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

* EXSA_dimer1 *

CA strain for 2401041206373816311

--- normal mode 13 ---

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
MET 1 GLN 2 -0.0001

GLN 2 GLY 3 0.0217

GLY 3 ALA 4 0.0002

ALA 4 LYS 5 -0.0001

LYS 5 SER 6 0.0629

SER 6 LEU 7 -0.0001

LEU 7 GLY 8 -0.0002

GLY 8 ARG 9 0.2996

ARG 9 LYS 10 -0.0002

LYS 10 GLN 11 0.0001

GLN 11 ILE 12 0.0444

ILE 12 THR 13 0.0003

THR 13 SER 14 -0.0002

SER 14 CYS 15 -0.0863

CYS 15 HIS 16 0.0003

HIS 16 TRP 17 -0.0002

TRP 17 ASN 18 -0.0279

ASN 18 ILE 19 0.0005

ILE 19 PRO 20 -0.0002

PRO 20 THR 21 -0.0081

THR 21 PHE 22 0.0000

PHE 22 GLU 23 -0.0001

GLU 23 TYR 24 -0.0108

TYR 24 ARG 25 -0.0002

ARG 25 VAL 26 0.0002

VAL 26 ASN 27 -0.0559

ASN 27 LYS 28 0.0003

LYS 28 GLU 29 0.0002

GLU 29 GLU 30 0.0567

GLU 30 GLY 31 0.0001

GLY 31 VAL 32 0.0001

VAL 32 TYR 33 -0.0311

TYR 33 VAL 34 0.0002

VAL 34 LEU 35 -0.0006

LEU 35 LEU 36 -0.0199

LEU 36 GLU 37 -0.0002

GLU 37 GLY 38 0.0003

GLY 38 GLU 39 0.0245

GLU 39 LEU 40 -0.0001

LEU 40 THR 41 0.0003

THR 41 VAL 42 -0.0305

VAL 42 GLN 43 0.0001

GLN 43 ASP 44 0.0000

ASP 44 ILE 45 -0.0081

ILE 45 ASP 46 -0.0003

ASP 46 SER 47 0.0001

SER 47 THR 48 0.0244

THR 48 PHE 49 -0.0001

PHE 49 CYS 50 -0.0003

CYS 50 LEU 51 0.0754

LEU 51 ALA 52 -0.0001

ALA 52 PRO 53 0.0002

PRO 53 GLY 54 0.0375

GLY 54 GLU 55 -0.0002

GLU 55 LEU 56 0.0000

LEU 56 LEU 57 0.0516

LEU 57 PHE 58 -0.0000

PHE 58 VAL 59 0.0002

VAL 59 ARG 60 -0.0126

ARG 60 ARG 61 -0.0003

ARG 61 GLY 62 0.0003

GLY 62 SER 63 -0.1048

SER 63 TYR 64 0.0002

TYR 64 VAL 65 -0.0000

VAL 65 VAL 66 -0.0147

VAL 66 SER 67 0.0001

SER 67 THR 68 -0.0000

THR 68 LYS 69 -0.0060

LYS 69 GLY 70 0.0002

GLY 70 LYS 71 0.0001

LYS 71 ASP 72 -0.0006

ASP 72 SER 73 -0.0002

SER 73 ARG 74 -0.0003

ARG 74 ILE 75 -0.0029

ILE 75 LEU 76 -0.0001

LEU 76 TRP 77 0.0000

TRP 77 ILE 78 -0.0096

ILE 78 PRO 79 0.0002

PRO 79 LEU 80 -0.0003

LEU 80 SER 81 -0.0368

SER 81 ALA 82 -0.0001

ALA 82 GLN 83 -0.0001

GLN 83 PHE 84 -0.0607

PHE 84 LEU 85 -0.0002

LEU 85 GLN 86 -0.0002

GLN 86 GLY 87 0.0112

GLY 87 PHE 88 0.0001

PHE 88 VAL 89 -0.0000

VAL 89 GLN 90 -0.0089

GLN 90 ARG 91 0.0000

ARG 91 PHE 92 0.0000

PHE 92 GLY 93 -0.0107

GLY 93 ALA 94 0.0003

ALA 94 LEU 95 0.0002

