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

* DARK TET *

CA strain for 22022316112813361

--- 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
PRO 80 GLU 81 0.0065

GLU 81 ASP 82 0.0028

ASP 82 LEU 83 0.0045

LEU 83 GLY 84 0.1017

GLY 84 THR 85 0.0023

THR 85 GLY 86 0.0024

GLY 86 LEU 87 0.0027

LEU 87 LEU 88 0.0627

LEU 88 GLU 89 0.0012

GLU 89 ALA 90 0.0050

ALA 90 LEU 91 0.0047

LEU 91 LEU 92 0.0206

LEU 92 ARG 93 0.0043

ARG 93 GLY 94 0.0089

GLY 94 ASP 95 0.0103

ASP 95 LEU 96 0.0031

LEU 96 ALA 97 0.0079

ALA 97 GLY 98 0.0080

GLY 98 ALA 99 0.0048

ALA 99 GLU 100 0.0023

GLU 100 ALA 101 0.0017

ALA 101 LEU 102 0.0015

LEU 102 PHE 103 0.0014

PHE 103 ARG 104 0.0748

ARG 104 ARG 105 0.0002

ARG 105 GLY 106 0.0003

GLY 106 LEU 107 0.0002

LEU 107 ARG 108 0.0693

ARG 108 PHE 109 0.0005

PHE 109 TRP 110 0.0009

TRP 110 GLY 111 0.0006

GLY 111 PRO 112 0.1098

PRO 112 GLU 113 0.0005

GLU 113 GLY 114 0.0002

GLY 114 VAL 115 0.0006

VAL 115 LEU 116 0.1288

LEU 116 GLU 117 0.0001

GLU 117 HIS 118 0.0010

HIS 118 LEU 119 0.0008

LEU 119 LEU 120 0.1379

LEU 120 LEU 121 0.0073

LEU 121 PRO 122 0.0074

PRO 122 VAL 123 0.0031

VAL 123 LEU 124 0.0882

LEU 124 ARG 125 0.0133

ARG 125 GLU 126 0.0019

GLU 126 VAL 127 0.0129

VAL 127 GLY 128 0.0333

GLY 128 GLU 129 0.0096

GLU 129 ALA 130 0.0014

ALA 130 TRP 131 0.0109

TRP 131 HIS 132 0.0291

HIS 132 ARG 133 0.0047

ARG 133 GLY 134 0.0063

GLY 134 GLU 135 0.0082

GLU 135 ILE 136 0.0097

ILE 136 GLY 137 0.0108

GLY 137 VAL 138 0.0033

VAL 138 ALA 139 0.0096

ALA 139 GLU 140 0.0587

GLU 140 GLU 141 0.0007

GLU 141 HIS 142 0.0149

HIS 142 LEU 143 0.0109

LEU 143 ALA 144 0.0568

ALA 144 SER 145 0.0023

SER 145 THR 146 0.0134

THR 146 PHE 147 0.0122

PHE 147 LEU 148 0.0239

LEU 148 ARG 149 0.0060

ARG 149 ALA 150 0.0087

ALA 150 ARG 151 0.0089

ARG 151 LEU 152 -0.0102

LEU 152 GLN 153 0.0050

GLN 153 GLU 154 0.0046

GLU 154 LEU 155 0.0030

LEU 155 LEU 156 0.0002

LEU 156 ASP 157 0.0028

ASP 157 LEU 158 0.0035

LEU 158 ALA 159 0.0003

ALA 159 GLY 160 -0.0006

GLY 160 PHE 161 0.0022

PHE 161 PRO 162 0.0002

PRO 162 PRO 163 0.0018

PRO 163 GLY 164 0.0037

GLY 164 PRO 165 0.0086

PRO 165 PRO 166 0.0024

PRO 166 VAL 167 0.0081

VAL 167 LEU 168 0.0140

LEU 168 VAL 169 0.0052

VAL 169 THR 170 0.0105

THR 170 THR 171 0.0132

THR 171 PRO 172 0.0217

PRO 172 PRO 173 0.0150

PRO 173 GLY 174 0.0022

