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

* DARK TET *

CA strain for 22022316112813361

--- normal mode 11 ---

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 0.0066

GLU 81 ASP 82 0.0158

ASP 82 LEU 83 0.0011

LEU 83 GLY 84 -0.0573

GLY 84 THR 85 0.0034

THR 85 GLY 86 0.0014

GLY 86 LEU 87 0.0025

LEU 87 LEU 88 0.0084

LEU 88 GLU 89 0.0005

GLU 89 ALA 90 0.0020

ALA 90 LEU 91 0.0016

LEU 91 LEU 92 0.0505

LEU 92 ARG 93 0.0006

ARG 93 GLY 94 0.0012

GLY 94 ASP 95 0.0015

ASP 95 LEU 96 0.0081

LEU 96 ALA 97 0.0018

ALA 97 GLY 98 0.0012

GLY 98 ALA 99 0.0006

ALA 99 GLU 100 0.0196

GLU 100 ALA 101 0.0013

ALA 101 LEU 102 0.0004

LEU 102 PHE 103 0.0016

PHE 103 ARG 104 0.0037

ARG 104 ARG 105 0.0016

ARG 105 GLY 106 0.0023

GLY 106 LEU 107 0.0002

LEU 107 ARG 108 -0.0271

ARG 108 PHE 109 0.0017

PHE 109 TRP 110 0.0035

TRP 110 GLY 111 0.0037

GLY 111 PRO 112 -0.1695

PRO 112 GLU 113 0.0027

GLU 113 GLY 114 0.0004

GLY 114 VAL 115 0.0024

VAL 115 LEU 116 -0.0639

LEU 116 GLU 117 0.0018

GLU 117 HIS 118 0.0025

HIS 118 LEU 119 0.0044

LEU 119 LEU 120 0.0039

LEU 120 LEU 121 0.0027

LEU 121 PRO 122 0.0013

PRO 122 VAL 123 0.0023

VAL 123 LEU 124 0.0092

LEU 124 ARG 125 0.0009

ARG 125 GLU 126 0.0022

GLU 126 VAL 127 0.0004

VAL 127 GLY 128 0.0393

GLY 128 GLU 129 0.0021

GLU 129 ALA 130 0.0005

ALA 130 TRP 131 0.0018

TRP 131 HIS 132 -0.0176

HIS 132 ARG 133 0.0028

ARG 133 GLY 134 -0.0000

GLY 134 GLU 135 0.0029

GLU 135 ILE 136 0.0398

ILE 136 GLY 137 0.0115

GLY 137 VAL 138 0.0057

VAL 138 ALA 139 0.0079

ALA 139 GLU 140 0.0339

GLU 140 GLU 141 0.0015

GLU 141 HIS 142 0.0003

HIS 142 LEU 143 0.0015

LEU 143 ALA 144 0.0193

ALA 144 SER 145 0.0003

SER 145 THR 146 0.0002

THR 146 PHE 147 -0.0001

PHE 147 LEU 148 0.0155

LEU 148 ARG 149 0.0001

ARG 149 ALA 150 0.0005

ALA 150 ARG 151 0.0003

ARG 151 LEU 152 0.0406

LEU 152 GLN 153 0.0001

GLN 153 GLU 154 0.0012

GLU 154 LEU 155 0.0012

LEU 155 LEU 156 -0.0023

LEU 156 ASP 157 0.0010

ASP 157 LEU 158 0.0020

LEU 158 ALA 159 0.0022

ALA 159 GLY 160 -0.0139

GLY 160 PHE 161 0.0016

PHE 161 PRO 162 0.0028

PRO 162 PRO 163 0.0001

PRO 163 GLY 164 0.0201

GLY 164 PRO 165 0.0075

PRO 165 PRO 166 0.0045

PRO 166 VAL 167 0.0064

VAL 167 LEU 168 -0.0263

LEU 168 VAL 169 0.0008

VAL 169 THR 170 0.0058

THR 170 THR 171 0.0054

THR 171 PRO 172 -0.0212

PRO 172 PRO 173 0.0097