LEU 95 LEU 96 0.0179

LEU 96 SER 97 0.0000

SER 97 GLU 98 0.0001

GLU 98 VAL 99 0.0267

VAL 99 GLU 100 0.0003

GLU 100 ARG 101 -0.0000

ARG 101 CYS 102 -0.0470

CYS 102 ASP 103 -0.0002

ASP 103 GLU 104 -0.0000

GLU 104 PRO 105 0.0288

PRO 105 VAL 106 -0.0001

VAL 106 PRO 107 0.0000

PRO 107 GLY 108 0.0239

GLY 108 ILE 109 -0.0002

ILE 109 ILE 110 0.0001

ILE 110 ALA 111 0.0356

ALA 111 PHE 112 -0.0003

PHE 112 ALA 113 0.0001

ALA 113 ALA 114 0.0873

ALA 114 THR 115 -0.0000

THR 115 PRO 116 -0.0001

PRO 116 LEU 117 -0.0230

LEU 117 LEU 118 0.0001

LEU 118 ALA 119 0.0001

ALA 119 GLY 120 0.0129

GLY 120 CYS 121 0.0003

CYS 121 VAL 122 0.0001

VAL 122 LYS 123 -0.0024

LYS 123 GLY 124 0.0002

GLY 124 LEU 125 -0.0003

LEU 125 LYS 126 -0.0126

LYS 126 GLU 127 0.0002

GLU 127 LEU 128 0.0002

LEU 128 LEU 129 -0.0031

LEU 129 VAL 130 0.0003

VAL 130 HIS 131 -0.0001

HIS 131 GLU 132 0.0571

GLU 132 HIS 133 -0.0002

HIS 133 PRO 134 0.0001

PRO 134 PRO 135 -0.0670

PRO 135 MET 136 0.0004

MET 136 LEU 137 -0.0000

LEU 137 ALA 138 -0.0526

ALA 138 CYS 139 -0.0002

CYS 139 LEU 140 -0.0001

LEU 140 LYS 141 0.0097

LYS 141 ILE 142 0.0002

ILE 142 GLU 143 0.0001

GLU 143 GLU 144 0.0039

GLU 144 LEU 145 0.0000

LEU 145 LEU 146 0.0000

LEU 146 MET 147 -0.0088

MET 147 LEU 148 -0.0000

LEU 148 PHE 149 -0.0003

PHE 149 ALA 150 -0.0653

ALA 150 PHE 151 0.0002

PHE 151 SER 152 0.0001

SER 152 PRO 153 0.0497

PRO 153 GLN 154 0.0000

GLN 154 GLY 155 0.0001

GLY 155 PRO 156 -0.0176

PRO 156 LEU 157 -0.0002

LEU 157 LEU 158 -0.0002

LEU 158 MET 159 -0.0264

MET 159 SER 160 0.0001

SER 160 VAL 161 -0.0003

VAL 161 LEU 162 -0.0361

LEU 162 ARG 163 0.0004

ARG 163 GLN 164 0.0002

GLN 164 LEU 165 -0.0105

LEU 165 SER 166 -0.0002

SER 166 ASN 167 -0.0003

ASN 167 ARG 168 -0.0709

ARG 168 HIS 169 -0.0003

HIS 169 VAL 170 -0.0002

VAL 170 GLU 171 0.0152

GLU 171 ARG 172 -0.0005

ARG 172 LEU 173 0.0002

LEU 173 GLN 174 0.0156

GLN 174 LEU 175 -0.0002

LEU 175 PHE 176 0.0002

PHE 176 MET 177 0.0138

MET 177 GLU 178 0.0001

GLU 178 LYS 179 0.0001

LYS 179 HIS 180 0.0076

HIS 180 TYR 181 -0.0001

TYR 181 LEU 182 0.0003

LEU 182 ASN 183 0.0399

ASN 183 GLU 184 0.0002

GLU 184 TRP 185 -0.0003

TRP 185 LYS 186 0.0852

LYS 186 LEU 187 0.0001

LEU 187 SER 188 -0.0002

