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

* DARK TET *

CA strain for 22022316112813361

--- 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
PRO 80 GLU 81 0.0036

GLU 81 ASP 82 0.0033

ASP 82 LEU 83 0.0017

LEU 83 GLY 84 0.0252

GLY 84 THR 85 0.0029

THR 85 GLY 86 0.0025

GLY 86 LEU 87 0.0024

LEU 87 LEU 88 0.0276

LEU 88 GLU 89 0.0018

GLU 89 ALA 90 0.0036

ALA 90 LEU 91 0.0040

LEU 91 LEU 92 -0.0399

LEU 92 ARG 93 0.0025

ARG 93 GLY 94 0.0061

GLY 94 ASP 95 0.0060

ASP 95 LEU 96 0.0077

LEU 96 ALA 97 0.0051

ALA 97 GLY 98 0.0034

GLY 98 ALA 99 0.0042

ALA 99 GLU 100 0.0647

GLU 100 ALA 101 0.0010

ALA 101 LEU 102 0.0013

LEU 102 PHE 103 0.0013

PHE 103 ARG 104 0.0215

ARG 104 ARG 105 0.0006

ARG 105 GLY 106 0.0006

GLY 106 LEU 107 0.0005

LEU 107 ARG 108 -0.0909

ARG 108 PHE 109 0.0009

PHE 109 TRP 110 0.0006

TRP 110 GLY 111 0.0005

GLY 111 PRO 112 -0.1503

PRO 112 GLU 113 0.0035

GLU 113 GLY 114 0.0003

GLY 114 VAL 115 0.0037

VAL 115 LEU 116 -0.0866

LEU 116 GLU 117 0.0007

GLU 117 HIS 118 0.0023

HIS 118 LEU 119 0.0005

LEU 119 LEU 120 -0.0594

LEU 120 LEU 121 0.0031

LEU 121 PRO 122 0.0017

PRO 122 VAL 123 0.0027

VAL 123 LEU 124 -0.0023

LEU 124 ARG 125 0.0011

ARG 125 GLU 126 0.0094

GLU 126 VAL 127 0.0017

VAL 127 GLY 128 -0.0136

GLY 128 GLU 129 0.0081

GLU 129 ALA 130 0.0039

ALA 130 TRP 131 0.0096

TRP 131 HIS 132 0.0217

HIS 132 ARG 133 0.0118

ARG 133 GLY 134 0.0005

GLY 134 GLU 135 0.0114

GLU 135 ILE 136 0.0021

ILE 136 GLY 137 0.0088

GLY 137 VAL 138 0.0068

VAL 138 ALA 139 0.0089

ALA 139 GLU 140 -0.0001

GLU 140 GLU 141 0.0011

GLU 141 HIS 142 0.0042

HIS 142 LEU 143 0.0045

LEU 143 ALA 144 -0.0579

ALA 144 SER 145 0.0043

SER 145 THR 146 0.0010

THR 146 PHE 147 0.0034

PHE 147 LEU 148 -0.0545

LEU 148 ARG 149 0.0020

ARG 149 ALA 150 0.0022

ALA 150 ARG 151 0.0013

ARG 151 LEU 152 -0.0353

LEU 152 GLN 153 0.0002

GLN 153 GLU 154 0.0015

GLU 154 LEU 155 0.0008

LEU 155 LEU 156 0.0113

LEU 156 ASP 157 0.0008

ASP 157 LEU 158 0.0015

LEU 158 ALA 159 0.0012

ALA 159 GLY 160 -0.0622

GLY 160 PHE 161 0.0007

PHE 161 PRO 162 0.0031

PRO 162 PRO 163 0.0008

PRO 163 GLY 164 -0.1489

GLY 164 PRO 165 0.0104

PRO 165 PRO 166 0.0051

PRO 166 VAL 167 0.0019

VAL 167 LEU 168 -0.0353

LEU 168 VAL 169 0.0022

VAL 169 THR 170 0.0106

THR 170 THR 171 0.0064

THR 171 PRO 172 -0.0147

PRO 172 PRO 173 0.0203

PRO 173 GLY 174 0.0103