GLY 174 GLU 175 0.0151

GLU 175 ARG 176 0.0011

ARG 176 HIS 177 0.0146

HIS 177 GLU 178 0.0126

GLU 178 ILE 179 0.0138

ILE 179 GLY 180 0.0139

GLY 180 ALA 181 0.0066

ALA 181 MET 182 0.0076

MET 182 LEU 183 0.0103

LEU 183 ALA 184 -0.0307

ALA 184 ALA 185 0.0073

ALA 185 TYR 186 0.0049

TYR 186 HIS 187 0.0052

HIS 187 LEU 188 -0.0190

LEU 188 ARG 189 0.0012

ARG 189 ARG 190 0.0012

ARG 190 LYS 191 0.0003

LYS 191 GLY 192 -0.0418

GLY 192 VAL 193 0.0024

VAL 193 PRO 194 0.0026

PRO 194 ALA 195 0.0025

ALA 195 LEU 196 0.0720

LEU 196 TYR 197 0.0041

TYR 197 LEU 198 0.0131

LEU 198 GLY 199 0.0029

GLY 199 PRO 200 -0.0086

PRO 200 ASP 201 0.0128

ASP 201 THR 202 0.0035

THR 202 PRO 203 0.0096

PRO 203 LEU 204 -0.0002

LEU 204 PRO 205 0.0094

PRO 205 ASP 206 0.0090

ASP 206 LEU 207 0.0143

LEU 207 ARG 208 0.0065

ARG 208 ALA 209 0.0158

ALA 209 LEU 210 0.0108

LEU 210 ALA 211 0.0118

ALA 211 ARG 212 0.0144

ARG 212 ARG 213 0.0135

ARG 213 LEU 214 0.0129

LEU 214 GLY 215 0.0061

GLY 215 ALA 216 -0.0004

ALA 216 GLY 217 0.0127

GLY 217 ALA 218 0.0085

ALA 218 VAL 219 0.0062

VAL 219 VAL 220 0.0046

VAL 220 LEU 221 0.0094

LEU 221 SER 222 0.0035

SER 222 ALA 223 0.0148

ALA 223 VAL 224 -0.0236

VAL 224 LEU 225 0.0177

LEU 225 SER 226 0.0106

SER 226 GLU 227 0.0178

GLU 227 PRO 228 0.0122

PRO 228 LEU 229 0.0078

LEU 229 ARG 230 0.0203

ARG 230 ALA 231 0.0204

ALA 231 LEU 232 0.0063

LEU 232 PRO 233 0.0053

PRO 233 ASP 234 0.0120

ASP 234 GLY 235 0.0163

GLY 235 ALA 236 -0.0020

ALA 236 LEU 237 0.0196

LEU 237 LYS 238 0.0019

LYS 238 ASP 239 0.0172

ASP 239 LEU 240 0.0033

LEU 240 ALA 241 0.0131

ALA 241 PRO 242 0.0085

PRO 242 ARG 243 0.0075

ARG 243 VAL 244 -0.0077

VAL 244 PHE 245 0.0072

PHE 245 LEU 246 0.0066

LEU 246 GLY 247 0.0055

GLY 247 GLY 248 -0.0389

GLY 248 GLN 249 0.0087

GLN 249 GLY 250 0.0153

GLY 250 ALA 251 0.0028

ALA 251 GLY 252 -0.0051

GLY 252 PRO 253 0.0018

PRO 253 GLU 254 0.0170

GLU 254 GLU 255 0.0162

GLU 255 ALA 256 0.0008

ALA 256 ARG 257 0.0057

ARG 257 ARG 258 0.0189

ARG 258 LEU 259 0.0187

LEU 259 GLY 260 0.0214

GLY 260 ALA 261 0.0113

ALA 261 GLU 262 0.0163

GLU 262 TYR 263 0.0039

TYR 263 MET 264 0.0716

MET 264 GLU 265 0.0068

GLU 265 ASP 266 0.0180

ASP 266 LEU 267 0.0187

LEU 267 LYS 268 -0.0079

LYS 268 GLY 269 0.0036

GLY 269 LEU 270 0.0144

LEU 270 ALA 271 0.0139

ALA 271 GLU 272 0.0013