PRO 173 GLY 174 0.0010

GLY 174 GLU 175 0.0087

GLU 175 ARG 176 -0.1870

ARG 176 HIS 177 0.0002

HIS 177 GLU 178 0.0017

GLU 178 ILE 179 0.0002

ILE 179 GLY 180 0.0363

GLY 180 ALA 181 0.0001

ALA 181 MET 182 0.0035

MET 182 LEU 183 0.0018

LEU 183 ALA 184 0.0060

ALA 184 ALA 185 0.0013

ALA 185 TYR 186 0.0018

TYR 186 HIS 187 0.0021

HIS 187 LEU 188 -0.0329

LEU 188 ARG 189 0.0020

ARG 189 ARG 190 0.0013

ARG 190 LYS 191 0.0033

LYS 191 GLY 192 -0.0769

GLY 192 VAL 193 0.0031

VAL 193 PRO 194 0.0024

PRO 194 ALA 195 0.0031

ALA 195 LEU 196 -0.0292

LEU 196 TYR 197 0.0018

TYR 197 LEU 198 0.0039

LEU 198 GLY 199 0.0010

GLY 199 PRO 200 -0.0081

PRO 200 ASP 201 0.0053

ASP 201 THR 202 0.0006

THR 202 PRO 203 0.0047

PRO 203 LEU 204 -0.1166

LEU 204 PRO 205 0.0049

PRO 205 ASP 206 0.0125

ASP 206 LEU 207 0.0114

LEU 207 ARG 208 -0.0411

ARG 208 ALA 209 0.0128

ALA 209 LEU 210 0.0077

LEU 210 ALA 211 0.0160

ALA 211 ARG 212 -0.0339

ARG 212 ARG 213 0.0162

ARG 213 LEU 214 0.0059

LEU 214 GLY 215 0.0139

GLY 215 ALA 216 -0.0113

ALA 216 GLY 217 0.0121

GLY 217 ALA 218 0.0076

ALA 218 VAL 219 0.0097

VAL 219 VAL 220 -0.0135

VAL 220 LEU 221 0.0060

LEU 221 SER 222 0.0002

SER 222 ALA 223 0.0082

ALA 223 VAL 224 -0.0102

VAL 224 LEU 225 0.0152

LEU 225 SER 226 0.0177

SER 226 GLU 227 0.0170

GLU 227 PRO 228 0.0483

PRO 228 LEU 229 0.0187

LEU 229 ARG 230 0.0192

ARG 230 ALA 231 0.0163

ALA 231 LEU 232 0.0222

LEU 232 PRO 233 0.0111

PRO 233 ASP 234 0.0203

ASP 234 GLY 235 0.0160

GLY 235 ALA 236 0.0084

ALA 236 LEU 237 0.0217

LEU 237 LYS 238 0.0123

LYS 238 ASP 239 0.0129

ASP 239 LEU 240 0.0025

LEU 240 ALA 241 0.0146

ALA 241 PRO 242 0.0138

PRO 242 ARG 243 0.0011

ARG 243 VAL 244 0.0073

VAL 244 PHE 245 0.0003

PHE 245 LEU 246 0.0058

LEU 246 GLY 247 0.0004

GLY 247 GLY 248 -0.0570

GLY 248 GLN 249 0.0026

GLN 249 GLY 250 0.0137

GLY 250 ALA 251 0.0123

ALA 251 GLY 252 -0.0833

GLY 252 PRO 253 0.0135

PRO 253 GLU 254 0.0168

GLU 254 GLU 255 0.0172

GLU 255 ALA 256 -0.0095

ALA 256 ARG 257 0.0144

ARG 257 ARG 258 0.0194

ARG 258 LEU 259 0.0184

LEU 259 GLY 260 0.0210

GLY 260 ALA 261 0.0133

ALA 261 GLU 262 0.0136

GLU 262 TYR 263 0.0004

TYR 263 MET 264 0.0871

MET 264 GLU 265 0.0005

GLU 265 ASP 266 0.0100

ASP 266 LEU 267 0.0081

LEU 267 LYS 268 -0.0313

LYS 268 GLY 269 0.0027

GLY 269 LEU 270 0.0029

LEU 270 ALA 271 0.0053