GLY 174 GLU 175 0.0191

GLU 175 ARG 176 0.2062

ARG 176 HIS 177 0.0039

HIS 177 GLU 178 0.0076

GLU 178 ILE 179 0.0055

ILE 179 GLY 180 -0.0279

GLY 180 ALA 181 0.0013

ALA 181 MET 182 0.0069

MET 182 LEU 183 0.0028

LEU 183 ALA 184 0.0225

ALA 184 ALA 185 0.0015

ALA 185 TYR 186 0.0048

TYR 186 HIS 187 0.0050

HIS 187 LEU 188 0.0020

LEU 188 ARG 189 0.0026

ARG 189 ARG 190 0.0024

ARG 190 LYS 191 0.0038

LYS 191 GLY 192 -0.0281

GLY 192 VAL 193 0.0025

VAL 193 PRO 194 0.0011

PRO 194 ALA 195 0.0020

ALA 195 LEU 196 -0.1381

LEU 196 TYR 197 0.0027

TYR 197 LEU 198 0.0046

LEU 198 GLY 199 0.0020

GLY 199 PRO 200 -0.0150

PRO 200 ASP 201 0.0147

ASP 201 THR 202 0.0071

THR 202 PRO 203 0.0149

PRO 203 LEU 204 0.1604

LEU 204 PRO 205 0.0008

PRO 205 ASP 206 0.0219

ASP 206 LEU 207 0.0078

LEU 207 ARG 208 0.0596

ARG 208 ALA 209 0.0099

ALA 209 LEU 210 0.0209

LEU 210 ALA 211 0.0231

ALA 211 ARG 212 0.0342

ARG 212 ARG 213 0.0149

ARG 213 LEU 214 0.0099

LEU 214 GLY 215 0.0170

GLY 215 ALA 216 0.0725

ALA 216 GLY 217 0.0235

GLY 217 ALA 218 0.0067

ALA 218 VAL 219 0.0172

VAL 219 VAL 220 0.0009

VAL 220 LEU 221 0.0126

LEU 221 SER 222 0.0059

SER 222 ALA 223 0.0117

ALA 223 VAL 224 0.0246

VAL 224 LEU 225 0.0354

LEU 225 SER 226 0.0396

SER 226 GLU 227 0.0412

GLU 227 PRO 228 -0.0360

PRO 228 LEU 229 0.0488

LEU 229 ARG 230 0.0325

ARG 230 ALA 231 0.0289

ALA 231 LEU 232 -0.0013

LEU 232 PRO 233 0.0401

PRO 233 ASP 234 0.0452

ASP 234 GLY 235 0.0238

GLY 235 ALA 236 0.0947

ALA 236 LEU 237 0.0478

LEU 237 LYS 238 0.0371

LYS 238 ASP 239 0.0104

ASP 239 LEU 240 0.0359

LEU 240 ALA 241 0.0204

ALA 241 PRO 242 0.0209

PRO 242 ARG 243 0.0020

ARG 243 VAL 244 0.0192

VAL 244 PHE 245 0.0065

PHE 245 LEU 246 0.0138

LEU 246 GLY 247 0.0088

GLY 247 GLY 248 0.0951

GLY 248 GLN 249 0.0079

GLN 249 GLY 250 0.0390

GLY 250 ALA 251 0.0387

ALA 251 GLY 252 0.1671

GLY 252 PRO 253 0.0395

PRO 253 GLU 254 0.0408

GLU 254 GLU 255 0.0240

GLU 255 ALA 256 0.0577

ALA 256 ARG 257 0.0402

ARG 257 ARG 258 0.0395

ARG 258 LEU 259 0.0216

LEU 259 GLY 260 -0.0253

GLY 260 ALA 261 0.0346

ALA 261 GLU 262 0.0278

GLU 262 TYR 263 0.0120

TYR 263 MET 264 -0.1268

MET 264 GLU 265 0.0086

GLU 265 ASP 266 0.0285

ASP 266 LEU 267 0.0109

LEU 267 LYS 268 0.0307

LYS 268 GLY 269 0.0167

GLY 269 LEU 270 0.0111

LEU 270 ALA 271 0.0077

ALA 271 GLU 272 0.0186

