 HIS 142 0.0038

HIS 142 LEU 143 -0.0001

LEU 143 ALA 144 -0.0075

ALA 144 SER 145 0.0001

SER 145 THR 146 0.0066

THR 146 PHE 147 -0.0001

PHE 147 LEU 148 -0.0284

LEU 148 ARG 149 -0.0001

ARG 149 ALA 150 0.0490

ALA 150 ARG 151 0.0003

ARG 151 LEU 152 -0.0575

LEU 152 GLN 153 -0.0000

GLN 153 GLU 154 0.1254

GLU 154 LEU 155 0.0000

LEU 155 LEU 156 -0.0107

LEU 156 ASP 157 0.0002

ASP 157 LEU 158 0.0082

LEU 158 ALA 159 -0.0000

ALA 159 GLY 160 0.0697

GLY 160 PHE 161 0.0000

PHE 161 PRO 162 0.0009

PRO 162 PRO 163 0.0002

PRO 163 GLY 164 0.0034

GLY 164 PRO 165 0.0004

PRO 165 PRO 166 -0.0257

PRO 166 VAL 167 0.0002

VAL 167 LEU 168 -0.0105

LEU 168 VAL 169 -0.0001

VAL 169 THR 170 -0.0019

THR 170 THR 171 0.0001

THR 171 PRO 172 0.0263

PRO 172 PRO 173 -0.0001

PRO 173 GLY 174 -0.0306

GLY 174 GLU 175 -0.0001

GLU 175 ARG 176 0.0175

ARG 176 HIS 177 0.0003

HIS 177 GLU 178 0.0254

GLU 178 ILE 179 -0.0001

ILE 179 GLY 180 -0.0107

GLY 180 ALA 181 0.0003

ALA 181 MET 182 0.0567

MET 182 LEU 183 0.0002

LEU 183 ALA 184 -0.0210

ALA 184 ALA 185 -0.0004

ALA 185 TYR 186 0.0135

TYR 186 HIS 187 0.0001

HIS 187 LEU 188 -0.0300

LEU 188 ARG 189 -0.0003

ARG 189 ARG 190 -0.0018

ARG 190 LYS 191 0.0002

LYS 191 GLY 192 0.0052

GLY 192 VAL 193 -0.0002

VAL 193 PRO 194 0.0013

PRO 194 ALA 195 -0.0000

ALA 195 LEU 196 -0.0180

LEU 196 TYR 197 -0.0001

TYR 197 LEU 198 0.0269

LEU 198 GLY 199 -0.0000

GLY 199 PRO 200 0.0098

PRO 200 ASP 201 -0.0000

ASP 201 THR 202 -0.0161

THR 202 PRO 203 -0.0001

PRO 203 LEU 204 0.0053

LEU 204 PRO 205 0.0000

PRO 205 ASP 206 -0.0030

ASP 206 LEU 207 -0.0001

LEU 207 ARG 208 -0.0004

ARG 208 ALA 209 0.0000

ALA 209 LEU 210 0.0117

LEU 210 ALA 211 0.0004

ALA 211 ARG 212 -0.0018

ARG 212 ARG 213 -0.0001

ARG 213 LEU 214 0.0167

LEU 214 GLY 215 0.0002

GLY 215 ALA 216 -0.0071

ALA 216 GLY 217 0.0002

GLY 217 ALA 218 -0.0133

ALA 218 VAL 219 0.0001

VAL 219 VAL 220 -0.0156

VAL 220 LEU 221 0.0003

LEU 221 SER 222 -0.0122

SER 222 ALA 223 -0.0000

ALA 223 VAL 224 -0.0161

VAL 224 LEU 225 0.0001

LEU 225 SER 226 -0.0130

SER 226 GLU 227 -0.0001

GLU 227 PRO 228 -0.0002

PRO 228 LEU 229 0.0001

LEU 229 ARG 230 0.0117

ARG 230 ALA 231 -0.0002

ALA 231 LEU 232 -0.0053

LEU 232 PRO 233 0.0001

PRO 233 ASP 234 -0.0024

ASP 234 GLY 235 -0.0001

GLY 235 ALA 236 0.0063

ALA 236 LEU 237 0.0000

LEU 237 LYS 238 -0.0043

LYS 238 ASP 239 -0.0001

ASP 239 LEU 240 0.0121

LEU 240 ALA 241 0.0002

ALA 241 PRO 242 -0.0169

PRO 242 ARG 243 0.0001

ARG 243 VAL 244 -0.0047

VAL 244 PHE 245 -0.0001

PHE 245 LEU 246 -0.0084

LEU 246 GLY 247 0.0002

GLY 247 GLY 248 -0.0080

GLY 248 GLN 249 0.0001

GLN 249 GLY 250 -0.0266

GLY 250 ALA 251 0.0002

ALA 251 GLY 252 0.0044

GLY 252 PRO 253 0.0001