ALA 271 GLU 272 0.0249

GLU 272 ALA 273 0.0063

ALA 273 LEU 274 0.0052

LEU 274 ASP 82 0.0449

ASP 82 LEU 83 0.0028

LEU 83 GLY 84 0.0064

GLY 84 THR 85 0.0069

THR 85 GLY 86 0.0221

GLY 86 LEU 87 0.0050

LEU 87 LEU 88 0.0050

LEU 88 GLU 89 0.0045

GLU 89 ALA 90 0.0066

ALA 90 LEU 91 0.0041

LEU 91 LEU 92 0.0026

LEU 92 ARG 93 0.0028

ARG 93 GLY 94 -0.0261

GLY 94 ASP 95 0.0050

ASP 95 LEU 96 0.0060

LEU 96 ALA 97 0.0061

ALA 97 GLY 98 0.1049

GLY 98 ALA 99 0.0067

ALA 99 GLU 100 0.0078

GLU 100 ALA 101 0.0067

ALA 101 LEU 102 0.0984

LEU 102 PHE 103 0.0033

PHE 103 ARG 104 0.0032

ARG 104 ARG 105 0.0023

ARG 105 GLY 106 0.1441

GLY 106 LEU 107 0.0027

LEU 107 ARG 108 0.0005

ARG 108 PHE 109 0.0027

PHE 109 TRP 110 0.0422

TRP 110 GLY 111 0.0027

GLY 111 PRO 112 0.0032

PRO 112 GLU 113 0.0021

GLU 113 GLY 114 -0.0211

GLY 114 VAL 115 0.0012

VAL 115 LEU 116 0.0038

LEU 116 GLU 117 0.0006

GLU 117 HIS 118 0.0210

HIS 118 LEU 119 0.0010

LEU 119 LEU 120 0.0022

LEU 120 LEU 121 0.0014

LEU 121 PRO 122 0.0089

PRO 122 VAL 123 0.0016

VAL 123 LEU 124 0.0060

LEU 124 ARG 125 0.0010

ARG 125 GLU 126 0.0259

GLU 126 VAL 127 0.0023

VAL 127 GLY 128 0.0090

GLY 128 GLU 129 0.0075

GLU 129 ALA 130 0.0210

ALA 130 TRP 131 0.0115

TRP 131 HIS 132 0.0070

HIS 132 ARG 133 0.0150

ARG 133 GLY 134 -0.0171

GLY 134 GLU 135 0.0172

GLU 135 ILE 136 0.0165

ILE 136 GLY 137 0.0111

GLY 137 VAL 138 0.1166

VAL 138 ALA 139 0.0072

ALA 139 GLU 140 0.0072

GLU 140 GLU 141 0.0019

GLU 141 HIS 142 0.0374

HIS 142 LEU 143 0.0033

LEU 143 ALA 144 0.0009

ALA 144 SER 145 0.0025

SER 145 THR 146 0.0027

THR 146 PHE 147 0.0011

PHE 147 LEU 148 0.0002

LEU 148 ARG 149 0.0015

ARG 149 ALA 150 -0.0501

ALA 150 ARG 151 0.0000

ARG 151 LEU 152 0.0013

LEU 152 GLN 153 0.0004

GLN 153 GLU 154 -0.0610

GLU 154 LEU 155 -0.0000

LEU 155 LEU 156 0.0007

LEU 156 ASP 157 0.0004

ASP 157 LEU 158 -0.0147

LEU 158 ALA 159 0.0078

ALA 159 GLY 160 0.0042

GLY 160 PHE 161 0.0033

PHE 161 PRO 162 0.1198

PRO 162 PRO 163 0.0084

PRO 163 GLY 164 0.0118

GLY 164 PRO 165 0.0112

PRO 165 PRO 166 -0.0490

PRO 166 VAL 167 0.0071

VAL 167 LEU 168 0.0155

LEU 168 VAL 169 0.0061

VAL 169 THR 170 -0.0138

THR 170 THR 171 0.0154

THR 171 PRO 172 0.0185

PRO 172 PRO 173 0.0124

PRO 173 GLY 174 -0.0700

GLY 174 GLU 175 0.0043

GLU 175 ARG 176 0.0028

ARG 176 HIS 177 0.0034

HIS 177 GLU 178 0.0409