SER 188 ASP 189 0.0109

ASP 189 PHE 190 -0.0003

PHE 190 SER 191 0.0001

SER 191 ARG 192 0.0013

ARG 192 GLU 193 -0.0001

GLU 193 PHE 194 -0.0001

PHE 194 GLY 195 0.0011

GLY 195 MET 196 0.0003

MET 196 GLY 197 -0.0002

GLY 197 LEU 198 -0.0010

LEU 198 THR 199 -0.0002

THR 199 THR 200 0.0000

THR 200 PHE 201 -0.0034

PHE 201 LYS 202 0.0001

LYS 202 GLU 203 -0.0002

GLU 203 LEU 204 -0.0086

LEU 204 PHE 205 -0.0002

PHE 205 GLY 206 0.0000

GLY 206 SER 207 -0.0200

SER 207 VAL 208 0.0000

VAL 208 TYR 209 0.0002

TYR 209 GLY 210 -0.0121

GLY 210 VAL 211 -0.0000

VAL 211 SER 212 -0.0001

SER 212 PRO 213 0.0122

PRO 213 ARG 214 0.0002

ARG 214 ALA 215 0.0001

ALA 215 TRP 216 -0.0251

TRP 216 ILE 217 -0.0001

ILE 217 SER 218 -0.0004

SER 218 GLU 219 -0.0079

GLU 219 ARG 220 0.0001

ARG 220 ARG 221 0.0003

ARG 221 ILE 222 0.0058

ILE 222 LEU 223 -0.0002

LEU 223 TYR 224 0.0004

TYR 224 ALA 225 -0.0112

ALA 225 HIS 226 0.0001

HIS 226 GLN 227 0.0005

GLN 227 LEU 228 -0.0198

LEU 228 LEU 229 0.0000

LEU 229 LEU 230 -0.0001

LEU 230 ASN 231 -0.0151

ASN 231 SER 232 0.0001

SER 232 ASP 233 0.0003

ASP 233 MET 234 0.0422

MET 234 SER 235 -0.0001

SER 235 ILE 236 -0.0003

ILE 236 VAL 237 0.0014

VAL 237 ASP 238 0.0001

ASP 238 ILE 239 -0.0002

ILE 239 ALA 240 0.0232

ALA 240 MET 241 -0.0000

MET 241 GLU 242 0.0002

GLU 242 ALA 243 -0.0139

ALA 243 GLY 244 -0.0001

GLY 244 PHE 245 0.0001

PHE 245 SER 246 0.0155

SER 246 SER 247 -0.0001

SER 247 GLN 248 -0.0002

GLN 248 SER 249 -0.0229

SER 249 TYR 250 0.0001

TYR 250 PHE 251 -0.0003

PHE 251 THR 252 -0.0226

THR 252 GLN 253 0.0000

GLN 253 SER 254 -0.0003

SER 254 TYR 255 0.0024

TYR 255 ARG 256 0.0002

ARG 256 ARG 257 0.0000

ARG 257 ARG 258 0.0433

ARG 258 PHE 259 0.0001

PHE 259 GLY 260 0.0004

GLY 260 CYS 261 -0.0454

CYS 261 THR 262 -0.0002

THR 262 PRO 263 0.0001

PRO 263 SER 264 0.0151

SER 264 ARG 265 0.0001

ARG 265 SER 266 0.0000

SER 266 ARG 267 -0.0242

ARG 267 GLN 268 -0.0000

GLN 268 GLY 269 0.0001

GLY 269 LYS 270 0.0283

LYS 270 ASP 271 0.0003

ASP 271 GLU 272 0.0000

GLU 272 CYS 273 -0.0262

CYS 273 ARG 274 -0.0001

ARG 274 ALA 275 0.0001

ALA 275 LYS 276 0.0764

LYS 276 ASN 277 -0.0000

ASN 277 ASN 278 -0.0002

ASN 278 NMA 278 0.0001

NMA 278 MET 1 -0.0430

MET 1 GLN 2 -0.0002

