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

* *

CA strain for 220224165159117000

--- 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
ASP 82 LEU 83 0.0000

LEU 83 GLY 84 -0.0347

GLY 84 THR 85 0.0003

THR 85 GLY 86 0.0227

GLY 86 LEU 87 0.0000

LEU 87 LEU 88 0.0030

LEU 88 GLU 89 -0.0003

GLU 89 ALA 90 0.0631

ALA 90 LEU 91 0.0002

LEU 91 LEU 92 0.0415

LEU 92 ARG 93 -0.0002

ARG 93 GLY 94 0.0045

GLY 94 ASP 95 -0.0002

ASP 95 LEU 96 -0.0348

LEU 96 ALA 97 -0.0003

ALA 97 GLY 98 0.1459

GLY 98 ALA 99 0.0002

ALA 99 GLU 100 0.1639

GLU 100 ALA 101 -0.0001

ALA 101 LEU 102 -0.0387

LEU 102 PHE 103 -0.0001

PHE 103 ARG 104 0.0319

ARG 104 ARG 105 0.0002

ARG 105 GLY 106 0.0234

GLY 106 LEU 107 0.0002

LEU 107 ARG 108 0.0091

ARG 108 PHE 109 0.0000

PHE 109 TRP 110 0.0088

TRP 110 GLY 111 0.0001

GLY 111 PRO 112 0.0592

PRO 112 GLU 113 -0.0002

GLU 113 GLY 114 0.0627

GLY 114 VAL 115 0.0000

VAL 115 LEU 116 -0.0130

LEU 116 GLU 117 0.0002

GLU 117 HIS 118 0.0574

HIS 118 LEU 119 -0.0001

LEU 119 LEU 120 -0.0179

LEU 120 LEU 121 0.0004

LEU 121 PRO 122 0.0416

PRO 122 VAL 123 0.0004

VAL 123 LEU 124 -0.0148

LEU 124 ARG 125 0.0000

ARG 125 GLU 126 0.0317

GLU 126 VAL 127 -0.0001

VAL 127 GLY 128 0.0274

GLY 128 GLU 129 -0.0001

GLU 129 ALA 130 0.0122

ALA 130 TRP 131 -0.0002

TRP 131 HIS 132 0.0100

HIS 132 ARG 133 0.0001

ARG 133 GLY 134 -0.0021

GLY 134 GLU 135 -0.0004

GLU 135 ILE 136 0.0037

ILE 136 GLY 137 -0.0001

GLY 137 VAL 138 -0.0098

VAL 138 ALA 139 -0.0001

ALA 139 GLU 140 -0.0126

GLU 140 GLU 141 -0.0001

GLU 141 HIS 142 0.0021

HIS 142 LEU 143 0.0001

LEU 143 ALA 144 -0.0025

ALA 144 SER 145 0.0001

SER 145 THR 146 -0.0039

THR 146 PHE 147 -0.0000

PHE 147 LEU 148 -0.0053

LEU 148 ARG 149 -0.0003

ARG 149 ALA 150 0.1141

ALA 150 ARG 151 -0.0000

ARG 151 LEU 152 0.0370

LEU 152 GLN 153 0.0002

GLN 153 GLU 154 0.1415

GLU 154 LEU 155 0.0002

LEU 155 LEU 156 -0.0011

LEU 156 ASP 157 0.0003

ASP 157 LEU 158 0.0232

LEU 158 ALA 159 0.0002

ALA 159 GLY 160 0.0338

GLY 160 PHE 161 -0.0004

PHE 161 PRO 162 -0.0287

PRO 162 PRO 163 -0.0002

PRO 163 GLY 164 -0.0317

GLY 164 PRO 165 0.0000

PRO 165 PRO 166 -0.0107

PRO 166 VAL 167 0.0000

VAL 167 LEU 168 0.0007

LEU 168 VAL 169 -0.0000

VAL 169 THR 170 -0.0017

THR 170 THR 171 0.0000

THR 171 PRO 172 0.0111

PRO 172 PRO 173 0.0001

PRO 173 GLY 174 -0.0160

GLY 174 GLU 175 0.0002

GLU 175 ARG 176 0.0090

ARG 176 HIS 177 0.0000

HIS 177 GLU 178 0.0075