GLU 178 ILE 179 0.0050

ILE 179 GLY 180 0.0069

GLY 180 ALA 181 0.0033

ALA 181 MET 182 0.0283

MET 182 LEU 183 0.0013

LEU 183 ALA 184 0.0097

ALA 184 ALA 185 0.0025

ALA 185 TYR 186 0.0262

TYR 186 HIS 187 0.0059

HIS 187 LEU 188 0.0058

LEU 188 ARG 189 0.0091

ARG 189 ARG 190 -0.0275

ARG 190 LYS 191 0.0219

LYS 191 GLY 192 0.0056

GLY 192 VAL 193 0.0150

VAL 193 PRO 194 -0.0414

PRO 194 ALA 195 0.0092

ALA 195 LEU 196 0.0073

LEU 196 TYR 197 0.0080

TYR 197 LEU 198 -0.0417

LEU 198 GLY 199 0.0081

GLY 199 PRO 200 0.0084

PRO 200 ASP 201 0.0076

ASP 201 THR 202 -0.0116

THR 202 PRO 203 0.0240

PRO 203 LEU 204 0.0357

LEU 204 PRO 205 0.0003

PRO 205 ASP 206 0.0629

ASP 206 LEU 207 0.0121

LEU 207 ARG 208 0.0213

ARG 208 ALA 209 0.0070

ALA 209 LEU 210 0.1232

LEU 210 ALA 211 0.0354

ALA 211 ARG 212 0.0063

ARG 212 ARG 213 0.0316

ARG 213 LEU 214 0.0113

LEU 214 GLY 215 0.0383

GLY 215 ALA 216 0.0014

ALA 216 GLY 217 0.0287

GLY 217 ALA 218 -0.0562

ALA 218 VAL 219 0.0234

VAL 219 VAL 220 0.0074

VAL 220 LEU 221 0.0226

LEU 221 SER 222 -0.0087

SER 222 ALA 223 0.0166

ALA 223 VAL 224 0.0158

VAL 224 LEU 225 0.0206

LEU 225 SER 226 -0.0642

SER 226 GLU 227 0.0249

GLU 227 PRO 228 0.0091

PRO 228 LEU 229 0.0332

LEU 229 ARG 230 0.0761

ARG 230 ALA 231 0.0104

ALA 231 LEU 232 0.0343

LEU 232 PRO 233 0.0424

PRO 233 ASP 234 0.0083

ASP 234 GLY 235 0.0406

GLY 235 ALA 236 0.0360

ALA 236 LEU 237 0.0415

LEU 237 LYS 238 0.0077

LYS 238 ASP 239 0.0114

ASP 239 LEU 240 0.0432

LEU 240 ALA 241 0.0434

ALA 241 PRO 242 -0.1017

PRO 242 ARG 243 0.0047

ARG 243 VAL 244 0.0294

VAL 244 PHE 245 0.0081

PHE 245 LEU 246 -0.0366

LEU 246 GLY 247 0.0185

GLY 247 GLY 248 0.0315

GLY 248 GLN 249 0.0176

GLN 249 GLY 250 0.0533

GLY 250 ALA 251 0.0395

ALA 251 GLY 252 0.0178

GLY 252 PRO 253 0.0392

PRO 253 GLU 254 0.1098

GLU 254 GLU 255 0.0177

GLU 255 ALA 256 0.0341

ALA 256 ARG 257 0.0401

ARG 257 ARG 258 0.0409

ARG 258 LEU 259 0.0179

LEU 259 GLY 260 0.0349

GLY 260 ALA 261 0.0333

ALA 261 GLU 262 0.0681

GLU 262 TYR 263 0.0214

TYR 263 MET 264 0.0347

MET 264 GLU 265 0.0208

GLU 265 ASP 266 0.1408

ASP 266 LEU 267 0.0052

LEU 267 LYS 268 0.0132

LYS 268 GLY 269 0.0158

GLY 269 LEU 270 0.0267

LEU 270 ALA 271 0.0361

ALA 271 GLU 272 0.0159

GLU 272 ALA 273 0.0370

ALA 273 LEU 274 -0.0558

LEU 274 TRP 275 0.0635

TRP 275 LEU 276 0.0528

LEU 276 PRO 277 0.0512