GLU 272 ALA 273 0.0353

ALA 273 LEU 274 0.0034

LEU 274 ASP 82 0.0152

ASP 82 LEU 83 0.0005

LEU 83 GLY 84 0.0006

GLY 84 THR 85 0.0005

THR 85 GLY 86 -0.0466

GLY 86 LEU 87 -0.0000

LEU 87 LEU 88 0.0009

LEU 88 GLU 89 0.0007

GLU 89 ALA 90 -0.0381

ALA 90 LEU 91 0.0006

LEU 91 LEU 92 0.0018

LEU 92 ARG 93 0.0021

ARG 93 GLY 94 -0.0471

GLY 94 ASP 95 0.0015

ASP 95 LEU 96 0.0040

LEU 96 ALA 97 0.0023

ALA 97 GLY 98 -0.0419

GLY 98 ALA 99 0.0029

ALA 99 GLU 100 0.0027

GLU 100 ALA 101 0.0015

ALA 101 LEU 102 0.0074

LEU 102 PHE 103 0.0005

PHE 103 ARG 104 0.0005

ARG 104 ARG 105 0.0003

ARG 105 GLY 106 0.0133

GLY 106 LEU 107 0.0004

LEU 107 ARG 108 0.0001

ARG 108 PHE 109 0.0003

PHE 109 TRP 110 -0.0394

TRP 110 GLY 111 0.0017

GLY 111 PRO 112 0.0003

PRO 112 GLU 113 0.0018

GLU 113 GLY 114 0.0235

GLY 114 VAL 115 0.0002

VAL 115 LEU 116 -0.0000

LEU 116 GLU 117 0.0001

GLU 117 HIS 118 0.0465

HIS 118 LEU 119 0.0008

LEU 119 LEU 120 0.0009

LEU 120 LEU 121 0.0005

LEU 121 PRO 122 0.0374

PRO 122 VAL 123 0.0003

VAL 123 LEU 124 -0.0001

LEU 124 ARG 125 0.0001

ARG 125 GLU 126 0.0409

GLU 126 VAL 127 0.0011

VAL 127 GLY 128 0.0005

GLY 128 GLU 129 0.0008

GLU 129 ALA 130 0.0438

ALA 130 TRP 131 0.0019

TRP 131 HIS 132 0.0003

HIS 132 ARG 133 0.0016

ARG 133 GLY 134 0.0085

GLY 134 GLU 135 -0.0002

GLU 135 ILE 136 0.0001

ILE 136 GLY 137 0.0004

GLY 137 VAL 138 -0.0550

VAL 138 ALA 139 0.0040

ALA 139 GLU 140 0.0012

GLU 140 GLU 141 0.0031

GLU 141 HIS 142 -0.0399

HIS 142 LEU 143 0.0010

LEU 143 ALA 144 0.0006

ALA 144 SER 145 0.0006

SER 145 THR 146 -0.0563

THR 146 PHE 147 0.0003

PHE 147 LEU 148 0.0002

LEU 148 ARG 149 0.0004

ARG 149 ALA 150 -0.0578

ALA 150 ARG 151 0.0009

ARG 151 LEU 152 0.0002

LEU 152 GLN 153 0.0012

GLN 153 GLU 154 0.0005

GLU 154 LEU 155 0.0006

LEU 155 LEU 156 0.0003

LEU 156 ASP 157 0.0004

ASP 157 LEU 158 -0.0139

LEU 158 ALA 159 0.0103

ALA 159 GLY 160 0.0099

GLY 160 PHE 161 0.0016

PHE 161 PRO 162 -0.0061

PRO 162 PRO 163 0.0020

PRO 163 GLY 164 0.0004

GLY 164 PRO 165 0.0020

PRO 165 PRO 166 0.0115

PRO 166 VAL 167 0.0070

VAL 167 LEU 168 0.0075

LEU 168 VAL 169 0.0016

VAL 169 THR 170 0.0398

THR 170 THR 171 0.0074

THR 171 PRO 172 0.0075

PRO 172 PRO 173 0.0084

PRO 173 GLY 174 0.0499

GLY 174 GLU 175 0.0019

GLU 175 ARG 176 0.0015

ARG 176 HIS 177 0.0017

HIS 177 GLU 178 -0.0324

GLU 178 ILE 179 0.0023

ILE 179 GLY 180 0.0028