GLU 178 ILE 179 -0.0000

ILE 179 GLY 180 0.0214

GLY 180 ALA 181 -0.0003

ALA 181 MET 182 0.0251

MET 182 LEU 183 -0.0000

LEU 183 ALA 184 0.0185

ALA 184 ALA 185 0.0003

ALA 185 TYR 186 0.0122

TYR 186 HIS 187 0.0002

HIS 187 LEU 188 0.0298

LEU 188 ARG 189 -0.0002

ARG 189 ARG 190 0.0557

ARG 190 LYS 191 -0.0002

LYS 191 GLY 192 0.0268

GLY 192 VAL 193 -0.0001

VAL 193 PRO 194 0.0153

PRO 194 ALA 195 -0.0000

ALA 195 LEU 196 0.0224

LEU 196 TYR 197 -0.0001

TYR 197 LEU 198 0.0217

LEU 198 GLY 199 0.0001

GLY 199 PRO 200 0.0060

PRO 200 ASP 201 0.0001

ASP 201 THR 202 -0.0271

THR 202 PRO 203 0.0001

PRO 203 LEU 204 -0.0046

LEU 204 PRO 205 -0.0002

PRO 205 ASP 206 0.0028

ASP 206 LEU 207 -0.0001

LEU 207 ARG 208 -0.0063

ARG 208 ALA 209 -0.0000

ALA 209 LEU 210 0.0100

LEU 210 ALA 211 -0.0002

ALA 211 ARG 212 0.0038

ARG 212 ARG 213 -0.0001

ARG 213 LEU 214 0.0071

LEU 214 GLY 215 0.0001

GLY 215 ALA 216 0.0022

ALA 216 GLY 217 0.0000

GLY 217 ALA 218 0.0081

ALA 218 VAL 219 -0.0001

VAL 219 VAL 220 0.0126

VAL 220 LEU 221 0.0002

LEU 221 SER 222 0.0087

SER 222 ALA 223 0.0002

ALA 223 VAL 224 0.0158

VAL 224 LEU 225 -0.0001

LEU 225 SER 226 0.0240

SER 226 GLU 227 0.0002

GLU 227 PRO 228 0.0063

PRO 228 LEU 229 0.0002

LEU 229 ARG 230 -0.0078

ARG 230 ALA 231 -0.0000

ALA 231 LEU 232 0.0026

LEU 232 PRO 233 -0.0004

PRO 233 ASP 234 0.0025

ASP 234 GLY 235 0.0000

GLY 235 ALA 236 0.0012

ALA 236 LEU 237 -0.0000

LEU 237 LYS 238 0.0007

LYS 238 ASP 239 -0.0000

ASP 239 LEU 240 -0.0010

LEU 240 ALA 241 0.0003

ALA 241 PRO 242 -0.0063

PRO 242 ARG 243 0.0003

ARG 243 VAL 244 0.0068

VAL 244 PHE 245 0.0003

PHE 245 LEU 246 0.0126

LEU 246 GLY 247 -0.0001

GLY 247 GLY 248 0.0207

GLY 248 GLN 249 0.0001

GLN 249 GLY 250 -0.0078

GLY 250 ALA 251 0.0002

ALA 251 GLY 252 0.0235

GLY 252 PRO 253 -0.0002

PRO 253 GLU 254 -0.0072

GLU 254 GLU 255 -0.0001

GLU 255 ALA 256 -0.0104

ALA 256 ARG 257 -0.0002

ARG 257 ARG 258 -0.0003

ARG 258 LEU 259 0.0003

LEU 259 GLY 260 -0.0005

GLY 260 ALA 261 -0.0000

ALA 261 GLU 262 -0.0085

GLU 262 TYR 263 -0.0003

TYR 263 MET 264 -0.0255

MET 264 GLU 265 0.0004

GLU 265 ASP 266 -0.0544

ASP 266 LEU 267 -0.0001

LEU 267 LYS 268 -0.0109

LYS 268 GLY 269 -0.0002

GLY 269 LEU 270 -0.0051

LEU 270 ALA 271 0.0000

ALA 271 GLU 272 -0.0113

GLU 272 ALA 273 -0.0001

ALA 273 LEU 274 -0.0010

LEU 274 TRP 275 -0.0001

TRP 275 LEU 276 -0.0120

LEU 276 PRO 277 0.0002

PRO 277 ARG 278 0.0162