PRO 277 ARG 278 -0.0492

ARG 278 ARG 79 0.1948

ARG 79 PRO 80 0.0143

PRO 80 GLU 81 0.0140

GLU 81 ASP 82 0.0225

ASP 82 LEU 83 0.0453

LEU 83 GLY 84 0.0099

GLY 84 THR 85 0.0109

THR 85 GLY 86 0.0101

GLY 86 LEU 87 0.0218

LEU 87 LEU 88 0.0020

LEU 88 GLU 89 0.0024

GLU 89 ALA 90 0.0035

ALA 90 LEU 91 -0.0327

LEU 91 LEU 92 0.0006

LEU 92 ARG 93 0.0040

ARG 93 GLY 94 0.0029

GLY 94 ASP 95 -0.1443

ASP 95 LEU 96 0.0026

LEU 96 ALA 97 0.0022

ALA 97 GLY 98 0.0015

GLY 98 ALA 99 0.1057

ALA 99 GLU 100 0.0021

GLU 100 ALA 101 0.0033

ALA 101 LEU 102 0.0007

LEU 102 PHE 103 -0.0460

PHE 103 ARG 104 0.0029

ARG 104 ARG 105 0.0031

ARG 105 GLY 106 0.0042

GLY 106 LEU 107 -0.0059

LEU 107 ARG 108 0.0058

ARG 108 PHE 109 0.0007

PHE 109 TRP 110 0.0045

TRP 110 GLY 111 0.1128

GLY 111 PRO 112 0.0018

PRO 112 GLU 113 0.0065

GLU 113 GLY 114 0.0005

GLY 114 VAL 115 -0.0383

VAL 115 LEU 116 0.0053

LEU 116 GLU 117 0.0007

GLU 117 HIS 118 0.0041

HIS 118 LEU 119 -0.0910

LEU 119 LEU 120 0.0018

LEU 120 LEU 121 0.0031

LEU 121 PRO 122 0.0012

PRO 122 VAL 123 -0.0244

VAL 123 LEU 124 0.0031

LEU 124 ARG 125 0.0012

ARG 125 GLU 126 0.0040

GLU 126 VAL 127 0.0077

VAL 127 GLY 128 0.0025

GLY 128 GLU 129 0.0019

GLU 129 ALA 130 0.0016

ALA 130 TRP 131 -0.0063

TRP 131 HIS 132 0.0045

HIS 132 ARG 133 0.0055

ARG 133 GLY 134 0.0006

GLY 134 GLU 135 0.0958

GLU 135 ILE 136 0.0054

ILE 136 GLY 137 0.0106

GLY 137 VAL 138 0.0046

VAL 138 ALA 139 -0.0100

ALA 139 GLU 140 0.0061

GLU 140 GLU 141 0.0059

GLU 141 HIS 142 0.0017

HIS 142 LEU 143 0.0417

LEU 143 ALA 144 0.0026

ALA 144 SER 145 0.0021

SER 145 THR 146 0.0013

THR 146 PHE 147 -0.0096

PHE 147 LEU 148 0.0002

LEU 148 ARG 149 0.0003

ARG 149 ALA 150 0.0004

ALA 150 ARG 151 -0.0094

ARG 151 LEU 152 0.0005

LEU 152 GLN 153 0.0004

GLN 153 GLU 154 0.0003

GLU 154 LEU 155 -0.1218

LEU 155 LEU 156 0.0016

LEU 156 ASP 157 0.0013

ASP 157 LEU 158 0.0026

LEU 158 ALA 159 -0.0680

ALA 159 GLY 160 0.0012

GLY 160 PHE 161 0.0016

PHE 161 PRO 162 0.0031

PRO 162 PRO 163 -0.0031

PRO 163 GLY 164 0.0036

GLY 164 PRO 165 0.0035

PRO 165 PRO 166 0.0045

PRO 166 VAL 167 0.0301

VAL 167 LEU 168 0.0088

LEU 168 VAL 169 0.0007

VAL 169 THR 170 0.0083

THR 170 THR 171 -0.0122

THR 171 PRO 172 0.0110

PRO 172 PRO 173 0.0114

PRO 173 GLY 174 0.0028

GLY 174 GLU 175 -0.0368

GLU 175 ARG 176 0.0010

ARG 176 HIS 177 0.0004