GLY 180 ALA 181 0.0006

ALA 181 MET 182 -0.0790

MET 182 LEU 183 0.0038

LEU 183 ALA 184 0.0005

ALA 184 ALA 185 0.0035

ALA 185 TYR 186 -0.0103

TYR 186 HIS 187 0.0050

HIS 187 LEU 188 0.0009

LEU 188 ARG 189 0.0046

ARG 189 ARG 190 0.0276

ARG 190 LYS 191 0.0133

LYS 191 GLY 192 0.0103

GLY 192 VAL 193 0.0057

VAL 193 PRO 194 0.0440

PRO 194 ALA 195 0.0043

ALA 195 LEU 196 0.0076

LEU 196 TYR 197 0.0018

TYR 197 LEU 198 0.0601

LEU 198 GLY 199 0.0011

GLY 199 PRO 200 0.0030

PRO 200 ASP 201 0.0026

ASP 201 THR 202 0.0000

THR 202 PRO 203 0.0112

PRO 203 LEU 204 0.0102

LEU 204 PRO 205 0.0058

PRO 205 ASP 206 0.0054

ASP 206 LEU 207 0.0142

LEU 207 ARG 208 0.0016

ARG 208 ALA 209 0.0131

ALA 209 LEU 210 -0.0416

LEU 210 ALA 211 0.0191

ALA 211 ARG 212 0.0018

ARG 212 ARG 213 0.0203

ARG 213 LEU 214 0.0115

LEU 214 GLY 215 0.0160

GLY 215 ALA 216 0.0047

ALA 216 GLY 217 0.0205

GLY 217 ALA 218 0.0611

ALA 218 VAL 219 0.0049

VAL 219 VAL 220 0.0011

VAL 220 LEU 221 0.0059

LEU 221 SER 222 0.0151

SER 222 ALA 223 0.0048

ALA 223 VAL 224 0.0005

VAL 224 LEU 225 0.0074

LEU 225 SER 226 0.0665

SER 226 GLU 227 0.0152

GLU 227 PRO 228 0.0047

PRO 228 LEU 229 0.0129

LEU 229 ARG 230 0.0085

ARG 230 ALA 231 0.0184

ALA 231 LEU 232 0.0049

LEU 232 PRO 233 0.0116

PRO 233 ASP 234 0.0098

ASP 234 GLY 235 0.0156

GLY 235 ALA 236 0.0192

ALA 236 LEU 237 0.0199

LEU 237 LYS 238 0.0112

LYS 238 ASP 239 0.0116

ASP 239 LEU 240 0.0118

LEU 240 ALA 241 0.0169

ALA 241 PRO 242 0.0602

PRO 242 ARG 243 0.0028

ARG 243 VAL 244 0.0066

VAL 244 PHE 245 0.0019

PHE 245 LEU 246 0.0610

LEU 246 GLY 247 0.0015

GLY 247 GLY 248 0.0041

GLY 248 GLN 249 0.0030

GLN 249 GLY 250 -0.0578

GLY 250 ALA 251 0.0090

ALA 251 GLY 252 0.0172

GLY 252 PRO 253 0.0094

PRO 253 GLU 254 -0.0320

GLU 254 GLU 255 0.0178

GLU 255 ALA 256 0.0121

ALA 256 ARG 257 0.0123

ARG 257 ARG 258 0.0087

ARG 258 LEU 259 0.0160

LEU 259 GLY 260 0.0087

GLY 260 ALA 261 0.0113

ALA 261 GLU 262 -0.0418

GLU 262 TYR 263 0.0002

TYR 263 MET 264 0.0074

MET 264 GLU 265 0.0002

GLU 265 ASP 266 -0.2178

ASP 266 LEU 267 0.0047

LEU 267 LYS 268 0.0037

LYS 268 GLY 269 0.0018

GLY 269 LEU 270 -0.0374

LEU 270 ALA 271 0.0136

ALA 271 GLU 272 0.0129

GLU 272 ALA 273 0.0076

ALA 273 LEU 274 0.0430

LEU 274 TRP 275 0.0325

TRP 275 LEU 276 0.0308

LEU 276 PRO 277 0.0065

PRO 277 ARG 278 0.1030