GLU 272 ALA 273 0.0069

ALA 273 LEU 274 0.0091

LEU 274 ASP 82 0.0158

ASP 82 LEU 83 0.0130

LEU 83 GLY 84 0.0118

GLY 84 THR 85 0.0031

THR 85 GLY 86 0.0081

GLY 86 LEU 87 0.0113

LEU 87 LEU 88 0.0096

LEU 88 GLU 89 0.0038

GLU 89 ALA 90 0.0198

ALA 90 LEU 91 0.0118

LEU 91 LEU 92 0.0048

LEU 92 ARG 93 0.0084

ARG 93 GLY 94 0.0100

GLY 94 ASP 95 0.0089

ASP 95 LEU 96 0.0059

LEU 96 ALA 97 0.0105

ALA 97 GLY 98 0.0150

GLY 98 ALA 99 0.0125

ALA 99 GLU 100 0.0108

GLU 100 ALA 101 0.0158

ALA 101 LEU 102 0.0487

LEU 102 PHE 103 0.0073

PHE 103 ARG 104 0.0096

ARG 104 ARG 105 0.0111

ARG 105 GLY 106 0.0980

GLY 106 LEU 107 0.0068

LEU 107 ARG 108 0.0118

ARG 108 PHE 109 0.0122

PHE 109 TRP 110 -0.0560

TRP 110 GLY 111 0.0082

GLY 111 PRO 112 0.0096

PRO 112 GLU 113 0.0093

GLU 113 GLY 114 0.0080

GLY 114 VAL 115 0.0035

VAL 115 LEU 116 0.0077

LEU 116 GLU 117 0.0091

GLU 117 HIS 118 0.0561

HIS 118 LEU 119 0.0035

LEU 119 LEU 120 0.0060

LEU 120 LEU 121 0.0046

LEU 121 PRO 122 0.0518

PRO 122 VAL 123 0.0045

VAL 123 LEU 124 0.0098

LEU 124 ARG 125 0.0102

ARG 125 GLU 126 0.0171

GLU 126 VAL 127 0.0124

VAL 127 GLY 128 0.0124

GLY 128 GLU 129 0.0117

GLU 129 ALA 130 0.0183

ALA 130 TRP 131 0.0142

TRP 131 HIS 132 0.0135

HIS 132 ARG 133 0.0060

ARG 133 GLY 134 0.0096

GLY 134 GLU 135 0.0136

GLU 135 ILE 136 0.0124

ILE 136 GLY 137 0.0139

GLY 137 VAL 138 0.0088

VAL 138 ALA 139 0.0126

ALA 139 GLU 140 0.0134

GLU 140 GLU 141 0.0026

GLU 141 HIS 142 0.0326

HIS 142 LEU 143 0.0113

LEU 143 ALA 144 0.0085

ALA 144 SER 145 0.0048

SER 145 THR 146 0.0420

THR 146 PHE 147 0.0083

PHE 147 LEU 148 0.0034

LEU 148 ARG 149 0.0058

ARG 149 ALA 150 -0.0169

ALA 150 ARG 151 0.0094

ARG 151 LEU 152 0.0020

LEU 152 GLN 153 0.0089

GLN 153 GLU 154 -0.0774

GLU 154 LEU 155 0.0058

LEU 155 LEU 156 0.0038

LEU 156 ASP 157 0.0078

ASP 157 LEU 158 -0.0313

LEU 158 ALA 159 0.0054

ALA 159 GLY 160 0.0055

GLY 160 PHE 161 0.0014

PHE 161 PRO 162 -0.0060

PRO 162 PRO 163 0.0062

PRO 163 GLY 164 0.0078

GLY 164 PRO 165 0.0148

PRO 165 PRO 166 0.0246

PRO 166 VAL 167 0.0138

VAL 167 LEU 168 0.0095

LEU 168 VAL 169 0.0055

VAL 169 THR 170 0.0070

THR 170 THR 171 0.0160

THR 171 PRO 172 0.0185

PRO 172 PRO 173 0.0168

PRO 173 GLY 174 -0.0269

GLY 174 GLU 175 0.0151

GLU 175 ARG 176 0.0090

ARG 176 HIS 177 0.0150

HIS 177 GLU 178 0.0144

GLU 178 ILE 179 0.0124