HIS 177 GLU 178 0.0015

GLU 178 ILE 179 0.0249

ILE 179 GLY 180 0.0038

GLY 180 ALA 181 0.0004

ALA 181 MET 182 0.0037

MET 182 LEU 183 -0.0004

LEU 183 ALA 184 0.0029

ALA 184 ALA 185 0.0020

ALA 185 TYR 186 0.0018

TYR 186 HIS 187 -0.0520

HIS 187 LEU 188 0.0012

LEU 188 ARG 189 0.0040

ARG 189 ARG 190 0.0019

ARG 190 LYS 191 -0.0311

LYS 191 GLY 192 0.0001

GLY 192 VAL 193 0.0043

VAL 193 PRO 194 0.0025

PRO 194 ALA 195 0.0309

ALA 195 LEU 196 0.0058

LEU 196 TYR 197 0.0024

TYR 197 LEU 198 0.0054

LEU 198 GLY 199 -0.0219

GLY 199 PRO 200 0.0020

PRO 200 ASP 201 0.0026

ASP 201 THR 202 0.0003

THR 202 PRO 203 0.0443

PRO 203 LEU 204 0.0175

LEU 204 PRO 205 0.0021

PRO 205 ASP 206 0.0189

ASP 206 LEU 207 0.0447

LEU 207 ARG 208 0.0078

ARG 208 ALA 209 0.0110

ALA 209 LEU 210 0.0123

LEU 210 ALA 211 0.0995

ALA 211 ARG 212 0.0002

ARG 212 ARG 213 0.0174

ARG 213 LEU 214 0.0095

LEU 214 GLY 215 0.0040

GLY 215 ALA 216 0.0017

ALA 216 GLY 217 0.0194

GLY 217 ALA 218 0.0109

ALA 218 VAL 219 0.0441

VAL 219 VAL 220 0.0006

VAL 220 LEU 221 0.0084

LEU 221 SER 222 0.0014

SER 222 ALA 223 -0.0554

ALA 223 VAL 224 0.0053

VAL 224 LEU 225 0.0156

LEU 225 SER 226 0.0166

SER 226 GLU 227 -0.0470

GLU 227 PRO 228 0.0039

PRO 228 LEU 229 0.0269

LEU 229 ARG 230 0.0228

ARG 230 ALA 231 -0.0258

ALA 231 LEU 232 0.0099

LEU 232 PRO 233 0.0181

PRO 233 ASP 234 0.0237

ASP 234 GLY 235 -0.0014

GLY 235 ALA 236 0.0281

ALA 236 LEU 237 0.0273

LEU 237 LYS 238 0.0196

LYS 238 ASP 239 0.0030

ASP 239 LEU 240 0.0150

LEU 240 ALA 241 0.0172

ALA 241 PRO 242 0.0170

PRO 242 ARG 243 0.0184

ARG 243 VAL 244 0.0103

VAL 244 PHE 245 0.0005

PHE 245 LEU 246 0.0078

LEU 246 GLY 247 0.0302

GLY 247 GLY 248 0.0091

GLY 248 GLN 249 0.0041

GLN 249 GLY 250 0.0113

GLY 250 ALA 251 0.0831

ALA 251 GLY 252 0.0267

GLY 252 PRO 253 0.0241

PRO 253 GLU 254 0.0292

GLU 254 GLU 255 0.0287

GLU 255 ALA 256 0.0133

ALA 256 ARG 257 0.0195

ARG 257 ARG 258 0.0217

ARG 258 LEU 259 0.0262

LEU 259 GLY 260 0.0152

GLY 260 ALA 261 0.0158

ALA 261 GLU 262 0.0158

GLU 262 TYR 263 0.0316

TYR 263 MET 264 0.0153

MET 264 GLU 265 0.0022

GLU 265 ASP 266 0.0178

ASP 266 LEU 267 -0.0793

LEU 267 LYS 268 0.0134

LYS 268 GLY 269 0.0111

GLY 269 LEU 270 0.0044

LEU 270 ALA 271 -0.0482

ALA 271 GLU 272 0.0183

GLU 272 ALA 273 0.0159

ALA 273 LEU 274 0.0052

LEU 274 ASP 82 -0.0326