ARG 278 ARG 79 -0.1280

ARG 79 PRO 80 0.0004

PRO 80 GLU 81 0.0033

GLU 81 ASP 82 0.0035

ASP 82 LEU 83 0.0346

LEU 83 GLY 84 0.0012

GLY 84 THR 85 0.0020

THR 85 GLY 86 0.0020

GLY 86 LEU 87 0.0033

LEU 87 LEU 88 0.0012

LEU 88 GLU 89 0.0018

GLU 89 ALA 90 0.0020

ALA 90 LEU 91 -0.0062

LEU 91 LEU 92 0.0017

LEU 92 ARG 93 0.0023

ARG 93 GLY 94 0.0030

GLY 94 ASP 95 -0.0386

ASP 95 LEU 96 0.0034

LEU 96 ALA 97 0.0034

ALA 97 GLY 98 0.0015

GLY 98 ALA 99 0.0524

ALA 99 GLU 100 0.0017

GLU 100 ALA 101 0.0006

ALA 101 LEU 102 0.0017

LEU 102 PHE 103 0.0245

PHE 103 ARG 104 0.0002

ARG 104 ARG 105 0.0002

ARG 105 GLY 106 0.0002

GLY 106 LEU 107 0.0345

LEU 107 ARG 108 0.0005

ARG 108 PHE 109 0.0004

PHE 109 TRP 110 0.0001

TRP 110 GLY 111 -0.0560

GLY 111 PRO 112 0.0014

PRO 112 GLU 113 0.0031

GLU 113 GLY 114 0.0004

GLY 114 VAL 115 -0.0285

VAL 115 LEU 116 0.0004

LEU 116 GLU 117 0.0003

GLU 117 HIS 118 0.0006

HIS 118 LEU 119 -0.0480

LEU 119 LEU 120 0.0005

LEU 120 LEU 121 0.0014

LEU 121 PRO 122 0.0003

PRO 122 VAL 123 -0.0339

VAL 123 LEU 124 0.0037

LEU 124 ARG 125 0.0008

ARG 125 GLU 126 0.0037

GLU 126 VAL 127 -0.0165

VAL 127 GLY 128 0.0043

GLY 128 GLU 129 0.0033

GLU 129 ALA 130 0.0026

ALA 130 TRP 131 -0.0003

TRP 131 HIS 132 0.0029

HIS 132 ARG 133 0.0062

ARG 133 GLY 134 0.0002

GLY 134 GLU 135 0.0482

GLU 135 ILE 136 0.0050

ILE 136 GLY 137 0.0046

GLY 137 VAL 138 0.0042

VAL 138 ALA 139 0.0070

ALA 139 GLU 140 0.0034

GLU 140 GLU 141 0.0003

GLU 141 HIS 142 0.0035

HIS 142 LEU 143 0.0272

LEU 143 ALA 144 0.0004

ALA 144 SER 145 0.0011

SER 145 THR 146 0.0017

THR 146 PHE 147 -0.0559

PHE 147 LEU 148 0.0008

LEU 148 ARG 149 0.0011

ARG 149 ALA 150 0.0007

ALA 150 ARG 151 -0.0801

ARG 151 LEU 152 0.0005

LEU 152 GLN 153 -0.0002

GLN 153 GLU 154 0.0006

GLU 154 LEU 155 -0.1044

LEU 155 LEU 156 0.0010

LEU 156 ASP 157 0.0012

ASP 157 LEU 158 0.0023

LEU 158 ALA 159 -0.0188

ALA 159 GLY 160 0.0005

GLY 160 PHE 161 0.0005

PHE 161 PRO 162 0.0009

PRO 162 PRO 163 0.0689

PRO 163 GLY 164 0.0192

GLY 164 PRO 165 0.0191

PRO 165 PRO 166 0.0063

PRO 166 VAL 167 -0.0565

VAL 167 LEU 168 0.0036

LEU 168 VAL 169 0.0008

VAL 169 THR 170 0.0035

THR 170 THR 171 -0.0777

THR 171 PRO 172 0.0116

PRO 172 PRO 173 0.0096

PRO 173 GLY 174 0.0070

GLY 174 GLU 175 -0.0068

GLU 175 ARG 176 0.0037

ARG 176 HIS 177 0.0024

HIS 177 GLU 178 0.0035

GLU 178 ILE 179 -0.0230