ILE 179 GLY 180 0.0064

GLY 180 ALA 181 0.0070

ALA 181 MET 182 -0.0455

MET 182 LEU 183 0.0155

LEU 183 ALA 184 0.0021

ALA 184 ALA 185 0.0153

ALA 185 TYR 186 -0.0297

TYR 186 HIS 187 0.0122

HIS 187 LEU 188 0.0026

LEU 188 ARG 189 0.0141

ARG 189 ARG 190 0.0176

ARG 190 LYS 191 0.0065

LYS 191 GLY 192 0.0128

GLY 192 VAL 193 0.0155

VAL 193 PRO 194 0.0233

PRO 194 ALA 195 0.0076

ALA 195 LEU 196 0.0108

LEU 196 TYR 197 0.0035

TYR 197 LEU 198 -0.0113

LEU 198 GLY 199 0.0025

GLY 199 PRO 200 0.0173

PRO 200 ASP 201 0.0175

ASP 201 THR 202 -0.0295

THR 202 PRO 203 0.0157

PRO 203 LEU 204 0.0043

LEU 204 PRO 205 0.0128

PRO 205 ASP 206 0.0431

ASP 206 LEU 207 0.0169

LEU 207 ARG 208 0.0016

ARG 208 ALA 209 0.0174

ALA 209 LEU 210 0.0445

LEU 210 ALA 211 0.0099

ALA 211 ARG 212 0.0054

ARG 212 ARG 213 0.0138

ARG 213 LEU 214 0.0094

LEU 214 GLY 215 0.0050

GLY 215 ALA 216 0.0108

ALA 216 GLY 217 0.0119

GLY 217 ALA 218 0.0175

ALA 218 VAL 219 0.0057

VAL 219 VAL 220 0.0083

VAL 220 LEU 221 0.0090

LEU 221 SER 222 -0.0011

SER 222 ALA 223 0.0160

ALA 223 VAL 224 0.0029

VAL 224 LEU 225 0.0192

LEU 225 SER 226 0.0116

SER 226 GLU 227 0.0215

GLU 227 PRO 228 0.0149

PRO 228 LEU 229 0.0091

LEU 229 ARG 230 0.0250

ARG 230 ALA 231 0.0278

ALA 231 LEU 232 0.0037

LEU 232 PRO 233 0.0101

PRO 233 ASP 234 0.0028

ASP 234 GLY 235 0.0198

GLY 235 ALA 236 0.0184

ALA 236 LEU 237 0.0273

LEU 237 LYS 238 -0.0125

LYS 238 ASP 239 0.0203

ASP 239 LEU 240 0.0103

LEU 240 ALA 241 0.0165

ALA 241 PRO 242 0.0253

PRO 242 ARG 243 0.0115

ARG 243 VAL 244 0.0052

VAL 244 PHE 245 0.0106

PHE 245 LEU 246 0.0229

LEU 246 GLY 247 0.0069

GLY 247 GLY 248 0.0000

GLY 248 GLN 249 0.0091

GLN 249 GLY 250 -0.0216

GLY 250 ALA 251 0.0020

ALA 251 GLY 252 0.0202

GLY 252 PRO 253 0.0027

PRO 253 GLU 254 -0.0015

GLU 254 GLU 255 0.0214

GLU 255 ALA 256 0.0163

ALA 256 ARG 257 0.0105

ARG 257 ARG 258 0.0155

ARG 258 LEU 259 0.0244

LEU 259 GLY 260 0.0076

GLY 260 ALA 261 0.0196

ALA 261 GLU 262 -0.0103

GLU 262 TYR 263 0.0050

TYR 263 MET 264 0.0160

MET 264 GLU 265 0.0059

GLU 265 ASP 266 -0.0959

ASP 266 LEU 267 0.0147

LEU 267 LYS 268 0.0131

LYS 268 GLY 269 0.0046

GLY 269 LEU 270 0.0012

LEU 270 ALA 271 0.0138

ALA 271 GLU 272 0.0136

GLU 272 ALA 273 0.0170

ALA 273 LEU 274 0.0331

LEU 274 TRP 275 0.0172

TRP 275 LEU 276 0.0165

LEU 276 PRO 277 0.0132