GLN 2 GLY 3 -0.0465

GLY 3 ALA 4 0.0003

ALA 4 LYS 5 -0.0000

LYS 5 SER 6 -0.1011

SER 6 LEU 7 -0.0002

LEU 7 GLY 8 -0.0000

GLY 8 ARG 9 -0.3606

ARG 9 LYS 10 -0.0003

LYS 10 GLN 11 0.0002

GLN 11 ILE 12 -0.0436

ILE 12 THR 13 0.0002

THR 13 SER 14 -0.0003

SER 14 CYS 15 0.1260

CYS 15 HIS 16 0.0002

HIS 16 TRP 17 -0.0002

TRP 17 ASN 18 0.0409

ASN 18 ILE 19 0.0001

ILE 19 PRO 20 -0.0001

PRO 20 THR 21 0.0084

THR 21 PHE 22 0.0003

PHE 22 GLU 23 0.0000

GLU 23 TYR 24 0.0053

TYR 24 ARG 25 -0.0001

ARG 25 VAL 26 -0.0003

VAL 26 ASN 27 0.0579

ASN 27 LYS 28 0.0000

LYS 28 GLU 29 -0.0002

GLU 29 GLU 30 -0.0590

GLU 30 GLY 31 0.0003

GLY 31 VAL 32 -0.0001

VAL 32 TYR 33 0.0192

TYR 33 VAL 34 -0.0003

VAL 34 LEU 35 0.0003

LEU 35 LEU 36 0.0264

LEU 36 GLU 37 -0.0001

GLU 37 GLY 38 0.0001

GLY 38 GLU 39 -0.0075

GLU 39 LEU 40 0.0002

LEU 40 THR 41 0.0003

THR 41 VAL 42 0.0217

VAL 42 GLN 43 0.0002

GLN 43 ASP 44 -0.0001

ASP 44 ILE 45 0.0113

ILE 45 ASP 46 -0.0001

ASP 46 SER 47 -0.0001

SER 47 THR 48 -0.0180

THR 48 PHE 49 0.0003

PHE 49 CYS 50 -0.0000

CYS 50 LEU 51 -0.0523

LEU 51 ALA 52 0.0002

ALA 52 PRO 53 -0.0001

PRO 53 GLY 54 -0.0346

GLY 54 GLU 55 0.0003

GLU 55 LEU 56 0.0000

LEU 56 LEU 57 -0.0251

LEU 57 PHE 58 -0.0001

PHE 58 VAL 59 -0.0004

VAL 59 ARG 60 0.0196

ARG 60 ARG 61 -0.0004

ARG 61 GLY 62 0.0003

GLY 62 SER 63 0.0726

SER 63 TYR 64 -0.0004

TYR 64 VAL 65 0.0000

VAL 65 VAL 66 0.0183

VAL 66 SER 67 -0.0002

SER 67 THR 68 0.0002

THR 68 LYS 69 0.0073

LYS 69 GLY 70 0.0000

GLY 70 LYS 71 0.0001

LYS 71 ASP 72 0.0202

ASP 72 SER 73 -0.0002

SER 73 ARG 74 0.0002

ARG 74 ILE 75 -0.0123

ILE 75 LEU 76 -0.0001

LEU 76 TRP 77 -0.0000

TRP 77 ILE 78 0.0108

ILE 78 PRO 79 -0.0000

PRO 79 LEU 80 -0.0002

LEU 80 SER 81 0.0370

SER 81 ALA 82 -0.0000

ALA 82 GLN 83 0.0003

GLN 83 PHE 84 0.0307

PHE 84 LEU 85 -0.0002

LEU 85 GLN 86 -0.0002

GLN 86 GLY 87 -0.0093

GLY 87 PHE 88 -0.0000

PHE 88 VAL 89 0.0003

VAL 89 GLN 90 0.0095

GLN 90 ARG 91 0.0003

ARG 91 PHE 92 -0.0001

PHE 92 GLY 93 -0.0065

GLY 93 ALA 94 -0.0002

ALA 94 LEU 95 0.0002

LEU 95 LEU 96 -0.0210

LEU 96 SER 97 0.0001

SER 97 GLU 98 -0.0006

GLU 98 VAL 99 -0.0442

VAL 99 GLU 100 -0.0000

GLU 100 ARG 101 -0.0004

ARG 101 CYS 102 0.0030

CYS 102 ASP 103 0.0001

ASP 103 GLU 104 0.0001