PRO 253 GLU 254 -0.0019

GLU 254 GLU 255 -0.0001

GLU 255 ALA 256 0.0050

ALA 256 ARG 257 -0.0000

ARG 257 ARG 258 -0.0022

ARG 258 LEU 259 0.0001

LEU 259 GLY 260 -0.0034

GLY 260 ALA 261 -0.0001

ALA 261 GLU 262 -0.0127

GLU 262 TYR 263 0.0003

TYR 263 MET 264 -0.0171

MET 264 GLU 265 -0.0001

GLU 265 ASP 266 -0.0269

ASP 266 LEU 267 -0.0002

LEU 267 LYS 268 0.0153

LYS 268 GLY 269 0.0002

GLY 269 LEU 270 -0.0180

LEU 270 ALA 271 -0.0002

ALA 271 GLU 272 0.0130

GLU 272 ALA 273 0.0002

ALA 273 LEU 274 -0.0080

LEU 274 TRP 275 0.0003

TRP 275 LEU 276 0.0054

LEU 276 PRO 277 0.0001

PRO 277 ARG 278 -0.0002

ARG 278 ARG 79 0.0123

ARG 79 PRO 80 -0.0000

PRO 80 GLU 81 -0.0308

GLU 81 ASP 82 0.0002

ASP 82 LEU 83 0.0131

LEU 83 GLY 84 -0.0003

GLY 84 THR 85 0.0026

THR 85 GLY 86 0.0002

GLY 86 LEU 87 -0.0048

LEU 87 LEU 88 0.0002

LEU 88 GLU 89 0.0013

GLU 89 ALA 90 0.0005

ALA 90 LEU 91 0.0172

LEU 91 LEU 92 -0.0000

LEU 92 ARG 93 0.0223

ARG 93 GLY 94 -0.0001

GLY 94 ASP 95 0.0338

ASP 95 LEU 96 0.0001

LEU 96 ALA 97 0.0253

ALA 97 GLY 98 -0.0001

GLY 98 ALA 99 -0.0379

ALA 99 GLU 100 0.0001

GLU 100 ALA 101 0.0320

ALA 101 LEU 102 -0.0001

LEU 102 PHE 103 -0.0226

PHE 103 ARG 104 -0.0002

ARG 104 ARG 105 0.0195

ARG 105 GLY 106 -0.0002

GLY 106 LEU 107 0.0430

LEU 107 ARG 108 -0.0001

ARG 108 PHE 109 -0.0208

PHE 109 TRP 110 -0.0002

TRP 110 GLY 111 0.0869

GLY 111 PRO 112 0.0005

PRO 112 GLU 113 -0.0224

GLU 113 GLY 114 -0.0003

GLY 114 VAL 115 -0.0340

VAL 115 LEU 116 0.0000

LEU 116 GLU 117 -0.0933

GLU 117 HIS 118 0.0001

HIS 118 LEU 119 -0.0761

LEU 119 LEU 120 -0.0001

LEU 120 LEU 121 0.0257

LEU 121 PRO 122 -0.0001

PRO 122 VAL 123 -0.0344

VAL 123 LEU 124 0.0002

LEU 124 ARG 125 0.0210

ARG 125 GLU 126 -0.0000

GLU 126 VAL 127 -0.0173

VAL 127 GLY 128 0.0003

GLY 128 GLU 129 0.0130

GLU 129 ALA 130 -0.0002

ALA 130 TRP 131 -0.0041

TRP 131 HIS 132 0.0001

HIS 132 ARG 133 0.0015

ARG 133 GLY 134 0.0001

GLY 134 GLU 135 0.0096

GLU 135 ILE 136 0.0002

ILE 136 GLY 137 -0.0181

GLY 137 VAL 138 -0.0002

VAL 138 ALA 139 0.0149

ALA 139 GLU 140 -0.0002

GLU 140 GLU 141 0.0109

GLU 141 HIS 142 -0.0001

HIS 142 LEU 143 0.0726

LEU 143 ALA 144 0.0002

ALA 144 SER 145 0.0162

SER 145 THR 146 -0.0002

THR 146 PHE 147 0.1006

PHE 147 LEU 148 -0.0001

LEU 148 ARG 149 -0.0052

ARG 149 ALA 150 -0.0003

ALA 150 ARG 151 0.0917

ARG 151 LEU 152 -0.0001

LEU 152 GLN 153 -0.0198

GLN 153 GLU 154 0.0004

GLU 154 LEU 155 -0.0082

LEU 155 LEU 156 0.0000

LEU 156 ASP 157 0.0257

ASP 157 LEU 158 -0.0001

LEU 158 ALA 159 -0.0132

ALA 159 GLY 160 0.0001

GLY 160 PHE 161 0.0295

PHE 161 PRO 162 -0.0000

PRO 162 PRO 163 0.0156

PRO 163 GLY 164 -0.0001

GLY 164 PRO 165 -0.0023

PRO 165 PRO 166 -0.0001

PRO 166 VAL 167 0.0024