PRO 277 ARG 278 0.0442

ARG 278 ARG 79 -0.1509

ARG 79 PRO 80 0.0095

PRO 80 GLU 81 0.0059

GLU 81 ASP 82 0.0044

ASP 82 LEU 83 0.0518

LEU 83 GLY 84 0.0045

GLY 84 THR 85 0.0036

THR 85 GLY 86 0.0030

GLY 86 LEU 87 0.0104

LEU 87 LEU 88 0.0069

LEU 88 GLU 89 0.0024

GLU 89 ALA 90 0.0075

ALA 90 LEU 91 -0.0329

LEU 91 LEU 92 0.0066

LEU 92 ARG 93 0.0045

ARG 93 GLY 94 0.0098

GLY 94 ASP 95 0.0073

ASP 95 LEU 96 0.0043

LEU 96 ALA 97 0.0089

ALA 97 GLY 98 0.0088

GLY 98 ALA 99 0.0242

ALA 99 GLU 100 0.0026

GLU 100 ALA 101 0.0027

ALA 101 LEU 102 0.0018

LEU 102 PHE 103 0.0730

PHE 103 ARG 104 0.0002

ARG 104 ARG 105 0.0002

ARG 105 GLY 106 0.0000

GLY 106 LEU 107 0.0071

LEU 107 ARG 108 0.0014

ARG 108 PHE 109 0.0002

PHE 109 TRP 110 0.0018

TRP 110 GLY 111 0.0351

GLY 111 PRO 112 0.0012

PRO 112 GLU 113 0.0009

GLU 113 GLY 114 0.0009

GLY 114 VAL 115 -0.0465

VAL 115 LEU 116 0.0004

LEU 116 GLU 117 0.0001

GLU 117 HIS 118 0.0004

HIS 118 LEU 119 -0.0104

LEU 119 LEU 120 0.0085

LEU 120 LEU 121 0.0079

LEU 121 PRO 122 0.0049

PRO 122 VAL 123 -0.0581

VAL 123 LEU 124 0.0129

LEU 124 ARG 125 0.0133

ARG 125 GLU 126 0.0033

GLU 126 VAL 127 -0.0608

VAL 127 GLY 128 0.0094

GLY 128 GLU 129 0.0128

GLU 129 ALA 130 0.0013

ALA 130 TRP 131 -0.0178

TRP 131 HIS 132 0.0093

HIS 132 ARG 133 0.0042

ARG 133 GLY 134 0.0063

GLY 134 GLU 135 0.0493

GLU 135 ILE 136 0.0083

ILE 136 GLY 137 0.0088

GLY 137 VAL 138 0.0031

VAL 138 ALA 139 0.0222

ALA 139 GLU 140 0.0122

GLU 140 GLU 141 0.0003

GLU 141 HIS 142 0.0122

HIS 142 LEU 143 0.0142

LEU 143 ALA 144 0.0074

ALA 144 SER 145 0.0028

SER 145 THR 146 0.0105

THR 146 PHE 147 -0.0146

PHE 147 LEU 148 0.0038

LEU 148 ARG 149 0.0063

ARG 149 ALA 150 0.0090

ALA 150 ARG 151 -0.0052

ARG 151 LEU 152 0.0012

LEU 152 GLN 153 0.0044

GLN 153 GLU 154 0.0043

GLU 154 LEU 155 -0.0053

LEU 155 LEU 156 0.0023

LEU 156 ASP 157 0.0025

ASP 157 LEU 158 0.0021

LEU 158 ALA 159 -0.0183

ALA 159 GLY 160 0.0009

GLY 160 PHE 161 0.0036

PHE 161 PRO 162 0.0003

PRO 162 PRO 163 -0.0026

PRO 163 GLY 164 0.0009

GLY 164 PRO 165 0.0047

PRO 165 PRO 166 0.0026

PRO 166 VAL 167 0.0517

VAL 167 LEU 168 0.0097

LEU 168 VAL 169 0.0053

VAL 169 THR 170 0.0101

THR 170 THR 171 0.0428

THR 171 PRO 172 0.0139

PRO 172 PRO 173 0.0145

PRO 173 GLY 174 0.0025

GLY 174 GLU 175 -0.0027

GLU 175 ARG 176 0.0061

ARG 176 HIS 177 0.0148