ASP 82 LEU 83 0.0028

LEU 83 GLY 84 0.0050

GLY 84 THR 85 0.0047

THR 85 GLY 86 -0.0263

GLY 86 LEU 87 0.0044

LEU 87 LEU 88 0.0045

LEU 88 GLU 89 0.0036

GLU 89 ALA 90 0.0028

ALA 90 LEU 91 0.0039

LEU 91 LEU 92 0.0017

LEU 92 ARG 93 0.0026

ARG 93 GLY 94 0.0223

GLY 94 ASP 95 0.0035

ASP 95 LEU 96 0.0034

LEU 96 ALA 97 0.0037

ALA 97 GLY 98 -0.0927

GLY 98 ALA 99 0.0041

ALA 99 GLU 100 0.0050

GLU 100 ALA 101 0.0046

ALA 101 LEU 102 -0.0747

LEU 102 PHE 103 0.0031

PHE 103 ARG 104 0.0035

ARG 104 ARG 105 0.0026

ARG 105 GLY 106 -0.1284

GLY 106 LEU 107 0.0017

LEU 107 ARG 108 0.0003

ARG 108 PHE 109 0.0014

PHE 109 TRP 110 -0.0319

TRP 110 GLY 111 0.0039

GLY 111 PRO 112 0.0037

PRO 112 GLU 113 0.0030

GLU 113 GLY 114 0.0313

GLY 114 VAL 115 0.0003

VAL 115 LEU 116 0.0036

LEU 116 GLU 117 0.0012

GLU 117 HIS 118 0.0068

HIS 118 LEU 119 0.0002

LEU 119 LEU 120 0.0021

LEU 120 LEU 121 0.0022

LEU 121 PRO 122 0.0239

PRO 122 VAL 123 0.0016

VAL 123 LEU 124 0.0058

LEU 124 ARG 125 0.0013

ARG 125 GLU 126 0.0151

GLU 126 VAL 127 0.0022

VAL 127 GLY 128 0.0109

GLY 128 GLU 129 0.0081

GLU 129 ALA 130 -0.0041

ALA 130 TRP 131 0.0115

TRP 131 HIS 132 0.0096

HIS 132 ARG 133 0.0170

ARG 133 GLY 134 0.0338

GLY 134 GLU 135 0.0216

GLU 135 ILE 136 0.0204

ILE 136 GLY 137 0.0133

GLY 137 VAL 138 -0.1262

VAL 138 ALA 139 0.0069

ALA 139 GLU 140 0.0067

GLU 140 GLU 141 0.0021

GLU 141 HIS 142 -0.0294

HIS 142 LEU 143 0.0025

LEU 143 ALA 144 0.0010

ALA 144 SER 145 0.0019

SER 145 THR 146 -0.0009

THR 146 PHE 147 0.0014

PHE 147 LEU 148 0.0003

LEU 148 ARG 149 0.0016

ARG 149 ALA 150 0.0319

ALA 150 ARG 151 0.0004

ARG 151 LEU 152 0.0026

LEU 152 GLN 153 0.0007

GLN 153 GLU 154 0.0608

GLU 154 LEU 155 0.0002

LEU 155 LEU 156 0.0019

LEU 156 ASP 157 0.0017

ASP 157 LEU 158 0.0209

LEU 158 ALA 159 0.0162

ALA 159 GLY 160 0.0098

GLY 160 PHE 161 0.0055

PHE 161 PRO 162 -0.0584

PRO 162 PRO 163 0.0100

PRO 163 GLY 164 0.0163

GLY 164 PRO 165 0.0145

PRO 165 PRO 166 0.0650

PRO 166 VAL 167 0.0100

VAL 167 LEU 168 0.0210

LEU 168 VAL 169 0.0051

VAL 169 THR 170 0.0608

THR 170 THR 171 0.0192

THR 171 PRO 172 0.0240

PRO 172 PRO 173 0.0197

PRO 173 GLY 174 0.1054

GLY 174 GLU 175 0.0052

GLU 175 ARG 176 0.0057

ARG 176 HIS 177 0.0038

HIS 177 GLU 178 -0.0079

GLU 178 ILE 179 0.0060

ILE 179 GLY 180 0.0115

GLY 180 ALA 181 0.0032

ALA 181 MET 182 -0.0351