VAL 167 LEU 168 -0.0000

LEU 168 VAL 169 -0.0084

VAL 169 THR 170 0.0002

THR 170 THR 171 -0.0019

THR 171 PRO 172 -0.0001

PRO 172 PRO 173 -0.0100

PRO 173 GLY 174 0.0001

GLY 174 GLU 175 -0.0019

GLU 175 ARG 176 -0.0003

ARG 176 HIS 177 -0.0000

HIS 177 GLU 178 0.0000

GLU 178 ILE 179 -0.0006

ILE 179 GLY 180 -0.0002

GLY 180 ALA 181 0.0029

ALA 181 MET 182 0.0003

MET 182 LEU 183 -0.0249

LEU 183 ALA 184 -0.0001

ALA 184 ALA 185 0.0324

ALA 185 TYR 186 -0.0001

TYR 186 HIS 187 -0.0392

HIS 187 LEU 188 0.0000

LEU 188 ARG 189 -0.0053

ARG 189 ARG 190 0.0001

ARG 190 LYS 191 -0.0292

LYS 191 GLY 192 0.0001

GLY 192 VAL 193 0.0288

VAL 193 PRO 194 0.0001

PRO 194 ALA 195 -0.0074

ALA 195 LEU 196 -0.0002

LEU 196 TYR 197 -0.0293

TYR 197 LEU 198 0.0001

LEU 198 GLY 199 -0.0220

GLY 199 PRO 200 -0.0004

PRO 200 ASP 201 0.0213

ASP 201 THR 202 0.0004

THR 202 PRO 203 0.0217

PRO 203 LEU 204 0.0001

LEU 204 PRO 205 -0.0062

PRO 205 ASP 206 0.0002

ASP 206 LEU 207 0.0070

LEU 207 ARG 208 -0.0002

ARG 208 ALA 209 -0.0018

ALA 209 LEU 210 0.0001

LEU 210 ALA 211 -0.0040

ALA 211 ARG 212 0.0000

ARG 212 ARG 213 0.0021

ARG 213 LEU 214 0.0002

LEU 214 GLY 215 0.0029

GLY 215 ALA 216 0.0003

ALA 216 GLY 217 0.0042

GLY 217 ALA 218 -0.0001

ALA 218 VAL 219 0.0015

VAL 219 VAL 220 -0.0001

VAL 220 LEU 221 -0.0011

LEU 221 SER 222 -0.0000

SER 222 ALA 223 0.0033

ALA 223 VAL 224 0.0001

VAL 224 LEU 225 -0.0129

LEU 225 SER 226 0.0001

SER 226 GLU 227 -0.0134

GLU 227 PRO 228 -0.0000

PRO 228 LEU 229 0.0176

LEU 229 ARG 230 0.0002

ARG 230 ALA 231 -0.0054

ALA 231 LEU 232 0.0001

LEU 232 PRO 233 0.0136

PRO 233 ASP 234 -0.0002

ASP 234 GLY 235 0.0048

GLY 235 ALA 236 0.0002

ALA 236 LEU 237 -0.0038

LEU 237 LYS 238 -0.0002

LYS 238 ASP 239 0.0038

ASP 239 LEU 240 0.0000

LEU 240 ALA 241 -0.0002

ALA 241 PRO 242 -0.0002

PRO 242 ARG 243 -0.0020

ARG 243 VAL 244 0.0005

VAL 244 PHE 245 -0.0133

PHE 245 LEU 246 0.0001

LEU 246 GLY 247 0.0048

GLY 247 GLY 248 0.0000

GLY 248 GLN 249 0.0078

GLN 249 GLY 250 0.0000

GLY 250 ALA 251 0.0164

ALA 251 GLY 252 0.0000

GLY 252 PRO 253 0.0228

PRO 253 GLU 254 -0.0001

GLU 254 GLU 255 0.0166

GLU 255 ALA 256 -0.0005

ALA 256 ARG 257 -0.0025

ARG 257 ARG 258 0.0003

ARG 258 LEU 259 0.0050

LEU 259 GLY 260 0.0005

GLY 260 ALA 261 -0.0179

ALA 261 GLU 262 -0.0001

GLU 262 TYR 263 0.0096

TYR 263 MET 264 -0.0003

MET 264 GLU 265 0.0223

GLU 265 ASP 266 -0.0002

ASP 266 LEU 267 -0.0187

LEU 267 LYS 268 0.0000

LYS 268 GLY 269 -0.0335

GLY 269 LEU 270 0.0001

LEU 270 ALA 271 -0.0296

ALA 271 GLU 272 -0.0002

GLU 272 ALA 273 -0.0443

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 220224165159117000

--- normal mode 8 ---

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

* *