HIS 177 GLU 178 0.0117

GLU 178 ILE 179 -0.0286

ILE 179 GLY 180 0.0049

GLY 180 ALA 181 0.0067

ALA 181 MET 182 0.0095

MET 182 LEU 183 -0.0605

LEU 183 ALA 184 0.0008

ALA 184 ALA 185 0.0080

ALA 185 TYR 186 0.0064

TYR 186 HIS 187 -0.0119

HIS 187 LEU 188 0.0010

LEU 188 ARG 189 0.0027

ARG 189 ARG 190 0.0028

ARG 190 LYS 191 -0.0101

LYS 191 GLY 192 0.0022

GLY 192 VAL 193 0.0018

VAL 193 PRO 194 0.0017

PRO 194 ALA 195 0.0353

ALA 195 LEU 196 0.0121

LEU 196 TYR 197 0.0048

TYR 197 LEU 198 0.0134

LEU 198 GLY 199 0.0288

GLY 199 PRO 200 0.0150

PRO 200 ASP 201 0.0138

ASP 201 THR 202 0.0039

THR 202 PRO 203 -0.0060

PRO 203 LEU 204 0.0026

LEU 204 PRO 205 0.0093

PRO 205 ASP 206 0.0089

ASP 206 LEU 207 0.0006

LEU 207 ARG 208 0.0005

ARG 208 ALA 209 0.0150

ALA 209 LEU 210 0.0113

LEU 210 ALA 211 0.0100

ALA 211 ARG 212 0.0038

ARG 212 ARG 213 0.0127

ARG 213 LEU 214 0.0122

LEU 214 GLY 215 -0.0007

GLY 215 ALA 216 0.0065

ALA 216 GLY 217 0.0107

GLY 217 ALA 218 0.0072

ALA 218 VAL 219 0.0146

VAL 219 VAL 220 0.0056

VAL 220 LEU 221 0.0079

LEU 221 SER 222 0.0029

SER 222 ALA 223 0.0228

ALA 223 VAL 224 0.0021

VAL 224 LEU 225 0.0170

LEU 225 SER 226 0.0099

SER 226 GLU 227 -0.0098

GLU 227 PRO 228 0.0143

PRO 228 LEU 229 0.0067

LEU 229 ARG 230 0.0188

ARG 230 ALA 231 0.0089

ALA 231 LEU 232 0.0027

LEU 232 PRO 233 0.0059

PRO 233 ASP 234 0.0094

ASP 234 GLY 235 0.0261

GLY 235 ALA 236 0.0112

ALA 236 LEU 237 0.0192

LEU 237 LYS 238 0.0011

LYS 238 ASP 239 0.0268

ASP 239 LEU 240 0.0066

LEU 240 ALA 241 0.0137

ALA 241 PRO 242 0.0084

PRO 242 ARG 243 0.0042

ARG 243 VAL 244 0.0058

VAL 244 PHE 245 0.0077

PHE 245 LEU 246 0.0072

LEU 246 GLY 247 0.0122

GLY 247 GLY 248 0.0002

GLY 248 GLN 249 0.0098

GLN 249 GLY 250 0.0136

GLY 250 ALA 251 0.0102

ALA 251 GLY 252 0.0142

GLY 252 PRO 253 0.0013

PRO 253 GLU 254 0.0179

GLU 254 GLU 255 0.0236

GLU 255 ALA 256 0.0132

ALA 256 ARG 257 0.0060

ARG 257 ARG 258 0.0174

ARG 258 LEU 259 0.0306

LEU 259 GLY 260 0.0073

GLY 260 ALA 261 0.0123

ALA 261 GLU 262 0.0173

GLU 262 TYR 263 0.0117

TYR 263 MET 264 0.0125

MET 264 GLU 265 0.0053

GLU 265 ASP 266 0.0149

ASP 266 LEU 267 -0.0223

LEU 267 LYS 268 0.0111

LYS 268 GLY 269 0.0039

GLY 269 LEU 270 0.0126

LEU 270 ALA 271 -0.0456

ALA 271 GLU 272 0.0109

GLU 272 ALA 273 0.0093

ALA 273 LEU 274 0.0099

LEU 274 ASP 82 -0.0007