GLU 104 PRO 105 -0.0422

PRO 105 VAL 106 -0.0003

VAL 106 PRO 107 0.0003

PRO 107 GLY 108 -0.0628

GLY 108 ILE 109 0.0001

ILE 109 ILE 110 0.0002

ILE 110 ALA 111 -0.0082

ALA 111 PHE 112 -0.0002

PHE 112 ALA 113 0.0001

ALA 113 ALA 114 -0.0521

ALA 114 THR 115 0.0001

THR 115 PRO 116 0.0001

PRO 116 LEU 117 0.0108

LEU 117 LEU 118 -0.0004

LEU 118 ALA 119 0.0001

ALA 119 GLY 120 0.0029

GLY 120 CYS 121 -0.0001

CYS 121 VAL 122 0.0006

VAL 122 LYS 123 0.0188

LYS 123 GLY 124 -0.0002

GLY 124 LEU 125 0.0000

LEU 125 LYS 126 -0.0014

LYS 126 GLU 127 -0.0003

GLU 127 LEU 128 -0.0003

LEU 128 LEU 129 0.0131

LEU 129 VAL 130 0.0001

VAL 130 HIS 131 0.0001

HIS 131 GLU 132 -0.0471

GLU 132 HIS 133 -0.0002

HIS 133 PRO 134 0.0004

PRO 134 PRO 135 0.0555

PRO 135 MET 136 0.0003

MET 136 LEU 137 -0.0003

LEU 137 ALA 138 0.0658

ALA 138 CYS 139 0.0001

CYS 139 LEU 140 0.0003

LEU 140 LYS 141 -0.0071

LYS 141 ILE 142 -0.0003

ILE 142 GLU 143 0.0003

GLU 143 GLU 144 -0.0083

GLU 144 LEU 145 0.0001

LEU 145 LEU 146 -0.0004

LEU 146 MET 147 0.0071

MET 147 LEU 148 0.0004

LEU 148 PHE 149 0.0001

PHE 149 ALA 150 0.0469

ALA 150 PHE 151 -0.0000

PHE 151 SER 152 0.0001

SER 152 PRO 153 -0.0409

PRO 153 GLN 154 0.0001

GLN 154 GLY 155 0.0000

GLY 155 PRO 156 0.0167

PRO 156 LEU 157 0.0000

LEU 157 LEU 158 0.0002

LEU 158 MET 159 0.0131

MET 159 SER 160 -0.0002

SER 160 VAL 161 0.0001

VAL 161 LEU 162 0.0285

LEU 162 ARG 163 0.0001

ARG 163 GLN 164 -0.0001

GLN 164 LEU 165 0.0144

LEU 165 SER 166 -0.0001

SER 166 ASN 167 0.0001

ASN 167 ARG 168 0.0498

ARG 168 HIS 169 -0.0001

HIS 169 VAL 170 -0.0000

VAL 170 GLU 171 -0.0128

GLU 171 ARG 172 0.0001

ARG 172 LEU 173 -0.0001

LEU 173 GLN 174 -0.0172

GLN 174 LEU 175 0.0003

LEU 175 PHE 176 0.0003

PHE 176 MET 177 -0.0244

MET 177 GLU 178 0.0001

GLU 178 LYS 179 -0.0002

LYS 179 HIS 180 0.0136

HIS 180 TYR 181 0.0003

TYR 181 LEU 182 0.0004

LEU 182 ASN 183 -0.0560

ASN 183 GLU 184 -0.0001

GLU 184 TRP 185 0.0003

TRP 185 LYS 186 -0.0792

LYS 186 LEU 187 -0.0001

LEU 187 SER 188 0.0002

SER 188 ASP 189 -0.0099

ASP 189 PHE 190 0.0002

PHE 190 SER 191 0.0002

SER 191 ARG 192 -0.0099

ARG 192 GLU 193 -0.0001

GLU 193 PHE 194 0.0001

PHE 194 GLY 195 -0.0062

GLY 195 MET 196 -0.0001

MET 196 GLY 197 -0.0004