ILE 179 GLY 180 0.0031

GLY 180 ALA 181 0.0004

ALA 181 MET 182 0.0033

MET 182 LEU 183 -0.0450

LEU 183 ALA 184 0.0040

ALA 184 ALA 185 0.0011

ALA 185 TYR 186 0.0041

TYR 186 HIS 187 -0.0320

HIS 187 LEU 188 0.0011

LEU 188 ARG 189 0.0032

ARG 189 ARG 190 0.0021

ARG 190 LYS 191 -0.0616

LYS 191 GLY 192 0.0014

GLY 192 VAL 193 0.0051

VAL 193 PRO 194 0.0025

PRO 194 ALA 195 -0.1083

ALA 195 LEU 196 0.0009

LEU 196 TYR 197 0.0012

TYR 197 LEU 198 0.0010

LEU 198 GLY 199 -0.0402

GLY 199 PRO 200 0.0034

PRO 200 ASP 201 0.0064

ASP 201 THR 202 0.0037

THR 202 PRO 203 -0.0180

PRO 203 LEU 204 0.0112

LEU 204 PRO 205 0.0003

PRO 205 ASP 206 0.0109

ASP 206 LEU 207 -0.0057

LEU 207 ARG 208 0.0107

ARG 208 ALA 209 0.0025

ALA 209 LEU 210 0.0130

LEU 210 ALA 211 0.0265

ALA 211 ARG 212 0.0027

ARG 212 ARG 213 0.0045

ARG 213 LEU 214 0.0050

LEU 214 GLY 215 0.0913

GLY 215 ALA 216 0.0004

ALA 216 GLY 217 0.0156

GLY 217 ALA 218 0.0042

ALA 218 VAL 219 0.0385

VAL 219 VAL 220 0.0028

VAL 220 LEU 221 0.0068

LEU 221 SER 222 0.0042

SER 222 ALA 223 -0.0807

ALA 223 VAL 224 0.0098

VAL 224 LEU 225 0.0143

LEU 225 SER 226 0.0149

SER 226 GLU 227 -0.0417

GLU 227 PRO 228 0.0008

PRO 228 LEU 229 0.0246

LEU 229 ARG 230 0.0166

ARG 230 ALA 231 -0.0253

ALA 231 LEU 232 0.0120

LEU 232 PRO 233 0.0207

PRO 233 ASP 234 0.0208

ASP 234 GLY 235 -0.0185

GLY 235 ALA 236 0.0221

ALA 236 LEU 237 0.0238

LEU 237 LYS 238 0.0207

LYS 238 ASP 239 -0.0026

ASP 239 LEU 240 0.0114

LEU 240 ALA 241 0.0107

ALA 241 PRO 242 0.0110

PRO 242 ARG 243 0.0221

ARG 243 VAL 244 0.0084

VAL 244 PHE 245 0.0029

PHE 245 LEU 246 0.0063

LEU 246 GLY 247 0.0233

GLY 247 GLY 248 0.0123

GLY 248 GLN 249 0.0046

GLN 249 GLY 250 0.0124

GLY 250 ALA 251 0.0686

ALA 251 GLY 252 0.0175

GLY 252 PRO 253 0.0255

PRO 253 GLU 254 0.0258

GLU 254 GLU 255 0.0320

GLU 255 ALA 256 0.0096

ALA 256 ARG 257 0.0191

ARG 257 ARG 258 0.0189

ARG 258 LEU 259 0.0269

LEU 259 GLY 260 0.0130

GLY 260 ALA 261 0.0151

ALA 261 GLU 262 0.0117

GLU 262 TYR 263 0.0475

TYR 263 MET 264 0.0161

MET 264 GLU 265 0.0064

GLU 265 ASP 266 0.0144

ASP 266 LEU 267 -0.0715

LEU 267 LYS 268 0.0146

LYS 268 GLY 269 0.0144

GLY 269 LEU 270 0.0040

LEU 270 ALA 271 -0.1161

ALA 271 GLU 272 0.0257

GLU 272 ALA 273 0.0323

ALA 273 LEU 274 0.0034

LEU 274 ASP 82 0.0139

ASP 82 LEU 83 0.0001

LEU 83 GLY 84 0.0011

GLY 84 THR 85 0.0013