ASP 82 LEU 83 0.0116

LEU 83 GLY 84 0.0112

GLY 84 THR 85 0.0036

THR 85 GLY 86 0.0141

GLY 86 LEU 87 0.0112

LEU 87 LEU 88 0.0101

LEU 88 GLU 89 0.0035

GLU 89 ALA 90 0.0079

ALA 90 LEU 91 0.0120

LEU 91 LEU 92 0.0051

LEU 92 ARG 93 0.0082

ARG 93 GLY 94 0.0075

GLY 94 ASP 95 0.0089

ASP 95 LEU 96 0.0054

LEU 96 ALA 97 0.0104

ALA 97 GLY 98 0.0132

GLY 98 ALA 99 0.0125

ALA 99 GLU 100 0.0127

GLU 100 ALA 101 0.0167

ALA 101 LEU 102 -0.0292

LEU 102 PHE 103 0.0074

PHE 103 ARG 104 0.0100

ARG 104 ARG 105 0.0111

ARG 105 GLY 106 -0.0817

GLY 106 LEU 107 0.0070

LEU 107 ARG 108 0.0105

ARG 108 PHE 109 0.0098

PHE 109 TRP 110 0.0660

TRP 110 GLY 111 0.0073

GLY 111 PRO 112 0.0078

PRO 112 GLU 113 0.0061

GLU 113 GLY 114 0.0139

GLY 114 VAL 115 0.0024

VAL 115 LEU 116 0.0079

LEU 116 GLU 117 0.0085

GLU 117 HIS 118 -0.0424

HIS 118 LEU 119 0.0027

LEU 119 LEU 120 0.0059

LEU 120 LEU 121 0.0041

LEU 121 PRO 122 -0.0262

PRO 122 VAL 123 0.0034

VAL 123 LEU 124 0.0098

LEU 124 ARG 125 0.0100

ARG 125 GLU 126 -0.0023

GLU 126 VAL 127 0.0127

VAL 127 GLY 128 0.0125

GLY 128 GLU 129 0.0126

GLU 129 ALA 130 -0.0109

ALA 130 TRP 131 0.0145

TRP 131 HIS 132 0.0139

HIS 132 ARG 133 0.0070

ARG 133 GLY 134 0.0065

GLY 134 GLU 135 0.0152

GLU 135 ILE 136 0.0138

ILE 136 GLY 137 0.0154

GLY 137 VAL 138 0.0008

VAL 138 ALA 139 0.0129

ALA 139 GLU 140 0.0136

GLU 140 GLU 141 0.0023

GLU 141 HIS 142 -0.0016

HIS 142 LEU 143 0.0113

LEU 143 ALA 144 0.0087

ALA 144 SER 145 0.0045

SER 145 THR 146 -0.0060

THR 146 PHE 147 0.0085

PHE 147 LEU 148 0.0030

LEU 148 ARG 149 0.0060

ARG 149 ALA 150 0.0406

ALA 150 ARG 151 0.0095

ARG 151 LEU 152 0.0020

LEU 152 GLN 153 0.0094

GLN 153 GLU 154 0.0884

GLU 154 LEU 155 0.0061

LEU 155 LEU 156 0.0034

LEU 156 ASP 157 0.0080

ASP 157 LEU 158 0.0340

LEU 158 ALA 159 0.0052

ALA 159 GLY 160 0.0068

GLY 160 PHE 161 0.0016

PHE 161 PRO 162 0.0197

PRO 162 PRO 163 0.0073

PRO 163 GLY 164 0.0067

GLY 164 PRO 165 0.0162

PRO 165 PRO 166 -0.0132

PRO 166 VAL 167 0.0156

VAL 167 LEU 168 0.0095

LEU 168 VAL 169 0.0066

VAL 169 THR 170 0.0114

THR 170 THR 171 0.0166

THR 171 PRO 172 0.0192

PRO 172 PRO 173 0.0170

PRO 173 GLY 174 0.0319

GLY 174 GLU 175 0.0167

GLU 175 ARG 176 0.0092

ARG 176 HIS 177 0.0169

HIS 177 GLU 178 0.0170

GLU 178 ILE 179 0.0130

ILE 179 GLY 180 0.0057

GLY 180 ALA 181 0.0079

ALA 181 MET 182 0.0667