ARG 278 ARG 79 -0.1607

ARG 79 PRO 80 0.0002

PRO 80 GLU 81 -0.0540

GLU 81 ASP 82 -0.0001

ASP 82 LEU 83 0.0763

LEU 83 GLY 84 -0.0001

GLY 84 THR 85 0.0182

THR 85 GLY 86 0.0001

GLY 86 LEU 87 0.0185

LEU 87 LEU 88 0.0001

LEU 88 GLU 89 0.0505

GLU 89 ALA 90 0.0002

ALA 90 LEU 91 -0.0126

LEU 91 LEU 92 0.0002

LEU 92 ARG 93 0.0137

ARG 93 GLY 94 0.0001

GLY 94 ASP 95 0.0061

ASP 95 LEU 96 -0.0002

LEU 96 ALA 97 0.0092

ALA 97 GLY 98 0.0002

GLY 98 ALA 99 0.0018

ALA 99 GLU 100 0.0002

GLU 100 ALA 101 -0.0548

ALA 101 LEU 102 -0.0002

LEU 102 PHE 103 -0.0124

PHE 103 ARG 104 0.0002

ARG 104 ARG 105 -0.1492

ARG 105 GLY 106 -0.0001

GLY 106 LEU 107 -0.0361

LEU 107 ARG 108 0.0000

ARG 108 PHE 109 -0.0110

PHE 109 TRP 110 0.0002

TRP 110 GLY 111 0.0668

GLY 111 PRO 112 -0.0000

PRO 112 GLU 113 -0.0435

GLU 113 GLY 114 0.0002

GLY 114 VAL 115 0.0680

VAL 115 LEU 116 -0.0003

LEU 116 GLU 117 -0.0361

GLU 117 HIS 118 0.0002

HIS 118 LEU 119 0.0065

LEU 119 LEU 120 -0.0000

LEU 120 LEU 121 0.0022

LEU 121 PRO 122 0.0002

PRO 122 VAL 123 0.0187

VAL 123 LEU 124 -0.0001

LEU 124 ARG 125 0.0210

ARG 125 GLU 126 -0.0001

GLU 126 VAL 127 0.0058

VAL 127 GLY 128 0.0001

GLY 128 GLU 129 0.0042

GLU 129 ALA 130 0.0004

ALA 130 TRP 131 -0.0049

TRP 131 HIS 132 0.0002

HIS 132 ARG 133 0.0085

ARG 133 GLY 134 0.0000

GLY 134 GLU 135 -0.0016

GLU 135 ILE 136 -0.0003

ILE 136 GLY 137 -0.0046

GLY 137 VAL 138 -0.0000

VAL 138 ALA 139 -0.0002

ALA 139 GLU 140 -0.0001

GLU 140 GLU 141 -0.0129

GLU 141 HIS 142 -0.0004

HIS 142 LEU 143 -0.0372

LEU 143 ALA 144 0.0004

ALA 144 SER 145 -0.0240

SER 145 THR 146 -0.0001

THR 146 PHE 147 -0.0203

PHE 147 LEU 148 0.0001

LEU 148 ARG 149 -0.0444

ARG 149 ALA 150 0.0002

ALA 150 ARG 151 -0.0115

ARG 151 LEU 152 -0.0001

LEU 152 GLN 153 -0.0193

GLN 153 GLU 154 -0.0002

GLU 154 LEU 155 0.0422

LEU 155 LEU 156 -0.0001

LEU 156 ASP 157 0.0155

ASP 157 LEU 158 -0.0000

LEU 158 ALA 159 0.0087

ALA 159 GLY 160 -0.0001

GLY 160 PHE 161 0.0120

PHE 161 PRO 162 0.0001

PRO 162 PRO 163 -0.0037

PRO 163 GLY 164 0.0000

GLY 164 PRO 165 -0.0151

PRO 165 PRO 166 0.0000

PRO 166 VAL 167 -0.0046

VAL 167 LEU 168 0.0001

LEU 168 VAL 169 -0.0171

VAL 169 THR 170 -0.0001

THR 170 THR 171 0.0130

THR 171 PRO 172 0.0001

PRO 172 PRO 173 0.0058

PRO 173 GLY 174 -0.0005

GLY 174 GLU 175 -0.0062

GLU 175 ARG 176 0.0003

ARG 176 HIS 177 0.0052

HIS 177 GLU 178 0.0001

GLU 178 ILE 179 -0.0263

ILE 179 GLY 180 -0.0002