THR 85 GLY 86 -0.0347

GLY 86 LEU 87 0.0002

LEU 87 LEU 88 0.0011

LEU 88 GLU 89 0.0009

GLU 89 ALA 90 -0.0368

ALA 90 LEU 91 0.0007

LEU 91 LEU 92 0.0013

LEU 92 ARG 93 0.0013

ARG 93 GLY 94 -0.0384

GLY 94 ASP 95 0.0023

ASP 95 LEU 96 0.0047

LEU 96 ALA 97 0.0033

ALA 97 GLY 98 -0.0314

GLY 98 ALA 99 0.0040

ALA 99 GLU 100 0.0034

GLU 100 ALA 101 0.0027

ALA 101 LEU 102 0.0097

LEU 102 PHE 103 0.0009

PHE 103 ARG 104 0.0010

ARG 104 ARG 105 0.0003

ARG 105 GLY 106 0.0316

GLY 106 LEU 107 0.0002

LEU 107 ARG 108 0.0000

ARG 108 PHE 109 -0.0000

PHE 109 TRP 110 -0.0292

TRP 110 GLY 111 0.0007

GLY 111 PRO 112 0.0008

PRO 112 GLU 113 0.0007

GLU 113 GLY 114 0.0175

GLY 114 VAL 115 0.0002

VAL 115 LEU 116 0.0006

LEU 116 GLU 117 0.0002

GLU 117 HIS 118 0.0328

HIS 118 LEU 119 0.0011

LEU 119 LEU 120 0.0009

LEU 120 LEU 121 0.0008

LEU 121 PRO 122 0.0296

PRO 122 VAL 123 0.0004

VAL 123 LEU 124 0.0004

LEU 124 ARG 125 0.0002

ARG 125 GLU 126 0.0187

GLU 126 VAL 127 0.0002

VAL 127 GLY 128 0.0002

GLY 128 GLU 129 0.0001

GLU 129 ALA 130 0.0303

ALA 130 TRP 131 0.0003

TRP 131 HIS 132 0.0006

HIS 132 ARG 133 0.0003

ARG 133 GLY 134 0.0014

GLY 134 GLU 135 0.0006

GLU 135 ILE 136 0.0005

ILE 136 GLY 137 0.0005

GLY 137 VAL 138 -0.0244

VAL 138 ALA 139 0.0014

ALA 139 GLU 140 0.0005

GLU 140 GLU 141 0.0014

GLU 141 HIS 142 -0.0324

HIS 142 LEU 143 0.0004

LEU 143 ALA 144 0.0005

ALA 144 SER 145 0.0003

SER 145 THR 146 -0.0499

THR 146 PHE 147 0.0004

PHE 147 LEU 148 0.0003

LEU 148 ARG 149 0.0004

ARG 149 ALA 150 -0.0640

ALA 150 ARG 151 0.0005

ARG 151 LEU 152 0.0001

LEU 152 GLN 153 0.0006

GLN 153 GLU 154 -0.0031

GLU 154 LEU 155 0.0006

LEU 155 LEU 156 0.0005

LEU 156 ASP 157 0.0004

ASP 157 LEU 158 -0.0027

LEU 158 ALA 159 0.0067

ALA 159 GLY 160 0.0075

GLY 160 PHE 161 0.0012

PHE 161 PRO 162 -0.0192

PRO 162 PRO 163 0.0031

PRO 163 GLY 164 0.0002

GLY 164 PRO 165 0.0016

PRO 165 PRO 166 -0.0006

PRO 166 VAL 167 0.0042

VAL 167 LEU 168 0.0032

LEU 168 VAL 169 0.0013

VAL 169 THR 170 0.0364

THR 170 THR 171 0.0034

THR 171 PRO 172 0.0047

PRO 172 PRO 173 0.0040

PRO 173 GLY 174 0.0210

GLY 174 GLU 175 0.0021

GLU 175 ARG 176 0.0013

ARG 176 HIS 177 0.0018

HIS 177 GLU 178 -0.0166

GLU 178 ILE 179 0.0013

ILE 179 GLY 180 0.0010

GLY 180 ALA 181 0.0005

ALA 181 MET 182 -0.0673

MET 182 LEU 183 0.0020

LEU 183 ALA 184 -0.0000