MET 182 LEU 183 0.0149

LEU 183 ALA 184 0.0017

ALA 184 ALA 185 0.0153

ALA 185 TYR 186 0.0450

TYR 186 HIS 187 0.0108

HIS 187 LEU 188 0.0024

LEU 188 ARG 189 0.0127

ARG 189 ARG 190 0.0017

ARG 190 LYS 191 0.0059

LYS 191 GLY 192 0.0133

GLY 192 VAL 193 0.0150

VAL 193 PRO 194 0.0216

PRO 194 ALA 195 0.0081

ALA 195 LEU 196 0.0109

LEU 196 TYR 197 0.0045

TYR 197 LEU 198 0.0321

LEU 198 GLY 199 0.0027

GLY 199 PRO 200 0.0180

PRO 200 ASP 201 0.0178

ASP 201 THR 202 0.0382

THR 202 PRO 203 0.0163

PRO 203 LEU 204 0.0027

LEU 204 PRO 205 0.0147

PRO 205 ASP 206 -0.0158

ASP 206 LEU 207 0.0164

LEU 207 ARG 208 0.0029

ARG 208 ALA 209 0.0179

ALA 209 LEU 210 0.0078

LEU 210 ALA 211 0.0092

ALA 211 ARG 212 0.0090

ARG 212 ARG 213 0.0150

ARG 213 LEU 214 0.0259

LEU 214 GLY 215 0.0033

GLY 215 ALA 216 0.0135

ALA 216 GLY 217 0.0109

GLY 217 ALA 218 0.0082

ALA 218 VAL 219 0.0057

VAL 219 VAL 220 0.0092

VAL 220 LEU 221 0.0096

LEU 221 SER 222 0.0119

SER 222 ALA 223 0.0171

ALA 223 VAL 224 0.0040

VAL 224 LEU 225 0.0200

LEU 225 SER 226 0.0377

SER 226 GLU 227 0.0212

GLU 227 PRO 228 0.0170

PRO 228 LEU 229 0.0068

LEU 229 ARG 230 0.0369

ARG 230 ALA 231 0.0277

ALA 231 LEU 232 0.0043

LEU 232 PRO 233 0.0096

PRO 233 ASP 234 0.0239

ASP 234 GLY 235 0.0194

GLY 235 ALA 236 0.0182

ALA 236 LEU 237 0.0285

LEU 237 LYS 238 0.0191

LYS 238 ASP 239 0.0192

ASP 239 LEU 240 0.0081

LEU 240 ALA 241 0.0165

ALA 241 PRO 242 -0.0098

PRO 242 ARG 243 0.0115

ARG 243 VAL 244 0.0063

VAL 244 PHE 245 0.0118

PHE 245 LEU 246 -0.0013

LEU 246 GLY 247 0.0080

GLY 247 GLY 248 -0.0000

GLY 248 GLN 249 0.0106

GLN 249 GLY 250 0.0570

GLY 250 ALA 251 0.0014

ALA 251 GLY 252 0.0191

GLY 252 PRO 253 0.0026

PRO 253 GLU 254 0.0430

GLU 254 GLU 255 0.0219

GLU 255 ALA 256 0.0170

ALA 256 ARG 257 0.0107

ARG 257 ARG 258 0.0190

ARG 258 LEU 259 0.0255

LEU 259 GLY 260 0.0079

GLY 260 ALA 261 0.0212

ALA 261 GLU 262 0.0378

GLU 262 TYR 263 0.0070

TYR 263 MET 264 0.0182

MET 264 GLU 265 0.0124

GLU 265 ASP 266 0.0822

ASP 266 LEU 267 0.0279

LEU 267 LYS 268 0.0201

LYS 268 GLY 269 0.0158

GLY 269 LEU 270 0.0155

LEU 270 ALA 271 0.0205

ALA 271 GLU 272 0.0107

GLU 272 ALA 273 0.0198

ALA 273 LEU 274 -0.0064

LEU 274 ALA 275 0.0177

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 9 ---

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

* DARK TET *