GLY 180 ALA 181 -0.0166

ALA 181 MET 182 0.0002

MET 182 LEU 183 0.0050

LEU 183 ALA 184 0.0001

ALA 184 ALA 185 -0.0296

ALA 185 TYR 186 -0.0001

TYR 186 HIS 187 -0.0048

HIS 187 LEU 188 0.0000

LEU 188 ARG 189 -0.0443

ARG 189 ARG 190 0.0000

ARG 190 LYS 191 -0.0250

LYS 191 GLY 192 -0.0001

GLY 192 VAL 193 -0.0429

VAL 193 PRO 194 -0.0000

PRO 194 ALA 195 -0.0039

ALA 195 LEU 196 -0.0000

LEU 196 TYR 197 -0.0255

TYR 197 LEU 198 -0.0002

LEU 198 GLY 199 -0.0020

GLY 199 PRO 200 -0.0001

PRO 200 ASP 201 -0.0056

ASP 201 THR 202 -0.0002

THR 202 PRO 203 0.0013

PRO 203 LEU 204 0.0003

LEU 204 PRO 205 -0.0021

PRO 205 ASP 206 0.0001

ASP 206 LEU 207 0.0187

LEU 207 ARG 208 0.0001

ARG 208 ALA 209 0.0061

ALA 209 LEU 210 0.0000

LEU 210 ALA 211 0.0101

ALA 211 ARG 212 0.0002

ARG 212 ARG 213 0.0040

ARG 213 LEU 214 -0.0001

LEU 214 GLY 215 0.0026

GLY 215 ALA 216 -0.0002

ALA 216 GLY 217 0.0103

GLY 217 ALA 218 -0.0002

ALA 218 VAL 219 -0.0029

VAL 219 VAL 220 -0.0001

VAL 220 LEU 221 0.0038

LEU 221 SER 222 0.0000

SER 222 ALA 223 0.0046

ALA 223 VAL 224 0.0001

VAL 224 LEU 225 -0.0015

LEU 225 SER 226 -0.0001

SER 226 GLU 227 0.0044

GLU 227 PRO 228 0.0001

PRO 228 LEU 229 -0.0104

LEU 229 ARG 230 -0.0001

ARG 230 ALA 231 0.0062

ALA 231 LEU 232 0.0001

LEU 232 PRO 233 -0.0087

PRO 233 ASP 234 -0.0002

ASP 234 GLY 235 0.0005

GLY 235 ALA 236 0.0001

ALA 236 LEU 237 0.0055

LEU 237 LYS 238 0.0001

LYS 238 ASP 239 0.0015

ASP 239 LEU 240 -0.0004

LEU 240 ALA 241 -0.0029

ALA 241 PRO 242 0.0001

PRO 242 ARG 243 0.0116

ARG 243 VAL 244 -0.0002

VAL 244 PHE 245 0.0188

PHE 245 LEU 246 0.0000

LEU 246 GLY 247 0.0100

GLY 247 GLY 248 -0.0002

GLY 248 GLN 249 -0.0062

GLN 249 GLY 250 0.0001

GLY 250 ALA 251 0.0024

ALA 251 GLY 252 0.0001

GLY 252 PRO 253 0.0090

PRO 253 GLU 254 0.0002

GLU 254 GLU 255 -0.0031

GLU 255 ALA 256 0.0003

ALA 256 ARG 257 0.0004

ARG 257 ARG 258 0.0001

ARG 258 LEU 259 -0.0014

LEU 259 GLY 260 0.0001

GLY 260 ALA 261 0.0119

ALA 261 GLU 262 0.0002

GLU 262 TYR 263 0.0094

TYR 263 MET 264 -0.0005

MET 264 GLU 265 0.0058

GLU 265 ASP 266 -0.0005

ASP 266 LEU 267 -0.0086

LEU 267 LYS 268 0.0004

LYS 268 GLY 269 0.0380

GLY 269 LEU 270 -0.0000

LEU 270 ALA 271 0.0343

ALA 271 GLU 272 -0.0001

GLU 272 ALA 273 0.0327

ALA 273 LEU 274 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 220224165159117000

--- normal mode 9 ---

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

* *