MET 182 LEU 183 0.0021

LEU 183 ALA 184 0.0123

ALA 184 ALA 185 0.0042

ALA 185 TYR 186 -0.0277

TYR 186 HIS 187 0.0085

HIS 187 LEU 188 0.0085

LEU 188 ARG 189 0.0142

ARG 189 ARG 190 0.0374

ARG 190 LYS 191 0.0351

LYS 191 GLY 192 0.0136

GLY 192 VAL 193 0.0187

VAL 193 PRO 194 0.0483

PRO 194 ALA 195 0.0122

ALA 195 LEU 196 0.0117

LEU 196 TYR 197 0.0104

TYR 197 LEU 198 0.0607

LEU 198 GLY 199 0.0088

GLY 199 PRO 200 0.0102

PRO 200 ASP 201 0.0097

ASP 201 THR 202 0.0093

THR 202 PRO 203 0.0309

PRO 203 LEU 204 0.0467

LEU 204 PRO 205 0.0004

PRO 205 ASP 206 0.0173

ASP 206 LEU 207 0.0221

LEU 207 ARG 208 0.0270

ARG 208 ALA 209 0.0195

ALA 209 LEU 210 -0.0802

LEU 210 ALA 211 0.0393

ALA 211 ARG 212 0.0016

ARG 212 ARG 213 0.0394

ARG 213 LEU 214 0.0081

LEU 214 GLY 215 0.0470

GLY 215 ALA 216 0.0020

ALA 216 GLY 217 0.0440

GLY 217 ALA 218 0.1076

ALA 218 VAL 219 0.0269

VAL 219 VAL 220 0.0057

VAL 220 LEU 221 0.0258

LEU 221 SER 222 0.0395

SER 222 ALA 223 0.0195

ALA 223 VAL 224 0.0154

VAL 224 LEU 225 0.0248

LEU 225 SER 226 0.1671

SER 226 GLU 227 0.0361

GLU 227 PRO 228 0.0074

PRO 228 LEU 229 0.0459

LEU 229 ARG 230 0.0509

ARG 230 ALA 231 0.0230

ALA 231 LEU 232 0.0374

LEU 232 PRO 233 0.0497

PRO 233 ASP 234 0.0410

ASP 234 GLY 235 0.0520

GLY 235 ALA 236 0.0549

ALA 236 LEU 237 0.0545

LEU 237 LYS 238 0.0504

LYS 238 ASP 239 0.0307

ASP 239 LEU 240 0.0495

LEU 240 ALA 241 0.0492

ALA 241 PRO 242 0.1526

PRO 242 ARG 243 0.0054

ARG 243 VAL 244 0.0281

VAL 244 PHE 245 0.0054

PHE 245 LEU 246 0.0713

LEU 246 GLY 247 0.0196

GLY 247 GLY 248 0.0380

GLY 248 GLN 249 0.0207

GLN 249 GLY 250 -0.0014

GLY 250 ALA 251 0.0516

ALA 251 GLY 252 0.0359

GLY 252 PRO 253 0.0521

PRO 253 GLU 254 0.0114

GLU 254 GLU 255 0.0336

GLU 255 ALA 256 0.0465

ALA 256 ARG 257 0.0554

ARG 257 ARG 258 0.0499

ARG 258 LEU 259 0.0313

LEU 259 GLY 260 0.0439

GLY 260 ALA 261 0.0383

ALA 261 GLU 262 -0.0256

GLU 262 TYR 263 0.0172

TYR 263 MET 264 0.0369

MET 264 GLU 265 0.0086

GLU 265 ASP 266 -0.1121

ASP 266 LEU 267 0.0188

LEU 267 LYS 268 0.0386

LYS 268 GLY 269 0.0396

GLY 269 LEU 270 0.0224

LEU 270 ALA 271 0.0307

ALA 271 GLU 272 0.0272

GLU 272 ALA 273 0.0285

ALA 273 LEU 274 0.0706

LEU 274 ALA 275 0.0371

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 11 ---

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

* DARK TET *