ALA 184 ALA 185 0.0020

ALA 185 TYR 186 -0.0105

TYR 186 HIS 187 0.0025

HIS 187 LEU 188 0.0006

LEU 188 ARG 189 0.0020

ARG 189 ARG 190 0.0208

ARG 190 LYS 191 0.0079

LYS 191 GLY 192 0.0073

GLY 192 VAL 193 0.0024

VAL 193 PRO 194 0.0200

PRO 194 ALA 195 0.0025

ALA 195 LEU 196 0.0041

LEU 196 TYR 197 0.0010

TYR 197 LEU 198 0.0495

LEU 198 GLY 199 0.0011

GLY 199 PRO 200 0.0022

PRO 200 ASP 201 0.0018

ASP 201 THR 202 -0.0043

THR 202 PRO 203 0.0068

PRO 203 LEU 204 0.0037

LEU 204 PRO 205 0.0046

PRO 205 ASP 206 -0.0022

ASP 206 LEU 207 0.0086

LEU 207 ARG 208 0.0001

ARG 208 ALA 209 0.0081

ALA 209 LEU 210 -0.0247

LEU 210 ALA 211 0.0077

ALA 211 ARG 212 0.0021

ARG 212 ARG 213 0.0086

ARG 213 LEU 214 0.0119

LEU 214 GLY 215 0.0054

GLY 215 ALA 216 0.0050

ALA 216 GLY 217 0.0103

GLY 217 ALA 218 0.0459

ALA 218 VAL 219 0.0019

VAL 219 VAL 220 0.0008

VAL 220 LEU 221 0.0023

LEU 221 SER 222 0.0093

SER 222 ALA 223 0.0027

ALA 223 VAL 224 0.0006

VAL 224 LEU 225 0.0038

LEU 225 SER 226 0.0115

SER 226 GLU 227 0.0072

GLU 227 PRO 228 0.0027

PRO 228 LEU 229 0.0048

LEU 229 ARG 230 -0.0031

ARG 230 ALA 231 0.0098

ALA 231 LEU 232 0.0013

LEU 232 PRO 233 0.0049

PRO 233 ASP 234 0.0024

ASP 234 GLY 235 0.0067

GLY 235 ALA 236 0.0086

ALA 236 LEU 237 0.0102

LEU 237 LYS 238 0.0034

LYS 238 ASP 239 0.0060

ASP 239 LEU 240 0.0043

LEU 240 ALA 241 0.0070

ALA 241 PRO 242 0.0425

PRO 242 ARG 243 0.0018

ARG 243 VAL 244 0.0018

VAL 244 PHE 245 0.0017

PHE 245 LEU 246 0.0361

LEU 246 GLY 247 0.0010

GLY 247 GLY 248 0.0010

GLY 248 GLN 249 0.0011

GLN 249 GLY 250 -0.0541

GLY 250 ALA 251 0.0035

ALA 251 GLY 252 0.0089

GLY 252 PRO 253 0.0040

PRO 253 GLU 254 -0.0275

GLU 254 GLU 255 0.0095

GLU 255 ALA 256 0.0059

ALA 256 ARG 257 0.0057

ARG 257 ARG 258 0.0094

ARG 258 LEU 259 0.0083

LEU 259 GLY 260 0.0031

GLY 260 ALA 261 0.0067

ALA 261 GLU 262 -0.0282

GLU 262 TYR 263 0.0004

TYR 263 MET 264 0.0034

MET 264 GLU 265 0.0011

GLU 265 ASP 266 -0.1191

ASP 266 LEU 267 0.0090

LEU 267 LYS 268 0.0084

LYS 268 GLY 269 0.0049

GLY 269 LEU 270 0.0053

LEU 270 ALA 271 0.0048

ALA 271 GLU 272 0.0038

GLU 272 ALA 273 0.0036

ALA 273 LEU 274 0.0408

LEU 274 ALA 275 0.0040

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.

*** DARK TET ***

CA strain for 22022316112813361

--- normal mode 10 ---

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

* DARK TET *