GLY 197 LEU 198 0.0044

LEU 198 THR 199 -0.0002

THR 199 THR 200 -0.0001

THR 200 PHE 201 -0.0030

PHE 201 LYS 202 0.0003

LYS 202 GLU 203 -0.0000

GLU 203 LEU 204 0.0136

LEU 204 PHE 205 0.0000

PHE 205 GLY 206 -0.0002

GLY 206 SER 207 0.0160

SER 207 VAL 208 -0.0000

VAL 208 TYR 209 -0.0000

TYR 209 GLY 210 0.0073

GLY 210 VAL 211 -0.0003

VAL 211 SER 212 -0.0001

SER 212 PRO 213 -0.0002

PRO 213 ARG 214 0.0001

ARG 214 ALA 215 -0.0001

ALA 215 TRP 216 0.0264

TRP 216 ILE 217 0.0005

ILE 217 SER 218 0.0001

SER 218 GLU 219 0.0008

GLU 219 ARG 220 -0.0000

ARG 220 ARG 221 0.0000

ARG 221 ILE 222 -0.0134

ILE 222 LEU 223 0.0001

LEU 223 TYR 224 0.0000

TYR 224 ALA 225 0.0150

ALA 225 HIS 226 -0.0003

HIS 226 GLN 227 0.0004

GLN 227 LEU 228 0.0326

LEU 228 LEU 229 -0.0003

LEU 229 LEU 230 0.0002

LEU 230 ASN 231 0.0094

ASN 231 SER 232 0.0000

SER 232 ASP 233 0.0000

ASP 233 MET 234 -0.0661

MET 234 SER 235 -0.0002

SER 235 ILE 236 0.0001

ILE 236 VAL 237 0.0019

VAL 237 ASP 238 -0.0001

ASP 238 ILE 239 -0.0001

ILE 239 ALA 240 -0.0423

ALA 240 MET 241 -0.0003

MET 241 GLU 242 0.0002

GLU 242 ALA 243 0.0155

ALA 243 GLY 244 -0.0000

GLY 244 PHE 245 -0.0000

PHE 245 SER 246 -0.0289

SER 246 SER 247 -0.0000

SER 247 GLN 248 -0.0000

GLN 248 SER 249 0.0308

SER 249 TYR 250 -0.0001

TYR 250 PHE 251 -0.0005

PHE 251 THR 252 0.0291

THR 252 GLN 253 0.0003

GLN 253 SER 254 0.0002

SER 254 TYR 255 -0.0150

TYR 255 ARG 256 0.0000

ARG 256 ARG 257 0.0002

ARG 257 ARG 258 -0.0492

ARG 258 PHE 259 -0.0000

PHE 259 GLY 260 0.0001

GLY 260 CYS 261 0.0688

CYS 261 THR 262 -0.0002

THR 262 PRO 263 0.0001

PRO 263 SER 264 -0.0228

SER 264 ARG 265 0.0001

ARG 265 SER 266 -0.0003

SER 266 ARG 267 0.0297

ARG 267 GLN 268 -0.0002

GLN 268 GLY 269 -0.0002

GLY 269 LYS 270 -0.0451

LYS 270 ASP 271 -0.0003

ASP 271 GLU 272 0.0002

GLU 272 CYS 273 0.0122

CYS 273 ARG 274 0.0001

ARG 274 ALA 275 -0.0002

ALA 275 LYS 276 -0.0888

LYS 276 ASN 277 -0.0002

ASN 277 ASN 278 -0.0003

ASN 278 NMA 278 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: April 25th, 2023.

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

*** EXSA_dimer1 ***

CA strain for 2401041206373816311

--- normal mode 13 ---

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

* EXSA_dimer1 *